data_9H3H
# 
_entry.id   9H3H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9H3H         pdb_00009h3h 10.2210/pdb9h3h/pdb 
WWPDB D_1292142521 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        9H3H 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-16 
_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              c.sauter@ibmc-cnrs.unistra.fr 
_pdbx_contact_author.name_first         Claude 
_pdbx_contact_author.name_last          Sauter 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8766-287X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pachl, P.'      1 ? 
'Coudray, L.'    2 ? 
'Rezacova, P.'   3 ? 
'Fejfarova, A.'  4 ? 
'Vincent, R.'    5 ? 
'Engilberge, S.' 6 ? 
'Sauter, C.'     7 ? 
# 
_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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs Open Bio' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-5463 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Protein crystallization and structure determination at room temperature in the CrystalChip.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/2211-5463.13932 
_citation.pdbx_database_id_PubMed   39572886 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pachl, P.'        1  0000-0001-9215-9817 
primary 'Coudray, L.'      2  ?                   
primary 'Vincent, R.'      3  0009-0004-0542-3384 
primary 'Nilles, L.'       4  ?                   
primary 'Scheer, H.'       5  ?                   
primary 'Ritzenthaler, C.' 6  ?                   
primary 'Fejfarova, A.'    7  0009-0002-8953-4377 
primary 'Rezacova, P.'     8  ?                   
primary 'Engilberge, S.'   9  ?                   
primary 'Sauter, C.'       10 0000-0002-8766-287X 
# 
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 'Carbonic anhydrase 2' 28932.641 1   4.2.1.1 ? lyase ? 
2 non-polymer syn 'ZINC ION'             65.409    1   ?       ? ?     ? 
3 water       nat water                  18.015    204 ?       ? ?     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_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       
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   TRP n 
1 3   GLY n 
1 4   TYR n 
1 5   GLY n 
1 6   LYS n 
1 7   HIS n 
1 8   ASN n 
1 9   GLY n 
1 10  PRO n 
1 11  GLU n 
1 12  HIS n 
1 13  TRP n 
1 14  HIS n 
1 15  LYS n 
1 16  ASP n 
1 17  PHE n 
1 18  PRO n 
1 19  ILE n 
1 20  ALA n 
1 21  LYS n 
1 22  GLY n 
1 23  GLU n 
1 24  ARG n 
1 25  GLN n 
1 26  SER n 
1 27  PRO n 
1 28  VAL n 
1 29  ASP n 
1 30  ILE n 
1 31  ASP n 
1 32  THR n 
1 33  HIS n 
1 34  THR n 
1 35  ALA n 
1 36  LYS n 
1 37  TYR n 
1 38  ASP n 
1 39  PRO n 
1 40  SER n 
1 41  LEU n 
1 42  LYS n 
1 43  PRO n 
1 44  LEU n 
1 45  SER n 
1 46  VAL n 
1 47  SER n 
1 48  TYR n 
1 49  ASP n 
1 50  GLN n 
1 51  ALA n 
1 52  THR n 
1 53  SER n 
1 54  LEU n 
1 55  ARG n 
1 56  ILE n 
1 57  LEU n 
1 58  ASN n 
1 59  ASN n 
1 60  GLY n 
1 61  HIS n 
1 62  ALA n 
1 63  PHE n 
1 64  ASN n 
1 65  VAL n 
1 66  GLU n 
1 67  PHE n 
1 68  ASP n 
1 69  ASP n 
1 70  SER n 
1 71  GLN n 
1 72  ASP n 
1 73  LYS n 
1 74  ALA n 
1 75  VAL n 
1 76  LEU n 
1 77  LYS n 
1 78  GLY n 
1 79  GLY n 
1 80  PRO n 
1 81  LEU n 
1 82  ASP n 
1 83  GLY n 
1 84  THR n 
1 85  TYR n 
1 86  ARG n 
1 87  LEU n 
1 88  ILE n 
1 89  GLN n 
1 90  PHE n 
1 91  HIS n 
1 92  PHE n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  SER n 
1 97  LEU n 
1 98  ASP n 
1 99  GLY n 
1 100 GLN n 
1 101 GLY n 
1 102 SER n 
1 103 GLU n 
1 104 HIS n 
1 105 THR n 
1 106 VAL n 
1 107 ASP n 
1 108 LYS n 
1 109 LYS n 
1 110 LYS n 
1 111 TYR n 
1 112 ALA n 
1 113 ALA n 
1 114 GLU n 
1 115 LEU n 
1 116 HIS n 
1 117 LEU n 
1 118 VAL n 
1 119 HIS n 
1 120 TRP n 
1 121 ASN n 
1 122 THR n 
1 123 LYS n 
1 124 TYR n 
1 125 GLY n 
1 126 ASP n 
1 127 PHE n 
1 128 GLY n 
1 129 LYS n 
1 130 ALA n 
1 131 VAL n 
1 132 GLN n 
1 133 GLN n 
1 134 PRO n 
1 135 ASP n 
1 136 GLY n 
1 137 LEU n 
1 138 ALA n 
1 139 VAL n 
1 140 LEU n 
1 141 GLY n 
1 142 ILE n 
1 143 PHE n 
1 144 LEU n 
1 145 LYS n 
1 146 VAL n 
1 147 GLY n 
1 148 SER n 
1 149 ALA n 
1 150 LYS n 
1 151 PRO n 
1 152 GLY n 
1 153 LEU n 
1 154 GLN n 
1 155 LYS n 
1 156 VAL n 
1 157 VAL n 
1 158 ASP n 
1 159 VAL n 
1 160 LEU n 
1 161 ASP n 
1 162 SER n 
1 163 ILE n 
1 164 LYS n 
1 165 THR n 
1 166 LYS n 
1 167 GLY n 
1 168 LYS n 
1 169 SER n 
1 170 ALA n 
1 171 ASP n 
1 172 PHE n 
1 173 THR n 
1 174 ASN n 
1 175 PHE n 
1 176 ASP n 
1 177 PRO n 
1 178 ARG n 
1 179 GLY n 
1 180 LEU n 
1 181 LEU n 
1 182 PRO n 
1 183 GLU n 
1 184 SER n 
1 185 LEU n 
1 186 ASP n 
1 187 TYR n 
1 188 TRP n 
1 189 THR n 
1 190 TYR n 
1 191 PRO n 
1 192 GLY n 
1 193 SER n 
1 194 LEU n 
1 195 THR n 
1 196 THR n 
1 197 PRO n 
1 198 PRO n 
1 199 LEU n 
1 200 LEU n 
1 201 GLU n 
1 202 CYS n 
1 203 VAL n 
1 204 THR n 
1 205 TRP n 
1 206 ILE n 
1 207 VAL n 
1 208 LEU n 
1 209 LYS n 
1 210 GLU n 
1 211 PRO n 
1 212 ILE n 
1 213 SER n 
1 214 VAL n 
1 215 SER n 
1 216 SER n 
1 217 GLU n 
1 218 GLN n 
1 219 VAL n 
1 220 LEU n 
1 221 LYS n 
1 222 PHE n 
1 223 ARG n 
1 224 LYS n 
1 225 LEU n 
1 226 ASN n 
1 227 PHE n 
1 228 ASN n 
1 229 GLY n 
1 230 GLU n 
1 231 GLY n 
1 232 GLU n 
1 233 PRO n 
1 234 GLU n 
1 235 GLU n 
1 236 LEU n 
1 237 MET n 
1 238 VAL n 
1 239 ASP n 
1 240 ASN n 
1 241 TRP n 
1 242 ARG n 
1 243 PRO n 
1 244 ALA n 
1 245 GLN n 
1 246 PRO n 
1 247 LEU n 
1 248 LYS n 
1 249 ASN n 
1 250 ARG n 
1 251 GLN n 
1 252 ILE n 
1 253 LYS n 
1 254 ALA n 
1 255 SER n 
1 256 PHE n 
1 257 LYS 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                   257 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   HIS 1   4   4   HIS HIS A . n 
A 1 2   TRP 2   5   5   TRP TRP A . n 
A 1 3   GLY 3   6   6   GLY GLY A . n 
A 1 4   TYR 4   7   7   TYR TYR A . n 
A 1 5   GLY 5   8   8   GLY GLY A . n 
A 1 6   LYS 6   9   9   LYS LYS A . n 
A 1 7   HIS 7   10  10  HIS HIS A . n 
A 1 8   ASN 8   11  11  ASN ASN A . n 
A 1 9   GLY 9   12  12  GLY GLY A . n 
A 1 10  PRO 10  13  13  PRO PRO A . n 
A 1 11  GLU 11  14  14  GLU GLU A . n 
A 1 12  HIS 12  15  15  HIS HIS A . n 
A 1 13  TRP 13  16  16  TRP TRP A . n 
A 1 14  HIS 14  17  17  HIS HIS A . n 
A 1 15  LYS 15  18  18  LYS LYS A . n 
A 1 16  ASP 16  19  19  ASP ASP A . n 
A 1 17  PHE 17  20  20  PHE PHE A . n 
A 1 18  PRO 18  21  21  PRO PRO A . n 
A 1 19  ILE 19  22  22  ILE ILE A . n 
A 1 20  ALA 20  23  23  ALA ALA A . n 
A 1 21  LYS 21  24  24  LYS LYS A . n 
A 1 22  GLY 22  25  25  GLY GLY A . n 
A 1 23  GLU 23  26  26  GLU GLU A . n 
A 1 24  ARG 24  27  27  ARG ARG A . n 
A 1 25  GLN 25  28  28  GLN GLN A . n 
A 1 26  SER 26  29  29  SER SER A . n 
A 1 27  PRO 27  30  30  PRO PRO A . n 
A 1 28  VAL 28  31  31  VAL VAL A . n 
A 1 29  ASP 29  32  32  ASP ASP A . n 
A 1 30  ILE 30  33  33  ILE ILE A . n 
A 1 31  ASP 31  34  34  ASP ASP A . n 
A 1 32  THR 32  35  35  THR THR A . n 
A 1 33  HIS 33  36  36  HIS HIS A . n 
A 1 34  THR 34  37  37  THR THR A . n 
A 1 35  ALA 35  38  38  ALA ALA A . n 
A 1 36  LYS 36  39  39  LYS LYS A . n 
A 1 37  TYR 37  40  40  TYR TYR A . n 
A 1 38  ASP 38  41  41  ASP ASP A . n 
A 1 39  PRO 39  42  42  PRO PRO A . n 
A 1 40  SER 40  43  43  SER SER A . n 
A 1 41  LEU 41  44  44  LEU LEU A . n 
A 1 42  LYS 42  45  45  LYS LYS A . n 
A 1 43  PRO 43  46  46  PRO PRO A . n 
A 1 44  LEU 44  47  47  LEU LEU A . n 
A 1 45  SER 45  48  48  SER SER A . n 
A 1 46  VAL 46  49  49  VAL VAL A . n 
A 1 47  SER 47  50  50  SER SER A . n 
A 1 48  TYR 48  51  51  TYR TYR A . n 
A 1 49  ASP 49  52  52  ASP ASP A . n 
A 1 50  GLN 50  53  53  GLN GLN A . n 
A 1 51  ALA 51  54  54  ALA ALA A . n 
A 1 52  THR 52  55  55  THR THR A . n 
A 1 53  SER 53  56  56  SER SER A . n 
A 1 54  LEU 54  57  57  LEU LEU A . n 
A 1 55  ARG 55  58  58  ARG ARG A . n 
A 1 56  ILE 56  59  59  ILE ILE A . n 
A 1 57  LEU 57  60  60  LEU LEU A . n 
A 1 58  ASN 58  61  61  ASN ASN A . n 
A 1 59  ASN 59  62  62  ASN ASN A . n 
A 1 60  GLY 60  63  63  GLY GLY A . n 
A 1 61  HIS 61  64  64  HIS HIS A . n 
A 1 62  ALA 62  65  65  ALA ALA A . n 
A 1 63  PHE 63  66  66  PHE PHE A . n 
A 1 64  ASN 64  67  67  ASN ASN A . n 
A 1 65  VAL 65  68  68  VAL VAL A . n 
A 1 66  GLU 66  69  69  GLU GLU A . n 
A 1 67  PHE 67  70  70  PHE PHE A . n 
A 1 68  ASP 68  71  71  ASP ASP A . n 
A 1 69  ASP 69  72  72  ASP ASP A . n 
A 1 70  SER 70  73  73  SER SER A . n 
A 1 71  GLN 71  74  74  GLN GLN A . n 
A 1 72  ASP 72  75  75  ASP ASP A . n 
A 1 73  LYS 73  76  76  LYS LYS A . n 
A 1 74  ALA 74  77  77  ALA ALA A . n 
A 1 75  VAL 75  78  78  VAL VAL A . n 
A 1 76  LEU 76  79  79  LEU LEU A . n 
A 1 77  LYS 77  80  80  LYS LYS A . n 
A 1 78  GLY 78  81  81  GLY GLY A . n 
A 1 79  GLY 79  82  82  GLY GLY A . n 
A 1 80  PRO 80  83  83  PRO PRO A . n 
A 1 81  LEU 81  84  84  LEU LEU A . n 
A 1 82  ASP 82  85  85  ASP ASP A . n 
A 1 83  GLY 83  86  86  GLY GLY A . n 
A 1 84  THR 84  87  87  THR THR A . n 
A 1 85  TYR 85  88  88  TYR TYR A . n 
A 1 86  ARG 86  89  89  ARG ARG A . n 
A 1 87  LEU 87  90  90  LEU LEU A . n 
A 1 88  ILE 88  91  91  ILE ILE A . n 
A 1 89  GLN 89  92  92  GLN GLN A . n 
A 1 90  PHE 90  93  93  PHE PHE A . n 
A 1 91  HIS 91  94  94  HIS HIS A . n 
A 1 92  PHE 92  95  95  PHE PHE A . n 
A 1 93  HIS 93  96  96  HIS HIS A . n 
A 1 94  TRP 94  97  97  TRP TRP A . n 
A 1 95  GLY 95  98  98  GLY GLY A . n 
A 1 96  SER 96  99  99  SER SER A . n 
A 1 97  LEU 97  100 100 LEU LEU A . n 
A 1 98  ASP 98  101 101 ASP ASP A . n 
A 1 99  GLY 99  102 102 GLY GLY A . n 
A 1 100 GLN 100 103 103 GLN GLN A . n 
A 1 101 GLY 101 104 104 GLY GLY A . n 
A 1 102 SER 102 105 105 SER SER A . n 
A 1 103 GLU 103 106 106 GLU GLU A . n 
A 1 104 HIS 104 107 107 HIS HIS A . n 
A 1 105 THR 105 108 108 THR THR A . n 
A 1 106 VAL 106 109 109 VAL VAL A . n 
A 1 107 ASP 107 110 110 ASP ASP A . n 
A 1 108 LYS 108 111 111 LYS LYS A . n 
A 1 109 LYS 109 112 112 LYS LYS A . n 
A 1 110 LYS 110 113 113 LYS LYS A . n 
A 1 111 TYR 111 114 114 TYR TYR A . n 
A 1 112 ALA 112 115 115 ALA ALA A . n 
A 1 113 ALA 113 116 116 ALA ALA A . n 
A 1 114 GLU 114 117 117 GLU GLU A . n 
A 1 115 LEU 115 118 118 LEU LEU A . n 
A 1 116 HIS 116 119 119 HIS HIS A . n 
A 1 117 LEU 117 120 120 LEU LEU A . n 
A 1 118 VAL 118 121 121 VAL VAL A . n 
A 1 119 HIS 119 122 122 HIS HIS A . n 
A 1 120 TRP 120 123 123 TRP TRP A . n 
A 1 121 ASN 121 124 124 ASN ASN A . n 
A 1 122 THR 122 125 125 THR THR A . n 
A 1 123 LYS 123 126 126 LYS LYS A . n 
A 1 124 TYR 124 127 127 TYR TYR A . n 
A 1 125 GLY 125 128 128 GLY GLY A . n 
A 1 126 ASP 126 129 129 ASP ASP A . n 
A 1 127 PHE 127 130 130 PHE PHE A . n 
A 1 128 GLY 128 131 131 GLY GLY A . n 
A 1 129 LYS 129 132 132 LYS LYS A . n 
A 1 130 ALA 130 133 133 ALA ALA A . n 
A 1 131 VAL 131 134 134 VAL VAL A . n 
A 1 132 GLN 132 135 135 GLN GLN A . n 
A 1 133 GLN 133 136 136 GLN GLN A . n 
A 1 134 PRO 134 137 137 PRO PRO A . n 
A 1 135 ASP 135 138 138 ASP ASP A . n 
A 1 136 GLY 136 139 139 GLY GLY A . n 
A 1 137 LEU 137 140 140 LEU LEU A . n 
A 1 138 ALA 138 141 141 ALA ALA A . n 
A 1 139 VAL 139 142 142 VAL VAL A . n 
A 1 140 LEU 140 143 143 LEU LEU A . n 
A 1 141 GLY 141 144 144 GLY GLY A . n 
A 1 142 ILE 142 145 145 ILE ILE A . n 
A 1 143 PHE 143 146 146 PHE PHE A . n 
A 1 144 LEU 144 147 147 LEU LEU A . n 
A 1 145 LYS 145 148 148 LYS LYS A . n 
A 1 146 VAL 146 149 149 VAL VAL A . n 
A 1 147 GLY 147 150 150 GLY GLY A . n 
A 1 148 SER 148 151 151 SER SER A . n 
A 1 149 ALA 149 152 152 ALA ALA A . n 
A 1 150 LYS 150 153 153 LYS LYS A . n 
A 1 151 PRO 151 154 154 PRO PRO A . n 
A 1 152 GLY 152 155 155 GLY GLY A . n 
A 1 153 LEU 153 156 156 LEU LEU A . n 
A 1 154 GLN 154 157 157 GLN GLN A . n 
A 1 155 LYS 155 158 158 LYS LYS A . n 
A 1 156 VAL 156 159 159 VAL VAL A . n 
A 1 157 VAL 157 160 160 VAL VAL A . n 
A 1 158 ASP 158 161 161 ASP ASP A . n 
A 1 159 VAL 159 162 162 VAL VAL A . n 
A 1 160 LEU 160 163 163 LEU LEU A . n 
A 1 161 ASP 161 164 164 ASP ASP A . n 
A 1 162 SER 162 165 165 SER SER A . n 
A 1 163 ILE 163 166 166 ILE ILE A . n 
A 1 164 LYS 164 167 167 LYS LYS A . n 
A 1 165 THR 165 168 168 THR THR A . n 
A 1 166 LYS 166 169 169 LYS LYS A . n 
A 1 167 GLY 167 170 170 GLY GLY A . n 
A 1 168 LYS 168 171 171 LYS LYS A . n 
A 1 169 SER 169 172 172 SER SER A . n 
A 1 170 ALA 170 173 173 ALA ALA A . n 
A 1 171 ASP 171 174 174 ASP ASP A . n 
A 1 172 PHE 172 175 175 PHE PHE A . n 
A 1 173 THR 173 176 176 THR THR A . n 
A 1 174 ASN 174 177 177 ASN ASN A . n 
A 1 175 PHE 175 178 178 PHE PHE A . n 
A 1 176 ASP 176 179 179 ASP ASP A . n 
A 1 177 PRO 177 180 180 PRO PRO A . n 
A 1 178 ARG 178 181 181 ARG ARG A . n 
A 1 179 GLY 179 182 182 GLY GLY A . n 
A 1 180 LEU 180 183 183 LEU LEU A . n 
A 1 181 LEU 181 184 184 LEU LEU A . n 
A 1 182 PRO 182 185 185 PRO PRO A . n 
A 1 183 GLU 183 186 186 GLU GLU A . n 
A 1 184 SER 184 187 187 SER SER A . n 
A 1 185 LEU 185 188 188 LEU LEU A . n 
A 1 186 ASP 186 189 189 ASP ASP A . n 
A 1 187 TYR 187 190 190 TYR TYR A . n 
A 1 188 TRP 188 191 191 TRP TRP A . n 
A 1 189 THR 189 192 192 THR THR A . n 
A 1 190 TYR 190 193 193 TYR TYR A . n 
A 1 191 PRO 191 194 194 PRO PRO A . n 
A 1 192 GLY 192 195 195 GLY GLY A . n 
A 1 193 SER 193 196 196 SER SER A . n 
A 1 194 LEU 194 197 197 LEU LEU A . n 
A 1 195 THR 195 198 198 THR THR A . n 
A 1 196 THR 196 199 199 THR THR A . n 
A 1 197 PRO 197 200 200 PRO PRO A . n 
A 1 198 PRO 198 201 201 PRO PRO A . n 
A 1 199 LEU 199 202 202 LEU LEU A . n 
A 1 200 LEU 200 203 203 LEU LEU A . n 
A 1 201 GLU 201 204 204 GLU GLU A . n 
A 1 202 CYS 202 205 205 CYS CYS A . n 
A 1 203 VAL 203 206 206 VAL VAL A . n 
A 1 204 THR 204 207 207 THR THR A . n 
A 1 205 TRP 205 208 208 TRP TRP A . n 
A 1 206 ILE 206 209 209 ILE ILE A . n 
A 1 207 VAL 207 210 210 VAL VAL A . n 
A 1 208 LEU 208 211 211 LEU LEU A . n 
A 1 209 LYS 209 212 212 LYS LYS A . n 
A 1 210 GLU 210 213 213 GLU GLU A . n 
A 1 211 PRO 211 214 214 PRO PRO A . n 
A 1 212 ILE 212 215 215 ILE ILE A . n 
A 1 213 SER 213 216 216 SER SER A . n 
A 1 214 VAL 214 217 217 VAL VAL A . n 
A 1 215 SER 215 218 218 SER SER A . n 
A 1 216 SER 216 219 219 SER SER A . n 
A 1 217 GLU 217 220 220 GLU GLU A . n 
A 1 218 GLN 218 221 221 GLN GLN A . n 
A 1 219 VAL 219 222 222 VAL VAL A . n 
A 1 220 LEU 220 223 223 LEU LEU A . n 
A 1 221 LYS 221 224 224 LYS LYS A . n 
A 1 222 PHE 222 225 225 PHE PHE A . n 
A 1 223 ARG 223 226 226 ARG ARG A . n 
A 1 224 LYS 224 227 227 LYS LYS A . n 
A 1 225 LEU 225 228 228 LEU LEU A . n 
A 1 226 ASN 226 229 229 ASN ASN A . n 
A 1 227 PHE 227 230 230 PHE PHE A . n 
A 1 228 ASN 228 231 231 ASN ASN A . n 
A 1 229 GLY 229 232 232 GLY GLY A . n 
A 1 230 GLU 230 233 233 GLU GLU A . n 
A 1 231 GLY 231 234 234 GLY GLY A . n 
A 1 232 GLU 232 235 235 GLU GLU A . n 
A 1 233 PRO 233 236 236 PRO PRO A . n 
A 1 234 GLU 234 237 237 GLU GLU A . n 
A 1 235 GLU 235 238 238 GLU GLU A . n 
A 1 236 LEU 236 239 239 LEU LEU A . n 
A 1 237 MET 237 240 240 MET MET A . n 
A 1 238 VAL 238 241 241 VAL VAL A . n 
A 1 239 ASP 239 242 242 ASP ASP A . n 
A 1 240 ASN 240 243 243 ASN ASN A . n 
A 1 241 TRP 241 244 244 TRP TRP A . n 
A 1 242 ARG 242 245 245 ARG ARG A . n 
A 1 243 PRO 243 246 246 PRO PRO A . n 
A 1 244 ALA 244 247 247 ALA ALA A . n 
A 1 245 GLN 245 248 248 GLN GLN A . n 
A 1 246 PRO 246 249 249 PRO PRO A . n 
A 1 247 LEU 247 250 250 LEU LEU A . n 
A 1 248 LYS 248 251 251 LYS LYS A . n 
A 1 249 ASN 249 252 252 ASN ASN A . n 
A 1 250 ARG 250 253 253 ARG ARG A . n 
A 1 251 GLN 251 254 254 GLN GLN A . n 
A 1 252 ILE 252 255 255 ILE ILE A . n 
A 1 253 LYS 253 256 256 LYS LYS A . n 
A 1 254 ALA 254 257 257 ALA ALA A . n 
A 1 255 SER 255 258 258 SER SER A . n 
A 1 256 PHE 256 259 259 PHE PHE A . n 
A 1 257 LYS 257 260 260 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 301 ZN  ZN  A . 
C 3 HOH 1   401 166 HOH HOH A . 
C 3 HOH 2   402 60  HOH HOH A . 
C 3 HOH 3   403 114 HOH HOH A . 
C 3 HOH 4   404 202 HOH HOH A . 
C 3 HOH 5   405 150 HOH HOH A . 
C 3 HOH 6   406 116 HOH HOH A . 
C 3 HOH 7   407 140 HOH HOH A . 
C 3 HOH 8   408 184 HOH HOH A . 
C 3 HOH 9   409 62  HOH HOH A . 
C 3 HOH 10  410 200 HOH HOH A . 
C 3 HOH 11  411 55  HOH HOH A . 
C 3 HOH 12  412 80  HOH HOH A . 
C 3 HOH 13  413 18  HOH HOH A . 
C 3 HOH 14  414 217 HOH HOH A . 
C 3 HOH 15  415 165 HOH HOH A . 
C 3 HOH 16  416 213 HOH HOH A . 
C 3 HOH 17  417 141 HOH HOH A . 
C 3 HOH 18  418 136 HOH HOH A . 
C 3 HOH 19  419 2   HOH HOH A . 
C 3 HOH 20  420 112 HOH HOH A . 
C 3 HOH 21  421 170 HOH HOH A . 
C 3 HOH 22  422 67  HOH HOH A . 
C 3 HOH 23  423 43  HOH HOH A . 
C 3 HOH 24  424 152 HOH HOH A . 
C 3 HOH 25  425 144 HOH HOH A . 
C 3 HOH 26  426 24  HOH HOH A . 
C 3 HOH 27  427 181 HOH HOH A . 
C 3 HOH 28  428 57  HOH HOH A . 
C 3 HOH 29  429 49  HOH HOH A . 
C 3 HOH 30  430 131 HOH HOH A . 
C 3 HOH 31  431 218 HOH HOH A . 
C 3 HOH 32  432 117 HOH HOH A . 
C 3 HOH 33  433 22  HOH HOH A . 
C 3 HOH 34  434 10  HOH HOH A . 
C 3 HOH 35  435 58  HOH HOH A . 
C 3 HOH 36  436 126 HOH HOH A . 
C 3 HOH 37  437 88  HOH HOH A . 
C 3 HOH 38  438 107 HOH HOH A . 
C 3 HOH 39  439 191 HOH HOH A . 
C 3 HOH 40  440 102 HOH HOH A . 
C 3 HOH 41  441 50  HOH HOH A . 
C 3 HOH 42  442 69  HOH HOH A . 
C 3 HOH 43  443 180 HOH HOH A . 
C 3 HOH 44  444 79  HOH HOH A . 
C 3 HOH 45  445 109 HOH HOH A . 
C 3 HOH 46  446 72  HOH HOH A . 
C 3 HOH 47  447 17  HOH HOH A . 
C 3 HOH 48  448 28  HOH HOH A . 
C 3 HOH 49  449 70  HOH HOH A . 
C 3 HOH 50  450 122 HOH HOH A . 
C 3 HOH 51  451 23  HOH HOH A . 
C 3 HOH 52  452 14  HOH HOH A . 
C 3 HOH 53  453 64  HOH HOH A . 
C 3 HOH 54  454 9   HOH HOH A . 
C 3 HOH 55  455 153 HOH HOH A . 
C 3 HOH 56  456 68  HOH HOH A . 
C 3 HOH 57  457 190 HOH HOH A . 
C 3 HOH 58  458 3   HOH HOH A . 
C 3 HOH 59  459 98  HOH HOH A . 
C 3 HOH 60  460 139 HOH HOH A . 
C 3 HOH 61  461 19  HOH HOH A . 
C 3 HOH 62  462 25  HOH HOH A . 
C 3 HOH 63  463 65  HOH HOH A . 
C 3 HOH 64  464 204 HOH HOH A . 
C 3 HOH 65  465 148 HOH HOH A . 
C 3 HOH 66  466 74  HOH HOH A . 
C 3 HOH 67  467 47  HOH HOH A . 
C 3 HOH 68  468 1   HOH HOH A . 
C 3 HOH 69  469 138 HOH HOH A . 
C 3 HOH 70  470 89  HOH HOH A . 
C 3 HOH 71  471 176 HOH HOH A . 
C 3 HOH 72  472 83  HOH HOH A . 
C 3 HOH 73  473 59  HOH HOH A . 
C 3 HOH 74  474 48  HOH HOH A . 
C 3 HOH 75  475 37  HOH HOH A . 
C 3 HOH 76  476 6   HOH HOH A . 
C 3 HOH 77  477 26  HOH HOH A . 
C 3 HOH 78  478 63  HOH HOH A . 
C 3 HOH 79  479 54  HOH HOH A . 
C 3 HOH 80  480 115 HOH HOH A . 
C 3 HOH 81  481 52  HOH HOH A . 
C 3 HOH 82  482 45  HOH HOH A . 
C 3 HOH 83  483 4   HOH HOH A . 
C 3 HOH 84  484 33  HOH HOH A . 
C 3 HOH 85  485 95  HOH HOH A . 
C 3 HOH 86  486 29  HOH HOH A . 
C 3 HOH 87  487 36  HOH HOH A . 
C 3 HOH 88  488 216 HOH HOH A . 
C 3 HOH 89  489 73  HOH HOH A . 
C 3 HOH 90  490 75  HOH HOH A . 
C 3 HOH 91  491 32  HOH HOH A . 
C 3 HOH 92  492 53  HOH HOH A . 
C 3 HOH 93  493 100 HOH HOH A . 
C 3 HOH 94  494 156 HOH HOH A . 
C 3 HOH 95  495 164 HOH HOH A . 
C 3 HOH 96  496 12  HOH HOH A . 
C 3 HOH 97  497 123 HOH HOH A . 
C 3 HOH 98  498 46  HOH HOH A . 
C 3 HOH 99  499 8   HOH HOH A . 
C 3 HOH 100 500 16  HOH HOH A . 
C 3 HOH 101 501 121 HOH HOH A . 
C 3 HOH 102 502 78  HOH HOH A . 
C 3 HOH 103 503 119 HOH HOH A . 
C 3 HOH 104 504 169 HOH HOH A . 
C 3 HOH 105 505 203 HOH HOH A . 
C 3 HOH 106 506 160 HOH HOH A . 
C 3 HOH 107 507 15  HOH HOH A . 
C 3 HOH 108 508 161 HOH HOH A . 
C 3 HOH 109 509 113 HOH HOH A . 
C 3 HOH 110 510 13  HOH HOH A . 
C 3 HOH 111 511 94  HOH HOH A . 
C 3 HOH 112 512 81  HOH HOH A . 
C 3 HOH 113 513 163 HOH HOH A . 
C 3 HOH 114 514 39  HOH HOH A . 
C 3 HOH 115 515 97  HOH HOH A . 
C 3 HOH 116 516 41  HOH HOH A . 
C 3 HOH 117 517 96  HOH HOH A . 
C 3 HOH 118 518 21  HOH HOH A . 
C 3 HOH 119 519 137 HOH HOH A . 
C 3 HOH 120 520 66  HOH HOH A . 
C 3 HOH 121 521 106 HOH HOH A . 
C 3 HOH 122 522 189 HOH HOH A . 
C 3 HOH 123 523 177 HOH HOH A . 
C 3 HOH 124 524 34  HOH HOH A . 
C 3 HOH 125 525 186 HOH HOH A . 
C 3 HOH 126 526 51  HOH HOH A . 
C 3 HOH 127 527 5   HOH HOH A . 
C 3 HOH 128 528 120 HOH HOH A . 
C 3 HOH 129 529 77  HOH HOH A . 
C 3 HOH 130 530 44  HOH HOH A . 
C 3 HOH 131 531 31  HOH HOH A . 
C 3 HOH 132 532 42  HOH HOH A . 
C 3 HOH 133 533 110 HOH HOH A . 
C 3 HOH 134 534 71  HOH HOH A . 
C 3 HOH 135 535 129 HOH HOH A . 
C 3 HOH 136 536 154 HOH HOH A . 
C 3 HOH 137 537 168 HOH HOH A . 
C 3 HOH 138 538 135 HOH HOH A . 
C 3 HOH 139 539 198 HOH HOH A . 
C 3 HOH 140 540 105 HOH HOH A . 
C 3 HOH 141 541 145 HOH HOH A . 
C 3 HOH 142 542 127 HOH HOH A . 
C 3 HOH 143 543 193 HOH HOH A . 
C 3 HOH 144 544 132 HOH HOH A . 
C 3 HOH 145 545 27  HOH HOH A . 
C 3 HOH 146 546 159 HOH HOH A . 
C 3 HOH 147 547 101 HOH HOH A . 
C 3 HOH 148 548 108 HOH HOH A . 
C 3 HOH 149 549 92  HOH HOH A . 
C 3 HOH 150 550 61  HOH HOH A . 
C 3 HOH 151 551 167 HOH HOH A . 
C 3 HOH 152 552 104 HOH HOH A . 
C 3 HOH 153 553 130 HOH HOH A . 
C 3 HOH 154 554 7   HOH HOH A . 
C 3 HOH 155 555 187 HOH HOH A . 
C 3 HOH 156 556 151 HOH HOH A . 
C 3 HOH 157 557 171 HOH HOH A . 
C 3 HOH 158 558 11  HOH HOH A . 
C 3 HOH 159 559 196 HOH HOH A . 
C 3 HOH 160 560 85  HOH HOH A . 
C 3 HOH 161 561 214 HOH HOH A . 
C 3 HOH 162 562 35  HOH HOH A . 
C 3 HOH 163 563 194 HOH HOH A . 
C 3 HOH 164 564 192 HOH HOH A . 
C 3 HOH 165 565 134 HOH HOH A . 
C 3 HOH 166 566 182 HOH HOH A . 
C 3 HOH 167 567 82  HOH HOH A . 
C 3 HOH 168 568 38  HOH HOH A . 
C 3 HOH 169 569 157 HOH HOH A . 
C 3 HOH 170 570 30  HOH HOH A . 
C 3 HOH 171 571 90  HOH HOH A . 
C 3 HOH 172 572 173 HOH HOH A . 
C 3 HOH 173 573 20  HOH HOH A . 
C 3 HOH 174 574 143 HOH HOH A . 
C 3 HOH 175 575 178 HOH HOH A . 
C 3 HOH 176 576 86  HOH HOH A . 
C 3 HOH 177 577 215 HOH HOH A . 
C 3 HOH 178 578 158 HOH HOH A . 
C 3 HOH 179 579 174 HOH HOH A . 
C 3 HOH 180 580 155 HOH HOH A . 
C 3 HOH 181 581 76  HOH HOH A . 
C 3 HOH 182 582 125 HOH HOH A . 
C 3 HOH 183 583 188 HOH HOH A . 
C 3 HOH 184 584 133 HOH HOH A . 
C 3 HOH 185 585 146 HOH HOH A . 
C 3 HOH 186 586 40  HOH HOH A . 
C 3 HOH 187 587 93  HOH HOH A . 
C 3 HOH 188 588 185 HOH HOH A . 
C 3 HOH 189 589 179 HOH HOH A . 
C 3 HOH 190 590 149 HOH HOH A . 
C 3 HOH 191 591 199 HOH HOH A . 
C 3 HOH 192 592 118 HOH HOH A . 
C 3 HOH 193 593 84  HOH HOH A . 
C 3 HOH 194 594 147 HOH HOH A . 
C 3 HOH 195 595 162 HOH HOH A . 
C 3 HOH 196 596 87  HOH HOH A . 
C 3 HOH 197 597 111 HOH HOH A . 
C 3 HOH 198 598 91  HOH HOH A . 
C 3 HOH 199 599 175 HOH HOH A . 
C 3 HOH 200 600 142 HOH HOH A . 
C 3 HOH 201 601 172 HOH HOH A . 
C 3 HOH 202 602 195 HOH HOH A . 
C 3 HOH 203 603 183 HOH HOH A . 
C 3 HOH 204 604 219 HOH HOH A . 
# 
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 ? ? ? 1.18.2_3874 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.600 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H3H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.750 
_cell.length_a_esd                 ? 
_cell.length_b                     41.650 
_cell.length_b_esd                 ? 
_cell.length_c                     72.850 
_cell.length_c_esd                 ? 
_cell.volume                       125523.644 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9H3H 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H3H 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.30 
_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          COUNTER-DIFFUSION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.8 
_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    
;Protein crystallized by counter-diffusion in the CrystalChip, stock solution 35 mg/mL, in a reservoir containing 50 mM Tris, 1.6 M sodium citrate, at pH 7.8
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_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                        'ESRF BEAMLINE BM07' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BM07 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          16.74 
_reflns.entry_id                                       9H3H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               50 
_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                                     160567 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.64 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.04 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.322 
_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                                   0.958 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.277 
_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                                    1.8 
_reflns_shell.d_res_low                                     1.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.18 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11315 
_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                               3.55 
_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                                  0.308 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.7 
_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                               20.35 
_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                                 9H3H 
_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                            1.80 
_refine.ls_d_res_low                             41.37 
_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                     23244 
_refine.ls_number_reflns_R_free                  1163 
_refine.ls_number_reflns_R_work                  22081 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.83 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1703 
_refine.ls_R_factor_R_free                       0.2147 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1680 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 20.7595 
_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                            0.2232 
_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.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        41.37 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               2253 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2048 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0075  ? 2121 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0922  ? 2883 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0613  ? 302  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0066  ? 374  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.5486 ? 781  ? f_dihedral_angle_d ? ? 
# 
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' 1.80 1.88  . . 142 2697 99.51  . . . . 0.2587 . . . . . . . . . . . 0.3045 
'X-RAY DIFFRACTION' 1.88 1.98  . . 145 2771 99.93  . . . . 0.2267 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 1.98 2.10  . . 144 2721 99.93  . . . . 0.2002 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 2.10 2.27  . . 144 2750 99.97  . . . . 0.1792 . . . . . . . . . . . 0.2086 
'X-RAY DIFFRACTION' 2.27 2.50  . . 146 2773 99.97  . . . . 0.1705 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 2.50 2.86  . . 146 2756 99.93  . . . . 0.1707 . . . . . . . . . . . 0.2207 
'X-RAY DIFFRACTION' 2.86 3.60  . . 146 2778 100.00 . . . . 0.1503 . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 3.60 41.37 . . 150 2835 99.47  . . . . 0.1329 . . . . . . . . . . . 0.1721 
# 
_struct.entry_id                     9H3H 
_struct.title                        
'Human Carbonic anhydrase II crystallization and structure determination at room temperature in the CrystalChip' 
_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        9H3H 
_struct_keywords.text            'Human Carbonic anhydrase II, microfluidics, room temperature, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           4 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9H3H 
_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                 257 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  4 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       4 
_struct_ref_seq.pdbx_auth_seq_align_end       260 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLY A 9   ? ASP A 16  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 17  ? GLY A 22  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 123 ? GLY A 125 ? LYS A 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 126 ? VAL A 131 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 150 ? GLY A 152 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 153 ? LEU A 160 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 161 ? LYS A 164 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 176 ? LEU A 181 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 215 ? ARG A 223 ? SER A 218 ARG A 226 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 91  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
metalc2 metalc ? ? A HIS 93  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc3 metalc ? ? A HIS 116 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C HOH . O  ? ? A ZN  301 A HOH 432 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 111.6 ? 
2 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 116.2 ? 
3 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 104.8 ? 
4 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? C HOH .   ? A HOH 432 ? 1_555 103.7 ? 
5 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? C HOH .   ? A HOH 432 ? 1_555 113.1 ? 
6 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? C HOH .   ? A HOH 432 ? 1_555 107.6 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 26  A . ? SER 29  A PRO 27  A ? PRO 30  A 1 -0.85 
2 PRO 197 A . ? PRO 200 A PRO 198 A ? PRO 201 A 1 15.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
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  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? 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  ASP A 29  ? ILE A 30  ? ASP A 32  ILE A 33  
AA1 2  THR A 105 ? VAL A 106 ? THR A 108 VAL A 109 
AA2 1  LYS A 36  ? TYR A 37  ? LYS A 39  TYR A 40  
AA2 2  LYS A 253 ? ALA A 254 ? LYS A 256 ALA A 257 
AA2 3  TYR A 187 ? GLY A 192 ? TYR A 190 GLY A 195 
AA2 4  VAL A 203 ? LEU A 208 ? VAL A 206 LEU A 211 
AA2 5  LEU A 137 ? VAL A 146 ? LEU A 140 VAL A 149 
AA2 6  ALA A 113 ? ASN A 121 ? ALA A 116 ASN A 124 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 88  TRP A 97  
AA2 8  PHE A 63  ? PHE A 67  ? PHE A 66  PHE A 70  
AA2 9  SER A 53  ? ASN A 58  ? SER A 56  ASN A 61  
AA2 10 SER A 169 ? ASP A 171 ? SER A 172 ASP A 174 
AA3 1  LEU A 44  ? SER A 47  ? LEU A 47  SER A 50  
AA3 2  VAL A 75  ? GLY A 78  ? VAL A 78  GLY A 81  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 88  TRP A 97  
AA3 4  ALA A 113 ? ASN A 121 ? ALA A 116 ASN A 124 
AA3 5  LEU A 137 ? VAL A 146 ? LEU A 140 VAL A 149 
AA3 6  ILE A 212 ? VAL A 214 ? ILE A 215 VAL A 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 30  ? N ILE A 33  O THR A 105 ? O THR A 108 
AA2 1 2  N LYS A 36  ? N LYS A 39  O ALA A 254 ? O ALA A 257 
AA2 2 3  O LYS A 253 ? O LYS A 256 N THR A 189 ? N THR A 192 
AA2 3 4  N GLY A 192 ? N GLY A 195 O VAL A 203 ? O VAL A 206 
AA2 4 5  O ILE A 206 ? O ILE A 209 N GLY A 141 ? N GLY A 144 
AA2 5 6  O ILE A 142 ? O ILE A 145 N LEU A 115 ? N LEU A 118 
AA2 6 7  O HIS A 116 ? O HIS A 119 N HIS A 91  ? N HIS A 94  
AA2 7 8  O PHE A 90  ? O PHE A 93  N VAL A 65  ? N VAL A 68  
AA2 8 9  O ASN A 64  ? O ASN A 67  N LEU A 57  ? N LEU A 60  
AA2 9 10 N ILE A 56  ? N ILE A 59  O ALA A 170 ? O ALA A 173 
AA3 1 2  N SER A 47  ? N SER A 50  O VAL A 75  ? O VAL A 78  
AA3 2 3  N LEU A 76  ? N LEU A 79  O TYR A 85  ? O TYR A 88  
AA3 3 4  N HIS A 91  ? N HIS A 94  O HIS A 116 ? O HIS A 119 
AA3 4 5  N LEU A 115 ? N LEU A 118 O ILE A 142 ? O ILE A 145 
AA3 5 6  N PHE A 143 ? N PHE A 146 O ILE A 212 ? O ILE A 215 
# 
_pdbx_entry_details.entry_id                   9H3H 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 243 ? ? -92.10 50.38   
2 1 LYS A 251 ? ? 56.72  -134.70 
3 1 ASN A 252 ? ? -87.54 47.51   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 
ZN  ZN   ZN N N 391 
# 
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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Centre National de la Recherche Scientifique (CNRS)' France ?                       1 
'Agence Nationale de la Recherche (ANR)'              France ANR-10-LABX-0036_NETRNA 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6gxb 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_related_exp_data_set.ordinal              1 
_pdbx_related_exp_data_set.data_reference       10.15151/ESRF-ES-1752158517 
_pdbx_related_exp_data_set.metadata_reference   ? 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   CrystalChip 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9H3H 
_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]   0.023392 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006093 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024010 
_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]   0.014185 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . HIS A 1 1   ? -8.09800  22.20400 62.35400 1.000 25.47083  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 1   ? -6.98200  22.81600 61.63700 1.000 30.44337  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 1   ? -6.22200  21.74400 60.86500 1.000 27.41192  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 1   ? -6.41800  20.55200 61.09800 1.000 25.22631  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 1   ? -6.04900  23.55500 62.60000 1.000 28.25355  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 1   ? -5.42500  24.78400 62.01000 1.000 61.33671  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 1   ? -6.14100  25.70200 61.27000 1.000 74.34368  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 1   ? -4.15200  25.24300 62.05000 1.000 58.49887  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 1   ? -5.33600  26.67500 60.88200 1.000 72.12646  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 1   ? -4.12200  26.42100 61.34100 1.000 74.83275  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 2   ? -5.36300  22.15600 59.93900 1.000 24.51461  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 2   ? -4.69100  21.18000 59.09400 1.000 19.03427  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 2   ? -3.67200  20.38700 59.90200 1.000 19.22746  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 2   ? -3.15600  20.84900 60.92600 1.000 19.30021  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 2   ? -4.00700  21.86200 57.90900 1.000 14.90025  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 2   ? -2.87600  22.75900 58.28900 1.000 20.20222  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 2   ? -2.94700  24.08500 58.58900 1.000 21.50379  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 2   ? -1.49300  22.39700 58.39100 1.000 18.08926  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 2   ? -1.69900  24.57200 58.89300 1.000 19.53201  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 2   ? -0.78600  23.55600 58.77500 1.000 24.09281  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 2   ? -0.78600  21.20700 58.19300 1.000 24.91145  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 2   ? 0.59500   23.56000 58.96800 1.000 17.85007  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 2   ? 0.58500   21.21200 58.38800 1.000 22.68093  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 2   ? 1.26200   22.38600 58.77200 1.000 19.32693  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 3   ? -3.39800  19.17600 59.43200 1.000 15.76287  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 3   ? -2.35500  18.35300 60.00500 1.000 13.59414  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 3   ? -2.04300  17.17600 59.10600 1.000 19.29891  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 3   ? -2.08200  17.31000 57.87800 1.000 15.19647  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 4   ? -1.76400  16.01000 59.69800 1.000 12.22004  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 4   ? -1.39300  14.82700 58.92900 1.000 15.38949  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 4   ? -2.21100  13.59200 59.29800 1.000 19.44446  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 4   ? -1.81800  12.47500 58.93800 1.000 23.05466  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 4   ? 0.10500   14.52900 59.09300 1.000 17.00809  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 4   ? 1.00700   15.61900 58.54500 1.000 14.91250  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 4   ? 1.38400   15.62600 57.20900 1.000 12.91489  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 4   ? 1.50000   16.62100 59.37400 1.000 15.69232  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 4   ? 2.21400   16.63200 56.70500 1.000 10.31043  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 4   ? 2.33800   17.62200 58.88300 1.000 17.63070  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 4   ? 2.68600   17.62200 57.54900 1.000 16.66903  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 4   ? 3.51400   18.62000 57.06400 1.000 14.27079  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 5   ? -3.34300  13.76000 59.97700 1.000 22.50976  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 5   ? -4.21500  12.65000 60.30700 1.000 23.65074  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 5   ? -5.21900  12.34600 59.20700 1.000 24.13894  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 5   ? -5.22500  12.94300 58.13000 1.000 25.66924  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 6   ? -6.10600  11.39300 59.51000 1.000 32.41345  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 6   ? -7.06600  10.92500 58.51000 1.000 26.52987  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 6   ? -8.07200  12.00300 58.13900 1.000 25.60657  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 6   ? -8.53700  12.05500 56.99200 1.000 25.02594  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 6   ? -7.80600  9.68200  59.02000 1.000 33.65865  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 6   ? -6.98100  8.76300  59.91800 1.000 50.01601  ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 6   ? -7.54500  7.33800  59.99100 1.000 71.66932  ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 6   ? -6.63400  6.40200  60.77900 1.000 70.04534  ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 6   ? -7.09200  4.97700  60.72000 1.000 68.92337  ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 7   ? -8.41700  12.87400 59.08100 1.000 17.23079  ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 7   ? -9.49200  13.82800 58.86600 1.000 22.00476  ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 7   ? -9.00000  15.22700 58.52600 1.000 20.12211  ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 7   ? -9.81100  16.06200 58.12300 1.000 22.14368  ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 7   ? -10.39600 13.87400 60.10800 1.000 21.86288  ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 7   ? -10.98900 12.54300 60.45800 1.000 30.88412  ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 7   ? -12.08900 12.02200 59.80600 1.000 32.23701  ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 7   ? -10.62200 11.61700 61.37700 1.000 33.30394  ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 7   ? -12.37500 10.83400 60.31100 1.000 49.00077  ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 7   ? -11.50100 10.56600 61.26900 1.000 30.93596  ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 8   ? -7.69600  15.50200 58.67400 1.000 20.11004  ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 8   ? -7.16200  16.82100 58.35200 1.000 19.38645  ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 8   ? -5.86600  16.75400 57.54100 1.000 17.70326  ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 8   ? -5.14600  17.76100 57.45800 1.000 17.13587  ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 8   ? -6.92000  17.62800 59.62800 1.000 18.79247  ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 8   ? -5.90800  16.96800 60.55400 1.000 18.83080  ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 8   ? -5.37300  15.89000 60.26000 1.000 19.25079  ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 8   ? -5.63000  17.62100 61.67700 1.000 22.86916  ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 9   ? -5.57300  15.61000 56.92200 1.000 17.66528  ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 9   ? -4.30000  15.38900 56.27000 1.000 16.96887  ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 9   ? -4.21300  16.04000 54.90000 1.000 16.01424  ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 9   ? -5.11200  16.75300 54.45200 1.000 16.05555  ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 10  ? -3.09300  15.77800 54.20800 1.000 12.62143  ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 10  ? -2.80900  16.49100 52.94500 1.000 18.77937  ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 10  ? -3.91800  16.44200 51.91200 1.000 16.62762  ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 10  ? -4.08700  17.41400 51.16100 1.000 16.77201  ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 10  ? -1.54800  15.78400 52.43500 1.000 16.20894  ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 10  ? -0.84100  15.36700 53.68300 1.000 16.59735  ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 10  ? -1.92900  15.00400 54.67300 1.000 16.81041  ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 11  ? -4.70700  15.37300 51.87100 1.000 14.55921  ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 11  ? -5.78700  15.24900 50.85300 1.000 18.40891  ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 11  ? -6.91000  16.26000 51.14700 1.000 16.76938  ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 11  ? -7.75900  16.46700 50.27000 1.000 18.23097  ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 11  ? -6.35400  13.83300 50.86600 1.000 25.20787  ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 11  ? -6.81900  13.38000 52.24600 1.000 36.76489  ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 11  ? -5.85000  12.52900 53.04900 1.000 56.10208  ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 11  ? -4.72200  12.98300 53.32400 1.000 29.84924  ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 11  ? -6.23700  11.39800 53.41100 1.000 65.14317  ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 12  ? -6.92700  16.81800 52.35300 1.000 13.72896  ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 12  ? -7.93700  17.78800 52.75400 1.000 14.36358  ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 12  ? -7.48900  19.23300 52.57700 1.000 19.22870  ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 12  ? -8.33600  20.13500 52.63100 1.000 14.35901  ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 12  ? -8.32000  17.58000 54.23100 1.000 13.02858  ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 12  ? -9.05600  16.30200 54.50100 1.000 21.33177  ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 12  ? -10.43200 16.20600 54.45300 1.000 19.56320  ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 12  ? -8.60500  15.07100 54.84600 1.000 15.57041  ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 12  ? -10.79400 14.96300 54.73100 1.000 21.41502  ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 12  ? -9.70500  14.25600 54.97400 1.000 21.42050  ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 13  ? -6.18700  19.48400 52.38100 1.000 12.88324  ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 13  ? -5.67600  20.84600 52.54700 1.000 14.43620  ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 13  ? -6.28000  21.81900 51.54300 1.000 14.77521  ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 13  ? -6.38900  23.02100 51.83100 1.000 16.68750  ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 13  ? -4.14800  20.85900 52.42900 1.000 14.06813  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 13  ? -3.43700  20.17900 53.56000 1.000 13.44508  ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 13  ? -3.99300  19.68100 54.70800 1.000 13.66052  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 13  ? -2.02800  19.90300 53.64100 1.000 11.85246  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 13  ? -3.01000  19.12200 55.50600 1.000 12.69868  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 13  ? -1.79800  19.25200 54.87500 1.000 14.57280  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 13  ? -0.94300  20.15700 52.79500 1.000 12.60618  ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 13  ? -0.52500  18.83800 55.28100 1.000 18.07243  ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 13  ? 0.32600   19.76100 53.20000 1.000 9.76893   ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 13  ? 0.52500   19.11100 54.44100 1.000 16.95863  ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 14  ? -6.67700  21.32600 50.36700 1.000 13.32091  ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 14  ? -7.17300  22.20400 49.31100 1.000 16.84635  ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 14  ? -8.44100  22.94800 49.71500 1.000 15.58657  ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 14  ? -8.72800  23.99100 49.13400 1.000 14.55250  ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 14  ? -7.43200  21.40800 48.03000 1.000 21.41356  ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 14  ? -8.64600  20.53500 48.10400 1.000 20.34396  ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 14  ? -8.64400  19.30400 48.72500 1.000 20.68235  ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 14  ? -9.90600  20.72300 47.64700 1.000 16.52982  ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 14  ? -9.85000  18.77000 48.64300 1.000 19.02839  ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 14  ? -10.63500 19.61200 47.99700 1.000 20.36261  ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 15  ? -9.20400  22.44300 50.69400 1.000 18.14217  ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 15  ? -10.43000 23.14000 51.09100 1.000 22.51301  ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 15  ? -10.13700 24.46300 51.79000 1.000 22.11701  ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 15  ? -10.89000 25.42800 51.62400 1.000 21.31509  ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 15  ? -11.28700 22.24100 51.98900 1.000 15.59116  ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 15  ? -11.89400 21.03200 51.26700 1.000 18.06187  ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 15  ? -12.56900 20.08200 52.25900 1.000 15.10594  ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 15  ? -11.57600 19.07800 52.83000 1.000 18.12907  ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 15  ? -12.21900 18.22600 53.86700 1.000 18.97763  ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 16  ? -9.05700  24.53800 52.56700 1.000 15.74306  ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 16  ? -8.64000  25.79100 53.18400 1.000 15.17846  ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 16  ? -7.59400  26.54100 52.37200 1.000 23.05685  ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 16  ? -7.48900  27.76300 52.50600 1.000 18.59616  ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 16  ? -8.07800  25.53900 54.58800 1.000 22.04255  ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 16  ? -9.14300  25.12700 55.57300 1.000 29.30140  ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 16  ? -10.06500 25.93000 55.81300 1.000 25.43280  ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 16  ? -9.07600  23.98800 56.07500 1.000 28.36861  ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 17  ? -6.80600  25.83500 51.55800 1.000 12.91308  ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 17  ? -5.69900  26.42100 50.79900 1.000 16.11761  ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 17  ? -5.81800  25.91500 49.37300 1.000 15.97245  ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 17  ? -5.19700  24.91200 49.00000 1.000 17.55497  ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 17  ? -4.34400  26.06000 51.41300 1.000 15.05860  ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 17  ? -4.26000  26.37100 52.87800 1.000 16.13670  ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 17  ? -3.92700  27.64800 53.31300 1.000 17.75951  ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 17  ? -4.54100  25.39300 53.82100 1.000 14.52230  ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 17  ? -3.87600  27.93700 54.67800 1.000 19.91597  ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 17  ? -4.49100  25.67100 55.18400 1.000 16.65346  ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 17  ? -4.15300  26.94300 55.60900 1.000 18.62549  ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 18  ? -6.62200  26.58200 48.54300 1.000 15.24422  ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 18  ? -6.86300  26.05800 47.19500 1.000 15.33536  ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 18  ? -5.62200  26.03300 46.30900 1.000 17.79520  ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 18  ? -5.60800  25.27500 45.33500 1.000 14.98860  ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 18  ? -7.95000  26.99600 46.64100 1.000 24.76717  ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 18  ? -7.93500  28.18500 47.53300 1.000 20.80104  ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 18  ? -7.53400  27.68400 48.87900 1.000 21.84748  ? 21  PRO A CD  1 
ATOM   161  N  N   . ILE A 1 19  ? -4.56200  26.78600 46.62800 1.000 14.06784  ? 22  ILE A N   1 
ATOM   162  C  CA  . ILE A 1 19  ? -3.31700  26.65200 45.87600 1.000 11.66324  ? 22  ILE A CA  1 
ATOM   163  C  C   . ILE A 1 19  ? -2.70000  25.26000 46.02000 1.000 14.66218  ? 22  ILE A C   1 
ATOM   164  O  O   . ILE A 1 19  ? -1.74400  24.93800 45.30600 1.000 15.64851  ? 22  ILE A O   1 
ATOM   165  C  CB  . ILE A 1 19  ? -2.30800  27.74000 46.30200 1.000 12.50390  ? 22  ILE A CB  1 
ATOM   166  C  CG1 . ILE A 1 19  ? -1.26400  27.96000 45.20700 1.000 18.64968  ? 22  ILE A CG1 1 
ATOM   167  C  CG2 . ILE A 1 19  ? -1.65300  27.36900 47.61100 1.000 14.96038  ? 22  ILE A CG2 1 
ATOM   168  C  CD1 . ILE A 1 19  ? -0.38700  29.14100 45.46400 1.000 22.19129  ? 22  ILE A CD1 1 
ATOM   169  N  N   . ALA A 1 20  ? -3.24300  24.42300 46.91300 1.000 14.48535  ? 23  ALA A N   1 
ATOM   170  C  CA  . ALA A 1 20  ? -2.82200  23.02500 47.01100 1.000 16.78097  ? 23  ALA A CA  1 
ATOM   171  C  C   . ALA A 1 20  ? -2.94400  22.29100 45.68700 1.000 17.53136  ? 23  ALA A C   1 
ATOM   172  O  O   . ALA A 1 20  ? -2.25800  21.28700 45.46800 1.000 15.36327  ? 23  ALA A O   1 
ATOM   173  C  CB  . ALA A 1 20  ? -3.64900  22.29200 48.07200 1.000 14.41726  ? 23  ALA A CB  1 
ATOM   174  N  N   . LYS A 1 21  ? -3.84900  22.73600 44.81300 1.000 17.55573  ? 24  LYS A N   1 
ATOM   175  C  CA  . LYS A 1 21  ? -4.00700  22.14200 43.49700 1.000 17.60625  ? 24  LYS A CA  1 
ATOM   176  C  C   . LYS A 1 21  ? -3.35200  22.99000 42.41000 1.000 18.34185  ? 24  LYS A C   1 
ATOM   177  O  O   . LYS A 1 21  ? -3.72100  22.87600 41.23700 1.000 23.07001  ? 24  LYS A O   1 
ATOM   178  C  CB  . LYS A 1 21  ? -5.49100  21.93300 43.18300 1.000 15.47409  ? 24  LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 21  ? -6.25800  21.03000 44.15900 1.000 23.52739  ? 24  LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 21  ? -7.55400  20.52700 43.49700 1.000 34.61919  ? 24  LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 21  ? -8.48400  19.82500 44.47900 1.000 38.15387  ? 24  LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 21  ? -8.07000  18.42400 44.77000 1.000 39.11138  ? 24  LYS A NZ  1 
ATOM   183  N  N   . GLY A 1 22  ? -2.39800  23.84500 42.78100 1.000 18.32973  ? 25  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 22  ? -1.80400  24.79500 41.86300 1.000 16.28462  ? 25  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 22  ? -0.82000  24.16000 40.89600 1.000 20.55020  ? 25  GLY A C   1 
ATOM   186  O  O   . GLY A 1 22  ? -0.64100  22.94300 40.84700 1.000 20.54361  ? 25  GLY A O   1 
ATOM   187  N  N   . GLU A 1 23  ? -0.15400  25.02100 40.12300 1.000 16.66853  ? 26  GLU A N   1 
ATOM   188  C  CA  . GLU A 1 23  ? 0.69800   24.57200 39.02300 1.000 17.84614  ? 26  GLU A CA  1 
ATOM   189  C  C   . GLU A 1 23  ? 2.15600   24.32000 39.41500 1.000 17.36438  ? 26  GLU A C   1 
ATOM   190  O  O   . GLU A 1 23  ? 2.89700   23.72000 38.62400 1.000 18.89437  ? 26  GLU A O   1 
ATOM   191  C  CB  . GLU A 1 23  ? 0.66400   25.59200 37.87900 1.000 24.55340  ? 26  GLU A CB  1 
ATOM   192  C  CG  . GLU A 1 23  ? -0.68700  25.68000 37.16000 1.000 33.90524  ? 26  GLU A CG  1 
ATOM   193  C  CD  . GLU A 1 23  ? -0.92700  24.51400 36.20800 1.000 35.54864  ? 26  GLU A CD  1 
ATOM   194  O  OE1 . GLU A 1 23  ? -0.17300  24.38000 35.21700 1.000 54.70822  ? 26  GLU A OE1 1 
ATOM   195  O  OE2 . GLU A 1 23  ? -1.86300  23.72200 36.45600 1.000 49.09248  ? 26  GLU A OE2 1 
ATOM   196  N  N   . ARG A 1 24  ? 2.61200   24.75600 40.58500 1.000 13.91053  ? 27  ARG A N   1 
ATOM   197  C  CA  . ARG A 1 24  ? 4.00500   24.48200 40.95000 1.000 14.76528  ? 27  ARG A CA  1 
ATOM   198  C  C   . ARG A 1 24  ? 4.09700   24.04500 42.41700 1.000 11.94116  ? 27  ARG A C   1 
ATOM   199  O  O   . ARG A 1 24  ? 4.84300   24.58400 43.22900 1.000 10.21598  ? 27  ARG A O   1 
ATOM   200  C  CB  . ARG A 1 24  ? 4.91600   25.66700 40.61600 1.000 16.79325  ? 27  ARG A CB  1 
ATOM   201  C  CG  . ARG A 1 24  ? 4.66300   26.93500 41.36100 1.000 26.94023  ? 27  ARG A CG  1 
ATOM   202  C  CD  . ARG A 1 24  ? 5.68900   28.02900 41.02700 1.000 30.49457  ? 27  ARG A CD  1 
ATOM   203  N  NE  . ARG A 1 24  ? 6.86300   28.04600 41.89700 1.000 19.15307  ? 27  ARG A NE  1 
ATOM   204  C  CZ  . ARG A 1 24  ? 7.76000   29.02500 41.91100 1.000 19.63515  ? 27  ARG A CZ  1 
ATOM   205  N  NH1 . ARG A 1 24  ? 7.64700   30.07700 41.11600 1.000 16.53176  ? 27  ARG A NH1 1 
ATOM   206  N  NH2 . ARG A 1 24  ? 8.79700   28.95000 42.74300 1.000 15.60784  ? 27  ARG A NH2 1 
ATOM   207  N  N   . GLN A 1 25  ? 3.37300   22.97900 42.74300 1.000 15.78779  ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 25  ? 3.35800   22.43100 44.09100 1.000 10.45805  ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 25  ? 4.49200   21.43800 44.31600 1.000 10.95420  ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 25  ? 4.95800   20.75500 43.39000 1.000 13.73861  ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 25  ? 2.01600   21.75300 44.37300 1.000 14.20406  ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 25  ? 0.87100   22.73400 44.54600 1.000 12.05487  ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 25  ? 1.03400   23.58200 45.78900 1.000 13.31677  ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 25  ? 0.85700   23.09600 46.90700 1.000 16.75450  ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 25  ? 1.38900   24.85900 45.60200 1.000 10.63864  ? 28  GLN A NE2 1 
ATOM   216  N  N   . SER A 1 26  ? 4.91000   21.34100 45.57700 1.000 9.77035   ? 29  SER A N   1 
ATOM   217  C  CA  . SER A 1 26  ? 5.94800   20.43300 46.04000 1.000 10.53568  ? 29  SER A CA  1 
ATOM   218  C  C   . SER A 1 26  ? 5.41200   19.53400 47.14800 1.000 10.33837  ? 29  SER A C   1 
ATOM   219  O  O   . SER A 1 26  ? 4.43800   19.88500 47.82100 1.000 11.20882  ? 29  SER A O   1 
ATOM   220  C  CB  . SER A 1 26  ? 7.15800   21.22000 46.56300 1.000 9.65274   ? 29  SER A CB  1 
ATOM   221  O  OG  . SER A 1 26  ? 7.70700   21.99000 45.51100 1.000 13.22843  ? 29  SER A OG  1 
ATOM   222  N  N   . PRO A 1 27  ? 6.04600   18.36900 47.39100 1.000 9.55514   ? 30  PRO A N   1 
ATOM   223  C  CA  . PRO A 1 27  ? 7.21500   17.79500 46.71600 1.000 8.80089   ? 30  PRO A CA  1 
ATOM   224  C  C   . PRO A 1 27  ? 6.83400   17.13100 45.40700 1.000 8.67118   ? 30  PRO A C   1 
ATOM   225  O  O   . PRO A 1 27  ? 5.64900   17.08200 45.05800 1.000 12.50569  ? 30  PRO A O   1 
ATOM   226  C  CB  . PRO A 1 27  ? 7.71900   16.75900 47.73400 1.000 9.32867   ? 30  PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 27  ? 6.41900   16.23400 48.31600 1.000 8.33434   ? 30  PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 27  ? 5.53900   17.46400 48.43900 1.000 7.00992   ? 30  PRO A CD  1 
ATOM   229  N  N   . VAL A 1 28  ? 7.83400   16.61900 44.67800 1.000 11.69408  ? 31  VAL A N   1 
ATOM   230  C  CA  . VAL A 1 28  ? 7.63600   15.86500 43.44200 1.000 10.57380  ? 31  VAL A CA  1 
ATOM   231  C  C   . VAL A 1 28  ? 8.54500   14.64400 43.45600 1.000 13.76771  ? 31  VAL A C   1 
ATOM   232  O  O   . VAL A 1 28  ? 9.52500   14.57100 44.20400 1.000 12.24278  ? 31  VAL A O   1 
ATOM   233  C  CB  . VAL A 1 28  ? 7.93400   16.69700 42.17200 1.000 10.94972  ? 31  VAL A CB  1 
ATOM   234  C  CG1 . VAL A 1 28  ? 7.00900   17.88700 42.07100 1.000 13.91806  ? 31  VAL A CG1 1 
ATOM   235  C  CG2 . VAL A 1 28  ? 9.39100   17.14900 42.15800 1.000 10.95048  ? 31  VAL A CG2 1 
ATOM   236  N  N   . ASP A 1 29  ? 8.21000   13.67600 42.60500 1.000 11.24099  ? 32  ASP A N   1 
ATOM   237  C  CA  . ASP A 1 29  ? 9.11700   12.57400 42.32100 1.000 12.61044  ? 32  ASP A CA  1 
ATOM   238  C  C   . ASP A 1 29  ? 10.17500  13.04100 41.32900 1.000 9.27838   ? 32  ASP A C   1 
ATOM   239  O  O   . ASP A 1 29  ? 9.85200   13.62100 40.29200 1.000 17.24169  ? 32  ASP A O   1 
ATOM   240  C  CB  . ASP A 1 29  ? 8.35600   11.37000 41.76100 1.000 16.35509  ? 32  ASP A CB  1 
ATOM   241  C  CG  . ASP A 1 29  ? 9.27600   10.19700 41.41100 1.000 24.78582  ? 32  ASP A CG  1 
ATOM   242  O  OD1 . ASP A 1 29  ? 10.00300  9.71300  42.31000 1.000 14.62997  ? 32  ASP A OD1 1 
ATOM   243  O  OD2 . ASP A 1 29  ? 9.26000   9.75200  40.23200 1.000 20.11470  ? 32  ASP A OD2 1 
ATOM   244  N  N   . ILE A 1 30  ? 11.43900  12.79200 41.65200 1.000 15.14495  ? 33  ILE A N   1 
ATOM   245  C  CA  . ILE A 1 30  ? 12.54800  13.12200 40.76200 1.000 15.15676  ? 33  ILE A CA  1 
ATOM   246  C  C   . ILE A 1 30  ? 12.84400  11.88300 39.92000 1.000 14.47387  ? 33  ILE A C   1 
ATOM   247  O  O   . ILE A 1 30  ? 13.45400  10.92300 40.39100 1.000 16.32598  ? 33  ILE A O   1 
ATOM   248  C  CB  . ILE A 1 30  ? 13.77800  13.58400 41.54200 1.000 13.39732  ? 33  ILE A CB  1 
ATOM   249  C  CG1 . ILE A 1 30  ? 13.46600  14.86700 42.32600 1.000 14.94416  ? 33  ILE A CG1 1 
ATOM   250  C  CG2 . ILE A 1 30  ? 14.95700  13.80000 40.59900 1.000 12.98137  ? 33  ILE A CG2 1 
ATOM   251  C  CD1 . ILE A 1 30  ? 14.55900  15.23400 43.31100 1.000 18.17209  ? 33  ILE A CD1 1 
ATOM   252  N  N   . ASP A 1 31  ? 12.39900  11.91000 38.66500 1.000 13.94919  ? 34  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 31  ? 12.74300  10.88600 37.67800 1.000 16.00813  ? 34  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 31  ? 14.15300  11.18100 37.17200 1.000 14.56253  ? 34  ASP A C   1 
ATOM   255  O  O   . ASP A 1 31  ? 14.35100  12.12800 36.40400 1.000 20.40973  ? 34  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 31  ? 11.71100  10.91300 36.55000 1.000 19.14659  ? 34  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 31  ? 11.96200  9.86000  35.46600 1.000 25.36173  ? 34  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 31  ? 13.07200  9.30400  35.37000 1.000 25.24266  ? 34  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 31  ? 11.02600  9.60100  34.69300 1.000 37.47691  ? 34  ASP A OD2 1 
ATOM   260  N  N   . THR A 1 32  ? 15.13800  10.37800 37.59800 1.000 15.65559  ? 35  THR A N   1 
ATOM   261  C  CA  . THR A 1 32  ? 16.53200  10.67000 37.26900 1.000 16.35900  ? 35  THR A CA  1 
ATOM   262  C  C   . THR A 1 32  ? 16.83400  10.52600 35.78700 1.000 22.41545  ? 35  THR A C   1 
ATOM   263  O  O   . THR A 1 32  ? 17.87400  11.01100 35.33500 1.000 18.97725  ? 35  THR A O   1 
ATOM   264  C  CB  . THR A 1 32  ? 17.49000  9.75500  38.02800 1.000 17.66198  ? 35  THR A CB  1 
ATOM   265  O  OG1 . THR A 1 32  ? 17.22900  8.38300  37.68200 1.000 18.89088  ? 35  THR A OG1 1 
ATOM   266  C  CG2 . THR A 1 32  ? 17.33900  9.95100  39.52800 1.000 20.48016  ? 35  THR A CG2 1 
ATOM   267  N  N   . HIS A 1 33  ? 15.97300  9.85100  35.03100 1.000 21.73958  ? 36  HIS A N   1 
ATOM   268  C  CA  . HIS A 1 33  ? 16.24100  9.64100  33.61700 1.000 26.66124  ? 36  HIS A CA  1 
ATOM   269  C  C   . HIS A 1 33  ? 15.61700  10.70500 32.72800 1.000 26.18774  ? 36  HIS A C   1 
ATOM   270  O  O   . HIS A 1 33  ? 15.97500  10.79100 31.55000 1.000 29.10319  ? 36  HIS A O   1 
ATOM   271  C  CB  . HIS A 1 33  ? 15.76200  8.25000  33.20000 1.000 24.76331  ? 36  HIS A CB  1 
ATOM   272  C  CG  . HIS A 1 33  ? 16.58200  7.14500  33.78400 1.000 22.75556  ? 36  HIS A CG  1 
ATOM   273  N  ND1 . HIS A 1 33  ? 16.08200  6.24900  34.70500 1.000 25.59212  ? 36  HIS A ND1 1 
ATOM   274  C  CD2 . HIS A 1 33  ? 17.88200  6.81000  33.59800 1.000 32.88485  ? 36  HIS A CD2 1 
ATOM   275  C  CE1 . HIS A 1 33  ? 17.03400  5.40100  35.04900 1.000 25.73591  ? 36  HIS A CE1 1 
ATOM   276  N  NE2 . HIS A 1 33  ? 18.13400  5.71700  34.39000 1.000 33.93152  ? 36  HIS A NE2 1 
ATOM   277  N  N   . THR A 1 34  ? 14.71900  11.53300 33.26000 1.000 23.26573  ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 34  ? 14.18900  12.65700 32.50400 1.000 24.98640  ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 34  ? 14.68000  14.00800 33.01400 1.000 21.97691  ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 34  ? 14.38200  15.03400 32.39400 1.000 21.99872  ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 34  ? 12.65300  12.62100 32.50900 1.000 29.57537  ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 34  ? 12.16800  12.79100 33.84400 1.000 34.65843  ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 34  ? 12.16700  11.29000 31.98400 1.000 37.86498  ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 35  ? 15.43000  14.03900 34.10800 1.000 19.01177  ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 35  ? 16.02400  15.28900 34.56200 1.000 18.18387  ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 35  ? 17.12000  15.72200 33.59400 1.000 23.54521  ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 35  ? 17.93500  14.91200 33.15300 1.000 27.60631  ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 35  ? 16.59600  15.13300 35.96600 1.000 18.53903  ? 38  ALA A CB  1 
ATOM   289  N  N   . LYS A 1 36  ? 17.13900  17.01200 33.27000 1.000 20.13411  ? 39  LYS A N   1 
ATOM   290  C  CA  . LYS A 1 36  ? 18.04800  17.55000 32.26700 1.000 18.15399  ? 39  LYS A CA  1 
ATOM   291  C  C   . LYS A 1 36  ? 19.33800  18.03100 32.92300 1.000 23.35266  ? 39  LYS A C   1 
ATOM   292  O  O   . LYS A 1 36  ? 19.32000  18.94300 33.75900 1.000 15.28632  ? 39  LYS A O   1 
ATOM   293  C  CB  . LYS A 1 36  ? 17.37900  18.69700 31.51500 1.000 23.20993  ? 39  LYS A CB  1 
ATOM   294  C  CG  . LYS A 1 36  ? 18.20600  19.27700 30.38900 1.000 34.82154  ? 39  LYS A CG  1 
ATOM   295  C  CD  . LYS A 1 36  ? 17.89000  18.58000 29.08000 1.000 42.31802  ? 39  LYS A CD  1 
ATOM   296  C  CE  . LYS A 1 36  ? 19.03500  18.70900 28.08000 1.000 43.35480  ? 39  LYS A CE  1 
ATOM   297  N  NZ  . LYS A 1 36  ? 18.85300  19.86100 27.15600 1.000 46.15609  ? 39  LYS A NZ  1 
ATOM   298  N  N   . TYR A 1 37  ? 20.46200  17.43500 32.53800 1.000 24.45253  ? 40  TYR A N   1 
ATOM   299  C  CA  . TYR A 1 37  ? 21.73600  18.02700 32.91200 1.000 20.68621  ? 40  TYR A CA  1 
ATOM   300  C  C   . TYR A 1 37  ? 21.86800  19.39700 32.25700 1.000 23.40406  ? 40  TYR A C   1 
ATOM   301  O  O   . TYR A 1 37  ? 21.69900  19.53900 31.04100 1.000 26.96253  ? 40  TYR A O   1 
ATOM   302  C  CB  . TYR A 1 37  ? 22.90000  17.12000 32.50500 1.000 23.62756  ? 40  TYR A CB  1 
ATOM   303  C  CG  . TYR A 1 37  ? 24.24200  17.79300 32.65600 1.000 33.78703  ? 40  TYR A CG  1 
ATOM   304  C  CD1 . TYR A 1 37  ? 24.73300  18.13000 33.90900 1.000 31.57605  ? 40  TYR A CD1 1 
ATOM   305  C  CD2 . TYR A 1 37  ? 25.00700  18.11300 31.54500 1.000 40.88786  ? 40  TYR A CD2 1 
ATOM   306  C  CE1 . TYR A 1 37  ? 25.95900  18.75300 34.05100 1.000 31.01851  ? 40  TYR A CE1 1 
ATOM   307  C  CE2 . TYR A 1 37  ? 26.23400  18.74100 31.67600 1.000 36.58977  ? 40  TYR A CE2 1 
ATOM   308  C  CZ  . TYR A 1 37  ? 26.70400  19.05700 32.93100 1.000 40.38068  ? 40  TYR A CZ  1 
ATOM   309  O  OH  . TYR A 1 37  ? 27.92400  19.68400 33.06100 1.000 40.46705  ? 40  TYR A OH  1 
ATOM   310  N  N   . ASP A 1 38  ? 22.14000  20.41200 33.06900 1.000 20.19562  ? 41  ASP A N   1 
ATOM   311  C  CA  . ASP A 1 38  ? 22.27700  21.78900 32.59300 1.000 20.18319  ? 41  ASP A CA  1 
ATOM   312  C  C   . ASP A 1 38  ? 23.67700  22.27600 32.94100 1.000 34.91685  ? 41  ASP A C   1 
ATOM   313  O  O   . ASP A 1 38  ? 23.93800  22.65500 34.09700 1.000 24.39740  ? 41  ASP A O   1 
ATOM   314  C  CB  . ASP A 1 38  ? 21.20600  22.69000 33.21400 1.000 25.46638  ? 41  ASP A CB  1 
ATOM   315  C  CG  . ASP A 1 38  ? 21.26400  24.13200 32.70500 1.000 34.42020  ? 41  ASP A CG  1 
ATOM   316  O  OD1 . ASP A 1 38  ? 22.32300  24.56600 32.21400 1.000 34.91900  ? 41  ASP A OD1 1 
ATOM   317  O  OD2 . ASP A 1 38  ? 20.24200  24.84100 32.80800 1.000 43.61781  ? 41  ASP A OD2 1 
ATOM   318  N  N   . PRO A 1 39  ? 24.61100  22.30100 31.98300 1.000 41.57380  ? 42  PRO A N   1 
ATOM   319  C  CA  . PRO A 1 39  ? 25.98400  22.73100 32.30300 1.000 43.72242  ? 42  PRO A CA  1 
ATOM   320  C  C   . PRO A 1 39  ? 26.10600  24.21600 32.60800 1.000 33.27193  ? 42  PRO A C   1 
ATOM   321  O  O   . PRO A 1 39  ? 27.20100  24.66500 32.96800 1.000 40.16969  ? 42  PRO A O   1 
ATOM   322  C  CB  . PRO A 1 39  ? 26.77100  22.35800 31.04000 1.000 37.44620  ? 42  PRO A CB  1 
ATOM   323  C  CG  . PRO A 1 39  ? 25.75300  22.43000 29.94300 1.000 41.26197  ? 42  PRO A CG  1 
ATOM   324  C  CD  . PRO A 1 39  ? 24.44200  21.98700 30.55200 1.000 34.97776  ? 42  PRO A CD  1 
ATOM   325  N  N   . SER A 1 40  ? 25.03500  24.99200 32.47300 1.000 32.95881  ? 43  SER A N   1 
ATOM   326  C  CA  . SER A 1 40  ? 25.07700  26.39400 32.86600 1.000 42.66078  ? 43  SER A CA  1 
ATOM   327  C  C   . SER A 1 40  ? 24.83100  26.59600 34.35800 1.000 36.27256  ? 43  SER A C   1 
ATOM   328  O  O   . SER A 1 40  ? 25.00400  27.71800 34.84800 1.000 30.54537  ? 43  SER A O   1 
ATOM   329  C  CB  . SER A 1 40  ? 24.05300  27.20200 32.06400 1.000 36.88032  ? 43  SER A CB  1 
ATOM   330  O  OG  . SER A 1 40  ? 22.77800  27.16100 32.67700 1.000 38.08828  ? 43  SER A OG  1 
ATOM   331  N  N   . LEU A 1 41  ? 24.42700  25.55300 35.08300 1.000 24.38306  ? 44  LEU A N   1 
ATOM   332  C  CA  . LEU A 1 41  ? 24.26200  25.65800 36.52500 1.000 33.08844  ? 44  LEU A CA  1 
ATOM   333  C  C   . LEU A 1 41  ? 25.62200  25.76100 37.20500 1.000 27.21165  ? 44  LEU A C   1 
ATOM   334  O  O   . LEU A 1 41  ? 26.56400  25.04500 36.86100 1.000 28.78536  ? 44  LEU A O   1 
ATOM   335  C  CB  . LEU A 1 41  ? 23.50000  24.44800 37.07200 1.000 25.76866  ? 44  LEU A CB  1 
ATOM   336  C  CG  . LEU A 1 41  ? 22.00100  24.34600 36.78400 1.000 24.83916  ? 44  LEU A CG  1 
ATOM   337  C  CD1 . LEU A 1 41  ? 21.45100  23.02800 37.34500 1.000 20.12768  ? 44  LEU A CD1 1 
ATOM   338  C  CD2 . LEU A 1 41  ? 21.25400  25.53400 37.37700 1.000 21.44181  ? 44  LEU A CD2 1 
ATOM   339  N  N   . LYS A 1 42  ? 25.70800  26.64200 38.18500 1.000 30.18916  ? 45  LYS A N   1 
ATOM   340  C  CA  . LYS A 1 42  ? 26.91300  26.89600 38.95900 1.000 30.07405  ? 45  LYS A CA  1 
ATOM   341  C  C   . LYS A 1 42  ? 26.96200  26.01300 40.19900 1.000 24.17972  ? 45  LYS A C   1 
ATOM   342  O  O   . LYS A 1 42  ? 25.93400  25.51000 40.66600 1.000 25.10900  ? 45  LYS A O   1 
ATOM   343  C  CB  . LYS A 1 42  ? 26.96400  28.36600 39.36900 1.000 29.00321  ? 45  LYS A CB  1 
ATOM   344  C  CG  . LYS A 1 42  ? 27.01200  29.32900 38.19600 1.000 36.66150  ? 45  LYS A CG  1 
ATOM   345  C  CD  . LYS A 1 42  ? 26.76900  30.75800 38.65600 1.000 42.86755  ? 45  LYS A CD  1 
ATOM   346  C  CE  . LYS A 1 42  ? 26.46600  31.67900 37.47700 1.000 56.69362  ? 45  LYS A CE  1 
ATOM   347  N  NZ  . LYS A 1 42  ? 25.01100  31.70600 37.12500 1.000 55.13210  ? 45  LYS A NZ  1 
ATOM   348  N  N   . PRO A 1 43  ? 28.15200  25.79200 40.75700 1.000 23.97369  ? 46  PRO A N   1 
ATOM   349  C  CA  . PRO A 1 43  ? 28.22900  25.10900 42.05200 1.000 24.95562  ? 46  PRO A CA  1 
ATOM   350  C  C   . PRO A 1 43  ? 27.48500  25.89800 43.11800 1.000 16.45214  ? 46  PRO A C   1 
ATOM   351  O  O   . PRO A 1 43  ? 27.43500  27.13000 43.09100 1.000 16.85438  ? 46  PRO A O   1 
ATOM   352  C  CB  . PRO A 1 43  ? 29.73600  25.06500 42.34700 1.000 26.90969  ? 46  PRO A CB  1 
ATOM   353  C  CG  . PRO A 1 43  ? 30.39700  25.25800 41.03100 1.000 28.33747  ? 46  PRO A CG  1 
ATOM   354  C  CD  . PRO A 1 43  ? 29.48700  26.14300 40.23800 1.000 28.79083  ? 46  PRO A CD  1 
ATOM   355  N  N   . LEU A 1 44  ? 26.89500  25.17200 44.06100 1.000 19.44062  ? 47  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 44  ? 26.33800  25.81300 45.24200 1.000 17.93873  ? 47  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 44  ? 27.44000  26.43600 46.07600 1.000 24.77469  ? 47  LEU A C   1 
ATOM   358  O  O   . LEU A 1 44  ? 28.54200  25.89000 46.18200 1.000 20.03554  ? 47  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 44  ? 25.59100  24.80400 46.10300 1.000 17.21837  ? 47  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 44  ? 24.27000  24.35700 45.52100 1.000 23.10181  ? 47  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 44  ? 23.77400  23.15900 46.30800 1.000 20.54536  ? 47  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 44  ? 23.29800  25.52500 45.60600 1.000 16.15321  ? 47  LEU A CD2 1 
ATOM   363  N  N   . SER A 1 45  ? 27.12900  27.56800 46.69300 1.000 14.86428  ? 48  SER A N   1 
ATOM   364  C  CA  . SER A 1 45  ? 28.01500  28.20800 47.66000 1.000 25.69317  ? 48  SER A CA  1 
ATOM   365  C  C   . SER A 1 45  ? 27.28200  28.25500 48.99100 1.000 21.24539  ? 48  SER A C   1 
ATOM   366  O  O   . SER A 1 45  ? 26.30500  28.99500 49.14200 1.000 22.91187  ? 48  SER A O   1 
ATOM   367  C  CB  . SER A 1 45  ? 28.42800  29.60600 47.20300 1.000 23.13252  ? 48  SER A CB  1 
ATOM   368  O  OG  . SER A 1 45  ? 29.15200  30.26800 48.22400 1.000 26.16879  ? 48  SER A OG  1 
ATOM   369  N  N   . VAL A 1 46  ? 27.74000  27.45100 49.94300 1.000 14.92611  ? 49  VAL A N   1 
ATOM   370  C  CA  . VAL A 1 46  ? 27.15600  27.36700 51.27300 1.000 23.02078  ? 49  VAL A CA  1 
ATOM   371  C  C   . VAL A 1 46  ? 28.15300  27.98900 52.23900 1.000 25.19131  ? 49  VAL A C   1 
ATOM   372  O  O   . VAL A 1 46  ? 29.26200  27.47400 52.42400 1.000 25.23004  ? 49  VAL A O   1 
ATOM   373  C  CB  . VAL A 1 46  ? 26.83200  25.91800 51.65900 1.000 25.38241  ? 49  VAL A CB  1 
ATOM   374  C  CG1 . VAL A 1 46  ? 26.07200  25.87900 52.97100 1.000 28.19236  ? 49  VAL A CG1 1 
ATOM   375  C  CG2 . VAL A 1 46  ? 26.03000  25.24500 50.55000 1.000 27.46673  ? 49  VAL A CG2 1 
ATOM   376  N  N   . SER A 1 47  ? 27.76900  29.10400 52.85000 1.000 17.75143  ? 50  SER A N   1 
ATOM   377  C  CA  A SER A 1 47  ? 28.62300  29.83500 53.78500 0.560 19.29890  ? 50  SER A CA  1 
ATOM   378  C  CA  B SER A 1 47  ? 28.62500  29.83300 53.78200 0.440 19.34888  ? 50  SER A CA  1 
ATOM   379  C  C   . SER A 1 47  ? 27.92000  29.84800 55.13500 1.000 17.42392  ? 50  SER A C   1 
ATOM   380  O  O   . SER A 1 47  ? 27.15800  30.76400 55.43800 1.000 16.44926  ? 50  SER A O   1 
ATOM   381  C  CB  A SER A 1 47  ? 28.91100  31.24300 53.29400 0.560 23.21006  ? 50  SER A CB  1 
ATOM   382  C  CB  B SER A 1 47  ? 28.92100  31.24200 53.27800 0.440 23.19492  ? 50  SER A CB  1 
ATOM   383  O  OG  A SER A 1 47  ? 29.85900  31.21400 52.25000 0.560 26.60725  ? 50  SER A OG  1 
ATOM   384  O  OG  B SER A 1 47  ? 29.79300  31.92000 54.16400 0.440 25.25699  ? 50  SER A OG  1 
ATOM   385  N  N   . TYR A 1 48  ? 28.18900  28.82500 55.94000 1.000 19.77575  ? 51  TYR A N   1 
ATOM   386  C  CA  . TYR A 1 48  ? 27.56600  28.65600 57.24300 1.000 17.50691  ? 51  TYR A CA  1 
ATOM   387  C  C   . TYR A 1 48  ? 28.54600  28.84500 58.39300 1.000 25.46738  ? 51  TYR A C   1 
ATOM   388  O  O   . TYR A 1 48  ? 28.19500  28.55000 59.53900 1.000 24.25562  ? 51  TYR A O   1 
ATOM   389  C  CB  . TYR A 1 48  ? 26.93800  27.26300 57.35400 1.000 13.83143  ? 51  TYR A CB  1 
ATOM   390  C  CG  . TYR A 1 48  ? 25.66400  27.00800 56.55700 1.000 14.21870  ? 51  TYR A CG  1 
ATOM   391  C  CD1 . TYR A 1 48  ? 24.97500  28.03700 55.92400 1.000 15.99433  ? 51  TYR A CD1 1 
ATOM   392  C  CD2 . TYR A 1 48  ? 25.15600  25.72100 56.45400 1.000 13.47126  ? 51  TYR A CD2 1 
ATOM   393  C  CE1 . TYR A 1 48  ? 23.80400  27.78100 55.20500 1.000 15.80560  ? 51  TYR A CE1 1 
ATOM   394  C  CE2 . TYR A 1 48  ? 23.99700  25.45300 55.74600 1.000 15.74004  ? 51  TYR A CE2 1 
ATOM   395  C  CZ  . TYR A 1 48  ? 23.32400  26.48300 55.11600 1.000 18.16229  ? 51  TYR A CZ  1 
ATOM   396  O  OH  . TYR A 1 48  ? 22.16700  26.19700 54.41000 1.000 17.24920  ? 51  TYR A OH  1 
ATOM   397  N  N   . ASP A 1 49  ? 29.75800  29.34000 58.12000 1.000 19.61107  ? 52  ASP A N   1 
ATOM   398  C  CA  . ASP A 1 49  ? 30.76500  29.42500 59.17200 1.000 25.43472  ? 52  ASP A CA  1 
ATOM   399  C  C   . ASP A 1 49  ? 30.35600  30.38700 60.28600 1.000 23.41884  ? 52  ASP A C   1 
ATOM   400  O  O   . ASP A 1 49  ? 30.75800  30.20100 61.44000 1.000 21.76218  ? 52  ASP A O   1 
ATOM   401  C  CB  . ASP A 1 49  ? 32.11700  29.83200 58.57600 1.000 23.40592  ? 52  ASP A CB  1 
ATOM   402  C  CG  . ASP A 1 49  ? 32.02700  31.06500 57.70400 1.000 40.55377  ? 52  ASP A CG  1 
ATOM   403  O  OD1 . ASP A 1 49  ? 31.33900  31.01400 56.66400 1.000 42.26386  ? 52  ASP A OD1 1 
ATOM   404  O  OD2 . ASP A 1 49  ? 32.64200  32.09000 58.06300 1.000 54.56635  ? 52  ASP A OD2 1 
ATOM   405  N  N   . GLN A 1 50  ? 29.55100  31.40100 59.97900 1.000 20.01402  ? 53  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 50  ? 29.15000  32.39400 60.96800 1.000 23.09736  ? 53  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 50  ? 27.72100  32.18600 61.46200 1.000 21.41199  ? 53  GLN A C   1 
ATOM   408  O  O   . GLN A 1 50  ? 27.16100  33.08100 62.10200 1.000 17.78376  ? 53  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 50  ? 29.32200  33.80300 60.39500 1.000 27.64230  ? 53  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 50  ? 30.77600  34.19200 60.14400 1.000 32.83978  ? 53  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 50  ? 31.56400  34.35400 61.43100 1.000 53.53287  ? 53  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 50  ? 31.29800  35.25900 62.22600 1.000 59.68215  ? 53  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 50  ? 32.53000  33.47000 61.65100 1.000 58.43185  ? 53  GLN A NE2 1 
ATOM   414  N  N   . ALA A 1 51  ? 27.13200  31.02000 61.19600 1.000 17.87532  ? 54  ALA A N   1 
ATOM   415  C  CA  . ALA A 1 51  ? 25.75600  30.75500 61.59400 1.000 13.72673  ? 54  ALA A CA  1 
ATOM   416  C  C   . ALA A 1 51  ? 25.56200  30.94300 63.09800 1.000 23.94333  ? 54  ALA A C   1 
ATOM   417  O  O   . ALA A 1 51  ? 26.42000  30.57700 63.90800 1.000 20.28136  ? 54  ALA A O   1 
ATOM   418  C  CB  . ALA A 1 51  ? 25.35600  29.33600 61.17900 1.000 16.68018  ? 54  ALA A CB  1 
ATOM   419  N  N   . THR A 1 52  ? 24.42600  31.53000 63.47000 1.000 17.92801  ? 55  THR A N   1 
ATOM   420  C  CA  . THR A 1 52  ? 24.06600  31.73900 64.87100 1.000 10.29534  ? 55  THR A CA  1 
ATOM   421  C  C   . THR A 1 52  ? 22.70800  31.09900 65.13700 1.000 15.39596  ? 55  THR A C   1 
ATOM   422  O  O   . THR A 1 52  ? 21.66500  31.71600 64.90000 1.000 16.43264  ? 55  THR A O   1 
ATOM   423  C  CB  . THR A 1 52  ? 24.03000  33.22400 65.21800 1.000 19.00309  ? 55  THR A CB  1 
ATOM   424  O  OG1 . THR A 1 52  ? 25.35000  33.76400 65.11800 1.000 28.80030  ? 55  THR A OG1 1 
ATOM   425  C  CG2 . THR A 1 52  ? 23.50100  33.41300 66.64700 1.000 27.15187  ? 55  THR A CG2 1 
ATOM   426  N  N   . SER A 1 53  ? 22.70400  29.88400 65.66400 1.000 10.50024  ? 56  SER A N   1 
ATOM   427  C  CA  . SER A 1 53  ? 21.43200  29.29400 66.04600 1.000 17.51205  ? 56  SER A CA  1 
ATOM   428  C  C   . SER A 1 53  ? 20.96100  29.92400 67.35100 1.000 19.80031  ? 56  SER A C   1 
ATOM   429  O  O   . SER A 1 53  ? 21.76000  30.41800 68.15400 1.000 19.34696  ? 56  SER A O   1 
ATOM   430  C  CB  . SER A 1 53  ? 21.53900  27.77100 66.17800 1.000 12.69440  ? 56  SER A CB  1 
ATOM   431  O  OG  . SER A 1 53  ? 22.36700  27.40300 67.26600 1.000 18.45993  ? 56  SER A OG  1 
ATOM   432  N  N   . LEU A 1 54  ? 19.64600  29.93300 67.54200 1.000 15.73090  ? 57  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 54  ? 19.04600  30.57800 68.70000 1.000 13.38303  ? 57  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 54  ? 18.18700  29.63700 69.52200 1.000 18.45994  ? 57  LEU A C   1 
ATOM   435  O  O   . LEU A 1 54  ? 18.30500  29.60800 70.75300 1.000 15.48420  ? 57  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 54  ? 18.19500  31.76900 68.24500 1.000 16.00595  ? 57  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 54  ? 18.94100  32.94900 67.63100 1.000 19.67982  ? 57  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 54  ? 17.96500  33.97700 67.06000 1.000 27.85041  ? 57  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 54  ? 19.83500  33.56300 68.68000 1.000 22.00538  ? 57  LEU A CD2 1 
ATOM   440  N  N   . ARG A 1 55  ? 17.32600  28.86300 68.87000 1.000 9.65791   ? 58  ARG A N   1 
ATOM   441  C  CA  . ARG A 1 55  ? 16.20100  28.27300 69.57400 1.000 11.06681  ? 58  ARG A CA  1 
ATOM   442  C  C   . ARG A 1 55  ? 15.76100  27.04300 68.80400 1.000 12.59257  ? 58  ARG A C   1 
ATOM   443  O  O   . ARG A 1 55  ? 16.00500  26.94000 67.60300 1.000 13.66513  ? 58  ARG A O   1 
ATOM   444  C  CB  . ARG A 1 55  ? 15.06500  29.30200 69.68200 1.000 15.04814  ? 58  ARG A CB  1 
ATOM   445  C  CG  . ARG A 1 55  ? 14.03400  29.06100 70.74300 1.000 26.70288  ? 58  ARG A CG  1 
ATOM   446  C  CD  . ARG A 1 55  ? 13.14600  30.28700 70.84100 1.000 23.70996  ? 58  ARG A CD  1 
ATOM   447  N  NE  . ARG A 1 55  ? 12.28500  30.43400 69.67000 1.000 27.06097  ? 58  ARG A NE  1 
ATOM   448  C  CZ  . ARG A 1 55  ? 10.96400  30.53100 69.73200 1.000 21.53557  ? 58  ARG A CZ  1 
ATOM   449  N  NH1 . ARG A 1 55  ? 10.32700  30.51700 70.89100 1.000 17.04650  ? 58  ARG A NH1 1 
ATOM   450  N  NH2 . ARG A 1 55  ? 10.26700  30.65300 68.60700 1.000 19.30665  ? 58  ARG A NH2 1 
ATOM   451  N  N   . ILE A 1 56  ? 15.14900  26.09900 69.51000 1.000 10.41107  ? 59  ILE A N   1 
ATOM   452  C  CA  . ILE A 1 56  ? 14.49500  24.96200 68.88100 1.000 10.96128  ? 59  ILE A CA  1 
ATOM   453  C  C   . ILE A 1 56  ? 13.07500  24.89400 69.41500 1.000 15.73681  ? 59  ILE A C   1 
ATOM   454  O  O   . ILE A 1 56  ? 12.83700  25.11700 70.61100 1.000 11.08082  ? 59  ILE A O   1 
ATOM   455  C  CB  . ILE A 1 56  ? 15.26400  23.64100 69.12700 1.000 10.18889  ? 59  ILE A CB  1 
ATOM   456  C  CG1 . ILE A 1 56  ? 14.61900  22.48700 68.35900 1.000 10.09678  ? 59  ILE A CG1 1 
ATOM   457  C  CG2 . ILE A 1 56  ? 15.36500  23.31700 70.61900 1.000 11.23269  ? 59  ILE A CG2 1 
ATOM   458  C  CD1 . ILE A 1 56  ? 15.52200  21.24400 68.24000 1.000 11.95797  ? 59  ILE A CD1 1 
ATOM   459  N  N   . LEU A 1 57  ? 12.12800  24.61400 68.52300 1.000 9.61404   ? 60  LEU A N   1 
ATOM   460  C  CA  . LEU A 1 57  ? 10.71900  24.83200 68.81200 1.000 15.30511  ? 60  LEU A CA  1 
ATOM   461  C  C   . LEU A 1 57  ? 9.89400   23.72200 68.18400 1.000 15.63164  ? 60  LEU A C   1 
ATOM   462  O  O   . LEU A 1 57  ? 10.11800  23.36200 67.02900 1.000 12.73328  ? 60  LEU A O   1 
ATOM   463  C  CB  . LEU A 1 57  ? 10.24700  26.19800 68.26400 1.000 18.24993  ? 60  LEU A CB  1 
ATOM   464  C  CG  . LEU A 1 57  ? 8.73900   26.36400 68.03100 1.000 23.12620  ? 60  LEU A CG  1 
ATOM   465  C  CD1 . LEU A 1 57  ? 7.98500   26.57400 69.35200 1.000 23.01316  ? 60  LEU A CD1 1 
ATOM   466  C  CD2 . LEU A 1 57  ? 8.42700   27.47600 67.03100 1.000 20.30749  ? 60  LEU A CD2 1 
ATOM   467  N  N   . ASN A 1 58  ? 8.94500   23.18600 68.94800 1.000 15.73106  ? 61  ASN A N   1 
ATOM   468  C  CA  . ASN A 1 58  ? 7.95600   22.23400 68.44400 1.000 13.72860  ? 61  ASN A CA  1 
ATOM   469  C  C   . ASN A 1 58  ? 6.72400   23.05300 68.09800 1.000 14.34109  ? 61  ASN A C   1 
ATOM   470  O  O   . ASN A 1 58  ? 6.06800   23.59200 68.99300 1.000 12.69314  ? 61  ASN A O   1 
ATOM   471  C  CB  . ASN A 1 58  ? 7.64500   21.16200 69.49100 1.000 10.09319  ? 61  ASN A CB  1 
ATOM   472  C  CG  . ASN A 1 58  ? 6.58600   20.16000 69.03900 1.000 13.08328  ? 61  ASN A CG  1 
ATOM   473  O  OD1 . ASN A 1 58  ? 5.78500   20.43300 68.15100 1.000 16.90664  ? 61  ASN A OD1 1 
ATOM   474  N  ND2 . ASN A 1 58  ? 6.57800   18.98200 69.67000 1.000 15.74023  ? 61  ASN A ND2 1 
ATOM   475  N  N   . ASN A 1 59  ? 6.41500   23.15500 66.80500 1.000 12.81007  ? 62  ASN A N   1 
ATOM   476  C  CA  . ASN A 1 59  ? 5.31500   23.99600 66.34600 1.000 15.19333  ? 62  ASN A CA  1 
ATOM   477  C  C   . ASN A 1 59  ? 4.05900   23.19200 66.03800 1.000 18.25037  ? 62  ASN A C   1 
ATOM   478  O  O   . ASN A 1 59  ? 3.14900   23.70400 65.38300 1.000 20.39167  ? 62  ASN A O   1 
ATOM   479  C  CB  . ASN A 1 59  ? 5.74300   24.81900 65.11800 1.000 17.79050  ? 62  ASN A CB  1 
ATOM   480  C  CG  . ASN A 1 59  ? 6.05500   23.95600 63.89900 1.000 17.50009  ? 62  ASN A CG  1 
ATOM   481  O  OD1 . ASN A 1 59  ? 5.73900   22.77300 63.85700 1.000 15.54979  ? 62  ASN A OD1 1 
ATOM   482  N  ND2 . ASN A 1 59  ? 6.67900   24.56200 62.89500 1.000 19.49517  ? 62  ASN A ND2 1 
ATOM   483  N  N   . GLY A 1 60  ? 4.00500   21.93200 66.46100 1.000 14.54810  ? 63  GLY A N   1 
ATOM   484  C  CA  . GLY A 1 60  ? 2.82800   21.12700 66.26600 1.000 12.79635  ? 63  GLY A CA  1 
ATOM   485  C  C   . GLY A 1 60  ? 2.82000   20.30100 65.00100 1.000 13.63122  ? 63  GLY A C   1 
ATOM   486  O  O   . GLY A 1 60  ? 1.96800   19.41800 64.87200 1.000 16.40197  ? 63  GLY A O   1 
ATOM   487  N  N   . HIS A 1 61  ? 3.72500   20.56300 64.05000 1.000 16.83548  ? 64  HIS A N   1 
ATOM   488  C  CA  . HIS A 1 61  ? 3.85600   19.67400 62.90300 1.000 18.76978  ? 64  HIS A CA  1 
ATOM   489  C  C   . HIS A 1 61  ? 5.28700   19.30200 62.56900 1.000 14.98578  ? 64  HIS A C   1 
ATOM   490  O  O   . HIS A 1 61  ? 5.48200   18.38800 61.75900 1.000 20.75143  ? 64  HIS A O   1 
ATOM   491  C  CB  . HIS A 1 61  ? 3.18200   20.26000 61.65200 1.000 21.73460  ? 64  HIS A CB  1 
ATOM   492  C  CG  . HIS A 1 61  ? 3.56600   21.67200 61.33300 1.000 26.59428  ? 64  HIS A CG  1 
ATOM   493  N  ND1 . HIS A 1 61  ? 2.85100   22.76100 61.78500 1.000 31.21162  ? 64  HIS A ND1 1 
ATOM   494  C  CD2 . HIS A 1 61  ? 4.61500   22.17300 60.63900 1.000 31.77875  ? 64  HIS A CD2 1 
ATOM   495  C  CE1 . HIS A 1 61  ? 3.43600   23.87200 61.37100 1.000 35.79354  ? 64  HIS A CE1 1 
ATOM   496  N  NE2 . HIS A 1 61  ? 4.50600   23.54200 60.67100 1.000 32.17446  ? 64  HIS A NE2 1 
ATOM   497  N  N   . ALA A 1 62  ? 6.27700   19.93800 63.17900 1.000 10.06648  ? 65  ALA A N   1 
ATOM   498  C  CA  . ALA A 1 62  ? 7.67000   19.50700 63.13400 1.000 10.90077  ? 65  ALA A CA  1 
ATOM   499  C  C   . ALA A 1 62  ? 8.39500   20.25300 64.25100 1.000 15.30803  ? 65  ALA A C   1 
ATOM   500  O  O   . ALA A 1 62  ? 7.76400   20.90100 65.09400 1.000 13.13413  ? 65  ALA A O   1 
ATOM   501  C  CB  . ALA A 1 62  ? 8.29800   19.77900 61.77600 1.000 14.09199  ? 65  ALA A CB  1 
ATOM   502  N  N   . PHE A 1 63  ? 9.72200   20.12400 64.26800 1.000 13.83517  ? 66  PHE A N   1 
ATOM   503  C  CA  . PHE A 1 63  ? 10.51400  20.94800 65.21100 1.000 13.10488  ? 66  PHE A CA  1 
ATOM   504  C  C   . PHE A 1 63  ? 11.42500  21.80000 64.33700 1.000 11.91879  ? 66  PHE A C   1 
ATOM   505  O  O   . PHE A 1 63  ? 11.98700  21.30600 63.36300 1.000 12.28393  ? 66  PHE A O   1 
ATOM   506  C  CB  . PHE A 1 63  ? 11.35500  20.23900 66.26700 1.000 9.12555   ? 66  PHE A CB  1 
ATOM   507  C  CG  . PHE A 1 63  ? 12.32100  19.19900 65.72300 1.000 10.37785  ? 66  PHE A CG  1 
ATOM   508  C  CD1 . PHE A 1 63  ? 11.91400  17.88600 65.53700 1.000 18.10647  ? 66  PHE A CD1 1 
ATOM   509  C  CD2 . PHE A 1 63  ? 13.63100  19.53200 65.40400 1.000 12.12857  ? 66  PHE A CD2 1 
ATOM   510  C  CE1 . PHE A 1 63  ? 12.79000  16.93600 65.04100 1.000 15.02727  ? 66  PHE A CE1 1 
ATOM   511  C  CE2 . PHE A 1 63  ? 14.49800  18.57900 64.90600 1.000 11.91854  ? 66  PHE A CE2 1 
ATOM   512  C  CZ  . PHE A 1 63  ? 14.07600  17.28700 64.72700 1.000 14.34513  ? 66  PHE A CZ  1 
ATOM   513  N  N   . ASN A 1 64  ? 11.53200  23.06600 64.69700 1.000 12.94602  ? 67  ASN A N   1 
ATOM   514  C  CA  . ASN A 1 64  ? 12.34000  23.97800 63.87100 1.000 9.33310   ? 67  ASN A CA  1 
ATOM   515  C  C   . ASN A 1 64  ? 13.55700  24.46000 64.65800 1.000 11.34721  ? 67  ASN A C   1 
ATOM   516  O  O   . ASN A 1 64  ? 13.37400  24.84200 65.80600 1.000 13.96233  ? 67  ASN A O   1 
ATOM   517  C  CB  . ASN A 1 64  ? 11.56500  25.23200 63.49400 1.000 14.90936  ? 67  ASN A CB  1 
ATOM   518  C  CG  . ASN A 1 64  ? 10.53700  25.01300 62.41200 1.000 14.35900  ? 67  ASN A CG  1 
ATOM   519  O  OD1 . ASN A 1 64  ? 10.30600  23.88200 61.98500 1.000 14.67386  ? 67  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A 1 64  ? 9.90500   26.08900 61.97100 1.000 24.00672  ? 67  ASN A ND2 1 
ATOM   521  N  N   . VAL A 1 65  ? 14.73500  24.39400 64.05500 1.000 7.74887   ? 68  VAL A N   1 
ATOM   522  C  CA  . VAL A 1 65  ? 15.92000  25.03500 64.68400 1.000 8.16481   ? 68  VAL A CA  1 
ATOM   523  C  C   . VAL A 1 65  ? 16.01600  26.42000 64.01000 1.000 15.40243  ? 68  VAL A C   1 
ATOM   524  O  O   . VAL A 1 65  ? 16.13400  26.43900 62.77800 1.000 12.52681  ? 68  VAL A O   1 
ATOM   525  C  CB  . VAL A 1 65  ? 17.21900  24.21200 64.58700 1.000 14.88661  ? 68  VAL A CB  1 
ATOM   526  C  CG1 . VAL A 1 65  ? 18.42800  25.00400 65.07000 1.000 14.21900  ? 68  VAL A CG1 1 
ATOM   527  C  CG2 . VAL A 1 65  ? 17.10300  22.88000 65.30700 1.000 13.09719  ? 68  VAL A CG2 1 
ATOM   528  N  N   . GLU A 1 66  ? 15.88000  27.50600 64.76700 1.000 9.16966   ? 69  GLU A N   1 
ATOM   529  C  CA  . GLU A 1 66  ? 15.83100  28.85300 64.21600 1.000 7.46086   ? 69  GLU A CA  1 
ATOM   530  C  C   . GLU A 1 66  ? 17.17900  29.54400 64.36600 1.000 15.48521  ? 69  GLU A C   1 
ATOM   531  O  O   . GLU A 1 66  ? 17.90700  29.32700 65.33900 1.000 15.12747  ? 69  GLU A O   1 
ATOM   532  C  CB  . GLU A 1 66  ? 14.76200  29.70200 64.90400 1.000 13.79157  ? 69  GLU A CB  1 
ATOM   533  C  CG  . GLU A 1 66  ? 13.41600  29.04400 64.97700 1.000 13.93428  ? 69  GLU A CG  1 
ATOM   534  C  CD  . GLU A 1 66  ? 12.48000  29.76400 65.94200 1.000 21.12098  ? 69  GLU A CD  1 
ATOM   535  O  OE1 . GLU A 1 66  ? 12.97600  30.43100 66.86800 1.000 23.54038  ? 69  GLU A OE1 1 
ATOM   536  O  OE2 . GLU A 1 66  ? 11.25400  29.66600 65.76800 1.000 27.48117  ? 69  GLU A OE2 1 
ATOM   537  N  N   . PHE A 1 67  ? 17.49200  30.39300 63.39500 1.000 12.39758  ? 70  PHE A N   1 
ATOM   538  C  CA  . PHE A 1 67  ? 18.76400  31.09100 63.31200 1.000 11.96243  ? 70  PHE A CA  1 
ATOM   539  C  C   . PHE A 1 67  ? 18.52100  32.59200 63.32700 1.000 9.25204   ? 70  PHE A C   1 
ATOM   540  O  O   . PHE A 1 67  ? 17.44000  33.05300 62.97800 1.000 11.15119  ? 70  PHE A O   1 
ATOM   541  C  CB  . PHE A 1 67  ? 19.52000  30.68500 62.04100 1.000 9.34115   ? 70  PHE A CB  1 
ATOM   542  C  CG  . PHE A 1 67  ? 20.04200  29.27800 62.09200 1.000 15.53790  ? 70  PHE A CG  1 
ATOM   543  C  CD1 . PHE A 1 67  ? 19.21500  28.21400 61.79500 1.000 13.31724  ? 70  PHE A CD1 1 
ATOM   544  C  CD2 . PHE A 1 67  ? 21.34900  29.02100 62.47800 1.000 13.57183  ? 70  PHE A CD2 1 
ATOM   545  C  CE1 . PHE A 1 67  ? 19.68600  26.89900 61.86900 1.000 12.36469  ? 70  PHE A CE1 1 
ATOM   546  C  CE2 . PHE A 1 67  ? 21.82300  27.72000 62.55000 1.000 14.96283  ? 70  PHE A CE2 1 
ATOM   547  C  CZ  . PHE A 1 67  ? 20.99100  26.66200 62.25400 1.000 16.45176  ? 70  PHE A CZ  1 
ATOM   548  N  N   . ASP A 1 68  ? 19.53300  33.34200 63.75800 1.000 13.17866  ? 71  ASP A N   1 
ATOM   549  C  CA  . ASP A 1 68  ? 19.53400  34.80000 63.63300 1.000 15.88454  ? 71  ASP A CA  1 
ATOM   550  C  C   . ASP A 1 68  ? 19.70800  35.17400 62.16400 1.000 15.21405  ? 71  ASP A C   1 
ATOM   551  O  O   . ASP A 1 68  ? 20.75200  34.89400 61.56700 1.000 17.18644  ? 71  ASP A O   1 
ATOM   552  C  CB  . ASP A 1 68  ? 20.65500  35.39100 64.48600 1.000 18.18808  ? 71  ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 68  ? 20.84500  36.89900 64.26600 1.000 26.76075  ? 71  ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 68  ? 19.95300  37.55200 63.70400 1.000 22.00514  ? 71  ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 68  ? 21.90300  37.42400 64.65300 1.000 29.01726  ? 71  ASP A OD2 1 
ATOM   556  N  N   . ASP A 1 69  ? 18.68800  35.80100 61.57000 1.000 14.81232  ? 72  ASP A N   1 
ATOM   557  C  CA  . ASP A 1 69  ? 18.72200  36.16400 60.15600 1.000 15.37207  ? 72  ASP A CA  1 
ATOM   558  C  C   . ASP A 1 69  ? 18.65900  37.68000 59.96200 1.000 21.38583  ? 72  ASP A C   1 
ATOM   559  O  O   . ASP A 1 69  ? 18.20000  38.16300 58.92300 1.000 20.14055  ? 72  ASP A O   1 
ATOM   560  C  CB  . ASP A 1 69  ? 17.58900  35.47400 59.38500 1.000 15.91610  ? 72  ASP A CB  1 
ATOM   561  C  CG  . ASP A 1 69  ? 16.20200  35.94500 59.82000 1.000 21.30978  ? 72  ASP A CG  1 
ATOM   562  O  OD1 . ASP A 1 69  ? 16.09800  36.61600 60.86100 1.000 18.09775  ? 72  ASP A OD1 1 
ATOM   563  O  OD2 . ASP A 1 69  ? 15.21000  35.65000 59.11300 1.000 19.37562  ? 72  ASP A OD2 1 
ATOM   564  N  N   . SER A 1 70  ? 19.12200  38.44400 60.95400 1.000 18.54081  ? 73  SER A N   1 
ATOM   565  C  CA  . SER A 1 70  ? 19.14300  39.89700 60.84700 1.000 21.69268  ? 73  SER A CA  1 
ATOM   566  C  C   . SER A 1 70  ? 20.36600  40.42800 60.11200 1.000 28.08900  ? 73  SER A C   1 
ATOM   567  O  O   . SER A 1 70  ? 20.43900  41.63700 59.86100 1.000 35.25271  ? 73  SER A O   1 
ATOM   568  C  CB  . SER A 1 70  ? 19.07300  40.53100 62.24100 1.000 22.73181  ? 73  SER A CB  1 
ATOM   569  O  OG  . SER A 1 70  ? 20.16800  40.12400 63.05200 1.000 25.55479  ? 73  SER A OG  1 
ATOM   570  N  N   . GLN A 1 71  ? 21.33200  39.57300 59.77700 1.000 22.99040  ? 74  GLN A N   1 
ATOM   571  C  CA  . GLN A 1 71  ? 22.47300  39.94500 58.95300 1.000 20.26294  ? 74  GLN A CA  1 
ATOM   572  C  C   . GLN A 1 71  ? 22.88300  38.74100 58.12100 1.000 25.48786  ? 74  GLN A C   1 
ATOM   573  O  O   . GLN A 1 71  ? 22.50400  37.60500 58.40900 1.000 23.29343  ? 74  GLN A O   1 
ATOM   574  C  CB  . GLN A 1 71  ? 23.68100  40.40100 59.78100 1.000 24.00913  ? 74  GLN A CB  1 
ATOM   575  C  CG  . GLN A 1 71  ? 23.39500  41.36800 60.89800 1.000 30.35664  ? 74  GLN A CG  1 
ATOM   576  C  CD  . GLN A 1 71  ? 24.62400  41.61600 61.74400 1.000 35.77258  ? 74  GLN A CD  1 
ATOM   577  O  OE1 . GLN A 1 71  ? 25.52800  42.34800 61.34000 1.000 40.06375  ? 74  GLN A OE1 1 
ATOM   578  N  NE2 . GLN A 1 71  ? 24.67800  40.98600 62.91600 1.000 32.57934  ? 74  GLN A NE2 1 
ATOM   579  N  N   . ASP A 1 72  ? 23.68600  38.99400 57.08800 1.000 26.93880  ? 75  ASP A N   1 
ATOM   580  C  CA  . ASP A 1 72  ? 24.22600  37.92000 56.25400 1.000 22.29476  ? 75  ASP A CA  1 
ATOM   581  C  C   . ASP A 1 72  ? 25.27400  37.15800 57.06300 1.000 28.74342  ? 75  ASP A C   1 
ATOM   582  O  O   . ASP A 1 72  ? 26.47500  37.41900 56.99500 1.000 39.76220  ? 75  ASP A O   1 
ATOM   583  C  CB  . ASP A 1 72  ? 24.82000  38.47300 54.96500 1.000 28.18466  ? 75  ASP A CB  1 
ATOM   584  C  CG  . ASP A 1 72  ? 23.77700  39.10500 54.05900 1.000 29.34354  ? 75  ASP A CG  1 
ATOM   585  O  OD1 . ASP A 1 72  ? 22.57100  38.87900 54.27900 1.000 27.88114  ? 75  ASP A OD1 1 
ATOM   586  O  OD2 . ASP A 1 72  ? 24.17200  39.83000 53.12400 1.000 29.53271  ? 75  ASP A OD2 1 
ATOM   587  N  N   . LYS A 1 73  ? 24.79800  36.19600 57.85200 1.000 19.25065  ? 76  LYS A N   1 
ATOM   588  C  CA  . LYS A 1 73  ? 25.66400  35.33100 58.64600 1.000 18.28067  ? 76  LYS A CA  1 
ATOM   589  C  C   . LYS A 1 73  ? 25.80000  33.93900 58.04600 1.000 24.55789  ? 76  LYS A C   1 
ATOM   590  O  O   . LYS A 1 73  ? 26.91100  33.42000 57.90700 1.000 31.57724  ? 76  LYS A O   1 
ATOM   591  C  CB  . LYS A 1 73  ? 25.12200  35.20700 60.07600 1.000 23.13251  ? 76  LYS A CB  1 
ATOM   592  C  CG  . LYS A 1 73  ? 25.49800  36.33600 61.01400 1.000 35.05407  ? 76  LYS A CG  1 
ATOM   593  C  CD  . LYS A 1 73  ? 24.93100  36.05900 62.39800 1.000 30.04739  ? 76  LYS A CD  1 
ATOM   594  C  CE  . LYS A 1 73  ? 25.37200  37.10400 63.40600 1.000 40.01852  ? 76  LYS A CE  1 
ATOM   595  N  NZ  . LYS A 1 73  ? 24.80200  36.81100 64.74800 1.000 37.26347  ? 76  LYS A NZ  1 
ATOM   596  N  N   . ALA A 1 74  ? 24.67700  33.31400 57.71700 1.000 15.34192  ? 77  ALA A N   1 
ATOM   597  C  CA  . ALA A 1 74  ? 24.63500  31.98100 57.12700 1.000 18.93498  ? 77  ALA A CA  1 
ATOM   598  C  C   . ALA A 1 74  ? 23.84600  32.09700 55.82800 1.000 15.44586  ? 77  ALA A C   1 
ATOM   599  O  O   . ALA A 1 74  ? 22.63100  32.31100 55.85300 1.000 16.20419  ? 77  ALA A O   1 
ATOM   600  C  CB  . ALA A 1 74  ? 23.99400  30.98300 58.09000 1.000 10.61812  ? 77  ALA A CB  1 
ATOM   601  N  N   . VAL A 1 75  ? 24.52400  31.98800 54.69000 1.000 14.50685  ? 78  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 75  ? 23.88300  32.31500 53.42600 1.000 15.36500  ? 78  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 75  ? 24.13600  31.22800 52.39100 1.000 21.34030  ? 78  VAL A C   1 
ATOM   604  O  O   . VAL A 1 75  ? 25.12000  30.48800 52.44100 1.000 18.92749  ? 78  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 75  ? 24.34300  33.68200 52.87700 1.000 18.59376  ? 78  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 75  ? 24.00700  34.79600 53.86200 1.000 24.65762  ? 78  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 75  ? 25.83100  33.64900 52.56100 1.000 18.76162  ? 78  VAL A CG2 1 
ATOM   608  N  N   . LEU A 1 76  ? 23.22500  31.17100 51.43200 1.000 13.33754  ? 79  LEU A N   1 
ATOM   609  C  CA  . LEU A 1 76  ? 23.28800  30.27100 50.29700 1.000 12.49487  ? 79  LEU A CA  1 
ATOM   610  C  C   . LEU A 1 76  ? 23.33300  31.12800 49.03900 1.000 18.19296  ? 79  LEU A C   1 
ATOM   611  O  O   . LEU A 1 76  ? 22.55000  32.07400 48.90400 1.000 17.41186  ? 79  LEU A O   1 
ATOM   612  C  CB  . LEU A 1 76  ? 22.07300  29.33600 50.30800 1.000 12.38725  ? 79  LEU A CB  1 
ATOM   613  C  CG  . LEU A 1 76  ? 21.88800  28.33000 49.18000 1.000 17.64293  ? 79  LEU A CG  1 
ATOM   614  C  CD1 . LEU A 1 76  ? 23.08600  27.40300 49.12500 1.000 18.48878  ? 79  LEU A CD1 1 
ATOM   615  C  CD2 . LEU A 1 76  ? 20.57900  27.55400 49.38200 1.000 16.99172  ? 79  LEU A CD2 1 
ATOM   616  N  N   . LYS A 1 77  ? 24.31600  30.78600 48.15400 1.000 15.05262  ? 80  LYS A N   1 
ATOM   617  C  CA  . LYS A 1 77  ? 24.40300  31.57500 46.91200 1.000 21.63105  ? 80  LYS A CA  1 
ATOM   618  C  C   . LYS A 1 77  ? 24.74400  30.60900 45.78300 1.000 15.48265  ? 80  LYS A C   1 
ATOM   619  O  O   . LYS A 1 77  ? 24.86700  29.41200 46.04300 1.000 16.76274  ? 80  LYS A O   1 
ATOM   620  C  CB  . LYS A 1 77  ? 25.47400  32.67200 46.90400 1.000 22.21310  ? 80  LYS A CB  1 
ATOM   621  C  CG  . LYS A 1 77  ? 25.26600  33.85800 47.82800 1.000 38.38878  ? 80  LYS A CG  1 
ATOM   622  C  CD  . LYS A 1 77  ? 26.35900  34.90900 47.70700 1.000 40.18629  ? 80  LYS A CD  1 
ATOM   623  C  CE  . LYS A 1 77  ? 27.69800  34.47400 48.20000 1.000 56.85412  ? 80  LYS A CE  1 
ATOM   624  N  NZ  . LYS A 1 77  ? 27.68100  34.17500 49.63600 1.000 65.11717  ? 80  LYS A NZ  1 
ATOM   625  N  N   . GLY A 1 78  ? 24.87200  31.10200 44.58500 1.000 20.73060  ? 81  GLY A N   1 
ATOM   626  C  CA  . GLY A 1 78  ? 25.28400  30.25300 43.48800 1.000 19.90253  ? 81  GLY A CA  1 
ATOM   627  C  C   . GLY A 1 78  ? 24.19500  29.26800 43.10600 1.000 19.88820  ? 81  GLY A C   1 
ATOM   628  O  O   . GLY A 1 78  ? 22.99700  29.52200 43.27600 1.000 17.82677  ? 81  GLY A O   1 
ATOM   629  N  N   . GLY A 1 79  ? 24.61600  28.12300 42.57800 1.000 22.17184  ? 82  GLY A N   1 
ATOM   630  C  CA  . GLY A 1 79  ? 23.67000  27.18600 42.02700 1.000 20.29128  ? 82  GLY A CA  1 
ATOM   631  C  C   . GLY A 1 79  ? 22.76900  27.88900 41.03300 1.000 16.35653  ? 82  GLY A C   1 
ATOM   632  O  O   . GLY A 1 79  ? 23.22600  28.70700 40.22900 1.000 16.95702  ? 82  GLY A O   1 
ATOM   633  N  N   . PRO A 1 80  ? 21.46300  27.61800 41.09300 1.000 18.44723  ? 83  PRO A N   1 
ATOM   634  C  CA  . PRO A 1 80  ? 20.51000  28.28800 40.20000 1.000 21.20673  ? 83  PRO A CA  1 
ATOM   635  C  C   . PRO A 1 80  ? 20.05100  29.65100 40.68700 1.000 21.56959  ? 83  PRO A C   1 
ATOM   636  O  O   . PRO A 1 80  ? 19.13900  30.22800 40.08400 1.000 19.91187  ? 83  PRO A O   1 
ATOM   637  C  CB  . PRO A 1 80  ? 19.33400  27.30400 40.20200 1.000 20.25341  ? 83  PRO A CB  1 
ATOM   638  C  CG  . PRO A 1 80  ? 19.31800  26.82000 41.62700 1.000 20.40218  ? 83  PRO A CG  1 
ATOM   639  C  CD  . PRO A 1 80  ? 20.77700  26.71400 42.03900 1.000 21.50159  ? 83  PRO A CD  1 
ATOM   640  N  N   . LEU A 1 81  ? 20.62100  30.14600 41.78100 1.000 16.40678  ? 84  LEU A N   1 
ATOM   641  C  CA  . LEU A 1 81  ? 20.11600  31.32500 42.46700 1.000 9.97440   ? 84  LEU A CA  1 
ATOM   642  C  C   . LEU A 1 81  ? 20.79600  32.59500 41.97400 1.000 20.66370  ? 84  LEU A C   1 
ATOM   643  O  O   . LEU A 1 81  ? 21.98000  32.59400 41.62500 1.000 20.85195  ? 84  LEU A O   1 
ATOM   644  C  CB  . LEU A 1 81  ? 20.33800  31.20100 43.97500 1.000 15.30906  ? 84  LEU A CB  1 
ATOM   645  C  CG  . LEU A 1 81  ? 19.76900  29.95000 44.64500 1.000 11.85387  ? 84  LEU A CG  1 
ATOM   646  C  CD1 . LEU A 1 81  ? 20.12900  29.93700 46.12400 1.000 17.32854  ? 84  LEU A CD1 1 
ATOM   647  C  CD2 . LEU A 1 81  ? 18.24800  29.85200 44.43200 1.000 13.12897  ? 84  LEU A CD2 1 
ATOM   648  N  N   . ASP A 1 82  ? 20.03100  33.68400 41.97800 1.000 19.07759  ? 85  ASP A N   1 
ATOM   649  C  CA  . ASP A 1 82  ? 20.53400  35.04100 41.80900 1.000 24.15027  ? 85  ASP A CA  1 
ATOM   650  C  C   . ASP A 1 82  ? 20.44000  35.73300 43.15800 1.000 27.36111  ? 85  ASP A C   1 
ATOM   651  O  O   . ASP A 1 82  ? 19.41200  35.64100 43.83200 1.000 27.68567  ? 85  ASP A O   1 
ATOM   652  C  CB  . ASP A 1 82  ? 19.71700  35.83000 40.78400 1.000 33.82694  ? 85  ASP A CB  1 
ATOM   653  C  CG  . ASP A 1 82  ? 19.61500  35.13400 39.45100 1.000 49.78220  ? 85  ASP A CG  1 
ATOM   654  O  OD1 . ASP A 1 82  ? 20.65100  34.64400 38.94800 1.000 61.07172  ? 85  ASP A OD1 1 
ATOM   655  O  OD2 . ASP A 1 82  ? 18.49000  35.07600 38.90400 1.000 68.47285  ? 85  ASP A OD2 1 
ATOM   656  N  N   . GLY A 1 83  ? 21.49000  36.41700 43.55500 1.000 26.02643  ? 86  GLY A N   1 
ATOM   657  C  CA  . GLY A 1 83  ? 21.43900  37.08600 44.83500 1.000 23.50649  ? 86  GLY A CA  1 
ATOM   658  C  C   . GLY A 1 83  ? 21.73700  36.15600 46.00000 1.000 29.00647  ? 86  GLY A C   1 
ATOM   659  O  O   . GLY A 1 83  ? 22.19000  35.02000 45.84200 1.000 26.63980  ? 86  GLY A O   1 
ATOM   660  N  N   . THR A 1 84  ? 21.45100  36.66400 47.19800 1.000 20.64595  ? 87  THR A N   1 
ATOM   661  C  CA  . THR A 1 84  ? 21.87800  36.06700 48.45500 1.000 18.50511  ? 87  THR A CA  1 
ATOM   662  C  C   . THR A 1 84  ? 20.65500  35.64500 49.25900 1.000 20.12452  ? 87  THR A C   1 
ATOM   663  O  O   . THR A 1 84  ? 19.72000  36.43300 49.42400 1.000 15.17831  ? 87  THR A O   1 
ATOM   664  C  CB  . THR A 1 84  ? 22.71200  37.07100 49.26100 1.000 30.72609  ? 87  THR A CB  1 
ATOM   665  O  OG1 . THR A 1 84  ? 23.79400  37.56100 48.45600 1.000 32.99586  ? 87  THR A OG1 1 
ATOM   666  C  CG2 . THR A 1 84  ? 23.26900  36.42800 50.51100 1.000 26.46847  ? 87  THR A CG2 1 
ATOM   667  N  N   . TYR A 1 85  ? 20.66600  34.41200 49.76700 1.000 11.72933  ? 88  TYR A N   1 
ATOM   668  C  CA  . TYR A 1 85  ? 19.57200  33.89300 50.57400 1.000 13.20514  ? 88  TYR A CA  1 
ATOM   669  C  C   . TYR A 1 85  ? 20.09000  33.58500 51.97400 1.000 13.37375  ? 88  TYR A C   1 
ATOM   670  O  O   . TYR A 1 85  ? 21.07600  32.85300 52.11900 1.000 17.22546  ? 88  TYR A O   1 
ATOM   671  C  CB  . TYR A 1 85  ? 18.97300  32.63000 49.92500 1.000 9.45347   ? 88  TYR A CB  1 
ATOM   672  C  CG  . TYR A 1 85  ? 18.20300  32.85500 48.62400 1.000 14.35094  ? 88  TYR A CG  1 
ATOM   673  C  CD1 . TYR A 1 85  ? 18.85600  33.25800 47.45800 1.000 15.09842  ? 88  TYR A CD1 1 
ATOM   674  C  CD2 . TYR A 1 85  ? 16.82400  32.63700 48.56400 1.000 13.28661  ? 88  TYR A CD2 1 
ATOM   675  C  CE1 . TYR A 1 85  ? 18.14800  33.46700 46.27600 1.000 19.68342  ? 88  TYR A CE1 1 
ATOM   676  C  CE2 . TYR A 1 85  ? 16.10400  32.82900 47.38700 1.000 9.52365   ? 88  TYR A CE2 1 
ATOM   677  C  CZ  . TYR A 1 85  ? 16.77800  33.24300 46.24500 1.000 17.79997  ? 88  TYR A CZ  1 
ATOM   678  O  OH  . TYR A 1 85  ? 16.08400  33.43900 45.07600 1.000 15.36353  ? 88  TYR A OH  1 
ATOM   679  N  N   . ARG A 1 86  ? 19.43200  34.14900 53.00100 1.000 13.10608  ? 89  ARG A N   1 
ATOM   680  C  CA  . ARG A 1 86  ? 19.78200  33.92400 54.40700 1.000 15.36696  ? 89  ARG A CA  1 
ATOM   681  C  C   . ARG A 1 86  ? 19.04300  32.72800 55.00100 1.000 13.74298  ? 89  ARG A C   1 
ATOM   682  O  O   . ARG A 1 86  ? 17.82500  32.60600 54.85200 1.000 12.34386  ? 89  ARG A O   1 
ATOM   683  C  CB  . ARG A 1 86  ? 19.43400  35.14100 55.26900 1.000 14.32265  ? 89  ARG A CB  1 
ATOM   684  C  CG  . ARG A 1 86  ? 20.47100  36.21400 55.32800 1.000 24.67956  ? 89  ARG A CG  1 
ATOM   685  C  CD  . ARG A 1 86  ? 19.95600  37.37600 56.16300 1.000 16.25528  ? 89  ARG A CD  1 
ATOM   686  N  NE  . ARG A 1 86  ? 20.58500  38.61800 55.74600 1.000 22.66336  ? 89  ARG A NE  1 
ATOM   687  C  CZ  . ARG A 1 86  ? 20.11300  39.82300 56.02500 1.000 30.20874  ? 89  ARG A CZ  1 
ATOM   688  N  NH1 . ARG A 1 86  ? 19.02100  39.98300 56.75800 1.000 20.53231  ? 89  ARG A NH1 1 
ATOM   689  N  NH2 . ARG A 1 86  ? 20.74400  40.89300 55.54400 1.000 30.73826  ? 89  ARG A NH2 1 
ATOM   690  N  N   . LEU A 1 87  ? 19.77800  31.89800 55.73900 1.000 10.79752  ? 90  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 87  ? 19.17800  30.79900 56.48800 1.000 15.36525  ? 90  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 87  ? 18.32600  31.33600 57.63300 1.000 12.36766  ? 90  LEU A C   1 
ATOM   693  O  O   . LEU A 1 87  ? 18.80300  32.13500 58.44400 1.000 14.67373  ? 90  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 87  ? 20.27100  29.89100 57.04700 1.000 12.80832  ? 90  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 87  ? 19.88500  28.69800 57.93300 1.000 17.93966  ? 90  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 87  ? 19.05800  27.68400 57.16500 1.000 14.66035  ? 90  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 87  ? 21.12600  28.03300 58.53200 1.000 12.87403  ? 90  LEU A CD2 1 
ATOM   698  N  N   . ILE A 1 88  ? 17.07900  30.88000 57.72800 1.000 11.41981  ? 91  ILE A N   1 
ATOM   699  C  CA  . ILE A 1 88  ? 16.20000  31.26200 58.82500 1.000 11.04592  ? 91  ILE A CA  1 
ATOM   700  C  C   . ILE A 1 88  ? 15.89300  30.08700 59.74900 1.000 12.63231  ? 91  ILE A C   1 
ATOM   701  O  O   . ILE A 1 88  ? 15.88400  30.25000 60.97100 1.000 9.77751   ? 91  ILE A O   1 
ATOM   702  C  CB  . ILE A 1 88  ? 14.90000  31.92400 58.31000 1.000 10.78817  ? 91  ILE A CB  1 
ATOM   703  C  CG1 . ILE A 1 88  ? 13.96300  32.25000 59.48100 1.000 13.20437  ? 91  ILE A CG1 1 
ATOM   704  C  CG2 . ILE A 1 88  ? 14.20100  31.06300 57.25700 1.000 12.93830  ? 91  ILE A CG2 1 
ATOM   705  C  CD1 . ILE A 1 88  ? 12.82100  33.15700 59.08200 1.000 12.05822  ? 91  ILE A CD1 1 
ATOM   706  N  N   . GLN A 1 89  ? 15.64400  28.89900 59.20300 1.000 8.69571   ? 92  GLN A N   1 
ATOM   707  C  CA  . GLN A 1 89  ? 15.39000  27.75000 60.06600 1.000 7.81732   ? 92  GLN A CA  1 
ATOM   708  C  C   . GLN A 1 89  ? 15.66500  26.47400 59.28800 1.000 11.02682  ? 92  GLN A C   1 
ATOM   709  O  O   . GLN A 1 89  ? 15.71700  26.48000 58.06000 1.000 10.36865  ? 92  GLN A O   1 
ATOM   710  C  CB  . GLN A 1 89  ? 13.95000  27.73300 60.59800 1.000 10.49527  ? 92  GLN A CB  1 
ATOM   711  C  CG  . GLN A 1 89  ? 12.85900  27.96400 59.52400 1.000 13.73745  ? 92  GLN A CG  1 
ATOM   712  C  CD  . GLN A 1 89  ? 12.13100  26.69000 59.07800 1.000 19.94358  ? 92  GLN A CD  1 
ATOM   713  O  OE1 . GLN A 1 89  ? 12.68200  25.59000 59.09900 1.000 17.41975  ? 92  GLN A OE1 1 
ATOM   714  N  NE2 . GLN A 1 89  ? 10.88100  26.84800 58.66800 1.000 18.12768  ? 92  GLN A NE2 1 
ATOM   715  N  N   . PHE A 1 90  ? 15.82400  25.36900 60.01500 1.000 9.42146   ? 93  PHE A N   1 
ATOM   716  C  CA  . PHE A 1 90  ? 15.71300  24.06900 59.36800 1.000 9.18433   ? 93  PHE A CA  1 
ATOM   717  C  C   . PHE A 1 90  ? 14.81500  23.16800 60.20700 1.000 9.35345   ? 93  PHE A C   1 
ATOM   718  O  O   . PHE A 1 90  ? 14.56400  23.42200 61.38900 1.000 10.61578  ? 93  PHE A O   1 
ATOM   719  C  CB  . PHE A 1 90  ? 17.08200  23.39900 59.07900 1.000 7.86039   ? 93  PHE A CB  1 
ATOM   720  C  CG  . PHE A 1 90  ? 17.82700  22.91700 60.30100 1.000 10.49478  ? 93  PHE A CG  1 
ATOM   721  C  CD1 . PHE A 1 90  ? 17.45900  21.74400 60.95600 1.000 10.82365  ? 93  PHE A CD1 1 
ATOM   722  C  CD2 . PHE A 1 90  ? 18.94400  23.60900 60.75200 1.000 13.29941  ? 93  PHE A CD2 1 
ATOM   723  C  CE1 . PHE A 1 90  ? 18.15500  21.30400 62.07400 1.000 10.29984  ? 93  PHE A CE1 1 
ATOM   724  C  CE2 . PHE A 1 90  ? 19.66200  23.16300 61.85100 1.000 13.57778  ? 93  PHE A CE2 1 
ATOM   725  C  CZ  . PHE A 1 90  ? 19.26700  22.01000 62.51300 1.000 11.47815  ? 93  PHE A CZ  1 
ATOM   726  N  N   . HIS A 1 91  ? 14.30600  22.12700 59.55800 1.000 9.25469   ? 94  HIS A N   1 
ATOM   727  C  CA  . HIS A 1 91  ? 13.40700  21.16200 60.17400 1.000 10.50255  ? 94  HIS A CA  1 
ATOM   728  C  C   . HIS A 1 91  ? 13.46300  19.89000 59.33800 1.000 11.72155  ? 94  HIS A C   1 
ATOM   729  O  O   . HIS A 1 91  ? 14.11000  19.84800 58.28900 1.000 10.59551  ? 94  HIS A O   1 
ATOM   730  C  CB  . HIS A 1 91  ? 11.97500  21.69900 60.23900 1.000 7.05045   ? 94  HIS A CB  1 
ATOM   731  C  CG  . HIS A 1 91  ? 11.39800  22.00200 58.89900 1.000 10.75600  ? 94  HIS A CG  1 
ATOM   732  N  ND1 . HIS A 1 91  ? 11.45400  23.25600 58.32400 1.000 10.20244  ? 94  HIS A ND1 1 
ATOM   733  C  CD2 . HIS A 1 91  ? 10.77200  21.20600 58.00700 1.000 9.06004   ? 94  HIS A CD2 1 
ATOM   734  C  CE1 . HIS A 1 91  ? 10.88200  23.21700 57.13500 1.000 14.84413  ? 94  HIS A CE1 1 
ATOM   735  N  NE2 . HIS A 1 91  ? 10.46400  21.98300 56.92200 1.000 14.11276  ? 94  HIS A NE2 1 
ATOM   736  N  N   . PHE A 1 92  ? 12.75800  18.87600 59.82900 1.000 6.92894   ? 95  PHE A N   1 
ATOM   737  C  CA  . PHE A 1 92  ? 12.73200  17.56200 59.15600 1.000 7.31643   ? 95  PHE A CA  1 
ATOM   738  C  C   . PHE A 1 92  ? 11.31700  17.05300 58.93900 1.000 9.03975   ? 95  PHE A C   1 
ATOM   739  O  O   . PHE A 1 92  ? 10.40700  17.54500 59.59200 1.000 9.66547   ? 95  PHE A O   1 
ATOM   740  C  CB  . PHE A 1 92  ? 13.38400  16.50100 60.05300 1.000 9.21575   ? 95  PHE A CB  1 
ATOM   741  C  CG  . PHE A 1 92  ? 14.85800  16.72300 60.35600 1.000 11.52969  ? 95  PHE A CG  1 
ATOM   742  C  CD1 . PHE A 1 92  ? 15.25500  17.54200 61.40300 1.000 13.25529  ? 95  PHE A CD1 1 
ATOM   743  C  CD2 . PHE A 1 92  ? 15.84000  16.09600 59.60300 1.000 12.21576  ? 95  PHE A CD2 1 
ATOM   744  C  CE1 . PHE A 1 92  ? 16.59700  17.73400 61.68000 1.000 14.38932  ? 95  PHE A CE1 1 
ATOM   745  C  CE2 . PHE A 1 92  ? 17.17800  16.28900 59.89100 1.000 13.38962  ? 95  PHE A CE2 1 
ATOM   746  C  CZ  . PHE A 1 92  ? 17.55300  17.11300 60.92000 1.000 12.31940  ? 95  PHE A CZ  1 
ATOM   747  N  N   . HIS A 1 93  ? 11.18500  16.08200 58.04200 1.000 9.75440   ? 96  HIS A N   1 
ATOM   748  C  CA  . HIS A 1 93  ? 9.93100   15.34400 57.82300 1.000 7.20792   ? 96  HIS A CA  1 
ATOM   749  C  C   . HIS A 1 93  ? 10.32800  13.87400 57.97500 1.000 8.88020   ? 96  HIS A C   1 
ATOM   750  O  O   . HIS A 1 93  ? 11.36600  13.47500 57.46900 1.000 9.96910   ? 96  HIS A O   1 
ATOM   751  C  CB  . HIS A 1 93  ? 9.37000   15.58500 56.43100 1.000 11.71137  ? 96  HIS A CB  1 
ATOM   752  C  CG  . HIS A 1 93  ? 9.02900   17.00100 56.20300 1.000 9.36680   ? 96  HIS A CG  1 
ATOM   753  N  ND1 . HIS A 1 93  ? 7.77700   17.50400 56.46100 1.000 9.27551   ? 96  HIS A ND1 1 
ATOM   754  C  CD2 . HIS A 1 93  ? 9.76700   18.02400 55.77300 1.000 12.15747  ? 96  HIS A CD2 1 
ATOM   755  C  CE1 . HIS A 1 93  ? 7.77000   18.79100 56.16900 1.000 13.93319  ? 96  HIS A CE1 1 
ATOM   756  N  NE2 . HIS A 1 93  ? 8.96400   19.11900 55.75200 1.000 7.83134   ? 96  HIS A NE2 1 
ATOM   757  N  N   . TRP A 1 94  ? 9.52700   13.11900 58.70500 1.000 9.12670   ? 97  TRP A N   1 
ATOM   758  C  CA  . TRP A 1 94  ? 9.95700   11.72000 58.91900 1.000 9.25646   ? 97  TRP A CA  1 
ATOM   759  C  C   . TRP A 1 94  ? 8.76700   10.77300 58.94100 1.000 7.68161   ? 97  TRP A C   1 
ATOM   760  O  O   . TRP A 1 94  ? 7.63200   11.25300 58.94500 1.000 10.61346  ? 97  TRP A O   1 
ATOM   761  C  CB  . TRP A 1 94  ? 10.80700  11.60300 60.19300 1.000 9.47057   ? 97  TRP A CB  1 
ATOM   762  C  CG  . TRP A 1 94  ? 10.12600  12.02500 61.46200 1.000 10.17711  ? 97  TRP A CG  1 
ATOM   763  C  CD1 . TRP A 1 94  ? 9.44300   11.23600 62.33700 1.000 11.59940  ? 97  TRP A CD1 1 
ATOM   764  C  CD2 . TRP A 1 94  ? 10.08700  13.36000 62.00300 1.000 12.49185  ? 97  TRP A CD2 1 
ATOM   765  N  NE1 . TRP A 1 94  ? 8.97700   11.98300 63.38200 1.000 12.88432  ? 97  TRP A NE1 1 
ATOM   766  C  CE2 . TRP A 1 94  ? 9.35500   13.28700 63.20700 1.000 15.79775  ? 97  TRP A CE2 1 
ATOM   767  C  CE3 . TRP A 1 94  ? 10.59300  14.59500 61.58900 1.000 9.67988   ? 97  TRP A CE3 1 
ATOM   768  C  CZ2 . TRP A 1 94  ? 9.12100   14.40800 63.99300 1.000 9.04915   ? 97  TRP A CZ2 1 
ATOM   769  C  CZ3 . TRP A 1 94  ? 10.36000  15.70200 62.37100 1.000 11.40693  ? 97  TRP A CZ3 1 
ATOM   770  C  CH2 . TRP A 1 94  ? 9.63400   15.60500 63.55500 1.000 11.07606  ? 97  TRP A CH2 1 
ATOM   771  N  N   . GLY A 1 95  ? 9.07300   9.48100  58.96900 1.000 10.67862  ? 98  GLY A N   1 
ATOM   772  C  CA  . GLY A 1 95  ? 8.03100   8.48400  58.92500 1.000 9.67913   ? 98  GLY A CA  1 
ATOM   773  C  C   . GLY A 1 95  ? 7.82800   7.73500  60.24000 1.000 10.19590  ? 98  GLY A C   1 
ATOM   774  O  O   . GLY A 1 95  ? 8.56700   7.88700  61.21300 1.000 12.33347  ? 98  GLY A O   1 
ATOM   775  N  N   . SER A 1 96  ? 6.76400   6.92500  60.25400 1.000 10.40722  ? 99  SER A N   1 
ATOM   776  C  CA  . SER A 1 96  ? 6.55300   5.99400  61.35400 1.000 14.63114  ? 99  SER A CA  1 
ATOM   777  C  C   . SER A 1 96  ? 7.40600   4.74300  61.19900 1.000 18.11956  ? 99  SER A C   1 
ATOM   778  O  O   . SER A 1 96  ? 7.56300   3.98600  62.16400 1.000 17.27016  ? 99  SER A O   1 
ATOM   779  C  CB  . SER A 1 96  ? 5.07400   5.60900  61.43500 1.000 17.33360  ? 99  SER A CB  1 
ATOM   780  O  OG  . SER A 1 96  ? 4.62800   5.12300  60.17700 1.000 16.18323  ? 99  SER A OG  1 
ATOM   781  N  N   . LEU A 1 97  ? 7.94000   4.52200  60.00000 1.000 13.40629  ? 100 LEU A N   1 
ATOM   782  C  CA  . LEU A 1 97  ? 8.75500   3.37100  59.64700 1.000 17.31959  ? 100 LEU A CA  1 
ATOM   783  C  C   . LEU A 1 97  ? 9.91600   3.84500  58.78100 1.000 17.51538  ? 100 LEU A C   1 
ATOM   784  O  O   . LEU A 1 97  ? 9.81800   4.85800  58.08300 1.000 17.79569  ? 100 LEU A O   1 
ATOM   785  C  CB  . LEU A 1 97  ? 7.94600   2.32100  58.87800 1.000 19.13557  ? 100 LEU A CB  1 
ATOM   786  C  CG  . LEU A 1 97  ? 6.69200   1.77000  59.55200 1.000 24.12303  ? 100 LEU A CG  1 
ATOM   787  C  CD1 . LEU A 1 97  ? 5.67700   1.34900  58.50600 1.000 29.89781  ? 100 LEU A CD1 1 
ATOM   788  C  CD2 . LEU A 1 97  ? 7.08200   0.59800  60.43100 1.000 29.83856  ? 100 LEU A CD2 1 
ATOM   789  N  N   . ASP A 1 98  ? 11.00700  3.07100  58.79700 1.000 18.19014  ? 101 ASP A N   1 
ATOM   790  C  CA  . ASP A 1 98  ? 12.21300  3.46400  58.07000 1.000 15.46180  ? 101 ASP A CA  1 
ATOM   791  C  C   . ASP A 1 98  ? 11.99200  3.54400  56.56100 1.000 17.96879  ? 101 ASP A C   1 
ATOM   792  O  O   . ASP A 1 98  ? 12.74300  4.24800  55.87600 1.000 20.46727  ? 101 ASP A O   1 
ATOM   793  C  CB  . ASP A 1 98  ? 13.35800  2.49000  58.36100 1.000 21.78667  ? 101 ASP A CB  1 
ATOM   794  C  CG  . ASP A 1 98  ? 13.88000  2.58400  59.79300 1.000 25.69904  ? 101 ASP A CG  1 
ATOM   795  O  OD1 . ASP A 1 98  ? 13.45300  3.47500  60.56400 1.000 23.83325  ? 101 ASP A OD1 1 
ATOM   796  O  OD2 . ASP A 1 98  ? 14.74200  1.75400  60.13500 1.000 29.62948  ? 101 ASP A OD2 1 
ATOM   797  N  N   . GLY A 1 99  ? 10.98300  2.85100  56.02900 1.000 17.34546  ? 102 GLY A N   1 
ATOM   798  C  CA  . GLY A 1 99  ? 10.72500  2.84300  54.60200 1.000 19.17050  ? 102 GLY A CA  1 
ATOM   799  C  C   . GLY A 1 99  ? 9.94200   4.01300  54.05500 1.000 21.21931  ? 102 GLY A C   1 
ATOM   800  O  O   . GLY A 1 99  ? 9.63900   4.03400  52.86100 1.000 17.69036  ? 102 GLY A O   1 
ATOM   801  N  N   . GLN A 1 100 ? 9.60500   5.00000  54.88500 1.000 14.50542  ? 103 GLN A N   1 
ATOM   802  C  CA  . GLN A 1 100 ? 8.91200   6.17900  54.39600 1.000 12.46822  ? 103 GLN A CA  1 
ATOM   803  C  C   . GLN A 1 100 ? 9.29300   7.36800  55.25900 1.000 13.42169  ? 103 GLN A C   1 
ATOM   804  O  O   . GLN A 1 100 ? 9.85500   7.21700  56.34300 1.000 10.49913  ? 103 GLN A O   1 
ATOM   805  C  CB  . GLN A 1 100 ? 7.39900   5.97100  54.40500 1.000 13.81556  ? 103 GLN A CB  1 
ATOM   806  C  CG  . GLN A 1 100 ? 6.82000   5.81900  55.79900 1.000 13.49986  ? 103 GLN A CG  1 
ATOM   807  C  CD  . GLN A 1 100 ? 5.43400   5.21600  55.77700 1.000 25.82429  ? 103 GLN A CD  1 
ATOM   808  O  OE1 . GLN A 1 100 ? 5.19500   4.23900  55.07600 1.000 25.93964  ? 103 GLN A OE1 1 
ATOM   809  N  NE2 . GLN A 1 100 ? 4.51300   5.79800  56.53300 1.000 15.47671  ? 103 GLN A NE2 1 
ATOM   810  N  N   . GLY A 1 101 ? 8.97400   8.56500  54.77400 1.000 12.37884  ? 104 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 101 ? 9.23500   9.74200  55.58100 1.000 10.37893  ? 104 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 101 ? 9.71500   10.94000 54.79000 1.000 11.01350  ? 104 GLY A C   1 
ATOM   813  O  O   . GLY A 1 101 ? 9.46500   12.08900 55.18300 1.000 10.32301  ? 104 GLY A O   1 
ATOM   814  N  N   . SER A 1 102 ? 10.41600  10.70500 53.68200 1.000 8.76948   ? 105 SER A N   1 
ATOM   815  C  CA  . SER A 1 102 ? 10.83300  11.83200 52.86200 1.000 8.68083   ? 105 SER A CA  1 
ATOM   816  C  C   . SER A 1 102 ? 9.64300   12.37400 52.07600 1.000 10.90308  ? 105 SER A C   1 
ATOM   817  O  O   . SER A 1 102 ? 8.65200   11.67600 51.82200 1.000 12.44458  ? 105 SER A O   1 
ATOM   818  C  CB  . SER A 1 102 ? 11.97400  11.45500 51.90800 1.000 7.89446   ? 105 SER A CB  1 
ATOM   819  O  OG  . SER A 1 102 ? 11.55500  10.51100 50.93200 1.000 10.40171  ? 105 SER A OG  1 
ATOM   820  N  N   . GLU A 1 103 ? 9.73400   13.64900 51.72800 1.000 9.34690   ? 106 GLU A N   1 
ATOM   821  C  CA  . GLU A 1 103 ? 8.72500   14.27700 50.88700 1.000 9.51798   ? 106 GLU A CA  1 
ATOM   822  C  C   . GLU A 1 103 ? 9.04400   14.06800 49.41400 1.000 11.27520  ? 106 GLU A C   1 
ATOM   823  O  O   . GLU A 1 103 ? 8.25300   13.46300 48.68500 1.000 11.34562  ? 106 GLU A O   1 
ATOM   824  C  CB  . GLU A 1 103 ? 8.62100   15.75800 51.24700 1.000 9.57311   ? 106 GLU A CB  1 
ATOM   825  C  CG  . GLU A 1 103 ? 8.14800   15.90200 52.69000 1.000 10.10032  ? 106 GLU A CG  1 
ATOM   826  C  CD  . GLU A 1 103 ? 7.49200   17.23500 52.95200 1.000 12.12832  ? 106 GLU A CD  1 
ATOM   827  O  OE1 . GLU A 1 103 ? 8.10200   18.27800 52.66100 1.000 10.52672  ? 106 GLU A OE1 1 
ATOM   828  O  OE2 . GLU A 1 103 ? 6.36000   17.23500 53.45400 1.000 15.25440  ? 106 GLU A OE2 1 
ATOM   829  N  N   . HIS A 1 104 ? 10.20600  14.53600 48.96900 1.000 10.85826  ? 107 HIS A N   1 
ATOM   830  C  CA  . HIS A 1 104 ? 10.63500  14.17200 47.63400 1.000 8.24392   ? 107 HIS A CA  1 
ATOM   831  C  C   . HIS A 1 104 ? 10.99800  12.69600 47.59500 1.000 13.19651  ? 107 HIS A C   1 
ATOM   832  O  O   . HIS A 1 104 ? 11.32700  12.08100 48.61100 1.000 11.79508  ? 107 HIS A O   1 
ATOM   833  C  CB  . HIS A 1 104 ? 11.82700  15.01000 47.17400 1.000 9.87161   ? 107 HIS A CB  1 
ATOM   834  C  CG  . HIS A 1 104 ? 11.50800  16.45900 47.01700 1.000 10.30244  ? 107 HIS A CG  1 
ATOM   835  N  ND1 . HIS A 1 104 ? 11.59500  17.35200 48.06100 1.000 11.09473  ? 107 HIS A ND1 1 
ATOM   836  C  CD2 . HIS A 1 104 ? 11.07200  17.16600 45.94700 1.000 11.85703  ? 107 HIS A CD2 1 
ATOM   837  C  CE1 . HIS A 1 104 ? 11.23200  18.55300 47.63800 1.000 11.21597  ? 107 HIS A CE1 1 
ATOM   838  N  NE2 . HIS A 1 104 ? 10.92000  18.46900 46.35600 1.000 9.87896   ? 107 HIS A NE2 1 
ATOM   839  N  N   . THR A 1 105 ? 10.90600  12.12900 46.39800 1.000 12.19727  ? 108 THR A N   1 
ATOM   840  C  CA  . THR A 1 105 ? 11.31400  10.76000 46.14100 1.000 11.80225  ? 108 THR A CA  1 
ATOM   841  C  C   . THR A 1 105 ? 12.24800  10.76900 44.93500 1.000 12.41651  ? 108 THR A C   1 
ATOM   842  O  O   . THR A 1 105 ? 12.27800  11.72600 44.15900 1.000 12.68740  ? 108 THR A O   1 
ATOM   843  C  CB  . THR A 1 105 ? 10.08800  9.84000  45.91500 1.000 9.35116   ? 108 THR A CB  1 
ATOM   844  O  OG1 . THR A 1 105 ? 9.26900   10.35000 44.85000 1.000 12.82581  ? 108 THR A OG1 1 
ATOM   845  C  CG2 . THR A 1 105 ? 9.24700   9.76500  47.18200 1.000 8.66525   ? 108 THR A CG2 1 
ATOM   846  N  N   . VAL A 1 106 ? 13.05100  9.72300  44.79700 1.000 9.87508   ? 109 VAL A N   1 
ATOM   847  C  CA  . VAL A 1 106 ? 13.96200  9.60200  43.65500 1.000 13.57714  ? 109 VAL A CA  1 
ATOM   848  C  C   . VAL A 1 106 ? 13.63100  8.29900  42.95200 1.000 14.21193  ? 109 VAL A C   1 
ATOM   849  O  O   . VAL A 1 106 ? 13.79900  7.22100  43.53300 1.000 15.70993  ? 109 VAL A O   1 
ATOM   850  C  CB  . VAL A 1 106 ? 15.43600  9.64100  44.07000 1.000 15.37524  ? 109 VAL A CB  1 
ATOM   851  C  CG1 . VAL A 1 106 ? 16.33100  9.64100  42.83100 1.000 12.54207  ? 109 VAL A CG1 1 
ATOM   852  C  CG2 . VAL A 1 106 ? 15.72200  10.86100 44.94100 1.000 15.86481  ? 109 VAL A CG2 1 
ATOM   853  N  N   . ASP A 1 107 ? 13.16900  8.38600  41.70600 1.000 14.04526  ? 110 ASP A N   1 
ATOM   854  C  CA  . ASP A 1 107 ? 12.67400  7.21400  40.98500 1.000 13.73872  ? 110 ASP A CA  1 
ATOM   855  C  C   . ASP A 1 107 ? 11.73200  6.39900  41.87200 1.000 15.96726  ? 110 ASP A C   1 
ATOM   856  O  O   . ASP A 1 107 ? 11.84600  5.17900  41.99400 1.000 15.55979  ? 110 ASP A O   1 
ATOM   857  C  CB  . ASP A 1 107 ? 13.83500  6.35900  40.46800 1.000 15.72642  ? 110 ASP A CB  1 
ATOM   858  C  CG  . ASP A 1 107 ? 14.67600  7.09400  39.43100 1.000 13.73383  ? 110 ASP A CG  1 
ATOM   859  O  OD1 . ASP A 1 107 ? 14.12700  7.98100  38.74800 1.000 14.83152  ? 110 ASP A OD1 1 
ATOM   860  O  OD2 . ASP A 1 107 ? 15.87500  6.79500  39.31700 1.000 21.71161  ? 110 ASP A OD2 1 
ATOM   861  N  N   . LYS A 1 108 ? 10.81700  7.11300  42.53000 1.000 14.50659  ? 111 LYS A N   1 
ATOM   862  C  CA  . LYS A 1 108 ? 9.77800   6.60600  43.42600 1.000 16.45183  ? 111 LYS A CA  1 
ATOM   863  C  C   . LYS A 1 108 ? 10.32600  6.05500  44.74700 1.000 11.70265  ? 111 LYS A C   1 
ATOM   864  O  O   . LYS A 1 108 ? 9.53500   5.57900  45.57200 1.000 19.50456  ? 111 LYS A O   1 
ATOM   865  C  CB  . LYS A 1 108 ? 8.90200   5.53100  42.75300 1.000 17.58187  ? 111 LYS A CB  1 
ATOM   866  C  CG  . LYS A 1 108 ? 8.26900   5.96100  41.43000 1.000 23.07461  ? 111 LYS A CG  1 
ATOM   867  C  CD  . LYS A 1 108 ? 7.10100   6.89800  41.65000 1.000 23.33541  ? 111 LYS A CD  1 
ATOM   868  C  CE  . LYS A 1 108 ? 6.39500   7.23600  40.34300 1.000 40.40562  ? 111 LYS A CE  1 
ATOM   869  N  NZ  . LYS A 1 108 ? 4.92100   7.36300  40.50400 1.000 43.71187  ? 111 LYS A NZ  1 
ATOM   870  N  N   . LYS A 1 109 ? 11.63500  6.12600  44.99000 1.000 13.10127  ? 112 LYS A N   1 
ATOM   871  C  CA  . LYS A 1 109 ? 12.21400  5.63500  46.23400 1.000 12.46790  ? 112 LYS A CA  1 
ATOM   872  C  C   . LYS A 1 109 ? 11.99300  6.64400  47.35700 1.000 15.97728  ? 112 LYS A C   1 
ATOM   873  O  O   . LYS A 1 109 ? 12.30300  7.82700  47.20500 1.000 10.50453  ? 112 LYS A O   1 
ATOM   874  C  CB  . LYS A 1 109 ? 13.70500  5.35800  46.05700 1.000 17.76708  ? 112 LYS A CB  1 
ATOM   875  C  CG  . LYS A 1 109 ? 14.45800  4.98200  47.31900 1.000 22.42123  ? 112 LYS A CG  1 
ATOM   876  C  CD  . LYS A 1 109 ? 15.97000  5.13700  47.08900 1.000 26.30994  ? 112 LYS A CD  1 
ATOM   877  C  CE  . LYS A 1 109 ? 16.79700  4.57100  48.23700 1.000 39.35238  ? 112 LYS A CE  1 
ATOM   878  N  NZ  . LYS A 1 109 ? 15.95400  4.18500  49.39500 1.000 38.74168  ? 112 LYS A NZ  1 
ATOM   879  N  N   . LYS A 1 110 ? 11.45300  6.17300  48.47800 1.000 15.83322  ? 113 LYS A N   1 
ATOM   880  C  CA  . LYS A 1 110 ? 11.25100  6.99200  49.66600 1.000 18.19922  ? 113 LYS A CA  1 
ATOM   881  C  C   . LYS A 1 110 ? 12.42600  6.80700  50.61800 1.000 16.38465  ? 113 LYS A C   1 
ATOM   882  O  O   . LYS A 1 110 ? 12.93100  5.69400  50.78300 1.000 17.33051  ? 113 LYS A O   1 
ATOM   883  C  CB  . LYS A 1 110 ? 9.94800   6.61400  50.38800 1.000 16.20388  ? 113 LYS A CB  1 
ATOM   884  C  CG  . LYS A 1 110 ? 8.66800   6.99600  49.66500 1.000 16.31430  ? 113 LYS A CG  1 
ATOM   885  C  CD  . LYS A 1 110 ? 7.45700   6.47700  50.43400 1.000 16.69301  ? 113 LYS A CD  1 
ATOM   886  C  CE  . LYS A 1 110 ? 6.15100   6.90900  49.78000 1.000 30.26903  ? 113 LYS A CE  1 
ATOM   887  N  NZ  . LYS A 1 110 ? 5.85800   6.11100  48.55600 1.000 34.72646  ? 113 LYS A NZ  1 
ATOM   888  N  N   . TYR A 1 111 ? 12.85500  7.89800  51.24600 1.000 12.13689  ? 114 TYR A N   1 
ATOM   889  C  CA  . TYR A 1 111 ? 13.87100  7.86200  52.28700 1.000 10.89180  ? 114 TYR A CA  1 
ATOM   890  C  C   . TYR A 1 111 ? 13.22400  7.96000  53.66900 1.000 13.08390  ? 114 TYR A C   1 
ATOM   891  O  O   . TYR A 1 111 ? 12.04900  8.30200  53.81200 1.000 13.10691  ? 114 TYR A O   1 
ATOM   892  C  CB  . TYR A 1 111 ? 14.88500  8.98900  52.07500 1.000 9.58145   ? 114 TYR A CB  1 
ATOM   893  C  CG  . TYR A 1 111 ? 15.82600  8.70100  50.93300 1.000 10.90110  ? 114 TYR A CG  1 
ATOM   894  C  CD1 . TYR A 1 111 ? 17.00800  8.00300  51.14800 1.000 18.62891  ? 114 TYR A CD1 1 
ATOM   895  C  CD2 . TYR A 1 111 ? 15.52400  9.10500  49.63100 1.000 12.89334  ? 114 TYR A CD2 1 
ATOM   896  C  CE1 . TYR A 1 111 ? 17.88300  7.72500  50.10000 1.000 21.46680  ? 114 TYR A CE1 1 
ATOM   897  C  CE2 . TYR A 1 111 ? 16.39400  8.82500  48.56400 1.000 12.67330  ? 114 TYR A CE2 1 
ATOM   898  C  CZ  . TYR A 1 111 ? 17.57400  8.13500  48.81600 1.000 23.46241  ? 114 TYR A CZ  1 
ATOM   899  O  OH  . TYR A 1 111 ? 18.45200  7.84600  47.79200 1.000 30.27639  ? 114 TYR A OH  1 
ATOM   900  N  N   . ALA A 1 112 ? 14.01200  7.64300  54.70400 1.000 11.07715  ? 115 ALA A N   1 
ATOM   901  C  CA  . ALA A 1 112 ? 13.45500  7.60900  56.05100 1.000 14.43749  ? 115 ALA A CA  1 
ATOM   902  C  C   . ALA A 1 112 ? 13.08100  8.99900  56.55800 1.000 9.83938   ? 115 ALA A C   1 
ATOM   903  O  O   . ALA A 1 112 ? 12.20400  9.11900  57.42100 1.000 12.74719  ? 115 ALA A O   1 
ATOM   904  C  CB  . ALA A 1 112 ? 14.44100  6.94000  57.01000 1.000 15.46595  ? 115 ALA A CB  1 
ATOM   905  N  N   . ALA A 1 113 ? 13.72700  10.04400 56.06000 1.000 6.98676   ? 116 ALA A N   1 
ATOM   906  C  CA  . ALA A 1 113 ? 13.40600  11.40400 56.47300 1.000 8.50309   ? 116 ALA A CA  1 
ATOM   907  C  C   . ALA A 1 113 ? 13.99600  12.36400 55.45100 1.000 12.08788  ? 116 ALA A C   1 
ATOM   908  O  O   . ALA A 1 113 ? 14.75800  11.96800 54.56600 1.000 10.79376  ? 116 ALA A O   1 
ATOM   909  C  CB  . ALA A 1 113 ? 13.93700  11.70600 57.88100 1.000 10.43203  ? 116 ALA A CB  1 
ATOM   910  N  N   . GLU A 1 114 ? 13.63800  13.63900 55.59200 1.000 11.25273  ? 117 GLU A N   1 
ATOM   911  C  CA  . GLU A 1 114 ? 14.12000  14.68300 54.69700 1.000 8.24097   ? 117 GLU A CA  1 
ATOM   912  C  C   . GLU A 1 114 ? 14.34600  15.95500 55.49100 1.000 10.86382  ? 117 GLU A C   1 
ATOM   913  O  O   . GLU A 1 114 ? 13.44500  16.41800 56.19900 1.000 11.00083  ? 117 GLU A O   1 
ATOM   914  C  CB  . GLU A 1 114 ? 13.14000  14.95200 53.55400 1.000 9.78704   ? 117 GLU A CB  1 
ATOM   915  C  CG  . GLU A 1 114 ? 13.65200  15.96200 52.50800 1.000 12.02135  ? 117 GLU A CG  1 
ATOM   916  C  CD  . GLU A 1 114 ? 12.75300  15.99600 51.27000 1.000 9.81642   ? 117 GLU A CD  1 
ATOM   917  O  OE1 . GLU A 1 114 ? 12.13800  14.95800 50.93500 1.000 11.36511  ? 117 GLU A OE1 1 
ATOM   918  O  OE2 . GLU A 1 114 ? 12.63700  17.06800 50.65100 1.000 12.63892  ? 117 GLU A OE2 1 
ATOM   919  N  N   . LEU A 1 115 ? 15.54400  16.51000 55.34900 1.000 12.00186  ? 118 LEU A N   1 
ATOM   920  C  CA  . LEU A 1 115 ? 15.95400  17.73300 56.02200 1.000 7.88492   ? 118 LEU A CA  1 
ATOM   921  C  C   . LEU A 1 115 ? 15.73500  18.91200 55.08600 1.000 6.58943   ? 118 LEU A C   1 
ATOM   922  O  O   . LEU A 1 115 ? 16.11600  18.85700 53.91200 1.000 7.72788   ? 118 LEU A O   1 
ATOM   923  C  CB  . LEU A 1 115 ? 17.42200  17.64400 56.43700 1.000 7.31891   ? 118 LEU A CB  1 
ATOM   924  C  CG  . LEU A 1 115 ? 18.14400  18.91700 56.86000 1.000 8.81847   ? 118 LEU A CG  1 
ATOM   925  C  CD1 . LEU A 1 115 ? 17.53300  19.51100 58.12900 1.000 13.40556  ? 118 LEU A CD1 1 
ATOM   926  C  CD2 . LEU A 1 115 ? 19.62700  18.58700 57.07600 1.000 13.33126  ? 118 LEU A CD2 1 
ATOM   927  N  N   . HIS A 1 116 ? 15.11000  19.95900 55.62900 1.000 7.32202   ? 119 HIS A N   1 
ATOM   928  C  CA  . HIS A 1 116 ? 14.84700  21.19600 54.85700 1.000 8.02300   ? 119 HIS A CA  1 
ATOM   929  C  C   . HIS A 1 116 ? 15.52200  22.40700 55.52500 1.000 11.55641  ? 119 HIS A C   1 
ATOM   930  O  O   . HIS A 1 116 ? 15.15200  22.73000 56.64800 1.000 9.23804   ? 119 HIS A O   1 
ATOM   931  C  CB  . HIS A 1 116 ? 13.33600  21.43200 54.67700 1.000 5.09828   ? 119 HIS A CB  1 
ATOM   932  C  CG  . HIS A 1 116 ? 12.63200  20.46900 53.78400 1.000 9.14626   ? 119 HIS A CG  1 
ATOM   933  N  ND1 . HIS A 1 116 ? 11.26700  20.28400 53.71800 1.000 10.94998  ? 119 HIS A ND1 1 
ATOM   934  C  CD2 . HIS A 1 116 ? 13.15800  19.64700 52.87700 1.000 10.23218  ? 119 HIS A CD2 1 
ATOM   935  C  CE1 . HIS A 1 116 ? 11.00100  19.36100 52.81700 1.000 11.57021  ? 119 HIS A CE1 1 
ATOM   936  N  NE2 . HIS A 1 116 ? 12.13100  18.96900 52.28500 1.000 8.94281   ? 119 HIS A NE2 1 
ATOM   937  N  N   . LEU A 1 117 ? 16.51500  22.98700 54.85200 1.000 8.35777   ? 120 LEU A N   1 
ATOM   938  C  CA  . LEU A 1 117 ? 17.15000  24.22600 55.29500 1.000 9.82024   ? 120 LEU A CA  1 
ATOM   939  C  C   . LEU A 1 117 ? 16.53200  25.36000 54.49300 1.000 10.28368  ? 120 LEU A C   1 
ATOM   940  O  O   . LEU A 1 117 ? 16.69400  25.42300 53.27300 1.000 11.59909  ? 120 LEU A O   1 
ATOM   941  C  CB  . LEU A 1 117 ? 18.66200  24.18400 55.10500 1.000 6.45523   ? 120 LEU A CB  1 
ATOM   942  C  CG  . LEU A 1 117 ? 19.33400  23.11500 55.97700 1.000 13.62112  ? 120 LEU A CG  1 
ATOM   943  C  CD1 . LEU A 1 117 ? 20.06800  22.10200 55.12800 1.000 11.21275  ? 120 LEU A CD1 1 
ATOM   944  C  CD2 . LEU A 1 117 ? 20.28500  23.74800 56.97000 1.000 16.77782  ? 120 LEU A CD2 1 
ATOM   945  N  N   . VAL A 1 118 ? 15.82500  26.24700 55.18000 1.000 8.36161   ? 121 VAL A N   1 
ATOM   946  C  CA  . VAL A 1 118 ? 14.99200  27.25400 54.53600 1.000 8.92547   ? 121 VAL A CA  1 
ATOM   947  C  C   . VAL A 1 118 ? 15.75000  28.57300 54.51800 1.000 10.72650  ? 121 VAL A C   1 
ATOM   948  O  O   . VAL A 1 118 ? 16.20600  29.04700 55.56800 1.000 10.23180  ? 121 VAL A O   1 
ATOM   949  C  CB  . VAL A 1 118 ? 13.64300  27.39700 55.26700 1.000 9.48216   ? 121 VAL A CB  1 
ATOM   950  C  CG1 . VAL A 1 118 ? 12.78000  28.45400 54.61300 1.000 9.26580   ? 121 VAL A CG1 1 
ATOM   951  C  CG2 . VAL A 1 118 ? 12.91500  26.04300 55.35000 1.000 12.15192  ? 121 VAL A CG2 1 
ATOM   952  N  N   . HIS A 1 119 ? 15.86000  29.18200 53.33500 1.000 7.79559   ? 122 HIS A N   1 
ATOM   953  C  CA  . HIS A 1 119 ? 16.54300  30.46400 53.17900 1.000 8.54036   ? 122 HIS A CA  1 
ATOM   954  C  C   . HIS A 1 119 ? 15.63400  31.44700 52.45000 1.000 14.19524  ? 122 HIS A C   1 
ATOM   955  O  O   . HIS A 1 119 ? 14.82500  31.04800 51.60900 1.000 11.80445  ? 122 HIS A O   1 
ATOM   956  C  CB  . HIS A 1 119 ? 17.85900  30.34700 52.38600 1.000 9.04552   ? 122 HIS A CB  1 
ATOM   957  C  CG  . HIS A 1 119 ? 18.75400  29.21000 52.79800 1.000 8.30049   ? 122 HIS A CG  1 
ATOM   958  N  ND1 . HIS A 1 119 ? 18.45600  27.88500 52.54600 1.000 12.33858  ? 122 HIS A ND1 1 
ATOM   959  C  CD2 . HIS A 1 119 ? 19.98000  29.21300 53.37800 1.000 10.23361  ? 122 HIS A CD2 1 
ATOM   960  C  CE1 . HIS A 1 119 ? 19.44000  27.12100 52.99200 1.000 12.32800  ? 122 HIS A CE1 1 
ATOM   961  N  NE2 . HIS A 1 119 ? 20.38300  27.90500 53.49100 1.000 9.86876   ? 122 HIS A NE2 1 
ATOM   962  N  N   . TRP A 1 120 ? 15.80100  32.73400 52.75200 1.000 11.47938  ? 123 TRP A N   1 
ATOM   963  C  CA  . TRP A 1 120 ? 14.98200  33.77700 52.08700 1.000 12.41792  ? 123 TRP A CA  1 
ATOM   964  C  C   . TRP A 1 120 ? 15.83900  34.82900 51.36400 1.000 13.12790  ? 123 TRP A C   1 
ATOM   965  O  O   . TRP A 1 120 ? 16.92600  35.14100 51.84300 1.000 12.72542  ? 123 TRP A O   1 
ATOM   966  C  CB  . TRP A 1 120 ? 13.98300  34.41800 53.06200 1.000 14.15282  ? 123 TRP A CB  1 
ATOM   967  C  CG  . TRP A 1 120 ? 14.57300  35.09200 54.26600 1.000 13.11950  ? 123 TRP A CG  1 
ATOM   968  C  CD1 . TRP A 1 120 ? 14.82500  34.53500 55.48400 1.000 14.59138  ? 123 TRP A CD1 1 
ATOM   969  C  CD2 . TRP A 1 120 ? 14.95100  36.47900 54.37000 1.000 13.11291  ? 123 TRP A CD2 1 
ATOM   970  N  NE1 . TRP A 1 120 ? 15.33900  35.47200 56.33500 1.000 9.30293   ? 123 TRP A NE1 1 
ATOM   971  C  CE2 . TRP A 1 120 ? 15.43100  36.67100 55.68200 1.000 15.16156  ? 123 TRP A CE2 1 
ATOM   972  C  CE3 . TRP A 1 120 ? 14.93600  37.56300 53.48800 1.000 16.37338  ? 123 TRP A CE3 1 
ATOM   973  C  CZ2 . TRP A 1 120 ? 15.88900  37.90800 56.12500 1.000 14.45217  ? 123 TRP A CZ2 1 
ATOM   974  C  CZ3 . TRP A 1 120 ? 15.39300  38.78300 53.93000 1.000 17.30259  ? 123 TRP A CZ3 1 
ATOM   975  C  CH2 . TRP A 1 120 ? 15.86300  38.95000 55.23000 1.000 17.28324  ? 123 TRP A CH2 1 
ATOM   976  N  N   . ASN A 1 121 ? 15.32200  35.34700 50.25600 1.000 10.88407  ? 124 ASN A N   1 
ATOM   977  C  CA  . ASN A 1 121 ? 16.04100  36.30600 49.37900 1.000 11.81415  ? 124 ASN A CA  1 
ATOM   978  C  C   . ASN A 1 121 ? 16.15800  37.67500 50.05300 1.000 11.16830  ? 124 ASN A C   1 
ATOM   979  O  O   . ASN A 1 121 ? 15.14200  38.31100 50.26500 1.000 12.75712  ? 124 ASN A O   1 
ATOM   980  C  CB  . ASN A 1 121 ? 15.34000  36.37700 48.02800 1.000 13.11847  ? 124 ASN A CB  1 
ATOM   981  C  CG  . ASN A 1 121 ? 16.16100  37.01100 46.93600 1.000 16.36071  ? 124 ASN A CG  1 
ATOM   982  O  OD1 . ASN A 1 121 ? 17.00700  37.86600 47.20100 1.000 15.15481  ? 124 ASN A OD1 1 
ATOM   983  N  ND2 . ASN A 1 121 ? 15.91200  36.60400 45.70200 1.000 25.41096  ? 124 ASN A ND2 1 
ATOM   984  N  N   . THR A 1 122 ? 17.39800  38.11900 50.27200 1.000 16.83542  ? 125 THR A N   1 
ATOM   985  C  CA  . THR A 1 122 ? 17.65000  39.37300 50.99600 1.000 17.51832  ? 125 THR A CA  1 
ATOM   986  C  C   . THR A 1 122 ? 17.02300  40.57100 50.28800 1.000 16.70989  ? 125 THR A C   1 
ATOM   987  O  O   . THR A 1 122 ? 16.72600  41.54200 50.97400 1.000 17.83506  ? 125 THR A O   1 
ATOM   988  C  CB  . THR A 1 122 ? 19.15900  39.53200 51.21200 1.000 15.07556  ? 125 THR A CB  1 
ATOM   989  O  OG1 . THR A 1 122 ? 19.81600  39.47300 49.95600 1.000 20.96402  ? 125 THR A OG1 1 
ATOM   990  C  CG2 . THR A 1 122 ? 19.68500  38.44900 52.13800 1.000 25.94901  ? 125 THR A CG2 1 
ATOM   991  N  N   . LYS A 1 123 ? 16.83600  40.49200 48.97100 1.000 13.28001  ? 126 LYS A N   1 
ATOM   992  C  CA  . LYS A 1 123 ? 16.28400  41.64900 48.23000 1.000 17.81223  ? 126 LYS A CA  1 
ATOM   993  C  C   . LYS A 1 123 ? 14.89800  42.02100 48.79400 1.000 21.55290  ? 126 LYS A C   1 
ATOM   994  O  O   . LYS A 1 123 ? 14.52300  43.19100 48.65600 1.000 21.00678  ? 126 LYS A O   1 
ATOM   995  C  CB  . LYS A 1 123 ? 16.24400  41.33200 46.73700 1.000 20.80949  ? 126 LYS A CB  1 
ATOM   996  C  CG  . LYS A 1 123 ? 15.03400  40.67000 46.13500 1.000 35.49428  ? 126 LYS A CG  1 
ATOM   997  C  CD  . LYS A 1 123 ? 14.96700  41.04600 44.66000 1.000 36.35800  ? 126 LYS A CD  1 
ATOM   998  C  CE  . LYS A 1 123 ? 14.77000  39.86300 43.78200 1.000 37.60816  ? 126 LYS A CE  1 
ATOM   999  N  NZ  . LYS A 1 123 ? 14.72600  40.21200 42.36300 1.000 50.38379  ? 126 LYS A NZ  1 
ATOM   1000 N  N   . TYR A 1 124 ? 14.18500  41.07400 49.40600 1.000 13.19072  ? 127 TYR A N   1 
ATOM   1001 C  CA  . TYR A 1 124 ? 12.79700  41.32300 49.88900 1.000 11.17058  ? 127 TYR A CA  1 
ATOM   1002 C  C   . TYR A 1 124 ? 12.76500  41.79700 51.35600 1.000 19.02389  ? 127 TYR A C   1 
ATOM   1003 O  O   . TYR A 1 124 ? 11.66800  42.00700 51.85800 1.000 17.88738  ? 127 TYR A O   1 
ATOM   1004 C  CB  . TYR A 1 124 ? 11.93100  40.10100 49.57800 1.000 17.57047  ? 127 TYR A CB  1 
ATOM   1005 C  CG  . TYR A 1 124 ? 11.86000  39.79300 48.09200 1.000 23.65415  ? 127 TYR A CG  1 
ATOM   1006 C  CD1 . TYR A 1 124 ? 11.40400  40.74000 47.18500 1.000 25.08222  ? 127 TYR A CD1 1 
ATOM   1007 C  CD2 . TYR A 1 124 ? 12.26400  38.56100 47.59700 1.000 18.47666  ? 127 TYR A CD2 1 
ATOM   1008 C  CE1 . TYR A 1 124 ? 11.34600  40.46800 45.82900 1.000 17.38353  ? 127 TYR A CE1 1 
ATOM   1009 C  CE2 . TYR A 1 124 ? 12.20900  38.27500 46.24700 1.000 15.96374  ? 127 TYR A CE2 1 
ATOM   1010 C  CZ  . TYR A 1 124 ? 11.74800  39.23100 45.36100 1.000 20.77936  ? 127 TYR A CZ  1 
ATOM   1011 O  OH  . TYR A 1 124 ? 11.69700  38.94800 44.03200 1.000 24.35055  ? 127 TYR A OH  1 
ATOM   1012 N  N   . GLY A 1 125 ? 13.91400  41.91800 52.01600 1.000 17.82803  ? 128 GLY A N   1 
ATOM   1013 C  CA  . GLY A 1 125 ? 13.94500  42.54200 53.35100 1.000 16.05474  ? 128 GLY A CA  1 
ATOM   1014 C  C   . GLY A 1 125 ? 13.55400  41.66800 54.52200 1.000 18.66695  ? 128 GLY A C   1 
ATOM   1015 O  O   . GLY A 1 125 ? 14.21700  41.77400 55.55200 1.000 19.16828  ? 128 GLY A O   1 
ATOM   1016 N  N   . ASP A 1 126 ? 12.47800  40.89200 54.41100 1.000 18.02862  ? 129 ASP A N   1 
ATOM   1017 C  CA  . ASP A 1 126 ? 12.16300  39.98700 55.50700 1.000 15.84860  ? 129 ASP A CA  1 
ATOM   1018 C  C   . ASP A 1 126 ? 11.47100  38.75300 54.94100 1.000 19.57207  ? 129 ASP A C   1 
ATOM   1019 O  O   . ASP A 1 126 ? 11.06500  38.71600 53.77600 1.000 15.17438  ? 129 ASP A O   1 
ATOM   1020 C  CB  . ASP A 1 126 ? 11.34000  40.68100 56.62000 1.000 15.35352  ? 129 ASP A CB  1 
ATOM   1021 C  CG  . ASP A 1 126 ? 9.95200   41.11400 56.17900 1.000 25.87707  ? 129 ASP A CG  1 
ATOM   1022 O  OD1 . ASP A 1 126 ? 9.13500   40.26000 55.78600 1.000 29.26636  ? 129 ASP A OD1 1 
ATOM   1023 O  OD2 . ASP A 1 126 ? 9.65000   42.32200 56.25200 1.000 33.32017  ? 129 ASP A OD2 1 
ATOM   1024 N  N   . PHE A 1 127 ? 11.37500  37.72700 55.78600 1.000 18.30110  ? 130 PHE A N   1 
ATOM   1025 C  CA  . PHE A 1 127 ? 10.81300  36.44700 55.36600 1.000 16.48970  ? 130 PHE A CA  1 
ATOM   1026 C  C   . PHE A 1 127 ? 9.37700   36.59800 54.88500 1.000 18.46423  ? 130 PHE A C   1 
ATOM   1027 O  O   . PHE A 1 127 ? 9.00800   36.03500 53.84800 1.000 13.29428  ? 130 PHE A O   1 
ATOM   1028 C  CB  . PHE A 1 127 ? 10.89600  35.44300 56.51600 1.000 15.70642  ? 130 PHE A CB  1 
ATOM   1029 C  CG  . PHE A 1 127 ? 10.28100  34.10700 56.21000 1.000 15.31557  ? 130 PHE A CG  1 
ATOM   1030 C  CD1 . PHE A 1 127 ? 11.01400  33.12500 55.56100 1.000 14.98395  ? 130 PHE A CD1 1 
ATOM   1031 C  CD2 . PHE A 1 127 ? 8.97800   33.82100 56.59400 1.000 18.67730  ? 130 PHE A CD2 1 
ATOM   1032 C  CE1 . PHE A 1 127 ? 10.45600  31.88900 55.29000 1.000 19.54712  ? 130 PHE A CE1 1 
ATOM   1033 C  CE2 . PHE A 1 127 ? 8.41100   32.58600 56.32300 1.000 20.88771  ? 130 PHE A CE2 1 
ATOM   1034 C  CZ  . PHE A 1 127 ? 9.15000   31.62000 55.66900 1.000 22.00362  ? 130 PHE A CZ  1 
ATOM   1035 N  N   . GLY A 1 128 ? 8.55200   37.35700 55.62500 1.000 15.69108  ? 131 GLY A N   1 
ATOM   1036 C  CA  . GLY A 1 128 ? 7.15000   37.50700 55.25600 1.000 16.83322  ? 131 GLY A CA  1 
ATOM   1037 C  C   . GLY A 1 128 ? 6.94300   38.13500 53.88800 1.000 18.36381  ? 131 GLY A C   1 
ATOM   1038 O  O   . GLY A 1 128 ? 5.97600   37.81400 53.19300 1.000 17.25218  ? 131 GLY A O   1 
ATOM   1039 N  N   . LYS A 1 129 ? 7.84200   39.02300 53.46900 1.000 14.27232  ? 132 LYS A N   1 
ATOM   1040 C  CA  . LYS A 1 129 ? 7.74900   39.59100 52.09600 1.000 15.32908  ? 132 LYS A CA  1 
ATOM   1041 C  C   . LYS A 1 129 ? 8.26100   38.57900 51.04200 1.000 18.00362  ? 132 LYS A C   1 
ATOM   1042 O  O   . LYS A 1 129 ? 7.67700   38.49200 49.96600 1.000 13.51600  ? 132 LYS A O   1 
ATOM   1043 C  CB  . LYS A 1 129 ? 8.54400   40.89300 52.06800 1.000 18.32857  ? 132 LYS A CB  1 
ATOM   1044 C  CG  . LYS A 1 129 ? 7.99600   41.98300 52.95600 1.000 22.72119  ? 132 LYS A CG  1 
ATOM   1045 C  CD  . LYS A 1 129 ? 6.57600   42.34900 52.55000 1.000 29.03153  ? 132 LYS A CD  1 
ATOM   1046 C  CE  . LYS A 1 129 ? 6.26900   43.78000 52.83900 1.000 34.45631  ? 132 LYS A CE  1 
ATOM   1047 N  NZ  . LYS A 1 129 ? 4.88200   43.94500 53.27200 1.000 62.29127  ? 132 LYS A NZ  1 
ATOM   1048 N  N   . ALA A 1 130 ? 9.26300   37.78400 51.40600 1.000 13.10458  ? 133 ALA A N   1 
ATOM   1049 C  CA  . ALA A 1 130 ? 9.86500   36.79700 50.47900 1.000 19.41375  ? 133 ALA A CA  1 
ATOM   1050 C  C   . ALA A 1 130 ? 8.85400   35.73900 50.02100 1.000 14.50647  ? 133 ALA A C   1 
ATOM   1051 O  O   . ALA A 1 130 ? 8.87700   35.35800 48.85500 1.000 13.34762  ? 133 ALA A O   1 
ATOM   1052 C  CB  . ALA A 1 130 ? 11.02000  36.14000 51.18900 1.000 13.60340  ? 133 ALA A CB  1 
ATOM   1053 N  N   . VAL A 1 131 ? 7.99300   35.29100 50.92400 1.000 13.68312  ? 134 VAL A N   1 
ATOM   1054 C  CA  . VAL A 1 131 ? 7.02400   34.18200 50.63000 1.000 13.93193  ? 134 VAL A CA  1 
ATOM   1055 C  C   . VAL A 1 131 ? 6.04100   34.63500 49.53300 1.000 16.90957  ? 134 VAL A C   1 
ATOM   1056 O  O   . VAL A 1 131 ? 5.39500   33.78000 48.92500 1.000 17.96290  ? 134 VAL A O   1 
ATOM   1057 C  CB  . VAL A 1 131 ? 6.33500   33.63700 51.89700 1.000 16.41769  ? 134 VAL A CB  1 
ATOM   1058 C  CG1 . VAL A 1 131 ? 7.34800   32.96300 52.80600 1.000 22.10850  ? 134 VAL A CG1 1 
ATOM   1059 C  CG2 . VAL A 1 131 ? 5.57600   34.71900 52.64700 1.000 16.71508  ? 134 VAL A CG2 1 
ATOM   1060 N  N   . GLN A 1 132 ? 5.86500   35.93400 49.38900 1.000 17.37923  ? 135 GLN A N   1 
ATOM   1061 C  CA  . GLN A 1 132 ? 4.90500   36.47700 48.40400 1.000 17.52421  ? 135 GLN A CA  1 
ATOM   1062 C  C   . GLN A 1 132 ? 5.53600   36.54800 47.00400 1.000 24.22911  ? 135 GLN A C   1 
ATOM   1063 O  O   . GLN A 1 132 ? 4.88000   37.06100 46.09200 1.000 19.26977  ? 135 GLN A O   1 
ATOM   1064 C  CB  . GLN A 1 132 ? 4.48300   37.83800 48.94000 1.000 14.20601  ? 135 GLN A CB  1 
ATOM   1065 C  CG  . GLN A 1 132 ? 3.76100   37.79000 50.27900 1.000 24.45616  ? 135 GLN A CG  1 
ATOM   1066 C  CD  . GLN A 1 132 ? 3.38500   39.17000 50.76900 1.000 48.63746  ? 135 GLN A CD  1 
ATOM   1067 O  OE1 . GLN A 1 132 ? 3.65900   40.18000 50.11200 1.000 61.11214  ? 135 GLN A OE1 1 
ATOM   1068 N  NE2 . GLN A 1 132 ? 2.74800   39.22900 51.92700 1.000 55.28022  ? 135 GLN A NE2 1 
ATOM   1069 N  N   . GLN A 1 133 ? 6.80400   36.18600 46.88400 1.000 13.38493  ? 136 GLN A N   1 
ATOM   1070 C  CA  . GLN A 1 133 ? 7.49400   36.36300 45.58600 1.000 15.54583  ? 136 GLN A CA  1 
ATOM   1071 C  C   . GLN A 1 133 ? 7.90200   35.02100 44.96300 1.000 17.41401  ? 136 GLN A C   1 
ATOM   1072 O  O   . GLN A 1 133 ? 8.25200   34.10100 45.70100 1.000 17.06059  ? 136 GLN A O   1 
ATOM   1073 C  CB  . GLN A 1 133 ? 8.68900   37.26700 45.82600 1.000 13.88041  ? 136 GLN A CB  1 
ATOM   1074 C  CG  . GLN A 1 133 ? 8.33100   38.58600 46.49800 1.000 24.23349  ? 136 GLN A CG  1 
ATOM   1075 C  CD  . GLN A 1 133 ? 7.49200   39.48100 45.61500 1.000 26.11770  ? 136 GLN A CD  1 
ATOM   1076 O  OE1 . GLN A 1 133 ? 7.71800   39.58800 44.40800 1.000 28.66274  ? 136 GLN A OE1 1 
ATOM   1077 N  NE2 . GLN A 1 133 ? 6.50000   40.12500 46.20600 1.000 38.96615  ? 136 GLN A NE2 1 
ATOM   1078 N  N   . PRO A 1 134 ? 7.87600   34.90800 43.62100 1.000 17.71099  ? 137 PRO A N   1 
ATOM   1079 C  CA  . PRO A 1 134 ? 8.20500   33.62600 42.98200 1.000 13.78480  ? 137 PRO A CA  1 
ATOM   1080 C  C   . PRO A 1 134 ? 9.62800   33.16300 43.23400 1.000 18.37348  ? 137 PRO A C   1 
ATOM   1081 O  O   . PRO A 1 134 ? 9.88400   31.95100 43.22000 1.000 16.34818  ? 137 PRO A O   1 
ATOM   1082 C  CB  . PRO A 1 134 ? 7.96000   33.90400 41.48900 1.000 20.17592  ? 137 PRO A CB  1 
ATOM   1083 C  CG  . PRO A 1 134 ? 8.01200   35.37100 41.35100 1.000 25.99636  ? 137 PRO A CG  1 
ATOM   1084 C  CD  . PRO A 1 134 ? 7.48100   35.92700 42.63300 1.000 25.14155  ? 137 PRO A CD  1 
ATOM   1085 N  N   . ASP A 1 135 ? 10.56300  34.08700 43.45700 1.000 12.99405  ? 138 ASP A N   1 
ATOM   1086 C  CA  . ASP A 1 135 ? 11.94500  33.74500 43.77400 1.000 13.11986  ? 138 ASP A CA  1 
ATOM   1087 C  C   . ASP A 1 135 ? 12.29500  34.08600 45.22200 1.000 15.67714  ? 138 ASP A C   1 
ATOM   1088 O  O   . ASP A 1 135 ? 13.44200  34.41900 45.52600 1.000 13.20399  ? 138 ASP A O   1 
ATOM   1089 C  CB  . ASP A 1 135 ? 12.90200  34.45800 42.81800 1.000 13.78231  ? 138 ASP A CB  1 
ATOM   1090 C  CG  . ASP A 1 135 ? 12.76400  35.96500 42.86800 1.000 19.76233  ? 138 ASP A CG  1 
ATOM   1091 O  OD1 . ASP A 1 135 ? 11.83600  36.47500 43.54000 1.000 22.87923  ? 138 ASP A OD1 1 
ATOM   1092 O  OD2 . ASP A 1 135 ? 13.59500  36.64900 42.23600 1.000 19.97415  ? 138 ASP A OD2 1 
ATOM   1093 N  N   . GLY A 1 136 ? 11.31200  34.02400 46.12300 1.000 8.63246   ? 139 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 136 ? 11.52300  34.52800 47.46500 1.000 10.45813  ? 139 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 136 ? 12.30800  33.60600 48.37200 1.000 9.69666   ? 139 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 136 ? 13.04200  34.08200 49.24700 1.000 11.19346  ? 139 GLY A O   1 
ATOM   1097 N  N   . LEU A 1 137 ? 12.17700  32.28800 48.18200 1.000 7.69898   ? 140 LEU A N   1 
ATOM   1098 C  CA  . LEU A 1 137 ? 12.77000  31.30100 49.07400 1.000 8.15222   ? 140 LEU A CA  1 
ATOM   1099 C  C   . LEU A 1 137 ? 13.64700  30.32100 48.31000 1.000 9.15883   ? 140 LEU A C   1 
ATOM   1100 O  O   . LEU A 1 137 ? 13.40100  30.02300 47.14000 1.000 11.09962  ? 140 LEU A O   1 
ATOM   1101 C  CB  . LEU A 1 137 ? 11.70000  30.50300 49.80900 1.000 13.61594  ? 140 LEU A CB  1 
ATOM   1102 C  CG  . LEU A 1 137 ? 11.30000  30.93700 51.22400 1.000 16.15223  ? 140 LEU A CG  1 
ATOM   1103 C  CD1 . LEU A 1 137 ? 11.01500  32.42600 51.33700 1.000 14.51833  ? 140 LEU A CD1 1 
ATOM   1104 C  CD2 . LEU A 1 137 ? 10.11700  30.08700 51.69800 1.000 13.82274  ? 140 LEU A CD2 1 
ATOM   1105 N  N   . ALA A 1 138 ? 14.66500  29.80800 49.00000 1.000 10.17461  ? 141 ALA A N   1 
ATOM   1106 C  CA  . ALA A 1 138 ? 15.46700  28.68200 48.51800 1.000 13.14111  ? 141 ALA A CA  1 
ATOM   1107 C  C   . ALA A 1 138 ? 15.53800  27.66100 49.64000 1.000 11.82865  ? 141 ALA A C   1 
ATOM   1108 O  O   . ALA A 1 138 ? 15.99200  27.98400 50.74500 1.000 12.79056  ? 141 ALA A O   1 
ATOM   1109 C  CB  . ALA A 1 138 ? 16.87900  29.12000 48.09800 1.000 13.08105  ? 141 ALA A CB  1 
ATOM   1110 N  N   . VAL A 1 139 ? 15.08200  26.44100 49.37700 1.000 11.36189  ? 142 VAL A N   1 
ATOM   1111 C  CA  . VAL A 1 139 ? 15.12000  25.37600 50.37200 1.000 10.52633  ? 142 VAL A CA  1 
ATOM   1112 C  C   . VAL A 1 139 ? 16.09400  24.30800 49.90100 1.000 11.99753  ? 142 VAL A C   1 
ATOM   1113 O  O   . VAL A 1 139 ? 15.94400  23.76200 48.80400 1.000 9.98004   ? 142 VAL A O   1 
ATOM   1114 C  CB  . VAL A 1 139 ? 13.73300  24.77300 50.63700 1.000 11.12631  ? 142 VAL A CB  1 
ATOM   1115 C  CG1 . VAL A 1 139 ? 13.84700  23.72400 51.75300 1.000 9.53682   ? 142 VAL A CG1 1 
ATOM   1116 C  CG2 . VAL A 1 139 ? 12.73900  25.87600 51.01200 1.000 9.77711   ? 142 VAL A CG2 1 
ATOM   1117 N  N   . LEU A 1 140 ? 17.10500  24.03800 50.72000 1.000 8.57878   ? 143 LEU A N   1 
ATOM   1118 C  CA  . LEU A 1 140 ? 18.04500  22.94800 50.49100 1.000 8.54909   ? 143 LEU A CA  1 
ATOM   1119 C  C   . LEU A 1 140 ? 17.46200  21.68400 51.11600 1.000 11.64856  ? 143 LEU A C   1 
ATOM   1120 O  O   . LEU A 1 140 ? 17.19500  21.65700 52.32300 1.000 12.81662  ? 143 LEU A O   1 
ATOM   1121 C  CB  . LEU A 1 140 ? 19.39600  23.29800 51.11700 1.000 11.75702  ? 143 LEU A CB  1 
ATOM   1122 C  CG  . LEU A 1 140 ? 20.57300  22.33500 51.10900 1.000 24.26874  ? 143 LEU A CG  1 
ATOM   1123 C  CD1 . LEU A 1 140 ? 20.99500  22.06200 49.68500 1.000 22.12779  ? 143 LEU A CD1 1 
ATOM   1124 C  CD2 . LEU A 1 140 ? 21.71800  22.95000 51.91800 1.000 26.15578  ? 143 LEU A CD2 1 
ATOM   1125 N  N   . GLY A 1 141 ? 17.26000  20.64800 50.30500 1.000 9.07313   ? 144 GLY A N   1 
ATOM   1126 C  CA  . GLY A 1 141 ? 16.68600  19.38800 50.76100 1.000 7.19894   ? 144 GLY A CA  1 
ATOM   1127 C  C   . GLY A 1 141 ? 17.73800  18.29200 50.77400 1.000 11.51509  ? 144 GLY A C   1 
ATOM   1128 O  O   . GLY A 1 141 ? 18.47500  18.11900 49.80400 1.000 12.16385  ? 144 GLY A O   1 
ATOM   1129 N  N   . ILE A 1 142 ? 17.80800  17.57500 51.89200 1.000 9.62918   ? 145 ILE A N   1 
ATOM   1130 C  CA  . ILE A 1 142 ? 18.80200  16.53100 52.11000 1.000 6.92663   ? 145 ILE A CA  1 
ATOM   1131 C  C   . ILE A 1 142 ? 18.07200  15.28900 52.60000 1.000 11.21572  ? 145 ILE A C   1 
ATOM   1132 O  O   . ILE A 1 142 ? 17.30900  15.35200 53.57400 1.000 10.56255  ? 145 ILE A O   1 
ATOM   1133 C  CB  . ILE A 1 142 ? 19.87900  16.97600 53.11800 1.000 8.64939   ? 145 ILE A CB  1 
ATOM   1134 C  CG1 . ILE A 1 142 ? 20.61400  18.21900 52.59000 1.000 11.95367  ? 145 ILE A CG1 1 
ATOM   1135 C  CG2 . ILE A 1 142 ? 20.87000  15.84800 53.37300 1.000 12.00444  ? 145 ILE A CG2 1 
ATOM   1136 C  CD1 . ILE A 1 142 ? 21.61600  18.83700 53.57600 1.000 9.47984   ? 145 ILE A CD1 1 
ATOM   1137 N  N   . PHE A 1 143 ? 18.27900  14.17100 51.91100 1.000 13.45953  ? 146 PHE A N   1 
ATOM   1138 C  CA  . PHE A 1 143 ? 17.66600  12.91700 52.32400 1.000 8.49231   ? 146 PHE A CA  1 
ATOM   1139 C  C   . PHE A 1 143 ? 18.44200  12.28300 53.47900 1.000 12.26705  ? 146 PHE A C   1 
ATOM   1140 O  O   . PHE A 1 143 ? 19.65300  12.45700 53.61000 1.000 11.70458  ? 146 PHE A O   1 
ATOM   1141 C  CB  . PHE A 1 143 ? 17.61900  11.93400 51.15600 1.000 9.31762   ? 146 PHE A CB  1 
ATOM   1142 C  CG  . PHE A 1 143 ? 16.79100  12.40600 49.99200 1.000 7.47604   ? 146 PHE A CG  1 
ATOM   1143 C  CD1 . PHE A 1 143 ? 15.42900  12.62500 50.14000 1.000 12.03921  ? 146 PHE A CD1 1 
ATOM   1144 C  CD2 . PHE A 1 143 ? 17.37200  12.61100 48.74800 1.000 7.86718   ? 146 PHE A CD2 1 
ATOM   1145 C  CE1 . PHE A 1 143 ? 14.65200  13.04400 49.06700 1.000 10.74393  ? 146 PHE A CE1 1 
ATOM   1146 C  CE2 . PHE A 1 143 ? 16.60900  13.02100 47.66500 1.000 10.77473  ? 146 PHE A CE2 1 
ATOM   1147 C  CZ  . PHE A 1 143 ? 15.24300  13.23300 47.82700 1.000 14.20296  ? 146 PHE A CZ  1 
ATOM   1148 N  N   . LEU A 1 144 ? 17.73000  11.52300 54.30300 1.000 10.90214  ? 147 LEU A N   1 
ATOM   1149 C  CA  . LEU A 1 144 ? 18.32700  10.73300 55.37100 1.000 11.19709  ? 147 LEU A CA  1 
ATOM   1150 C  C   . LEU A 1 144 ? 18.00100  9.26600  55.12900 1.000 13.04723  ? 147 LEU A C   1 
ATOM   1151 O  O   . LEU A 1 144 ? 16.83600  8.91900  54.90200 1.000 10.28718  ? 147 LEU A O   1 
ATOM   1152 C  CB  . LEU A 1 144 ? 17.79200  11.16000 56.74500 1.000 8.30336   ? 147 LEU A CB  1 
ATOM   1153 C  CG  . LEU A 1 144 ? 18.39400  12.38200 57.45900 1.000 11.15838  ? 147 LEU A CG  1 
ATOM   1154 C  CD1 . LEU A 1 144 ? 18.17200  13.67600 56.69000 1.000 14.94274  ? 147 LEU A CD1 1 
ATOM   1155 C  CD2 . LEU A 1 144 ? 17.81900  12.51600 58.87600 1.000 16.24683  ? 147 LEU A CD2 1 
ATOM   1156 N  N   . LYS A 1 145 ? 19.02100  8.41400  55.16300 1.000 16.35371  ? 148 LYS A N   1 
ATOM   1157 C  CA  . LYS A 1 145 ? 18.82200  6.97400  55.20500 1.000 13.02157  ? 148 LYS A CA  1 
ATOM   1158 C  C   . LYS A 1 145 ? 19.33900  6.43800  56.53300 1.000 18.11376  ? 148 LYS A C   1 
ATOM   1159 O  O   . LYS A 1 145 ? 20.18800  7.05100  57.18700 1.000 14.43450  ? 148 LYS A O   1 
ATOM   1160 C  CB  . LYS A 1 145 ? 19.52100  6.26400  54.03600 1.000 16.01497  ? 148 LYS A CB  1 
ATOM   1161 C  CG  . LYS A 1 145 ? 21.02600  6.38500  54.05700 1.000 24.41340  ? 148 LYS A CG  1 
ATOM   1162 C  CD  . LYS A 1 145 ? 21.66000  5.69600  52.85500 1.000 29.99352  ? 148 LYS A CD  1 
ATOM   1163 C  CE  . LYS A 1 145 ? 23.15300  5.49900  53.07600 1.000 39.54061  ? 148 LYS A CE  1 
ATOM   1164 N  NZ  . LYS A 1 145 ? 23.90400  5.30400  51.79900 1.000 56.35752  ? 148 LYS A NZ  1 
ATOM   1165 N  N   . VAL A 1 146 ? 18.80300  5.29800  56.93700 1.000 16.46297  ? 149 VAL A N   1 
ATOM   1166 C  CA  . VAL A 1 146 ? 19.19700  4.67300  58.19400 1.000 17.07112  ? 149 VAL A CA  1 
ATOM   1167 C  C   . VAL A 1 146 ? 20.42400  3.80900  57.94100 1.000 18.37623  ? 149 VAL A C   1 
ATOM   1168 O  O   . VAL A 1 146 ? 20.45400  3.00600  56.99900 1.000 20.19508  ? 149 VAL A O   1 
ATOM   1169 C  CB  . VAL A 1 146 ? 18.04400  3.85300  58.79400 1.000 18.82577  ? 149 VAL A CB  1 
ATOM   1170 C  CG1 . VAL A 1 146 ? 18.50400  3.11100  60.04200 1.000 22.44938  ? 149 VAL A CG1 1 
ATOM   1171 C  CG2 . VAL A 1 146 ? 16.88400  4.77000  59.13700 1.000 20.52407  ? 149 VAL A CG2 1 
ATOM   1172 N  N   . GLY A 1 147 ? 21.44400  4.00200  58.76600 1.000 17.65097  ? 150 GLY A N   1 
ATOM   1173 C  CA  . GLY A 1 147 ? 22.69900  3.28800  58.68700 1.000 21.02575  ? 150 GLY A CA  1 
ATOM   1174 C  C   . GLY A 1 147 ? 23.55800  3.69500  59.86700 1.000 17.71357  ? 150 GLY A C   1 
ATOM   1175 O  O   . GLY A 1 147 ? 23.14300  3.52500  61.01700 1.000 19.68108  ? 150 GLY A O   1 
ATOM   1176 N  N   . SER A 1 148 ? 24.73900  4.25000  59.60600 1.000 22.47779  ? 151 SER A N   1 
ATOM   1177 C  CA  A SER A 1 148 ? 25.59700  4.72100  60.68100 0.490 26.73061  ? 151 SER A CA  1 
ATOM   1178 C  CA  B SER A 1 148 ? 25.60500  4.72800  60.67300 0.510 26.73210  ? 151 SER A CA  1 
ATOM   1179 C  C   . SER A 1 148 ? 25.08700  6.04900  61.23100 1.000 26.35643  ? 151 SER A C   1 
ATOM   1180 O  O   . SER A 1 148 ? 24.38200  6.80400  60.55400 1.000 15.08470  ? 151 SER A O   1 
ATOM   1181 C  CB  A SER A 1 148 ? 27.03700  4.87900  60.19800 0.490 26.69396  ? 151 SER A CB  1 
ATOM   1182 C  CB  B SER A 1 148 ? 27.03600  4.90600  60.16900 0.510 26.71148  ? 151 SER A CB  1 
ATOM   1183 O  OG  A SER A 1 148 ? 27.09000  5.67000  59.02300 0.490 28.40821  ? 151 SER A OG  1 
ATOM   1184 O  OG  B SER A 1 148 ? 27.36700  3.92500  59.20200 0.510 25.13917  ? 151 SER A OG  1 
ATOM   1185 N  N   . ALA A 1 149 ? 25.45700  6.32700  62.48100 1.000 19.76220  ? 152 ALA A N   1 
ATOM   1186 C  CA  . ALA A 1 149 ? 25.02100  7.53900  63.15800 1.000 18.77385  ? 152 ALA A CA  1 
ATOM   1187 C  C   . ALA A 1 149 ? 25.67400  8.77900  62.55200 1.000 23.95736  ? 152 ALA A C   1 
ATOM   1188 O  O   . ALA A 1 149 ? 26.78300  8.73700  62.01500 1.000 22.44028  ? 152 ALA A O   1 
ATOM   1189 C  CB  . ALA A 1 149 ? 25.34200  7.46300  64.65500 1.000 21.75951  ? 152 ALA A CB  1 
ATOM   1190 N  N   . LYS A 1 150 ? 24.96000  9.89800  62.63900 1.000 20.79669  ? 153 LYS A N   1 
ATOM   1191 C  CA  . LYS A 1 150 ? 25.48600  11.17100 62.17600 1.000 18.67663  ? 153 LYS A CA  1 
ATOM   1192 C  C   . LYS A 1 150 ? 25.89500  11.96300 63.39700 1.000 13.90968  ? 153 LYS A C   1 
ATOM   1193 O  O   . LYS A 1 150 ? 25.02400  12.47700 64.11600 1.000 15.42925  ? 153 LYS A O   1 
ATOM   1194 C  CB  . LYS A 1 150 ? 24.44500  11.93900 61.36300 1.000 22.01005  ? 153 LYS A CB  1 
ATOM   1195 C  CG  . LYS A 1 150 ? 25.01600  13.16100 60.66500 1.000 20.72570  ? 153 LYS A CG  1 
ATOM   1196 C  CD  . LYS A 1 150 ? 25.86100  12.73800 59.48900 1.000 21.12275  ? 153 LYS A CD  1 
ATOM   1197 C  CE  . LYS A 1 150 ? 26.33000  13.92800 58.69200 1.000 33.87277  ? 153 LYS A CE  1 
ATOM   1198 N  NZ  . LYS A 1 150 ? 27.23000  13.50600 57.58900 1.000 30.69513  ? 153 LYS A NZ  1 
ATOM   1199 N  N   . PRO A 1 151 ? 27.18900  12.08900 63.68900 1.000 19.12417  ? 154 PRO A N   1 
ATOM   1200 C  CA  . PRO A 1 151 ? 27.58100  12.72300 64.96000 1.000 19.38634  ? 154 PRO A CA  1 
ATOM   1201 C  C   . PRO A 1 151 ? 27.05800  14.14000 65.10700 1.000 14.28519  ? 154 PRO A C   1 
ATOM   1202 O  O   . PRO A 1 151 ? 26.62700  14.52100 66.20200 1.000 18.99614  ? 154 PRO A O   1 
ATOM   1203 C  CB  . PRO A 1 151 ? 29.11700  12.67900 64.90900 1.000 26.47965  ? 154 PRO A CB  1 
ATOM   1204 C  CG  . PRO A 1 151 ? 29.43400  11.55600 63.95500 1.000 28.42922  ? 154 PRO A CG  1 
ATOM   1205 C  CD  . PRO A 1 151 ? 28.34800  11.60300 62.92300 1.000 26.54478  ? 154 PRO A CD  1 
ATOM   1206 N  N   . GLY A 1 152 ? 27.06900  14.92600 64.02700 1.000 15.66609  ? 155 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 152 ? 26.61300  16.30800 64.06100 1.000 19.14960  ? 155 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 152 ? 25.12000  16.48100 64.27800 1.000 21.07609  ? 155 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 152 ? 24.66700  17.61000 64.49400 1.000 23.51027  ? 155 GLY A O   1 
ATOM   1210 N  N   . LEU A 1 153 ? 24.35000  15.40100 64.21000 1.000 16.60109  ? 156 LEU A N   1 
ATOM   1211 C  CA  . LEU A 1 153 ? 22.92300  15.45100 64.50300 1.000 11.81935  ? 156 LEU A CA  1 
ATOM   1212 C  C   . LEU A 1 153 ? 22.62000  15.25300 65.98000 1.000 14.19985  ? 156 LEU A C   1 
ATOM   1213 O  O   . LEU A 1 153 ? 21.55100  15.67400 66.44500 1.000 16.48438  ? 156 LEU A O   1 
ATOM   1214 C  CB  . LEU A 1 153 ? 22.19300  14.37800 63.68600 1.000 18.03327  ? 156 LEU A CB  1 
ATOM   1215 C  CG  . LEU A 1 153 ? 20.66400  14.34800 63.72200 1.000 22.54508  ? 156 LEU A CG  1 
ATOM   1216 C  CD1 . LEU A 1 153 ? 20.09800  15.66300 63.20000 1.000 17.03399  ? 156 LEU A CD1 1 
ATOM   1217 C  CD2 . LEU A 1 153 ? 20.13000  13.15100 62.93700 1.000 21.72149  ? 156 LEU A CD2 1 
ATOM   1218 N  N   . GLN A 1 154 ? 23.54400  14.65400 66.73400 1.000 18.03813  ? 157 GLN A N   1 
ATOM   1219 C  CA  . GLN A 1 154 ? 23.20200  14.16500 68.06800 1.000 18.69322  ? 157 GLN A CA  1 
ATOM   1220 C  C   . GLN A 1 154 ? 22.78500  15.29400 69.00200 1.000 12.25032  ? 157 GLN A C   1 
ATOM   1221 O  O   . GLN A 1 154 ? 21.89400  15.10700 69.83600 1.000 15.44127  ? 157 GLN A O   1 
ATOM   1222 C  CB  . GLN A 1 154 ? 24.37200  13.37400 68.66000 1.000 21.96990  ? 157 GLN A CB  1 
ATOM   1223 C  CG  . GLN A 1 154 ? 24.00000  12.54500 69.90200 1.000 19.44897  ? 157 GLN A CG  1 
ATOM   1224 C  CD  . GLN A 1 154 ? 22.89900  11.51500 69.64000 1.000 23.06657  ? 157 GLN A CD  1 
ATOM   1225 O  OE1 . GLN A 1 154 ? 22.83900  10.89900 68.57300 1.000 17.98461  ? 157 GLN A OE1 1 
ATOM   1226 N  NE2 . GLN A 1 154 ? 22.02100  11.33100 70.62200 1.000 21.34687  ? 157 GLN A NE2 1 
ATOM   1227 N  N   . LYS A 1 155 ? 23.38000  16.47900 68.85400 1.000 17.68999  ? 158 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 155 ? 23.00100  17.60100 69.70500 1.000 16.59053  ? 158 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 155 ? 21.51700  17.92400 69.55300 1.000 15.50183  ? 158 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 155 ? 20.83800  18.25000 70.53200 1.000 16.35778  ? 158 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 155 ? 23.86500  18.81500 69.36300 1.000 24.04590  ? 158 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 155 ? 23.64600  20.02700 70.24300 1.000 44.14864  ? 158 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 155 ? 24.59700  21.16400 69.85200 1.000 47.03450  ? 158 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 155 ? 24.07200  22.51200 70.33400 1.000 37.22932  ? 158 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 155 ? 25.17700  23.48400 70.58400 1.000 39.12360  ? 158 LYS A NZ  1 
ATOM   1236 N  N   . VAL A 1 156 ? 20.99900  17.82800 68.32600 1.000 13.30250  ? 159 VAL A N   1 
ATOM   1237 C  CA  . VAL A 1 156 ? 19.56800  18.02100 68.09500 1.000 11.08025  ? 159 VAL A CA  1 
ATOM   1238 C  C   . VAL A 1 156 ? 18.76700  16.91900 68.77800 1.000 11.59555  ? 159 VAL A C   1 
ATOM   1239 O  O   . VAL A 1 156 ? 17.78800  17.18400 69.48200 1.000 15.80275  ? 159 VAL A O   1 
ATOM   1240 C  CB  . VAL A 1 156 ? 19.27100  18.06100 66.58500 1.000 17.58723  ? 159 VAL A CB  1 
ATOM   1241 C  CG1 . VAL A 1 156 ? 17.76600  18.13600 66.35000 1.000 15.99167  ? 159 VAL A CG1 1 
ATOM   1242 C  CG2 . VAL A 1 156 ? 20.00500  19.22700 65.92500 1.000 19.85490  ? 159 VAL A CG2 1 
ATOM   1243 N  N   . VAL A 1 157 ? 19.17400  15.66700 68.57700 1.000 14.38821  ? 160 VAL A N   1 
ATOM   1244 C  CA  . VAL A 1 157 ? 18.42500  14.53400 69.11800 1.000 15.36778  ? 160 VAL A CA  1 
ATOM   1245 C  C   . VAL A 1 157 ? 18.33800  14.62400 70.63300 1.000 16.53211  ? 160 VAL A C   1 
ATOM   1246 O  O   . VAL A 1 157 ? 17.29900  14.32100 71.22400 1.000 19.67283  ? 160 VAL A O   1 
ATOM   1247 C  CB  . VAL A 1 157 ? 19.06800  13.20800 68.66100 1.000 22.03097  ? 160 VAL A CB  1 
ATOM   1248 C  CG1 . VAL A 1 157 ? 18.74300  12.07800 69.62700 1.000 28.98444  ? 160 VAL A CG1 1 
ATOM   1249 C  CG2 . VAL A 1 157 ? 18.61300  12.86200 67.25400 1.000 20.48442  ? 160 VAL A CG2 1 
ATOM   1250 N  N   . ASP A 1 158 ? 19.41300  15.06600 71.28600 1.000 17.31312  ? 161 ASP A N   1 
ATOM   1251 C  CA  . ASP A 1 158 ? 19.43400  15.02500 72.74100 1.000 23.20884  ? 161 ASP A CA  1 
ATOM   1252 C  C   . ASP A 1 158 ? 18.50200  16.05700 73.36600 1.000 30.37451  ? 161 ASP A C   1 
ATOM   1253 O  O   . ASP A 1 158 ? 18.05900  15.86000 74.49900 1.000 27.52973  ? 161 ASP A O   1 
ATOM   1254 C  CB  . ASP A 1 158 ? 20.85900  15.22500 73.25400 1.000 22.98698  ? 161 ASP A CB  1 
ATOM   1255 C  CG  . ASP A 1 158 ? 21.68300  13.94600 73.19600 1.000 25.66088  ? 161 ASP A CG  1 
ATOM   1256 O  OD1 . ASP A 1 158 ? 21.09900  12.84000 73.22500 1.000 30.22821  ? 161 ASP A OD1 1 
ATOM   1257 O  OD2 . ASP A 1 158 ? 22.91500  14.05100 73.10600 1.000 31.87047  ? 161 ASP A OD2 1 
ATOM   1258 N  N   . VAL A 1 159 ? 18.18700  17.14300 72.65600 1.000 15.90449  ? 162 VAL A N   1 
ATOM   1259 C  CA  . VAL A 1 159 ? 17.33700  18.17700 73.23300 1.000 16.71996  ? 162 VAL A CA  1 
ATOM   1260 C  C   . VAL A 1 159 ? 15.85200  17.92100 73.00500 1.000 17.70265  ? 162 VAL A C   1 
ATOM   1261 O  O   . VAL A 1 159 ? 15.01800  18.64200 73.57200 1.000 16.99327  ? 162 VAL A O   1 
ATOM   1262 C  CB  . VAL A 1 159 ? 17.74400  19.55800 72.68200 1.000 21.01198  ? 162 VAL A CB  1 
ATOM   1263 C  CG1 . VAL A 1 159 ? 17.25400  19.73000 71.25600 1.000 20.45482  ? 162 VAL A CG1 1 
ATOM   1264 C  CG2 . VAL A 1 159 ? 17.22800  20.66700 73.57600 1.000 33.57526  ? 162 VAL A CG2 1 
ATOM   1265 N  N   . LEU A 1 160 ? 15.49400  16.90100 72.21600 1.000 17.92287  ? 163 LEU A N   1 
ATOM   1266 C  CA  . LEU A 1 160 ? 14.10500  16.72600 71.81100 1.000 11.94943  ? 163 LEU A CA  1 
ATOM   1267 C  C   . LEU A 1 160 ? 13.19000  16.43100 72.99700 1.000 19.66121  ? 163 LEU A C   1 
ATOM   1268 O  O   . LEU A 1 160 ? 11.99200  16.74100 72.94400 1.000 18.21755  ? 163 LEU A O   1 
ATOM   1269 C  CB  . LEU A 1 160 ? 14.00400  15.61800 70.75700 1.000 19.01073  ? 163 LEU A CB  1 
ATOM   1270 C  CG  . LEU A 1 160 ? 14.64300  15.91400 69.38700 1.000 17.51678  ? 163 LEU A CG  1 
ATOM   1271 C  CD1 . LEU A 1 160 ? 14.24700  14.86700 68.35100 1.000 18.25403  ? 163 LEU A CD1 1 
ATOM   1272 C  CD2 . LEU A 1 160 ? 14.26600  17.29900 68.89200 1.000 13.88147  ? 163 LEU A CD2 1 
ATOM   1273 N  N   . ASP A 1 161 ? 13.73000  15.85400 74.07700 1.000 19.88273  ? 164 ASP A N   1 
ATOM   1274 C  CA  . ASP A 1 161 ? 12.91000  15.58300 75.25700 1.000 31.29102  ? 164 ASP A CA  1 
ATOM   1275 C  C   . ASP A 1 161 ? 12.39100  16.86700 75.88900 1.000 19.43761  ? 164 ASP A C   1 
ATOM   1276 O  O   . ASP A 1 161 ? 11.32500  16.86500 76.51400 1.000 30.17441  ? 164 ASP A O   1 
ATOM   1277 C  CB  . ASP A 1 161 ? 13.70700  14.78800 76.29600 1.000 33.87937  ? 164 ASP A CB  1 
ATOM   1278 C  CG  . ASP A 1 161 ? 13.97500  13.36200 75.86500 1.000 46.74612  ? 164 ASP A CG  1 
ATOM   1279 O  OD1 . ASP A 1 161 ? 13.24200  12.84400 74.99600 1.000 57.43300  ? 164 ASP A OD1 1 
ATOM   1280 O  OD2 . ASP A 1 161 ? 14.92100  12.75700 76.40900 1.000 62.86707  ? 164 ASP A OD2 1 
ATOM   1281 N  N   . SER A 1 162 ? 13.12100  17.97300 75.73900 1.000 16.71578  ? 165 SER A N   1 
ATOM   1282 C  CA  . SER A 1 162 ? 12.68000  19.23100 76.32700 1.000 16.91417  ? 165 SER A CA  1 
ATOM   1283 C  C   . SER A 1 162 ? 11.62900  19.96100 75.49100 1.000 18.48962  ? 165 SER A C   1 
ATOM   1284 O  O   . SER A 1 162 ? 11.07000  20.95200 75.96800 1.000 19.66131  ? 165 SER A O   1 
ATOM   1285 C  CB  . SER A 1 162 ? 13.87700  20.15100 76.56200 1.000 19.45215  ? 165 SER A CB  1 
ATOM   1286 O  OG  . SER A 1 162 ? 14.43700  20.56400 75.33700 1.000 34.99981  ? 165 SER A OG  1 
ATOM   1287 N  N   . ILE A 1 163 ? 11.34300  19.51100 74.26600 1.000 14.08596  ? 166 ILE A N   1 
ATOM   1288 C  CA  . ILE A 1 163 ? 10.32200  20.14600 73.43600 1.000 11.56234  ? 166 ILE A CA  1 
ATOM   1289 C  C   . ILE A 1 163 ? 9.34000   19.09000 72.94300 1.000 16.87292  ? 166 ILE A C   1 
ATOM   1290 O  O   . ILE A 1 163 ? 8.96900   19.06600 71.76200 1.000 16.75866  ? 166 ILE A O   1 
ATOM   1291 C  CB  . ILE A 1 163 ? 10.94100  20.91900 72.25400 1.000 14.22350  ? 166 ILE A CB  1 
ATOM   1292 C  CG1 . ILE A 1 163 ? 11.78400  19.99800 71.36100 1.000 14.46486  ? 166 ILE A CG1 1 
ATOM   1293 C  CG2 . ILE A 1 163 ? 11.76200  22.10300 72.74900 1.000 18.39851  ? 166 ILE A CG2 1 
ATOM   1294 C  CD1 . ILE A 1 163 ? 11.75900  20.39700 69.89600 1.000 14.79680  ? 166 ILE A CD1 1 
ATOM   1295 N  N   . LYS A 1 164 ? 8.89900   18.17900 73.80300 1.000 13.97604  ? 167 LYS A N   1 
ATOM   1296 C  CA  . LYS A 1 164 ? 8.08400   17.03400 73.33200 1.000 16.44086  ? 167 LYS A CA  1 
ATOM   1297 C  C   . LYS A 1 164 ? 6.73100   17.46200 72.77200 1.000 13.97400  ? 167 LYS A C   1 
ATOM   1298 O  O   . LYS A 1 164 ? 6.29500   16.82400 71.82100 1.000 18.51357  ? 167 LYS A O   1 
ATOM   1299 C  CB  . LYS A 1 164 ? 7.75100   16.07500 74.48500 1.000 17.52541  ? 167 LYS A CB  1 
ATOM   1300 C  CG  . LYS A 1 164 ? 7.27400   14.71300 74.02400 1.000 24.90400  ? 167 LYS A CG  1 
ATOM   1301 C  CD  . LYS A 1 164 ? 7.17400   13.67700 75.13500 1.000 36.74372  ? 167 LYS A CD  1 
ATOM   1302 C  CE  . LYS A 1 164 ? 5.77400   13.21300 75.33600 1.000 34.36333  ? 167 LYS A CE  1 
ATOM   1303 N  NZ  . LYS A 1 164 ? 5.65400   11.76400 75.18000 1.000 48.26333  ? 167 LYS A NZ  1 
ATOM   1304 N  N   . THR A 1 165 ? 6.15300   18.52900 73.29900 1.000 12.67919  ? 168 THR A N   1 
ATOM   1305 C  CA  . THR A 1 165 ? 4.76300   18.89300 72.98100 1.000 19.88077  ? 168 THR A CA  1 
ATOM   1306 C  C   . THR A 1 165 ? 4.68900   20.22000 72.27700 1.000 13.92454  ? 168 THR A C   1 
ATOM   1307 O  O   . THR A 1 165 ? 5.62200   20.99800 72.38100 1.000 17.05694  ? 168 THR A O   1 
ATOM   1308 C  CB  . THR A 1 165 ? 3.92500   18.89200 74.26700 1.000 14.16737  ? 168 THR A CB  1 
ATOM   1309 O  OG1 . THR A 1 165 ? 4.58800   19.69800 75.23100 1.000 16.95395  ? 168 THR A OG1 1 
ATOM   1310 C  CG2 . THR A 1 165 ? 3.73000   17.48900 74.81300 1.000 20.99249  ? 168 THR A CG2 1 
ATOM   1311 N  N   . LYS A 1 166 ? 3.59000   20.43700 71.57600 1.000 15.93935  ? 169 LYS A N   1 
ATOM   1312 C  CA  . LYS A 1 166 ? 3.45600   21.63800 70.73800 1.000 17.92572  ? 169 LYS A CA  1 
ATOM   1313 C  C   . LYS A 1 166 ? 3.57200   22.90800 71.57800 1.000 20.55886  ? 169 LYS A C   1 
ATOM   1314 O  O   . LYS A 1 166 ? 2.99800   22.95900 72.66200 1.000 20.32694  ? 169 LYS A O   1 
ATOM   1315 C  CB  . LYS A 1 166 ? 2.10200   21.58600 70.01800 1.000 15.24190  ? 169 LYS A CB  1 
ATOM   1316 C  CG  . LYS A 1 166 ? 1.61700   22.82500 69.30500 1.000 20.67492  ? 169 LYS A CG  1 
ATOM   1317 C  CD  . LYS A 1 166 ? 0.23000   22.58600 68.72200 1.000 29.16820  ? 169 LYS A CD  1 
ATOM   1318 C  CE  . LYS A 1 166 ? -0.12100  23.57600 67.66100 1.000 42.58317  ? 169 LYS A CE  1 
ATOM   1319 N  NZ  . LYS A 1 166 ? -1.57300  23.70400 67.50400 1.000 66.72643  ? 169 LYS A NZ  1 
ATOM   1320 N  N   . GLY A 1 167 ? 4.30000   23.88000 71.04600 1.000 14.97301  ? 170 GLY A N   1 
ATOM   1321 C  CA  . GLY A 1 167 ? 4.47600   25.18900 71.68800 1.000 16.43279  ? 170 GLY A CA  1 
ATOM   1322 C  C   . GLY A 1 167 ? 5.65200   25.23200 72.63200 1.000 16.54649  ? 170 GLY A C   1 
ATOM   1323 O  O   . GLY A 1 167 ? 6.03000   26.34000 73.01800 1.000 19.13454  ? 170 GLY A O   1 
ATOM   1324 N  N   . LYS A 1 168 ? 6.26400   24.08700 72.89200 1.000 12.13617  ? 171 LYS A N   1 
ATOM   1325 C  CA  . LYS A 1 168 ? 7.48700   24.05800 73.72200 1.000 13.29838  ? 171 LYS A CA  1 
ATOM   1326 C  C   . LYS A 1 168 ? 8.69700   24.58000 72.93300 1.000 16.86634  ? 171 LYS A C   1 
ATOM   1327 O  O   . LYS A 1 168 ? 8.85500   24.19200 71.78200 1.000 16.07574  ? 171 LYS A O   1 
ATOM   1328 C  CB  . LYS A 1 168 ? 7.75000   22.67400 74.30900 1.000 13.45345  ? 171 LYS A CB  1 
ATOM   1329 C  CG  . LYS A 1 168 ? 6.66800   22.16400 75.23200 1.000 18.40727  ? 171 LYS A CG  1 
ATOM   1330 C  CD  . LYS A 1 168 ? 6.61700   22.90300 76.56000 1.000 33.26342  ? 171 LYS A CD  1 
ATOM   1331 C  CE  . LYS A 1 168 ? 6.25400   21.98300 77.67800 1.000 40.46088  ? 171 LYS A CE  1 
ATOM   1332 N  NZ  . LYS A 1 168 ? 6.03200   22.71000 78.92800 1.000 46.20325  ? 171 LYS A NZ  1 
ATOM   1333 N  N   . SER A 1 169 ? 9.55300   25.34100 73.60200 1.000 16.32121  ? 172 SER A N   1 
ATOM   1334 C  CA  . SER A 1 169 ? 10.76600  25.91300 72.97600 1.000 14.31890  ? 172 SER A CA  1 
ATOM   1335 C  C   . SER A 1 169 ? 11.93500  25.77400 73.95400 1.000 18.79934  ? 172 SER A C   1 
ATOM   1336 O  O   . SER A 1 169 ? 11.69300  25.74700 75.16500 1.000 21.04909  ? 172 SER A O   1 
ATOM   1337 C  CB  . SER A 1 169 ? 10.55900  27.37000 72.64000 1.000 16.53159  ? 172 SER A CB  1 
ATOM   1338 O  OG  . SER A 1 169 ? 10.64400  28.20800 73.77700 1.000 21.60041  ? 172 SER A OG  1 
ATOM   1339 N  N   . ALA A 1 170 ? 13.14200  25.66300 73.43500 1.000 17.79961  ? 173 ALA A N   1 
ATOM   1340 C  CA  . ALA A 1 170 ? 14.33100  25.62100 74.26900 1.000 16.72303  ? 173 ALA A CA  1 
ATOM   1341 C  C   . ALA A 1 170 ? 15.42900  26.43600 73.60900 1.000 17.71355  ? 173 ALA A C   1 
ATOM   1342 O  O   . ALA A 1 170 ? 15.51000  26.52100 72.38000 1.000 15.01353  ? 173 ALA A O   1 
ATOM   1343 C  CB  . ALA A 1 170 ? 14.81800  24.18700 74.49400 1.000 17.04292  ? 173 ALA A CB  1 
ATOM   1344 N  N   . ASP A 1 171 ? 16.28300  27.02200 74.43900 1.000 17.08134  ? 174 ASP A N   1 
ATOM   1345 C  CA  . ASP A 1 171 ? 17.45800  27.70500 73.92100 1.000 18.19962  ? 174 ASP A CA  1 
ATOM   1346 C  C   . ASP A 1 171 ? 18.35500  26.70500 73.20300 1.000 19.14180  ? 174 ASP A C   1 
ATOM   1347 O  O   . ASP A 1 171 ? 18.56300  25.58300 73.67100 1.000 19.69577  ? 174 ASP A O   1 
ATOM   1348 C  CB  . ASP A 1 171 ? 18.20300  28.40700 75.05700 1.000 22.68466  ? 174 ASP A CB  1 
ATOM   1349 C  CG  . ASP A 1 171 ? 17.37800  29.53600 75.67600 1.000 32.66661  ? 174 ASP A CG  1 
ATOM   1350 O  OD1 . ASP A 1 171 ? 16.87500  30.39200 74.92100 1.000 41.68136  ? 174 ASP A OD1 1 
ATOM   1351 O  OD2 . ASP A 1 171 ? 17.20100  29.55100 76.91100 1.000 44.77336  ? 174 ASP A OD2 1 
ATOM   1352 N  N   . PHE A 1 172 ? 18.85200  27.10100 72.02600 1.000 17.16008  ? 175 PHE A N   1 
ATOM   1353 C  CA  . PHE A 1 172 ? 19.62900  26.16000 71.22200 1.000 19.05863  ? 175 PHE A CA  1 
ATOM   1354 C  C   . PHE A 1 172 ? 20.70300  26.96200 70.48500 1.000 14.19328  ? 175 PHE A C   1 
ATOM   1355 O  O   . PHE A 1 172 ? 20.58400  27.28300 69.30000 1.000 15.68047  ? 175 PHE A O   1 
ATOM   1356 C  CB  . PHE A 1 172 ? 18.74300  25.37900 70.25100 1.000 12.79769  ? 175 PHE A CB  1 
ATOM   1357 C  CG  . PHE A 1 172 ? 19.36900  24.10800 69.76200 1.000 12.78029  ? 175 PHE A CG  1 
ATOM   1358 C  CD1 . PHE A 1 172 ? 19.61900  23.06800 70.64200 1.000 17.36448  ? 175 PHE A CD1 1 
ATOM   1359 C  CD2 . PHE A 1 172 ? 19.71200  23.95400 68.43400 1.000 13.51894  ? 175 PHE A CD2 1 
ATOM   1360 C  CE1 . PHE A 1 172 ? 20.19800  21.89100 70.19900 1.000 19.42489  ? 175 PHE A CE1 1 
ATOM   1361 C  CE2 . PHE A 1 172 ? 20.29200  22.77500 67.98400 1.000 17.61888  ? 175 PHE A CE2 1 
ATOM   1362 C  CZ  . PHE A 1 172 ? 20.53300  21.74800 68.87300 1.000 18.05608  ? 175 PHE A CZ  1 
ATOM   1363 N  N   . THR A 1 173 ? 21.77000  27.29500 71.20700 1.000 11.19994  ? 176 THR A N   1 
ATOM   1364 C  CA  . THR A 1 173 ? 22.83000  28.13100 70.67000 1.000 11.52104  ? 176 THR A CA  1 
ATOM   1365 C  C   . THR A 1 173 ? 24.03600  27.30600 70.24900 1.000 13.67412  ? 176 THR A C   1 
ATOM   1366 O  O   . THR A 1 173 ? 24.25500  26.17900 70.70600 1.000 15.21956  ? 176 THR A O   1 
ATOM   1367 C  CB  . THR A 1 173 ? 23.28100  29.18200 71.68900 1.000 10.71331  ? 176 THR A CB  1 
ATOM   1368 O  OG1 . THR A 1 173 ? 23.61300  28.53100 72.91900 1.000 16.04993  ? 176 THR A OG1 1 
ATOM   1369 C  CG2 . THR A 1 173 ? 22.20200  30.20800 71.93000 1.000 18.15562  ? 176 THR A CG2 1 
ATOM   1370 N  N   . ASN A 1 174 ? 24.83200  27.91300 69.37300 1.000 12.75312  ? 177 ASN A N   1 
ATOM   1371 C  CA  . ASN A 1 174 ? 26.12000  27.38000 68.94200 1.000 13.84723  ? 177 ASN A CA  1 
ATOM   1372 C  C   . ASN A 1 174 ? 25.98200  26.03500 68.23100 1.000 16.25411  ? 177 ASN A C   1 
ATOM   1373 O  O   . ASN A 1 174 ? 26.89300  25.20400 68.26000 1.000 17.23268  ? 177 ASN A O   1 
ATOM   1374 C  CB  . ASN A 1 174 ? 27.09100  27.27900 70.12200 1.000 15.08557  ? 177 ASN A CB  1 
ATOM   1375 C  CG  . ASN A 1 174 ? 27.35200  28.62900 70.77100 1.000 18.68493  ? 177 ASN A CG  1 
ATOM   1376 O  OD1 . ASN A 1 174 ? 27.96100  29.51300 70.16900 1.000 20.66414  ? 177 ASN A OD1 1 
ATOM   1377 N  ND2 . ASN A 1 174 ? 26.88900  28.79600 72.00000 1.000 16.09741  ? 177 ASN A ND2 1 
ATOM   1378 N  N   . PHE A 1 175 ? 24.85500  25.78900 67.57000 1.000 13.13322  ? 178 PHE A N   1 
ATOM   1379 C  CA  . PHE A 1 175 ? 24.74900  24.60600 66.72700 1.000 11.74891  ? 178 PHE A CA  1 
ATOM   1380 C  C   . PHE A 1 175 ? 25.26500  24.92200 65.32800 1.000 9.89573   ? 178 PHE A C   1 
ATOM   1381 O  O   . PHE A 1 175 ? 24.83500  25.89900 64.71200 1.000 17.23231  ? 178 PHE A O   1 
ATOM   1382 C  CB  . PHE A 1 175 ? 23.31700  24.08200 66.62900 1.000 17.06107  ? 178 PHE A CB  1 
ATOM   1383 C  CG  . PHE A 1 175 ? 23.21000  22.86000 65.76600 1.000 13.69975  ? 178 PHE A CG  1 
ATOM   1384 C  CD1 . PHE A 1 175 ? 23.55600  21.61700 66.26900 1.000 16.18606  ? 178 PHE A CD1 1 
ATOM   1385 C  CD2 . PHE A 1 175 ? 22.81800  22.95900 64.44000 1.000 11.58847  ? 178 PHE A CD2 1 
ATOM   1386 C  CE1 . PHE A 1 175 ? 23.48900  20.48500 65.46900 1.000 16.02621  ? 178 PHE A CE1 1 
ATOM   1387 C  CE2 . PHE A 1 175 ? 22.73900  21.82800 63.62800 1.000 11.84699  ? 178 PHE A CE2 1 
ATOM   1388 C  CZ  . PHE A 1 175 ? 23.06600  20.59400 64.14300 1.000 15.04073  ? 178 PHE A CZ  1 
ATOM   1389 N  N   . ASP A 1 176 ? 26.15300  24.06600 64.81700 1.000 14.74383  ? 179 ASP A N   1 
ATOM   1390 C  CA  . ASP A 1 176 ? 26.78100  24.28600 63.52000 1.000 15.07285  ? 179 ASP A CA  1 
ATOM   1391 C  C   . ASP A 1 176 ? 26.09400  23.44000 62.45900 1.000 12.68362  ? 179 ASP A C   1 
ATOM   1392 O  O   . ASP A 1 176 ? 26.26700  22.20900 62.45800 1.000 13.37646  ? 179 ASP A O   1 
ATOM   1393 C  CB  . ASP A 1 176 ? 28.26400  23.93800 63.59300 1.000 15.21260  ? 179 ASP A CB  1 
ATOM   1394 C  CG  . ASP A 1 176 ? 29.02700  24.33200 62.33800 1.000 21.60829  ? 179 ASP A CG  1 
ATOM   1395 O  OD1 . ASP A 1 176 ? 28.42500  24.40600 61.23900 1.000 16.73625  ? 179 ASP A OD1 1 
ATOM   1396 O  OD2 . ASP A 1 176 ? 30.24400  24.56800 62.46200 1.000 24.24542  ? 179 ASP A OD2 1 
ATOM   1397 N  N   . PRO A 1 177 ? 25.34300  24.03600 61.52400 1.000 12.77483  ? 180 PRO A N   1 
ATOM   1398 C  CA  . PRO A 1 177 ? 24.62400  23.22000 60.53100 1.000 12.50337  ? 180 PRO A CA  1 
ATOM   1399 C  C   . PRO A 1 177 ? 25.53600  22.57100 59.49500 1.000 17.00439  ? 180 PRO A C   1 
ATOM   1400 O  O   . PRO A 1 177 ? 25.07400  21.69000 58.75700 1.000 12.88098  ? 180 PRO A O   1 
ATOM   1401 C  CB  . PRO A 1 177 ? 23.65900  24.22100 59.88200 1.000 15.68264  ? 180 PRO A CB  1 
ATOM   1402 C  CG  . PRO A 1 177 ? 24.30600  25.54100 60.06100 1.000 18.65423  ? 180 PRO A CG  1 
ATOM   1403 C  CD  . PRO A 1 177 ? 25.03900  25.47100 61.38500 1.000 17.30031  ? 180 PRO A CD  1 
ATOM   1404 N  N   . ARG A 1 178 ? 26.81100  22.96000 59.42900 1.000 13.08194  ? 181 ARG A N   1 
ATOM   1405 C  CA  . ARG A 1 178 ? 27.73600  22.28100 58.52200 1.000 19.06388  ? 181 ARG A CA  1 
ATOM   1406 C  C   . ARG A 1 178 ? 27.86400  20.80100 58.86100 1.000 18.17061  ? 181 ARG A C   1 
ATOM   1407 O  O   . ARG A 1 178 ? 28.20700  20.00400 57.98300 1.000 15.75934  ? 181 ARG A O   1 
ATOM   1408 C  CB  . ARG A 1 178 ? 29.11100  22.96500 58.55000 1.000 9.72444   ? 181 ARG A CB  1 
ATOM   1409 C  CG  . ARG A 1 178 ? 29.08600  24.39900 58.02800 1.000 17.15218  ? 181 ARG A CG  1 
ATOM   1410 C  CD  . ARG A 1 178 ? 30.45500  25.05300 58.10900 1.000 16.02127  ? 181 ARG A CD  1 
ATOM   1411 N  NE  . ARG A 1 178 ? 30.90900  25.16300 59.49300 1.000 20.45352  ? 181 ARG A NE  1 
ATOM   1412 C  CZ  . ARG A 1 178 ? 31.99400  25.82200 59.87500 1.000 27.22870  ? 181 ARG A CZ  1 
ATOM   1413 N  NH1 . ARG A 1 178 ? 32.78900  26.41100 58.99800 1.000 26.73250  ? 181 ARG A NH1 1 
ATOM   1414 N  NH2 . ARG A 1 178 ? 32.28800  25.89300 61.17200 1.000 27.69705  ? 181 ARG A NH2 1 
ATOM   1415 N  N   . GLY A 1 179 ? 27.55200  20.41100 60.09900 1.000 18.09833  ? 182 GLY A N   1 
ATOM   1416 C  CA  . GLY A 1 179 ? 27.56600  19.00400 60.47600 1.000 16.71347  ? 182 GLY A CA  1 
ATOM   1417 C  C   . GLY A 1 179 ? 26.50000  18.15300 59.81600 1.000 16.53641  ? 182 GLY A C   1 
ATOM   1418 O  O   . GLY A 1 179 ? 26.56700  16.92300 59.92700 1.000 19.19187  ? 182 GLY A O   1 
ATOM   1419 N  N   . LEU A 1 180 ? 25.53300  18.76300 59.12300 1.000 15.51059  ? 183 LEU A N   1 
ATOM   1420 C  CA  . LEU A 1 180 ? 24.42700  18.02900 58.50800 1.000 14.97341  ? 183 LEU A CA  1 
ATOM   1421 C  C   . LEU A 1 180 ? 24.58400  17.84200 57.00700 1.000 18.27704  ? 183 LEU A C   1 
ATOM   1422 O  O   . LEU A 1 180 ? 23.69700  17.24800 56.37100 1.000 21.27513  ? 183 LEU A O   1 
ATOM   1423 C  CB  . LEU A 1 180 ? 23.10100  18.74700 58.79500 1.000 14.61660  ? 183 LEU A CB  1 
ATOM   1424 C  CG  . LEU A 1 180 ? 22.81600  19.00700 60.27700 1.000 18.00129  ? 183 LEU A CG  1 
ATOM   1425 C  CD1 . LEU A 1 180 ? 21.55700  19.83100 60.45400 1.000 23.30254  ? 183 LEU A CD1 1 
ATOM   1426 C  CD2 . LEU A 1 180 ? 22.71800  17.70800 61.06300 1.000 22.38733  ? 183 LEU A CD2 1 
ATOM   1427 N  N   . LEU A 1 181 ? 25.68300  18.32400 56.42100 1.000 11.10063  ? 184 LEU A N   1 
ATOM   1428 C  CA  . LEU A 1 181 ? 25.76800  18.29200 54.97100 1.000 13.01639  ? 184 LEU A CA  1 
ATOM   1429 C  C   . LEU A 1 181 ? 26.47200  17.02700 54.49700 1.000 19.25775  ? 184 LEU A C   1 
ATOM   1430 O  O   . LEU A 1 181 ? 27.35300  16.50100 55.18700 1.000 18.04404  ? 184 LEU A O   1 
ATOM   1431 C  CB  . LEU A 1 181 ? 26.51500  19.52200 54.45100 1.000 10.96938  ? 184 LEU A CB  1 
ATOM   1432 C  CG  . LEU A 1 181 ? 25.92000  20.89600 54.81300 1.000 16.44218  ? 184 LEU A CG  1 
ATOM   1433 C  CD1 . LEU A 1 181 ? 26.77700  22.06200 54.30400 1.000 17.34882  ? 184 LEU A CD1 1 
ATOM   1434 C  CD2 . LEU A 1 181 ? 24.49300  21.01600 54.28200 1.000 15.22387  ? 184 LEU A CD2 1 
ATOM   1435 N  N   . PRO A 1 182 ? 26.08500  16.50700 53.32800 1.000 16.08883  ? 185 PRO A N   1 
ATOM   1436 C  CA  . PRO A 1 182 ? 26.80900  15.36700 52.75600 1.000 15.97981  ? 185 PRO A CA  1 
ATOM   1437 C  C   . PRO A 1 182 ? 28.15500  15.79600 52.18900 1.000 15.42386  ? 185 PRO A C   1 
ATOM   1438 O  O   . PRO A 1 182 ? 28.48100  16.98600 52.15900 1.000 14.80396  ? 185 PRO A O   1 
ATOM   1439 C  CB  . PRO A 1 182 ? 25.86500  14.86400 51.65100 1.000 12.52529  ? 185 PRO A CB  1 
ATOM   1440 C  CG  . PRO A 1 182 ? 25.14600  16.07100 51.22400 1.000 16.34979  ? 185 PRO A CG  1 
ATOM   1441 C  CD  . PRO A 1 182 ? 24.94100  16.90000 52.49100 1.000 11.03409  ? 185 PRO A CD  1 
ATOM   1442 N  N   . GLU A 1 183 ? 28.92900  14.82700 51.70700 1.000 17.90394  ? 186 GLU A N   1 
ATOM   1443 C  CA  . GLU A 1 183 ? 30.23500  15.13500 51.13800 1.000 14.76857  ? 186 GLU A CA  1 
ATOM   1444 C  C   . GLU A 1 183 ? 30.10000  15.91800 49.83700 1.000 22.19861  ? 186 GLU A C   1 
ATOM   1445 O  O   . GLU A 1 183 ? 30.75300  16.95200 49.65200 1.000 20.22288  ? 186 GLU A O   1 
ATOM   1446 C  CB  . GLU A 1 183 ? 31.00200  13.83700 50.91400 1.000 11.98499  ? 186 GLU A CB  1 
ATOM   1447 C  CG  . GLU A 1 183 ? 32.39400  14.01200 50.39400 1.000 34.39369  ? 186 GLU A CG  1 
ATOM   1448 C  CD  . GLU A 1 183 ? 32.95000  12.70400 49.86900 1.000 38.13041  ? 186 GLU A CD  1 
ATOM   1449 O  OE1 . GLU A 1 183 ? 32.90400  11.70700 50.62200 1.000 26.77386  ? 186 GLU A OE1 1 
ATOM   1450 O  OE2 . GLU A 1 183 ? 33.40000  12.67700 48.70100 1.000 28.72027  ? 186 GLU A OE2 1 
ATOM   1451 N  N   . SER A 1 184 ? 29.26700  15.43600 48.92200 1.000 12.08312  ? 187 SER A N   1 
ATOM   1452 C  CA  . SER A 1 184 ? 29.06700  16.10200 47.64400 1.000 15.39188  ? 187 SER A CA  1 
ATOM   1453 C  C   . SER A 1 184 ? 27.90200  17.07900 47.70700 1.000 18.65070  ? 187 SER A C   1 
ATOM   1454 O  O   . SER A 1 184 ? 26.93300  16.87500 48.44600 1.000 18.33101  ? 187 SER A O   1 
ATOM   1455 C  CB  . SER A 1 184 ? 28.80300  15.08500 46.53700 1.000 22.43870  ? 187 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 184 ? 28.32100  15.73600 45.37200 1.000 19.57930  ? 187 SER A OG  1 
ATOM   1457 N  N   . LEU A 1 185 ? 27.99400  18.13300 46.89000 1.000 13.05959  ? 188 LEU A N   1 
ATOM   1458 C  CA  . LEU A 1 185 ? 26.93800  19.12700 46.74500 1.000 12.33425  ? 188 LEU A CA  1 
ATOM   1459 C  C   . LEU A 1 185 ? 26.24200  19.06700 45.38200 1.000 15.25272  ? 188 LEU A C   1 
ATOM   1460 O  O   . LEU A 1 185 ? 25.58400  20.03600 44.99100 1.000 19.47014  ? 188 LEU A O   1 
ATOM   1461 C  CB  . LEU A 1 185 ? 27.49500  20.53500 46.98000 1.000 22.16461  ? 188 LEU A CB  1 
ATOM   1462 C  CG  . LEU A 1 185 ? 27.96200  20.90500 48.38600 1.000 27.58776  ? 188 LEU A CG  1 
ATOM   1463 C  CD1 . LEU A 1 185 ? 28.17000  22.41500 48.50100 1.000 25.18587  ? 188 LEU A CD1 1 
ATOM   1464 C  CD2 . LEU A 1 185 ? 26.99400  20.42000 49.43800 1.000 21.87246  ? 188 LEU A CD2 1 
ATOM   1465 N  N   . ASP A 1 186 ? 26.37700  17.96000 44.64700 1.000 17.01546  ? 189 ASP A N   1 
ATOM   1466 C  CA  . ASP A 1 186 ? 25.60700  17.78800 43.42300 1.000 16.92431  ? 189 ASP A CA  1 
ATOM   1467 C  C   . ASP A 1 186 ? 24.11600  17.80600 43.74600 1.000 20.81052  ? 189 ASP A C   1 
ATOM   1468 O  O   . ASP A 1 186 ? 23.68400  17.30800 44.78800 1.000 13.23055  ? 189 ASP A O   1 
ATOM   1469 C  CB  . ASP A 1 186 ? 25.96400  16.47100 42.73200 1.000 17.57181  ? 189 ASP A CB  1 
ATOM   1470 C  CG  . ASP A 1 186 ? 27.40600  16.42500 42.23700 1.000 22.83394  ? 189 ASP A CG  1 
ATOM   1471 O  OD1 . ASP A 1 186 ? 28.01500  17.49000 42.02300 1.000 26.85722  ? 189 ASP A OD1 1 
ATOM   1472 O  OD2 . ASP A 1 186 ? 27.91600  15.30600 42.04600 1.000 26.88518  ? 189 ASP A OD2 1 
ATOM   1473 N  N   . TYR A 1 187 ? 23.31800  18.37300 42.83700 1.000 13.38360  ? 190 TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 187 ? 21.92300  18.61900 43.16500 1.000 9.41192   ? 190 TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 187 ? 21.04600  18.56800 41.92000 1.000 17.13633  ? 190 TYR A C   1 
ATOM   1476 O  O   . TYR A 1 187 ? 21.51500  18.69400 40.78600 1.000 12.06413  ? 190 TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 187 ? 21.74600  19.98400 43.84600 1.000 9.02912   ? 190 TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 187 ? 22.17100  21.16100 42.98100 1.000 10.92771  ? 190 TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 187 ? 21.27400  21.77200 42.10000 1.000 12.05573  ? 190 TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 187 ? 23.47100  21.66300 43.04700 1.000 15.99069  ? 190 TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 187 ? 21.66600  22.85600 41.30500 1.000 14.09817  ? 190 TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 187 ? 23.87000  22.75400 42.26200 1.000 16.85900  ? 190 TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 187 ? 22.96800  23.33400 41.39600 1.000 16.94516  ? 190 TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 187 ? 23.36100  24.40000 40.62800 1.000 15.22767  ? 190 TYR A OH  1 
ATOM   1485 N  N   . TRP A 1 188 ? 19.76300  18.37200 42.16700 1.000 11.37084  ? 191 TRP A N   1 
ATOM   1486 C  CA  . TRP A 1 188 ? 18.67800  18.66700 41.24300 1.000 10.57803  ? 191 TRP A CA  1 
ATOM   1487 C  C   . TRP A 1 188 ? 17.99700  19.96300 41.68100 1.000 12.04811  ? 191 TRP A C   1 
ATOM   1488 O  O   . TRP A 1 188 ? 17.96300  20.29000 42.86900 1.000 13.33358  ? 191 TRP A O   1 
ATOM   1489 C  CB  . TRP A 1 188 ? 17.64500  17.54200 41.24400 1.000 11.13473  ? 191 TRP A CB  1 
ATOM   1490 C  CG  . TRP A 1 188 ? 18.12400  16.18200 40.83500 1.000 9.71909   ? 191 TRP A CG  1 
ATOM   1491 C  CD1 . TRP A 1 188 ? 18.34700  15.74300 39.55600 1.000 12.99065  ? 191 TRP A CD1 1 
ATOM   1492 C  CD2 . TRP A 1 188 ? 18.34800  15.05300 41.69100 1.000 13.47246  ? 191 TRP A CD2 1 
ATOM   1493 N  NE1 . TRP A 1 188 ? 18.72300  14.42700 39.57100 1.000 16.62797  ? 191 TRP A NE1 1 
ATOM   1494 C  CE2 . TRP A 1 188 ? 18.73400  13.97700 40.86800 1.000 15.61021  ? 191 TRP A CE2 1 
ATOM   1495 C  CE3 . TRP A 1 188 ? 18.27100  14.85300 43.07700 1.000 14.48626  ? 191 TRP A CE3 1 
ATOM   1496 C  CZ2 . TRP A 1 188 ? 19.04900  12.71100 41.38200 1.000 14.48731  ? 191 TRP A CZ2 1 
ATOM   1497 C  CZ3 . TRP A 1 188 ? 18.57800  13.59600 43.58900 1.000 13.66513  ? 191 TRP A CZ3 1 
ATOM   1498 C  CH2 . TRP A 1 188 ? 18.96600  12.54200 42.74300 1.000 14.51284  ? 191 TRP A CH2 1 
ATOM   1499 N  N   . THR A 1 189 ? 17.41500  20.68600 40.73000 1.000 10.79797  ? 192 THR A N   1 
ATOM   1500 C  CA  . THR A 1 189 ? 16.68900  21.90300 41.08400 1.000 11.96453  ? 192 THR A CA  1 
ATOM   1501 C  C   . THR A 1 189 ? 15.42900  22.03200 40.23800 1.000 11.41236  ? 192 THR A C   1 
ATOM   1502 O  O   . THR A 1 189 ? 15.38900  21.60400 39.08500 1.000 11.58139  ? 192 THR A O   1 
ATOM   1503 C  CB  . THR A 1 189 ? 17.57300  23.15600 40.93700 1.000 10.84564  ? 192 THR A CB  1 
ATOM   1504 O  OG1 . THR A 1 189 ? 16.83900  24.31400 41.36700 1.000 11.39855  ? 192 THR A OG1 1 
ATOM   1505 C  CG2 . THR A 1 189 ? 18.01900  23.34100 39.50500 1.000 17.36426  ? 192 THR A CG2 1 
ATOM   1506 N  N   . TYR A 1 190 ? 14.38100  22.60100 40.83600 1.000 9.80205   ? 193 TYR A N   1 
ATOM   1507 C  CA  . TYR A 1 190 ? 13.12900  22.84800 40.13400 1.000 9.65287   ? 193 TYR A CA  1 
ATOM   1508 C  C   . TYR A 1 190 ? 12.34300  23.90000 40.91600 1.000 10.94228  ? 193 TYR A C   1 
ATOM   1509 O  O   . TYR A 1 190 ? 12.59800  24.10700 42.10700 1.000 12.28331  ? 193 TYR A O   1 
ATOM   1510 C  CB  . TYR A 1 190 ? 12.31300  21.55300 39.97400 1.000 9.25523   ? 193 TYR A CB  1 
ATOM   1511 C  CG  . TYR A 1 190 ? 11.59500  21.13600 41.23000 1.000 12.15472  ? 193 TYR A CG  1 
ATOM   1512 C  CD1 . TYR A 1 190 ? 12.25200  20.42500 42.22600 1.000 11.39479  ? 193 TYR A CD1 1 
ATOM   1513 C  CD2 . TYR A 1 190 ? 10.26500  21.47300 41.43000 1.000 8.87052   ? 193 TYR A CD2 1 
ATOM   1514 C  CE1 . TYR A 1 190 ? 11.59100  20.04500 43.39200 1.000 9.03344   ? 193 TYR A CE1 1 
ATOM   1515 C  CE2 . TYR A 1 190 ? 9.60200   21.11100 42.58600 1.000 10.55268  ? 193 TYR A CE2 1 
ATOM   1516 C  CZ  . TYR A 1 190 ? 10.26600  20.40300 43.56000 1.000 8.13146   ? 193 TYR A CZ  1 
ATOM   1517 O  OH  . TYR A 1 190 ? 9.59400   20.05600 44.69200 1.000 12.21796  ? 193 TYR A OH  1 
ATOM   1518 N  N   . PRO A 1 191 ? 11.41700  24.61500 40.25800 1.000 9.96391   ? 194 PRO A N   1 
ATOM   1519 C  CA  . PRO A 1 191 ? 10.61600  25.62100 40.97300 1.000 10.01503  ? 194 PRO A CA  1 
ATOM   1520 C  C   . PRO A 1 191 ? 9.39100   25.00100 41.62500 1.000 8.42521   ? 194 PRO A C   1 
ATOM   1521 O  O   . PRO A 1 191 ? 8.65300   24.24800 40.98100 1.000 8.76963   ? 194 PRO A O   1 
ATOM   1522 C  CB  . PRO A 1 191 ? 10.21800  26.61100 39.86600 1.000 12.29552  ? 194 PRO A CB  1 
ATOM   1523 C  CG  . PRO A 1 191 ? 10.18400  25.78700 38.62700 1.000 16.86693  ? 194 PRO A CG  1 
ATOM   1524 C  CD  . PRO A 1 191 ? 11.26100  24.72400 38.79100 1.000 14.94383  ? 194 PRO A CD  1 
ATOM   1525 N  N   . GLY A 1 192 ? 9.13400   25.32700 42.87800 1.000 8.42338   ? 195 GLY A N   1 
ATOM   1526 C  CA  . GLY A 1 192 ? 8.13900   24.60900 43.65500 1.000 6.95925   ? 195 GLY A CA  1 
ATOM   1527 C  C   . GLY A 1 192 ? 7.50000   25.49400 44.69400 1.000 7.89109   ? 195 GLY A C   1 
ATOM   1528 O  O   . GLY A 1 192 ? 7.45500   26.71800 44.54300 1.000 10.99696  ? 195 GLY A O   1 
ATOM   1529 N  N   . SER A 1 193 ? 7.01800   24.86200 45.75900 1.000 11.18873  ? 196 SER A N   1 
ATOM   1530 C  CA  . SER A 1 193 ? 6.19800   25.50700 46.77600 1.000 12.36291  ? 196 SER A CA  1 
ATOM   1531 C  C   . SER A 1 193 ? 6.66700   25.10000 48.16700 1.000 12.70335  ? 196 SER A C   1 
ATOM   1532 O  O   . SER A 1 193 ? 7.45100   24.16400 48.33200 1.000 13.21409  ? 196 SER A O   1 
ATOM   1533 C  CB  . SER A 1 193 ? 4.72200   25.11900 46.61400 1.000 11.89606  ? 196 SER A CB  1 
ATOM   1534 O  OG  . SER A 1 193 ? 4.49000   23.80900 47.13600 1.000 13.17571  ? 196 SER A OG  1 
ATOM   1535 N  N   . LEU A 1 194 ? 6.16400   25.80300 49.18000 1.000 8.80484   ? 197 LEU A N   1 
ATOM   1536 C  CA  . LEU A 1 194 ? 6.18500   25.25000 50.53200 1.000 8.56671   ? 197 LEU A CA  1 
ATOM   1537 C  C   . LEU A 1 194 ? 5.42300   23.92800 50.53600 1.000 10.39700  ? 197 LEU A C   1 
ATOM   1538 O  O   . LEU A 1 194 ? 4.47400   23.73000 49.76900 1.000 10.45818  ? 197 LEU A O   1 
ATOM   1539 C  CB  . LEU A 1 194 ? 5.57600   26.22900 51.53800 1.000 12.08876  ? 197 LEU A CB  1 
ATOM   1540 C  CG  . LEU A 1 194 ? 6.21000   27.62100 51.59600 1.000 12.95230  ? 197 LEU A CG  1 
ATOM   1541 C  CD1 . LEU A 1 194 ? 5.36900   28.55700 52.45200 1.000 16.40700  ? 197 LEU A CD1 1 
ATOM   1542 C  CD2 . LEU A 1 194 ? 7.63500   27.54300 52.12200 1.000 13.53069  ? 197 LEU A CD2 1 
ATOM   1543 N  N   . THR A 1 195 ? 5.84100   22.99800 51.38500 1.000 8.85109   ? 198 THR A N   1 
ATOM   1544 C  CA  . THR A 1 195 ? 5.12600   21.72800 51.43000 1.000 6.62316   ? 198 THR A CA  1 
ATOM   1545 C  C   . THR A 1 195 ? 4.14900   21.64900 52.59300 1.000 8.92230   ? 198 THR A C   1 
ATOM   1546 O  O   . THR A 1 195 ? 3.51400   20.61100 52.77700 1.000 9.85182   ? 198 THR A O   1 
ATOM   1547 C  CB  . THR A 1 195 ? 6.09400   20.54200 51.49100 1.000 6.48047   ? 198 THR A CB  1 
ATOM   1548 O  OG1 . THR A 1 195 ? 6.79900   20.56100 52.73900 1.000 10.35531  ? 198 THR A OG1 1 
ATOM   1549 C  CG2 . THR A 1 195 ? 7.08000   20.54800 50.29000 1.000 10.70116  ? 198 THR A CG2 1 
ATOM   1550 N  N   . THR A 1 196 ? 4.02300   22.70500 53.38100 1.000 11.74861  ? 199 THR A N   1 
ATOM   1551 C  CA  . THR A 1 196 ? 2.96400   22.84300 54.36300 1.000 10.57157  ? 199 THR A CA  1 
ATOM   1552 C  C   . THR A 1 196 ? 2.16500   24.10600 54.06600 1.000 13.05275  ? 199 THR A C   1 
ATOM   1553 O  O   . THR A 1 196 ? 2.66600   25.02900 53.41000 1.000 12.03354  ? 199 THR A O   1 
ATOM   1554 C  CB  . THR A 1 196 ? 3.54700   22.91800 55.78100 1.000 12.73844  ? 199 THR A CB  1 
ATOM   1555 O  OG1 . THR A 1 196 ? 4.51700   23.98300 55.83600 1.000 13.96533  ? 199 THR A OG1 1 
ATOM   1556 C  CG2 . THR A 1 196 ? 4.23700   21.59400 56.11900 1.000 12.55140  ? 199 THR A CG2 1 
ATOM   1557 N  N   . PRO A 1 197 ? 0.91800   24.17600 54.52100 1.000 11.94903  ? 200 PRO A N   1 
ATOM   1558 C  CA  . PRO A 1 197 ? 0.17200   25.43400 54.41500 1.000 16.79375  ? 200 PRO A CA  1 
ATOM   1559 C  C   . PRO A 1 197 ? 0.98800   26.58400 54.97600 1.000 13.74293  ? 200 PRO A C   1 
ATOM   1560 O  O   . PRO A 1 197 ? 1.66000   26.43600 56.01200 1.000 15.91966  ? 200 PRO A O   1 
ATOM   1561 C  CB  . PRO A 1 197 ? -1.08600  25.16400 55.25600 1.000 12.34204  ? 200 PRO A CB  1 
ATOM   1562 C  CG  . PRO A 1 197 ? -1.31700  23.69400 55.05600 1.000 16.42422  ? 200 PRO A CG  1 
ATOM   1563 C  CD  . PRO A 1 197 ? 0.08600   23.08900 55.06500 1.000 13.27546  ? 200 PRO A CD  1 
ATOM   1564 N  N   . PRO A 1 198 ? 1.03000   27.75400 54.28500 1.000 16.65976  ? 201 PRO A N   1 
ATOM   1565 C  CA  . PRO A 1 198 ? 0.09500   28.09600 53.20700 1.000 12.66045  ? 201 PRO A CA  1 
ATOM   1566 C  C   . PRO A 1 198 ? 0.38100   27.60600 51.76200 1.000 16.11236  ? 201 PRO A C   1 
ATOM   1567 O  O   . PRO A 1 198 ? -0.33600  28.04400 50.85200 1.000 16.44580  ? 201 PRO A O   1 
ATOM   1568 C  CB  . PRO A 1 198 ? 0.09300   29.63000 53.28300 1.000 15.64485  ? 201 PRO A CB  1 
ATOM   1569 C  CG  . PRO A 1 198 ? 1.49800   29.99100 53.66300 1.000 16.66899  ? 201 PRO A CG  1 
ATOM   1570 C  CD  . PRO A 1 198 ? 1.95500   28.85800 54.55000 1.000 16.43162  ? 201 PRO A CD  1 
ATOM   1571 N  N   . LEU A 1 199 ? 1.41100   26.77400 51.56000 1.000 13.19849  ? 202 LEU A N   1 
ATOM   1572 C  CA  . LEU A 1 199 ? 1.70000   26.13000 50.24200 1.000 11.75849  ? 202 LEU A CA  1 
ATOM   1573 C  C   . LEU A 1 199 ? 2.00600   27.14600 49.12700 1.000 8.31194   ? 202 LEU A C   1 
ATOM   1574 O  O   . LEU A 1 199 ? 1.78600   26.82400 47.96900 1.000 12.77156  ? 202 LEU A O   1 
ATOM   1575 C  CB  . LEU A 1 199 ? 0.55200   25.20700 49.84600 1.000 15.42033  ? 202 LEU A CB  1 
ATOM   1576 C  CG  . LEU A 1 199 ? 0.19400   24.11900 50.86000 1.000 15.58534  ? 202 LEU A CG  1 
ATOM   1577 C  CD1 . LEU A 1 199 ? -1.19100  23.58000 50.58000 1.000 19.39546  ? 202 LEU A CD1 1 
ATOM   1578 C  CD2 . LEU A 1 199 ? 1.22300   23.01300 50.82900 1.000 11.93412  ? 202 LEU A CD2 1 
ATOM   1579 N  N   . LEU A 1 200 ? 2.57300   28.27600 49.49900 1.000 10.88760  ? 203 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 200 ? 2.90700   29.34000 48.52800 1.000 11.48236  ? 203 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 200 ? 3.96600   28.86300 47.51800 1.000 10.24117  ? 203 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 200 ? 4.90100   28.18300 47.90900 1.000 12.81003  ? 203 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 200 ? 3.35400   30.58200 49.29400 1.000 9.83833   ? 203 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 200 ? 2.35300   31.12000 50.31900 1.000 17.78340  ? 203 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 200 ? 2.95500   32.22400 51.15800 1.000 18.96103  ? 203 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 200 ? 1.08300   31.59000 49.65400 1.000 17.10655  ? 203 LEU A CD2 1 
ATOM   1587 N  N   . GLU A 1 201 ? 3.77300   29.25300 46.26700 1.000 8.00648   ? 204 GLU A N   1 
ATOM   1588 C  CA  . GLU A 1 201 ? 4.69500   28.86800 45.17600 1.000 11.97161  ? 204 GLU A CA  1 
ATOM   1589 C  C   . GLU A 1 201 ? 5.83000   29.89700 45.10400 1.000 17.29889  ? 204 GLU A C   1 
ATOM   1590 O  O   . GLU A 1 201 ? 5.88000   30.66600 44.14300 1.000 13.84107  ? 204 GLU A O   1 
ATOM   1591 C  CB  . GLU A 1 201 ? 3.77000   28.71900 43.97000 1.000 13.90974  ? 204 GLU A CB  1 
ATOM   1592 C  CG  . GLU A 1 201 ? 2.73200   27.62200 44.18800 1.000 14.90102  ? 204 GLU A CG  1 
ATOM   1593 C  CD  . GLU A 1 201 ? 1.82800   27.33100 43.00400 1.000 13.41549  ? 204 GLU A CD  1 
ATOM   1594 O  OE1 . GLU A 1 201 ? 1.57500   28.27300 42.24400 1.000 12.12270  ? 204 GLU A OE1 1 
ATOM   1595 O  OE2 . GLU A 1 201 ? 1.40300   26.17700 42.84200 1.000 13.68591  ? 204 GLU A OE2 1 
ATOM   1596 N  N   . CYS A 1 202 ? 6.66300   29.90800 46.13500 1.000 9.99385   ? 205 CYS A N   1 
ATOM   1597 C  CA  . CYS A 1 202 ? 7.74700   30.91300 46.23100 1.000 10.08020  ? 205 CYS A CA  1 
ATOM   1598 C  C   . CYS A 1 202 ? 9.11700   30.24400 46.37300 1.000 11.12543  ? 205 CYS A C   1 
ATOM   1599 O  O   . CYS A 1 202 ? 10.04800  30.94400 46.76400 1.000 11.26319  ? 205 CYS A O   1 
ATOM   1600 C  CB  . CYS A 1 202 ? 7.49100   31.76300 47.46300 1.000 11.57397  ? 205 CYS A CB  1 
ATOM   1601 S  SG  . CYS A 1 202 ? 7.35400   30.77100 48.96900 1.000 15.22033  ? 205 CYS A SG  1 
ATOM   1602 N  N   . VAL A 1 203 ? 9.19800   28.94500 46.07600 1.000 11.18552  ? 206 VAL A N   1 
ATOM   1603 C  CA  . VAL A 1 203 ? 10.45200  28.22400 46.42300 1.000 12.00447  ? 206 VAL A CA  1 
ATOM   1604 C  C   . VAL A 1 203 ? 11.25600  27.68300 45.24100 1.000 11.32010  ? 206 VAL A C   1 
ATOM   1605 O  O   . VAL A 1 203 ? 10.66700  27.04300 44.37600 1.000 14.77523  ? 206 VAL A O   1 
ATOM   1606 C  CB  . VAL A 1 203 ? 10.15600  27.05000 47.37900 1.000 12.54593  ? 206 VAL A CB  1 
ATOM   1607 C  CG1 . VAL A 1 203 ? 11.41200  26.26200 47.71300 1.000 12.76542  ? 206 VAL A CG1 1 
ATOM   1608 C  CG2 . VAL A 1 203 ? 9.40600   27.46800 48.63500 1.000 11.64545  ? 206 VAL A CG2 1 
ATOM   1609 N  N   . THR A 1 204 ? 12.53400  28.02900 45.20300 1.000 10.70981  ? 207 THR A N   1 
ATOM   1610 C  CA  . THR A 1 204 ? 13.46600  27.31700 44.33500 1.000 8.05409   ? 207 THR A CA  1 
ATOM   1611 C  C   . THR A 1 204 ? 13.99600  26.13400 45.13300 1.000 10.30180  ? 207 THR A C   1 
ATOM   1612 O  O   . THR A 1 204 ? 14.71600  26.31300 46.12700 1.000 12.01748  ? 207 THR A O   1 
ATOM   1613 C  CB  . THR A 1 204 ? 14.60300  28.22700 43.86800 1.000 13.48574  ? 207 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 204 ? 14.06500  29.32100 43.10300 1.000 10.63274  ? 207 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 204 ? 15.59800  27.44800 43.01700 1.000 14.02059  ? 207 THR A CG2 1 
ATOM   1616 N  N   . TRP A 1 205 ? 13.60400  24.92800 44.73700 1.000 11.02038  ? 208 TRP A N   1 
ATOM   1617 C  CA  . TRP A 1 205 ? 14.05800  23.74200 45.44100 1.000 11.40396  ? 208 TRP A CA  1 
ATOM   1618 C  C   . TRP A 1 205 ? 15.43400  23.32200 44.95300 1.000 10.91775  ? 208 TRP A C   1 
ATOM   1619 O  O   . TRP A 1 205 ? 15.70400  23.30500 43.74900 1.000 12.03028  ? 208 TRP A O   1 
ATOM   1620 C  CB  . TRP A 1 205 ? 13.06400  22.59200 45.26300 1.000 12.45751  ? 208 TRP A CB  1 
ATOM   1621 C  CG  . TRP A 1 205 ? 11.94700  22.71900 46.23200 1.000 10.18640  ? 208 TRP A CG  1 
ATOM   1622 C  CD1 . TRP A 1 205 ? 10.74000  23.31900 46.02200 1.000 9.84354   ? 208 TRP A CD1 1 
ATOM   1623 C  CD2 . TRP A 1 205 ? 11.95700  22.29600 47.60100 1.000 11.72243  ? 208 TRP A CD2 1 
ATOM   1624 N  NE1 . TRP A 1 205 ? 9.98600   23.27400 47.17400 1.000 10.45114  ? 208 TRP A NE1 1 
ATOM   1625 C  CE2 . TRP A 1 205 ? 10.71000  22.64900 48.15600 1.000 10.31352  ? 208 TRP A CE2 1 
ATOM   1626 C  CE3 . TRP A 1 205 ? 12.89700  21.63900 48.41000 1.000 9.84426   ? 208 TRP A CE3 1 
ATOM   1627 C  CZ2 . TRP A 1 205 ? 10.37500  22.36800 49.47900 1.000 10.63653  ? 208 TRP A CZ2 1 
ATOM   1628 C  CZ3 . TRP A 1 205 ? 12.55900  21.36300 49.73400 1.000 11.34663  ? 208 TRP A CZ3 1 
ATOM   1629 C  CH2 . TRP A 1 205 ? 11.30800  21.71800 50.24400 1.000 11.90599  ? 208 TRP A CH2 1 
ATOM   1630 N  N   . ILE A 1 206 ? 16.30000  22.97100 45.90200 1.000 11.20770  ? 209 ILE A N   1 
ATOM   1631 C  CA  . ILE A 1 206 ? 17.64700  22.48500 45.60100 1.000 8.72641   ? 209 ILE A CA  1 
ATOM   1632 C  C   . ILE A 1 206 ? 17.79500  21.19600 46.40100 1.000 13.99245  ? 209 ILE A C   1 
ATOM   1633 O  O   . ILE A 1 206 ? 17.95200  21.23300 47.62300 1.000 11.43065  ? 209 ILE A O   1 
ATOM   1634 C  CB  . ILE A 1 206 ? 18.73300  23.50500 45.95600 1.000 12.60385  ? 209 ILE A CB  1 
ATOM   1635 C  CG1 . ILE A 1 206 ? 18.51400  24.80100 45.16700 1.000 12.92192  ? 209 ILE A CG1 1 
ATOM   1636 C  CG2 . ILE A 1 206 ? 20.10500  22.95700 45.63200 1.000 16.53844  ? 209 ILE A CG2 1 
ATOM   1637 C  CD1 . ILE A 1 206 ? 19.38900  25.94900 45.62600 1.000 17.35333  ? 209 ILE A CD1 1 
ATOM   1638 N  N   . VAL A 1 207 ? 17.69700  20.05400 45.72800 1.000 11.88262  ? 210 VAL A N   1 
ATOM   1639 C  CA  . VAL A 1 207 ? 17.67000  18.75200 46.39100 1.000 14.01385  ? 210 VAL A CA  1 
ATOM   1640 C  C   . VAL A 1 207 ? 18.99300  18.05300 46.11400 1.000 11.21169  ? 210 VAL A C   1 
ATOM   1641 O  O   . VAL A 1 207 ? 19.34900  17.83200 44.95100 1.000 11.83833  ? 210 VAL A O   1 
ATOM   1642 C  CB  . VAL A 1 207 ? 16.48900  17.89100 45.91700 1.000 12.23251  ? 210 VAL A CB  1 
ATOM   1643 C  CG1 . VAL A 1 207 ? 16.54700  16.48500 46.57200 1.000 13.08122  ? 210 VAL A CG1 1 
ATOM   1644 C  CG2 . VAL A 1 207 ? 15.14700  18.58700 46.18900 1.000 11.88219  ? 210 VAL A CG2 1 
ATOM   1645 N  N   . LEU A 1 208 ? 19.71700  17.69900 47.18100 1.000 12.68884  ? 211 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 208 ? 21.04600  17.11300 47.04500 1.000 8.80348   ? 211 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 208 ? 20.93400  15.64000 46.68100 1.000 12.93494  ? 211 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 208 ? 20.09200  14.91800 47.21900 1.000 12.89047  ? 211 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 208 ? 21.84600  17.25700 48.34300 1.000 11.31175  ? 211 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 208 ? 22.17300  18.68200 48.79300 1.000 13.96181  ? 211 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 208 ? 23.26600  18.67300 49.84900 1.000 16.26893  ? 211 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 208 ? 22.60500  19.52600 47.60200 1.000 19.48792  ? 211 LEU A CD2 1 
ATOM   1653 N  N   . LYS A 1 209 ? 21.79900  15.19500 45.77300 1.000 10.07376  ? 212 LYS A N   1 
ATOM   1654 C  CA  . LYS A 1 209 ? 21.76500  13.80800 45.31400 1.000 11.18170  ? 212 LYS A CA  1 
ATOM   1655 C  C   . LYS A 1 209 ? 22.21100  12.84400 46.40800 1.000 11.84404  ? 212 LYS A C   1 
ATOM   1656 O  O   . LYS A 1 209 ? 21.63800  11.76000 46.56900 1.000 13.76213  ? 212 LYS A O   1 
ATOM   1657 C  CB  . LYS A 1 209 ? 22.65200  13.64400 44.07500 1.000 18.99668  ? 212 LYS A CB  1 
ATOM   1658 C  CG  . LYS A 1 209 ? 22.83800  12.19100 43.64400 1.000 24.87159  ? 212 LYS A CG  1 
ATOM   1659 C  CD  . LYS A 1 209 ? 24.05000  11.99500 42.74400 1.000 27.39562  ? 212 LYS A CD  1 
ATOM   1660 C  CE  . LYS A 1 209 ? 23.96600  10.66000 42.01500 1.000 48.59649  ? 212 LYS A CE  1 
ATOM   1661 N  NZ  . LYS A 1 209 ? 25.29500  10.01900 41.82400 1.000 52.12874  ? 212 LYS A NZ  1 
ATOM   1662 N  N   . GLU A 1 210 ? 23.23600  13.22000 47.17000 1.000 11.32858  ? 213 GLU A N   1 
ATOM   1663 C  CA  . GLU A 1 210 ? 23.82200  12.30900 48.15100 1.000 13.36442  ? 213 GLU A CA  1 
ATOM   1664 C  C   . GLU A 1 210 ? 23.07900  12.39400 49.48000 1.000 13.28546  ? 213 GLU A C   1 
ATOM   1665 O  O   . GLU A 1 210 ? 23.05900  13.47000 50.09900 1.000 11.12748  ? 213 GLU A O   1 
ATOM   1666 C  CB  . GLU A 1 210 ? 25.29500  12.62900 48.36400 1.000 12.05157  ? 213 GLU A CB  1 
ATOM   1667 C  CG  . GLU A 1 210 ? 25.95500  11.73600 49.39400 1.000 16.93797  ? 213 GLU A CG  1 
ATOM   1668 C  CD  . GLU A 1 210 ? 27.39600  12.16100 49.70200 1.000 29.53667  ? 213 GLU A CD  1 
ATOM   1669 O  OE1 . GLU A 1 210 ? 28.02000  12.84100 48.86400 1.000 23.24381  ? 213 GLU A OE1 1 
ATOM   1670 O  OE2 . GLU A 1 210 ? 27.90300  11.82400 50.79100 1.000 33.29666  ? 213 GLU A OE2 1 
ATOM   1671 N  N   . PRO A 1 211 ? 22.48300  11.31100 49.96600 1.000 12.47687  ? 214 PRO A N   1 
ATOM   1672 C  CA  . PRO A 1 211 ? 21.86300  11.34000 51.29800 1.000 10.09640  ? 214 PRO A CA  1 
ATOM   1673 C  C   . PRO A 1 211 ? 22.91700  11.28700 52.40000 1.000 14.42812  ? 214 PRO A C   1 
ATOM   1674 O  O   . PRO A 1 211 ? 24.08200  10.94800 52.17400 1.000 18.67745  ? 214 PRO A O   1 
ATOM   1675 C  CB  . PRO A 1 211 ? 20.97400  10.08800 51.31700 1.000 14.59592  ? 214 PRO A CB  1 
ATOM   1676 C  CG  . PRO A 1 211 ? 21.54000  9.17900  50.26600 1.000 24.30555  ? 214 PRO A CG  1 
ATOM   1677 C  CD  . PRO A 1 211 ? 22.31800  10.01300 49.28200 1.000 14.90814  ? 214 PRO A CD  1 
ATOM   1678 N  N   . ILE A 1 212 ? 22.49600  11.66500 53.60800 1.000 13.70355  ? 215 ILE A N   1 
ATOM   1679 C  CA  . ILE A 1 212 ? 23.31700  11.46000 54.79600 1.000 12.80031  ? 215 ILE A CA  1 
ATOM   1680 C  C   . ILE A 1 212 ? 22.75500  10.26400 55.54500 1.000 12.62599  ? 215 ILE A C   1 
ATOM   1681 O  O   . ILE A 1 212 ? 21.57400  9.92400  55.41800 1.000 16.04585  ? 215 ILE A O   1 
ATOM   1682 C  CB  . ILE A 1 212 ? 23.39400  12.70500 55.71000 1.000 16.39877  ? 215 ILE A CB  1 
ATOM   1683 C  CG1 . ILE A 1 212 ? 22.00300  13.11100 56.21100 1.000 14.19289  ? 215 ILE A CG1 1 
ATOM   1684 C  CG2 . ILE A 1 212 ? 24.07100  13.87700 54.98100 1.000 15.19463  ? 215 ILE A CG2 1 
ATOM   1685 C  CD1 . ILE A 1 212 ? 22.04900  14.01400 57.43600 1.000 15.62195  ? 215 ILE A CD1 1 
ATOM   1686 N  N   . SER A 1 213 ? 23.61900  9.60400  56.31100 1.000 17.71245  ? 216 SER A N   1 
ATOM   1687 C  CA  A SER A 1 213 ? 23.23500  8.45800  57.12000 0.470 20.58257  ? 216 SER A CA  1 
ATOM   1688 C  CA  B SER A 1 213 ? 23.24500  8.45400  57.12200 0.530 20.60233  ? 216 SER A CA  1 
ATOM   1689 C  C   . SER A 1 213 ? 22.99100  8.89100  58.55900 1.000 17.15475  ? 216 SER A C   1 
ATOM   1690 O  O   . SER A 1 213 ? 23.74100  9.70300  59.11000 1.000 20.77108  ? 216 SER A O   1 
ATOM   1691 C  CB  A SER A 1 213 ? 24.31900  7.37600  57.07600 0.470 25.18030  ? 216 SER A CB  1 
ATOM   1692 C  CB  B SER A 1 213 ? 24.35000  7.39300  57.08500 0.530 25.18487  ? 216 SER A CB  1 
ATOM   1693 O  OG  A SER A 1 213 ? 24.46900  6.86800  55.76100 0.470 20.60638  ? 216 SER A OG  1 
ATOM   1694 O  OG  B SER A 1 213 ? 23.96800  6.22000  57.78200 0.530 21.56200  ? 216 SER A OG  1 
ATOM   1695 N  N   . VAL A 1 214 ? 21.91500  8.36400  59.15600 1.000 14.64062  ? 217 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 214 ? 21.62400  8.53500  60.57400 1.000 18.43337  ? 217 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 214 ? 21.35600  7.14800  61.14000 1.000 13.44980  ? 217 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 214 ? 21.00100  6.21700  60.41400 1.000 18.08884  ? 217 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 214 ? 20.42800  9.48200  60.85400 1.000 21.34480  ? 217 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 214 ? 20.67400  10.84700 60.20900 1.000 19.97441  ? 217 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 214 ? 19.10600  8.85500  60.38600 1.000 18.41490  ? 217 VAL A CG2 1 
ATOM   1702 N  N   . SER A 1 215 ? 21.55300  7.00200  62.44400 1.000 19.85812  ? 218 SER A N   1 
ATOM   1703 C  CA  . SER A 1 215 ? 21.34300  5.67400  62.99900 1.000 21.35606  ? 218 SER A CA  1 
ATOM   1704 C  C   . SER A 1 215 ? 19.86900  5.43500  63.31300 1.000 18.89868  ? 218 SER A C   1 
ATOM   1705 O  O   . SER A 1 215 ? 19.06400  6.36300  63.45200 1.000 17.36450  ? 218 SER A O   1 
ATOM   1706 C  CB  . SER A 1 215 ? 22.17600  5.46700  64.25700 1.000 16.87433  ? 218 SER A CB  1 
ATOM   1707 O  OG  . SER A 1 215 ? 21.75200  6.35100  65.26300 1.000 16.51860  ? 218 SER A OG  1 
ATOM   1708 N  N   . SER A 1 216 ? 19.52200  4.15200  63.42200 1.000 16.05633  ? 219 SER A N   1 
ATOM   1709 C  CA  . SER A 1 216 ? 18.17200  3.79300  63.83100 1.000 16.91901  ? 219 SER A CA  1 
ATOM   1710 C  C   . SER A 1 216 ? 17.78100  4.50100  65.12100 1.000 21.62912  ? 219 SER A C   1 
ATOM   1711 O  O   . SER A 1 216 ? 16.65300  4.99400  65.24600 1.000 19.23096  ? 219 SER A O   1 
ATOM   1712 C  CB  . SER A 1 216 ? 18.06200  2.27700  63.99800 1.000 21.30850  ? 219 SER A CB  1 
ATOM   1713 O  OG  . SER A 1 216 ? 16.70700  1.90900  64.12200 1.000 30.59638  ? 219 SER A OG  1 
ATOM   1714 N  N   . GLU A 1 217 ? 18.71200  4.58200  66.08300 1.000 16.61928  ? 220 GLU A N   1 
ATOM   1715 C  CA  . GLU A 1 217 ? 18.41300  5.20200  67.37600 1.000 19.28503  ? 220 GLU A CA  1 
ATOM   1716 C  C   . GLU A 1 217 ? 18.12400  6.68800  67.23400 1.000 16.06743  ? 220 GLU A C   1 
ATOM   1717 O  O   . GLU A 1 217 ? 17.29900  7.23900  67.97400 1.000 16.75244  ? 220 GLU A O   1 
ATOM   1718 C  CB  . GLU A 1 217 ? 19.57300  5.00700  68.34900 1.000 21.00633  ? 220 GLU A CB  1 
ATOM   1719 C  CG  . GLU A 1 217 ? 19.77000  3.57900  68.83500 1.000 24.62437  ? 220 GLU A CG  1 
ATOM   1720 C  CD  . GLU A 1 217 ? 20.56900  2.72900  67.86500 1.000 25.06289  ? 220 GLU A CD  1 
ATOM   1721 O  OE1 . GLU A 1 217 ? 20.87400  3.20100  66.75100 1.000 26.71464  ? 220 GLU A OE1 1 
ATOM   1722 O  OE2 . GLU A 1 217 ? 20.89400  1.57700  68.22100 1.000 51.07441  ? 220 GLU A OE2 1 
ATOM   1723 N  N   . GLN A 1 218 ? 18.82400  7.36000  66.31600 1.000 14.54374  ? 221 GLN A N   1 
ATOM   1724 C  CA  . GLN A 1 218 ? 18.60000  8.78600  66.12000 1.000 12.68374  ? 221 GLN A CA  1 
ATOM   1725 C  C   . GLN A 1 218 ? 17.20300  9.04900  65.56700 1.000 14.34163  ? 221 GLN A C   1 
ATOM   1726 O  O   . GLN A 1 218 ? 16.47100  9.89400  66.08700 1.000 15.96423  ? 221 GLN A O   1 
ATOM   1727 C  CB  . GLN A 1 218 ? 19.68900  9.36000  65.20500 1.000 15.12122  ? 221 GLN A CB  1 
ATOM   1728 C  CG  . GLN A 1 218 ? 21.05200  9.37900  65.88600 1.000 15.01025  ? 221 GLN A CG  1 
ATOM   1729 C  CD  . GLN A 1 218 ? 22.15400  9.97200  65.02100 1.000 13.36436  ? 221 GLN A CD  1 
ATOM   1730 O  OE1 . GLN A 1 218 ? 22.28900  9.62800  63.85100 1.000 18.23463  ? 221 GLN A OE1 1 
ATOM   1731 N  NE2 . GLN A 1 218 ? 22.95300  10.85800 65.60500 1.000 16.50208  ? 221 GLN A NE2 1 
ATOM   1732 N  N   . VAL A 1 219 ? 16.78700  8.29800  64.54400 1.000 16.37309  ? 222 VAL A N   1 
ATOM   1733 C  CA  . VAL A 1 219 ? 15.46200  8.56700  63.99000 1.000 14.54194  ? 222 VAL A CA  1 
ATOM   1734 C  C   . VAL A 1 219 ? 14.36900  8.10700  64.95600 1.000 18.32894  ? 222 VAL A C   1 
ATOM   1735 O  O   . VAL A 1 219 ? 13.28600  8.70000  64.99600 1.000 16.88650  ? 222 VAL A O   1 
ATOM   1736 C  CB  . VAL A 1 219 ? 15.30500  7.94300  62.58900 1.000 23.94140  ? 222 VAL A CB  1 
ATOM   1737 C  CG1 . VAL A 1 219 ? 15.36100  6.43000  62.64800 1.000 30.74092  ? 222 VAL A CG1 1 
ATOM   1738 C  CG2 . VAL A 1 219 ? 13.99700  8.39500  61.96000 1.000 19.03908  ? 222 VAL A CG2 1 
ATOM   1739 N  N   . LEU A 1 220 ? 14.64200  7.08500  65.77800 1.000 17.06724  ? 223 LEU A N   1 
ATOM   1740 C  CA  . LEU A 1 220 ? 13.66600  6.67200  66.78500 1.000 20.62981  ? 223 LEU A CA  1 
ATOM   1741 C  C   . LEU A 1 220 ? 13.27100  7.83300  67.69400 1.000 16.29514  ? 223 LEU A C   1 
ATOM   1742 O  O   . LEU A 1 220 ? 12.09600  7.98500  68.03900 1.000 18.79357  ? 223 LEU A O   1 
ATOM   1743 C  CB  . LEU A 1 220 ? 14.21200  5.51300  67.61800 1.000 24.12552  ? 223 LEU A CB  1 
ATOM   1744 C  CG  . LEU A 1 220 ? 14.01800  4.10400  67.06400 1.000 31.40866  ? 223 LEU A CG  1 
ATOM   1745 C  CD1 . LEU A 1 220 ? 14.53100  3.07600  68.07400 1.000 36.06514  ? 223 LEU A CD1 1 
ATOM   1746 C  CD2 . LEU A 1 220 ? 12.55300  3.84900  66.73500 1.000 35.66717  ? 223 LEU A CD2 1 
ATOM   1747 N  N   . LYS A 1 221 ? 14.23500  8.67100  68.07600 1.000 15.27478  ? 224 LYS A N   1 
ATOM   1748 C  CA  . LYS A 1 221 ? 13.94200  9.79400  68.96000 1.000 17.58088  ? 224 LYS A CA  1 
ATOM   1749 C  C   . LYS A 1 221 ? 13.05000  10.84300 68.29600 1.000 16.98203  ? 224 LYS A C   1 
ATOM   1750 O  O   . LYS A 1 221 ? 12.23600  11.46900 68.98300 1.000 18.17117  ? 224 LYS A O   1 
ATOM   1751 C  CB  . LYS A 1 221 ? 15.24200  10.43600 69.44000 1.000 16.37865  ? 224 LYS A CB  1 
ATOM   1752 C  CG  . LYS A 1 221 ? 16.18800  9.47400  70.16200 1.000 37.29240  ? 224 LYS A CG  1 
ATOM   1753 C  CD  . LYS A 1 221 ? 16.05800  9.56600  71.67000 1.000 44.79951  ? 224 LYS A CD  1 
ATOM   1754 C  CE  . LYS A 1 221 ? 17.41600  9.77300  72.33200 1.000 45.57469  ? 224 LYS A CE  1 
ATOM   1755 N  NZ  . LYS A 1 221 ? 18.22200  8.52500  72.43100 1.000 42.94279  ? 224 LYS A NZ  1 
ATOM   1756 N  N   . PHE A 1 222 ? 13.18400  11.05200 66.97600 1.000 15.33028  ? 225 PHE A N   1 
ATOM   1757 C  CA  . PHE A 1 222 ? 12.23700  11.90800 66.25700 1.000 14.90964  ? 225 PHE A CA  1 
ATOM   1758 C  C   . PHE A 1 222 ? 10.80800  11.46700 66.51300 1.000 12.33019  ? 225 PHE A C   1 
ATOM   1759 O  O   . PHE A 1 222 ? 9.91300   12.29100 66.70800 1.000 15.02205  ? 225 PHE A O   1 
ATOM   1760 C  CB  . PHE A 1 222 ? 12.46700  11.85600 64.74100 1.000 14.82376  ? 225 PHE A CB  1 
ATOM   1761 C  CG  . PHE A 1 222 ? 13.67300  12.61900 64.25300 1.000 12.77127  ? 225 PHE A CG  1 
ATOM   1762 C  CD1 . PHE A 1 222 ? 14.68100  13.01000 65.11300 1.000 21.36276  ? 225 PHE A CD1 1 
ATOM   1763 C  CD2 . PHE A 1 222 ? 13.78600  12.93500 62.90900 1.000 21.80951  ? 225 PHE A CD2 1 
ATOM   1764 C  CE1 . PHE A 1 222 ? 15.78000  13.70200 64.63700 1.000 21.06958  ? 225 PHE A CE1 1 
ATOM   1765 C  CE2 . PHE A 1 222 ? 14.87700  13.63200 62.43000 1.000 22.52556  ? 225 PHE A CE2 1 
ATOM   1766 C  CZ  . PHE A 1 222 ? 15.87400  14.02100 63.29100 1.000 15.48512  ? 225 PHE A CZ  1 
ATOM   1767 N  N   . ARG A 1 223 ? 10.60247  10.15752 66.47143 1.000 14.76591  ? 226 ARG A N   1 
ATOM   1768 C  CA  . ARG A 1 223 ? 9.23420   9.58734  66.57212 1.000 15.91476  ? 226 ARG A CA  1 
ATOM   1769 C  C   . ARG A 1 223 ? 8.62149   9.62119  67.98604 1.000 18.38846  ? 226 ARG A C   1 
ATOM   1770 O  O   . ARG A 1 223 ? 7.50314   9.12705  68.13899 1.000 20.18653  ? 226 ARG A O   1 
ATOM   1771 C  CB  . ARG A 1 223 ? 9.33817   8.14641  66.07851 1.000 11.86847  ? 226 ARG A CB  1 
ATOM   1772 C  CG  . ARG A 1 223 ? 9.82175   7.98231  64.64539 1.000 11.23195  ? 226 ARG A CG  1 
ATOM   1773 C  CD  . ARG A 1 223 ? 9.88543   6.52809  64.20992 1.000 16.20609  ? 226 ARG A CD  1 
ATOM   1774 N  NE  . ARG A 1 223 ? 10.39665  6.40120  62.84187 1.000 13.77631  ? 226 ARG A NE  1 
ATOM   1775 C  CZ  . ARG A 1 223 ? 11.28292  5.50986  62.42543 1.000 20.38943  ? 226 ARG A CZ  1 
ATOM   1776 N  NH1 . ARG A 1 223 ? 11.76222  4.60744  63.25888 1.000 22.42089  ? 226 ARG A NH1 1 
ATOM   1777 N  NH2 . ARG A 1 223 ? 11.68920  5.52251  61.17241 1.000 19.05047  ? 226 ARG A NH2 1 
ATOM   1778 N  N   . LYS A 1 224 ? 9.35017   10.14282 68.96228 1.000 14.71102  ? 227 LYS A N   1 
ATOM   1779 C  CA  . LYS A 1 224 ? 8.82036   10.21651 70.34573 1.000 15.67630  ? 227 LYS A CA  1 
ATOM   1780 C  C   . LYS A 1 224 ? 8.18157   11.59168 70.57335 1.000 16.11022  ? 227 LYS A C   1 
ATOM   1781 O  O   . LYS A 1 224 ? 7.54662   11.80040 71.60362 1.000 18.35375  ? 227 LYS A O   1 
ATOM   1782 C  CB  . LYS A 1 224 ? 9.92630   9.89930  71.35175 1.000 18.78284  ? 227 LYS A CB  1 
ATOM   1783 C  CG  . LYS A 1 224 ? 10.36661  8.44861  71.34402 1.000 30.72638  ? 227 LYS A CG  1 
ATOM   1784 C  CD  . LYS A 1 224 ? 11.45029  8.12619  72.36350 1.000 47.21670  ? 227 LYS A CD  1 
ATOM   1785 C  CE  . LYS A 1 224 ? 11.11418  8.64109  73.72553 1.000 69.51333  ? 227 LYS A CE  1 
ATOM   1786 N  NZ  . LYS A 1 224 ? 11.85609  7.93119  74.77091 1.000 60.64218  ? 227 LYS A NZ  1 
ATOM   1787 N  N   . LEU A 1 225 ? 8.34044   12.47415 69.60161 1.000 15.35902  ? 228 LEU A N   1 
ATOM   1788 C  CA  . LEU A 1 225 ? 7.72696   13.81421 69.70828 1.000 13.92625  ? 228 LEU A CA  1 
ATOM   1789 C  C   . LEU A 1 225 ? 6.20007   13.71493 69.59360 1.000 16.00994  ? 228 LEU A C   1 
ATOM   1790 O  O   . LEU A 1 225 ? 5.69427   12.67382 69.18207 1.000 18.55052  ? 228 LEU A O   1 
ATOM   1791 C  CB  . LEU A 1 225 ? 8.28988   14.76897 68.66374 1.000 11.75806  ? 228 LEU A CB  1 
ATOM   1792 C  CG  . LEU A 1 225 ? 9.74503   15.18946 68.87326 1.000 15.67307  ? 228 LEU A CG  1 
ATOM   1793 C  CD1 . LEU A 1 225 ? 10.21809  15.86833 67.61705 1.000 18.41209  ? 228 LEU A CD1 1 
ATOM   1794 C  CD2 . LEU A 1 225 ? 9.87292   16.11976 70.05633 1.000 22.37872  ? 228 LEU A CD2 1 
ATOM   1795 N  N   . ASN A 1 226 ? 5.53425   14.80293 69.93717 1.000 13.04939  ? 229 ASN A N   1 
ATOM   1796 C  CA  . ASN A 1 226 ? 4.06216   14.80408 69.96085 1.000 16.10574  ? 229 ASN A CA  1 
ATOM   1797 C  C   . ASN A 1 226 ? 3.46973   15.94324 69.12663 1.000 14.42488  ? 229 ASN A C   1 
ATOM   1798 O  O   . ASN A 1 226 ? 3.95807   17.06750 69.21080 1.000 15.19532  ? 229 ASN A O   1 
ATOM   1799 C  CB  . ASN A 1 226 ? 3.55110   14.98835 71.37595 1.000 17.31653  ? 229 ASN A CB  1 
ATOM   1800 C  CG  . ASN A 1 226 ? 3.62208   13.75152 72.24026 1.000 32.85827  ? 229 ASN A CG  1 
ATOM   1801 O  OD1 . ASN A 1 226 ? 4.12954   12.70536 71.82522 1.000 27.12875  ? 229 ASN A OD1 1 
ATOM   1802 N  ND2 . ASN A 1 226 ? 3.10924   13.85984 73.45375 1.000 21.82089  ? 229 ASN A ND2 1 
ATOM   1803 N  N   . PHE A 1 227 ? 2.44700   15.62200 68.34800 1.000 17.01498  ? 230 PHE A N   1 
ATOM   1804 C  CA  . PHE A 1 227 ? 1.72200   16.67100 67.63000 1.000 14.23152  ? 230 PHE A CA  1 
ATOM   1805 C  C   . PHE A 1 227 ? 0.95700   17.57200 68.58700 1.000 21.23467  ? 230 PHE A C   1 
ATOM   1806 O  O   . PHE A 1 227 ? 0.77800   18.76500 68.31200 1.000 18.52669  ? 230 PHE A O   1 
ATOM   1807 C  CB  . PHE A 1 227 ? 0.69300   16.09000 66.65400 1.000 11.23640  ? 230 PHE A CB  1 
ATOM   1808 C  CG  . PHE A 1 227 ? 1.26200   15.51100 65.37400 1.000 22.37377  ? 230 PHE A CG  1 
ATOM   1809 C  CD1 . PHE A 1 227 ? 1.99200   16.29800 64.50200 1.000 13.75988  ? 230 PHE A CD1 1 
ATOM   1810 C  CD2 . PHE A 1 227 ? 0.96500   14.20000 65.00700 1.000 23.70886  ? 230 PHE A CD2 1 
ATOM   1811 C  CE1 . PHE A 1 227 ? 2.48700   15.76900 63.30900 1.000 19.34189  ? 230 PHE A CE1 1 
ATOM   1812 C  CE2 . PHE A 1 227 ? 1.43900   13.66200 63.81500 1.000 13.73459  ? 230 PHE A CE2 1 
ATOM   1813 C  CZ  . PHE A 1 227 ? 2.20400   14.45100 62.96600 1.000 14.38565  ? 230 PHE A CZ  1 
ATOM   1814 N  N   . ASN A 1 228 ? 0.45600   16.99800 69.67500 1.000 18.75317  ? 231 ASN A N   1 
ATOM   1815 C  CA  . ASN A 1 228 ? -0.44400  17.63100 70.62600 1.000 21.34789  ? 231 ASN A CA  1 
ATOM   1816 C  C   . ASN A 1 228 ? 0.30200   18.54200 71.59900 1.000 20.66136  ? 231 ASN A C   1 
ATOM   1817 O  O   . ASN A 1 228 ? 1.51000   18.42500 71.80900 1.000 19.52365  ? 231 ASN A O   1 
ATOM   1818 C  CB  . ASN A 1 228 ? -1.17300  16.55800 71.42400 1.000 13.39921  ? 231 ASN A CB  1 
ATOM   1819 C  CG  . ASN A 1 228 ? -0.20600  15.61000 72.12000 1.000 22.72585  ? 231 ASN A CG  1 
ATOM   1820 O  OD1 . ASN A 1 228 ? 0.29900   14.65100 71.51600 1.000 17.99732  ? 231 ASN A OD1 1 
ATOM   1821 N  ND2 . ASN A 1 228 ? 0.07500   15.88500 73.38900 1.000 22.41870  ? 231 ASN A ND2 1 
ATOM   1822 N  N   . GLY A 1 229 ? -0.45600  19.43200 72.23600 1.000 14.33714  ? 232 GLY A N   1 
ATOM   1823 C  CA  . GLY A 1 229 ? 0.08100   20.19600 73.33400 1.000 19.03018  ? 232 GLY A CA  1 
ATOM   1824 C  C   . GLY A 1 229 ? 0.08100   19.41100 74.63100 1.000 20.71572  ? 232 GLY A C   1 
ATOM   1825 O  O   . GLY A 1 229 ? -0.60500  18.39900 74.78000 1.000 19.80173  ? 232 GLY A O   1 
ATOM   1826 N  N   . GLU A 1 230 ? 0.89200   19.87700 75.57600 1.000 18.98391  ? 233 GLU A N   1 
ATOM   1827 C  CA  . GLU A 1 230 ? 0.91200   19.28000 76.90400 1.000 23.45047  ? 233 GLU A CA  1 
ATOM   1828 C  C   . GLU A 1 230 ? -0.50500  19.21400 77.46500 1.000 24.99896  ? 233 GLU A C   1 
ATOM   1829 O  O   . GLU A 1 230 ? -1.33400  20.08800 77.20500 1.000 23.77226  ? 233 GLU A O   1 
ATOM   1830 C  CB  . GLU A 1 230 ? 1.81500   20.10000 77.83400 1.000 19.56211  ? 233 GLU A CB  1 
ATOM   1831 C  CG  . GLU A 1 230 ? 2.20600   19.39100 79.12300 1.000 29.89250  ? 233 GLU A CG  1 
ATOM   1832 C  CD  . GLU A 1 230 ? 2.94500   20.30500 80.07700 1.000 40.55469  ? 233 GLU A CD  1 
ATOM   1833 O  OE1 . GLU A 1 230 ? 3.32100   21.42100 79.65900 1.000 39.50996  ? 233 GLU A OE1 1 
ATOM   1834 O  OE2 . GLU A 1 230 ? 3.15000   19.91200 81.24500 1.000 60.57330  ? 233 GLU A OE2 1 
ATOM   1835 N  N   . GLY A 1 231 ? -0.79100  18.16100 78.22400 1.000 28.12367  ? 234 GLY A N   1 
ATOM   1836 C  CA  . GLY A 1 231 ? -2.11300  18.01800 78.80000 1.000 34.13661  ? 234 GLY A CA  1 
ATOM   1837 C  C   . GLY A 1 231 ? -3.21500  17.65000 77.82700 1.000 44.65339  ? 234 GLY A C   1 
ATOM   1838 O  O   . GLY A 1 231 ? -4.39100  17.65400 78.21900 1.000 37.24207  ? 234 GLY A O   1 
ATOM   1839 N  N   . GLU A 1 232 ? -2.88400  17.35200 76.57600 1.000 30.12749  ? 235 GLU A N   1 
ATOM   1840 C  CA  . GLU A 1 232 ? -3.82900  16.83400 75.60100 1.000 20.17577  ? 235 GLU A CA  1 
ATOM   1841 C  C   . GLU A 1 232 ? -3.52700  15.36200 75.35500 1.000 23.20750  ? 235 GLU A C   1 
ATOM   1842 O  O   . GLU A 1 232 ? -2.44800  14.88200 75.71400 1.000 30.18057  ? 235 GLU A O   1 
ATOM   1843 C  CB  . GLU A 1 232 ? -3.74200  17.62800 74.28900 1.000 26.03518  ? 235 GLU A CB  1 
ATOM   1844 C  CG  . GLU A 1 232 ? -4.24500  19.07100 74.38600 1.000 30.30491  ? 235 GLU A CG  1 
ATOM   1845 C  CD  . GLU A 1 232 ? -3.94300  19.91000 73.14300 1.000 35.37784  ? 235 GLU A CD  1 
ATOM   1846 O  OE1 . GLU A 1 232 ? -3.16600  19.46400 72.27400 1.000 34.83436  ? 235 GLU A OE1 1 
ATOM   1847 O  OE2 . GLU A 1 232 ? -4.49100  21.02900 73.03400 1.000 51.17131  ? 235 GLU A OE2 1 
ATOM   1848 N  N   . PRO A 1 233 ? -4.46400  14.59900 74.78000 1.000 31.30723  ? 236 PRO A N   1 
ATOM   1849 C  CA  . PRO A 1 233 ? -4.15200  13.19900 74.45800 1.000 25.66420  ? 236 PRO A CA  1 
ATOM   1850 C  C   . PRO A 1 233 ? -2.96600  13.11700 73.50600 1.000 16.73353  ? 236 PRO A C   1 
ATOM   1851 O  O   . PRO A 1 233 ? -2.80200  13.94000 72.60400 1.000 25.41775  ? 236 PRO A O   1 
ATOM   1852 C  CB  . PRO A 1 233 ? -5.43900  12.68400 73.80000 1.000 26.65471  ? 236 PRO A CB  1 
ATOM   1853 C  CG  . PRO A 1 233 ? -6.51900  13.62600 74.26300 1.000 38.23488  ? 236 PRO A CG  1 
ATOM   1854 C  CD  . PRO A 1 233 ? -5.84800  14.95900 74.41800 1.000 36.32410  ? 236 PRO A CD  1 
ATOM   1855 N  N   . GLU A 1 234 ? -2.12900  12.11200 73.73000 1.000 20.13779  ? 237 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 234 ? -0.87200  11.98400 73.00300 1.000 21.17954  ? 237 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 234 ? -1.11500  11.45800 71.59200 1.000 25.68824  ? 237 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 234 ? -1.71100  10.39100 71.40800 1.000 22.81997  ? 237 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 234 ? 0.07900   11.06400 73.76400 1.000 21.93554  ? 237 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 234 ? 1.41100   10.84100 73.06900 1.000 33.66144  ? 237 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 234 ? 2.41500   10.13800 73.96200 1.000 42.35770  ? 237 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 234 ? 1.99800   9.25800  74.74400 1.000 43.55314  ? 237 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 234 ? 3.61700   10.47600 73.89200 1.000 29.32271  ? 237 GLU A OE2 1 
ATOM   1864 N  N   . GLU A 1 235 ? -0.63100  12.19300 70.59700 1.000 20.81972  ? 238 GLU A N   1 
ATOM   1865 C  CA  . GLU A 1 235 ? -0.62600  11.72400 69.18700 1.000 20.32140  ? 238 GLU A CA  1 
ATOM   1866 C  C   . GLU A 1 235 ? 0.86700   11.84400 68.76500 1.000 17.37668  ? 238 GLU A C   1 
ATOM   1867 O  O   . GLU A 1 235 ? 1.42900   12.97000 68.78400 1.000 16.95308  ? 238 GLU A O   1 
ATOM   1868 C  CB  . GLU A 1 235 ? -1.55600  12.49700 68.24300 1.000 19.01110  ? 238 GLU A CB  1 
ATOM   1869 C  CG  . GLU A 1 235 ? -1.62200  11.98900 66.80500 1.000 43.62896  ? 238 GLU A CG  1 
ATOM   1870 C  CD  . GLU A 1 235 ? -2.59600  12.76300 65.92800 1.000 78.72273  ? 238 GLU A CD  1 
ATOM   1871 O  OE1 . GLU A 1 235 ? -3.21300  13.73800 66.41300 1.000 65.14910  ? 238 GLU A OE1 1 
ATOM   1872 O  OE2 . GLU A 1 235 ? -2.73500  12.40600 64.74100 1.000 80.45073  ? 238 GLU A OE2 1 
ATOM   1873 N  N   . LEU A 1 236 ? 1.52000   10.72300 68.48600 1.000 14.79185  ? 239 LEU A N   1 
ATOM   1874 C  CA  . LEU A 1 236 ? 2.93100   10.74100 68.13300 1.000 11.17840  ? 239 LEU A CA  1 
ATOM   1875 C  C   . LEU A 1 236 ? 3.15000   11.50400 66.83500 1.000 13.25134  ? 239 LEU A C   1 
ATOM   1876 O  O   . LEU A 1 236 ? 2.41000   11.33200 65.86100 1.000 14.88840  ? 239 LEU A O   1 
ATOM   1877 C  CB  . LEU A 1 236 ? 3.46500   9.31700  67.98900 1.000 16.82296  ? 239 LEU A CB  1 
ATOM   1878 C  CG  . LEU A 1 236 ? 3.47700   8.46500  69.25200 1.000 25.49990  ? 239 LEU A CG  1 
ATOM   1879 C  CD1 . LEU A 1 236 ? 4.14700   7.11700  68.97900 1.000 16.25410  ? 239 LEU A CD1 1 
ATOM   1880 C  CD2 . LEU A 1 236 ? 4.17000   9.22700  70.37300 1.000 25.77118  ? 239 LEU A CD2 1 
ATOM   1881 N  N   . MET A 1 237 ? 4.18900   12.34500 66.82200 1.000 14.38283  ? 240 MET A N   1 
ATOM   1882 C  CA  . MET A 1 237 ? 4.58700   13.09900 65.63100 1.000 15.80501  ? 240 MET A CA  1 
ATOM   1883 C  C   . MET A 1 237 ? 5.37500   12.17300 64.70900 1.000 12.26650  ? 240 MET A C   1 
ATOM   1884 O  O   . MET A 1 237 ? 6.59400   12.02800 64.81800 1.000 13.93230  ? 240 MET A O   1 
ATOM   1885 C  CB  . MET A 1 237 ? 5.40200   14.33000 66.00600 1.000 16.45452  ? 240 MET A CB  1 
ATOM   1886 C  CG  . MET A 1 237 ? 5.74200   15.26300 64.82400 1.000 14.73156  ? 240 MET A CG  1 
ATOM   1887 S  SD  . MET A 1 237 ? 6.73200   16.68600 65.33500 1.000 13.67421  ? 240 MET A SD  1 
ATOM   1888 C  CE  . MET A 1 237 ? 5.55500   17.66000 66.28000 1.000 15.11312  ? 240 MET A CE  1 
ATOM   1889 N  N   . VAL A 1 238 ? 4.65400   11.52800 63.79100 1.000 14.13350  ? 241 VAL A N   1 
ATOM   1890 C  CA  . VAL A 1 238 ? 5.23700   10.67600 62.75900 1.000 11.78705  ? 241 VAL A CA  1 
ATOM   1891 C  C   . VAL A 1 238 ? 4.47900   10.93500 61.46400 1.000 12.64883  ? 241 VAL A C   1 
ATOM   1892 O  O   . VAL A 1 238 ? 3.35100   11.43400 61.46700 1.000 15.99048  ? 241 VAL A O   1 
ATOM   1893 C  CB  . VAL A 1 238 ? 5.19400   9.16100  63.11000 1.000 9.60254   ? 241 VAL A CB  1 
ATOM   1894 C  CG1 . VAL A 1 238 ? 6.03700   8.86500  64.34900 1.000 14.82539  ? 241 VAL A CG1 1 
ATOM   1895 C  CG2 . VAL A 1 238 ? 3.75400   8.68000  63.28700 1.000 17.49225  ? 241 VAL A CG2 1 
ATOM   1896 N  N   . ASP A 1 239 ? 5.12700   10.58600 60.35000 1.000 8.00322   ? 242 ASP A N   1 
ATOM   1897 C  CA  . ASP A 1 239 ? 4.55700   10.70800 59.00600 1.000 11.68219  ? 242 ASP A CA  1 
ATOM   1898 C  C   . ASP A 1 239 ? 4.03600   12.11700 58.76200 1.000 12.49245  ? 242 ASP A C   1 
ATOM   1899 O  O   . ASP A 1 239 ? 2.90600   12.31400 58.31300 1.000 10.37423  ? 242 ASP A O   1 
ATOM   1900 C  CB  . ASP A 1 239 ? 3.45100   9.67700  58.76500 1.000 10.61762  ? 242 ASP A CB  1 
ATOM   1901 C  CG  . ASP A 1 239 ? 3.97300   8.25600  58.73700 1.000 11.38396  ? 242 ASP A CG  1 
ATOM   1902 O  OD1 . ASP A 1 239 ? 5.01300   8.01000  58.09700 1.000 12.28699  ? 242 ASP A OD1 1 
ATOM   1903 O  OD2 . ASP A 1 239 ? 3.33200   7.38200  59.34700 1.000 15.37383  ? 242 ASP A OD2 1 
ATOM   1904 N  N   . ASN A 1 240 ? 4.87200   13.10800 59.08000 1.000 11.45584  ? 243 ASN A N   1 
ATOM   1905 C  CA  . ASN A 1 240 ? 4.53600   14.50800 58.80800 1.000 7.51516   ? 243 ASN A CA  1 
ATOM   1906 C  C   . ASN A 1 240 ? 5.07400   14.93300 57.43500 1.000 14.92299  ? 243 ASN A C   1 
ATOM   1907 O  O   . ASN A 1 240 ? 5.74600   15.94600 57.27300 1.000 14.66657  ? 243 ASN A O   1 
ATOM   1908 C  CB  . ASN A 1 240 ? 5.06300   15.40600 59.92100 1.000 10.98788  ? 243 ASN A CB  1 
ATOM   1909 C  CG  . ASN A 1 240 ? 6.55500   15.26400 60.14700 1.000 11.97230  ? 243 ASN A CG  1 
ATOM   1910 O  OD1 . ASN A 1 240 ? 7.19900   14.35400 59.62800 1.000 13.84563  ? 243 ASN A OD1 1 
ATOM   1911 N  ND2 . ASN A 1 240 ? 7.12400   16.18500 60.92400 1.000 13.90282  ? 243 ASN A ND2 1 
ATOM   1912 N  N   . TRP A 1 241 ? 4.77700   14.13400 56.42000 1.000 13.64353  ? 244 TRP A N   1 
ATOM   1913 C  CA  . TRP A 1 241 ? 5.27300   14.38300 55.07700 1.000 11.21251  ? 244 TRP A CA  1 
ATOM   1914 C  C   . TRP A 1 241 ? 4.08900   14.44600 54.12800 1.000 13.10704  ? 244 TRP A C   1 
ATOM   1915 O  O   . TRP A 1 241 ? 3.09400   13.74000 54.31500 1.000 12.01615  ? 244 TRP A O   1 
ATOM   1916 C  CB  . TRP A 1 241 ? 6.28100   13.29800 54.62900 1.000 11.45786  ? 244 TRP A CB  1 
ATOM   1917 C  CG  . TRP A 1 241 ? 5.81300   11.88100 54.86000 1.000 7.37677   ? 244 TRP A CG  1 
ATOM   1918 C  CD1 . TRP A 1 241 ? 5.93200   11.15200 56.01600 1.000 9.32989   ? 244 TRP A CD1 1 
ATOM   1919 C  CD2 . TRP A 1 241 ? 5.17500   11.01700 53.90300 1.000 13.55678  ? 244 TRP A CD2 1 
ATOM   1920 N  NE1 . TRP A 1 241 ? 5.40100   9.88900  55.83700 1.000 8.28067   ? 244 TRP A NE1 1 
ATOM   1921 C  CE2 . TRP A 1 241 ? 4.92500   9.78500  54.55200 1.000 15.14047  ? 244 TRP A CE2 1 
ATOM   1922 C  CE3 . TRP A 1 241 ? 4.78200   11.16900 52.56400 1.000 17.04732  ? 244 TRP A CE3 1 
ATOM   1923 C  CZ2 . TRP A 1 241 ? 4.29700   8.71200  53.90700 1.000 10.28004  ? 244 TRP A CZ2 1 
ATOM   1924 C  CZ3 . TRP A 1 241 ? 4.16000   10.09900 51.91700 1.000 19.41887  ? 244 TRP A CZ3 1 
ATOM   1925 C  CH2 . TRP A 1 241 ? 3.93100   8.88600  52.59000 1.000 15.27267  ? 244 TRP A CH2 1 
ATOM   1926 N  N   . ARG A 1 242 ? 4.19900   15.31900 53.12000 1.000 10.17804  ? 245 ARG A N   1 
ATOM   1927 C  CA  . ARG A 1 242 ? 3.21800   15.46800 52.05600 1.000 11.86994  ? 245 ARG A CA  1 
ATOM   1928 C  C   . ARG A 1 242 ? 3.59400   14.57400 50.87600 1.000 14.46642  ? 245 ARG A C   1 
ATOM   1929 O  O   . ARG A 1 242 ? 4.76600   14.51600 50.49800 1.000 13.53309  ? 245 ARG A O   1 
ATOM   1930 C  CB  . ARG A 1 242 ? 3.15400   16.91700 51.58200 1.000 14.45723  ? 245 ARG A CB  1 
ATOM   1931 C  CG  . ARG A 1 242 ? 2.04500   17.17400 50.60300 1.000 9.27521   ? 245 ARG A CG  1 
ATOM   1932 C  CD  . ARG A 1 242 ? 2.14000   18.56400 49.99000 1.000 9.85562   ? 245 ARG A CD  1 
ATOM   1933 N  NE  . ARG A 1 242 ? 0.91100   18.89500 49.27700 1.000 11.00952  ? 245 ARG A NE  1 
ATOM   1934 C  CZ  . ARG A 1 242 ? 0.76800   19.92000 48.44600 1.000 15.78916  ? 245 ARG A CZ  1 
ATOM   1935 N  NH1 . ARG A 1 242 ? 1.78500   20.71200 48.13500 1.000 10.03612  ? 245 ARG A NH1 1 
ATOM   1936 N  NH2 . ARG A 1 242 ? -0.43000  20.15900 47.91400 1.000 18.34148  ? 245 ARG A NH2 1 
ATOM   1937 N  N   . PRO A 1 243 ? 2.62600   13.86500 50.29500 1.000 14.01551  ? 246 PRO A N   1 
ATOM   1938 C  CA  . PRO A 1 243 ? 2.91800   13.01900 49.13100 1.000 13.96290  ? 246 PRO A CA  1 
ATOM   1939 C  C   . PRO A 1 243 ? 3.33800   13.84200 47.92300 1.000 13.73204  ? 246 PRO A C   1 
ATOM   1940 O  O   . PRO A 1 243 ? 3.04000   15.03200 47.81100 1.000 12.51029  ? 246 PRO A O   1 
ATOM   1941 C  CB  . PRO A 1 243 ? 1.58600   12.31000 48.85300 1.000 18.09367  ? 246 PRO A CB  1 
ATOM   1942 C  CG  . PRO A 1 243 ? 0.75600   12.51200 50.06700 1.000 21.06092  ? 246 PRO A CG  1 
ATOM   1943 C  CD  . PRO A 1 243 ? 1.20900   13.79500 50.68400 1.000 16.27969  ? 246 PRO A CD  1 
ATOM   1944 N  N   . ALA A 1 244 ? 4.00300   13.16000 46.98900 1.000 12.22143  ? 247 ALA A N   1 
ATOM   1945 C  CA  . ALA A 1 244 ? 4.45600   13.79800 45.76100 1.000 11.81103  ? 247 ALA A CA  1 
ATOM   1946 C  C   . ALA A 1 244 ? 3.27400   14.34000 44.95900 1.000 15.88713  ? 247 ALA A C   1 
ATOM   1947 O  O   . ALA A 1 244 ? 2.21600   13.71200 44.86900 1.000 13.65631  ? 247 ALA A O   1 
ATOM   1948 C  CB  . ALA A 1 244 ? 5.26200   12.80200 44.92100 1.000 17.85578  ? 247 ALA A CB  1 
ATOM   1949 N  N   . GLN A 1 245 ? 3.46100   15.51800 44.38000 1.000 13.18042  ? 248 GLN A N   1 
ATOM   1950 C  CA  . GLN A 1 245 ? 2.45900   16.22700 43.59500 1.000 9.87239   ? 248 GLN A CA  1 
ATOM   1951 C  C   . GLN A 1 245 ? 2.79400   16.18300 42.10900 1.000 16.67776  ? 248 GLN A C   1 
ATOM   1952 O  O   . GLN A 1 245 ? 3.95300   15.98200 41.73400 1.000 15.71756  ? 248 GLN A O   1 
ATOM   1953 C  CB  . GLN A 1 245 ? 2.38200   17.68900 44.05800 1.000 13.11646  ? 248 GLN A CB  1 
ATOM   1954 C  CG  . GLN A 1 245 ? 2.07900   17.83800 45.54300 1.000 14.43054  ? 248 GLN A CG  1 
ATOM   1955 C  CD  . GLN A 1 245 ? 0.75800   17.19000 45.91800 1.000 20.29886  ? 248 GLN A CD  1 
ATOM   1956 O  OE1 . GLN A 1 245 ? -0.29100  17.54900 45.38700 1.000 19.52960  ? 248 GLN A OE1 1 
ATOM   1957 N  NE2 . GLN A 1 245 ? 0.80900   16.21100 46.81700 1.000 15.60244  ? 248 GLN A NE2 1 
ATOM   1958 N  N   . PRO A 1 246 ? 1.81000   16.41200 41.23100 1.000 16.28897  ? 249 PRO A N   1 
ATOM   1959 C  CA  . PRO A 1 246 ? 2.08200   16.34400 39.78800 1.000 16.90427  ? 249 PRO A CA  1 
ATOM   1960 C  C   . PRO A 1 246 ? 3.11800   17.37200 39.34800 1.000 17.72132  ? 249 PRO A C   1 
ATOM   1961 O  O   . PRO A 1 246 ? 3.09800   18.53000 39.77500 1.000 14.69260  ? 249 PRO A O   1 
ATOM   1962 C  CB  . PRO A 1 246 ? 0.71400   16.63400 39.15500 1.000 23.38317  ? 249 PRO A CB  1 
ATOM   1963 C  CG  . PRO A 1 246 ? -0.27700  16.31500 40.22000 1.000 20.77670  ? 249 PRO A CG  1 
ATOM   1964 C  CD  . PRO A 1 246 ? 0.39500   16.71200 41.50400 1.000 18.69620  ? 249 PRO A CD  1 
ATOM   1965 N  N   . LEU A 1 247 ? 4.03500   16.96100 38.47800 1.000 15.31365  ? 250 LEU A N   1 
ATOM   1966 C  CA  . LEU A 1 247 ? 5.10000   17.87900 37.99900 1.000 11.95892  ? 250 LEU A CA  1 
ATOM   1967 C  C   . LEU A 1 247 ? 4.48900   18.96600 37.08800 1.000 21.34619  ? 250 LEU A C   1 
ATOM   1968 O  O   . LEU A 1 247 ? 5.01800   20.08400 37.07300 1.000 16.60652  ? 250 LEU A O   1 
ATOM   1969 C  CB  . LEU A 1 247 ? 6.20900   17.11400 37.27500 1.000 16.10446  ? 250 LEU A CB  1 
ATOM   1970 C  CG  . LEU A 1 247 ? 7.50200   17.88500 37.00200 1.000 20.66959  ? 250 LEU A CG  1 
ATOM   1971 C  CD1 . LEU A 1 247 ? 7.96500   18.63900 38.23200 1.000 17.32229  ? 250 LEU A CD1 1 
ATOM   1972 C  CD2 . LEU A 1 247 ? 8.57700   16.93000 36.52800 1.000 22.22516  ? 250 LEU A CD2 1 
ATOM   1973 N  N   . LYS A 1 248 ? 3.45800   18.59600 36.32700 1.000 13.85372  ? 251 LYS A N   1 
ATOM   1974 C  CA  . LYS A 1 248 ? 2.80400   19.56000 35.40700 1.000 19.75933  ? 251 LYS A CA  1 
ATOM   1975 C  C   . LYS A 1 248 ? 3.83400   20.15900 34.42200 1.000 18.91670  ? 251 LYS A C   1 
ATOM   1976 O  O   . LYS A 1 248 ? 4.66000   19.39900 33.90100 1.000 23.55484  ? 251 LYS A O   1 
ATOM   1977 C  CB  . LYS A 1 248 ? 1.99600   20.57200 36.22300 1.000 22.64786  ? 251 LYS A CB  1 
ATOM   1978 C  CG  . LYS A 1 248 ? 0.78400   19.96300 36.89700 1.000 22.82279  ? 251 LYS A CG  1 
ATOM   1979 C  CD  . LYS A 1 248 ? -0.20800  20.98800 37.42100 1.000 28.55066  ? 251 LYS A CD  1 
ATOM   1980 C  CE  . LYS A 1 248 ? -1.49300  20.35200 37.83000 1.000 40.28510  ? 251 LYS A CE  1 
ATOM   1981 N  NZ  . LYS A 1 248 ? -1.85600  20.72800 39.19600 1.000 35.58705  ? 251 LYS A NZ  1 
ATOM   1982 N  N   . ASN A 1 249 ? 3.80600   21.46000 34.21800 1.000 14.90069  ? 252 ASN A N   1 
ATOM   1983 C  CA  . ASN A 1 249 ? 4.64400   22.07600 33.15100 1.000 32.27383  ? 252 ASN A CA  1 
ATOM   1984 C  C   . ASN A 1 249 ? 6.03700   22.41600 33.67800 1.000 32.03720  ? 252 ASN A C   1 
ATOM   1985 O  O   . ASN A 1 249 ? 6.46600   23.56400 33.50900 1.000 40.28291  ? 252 ASN A O   1 
ATOM   1986 C  CB  . ASN A 1 249 ? 3.94700   23.31700 32.60500 1.000 36.31091  ? 252 ASN A CB  1 
ATOM   1987 C  CG  . ASN A 1 249 ? 4.68200   23.94300 31.44600 1.000 67.84022  ? 252 ASN A CG  1 
ATOM   1988 O  OD1 . ASN A 1 249 ? 5.16700   23.23800 30.55500 1.000 62.92032  ? 252 ASN A OD1 1 
ATOM   1989 N  ND2 . ASN A 1 249 ? 4.80600   25.26000 31.46400 1.000 75.95214  ? 252 ASN A ND2 1 
ATOM   1990 N  N   . ARG A 1 250 ? 6.67300   21.48100 34.36900 1.000 21.39024  ? 253 ARG A N   1 
ATOM   1991 C  CA  . ARG A 1 250 ? 7.96700   21.85900 34.97200 1.000 15.24508  ? 253 ARG A CA  1 
ATOM   1992 C  C   . ARG A 1 250 ? 9.05400   20.88200 34.53800 1.000 18.09068  ? 253 ARG A C   1 
ATOM   1993 O  O   . ARG A 1 250 ? 8.74200   19.74200 34.21300 1.000 19.71137  ? 253 ARG A O   1 
ATOM   1994 C  CB  . ARG A 1 250 ? 7.91300   21.97900 36.50300 1.000 18.87765  ? 253 ARG A CB  1 
ATOM   1995 C  CG  . ARG A 1 250 ? 7.17200   23.19600 37.03300 1.000 17.19761  ? 253 ARG A CG  1 
ATOM   1996 C  CD  . ARG A 1 250 ? 7.03800   23.09200 38.53700 1.000 16.45259  ? 253 ARG A CD  1 
ATOM   1997 N  NE  . ARG A 1 250 ? 6.22900   21.94300 38.95100 1.000 14.26916  ? 253 ARG A NE  1 
ATOM   1998 C  CZ  . ARG A 1 250 ? 5.95600   21.63700 40.20600 1.000 15.89972  ? 253 ARG A CZ  1 
ATOM   1999 N  NH1 . ARG A 1 250 ? 6.55700   22.28600 41.18700 1.000 11.96386  ? 253 ARG A NH1 1 
ATOM   2000 N  NH2 . ARG A 1 250 ? 5.08000   20.68700 40.46900 1.000 12.85376  ? 253 ARG A NH2 1 
ATOM   2001 N  N   . GLN A 1 251 ? 10.28100  21.37100 34.58200 1.000 18.05300  ? 254 GLN A N   1 
ATOM   2002 C  CA  . GLN A 1 251 ? 11.42600  20.53000 34.21600 1.000 23.95017  ? 254 GLN A CA  1 
ATOM   2003 C  C   . GLN A 1 251 ? 12.38800  20.51300 35.39800 1.000 19.64917  ? 254 GLN A C   1 
ATOM   2004 O  O   . GLN A 1 251 ? 12.60900  21.57500 35.98200 1.000 22.15762  ? 254 GLN A O   1 
ATOM   2005 C  CB  . GLN A 1 251 ? 12.20000  21.02600 32.99900 1.000 29.57694  ? 254 GLN A CB  1 
ATOM   2006 C  CG  . GLN A 1 251 ? 13.46200  20.21700 32.72700 1.000 45.23893  ? 254 GLN A CG  1 
ATOM   2007 C  CD  . GLN A 1 251 ? 13.35600  19.37900 31.47600 1.000 58.83385  ? 254 GLN A CD  1 
ATOM   2008 O  OE1 . GLN A 1 251 ? 13.09200  19.88800 30.38400 1.000 53.28047  ? 254 GLN A OE1 1 
ATOM   2009 N  NE2 . GLN A 1 251 ? 13.58700  18.08300 31.62900 1.000 58.54467  ? 254 GLN A NE2 1 
ATOM   2010 N  N   . ILE A 1 252 ? 12.82800  19.32800 35.75500 1.000 12.20620  ? 255 ILE A N   1 
ATOM   2011 C  CA  . ILE A 1 252 ? 13.85700  19.18900 36.77500 1.000 13.49636  ? 255 ILE A CA  1 
ATOM   2012 C  C   . ILE A 1 252 ? 15.21900  19.19300 36.09000 1.000 19.42333  ? 255 ILE A C   1 
ATOM   2013 O  O   . ILE A 1 252 ? 15.45000  18.44100 35.13500 1.000 17.54225  ? 255 ILE A O   1 
ATOM   2014 C  CB  . ILE A 1 252 ? 13.64900  17.90700 37.59300 1.000 15.02189  ? 255 ILE A CB  1 
ATOM   2015 C  CG1 . ILE A 1 252 ? 12.33500  17.98600 38.38400 1.000 18.20898  ? 255 ILE A CG1 1 
ATOM   2016 C  CG2 . ILE A 1 252 ? 14.82200  17.68500 38.53100 1.000 16.05030  ? 255 ILE A CG2 1 
ATOM   2017 C  CD1 . ILE A 1 252 ? 11.81500  16.64300 38.82300 1.000 18.95534  ? 255 ILE A CD1 1 
ATOM   2018 N  N   . LYS A 1 253 ? 16.11100  20.05000 36.56500 1.000 16.05439  ? 256 LYS A N   1 
ATOM   2019 C  CA  . LYS A 1 253 ? 17.46200  20.16000 36.04200 1.000 13.48106  ? 256 LYS A CA  1 
ATOM   2020 C  C   . LYS A 1 253 ? 18.43200  19.53800 37.03700 1.000 18.59579  ? 256 LYS A C   1 
ATOM   2021 O  O   . LYS A 1 253 ? 18.17300  19.51900 38.24100 1.000 13.66290  ? 256 LYS A O   1 
ATOM   2022 C  CB  . LYS A 1 253 ? 17.83300  21.62500 35.78700 1.000 15.50571  ? 256 LYS A CB  1 
ATOM   2023 C  CG  . LYS A 1 253 ? 16.71300  22.43500 35.15700 1.000 25.47007  ? 256 LYS A CG  1 
ATOM   2024 C  CD  . LYS A 1 253 ? 17.20900  23.25000 33.97100 1.000 49.11712  ? 256 LYS A CD  1 
ATOM   2025 C  CE  . LYS A 1 253 ? 16.19600  24.31700 33.56400 1.000 52.17505  ? 256 LYS A CE  1 
ATOM   2026 N  NZ  . LYS A 1 253 ? 16.23600  25.51000 34.46600 1.000 58.89068  ? 256 LYS A NZ  1 
ATOM   2027 N  N   . ALA A 1 254 ? 19.53900  19.01000 36.52800 1.000 14.21440  ? 257 ALA A N   1 
ATOM   2028 C  CA  . ALA A 1 254 ? 20.56900  18.40100 37.35800 1.000 11.07664  ? 257 ALA A CA  1 
ATOM   2029 C  C   . ALA A 1 254 ? 21.89100  19.12400 37.14900 1.000 20.07225  ? 257 ALA A C   1 
ATOM   2030 O  O   . ALA A 1 254 ? 22.21300  19.53900 36.02900 1.000 18.72796  ? 257 ALA A O   1 
ATOM   2031 C  CB  . ALA A 1 254 ? 20.72000  16.90800 37.04200 1.000 15.87998  ? 257 ALA A CB  1 
ATOM   2032 N  N   . SER A 1 255 ? 22.64300  19.29400 38.23900 1.000 11.77844  ? 258 SER A N   1 
ATOM   2033 C  CA  . SER A 1 255 ? 23.96400  19.90800 38.17600 1.000 15.64444  ? 258 SER A CA  1 
ATOM   2034 C  C   . SER A 1 255 ? 25.04400  18.92400 37.75000 1.000 17.76975  ? 258 SER A C   1 
ATOM   2035 O  O   . SER A 1 255 ? 26.21400  19.30900 37.67900 1.000 21.22486  ? 258 SER A O   1 
ATOM   2036 C  CB  . SER A 1 255 ? 24.34000  20.51700 39.53600 1.000 11.82275  ? 258 SER A CB  1 
ATOM   2037 O  OG  . SER A 1 255 ? 24.67800  19.50700 40.48200 1.000 15.73657  ? 258 SER A OG  1 
ATOM   2038 N  N   . PHE A 1 256 ? 24.68200  17.67600 37.46500 1.000 16.50268  ? 259 PHE A N   1 
ATOM   2039 C  CA  . PHE A 1 256 ? 25.64900  16.60900 37.25600 1.000 20.60097  ? 259 PHE A CA  1 
ATOM   2040 C  C   . PHE A 1 256 ? 25.12800  15.65900 36.18900 1.000 29.23988  ? 259 PHE A C   1 
ATOM   2041 O  O   . PHE A 1 256 ? 23.93700  15.64600 35.86300 1.000 27.34187  ? 259 PHE A O   1 
ATOM   2042 C  CB  . PHE A 1 256 ? 25.91900  15.83400 38.55300 1.000 19.57657  ? 259 PHE A CB  1 
ATOM   2043 C  CG  . PHE A 1 256 ? 24.71500  15.08100 39.05900 1.000 23.31287  ? 259 PHE A CG  1 
ATOM   2044 C  CD1 . PHE A 1 256 ? 23.71900  15.73600 39.76400 1.000 15.68280  ? 259 PHE A CD1 1 
ATOM   2045 C  CD2 . PHE A 1 256 ? 24.56200  13.72800 38.79200 1.000 28.71631  ? 259 PHE A CD2 1 
ATOM   2046 C  CE1 . PHE A 1 256 ? 22.59800  15.04800 40.21000 1.000 21.88262  ? 259 PHE A CE1 1 
ATOM   2047 C  CE2 . PHE A 1 256 ? 23.44700  13.03600 39.24100 1.000 32.62951  ? 259 PHE A CE2 1 
ATOM   2048 C  CZ  . PHE A 1 256 ? 22.46400  13.70000 39.95600 1.000 23.60925  ? 259 PHE A CZ  1 
ATOM   2049 N  N   . LYS A 1 257 ? 26.03800  14.84600 35.66200 1.000 38.74297  ? 260 LYS A N   1 
ATOM   2050 C  CA  . LYS A 1 257 ? 25.71600  13.89900 34.60300 1.000 37.79232  ? 260 LYS A CA  1 
ATOM   2051 C  C   . LYS A 1 257 ? 26.26900  12.52100 34.94300 1.000 46.16682  ? 260 LYS A C   1 
ATOM   2052 O  O   . LYS A 1 257 ? 27.10000  12.38400 35.84700 1.000 40.91280  ? 260 LYS A O   1 
ATOM   2053 C  CB  . LYS A 1 257 ? 26.27700  14.39300 33.26500 1.000 40.69367  ? 260 LYS A CB  1 
ATOM   2054 C  CG  . LYS A 1 257 ? 26.39900  13.31800 32.20400 1.000 61.33884  ? 260 LYS A CG  1 
ATOM   2055 C  CD  . LYS A 1 257 ? 27.35800  13.74800 31.10600 1.000 75.27819  ? 260 LYS A CD  1 
ATOM   2056 C  CE  . LYS A 1 257 ? 27.21700  12.85400 29.88100 1.000 102.61207 ? 260 LYS A CE  1 
ATOM   2057 N  NZ  . LYS A 1 257 ? 28.22000  13.20200 28.83300 1.000 98.20676  ? 260 LYS A NZ  1 
HETATM 2058 ZN ZN  . ZN  B 2 .   ? 9.75800   20.82500 55.20000 1.000 11.82415  ? 301 ZN  A ZN  1 
HETATM 2059 O  O   . HOH C 3 .   ? 30.12700  35.82500 64.12700 1.000 46.19069  ? 401 HOH A O   1 
HETATM 2060 O  O   . HOH C 3 .   ? 14.31700  6.98600  36.09800 1.000 31.03214  ? 402 HOH A O   1 
HETATM 2061 O  O   . HOH C 3 .   ? 6.98800   40.74500 48.47600 1.000 36.01266  ? 403 HOH A O   1 
HETATM 2062 O  O   . HOH C 3 .   ? -0.51400  14.29400 77.02700 1.000 42.18791  ? 404 HOH A O   1 
HETATM 2063 O  O   . HOH C 3 .   ? 16.53700  36.09400 37.87000 1.000 41.47299  ? 405 HOH A O   1 
HETATM 2064 O  O   . HOH C 3 .   ? -1.14200  20.27300 41.50900 1.000 28.87758  ? 406 HOH A O   1 
HETATM 2065 O  O   . HOH C 3 .   ? 1.28600   7.06000  60.68500 1.000 38.49422  ? 407 HOH A O   1 
HETATM 2066 O  O   . HOH C 3 .   ? 11.61300  7.98400  32.87300 1.000 36.62423  ? 408 HOH A O   1 
HETATM 2067 O  O   . HOH C 3 .   ? 22.02700  1.63200  65.17200 1.000 35.63471  ? 409 HOH A O   1 
HETATM 2068 O  O   . HOH C 3 .   ? 17.52600  3.82800  51.32600 1.000 54.98627  ? 410 HOH A O   1 
HETATM 2069 O  O   . HOH C 3 .   ? 17.37600  5.93200  41.14900 1.000 32.27654  ? 411 HOH A O   1 
HETATM 2070 O  O   . HOH C 3 .   ? 21.68600  18.89700 72.83600 1.000 32.37127  ? 412 HOH A O   1 
HETATM 2071 O  O   . HOH C 3 .   ? 13.85100  31.32900 44.64400 1.000 20.23948  ? 413 HOH A O   1 
HETATM 2072 O  O   . HOH C 3 .   ? 16.321    43.154   55.947   1.000 34.77654  ? 414 HOH A O   1 
HETATM 2073 O  O   . HOH C 3 .   ? 9.11600   18.08500 76.89100 1.000 29.47558  ? 415 HOH A O   1 
HETATM 2074 O  O   . HOH C 3 .   ? 18.977    1.146    56.057   1.000 47.82318  ? 416 HOH A O   1 
HETATM 2075 O  O   . HOH C 3 .   ? 15.65900  0.31900  62.06900 1.000 37.37719  ? 417 HOH A O   1 
HETATM 2076 O  O   . HOH C 3 .   ? -8.08500  15.75300 47.81100 1.000 35.15227  ? 418 HOH A O   1 
HETATM 2077 O  O   . HOH C 3 .   ? 4.36300   18.56500 54.62500 1.000 11.02557  ? 419 HOH A O   1 
HETATM 2078 O  O   . HOH C 3 .   ? 29.28700  16.89900 56.85400 1.000 33.68576  ? 420 HOH A O   1 
HETATM 2079 O  O   . HOH C 3 .   ? 27.72500  31.37700 50.08300 1.000 31.17290  ? 421 HOH A O   1 
HETATM 2080 O  O   . HOH C 3 .   ? 4.71400   32.04300 42.28100 1.000 26.17604  ? 422 HOH A O   1 
HETATM 2081 O  O   . HOH C 3 .   ? 29.14600  32.29900 57.17900 1.000 29.12573  ? 423 HOH A O   1 
HETATM 2082 O  O   . HOH C 3 .   ? 3.37000   37.47300 53.73600 1.000 35.41004  ? 424 HOH A O   1 
HETATM 2083 O  O   . HOH C 3 .   ? 19.56400  7.25200  37.37700 1.000 40.33709  ? 425 HOH A O   1 
HETATM 2084 O  O   . HOH C 3 .   ? 23.13100  5.75800  67.40300 1.000 23.87028  ? 426 HOH A O   1 
HETATM 2085 O  O   . HOH C 3 .   ? 4.41000   23.96200 80.55500 1.000 61.64818  ? 427 HOH A O   1 
HETATM 2086 O  O   . HOH C 3 .   ? 21.25600  2.12600  62.17000 1.000 22.10498  ? 428 HOH A O   1 
HETATM 2087 O  O   . HOH C 3 .   ? 26.58700  19.84100 63.53000 1.000 20.80382  ? 429 HOH A O   1 
HETATM 2088 O  O   . HOH C 3 .   ? 15.69900  35.48300 41.19400 1.000 37.92246  ? 430 HOH A O   1 
HETATM 2089 O  O   . HOH C 3 .   ? 31.65900  28.26200 51.69800 1.000 32.38413  ? 431 HOH A O   1 
HETATM 2090 O  O   . HOH C 3 .   ? 8.21900   22.26100 54.15500 1.000 22.38307  ? 432 HOH A O   1 
HETATM 2091 O  O   . HOH C 3 .   ? -0.39000  27.89100 40.53600 1.000 21.30688  ? 433 HOH A O   1 
HETATM 2092 O  O   . HOH C 3 .   ? 11.83100  18.85300 62.42100 1.000 13.18559  ? 434 HOH A O   1 
HETATM 2093 O  O   . HOH C 3 .   ? 9.93300   7.72400  38.68800 1.000 26.66421  ? 435 HOH A O   1 
HETATM 2094 O  O   . HOH C 3 .   ? 24.06100  31.58200 40.36100 1.000 44.50458  ? 436 HOH A O   1 
HETATM 2095 O  O   . HOH C 3 .   ? 21.89400  10.43400 73.95600 1.000 29.00077  ? 437 HOH A O   1 
HETATM 2096 O  O   . HOH C 3 .   ? 4.28100   26.67600 55.79900 1.000 38.21137  ? 438 HOH A O   1 
HETATM 2097 O  O   . HOH C 3 .   ? 11.95600  7.29000  37.40800 1.000 39.39800  ? 439 HOH A O   1 
HETATM 2098 O  O   . HOH C 3 .   ? 19.65300  38.85500 47.38600 1.000 24.93862  ? 440 HOH A O   1 
HETATM 2099 O  O   . HOH C 3 .   ? 26.66300  11.69300 53.12900 1.000 24.16621  ? 441 HOH A O   1 
HETATM 2100 O  O   . HOH C 3 .   ? 13.98300  3.18900  50.86200 1.000 28.27047  ? 442 HOH A O   1 
HETATM 2101 O  O   . HOH C 3 .   ? 22.47000  18.79500 28.60600 1.000 46.09583  ? 443 HOH A O   1 
HETATM 2102 O  O   . HOH C 3 .   ? 14.14700  2.91000  63.07200 1.000 35.24414  ? 444 HOH A O   1 
HETATM 2103 O  O   . HOH C 3 .   ? -4.31400  15.06800 70.72300 1.000 32.92977  ? 445 HOH A O   1 
HETATM 2104 O  O   . HOH C 3 .   ? 5.42300   18.74200 77.58200 1.000 31.49617  ? 446 HOH A O   1 
HETATM 2105 O  O   . HOH C 3 .   ? 24.35000  30.60600 68.78900 1.000 17.78451  ? 447 HOH A O   1 
HETATM 2106 O  O   . HOH C 3 .   ? -1.24200  15.95900 62.32100 1.000 24.09146  ? 448 HOH A O   1 
HETATM 2107 O  O   . HOH C 3 .   ? 19.44900  10.47200 45.72200 1.000 26.00309  ? 449 HOH A O   1 
HETATM 2108 O  O   . HOH C 3 .   ? 22.25500  40.21200 51.29200 1.000 35.09366  ? 450 HOH A O   1 
HETATM 2109 O  O   . HOH C 3 .   ? 21.09700  33.37200 59.07000 1.000 21.52382  ? 451 HOH A O   1 
HETATM 2110 O  O   . HOH C 3 .   ? 2.82400   21.83700 75.09100 1.000 20.43430  ? 452 HOH A O   1 
HETATM 2111 O  O   . HOH C 3 .   ? -1.29300  19.56700 43.65000 1.000 30.56843  ? 453 HOH A O   1 
HETATM 2112 O  O   . HOH C 3 .   ? 10.127    2.415    50.776   1.000 23.29013  ? 454 HOH A O   1 
HETATM 2113 O  O   . HOH C 3 .   ? 10.13500  28.72000 63.51800 1.000 23.92276  ? 455 HOH A O   1 
HETATM 2114 O  O   . HOH C 3 .   ? 21.91400  13.88800 35.70000 1.000 31.53792  ? 456 HOH A O   1 
HETATM 2115 O  O   . HOH C 3 .   ? 30.43500  16.38900 43.84500 1.000 50.66954  ? 457 HOH A O   1 
HETATM 2116 O  O   . HOH C 3 .   ? 7.64100   9.24100  52.35600 1.000 13.52630  ? 458 HOH A O   1 
HETATM 2117 O  O   . HOH C 3 .   ? -10.810   24.609   47.546   1.000 35.82717  ? 459 HOH A O   1 
HETATM 2118 O  O   . HOH C 3 .   ? 1.46600   12.02100 55.62200 1.000 34.09693  ? 460 HOH A O   1 
HETATM 2119 O  O   . HOH C 3 .   ? 17.04900  33.38400 42.55000 1.000 17.68867  ? 461 HOH A O   1 
HETATM 2120 O  O   . HOH C 3 .   ? 6.51900   11.49400 49.38100 1.000 20.44165  ? 462 HOH A O   1 
HETATM 2121 O  O   . HOH C 3 .   ? 0.36600   9.73700  65.03400 1.000 26.13161  ? 463 HOH A O   1 
HETATM 2122 O  O   . HOH C 3 .   ? -10.69100 21.82800 63.10600 1.000 40.55269  ? 464 HOH A O   1 
HETATM 2123 O  O   . HOH C 3 .   ? -7.37500  29.59500 54.52400 1.000 39.17404  ? 465 HOH A O   1 
HETATM 2124 O  O   . HOH C 3 .   ? 31.18400  26.58000 46.18600 1.000 35.05151  ? 466 HOH A O   1 
HETATM 2125 O  O   . HOH C 3 .   ? -10.22700 16.89800 45.46000 1.000 33.76303  ? 467 HOH A O   1 
HETATM 2126 O  O   . HOH C 3 .   ? 11.07700  7.21600  59.02400 1.000 9.88705   ? 468 HOH A O   1 
HETATM 2127 O  O   . HOH C 3 .   ? 27.94000  34.83400 64.05000 1.000 40.04471  ? 469 HOH A O   1 
HETATM 2128 O  O   . HOH C 3 .   ? 7.62000   10.65100 38.22900 1.000 32.55841  ? 470 HOH A O   1 
HETATM 2129 O  O   . HOH C 3 .   ? 15.967    4.254    38.295   1.000 38.24157  ? 471 HOH A O   1 
HETATM 2130 O  O   . HOH C 3 .   ? 28.51200  27.48800 62.04600 1.000 29.89271  ? 472 HOH A O   1 
HETATM 2131 O  O   . HOH C 3 .   ? 29.92100  26.86700 55.01600 1.000 28.80391  ? 473 HOH A O   1 
HETATM 2132 O  O   . HOH C 3 .   ? 6.55900   9.84800  73.43800 1.000 31.84893  ? 474 HOH A O   1 
HETATM 2133 O  O   . HOH C 3 .   ? 5.73600   14.04600 40.94200 1.000 17.25536  ? 475 HOH A O   1 
HETATM 2134 O  O   . HOH C 3 .   ? 24.75700  15.74800 46.78700 1.000 16.12905  ? 476 HOH A O   1 
HETATM 2135 O  O   . HOH C 3 .   ? 23.68300  33.69500 43.94100 1.000 17.35992  ? 477 HOH A O   1 
HETATM 2136 O  O   . HOH C 3 .   ? 18.88600  31.71600 72.45200 1.000 31.79938  ? 478 HOH A O   1 
HETATM 2137 O  O   . HOH C 3 .   ? 9.018     31.212   65.218   1.000 28.74790  ? 479 HOH A O   1 
HETATM 2138 O  O   . HOH C 3 .   ? 9.10700   11.24700 33.54800 1.000 36.13443  ? 480 HOH A O   1 
HETATM 2139 O  O   . HOH C 3 .   ? 29.95500  25.82000 49.54000 1.000 27.81383  ? 481 HOH A O   1 
HETATM 2140 O  O   . HOH C 3 .   ? -12.51100 20.23200 55.77500 1.000 20.97286  ? 482 HOH A O   1 
HETATM 2141 O  O   . HOH C 3 .   ? 20.31800  14.26800 49.91700 1.000 11.50413  ? 483 HOH A O   1 
HETATM 2142 O  O   . HOH C 3 .   ? -5.46500  18.92300 49.25900 1.000 16.55420  ? 484 HOH A O   1 
HETATM 2143 O  O   . HOH C 3 .   ? 1.58800   16.62100 35.69300 1.000 27.84196  ? 485 HOH A O   1 
HETATM 2144 O  O   . HOH C 3 .   ? 5.45900   19.53100 58.85600 1.000 20.16738  ? 486 HOH A O   1 
HETATM 2145 O  O   . HOH C 3 .   ? 26.04300  16.71500 67.83600 1.000 24.83003  ? 487 HOH A O   1 
HETATM 2146 O  O   . HOH C 3 .   ? 15.96500  14.03900 74.13500 1.000 42.17067  ? 488 HOH A O   1 
HETATM 2147 O  O   . HOH C 3 .   ? 30.18800  18.86500 45.31200 1.000 29.24047  ? 489 HOH A O   1 
HETATM 2148 O  O   . HOH C 3 .   ? 3.75700   33.39000 46.68400 1.000 27.93171  ? 490 HOH A O   1 
HETATM 2149 O  O   . HOH C 3 .   ? 7.21800   23.39400 56.30100 1.000 17.09573  ? 491 HOH A O   1 
HETATM 2150 O  O   . HOH C 3 .   ? 3.36000   23.80800 35.85700 1.000 23.82330  ? 492 HOH A O   1 
HETATM 2151 O  O   . HOH C 3 .   ? 18.57500  12.21500 32.71000 1.000 32.39344  ? 493 HOH A O   1 
HETATM 2152 O  O   . HOH C 3 .   ? 17.86600  42.92100 53.13700 1.000 49.42322  ? 494 HOH A O   1 
HETATM 2153 O  O   . HOH C 3 .   ? 0.18600   21.91500 62.09000 1.000 34.93985  ? 495 HOH A O   1 
HETATM 2154 O  O   . HOH C 3 .   ? 22.65500  32.80800 61.49700 1.000 16.82130  ? 496 HOH A O   1 
HETATM 2155 O  O   . HOH C 3 .   ? 9.53800   29.33200 58.57900 1.000 33.98256  ? 497 HOH A O   1 
HETATM 2156 O  O   . HOH C 3 .   ? 19.47500  12.98400 37.26100 1.000 25.68080  ? 498 HOH A O   1 
HETATM 2157 O  O   . HOH C 3 .   ? -1.85100  17.81700 49.47500 1.000 16.76800  ? 499 HOH A O   1 
HETATM 2158 O  O   . HOH C 3 .   ? 25.25100  28.51300 65.72300 1.000 16.98171  ? 500 HOH A O   1 
HETATM 2159 O  O   . HOH C 3 .   ? 20.43200  5.83900  48.21100 1.000 40.46975  ? 501 HOH A O   1 
HETATM 2160 O  O   . HOH C 3 .   ? 1.18200   31.03500 42.83200 1.000 38.25970  ? 502 HOH A O   1 
HETATM 2161 O  O   . HOH C 3 .   ? 10.93900  0.75800  60.46400 1.000 26.57234  ? 503 HOH A O   1 
HETATM 2162 O  O   . HOH C 3 .   ? 11.70600  23.52300 77.03400 1.000 33.74295  ? 504 HOH A O   1 
HETATM 2163 O  O   . HOH C 3 .   ? 26.47200  4.09500  63.94900 1.000 43.93531  ? 505 HOH A O   1 
HETATM 2164 O  O   . HOH C 3 .   ? 28.89500  18.51200 38.26700 1.000 34.17278  ? 506 HOH A O   1 
HETATM 2165 O  O   . HOH C 3 .   ? -2.26400  30.07600 50.27400 1.000 18.59660  ? 507 HOH A O   1 
HETATM 2166 O  O   . HOH C 3 .   ? 29.87100  12.10700 35.18200 1.000 43.03742  ? 508 HOH A O   1 
HETATM 2167 O  O   . HOH C 3 .   ? -5.45000  26.29400 42.66100 1.000 36.12836  ? 509 HOH A O   1 
HETATM 2168 O  O   . HOH C 3 .   ? 21.94800  26.46400 74.00500 1.000 24.55207  ? 510 HOH A O   1 
HETATM 2169 O  O   . HOH C 3 .   ? 15.60800  26.66500 77.20600 1.000 30.58101  ? 511 HOH A O   1 
HETATM 2170 O  O   . HOH C 3 .   ? 12.22000  17.00500 34.18200 1.000 23.77192  ? 512 HOH A O   1 
HETATM 2171 O  O   . HOH C 3 .   ? 18.19000  23.75600 31.10800 1.000 46.54289  ? 513 HOH A O   1 
HETATM 2172 O  O   . HOH C 3 .   ? 26.28900  22.30300 35.71800 1.000 28.30579  ? 514 HOH A O   1 
HETATM 2173 O  O   . HOH C 3 .   ? 16.80800  3.98100  55.33500 1.000 30.02236  ? 515 HOH A O   1 
HETATM 2174 O  O   . HOH C 3 .   ? 28.22500  15.06700 61.39200 1.000 24.05070  ? 516 HOH A O   1 
HETATM 2175 O  O   . HOH C 3 .   ? 12.77800  14.54500 36.06000 1.000 26.65442  ? 517 HOH A O   1 
HETATM 2176 O  O   . HOH C 3 .   ? 6.84900   6.65000  45.89000 1.000 21.19914  ? 518 HOH A O   1 
HETATM 2177 O  O   . HOH C 3 .   ? 29.31300  7.33500  62.17400 1.000 35.29061  ? 519 HOH A O   1 
HETATM 2178 O  O   . HOH C 3 .   ? -0.68500  20.01900 65.86900 1.000 28.20773  ? 520 HOH A O   1 
HETATM 2179 O  O   . HOH C 3 .   ? 4.84800   9.26200  42.69600 1.000 33.04909  ? 521 HOH A O   1 
HETATM 2180 O  O   . HOH C 3 .   ? 8.50500   30.28500 73.13700 1.000 42.40217  ? 522 HOH A O   1 
HETATM 2181 O  O   . HOH C 3 .   ? 29.65500  15.91700 39.79500 1.000 41.26267  ? 523 HOH A O   1 
HETATM 2182 O  O   . HOH C 3 .   ? 15.09300  25.63000 39.43900 1.000 20.01353  ? 524 HOH A O   1 
HETATM 2183 O  O   . HOH C 3 .   ? 4.58600   27.57900 75.22700 1.000 42.44603  ? 525 HOH A O   1 
HETATM 2184 O  O   . HOH C 3 .   ? 11.42400  3.25700  48.48000 1.000 27.32943  ? 526 HOH A O   1 
HETATM 2185 O  O   . HOH C 3 .   ? 27.24100  22.14000 43.83500 1.000 22.37216  ? 527 HOH A O   1 
HETATM 2186 O  O   . HOH C 3 .   ? 8.60500   26.33200 76.17800 1.000 34.46285  ? 528 HOH A O   1 
HETATM 2187 O  O   . HOH C 3 .   ? 7.98000   23.68100 60.22900 1.000 29.44843  ? 529 HOH A O   1 
HETATM 2188 O  O   . HOH C 3 .   ? 15.15100  32.28500 67.49100 1.000 29.16467  ? 530 HOH A O   1 
HETATM 2189 O  O   . HOH C 3 .   ? 6.50600   9.40300  45.01000 1.000 18.52064  ? 531 HOH A O   1 
HETATM 2190 O  O   . HOH C 3 .   ? 16.25500  5.64400  43.73200 1.000 27.46873  ? 532 HOH A O   1 
HETATM 2191 O  O   . HOH C 3 .   ? 25.64000  4.16500  56.53200 1.000 40.40549  ? 533 HOH A O   1 
HETATM 2192 O  O   . HOH C 3 .   ? -7.57500  13.67600 61.77100 1.000 30.43217  ? 534 HOH A O   1 
HETATM 2193 O  O   . HOH C 3 .   ? 29.27700  30.45300 64.61100 1.000 35.28887  ? 535 HOH A O   1 
HETATM 2194 O  O   . HOH C 3 .   ? 4.23000   21.19000 83.67200 1.000 56.33993  ? 536 HOH A O   1 
HETATM 2195 O  O   . HOH C 3 .   ? 24.24400  41.88300 56.86900 1.000 30.49396  ? 537 HOH A O   1 
HETATM 2196 O  O   . HOH C 3 .   ? -1.74700  15.31800 47.99000 1.000 43.26176  ? 538 HOH A O   1 
HETATM 2197 O  O   . HOH C 3 .   ? 27.29000  29.51000 34.32800 1.000 49.76255  ? 539 HOH A O   1 
HETATM 2198 O  O   . HOH C 3 .   ? 14.15900  40.58300 58.25300 1.000 35.70397  ? 540 HOH A O   1 
HETATM 2199 O  O   . HOH C 3 .   ? 28.91800  26.22000 31.12700 1.000 44.39859  ? 541 HOH A O   1 
HETATM 2200 O  O   . HOH C 3 .   ? 0.07500   18.58900 62.75000 1.000 24.96405  ? 542 HOH A O   1 
HETATM 2201 O  O   . HOH C 3 .   ? 34.77500  10.02100 49.06000 1.000 47.16343  ? 543 HOH A O   1 
HETATM 2202 O  O   . HOH C 3 .   ? 0.42700   11.25700 60.96200 1.000 27.37486  ? 544 HOH A O   1 
HETATM 2203 O  O   . HOH C 3 .   ? 27.08600  21.98600 66.72600 1.000 23.65285  ? 545 HOH A O   1 
HETATM 2204 O  O   . HOH C 3 .   ? 6.02900   28.86900 71.43800 1.000 32.76939  ? 546 HOH A O   1 
HETATM 2205 O  O   . HOH C 3 .   ? 16.83400  37.71200 43.08500 1.000 33.01069  ? 547 HOH A O   1 
HETATM 2206 O  O   . HOH C 3 .   ? 16.43400  5.95500  70.53000 1.000 36.89340  ? 548 HOH A O   1 
HETATM 2207 O  O   . HOH C 3 .   ? 10.46400  13.88300 37.37700 1.000 26.48177  ? 549 HOH A O   1 
HETATM 2208 O  O   . HOH C 3 .   ? 26.71500  9.36400  59.06500 1.000 28.73475  ? 550 HOH A O   1 
HETATM 2209 O  O   . HOH C 3 .   ? 27.98700  13.35000 68.60300 1.000 35.06750  ? 551 HOH A O   1 
HETATM 2210 O  O   . HOH C 3 .   ? 4.03900   14.15900 37.40600 1.000 40.37779  ? 552 HOH A O   1 
HETATM 2211 O  O   . HOH C 3 .   ? 8.65000   25.19200 57.48500 1.000 37.60129  ? 553 HOH A O   1 
HETATM 2212 O  O   . HOH C 3 .   ? 1.79500   21.02700 41.06200 1.000 14.91264  ? 554 HOH A O   1 
HETATM 2213 O  O   . HOH C 3 .   ? 14.27200  4.13100  53.27300 1.000 34.48526  ? 555 HOH A O   1 
HETATM 2214 O  O   . HOH C 3 .   ? 6.93000   27.56400 63.14300 1.000 32.46935  ? 556 HOH A O   1 
HETATM 2215 O  O   . HOH C 3 .   ? 10.38100  5.82800  69.30700 1.000 33.98180  ? 557 HOH A O   1 
HETATM 2216 O  O   . HOH C 3 .   ? 5.05200   10.33800 47.42900 1.000 21.63180  ? 558 HOH A O   1 
HETATM 2217 O  O   . HOH C 3 .   ? 1.63700   4.84800  56.83900 1.000 38.31673  ? 559 HOH A O   1 
HETATM 2218 O  O   . HOH C 3 .   ? 27.28100  20.87000 41.29700 1.000 35.09036  ? 560 HOH A O   1 
HETATM 2219 O  O   . HOH C 3 .   ? 16.690    -0.006   58.576   1.000 39.07445  ? 561 HOH A O   1 
HETATM 2220 O  O   . HOH C 3 .   ? 26.42700  10.95000 56.11900 1.000 25.62443  ? 562 HOH A O   1 
HETATM 2221 O  O   . HOH C 3 .   ? 9.59300   2.55200  45.99200 1.000 37.75788  ? 563 HOH A O   1 
HETATM 2222 O  O   . HOH C 3 .   ? -5.305    16.793   81.006   1.000 43.75245  ? 564 HOH A O   1 
HETATM 2223 O  O   . HOH C 3 .   ? 5.284     30.584   39.240   1.000 37.78305  ? 565 HOH A O   1 
HETATM 2224 O  O   . HOH C 3 .   ? 14.33900  23.99500 36.72100 1.000 39.18662  ? 566 HOH A O   1 
HETATM 2225 O  O   . HOH C 3 .   ? 12.68900  12.27200 71.91000 1.000 32.51823  ? 567 HOH A O   1 
HETATM 2226 O  O   . HOH C 3 .   ? 13.01800  37.75400 58.38200 1.000 18.59602  ? 568 HOH A O   1 
HETATM 2227 O  O   . HOH C 3 .   ? 28.97000  26.12500 35.28300 1.000 44.72525  ? 569 HOH A O   1 
HETATM 2228 O  O   . HOH C 3 .   ? 1.94400   31.69400 45.67300 1.000 19.12815  ? 570 HOH A O   1 
HETATM 2229 O  O   . HOH C 3 .   ? 8.61800   23.84400 52.49500 1.000 22.43937  ? 571 HOH A O   1 
HETATM 2230 O  O   . HOH C 3 .   ? -6.42400  24.70000 58.30500 1.000 33.71779  ? 572 HOH A O   1 
HETATM 2231 O  O   . HOH C 3 .   ? -4.61800  29.08800 48.77000 1.000 18.34478  ? 573 HOH A O   1 
HETATM 2232 O  O   . HOH C 3 .   ? -9.68600  19.10200 57.21500 1.000 34.51957  ? 574 HOH A O   1 
HETATM 2233 O  O   . HOH C 3 .   ? 20.63900  23.28400 74.45500 1.000 47.76993  ? 575 HOH A O   1 
HETATM 2234 O  O   . HOH C 3 .   ? 8.74500   38.81100 58.60900 1.000 35.84759  ? 576 HOH A O   1 
HETATM 2235 O  O   . HOH C 3 .   ? 19.92400  42.59300 49.12600 1.000 38.87962  ? 577 HOH A O   1 
HETATM 2236 O  O   . HOH C 3 .   ? 29.00500  15.97400 36.53600 1.000 30.87181  ? 578 HOH A O   1 
HETATM 2237 O  O   . HOH C 3 .   ? 13.46200  28.09300 40.10400 1.000 39.22920  ? 579 HOH A O   1 
HETATM 2238 O  O   . HOH C 3 .   ? 20.79700  42.76400 52.82700 1.000 37.17618  ? 580 HOH A O   1 
HETATM 2239 O  O   . HOH C 3 .   ? 4.57700   33.69700 44.11300 1.000 32.83057  ? 581 HOH A O   1 
HETATM 2240 O  O   . HOH C 3 .   ? 7.37300   26.67400 59.92400 1.000 36.49994  ? 582 HOH A O   1 
HETATM 2241 O  O   . HOH C 3 .   ? 19.920    16.882   77.230   1.000 44.61980  ? 583 HOH A O   1 
HETATM 2242 O  O   . HOH C 3 .   ? -7.60100  20.12400 56.82000 1.000 29.62205  ? 584 HOH A O   1 
HETATM 2243 O  O   . HOH C 3 .   ? 3.29600   8.54100  48.06900 1.000 35.52612  ? 585 HOH A O   1 
HETATM 2244 O  O   . HOH C 3 .   ? 7.26900   21.65200 58.59900 1.000 24.05108  ? 586 HOH A O   1 
HETATM 2245 O  O   . HOH C 3 .   ? 2.69200   23.78600 76.89700 1.000 33.99357  ? 587 HOH A O   1 
HETATM 2246 O  O   . HOH C 3 .   ? 8.75100   19.98300 78.68100 1.000 36.90570  ? 588 HOH A O   1 
HETATM 2247 O  O   . HOH C 3 .   ? 27.45100  19.64400 66.06900 1.000 38.45536  ? 589 HOH A O   1 
HETATM 2248 O  O   . HOH C 3 .   ? 8.62600   27.68000 55.67500 1.000 42.16895  ? 590 HOH A O   1 
HETATM 2249 O  O   . HOH C 3 .   ? 12.765    26.443   35.928   1.000 44.74995  ? 591 HOH A O   1 
HETATM 2250 O  O   . HOH C 3 .   ? -10.590   22.774   45.681   1.000 29.30671  ? 592 HOH A O   1 
HETATM 2251 O  O   . HOH C 3 .   ? -9.03800  15.83800 62.65600 1.000 35.67124  ? 593 HOH A O   1 
HETATM 2252 O  O   . HOH C 3 .   ? 35.591    28.724   57.149   1.000 41.66404  ? 594 HOH A O   1 
HETATM 2253 O  O   . HOH C 3 .   ? 11.29100  30.60500 61.76200 1.000 45.88589  ? 595 HOH A O   1 
HETATM 2254 O  O   . HOH C 3 .   ? 29.24200  19.33500 63.82000 1.000 38.24061  ? 596 HOH A O   1 
HETATM 2255 O  O   . HOH C 3 .   ? 4.16800   11.74600 41.14100 1.000 33.49694  ? 597 HOH A O   1 
HETATM 2256 O  O   . HOH C 3 .   ? 15.14700  33.66800 69.70300 1.000 32.61636  ? 598 HOH A O   1 
HETATM 2257 O  O   . HOH C 3 .   ? 27.48000  15.86500 70.22800 1.000 35.51909  ? 599 HOH A O   1 
HETATM 2258 O  O   . HOH C 3 .   ? 2.15700   26.21900 75.40000 1.000 32.81710  ? 600 HOH A O   1 
HETATM 2259 O  O   . HOH C 3 .   ? -12.664   21.422   44.420   1.000 42.00781  ? 601 HOH A O   1 
HETATM 2260 O  O   . HOH C 3 .   ? -2.81400  31.80000 51.98200 1.000 44.38076  ? 602 HOH A O   1 
HETATM 2261 O  O   . HOH C 3 .   ? 6.10000   28.57100 56.16900 1.000 45.85235  ? 603 HOH A O   1 
HETATM 2262 O  O   . HOH C 3 .   ? 29.60600  33.36000 34.70200 1.000 52.87210  ? 604 HOH A O   1 
# 
