data_8S8S
# 
_entry.id   8S8S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8S8S         pdb_00008s8s 10.2210/pdb8s8s/pdb 
WWPDB D_1292137066 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8S8S 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-07 
_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                 2 
_pdbx_contact_author.email              Reinhard.Sterner@biologie.uni-regensburg.de 
_pdbx_contact_author.name_first         Reinhard 
_pdbx_contact_author.name_last          Sterner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8177-8460 
# 
_audit_author.name               'Rajendran, C.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            4 
_citation.language                  ? 
_citation.page_first                3258 
_citation.page_last                 3276 
_citation.title                     
;Conformational Modulation of a Mobile Loop Controls Catalysis in the ( beta alpha ) 8 -Barrel Enzyme of Histidine Biosynthesis HisF.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.4c00558 
_citation.pdbx_database_id_PubMed   39211614 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hupfeld, E.'       1  ?                   
primary 'Schlee, S.'        2  ?                   
primary 'Wurm, J.P.'        3  ?                   
primary 'Rajendran, C.'     4  ?                   
primary 'Yehorova, D.'      5  ?                   
primary 'Vos, E.'           6  ?                   
primary 'Ravindra Raju, D.' 7  0000-0003-0657-1560 
primary 'Kamerlin, S.C.L.'  8  0000-0002-3190-1173 
primary 'Sprangers, R.'     9  ?                   
primary 'Sterner, R.'       10 0000-0001-8177-8460 
# 
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 'Imidazole glycerol phosphate synthase subunit HisF' 27605.686 1   4.3.2.10 ? ? ? 
2 water   nat water                                                18.015    258 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IGP synthase cyclase subunit,IGP synthase subunit HisF,ImGP synthase subunit HisF,IGPS subunit HisF' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;LAKRIIACLDVKDGRVVKPTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGG
GIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVE
KRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYL
KKHGVNVRLEL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LAKRIIACLDVKDGRVVKPTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGG
GIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVE
KRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYL
KKHGVNVRLEL
;
_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   LEU n 
1 2   ALA n 
1 3   LYS n 
1 4   ARG n 
1 5   ILE n 
1 6   ILE n 
1 7   ALA n 
1 8   CYS n 
1 9   LEU n 
1 10  ASP n 
1 11  VAL n 
1 12  LYS n 
1 13  ASP n 
1 14  GLY n 
1 15  ARG n 
1 16  VAL n 
1 17  VAL n 
1 18  LYS n 
1 19  PRO n 
1 20  THR n 
1 21  ASN n 
1 22  PHE n 
1 23  GLU n 
1 24  ASN n 
1 25  LEU n 
1 26  ARG n 
1 27  ASP n 
1 28  SER n 
1 29  GLY n 
1 30  ASP n 
1 31  PRO n 
1 32  VAL n 
1 33  GLU n 
1 34  LEU n 
1 35  GLY n 
1 36  LYS n 
1 37  PHE n 
1 38  TYR n 
1 39  SER n 
1 40  GLU n 
1 41  ILE n 
1 42  GLY n 
1 43  ILE n 
1 44  ASP n 
1 45  GLU n 
1 46  LEU n 
1 47  VAL n 
1 48  PHE n 
1 49  LEU n 
1 50  ASP n 
1 51  ILE n 
1 52  THR n 
1 53  ALA n 
1 54  SER n 
1 55  VAL n 
1 56  GLU n 
1 57  LYS n 
1 58  ARG n 
1 59  LYS n 
1 60  THR n 
1 61  MET n 
1 62  LEU n 
1 63  GLU n 
1 64  LEU n 
1 65  VAL n 
1 66  GLU n 
1 67  LYS n 
1 68  VAL n 
1 69  ALA n 
1 70  GLU n 
1 71  GLN n 
1 72  ILE n 
1 73  ASP n 
1 74  ILE n 
1 75  PRO n 
1 76  PHE n 
1 77  THR n 
1 78  VAL n 
1 79  GLY n 
1 80  GLY n 
1 81  GLY n 
1 82  ILE n 
1 83  HIS n 
1 84  ASP n 
1 85  PHE n 
1 86  GLU n 
1 87  THR n 
1 88  ALA n 
1 89  SER n 
1 90  GLU n 
1 91  LEU n 
1 92  ILE n 
1 93  LEU n 
1 94  ARG n 
1 95  GLY n 
1 96  ALA n 
1 97  ASP n 
1 98  LYS n 
1 99  VAL n 
1 100 SER n 
1 101 ILE n 
1 102 ASN n 
1 103 THR n 
1 104 ALA n 
1 105 ALA n 
1 106 VAL n 
1 107 GLU n 
1 108 ASN n 
1 109 PRO n 
1 110 SER n 
1 111 LEU n 
1 112 ILE n 
1 113 THR n 
1 114 GLN n 
1 115 ILE n 
1 116 ALA n 
1 117 GLN n 
1 118 THR n 
1 119 PHE n 
1 120 GLY n 
1 121 SER n 
1 122 GLN n 
1 123 ALA n 
1 124 VAL n 
1 125 VAL n 
1 126 VAL n 
1 127 ALA n 
1 128 ILE n 
1 129 ASP n 
1 130 ALA n 
1 131 LYS n 
1 132 ARG n 
1 133 VAL n 
1 134 ASP n 
1 135 GLY n 
1 136 GLU n 
1 137 PHE n 
1 138 MET n 
1 139 VAL n 
1 140 PHE n 
1 141 THR n 
1 142 TYR n 
1 143 SER n 
1 144 GLY n 
1 145 LYS n 
1 146 LYS n 
1 147 ASN n 
1 148 THR n 
1 149 GLY n 
1 150 ILE n 
1 151 LEU n 
1 152 LEU n 
1 153 ARG n 
1 154 ASP n 
1 155 TRP n 
1 156 VAL n 
1 157 VAL n 
1 158 GLU n 
1 159 VAL n 
1 160 GLU n 
1 161 LYS n 
1 162 ARG n 
1 163 GLY n 
1 164 ALA n 
1 165 GLY n 
1 166 GLU n 
1 167 ILE n 
1 168 LEU n 
1 169 LEU n 
1 170 THR n 
1 171 SER n 
1 172 ILE n 
1 173 ASP n 
1 174 ARG n 
1 175 ASP n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 SER n 
1 180 GLY n 
1 181 TYR n 
1 182 ASP n 
1 183 THR n 
1 184 GLU n 
1 185 MET n 
1 186 ILE n 
1 187 ARG n 
1 188 PHE n 
1 189 VAL n 
1 190 ARG n 
1 191 PRO n 
1 192 LEU n 
1 193 THR n 
1 194 THR n 
1 195 LEU n 
1 196 PRO n 
1 197 ILE n 
1 198 ILE n 
1 199 ALA n 
1 200 SER n 
1 201 GLY n 
1 202 GLY n 
1 203 ALA n 
1 204 GLY n 
1 205 LYS n 
1 206 MET n 
1 207 GLU n 
1 208 HIS n 
1 209 PHE n 
1 210 LEU n 
1 211 GLU n 
1 212 ALA n 
1 213 PHE n 
1 214 LEU n 
1 215 ALA n 
1 216 GLY n 
1 217 ALA n 
1 218 ASP n 
1 219 ALA n 
1 220 ALA n 
1 221 LEU n 
1 222 ALA n 
1 223 ALA n 
1 224 SER n 
1 225 VAL n 
1 226 PHE n 
1 227 HIS n 
1 228 PHE n 
1 229 ARG n 
1 230 GLU n 
1 231 ILE n 
1 232 ASP n 
1 233 VAL n 
1 234 ARG n 
1 235 GLU n 
1 236 LEU n 
1 237 LYS n 
1 238 GLU n 
1 239 TYR n 
1 240 LEU n 
1 241 LYS n 
1 242 LYS n 
1 243 HIS n 
1 244 GLY n 
1 245 VAL n 
1 246 ASN n 
1 247 VAL n 
1 248 ARG n 
1 249 LEU n 
1 250 GLU n 
1 251 LEU 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                   251 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'hisF, TM_1036' 
_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      'Thermotoga maritima' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2336 
_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 
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   LEU 1   2   2   LEU LEU A . n 
A 1 2   ALA 2   3   3   ALA ALA A . n 
A 1 3   LYS 3   4   4   LYS LYS A . n 
A 1 4   ARG 4   5   5   ARG ARG A . n 
A 1 5   ILE 5   6   6   ILE ILE A . n 
A 1 6   ILE 6   7   7   ILE ILE A . n 
A 1 7   ALA 7   8   8   ALA ALA A . n 
A 1 8   CYS 8   9   9   CYS CYS A . n 
A 1 9   LEU 9   10  10  LEU LEU A . n 
A 1 10  ASP 10  11  11  ASP ASP A . n 
A 1 11  VAL 11  12  12  VAL VAL A . n 
A 1 12  LYS 12  13  13  LYS LYS A . n 
A 1 13  ASP 13  14  14  ASP ASP A . n 
A 1 14  GLY 14  15  15  GLY GLY A . n 
A 1 15  ARG 15  16  16  ARG ARG A . n 
A 1 16  VAL 16  17  17  VAL VAL A . n 
A 1 17  VAL 17  18  18  VAL VAL A . n 
A 1 18  LYS 18  19  19  LYS LYS A . n 
A 1 19  PRO 19  20  20  PRO PRO A . n 
A 1 20  THR 20  21  21  THR THR A . n 
A 1 21  ASN 21  22  22  ASN ASN A . n 
A 1 22  PHE 22  23  23  PHE PHE A . n 
A 1 23  GLU 23  24  24  GLU GLU A . n 
A 1 24  ASN 24  25  25  ASN ASN A . n 
A 1 25  LEU 25  26  26  LEU LEU A . n 
A 1 26  ARG 26  27  27  ARG ARG A . n 
A 1 27  ASP 27  28  28  ASP ASP A . n 
A 1 28  SER 28  29  29  SER SER A . n 
A 1 29  GLY 29  30  30  GLY GLY A . n 
A 1 30  ASP 30  31  31  ASP ASP A . n 
A 1 31  PRO 31  32  32  PRO PRO A . n 
A 1 32  VAL 32  33  33  VAL VAL A . n 
A 1 33  GLU 33  34  34  GLU GLU A . n 
A 1 34  LEU 34  35  35  LEU LEU A . n 
A 1 35  GLY 35  36  36  GLY GLY A . n 
A 1 36  LYS 36  37  37  LYS LYS A . n 
A 1 37  PHE 37  38  38  PHE PHE A . n 
A 1 38  TYR 38  39  39  TYR TYR A . n 
A 1 39  SER 39  40  40  SER SER A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  ILE 41  42  42  ILE ILE A . n 
A 1 42  GLY 42  43  43  GLY GLY A . n 
A 1 43  ILE 43  44  44  ILE ILE A . n 
A 1 44  ASP 44  45  45  ASP ASP A . n 
A 1 45  GLU 45  46  46  GLU GLU A . n 
A 1 46  LEU 46  47  47  LEU LEU A . n 
A 1 47  VAL 47  48  48  VAL VAL A . n 
A 1 48  PHE 48  49  49  PHE PHE A . n 
A 1 49  LEU 49  50  50  LEU LEU A . n 
A 1 50  ASP 50  51  51  ASP ASP A . n 
A 1 51  ILE 51  52  52  ILE ILE A . n 
A 1 52  THR 52  53  53  THR THR A . n 
A 1 53  ALA 53  54  54  ALA ALA A . n 
A 1 54  SER 54  55  55  SER SER A . n 
A 1 55  VAL 55  56  56  VAL VAL A . n 
A 1 56  GLU 56  57  57  GLU GLU A . n 
A 1 57  LYS 57  58  58  LYS LYS A . n 
A 1 58  ARG 58  59  59  ARG ARG A . n 
A 1 59  LYS 59  60  60  LYS LYS A . n 
A 1 60  THR 60  61  61  THR THR A . n 
A 1 61  MET 61  62  62  MET MET A . n 
A 1 62  LEU 62  63  63  LEU LEU A . n 
A 1 63  GLU 63  64  64  GLU GLU A . n 
A 1 64  LEU 64  65  65  LEU LEU A . n 
A 1 65  VAL 65  66  66  VAL VAL A . n 
A 1 66  GLU 66  67  67  GLU GLU A . n 
A 1 67  LYS 67  68  68  LYS LYS A . n 
A 1 68  VAL 68  69  69  VAL VAL A . n 
A 1 69  ALA 69  70  70  ALA ALA A . n 
A 1 70  GLU 70  71  71  GLU GLU A . n 
A 1 71  GLN 71  72  72  GLN GLN A . n 
A 1 72  ILE 72  73  73  ILE ILE A . n 
A 1 73  ASP 73  74  74  ASP ASP A . n 
A 1 74  ILE 74  75  75  ILE ILE A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  PHE 76  77  77  PHE PHE A . n 
A 1 77  THR 77  78  78  THR THR A . n 
A 1 78  VAL 78  79  79  VAL VAL A . n 
A 1 79  GLY 79  80  80  GLY GLY A . n 
A 1 80  GLY 80  81  81  GLY GLY A . n 
A 1 81  GLY 81  82  82  GLY GLY A . n 
A 1 82  ILE 82  83  83  ILE ILE A . n 
A 1 83  HIS 83  84  84  HIS HIS A . n 
A 1 84  ASP 84  85  85  ASP ASP A . n 
A 1 85  PHE 85  86  86  PHE PHE A . n 
A 1 86  GLU 86  87  87  GLU GLU A . n 
A 1 87  THR 87  88  88  THR THR A . n 
A 1 88  ALA 88  89  89  ALA ALA A . n 
A 1 89  SER 89  90  90  SER SER A . n 
A 1 90  GLU 90  91  91  GLU GLU A . n 
A 1 91  LEU 91  92  92  LEU LEU A . n 
A 1 92  ILE 92  93  93  ILE ILE A . n 
A 1 93  LEU 93  94  94  LEU LEU A . n 
A 1 94  ARG 94  95  95  ARG ARG A . n 
A 1 95  GLY 95  96  96  GLY GLY A . n 
A 1 96  ALA 96  97  97  ALA ALA A . n 
A 1 97  ASP 97  98  98  ASP ASP A . n 
A 1 98  LYS 98  99  99  LYS LYS A . n 
A 1 99  VAL 99  100 100 VAL VAL A . n 
A 1 100 SER 100 101 101 SER SER A . n 
A 1 101 ILE 101 102 102 ILE ILE A . n 
A 1 102 ASN 102 103 103 ASN ASN A . n 
A 1 103 THR 103 104 104 THR THR A . n 
A 1 104 ALA 104 105 105 ALA ALA A . n 
A 1 105 ALA 105 106 106 ALA ALA A . n 
A 1 106 VAL 106 107 107 VAL VAL A . n 
A 1 107 GLU 107 108 108 GLU GLU A . n 
A 1 108 ASN 108 109 109 ASN ASN A . n 
A 1 109 PRO 109 110 110 PRO PRO A . n 
A 1 110 SER 110 111 111 SER SER A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 ILE 112 113 113 ILE ILE A . n 
A 1 113 THR 113 114 114 THR THR A . n 
A 1 114 GLN 114 115 115 GLN GLN A . n 
A 1 115 ILE 115 116 116 ILE ILE A . n 
A 1 116 ALA 116 117 117 ALA ALA A . n 
A 1 117 GLN 117 118 118 GLN GLN A . n 
A 1 118 THR 118 119 119 THR THR A . n 
A 1 119 PHE 119 120 120 PHE PHE A . n 
A 1 120 GLY 120 121 121 GLY GLY A . n 
A 1 121 SER 121 122 122 SER SER A . n 
A 1 122 GLN 122 123 123 GLN GLN A . n 
A 1 123 ALA 123 124 124 ALA ALA A . n 
A 1 124 VAL 124 125 125 VAL VAL A . n 
A 1 125 VAL 125 126 126 VAL VAL A . n 
A 1 126 VAL 126 127 127 VAL VAL A . n 
A 1 127 ALA 127 128 128 ALA ALA A . n 
A 1 128 ILE 128 129 129 ILE ILE A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 LYS 131 132 132 LYS LYS A . n 
A 1 132 ARG 132 133 133 ARG ARG A . n 
A 1 133 VAL 133 134 134 VAL VAL A . n 
A 1 134 ASP 134 135 135 ASP ASP A . n 
A 1 135 GLY 135 136 136 GLY GLY A . n 
A 1 136 GLU 136 137 137 GLU GLU A . n 
A 1 137 PHE 137 138 138 PHE PHE A . n 
A 1 138 MET 138 139 139 MET MET A . n 
A 1 139 VAL 139 140 140 VAL VAL A . n 
A 1 140 PHE 140 141 141 PHE PHE A . n 
A 1 141 THR 141 142 142 THR THR A . n 
A 1 142 TYR 142 143 143 TYR TYR A . n 
A 1 143 SER 143 144 144 SER SER A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 LYS 145 146 146 LYS LYS A . n 
A 1 146 LYS 146 147 147 LYS LYS A . n 
A 1 147 ASN 147 148 148 ASN ASN A . n 
A 1 148 THR 148 149 149 THR THR A . n 
A 1 149 GLY 149 150 150 GLY GLY A . n 
A 1 150 ILE 150 151 151 ILE ILE A . n 
A 1 151 LEU 151 152 152 LEU LEU A . n 
A 1 152 LEU 152 153 153 LEU LEU A . n 
A 1 153 ARG 153 154 154 ARG ARG A . n 
A 1 154 ASP 154 155 155 ASP ASP A . n 
A 1 155 TRP 155 156 156 TRP TRP A . n 
A 1 156 VAL 156 157 157 VAL VAL A . n 
A 1 157 VAL 157 158 158 VAL VAL A . n 
A 1 158 GLU 158 159 159 GLU GLU A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 GLU 160 161 161 GLU GLU A . n 
A 1 161 LYS 161 162 162 LYS LYS A . n 
A 1 162 ARG 162 163 163 ARG ARG A . n 
A 1 163 GLY 163 164 164 GLY GLY A . n 
A 1 164 ALA 164 165 165 ALA ALA A . n 
A 1 165 GLY 165 166 166 GLY GLY A . n 
A 1 166 GLU 166 167 167 GLU GLU A . n 
A 1 167 ILE 167 168 168 ILE ILE A . n 
A 1 168 LEU 168 169 169 LEU LEU A . n 
A 1 169 LEU 169 170 170 LEU LEU A . n 
A 1 170 THR 170 171 171 THR THR A . n 
A 1 171 SER 171 172 172 SER SER A . n 
A 1 172 ILE 172 173 173 ILE ILE A . n 
A 1 173 ASP 173 174 174 ASP ASP A . n 
A 1 174 ARG 174 175 175 ARG ARG A . n 
A 1 175 ASP 175 176 176 ASP ASP A . n 
A 1 176 GLY 176 177 177 GLY GLY A . n 
A 1 177 THR 177 178 178 THR THR A . n 
A 1 178 LYS 178 179 179 LYS LYS A . n 
A 1 179 SER 179 180 180 SER SER A . n 
A 1 180 GLY 180 181 181 GLY GLY A . n 
A 1 181 TYR 181 182 182 TYR TYR A . n 
A 1 182 ASP 182 183 183 ASP ASP A . n 
A 1 183 THR 183 184 184 THR THR A . n 
A 1 184 GLU 184 185 185 GLU GLU A . n 
A 1 185 MET 185 186 186 MET MET A . n 
A 1 186 ILE 186 187 187 ILE ILE A . n 
A 1 187 ARG 187 188 188 ARG ARG A . n 
A 1 188 PHE 188 189 189 PHE PHE A . n 
A 1 189 VAL 189 190 190 VAL VAL A . n 
A 1 190 ARG 190 191 191 ARG ARG A . n 
A 1 191 PRO 191 192 192 PRO PRO A . n 
A 1 192 LEU 192 193 193 LEU LEU A . n 
A 1 193 THR 193 194 194 THR THR A . n 
A 1 194 THR 194 195 195 THR THR A . n 
A 1 195 LEU 195 196 196 LEU LEU A . n 
A 1 196 PRO 196 197 197 PRO PRO A . n 
A 1 197 ILE 197 198 198 ILE ILE A . n 
A 1 198 ILE 198 199 199 ILE ILE A . n 
A 1 199 ALA 199 200 200 ALA ALA A . n 
A 1 200 SER 200 201 201 SER SER A . n 
A 1 201 GLY 201 202 202 GLY GLY A . n 
A 1 202 GLY 202 203 203 GLY GLY A . n 
A 1 203 ALA 203 204 204 ALA ALA A . n 
A 1 204 GLY 204 205 205 GLY GLY A . n 
A 1 205 LYS 205 206 206 LYS LYS A . n 
A 1 206 MET 206 207 207 MET MET A . n 
A 1 207 GLU 207 208 208 GLU GLU A . n 
A 1 208 HIS 208 209 209 HIS HIS A . n 
A 1 209 PHE 209 210 210 PHE PHE A . n 
A 1 210 LEU 210 211 211 LEU LEU A . n 
A 1 211 GLU 211 212 212 GLU GLU A . n 
A 1 212 ALA 212 213 213 ALA ALA A . n 
A 1 213 PHE 213 214 214 PHE PHE A . n 
A 1 214 LEU 214 215 215 LEU LEU A . n 
A 1 215 ALA 215 216 216 ALA ALA A . n 
A 1 216 GLY 216 217 217 GLY GLY A . n 
A 1 217 ALA 217 218 218 ALA ALA A . n 
A 1 218 ASP 218 219 219 ASP ASP A . n 
A 1 219 ALA 219 220 220 ALA ALA A . n 
A 1 220 ALA 220 221 221 ALA ALA A . n 
A 1 221 LEU 221 222 222 LEU LEU A . n 
A 1 222 ALA 222 223 223 ALA ALA A . n 
A 1 223 ALA 223 224 224 ALA ALA A . n 
A 1 224 SER 224 225 225 SER SER A . n 
A 1 225 VAL 225 226 226 VAL VAL A . n 
A 1 226 PHE 226 227 227 PHE PHE A . n 
A 1 227 HIS 227 228 228 HIS HIS A . n 
A 1 228 PHE 228 229 229 PHE PHE A . n 
A 1 229 ARG 229 230 230 ARG ARG A . n 
A 1 230 GLU 230 231 231 GLU GLU A . n 
A 1 231 ILE 231 232 232 ILE ILE A . n 
A 1 232 ASP 232 233 233 ASP ASP A . n 
A 1 233 VAL 233 234 234 VAL VAL A . n 
A 1 234 ARG 234 235 235 ARG ARG A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 LEU 236 237 237 LEU LEU A . n 
A 1 237 LYS 237 238 238 LYS LYS A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 TYR 239 240 240 TYR TYR A . n 
A 1 240 LEU 240 241 241 LEU LEU A . n 
A 1 241 LYS 241 242 242 LYS LYS A . n 
A 1 242 LYS 242 243 243 LYS LYS A . n 
A 1 243 HIS 243 244 244 HIS HIS A . n 
A 1 244 GLY 244 245 245 GLY GLY A . n 
A 1 245 VAL 245 246 246 VAL VAL A . n 
A 1 246 ASN 246 247 247 ASN ASN A . n 
A 1 247 VAL 247 248 248 VAL VAL A . n 
A 1 248 ARG 248 249 249 ARG ARG A . n 
A 1 249 LEU 249 250 250 LEU LEU A . n 
A 1 250 GLU 250 251 251 GLU GLU A . n 
A 1 251 LEU 251 252 252 LEU LEU A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   301 156 HOH HOH A . 
B 2 HOH 2   302 133 HOH HOH A . 
B 2 HOH 3   303 119 HOH HOH A . 
B 2 HOH 4   304 242 HOH HOH A . 
B 2 HOH 5   305 244 HOH HOH A . 
B 2 HOH 6   306 83  HOH HOH A . 
B 2 HOH 7   307 134 HOH HOH A . 
B 2 HOH 8   308 247 HOH HOH A . 
B 2 HOH 9   309 211 HOH HOH A . 
B 2 HOH 10  310 226 HOH HOH A . 
B 2 HOH 11  311 209 HOH HOH A . 
B 2 HOH 12  312 80  HOH HOH A . 
B 2 HOH 13  313 227 HOH HOH A . 
B 2 HOH 14  314 55  HOH HOH A . 
B 2 HOH 15  315 120 HOH HOH A . 
B 2 HOH 16  316 126 HOH HOH A . 
B 2 HOH 17  317 213 HOH HOH A . 
B 2 HOH 18  318 169 HOH HOH A . 
B 2 HOH 19  319 57  HOH HOH A . 
B 2 HOH 20  320 214 HOH HOH A . 
B 2 HOH 21  321 199 HOH HOH A . 
B 2 HOH 22  322 76  HOH HOH A . 
B 2 HOH 23  323 86  HOH HOH A . 
B 2 HOH 24  324 206 HOH HOH A . 
B 2 HOH 25  325 185 HOH HOH A . 
B 2 HOH 26  326 181 HOH HOH A . 
B 2 HOH 27  327 159 HOH HOH A . 
B 2 HOH 28  328 46  HOH HOH A . 
B 2 HOH 29  329 204 HOH HOH A . 
B 2 HOH 30  330 24  HOH HOH A . 
B 2 HOH 31  331 178 HOH HOH A . 
B 2 HOH 32  332 184 HOH HOH A . 
B 2 HOH 33  333 58  HOH HOH A . 
B 2 HOH 34  334 229 HOH HOH A . 
B 2 HOH 35  335 165 HOH HOH A . 
B 2 HOH 36  336 9   HOH HOH A . 
B 2 HOH 37  337 61  HOH HOH A . 
B 2 HOH 38  338 139 HOH HOH A . 
B 2 HOH 39  339 109 HOH HOH A . 
B 2 HOH 40  340 173 HOH HOH A . 
B 2 HOH 41  341 122 HOH HOH A . 
B 2 HOH 42  342 62  HOH HOH A . 
B 2 HOH 43  343 20  HOH HOH A . 
B 2 HOH 44  344 34  HOH HOH A . 
B 2 HOH 45  345 4   HOH HOH A . 
B 2 HOH 46  346 3   HOH HOH A . 
B 2 HOH 47  347 72  HOH HOH A . 
B 2 HOH 48  348 6   HOH HOH A . 
B 2 HOH 49  349 59  HOH HOH A . 
B 2 HOH 50  350 66  HOH HOH A . 
B 2 HOH 51  351 121 HOH HOH A . 
B 2 HOH 52  352 222 HOH HOH A . 
B 2 HOH 53  353 236 HOH HOH A . 
B 2 HOH 54  354 116 HOH HOH A . 
B 2 HOH 55  355 103 HOH HOH A . 
B 2 HOH 56  356 235 HOH HOH A . 
B 2 HOH 57  357 91  HOH HOH A . 
B 2 HOH 58  358 217 HOH HOH A . 
B 2 HOH 59  359 18  HOH HOH A . 
B 2 HOH 60  360 15  HOH HOH A . 
B 2 HOH 61  361 115 HOH HOH A . 
B 2 HOH 62  362 113 HOH HOH A . 
B 2 HOH 63  363 52  HOH HOH A . 
B 2 HOH 64  364 77  HOH HOH A . 
B 2 HOH 65  365 33  HOH HOH A . 
B 2 HOH 66  366 38  HOH HOH A . 
B 2 HOH 67  367 154 HOH HOH A . 
B 2 HOH 68  368 70  HOH HOH A . 
B 2 HOH 69  369 21  HOH HOH A . 
B 2 HOH 70  370 136 HOH HOH A . 
B 2 HOH 71  371 75  HOH HOH A . 
B 2 HOH 72  372 65  HOH HOH A . 
B 2 HOH 73  373 48  HOH HOH A . 
B 2 HOH 74  374 233 HOH HOH A . 
B 2 HOH 75  375 8   HOH HOH A . 
B 2 HOH 76  376 212 HOH HOH A . 
B 2 HOH 77  377 74  HOH HOH A . 
B 2 HOH 78  378 32  HOH HOH A . 
B 2 HOH 79  379 187 HOH HOH A . 
B 2 HOH 80  380 29  HOH HOH A . 
B 2 HOH 81  381 208 HOH HOH A . 
B 2 HOH 82  382 22  HOH HOH A . 
B 2 HOH 83  383 56  HOH HOH A . 
B 2 HOH 84  384 108 HOH HOH A . 
B 2 HOH 85  385 14  HOH HOH A . 
B 2 HOH 86  386 26  HOH HOH A . 
B 2 HOH 87  387 148 HOH HOH A . 
B 2 HOH 88  388 47  HOH HOH A . 
B 2 HOH 89  389 104 HOH HOH A . 
B 2 HOH 90  390 147 HOH HOH A . 
B 2 HOH 91  391 106 HOH HOH A . 
B 2 HOH 92  392 97  HOH HOH A . 
B 2 HOH 93  393 81  HOH HOH A . 
B 2 HOH 94  394 166 HOH HOH A . 
B 2 HOH 95  395 167 HOH HOH A . 
B 2 HOH 96  396 164 HOH HOH A . 
B 2 HOH 97  397 127 HOH HOH A . 
B 2 HOH 98  398 192 HOH HOH A . 
B 2 HOH 99  399 176 HOH HOH A . 
B 2 HOH 100 400 252 HOH HOH A . 
B 2 HOH 101 401 258 HOH HOH A . 
B 2 HOH 102 402 84  HOH HOH A . 
B 2 HOH 103 403 102 HOH HOH A . 
B 2 HOH 104 404 2   HOH HOH A . 
B 2 HOH 105 405 99  HOH HOH A . 
B 2 HOH 106 406 71  HOH HOH A . 
B 2 HOH 107 407 171 HOH HOH A . 
B 2 HOH 108 408 234 HOH HOH A . 
B 2 HOH 109 409 43  HOH HOH A . 
B 2 HOH 110 410 69  HOH HOH A . 
B 2 HOH 111 411 149 HOH HOH A . 
B 2 HOH 112 412 123 HOH HOH A . 
B 2 HOH 113 413 168 HOH HOH A . 
B 2 HOH 114 414 51  HOH HOH A . 
B 2 HOH 115 415 182 HOH HOH A . 
B 2 HOH 116 416 246 HOH HOH A . 
B 2 HOH 117 417 105 HOH HOH A . 
B 2 HOH 118 418 31  HOH HOH A . 
B 2 HOH 119 419 49  HOH HOH A . 
B 2 HOH 120 420 146 HOH HOH A . 
B 2 HOH 121 421 224 HOH HOH A . 
B 2 HOH 122 422 30  HOH HOH A . 
B 2 HOH 123 423 27  HOH HOH A . 
B 2 HOH 124 424 183 HOH HOH A . 
B 2 HOH 125 425 151 HOH HOH A . 
B 2 HOH 126 426 135 HOH HOH A . 
B 2 HOH 127 427 129 HOH HOH A . 
B 2 HOH 128 428 79  HOH HOH A . 
B 2 HOH 129 429 23  HOH HOH A . 
B 2 HOH 130 430 11  HOH HOH A . 
B 2 HOH 131 431 101 HOH HOH A . 
B 2 HOH 132 432 112 HOH HOH A . 
B 2 HOH 133 433 12  HOH HOH A . 
B 2 HOH 134 434 143 HOH HOH A . 
B 2 HOH 135 435 195 HOH HOH A . 
B 2 HOH 136 436 124 HOH HOH A . 
B 2 HOH 137 437 228 HOH HOH A . 
B 2 HOH 138 438 39  HOH HOH A . 
B 2 HOH 139 439 17  HOH HOH A . 
B 2 HOH 140 440 19  HOH HOH A . 
B 2 HOH 141 441 78  HOH HOH A . 
B 2 HOH 142 442 197 HOH HOH A . 
B 2 HOH 143 443 7   HOH HOH A . 
B 2 HOH 144 444 25  HOH HOH A . 
B 2 HOH 145 445 10  HOH HOH A . 
B 2 HOH 146 446 5   HOH HOH A . 
B 2 HOH 147 447 42  HOH HOH A . 
B 2 HOH 148 448 36  HOH HOH A . 
B 2 HOH 149 449 63  HOH HOH A . 
B 2 HOH 150 450 37  HOH HOH A . 
B 2 HOH 151 451 144 HOH HOH A . 
B 2 HOH 152 452 13  HOH HOH A . 
B 2 HOH 153 453 100 HOH HOH A . 
B 2 HOH 154 454 128 HOH HOH A . 
B 2 HOH 155 455 44  HOH HOH A . 
B 2 HOH 156 456 125 HOH HOH A . 
B 2 HOH 157 457 174 HOH HOH A . 
B 2 HOH 158 458 175 HOH HOH A . 
B 2 HOH 159 459 216 HOH HOH A . 
B 2 HOH 160 460 177 HOH HOH A . 
B 2 HOH 161 461 41  HOH HOH A . 
B 2 HOH 162 462 201 HOH HOH A . 
B 2 HOH 163 463 161 HOH HOH A . 
B 2 HOH 164 464 45  HOH HOH A . 
B 2 HOH 165 465 253 HOH HOH A . 
B 2 HOH 166 466 16  HOH HOH A . 
B 2 HOH 167 467 64  HOH HOH A . 
B 2 HOH 168 468 28  HOH HOH A . 
B 2 HOH 169 469 85  HOH HOH A . 
B 2 HOH 170 470 219 HOH HOH A . 
B 2 HOH 171 471 131 HOH HOH A . 
B 2 HOH 172 472 60  HOH HOH A . 
B 2 HOH 173 473 94  HOH HOH A . 
B 2 HOH 174 474 137 HOH HOH A . 
B 2 HOH 175 475 245 HOH HOH A . 
B 2 HOH 176 476 157 HOH HOH A . 
B 2 HOH 177 477 130 HOH HOH A . 
B 2 HOH 178 478 73  HOH HOH A . 
B 2 HOH 179 479 53  HOH HOH A . 
B 2 HOH 180 480 239 HOH HOH A . 
B 2 HOH 181 481 114 HOH HOH A . 
B 2 HOH 182 482 188 HOH HOH A . 
B 2 HOH 183 483 88  HOH HOH A . 
B 2 HOH 184 484 225 HOH HOH A . 
B 2 HOH 185 485 138 HOH HOH A . 
B 2 HOH 186 486 202 HOH HOH A . 
B 2 HOH 187 487 87  HOH HOH A . 
B 2 HOH 188 488 50  HOH HOH A . 
B 2 HOH 189 489 92  HOH HOH A . 
B 2 HOH 190 490 256 HOH HOH A . 
B 2 HOH 191 491 68  HOH HOH A . 
B 2 HOH 192 492 1   HOH HOH A . 
B 2 HOH 193 493 82  HOH HOH A . 
B 2 HOH 194 494 196 HOH HOH A . 
B 2 HOH 195 495 90  HOH HOH A . 
B 2 HOH 196 496 118 HOH HOH A . 
B 2 HOH 197 497 231 HOH HOH A . 
B 2 HOH 198 498 232 HOH HOH A . 
B 2 HOH 199 499 162 HOH HOH A . 
B 2 HOH 200 500 230 HOH HOH A . 
B 2 HOH 201 501 255 HOH HOH A . 
B 2 HOH 202 502 107 HOH HOH A . 
B 2 HOH 203 503 243 HOH HOH A . 
B 2 HOH 204 504 193 HOH HOH A . 
B 2 HOH 205 505 241 HOH HOH A . 
B 2 HOH 206 506 191 HOH HOH A . 
B 2 HOH 207 507 198 HOH HOH A . 
B 2 HOH 208 508 172 HOH HOH A . 
B 2 HOH 209 509 89  HOH HOH A . 
B 2 HOH 210 510 215 HOH HOH A . 
B 2 HOH 211 511 54  HOH HOH A . 
B 2 HOH 212 512 170 HOH HOH A . 
B 2 HOH 213 513 220 HOH HOH A . 
B 2 HOH 214 514 240 HOH HOH A . 
B 2 HOH 215 515 238 HOH HOH A . 
B 2 HOH 216 516 95  HOH HOH A . 
B 2 HOH 217 517 210 HOH HOH A . 
B 2 HOH 218 518 250 HOH HOH A . 
B 2 HOH 219 519 254 HOH HOH A . 
B 2 HOH 220 520 163 HOH HOH A . 
B 2 HOH 221 521 93  HOH HOH A . 
B 2 HOH 222 522 223 HOH HOH A . 
B 2 HOH 223 523 179 HOH HOH A . 
B 2 HOH 224 524 218 HOH HOH A . 
B 2 HOH 225 525 142 HOH HOH A . 
B 2 HOH 226 526 221 HOH HOH A . 
B 2 HOH 227 527 237 HOH HOH A . 
B 2 HOH 228 528 189 HOH HOH A . 
B 2 HOH 229 529 205 HOH HOH A . 
B 2 HOH 230 530 186 HOH HOH A . 
B 2 HOH 231 531 110 HOH HOH A . 
B 2 HOH 232 532 98  HOH HOH A . 
B 2 HOH 233 533 249 HOH HOH A . 
B 2 HOH 234 534 194 HOH HOH A . 
B 2 HOH 235 535 111 HOH HOH A . 
B 2 HOH 236 536 160 HOH HOH A . 
B 2 HOH 237 537 251 HOH HOH A . 
B 2 HOH 238 538 155 HOH HOH A . 
B 2 HOH 239 539 158 HOH HOH A . 
B 2 HOH 240 540 152 HOH HOH A . 
B 2 HOH 241 541 200 HOH HOH A . 
B 2 HOH 242 542 35  HOH HOH A . 
B 2 HOH 243 543 96  HOH HOH A . 
B 2 HOH 244 544 180 HOH HOH A . 
B 2 HOH 245 545 132 HOH HOH A . 
B 2 HOH 246 546 67  HOH HOH A . 
B 2 HOH 247 547 117 HOH HOH A . 
B 2 HOH 248 548 248 HOH HOH A . 
B 2 HOH 249 549 40  HOH HOH A . 
B 2 HOH 250 550 141 HOH HOH A . 
B 2 HOH 251 551 203 HOH HOH A . 
B 2 HOH 252 552 145 HOH HOH A . 
B 2 HOH 253 553 207 HOH HOH A . 
B 2 HOH 254 554 153 HOH HOH A . 
B 2 HOH 255 555 190 HOH HOH A . 
B 2 HOH 256 556 140 HOH HOH A . 
B 2 HOH 257 557 150 HOH HOH A . 
B 2 HOH 258 558 257 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 GLU 24 ? CG  ? A GLU 23 CG  
2  1 Y 1 A GLU 24 ? CD  ? A GLU 23 CD  
3  1 Y 1 A GLU 24 ? OE1 ? A GLU 23 OE1 
4  1 Y 1 A GLU 24 ? OE2 ? A GLU 23 OE2 
5  1 Y 1 A LYS 37 ? CD  ? A LYS 36 CD  
6  1 Y 1 A LYS 37 ? CE  ? A LYS 36 CE  
7  1 Y 1 A LYS 37 ? NZ  ? A LYS 36 NZ  
8  1 Y 1 A LYS 60 ? CG  ? A LYS 59 CG  
9  1 Y 1 A LYS 60 ? CD  ? A LYS 59 CD  
10 1 Y 1 A LYS 60 ? CE  ? A LYS 59 CE  
11 1 Y 1 A LYS 60 ? NZ  ? A LYS 59 NZ  
12 1 Y 1 A ASP 74 ? CG  ? A ASP 73 CG  
13 1 Y 1 A ASP 74 ? OD1 ? A ASP 73 OD1 
14 1 Y 1 A ASP 74 ? OD2 ? A ASP 73 OD2 
15 1 Y 1 A GLU 91 ? CG  ? A GLU 90 CG  
16 1 Y 1 A GLU 91 ? CD  ? A GLU 90 CD  
17 1 Y 1 A GLU 91 ? OE1 ? A GLU 90 OE1 
18 1 Y 1 A GLU 91 ? OE2 ? A GLU 90 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.14_3260: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S8S 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.272 
_cell.length_a_esd                 ? 
_cell.length_b                     58.059 
_cell.length_b_esd                 ? 
_cell.length_c                     82.383 
_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                         8S8S 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8S8S 
_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             1.92 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.86 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    'ammonium phosphate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 200K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-12-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S8S 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.314 
_reflns.d_resolution_low                               47.46 
_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                                     49373 
_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                           96.16 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.86 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.314 
_reflns_shell.d_res_low                                     47.46 
_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                             49373 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.999 
_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               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S8S 
_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                            1.314 
_refine.ls_d_res_low                             47.458 
_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                     49361 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.10 
_refine.ls_percent_reflns_R_free                 4.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1889 
_refine.ls_R_factor_R_free                       0.2095 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1880 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.13 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1923 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             258 
_refine_hist.number_atoms_total               2181 
_refine_hist.d_res_high                       1.314 
_refine_hist.d_res_low                        47.458 
# 
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' ? 0.005 ? 2043 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.760 ? 2769 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.766 ? 1180 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076 ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 360  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.314  1.3466 . . 101 2410 69.00  . . . . 0.4475 . . . . . . . . . . . 0.4637 
'X-RAY DIFFRACTION' 1.3466 1.3831 . . 126 2961 85.00  . . . . 0.4209 . . . . . . . . . . . 0.4252 
'X-RAY DIFFRACTION' 1.3831 1.4238 . . 142 3350 97.00  . . . . 0.3739 . . . . . . . . . . . 0.3518 
'X-RAY DIFFRACTION' 1.4238 1.4697 . . 144 3436 99.00  . . . . 0.3066 . . . . . . . . . . . 0.3804 
'X-RAY DIFFRACTION' 1.4697 1.5222 . . 147 3475 100.00 . . . . 0.2689 . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 1.5222 1.5832 . . 147 3476 99.00  . . . . 0.2439 . . . . . . . . . . . 0.2546 
'X-RAY DIFFRACTION' 1.5832 1.6553 . . 147 3482 100.00 . . . . 0.1857 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.6553 1.7425 . . 146 3447 99.00  . . . . 0.1924 . . . . . . . . . . . 0.2241 
'X-RAY DIFFRACTION' 1.7425 1.8517 . . 147 3494 100.00 . . . . 0.1899 . . . . . . . . . . . 0.2252 
'X-RAY DIFFRACTION' 1.8517 1.9947 . . 148 3498 100.00 . . . . 0.1889 . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 1.9947 2.1954 . . 149 3537 100.00 . . . . 0.1768 . . . . . . . . . . . 0.1923 
'X-RAY DIFFRACTION' 2.1954 2.5131 . . 148 3499 99.00  . . . . 0.1764 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 2.5131 3.1661 . . 152 3588 100.00 . . . . 0.1798 . . . . . . . . . . . 0.1797 
'X-RAY DIFFRACTION' 3.1661 47.4   . . 155 3709 99.00  . . . . 0.1581 . . . . . . . . . . . 0.1916 
# 
_struct.entry_id                     8S8S 
_struct.title                        'An induced-fit motion of a mobile loop' 
_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        8S8S 
_struct_keywords.text            'histidine and purine biosynthesis, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL 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                    UNP 
_struct_ref.db_code                    HIS6_THEMA 
_struct_ref.pdbx_db_accession          Q9X0C6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LAKRIIACLDVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGG
GIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVE
KRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYL
KKHGVNVRLE
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8S8S 
_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                 250 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9X0C6 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  251 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       251 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8S8S PRO A 19  ? UNP Q9X0C6 GLY 20 conflict         20  1 
1 8S8S LEU A 251 ? UNP Q9X0C6 ?   ?  'expression tag' 252 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 0     ? 
1 MORE         0     ? 
1 'SSA (A^2)'  10900 ? 
# 
_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   none 
_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 ASP A 30  ? ILE A 41  ? ASP A 31  ILE A 42  1 ? 12 
HELX_P HELX_P2  AA2 ALA A 53  ? GLU A 70  ? ALA A 54  GLU A 71  1 ? 18 
HELX_P HELX_P3  AA3 ASP A 84  ? ARG A 94  ? ASP A 85  ARG A 95  1 ? 11 
HELX_P HELX_P4  AA4 ASN A 102 ? ASN A 108 ? ASN A 103 ASN A 109 1 ? 7  
HELX_P HELX_P5  AA5 PRO A 109 ? GLY A 120 ? PRO A 110 GLY A 121 1 ? 12 
HELX_P HELX_P6  AA6 LEU A 152 ? ARG A 162 ? LEU A 153 ARG A 163 1 ? 11 
HELX_P HELX_P7  AA7 ASP A 182 ? ARG A 190 ? ASP A 183 ARG A 191 1 ? 9  
HELX_P HELX_P8  AA8 PRO A 191 ? THR A 193 ? PRO A 192 THR A 194 5 ? 3  
HELX_P HELX_P9  AA9 LYS A 205 ? ALA A 215 ? LYS A 206 ALA A 216 1 ? 11 
HELX_P HELX_P10 AB1 ALA A 223 ? PHE A 228 ? ALA A 224 PHE A 229 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 232 ? HIS A 243 ? ASP A 233 HIS A 244 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 15  ? VAL A 16  ? ARG A 16  VAL A 17  
AA1 2 ARG A 4   ? LYS A 12  ? ARG A 5   LYS A 13  
AA1 3 GLU A 45  ? ASP A 50  ? GLU A 46  ASP A 51  
AA1 4 PHE A 76  ? GLY A 79  ? PHE A 77  GLY A 80  
AA1 5 LYS A 98  ? ILE A 101 ? LYS A 99  ILE A 102 
AA1 6 VAL A 124 ? VAL A 133 ? VAL A 125 VAL A 134 
AA1 7 GLU A 136 ? THR A 141 ? GLU A 137 THR A 142 
AA1 8 LYS A 146 ? LEU A 151 ? LYS A 147 LEU A 152 
AA2 1 ARG A 15  ? VAL A 16  ? ARG A 16  VAL A 17  
AA2 2 ARG A 4   ? LYS A 12  ? ARG A 5   LYS A 13  
AA2 3 ALA A 219 ? ALA A 222 ? ALA A 220 ALA A 223 
AA2 4 ILE A 197 ? SER A 200 ? ILE A 198 SER A 201 
AA2 5 GLU A 166 ? SER A 171 ? GLU A 167 SER A 172 
AA2 6 VAL A 124 ? VAL A 133 ? VAL A 125 VAL A 134 
AA2 7 GLU A 136 ? THR A 141 ? GLU A 137 THR A 142 
AA2 8 LYS A 146 ? LEU A 151 ? LYS A 147 LEU A 152 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 15  ? O ARG A 16  N LYS A 12  ? N LYS A 13  
AA1 2 3 N LEU A 9   ? N LEU A 10  O VAL A 47  ? O VAL A 48  
AA1 3 4 N PHE A 48  ? N PHE A 49  O THR A 77  ? O THR A 78  
AA1 4 5 N VAL A 78  ? N VAL A 79  O SER A 100 ? O SER A 101 
AA1 5 6 N VAL A 99  ? N VAL A 100 O VAL A 125 ? O VAL A 126 
AA1 6 7 N LYS A 131 ? N LYS A 132 O MET A 138 ? O MET A 139 
AA1 7 8 N VAL A 139 ? N VAL A 140 O ILE A 150 ? O ILE A 151 
AA2 1 2 O ARG A 15  ? O ARG A 16  N LYS A 12  ? N LYS A 13  
AA2 2 3 N ILE A 6   ? N ILE A 7   O ALA A 220 ? O ALA A 221 
AA2 3 4 O ALA A 219 ? O ALA A 220 N ALA A 199 ? N ALA A 200 
AA2 4 5 O ILE A 198 ? O ILE A 199 N ILE A 167 ? N ILE A 168 
AA2 5 6 O LEU A 168 ? O LEU A 169 N ILE A 128 ? N ILE A 129 
AA2 6 7 N LYS A 131 ? N LYS A 132 O MET A 138 ? O MET A 139 
AA2 7 8 N VAL A 139 ? N VAL A 140 O ILE A 150 ? O ILE A 151 
# 
_pdbx_entry_details.entry_id                   8S8S 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 O   A HOH 309 ? ? O A HOH 353 ? ? 1.92 
2  1 O   A HOH 408 ? ? O A HOH 486 ? ? 2.01 
3  1 O   A HOH 329 ? ? O A HOH 537 ? ? 2.05 
4  1 O   A HOH 522 ? ? O A HOH 541 ? ? 2.05 
5  1 OE1 A GLU 212 ? ? O A HOH 301 ? ? 2.12 
6  1 OE2 A GLU 71  ? ? O A HOH 302 ? ? 2.14 
7  1 O   A HOH 528 ? ? O A HOH 532 ? ? 2.15 
8  1 O   A HOH 306 ? ? O A HOH 395 ? ? 2.17 
9  1 NH2 A ARG 230 ? ? O A HOH 303 ? ? 2.18 
10 1 O   A HOH 396 ? ? O A HOH 397 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 103 ? ? -141.52 -83.31 
2 1 ALA A 224 ? ? -136.83 -90.19 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          wild 
# 
_atom_sites.entry_id                    8S8S 
_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]   0.022588 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017224 
_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]   0.012138 
_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   . LEU A 1 1   ? 20.431 14.369  -12.487 1.00 36.13 ? 2   LEU A N   1 
ATOM   2    C CA  . LEU A 1 1   ? 19.998 13.540  -13.614 1.00 31.55 ? 2   LEU A CA  1 
ATOM   3    C C   . LEU A 1 1   ? 18.512 13.208  -13.518 1.00 25.56 ? 2   LEU A C   1 
ATOM   4    O O   . LEU A 1 1   ? 17.956 13.143  -12.422 1.00 25.09 ? 2   LEU A O   1 
ATOM   5    C CB  . LEU A 1 1   ? 20.815 12.247  -13.681 1.00 33.56 ? 2   LEU A CB  1 
ATOM   6    C CG  . LEU A 1 1   ? 22.309 12.368  -13.996 1.00 31.46 ? 2   LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 1   ? 22.842 11.084  -14.623 1.00 30.50 ? 2   LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 1   ? 22.581 13.560  -14.904 1.00 37.80 ? 2   LEU A CD2 1 
ATOM   9    N N   . ALA A 1 2   ? 17.865 13.013  -14.669 1.00 21.87 ? 3   ALA A N   1 
ATOM   10   C CA  . ALA A 1 2   ? 16.454 12.648  -14.662 1.00 21.06 ? 3   ALA A CA  1 
ATOM   11   C C   . ALA A 1 2   ? 16.274 11.358  -13.875 1.00 21.79 ? 3   ALA A C   1 
ATOM   12   O O   . ALA A 1 2   ? 17.116 10.458  -13.930 1.00 22.49 ? 3   ALA A O   1 
ATOM   13   C CB  . ALA A 1 2   ? 15.951 12.440  -16.092 1.00 21.29 ? 3   ALA A CB  1 
ATOM   14   N N   . LYS A 1 3   ? 15.163 11.264  -13.152 1.00 17.19 ? 4   LYS A N   1 
ATOM   15   C CA  . LYS A 1 3   ? 14.940 10.105  -12.300 1.00 17.74 ? 4   LYS A CA  1 
ATOM   16   C C   . LYS A 1 3   ? 14.618 8.876   -13.136 1.00 19.34 ? 4   LYS A C   1 
ATOM   17   O O   . LYS A 1 3   ? 14.064 8.967   -14.235 1.00 22.64 ? 4   LYS A O   1 
ATOM   18   C CB  . LYS A 1 3   ? 13.783 10.367  -11.333 1.00 18.72 ? 4   LYS A CB  1 
ATOM   19   C CG  . LYS A 1 3   ? 13.944 11.630  -10.519 1.00 19.37 ? 4   LYS A CG  1 
ATOM   20   C CD  . LYS A 1 3   ? 15.253 11.647  -9.734  1.00 19.53 ? 4   LYS A CD  1 
ATOM   21   C CE  . LYS A 1 3   ? 15.296 12.883  -8.841  1.00 20.80 ? 4   LYS A CE  1 
ATOM   22   N NZ  . LYS A 1 3   ? 16.539 12.958  -8.034  1.00 20.18 ? 4   LYS A NZ  1 
ATOM   23   N N   . ARG A 1 4   ? 14.945 7.706   -12.587 1.00 17.48 ? 5   ARG A N   1 
ATOM   24   C CA  . ARG A 1 4   ? 14.692 6.434   -13.243 1.00 16.96 ? 5   ARG A CA  1 
ATOM   25   C C   . ARG A 1 4   ? 13.713 5.600   -12.428 1.00 15.94 ? 5   ARG A C   1 
ATOM   26   O O   . ARG A 1 4   ? 13.758 5.601   -11.190 1.00 18.25 ? 5   ARG A O   1 
ATOM   27   C CB  . ARG A 1 4   ? 15.989 5.633   -13.381 1.00 18.20 ? 5   ARG A CB  1 
ATOM   28   C CG  . ARG A 1 4   ? 16.952 6.179   -14.431 1.00 22.43 ? 5   ARG A CG  1 
ATOM   29   C CD  . ARG A 1 4   ? 18.327 5.543   -14.294 1.00 22.49 ? 5   ARG A CD  1 
ATOM   30   N NE  . ARG A 1 4   ? 19.032 6.078   -13.139 1.00 23.08 ? 5   ARG A NE  1 
ATOM   31   C CZ  . ARG A 1 4   ? 19.830 5.359   -12.357 1.00 24.70 ? 5   ARG A CZ  1 
ATOM   32   N NH1 . ARG A 1 4   ? 20.014 4.067   -12.594 1.00 25.86 ? 5   ARG A NH1 1 
ATOM   33   N NH2 . ARG A 1 4   ? 20.436 5.930   -11.327 1.00 23.85 ? 5   ARG A NH2 1 
ATOM   34   N N   . ILE A 1 5   ? 12.838 4.896   -13.136 1.00 15.68 ? 6   ILE A N   1 
ATOM   35   C CA  . ILE A 1 5   ? 11.940 3.904   -12.553 1.00 15.08 ? 6   ILE A CA  1 
ATOM   36   C C   . ILE A 1 5   ? 12.482 2.530   -12.931 1.00 17.32 ? 6   ILE A C   1 
ATOM   37   O O   . ILE A 1 5   ? 12.671 2.233   -14.121 1.00 16.40 ? 6   ILE A O   1 
ATOM   38   C CB  . ILE A 1 5   ? 10.497 4.084   -13.051 1.00 15.19 ? 6   ILE A CB  1 
ATOM   39   C CG1 . ILE A 1 5   ? 10.021 5.525   -12.828 1.00 18.42 ? 6   ILE A CG1 1 
ATOM   40   C CG2 . ILE A 1 5   ? 9.569  3.099   -12.342 1.00 16.85 ? 6   ILE A CG2 1 
ATOM   41   C CD1 . ILE A 1 5   ? 10.095 5.983   -11.388 1.00 18.88 ? 6   ILE A CD1 1 
ATOM   42   N N   . ILE A 1 6   ? 12.744 1.695   -11.924 1.00 14.98 ? 7   ILE A N   1 
ATOM   43   C CA  . ILE A 1 6   ? 13.445 0.429   -12.119 1.00 16.05 ? 7   ILE A CA  1 
ATOM   44   C C   . ILE A 1 6   ? 12.576 -0.722  -11.632 1.00 17.29 ? 7   ILE A C   1 
ATOM   45   O O   . ILE A 1 6   ? 12.022 -0.666  -10.528 1.00 16.63 ? 7   ILE A O   1 
ATOM   46   C CB  . ILE A 1 6   ? 14.812 0.439   -11.417 1.00 15.61 ? 7   ILE A CB  1 
ATOM   47   C CG1 . ILE A 1 6   ? 15.644 1.607   -11.949 1.00 17.98 ? 7   ILE A CG1 1 
ATOM   48   C CG2 . ILE A 1 6   ? 15.552 -0.890  -11.667 1.00 16.84 ? 7   ILE A CG2 1 
ATOM   49   C CD1 . ILE A 1 6   ? 17.051 1.657   -11.397 1.00 17.71 ? 7   ILE A CD1 1 
ATOM   50   N N   . ALA A 1 7   ? 12.450 -1.759  -12.456 1.00 16.49 ? 8   ALA A N   1 
ATOM   51   C CA  . ALA A 1 7   ? 11.730 -2.963  -12.066 1.00 15.95 ? 8   ALA A CA  1 
ATOM   52   C C   . ALA A 1 7   ? 12.725 -4.033  -11.627 1.00 15.46 ? 8   ALA A C   1 
ATOM   53   O O   . ALA A 1 7   ? 13.738 -4.271  -12.299 1.00 15.59 ? 8   ALA A O   1 
ATOM   54   C CB  . ALA A 1 7   ? 10.856 -3.483  -13.210 1.00 17.42 ? 8   ALA A CB  1 
ATOM   55   N N   . CYS A 1 8   ? 12.442 -4.659  -10.491 1.00 16.28 ? 9   CYS A N   1 
ATOM   56   C CA  . CYS A 1 8   ? 13.258 -5.745  -9.966  1.00 15.75 ? 9   CYS A CA  1 
ATOM   57   C C   . CYS A 1 8   ? 12.561 -7.067  -10.252 1.00 16.01 ? 9   CYS A C   1 
ATOM   58   O O   . CYS A 1 8   ? 11.403 -7.256  -9.867  1.00 16.81 ? 9   CYS A O   1 
ATOM   59   C CB  . CYS A 1 8   ? 13.490 -5.591  -8.466  1.00 15.24 ? 9   CYS A CB  1 
ATOM   60   S SG  . CYS A 1 8   ? 14.587 -6.915  -7.814  1.00 27.91 ? 9   CYS A SG  1 
ATOM   61   N N   . LEU A 1 9   ? 13.268 -7.965  -10.928 1.00 16.05 ? 10  LEU A N   1 
ATOM   62   C CA  . LEU A 1 9   ? 12.777 -9.292  -11.271 1.00 17.37 ? 10  LEU A CA  1 
ATOM   63   C C   . LEU A 1 9   ? 13.565 -10.301 -10.441 1.00 16.44 ? 10  LEU A C   1 
ATOM   64   O O   . LEU A 1 9   ? 14.755 -10.540 -10.697 1.00 15.69 ? 10  LEU A O   1 
ATOM   65   C CB  . LEU A 1 9   ? 12.920 -9.558  -12.773 1.00 19.56 ? 10  LEU A CB  1 
ATOM   66   C CG  . LEU A 1 9   ? 11.774 -9.062  -13.672 1.00 24.68 ? 10  LEU A CG  1 
ATOM   67   C CD1 . LEU A 1 9   ? 11.554 -7.562  -13.541 1.00 28.17 ? 10  LEU A CD1 1 
ATOM   68   C CD2 . LEU A 1 9   ? 12.009 -9.427  -15.135 1.00 24.88 ? 10  LEU A CD2 1 
ATOM   69   N N   . ASP A 1 10  ? 12.907 -10.852 -9.428  1.00 16.62 ? 11  ASP A N   1 
ATOM   70   C CA  . ASP A 1 10  ? 13.467 -11.941 -8.637  1.00 16.00 ? 11  ASP A CA  1 
ATOM   71   C C   . ASP A 1 10  ? 13.364 -13.243 -9.422  1.00 17.21 ? 11  ASP A C   1 
ATOM   72   O O   . ASP A 1 10  ? 12.278 -13.622 -9.873  1.00 18.17 ? 11  ASP A O   1 
ATOM   73   C CB  . ASP A 1 10  ? 12.694 -12.058 -7.324  1.00 19.02 ? 11  ASP A CB  1 
ATOM   74   C CG  . ASP A 1 10  ? 12.742 -10.776 -6.503  1.00 25.05 ? 11  ASP A CG  1 
ATOM   75   O OD1 . ASP A 1 10  ? 13.781 -10.524 -5.862  1.00 23.12 ? 11  ASP A OD1 1 
ATOM   76   O OD2 . ASP A 1 10  ? 11.755 -10.003 -6.509  1.00 22.35 ? 11  ASP A OD2 1 
ATOM   77   N N   . VAL A 1 11  ? 14.500 -13.930 -9.586  1.00 17.06 ? 12  VAL A N   1 
ATOM   78   C CA  . VAL A 1 11  ? 14.568 -15.105 -10.446 1.00 17.47 ? 12  VAL A CA  1 
ATOM   79   C C   . VAL A 1 11  ? 15.212 -16.268 -9.702  1.00 16.43 ? 12  VAL A C   1 
ATOM   80   O O   . VAL A 1 11  ? 16.050 -16.079 -8.816  1.00 17.82 ? 12  VAL A O   1 
ATOM   81   C CB  . VAL A 1 11  ? 15.320 -14.818 -11.774 1.00 19.06 ? 12  VAL A CB  1 
ATOM   82   C CG1 . VAL A 1 11  ? 14.534 -13.799 -12.614 1.00 18.44 ? 12  VAL A CG1 1 
ATOM   83   C CG2 . VAL A 1 11  ? 16.726 -14.313 -11.501 1.00 20.62 ? 12  VAL A CG2 1 
ATOM   84   N N   . LYS A 1 12  ? 14.807 -17.479 -10.082 1.00 17.79 ? 13  LYS A N   1 
ATOM   85   C CA  . LYS A 1 12  ? 15.381 -18.705 -9.545  1.00 18.70 ? 13  LYS A CA  1 
ATOM   86   C C   . LYS A 1 12  ? 15.222 -19.785 -10.600 1.00 18.38 ? 13  LYS A C   1 
ATOM   87   O O   . LYS A 1 12  ? 14.137 -19.951 -11.165 1.00 18.95 ? 13  LYS A O   1 
ATOM   88   C CB  . LYS A 1 12  ? 14.655 -19.118 -8.264  1.00 19.99 ? 13  LYS A CB  1 
ATOM   89   C CG  . LYS A 1 12  ? 15.220 -20.358 -7.589  1.00 21.55 ? 13  LYS A CG  1 
ATOM   90   C CD  . LYS A 1 12  ? 14.445 -20.701 -6.325  1.00 21.23 ? 13  LYS A CD  1 
ATOM   91   C CE  . LYS A 1 12  ? 15.175 -21.775 -5.513  1.00 24.79 ? 13  LYS A CE  1 
ATOM   92   N NZ  . LYS A 1 12  ? 15.091 -23.107 -6.176  1.00 35.47 ? 13  LYS A NZ  1 
ATOM   93   N N   . ASP A 1 13  ? 16.305 -20.513 -10.861 1.00 21.13 ? 14  ASP A N   1 
ATOM   94   C CA  . ASP A 1 13  ? 16.281 -21.601 -11.838 1.00 20.59 ? 14  ASP A CA  1 
ATOM   95   C C   . ASP A 1 13  ? 15.817 -21.109 -13.209 1.00 23.15 ? 14  ASP A C   1 
ATOM   96   O O   . ASP A 1 13  ? 15.115 -21.818 -13.931 1.00 25.64 ? 14  ASP A O   1 
ATOM   97   C CB  . ASP A 1 13  ? 15.417 -22.769 -11.351 1.00 22.50 ? 14  ASP A CB  1 
ATOM   98   C CG  . ASP A 1 13  ? 15.823 -23.265 -9.964  1.00 23.36 ? 14  ASP A CG  1 
ATOM   99   O OD1 . ASP A 1 13  ? 17.031 -23.286 -9.669  1.00 29.10 ? 14  ASP A OD1 1 
ATOM   100  O OD2 . ASP A 1 13  ? 14.932 -23.634 -9.166  1.00 30.83 ? 14  ASP A OD2 1 
ATOM   101  N N   . GLY A 1 14  ? 16.169 -19.875 -13.560 1.00 23.17 ? 15  GLY A N   1 
ATOM   102  C CA  . GLY A 1 14  ? 15.818 -19.348 -14.862 1.00 24.01 ? 15  GLY A CA  1 
ATOM   103  C C   . GLY A 1 14  ? 14.414 -18.813 -14.995 1.00 23.36 ? 15  GLY A C   1 
ATOM   104  O O   . GLY A 1 14  ? 14.004 -18.478 -16.112 1.00 26.99 ? 15  GLY A O   1 
ATOM   105  N N   . ARG A 1 15  ? 13.651 -18.728 -13.907 1.00 19.39 ? 16  ARG A N   1 
ATOM   106  C CA  . ARG A 1 15  ? 12.282 -18.252 -13.993 1.00 22.88 ? 16  ARG A CA  1 
ATOM   107  C C   . ARG A 1 15  ? 12.005 -17.151 -12.978 1.00 20.27 ? 16  ARG A C   1 
ATOM   108  O O   . ARG A 1 15  ? 12.651 -17.054 -11.930 1.00 20.32 ? 16  ARG A O   1 
ATOM   109  C CB  . ARG A 1 15  ? 11.288 -19.399 -13.879 1.00 28.39 ? 16  ARG A CB  1 
ATOM   110  C CG  . ARG A 1 15  ? 11.276 -20.212 -15.166 1.00 36.72 ? 16  ARG A CG  1 
ATOM   111  C CD  . ARG A 1 15  ? 10.175 -21.224 -15.223 1.00 43.09 ? 16  ARG A CD  1 
ATOM   112  N NE  . ARG A 1 15  ? 8.830  -20.660 -15.221 1.00 37.53 ? 16  ARG A NE  1 
ATOM   113  C CZ  . ARG A 1 15  ? 8.252  -20.068 -16.262 1.00 30.33 ? 16  ARG A CZ  1 
ATOM   114  N NH1 . ARG A 1 15  ? 8.907  -19.922 -17.409 1.00 29.52 ? 16  ARG A NH1 1 
ATOM   115  N NH2 . ARG A 1 15  ? 7.009  -19.622 -16.149 1.00 28.22 ? 16  ARG A NH2 1 
ATOM   116  N N   . VAL A 1 16  ? 11.045 -16.297 -13.327 1.00 19.79 ? 17  VAL A N   1 
ATOM   117  C CA  . VAL A 1 16  ? 10.581 -15.281 -12.398 1.00 19.96 ? 17  VAL A CA  1 
ATOM   118  C C   . VAL A 1 16  ? 9.819  -15.979 -11.284 1.00 17.70 ? 17  VAL A C   1 
ATOM   119  O O   . VAL A 1 16  ? 8.996  -16.866 -11.545 1.00 20.86 ? 17  VAL A O   1 
ATOM   120  C CB  . VAL A 1 16  ? 9.706  -14.271 -13.152 1.00 21.13 ? 17  VAL A CB  1 
ATOM   121  C CG1 . VAL A 1 16  ? 9.053  -13.276 -12.188 1.00 22.41 ? 17  VAL A CG1 1 
ATOM   122  C CG2 . VAL A 1 16  ? 10.534 -13.557 -14.212 1.00 25.49 ? 17  VAL A CG2 1 
ATOM   123  N N   . VAL A 1 17  ? 10.081 -15.594 -10.035 1.00 16.19 ? 18  VAL A N   1 
ATOM   124  C CA  . VAL A 1 17  ? 9.425  -16.288 -8.925  1.00 18.33 ? 18  VAL A CA  1 
ATOM   125  C C   . VAL A 1 17  ? 8.110  -15.654 -8.483  1.00 17.64 ? 18  VAL A C   1 
ATOM   126  O O   . VAL A 1 17  ? 7.311  -16.315 -7.799  1.00 19.07 ? 18  VAL A O   1 
ATOM   127  C CB  . VAL A 1 17  ? 10.336 -16.526 -7.710  1.00 23.33 ? 18  VAL A CB  1 
ATOM   128  C CG1 . VAL A 1 17  ? 11.555 -17.322 -8.126  1.00 22.77 ? 18  VAL A CG1 1 
ATOM   129  C CG2 . VAL A 1 17  ? 10.734 -15.209 -7.064  1.00 21.53 ? 18  VAL A CG2 1 
ATOM   130  N N   . LYS A 1 18  ? 7.858  -14.397 -8.850  1.00 18.06 ? 19  LYS A N   1 
ATOM   131  C CA  . LYS A 1 18  ? 6.657  -13.691 -8.432  1.00 17.13 ? 19  LYS A CA  1 
ATOM   132  C C   . LYS A 1 18  ? 5.584  -13.774 -9.507  1.00 15.92 ? 19  LYS A C   1 
ATOM   133  O O   . LYS A 1 18  ? 5.895  -13.831 -10.700 1.00 19.57 ? 19  LYS A O   1 
ATOM   134  C CB  . LYS A 1 18  ? 6.982  -12.216 -8.205  1.00 16.87 ? 19  LYS A CB  1 
ATOM   135  C CG  . LYS A 1 18  ? 8.114  -11.981 -7.257  1.00 23.61 ? 19  LYS A CG  1 
ATOM   136  C CD  . LYS A 1 18  ? 7.652  -12.044 -5.834  1.00 27.95 ? 19  LYS A CD  1 
ATOM   137  C CE  . LYS A 1 18  ? 8.665  -11.383 -4.911  1.00 35.92 ? 19  LYS A CE  1 
ATOM   138  N NZ  . LYS A 1 18  ? 8.321  -11.643 -3.492  1.00 33.91 ? 19  LYS A NZ  1 
ATOM   139  N N   . PRO A 1 19  ? 4.318  -13.763 -9.099  1.00 18.37 ? 20  PRO A N   1 
ATOM   140  C CA  . PRO A 1 19  ? 3.215  -13.709 -10.063 1.00 18.38 ? 20  PRO A CA  1 
ATOM   141  C C   . PRO A 1 19  ? 3.059  -12.303 -10.625 1.00 17.56 ? 20  PRO A C   1 
ATOM   142  O O   . PRO A 1 19  ? 3.562  -11.326 -10.073 1.00 18.28 ? 20  PRO A O   1 
ATOM   143  C CB  . PRO A 1 19  ? 1.995  -14.054 -9.201  1.00 19.03 ? 20  PRO A CB  1 
ATOM   144  C CG  . PRO A 1 19  ? 2.359  -13.592 -7.844  1.00 17.01 ? 20  PRO A CG  1 
ATOM   145  C CD  . PRO A 1 19  ? 3.843  -13.835 -7.709  1.00 18.49 ? 20  PRO A CD  1 
ATOM   146  N N   . THR A 1 20  ? 2.360  -12.214 -11.754 1.00 17.87 ? 21  THR A N   1 
ATOM   147  C CA  . THR A 1 20  ? 1.970  -10.929 -12.324 1.00 15.32 ? 21  THR A CA  1 
ATOM   148  C C   . THR A 1 20  ? 0.505  -10.981 -12.710 1.00 16.57 ? 21  THR A C   1 
ATOM   149  O O   . THR A 1 20  ? -0.104 -12.053 -12.794 1.00 19.64 ? 21  THR A O   1 
ATOM   150  C CB  . THR A 1 20  ? 2.782  -10.518 -13.563 1.00 21.96 ? 21  THR A CB  1 
ATOM   151  O OG1 . THR A 1 20  ? 2.182  -11.076 -14.741 1.00 24.57 ? 21  THR A OG1 1 
ATOM   152  C CG2 . THR A 1 20  ? 4.225  -10.955 -13.460 1.00 22.03 ? 21  THR A CG2 1 
ATOM   153  N N   . ASN A 1 21  ? -0.045 -9.786  -12.953 1.00 18.82 ? 22  ASN A N   1 
ATOM   154  C CA  . ASN A 1 21  ? -1.385 -9.603  -13.498 1.00 19.01 ? 22  ASN A CA  1 
ATOM   155  C C   . ASN A 1 21  ? -1.347 -9.156  -14.956 1.00 24.84 ? 22  ASN A C   1 
ATOM   156  O O   . ASN A 1 21  ? -2.304 -8.540  -15.437 1.00 26.70 ? 22  ASN A O   1 
ATOM   157  C CB  . ASN A 1 21  ? -2.182 -8.594  -12.665 1.00 19.86 ? 22  ASN A CB  1 
ATOM   158  C CG  . ASN A 1 21  ? -2.708 -9.186  -11.376 1.00 19.55 ? 22  ASN A CG  1 
ATOM   159  O OD1 . ASN A 1 21  ? -2.896 -10.405 -11.265 1.00 20.81 ? 22  ASN A OD1 1 
ATOM   160  N ND2 . ASN A 1 21  ? -2.960 -8.331  -10.393 1.00 18.77 ? 22  ASN A ND2 1 
ATOM   161  N N   . PHE A 1 22  ? -0.246 -9.414  -15.656 1.00 21.35 ? 23  PHE A N   1 
ATOM   162  C CA  . PHE A 1 22  ? -0.125 -9.069  -17.072 1.00 25.18 ? 23  PHE A CA  1 
ATOM   163  C C   . PHE A 1 22  ? -0.657 -10.247 -17.879 1.00 33.91 ? 23  PHE A C   1 
ATOM   164  O O   . PHE A 1 22  ? 0.087  -11.141 -18.278 1.00 32.78 ? 23  PHE A O   1 
ATOM   165  C CB  . PHE A 1 22  ? 1.328  -8.772  -17.433 1.00 23.87 ? 23  PHE A CB  1 
ATOM   166  C CG  . PHE A 1 22  ? 1.960  -7.679  -16.617 1.00 26.89 ? 23  PHE A CG  1 
ATOM   167  C CD1 . PHE A 1 22  ? 1.354  -6.444  -16.485 1.00 28.60 ? 23  PHE A CD1 1 
ATOM   168  C CD2 . PHE A 1 22  ? 3.178  -7.894  -15.989 1.00 28.11 ? 23  PHE A CD2 1 
ATOM   169  C CE1 . PHE A 1 22  ? 1.947  -5.444  -15.734 1.00 26.47 ? 23  PHE A CE1 1 
ATOM   170  C CE2 . PHE A 1 22  ? 3.774  -6.900  -15.241 1.00 27.40 ? 23  PHE A CE2 1 
ATOM   171  C CZ  . PHE A 1 22  ? 3.154  -5.673  -15.110 1.00 24.75 ? 23  PHE A CZ  1 
ATOM   172  N N   . GLU A 1 23  ? -1.966 -10.249 -18.132 1.00 44.57 ? 24  GLU A N   1 
ATOM   173  C CA  . GLU A 1 23  ? -2.574 -11.349 -18.872 1.00 46.89 ? 24  GLU A CA  1 
ATOM   174  C C   . GLU A 1 23  ? -2.250 -11.320 -20.360 1.00 46.87 ? 24  GLU A C   1 
ATOM   175  O O   . GLU A 1 23  ? -2.570 -12.284 -21.064 1.00 46.18 ? 24  GLU A O   1 
ATOM   176  C CB  . GLU A 1 23  ? -4.091 -11.365 -18.664 1.00 48.82 ? 24  GLU A CB  1 
ATOM   177  N N   . ASN A 1 24  ? -1.624 -10.251 -20.851 1.00 40.23 ? 25  ASN A N   1 
ATOM   178  C CA  . ASN A 1 24  ? -1.250 -10.149 -22.255 1.00 47.75 ? 25  ASN A CA  1 
ATOM   179  C C   . ASN A 1 24  ? 0.040  -10.889 -22.590 1.00 45.87 ? 25  ASN A C   1 
ATOM   180  O O   . ASN A 1 24  ? 0.439  -10.908 -23.760 1.00 45.84 ? 25  ASN A O   1 
ATOM   181  C CB  . ASN A 1 24  ? -1.128 -8.678  -22.666 1.00 46.32 ? 25  ASN A CB  1 
ATOM   182  C CG  . ASN A 1 24  ? -0.091 -7.929  -21.853 1.00 45.65 ? 25  ASN A CG  1 
ATOM   183  O OD1 . ASN A 1 24  ? -0.378 -7.433  -20.764 1.00 48.52 ? 25  ASN A OD1 1 
ATOM   184  N ND2 . ASN A 1 24  ? 1.122  -7.837  -22.386 1.00 52.29 ? 25  ASN A ND2 1 
ATOM   185  N N   . LEU A 1 25  ? 0.697  -11.493 -21.606 1.00 42.09 ? 26  LEU A N   1 
ATOM   186  C CA  . LEU A 1 25  ? 1.949  -12.197 -21.826 1.00 32.14 ? 26  LEU A CA  1 
ATOM   187  C C   . LEU A 1 25  ? 1.698  -13.692 -21.942 1.00 36.22 ? 26  LEU A C   1 
ATOM   188  O O   . LEU A 1 25  ? 0.837  -14.246 -21.251 1.00 39.89 ? 26  LEU A O   1 
ATOM   189  C CB  . LEU A 1 25  ? 2.932  -11.930 -20.682 1.00 36.17 ? 26  LEU A CB  1 
ATOM   190  C CG  . LEU A 1 25  ? 3.391  -10.478 -20.529 1.00 38.69 ? 26  LEU A CG  1 
ATOM   191  C CD1 . LEU A 1 25  ? 4.520  -10.364 -19.513 1.00 32.71 ? 26  LEU A CD1 1 
ATOM   192  C CD2 . LEU A 1 25  ? 3.819  -9.910  -21.872 1.00 35.02 ? 26  LEU A CD2 1 
ATOM   193  N N   . ARG A 1 26  ? 2.459  -14.340 -22.825 1.00 30.06 ? 27  ARG A N   1 
ATOM   194  C CA  . ARG A 1 26  ? 2.371  -15.789 -22.966 1.00 35.57 ? 27  ARG A CA  1 
ATOM   195  C C   . ARG A 1 26  ? 2.818  -16.489 -21.690 1.00 40.40 ? 27  ARG A C   1 
ATOM   196  O O   . ARG A 1 26  ? 2.093  -17.328 -21.141 1.00 40.90 ? 27  ARG A O   1 
ATOM   197  C CB  . ARG A 1 26  ? 3.232  -16.252 -24.142 1.00 32.30 ? 27  ARG A CB  1 
ATOM   198  C CG  . ARG A 1 26  ? 2.928  -17.672 -24.586 1.00 43.80 ? 27  ARG A CG  1 
ATOM   199  C CD  . ARG A 1 26  ? 3.996  -18.215 -25.515 1.00 44.63 ? 27  ARG A CD  1 
ATOM   200  N NE  . ARG A 1 26  ? 4.412  -19.558 -25.120 1.00 56.89 ? 27  ARG A NE  1 
ATOM   201  C CZ  . ARG A 1 26  ? 5.418  -19.823 -24.293 1.00 49.24 ? 27  ARG A CZ  1 
ATOM   202  N NH1 . ARG A 1 26  ? 5.713  -21.081 -23.993 1.00 51.53 ? 27  ARG A NH1 1 
ATOM   203  N NH2 . ARG A 1 26  ? 6.136  -18.834 -23.774 1.00 44.73 ? 27  ARG A NH2 1 
ATOM   204  N N   . ASP A 1 27  ? 4.015  -16.158 -21.206 1.00 38.94 ? 28  ASP A N   1 
ATOM   205  C CA  . ASP A 1 27  ? 4.615  -16.807 -20.041 1.00 36.38 ? 28  ASP A CA  1 
ATOM   206  C C   . ASP A 1 27  ? 5.170  -15.712 -19.137 1.00 35.74 ? 28  ASP A C   1 
ATOM   207  O O   . ASP A 1 27  ? 6.295  -15.247 -19.343 1.00 33.52 ? 28  ASP A O   1 
ATOM   208  C CB  . ASP A 1 27  ? 5.713  -17.776 -20.467 1.00 35.44 ? 28  ASP A CB  1 
ATOM   209  C CG  . ASP A 1 27  ? 6.290  -18.557 -19.299 1.00 38.23 ? 28  ASP A CG  1 
ATOM   210  O OD1 . ASP A 1 27  ? 5.865  -18.325 -18.145 1.00 38.16 ? 28  ASP A OD1 1 
ATOM   211  O OD2 . ASP A 1 27  ? 7.172  -19.405 -19.536 1.00 34.37 ? 28  ASP A OD2 1 
ATOM   212  N N   . SER A 1 28  ? 4.379  -15.328 -18.129 1.00 36.57 ? 29  SER A N   1 
ATOM   213  C CA  . SER A 1 28  ? 4.785  -14.308 -17.170 1.00 40.69 ? 29  SER A CA  1 
ATOM   214  C C   . SER A 1 28  ? 6.012  -14.715 -16.369 1.00 30.75 ? 29  SER A C   1 
ATOM   215  O O   . SER A 1 28  ? 6.677  -13.842 -15.801 1.00 33.29 ? 29  SER A O   1 
ATOM   216  C CB  . SER A 1 28  ? 3.642  -14.016 -16.197 1.00 39.91 ? 29  SER A CB  1 
ATOM   217  O OG  . SER A 1 28  ? 2.875  -12.910 -16.627 1.00 48.78 ? 29  SER A OG  1 
ATOM   218  N N   . GLY A 1 29  ? 6.321  -16.013 -16.302 1.00 29.34 ? 30  GLY A N   1 
ATOM   219  C CA  . GLY A 1 29  ? 7.474  -16.494 -15.569 1.00 29.25 ? 30  GLY A CA  1 
ATOM   220  C C   . GLY A 1 29  ? 8.771  -16.521 -16.343 1.00 24.27 ? 30  GLY A C   1 
ATOM   221  O O   . GLY A 1 29  ? 9.828  -16.808 -15.771 1.00 24.70 ? 30  GLY A O   1 
ATOM   222  N N   . ASP A 1 30  ? 8.725  -16.240 -17.642 1.00 24.49 ? 31  ASP A N   1 
ATOM   223  C CA  . ASP A 1 30  ? 9.929  -16.152 -18.453 1.00 23.03 ? 31  ASP A CA  1 
ATOM   224  C C   . ASP A 1 30  ? 10.548 -14.781 -18.208 1.00 21.65 ? 31  ASP A C   1 
ATOM   225  O O   . ASP A 1 30  ? 9.952  -13.761 -18.570 1.00 21.98 ? 31  ASP A O   1 
ATOM   226  C CB  . ASP A 1 30  ? 9.570  -16.348 -19.931 1.00 22.88 ? 31  ASP A CB  1 
ATOM   227  C CG  . ASP A 1 30  ? 10.764 -16.176 -20.876 1.00 29.75 ? 31  ASP A CG  1 
ATOM   228  O OD1 . ASP A 1 30  ? 11.877 -15.839 -20.430 1.00 28.30 ? 31  ASP A OD1 1 
ATOM   229  O OD2 . ASP A 1 30  ? 10.583 -16.401 -22.091 1.00 36.63 ? 31  ASP A OD2 1 
ATOM   230  N N   . PRO A 1 31  ? 11.731 -14.714 -17.601 1.00 19.76 ? 32  PRO A N   1 
ATOM   231  C CA  . PRO A 1 31  ? 12.316 -13.396 -17.293 1.00 21.35 ? 32  PRO A CA  1 
ATOM   232  C C   . PRO A 1 31  ? 12.637 -12.574 -18.518 1.00 21.27 ? 32  PRO A C   1 
ATOM   233  O O   . PRO A 1 31  ? 12.656 -11.340 -18.435 1.00 19.86 ? 32  PRO A O   1 
ATOM   234  C CB  . PRO A 1 31  ? 13.575 -13.738 -16.482 1.00 22.64 ? 32  PRO A CB  1 
ATOM   235  C CG  . PRO A 1 31  ? 13.879 -15.158 -16.848 1.00 26.93 ? 32  PRO A CG  1 
ATOM   236  C CD  . PRO A 1 31  ? 12.576 -15.829 -17.141 1.00 21.90 ? 32  PRO A CD  1 
ATOM   237  N N   . VAL A 1 32  ? 12.896 -13.219 -19.653 1.00 20.65 ? 33  VAL A N   1 
ATOM   238  C CA  . VAL A 1 32  ? 13.150 -12.481 -20.885 1.00 21.59 ? 33  VAL A CA  1 
ATOM   239  C C   . VAL A 1 32  ? 11.863 -11.847 -21.392 1.00 22.28 ? 33  VAL A C   1 
ATOM   240  O O   . VAL A 1 32  ? 11.829 -10.657 -21.718 1.00 20.82 ? 33  VAL A O   1 
ATOM   241  C CB  . VAL A 1 32  ? 13.780 -13.401 -21.944 1.00 24.70 ? 33  VAL A CB  1 
ATOM   242  C CG1 . VAL A 1 32  ? 13.991 -12.640 -23.244 1.00 29.40 ? 33  VAL A CG1 1 
ATOM   243  C CG2 . VAL A 1 32  ? 15.092 -13.966 -21.428 1.00 29.99 ? 33  VAL A CG2 1 
ATOM   244  N N   . GLU A 1 33  ? 10.786 -12.630 -21.459 1.00 22.21 ? 34  GLU A N   1 
ATOM   245  C CA  . GLU A 1 33  ? 9.519  -12.074 -21.920 1.00 20.81 ? 34  GLU A CA  1 
ATOM   246  C C   . GLU A 1 33  ? 9.037  -10.973 -20.985 1.00 21.39 ? 34  GLU A C   1 
ATOM   247  O O   . GLU A 1 33  ? 8.533  -9.937  -21.439 1.00 21.33 ? 34  GLU A O   1 
ATOM   248  C CB  . GLU A 1 33  ? 8.457  -13.160 -22.058 1.00 22.17 ? 34  GLU A CB  1 
ATOM   249  C CG  . GLU A 1 33  ? 7.155  -12.607 -22.641 1.00 26.73 ? 34  GLU A CG  1 
ATOM   250  C CD  . GLU A 1 33  ? 6.073  -13.657 -22.825 1.00 36.65 ? 34  GLU A CD  1 
ATOM   251  O OE1 . GLU A 1 33  ? 4.959  -13.290 -23.261 1.00 39.62 ? 34  GLU A OE1 1 
ATOM   252  O OE2 . GLU A 1 33  ? 6.334  -14.839 -22.533 1.00 38.90 ? 34  GLU A OE2 1 
ATOM   253  N N   . LEU A 1 34  ? 9.200  -11.164 -19.674 1.00 18.65 ? 35  LEU A N   1 
ATOM   254  C CA  . LEU A 1 34  ? 8.726  -10.154 -18.734 1.00 19.99 ? 35  LEU A CA  1 
ATOM   255  C C   . LEU A 1 34  ? 9.612  -8.919  -18.764 1.00 18.19 ? 35  LEU A C   1 
ATOM   256  O O   . LEU A 1 34  ? 9.125  -7.786  -18.679 1.00 17.80 ? 35  LEU A O   1 
ATOM   257  C CB  . LEU A 1 34  ? 8.649  -10.735 -17.323 1.00 18.90 ? 35  LEU A CB  1 
ATOM   258  C CG  . LEU A 1 34  ? 8.124  -9.776  -16.248 1.00 17.58 ? 35  LEU A CG  1 
ATOM   259  C CD1 . LEU A 1 34  ? 6.718  -9.276  -16.583 1.00 18.79 ? 35  LEU A CD1 1 
ATOM   260  C CD2 . LEU A 1 34  ? 8.143  -10.452 -14.893 1.00 19.37 ? 35  LEU A CD2 1 
ATOM   261  N N   . GLY A 1 35  ? 10.921 -9.109  -18.892 1.00 18.19 ? 36  GLY A N   1 
ATOM   262  C CA  . GLY A 1 35  ? 11.797 -7.958  -18.966 1.00 18.88 ? 36  GLY A CA  1 
ATOM   263  C C   . GLY A 1 35  ? 11.591 -7.158  -20.236 1.00 18.78 ? 36  GLY A C   1 
ATOM   264  O O   . GLY A 1 35  ? 11.614 -5.927  -20.212 1.00 17.40 ? 36  GLY A O   1 
ATOM   265  N N   . LYS A 1 36  ? 11.396 -7.847  -21.362 1.00 17.97 ? 37  LYS A N   1 
ATOM   266  C CA  . LYS A 1 36  ? 11.099 -7.152  -22.608 1.00 18.98 ? 37  LYS A CA  1 
ATOM   267  C C   . LYS A 1 36  ? 9.802  -6.367  -22.481 1.00 19.03 ? 37  LYS A C   1 
ATOM   268  O O   . LYS A 1 36  ? 9.718  -5.213  -22.916 1.00 19.12 ? 37  LYS A O   1 
ATOM   269  C CB  . LYS A 1 36  ? 11.021 -8.162  -23.755 1.00 22.39 ? 37  LYS A CB  1 
ATOM   270  C CG  . LYS A 1 36  ? 10.885 -7.530  -25.134 1.00 27.36 ? 37  LYS A CG  1 
ATOM   271  N N   . PHE A 1 37  ? 8.796  -6.966  -21.845 1.00 17.34 ? 38  PHE A N   1 
ATOM   272  C CA  . PHE A 1 37  ? 7.528  -6.285  -21.623 1.00 18.22 ? 38  PHE A CA  1 
ATOM   273  C C   . PHE A 1 37  ? 7.728  -5.007  -20.819 1.00 17.87 ? 38  PHE A C   1 
ATOM   274  O O   . PHE A 1 37  ? 7.240  -3.940  -21.201 1.00 17.74 ? 38  PHE A O   1 
ATOM   275  C CB  . PHE A 1 37  ? 6.560  -7.236  -20.920 1.00 19.74 ? 38  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 37  ? 5.265  -6.598  -20.517 1.00 21.58 ? 38  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 37  ? 4.279  -6.343  -21.456 1.00 23.86 ? 38  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 37  ? 5.046  -6.233  -19.203 1.00 22.31 ? 38  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 37  ? 3.083  -5.747  -21.077 1.00 29.17 ? 38  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 37  ? 3.860  -5.642  -18.820 1.00 25.73 ? 38  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 37  ? 2.880  -5.396  -19.763 1.00 25.08 ? 38  PHE A CZ  1 
ATOM   282  N N   . TYR A 1 38  ? 8.450  -5.093  -19.698 1.00 17.99 ? 39  TYR A N   1 
ATOM   283  C CA  . TYR A 1 38  ? 8.684  -3.904  -18.887 1.00 17.73 ? 39  TYR A CA  1 
ATOM   284  C C   . TYR A 1 38  ? 9.415  -2.841  -19.689 1.00 19.81 ? 39  TYR A C   1 
ATOM   285  O O   . TYR A 1 38  ? 9.096  -1.650  -19.592 1.00 17.64 ? 39  TYR A O   1 
ATOM   286  C CB  . TYR A 1 38  ? 9.468  -4.269  -17.623 1.00 16.34 ? 39  TYR A CB  1 
ATOM   287  C CG  . TYR A 1 38  ? 8.583  -4.659  -16.460 1.00 17.94 ? 39  TYR A CG  1 
ATOM   288  C CD1 . TYR A 1 38  ? 7.530  -3.843  -16.068 1.00 19.39 ? 39  TYR A CD1 1 
ATOM   289  C CD2 . TYR A 1 38  ? 8.788  -5.844  -15.757 1.00 16.40 ? 39  TYR A CD2 1 
ATOM   290  C CE1 . TYR A 1 38  ? 6.716  -4.184  -15.014 1.00 20.89 ? 39  TYR A CE1 1 
ATOM   291  C CE2 . TYR A 1 38  ? 7.982  -6.189  -14.690 1.00 17.03 ? 39  TYR A CE2 1 
ATOM   292  C CZ  . TYR A 1 38  ? 6.935  -5.371  -14.335 1.00 19.71 ? 39  TYR A CZ  1 
ATOM   293  O OH  . TYR A 1 38  ? 6.130  -5.709  -13.276 1.00 18.28 ? 39  TYR A OH  1 
ATOM   294  N N   . SER A 1 39  ? 10.386 -3.256  -20.509 1.00 16.80 ? 40  SER A N   1 
ATOM   295  C CA  . SER A 1 39  ? 11.124 -2.295  -21.324 1.00 21.11 ? 40  SER A CA  1 
ATOM   296  C C   . SER A 1 39  ? 10.223 -1.606  -22.341 1.00 22.75 ? 40  SER A C   1 
ATOM   297  O O   . SER A 1 39  ? 10.528 -0.491  -22.781 1.00 27.31 ? 40  SER A O   1 
ATOM   298  C CB  . SER A 1 39  ? 12.285 -2.988  -22.033 1.00 23.80 ? 40  SER A CB  1 
ATOM   299  O OG  . SER A 1 39  ? 11.833 -3.748  -23.139 1.00 29.01 ? 40  SER A OG  1 
ATOM   300  N N   . GLU A 1 40  ? 9.117  -2.242  -22.723 1.00 19.78 ? 41  GLU A N   1 
ATOM   301  C CA  . GLU A 1 40  ? 8.185  -1.689  -23.700 1.00 21.67 ? 41  GLU A CA  1 
ATOM   302  C C   . GLU A 1 40  ? 7.080  -0.846  -23.078 1.00 24.36 ? 41  GLU A C   1 
ATOM   303  O O   . GLU A 1 40  ? 6.362  -0.157  -23.817 1.00 24.33 ? 41  GLU A O   1 
ATOM   304  C CB  . GLU A 1 40  ? 7.577  -2.820  -24.543 1.00 23.48 ? 41  GLU A CB  1 
ATOM   305  C CG  . GLU A 1 40  ? 8.582  -3.472  -25.477 1.00 25.13 ? 41  GLU A CG  1 
ATOM   306  C CD  . GLU A 1 40  ? 8.058  -4.723  -26.169 1.00 24.88 ? 41  GLU A CD  1 
ATOM   307  O OE1 . GLU A 1 40  ? 6.951  -5.190  -25.830 1.00 33.44 ? 41  GLU A OE1 1 
ATOM   308  O OE2 . GLU A 1 40  ? 8.781  -5.254  -27.041 1.00 31.96 ? 41  GLU A OE2 1 
ATOM   309  N N   . ILE A 1 41  ? 6.921  -0.871  -21.753 1.00 21.62 ? 42  ILE A N   1 
ATOM   310  C CA  . ILE A 1 41  ? 5.881  -0.101  -21.081 1.00 21.87 ? 42  ILE A CA  1 
ATOM   311  C C   . ILE A 1 41  ? 6.449  1.048   -20.257 1.00 19.76 ? 42  ILE A C   1 
ATOM   312  O O   . ILE A 1 41  ? 5.728  1.637   -19.445 1.00 24.71 ? 42  ILE A O   1 
ATOM   313  C CB  . ILE A 1 41  ? 4.934  -0.980  -20.250 1.00 21.56 ? 42  ILE A CB  1 
ATOM   314  C CG1 . ILE A 1 41  ? 5.680  -1.579  -19.053 1.00 22.61 ? 42  ILE A CG1 1 
ATOM   315  C CG2 . ILE A 1 41  ? 4.315  -2.056  -21.117 1.00 24.31 ? 42  ILE A CG2 1 
ATOM   316  C CD1 . ILE A 1 41  ? 4.747  -2.187  -18.012 1.00 23.99 ? 42  ILE A CD1 1 
ATOM   317  N N   . GLY A 1 42  ? 7.726  1.372   -20.423 1.00 21.75 ? 43  GLY A N   1 
ATOM   318  C CA  . GLY A 1 42  ? 8.275  2.589   -19.852 1.00 23.98 ? 43  GLY A CA  1 
ATOM   319  C C   . GLY A 1 42  ? 9.226  2.411   -18.689 1.00 19.43 ? 43  GLY A C   1 
ATOM   320  O O   . GLY A 1 42  ? 9.664  3.413   -18.120 1.00 20.37 ? 43  GLY A O   1 
ATOM   321  N N   . ILE A 1 43  ? 9.563  1.182   -18.309 1.00 17.61 ? 44  ILE A N   1 
ATOM   322  C CA  . ILE A 1 43  ? 10.578 0.982   -17.283 1.00 16.95 ? 44  ILE A CA  1 
ATOM   323  C C   . ILE A 1 43  ? 11.939 1.396   -17.835 1.00 18.39 ? 44  ILE A C   1 
ATOM   324  O O   . ILE A 1 43  ? 12.257 1.153   -19.008 1.00 20.55 ? 44  ILE A O   1 
ATOM   325  C CB  . ILE A 1 43  ? 10.542 -0.482  -16.812 1.00 14.57 ? 44  ILE A CB  1 
ATOM   326  C CG1 . ILE A 1 43  ? 9.344  -0.715  -15.888 1.00 19.42 ? 44  ILE A CG1 1 
ATOM   327  C CG2 . ILE A 1 43  ? 11.822 -0.857  -16.103 1.00 18.90 ? 44  ILE A CG2 1 
ATOM   328  C CD1 . ILE A 1 43  ? 9.493  -0.078  -14.523 1.00 18.70 ? 44  ILE A CD1 1 
ATOM   329  N N   . ASP A 1 44  ? 12.740 2.064   -17.008 1.00 16.73 ? 45  ASP A N   1 
ATOM   330  C CA  . ASP A 1 44  ? 13.994 2.615   -17.504 1.00 17.60 ? 45  ASP A CA  1 
ATOM   331  C C   . ASP A 1 44  ? 15.152 1.631   -17.421 1.00 17.15 ? 45  ASP A C   1 
ATOM   332  O O   . ASP A 1 44  ? 16.060 1.668   -18.265 1.00 21.18 ? 45  ASP A O   1 
ATOM   333  C CB  . ASP A 1 44  ? 14.338 3.886   -16.736 1.00 17.61 ? 45  ASP A CB  1 
ATOM   334  C CG  . ASP A 1 44  ? 13.280 4.953   -16.902 1.00 21.88 ? 45  ASP A CG  1 
ATOM   335  O OD1 . ASP A 1 44  ? 12.925 5.261   -18.061 1.00 23.29 ? 45  ASP A OD1 1 
ATOM   336  O OD2 . ASP A 1 44  ? 12.790 5.477   -15.881 1.00 19.91 ? 45  ASP A OD2 1 
ATOM   337  N N   . GLU A 1 45  ? 15.162 0.788   -16.390 1.00 17.90 ? 46  GLU A N   1 
ATOM   338  C CA  . GLU A 1 45  ? 16.197 -0.220  -16.215 1.00 18.07 ? 46  GLU A CA  1 
ATOM   339  C C   . GLU A 1 45  ? 15.583 -1.394  -15.477 1.00 16.81 ? 46  GLU A C   1 
ATOM   340  O O   . GLU A 1 45  ? 14.554 -1.271  -14.807 1.00 17.05 ? 46  GLU A O   1 
ATOM   341  C CB  . GLU A 1 45  ? 17.378 0.284   -15.381 1.00 22.70 ? 46  GLU A CB  1 
ATOM   342  C CG  . GLU A 1 45  ? 18.165 1.398   -16.013 1.00 22.21 ? 46  GLU A CG  1 
ATOM   343  C CD  . GLU A 1 45  ? 19.360 1.806   -15.179 1.00 25.49 ? 46  GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 45  ? 19.796 1.009   -14.320 1.00 26.30 ? 46  GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 45  ? 19.860 2.930   -15.384 1.00 29.17 ? 46  GLU A OE2 1 
ATOM   346  N N   . LEU A 1 46  ? 16.246 -2.535  -15.592 1.00 16.54 ? 47  LEU A N   1 
ATOM   347  C CA  . LEU A 1 46  ? 15.861 -3.757  -14.911 1.00 18.14 ? 47  LEU A CA  1 
ATOM   348  C C   . LEU A 1 46  ? 16.966 -4.176  -13.953 1.00 16.70 ? 47  LEU A C   1 
ATOM   349  O O   . LEU A 1 46  ? 18.144 -3.936  -14.203 1.00 17.59 ? 47  LEU A O   1 
ATOM   350  C CB  . LEU A 1 46  ? 15.682 -4.887  -15.926 1.00 18.95 ? 47  LEU A CB  1 
ATOM   351  C CG  . LEU A 1 46  ? 14.583 -4.661  -16.960 1.00 18.19 ? 47  LEU A CG  1 
ATOM   352  C CD1 . LEU A 1 46  ? 14.582 -5.794  -17.973 1.00 23.49 ? 47  LEU A CD1 1 
ATOM   353  C CD2 . LEU A 1 46  ? 13.222 -4.580  -16.285 1.00 20.73 ? 47  LEU A CD2 1 
ATOM   354  N N   . VAL A 1 47  ? 16.571 -4.810  -12.852 1.00 16.65 ? 48  VAL A N   1 
ATOM   355  C CA  . VAL A 1 47  ? 17.498 -5.493  -11.960 1.00 16.86 ? 48  VAL A CA  1 
ATOM   356  C C   . VAL A 1 47  ? 17.009 -6.922  -11.818 1.00 17.68 ? 48  VAL A C   1 
ATOM   357  O O   . VAL A 1 47  ? 15.834 -7.142  -11.509 1.00 18.23 ? 48  VAL A O   1 
ATOM   358  C CB  . VAL A 1 47  ? 17.540 -4.808  -10.581 1.00 18.38 ? 48  VAL A CB  1 
ATOM   359  C CG1 . VAL A 1 47  ? 18.368 -5.620  -9.600  1.00 20.06 ? 48  VAL A CG1 1 
ATOM   360  C CG2 . VAL A 1 47  ? 18.073 -3.385  -10.690 1.00 17.73 ? 48  VAL A CG2 1 
ATOM   361  N N   . PHE A 1 48  ? 17.890 -7.890  -12.062 1.00 16.30 ? 49  PHE A N   1 
ATOM   362  C CA  . PHE A 1 48  ? 17.571 -9.302  -11.873 1.00 19.46 ? 49  PHE A CA  1 
ATOM   363  C C   . PHE A 1 48  ? 18.327 -9.776  -10.642 1.00 21.09 ? 49  PHE A C   1 
ATOM   364  O O   . PHE A 1 48  ? 19.553 -9.661  -10.592 1.00 20.46 ? 49  PHE A O   1 
ATOM   365  C CB  . PHE A 1 48  ? 18.000 -10.129 -13.086 1.00 19.13 ? 49  PHE A CB  1 
ATOM   366  C CG  . PHE A 1 48  ? 17.236 -9.820  -14.345 1.00 17.13 ? 49  PHE A CG  1 
ATOM   367  C CD1 . PHE A 1 48  ? 17.669 -8.820  -15.206 1.00 18.02 ? 49  PHE A CD1 1 
ATOM   368  C CD2 . PHE A 1 48  ? 16.099 -10.538 -14.678 1.00 17.12 ? 49  PHE A CD2 1 
ATOM   369  C CE1 . PHE A 1 48  ? 16.972 -8.539  -16.374 1.00 21.07 ? 49  PHE A CE1 1 
ATOM   370  C CE2 . PHE A 1 48  ? 15.395 -10.263 -15.846 1.00 19.63 ? 49  PHE A CE2 1 
ATOM   371  C CZ  . PHE A 1 48  ? 15.825 -9.258  -16.691 1.00 21.83 ? 49  PHE A CZ  1 
ATOM   372  N N   A LEU A 1 49  ? 17.603 -10.287 -9.650  0.58 18.20 ? 50  LEU A N   1 
ATOM   373  N N   B LEU A 1 49  ? 17.598 -10.288 -9.654  0.42 18.21 ? 50  LEU A N   1 
ATOM   374  C CA  A LEU A 1 49  ? 18.201 -10.795 -8.418  0.58 17.77 ? 50  LEU A CA  1 
ATOM   375  C CA  B LEU A 1 49  ? 18.178 -10.798 -8.415  0.42 17.78 ? 50  LEU A CA  1 
ATOM   376  C C   A LEU A 1 49  ? 17.941 -12.291 -8.357  0.58 15.75 ? 50  LEU A C   1 
ATOM   377  C C   B LEU A 1 49  ? 17.933 -12.299 -8.381  0.42 15.79 ? 50  LEU A C   1 
ATOM   378  O O   A LEU A 1 49  ? 16.790 -12.721 -8.219  0.58 17.66 ? 50  LEU A O   1 
ATOM   379  O O   B LEU A 1 49  ? 16.783 -12.741 -8.288  0.42 17.69 ? 50  LEU A O   1 
ATOM   380  C CB  A LEU A 1 49  ? 17.626 -10.094 -7.190  0.58 19.14 ? 50  LEU A CB  1 
ATOM   381  C CB  B LEU A 1 49  ? 17.547 -10.120 -7.202  0.42 19.15 ? 50  LEU A CB  1 
ATOM   382  C CG  A LEU A 1 49  ? 17.976 -8.611  -7.075  0.58 21.33 ? 50  LEU A CG  1 
ATOM   383  C CG  B LEU A 1 49  ? 18.341 -10.171 -5.896  0.42 22.46 ? 50  LEU A CG  1 
ATOM   384  C CD1 A LEU A 1 49  ? 17.511 -8.036  -5.743  0.58 24.94 ? 50  LEU A CD1 1 
ATOM   385  C CD1 B LEU A 1 49  ? 19.812 -9.908  -6.154  0.42 20.78 ? 50  LEU A CD1 1 
ATOM   386  C CD2 A LEU A 1 49  ? 19.466 -8.387  -7.263  0.58 20.20 ? 50  LEU A CD2 1 
ATOM   387  C CD2 B LEU A 1 49  ? 17.789 -9.164  -4.898  0.42 25.50 ? 50  LEU A CD2 1 
ATOM   388  N N   . ASP A 1 50  ? 19.011 -13.078 -8.447  1.00 18.13 ? 51  ASP A N   1 
ATOM   389  C CA  . ASP A 1 50  ? 18.914 -14.525 -8.553  1.00 19.44 ? 51  ASP A CA  1 
ATOM   390  C C   . ASP A 1 50  ? 19.094 -15.194 -7.197  1.00 18.02 ? 51  ASP A C   1 
ATOM   391  O O   . ASP A 1 50  ? 19.998 -14.843 -6.429  1.00 19.51 ? 51  ASP A O   1 
ATOM   392  C CB  . ASP A 1 50  ? 19.955 -15.045 -9.543  1.00 19.18 ? 51  ASP A CB  1 
ATOM   393  C CG  . ASP A 1 50  ? 19.962 -16.546 -9.635  1.00 21.90 ? 51  ASP A CG  1 
ATOM   394  O OD1 . ASP A 1 50  ? 20.729 -17.162 -8.858  1.00 20.72 ? 51  ASP A OD1 1 
ATOM   395  O OD2 . ASP A 1 50  ? 19.200 -17.109 -10.455 1.00 20.73 ? 51  ASP A OD2 1 
ATOM   396  N N   . ILE A 1 51  ? 18.240 -16.181 -6.923  1.00 18.93 ? 52  ILE A N   1 
ATOM   397  C CA  . ILE A 1 51  ? 18.343 -16.978 -5.703  1.00 18.54 ? 52  ILE A CA  1 
ATOM   398  C C   . ILE A 1 51  ? 18.455 -18.469 -6.020  1.00 18.20 ? 52  ILE A C   1 
ATOM   399  O O   . ILE A 1 51  ? 18.005 -19.312 -5.235  1.00 21.08 ? 52  ILE A O   1 
ATOM   400  C CB  . ILE A 1 51  ? 17.170 -16.693 -4.747  1.00 19.35 ? 52  ILE A CB  1 
ATOM   401  C CG1 . ILE A 1 51  ? 15.843 -16.883 -5.481  1.00 18.76 ? 52  ILE A CG1 1 
ATOM   402  C CG2 . ILE A 1 51  ? 17.273 -15.270 -4.184  1.00 20.69 ? 52  ILE A CG2 1 
ATOM   403  C CD1 . ILE A 1 51  ? 14.631 -17.012 -4.563  1.00 21.75 ? 52  ILE A CD1 1 
ATOM   404  N N   . THR A 1 52  ? 19.040 -18.804 -7.168  1.00 19.82 ? 53  THR A N   1 
ATOM   405  C CA  . THR A 1 52  ? 19.297 -20.202 -7.512  1.00 17.89 ? 53  THR A CA  1 
ATOM   406  C C   . THR A 1 52  ? 20.314 -20.810 -6.546  1.00 22.04 ? 53  THR A C   1 
ATOM   407  O O   . THR A 1 52  ? 21.225 -20.136 -6.065  1.00 22.46 ? 53  THR A O   1 
ATOM   408  C CB  . THR A 1 52  ? 19.835 -20.264 -8.945  1.00 19.89 ? 53  THR A CB  1 
ATOM   409  O OG1 . THR A 1 52  ? 18.838 -19.762 -9.848  1.00 21.24 ? 53  THR A OG1 1 
ATOM   410  C CG2 . THR A 1 52  ? 20.198 -21.687 -9.363  1.00 21.17 ? 53  THR A CG2 1 
ATOM   411  N N   . ALA A 1 53  ? 20.147 -22.104 -6.260  1.00 22.27 ? 54  ALA A N   1 
ATOM   412  C CA  . ALA A 1 53  ? 21.125 -22.822 -5.447  1.00 25.56 ? 54  ALA A CA  1 
ATOM   413  C C   . ALA A 1 53  ? 22.524 -22.699 -6.044  1.00 23.03 ? 54  ALA A C   1 
ATOM   414  O O   . ALA A 1 53  ? 22.699 -22.693 -7.266  1.00 23.27 ? 54  ALA A O   1 
ATOM   415  C CB  . ALA A 1 53  ? 20.730 -24.297 -5.350  1.00 28.79 ? 54  ALA A CB  1 
ATOM   416  N N   . SER A 1 54  ? 23.530 -22.609 -5.162  1.00 24.67 ? 55  SER A N   1 
ATOM   417  C CA  . SER A 1 54  ? 24.895 -22.303 -5.584  1.00 28.41 ? 55  SER A CA  1 
ATOM   418  C C   . SER A 1 54  ? 25.418 -23.282 -6.629  1.00 24.76 ? 55  SER A C   1 
ATOM   419  O O   . SER A 1 54  ? 26.220 -22.895 -7.491  1.00 28.53 ? 55  SER A O   1 
ATOM   420  C CB  . SER A 1 54  ? 25.829 -22.291 -4.370  1.00 31.00 ? 55  SER A CB  1 
ATOM   421  O OG  . SER A 1 54  ? 25.478 -21.257 -3.467  1.00 33.42 ? 55  SER A OG  1 
ATOM   422  N N   . VAL A 1 55  ? 24.986 -24.546 -6.565  1.00 28.97 ? 56  VAL A N   1 
ATOM   423  C CA  . VAL A 1 55  ? 25.515 -25.572 -7.464  1.00 31.80 ? 56  VAL A CA  1 
ATOM   424  C C   . VAL A 1 55  ? 25.240 -25.226 -8.922  1.00 30.66 ? 56  VAL A C   1 
ATOM   425  O O   . VAL A 1 55  ? 26.062 -25.501 -9.804  1.00 28.79 ? 56  VAL A O   1 
ATOM   426  C CB  . VAL A 1 55  ? 24.958 -26.957 -7.082  1.00 35.42 ? 56  VAL A CB  1 
ATOM   427  C CG1 . VAL A 1 55  ? 25.293 -27.270 -5.648  1.00 37.68 ? 56  VAL A CG1 1 
ATOM   428  C CG2 . VAL A 1 55  ? 23.449 -27.024 -7.276  1.00 35.63 ? 56  VAL A CG2 1 
ATOM   429  N N   A GLU A 1 56  ? 24.097 -24.605 -9.202  0.52 28.99 ? 57  GLU A N   1 
ATOM   430  N N   B GLU A 1 56  ? 24.094 -24.605 -9.196  0.48 28.99 ? 57  GLU A N   1 
ATOM   431  C CA  A GLU A 1 56  ? 23.731 -24.245 -10.562 0.52 29.33 ? 57  GLU A CA  1 
ATOM   432  C CA  B GLU A 1 56  ? 23.701 -24.246 -10.551 0.48 29.34 ? 57  GLU A CA  1 
ATOM   433  C C   A GLU A 1 56  ? 23.672 -22.743 -10.784 0.52 27.08 ? 57  GLU A C   1 
ATOM   434  C C   B GLU A 1 56  ? 23.674 -22.743 -10.785 0.48 27.09 ? 57  GLU A C   1 
ATOM   435  O O   A GLU A 1 56  ? 23.339 -22.312 -11.894 0.52 27.30 ? 57  GLU A O   1 
ATOM   436  O O   B GLU A 1 56  ? 23.366 -22.313 -11.901 0.48 27.28 ? 57  GLU A O   1 
ATOM   437  C CB  A GLU A 1 56  ? 22.392 -24.891 -10.953 0.52 30.74 ? 57  GLU A CB  1 
ATOM   438  C CB  B GLU A 1 56  ? 22.331 -24.849 -10.894 0.48 30.70 ? 57  GLU A CB  1 
ATOM   439  C CG  A GLU A 1 56  ? 22.443 -26.412 -10.985 0.52 36.14 ? 57  GLU A CG  1 
ATOM   440  C CG  B GLU A 1 56  ? 22.273 -26.363 -10.761 0.48 35.83 ? 57  GLU A CG  1 
ATOM   441  C CD  A GLU A 1 56  ? 21.088 -27.041 -11.223 0.52 42.36 ? 57  GLU A CD  1 
ATOM   442  C CD  B GLU A 1 56  ? 23.251 -27.060 -11.687 0.48 39.07 ? 57  GLU A CD  1 
ATOM   443  O OE1 A GLU A 1 56  ? 20.093 -26.546 -10.652 0.52 38.90 ? 57  GLU A OE1 1 
ATOM   444  O OE1 B GLU A 1 56  ? 23.351 -26.651 -12.864 0.48 39.44 ? 57  GLU A OE1 1 
ATOM   445  O OE2 A GLU A 1 56  ? 21.018 -28.035 -11.977 0.52 46.79 ? 57  GLU A OE2 1 
ATOM   446  O OE2 B GLU A 1 56  ? 23.923 -28.014 -11.237 0.48 43.28 ? 57  GLU A OE2 1 
ATOM   447  N N   . LYS A 1 57  ? 24.020 -21.938 -9.775  1.00 25.22 ? 58  LYS A N   1 
ATOM   448  C CA  . LYS A 1 57  ? 23.841 -20.491 -9.871  1.00 22.66 ? 58  LYS A CA  1 
ATOM   449  C C   . LYS A 1 57  ? 24.667 -19.877 -10.997 1.00 26.44 ? 58  LYS A C   1 
ATOM   450  O O   . LYS A 1 57  ? 24.165 -19.043 -11.760 1.00 22.73 ? 58  LYS A O   1 
ATOM   451  C CB  . LYS A 1 57  ? 24.164 -19.823 -8.532  1.00 25.72 ? 58  LYS A CB  1 
ATOM   452  C CG  . LYS A 1 57  ? 24.135 -18.305 -8.605  1.00 22.98 ? 58  LYS A CG  1 
ATOM   453  C CD  . LYS A 1 57  ? 24.610 -17.637 -7.322  1.00 26.83 ? 58  LYS A CD  1 
ATOM   454  C CE  . LYS A 1 57  ? 23.483 -17.525 -6.304  1.00 28.22 ? 58  LYS A CE  1 
ATOM   455  N NZ  . LYS A 1 57  ? 22.462 -16.503 -6.692  1.00 23.14 ? 58  LYS A NZ  1 
ATOM   456  N N   . ARG A 1 58  ? 25.944 -20.258 -11.109 1.00 23.11 ? 59  ARG A N   1 
ATOM   457  C CA  . ARG A 1 58  ? 26.818 -19.603 -12.075 1.00 25.85 ? 59  ARG A CA  1 
ATOM   458  C C   . ARG A 1 58  ? 26.284 -19.754 -13.493 1.00 21.97 ? 59  ARG A C   1 
ATOM   459  O O   . ARG A 1 58  ? 26.156 -18.767 -14.229 1.00 24.35 ? 59  ARG A O   1 
ATOM   460  C CB  . ARG A 1 58  ? 28.233 -20.172 -11.974 1.00 27.43 ? 59  ARG A CB  1 
ATOM   461  C CG  . ARG A 1 58  ? 29.289 -19.275 -12.595 1.00 37.00 ? 59  ARG A CG  1 
ATOM   462  C CD  . ARG A 1 58  ? 30.594 -20.021 -12.839 1.00 41.07 ? 59  ARG A CD  1 
ATOM   463  N NE  . ARG A 1 58  ? 31.706 -19.407 -12.120 1.00 53.92 ? 59  ARG A NE  1 
ATOM   464  C CZ  . ARG A 1 58  ? 32.326 -18.292 -12.499 1.00 50.48 ? 59  ARG A CZ  1 
ATOM   465  N NH1 . ARG A 1 58  ? 31.953 -17.649 -13.606 1.00 41.43 ? 59  ARG A NH1 1 
ATOM   466  N NH2 . ARG A 1 58  ? 33.327 -17.820 -11.770 1.00 46.63 ? 59  ARG A NH2 1 
ATOM   467  N N   . LYS A 1 59  ? 25.994 -20.992 -13.902 1.00 26.42 ? 60  LYS A N   1 
ATOM   468  C CA  . LYS A 1 59  ? 25.522 -21.227 -15.261 1.00 28.47 ? 60  LYS A CA  1 
ATOM   469  C C   . LYS A 1 59  ? 24.130 -20.648 -15.465 1.00 25.13 ? 60  LYS A C   1 
ATOM   470  O O   . LYS A 1 59  ? 23.813 -20.152 -16.552 1.00 28.67 ? 60  LYS A O   1 
ATOM   471  C CB  . LYS A 1 59  ? 25.532 -22.724 -15.571 1.00 29.79 ? 60  LYS A CB  1 
ATOM   472  N N   . THR A 1 60  ? 23.295 -20.690 -14.426 1.00 23.98 ? 61  THR A N   1 
ATOM   473  C CA  . THR A 1 60  ? 21.943 -20.145 -14.529 1.00 22.13 ? 61  THR A CA  1 
ATOM   474  C C   . THR A 1 60  ? 21.963 -18.639 -14.757 1.00 24.23 ? 61  THR A C   1 
ATOM   475  O O   . THR A 1 60  ? 21.203 -18.124 -15.587 1.00 23.04 ? 61  THR A O   1 
ATOM   476  C CB  . THR A 1 60  ? 21.137 -20.500 -13.277 1.00 20.87 ? 61  THR A CB  1 
ATOM   477  O OG1 . THR A 1 60  ? 21.003 -21.926 -13.169 1.00 24.76 ? 61  THR A OG1 1 
ATOM   478  C CG2 . THR A 1 60  ? 19.751 -19.899 -13.347 1.00 26.55 ? 61  THR A CG2 1 
ATOM   479  N N   . MET A 1 61  ? 22.820 -17.914 -14.030 1.00 21.82 ? 62  MET A N   1 
ATOM   480  C CA  . MET A 1 61  ? 22.897 -16.467 -14.202 1.00 20.58 ? 62  MET A CA  1 
ATOM   481  C C   . MET A 1 61  ? 23.529 -16.094 -15.536 1.00 21.82 ? 62  MET A C   1 
ATOM   482  O O   . MET A 1 61  ? 23.141 -15.098 -16.155 1.00 22.74 ? 62  MET A O   1 
ATOM   483  C CB  . MET A 1 61  ? 23.638 -15.826 -13.025 1.00 22.13 ? 62  MET A CB  1 
ATOM   484  C CG  . MET A 1 61  ? 22.850 -15.895 -11.719 1.00 19.79 ? 62  MET A CG  1 
ATOM   485  S SD  . MET A 1 61  ? 23.684 -15.289 -10.252 1.00 22.19 ? 62  MET A SD  1 
ATOM   486  C CE  . MET A 1 61  ? 23.643 -13.522 -10.500 1.00 24.96 ? 62  MET A CE  1 
ATOM   487  N N   . LEU A 1 62  ? 24.518 -16.872 -16.000 1.00 23.29 ? 63  LEU A N   1 
ATOM   488  C CA  . LEU A 1 62  ? 25.104 -16.585 -17.305 1.00 23.27 ? 63  LEU A CA  1 
ATOM   489  C C   . LEU A 1 62  ? 24.090 -16.809 -18.424 1.00 20.32 ? 63  LEU A C   1 
ATOM   490  O O   . LEU A 1 62  ? 24.019 -16.017 -19.372 1.00 25.17 ? 63  LEU A O   1 
ATOM   491  C CB  . LEU A 1 62  ? 26.353 -17.441 -17.512 1.00 22.69 ? 63  LEU A CB  1 
ATOM   492  C CG  . LEU A 1 62  ? 27.561 -16.919 -16.734 1.00 25.01 ? 63  LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 62  ? 28.589 -18.024 -16.578 1.00 29.26 ? 63  LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 62  ? 28.170 -15.722 -17.433 1.00 26.58 ? 63  LEU A CD2 1 
ATOM   495  N N   . GLU A 1 63  ? 23.305 -17.884 -18.332 1.00 23.26 ? 64  GLU A N   1 
ATOM   496  C CA  . GLU A 1 63  ? 22.267 -18.133 -19.328 1.00 23.63 ? 64  GLU A CA  1 
ATOM   497  C C   . GLU A 1 63  ? 21.229 -17.016 -19.321 1.00 28.69 ? 64  GLU A C   1 
ATOM   498  O O   . GLU A 1 63  ? 20.793 -16.555 -20.382 1.00 27.82 ? 64  GLU A O   1 
ATOM   499  C CB  . GLU A 1 63  ? 21.610 -19.487 -19.066 1.00 28.10 ? 64  GLU A CB  1 
ATOM   500  C CG  . GLU A 1 63  ? 20.414 -19.786 -19.967 1.00 35.60 ? 64  GLU A CG  1 
ATOM   501  C CD  . GLU A 1 63  ? 20.213 -21.274 -20.215 1.00 59.46 ? 64  GLU A CD  1 
ATOM   502  O OE1 . GLU A 1 63  ? 20.254 -21.695 -21.394 1.00 64.97 ? 64  GLU A OE1 1 
ATOM   503  O OE2 . GLU A 1 63  ? 20.015 -22.024 -19.234 1.00 56.28 ? 64  GLU A OE2 1 
ATOM   504  N N   . LEU A 1 64  ? 20.839 -16.558 -18.129 1.00 24.88 ? 65  LEU A N   1 
ATOM   505  C CA  . LEU A 1 64  ? 19.883 -15.460 -18.021 1.00 25.33 ? 65  LEU A CA  1 
ATOM   506  C C   . LEU A 1 64  ? 20.410 -14.207 -18.704 1.00 25.60 ? 65  LEU A C   1 
ATOM   507  O O   . LEU A 1 64  ? 19.707 -13.579 -19.505 1.00 25.01 ? 65  LEU A O   1 
ATOM   508  C CB  . LEU A 1 64  ? 19.609 -15.176 -16.544 1.00 25.56 ? 65  LEU A CB  1 
ATOM   509  C CG  . LEU A 1 64  ? 18.694 -13.993 -16.236 1.00 32.40 ? 65  LEU A CG  1 
ATOM   510  C CD1 . LEU A 1 64  ? 17.271 -14.410 -16.397 1.00 30.04 ? 65  LEU A CD1 1 
ATOM   511  C CD2 . LEU A 1 64  ? 18.951 -13.484 -14.827 1.00 32.32 ? 65  LEU A CD2 1 
ATOM   512  N N   . VAL A 1 65  ? 21.653 -13.830 -18.399 1.00 23.97 ? 66  VAL A N   1 
ATOM   513  C CA  . VAL A 1 65  ? 22.215 -12.586 -18.917 1.00 22.59 ? 66  VAL A CA  1 
ATOM   514  C C   . VAL A 1 65  ? 22.224 -12.584 -20.442 1.00 27.27 ? 66  VAL A C   1 
ATOM   515  O O   . VAL A 1 65  ? 21.825 -11.603 -21.079 1.00 29.47 ? 66  VAL A O   1 
ATOM   516  C CB  . VAL A 1 65  ? 23.617 -12.343 -18.329 1.00 25.88 ? 66  VAL A CB  1 
ATOM   517  C CG1 . VAL A 1 65  ? 24.398 -11.377 -19.186 1.00 31.40 ? 66  VAL A CG1 1 
ATOM   518  C CG2 . VAL A 1 65  ? 23.506 -11.829 -16.900 1.00 28.98 ? 66  VAL A CG2 1 
ATOM   519  N N   . GLU A 1 66  ? 22.678 -13.683 -21.051 1.00 25.46 ? 67  GLU A N   1 
ATOM   520  C CA  . GLU A 1 66  ? 22.804 -13.699 -22.507 1.00 29.01 ? 67  GLU A CA  1 
ATOM   521  C C   . GLU A 1 66  ? 21.440 -13.624 -23.181 1.00 27.15 ? 67  GLU A C   1 
ATOM   522  O O   . GLU A 1 66  ? 21.280 -12.921 -24.188 1.00 28.64 ? 67  GLU A O   1 
ATOM   523  C CB  . GLU A 1 66  ? 23.598 -14.919 -22.979 1.00 30.37 ? 67  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 66  ? 23.007 -16.259 -22.594 1.00 28.71 ? 67  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 66  ? 23.847 -17.431 -23.077 1.00 33.82 ? 67  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 66  ? 23.393 -18.589 -22.943 1.00 38.34 ? 67  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 66  ? 24.957 -17.192 -23.594 1.00 37.32 ? 67  GLU A OE2 1 
ATOM   528  N N   . LYS A 1 67  ? 20.439 -14.302 -22.614 1.00 24.58 ? 68  LYS A N   1 
ATOM   529  C CA  . LYS A 1 67  ? 19.108 -14.312 -23.211 1.00 26.36 ? 68  LYS A CA  1 
ATOM   530  C C   . LYS A 1 67  ? 18.416 -12.967 -23.037 1.00 28.10 ? 68  LYS A C   1 
ATOM   531  O O   . LYS A 1 67  ? 17.681 -12.520 -23.927 1.00 27.05 ? 68  LYS A O   1 
ATOM   532  C CB  . LYS A 1 67  ? 18.272 -15.425 -22.591 1.00 25.76 ? 68  LYS A CB  1 
ATOM   533  C CG  . LYS A 1 67  ? 18.714 -16.826 -23.001 1.00 29.33 ? 68  LYS A CG  1 
ATOM   534  C CD  . LYS A 1 67  ? 17.787 -17.869 -22.409 1.00 35.37 ? 68  LYS A CD  1 
ATOM   535  C CE  . LYS A 1 67  ? 18.174 -19.269 -22.839 1.00 47.45 ? 68  LYS A CE  1 
ATOM   536  N NZ  . LYS A 1 67  ? 17.063 -20.229 -22.601 1.00 50.32 ? 68  LYS A NZ  1 
ATOM   537  N N   . VAL A 1 68  ? 18.637 -12.307 -21.900 1.00 28.25 ? 69  VAL A N   1 
ATOM   538  C CA  . VAL A 1 68  ? 18.081 -10.973 -21.698 1.00 25.08 ? 69  VAL A CA  1 
ATOM   539  C C   . VAL A 1 68  ? 18.735 -9.972  -22.643 1.00 30.51 ? 69  VAL A C   1 
ATOM   540  O O   . VAL A 1 68  ? 18.048 -9.200  -23.323 1.00 31.67 ? 69  VAL A O   1 
ATOM   541  C CB  . VAL A 1 68  ? 18.213 -10.547 -20.223 1.00 24.56 ? 69  VAL A CB  1 
ATOM   542  C CG1 . VAL A 1 68  ? 17.941 -9.059  -20.070 1.00 30.63 ? 69  VAL A CG1 1 
ATOM   543  C CG2 . VAL A 1 68  ? 17.269 -11.351 -19.358 1.00 25.43 ? 69  VAL A CG2 1 
ATOM   544  N N   . ALA A 1 69  ? 20.072 -9.984  -22.717 1.00 28.17 ? 70  ALA A N   1 
ATOM   545  C CA  . ALA A 1 69  ? 20.790 -8.973  -23.487 1.00 29.52 ? 70  ALA A CA  1 
ATOM   546  C C   . ALA A 1 69  ? 20.383 -8.975  -24.952 1.00 33.73 ? 70  ALA A C   1 
ATOM   547  O O   . ALA A 1 69  ? 20.379 -7.922  -25.594 1.00 35.04 ? 70  ALA A O   1 
ATOM   548  C CB  . ALA A 1 69  ? 22.302 -9.171  -23.357 1.00 30.20 ? 70  ALA A CB  1 
ATOM   549  N N   . GLU A 1 70  ? 20.040 -10.135 -25.501 1.00 31.98 ? 71  GLU A N   1 
ATOM   550  C CA  . GLU A 1 70  ? 19.741 -10.174 -26.924 1.00 40.53 ? 71  GLU A CA  1 
ATOM   551  C C   . GLU A 1 70  ? 18.329 -9.709  -27.262 1.00 38.39 ? 71  GLU A C   1 
ATOM   552  O O   . GLU A 1 70  ? 18.045 -9.481  -28.444 1.00 38.18 ? 71  GLU A O   1 
ATOM   553  C CB  . GLU A 1 70  ? 20.025 -11.561 -27.499 1.00 39.30 ? 71  GLU A CB  1 
ATOM   554  C CG  . GLU A 1 70  ? 19.042 -12.631 -27.086 1.00 41.56 ? 71  GLU A CG  1 
ATOM   555  C CD  . GLU A 1 70  ? 19.117 -13.846 -27.988 1.00 43.79 ? 71  GLU A CD  1 
ATOM   556  O OE1 . GLU A 1 70  ? 20.010 -13.883 -28.864 1.00 50.87 ? 71  GLU A OE1 1 
ATOM   557  O OE2 . GLU A 1 70  ? 18.293 -14.767 -27.818 1.00 46.51 ? 71  GLU A OE2 1 
ATOM   558  N N   . GLN A 1 71  ? 17.451 -9.528  -26.265 1.00 32.66 ? 72  GLN A N   1 
ATOM   559  C CA  . GLN A 1 71  ? 16.084 -9.101  -26.531 1.00 29.49 ? 72  GLN A CA  1 
ATOM   560  C C   . GLN A 1 71  ? 15.713 -7.736  -25.963 1.00 36.76 ? 72  GLN A C   1 
ATOM   561  O O   . GLN A 1 71  ? 14.741 -7.142  -26.437 1.00 38.84 ? 72  GLN A O   1 
ATOM   562  C CB  . GLN A 1 71  ? 15.075 -10.146 -26.035 1.00 37.82 ? 72  GLN A CB  1 
ATOM   563  C CG  . GLN A 1 71  ? 15.129 -11.439 -26.835 1.00 37.14 ? 72  GLN A CG  1 
ATOM   564  C CD  . GLN A 1 71  ? 13.820 -12.211 -26.792 1.00 47.06 ? 72  GLN A CD  1 
ATOM   565  O OE1 . GLN A 1 71  ? 12.753 -11.648 -27.032 1.00 49.00 ? 72  GLN A OE1 1 
ATOM   566  N NE2 . GLN A 1 71  ? 13.899 -13.510 -26.515 1.00 42.93 ? 72  GLN A NE2 1 
ATOM   567  N N   . ILE A 1 72  ? 16.435 -7.217  -24.972 1.00 33.14 ? 73  ILE A N   1 
ATOM   568  C CA  . ILE A 1 72  ? 16.073 -5.930  -24.381 1.00 31.99 ? 73  ILE A CA  1 
ATOM   569  C C   . ILE A 1 72  ? 17.102 -4.878  -24.765 1.00 36.59 ? 73  ILE A C   1 
ATOM   570  O O   . ILE A 1 72  ? 18.286 -5.174  -24.967 1.00 36.53 ? 73  ILE A O   1 
ATOM   571  C CB  . ILE A 1 72  ? 15.842 -5.966  -22.853 1.00 39.54 ? 73  ILE A CB  1 
ATOM   572  C CG1 . ILE A 1 72  ? 17.167 -5.971  -22.103 1.00 36.39 ? 73  ILE A CG1 1 
ATOM   573  C CG2 . ILE A 1 72  ? 14.996 -7.167  -22.464 1.00 35.81 ? 73  ILE A CG2 1 
ATOM   574  C CD1 . ILE A 1 72  ? 17.037 -5.530  -20.668 1.00 34.05 ? 73  ILE A CD1 1 
ATOM   575  N N   . ASP A 1 73  ? 16.633 -3.634  -24.868 1.00 33.33 ? 74  ASP A N   1 
ATOM   576  C CA  . ASP A 1 73  ? 17.462 -2.503  -25.270 1.00 39.43 ? 74  ASP A CA  1 
ATOM   577  C C   . ASP A 1 73  ? 17.566 -1.438  -24.181 1.00 37.48 ? 74  ASP A C   1 
ATOM   578  O O   . ASP A 1 73  ? 17.954 -0.302  -24.469 1.00 45.75 ? 74  ASP A O   1 
ATOM   579  C CB  . ASP A 1 73  ? 16.954 -1.888  -26.576 1.00 41.26 ? 74  ASP A CB  1 
ATOM   580  N N   . ILE A 1 74  ? 17.221 -1.776  -22.942 1.00 26.25 ? 75  ILE A N   1 
ATOM   581  C CA  . ILE A 1 74  ? 17.415 -0.878  -21.807 1.00 22.98 ? 75  ILE A CA  1 
ATOM   582  C C   . ILE A 1 74  ? 18.486 -1.493  -20.910 1.00 21.84 ? 75  ILE A C   1 
ATOM   583  O O   . ILE A 1 74  ? 18.737 -2.705  -20.996 1.00 24.32 ? 75  ILE A O   1 
ATOM   584  C CB  . ILE A 1 74  ? 16.100 -0.642  -21.044 1.00 23.24 ? 75  ILE A CB  1 
ATOM   585  C CG1 . ILE A 1 74  ? 15.578 -1.953  -20.462 1.00 20.02 ? 75  ILE A CG1 1 
ATOM   586  C CG2 . ILE A 1 74  ? 15.064 0.007   -21.954 1.00 27.52 ? 75  ILE A CG2 1 
ATOM   587  C CD1 . ILE A 1 74  ? 14.446 -1.755  -19.467 1.00 21.36 ? 75  ILE A CD1 1 
ATOM   588  N N   . PRO A 1 75  ? 19.130 -0.716  -20.042 1.00 21.16 ? 76  PRO A N   1 
ATOM   589  C CA  . PRO A 1 75  ? 20.176 -1.288  -19.187 1.00 23.24 ? 76  PRO A CA  1 
ATOM   590  C C   . PRO A 1 75  ? 19.599 -2.259  -18.175 1.00 22.41 ? 76  PRO A C   1 
ATOM   591  O O   . PRO A 1 75  ? 18.482 -2.091  -17.673 1.00 20.77 ? 76  PRO A O   1 
ATOM   592  C CB  . PRO A 1 75  ? 20.772 -0.069  -18.476 1.00 23.32 ? 76  PRO A CB  1 
ATOM   593  C CG  . PRO A 1 75  ? 20.326 1.120   -19.262 1.00 24.58 ? 76  PRO A CG  1 
ATOM   594  C CD  . PRO A 1 75  ? 19.001 0.737   -19.854 1.00 21.81 ? 76  PRO A CD  1 
ATOM   595  N N   . PHE A 1 76  ? 20.384 -3.284  -17.865 1.00 20.63 ? 77  PHE A N   1 
ATOM   596  C CA  . PHE A 1 76  ? 20.000 -4.194  -16.804 1.00 22.22 ? 77  PHE A CA  1 
ATOM   597  C C   . PHE A 1 76  ? 21.196 -4.548  -15.931 1.00 20.47 ? 77  PHE A C   1 
ATOM   598  O O   . PHE A 1 76  ? 22.359 -4.536  -16.370 1.00 19.59 ? 77  PHE A O   1 
ATOM   599  C CB  . PHE A 1 76  ? 19.249 -5.435  -17.297 1.00 19.32 ? 77  PHE A CB  1 
ATOM   600  C CG  . PHE A 1 76  ? 20.091 -6.402  -18.082 1.00 22.75 ? 77  PHE A CG  1 
ATOM   601  C CD1 . PHE A 1 76  ? 20.451 -6.131  -19.396 1.00 27.38 ? 77  PHE A CD1 1 
ATOM   602  C CD2 . PHE A 1 76  ? 20.479 -7.611  -17.522 1.00 24.08 ? 77  PHE A CD2 1 
ATOM   603  C CE1 . PHE A 1 76  ? 21.206 -7.041  -20.129 1.00 23.82 ? 77  PHE A CE1 1 
ATOM   604  C CE2 . PHE A 1 76  ? 21.227 -8.520  -18.246 1.00 27.00 ? 77  PHE A CE2 1 
ATOM   605  C CZ  . PHE A 1 76  ? 21.591 -8.237  -19.551 1.00 27.76 ? 77  PHE A CZ  1 
ATOM   606  N N   . THR A 1 77  ? 20.881 -4.816  -14.669 1.00 17.74 ? 78  THR A N   1 
ATOM   607  C CA  . THR A 1 77  ? 21.829 -5.233  -13.648 1.00 17.19 ? 78  THR A CA  1 
ATOM   608  C C   . THR A 1 77  ? 21.478 -6.654  -13.242 1.00 16.94 ? 78  THR A C   1 
ATOM   609  O O   . THR A 1 77  ? 20.298 -7.008  -13.138 1.00 17.49 ? 78  THR A O   1 
ATOM   610  C CB  . THR A 1 77  ? 21.717 -4.338  -12.409 1.00 18.52 ? 78  THR A CB  1 
ATOM   611  O OG1 . THR A 1 77  ? 21.843 -2.964  -12.782 1.00 19.53 ? 78  THR A OG1 1 
ATOM   612  C CG2 . THR A 1 77  ? 22.782 -4.684  -11.375 1.00 19.83 ? 78  THR A CG2 1 
ATOM   613  N N   . VAL A 1 78  ? 22.498 -7.477  -13.014 1.00 18.21 ? 79  VAL A N   1 
ATOM   614  C CA  . VAL A 1 78  ? 22.299 -8.811  -12.474 1.00 19.31 ? 79  VAL A CA  1 
ATOM   615  C C   . VAL A 1 78  ? 23.026 -8.886  -11.141 1.00 19.34 ? 79  VAL A C   1 
ATOM   616  O O   . VAL A 1 78  ? 24.108 -8.312  -10.982 1.00 18.01 ? 79  VAL A O   1 
ATOM   617  C CB  . VAL A 1 78  ? 22.758 -9.916  -13.455 1.00 19.43 ? 79  VAL A CB  1 
ATOM   618  C CG1 . VAL A 1 78  ? 24.275 -9.898  -13.659 1.00 23.37 ? 79  VAL A CG1 1 
ATOM   619  C CG2 . VAL A 1 78  ? 22.273 -11.284 -13.005 1.00 24.22 ? 79  VAL A CG2 1 
ATOM   620  N N   . GLY A 1 79  ? 22.421 -9.574  -10.179 1.00 18.14 ? 80  GLY A N   1 
ATOM   621  C CA  . GLY A 1 79  ? 23.049 -9.726  -8.883  1.00 22.33 ? 80  GLY A CA  1 
ATOM   622  C C   . GLY A 1 79  ? 22.467 -10.905 -8.145  1.00 19.52 ? 80  GLY A C   1 
ATOM   623  O O   . GLY A 1 79  ? 21.535 -11.566 -8.610  1.00 17.64 ? 80  GLY A O   1 
ATOM   624  N N   . GLY A 1 80  ? 23.025 -11.143 -6.962  1.00 20.74 ? 81  GLY A N   1 
ATOM   625  C CA  . GLY A 1 80  ? 22.608 -12.248 -6.127  1.00 26.85 ? 81  GLY A CA  1 
ATOM   626  C C   . GLY A 1 80  ? 23.705 -13.278 -5.986  1.00 25.78 ? 81  GLY A C   1 
ATOM   627  O O   . GLY A 1 80  ? 23.824 -14.179 -6.821  1.00 25.91 ? 81  GLY A O   1 
ATOM   628  N N   . GLY A 1 81  ? 24.535 -13.138 -4.957  1.00 25.06 ? 82  GLY A N   1 
ATOM   629  C CA  . GLY A 1 81  ? 25.572 -14.123 -4.714  1.00 27.34 ? 82  GLY A CA  1 
ATOM   630  C C   . GLY A 1 81  ? 26.753 -14.050 -5.655  1.00 28.14 ? 82  GLY A C   1 
ATOM   631  O O   . GLY A 1 81  ? 27.411 -15.071 -5.890  1.00 29.41 ? 82  GLY A O   1 
ATOM   632  N N   . ILE A 1 82  ? 27.034 -12.878 -6.219  1.00 21.27 ? 83  ILE A N   1 
ATOM   633  C CA  . ILE A 1 82  ? 28.256 -12.684 -6.994  1.00 20.34 ? 83  ILE A CA  1 
ATOM   634  C C   . ILE A 1 82  ? 29.388 -12.496 -5.992  1.00 22.86 ? 83  ILE A C   1 
ATOM   635  O O   . ILE A 1 82  ? 29.428 -11.497 -5.269  1.00 21.42 ? 83  ILE A O   1 
ATOM   636  C CB  . ILE A 1 82  ? 28.142 -11.494 -7.954  1.00 20.42 ? 83  ILE A CB  1 
ATOM   637  C CG1 . ILE A 1 82  ? 27.026 -11.748 -8.971  1.00 24.49 ? 83  ILE A CG1 1 
ATOM   638  C CG2 . ILE A 1 82  ? 29.467 -11.239 -8.665  1.00 22.49 ? 83  ILE A CG2 1 
ATOM   639  C CD1 . ILE A 1 82  ? 26.645 -10.527 -9.781  1.00 26.13 ? 83  ILE A CD1 1 
ATOM   640  N N   . HIS A 1 83  ? 30.308 -13.459 -5.934  1.00 25.51 ? 84  HIS A N   1 
ATOM   641  C CA  . HIS A 1 83  ? 31.261 -13.511 -4.834  1.00 24.20 ? 84  HIS A CA  1 
ATOM   642  C C   . HIS A 1 83  ? 32.681 -13.113 -5.196  1.00 22.46 ? 84  HIS A C   1 
ATOM   643  O O   . HIS A 1 83  ? 33.498 -12.944 -4.283  1.00 26.63 ? 84  HIS A O   1 
ATOM   644  C CB  . HIS A 1 83  ? 31.265 -14.904 -4.187  1.00 29.12 ? 84  HIS A CB  1 
ATOM   645  C CG  . HIS A 1 83  ? 29.992 -15.237 -3.472  1.00 37.91 ? 84  HIS A CG  1 
ATOM   646  N ND1 . HIS A 1 83  ? 29.330 -16.434 -3.645  1.00 49.39 ? 84  HIS A ND1 1 
ATOM   647  C CD2 . HIS A 1 83  ? 29.253 -14.523 -2.591  1.00 39.30 ? 84  HIS A CD2 1 
ATOM   648  C CE1 . HIS A 1 83  ? 28.241 -16.444 -2.896  1.00 47.12 ? 84  HIS A CE1 1 
ATOM   649  N NE2 . HIS A 1 83  ? 28.172 -15.296 -2.246  1.00 49.30 ? 84  HIS A NE2 1 
ATOM   650  N N   . ASP A 1 84  ? 33.015 -12.963 -6.474  1.00 22.32 ? 85  ASP A N   1 
ATOM   651  C CA  . ASP A 1 84  ? 34.406 -12.703 -6.828  1.00 23.34 ? 85  ASP A CA  1 
ATOM   652  C C   . ASP A 1 84  ? 34.500 -12.016 -8.187  1.00 22.63 ? 85  ASP A C   1 
ATOM   653  O O   . ASP A 1 84  ? 33.510 -11.853 -8.907  1.00 21.99 ? 85  ASP A O   1 
ATOM   654  C CB  . ASP A 1 84  ? 35.268 -13.970 -6.731  1.00 26.48 ? 85  ASP A CB  1 
ATOM   655  C CG  . ASP A 1 84  ? 34.796 -15.081 -7.645  1.00 31.25 ? 85  ASP A CG  1 
ATOM   656  O OD1 . ASP A 1 84  ? 34.157 -14.795 -8.678  1.00 27.49 ? 85  ASP A OD1 1 
ATOM   657  O OD2 . ASP A 1 84  ? 35.085 -16.256 -7.334  1.00 35.82 ? 85  ASP A OD2 1 
ATOM   658  N N   . PHE A 1 85  ? 35.721 -11.611 -8.527  1.00 22.87 ? 86  PHE A N   1 
ATOM   659  C CA  . PHE A 1 85  ? 35.957 -10.881 -9.765  1.00 20.87 ? 86  PHE A CA  1 
ATOM   660  C C   . PHE A 1 85  ? 35.638 -11.734 -10.986 1.00 24.19 ? 86  PHE A C   1 
ATOM   661  O O   . PHE A 1 85  ? 35.033 -11.245 -11.947 1.00 22.31 ? 86  PHE A O   1 
ATOM   662  C CB  . PHE A 1 85  ? 37.409 -10.395 -9.817  1.00 23.40 ? 86  PHE A CB  1 
ATOM   663  C CG  . PHE A 1 85  ? 37.757 -9.690  -11.095 1.00 22.27 ? 86  PHE A CG  1 
ATOM   664  C CD1 . PHE A 1 85  ? 38.243 -10.401 -12.184 1.00 21.17 ? 86  PHE A CD1 1 
ATOM   665  C CD2 . PHE A 1 85  ? 37.575 -8.326  -11.223 1.00 20.61 ? 86  PHE A CD2 1 
ATOM   666  C CE1 . PHE A 1 85  ? 38.550 -9.757  -13.365 1.00 25.53 ? 86  PHE A CE1 1 
ATOM   667  C CE2 . PHE A 1 85  ? 37.872 -7.683  -12.399 1.00 21.68 ? 86  PHE A CE2 1 
ATOM   668  C CZ  . PHE A 1 85  ? 38.366 -8.398  -13.473 1.00 23.47 ? 86  PHE A CZ  1 
ATOM   669  N N   . GLU A 1 86  ? 36.068 -12.999 -10.985 1.00 23.05 ? 87  GLU A N   1 
ATOM   670  C CA  . GLU A 1 86  ? 35.833 -13.861 -12.139 1.00 26.23 ? 87  GLU A CA  1 
ATOM   671  C C   . GLU A 1 86  ? 34.347 -13.978 -12.439 1.00 27.49 ? 87  GLU A C   1 
ATOM   672  O O   . GLU A 1 86  ? 33.940 -13.964 -13.606 1.00 25.59 ? 87  GLU A O   1 
ATOM   673  C CB  . GLU A 1 86  ? 36.414 -15.252 -11.881 1.00 29.30 ? 87  GLU A CB  1 
ATOM   674  C CG  . GLU A 1 86  ? 37.806 -15.251 -11.263 1.00 41.88 ? 87  GLU A CG  1 
ATOM   675  C CD  . GLU A 1 86  ? 37.760 -15.154 -9.750  1.00 44.38 ? 87  GLU A CD  1 
ATOM   676  O OE1 . GLU A 1 86  ? 38.117 -14.079 -9.207  1.00 33.70 ? 87  GLU A OE1 1 
ATOM   677  O OE2 . GLU A 1 86  ? 37.337 -16.144 -9.109  1.00 56.06 ? 87  GLU A OE2 1 
ATOM   678  N N   . THR A 1 87  ? 33.524 -14.111 -11.396 1.00 23.37 ? 88  THR A N   1 
ATOM   679  C CA  . THR A 1 87  ? 32.085 -14.220 -11.603 1.00 20.94 ? 88  THR A CA  1 
ATOM   680  C C   . THR A 1 87  ? 31.520 -12.933 -12.185 1.00 22.65 ? 88  THR A C   1 
ATOM   681  O O   . THR A 1 87  ? 30.758 -12.964 -13.159 1.00 24.49 ? 88  THR A O   1 
ATOM   682  C CB  . THR A 1 87  ? 31.372 -14.592 -10.302 1.00 22.67 ? 88  THR A CB  1 
ATOM   683  O OG1 . THR A 1 87  ? 31.949 -15.792 -9.761  1.00 26.65 ? 88  THR A OG1 1 
ATOM   684  C CG2 . THR A 1 87  ? 29.893 -14.820 -10.566 1.00 23.95 ? 88  THR A CG2 1 
ATOM   685  N N   . ALA A 1 88  ? 31.893 -11.788 -11.604 1.00 21.27 ? 89  ALA A N   1 
ATOM   686  C CA  . ALA A 1 88  ? 31.406 -10.504 -12.099 1.00 20.83 ? 89  ALA A CA  1 
ATOM   687  C C   . ALA A 1 88  ? 31.851 -10.257 -13.534 1.00 27.24 ? 89  ALA A C   1 
ATOM   688  O O   . ALA A 1 88  ? 31.048 -9.840  -14.378 1.00 25.40 ? 89  ALA A O   1 
ATOM   689  C CB  . ALA A 1 88  ? 31.876 -9.378  -11.181 1.00 20.35 ? 89  ALA A CB  1 
ATOM   690  N N   . SER A 1 89  ? 33.125 -10.521 -13.831 1.00 22.56 ? 90  SER A N   1 
ATOM   691  C CA  . SER A 1 89  ? 33.640 -10.328 -15.182 1.00 25.84 ? 90  SER A CA  1 
ATOM   692  C C   . SER A 1 89  ? 32.883 -11.167 -16.205 1.00 26.81 ? 90  SER A C   1 
ATOM   693  O O   . SER A 1 89  ? 32.539 -10.674 -17.285 1.00 28.44 ? 90  SER A O   1 
ATOM   694  C CB  . SER A 1 89  ? 35.126 -10.679 -15.206 1.00 27.68 ? 90  SER A CB  1 
ATOM   695  O OG  A SER A 1 89  ? 35.895 -9.606  -14.714 0.41 32.37 ? 90  SER A OG  1 
ATOM   696  O OG  B SER A 1 89  ? 35.725 -10.305 -16.433 0.59 28.94 ? 90  SER A OG  1 
ATOM   697  N N   . GLU A 1 90  ? 32.626 -12.439 -15.895 1.00 25.56 ? 91  GLU A N   1 
ATOM   698  C CA  . GLU A 1 90  ? 31.945 -13.308 -16.853 1.00 25.06 ? 91  GLU A CA  1 
ATOM   699  C C   . GLU A 1 90  ? 30.539 -12.803 -17.159 1.00 32.44 ? 91  GLU A C   1 
ATOM   700  O O   . GLU A 1 90  ? 30.072 -12.888 -18.302 1.00 30.22 ? 91  GLU A O   1 
ATOM   701  C CB  . GLU A 1 90  ? 31.888 -14.739 -16.319 1.00 27.76 ? 91  GLU A CB  1 
ATOM   702  N N   . LEU A 1 91  ? 29.848 -12.270 -16.149 1.00 26.08 ? 92  LEU A N   1 
ATOM   703  C CA  . LEU A 1 91  ? 28.482 -11.793 -16.353 1.00 26.27 ? 92  LEU A CA  1 
ATOM   704  C C   . LEU A 1 91  ? 28.450 -10.529 -17.205 1.00 25.63 ? 92  LEU A C   1 
ATOM   705  O O   . LEU A 1 91  ? 27.560 -10.370 -18.051 1.00 28.15 ? 92  LEU A O   1 
ATOM   706  C CB  . LEU A 1 91  ? 27.823 -11.547 -14.999 1.00 20.38 ? 92  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 91  ? 27.523 -12.832 -14.237 1.00 19.03 ? 92  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 91  ? 27.260 -12.579 -12.752 1.00 23.67 ? 92  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 91  ? 26.338 -13.556 -14.867 1.00 21.60 ? 92  LEU A CD2 1 
ATOM   710  N N   . ILE A 1 92  ? 29.396 -9.613  -16.989 1.00 23.83 ? 93  ILE A N   1 
ATOM   711  C CA  . ILE A 1 92  ? 29.466 -8.415  -17.820 1.00 24.28 ? 93  ILE A CA  1 
ATOM   712  C C   . ILE A 1 92  ? 29.831 -8.778  -19.256 1.00 33.17 ? 93  ILE A C   1 
ATOM   713  O O   . ILE A 1 92  ? 29.251 -8.247  -20.211 1.00 29.91 ? 93  ILE A O   1 
ATOM   714  C CB  . ILE A 1 92  ? 30.441 -7.393  -17.210 1.00 25.48 ? 93  ILE A CB  1 
ATOM   715  C CG1 . ILE A 1 92  ? 29.968 -6.981  -15.814 1.00 25.87 ? 93  ILE A CG1 1 
ATOM   716  C CG2 . ILE A 1 92  ? 30.573 -6.178  -18.113 1.00 26.98 ? 93  ILE A CG2 1 
ATOM   717  C CD1 . ILE A 1 92  ? 30.977 -6.145  -15.054 1.00 26.77 ? 93  ILE A CD1 1 
ATOM   718  N N   . LEU A 1 93  ? 30.798 -9.685  -19.435 1.00 32.04 ? 94  LEU A N   1 
ATOM   719  C CA  . LEU A 1 93  ? 31.192 -10.079 -20.785 1.00 32.94 ? 94  LEU A CA  1 
ATOM   720  C C   . LEU A 1 93  ? 30.061 -10.795 -21.513 1.00 37.17 ? 94  LEU A C   1 
ATOM   721  O O   . LEU A 1 93  ? 29.966 -10.709 -22.743 1.00 38.52 ? 94  LEU A O   1 
ATOM   722  C CB  . LEU A 1 93  ? 32.441 -10.960 -20.738 1.00 29.75 ? 94  LEU A CB  1 
ATOM   723  C CG  . LEU A 1 93  ? 33.744 -10.288 -20.302 1.00 34.56 ? 94  LEU A CG  1 
ATOM   724  C CD1 . LEU A 1 93  ? 34.850 -11.322 -20.200 1.00 36.49 ? 94  LEU A CD1 1 
ATOM   725  C CD2 . LEU A 1 93  ? 34.137 -9.172  -21.258 1.00 35.34 ? 94  LEU A CD2 1 
ATOM   726  N N   . ARG A 1 94  ? 29.198 -11.496 -20.778 1.00 33.15 ? 95  ARG A N   1 
ATOM   727  C CA  . ARG A 1 94  ? 28.057 -12.178 -21.370 1.00 33.21 ? 95  ARG A CA  1 
ATOM   728  C C   . ARG A 1 94  ? 26.924 -11.230 -21.746 1.00 34.61 ? 95  ARG A C   1 
ATOM   729  O O   . ARG A 1 94  ? 26.000 -11.648 -22.451 1.00 39.55 ? 95  ARG A O   1 
ATOM   730  C CB  . ARG A 1 94  ? 27.550 -13.267 -20.422 1.00 33.22 ? 95  ARG A CB  1 
ATOM   731  C CG  . ARG A 1 94  ? 26.826 -14.413 -21.108 1.00 36.92 ? 95  ARG A CG  1 
ATOM   732  C CD  . ARG A 1 94  ? 27.783 -15.236 -21.947 1.00 36.26 ? 95  ARG A CD  1 
ATOM   733  N NE  . ARG A 1 94  ? 28.583 -16.145 -21.138 1.00 33.86 ? 95  ARG A NE  1 
ATOM   734  C CZ  . ARG A 1 94  ? 28.238 -17.397 -20.855 1.00 37.00 ? 95  ARG A CZ  1 
ATOM   735  N NH1 . ARG A 1 94  ? 27.103 -17.903 -21.321 1.00 35.13 ? 95  ARG A NH1 1 
ATOM   736  N NH2 . ARG A 1 94  ? 29.031 -18.146 -20.108 1.00 39.27 ? 95  ARG A NH2 1 
ATOM   737  N N   . GLY A 1 95  ? 26.960 -9.980  -21.293 1.00 31.17 ? 96  GLY A N   1 
ATOM   738  C CA  . GLY A 1 95  ? 25.993 -9.011  -21.766 1.00 35.97 ? 96  GLY A CA  1 
ATOM   739  C C   . GLY A 1 95  ? 25.328 -8.147  -20.713 1.00 29.51 ? 96  GLY A C   1 
ATOM   740  O O   . GLY A 1 95  ? 24.556 -7.249  -21.056 1.00 30.16 ? 96  GLY A O   1 
ATOM   741  N N   . ALA A 1 96  ? 25.605 -8.392  -19.435 1.00 29.77 ? 97  ALA A N   1 
ATOM   742  C CA  . ALA A 1 96  ? 25.026 -7.551  -18.394 1.00 27.15 ? 97  ALA A CA  1 
ATOM   743  C C   . ALA A 1 96  ? 25.655 -6.164  -18.440 1.00 28.88 ? 97  ALA A C   1 
ATOM   744  O O   . ALA A 1 96  ? 26.877 -6.022  -18.549 1.00 24.34 ? 97  ALA A O   1 
ATOM   745  C CB  . ALA A 1 96  ? 25.250 -8.183  -17.022 1.00 27.67 ? 97  ALA A CB  1 
ATOM   746  N N   . ASP A 1 97  ? 24.822 -5.129  -18.372 1.00 23.45 ? 98  ASP A N   1 
ATOM   747  C CA  . ASP A 1 97  ? 25.370 -3.782  -18.328 1.00 21.07 ? 98  ASP A CA  1 
ATOM   748  C C   . ASP A 1 97  ? 26.062 -3.513  -17.000 1.00 21.16 ? 98  ASP A C   1 
ATOM   749  O O   . ASP A 1 97  ? 27.075 -2.806  -16.950 1.00 23.69 ? 98  ASP A O   1 
ATOM   750  C CB  . ASP A 1 97  ? 24.259 -2.770  -18.580 1.00 24.59 ? 98  ASP A CB  1 
ATOM   751  C CG  . ASP A 1 97  ? 23.627 -2.961  -19.921 1.00 28.15 ? 98  ASP A CG  1 
ATOM   752  O OD1 . ASP A 1 97  ? 24.270 -2.607  -20.930 1.00 35.97 ? 98  ASP A OD1 1 
ATOM   753  O OD2 . ASP A 1 97  ? 22.517 -3.513  -19.972 1.00 26.83 ? 98  ASP A OD2 1 
ATOM   754  N N   . LYS A 1 98  ? 25.526 -4.066  -15.916 1.00 19.78 ? 99  LYS A N   1 
ATOM   755  C CA  . LYS A 1 98  ? 26.016 -3.800  -14.576 1.00 19.97 ? 99  LYS A CA  1 
ATOM   756  C C   . LYS A 1 98  ? 25.875 -5.063  -13.746 1.00 18.31 ? 99  LYS A C   1 
ATOM   757  O O   . LYS A 1 98  ? 24.991 -5.893  -13.985 1.00 18.39 ? 99  LYS A O   1 
ATOM   758  C CB  . LYS A 1 98  ? 25.201 -2.695  -13.888 1.00 21.94 ? 99  LYS A CB  1 
ATOM   759  C CG  . LYS A 1 98  ? 24.921 -1.479  -14.757 1.00 22.25 ? 99  LYS A CG  1 
ATOM   760  C CD  . LYS A 1 98  ? 24.377 -0.329  -13.945 1.00 25.39 ? 99  LYS A CD  1 
ATOM   761  C CE  . LYS A 1 98  ? 22.951 -0.008  -14.355 1.00 34.52 ? 99  LYS A CE  1 
ATOM   762  N NZ  . LYS A 1 98  ? 22.555 1.353   -13.902 1.00 27.52 ? 99  LYS A NZ  1 
ATOM   763  N N   . VAL A 1 99  ? 26.756 -5.204  -12.762 1.00 17.65 ? 100 VAL A N   1 
ATOM   764  C CA  . VAL A 1 99  ? 26.606 -6.248  -11.757 1.00 19.66 ? 100 VAL A CA  1 
ATOM   765  C C   . VAL A 1 99  ? 26.396 -5.587  -10.407 1.00 18.95 ? 100 VAL A C   1 
ATOM   766  O O   . VAL A 1 99  ? 26.941 -4.516  -10.124 1.00 20.15 ? 100 VAL A O   1 
ATOM   767  C CB  . VAL A 1 99  ? 27.797 -7.230  -11.695 1.00 18.77 ? 100 VAL A CB  1 
ATOM   768  C CG1 . VAL A 1 99  ? 27.812 -8.111  -12.938 1.00 21.28 ? 100 VAL A CG1 1 
ATOM   769  C CG2 . VAL A 1 99  ? 29.114 -6.473  -11.504 1.00 22.58 ? 100 VAL A CG2 1 
ATOM   770  N N   . SER A 1 100 ? 25.599 -6.244  -9.568  1.00 18.31 ? 101 SER A N   1 
ATOM   771  C CA  . SER A 1 100 ? 25.410 -5.817  -8.193  1.00 20.60 ? 101 SER A CA  1 
ATOM   772  C C   . SER A 1 100 ? 26.198 -6.743  -7.279  1.00 18.12 ? 101 SER A C   1 
ATOM   773  O O   . SER A 1 100 ? 26.102 -7.973  -7.392  1.00 19.99 ? 101 SER A O   1 
ATOM   774  C CB  . SER A 1 100 ? 23.928 -5.820  -7.815  1.00 21.04 ? 101 SER A CB  1 
ATOM   775  O OG  . SER A 1 100 ? 23.737 -5.453  -6.457  1.00 28.51 ? 101 SER A OG  1 
ATOM   776  N N   . ILE A 1 101 ? 26.989 -6.149  -6.399  1.00 16.73 ? 102 ILE A N   1 
ATOM   777  C CA  . ILE A 1 101 ? 27.704 -6.873  -5.362  1.00 17.53 ? 102 ILE A CA  1 
ATOM   778  C C   . ILE A 1 101 ? 27.306 -6.291  -4.017  1.00 17.36 ? 102 ILE A C   1 
ATOM   779  O O   . ILE A 1 101 ? 27.004 -5.099  -3.886  1.00 16.26 ? 102 ILE A O   1 
ATOM   780  C CB  . ILE A 1 101 ? 29.235 -6.863  -5.560  1.00 18.65 ? 102 ILE A CB  1 
ATOM   781  C CG1 . ILE A 1 101 ? 29.732 -5.431  -5.730  1.00 19.35 ? 102 ILE A CG1 1 
ATOM   782  C CG2 . ILE A 1 101 ? 29.601 -7.715  -6.762  1.00 23.58 ? 102 ILE A CG2 1 
ATOM   783  C CD1 . ILE A 1 101 ? 31.255 -5.314  -5.818  1.00 22.22 ? 102 ILE A CD1 1 
ATOM   784  N N   . ASN A 1 102 ? 27.312 -7.147  -3.009  1.00 17.25 ? 103 ASN A N   1 
ATOM   785  C CA  . ASN A 1 102 ? 26.890 -6.755  -1.674  1.00 16.17 ? 103 ASN A CA  1 
ATOM   786  C C   . ASN A 1 102 ? 27.790 -7.424  -0.649  1.00 16.13 ? 103 ASN A C   1 
ATOM   787  O O   . ASN A 1 102 ? 28.776 -6.832  -0.198  1.00 17.05 ? 103 ASN A O   1 
ATOM   788  C CB  . ASN A 1 102 ? 25.414 -7.100  -1.458  1.00 19.61 ? 103 ASN A CB  1 
ATOM   789  C CG  . ASN A 1 102 ? 24.896 -6.611  -0.133  1.00 18.23 ? 103 ASN A CG  1 
ATOM   790  O OD1 . ASN A 1 102 ? 25.666 -6.255  0.758   1.00 22.10 ? 103 ASN A OD1 1 
ATOM   791  N ND2 . ASN A 1 102 ? 23.574 -6.570  -0.002  1.00 24.95 ? 103 ASN A ND2 1 
ATOM   792  N N   . THR A 1 103 ? 27.478 -8.676  -0.310  1.00 16.11 ? 104 THR A N   1 
ATOM   793  C CA  . THR A 1 103 ? 28.280 -9.397  0.669   1.00 17.26 ? 104 THR A CA  1 
ATOM   794  C C   . THR A 1 103 ? 29.750 -9.422  0.276   1.00 15.55 ? 104 THR A C   1 
ATOM   795  O O   . THR A 1 103 ? 30.626 -9.186  1.116   1.00 16.82 ? 104 THR A O   1 
ATOM   796  C CB  . THR A 1 103 ? 27.726 -10.808 0.812   1.00 16.93 ? 104 THR A CB  1 
ATOM   797  O OG1 . THR A 1 103 ? 26.375 -10.723 1.294   1.00 19.78 ? 104 THR A OG1 1 
ATOM   798  C CG2 . THR A 1 103 ? 28.563 -11.619 1.792   1.00 19.10 ? 104 THR A CG2 1 
ATOM   799  N N   . ALA A 1 104 ? 30.037 -9.672  -1.002  1.00 17.05 ? 105 ALA A N   1 
ATOM   800  C CA  . ALA A 1 104 ? 31.422 -9.792  -1.432  1.00 17.98 ? 105 ALA A CA  1 
ATOM   801  C C   . ALA A 1 104 ? 32.135 -8.455  -1.367  1.00 19.32 ? 105 ALA A C   1 
ATOM   802  O O   . ALA A 1 104 ? 33.350 -8.412  -1.134  1.00 19.98 ? 105 ALA A O   1 
ATOM   803  C CB  . ALA A 1 104 ? 31.479 -10.348 -2.853  1.00 20.09 ? 105 ALA A CB  1 
ATOM   804  N N   . ALA A 1 105 ? 31.402 -7.359  -1.567  1.00 18.37 ? 106 ALA A N   1 
ATOM   805  C CA  . ALA A 1 105 ? 32.009 -6.033  -1.472  1.00 17.77 ? 106 ALA A CA  1 
ATOM   806  C C   . ALA A 1 105 ? 32.378 -5.693  -0.032  1.00 18.50 ? 106 ALA A C   1 
ATOM   807  O O   . ALA A 1 105 ? 33.451 -5.137  0.224   1.00 19.02 ? 106 ALA A O   1 
ATOM   808  C CB  . ALA A 1 105 ? 31.060 -4.984  -2.048  1.00 22.41 ? 106 ALA A CB  1 
ATOM   809  N N   . VAL A 1 106 ? 31.502 -6.016  0.920   1.00 16.94 ? 107 VAL A N   1 
ATOM   810  C CA  . VAL A 1 106 ? 31.804 -5.787  2.331   1.00 17.63 ? 107 VAL A CA  1 
ATOM   811  C C   . VAL A 1 106 ? 33.031 -6.588  2.749   1.00 18.14 ? 107 VAL A C   1 
ATOM   812  O O   . VAL A 1 106 ? 33.934 -6.075  3.422   1.00 20.27 ? 107 VAL A O   1 
ATOM   813  C CB  . VAL A 1 106 ? 30.583 -6.131  3.205   1.00 15.83 ? 107 VAL A CB  1 
ATOM   814  C CG1 . VAL A 1 106 ? 30.969 -6.099  4.673   1.00 22.01 ? 107 VAL A CG1 1 
ATOM   815  C CG2 . VAL A 1 106 ? 29.427 -5.166  2.911   1.00 19.07 ? 107 VAL A CG2 1 
ATOM   816  N N   . GLU A 1 107 ? 33.083 -7.860  2.355   1.00 19.41 ? 108 GLU A N   1 
ATOM   817  C CA  . GLU A 1 107 ? 34.168 -8.718  2.806   1.00 19.26 ? 108 GLU A CA  1 
ATOM   818  C C   . GLU A 1 107 ? 35.469 -8.448  2.067   1.00 21.13 ? 108 GLU A C   1 
ATOM   819  O O   . GLU A 1 107 ? 36.538 -8.744  2.608   1.00 23.32 ? 108 GLU A O   1 
ATOM   820  C CB  . GLU A 1 107 ? 33.755 -10.188 2.718   1.00 21.68 ? 108 GLU A CB  1 
ATOM   821  C CG  . GLU A 1 107 ? 32.617 -10.492 3.682   1.00 18.76 ? 108 GLU A CG  1 
ATOM   822  C CD  . GLU A 1 107 ? 32.052 -11.900 3.568   1.00 27.29 ? 108 GLU A CD  1 
ATOM   823  O OE1 . GLU A 1 107 ? 32.573 -12.706 2.768   1.00 26.79 ? 108 GLU A OE1 1 
ATOM   824  O OE2 . GLU A 1 107 ? 31.063 -12.197 4.275   1.00 22.04 ? 108 GLU A OE2 1 
ATOM   825  N N   . ASN A 1 108 ? 35.407 -7.874  0.866   1.00 19.20 ? 109 ASN A N   1 
ATOM   826  C CA  . ASN A 1 108 ? 36.609 -7.516  0.108   1.00 20.74 ? 109 ASN A CA  1 
ATOM   827  C C   . ASN A 1 108 ? 36.345 -6.230  -0.666  1.00 18.60 ? 109 ASN A C   1 
ATOM   828  O O   . ASN A 1 108 ? 36.056 -6.258  -1.866  1.00 18.80 ? 109 ASN A O   1 
ATOM   829  C CB  . ASN A 1 108 ? 37.008 -8.648  -0.844  1.00 21.41 ? 109 ASN A CB  1 
ATOM   830  C CG  . ASN A 1 108 ? 38.316 -8.372  -1.571  1.00 23.45 ? 109 ASN A CG  1 
ATOM   831  O OD1 . ASN A 1 108 ? 39.089 -7.500  -1.178  1.00 27.36 ? 109 ASN A OD1 1 
ATOM   832  N ND2 . ASN A 1 108 ? 38.566 -9.123  -2.636  1.00 28.88 ? 109 ASN A ND2 1 
ATOM   833  N N   . PRO A 1 109 ? 36.438 -5.071  -0.003  1.00 17.51 ? 110 PRO A N   1 
ATOM   834  C CA  . PRO A 1 109 ? 36.111 -3.811  -0.694  1.00 17.55 ? 110 PRO A CA  1 
ATOM   835  C C   . PRO A 1 109 ? 36.917 -3.559  -1.960  1.00 19.23 ? 110 PRO A C   1 
ATOM   836  O O   . PRO A 1 109 ? 36.416 -2.892  -2.874  1.00 18.25 ? 110 PRO A O   1 
ATOM   837  C CB  . PRO A 1 109 ? 36.351 -2.737  0.379   1.00 19.49 ? 110 PRO A CB  1 
ATOM   838  C CG  . PRO A 1 109 ? 36.185 -3.461  1.680   1.00 23.58 ? 110 PRO A CG  1 
ATOM   839  C CD  . PRO A 1 109 ? 36.668 -4.870  1.440   1.00 18.65 ? 110 PRO A CD  1 
ATOM   840  N N   . SER A 1 110 ? 38.152 -4.073  -2.045  1.00 19.00 ? 111 SER A N   1 
ATOM   841  C CA  . SER A 1 110 ? 38.954 -3.913  -3.252  1.00 18.89 ? 111 SER A CA  1 
ATOM   842  C C   . SER A 1 110 ? 38.293 -4.528  -4.473  1.00 17.54 ? 111 SER A C   1 
ATOM   843  O O   . SER A 1 110 ? 38.619 -4.140  -5.600  1.00 18.57 ? 111 SER A O   1 
ATOM   844  C CB  . SER A 1 110 ? 40.326 -4.568  -3.056  1.00 19.41 ? 111 SER A CB  1 
ATOM   845  O OG  . SER A 1 110 ? 40.983 -4.011  -1.935  1.00 29.72 ? 111 SER A OG  1 
ATOM   846  N N   . LEU A 1 111 ? 37.369 -5.469  -4.277  1.00 18.07 ? 112 LEU A N   1 
ATOM   847  C CA  . LEU A 1 111 ? 36.651 -6.046  -5.403  1.00 17.61 ? 112 LEU A CA  1 
ATOM   848  C C   . LEU A 1 111 ? 35.888 -4.979  -6.173  1.00 18.45 ? 112 LEU A C   1 
ATOM   849  O O   . LEU A 1 111 ? 35.783 -5.054  -7.404  1.00 18.47 ? 112 LEU A O   1 
ATOM   850  C CB  . LEU A 1 111 ? 35.683 -7.110  -4.896  1.00 19.02 ? 112 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 111 ? 34.790 -7.774  -5.944  1.00 22.64 ? 112 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 111 ? 35.630 -8.450  -7.017  1.00 22.80 ? 112 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 111 ? 33.857 -8.778  -5.278  1.00 23.58 ? 112 LEU A CD2 1 
ATOM   854  N N   . ILE A 1 112 ? 35.357 -3.972  -5.466  1.00 16.61 ? 113 ILE A N   1 
ATOM   855  C CA  . ILE A 1 112 ? 34.675 -2.867  -6.132  1.00 17.58 ? 113 ILE A CA  1 
ATOM   856  C C   . ILE A 1 112 ? 35.615 -2.215  -7.130  1.00 19.30 ? 113 ILE A C   1 
ATOM   857  O O   . ILE A 1 112 ? 35.265 -1.988  -8.297  1.00 18.70 ? 113 ILE A O   1 
ATOM   858  C CB  . ILE A 1 112 ? 34.196 -1.830  -5.101  1.00 17.06 ? 113 ILE A CB  1 
ATOM   859  C CG1 . ILE A 1 112 ? 33.213 -2.446  -4.103  1.00 18.78 ? 113 ILE A CG1 1 
ATOM   860  C CG2 . ILE A 1 112 ? 33.575 -0.617  -5.811  1.00 18.44 ? 113 ILE A CG2 1 
ATOM   861  C CD1 . ILE A 1 112 ? 32.993 -1.572  -2.882  1.00 15.80 ? 113 ILE A CD1 1 
ATOM   862  N N   . THR A 1 113 ? 36.827 -1.895  -6.669  1.00 16.79 ? 114 THR A N   1 
ATOM   863  C CA  . THR A 1 113 ? 37.811 -1.225  -7.511  1.00 19.47 ? 114 THR A CA  1 
ATOM   864  C C   . THR A 1 113 ? 38.238 -2.099  -8.678  1.00 19.02 ? 114 THR A C   1 
ATOM   865  O O   . THR A 1 113 ? 38.371 -1.612  -9.804  1.00 18.61 ? 114 THR A O   1 
ATOM   866  C CB  . THR A 1 113 ? 39.012 -0.854  -6.656  1.00 18.67 ? 114 THR A CB  1 
ATOM   867  O OG1 . THR A 1 113 ? 38.562 -0.279  -5.423  1.00 19.08 ? 114 THR A OG1 1 
ATOM   868  C CG2 . THR A 1 113 ? 39.911 0.138   -7.395  1.00 18.66 ? 114 THR A CG2 1 
ATOM   869  N N   . GLN A 1 114 ? 38.451 -3.391  -8.438  1.00 17.52 ? 115 GLN A N   1 
ATOM   870  C CA  . GLN A 1 114 ? 38.875 -4.269  -9.523  1.00 20.20 ? 115 GLN A CA  1 
ATOM   871  C C   . GLN A 1 114 ? 37.856 -4.297  -10.653 1.00 20.60 ? 115 GLN A C   1 
ATOM   872  O O   . GLN A 1 114 ? 38.224 -4.220  -11.831 1.00 21.78 ? 115 GLN A O   1 
ATOM   873  C CB  . GLN A 1 114 ? 39.140 -5.676  -8.995  1.00 19.48 ? 115 GLN A CB  1 
ATOM   874  C CG  . GLN A 1 114 ? 40.181 -5.705  -7.890  1.00 18.52 ? 115 GLN A CG  1 
ATOM   875  C CD  . GLN A 1 114 ? 40.345 -7.073  -7.281  1.00 21.49 ? 115 GLN A CD  1 
ATOM   876  O OE1 . GLN A 1 114 ? 39.865 -8.067  -7.822  1.00 23.09 ? 115 GLN A OE1 1 
ATOM   877  N NE2 . GLN A 1 114 ? 41.048 -7.140  -6.156  1.00 26.35 ? 115 GLN A NE2 1 
ATOM   878  N N   . ILE A 1 115 ? 36.568 -4.409  -10.322 1.00 20.24 ? 116 ILE A N   1 
ATOM   879  C CA  . ILE A 1 115 ? 35.555 -4.438  -11.368 1.00 19.80 ? 116 ILE A CA  1 
ATOM   880  C C   . ILE A 1 115 ? 35.444 -3.077  -12.040 1.00 18.88 ? 116 ILE A C   1 
ATOM   881  O O   . ILE A 1 115 ? 35.360 -2.985  -13.271 1.00 23.11 ? 116 ILE A O   1 
ATOM   882  C CB  . ILE A 1 115 ? 34.202 -4.908  -10.806 1.00 20.09 ? 116 ILE A CB  1 
ATOM   883  C CG1 . ILE A 1 115 ? 34.330 -6.234  -10.067 1.00 21.73 ? 116 ILE A CG1 1 
ATOM   884  C CG2 . ILE A 1 115 ? 33.177 -5.047  -11.936 1.00 24.02 ? 116 ILE A CG2 1 
ATOM   885  C CD1 . ILE A 1 115 ? 33.074 -6.563  -9.252  1.00 23.39 ? 116 ILE A CD1 1 
ATOM   886  N N   . ALA A 1 116 ? 35.452 -2.003  -11.249 1.00 18.87 ? 117 ALA A N   1 
ATOM   887  C CA  . ALA A 1 116 ? 35.302 -0.662  -11.804 1.00 19.78 ? 117 ALA A CA  1 
ATOM   888  C C   . ALA A 1 116 ? 36.449 -0.308  -12.748 1.00 23.66 ? 117 ALA A C   1 
ATOM   889  O O   . ALA A 1 116 ? 36.237 0.351   -13.771 1.00 23.80 ? 117 ALA A O   1 
ATOM   890  C CB  . ALA A 1 116 ? 35.210 0.365   -10.676 1.00 22.97 ? 117 ALA A CB  1 
ATOM   891  N N   . GLN A 1 117 ? 37.676 -0.720  -12.418 1.00 23.80 ? 118 GLN A N   1 
ATOM   892  C CA  . GLN A 1 117 ? 38.803 -0.363  -13.272 1.00 25.79 ? 118 GLN A CA  1 
ATOM   893  C C   . GLN A 1 117 ? 38.811 -1.177  -14.555 1.00 28.40 ? 118 GLN A C   1 
ATOM   894  O O   . GLN A 1 117 ? 39.321 -0.712  -15.581 1.00 34.01 ? 118 GLN A O   1 
ATOM   895  C CB  . GLN A 1 117 ? 40.117 -0.531  -12.515 1.00 26.84 ? 118 GLN A CB  1 
ATOM   896  C CG  . GLN A 1 117 ? 40.292 0.441   -11.362 1.00 27.88 ? 118 GLN A CG  1 
ATOM   897  C CD  . GLN A 1 117 ? 40.512 1.868   -11.819 1.00 34.43 ? 118 GLN A CD  1 
ATOM   898  O OE1 . GLN A 1 117 ? 40.877 2.116   -12.968 1.00 33.46 ? 118 GLN A OE1 1 
ATOM   899  N NE2 . GLN A 1 117 ? 40.283 2.817   -10.919 1.00 34.01 ? 118 GLN A NE2 1 
ATOM   900  N N   . THR A 1 118 ? 38.258 -2.385  -14.518 1.00 23.26 ? 119 THR A N   1 
ATOM   901  C CA  . THR A 1 118 ? 38.229 -3.235  -15.700 1.00 23.98 ? 119 THR A CA  1 
ATOM   902  C C   . THR A 1 118 ? 37.116 -2.816  -16.653 1.00 31.45 ? 119 THR A C   1 
ATOM   903  O O   . THR A 1 118 ? 37.326 -2.730  -17.866 1.00 30.37 ? 119 THR A O   1 
ATOM   904  C CB  . THR A 1 118 ? 38.057 -4.699  -15.289 1.00 28.19 ? 119 THR A CB  1 
ATOM   905  O OG1 . THR A 1 118 ? 39.119 -5.087  -14.405 1.00 28.16 ? 119 THR A OG1 1 
ATOM   906  C CG2 . THR A 1 118 ? 38.070 -5.599  -16.512 1.00 28.83 ? 119 THR A CG2 1 
ATOM   907  N N   . PHE A 1 119 ? 35.926 -2.539  -16.116 1.00 27.92 ? 120 PHE A N   1 
ATOM   908  C CA  . PHE A 1 119 ? 34.731 -2.350  -16.926 1.00 27.37 ? 120 PHE A CA  1 
ATOM   909  C C   . PHE A 1 119 ? 34.122 -0.963  -16.822 1.00 29.64 ? 120 PHE A C   1 
ATOM   910  O O   . PHE A 1 119 ? 33.089 -0.713  -17.455 1.00 33.91 ? 120 PHE A O   1 
ATOM   911  C CB  . PHE A 1 119 ? 33.660 -3.386  -16.550 1.00 27.02 ? 120 PHE A CB  1 
ATOM   912  C CG  . PHE A 1 119 ? 34.095 -4.810  -16.741 1.00 28.61 ? 120 PHE A CG  1 
ATOM   913  C CD1 . PHE A 1 119 ? 34.113 -5.377  -18.006 1.00 30.95 ? 120 PHE A CD1 1 
ATOM   914  C CD2 . PHE A 1 119 ? 34.479 -5.584  -15.660 1.00 25.32 ? 120 PHE A CD2 1 
ATOM   915  C CE1 . PHE A 1 119 ? 34.509 -6.684  -18.188 1.00 31.31 ? 120 PHE A CE1 1 
ATOM   916  C CE2 . PHE A 1 119 ? 34.874 -6.890  -15.835 1.00 30.92 ? 120 PHE A CE2 1 
ATOM   917  C CZ  . PHE A 1 119 ? 34.894 -7.441  -17.102 1.00 30.60 ? 120 PHE A CZ  1 
ATOM   918  N N   . GLY A 1 120 ? 34.717 -0.065  -16.055 1.00 24.26 ? 121 GLY A N   1 
ATOM   919  C CA  . GLY A 1 120 ? 34.152 1.243   -15.766 1.00 26.10 ? 121 GLY A CA  1 
ATOM   920  C C   . GLY A 1 120 ? 33.268 1.205   -14.535 1.00 20.28 ? 121 GLY A C   1 
ATOM   921  O O   . GLY A 1 120 ? 32.613 0.208   -14.234 1.00 22.74 ? 121 GLY A O   1 
ATOM   922  N N   . SER A 1 121 ? 33.274 2.317   -13.795 1.00 22.36 ? 122 SER A N   1 
ATOM   923  C CA  . SER A 1 121 ? 32.458 2.400   -12.585 1.00 19.91 ? 122 SER A CA  1 
ATOM   924  C C   . SER A 1 121 ? 30.979 2.206   -12.887 1.00 25.63 ? 122 SER A C   1 
ATOM   925  O O   . SER A 1 121 ? 30.245 1.671   -12.050 1.00 22.77 ? 122 SER A O   1 
ATOM   926  C CB  . SER A 1 121 ? 32.684 3.734   -11.877 1.00 21.45 ? 122 SER A CB  1 
ATOM   927  O OG  A SER A 1 121 ? 33.980 3.775   -11.285 0.85 26.94 ? 122 SER A OG  1 
ATOM   928  O OG  B SER A 1 121 ? 32.388 4.820   -12.736 0.15 26.03 ? 122 SER A OG  1 
ATOM   929  N N   . GLN A 1 122 ? 30.529 2.599   -14.082 1.00 23.21 ? 123 GLN A N   1 
ATOM   930  C CA  . GLN A 1 122 ? 29.121 2.443   -14.438 1.00 22.71 ? 123 GLN A CA  1 
ATOM   931  C C   . GLN A 1 122 ? 28.665 0.988   -14.401 1.00 26.51 ? 123 GLN A C   1 
ATOM   932  O O   . GLN A 1 122 ? 27.464 0.725   -14.266 1.00 26.37 ? 123 GLN A O   1 
ATOM   933  C CB  . GLN A 1 122 ? 28.865 3.052   -15.819 1.00 27.42 ? 123 GLN A CB  1 
ATOM   934  C CG  . GLN A 1 122 ? 29.109 2.097   -16.984 1.00 33.81 ? 123 GLN A CG  1 
ATOM   935  C CD  . GLN A 1 122 ? 30.590 1.886   -17.278 1.00 38.20 ? 123 GLN A CD  1 
ATOM   936  O OE1 . GLN A 1 122 ? 31.424 2.745   -16.987 1.00 34.86 ? 123 GLN A OE1 1 
ATOM   937  N NE2 . GLN A 1 122 ? 30.919 0.735   -17.859 1.00 36.51 ? 123 GLN A NE2 1 
ATOM   938  N N   . ALA A 1 123 ? 29.585 0.037   -14.509 1.00 23.58 ? 124 ALA A N   1 
ATOM   939  C CA  . ALA A 1 123 ? 29.232 -1.373  -14.481 1.00 20.15 ? 124 ALA A CA  1 
ATOM   940  C C   . ALA A 1 123 ? 29.086 -1.927  -13.069 1.00 17.37 ? 124 ALA A C   1 
ATOM   941  O O   . ALA A 1 123 ? 28.730 -3.100  -12.921 1.00 22.43 ? 124 ALA A O   1 
ATOM   942  C CB  . ALA A 1 123 ? 30.283 -2.187  -15.248 1.00 24.20 ? 124 ALA A CB  1 
ATOM   943  N N   . VAL A 1 124 ? 29.353 -1.131  -12.038 1.00 20.57 ? 125 VAL A N   1 
ATOM   944  C CA  . VAL A 1 124 ? 29.412 -1.615  -10.663 1.00 17.83 ? 125 VAL A CA  1 
ATOM   945  C C   . VAL A 1 124 ? 28.306 -0.964  -9.853  1.00 20.77 ? 125 VAL A C   1 
ATOM   946  O O   . VAL A 1 124 ? 28.323 0.252   -9.618  1.00 21.96 ? 125 VAL A O   1 
ATOM   947  C CB  . VAL A 1 124 ? 30.772 -1.347  -10.010 1.00 21.53 ? 125 VAL A CB  1 
ATOM   948  C CG1 . VAL A 1 124 ? 30.793 -1.935  -8.612  1.00 23.47 ? 125 VAL A CG1 1 
ATOM   949  C CG2 . VAL A 1 124 ? 31.883 -1.927  -10.854 1.00 26.64 ? 125 VAL A CG2 1 
ATOM   950  N N   . VAL A 1 125 ? 27.368 -1.782  -9.393  1.00 17.57 ? 126 VAL A N   1 
ATOM   951  C CA  . VAL A 1 125 ? 26.357 -1.377  -8.426  1.00 18.20 ? 126 VAL A CA  1 
ATOM   952  C C   . VAL A 1 125 ? 26.708 -2.052  -7.112  1.00 17.36 ? 126 VAL A C   1 
ATOM   953  O O   . VAL A 1 125 ? 26.870 -3.276  -7.063  1.00 18.06 ? 126 VAL A O   1 
ATOM   954  C CB  . VAL A 1 125 ? 24.957 -1.807  -8.896  1.00 18.80 ? 126 VAL A CB  1 
ATOM   955  C CG1 . VAL A 1 125 ? 23.896 -1.530  -7.818  1.00 19.73 ? 126 VAL A CG1 1 
ATOM   956  C CG2 . VAL A 1 125 ? 24.606 -1.130  -10.219 1.00 18.45 ? 126 VAL A CG2 1 
ATOM   957  N N   . VAL A 1 126 ? 26.845 -1.275  -6.054  1.00 15.88 ? 127 VAL A N   1 
ATOM   958  C CA  . VAL A 1 126 ? 26.948 -1.847  -4.719  1.00 15.49 ? 127 VAL A CA  1 
ATOM   959  C C   . VAL A 1 126 ? 25.571 -1.789  -4.071  1.00 15.15 ? 127 VAL A C   1 
ATOM   960  O O   . VAL A 1 126 ? 25.015 -0.705  -3.853  1.00 15.75 ? 127 VAL A O   1 
ATOM   961  C CB  . VAL A 1 126 ? 28.028 -1.158  -3.874  1.00 16.90 ? 127 VAL A CB  1 
ATOM   962  C CG1 . VAL A 1 126 ? 28.041 -1.746  -2.466  1.00 17.07 ? 127 VAL A CG1 1 
ATOM   963  C CG2 . VAL A 1 126 ? 29.394 -1.314  -4.548  1.00 19.16 ? 127 VAL A CG2 1 
ATOM   964  N N   . ALA A 1 127 ? 25.010 -2.958  -3.799  1.00 15.32 ? 128 ALA A N   1 
ATOM   965  C CA  . ALA A 1 127 ? 23.761 -3.048  -3.066  1.00 15.28 ? 128 ALA A CA  1 
ATOM   966  C C   . ALA A 1 127 ? 24.081 -2.992  -1.583  1.00 17.58 ? 128 ALA A C   1 
ATOM   967  O O   . ALA A 1 127 ? 24.952 -3.722  -1.095  1.00 17.57 ? 128 ALA A O   1 
ATOM   968  C CB  . ALA A 1 127 ? 23.060 -4.359  -3.408  1.00 16.58 ? 128 ALA A CB  1 
ATOM   969  N N   . ILE A 1 128 ? 23.412 -2.092  -0.878  1.00 15.73 ? 129 ILE A N   1 
ATOM   970  C CA  . ILE A 1 128 ? 23.575 -1.922  0.561   1.00 14.55 ? 129 ILE A CA  1 
ATOM   971  C C   . ILE A 1 128 ? 22.216 -2.164  1.193   1.00 18.93 ? 129 ILE A C   1 
ATOM   972  O O   . ILE A 1 128 ? 21.256 -1.437  0.910   1.00 17.47 ? 129 ILE A O   1 
ATOM   973  C CB  . ILE A 1 128 ? 24.097 -0.525  0.927   1.00 15.95 ? 129 ILE A CB  1 
ATOM   974  C CG1 . ILE A 1 128 ? 25.436 -0.269  0.243   1.00 15.97 ? 129 ILE A CG1 1 
ATOM   975  C CG2 . ILE A 1 128 ? 24.239 -0.409  2.428   1.00 20.26 ? 129 ILE A CG2 1 
ATOM   976  C CD1 . ILE A 1 128 ? 25.997 1.123   0.510   1.00 18.46 ? 129 ILE A CD1 1 
ATOM   977  N N   . ASP A 1 129 ? 22.127 -3.194  2.021   1.00 17.23 ? 130 ASP A N   1 
ATOM   978  C CA  . ASP A 1 129 ? 20.938 -3.464  2.814   1.00 16.10 ? 130 ASP A CA  1 
ATOM   979  C C   . ASP A 1 129 ? 21.199 -2.942  4.219   1.00 16.86 ? 130 ASP A C   1 
ATOM   980  O O   . ASP A 1 129 ? 22.194 -3.315  4.851   1.00 17.61 ? 130 ASP A O   1 
ATOM   981  C CB  . ASP A 1 129 ? 20.655 -4.967  2.850   1.00 17.42 ? 130 ASP A CB  1 
ATOM   982  C CG  . ASP A 1 129 ? 20.449 -5.557  1.467   1.00 21.31 ? 130 ASP A CG  1 
ATOM   983  O OD1 . ASP A 1 129 ? 19.979 -4.835  0.569   1.00 25.55 ? 130 ASP A OD1 1 
ATOM   984  O OD2 . ASP A 1 129 ? 20.727 -6.761  1.273   1.00 22.56 ? 130 ASP A OD2 1 
ATOM   985  N N   . ALA A 1 130 ? 20.338 -2.049  4.695   1.00 14.86 ? 131 ALA A N   1 
ATOM   986  C CA  . ALA A 1 130 ? 20.597 -1.402  5.969   1.00 15.12 ? 131 ALA A CA  1 
ATOM   987  C C   . ALA A 1 130 ? 19.363 -1.438  6.858   1.00 14.66 ? 131 ALA A C   1 
ATOM   988  O O   . ALA A 1 130 ? 18.228 -1.494  6.381   1.00 16.77 ? 131 ALA A O   1 
ATOM   989  C CB  . ALA A 1 130 ? 21.086 0.044   5.789   1.00 15.90 ? 131 ALA A CB  1 
ATOM   990  N N   . LYS A 1 131 ? 19.618 -1.377  8.161   1.00 17.52 ? 132 LYS A N   1 
ATOM   991  C CA  . LYS A 1 131 ? 18.582 -1.454  9.174   1.00 20.61 ? 132 LYS A CA  1 
ATOM   992  C C   . LYS A 1 131 ? 19.024 -0.654  10.392  1.00 17.93 ? 132 LYS A C   1 
ATOM   993  O O   . LYS A 1 131 ? 20.216 -0.552  10.689  1.00 19.55 ? 132 LYS A O   1 
ATOM   994  C CB  . LYS A 1 131 ? 18.357 -2.929  9.546   1.00 23.56 ? 132 LYS A CB  1 
ATOM   995  C CG  . LYS A 1 131 ? 17.391 -3.187  10.680  1.00 28.64 ? 132 LYS A CG  1 
ATOM   996  C CD  . LYS A 1 131 ? 17.630 -4.568  11.271  1.00 35.75 ? 132 LYS A CD  1 
ATOM   997  C CE  . LYS A 1 131 ? 17.494 -5.630  10.195  1.00 40.23 ? 132 LYS A CE  1 
ATOM   998  N NZ  . LYS A 1 131 ? 16.720 -6.814  10.655  1.00 44.07 ? 132 LYS A NZ  1 
ATOM   999  N N   . ARG A 1 132 ? 18.047 -0.097  11.104  1.00 19.46 ? 133 ARG A N   1 
ATOM   1000 C CA  . ARG A 1 132 ? 18.330 0.573   12.364  1.00 19.05 ? 133 ARG A CA  1 
ATOM   1001 C C   . ARG A 1 132 ? 18.678 -0.454  13.434  1.00 18.56 ? 133 ARG A C   1 
ATOM   1002 O O   . ARG A 1 132 ? 17.905 -1.388  13.681  1.00 20.88 ? 133 ARG A O   1 
ATOM   1003 C CB  . ARG A 1 132 ? 17.093 1.343   12.813  1.00 22.08 ? 133 ARG A CB  1 
ATOM   1004 C CG  . ARG A 1 132 ? 16.768 2.543   11.972  1.00 21.38 ? 133 ARG A CG  1 
ATOM   1005 C CD  . ARG A 1 132 ? 15.288 2.857   12.034  1.00 23.69 ? 133 ARG A CD  1 
ATOM   1006 N NE  . ARG A 1 132 ? 14.969 4.024   11.218  1.00 20.65 ? 133 ARG A NE  1 
ATOM   1007 C CZ  . ARG A 1 132 ? 14.647 3.974   9.929   1.00 21.97 ? 133 ARG A CZ  1 
ATOM   1008 N NH1 . ARG A 1 132 ? 14.583 2.807   9.291   1.00 19.96 ? 133 ARG A NH1 1 
ATOM   1009 N NH2 . ARG A 1 132 ? 14.384 5.101   9.277   1.00 21.05 ? 133 ARG A NH2 1 
ATOM   1010 N N   . VAL A 1 133 ? 19.835 -0.273  14.072  1.00 20.17 ? 134 VAL A N   1 
ATOM   1011 C CA  . VAL A 1 133 ? 20.281 -1.113  15.185  1.00 20.96 ? 134 VAL A CA  1 
ATOM   1012 C C   . VAL A 1 133 ? 20.840 -0.197  16.263  1.00 22.20 ? 134 VAL A C   1 
ATOM   1013 O O   . VAL A 1 133 ? 21.784 0.556   16.007  1.00 24.02 ? 134 VAL A O   1 
ATOM   1014 C CB  . VAL A 1 133 ? 21.364 -2.130  14.774  1.00 21.51 ? 134 VAL A CB  1 
ATOM   1015 C CG1 . VAL A 1 133 ? 21.763 -2.970  15.979  1.00 27.46 ? 134 VAL A CG1 1 
ATOM   1016 C CG2 . VAL A 1 133 ? 20.887 -3.014  13.637  1.00 23.90 ? 134 VAL A CG2 1 
ATOM   1017 N N   . ASP A 1 134 ? 20.260 -0.258  17.465  1.00 25.97 ? 135 ASP A N   1 
ATOM   1018 C CA  . ASP A 1 134 ? 20.777 0.472   18.628  1.00 30.85 ? 135 ASP A CA  1 
ATOM   1019 C C   . ASP A 1 134 ? 20.997 1.959   18.335  1.00 28.04 ? 135 ASP A C   1 
ATOM   1020 O O   . ASP A 1 134 ? 21.933 2.580   18.846  1.00 36.65 ? 135 ASP A O   1 
ATOM   1021 C CB  . ASP A 1 134 ? 22.037 -0.182  19.200  1.00 30.65 ? 135 ASP A CB  1 
ATOM   1022 C CG  . ASP A 1 134 ? 21.803 -1.621  19.639  1.00 34.96 ? 135 ASP A CG  1 
ATOM   1023 O OD1 . ASP A 1 134 ? 20.630 -2.013  19.826  1.00 34.85 ? 135 ASP A OD1 1 
ATOM   1024 O OD2 . ASP A 1 134 ? 22.795 -2.362  19.801  1.00 39.35 ? 135 ASP A OD2 1 
ATOM   1025 N N   . GLY A 1 135 ? 20.139 2.536   17.501  1.00 23.56 ? 136 GLY A N   1 
ATOM   1026 C CA  . GLY A 1 135 ? 20.161 3.958   17.235  1.00 27.24 ? 136 GLY A CA  1 
ATOM   1027 C C   . GLY A 1 135 ? 20.959 4.392   16.028  1.00 31.19 ? 136 GLY A C   1 
ATOM   1028 O O   . GLY A 1 135 ? 21.126 5.599   15.823  1.00 27.51 ? 136 GLY A O   1 
ATOM   1029 N N   . GLU A 1 136 ? 21.460 3.455   15.224  1.00 25.65 ? 137 GLU A N   1 
ATOM   1030 C CA  . GLU A 1 136 ? 22.276 3.795   14.067  1.00 24.81 ? 137 GLU A CA  1 
ATOM   1031 C C   . GLU A 1 136 ? 21.884 2.912   12.892  1.00 22.88 ? 137 GLU A C   1 
ATOM   1032 O O   . GLU A 1 136 ? 21.485 1.758   13.073  1.00 22.12 ? 137 GLU A O   1 
ATOM   1033 C CB  A GLU A 1 136 ? 23.765 3.570   14.359  0.40 30.96 ? 137 GLU A CB  1 
ATOM   1034 C CB  B GLU A 1 136 ? 23.767 3.617   14.369  0.60 31.00 ? 137 GLU A CB  1 
ATOM   1035 C CG  A GLU A 1 136 ? 24.297 4.284   15.596  0.40 34.84 ? 137 GLU A CG  1 
ATOM   1036 C CG  B GLU A 1 136 ? 24.293 4.528   15.470  0.60 34.70 ? 137 GLU A CG  1 
ATOM   1037 C CD  A GLU A 1 136 ? 25.650 3.752   16.039  0.40 34.65 ? 137 GLU A CD  1 
ATOM   1038 C CD  B GLU A 1 136 ? 24.473 5.958   15.008  0.60 35.69 ? 137 GLU A CD  1 
ATOM   1039 O OE1 A GLU A 1 136 ? 25.710 2.610   16.543  0.40 39.69 ? 137 GLU A OE1 1 
ATOM   1040 O OE1 B GLU A 1 136 ? 24.492 6.866   15.869  0.60 39.71 ? 137 GLU A OE1 1 
ATOM   1041 O OE2 A GLU A 1 136 ? 26.655 4.474   15.884  0.40 40.48 ? 137 GLU A OE2 1 
ATOM   1042 O OE2 B GLU A 1 136 ? 24.600 6.175   13.785  0.60 36.34 ? 137 GLU A OE2 1 
ATOM   1043 N N   . PHE A 1 137 ? 22.027 3.450   11.680  1.00 19.02 ? 138 PHE A N   1 
ATOM   1044 C CA  . PHE A 1 137 ? 21.849 2.636   10.482  1.00 18.28 ? 138 PHE A CA  1 
ATOM   1045 C C   . PHE A 1 137 ? 23.055 1.721   10.311  1.00 18.01 ? 138 PHE A C   1 
ATOM   1046 O O   . PHE A 1 137 ? 24.193 2.193   10.231  1.00 17.76 ? 138 PHE A O   1 
ATOM   1047 C CB  . PHE A 1 137 ? 21.730 3.530   9.255   1.00 18.80 ? 138 PHE A CB  1 
ATOM   1048 C CG  . PHE A 1 137 ? 20.451 4.300   9.179   1.00 19.05 ? 138 PHE A CG  1 
ATOM   1049 C CD1 . PHE A 1 137 ? 19.238 3.647   9.122   1.00 18.12 ? 138 PHE A CD1 1 
ATOM   1050 C CD2 . PHE A 1 137 ? 20.462 5.685   9.120   1.00 20.91 ? 138 PHE A CD2 1 
ATOM   1051 C CE1 . PHE A 1 137 ? 18.056 4.349   9.028   1.00 23.15 ? 138 PHE A CE1 1 
ATOM   1052 C CE2 . PHE A 1 137 ? 19.269 6.398   9.028   1.00 21.28 ? 138 PHE A CE2 1 
ATOM   1053 C CZ  . PHE A 1 137 ? 18.072 5.726   8.982   1.00 23.68 ? 138 PHE A CZ  1 
ATOM   1054 N N   A MET A 1 138 ? 22.810 0.410   10.267  0.56 16.85 ? 139 MET A N   1 
ATOM   1055 N N   B MET A 1 138 ? 22.803 0.418   10.229  0.44 16.89 ? 139 MET A N   1 
ATOM   1056 C CA  A MET A 1 138 ? 23.867 -0.583  10.143  0.56 19.22 ? 139 MET A CA  1 
ATOM   1057 C CA  B MET A 1 138 ? 23.856 -0.579  10.143  0.44 19.20 ? 139 MET A CA  1 
ATOM   1058 C C   A MET A 1 138 ? 23.735 -1.351  8.835   0.56 15.74 ? 139 MET A C   1 
ATOM   1059 C C   B MET A 1 138 ? 23.731 -1.374  8.849   0.44 15.76 ? 139 MET A C   1 
ATOM   1060 O O   A MET A 1 138 ? 22.629 -1.568  8.331   0.56 16.72 ? 139 MET A O   1 
ATOM   1061 O O   B MET A 1 138 ? 22.625 -1.622  8.360   0.44 16.71 ? 139 MET A O   1 
ATOM   1062 C CB  A MET A 1 138 ? 23.818 -1.588  11.294  0.56 19.16 ? 139 MET A CB  1 
ATOM   1063 C CB  B MET A 1 138 ? 23.767 -1.534  11.328  0.44 19.19 ? 139 MET A CB  1 
ATOM   1064 C CG  A MET A 1 138 ? 23.883 -0.948  12.652  0.56 19.56 ? 139 MET A CG  1 
ATOM   1065 C CG  B MET A 1 138 ? 24.991 -2.384  11.521  0.44 24.36 ? 139 MET A CG  1 
ATOM   1066 S SD  A MET A 1 138 ? 25.449 -0.099  12.872  0.56 25.66 ? 139 MET A SD  1 
ATOM   1067 S SD  B MET A 1 138 ? 26.382 -1.476  12.207  0.44 32.32 ? 139 MET A SD  1 
ATOM   1068 C CE  A MET A 1 138 ? 26.579 -1.413  12.463  0.56 31.02 ? 139 MET A CE  1 
ATOM   1069 C CE  B MET A 1 138 ? 25.553 -0.330  13.300  0.44 28.36 ? 139 MET A CE  1 
ATOM   1070 N N   . VAL A 1 139 ? 24.882 -1.783  8.306   1.00 16.50 ? 140 VAL A N   1 
ATOM   1071 C CA  . VAL A 1 139 ? 24.945 -2.552  7.059   1.00 16.49 ? 140 VAL A CA  1 
ATOM   1072 C C   . VAL A 1 139 ? 24.811 -4.041  7.366   1.00 14.54 ? 140 VAL A C   1 
ATOM   1073 O O   . VAL A 1 139 ? 25.484 -4.559  8.266   1.00 16.57 ? 140 VAL A O   1 
ATOM   1074 C CB  . VAL A 1 139 ? 26.270 -2.277  6.322   1.00 15.48 ? 140 VAL A CB  1 
ATOM   1075 C CG1 . VAL A 1 139 ? 26.382 -3.148  5.073   1.00 19.71 ? 140 VAL A CG1 1 
ATOM   1076 C CG2 . VAL A 1 139 ? 26.381 -0.788  5.955   1.00 16.14 ? 140 VAL A CG2 1 
ATOM   1077 N N   . PHE A 1 140 ? 23.947 -4.727  6.616   1.00 14.76 ? 141 PHE A N   1 
ATOM   1078 C CA  . PHE A 1 140 ? 23.700 -6.159  6.777   1.00 15.84 ? 141 PHE A CA  1 
ATOM   1079 C C   . PHE A 1 140 ? 24.063 -6.886  5.493   1.00 17.80 ? 141 PHE A C   1 
ATOM   1080 O O   . PHE A 1 140 ? 23.720 -6.432  4.400   1.00 18.19 ? 141 PHE A O   1 
ATOM   1081 C CB  . PHE A 1 140 ? 22.215 -6.431  7.105   1.00 15.90 ? 141 PHE A CB  1 
ATOM   1082 C CG  . PHE A 1 140 ? 21.864 -6.194  8.542   1.00 15.33 ? 141 PHE A CG  1 
ATOM   1083 C CD1 . PHE A 1 140 ? 21.883 -4.917  9.078   1.00 17.88 ? 141 PHE A CD1 1 
ATOM   1084 C CD2 . PHE A 1 140 ? 21.527 -7.259  9.371   1.00 17.60 ? 141 PHE A CD2 1 
ATOM   1085 C CE1 . PHE A 1 140 ? 21.573 -4.706  10.414  1.00 20.51 ? 141 PHE A CE1 1 
ATOM   1086 C CE2 . PHE A 1 140 ? 21.221 -7.052  10.700  1.00 19.40 ? 141 PHE A CE2 1 
ATOM   1087 C CZ  . PHE A 1 140 ? 21.241 -5.780  11.225  1.00 20.87 ? 141 PHE A CZ  1 
ATOM   1088 N N   . THR A 1 141 ? 24.715 -8.044  5.628   1.00 17.25 ? 142 THR A N   1 
ATOM   1089 C CA  . THR A 1 141 ? 25.063 -8.899  4.502   1.00 15.48 ? 142 THR A CA  1 
ATOM   1090 C C   . THR A 1 141 ? 24.260 -10.193 4.583   1.00 17.42 ? 142 THR A C   1 
ATOM   1091 O O   . THR A 1 141 ? 23.436 -10.374 5.483   1.00 17.41 ? 142 THR A O   1 
ATOM   1092 C CB  . THR A 1 141 ? 26.556 -9.209  4.512   1.00 15.82 ? 142 THR A CB  1 
ATOM   1093 O OG1 . THR A 1 141 ? 26.939 -9.594  5.837   1.00 17.43 ? 142 THR A OG1 1 
ATOM   1094 C CG2 . THR A 1 141 ? 27.364 -7.970  4.086   1.00 18.03 ? 142 THR A CG2 1 
ATOM   1095 N N   . TYR A 1 142 ? 24.515 -11.091 3.628   1.00 17.52 ? 143 TYR A N   1 
ATOM   1096 C CA  . TYR A 1 142 ? 23.833 -12.390 3.534   1.00 17.47 ? 143 TYR A CA  1 
ATOM   1097 C C   . TYR A 1 142 ? 22.313 -12.240 3.551   1.00 20.77 ? 143 TYR A C   1 
ATOM   1098 O O   . TYR A 1 142 ? 21.620 -12.738 4.439   1.00 20.13 ? 143 TYR A O   1 
ATOM   1099 C CB  . TYR A 1 142 ? 24.329 -13.383 4.589   1.00 21.95 ? 143 TYR A CB  1 
ATOM   1100 C CG  . TYR A 1 142 ? 25.784 -13.696 4.396   1.00 20.09 ? 143 TYR A CG  1 
ATOM   1101 C CD1 . TYR A 1 142 ? 26.192 -14.698 3.519   1.00 21.90 ? 143 TYR A CD1 1 
ATOM   1102 C CD2 . TYR A 1 142 ? 26.760 -12.969 5.061   1.00 17.34 ? 143 TYR A CD2 1 
ATOM   1103 C CE1 . TYR A 1 142 ? 27.534 -14.965 3.321   1.00 20.92 ? 143 TYR A CE1 1 
ATOM   1104 C CE2 . TYR A 1 142 ? 28.097 -13.228 4.873   1.00 19.47 ? 143 TYR A CE2 1 
ATOM   1105 C CZ  . TYR A 1 142 ? 28.483 -14.231 4.009   1.00 19.46 ? 143 TYR A CZ  1 
ATOM   1106 O OH  . TYR A 1 142 ? 29.832 -14.468 3.810   1.00 22.28 ? 143 TYR A OH  1 
ATOM   1107 N N   . SER A 1 143 ? 21.807 -11.543 2.534   1.00 20.92 ? 144 SER A N   1 
ATOM   1108 C CA  . SER A 1 143 ? 20.365 -11.359 2.341   1.00 21.42 ? 144 SER A CA  1 
ATOM   1109 C C   . SER A 1 143 ? 19.708 -10.761 3.579   1.00 22.84 ? 144 SER A C   1 
ATOM   1110 O O   . SER A 1 143 ? 18.619 -11.170 4.001   1.00 23.30 ? 144 SER A O   1 
ATOM   1111 C CB  . SER A 1 143 ? 19.687 -12.661 1.915   1.00 24.80 ? 144 SER A CB  1 
ATOM   1112 O OG  . SER A 1 143 ? 20.361 -13.246 0.812   1.00 34.78 ? 144 SER A OG  1 
ATOM   1113 N N   . GLY A 1 144 ? 20.384 -9.785  4.174   1.00 21.22 ? 145 GLY A N   1 
ATOM   1114 C CA  . GLY A 1 144 ? 19.841 -9.053  5.293   1.00 21.62 ? 145 GLY A CA  1 
ATOM   1115 C C   . GLY A 1 144 ? 19.937 -9.729  6.638   1.00 22.24 ? 145 GLY A C   1 
ATOM   1116 O O   . GLY A 1 144 ? 19.321 -9.246  7.592   1.00 28.05 ? 145 GLY A O   1 
ATOM   1117 N N   . LYS A 1 145 ? 20.702 -10.813 6.759   1.00 22.16 ? 146 LYS A N   1 
ATOM   1118 C CA  . LYS A 1 145 ? 20.695 -11.599 7.986   1.00 24.67 ? 146 LYS A CA  1 
ATOM   1119 C C   . LYS A 1 145 ? 21.864 -11.310 8.917   1.00 25.05 ? 146 LYS A C   1 
ATOM   1120 O O   . LYS A 1 145 ? 21.767 -11.613 10.110  1.00 28.82 ? 146 LYS A O   1 
ATOM   1121 C CB  . LYS A 1 145 ? 20.672 -13.100 7.656   1.00 29.37 ? 146 LYS A CB  1 
ATOM   1122 C CG  . LYS A 1 145 ? 19.397 -13.585 6.930   1.00 33.04 ? 146 LYS A CG  1 
ATOM   1123 C CD  . LYS A 1 145 ? 18.212 -12.636 7.111   1.00 44.91 ? 146 LYS A CD  1 
ATOM   1124 C CE  . LYS A 1 145 ? 16.911 -13.218 6.556   1.00 44.94 ? 146 LYS A CE  1 
ATOM   1125 N NZ  . LYS A 1 145 ? 16.927 -13.320 5.066   1.00 42.90 ? 146 LYS A NZ  1 
ATOM   1126 N N   . LYS A 1 146 ? 22.962 -10.748 8.416   1.00 17.37 ? 147 LYS A N   1 
ATOM   1127 C CA  . LYS A 1 146 ? 24.192 -10.635 9.185   1.00 17.15 ? 147 LYS A CA  1 
ATOM   1128 C C   . LYS A 1 146 ? 24.459 -9.160  9.453   1.00 17.26 ? 147 LYS A C   1 
ATOM   1129 O O   . LYS A 1 146 ? 24.721 -8.398  8.521   1.00 17.44 ? 147 LYS A O   1 
ATOM   1130 C CB  . LYS A 1 146 ? 25.332 -11.254 8.383   1.00 18.83 ? 147 LYS A CB  1 
ATOM   1131 C CG  . LYS A 1 146 ? 26.687 -11.038 8.963   1.00 17.48 ? 147 LYS A CG  1 
ATOM   1132 C CD  . LYS A 1 146 ? 26.800 -11.506 10.405  1.00 17.74 ? 147 LYS A CD  1 
ATOM   1133 C CE  . LYS A 1 146 ? 28.215 -11.198 10.907  1.00 21.53 ? 147 LYS A CE  1 
ATOM   1134 N NZ  . LYS A 1 146 ? 28.445 -11.653 12.307  1.00 23.25 ? 147 LYS A NZ  1 
ATOM   1135 N N   . ASN A 1 147 ? 24.434 -8.769  10.725  1.00 17.10 ? 148 ASN A N   1 
ATOM   1136 C CA  . ASN A 1 147 ? 24.859 -7.430  11.122  1.00 19.23 ? 148 ASN A CA  1 
ATOM   1137 C C   . ASN A 1 147 ? 26.374 -7.365  10.998  1.00 21.12 ? 148 ASN A C   1 
ATOM   1138 O O   . ASN A 1 147 ? 27.090 -8.030  11.751  1.00 20.21 ? 148 ASN A O   1 
ATOM   1139 C CB  . ASN A 1 147 ? 24.425 -7.168  12.562  1.00 20.69 ? 148 ASN A CB  1 
ATOM   1140 C CG  . ASN A 1 147 ? 24.766 -5.772  13.040  1.00 24.14 ? 148 ASN A CG  1 
ATOM   1141 O OD1 . ASN A 1 147 ? 25.670 -5.121  12.518  1.00 24.24 ? 148 ASN A OD1 1 
ATOM   1142 N ND2 . ASN A 1 147 ? 24.044 -5.305  14.053  1.00 24.35 ? 148 ASN A ND2 1 
ATOM   1143 N N   . THR A 1 148 ? 26.872 -6.563  10.052  1.00 17.76 ? 149 THR A N   1 
ATOM   1144 C CA  . THR A 1 148 ? 28.312 -6.513  9.810   1.00 17.66 ? 149 THR A CA  1 
ATOM   1145 C C   . THR A 1 148 ? 29.070 -5.735  10.871  1.00 20.86 ? 149 THR A C   1 
ATOM   1146 O O   . THR A 1 148 ? 30.303 -5.816  10.906  1.00 22.63 ? 149 THR A O   1 
ATOM   1147 C CB  . THR A 1 148 ? 28.631 -5.830  8.478   1.00 18.29 ? 149 THR A CB  1 
ATOM   1148 O OG1 . THR A 1 148 ? 28.172 -4.470  8.514   1.00 17.22 ? 149 THR A OG1 1 
ATOM   1149 C CG2 . THR A 1 148 ? 28.007 -6.568  7.309   1.00 18.69 ? 149 THR A CG2 1 
ATOM   1150 N N   . GLY A 1 149 ? 28.383 -4.947  11.696  1.00 22.33 ? 150 GLY A N   1 
ATOM   1151 C CA  . GLY A 1 149 ? 29.050 -3.998  12.565  1.00 22.69 ? 150 GLY A CA  1 
ATOM   1152 C C   . GLY A 1 149 ? 29.549 -2.746  11.874  1.00 23.15 ? 150 GLY A C   1 
ATOM   1153 O O   . GLY A 1 149 ? 30.159 -1.890  12.532  1.00 24.81 ? 150 GLY A O   1 
ATOM   1154 N N   . ILE A 1 150 ? 29.311 -2.609  10.574  1.00 19.29 ? 151 ILE A N   1 
ATOM   1155 C CA  . ILE A 1 150 ? 29.745 -1.454  9.802   1.00 19.41 ? 151 ILE A CA  1 
ATOM   1156 C C   . ILE A 1 150 ? 28.570 -0.501  9.712   1.00 18.58 ? 151 ILE A C   1 
ATOM   1157 O O   . ILE A 1 150 ? 27.470 -0.898  9.304   1.00 18.57 ? 151 ILE A O   1 
ATOM   1158 C CB  . ILE A 1 150 ? 30.186 -1.867  8.391   1.00 19.28 ? 151 ILE A CB  1 
ATOM   1159 C CG1 . ILE A 1 150 ? 31.339 -2.873  8.467   1.00 20.82 ? 151 ILE A CG1 1 
ATOM   1160 C CG2 . ILE A 1 150 ? 30.556 -0.631  7.571   1.00 21.09 ? 151 ILE A CG2 1 
ATOM   1161 C CD1 . ILE A 1 150 ? 31.671 -3.493  7.136   1.00 29.03 ? 151 ILE A CD1 1 
ATOM   1162 N N   . LEU A 1 151 ? 28.801 0.754   10.078  1.00 17.79 ? 152 LEU A N   1 
ATOM   1163 C CA  . LEU A 1 151 ? 27.757 1.760   9.997   1.00 18.38 ? 152 LEU A CA  1 
ATOM   1164 C C   . LEU A 1 151 ? 27.516 2.172   8.550   1.00 15.67 ? 152 LEU A C   1 
ATOM   1165 O O   . LEU A 1 151 ? 28.456 2.340   7.765   1.00 17.84 ? 152 LEU A O   1 
ATOM   1166 C CB  . LEU A 1 151 ? 28.165 3.000   10.793  1.00 18.84 ? 152 LEU A CB  1 
ATOM   1167 C CG  . LEU A 1 151 ? 28.238 2.869   12.310  1.00 27.12 ? 152 LEU A CG  1 
ATOM   1168 C CD1 . LEU A 1 151 ? 29.136 3.960   12.877  1.00 35.79 ? 152 LEU A CD1 1 
ATOM   1169 C CD2 . LEU A 1 151 ? 26.868 3.010   12.865  1.00 32.25 ? 152 LEU A CD2 1 
ATOM   1170 N N   . LEU A 1 152 ? 26.243 2.370   8.213   1.00 16.31 ? 153 LEU A N   1 
ATOM   1171 C CA  . LEU A 1 152 ? 25.880 2.832   6.877   1.00 15.10 ? 153 LEU A CA  1 
ATOM   1172 C C   . LEU A 1 152 ? 26.621 4.114   6.503   1.00 17.83 ? 153 LEU A C   1 
ATOM   1173 O O   . LEU A 1 152 ? 27.090 4.258   5.368   1.00 16.94 ? 153 LEU A O   1 
ATOM   1174 C CB  . LEU A 1 152 ? 24.367 3.057   6.819   1.00 17.16 ? 153 LEU A CB  1 
ATOM   1175 C CG  . LEU A 1 152 ? 23.805 3.563   5.494   1.00 15.35 ? 153 LEU A CG  1 
ATOM   1176 C CD1 . LEU A 1 152 ? 23.990 2.549   4.375   1.00 17.70 ? 153 LEU A CD1 1 
ATOM   1177 C CD2 . LEU A 1 152 ? 22.328 3.910   5.652   1.00 17.61 ? 153 LEU A CD2 1 
ATOM   1178 N N   . ARG A 1 153 ? 26.764 5.043   7.454   1.00 16.23 ? 154 ARG A N   1 
ATOM   1179 C CA  . ARG A 1 153 ? 27.407 6.317   7.142   1.00 18.12 ? 154 ARG A CA  1 
ATOM   1180 C C   . ARG A 1 153 ? 28.864 6.143   6.738   1.00 18.71 ? 154 ARG A C   1 
ATOM   1181 O O   . ARG A 1 153 ? 29.375 6.928   5.939   1.00 20.69 ? 154 ARG A O   1 
ATOM   1182 C CB  . ARG A 1 153 ? 27.278 7.288   8.314   1.00 17.52 ? 154 ARG A CB  1 
ATOM   1183 C CG  . ARG A 1 153 ? 28.043 6.913   9.564   1.00 21.72 ? 154 ARG A CG  1 
ATOM   1184 C CD  . ARG A 1 153 ? 27.507 7.699   10.748  1.00 19.05 ? 154 ARG A CD  1 
ATOM   1185 N NE  . ARG A 1 153 ? 28.303 7.511   11.953  1.00 21.74 ? 154 ARG A NE  1 
ATOM   1186 C CZ  . ARG A 1 153 ? 27.895 7.868   13.167  1.00 22.19 ? 154 ARG A CZ  1 
ATOM   1187 N NH1 . ARG A 1 153 ? 26.707 8.446   13.328  1.00 31.75 ? 154 ARG A NH1 1 
ATOM   1188 N NH2 . ARG A 1 153 ? 28.675 7.658   14.219  1.00 32.78 ? 154 ARG A NH2 1 
ATOM   1189 N N   . ASP A 1 154 ? 29.543 5.124   7.267   1.00 17.49 ? 155 ASP A N   1 
ATOM   1190 C CA  . ASP A 1 154 ? 30.921 4.862   6.876   1.00 16.82 ? 155 ASP A CA  1 
ATOM   1191 C C   . ASP A 1 154 ? 30.995 4.094   5.563   1.00 18.12 ? 155 ASP A C   1 
ATOM   1192 O O   . ASP A 1 154 ? 31.861 4.365   4.723   1.00 18.82 ? 155 ASP A O   1 
ATOM   1193 C CB  . ASP A 1 154 ? 31.629 4.077   7.977   1.00 22.35 ? 155 ASP A CB  1 
ATOM   1194 C CG  . ASP A 1 154 ? 31.763 4.866   9.252   1.00 23.65 ? 155 ASP A CG  1 
ATOM   1195 O OD1 . ASP A 1 154 ? 31.989 6.094   9.172   1.00 26.22 ? 155 ASP A OD1 1 
ATOM   1196 O OD2 . ASP A 1 154 ? 31.643 4.269   10.336  1.00 25.71 ? 155 ASP A OD2 1 
ATOM   1197 N N   . TRP A 1 155 ? 30.094 3.136   5.366   1.00 15.92 ? 156 TRP A N   1 
ATOM   1198 C CA  . TRP A 1 155 ? 30.182 2.282   4.191   1.00 17.36 ? 156 TRP A CA  1 
ATOM   1199 C C   . TRP A 1 155 ? 29.846 3.036   2.909   1.00 15.15 ? 156 TRP A C   1 
ATOM   1200 O O   . TRP A 1 155 ? 30.476 2.809   1.870   1.00 16.46 ? 156 TRP A O   1 
ATOM   1201 C CB  . TRP A 1 155 ? 29.280 1.065   4.398   1.00 16.15 ? 156 TRP A CB  1 
ATOM   1202 C CG  . TRP A 1 155 ? 29.361 -0.005  3.329   1.00 16.92 ? 156 TRP A CG  1 
ATOM   1203 C CD1 . TRP A 1 155 ? 28.300 -0.573  2.689   1.00 16.80 ? 156 TRP A CD1 1 
ATOM   1204 C CD2 . TRP A 1 155 ? 30.541 -0.628  2.785   1.00 15.63 ? 156 TRP A CD2 1 
ATOM   1205 N NE1 . TRP A 1 155 ? 28.740 -1.519  1.792   1.00 17.69 ? 156 TRP A NE1 1 
ATOM   1206 C CE2 . TRP A 1 155 ? 30.110 -1.561  1.825   1.00 16.83 ? 156 TRP A CE2 1 
ATOM   1207 C CE3 . TRP A 1 155 ? 31.915 -0.488  3.015   1.00 18.02 ? 156 TRP A CE3 1 
ATOM   1208 C CZ2 . TRP A 1 155 ? 30.996 -2.343  1.089   1.00 18.66 ? 156 TRP A CZ2 1 
ATOM   1209 C CZ3 . TRP A 1 155 ? 32.798 -1.277  2.275   1.00 20.47 ? 156 TRP A CZ3 1 
ATOM   1210 C CH2 . TRP A 1 155 ? 32.330 -2.191  1.330   1.00 18.66 ? 156 TRP A CH2 1 
ATOM   1211 N N   . VAL A 1 156 ? 28.869 3.942   2.953   1.00 16.75 ? 157 VAL A N   1 
ATOM   1212 C CA  . VAL A 1 156 ? 28.514 4.709   1.765   1.00 18.18 ? 157 VAL A CA  1 
ATOM   1213 C C   . VAL A 1 156 ? 29.712 5.511   1.263   1.00 18.85 ? 157 VAL A C   1 
ATOM   1214 O O   . VAL A 1 156 ? 30.022 5.519   0.062   1.00 18.00 ? 157 VAL A O   1 
ATOM   1215 C CB  . VAL A 1 156 ? 27.302 5.607   2.081   1.00 17.28 ? 157 VAL A CB  1 
ATOM   1216 C CG1 . VAL A 1 156 ? 27.163 6.695   1.043   1.00 21.73 ? 157 VAL A CG1 1 
ATOM   1217 C CG2 . VAL A 1 156 ? 26.019 4.766   2.178   1.00 17.52 ? 157 VAL A CG2 1 
ATOM   1218 N N   . VAL A 1 157 ? 30.435 6.150   2.182   1.00 17.18 ? 158 VAL A N   1 
ATOM   1219 C CA  . VAL A 1 157 ? 31.618 6.914   1.794   1.00 17.53 ? 158 VAL A CA  1 
ATOM   1220 C C   . VAL A 1 157 ? 32.685 5.990   1.216   1.00 18.23 ? 158 VAL A C   1 
ATOM   1221 O O   . VAL A 1 157 ? 33.286 6.284   0.174   1.00 20.35 ? 158 VAL A O   1 
ATOM   1222 C CB  . VAL A 1 157 ? 32.132 7.714   3.003   1.00 18.95 ? 158 VAL A CB  1 
ATOM   1223 C CG1 . VAL A 1 157 ? 33.436 8.407   2.650   1.00 18.69 ? 158 VAL A CG1 1 
ATOM   1224 C CG2 . VAL A 1 157 ? 31.089 8.732   3.445   1.00 21.04 ? 158 VAL A CG2 1 
ATOM   1225 N N   . GLU A 1 158 ? 32.921 4.848   1.866   1.00 17.55 ? 159 GLU A N   1 
ATOM   1226 C CA  . GLU A 1 158 ? 33.960 3.928   1.400   1.00 18.83 ? 159 GLU A CA  1 
ATOM   1227 C C   . GLU A 1 158 ? 33.633 3.378   0.019   1.00 17.29 ? 159 GLU A C   1 
ATOM   1228 O O   . GLU A 1 158 ? 34.514 3.253   -0.843  1.00 17.97 ? 159 GLU A O   1 
ATOM   1229 C CB  . GLU A 1 158 ? 34.111 2.785   2.403   1.00 19.26 ? 159 GLU A CB  1 
ATOM   1230 C CG  . GLU A 1 158 ? 35.224 1.797   2.058   1.00 19.87 ? 159 GLU A CG  1 
ATOM   1231 C CD  . GLU A 1 158 ? 36.613 2.419   2.153   1.00 28.16 ? 159 GLU A CD  1 
ATOM   1232 O OE1 . GLU A 1 158 ? 36.805 3.329   2.985   1.00 32.32 ? 159 GLU A OE1 1 
ATOM   1233 O OE2 . GLU A 1 158 ? 37.514 2.000   1.393   1.00 33.53 ? 159 GLU A OE2 1 
ATOM   1234 N N   . VAL A 1 159 ? 32.364 3.037   -0.207  1.00 17.66 ? 160 VAL A N   1 
ATOM   1235 C CA  . VAL A 1 159 ? 31.943 2.476   -1.482  1.00 17.95 ? 160 VAL A CA  1 
ATOM   1236 C C   . VAL A 1 159 ? 32.228 3.435   -2.636  1.00 18.21 ? 160 VAL A C   1 
ATOM   1237 O O   . VAL A 1 159 ? 32.684 3.017   -3.712  1.00 17.73 ? 160 VAL A O   1 
ATOM   1238 C CB  . VAL A 1 159 ? 30.465 2.059   -1.371  1.00 21.05 ? 160 VAL A CB  1 
ATOM   1239 C CG1 . VAL A 1 159 ? 29.778 2.086   -2.698  1.00 23.73 ? 160 VAL A CG1 1 
ATOM   1240 C CG2 . VAL A 1 159 ? 30.389 0.685   -0.716  1.00 20.05 ? 160 VAL A CG2 1 
ATOM   1241 N N   . GLU A 1 160 ? 31.980 4.734   -2.436  1.00 17.26 ? 161 GLU A N   1 
ATOM   1242 C CA  . GLU A 1 160 ? 32.319 5.702   -3.474  1.00 16.83 ? 161 GLU A CA  1 
ATOM   1243 C C   . GLU A 1 160 ? 33.828 5.805   -3.661  1.00 18.26 ? 161 GLU A C   1 
ATOM   1244 O O   . GLU A 1 160 ? 34.315 5.811   -4.794  1.00 18.71 ? 161 GLU A O   1 
ATOM   1245 C CB  . GLU A 1 160 ? 31.715 7.073   -3.171  1.00 21.17 ? 161 GLU A CB  1 
ATOM   1246 C CG  . GLU A 1 160 ? 32.042 8.086   -4.269  1.00 20.92 ? 161 GLU A CG  1 
ATOM   1247 C CD  . GLU A 1 160 ? 31.394 9.440   -4.081  1.00 28.08 ? 161 GLU A CD  1 
ATOM   1248 O OE1 . GLU A 1 160 ? 30.477 9.568   -3.250  1.00 22.09 ? 161 GLU A OE1 1 
ATOM   1249 O OE2 . GLU A 1 160 ? 31.804 10.384  -4.788  1.00 35.71 ? 161 GLU A OE2 1 
ATOM   1250 N N   . LYS A 1 161 ? 34.579 5.844   -2.563  1.00 19.07 ? 162 LYS A N   1 
ATOM   1251 C CA  . LYS A 1 161 ? 36.037 5.918   -2.663  1.00 17.84 ? 162 LYS A CA  1 
ATOM   1252 C C   . LYS A 1 161 ? 36.601 4.750   -3.453  1.00 19.84 ? 162 LYS A C   1 
ATOM   1253 O O   . LYS A 1 161 ? 37.602 4.905   -4.168  1.00 21.29 ? 162 LYS A O   1 
ATOM   1254 C CB  . LYS A 1 161 ? 36.662 5.938   -1.271  1.00 23.25 ? 162 LYS A CB  1 
ATOM   1255 C CG  . LYS A 1 161 ? 36.603 7.272   -0.572  1.00 23.99 ? 162 LYS A CG  1 
ATOM   1256 C CD  . LYS A 1 161 ? 37.501 7.246   0.650   1.00 33.71 ? 162 LYS A CD  1 
ATOM   1257 C CE  . LYS A 1 161 ? 36.990 8.163   1.745   1.00 37.45 ? 162 LYS A CE  1 
ATOM   1258 N NZ  . LYS A 1 161 ? 37.601 7.816   3.060   1.00 47.38 ? 162 LYS A NZ  1 
ATOM   1259 N N   . ARG A 1 162 ? 35.989 3.573   -3.327  1.00 17.59 ? 163 ARG A N   1 
ATOM   1260 C CA  . ARG A 1 162 ? 36.486 2.369   -3.982  1.00 19.89 ? 163 ARG A CA  1 
ATOM   1261 C C   . ARG A 1 162 ? 36.119 2.290   -5.459  1.00 18.98 ? 163 ARG A C   1 
ATOM   1262 O O   . ARG A 1 162 ? 36.622 1.402   -6.156  1.00 20.03 ? 163 ARG A O   1 
ATOM   1263 C CB  . ARG A 1 162 ? 35.969 1.121   -3.263  1.00 18.33 ? 163 ARG A CB  1 
ATOM   1264 C CG  . ARG A 1 162 ? 36.444 0.980   -1.839  1.00 22.19 ? 163 ARG A CG  1 
ATOM   1265 C CD  . ARG A 1 162 ? 37.878 0.454   -1.753  1.00 23.32 ? 163 ARG A CD  1 
ATOM   1266 N NE  . ARG A 1 162 ? 38.247 0.253   -0.356  1.00 24.84 ? 163 ARG A NE  1 
ATOM   1267 C CZ  . ARG A 1 162 ? 39.201 -0.577  0.057   1.00 30.50 ? 163 ARG A CZ  1 
ATOM   1268 N NH1 . ARG A 1 162 ? 39.890 -1.298  -0.819  1.00 32.45 ? 163 ARG A NH1 1 
ATOM   1269 N NH2 . ARG A 1 162 ? 39.459 -0.694  1.351   1.00 33.86 ? 163 ARG A NH2 1 
ATOM   1270 N N   . GLY A 1 163 ? 35.234 3.157   -5.949  1.00 18.89 ? 164 GLY A N   1 
ATOM   1271 C CA  . GLY A 1 163 ? 34.932 3.217   -7.365  1.00 21.17 ? 164 GLY A CA  1 
ATOM   1272 C C   . GLY A 1 163 ? 33.567 2.711   -7.791  1.00 22.02 ? 164 GLY A C   1 
ATOM   1273 O O   . GLY A 1 163 ? 33.357 2.487   -8.989  1.00 21.21 ? 164 GLY A O   1 
ATOM   1274 N N   . ALA A 1 164 ? 32.642 2.494   -6.866  1.00 18.61 ? 165 ALA A N   1 
ATOM   1275 C CA  . ALA A 1 164 ? 31.313 2.070   -7.281  1.00 19.65 ? 165 ALA A CA  1 
ATOM   1276 C C   . ALA A 1 164 ? 30.662 3.144   -8.148  1.00 18.58 ? 165 ALA A C   1 
ATOM   1277 O O   . ALA A 1 164 ? 30.929 4.337   -8.007  1.00 20.97 ? 165 ALA A O   1 
ATOM   1278 C CB  . ALA A 1 164 ? 30.444 1.820   -6.057  1.00 20.62 ? 165 ALA A CB  1 
ATOM   1279 N N   . GLY A 1 165 ? 29.779 2.704   -9.040  1.00 17.19 ? 166 GLY A N   1 
ATOM   1280 C CA  . GLY A 1 165 ? 29.088 3.647   -9.898  1.00 17.60 ? 166 GLY A CA  1 
ATOM   1281 C C   . GLY A 1 165 ? 27.726 4.047   -9.377  1.00 19.61 ? 166 GLY A C   1 
ATOM   1282 O O   . GLY A 1 165 ? 27.208 5.104   -9.738  1.00 19.58 ? 166 GLY A O   1 
ATOM   1283 N N   A GLU A 1 166 ? 27.136 3.201   -8.539  0.62 17.62 ? 167 GLU A N   1 
ATOM   1284 N N   B GLU A 1 166 ? 27.167 3.243   -8.479  0.38 17.70 ? 167 GLU A N   1 
ATOM   1285 C CA  A GLU A 1 166 ? 25.771 3.390   -8.068  0.62 18.17 ? 167 GLU A CA  1 
ATOM   1286 C CA  B GLU A 1 166 ? 25.777 3.397   -8.072  0.38 18.22 ? 167 GLU A CA  1 
ATOM   1287 C C   A GLU A 1 166 ? 25.603 2.625   -6.769  0.62 17.44 ? 167 GLU A C   1 
ATOM   1288 C C   B GLU A 1 166 ? 25.565 2.594   -6.799  0.38 17.49 ? 167 GLU A C   1 
ATOM   1289 O O   A GLU A 1 166 ? 26.279 1.625   -6.537  0.62 17.33 ? 167 GLU A O   1 
ATOM   1290 O O   B GLU A 1 166 ? 26.199 1.557   -6.599  0.38 17.25 ? 167 GLU A O   1 
ATOM   1291 C CB  A GLU A 1 166 ? 24.776 2.809   -9.071  0.62 22.25 ? 167 GLU A CB  1 
ATOM   1292 C CB  B GLU A 1 166 ? 24.867 2.858   -9.178  0.38 22.18 ? 167 GLU A CB  1 
ATOM   1293 C CG  A GLU A 1 166 ? 24.523 3.656   -10.297 0.62 23.77 ? 167 GLU A CG  1 
ATOM   1294 C CG  B GLU A 1 166 ? 23.385 3.048   -8.977  0.38 17.99 ? 167 GLU A CG  1 
ATOM   1295 C CD  A GLU A 1 166 ? 23.348 3.128   -11.086 0.62 27.94 ? 167 GLU A CD  1 
ATOM   1296 C CD  B GLU A 1 166 ? 22.618 2.747   -10.249 0.38 23.57 ? 167 GLU A CD  1 
ATOM   1297 O OE1 A GLU A 1 166 ? 23.498 2.091   -11.770 0.62 32.79 ? 167 GLU A OE1 1 
ATOM   1298 O OE1 B GLU A 1 166 ? 22.938 1.740   -10.917 0.38 26.65 ? 167 GLU A OE1 1 
ATOM   1299 O OE2 A GLU A 1 166 ? 22.267 3.738   -10.997 0.62 26.72 ? 167 GLU A OE2 1 
ATOM   1300 O OE2 B GLU A 1 166 ? 21.699 3.520   -10.587 0.38 27.90 ? 167 GLU A OE2 1 
ATOM   1301 N N   . ILE A 1 167 ? 24.663 3.075   -5.948  1.00 17.57 ? 168 ILE A N   1 
ATOM   1302 C CA  . ILE A 1 167 ? 24.299 2.390   -4.714  1.00 16.35 ? 168 ILE A CA  1 
ATOM   1303 C C   . ILE A 1 167 ? 22.838 1.987   -4.821  1.00 15.42 ? 168 ILE A C   1 
ATOM   1304 O O   . ILE A 1 167 ? 21.979 2.836   -5.089  1.00 16.89 ? 168 ILE A O   1 
ATOM   1305 C CB  . ILE A 1 167 ? 24.520 3.293   -3.493  1.00 17.77 ? 168 ILE A CB  1 
ATOM   1306 C CG1 . ILE A 1 167 ? 26.018 3.489   -3.254  1.00 19.04 ? 168 ILE A CG1 1 
ATOM   1307 C CG2 . ILE A 1 167 ? 23.836 2.697   -2.263  1.00 19.61 ? 168 ILE A CG2 1 
ATOM   1308 C CD1 . ILE A 1 167 ? 26.330 4.522   -2.203  1.00 22.77 ? 168 ILE A CD1 1 
ATOM   1309 N N   . LEU A 1 168 ? 22.559 0.700   -4.627  1.00 16.19 ? 169 LEU A N   1 
ATOM   1310 C CA  . LEU A 1 168 ? 21.191 0.209   -4.525  1.00 16.29 ? 169 LEU A CA  1 
ATOM   1311 C C   . LEU A 1 168 ? 20.907 0.070   -3.034  1.00 16.78 ? 169 LEU A C   1 
ATOM   1312 O O   . LEU A 1 168 ? 21.397 -0.859  -2.389  1.00 18.20 ? 169 LEU A O   1 
ATOM   1313 C CB  . LEU A 1 168 ? 21.051 -1.126  -5.258  1.00 16.59 ? 169 LEU A CB  1 
ATOM   1314 C CG  . LEU A 1 168 ? 19.646 -1.614  -5.621  1.00 22.50 ? 169 LEU A CG  1 
ATOM   1315 C CD1 . LEU A 1 168 ? 19.719 -2.856  -6.494  1.00 21.67 ? 169 LEU A CD1 1 
ATOM   1316 C CD2 . LEU A 1 168 ? 18.781 -1.898  -4.406  1.00 29.03 ? 169 LEU A CD2 1 
ATOM   1317 N N   . LEU A 1 169 ? 20.120 0.992   -2.488  1.00 16.03 ? 170 LEU A N   1 
ATOM   1318 C CA  . LEU A 1 169 ? 19.983 1.139   -1.045  1.00 15.28 ? 170 LEU A CA  1 
ATOM   1319 C C   . LEU A 1 169 ? 18.652 0.536   -0.630  1.00 15.79 ? 170 LEU A C   1 
ATOM   1320 O O   . LEU A 1 169 ? 17.594 1.129   -0.880  1.00 16.19 ? 170 LEU A O   1 
ATOM   1321 C CB  . LEU A 1 169 ? 20.015 2.624   -0.674  1.00 17.03 ? 170 LEU A CB  1 
ATOM   1322 C CG  . LEU A 1 169 ? 19.951 2.943   0.825   1.00 17.77 ? 170 LEU A CG  1 
ATOM   1323 C CD1 . LEU A 1 169 ? 21.190 2.418   1.540   1.00 21.85 ? 170 LEU A CD1 1 
ATOM   1324 C CD2 . LEU A 1 169 ? 19.795 4.445   1.047   1.00 18.79 ? 170 LEU A CD2 1 
ATOM   1325 N N   . THR A 1 170 ? 18.683 -0.636  0.001   1.00 14.64 ? 171 THR A N   1 
ATOM   1326 C CA  . THR A 1 170 ? 17.444 -1.255  0.476   1.00 16.96 ? 171 THR A CA  1 
ATOM   1327 C C   . THR A 1 170 ? 17.287 -1.057  1.974   1.00 17.42 ? 171 THR A C   1 
ATOM   1328 O O   . THR A 1 170 ? 18.199 -1.351  2.751   1.00 17.46 ? 171 THR A O   1 
ATOM   1329 C CB  . THR A 1 170 ? 17.374 -2.745  0.156   1.00 16.68 ? 171 THR A CB  1 
ATOM   1330 O OG1 . THR A 1 170 ? 17.442 -2.933  -1.259  1.00 19.66 ? 171 THR A OG1 1 
ATOM   1331 C CG2 . THR A 1 170 ? 16.077 -3.347  0.681   1.00 19.76 ? 171 THR A CG2 1 
ATOM   1332 N N   . SER A 1 171 ? 16.127 -0.568  2.382   1.00 15.94 ? 172 SER A N   1 
ATOM   1333 C CA  . SER A 1 171 ? 15.805 -0.498  3.798   1.00 14.86 ? 172 SER A CA  1 
ATOM   1334 C C   . SER A 1 171 ? 15.153 -1.811  4.207   1.00 17.88 ? 172 SER A C   1 
ATOM   1335 O O   . SER A 1 171 ? 14.021 -2.098  3.802   1.00 17.72 ? 172 SER A O   1 
ATOM   1336 C CB  . SER A 1 171 ? 14.858 0.666   4.059   1.00 17.75 ? 172 SER A CB  1 
ATOM   1337 O OG  . SER A 1 171 ? 14.468 0.673   5.423   1.00 18.65 ? 172 SER A OG  1 
ATOM   1338 N N   . ILE A 1 172 ? 15.879 -2.615  4.990   1.00 17.08 ? 173 ILE A N   1 
ATOM   1339 C CA  . ILE A 1 172 ? 15.300 -3.838  5.545   1.00 18.97 ? 173 ILE A CA  1 
ATOM   1340 C C   . ILE A 1 172 ? 14.082 -3.496  6.406   1.00 21.43 ? 173 ILE A C   1 
ATOM   1341 O O   . ILE A 1 172 ? 13.142 -4.290  6.510   1.00 29.70 ? 173 ILE A O   1 
ATOM   1342 C CB  . ILE A 1 172 ? 16.381 -4.623  6.324   1.00 19.51 ? 173 ILE A CB  1 
ATOM   1343 C CG1 . ILE A 1 172 ? 17.577 -4.948  5.430   1.00 19.77 ? 173 ILE A CG1 1 
ATOM   1344 C CG2 . ILE A 1 172 ? 15.828 -5.941  6.877   1.00 24.78 ? 173 ILE A CG2 1 
ATOM   1345 C CD1 . ILE A 1 172 ? 18.792 -5.404  6.200   1.00 20.74 ? 173 ILE A CD1 1 
ATOM   1346 N N   . ASP A 1 173 ? 14.073 -2.302  7.010   1.00 23.31 ? 174 ASP A N   1 
ATOM   1347 C CA  . ASP A 1 173 ? 12.959 -1.854  7.847   1.00 25.91 ? 174 ASP A CA  1 
ATOM   1348 C C   . ASP A 1 173 ? 11.663 -1.694  7.045   1.00 32.22 ? 174 ASP A C   1 
ATOM   1349 O O   . ASP A 1 173 ? 10.572 -1.867  7.601   1.00 36.05 ? 174 ASP A O   1 
ATOM   1350 C CB  . ASP A 1 173 ? 13.350 -0.544  8.559   1.00 28.76 ? 174 ASP A CB  1 
ATOM   1351 C CG  . ASP A 1 173 ? 14.332 -0.763  9.733   1.00 26.39 ? 174 ASP A CG  1 
ATOM   1352 O OD1 . ASP A 1 173 ? 14.167 -1.773  10.449  1.00 29.57 ? 174 ASP A OD1 1 
ATOM   1353 O OD2 . ASP A 1 173 ? 15.258 0.069   9.953   1.00 20.91 ? 174 ASP A OD2 1 
ATOM   1354 N N   . ARG A 1 174 ? 11.751 -1.379  5.741   1.00 25.76 ? 175 ARG A N   1 
ATOM   1355 C CA  . ARG A 1 174 ? 10.572 -1.162  4.902   1.00 23.32 ? 175 ARG A CA  1 
ATOM   1356 C C   . ARG A 1 174 ? 10.354 -2.214  3.820   1.00 24.78 ? 175 ARG A C   1 
ATOM   1357 O O   . ARG A 1 174 ? 9.255  -2.275  3.254   1.00 22.76 ? 175 ARG A O   1 
ATOM   1358 C CB  . ARG A 1 174 ? 10.642 0.212   4.216   1.00 21.78 ? 175 ARG A CB  1 
ATOM   1359 C CG  . ARG A 1 174 ? 10.719 1.384   5.167   1.00 22.87 ? 175 ARG A CG  1 
ATOM   1360 C CD  . ARG A 1 174 ? 9.447  1.526   5.967   1.00 34.45 ? 175 ARG A CD  1 
ATOM   1361 N NE  . ARG A 1 174 ? 9.495  2.708   6.820   1.00 37.82 ? 175 ARG A NE  1 
ATOM   1362 C CZ  . ARG A 1 174 ? 9.020  3.893   6.460   1.00 39.31 ? 175 ARG A CZ  1 
ATOM   1363 N NH1 . ARG A 1 174 ? 8.468  4.045   5.265   1.00 32.01 ? 175 ARG A NH1 1 
ATOM   1364 N NH2 . ARG A 1 174 ? 9.101  4.925   7.290   1.00 44.11 ? 175 ARG A NH2 1 
ATOM   1365 N N   . ASP A 1 175 ? 11.358 -3.026  3.505   1.00 25.45 ? 176 ASP A N   1 
ATOM   1366 C CA  . ASP A 1 175 ? 11.249 -3.969  2.398   1.00 22.43 ? 176 ASP A CA  1 
ATOM   1367 C C   . ASP A 1 175 ? 10.153 -4.998  2.660   1.00 27.29 ? 176 ASP A C   1 
ATOM   1368 O O   . ASP A 1 175 ? 9.941  -5.431  3.796   1.00 27.85 ? 176 ASP A O   1 
ATOM   1369 C CB  . ASP A 1 175 ? 12.591 -4.676  2.202   1.00 25.08 ? 176 ASP A CB  1 
ATOM   1370 C CG  . ASP A 1 175 ? 12.708 -5.352  0.847   1.00 34.59 ? 176 ASP A CG  1 
ATOM   1371 O OD1 . ASP A 1 175 ? 12.053 -4.900  -0.113  1.00 30.76 ? 176 ASP A OD1 1 
ATOM   1372 O OD2 . ASP A 1 175 ? 13.470 -6.338  0.741   1.00 40.44 ? 176 ASP A OD2 1 
ATOM   1373 N N   . GLY A 1 176 ? 9.453  -5.388  1.593   1.00 25.92 ? 177 GLY A N   1 
ATOM   1374 C CA  . GLY A 1 176 ? 8.322  -6.287  1.698   1.00 30.74 ? 177 GLY A CA  1 
ATOM   1375 C C   . GLY A 1 176 ? 7.029  -5.628  2.115   1.00 32.11 ? 177 GLY A C   1 
ATOM   1376 O O   . GLY A 1 176 ? 5.984  -6.292  2.117   1.00 34.03 ? 177 GLY A O   1 
ATOM   1377 N N   . THR A 1 177 ? 7.061  -4.354  2.472   1.00 22.02 ? 178 THR A N   1 
ATOM   1378 C CA  . THR A 1 177 ? 5.879  -3.600  2.843   1.00 22.69 ? 178 THR A CA  1 
ATOM   1379 C C   . THR A 1 177 ? 5.509  -2.633  1.727   1.00 24.05 ? 178 THR A C   1 
ATOM   1380 O O   . THR A 1 177 ? 6.253  -2.415  0.763   1.00 24.56 ? 178 THR A O   1 
ATOM   1381 C CB  . THR A 1 177 ? 6.105  -2.843  4.157   1.00 22.11 ? 178 THR A CB  1 
ATOM   1382 O OG1 . THR A 1 177 ? 6.902  -1.668  3.920   1.00 24.55 ? 178 THR A OG1 1 
ATOM   1383 C CG2 . THR A 1 177 ? 6.811  -3.728  5.168   1.00 27.05 ? 178 THR A CG2 1 
ATOM   1384 N N   . LYS A 1 178 ? 4.325  -2.062  1.868   1.00 24.22 ? 179 LYS A N   1 
ATOM   1385 C CA  . LYS A 1 178 ? 3.813  -1.055  0.957   1.00 20.29 ? 179 LYS A CA  1 
ATOM   1386 C C   . LYS A 1 178 ? 3.557  0.245   1.704   1.00 20.74 ? 179 LYS A C   1 
ATOM   1387 O O   . LYS A 1 178 ? 2.663  1.009   1.344   1.00 23.81 ? 179 LYS A O   1 
ATOM   1388 C CB  . LYS A 1 178 ? 2.545  -1.561  0.269   1.00 24.79 ? 179 LYS A CB  1 
ATOM   1389 C CG  A LYS A 1 178 ? 2.687  -2.914  -0.404  0.45 27.80 ? 179 LYS A CG  1 
ATOM   1390 C CG  B LYS A 1 178 ? 2.745  -2.894  -0.438  0.55 27.73 ? 179 LYS A CG  1 
ATOM   1391 C CD  A LYS A 1 178 ? 1.369  -3.328  -1.051  0.45 31.06 ? 179 LYS A CD  1 
ATOM   1392 C CD  B LYS A 1 178 ? 1.494  -3.335  -1.186  0.55 31.15 ? 179 LYS A CD  1 
ATOM   1393 C CE  A LYS A 1 178 ? 1.396  -4.779  -1.503  0.45 35.41 ? 179 LYS A CE  1 
ATOM   1394 C CE  B LYS A 1 178 ? 1.622  -4.776  -1.660  0.55 35.42 ? 179 LYS A CE  1 
ATOM   1395 N NZ  A LYS A 1 178 ? 0.033  -5.265  -1.862  0.45 36.62 ? 179 LYS A NZ  1 
ATOM   1396 N NZ  B LYS A 1 178 ? 2.599  -4.921  -2.777  0.55 38.18 ? 179 LYS A NZ  1 
ATOM   1397 N N   . SER A 1 179 ? 4.338  0.487   2.763   1.00 25.77 ? 180 SER A N   1 
ATOM   1398 C CA  . SER A 1 179 ? 4.139  1.626   3.651   1.00 23.77 ? 180 SER A CA  1 
ATOM   1399 C C   . SER A 1 179 ? 4.891  2.864   3.200   1.00 24.34 ? 180 SER A C   1 
ATOM   1400 O O   . SER A 1 179 ? 4.680  3.940   3.770   1.00 25.60 ? 180 SER A O   1 
ATOM   1401 C CB  . SER A 1 179 ? 4.611  1.282   5.071   1.00 27.42 ? 180 SER A CB  1 
ATOM   1402 O OG  . SER A 1 179 ? 5.990  0.929   5.099   1.00 32.66 ? 180 SER A OG  1 
ATOM   1403 N N   . GLY A 1 180 ? 5.763  2.739   2.208   1.00 18.49 ? 181 GLY A N   1 
ATOM   1404 C CA  . GLY A 1 180 ? 6.572  3.871   1.798   1.00 18.11 ? 181 GLY A CA  1 
ATOM   1405 C C   . GLY A 1 180 ? 8.047  3.540   1.827   1.00 17.56 ? 181 GLY A C   1 
ATOM   1406 O O   . GLY A 1 180 ? 8.503  2.713   2.623   1.00 18.30 ? 181 GLY A O   1 
ATOM   1407 N N   . TYR A 1 181 ? 8.804  4.166   0.941   1.00 15.64 ? 182 TYR A N   1 
ATOM   1408 C CA  . TYR A 1 181 ? 10.247 4.072   1.028   1.00 18.45 ? 182 TYR A CA  1 
ATOM   1409 C C   . TYR A 1 181 ? 10.738 4.713   2.326   1.00 15.79 ? 182 TYR A C   1 
ATOM   1410 O O   . TYR A 1 181 ? 10.075 5.564   2.933   1.00 17.22 ? 182 TYR A O   1 
ATOM   1411 C CB  . TYR A 1 181 ? 10.897 4.780   -0.156  1.00 15.15 ? 182 TYR A CB  1 
ATOM   1412 C CG  . TYR A 1 181 ? 10.726 4.115   -1.503  1.00 15.00 ? 182 TYR A CG  1 
ATOM   1413 C CD1 . TYR A 1 181 ? 11.524 3.031   -1.877  1.00 15.46 ? 182 TYR A CD1 1 
ATOM   1414 C CD2 . TYR A 1 181 ? 9.774  4.571   -2.410  1.00 14.27 ? 182 TYR A CD2 1 
ATOM   1415 C CE1 . TYR A 1 181 ? 11.382 2.447   -3.121  1.00 16.38 ? 182 TYR A CE1 1 
ATOM   1416 C CE2 . TYR A 1 181 ? 9.633  4.003   -3.655  1.00 15.93 ? 182 TYR A CE2 1 
ATOM   1417 C CZ  . TYR A 1 181 ? 10.422 2.916   -4.000  1.00 15.86 ? 182 TYR A CZ  1 
ATOM   1418 O OH  . TYR A 1 181 ? 10.291 2.340   -5.243  1.00 16.99 ? 182 TYR A OH  1 
ATOM   1419 N N   . ASP A 1 182 ? 11.938 4.310   2.739   1.00 16.52 ? 183 ASP A N   1 
ATOM   1420 C CA  . ASP A 1 182 ? 12.550 4.816   3.966   1.00 17.10 ? 183 ASP A CA  1 
ATOM   1421 C C   . ASP A 1 182 ? 13.205 6.156   3.648   1.00 16.47 ? 183 ASP A C   1 
ATOM   1422 O O   . ASP A 1 182 ? 14.414 6.258   3.429   1.00 15.98 ? 183 ASP A O   1 
ATOM   1423 C CB  . ASP A 1 182 ? 13.566 3.802   4.468   1.00 16.10 ? 183 ASP A CB  1 
ATOM   1424 C CG  . ASP A 1 182 ? 13.990 4.029   5.913   1.00 17.71 ? 183 ASP A CG  1 
ATOM   1425 O OD1 . ASP A 1 182 ? 13.870 5.168   6.418   1.00 18.09 ? 183 ASP A OD1 1 
ATOM   1426 O OD2 . ASP A 1 182 ? 14.484 3.057   6.532   1.00 19.57 ? 183 ASP A OD2 1 
ATOM   1427 N N   . THR A 1 183 ? 12.372 7.201   3.624   1.00 15.37 ? 184 THR A N   1 
ATOM   1428 C CA  . THR A 1 183 ? 12.866 8.525   3.275   1.00 17.06 ? 184 THR A CA  1 
ATOM   1429 C C   . THR A 1 183 ? 13.847 9.052   4.309   1.00 17.00 ? 184 THR A C   1 
ATOM   1430 O O   . THR A 1 183 ? 14.744 9.824   3.959   1.00 16.73 ? 184 THR A O   1 
ATOM   1431 C CB  . THR A 1 183 ? 11.693 9.492   3.086   1.00 18.97 ? 184 THR A CB  1 
ATOM   1432 O OG1 . THR A 1 183 ? 10.854 9.461   4.245   1.00 21.14 ? 184 THR A OG1 1 
ATOM   1433 C CG2 . THR A 1 183 ? 10.870 9.103   1.873   1.00 20.46 ? 184 THR A CG2 1 
ATOM   1434 N N   . GLU A 1 184 ? 13.692 8.671   5.583   1.00 16.30 ? 185 GLU A N   1 
ATOM   1435 C CA  . GLU A 1 184 ? 14.685 9.081   6.572   1.00 17.01 ? 185 GLU A CA  1 
ATOM   1436 C C   . GLU A 1 184 ? 16.055 8.538   6.200   1.00 16.61 ? 185 GLU A C   1 
ATOM   1437 O O   . GLU A 1 184 ? 17.061 9.252   6.263   1.00 17.88 ? 185 GLU A O   1 
ATOM   1438 C CB  . GLU A 1 184 ? 14.291 8.588   7.962   1.00 17.88 ? 185 GLU A CB  1 
ATOM   1439 C CG  . GLU A 1 184 ? 15.280 8.996   9.044   1.00 18.42 ? 185 GLU A CG  1 
ATOM   1440 C CD  . GLU A 1 184 ? 15.030 8.349   10.402  1.00 24.26 ? 185 GLU A CD  1 
ATOM   1441 O OE1 . GLU A 1 184 ? 14.052 7.584   10.559  1.00 23.89 ? 185 GLU A OE1 1 
ATOM   1442 O OE2 . GLU A 1 184 ? 15.826 8.619   11.329  1.00 28.58 ? 185 GLU A OE2 1 
ATOM   1443 N N   . MET A 1 185 ? 16.107 7.271   5.783   1.00 15.99 ? 186 MET A N   1 
ATOM   1444 C CA  . MET A 1 185 ? 17.389 6.676   5.421   1.00 16.10 ? 186 MET A CA  1 
ATOM   1445 C C   . MET A 1 185 ? 17.958 7.298   4.148   1.00 16.26 ? 186 MET A C   1 
ATOM   1446 O O   . MET A 1 185 ? 19.166 7.551   4.059   1.00 16.11 ? 186 MET A O   1 
ATOM   1447 C CB  . MET A 1 185 ? 17.236 5.162   5.251   1.00 15.68 ? 186 MET A CB  1 
ATOM   1448 C CG  . MET A 1 185 ? 18.553 4.471   4.944   1.00 16.03 ? 186 MET A CG  1 
ATOM   1449 S SD  . MET A 1 185 ? 18.339 2.739   4.466   1.00 18.25 ? 186 MET A SD  1 
ATOM   1450 C CE  . MET A 1 185 ? 17.863 2.033   6.046   1.00 19.67 ? 186 MET A CE  1 
ATOM   1451 N N   . ILE A 1 186 ? 17.099 7.537   3.153   1.00 16.86 ? 187 ILE A N   1 
ATOM   1452 C CA  . ILE A 1 186 ? 17.555 8.090   1.882   1.00 15.84 ? 187 ILE A CA  1 
ATOM   1453 C C   . ILE A 1 186 ? 18.125 9.487   2.096   1.00 16.20 ? 187 ILE A C   1 
ATOM   1454 O O   . ILE A 1 186 ? 19.211 9.813   1.605   1.00 16.80 ? 187 ILE A O   1 
ATOM   1455 C CB  . ILE A 1 186 ? 16.412 8.094   0.853   1.00 17.19 ? 187 ILE A CB  1 
ATOM   1456 C CG1 . ILE A 1 186 ? 15.960 6.667   0.520   1.00 16.42 ? 187 ILE A CG1 1 
ATOM   1457 C CG2 . ILE A 1 186 ? 16.831 8.871   -0.400  1.00 16.97 ? 187 ILE A CG2 1 
ATOM   1458 C CD1 . ILE A 1 186 ? 14.589 6.622   -0.103  1.00 17.49 ? 187 ILE A CD1 1 
ATOM   1459 N N   A ARG A 1 187 ? 17.391 10.323  2.837   0.52 15.58 ? 188 ARG A N   1 
ATOM   1460 N N   B ARG A 1 187 ? 17.402 10.331  2.835   0.48 15.60 ? 188 ARG A N   1 
ATOM   1461 C CA  A ARG A 1 187 ? 17.867 11.673  3.141   0.52 16.57 ? 188 ARG A CA  1 
ATOM   1462 C CA  B ARG A 1 187 ? 17.908 11.682  3.086   0.48 16.51 ? 188 ARG A CA  1 
ATOM   1463 C C   A ARG A 1 187 ? 19.177 11.640  3.912   0.52 18.96 ? 188 ARG A C   1 
ATOM   1464 C C   B ARG A 1 187 ? 19.179 11.661  3.930   0.48 18.96 ? 188 ARG A C   1 
ATOM   1465 O O   A ARG A 1 187 ? 20.056 12.485  3.697   0.52 17.83 ? 188 ARG A O   1 
ATOM   1466 O O   B ARG A 1 187 ? 20.047 12.525  3.762   0.48 17.88 ? 188 ARG A O   1 
ATOM   1467 C CB  A ARG A 1 187 ? 16.813 12.408  3.966   0.52 17.95 ? 188 ARG A CB  1 
ATOM   1468 C CB  B ARG A 1 187 ? 16.822 12.537  3.745   0.48 18.42 ? 188 ARG A CB  1 
ATOM   1469 C CG  A ARG A 1 187 ? 15.610 12.834  3.169   0.52 18.47 ? 188 ARG A CG  1 
ATOM   1470 C CG  B ARG A 1 187 ? 17.231 13.984  4.072   0.48 17.06 ? 188 ARG A CG  1 
ATOM   1471 C CD  A ARG A 1 187 ? 14.591 13.581  4.013   0.52 20.09 ? 188 ARG A CD  1 
ATOM   1472 C CD  B ARG A 1 187 ? 17.906 14.698  2.897   0.48 21.24 ? 188 ARG A CD  1 
ATOM   1473 N NE  A ARG A 1 187 ? 13.449 13.992  3.204   0.52 23.29 ? 188 ARG A NE  1 
ATOM   1474 N NE  B ARG A 1 187 ? 16.947 15.153  1.890   0.48 21.10 ? 188 ARG A NE  1 
ATOM   1475 C CZ  A ARG A 1 187 ? 13.442 15.063  2.417   0.52 24.33 ? 188 ARG A CZ  1 
ATOM   1476 C CZ  B ARG A 1 187 ? 17.284 15.526  0.659   0.48 20.60 ? 188 ARG A CZ  1 
ATOM   1477 N NH1 A ARG A 1 187 ? 14.514 15.840  2.338   0.52 20.22 ? 188 ARG A NH1 1 
ATOM   1478 N NH1 B ARG A 1 187 ? 18.553 15.501  0.290   0.48 24.11 ? 188 ARG A NH1 1 
ATOM   1479 N NH2 A ARG A 1 187 ? 12.361 15.354  1.705   0.52 23.33 ? 188 ARG A NH2 1 
ATOM   1480 N NH2 B ARG A 1 187 ? 16.354 15.925  -0.203  0.48 20.67 ? 188 ARG A NH2 1 
ATOM   1481 N N   . PHE A 1 188 ? 19.313 10.682  4.828   1.00 16.66 ? 189 PHE A N   1 
ATOM   1482 C CA  . PHE A 1 188 ? 20.519 10.573  5.633   1.00 15.74 ? 189 PHE A CA  1 
ATOM   1483 C C   . PHE A 1 188 ? 21.735 10.286  4.762   1.00 16.92 ? 189 PHE A C   1 
ATOM   1484 O O   . PHE A 1 188 ? 22.805 10.878  4.958   1.00 17.29 ? 189 PHE A O   1 
ATOM   1485 C CB  . PHE A 1 188 ? 20.334 9.442   6.648   1.00 16.97 ? 189 PHE A CB  1 
ATOM   1486 C CG  . PHE A 1 188 ? 21.546 9.186   7.480   1.00 16.86 ? 189 PHE A CG  1 
ATOM   1487 C CD1 . PHE A 1 188 ? 21.917 10.072  8.481   1.00 21.32 ? 189 PHE A CD1 1 
ATOM   1488 C CD2 . PHE A 1 188 ? 22.325 8.067   7.259   1.00 19.19 ? 189 PHE A CD2 1 
ATOM   1489 C CE1 . PHE A 1 188 ? 23.046 9.841   9.253   1.00 23.38 ? 189 PHE A CE1 1 
ATOM   1490 C CE2 . PHE A 1 188 ? 23.461 7.832   8.022   1.00 20.02 ? 189 PHE A CE2 1 
ATOM   1491 C CZ  . PHE A 1 188 ? 23.814 8.716   9.033   1.00 20.97 ? 189 PHE A CZ  1 
ATOM   1492 N N   . VAL A 1 189 ? 21.592 9.354   3.810   1.00 16.24 ? 190 VAL A N   1 
ATOM   1493 C CA  . VAL A 1 189 ? 22.697 8.960   2.935   1.00 17.12 ? 190 VAL A CA  1 
ATOM   1494 C C   . VAL A 1 189 ? 23.021 10.046  1.909   1.00 16.69 ? 190 VAL A C   1 
ATOM   1495 O O   . VAL A 1 189 ? 24.176 10.181  1.492   1.00 17.90 ? 190 VAL A O   1 
ATOM   1496 C CB  . VAL A 1 189 ? 22.337 7.615   2.261   1.00 18.32 ? 190 VAL A CB  1 
ATOM   1497 C CG1 . VAL A 1 189 ? 23.264 7.307   1.084   1.00 23.93 ? 190 VAL A CG1 1 
ATOM   1498 C CG2 . VAL A 1 189 ? 22.387 6.501   3.278   1.00 21.49 ? 190 VAL A CG2 1 
ATOM   1499 N N   . ARG A 1 190 ? 22.022 10.830  1.485   1.00 17.86 ? 191 ARG A N   1 
ATOM   1500 C CA  . ARG A 1 190 ? 22.172 11.716  0.324   1.00 16.60 ? 191 ARG A CA  1 
ATOM   1501 C C   . ARG A 1 190 ? 23.403 12.618  0.354   1.00 18.17 ? 191 ARG A C   1 
ATOM   1502 O O   . ARG A 1 190 ? 24.125 12.663  -0.654  1.00 18.01 ? 191 ARG A O   1 
ATOM   1503 C CB  . ARG A 1 190 ? 20.871 12.494  0.072   1.00 16.43 ? 191 ARG A CB  1 
ATOM   1504 C CG  . ARG A 1 190 ? 20.944 13.477  -1.103  1.00 19.75 ? 191 ARG A CG  1 
ATOM   1505 C CD  . ARG A 1 190 ? 20.951 12.785  -2.465  1.00 19.09 ? 191 ARG A CD  1 
ATOM   1506 N NE  . ARG A 1 190 ? 22.278 12.280  -2.848  1.00 16.86 ? 191 ARG A NE  1 
ATOM   1507 C CZ  . ARG A 1 190 ? 22.495 11.518  -3.915  1.00 18.82 ? 191 ARG A CZ  1 
ATOM   1508 N NH1 . ARG A 1 190 ? 21.480 11.184  -4.708  1.00 19.45 ? 191 ARG A NH1 1 
ATOM   1509 N NH2 . ARG A 1 190 ? 23.723 11.088  -4.202  1.00 18.39 ? 191 ARG A NH2 1 
ATOM   1510 N N   . PRO A 1 191 ? 23.716 13.330  1.440   1.00 16.34 ? 192 PRO A N   1 
ATOM   1511 C CA  . PRO A 1 191 ? 24.883 14.218  1.417   1.00 19.44 ? 192 PRO A CA  1 
ATOM   1512 C C   . PRO A 1 191 ? 26.205 13.494  1.579   1.00 19.95 ? 192 PRO A C   1 
ATOM   1513 O O   . PRO A 1 191 ? 27.264 14.126  1.448   1.00 21.72 ? 192 PRO A O   1 
ATOM   1514 C CB  . PRO A 1 191 ? 24.626 15.136  2.613   1.00 21.12 ? 192 PRO A CB  1 
ATOM   1515 C CG  . PRO A 1 191 ? 23.904 14.251  3.592   1.00 20.83 ? 192 PRO A CG  1 
ATOM   1516 C CD  . PRO A 1 191 ? 23.011 13.391  2.736   1.00 16.89 ? 192 PRO A CD  1 
ATOM   1517 N N   . LEU A 1 192 ? 26.185 12.195  1.866   1.00 17.21 ? 193 LEU A N   1 
ATOM   1518 C CA  . LEU A 1 192 ? 27.413 11.441  2.063   1.00 17.87 ? 193 LEU A CA  1 
ATOM   1519 C C   . LEU A 1 192 ? 28.012 10.928  0.763   1.00 18.90 ? 193 LEU A C   1 
ATOM   1520 O O   . LEU A 1 192 ? 29.157 10.461  0.776   1.00 21.61 ? 193 LEU A O   1 
ATOM   1521 C CB  . LEU A 1 192 ? 27.128 10.248  2.978   1.00 17.01 ? 193 LEU A CB  1 
ATOM   1522 C CG  . LEU A 1 192 ? 26.764 10.603  4.418   1.00 18.03 ? 193 LEU A CG  1 
ATOM   1523 C CD1 . LEU A 1 192 ? 26.391 9.349   5.197   1.00 23.69 ? 193 LEU A CD1 1 
ATOM   1524 C CD2 . LEU A 1 192 ? 27.921 11.314  5.090   1.00 25.30 ? 193 LEU A CD2 1 
ATOM   1525 N N   . THR A 1 193 ? 27.282 10.998  -0.349  1.00 18.05 ? 194 THR A N   1 
ATOM   1526 C CA  . THR A 1 193 ? 27.775 10.452  -1.603  1.00 20.06 ? 194 THR A CA  1 
ATOM   1527 C C   . THR A 1 193 ? 27.249 11.284  -2.760  1.00 19.28 ? 194 THR A C   1 
ATOM   1528 O O   . THR A 1 193 ? 26.130 11.810  -2.718  1.00 18.83 ? 194 THR A O   1 
ATOM   1529 C CB  . THR A 1 193 ? 27.408 8.959   -1.776  1.00 20.42 ? 194 THR A CB  1 
ATOM   1530 O OG1 . THR A 1 193 ? 27.973 8.459   -2.998  1.00 21.15 ? 194 THR A OG1 1 
ATOM   1531 C CG2 . THR A 1 193 ? 25.900 8.758   -1.811  1.00 21.12 ? 194 THR A CG2 1 
ATOM   1532 N N   . THR A 1 194 ? 28.069 11.385  -3.802  1.00 20.84 ? 195 THR A N   1 
ATOM   1533 C CA  . THR A 1 194 ? 27.653 11.952  -5.074  1.00 21.29 ? 195 THR A CA  1 
ATOM   1534 C C   . THR A 1 194 ? 27.122 10.902  -6.040  1.00 24.54 ? 195 THR A C   1 
ATOM   1535 O O   . THR A 1 194 ? 26.686 11.260  -7.139  1.00 21.88 ? 195 THR A O   1 
ATOM   1536 C CB  . THR A 1 194 ? 28.828 12.692  -5.726  1.00 23.67 ? 195 THR A CB  1 
ATOM   1537 O OG1 . THR A 1 194 ? 29.814 11.742  -6.149  1.00 28.96 ? 195 THR A OG1 1 
ATOM   1538 C CG2 . THR A 1 194 ? 29.457 13.662  -4.739  1.00 33.04 ? 195 THR A CG2 1 
ATOM   1539 N N   . LEU A 1 195 ? 27.149 9.613   -5.659  1.00 17.65 ? 196 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 195 ? 26.742 8.555   -6.564  1.00 18.82 ? 196 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 195 ? 25.222 8.506   -6.686  1.00 19.49 ? 196 LEU A C   1 
ATOM   1542 O O   . LEU A 1 195 ? 24.503 8.870   -5.752  1.00 19.38 ? 196 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 195 ? 27.201 7.208   -6.030  1.00 20.04 ? 196 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 195 ? 28.695 6.946   -5.940  1.00 20.04 ? 196 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 195 ? 28.900 5.518   -5.448  1.00 21.40 ? 196 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 195 ? 29.340 7.181   -7.300  1.00 23.83 ? 196 LEU A CD2 1 
ATOM   1547 N N   . PRO A 1 196 ? 24.710 8.036   -7.821  1.00 17.71 ? 197 PRO A N   1 
ATOM   1548 C CA  . PRO A 1 196 ? 23.278 7.738   -7.905  1.00 18.19 ? 197 PRO A CA  1 
ATOM   1549 C C   . PRO A 1 196 ? 22.863 6.753   -6.824  1.00 17.26 ? 197 PRO A C   1 
ATOM   1550 O O   . PRO A 1 196 ? 23.552 5.765   -6.553  1.00 18.30 ? 197 PRO A O   1 
ATOM   1551 C CB  . PRO A 1 196 ? 23.117 7.144   -9.306  1.00 20.27 ? 197 PRO A CB  1 
ATOM   1552 C CG  . PRO A 1 196 ? 24.306 7.624   -10.072 1.00 25.12 ? 197 PRO A CG  1 
ATOM   1553 C CD  . PRO A 1 196 ? 25.414 7.802   -9.091  1.00 21.15 ? 197 PRO A CD  1 
ATOM   1554 N N   . ILE A 1 197 ? 21.732 7.050   -6.192  1.00 15.94 ? 198 ILE A N   1 
ATOM   1555 C CA  . ILE A 1 197 ? 21.130 6.214   -5.159  1.00 16.94 ? 198 ILE A CA  1 
ATOM   1556 C C   . ILE A 1 197 ? 19.824 5.660   -5.709  1.00 14.90 ? 198 ILE A C   1 
ATOM   1557 O O   . ILE A 1 197 ? 18.922 6.427   -6.084  1.00 16.19 ? 198 ILE A O   1 
ATOM   1558 C CB  . ILE A 1 197 ? 20.863 7.011   -3.875  1.00 16.00 ? 198 ILE A CB  1 
ATOM   1559 C CG1 . ILE A 1 197 ? 22.166 7.564   -3.296  1.00 22.83 ? 198 ILE A CG1 1 
ATOM   1560 C CG2 . ILE A 1 197 ? 20.132 6.141   -2.857  1.00 20.56 ? 198 ILE A CG2 1 
ATOM   1561 C CD1 . ILE A 1 197 ? 21.931 8.515   -2.144  1.00 23.72 ? 198 ILE A CD1 1 
ATOM   1562 N N   . ILE A 1 198 ? 19.703 4.335   -5.729  1.00 15.47 ? 199 ILE A N   1 
ATOM   1563 C CA  . ILE A 1 198 ? 18.452 3.672   -6.084  1.00 16.09 ? 199 ILE A CA  1 
ATOM   1564 C C   . ILE A 1 198 ? 17.728 3.332   -4.789  1.00 16.47 ? 199 ILE A C   1 
ATOM   1565 O O   . ILE A 1 198 ? 18.239 2.555   -3.974  1.00 17.60 ? 199 ILE A O   1 
ATOM   1566 C CB  . ILE A 1 198 ? 18.699 2.383   -6.886  1.00 16.04 ? 199 ILE A CB  1 
ATOM   1567 C CG1 . ILE A 1 198 ? 19.582 2.623   -8.118  1.00 17.73 ? 199 ILE A CG1 1 
ATOM   1568 C CG2 . ILE A 1 198 ? 17.359 1.709   -7.241  1.00 17.97 ? 199 ILE A CG2 1 
ATOM   1569 C CD1 . ILE A 1 198 ? 20.130 1.290   -8.711  1.00 20.40 ? 199 ILE A CD1 1 
ATOM   1570 N N   . ALA A 1 199 ? 16.541 3.904   -4.594  1.00 14.50 ? 200 ALA A N   1 
ATOM   1571 C CA  . ALA A 1 199 ? 15.730 3.595   -3.426  1.00 17.44 ? 200 ALA A CA  1 
ATOM   1572 C C   . ALA A 1 199 ? 15.050 2.253   -3.630  1.00 16.87 ? 200 ALA A C   1 
ATOM   1573 O O   . ALA A 1 199 ? 14.488 1.986   -4.693  1.00 15.47 ? 200 ALA A O   1 
ATOM   1574 C CB  . ALA A 1 199 ? 14.642 4.650   -3.262  1.00 18.60 ? 200 ALA A CB  1 
ATOM   1575 N N   . SER A 1 200 ? 15.054 1.434   -2.582  1.00 17.57 ? 201 SER A N   1 
ATOM   1576 C CA  . SER A 1 200 ? 14.503 0.086   -2.670  1.00 16.31 ? 201 SER A CA  1 
ATOM   1577 C C   . SER A 1 200 ? 13.880 -0.305  -1.341  1.00 14.58 ? 201 SER A C   1 
ATOM   1578 O O   . SER A 1 200 ? 14.505 -0.153  -0.290  1.00 16.26 ? 201 SER A O   1 
ATOM   1579 C CB  . SER A 1 200 ? 15.634 -0.879  -3.037  1.00 17.70 ? 201 SER A CB  1 
ATOM   1580 O OG  . SER A 1 200 ? 15.277 -2.225  -2.858  1.00 21.66 ? 201 SER A OG  1 
ATOM   1581 N N   . GLY A 1 201 ? 12.648 -0.800  -1.394  1.00 16.03 ? 202 GLY A N   1 
ATOM   1582 C CA  . GLY A 1 201 ? 11.975 -1.316  -0.221  1.00 15.38 ? 202 GLY A CA  1 
ATOM   1583 C C   . GLY A 1 201 ? 10.905 -0.384  0.298   1.00 16.06 ? 202 GLY A C   1 
ATOM   1584 O O   . GLY A 1 201 ? 11.224 0.707   0.780   1.00 17.07 ? 202 GLY A O   1 
ATOM   1585 N N   . GLY A 1 202 ? 9.643  -0.797  0.218   1.00 16.70 ? 203 GLY A N   1 
ATOM   1586 C CA  . GLY A 1 202 ? 8.539  -0.037  0.787   1.00 18.44 ? 203 GLY A CA  1 
ATOM   1587 C C   . GLY A 1 202 ? 7.525  0.507   -0.200  1.00 18.20 ? 203 GLY A C   1 
ATOM   1588 O O   . GLY A 1 202 ? 6.488  1.019   0.240   1.00 17.87 ? 203 GLY A O   1 
ATOM   1589 N N   . ALA A 1 203 ? 7.754  0.419   -1.512  1.00 18.39 ? 204 ALA A N   1 
ATOM   1590 C CA  . ALA A 1 203 ? 6.868  1.067   -2.475  1.00 17.47 ? 204 ALA A CA  1 
ATOM   1591 C C   . ALA A 1 203 ? 5.460  0.503   -2.378  1.00 19.30 ? 204 ALA A C   1 
ATOM   1592 O O   . ALA A 1 203 ? 5.274  -0.711  -2.400  1.00 20.01 ? 204 ALA A O   1 
ATOM   1593 C CB  . ALA A 1 203 ? 7.378  0.831   -3.895  1.00 21.07 ? 204 ALA A CB  1 
ATOM   1594 N N   . GLY A 1 204 ? 4.467  1.389   -2.312  1.00 18.69 ? 205 GLY A N   1 
ATOM   1595 C CA  . GLY A 1 204 ? 3.078  0.959   -2.290  1.00 18.50 ? 205 GLY A CA  1 
ATOM   1596 C C   . GLY A 1 204 ? 2.149  1.815   -3.126  1.00 20.85 ? 205 GLY A C   1 
ATOM   1597 O O   . GLY A 1 204 ? 1.173  1.320   -3.704  1.00 23.08 ? 205 GLY A O   1 
ATOM   1598 N N   . LYS A 1 205 ? 2.444  3.112   -3.196  1.00 18.02 ? 206 LYS A N   1 
ATOM   1599 C CA  . LYS A 1 205 ? 1.594  4.095   -3.851  1.00 21.05 ? 206 LYS A CA  1 
ATOM   1600 C C   . LYS A 1 205 ? 2.464  5.042   -4.663  1.00 17.65 ? 206 LYS A C   1 
ATOM   1601 O O   . LYS A 1 205 ? 3.655  5.201   -4.393  1.00 17.94 ? 206 LYS A O   1 
ATOM   1602 C CB  . LYS A 1 205 ? 0.830  4.926   -2.816  1.00 21.57 ? 206 LYS A CB  1 
ATOM   1603 C CG  . LYS A 1 205 ? 0.025  4.132   -1.806  1.00 24.73 ? 206 LYS A CG  1 
ATOM   1604 C CD  . LYS A 1 205 ? -1.033 5.018   -1.162  1.00 36.05 ? 206 LYS A CD  1 
ATOM   1605 C CE  . LYS A 1 205 ? -2.075 5.455   -2.200  1.00 45.55 ? 206 LYS A CE  1 
ATOM   1606 N NZ  . LYS A 1 205 ? -3.157 6.324   -1.640  1.00 48.58 ? 206 LYS A NZ  1 
ATOM   1607 N N   . MET A 1 206 ? 1.843  5.713   -5.641  1.00 20.04 ? 207 MET A N   1 
ATOM   1608 C CA  . MET A 1 206 ? 2.595  6.642   -6.490  1.00 17.44 ? 207 MET A CA  1 
ATOM   1609 C C   . MET A 1 206 ? 3.257  7.741   -5.668  1.00 16.00 ? 207 MET A C   1 
ATOM   1610 O O   . MET A 1 206 ? 4.400  8.134   -5.946  1.00 15.90 ? 207 MET A O   1 
ATOM   1611 C CB  . MET A 1 206 ? 1.678  7.243   -7.554  1.00 18.14 ? 207 MET A CB  1 
ATOM   1612 C CG  . MET A 1 206 ? 1.270  6.247   -8.625  1.00 21.26 ? 207 MET A CG  1 
ATOM   1613 S SD  . MET A 1 206 ? 0.526  6.994   -10.085 1.00 20.04 ? 207 MET A SD  1 
ATOM   1614 C CE  . MET A 1 206 ? -0.960 7.681   -9.356  1.00 22.81 ? 207 MET A CE  1 
ATOM   1615 N N   . GLU A 1 207 ? 2.562  8.233   -4.636  1.00 17.19 ? 208 GLU A N   1 
ATOM   1616 C CA  . GLU A 1 207 ? 3.126  9.297   -3.810  1.00 18.25 ? 208 GLU A CA  1 
ATOM   1617 C C   . GLU A 1 207 ? 4.418  8.855   -3.138  1.00 17.44 ? 208 GLU A C   1 
ATOM   1618 O O   . GLU A 1 207 ? 5.271  9.692   -2.828  1.00 17.92 ? 208 GLU A O   1 
ATOM   1619 C CB  . GLU A 1 207 ? 2.117  9.743   -2.750  1.00 21.04 ? 208 GLU A CB  1 
ATOM   1620 C CG  . GLU A 1 207 ? 1.740  8.641   -1.776  1.00 23.30 ? 208 GLU A CG  1 
ATOM   1621 C CD  . GLU A 1 207 ? 0.385  8.840   -1.130  1.00 37.14 ? 208 GLU A CD  1 
ATOM   1622 O OE1 . GLU A 1 207 ? 0.348  9.212   0.063   1.00 34.71 ? 208 GLU A OE1 1 
ATOM   1623 O OE2 . GLU A 1 207 ? -0.641 8.623   -1.813  1.00 40.13 ? 208 GLU A OE2 1 
ATOM   1624 N N   . HIS A 1 208 ? 4.587  7.542   -2.915  1.00 16.55 ? 209 HIS A N   1 
ATOM   1625 C CA  . HIS A 1 208 ? 5.818  7.070   -2.285  1.00 14.59 ? 209 HIS A CA  1 
ATOM   1626 C C   . HIS A 1 208 ? 7.034  7.317   -3.168  1.00 14.56 ? 209 HIS A C   1 
ATOM   1627 O O   . HIS A 1 208 ? 8.131  7.577   -2.661  1.00 15.92 ? 209 HIS A O   1 
ATOM   1628 C CB  . HIS A 1 208 ? 5.715  5.578   -1.987  1.00 15.63 ? 209 HIS A CB  1 
ATOM   1629 C CG  . HIS A 1 208 ? 4.703  5.251   -0.943  1.00 18.55 ? 209 HIS A CG  1 
ATOM   1630 N ND1 . HIS A 1 208 ? 4.162  3.992   -0.804  1.00 18.39 ? 209 HIS A ND1 1 
ATOM   1631 C CD2 . HIS A 1 208 ? 4.144  6.015   0.023   1.00 19.20 ? 209 HIS A CD2 1 
ATOM   1632 C CE1 . HIS A 1 208 ? 3.308  3.996   0.203   1.00 19.73 ? 209 HIS A CE1 1 
ATOM   1633 N NE2 . HIS A 1 208 ? 3.277  5.211   0.722   1.00 21.97 ? 209 HIS A NE2 1 
ATOM   1634 N N   . PHE A 1 209 ? 6.867  7.194   -4.486  1.00 15.68 ? 210 PHE A N   1 
ATOM   1635 C CA  . PHE A 1 209 ? 7.966  7.457   -5.400  1.00 15.89 ? 210 PHE A CA  1 
ATOM   1636 C C   . PHE A 1 209 ? 8.320  8.928   -5.374  1.00 16.15 ? 210 PHE A C   1 
ATOM   1637 O O   . PHE A 1 209 ? 9.499  9.285   -5.309  1.00 15.93 ? 210 PHE A O   1 
ATOM   1638 C CB  . PHE A 1 209 ? 7.592  7.024   -6.816  1.00 17.04 ? 210 PHE A CB  1 
ATOM   1639 C CG  . PHE A 1 209 ? 7.516  5.534   -6.996  1.00 17.07 ? 210 PHE A CG  1 
ATOM   1640 C CD1 . PHE A 1 209 ? 6.423  4.817   -6.539  1.00 21.19 ? 210 PHE A CD1 1 
ATOM   1641 C CD2 . PHE A 1 209 ? 8.538  4.858   -7.632  1.00 17.77 ? 210 PHE A CD2 1 
ATOM   1642 C CE1 . PHE A 1 209 ? 6.370  3.437   -6.718  1.00 19.90 ? 210 PHE A CE1 1 
ATOM   1643 C CE2 . PHE A 1 209 ? 8.481  3.478   -7.809  1.00 19.71 ? 210 PHE A CE2 1 
ATOM   1644 C CZ  . PHE A 1 209 ? 7.393  2.780   -7.355  1.00 20.30 ? 210 PHE A CZ  1 
ATOM   1645 N N   . LEU A 1 210 ? 7.300  9.792   -5.392  1.00 15.81 ? 211 LEU A N   1 
ATOM   1646 C CA  . LEU A 1 210 ? 7.533  11.225  -5.265  1.00 16.00 ? 211 LEU A CA  1 
ATOM   1647 C C   . LEU A 1 210 ? 8.313  11.544  -3.995  1.00 16.04 ? 211 LEU A C   1 
ATOM   1648 O O   . LEU A 1 210 ? 9.303  12.283  -4.034  1.00 15.59 ? 211 LEU A O   1 
ATOM   1649 C CB  . LEU A 1 210 ? 6.181  11.945  -5.291  1.00 16.07 ? 211 LEU A CB  1 
ATOM   1650 C CG  . LEU A 1 210 ? 6.229  13.470  -5.211  1.00 16.87 ? 211 LEU A CG  1 
ATOM   1651 C CD1 . LEU A 1 210 ? 7.214  14.043  -6.202  1.00 19.17 ? 211 LEU A CD1 1 
ATOM   1652 C CD2 . LEU A 1 210 ? 4.837  14.025  -5.466  1.00 19.29 ? 211 LEU A CD2 1 
ATOM   1653 N N   . GLU A 1 211 ? 7.899  10.966  -2.860  1.00 16.59 ? 212 GLU A N   1 
ATOM   1654 C CA  . GLU A 1 211 ? 8.579  11.238  -1.595  1.00 17.61 ? 212 GLU A CA  1 
ATOM   1655 C C   . GLU A 1 211 ? 10.027 10.766  -1.627  1.00 15.84 ? 212 GLU A C   1 
ATOM   1656 O O   . GLU A 1 211 ? 10.916 11.433  -1.092  1.00 17.13 ? 212 GLU A O   1 
ATOM   1657 C CB  . GLU A 1 211 ? 7.836  10.581  -0.431  1.00 20.89 ? 212 GLU A CB  1 
ATOM   1658 C CG  . GLU A 1 211 ? 6.392  11.025  -0.244  1.00 24.85 ? 212 GLU A CG  1 
ATOM   1659 C CD  . GLU A 1 211 ? 5.625  10.094  0.694   1.00 28.88 ? 212 GLU A CD  1 
ATOM   1660 O OE1 . GLU A 1 211 ? 4.589  10.518  1.241   1.00 39.61 ? 212 GLU A OE1 1 
ATOM   1661 O OE2 . GLU A 1 211 ? 6.071  8.940   0.896   1.00 38.22 ? 212 GLU A OE2 1 
ATOM   1662 N N   . ALA A 1 212 ? 10.279 9.599   -2.230  1.00 16.06 ? 213 ALA A N   1 
ATOM   1663 C CA  . ALA A 1 212 ? 11.646 9.103   -2.332  1.00 14.64 ? 213 ALA A CA  1 
ATOM   1664 C C   . ALA A 1 212 ? 12.527 10.039  -3.150  1.00 17.42 ? 213 ALA A C   1 
ATOM   1665 O O   . ALA A 1 212 ? 13.699 10.256  -2.810  1.00 16.25 ? 213 ALA A O   1 
ATOM   1666 C CB  . ALA A 1 212 ? 11.642 7.722   -2.978  1.00 16.92 ? 213 ALA A CB  1 
ATOM   1667 N N   . PHE A 1 213 ? 11.996 10.554  -4.261  1.00 15.55 ? 214 PHE A N   1 
ATOM   1668 C CA  . PHE A 1 213 ? 12.756 11.500  -5.071  1.00 15.12 ? 214 PHE A CA  1 
ATOM   1669 C C   . PHE A 1 213 ? 12.978 12.816  -4.338  1.00 17.46 ? 214 PHE A C   1 
ATOM   1670 O O   . PHE A 1 213 ? 14.074 13.378  -4.403  1.00 18.21 ? 214 PHE A O   1 
ATOM   1671 C CB  . PHE A 1 213 ? 12.086 11.689  -6.430  1.00 16.25 ? 214 PHE A CB  1 
ATOM   1672 C CG  . PHE A 1 213 ? 12.115 10.450  -7.276  1.00 16.38 ? 214 PHE A CG  1 
ATOM   1673 C CD1 . PHE A 1 213 ? 13.298 9.745   -7.430  1.00 17.33 ? 214 PHE A CD1 1 
ATOM   1674 C CD2 . PHE A 1 213 ? 10.972 9.968   -7.898  1.00 16.77 ? 214 PHE A CD2 1 
ATOM   1675 C CE1 . PHE A 1 213 ? 13.337 8.582   -8.196  1.00 16.31 ? 214 PHE A CE1 1 
ATOM   1676 C CE2 . PHE A 1 213 ? 11.016 8.803   -8.672  1.00 16.80 ? 214 PHE A CE2 1 
ATOM   1677 C CZ  . PHE A 1 213 ? 12.202 8.118   -8.814  1.00 15.94 ? 214 PHE A CZ  1 
ATOM   1678 N N   . LEU A 1 214 ? 11.981 13.290  -3.589  1.00 15.36 ? 215 LEU A N   1 
ATOM   1679 C CA  . LEU A 1 214 ? 12.206 14.498  -2.793  1.00 16.46 ? 215 LEU A CA  1 
ATOM   1680 C C   . LEU A 1 214 ? 13.204 14.267  -1.665  1.00 20.25 ? 215 LEU A C   1 
ATOM   1681 O O   . LEU A 1 214 ? 13.821 15.224  -1.192  1.00 24.12 ? 215 LEU A O   1 
ATOM   1682 C CB  . LEU A 1 214 ? 10.884 15.024  -2.245  1.00 17.85 ? 215 LEU A CB  1 
ATOM   1683 C CG  . LEU A 1 214 ? 9.936  15.447  -3.361  1.00 19.46 ? 215 LEU A CG  1 
ATOM   1684 C CD1 . LEU A 1 214 ? 8.532  15.672  -2.798  1.00 20.61 ? 215 LEU A CD1 1 
ATOM   1685 C CD2 . LEU A 1 214 ? 10.464 16.695  -4.077  1.00 21.07 ? 215 LEU A CD2 1 
ATOM   1686 N N   . ALA A 1 215 ? 13.382 13.019  -1.232  1.00 17.04 ? 216 ALA A N   1 
ATOM   1687 C CA  . ALA A 1 215 ? 14.387 12.686  -0.236  1.00 19.96 ? 216 ALA A CA  1 
ATOM   1688 C C   . ALA A 1 215 ? 15.788 12.603  -0.823  1.00 16.36 ? 216 ALA A C   1 
ATOM   1689 O O   . ALA A 1 215 ? 16.759 12.512  -0.064  1.00 19.88 ? 216 ALA A O   1 
ATOM   1690 C CB  . ALA A 1 215 ? 14.025 11.357  0.434   1.00 17.94 ? 216 ALA A CB  1 
ATOM   1691 N N   . GLY A 1 216 ? 15.921 12.630  -2.147  1.00 16.94 ? 217 GLY A N   1 
ATOM   1692 C CA  . GLY A 1 216 ? 17.221 12.609  -2.800  1.00 18.85 ? 217 GLY A CA  1 
ATOM   1693 C C   . GLY A 1 216 ? 17.501 11.379  -3.646  1.00 15.33 ? 217 GLY A C   1 
ATOM   1694 O O   . GLY A 1 216 ? 18.577 11.298  -4.254  1.00 16.95 ? 217 GLY A O   1 
ATOM   1695 N N   . ALA A 1 217 ? 16.603 10.408  -3.738  1.00 16.57 ? 218 ALA A N   1 
ATOM   1696 C CA  . ALA A 1 217 ? 16.898 9.246   -4.564  1.00 16.94 ? 218 ALA A CA  1 
ATOM   1697 C C   . ALA A 1 217 ? 17.007 9.653   -6.028  1.00 15.35 ? 218 ALA A C   1 
ATOM   1698 O O   . ALA A 1 217 ? 16.297 10.548  -6.497  1.00 16.76 ? 218 ALA A O   1 
ATOM   1699 C CB  . ALA A 1 217 ? 15.792 8.203   -4.407  1.00 17.02 ? 218 ALA A CB  1 
ATOM   1700 N N   . ASP A 1 218 ? 17.914 8.990   -6.749  1.00 15.32 ? 219 ASP A N   1 
ATOM   1701 C CA  . ASP A 1 218 ? 18.046 9.167   -8.191  1.00 16.33 ? 219 ASP A CA  1 
ATOM   1702 C C   . ASP A 1 218 ? 17.208 8.180   -8.990  1.00 18.23 ? 219 ASP A C   1 
ATOM   1703 O O   . ASP A 1 218 ? 16.931 8.417   -10.174 1.00 17.39 ? 219 ASP A O   1 
ATOM   1704 C CB  . ASP A 1 218 ? 19.515 9.042   -8.591  1.00 17.40 ? 219 ASP A CB  1 
ATOM   1705 C CG  . ASP A 1 218 ? 20.381 10.055  -7.883  1.00 19.00 ? 219 ASP A CG  1 
ATOM   1706 O OD1 . ASP A 1 218 ? 20.392 11.232  -8.317  1.00 25.22 ? 219 ASP A OD1 1 
ATOM   1707 O OD2 . ASP A 1 218 ? 21.032 9.692   -6.882  1.00 19.69 ? 219 ASP A OD2 1 
ATOM   1708 N N   . ALA A 1 219 ? 16.807 7.076   -8.371  1.00 15.17 ? 220 ALA A N   1 
ATOM   1709 C CA  . ALA A 1 219 ? 15.998 6.066   -9.020  1.00 17.14 ? 220 ALA A CA  1 
ATOM   1710 C C   . ALA A 1 219 ? 15.193 5.381   -7.937  1.00 14.15 ? 220 ALA A C   1 
ATOM   1711 O O   . ALA A 1 219 ? 15.551 5.417   -6.755  1.00 15.66 ? 220 ALA A O   1 
ATOM   1712 C CB  . ALA A 1 219 ? 16.874 5.018   -9.719  1.00 16.37 ? 220 ALA A CB  1 
ATOM   1713 N N   . ALA A 1 220 ? 14.102 4.756   -8.347  1.00 15.37 ? 221 ALA A N   1 
ATOM   1714 C CA  . ALA A 1 220 ? 13.259 4.037   -7.410  1.00 15.43 ? 221 ALA A CA  1 
ATOM   1715 C C   . ALA A 1 220 ? 12.969 2.667   -7.989  1.00 16.39 ? 221 ALA A C   1 
ATOM   1716 O O   . ALA A 1 220 ? 12.580 2.547   -9.158  1.00 16.64 ? 221 ALA A O   1 
ATOM   1717 C CB  . ALA A 1 220 ? 11.970 4.798   -7.128  1.00 17.13 ? 221 ALA A CB  1 
ATOM   1718 N N   A LEU A 1 221 ? 13.166 1.644   -7.166  0.73 15.87 ? 222 LEU A N   1 
ATOM   1719 N N   B LEU A 1 221 ? 13.151 1.639   -7.164  0.27 15.95 ? 222 LEU A N   1 
ATOM   1720 C CA  A LEU A 1 221 ? 13.025 0.253   -7.549  0.73 17.81 ? 222 LEU A CA  1 
ATOM   1721 C CA  B LEU A 1 221 ? 13.043 0.245   -7.565  0.27 17.79 ? 222 LEU A CA  1 
ATOM   1722 C C   A LEU A 1 221 ? 11.781 -0.328  -6.890  0.73 17.85 ? 222 LEU A C   1 
ATOM   1723 C C   B LEU A 1 221 ? 11.856 -0.404  -6.867  0.27 17.83 ? 222 LEU A C   1 
ATOM   1724 O O   A LEU A 1 221 ? 11.465 -0.012  -5.741  0.73 17.50 ? 222 LEU A O   1 
ATOM   1725 O O   B LEU A 1 221 ? 11.648 -0.207  -5.666  0.27 17.41 ? 222 LEU A O   1 
ATOM   1726 C CB  A LEU A 1 221 ? 14.273 -0.509  -7.093  0.73 18.64 ? 222 LEU A CB  1 
ATOM   1727 C CB  B LEU A 1 221 ? 14.321 -0.497  -7.165  0.27 18.57 ? 222 LEU A CB  1 
ATOM   1728 C CG  A LEU A 1 221 ? 14.380 -2.010  -7.323  0.73 17.89 ? 222 LEU A CG  1 
ATOM   1729 C CG  B LEU A 1 221 ? 14.358 -2.007  -7.377  0.27 17.91 ? 222 LEU A CG  1 
ATOM   1730 C CD1 A LEU A 1 221 ? 15.832 -2.383  -7.508  0.73 21.95 ? 222 LEU A CD1 1 
ATOM   1731 C CD1 B LEU A 1 221 ? 14.345 -2.295  -8.850  0.27 18.31 ? 222 LEU A CD1 1 
ATOM   1732 C CD2 A LEU A 1 221 ? 13.780 -2.750  -6.138  0.73 18.17 ? 222 LEU A CD2 1 
ATOM   1733 C CD2 B LEU A 1 221 ? 15.581 -2.622  -6.716  0.27 19.25 ? 222 LEU A CD2 1 
ATOM   1734 N N   . ALA A 1 222 ? 11.081 -1.184  -7.618  1.00 16.44 ? 223 ALA A N   1 
ATOM   1735 C CA  . ALA A 1 222 ? 9.953  -1.903  -7.043  1.00 15.14 ? 223 ALA A CA  1 
ATOM   1736 C C   . ALA A 1 222 ? 9.756  -3.189  -7.828  1.00 15.45 ? 223 ALA A C   1 
ATOM   1737 O O   . ALA A 1 222 ? 10.338 -3.384  -8.897  1.00 15.96 ? 223 ALA A O   1 
ATOM   1738 C CB  . ALA A 1 222 ? 8.670  -1.055  -7.014  1.00 17.20 ? 223 ALA A CB  1 
ATOM   1739 N N   . ALA A 1 223 ? 8.882  -4.050  -7.303  1.00 16.38 ? 224 ALA A N   1 
ATOM   1740 C CA  . ALA A 1 223 ? 8.678  -5.382  -7.863  1.00 17.34 ? 224 ALA A CA  1 
ATOM   1741 C C   . ALA A 1 223 ? 7.197  -5.712  -7.919  1.00 17.61 ? 224 ALA A C   1 
ATOM   1742 O O   . ALA A 1 223 ? 6.528  -5.403  -8.912  1.00 15.73 ? 224 ALA A O   1 
ATOM   1743 C CB  . ALA A 1 223 ? 9.439  -6.439  -7.052  1.00 20.24 ? 224 ALA A CB  1 
ATOM   1744 N N   . SER A 1 224 ? 6.673  -6.318  -6.845  1.00 17.99 ? 225 SER A N   1 
ATOM   1745 C CA  . SER A 1 224 ? 5.291  -6.804  -6.859  1.00 17.56 ? 225 SER A CA  1 
ATOM   1746 C C   . SER A 1 224 ? 4.276  -5.697  -7.141  1.00 17.51 ? 225 SER A C   1 
ATOM   1747 O O   . SER A 1 224 ? 3.251  -5.958  -7.779  1.00 16.92 ? 225 SER A O   1 
ATOM   1748 C CB  . SER A 1 224 ? 4.963  -7.522  -5.554  1.00 20.74 ? 225 SER A CB  1 
ATOM   1749 O OG  . SER A 1 224 ? 4.897  -6.613  -4.474  1.00 30.05 ? 225 SER A OG  1 
ATOM   1750 N N   . VAL A 1 225 ? 4.513  -4.467  -6.668  1.00 16.32 ? 226 VAL A N   1 
ATOM   1751 C CA  . VAL A 1 225 ? 3.541  -3.415  -6.972  1.00 17.51 ? 226 VAL A CA  1 
ATOM   1752 C C   . VAL A 1 225 ? 3.432  -3.189  -8.476  1.00 15.71 ? 226 VAL A C   1 
ATOM   1753 O O   . VAL A 1 225 ? 2.350  -2.873  -8.987  1.00 17.48 ? 226 VAL A O   1 
ATOM   1754 C CB  . VAL A 1 225 ? 3.778  -2.110  -6.181  1.00 22.14 ? 226 VAL A CB  1 
ATOM   1755 C CG1 . VAL A 1 225 ? 3.684  -2.370  -4.675  1.00 24.60 ? 226 VAL A CG1 1 
ATOM   1756 C CG2 . VAL A 1 225 ? 5.101  -1.480  -6.557  1.00 20.94 ? 226 VAL A CG2 1 
ATOM   1757 N N   . PHE A 1 226 ? 4.538  -3.366  -9.214  1.00 14.68 ? 227 PHE A N   1 
ATOM   1758 C CA  . PHE A 1 226 ? 4.462  -3.308  -10.667 1.00 14.70 ? 227 PHE A CA  1 
ATOM   1759 C C   . PHE A 1 226 ? 3.853  -4.588  -11.235 1.00 16.71 ? 227 PHE A C   1 
ATOM   1760 O O   . PHE A 1 226 ? 2.969  -4.531  -12.096 1.00 16.84 ? 227 PHE A O   1 
ATOM   1761 C CB  . PHE A 1 226 ? 5.856  -3.081  -11.280 1.00 15.73 ? 227 PHE A CB  1 
ATOM   1762 C CG  . PHE A 1 226 ? 6.473  -1.725  -10.984 1.00 15.85 ? 227 PHE A CG  1 
ATOM   1763 C CD1 . PHE A 1 226 ? 5.707  -0.580  -10.871 1.00 20.69 ? 227 PHE A CD1 1 
ATOM   1764 C CD2 . PHE A 1 226 ? 7.841  -1.620  -10.836 1.00 18.58 ? 227 PHE A CD2 1 
ATOM   1765 C CE1 . PHE A 1 226 ? 6.296  0.654   -10.609 1.00 20.01 ? 227 PHE A CE1 1 
ATOM   1766 C CE2 . PHE A 1 226 ? 8.428  -0.400  -10.574 1.00 17.70 ? 227 PHE A CE2 1 
ATOM   1767 C CZ  . PHE A 1 226 ? 7.660  0.734   -10.459 1.00 18.85 ? 227 PHE A CZ  1 
ATOM   1768 N N   . HIS A 1 227 ? 4.294  -5.752  -10.744 1.00 15.40 ? 228 HIS A N   1 
ATOM   1769 C CA  . HIS A 1 227 ? 3.819  -7.016  -11.310 1.00 16.46 ? 228 HIS A CA  1 
ATOM   1770 C C   . HIS A 1 227 ? 2.304  -7.143  -11.214 1.00 17.48 ? 228 HIS A C   1 
ATOM   1771 O O   . HIS A 1 227 ? 1.658  -7.669  -12.131 1.00 17.06 ? 228 HIS A O   1 
ATOM   1772 C CB  . HIS A 1 227 ? 4.410  -8.212  -10.566 1.00 16.99 ? 228 HIS A CB  1 
ATOM   1773 C CG  . HIS A 1 227 ? 5.899  -8.253  -10.515 1.00 17.17 ? 228 HIS A CG  1 
ATOM   1774 N ND1 . HIS A 1 227 ? 6.718  -7.711  -11.485 1.00 19.13 ? 228 HIS A ND1 1 
ATOM   1775 C CD2 . HIS A 1 227 ? 6.717  -8.819  -9.601  1.00 15.16 ? 228 HIS A CD2 1 
ATOM   1776 C CE1 . HIS A 1 227 ? 7.980  -7.924  -11.155 1.00 20.26 ? 228 HIS A CE1 1 
ATOM   1777 N NE2 . HIS A 1 227 ? 8.006  -8.608  -10.022 1.00 17.38 ? 228 HIS A NE2 1 
ATOM   1778 N N   . PHE A 1 228 ? 1.728  -6.731  -10.083 1.00 16.17 ? 229 PHE A N   1 
ATOM   1779 C CA  . PHE A 1 228 ? 0.298  -6.835  -9.824  1.00 16.07 ? 229 PHE A CA  1 
ATOM   1780 C C   . PHE A 1 228 ? -0.485 -5.681  -10.413 1.00 18.54 ? 229 PHE A C   1 
ATOM   1781 O O   . PHE A 1 228 ? -1.716 -5.682  -10.319 1.00 18.81 ? 229 PHE A O   1 
ATOM   1782 C CB  . PHE A 1 228 ? 0.052  -6.850  -8.313  1.00 19.46 ? 229 PHE A CB  1 
ATOM   1783 C CG  . PHE A 1 228 ? 0.294  -8.183  -7.657  1.00 19.18 ? 229 PHE A CG  1 
ATOM   1784 C CD1 . PHE A 1 228 ? -0.120 -9.361  -8.259  1.00 22.32 ? 229 PHE A CD1 1 
ATOM   1785 C CD2 . PHE A 1 228 ? 0.881  -8.242  -6.406  1.00 24.00 ? 229 PHE A CD2 1 
ATOM   1786 C CE1 . PHE A 1 228 ? 0.088  -10.589 -7.634  1.00 26.68 ? 229 PHE A CE1 1 
ATOM   1787 C CE2 . PHE A 1 228 ? 1.088  -9.457  -5.772  1.00 27.36 ? 229 PHE A CE2 1 
ATOM   1788 C CZ  . PHE A 1 228 ? 0.689  -10.634 -6.390  1.00 24.67 ? 229 PHE A CZ  1 
ATOM   1789 N N   . ARG A 1 229 ? 0.189  -4.685  -10.987 1.00 17.04 ? 230 ARG A N   1 
ATOM   1790 C CA  . ARG A 1 229 ? -0.459 -3.496  -11.534 1.00 20.57 ? 230 ARG A CA  1 
ATOM   1791 C C   . ARG A 1 229 ? -1.126 -2.670  -10.441 1.00 19.76 ? 230 ARG A C   1 
ATOM   1792 O O   . ARG A 1 229 ? -2.137 -2.006  -10.675 1.00 22.22 ? 230 ARG A O   1 
ATOM   1793 C CB  . ARG A 1 229 ? -1.415 -3.818  -12.690 1.00 23.87 ? 230 ARG A CB  1 
ATOM   1794 C CG  . ARG A 1 229 ? -0.892 -4.899  -13.631 1.00 28.66 ? 230 ARG A CG  1 
ATOM   1795 C CD  . ARG A 1 229 ? -1.813 -5.095  -14.812 1.00 36.28 ? 230 ARG A CD  1 
ATOM   1796 N NE  . ARG A 1 229 ? -1.919 -3.874  -15.601 1.00 38.11 ? 230 ARG A NE  1 
ATOM   1797 C CZ  . ARG A 1 229 ? -2.290 -3.839  -16.875 1.00 41.95 ? 230 ARG A CZ  1 
ATOM   1798 N NH1 . ARG A 1 229 ? -2.595 -4.965  -17.508 1.00 51.56 ? 230 ARG A NH1 1 
ATOM   1799 N NH2 . ARG A 1 229 ? -2.356 -2.681  -17.514 1.00 47.31 ? 230 ARG A NH2 1 
ATOM   1800 N N   . GLU A 1 230 ? -0.565 -2.715  -9.236  1.00 17.67 ? 231 GLU A N   1 
ATOM   1801 C CA  . GLU A 1 230 ? -0.967 -1.783  -8.194  1.00 18.04 ? 231 GLU A CA  1 
ATOM   1802 C C   . GLU A 1 230 ? -0.419 -0.392  -8.456  1.00 19.40 ? 231 GLU A C   1 
ATOM   1803 O O   . GLU A 1 230 ? -0.971 0.591   -7.949  1.00 21.91 ? 231 GLU A O   1 
ATOM   1804 C CB  . GLU A 1 230 ? -0.540 -2.304  -6.824  1.00 20.81 ? 231 GLU A CB  1 
ATOM   1805 C CG  . GLU A 1 230 ? -1.301 -3.568  -6.430  1.00 20.40 ? 231 GLU A CG  1 
ATOM   1806 C CD  . GLU A 1 230 ? -0.700 -4.325  -5.265  1.00 25.30 ? 231 GLU A CD  1 
ATOM   1807 O OE1 . GLU A 1 230 ? 0.255  -3.827  -4.629  1.00 28.17 ? 231 GLU A OE1 1 
ATOM   1808 O OE2 . GLU A 1 230 ? -1.201 -5.436  -4.979  1.00 25.69 ? 231 GLU A OE2 1 
ATOM   1809 N N   . ILE A 1 231 ? 0.665  -0.304  -9.222  1.00 17.70 ? 232 ILE A N   1 
ATOM   1810 C CA  . ILE A 1 231 ? 1.182  0.938   -9.772  1.00 18.92 ? 232 ILE A CA  1 
ATOM   1811 C C   . ILE A 1 231 ? 1.439  0.706   -11.253 1.00 19.92 ? 232 ILE A C   1 
ATOM   1812 O O   . ILE A 1 231 ? 2.079  -0.282  -11.630 1.00 19.70 ? 232 ILE A O   1 
ATOM   1813 C CB  . ILE A 1 231 ? 2.468  1.374   -9.057  1.00 20.50 ? 232 ILE A CB  1 
ATOM   1814 C CG1 . ILE A 1 231 ? 2.125  1.739   -7.608  1.00 27.66 ? 232 ILE A CG1 1 
ATOM   1815 C CG2 . ILE A 1 231 ? 3.100  2.559   -9.793  1.00 22.68 ? 232 ILE A CG2 1 
ATOM   1816 C CD1 . ILE A 1 231 ? 3.292  2.181   -6.784  1.00 27.59 ? 232 ILE A CD1 1 
ATOM   1817 N N   . ASP A 1 232 ? 0.910  1.592   -12.086 1.00 17.22 ? 233 ASP A N   1 
ATOM   1818 C CA  . ASP A 1 232 ? 1.108  1.543   -13.525 1.00 16.86 ? 233 ASP A CA  1 
ATOM   1819 C C   . ASP A 1 232 ? 2.267  2.467   -13.889 1.00 16.86 ? 233 ASP A C   1 
ATOM   1820 O O   . ASP A 1 232 ? 2.331  3.607   -13.414 1.00 18.55 ? 233 ASP A O   1 
ATOM   1821 C CB  . ASP A 1 232 ? -0.178 1.995   -14.219 1.00 21.00 ? 233 ASP A CB  1 
ATOM   1822 C CG  . ASP A 1 232 ? -0.072 1.927   -15.720 1.00 24.25 ? 233 ASP A CG  1 
ATOM   1823 O OD1 . ASP A 1 232 ? -0.341 0.842   -16.279 1.00 28.06 ? 233 ASP A OD1 1 
ATOM   1824 O OD2 . ASP A 1 232 ? 0.307  2.948   -16.339 1.00 23.58 ? 233 ASP A OD2 1 
ATOM   1825 N N   . VAL A 1 233 ? 3.198  1.967   -14.707 1.00 18.59 ? 234 VAL A N   1 
ATOM   1826 C CA  . VAL A 1 233 ? 4.427  2.716   -14.968 1.00 18.92 ? 234 VAL A CA  1 
ATOM   1827 C C   . VAL A 1 233 ? 4.125  4.031   -15.681 1.00 19.46 ? 234 VAL A C   1 
ATOM   1828 O O   . VAL A 1 233 ? 4.653  5.087   -15.317 1.00 18.66 ? 234 VAL A O   1 
ATOM   1829 C CB  . VAL A 1 233 ? 5.440  1.856   -15.741 1.00 19.43 ? 234 VAL A CB  1 
ATOM   1830 C CG1 . VAL A 1 233 ? 6.653  2.695   -16.106 1.00 21.22 ? 234 VAL A CG1 1 
ATOM   1831 C CG2 . VAL A 1 233 ? 5.832  0.633   -14.915 1.00 20.64 ? 234 VAL A CG2 1 
ATOM   1832 N N   . ARG A 1 234 ? 3.272  3.991   -16.705 1.00 21.08 ? 235 ARG A N   1 
ATOM   1833 C CA  . ARG A 1 234 ? 2.943  5.223   -17.418 1.00 20.43 ? 235 ARG A CA  1 
ATOM   1834 C C   . ARG A 1 234 ? 2.243  6.214   -16.497 1.00 20.23 ? 235 ARG A C   1 
ATOM   1835 O O   . ARG A 1 234 ? 2.586  7.403   -16.471 1.00 19.52 ? 235 ARG A O   1 
ATOM   1836 C CB  . ARG A 1 234 ? 2.081  4.910   -18.640 1.00 22.22 ? 235 ARG A CB  1 
ATOM   1837 C CG  . ARG A 1 234 ? 1.459  6.150   -19.291 1.00 26.02 ? 235 ARG A CG  1 
ATOM   1838 C CD  . ARG A 1 234 ? 0.598  5.783   -20.505 1.00 27.06 ? 235 ARG A CD  1 
ATOM   1839 N NE  . ARG A 1 234 ? 1.329  4.977   -21.485 1.00 26.95 ? 235 ARG A NE  1 
ATOM   1840 C CZ  . ARG A 1 234 ? 2.114  5.478   -22.436 1.00 33.64 ? 235 ARG A CZ  1 
ATOM   1841 N NH1 . ARG A 1 234 ? 2.271  6.791   -22.556 1.00 32.21 ? 235 ARG A NH1 1 
ATOM   1842 N NH2 . ARG A 1 234 ? 2.741  4.667   -23.275 1.00 33.66 ? 235 ARG A NH2 1 
ATOM   1843 N N   A GLU A 1 235 ? 1.257  5.746   -15.729 0.47 19.51 ? 236 GLU A N   1 
ATOM   1844 N N   B GLU A 1 235 ? 1.244  5.744   -15.741 0.53 19.50 ? 236 GLU A N   1 
ATOM   1845 C CA  A GLU A 1 235 ? 0.558  6.646   -14.818 0.47 18.86 ? 236 GLU A CA  1 
ATOM   1846 C CA  B GLU A 1 235 ? 0.546  6.623   -14.807 0.53 18.85 ? 236 GLU A CA  1 
ATOM   1847 C C   A GLU A 1 235 ? 1.502  7.216   -13.771 0.47 19.51 ? 236 GLU A C   1 
ATOM   1848 C C   B GLU A 1 235 ? 1.507  7.214   -13.785 0.53 19.51 ? 236 GLU A C   1 
ATOM   1849 O O   A GLU A 1 235 ? 1.404  8.396   -13.407 0.47 18.50 ? 236 GLU A O   1 
ATOM   1850 O O   B GLU A 1 235 ? 1.429  8.407   -13.459 0.53 18.50 ? 236 GLU A O   1 
ATOM   1851 C CB  A GLU A 1 235 ? -0.605 5.923   -14.147 0.47 20.91 ? 236 GLU A CB  1 
ATOM   1852 C CB  B GLU A 1 235 ? -0.573 5.857   -14.100 0.53 20.90 ? 236 GLU A CB  1 
ATOM   1853 C CG  A GLU A 1 235 ? -1.474 6.846   -13.327 0.47 22.00 ? 236 GLU A CG  1 
ATOM   1854 C CG  B GLU A 1 235 ? -1.724 5.421   -15.006 0.53 22.69 ? 236 GLU A CG  1 
ATOM   1855 C CD  A GLU A 1 235 ? -2.747 6.181   -12.854 0.47 26.60 ? 236 GLU A CD  1 
ATOM   1856 C CD  B GLU A 1 235 ? -2.646 6.565   -15.388 0.53 29.00 ? 236 GLU A CD  1 
ATOM   1857 O OE1 A GLU A 1 235 ? -2.983 5.014   -13.232 0.47 30.42 ? 236 GLU A OE1 1 
ATOM   1858 O OE1 B GLU A 1 235 ? -2.574 7.630   -14.742 0.53 27.27 ? 236 GLU A OE1 1 
ATOM   1859 O OE2 A GLU A 1 235 ? -3.512 6.828   -12.110 0.47 31.89 ? 236 GLU A OE2 1 
ATOM   1860 O OE2 B GLU A 1 235 ? -3.449 6.393   -16.333 0.53 33.72 ? 236 GLU A OE2 1 
ATOM   1861 N N   . LEU A 1 236 ? 2.422  6.392   -13.270 1.00 17.40 ? 237 LEU A N   1 
ATOM   1862 C CA  . LEU A 1 236 ? 3.411  6.875   -12.314 1.00 18.61 ? 237 LEU A CA  1 
ATOM   1863 C C   . LEU A 1 236 ? 4.275  7.965   -12.927 1.00 16.27 ? 237 LEU A C   1 
ATOM   1864 O O   . LEU A 1 236 ? 4.490  9.016   -12.317 1.00 15.42 ? 237 LEU A O   1 
ATOM   1865 C CB  . LEU A 1 236 ? 4.281  5.709   -11.840 1.00 16.68 ? 237 LEU A CB  1 
ATOM   1866 C CG  . LEU A 1 236 ? 5.473  6.075   -10.951 1.00 16.20 ? 237 LEU A CG  1 
ATOM   1867 C CD1 . LEU A 1 236 ? 5.040  6.656   -9.632  1.00 17.04 ? 237 LEU A CD1 1 
ATOM   1868 C CD2 . LEU A 1 236 ? 6.339  4.840   -10.699 1.00 16.37 ? 237 LEU A CD2 1 
ATOM   1869 N N   . LYS A 1 237 ? 4.769  7.746   -14.145 1.00 18.45 ? 238 LYS A N   1 
ATOM   1870 C CA  . LYS A 1 237 ? 5.623  8.758   -14.756 1.00 16.82 ? 238 LYS A CA  1 
ATOM   1871 C C   . LYS A 1 237 ? 4.858  10.051  -15.017 1.00 19.69 ? 238 LYS A C   1 
ATOM   1872 O O   . LYS A 1 237 ? 5.393  11.140  -14.790 1.00 18.70 ? 238 LYS A O   1 
ATOM   1873 C CB  . LYS A 1 237 ? 6.295  8.221   -16.018 1.00 18.90 ? 238 LYS A CB  1 
ATOM   1874 C CG  . LYS A 1 237 ? 7.435  7.248   -15.714 1.00 17.63 ? 238 LYS A CG  1 
ATOM   1875 C CD  . LYS A 1 237 ? 8.151  6.847   -16.969 1.00 20.60 ? 238 LYS A CD  1 
ATOM   1876 C CE  . LYS A 1 237 ? 9.495  6.182   -16.648 1.00 20.30 ? 238 LYS A CE  1 
ATOM   1877 N NZ  . LYS A 1 237 ? 10.275 6.011   -17.904 1.00 23.09 ? 238 LYS A NZ  1 
ATOM   1878 N N   . GLU A 1 238 ? 3.601  9.949   -15.467 1.00 17.18 ? 239 GLU A N   1 
ATOM   1879 C CA  . GLU A 1 238 ? 2.792  11.152  -15.671 1.00 17.82 ? 239 GLU A CA  1 
ATOM   1880 C C   . GLU A 1 238 ? 2.570  11.889  -14.356 1.00 19.02 ? 239 GLU A C   1 
ATOM   1881 O O   . GLU A 1 238 ? 2.642  13.125  -14.307 1.00 19.26 ? 239 GLU A O   1 
ATOM   1882 C CB  . GLU A 1 238 ? 1.453  10.790  -16.316 1.00 20.34 ? 239 GLU A CB  1 
ATOM   1883 C CG  . GLU A 1 238 ? 1.536  10.322  -17.762 1.00 25.69 ? 239 GLU A CG  1 
ATOM   1884 C CD  . GLU A 1 238 ? 1.851  11.443  -18.734 1.00 39.69 ? 239 GLU A CD  1 
ATOM   1885 O OE1 . GLU A 1 238 ? 1.824  12.626  -18.323 1.00 34.63 ? 239 GLU A OE1 1 
ATOM   1886 O OE2 . GLU A 1 238 ? 2.124  11.138  -19.915 1.00 40.78 ? 239 GLU A OE2 1 
ATOM   1887 N N   . TYR A 1 239 ? 2.278  11.144  -13.288 1.00 18.13 ? 240 TYR A N   1 
ATOM   1888 C CA  . TYR A 1 239 ? 2.092  11.717  -11.957 1.00 17.03 ? 240 TYR A CA  1 
ATOM   1889 C C   . TYR A 1 239 ? 3.353  12.431  -11.486 1.00 17.26 ? 240 TYR A C   1 
ATOM   1890 O O   . TYR A 1 239 ? 3.297  13.553  -10.967 1.00 16.72 ? 240 TYR A O   1 
ATOM   1891 C CB  . TYR A 1 239 ? 1.726  10.582  -10.999 1.00 16.12 ? 240 TYR A CB  1 
ATOM   1892 C CG  . TYR A 1 239 ? 1.704  10.893  -9.512  1.00 16.47 ? 240 TYR A CG  1 
ATOM   1893 C CD1 . TYR A 1 239 ? 2.841  10.770  -8.731  1.00 16.94 ? 240 TYR A CD1 1 
ATOM   1894 C CD2 . TYR A 1 239 ? 0.530  11.271  -8.882  1.00 18.08 ? 240 TYR A CD2 1 
ATOM   1895 C CE1 . TYR A 1 239 ? 2.812  11.024  -7.368  1.00 16.25 ? 240 TYR A CE1 1 
ATOM   1896 C CE2 . TYR A 1 239 ? 0.493  11.529  -7.517  1.00 19.13 ? 240 TYR A CE2 1 
ATOM   1897 C CZ  . TYR A 1 239 ? 1.642  11.418  -6.771  1.00 17.73 ? 240 TYR A CZ  1 
ATOM   1898 O OH  . TYR A 1 239 ? 1.605  11.665  -5.421  1.00 20.73 ? 240 TYR A OH  1 
ATOM   1899 N N   . LEU A 1 240 ? 4.513  11.798  -11.665 1.00 16.77 ? 241 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 240 ? 5.760  12.426  -11.243 1.00 17.01 ? 241 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 240 ? 6.044  13.689  -12.046 1.00 16.96 ? 241 LEU A C   1 
ATOM   1902 O O   . LEU A 1 240 ? 6.447  14.717  -11.480 1.00 18.99 ? 241 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 240 ? 6.913  11.432  -11.383 1.00 16.50 ? 241 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 240 ? 6.818  10.229  -10.435 1.00 16.20 ? 241 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 240 ? 7.832  9.151   -10.842 1.00 15.71 ? 241 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 240 ? 7.025  10.658  -8.978  1.00 16.85 ? 241 LEU A CD2 1 
ATOM   1907 N N   . LYS A 1 241 ? 5.852  13.630  -13.368 1.00 18.06 ? 242 LYS A N   1 
ATOM   1908 C CA  . LYS A 1 241 ? 6.080  14.807  -14.202 1.00 17.47 ? 242 LYS A CA  1 
ATOM   1909 C C   . LYS A 1 241 ? 5.174  15.955  -13.785 1.00 19.32 ? 242 LYS A C   1 
ATOM   1910 O O   . LYS A 1 241 ? 5.625  17.104  -13.681 1.00 20.03 ? 242 LYS A O   1 
ATOM   1911 C CB  . LYS A 1 241 ? 5.855  14.445  -15.671 1.00 21.99 ? 242 LYS A CB  1 
ATOM   1912 C CG  . LYS A 1 241 ? 6.030  15.592  -16.657 1.00 24.96 ? 242 LYS A CG  1 
ATOM   1913 C CD  . LYS A 1 241 ? 5.465  15.208  -18.024 1.00 36.50 ? 242 LYS A CD  1 
ATOM   1914 C CE  . LYS A 1 241 ? 6.007  16.099  -19.134 1.00 47.31 ? 242 LYS A CE  1 
ATOM   1915 N NZ  . LYS A 1 241 ? 5.459  17.479  -19.054 1.00 54.07 ? 242 LYS A NZ  1 
ATOM   1916 N N   . LYS A 1 242 ? 3.905  15.655  -13.504 1.00 16.76 ? 243 LYS A N   1 
ATOM   1917 C CA  . LYS A 1 242 ? 2.960  16.694  -13.093 1.00 18.58 ? 243 LYS A CA  1 
ATOM   1918 C C   . LYS A 1 242 ? 3.390  17.362  -11.794 1.00 20.22 ? 243 LYS A C   1 
ATOM   1919 O O   . LYS A 1 242 ? 3.167  18.566  -11.612 1.00 20.06 ? 243 LYS A O   1 
ATOM   1920 C CB  . LYS A 1 242 ? 1.561  16.089  -12.949 1.00 21.64 ? 243 LYS A CB  1 
ATOM   1921 C CG  . LYS A 1 242 ? 0.460  17.094  -12.647 1.00 24.93 ? 243 LYS A CG  1 
ATOM   1922 C CD  . LYS A 1 242 ? 0.146  17.947  -13.863 1.00 37.42 ? 243 LYS A CD  1 
ATOM   1923 C CE  . LYS A 1 242 ? -1.357 18.058  -14.078 1.00 50.21 ? 243 LYS A CE  1 
ATOM   1924 N NZ  . LYS A 1 242 ? -2.097 17.991  -12.789 1.00 46.33 ? 243 LYS A NZ  1 
ATOM   1925 N N   . HIS A 1 243 ? 4.013  16.614  -10.890 1.00 18.85 ? 244 HIS A N   1 
ATOM   1926 C CA  . HIS A 1 243 ? 4.453  17.139  -9.607  1.00 19.05 ? 244 HIS A CA  1 
ATOM   1927 C C   . HIS A 1 243 ? 5.852  17.733  -9.650  1.00 17.71 ? 244 HIS A C   1 
ATOM   1928 O O   . HIS A 1 243 ? 6.422  18.021  -8.596  1.00 22.53 ? 244 HIS A O   1 
ATOM   1929 C CB  . HIS A 1 243 ? 4.325  16.065  -8.524  1.00 21.20 ? 244 HIS A CB  1 
ATOM   1930 C CG  . HIS A 1 243 ? 2.907  15.762  -8.160  1.00 20.38 ? 244 HIS A CG  1 
ATOM   1931 N ND1 . HIS A 1 243 ? 2.120  14.897  -8.889  1.00 19.37 ? 244 HIS A ND1 1 
ATOM   1932 C CD2 . HIS A 1 243 ? 2.126  16.222  -7.154  1.00 19.85 ? 244 HIS A CD2 1 
ATOM   1933 C CE1 . HIS A 1 243 ? 0.915  14.840  -8.350  1.00 23.80 ? 244 HIS A CE1 1 
ATOM   1934 N NE2 . HIS A 1 243 ? 0.893  15.635  -7.295  1.00 22.30 ? 244 HIS A NE2 1 
ATOM   1935 N N   . GLY A 1 244 ? 6.426  17.889  -10.833 1.00 17.97 ? 245 GLY A N   1 
ATOM   1936 C CA  . GLY A 1 244 ? 7.681  18.585  -10.982 1.00 21.11 ? 245 GLY A CA  1 
ATOM   1937 C C   . GLY A 1 244 ? 8.923  17.724  -10.958 1.00 22.04 ? 245 GLY A C   1 
ATOM   1938 O O   . GLY A 1 244 ? 10.030 18.273  -10.884 1.00 24.81 ? 245 GLY A O   1 
ATOM   1939 N N   . VAL A 1 245 ? 8.789  16.396  -11.018 1.00 20.71 ? 246 VAL A N   1 
ATOM   1940 C CA  . VAL A 1 245 ? 9.954  15.523  -11.089 1.00 19.66 ? 246 VAL A CA  1 
ATOM   1941 C C   . VAL A 1 245 ? 10.377 15.371  -12.540 1.00 20.42 ? 246 VAL A C   1 
ATOM   1942 O O   . VAL A 1 245 ? 9.540  15.198  -13.439 1.00 22.46 ? 246 VAL A O   1 
ATOM   1943 C CB  . VAL A 1 245 ? 9.653  14.157  -10.447 1.00 18.25 ? 246 VAL A CB  1 
ATOM   1944 C CG1 . VAL A 1 245 ? 10.844 13.220  -10.611 1.00 19.91 ? 246 VAL A CG1 1 
ATOM   1945 C CG2 . VAL A 1 245 ? 9.337  14.333  -9.000  1.00 22.00 ? 246 VAL A CG2 1 
ATOM   1946 N N   . ASN A 1 246 ? 11.684 15.430  -12.771 1.00 19.72 ? 247 ASN A N   1 
ATOM   1947 C CA  . ASN A 1 246 ? 12.251 15.236  -14.100 1.00 22.47 ? 247 ASN A CA  1 
ATOM   1948 C C   . ASN A 1 246 ? 12.395 13.739  -14.326 1.00 24.19 ? 247 ASN A C   1 
ATOM   1949 O O   . ASN A 1 246 ? 13.292 13.100  -13.775 1.00 25.04 ? 247 ASN A O   1 
ATOM   1950 C CB  . ASN A 1 246 ? 13.601 15.937  -14.191 1.00 22.67 ? 247 ASN A CB  1 
ATOM   1951 C CG  . ASN A 1 246 ? 14.172 15.921  -15.592 1.00 34.04 ? 247 ASN A CG  1 
ATOM   1952 O OD1 . ASN A 1 246 ? 13.460 15.662  -16.558 1.00 37.61 ? 247 ASN A OD1 1 
ATOM   1953 N ND2 . ASN A 1 246 ? 15.466 16.200  -15.710 1.00 34.05 ? 247 ASN A ND2 1 
ATOM   1954 N N   . VAL A 1 247 ? 11.500 13.174  -15.132 1.00 22.20 ? 248 VAL A N   1 
ATOM   1955 C CA  . VAL A 1 247 ? 11.492 11.741  -15.391 1.00 21.33 ? 248 VAL A CA  1 
ATOM   1956 C C   . VAL A 1 247 ? 11.769 11.485  -16.865 1.00 26.90 ? 248 VAL A C   1 
ATOM   1957 O O   . VAL A 1 247 ? 11.647 12.371  -17.715 1.00 29.08 ? 248 VAL A O   1 
ATOM   1958 C CB  . VAL A 1 247 ? 10.172 11.066  -14.960 1.00 23.93 ? 248 VAL A CB  1 
ATOM   1959 C CG1 . VAL A 1 247 ? 10.006 11.126  -13.453 1.00 25.55 ? 248 VAL A CG1 1 
ATOM   1960 C CG2 . VAL A 1 247 ? 8.984  11.707  -15.657 1.00 28.36 ? 248 VAL A CG2 1 
ATOM   1961 N N   A ARG A 1 248 ? 12.161 10.246  -17.159 0.61 25.05 ? 249 ARG A N   1 
ATOM   1962 N N   B ARG A 1 248 ? 12.157 10.244  -17.159 0.39 25.09 ? 249 ARG A N   1 
ATOM   1963 C CA  A ARG A 1 248 ? 12.414 9.821   -18.529 0.61 29.03 ? 249 ARG A CA  1 
ATOM   1964 C CA  B ARG A 1 248 ? 12.411 9.819   -18.529 0.39 29.07 ? 249 ARG A CA  1 
ATOM   1965 C C   A ARG A 1 248 ? 11.090 9.424   -19.166 0.61 29.86 ? 249 ARG A C   1 
ATOM   1966 C C   B ARG A 1 248 ? 11.092 9.416   -19.171 0.39 29.88 ? 249 ARG A C   1 
ATOM   1967 O O   A ARG A 1 248 ? 10.419 8.499   -18.695 0.61 29.57 ? 249 ARG A O   1 
ATOM   1968 O O   B ARG A 1 248 ? 10.428 8.481   -18.711 0.39 29.55 ? 249 ARG A O   1 
ATOM   1969 C CB  A ARG A 1 248 ? 13.372 8.631   -18.541 0.61 26.98 ? 249 ARG A CB  1 
ATOM   1970 C CB  B ARG A 1 248 ? 13.391 8.647   -18.546 0.39 27.07 ? 249 ARG A CB  1 
ATOM   1971 C CG  A ARG A 1 248 ? 14.728 8.893   -17.907 0.61 29.84 ? 249 ARG A CG  1 
ATOM   1972 C CG  B ARG A 1 248 ? 14.834 9.066   -18.368 0.39 31.58 ? 249 ARG A CG  1 
ATOM   1973 C CD  A ARG A 1 248 ? 15.641 7.692   -18.106 0.61 31.80 ? 249 ARG A CD  1 
ATOM   1974 C CD  B ARG A 1 248 ? 15.753 7.898   -18.052 0.39 31.83 ? 249 ARG A CD  1 
ATOM   1975 N NE  A ARG A 1 248 ? 17.017 7.942   -17.687 0.61 33.37 ? 249 ARG A NE  1 
ATOM   1976 N NE  B ARG A 1 248 ? 17.110 8.369   -17.785 0.39 33.42 ? 249 ARG A NE  1 
ATOM   1977 C CZ  A ARG A 1 248 ? 18.000 7.052   -17.787 0.61 31.82 ? 249 ARG A CZ  1 
ATOM   1978 C CZ  B ARG A 1 248 ? 17.474 8.942   -16.644 0.39 31.06 ? 249 ARG A CZ  1 
ATOM   1979 N NH1 A ARG A 1 248 ? 17.758 5.849   -18.290 0.61 30.34 ? 249 ARG A NH1 1 
ATOM   1980 N NH1 B ARG A 1 248 ? 16.578 9.096   -15.683 0.39 30.28 ? 249 ARG A NH1 1 
ATOM   1981 N NH2 A ARG A 1 248 ? 19.222 7.363   -17.379 0.61 39.38 ? 249 ARG A NH2 1 
ATOM   1982 N NH2 B ARG A 1 248 ? 18.719 9.359   -16.459 0.39 28.04 ? 249 ARG A NH2 1 
ATOM   1983 N N   . LEU A 1 249 ? 10.712 10.114  -20.236 1.00 29.95 ? 250 LEU A N   1 
ATOM   1984 C CA  . LEU A 1 249 ? 9.426  9.896   -20.879 1.00 36.03 ? 250 LEU A CA  1 
ATOM   1985 C C   . LEU A 1 249 ? 9.548  9.272   -22.262 1.00 39.99 ? 250 LEU A C   1 
ATOM   1986 O O   . LEU A 1 249 ? 8.556  9.215   -22.996 1.00 50.00 ? 250 LEU A O   1 
ATOM   1987 C CB  . LEU A 1 249 ? 8.628  11.199  -20.922 1.00 42.39 ? 250 LEU A CB  1 
ATOM   1988 C CG  . LEU A 1 249 ? 8.127  11.585  -19.527 1.00 40.66 ? 250 LEU A CG  1 
ATOM   1989 C CD1 . LEU A 1 249 ? 8.035  13.096  -19.387 1.00 45.13 ? 250 LEU A CD1 1 
ATOM   1990 C CD2 . LEU A 1 249 ? 6.788  10.924  -19.228 1.00 42.59 ? 250 LEU A CD2 1 
ATOM   1991 N N   . GLU A 1 250 ? 10.733 8.786   -22.635 1.00 45.07 ? 251 GLU A N   1 
ATOM   1992 C CA  . GLU A 1 250 ? 10.884 8.035   -23.881 1.00 51.01 ? 251 GLU A CA  1 
ATOM   1993 C C   . GLU A 1 250 ? 10.329 6.612   -23.708 1.00 50.04 ? 251 GLU A C   1 
ATOM   1994 O O   . GLU A 1 250 ? 11.022 5.602   -23.834 1.00 54.22 ? 251 GLU A O   1 
ATOM   1995 C CB  . GLU A 1 250 ? 12.321 8.108   -24.404 1.00 48.22 ? 251 GLU A CB  1 
ATOM   1996 C CG  . GLU A 1 250 ? 13.379 7.225   -23.720 1.00 46.32 ? 251 GLU A CG  1 
ATOM   1997 C CD  . GLU A 1 250 ? 14.074 7.892   -22.550 1.00 44.39 ? 251 GLU A CD  1 
ATOM   1998 O OE1 . GLU A 1 250 ? 15.035 7.293   -22.019 1.00 45.52 ? 251 GLU A OE1 1 
ATOM   1999 O OE2 . GLU A 1 250 ? 13.665 9.007   -22.162 1.00 47.94 ? 251 GLU A OE2 1 
ATOM   2000 N N   . LEU A 1 251 ? 9.023  6.562   -23.421 1.00 58.79 ? 252 LEU A N   1 
ATOM   2001 C CA  . LEU A 1 251 ? 8.301  5.340   -23.033 1.00 44.72 ? 252 LEU A CA  1 
ATOM   2002 C C   . LEU A 1 251 ? 8.709  4.091   -23.809 1.00 51.18 ? 252 LEU A C   1 
ATOM   2003 O O   . LEU A 1 251 ? 8.365  2.974   -23.419 1.00 48.18 ? 252 LEU A O   1 
ATOM   2004 C CB  . LEU A 1 251 ? 6.781  5.533   -23.171 1.00 46.44 ? 252 LEU A CB  1 
ATOM   2005 C CG  . LEU A 1 251 ? 5.910  6.141   -22.058 1.00 41.45 ? 252 LEU A CG  1 
ATOM   2006 C CD1 . LEU A 1 251 ? 6.143  5.487   -20.693 1.00 39.78 ? 252 LEU A CD1 1 
ATOM   2007 C CD2 . LEU A 1 251 ? 6.063  7.647   -21.964 1.00 52.43 ? 252 LEU A CD2 1 
HETATM 2008 O O   . HOH B 2 .   ? 3.373  12.007  0.340   1.00 39.28 ? 301 HOH A O   1 
HETATM 2009 O O   . HOH B 2 .   ? 18.014 -16.655 -26.855 1.00 41.30 ? 302 HOH A O   1 
HETATM 2010 O O   . HOH B 2 .   ? -2.241 -0.516  -17.736 1.00 41.53 ? 303 HOH A O   1 
HETATM 2011 O O   . HOH B 2 .   ? 12.834 14.664  -18.432 1.00 38.15 ? 304 HOH A O   1 
HETATM 2012 O O   . HOH B 2 .   ? 7.730  -16.501 -23.140 1.00 41.64 ? 305 HOH A O   1 
HETATM 2013 O O   . HOH B 2 .   ? 20.406 -5.702  -25.990 1.00 38.24 ? 306 HOH A O   1 
HETATM 2014 O O   . HOH B 2 .   ? 17.782 -8.502  9.468   1.00 40.90 ? 307 HOH A O   1 
HETATM 2015 O O   . HOH B 2 .   ? 24.904 -1.374  19.939  1.00 47.14 ? 308 HOH A O   1 
HETATM 2016 O O   . HOH B 2 .   ? 19.137 -23.453 -13.000 1.00 38.78 ? 309 HOH A O   1 
HETATM 2017 O O   . HOH B 2 .   ? 40.764 1.828   -15.385 1.00 36.32 ? 310 HOH A O   1 
HETATM 2018 O O   . HOH B 2 .   ? 16.960 8.566   -21.186 1.00 42.98 ? 311 HOH A O   1 
HETATM 2019 O O   . HOH B 2 .   ? 9.258  -7.503  -27.958 1.00 37.85 ? 312 HOH A O   1 
HETATM 2020 O O   . HOH B 2 .   ? 27.004 -15.065 -0.073  1.00 45.23 ? 313 HOH A O   1 
HETATM 2021 O O   . HOH B 2 .   ? 5.565  -14.723 -12.989 1.00 27.91 ? 314 HOH A O   1 
HETATM 2022 O O   . HOH B 2 .   ? 14.240 -2.953  -24.793 1.00 37.80 ? 315 HOH A O   1 
HETATM 2023 O O   . HOH B 2 .   ? -0.740 -5.569  -19.149 1.00 47.85 ? 316 HOH A O   1 
HETATM 2024 O O   . HOH B 2 .   ? 26.702 -19.333 -4.474  1.00 44.32 ? 317 HOH A O   1 
HETATM 2025 O O   . HOH B 2 .   ? -0.760 -7.231  -3.194  1.00 36.90 ? 318 HOH A O   1 
HETATM 2026 O O   . HOH B 2 .   ? 6.054  -7.183  -24.593 1.00 32.48 ? 319 HOH A O   1 
HETATM 2027 O O   . HOH B 2 .   ? 35.100 -18.200 -8.930  1.00 40.50 ? 320 HOH A O   1 
HETATM 2028 O O   . HOH B 2 .   ? 23.388 5.046   -12.833 1.00 39.03 ? 321 HOH A O   1 
HETATM 2029 O O   . HOH B 2 .   ? 18.249 9.260   11.080  1.00 38.27 ? 322 HOH A O   1 
HETATM 2030 O O   . HOH B 2 .   ? 1.114  9.081   -21.004 1.00 39.68 ? 323 HOH A O   1 
HETATM 2031 O O   . HOH B 2 .   ? 12.670 -24.756 -9.661  1.00 40.00 ? 324 HOH A O   1 
HETATM 2032 O O   . HOH B 2 .   ? 0.384  -1.091  -3.256  1.00 40.26 ? 325 HOH A O   1 
HETATM 2033 O O   . HOH B 2 .   ? 28.552 -26.180 -9.720  1.00 39.00 ? 326 HOH A O   1 
HETATM 2034 O O   . HOH B 2 .   ? 10.992 -8.337  -4.689  1.00 37.14 ? 327 HOH A O   1 
HETATM 2035 O O   . HOH B 2 .   ? 36.171 5.741   3.657   1.00 32.27 ? 328 HOH A O   1 
HETATM 2036 O O   . HOH B 2 .   ? 12.451 18.586  -10.029 1.00 41.47 ? 329 HOH A O   1 
HETATM 2037 O O   . HOH B 2 .   ? 23.183 6.223   11.620  1.00 26.13 ? 330 HOH A O   1 
HETATM 2038 O O   . HOH B 2 .   ? 31.440 -17.297 -19.687 1.00 41.19 ? 331 HOH A O   1 
HETATM 2039 O O   . HOH B 2 .   ? 25.991 -12.910 -24.716 1.00 37.85 ? 332 HOH A O   1 
HETATM 2040 O O   . HOH B 2 .   ? 19.826 -1.714  -13.828 1.00 29.95 ? 333 HOH A O   1 
HETATM 2041 O O   . HOH B 2 .   ? -0.322 7.978   -4.307  1.00 25.14 ? 334 HOH A O   1 
HETATM 2042 O O   . HOH B 2 .   ? 10.117 -12.190 -9.640  1.00 30.83 ? 335 HOH A O   1 
HETATM 2043 O O   . HOH B 2 .   ? 22.352 -8.222  2.696   1.00 20.22 ? 336 HOH A O   1 
HETATM 2044 O O   . HOH B 2 .   ? 11.954 8.147   -15.544 1.00 25.87 ? 337 HOH A O   1 
HETATM 2045 O O   . HOH B 2 .   ? 6.180  -10.168 -3.172  1.00 37.61 ? 338 HOH A O   1 
HETATM 2046 O O   . HOH B 2 .   ? 17.486 -3.580  15.056  1.00 36.10 ? 339 HOH A O   1 
HETATM 2047 O O   . HOH B 2 .   ? 8.257  9.760   4.051   1.00 35.64 ? 340 HOH A O   1 
HETATM 2048 O O   . HOH B 2 .   ? 31.908 0.071   12.620  1.00 34.37 ? 341 HOH A O   1 
HETATM 2049 O O   . HOH B 2 .   ? 15.434 -12.559 -5.629  1.00 28.05 ? 342 HOH A O   1 
HETATM 2050 O O   . HOH B 2 .   ? 2.328  -2.190  -13.428 1.00 22.45 ? 343 HOH A O   1 
HETATM 2051 O O   . HOH B 2 .   ? 18.037 -23.740 -7.274  1.00 29.57 ? 344 HOH A O   1 
HETATM 2052 O O   . HOH B 2 .   ? 10.359 -9.494  -8.688  1.00 18.99 ? 345 HOH A O   1 
HETATM 2053 O O   . HOH B 2 .   ? 24.570 -4.612  2.509   1.00 17.72 ? 346 HOH A O   1 
HETATM 2054 O O   . HOH B 2 .   ? 11.529 1.846   -21.451 1.00 33.45 ? 347 HOH A O   1 
HETATM 2055 O O   . HOH B 2 .   ? 25.625 -10.165 -5.984  1.00 20.10 ? 348 HOH A O   1 
HETATM 2056 O O   . HOH B 2 .   ? 39.748 -5.293  0.135   1.00 33.06 ? 349 HOH A O   1 
HETATM 2057 O O   . HOH B 2 .   ? -3.432 -12.111 -9.295  1.00 31.73 ? 350 HOH A O   1 
HETATM 2058 O O   . HOH B 2 .   ? 27.031 -9.980  13.820  1.00 38.62 ? 351 HOH A O   1 
HETATM 2059 O O   . HOH B 2 .   ? 11.319 -19.579 -18.484 1.00 45.08 ? 352 HOH A O   1 
HETATM 2060 O O   . HOH B 2 .   ? 18.510 -24.636 -11.625 1.00 41.03 ? 353 HOH A O   1 
HETATM 2061 O O   . HOH B 2 .   ? 6.479  -3.055  -1.815  1.00 27.59 ? 354 HOH A O   1 
HETATM 2062 O O   . HOH B 2 .   ? 22.695 -14.478 1.193   1.00 34.02 ? 355 HOH A O   1 
HETATM 2063 O O   . HOH B 2 .   ? 2.771  8.700   1.954   1.00 43.95 ? 356 HOH A O   1 
HETATM 2064 O O   . HOH B 2 .   ? 20.935 -3.693  -22.143 1.00 30.93 ? 357 HOH A O   1 
HETATM 2065 O O   . HOH B 2 .   ? 39.288 6.958   -4.425  1.00 38.50 ? 358 HOH A O   1 
HETATM 2066 O O   . HOH B 2 .   ? 20.044 -3.371  -1.685  1.00 20.09 ? 359 HOH A O   1 
HETATM 2067 O O   . HOH B 2 .   ? 21.002 14.110  5.692   1.00 20.15 ? 360 HOH A O   1 
HETATM 2068 O O   . HOH B 2 .   ? 23.933 -4.373  18.449  1.00 38.39 ? 361 HOH A O   1 
HETATM 2069 O O   . HOH B 2 .   ? 23.197 -12.195 -25.914 1.00 32.27 ? 362 HOH A O   1 
HETATM 2070 O O   . HOH B 2 .   ? 18.512 12.394  -9.907  1.00 24.26 ? 363 HOH A O   1 
HETATM 2071 O O   . HOH B 2 .   ? 15.978 14.821  -11.728 1.00 28.44 ? 364 HOH A O   1 
HETATM 2072 O O   . HOH B 2 .   ? 7.778  -20.329 -12.755 1.00 27.06 ? 365 HOH A O   1 
HETATM 2073 O O   . HOH B 2 .   ? 17.937 1.640   16.218  1.00 25.44 ? 366 HOH A O   1 
HETATM 2074 O O   . HOH B 2 .   ? 13.308 17.843  -1.614  1.00 29.37 ? 367 HOH A O   1 
HETATM 2075 O O   . HOH B 2 .   ? 39.228 -8.968  2.754   1.00 29.32 ? 368 HOH A O   1 
HETATM 2076 O O   . HOH B 2 .   ? -0.784 12.415  -4.399  1.00 24.26 ? 369 HOH A O   1 
HETATM 2077 O O   . HOH B 2 .   ? 24.045 -5.988  -23.394 1.00 37.50 ? 370 HOH A O   1 
HETATM 2078 O O   . HOH B 2 .   ? 8.142  17.983  -14.147 1.00 30.52 ? 371 HOH A O   1 
HETATM 2079 O O   . HOH B 2 .   ? 32.970 5.930   -7.218  1.00 25.61 ? 372 HOH A O   1 
HETATM 2080 O O   . HOH B 2 .   ? 15.306 -2.002  12.898  1.00 28.32 ? 373 HOH A O   1 
HETATM 2081 O O   . HOH B 2 .   ? -0.371 -1.744  -14.952 1.00 31.95 ? 374 HOH A O   1 
HETATM 2082 O O   . HOH B 2 .   ? 31.501 1.568   10.571  1.00 22.10 ? 375 HOH A O   1 
HETATM 2083 O O   . HOH B 2 .   ? 34.996 -13.495 1.823   1.00 40.67 ? 376 HOH A O   1 
HETATM 2084 O O   . HOH B 2 .   ? 30.878 6.639   11.899  1.00 34.73 ? 377 HOH A O   1 
HETATM 2085 O O   . HOH B 2 .   ? 18.617 8.851   -12.322 1.00 25.93 ? 378 HOH A O   1 
HETATM 2086 O O   . HOH B 2 .   ? 10.951 10.657  6.694   1.00 45.41 ? 379 HOH A O   1 
HETATM 2087 O O   . HOH B 2 .   ? 15.351 14.902  -6.270  1.00 23.70 ? 380 HOH A O   1 
HETATM 2088 O O   . HOH B 2 .   ? 11.005 -4.014  -28.031 1.00 41.21 ? 381 HOH A O   1 
HETATM 2089 O O   . HOH B 2 .   ? 17.476 -17.556 -12.527 1.00 23.77 ? 382 HOH A O   1 
HETATM 2090 O O   . HOH B 2 .   ? 16.456 -24.882 -4.610  1.00 34.02 ? 383 HOH A O   1 
HETATM 2091 O O   . HOH B 2 .   ? 40.112 -10.671 -7.020  1.00 28.89 ? 384 HOH A O   1 
HETATM 2092 O O   . HOH B 2 .   ? 27.191 -3.560  0.482   1.00 18.56 ? 385 HOH A O   1 
HETATM 2093 O O   . HOH B 2 .   ? 11.765 -20.936 -10.199 1.00 24.80 ? 386 HOH A O   1 
HETATM 2094 O O   . HOH B 2 .   ? 1.375  -0.344  -18.063 1.00 33.27 ? 387 HOH A O   1 
HETATM 2095 O O   . HOH B 2 .   ? 7.333  -9.531  -23.877 1.00 28.01 ? 388 HOH A O   1 
HETATM 2096 O O   . HOH B 2 .   ? 28.427 7.088   -11.200 1.00 30.42 ? 389 HOH A O   1 
HETATM 2097 O O   . HOH B 2 .   ? 7.675  6.699   3.652   1.00 34.48 ? 390 HOH A O   1 
HETATM 2098 O O   . HOH B 2 .   ? 28.479 -5.417  -20.702 1.00 37.30 ? 391 HOH A O   1 
HETATM 2099 O O   . HOH B 2 .   ? -0.892 9.878   -13.724 1.00 28.99 ? 392 HOH A O   1 
HETATM 2100 O O   . HOH B 2 .   ? 16.156 6.312   12.791  1.00 29.26 ? 393 HOH A O   1 
HETATM 2101 O O   . HOH B 2 .   ? 1.713  14.627  -16.417 1.00 34.53 ? 394 HOH A O   1 
HETATM 2102 O O   . HOH B 2 .   ? 21.338 -5.869  -24.033 1.00 39.01 ? 395 HOH A O   1 
HETATM 2103 O O   . HOH B 2 .   ? 14.803 5.337   -20.079 1.00 40.36 ? 396 HOH A O   1 
HETATM 2104 O O   . HOH B 2 .   ? 16.113 3.588   -20.245 1.00 33.16 ? 397 HOH A O   1 
HETATM 2105 O O   . HOH B 2 .   ? 15.366 -6.402  2.744   1.00 40.28 ? 398 HOH A O   1 
HETATM 2106 O O   . HOH B 2 .   ? 13.395 -23.966 -14.129 1.00 37.64 ? 399 HOH A O   1 
HETATM 2107 O O   . HOH B 2 .   ? 5.200  -10.893 -24.614 1.00 42.58 ? 400 HOH A O   1 
HETATM 2108 O O   . HOH B 2 .   ? 22.376 13.018  -7.597  1.00 46.16 ? 401 HOH A O   1 
HETATM 2109 O O   . HOH B 2 .   ? 31.649 10.903  -0.338  1.00 32.57 ? 402 HOH A O   1 
HETATM 2110 O O   . HOH B 2 .   ? 33.296 -13.318 -1.550  1.00 33.29 ? 403 HOH A O   1 
HETATM 2111 O O   . HOH B 2 .   ? 13.359 2.400   1.266   1.00 18.50 ? 404 HOH A O   1 
HETATM 2112 O O   . HOH B 2 .   ? 13.371 -4.210  -2.561  1.00 32.45 ? 405 HOH A O   1 
HETATM 2113 O O   . HOH B 2 .   ? 4.478  -3.943  -25.955 1.00 32.59 ? 406 HOH A O   1 
HETATM 2114 O O   . HOH B 2 .   ? 31.341 8.468   7.143   1.00 33.30 ? 407 HOH A O   1 
HETATM 2115 O O   . HOH B 2 .   ? 30.451 -15.011 1.159   1.00 46.32 ? 408 HOH A O   1 
HETATM 2116 O O   . HOH B 2 .   ? 27.546 -22.256 -9.845  1.00 33.82 ? 409 HOH A O   1 
HETATM 2117 O O   . HOH B 2 .   ? 34.290 5.497   5.451   1.00 27.21 ? 410 HOH A O   1 
HETATM 2118 O O   . HOH B 2 .   ? 39.515 3.428   -5.541  1.00 34.81 ? 411 HOH A O   1 
HETATM 2119 O O   . HOH B 2 .   ? 2.992  1.697   -18.952 1.00 26.32 ? 412 HOH A O   1 
HETATM 2120 O O   . HOH B 2 .   ? 33.556 9.788   -6.869  1.00 40.89 ? 413 HOH A O   1 
HETATM 2121 O O   . HOH B 2 .   ? 3.884  -9.984  -7.652  1.00 23.64 ? 414 HOH A O   1 
HETATM 2122 O O   . HOH B 2 .   ? 10.429 -10.452 -2.112  1.00 43.95 ? 415 HOH A O   1 
HETATM 2123 O O   . HOH B 2 .   ? 21.265 -17.995 -4.275  1.00 37.65 ? 416 HOH A O   1 
HETATM 2124 O O   . HOH B 2 .   ? 26.695 1.650   -11.746 1.00 31.18 ? 417 HOH A O   1 
HETATM 2125 O O   . HOH B 2 .   ? -1.103 1.565   -5.308  1.00 29.13 ? 418 HOH A O   1 
HETATM 2126 O O   . HOH B 2 .   ? 17.280 11.682  7.643   1.00 26.50 ? 419 HOH A O   1 
HETATM 2127 O O   . HOH B 2 .   ? 21.083 -1.111  -10.813 1.00 32.82 ? 420 HOH A O   1 
HETATM 2128 O O   . HOH B 2 .   ? 14.439 -8.738  -3.784  1.00 41.74 ? 421 HOH A O   1 
HETATM 2129 O O   . HOH B 2 .   ? 19.046 13.095  -6.374  1.00 28.32 ? 422 HOH A O   1 
HETATM 2130 O O   . HOH B 2 .   ? -0.742 4.743   -6.211  1.00 24.72 ? 423 HOH A O   1 
HETATM 2131 O O   . HOH B 2 .   ? 25.043 -20.926 -18.969 1.00 41.50 ? 424 HOH A O   1 
HETATM 2132 O O   . HOH B 2 .   ? 40.700 -0.598  -3.606  1.00 29.41 ? 425 HOH A O   1 
HETATM 2133 O O   . HOH B 2 .   ? 31.155 -14.678 -20.202 1.00 34.00 ? 426 HOH A O   1 
HETATM 2134 O O   . HOH B 2 .   ? 1.327  5.519   2.752   1.00 37.71 ? 427 HOH A O   1 
HETATM 2135 O O   . HOH B 2 .   ? 11.437 7.279   9.515   1.00 31.34 ? 428 HOH A O   1 
HETATM 2136 O O   . HOH B 2 .   ? 10.404 -0.967  -3.233  1.00 20.18 ? 429 HOH A O   1 
HETATM 2137 O O   . HOH B 2 .   ? 7.551  -18.618 -6.159  1.00 20.82 ? 430 HOH A O   1 
HETATM 2138 O O   . HOH B 2 .   ? 28.812 14.098  -0.932  1.00 29.82 ? 431 HOH A O   1 
HETATM 2139 O O   . HOH B 2 .   ? 29.899 -15.572 -13.923 1.00 31.91 ? 432 HOH A O   1 
HETATM 2140 O O   . HOH B 2 .   ? 23.900 -10.692 12.761  1.00 25.41 ? 433 HOH A O   1 
HETATM 2141 O O   . HOH B 2 .   ? 27.990 -16.913 -7.992  1.00 31.68 ? 434 HOH A O   1 
HETATM 2142 O O   . HOH B 2 .   ? 18.703 -19.093 -16.569 1.00 34.77 ? 435 HOH A O   1 
HETATM 2143 O O   . HOH B 2 .   ? 14.116 -17.180 -21.591 1.00 37.43 ? 436 HOH A O   1 
HETATM 2144 O O   . HOH B 2 .   ? 4.959  6.785   3.816   1.00 42.38 ? 437 HOH A O   1 
HETATM 2145 O O   . HOH B 2 .   ? 2.734  -0.706  -15.613 1.00 24.83 ? 438 HOH A O   1 
HETATM 2146 O O   . HOH B 2 .   ? 10.618 13.009  1.281   1.00 26.76 ? 439 HOH A O   1 
HETATM 2147 O O   . HOH B 2 .   ? 28.089 -9.997  -3.226  1.00 20.40 ? 440 HOH A O   1 
HETATM 2148 O O   . HOH B 2 .   ? 26.791 -23.404 -12.572 1.00 28.13 ? 441 HOH A O   1 
HETATM 2149 O O   . HOH B 2 .   ? -2.893 9.619   -11.826 1.00 38.37 ? 442 HOH A O   1 
HETATM 2150 O O   . HOH B 2 .   ? 11.633 6.942   6.744   1.00 21.99 ? 443 HOH A O   1 
HETATM 2151 O O   . HOH B 2 .   ? 13.564 15.823  -10.633 1.00 21.82 ? 444 HOH A O   1 
HETATM 2152 O O   . HOH B 2 .   ? 8.208  6.866   0.145   1.00 18.65 ? 445 HOH A O   1 
HETATM 2153 O O   . HOH B 2 .   ? 25.070 4.904   9.821   1.00 18.74 ? 446 HOH A O   1 
HETATM 2154 O O   . HOH B 2 .   ? 16.179 2.740   1.042   1.00 21.68 ? 447 HOH A O   1 
HETATM 2155 O O   . HOH B 2 .   ? 16.418 -14.563 -25.574 1.00 33.70 ? 448 HOH A O   1 
HETATM 2156 O O   . HOH B 2 .   ? 17.929 -1.946  17.751  1.00 32.16 ? 449 HOH A O   1 
HETATM 2157 O O   . HOH B 2 .   ? 27.443 -16.386 -13.196 1.00 28.27 ? 450 HOH A O   1 
HETATM 2158 O O   . HOH B 2 .   ? 16.946 16.858  -13.304 1.00 42.03 ? 451 HOH A O   1 
HETATM 2159 O O   . HOH B 2 .   ? 9.027  -3.478  -0.710  1.00 22.77 ? 452 HOH A O   1 
HETATM 2160 O O   . HOH B 2 .   ? 30.438 -16.053 -7.293  1.00 31.02 ? 453 HOH A O   1 
HETATM 2161 O O   . HOH B 2 .   ? 0.210  12.148  -21.856 1.00 48.48 ? 454 HOH A O   1 
HETATM 2162 O O   . HOH B 2 .   ? 37.711 -11.958 -6.436  1.00 30.65 ? 455 HOH A O   1 
HETATM 2163 O O   . HOH B 2 .   ? 3.407  -6.475  0.780   1.00 41.22 ? 456 HOH A O   1 
HETATM 2164 O O   . HOH B 2 .   ? 23.495 -3.282  22.471  1.00 36.40 ? 457 HOH A O   1 
HETATM 2165 O O   . HOH B 2 .   ? 24.548 -0.346  16.186  1.00 37.72 ? 458 HOH A O   1 
HETATM 2166 O O   . HOH B 2 .   ? 33.183 -5.511  11.235  1.00 34.71 ? 459 HOH A O   1 
HETATM 2167 O O   . HOH B 2 .   ? -1.220 -13.653 -10.627 1.00 41.32 ? 460 HOH A O   1 
HETATM 2168 O O   . HOH B 2 .   ? 32.922 -15.526 3.434   1.00 29.29 ? 461 HOH A O   1 
HETATM 2169 O O   . HOH B 2 .   ? 21.850 2.366   21.757  1.00 45.78 ? 462 HOH A O   1 
HETATM 2170 O O   . HOH B 2 .   ? 12.246 -23.686 -6.563  1.00 37.99 ? 463 HOH A O   1 
HETATM 2171 O O   . HOH B 2 .   ? 23.108 -23.403 -2.372  1.00 30.92 ? 464 HOH A O   1 
HETATM 2172 O O   . HOH B 2 .   ? 23.766 -25.449 -15.513 1.00 47.39 ? 465 HOH A O   1 
HETATM 2173 O O   . HOH B 2 .   ? -0.476 3.930   -10.944 1.00 20.39 ? 466 HOH A O   1 
HETATM 2174 O O   . HOH B 2 .   ? 21.739 -6.897  14.985  1.00 30.60 ? 467 HOH A O   1 
HETATM 2175 O O   . HOH B 2 .   ? 23.707 -7.910  -4.820  1.00 27.35 ? 468 HOH A O   1 
HETATM 2176 O O   . HOH B 2 .   ? 34.976 4.569   -14.670 1.00 34.82 ? 469 HOH A O   1 
HETATM 2177 O O   . HOH B 2 .   ? 29.755 -1.673  15.453  1.00 41.61 ? 470 HOH A O   1 
HETATM 2178 O O   . HOH B 2 .   ? 22.188 11.320  -10.665 1.00 36.77 ? 471 HOH A O   1 
HETATM 2179 O O   . HOH B 2 .   ? 21.065 16.330  1.622   1.00 29.88 ? 472 HOH A O   1 
HETATM 2180 O O   . HOH B 2 .   ? 34.734 -11.034 -1.240  1.00 31.12 ? 473 HOH A O   1 
HETATM 2181 O O   . HOH B 2 .   ? -3.361 -12.744 -13.030 1.00 41.68 ? 474 HOH A O   1 
HETATM 2182 O O   . HOH B 2 .   ? 1.417  -15.506 -17.987 1.00 44.04 ? 475 HOH A O   1 
HETATM 2183 O O   . HOH B 2 .   ? 21.383 -15.699 4.504   1.00 35.15 ? 476 HOH A O   1 
HETATM 2184 O O   . HOH B 2 .   ? 0.414  12.152  0.491   1.00 36.41 ? 477 HOH A O   1 
HETATM 2185 O O   . HOH B 2 .   ? 20.800 -13.741 -3.774  1.00 35.04 ? 478 HOH A O   1 
HETATM 2186 O O   . HOH B 2 .   ? 23.300 -9.900  0.539   1.00 28.46 ? 479 HOH A O   1 
HETATM 2187 O O   . HOH B 2 .   ? 31.498 -2.396  -19.343 1.00 40.34 ? 480 HOH A O   1 
HETATM 2188 O O   . HOH B 2 .   ? 35.510 3.017   5.669   1.00 37.76 ? 481 HOH A O   1 
HETATM 2189 O O   . HOH B 2 .   ? 34.475 -3.532  4.928   1.00 42.58 ? 482 HOH A O   1 
HETATM 2190 O O   . HOH B 2 .   ? 25.121 14.720  -2.630  1.00 35.05 ? 483 HOH A O   1 
HETATM 2191 O O   . HOH B 2 .   ? 37.969 3.171   -8.970  1.00 32.46 ? 484 HOH A O   1 
HETATM 2192 O O   . HOH B 2 .   ? 36.686 -11.292 -3.656  1.00 36.63 ? 485 HOH A O   1 
HETATM 2193 O O   . HOH B 2 .   ? 31.138 -13.404 0.169   1.00 44.17 ? 486 HOH A O   1 
HETATM 2194 O O   . HOH B 2 .   ? 9.396  15.930  1.257   1.00 33.43 ? 487 HOH A O   1 
HETATM 2195 O O   . HOH B 2 .   ? 9.160  -19.731 -10.495 1.00 27.10 ? 488 HOH A O   1 
HETATM 2196 O O   . HOH B 2 .   ? 33.412 9.168   -0.842  1.00 30.83 ? 489 HOH A O   1 
HETATM 2197 O O   . HOH B 2 .   ? 34.026 7.379   7.283   1.00 46.11 ? 490 HOH A O   1 
HETATM 2198 O O   . HOH B 2 .   ? 21.233 8.855   -11.778 1.00 25.81 ? 491 HOH A O   1 
HETATM 2199 O O   . HOH B 2 .   ? 7.125  -3.831  -4.793  1.00 15.09 ? 492 HOH A O   1 
HETATM 2200 O O   . HOH B 2 .   ? 41.277 -9.418  -4.090  1.00 30.04 ? 493 HOH A O   1 
HETATM 2201 O O   . HOH B 2 .   ? 25.552 9.779   15.903  1.00 39.94 ? 494 HOH A O   1 
HETATM 2202 O O   . HOH B 2 .   ? 8.089  -7.346  -4.279  1.00 33.89 ? 495 HOH A O   1 
HETATM 2203 O O   . HOH B 2 .   ? 25.222 -13.186 -0.219  1.00 38.65 ? 496 HOH A O   1 
HETATM 2204 O O   . HOH B 2 .   ? 37.553 -0.602  3.856   1.00 35.39 ? 497 HOH A O   1 
HETATM 2205 O O   . HOH B 2 .   ? 27.893 -6.856  14.563  1.00 37.88 ? 498 HOH A O   1 
HETATM 2206 O O   . HOH B 2 .   ? 19.359 -6.095  -27.960 1.00 42.93 ? 499 HOH A O   1 
HETATM 2207 O O   . HOH B 2 .   ? 10.010 15.259  -16.980 1.00 38.45 ? 500 HOH A O   1 
HETATM 2208 O O   . HOH B 2 .   ? 5.814  -7.896  -1.721  1.00 48.86 ? 501 HOH A O   1 
HETATM 2209 O O   . HOH B 2 .   ? 25.060 -3.046  16.046  1.00 33.84 ? 502 HOH A O   1 
HETATM 2210 O O   . HOH B 2 .   ? 1.385  -15.235 -12.327 1.00 33.21 ? 503 HOH A O   1 
HETATM 2211 O O   . HOH B 2 .   ? 18.398 -8.012  13.172  1.00 41.51 ? 504 HOH A O   1 
HETATM 2212 O O   . HOH B 2 .   ? 16.227 -8.964  4.080   1.00 43.39 ? 505 HOH A O   1 
HETATM 2213 O O   . HOH B 2 .   ? 1.885  -8.141  -2.448  1.00 42.82 ? 506 HOH A O   1 
HETATM 2214 O O   . HOH B 2 .   ? -2.795 -11.926 -24.417 1.00 37.53 ? 507 HOH A O   1 
HETATM 2215 O O   . HOH B 2 .   ? 8.086  0.033   -26.785 1.00 36.87 ? 508 HOH A O   1 
HETATM 2216 O O   . HOH B 2 .   ? 21.845 -7.515  -2.843  1.00 36.12 ? 509 HOH A O   1 
HETATM 2217 O O   . HOH B 2 .   ? 7.779  -23.800 -16.232 1.00 45.81 ? 510 HOH A O   1 
HETATM 2218 O O   . HOH B 2 .   ? 25.423 -10.676 -2.256  1.00 29.41 ? 511 HOH A O   1 
HETATM 2219 O O   . HOH B 2 .   ? 19.936 -17.177 -30.015 1.00 38.08 ? 512 HOH A O   1 
HETATM 2220 O O   . HOH B 2 .   ? 13.232 2.879   -23.517 1.00 43.65 ? 513 HOH A O   1 
HETATM 2221 O O   . HOH B 2 .   ? 35.803 10.422  4.601   1.00 38.41 ? 514 HOH A O   1 
HETATM 2222 O O   . HOH B 2 .   ? 15.960 -9.593  6.566   1.00 39.42 ? 515 HOH A O   1 
HETATM 2223 O O   . HOH B 2 .   ? 22.871 7.509   -13.340 1.00 34.12 ? 516 HOH A O   1 
HETATM 2224 O O   . HOH B 2 .   ? 11.111 4.165   10.416  1.00 40.25 ? 517 HOH A O   1 
HETATM 2225 O O   . HOH B 2 .   ? 23.019 14.260  -5.757  1.00 43.03 ? 518 HOH A O   1 
HETATM 2226 O O   . HOH B 2 .   ? 9.833  -24.116 -15.503 1.00 47.87 ? 519 HOH A O   1 
HETATM 2227 O O   . HOH B 2 .   ? 33.443 1.326   5.866   1.00 31.18 ? 520 HOH A O   1 
HETATM 2228 O O   . HOH B 2 .   ? 9.727  -3.653  -3.759  1.00 30.21 ? 521 HOH A O   1 
HETATM 2229 O O   . HOH B 2 .   ? -1.933 15.271  -10.310 1.00 45.78 ? 522 HOH A O   1 
HETATM 2230 O O   . HOH B 2 .   ? 12.954 19.143  2.858   1.00 36.61 ? 523 HOH A O   1 
HETATM 2231 O O   . HOH B 2 .   ? 11.815 2.119   11.728  1.00 42.11 ? 524 HOH A O   1 
HETATM 2232 O O   . HOH B 2 .   ? 18.768 5.586   12.943  1.00 37.74 ? 525 HOH A O   1 
HETATM 2233 O O   . HOH B 2 .   ? -1.128 -5.517  1.671   1.00 50.19 ? 526 HOH A O   1 
HETATM 2234 O O   . HOH B 2 .   ? 23.674 -22.549 -19.721 1.00 47.67 ? 527 HOH A O   1 
HETATM 2235 O O   . HOH B 2 .   ? 38.754 -11.253 0.960   1.00 49.06 ? 528 HOH A O   1 
HETATM 2236 O O   . HOH B 2 .   ? 26.378 -17.097 0.503   1.00 47.67 ? 529 HOH A O   1 
HETATM 2237 O O   . HOH B 2 .   ? 28.447 9.761   -10.110 1.00 44.82 ? 530 HOH A O   1 
HETATM 2238 O O   . HOH B 2 .   ? -1.092 12.823  -13.510 1.00 35.69 ? 531 HOH A O   1 
HETATM 2239 O O   . HOH B 2 .   ? 36.754 -11.871 0.458   1.00 35.07 ? 532 HOH A O   1 
HETATM 2240 O O   . HOH B 2 .   ? 15.774 -5.988  -3.267  1.00 45.64 ? 533 HOH A O   1 
HETATM 2241 O O   . HOH B 2 .   ? 27.712 -19.401 -7.057  1.00 38.57 ? 534 HOH A O   1 
HETATM 2242 O O   . HOH B 2 .   ? 3.177  6.257   -26.787 1.00 34.82 ? 535 HOH A O   1 
HETATM 2243 O O   . HOH B 2 .   ? 8.369  12.218  2.933   1.00 37.83 ? 536 HOH A O   1 
HETATM 2244 O O   . HOH B 2 .   ? 13.921 18.750  -11.445 1.00 43.17 ? 537 HOH A O   1 
HETATM 2245 O O   . HOH B 2 .   ? 18.937 13.829  7.352   1.00 30.30 ? 538 HOH A O   1 
HETATM 2246 O O   . HOH B 2 .   ? 40.045 -6.290  2.574   1.00 36.20 ? 539 HOH A O   1 
HETATM 2247 O O   . HOH B 2 .   ? -2.198 10.114  -5.565  1.00 41.11 ? 540 HOH A O   1 
HETATM 2248 O O   . HOH B 2 .   ? -1.105 13.566  -11.088 1.00 38.80 ? 541 HOH A O   1 
HETATM 2249 O O   . HOH B 2 .   ? 26.878 -16.170 -10.470 1.00 27.57 ? 542 HOH A O   1 
HETATM 2250 O O   . HOH B 2 .   ? 33.652 0.877   8.980   1.00 33.52 ? 543 HOH A O   1 
HETATM 2251 O O   . HOH B 2 .   ? 11.626 -5.295  -4.416  1.00 43.83 ? 544 HOH A O   1 
HETATM 2252 O O   . HOH B 2 .   ? 16.960 -11.870 -3.513  1.00 34.31 ? 545 HOH A O   1 
HETATM 2253 O O   . HOH B 2 .   ? 30.872 -8.531  7.784   1.00 25.77 ? 546 HOH A O   1 
HETATM 2254 O O   . HOH B 2 .   ? 19.694 -5.779  -3.490  1.00 31.68 ? 547 HOH A O   1 
HETATM 2255 O O   . HOH B 2 .   ? 2.269  13.656  -23.270 1.00 45.82 ? 548 HOH A O   1 
HETATM 2256 O O   . HOH B 2 .   ? 13.042 15.320  -8.037  1.00 26.27 ? 549 HOH A O   1 
HETATM 2257 O O   . HOH B 2 .   ? 4.459  -11.035 -5.096  1.00 32.36 ? 550 HOH A O   1 
HETATM 2258 O O   . HOH B 2 .   ? 21.356 -9.597  13.889  1.00 40.65 ? 551 HOH A O   1 
HETATM 2259 O O   . HOH B 2 .   ? 33.319 -7.653  7.451   1.00 33.40 ? 552 HOH A O   1 
HETATM 2260 O O   . HOH B 2 .   ? 19.353 15.584  -4.765  1.00 40.91 ? 553 HOH A O   1 
HETATM 2261 O O   . HOH B 2 .   ? 22.696 -16.806 2.957   1.00 37.53 ? 554 HOH A O   1 
HETATM 2262 O O   . HOH B 2 .   ? 14.752 12.881  7.540   1.00 33.44 ? 555 HOH A O   1 
HETATM 2263 O O   . HOH B 2 .   ? 27.732 -3.350  16.318  1.00 37.24 ? 556 HOH A O   1 
HETATM 2264 O O   . HOH B 2 .   ? 2.696  -10.747 -2.993  1.00 39.55 ? 557 HOH A O   1 
HETATM 2265 O O   . HOH B 2 .   ? 18.776 -20.133 -27.811 1.00 45.57 ? 558 HOH A O   1 
# 
