data_9FPV
# 
_entry.id   9FPV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FPV         pdb_00009fpv 10.2210/pdb9fpv/pdb 
WWPDB D_1292139314 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FPV 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-13 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexeyus1@gmail.com 
_pdbx_contact_author.name_first         Alexey 
_pdbx_contact_author.name_last          Smirnov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5080-9367 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'    1 0000-0001-5080-9367 
'Manakova, E.N.' 2 0000-0002-6027-2265 
'Grazulis, S.'   3 0000-0002-7928-5218 
'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of carbonic anhydrase XIII with methyl 4-benzylsulfanyl-3-sulfamoyl-benzoate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'    1 0000-0001-5080-9367 
primary 'Manakova, E.N.' 2 0000-0002-6027-2265 
primary 'Grazulis, S.'   3 0000-0002-7928-5218 
primary 'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
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 13'                                29613.318 2   4.2.1.1 ? 'human carbonic anhydrase XIII' ? 
2 non-polymer syn 'ZINC ION'                                             65.409    2   ?       ? ?                               ? 
3 non-polymer syn 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' 337.414   2   ?       ? ?                               ? 
4 water       nat water                                                  18.015    419 ?       ? ?                               ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII,Carbonic anhydrase XIII,CA-XIII' 
# 
_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       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 B,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 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' A1IEL 
4 water                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   263 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA13 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
A1IEL non-polymer         . 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' ? 'C15 H15 N O4 S2' 337.414 
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   MET 1   1   ?   ?   ?   B . n 
A 1 2   MET 2   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ARG 4   4   ?   ?   ?   B . n 
A 1 5   LEU 5   5   ?   ?   ?   B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   TRP 7   7   7   TRP TRP B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   TYR 9   9   9   TYR TYR B . n 
A 1 10  ARG 10  10  10  ARG ARG B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  PRO 15  15  15  PRO PRO B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  HIS 17  17  17  HIS HIS B . n 
A 1 18  TRP 18  18  18  TRP TRP B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  PHE 21  21  21  PHE PHE B . n 
A 1 22  PHE 22  22  22  PHE PHE B . n 
A 1 23  PRO 23  23  23  PRO PRO B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  ALA 25  25  25  ALA ALA B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLY 27  27  27  GLY GLY B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  GLN 29  29  29  GLN GLN B . n 
A 1 30  GLN 30  30  30  GLN GLN B . n 
A 1 31  SER 31  31  31  SER SER B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  ILE 33  33  33  ILE ILE B . n 
A 1 34  GLU 34  34  34  GLU GLU B . n 
A 1 35  ILE 35  35  35  ILE ILE B . n 
A 1 36  LYS 36  36  36  LYS LYS B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LYS 38  38  38  LYS LYS B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  LYS 41  41  41  LYS LYS B . n 
A 1 42  TYR 42  42  42  TYR TYR B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  SER 45  45  45  SER SER B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  ARG 47  47  47  ARG ARG B . n 
A 1 48  PRO 48  48  48  PRO PRO B . n 
A 1 49  LEU 49  49  49  LEU LEU B . n 
A 1 50  SER 50  50  50  SER SER B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ASP 54  54  54  ASP ASP B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  SER 56  56  56  SER SER B . n 
A 1 57  SER 57  57  57  SER SER B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  LYS 59  59  59  LYS LYS B . n 
A 1 60  ILE 60  60  60  ILE ILE B . n 
A 1 61  ILE 61  61  61  ILE ILE B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  SER 64  64  64  SER SER B . n 
A 1 65  GLY 65  65  65  GLY GLY B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  ASN 69  69  69  ASN ASN B . n 
A 1 70  VAL 70  70  70  VAL VAL B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  PHE 72  72  72  PHE PHE B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  GLU 76  76  76  GLU GLU B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  SER 79  79  79  SER SER B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ARG 82  82  82  ARG ARG B . n 
A 1 83  GLY 83  83  83  GLY GLY B . n 
A 1 84  GLY 84  84  84  GLY GLY B . n 
A 1 85  PRO 85  85  85  PRO PRO B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  TYR 90  90  90  TYR TYR B . n 
A 1 91  ARG 91  91  91  ARG ARG B . n 
A 1 92  LEU 92  92  92  LEU LEU B . n 
A 1 93  ARG 93  93  93  ARG ARG B . n 
A 1 94  GLN 94  94  94  GLN GLN B . n 
A 1 95  VAL 95  95  95  VAL VAL B . n 
A 1 96  HIS 96  96  96  HIS HIS B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  HIS 98  98  98  HIS HIS B . n 
A 1 99  TRP 99  99  99  TRP TRP B . n 
A 1 100 GLY 100 100 100 GLY GLY B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 ALA 102 102 102 ALA ALA B . n 
A 1 103 ASP 103 103 103 ASP ASP B . n 
A 1 104 ASP 104 104 104 ASP ASP B . n 
A 1 105 HIS 105 105 105 HIS HIS B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 SER 107 107 107 SER SER B . n 
A 1 108 GLU 108 108 108 GLU GLU B . n 
A 1 109 HIS 109 109 109 HIS HIS B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 VAL 111 111 111 VAL VAL B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 GLY 113 113 113 GLY GLY B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 SER 115 115 115 SER SER B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 ALA 117 117 117 ALA ALA B . n 
A 1 118 ALA 118 118 118 ALA ALA B . n 
A 1 119 GLU 119 119 119 GLU GLU B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 VAL 123 123 123 VAL VAL B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 TRP 125 125 125 TRP TRP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 SER 127 127 127 SER SER B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LYS 129 129 129 LYS LYS B . n 
A 1 130 TYR 130 130 130 TYR TYR B . n 
A 1 131 PRO 131 131 131 PRO PRO B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 PHE 133 133 133 PHE PHE B . n 
A 1 134 VAL 134 134 134 VAL VAL B . n 
A 1 135 GLU 135 135 135 GLU GLU B . n 
A 1 136 ALA 136 136 136 ALA ALA B . n 
A 1 137 ALA 137 137 137 ALA ALA B . n 
A 1 138 HIS 138 138 138 HIS HIS B . n 
A 1 139 GLU 139 139 139 GLU GLU B . n 
A 1 140 PRO 140 140 140 PRO PRO B . n 
A 1 141 ASP 141 141 141 ASP ASP B . n 
A 1 142 GLY 142 142 142 GLY GLY B . n 
A 1 143 LEU 143 143 143 LEU LEU B . n 
A 1 144 ALA 144 144 144 ALA ALA B . n 
A 1 145 VAL 145 145 145 VAL VAL B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLY 147 147 147 GLY GLY B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 PHE 149 149 149 PHE PHE B . n 
A 1 150 LEU 150 150 150 LEU LEU B . n 
A 1 151 GLN 151 151 151 GLN GLN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 GLY 153 153 153 GLY GLY B . n 
A 1 154 GLU 154 154 154 GLU GLU B . n 
A 1 155 PRO 155 155 155 PRO PRO B . n 
A 1 156 ASN 156 156 156 ASN ASN B . n 
A 1 157 SER 157 157 157 SER SER B . n 
A 1 158 GLN 158 158 158 GLN GLN B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 GLN 160 160 160 GLN GLN B . n 
A 1 161 LYS 161 161 161 LYS LYS B . n 
A 1 162 ILE 162 162 162 ILE ILE B . n 
A 1 163 THR 163 163 163 THR THR B . n 
A 1 164 ASP 164 164 164 ASP ASP B . n 
A 1 165 THR 165 165 165 THR THR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 ASP 167 167 167 ASP ASP B . n 
A 1 168 SER 168 168 168 SER SER B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 LYS 170 170 170 LYS LYS B . n 
A 1 171 GLU 171 171 171 GLU GLU B . n 
A 1 172 LYS 172 172 172 LYS LYS B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 LYS 174 174 174 LYS LYS B . n 
A 1 175 GLN 175 175 175 GLN GLN B . n 
A 1 176 THR 176 176 176 THR THR B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 PHE 178 178 178 PHE PHE B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 ASP 182 182 182 ASP ASP B . n 
A 1 183 LEU 183 183 183 LEU LEU B . n 
A 1 184 LEU 184 184 184 LEU LEU B . n 
A 1 185 SER 185 185 185 SER SER B . n 
A 1 186 LEU 186 186 186 LEU LEU B . n 
A 1 187 LEU 187 187 187 LEU LEU B . n 
A 1 188 PRO 188 188 188 PRO PRO B . n 
A 1 189 PRO 189 189 189 PRO PRO B . n 
A 1 190 SER 190 190 190 SER SER B . n 
A 1 191 TRP 191 191 191 TRP TRP B . n 
A 1 192 ASP 192 192 192 ASP ASP B . n 
A 1 193 TYR 193 193 193 TYR TYR B . n 
A 1 194 TRP 194 194 194 TRP TRP B . n 
A 1 195 THR 195 195 195 THR THR B . n 
A 1 196 TYR 196 196 196 TYR TYR B . n 
A 1 197 PRO 197 197 197 PRO PRO B . n 
A 1 198 GLY 198 198 198 GLY GLY B . n 
A 1 199 SER 199 199 199 SER SER B . n 
A 1 200 LEU 200 200 200 LEU LEU B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 PRO 203 203 203 PRO PRO B . n 
A 1 204 PRO 204 204 204 PRO PRO B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 LEU 206 206 206 LEU LEU B . n 
A 1 207 GLU 207 207 207 GLU GLU B . n 
A 1 208 SER 208 208 208 SER SER B . n 
A 1 209 VAL 209 209 209 VAL VAL B . n 
A 1 210 THR 210 210 210 THR THR B . n 
A 1 211 TRP 211 211 211 TRP TRP B . n 
A 1 212 ILE 212 212 212 ILE ILE B . n 
A 1 213 VAL 213 213 213 VAL VAL B . n 
A 1 214 LEU 214 214 214 LEU LEU B . n 
A 1 215 LYS 215 215 215 LYS LYS B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 PRO 217 217 217 PRO PRO B . n 
A 1 218 ILE 218 218 218 ILE ILE B . n 
A 1 219 ASN 219 219 219 ASN ASN B . n 
A 1 220 ILE 220 220 220 ILE ILE B . n 
A 1 221 SER 221 221 221 SER SER B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 GLN 223 223 223 GLN GLN B . n 
A 1 224 GLN 224 224 224 GLN GLN B . n 
A 1 225 LEU 225 225 225 LEU LEU B . n 
A 1 226 ALA 226 226 226 ALA ALA B . n 
A 1 227 LYS 227 227 227 LYS LYS B . n 
A 1 228 PHE 228 228 228 PHE PHE B . n 
A 1 229 ARG 229 229 229 ARG ARG B . n 
A 1 230 SER 230 230 230 SER SER B . n 
A 1 231 LEU 231 231 231 LEU LEU B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 CYS 233 233 233 CYS CYS B . n 
A 1 234 THR 234 234 234 THR THR B . n 
A 1 235 ALA 235 235 235 ALA ALA B . n 
A 1 236 GLU 236 236 236 GLU GLU B . n 
A 1 237 GLY 237 237 237 GLY GLY B . n 
A 1 238 GLU 238 238 238 GLU GLU B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 ALA 240 240 240 ALA ALA B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 PHE 242 242 242 PHE PHE B . n 
A 1 243 LEU 243 243 243 LEU LEU B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 SER 245 245 245 SER SER B . n 
A 1 246 ASN 246 246 246 ASN ASN B . n 
A 1 247 HIS 247 247 247 HIS HIS B . n 
A 1 248 ARG 248 248 248 ARG ARG B . n 
A 1 249 PRO 249 249 249 PRO PRO B . n 
A 1 250 PRO 250 250 250 PRO PRO B . n 
A 1 251 GLN 251 251 251 GLN GLN B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 LYS 254 254 254 LYS LYS B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 ARG 256 256 256 ARG ARG B . n 
A 1 257 LYS 257 257 257 LYS LYS B . n 
A 1 258 VAL 258 258 258 VAL VAL B . n 
A 1 259 ARG 259 259 259 ARG ARG B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 SER 261 261 261 SER SER B . n 
A 1 262 PHE 262 262 262 PHE PHE B . n 
A 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   MET 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ARG 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   5   LEU LEU A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   TRP 7   7   7   TRP TRP A . n 
B 1 8   GLY 8   8   8   GLY GLY A . n 
B 1 9   TYR 9   9   9   TYR TYR A . n 
B 1 10  ARG 10  10  10  ARG ARG A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  PRO 15  15  15  PRO PRO A . n 
B 1 16  ILE 16  16  16  ILE ILE A . n 
B 1 17  HIS 17  17  17  HIS HIS A . n 
B 1 18  TRP 18  18  18  TRP TRP A . n 
B 1 19  LYS 19  19  19  LYS LYS A . n 
B 1 20  GLU 20  20  20  GLU GLU A . n 
B 1 21  PHE 21  21  21  PHE PHE A . n 
B 1 22  PHE 22  22  22  PHE PHE A . n 
B 1 23  PRO 23  23  23  PRO PRO A . n 
B 1 24  ILE 24  24  24  ILE ILE A . n 
B 1 25  ALA 25  25  25  ALA ALA A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  GLY 27  27  27  GLY GLY A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  GLN 29  29  29  GLN GLN A . n 
B 1 30  GLN 30  30  30  GLN GLN A . n 
B 1 31  SER 31  31  31  SER SER A . n 
B 1 32  PRO 32  32  32  PRO PRO A . n 
B 1 33  ILE 33  33  33  ILE ILE A . n 
B 1 34  GLU 34  34  34  GLU GLU A . n 
B 1 35  ILE 35  35  35  ILE ILE A . n 
B 1 36  LYS 36  36  36  LYS LYS A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LYS 38  38  38  LYS LYS A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  VAL 40  40  40  VAL VAL A . n 
B 1 41  LYS 41  41  41  LYS LYS A . n 
B 1 42  TYR 42  42  42  TYR TYR A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  SER 44  44  44  SER SER A . n 
B 1 45  SER 45  45  45  SER SER A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  ARG 47  47  47  ARG ARG A . n 
B 1 48  PRO 48  48  48  PRO PRO A . n 
B 1 49  LEU 49  49  49  LEU LEU A . n 
B 1 50  SER 50  50  50  SER SER A . n 
B 1 51  ILE 51  51  51  ILE ILE A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ASP 54  54  54  ASP ASP A . n 
B 1 55  PRO 55  55  55  PRO PRO A . n 
B 1 56  SER 56  56  56  SER SER A . n 
B 1 57  SER 57  57  57  SER SER A . n 
B 1 58  ALA 58  58  58  ALA ALA A . n 
B 1 59  LYS 59  59  59  LYS LYS A . n 
B 1 60  ILE 60  60  60  ILE ILE A . n 
B 1 61  ILE 61  61  61  ILE ILE A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  SER 64  64  64  SER SER A . n 
B 1 65  GLY 65  65  65  GLY GLY A . n 
B 1 66  HIS 66  66  66  HIS HIS A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  PHE 68  68  68  PHE PHE A . n 
B 1 69  ASN 69  69  69  ASN ASN A . n 
B 1 70  VAL 70  70  70  VAL VAL A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  PHE 72  72  72  PHE PHE A . n 
B 1 73  ASP 73  73  73  ASP ASP A . n 
B 1 74  ASP 74  74  74  ASP ASP A . n 
B 1 75  THR 75  75  75  THR THR A . n 
B 1 76  GLU 76  76  76  GLU GLU A . n 
B 1 77  ASN 77  77  77  ASN ASN A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  SER 79  79  79  SER SER A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  ARG 82  82  82  ARG ARG A . n 
B 1 83  GLY 83  83  83  GLY GLY A . n 
B 1 84  GLY 84  84  84  GLY GLY A . n 
B 1 85  PRO 85  85  85  PRO PRO A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  GLY 88  88  88  GLY GLY A . n 
B 1 89  SER 89  89  89  SER SER A . n 
B 1 90  TYR 90  90  90  TYR TYR A . n 
B 1 91  ARG 91  91  91  ARG ARG A . n 
B 1 92  LEU 92  92  92  LEU LEU A . n 
B 1 93  ARG 93  93  93  ARG ARG A . n 
B 1 94  GLN 94  94  94  GLN GLN A . n 
B 1 95  VAL 95  95  95  VAL VAL A . n 
B 1 96  HIS 96  96  96  HIS HIS A . n 
B 1 97  LEU 97  97  97  LEU LEU A . n 
B 1 98  HIS 98  98  98  HIS HIS A . n 
B 1 99  TRP 99  99  99  TRP TRP A . n 
B 1 100 GLY 100 100 100 GLY GLY A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 ALA 102 102 102 ALA ALA A . n 
B 1 103 ASP 103 103 103 ASP ASP A . n 
B 1 104 ASP 104 104 104 ASP ASP A . n 
B 1 105 HIS 105 105 105 HIS HIS A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 SER 107 107 107 SER SER A . n 
B 1 108 GLU 108 108 108 GLU GLU A . n 
B 1 109 HIS 109 109 109 HIS HIS A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 VAL 111 111 111 VAL VAL A . n 
B 1 112 ASP 112 112 112 ASP ASP A . n 
B 1 113 GLY 113 113 113 GLY GLY A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 SER 115 115 115 SER SER A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 ALA 117 117 117 ALA ALA A . n 
B 1 118 ALA 118 118 118 ALA ALA A . n 
B 1 119 GLU 119 119 119 GLU GLU A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 HIS 121 121 121 HIS HIS A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 VAL 123 123 123 VAL VAL A . n 
B 1 124 HIS 124 124 124 HIS HIS A . n 
B 1 125 TRP 125 125 125 TRP TRP A . n 
B 1 126 ASN 126 126 126 ASN ASN A . n 
B 1 127 SER 127 127 127 SER SER A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LYS 129 129 129 LYS LYS A . n 
B 1 130 TYR 130 130 130 TYR TYR A . n 
B 1 131 PRO 131 131 131 PRO PRO A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 PHE 133 133 133 PHE PHE A . n 
B 1 134 VAL 134 134 134 VAL VAL A . n 
B 1 135 GLU 135 135 135 GLU GLU A . n 
B 1 136 ALA 136 136 136 ALA ALA A . n 
B 1 137 ALA 137 137 137 ALA ALA A . n 
B 1 138 HIS 138 138 138 HIS HIS A . n 
B 1 139 GLU 139 139 139 GLU GLU A . n 
B 1 140 PRO 140 140 140 PRO PRO A . n 
B 1 141 ASP 141 141 141 ASP ASP A . n 
B 1 142 GLY 142 142 142 GLY GLY A . n 
B 1 143 LEU 143 143 143 LEU LEU A . n 
B 1 144 ALA 144 144 144 ALA ALA A . n 
B 1 145 VAL 145 145 145 VAL VAL A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLY 147 147 147 GLY GLY A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 PHE 149 149 149 PHE PHE A . n 
B 1 150 LEU 150 150 150 LEU LEU A . n 
B 1 151 GLN 151 151 151 GLN GLN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 GLY 153 153 153 GLY GLY A . n 
B 1 154 GLU 154 154 154 GLU GLU A . n 
B 1 155 PRO 155 155 155 PRO PRO A . n 
B 1 156 ASN 156 156 156 ASN ASN A . n 
B 1 157 SER 157 157 157 SER SER A . n 
B 1 158 GLN 158 158 158 GLN GLN A . n 
B 1 159 LEU 159 159 159 LEU LEU A . n 
B 1 160 GLN 160 160 160 GLN GLN A . n 
B 1 161 LYS 161 161 161 LYS LYS A . n 
B 1 162 ILE 162 162 162 ILE ILE A . n 
B 1 163 THR 163 163 163 THR THR A . n 
B 1 164 ASP 164 164 164 ASP ASP A . n 
B 1 165 THR 165 165 165 THR THR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 ASP 167 167 167 ASP ASP A . n 
B 1 168 SER 168 168 168 SER SER A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 LYS 170 170 170 LYS LYS A . n 
B 1 171 GLU 171 171 171 GLU GLU A . n 
B 1 172 LYS 172 172 172 LYS LYS A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 LYS 174 174 174 LYS LYS A . n 
B 1 175 GLN 175 175 175 GLN GLN A . n 
B 1 176 THR 176 176 176 THR THR A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 PHE 178 178 178 PHE PHE A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 ASP 182 182 182 ASP ASP A . n 
B 1 183 LEU 183 183 183 LEU LEU A . n 
B 1 184 LEU 184 184 184 LEU LEU A . n 
B 1 185 SER 185 185 185 SER SER A . n 
B 1 186 LEU 186 186 186 LEU LEU A . n 
B 1 187 LEU 187 187 187 LEU LEU A . n 
B 1 188 PRO 188 188 188 PRO PRO A . n 
B 1 189 PRO 189 189 189 PRO PRO A . n 
B 1 190 SER 190 190 190 SER SER A . n 
B 1 191 TRP 191 191 191 TRP TRP A . n 
B 1 192 ASP 192 192 192 ASP ASP A . n 
B 1 193 TYR 193 193 193 TYR TYR A . n 
B 1 194 TRP 194 194 194 TRP TRP A . n 
B 1 195 THR 195 195 195 THR THR A . n 
B 1 196 TYR 196 196 196 TYR TYR A . n 
B 1 197 PRO 197 197 197 PRO PRO A . n 
B 1 198 GLY 198 198 198 GLY GLY A . n 
B 1 199 SER 199 199 199 SER SER A . n 
B 1 200 LEU 200 200 200 LEU LEU A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 PRO 203 203 203 PRO PRO A . n 
B 1 204 PRO 204 204 204 PRO PRO A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 LEU 206 206 206 LEU LEU A . n 
B 1 207 GLU 207 207 207 GLU GLU A . n 
B 1 208 SER 208 208 208 SER SER A . n 
B 1 209 VAL 209 209 209 VAL VAL A . n 
B 1 210 THR 210 210 210 THR THR A . n 
B 1 211 TRP 211 211 211 TRP TRP A . n 
B 1 212 ILE 212 212 212 ILE ILE A . n 
B 1 213 VAL 213 213 213 VAL VAL A . n 
B 1 214 LEU 214 214 214 LEU LEU A . n 
B 1 215 LYS 215 215 215 LYS LYS A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 PRO 217 217 217 PRO PRO A . n 
B 1 218 ILE 218 218 218 ILE ILE A . n 
B 1 219 ASN 219 219 219 ASN ASN A . n 
B 1 220 ILE 220 220 220 ILE ILE A . n 
B 1 221 SER 221 221 221 SER SER A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 GLN 223 223 223 GLN GLN A . n 
B 1 224 GLN 224 224 224 GLN GLN A . n 
B 1 225 LEU 225 225 225 LEU LEU A . n 
B 1 226 ALA 226 226 226 ALA ALA A . n 
B 1 227 LYS 227 227 227 LYS LYS A . n 
B 1 228 PHE 228 228 228 PHE PHE A . n 
B 1 229 ARG 229 229 229 ARG ARG A . n 
B 1 230 SER 230 230 230 SER SER A . n 
B 1 231 LEU 231 231 231 LEU LEU A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 CYS 233 233 233 CYS CYS A . n 
B 1 234 THR 234 234 234 THR THR A . n 
B 1 235 ALA 235 235 235 ALA ALA A . n 
B 1 236 GLU 236 236 236 GLU GLU A . n 
B 1 237 GLY 237 237 237 GLY GLY A . n 
B 1 238 GLU 238 238 238 GLU GLU A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 ALA 240 240 240 ALA ALA A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 PHE 242 242 242 PHE PHE A . n 
B 1 243 LEU 243 243 243 LEU LEU A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 SER 245 245 245 SER SER A . n 
B 1 246 ASN 246 246 246 ASN ASN A . n 
B 1 247 HIS 247 247 247 HIS HIS A . n 
B 1 248 ARG 248 248 248 ARG ARG A . n 
B 1 249 PRO 249 249 249 PRO PRO A . n 
B 1 250 PRO 250 250 250 PRO PRO A . n 
B 1 251 GLN 251 251 251 GLN GLN A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 LYS 254 254 254 LYS LYS A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 ARG 256 256 256 ARG ARG A . n 
B 1 257 LYS 257 257 257 LYS LYS A . n 
B 1 258 VAL 258 258 258 VAL VAL A . n 
B 1 259 ARG 259 259 259 ARG ARG A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 SER 261 261 261 SER SER A . n 
B 1 262 PHE 262 262 ?   ?   ?   A . n 
B 1 263 HIS 263 263 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IEL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IEL 
_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 
C 2 ZN    1   301 1   ZN    ZN  B . 
D 3 A1IEL 1   302 1   A1IEL J13 B . 
E 2 ZN    1   301 2   ZN    ZN  A . 
F 3 A1IEL 1   302 2   A1IEL J13 A . 
G 4 HOH   1   401 73  HOH   HOH B . 
G 4 HOH   2   402 318 HOH   HOH B . 
G 4 HOH   3   403 261 HOH   HOH B . 
G 4 HOH   4   404 176 HOH   HOH B . 
G 4 HOH   5   405 208 HOH   HOH B . 
G 4 HOH   6   406 364 HOH   HOH B . 
G 4 HOH   7   407 175 HOH   HOH B . 
G 4 HOH   8   408 325 HOH   HOH B . 
G 4 HOH   9   409 270 HOH   HOH B . 
G 4 HOH   10  410 303 HOH   HOH B . 
G 4 HOH   11  411 161 HOH   HOH B . 
G 4 HOH   12  412 294 HOH   HOH B . 
G 4 HOH   13  413 54  HOH   HOH B . 
G 4 HOH   14  414 322 HOH   HOH B . 
G 4 HOH   15  415 182 HOH   HOH B . 
G 4 HOH   16  416 274 HOH   HOH B . 
G 4 HOH   17  417 256 HOH   HOH B . 
G 4 HOH   18  418 153 HOH   HOH B . 
G 4 HOH   19  419 30  HOH   HOH B . 
G 4 HOH   20  420 109 HOH   HOH B . 
G 4 HOH   21  421 378 HOH   HOH B . 
G 4 HOH   22  422 113 HOH   HOH B . 
G 4 HOH   23  423 38  HOH   HOH B . 
G 4 HOH   24  424 315 HOH   HOH B . 
G 4 HOH   25  425 403 HOH   HOH B . 
G 4 HOH   26  426 101 HOH   HOH B . 
G 4 HOH   27  427 308 HOH   HOH B . 
G 4 HOH   28  428 298 HOH   HOH B . 
G 4 HOH   29  429 248 HOH   HOH B . 
G 4 HOH   30  430 212 HOH   HOH B . 
G 4 HOH   31  431 16  HOH   HOH B . 
G 4 HOH   32  432 196 HOH   HOH B . 
G 4 HOH   33  433 230 HOH   HOH B . 
G 4 HOH   34  434 349 HOH   HOH B . 
G 4 HOH   35  435 3   HOH   HOH B . 
G 4 HOH   36  436 24  HOH   HOH B . 
G 4 HOH   37  437 284 HOH   HOH B . 
G 4 HOH   38  438 125 HOH   HOH B . 
G 4 HOH   39  439 72  HOH   HOH B . 
G 4 HOH   40  440 27  HOH   HOH B . 
G 4 HOH   41  441 116 HOH   HOH B . 
G 4 HOH   42  442 361 HOH   HOH B . 
G 4 HOH   43  443 264 HOH   HOH B . 
G 4 HOH   44  444 57  HOH   HOH B . 
G 4 HOH   45  445 140 HOH   HOH B . 
G 4 HOH   46  446 150 HOH   HOH B . 
G 4 HOH   47  447 170 HOH   HOH B . 
G 4 HOH   48  448 282 HOH   HOH B . 
G 4 HOH   49  449 49  HOH   HOH B . 
G 4 HOH   50  450 352 HOH   HOH B . 
G 4 HOH   51  451 295 HOH   HOH B . 
G 4 HOH   52  452 250 HOH   HOH B . 
G 4 HOH   53  453 399 HOH   HOH B . 
G 4 HOH   54  454 84  HOH   HOH B . 
G 4 HOH   55  455 168 HOH   HOH B . 
G 4 HOH   56  456 42  HOH   HOH B . 
G 4 HOH   57  457 117 HOH   HOH B . 
G 4 HOH   58  458 415 HOH   HOH B . 
G 4 HOH   59  459 31  HOH   HOH B . 
G 4 HOH   60  460 209 HOH   HOH B . 
G 4 HOH   61  461 302 HOH   HOH B . 
G 4 HOH   62  462 376 HOH   HOH B . 
G 4 HOH   63  463 289 HOH   HOH B . 
G 4 HOH   64  464 200 HOH   HOH B . 
G 4 HOH   65  465 43  HOH   HOH B . 
G 4 HOH   66  466 149 HOH   HOH B . 
G 4 HOH   67  467 323 HOH   HOH B . 
G 4 HOH   68  468 76  HOH   HOH B . 
G 4 HOH   69  469 389 HOH   HOH B . 
G 4 HOH   70  470 67  HOH   HOH B . 
G 4 HOH   71  471 37  HOH   HOH B . 
G 4 HOH   72  472 64  HOH   HOH B . 
G 4 HOH   73  473 56  HOH   HOH B . 
G 4 HOH   74  474 338 HOH   HOH B . 
G 4 HOH   75  475 136 HOH   HOH B . 
G 4 HOH   76  476 20  HOH   HOH B . 
G 4 HOH   77  477 173 HOH   HOH B . 
G 4 HOH   78  478 234 HOH   HOH B . 
G 4 HOH   79  479 47  HOH   HOH B . 
G 4 HOH   80  480 163 HOH   HOH B . 
G 4 HOH   81  481 262 HOH   HOH B . 
G 4 HOH   82  482 226 HOH   HOH B . 
G 4 HOH   83  483 70  HOH   HOH B . 
G 4 HOH   84  484 326 HOH   HOH B . 
G 4 HOH   85  485 259 HOH   HOH B . 
G 4 HOH   86  486 78  HOH   HOH B . 
G 4 HOH   87  487 157 HOH   HOH B . 
G 4 HOH   88  488 23  HOH   HOH B . 
G 4 HOH   89  489 4   HOH   HOH B . 
G 4 HOH   90  490 134 HOH   HOH B . 
G 4 HOH   91  491 65  HOH   HOH B . 
G 4 HOH   92  492 51  HOH   HOH B . 
G 4 HOH   93  493 11  HOH   HOH B . 
G 4 HOH   94  494 306 HOH   HOH B . 
G 4 HOH   95  495 102 HOH   HOH B . 
G 4 HOH   96  496 189 HOH   HOH B . 
G 4 HOH   97  497 22  HOH   HOH B . 
G 4 HOH   98  498 158 HOH   HOH B . 
G 4 HOH   99  499 369 HOH   HOH B . 
G 4 HOH   100 500 69  HOH   HOH B . 
G 4 HOH   101 501 127 HOH   HOH B . 
G 4 HOH   102 502 362 HOH   HOH B . 
G 4 HOH   103 503 94  HOH   HOH B . 
G 4 HOH   104 504 236 HOH   HOH B . 
G 4 HOH   105 505 55  HOH   HOH B . 
G 4 HOH   106 506 183 HOH   HOH B . 
G 4 HOH   107 507 59  HOH   HOH B . 
G 4 HOH   108 508 167 HOH   HOH B . 
G 4 HOH   109 509 110 HOH   HOH B . 
G 4 HOH   110 510 17  HOH   HOH B . 
G 4 HOH   111 511 351 HOH   HOH B . 
G 4 HOH   112 512 350 HOH   HOH B . 
G 4 HOH   113 513 115 HOH   HOH B . 
G 4 HOH   114 514 331 HOH   HOH B . 
G 4 HOH   115 515 152 HOH   HOH B . 
G 4 HOH   116 516 185 HOH   HOH B . 
G 4 HOH   117 517 181 HOH   HOH B . 
G 4 HOH   118 518 277 HOH   HOH B . 
G 4 HOH   119 519 123 HOH   HOH B . 
G 4 HOH   120 520 233 HOH   HOH B . 
G 4 HOH   121 521 382 HOH   HOH B . 
G 4 HOH   122 522 63  HOH   HOH B . 
G 4 HOH   123 523 130 HOH   HOH B . 
G 4 HOH   124 524 2   HOH   HOH B . 
G 4 HOH   125 525 18  HOH   HOH B . 
G 4 HOH   126 526 383 HOH   HOH B . 
G 4 HOH   127 527 35  HOH   HOH B . 
G 4 HOH   128 528 119 HOH   HOH B . 
G 4 HOH   129 529 231 HOH   HOH B . 
G 4 HOH   130 530 213 HOH   HOH B . 
G 4 HOH   131 531 45  HOH   HOH B . 
G 4 HOH   132 532 107 HOH   HOH B . 
G 4 HOH   133 533 363 HOH   HOH B . 
G 4 HOH   134 534 223 HOH   HOH B . 
G 4 HOH   135 535 235 HOH   HOH B . 
G 4 HOH   136 536 87  HOH   HOH B . 
G 4 HOH   137 537 162 HOH   HOH B . 
G 4 HOH   138 538 202 HOH   HOH B . 
G 4 HOH   139 539 243 HOH   HOH B . 
G 4 HOH   140 540 96  HOH   HOH B . 
G 4 HOH   141 541 287 HOH   HOH B . 
G 4 HOH   142 542 328 HOH   HOH B . 
G 4 HOH   143 543 108 HOH   HOH B . 
G 4 HOH   144 544 190 HOH   HOH B . 
G 4 HOH   145 545 71  HOH   HOH B . 
G 4 HOH   146 546 126 HOH   HOH B . 
G 4 HOH   147 547 186 HOH   HOH B . 
G 4 HOH   148 548 375 HOH   HOH B . 
G 4 HOH   149 549 139 HOH   HOH B . 
G 4 HOH   150 550 388 HOH   HOH B . 
G 4 HOH   151 551 269 HOH   HOH B . 
G 4 HOH   152 552 381 HOH   HOH B . 
G 4 HOH   153 553 379 HOH   HOH B . 
G 4 HOH   154 554 91  HOH   HOH B . 
G 4 HOH   155 555 165 HOH   HOH B . 
G 4 HOH   156 556 89  HOH   HOH B . 
G 4 HOH   157 557 138 HOH   HOH B . 
G 4 HOH   158 558 75  HOH   HOH B . 
G 4 HOH   159 559 193 HOH   HOH B . 
G 4 HOH   160 560 211 HOH   HOH B . 
G 4 HOH   161 561 314 HOH   HOH B . 
G 4 HOH   162 562 135 HOH   HOH B . 
G 4 HOH   163 563 372 HOH   HOH B . 
G 4 HOH   164 564 391 HOH   HOH B . 
G 4 HOH   165 565 133 HOH   HOH B . 
G 4 HOH   166 566 237 HOH   HOH B . 
G 4 HOH   167 567 374 HOH   HOH B . 
G 4 HOH   168 568 242 HOH   HOH B . 
G 4 HOH   169 569 330 HOH   HOH B . 
G 4 HOH   170 570 246 HOH   HOH B . 
G 4 HOH   171 571 333 HOH   HOH B . 
G 4 HOH   172 572 291 HOH   HOH B . 
G 4 HOH   173 573 346 HOH   HOH B . 
G 4 HOH   174 574 358 HOH   HOH B . 
G 4 HOH   175 575 118 HOH   HOH B . 
G 4 HOH   176 576 285 HOH   HOH B . 
G 4 HOH   177 577 348 HOH   HOH B . 
G 4 HOH   178 578 172 HOH   HOH B . 
G 4 HOH   179 579 317 HOH   HOH B . 
G 4 HOH   180 580 180 HOH   HOH B . 
G 4 HOH   181 581 247 HOH   HOH B . 
G 4 HOH   182 582 271 HOH   HOH B . 
G 4 HOH   183 583 402 HOH   HOH B . 
G 4 HOH   184 584 95  HOH   HOH B . 
G 4 HOH   185 585 385 HOH   HOH B . 
G 4 HOH   186 586 81  HOH   HOH B . 
G 4 HOH   187 587 360 HOH   HOH B . 
G 4 HOH   188 588 397 HOH   HOH B . 
G 4 HOH   189 589 220 HOH   HOH B . 
G 4 HOH   190 590 272 HOH   HOH B . 
G 4 HOH   191 591 160 HOH   HOH B . 
G 4 HOH   192 592 347 HOH   HOH B . 
G 4 HOH   193 593 407 HOH   HOH B . 
G 4 HOH   194 594 40  HOH   HOH B . 
G 4 HOH   195 595 355 HOH   HOH B . 
G 4 HOH   196 596 319 HOH   HOH B . 
G 4 HOH   197 597 151 HOH   HOH B . 
G 4 HOH   198 598 401 HOH   HOH B . 
G 4 HOH   199 599 393 HOH   HOH B . 
G 4 HOH   200 600 339 HOH   HOH B . 
G 4 HOH   201 601 390 HOH   HOH B . 
G 4 HOH   202 602 205 HOH   HOH B . 
G 4 HOH   203 603 336 HOH   HOH B . 
G 4 HOH   204 604 332 HOH   HOH B . 
G 4 HOH   205 605 257 HOH   HOH B . 
G 4 HOH   206 606 313 HOH   HOH B . 
G 4 HOH   207 607 310 HOH   HOH B . 
G 4 HOH   208 608 321 HOH   HOH B . 
G 4 HOH   209 609 279 HOH   HOH B . 
G 4 HOH   210 610 384 HOH   HOH B . 
G 4 HOH   211 611 405 HOH   HOH B . 
H 4 HOH   1   401 337 HOH   HOH A . 
H 4 HOH   2   402 316 HOH   HOH A . 
H 4 HOH   3   403 387 HOH   HOH A . 
H 4 HOH   4   404 227 HOH   HOH A . 
H 4 HOH   5   405 312 HOH   HOH A . 
H 4 HOH   6   406 301 HOH   HOH A . 
H 4 HOH   7   407 377 HOH   HOH A . 
H 4 HOH   8   408 419 HOH   HOH A . 
H 4 HOH   9   409 199 HOH   HOH A . 
H 4 HOH   10  410 184 HOH   HOH A . 
H 4 HOH   11  411 194 HOH   HOH A . 
H 4 HOH   12  412 154 HOH   HOH A . 
H 4 HOH   13  413 93  HOH   HOH A . 
H 4 HOH   14  414 265 HOH   HOH A . 
H 4 HOH   15  415 307 HOH   HOH A . 
H 4 HOH   16  416 141 HOH   HOH A . 
H 4 HOH   17  417 100 HOH   HOH A . 
H 4 HOH   18  418 214 HOH   HOH A . 
H 4 HOH   19  419 368 HOH   HOH A . 
H 4 HOH   20  420 137 HOH   HOH A . 
H 4 HOH   21  421 5   HOH   HOH A . 
H 4 HOH   22  422 224 HOH   HOH A . 
H 4 HOH   23  423 15  HOH   HOH A . 
H 4 HOH   24  424 216 HOH   HOH A . 
H 4 HOH   25  425 207 HOH   HOH A . 
H 4 HOH   26  426 244 HOH   HOH A . 
H 4 HOH   27  427 6   HOH   HOH A . 
H 4 HOH   28  428 229 HOH   HOH A . 
H 4 HOH   29  429 206 HOH   HOH A . 
H 4 HOH   30  430 408 HOH   HOH A . 
H 4 HOH   31  431 68  HOH   HOH A . 
H 4 HOH   32  432 219 HOH   HOH A . 
H 4 HOH   33  433 79  HOH   HOH A . 
H 4 HOH   34  434 58  HOH   HOH A . 
H 4 HOH   35  435 41  HOH   HOH A . 
H 4 HOH   36  436 85  HOH   HOH A . 
H 4 HOH   37  437 386 HOH   HOH A . 
H 4 HOH   38  438 273 HOH   HOH A . 
H 4 HOH   39  439 86  HOH   HOH A . 
H 4 HOH   40  440 370 HOH   HOH A . 
H 4 HOH   41  441 178 HOH   HOH A . 
H 4 HOH   42  442 131 HOH   HOH A . 
H 4 HOH   43  443 238 HOH   HOH A . 
H 4 HOH   44  444 33  HOH   HOH A . 
H 4 HOH   45  445 32  HOH   HOH A . 
H 4 HOH   46  446 159 HOH   HOH A . 
H 4 HOH   47  447 254 HOH   HOH A . 
H 4 HOH   48  448 52  HOH   HOH A . 
H 4 HOH   49  449 19  HOH   HOH A . 
H 4 HOH   50  450 13  HOH   HOH A . 
H 4 HOH   51  451 367 HOH   HOH A . 
H 4 HOH   52  452 218 HOH   HOH A . 
H 4 HOH   53  453 147 HOH   HOH A . 
H 4 HOH   54  454 90  HOH   HOH A . 
H 4 HOH   55  455 293 HOH   HOH A . 
H 4 HOH   56  456 329 HOH   HOH A . 
H 4 HOH   57  457 145 HOH   HOH A . 
H 4 HOH   58  458 203 HOH   HOH A . 
H 4 HOH   59  459 48  HOH   HOH A . 
H 4 HOH   60  460 1   HOH   HOH A . 
H 4 HOH   61  461 21  HOH   HOH A . 
H 4 HOH   62  462 62  HOH   HOH A . 
H 4 HOH   63  463 60  HOH   HOH A . 
H 4 HOH   64  464 290 HOH   HOH A . 
H 4 HOH   65  465 292 HOH   HOH A . 
H 4 HOH   66  466 129 HOH   HOH A . 
H 4 HOH   67  467 25  HOH   HOH A . 
H 4 HOH   68  468 414 HOH   HOH A . 
H 4 HOH   69  469 411 HOH   HOH A . 
H 4 HOH   70  470 34  HOH   HOH A . 
H 4 HOH   71  471 10  HOH   HOH A . 
H 4 HOH   72  472 253 HOH   HOH A . 
H 4 HOH   73  473 106 HOH   HOH A . 
H 4 HOH   74  474 320 HOH   HOH A . 
H 4 HOH   75  475 240 HOH   HOH A . 
H 4 HOH   76  476 340 HOH   HOH A . 
H 4 HOH   77  477 251 HOH   HOH A . 
H 4 HOH   78  478 39  HOH   HOH A . 
H 4 HOH   79  479 61  HOH   HOH A . 
H 4 HOH   80  480 29  HOH   HOH A . 
H 4 HOH   81  481 36  HOH   HOH A . 
H 4 HOH   82  482 7   HOH   HOH A . 
H 4 HOH   83  483 99  HOH   HOH A . 
H 4 HOH   84  484 166 HOH   HOH A . 
H 4 HOH   85  485 267 HOH   HOH A . 
H 4 HOH   86  486 50  HOH   HOH A . 
H 4 HOH   87  487 275 HOH   HOH A . 
H 4 HOH   88  488 74  HOH   HOH A . 
H 4 HOH   89  489 296 HOH   HOH A . 
H 4 HOH   90  490 201 HOH   HOH A . 
H 4 HOH   91  491 155 HOH   HOH A . 
H 4 HOH   92  492 122 HOH   HOH A . 
H 4 HOH   93  493 8   HOH   HOH A . 
H 4 HOH   94  494 124 HOH   HOH A . 
H 4 HOH   95  495 169 HOH   HOH A . 
H 4 HOH   96  496 103 HOH   HOH A . 
H 4 HOH   97  497 104 HOH   HOH A . 
H 4 HOH   98  498 98  HOH   HOH A . 
H 4 HOH   99  499 146 HOH   HOH A . 
H 4 HOH   100 500 311 HOH   HOH A . 
H 4 HOH   101 501 252 HOH   HOH A . 
H 4 HOH   102 502 404 HOH   HOH A . 
H 4 HOH   103 503 191 HOH   HOH A . 
H 4 HOH   104 504 97  HOH   HOH A . 
H 4 HOH   105 505 142 HOH   HOH A . 
H 4 HOH   106 506 198 HOH   HOH A . 
H 4 HOH   107 507 144 HOH   HOH A . 
H 4 HOH   108 508 174 HOH   HOH A . 
H 4 HOH   109 509 120 HOH   HOH A . 
H 4 HOH   110 510 44  HOH   HOH A . 
H 4 HOH   111 511 148 HOH   HOH A . 
H 4 HOH   112 512 177 HOH   HOH A . 
H 4 HOH   113 513 210 HOH   HOH A . 
H 4 HOH   114 514 366 HOH   HOH A . 
H 4 HOH   115 515 156 HOH   HOH A . 
H 4 HOH   116 516 356 HOH   HOH A . 
H 4 HOH   117 517 286 HOH   HOH A . 
H 4 HOH   118 518 228 HOH   HOH A . 
H 4 HOH   119 519 217 HOH   HOH A . 
H 4 HOH   120 520 132 HOH   HOH A . 
H 4 HOH   121 521 225 HOH   HOH A . 
H 4 HOH   122 522 342 HOH   HOH A . 
H 4 HOH   123 523 309 HOH   HOH A . 
H 4 HOH   124 524 371 HOH   HOH A . 
H 4 HOH   125 525 215 HOH   HOH A . 
H 4 HOH   126 526 14  HOH   HOH A . 
H 4 HOH   127 527 28  HOH   HOH A . 
H 4 HOH   128 528 82  HOH   HOH A . 
H 4 HOH   129 529 143 HOH   HOH A . 
H 4 HOH   130 530 12  HOH   HOH A . 
H 4 HOH   131 531 417 HOH   HOH A . 
H 4 HOH   132 532 281 HOH   HOH A . 
H 4 HOH   133 533 365 HOH   HOH A . 
H 4 HOH   134 534 26  HOH   HOH A . 
H 4 HOH   135 535 258 HOH   HOH A . 
H 4 HOH   136 536 192 HOH   HOH A . 
H 4 HOH   137 537 114 HOH   HOH A . 
H 4 HOH   138 538 53  HOH   HOH A . 
H 4 HOH   139 539 105 HOH   HOH A . 
H 4 HOH   140 540 9   HOH   HOH A . 
H 4 HOH   141 541 324 HOH   HOH A . 
H 4 HOH   142 542 66  HOH   HOH A . 
H 4 HOH   143 543 164 HOH   HOH A . 
H 4 HOH   144 544 171 HOH   HOH A . 
H 4 HOH   145 545 297 HOH   HOH A . 
H 4 HOH   146 546 300 HOH   HOH A . 
H 4 HOH   147 547 88  HOH   HOH A . 
H 4 HOH   148 548 280 HOH   HOH A . 
H 4 HOH   149 549 92  HOH   HOH A . 
H 4 HOH   150 550 46  HOH   HOH A . 
H 4 HOH   151 551 128 HOH   HOH A . 
H 4 HOH   152 552 195 HOH   HOH A . 
H 4 HOH   153 553 188 HOH   HOH A . 
H 4 HOH   154 554 80  HOH   HOH A . 
H 4 HOH   155 555 121 HOH   HOH A . 
H 4 HOH   156 556 241 HOH   HOH A . 
H 4 HOH   157 557 373 HOH   HOH A . 
H 4 HOH   158 558 83  HOH   HOH A . 
H 4 HOH   159 559 283 HOH   HOH A . 
H 4 HOH   160 560 327 HOH   HOH A . 
H 4 HOH   161 561 239 HOH   HOH A . 
H 4 HOH   162 562 249 HOH   HOH A . 
H 4 HOH   163 563 344 HOH   HOH A . 
H 4 HOH   164 564 357 HOH   HOH A . 
H 4 HOH   165 565 334 HOH   HOH A . 
H 4 HOH   166 566 77  HOH   HOH A . 
H 4 HOH   167 567 276 HOH   HOH A . 
H 4 HOH   168 568 299 HOH   HOH A . 
H 4 HOH   169 569 187 HOH   HOH A . 
H 4 HOH   170 570 179 HOH   HOH A . 
H 4 HOH   171 571 268 HOH   HOH A . 
H 4 HOH   172 572 260 HOH   HOH A . 
H 4 HOH   173 573 395 HOH   HOH A . 
H 4 HOH   174 574 335 HOH   HOH A . 
H 4 HOH   175 575 112 HOH   HOH A . 
H 4 HOH   176 576 288 HOH   HOH A . 
H 4 HOH   177 577 255 HOH   HOH A . 
H 4 HOH   178 578 359 HOH   HOH A . 
H 4 HOH   179 579 304 HOH   HOH A . 
H 4 HOH   180 580 222 HOH   HOH A . 
H 4 HOH   181 581 416 HOH   HOH A . 
H 4 HOH   182 582 204 HOH   HOH A . 
H 4 HOH   183 583 353 HOH   HOH A . 
H 4 HOH   184 584 278 HOH   HOH A . 
H 4 HOH   185 585 245 HOH   HOH A . 
H 4 HOH   186 586 266 HOH   HOH A . 
H 4 HOH   187 587 418 HOH   HOH A . 
H 4 HOH   188 588 197 HOH   HOH A . 
H 4 HOH   189 589 343 HOH   HOH A . 
H 4 HOH   190 590 412 HOH   HOH A . 
H 4 HOH   191 591 341 HOH   HOH A . 
H 4 HOH   192 592 345 HOH   HOH A . 
H 4 HOH   193 593 396 HOH   HOH A . 
H 4 HOH   194 594 400 HOH   HOH A . 
H 4 HOH   195 595 413 HOH   HOH A . 
H 4 HOH   196 596 392 HOH   HOH A . 
H 4 HOH   197 597 305 HOH   HOH A . 
H 4 HOH   198 598 111 HOH   HOH A . 
H 4 HOH   199 599 380 HOH   HOH A . 
H 4 HOH   200 600 354 HOH   HOH A . 
H 4 HOH   201 601 410 HOH   HOH A . 
H 4 HOH   202 602 221 HOH   HOH A . 
H 4 HOH   203 603 232 HOH   HOH A . 
H 4 HOH   204 604 406 HOH   HOH A . 
H 4 HOH   205 605 409 HOH   HOH A . 
H 4 HOH   206 606 398 HOH   HOH A . 
H 4 HOH   207 607 394 HOH   HOH A . 
H 4 HOH   208 608 263 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B LYS 41  ? CD  ? A LYS 41  CD  
2  1 Y 1 B LYS 41  ? CE  ? A LYS 41  CE  
3  1 Y 1 B LYS 41  ? NZ  ? A LYS 41  NZ  
4  1 Y 1 A GLU 11  ? CD  ? B GLU 11  CD  
5  1 Y 1 A GLU 11  ? OE1 ? B GLU 11  OE1 
6  1 Y 1 A GLU 11  ? OE2 ? B GLU 11  OE2 
7  1 Y 1 A LYS 38  ? CG  ? B LYS 38  CG  
8  1 Y 1 A LYS 38  ? CD  ? B LYS 38  CD  
9  1 Y 1 A LYS 38  ? CE  ? B LYS 38  CE  
10 1 Y 1 A LYS 38  ? NZ  ? B LYS 38  NZ  
11 1 Y 1 A GLU 39  ? CD  ? B GLU 39  CD  
12 1 Y 1 A GLU 39  ? OE1 ? B GLU 39  OE1 
13 1 Y 1 A GLU 39  ? OE2 ? B GLU 39  OE2 
14 1 Y 1 A LYS 41  ? CE  ? B LYS 41  CE  
15 1 Y 1 A LYS 41  ? NZ  ? B LYS 41  NZ  
16 1 Y 1 A LYS 227 ? CE  ? B LYS 227 CE  
17 1 Y 1 A LYS 227 ? NZ  ? B LYS 227 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FPV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.054 
_cell.length_a_esd                 ? 
_cell.length_b                     57.958 
_cell.length_b_esd                 ? 
_cell.length_c                     160.174 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9FPV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FPV 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.8 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M sodium citrate pH5.5, 0.1M sodium acetate pH4.5 and 26% of PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-12-20 
_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   0.976200 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FPV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.700 
_reflns.d_resolution_low                               160.174 
_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                                     57402 
_reflns.number_obs                                     57402 
_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                           100.000 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.200 
_reflns.pdbx_netI_over_av_sigmaI                       5.000 
_reflns.pdbx_netI_over_sigmaI                          16.800 
_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                                0.095 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       755947 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.088 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.700 1.790   ? 2.100 107978 ? ? ? 8246 ? ? ? ? ? ? ? ? ? ? ? 13.100 ? ? 7.400  0.347 0.095 ? 1  1 ? ? ? 100.000 ? 0.323 0.323 ? ? 
? ? ? ? ? ? 
1.790 1.900   ? 3.000 99512  ? ? ? 7844 ? ? ? ? ? ? ? ? ? ? ? 12.700 ? ? 9.400  0.238 0.067 ? 2  1 ? ? ? 100.000 ? 0.221 0.221 ? ? 
? ? ? ? ? ? 
1.900 2.030   ? 3.900 100657 ? ? ? 7356 ? ? ? ? ? ? ? ? ? ? ? 13.700 ? ? 12.500 0.176 0.047 ? 3  1 ? ? ? 100.000 ? 0.163 0.163 ? ? 
? ? ? ? ? ? 
2.030 2.190   ? 5.000 92756  ? ? ? 6869 ? ? ? ? ? ? ? ? ? ? ? 13.500 ? ? 15.200 0.141 0.038 ? 4  1 ? ? ? 100.000 ? 0.131 0.131 ? ? 
? ? ? ? ? ? 
2.190 2.400   ? 5.600 80196  ? ? ? 6359 ? ? ? ? ? ? ? ? ? ? ? 12.600 ? ? 16.900 0.123 0.035 ? 5  1 ? ? ? 100.000 ? 0.113 0.113 ? ? 
? ? ? ? ? ? 
2.400 2.690   ? 6.300 80165  ? ? ? 5754 ? ? ? ? ? ? ? ? ? ? ? 13.900 ? ? 20.000 0.108 0.029 ? 6  1 ? ? ? 100.000 ? 0.101 0.101 ? ? 
? ? ? ? ? ? 
2.690 3.100   ? 7.000 69176  ? ? ? 5135 ? ? ? ? ? ? ? ? ? ? ? 13.500 ? ? 23.600 0.097 0.026 ? 7  1 ? ? ? 100.000 ? 0.090 0.090 ? ? 
? ? ? ? ? ? 
3.100 3.800   ? 7.800 55518  ? ? ? 4379 ? ? ? ? ? ? ? ? ? ? ? 12.700 ? ? 28.100 0.082 0.023 ? 8  1 ? ? ? 100.000 ? 0.077 0.077 ? ? 
? ? ? ? ? ? 
3.800 5.380   ? 9.500 45802  ? ? ? 3439 ? ? ? ? ? ? ? ? ? ? ? 13.300 ? ? 32.000 0.069 0.019 ? 9  1 ? ? ? 100.000 ? 0.065 0.065 ? ? 
? ? ? ? ? ? 
5.380 160.174 ? 8.700 24187  ? ? ? 2021 ? ? ? ? ? ? ? ? ? ? ? 12.000 ? ? 28.300 0.065 0.019 ? 10 1 ? ? ? 100.000 ? 0.060 0.060 ? ? 
? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.8100 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.8200 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -1.6300 
_refine.B_iso_max                                71.790 
_refine.B_iso_mean                               21.6140 
_refine.B_iso_min                                9.260 
_refine.correlation_coeff_Fo_to_Fc               0.9670 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 9FPV 
_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                            1.7000 
_refine.ls_d_res_low                             80.0900 
_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                     51466 
_refine.ls_number_reflns_R_free                  5801 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1611 
_refine.ls_R_factor_R_free                       0.1942 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1576 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1040 
_refine.pdbx_overall_ESU_R_Free                  0.1020 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.7000 
_refine_hist.d_res_low                        80.0900 
_refine_hist.number_atoms_solvent             419 
_refine_hist.number_atoms_total               4542 
_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       515 
_refine_hist.pdbx_B_iso_mean_ligand           31.60 
_refine_hist.pdbx_B_iso_mean_solvent          32.03 
_refine_hist.pdbx_number_atoms_protein        4077 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  4308 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.897  1.644  5882 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.807  5.000  527  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 30.523 22.837 215  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.652 15.000 680  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.974 15.000 20   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  540  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  3381 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7000 
_refine_ls_shell.d_res_low                        1.7440 
_refine_ls_shell.number_reflns_all                4146 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             418 
_refine_ls_shell.number_reflns_R_work             3728 
_refine_ls_shell.percent_reflns_obs               99.6400 
_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            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1570 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2010 
# 
_struct.entry_id                     9FPV 
_struct.title                        
'Crystal structure of carbonic anhydrase XIII with methyl 4-benzylsulfanyl-3-sulfamoyl-benzoate' 
_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        9FPV 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE, LYASE-LYASE INHIBITOR COMPLEX, 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FPV B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 9FPV A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FPV MET B 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 1 
2 9FPV MET A 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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 14  ? PHE A 21  ? GLY B 14  PHE B 21  5 ? 8 
HELX_P HELX_P2  AA2 PHE A 22  ? GLY A 27  ? PHE B 22  GLY B 27  5 ? 6 
HELX_P HELX_P3  AA3 SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P4  AA4 ASN A 156 ? GLN A 158 ? ASN B 156 GLN B 158 5 ? 3 
HELX_P HELX_P5  AA5 LEU A 159 ? LEU A 166 ? LEU B 159 LEU B 166 1 ? 8 
HELX_P HELX_P6  AA6 ASP A 167 ? LYS A 170 ? ASP B 167 LYS B 170 5 ? 4 
HELX_P HELX_P7  AA7 ASP A 182 ? LEU A 187 ? ASP B 182 LEU B 187 1 ? 6 
HELX_P HELX_P8  AA8 SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9 
HELX_P HELX_P9  AA9 GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P10 AB1 PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P11 AB2 LYS B 36  ? VAL B 40  ? LYS A 36  VAL A 40  5 ? 5 
HELX_P HELX_P12 AB3 ASP B 54  ? SER B 56  ? ASP A 54  SER A 56  5 ? 3 
HELX_P HELX_P13 AB4 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P14 AB5 ASN B 156 ? GLN B 158 ? ASN A 156 GLN A 158 5 ? 3 
HELX_P HELX_P15 AB6 LEU B 159 ? ASP B 164 ? LEU A 159 ASP A 164 1 ? 6 
HELX_P HELX_P16 AB7 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P17 AB8 ASP B 182 ? LEU B 187 ? ASP A 182 LEU A 187 5 ? 6 
HELX_P HELX_P18 AB9 SER B 221 ? ARG B 229 ? SER A 221 ARG A 229 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 96  NE2 ? ? ? 1_555 C ZN    . ZN  ? ? B HIS 96  B ZN    301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN    . ZN  ? ? B HIS 98  B ZN    301 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc3  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN    . ZN  ? ? B HIS 121 B ZN    301 1_555 ? ? ? ? ? ? ? 1.942 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D A1IEL . S11 ? ? B ZN  301 B A1IEL 302 1_555 ? ? ? ? ? ? ? 2.890 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D A1IEL . N13 ? ? B ZN  301 B A1IEL 302 1_555 ? ? ? ? ? ? ? 1.837 ? ? 
metalc6  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc7  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 98  A ZN    301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc8  metalc ? ? B HIS 121 ND1 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 121 A ZN    301 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
metalc9  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F A1IEL . S11 ? ? A ZN  301 A A1IEL 302 1_555 ? ? ? ? ? ? ? 2.920 ? ? 
metalc10 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F A1IEL . N13 ? ? A ZN  301 A A1IEL 302 1_555 ? ? ? ? ? ? ? 1.710 ? ? 
# 
_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   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS   98  ? B HIS   98  ? 1_555 103.0 ? 
2  NE2 ? A HIS   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS   121 ? B HIS   121 ? 1_555 111.9 ? 
3  NE2 ? A HIS   98  ? B HIS   98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS   121 ? B HIS   121 ? 1_555 97.2  ? 
4  NE2 ? A HIS   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S11 ? D A1IEL .   ? B A1IEL 302 ? 1_555 92.6  ? 
5  NE2 ? A HIS   98  ? B HIS   98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S11 ? D A1IEL .   ? B A1IEL 302 ? 1_555 135.6 ? 
6  ND1 ? A HIS   121 ? B HIS   121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S11 ? D A1IEL .   ? B A1IEL 302 ? 1_555 115.2 ? 
7  NE2 ? A HIS   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N13 ? D A1IEL .   ? B A1IEL 302 ? 1_555 121.3 ? 
8  NE2 ? A HIS   98  ? B HIS   98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N13 ? D A1IEL .   ? B A1IEL 302 ? 1_555 102.1 ? 
9  ND1 ? A HIS   121 ? B HIS   121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N13 ? D A1IEL .   ? B A1IEL 302 ? 1_555 116.4 ? 
10 S11 ? D A1IEL .   ? B A1IEL 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N13 ? D A1IEL .   ? B A1IEL 302 ? 1_555 37.1  ? 
11 NE2 ? B HIS   96  ? A HIS   96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS   98  ? A HIS   98  ? 1_555 100.7 ? 
12 NE2 ? B HIS   96  ? A HIS   96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS   121 ? A HIS   121 ? 1_555 112.9 ? 
13 NE2 ? B HIS   98  ? A HIS   98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS   121 ? A HIS   121 ? 1_555 96.2  ? 
14 NE2 ? B HIS   96  ? A HIS   96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S11 ? F A1IEL .   ? A A1IEL 302 ? 1_555 91.4  ? 
15 NE2 ? B HIS   98  ? A HIS   98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S11 ? F A1IEL .   ? A A1IEL 302 ? 1_555 136.6 ? 
16 ND1 ? B HIS   121 ? A HIS   121 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S11 ? F A1IEL .   ? A A1IEL 302 ? 1_555 117.1 ? 
17 NE2 ? B HIS   96  ? A HIS   96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N13 ? F A1IEL .   ? A A1IEL 302 ? 1_555 119.8 ? 
18 NE2 ? B HIS   98  ? A HIS   98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N13 ? F A1IEL .   ? A A1IEL 302 ? 1_555 109.8 ? 
19 ND1 ? B HIS   121 ? A HIS   121 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N13 ? F A1IEL .   ? A A1IEL 302 ? 1_555 113.6 ? 
20 S11 ? F A1IEL .   ? A A1IEL 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N13 ? F A1IEL .   ? A A1IEL 302 ? 1_555 33.0  ? 
# 
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 31  A . ? SER 31  B PRO 32  A ? PRO 32  B 1 1.85  
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 6.93  
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -5.76 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 3.99  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 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      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 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  GLU A 34  ? ILE A 35  ? GLU B 34  ILE B 35  
AA1 2  ILE A 110 ? VAL A 111 ? ILE B 110 VAL B 111 
AA2 1  LYS A 41  ? TYR A 42  ? LYS B 41  TYR B 42  
AA2 2  ARG A 259 ? ALA A 260 ? ARG B 259 ALA B 260 
AA2 3  TYR A 193 ? GLY A 198 ? TYR B 193 GLY B 198 
AA2 4  VAL A 209 ? LEU A 214 ? VAL B 209 LEU B 214 
AA2 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
AA2 6  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
AA2 7  SER A 89  ? TRP A 99  ? SER B 89  TRP B 99  
AA2 8  PHE A 68  ? PHE A 72  ? PHE B 68  PHE B 72  
AA2 9  ALA A 58  ? ASN A 63  ? ALA B 58  ASN B 63  
AA2 10 GLN A 175 ? ARG A 177 ? GLN B 175 ARG B 177 
AA3 1  LEU A 49  ? LYS A 52  ? LEU B 49  LYS B 52  
AA3 2  VAL A 80  ? GLY A 83  ? VAL B 80  GLY B 83  
AA3 3  SER A 89  ? TRP A 99  ? SER B 89  TRP B 99  
AA3 4  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
AA3 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
AA3 6  ILE A 218 ? ILE A 220 ? ILE B 218 ILE B 220 
AA4 1  GLU B 34  ? ILE B 35  ? GLU A 34  ILE A 35  
AA4 2  ILE B 110 ? VAL B 111 ? ILE A 110 VAL A 111 
AA5 1  LYS B 41  ? TYR B 42  ? LYS A 41  TYR A 42  
AA5 2  ARG B 259 ? ALA B 260 ? ARG A 259 ALA A 260 
AA5 3  TYR B 193 ? GLY B 198 ? TYR A 193 GLY A 198 
AA5 4  VAL B 209 ? LEU B 214 ? VAL A 209 LEU A 214 
AA5 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
AA5 6  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
AA5 7  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
AA5 8  PHE B 68  ? PHE B 72  ? PHE A 68  PHE A 72  
AA5 9  ALA B 58  ? ASN B 63  ? ALA A 58  ASN A 63  
AA5 10 GLN B 175 ? ARG B 177 ? GLN A 175 ARG A 177 
AA6 1  LEU B 49  ? LYS B 52  ? LEU A 49  LYS A 52  
AA6 2  VAL B 80  ? GLY B 83  ? VAL A 80  GLY A 83  
AA6 3  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
AA6 4  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
AA6 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
AA6 6  ILE B 218 ? ILE B 220 ? ILE A 218 ILE A 220 
# 
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 35  ? N ILE B 35  O ILE A 110 ? O ILE B 110 
AA2 1 2  N LYS A 41  ? N LYS B 41  O ALA A 260 ? O ALA B 260 
AA2 2 3  O ARG A 259 ? O ARG B 259 N THR A 195 ? N THR B 195 
AA2 3 4  N GLY A 198 ? N GLY B 198 O VAL A 209 ? O VAL B 209 
AA2 4 5  O LEU A 214 ? O LEU B 214 N GLY A 147 ? N GLY B 147 
AA2 5 6  O VAL A 148 ? O VAL B 148 N LEU A 120 ? N LEU B 120 
AA2 6 7  O VAL A 123 ? O VAL B 123 N GLN A 94  ? N GLN B 94  
AA2 7 8  O VAL A 95  ? O VAL B 95  N VAL A 70  ? N VAL B 70  
AA2 8 9  O ASP A 71  ? O ASP B 71  N ILE A 60  ? N ILE B 60  
AA2 9 10 N ILE A 61  ? N ILE B 61  O THR A 176 ? O THR B 176 
AA3 1 2  N SER A 50  ? N SER B 50  O ARG A 82  ? O ARG B 82  
AA3 2 3  N LEU A 81  ? N LEU B 81  O TYR A 90  ? O TYR B 90  
AA3 3 4  N GLN A 94  ? N GLN B 94  O VAL A 123 ? O VAL B 123 
AA3 4 5  N LEU A 120 ? N LEU B 120 O VAL A 148 ? O VAL B 148 
AA3 5 6  N GLN A 151 ? N GLN B 151 O ILE A 218 ? O ILE B 218 
AA4 1 2  N ILE B 35  ? N ILE A 35  O ILE B 110 ? O ILE A 110 
AA5 1 2  N LYS B 41  ? N LYS A 41  O ALA B 260 ? O ALA A 260 
AA5 2 3  O ARG B 259 ? O ARG A 259 N THR B 195 ? N THR A 195 
AA5 3 4  N GLY B 198 ? N GLY A 198 O VAL B 209 ? O VAL A 209 
AA5 4 5  O LEU B 214 ? O LEU A 214 N GLY B 147 ? N GLY A 147 
AA5 5 6  O VAL B 148 ? O VAL A 148 N LEU B 120 ? N LEU A 120 
AA5 6 7  O VAL B 123 ? O VAL A 123 N GLN B 94  ? N GLN A 94  
AA5 7 8  O VAL B 95  ? O VAL A 95  N VAL B 70  ? N VAL A 70  
AA5 8 9  O ASP B 71  ? O ASP A 71  N LYS B 59  ? N LYS A 59  
AA5 9 10 N ILE B 61  ? N ILE A 61  O THR B 176 ? O THR A 176 
AA6 1 2  N SER B 50  ? N SER A 50  O ARG B 82  ? O ARG A 82  
AA6 2 3  N LEU B 81  ? N LEU A 81  O TYR B 90  ? O TYR A 90  
AA6 3 4  N GLN B 94  ? N GLN A 94  O VAL B 123 ? O VAL A 123 
AA6 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
AA6 5 6  N PHE B 149 ? N PHE A 149 O ILE B 218 ? O ILE A 218 
# 
_pdbx_entry_details.entry_id                   9FPV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 LYS B 59  ? ? -134.58 -38.90  
2 1 SER B 67  ? ? -172.56 -179.26 
3 1 GLU B 76  ? ? -143.20 -155.48 
4 1 ASN B 77  ? ? -105.46 41.96   
5 1 HIS B 105 ? ? -152.84 74.39   
6 1 ASN B 246 ? ? -154.24 42.76   
7 1 SER A 67  ? ? -171.06 -178.21 
8 1 HIS A 105 ? ? -161.98 105.96  
9 1 ASN A 246 ? ? -146.45 39.14   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B MET 1   ? A MET 1   
2  1 Y 1 B MET 2   ? A MET 2   
3  1 Y 1 B SER 3   ? A SER 3   
4  1 Y 1 B ARG 4   ? A ARG 4   
5  1 Y 1 B LEU 5   ? A LEU 5   
6  1 Y 1 A MET 1   ? B MET 1   
7  1 Y 1 A MET 2   ? B MET 2   
8  1 Y 1 A SER 3   ? B SER 3   
9  1 Y 1 A ARG 4   ? B ARG 4   
10 1 Y 1 A PHE 262 ? B PHE 262 
11 1 Y 1 A HIS 263 ? B HIS 263 
# 
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 
A1IEL C1   C  Y N 1   
A1IEL C2   C  Y N 2   
A1IEL C3   C  Y N 3   
A1IEL C4   C  Y N 4   
A1IEL C5   C  Y N 5   
A1IEL C6   C  Y N 6   
A1IEL C9   C  N N 7   
A1IEL C16  C  N N 8   
A1IEL C20  C  Y N 9   
A1IEL O14  O  N N 10  
A1IEL S11  S  N N 11  
A1IEL O12  O  N N 12  
A1IEL N13  N  N N 13  
A1IEL C7   C  N N 14  
A1IEL O10  O  N N 15  
A1IEL O8   O  N N 16  
A1IEL S15  S  N N 17  
A1IEL C17  C  Y N 18  
A1IEL C21  C  Y N 19  
A1IEL C22  C  Y N 20  
A1IEL C19  C  Y N 21  
A1IEL C18  C  Y N 22  
A1IEL H1   H  N N 23  
A1IEL H2   H  N N 24  
A1IEL H3   H  N N 25  
A1IEL H4   H  N N 26  
A1IEL H5   H  N N 27  
A1IEL H6   H  N N 28  
A1IEL H7   H  N N 29  
A1IEL H8   H  N N 30  
A1IEL H9   H  N N 31  
A1IEL H10  H  N N 32  
A1IEL H11  H  N N 33  
A1IEL H12  H  N N 34  
A1IEL H13  H  N N 35  
A1IEL H14  H  N N 36  
A1IEL H15  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
PHE   N    N  N N 287 
PHE   CA   C  N S 288 
PHE   C    C  N N 289 
PHE   O    O  N N 290 
PHE   CB   C  N N 291 
PHE   CG   C  Y N 292 
PHE   CD1  C  Y N 293 
PHE   CD2  C  Y N 294 
PHE   CE1  C  Y N 295 
PHE   CE2  C  Y N 296 
PHE   CZ   C  Y N 297 
PHE   OXT  O  N N 298 
PHE   H    H  N N 299 
PHE   H2   H  N N 300 
PHE   HA   H  N N 301 
PHE   HB2  H  N N 302 
PHE   HB3  H  N N 303 
PHE   HD1  H  N N 304 
PHE   HD2  H  N N 305 
PHE   HE1  H  N N 306 
PHE   HE2  H  N N 307 
PHE   HZ   H  N N 308 
PHE   HXT  H  N N 309 
PRO   N    N  N N 310 
PRO   CA   C  N S 311 
PRO   C    C  N N 312 
PRO   O    O  N N 313 
PRO   CB   C  N N 314 
PRO   CG   C  N N 315 
PRO   CD   C  N N 316 
PRO   OXT  O  N N 317 
PRO   H    H  N N 318 
PRO   HA   H  N N 319 
PRO   HB2  H  N N 320 
PRO   HB3  H  N N 321 
PRO   HG2  H  N N 322 
PRO   HG3  H  N N 323 
PRO   HD2  H  N N 324 
PRO   HD3  H  N N 325 
PRO   HXT  H  N N 326 
SER   N    N  N N 327 
SER   CA   C  N S 328 
SER   C    C  N N 329 
SER   O    O  N N 330 
SER   CB   C  N N 331 
SER   OG   O  N N 332 
SER   OXT  O  N N 333 
SER   H    H  N N 334 
SER   H2   H  N N 335 
SER   HA   H  N N 336 
SER   HB2  H  N N 337 
SER   HB3  H  N N 338 
SER   HG   H  N N 339 
SER   HXT  H  N N 340 
THR   N    N  N N 341 
THR   CA   C  N S 342 
THR   C    C  N N 343 
THR   O    O  N N 344 
THR   CB   C  N R 345 
THR   OG1  O  N N 346 
THR   CG2  C  N N 347 
THR   OXT  O  N N 348 
THR   H    H  N N 349 
THR   H2   H  N N 350 
THR   HA   H  N N 351 
THR   HB   H  N N 352 
THR   HG1  H  N N 353 
THR   HG21 H  N N 354 
THR   HG22 H  N N 355 
THR   HG23 H  N N 356 
THR   HXT  H  N N 357 
TRP   N    N  N N 358 
TRP   CA   C  N S 359 
TRP   C    C  N N 360 
TRP   O    O  N N 361 
TRP   CB   C  N N 362 
TRP   CG   C  Y N 363 
TRP   CD1  C  Y N 364 
TRP   CD2  C  Y N 365 
TRP   NE1  N  Y N 366 
TRP   CE2  C  Y N 367 
TRP   CE3  C  Y N 368 
TRP   CZ2  C  Y N 369 
TRP   CZ3  C  Y N 370 
TRP   CH2  C  Y N 371 
TRP   OXT  O  N N 372 
TRP   H    H  N N 373 
TRP   H2   H  N N 374 
TRP   HA   H  N N 375 
TRP   HB2  H  N N 376 
TRP   HB3  H  N N 377 
TRP   HD1  H  N N 378 
TRP   HE1  H  N N 379 
TRP   HE3  H  N N 380 
TRP   HZ2  H  N N 381 
TRP   HZ3  H  N N 382 
TRP   HH2  H  N N 383 
TRP   HXT  H  N N 384 
TYR   N    N  N N 385 
TYR   CA   C  N S 386 
TYR   C    C  N N 387 
TYR   O    O  N N 388 
TYR   CB   C  N N 389 
TYR   CG   C  Y N 390 
TYR   CD1  C  Y N 391 
TYR   CD2  C  Y N 392 
TYR   CE1  C  Y N 393 
TYR   CE2  C  Y N 394 
TYR   CZ   C  Y N 395 
TYR   OH   O  N N 396 
TYR   OXT  O  N N 397 
TYR   H    H  N N 398 
TYR   H2   H  N N 399 
TYR   HA   H  N N 400 
TYR   HB2  H  N N 401 
TYR   HB3  H  N N 402 
TYR   HD1  H  N N 403 
TYR   HD2  H  N N 404 
TYR   HE1  H  N N 405 
TYR   HE2  H  N N 406 
TYR   HH   H  N N 407 
TYR   HXT  H  N N 408 
VAL   N    N  N N 409 
VAL   CA   C  N S 410 
VAL   C    C  N N 411 
VAL   O    O  N N 412 
VAL   CB   C  N N 413 
VAL   CG1  C  N N 414 
VAL   CG2  C  N N 415 
VAL   OXT  O  N N 416 
VAL   H    H  N N 417 
VAL   H2   H  N N 418 
VAL   HA   H  N N 419 
VAL   HB   H  N N 420 
VAL   HG11 H  N N 421 
VAL   HG12 H  N N 422 
VAL   HG13 H  N N 423 
VAL   HG21 H  N N 424 
VAL   HG22 H  N N 425 
VAL   HG23 H  N N 426 
VAL   HXT  H  N N 427 
ZN    ZN   ZN N N 428 
# 
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 
A1IEL C9  O8   sing N N 1   
A1IEL O8  C7   sing N N 2   
A1IEL O10 C7   doub N N 3   
A1IEL C7  C1   sing N N 4   
A1IEL C1  C2   doub Y N 5   
A1IEL C1  C6   sing Y N 6   
A1IEL N13 S11  sing N N 7   
A1IEL C2  C3   sing Y N 8   
A1IEL C6  C5   doub Y N 9   
A1IEL C3  S11  sing N N 10  
A1IEL C3  C4   doub Y N 11  
A1IEL S11 O12  doub N N 12  
A1IEL S11 O14  doub N N 13  
A1IEL C5  C4   sing Y N 14  
A1IEL C4  S15  sing N N 15  
A1IEL S15 C16  sing N N 16  
A1IEL C16 C17  sing N N 17  
A1IEL C20 C17  doub Y N 18  
A1IEL C20 C21  sing Y N 19  
A1IEL C17 C18  sing Y N 20  
A1IEL C21 C22  doub Y N 21  
A1IEL C18 C19  doub Y N 22  
A1IEL C22 C19  sing Y N 23  
A1IEL C2  H1   sing N N 24  
A1IEL C5  H2   sing N N 25  
A1IEL C6  H3   sing N N 26  
A1IEL C9  H4   sing N N 27  
A1IEL C9  H5   sing N N 28  
A1IEL C9  H6   sing N N 29  
A1IEL C16 H7   sing N N 30  
A1IEL C16 H8   sing N N 31  
A1IEL C20 H9   sing N N 32  
A1IEL N13 H10  sing N N 33  
A1IEL N13 H11  sing N N 34  
A1IEL C21 H12  sing N N 35  
A1IEL C22 H13  sing N N 36  
A1IEL C19 H14  sing N N 37  
A1IEL C18 H15  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TRP   N   CA   sing N N 344 
TRP   N   H    sing N N 345 
TRP   N   H2   sing N N 346 
TRP   CA  C    sing N N 347 
TRP   CA  CB   sing N N 348 
TRP   CA  HA   sing N N 349 
TRP   C   O    doub N N 350 
TRP   C   OXT  sing N N 351 
TRP   CB  CG   sing N N 352 
TRP   CB  HB2  sing N N 353 
TRP   CB  HB3  sing N N 354 
TRP   CG  CD1  doub Y N 355 
TRP   CG  CD2  sing Y N 356 
TRP   CD1 NE1  sing Y N 357 
TRP   CD1 HD1  sing N N 358 
TRP   CD2 CE2  doub Y N 359 
TRP   CD2 CE3  sing Y N 360 
TRP   NE1 CE2  sing Y N 361 
TRP   NE1 HE1  sing N N 362 
TRP   CE2 CZ2  sing Y N 363 
TRP   CE3 CZ3  doub Y N 364 
TRP   CE3 HE3  sing N N 365 
TRP   CZ2 CH2  doub Y N 366 
TRP   CZ2 HZ2  sing N N 367 
TRP   CZ3 CH2  sing Y N 368 
TRP   CZ3 HZ3  sing N N 369 
TRP   CH2 HH2  sing N N 370 
TRP   OXT HXT  sing N N 371 
TYR   N   CA   sing N N 372 
TYR   N   H    sing N N 373 
TYR   N   H2   sing N N 374 
TYR   CA  C    sing N N 375 
TYR   CA  CB   sing N N 376 
TYR   CA  HA   sing N N 377 
TYR   C   O    doub N N 378 
TYR   C   OXT  sing N N 379 
TYR   CB  CG   sing N N 380 
TYR   CB  HB2  sing N N 381 
TYR   CB  HB3  sing N N 382 
TYR   CG  CD1  doub Y N 383 
TYR   CG  CD2  sing Y N 384 
TYR   CD1 CE1  sing Y N 385 
TYR   CD1 HD1  sing N N 386 
TYR   CD2 CE2  doub Y N 387 
TYR   CD2 HD2  sing N N 388 
TYR   CE1 CZ   doub Y N 389 
TYR   CE1 HE1  sing N N 390 
TYR   CE2 CZ   sing Y N 391 
TYR   CE2 HE2  sing N N 392 
TYR   CZ  OH   sing N N 393 
TYR   OH  HH   sing N N 394 
TYR   OXT HXT  sing N N 395 
VAL   N   CA   sing N N 396 
VAL   N   H    sing N N 397 
VAL   N   H2   sing N N 398 
VAL   CA  C    sing N N 399 
VAL   CA  CB   sing N N 400 
VAL   CA  HA   sing N N 401 
VAL   C   O    doub N N 402 
VAL   C   OXT  sing N N 403 
VAL   CB  CG1  sing N N 404 
VAL   CB  CG2  sing N N 405 
VAL   CB  HB   sing N N 406 
VAL   CG1 HG11 sing N N 407 
VAL   CG1 HG12 sing N N 408 
VAL   CG1 HG13 sing N N 409 
VAL   CG2 HG21 sing N N 410 
VAL   CG2 HG22 sing N N 411 
VAL   CG2 HG23 sing N N 412 
VAL   OXT HXT  sing N N 413 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5LLN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FPV 
_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]   0.018164 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017254 
_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]   0.006243 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . SER   A 1 6   ? 1.544   13.364  12.437 1.00 41.28 ? 6   SER   B N   1 
ATOM   2    C  CA  . SER   A 1 6   ? 0.758   12.301  13.120 1.00 42.28 ? 6   SER   B CA  1 
ATOM   3    C  C   . SER   A 1 6   ? 0.655   11.078  12.214 1.00 36.14 ? 6   SER   B C   1 
ATOM   4    O  O   . SER   A 1 6   ? 0.752   11.192  10.988 1.00 34.61 ? 6   SER   B O   1 
ATOM   5    C  CB  . SER   A 1 6   ? -0.606  12.786  13.491 1.00 47.00 ? 6   SER   B CB  1 
ATOM   6    O  OG  . SER   A 1 6   ? -1.096  12.037  14.592 1.00 54.32 ? 6   SER   B OG  1 
ATOM   7    N  N   . TRP   A 1 7   ? 0.373   9.926   12.826 1.00 26.70 ? 7   TRP   B N   1 
ATOM   8    C  CA  . TRP   A 1 7   ? 0.681   8.636   12.202 1.00 22.13 ? 7   TRP   B CA  1 
ATOM   9    C  C   . TRP   A 1 7   ? -0.388  8.245   11.182 1.00 19.55 ? 7   TRP   B C   1 
ATOM   10   O  O   . TRP   A 1 7   ? -1.544  8.655   11.286 1.00 23.06 ? 7   TRP   B O   1 
ATOM   11   C  CB  . TRP   A 1 7   ? 0.859   7.536   13.268 1.00 21.45 ? 7   TRP   B CB  1 
ATOM   12   C  CG  . TRP   A 1 7   ? -0.398  7.142   13.969 1.00 21.75 ? 7   TRP   B CG  1 
ATOM   13   C  CD1 . TRP   A 1 7   ? -0.935  7.680   15.109 1.00 22.68 ? 7   TRP   B CD1 1 
ATOM   14   C  CD2 . TRP   A 1 7   ? -1.307  6.116   13.534 1.00 19.87 ? 7   TRP   B CD2 1 
ATOM   15   N  NE1 . TRP   A 1 7   ? -2.137  7.082   15.391 1.00 24.33 ? 7   TRP   B NE1 1 
ATOM   16   C  CE2 . TRP   A 1 7   ? -2.391  6.121   14.445 1.00 20.28 ? 7   TRP   B CE2 1 
ATOM   17   C  CE3 . TRP   A 1 7   ? -1.302  5.196   12.464 1.00 19.49 ? 7   TRP   B CE3 1 
ATOM   18   C  CZ2 . TRP   A 1 7   ? -3.445  5.202   14.328 1.00 19.49 ? 7   TRP   B CZ2 1 
ATOM   19   C  CZ3 . TRP   A 1 7   ? -2.370  4.330   12.306 1.00 17.23 ? 7   TRP   B CZ3 1 
ATOM   20   C  CH2 . TRP   A 1 7   ? -3.403  4.337   13.254 1.00 18.98 ? 7   TRP   B CH2 1 
ATOM   21   N  N   . GLY   A 1 8   ? 0.032   7.439   10.207 1.00 19.45 ? 8   GLY   B N   1 
ATOM   22   C  CA  . GLY   A 1 8   ? -0.873  6.896   9.212  1.00 18.68 ? 8   GLY   B CA  1 
ATOM   23   C  C   . GLY   A 1 8   ? -0.187  5.826   8.382  1.00 17.36 ? 8   GLY   B C   1 
ATOM   24   O  O   . GLY   A 1 8   ? 0.645   5.078   8.895  1.00 17.95 ? 8   GLY   B O   1 
ATOM   25   N  N   . TYR   A 1 9   ? -0.536  5.767   7.089  1.00 16.58 ? 9   TYR   B N   1 
ATOM   26   C  CA  . TYR   A 1 9   ? -0.010  4.704   6.250  1.00 15.64 ? 9   TYR   B CA  1 
ATOM   27   C  C   . TYR   A 1 9   ? 0.613   5.275   4.968  1.00 18.33 ? 9   TYR   B C   1 
ATOM   28   O  O   . TYR   A 1 9   ? 0.872   4.525   4.030  1.00 22.35 ? 9   TYR   B O   1 
ATOM   29   C  CB  . TYR   A 1 9   ? -1.121  3.697   5.879  1.00 15.61 ? 9   TYR   B CB  1 
ATOM   30   C  CG  . TYR   A 1 9   ? -1.649  2.937   7.075  1.00 14.11 ? 9   TYR   B CG  1 
ATOM   31   C  CD1 . TYR   A 1 9   ? -1.103  1.718   7.438  1.00 14.74 ? 9   TYR   B CD1 1 
ATOM   32   C  CD2 . TYR   A 1 9   ? -2.736  3.444   7.790  1.00 15.32 ? 9   TYR   B CD2 1 
ATOM   33   C  CE1 . TYR   A 1 9   ? -1.566  1.038   8.560  1.00 13.74 ? 9   TYR   B CE1 1 
ATOM   34   C  CE2 . TYR   A 1 9   ? -3.252  2.751   8.890  1.00 15.81 ? 9   TYR   B CE2 1 
ATOM   35   C  CZ  . TYR   A 1 9   ? -2.663  1.548   9.255  1.00 16.40 ? 9   TYR   B CZ  1 
ATOM   36   O  OH  . TYR   A 1 9   ? -3.227  0.902   10.339 1.00 15.08 ? 9   TYR   B OH  1 
ATOM   37   N  N   . ARG   A 1 10  ? 0.846   6.588   4.977  1.00 21.08 ? 10  ARG   B N   1 
ATOM   38   C  CA  . ARG   A 1 10  ? 1.432   7.310   3.852  1.00 25.07 ? 10  ARG   B CA  1 
ATOM   39   C  C   . ARG   A 1 10  ? 2.961   7.227   3.938  1.00 28.29 ? 10  ARG   B C   1 
ATOM   40   O  O   . ARG   A 1 10  ? 3.536   6.656   4.864  1.00 26.43 ? 10  ARG   B O   1 
ATOM   41   C  CB  . ARG   A 1 10  ? 0.905   8.745   3.853  1.00 24.87 ? 10  ARG   B CB  1 
ATOM   42   C  CG  . ARG   A 1 10  ? -0.595  8.848   3.599  1.00 29.44 ? 10  ARG   B CG  1 
ATOM   43   C  CD  . ARG   A 1 10  ? -1.156  10.246  3.830  1.00 33.76 ? 10  ARG   B CD  1 
ATOM   44   N  NE  . ARG   A 1 10  ? -1.002  10.981  2.587  1.00 41.93 ? 10  ARG   B NE  1 
ATOM   45   C  CZ  . ARG   A 1 10  ? -1.358  12.254  2.385  1.00 40.96 ? 10  ARG   B CZ  1 
ATOM   46   N  NH1 . ARG   A 1 10  ? -1.889  12.979  3.355  1.00 36.97 ? 10  ARG   B NH1 1 
ATOM   47   N  NH2 . ARG   A 1 10  ? -1.179  12.793  1.189  1.00 46.25 ? 10  ARG   B NH2 1 
ATOM   48   N  N   . GLU   A 1 11  ? 3.650   7.773   2.934  1.00 28.97 ? 11  GLU   B N   1 
ATOM   49   C  CA  . GLU   A 1 11  ? 5.071   7.472   2.848  1.00 29.99 ? 11  GLU   B CA  1 
ATOM   50   C  C   . GLU   A 1 11  ? 5.810   7.987   4.081  1.00 29.01 ? 11  GLU   B C   1 
ATOM   51   O  O   . GLU   A 1 11  ? 6.576   7.253   4.684  1.00 29.87 ? 11  GLU   B O   1 
ATOM   52   C  CB  . GLU   A 1 11  ? 5.648   8.050   1.558  1.00 39.42 ? 11  GLU   B CB  1 
ATOM   53   C  CG  . GLU   A 1 11  ? 6.950   7.375   1.174  1.00 47.29 ? 11  GLU   B CG  1 
ATOM   54   C  CD  . GLU   A 1 11  ? 7.731   8.134   0.118  1.00 60.60 ? 11  GLU   B CD  1 
ATOM   55   O  OE1 . GLU   A 1 11  ? 7.468   9.359   -0.064 1.00 64.98 ? 11  GLU   B OE1 1 
ATOM   56   O  OE2 . GLU   A 1 11  ? 8.602   7.500   -0.520 1.00 62.68 ? 11  GLU   B OE2 1 
ATOM   57   N  N   . HIS   A 1 12  ? 5.524   9.224   4.507  1.00 30.30 ? 12  HIS   B N   1 
ATOM   58   C  CA  . HIS   A 1 12  ? 6.273   9.825   5.598  1.00 31.06 ? 12  HIS   B CA  1 
ATOM   59   C  C   . HIS   A 1 12  ? 5.736   9.494   6.985  1.00 31.75 ? 12  HIS   B C   1 
ATOM   60   O  O   . HIS   A 1 12  ? 6.422   9.791   7.954  1.00 31.00 ? 12  HIS   B O   1 
ATOM   61   C  CB  . HIS   A 1 12  ? 6.347   11.344  5.440  1.00 41.44 ? 12  HIS   B CB  1 
ATOM   62   C  CG  . HIS   A 1 12  ? 7.038   11.725  4.176  1.00 50.80 ? 12  HIS   B CG  1 
ATOM   63   N  ND1 . HIS   A 1 12  ? 8.264   11.183  3.828  1.00 50.66 ? 12  HIS   B ND1 1 
ATOM   64   C  CD2 . HIS   A 1 12  ? 6.673   12.557  3.179  1.00 53.21 ? 12  HIS   B CD2 1 
ATOM   65   C  CE1 . HIS   A 1 12  ? 8.631   11.670  2.660  1.00 64.49 ? 12  HIS   B CE1 1 
ATOM   66   N  NE2 . HIS   A 1 12  ? 7.669   12.531  2.245  1.00 63.52 ? 12  HIS   B NE2 1 
ATOM   67   N  N   . ASN   A 1 13  ? 4.544   8.875   7.118  1.00 25.02 ? 13  ASN   B N   1 
ATOM   68   C  CA  . ASN   A 1 13  ? 4.005   8.708   8.462  1.00 21.75 ? 13  ASN   B CA  1 
ATOM   69   C  C   . ASN   A 1 13  ? 3.622   7.253   8.695  1.00 22.46 ? 13  ASN   B C   1 
ATOM   70   O  O   . ASN   A 1 13  ? 2.995   6.913   9.739  1.00 21.41 ? 13  ASN   B O   1 
ATOM   71   C  CB  . ASN   A 1 13  ? 2.834   9.650   8.764  1.00 23.49 ? 13  ASN   B CB  1 
ATOM   72   C  CG  . ASN   A 1 13  ? 1.632   9.344   7.892  1.00 23.18 ? 13  ASN   B CG  1 
ATOM   73   O  OD1 . ASN   A 1 13  ? 1.668   8.441   7.060  1.00 22.77 ? 13  ASN   B OD1 1 
ATOM   74   N  ND2 . ASN   A 1 13  ? 0.591   10.151  8.010  1.00 25.01 ? 13  ASN   B ND2 1 
ATOM   75   N  N   . GLY   A 1 14  ? 4.067   6.424   7.735  1.00 19.83 ? 14  GLY   B N   1 
ATOM   76   C  CA  . GLY   A 1 14  ? 3.636   5.025   7.655  1.00 21.21 ? 14  GLY   B CA  1 
ATOM   77   C  C   . GLY   A 1 14  ? 4.359   4.088   8.621  1.00 21.80 ? 14  GLY   B C   1 
ATOM   78   O  O   . GLY   A 1 14  ? 5.275   4.484   9.372  1.00 21.50 ? 14  GLY   B O   1 
ATOM   79   N  N   . PRO   A 1 15  ? 3.950   2.784   8.646  1.00 18.84 ? 15  PRO   B N   1 
ATOM   80   C  CA  . PRO   A 1 15  ? 4.512   1.796   9.573  1.00 19.42 ? 15  PRO   B CA  1 
ATOM   81   C  C   . PRO   A 1 15  ? 6.022   1.751   9.789  1.00 20.10 ? 15  PRO   B C   1 
ATOM   82   O  O   . PRO   A 1 15  ? 6.474   1.535   10.911 1.00 21.22 ? 15  PRO   B O   1 
ATOM   83   C  CB  . PRO   A 1 15  ? 3.978   0.464   9.042  1.00 19.98 ? 15  PRO   B CB  1 
ATOM   84   C  CG  . PRO   A 1 15  ? 2.643   0.844   8.363  1.00 17.17 ? 15  PRO   B CG  1 
ATOM   85   C  CD  . PRO   A 1 15  ? 2.804   2.256   7.861  1.00 19.03 ? 15  PRO   B CD  1 
ATOM   86   N  N   . ILE   A 1 16  ? 6.779   1.964   8.708  1.00 25.06 ? 16  ILE   B N   1 
ATOM   87   C  CA  . ILE   A 1 16  ? 8.224   1.892   8.798  1.00 28.68 ? 16  ILE   B CA  1 
ATOM   88   C  C   . ILE   A 1 16  ? 8.783   3.022   9.666  1.00 25.28 ? 16  ILE   B C   1 
ATOM   89   O  O   . ILE   A 1 16  ? 9.940   2.917   10.064 1.00 29.52 ? 16  ILE   B O   1 
ATOM   90   C  CB  . ILE   A 1 16  ? 8.852   1.932   7.397  1.00 36.11 ? 16  ILE   B CB  1 
ATOM   91   C  CG1 . ILE   A 1 16  ? 10.216  1.241   7.397  1.00 44.43 ? 16  ILE   B CG1 1 
ATOM   92   C  CG2 . ILE   A 1 16  ? 8.950   3.365   6.897  1.00 34.43 ? 16  ILE   B CG2 1 
ATOM   93   C  CD1 . ILE   A 1 16  ? 10.104  -0.276  7.417  1.00 48.78 ? 16  ILE   B CD1 1 
ATOM   94   N  N   . HIS   A 1 17  ? 7.983   4.060   9.948  1.00 22.15 ? 17  HIS   B N   1 
ATOM   95   C  CA  . HIS   A 1 17  ? 8.390   5.258   10.672 1.00 25.37 ? 17  HIS   B CA  1 
ATOM   96   C  C   . HIS   A 1 17  ? 7.822   5.247   12.078 1.00 25.49 ? 17  HIS   B C   1 
ATOM   97   O  O   . HIS   A 1 17  ? 8.130   6.115   12.893 1.00 27.55 ? 17  HIS   B O   1 
ATOM   98   C  CB  . HIS   A 1 17  ? 7.923   6.557   9.990  1.00 26.52 ? 17  HIS   B CB  1 
ATOM   99   C  CG  . HIS   A 1 17  ? 8.585   6.780   8.669  1.00 31.89 ? 17  HIS   B CG  1 
ATOM   100  N  ND1 . HIS   A 1 17  ? 9.968   6.913   8.542  1.00 35.57 ? 17  HIS   B ND1 1 
ATOM   101  C  CD2 . HIS   A 1 17  ? 8.078   6.842   7.415  1.00 32.68 ? 17  HIS   B CD2 1 
ATOM   102  C  CE1 . HIS   A 1 17  ? 10.278  7.079   7.265  1.00 37.22 ? 17  HIS   B CE1 1 
ATOM   103  N  NE2 . HIS   A 1 17  ? 9.141   7.063   6.560  1.00 36.43 ? 17  HIS   B NE2 1 
ATOM   104  N  N   . TRP   A 1 18  ? 6.955   4.260   12.378 1.00 22.63 ? 18  TRP   B N   1 
ATOM   105  C  CA  . TRP   A 1 18  ? 6.341   4.279   13.689 1.00 21.76 ? 18  TRP   B CA  1 
ATOM   106  C  C   . TRP   A 1 18  ? 7.390   4.063   14.789 1.00 23.80 ? 18  TRP   B C   1 
ATOM   107  O  O   . TRP   A 1 18  ? 7.204   4.586   15.871 1.00 24.98 ? 18  TRP   B O   1 
ATOM   108  C  CB  . TRP   A 1 18  ? 5.174   3.270   13.800 1.00 18.93 ? 18  TRP   B CB  1 
ATOM   109  C  CG  . TRP   A 1 18  ? 3.999   3.534   12.895 1.00 18.07 ? 18  TRP   B CG  1 
ATOM   110  C  CD1 . TRP   A 1 18  ? 3.700   4.636   12.147 1.00 17.49 ? 18  TRP   B CD1 1 
ATOM   111  C  CD2 . TRP   A 1 18  ? 2.908   2.608   12.679 1.00 16.52 ? 18  TRP   B CD2 1 
ATOM   112  N  NE1 . TRP   A 1 18  ? 2.549   4.451   11.421 1.00 17.85 ? 18  TRP   B NE1 1 
ATOM   113  C  CE2 . TRP   A 1 18  ? 2.038   3.211   11.739 1.00 18.06 ? 18  TRP   B CE2 1 
ATOM   114  C  CE3 . TRP   A 1 18  ? 2.639   1.320   13.169 1.00 17.09 ? 18  TRP   B CE3 1 
ATOM   115  C  CZ2 . TRP   A 1 18  ? 0.865   2.590   11.293 1.00 19.02 ? 18  TRP   B CZ2 1 
ATOM   116  C  CZ3 . TRP   A 1 18  ? 1.488   0.685   12.695 1.00 15.62 ? 18  TRP   B CZ3 1 
ATOM   117  C  CH2 . TRP   A 1 18  ? 0.616   1.323   11.789 1.00 16.28 ? 18  TRP   B CH2 1 
ATOM   118  N  N   . LYS   A 1 19  ? 8.450   3.292   14.519 1.00 27.06 ? 19  LYS   B N   1 
ATOM   119  C  CA  . LYS   A 1 19  ? 9.479   3.024   15.520 1.00 30.41 ? 19  LYS   B CA  1 
ATOM   120  C  C   . LYS   A 1 19  ? 10.263  4.288   15.893 1.00 32.71 ? 19  LYS   B C   1 
ATOM   121  O  O   . LYS   A 1 19  ? 10.931  4.285   16.927 1.00 32.22 ? 19  LYS   B O   1 
ATOM   122  C  CB  . LYS   A 1 19  ? 10.439  1.907   15.088 1.00 33.20 ? 19  LYS   B CB  1 
ATOM   123  C  CG  . LYS   A 1 19  ? 11.498  2.304   14.070 1.00 38.16 ? 19  LYS   B CG  1 
ATOM   124  C  CD  . LYS   A 1 19  ? 12.486  1.186   13.761 1.00 43.65 ? 19  LYS   B CD  1 
ATOM   125  C  CE  . LYS   A 1 19  ? 12.044  0.274   12.630 1.00 51.67 ? 19  LYS   B CE  1 
ATOM   126  N  NZ  . LYS   A 1 19  ? 11.145  -0.817  13.096 1.00 55.72 ? 19  LYS   B NZ  1 
ATOM   127  N  N   . GLU   A 1 20  ? 10.145  5.351   15.084 1.00 34.03 ? 20  GLU   B N   1 
ATOM   128  C  CA  . GLU   A 1 20  ? 10.786  6.635   15.366 1.00 36.39 ? 20  GLU   B CA  1 
ATOM   129  C  C   . GLU   A 1 20  ? 10.016  7.375   16.467 1.00 32.69 ? 20  GLU   B C   1 
ATOM   130  O  O   . GLU   A 1 20  ? 10.575  8.268   17.111 1.00 33.47 ? 20  GLU   B O   1 
ATOM   131  C  CB  . GLU   A 1 20  ? 10.997  7.460   14.078 1.00 39.13 ? 20  GLU   B CB  1 
ATOM   132  C  CG  . GLU   A 1 20  ? 12.033  6.862   13.128 1.00 45.74 ? 20  GLU   B CG  1 
ATOM   133  C  CD  . GLU   A 1 20  ? 11.777  6.990   11.626 1.00 56.21 ? 20  GLU   B CD  1 
ATOM   134  O  OE1 . GLU   A 1 20  ? 11.081  7.962   11.198 1.00 48.67 ? 20  GLU   B OE1 1 
ATOM   135  O  OE2 . GLU   A 1 20  ? 12.268  6.106   10.870 1.00 58.00 ? 20  GLU   B OE2 1 
ATOM   136  N  N   . PHE   A 1 21  ? 8.755   6.982   16.734 1.00 30.73 ? 21  PHE   B N   1 
ATOM   137  C  CA  . PHE   A 1 21  ? 7.917   7.752   17.648 1.00 28.88 ? 21  PHE   B CA  1 
ATOM   138  C  C   . PHE   A 1 21  ? 7.307   6.937   18.786 1.00 29.49 ? 21  PHE   B C   1 
ATOM   139  O  O   . PHE   A 1 21  ? 6.854   7.517   19.782 1.00 30.09 ? 21  PHE   B O   1 
ATOM   140  C  CB  . PHE   A 1 21  ? 6.738   8.361   16.894 1.00 33.92 ? 21  PHE   B CB  1 
ATOM   141  C  CG  . PHE   A 1 21  ? 7.204   9.385   15.898 1.00 42.79 ? 21  PHE   B CG  1 
ATOM   142  C  CD1 . PHE   A 1 21  ? 7.381   10.706  16.289 1.00 40.66 ? 21  PHE   B CD1 1 
ATOM   143  C  CD2 . PHE   A 1 21  ? 7.510   9.010   14.590 1.00 40.71 ? 21  PHE   B CD2 1 
ATOM   144  C  CE1 . PHE   A 1 21  ? 7.827   11.651  15.375 1.00 44.92 ? 21  PHE   B CE1 1 
ATOM   145  C  CE2 . PHE   A 1 21  ? 7.975   9.953   13.684 1.00 50.91 ? 21  PHE   B CE2 1 
ATOM   146  C  CZ  . PHE   A 1 21  ? 8.128   11.271  14.082 1.00 49.22 ? 21  PHE   B CZ  1 
ATOM   147  N  N   . PHE   A 1 22  ? 7.151   5.616   18.588 1.00 27.82 ? 22  PHE   B N   1 
ATOM   148  C  CA  . PHE   A 1 22  ? 6.560   4.760   19.616 1.00 25.20 ? 22  PHE   B CA  1 
ATOM   149  C  C   . PHE   A 1 22  ? 7.588   3.716   20.015 1.00 24.71 ? 22  PHE   B C   1 
ATOM   150  O  O   . PHE   A 1 22  ? 7.935   2.827   19.230 1.00 24.91 ? 22  PHE   B O   1 
ATOM   151  C  CB  . PHE   A 1 22  ? 5.292   4.085   19.062 1.00 25.30 ? 22  PHE   B CB  1 
ATOM   152  C  CG  . PHE   A 1 22  ? 4.213   5.086   18.732 1.00 25.21 ? 22  PHE   B CG  1 
ATOM   153  C  CD1 . PHE   A 1 22  ? 3.287   5.476   19.693 1.00 28.59 ? 22  PHE   B CD1 1 
ATOM   154  C  CD2 . PHE   A 1 22  ? 4.126   5.651   17.461 1.00 25.62 ? 22  PHE   B CD2 1 
ATOM   155  C  CE1 . PHE   A 1 22  ? 2.307   6.410   19.399 1.00 29.09 ? 22  PHE   B CE1 1 
ATOM   156  C  CE2 . PHE   A 1 22  ? 3.154   6.607   17.177 1.00 28.92 ? 22  PHE   B CE2 1 
ATOM   157  C  CZ  . PHE   A 1 22  ? 2.258   6.995   18.150 1.00 28.79 ? 22  PHE   B CZ  1 
ATOM   158  N  N   . PRO   A 1 23  ? 8.202   3.851   21.203 1.00 23.34 ? 23  PRO   B N   1 
ATOM   159  C  CA  . PRO   A 1 23  ? 9.233   2.920   21.645 1.00 25.49 ? 23  PRO   B CA  1 
ATOM   160  C  C   . PRO   A 1 23  ? 8.819   1.456   21.499 1.00 26.77 ? 23  PRO   B C   1 
ATOM   161  O  O   . PRO   A 1 23  ? 9.623   0.636   21.072 1.00 24.55 ? 23  PRO   B O   1 
ATOM   162  C  CB  . PRO   A 1 23  ? 9.499   3.337   23.104 1.00 24.98 ? 23  PRO   B CB  1 
ATOM   163  C  CG  . PRO   A 1 23  ? 9.152   4.829   23.112 1.00 25.92 ? 23  PRO   B CG  1 
ATOM   164  C  CD  . PRO   A 1 23  ? 8.020   5.005   22.121 1.00 25.79 ? 23  PRO   B CD  1 
ATOM   165  N  N   . ILE   A 1 24  ? 7.535   1.151   21.758 1.00 22.98 ? 24  ILE   B N   1 
ATOM   166  C  CA  . ILE   A 1 24  ? 7.126   -0.250  21.805 1.00 23.22 ? 24  ILE   B CA  1 
ATOM   167  C  C   . ILE   A 1 24  ? 7.056   -0.858  20.395 1.00 21.37 ? 24  ILE   B C   1 
ATOM   168  O  O   . ILE   A 1 24  ? 6.929   -2.069  20.275 1.00 20.96 ? 24  ILE   B O   1 
ATOM   169  C  CB  . ILE   A 1 24  ? 5.772   -0.422  22.552 1.00 21.45 ? 24  ILE   B CB  1 
ATOM   170  C  CG1 . ILE   A 1 24  ? 5.587   -1.836  23.078 1.00 24.96 ? 24  ILE   B CG1 1 
ATOM   171  C  CG2 . ILE   A 1 24  ? 4.574   -0.021  21.713 1.00 26.05 ? 24  ILE   B CG2 1 
ATOM   172  C  CD1 . ILE   A 1 24  ? 6.530   -2.203  24.239 1.00 35.81 ? 24  ILE   B CD1 1 
ATOM   173  N  N   . ALA   A 1 25  ? 7.080   -0.039  19.344 1.00 19.35 ? 25  ALA   B N   1 
ATOM   174  C  CA  . ALA   A 1 25  ? 7.040   -0.567  17.979 1.00 23.39 ? 25  ALA   B CA  1 
ATOM   175  C  C   . ALA   A 1 25  ? 8.109   -1.620  17.697 1.00 25.58 ? 25  ALA   B C   1 
ATOM   176  O  O   . ALA   A 1 25  ? 7.882   -2.465  16.806 1.00 24.81 ? 25  ALA   B O   1 
ATOM   177  C  CB  . ALA   A 1 25  ? 7.108   0.530   16.940 1.00 22.33 ? 25  ALA   B CB  1 
ATOM   178  N  N   . ASP   A 1 26  ? 9.257   -1.546  18.410 1.00 26.10 ? 26  ASP   B N   1 
ATOM   179  C  CA  . ASP   A 1 26  ? 10.376  -2.472  18.255 1.00 30.26 ? 26  ASP   B CA  1 
ATOM   180  C  C   . ASP   A 1 26  ? 10.384  -3.560  19.333 1.00 30.00 ? 26  ASP   B C   1 
ATOM   181  O  O   . ASP   A 1 26  ? 11.373  -4.275  19.482 1.00 28.46 ? 26  ASP   B O   1 
ATOM   182  C  CB  . ASP   A 1 26  ? 11.717  -1.729  18.331 1.00 37.47 ? 26  ASP   B CB  1 
ATOM   183  C  CG  . ASP   A 1 26  ? 12.236  -1.323  16.962 1.00 48.17 ? 26  ASP   B CG  1 
ATOM   184  O  OD1 . ASP   A 1 26  ? 11.507  -1.563  15.961 1.00 48.03 ? 26  ASP   B OD1 1 
ATOM   185  O  OD2 . ASP   A 1 26  ? 13.378  -0.782  16.896 1.00 57.40 ? 26  ASP   B OD2 1 
ATOM   186  N  N   . GLY   A 1 27  ? 9.278   -3.670  20.092 1.00 27.53 ? 27  GLY   B N   1 
ATOM   187  C  CA  . GLY   A 1 27  ? 9.205   -4.515  21.276 1.00 21.47 ? 27  GLY   B CA  1 
ATOM   188  C  C   . GLY   A 1 27  ? 9.196   -6.000  20.900 1.00 22.83 ? 27  GLY   B C   1 
ATOM   189  O  O   . GLY   A 1 27  ? 9.307   -6.364  19.746 1.00 25.18 ? 27  GLY   B O   1 
ATOM   190  N  N   . ASP   A 1 28  ? 9.065   -6.857  21.907 1.00 23.76 ? 28  ASP   B N   1 
ATOM   191  C  CA  . ASP   A 1 28  ? 9.267   -8.271  21.695 1.00 24.24 ? 28  ASP   B CA  1 
ATOM   192  C  C   . ASP   A 1 28  ? 7.945   -9.010  21.473 1.00 21.46 ? 28  ASP   B C   1 
ATOM   193  O  O   . ASP   A 1 28  ? 7.981   -10.224 21.233 1.00 23.89 ? 28  ASP   B O   1 
ATOM   194  C  CB  . ASP   A 1 28  ? 10.023  -8.897  22.869 1.00 33.23 ? 28  ASP   B CB  1 
ATOM   195  C  CG  . ASP   A 1 28  ? 11.454  -8.378  23.018 1.00 43.41 ? 28  ASP   B CG  1 
ATOM   196  O  OD1 . ASP   A 1 28  ? 12.137  -8.147  21.973 1.00 44.27 ? 28  ASP   B OD1 1 
ATOM   197  O  OD2 . ASP   A 1 28  ? 11.868  -8.186  24.175 1.00 48.60 ? 28  ASP   B OD2 1 
ATOM   198  N  N   . GLN   A 1 29  ? 6.807   -8.314  21.602 1.00 17.94 ? 29  GLN   B N   1 
ATOM   199  C  CA  . GLN   A 1 29  ? 5.519   -9.011  21.389 1.00 17.45 ? 29  GLN   B CA  1 
ATOM   200  C  C   . GLN   A 1 29  ? 4.662   -8.263  20.362 1.00 16.16 ? 29  GLN   B C   1 
ATOM   201  O  O   . GLN   A 1 29  ? 3.488   -7.996  20.617 1.00 15.94 ? 29  GLN   B O   1 
ATOM   202  C  CB  . GLN   A 1 29  ? 4.724   -9.185  22.691 1.00 21.02 ? 29  GLN   B CB  1 
ATOM   203  C  CG  . GLN   A 1 29  ? 5.546   -9.964  23.716 1.00 25.70 ? 29  GLN   B CG  1 
ATOM   204  C  CD  . GLN   A 1 29  ? 4.717   -10.912 24.538 1.00 32.99 ? 29  GLN   B CD  1 
ATOM   205  O  OE1 . GLN   A 1 29  ? 3.643   -10.543 25.021 1.00 28.33 ? 29  GLN   B OE1 1 
ATOM   206  N  NE2 . GLN   A 1 29  ? 5.227   -12.134 24.704 1.00 32.34 ? 29  GLN   B NE2 1 
ATOM   207  N  N   . GLN   A 1 30  ? 5.260   -7.892  19.222 1.00 15.04 ? 30  GLN   B N   1 
ATOM   208  C  CA  . GLN   A 1 30  ? 4.504   -7.051  18.289 1.00 13.74 ? 30  GLN   B CA  1 
ATOM   209  C  C   . GLN   A 1 30  ? 3.727   -7.873  17.239 1.00 13.11 ? 30  GLN   B C   1 
ATOM   210  O  O   . GLN   A 1 30  ? 4.038   -9.008  16.930 1.00 13.90 ? 30  GLN   B O   1 
ATOM   211  C  CB  . GLN   A 1 30  ? 5.484   -6.099  17.573 1.00 14.40 ? 30  GLN   B CB  1 
ATOM   212  C  CG  . GLN   A 1 30  ? 5.971   -4.980  18.485 1.00 15.44 ? 30  GLN   B CG  1 
ATOM   213  C  CD  . GLN   A 1 30  ? 4.885   -3.963  18.792 1.00 16.78 ? 30  GLN   B CD  1 
ATOM   214  O  OE1 . GLN   A 1 30  ? 4.413   -3.237  17.908 1.00 17.12 ? 30  GLN   B OE1 1 
ATOM   215  N  NE2 . GLN   A 1 30  ? 4.450   -3.873  20.051 1.00 16.23 ? 30  GLN   B NE2 1 
ATOM   216  N  N   . SER   A 1 31  ? 2.661   -7.258  16.691 1.00 12.17 ? 31  SER   B N   1 
ATOM   217  C  CA  . SER   A 1 31  ? 1.766   -7.924  15.752 1.00 11.50 ? 31  SER   B CA  1 
ATOM   218  C  C   . SER   A 1 31  ? 1.629   -7.063  14.512 1.00 11.92 ? 31  SER   B C   1 
ATOM   219  O  O   . SER   A 1 31  ? 1.826   -5.851  14.583 1.00 12.42 ? 31  SER   B O   1 
ATOM   220  C  CB  . SER   A 1 31  ? 0.377   -8.108  16.352 1.00 10.59 ? 31  SER   B CB  1 
ATOM   221  O  OG  . SER   A 1 31  ? 0.420   -9.039  17.417 1.00 13.40 ? 31  SER   B OG  1 
ATOM   222  N  N   . PRO   A 1 32  ? 1.255   -7.610  13.330 1.00 12.61 ? 32  PRO   B N   1 
ATOM   223  C  CA  . PRO   A 1 32  ? 0.915   -9.012  13.114 1.00 12.22 ? 32  PRO   B CA  1 
ATOM   224  C  C   . PRO   A 1 32  ? 2.160   -9.850  12.817 1.00 13.24 ? 32  PRO   B C   1 
ATOM   225  O  O   . PRO   A 1 32  ? 3.276   -9.344  12.882 1.00 14.06 ? 32  PRO   B O   1 
ATOM   226  C  CB  . PRO   A 1 32  ? 0.118   -8.930  11.801 1.00 12.64 ? 32  PRO   B CB  1 
ATOM   227  C  CG  . PRO   A 1 32  ? 0.837   -7.819  11.014 1.00 12.04 ? 32  PRO   B CG  1 
ATOM   228  C  CD  . PRO   A 1 32  ? 1.186   -6.793  12.091 1.00 13.77 ? 32  PRO   B CD  1 
ATOM   229  N  N   . ILE   A 1 33  ? 1.962   -11.146 12.561 1.00 13.64 ? 33  ILE   B N   1 
ATOM   230  C  CA  . ILE   A 1 33  ? 3.093   -12.042 12.297 1.00 14.23 ? 33  ILE   B CA  1 
ATOM   231  C  C   . ILE   A 1 33  ? 2.789   -12.927 11.092 1.00 16.17 ? 33  ILE   B C   1 
ATOM   232  O  O   . ILE   A 1 33  ? 1.652   -13.019 10.665 1.00 13.83 ? 33  ILE   B O   1 
ATOM   233  C  CB  . ILE   A 1 33  ? 3.357   -12.936 13.526 1.00 15.28 ? 33  ILE   B CB  1 
ATOM   234  C  CG1 . ILE   A 1 33  ? 2.175   -13.879 13.780 1.00 17.13 ? 33  ILE   B CG1 1 
ATOM   235  C  CG2 . ILE   A 1 33  ? 3.711   -12.084 14.751 1.00 16.12 ? 33  ILE   B CG2 1 
ATOM   236  C  CD1 . ILE   A 1 33  ? 2.471   -14.994 14.799 1.00 16.52 ? 33  ILE   B CD1 1 
ATOM   237  N  N   . GLU   A 1 34  ? 3.827   -13.618 10.594 1.00 14.76 ? 34  GLU   B N   1 
ATOM   238  C  CA  . GLU   A 1 34  ? 3.653   -14.735 9.673  1.00 16.90 ? 34  GLU   B CA  1 
ATOM   239  C  C   . GLU   A 1 34  ? 3.296   -16.001 10.448 1.00 16.50 ? 34  GLU   B C   1 
ATOM   240  O  O   . GLU   A 1 34  ? 3.899   -16.298 11.493 1.00 17.01 ? 34  GLU   B O   1 
ATOM   241  C  CB  . GLU   A 1 34  ? 5.012   -15.041 9.017  1.00 20.21 ? 34  GLU   B CB  1 
ATOM   242  C  CG  . GLU   A 1 34  ? 5.639   -13.843 8.330  1.00 27.22 ? 34  GLU   B CG  1 
ATOM   243  C  CD  . GLU   A 1 34  ? 5.247   -13.692 6.868  1.00 31.78 ? 34  GLU   B CD  1 
ATOM   244  O  OE1 . GLU   A 1 34  ? 4.686   -14.674 6.266  1.00 27.54 ? 34  GLU   B OE1 1 
ATOM   245  O  OE2 . GLU   A 1 34  ? 5.526   -12.589 6.313  1.00 39.55 ? 34  GLU   B OE2 1 
ATOM   246  N  N   . ILE   A 1 35  ? 2.251   -16.681 9.971  1.00 14.61 ? 35  ILE   B N   1 
ATOM   247  C  CA  . ILE   A 1 35  ? 1.852   -17.948 10.566 1.00 16.38 ? 35  ILE   B CA  1 
ATOM   248  C  C   . ILE   A 1 35  ? 2.304   -19.049 9.616  1.00 18.14 ? 35  ILE   B C   1 
ATOM   249  O  O   . ILE   A 1 35  ? 1.864   -19.078 8.462  1.00 18.50 ? 35  ILE   B O   1 
ATOM   250  C  CB  . ILE   A 1 35  ? 0.335   -17.952 10.815 1.00 17.68 ? 35  ILE   B CB  1 
ATOM   251  C  CG1 . ILE   A 1 35  ? -0.084  -16.872 11.825 1.00 17.21 ? 35  ILE   B CG1 1 
ATOM   252  C  CG2 . ILE   A 1 35  ? -0.137  -19.351 11.253 1.00 18.38 ? 35  ILE   B CG2 1 
ATOM   253  C  CD1 . ILE   A 1 35  ? -1.614  -16.673 11.818 1.00 19.99 ? 35  ILE   B CD1 1 
ATOM   254  N  N   . LYS   A 1 36  ? 3.252   -19.892 10.092 1.00 17.92 ? 36  LYS   B N   1 
ATOM   255  C  CA  . LYS   A 1 36  ? 3.717   -21.045 9.332  1.00 19.96 ? 36  LYS   B CA  1 
ATOM   256  C  C   . LYS   A 1 36  ? 3.015   -22.274 9.906  1.00 19.90 ? 36  LYS   B C   1 
ATOM   257  O  O   . LYS   A 1 36  ? 3.323   -22.678 11.027 1.00 21.99 ? 36  LYS   B O   1 
ATOM   258  C  CB  . LYS   A 1 36  ? 5.231   -21.162 9.471  1.00 21.85 ? 36  LYS   B CB  1 
ATOM   259  C  CG  . LYS   A 1 36  ? 6.036   -20.045 8.834  1.00 27.38 ? 36  LYS   B CG  1 
ATOM   260  C  CD  . LYS   A 1 36  ? 7.545   -20.282 9.072  1.00 27.95 ? 36  LYS   B CD  1 
ATOM   261  C  CE  . LYS   A 1 36  ? 8.448   -19.356 8.300  1.00 29.34 ? 36  LYS   B CE  1 
ATOM   262  N  NZ  . LYS   A 1 36  ? 9.848   -19.490 8.768  1.00 26.92 ? 36  LYS   B NZ  1 
ATOM   263  N  N   . THR   A 1 37  ? 2.067   -22.815 9.131  1.00 20.33 ? 37  THR   B N   1 
ATOM   264  C  CA  . THR   A 1 37  ? 1.070   -23.737 9.645  1.00 22.07 ? 37  THR   B CA  1 
ATOM   265  C  C   . THR   A 1 37  ? 1.692   -25.064 10.056 1.00 24.86 ? 37  THR   B C   1 
ATOM   266  O  O   . THR   A 1 37  ? 1.153   -25.739 10.934 1.00 30.27 ? 37  THR   B O   1 
ATOM   267  C  CB  . THR   A 1 37  ? -0.091  -23.970 8.675  1.00 23.49 ? 37  THR   B CB  1 
ATOM   268  O  OG1 . THR   A 1 37  ? 0.356   -24.567 7.457  1.00 25.01 ? 37  THR   B OG1 1 
ATOM   269  C  CG2 . THR   A 1 37  ? -0.860  -22.709 8.353  1.00 24.25 ? 37  THR   B CG2 1 
ATOM   270  N  N   . LYS   A 1 38  ? 2.835   -25.417 9.452  1.00 24.08 ? 38  LYS   B N   1 
ATOM   271  C  CA  . LYS   A 1 38  ? 3.427   -26.686 9.832  1.00 27.21 ? 38  LYS   B CA  1 
ATOM   272  C  C   . LYS   A 1 38  ? 4.319   -26.518 11.065 1.00 26.39 ? 38  LYS   B C   1 
ATOM   273  O  O   . LYS   A 1 38  ? 4.730   -27.528 11.635 1.00 31.13 ? 38  LYS   B O   1 
ATOM   274  C  CB  . LYS   A 1 38  ? 4.114   -27.339 8.628  1.00 30.58 ? 38  LYS   B CB  1 
ATOM   275  C  CG  . LYS   A 1 38  ? 3.126   -27.977 7.662  1.00 38.65 ? 38  LYS   B CG  1 
ATOM   276  C  CD  . LYS   A 1 38  ? 3.766   -28.736 6.527  1.00 46.83 ? 38  LYS   B CD  1 
ATOM   277  C  CE  . LYS   A 1 38  ? 2.875   -28.775 5.303  1.00 53.95 ? 38  LYS   B CE  1 
ATOM   278  N  NZ  . LYS   A 1 38  ? 3.238   -29.917 4.428  1.00 56.63 ? 38  LYS   B NZ  1 
ATOM   279  N  N   . GLU   A 1 39  ? 4.565   -25.266 11.513 1.00 25.56 ? 39  GLU   B N   1 
ATOM   280  C  CA  . GLU   A 1 39  ? 5.458   -24.992 12.627 1.00 23.36 ? 39  GLU   B CA  1 
ATOM   281  C  C   . GLU   A 1 39  ? 4.697   -24.667 13.919 1.00 24.82 ? 39  GLU   B C   1 
ATOM   282  O  O   . GLU   A 1 39  ? 5.291   -24.600 14.990 1.00 28.17 ? 39  GLU   B O   1 
ATOM   283  C  CB  . GLU   A 1 39  ? 6.451   -23.894 12.261 1.00 26.39 ? 39  GLU   B CB  1 
ATOM   284  C  CG  . GLU   A 1 39  ? 7.079   -24.135 10.874 1.00 32.96 ? 39  GLU   B CG  1 
ATOM   285  C  CD  . GLU   A 1 39  ? 7.728   -25.492 10.555 1.00 43.69 ? 39  GLU   B CD  1 
ATOM   286  O  OE1 . GLU   A 1 39  ? 8.440   -26.029 11.452 1.00 46.52 ? 39  GLU   B OE1 1 
ATOM   287  O  OE2 . GLU   A 1 39  ? 7.555   -26.020 9.376  1.00 39.35 ? 39  GLU   B OE2 1 
ATOM   288  N  N   A VAL   A 1 40  ? 3.375   -24.520 13.793 0.50 23.56 ? 40  VAL   B N   1 
ATOM   289  N  N   B VAL   A 1 40  ? 3.389   -24.453 13.805 0.50 23.16 ? 40  VAL   B N   1 
ATOM   290  C  CA  A VAL   A 1 40  ? 2.493   -24.198 14.907 0.50 25.13 ? 40  VAL   B CA  1 
ATOM   291  C  CA  B VAL   A 1 40  ? 2.607   -24.142 14.990 0.50 24.47 ? 40  VAL   B CA  1 
ATOM   292  C  C   A VAL   A 1 40  ? 2.243   -25.449 15.743 0.50 27.90 ? 40  VAL   B C   1 
ATOM   293  C  C   B VAL   A 1 40  ? 2.397   -25.426 15.780 0.50 27.42 ? 40  VAL   B C   1 
ATOM   294  O  O   A VAL   A 1 40  ? 2.193   -26.543 15.206 0.50 31.66 ? 40  VAL   B O   1 
ATOM   295  O  O   B VAL   A 1 40  ? 2.542   -26.515 15.251 0.50 30.52 ? 40  VAL   B O   1 
ATOM   296  C  CB  A VAL   A 1 40  ? 1.183   -23.601 14.364 0.50 24.41 ? 40  VAL   B CB  1 
ATOM   297  C  CB  B VAL   A 1 40  ? 1.277   -23.484 14.599 0.50 23.48 ? 40  VAL   B CB  1 
ATOM   298  C  CG1 A VAL   A 1 40  ? 0.103   -23.539 15.430 0.50 23.65 ? 40  VAL   B CG1 1 
ATOM   299  C  CG1 B VAL   A 1 40  ? 1.536   -22.249 13.748 0.50 24.26 ? 40  VAL   B CG1 1 
ATOM   300  C  CG2 A VAL   A 1 40  ? 1.435   -22.224 13.769 0.50 25.47 ? 40  VAL   B CG2 1 
ATOM   301  C  CG2 B VAL   A 1 40  ? 0.387   -24.471 13.866 0.50 21.97 ? 40  VAL   B CG2 1 
ATOM   302  N  N   . LYS   A 1 41  ? 2.063   -25.271 17.057 1.00 28.99 ? 41  LYS   B N   1 
ATOM   303  C  CA  . LYS   A 1 41  ? 1.966   -26.405 17.962 1.00 29.89 ? 41  LYS   B CA  1 
ATOM   304  C  C   . LYS   A 1 41  ? 0.489   -26.640 18.314 1.00 24.58 ? 41  LYS   B C   1 
ATOM   305  O  O   . LYS   A 1 41  ? -0.076  -25.773 18.954 1.00 24.69 ? 41  LYS   B O   1 
ATOM   306  C  CB  . LYS   A 1 41  ? 2.847   -26.030 19.163 1.00 32.80 ? 41  LYS   B CB  1 
ATOM   307  C  CG  . LYS   A 1 41  ? 4.359   -25.957 18.903 1.00 36.99 ? 41  LYS   B CG  1 
ATOM   308  N  N   . TYR   A 1 42  ? -0.110  -27.788 17.951 1.00 26.47 ? 42  TYR   B N   1 
ATOM   309  C  CA  . TYR   A 1 42  ? -1.435  -28.153 18.477 1.00 26.40 ? 42  TYR   B CA  1 
ATOM   310  C  C   . TYR   A 1 42  ? -1.386  -28.261 20.009 1.00 29.40 ? 42  TYR   B C   1 
ATOM   311  O  O   . TYR   A 1 42  ? -0.466  -28.889 20.532 1.00 26.76 ? 42  TYR   B O   1 
ATOM   312  C  CB  . TYR   A 1 42  ? -1.956  -29.461 17.867 1.00 32.86 ? 42  TYR   B CB  1 
ATOM   313  C  CG  . TYR   A 1 42  ? -3.162  -30.011 18.588 1.00 28.77 ? 42  TYR   B CG  1 
ATOM   314  C  CD1 . TYR   A 1 42  ? -4.417  -29.397 18.506 1.00 32.58 ? 42  TYR   B CD1 1 
ATOM   315  C  CD2 . TYR   A 1 42  ? -3.059  -31.142 19.396 1.00 33.38 ? 42  TYR   B CD2 1 
ATOM   316  C  CE1 . TYR   A 1 42  ? -5.517  -29.884 19.197 1.00 31.85 ? 42  TYR   B CE1 1 
ATOM   317  C  CE2 . TYR   A 1 42  ? -4.145  -31.628 20.107 1.00 36.86 ? 42  TYR   B CE2 1 
ATOM   318  C  CZ  . TYR   A 1 42  ? -5.379  -31.012 20.000 1.00 36.01 ? 42  TYR   B CZ  1 
ATOM   319  O  OH  . TYR   A 1 42  ? -6.433  -31.529 20.705 1.00 35.75 ? 42  TYR   B OH  1 
ATOM   320  N  N   . ASP   A 1 43  ? -2.343  -27.636 20.745 1.00 21.33 ? 43  ASP   B N   1 
ATOM   321  C  CA  . ASP   A 1 43  ? -2.333  -27.591 22.197 1.00 21.40 ? 43  ASP   B CA  1 
ATOM   322  C  C   . ASP   A 1 43  ? -3.679  -28.105 22.711 1.00 28.18 ? 43  ASP   B C   1 
ATOM   323  O  O   . ASP   A 1 43  ? -4.701  -27.440 22.561 1.00 24.05 ? 43  ASP   B O   1 
ATOM   324  C  CB  . ASP   A 1 43  ? -2.024  -26.186 22.753 1.00 25.38 ? 43  ASP   B CB  1 
ATOM   325  C  CG  . ASP   A 1 43  ? -1.831  -26.088 24.261 1.00 26.43 ? 43  ASP   B CG  1 
ATOM   326  O  OD1 . ASP   A 1 43  ? -2.115  -27.089 24.971 1.00 30.19 ? 43  ASP   B OD1 1 
ATOM   327  O  OD2 . ASP   A 1 43  ? -1.336  -25.003 24.753 1.00 31.22 ? 43  ASP   B OD2 1 
ATOM   328  N  N   . SER   A 1 44  ? -3.701  -29.291 23.338 1.00 27.73 ? 44  SER   B N   1 
ATOM   329  C  CA  . SER   A 1 44  ? -4.985  -29.833 23.812 1.00 25.14 ? 44  SER   B CA  1 
ATOM   330  C  C   . SER   A 1 44  ? -5.531  -29.054 25.012 1.00 28.14 ? 44  SER   B C   1 
ATOM   331  O  O   . SER   A 1 44  ? -6.676  -29.274 25.426 1.00 32.52 ? 44  SER   B O   1 
ATOM   332  C  CB  . SER   A 1 44  ? -4.857  -31.323 24.140 1.00 27.24 ? 44  SER   B CB  1 
ATOM   333  O  OG  . SER   A 1 44  ? -3.842  -31.463 25.127 1.00 29.31 ? 44  SER   B OG  1 
ATOM   334  N  N   . SER   A 1 45  ? -4.724  -28.171 25.616 1.00 26.64 ? 45  SER   B N   1 
ATOM   335  C  CA  . SER   A 1 45  ? -5.186  -27.399 26.754 1.00 25.35 ? 45  SER   B CA  1 
ATOM   336  C  C   . SER   A 1 45  ? -6.034  -26.196 26.297 1.00 25.17 ? 45  SER   B C   1 
ATOM   337  O  O   . SER   A 1 45  ? -6.701  -25.544 27.114 1.00 25.19 ? 45  SER   B O   1 
ATOM   338  C  CB  . SER   A 1 45  ? -4.062  -27.033 27.677 1.00 31.24 ? 45  SER   B CB  1 
ATOM   339  O  OG  . SER   A 1 45  ? -3.381  -25.858 27.248 1.00 31.75 ? 45  SER   B OG  1 
ATOM   340  N  N   . LEU   A 1 46  ? -6.017  -25.920 24.992 1.00 19.64 ? 46  LEU   B N   1 
ATOM   341  C  CA  . LEU   A 1 46  ? -6.880  -24.860 24.471 1.00 16.71 ? 46  LEU   B CA  1 
ATOM   342  C  C   . LEU   A 1 46  ? -8.335  -25.317 24.525 1.00 18.43 ? 46  LEU   B C   1 
ATOM   343  O  O   . LEU   A 1 46  ? -8.610  -26.514 24.516 1.00 21.94 ? 46  LEU   B O   1 
ATOM   344  C  CB  . LEU   A 1 46  ? -6.474  -24.503 23.044 1.00 14.71 ? 46  LEU   B CB  1 
ATOM   345  C  CG  . LEU   A 1 46  ? -5.174  -23.721 22.947 1.00 15.07 ? 46  LEU   B CG  1 
ATOM   346  C  CD1 . LEU   A 1 46  ? -4.728  -23.673 21.477 1.00 15.94 ? 46  LEU   B CD1 1 
ATOM   347  C  CD2 . LEU   A 1 46  ? -5.315  -22.311 23.534 1.00 15.57 ? 46  LEU   B CD2 1 
ATOM   348  N  N   . ARG   A 1 47  ? -9.245  -24.351 24.622 1.00 15.60 ? 47  ARG   B N   1 
ATOM   349  C  CA  . ARG   A 1 47  ? -10.656 -24.738 24.677 1.00 16.69 ? 47  ARG   B CA  1 
ATOM   350  C  C   . ARG   A 1 47  ? -11.330 -24.205 23.419 1.00 16.11 ? 47  ARG   B C   1 
ATOM   351  O  O   . ARG   A 1 47  ? -10.862 -23.279 22.726 1.00 15.45 ? 47  ARG   B O   1 
ATOM   352  C  CB  . ARG   A 1 47  ? -11.325 -23.964 25.814 1.00 21.28 ? 47  ARG   B CB  1 
ATOM   353  C  CG  . ARG   A 1 47  ? -11.273 -24.514 27.235 1.00 30.03 ? 47  ARG   B CG  1 
ATOM   354  C  CD  . ARG   A 1 47  ? -10.946 -25.979 27.234 1.00 41.65 ? 47  ARG   B CD  1 
ATOM   355  N  NE  . ARG   A 1 47  ? -10.507 -26.572 28.476 1.00 56.65 ? 47  ARG   B NE  1 
ATOM   356  C  CZ  . ARG   A 1 47  ? -9.658  -27.584 28.536 1.00 48.08 ? 47  ARG   B CZ  1 
ATOM   357  N  NH1 . ARG   A 1 47  ? -9.303  -28.073 29.700 1.00 49.76 ? 47  ARG   B NH1 1 
ATOM   358  N  NH2 . ARG   A 1 47  ? -9.142  -28.085 27.438 1.00 53.19 ? 47  ARG   B NH2 1 
ATOM   359  N  N   . PRO   A 1 48  ? -12.520 -24.746 23.065 1.00 14.43 ? 48  PRO   B N   1 
ATOM   360  C  CA  . PRO   A 1 48  ? -13.265 -24.167 21.941 1.00 15.75 ? 48  PRO   B CA  1 
ATOM   361  C  C   . PRO   A 1 48  ? -13.718 -22.721 22.163 1.00 11.88 ? 48  PRO   B C   1 
ATOM   362  O  O   . PRO   A 1 48  ? -13.956 -22.279 23.302 1.00 13.02 ? 48  PRO   B O   1 
ATOM   363  C  CB  . PRO   A 1 48  ? -14.537 -25.043 21.862 1.00 17.41 ? 48  PRO   B CB  1 
ATOM   364  C  CG  . PRO   A 1 48  ? -14.258 -26.247 22.739 1.00 18.67 ? 48  PRO   B CG  1 
ATOM   365  C  CD  . PRO   A 1 48  ? -13.108 -25.945 23.686 1.00 17.01 ? 48  PRO   B CD  1 
ATOM   366  N  N   . LEU   A 1 49  ? -13.828 -21.933 21.076 1.00 13.97 ? 49  LEU   B N   1 
ATOM   367  C  CA  . LEU   A 1 49  ? -14.326 -20.572 21.259 1.00 13.59 ? 49  LEU   B CA  1 
ATOM   368  C  C   . LEU   A 1 49  ? -15.822 -20.670 21.543 1.00 14.50 ? 49  LEU   B C   1 
ATOM   369  O  O   . LEU   A 1 49  ? -16.503 -21.505 20.966 1.00 15.75 ? 49  LEU   B O   1 
ATOM   370  C  CB  . LEU   A 1 49  ? -14.141 -19.775 19.958 1.00 14.23 ? 49  LEU   B CB  1 
ATOM   371  C  CG  . LEU   A 1 49  ? -12.686 -19.495 19.593 1.00 13.94 ? 49  LEU   B CG  1 
ATOM   372  C  CD1 . LEU   A 1 49  ? -12.663 -18.816 18.231 1.00 14.83 ? 49  LEU   B CD1 1 
ATOM   373  C  CD2 . LEU   A 1 49  ? -12.090 -18.568 20.635 1.00 16.76 ? 49  LEU   B CD2 1 
ATOM   374  N  N   . SER   A 1 50  ? -16.329 -19.761 22.371 1.00 13.08 ? 50  SER   B N   1 
ATOM   375  C  CA  . SER   A 1 50  ? -17.748 -19.676 22.705 1.00 15.09 ? 50  SER   B CA  1 
ATOM   376  C  C   . SER   A 1 50  ? -18.155 -18.205 22.552 1.00 15.01 ? 50  SER   B C   1 
ATOM   377  O  O   . SER   A 1 50  ? -17.695 -17.344 23.312 1.00 16.91 ? 50  SER   B O   1 
ATOM   378  C  CB  . SER   A 1 50  ? -17.975 -20.200 24.098 1.00 15.19 ? 50  SER   B CB  1 
ATOM   379  O  OG  . SER   A 1 50  ? -19.326 -20.041 24.559 1.00 17.22 ? 50  SER   B OG  1 
ATOM   380  N  N   . ILE   A 1 51  ? -18.968 -17.953 21.512 1.00 15.03 ? 51  ILE   B N   1 
ATOM   381  C  CA  . ILE   A 1 51  ? -19.235 -16.557 21.098 1.00 16.60 ? 51  ILE   B CA  1 
ATOM   382  C  C   . ILE   A 1 51  ? -20.716 -16.236 21.278 1.00 18.82 ? 51  ILE   B C   1 
ATOM   383  O  O   . ILE   A 1 51  ? -21.545 -16.997 20.805 1.00 20.12 ? 51  ILE   B O   1 
ATOM   384  C  CB  . ILE   A 1 51  ? -18.814 -16.417 19.631 1.00 20.49 ? 51  ILE   B CB  1 
ATOM   385  C  CG1 . ILE   A 1 51  ? -17.342 -16.798 19.453 1.00 23.53 ? 51  ILE   B CG1 1 
ATOM   386  C  CG2 . ILE   A 1 51  ? -19.078 -15.006 19.119 1.00 24.19 ? 51  ILE   B CG2 1 
ATOM   387  C  CD1 . ILE   A 1 51  ? -16.744 -16.521 18.064 1.00 28.12 ? 51  ILE   B CD1 1 
ATOM   388  N  N   . LYS   A 1 52  ? -21.048 -15.054 21.833 1.00 17.41 ? 52  LYS   B N   1 
ATOM   389  C  CA  . LYS   A 1 52  ? -22.433 -14.603 21.875 1.00 18.50 ? 52  LYS   B CA  1 
ATOM   390  C  C   . LYS   A 1 52  ? -22.431 -13.135 21.503 1.00 17.49 ? 52  LYS   B C   1 
ATOM   391  O  O   . LYS   A 1 52  ? -21.910 -12.353 22.276 1.00 18.90 ? 52  LYS   B O   1 
ATOM   392  C  CB  . LYS   A 1 52  ? -23.028 -14.598 23.287 1.00 25.02 ? 52  LYS   B CB  1 
ATOM   393  C  CG  . LYS   A 1 52  ? -24.516 -14.185 23.329 1.00 26.28 ? 52  LYS   B CG  1 
ATOM   394  C  CD  . LYS   A 1 52  ? -24.920 -13.595 24.639 1.00 32.67 ? 52  LYS   B CD  1 
ATOM   395  C  CE  . LYS   A 1 52  ? -26.405 -13.286 24.668 1.00 37.31 ? 52  LYS   B CE  1 
ATOM   396  N  NZ  . LYS   A 1 52  ? -26.716 -11.928 24.156 1.00 31.34 ? 52  LYS   B NZ  1 
ATOM   397  N  N   . TYR   A 1 53  ? -22.953 -12.805 20.308 1.00 15.77 ? 53  TYR   B N   1 
ATOM   398  C  CA  . TYR   A 1 53  ? -22.931 -11.418 19.854 1.00 16.25 ? 53  TYR   B CA  1 
ATOM   399  C  C   . TYR   A 1 53  ? -24.357 -10.948 19.577 1.00 20.43 ? 53  TYR   B C   1 
ATOM   400  O  O   . TYR   A 1 53  ? -24.996 -11.463 18.644 1.00 23.44 ? 53  TYR   B O   1 
ATOM   401  C  CB  . TYR   A 1 53  ? -22.166 -11.283 18.547 1.00 17.35 ? 53  TYR   B CB  1 
ATOM   402  C  CG  . TYR   A 1 53  ? -20.657 -11.453 18.625 1.00 15.24 ? 53  TYR   B CG  1 
ATOM   403  C  CD1 . TYR   A 1 53  ? -19.935 -11.174 19.791 1.00 15.21 ? 53  TYR   B CD1 1 
ATOM   404  C  CD2 . TYR   A 1 53  ? -19.963 -11.871 17.509 1.00 15.05 ? 53  TYR   B CD2 1 
ATOM   405  C  CE1 . TYR   A 1 53  ? -18.546 -11.259 19.794 1.00 15.57 ? 53  TYR   B CE1 1 
ATOM   406  C  CE2 . TYR   A 1 53  ? -18.581 -12.008 17.497 1.00 15.87 ? 53  TYR   B CE2 1 
ATOM   407  C  CZ  . TYR   A 1 53  ? -17.878 -11.695 18.656 1.00 15.97 ? 53  TYR   B CZ  1 
ATOM   408  O  OH  . TYR   A 1 53  ? -16.530 -11.854 18.673 1.00 15.62 ? 53  TYR   B OH  1 
ATOM   409  N  N   . ASP   A 1 54  ? -24.838 -9.977  20.366 1.00 18.13 ? 54  ASP   B N   1 
ATOM   410  C  CA  . ASP   A 1 54  ? -26.238 -9.573  20.301 1.00 20.10 ? 54  ASP   B CA  1 
ATOM   411  C  C   . ASP   A 1 54  ? -26.354 -8.590  19.144 1.00 19.79 ? 54  ASP   B C   1 
ATOM   412  O  O   . ASP   A 1 54  ? -25.563 -7.653  19.049 1.00 17.80 ? 54  ASP   B O   1 
ATOM   413  C  CB  . ASP   A 1 54  ? -26.612 -8.895  21.626 1.00 18.49 ? 54  ASP   B CB  1 
ATOM   414  C  CG  . ASP   A 1 54  ? -28.110 -8.718  21.845 1.00 25.12 ? 54  ASP   B CG  1 
ATOM   415  O  OD1 . ASP   A 1 54  ? -28.785 -8.182  20.916 1.00 26.08 ? 54  ASP   B OD1 1 
ATOM   416  O  OD2 . ASP   A 1 54  ? -28.573 -9.080  22.961 1.00 27.05 ? 54  ASP   B OD2 1 
ATOM   417  N  N   . PRO   A 1 55  ? -27.300 -8.755  18.189 1.00 22.48 ? 55  PRO   B N   1 
ATOM   418  C  CA  . PRO   A 1 55  ? -27.417 -7.809  17.074 1.00 23.04 ? 55  PRO   B CA  1 
ATOM   419  C  C   . PRO   A 1 55  ? -27.832 -6.416  17.525 1.00 23.78 ? 55  PRO   B C   1 
ATOM   420  O  O   . PRO   A 1 55  ? -27.542 -5.435  16.841 1.00 27.51 ? 55  PRO   B O   1 
ATOM   421  C  CB  . PRO   A 1 55  ? -28.467 -8.442  16.136 1.00 23.78 ? 55  PRO   B CB  1 
ATOM   422  C  CG  . PRO   A 1 55  ? -29.216 -9.411  17.022 1.00 26.74 ? 55  PRO   B CG  1 
ATOM   423  C  CD  . PRO   A 1 55  ? -28.229 -9.899  18.074 1.00 22.98 ? 55  PRO   B CD  1 
ATOM   424  N  N   . SER   A 1 56  ? -28.426 -6.308  18.718 1.00 21.66 ? 56  SER   B N   1 
ATOM   425  C  CA  . SER   A 1 56  ? -28.666 -4.967  19.241 1.00 22.72 ? 56  SER   B CA  1 
ATOM   426  C  C   . SER   A 1 56  ? -27.436 -4.245  19.820 1.00 21.65 ? 56  SER   B C   1 
ATOM   427  O  O   . SER   A 1 56  ? -27.520 -3.072  20.200 1.00 24.37 ? 56  SER   B O   1 
ATOM   428  C  CB  . SER   A 1 56  ? -29.810 -5.007  20.247 1.00 24.08 ? 56  SER   B CB  1 
ATOM   429  O  OG  . SER   A 1 56  ? -29.359 -5.471  21.513 1.00 29.65 ? 56  SER   B OG  1 
ATOM   430  N  N   . SER   A 1 57  ? -26.272 -4.884  19.933 1.00 17.74 ? 57  SER   B N   1 
ATOM   431  C  CA  . SER   A 1 57  ? -25.124 -4.228  20.532 1.00 16.33 ? 57  SER   B CA  1 
ATOM   432  C  C   . SER   A 1 57  ? -24.498 -3.164  19.625 1.00 15.13 ? 57  SER   B C   1 
ATOM   433  O  O   . SER   A 1 57  ? -23.928 -2.226  20.164 1.00 16.49 ? 57  SER   B O   1 
ATOM   434  C  CB  . SER   A 1 57  ? -24.042 -5.258  20.928 1.00 16.44 ? 57  SER   B CB  1 
ATOM   435  O  OG  . SER   A 1 57  ? -24.552 -6.063  21.999 1.00 18.28 ? 57  SER   B OG  1 
ATOM   436  N  N   . ALA   A 1 58  ? -24.535 -3.338  18.293 1.00 14.56 ? 58  ALA   B N   1 
ATOM   437  C  CA  . ALA   A 1 58  ? -23.911 -2.320  17.426 1.00 16.33 ? 58  ALA   B CA  1 
ATOM   438  C  C   . ALA   A 1 58  ? -24.698 -1.011  17.498 1.00 15.09 ? 58  ALA   B C   1 
ATOM   439  O  O   . ALA   A 1 58  ? -25.936 -1.067  17.563 1.00 17.10 ? 58  ALA   B O   1 
ATOM   440  C  CB  . ALA   A 1 58  ? -23.993 -2.776  16.002 1.00 16.51 ? 58  ALA   B CB  1 
ATOM   441  N  N   . LYS   A 1 59  ? -23.988 0.131   17.483 1.00 15.48 ? 59  LYS   B N   1 
ATOM   442  C  CA  . LYS   A 1 59  ? -24.752 1.367   17.626 1.00 15.62 ? 59  LYS   B CA  1 
ATOM   443  C  C   . LYS   A 1 59  ? -24.331 2.458   16.622 1.00 18.44 ? 59  LYS   B C   1 
ATOM   444  O  O   . LYS   A 1 59  ? -25.210 3.204   16.197 1.00 18.24 ? 59  LYS   B O   1 
ATOM   445  C  CB  . LYS   A 1 59  ? -24.567 1.937   19.023 1.00 15.76 ? 59  LYS   B CB  1 
ATOM   446  C  CG  . LYS   A 1 59  ? -25.041 1.044   20.163 1.00 16.64 ? 59  LYS   B CG  1 
ATOM   447  C  CD  . LYS   A 1 59  ? -26.546 0.856   20.163 1.00 16.30 ? 59  LYS   B CD  1 
ATOM   448  C  CE  . LYS   A 1 59  ? -26.904 -0.165  21.239 1.00 19.66 ? 59  LYS   B CE  1 
ATOM   449  N  NZ  . LYS   A 1 59  ? -28.372 -0.409  21.248 1.00 21.75 ? 59  LYS   B NZ  1 
ATOM   450  N  N   . ILE   A 1 60  ? -23.033 2.606   16.329 1.00 16.70 ? 60  ILE   B N   1 
ATOM   451  C  CA  . ILE   A 1 60  ? -22.505 3.734   15.558 1.00 16.30 ? 60  ILE   B CA  1 
ATOM   452  C  C   . ILE   A 1 60  ? -21.407 3.217   14.635 1.00 16.30 ? 60  ILE   B C   1 
ATOM   453  O  O   . ILE   A 1 60  ? -20.692 2.282   15.009 1.00 16.43 ? 60  ILE   B O   1 
ATOM   454  C  CB  . ILE   A 1 60  ? -21.851 4.781   16.507 1.00 18.80 ? 60  ILE   B CB  1 
ATOM   455  C  CG1 . ILE   A 1 60  ? -22.767 5.273   17.644 1.00 20.36 ? 60  ILE   B CG1 1 
ATOM   456  C  CG2 . ILE   A 1 60  ? -21.161 5.923   15.721 1.00 18.07 ? 60  ILE   B CG2 1 
ATOM   457  C  CD1 . ILE   A 1 60  ? -23.815 6.279   17.233 1.00 23.73 ? 60  ILE   B CD1 1 
ATOM   458  N  N   . ILE   A 1 61  ? -21.325 3.763   13.415 1.00 15.82 ? 61  ILE   B N   1 
ATOM   459  C  CA  . ILE   A 1 61  ? -20.136 3.500   12.591 1.00 14.58 ? 61  ILE   B CA  1 
ATOM   460  C  C   . ILE   A 1 61  ? -19.491 4.850   12.274 1.00 18.47 ? 61  ILE   B C   1 
ATOM   461  O  O   . ILE   A 1 61  ? -20.188 5.824   12.019 1.00 16.90 ? 61  ILE   B O   1 
ATOM   462  C  CB  . ILE   A 1 61  ? -20.481 2.729   11.302 1.00 15.30 ? 61  ILE   B CB  1 
ATOM   463  C  CG1 . ILE   A 1 61  ? -19.217 2.315   10.511 1.00 13.92 ? 61  ILE   B CG1 1 
ATOM   464  C  CG2 . ILE   A 1 61  ? -21.450 3.501   10.398 1.00 17.48 ? 61  ILE   B CG2 1 
ATOM   465  C  CD1 . ILE   A 1 61  ? -19.525 1.321   9.417  1.00 14.60 ? 61  ILE   B CD1 1 
ATOM   466  N  N   . SER   A 1 62  ? -18.164 4.879   12.271 1.00 16.07 ? 62  SER   B N   1 
ATOM   467  C  CA  . SER   A 1 62  ? -17.464 6.140   12.072 1.00 16.85 ? 62  SER   B CA  1 
ATOM   468  C  C   . SER   A 1 62  ? -16.184 5.926   11.277 1.00 15.92 ? 62  SER   B C   1 
ATOM   469  O  O   . SER   A 1 62  ? -15.716 4.787   11.125 1.00 16.67 ? 62  SER   B O   1 
ATOM   470  C  CB  . SER   A 1 62  ? -17.144 6.729   13.394 1.00 20.61 ? 62  SER   B CB  1 
ATOM   471  O  OG  . SER   A 1 62  ? -16.207 5.918   14.071 1.00 23.03 ? 62  SER   B OG  1 
ATOM   472  N  N   . ASN   A 1 63  ? -15.697 7.018   10.656 1.00 14.65 ? 63  ASN   B N   1 
ATOM   473  C  CA  . ASN   A 1 63  ? -14.409 6.947   9.969  1.00 13.45 ? 63  ASN   B CA  1 
ATOM   474  C  C   . ASN   A 1 63  ? -13.372 7.514   10.931 1.00 14.12 ? 63  ASN   B C   1 
ATOM   475  O  O   . ASN   A 1 63  ? -13.373 8.713   11.250 1.00 16.68 ? 63  ASN   B O   1 
ATOM   476  C  CB  . ASN   A 1 63  ? -14.482 7.734   8.663  1.00 14.21 ? 63  ASN   B CB  1 
ATOM   477  C  CG  . ASN   A 1 63  ? -13.168 7.793   7.910  1.00 16.47 ? 63  ASN   B CG  1 
ATOM   478  O  OD1 . ASN   A 1 63  ? -12.133 7.385   8.432  1.00 18.47 ? 63  ASN   B OD1 1 
ATOM   479  N  ND2 . ASN   A 1 63  ? -13.213 8.281   6.667  1.00 15.27 ? 63  ASN   B ND2 1 
ATOM   480  N  N   . SER   A 1 64  ? -12.436 6.677   11.410 1.00 13.94 ? 64  SER   B N   1 
ATOM   481  C  CA  . SER   A 1 64  ? -11.408 7.138   12.337 1.00 14.89 ? 64  SER   B CA  1 
ATOM   482  C  C   . SER   A 1 64  ? -10.267 7.880   11.630 1.00 15.83 ? 64  SER   B C   1 
ATOM   483  O  O   . SER   A 1 64  ? -9.378  8.433   12.277 1.00 22.65 ? 64  SER   B O   1 
ATOM   484  C  CB  . SER   A 1 64  ? -10.838 5.955   13.093 1.00 16.81 ? 64  SER   B CB  1 
ATOM   485  O  OG  . SER   A 1 64  ? -10.093 5.124   12.196 1.00 16.19 ? 64  SER   B OG  1 
ATOM   486  N  N   . GLY   A 1 65  ? -10.241 7.791   10.313 1.00 17.40 ? 65  GLY   B N   1 
ATOM   487  C  CA  . GLY   A 1 65  ? -9.106  8.207   9.514  1.00 16.31 ? 65  GLY   B CA  1 
ATOM   488  C  C   . GLY   A 1 65  ? -8.159  7.051   9.181  1.00 15.60 ? 65  GLY   B C   1 
ATOM   489  O  O   . GLY   A 1 65  ? -7.333  7.194   8.264  1.00 16.76 ? 65  GLY   B O   1 
ATOM   490  N  N   . HIS   A 1 66  ? -8.311  5.909   9.899  1.00 14.99 ? 66  HIS   B N   1 
ATOM   491  C  CA  . HIS   A 1 66  ? -7.432  4.768   9.665  1.00 14.14 ? 66  HIS   B CA  1 
ATOM   492  C  C   . HIS   A 1 66  ? -8.194  3.506   9.224  1.00 13.74 ? 66  HIS   B C   1 
ATOM   493  O  O   . HIS   A 1 66  ? -7.537  2.579   8.779  1.00 14.54 ? 66  HIS   B O   1 
ATOM   494  C  CB  . HIS   A 1 66  ? -6.631  4.415   10.947 1.00 17.30 ? 66  HIS   B CB  1 
ATOM   495  C  CG  . HIS   A 1 66  ? -6.186  5.624   11.684 1.00 23.16 ? 66  HIS   B CG  1 
ATOM   496  N  ND1 . HIS   A 1 66  ? -5.145  6.417   11.199 1.00 26.64 ? 66  HIS   B ND1 1 
ATOM   497  C  CD2 . HIS   A 1 66  ? -6.581  6.158   12.863 1.00 21.78 ? 66  HIS   B CD2 1 
ATOM   498  C  CE1 . HIS   A 1 66  ? -4.932  7.422   12.041 1.00 27.34 ? 66  HIS   B CE1 1 
ATOM   499  N  NE2 . HIS   A 1 66  ? -5.825  7.328   13.022 1.00 26.05 ? 66  HIS   B NE2 1 
ATOM   500  N  N   . SER   A 1 67  ? -9.528  3.484   9.424  1.00 12.68 ? 67  SER   B N   1 
ATOM   501  C  CA  . SER   A 1 67  ? -10.414 2.421   9.007  1.00 13.07 ? 67  SER   B CA  1 
ATOM   502  C  C   . SER   A 1 67  ? -11.810 2.946   9.287  1.00 14.85 ? 67  SER   B C   1 
ATOM   503  O  O   . SER   A 1 67  ? -11.943 4.085   9.770  1.00 16.41 ? 67  SER   B O   1 
ATOM   504  C  CB  . SER   A 1 67  ? -10.114 1.101   9.776  1.00 14.95 ? 67  SER   B CB  1 
ATOM   505  O  OG  . SER   A 1 67  ? -10.874 0.058   9.177  1.00 13.38 ? 67  SER   B OG  1 
ATOM   506  N  N   . PHE   A 1 68  ? -12.835 2.153   9.007  1.00 12.77 ? 68  PHE   B N   1 
ATOM   507  C  CA  . PHE   A 1 68  ? -14.109 2.422   9.647  1.00 13.95 ? 68  PHE   B CA  1 
ATOM   508  C  C   . PHE   A 1 68  ? -14.051 1.723   11.013 1.00 14.06 ? 68  PHE   B C   1 
ATOM   509  O  O   . PHE   A 1 68  ? -13.290 0.774   11.182 1.00 17.23 ? 68  PHE   B O   1 
ATOM   510  C  CB  . PHE   A 1 68  ? -15.303 1.901   8.826  1.00 14.74 ? 68  PHE   B CB  1 
ATOM   511  C  CG  . PHE   A 1 68  ? -15.456 0.392   8.778  1.00 15.94 ? 68  PHE   B CG  1 
ATOM   512  C  CD1 . PHE   A 1 68  ? -16.077 -0.300  9.814  1.00 16.95 ? 68  PHE   B CD1 1 
ATOM   513  C  CD2 . PHE   A 1 68  ? -14.883 -0.337  7.733  1.00 17.79 ? 68  PHE   B CD2 1 
ATOM   514  C  CE1 . PHE   A 1 68  ? -16.123 -1.700  9.812  1.00 21.11 ? 68  PHE   B CE1 1 
ATOM   515  C  CE2 . PHE   A 1 68  ? -14.966 -1.738  7.715  1.00 18.08 ? 68  PHE   B CE2 1 
ATOM   516  C  CZ  . PHE   A 1 68  ? -15.577 -2.403  8.755  1.00 16.95 ? 68  PHE   B CZ  1 
ATOM   517  N  N   . ASN   A 1 69  ? -14.904 2.140   11.934 1.00 14.87 ? 69  ASN   B N   1 
ATOM   518  C  CA  . ASN   A 1 69  ? -15.009 1.551   13.261 1.00 14.57 ? 69  ASN   B CA  1 
ATOM   519  C  C   . ASN   A 1 69  ? -16.499 1.395   13.530 1.00 16.37 ? 69  ASN   B C   1 
ATOM   520  O  O   . ASN   A 1 69  ? -17.225 2.396   13.485 1.00 16.96 ? 69  ASN   B O   1 
ATOM   521  C  CB  . ASN   A 1 69  ? -14.470 2.526   14.317 1.00 20.44 ? 69  ASN   B CB  1 
ATOM   522  C  CG  . ASN   A 1 69  ? -12.967 2.588   14.458 1.00 24.82 ? 69  ASN   B CG  1 
ATOM   523  O  OD1 . ASN   A 1 69  ? -12.238 1.703   14.019 1.00 27.39 ? 69  ASN   B OD1 1 
ATOM   524  N  ND2 . ASN   A 1 69  ? -12.461 3.603   15.137 1.00 29.22 ? 69  ASN   B ND2 1 
ATOM   525  N  N   . VAL   A 1 70  ? -16.937 0.159   13.833 1.00 14.04 ? 70  VAL   B N   1 
ATOM   526  C  CA  . VAL   A 1 70  ? -18.298 -0.036  14.328 1.00 13.77 ? 70  VAL   B CA  1 
ATOM   527  C  C   . VAL   A 1 70  ? -18.152 -0.118  15.838 1.00 15.61 ? 70  VAL   B C   1 
ATOM   528  O  O   . VAL   A 1 70  ? -17.399 -0.969  16.353 1.00 15.46 ? 70  VAL   B O   1 
ATOM   529  C  CB  . VAL   A 1 70  ? -18.957 -1.318  13.783 1.00 14.25 ? 70  VAL   B CB  1 
ATOM   530  C  CG1 . VAL   A 1 70  ? -20.295 -1.572  14.497 1.00 15.30 ? 70  VAL   B CG1 1 
ATOM   531  C  CG2 . VAL   A 1 70  ? -19.158 -1.269  12.262 1.00 16.72 ? 70  VAL   B CG2 1 
ATOM   532  N  N   . ASP   A 1 71  ? -18.852 0.763   16.574 1.00 13.94 ? 71  ASP   B N   1 
ATOM   533  C  CA  . ASP   A 1 71  ? -18.755 0.766   18.030 1.00 15.83 ? 71  ASP   B CA  1 
ATOM   534  C  C   . ASP   A 1 71  ? -19.965 0.036   18.589 1.00 16.93 ? 71  ASP   B C   1 
ATOM   535  O  O   . ASP   A 1 71  ? -21.059 0.209   18.063 1.00 16.17 ? 71  ASP   B O   1 
ATOM   536  C  CB  . ASP   A 1 71  ? -18.770 2.196   18.594 1.00 20.52 ? 71  ASP   B CB  1 
ATOM   537  C  CG  . ASP   A 1 71  ? -17.501 2.996   18.342 1.00 27.34 ? 71  ASP   B CG  1 
ATOM   538  O  OD1 . ASP   A 1 71  ? -16.434 2.376   18.153 1.00 29.46 ? 71  ASP   B OD1 1 
ATOM   539  O  OD2 . ASP   A 1 71  ? -17.594 4.246   18.347 1.00 30.80 ? 71  ASP   B OD2 1 
ATOM   540  N  N   . PHE   A 1 72  ? -19.735 -0.773  19.650 1.00 14.31 ? 72  PHE   B N   1 
ATOM   541  C  CA  . PHE   A 1 72  ? -20.769 -1.560  20.297 1.00 15.41 ? 72  PHE   B CA  1 
ATOM   542  C  C   . PHE   A 1 72  ? -20.977 -1.015  21.718 1.00 15.57 ? 72  PHE   B C   1 
ATOM   543  O  O   . PHE   A 1 72  ? -20.046 -0.503  22.349 1.00 18.01 ? 72  PHE   B O   1 
ATOM   544  C  CB  . PHE   A 1 72  ? -20.297 -3.032  20.355 1.00 14.36 ? 72  PHE   B CB  1 
ATOM   545  C  CG  . PHE   A 1 72  ? -20.200 -3.662  18.987 1.00 13.80 ? 72  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   A 1 72  ? -19.066 -3.509  18.190 1.00 16.26 ? 72  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   A 1 72  ? -21.249 -4.392  18.455 1.00 14.45 ? 72  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   A 1 72  ? -19.047 -4.109  16.926 1.00 16.93 ? 72  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   A 1 72  ? -21.246 -4.940  17.179 1.00 15.67 ? 72  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   A 1 72  ? -20.109 -4.801  16.400 1.00 17.10 ? 72  PHE   B CZ  1 
ATOM   551  N  N   . ASP   A 1 73  ? -22.189 -1.207  22.238 1.00 16.57 ? 73  ASP   B N   1 
ATOM   552  C  CA  . ASP   A 1 73  ? -22.481 -0.815  23.597 1.00 17.28 ? 73  ASP   B CA  1 
ATOM   553  C  C   . ASP   A 1 73  ? -21.858 -1.857  24.507 1.00 17.91 ? 73  ASP   B C   1 
ATOM   554  O  O   . ASP   A 1 73  ? -22.349 -2.988  24.531 1.00 22.25 ? 73  ASP   B O   1 
ATOM   555  C  CB  . ASP   A 1 73  ? -24.003 -0.756  23.768 1.00 18.65 ? 73  ASP   B CB  1 
ATOM   556  C  CG  . ASP   A 1 73  ? -24.425 -0.348  25.167 1.00 19.35 ? 73  ASP   B CG  1 
ATOM   557  O  OD1 . ASP   A 1 73  ? -23.548 -0.087  25.988 1.00 21.77 ? 73  ASP   B OD1 1 
ATOM   558  O  OD2 . ASP   A 1 73  ? -25.668 -0.315  25.389 1.00 22.61 ? 73  ASP   B OD2 1 
ATOM   559  N  N   . ASP   A 1 74  ? -20.791 -1.483  25.198 1.00 17.35 ? 74  ASP   B N   1 
ATOM   560  C  CA  . ASP   A 1 74  ? -20.116 -2.401  26.104 1.00 18.62 ? 74  ASP   B CA  1 
ATOM   561  C  C   . ASP   A 1 74  ? -20.454 -2.047  27.553 1.00 19.15 ? 74  ASP   B C   1 
ATOM   562  O  O   . ASP   A 1 74  ? -19.618 -2.280  28.431 1.00 20.18 ? 74  ASP   B O   1 
ATOM   563  C  CB  . ASP   A 1 74  ? -18.592 -2.448  25.895 1.00 18.08 ? 74  ASP   B CB  1 
ATOM   564  C  CG  . ASP   A 1 74  ? -17.869 -1.126  26.056 1.00 21.51 ? 74  ASP   B CG  1 
ATOM   565  O  OD1 . ASP   A 1 74  ? -18.551 -0.124  26.277 1.00 23.09 ? 74  ASP   B OD1 1 
ATOM   566  O  OD2 . ASP   A 1 74  ? -16.617 -1.101  26.073 1.00 22.63 ? 74  ASP   B OD2 1 
ATOM   567  N  N   . THR   A 1 75  ? -21.687 -1.547  27.763 1.00 21.78 ? 75  THR   B N   1 
ATOM   568  C  CA  . THR   A 1 75  ? -22.145 -1.190  29.103 1.00 20.54 ? 75  THR   B CA  1 
ATOM   569  C  C   . THR   A 1 75  ? -22.247 -2.444  29.960 1.00 21.11 ? 75  THR   B C   1 
ATOM   570  O  O   . THR   A 1 75  ? -21.991 -2.357  31.155 1.00 21.29 ? 75  THR   B O   1 
ATOM   571  C  CB  . THR   A 1 75  ? -23.568 -0.626  29.077 1.00 22.59 ? 75  THR   B CB  1 
ATOM   572  O  OG1 . THR   A 1 75  ? -23.489 0.618   28.380 1.00 24.24 ? 75  THR   B OG1 1 
ATOM   573  C  CG2 . THR   A 1 75  ? -24.094 -0.347  30.473 1.00 27.94 ? 75  THR   B CG2 1 
ATOM   574  N  N   . GLU   A 1 76  ? -22.706 -3.565  29.381 1.00 20.00 ? 76  GLU   B N   1 
ATOM   575  C  CA  . GLU   A 1 76  ? -22.673 -4.822  30.140 1.00 23.70 ? 76  GLU   B CA  1 
ATOM   576  C  C   . GLU   A 1 76  ? -22.338 -5.973  29.200 1.00 21.20 ? 76  GLU   B C   1 
ATOM   577  O  O   . GLU   A 1 76  ? -21.613 -5.730  28.231 1.00 21.47 ? 76  GLU   B O   1 
ATOM   578  C  CB  . GLU   A 1 76  ? -23.942 -5.048  30.992 1.00 26.53 ? 76  GLU   B CB  1 
ATOM   579  C  CG  . GLU   A 1 76  ? -25.199 -5.173  30.147 1.00 26.02 ? 76  GLU   B CG  1 
ATOM   580  C  CD  . GLU   A 1 76  ? -26.482 -5.273  30.948 1.00 36.96 ? 76  GLU   B CD  1 
ATOM   581  O  OE1 . GLU   A 1 76  ? -26.416 -5.712  32.132 1.00 38.02 ? 76  GLU   B OE1 1 
ATOM   582  O  OE2 . GLU   A 1 76  ? -27.548 -4.921  30.387 1.00 47.58 ? 76  GLU   B OE2 1 
ATOM   583  N  N   . ASN   A 1 77  ? -22.741 -7.208  29.555 1.00 19.25 ? 77  ASN   B N   1 
ATOM   584  C  CA  . ASN   A 1 77  ? -22.186 -8.420  28.951 1.00 20.74 ? 77  ASN   B CA  1 
ATOM   585  C  C   . ASN   A 1 77  ? -23.164 -9.055  27.975 1.00 18.46 ? 77  ASN   B C   1 
ATOM   586  O  O   . ASN   A 1 77  ? -23.283 -10.290 27.865 1.00 21.42 ? 77  ASN   B O   1 
ATOM   587  C  CB  . ASN   A 1 77  ? -21.808 -9.505  29.970 1.00 20.05 ? 77  ASN   B CB  1 
ATOM   588  C  CG  . ASN   A 1 77  ? -20.418 -9.360  30.524 1.00 19.42 ? 77  ASN   B CG  1 
ATOM   589  O  OD1 . ASN   A 1 77  ? -19.564 -8.698  29.934 1.00 17.24 ? 77  ASN   B OD1 1 
ATOM   590  N  ND2 . ASN   A 1 77  ? -20.176 -10.004 31.666 1.00 22.61 ? 77  ASN   B ND2 1 
ATOM   591  N  N   . LYS   A 1 78  ? -23.814 -8.216  27.181 1.00 15.34 ? 78  LYS   B N   1 
ATOM   592  C  CA  . LYS   A 1 78  ? -24.728 -8.709  26.164 1.00 17.28 ? 78  LYS   B CA  1 
ATOM   593  C  C   . LYS   A 1 78  ? -23.960 -9.350  25.011 1.00 16.50 ? 78  LYS   B C   1 
ATOM   594  O  O   . LYS   A 1 78  ? -24.502 -10.259 24.398 1.00 16.26 ? 78  LYS   B O   1 
ATOM   595  C  CB  . LYS   A 1 78  ? -25.605 -7.572  25.615 1.00 20.59 ? 78  LYS   B CB  1 
ATOM   596  C  CG  . LYS   A 1 78  ? -26.693 -7.175  26.609 1.00 25.74 ? 78  LYS   B CG  1 
ATOM   597  C  CD  . LYS   A 1 78  ? -27.691 -6.208  26.030 1.00 32.11 ? 78  LYS   B CD  1 
ATOM   598  C  CE  . LYS   A 1 78  ? -28.381 -5.423  27.126 1.00 39.00 ? 78  LYS   B CE  1 
ATOM   599  N  NZ  . LYS   A 1 78  ? -29.043 -4.195  26.613 1.00 42.06 ? 78  LYS   B NZ  1 
ATOM   600  N  N   . SER   A 1 79  ? -22.720 -8.886  24.729 1.00 14.91 ? 79  SER   B N   1 
ATOM   601  C  CA  . SER   A 1 79  ? -21.945 -9.468  23.626 1.00 12.86 ? 79  SER   B CA  1 
ATOM   602  C  C   . SER   A 1 79  ? -20.545 -9.801  24.146 1.00 13.52 ? 79  SER   B C   1 
ATOM   603  O  O   . SER   A 1 79  ? -19.837 -8.888  24.613 1.00 13.32 ? 79  SER   B O   1 
ATOM   604  C  CB  . SER   A 1 79  ? -21.801 -8.495  22.432 1.00 12.96 ? 79  SER   B CB  1 
ATOM   605  O  OG  . SER   A 1 79  ? -23.053 -8.298  21.802 1.00 16.08 ? 79  SER   B OG  1 
ATOM   606  N  N   . VAL   A 1 80  ? -20.192 -11.106 24.104 1.00 13.26 ? 80  VAL   B N   1 
ATOM   607  C  CA  . VAL   A 1 80  ? -18.960 -11.541 24.774 1.00 13.78 ? 80  VAL   B CA  1 
ATOM   608  C  C   . VAL   A 1 80  ? -18.308 -12.647 23.968 1.00 13.89 ? 80  VAL   B C   1 
ATOM   609  O  O   . VAL   A 1 80  ? -18.947 -13.407 23.207 1.00 14.19 ? 80  VAL   B O   1 
ATOM   610  C  CB  . VAL   A 1 80  ? -19.227 -12.079 26.208 1.00 16.29 ? 80  VAL   B CB  1 
ATOM   611  C  CG1 . VAL   A 1 80  ? -19.694 -10.993 27.184 1.00 16.52 ? 80  VAL   B CG1 1 
ATOM   612  C  CG2 . VAL   A 1 80  ? -20.214 -13.231 26.176 1.00 19.39 ? 80  VAL   B CG2 1 
ATOM   613  N  N   . LEU   A 1 81  ? -17.002 -12.776 24.206 1.00 13.38 ? 81  LEU   B N   1 
ATOM   614  C  CA  . LEU   A 1 81  ? -16.215 -13.887 23.705 1.00 12.87 ? 81  LEU   B CA  1 
ATOM   615  C  C   . LEU   A 1 81  ? -15.642 -14.635 24.913 1.00 12.94 ? 81  LEU   B C   1 
ATOM   616  O  O   . LEU   A 1 81  ? -15.080 -14.037 25.835 1.00 13.05 ? 81  LEU   B O   1 
ATOM   617  C  CB  . LEU   A 1 81  ? -15.068 -13.316 22.850 1.00 13.62 ? 81  LEU   B CB  1 
ATOM   618  C  CG  . LEU   A 1 81  ? -13.992 -14.332 22.420 1.00 15.05 ? 81  LEU   B CG  1 
ATOM   619  C  CD1 . LEU   A 1 81  ? -14.607 -15.352 21.465 1.00 18.42 ? 81  LEU   B CD1 1 
ATOM   620  C  CD2 . LEU   A 1 81  ? -12.894 -13.581 21.665 1.00 14.75 ? 81  LEU   B CD2 1 
ATOM   621  N  N   . ARG   A 1 82  ? -15.781 -15.960 24.895 1.00 13.17 ? 82  ARG   B N   1 
ATOM   622  C  CA  . ARG   A 1 82  ? -15.257 -16.759 26.002 1.00 14.62 ? 82  ARG   B CA  1 
ATOM   623  C  C   . ARG   A 1 82  ? -14.566 -17.974 25.376 1.00 12.68 ? 82  ARG   B C   1 
ATOM   624  O  O   . ARG   A 1 82  ? -14.705 -18.279 24.193 1.00 13.99 ? 82  ARG   B O   1 
ATOM   625  C  CB  . ARG   A 1 82  ? -16.414 -17.275 26.887 1.00 18.57 ? 82  ARG   B CB  1 
ATOM   626  C  CG  . ARG   A 1 82  ? -17.479 -16.243 27.264 1.00 23.41 ? 82  ARG   B CG  1 
ATOM   627  C  CD  . ARG   A 1 82  ? -18.919 -16.690 27.437 1.00 25.96 ? 82  ARG   B CD  1 
ATOM   628  N  NE  . ARG   A 1 82  ? -19.578 -17.349 26.303 1.00 27.21 ? 82  ARG   B NE  1 
ATOM   629  C  CZ  . ARG   A 1 82  ? -20.904 -17.329 26.155 1.00 24.04 ? 82  ARG   B CZ  1 
ATOM   630  N  NH1 . ARG   A 1 82  ? -21.625 -16.623 27.013 1.00 23.76 ? 82  ARG   B NH1 1 
ATOM   631  N  NH2 . ARG   A 1 82  ? -21.470 -17.952 25.134 1.00 24.20 ? 82  ARG   B NH2 1 
ATOM   632  N  N   . GLY   A 1 83  ? -13.815 -18.712 26.195 1.00 15.44 ? 83  GLY   B N   1 
ATOM   633  C  CA  . GLY   A 1 83  ? -13.180 -19.948 25.715 1.00 13.37 ? 83  GLY   B CA  1 
ATOM   634  C  C   . GLY   A 1 83  ? -11.880 -19.666 24.954 1.00 15.94 ? 83  GLY   B C   1 
ATOM   635  O  O   . GLY   A 1 83  ? -11.170 -18.661 25.205 1.00 17.28 ? 83  GLY   B O   1 
ATOM   636  N  N   . GLY   A 1 84  ? -11.564 -20.556 24.021 1.00 14.31 ? 84  GLY   B N   1 
ATOM   637  C  CA  . GLY   A 1 84  ? -10.286 -20.409 23.331 1.00 16.95 ? 84  GLY   B CA  1 
ATOM   638  C  C   . GLY   A 1 84  ? -9.128  -20.451 24.322 1.00 18.11 ? 84  GLY   B C   1 
ATOM   639  O  O   . GLY   A 1 84  ? -9.094  -21.274 25.244 1.00 17.96 ? 84  GLY   B O   1 
ATOM   640  N  N   . PRO   A 1 85  ? -8.114  -19.560 24.168 1.00 15.84 ? 85  PRO   B N   1 
ATOM   641  C  CA  . PRO   A 1 85  ? -7.032  -19.463 25.148 1.00 15.59 ? 85  PRO   B CA  1 
ATOM   642  C  C   . PRO   A 1 85  ? -7.380  -18.596 26.357 1.00 15.33 ? 85  PRO   B C   1 
ATOM   643  O  O   . PRO   A 1 85  ? -6.545  -18.463 27.246 1.00 17.08 ? 85  PRO   B O   1 
ATOM   644  C  CB  . PRO   A 1 85  ? -5.960  -18.792 24.249 1.00 15.20 ? 85  PRO   B CB  1 
ATOM   645  C  CG  . PRO   A 1 85  ? -6.753  -17.826 23.424 1.00 15.29 ? 85  PRO   B CG  1 
ATOM   646  C  CD  . PRO   A 1 85  ? -7.983  -18.622 23.024 1.00 15.43 ? 85  PRO   B CD  1 
ATOM   647  N  N   . LEU   A 1 86  ? -8.596  -18.005 26.411 1.00 14.83 ? 86  LEU   B N   1 
ATOM   648  C  CA  . LEU   A 1 86  ? -8.872  -16.945 27.367 1.00 15.53 ? 86  LEU   B CA  1 
ATOM   649  C  C   . LEU   A 1 86  ? -9.344  -17.499 28.721 1.00 16.05 ? 86  LEU   B C   1 
ATOM   650  O  O   . LEU   A 1 86  ? -10.105 -18.467 28.769 1.00 17.36 ? 86  LEU   B O   1 
ATOM   651  C  CB  . LEU   A 1 86  ? -10.015 -16.100 26.780 1.00 14.94 ? 86  LEU   B CB  1 
ATOM   652  C  CG  . LEU   A 1 86  ? -9.712  -15.562 25.367 1.00 13.87 ? 86  LEU   B CG  1 
ATOM   653  C  CD1 . LEU   A 1 86  ? -10.914 -14.767 24.857 1.00 15.57 ? 86  LEU   B CD1 1 
ATOM   654  C  CD2 . LEU   A 1 86  ? -8.531  -14.603 25.445 1.00 15.60 ? 86  LEU   B CD2 1 
ATOM   655  N  N   . THR   A 1 87  ? -8.957  -16.803 29.788 1.00 16.41 ? 87  THR   B N   1 
ATOM   656  C  CA  . THR   A 1 87  ? -9.578  -16.993 31.098 1.00 17.33 ? 87  THR   B CA  1 
ATOM   657  C  C   . THR   A 1 87  ? -10.686 -15.951 31.285 1.00 20.28 ? 87  THR   B C   1 
ATOM   658  O  O   . THR   A 1 87  ? -10.399 -14.759 31.175 1.00 25.03 ? 87  THR   B O   1 
ATOM   659  C  CB  . THR   A 1 87  ? -8.532  -16.822 32.197 1.00 19.24 ? 87  THR   B CB  1 
ATOM   660  O  OG1 . THR   A 1 87  ? -7.565  -17.853 31.986 1.00 22.41 ? 87  THR   B OG1 1 
ATOM   661  C  CG2 . THR   A 1 87  ? -9.172  -17.002 33.558 1.00 20.20 ? 87  THR   B CG2 1 
ATOM   662  N  N   . GLY   A 1 88  ? -11.914 -16.416 31.556 1.00 20.77 ? 88  GLY   B N   1 
ATOM   663  C  CA  . GLY   A 1 88  ? -13.049 -15.539 31.816 1.00 20.12 ? 88  GLY   B CA  1 
ATOM   664  C  C   . GLY   A 1 88  ? -13.670 -15.012 30.519 1.00 22.07 ? 88  GLY   B C   1 
ATOM   665  O  O   . GLY   A 1 88  ? -13.536 -15.586 29.440 1.00 24.79 ? 88  GLY   B O   1 
ATOM   666  N  N   . SER   A 1 89  ? -14.351 -13.882 30.656 1.00 17.13 ? 89  SER   B N   1 
ATOM   667  C  CA  . SER   A 1 89  ? -15.228 -13.365 29.638 1.00 16.45 ? 89  SER   B CA  1 
ATOM   668  C  C   . SER   A 1 89  ? -14.700 -12.017 29.144 1.00 15.33 ? 89  SER   B C   1 
ATOM   669  O  O   . SER   A 1 89  ? -14.365 -11.129 29.939 1.00 17.15 ? 89  SER   B O   1 
ATOM   670  C  CB  . SER   A 1 89  ? -16.606 -13.215 30.282 1.00 19.39 ? 89  SER   B CB  1 
ATOM   671  O  OG  . SER   A 1 89  ? -17.544 -12.787 29.314 1.00 22.17 ? 89  SER   B OG  1 
ATOM   672  N  N   . TYR   A 1 90  ? -14.588 -11.895 27.808 1.00 13.82 ? 90  TYR   B N   1 
ATOM   673  C  CA  . TYR   A 1 90  ? -14.132 -10.640 27.195 1.00 14.67 ? 90  TYR   B CA  1 
ATOM   674  C  C   . TYR   A 1 90  ? -15.301 -9.991  26.437 1.00 15.00 ? 90  TYR   B C   1 
ATOM   675  O  O   . TYR   A 1 90  ? -15.991 -10.646 25.643 1.00 17.51 ? 90  TYR   B O   1 
ATOM   676  C  CB  . TYR   A 1 90  ? -12.950 -10.932 26.265 1.00 12.98 ? 90  TYR   B CB  1 
ATOM   677  C  CG  . TYR   A 1 90  ? -11.622 -11.213 26.935 1.00 12.75 ? 90  TYR   B CG  1 
ATOM   678  C  CD1 . TYR   A 1 90  ? -11.466 -12.297 27.811 1.00 13.26 ? 90  TYR   B CD1 1 
ATOM   679  C  CD2 . TYR   A 1 90  ? -10.510 -10.415 26.683 1.00 12.13 ? 90  TYR   B CD2 1 
ATOM   680  C  CE1 . TYR   A 1 90  ? -10.230 -12.559 28.404 1.00 13.25 ? 90  TYR   B CE1 1 
ATOM   681  C  CE2 . TYR   A 1 90  ? -9.275  -10.681 27.275 1.00 12.60 ? 90  TYR   B CE2 1 
ATOM   682  C  CZ  . TYR   A 1 90  ? -9.157  -11.751 28.144 1.00 13.12 ? 90  TYR   B CZ  1 
ATOM   683  O  OH  . TYR   A 1 90  ? -7.937  -12.041 28.694 1.00 13.87 ? 90  TYR   B OH  1 
ATOM   684  N  N   . ARG   A 1 91  ? -15.506 -8.688  26.658 1.00 12.92 ? 91  ARG   B N   1 
ATOM   685  C  CA  . ARG   A 1 91  ? -16.675 -7.962  26.186 1.00 12.89 ? 91  ARG   B CA  1 
ATOM   686  C  C   . ARG   A 1 91  ? -16.387 -7.295  24.839 1.00 12.31 ? 91  ARG   B C   1 
ATOM   687  O  O   . ARG   A 1 91  ? -15.350 -6.670  24.703 1.00 11.15 ? 91  ARG   B O   1 
ATOM   688  C  CB  . ARG   A 1 91  ? -16.966 -6.855  27.208 1.00 14.53 ? 91  ARG   B CB  1 
ATOM   689  C  CG  . ARG   A 1 91  ? -18.344 -6.248  27.050 1.00 15.78 ? 91  ARG   B CG  1 
ATOM   690  C  CD  . ARG   A 1 91  ? -18.615 -5.320  28.241 1.00 15.88 ? 91  ARG   B CD  1 
ATOM   691  N  NE  . ARG   A 1 91  ? -18.750 -6.028  29.529 1.00 16.91 ? 91  ARG   B NE  1 
ATOM   692  C  CZ  . ARG   A 1 91  ? -18.929 -5.398  30.688 1.00 16.05 ? 91  ARG   B CZ  1 
ATOM   693  N  NH1 . ARG   A 1 91  ? -18.955 -4.069  30.733 1.00 17.52 ? 91  ARG   B NH1 1 
ATOM   694  N  NH2 . ARG   A 1 91  ? -19.016 -6.107  31.804 1.00 18.24 ? 91  ARG   B NH2 1 
ATOM   695  N  N   . LEU   A 1 92  ? -17.316 -7.433  23.886 1.00 11.53 ? 92  LEU   B N   1 
ATOM   696  C  CA  . LEU   A 1 92  ? -17.183 -6.853  22.550 1.00 13.69 ? 92  LEU   B CA  1 
ATOM   697  C  C   . LEU   A 1 92  ? -17.156 -5.323  22.641 1.00 14.23 ? 92  LEU   B C   1 
ATOM   698  O  O   . LEU   A 1 92  ? -18.050 -4.744  23.235 1.00 15.69 ? 92  LEU   B O   1 
ATOM   699  C  CB  . LEU   A 1 92  ? -18.328 -7.374  21.683 1.00 13.57 ? 92  LEU   B CB  1 
ATOM   700  C  CG  . LEU   A 1 92  ? -18.412 -6.783  20.280 1.00 12.58 ? 92  LEU   B CG  1 
ATOM   701  C  CD1 . LEU   A 1 92  ? -17.176 -7.138  19.451 1.00 13.45 ? 92  LEU   B CD1 1 
ATOM   702  C  CD2 . LEU   A 1 92  ? -19.709 -7.255  19.602 1.00 12.79 ? 92  LEU   B CD2 1 
ATOM   703  N  N   . ARG   A 1 93  ? -16.153 -4.686  22.022 1.00 13.08 ? 93  ARG   B N   1 
ATOM   704  C  CA  . ARG   A 1 93  ? -16.056 -3.234  21.947 1.00 13.78 ? 93  ARG   B CA  1 
ATOM   705  C  C   . ARG   A 1 93  ? -16.187 -2.631  20.544 1.00 13.82 ? 93  ARG   B C   1 
ATOM   706  O  O   . ARG   A 1 93  ? -16.945 -1.657  20.334 1.00 13.90 ? 93  ARG   B O   1 
ATOM   707  C  CB  . ARG   A 1 93  ? -14.676 -2.874  22.513 1.00 18.51 ? 93  ARG   B CB  1 
ATOM   708  C  CG  . ARG   A 1 93  ? -14.250 -1.421  22.316 1.00 22.24 ? 93  ARG   B CG  1 
ATOM   709  C  CD  . ARG   A 1 93  ? -14.459 -0.671  23.580 1.00 24.55 ? 93  ARG   B CD  1 
ATOM   710  N  NE  . ARG   A 1 93  ? -13.973 0.705   23.451 1.00 22.91 ? 93  ARG   B NE  1 
ATOM   711  C  CZ  . ARG   A 1 93  ? -14.353 1.641   24.309 1.00 25.75 ? 93  ARG   B CZ  1 
ATOM   712  N  NH1 . ARG   A 1 93  ? -15.193 1.344   25.290 1.00 22.62 ? 93  ARG   B NH1 1 
ATOM   713  N  NH2 . ARG   A 1 93  ? -13.889 2.872   24.168 1.00 26.22 ? 93  ARG   B NH2 1 
ATOM   714  N  N   A GLN   A 1 94  ? -15.471 -3.196  19.559 0.50 12.96 ? 94  GLN   B N   1 
ATOM   715  N  N   B GLN   A 1 94  ? -15.467 -3.185  19.564 0.50 12.24 ? 94  GLN   B N   1 
ATOM   716  C  CA  A GLN   A 1 94  ? -15.353 -2.507  18.275 0.50 14.68 ? 94  GLN   B CA  1 
ATOM   717  C  CA  B GLN   A 1 94  ? -15.538 -2.554  18.252 0.50 13.21 ? 94  GLN   B CA  1 
ATOM   718  C  C   A GLN   A 1 94  ? -15.012 -3.508  17.170 0.50 12.97 ? 94  GLN   B C   1 
ATOM   719  C  C   B GLN   A 1 94  ? -15.066 -3.523  17.173 0.50 12.23 ? 94  GLN   B C   1 
ATOM   720  O  O   A GLN   A 1 94  ? -14.379 -4.540  17.453 0.50 13.58 ? 94  GLN   B O   1 
ATOM   721  O  O   B GLN   A 1 94  ? -14.382 -4.518  17.471 0.50 13.04 ? 94  GLN   B O   1 
ATOM   722  C  CB  A GLN   A 1 94  ? -14.282 -1.419  18.455 0.50 17.02 ? 94  GLN   B CB  1 
ATOM   723  C  CB  B GLN   A 1 94  ? -14.692 -1.276  18.270 0.50 14.60 ? 94  GLN   B CB  1 
ATOM   724  C  CG  A GLN   A 1 94  ? -13.982 -0.569  17.229 0.50 20.45 ? 94  GLN   B CG  1 
ATOM   725  C  CG  B GLN   A 1 94  ? -13.198 -1.529  18.420 0.50 14.80 ? 94  GLN   B CG  1 
ATOM   726  C  CD  A GLN   A 1 94  ? -12.615 -0.956  16.710 0.50 24.37 ? 94  GLN   B CD  1 
ATOM   727  C  CD  B GLN   A 1 94  ? -12.548 -1.279  17.073 0.50 18.53 ? 94  GLN   B CD  1 
ATOM   728  O  OE1 A GLN   A 1 94  ? -12.462 -1.990  16.072 0.50 25.73 ? 94  GLN   B OE1 1 
ATOM   729  O  OE1 B GLN   A 1 94  ? -12.294 -2.201  16.313 0.50 20.04 ? 94  GLN   B OE1 1 
ATOM   730  N  NE2 A GLN   A 1 94  ? -11.594 -0.178  17.040 0.50 28.67 ? 94  GLN   B NE2 1 
ATOM   731  N  NE2 B GLN   A 1 94  ? -12.437 -0.017  16.682 0.50 21.47 ? 94  GLN   B NE2 1 
ATOM   732  N  N   . VAL   A 1 95  ? -15.412 -3.200  15.908 1.00 11.87 ? 95  VAL   B N   1 
ATOM   733  C  CA  . VAL   A 1 95  ? -14.958 -3.968  14.750 1.00 12.68 ? 95  VAL   B CA  1 
ATOM   734  C  C   . VAL   A 1 95  ? -14.382 -2.997  13.713 1.00 11.93 ? 95  VAL   B C   1 
ATOM   735  O  O   . VAL   A 1 95  ? -14.899 -1.882  13.585 1.00 11.97 ? 95  VAL   B O   1 
ATOM   736  C  CB  . VAL   A 1 95  ? -16.142 -4.766  14.152 1.00 13.18 ? 95  VAL   B CB  1 
ATOM   737  C  CG1 . VAL   A 1 95  ? -15.834 -5.267  12.745 1.00 15.60 ? 95  VAL   B CG1 1 
ATOM   738  C  CG2 . VAL   A 1 95  ? -16.526 -5.929  15.063 1.00 14.11 ? 95  VAL   B CG2 1 
ATOM   739  N  N   . HIS   A 1 96  ? -13.273 -3.393  13.072 1.00 11.93 ? 96  HIS   B N   1 
ATOM   740  C  CA  . HIS   A 1 96  ? -12.748 -2.610  11.939 1.00 10.46 ? 96  HIS   B CA  1 
ATOM   741  C  C   . HIS   A 1 96  ? -12.085 -3.569  10.951 1.00 10.04 ? 96  HIS   B C   1 
ATOM   742  O  O   . HIS   A 1 96  ? -12.106 -4.788  11.128 1.00 10.79 ? 96  HIS   B O   1 
ATOM   743  C  CB  . HIS   A 1 96  ? -11.694 -1.578  12.425 1.00 10.33 ? 96  HIS   B CB  1 
ATOM   744  C  CG  . HIS   A 1 96  ? -10.532 -2.224  13.101 1.00 11.40 ? 96  HIS   B CG  1 
ATOM   745  N  ND1 . HIS   A 1 96  ? -10.555 -2.484  14.475 1.00 11.24 ? 96  HIS   B ND1 1 
ATOM   746  C  CD2 . HIS   A 1 96  ? -9.358  -2.727  12.630 1.00 11.10 ? 96  HIS   B CD2 1 
ATOM   747  C  CE1 . HIS   A 1 96  ? -9.407  -3.070  14.825 1.00 12.41 ? 96  HIS   B CE1 1 
ATOM   748  N  NE2 . HIS   A 1 96  ? -8.701  -3.272  13.713 1.00 12.35 ? 96  HIS   B NE2 1 
ATOM   749  N  N   . LEU   A 1 97  ? -11.554 -3.011  9.839  1.00 9.58  ? 97  LEU   B N   1 
ATOM   750  C  CA  . LEU   A 1 97  ? -11.082 -3.820  8.725  1.00 10.31 ? 97  LEU   B CA  1 
ATOM   751  C  C   . LEU   A 1 97  ? -9.737  -3.272  8.261  1.00 12.25 ? 97  LEU   B C   1 
ATOM   752  O  O   . LEU   A 1 97  ? -9.531  -2.046  8.229  1.00 12.16 ? 97  LEU   B O   1 
ATOM   753  C  CB  . LEU   A 1 97  ? -12.136 -3.761  7.587  1.00 11.13 ? 97  LEU   B CB  1 
ATOM   754  C  CG  . LEU   A 1 97  ? -11.848 -4.617  6.360  1.00 12.83 ? 97  LEU   B CG  1 
ATOM   755  C  CD1 . LEU   A 1 97  ? -12.010 -6.091  6.674  1.00 13.03 ? 97  LEU   B CD1 1 
ATOM   756  C  CD2 . LEU   A 1 97  ? -12.766 -4.251  5.192  1.00 13.29 ? 97  LEU   B CD2 1 
ATOM   757  N  N   . HIS   A 1 98  ? -8.857  -4.171  7.817  1.00 9.91  ? 98  HIS   B N   1 
ATOM   758  C  CA  . HIS   A 1 98  ? -7.624  -3.771  7.151  1.00 11.78 ? 98  HIS   B CA  1 
ATOM   759  C  C   . HIS   A 1 98  ? -7.631  -4.288  5.721  1.00 11.76 ? 98  HIS   B C   1 
ATOM   760  O  O   . HIS   A 1 98  ? -8.083  -5.400  5.453  1.00 12.31 ? 98  HIS   B O   1 
ATOM   761  C  CB  . HIS   A 1 98  ? -6.393  -4.384  7.865  1.00 10.74 ? 98  HIS   B CB  1 
ATOM   762  C  CG  . HIS   A 1 98  ? -6.261  -3.946  9.301  1.00 10.60 ? 98  HIS   B CG  1 
ATOM   763  N  ND1 . HIS   A 1 98  ? -5.515  -2.814  9.682  1.00 11.18 ? 98  HIS   B ND1 1 
ATOM   764  C  CD2 . HIS   A 1 98  ? -6.772  -4.461  10.450 1.00 11.45 ? 98  HIS   B CD2 1 
ATOM   765  C  CE1 . HIS   A 1 98  ? -5.597  -2.656  11.014 1.00 12.36 ? 98  HIS   B CE1 1 
ATOM   766  N  NE2 . HIS   A 1 98  ? -6.372  -3.671  11.517 1.00 10.35 ? 98  HIS   B NE2 1 
ATOM   767  N  N   . TRP   A 1 99  ? -7.011  -3.511  4.823  1.00 10.84 ? 99  TRP   B N   1 
ATOM   768  C  CA  . TRP   A 1 99  ? -6.891  -3.901  3.406  1.00 11.74 ? 99  TRP   B CA  1 
ATOM   769  C  C   . TRP   A 1 99  ? -5.596  -3.312  2.846  1.00 11.95 ? 99  TRP   B C   1 
ATOM   770  O  O   . TRP   A 1 99  ? -4.863  -2.588  3.537  1.00 12.18 ? 99  TRP   B O   1 
ATOM   771  C  CB  . TRP   A 1 99  ? -8.119  -3.407  2.633  1.00 11.44 ? 99  TRP   B CB  1 
ATOM   772  C  CG  . TRP   A 1 99  ? -8.293  -1.916  2.724  1.00 11.27 ? 99  TRP   B CG  1 
ATOM   773  C  CD1 . TRP   A 1 99  ? -7.705  -0.945  1.930  1.00 11.34 ? 99  TRP   B CD1 1 
ATOM   774  C  CD2 . TRP   A 1 99  ? -9.172  -1.213  3.641  1.00 11.23 ? 99  TRP   B CD2 1 
ATOM   775  N  NE1 . TRP   A 1 99  ? -8.144  0.320   2.333  1.00 12.86 ? 99  TRP   B NE1 1 
ATOM   776  C  CE2 . TRP   A 1 99  ? -9.057  0.176   3.364  1.00 12.59 ? 99  TRP   B CE2 1 
ATOM   777  C  CE3 . TRP   A 1 99  ? -9.997  -1.631  4.703  1.00 11.72 ? 99  TRP   B CE3 1 
ATOM   778  C  CZ2 . TRP   A 1 99  ? -9.768  1.120   4.111  1.00 13.01 ? 99  TRP   B CZ2 1 
ATOM   779  C  CZ3 . TRP   A 1 99  ? -10.739 -0.707  5.388  1.00 12.93 ? 99  TRP   B CZ3 1 
ATOM   780  C  CH2 . TRP   A 1 99  ? -10.610 0.658   5.124  1.00 13.10 ? 99  TRP   B CH2 1 
ATOM   781  N  N   . GLY   A 1 100 ? -5.317  -3.637  1.577  1.00 12.25 ? 100 GLY   B N   1 
ATOM   782  C  CA  . GLY   A 1 100 ? -4.164  -3.047  0.882  1.00 14.09 ? 100 GLY   B CA  1 
ATOM   783  C  C   . GLY   A 1 100 ? -4.618  -2.361  -0.404 1.00 13.98 ? 100 GLY   B C   1 
ATOM   784  O  O   . GLY   A 1 100 ? -5.809  -2.338  -0.705 1.00 12.75 ? 100 GLY   B O   1 
ATOM   785  N  N   . SER   A 1 101 ? -3.657  -1.789  -1.161 1.00 14.49 ? 101 SER   B N   1 
ATOM   786  C  CA  . SER   A 1 101 ? -4.114  -1.187  -2.421 1.00 14.59 ? 101 SER   B CA  1 
ATOM   787  C  C   . SER   A 1 101 ? -4.386  -2.238  -3.503 1.00 17.46 ? 101 SER   B C   1 
ATOM   788  O  O   . SER   A 1 101 ? -5.119  -1.963  -4.454 1.00 16.18 ? 101 SER   B O   1 
ATOM   789  C  CB  . SER   A 1 101 ? -3.116  -0.166  -2.930 1.00 16.66 ? 101 SER   B CB  1 
ATOM   790  O  OG  . SER   A 1 101 ? -1.954  -0.859  -3.360 1.00 19.40 ? 101 SER   B OG  1 
ATOM   791  N  N   . ALA   A 1 102 ? -3.917  -3.456  -3.306 1.00 16.67 ? 102 ALA   B N   1 
ATOM   792  C  CA  . ALA   A 1 102 ? -4.198  -4.542  -4.237 1.00 18.91 ? 102 ALA   B CA  1 
ATOM   793  C  C   . ALA   A 1 102 ? -4.908  -5.702  -3.533 1.00 18.46 ? 102 ALA   B C   1 
ATOM   794  O  O   . ALA   A 1 102 ? -4.616  -6.000  -2.387 1.00 18.97 ? 102 ALA   B O   1 
ATOM   795  C  CB  . ALA   A 1 102 ? -2.879  -5.027  -4.813 1.00 19.62 ? 102 ALA   B CB  1 
ATOM   796  N  N   . ASP   A 1 103 ? -5.818  -6.373  -4.252 1.00 18.14 ? 103 ASP   B N   1 
ATOM   797  C  CA  . ASP   A 1 103 ? -6.595  -7.470  -3.664 1.00 18.34 ? 103 ASP   B CA  1 
ATOM   798  C  C   . ASP   A 1 103 ? -5.740  -8.683  -3.277 1.00 20.20 ? 103 ASP   B C   1 
ATOM   799  O  O   . ASP   A 1 103 ? -6.248  -9.580  -2.581 1.00 21.37 ? 103 ASP   B O   1 
ATOM   800  C  CB  . ASP   A 1 103 ? -7.722  -7.870  -4.624 1.00 17.20 ? 103 ASP   B CB  1 
ATOM   801  C  CG  . ASP   A 1 103 ? -8.860  -6.874  -4.757 1.00 18.83 ? 103 ASP   B CG  1 
ATOM   802  O  OD1 . ASP   A 1 103 ? -8.812  -5.797  -4.125 1.00 22.75 ? 103 ASP   B OD1 1 
ATOM   803  O  OD2 . ASP   A 1 103 ? -9.767  -7.161  -5.575 1.00 26.71 ? 103 ASP   B OD2 1 
ATOM   804  N  N   . ASP   A 1 104 ? -4.516  -8.825  -3.794 1.00 21.81 ? 104 ASP   B N   1 
ATOM   805  C  CA  . ASP   A 1 104 ? -3.805  -10.024 -3.352 1.00 26.66 ? 104 ASP   B CA  1 
ATOM   806  C  C   . ASP   A 1 104 ? -2.750  -9.740  -2.284 1.00 24.54 ? 104 ASP   B C   1 
ATOM   807  O  O   . ASP   A 1 104 ? -1.917  -10.610 -1.987 1.00 23.12 ? 104 ASP   B O   1 
ATOM   808  C  CB  . ASP   A 1 104 ? -3.248  -10.811 -4.535 1.00 32.90 ? 104 ASP   B CB  1 
ATOM   809  C  CG  . ASP   A 1 104 ? -2.302  -9.982  -5.362 1.00 37.79 ? 104 ASP   B CG  1 
ATOM   810  O  OD1 . ASP   A 1 104 ? -2.040  -8.826  -4.970 1.00 30.91 ? 104 ASP   B OD1 1 
ATOM   811  O  OD2 . ASP   A 1 104 ? -1.851  -10.503 -6.404 1.00 52.54 ? 104 ASP   B OD2 1 
ATOM   812  N  N   . HIS   A 1 105 ? -2.826  -8.558  -1.644 1.00 22.03 ? 105 HIS   B N   1 
ATOM   813  C  CA  . HIS   A 1 105 ? -1.907  -8.283  -0.560 1.00 19.76 ? 105 HIS   B CA  1 
ATOM   814  C  C   . HIS   A 1 105 ? -2.570  -7.289  0.400  1.00 19.68 ? 105 HIS   B C   1 
ATOM   815  O  O   . HIS   A 1 105 ? -2.227  -6.104  0.394  1.00 21.57 ? 105 HIS   B O   1 
ATOM   816  C  CB  . HIS   A 1 105 ? -0.595  -7.746  -1.160 1.00 22.51 ? 105 HIS   B CB  1 
ATOM   817  C  CG  . HIS   A 1 105 ? 0.576   -7.823  -0.238 1.00 24.12 ? 105 HIS   B CG  1 
ATOM   818  N  ND1 . HIS   A 1 105 ? 1.121   -6.712  0.410  1.00 30.66 ? 105 HIS   B ND1 1 
ATOM   819  C  CD2 . HIS   A 1 105 ? 1.322   -8.882  0.144  1.00 25.84 ? 105 HIS   B CD2 1 
ATOM   820  C  CE1 . HIS   A 1 105 ? 2.155   -7.091  1.147  1.00 30.12 ? 105 HIS   B CE1 1 
ATOM   821  N  NE2 . HIS   A 1 105 ? 2.273   -8.430  1.027  1.00 31.29 ? 105 HIS   B NE2 1 
ATOM   822  N  N   . GLY   A 1 106 ? -3.536  -7.740  1.198  1.00 16.27 ? 106 GLY   B N   1 
ATOM   823  C  CA  . GLY   A 1 106 ? -4.322  -6.804  1.997  1.00 15.83 ? 106 GLY   B CA  1 
ATOM   824  C  C   . GLY   A 1 106 ? -4.370  -7.175  3.479  1.00 16.64 ? 106 GLY   B C   1 
ATOM   825  O  O   . GLY   A 1 106 ? -4.648  -6.327  4.321  1.00 19.27 ? 106 GLY   B O   1 
ATOM   826  N  N   . SER   A 1 107 ? -4.069  -8.438  3.829  1.00 14.72 ? 107 SER   B N   1 
ATOM   827  C  CA  . SER   A 1 107 ? -4.239  -8.797  5.231  1.00 13.55 ? 107 SER   B CA  1 
ATOM   828  C  C   . SER   A 1 107 ? -3.031  -8.395  6.086  1.00 14.69 ? 107 SER   B C   1 
ATOM   829  O  O   . SER   A 1 107 ? -2.001  -8.004  5.539  1.00 17.43 ? 107 SER   B O   1 
ATOM   830  C  CB  . SER   A 1 107 ? -4.620  -10.276 5.358  1.00 12.42 ? 107 SER   B CB  1 
ATOM   831  O  OG  . SER   A 1 107 ? -3.547  -11.133 4.898  1.00 14.20 ? 107 SER   B OG  1 
ATOM   832  N  N   . GLU   A 1 108 ? -3.157  -8.498  7.426  1.00 12.97 ? 108 GLU   B N   1 
ATOM   833  C  CA  . GLU   A 1 108 ? -2.066  -8.216  8.343  1.00 13.08 ? 108 GLU   B CA  1 
ATOM   834  C  C   . GLU   A 1 108 ? -1.328  -9.517  8.652  1.00 12.91 ? 108 GLU   B C   1 
ATOM   835  O  O   . GLU   A 1 108 ? -0.129  -9.618  8.437  1.00 14.64 ? 108 GLU   B O   1 
ATOM   836  C  CB  . GLU   A 1 108 ? -2.627  -7.561  9.601  1.00 14.26 ? 108 GLU   B CB  1 
ATOM   837  C  CG  . GLU   A 1 108 ? -3.094  -6.137  9.274  1.00 17.18 ? 108 GLU   B CG  1 
ATOM   838  C  CD  . GLU   A 1 108 ? -3.003  -5.123  10.390 1.00 16.23 ? 108 GLU   B CD  1 
ATOM   839  O  OE1 . GLU   A 1 108 ? -3.450  -5.476  11.488 1.00 15.75 ? 108 GLU   B OE1 1 
ATOM   840  O  OE2 . GLU   A 1 108 ? -2.552  -3.969  10.141 1.00 15.39 ? 108 GLU   B OE2 1 
ATOM   841  N  N   . HIS   A 1 109 ? -2.051  -10.510 9.173  1.00 13.73 ? 109 HIS   B N   1 
ATOM   842  C  CA  . HIS   A 1 109 ? -1.457  -11.830 9.338  1.00 12.72 ? 109 HIS   B CA  1 
ATOM   843  C  C   . HIS   A 1 109 ? -1.315  -12.468 7.970  1.00 13.83 ? 109 HIS   B C   1 
ATOM   844  O  O   . HIS   A 1 109 ? -2.183  -12.267 7.113  1.00 13.63 ? 109 HIS   B O   1 
ATOM   845  C  CB  . HIS   A 1 109 ? -2.379  -12.700 10.238 1.00 11.46 ? 109 HIS   B CB  1 
ATOM   846  C  CG  . HIS   A 1 109 ? -2.333  -12.177 11.634 1.00 12.17 ? 109 HIS   B CG  1 
ATOM   847  N  ND1 . HIS   A 1 109 ? -3.245  -11.229 12.137 1.00 13.39 ? 109 HIS   B ND1 1 
ATOM   848  C  CD2 . HIS   A 1 109 ? -1.422  -12.379 12.609 1.00 13.13 ? 109 HIS   B CD2 1 
ATOM   849  C  CE1 . HIS   A 1 109 ? -2.887  -10.909 13.370 1.00 13.64 ? 109 HIS   B CE1 1 
ATOM   850  N  NE2 . HIS   A 1 109 ? -1.788  -11.634 13.693 1.00 13.03 ? 109 HIS   B NE2 1 
ATOM   851  N  N   . ILE   A 1 110 ? -0.259  -13.297 7.808  1.00 13.83 ? 110 ILE   B N   1 
ATOM   852  C  CA  . ILE   A 1 110 ? 0.024   -13.907 6.520  1.00 15.72 ? 110 ILE   B CA  1 
ATOM   853  C  C   . ILE   A 1 110 ? 0.157   -15.402 6.836  1.00 17.17 ? 110 ILE   B C   1 
ATOM   854  O  O   . ILE   A 1 110 ? 0.815   -15.734 7.801  1.00 18.89 ? 110 ILE   B O   1 
ATOM   855  C  CB  . ILE   A 1 110 ? 1.311   -13.288 5.940  1.00 16.54 ? 110 ILE   B CB  1 
ATOM   856  C  CG1 . ILE   A 1 110 ? 1.060   -11.791 5.659  1.00 20.96 ? 110 ILE   B CG1 1 
ATOM   857  C  CG2 . ILE   A 1 110 ? 1.785   -14.005 4.655  1.00 18.03 ? 110 ILE   B CG2 1 
ATOM   858  C  CD1 . ILE   A 1 110 ? 2.202   -11.058 5.040  1.00 26.03 ? 110 ILE   B CD1 1 
ATOM   859  N  N   . VAL   A 1 111 ? -0.505  -16.259 6.068  1.00 16.41 ? 111 VAL   B N   1 
ATOM   860  C  CA  . VAL   A 1 111 ? -0.550  -17.700 6.366  1.00 16.46 ? 111 VAL   B CA  1 
ATOM   861  C  C   . VAL   A 1 111 ? 0.169   -18.524 5.281  1.00 15.37 ? 111 VAL   B C   1 
ATOM   862  O  O   . VAL   A 1 111 ? -0.246  -18.574 4.139  1.00 15.76 ? 111 VAL   B O   1 
ATOM   863  C  CB  . VAL   A 1 111 ? -2.001  -18.184 6.505  1.00 17.38 ? 111 VAL   B CB  1 
ATOM   864  C  CG1 . VAL   A 1 111 ? -2.061  -19.660 6.919  1.00 17.90 ? 111 VAL   B CG1 1 
ATOM   865  C  CG2 . VAL   A 1 111 ? -2.663  -17.359 7.600  1.00 19.78 ? 111 VAL   B CG2 1 
ATOM   866  N  N   . ASP   A 1 112 ? 1.324   -19.094 5.653  1.00 16.55 ? 112 ASP   B N   1 
ATOM   867  C  CA  . ASP   A 1 112 ? 2.145   -19.810 4.673  1.00 18.21 ? 112 ASP   B CA  1 
ATOM   868  C  C   . ASP   A 1 112 ? 2.381   -18.955 3.429  1.00 19.26 ? 112 ASP   B C   1 
ATOM   869  O  O   . ASP   A 1 112 ? 2.321   -19.451 2.281  1.00 18.77 ? 112 ASP   B O   1 
ATOM   870  C  CB  . ASP   A 1 112 ? 1.564   -21.190 4.336  1.00 23.60 ? 112 ASP   B CB  1 
ATOM   871  C  CG  . ASP   A 1 112 ? 1.557   -22.164 5.510  1.00 24.91 ? 112 ASP   B CG  1 
ATOM   872  O  OD1 . ASP   A 1 112 ? 2.468   -22.077 6.362  1.00 25.58 ? 112 ASP   B OD1 1 
ATOM   873  O  OD2 . ASP   A 1 112 ? 0.647   -23.033 5.542  1.00 28.39 ? 112 ASP   B OD2 1 
ATOM   874  N  N   . GLY   A 1 113 ? 2.679   -17.680 3.668  1.00 16.59 ? 113 GLY   B N   1 
ATOM   875  C  CA  . GLY   A 1 113 ? 3.018   -16.752 2.601  1.00 17.00 ? 113 GLY   B CA  1 
ATOM   876  C  C   . GLY   A 1 113 ? 1.809   -16.153 1.891  1.00 19.69 ? 113 GLY   B C   1 
ATOM   877  O  O   . GLY   A 1 113 ? 2.001   -15.329 0.996  1.00 19.27 ? 113 GLY   B O   1 
ATOM   878  N  N   . VAL   A 1 114 ? 0.590   -16.579 2.265  1.00 18.61 ? 114 VAL   B N   1 
ATOM   879  C  CA  . VAL   A 1 114 ? -0.605  -16.057 1.616  1.00 16.84 ? 114 VAL   B CA  1 
ATOM   880  C  C   . VAL   A 1 114 ? -1.091  -14.835 2.386  1.00 18.00 ? 114 VAL   B C   1 
ATOM   881  O  O   . VAL   A 1 114 ? -1.364  -14.890 3.587  1.00 17.82 ? 114 VAL   B O   1 
ATOM   882  C  CB  . VAL   A 1 114 ? -1.733  -17.098 1.520  1.00 17.89 ? 114 VAL   B CB  1 
ATOM   883  C  CG1 . VAL   A 1 114 ? -3.011  -16.441 0.954  1.00 16.68 ? 114 VAL   B CG1 1 
ATOM   884  C  CG2 . VAL   A 1 114 ? -1.332  -18.323 0.707  1.00 20.83 ? 114 VAL   B CG2 1 
ATOM   885  N  N   . SER   A 1 115 ? -1.163  -13.713 1.667  1.00 18.09 ? 115 SER   B N   1 
ATOM   886  C  CA  . SER   A 1 115 ? -1.816  -12.535 2.194  1.00 19.06 ? 115 SER   B CA  1 
ATOM   887  C  C   . SER   A 1 115 ? -3.214  -12.529 1.589  1.00 18.35 ? 115 SER   B C   1 
ATOM   888  O  O   . SER   A 1 115 ? -3.361  -12.616 0.378  1.00 19.95 ? 115 SER   B O   1 
ATOM   889  C  CB  . SER   A 1 115 ? -0.989  -11.319 1.818  1.00 22.82 ? 115 SER   B CB  1 
ATOM   890  O  OG  . SER   A 1 115 ? -1.566  -10.112 2.343  1.00 31.91 ? 115 SER   B OG  1 
ATOM   891  N  N   . TYR   A 1 116 ? -4.262  -12.397 2.430  1.00 16.06 ? 116 TYR   B N   1 
ATOM   892  C  CA  . TYR   A 1 116 ? -5.630  -12.380 1.944  1.00 15.94 ? 116 TYR   B CA  1 
ATOM   893  C  C   . TYR   A 1 116 ? -6.003  -10.982 1.466  1.00 15.36 ? 116 TYR   B C   1 
ATOM   894  O  O   . TYR   A 1 116 ? -5.200  -10.055 1.556  1.00 14.85 ? 116 TYR   B O   1 
ATOM   895  C  CB  . TYR   A 1 116 ? -6.552  -12.913 3.043  1.00 15.10 ? 116 TYR   B CB  1 
ATOM   896  C  CG  . TYR   A 1 116 ? -6.354  -14.394 3.309  1.00 15.07 ? 116 TYR   B CG  1 
ATOM   897  C  CD1 . TYR   A 1 116 ? -5.393  -14.839 4.206  1.00 19.04 ? 116 TYR   B CD1 1 
ATOM   898  C  CD2 . TYR   A 1 116 ? -7.136  -15.331 2.647  1.00 19.16 ? 116 TYR   B CD2 1 
ATOM   899  C  CE1 . TYR   A 1 116 ? -5.246  -16.198 4.468  1.00 19.14 ? 116 TYR   B CE1 1 
ATOM   900  C  CE2 . TYR   A 1 116 ? -6.962  -16.693 2.857  1.00 20.08 ? 116 TYR   B CE2 1 
ATOM   901  C  CZ  . TYR   A 1 116 ? -6.016  -17.113 3.780  1.00 22.17 ? 116 TYR   B CZ  1 
ATOM   902  O  OH  . TYR   A 1 116 ? -5.789  -18.447 4.029  1.00 31.98 ? 116 TYR   B OH  1 
ATOM   903  N  N   . ALA   A 1 117 ? -7.225  -10.849 0.909  1.00 14.63 ? 117 ALA   B N   1 
ATOM   904  C  CA  . ALA   A 1 117 ? -7.588  -9.528  0.402  1.00 13.18 ? 117 ALA   B CA  1 
ATOM   905  C  C   . ALA   A 1 117 ? -7.805  -8.504  1.517  1.00 13.84 ? 117 ALA   B C   1 
ATOM   906  O  O   . ALA   A 1 117 ? -7.577  -7.317  1.321  1.00 12.97 ? 117 ALA   B O   1 
ATOM   907  C  CB  . ALA   A 1 117 ? -8.797  -9.628  -0.515 1.00 14.02 ? 117 ALA   B CB  1 
ATOM   908  N  N   . ALA   A 1 118 ? -8.273  -8.955  2.686  1.00 12.70 ? 118 ALA   B N   1 
ATOM   909  C  CA  . ALA   A 1 118 ? -8.549  -8.031  3.778  1.00 10.34 ? 118 ALA   B CA  1 
ATOM   910  C  C   . ALA   A 1 118 ? -8.559  -8.858  5.047  1.00 10.86 ? 118 ALA   B C   1 
ATOM   911  O  O   . ALA   A 1 118 ? -8.518  -10.087 4.989  1.00 10.18 ? 118 ALA   B O   1 
ATOM   912  C  CB  . ALA   A 1 118 ? -9.872  -7.290  3.547  1.00 12.07 ? 118 ALA   B CB  1 
ATOM   913  N  N   . GLU   A 1 119 ? -8.611  -8.183  6.189  1.00 10.19 ? 119 GLU   B N   1 
ATOM   914  C  CA  . GLU   A 1 119 ? -8.692  -8.891  7.482  1.00 10.19 ? 119 GLU   B CA  1 
ATOM   915  C  C   . GLU   A 1 119 ? -9.575  -8.039  8.401  1.00 10.29 ? 119 GLU   B C   1 
ATOM   916  O  O   . GLU   A 1 119 ? -9.298  -6.853  8.649  1.00 12.19 ? 119 GLU   B O   1 
ATOM   917  C  CB  . GLU   A 1 119 ? -7.255  -9.025  8.022  1.00 11.18 ? 119 GLU   B CB  1 
ATOM   918  C  CG  . GLU   A 1 119 ? -7.157  -9.832  9.330  1.00 10.93 ? 119 GLU   B CG  1 
ATOM   919  C  CD  . GLU   A 1 119 ? -5.730  -10.170 9.762  1.00 14.30 ? 119 GLU   B CD  1 
ATOM   920  O  OE1 . GLU   A 1 119 ? -4.890  -10.349 8.889  1.00 14.45 ? 119 GLU   B OE1 1 
ATOM   921  O  OE2 . GLU   A 1 119 ? -5.469  -10.241 10.978 1.00 15.59 ? 119 GLU   B OE2 1 
ATOM   922  N  N   . LEU   A 1 120 ? -10.580 -8.703  8.998  1.00 10.79 ? 120 LEU   B N   1 
ATOM   923  C  CA  . LEU   A 1 120 ? -11.521 -8.065  9.916  1.00 11.65 ? 120 LEU   B CA  1 
ATOM   924  C  C   . LEU   A 1 120 ? -10.974 -8.344  11.322 1.00 12.16 ? 120 LEU   B C   1 
ATOM   925  O  O   . LEU   A 1 120 ? -10.569 -9.478  11.641 1.00 12.81 ? 120 LEU   B O   1 
ATOM   926  C  CB  . LEU   A 1 120 ? -12.872 -8.771  9.714  1.00 14.04 ? 120 LEU   B CB  1 
ATOM   927  C  CG  . LEU   A 1 120 ? -14.022 -8.122  10.482 1.00 16.22 ? 120 LEU   B CG  1 
ATOM   928  C  CD1 . LEU   A 1 120 ? -14.533 -6.843  9.774  1.00 15.58 ? 120 LEU   B CD1 1 
ATOM   929  C  CD2 . LEU   A 1 120 ? -15.168 -9.162  10.683 1.00 19.72 ? 120 LEU   B CD2 1 
ATOM   930  N  N   . HIS   A 1 121 ? -11.000 -7.317  12.153 1.00 9.98  ? 121 HIS   B N   1 
ATOM   931  C  CA  . HIS   A 1 121 ? -10.591 -7.489  13.549 1.00 10.70 ? 121 HIS   B CA  1 
ATOM   932  C  C   . HIS   A 1 121 ? -11.768 -7.159  14.455 1.00 11.31 ? 121 HIS   B C   1 
ATOM   933  O  O   . HIS   A 1 121 ? -12.413 -6.080  14.288 1.00 12.69 ? 121 HIS   B O   1 
ATOM   934  C  CB  . HIS   A 1 121 ? -9.466  -6.510  13.859 1.00 10.96 ? 121 HIS   B CB  1 
ATOM   935  C  CG  . HIS   A 1 121 ? -8.171  -6.956  13.279 1.00 10.22 ? 121 HIS   B CG  1 
ATOM   936  N  ND1 . HIS   A 1 121 ? -7.041  -6.081  13.201 1.00 10.74 ? 121 HIS   B ND1 1 
ATOM   937  C  CD2 . HIS   A 1 121 ? -7.836  -8.167  12.782 1.00 11.04 ? 121 HIS   B CD2 1 
ATOM   938  C  CE1 . HIS   A 1 121 ? -6.091  -6.797  12.588 1.00 11.20 ? 121 HIS   B CE1 1 
ATOM   939  N  NE2 . HIS   A 1 121 ? -6.528  -8.076  12.412 1.00 11.71 ? 121 HIS   B NE2 1 
ATOM   940  N  N   . VAL   A 1 122 ? -12.048 -8.084  15.421 1.00 10.56 ? 122 VAL   B N   1 
ATOM   941  C  CA  . VAL   A 1 122 ? -13.130 -7.920  16.379 1.00 10.50 ? 122 VAL   B CA  1 
ATOM   942  C  C   . VAL   A 1 122 ? -12.483 -7.760  17.751 1.00 11.56 ? 122 VAL   B C   1 
ATOM   943  O  O   . VAL   A 1 122 ? -11.815 -8.690  18.224 1.00 10.03 ? 122 VAL   B O   1 
ATOM   944  C  CB  . VAL   A 1 122 ? -14.104 -9.137  16.343 1.00 10.54 ? 122 VAL   B CB  1 
ATOM   945  C  CG1 . VAL   A 1 122 ? -15.313 -8.786  17.193 1.00 13.23 ? 122 VAL   B CG1 1 
ATOM   946  C  CG2 . VAL   A 1 122 ? -14.538 -9.479  14.919 1.00 12.79 ? 122 VAL   B CG2 1 
ATOM   947  N  N   . VAL   A 1 123 ? -12.619 -6.567  18.372 1.00 10.57 ? 123 VAL   B N   1 
ATOM   948  C  CA  . VAL   A 1 123 ? -11.810 -6.209  19.547 1.00 10.24 ? 123 VAL   B CA  1 
ATOM   949  C  C   . VAL   A 1 123 ? -12.648 -6.348  20.813 1.00 11.47 ? 123 VAL   B C   1 
ATOM   950  O  O   . VAL   A 1 123 ? -13.785 -5.870  20.865 1.00 11.23 ? 123 VAL   B O   1 
ATOM   951  C  CB  . VAL   A 1 123 ? -11.331 -4.747  19.432 1.00 11.24 ? 123 VAL   B CB  1 
ATOM   952  C  CG1 . VAL   A 1 123 ? -10.504 -4.303  20.652 1.00 13.17 ? 123 VAL   B CG1 1 
ATOM   953  C  CG2 . VAL   A 1 123 ? -10.524 -4.565  18.160 1.00 12.01 ? 123 VAL   B CG2 1 
ATOM   954  N  N   . HIS   A 1 124 ? -12.069 -7.028  21.817 1.00 10.90 ? 124 HIS   B N   1 
ATOM   955  C  CA  . HIS   A 1 124 ? -12.795 -7.301  23.068 1.00 11.95 ? 124 HIS   B CA  1 
ATOM   956  C  C   . HIS   A 1 124 ? -11.877 -7.044  24.252 1.00 13.24 ? 124 HIS   B C   1 
ATOM   957  O  O   . HIS   A 1 124 ? -10.639 -7.073  24.138 1.00 13.13 ? 124 HIS   B O   1 
ATOM   958  C  CB  . HIS   A 1 124 ? -13.181 -8.802  23.206 1.00 11.50 ? 124 HIS   B CB  1 
ATOM   959  C  CG  . HIS   A 1 124 ? -13.812 -9.473  22.030 1.00 11.99 ? 124 HIS   B CG  1 
ATOM   960  N  ND1 . HIS   A 1 124 ? -13.094 -9.773  20.875 1.00 12.32 ? 124 HIS   B ND1 1 
ATOM   961  C  CD2 . HIS   A 1 124 ? -15.052 -9.984  21.854 1.00 11.65 ? 124 HIS   B CD2 1 
ATOM   962  C  CE1 . HIS   A 1 124 ? -13.900 -10.380 20.021 1.00 11.62 ? 124 HIS   B CE1 1 
ATOM   963  N  NE2 . HIS   A 1 124 ? -15.122 -10.478 20.579 1.00 12.47 ? 124 HIS   B NE2 1 
ATOM   964  N  N   . TRP   A 1 125 ? -12.474 -6.784  25.434 1.00 14.01 ? 125 TRP   B N   1 
ATOM   965  C  CA  . TRP   A 1 125 ? -11.647 -6.432  26.595 1.00 12.59 ? 125 TRP   B CA  1 
ATOM   966  C  C   . TRP   A 1 125 ? -12.081 -7.242  27.818 1.00 12.42 ? 125 TRP   B C   1 
ATOM   967  O  O   . TRP   A 1 125 ? -13.232 -7.638  27.917 1.00 11.60 ? 125 TRP   B O   1 
ATOM   968  C  CB  . TRP   A 1 125 ? -11.638 -4.924  26.888 1.00 12.87 ? 125 TRP   B CB  1 
ATOM   969  C  CG  . TRP   A 1 125 ? -12.994 -4.337  27.181 1.00 13.56 ? 125 TRP   B CG  1 
ATOM   970  C  CD1 . TRP   A 1 125 ? -13.858 -3.831  26.256 1.00 12.88 ? 125 TRP   B CD1 1 
ATOM   971  C  CD2 . TRP   A 1 125 ? -13.562 -3.993  28.469 1.00 12.93 ? 125 TRP   B CD2 1 
ATOM   972  N  NE1 . TRP   A 1 125 ? -14.965 -3.278  26.861 1.00 15.09 ? 125 TRP   B NE1 1 
ATOM   973  C  CE2 . TRP   A 1 125 ? -14.783 -3.319  28.218 1.00 14.08 ? 125 TRP   B CE2 1 
ATOM   974  C  CE3 . TRP   A 1 125 ? -13.166 -4.172  29.803 1.00 14.69 ? 125 TRP   B CE3 1 
ATOM   975  C  CZ2 . TRP   A 1 125 ? -15.623 -2.848  29.245 1.00 15.58 ? 125 TRP   B CZ2 1 
ATOM   976  C  CZ3 . TRP   A 1 125 ? -13.976 -3.656  30.810 1.00 15.25 ? 125 TRP   B CZ3 1 
ATOM   977  C  CH2 . TRP   A 1 125 ? -15.189 -3.026  30.544 1.00 15.34 ? 125 TRP   B CH2 1 
ATOM   978  N  N   . ASN   A 1 126 ? -11.133 -7.510  28.720 1.00 12.43 ? 126 ASN   B N   1 
ATOM   979  C  CA  . ASN   A 1 126 ? -11.385 -8.437  29.819 1.00 11.68 ? 126 ASN   B CA  1 
ATOM   980  C  C   . ASN   A 1 126 ? -12.121 -7.707  30.971 1.00 13.06 ? 126 ASN   B C   1 
ATOM   981  O  O   . ASN   A 1 126 ? -11.497 -7.148  31.908 1.00 14.83 ? 126 ASN   B O   1 
ATOM   982  C  CB  . ASN   A 1 126 ? -10.005 -8.916  30.304 1.00 13.89 ? 126 ASN   B CB  1 
ATOM   983  C  CG  . ASN   A 1 126 ? -10.082 -10.013 31.345 1.00 15.95 ? 126 ASN   B CG  1 
ATOM   984  O  OD1 . ASN   A 1 126 ? -11.130 -10.228 31.946 1.00 16.14 ? 126 ASN   B OD1 1 
ATOM   985  N  ND2 . ASN   A 1 126 ? -8.959  -10.637 31.609 1.00 17.30 ? 126 ASN   B ND2 1 
ATOM   986  N  N   . SER   A 1 127 ? -13.454 -7.760  30.939 1.00 14.51 ? 127 SER   B N   1 
ATOM   987  C  CA  . SER   A 1 127 ? -14.268 -7.066  31.939 1.00 15.71 ? 127 SER   B CA  1 
ATOM   988  C  C   . SER   A 1 127 ? -14.330 -7.852  33.251 1.00 15.92 ? 127 SER   B C   1 
ATOM   989  O  O   . SER   A 1 127 ? -14.766 -7.325  34.276 1.00 16.19 ? 127 SER   B O   1 
ATOM   990  C  CB  . SER   A 1 127 ? -15.648 -6.780  31.383 1.00 15.04 ? 127 SER   B CB  1 
ATOM   991  O  OG  . SER   A 1 127 ? -16.328 -8.006  31.113 1.00 16.50 ? 127 SER   B OG  1 
ATOM   992  N  N   . ASP   A 1 128 ? -13.910 -9.113  33.246 1.00 16.57 ? 128 ASP   B N   1 
ATOM   993  C  CA  . ASP   A 1 128 ? -13.843 -9.887  34.483 1.00 18.90 ? 128 ASP   B CA  1 
ATOM   994  C  C   . ASP   A 1 128 ? -12.734 -9.376  35.402 1.00 19.82 ? 128 ASP   B C   1 
ATOM   995  O  O   . ASP   A 1 128 ? -12.806 -9.636  36.611 1.00 23.24 ? 128 ASP   B O   1 
ATOM   996  C  CB  . ASP   A 1 128 ? -13.659 -11.383 34.213 1.00 19.38 ? 128 ASP   B CB  1 
ATOM   997  C  CG  . ASP   A 1 128 ? -14.919 -12.151 33.818 1.00 24.80 ? 128 ASP   B CG  1 
ATOM   998  O  OD1 . ASP   A 1 128 ? -16.046 -11.553 33.779 1.00 28.25 ? 128 ASP   B OD1 1 
ATOM   999  O  OD2 . ASP   A 1 128 ? -14.776 -13.348 33.466 1.00 23.75 ? 128 ASP   B OD2 1 
ATOM   1000 N  N   . LYS   A 1 129 ? -11.691 -8.721  34.855 1.00 17.53 ? 129 LYS   B N   1 
ATOM   1001 C  CA  . LYS   A 1 129 ? -10.526 -8.297  35.605 1.00 17.03 ? 129 LYS   B CA  1 
ATOM   1002 C  C   . LYS   A 1 129 ? -10.287 -6.789  35.611 1.00 16.91 ? 129 LYS   B C   1 
ATOM   1003 O  O   . LYS   A 1 129 ? -9.612  -6.284  36.522 1.00 17.38 ? 129 LYS   B O   1 
ATOM   1004 C  CB  . LYS   A 1 129 ? -9.227  -8.939  35.098 1.00 20.11 ? 129 LYS   B CB  1 
ATOM   1005 C  CG  . LYS   A 1 129 ? -8.978  -10.385 35.509 1.00 24.04 ? 129 LYS   B CG  1 
ATOM   1006 C  CD  . LYS   A 1 129 ? -7.560  -10.901 35.201 1.00 25.52 ? 129 LYS   B CD  1 
ATOM   1007 C  CE  . LYS   A 1 129 ? -6.436  -10.093 35.820 1.00 30.58 ? 129 LYS   B CE  1 
ATOM   1008 N  NZ  . LYS   A 1 129 ? -5.117  -10.780 35.687 1.00 33.81 ? 129 LYS   B NZ  1 
ATOM   1009 N  N   . TYR   A 1 130 ? -10.790 -6.064  34.598 1.00 14.47 ? 130 TYR   B N   1 
ATOM   1010 C  CA  . TYR   A 1 130 ? -10.515 -4.631  34.433 1.00 14.64 ? 130 TYR   B CA  1 
ATOM   1011 C  C   . TYR   A 1 130 ? -11.824 -3.867  34.311 1.00 15.65 ? 130 TYR   B C   1 
ATOM   1012 O  O   . TYR   A 1 130 ? -12.834 -4.400  33.864 1.00 15.56 ? 130 TYR   B O   1 
ATOM   1013 C  CB  . TYR   A 1 130 ? -9.625  -4.386  33.195 1.00 15.91 ? 130 TYR   B CB  1 
ATOM   1014 C  CG  . TYR   A 1 130 ? -8.351  -5.180  33.327 1.00 16.55 ? 130 TYR   B CG  1 
ATOM   1015 C  CD1 . TYR   A 1 130 ? -7.418  -4.859  34.320 1.00 19.06 ? 130 TYR   B CD1 1 
ATOM   1016 C  CD2 . TYR   A 1 130 ? -8.103  -6.299  32.538 1.00 13.80 ? 130 TYR   B CD2 1 
ATOM   1017 C  CE1 . TYR   A 1 130 ? -6.305  -5.654  34.515 1.00 21.38 ? 130 TYR   B CE1 1 
ATOM   1018 C  CE2 . TYR   A 1 130 ? -6.965  -7.089  32.693 1.00 16.22 ? 130 TYR   B CE2 1 
ATOM   1019 C  CZ  . TYR   A 1 130 ? -6.070  -6.769  33.708 1.00 21.79 ? 130 TYR   B CZ  1 
ATOM   1020 O  OH  . TYR   A 1 130 ? -4.958  -7.554  33.923 1.00 22.53 ? 130 TYR   B OH  1 
ATOM   1021 N  N   . PRO   A 1 131 ? -11.879 -2.606  34.790 1.00 15.66 ? 131 PRO   B N   1 
ATOM   1022 C  CA  . PRO   A 1 131 ? -13.150 -1.879  34.827 1.00 16.75 ? 131 PRO   B CA  1 
ATOM   1023 C  C   . PRO   A 1 131 ? -13.539 -1.179  33.527 1.00 16.60 ? 131 PRO   B C   1 
ATOM   1024 O  O   . PRO   A 1 131 ? -14.665 -0.677  33.387 1.00 17.49 ? 131 PRO   B O   1 
ATOM   1025 C  CB  . PRO   A 1 131 ? -12.893 -0.793  35.878 1.00 18.79 ? 131 PRO   B CB  1 
ATOM   1026 C  CG  . PRO   A 1 131 ? -11.404 -0.530  35.775 1.00 18.07 ? 131 PRO   B CG  1 
ATOM   1027 C  CD  . PRO   A 1 131 ? -10.799 -1.893  35.487 1.00 16.34 ? 131 PRO   B CD  1 
ATOM   1028 N  N   . SER   A 1 132 ? -12.590 -1.070  32.606 1.00 16.31 ? 132 SER   B N   1 
ATOM   1029 C  CA  . SER   A 1 132 ? -12.901 -0.427  31.328 1.00 16.24 ? 132 SER   B CA  1 
ATOM   1030 C  C   . SER   A 1 132 ? -11.913 -0.897  30.257 1.00 16.26 ? 132 SER   B C   1 
ATOM   1031 O  O   . SER   A 1 132 ? -10.851 -1.434  30.557 1.00 16.35 ? 132 SER   B O   1 
ATOM   1032 C  CB  . SER   A 1 132 ? -12.812 1.073   31.437 1.00 16.68 ? 132 SER   B CB  1 
ATOM   1033 O  OG  . SER   A 1 132 ? -11.454 1.433   31.740 1.00 18.10 ? 132 SER   B OG  1 
ATOM   1034 N  N   . PHE   A 1 133 ? -12.297 -0.673  28.991 1.00 17.85 ? 133 PHE   B N   1 
ATOM   1035 C  CA  . PHE   A 1 133 ? -11.425 -0.895  27.844 1.00 18.36 ? 133 PHE   B CA  1 
ATOM   1036 C  C   . PHE   A 1 133 ? -10.081 -0.171  28.001 1.00 18.02 ? 133 PHE   B C   1 
ATOM   1037 O  O   . PHE   A 1 133 ? -9.021  -0.769  27.785 1.00 16.86 ? 133 PHE   B O   1 
ATOM   1038 C  CB  . PHE   A 1 133 ? -12.169 -0.488  26.560 1.00 17.31 ? 133 PHE   B CB  1 
ATOM   1039 C  CG  . PHE   A 1 133 ? -11.271 -0.508  25.360 1.00 20.72 ? 133 PHE   B CG  1 
ATOM   1040 C  CD1 . PHE   A 1 133 ? -10.920 -1.704  24.758 1.00 20.52 ? 133 PHE   B CD1 1 
ATOM   1041 C  CD2 . PHE   A 1 133 ? -10.652 0.659   24.929 1.00 27.15 ? 133 PHE   B CD2 1 
ATOM   1042 C  CE1 . PHE   A 1 133 ? -10.055 -1.724  23.671 1.00 23.37 ? 133 PHE   B CE1 1 
ATOM   1043 C  CE2 . PHE   A 1 133 ? -9.724  0.634   23.897 1.00 27.91 ? 133 PHE   B CE2 1 
ATOM   1044 C  CZ  . PHE   A 1 133 ? -9.437  -0.553  23.263 1.00 26.04 ? 133 PHE   B CZ  1 
ATOM   1045 N  N   . VAL   A 1 134 ? -10.114 1.090   28.453 1.00 20.93 ? 134 VAL   B N   1 
ATOM   1046 C  CA  . VAL   A 1 134 ? -8.864  1.828   28.494 1.00 24.95 ? 134 VAL   B CA  1 
ATOM   1047 C  C   . VAL   A 1 134 ? -7.913  1.194   29.503 1.00 22.81 ? 134 VAL   B C   1 
ATOM   1048 O  O   . VAL   A 1 134 ? -6.730  1.017   29.218 1.00 20.41 ? 134 VAL   B O   1 
ATOM   1049 C  CB  . VAL   A 1 134 ? -9.109  3.334   28.691 1.00 27.39 ? 134 VAL   B CB  1 
ATOM   1050 C  CG1 . VAL   A 1 134 ? -7.796  4.097   28.688 1.00 36.27 ? 134 VAL   B CG1 1 
ATOM   1051 C  CG2 . VAL   A 1 134 ? -10.019 3.855   27.589 1.00 30.24 ? 134 VAL   B CG2 1 
ATOM   1052 N  N   . GLU   A 1 135 ? -8.430  0.797   30.685 1.00 19.98 ? 135 GLU   B N   1 
ATOM   1053 C  CA  . GLU   A 1 135 ? -7.520  0.194   31.646 1.00 18.38 ? 135 GLU   B CA  1 
ATOM   1054 C  C   . GLU   A 1 135 ? -7.009  -1.156  31.131 1.00 18.88 ? 135 GLU   B C   1 
ATOM   1055 O  O   . GLU   A 1 135 ? -5.819  -1.458  31.276 1.00 19.59 ? 135 GLU   B O   1 
ATOM   1056 C  CB  . GLU   A 1 135 ? -8.165  0.043   33.035 1.00 24.60 ? 135 GLU   B CB  1 
ATOM   1057 C  CG  . GLU   A 1 135 ? -8.572  1.365   33.646 1.00 27.94 ? 135 GLU   B CG  1 
ATOM   1058 C  CD  . GLU   A 1 135 ? -7.408  2.204   34.151 1.00 33.19 ? 135 GLU   B CD  1 
ATOM   1059 O  OE1 . GLU   A 1 135 ? -7.660  3.329   34.652 1.00 40.05 ? 135 GLU   B OE1 1 
ATOM   1060 O  OE2 . GLU   A 1 135 ? -6.268  1.689   34.144 1.00 33.09 ? 135 GLU   B OE2 1 
ATOM   1061 N  N   . ALA   A 1 136 ? -7.887  -1.955  30.499 1.00 15.93 ? 136 ALA   B N   1 
ATOM   1062 C  CA  . ALA   A 1 136 ? -7.508  -3.277  30.022 1.00 14.93 ? 136 ALA   B CA  1 
ATOM   1063 C  C   . ALA   A 1 136 ? -6.439  -3.178  28.931 1.00 17.38 ? 136 ALA   B C   1 
ATOM   1064 O  O   . ALA   A 1 136 ? -5.590  -4.070  28.804 1.00 18.18 ? 136 ALA   B O   1 
ATOM   1065 C  CB  . ALA   A 1 136 ? -8.721  -3.991  29.447 1.00 13.88 ? 136 ALA   B CB  1 
ATOM   1066 N  N   . ALA   A 1 137 ? -6.492  -2.100  28.169 1.00 17.72 ? 137 ALA   B N   1 
ATOM   1067 C  CA  . ALA   A 1 137 ? -5.606  -1.971  26.995 1.00 17.98 ? 137 ALA   B CA  1 
ATOM   1068 C  C   . ALA   A 1 137 ? -4.155  -1.909  27.450 1.00 19.44 ? 137 ALA   B C   1 
ATOM   1069 O  O   . ALA   A 1 137 ? -3.278  -2.177  26.646 1.00 20.84 ? 137 ALA   B O   1 
ATOM   1070 C  CB  . ALA   A 1 137 ? -5.919  -0.759  26.171 1.00 19.69 ? 137 ALA   B CB  1 
ATOM   1071 N  N   . HIS   A 1 138 ? -3.916  -1.631  28.747 1.00 21.67 ? 138 HIS   B N   1 
ATOM   1072 C  CA  . HIS   A 1 138 ? -2.566  -1.533  29.308 1.00 22.23 ? 138 HIS   B CA  1 
ATOM   1073 C  C   . HIS   A 1 138 ? -2.104  -2.736  30.130 1.00 25.10 ? 138 HIS   B C   1 
ATOM   1074 O  O   . HIS   A 1 138 ? -1.127  -2.636  30.881 1.00 24.60 ? 138 HIS   B O   1 
ATOM   1075 C  CB  . HIS   A 1 138 ? -2.420  -0.256  30.151 1.00 24.16 ? 138 HIS   B CB  1 
ATOM   1076 C  CG  . HIS   A 1 138 ? -2.518  0.967   29.325 1.00 23.29 ? 138 HIS   B CG  1 
ATOM   1077 N  ND1 . HIS   A 1 138 ? -1.378  1.639   28.874 1.00 29.58 ? 138 HIS   B ND1 1 
ATOM   1078 C  CD2 . HIS   A 1 138 ? -3.591  1.610   28.798 1.00 27.58 ? 138 HIS   B CD2 1 
ATOM   1079 C  CE1 . HIS   A 1 138 ? -1.753  2.692   28.163 1.00 27.66 ? 138 HIS   B CE1 1 
ATOM   1080 N  NE2 . HIS   A 1 138 ? -3.108  2.686   28.087 1.00 31.19 ? 138 HIS   B NE2 1 
ATOM   1081 N  N   . GLU   A 1 139 ? -2.741  -3.893  29.987 1.00 18.99 ? 139 GLU   B N   1 
ATOM   1082 C  CA  . GLU   A 1 139 ? -2.346  -5.073  30.736 1.00 23.83 ? 139 GLU   B CA  1 
ATOM   1083 C  C   . GLU   A 1 139 ? -2.148  -6.227  29.775 1.00 21.58 ? 139 GLU   B C   1 
ATOM   1084 O  O   . GLU   A 1 139 ? -2.937  -6.354  28.830 1.00 18.55 ? 139 GLU   B O   1 
ATOM   1085 C  CB  . GLU   A 1 139 ? -3.473  -5.562  31.663 1.00 28.27 ? 139 GLU   B CB  1 
ATOM   1086 C  CG  . GLU   A 1 139 ? -3.916  -4.519  32.672 1.00 31.81 ? 139 GLU   B CG  1 
ATOM   1087 C  CD  . GLU   A 1 139 ? -2.855  -4.255  33.713 1.00 35.60 ? 139 GLU   B CD  1 
ATOM   1088 O  OE1 . GLU   A 1 139 ? -1.850  -4.995  33.728 1.00 40.09 ? 139 GLU   B OE1 1 
ATOM   1089 O  OE2 . GLU   A 1 139 ? -3.054  -3.311  34.517 1.00 45.44 ? 139 GLU   B OE2 1 
ATOM   1090 N  N   . PRO   A 1 140 ? -1.199  -7.157  30.033 1.00 20.71 ? 140 PRO   B N   1 
ATOM   1091 C  CA  . PRO   A 1 140 ? -0.936  -8.270  29.120 1.00 21.80 ? 140 PRO   B CA  1 
ATOM   1092 C  C   . PRO   A 1 140 ? -2.133  -9.146  28.798 1.00 20.75 ? 140 PRO   B C   1 
ATOM   1093 O  O   . PRO   A 1 140 ? -2.220  -9.665  27.672 1.00 19.20 ? 140 PRO   B O   1 
ATOM   1094 C  CB  . PRO   A 1 140 ? 0.101   -9.174  29.807 1.00 23.14 ? 140 PRO   B CB  1 
ATOM   1095 C  CG  . PRO   A 1 140 ? 0.762   -8.218  30.806 1.00 26.62 ? 140 PRO   B CG  1 
ATOM   1096 C  CD  . PRO   A 1 140 ? -0.256  -7.159  31.185 1.00 24.01 ? 140 PRO   B CD  1 
ATOM   1097 N  N   . ASP   A 1 141 ? -3.057  -9.281  29.755 1.00 16.90 ? 141 ASP   B N   1 
ATOM   1098 C  CA  . ASP   A 1 141 ? -4.238  -10.087 29.473 1.00 16.86 ? 141 ASP   B CA  1 
ATOM   1099 C  C   . ASP   A 1 141 ? -5.483  -9.219  29.298 1.00 17.30 ? 141 ASP   B C   1 
ATOM   1100 O  O   . ASP   A 1 141 ? -6.601  -9.697  29.535 1.00 16.64 ? 141 ASP   B O   1 
ATOM   1101 C  CB  . ASP   A 1 141 ? -4.450  -11.119 30.587 1.00 19.71 ? 141 ASP   B CB  1 
ATOM   1102 C  CG  . ASP   A 1 141 ? -4.667  -10.466 31.937 1.00 20.96 ? 141 ASP   B CG  1 
ATOM   1103 O  OD1 . ASP   A 1 141 ? -4.476  -9.202  32.056 1.00 20.57 ? 141 ASP   B OD1 1 
ATOM   1104 O  OD2 . ASP   A 1 141 ? -5.049  -11.214 32.897 1.00 25.43 ? 141 ASP   B OD2 1 
ATOM   1105 N  N   . GLY   A 1 142 ? -5.318  -7.960  28.868 1.00 14.61 ? 142 GLY   B N   1 
ATOM   1106 C  CA  . GLY   A 1 142 ? -6.469  -7.073  28.867 1.00 15.11 ? 142 GLY   B CA  1 
ATOM   1107 C  C   . GLY   A 1 142 ? -7.369  -7.219  27.644 1.00 13.54 ? 142 GLY   B C   1 
ATOM   1108 O  O   . GLY   A 1 142 ? -8.581  -7.029  27.764 1.00 12.26 ? 142 GLY   B O   1 
ATOM   1109 N  N   . LEU   A 1 143 ? -6.787  -7.532  26.468 1.00 12.74 ? 143 LEU   B N   1 
ATOM   1110 C  CA  . LEU   A 1 143 ? -7.557  -7.530  25.234 1.00 12.13 ? 143 LEU   B CA  1 
ATOM   1111 C  C   . LEU   A 1 143 ? -7.490  -8.895  24.533 1.00 10.67 ? 143 LEU   B C   1 
ATOM   1112 O  O   . LEU   A 1 143 ? -6.523  -9.684  24.643 1.00 12.73 ? 143 LEU   B O   1 
ATOM   1113 C  CB  . LEU   A 1 143 ? -7.022  -6.443  24.276 1.00 11.69 ? 143 LEU   B CB  1 
ATOM   1114 C  CG  . LEU   A 1 143 ? -6.925  -5.015  24.828 1.00 12.59 ? 143 LEU   B CG  1 
ATOM   1115 C  CD1 . LEU   A 1 143 ? -6.454  -4.080  23.688 1.00 13.95 ? 143 LEU   B CD1 1 
ATOM   1116 C  CD2 . LEU   A 1 143 ? -8.281  -4.561  25.369 1.00 14.85 ? 143 LEU   B CD2 1 
ATOM   1117 N  N   . ALA   A 1 144 ? -8.572  -9.155  23.776 1.00 10.84 ? 144 ALA   B N   1 
ATOM   1118 C  CA  . ALA   A 1 144 ? -8.593  -10.294 22.862 1.00 10.63 ? 144 ALA   B CA  1 
ATOM   1119 C  C   . ALA   A 1 144 ? -9.124  -9.783  21.512 1.00 12.57 ? 144 ALA   B C   1 
ATOM   1120 O  O   . ALA   A 1 144 ? -10.221 -9.209  21.438 1.00 12.83 ? 144 ALA   B O   1 
ATOM   1121 C  CB  . ALA   A 1 144 ? -9.461  -11.413 23.437 1.00 12.54 ? 144 ALA   B CB  1 
ATOM   1122 N  N   . VAL   A 1 145 ? -8.407  -10.129 20.442 1.00 11.94 ? 145 VAL   B N   1 
ATOM   1123 C  CA  . VAL   A 1 145 ? -8.851  -9.698  19.115 1.00 11.94 ? 145 VAL   B CA  1 
ATOM   1124 C  C   . VAL   A 1 145 ? -9.023  -10.947 18.247 1.00 12.79 ? 145 VAL   B C   1 
ATOM   1125 O  O   . VAL   A 1 145 ? -8.094  -11.743 18.131 1.00 13.14 ? 145 VAL   B O   1 
ATOM   1126 C  CB  . VAL   A 1 145 ? -7.901  -8.682  18.477 1.00 12.85 ? 145 VAL   B CB  1 
ATOM   1127 C  CG1 . VAL   A 1 145 ? -8.389  -8.275  17.070 1.00 14.66 ? 145 VAL   B CG1 1 
ATOM   1128 C  CG2 . VAL   A 1 145 ? -7.707  -7.462  19.411 1.00 13.07 ? 145 VAL   B CG2 1 
ATOM   1129 N  N   . LEU   A 1 146 ? -10.218 -11.075 17.650 1.00 11.86 ? 146 LEU   B N   1 
ATOM   1130 C  CA  . LEU   A 1 146 ? -10.513 -12.174 16.751 1.00 13.31 ? 146 LEU   B CA  1 
ATOM   1131 C  C   . LEU   A 1 146 ? -10.228 -11.636 15.357 1.00 13.83 ? 146 LEU   B C   1 
ATOM   1132 O  O   . LEU   A 1 146 ? -10.725 -10.551 14.993 1.00 14.31 ? 146 LEU   B O   1 
ATOM   1133 C  CB  . LEU   A 1 146 ? -12.009 -12.470 16.960 1.00 16.33 ? 146 LEU   B CB  1 
ATOM   1134 C  CG  . LEU   A 1 146 ? -12.587 -13.651 16.214 1.00 21.70 ? 146 LEU   B CG  1 
ATOM   1135 C  CD1 . LEU   A 1 146 ? -11.905 -14.926 16.729 1.00 23.32 ? 146 LEU   B CD1 1 
ATOM   1136 C  CD2 . LEU   A 1 146 ? -14.079 -13.689 16.576 1.00 19.61 ? 146 LEU   B CD2 1 
ATOM   1137 N  N   . GLY   A 1 147 ? -9.357  -12.344 14.619 1.00 12.23 ? 147 GLY   B N   1 
ATOM   1138 C  CA  . GLY   A 1 147 ? -9.089  -11.993 13.236 1.00 13.90 ? 147 GLY   B CA  1 
ATOM   1139 C  C   . GLY   A 1 147 ? -9.773  -12.929 12.248 1.00 15.07 ? 147 GLY   B C   1 
ATOM   1140 O  O   . GLY   A 1 147 ? -9.733  -14.155 12.412 1.00 15.23 ? 147 GLY   B O   1 
ATOM   1141 N  N   . VAL   A 1 148 ? -10.352 -12.329 11.193 1.00 13.33 ? 148 VAL   B N   1 
ATOM   1142 C  CA  . VAL   A 1 148 ? -11.090 -13.094 10.195 1.00 13.66 ? 148 VAL   B CA  1 
ATOM   1143 C  C   . VAL   A 1 148 ? -10.555 -12.679 8.831  1.00 13.25 ? 148 VAL   B C   1 
ATOM   1144 O  O   . VAL   A 1 148 ? -10.577 -11.489 8.522  1.00 13.26 ? 148 VAL   B O   1 
ATOM   1145 C  CB  . VAL   A 1 148 ? -12.623 -12.879 10.296 1.00 14.46 ? 148 VAL   B CB  1 
ATOM   1146 C  CG1 . VAL   A 1 148 ? -13.319 -13.701 9.228  1.00 14.31 ? 148 VAL   B CG1 1 
ATOM   1147 C  CG2 . VAL   A 1 148 ? -13.146 -13.288 11.685 1.00 16.00 ? 148 VAL   B CG2 1 
ATOM   1148 N  N   . PHE   A 1 149 ? -10.048 -13.633 8.025  1.00 12.70 ? 149 PHE   B N   1 
ATOM   1149 C  CA  . PHE   A 1 149 ? -9.552  -13.260 6.712  1.00 13.23 ? 149 PHE   B CA  1 
ATOM   1150 C  C   . PHE   A 1 149 ? -10.692 -13.147 5.713  1.00 13.82 ? 149 PHE   B C   1 
ATOM   1151 O  O   . PHE   A 1 149 ? -11.686 -13.897 5.825  1.00 14.40 ? 149 PHE   B O   1 
ATOM   1152 C  CB  . PHE   A 1 149 ? -8.602  -14.350 6.214  1.00 13.50 ? 149 PHE   B CB  1 
ATOM   1153 C  CG  . PHE   A 1 149 ? -7.374  -14.510 7.073  1.00 13.31 ? 149 PHE   B CG  1 
ATOM   1154 C  CD1 . PHE   A 1 149 ? -6.442  -13.474 7.159  1.00 13.75 ? 149 PHE   B CD1 1 
ATOM   1155 C  CD2 . PHE   A 1 149 ? -7.129  -15.729 7.722  1.00 12.68 ? 149 PHE   B CD2 1 
ATOM   1156 C  CE1 . PHE   A 1 149 ? -5.282  -13.655 7.893  1.00 12.99 ? 149 PHE   B CE1 1 
ATOM   1157 C  CE2 . PHE   A 1 149 ? -5.945  -15.919 8.442  1.00 13.75 ? 149 PHE   B CE2 1 
ATOM   1158 C  CZ  . PHE   A 1 149 ? -5.050  -14.868 8.553  1.00 13.94 ? 149 PHE   B CZ  1 
ATOM   1159 N  N   . LEU   A 1 150 ? -10.526 -12.230 4.739  1.00 12.53 ? 150 LEU   B N   1 
ATOM   1160 C  CA  . LEU   A 1 150 ? -11.484 -12.107 3.636  1.00 13.04 ? 150 LEU   B CA  1 
ATOM   1161 C  C   . LEU   A 1 150 ? -10.754 -12.426 2.333  1.00 13.10 ? 150 LEU   B C   1 
ATOM   1162 O  O   . LEU   A 1 150 ? -9.676  -11.898 2.041  1.00 13.00 ? 150 LEU   B O   1 
ATOM   1163 C  CB  . LEU   A 1 150 ? -12.088 -10.681 3.582  1.00 12.52 ? 150 LEU   B CB  1 
ATOM   1164 C  CG  . LEU   A 1 150 ? -13.037 -10.254 4.710  1.00 13.86 ? 150 LEU   B CG  1 
ATOM   1165 C  CD1 . LEU   A 1 150 ? -12.256 -9.839  5.953  1.00 14.22 ? 150 LEU   B CD1 1 
ATOM   1166 C  CD2 . LEU   A 1 150 ? -13.792 -8.963  4.236  1.00 16.73 ? 150 LEU   B CD2 1 
ATOM   1167 N  N   . GLN   A 1 151 ? -11.368 -13.272 1.520  1.00 14.94 ? 151 GLN   B N   1 
ATOM   1168 C  CA  . GLN   A 1 151 ? -10.808 -13.613 0.224  1.00 17.34 ? 151 GLN   B CA  1 
ATOM   1169 C  C   . GLN   A 1 151 ? -11.770 -13.200 -0.877 1.00 15.84 ? 151 GLN   B C   1 
ATOM   1170 O  O   . GLN   A 1 151 ? -12.981 -13.127 -0.666 1.00 16.69 ? 151 GLN   B O   1 
ATOM   1171 C  CB  . GLN   A 1 151 ? -10.388 -15.083 0.122  1.00 21.39 ? 151 GLN   B CB  1 
ATOM   1172 C  CG  . GLN   A 1 151 ? -11.541 -16.033 0.012  1.00 25.97 ? 151 GLN   B CG  1 
ATOM   1173 C  CD  . GLN   A 1 151 ? -11.113 -17.483 0.115  1.00 31.90 ? 151 GLN   B CD  1 
ATOM   1174 O  OE1 . GLN   A 1 151 ? -9.934  -17.851 -0.006 1.00 36.61 ? 151 GLN   B OE1 1 
ATOM   1175 N  NE2 . GLN   A 1 151 ? -12.107 -18.318 0.343  1.00 33.19 ? 151 GLN   B NE2 1 
ATOM   1176 N  N   . ILE   A 1 152 ? -11.208 -12.793 -2.030 1.00 15.36 ? 152 ILE   B N   1 
ATOM   1177 C  CA  . ILE   A 1 152 ? -12.069 -12.319 -3.110 1.00 18.15 ? 152 ILE   B CA  1 
ATOM   1178 C  C   . ILE   A 1 152 ? -12.894 -13.497 -3.615 1.00 19.87 ? 152 ILE   B C   1 
ATOM   1179 O  O   . ILE   A 1 152 ? -12.370 -14.611 -3.842 1.00 23.33 ? 152 ILE   B O   1 
ATOM   1180 C  CB  . ILE   A 1 152 ? -11.254 -11.735 -4.274 1.00 20.54 ? 152 ILE   B CB  1 
ATOM   1181 C  CG1 . ILE   A 1 152 ? -10.471 -10.476 -3.882 1.00 21.47 ? 152 ILE   B CG1 1 
ATOM   1182 C  CG2 . ILE   A 1 152 ? -12.169 -11.442 -5.476 1.00 23.98 ? 152 ILE   B CG2 1 
ATOM   1183 C  CD1 . ILE   A 1 152 ? -11.317 -9.335  -3.335 1.00 19.02 ? 152 ILE   B CD1 1 
ATOM   1184 N  N   . GLY   A 1 153 ? -14.180 -13.228 -3.807 1.00 19.72 ? 153 GLY   B N   1 
ATOM   1185 C  CA  . GLY   A 1 153 ? -15.112 -14.253 -4.261 1.00 21.83 ? 153 GLY   B CA  1 
ATOM   1186 C  C   . GLY   A 1 153 ? -16.486 -13.670 -4.574 1.00 22.27 ? 153 GLY   B C   1 
ATOM   1187 O  O   . GLY   A 1 153 ? -16.600 -12.529 -5.038 1.00 25.84 ? 153 GLY   B O   1 
ATOM   1188 N  N   . GLU   A 1 154 ? -17.524 -14.449 -4.272 1.00 23.31 ? 154 GLU   B N   1 
ATOM   1189 C  CA  . GLU   A 1 154 ? -18.899 -13.987 -4.326 1.00 23.72 ? 154 GLU   B CA  1 
ATOM   1190 C  C   . GLU   A 1 154 ? -19.016 -12.749 -3.420 1.00 24.03 ? 154 GLU   B C   1 
ATOM   1191 O  O   . GLU   A 1 154 ? -18.372 -12.658 -2.370 1.00 22.24 ? 154 GLU   B O   1 
ATOM   1192 C  CB  . GLU   A 1 154 ? -19.776 -15.214 -4.002 1.00 28.89 ? 154 GLU   B CB  1 
ATOM   1193 C  CG  . GLU   A 1 154 ? -21.181 -14.947 -3.462 1.00 38.16 ? 154 GLU   B CG  1 
ATOM   1194 C  CD  . GLU   A 1 154 ? -21.929 -16.221 -3.042 1.00 42.96 ? 154 GLU   B CD  1 
ATOM   1195 O  OE1 . GLU   A 1 154 ? -22.075 -17.153 -3.893 1.00 44.41 ? 154 GLU   B OE1 1 
ATOM   1196 O  OE2 . GLU   A 1 154 ? -22.354 -16.301 -1.858 1.00 44.61 ? 154 GLU   B OE2 1 
ATOM   1197 N  N   . PRO   A 1 155 ? -19.866 -11.758 -3.767 1.00 21.17 ? 155 PRO   B N   1 
ATOM   1198 C  CA  . PRO   A 1 155 ? -20.199 -10.688 -2.828 1.00 17.81 ? 155 PRO   B CA  1 
ATOM   1199 C  C   . PRO   A 1 155 ? -20.752 -11.287 -1.542 1.00 19.38 ? 155 PRO   B C   1 
ATOM   1200 O  O   . PRO   A 1 155 ? -21.372 -12.367 -1.544 1.00 20.39 ? 155 PRO   B O   1 
ATOM   1201 C  CB  . PRO   A 1 155 ? -21.323 -9.875  -3.494 1.00 21.69 ? 155 PRO   B CB  1 
ATOM   1202 C  CG  . PRO   A 1 155 ? -21.292 -10.325 -4.947 1.00 20.55 ? 155 PRO   B CG  1 
ATOM   1203 C  CD  . PRO   A 1 155 ? -20.584 -11.648 -5.058 1.00 20.53 ? 155 PRO   B CD  1 
ATOM   1204 N  N   . ASN   A 1 156 ? -20.423 -10.620 -0.420 1.00 17.71 ? 156 ASN   B N   1 
ATOM   1205 C  CA  . ASN   A 1 156 ? -20.861 -11.059 0.888  1.00 18.00 ? 156 ASN   B CA  1 
ATOM   1206 C  C   . ASN   A 1 156 ? -22.044 -10.188 1.293  1.00 17.04 ? 156 ASN   B C   1 
ATOM   1207 O  O   . ASN   A 1 156 ? -21.920 -8.991  1.551  1.00 17.27 ? 156 ASN   B O   1 
ATOM   1208 C  CB  . ASN   A 1 156 ? -19.735 -10.895 1.896  1.00 22.17 ? 156 ASN   B CB  1 
ATOM   1209 C  CG  . ASN   A 1 156 ? -20.002 -11.674 3.164  1.00 22.92 ? 156 ASN   B CG  1 
ATOM   1210 O  OD1 . ASN   A 1 156 ? -21.145 -11.700 3.662  1.00 24.21 ? 156 ASN   B OD1 1 
ATOM   1211 N  ND2 . ASN   A 1 156 ? -18.947 -12.276 3.685  1.00 16.31 ? 156 ASN   B ND2 1 
ATOM   1212 N  N   . SER   A 1 157 ? -23.243 -10.805 1.381  1.00 17.68 ? 157 SER   B N   1 
ATOM   1213 C  CA  . SER   A 1 157 ? -24.389 -9.974  1.719  1.00 18.38 ? 157 SER   B CA  1 
ATOM   1214 C  C   . SER   A 1 157 ? -24.329 -9.430  3.141  1.00 18.91 ? 157 SER   B C   1 
ATOM   1215 O  O   . SER   A 1 157 ? -24.919 -8.402  3.413  1.00 21.63 ? 157 SER   B O   1 
ATOM   1216 C  CB  . SER   A 1 157 ? -25.705 -10.721 1.491  1.00 21.80 ? 157 SER   B CB  1 
ATOM   1217 O  OG  . SER   A 1 157 ? -25.721 -11.831 2.381  1.00 24.98 ? 157 SER   B OG  1 
ATOM   1218 N  N   . GLN   A 1 158 ? -23.527 -10.064 3.998  1.00 20.84 ? 158 GLN   B N   1 
ATOM   1219 C  CA  . GLN   A 1 158 ? -23.356 -9.630  5.370  1.00 24.44 ? 158 GLN   B CA  1 
ATOM   1220 C  C   . GLN   A 1 158 ? -22.442 -8.403  5.479  1.00 24.96 ? 158 GLN   B C   1 
ATOM   1221 O  O   . GLN   A 1 158 ? -22.350 -7.897  6.573  1.00 27.74 ? 158 GLN   B O   1 
ATOM   1222 C  CB  . GLN   A 1 158 ? -22.804 -10.761 6.253  1.00 25.60 ? 158 GLN   B CB  1 
ATOM   1223 C  CG  . GLN   A 1 158 ? -23.595 -12.065 6.205  1.00 32.39 ? 158 GLN   B CG  1 
ATOM   1224 C  CD  . GLN   A 1 158 ? -25.053 -11.916 6.567  1.00 41.11 ? 158 GLN   B CD  1 
ATOM   1225 O  OE1 . GLN   A 1 158 ? -25.908 -12.623 6.027  1.00 48.45 ? 158 GLN   B OE1 1 
ATOM   1226 N  NE2 . GLN   A 1 158 ? -25.360 -11.018 7.500  1.00 38.08 ? 158 GLN   B NE2 1 
ATOM   1227 N  N   . LEU   A 1 159 ? -21.765 -7.975  4.392  1.00 19.14 ? 159 LEU   B N   1 
ATOM   1228 C  CA  . LEU   A 1 159 ? -21.013 -6.732  4.383  1.00 19.09 ? 159 LEU   B CA  1 
ATOM   1229 C  C   . LEU   A 1 159 ? -21.798 -5.556  3.795  1.00 23.18 ? 159 LEU   B C   1 
ATOM   1230 O  O   . LEU   A 1 159 ? -21.317 -4.419  3.862  1.00 20.08 ? 159 LEU   B O   1 
ATOM   1231 C  CB  . LEU   A 1 159 ? -19.725 -6.918  3.599  1.00 20.57 ? 159 LEU   B CB  1 
ATOM   1232 C  CG  . LEU   A 1 159 ? -18.736 -7.851  4.294  1.00 20.16 ? 159 LEU   B CG  1 
ATOM   1233 C  CD1 . LEU   A 1 159 ? -17.559 -8.197  3.397  1.00 24.22 ? 159 LEU   B CD1 1 
ATOM   1234 C  CD2 . LEU   A 1 159 ? -18.253 -7.247  5.608  1.00 22.82 ? 159 LEU   B CD2 1 
ATOM   1235 N  N   . GLN   A 1 160 ? -23.024 -5.805  3.315  1.00 23.90 ? 160 GLN   B N   1 
ATOM   1236 C  CA  . GLN   A 1 160 ? -23.766 -4.816  2.540  1.00 26.45 ? 160 GLN   B CA  1 
ATOM   1237 C  C   . GLN   A 1 160 ? -24.208 -3.675  3.450  1.00 24.00 ? 160 GLN   B C   1 
ATOM   1238 O  O   . GLN   A 1 160 ? -24.136 -2.512  3.057  1.00 26.53 ? 160 GLN   B O   1 
ATOM   1239 C  CB  . GLN   A 1 160 ? -25.000 -5.470  1.905  1.00 31.37 ? 160 GLN   B CB  1 
ATOM   1240 C  CG  . GLN   A 1 160 ? -25.825 -4.524  1.038  1.00 36.71 ? 160 GLN   B CG  1 
ATOM   1241 C  CD  . GLN   A 1 160 ? -25.090 -4.244  -0.255 1.00 41.77 ? 160 GLN   B CD  1 
ATOM   1242 O  OE1 . GLN   A 1 160 ? -24.562 -5.149  -0.897 1.00 39.19 ? 160 GLN   B OE1 1 
ATOM   1243 N  NE2 . GLN   A 1 160 ? -25.029 -2.976  -0.647 1.00 42.14 ? 160 GLN   B NE2 1 
ATOM   1244 N  N   . LYS   A 1 161 ? -24.616 -4.000  4.677  1.00 21.63 ? 161 LYS   B N   1 
ATOM   1245 C  CA  . LYS   A 1 161 ? -24.996 -2.976  5.626  1.00 20.77 ? 161 LYS   B CA  1 
ATOM   1246 C  C   . LYS   A 1 161 ? -23.830 -1.994  5.782  1.00 21.28 ? 161 LYS   B C   1 
ATOM   1247 O  O   . LYS   A 1 161 ? -24.037 -0.780  5.845  1.00 20.47 ? 161 LYS   B O   1 
ATOM   1248 C  CB  . LYS   A 1 161 ? -25.398 -3.584  6.983  1.00 24.62 ? 161 LYS   B CB  1 
ATOM   1249 C  CG  . LYS   A 1 161 ? -26.239 -2.682  7.888  1.00 26.66 ? 161 LYS   B CG  1 
ATOM   1250 C  CD  . LYS   A 1 161 ? -26.457 -3.222  9.315  1.00 29.71 ? 161 LYS   B CD  1 
ATOM   1251 C  CE  . LYS   A 1 161 ? -26.942 -2.204  10.325 1.00 29.82 ? 161 LYS   B CE  1 
ATOM   1252 N  NZ  . LYS   A 1 161 ? -28.361 -1.794  10.079 1.00 28.62 ? 161 LYS   B NZ  1 
ATOM   1253 N  N   . ILE   A 1 162 ? -22.588 -2.509  5.870  1.00 19.12 ? 162 ILE   B N   1 
ATOM   1254 C  CA  . ILE   A 1 162 ? -21.462 -1.618  6.069  1.00 18.71 ? 162 ILE   B CA  1 
ATOM   1255 C  C   . ILE   A 1 162 ? -21.232 -0.754  4.823  1.00 18.40 ? 162 ILE   B C   1 
ATOM   1256 O  O   . ILE   A 1 162 ? -20.994 0.454   4.921  1.00 18.06 ? 162 ILE   B O   1 
ATOM   1257 C  CB  . ILE   A 1 162 ? -20.195 -2.401  6.513  1.00 17.28 ? 162 ILE   B CB  1 
ATOM   1258 C  CG1 . ILE   A 1 162 ? -20.395 -3.023  7.899  1.00 17.92 ? 162 ILE   B CG1 1 
ATOM   1259 C  CG2 . ILE   A 1 162 ? -18.992 -1.459  6.492  1.00 17.03 ? 162 ILE   B CG2 1 
ATOM   1260 C  CD1 . ILE   A 1 162 ? -19.335 -4.034  8.320  1.00 19.12 ? 162 ILE   B CD1 1 
ATOM   1261 N  N   . THR   A 1 163 ? -21.153 -1.383  3.647  1.00 18.46 ? 163 THR   B N   1 
ATOM   1262 C  CA  . THR   A 1 163 ? -20.763 -0.672  2.444  1.00 21.39 ? 163 THR   B CA  1 
ATOM   1263 C  C   . THR   A 1 163 ? -21.782 0.422   2.126  1.00 21.05 ? 163 THR   B C   1 
ATOM   1264 O  O   . THR   A 1 163 ? -21.382 1.464   1.622  1.00 21.98 ? 163 THR   B O   1 
ATOM   1265 C  CB  . THR   A 1 163 ? -20.461 -1.595  1.250  1.00 21.66 ? 163 THR   B CB  1 
ATOM   1266 O  OG1 . THR   A 1 163 ? -21.640 -2.292  0.865  1.00 26.56 ? 163 THR   B OG1 1 
ATOM   1267 C  CG2 . THR   A 1 163 ? -19.399 -2.624  1.548  1.00 23.64 ? 163 THR   B CG2 1 
ATOM   1268 N  N   . ASP   A 1 164 ? -23.068 0.170   2.419  1.00 23.34 ? 164 ASP   B N   1 
ATOM   1269 C  CA  . ASP   A 1 164 ? -24.113 1.177   2.263  1.00 23.78 ? 164 ASP   B CA  1 
ATOM   1270 C  C   . ASP   A 1 164 ? -23.870 2.447   3.089  1.00 23.67 ? 164 ASP   B C   1 
ATOM   1271 O  O   . ASP   A 1 164 ? -24.419 3.500   2.753  1.00 28.22 ? 164 ASP   B O   1 
ATOM   1272 C  CB  . ASP   A 1 164 ? -25.491 0.596   2.576  1.00 23.49 ? 164 ASP   B CB  1 
ATOM   1273 C  CG  . ASP   A 1 164 ? -26.000 -0.343  1.490  1.00 29.81 ? 164 ASP   B CG  1 
ATOM   1274 O  OD1 . ASP   A 1 164 ? -25.413 -0.330  0.410  1.00 28.36 ? 164 ASP   B OD1 1 
ATOM   1275 O  OD2 . ASP   A 1 164 ? -26.995 -1.097  1.756  1.00 31.65 ? 164 ASP   B OD2 1 
ATOM   1276 N  N   . THR   A 1 165 ? -23.140 2.374   4.206  1.00 18.67 ? 165 THR   B N   1 
ATOM   1277 C  CA  . THR   A 1 165 ? -22.935 3.559   5.018  1.00 19.69 ? 165 THR   B CA  1 
ATOM   1278 C  C   . THR   A 1 165 ? -21.737 4.387   4.593  1.00 19.51 ? 165 THR   B C   1 
ATOM   1279 O  O   . THR   A 1 165 ? -21.586 5.494   5.101  1.00 21.18 ? 165 THR   B O   1 
ATOM   1280 C  CB  . THR   A 1 165 ? -22.711 3.234   6.502  1.00 21.31 ? 165 THR   B CB  1 
ATOM   1281 O  OG1 . THR   A 1 165 ? -21.431 2.592   6.648  1.00 21.82 ? 165 THR   B OG1 1 
ATOM   1282 C  CG2 . THR   A 1 165 ? -23.852 2.438   7.094  1.00 20.91 ? 165 THR   B CG2 1 
ATOM   1283 N  N   . LEU   A 1 166 ? -20.875 3.870   3.701  1.00 19.14 ? 166 LEU   B N   1 
ATOM   1284 C  CA  . LEU   A 1 166 ? -19.560 4.466   3.620  1.00 17.69 ? 166 LEU   B CA  1 
ATOM   1285 C  C   . LEU   A 1 166 ? -19.675 5.866   3.021  1.00 18.24 ? 166 LEU   B C   1 
ATOM   1286 O  O   . LEU   A 1 166 ? -18.858 6.725   3.341  1.00 22.61 ? 166 LEU   B O   1 
ATOM   1287 C  CB  . LEU   A 1 166 ? -18.602 3.603   2.786  1.00 19.44 ? 166 LEU   B CB  1 
ATOM   1288 C  CG  . LEU   A 1 166 ? -18.320 2.211   3.353  1.00 20.18 ? 166 LEU   B CG  1 
ATOM   1289 C  CD1 . LEU   A 1 166 ? -17.402 1.405   2.444  1.00 22.72 ? 166 LEU   B CD1 1 
ATOM   1290 C  CD2 . LEU   A 1 166 ? -17.698 2.334   4.749  1.00 21.43 ? 166 LEU   B CD2 1 
ATOM   1291 N  N   . ASP   A 1 167 ? -20.633 6.067   2.112  1.00 22.62 ? 167 ASP   B N   1 
ATOM   1292 C  CA  . ASP   A 1 167 ? -20.777 7.403   1.544  1.00 26.60 ? 167 ASP   B CA  1 
ATOM   1293 C  C   . ASP   A 1 167 ? -21.049 8.455   2.626  1.00 27.41 ? 167 ASP   B C   1 
ATOM   1294 O  O   . ASP   A 1 167 ? -20.696 9.624   2.454  1.00 34.20 ? 167 ASP   B O   1 
ATOM   1295 C  CB  . ASP   A 1 167 ? -21.840 7.437   0.442  1.00 29.31 ? 167 ASP   B CB  1 
ATOM   1296 C  CG  . ASP   A 1 167 ? -21.443 6.743   -0.846 1.00 37.91 ? 167 ASP   B CG  1 
ATOM   1297 O  OD1 . ASP   A 1 167 ? -20.232 6.737   -1.190 1.00 36.01 ? 167 ASP   B OD1 1 
ATOM   1298 O  OD2 . ASP   A 1 167 ? -22.369 6.247   -1.522 1.00 45.99 ? 167 ASP   B OD2 1 
ATOM   1299 N  N   . SER   A 1 168 ? -21.704 8.087   3.735  1.00 21.35 ? 168 SER   B N   1 
ATOM   1300 C  CA  . SER   A 1 168 ? -22.044 9.080   4.731  1.00 23.37 ? 168 SER   B CA  1 
ATOM   1301 C  C   . SER   A 1 168 ? -20.908 9.331   5.725  1.00 23.22 ? 168 SER   B C   1 
ATOM   1302 O  O   . SER   A 1 168 ? -20.971 10.265  6.542  1.00 23.06 ? 168 SER   B O   1 
ATOM   1303 C  CB  . SER   A 1 168 ? -23.391 8.771   5.363  1.00 26.60 ? 168 SER   B CB  1 
ATOM   1304 O  OG  . SER   A 1 168 ? -23.218 7.732   6.281  1.00 35.39 ? 168 SER   B OG  1 
ATOM   1305 N  N   . ILE   A 1 169 ? -19.821 8.542   5.619  1.00 18.61 ? 169 ILE   B N   1 
ATOM   1306 C  CA  . ILE   A 1 169 ? -18.719 8.694   6.549  1.00 17.46 ? 169 ILE   B CA  1 
ATOM   1307 C  C   . ILE   A 1 169 ? -17.430 8.824   5.737  1.00 17.57 ? 169 ILE   B C   1 
ATOM   1308 O  O   . ILE   A 1 169 ? -16.371 8.433   6.175  1.00 19.18 ? 169 ILE   B O   1 
ATOM   1309 C  CB  . ILE   A 1 169 ? -18.667 7.581   7.637  1.00 17.24 ? 169 ILE   B CB  1 
ATOM   1310 C  CG1 . ILE   A 1 169 ? -18.499 6.171   7.074  1.00 17.17 ? 169 ILE   B CG1 1 
ATOM   1311 C  CG2 . ILE   A 1 169 ? -19.859 7.664   8.603  1.00 18.69 ? 169 ILE   B CG2 1 
ATOM   1312 C  CD1 . ILE   A 1 169 ? -17.786 5.247   8.099  1.00 18.89 ? 169 ILE   B CD1 1 
ATOM   1313 N  N   . LYS   A 1 170 ? -17.494 9.526   4.599  1.00 17.06 ? 170 LYS   B N   1 
ATOM   1314 C  CA  . LYS   A 1 170 ? -16.315 9.609   3.752  1.00 19.01 ? 170 LYS   B CA  1 
ATOM   1315 C  C   . LYS   A 1 170 ? -15.136 10.323  4.424  1.00 17.13 ? 170 LYS   B C   1 
ATOM   1316 O  O   . LYS   A 1 170 ? -13.989 9.899   4.287  1.00 16.65 ? 170 LYS   B O   1 
ATOM   1317 C  CB  . LYS   A 1 170 ? -16.689 10.252  2.411  1.00 22.52 ? 170 LYS   B CB  1 
ATOM   1318 C  CG  . LYS   A 1 170 ? -15.531 10.414  1.445  1.00 30.76 ? 170 LYS   B CG  1 
ATOM   1319 C  CD  . LYS   A 1 170 ? -15.939 11.098  0.149  1.00 35.25 ? 170 LYS   B CD  1 
ATOM   1320 C  CE  . LYS   A 1 170 ? -14.732 11.671  -0.572 1.00 43.07 ? 170 LYS   B CE  1 
ATOM   1321 N  NZ  . LYS   A 1 170 ? -14.976 11.834  -2.023 1.00 52.00 ? 170 LYS   B NZ  1 
ATOM   1322 N  N   . GLU   A 1 171 ? -15.391 11.434  5.128  1.00 19.03 ? 171 GLU   B N   1 
ATOM   1323 C  CA  . GLU   A 1 171 ? -14.323 12.211  5.748  1.00 18.29 ? 171 GLU   B CA  1 
ATOM   1324 C  C   . GLU   A 1 171 ? -14.013 11.696  7.153  1.00 18.87 ? 171 GLU   B C   1 
ATOM   1325 O  O   . GLU   A 1 171 ? -14.896 11.212  7.867  1.00 18.56 ? 171 GLU   B O   1 
ATOM   1326 C  CB  . GLU   A 1 171 ? -14.753 13.687  5.849  1.00 23.81 ? 171 GLU   B CB  1 
ATOM   1327 C  CG  . GLU   A 1 171 ? -15.171 14.259  4.482  1.00 27.10 ? 171 GLU   B CG  1 
ATOM   1328 C  CD  . GLU   A 1 171 ? -16.519 13.907  3.836  1.00 32.89 ? 171 GLU   B CD  1 
ATOM   1329 O  OE1 . GLU   A 1 171 ? -16.609 14.017  2.583  1.00 41.65 ? 171 GLU   B OE1 1 
ATOM   1330 O  OE2 . GLU   A 1 171 ? -17.499 13.509  4.545  1.00 33.29 ? 171 GLU   B OE2 1 
ATOM   1331 N  N   . LYS   A 1 172 ? -12.744 11.807  7.554  1.00 17.31 ? 172 LYS   B N   1 
ATOM   1332 C  CA  . LYS   A 1 172 ? -12.284 11.504  8.900  1.00 17.87 ? 172 LYS   B CA  1 
ATOM   1333 C  C   . LYS   A 1 172 ? -13.108 12.262  9.946  1.00 19.49 ? 172 LYS   B C   1 
ATOM   1334 O  O   . LYS   A 1 172 ? -13.305 13.485  9.811  1.00 20.43 ? 172 LYS   B O   1 
ATOM   1335 C  CB  . LYS   A 1 172 ? -10.805 11.872  9.097  1.00 18.22 ? 172 LYS   B CB  1 
ATOM   1336 C  CG  . LYS   A 1 172 ? -10.304 11.720  10.532 1.00 18.07 ? 172 LYS   B CG  1 
ATOM   1337 C  CD  . LYS   A 1 172 ? -8.836  12.086  10.593 1.00 22.30 ? 172 LYS   B CD  1 
ATOM   1338 C  CE  . LYS   A 1 172 ? -8.081  11.630  11.826 1.00 27.31 ? 172 LYS   B CE  1 
ATOM   1339 N  NZ  . LYS   A 1 172 ? -6.647  11.974  11.630 1.00 36.56 ? 172 LYS   B NZ  1 
ATOM   1340 N  N   . GLY   A 1 173 ? -13.657 11.502  10.903 1.00 17.46 ? 173 GLY   B N   1 
ATOM   1341 C  CA  . GLY   A 1 173 ? -14.428 12.008  12.032 1.00 19.81 ? 173 GLY   B CA  1 
ATOM   1342 C  C   . GLY   A 1 173 ? -15.939 11.953  11.842 1.00 18.26 ? 173 GLY   B C   1 
ATOM   1343 O  O   . GLY   A 1 173 ? -16.652 12.100  12.831 1.00 23.75 ? 173 GLY   B O   1 
ATOM   1344 N  N   . LYS   A 1 174 ? -16.429 11.683  10.625 1.00 15.45 ? 174 LYS   B N   1 
ATOM   1345 C  CA  . LYS   A 1 174 ? -17.854 11.509  10.427 1.00 16.86 ? 174 LYS   B CA  1 
ATOM   1346 C  C   . LYS   A 1 174 ? -18.358 10.221  11.072 1.00 17.96 ? 174 LYS   B C   1 
ATOM   1347 O  O   . LYS   A 1 174 ? -17.646 9.217   11.146 1.00 17.90 ? 174 LYS   B O   1 
ATOM   1348 C  CB  . LYS   A 1 174 ? -18.191 11.446  8.947  1.00 17.14 ? 174 LYS   B CB  1 
ATOM   1349 C  CG  . LYS   A 1 174 ? -17.760 12.714  8.220  1.00 25.16 ? 174 LYS   B CG  1 
ATOM   1350 C  CD  . LYS   A 1 174 ? -18.482 13.892  8.778  1.00 27.37 ? 174 LYS   B CD  1 
ATOM   1351 C  CE  . LYS   A 1 174 ? -18.202 15.149  7.965  1.00 34.93 ? 174 LYS   B CE  1 
ATOM   1352 N  NZ  . LYS   A 1 174 ? -18.806 15.037  6.618  1.00 35.28 ? 174 LYS   B NZ  1 
ATOM   1353 N  N   . GLN   A 1 175 ? -19.612 10.281  11.532 1.00 16.80 ? 175 GLN   B N   1 
ATOM   1354 C  CA  . GLN   A 1 175 ? -20.212 9.125   12.183 1.00 19.25 ? 175 GLN   B CA  1 
ATOM   1355 C  C   . GLN   A 1 175 ? -21.688 9.084   11.833 1.00 20.36 ? 175 GLN   B C   1 
ATOM   1356 O  O   . GLN   A 1 175 ? -22.289 10.130  11.510 1.00 21.39 ? 175 GLN   B O   1 
ATOM   1357 C  CB  . GLN   A 1 175 ? -20.006 9.164   13.703 1.00 23.22 ? 175 GLN   B CB  1 
ATOM   1358 C  CG  . GLN   A 1 175 ? -20.676 10.348  14.418 1.00 26.79 ? 175 GLN   B CG  1 
ATOM   1359 C  CD  . GLN   A 1 175 ? -20.523 10.106  15.902 1.00 35.61 ? 175 GLN   B CD  1 
ATOM   1360 O  OE1 . GLN   A 1 175 ? -21.396 9.525   16.556 1.00 39.88 ? 175 GLN   B OE1 1 
ATOM   1361 N  NE2 . GLN   A 1 175 ? -19.353 10.426  16.426 1.00 42.74 ? 175 GLN   B NE2 1 
ATOM   1362 N  N   . THR   A 1 176 ? -22.243 7.868   11.819 1.00 16.88 ? 176 THR   B N   1 
ATOM   1363 C  CA  . THR   A 1 176 ? -23.657 7.671   11.545 1.00 17.88 ? 176 THR   B CA  1 
ATOM   1364 C  C   . THR   A 1 176 ? -24.203 6.502   12.384 1.00 19.29 ? 176 THR   B C   1 
ATOM   1365 O  O   . THR   A 1 176 ? -23.470 5.600   12.803 1.00 19.97 ? 176 THR   B O   1 
ATOM   1366 C  CB  . THR   A 1 176 ? -23.941 7.635   10.029 1.00 20.18 ? 176 THR   B CB  1 
ATOM   1367 O  OG1 . THR   A 1 176 ? -25.342 7.845   9.786  1.00 23.73 ? 176 THR   B OG1 1 
ATOM   1368 C  CG2 . THR   A 1 176 ? -23.556 6.334   9.341  1.00 20.40 ? 176 THR   B CG2 1 
ATOM   1369 N  N   . ARG   A 1 177 ? -25.516 6.518   12.632 1.00 18.57 ? 177 ARG   B N   1 
ATOM   1370 C  CA  . ARG   A 1 177 ? -26.167 5.428   13.340 1.00 17.24 ? 177 ARG   B CA  1 
ATOM   1371 C  C   . ARG   A 1 177 ? -25.928 4.114   12.619 1.00 16.56 ? 177 ARG   B C   1 
ATOM   1372 O  O   . ARG   A 1 177 ? -25.965 4.043   11.400 1.00 17.35 ? 177 ARG   B O   1 
ATOM   1373 C  CB  . ARG   A 1 177 ? -27.691 5.673   13.366 1.00 19.30 ? 177 ARG   B CB  1 
ATOM   1374 C  CG  . ARG   A 1 177 ? -28.511 4.561   14.003 1.00 24.04 ? 177 ARG   B CG  1 
ATOM   1375 C  CD  . ARG   A 1 177 ? -30.005 4.822   13.929 1.00 25.74 ? 177 ARG   B CD  1 
ATOM   1376 N  NE  . ARG   A 1 177 ? -30.382 6.082   14.593 1.00 25.00 ? 177 ARG   B NE  1 
ATOM   1377 C  CZ  . ARG   A 1 177 ? -30.969 6.173   15.801 1.00 25.03 ? 177 ARG   B CZ  1 
ATOM   1378 N  NH1 . ARG   A 1 177 ? -31.282 7.358   16.297 1.00 20.60 ? 177 ARG   B NH1 1 
ATOM   1379 N  NH2 . ARG   A 1 177 ? -31.202 5.080   16.525 1.00 25.92 ? 177 ARG   B NH2 1 
ATOM   1380 N  N   . PHE   A 1 178 ? -25.730 3.051   13.421 1.00 18.30 ? 178 PHE   B N   1 
ATOM   1381 C  CA  . PHE   A 1 178 ? -25.505 1.750   12.810 1.00 18.48 ? 178 PHE   B CA  1 
ATOM   1382 C  C   . PHE   A 1 178 ? -25.958 0.680   13.805 1.00 21.03 ? 178 PHE   B C   1 
ATOM   1383 O  O   . PHE   A 1 178 ? -25.266 0.372   14.772 1.00 18.98 ? 178 PHE   B O   1 
ATOM   1384 C  CB  . PHE   A 1 178 ? -24.009 1.577   12.502 1.00 17.78 ? 178 PHE   B CB  1 
ATOM   1385 C  CG  . PHE   A 1 178 ? -23.702 0.335   11.684 1.00 17.77 ? 178 PHE   B CG  1 
ATOM   1386 C  CD1 . PHE   A 1 178 ? -23.823 0.341   10.306 1.00 21.88 ? 178 PHE   B CD1 1 
ATOM   1387 C  CD2 . PHE   A 1 178 ? -23.242 -0.831  12.302 1.00 19.27 ? 178 PHE   B CD2 1 
ATOM   1388 C  CE1 . PHE   A 1 178 ? -23.512 -0.782  9.545  1.00 22.06 ? 178 PHE   B CE1 1 
ATOM   1389 C  CE2 . PHE   A 1 178 ? -22.911 -1.950  11.539 1.00 18.93 ? 178 PHE   B CE2 1 
ATOM   1390 C  CZ  . PHE   A 1 178 ? -23.041 -1.923  10.162 1.00 20.59 ? 178 PHE   B CZ  1 
ATOM   1391 N  N   . THR   A 1 179 ? -27.139 0.110   13.570 1.00 25.47 ? 179 THR   B N   1 
ATOM   1392 C  CA  . THR   A 1 179 ? -27.669 -0.793  14.582 1.00 26.62 ? 179 THR   B CA  1 
ATOM   1393 C  C   . THR   A 1 179 ? -28.316 -1.995  13.906 1.00 26.28 ? 179 THR   B C   1 
ATOM   1394 O  O   . THR   A 1 179 ? -28.453 -2.007  12.684 1.00 29.74 ? 179 THR   B O   1 
ATOM   1395 C  CB  . THR   A 1 179 ? -28.548 -0.078  15.612 1.00 37.12 ? 179 THR   B CB  1 
ATOM   1396 O  OG1 . THR   A 1 179 ? -28.777 -1.028  16.667 1.00 47.07 ? 179 THR   B OG1 1 
ATOM   1397 C  CG2 . THR   A 1 179 ? -29.813 0.483   15.003 1.00 29.94 ? 179 THR   B CG2 1 
ATOM   1398 N  N   A ASN   A 1 180 ? -28.703 -2.984  14.725 0.50 23.90 ? 180 ASN   B N   1 
ATOM   1399 N  N   B ASN   A 1 180 ? -28.675 -2.998  14.723 0.50 24.03 ? 180 ASN   B N   1 
ATOM   1400 C  CA  A ASN   A 1 180 ? -29.265 -4.239  14.258 0.50 25.31 ? 180 ASN   B CA  1 
ATOM   1401 C  CA  B ASN   A 1 180 ? -29.282 -4.228  14.248 0.50 25.51 ? 180 ASN   B CA  1 
ATOM   1402 C  C   A ASN   A 1 180 ? -28.303 -4.886  13.262 0.50 23.93 ? 180 ASN   B C   1 
ATOM   1403 C  C   B ASN   A 1 180 ? -28.314 -4.899  13.266 0.50 24.03 ? 180 ASN   B C   1 
ATOM   1404 O  O   A ASN   A 1 180 ? -28.637 -5.096  12.095 0.50 25.61 ? 180 ASN   B O   1 
ATOM   1405 O  O   B ASN   A 1 180 ? -28.650 -5.128  12.103 0.50 25.82 ? 180 ASN   B O   1 
ATOM   1406 C  CB  A ASN   A 1 180 ? -30.680 -4.083  13.705 0.50 26.78 ? 180 ASN   B CB  1 
ATOM   1407 C  CB  B ASN   A 1 180 ? -30.710 -3.976  13.747 0.50 27.08 ? 180 ASN   B CB  1 
ATOM   1408 C  CG  A ASN   A 1 180 ? -31.369 -5.426  13.622 0.50 27.01 ? 180 ASN   B CG  1 
ATOM   1409 C  CG  B ASN   A 1 180 ? -31.645 -3.500  14.842 0.50 27.66 ? 180 ASN   B CG  1 
ATOM   1410 O  OD1 A ASN   A 1 180 ? -31.111 -6.305  14.452 0.50 30.28 ? 180 ASN   B OD1 1 
ATOM   1411 O  OD1 B ASN   A 1 180 ? -31.568 -3.956  15.984 0.50 30.70 ? 180 ASN   B OD1 1 
ATOM   1412 N  ND2 A ASN   A 1 180 ? -32.246 -5.583  12.645 0.50 29.33 ? 180 ASN   B ND2 1 
ATOM   1413 N  ND2 B ASN   A 1 180 ? -32.546 -2.588  14.504 0.50 32.35 ? 180 ASN   B ND2 1 
ATOM   1414 N  N   . PHE   A 1 181 ? -27.082 -5.158  13.740 1.00 23.82 ? 181 PHE   B N   1 
ATOM   1415 C  CA  . PHE   A 1 181 ? -26.007 -5.710  12.922 1.00 20.67 ? 181 PHE   B CA  1 
ATOM   1416 C  C   . PHE   A 1 181 ? -25.687 -7.117  13.423 1.00 22.56 ? 181 PHE   B C   1 
ATOM   1417 O  O   . PHE   A 1 181 ? -25.247 -7.278  14.560 1.00 21.51 ? 181 PHE   B O   1 
ATOM   1418 C  CB  . PHE   A 1 181 ? -24.777 -4.798  13.016 1.00 21.13 ? 181 PHE   B CB  1 
ATOM   1419 C  CG  . PHE   A 1 181 ? -23.473 -5.293  12.426 1.00 21.01 ? 181 PHE   B CG  1 
ATOM   1420 C  CD1 . PHE   A 1 181 ? -23.406 -5.738  11.115 1.00 20.34 ? 181 PHE   B CD1 1 
ATOM   1421 C  CD2 . PHE   A 1 181 ? -22.297 -5.267  13.169 1.00 20.31 ? 181 PHE   B CD2 1 
ATOM   1422 C  CE1 . PHE   A 1 181 ? -22.209 -6.163  10.565 1.00 23.46 ? 181 PHE   B CE1 1 
ATOM   1423 C  CE2 . PHE   A 1 181 ? -21.099 -5.701  12.616 1.00 21.85 ? 181 PHE   B CE2 1 
ATOM   1424 C  CZ  . PHE   A 1 181 ? -21.060 -6.145  11.317 1.00 22.50 ? 181 PHE   B CZ  1 
ATOM   1425 N  N   . ASP   A 1 182 ? -25.861 -8.116  12.554 1.00 21.43 ? 182 ASP   B N   1 
ATOM   1426 C  CA  . ASP   A 1 182 ? -25.709 -9.498  12.977 1.00 21.93 ? 182 ASP   B CA  1 
ATOM   1427 C  C   . ASP   A 1 182 ? -24.270 -9.967  12.754 1.00 20.55 ? 182 ASP   B C   1 
ATOM   1428 O  O   . ASP   A 1 182 ? -23.944 -10.649 11.808 1.00 21.60 ? 182 ASP   B O   1 
ATOM   1429 C  CB  . ASP   A 1 182 ? -26.738 -10.353 12.229 1.00 26.95 ? 182 ASP   B CB  1 
ATOM   1430 C  CG  . ASP   A 1 182 ? -26.758 -11.822 12.637 1.00 34.07 ? 182 ASP   B CG  1 
ATOM   1431 O  OD1 . ASP   A 1 182 ? -26.064 -12.211 13.615 1.00 35.69 ? 182 ASP   B OD1 1 
ATOM   1432 O  OD2 . ASP   A 1 182 ? -27.495 -12.575 11.968 1.00 30.57 ? 182 ASP   B OD2 1 
ATOM   1433 N  N   . LEU   A 1 183 ? -23.377 -9.569  13.659 1.00 19.91 ? 183 LEU   B N   1 
ATOM   1434 C  CA  . LEU   A 1 183 ? -21.963 -9.843  13.488 1.00 16.78 ? 183 LEU   B CA  1 
ATOM   1435 C  C   . LEU   A 1 183 ? -21.731 -11.347 13.500 1.00 18.72 ? 183 LEU   B C   1 
ATOM   1436 O  O   . LEU   A 1 183 ? -20.801 -11.841 12.866 1.00 16.96 ? 183 LEU   B O   1 
ATOM   1437 C  CB  . LEU   A 1 183 ? -21.241 -9.201  14.684 1.00 14.60 ? 183 LEU   B CB  1 
ATOM   1438 C  CG  . LEU   A 1 183 ? -19.709 -9.410  14.739 1.00 15.30 ? 183 LEU   B CG  1 
ATOM   1439 C  CD1 . LEU   A 1 183 ? -18.980 -8.982  13.455 1.00 17.60 ? 183 LEU   B CD1 1 
ATOM   1440 C  CD2 . LEU   A 1 183 ? -19.165 -8.653  15.967 1.00 14.10 ? 183 LEU   B CD2 1 
ATOM   1441 N  N   . LEU   A 1 184 ? -22.565 -12.078 14.274 1.00 18.23 ? 184 LEU   B N   1 
ATOM   1442 C  CA  . LEU   A 1 184 ? -22.348 -13.517 14.326 1.00 19.84 ? 184 LEU   B CA  1 
ATOM   1443 C  C   . LEU   A 1 184 ? -22.407 -14.133 12.928 1.00 17.81 ? 184 LEU   B C   1 
ATOM   1444 O  O   . LEU   A 1 184 ? -21.640 -15.056 12.606 1.00 19.42 ? 184 LEU   B O   1 
ATOM   1445 C  CB  . LEU   A 1 184 ? -23.460 -14.135 15.179 1.00 23.04 ? 184 LEU   B CB  1 
ATOM   1446 C  CG  . LEU   A 1 184 ? -23.241 -15.628 15.395 1.00 25.97 ? 184 LEU   B CG  1 
ATOM   1447 C  CD1 . LEU   A 1 184 ? -22.046 -15.790 16.325 1.00 28.22 ? 184 LEU   B CD1 1 
ATOM   1448 C  CD2 . LEU   A 1 184 ? -24.484 -16.272 16.022 1.00 26.44 ? 184 LEU   B CD2 1 
ATOM   1449 N  N   . SER   A 1 185 ? -23.320 -13.614 12.093 1.00 17.91 ? 185 SER   B N   1 
ATOM   1450 C  CA  . SER   A 1 185 ? -23.503 -14.166 10.744 1.00 19.90 ? 185 SER   B CA  1 
ATOM   1451 C  C   . SER   A 1 185 ? -22.374 -13.825 9.777  1.00 21.45 ? 185 SER   B C   1 
ATOM   1452 O  O   . SER   A 1 185 ? -22.250 -14.427 8.711  1.00 22.73 ? 185 SER   B O   1 
ATOM   1453 C  CB  . SER   A 1 185 ? -24.830 -13.729 10.165 1.00 21.35 ? 185 SER   B CB  1 
ATOM   1454 O  OG  . SER   A 1 185 ? -25.846 -14.387 10.908 1.00 28.37 ? 185 SER   B OG  1 
ATOM   1455 N  N   . LEU   A 1 186 ? -21.493 -12.902 10.155 1.00 21.11 ? 186 LEU   B N   1 
ATOM   1456 C  CA  . LEU   A 1 186 ? -20.367 -12.595 9.288  1.00 20.26 ? 186 LEU   B CA  1 
ATOM   1457 C  C   . LEU   A 1 186 ? -19.242 -13.624 9.485  1.00 22.09 ? 186 LEU   B C   1 
ATOM   1458 O  O   . LEU   A 1 186 ? -18.440 -13.858 8.575  1.00 22.07 ? 186 LEU   B O   1 
ATOM   1459 C  CB  . LEU   A 1 186 ? -19.960 -11.157 9.644  1.00 22.59 ? 186 LEU   B CB  1 
ATOM   1460 C  CG  . LEU   A 1 186 ? -18.990 -10.382 8.773  1.00 23.23 ? 186 LEU   B CG  1 
ATOM   1461 C  CD1 . LEU   A 1 186 ? -19.413 -10.430 7.293  1.00 20.40 ? 186 LEU   B CD1 1 
ATOM   1462 C  CD2 . LEU   A 1 186 ? -18.921 -8.929  9.287  1.00 22.34 ? 186 LEU   B CD2 1 
ATOM   1463 N  N   . LEU   A 1 187 ? -19.164 -14.285 10.661 1.00 20.11 ? 187 LEU   B N   1 
ATOM   1464 C  CA  . LEU   A 1 187 ? -18.078 -15.218 10.941 1.00 19.99 ? 187 LEU   B CA  1 
ATOM   1465 C  C   . LEU   A 1 187 ? -18.199 -16.461 10.071 1.00 19.67 ? 187 LEU   B C   1 
ATOM   1466 O  O   . LEU   A 1 187 ? -19.315 -16.817 9.638  1.00 20.53 ? 187 LEU   B O   1 
ATOM   1467 C  CB  . LEU   A 1 187 ? -18.129 -15.669 12.408 1.00 20.36 ? 187 LEU   B CB  1 
ATOM   1468 C  CG  . LEU   A 1 187 ? -18.036 -14.559 13.431 1.00 23.71 ? 187 LEU   B CG  1 
ATOM   1469 C  CD1 . LEU   A 1 187 ? -18.103 -15.165 14.826 1.00 25.58 ? 187 LEU   B CD1 1 
ATOM   1470 C  CD2 . LEU   A 1 187 ? -16.731 -13.789 13.241 1.00 23.01 ? 187 LEU   B CD2 1 
ATOM   1471 N  N   . PRO   A 1 188 ? -17.074 -17.145 9.794  1.00 18.17 ? 188 PRO   B N   1 
ATOM   1472 C  CA  . PRO   A 1 188 ? -17.075 -18.372 8.998  1.00 18.19 ? 188 PRO   B CA  1 
ATOM   1473 C  C   . PRO   A 1 188 ? -17.690 -19.520 9.808  1.00 21.23 ? 188 PRO   B C   1 
ATOM   1474 O  O   . PRO   A 1 188 ? -17.895 -19.380 11.015 1.00 23.08 ? 188 PRO   B O   1 
ATOM   1475 C  CB  . PRO   A 1 188 ? -15.599 -18.676 8.735  1.00 19.13 ? 188 PRO   B CB  1 
ATOM   1476 C  CG  . PRO   A 1 188 ? -14.880 -18.002 9.898  1.00 17.01 ? 188 PRO   B CG  1 
ATOM   1477 C  CD  . PRO   A 1 188 ? -15.720 -16.816 10.338 1.00 16.50 ? 188 PRO   B CD  1 
ATOM   1478 N  N   . PRO   A 1 189 ? -18.063 -20.624 9.125  1.00 26.78 ? 189 PRO   B N   1 
ATOM   1479 C  CA  . PRO   A 1 189 ? -18.736 -21.758 9.782  1.00 30.43 ? 189 PRO   B CA  1 
ATOM   1480 C  C   . PRO   A 1 189 ? -17.880 -22.565 10.769 1.00 30.00 ? 189 PRO   B C   1 
ATOM   1481 O  O   . PRO   A 1 189 ? -18.428 -23.086 11.746 1.00 34.77 ? 189 PRO   B O   1 
ATOM   1482 C  CB  . PRO   A 1 189 ? -19.320 -22.554 8.599  1.00 32.52 ? 189 PRO   B CB  1 
ATOM   1483 C  CG  . PRO   A 1 189 ? -18.441 -22.216 7.400  1.00 31.79 ? 189 PRO   B CG  1 
ATOM   1484 C  CD  . PRO   A 1 189 ? -17.955 -20.792 7.667  1.00 27.53 ? 189 PRO   B CD  1 
ATOM   1485 N  N   . SER   A 1 190 ? -16.561 -22.659 10.510 1.00 25.02 ? 190 SER   B N   1 
ATOM   1486 C  CA  . SER   A 1 190 ? -15.601 -23.283 11.417 1.00 22.89 ? 190 SER   B CA  1 
ATOM   1487 C  C   . SER   A 1 190 ? -14.941 -22.225 12.308 1.00 21.09 ? 190 SER   B C   1 
ATOM   1488 O  O   . SER   A 1 190 ? -14.520 -21.171 11.792 1.00 19.92 ? 190 SER   B O   1 
ATOM   1489 C  CB  . SER   A 1 190 ? -14.559 -24.055 10.659 1.00 23.91 ? 190 SER   B CB  1 
ATOM   1490 O  OG  . SER   A 1 190 ? -13.579 -24.575 11.553 1.00 23.28 ? 190 SER   B OG  1 
ATOM   1491 N  N   . TRP   A 1 191 ? -14.896 -22.502 13.622 1.00 17.93 ? 191 TRP   B N   1 
ATOM   1492 C  CA  . TRP   A 1 191 ? -14.193 -21.605 14.530 1.00 17.27 ? 191 TRP   B CA  1 
ATOM   1493 C  C   . TRP   A 1 191 ? -12.830 -22.158 14.963 1.00 17.58 ? 191 TRP   B C   1 
ATOM   1494 O  O   . TRP   A 1 191 ? -12.336 -21.741 16.009 1.00 16.50 ? 191 TRP   B O   1 
ATOM   1495 C  CB  . TRP   A 1 191 ? -15.075 -21.220 15.737 1.00 17.77 ? 191 TRP   B CB  1 
ATOM   1496 C  CG  . TRP   A 1 191 ? -16.341 -20.483 15.378 1.00 19.11 ? 191 TRP   B CG  1 
ATOM   1497 C  CD1 . TRP   A 1 191 ? -16.659 -19.876 14.183 1.00 22.17 ? 191 TRP   B CD1 1 
ATOM   1498 C  CD2 . TRP   A 1 191 ? -17.446 -20.242 16.258 1.00 20.28 ? 191 TRP   B CD2 1 
ATOM   1499 N  NE1 . TRP   A 1 191 ? -17.902 -19.291 14.274 1.00 22.20 ? 191 TRP   B NE1 1 
ATOM   1500 C  CE2 . TRP   A 1 191 ? -18.399 -19.482 15.541 1.00 21.20 ? 191 TRP   B CE2 1 
ATOM   1501 C  CE3 . TRP   A 1 191 ? -17.695 -20.561 17.597 1.00 22.62 ? 191 TRP   B CE3 1 
ATOM   1502 C  CZ2 . TRP   A 1 191 ? -19.594 -19.056 16.124 1.00 22.99 ? 191 TRP   B CZ2 1 
ATOM   1503 C  CZ3 . TRP   A 1 191 ? -18.897 -20.161 18.168 1.00 23.48 ? 191 TRP   B CZ3 1 
ATOM   1504 C  CH2 . TRP   A 1 191 ? -19.830 -19.411 17.435 1.00 25.02 ? 191 TRP   B CH2 1 
ATOM   1505 N  N   . ASP   A 1 192 ? -12.175 -22.996 14.145 1.00 19.06 ? 192 ASP   B N   1 
ATOM   1506 C  CA  . ASP   A 1 192 ? -10.784 -23.428 14.363 1.00 18.81 ? 192 ASP   B CA  1 
ATOM   1507 C  C   . ASP   A 1 192 ? -9.849  -22.208 14.293 1.00 18.76 ? 192 ASP   B C   1 
ATOM   1508 O  O   . ASP   A 1 192 ? -10.055 -21.303 13.454 1.00 17.74 ? 192 ASP   B O   1 
ATOM   1509 C  CB  . ASP   A 1 192 ? -10.352 -24.438 13.312 1.00 21.09 ? 192 ASP   B CB  1 
ATOM   1510 C  CG  . ASP   A 1 192 ? -10.959 -25.854 13.432 1.00 29.06 ? 192 ASP   B CG  1 
ATOM   1511 O  OD1 . ASP   A 1 192 ? -11.663 -26.134 14.417 1.00 32.60 ? 192 ASP   B OD1 1 
ATOM   1512 O  OD2 . ASP   A 1 192 ? -10.673 -26.676 12.553 1.00 35.89 ? 192 ASP   B OD2 1 
ATOM   1513 N  N   . TYR   A 1 193 ? -8.811  -22.179 15.144 1.00 15.23 ? 193 TYR   B N   1 
ATOM   1514 C  CA  . TYR   A 1 193 ? -8.051  -20.931 15.214 1.00 14.39 ? 193 TYR   B CA  1 
ATOM   1515 C  C   . TYR   A 1 193 ? -6.591  -21.204 15.574 1.00 16.04 ? 193 TYR   B C   1 
ATOM   1516 O  O   . TYR   A 1 193 ? -6.263  -22.280 16.099 1.00 17.94 ? 193 TYR   B O   1 
ATOM   1517 C  CB  . TYR   A 1 193 ? -8.690  -20.028 16.287 1.00 13.68 ? 193 TYR   B CB  1 
ATOM   1518 C  CG  . TYR   A 1 193 ? -8.652  -20.576 17.690 1.00 13.99 ? 193 TYR   B CG  1 
ATOM   1519 C  CD1 . TYR   A 1 193 ? -7.544  -20.373 18.532 1.00 14.98 ? 193 TYR   B CD1 1 
ATOM   1520 C  CD2 . TYR   A 1 193 ? -9.734  -21.310 18.192 1.00 14.02 ? 193 TYR   B CD2 1 
ATOM   1521 C  CE1 . TYR   A 1 193 ? -7.522  -20.915 19.811 1.00 15.03 ? 193 TYR   B CE1 1 
ATOM   1522 C  CE2 . TYR   A 1 193 ? -9.706  -21.862 19.469 1.00 14.64 ? 193 TYR   B CE2 1 
ATOM   1523 C  CZ  . TYR   A 1 193 ? -8.592  -21.661 20.282 1.00 15.97 ? 193 TYR   B CZ  1 
ATOM   1524 O  OH  . TYR   A 1 193 ? -8.558  -22.156 21.566 1.00 16.17 ? 193 TYR   B OH  1 
ATOM   1525 N  N   . TRP   A 1 194 ? -5.746  -20.185 15.315 1.00 13.79 ? 194 TRP   B N   1 
ATOM   1526 C  CA  . TRP   A 1 194 ? -4.412  -20.102 15.889 1.00 13.29 ? 194 TRP   B CA  1 
ATOM   1527 C  C   . TRP   A 1 194 ? -4.393  -19.013 16.966 1.00 13.71 ? 194 TRP   B C   1 
ATOM   1528 O  O   . TRP   A 1 194 ? -5.142  -18.041 16.876 1.00 13.56 ? 194 TRP   B O   1 
ATOM   1529 C  CB  . TRP   A 1 194 ? -3.399  -19.721 14.775 1.00 13.58 ? 194 TRP   B CB  1 
ATOM   1530 C  CG  . TRP   A 1 194 ? -3.341  -20.731 13.667 1.00 14.20 ? 194 TRP   B CG  1 
ATOM   1531 C  CD1 . TRP   A 1 194 ? -2.728  -21.967 13.706 1.00 15.23 ? 194 TRP   B CD1 1 
ATOM   1532 C  CD2 . TRP   A 1 194 ? -3.771  -20.549 12.306 1.00 14.72 ? 194 TRP   B CD2 1 
ATOM   1533 N  NE1 . TRP   A 1 194 ? -2.805  -22.573 12.489 1.00 17.54 ? 194 TRP   B NE1 1 
ATOM   1534 C  CE2 . TRP   A 1 194 ? -3.475  -21.749 11.610 1.00 14.46 ? 194 TRP   B CE2 1 
ATOM   1535 C  CE3 . TRP   A 1 194 ? -4.475  -19.536 11.640 1.00 14.28 ? 194 TRP   B CE3 1 
ATOM   1536 C  CZ2 . TRP   A 1 194 ? -3.791  -21.937 10.264 1.00 16.85 ? 194 TRP   B CZ2 1 
ATOM   1537 C  CZ3 . TRP   A 1 194 ? -4.760  -19.713 10.298 1.00 13.58 ? 194 TRP   B CZ3 1 
ATOM   1538 C  CH2 . TRP   A 1 194 ? -4.405  -20.880 9.608  1.00 15.72 ? 194 TRP   B CH2 1 
ATOM   1539 N  N   . THR   A 1 195 ? -3.466  -19.076 17.929 1.00 11.99 ? 195 THR   B N   1 
ATOM   1540 C  CA  . THR   A 1 195 ? -3.386  -18.003 18.912 1.00 12.04 ? 195 THR   B CA  1 
ATOM   1541 C  C   . THR   A 1 195 ? -1.928  -17.742 19.302 1.00 12.52 ? 195 THR   B C   1 
ATOM   1542 O  O   . THR   A 1 195 ? -1.117  -18.678 19.336 1.00 12.18 ? 195 THR   B O   1 
ATOM   1543 C  CB  . THR   A 1 195 ? -4.235  -18.325 20.154 1.00 12.78 ? 195 THR   B CB  1 
ATOM   1544 O  OG1 . THR   A 1 195 ? -4.209  -17.273 21.103 1.00 13.69 ? 195 THR   B OG1 1 
ATOM   1545 C  CG2 . THR   A 1 195 ? -3.796  -19.641 20.795 1.00 12.85 ? 195 THR   B CG2 1 
ATOM   1546 N  N   . TYR   A 1 196 ? -1.645  -16.488 19.661 1.00 11.87 ? 196 TYR   B N   1 
ATOM   1547 C  CA  . TYR   A 1 196 ? -0.342  -16.095 20.185 1.00 12.21 ? 196 TYR   B CA  1 
ATOM   1548 C  C   . TYR   A 1 196 ? -0.517  -14.781 20.931 1.00 11.76 ? 196 TYR   B C   1 
ATOM   1549 O  O   . TYR   A 1 196 ? -1.499  -14.028 20.725 1.00 12.39 ? 196 TYR   B O   1 
ATOM   1550 C  CB  . TYR   A 1 196 ? 0.639   -15.993 19.003 1.00 12.12 ? 196 TYR   B CB  1 
ATOM   1551 C  CG  . TYR   A 1 196 ? 0.433   -14.775 18.150 1.00 13.16 ? 196 TYR   B CG  1 
ATOM   1552 C  CD1 . TYR   A 1 196 ? -0.484  -14.788 17.113 1.00 13.46 ? 196 TYR   B CD1 1 
ATOM   1553 C  CD2 . TYR   A 1 196 ? 1.197   -13.623 18.358 1.00 12.07 ? 196 TYR   B CD2 1 
ATOM   1554 C  CE1 . TYR   A 1 196 ? -0.712  -13.641 16.345 1.00 13.68 ? 196 TYR   B CE1 1 
ATOM   1555 C  CE2 . TYR   A 1 196 ? 0.999   -12.487 17.590 1.00 12.85 ? 196 TYR   B CE2 1 
ATOM   1556 C  CZ  . TYR   A 1 196 ? 0.039   -12.500 16.587 1.00 13.11 ? 196 TYR   B CZ  1 
ATOM   1557 O  OH  . TYR   A 1 196 ? -0.132  -11.368 15.834 1.00 12.52 ? 196 TYR   B OH  1 
ATOM   1558 N  N   . PRO   A 1 197 ? 0.428   -14.423 21.830 1.00 12.49 ? 197 PRO   B N   1 
ATOM   1559 C  CA  . PRO   A 1 197 ? 0.404   -13.132 22.504 1.00 12.66 ? 197 PRO   B CA  1 
ATOM   1560 C  C   . PRO   A 1 197 ? 1.021   -12.071 21.608 1.00 13.35 ? 197 PRO   B C   1 
ATOM   1561 O  O   . PRO   A 1 197 ? 2.141   -12.268 21.096 1.00 13.46 ? 197 PRO   B O   1 
ATOM   1562 C  CB  . PRO   A 1 197 ? 1.314   -13.349 23.746 1.00 13.35 ? 197 PRO   B CB  1 
ATOM   1563 C  CG  . PRO   A 1 197 ? 2.234   -14.441 23.333 1.00 14.52 ? 197 PRO   B CG  1 
ATOM   1564 C  CD  . PRO   A 1 197 ? 1.515   -15.309 22.314 1.00 15.11 ? 197 PRO   B CD  1 
ATOM   1565 N  N   . GLY   A 1 198 ? 0.298   -10.954 21.489 1.00 13.14 ? 198 GLY   B N   1 
ATOM   1566 C  CA  . GLY   A 1 198 ? 0.833   -9.887  20.635 1.00 13.57 ? 198 GLY   B CA  1 
ATOM   1567 C  C   . GLY   A 1 198 ? 0.372   -8.504  21.048 1.00 13.63 ? 198 GLY   B C   1 
ATOM   1568 O  O   . GLY   A 1 198 ? 0.211   -8.196  22.230 1.00 12.66 ? 198 GLY   B O   1 
ATOM   1569 N  N   . SER   A 1 199 ? 0.158   -7.654  20.007 1.00 12.81 ? 199 SER   B N   1 
ATOM   1570 C  CA  . SER   A 1 199 ? -0.032  -6.238  20.280 1.00 12.65 ? 199 SER   B CA  1 
ATOM   1571 C  C   . SER   A 1 199 ? -1.164  -5.688  19.417 1.00 12.45 ? 199 SER   B C   1 
ATOM   1572 O  O   . SER   A 1 199 ? -1.616  -6.337  18.463 1.00 12.32 ? 199 SER   B O   1 
ATOM   1573 C  CB  . SER   A 1 199 ? 1.252   -5.441  19.935 1.00 13.28 ? 199 SER   B CB  1 
ATOM   1574 O  OG  . SER   A 1 199 ? 1.377   -5.363  18.503 1.00 14.05 ? 199 SER   B OG  1 
ATOM   1575 N  N   . LEU   A 1 200 ? -1.578  -4.462  19.759 1.00 11.02 ? 200 LEU   B N   1 
ATOM   1576 C  CA  . LEU   A 1 200 ? -2.340  -3.669  18.780 1.00 13.19 ? 200 LEU   B CA  1 
ATOM   1577 C  C   . LEU   A 1 200 ? -1.483  -3.534  17.521 1.00 13.95 ? 200 LEU   B C   1 
ATOM   1578 O  O   . LEU   A 1 200 ? -0.276  -3.373  17.604 1.00 12.15 ? 200 LEU   B O   1 
ATOM   1579 C  CB  . LEU   A 1 200 ? -2.661  -2.273  19.338 1.00 13.55 ? 200 LEU   B CB  1 
ATOM   1580 C  CG  . LEU   A 1 200 ? -3.457  -2.277  20.660 1.00 16.22 ? 200 LEU   B CG  1 
ATOM   1581 C  CD1 . LEU   A 1 200 ? -3.641  -0.834  21.113 1.00 19.22 ? 200 LEU   B CD1 1 
ATOM   1582 C  CD2 . LEU   A 1 200 ? -4.828  -2.922  20.482 1.00 17.07 ? 200 LEU   B CD2 1 
ATOM   1583 N  N   . THR   A 1 201 ? -2.143  -3.429  16.368 1.00 13.27 ? 201 THR   B N   1 
ATOM   1584 C  CA  . THR   A 1 201 ? -1.379  -3.253  15.123 1.00 12.16 ? 201 THR   B CA  1 
ATOM   1585 C  C   . THR   A 1 201 ? -1.401  -1.808  14.635 1.00 12.96 ? 201 THR   B C   1 
ATOM   1586 O  O   . THR   A 1 201 ? -0.879  -1.538  13.534 1.00 13.68 ? 201 THR   B O   1 
ATOM   1587 C  CB  . THR   A 1 201 ? -1.805  -4.155  13.967 1.00 13.37 ? 201 THR   B CB  1 
ATOM   1588 O  OG1 . THR   A 1 201 ? -3.117  -3.770  13.487 1.00 12.20 ? 201 THR   B OG1 1 
ATOM   1589 C  CG2 . THR   A 1 201 ? -1.772  -5.632  14.346 1.00 13.41 ? 201 THR   B CG2 1 
ATOM   1590 N  N   . VAL   A 1 202 ? -1.916  -0.917  15.476 1.00 13.48 ? 202 VAL   B N   1 
ATOM   1591 C  CA  . VAL   A 1 202 ? -1.825  0.519   15.210 1.00 14.05 ? 202 VAL   B CA  1 
ATOM   1592 C  C   . VAL   A 1 202 ? -1.282  1.201   16.465 1.00 14.65 ? 202 VAL   B C   1 
ATOM   1593 O  O   . VAL   A 1 202 ? -1.456  0.713   17.579 1.00 15.39 ? 202 VAL   B O   1 
ATOM   1594 C  CB  . VAL   A 1 202 ? -3.203  1.103   14.862 1.00 15.37 ? 202 VAL   B CB  1 
ATOM   1595 C  CG1 . VAL   A 1 202 ? -3.717  0.652   13.505 1.00 16.06 ? 202 VAL   B CG1 1 
ATOM   1596 C  CG2 . VAL   A 1 202 ? -4.248  0.917   15.984 1.00 17.40 ? 202 VAL   B CG2 1 
ATOM   1597 N  N   . PRO   A 1 203 ? -0.665  2.397   16.372 1.00 15.85 ? 203 PRO   B N   1 
ATOM   1598 C  CA  . PRO   A 1 203 ? -0.339  3.144   17.589 1.00 15.72 ? 203 PRO   B CA  1 
ATOM   1599 C  C   . PRO   A 1 203 ? -1.553  3.222   18.504 1.00 15.00 ? 203 PRO   B C   1 
ATOM   1600 O  O   . PRO   A 1 203 ? -2.659  3.490   18.026 1.00 18.54 ? 203 PRO   B O   1 
ATOM   1601 C  CB  . PRO   A 1 203 ? 0.030   4.530   16.973 1.00 16.72 ? 203 PRO   B CB  1 
ATOM   1602 C  CG  . PRO   A 1 203 ? 0.603   4.186   15.646 1.00 15.02 ? 203 PRO   B CG  1 
ATOM   1603 C  CD  . PRO   A 1 203 ? -0.310  3.088   15.112 1.00 13.07 ? 203 PRO   B CD  1 
ATOM   1604 N  N   . PRO   A 1 204 ? -1.415  3.063   19.854 1.00 17.03 ? 204 PRO   B N   1 
ATOM   1605 C  CA  . PRO   A 1 204 ? -0.124  2.959   20.528 1.00 18.17 ? 204 PRO   B CA  1 
ATOM   1606 C  C   . PRO   A 1 204 ? 0.633   1.623   20.610 1.00 17.72 ? 204 PRO   B C   1 
ATOM   1607 O  O   . PRO   A 1 204 ? 1.591   1.515   21.368 1.00 19.72 ? 204 PRO   B O   1 
ATOM   1608 C  CB  . PRO   A 1 204 ? -0.505  3.418   21.962 1.00 19.87 ? 204 PRO   B CB  1 
ATOM   1609 C  CG  . PRO   A 1 204 ? -1.904  2.868   22.160 1.00 21.56 ? 204 PRO   B CG  1 
ATOM   1610 C  CD  . PRO   A 1 204 ? -2.550  3.125   20.816 1.00 19.01 ? 204 PRO   B CD  1 
ATOM   1611 N  N   . LEU   A 1 205 ? 0.197   0.589   19.841 1.00 16.81 ? 205 LEU   B N   1 
ATOM   1612 C  CA  . LEU   A 1 205 ? 0.962   -0.643  19.655 1.00 14.35 ? 205 LEU   B CA  1 
ATOM   1613 C  C   . LEU   A 1 205 ? 1.143   -1.429  20.968 1.00 14.11 ? 205 LEU   B C   1 
ATOM   1614 O  O   . LEU   A 1 205 ? 2.111   -2.175  21.100 1.00 14.96 ? 205 LEU   B O   1 
ATOM   1615 C  CB  . LEU   A 1 205 ? 2.311   -0.345  18.974 1.00 16.37 ? 205 LEU   B CB  1 
ATOM   1616 C  CG  . LEU   A 1 205 ? 2.153   0.260   17.569 1.00 17.86 ? 205 LEU   B CG  1 
ATOM   1617 C  CD1 . LEU   A 1 205 ? 3.503   0.810   17.086 1.00 19.70 ? 205 LEU   B CD1 1 
ATOM   1618 C  CD2 . LEU   A 1 205 ? 1.620   -0.782  16.603 1.00 16.52 ? 205 LEU   B CD2 1 
ATOM   1619 N  N   . LEU   A 1 206 ? 0.174   -1.269  21.894 1.00 13.65 ? 206 LEU   B N   1 
ATOM   1620 C  CA  . LEU   A 1 206 ? 0.290   -1.824  23.252 1.00 13.91 ? 206 LEU   B CA  1 
ATOM   1621 C  C   . LEU   A 1 206 ? 0.337   -3.353  23.187 1.00 14.46 ? 206 LEU   B C   1 
ATOM   1622 O  O   . LEU   A 1 206 ? -0.430  -3.989  22.461 1.00 15.26 ? 206 LEU   B O   1 
ATOM   1623 C  CB  . LEU   A 1 206 ? -0.873  -1.299  24.115 1.00 17.23 ? 206 LEU   B CB  1 
ATOM   1624 C  CG  . LEU   A 1 206 ? -0.884  0.218   24.344 1.00 15.96 ? 206 LEU   B CG  1 
ATOM   1625 C  CD1 . LEU   A 1 206 ? -2.219  0.666   24.926 1.00 20.39 ? 206 LEU   B CD1 1 
ATOM   1626 C  CD2 . LEU   A 1 206 ? 0.278   0.606   25.251 1.00 22.08 ? 206 LEU   B CD2 1 
ATOM   1627 N  N   . GLU   A 1 207 ? 1.207   -3.997  23.978 1.00 14.63 ? 207 GLU   B N   1 
ATOM   1628 C  CA  . GLU   A 1 207 ? 1.370   -5.446  24.037 1.00 14.28 ? 207 GLU   B CA  1 
ATOM   1629 C  C   . GLU   A 1 207 ? 0.378   -6.079  25.031 1.00 15.37 ? 207 GLU   B C   1 
ATOM   1630 O  O   . GLU   A 1 207 ? 0.752   -6.633  26.088 1.00 16.83 ? 207 GLU   B O   1 
ATOM   1631 C  CB  . GLU   A 1 207 ? 2.844   -5.752  24.321 1.00 14.88 ? 207 GLU   B CB  1 
ATOM   1632 C  CG  . GLU   A 1 207 ? 3.736   -5.285  23.150 1.00 15.87 ? 207 GLU   B CG  1 
ATOM   1633 C  CD  . GLU   A 1 207 ? 5.219   -5.629  23.199 1.00 19.69 ? 207 GLU   B CD  1 
ATOM   1634 O  OE1 . GLU   A 1 207 ? 5.728   -5.921  24.327 1.00 21.69 ? 207 GLU   B OE1 1 
ATOM   1635 O  OE2 . GLU   A 1 207 ? 5.892   -5.567  22.141 1.00 17.52 ? 207 GLU   B OE2 1 
ATOM   1636 N  N   . SER   A 1 208 ? -0.901  -5.939  24.722 1.00 15.31 ? 208 SER   B N   1 
ATOM   1637 C  CA  . SER   A 1 208 ? -1.991  -6.341  25.616 1.00 13.77 ? 208 SER   B CA  1 
ATOM   1638 C  C   . SER   A 1 208 ? -2.946  -7.338  24.940 1.00 15.55 ? 208 SER   B C   1 
ATOM   1639 O  O   . SER   A 1 208 ? -4.043  -7.552  25.475 1.00 14.42 ? 208 SER   B O   1 
ATOM   1640 C  CB  . SER   A 1 208 ? -2.745  -5.079  26.023 1.00 17.09 ? 208 SER   B CB  1 
ATOM   1641 O  OG  . SER   A 1 208 ? -3.157  -4.328  24.874 1.00 19.30 ? 208 SER   B OG  1 
ATOM   1642 N  N   . VAL   A 1 209 ? -2.572  -7.911  23.778 1.00 12.31 ? 209 VAL   B N   1 
ATOM   1643 C  CA  . VAL   A 1 209 ? -3.568  -8.604  22.961 1.00 11.35 ? 209 VAL   B CA  1 
ATOM   1644 C  C   . VAL   A 1 209 ? -3.309  -10.103 22.937 1.00 11.43 ? 209 VAL   B C   1 
ATOM   1645 O  O   . VAL   A 1 209 ? -2.222  -10.550 22.539 1.00 13.73 ? 209 VAL   B O   1 
ATOM   1646 C  CB  . VAL   A 1 209 ? -3.633  -8.063  21.510 1.00 11.21 ? 209 VAL   B CB  1 
ATOM   1647 C  CG1 . VAL   A 1 209 ? -4.664  -8.840  20.679 1.00 12.74 ? 209 VAL   B CG1 1 
ATOM   1648 C  CG2 . VAL   A 1 209 ? -3.968  -6.566  21.511 1.00 13.40 ? 209 VAL   B CG2 1 
ATOM   1649 N  N   . THR   A 1 210 ? -4.351  -10.873 23.263 1.00 10.10 ? 210 THR   B N   1 
ATOM   1650 C  CA  . THR   A 1 210 ? -4.347  -12.283 22.929 1.00 10.81 ? 210 THR   B CA  1 
ATOM   1651 C  C   . THR   A 1 210 ? -5.000  -12.405 21.548 1.00 11.81 ? 210 THR   B C   1 
ATOM   1652 O  O   . THR   A 1 210 ? -6.203  -12.127 21.378 1.00 11.99 ? 210 THR   B O   1 
ATOM   1653 C  CB  . THR   A 1 210 ? -5.147  -13.093 23.962 1.00 12.35 ? 210 THR   B CB  1 
ATOM   1654 O  OG1 . THR   A 1 210 ? -4.547  -13.023 25.262 1.00 13.88 ? 210 THR   B OG1 1 
ATOM   1655 C  CG2 . THR   A 1 210 ? -5.128  -14.550 23.576 1.00 13.56 ? 210 THR   B CG2 1 
ATOM   1656 N  N   . TRP   A 1 211 ? -4.183  -12.770 20.540 1.00 10.13 ? 211 TRP   B N   1 
ATOM   1657 C  CA  . TRP   A 1 211 ? -4.695  -12.891 19.176 1.00 10.87 ? 211 TRP   B CA  1 
ATOM   1658 C  C   . TRP   A 1 211 ? -5.331  -14.255 18.938 1.00 12.92 ? 211 TRP   B C   1 
ATOM   1659 O  O   . TRP   A 1 211 ? -4.769  -15.258 19.356 1.00 12.19 ? 211 TRP   B O   1 
ATOM   1660 C  CB  . TRP   A 1 211 ? -3.551  -12.687 18.164 1.00 11.79 ? 211 TRP   B CB  1 
ATOM   1661 C  CG  . TRP   A 1 211 ? -3.335  -11.219 17.947 1.00 11.48 ? 211 TRP   B CG  1 
ATOM   1662 C  CD1 . TRP   A 1 211 ? -2.392  -10.424 18.540 1.00 12.48 ? 211 TRP   B CD1 1 
ATOM   1663 C  CD2 . TRP   A 1 211 ? -4.086  -10.369 17.058 1.00 11.26 ? 211 TRP   B CD2 1 
ATOM   1664 N  NE1 . TRP   A 1 211 ? -2.544  -9.128  18.117 1.00 13.32 ? 211 TRP   B NE1 1 
ATOM   1665 C  CE2 . TRP   A 1 211 ? -3.576  -9.060  17.227 1.00 12.06 ? 211 TRP   B CE2 1 
ATOM   1666 C  CE3 . TRP   A 1 211 ? -5.195  -10.575 16.213 1.00 11.95 ? 211 TRP   B CE3 1 
ATOM   1667 C  CZ2 . TRP   A 1 211 ? -4.084  -7.976  16.515 1.00 12.02 ? 211 TRP   B CZ2 1 
ATOM   1668 C  CZ3 . TRP   A 1 211 ? -5.701  -9.519  15.480 1.00 11.88 ? 211 TRP   B CZ3 1 
ATOM   1669 C  CH2 . TRP   A 1 211 ? -5.159  -8.237  15.667 1.00 12.23 ? 211 TRP   B CH2 1 
ATOM   1670 N  N   . ILE   A 1 212 ? -6.554  -14.250 18.349 1.00 10.41 ? 212 ILE   B N   1 
ATOM   1671 C  CA  . ILE   A 1 212 ? -7.199  -15.503 17.962 1.00 10.50 ? 212 ILE   B CA  1 
ATOM   1672 C  C   . ILE   A 1 212 ? -7.507  -15.315 16.483 1.00 12.02 ? 212 ILE   B C   1 
ATOM   1673 O  O   . ILE   A 1 212 ? -8.403  -14.555 16.125 1.00 11.48 ? 212 ILE   B O   1 
ATOM   1674 C  CB  . ILE   A 1 212 ? -8.490  -15.639 18.806 1.00 11.82 ? 212 ILE   B CB  1 
ATOM   1675 C  CG1 . ILE   A 1 212 ? -8.136  -15.749 20.293 1.00 13.50 ? 212 ILE   B CG1 1 
ATOM   1676 C  CG2 . ILE   A 1 212 ? -9.333  -16.842 18.324 1.00 12.88 ? 212 ILE   B CG2 1 
ATOM   1677 C  CD1 . ILE   A 1 212 ? -9.332  -15.562 21.217 1.00 16.14 ? 212 ILE   B CD1 1 
ATOM   1678 N  N   . VAL   A 1 213 ? -6.751  -15.993 15.622 1.00 11.36 ? 213 VAL   B N   1 
ATOM   1679 C  CA  . VAL   A 1 213 ? -6.910  -15.819 14.179 1.00 11.74 ? 213 VAL   B CA  1 
ATOM   1680 C  C   . VAL   A 1 213 ? -7.606  -17.052 13.607 1.00 13.14 ? 213 VAL   B C   1 
ATOM   1681 O  O   . VAL   A 1 213 ? -7.120  -18.187 13.749 1.00 13.61 ? 213 VAL   B O   1 
ATOM   1682 C  CB  . VAL   A 1 213 ? -5.506  -15.664 13.576 1.00 12.08 ? 213 VAL   B CB  1 
ATOM   1683 C  CG1 . VAL   A 1 213 ? -5.580  -15.584 12.030 1.00 12.66 ? 213 VAL   B CG1 1 
ATOM   1684 C  CG2 . VAL   A 1 213 ? -4.763  -14.410 14.076 1.00 13.03 ? 213 VAL   B CG2 1 
ATOM   1685 N  N   . LEU   A 1 214 ? -8.814  -16.847 13.032 1.00 12.69 ? 214 LEU   B N   1 
ATOM   1686 C  CA  . LEU   A 1 214 ? -9.529  -18.006 12.510 1.00 14.43 ? 214 LEU   B CA  1 
ATOM   1687 C  C   . LEU   A 1 214 ? -8.888  -18.488 11.206 1.00 13.99 ? 214 LEU   B C   1 
ATOM   1688 O  O   . LEU   A 1 214 ? -8.510  -17.743 10.306 1.00 14.22 ? 214 LEU   B O   1 
ATOM   1689 C  CB  . LEU   A 1 214 ? -10.996 -17.609 12.254 1.00 13.16 ? 214 LEU   B CB  1 
ATOM   1690 C  CG  . LEU   A 1 214 ? -11.756 -17.067 13.477 1.00 16.09 ? 214 LEU   B CG  1 
ATOM   1691 C  CD1 . LEU   A 1 214 ? -13.246 -16.894 13.140 1.00 18.57 ? 214 LEU   B CD1 1 
ATOM   1692 C  CD2 . LEU   A 1 214 ? -11.635 -18.001 14.657 1.00 18.12 ? 214 LEU   B CD2 1 
ATOM   1693 N  N   . LYS   A 1 215 ? -8.834  -19.820 11.049 1.00 14.18 ? 215 LYS   B N   1 
ATOM   1694 C  CA  . LYS   A 1 215 ? -8.270  -20.413 9.864  1.00 15.07 ? 215 LYS   B CA  1 
ATOM   1695 C  C   . LYS   A 1 215 ? -9.125  -20.215 8.598  1.00 16.49 ? 215 LYS   B C   1 
ATOM   1696 O  O   . LYS   A 1 215 ? -8.560  -20.049 7.537  1.00 18.22 ? 215 LYS   B O   1 
ATOM   1697 C  CB  . LYS   A 1 215 ? -8.178  -21.927 10.121 1.00 18.46 ? 215 LYS   B CB  1 
ATOM   1698 C  CG  . LYS   A 1 215 ? -7.748  -22.705 8.898  1.00 23.54 ? 215 LYS   B CG  1 
ATOM   1699 C  CD  . LYS   A 1 215 ? -7.505  -24.193 9.136  1.00 29.84 ? 215 LYS   B CD  1 
ATOM   1700 C  CE  . LYS   A 1 215 ? -6.959  -24.826 7.861  1.00 33.35 ? 215 LYS   B CE  1 
ATOM   1701 N  NZ  . LYS   A 1 215 ? -6.373  -26.172 8.113  1.00 39.00 ? 215 LYS   B NZ  1 
ATOM   1702 N  N   . GLN   A 1 216 ? -10.438 -20.323 8.718  1.00 16.33 ? 216 GLN   B N   1 
ATOM   1703 C  CA  . GLN   A 1 216 ? -11.339 -20.313 7.561  1.00 15.47 ? 216 GLN   B CA  1 
ATOM   1704 C  C   . GLN   A 1 216 ? -11.660 -18.886 7.134  1.00 15.35 ? 216 GLN   B C   1 
ATOM   1705 O  O   . GLN   A 1 216 ? -12.191 -18.122 7.918  1.00 15.39 ? 216 GLN   B O   1 
ATOM   1706 C  CB  . GLN   A 1 216 ? -12.652 -21.010 7.898  1.00 19.23 ? 216 GLN   B CB  1 
ATOM   1707 C  CG  . GLN   A 1 216 ? -13.510 -21.129 6.628  1.00 20.93 ? 216 GLN   B CG  1 
ATOM   1708 C  CD  . GLN   A 1 216 ? -14.683 -22.082 6.694  1.00 26.45 ? 216 GLN   B CD  1 
ATOM   1709 O  OE1 . GLN   A 1 216 ? -15.221 -22.460 5.649  1.00 36.32 ? 216 GLN   B OE1 1 
ATOM   1710 N  NE2 . GLN   A 1 216 ? -15.132 -22.419 7.892  1.00 25.93 ? 216 GLN   B NE2 1 
ATOM   1711 N  N   A PRO   A 1 217 ? -11.286 -18.454 5.912  0.50 15.08 ? 217 PRO   B N   1 
ATOM   1712 N  N   B PRO   A 1 217 ? -11.430 -18.503 5.865  0.50 15.46 ? 217 PRO   B N   1 
ATOM   1713 C  CA  A PRO   A 1 217 ? -11.641 -17.110 5.417  0.50 15.20 ? 217 PRO   B CA  1 
ATOM   1714 C  CA  B PRO   A 1 217 ? -11.801 -17.157 5.441  0.50 15.33 ? 217 PRO   B CA  1 
ATOM   1715 C  C   A PRO   A 1 217 ? -13.094 -16.998 4.934  0.50 15.51 ? 217 PRO   B C   1 
ATOM   1716 C  C   B PRO   A 1 217 ? -13.297 -17.022 5.159  0.50 14.59 ? 217 PRO   B C   1 
ATOM   1717 O  O   A PRO   A 1 217 ? -13.672 -18.028 4.564  0.50 16.73 ? 217 PRO   B O   1 
ATOM   1718 O  O   B PRO   A 1 217 ? -14.091 -17.986 5.101  0.50 12.52 ? 217 PRO   B O   1 
ATOM   1719 C  CB  A PRO   A 1 217 ? -10.742 -16.913 4.180  0.50 15.70 ? 217 PRO   B CB  1 
ATOM   1720 C  CB  B PRO   A 1 217 ? -11.028 -16.979 4.125  0.50 16.59 ? 217 PRO   B CB  1 
ATOM   1721 C  CG  A PRO   A 1 217 ? -9.760  -18.076 4.194  0.50 14.89 ? 217 PRO   B CG  1 
ATOM   1722 C  CG  B PRO   A 1 217 ? -10.986 -18.379 3.569  0.50 17.94 ? 217 PRO   B CG  1 
ATOM   1723 C  CD  A PRO   A 1 217 ? -10.393 -19.180 5.003  0.50 15.90 ? 217 PRO   B CD  1 
ATOM   1724 C  CD  B PRO   A 1 217 ? -10.827 -19.284 4.776  0.50 17.10 ? 217 PRO   B CD  1 
ATOM   1725 N  N   . ILE   A 1 218 ? -13.668 -15.764 4.957  1.00 14.00 ? 218 ILE   B N   1 
ATOM   1726 C  CA  . ILE   A 1 218 ? -15.005 -15.459 4.439  1.00 13.59 ? 218 ILE   B CA  1 
ATOM   1727 C  C   . ILE   A 1 218 ? -14.814 -14.728 3.100  1.00 14.19 ? 218 ILE   B C   1 
ATOM   1728 O  O   . ILE   A 1 218 ? -13.684 -14.405 2.713  1.00 16.25 ? 218 ILE   B O   1 
ATOM   1729 C  CB  . ILE   A 1 218 ? -15.825 -14.620 5.439  1.00 14.64 ? 218 ILE   B CB  1 
ATOM   1730 C  CG1 . ILE   A 1 218 ? -15.233 -13.217 5.652  1.00 15.04 ? 218 ILE   B CG1 1 
ATOM   1731 C  CG2 . ILE   A 1 218 ? -15.988 -15.369 6.754  1.00 14.86 ? 218 ILE   B CG2 1 
ATOM   1732 C  CD1 . ILE   A 1 218 ? -16.121 -12.280 6.481  1.00 17.29 ? 218 ILE   B CD1 1 
ATOM   1733 N  N   . ASN   A 1 219 ? -15.922 -14.590 2.349  1.00 14.76 ? 219 ASN   B N   1 
ATOM   1734 C  CA  . ASN   A 1 219 ? -15.769 -13.998 1.020  1.00 15.28 ? 219 ASN   B CA  1 
ATOM   1735 C  C   . ASN   A 1 219 ? -16.064 -12.499 1.005  1.00 13.58 ? 219 ASN   B C   1 
ATOM   1736 O  O   . ASN   A 1 219 ? -16.789 -11.971 1.850  1.00 16.26 ? 219 ASN   B O   1 
ATOM   1737 C  CB  . ASN   A 1 219 ? -16.742 -14.690 0.055  1.00 18.67 ? 219 ASN   B CB  1 
ATOM   1738 C  CG  . ASN   A 1 219 ? -18.145 -14.729 0.636  1.00 25.02 ? 219 ASN   B CG  1 
ATOM   1739 O  OD1 . ASN   A 1 219 ? -18.354 -15.335 1.700  1.00 30.80 ? 219 ASN   B OD1 1 
ATOM   1740 N  ND2 . ASN   A 1 219 ? -19.108 -14.080 -0.042 1.00 27.04 ? 219 ASN   B ND2 1 
ATOM   1741 N  N   . ILE   A 1 220 ? -15.485 -11.799 0.003  1.00 13.62 ? 220 ILE   B N   1 
ATOM   1742 C  CA  . ILE   A 1 220 ? -15.864 -10.417 -0.318 1.00 14.30 ? 220 ILE   B CA  1 
ATOM   1743 C  C   . ILE   A 1 220 ? -15.695 -10.258 -1.832 1.00 14.28 ? 220 ILE   B C   1 
ATOM   1744 O  O   . ILE   A 1 220 ? -14.788 -10.865 -2.388 1.00 14.11 ? 220 ILE   B O   1 
ATOM   1745 C  CB  . ILE   A 1 220 ? -14.964 -9.372  0.413  1.00 13.81 ? 220 ILE   B CB  1 
ATOM   1746 C  CG1 . ILE   A 1 220 ? -15.462 -7.916  0.261  1.00 15.43 ? 220 ILE   B CG1 1 
ATOM   1747 C  CG2 . ILE   A 1 220 ? -13.482 -9.530  0.059  1.00 15.85 ? 220 ILE   B CG2 1 
ATOM   1748 C  CD1 . ILE   A 1 220 ? -14.891 -6.900  1.295  1.00 17.74 ? 220 ILE   B CD1 1 
ATOM   1749 N  N   . SER   A 1 221 ? -16.511 -9.403  -2.465 1.00 13.62 ? 221 SER   B N   1 
ATOM   1750 C  CA  . SER   A 1 221 ? -16.216 -9.106  -3.867 1.00 14.50 ? 221 SER   B CA  1 
ATOM   1751 C  C   . SER   A 1 221 ? -15.159 -7.994  -4.027 1.00 15.39 ? 221 SER   B C   1 
ATOM   1752 O  O   . SER   A 1 221 ? -14.983 -7.152  -3.140 1.00 13.93 ? 221 SER   B O   1 
ATOM   1753 C  CB  . SER   A 1 221 ? -17.482 -8.774  -4.615 1.00 14.77 ? 221 SER   B CB  1 
ATOM   1754 O  OG  . SER   A 1 221 ? -17.960 -7.469  -4.260 1.00 16.65 ? 221 SER   B OG  1 
ATOM   1755 N  N   A SER   A 1 222 ? -14.507 -7.955  -5.203 0.50 15.97 ? 222 SER   B N   1 
ATOM   1756 N  N   B SER   A 1 222 ? -14.510 -7.963  -5.210 0.50 17.18 ? 222 SER   B N   1 
ATOM   1757 C  CA  A SER   A 1 222 ? -13.564 -6.885  -5.488 0.50 14.97 ? 222 SER   B CA  1 
ATOM   1758 C  CA  B SER   A 1 222 ? -13.565 -6.900  -5.523 0.50 16.94 ? 222 SER   B CA  1 
ATOM   1759 C  C   A SER   A 1 222 ? -14.271 -5.527  -5.434 0.50 15.81 ? 222 SER   B C   1 
ATOM   1760 C  C   B SER   A 1 222 ? -14.257 -5.534  -5.472 0.50 17.03 ? 222 SER   B C   1 
ATOM   1761 O  O   A SER   A 1 222 ? -13.711 -4.552  -4.932 0.50 15.54 ? 222 SER   B O   1 
ATOM   1762 O  O   B SER   A 1 222 ? -13.666 -4.560  -5.008 0.50 16.65 ? 222 SER   B O   1 
ATOM   1763 C  CB  A SER   A 1 222 ? -12.882 -7.107  -6.815 0.50 14.17 ? 222 SER   B CB  1 
ATOM   1764 C  CB  B SER   A 1 222 ? -12.857 -7.126  -6.850 0.50 17.75 ? 222 SER   B CB  1 
ATOM   1765 O  OG  A SER   A 1 222 ? -13.864 -7.200  -7.835 0.50 13.94 ? 222 SER   B OG  1 
ATOM   1766 O  OG  B SER   A 1 222 ? -12.067 -8.309  -6.832 0.50 22.38 ? 222 SER   B OG  1 
ATOM   1767 N  N   . GLN   A 1 223 ? -15.524 -5.459  -5.922 1.00 15.76 ? 223 GLN   B N   1 
ATOM   1768 C  CA  . GLN   A 1 223 ? -16.254 -4.199  -5.883 1.00 14.90 ? 223 GLN   B CA  1 
ATOM   1769 C  C   . GLN   A 1 223 ? -16.528 -3.718  -4.454 1.00 15.13 ? 223 GLN   B C   1 
ATOM   1770 O  O   . GLN   A 1 223 ? -16.454 -2.511  -4.187 1.00 15.33 ? 223 GLN   B O   1 
ATOM   1771 C  CB  . GLN   A 1 223 ? -17.521 -4.279  -6.745 1.00 18.93 ? 223 GLN   B CB  1 
ATOM   1772 C  CG  . GLN   A 1 223 ? -17.218 -4.510  -8.228 1.00 22.48 ? 223 GLN   B CG  1 
ATOM   1773 C  CD  . GLN   A 1 223 ? -16.990 -5.938  -8.684 1.00 23.18 ? 223 GLN   B CD  1 
ATOM   1774 O  OE1 . GLN   A 1 223 ? -16.722 -6.186  -9.873 1.00 30.54 ? 223 GLN   B OE1 1 
ATOM   1775 N  NE2 . GLN   A 1 223 ? -17.075 -6.904  -7.784 1.00 19.98 ? 223 GLN   B NE2 1 
ATOM   1776 N  N   . GLN   A 1 224 ? -16.849 -4.659  -3.552 1.00 14.97 ? 224 GLN   B N   1 
ATOM   1777 C  CA  . GLN   A 1 224 ? -17.160 -4.324  -2.176 1.00 14.50 ? 224 GLN   B CA  1 
ATOM   1778 C  C   . GLN   A 1 224 ? -15.873 -3.784  -1.546 1.00 13.72 ? 224 GLN   B C   1 
ATOM   1779 O  O   . GLN   A 1 224 ? -15.861 -2.773  -0.872 1.00 15.57 ? 224 GLN   B O   1 
ATOM   1780 C  CB  . GLN   A 1 224 ? -17.602 -5.570  -1.397 1.00 14.35 ? 224 GLN   B CB  1 
ATOM   1781 C  CG  . GLN   A 1 224 ? -19.093 -5.838  -1.565 1.00 15.72 ? 224 GLN   B CG  1 
ATOM   1782 C  CD  . GLN   A 1 224 ? -19.550 -7.088  -0.853 1.00 16.86 ? 224 GLN   B CD  1 
ATOM   1783 O  OE1 . GLN   A 1 224 ? -18.917 -8.128  -0.918 1.00 16.04 ? 224 GLN   B OE1 1 
ATOM   1784 N  NE2 . GLN   A 1 224 ? -20.700 -6.984  -0.216 1.00 18.78 ? 224 GLN   B NE2 1 
ATOM   1785 N  N   . LEU   A 1 225 ? -14.754 -4.479  -1.780 1.00 14.30 ? 225 LEU   B N   1 
ATOM   1786 C  CA  . LEU   A 1 225 ? -13.516 -4.079  -1.135 1.00 13.44 ? 225 LEU   B CA  1 
ATOM   1787 C  C   . LEU   A 1 225 ? -13.053 -2.729  -1.675 1.00 14.14 ? 225 LEU   B C   1 
ATOM   1788 O  O   . LEU   A 1 225 ? -12.595 -1.864  -0.920 1.00 14.45 ? 225 LEU   B O   1 
ATOM   1789 C  CB  . LEU   A 1 225 ? -12.482 -5.189  -1.367 1.00 14.74 ? 225 LEU   B CB  1 
ATOM   1790 C  CG  . LEU   A 1 225 ? -11.115 -5.012  -0.692 1.00 16.16 ? 225 LEU   B CG  1 
ATOM   1791 C  CD1 . LEU   A 1 225 ? -11.270 -4.779  0.807  1.00 18.48 ? 225 LEU   B CD1 1 
ATOM   1792 C  CD2 . LEU   A 1 225 ? -10.324 -6.304  -0.917 1.00 17.39 ? 225 LEU   B CD2 1 
ATOM   1793 N  N   . ALA   A 1 226 ? -13.192 -2.486  -3.003 1.00 14.10 ? 226 ALA   B N   1 
ATOM   1794 C  CA  . ALA   A 1 226 ? -12.804 -1.204  -3.567 1.00 15.60 ? 226 ALA   B CA  1 
ATOM   1795 C  C   . ALA   A 1 226 ? -13.533 -0.016  -2.908 1.00 16.97 ? 226 ALA   B C   1 
ATOM   1796 O  O   . ALA   A 1 226 ? -12.977 1.068   -2.809 1.00 16.82 ? 226 ALA   B O   1 
ATOM   1797 C  CB  . ALA   A 1 226 ? -13.046 -1.214  -5.080 1.00 18.04 ? 226 ALA   B CB  1 
ATOM   1798 N  N   . LYS   A 1 227 ? -14.784 -0.187  -2.434 1.00 17.09 ? 227 LYS   B N   1 
ATOM   1799 C  CA  . LYS   A 1 227 ? -15.509 0.879   -1.763 1.00 16.73 ? 227 LYS   B CA  1 
ATOM   1800 C  C   . LYS   A 1 227 ? -14.773 1.354   -0.505 1.00 17.16 ? 227 LYS   B C   1 
ATOM   1801 O  O   . LYS   A 1 227 ? -14.784 2.544   -0.199 1.00 17.21 ? 227 LYS   B O   1 
ATOM   1802 C  CB  . LYS   A 1 227 ? -16.930 0.439   -1.396 1.00 22.81 ? 227 LYS   B CB  1 
ATOM   1803 C  CG  . LYS   A 1 227 ? -17.913 0.450   -2.553 1.00 30.16 ? 227 LYS   B CG  1 
ATOM   1804 C  CD  . LYS   A 1 227 ? -19.174 1.230   -2.150 1.00 39.39 ? 227 LYS   B CD  1 
ATOM   1805 C  CE  . LYS   A 1 227 ? -18.871 2.691   -1.859 1.00 41.18 ? 227 LYS   B CE  1 
ATOM   1806 N  NZ  . LYS   A 1 227 ? -20.082 3.463   -1.489 1.00 41.77 ? 227 LYS   B NZ  1 
ATOM   1807 N  N   . PHE   A 1 228 ? -14.095 0.443   0.237  1.00 15.30 ? 228 PHE   B N   1 
ATOM   1808 C  CA  . PHE   A 1 228 ? -13.414 0.906   1.447  1.00 13.43 ? 228 PHE   B CA  1 
ATOM   1809 C  C   . PHE   A 1 228 ? -12.283 1.886   1.113  1.00 13.05 ? 228 PHE   B C   1 
ATOM   1810 O  O   . PHE   A 1 228 ? -11.965 2.771   1.893  1.00 13.89 ? 228 PHE   B O   1 
ATOM   1811 C  CB  . PHE   A 1 228 ? -12.880 -0.319  2.201  1.00 13.89 ? 228 PHE   B CB  1 
ATOM   1812 C  CG  . PHE   A 1 228 ? -14.032 -1.137  2.757  1.00 13.96 ? 228 PHE   B CG  1 
ATOM   1813 C  CD1 . PHE   A 1 228 ? -14.690 -0.713  3.915  1.00 13.92 ? 228 PHE   B CD1 1 
ATOM   1814 C  CD2 . PHE   A 1 228 ? -14.428 -2.330  2.186  1.00 17.08 ? 228 PHE   B CD2 1 
ATOM   1815 C  CE1 . PHE   A 1 228 ? -15.744 -1.430  4.475  1.00 16.65 ? 228 PHE   B CE1 1 
ATOM   1816 C  CE2 . PHE   A 1 228 ? -15.502 -3.041  2.741  1.00 18.10 ? 228 PHE   B CE2 1 
ATOM   1817 C  CZ  . PHE   A 1 228 ? -16.151 -2.612  3.881  1.00 14.71 ? 228 PHE   B CZ  1 
ATOM   1818 N  N   . ARG   A 1 229 ? -11.636 1.704   -0.048 1.00 13.80 ? 229 ARG   B N   1 
ATOM   1819 C  CA  . ARG   A 1 229 ? -10.509 2.575   -0.396 1.00 12.97 ? 229 ARG   B CA  1 
ATOM   1820 C  C   . ARG   A 1 229 ? -10.973 3.992   -0.749 1.00 15.00 ? 229 ARG   B C   1 
ATOM   1821 O  O   . ARG   A 1 229 ? -10.125 4.874   -0.855 1.00 16.10 ? 229 ARG   B O   1 
ATOM   1822 C  CB  . ARG   A 1 229 ? -9.768  2.003   -1.616 1.00 13.71 ? 229 ARG   B CB  1 
ATOM   1823 C  CG  . ARG   A 1 229 ? -9.171  0.618   -1.378 1.00 14.20 ? 229 ARG   B CG  1 
ATOM   1824 C  CD  . ARG   A 1 229 ? -8.298  0.119   -2.511 1.00 14.22 ? 229 ARG   B CD  1 
ATOM   1825 N  NE  . ARG   A 1 229 ? -7.910  -1.280  -2.301 1.00 14.33 ? 229 ARG   B NE  1 
ATOM   1826 C  CZ  . ARG   A 1 229 ? -8.448  -2.372  -2.827 1.00 14.60 ? 229 ARG   B CZ  1 
ATOM   1827 N  NH1 . ARG   A 1 229 ? -9.383  -2.269  -3.769 1.00 14.69 ? 229 ARG   B NH1 1 
ATOM   1828 N  NH2 . ARG   A 1 229 ? -8.002  -3.571  -2.433 1.00 14.52 ? 229 ARG   B NH2 1 
ATOM   1829 N  N   . SER   A 1 230 ? -12.288 4.211   -0.848 1.00 16.99 ? 230 SER   B N   1 
ATOM   1830 C  CA  . SER   A 1 230 ? -12.786 5.552   -1.095 1.00 16.74 ? 230 SER   B CA  1 
ATOM   1831 C  C   . SER   A 1 230 ? -12.949 6.356   0.190  1.00 18.06 ? 230 SER   B C   1 
ATOM   1832 O  O   . SER   A 1 230 ? -13.252 7.557   0.127  1.00 17.38 ? 230 SER   B O   1 
ATOM   1833 C  CB  . SER   A 1 230 ? -14.038 5.491   -1.947 1.00 20.27 ? 230 SER   B CB  1 
ATOM   1834 O  OG  . SER   A 1 230 ? -15.149 4.986   -1.220 1.00 29.28 ? 230 SER   B OG  1 
ATOM   1835 N  N   . LEU   A 1 231 ? -12.758 5.720   1.370  1.00 16.06 ? 231 LEU   B N   1 
ATOM   1836 C  CA  . LEU   A 1 231 ? -12.757 6.528   2.590  1.00 16.57 ? 231 LEU   B CA  1 
ATOM   1837 C  C   . LEU   A 1 231 ? -11.569 7.491   2.554  1.00 15.82 ? 231 LEU   B C   1 
ATOM   1838 O  O   . LEU   A 1 231 ? -10.516 7.156   1.989  1.00 15.24 ? 231 LEU   B O   1 
ATOM   1839 C  CB  . LEU   A 1 231 ? -12.602 5.620   3.829  1.00 16.72 ? 231 LEU   B CB  1 
ATOM   1840 C  CG  . LEU   A 1 231 ? -13.826 4.773   4.160  1.00 18.03 ? 231 LEU   B CG  1 
ATOM   1841 C  CD1 . LEU   A 1 231 ? -13.466 3.738   5.232  1.00 17.19 ? 231 LEU   B CD1 1 
ATOM   1842 C  CD2 . LEU   A 1 231 ? -15.014 5.642   4.585  1.00 16.89 ? 231 LEU   B CD2 1 
ATOM   1843 N  N   . LEU   A 1 232 ? -11.694 8.665   3.202  1.00 15.03 ? 232 LEU   B N   1 
ATOM   1844 C  CA  . LEU   A 1 232 ? -10.514 9.523   3.323  1.00 15.91 ? 232 LEU   B CA  1 
ATOM   1845 C  C   . LEU   A 1 232 ? -9.788  9.373   4.658  1.00 16.01 ? 232 LEU   B C   1 
ATOM   1846 O  O   . LEU   A 1 232 ? -10.413 9.102   5.676  1.00 19.51 ? 232 LEU   B O   1 
ATOM   1847 C  CB  . LEU   A 1 232 ? -10.934 10.993  3.193  1.00 17.02 ? 232 LEU   B CB  1 
ATOM   1848 C  CG  . LEU   A 1 232 ? -11.717 11.333  1.928  1.00 20.25 ? 232 LEU   B CG  1 
ATOM   1849 C  CD1 . LEU   A 1 232 ? -12.149 12.787  2.006  1.00 21.57 ? 232 LEU   B CD1 1 
ATOM   1850 C  CD2 . LEU   A 1 232 ? -10.841 11.105  0.704  1.00 22.68 ? 232 LEU   B CD2 1 
ATOM   1851 N  N   . CYS   A 1 233 ? -8.463  9.619   4.664  1.00 16.00 ? 233 CYS   B N   1 
ATOM   1852 C  CA  . CYS   A 1 233 ? -7.722  9.733   5.895  1.00 16.99 ? 233 CYS   B CA  1 
ATOM   1853 C  C   . CYS   A 1 233 ? -7.676  11.180  6.415  1.00 20.89 ? 233 CYS   B C   1 
ATOM   1854 O  O   . CYS   A 1 233 ? -7.000  11.455  7.411  1.00 21.92 ? 233 CYS   B O   1 
ATOM   1855 C  CB  . CYS   A 1 233 ? -6.353  9.077   5.810  1.00 18.29 ? 233 CYS   B CB  1 
ATOM   1856 S  SG  . CYS   A 1 233 ? -5.232  9.889   4.626  1.00 24.35 ? 233 CYS   B SG  1 
ATOM   1857 N  N   . THR   A 1 234 ? -8.431  12.071  5.770  1.00 20.15 ? 234 THR   B N   1 
ATOM   1858 C  CA  . THR   A 1 234 ? -8.368  13.511  6.023  1.00 20.28 ? 234 THR   B CA  1 
ATOM   1859 C  C   . THR   A 1 234 ? -9.745  14.006  6.444  1.00 21.04 ? 234 THR   B C   1 
ATOM   1860 O  O   . THR   A 1 234 ? -10.744 13.415  6.075  1.00 20.78 ? 234 THR   B O   1 
ATOM   1861 C  CB  . THR   A 1 234 ? -7.817  14.243  4.773  1.00 18.61 ? 234 THR   B CB  1 
ATOM   1862 O  OG1 . THR   A 1 234 ? -8.575  13.811  3.647  1.00 19.78 ? 234 THR   B OG1 1 
ATOM   1863 C  CG2 . THR   A 1 234 ? -6.352  13.938  4.523  1.00 19.81 ? 234 THR   B CG2 1 
ATOM   1864 N  N   . ALA   A 1 235 ? -9.791  15.069  7.271  1.00 23.38 ? 235 ALA   B N   1 
ATOM   1865 C  CA  . ALA   A 1 235 ? -11.056 15.663  7.692  1.00 24.68 ? 235 ALA   B CA  1 
ATOM   1866 C  C   . ALA   A 1 235 ? -11.658 16.651  6.671  1.00 30.73 ? 235 ALA   B C   1 
ATOM   1867 O  O   . ALA   A 1 235 ? -11.007 17.076  5.719  1.00 26.15 ? 235 ALA   B O   1 
ATOM   1868 C  CB  . ALA   A 1 235 ? -10.896 16.241  9.088  1.00 27.80 ? 235 ALA   B CB  1 
ATOM   1869 N  N   . GLU   A 1 236 ? -12.965 16.935  6.827  1.00 28.27 ? 236 GLU   B N   1 
ATOM   1870 C  CA  . GLU   A 1 236 ? -13.691 17.901  6.022  1.00 33.83 ? 236 GLU   B CA  1 
ATOM   1871 C  C   . GLU   A 1 236 ? -12.858 19.177  5.981  1.00 36.99 ? 236 GLU   B C   1 
ATOM   1872 O  O   . GLU   A 1 236 ? -12.303 19.574  7.011  1.00 30.46 ? 236 GLU   B O   1 
ATOM   1873 C  CB  . GLU   A 1 236 ? -15.012 18.220  6.739  1.00 43.23 ? 236 GLU   B CB  1 
ATOM   1874 C  CG  . GLU   A 1 236 ? -16.124 18.740  5.849  1.00 51.47 ? 236 GLU   B CG  1 
ATOM   1875 C  CD  . GLU   A 1 236 ? -17.507 18.553  6.461  1.00 61.87 ? 236 GLU   B CD  1 
ATOM   1876 O  OE1 . GLU   A 1 236 ? -17.727 19.041  7.613  1.00 52.16 ? 236 GLU   B OE1 1 
ATOM   1877 O  OE2 . GLU   A 1 236 ? -18.371 17.917  5.790  1.00 62.41 ? 236 GLU   B OE2 1 
ATOM   1878 N  N   . GLY   A 1 237 ? -12.755 19.757  4.776  1.00 40.88 ? 237 GLY   B N   1 
ATOM   1879 C  CA  . GLY   A 1 237 ? -12.015 20.990  4.558  1.00 48.56 ? 237 GLY   B CA  1 
ATOM   1880 C  C   . GLY   A 1 237 ? -10.490 20.861  4.639  1.00 49.18 ? 237 GLY   B C   1 
ATOM   1881 O  O   . GLY   A 1 237 ? -9.809  21.881  4.679  1.00 51.72 ? 237 GLY   B O   1 
ATOM   1882 N  N   . GLU   A 1 238 ? -9.934  19.638  4.706  1.00 46.75 ? 238 GLU   B N   1 
ATOM   1883 C  CA  . GLU   A 1 238 ? -8.508  19.452  4.460  1.00 41.90 ? 238 GLU   B CA  1 
ATOM   1884 C  C   . GLU   A 1 238 ? -8.351  18.924  3.034  1.00 37.94 ? 238 GLU   B C   1 
ATOM   1885 O  O   . GLU   A 1 238 ? -9.294  18.365  2.469  1.00 36.28 ? 238 GLU   B O   1 
ATOM   1886 C  CB  . GLU   A 1 238 ? -7.878  18.319  5.280  1.00 47.58 ? 238 GLU   B CB  1 
ATOM   1887 C  CG  . GLU   A 1 238 ? -7.690  18.491  6.782  1.00 50.23 ? 238 GLU   B CG  1 
ATOM   1888 C  CD  . GLU   A 1 238 ? -6.853  17.303  7.277  1.00 57.83 ? 238 GLU   B CD  1 
ATOM   1889 O  OE1 . GLU   A 1 238 ? -5.648  17.242  6.931  1.00 60.61 ? 238 GLU   B OE1 1 
ATOM   1890 O  OE2 . GLU   A 1 238 ? -7.401  16.380  7.941  1.00 47.84 ? 238 GLU   B OE2 1 
ATOM   1891 N  N   . ALA   A 1 239 ? -7.149  19.069  2.471  1.00 33.33 ? 239 ALA   B N   1 
ATOM   1892 C  CA  . ALA   A 1 239 ? -6.811  18.486  1.175  1.00 31.89 ? 239 ALA   B CA  1 
ATOM   1893 C  C   . ALA   A 1 239 ? -6.984  16.964  1.232  1.00 27.48 ? 239 ALA   B C   1 
ATOM   1894 O  O   . ALA   A 1 239 ? -6.294  16.323  2.000  1.00 29.95 ? 239 ALA   B O   1 
ATOM   1895 C  CB  . ALA   A 1 239 ? -5.375  18.797  0.849  1.00 31.41 ? 239 ALA   B CB  1 
ATOM   1896 N  N   . ALA   A 1 240 ? -7.825  16.413  0.359  1.00 27.17 ? 240 ALA   B N   1 
ATOM   1897 C  CA  . ALA   A 1 240 ? -8.248  15.016  0.475  1.00 25.18 ? 240 ALA   B CA  1 
ATOM   1898 C  C   . ALA   A 1 240 ? -7.083  14.064  0.211  1.00 24.85 ? 240 ALA   B C   1 
ATOM   1899 O  O   . ALA   A 1 240 ? -6.252  14.291  -0.677 1.00 28.04 ? 240 ALA   B O   1 
ATOM   1900 C  CB  . ALA   A 1 240 ? -9.410  14.729  -0.441 1.00 24.88 ? 240 ALA   B CB  1 
ATOM   1901 N  N   . ALA   A 1 241 ? -7.026  12.970  0.987  1.00 19.40 ? 241 ALA   B N   1 
ATOM   1902 C  CA  . ALA   A 1 241 ? -6.169  11.855  0.625  1.00 18.17 ? 241 ALA   B CA  1 
ATOM   1903 C  C   . ALA   A 1 241 ? -6.908  10.574  0.993  1.00 16.63 ? 241 ALA   B C   1 
ATOM   1904 O  O   . ALA   A 1 241 ? -7.643  10.564  1.994  1.00 19.08 ? 241 ALA   B O   1 
ATOM   1905 C  CB  . ALA   A 1 241 ? -4.847  11.893  1.339  1.00 17.84 ? 241 ALA   B CB  1 
ATOM   1906 N  N   . PHE   A 1 242 ? -6.729  9.556   0.145  1.00 15.86 ? 242 PHE   B N   1 
ATOM   1907 C  CA  . PHE   A 1 242 ? -7.602  8.383   0.243  1.00 15.03 ? 242 PHE   B CA  1 
ATOM   1908 C  C   . PHE   A 1 242 ? -6.899  7.280   1.031  1.00 18.05 ? 242 PHE   B C   1 
ATOM   1909 O  O   . PHE   A 1 242 ? -5.681  7.134   0.947  1.00 17.60 ? 242 PHE   B O   1 
ATOM   1910 C  CB  . PHE   A 1 242 ? -7.829  7.803   -1.151 1.00 15.27 ? 242 PHE   B CB  1 
ATOM   1911 C  CG  . PHE   A 1 242 ? -8.785  8.651   -1.957 1.00 14.80 ? 242 PHE   B CG  1 
ATOM   1912 C  CD1 . PHE   A 1 242 ? -10.157 8.523   -1.773 1.00 16.18 ? 242 PHE   B CD1 1 
ATOM   1913 C  CD2 . PHE   A 1 242 ? -8.288  9.555   -2.903 1.00 16.92 ? 242 PHE   B CD2 1 
ATOM   1914 C  CE1 . PHE   A 1 242 ? -11.033 9.311   -2.501 1.00 20.50 ? 242 PHE   B CE1 1 
ATOM   1915 C  CE2 . PHE   A 1 242 ? -9.180  10.326  -3.637 1.00 18.43 ? 242 PHE   B CE2 1 
ATOM   1916 C  CZ  . PHE   A 1 242 ? -10.535 10.186  -3.434 1.00 20.08 ? 242 PHE   B CZ  1 
ATOM   1917 N  N   . LEU   A 1 243 ? -7.719  6.494   1.765  1.00 14.42 ? 243 LEU   B N   1 
ATOM   1918 C  CA  . LEU   A 1 243 ? -7.213  5.410   2.600  1.00 15.07 ? 243 LEU   B CA  1 
ATOM   1919 C  C   . LEU   A 1 243 ? -7.122  4.121   1.771  1.00 14.60 ? 243 LEU   B C   1 
ATOM   1920 O  O   . LEU   A 1 243 ? -7.979  3.229   1.891  1.00 14.17 ? 243 LEU   B O   1 
ATOM   1921 C  CB  . LEU   A 1 243 ? -8.152  5.290   3.808  1.00 13.68 ? 243 LEU   B CB  1 
ATOM   1922 C  CG  . LEU   A 1 243 ? -7.700  4.302   4.905  1.00 16.04 ? 243 LEU   B CG  1 
ATOM   1923 C  CD1 . LEU   A 1 243 ? -6.383  4.742   5.576  1.00 17.23 ? 243 LEU   B CD1 1 
ATOM   1924 C  CD2 . LEU   A 1 243 ? -8.850  4.194   5.929  1.00 19.58 ? 243 LEU   B CD2 1 
ATOM   1925 N  N   . VAL   A 1 244 ? -6.123  4.078   0.853  1.00 14.89 ? 244 VAL   B N   1 
ATOM   1926 C  CA  . VAL   A 1 244 ? -6.054  2.999   -0.133 1.00 14.31 ? 244 VAL   B CA  1 
ATOM   1927 C  C   . VAL   A 1 244 ? -5.474  1.729   0.472  1.00 14.70 ? 244 VAL   B C   1 
ATOM   1928 O  O   . VAL   A 1 244 ? -5.697  0.641   -0.065 1.00 14.63 ? 244 VAL   B O   1 
ATOM   1929 C  CB  . VAL   A 1 244 ? -5.305  3.390   -1.415 1.00 17.12 ? 244 VAL   B CB  1 
ATOM   1930 C  CG1 . VAL   A 1 244 ? -5.995  4.585   -2.084 1.00 19.01 ? 244 VAL   B CG1 1 
ATOM   1931 C  CG2 . VAL   A 1 244 ? -3.860  3.666   -1.124 1.00 16.29 ? 244 VAL   B CG2 1 
ATOM   1932 N  N   . SER   A 1 245 ? -4.804  1.876   1.611  1.00 13.85 ? 245 SER   B N   1 
ATOM   1933 C  CA  . SER   A 1 245 ? -4.108  0.782   2.284  1.00 13.36 ? 245 SER   B CA  1 
ATOM   1934 C  C   . SER   A 1 245 ? -3.920  1.139   3.763  1.00 12.52 ? 245 SER   B C   1 
ATOM   1935 O  O   . SER   A 1 245 ? -3.595  2.285   4.124  1.00 14.08 ? 245 SER   B O   1 
ATOM   1936 C  CB  . SER   A 1 245 ? -2.762  0.571   1.629  1.00 14.36 ? 245 SER   B CB  1 
ATOM   1937 O  OG  . SER   A 1 245 ? -2.057  -0.559  2.161  1.00 15.62 ? 245 SER   B OG  1 
ATOM   1938 N  N   . ASN   A 1 246 ? -4.108  0.146   4.657  1.00 12.23 ? 246 ASN   B N   1 
ATOM   1939 C  CA  . ASN   A 1 246 ? -4.060  0.429   6.090  1.00 11.23 ? 246 ASN   B CA  1 
ATOM   1940 C  C   . ASN   A 1 246 ? -3.659  -0.853  6.831  1.00 12.15 ? 246 ASN   B C   1 
ATOM   1941 O  O   . ASN   A 1 246 ? -4.158  -1.134  7.925  1.00 14.51 ? 246 ASN   B O   1 
ATOM   1942 C  CB  . ASN   A 1 246 ? -5.416  0.933   6.641  1.00 11.55 ? 246 ASN   B CB  1 
ATOM   1943 C  CG  . ASN   A 1 246 ? -6.571  -0.033  6.488  1.00 14.11 ? 246 ASN   B CG  1 
ATOM   1944 O  OD1 . ASN   A 1 246 ? -6.420  -1.082  5.870  1.00 15.12 ? 246 ASN   B OD1 1 
ATOM   1945 N  ND2 . ASN   A 1 246 ? -7.729  0.326   7.062  1.00 12.43 ? 246 ASN   B ND2 1 
ATOM   1946 N  N   . HIS   A 1 247 ? -2.677  -1.582  6.300  1.00 13.81 ? 247 HIS   B N   1 
ATOM   1947 C  CA  . HIS   A 1 247 ? -2.164  -2.776  6.986  1.00 14.26 ? 247 HIS   B CA  1 
ATOM   1948 C  C   . HIS   A 1 247 ? -0.699  -2.604  7.365  1.00 14.99 ? 247 HIS   B C   1 
ATOM   1949 O  O   . HIS   A 1 247 ? 0.112   -1.986  6.633  1.00 17.21 ? 247 HIS   B O   1 
ATOM   1950 C  CB  . HIS   A 1 247 ? -2.330  -4.084  6.156  1.00 15.02 ? 247 HIS   B CB  1 
ATOM   1951 C  CG  . HIS   A 1 247 ? -1.670  -4.068  4.813  1.00 18.14 ? 247 HIS   B CG  1 
ATOM   1952 N  ND1 . HIS   A 1 247 ? -0.384  -4.582  4.551  1.00 23.24 ? 247 HIS   B ND1 1 
ATOM   1953 C  CD2 . HIS   A 1 247 ? -2.059  -3.484  3.662  1.00 16.66 ? 247 HIS   B CD2 1 
ATOM   1954 C  CE1 . HIS   A 1 247 ? -0.083  -4.361  3.254  1.00 19.26 ? 247 HIS   B CE1 1 
ATOM   1955 N  NE2 . HIS   A 1 247 ? -1.092  -3.725  2.709  1.00 22.12 ? 247 HIS   B NE2 1 
ATOM   1956 N  N   . ARG   A 1 248 ? -0.380  -3.133  8.549  1.00 13.59 ? 248 ARG   B N   1 
ATOM   1957 C  CA  . ARG   A 1 248 ? 1.001   -3.088  9.046  1.00 14.34 ? 248 ARG   B CA  1 
ATOM   1958 C  C   . ARG   A 1 248 ? 1.747   -4.335  8.560  1.00 14.35 ? 248 ARG   B C   1 
ATOM   1959 O  O   . ARG   A 1 248 ? 1.217   -5.434  8.528  1.00 15.12 ? 248 ARG   B O   1 
ATOM   1960 C  CB  . ARG   A 1 248 ? 0.972   -3.085  10.582 1.00 13.78 ? 248 ARG   B CB  1 
ATOM   1961 C  CG  . ARG   A 1 248 ? 2.362   -2.899  11.192 1.00 13.63 ? 248 ARG   B CG  1 
ATOM   1962 C  CD  . ARG   A 1 248 ? 2.342   -3.036  12.733 1.00 13.13 ? 248 ARG   B CD  1 
ATOM   1963 N  NE  . ARG   A 1 248 ? 3.605   -2.544  13.282 1.00 15.16 ? 248 ARG   B NE  1 
ATOM   1964 C  CZ  . ARG   A 1 248 ? 4.074   -2.800  14.502 1.00 14.76 ? 248 ARG   B CZ  1 
ATOM   1965 N  NH1 . ARG   A 1 248 ? 3.399   -3.586  15.340 1.00 14.23 ? 248 ARG   B NH1 1 
ATOM   1966 N  NH2 . ARG   A 1 248 ? 5.192   -2.196  14.900 1.00 15.91 ? 248 ARG   B NH2 1 
ATOM   1967 N  N   . PRO   A 1 249 ? 3.033   -4.228  8.156  1.00 15.26 ? 249 PRO   B N   1 
ATOM   1968 C  CA  . PRO   A 1 249 ? 3.813   -5.411  7.797  1.00 17.37 ? 249 PRO   B CA  1 
ATOM   1969 C  C   . PRO   A 1 249 ? 4.069   -6.370  8.958  1.00 18.05 ? 249 PRO   B C   1 
ATOM   1970 O  O   . PRO   A 1 249 ? 3.943   -6.013  10.122 1.00 17.16 ? 249 PRO   B O   1 
ATOM   1971 C  CB  . PRO   A 1 249 ? 5.213   -4.829  7.483  1.00 18.94 ? 249 PRO   B CB  1 
ATOM   1972 C  CG  . PRO   A 1 249 ? 5.026   -3.370  7.239  1.00 22.53 ? 249 PRO   B CG  1 
ATOM   1973 C  CD  . PRO   A 1 249 ? 3.753   -2.967  7.945  1.00 19.18 ? 249 PRO   B CD  1 
ATOM   1974 N  N   . PRO   A 1 250 ? 4.388   -7.651  8.681  1.00 17.87 ? 250 PRO   B N   1 
ATOM   1975 C  CA  . PRO   A 1 250 ? 4.600   -8.637  9.760  1.00 19.10 ? 250 PRO   B CA  1 
ATOM   1976 C  C   . PRO   A 1 250 ? 5.850   -8.325  10.589 1.00 17.89 ? 250 PRO   B C   1 
ATOM   1977 O  O   . PRO   A 1 250 ? 6.824   -7.735  10.099 1.00 21.62 ? 250 PRO   B O   1 
ATOM   1978 C  CB  . PRO   A 1 250 ? 4.767   -9.981  9.017  1.00 20.54 ? 250 PRO   B CB  1 
ATOM   1979 C  CG  . PRO   A 1 250 ? 4.420   -9.707  7.582  1.00 23.35 ? 250 PRO   B CG  1 
ATOM   1980 C  CD  . PRO   A 1 250 ? 4.572   -8.218  7.337  1.00 20.56 ? 250 PRO   B CD  1 
ATOM   1981 N  N   . GLN   A 1 251 ? 5.808   -8.693  11.875 1.00 15.53 ? 251 GLN   B N   1 
ATOM   1982 C  CA  . GLN   A 1 251 ? 6.821   -8.325  12.861 1.00 15.71 ? 251 GLN   B CA  1 
ATOM   1983 C  C   . GLN   A 1 251 ? 7.518   -9.588  13.362 1.00 18.73 ? 251 GLN   B C   1 
ATOM   1984 O  O   . GLN   A 1 251 ? 7.010   -10.691 13.223 1.00 16.84 ? 251 GLN   B O   1 
ATOM   1985 C  CB  . GLN   A 1 251 ? 6.138   -7.622  14.042 1.00 16.67 ? 251 GLN   B CB  1 
ATOM   1986 C  CG  . GLN   A 1 251 ? 5.367   -6.378  13.631 1.00 19.17 ? 251 GLN   B CG  1 
ATOM   1987 C  CD  . GLN   A 1 251 ? 6.237   -5.365  12.927 1.00 20.34 ? 251 GLN   B CD  1 
ATOM   1988 O  OE1 . GLN   A 1 251 ? 5.916   -4.881  11.828 1.00 21.61 ? 251 GLN   B OE1 1 
ATOM   1989 N  NE2 . GLN   A 1 251 ? 7.379   -5.066  13.541 1.00 21.12 ? 251 GLN   B NE2 1 
ATOM   1990 N  N   . PRO   A 1 252 ? 8.776   -9.488  13.842 1.00 19.41 ? 252 PRO   B N   1 
ATOM   1991 C  CA  . PRO   A 1 252 ? 9.529   -10.670 14.293 1.00 19.76 ? 252 PRO   B CA  1 
ATOM   1992 C  C   . PRO   A 1 252 ? 8.856   -11.474 15.416 1.00 18.30 ? 252 PRO   B C   1 
ATOM   1993 O  O   . PRO   A 1 252 ? 8.339   -10.874 16.371 1.00 16.45 ? 252 PRO   B O   1 
ATOM   1994 C  CB  . PRO   A 1 252 ? 10.804  -10.019 14.878 1.00 20.36 ? 252 PRO   B CB  1 
ATOM   1995 C  CG  . PRO   A 1 252 ? 10.954  -8.725  14.126 1.00 24.09 ? 252 PRO   B CG  1 
ATOM   1996 C  CD  . PRO   A 1 252 ? 9.537   -8.224  13.949 1.00 21.84 ? 252 PRO   B CD  1 
ATOM   1997 N  N   . LEU   A 1 253 ? 8.905   -12.826 15.321 1.00 19.15 ? 253 LEU   B N   1 
ATOM   1998 C  CA  . LEU   A 1 253 ? 8.268   -13.669 16.329 1.00 18.82 ? 253 LEU   B CA  1 
ATOM   1999 C  C   . LEU   A 1 253 ? 8.938   -13.580 17.711 1.00 17.53 ? 253 LEU   B C   1 
ATOM   2000 O  O   . LEU   A 1 253 ? 8.298   -13.679 18.747 1.00 17.98 ? 253 LEU   B O   1 
ATOM   2001 C  CB  . LEU   A 1 253 ? 8.134   -15.104 15.800 1.00 20.65 ? 253 LEU   B CB  1 
ATOM   2002 C  CG  . LEU   A 1 253 ? 7.277   -16.072 16.633 1.00 23.21 ? 253 LEU   B CG  1 
ATOM   2003 C  CD1 . LEU   A 1 253 ? 5.839   -15.558 16.714 1.00 20.56 ? 253 LEU   B CD1 1 
ATOM   2004 C  CD2 . LEU   A 1 253 ? 7.264   -17.478 16.014 1.00 27.44 ? 253 LEU   B CD2 1 
ATOM   2005 N  N   . LYS   A 1 254 ? 10.269  -13.415 17.757 1.00 20.28 ? 254 LYS   B N   1 
ATOM   2006 C  CA  . LYS   A 1 254 ? 10.957  -13.184 19.014 1.00 18.54 ? 254 LYS   B CA  1 
ATOM   2007 C  C   . LYS   A 1 254 ? 10.650  -14.293 20.051 1.00 18.61 ? 254 LYS   B C   1 
ATOM   2008 O  O   . LYS   A 1 254 ? 10.474  -14.013 21.243 1.00 18.98 ? 254 LYS   B O   1 
ATOM   2009 C  CB  . LYS   A 1 254 ? 10.725  -11.757 19.527 1.00 25.30 ? 254 LYS   B CB  1 
ATOM   2010 C  CG  . LYS   A 1 254 ? 11.304  -10.655 18.632 1.00 25.92 ? 254 LYS   B CG  1 
ATOM   2011 C  CD  . LYS   A 1 254 ? 12.706  -10.309 18.993 1.00 31.47 ? 254 LYS   B CD  1 
ATOM   2012 C  CE  . LYS   A 1 254 ? 13.306  -9.187  18.155 1.00 39.01 ? 254 LYS   B CE  1 
ATOM   2013 N  NZ  . LYS   A 1 254 ? 12.444  -7.979  18.166 1.00 42.23 ? 254 LYS   B NZ  1 
ATOM   2014 N  N   . GLY   A 1 255 ? 10.577  -15.540 19.588 1.00 17.49 ? 255 GLY   B N   1 
ATOM   2015 C  CA  . GLY   A 1 255 ? 10.522  -16.658 20.519 1.00 18.79 ? 255 GLY   B CA  1 
ATOM   2016 C  C   . GLY   A 1 255 ? 9.129   -16.946 21.080 1.00 19.96 ? 255 GLY   B C   1 
ATOM   2017 O  O   . GLY   A 1 255 ? 8.981   -17.810 21.947 1.00 19.26 ? 255 GLY   B O   1 
ATOM   2018 N  N   . ARG   A 1 256 ? 8.118   -16.173 20.639 1.00 19.76 ? 256 ARG   B N   1 
ATOM   2019 C  CA  . ARG   A 1 256 ? 6.726   -16.498 20.997 1.00 16.68 ? 256 ARG   B CA  1 
ATOM   2020 C  C   . ARG   A 1 256 ? 6.238   -17.832 20.411 1.00 18.97 ? 256 ARG   B C   1 
ATOM   2021 O  O   . ARG   A 1 256 ? 6.652   -18.289 19.343 1.00 18.01 ? 256 ARG   B O   1 
ATOM   2022 C  CB  . ARG   A 1 256 ? 5.799   -15.348 20.605 1.00 16.61 ? 256 ARG   B CB  1 
ATOM   2023 C  CG  . ARG   A 1 256 ? 6.046   -14.106 21.424 1.00 15.81 ? 256 ARG   B CG  1 
ATOM   2024 C  CD  . ARG   A 1 256 ? 5.114   -13.066 20.803 1.00 15.16 ? 256 ARG   B CD  1 
ATOM   2025 N  NE  . ARG   A 1 256 ? 5.721   -12.528 19.587 1.00 15.58 ? 256 ARG   B NE  1 
ATOM   2026 C  CZ  . ARG   A 1 256 ? 5.135   -11.602 18.828 1.00 15.09 ? 256 ARG   B CZ  1 
ATOM   2027 N  NH1 . ARG   A 1 256 ? 3.898   -11.176 19.123 1.00 12.59 ? 256 ARG   B NH1 1 
ATOM   2028 N  NH2 . ARG   A 1 256 ? 5.765   -11.155 17.776 1.00 14.54 ? 256 ARG   B NH2 1 
ATOM   2029 N  N   . LYS   A 1 257 ? 5.340   -18.496 21.173 1.00 17.75 ? 257 LYS   B N   1 
ATOM   2030 C  CA  . LYS   A 1 257 ? 4.762   -19.752 20.724 1.00 17.43 ? 257 LYS   B CA  1 
ATOM   2031 C  C   . LYS   A 1 257 ? 3.411   -19.476 20.066 1.00 18.04 ? 257 LYS   B C   1 
ATOM   2032 O  O   . LYS   A 1 257 ? 2.555   -18.837 20.692 1.00 19.10 ? 257 LYS   B O   1 
ATOM   2033 C  CB  . LYS   A 1 257 ? 4.521   -20.585 21.979 1.00 22.25 ? 257 LYS   B CB  1 
ATOM   2034 C  CG  . LYS   A 1 257 ? 4.087   -22.014 21.681 1.00 26.52 ? 257 LYS   B CG  1 
ATOM   2035 C  CD  . LYS   A 1 257 ? 3.500   -22.732 22.877 1.00 32.62 ? 257 LYS   B CD  1 
ATOM   2036 C  CE  . LYS   A 1 257 ? 4.500   -23.583 23.611 1.00 35.48 ? 257 LYS   B CE  1 
ATOM   2037 N  NZ  . LYS   A 1 257 ? 3.843   -24.792 24.183 1.00 34.85 ? 257 LYS   B NZ  1 
ATOM   2038 N  N   . VAL   A 1 258 ? 3.264   -19.906 18.811 1.00 15.09 ? 258 VAL   B N   1 
ATOM   2039 C  CA  . VAL   A 1 258 ? 1.966   -19.829 18.141 1.00 15.46 ? 258 VAL   B CA  1 
ATOM   2040 C  C   . VAL   A 1 258 ? 1.305   -21.196 18.293 1.00 16.95 ? 258 VAL   B C   1 
ATOM   2041 O  O   . VAL   A 1 258 ? 1.902   -22.214 17.921 1.00 17.63 ? 258 VAL   B O   1 
ATOM   2042 C  CB  . VAL   A 1 258 ? 2.128   -19.484 16.661 1.00 17.14 ? 258 VAL   B CB  1 
ATOM   2043 C  CG1 . VAL   A 1 258 ? 0.792   -19.441 15.927 1.00 18.42 ? 258 VAL   B CG1 1 
ATOM   2044 C  CG2 . VAL   A 1 258 ? 2.970   -18.223 16.467 1.00 19.62 ? 258 VAL   B CG2 1 
ATOM   2045 N  N   . ARG   A 1 259 ? 0.060   -21.244 18.807 1.00 13.97 ? 259 ARG   B N   1 
ATOM   2046 C  CA  . ARG   A 1 259 ? -0.562  -22.535 19.076 1.00 14.09 ? 259 ARG   B CA  1 
ATOM   2047 C  C   . ARG   A 1 259 ? -1.791  -22.705 18.195 1.00 17.51 ? 259 ARG   B C   1 
ATOM   2048 O  O   . ARG   A 1 259 ? -2.375  -21.726 17.739 1.00 17.73 ? 259 ARG   B O   1 
ATOM   2049 C  CB  . ARG   A 1 259 ? -1.006  -22.643 20.536 1.00 16.11 ? 259 ARG   B CB  1 
ATOM   2050 C  CG  . ARG   A 1 259 ? 0.181   -22.523 21.484 1.00 16.88 ? 259 ARG   B CG  1 
ATOM   2051 C  CD  . ARG   A 1 259 ? -0.290  -22.612 22.912 1.00 18.02 ? 259 ARG   B CD  1 
ATOM   2052 N  NE  . ARG   A 1 259 ? -0.977  -21.387 23.312 1.00 18.19 ? 259 ARG   B NE  1 
ATOM   2053 C  CZ  . ARG   A 1 259 ? -1.811  -21.282 24.326 1.00 16.91 ? 259 ARG   B CZ  1 
ATOM   2054 N  NH1 . ARG   A 1 259 ? -2.105  -22.356 25.046 1.00 18.66 ? 259 ARG   B NH1 1 
ATOM   2055 N  NH2 . ARG   A 1 259 ? -2.305  -20.103 24.663 1.00 17.15 ? 259 ARG   B NH2 1 
ATOM   2056 N  N   . ALA   A 1 260 ? -2.103  -23.964 17.886 1.00 16.67 ? 260 ALA   B N   1 
ATOM   2057 C  CA  . ALA   A 1 260 ? -3.258  -24.285 17.063 1.00 15.97 ? 260 ALA   B CA  1 
ATOM   2058 C  C   . ALA   A 1 260 ? -4.306  -25.011 17.888 1.00 17.47 ? 260 ALA   B C   1 
ATOM   2059 O  O   . ALA   A 1 260 ? -3.975  -25.872 18.700 1.00 15.13 ? 260 ALA   B O   1 
ATOM   2060 C  CB  . ALA   A 1 260 ? -2.833  -25.162 15.903 1.00 17.57 ? 260 ALA   B CB  1 
ATOM   2061 N  N   . SER   A 1 261 ? -5.585  -24.688 17.634 1.00 17.06 ? 261 SER   B N   1 
ATOM   2062 C  CA  . SER   A 1 261 ? -6.695  -25.359 18.316 1.00 17.43 ? 261 SER   B CA  1 
ATOM   2063 C  C   . SER   A 1 261 ? -7.038  -26.712 17.700 1.00 19.87 ? 261 SER   B C   1 
ATOM   2064 O  O   . SER   A 1 261 ? -7.945  -27.393 18.203 1.00 21.55 ? 261 SER   B O   1 
ATOM   2065 C  CB  . SER   A 1 261 ? -7.937  -24.460 18.332 1.00 18.29 ? 261 SER   B CB  1 
ATOM   2066 O  OG  . SER   A 1 261 ? -8.544  -24.461 17.048 1.00 20.99 ? 261 SER   B OG  1 
ATOM   2067 N  N   . PHE   A 1 262 ? -6.362  -27.073 16.600 1.00 20.78 ? 262 PHE   B N   1 
ATOM   2068 C  CA  . PHE   A 1 262 ? -6.744  -28.215 15.774 1.00 24.47 ? 262 PHE   B CA  1 
ATOM   2069 C  C   . PHE   A 1 262 ? -5.490  -28.885 15.220 1.00 28.78 ? 262 PHE   B C   1 
ATOM   2070 O  O   . PHE   A 1 262 ? -4.409  -28.285 15.149 1.00 25.75 ? 262 PHE   B O   1 
ATOM   2071 C  CB  . PHE   A 1 262 ? -7.600  -27.746 14.589 1.00 22.45 ? 262 PHE   B CB  1 
ATOM   2072 C  CG  . PHE   A 1 262 ? -6.879  -26.736 13.721 1.00 25.14 ? 262 PHE   B CG  1 
ATOM   2073 C  CD1 . PHE   A 1 262 ? -6.724  -25.414 14.126 1.00 21.86 ? 262 PHE   B CD1 1 
ATOM   2074 C  CD2 . PHE   A 1 262 ? -6.282  -27.120 12.528 1.00 25.56 ? 262 PHE   B CD2 1 
ATOM   2075 C  CE1 . PHE   A 1 262 ? -5.951  -24.519 13.389 1.00 23.29 ? 262 PHE   B CE1 1 
ATOM   2076 C  CE2 . PHE   A 1 262 ? -5.566  -26.204 11.756 1.00 27.07 ? 262 PHE   B CE2 1 
ATOM   2077 C  CZ  . PHE   A 1 262 ? -5.396  -24.900 12.189 1.00 24.09 ? 262 PHE   B CZ  1 
ATOM   2078 N  N   . HIS   A 1 263 ? -5.663  -30.126 14.731 1.00 34.35 ? 263 HIS   B N   1 
ATOM   2079 C  CA  . HIS   A 1 263 ? -4.583  -30.762 13.988 1.00 41.71 ? 263 HIS   B CA  1 
ATOM   2080 C  C   . HIS   A 1 263 ? -5.146  -31.734 12.953 1.00 52.15 ? 263 HIS   B C   1 
ATOM   2081 O  O   . HIS   A 1 263 ? -4.370  -32.590 12.519 1.00 51.16 ? 263 HIS   B O   1 
ATOM   2082 C  CB  . HIS   A 1 263 ? -3.603  -31.478 14.932 1.00 47.77 ? 263 HIS   B CB  1 
ATOM   2083 C  CG  . HIS   A 1 263 ? -4.134  -32.719 15.569 1.00 51.79 ? 263 HIS   B CG  1 
ATOM   2084 N  ND1 . HIS   A 1 263 ? -5.256  -32.718 16.381 1.00 56.25 ? 263 HIS   B ND1 1 
ATOM   2085 C  CD2 . HIS   A 1 263 ? -3.674  -33.989 15.564 1.00 61.16 ? 263 HIS   B CD2 1 
ATOM   2086 C  CE1 . HIS   A 1 263 ? -5.487  -33.941 16.820 1.00 62.85 ? 263 HIS   B CE1 1 
ATOM   2087 N  NE2 . HIS   A 1 263 ? -4.529  -34.740 16.334 1.00 62.84 ? 263 HIS   B NE2 1 
ATOM   2088 O  OXT . HIS   A 1 263 ? -6.318  -31.690 12.553 1.00 53.91 ? 263 HIS   B OXT 1 
ATOM   2089 N  N   . LEU   B 1 5   ? -51.470 -41.576 23.509 1.00 59.66 ? 5   LEU   A N   1 
ATOM   2090 C  CA  . LEU   B 1 5   ? -51.233 -42.401 24.728 1.00 46.58 ? 5   LEU   A CA  1 
ATOM   2091 C  C   . LEU   B 1 5   ? -50.939 -41.487 25.916 1.00 52.69 ? 5   LEU   A C   1 
ATOM   2092 O  O   . LEU   B 1 5   ? -50.682 -40.292 25.747 1.00 52.64 ? 5   LEU   A O   1 
ATOM   2093 C  CB  . LEU   B 1 5   ? -50.104 -43.408 24.479 1.00 52.44 ? 5   LEU   A CB  1 
ATOM   2094 C  CG  . LEU   B 1 5   ? -50.561 -44.866 24.373 1.00 50.69 ? 5   LEU   A CG  1 
ATOM   2095 C  CD1 . LEU   B 1 5   ? -49.727 -45.639 23.352 1.00 47.33 ? 5   LEU   A CD1 1 
ATOM   2096 C  CD2 . LEU   B 1 5   ? -50.601 -45.551 25.739 1.00 50.99 ? 5   LEU   A CD2 1 
ATOM   2097 N  N   . SER   B 1 6   ? -50.964 -42.090 27.113 1.00 47.29 ? 6   SER   A N   1 
ATOM   2098 C  CA  . SER   B 1 6   ? -50.925 -41.382 28.380 1.00 36.33 ? 6   SER   A CA  1 
ATOM   2099 C  C   . SER   B 1 6   ? -49.661 -41.730 29.169 1.00 29.28 ? 6   SER   A C   1 
ATOM   2100 O  O   . SER   B 1 6   ? -49.752 -41.880 30.386 1.00 29.35 ? 6   SER   A O   1 
ATOM   2101 C  CB  . SER   B 1 6   ? -52.178 -41.702 29.187 1.00 39.43 ? 6   SER   A CB  1 
ATOM   2102 O  OG  . SER   B 1 6   ? -52.162 -43.041 29.684 1.00 39.08 ? 6   SER   A OG  1 
ATOM   2103 N  N   . TRP   B 1 7   ? -48.488 -41.826 28.502 1.00 22.08 ? 7   TRP   A N   1 
ATOM   2104 C  CA  . TRP   B 1 7   ? -47.271 -42.202 29.226 1.00 19.68 ? 7   TRP   A CA  1 
ATOM   2105 C  C   . TRP   B 1 7   ? -46.791 -41.036 30.103 1.00 17.35 ? 7   TRP   A C   1 
ATOM   2106 O  O   . TRP   B 1 7   ? -47.089 -39.866 29.826 1.00 17.18 ? 7   TRP   A O   1 
ATOM   2107 C  CB  . TRP   B 1 7   ? -46.174 -42.638 28.255 1.00 19.90 ? 7   TRP   A CB  1 
ATOM   2108 C  CG  . TRP   B 1 7   ? -45.667 -41.551 27.353 1.00 19.41 ? 7   TRP   A CG  1 
ATOM   2109 C  CD1 . TRP   B 1 7   ? -46.105 -41.181 26.106 1.00 19.90 ? 7   TRP   A CD1 1 
ATOM   2110 C  CD2 . TRP   B 1 7   ? -44.578 -40.663 27.656 1.00 17.85 ? 7   TRP   A CD2 1 
ATOM   2111 N  NE1 . TRP   B 1 7   ? -45.386 -40.113 25.623 1.00 19.82 ? 7   TRP   A NE1 1 
ATOM   2112 C  CE2 . TRP   B 1 7   ? -44.416 -39.789 26.560 1.00 19.41 ? 7   TRP   A CE2 1 
ATOM   2113 C  CE3 . TRP   B 1 7   ? -43.736 -40.531 28.770 1.00 19.85 ? 7   TRP   A CE3 1 
ATOM   2114 C  CZ2 . TRP   B 1 7   ? -43.420 -38.801 26.552 1.00 18.15 ? 7   TRP   A CZ2 1 
ATOM   2115 C  CZ3 . TRP   B 1 7   ? -42.752 -39.560 28.756 1.00 17.64 ? 7   TRP   A CZ3 1 
ATOM   2116 C  CH2 . TRP   B 1 7   ? -42.591 -38.726 27.654 1.00 17.17 ? 7   TRP   A CH2 1 
ATOM   2117 N  N   . GLY   B 1 8   ? -46.000 -41.371 31.145 1.00 18.91 ? 8   GLY   A N   1 
ATOM   2118 C  CA  . GLY   B 1 8   ? -45.358 -40.353 31.974 1.00 17.44 ? 8   GLY   A CA  1 
ATOM   2119 C  C   . GLY   B 1 8   ? -44.273 -40.917 32.887 1.00 14.77 ? 8   GLY   A C   1 
ATOM   2120 O  O   . GLY   B 1 8   ? -43.580 -41.875 32.552 1.00 15.23 ? 8   GLY   A O   1 
ATOM   2121 N  N   . TYR   B 1 9   ? -44.198 -40.358 34.108 1.00 16.86 ? 9   TYR   A N   1 
ATOM   2122 C  CA  . TYR   B 1 9   ? -43.214 -40.776 35.086 1.00 15.41 ? 9   TYR   A CA  1 
ATOM   2123 C  C   . TYR   B 1 9   ? -43.885 -41.100 36.417 1.00 19.03 ? 9   TYR   A C   1 
ATOM   2124 O  O   . TYR   B 1 9   ? -43.198 -41.277 37.425 1.00 19.92 ? 9   TYR   A O   1 
ATOM   2125 C  CB  . TYR   B 1 9   ? -42.141 -39.690 35.254 1.00 15.65 ? 9   TYR   A CB  1 
ATOM   2126 C  CG  . TYR   B 1 9   ? -41.359 -39.461 33.977 1.00 13.88 ? 9   TYR   A CG  1 
ATOM   2127 C  CD1 . TYR   B 1 9   ? -40.211 -40.191 33.737 1.00 14.03 ? 9   TYR   A CD1 1 
ATOM   2128 C  CD2 . TYR   B 1 9   ? -41.719 -38.474 33.081 1.00 14.20 ? 9   TYR   A CD2 1 
ATOM   2129 C  CE1 . TYR   B 1 9   ? -39.479 -40.013 32.566 1.00 13.49 ? 9   TYR   A CE1 1 
ATOM   2130 C  CE2 . TYR   B 1 9   ? -40.987 -38.265 31.929 1.00 15.48 ? 9   TYR   A CE2 1 
ATOM   2131 C  CZ  . TYR   B 1 9   ? -39.863 -39.025 31.689 1.00 14.19 ? 9   TYR   A CZ  1 
ATOM   2132 O  OH  . TYR   B 1 9   ? -39.095 -38.771 30.575 1.00 14.41 ? 9   TYR   A OH  1 
ATOM   2133 N  N   . ARG   B 1 10  ? -45.214 -41.283 36.359 1.00 22.21 ? 10  ARG   A N   1 
ATOM   2134 C  CA  . ARG   B 1 10  ? -45.964 -41.588 37.586 1.00 26.30 ? 10  ARG   A CA  1 
ATOM   2135 C  C   . ARG   B 1 10  ? -45.965 -43.096 37.851 1.00 25.46 ? 10  ARG   A C   1 
ATOM   2136 O  O   . ARG   B 1 10  ? -45.458 -43.898 37.080 1.00 23.94 ? 10  ARG   A O   1 
ATOM   2137 C  CB  . ARG   B 1 10  ? -47.367 -40.980 37.515 1.00 25.71 ? 10  ARG   A CB  1 
ATOM   2138 C  CG  . ARG   B 1 10  ? -47.403 -39.477 37.268 1.00 32.52 ? 10  ARG   A CG  1 
ATOM   2139 C  CD  . ARG   B 1 10  ? -48.739 -38.811 37.524 1.00 40.30 ? 10  ARG   A CD  1 
ATOM   2140 N  NE  . ARG   B 1 10  ? -48.613 -38.304 38.880 1.00 54.72 ? 10  ARG   A NE  1 
ATOM   2141 C  CZ  . ARG   B 1 10  ? -49.344 -38.663 39.931 1.00 67.52 ? 10  ARG   A CZ  1 
ATOM   2142 N  NH1 . ARG   B 1 10  ? -50.341 -39.531 39.804 1.00 71.53 ? 10  ARG   A NH1 1 
ATOM   2143 N  NH2 . ARG   B 1 10  ? -49.083 -38.114 41.105 1.00 71.79 ? 10  ARG   A NH2 1 
ATOM   2144 N  N   . GLU   B 1 11  ? -46.572 -43.519 38.981 1.00 28.80 ? 11  GLU   A N   1 
ATOM   2145 C  CA  . GLU   B 1 11  ? -46.555 -44.933 39.338 1.00 29.29 ? 11  GLU   A CA  1 
ATOM   2146 C  C   . GLU   B 1 11  ? -47.092 -45.830 38.215 1.00 31.58 ? 11  GLU   A C   1 
ATOM   2147 O  O   . GLU   B 1 11  ? -46.469 -46.836 37.877 1.00 31.28 ? 11  GLU   A O   1 
ATOM   2148 C  CB  . GLU   B 1 11  ? -47.363 -45.178 40.615 1.00 31.29 ? 11  GLU   A CB  1 
ATOM   2149 C  CG  . GLU   B 1 11  ? -47.098 -46.562 41.204 1.00 43.27 ? 11  GLU   A CG  1 
ATOM   2150 N  N   . HIS   B 1 12  ? -48.218 -45.439 37.602 1.00 32.41 ? 12  HIS   A N   1 
ATOM   2151 C  CA  . HIS   B 1 12  ? -48.955 -46.329 36.710 1.00 29.85 ? 12  HIS   A CA  1 
ATOM   2152 C  C   . HIS   B 1 12  ? -48.620 -46.125 35.227 1.00 30.60 ? 12  HIS   A C   1 
ATOM   2153 O  O   . HIS   B 1 12  ? -49.053 -46.926 34.388 1.00 28.96 ? 12  HIS   A O   1 
ATOM   2154 C  CB  . HIS   B 1 12  ? -50.463 -46.183 36.972 1.00 36.68 ? 12  HIS   A CB  1 
ATOM   2155 C  CG  . HIS   B 1 12  ? -50.825 -46.507 38.391 1.00 52.39 ? 12  HIS   A CG  1 
ATOM   2156 N  ND1 . HIS   B 1 12  ? -50.498 -47.731 38.984 1.00 54.53 ? 12  HIS   A ND1 1 
ATOM   2157 C  CD2 . HIS   B 1 12  ? -51.463 -45.781 39.342 1.00 56.55 ? 12  HIS   A CD2 1 
ATOM   2158 C  CE1 . HIS   B 1 12  ? -50.928 -47.737 40.232 1.00 61.64 ? 12  HIS   A CE1 1 
ATOM   2159 N  NE2 . HIS   B 1 12  ? -51.519 -46.549 40.477 1.00 63.12 ? 12  HIS   A NE2 1 
ATOM   2160 N  N   . ASN   B 1 13  ? -47.854 -45.071 34.889 1.00 23.54 ? 13  ASN   A N   1 
ATOM   2161 C  CA  . ASN   B 1 13  ? -47.597 -44.767 33.474 1.00 21.33 ? 13  ASN   A CA  1 
ATOM   2162 C  C   . ASN   B 1 13  ? -46.091 -44.576 33.244 1.00 19.91 ? 13  ASN   A C   1 
ATOM   2163 O  O   . ASN   B 1 13  ? -45.672 -44.174 32.151 1.00 18.99 ? 13  ASN   A O   1 
ATOM   2164 C  CB  . ASN   B 1 13  ? -48.402 -43.546 32.981 1.00 22.03 ? 13  ASN   A CB  1 
ATOM   2165 C  CG  . ASN   B 1 13  ? -48.045 -42.217 33.633 1.00 22.17 ? 13  ASN   A CG  1 
ATOM   2166 O  OD1 . ASN   B 1 13  ? -47.121 -42.155 34.433 1.00 22.68 ? 13  ASN   A OD1 1 
ATOM   2167 N  ND2 . ASN   B 1 13  ? -48.749 -41.149 33.292 1.00 22.58 ? 13  ASN   A ND2 1 
ATOM   2168 N  N   . GLY   B 1 14  ? -45.306 -44.848 34.284 1.00 19.43 ? 14  GLY   A N   1 
ATOM   2169 C  CA  . GLY   B 1 14  ? -43.875 -44.520 34.311 1.00 21.62 ? 14  GLY   A CA  1 
ATOM   2170 C  C   . GLY   B 1 14  ? -42.983 -45.498 33.549 1.00 19.13 ? 14  GLY   A C   1 
ATOM   2171 O  O   . GLY   B 1 14  ? -43.415 -46.478 32.967 1.00 19.11 ? 14  GLY   A O   1 
ATOM   2172 N  N   . PRO   B 1 15  ? -41.660 -45.250 33.464 1.00 18.60 ? 15  PRO   A N   1 
ATOM   2173 C  CA  . PRO   B 1 15  ? -40.755 -46.069 32.662 1.00 17.23 ? 15  PRO   A CA  1 
ATOM   2174 C  C   . PRO   B 1 15  ? -40.844 -47.593 32.646 1.00 21.42 ? 15  PRO   A C   1 
ATOM   2175 O  O   . PRO   B 1 15  ? -40.680 -48.184 31.583 1.00 19.90 ? 15  PRO   A O   1 
ATOM   2176 C  CB  . PRO   B 1 15  ? -39.377 -45.681 33.226 1.00 18.90 ? 15  PRO   A CB  1 
ATOM   2177 C  CG  . PRO   B 1 15  ? -39.559 -44.199 33.541 1.00 16.61 ? 15  PRO   A CG  1 
ATOM   2178 C  CD  . PRO   B 1 15  ? -40.983 -44.069 34.039 1.00 18.06 ? 15  PRO   A CD  1 
ATOM   2179 N  N   . ILE   B 1 16  ? -41.115 -48.202 33.821 1.00 22.78 ? 16  ILE   A N   1 
ATOM   2180 C  CA  . ILE   B 1 16  ? -41.281 -49.651 33.901 1.00 25.97 ? 16  ILE   A CA  1 
ATOM   2181 C  C   . ILE   B 1 16  ? -42.425 -50.147 32.996 1.00 23.59 ? 16  ILE   A C   1 
ATOM   2182 O  O   . ILE   B 1 16  ? -42.397 -51.298 32.557 1.00 27.64 ? 16  ILE   A O   1 
ATOM   2183 C  CB  . ILE   B 1 16  ? -41.457 -50.116 35.373 1.00 24.70 ? 16  ILE   A CB  1 
ATOM   2184 C  CG1 . ILE   B 1 16  ? -41.024 -51.570 35.562 1.00 32.80 ? 16  ILE   A CG1 1 
ATOM   2185 C  CG2 . ILE   B 1 16  ? -42.890 -49.944 35.825 1.00 31.94 ? 16  ILE   A CG2 1 
ATOM   2186 C  CD1 . ILE   B 1 16  ? -39.613 -51.862 35.104 1.00 38.32 ? 16  ILE   A CD1 1 
ATOM   2187 N  N   . HIS   B 1 17  ? -43.442 -49.307 32.775 1.00 21.80 ? 17  HIS   A N   1 
ATOM   2188 C  CA  . HIS   B 1 17  ? -44.676 -49.610 32.057 1.00 22.79 ? 17  HIS   A CA  1 
ATOM   2189 C  C   . HIS   B 1 17  ? -44.553 -49.239 30.572 1.00 22.84 ? 17  HIS   A C   1 
ATOM   2190 O  O   . HIS   B 1 17  ? -45.386 -49.605 29.760 1.00 21.00 ? 17  HIS   A O   1 
ATOM   2191 C  CB  . HIS   B 1 17  ? -45.871 -48.893 32.728 1.00 24.48 ? 17  HIS   A CB  1 
ATOM   2192 C  CG  . HIS   B 1 17  ? -46.134 -49.450 34.090 1.00 31.15 ? 17  HIS   A CG  1 
ATOM   2193 N  ND1 . HIS   B 1 17  ? -46.600 -50.741 34.268 1.00 31.50 ? 17  HIS   A ND1 1 
ATOM   2194 C  CD2 . HIS   B 1 17  ? -45.975 -48.923 35.329 1.00 34.45 ? 17  HIS   A CD2 1 
ATOM   2195 C  CE1 . HIS   B 1 17  ? -46.690 -51.003 35.560 1.00 34.50 ? 17  HIS   A CE1 1 
ATOM   2196 N  NE2 . HIS   B 1 17  ? -46.331 -49.893 36.239 1.00 34.68 ? 17  HIS   A NE2 1 
ATOM   2197 N  N   . TRP   B 1 18  ? -43.468 -48.533 30.170 1.00 20.80 ? 18  TRP   A N   1 
ATOM   2198 C  CA  . TRP   B 1 18  ? -43.417 -48.131 28.767 1.00 19.24 ? 18  TRP   A CA  1 
ATOM   2199 C  C   . TRP   B 1 18  ? -43.430 -49.326 27.792 1.00 19.32 ? 18  TRP   A C   1 
ATOM   2200 O  O   . TRP   B 1 18  ? -43.993 -49.189 26.699 1.00 19.78 ? 18  TRP   A O   1 
ATOM   2201 C  CB  . TRP   B 1 18  ? -42.219 -47.194 28.532 1.00 16.67 ? 18  TRP   A CB  1 
ATOM   2202 C  CG  . TRP   B 1 18  ? -42.332 -45.910 29.270 1.00 15.76 ? 18  TRP   A CG  1 
ATOM   2203 C  CD1 . TRP   B 1 18  ? -43.421 -45.409 29.925 1.00 15.04 ? 18  TRP   A CD1 1 
ATOM   2204 C  CD2 . TRP   B 1 18  ? -41.305 -44.893 29.358 1.00 14.20 ? 18  TRP   A CD2 1 
ATOM   2205 N  NE1 . TRP   B 1 18  ? -43.123 -44.167 30.471 1.00 16.75 ? 18  TRP   A NE1 1 
ATOM   2206 C  CE2 . TRP   B 1 18  ? -41.829 -43.842 30.136 1.00 14.86 ? 18  TRP   A CE2 1 
ATOM   2207 C  CE3 . TRP   B 1 18  ? -39.973 -44.836 28.871 1.00 13.80 ? 18  TRP   A CE3 1 
ATOM   2208 C  CZ2 . TRP   B 1 18  ? -41.098 -42.678 30.413 1.00 14.31 ? 18  TRP   A CZ2 1 
ATOM   2209 C  CZ3 . TRP   B 1 18  ? -39.238 -43.709 29.191 1.00 14.08 ? 18  TRP   A CZ3 1 
ATOM   2210 C  CH2 . TRP   B 1 18  ? -39.798 -42.652 29.916 1.00 12.86 ? 18  TRP   A CH2 1 
ATOM   2211 N  N   . LYS   B 1 19  ? -42.792 -50.451 28.155 1.00 21.01 ? 19  LYS   A N   1 
ATOM   2212 C  CA  . LYS   B 1 19  ? -42.717 -51.617 27.268 1.00 24.37 ? 19  LYS   A CA  1 
ATOM   2213 C  C   . LYS   B 1 19  ? -44.109 -52.191 26.995 1.00 24.55 ? 19  LYS   A C   1 
ATOM   2214 O  O   . LYS   B 1 19  ? -44.267 -52.979 26.062 1.00 24.67 ? 19  LYS   A O   1 
ATOM   2215 C  CB  . LYS   B 1 19  ? -41.866 -52.710 27.920 1.00 25.25 ? 19  LYS   A CB  1 
ATOM   2216 C  CG  . LYS   B 1 19  ? -42.402 -53.164 29.289 1.00 28.07 ? 19  LYS   A CG  1 
ATOM   2217 C  CD  . LYS   B 1 19  ? -41.584 -54.198 30.058 1.00 33.72 ? 19  LYS   A CD  1 
ATOM   2218 C  CE  . LYS   B 1 19  ? -40.248 -53.683 30.557 1.00 37.66 ? 19  LYS   A CE  1 
ATOM   2219 N  NZ  . LYS   B 1 19  ? -40.356 -52.908 31.825 1.00 34.05 ? 19  LYS   A NZ  1 
ATOM   2220 N  N   . GLU   B 1 20  ? -45.115 -51.772 27.771 1.00 25.85 ? 20  GLU   A N   1 
ATOM   2221 C  CA  . GLU   B 1 20  ? -46.489 -52.222 27.548 1.00 28.11 ? 20  GLU   A CA  1 
ATOM   2222 C  C   . GLU   B 1 20  ? -47.091 -51.627 26.274 1.00 29.74 ? 20  GLU   A C   1 
ATOM   2223 O  O   . GLU   B 1 20  ? -48.005 -52.206 25.663 1.00 31.44 ? 20  GLU   A O   1 
ATOM   2224 C  CB  . GLU   B 1 20  ? -47.362 -51.963 28.769 1.00 29.98 ? 20  GLU   A CB  1 
ATOM   2225 C  CG  . GLU   B 1 20  ? -47.043 -52.904 29.915 1.00 35.78 ? 20  GLU   A CG  1 
ATOM   2226 C  CD  . GLU   B 1 20  ? -47.447 -52.417 31.309 1.00 44.44 ? 20  GLU   A CD  1 
ATOM   2227 O  OE1 . GLU   B 1 20  ? -48.433 -51.624 31.413 1.00 47.90 ? 20  GLU   A OE1 1 
ATOM   2228 O  OE2 . GLU   B 1 20  ? -46.748 -52.793 32.297 1.00 45.05 ? 20  GLU   A OE2 1 
ATOM   2229 N  N   . PHE   B 1 21  ? -46.586 -50.468 25.853 1.00 24.16 ? 21  PHE   A N   1 
ATOM   2230 C  CA  . PHE   B 1 21  ? -47.157 -49.805 24.702 1.00 23.90 ? 21  PHE   A CA  1 
ATOM   2231 C  C   . PHE   B 1 21  ? -46.129 -49.510 23.625 1.00 22.43 ? 21  PHE   A C   1 
ATOM   2232 O  O   . PHE   B 1 21  ? -46.533 -49.189 22.516 1.00 25.82 ? 21  PHE   A O   1 
ATOM   2233 C  CB  . PHE   B 1 21  ? -48.001 -48.584 25.086 1.00 29.44 ? 21  PHE   A CB  1 
ATOM   2234 C  CG  . PHE   B 1 21  ? -49.284 -48.943 25.801 1.00 35.00 ? 21  PHE   A CG  1 
ATOM   2235 C  CD1 . PHE   B 1 21  ? -49.292 -49.163 27.179 1.00 38.51 ? 21  PHE   A CD1 1 
ATOM   2236 C  CD2 . PHE   B 1 21  ? -50.471 -49.101 25.085 1.00 43.38 ? 21  PHE   A CD2 1 
ATOM   2237 C  CE1 . PHE   B 1 21  ? -50.465 -49.528 27.833 1.00 42.66 ? 21  PHE   A CE1 1 
ATOM   2238 C  CE2 . PHE   B 1 21  ? -51.644 -49.463 25.737 1.00 42.97 ? 21  PHE   A CE2 1 
ATOM   2239 C  CZ  . PHE   B 1 21  ? -51.635 -49.672 27.108 1.00 45.75 ? 21  PHE   A CZ  1 
ATOM   2240 N  N   . PHE   B 1 22  ? -44.823 -49.630 23.928 1.00 21.19 ? 22  PHE   A N   1 
ATOM   2241 C  CA  . PHE   B 1 22  ? -43.823 -49.183 22.977 1.00 21.17 ? 22  PHE   A CA  1 
ATOM   2242 C  C   . PHE   B 1 22  ? -42.894 -50.359 22.756 1.00 19.74 ? 22  PHE   A C   1 
ATOM   2243 O  O   . PHE   B 1 22  ? -42.078 -50.658 23.607 1.00 20.30 ? 22  PHE   A O   1 
ATOM   2244 C  CB  . PHE   B 1 22  ? -43.103 -47.905 23.475 1.00 21.68 ? 22  PHE   A CB  1 
ATOM   2245 C  CG  . PHE   B 1 22  ? -44.056 -46.748 23.633 1.00 20.57 ? 22  PHE   A CG  1 
ATOM   2246 C  CD1 . PHE   B 1 22  ? -44.443 -46.016 22.525 1.00 23.74 ? 22  PHE   A CD1 1 
ATOM   2247 C  CD2 . PHE   B 1 22  ? -44.588 -46.434 24.871 1.00 20.27 ? 22  PHE   A CD2 1 
ATOM   2248 C  CE1 . PHE   B 1 22  ? -45.402 -45.022 22.642 1.00 20.97 ? 22  PHE   A CE1 1 
ATOM   2249 C  CE2 . PHE   B 1 22  ? -45.571 -45.457 24.981 1.00 22.85 ? 22  PHE   A CE2 1 
ATOM   2250 C  CZ  . PHE   B 1 22  ? -45.939 -44.722 23.883 1.00 22.35 ? 22  PHE   A CZ  1 
ATOM   2251 N  N   . PRO   B 1 23  ? -43.061 -51.031 21.606 1.00 20.96 ? 23  PRO   A N   1 
ATOM   2252 C  CA  . PRO   B 1 23  ? -42.397 -52.293 21.291 1.00 22.80 ? 23  PRO   A CA  1 
ATOM   2253 C  C   . PRO   B 1 23  ? -40.878 -52.274 21.473 1.00 24.73 ? 23  PRO   A C   1 
ATOM   2254 O  O   . PRO   B 1 23  ? -40.302 -53.212 22.021 1.00 28.19 ? 23  PRO   A O   1 
ATOM   2255 C  CB  . PRO   B 1 23  ? -42.770 -52.517 19.815 1.00 23.30 ? 23  PRO   A CB  1 
ATOM   2256 C  CG  . PRO   B 1 23  ? -44.166 -51.889 19.728 1.00 25.45 ? 23  PRO   A CG  1 
ATOM   2257 C  CD  . PRO   B 1 23  ? -44.097 -50.655 20.609 1.00 23.73 ? 23  PRO   A CD  1 
ATOM   2258 N  N   . ILE   B 1 24  ? -40.259 -51.148 21.116 1.00 21.59 ? 24  ILE   A N   1 
ATOM   2259 C  CA  . ILE   B 1 24  ? -38.791 -51.108 21.114 1.00 17.98 ? 24  ILE   A CA  1 
ATOM   2260 C  C   . ILE   B 1 24  ? -38.158 -50.812 22.493 1.00 20.42 ? 24  ILE   A C   1 
ATOM   2261 O  O   . ILE   B 1 24  ? -36.936 -50.656 22.580 1.00 18.22 ? 24  ILE   A O   1 
ATOM   2262 C  CB  . ILE   B 1 24  ? -38.353 -50.082 20.058 1.00 18.56 ? 24  ILE   A CB  1 
ATOM   2263 C  CG1 . ILE   B 1 24  ? -36.898 -50.262 19.580 1.00 20.40 ? 24  ILE   A CG1 1 
ATOM   2264 C  CG2 . ILE   B 1 24  ? -38.636 -48.652 20.556 1.00 17.57 ? 24  ILE   A CG2 1 
ATOM   2265 C  CD1 . ILE   B 1 24  ? -36.605 -51.609 18.914 1.00 23.93 ? 24  ILE   A CD1 1 
ATOM   2266 N  N   . ALA   B 1 25  ? -38.944 -50.662 23.561 1.00 17.69 ? 25  ALA   A N   1 
ATOM   2267 C  CA  . ALA   B 1 25  ? -38.379 -50.309 24.875 1.00 19.18 ? 25  ALA   A CA  1 
ATOM   2268 C  C   . ALA   B 1 25  ? -37.279 -51.237 25.404 1.00 20.49 ? 25  ALA   A C   1 
ATOM   2269 O  O   . ALA   B 1 25  ? -36.500 -50.788 26.264 1.00 19.24 ? 25  ALA   A O   1 
ATOM   2270 C  CB  . ALA   B 1 25  ? -39.484 -50.171 25.903 1.00 19.31 ? 25  ALA   A CB  1 
ATOM   2271 N  N   . ASP   B 1 26  ? -37.296 -52.526 24.989 1.00 23.15 ? 26  ASP   A N   1 
ATOM   2272 C  CA  . ASP   B 1 26  ? -36.293 -53.514 25.398 1.00 24.30 ? 26  ASP   A CA  1 
ATOM   2273 C  C   . ASP   B 1 26  ? -35.373 -53.889 24.227 1.00 23.80 ? 26  ASP   A C   1 
ATOM   2274 O  O   . ASP   B 1 26  ? -34.842 -55.007 24.153 1.00 22.26 ? 26  ASP   A O   1 
ATOM   2275 C  CB  . ASP   B 1 26  ? -36.957 -54.778 25.962 1.00 28.33 ? 26  ASP   A CB  1 
ATOM   2276 C  CG  . ASP   B 1 26  ? -37.563 -54.576 27.349 1.00 37.14 ? 26  ASP   A CG  1 
ATOM   2277 O  OD1 . ASP   B 1 26  ? -36.956 -53.836 28.174 1.00 40.33 ? 26  ASP   A OD1 1 
ATOM   2278 O  OD2 . ASP   B 1 26  ? -38.636 -55.174 27.612 1.00 47.30 ? 26  ASP   A OD2 1 
ATOM   2279 N  N   . GLY   B 1 27  ? -35.182 -52.936 23.299 1.00 21.75 ? 27  GLY   A N   1 
ATOM   2280 C  CA  . GLY   B 1 27  ? -34.400 -53.140 22.088 1.00 18.80 ? 27  GLY   A CA  1 
ATOM   2281 C  C   . GLY   B 1 27  ? -32.887 -53.183 22.373 1.00 17.47 ? 27  GLY   A C   1 
ATOM   2282 O  O   . GLY   B 1 27  ? -32.459 -53.076 23.518 1.00 21.86 ? 27  GLY   A O   1 
ATOM   2283 N  N   . ASP   B 1 28  ? -32.106 -53.312 21.305 1.00 16.89 ? 28  ASP   A N   1 
ATOM   2284 C  CA  . ASP   B 1 28  ? -30.672 -53.537 21.413 1.00 18.02 ? 28  ASP   A CA  1 
ATOM   2285 C  C   . ASP   B 1 28  ? -29.920 -52.208 21.547 1.00 17.52 ? 28  ASP   A C   1 
ATOM   2286 O  O   . ASP   B 1 28  ? -28.745 -52.205 21.913 1.00 17.67 ? 28  ASP   A O   1 
ATOM   2287 C  CB  . ASP   B 1 28  ? -30.174 -54.294 20.169 1.00 20.69 ? 28  ASP   A CB  1 
ATOM   2288 C  CG  . ASP   B 1 28  ? -30.300 -55.812 20.268 1.00 25.14 ? 28  ASP   A CG  1 
ATOM   2289 O  OD1 . ASP   B 1 28  ? -30.158 -56.330 21.376 1.00 26.87 ? 28  ASP   A OD1 1 
ATOM   2290 O  OD2 . ASP   B 1 28  ? -30.561 -56.441 19.241 1.00 33.66 ? 28  ASP   A OD2 1 
ATOM   2291 N  N   . GLN   B 1 29  ? -30.569 -51.075 21.187 1.00 17.97 ? 29  GLN   A N   1 
ATOM   2292 C  CA  . GLN   B 1 29  ? -29.854 -49.797 21.230 1.00 14.81 ? 29  GLN   A CA  1 
ATOM   2293 C  C   . GLN   B 1 29  ? -30.619 -48.750 22.035 1.00 14.59 ? 29  GLN   A C   1 
ATOM   2294 O  O   . GLN   B 1 29  ? -30.779 -47.623 21.560 1.00 14.03 ? 29  GLN   A O   1 
ATOM   2295 C  CB  . GLN   B 1 29  ? -29.524 -49.253 19.839 1.00 16.85 ? 29  GLN   A CB  1 
ATOM   2296 C  CG  . GLN   B 1 29  ? -28.694 -50.277 19.042 1.00 17.72 ? 29  GLN   A CG  1 
ATOM   2297 C  CD  . GLN   B 1 29  ? -28.036 -49.725 17.792 1.00 23.28 ? 29  GLN   A CD  1 
ATOM   2298 O  OE1 . GLN   B 1 29  ? -28.285 -48.592 17.375 1.00 21.69 ? 29  GLN   A OE1 1 
ATOM   2299 N  NE2 . GLN   B 1 29  ? -27.121 -50.510 17.215 1.00 27.64 ? 29  GLN   A NE2 1 
ATOM   2300 N  N   . GLN   B 1 30  ? -31.018 -49.087 23.265 1.00 12.91 ? 30  GLN   A N   1 
ATOM   2301 C  CA  . GLN   B 1 30  ? -31.778 -48.132 24.079 1.00 12.34 ? 30  GLN   A CA  1 
ATOM   2302 C  C   . GLN   B 1 30  ? -30.888 -47.235 24.939 1.00 13.22 ? 30  GLN   A C   1 
ATOM   2303 O  O   . GLN   B 1 30  ? -29.736 -47.550 25.269 1.00 14.30 ? 30  GLN   A O   1 
ATOM   2304 C  CB  . GLN   B 1 30  ? -32.742 -48.908 24.986 1.00 13.59 ? 30  GLN   A CB  1 
ATOM   2305 C  CG  . GLN   B 1 30  ? -33.870 -49.555 24.173 1.00 13.94 ? 30  GLN   A CG  1 
ATOM   2306 C  CD  . GLN   B 1 30  ? -34.813 -48.482 23.632 1.00 14.88 ? 30  GLN   A CD  1 
ATOM   2307 O  OE1 . GLN   B 1 30  ? -35.534 -47.844 24.407 1.00 14.23 ? 30  GLN   A OE1 1 
ATOM   2308 N  NE2 . GLN   B 1 30  ? -34.880 -48.321 22.306 1.00 14.07 ? 30  GLN   A NE2 1 
ATOM   2309 N  N   . SER   B 1 31  ? -31.452 -46.058 25.292 1.00 13.12 ? 31  SER   A N   1 
ATOM   2310 C  CA  . SER   B 1 31  ? -30.730 -45.050 26.079 1.00 11.14 ? 31  SER   A CA  1 
ATOM   2311 C  C   . SER   B 1 31  ? -31.579 -44.686 27.285 1.00 11.58 ? 31  SER   A C   1 
ATOM   2312 O  O   . SER   B 1 31  ? -32.803 -44.892 27.220 1.00 12.93 ? 31  SER   A O   1 
ATOM   2313 C  CB  . SER   B 1 31  ? -30.466 -43.791 25.206 1.00 12.00 ? 31  SER   A CB  1 
ATOM   2314 O  OG  . SER   B 1 31  ? -29.548 -44.123 24.173 1.00 12.74 ? 31  SER   A OG  1 
ATOM   2315 N  N   . PRO   B 1 32  ? -31.057 -44.067 28.366 1.00 11.64 ? 32  PRO   A N   1 
ATOM   2316 C  CA  . PRO   B 1 32  ? -29.629 -43.797 28.542 1.00 11.60 ? 32  PRO   A CA  1 
ATOM   2317 C  C   . PRO   B 1 32  ? -28.880 -45.066 28.969 1.00 12.71 ? 32  PRO   A C   1 
ATOM   2318 O  O   . PRO   B 1 32  ? -29.462 -46.155 28.991 1.00 13.89 ? 32  PRO   A O   1 
ATOM   2319 C  CB  . PRO   B 1 32  ? -29.675 -42.731 29.669 1.00 13.05 ? 32  PRO   A CB  1 
ATOM   2320 C  CG  . PRO   B 1 32  ? -30.856 -43.168 30.558 1.00 12.66 ? 32  PRO   A CG  1 
ATOM   2321 C  CD  . PRO   B 1 32  ? -31.887 -43.659 29.545 1.00 12.22 ? 32  PRO   A CD  1 
ATOM   2322 N  N   . ILE   B 1 33  ? -27.589 -44.889 29.283 1.00 12.97 ? 33  ILE   A N   1 
ATOM   2323 C  CA  . ILE   B 1 33  ? -26.702 -46.003 29.609 1.00 14.35 ? 33  ILE   A CA  1 
ATOM   2324 C  C   . ILE   B 1 33  ? -25.821 -45.594 30.778 1.00 14.57 ? 33  ILE   A C   1 
ATOM   2325 O  O   . ILE   B 1 33  ? -25.670 -44.402 31.088 1.00 12.73 ? 33  ILE   A O   1 
ATOM   2326 C  CB  . ILE   B 1 33  ? -25.803 -46.437 28.432 1.00 13.88 ? 33  ILE   A CB  1 
ATOM   2327 C  CG1 . ILE   B 1 33  ? -24.872 -45.280 28.000 1.00 15.24 ? 33  ILE   A CG1 1 
ATOM   2328 C  CG2 . ILE   B 1 33  ? -26.626 -47.015 27.283 1.00 14.20 ? 33  ILE   A CG2 1 
ATOM   2329 C  CD1 . ILE   B 1 33  ? -23.648 -45.739 27.263 1.00 17.82 ? 33  ILE   A CD1 1 
ATOM   2330 N  N   . GLU   B 1 34  ? -25.180 -46.621 31.382 1.00 13.92 ? 34  GLU   A N   1 
ATOM   2331 C  CA  . GLU   B 1 34  ? -24.056 -46.379 32.287 1.00 15.44 ? 34  GLU   A CA  1 
ATOM   2332 C  C   . GLU   B 1 34  ? -22.741 -46.357 31.507 1.00 15.21 ? 34  GLU   A C   1 
ATOM   2333 O  O   . GLU   B 1 34  ? -22.538 -47.194 30.632 1.00 17.23 ? 34  GLU   A O   1 
ATOM   2334 C  CB  . GLU   B 1 34  ? -24.004 -47.557 33.279 1.00 16.44 ? 34  GLU   A CB  1 
ATOM   2335 C  CG  . GLU   B 1 34  ? -25.125 -47.544 34.320 1.00 20.16 ? 34  GLU   A CG  1 
ATOM   2336 C  CD  . GLU   B 1 34  ? -24.797 -48.445 35.533 1.00 26.16 ? 34  GLU   A CD  1 
ATOM   2337 O  OE1 . GLU   B 1 34  ? -24.078 -47.979 36.484 1.00 31.85 ? 34  GLU   A OE1 1 
ATOM   2338 O  OE2 . GLU   B 1 34  ? -25.215 -49.629 35.494 1.00 23.13 ? 34  GLU   A OE2 1 
ATOM   2339 N  N   . ILE   B 1 35  ? -21.918 -45.316 31.762 1.00 15.51 ? 35  ILE   A N   1 
ATOM   2340 C  CA  . ILE   B 1 35  ? -20.612 -45.175 31.107 1.00 17.25 ? 35  ILE   A CA  1 
ATOM   2341 C  C   . ILE   B 1 35  ? -19.509 -45.590 32.085 1.00 17.98 ? 35  ILE   A C   1 
ATOM   2342 O  O   . ILE   B 1 35  ? -19.294 -44.918 33.056 1.00 18.54 ? 35  ILE   A O   1 
ATOM   2343 C  CB  . ILE   B 1 35  ? -20.372 -43.708 30.657 1.00 18.39 ? 35  ILE   A CB  1 
ATOM   2344 C  CG1 . ILE   B 1 35  ? -21.432 -43.279 29.642 1.00 18.63 ? 35  ILE   A CG1 1 
ATOM   2345 C  CG2 . ILE   B 1 35  ? -18.953 -43.533 30.101 1.00 17.77 ? 35  ILE   A CG2 1 
ATOM   2346 C  CD1 . ILE   B 1 35  ? -21.572 -41.780 29.505 1.00 19.56 ? 35  ILE   A CD1 1 
ATOM   2347 N  N   . LYS   B 1 36  ? -18.818 -46.690 31.792 1.00 19.56 ? 36  LYS   A N   1 
ATOM   2348 C  CA  . LYS   B 1 36  ? -17.679 -47.105 32.608 1.00 23.45 ? 36  LYS   A CA  1 
ATOM   2349 C  C   . LYS   B 1 36  ? -16.393 -46.603 31.950 1.00 21.69 ? 36  LYS   A C   1 
ATOM   2350 O  O   . LYS   B 1 36  ? -16.001 -47.140 30.918 1.00 24.04 ? 36  LYS   A O   1 
ATOM   2351 C  CB  . LYS   B 1 36  ? -17.672 -48.640 32.648 1.00 26.72 ? 36  LYS   A CB  1 
ATOM   2352 C  CG  . LYS   B 1 36  ? -16.573 -49.316 33.479 1.00 28.43 ? 36  LYS   A CG  1 
ATOM   2353 C  CD  . LYS   B 1 36  ? -16.909 -50.803 33.718 1.00 31.29 ? 36  LYS   A CD  1 
ATOM   2354 C  CE  . LYS   B 1 36  ? -18.042 -51.021 34.722 1.00 36.77 ? 36  LYS   A CE  1 
ATOM   2355 N  NZ  . LYS   B 1 36  ? -18.195 -52.433 35.158 1.00 32.04 ? 36  LYS   A NZ  1 
ATOM   2356 N  N   . THR   B 1 37  ? -15.738 -45.620 32.567 1.00 23.14 ? 37  THR   A N   1 
ATOM   2357 C  CA  . THR   B 1 37  ? -14.661 -44.902 31.873 1.00 27.85 ? 37  THR   A CA  1 
ATOM   2358 C  C   . THR   B 1 37  ? -13.489 -45.823 31.479 1.00 33.67 ? 37  THR   A C   1 
ATOM   2359 O  O   . THR   B 1 37  ? -12.894 -45.652 30.413 1.00 29.34 ? 37  THR   A O   1 
ATOM   2360 C  CB  . THR   B 1 37  ? -14.231 -43.626 32.612 1.00 29.55 ? 37  THR   A CB  1 
ATOM   2361 O  OG1 . THR   B 1 37  ? -13.658 -43.991 33.861 1.00 30.38 ? 37  THR   A OG1 1 
ATOM   2362 C  CG2 . THR   B 1 37  ? -15.339 -42.633 32.882 1.00 28.98 ? 37  THR   A CG2 1 
ATOM   2363 N  N   . LYS   B 1 38  ? -13.181 -46.836 32.297 1.00 29.93 ? 38  LYS   A N   1 
ATOM   2364 C  CA  . LYS   B 1 38  ? -12.066 -47.732 32.000 1.00 33.51 ? 38  LYS   A CA  1 
ATOM   2365 C  C   . LYS   B 1 38  ? -12.346 -48.617 30.773 1.00 35.61 ? 38  LYS   A C   1 
ATOM   2366 O  O   . LYS   B 1 38  ? -11.424 -49.178 30.184 1.00 38.92 ? 38  LYS   A O   1 
ATOM   2367 C  CB  . LYS   B 1 38  ? -11.662 -48.512 33.262 1.00 37.84 ? 38  LYS   A CB  1 
ATOM   2368 N  N   . GLU   B 1 39  ? -13.615 -48.732 30.345 1.00 32.32 ? 39  GLU   A N   1 
ATOM   2369 C  CA  . GLU   B 1 39  ? -13.961 -49.537 29.180 1.00 31.49 ? 39  GLU   A CA  1 
ATOM   2370 C  C   . GLU   B 1 39  ? -14.097 -48.659 27.916 1.00 33.81 ? 39  GLU   A C   1 
ATOM   2371 O  O   . GLU   B 1 39  ? -14.503 -49.154 26.859 1.00 30.71 ? 39  GLU   A O   1 
ATOM   2372 C  CB  . GLU   B 1 39  ? -15.251 -50.343 29.437 1.00 38.62 ? 39  GLU   A CB  1 
ATOM   2373 C  CG  . GLU   B 1 39  ? -15.058 -51.661 30.193 1.00 43.41 ? 39  GLU   A CG  1 
ATOM   2374 N  N   . VAL   B 1 40  ? -13.769 -47.359 28.006 1.00 29.58 ? 40  VAL   A N   1 
ATOM   2375 C  CA  . VAL   B 1 40  ? -14.073 -46.464 26.891 1.00 27.00 ? 40  VAL   A CA  1 
ATOM   2376 C  C   . VAL   B 1 40  ? -13.024 -46.658 25.799 1.00 33.72 ? 40  VAL   A C   1 
ATOM   2377 O  O   . VAL   B 1 40  ? -11.839 -46.705 26.109 1.00 34.45 ? 40  VAL   A O   1 
ATOM   2378 C  CB  . VAL   B 1 40  ? -14.205 -44.992 27.337 1.00 26.71 ? 40  VAL   A CB  1 
ATOM   2379 C  CG1 . VAL   B 1 40  ? -14.088 -44.026 26.141 1.00 25.48 ? 40  VAL   A CG1 1 
ATOM   2380 C  CG2 . VAL   B 1 40  ? -15.538 -44.781 28.067 1.00 24.78 ? 40  VAL   A CG2 1 
ATOM   2381 N  N   . LYS   B 1 41  ? -13.484 -46.749 24.544 1.00 27.74 ? 41  LYS   A N   1 
ATOM   2382 C  CA  . LYS   B 1 41  ? -12.618 -46.936 23.388 1.00 32.75 ? 41  LYS   A CA  1 
ATOM   2383 C  C   . LYS   B 1 41  ? -12.212 -45.574 22.800 1.00 32.09 ? 41  LYS   A C   1 
ATOM   2384 O  O   . LYS   B 1 41  ? -13.024 -44.904 22.179 1.00 27.69 ? 41  LYS   A O   1 
ATOM   2385 C  CB  . LYS   B 1 41  ? -13.345 -47.847 22.389 1.00 35.70 ? 41  LYS   A CB  1 
ATOM   2386 C  CG  . LYS   B 1 41  ? -12.692 -48.030 21.020 1.00 42.22 ? 41  LYS   A CG  1 
ATOM   2387 C  CD  . LYS   B 1 41  ? -13.697 -48.274 19.904 1.00 49.07 ? 41  LYS   A CD  1 
ATOM   2388 N  N   . TYR   B 1 42  ? -10.944 -45.158 22.963 1.00 34.44 ? 42  TYR   A N   1 
ATOM   2389 C  CA  . TYR   B 1 42  ? -10.481 -43.949 22.277 1.00 34.66 ? 42  TYR   A CA  1 
ATOM   2390 C  C   . TYR   B 1 42  ? -10.344 -44.246 20.774 1.00 30.08 ? 42  TYR   A C   1 
ATOM   2391 O  O   . TYR   B 1 42  ? -9.851  -45.318 20.392 1.00 29.99 ? 42  TYR   A O   1 
ATOM   2392 C  CB  . TYR   B 1 42  ? -9.253  -43.330 22.957 1.00 39.95 ? 42  TYR   A CB  1 
ATOM   2393 C  CG  . TYR   B 1 42  ? -8.616  -42.193 22.181 1.00 57.48 ? 42  TYR   A CG  1 
ATOM   2394 C  CD1 . TYR   B 1 42  ? -7.636  -42.431 21.215 1.00 68.94 ? 42  TYR   A CD1 1 
ATOM   2395 C  CD2 . TYR   B 1 42  ? -8.995  -40.870 22.386 1.00 65.70 ? 42  TYR   A CD2 1 
ATOM   2396 C  CE1 . TYR   B 1 42  ? -7.055  -41.408 20.474 1.00 62.89 ? 42  TYR   A CE1 1 
ATOM   2397 C  CE2 . TYR   B 1 42  ? -8.423  -39.832 21.659 1.00 67.84 ? 42  TYR   A CE2 1 
ATOM   2398 C  CZ  . TYR   B 1 42  ? -7.448  -40.100 20.709 1.00 70.58 ? 42  TYR   A CZ  1 
ATOM   2399 O  OH  . TYR   B 1 42  ? -6.898  -39.077 19.994 1.00 64.55 ? 42  TYR   A OH  1 
ATOM   2400 N  N   . ASP   B 1 43  ? -10.869 -43.345 19.906 1.00 23.76 ? 43  ASP   A N   1 
ATOM   2401 C  CA  . ASP   B 1 43  ? -11.028 -43.642 18.489 1.00 25.41 ? 43  ASP   A CA  1 
ATOM   2402 C  C   . ASP   B 1 43  ? -10.470 -42.479 17.669 1.00 25.37 ? 43  ASP   A C   1 
ATOM   2403 O  O   . ASP   B 1 43  ? -10.974 -41.358 17.722 1.00 23.01 ? 43  ASP   A O   1 
ATOM   2404 C  CB  . ASP   B 1 43  ? -12.505 -43.910 18.109 1.00 28.60 ? 43  ASP   A CB  1 
ATOM   2405 C  CG  . ASP   B 1 43  ? -12.711 -44.467 16.696 1.00 31.05 ? 43  ASP   A CG  1 
ATOM   2406 O  OD1 . ASP   B 1 43  ? -11.991 -44.051 15.768 1.00 30.75 ? 43  ASP   A OD1 1 
ATOM   2407 O  OD2 . ASP   B 1 43  ? -13.613 -45.340 16.523 1.00 35.31 ? 43  ASP   A OD2 1 
ATOM   2408 N  N   . SER   B 1 44  ? -9.409  -42.753 16.899 1.00 26.20 ? 44  SER   A N   1 
ATOM   2409 C  CA  . SER   B 1 44  ? -8.718  -41.694 16.174 1.00 24.75 ? 44  SER   A CA  1 
ATOM   2410 C  C   . SER   B 1 44  ? -9.544  -41.180 14.983 1.00 21.64 ? 44  SER   A C   1 
ATOM   2411 O  O   . SER   B 1 44  ? -9.222  -40.142 14.387 1.00 22.61 ? 44  SER   A O   1 
ATOM   2412 C  CB  . SER   B 1 44  ? -7.338  -42.208 15.719 1.00 25.69 ? 44  SER   A CB  1 
ATOM   2413 O  OG  . SER   B 1 44  ? -7.533  -43.316 14.843 1.00 31.06 ? 44  SER   A OG  1 
ATOM   2414 N  N   . SER   B 1 45  ? -10.634 -41.869 14.643 1.00 21.42 ? 45  SER   A N   1 
ATOM   2415 C  CA  . SER   B 1 45  ? -11.425 -41.443 13.498 1.00 20.72 ? 45  SER   A CA  1 
ATOM   2416 C  C   . SER   B 1 45  ? -12.431 -40.364 13.911 1.00 21.85 ? 45  SER   A C   1 
ATOM   2417 O  O   . SER   B 1 45  ? -12.998 -39.715 13.037 1.00 22.27 ? 45  SER   A O   1 
ATOM   2418 C  CB  . SER   B 1 45  ? -12.106 -42.614 12.781 1.00 25.41 ? 45  SER   A CB  1 
ATOM   2419 O  OG  . SER   B 1 45  ? -13.181 -43.133 13.565 1.00 28.34 ? 45  SER   A OG  1 
ATOM   2420 N  N   . LEU   B 1 46  ? -12.681 -40.217 15.221 1.00 19.77 ? 46  LEU   A N   1 
ATOM   2421 C  CA  . LEU   B 1 46  ? -13.577 -39.143 15.685 1.00 20.58 ? 46  LEU   A CA  1 
ATOM   2422 C  C   . LEU   B 1 46  ? -12.920 -37.781 15.433 1.00 23.66 ? 46  LEU   A C   1 
ATOM   2423 O  O   . LEU   B 1 46  ? -11.699 -37.656 15.513 1.00 23.25 ? 46  LEU   A O   1 
ATOM   2424 C  CB  . LEU   B 1 46  ? -13.835 -39.311 17.196 1.00 21.33 ? 46  LEU   A CB  1 
ATOM   2425 C  CG  . LEU   B 1 46  ? -14.667 -40.539 17.561 1.00 22.75 ? 46  LEU   A CG  1 
ATOM   2426 C  CD1 . LEU   B 1 46  ? -14.670 -40.734 19.073 1.00 24.34 ? 46  LEU   A CD1 1 
ATOM   2427 C  CD2 . LEU   B 1 46  ? -16.106 -40.390 17.019 1.00 20.72 ? 46  LEU   A CD2 1 
ATOM   2428 N  N   . ARG   B 1 47  ? -13.757 -36.757 15.207 1.00 25.71 ? 47  ARG   A N   1 
ATOM   2429 C  CA  . ARG   B 1 47  ? -13.347 -35.369 14.976 1.00 26.95 ? 47  ARG   A CA  1 
ATOM   2430 C  C   . ARG   B 1 47  ? -13.776 -34.561 16.209 1.00 26.07 ? 47  ARG   A C   1 
ATOM   2431 O  O   . ARG   B 1 47  ? -14.575 -35.030 17.031 1.00 29.12 ? 47  ARG   A O   1 
ATOM   2432 C  CB  . ARG   B 1 47  ? -14.132 -34.837 13.777 1.00 31.66 ? 47  ARG   A CB  1 
ATOM   2433 C  CG  . ARG   B 1 47  ? -13.507 -34.877 12.386 1.00 36.01 ? 47  ARG   A CG  1 
ATOM   2434 C  CD  . ARG   B 1 47  ? -12.269 -35.751 12.569 1.00 45.05 ? 47  ARG   A CD  1 
ATOM   2435 N  NE  . ARG   B 1 47  ? -11.682 -36.537 11.492 1.00 51.47 ? 47  ARG   A NE  1 
ATOM   2436 C  CZ  . ARG   B 1 47  ? -10.639 -37.346 11.623 1.00 50.44 ? 47  ARG   A CZ  1 
ATOM   2437 N  NH1 . ARG   B 1 47  ? -10.199 -38.037 10.589 1.00 52.06 ? 47  ARG   A NH1 1 
ATOM   2438 N  NH2 . ARG   B 1 47  ? -10.063 -37.503 12.793 1.00 51.23 ? 47  ARG   A NH2 1 
ATOM   2439 N  N   . PRO   B 1 48  ? -13.226 -33.350 16.457 1.00 25.64 ? 48  PRO   A N   1 
ATOM   2440 C  CA  . PRO   B 1 48  ? -13.741 -32.484 17.522 1.00 23.98 ? 48  PRO   A CA  1 
ATOM   2441 C  C   . PRO   B 1 48  ? -15.121 -32.006 17.070 1.00 21.62 ? 48  PRO   A C   1 
ATOM   2442 O  O   . PRO   B 1 48  ? -15.389 -31.986 15.866 1.00 24.05 ? 48  PRO   A O   1 
ATOM   2443 C  CB  . PRO   B 1 48  ? -12.809 -31.250 17.512 1.00 25.59 ? 48  PRO   A CB  1 
ATOM   2444 C  CG  . PRO   B 1 48  ? -11.589 -31.689 16.677 1.00 27.52 ? 48  PRO   A CG  1 
ATOM   2445 C  CD  . PRO   B 1 48  ? -12.105 -32.742 15.712 1.00 28.75 ? 48  PRO   A CD  1 
ATOM   2446 N  N   . LEU   B 1 49  ? -15.972 -31.679 18.061 1.00 25.23 ? 49  LEU   A N   1 
ATOM   2447 C  CA  . LEU   B 1 49  ? -17.284 -31.121 17.822 1.00 22.16 ? 49  LEU   A CA  1 
ATOM   2448 C  C   . LEU   B 1 49  ? -17.109 -29.711 17.235 1.00 21.49 ? 49  LEU   A C   1 
ATOM   2449 O  O   . LEU   B 1 49  ? -16.239 -28.971 17.701 1.00 21.87 ? 49  LEU   A O   1 
ATOM   2450 C  CB  . LEU   B 1 49  ? -17.981 -30.969 19.177 1.00 25.53 ? 49  LEU   A CB  1 
ATOM   2451 C  CG  . LEU   B 1 49  ? -18.984 -32.014 19.633 1.00 27.65 ? 49  LEU   A CG  1 
ATOM   2452 C  CD1 . LEU   B 1 49  ? -18.977 -33.337 18.855 1.00 27.02 ? 49  LEU   A CD1 1 
ATOM   2453 C  CD2 . LEU   B 1 49  ? -19.094 -32.138 21.149 1.00 22.38 ? 49  LEU   A CD2 1 
ATOM   2454 N  N   . SER   B 1 50  ? -17.950 -29.350 16.245 1.00 16.21 ? 50  SER   A N   1 
ATOM   2455 C  CA  . SER   B 1 50  ? -18.099 -27.953 15.820 1.00 15.53 ? 50  SER   A CA  1 
ATOM   2456 C  C   . SER   B 1 50  ? -19.526 -27.522 16.162 1.00 17.70 ? 50  SER   A C   1 
ATOM   2457 O  O   . SER   B 1 50  ? -20.477 -28.113 15.683 1.00 18.25 ? 50  SER   A O   1 
ATOM   2458 C  CB  . SER   B 1 50  ? -17.876 -27.890 14.318 1.00 19.72 ? 50  SER   A CB  1 
ATOM   2459 O  OG  . SER   B 1 50  ? -18.309 -26.620 13.797 1.00 22.17 ? 50  SER   A OG  1 
ATOM   2460 N  N   . ILE   B 1 51  ? -19.682 -26.512 17.016 1.00 17.10 ? 51  ILE   A N   1 
ATOM   2461 C  CA  . ILE   B 1 51  ? -21.009 -26.197 17.529 1.00 19.45 ? 51  ILE   A CA  1 
ATOM   2462 C  C   . ILE   B 1 51  ? -21.191 -24.703 17.310 1.00 23.10 ? 51  ILE   A C   1 
ATOM   2463 O  O   . ILE   B 1 51  ? -20.351 -23.923 17.759 1.00 26.05 ? 51  ILE   A O   1 
ATOM   2464 C  CB  . ILE   B 1 51  ? -21.163 -26.522 19.030 1.00 18.39 ? 51  ILE   A CB  1 
ATOM   2465 C  CG1 . ILE   B 1 51  ? -20.912 -27.992 19.398 1.00 18.34 ? 51  ILE   A CG1 1 
ATOM   2466 C  CG2 . ILE   B 1 51  ? -22.555 -26.089 19.520 1.00 21.84 ? 51  ILE   A CG2 1 
ATOM   2467 C  CD1 . ILE   B 1 51  ? -20.827 -28.276 20.891 1.00 22.50 ? 51  ILE   A CD1 1 
ATOM   2468 N  N   . LYS   B 1 52  ? -22.199 -24.325 16.511 1.00 22.42 ? 52  LYS   A N   1 
ATOM   2469 C  CA  . LYS   B 1 52  ? -22.489 -22.896 16.403 1.00 22.79 ? 52  LYS   A CA  1 
ATOM   2470 C  C   . LYS   B 1 52  ? -23.978 -22.721 16.665 1.00 20.58 ? 52  LYS   A C   1 
ATOM   2471 O  O   . LYS   B 1 52  ? -24.768 -23.379 15.989 1.00 19.49 ? 52  LYS   A O   1 
ATOM   2472 C  CB  . LYS   B 1 52  ? -22.137 -22.420 14.998 1.00 27.75 ? 52  LYS   A CB  1 
ATOM   2473 C  CG  . LYS   B 1 52  ? -22.630 -21.019 14.639 1.00 32.01 ? 52  LYS   A CG  1 
ATOM   2474 C  CD  . LYS   B 1 52  ? -22.248 -20.524 13.250 1.00 45.26 ? 52  LYS   A CD  1 
ATOM   2475 C  CE  . LYS   B 1 52  ? -23.254 -20.829 12.154 1.00 49.99 ? 52  LYS   A CE  1 
ATOM   2476 N  NZ  . LYS   B 1 52  ? -22.881 -20.189 10.868 1.00 49.23 ? 52  LYS   A NZ  1 
ATOM   2477 N  N   . TYR   B 1 53  ? -24.325 -22.040 17.761 1.00 23.33 ? 53  TYR   A N   1 
ATOM   2478 C  CA  . TYR   B 1 53  ? -25.712 -21.761 18.116 1.00 21.12 ? 53  TYR   A CA  1 
ATOM   2479 C  C   . TYR   B 1 53  ? -25.918 -20.246 17.991 1.00 28.16 ? 53  TYR   A C   1 
ATOM   2480 O  O   . TYR   B 1 53  ? -25.068 -19.446 18.413 1.00 29.85 ? 53  TYR   A O   1 
ATOM   2481 C  CB  . TYR   B 1 53  ? -26.107 -22.332 19.486 1.00 24.59 ? 53  TYR   A CB  1 
ATOM   2482 C  CG  . TYR   B 1 53  ? -26.016 -23.841 19.651 1.00 22.99 ? 53  TYR   A CG  1 
ATOM   2483 C  CD1 . TYR   B 1 53  ? -26.319 -24.715 18.611 1.00 21.34 ? 53  TYR   A CD1 1 
ATOM   2484 C  CD2 . TYR   B 1 53  ? -25.651 -24.405 20.872 1.00 21.85 ? 53  TYR   A CD2 1 
ATOM   2485 C  CE1 . TYR   B 1 53  ? -26.261 -26.097 18.783 1.00 20.52 ? 53  TYR   A CE1 1 
ATOM   2486 C  CE2 . TYR   B 1 53  ? -25.604 -25.783 21.068 1.00 20.08 ? 53  TYR   A CE2 1 
ATOM   2487 C  CZ  . TYR   B 1 53  ? -25.876 -26.630 20.006 1.00 18.86 ? 53  TYR   A CZ  1 
ATOM   2488 O  OH  . TYR   B 1 53  ? -25.794 -27.964 20.243 1.00 20.37 ? 53  TYR   A OH  1 
ATOM   2489 N  N   . ASP   B 1 54  ? -27.010 -19.850 17.322 1.00 20.64 ? 54  ASP   A N   1 
ATOM   2490 C  CA  . ASP   B 1 54  ? -27.327 -18.454 17.115 1.00 19.87 ? 54  ASP   A CA  1 
ATOM   2491 C  C   . ASP   B 1 54  ? -28.499 -18.110 18.020 1.00 19.31 ? 54  ASP   A C   1 
ATOM   2492 O  O   . ASP   B 1 54  ? -29.520 -18.786 18.008 1.00 19.37 ? 54  ASP   A O   1 
ATOM   2493 C  CB  . ASP   B 1 54  ? -27.788 -18.276 15.670 1.00 20.14 ? 54  ASP   A CB  1 
ATOM   2494 C  CG  . ASP   B 1 54  ? -28.125 -16.870 15.241 1.00 25.80 ? 54  ASP   A CG  1 
ATOM   2495 O  OD1 . ASP   B 1 54  ? -28.581 -16.073 16.087 1.00 25.43 ? 54  ASP   A OD1 1 
ATOM   2496 O  OD2 . ASP   B 1 54  ? -27.909 -16.572 14.023 1.00 28.84 ? 54  ASP   A OD2 1 
ATOM   2497 N  N   . PRO   B 1 55  ? -28.336 -17.159 18.956 1.00 17.73 ? 55  PRO   A N   1 
ATOM   2498 C  CA  . PRO   B 1 55  ? -29.384 -16.827 19.916 1.00 17.25 ? 55  PRO   A CA  1 
ATOM   2499 C  C   . PRO   B 1 55  ? -30.699 -16.427 19.265 1.00 20.17 ? 55  PRO   A C   1 
ATOM   2500 O  O   . PRO   B 1 55  ? -31.746 -16.620 19.873 1.00 20.62 ? 55  PRO   A O   1 
ATOM   2501 C  CB  . PRO   B 1 55  ? -28.803 -15.726 20.796 1.00 20.00 ? 55  PRO   A CB  1 
ATOM   2502 C  CG  . PRO   B 1 55  ? -27.297 -15.920 20.670 1.00 19.97 ? 55  PRO   A CG  1 
ATOM   2503 C  CD  . PRO   B 1 55  ? -27.068 -16.463 19.261 1.00 18.43 ? 55  PRO   A CD  1 
ATOM   2504 N  N   . SER   B 1 56  ? -30.643 -15.956 18.009 1.00 20.12 ? 56  SER   A N   1 
ATOM   2505 C  CA  . SER   B 1 56  ? -31.917 -15.609 17.382 1.00 21.96 ? 56  SER   A CA  1 
ATOM   2506 C  C   . SER   B 1 56  ? -32.713 -16.828 16.913 1.00 21.53 ? 56  SER   A C   1 
ATOM   2507 O  O   . SER   B 1 56  ? -33.845 -16.640 16.487 1.00 23.51 ? 56  SER   A O   1 
ATOM   2508 C  CB  . SER   B 1 56  ? -31.751 -14.624 16.249 1.00 24.88 ? 56  SER   A CB  1 
ATOM   2509 O  OG  . SER   B 1 56  ? -31.004 -15.237 15.213 1.00 29.11 ? 56  SER   A OG  1 
ATOM   2510 N  N   . SER   B 1 57  ? -32.150 -18.038 16.953 1.00 17.15 ? 57  SER   A N   1 
ATOM   2511 C  CA  . SER   B 1 57  ? -32.884 -19.239 16.571 1.00 15.36 ? 57  SER   A CA  1 
ATOM   2512 C  C   . SER   B 1 57  ? -34.010 -19.584 17.546 1.00 15.96 ? 57  SER   A C   1 
ATOM   2513 O  O   . SER   B 1 57  ? -34.949 -20.301 17.147 1.00 16.41 ? 57  SER   A O   1 
ATOM   2514 C  CB  . SER   B 1 57  ? -31.893 -20.427 16.499 1.00 16.61 ? 57  SER   A CB  1 
ATOM   2515 O  OG  . SER   B 1 57  ? -31.016 -20.270 15.395 1.00 20.70 ? 57  SER   A OG  1 
ATOM   2516 N  N   . ALA   B 1 58  ? -33.870 -19.195 18.833 1.00 14.57 ? 58  ALA   A N   1 
ATOM   2517 C  CA  . ALA   B 1 58  ? -34.841 -19.603 19.837 1.00 16.08 ? 58  ALA   A CA  1 
ATOM   2518 C  C   . ALA   B 1 58  ? -36.145 -18.840 19.613 1.00 16.78 ? 58  ALA   A C   1 
ATOM   2519 O  O   . ALA   B 1 58  ? -36.084 -17.635 19.313 1.00 18.38 ? 58  ALA   A O   1 
ATOM   2520 C  CB  . ALA   B 1 58  ? -34.301 -19.359 21.257 1.00 17.55 ? 58  ALA   A CB  1 
ATOM   2521 N  N   . LYS   B 1 59  ? -37.282 -19.535 19.755 1.00 16.27 ? 59  LYS   A N   1 
ATOM   2522 C  CA  . LYS   B 1 59  ? -38.592 -18.909 19.558 1.00 17.30 ? 59  LYS   A CA  1 
ATOM   2523 C  C   . LYS   B 1 59  ? -39.492 -18.950 20.804 1.00 15.06 ? 59  LYS   A C   1 
ATOM   2524 O  O   . LYS   B 1 59  ? -40.109 -17.925 21.130 1.00 16.43 ? 59  LYS   A O   1 
ATOM   2525 C  CB  . LYS   B 1 59  ? -39.295 -19.623 18.399 1.00 19.20 ? 59  LYS   A CB  1 
ATOM   2526 C  CG  . LYS   B 1 59  ? -38.659 -19.384 17.032 1.00 24.86 ? 59  LYS   A CG  1 
ATOM   2527 C  CD  . LYS   B 1 59  ? -38.291 -17.915 16.765 1.00 31.02 ? 59  LYS   A CD  1 
ATOM   2528 C  CE  . LYS   B 1 59  ? -37.151 -17.815 15.753 1.00 33.89 ? 59  LYS   A CE  1 
ATOM   2529 N  NZ  . LYS   B 1 59  ? -36.656 -16.433 15.589 1.00 45.11 ? 59  LYS   A NZ  1 
ATOM   2530 N  N   . ILE   B 1 60  ? -39.726 -20.160 21.360 1.00 15.55 ? 60  ILE   A N   1 
ATOM   2531 C  CA  . ILE   B 1 60  ? -40.693 -20.328 22.437 1.00 14.42 ? 60  ILE   A CA  1 
ATOM   2532 C  C   . ILE   B 1 60  ? -40.149 -21.314 23.491 1.00 14.74 ? 60  ILE   A C   1 
ATOM   2533 O  O   . ILE   B 1 60  ? -39.329 -22.167 23.175 1.00 14.18 ? 60  ILE   A O   1 
ATOM   2534 C  CB  . ILE   B 1 60  ? -42.101 -20.760 21.969 1.00 18.02 ? 60  ILE   A CB  1 
ATOM   2535 C  CG1 . ILE   B 1 60  ? -42.103 -22.115 21.266 1.00 21.05 ? 60  ILE   A CG1 1 
ATOM   2536 C  CG2 . ILE   B 1 60  ? -42.749 -19.708 21.055 1.00 19.55 ? 60  ILE   A CG2 1 
ATOM   2537 C  CD1 . ILE   B 1 60  ? -43.499 -22.727 21.079 1.00 21.46 ? 60  ILE   A CD1 1 
ATOM   2538 N  N   . ILE   B 1 61  ? -40.681 -21.203 24.701 1.00 14.81 ? 61  ILE   A N   1 
ATOM   2539 C  CA  . ILE   B 1 61  ? -40.495 -22.231 25.711 1.00 14.13 ? 61  ILE   A CA  1 
ATOM   2540 C  C   . ILE   B 1 61  ? -41.883 -22.704 26.136 1.00 14.09 ? 61  ILE   A C   1 
ATOM   2541 O  O   . ILE   B 1 61  ? -42.815 -21.884 26.252 1.00 15.30 ? 61  ILE   A O   1 
ATOM   2542 C  CB  . ILE   B 1 61  ? -39.627 -21.717 26.879 1.00 13.99 ? 61  ILE   A CB  1 
ATOM   2543 C  CG1 . ILE   B 1 61  ? -39.265 -22.895 27.799 1.00 15.37 ? 61  ILE   A CG1 1 
ATOM   2544 C  CG2 . ILE   B 1 61  ? -40.242 -20.513 27.638 1.00 14.18 ? 61  ILE   A CG2 1 
ATOM   2545 C  CD1 . ILE   B 1 61  ? -38.255 -22.491 28.917 1.00 14.09 ? 61  ILE   A CD1 1 
ATOM   2546 N  N   . SER   B 1 62  ? -42.038 -24.024 26.300 1.00 14.91 ? 62  SER   A N   1 
ATOM   2547 C  CA  . SER   B 1 62  ? -43.348 -24.563 26.644 1.00 15.77 ? 62  SER   A CA  1 
ATOM   2548 C  C   . SER   B 1 62  ? -43.213 -25.693 27.672 1.00 18.57 ? 62  SER   A C   1 
ATOM   2549 O  O   . SER   B 1 62  ? -42.146 -26.303 27.813 1.00 15.96 ? 62  SER   A O   1 
ATOM   2550 C  CB  . SER   B 1 62  ? -44.055 -25.049 25.410 1.00 17.97 ? 62  SER   A CB  1 
ATOM   2551 O  OG  . SER   B 1 62  ? -43.388 -26.179 24.882 1.00 23.58 ? 62  SER   A OG  1 
ATOM   2552 N  N   . ASN   B 1 63  ? -44.340 -25.998 28.352 1.00 15.04 ? 63  ASN   A N   1 
ATOM   2553 C  CA  . ASN   B 1 63  ? -44.433 -27.166 29.195 1.00 15.32 ? 63  ASN   A CA  1 
ATOM   2554 C  C   . ASN   B 1 63  ? -45.095 -28.307 28.424 1.00 17.60 ? 63  ASN   A C   1 
ATOM   2555 O  O   . ASN   B 1 63  ? -46.289 -28.248 28.087 1.00 17.77 ? 63  ASN   A O   1 
ATOM   2556 C  CB  . ASN   B 1 63  ? -45.152 -26.802 30.507 1.00 15.70 ? 63  ASN   A CB  1 
ATOM   2557 C  CG  . ASN   B 1 63  ? -45.334 -27.981 31.447 1.00 16.18 ? 63  ASN   A CG  1 
ATOM   2558 O  OD1 . ASN   B 1 63  ? -45.170 -29.121 31.057 1.00 16.95 ? 63  ASN   A OD1 1 
ATOM   2559 N  ND2 . ASN   B 1 63  ? -45.717 -27.733 32.699 1.00 17.14 ? 63  ASN   A ND2 1 
ATOM   2560 N  N   . SER   B 1 64  ? -44.326 -29.358 28.087 1.00 14.77 ? 64  SER   A N   1 
ATOM   2561 C  CA  . SER   B 1 64  ? -44.869 -30.480 27.320 1.00 15.52 ? 64  SER   A CA  1 
ATOM   2562 C  C   . SER   B 1 64  ? -45.671 -31.454 28.184 1.00 15.33 ? 64  SER   A C   1 
ATOM   2563 O  O   . SER   B 1 64  ? -46.257 -32.405 27.646 1.00 19.85 ? 64  SER   A O   1 
ATOM   2564 C  CB  . SER   B 1 64  ? -43.750 -31.256 26.683 1.00 16.79 ? 64  SER   A CB  1 
ATOM   2565 O  OG  . SER   B 1 64  ? -42.899 -31.825 27.679 1.00 17.01 ? 64  SER   A OG  1 
ATOM   2566 N  N   . GLY   B 1 65  ? -45.564 -31.312 29.502 1.00 15.75 ? 65  GLY   A N   1 
ATOM   2567 C  CA  . GLY   B 1 65  ? -46.114 -32.256 30.469 1.00 17.34 ? 65  GLY   A CA  1 
ATOM   2568 C  C   . GLY   B 1 65  ? -45.023 -33.219 30.935 1.00 17.50 ? 65  GLY   A C   1 
ATOM   2569 O  O   . GLY   B 1 65  ? -45.212 -33.950 31.911 1.00 18.13 ? 65  GLY   A O   1 
ATOM   2570 N  N   . HIS   B 1 66  ? -43.887 -33.201 30.207 1.00 14.98 ? 66  HIS   A N   1 
ATOM   2571 C  CA  . HIS   B 1 66  ? -42.780 -34.097 30.528 1.00 13.94 ? 66  HIS   A CA  1 
ATOM   2572 C  C   . HIS   B 1 66  ? -41.470 -33.368 30.849 1.00 15.19 ? 66  HIS   A C   1 
ATOM   2573 O  O   . HIS   B 1 66  ? -40.591 -33.988 31.423 1.00 15.38 ? 66  HIS   A O   1 
ATOM   2574 C  CB  . HIS   B 1 66  ? -42.508 -35.080 29.372 1.00 16.44 ? 66  HIS   A CB  1 
ATOM   2575 C  CG  . HIS   B 1 66  ? -43.746 -35.753 28.886 1.00 19.17 ? 66  HIS   A CG  1 
ATOM   2576 N  ND1 . HIS   B 1 66  ? -44.251 -35.548 27.596 1.00 22.99 ? 66  HIS   A ND1 1 
ATOM   2577 C  CD2 . HIS   B 1 66  ? -44.579 -36.625 29.512 1.00 18.66 ? 66  HIS   A CD2 1 
ATOM   2578 C  CE1 . HIS   B 1 66  ? -45.370 -36.244 27.476 1.00 19.48 ? 66  HIS   A CE1 1 
ATOM   2579 N  NE2 . HIS   B 1 66  ? -45.565 -36.936 28.598 1.00 23.57 ? 66  HIS   A NE2 1 
ATOM   2580 N  N   . SER   B 1 67  ? -41.334 -32.108 30.437 1.00 13.77 ? 67  SER   A N   1 
ATOM   2581 C  CA  . SER   B 1 67  ? -40.179 -31.259 30.762 1.00 11.93 ? 67  SER   A CA  1 
ATOM   2582 C  C   . SER   B 1 67  ? -40.574 -29.862 30.275 1.00 13.37 ? 67  SER   A C   1 
ATOM   2583 O  O   . SER   B 1 67  ? -41.699 -29.733 29.806 1.00 14.10 ? 67  SER   A O   1 
ATOM   2584 C  CB  . SER   B 1 67  ? -38.880 -31.758 30.083 1.00 14.71 ? 67  SER   A CB  1 
ATOM   2585 O  OG  . SER   B 1 67  ? -37.788 -30.962 30.563 1.00 14.21 ? 67  SER   A OG  1 
ATOM   2586 N  N   . PHE   B 1 68  ? -39.711 -28.857 30.395 1.00 11.70 ? 68  PHE   A N   1 
ATOM   2587 C  CA  . PHE   B 1 68  ? -39.845 -27.670 29.530 1.00 13.06 ? 68  PHE   A CA  1 
ATOM   2588 C  C   . PHE   B 1 68  ? -39.171 -28.004 28.201 1.00 14.90 ? 68  PHE   A C   1 
ATOM   2589 O  O   . PHE   B 1 68  ? -38.245 -28.832 28.157 1.00 15.60 ? 68  PHE   A O   1 
ATOM   2590 C  CB  . PHE   B 1 68  ? -39.230 -26.403 30.151 1.00 13.52 ? 68  PHE   A CB  1 
ATOM   2591 C  CG  . PHE   B 1 68  ? -37.716 -26.411 30.190 1.00 14.04 ? 68  PHE   A CG  1 
ATOM   2592 C  CD1 . PHE   B 1 68  ? -36.954 -26.055 29.082 1.00 16.17 ? 68  PHE   A CD1 1 
ATOM   2593 C  CD2 . PHE   B 1 68  ? -37.064 -26.879 31.336 1.00 16.12 ? 68  PHE   A CD2 1 
ATOM   2594 C  CE1 . PHE   B 1 68  ? -35.550 -26.119 29.122 1.00 14.96 ? 68  PHE   A CE1 1 
ATOM   2595 C  CE2 . PHE   B 1 68  ? -35.676 -26.886 31.403 1.00 16.20 ? 68  PHE   A CE2 1 
ATOM   2596 C  CZ  . PHE   B 1 68  ? -34.919 -26.503 30.292 1.00 16.62 ? 68  PHE   A CZ  1 
ATOM   2597 N  N   . ASN   B 1 69  ? -39.715 -27.451 27.096 1.00 13.18 ? 69  ASN   A N   1 
ATOM   2598 C  CA  . ASN   B 1 69  ? -39.054 -27.560 25.806 1.00 14.65 ? 69  ASN   A CA  1 
ATOM   2599 C  C   . ASN   B 1 69  ? -38.789 -26.146 25.298 1.00 13.55 ? 69  ASN   A C   1 
ATOM   2600 O  O   . ASN   B 1 69  ? -39.718 -25.371 25.154 1.00 13.94 ? 69  ASN   A O   1 
ATOM   2601 C  CB  . ASN   B 1 69  ? -39.964 -28.202 24.751 1.00 18.48 ? 69  ASN   A CB  1 
ATOM   2602 C  CG  . ASN   B 1 69  ? -40.146 -29.694 24.902 1.00 23.05 ? 69  ASN   A CG  1 
ATOM   2603 O  OD1 . ASN   B 1 69  ? -39.364 -30.370 25.572 1.00 23.93 ? 69  ASN   A OD1 1 
ATOM   2604 N  ND2 . ASN   B 1 69  ? -41.147 -30.241 24.214 1.00 24.85 ? 69  ASN   A ND2 1 
ATOM   2605 N  N   . VAL   B 1 70  ? -37.540 -25.848 24.960 1.00 12.40 ? 70  VAL   A N   1 
ATOM   2606 C  CA  . VAL   B 1 70  ? -37.276 -24.640 24.176 1.00 12.51 ? 70  VAL   A CA  1 
ATOM   2607 C  C   . VAL   B 1 70  ? -37.257 -25.072 22.717 1.00 13.02 ? 70  VAL   A C   1 
ATOM   2608 O  O   . VAL   B 1 70  ? -36.487 -25.956 22.350 1.00 12.73 ? 70  VAL   A O   1 
ATOM   2609 C  CB  . VAL   B 1 70  ? -35.933 -23.960 24.539 1.00 12.00 ? 70  VAL   A CB  1 
ATOM   2610 C  CG1 . VAL   B 1 70  ? -35.686 -22.711 23.660 1.00 15.06 ? 70  VAL   A CG1 1 
ATOM   2611 C  CG2 . VAL   B 1 70  ? -35.873 -23.587 26.013 1.00 13.27 ? 70  VAL   A CG2 1 
ATOM   2612 N  N   . ASP   B 1 71  ? -38.139 -24.467 21.895 1.00 12.82 ? 71  ASP   A N   1 
ATOM   2613 C  CA  . ASP   B 1 71  ? -38.188 -24.741 20.456 1.00 14.56 ? 71  ASP   A CA  1 
ATOM   2614 C  C   . ASP   B 1 71  ? -37.444 -23.689 19.618 1.00 14.52 ? 71  ASP   A C   1 
ATOM   2615 O  O   . ASP   B 1 71  ? -37.514 -22.486 19.888 1.00 14.88 ? 71  ASP   A O   1 
ATOM   2616 C  CB  . ASP   B 1 71  ? -39.668 -24.865 20.060 1.00 17.28 ? 71  ASP   A CB  1 
ATOM   2617 C  CG  . ASP   B 1 71  ? -40.288 -26.179 20.489 1.00 24.24 ? 71  ASP   A CG  1 
ATOM   2618 O  OD1 . ASP   B 1 71  ? -39.548 -27.218 20.615 1.00 31.01 ? 71  ASP   A OD1 1 
ATOM   2619 O  OD2 . ASP   B 1 71  ? -41.499 -26.174 20.748 1.00 32.40 ? 71  ASP   A OD2 1 
ATOM   2620 N  N   . PHE   B 1 72  ? -36.716 -24.169 18.612 1.00 14.75 ? 72  PHE   A N   1 
ATOM   2621 C  CA  . PHE   B 1 72  ? -35.892 -23.331 17.754 1.00 14.78 ? 72  PHE   A CA  1 
ATOM   2622 C  C   . PHE   B 1 72  ? -36.424 -23.352 16.329 1.00 16.66 ? 72  PHE   A C   1 
ATOM   2623 O  O   . PHE   B 1 72  ? -36.896 -24.357 15.852 1.00 17.70 ? 72  PHE   A O   1 
ATOM   2624 C  CB  . PHE   B 1 72  ? -34.458 -23.888 17.751 1.00 14.29 ? 72  PHE   A CB  1 
ATOM   2625 C  CG  . PHE   B 1 72  ? -33.795 -23.766 19.099 1.00 15.04 ? 72  PHE   A CG  1 
ATOM   2626 C  CD1 . PHE   B 1 72  ? -34.000 -24.743 20.064 1.00 13.35 ? 72  PHE   A CD1 1 
ATOM   2627 C  CD2 . PHE   B 1 72  ? -33.028 -22.679 19.456 1.00 15.13 ? 72  PHE   A CD2 1 
ATOM   2628 C  CE1 . PHE   B 1 72  ? -33.459 -24.597 21.335 1.00 14.18 ? 72  PHE   A CE1 1 
ATOM   2629 C  CE2 . PHE   B 1 72  ? -32.456 -22.551 20.720 1.00 15.36 ? 72  PHE   A CE2 1 
ATOM   2630 C  CZ  . PHE   B 1 72  ? -32.633 -23.541 21.669 1.00 13.54 ? 72  PHE   A CZ  1 
ATOM   2631 N  N   . ASP   B 1 73  ? -36.283 -22.223 15.626 1.00 17.73 ? 73  ASP   A N   1 
ATOM   2632 C  CA  . ASP   B 1 73  ? -36.523 -22.180 14.196 1.00 19.96 ? 73  ASP   A CA  1 
ATOM   2633 C  C   . ASP   B 1 73  ? -35.485 -23.080 13.554 1.00 22.04 ? 73  ASP   A C   1 
ATOM   2634 O  O   . ASP   B 1 73  ? -34.296 -22.769 13.694 1.00 23.86 ? 73  ASP   A O   1 
ATOM   2635 C  CB  . ASP   B 1 73  ? -36.321 -20.720 13.737 1.00 21.97 ? 73  ASP   A CB  1 
ATOM   2636 C  CG  . ASP   B 1 73  ? -36.533 -20.514 12.229 1.00 34.27 ? 73  ASP   A CG  1 
ATOM   2637 O  OD1 . ASP   B 1 73  ? -36.046 -21.363 11.405 1.00 28.91 ? 73  ASP   A OD1 1 
ATOM   2638 O  OD2 . ASP   B 1 73  ? -37.163 -19.480 11.873 1.00 41.62 ? 73  ASP   A OD2 1 
ATOM   2639 N  N   . ASP   B 1 74  ? -35.944 -24.185 12.942 1.00 18.90 ? 74  ASP   A N   1 
ATOM   2640 C  CA  . ASP   B 1 74  ? -35.070 -25.203 12.360 1.00 18.36 ? 74  ASP   A CA  1 
ATOM   2641 C  C   . ASP   B 1 74  ? -35.291 -25.271 10.829 1.00 20.22 ? 74  ASP   A C   1 
ATOM   2642 O  O   . ASP   B 1 74  ? -35.453 -26.367 10.256 1.00 18.62 ? 74  ASP   A O   1 
ATOM   2643 C  CB  . ASP   B 1 74  ? -35.339 -26.554 13.040 1.00 22.75 ? 74  ASP   A CB  1 
ATOM   2644 C  CG  . ASP   B 1 74  ? -36.711 -27.171 12.759 1.00 26.12 ? 74  ASP   A CG  1 
ATOM   2645 O  OD1 . ASP   B 1 74  ? -37.630 -26.433 12.250 1.00 30.11 ? 74  ASP   A OD1 1 
ATOM   2646 O  OD2 . ASP   B 1 74  ? -36.845 -28.415 12.990 1.00 21.91 ? 74  ASP   A OD2 1 
ATOM   2647 N  N   . THR   B 1 75  ? -35.379 -24.076 10.191 1.00 22.64 ? 75  THR   A N   1 
ATOM   2648 C  CA  . THR   B 1 75  ? -35.526 -23.943 8.735  1.00 24.33 ? 75  THR   A CA  1 
ATOM   2649 C  C   . THR   B 1 75  ? -34.215 -23.495 8.081  1.00 23.06 ? 75  THR   A C   1 
ATOM   2650 O  O   . THR   B 1 75  ? -34.086 -23.499 6.847  1.00 20.85 ? 75  THR   A O   1 
ATOM   2651 C  CB  . THR   B 1 75  ? -36.612 -22.883 8.427  1.00 26.10 ? 75  THR   A CB  1 
ATOM   2652 O  OG1 . THR   B 1 75  ? -36.101 -21.607 8.856  1.00 28.10 ? 75  THR   A OG1 1 
ATOM   2653 C  CG2 . THR   B 1 75  ? -37.913 -23.147 9.141  1.00 30.37 ? 75  THR   A CG2 1 
ATOM   2654 N  N   . GLU   B 1 76  ? -33.237 -23.062 8.879  1.00 20.67 ? 76  GLU   A N   1 
ATOM   2655 C  CA  . GLU   B 1 76  ? -31.968 -22.564 8.356  1.00 26.29 ? 76  GLU   A CA  1 
ATOM   2656 C  C   . GLU   B 1 76  ? -30.834 -23.265 9.087  1.00 20.64 ? 76  GLU   A C   1 
ATOM   2657 O  O   . GLU   B 1 76  ? -31.120 -23.916 10.091 1.00 18.83 ? 76  GLU   A O   1 
ATOM   2658 C  CB  . GLU   B 1 76  ? -31.804 -21.069 8.637  1.00 36.38 ? 76  GLU   A CB  1 
ATOM   2659 C  CG  . GLU   B 1 76  ? -33.002 -20.245 8.221  1.00 46.25 ? 76  GLU   A CG  1 
ATOM   2660 C  CD  . GLU   B 1 76  ? -32.962 -18.846 8.819  1.00 60.11 ? 76  GLU   A CD  1 
ATOM   2661 O  OE1 . GLU   B 1 76  ? -31.999 -18.090 8.494  1.00 51.28 ? 76  GLU   A OE1 1 
ATOM   2662 O  OE2 . GLU   B 1 76  ? -33.878 -18.524 9.627  1.00 62.09 ? 76  GLU   A OE2 1 
ATOM   2663 N  N   . ASN   B 1 77  ? -29.600 -23.047 8.625  1.00 20.74 ? 77  ASN   A N   1 
ATOM   2664 C  CA  . ASN   B 1 77  ? -28.402 -23.651 9.186  1.00 20.21 ? 77  ASN   A CA  1 
ATOM   2665 C  C   . ASN   B 1 77  ? -27.630 -22.657 10.058 1.00 19.53 ? 77  ASN   A C   1 
ATOM   2666 O  O   . ASN   B 1 77  ? -26.419 -22.794 10.161 1.00 21.73 ? 77  ASN   A O   1 
ATOM   2667 C  CB  . ASN   B 1 77  ? -27.484 -24.330 8.166  1.00 22.09 ? 77  ASN   A CB  1 
ATOM   2668 C  CG  . ASN   B 1 77  ? -27.956 -25.700 7.725  1.00 19.81 ? 77  ASN   A CG  1 
ATOM   2669 O  OD1 . ASN   B 1 77  ? -28.807 -26.315 8.380  1.00 18.26 ? 77  ASN   A OD1 1 
ATOM   2670 N  ND2 . ASN   B 1 77  ? -27.453 -26.167 6.582  1.00 20.71 ? 77  ASN   A ND2 1 
ATOM   2671 N  N   . LYS   B 1 78  ? -28.327 -21.740 10.758 1.00 18.32 ? 78  LYS   A N   1 
ATOM   2672 C  CA  . LYS   B 1 78  ? -27.714 -20.812 11.707 1.00 17.98 ? 78  LYS   A CA  1 
ATOM   2673 C  C   . LYS   B 1 78  ? -27.263 -21.484 13.009 1.00 17.96 ? 78  LYS   A C   1 
ATOM   2674 O  O   . LYS   B 1 78  ? -26.297 -21.001 13.607 1.00 18.69 ? 78  LYS   A O   1 
ATOM   2675 C  CB  . LYS   B 1 78  ? -28.671 -19.666 12.087 1.00 18.90 ? 78  LYS   A CB  1 
ATOM   2676 C  CG  . LYS   B 1 78  ? -29.009 -18.767 10.883 1.00 27.17 ? 78  LYS   A CG  1 
ATOM   2677 C  CD  . LYS   B 1 78  ? -29.956 -17.634 11.209 1.00 31.10 ? 78  LYS   A CD  1 
ATOM   2678 C  CE  . LYS   B 1 78  ? -29.658 -16.403 10.366 1.00 38.65 ? 78  LYS   A CE  1 
ATOM   2679 N  NZ  . LYS   B 1 78  ? -30.645 -15.329 10.643 1.00 46.42 ? 78  LYS   A NZ  1 
ATOM   2680 N  N   . SER   B 1 79  ? -27.924 -22.587 13.422 1.00 14.89 ? 79  SER   A N   1 
ATOM   2681 C  CA  . SER   B 1 79  ? -27.582 -23.282 14.665 1.00 12.92 ? 79  SER   A CA  1 
ATOM   2682 C  C   . SER   B 1 79  ? -27.440 -24.734 14.301 1.00 15.75 ? 79  SER   A C   1 
ATOM   2683 O  O   . SER   B 1 79  ? -28.442 -25.393 14.048 1.00 13.30 ? 79  SER   A O   1 
ATOM   2684 C  CB  . SER   B 1 79  ? -28.709 -23.154 15.682 1.00 13.40 ? 79  SER   A CB  1 
ATOM   2685 O  OG  . SER   B 1 79  ? -28.782 -21.769 16.088 1.00 15.18 ? 79  SER   A OG  1 
ATOM   2686 N  N   . VAL   B 1 80  ? -26.196 -25.206 14.314 1.00 13.67 ? 80  VAL   A N   1 
ATOM   2687 C  CA  . VAL   B 1 80  ? -25.930 -26.537 13.777 1.00 15.06 ? 80  VAL   A CA  1 
ATOM   2688 C  C   . VAL   B 1 80  ? -24.791 -27.188 14.555 1.00 14.32 ? 80  VAL   A C   1 
ATOM   2689 O  O   . VAL   B 1 80  ? -23.926 -26.494 15.099 1.00 18.04 ? 80  VAL   A O   1 
ATOM   2690 C  CB  . VAL   B 1 80  ? -25.562 -26.517 12.281 1.00 19.24 ? 80  VAL   A CB  1 
ATOM   2691 C  CG1 . VAL   B 1 80  ? -26.719 -26.101 11.387 1.00 18.72 ? 80  VAL   A CG1 1 
ATOM   2692 C  CG2 . VAL   B 1 80  ? -24.381 -25.608 12.023 1.00 18.18 ? 80  VAL   A CG2 1 
ATOM   2693 N  N   . LEU   B 1 81  ? -24.788 -28.541 14.502 1.00 14.92 ? 81  LEU   A N   1 
ATOM   2694 C  CA  . LEU   B 1 81  ? -23.764 -29.341 15.140 1.00 13.82 ? 81  LEU   A CA  1 
ATOM   2695 C  C   . LEU   B 1 81  ? -23.102 -30.183 14.051 1.00 15.27 ? 81  LEU   A C   1 
ATOM   2696 O  O   . LEU   B 1 81  ? -23.805 -30.784 13.248 1.00 15.94 ? 81  LEU   A O   1 
ATOM   2697 C  CB  . LEU   B 1 81  ? -24.458 -30.246 16.171 1.00 14.99 ? 81  LEU   A CB  1 
ATOM   2698 C  CG  . LEU   B 1 81  ? -23.532 -31.327 16.759 1.00 15.70 ? 81  LEU   A CG  1 
ATOM   2699 C  CD1 . LEU   B 1 81  ? -22.493 -30.652 17.638 1.00 18.75 ? 81  LEU   A CD1 1 
ATOM   2700 C  CD2 . LEU   B 1 81  ? -24.362 -32.310 17.597 1.00 17.94 ? 81  LEU   A CD2 1 
ATOM   2701 N  N   . ARG   B 1 82  ? -21.761 -30.189 14.026 1.00 13.99 ? 82  ARG   A N   1 
ATOM   2702 C  CA  . ARG   B 1 82  ? -21.021 -30.912 13.001 1.00 15.47 ? 82  ARG   A CA  1 
ATOM   2703 C  C   . ARG   B 1 82  ? -19.821 -31.560 13.689 1.00 15.45 ? 82  ARG   A C   1 
ATOM   2704 O  O   . ARG   B 1 82  ? -19.486 -31.239 14.824 1.00 17.38 ? 82  ARG   A O   1 
ATOM   2705 C  CB  . ARG   B 1 82  ? -20.482 -29.970 11.889 1.00 20.08 ? 82  ARG   A CB  1 
ATOM   2706 C  CG  . ARG   B 1 82  ? -21.558 -29.220 11.099 1.00 24.72 ? 82  ARG   A CG  1 
ATOM   2707 C  CD  . ARG   B 1 82  ? -21.013 -28.203 10.058 1.00 33.30 ? 82  ARG   A CD  1 
ATOM   2708 N  NE  . ARG   B 1 82  ? -20.773 -26.884 10.673 1.00 42.51 ? 82  ARG   A NE  1 
ATOM   2709 C  CZ  . ARG   B 1 82  ? -21.128 -25.664 10.202 1.00 53.42 ? 82  ARG   A CZ  1 
ATOM   2710 N  NH1 . ARG   B 1 82  ? -21.735 -25.516 9.025  1.00 44.53 ? 82  ARG   A NH1 1 
ATOM   2711 N  NH2 . ARG   B 1 82  ? -20.865 -24.587 10.936 1.00 47.51 ? 82  ARG   A NH2 1 
ATOM   2712 N  N   . GLY   B 1 83  ? -19.214 -32.538 12.999 1.00 16.83 ? 83  GLY   A N   1 
ATOM   2713 C  CA  . GLY   B 1 83  ? -17.961 -33.101 13.533 1.00 19.85 ? 83  GLY   A CA  1 
ATOM   2714 C  C   . GLY   B 1 83  ? -18.231 -34.206 14.553 1.00 19.09 ? 83  GLY   A C   1 
ATOM   2715 O  O   . GLY   B 1 83  ? -19.299 -34.807 14.570 1.00 16.44 ? 83  GLY   A O   1 
ATOM   2716 N  N   . GLY   B 1 84  ? -17.268 -34.466 15.449 1.00 20.25 ? 84  GLY   A N   1 
ATOM   2717 C  CA  . GLY   B 1 84  ? -17.434 -35.571 16.378 1.00 18.74 ? 84  GLY   A CA  1 
ATOM   2718 C  C   . GLY   B 1 84  ? -17.602 -36.874 15.610 1.00 16.61 ? 84  GLY   A C   1 
ATOM   2719 O  O   . GLY   B 1 84  ? -16.832 -37.121 14.683 1.00 17.28 ? 84  GLY   A O   1 
ATOM   2720 N  N   . PRO   B 1 85  ? -18.616 -37.720 15.929 1.00 16.72 ? 85  PRO   A N   1 
ATOM   2721 C  CA  . PRO   B 1 85  ? -18.896 -38.950 15.196 1.00 16.38 ? 85  PRO   A CA  1 
ATOM   2722 C  C   . PRO   B 1 85  ? -19.768 -38.782 13.953 1.00 18.14 ? 85  PRO   A C   1 
ATOM   2723 O  O   . PRO   B 1 85  ? -20.005 -39.749 13.243 1.00 19.58 ? 85  PRO   A O   1 
ATOM   2724 C  CB  . PRO   B 1 85  ? -19.689 -39.783 16.231 1.00 17.06 ? 85  PRO   A CB  1 
ATOM   2725 C  CG  . PRO   B 1 85  ? -20.468 -38.722 16.988 1.00 18.52 ? 85  PRO   A CG  1 
ATOM   2726 C  CD  . PRO   B 1 85  ? -19.559 -37.519 17.070 1.00 17.13 ? 85  PRO   A CD  1 
ATOM   2727 N  N   . LEU   B 1 86  ? -20.188 -37.535 13.668 1.00 16.94 ? 86  LEU   A N   1 
ATOM   2728 C  CA  . LEU   B 1 86  ? -21.271 -37.242 12.731 1.00 14.87 ? 86  LEU   A CA  1 
ATOM   2729 C  C   . LEU   B 1 86  ? -20.761 -37.061 11.309 1.00 15.09 ? 86  LEU   A C   1 
ATOM   2730 O  O   . LEU   B 1 86  ? -19.726 -36.429 11.108 1.00 17.27 ? 86  LEU   A O   1 
ATOM   2731 C  CB  . LEU   B 1 86  ? -21.963 -35.942 13.181 1.00 13.67 ? 86  LEU   A CB  1 
ATOM   2732 C  CG  . LEU   B 1 86  ? -22.586 -35.968 14.597 1.00 13.72 ? 86  LEU   A CG  1 
ATOM   2733 C  CD1 . LEU   B 1 86  ? -23.164 -34.603 14.946 1.00 14.84 ? 86  LEU   A CD1 1 
ATOM   2734 C  CD2 . LEU   B 1 86  ? -23.638 -37.079 14.683 1.00 14.33 ? 86  LEU   A CD2 1 
ATOM   2735 N  N   . THR   B 1 87  ? -21.549 -37.568 10.344 1.00 16.48 ? 87  THR   A N   1 
ATOM   2736 C  CA  . THR   B 1 87  ? -21.340 -37.211 8.942  1.00 17.96 ? 87  THR   A CA  1 
ATOM   2737 C  C   . THR   B 1 87  ? -22.397 -36.179 8.544  1.00 18.53 ? 87  THR   A C   1 
ATOM   2738 O  O   . THR   B 1 87  ? -23.583 -36.489 8.689  1.00 19.77 ? 87  THR   A O   1 
ATOM   2739 C  CB  . THR   B 1 87  ? -21.501 -38.450 8.055  1.00 20.50 ? 87  THR   A CB  1 
ATOM   2740 O  OG1 . THR   B 1 87  ? -20.540 -39.405 8.507  1.00 22.84 ? 87  THR   A OG1 1 
ATOM   2741 C  CG2 . THR   B 1 87  ? -21.268 -38.135 6.593  1.00 23.62 ? 87  THR   A CG2 1 
ATOM   2742 N  N   . GLY   B 1 88  ? -21.976 -35.010 8.058  1.00 21.39 ? 88  GLY   A N   1 
ATOM   2743 C  CA  . GLY   B 1 88  ? -22.968 -34.016 7.617  1.00 20.28 ? 88  GLY   A CA  1 
ATOM   2744 C  C   . GLY   B 1 88  ? -23.404 -33.078 8.751  1.00 20.00 ? 88  GLY   A C   1 
ATOM   2745 O  O   . GLY   B 1 88  ? -22.821 -33.059 9.838  1.00 22.19 ? 88  GLY   A O   1 
ATOM   2746 N  N   . SER   B 1 89  ? -24.453 -32.292 8.488  1.00 16.72 ? 89  SER   A N   1 
ATOM   2747 C  CA  . SER   B 1 89  ? -24.794 -31.170 9.335  1.00 16.07 ? 89  SER   A CA  1 
ATOM   2748 C  C   . SER   B 1 89  ? -26.104 -31.488 10.062 1.00 14.49 ? 89  SER   A C   1 
ATOM   2749 O  O   . SER   B 1 89  ? -27.083 -31.945 9.445  1.00 16.22 ? 89  SER   A O   1 
ATOM   2750 C  CB  . SER   B 1 89  ? -24.958 -29.919 8.466  1.00 19.58 ? 89  SER   A CB  1 
ATOM   2751 O  OG  . SER   B 1 89  ? -25.306 -28.767 9.245  1.00 21.73 ? 89  SER   A OG  1 
ATOM   2752 N  N   . TYR   B 1 90  ? -26.088 -31.307 11.395 1.00 13.33 ? 90  TYR   A N   1 
ATOM   2753 C  CA  . TYR   B 1 90  ? -27.245 -31.610 12.224 1.00 11.96 ? 90  TYR   A CA  1 
ATOM   2754 C  C   . TYR   B 1 90  ? -27.809 -30.299 12.792 1.00 13.85 ? 90  TYR   A C   1 
ATOM   2755 O  O   . TYR   B 1 90  ? -27.168 -29.523 13.531 1.00 14.95 ? 90  TYR   A O   1 
ATOM   2756 C  CB  . TYR   B 1 90  ? -26.835 -32.621 13.319 1.00 11.72 ? 90  TYR   A CB  1 
ATOM   2757 C  CG  . TYR   B 1 90  ? -26.688 -34.059 12.829 1.00 13.43 ? 90  TYR   A CG  1 
ATOM   2758 C  CD1 . TYR   B 1 90  ? -25.627 -34.431 11.971 1.00 12.90 ? 90  TYR   A CD1 1 
ATOM   2759 C  CD2 . TYR   B 1 90  ? -27.638 -35.038 13.148 1.00 12.96 ? 90  TYR   A CD2 1 
ATOM   2760 C  CE1 . TYR   B 1 90  ? -25.506 -35.750 11.509 1.00 16.00 ? 90  TYR   A CE1 1 
ATOM   2761 C  CE2 . TYR   B 1 90  ? -27.523 -36.355 12.693 1.00 13.68 ? 90  TYR   A CE2 1 
ATOM   2762 C  CZ  . TYR   B 1 90  ? -26.449 -36.708 11.864 1.00 14.72 ? 90  TYR   A CZ  1 
ATOM   2763 O  OH  . TYR   B 1 90  ? -26.343 -38.003 11.403 1.00 15.48 ? 90  TYR   A OH  1 
ATOM   2764 N  N   . ARG   B 1 91  ? -29.100 -30.058 12.491 1.00 11.63 ? 91  ARG   A N   1 
ATOM   2765 C  CA  . ARG   B 1 91  ? -29.717 -28.766 12.769 1.00 12.76 ? 91  ARG   A CA  1 
ATOM   2766 C  C   . ARG   B 1 91  ? -30.365 -28.810 14.158 1.00 13.29 ? 91  ARG   A C   1 
ATOM   2767 O  O   . ARG   B 1 91  ? -31.070 -29.787 14.495 1.00 12.11 ? 91  ARG   A O   1 
ATOM   2768 C  CB  . ARG   B 1 91  ? -30.814 -28.486 11.739 1.00 13.54 ? 91  ARG   A CB  1 
ATOM   2769 C  CG  . ARG   B 1 91  ? -31.320 -27.049 11.850 1.00 13.78 ? 91  ARG   A CG  1 
ATOM   2770 C  CD  . ARG   B 1 91  ? -32.318 -26.785 10.696 1.00 15.00 ? 91  ARG   A CD  1 
ATOM   2771 N  NE  . ARG   B 1 91  ? -31.564 -26.819 9.448  1.00 14.32 ? 91  ARG   A NE  1 
ATOM   2772 C  CZ  . ARG   B 1 91  ? -32.140 -27.031 8.255  1.00 13.28 ? 91  ARG   A CZ  1 
ATOM   2773 N  NH1 . ARG   B 1 91  ? -33.427 -27.270 8.196  1.00 14.92 ? 91  ARG   A NH1 1 
ATOM   2774 N  NH2 . ARG   B 1 91  ? -31.390 -27.077 7.159  1.00 13.23 ? 91  ARG   A NH2 1 
ATOM   2775 N  N   . LEU   B 1 92  ? -30.143 -27.746 14.947 1.00 11.37 ? 92  LEU   A N   1 
ATOM   2776 C  CA  . LEU   B 1 92  ? -30.730 -27.652 16.281 1.00 11.77 ? 92  LEU   A CA  1 
ATOM   2777 C  C   . LEU   B 1 92  ? -32.250 -27.561 16.227 1.00 12.58 ? 92  LEU   A C   1 
ATOM   2778 O  O   . LEU   B 1 92  ? -32.784 -26.761 15.450 1.00 12.83 ? 92  LEU   A O   1 
ATOM   2779 C  CB  . LEU   B 1 92  ? -30.209 -26.383 16.937 1.00 11.90 ? 92  LEU   A CB  1 
ATOM   2780 C  CG  . LEU   B 1 92  ? -30.771 -26.019 18.304 1.00 12.51 ? 92  LEU   A CG  1 
ATOM   2781 C  CD1 . LEU   B 1 92  ? -30.544 -27.136 19.331 1.00 11.33 ? 92  LEU   A CD1 1 
ATOM   2782 C  CD2 . LEU   B 1 92  ? -30.191 -24.708 18.790 1.00 13.29 ? 92  LEU   A CD2 1 
ATOM   2783 N  N   . ARG   B 1 93  ? -32.930 -28.345 17.080 1.00 11.10 ? 93  ARG   A N   1 
ATOM   2784 C  CA  . ARG   B 1 93  ? -34.403 -28.396 17.102 1.00 12.96 ? 93  ARG   A CA  1 
ATOM   2785 C  C   . ARG   B 1 93  ? -34.980 -27.945 18.441 1.00 13.28 ? 93  ARG   A C   1 
ATOM   2786 O  O   . ARG   B 1 93  ? -35.963 -27.176 18.506 1.00 12.72 ? 93  ARG   A O   1 
ATOM   2787 C  CB  . ARG   B 1 93  ? -34.881 -29.825 16.803 1.00 13.79 ? 93  ARG   A CB  1 
ATOM   2788 C  CG  . ARG   B 1 93  ? -36.352 -30.109 17.090 1.00 18.93 ? 93  ARG   A CG  1 
ATOM   2789 C  CD  . ARG   B 1 93  ? -37.237 -29.594 16.003 1.00 23.95 ? 93  ARG   A CD  1 
ATOM   2790 N  NE  . ARG   B 1 93  ? -38.609 -30.104 16.227 1.00 29.03 ? 93  ARG   A NE  1 
ATOM   2791 C  CZ  . ARG   B 1 93  ? -39.585 -30.016 15.331 1.00 32.86 ? 93  ARG   A CZ  1 
ATOM   2792 N  NH1 . ARG   B 1 93  ? -39.343 -29.485 14.143 1.00 28.60 ? 93  ARG   A NH1 1 
ATOM   2793 N  NH2 . ARG   B 1 93  ? -40.800 -30.463 15.618 1.00 30.51 ? 93  ARG   A NH2 1 
ATOM   2794 N  N   . GLN   B 1 94  ? -34.458 -28.533 19.528 1.00 11.89 ? 94  GLN   A N   1 
ATOM   2795 C  CA  . GLN   B 1 94  ? -35.063 -28.251 20.824 1.00 12.85 ? 94  GLN   A CA  1 
ATOM   2796 C  C   . GLN   B 1 94  ? -34.111 -28.584 21.975 1.00 11.97 ? 94  GLN   A C   1 
ATOM   2797 O  O   . GLN   B 1 94  ? -33.132 -29.325 21.789 1.00 11.17 ? 94  GLN   A O   1 
ATOM   2798 C  CB  . GLN   B 1 94  ? -36.402 -28.933 21.012 1.00 18.47 ? 94  GLN   A CB  1 
ATOM   2799 C  CG  . GLN   B 1 94  ? -36.317 -30.432 21.061 1.00 20.01 ? 94  GLN   A CG  1 
ATOM   2800 C  CD  . GLN   B 1 94  ? -36.653 -30.895 22.464 1.00 28.36 ? 94  GLN   A CD  1 
ATOM   2801 O  OE1 . GLN   B 1 94  ? -35.788 -30.876 23.338 1.00 28.47 ? 94  GLN   A OE1 1 
ATOM   2802 N  NE2 . GLN   B 1 94  ? -37.883 -31.341 22.686 1.00 32.23 ? 94  GLN   A NE2 1 
ATOM   2803 N  N   . VAL   B 1 95  ? -34.380 -27.962 23.130 1.00 11.45 ? 95  VAL   A N   1 
ATOM   2804 C  CA  . VAL   B 1 95  ? -33.604 -28.234 24.350 1.00 11.68 ? 95  VAL   A CA  1 
ATOM   2805 C  C   . VAL   B 1 95  ? -34.611 -28.580 25.447 1.00 11.12 ? 95  VAL   A C   1 
ATOM   2806 O  O   . VAL   B 1 95  ? -35.665 -27.938 25.551 1.00 12.58 ? 95  VAL   A O   1 
ATOM   2807 C  CB  . VAL   B 1 95  ? -32.812 -26.964 24.737 1.00 13.06 ? 95  VAL   A CB  1 
ATOM   2808 C  CG1 . VAL   B 1 95  ? -32.175 -27.119 26.116 1.00 12.91 ? 95  VAL   A CG1 1 
ATOM   2809 C  CG2 . VAL   B 1 95  ? -31.675 -26.773 23.721 1.00 13.38 ? 95  VAL   A CG2 1 
ATOM   2810 N  N   . HIS   B 1 96  ? -34.274 -29.536 26.315 1.00 10.95 ? 96  HIS   A N   1 
ATOM   2811 C  CA  . HIS   B 1 96  ? -35.093 -29.848 27.488 1.00 10.91 ? 96  HIS   A CA  1 
ATOM   2812 C  C   . HIS   B 1 96  ? -34.171 -30.396 28.584 1.00 10.11 ? 96  HIS   A C   1 
ATOM   2813 O  O   . HIS   B 1 96  ? -32.956 -30.497 28.394 1.00 10.78 ? 96  HIS   A O   1 
ATOM   2814 C  CB  . HIS   B 1 96  ? -36.181 -30.872 27.139 1.00 10.15 ? 96  HIS   A CB  1 
ATOM   2815 C  CG  . HIS   B 1 96  ? -35.607 -32.165 26.671 1.00 11.14 ? 96  HIS   A CG  1 
ATOM   2816 N  ND1 . HIS   B 1 96  ? -35.373 -32.429 25.315 1.00 12.04 ? 96  HIS   A ND1 1 
ATOM   2817 C  CD2 . HIS   B 1 96  ? -35.103 -33.225 27.354 1.00 11.82 ? 96  HIS   A CD2 1 
ATOM   2818 C  CE1 . HIS   B 1 96  ? -34.832 -33.632 25.219 1.00 13.05 ? 96  HIS   A CE1 1 
ATOM   2819 N  NE2 . HIS   B 1 96  ? -34.662 -34.115 26.421 1.00 11.33 ? 96  HIS   A NE2 1 
ATOM   2820 N  N   . LEU   B 1 97  ? -34.718 -30.650 29.766 1.00 10.70 ? 97  LEU   A N   1 
ATOM   2821 C  CA  . LEU   B 1 97  ? -33.928 -31.000 30.955 1.00 10.78 ? 97  LEU   A CA  1 
ATOM   2822 C  C   . LEU   B 1 97  ? -34.548 -32.195 31.658 1.00 10.87 ? 97  LEU   A C   1 
ATOM   2823 O  O   . LEU   B 1 97  ? -35.782 -32.318 31.700 1.00 11.10 ? 97  LEU   A O   1 
ATOM   2824 C  CB  . LEU   B 1 97  ? -33.926 -29.818 31.956 1.00 11.60 ? 97  LEU   A CB  1 
ATOM   2825 C  CG  . LEU   B 1 97  ? -33.031 -29.968 33.206 1.00 12.25 ? 97  LEU   A CG  1 
ATOM   2826 C  CD1 . LEU   B 1 97  ? -31.536 -29.948 32.812 1.00 14.85 ? 97  LEU   A CD1 1 
ATOM   2827 C  CD2 . LEU   B 1 97  ? -33.326 -28.804 34.161 1.00 13.86 ? 97  LEU   A CD2 1 
ATOM   2828 N  N   . HIS   B 1 98  ? -33.690 -33.052 32.207 1.00 10.89 ? 98  HIS   A N   1 
ATOM   2829 C  CA  . HIS   B 1 98  ? -34.171 -34.154 33.032 1.00 11.38 ? 98  HIS   A CA  1 
ATOM   2830 C  C   . HIS   B 1 98  ? -33.652 -33.986 34.456 1.00 12.45 ? 98  HIS   A C   1 
ATOM   2831 O  O   . HIS   B 1 98  ? -32.515 -33.532 34.662 1.00 12.02 ? 98  HIS   A O   1 
ATOM   2832 C  CB  . HIS   B 1 98  ? -33.713 -35.530 32.522 1.00 11.24 ? 98  HIS   A CB  1 
ATOM   2833 C  CG  . HIS   B 1 98  ? -34.088 -35.832 31.109 1.00 11.10 ? 98  HIS   A CG  1 
ATOM   2834 N  ND1 . HIS   B 1 98  ? -35.259 -36.498 30.787 1.00 11.36 ? 98  HIS   A ND1 1 
ATOM   2835 C  CD2 . HIS   B 1 98  ? -33.479 -35.567 29.937 1.00 10.52 ? 98  HIS   A CD2 1 
ATOM   2836 C  CE1 . HIS   B 1 98  ? -35.384 -36.607 29.448 1.00 10.75 ? 98  HIS   A CE1 1 
ATOM   2837 N  NE2 . HIS   B 1 98  ? -34.285 -36.016 28.922 1.00 9.26  ? 98  HIS   A NE2 1 
ATOM   2838 N  N   . TRP   B 1 99  ? -34.495 -34.369 35.426 1.00 9.80  ? 99  TRP   A N   1 
ATOM   2839 C  CA  . TRP   B 1 99  ? -34.072 -34.298 36.834 1.00 10.80 ? 99  TRP   A CA  1 
ATOM   2840 C  C   . TRP   B 1 99  ? -34.755 -35.418 37.618 1.00 12.30 ? 99  TRP   A C   1 
ATOM   2841 O  O   . TRP   B 1 99  ? -35.615 -36.151 37.084 1.00 11.54 ? 99  TRP   A O   1 
ATOM   2842 C  CB  . TRP   B 1 99  ? -34.434 -32.920 37.409 1.00 10.98 ? 99  TRP   A CB  1 
ATOM   2843 C  CG  . TRP   B 1 99  ? -35.903 -32.617 37.291 1.00 11.41 ? 99  TRP   A CG  1 
ATOM   2844 C  CD1 . TRP   B 1 99  ? -36.877 -33.033 38.146 1.00 12.01 ? 99  TRP   A CD1 1 
ATOM   2845 C  CD2 . TRP   B 1 99  ? -36.548 -31.851 36.250 1.00 11.25 ? 99  TRP   A CD2 1 
ATOM   2846 N  NE1 . TRP   B 1 99  ? -38.112 -32.576 37.716 1.00 12.32 ? 99  TRP   A NE1 1 
ATOM   2847 C  CE2 . TRP   B 1 99  ? -37.933 -31.865 36.537 1.00 12.98 ? 99  TRP   A CE2 1 
ATOM   2848 C  CE3 . TRP   B 1 99  ? -36.114 -31.219 35.056 1.00 11.87 ? 99  TRP   A CE3 1 
ATOM   2849 C  CZ2 . TRP   B 1 99  ? -38.852 -31.198 35.738 1.00 11.30 ? 99  TRP   A CZ2 1 
ATOM   2850 C  CZ3 . TRP   B 1 99  ? -37.020 -30.543 34.259 1.00 12.08 ? 99  TRP   A CZ3 1 
ATOM   2851 C  CH2 . TRP   B 1 99  ? -38.396 -30.544 34.598 1.00 12.07 ? 99  TRP   A CH2 1 
ATOM   2852 N  N   . GLY   B 1 100 ? -34.342 -35.567 38.887 1.00 12.25 ? 100 GLY   A N   1 
ATOM   2853 C  CA  . GLY   B 1 100 ? -34.995 -36.565 39.727 1.00 13.95 ? 100 GLY   A CA  1 
ATOM   2854 C  C   . GLY   B 1 100 ? -35.633 -35.890 40.944 1.00 14.13 ? 100 GLY   A C   1 
ATOM   2855 O  O   . GLY   B 1 100 ? -35.650 -34.658 41.070 1.00 13.37 ? 100 GLY   A O   1 
ATOM   2856 N  N   . SER   B 1 101 ? -36.268 -36.726 41.784 1.00 14.04 ? 101 SER   A N   1 
ATOM   2857 C  CA  . SER   B 1 101 ? -36.992 -36.150 42.901 1.00 16.01 ? 101 SER   A CA  1 
ATOM   2858 C  C   . SER   B 1 101 ? -36.041 -35.678 44.008 1.00 16.90 ? 101 SER   A C   1 
ATOM   2859 O  O   . SER   B 1 101 ? -36.464 -34.935 44.890 1.00 17.49 ? 101 SER   A O   1 
ATOM   2860 C  CB  . SER   B 1 101 ? -38.007 -37.151 43.398 1.00 16.59 ? 101 SER   A CB  1 
ATOM   2861 O  OG  . SER   B 1 101 ? -37.378 -38.236 44.080 1.00 18.48 ? 101 SER   A OG  1 
ATOM   2862 N  N   . ALA   B 1 102 ? -34.756 -36.065 43.965 1.00 15.32 ? 102 ALA   A N   1 
ATOM   2863 C  CA  . ALA   B 1 102 ? -33.805 -35.575 44.966 1.00 15.63 ? 102 ALA   A CA  1 
ATOM   2864 C  C   . ALA   B 1 102 ? -32.513 -35.229 44.239 1.00 15.00 ? 102 ALA   A C   1 
ATOM   2865 O  O   . ALA   B 1 102 ? -32.255 -35.782 43.180 1.00 16.27 ? 102 ALA   A O   1 
ATOM   2866 C  CB  . ALA   B 1 102 ? -33.536 -36.618 46.032 1.00 17.05 ? 102 ALA   A CB  1 
ATOM   2867 N  N   . ASP   B 1 103 ? -31.718 -34.337 44.826 1.00 15.07 ? 103 ASP   A N   1 
ATOM   2868 C  CA  . ASP   B 1 103 ? -30.515 -33.853 44.163 1.00 17.68 ? 103 ASP   A CA  1 
ATOM   2869 C  C   . ASP   B 1 103 ? -29.457 -34.925 43.873 1.00 18.84 ? 103 ASP   A C   1 
ATOM   2870 O  O   . ASP   B 1 103 ? -28.604 -34.697 42.991 1.00 17.80 ? 103 ASP   A O   1 
ATOM   2871 C  CB  . ASP   B 1 103 ? -29.829 -32.747 44.951 1.00 18.63 ? 103 ASP   A CB  1 
ATOM   2872 C  CG  . ASP   B 1 103 ? -30.649 -31.479 45.082 1.00 18.18 ? 103 ASP   A CG  1 
ATOM   2873 O  OD1 . ASP   B 1 103 ? -31.634 -31.314 44.316 1.00 20.04 ? 103 ASP   A OD1 1 
ATOM   2874 O  OD2 . ASP   B 1 103 ? -30.298 -30.676 46.002 1.00 22.64 ? 103 ASP   A OD2 1 
ATOM   2875 N  N   . ASP   B 1 104 ? -29.479 -36.056 44.607 1.00 17.72 ? 104 ASP   A N   1 
ATOM   2876 C  CA  . ASP   B 1 104 ? -28.364 -37.001 44.558 1.00 21.01 ? 104 ASP   A CA  1 
ATOM   2877 C  C   . ASP   B 1 104 ? -28.459 -37.860 43.296 1.00 19.68 ? 104 ASP   A C   1 
ATOM   2878 O  O   . ASP   B 1 104 ? -27.515 -38.591 42.999 1.00 22.36 ? 104 ASP   A O   1 
ATOM   2879 C  CB  . ASP   B 1 104 ? -28.314 -37.943 45.769 1.00 24.72 ? 104 ASP   A CB  1 
ATOM   2880 C  CG  . ASP   B 1 104 ? -29.518 -38.878 45.827 1.00 31.65 ? 104 ASP   A CG  1 
ATOM   2881 O  OD1 . ASP   B 1 104 ? -30.579 -38.396 46.220 1.00 30.88 ? 104 ASP   A OD1 1 
ATOM   2882 O  OD2 . ASP   B 1 104 ? -29.402 -40.098 45.420 1.00 31.91 ? 104 ASP   A OD2 1 
ATOM   2883 N  N   . HIS   B 1 105 ? -29.622 -37.873 42.633 1.00 18.50 ? 105 HIS   A N   1 
ATOM   2884 C  CA  . HIS   B 1 105 ? -29.707 -38.597 41.366 1.00 20.79 ? 105 HIS   A CA  1 
ATOM   2885 C  C   . HIS   B 1 105 ? -30.828 -38.330 40.382 1.00 20.60 ? 105 HIS   A C   1 
ATOM   2886 O  O   . HIS   B 1 105 ? -31.966 -38.752 40.508 1.00 28.92 ? 105 HIS   A O   1 
ATOM   2887 C  CB  . HIS   B 1 105 ? -29.627 -40.130 41.508 1.00 26.12 ? 105 HIS   A CB  1 
ATOM   2888 C  CG  . HIS   B 1 105 ? -30.865 -40.806 41.998 1.00 30.03 ? 105 HIS   A CG  1 
ATOM   2889 N  ND1 . HIS   B 1 105 ? -31.135 -40.966 43.346 1.00 32.87 ? 105 HIS   A ND1 1 
ATOM   2890 C  CD2 . HIS   B 1 105 ? -31.901 -41.383 41.335 1.00 37.20 ? 105 HIS   A CD2 1 
ATOM   2891 C  CE1 . HIS   B 1 105 ? -32.281 -41.612 43.498 1.00 33.11 ? 105 HIS   A CE1 1 
ATOM   2892 N  NE2 . HIS   B 1 105 ? -32.788 -41.851 42.277 1.00 37.94 ? 105 HIS   A NE2 1 
ATOM   2893 N  N   . GLY   B 1 106 ? -30.456 -37.652 39.330 1.00 21.38 ? 106 GLY   A N   1 
ATOM   2894 C  CA  . GLY   B 1 106 ? -31.472 -37.076 38.474 1.00 20.99 ? 106 GLY   A CA  1 
ATOM   2895 C  C   . GLY   B 1 106 ? -31.014 -37.121 37.028 1.00 19.40 ? 106 GLY   A C   1 
ATOM   2896 O  O   . GLY   B 1 106 ? -31.820 -36.951 36.114 1.00 20.60 ? 106 GLY   A O   1 
ATOM   2897 N  N   . SER   B 1 107 ? -29.710 -37.316 36.839 1.00 16.03 ? 107 SER   A N   1 
ATOM   2898 C  CA  . SER   B 1 107 ? -29.214 -37.464 35.456 1.00 13.63 ? 107 SER   A CA  1 
ATOM   2899 C  C   . SER   B 1 107 ? -29.655 -38.780 34.793 1.00 14.68 ? 107 SER   A C   1 
ATOM   2900 O  O   . SER   B 1 107 ? -30.012 -39.793 35.449 1.00 16.52 ? 107 SER   A O   1 
ATOM   2901 C  CB  . SER   B 1 107 ? -27.704 -37.274 35.345 1.00 13.56 ? 107 SER   A CB  1 
ATOM   2902 O  OG  . SER   B 1 107 ? -27.055 -38.335 36.042 1.00 15.24 ? 107 SER   A OG  1 
ATOM   2903 N  N   . GLU   B 1 108 ? -29.713 -38.774 33.452 1.00 12.65 ? 108 GLU   A N   1 
ATOM   2904 C  CA  . GLU   B 1 108 ? -30.102 -39.994 32.729 1.00 13.92 ? 108 GLU   A CA  1 
ATOM   2905 C  C   . GLU   B 1 108 ? -28.898 -40.916 32.531 1.00 13.09 ? 108 GLU   A C   1 
ATOM   2906 O  O   . GLU   B 1 108 ? -28.953 -42.093 32.919 1.00 14.87 ? 108 GLU   A O   1 
ATOM   2907 C  CB  . GLU   B 1 108 ? -30.754 -39.606 31.396 1.00 16.05 ? 108 GLU   A CB  1 
ATOM   2908 C  CG  . GLU   B 1 108 ? -32.139 -39.073 31.667 1.00 16.97 ? 108 GLU   A CG  1 
ATOM   2909 C  CD  . GLU   B 1 108 ? -33.170 -39.275 30.582 1.00 16.23 ? 108 GLU   A CD  1 
ATOM   2910 O  OE1 . GLU   B 1 108 ? -32.842 -39.055 29.403 1.00 14.42 ? 108 GLU   A OE1 1 
ATOM   2911 O  OE2 . GLU   B 1 108 ? -34.278 -39.653 30.921 1.00 15.04 ? 108 GLU   A OE2 1 
ATOM   2912 N  N   . HIS   B 1 109 ? -27.811 -40.365 31.981 1.00 13.32 ? 109 HIS   A N   1 
ATOM   2913 C  CA  . HIS   B 1 109 ? -26.548 -41.118 31.936 1.00 14.84 ? 109 HIS   A CA  1 
ATOM   2914 C  C   . HIS   B 1 109 ? -25.885 -41.114 33.320 1.00 15.22 ? 109 HIS   A C   1 
ATOM   2915 O  O   . HIS   B 1 109 ? -26.056 -40.168 34.081 1.00 14.09 ? 109 HIS   A O   1 
ATOM   2916 C  CB  . HIS   B 1 109 ? -25.611 -40.515 30.875 1.00 13.10 ? 109 HIS   A CB  1 
ATOM   2917 C  CG  . HIS   B 1 109 ? -26.190 -40.718 29.515 1.00 13.50 ? 109 HIS   A CG  1 
ATOM   2918 N  ND1 . HIS   B 1 109 ? -27.070 -39.788 28.917 1.00 12.86 ? 109 HIS   A ND1 1 
ATOM   2919 C  CD2 . HIS   B 1 109 ? -26.048 -41.752 28.650 1.00 13.98 ? 109 HIS   A CD2 1 
ATOM   2920 C  CE1 . HIS   B 1 109 ? -27.393 -40.257 27.706 1.00 13.37 ? 109 HIS   A CE1 1 
ATOM   2921 N  NE2 . HIS   B 1 109 ? -26.798 -41.477 27.529 1.00 15.44 ? 109 HIS   A NE2 1 
ATOM   2922 N  N   . ILE   B 1 110 ? -25.168 -42.207 33.644 1.00 15.56 ? 110 ILE   A N   1 
ATOM   2923 C  CA  . ILE   B 1 110 ? -24.490 -42.318 34.935 1.00 15.64 ? 110 ILE   A CA  1 
ATOM   2924 C  C   . ILE   B 1 110 ? -23.037 -42.653 34.615 1.00 15.76 ? 110 ILE   A C   1 
ATOM   2925 O  O   . ILE   B 1 110 ? -22.814 -43.516 33.775 1.00 20.11 ? 110 ILE   A O   1 
ATOM   2926 C  CB  . ILE   B 1 110 ? -25.169 -43.444 35.759 1.00 19.56 ? 110 ILE   A CB  1 
ATOM   2927 C  CG1 . ILE   B 1 110 ? -26.601 -43.015 36.136 1.00 18.03 ? 110 ILE   A CG1 1 
ATOM   2928 C  CG2 . ILE   B 1 110 ? -24.329 -43.733 37.013 1.00 20.83 ? 110 ILE   A CG2 1 
ATOM   2929 C  CD1 . ILE   B 1 110 ? -27.382 -44.020 36.968 1.00 22.18 ? 110 ILE   A CD1 1 
ATOM   2930 N  N   . VAL   B 1 111 ? -22.068 -42.009 35.275 1.00 16.55 ? 111 VAL   A N   1 
ATOM   2931 C  CA  . VAL   B 1 111 ? -20.653 -42.179 34.933 1.00 17.48 ? 111 VAL   A CA  1 
ATOM   2932 C  C   . VAL   B 1 111 ? -19.925 -42.840 36.108 1.00 19.25 ? 111 VAL   A C   1 
ATOM   2933 O  O   . VAL   B 1 111 ? -19.828 -42.222 37.166 1.00 20.94 ? 111 VAL   A O   1 
ATOM   2934 C  CB  . VAL   B 1 111 ? -19.995 -40.809 34.682 1.00 20.06 ? 111 VAL   A CB  1 
ATOM   2935 C  CG1 . VAL   B 1 111 ? -18.531 -40.955 34.281 1.00 22.31 ? 111 VAL   A CG1 1 
ATOM   2936 C  CG2 . VAL   B 1 111 ? -20.774 -40.048 33.614 1.00 19.47 ? 111 VAL   A CG2 1 
ATOM   2937 N  N   . ASP   B 1 112 ? -19.456 -44.066 35.860 1.00 20.85 ? 112 ASP   A N   1 
ATOM   2938 C  CA  . ASP   B 1 112 ? -18.790 -44.866 36.889 1.00 25.67 ? 112 ASP   A CA  1 
ATOM   2939 C  C   . ASP   B 1 112 ? -19.638 -44.913 38.176 1.00 24.62 ? 112 ASP   A C   1 
ATOM   2940 O  O   . ASP   B 1 112 ? -19.129 -44.717 39.294 1.00 24.71 ? 112 ASP   A O   1 
ATOM   2941 C  CB  . ASP   B 1 112 ? -17.379 -44.311 37.119 1.00 25.30 ? 112 ASP   A CB  1 
ATOM   2942 C  CG  . ASP   B 1 112 ? -16.391 -44.521 35.976 1.00 28.14 ? 112 ASP   A CG  1 
ATOM   2943 O  OD1 . ASP   B 1 112 ? -16.437 -45.571 35.323 1.00 29.27 ? 112 ASP   A OD1 1 
ATOM   2944 O  OD2 . ASP   B 1 112 ? -15.509 -43.659 35.810 1.00 32.46 ? 112 ASP   A OD2 1 
ATOM   2945 N  N   . GLY   B 1 113 ? -20.964 -45.119 38.059 1.00 22.70 ? 113 GLY   A N   1 
ATOM   2946 C  CA  . GLY   B 1 113 ? -21.861 -45.176 39.214 1.00 22.99 ? 113 GLY   A CA  1 
ATOM   2947 C  C   . GLY   B 1 113 ? -22.241 -43.834 39.863 1.00 23.93 ? 113 GLY   A C   1 
ATOM   2948 O  O   . GLY   B 1 113 ? -23.096 -43.763 40.762 1.00 25.11 ? 113 GLY   A O   1 
ATOM   2949 N  N   . VAL   B 1 114 ? -21.683 -42.723 39.370 1.00 21.21 ? 114 VAL   A N   1 
ATOM   2950 C  CA  . VAL   B 1 114 ? -22.085 -41.416 39.834 1.00 21.94 ? 114 VAL   A CA  1 
ATOM   2951 C  C   . VAL   B 1 114 ? -23.209 -40.845 38.972 1.00 21.44 ? 114 VAL   A C   1 
ATOM   2952 O  O   . VAL   B 1 114 ? -23.076 -40.795 37.727 1.00 19.93 ? 114 VAL   A O   1 
ATOM   2953 C  CB  . VAL   B 1 114 ? -20.888 -40.446 39.866 1.00 25.45 ? 114 VAL   A CB  1 
ATOM   2954 C  CG1 . VAL   B 1 114 ? -21.263 -39.215 40.686 1.00 31.45 ? 114 VAL   A CG1 1 
ATOM   2955 C  CG2 . VAL   B 1 114 ? -19.670 -41.115 40.493 1.00 31.39 ? 114 VAL   A CG2 1 
ATOM   2956 N  N   . SER   B 1 115 ? -24.291 -40.437 39.665 1.00 19.54 ? 115 SER   A N   1 
ATOM   2957 C  CA  . SER   B 1 115 ? -25.346 -39.627 39.100 1.00 17.87 ? 115 SER   A CA  1 
ATOM   2958 C  C   . SER   B 1 115 ? -25.036 -38.151 39.337 1.00 20.62 ? 115 SER   A C   1 
ATOM   2959 O  O   . SER   B 1 115 ? -24.540 -37.741 40.409 1.00 24.84 ? 115 SER   A O   1 
ATOM   2960 C  CB  . SER   B 1 115 ? -26.684 -39.973 39.674 1.00 17.99 ? 115 SER   A CB  1 
ATOM   2961 O  OG  . SER   B 1 115 ? -27.010 -41.317 39.273 1.00 18.67 ? 115 SER   A OG  1 
ATOM   2962 N  N   . TYR   B 1 116 ? -25.441 -37.342 38.371 1.00 16.12 ? 116 TYR   A N   1 
ATOM   2963 C  CA  . TYR   B 1 116 ? -25.500 -35.916 38.615 1.00 14.98 ? 116 TYR   A CA  1 
ATOM   2964 C  C   . TYR   B 1 116 ? -26.919 -35.548 39.011 1.00 14.28 ? 116 TYR   A C   1 
ATOM   2965 O  O   . TYR   B 1 116 ? -27.786 -36.427 39.000 1.00 18.34 ? 116 TYR   A O   1 
ATOM   2966 C  CB  . TYR   B 1 116 ? -25.006 -35.182 37.354 1.00 15.53 ? 116 TYR   A CB  1 
ATOM   2967 C  CG  . TYR   B 1 116 ? -23.527 -35.410 37.149 1.00 18.37 ? 116 TYR   A CG  1 
ATOM   2968 C  CD1 . TYR   B 1 116 ? -22.627 -34.600 37.821 1.00 21.70 ? 116 TYR   A CD1 1 
ATOM   2969 C  CD2 . TYR   B 1 116 ? -23.049 -36.446 36.372 1.00 17.57 ? 116 TYR   A CD2 1 
ATOM   2970 C  CE1 . TYR   B 1 116 ? -21.258 -34.751 37.659 1.00 24.20 ? 116 TYR   A CE1 1 
ATOM   2971 C  CE2 . TYR   B 1 116 ? -21.678 -36.617 36.200 1.00 21.41 ? 116 TYR   A CE2 1 
ATOM   2972 C  CZ  . TYR   B 1 116 ? -20.799 -35.766 36.846 1.00 24.17 ? 116 TYR   A CZ  1 
ATOM   2973 O  OH  . TYR   B 1 116 ? -19.445 -35.891 36.665 1.00 29.16 ? 116 TYR   A OH  1 
ATOM   2974 N  N   . ALA   B 1 117 ? -27.152 -34.265 39.268 1.00 14.16 ? 117 ALA   A N   1 
ATOM   2975 C  CA  . ALA   B 1 117 ? -28.442 -33.798 39.756 1.00 14.98 ? 117 ALA   A CA  1 
ATOM   2976 C  C   . ALA   B 1 117 ? -29.433 -33.655 38.602 1.00 16.08 ? 117 ALA   A C   1 
ATOM   2977 O  O   . ALA   B 1 117 ? -30.652 -33.841 38.775 1.00 15.77 ? 117 ALA   A O   1 
ATOM   2978 C  CB  . ALA   B 1 117 ? -28.259 -32.471 40.441 1.00 15.88 ? 117 ALA   A CB  1 
ATOM   2979 N  N   . ALA   B 1 118 ? -28.913 -33.300 37.407 1.00 13.78 ? 118 ALA   A N   1 
ATOM   2980 C  CA  . ALA   B 1 118 ? -29.835 -33.117 36.278 1.00 12.17 ? 118 ALA   A CA  1 
ATOM   2981 C  C   . ALA   B 1 118 ? -29.029 -33.239 34.972 1.00 12.35 ? 118 ALA   A C   1 
ATOM   2982 O  O   . ALA   B 1 118 ? -27.791 -33.428 35.027 1.00 11.61 ? 118 ALA   A O   1 
ATOM   2983 C  CB  . ALA   B 1 118 ? -30.539 -31.768 36.395 1.00 12.83 ? 118 ALA   A CB  1 
ATOM   2984 N  N   . GLU   B 1 119 ? -29.716 -33.260 33.815 1.00 10.79 ? 119 GLU   A N   1 
ATOM   2985 C  CA  . GLU   B 1 119 ? -29.009 -33.464 32.563 1.00 10.84 ? 119 GLU   A CA  1 
ATOM   2986 C  C   . GLU   B 1 119 ? -29.782 -32.710 31.477 1.00 10.84 ? 119 GLU   A C   1 
ATOM   2987 O  O   . GLU   B 1 119 ? -30.993 -32.923 31.299 1.00 12.04 ? 119 GLU   A O   1 
ATOM   2988 C  CB  . GLU   B 1 119 ? -28.945 -34.960 32.228 1.00 11.87 ? 119 GLU   A CB  1 
ATOM   2989 C  CG  . GLU   B 1 119 ? -28.106 -35.295 30.970 1.00 13.20 ? 119 GLU   A CG  1 
ATOM   2990 C  CD  . GLU   B 1 119 ? -27.926 -36.811 30.800 1.00 15.33 ? 119 GLU   A CD  1 
ATOM   2991 O  OE1 . GLU   B 1 119 ? -27.784 -37.573 31.832 1.00 15.83 ? 119 GLU   A OE1 1 
ATOM   2992 O  OE2 . GLU   B 1 119 ? -27.871 -37.278 29.641 1.00 16.33 ? 119 GLU   A OE2 1 
ATOM   2993 N  N   . LEU   B 1 120 ? -29.074 -31.802 30.790 1.00 11.11 ? 120 LEU   A N   1 
ATOM   2994 C  CA  . LEU   B 1 120 ? -29.646 -31.016 29.694 1.00 12.26 ? 120 LEU   A CA  1 
ATOM   2995 C  C   . LEU   B 1 120 ? -29.417 -31.777 28.394 1.00 11.79 ? 120 LEU   A C   1 
ATOM   2996 O  O   . LEU   B 1 120 ? -28.307 -32.299 28.162 1.00 12.58 ? 120 LEU   A O   1 
ATOM   2997 C  CB  . LEU   B 1 120 ? -28.852 -29.696 29.625 1.00 13.45 ? 120 LEU   A CB  1 
ATOM   2998 C  CG  . LEU   B 1 120 ? -29.397 -28.570 28.731 1.00 16.24 ? 120 LEU   A CG  1 
ATOM   2999 C  CD1 . LEU   B 1 120 ? -30.673 -27.948 29.346 1.00 15.56 ? 120 LEU   A CD1 1 
ATOM   3000 C  CD2 . LEU   B 1 120 ? -28.334 -27.474 28.593 1.00 18.94 ? 120 LEU   A CD2 1 
ATOM   3001 N  N   . HIS   B 1 121 ? -30.447 -31.836 27.553 1.00 11.43 ? 121 HIS   A N   1 
ATOM   3002 C  CA  . HIS   B 1 121 ? -30.356 -32.469 26.247 1.00 10.69 ? 121 HIS   A CA  1 
ATOM   3003 C  C   . HIS   B 1 121 ? -30.656 -31.453 25.149 1.00 11.15 ? 121 HIS   A C   1 
ATOM   3004 O  O   . HIS   B 1 121 ? -31.634 -30.712 25.250 1.00 11.90 ? 121 HIS   A O   1 
ATOM   3005 C  CB  . HIS   B 1 121 ? -31.341 -33.643 26.112 1.00 10.75 ? 121 HIS   A CB  1 
ATOM   3006 C  CG  . HIS   B 1 121 ? -30.986 -34.834 26.929 1.00 11.14 ? 121 HIS   A CG  1 
ATOM   3007 N  ND1 . HIS   B 1 121 ? -31.923 -35.853 27.173 1.00 10.94 ? 121 HIS   A ND1 1 
ATOM   3008 C  CD2 . HIS   B 1 121 ? -29.796 -35.163 27.465 1.00 12.05 ? 121 HIS   A CD2 1 
ATOM   3009 C  CE1 . HIS   B 1 121 ? -31.255 -36.758 27.942 1.00 12.82 ? 121 HIS   A CE1 1 
ATOM   3010 N  NE2 . HIS   B 1 121 ? -29.969 -36.385 28.087 1.00 13.37 ? 121 HIS   A NE2 1 
ATOM   3011 N  N   . VAL   B 1 122 ? -29.751 -31.430 24.144 1.00 11.13 ? 122 VAL   A N   1 
ATOM   3012 C  CA  . VAL   B 1 122 ? -29.866 -30.511 23.012 1.00 10.91 ? 122 VAL   A CA  1 
ATOM   3013 C  C   . VAL   B 1 122 ? -30.065 -31.401 21.786 1.00 11.03 ? 122 VAL   A C   1 
ATOM   3014 O  O   . VAL   B 1 122 ? -29.165 -32.151 21.427 1.00 10.91 ? 122 VAL   A O   1 
ATOM   3015 C  CB  . VAL   B 1 122 ? -28.559 -29.694 22.887 1.00 11.14 ? 122 VAL   A CB  1 
ATOM   3016 C  CG1 . VAL   B 1 122 ? -28.732 -28.604 21.804 1.00 12.38 ? 122 VAL   A CG1 1 
ATOM   3017 C  CG2 . VAL   B 1 122 ? -28.187 -29.047 24.222 1.00 14.01 ? 122 VAL   A CG2 1 
ATOM   3018 N  N   . VAL   B 1 123 ? -31.244 -31.319 21.149 1.00 9.64  ? 123 VAL   A N   1 
ATOM   3019 C  CA  . VAL   B 1 123 ? -31.678 -32.302 20.153 1.00 10.47 ? 123 VAL   A CA  1 
ATOM   3020 C  C   . VAL   B 1 123 ? -31.481 -31.698 18.748 1.00 11.65 ? 123 VAL   A C   1 
ATOM   3021 O  O   . VAL   B 1 123 ? -31.959 -30.586 18.500 1.00 12.37 ? 123 VAL   A O   1 
ATOM   3022 C  CB  . VAL   B 1 123 ? -33.174 -32.644 20.361 1.00 10.76 ? 123 VAL   A CB  1 
ATOM   3023 C  CG1 . VAL   B 1 123 ? -33.631 -33.684 19.339 1.00 11.99 ? 123 VAL   A CG1 1 
ATOM   3024 C  CG2 . VAL   B 1 123 ? -33.360 -33.242 21.761 1.00 11.50 ? 123 VAL   A CG2 1 
ATOM   3025 N  N   . HIS   B 1 124 ? -30.833 -32.455 17.858 1.00 10.57 ? 124 HIS   A N   1 
ATOM   3026 C  CA  . HIS   B 1 124 ? -30.537 -32.032 16.479 1.00 12.91 ? 124 HIS   A CA  1 
ATOM   3027 C  C   . HIS   B 1 124 ? -30.962 -33.094 15.473 1.00 12.36 ? 124 HIS   A C   1 
ATOM   3028 O  O   . HIS   B 1 124 ? -31.065 -34.273 15.839 1.00 12.88 ? 124 HIS   A O   1 
ATOM   3029 C  CB  . HIS   B 1 124 ? -29.036 -31.836 16.277 1.00 11.88 ? 124 HIS   A CB  1 
ATOM   3030 C  CG  . HIS   B 1 124 ? -28.384 -30.999 17.304 1.00 12.32 ? 124 HIS   A CG  1 
ATOM   3031 N  ND1 . HIS   B 1 124 ? -28.064 -31.534 18.558 1.00 13.36 ? 124 HIS   A ND1 1 
ATOM   3032 C  CD2 . HIS   B 1 124 ? -27.824 -29.769 17.249 1.00 13.23 ? 124 HIS   A CD2 1 
ATOM   3033 C  CE1 . HIS   B 1 124 ? -27.462 -30.632 19.270 1.00 13.17 ? 124 HIS   A CE1 1 
ATOM   3034 N  NE2 . HIS   B 1 124 ? -27.261 -29.543 18.512 1.00 13.88 ? 124 HIS   A NE2 1 
ATOM   3035 N  N   . TRP   B 1 125 ? -31.179 -32.678 14.199 1.00 10.72 ? 125 TRP   A N   1 
ATOM   3036 C  CA  . TRP   B 1 125 ? -31.586 -33.658 13.195 1.00 11.82 ? 125 TRP   A CA  1 
ATOM   3037 C  C   . TRP   B 1 125 ? -30.806 -33.453 11.886 1.00 12.01 ? 125 TRP   A C   1 
ATOM   3038 O  O   . TRP   B 1 125 ? -30.383 -32.324 11.594 1.00 12.45 ? 125 TRP   A O   1 
ATOM   3039 C  CB  . TRP   B 1 125 ? -33.097 -33.662 12.929 1.00 11.70 ? 125 TRP   A CB  1 
ATOM   3040 C  CG  . TRP   B 1 125 ? -33.670 -32.362 12.479 1.00 13.54 ? 125 TRP   A CG  1 
ATOM   3041 C  CD1 . TRP   B 1 125 ? -34.024 -31.333 13.308 1.00 14.43 ? 125 TRP   A CD1 1 
ATOM   3042 C  CD2 . TRP   B 1 125 ? -34.019 -31.961 11.149 1.00 12.23 ? 125 TRP   A CD2 1 
ATOM   3043 N  NE1 . TRP   B 1 125 ? -34.613 -30.317 12.590 1.00 13.77 ? 125 TRP   A NE1 1 
ATOM   3044 C  CE2 . TRP   B 1 125 ? -34.594 -30.670 11.267 1.00 12.69 ? 125 TRP   A CE2 1 
ATOM   3045 C  CE3 . TRP   B 1 125 ? -33.935 -32.592 9.905  1.00 14.28 ? 125 TRP   A CE3 1 
ATOM   3046 C  CZ2 . TRP   B 1 125 ? -35.119 -29.983 10.163 1.00 14.95 ? 125 TRP   A CZ2 1 
ATOM   3047 C  CZ3 . TRP   B 1 125 ? -34.414 -31.910 8.801  1.00 14.08 ? 125 TRP   A CZ3 1 
ATOM   3048 C  CH2 . TRP   B 1 125 ? -34.979 -30.637 8.944  1.00 14.62 ? 125 TRP   A CH2 1 
ATOM   3049 N  N   . ASN   B 1 126 ? -30.632 -34.558 11.145 1.00 11.88 ? 126 ASN   A N   1 
ATOM   3050 C  CA  . ASN   B 1 126 ? -29.801 -34.540 9.943  1.00 13.30 ? 126 ASN   A CA  1 
ATOM   3051 C  C   . ASN   B 1 126 ? -30.543 -33.907 8.761  1.00 13.79 ? 126 ASN   A C   1 
ATOM   3052 O  O   . ASN   B 1 126 ? -31.286 -34.587 8.049  1.00 13.16 ? 126 ASN   A O   1 
ATOM   3053 C  CB  . ASN   B 1 126 ? -29.459 -35.983 9.552  1.00 13.79 ? 126 ASN   A CB  1 
ATOM   3054 C  CG  . ASN   B 1 126 ? -28.383 -36.083 8.501  1.00 17.22 ? 126 ASN   A CG  1 
ATOM   3055 O  OD1 . ASN   B 1 126 ? -28.282 -35.198 7.632  1.00 16.82 ? 126 ASN   A OD1 1 
ATOM   3056 N  ND2 . ASN   B 1 126 ? -27.646 -37.197 8.506  1.00 16.41 ? 126 ASN   A ND2 1 
ATOM   3057 N  N   . SER   B 1 127 ? -30.282 -32.621 8.524  1.00 13.47 ? 127 SER   A N   1 
ATOM   3058 C  CA  . SER   B 1 127 ? -30.983 -31.880 7.478  1.00 15.38 ? 127 SER   A CA  1 
ATOM   3059 C  C   . SER   B 1 127 ? -30.231 -32.007 6.142  1.00 15.58 ? 127 SER   A C   1 
ATOM   3060 O  O   . SER   B 1 127 ? -30.755 -31.573 5.093  1.00 15.19 ? 127 SER   A O   1 
ATOM   3061 C  CB  . SER   B 1 127 ? -31.163 -30.416 7.878  1.00 12.48 ? 127 SER   A CB  1 
ATOM   3062 O  OG  . SER   B 1 127 ? -29.859 -29.863 8.039  1.00 15.52 ? 127 SER   A OG  1 
ATOM   3063 N  N   . ASP   B 1 128 ? -29.096 -32.713 6.127  1.00 14.71 ? 128 ASP   A N   1 
ATOM   3064 C  CA  . ASP   B 1 128 ? -28.448 -33.000 4.838  1.00 17.22 ? 128 ASP   A CA  1 
ATOM   3065 C  C   . ASP   B 1 128 ? -29.100 -34.171 4.114  1.00 15.82 ? 128 ASP   A C   1 
ATOM   3066 O  O   . ASP   B 1 128 ? -28.923 -34.306 2.887  1.00 16.33 ? 128 ASP   A O   1 
ATOM   3067 C  CB  . ASP   B 1 128 ? -26.957 -33.326 5.014  1.00 18.10 ? 128 ASP   A CB  1 
ATOM   3068 C  CG  . ASP   B 1 128 ? -26.064 -32.101 5.244  1.00 22.59 ? 128 ASP   A CG  1 
ATOM   3069 O  OD1 . ASP   B 1 128 ? -26.549 -30.932 5.131  1.00 23.85 ? 128 ASP   A OD1 1 
ATOM   3070 O  OD2 . ASP   B 1 128 ? -24.837 -32.300 5.497  1.00 20.57 ? 128 ASP   A OD2 1 
ATOM   3071 N  N   . LYS   B 1 129 ? -29.835 -35.031 4.841  1.00 15.07 ? 129 LYS   A N   1 
ATOM   3072 C  CA  . LYS   B 1 129 ? -30.472 -36.217 4.277  1.00 14.78 ? 129 LYS   A CA  1 
ATOM   3073 C  C   . LYS   B 1 129 ? -31.993 -36.248 4.371  1.00 15.72 ? 129 LYS   A C   1 
ATOM   3074 O  O   . LYS   B 1 129 ? -32.638 -36.955 3.579  1.00 17.83 ? 129 LYS   A O   1 
ATOM   3075 C  CB  . LYS   B 1 129 ? -29.973 -37.492 4.983  1.00 18.19 ? 129 LYS   A CB  1 
ATOM   3076 C  CG  . LYS   B 1 129 ? -28.578 -37.909 4.529  1.00 20.42 ? 129 LYS   A CG  1 
ATOM   3077 C  CD  . LYS   B 1 129 ? -28.097 -39.237 5.086  1.00 19.59 ? 129 LYS   A CD  1 
ATOM   3078 C  CE  . LYS   B 1 129 ? -28.924 -40.436 4.635  1.00 22.54 ? 129 LYS   A CE  1 
ATOM   3079 N  NZ  . LYS   B 1 129 ? -28.358 -41.740 5.080  1.00 25.08 ? 129 LYS   A NZ  1 
ATOM   3080 N  N   . TYR   B 1 130 ? -32.569 -35.598 5.405  1.00 14.95 ? 130 TYR   A N   1 
ATOM   3081 C  CA  . TYR   B 1 130 ? -33.984 -35.795 5.748  1.00 16.19 ? 130 TYR   A CA  1 
ATOM   3082 C  C   . TYR   B 1 130 ? -34.713 -34.459 5.679  1.00 13.11 ? 130 TYR   A C   1 
ATOM   3083 O  O   . TYR   B 1 130 ? -34.091 -33.398 5.914  1.00 16.36 ? 130 TYR   A O   1 
ATOM   3084 C  CB  . TYR   B 1 130 ? -34.130 -36.460 7.145  1.00 14.94 ? 130 TYR   A CB  1 
ATOM   3085 C  CG  . TYR   B 1 130 ? -33.370 -37.759 7.149  1.00 17.48 ? 130 TYR   A CG  1 
ATOM   3086 C  CD1 . TYR   B 1 130 ? -33.714 -38.768 6.247  1.00 19.33 ? 130 TYR   A CD1 1 
ATOM   3087 C  CD2 . TYR   B 1 130 ? -32.239 -37.958 7.941  1.00 17.45 ? 130 TYR   A CD2 1 
ATOM   3088 C  CE1 . TYR   B 1 130 ? -32.969 -39.933 6.143  1.00 21.65 ? 130 TYR   A CE1 1 
ATOM   3089 C  CE2 . TYR   B 1 130 ? -31.515 -39.135 7.870  1.00 17.17 ? 130 TYR   A CE2 1 
ATOM   3090 C  CZ  . TYR   B 1 130 ? -31.889 -40.143 6.991  1.00 20.74 ? 130 TYR   A CZ  1 
ATOM   3091 O  OH  . TYR   B 1 130 ? -31.160 -41.302 6.885  1.00 18.29 ? 130 TYR   A OH  1 
ATOM   3092 N  N   . PRO   B 1 131 ? -36.028 -34.471 5.332  1.00 15.72 ? 131 PRO   A N   1 
ATOM   3093 C  CA  . PRO   B 1 131 ? -36.781 -33.214 5.136  1.00 18.40 ? 131 PRO   A CA  1 
ATOM   3094 C  C   . PRO   B 1 131 ? -37.290 -32.573 6.431  1.00 18.08 ? 131 PRO   A C   1 
ATOM   3095 O  O   . PRO   B 1 131 ? -37.671 -31.396 6.467  1.00 18.32 ? 131 PRO   A O   1 
ATOM   3096 C  CB  . PRO   B 1 131 ? -37.990 -33.660 4.305  1.00 18.67 ? 131 PRO   A CB  1 
ATOM   3097 C  CG  . PRO   B 1 131 ? -38.205 -35.099 4.705  1.00 18.30 ? 131 PRO   A CG  1 
ATOM   3098 C  CD  . PRO   B 1 131 ? -36.794 -35.662 4.891  1.00 16.81 ? 131 PRO   A CD  1 
ATOM   3099 N  N   . SER   B 1 132 ? -37.288 -33.345 7.536  1.00 16.05 ? 132 SER   A N   1 
ATOM   3100 C  CA  . SER   B 1 132 ? -37.871 -32.839 8.765  1.00 15.27 ? 132 SER   A CA  1 
ATOM   3101 C  C   . SER   B 1 132 ? -37.333 -33.653 9.936  1.00 15.26 ? 132 SER   A C   1 
ATOM   3102 O  O   . SER   B 1 132 ? -36.857 -34.766 9.747  1.00 15.44 ? 132 SER   A O   1 
ATOM   3103 C  CB  . SER   B 1 132 ? -39.381 -32.991 8.731  1.00 18.12 ? 132 SER   A CB  1 
ATOM   3104 O  OG  . SER   B 1 132 ? -39.749 -34.366 8.642  1.00 18.14 ? 132 SER   A OG  1 
ATOM   3105 N  N   . PHE   B 1 133 ? -37.457 -33.083 11.133 1.00 16.50 ? 133 PHE   A N   1 
ATOM   3106 C  CA  . PHE   B 1 133 ? -37.188 -33.798 12.370 1.00 17.32 ? 133 PHE   A CA  1 
ATOM   3107 C  C   . PHE   B 1 133 ? -38.001 -35.102 12.404 1.00 18.08 ? 133 PHE   A C   1 
ATOM   3108 O  O   . PHE   B 1 133 ? -37.483 -36.172 12.727 1.00 16.96 ? 133 PHE   A O   1 
ATOM   3109 C  CB  . PHE   B 1 133 ? -37.467 -32.845 13.542 1.00 20.37 ? 133 PHE   A CB  1 
ATOM   3110 C  CG  . PHE   B 1 133 ? -37.464 -33.588 14.852 1.00 24.84 ? 133 PHE   A CG  1 
ATOM   3111 C  CD1 . PHE   B 1 133 ? -36.262 -33.968 15.449 1.00 19.92 ? 133 PHE   A CD1 1 
ATOM   3112 C  CD2 . PHE   B 1 133 ? -38.670 -34.028 15.392 1.00 26.94 ? 133 PHE   A CD2 1 
ATOM   3113 C  CE1 . PHE   B 1 133 ? -36.286 -34.700 16.628 1.00 23.57 ? 133 PHE   A CE1 1 
ATOM   3114 C  CE2 . PHE   B 1 133 ? -38.679 -34.810 16.537 1.00 27.41 ? 133 PHE   A CE2 1 
ATOM   3115 C  CZ  . PHE   B 1 133 ? -37.488 -35.119 17.161 1.00 25.45 ? 133 PHE   A CZ  1 
ATOM   3116 N  N   . VAL   B 1 134 ? -39.293 -35.033 12.145 1.00 18.78 ? 134 VAL   A N   1 
ATOM   3117 C  CA  . VAL   B 1 134 ? -40.142 -36.213 12.243 1.00 19.41 ? 134 VAL   A CA  1 
ATOM   3118 C  C   . VAL   B 1 134 ? -39.630 -37.376 11.380 1.00 20.05 ? 134 VAL   A C   1 
ATOM   3119 O  O   . VAL   B 1 134 ? -39.603 -38.544 11.798 1.00 20.76 ? 134 VAL   A O   1 
ATOM   3120 C  CB  . VAL   B 1 134 ? -41.577 -35.797 11.862 1.00 25.65 ? 134 VAL   A CB  1 
ATOM   3121 C  CG1 . VAL   B 1 134 ? -42.441 -37.006 11.552 1.00 32.16 ? 134 VAL   A CG1 1 
ATOM   3122 C  CG2 . VAL   B 1 134 ? -42.178 -34.954 12.960 1.00 27.13 ? 134 VAL   A CG2 1 
ATOM   3123 N  N   A GLU   B 1 135 ? -39.224 -37.103 10.132 0.50 18.03 ? 135 GLU   A N   1 
ATOM   3124 N  N   B GLU   B 1 135 ? -39.256 -37.063 10.132 0.50 17.06 ? 135 GLU   A N   1 
ATOM   3125 C  CA  A GLU   B 1 135 ? -38.745 -38.211 9.315  0.50 19.32 ? 135 GLU   A CA  1 
ATOM   3126 C  CA  B GLU   B 1 135 ? -38.726 -38.080 9.239  0.50 17.84 ? 135 GLU   A CA  1 
ATOM   3127 C  C   A GLU   B 1 135 ? -37.341 -38.659 9.743  0.50 18.08 ? 135 GLU   A C   1 
ATOM   3128 C  C   B GLU   B 1 135 ? -37.406 -38.622 9.798  0.50 17.17 ? 135 GLU   A C   1 
ATOM   3129 O  O   A GLU   B 1 135 ? -36.979 -39.837 9.642  0.50 18.16 ? 135 GLU   A O   1 
ATOM   3130 O  O   B GLU   B 1 135 ? -37.194 -39.830 9.888  0.50 17.72 ? 135 GLU   A O   1 
ATOM   3131 C  CB  A GLU   B 1 135 ? -38.790 -37.903 7.815  0.50 22.12 ? 135 GLU   A CB  1 
ATOM   3132 C  CB  B GLU   B 1 135 ? -38.562 -37.519 7.819  0.50 18.64 ? 135 GLU   A CB  1 
ATOM   3133 C  CG  A GLU   B 1 135 ? -37.849 -38.803 7.037  0.50 24.82 ? 135 GLU   A CG  1 
ATOM   3134 C  CG  B GLU   B 1 135 ? -39.865 -37.412 7.045  0.50 20.10 ? 135 GLU   A CG  1 
ATOM   3135 C  CD  A GLU   B 1 135 ? -38.281 -40.239 6.794  0.50 26.81 ? 135 GLU   A CD  1 
ATOM   3136 C  CD  B GLU   B 1 135 ? -40.556 -38.708 6.640  0.50 22.37 ? 135 GLU   A CD  1 
ATOM   3137 O  OE1 A GLU   B 1 135 ? -37.497 -41.156 7.112  0.50 22.61 ? 135 GLU   A OE1 1 
ATOM   3138 O  OE1 B GLU   B 1 135 ? -40.020 -39.787 6.921  0.50 24.36 ? 135 GLU   A OE1 1 
ATOM   3139 O  OE2 A GLU   B 1 135 ? -39.400 -40.445 6.247  0.50 29.53 ? 135 GLU   A OE2 1 
ATOM   3140 O  OE2 B GLU   B 1 135 ? -41.629 -38.635 6.031  0.50 22.52 ? 135 GLU   A OE2 1 
ATOM   3141 N  N   . ALA   B 1 136 ? -36.514 -37.715 10.194 1.00 16.51 ? 136 ALA   A N   1 
ATOM   3142 C  CA  . ALA   B 1 136 ? -35.176 -38.069 10.645 1.00 14.80 ? 136 ALA   A CA  1 
ATOM   3143 C  C   . ALA   B 1 136 ? -35.260 -38.982 11.873 1.00 14.78 ? 136 ALA   A C   1 
ATOM   3144 O  O   . ALA   B 1 136 ? -34.460 -39.892 11.988 1.00 14.80 ? 136 ALA   A O   1 
ATOM   3145 C  CB  . ALA   B 1 136 ? -34.360 -36.822 10.944 1.00 14.03 ? 136 ALA   A CB  1 
ATOM   3146 N  N   . ALA   B 1 137 ? -36.324 -38.834 12.664 1.00 17.37 ? 137 ALA   A N   1 
ATOM   3147 C  CA  . ALA   B 1 137 ? -36.391 -39.575 13.937 1.00 15.47 ? 137 ALA   A CA  1 
ATOM   3148 C  C   . ALA   B 1 137 ? -36.627 -41.062 13.678 1.00 17.86 ? 137 ALA   A C   1 
ATOM   3149 O  O   . ALA   B 1 137 ? -36.414 -41.866 14.582 1.00 18.40 ? 137 ALA   A O   1 
ATOM   3150 C  CB  . ALA   B 1 137 ? -37.450 -38.988 14.825 1.00 15.98 ? 137 ALA   A CB  1 
ATOM   3151 N  N   . HIS   B 1 138 ? -37.003 -41.433 12.434 1.00 18.86 ? 138 HIS   A N   1 
ATOM   3152 C  CA  . HIS   B 1 138 ? -37.180 -42.833 12.061 1.00 20.64 ? 138 HIS   A CA  1 
ATOM   3153 C  C   . HIS   B 1 138 ? -35.995 -43.444 11.319 1.00 21.24 ? 138 HIS   A C   1 
ATOM   3154 O  O   . HIS   B 1 138 ? -36.123 -44.523 10.701 1.00 23.29 ? 138 HIS   A O   1 
ATOM   3155 C  CB  . HIS   B 1 138 ? -38.480 -43.023 11.246 1.00 22.87 ? 138 HIS   A CB  1 
ATOM   3156 C  CG  . HIS   B 1 138 ? -39.691 -42.722 12.044 1.00 24.83 ? 138 HIS   A CG  1 
ATOM   3157 N  ND1 . HIS   B 1 138 ? -40.370 -43.706 12.736 1.00 29.59 ? 138 HIS   A ND1 1 
ATOM   3158 C  CD2 . HIS   B 1 138 ? -40.298 -41.561 12.355 1.00 27.71 ? 138 HIS   A CD2 1 
ATOM   3159 C  CE1 . HIS   B 1 138 ? -41.366 -43.166 13.407 1.00 26.05 ? 138 HIS   A CE1 1 
ATOM   3160 N  NE2 . HIS   B 1 138 ? -41.362 -41.862 13.173 1.00 28.30 ? 138 HIS   A NE2 1 
ATOM   3161 N  N   . GLU   B 1 139 ? -34.833 -42.797 11.354 1.00 18.47 ? 139 GLU   A N   1 
ATOM   3162 C  CA  . GLU   B 1 139 ? -33.660 -43.281 10.644 1.00 20.66 ? 139 GLU   A CA  1 
ATOM   3163 C  C   . GLU   B 1 139 ? -32.485 -43.457 11.613 1.00 19.26 ? 139 GLU   A C   1 
ATOM   3164 O  O   . GLU   B 1 139 ? -32.248 -42.622 12.496 1.00 17.95 ? 139 GLU   A O   1 
ATOM   3165 C  CB  . GLU   B 1 139 ? -33.275 -42.225 9.609  1.00 24.50 ? 139 GLU   A CB  1 
ATOM   3166 C  CG  . GLU   B 1 139 ? -34.406 -41.945 8.611  1.00 29.31 ? 139 GLU   A CG  1 
ATOM   3167 C  CD  . GLU   B 1 139 ? -34.636 -43.017 7.552  1.00 38.71 ? 139 GLU   A CD  1 
ATOM   3168 O  OE1 . GLU   B 1 139 ? -34.084 -44.163 7.671  1.00 37.08 ? 139 GLU   A OE1 1 
ATOM   3169 O  OE2 . GLU   B 1 139 ? -35.409 -42.713 6.591  1.00 47.08 ? 139 GLU   A OE2 1 
ATOM   3170 N  N   . PRO   B 1 140 ? -31.643 -44.503 11.450 1.00 20.34 ? 140 PRO   A N   1 
ATOM   3171 C  CA  . PRO   B 1 140 ? -30.501 -44.705 12.338 1.00 18.79 ? 140 PRO   A CA  1 
ATOM   3172 C  C   . PRO   B 1 140 ? -29.551 -43.525 12.465 1.00 18.80 ? 140 PRO   A C   1 
ATOM   3173 O  O   . PRO   B 1 140 ? -29.039 -43.284 13.559 1.00 19.64 ? 140 PRO   A O   1 
ATOM   3174 C  CB  . PRO   B 1 140 ? -29.773 -45.920 11.757 1.00 21.40 ? 140 PRO   A CB  1 
ATOM   3175 C  CG  . PRO   B 1 140 ? -30.936 -46.665 11.139 1.00 25.39 ? 140 PRO   A CG  1 
ATOM   3176 C  CD  . PRO   B 1 140 ? -31.770 -45.585 10.461 1.00 23.41 ? 140 PRO   A CD  1 
ATOM   3177 N  N   . ASP   B 1 141 ? -29.334 -42.793 11.377 1.00 17.04 ? 141 ASP   A N   1 
ATOM   3178 C  CA  . ASP   B 1 141 ? -28.438 -41.638 11.389 1.00 14.97 ? 141 ASP   A CA  1 
ATOM   3179 C  C   . ASP   B 1 141 ? -29.228 -40.324 11.442 1.00 16.13 ? 141 ASP   A C   1 
ATOM   3180 O  O   . ASP   B 1 141 ? -28.683 -39.254 11.071 1.00 15.06 ? 141 ASP   A O   1 
ATOM   3181 C  CB  . ASP   B 1 141 ? -27.559 -41.630 10.131 1.00 17.21 ? 141 ASP   A CB  1 
ATOM   3182 C  CG  . ASP   B 1 141 ? -28.320 -41.603 8.820  1.00 19.81 ? 141 ASP   A CG  1 
ATOM   3183 O  OD1 . ASP   B 1 141 ? -29.537 -41.846 8.847  1.00 20.07 ? 141 ASP   A OD1 1 
ATOM   3184 O  OD2 . ASP   B 1 141 ? -27.667 -41.448 7.741  1.00 23.64 ? 141 ASP   A OD2 1 
ATOM   3185 N  N   . GLY   B 1 142 ? -30.507 -40.396 11.867 1.00 12.53 ? 142 GLY   A N   1 
ATOM   3186 C  CA  . GLY   B 1 142 ? -31.368 -39.226 11.788 1.00 11.85 ? 142 GLY   A CA  1 
ATOM   3187 C  C   . GLY   B 1 142 ? -31.077 -38.141 12.823 1.00 11.97 ? 142 GLY   A C   1 
ATOM   3188 O  O   . GLY   B 1 142 ? -31.199 -36.958 12.515 1.00 13.38 ? 142 GLY   A O   1 
ATOM   3189 N  N   . LEU   B 1 143 ? -30.781 -38.521 14.079 1.00 13.41 ? 143 LEU   A N   1 
ATOM   3190 C  CA  . LEU   B 1 143 ? -30.749 -37.539 15.176 1.00 13.02 ? 143 LEU   A CA  1 
ATOM   3191 C  C   . LEU   B 1 143 ? -29.399 -37.547 15.907 1.00 12.38 ? 143 LEU   A C   1 
ATOM   3192 O  O   . LEU   B 1 143 ? -28.642 -38.521 15.891 1.00 13.78 ? 143 LEU   A O   1 
ATOM   3193 C  CB  . LEU   B 1 143 ? -31.831 -37.893 16.212 1.00 13.18 ? 143 LEU   A CB  1 
ATOM   3194 C  CG  . LEU   B 1 143 ? -33.279 -37.988 15.713 1.00 11.88 ? 143 LEU   A CG  1 
ATOM   3195 C  CD1 . LEU   B 1 143 ? -34.161 -38.211 16.940 1.00 11.22 ? 143 LEU   A CD1 1 
ATOM   3196 C  CD2 . LEU   B 1 143 ? -33.662 -36.659 14.986 1.00 12.96 ? 143 LEU   A CD2 1 
ATOM   3197 N  N   . ALA   B 1 144 ? -29.059 -36.394 16.496 1.00 11.53 ? 144 ALA   A N   1 
ATOM   3198 C  CA  . ALA   B 1 144 ? -27.899 -36.306 17.357 1.00 11.86 ? 144 ALA   A CA  1 
ATOM   3199 C  C   . ALA   B 1 144 ? -28.343 -35.540 18.599 1.00 12.48 ? 144 ALA   A C   1 
ATOM   3200 O  O   . ALA   B 1 144 ? -28.913 -34.444 18.473 1.00 13.36 ? 144 ALA   A O   1 
ATOM   3201 C  CB  . ALA   B 1 144 ? -26.734 -35.614 16.658 1.00 14.16 ? 144 ALA   A CB  1 
ATOM   3202 N  N   . VAL   B 1 145 ? -27.992 -36.066 19.776 1.00 11.45 ? 145 VAL   A N   1 
ATOM   3203 C  CA  . VAL   B 1 145 ? -28.382 -35.364 21.013 1.00 10.84 ? 145 VAL   A CA  1 
ATOM   3204 C  C   . VAL   B 1 145 ? -27.103 -35.122 21.816 1.00 12.35 ? 145 VAL   A C   1 
ATOM   3205 O  O   . VAL   B 1 145 ? -26.351 -36.086 22.083 1.00 12.57 ? 145 VAL   A O   1 
ATOM   3206 C  CB  . VAL   B 1 145 ? -29.447 -36.111 21.837 1.00 12.43 ? 145 VAL   A CB  1 
ATOM   3207 C  CG1 . VAL   B 1 145 ? -29.805 -35.313 23.124 1.00 11.17 ? 145 VAL   A CG1 1 
ATOM   3208 C  CG2 . VAL   B 1 145 ? -30.740 -36.307 20.988 1.00 14.67 ? 145 VAL   A CG2 1 
ATOM   3209 N  N   . LEU   B 1 146 ? -26.891 -33.855 22.221 1.00 11.94 ? 146 LEU   A N   1 
ATOM   3210 C  CA  . LEU   B 1 146 ? -25.778 -33.491 23.084 1.00 14.02 ? 146 LEU   A CA  1 
ATOM   3211 C  C   . LEU   B 1 146 ? -26.307 -33.455 24.509 1.00 13.98 ? 146 LEU   A C   1 
ATOM   3212 O  O   . LEU   B 1 146 ? -27.403 -32.919 24.769 1.00 14.84 ? 146 LEU   A O   1 
ATOM   3213 C  CB  . LEU   B 1 146 ? -25.377 -32.073 22.655 1.00 18.46 ? 146 LEU   A CB  1 
ATOM   3214 C  CG  . LEU   B 1 146 ? -23.943 -31.612 22.856 1.00 28.25 ? 146 LEU   A CG  1 
ATOM   3215 C  CD1 . LEU   B 1 146 ? -23.872 -30.093 22.900 1.00 29.94 ? 146 LEU   A CD1 1 
ATOM   3216 C  CD2 . LEU   B 1 146 ? -23.262 -32.260 24.030 1.00 36.71 ? 146 LEU   A CD2 1 
ATOM   3217 N  N   . GLY   B 1 147 ? -25.556 -34.103 25.413 1.00 12.70 ? 147 GLY   A N   1 
ATOM   3218 C  CA  . GLY   B 1 147 ? -25.958 -34.163 26.800 1.00 14.00 ? 147 GLY   A CA  1 
ATOM   3219 C  C   . GLY   B 1 147 ? -24.967 -33.406 27.670 1.00 13.25 ? 147 GLY   A C   1 
ATOM   3220 O  O   . GLY   B 1 147 ? -23.753 -33.540 27.464 1.00 13.61 ? 147 GLY   A O   1 
ATOM   3221 N  N   . VAL   B 1 148 ? -25.497 -32.609 28.609 1.00 13.10 ? 148 VAL   A N   1 
ATOM   3222 C  CA  . VAL   B 1 148 ? -24.685 -31.814 29.522 1.00 12.23 ? 148 VAL   A CA  1 
ATOM   3223 C  C   . VAL   B 1 148 ? -25.133 -32.148 30.941 1.00 13.47 ? 148 VAL   A C   1 
ATOM   3224 O  O   . VAL   B 1 148 ? -26.305 -31.948 31.292 1.00 13.31 ? 148 VAL   A O   1 
ATOM   3225 C  CB  . VAL   B 1 148 ? -24.787 -30.291 29.276 1.00 13.91 ? 148 VAL   A CB  1 
ATOM   3226 C  CG1 . VAL   B 1 148 ? -23.902 -29.530 30.254 1.00 15.95 ? 148 VAL   A CG1 1 
ATOM   3227 C  CG2 . VAL   B 1 148 ? -24.359 -29.960 27.852 1.00 14.88 ? 148 VAL   A CG2 1 
ATOM   3228 N  N   . PHE   B 1 149 ? -24.167 -32.540 31.796 1.00 12.20 ? 149 PHE   A N   1 
ATOM   3229 C  CA  . PHE   B 1 149 ? -24.539 -32.851 33.177 1.00 12.58 ? 149 PHE   A CA  1 
ATOM   3230 C  C   . PHE   B 1 149 ? -24.615 -31.579 34.002 1.00 14.12 ? 149 PHE   A C   1 
ATOM   3231 O  O   . PHE   B 1 149 ? -23.802 -30.655 33.818 1.00 12.91 ? 149 PHE   A O   1 
ATOM   3232 C  CB  . PHE   B 1 149 ? -23.505 -33.795 33.821 1.00 12.07 ? 149 PHE   A CB  1 
ATOM   3233 C  CG  . PHE   B 1 149 ? -23.435 -35.197 33.262 1.00 10.64 ? 149 PHE   A CG  1 
ATOM   3234 C  CD1 . PHE   B 1 149 ? -24.562 -36.016 33.299 1.00 12.07 ? 149 PHE   A CD1 1 
ATOM   3235 C  CD2 . PHE   B 1 149 ? -22.301 -35.689 32.628 1.00 13.35 ? 149 PHE   A CD2 1 
ATOM   3236 C  CE1 . PHE   B 1 149 ? -24.480 -37.313 32.771 1.00 12.86 ? 149 PHE   A CE1 1 
ATOM   3237 C  CE2 . PHE   B 1 149 ? -22.220 -36.984 32.132 1.00 13.18 ? 149 PHE   A CE2 1 
ATOM   3238 C  CZ  . PHE   B 1 149 ? -23.334 -37.787 32.192 1.00 13.49 ? 149 PHE   A CZ  1 
ATOM   3239 N  N   . LEU   B 1 150 ? -25.563 -31.542 34.970 1.00 13.40 ? 150 LEU   A N   1 
ATOM   3240 C  CA  . LEU   B 1 150 ? -25.603 -30.475 35.963 1.00 14.62 ? 150 LEU   A CA  1 
ATOM   3241 C  C   . LEU   B 1 150 ? -25.316 -31.021 37.357 1.00 15.33 ? 150 LEU   A C   1 
ATOM   3242 O  O   . LEU   B 1 150 ? -25.977 -31.964 37.803 1.00 15.87 ? 150 LEU   A O   1 
ATOM   3243 C  CB  . LEU   B 1 150 ? -26.956 -29.742 35.939 1.00 15.69 ? 150 LEU   A CB  1 
ATOM   3244 C  CG  . LEU   B 1 150 ? -27.275 -28.929 34.674 1.00 14.33 ? 150 LEU   A CG  1 
ATOM   3245 C  CD1 . LEU   B 1 150 ? -27.710 -29.913 33.548 1.00 14.73 ? 150 LEU   A CD1 1 
ATOM   3246 C  CD2 . LEU   B 1 150 ? -28.461 -28.028 34.965 1.00 16.80 ? 150 LEU   A CD2 1 
ATOM   3247 N  N   . GLN   B 1 151 ? -24.271 -30.475 38.014 1.00 15.10 ? 151 GLN   A N   1 
ATOM   3248 C  CA  . GLN   B 1 151 ? -23.917 -30.881 39.376 1.00 15.23 ? 151 GLN   A CA  1 
ATOM   3249 C  C   . GLN   B 1 151 ? -24.371 -29.808 40.351 1.00 15.38 ? 151 GLN   A C   1 
ATOM   3250 O  O   . GLN   B 1 151 ? -24.427 -28.636 39.986 1.00 16.08 ? 151 GLN   A O   1 
ATOM   3251 C  CB  . GLN   B 1 151 ? -22.410 -31.141 39.499 1.00 18.47 ? 151 GLN   A CB  1 
ATOM   3252 C  CG  . GLN   B 1 151 ? -21.597 -29.880 39.376 1.00 21.75 ? 151 GLN   A CG  1 
ATOM   3253 C  CD  . GLN   B 1 151 ? -20.110 -30.157 39.367 1.00 26.84 ? 151 GLN   A CD  1 
ATOM   3254 O  OE1 . GLN   B 1 151 ? -19.663 -31.300 39.500 1.00 24.04 ? 151 GLN   A OE1 1 
ATOM   3255 N  NE2 . GLN   B 1 151 ? -19.348 -29.096 39.161 1.00 30.67 ? 151 GLN   A NE2 1 
ATOM   3256 N  N   . ILE   B 1 152 ? -24.664 -30.208 41.589 1.00 15.95 ? 152 ILE   A N   1 
ATOM   3257 C  CA  . ILE   B 1 152 ? -25.027 -29.217 42.596 1.00 16.98 ? 152 ILE   A CA  1 
ATOM   3258 C  C   . ILE   B 1 152 ? -23.804 -28.349 42.886 1.00 18.39 ? 152 ILE   A C   1 
ATOM   3259 O  O   . ILE   B 1 152 ? -22.701 -28.829 43.128 1.00 19.09 ? 152 ILE   A O   1 
ATOM   3260 C  CB  . ILE   B 1 152 ? -25.590 -29.834 43.886 1.00 17.21 ? 152 ILE   A CB  1 
ATOM   3261 C  CG1 . ILE   B 1 152 ? -26.857 -30.655 43.625 1.00 17.61 ? 152 ILE   A CG1 1 
ATOM   3262 C  CG2 . ILE   B 1 152 ? -25.849 -28.689 44.898 1.00 19.62 ? 152 ILE   A CG2 1 
ATOM   3263 C  CD1 . ILE   B 1 152 ? -27.988 -29.830 43.018 1.00 20.29 ? 152 ILE   A CD1 1 
ATOM   3264 N  N   . GLY   B 1 153 ? -23.993 -27.036 42.805 1.00 20.83 ? 153 GLY   A N   1 
ATOM   3265 C  CA  . GLY   B 1 153 ? -22.947 -26.093 43.156 1.00 21.29 ? 153 GLY   A CA  1 
ATOM   3266 C  C   . GLY   B 1 153 ? -23.567 -24.722 43.392 1.00 22.91 ? 153 GLY   A C   1 
ATOM   3267 O  O   . GLY   B 1 153 ? -24.761 -24.587 43.670 1.00 21.04 ? 153 GLY   A O   1 
ATOM   3268 N  N   . GLU   B 1 154 ? -22.735 -23.689 43.277 1.00 22.52 ? 154 GLU   A N   1 
ATOM   3269 C  CA  . GLU   B 1 154 ? -23.286 -22.356 43.498 1.00 25.82 ? 154 GLU   A CA  1 
ATOM   3270 C  C   . GLU   B 1 154 ? -24.251 -22.033 42.350 1.00 21.32 ? 154 GLU   A C   1 
ATOM   3271 O  O   . GLU   B 1 154 ? -24.125 -22.573 41.239 1.00 19.96 ? 154 GLU   A O   1 
ATOM   3272 C  CB  . GLU   B 1 154 ? -22.135 -21.360 43.712 1.00 30.97 ? 154 GLU   A CB  1 
ATOM   3273 C  CG  . GLU   B 1 154 ? -21.636 -21.316 45.165 1.00 33.45 ? 154 GLU   A CG  1 
ATOM   3274 C  CD  . GLU   B 1 154 ? -20.165 -20.940 45.320 1.00 39.93 ? 154 GLU   A CD  1 
ATOM   3275 O  OE1 . GLU   B 1 154 ? -19.473 -20.861 44.264 1.00 38.79 ? 154 GLU   A OE1 1 
ATOM   3276 O  OE2 . GLU   B 1 154 ? -19.710 -20.692 46.494 1.00 35.07 ? 154 GLU   A OE2 1 
ATOM   3277 N  N   . PRO   B 1 155 ? -25.284 -21.181 42.544 1.00 20.40 ? 155 PRO   A N   1 
ATOM   3278 C  CA  . PRO   B 1 155 ? -26.247 -20.931 41.471 1.00 20.57 ? 155 PRO   A CA  1 
ATOM   3279 C  C   . PRO   B 1 155 ? -25.640 -20.375 40.183 1.00 21.55 ? 155 PRO   A C   1 
ATOM   3280 O  O   . PRO   B 1 155 ? -24.679 -19.573 40.187 1.00 23.12 ? 155 PRO   A O   1 
ATOM   3281 C  CB  . PRO   B 1 155 ? -27.295 -19.959 42.062 1.00 23.28 ? 155 PRO   A CB  1 
ATOM   3282 C  CG  . PRO   B 1 155 ? -26.618 -19.426 43.309 1.00 21.24 ? 155 PRO   A CG  1 
ATOM   3283 C  CD  . PRO   B 1 155 ? -25.572 -20.413 43.777 1.00 22.75 ? 155 PRO   A CD  1 
ATOM   3284 N  N   . ASN   B 1 156 ? -26.231 -20.836 39.072 1.00 18.45 ? 156 ASN   A N   1 
ATOM   3285 C  CA  . ASN   B 1 156 ? -25.738 -20.580 37.734 1.00 19.49 ? 156 ASN   A CA  1 
ATOM   3286 C  C   . ASN   B 1 156 ? -26.567 -19.457 37.117 1.00 19.00 ? 156 ASN   A C   1 
ATOM   3287 O  O   . ASN   B 1 156 ? -27.742 -19.663 36.817 1.00 19.38 ? 156 ASN   A O   1 
ATOM   3288 C  CB  . ASN   B 1 156 ? -25.868 -21.865 36.928 1.00 18.27 ? 156 ASN   A CB  1 
ATOM   3289 C  CG  . ASN   B 1 156 ? -25.181 -21.740 35.586 1.00 21.71 ? 156 ASN   A CG  1 
ATOM   3290 O  OD1 . ASN   B 1 156 ? -24.971 -20.627 35.080 1.00 21.93 ? 156 ASN   A OD1 1 
ATOM   3291 N  ND2 . ASN   B 1 156 ? -24.807 -22.876 35.053 1.00 16.83 ? 156 ASN   A ND2 1 
ATOM   3292 N  N   . SER   B 1 157 ? -25.938 -18.295 36.854 1.00 22.02 ? 157 SER   A N   1 
ATOM   3293 C  CA  . SER   B 1 157 ? -26.749 -17.159 36.422 1.00 24.62 ? 157 SER   A CA  1 
ATOM   3294 C  C   . SER   B 1 157 ? -27.210 -17.324 34.981 1.00 24.53 ? 157 SER   A C   1 
ATOM   3295 O  O   . SER   B 1 157 ? -28.151 -16.642 34.562 1.00 25.42 ? 157 SER   A O   1 
ATOM   3296 C  CB  . SER   B 1 157 ? -25.996 -15.855 36.572 1.00 29.09 ? 157 SER   A CB  1 
ATOM   3297 O  OG  . SER   B 1 157 ? -24.784 -15.958 35.839 1.00 35.61 ? 157 SER   A OG  1 
ATOM   3298 N  N   . GLN   B 1 158 ? -26.614 -18.273 34.250 1.00 22.80 ? 158 GLN   A N   1 
ATOM   3299 C  CA  . GLN   B 1 158 ? -27.007 -18.522 32.861 1.00 20.45 ? 158 GLN   A CA  1 
ATOM   3300 C  C   . GLN   B 1 158 ? -28.326 -19.280 32.788 1.00 22.48 ? 158 GLN   A C   1 
ATOM   3301 O  O   . GLN   B 1 158 ? -28.844 -19.487 31.682 1.00 22.61 ? 158 GLN   A O   1 
ATOM   3302 C  CB  . GLN   B 1 158 ? -25.917 -19.253 32.088 1.00 24.58 ? 158 GLN   A CB  1 
ATOM   3303 C  CG  . GLN   B 1 158 ? -24.596 -18.488 32.004 1.00 24.42 ? 158 GLN   A CG  1 
ATOM   3304 C  CD  . GLN   B 1 158 ? -24.822 -17.050 31.589 1.00 31.43 ? 158 GLN   A CD  1 
ATOM   3305 O  OE1 . GLN   B 1 158 ? -24.640 -16.143 32.404 1.00 39.56 ? 158 GLN   A OE1 1 
ATOM   3306 N  NE2 . GLN   B 1 158 ? -25.316 -16.840 30.376 1.00 25.67 ? 158 GLN   A NE2 1 
ATOM   3307 N  N   . LEU   B 1 159 ? -28.822 -19.758 33.948 1.00 19.74 ? 159 LEU   A N   1 
ATOM   3308 C  CA  . LEU   B 1 159 ? -30.102 -20.451 33.946 1.00 19.11 ? 159 LEU   A CA  1 
ATOM   3309 C  C   . LEU   B 1 159 ? -31.246 -19.483 34.225 1.00 19.12 ? 159 LEU   A C   1 
ATOM   3310 O  O   . LEU   B 1 159 ? -32.410 -19.883 34.127 1.00 19.66 ? 159 LEU   A O   1 
ATOM   3311 C  CB  . LEU   B 1 159 ? -30.089 -21.547 35.028 1.00 21.12 ? 159 LEU   A CB  1 
ATOM   3312 C  CG  . LEU   B 1 159 ? -29.268 -22.790 34.699 1.00 21.93 ? 159 LEU   A CG  1 
ATOM   3313 C  CD1 . LEU   B 1 159 ? -29.168 -23.675 35.930 1.00 22.18 ? 159 LEU   A CD1 1 
ATOM   3314 C  CD2 . LEU   B 1 159 ? -29.849 -23.552 33.507 1.00 21.54 ? 159 LEU   A CD2 1 
ATOM   3315 N  N   . GLN   B 1 160 ? -30.940 -18.231 34.604 1.00 19.25 ? 160 GLN   A N   1 
ATOM   3316 C  CA  . GLN   B 1 160 ? -32.022 -17.323 34.981 1.00 19.73 ? 160 GLN   A CA  1 
ATOM   3317 C  C   . GLN   B 1 160 ? -33.040 -17.131 33.850 1.00 18.90 ? 160 GLN   A C   1 
ATOM   3318 O  O   . GLN   B 1 160 ? -34.234 -17.039 34.103 1.00 18.22 ? 160 GLN   A O   1 
ATOM   3319 C  CB  . GLN   B 1 160 ? -31.474 -15.969 35.432 1.00 21.01 ? 160 GLN   A CB  1 
ATOM   3320 C  CG  . GLN   B 1 160 ? -32.539 -15.136 36.154 1.00 22.06 ? 160 GLN   A CG  1 
ATOM   3321 C  CD  . GLN   B 1 160 ? -32.265 -13.651 36.185 1.00 30.88 ? 160 GLN   A CD  1 
ATOM   3322 O  OE1 . GLN   B 1 160 ? -33.189 -12.831 36.254 1.00 32.41 ? 160 GLN   A OE1 1 
ATOM   3323 N  NE2 . GLN   B 1 160 ? -30.996 -13.293 36.118 1.00 28.15 ? 160 GLN   A NE2 1 
ATOM   3324 N  N   . LYS   B 1 161 ? -32.609 -17.073 32.588 1.00 20.11 ? 161 LYS   A N   1 
ATOM   3325 C  CA  . LYS   B 1 161 ? -33.558 -16.812 31.519 1.00 20.93 ? 161 LYS   A CA  1 
ATOM   3326 C  C   . LYS   B 1 161 ? -34.651 -17.883 31.508 1.00 19.01 ? 161 LYS   A C   1 
ATOM   3327 O  O   . LYS   B 1 161 ? -35.832 -17.573 31.310 1.00 20.68 ? 161 LYS   A O   1 
ATOM   3328 C  CB  . LYS   B 1 161 ? -32.864 -16.770 30.144 1.00 25.99 ? 161 LYS   A CB  1 
ATOM   3329 C  CG  . LYS   B 1 161 ? -33.685 -16.052 29.065 1.00 27.45 ? 161 LYS   A CG  1 
ATOM   3330 C  CD  . LYS   B 1 161 ? -33.319 -16.340 27.625 1.00 30.12 ? 161 LYS   A CD  1 
ATOM   3331 C  CE  . LYS   B 1 161 ? -34.368 -15.905 26.623 1.00 25.98 ? 161 LYS   A CE  1 
ATOM   3332 N  NZ  . LYS   B 1 161 ? -34.654 -14.429 26.697 1.00 24.77 ? 161 LYS   A NZ  1 
ATOM   3333 N  N   . ILE   B 1 162 ? -34.260 -19.146 31.767 1.00 15.80 ? 162 ILE   A N   1 
ATOM   3334 C  CA  . ILE   B 1 162 ? -35.212 -20.246 31.828 1.00 16.99 ? 162 ILE   A CA  1 
ATOM   3335 C  C   . ILE   B 1 162 ? -36.052 -20.141 33.103 1.00 17.10 ? 162 ILE   A C   1 
ATOM   3336 O  O   . ILE   B 1 162 ? -37.276 -20.284 33.053 1.00 16.70 ? 162 ILE   A O   1 
ATOM   3337 C  CB  . ILE   B 1 162 ? -34.519 -21.618 31.731 1.00 16.47 ? 162 ILE   A CB  1 
ATOM   3338 C  CG1 . ILE   B 1 162 ? -33.843 -21.754 30.357 1.00 17.62 ? 162 ILE   A CG1 1 
ATOM   3339 C  CG2 . ILE   B 1 162 ? -35.525 -22.745 31.912 1.00 17.22 ? 162 ILE   A CG2 1 
ATOM   3340 C  CD1 . ILE   B 1 162 ? -32.845 -22.921 30.325 1.00 17.03 ? 162 ILE   A CD1 1 
ATOM   3341 N  N   . THR   B 1 163 ? -35.407 -19.927 34.260 1.00 17.93 ? 163 THR   A N   1 
ATOM   3342 C  CA  . THR   B 1 163 ? -36.166 -20.078 35.502 1.00 16.68 ? 163 THR   A CA  1 
ATOM   3343 C  C   . THR   B 1 163 ? -37.188 -18.944 35.662 1.00 18.95 ? 163 THR   A C   1 
ATOM   3344 O  O   . THR   B 1 163 ? -38.282 -19.188 36.189 1.00 18.89 ? 163 THR   A O   1 
ATOM   3345 C  CB  . THR   B 1 163 ? -35.268 -20.168 36.758 1.00 17.18 ? 163 THR   A CB  1 
ATOM   3346 O  OG1 . THR   B 1 163 ? -34.419 -19.034 36.908 1.00 20.62 ? 163 THR   A OG1 1 
ATOM   3347 C  CG2 . THR   B 1 163 ? -34.414 -21.415 36.761 1.00 16.91 ? 163 THR   A CG2 1 
ATOM   3348 N  N   . ASP   B 1 164 ? -36.856 -17.749 35.136 1.00 18.32 ? 164 ASP   A N   1 
ATOM   3349 C  CA  . ASP   B 1 164 ? -37.799 -16.639 35.134 1.00 20.19 ? 164 ASP   A CA  1 
ATOM   3350 C  C   . ASP   B 1 164 ? -39.117 -16.978 34.418 1.00 21.70 ? 164 ASP   A C   1 
ATOM   3351 O  O   . ASP   B 1 164 ? -40.146 -16.366 34.729 1.00 23.34 ? 164 ASP   A O   1 
ATOM   3352 C  CB  . ASP   B 1 164 ? -37.187 -15.373 34.513 1.00 22.32 ? 164 ASP   A CB  1 
ATOM   3353 C  CG  . ASP   B 1 164 ? -36.379 -14.507 35.475 1.00 27.71 ? 164 ASP   A CG  1 
ATOM   3354 O  OD1 . ASP   B 1 164 ? -36.360 -14.821 36.713 1.00 29.81 ? 164 ASP   A OD1 1 
ATOM   3355 O  OD2 . ASP   B 1 164 ? -35.749 -13.525 34.983 1.00 32.01 ? 164 ASP   A OD2 1 
ATOM   3356 N  N   . THR   B 1 165 ? -39.126 -17.942 33.474 1.00 20.16 ? 165 THR   A N   1 
ATOM   3357 C  CA  . THR   B 1 165 ? -40.324 -18.257 32.693 1.00 19.56 ? 165 THR   A CA  1 
ATOM   3358 C  C   . THR   B 1 165 ? -41.197 -19.347 33.313 1.00 20.28 ? 165 THR   A C   1 
ATOM   3359 O  O   . THR   B 1 165 ? -42.316 -19.577 32.839 1.00 20.61 ? 165 THR   A O   1 
ATOM   3360 C  CB  . THR   B 1 165 ? -40.050 -18.747 31.257 1.00 21.73 ? 165 THR   A CB  1 
ATOM   3361 O  OG1 . THR   B 1 165 ? -39.478 -20.056 31.364 1.00 22.24 ? 165 THR   A OG1 1 
ATOM   3362 C  CG2 . THR   B 1 165 ? -39.153 -17.808 30.467 1.00 22.08 ? 165 THR   A CG2 1 
ATOM   3363 N  N   . LEU   B 1 166 ? -40.703 -20.050 34.350 1.00 18.99 ? 166 LEU   A N   1 
ATOM   3364 C  CA  . LEU   B 1 166 ? -41.369 -21.279 34.732 1.00 19.07 ? 166 LEU   A CA  1 
ATOM   3365 C  C   . LEU   B 1 166 ? -42.763 -21.013 35.301 1.00 19.69 ? 166 LEU   A C   1 
ATOM   3366 O  O   . LEU   B 1 166 ? -43.652 -21.839 35.122 1.00 20.20 ? 166 LEU   A O   1 
ATOM   3367 C  CB  . LEU   B 1 166 ? -40.497 -22.114 35.682 1.00 20.55 ? 166 LEU   A CB  1 
ATOM   3368 C  CG  . LEU   B 1 166 ? -39.151 -22.534 35.075 1.00 21.49 ? 166 LEU   A CG  1 
ATOM   3369 C  CD1 . LEU   B 1 166 ? -38.249 -23.102 36.178 1.00 21.47 ? 166 LEU   A CD1 1 
ATOM   3370 C  CD2 . LEU   B 1 166 ? -39.388 -23.605 33.999 1.00 23.94 ? 166 LEU   A CD2 1 
ATOM   3371 N  N   . ASP   B 1 167 ? -42.949 -19.876 35.998 1.00 22.39 ? 167 ASP   A N   1 
ATOM   3372 C  CA  . ASP   B 1 167 ? -44.289 -19.592 36.529 1.00 26.25 ? 167 ASP   A CA  1 
ATOM   3373 C  C   . ASP   B 1 167 ? -45.328 -19.491 35.400 1.00 26.39 ? 167 ASP   A C   1 
ATOM   3374 O  O   . ASP   B 1 167 ? -46.456 -19.993 35.505 1.00 26.70 ? 167 ASP   A O   1 
ATOM   3375 C  CB  . ASP   B 1 167 ? -44.259 -18.273 37.304 1.00 27.38 ? 167 ASP   A CB  1 
ATOM   3376 C  CG  . ASP   B 1 167 ? -43.826 -18.395 38.759 1.00 40.16 ? 167 ASP   A CG  1 
ATOM   3377 O  OD1 . ASP   B 1 167 ? -43.509 -19.532 39.199 1.00 37.11 ? 167 ASP   A OD1 1 
ATOM   3378 O  OD2 . ASP   B 1 167 ? -43.822 -17.344 39.453 1.00 41.83 ? 167 ASP   A OD2 1 
ATOM   3379 N  N   . SER   B 1 168 ? -44.938 -18.834 34.301 1.00 23.50 ? 168 SER   A N   1 
ATOM   3380 C  CA  . SER   B 1 168 ? -45.802 -18.635 33.148 1.00 22.49 ? 168 SER   A CA  1 
ATOM   3381 C  C   . SER   B 1 168 ? -46.074 -19.934 32.374 1.00 23.56 ? 168 SER   A C   1 
ATOM   3382 O  O   . SER   B 1 168 ? -46.965 -19.960 31.519 1.00 22.91 ? 168 SER   A O   1 
ATOM   3383 C  CB  . SER   B 1 168 ? -45.238 -17.536 32.271 1.00 25.23 ? 168 SER   A CB  1 
ATOM   3384 O  OG  . SER   B 1 168 ? -44.184 -18.048 31.465 1.00 29.37 ? 168 SER   A OG  1 
ATOM   3385 N  N   . ILE   B 1 169 ? -45.301 -21.011 32.602 1.00 18.37 ? 169 ILE   A N   1 
ATOM   3386 C  CA  . ILE   B 1 169 ? -45.563 -22.267 31.890 1.00 19.24 ? 169 ILE   A CA  1 
ATOM   3387 C  C   . ILE   B 1 169 ? -45.846 -23.410 32.884 1.00 19.66 ? 169 ILE   A C   1 
ATOM   3388 O  O   . ILE   B 1 169 ? -45.534 -24.585 32.648 1.00 17.20 ? 169 ILE   A O   1 
ATOM   3389 C  CB  . ILE   B 1 169 ? -44.447 -22.648 30.875 1.00 18.13 ? 169 ILE   A CB  1 
ATOM   3390 C  CG1 . ILE   B 1 169 ? -43.068 -22.732 31.533 1.00 18.15 ? 169 ILE   A CG1 1 
ATOM   3391 C  CG2 . ILE   B 1 169 ? -44.457 -21.739 29.644 1.00 18.65 ? 169 ILE   A CG2 1 
ATOM   3392 C  CD1 . ILE   B 1 169 ? -42.055 -23.560 30.716 1.00 20.50 ? 169 ILE   A CD1 1 
ATOM   3393 N  N   . LYS   B 1 170 ? -46.482 -23.071 34.013 1.00 18.38 ? 170 LYS   A N   1 
ATOM   3394 C  CA  . LYS   B 1 170 ? -46.588 -24.052 35.092 1.00 21.36 ? 170 LYS   A CA  1 
ATOM   3395 C  C   . LYS   B 1 170 ? -47.443 -25.249 34.656 1.00 20.05 ? 170 LYS   A C   1 
ATOM   3396 O  O   . LYS   B 1 170 ? -47.121 -26.407 34.934 1.00 17.91 ? 170 LYS   A O   1 
ATOM   3397 C  CB  . LYS   B 1 170 ? -47.227 -23.396 36.321 1.00 26.46 ? 170 LYS   A CB  1 
ATOM   3398 C  CG  . LYS   B 1 170 ? -47.456 -24.333 37.500 1.00 29.33 ? 170 LYS   A CG  1 
ATOM   3399 C  CD  . LYS   B 1 170 ? -47.712 -23.659 38.837 1.00 38.13 ? 170 LYS   A CD  1 
ATOM   3400 C  CE  . LYS   B 1 170 ? -47.585 -24.616 40.013 1.00 44.88 ? 170 LYS   A CE  1 
ATOM   3401 N  NZ  . LYS   B 1 170 ? -46.226 -24.634 40.628 1.00 41.55 ? 170 LYS   A NZ  1 
ATOM   3402 N  N   . GLU   B 1 171 ? -48.552 -25.004 33.931 1.00 21.60 ? 171 GLU   A N   1 
ATOM   3403 C  CA  . GLU   B 1 171 ? -49.421 -26.111 33.526 1.00 20.64 ? 171 GLU   A CA  1 
ATOM   3404 C  C   . GLU   B 1 171 ? -49.060 -26.671 32.141 1.00 20.30 ? 171 GLU   A C   1 
ATOM   3405 O  O   . GLU   B 1 171 ? -48.578 -25.961 31.252 1.00 18.20 ? 171 GLU   A O   1 
ATOM   3406 C  CB  . GLU   B 1 171 ? -50.879 -25.619 33.498 1.00 24.83 ? 171 GLU   A CB  1 
ATOM   3407 C  CG  . GLU   B 1 171 ? -51.327 -25.005 34.819 1.00 29.40 ? 171 GLU   A CG  1 
ATOM   3408 C  CD  . GLU   B 1 171 ? -51.023 -23.539 35.143 1.00 35.19 ? 171 GLU   A CD  1 
ATOM   3409 O  OE1 . GLU   B 1 171 ? -51.236 -23.147 36.310 1.00 40.18 ? 171 GLU   A OE1 1 
ATOM   3410 O  OE2 . GLU   B 1 171 ? -50.523 -22.774 34.266 1.00 33.16 ? 171 GLU   A OE2 1 
ATOM   3411 N  N   . LYS   B 1 172 ? -49.376 -27.937 31.912 1.00 20.35 ? 172 LYS   A N   1 
ATOM   3412 C  CA  . LYS   B 1 172 ? -49.038 -28.560 30.650 1.00 19.71 ? 172 LYS   A CA  1 
ATOM   3413 C  C   . LYS   B 1 172 ? -49.748 -27.859 29.489 1.00 22.66 ? 172 LYS   A C   1 
ATOM   3414 O  O   . LYS   B 1 172 ? -50.930 -27.533 29.597 1.00 22.28 ? 172 LYS   A O   1 
ATOM   3415 C  CB  . LYS   B 1 172 ? -49.488 -30.017 30.692 1.00 19.54 ? 172 LYS   A CB  1 
ATOM   3416 C  CG  . LYS   B 1 172 ? -49.409 -30.728 29.357 1.00 20.19 ? 172 LYS   A CG  1 
ATOM   3417 C  CD  . LYS   B 1 172 ? -49.950 -32.142 29.500 1.00 23.36 ? 172 LYS   A CD  1 
ATOM   3418 C  CE  . LYS   B 1 172 ? -49.569 -33.019 28.330 1.00 26.94 ? 172 LYS   A CE  1 
ATOM   3419 N  NZ  . LYS   B 1 172 ? -50.054 -34.392 28.539 1.00 28.80 ? 172 LYS   A NZ  1 
ATOM   3420 N  N   . GLY   B 1 173 ? -49.024 -27.634 28.381 1.00 21.61 ? 173 GLY   A N   1 
ATOM   3421 C  CA  . GLY   B 1 173 ? -49.567 -26.946 27.216 1.00 21.42 ? 173 GLY   A CA  1 
ATOM   3422 C  C   . GLY   B 1 173 ? -49.265 -25.444 27.164 1.00 20.87 ? 173 GLY   A C   1 
ATOM   3423 O  O   . GLY   B 1 173 ? -49.419 -24.809 26.110 1.00 23.74 ? 173 GLY   A O   1 
ATOM   3424 N  N   . LYS   B 1 174 ? -48.876 -24.848 28.293 1.00 16.45 ? 174 LYS   A N   1 
ATOM   3425 C  CA  . LYS   B 1 174 ? -48.632 -23.422 28.302 1.00 17.46 ? 174 LYS   A CA  1 
ATOM   3426 C  C   . LYS   B 1 174 ? -47.319 -23.132 27.560 1.00 17.30 ? 174 LYS   A C   1 
ATOM   3427 O  O   . LYS   B 1 174 ? -46.402 -23.926 27.662 1.00 17.83 ? 174 LYS   A O   1 
ATOM   3428 C  CB  . LYS   B 1 174 ? -48.549 -22.939 29.739 1.00 20.06 ? 174 LYS   A CB  1 
ATOM   3429 C  CG  . LYS   B 1 174 ? -49.900 -22.933 30.450 1.00 26.04 ? 174 LYS   A CG  1 
ATOM   3430 C  CD  . LYS   B 1 174 ? -50.276 -21.495 30.746 1.00 34.69 ? 174 LYS   A CD  1 
ATOM   3431 C  CE  . LYS   B 1 174 ? -51.477 -21.316 31.657 1.00 38.61 ? 174 LYS   A CE  1 
ATOM   3432 N  NZ  . LYS   B 1 174 ? -52.663 -21.833 30.951 1.00 41.24 ? 174 LYS   A NZ  1 
ATOM   3433 N  N   . GLN   B 1 175 ? -47.253 -21.971 26.895 1.00 17.78 ? 175 GLN   A N   1 
ATOM   3434 C  CA  . GLN   B 1 175 ? -46.030 -21.541 26.232 1.00 17.85 ? 175 GLN   A CA  1 
ATOM   3435 C  C   . GLN   B 1 175 ? -45.844 -20.051 26.389 1.00 18.83 ? 175 GLN   A C   1 
ATOM   3436 O  O   . GLN   B 1 175 ? -46.796 -19.315 26.659 1.00 21.79 ? 175 GLN   A O   1 
ATOM   3437 C  CB  . GLN   B 1 175 ? -46.054 -21.916 24.759 1.00 19.11 ? 175 GLN   A CB  1 
ATOM   3438 C  CG  . GLN   B 1 175 ? -46.933 -21.077 23.826 1.00 20.92 ? 175 GLN   A CG  1 
ATOM   3439 C  CD  . GLN   B 1 175 ? -46.893 -21.513 22.371 1.00 21.21 ? 175 GLN   A CD  1 
ATOM   3440 O  OE1 . GLN   B 1 175 ? -46.641 -20.695 21.448 1.00 22.72 ? 175 GLN   A OE1 1 
ATOM   3441 N  NE2 . GLN   B 1 175 ? -47.157 -22.784 22.111 1.00 20.66 ? 175 GLN   A NE2 1 
ATOM   3442 N  N   . THR   B 1 176 ? -44.611 -19.607 26.173 1.00 17.55 ? 176 THR   A N   1 
ATOM   3443 C  CA  . THR   B 1 176 ? -44.314 -18.193 26.192 1.00 19.70 ? 176 THR   A CA  1 
ATOM   3444 C  C   . THR   B 1 176 ? -43.164 -17.909 25.230 1.00 19.11 ? 176 THR   A C   1 
ATOM   3445 O  O   . THR   B 1 176 ? -42.347 -18.781 24.931 1.00 18.22 ? 176 THR   A O   1 
ATOM   3446 C  CB  . THR   B 1 176 ? -44.106 -17.701 27.635 1.00 25.89 ? 176 THR   A CB  1 
ATOM   3447 O  OG1 . THR   B 1 176 ? -44.252 -16.273 27.671 1.00 29.56 ? 176 THR   A OG1 1 
ATOM   3448 C  CG2 . THR   B 1 176 ? -42.740 -18.027 28.192 1.00 22.93 ? 176 THR   A CG2 1 
ATOM   3449 N  N   . ARG   B 1 177 ? -43.079 -16.653 24.781 1.00 18.12 ? 177 ARG   A N   1 
ATOM   3450 C  CA  . ARG   B 1 177 ? -42.029 -16.178 23.918 1.00 16.48 ? 177 ARG   A CA  1 
ATOM   3451 C  C   . ARG   B 1 177 ? -40.674 -16.458 24.565 1.00 16.73 ? 177 ARG   A C   1 
ATOM   3452 O  O   . ARG   B 1 177 ? -40.490 -16.161 25.741 1.00 18.49 ? 177 ARG   A O   1 
ATOM   3453 C  CB  . ARG   B 1 177 ? -42.169 -14.646 23.800 1.00 21.16 ? 177 ARG   A CB  1 
ATOM   3454 C  CG  . ARG   B 1 177 ? -41.279 -14.036 22.732 1.00 25.27 ? 177 ARG   A CG  1 
ATOM   3455 C  CD  . ARG   B 1 177 ? -41.390 -12.508 22.649 1.00 29.26 ? 177 ARG   A CD  1 
ATOM   3456 N  NE  . ARG   B 1 177 ? -40.616 -12.225 21.438 1.00 33.72 ? 177 ARG   A NE  1 
ATOM   3457 C  CZ  . ARG   B 1 177 ? -40.042 -11.065 21.112 1.00 43.42 ? 177 ARG   A CZ  1 
ATOM   3458 N  NH1 . ARG   B 1 177 ? -40.204 -9.999  21.884 1.00 41.79 ? 177 ARG   A NH1 1 
ATOM   3459 N  NH2 . ARG   B 1 177 ? -39.356 -10.974 19.976 1.00 42.04 ? 177 ARG   A NH2 1 
ATOM   3460 N  N   . PHE   B 1 178 ? -39.708 -16.935 23.775 1.00 15.93 ? 178 PHE   A N   1 
ATOM   3461 C  CA  . PHE   B 1 178 ? -38.400 -17.183 24.383 1.00 15.65 ? 178 PHE   A CA  1 
ATOM   3462 C  C   . PHE   B 1 178 ? -37.343 -16.950 23.313 1.00 19.53 ? 178 PHE   A C   1 
ATOM   3463 O  O   . PHE   B 1 178 ? -37.129 -17.835 22.498 1.00 19.19 ? 178 PHE   A O   1 
ATOM   3464 C  CB  . PHE   B 1 178 ? -38.354 -18.646 24.877 1.00 15.22 ? 178 PHE   A CB  1 
ATOM   3465 C  CG  . PHE   B 1 178 ? -37.214 -18.919 25.839 1.00 15.45 ? 178 PHE   A CG  1 
ATOM   3466 C  CD1 . PHE   B 1 178 ? -37.319 -18.567 27.175 1.00 17.03 ? 178 PHE   A CD1 1 
ATOM   3467 C  CD2 . PHE   B 1 178 ? -36.050 -19.570 25.411 1.00 16.79 ? 178 PHE   A CD2 1 
ATOM   3468 C  CE1 . PHE   B 1 178 ? -36.280 -18.852 28.054 1.00 17.39 ? 178 PHE   A CE1 1 
ATOM   3469 C  CE2 . PHE   B 1 178 ? -35.018 -19.846 26.292 1.00 15.96 ? 178 PHE   A CE2 1 
ATOM   3470 C  CZ  . PHE   B 1 178 ? -35.138 -19.486 27.609 1.00 16.97 ? 178 PHE   A CZ  1 
ATOM   3471 N  N   . THR   B 1 179 ? -36.769 -15.746 23.263 1.00 19.08 ? 179 THR   A N   1 
ATOM   3472 C  CA  . THR   B 1 179 ? -35.840 -15.447 22.193 1.00 21.98 ? 179 THR   A CA  1 
ATOM   3473 C  C   . THR   B 1 179 ? -34.522 -14.885 22.738 1.00 18.23 ? 179 THR   A C   1 
ATOM   3474 O  O   . THR   B 1 179 ? -34.407 -14.558 23.906 1.00 23.76 ? 179 THR   A O   1 
ATOM   3475 C  CB  . THR   B 1 179 ? -36.528 -14.605 21.124 1.00 29.61 ? 179 THR   A CB  1 
ATOM   3476 O  OG1 . THR   B 1 179 ? -35.584 -14.677 20.044 1.00 45.05 ? 179 THR   A OG1 1 
ATOM   3477 C  CG2 . THR   B 1 179 ? -36.834 -13.218 21.646 1.00 27.11 ? 179 THR   A CG2 1 
ATOM   3478 N  N   . ASN   B 1 180 ? -33.502 -14.792 21.865 1.00 18.07 ? 180 ASN   A N   1 
ATOM   3479 C  CA  . ASN   B 1 180 ? -32.226 -14.244 22.299 1.00 19.59 ? 180 ASN   A CA  1 
ATOM   3480 C  C   . ASN   B 1 180 ? -31.578 -15.114 23.386 1.00 20.00 ? 180 ASN   A C   1 
ATOM   3481 O  O   . ASN   B 1 180 ? -31.135 -14.619 24.424 1.00 21.87 ? 180 ASN   A O   1 
ATOM   3482 C  CB  . ASN   B 1 180 ? -32.344 -12.758 22.667 1.00 20.81 ? 180 ASN   A CB  1 
ATOM   3483 C  CG  . ASN   B 1 180 ? -30.981 -12.110 22.563 1.00 28.27 ? 180 ASN   A CG  1 
ATOM   3484 O  OD1 . ASN   B 1 180 ? -30.202 -12.446 21.666 1.00 34.12 ? 180 ASN   A OD1 1 
ATOM   3485 N  ND2 . ASN   B 1 180 ? -30.694 -11.161 23.442 1.00 30.19 ? 180 ASN   A ND2 1 
ATOM   3486 N  N   . PHE   B 1 181 ? -31.526 -16.439 23.158 1.00 19.38 ? 181 PHE   A N   1 
ATOM   3487 C  CA  . PHE   B 1 181 ? -31.090 -17.374 24.199 1.00 17.14 ? 181 PHE   A CA  1 
ATOM   3488 C  C   . PHE   B 1 181 ? -29.643 -17.804 23.963 1.00 18.87 ? 181 PHE   A C   1 
ATOM   3489 O  O   . PHE   B 1 181 ? -29.315 -18.379 22.913 1.00 19.33 ? 181 PHE   A O   1 
ATOM   3490 C  CB  . PHE   B 1 181 ? -32.035 -18.574 24.142 1.00 16.98 ? 181 PHE   A CB  1 
ATOM   3491 C  CG  . PHE   B 1 181 ? -31.729 -19.791 24.985 1.00 17.10 ? 181 PHE   A CG  1 
ATOM   3492 C  CD1 . PHE   B 1 181 ? -31.252 -19.633 26.275 1.00 15.68 ? 181 PHE   A CD1 1 
ATOM   3493 C  CD2 . PHE   B 1 181 ? -31.983 -21.074 24.497 1.00 16.12 ? 181 PHE   A CD2 1 
ATOM   3494 C  CE1 . PHE   B 1 181 ? -31.039 -20.732 27.109 1.00 17.57 ? 181 PHE   A CE1 1 
ATOM   3495 C  CE2 . PHE   B 1 181 ? -31.728 -22.158 25.314 1.00 16.14 ? 181 PHE   A CE2 1 
ATOM   3496 C  CZ  . PHE   B 1 181 ? -31.264 -21.987 26.606 1.00 18.16 ? 181 PHE   A CZ  1 
ATOM   3497 N  N   . ASP   B 1 182 ? -28.800 -17.541 24.980 1.00 17.31 ? 182 ASP   A N   1 
ATOM   3498 C  CA  . ASP   B 1 182 ? -27.376 -17.878 24.925 1.00 18.46 ? 182 ASP   A CA  1 
ATOM   3499 C  C   . ASP   B 1 182 ? -27.193 -19.360 25.302 1.00 15.68 ? 182 ASP   A C   1 
ATOM   3500 O  O   . ASP   B 1 182 ? -26.806 -19.655 26.418 1.00 19.11 ? 182 ASP   A O   1 
ATOM   3501 C  CB  . ASP   B 1 182 ? -26.604 -16.944 25.850 1.00 19.88 ? 182 ASP   A CB  1 
ATOM   3502 C  CG  . ASP   B 1 182 ? -25.090 -17.055 25.771 1.00 21.60 ? 182 ASP   A CG  1 
ATOM   3503 O  OD1 . ASP   B 1 182 ? -24.560 -17.927 25.001 1.00 20.23 ? 182 ASP   A OD1 1 
ATOM   3504 O  OD2 . ASP   B 1 182 ? -24.437 -16.291 26.492 1.00 22.11 ? 182 ASP   A OD2 1 
ATOM   3505 N  N   . LEU   B 1 183 ? -27.522 -20.271 24.371 1.00 16.68 ? 183 LEU   A N   1 
ATOM   3506 C  CA  . LEU   B 1 183 ? -27.423 -21.708 24.675 1.00 15.27 ? 183 LEU   A CA  1 
ATOM   3507 C  C   . LEU   B 1 183 ? -25.958 -22.122 24.835 1.00 17.20 ? 183 LEU   A C   1 
ATOM   3508 O  O   . LEU   B 1 183 ? -25.633 -22.965 25.690 1.00 15.50 ? 183 LEU   A O   1 
ATOM   3509 C  CB  . LEU   B 1 183 ? -28.066 -22.494 23.523 1.00 15.44 ? 183 LEU   A CB  1 
ATOM   3510 C  CG  . LEU   B 1 183 ? -28.036 -24.023 23.667 1.00 14.08 ? 183 LEU   A CG  1 
ATOM   3511 C  CD1 . LEU   B 1 183 ? -28.657 -24.551 24.980 1.00 15.67 ? 183 LEU   A CD1 1 
ATOM   3512 C  CD2 . LEU   B 1 183 ? -28.796 -24.626 22.499 1.00 16.46 ? 183 LEU   A CD2 1 
ATOM   3513 N  N   . LEU   B 1 184 ? -25.033 -21.435 24.130 1.00 17.36 ? 184 LEU   A N   1 
ATOM   3514 C  CA  . LEU   B 1 184 ? -23.645 -21.859 24.292 1.00 16.62 ? 184 LEU   A CA  1 
ATOM   3515 C  C   . LEU   B 1 184 ? -23.170 -21.684 25.727 1.00 16.96 ? 184 LEU   A C   1 
ATOM   3516 O  O   . LEU   B 1 184 ? -22.206 -22.360 26.137 1.00 16.86 ? 184 LEU   A O   1 
ATOM   3517 C  CB  . LEU   B 1 184 ? -22.724 -21.081 23.334 1.00 16.64 ? 184 LEU   A CB  1 
ATOM   3518 C  CG  . LEU   B 1 184 ? -22.859 -21.462 21.857 1.00 15.95 ? 184 LEU   A CG  1 
ATOM   3519 C  CD1 . LEU   B 1 184 ? -21.985 -20.552 21.015 1.00 18.04 ? 184 LEU   A CD1 1 
ATOM   3520 C  CD2 . LEU   B 1 184 ? -22.342 -22.892 21.668 1.00 18.87 ? 184 LEU   A CD2 1 
ATOM   3521 N  N   . SER   B 1 185 ? -23.795 -20.753 26.473 1.00 17.49 ? 185 SER   A N   1 
ATOM   3522 C  CA  . SER   B 1 185 ? -23.350 -20.444 27.825 1.00 18.12 ? 185 SER   A CA  1 
ATOM   3523 C  C   . SER   B 1 185 ? -23.710 -21.543 28.825 1.00 18.58 ? 185 SER   A C   1 
ATOM   3524 O  O   . SER   B 1 185 ? -23.236 -21.509 29.971 1.00 20.15 ? 185 SER   A O   1 
ATOM   3525 C  CB  . SER   B 1 185 ? -23.859 -19.128 28.312 1.00 17.72 ? 185 SER   A CB  1 
ATOM   3526 O  OG  . SER   B 1 185 ? -25.254 -19.222 28.561 1.00 22.20 ? 185 SER   A OG  1 
ATOM   3527 N  N   . LEU   B 1 186 ? -24.511 -22.526 28.373 1.00 17.52 ? 186 LEU   A N   1 
ATOM   3528 C  CA  . LEU   B 1 186 ? -24.873 -23.671 29.209 1.00 17.39 ? 186 LEU   A CA  1 
ATOM   3529 C  C   . LEU   B 1 186 ? -24.009 -24.877 28.855 1.00 19.23 ? 186 LEU   A C   1 
ATOM   3530 O  O   . LEU   B 1 186 ? -24.306 -26.015 29.271 1.00 20.82 ? 186 LEU   A O   1 
ATOM   3531 C  CB  . LEU   B 1 186 ? -26.362 -24.002 29.036 1.00 16.05 ? 186 LEU   A CB  1 
ATOM   3532 C  CG  . LEU   B 1 186 ? -27.289 -22.923 29.599 1.00 17.46 ? 186 LEU   A CG  1 
ATOM   3533 C  CD1 . LEU   B 1 186 ? -28.722 -23.364 29.362 1.00 17.94 ? 186 LEU   A CD1 1 
ATOM   3534 C  CD2 . LEU   B 1 186 ? -27.009 -22.660 31.083 1.00 21.51 ? 186 LEU   A CD2 1 
ATOM   3535 N  N   . LEU   B 1 187 ? -23.002 -24.666 27.990 1.00 16.71 ? 187 LEU   A N   1 
ATOM   3536 C  CA  . LEU   B 1 187 ? -22.027 -25.725 27.776 1.00 17.46 ? 187 LEU   A CA  1 
ATOM   3537 C  C   . LEU   B 1 187 ? -20.818 -25.459 28.670 1.00 17.61 ? 187 LEU   A C   1 
ATOM   3538 O  O   . LEU   B 1 187 ? -20.501 -24.288 28.968 1.00 17.11 ? 187 LEU   A O   1 
ATOM   3539 C  CB  . LEU   B 1 187 ? -21.557 -25.738 26.313 1.00 15.76 ? 187 LEU   A CB  1 
ATOM   3540 C  CG  . LEU   B 1 187 ? -22.618 -25.873 25.237 1.00 22.27 ? 187 LEU   A CG  1 
ATOM   3541 C  CD1 . LEU   B 1 187 ? -21.963 -26.025 23.841 1.00 20.07 ? 187 LEU   A CD1 1 
ATOM   3542 C  CD2 . LEU   B 1 187 ? -23.497 -27.081 25.521 1.00 20.59 ? 187 LEU   A CD2 1 
ATOM   3543 N  N   . PRO   B 1 188 ? -20.151 -26.544 29.128 1.00 14.63 ? 188 PRO   A N   1 
ATOM   3544 C  CA  . PRO   B 1 188 ? -18.917 -26.412 29.897 1.00 16.10 ? 188 PRO   A CA  1 
ATOM   3545 C  C   . PRO   B 1 188 ? -17.811 -25.944 28.959 1.00 16.95 ? 188 PRO   A C   1 
ATOM   3546 O  O   . PRO   B 1 188 ? -17.965 -25.974 27.751 1.00 16.66 ? 188 PRO   A O   1 
ATOM   3547 C  CB  . PRO   B 1 188 ? -18.679 -27.855 30.358 1.00 14.46 ? 188 PRO   A CB  1 
ATOM   3548 C  CG  . PRO   B 1 188 ? -19.207 -28.679 29.247 1.00 14.09 ? 188 PRO   A CG  1 
ATOM   3549 C  CD  . PRO   B 1 188 ? -20.504 -27.954 28.890 1.00 14.11 ? 188 PRO   A CD  1 
ATOM   3550 N  N   . PRO   B 1 189 ? -16.690 -25.429 29.531 1.00 17.51 ? 189 PRO   A N   1 
ATOM   3551 C  CA  . PRO   B 1 189 ? -15.553 -24.920 28.742 1.00 17.80 ? 189 PRO   A CA  1 
ATOM   3552 C  C   . PRO   B 1 189 ? -14.899 -25.940 27.841 1.00 17.27 ? 189 PRO   A C   1 
ATOM   3553 O  O   . PRO   B 1 189 ? -14.554 -25.603 26.723 1.00 15.72 ? 189 PRO   A O   1 
ATOM   3554 C  CB  . PRO   B 1 189 ? -14.586 -24.333 29.765 1.00 20.01 ? 189 PRO   A CB  1 
ATOM   3555 C  CG  . PRO   B 1 189 ? -15.425 -24.136 30.998 1.00 21.10 ? 189 PRO   A CG  1 
ATOM   3556 C  CD  . PRO   B 1 189 ? -16.592 -25.123 30.958 1.00 18.27 ? 189 PRO   A CD  1 
ATOM   3557 N  N   . SER   B 1 190 ? -14.828 -27.199 28.290 1.00 14.41 ? 190 SER   A N   1 
ATOM   3558 C  CA  . SER   B 1 190 ? -14.302 -28.269 27.456 1.00 15.31 ? 190 SER   A CA  1 
ATOM   3559 C  C   . SER   B 1 190 ? -15.443 -29.000 26.772 1.00 15.16 ? 190 SER   A C   1 
ATOM   3560 O  O   . SER   B 1 190 ? -16.409 -29.329 27.467 1.00 16.12 ? 190 SER   A O   1 
ATOM   3561 C  CB  . SER   B 1 190 ? -13.473 -29.216 28.315 1.00 17.09 ? 190 SER   A CB  1 
ATOM   3562 O  OG  . SER   B 1 190 ? -13.060 -30.319 27.526 1.00 19.66 ? 190 SER   A OG  1 
ATOM   3563 N  N   . TRP   B 1 191 ? -15.267 -29.356 25.494 1.00 15.97 ? 191 TRP   A N   1 
ATOM   3564 C  CA  . TRP   B 1 191 ? -16.262 -30.174 24.799 1.00 15.00 ? 191 TRP   A CA  1 
ATOM   3565 C  C   . TRP   B 1 191 ? -15.778 -31.606 24.602 1.00 15.74 ? 191 TRP   A C   1 
ATOM   3566 O  O   . TRP   B 1 191 ? -16.207 -32.266 23.666 1.00 17.01 ? 191 TRP   A O   1 
ATOM   3567 C  CB  . TRP   B 1 191 ? -16.643 -29.536 23.457 1.00 14.61 ? 191 TRP   A CB  1 
ATOM   3568 C  CG  . TRP   B 1 191 ? -17.192 -28.150 23.583 1.00 15.21 ? 191 TRP   A CG  1 
ATOM   3569 C  CD1 . TRP   B 1 191 ? -17.653 -27.486 24.704 1.00 15.91 ? 191 TRP   A CD1 1 
ATOM   3570 C  CD2 . TRP   B 1 191 ? -17.470 -27.286 22.466 1.00 14.87 ? 191 TRP   A CD2 1 
ATOM   3571 N  NE1 . TRP   B 1 191 ? -18.135 -26.236 24.327 1.00 16.72 ? 191 TRP   A NE1 1 
ATOM   3572 C  CE2 . TRP   B 1 191 ? -18.073 -26.108 22.963 1.00 15.88 ? 191 TRP   A CE2 1 
ATOM   3573 C  CE3 . TRP   B 1 191 ? -17.239 -27.405 21.080 1.00 16.03 ? 191 TRP   A CE3 1 
ATOM   3574 C  CZ2 . TRP   B 1 191 ? -18.354 -25.023 22.114 1.00 15.00 ? 191 TRP   A CZ2 1 
ATOM   3575 C  CZ3 . TRP   B 1 191 ? -17.551 -26.345 20.255 1.00 16.46 ? 191 TRP   A CZ3 1 
ATOM   3576 C  CH2 . TRP   B 1 191 ? -18.144 -25.188 20.768 1.00 15.76 ? 191 TRP   A CH2 1 
ATOM   3577 N  N   . ASP   B 1 192 ? -14.881 -32.076 25.476 1.00 16.90 ? 192 ASP   A N   1 
ATOM   3578 C  CA  . ASP   B 1 192 ? -14.491 -33.481 25.436 1.00 17.94 ? 192 ASP   A CA  1 
ATOM   3579 C  C   . ASP   B 1 192 ? -15.745 -34.304 25.702 1.00 16.40 ? 192 ASP   A C   1 
ATOM   3580 O  O   . ASP   B 1 192 ? -16.572 -33.896 26.538 1.00 14.91 ? 192 ASP   A O   1 
ATOM   3581 C  CB  . ASP   B 1 192 ? -13.430 -33.744 26.501 1.00 21.72 ? 192 ASP   A CB  1 
ATOM   3582 C  CG  . ASP   B 1 192 ? -12.103 -33.052 26.203 1.00 33.41 ? 192 ASP   A CG  1 
ATOM   3583 O  OD1 . ASP   B 1 192 ? -11.852 -32.705 25.007 1.00 42.17 ? 192 ASP   A OD1 1 
ATOM   3584 O  OD2 . ASP   B 1 192 ? -11.309 -32.884 27.165 1.00 42.78 ? 192 ASP   A OD2 1 
ATOM   3585 N  N   . TYR   B 1 193 ? -15.868 -35.428 24.975 1.00 15.51 ? 193 TYR   A N   1 
ATOM   3586 C  CA  . TYR   B 1 193 ? -17.148 -36.137 25.013 1.00 14.17 ? 193 TYR   A CA  1 
ATOM   3587 C  C   . TYR   B 1 193 ? -16.972 -37.648 24.892 1.00 14.57 ? 193 TYR   A C   1 
ATOM   3588 O  O   . TYR   B 1 193 ? -15.938 -38.177 24.418 1.00 14.28 ? 193 TYR   A O   1 
ATOM   3589 C  CB  . TYR   B 1 193 ? -18.054 -35.638 23.857 1.00 13.93 ? 193 TYR   A CB  1 
ATOM   3590 C  CG  . TYR   B 1 193 ? -17.558 -35.975 22.474 1.00 13.27 ? 193 TYR   A CG  1 
ATOM   3591 C  CD1 . TYR   B 1 193 ? -17.794 -37.222 21.878 1.00 15.38 ? 193 TYR   A CD1 1 
ATOM   3592 C  CD2 . TYR   B 1 193 ? -16.748 -35.076 21.779 1.00 16.57 ? 193 TYR   A CD2 1 
ATOM   3593 C  CE1 . TYR   B 1 193 ? -17.239 -37.531 20.634 1.00 16.45 ? 193 TYR   A CE1 1 
ATOM   3594 C  CE2 . TYR   B 1 193 ? -16.218 -35.366 20.525 1.00 15.24 ? 193 TYR   A CE2 1 
ATOM   3595 C  CZ  . TYR   B 1 193 ? -16.461 -36.595 19.954 1.00 18.90 ? 193 TYR   A CZ  1 
ATOM   3596 O  OH  . TYR   B 1 193 ? -15.842 -36.867 18.760 1.00 20.09 ? 193 TYR   A OH  1 
ATOM   3597 N  N   . TRP   B 1 194 ? -18.044 -38.357 25.283 1.00 13.14 ? 194 TRP   A N   1 
ATOM   3598 C  CA  . TRP   B 1 194 ? -18.232 -39.768 24.957 1.00 14.92 ? 194 TRP   A CA  1 
ATOM   3599 C  C   . TRP   B 1 194 ? -19.326 -39.895 23.879 1.00 14.21 ? 194 TRP   A C   1 
ATOM   3600 O  O   . TRP   B 1 194 ? -20.278 -39.113 23.910 1.00 14.58 ? 194 TRP   A O   1 
ATOM   3601 C  CB  . TRP   B 1 194 ? -18.730 -40.499 26.215 1.00 15.57 ? 194 TRP   A CB  1 
ATOM   3602 C  CG  . TRP   B 1 194 ? -17.752 -40.519 27.357 1.00 15.89 ? 194 TRP   A CG  1 
ATOM   3603 C  CD1 . TRP   B 1 194 ? -16.540 -41.145 27.347 1.00 18.15 ? 194 TRP   A CD1 1 
ATOM   3604 C  CD2 . TRP   B 1 194 ? -17.839 -39.822 28.597 1.00 14.68 ? 194 TRP   A CD2 1 
ATOM   3605 N  NE1 . TRP   B 1 194 ? -15.895 -40.936 28.545 1.00 18.04 ? 194 TRP   A NE1 1 
ATOM   3606 C  CE2 . TRP   B 1 194 ? -16.668 -40.147 29.339 1.00 17.67 ? 194 TRP   A CE2 1 
ATOM   3607 C  CE3 . TRP   B 1 194 ? -18.816 -39.030 29.220 1.00 15.96 ? 194 TRP   A CE3 1 
ATOM   3608 C  CZ2 . TRP   B 1 194 ? -16.459 -39.707 30.645 1.00 18.14 ? 194 TRP   A CZ2 1 
ATOM   3609 C  CZ3 . TRP   B 1 194 ? -18.593 -38.585 30.517 1.00 17.84 ? 194 TRP   A CZ3 1 
ATOM   3610 C  CH2 . TRP   B 1 194 ? -17.426 -38.921 31.222 1.00 17.55 ? 194 TRP   A CH2 1 
ATOM   3611 N  N   . THR   B 1 195 ? -19.297 -40.951 23.041 1.00 13.51 ? 195 THR   A N   1 
ATOM   3612 C  CA  . THR   B 1 195 ? -20.353 -41.131 22.020 1.00 13.10 ? 195 THR   A CA  1 
ATOM   3613 C  C   . THR   B 1 195 ? -20.743 -42.607 21.898 1.00 13.10 ? 195 THR   A C   1 
ATOM   3614 O  O   . THR   B 1 195 ? -19.890 -43.488 22.018 1.00 14.58 ? 195 THR   A O   1 
ATOM   3615 C  CB  . THR   B 1 195 ? -19.926 -40.492 20.689 1.00 14.10 ? 195 THR   A CB  1 
ATOM   3616 O  OG1 . THR   B 1 195 ? -21.025 -40.611 19.787 1.00 15.08 ? 195 THR   A OG1 1 
ATOM   3617 C  CG2 . THR   B 1 195 ? -18.736 -41.232 20.090 1.00 14.68 ? 195 THR   A CG2 1 
ATOM   3618 N  N   . TYR   B 1 196 ? -22.023 -42.879 21.635 1.00 11.34 ? 196 TYR   A N   1 
ATOM   3619 C  CA  . TYR   B 1 196 ? -22.441 -44.254 21.346 1.00 13.00 ? 196 TYR   A CA  1 
ATOM   3620 C  C   . TYR   B 1 196 ? -23.776 -44.168 20.613 1.00 13.38 ? 196 TYR   A C   1 
ATOM   3621 O  O   . TYR   B 1 196 ? -24.441 -43.122 20.677 1.00 13.50 ? 196 TYR   A O   1 
ATOM   3622 C  CB  . TYR   B 1 196 ? -22.608 -44.992 22.692 1.00 13.05 ? 196 TYR   A CB  1 
ATOM   3623 C  CG  . TYR   B 1 196 ? -23.807 -44.553 23.514 1.00 11.47 ? 196 TYR   A CG  1 
ATOM   3624 C  CD1 . TYR   B 1 196 ? -23.779 -43.437 24.347 1.00 12.31 ? 196 TYR   A CD1 1 
ATOM   3625 C  CD2 . TYR   B 1 196 ? -25.003 -45.250 23.432 1.00 12.23 ? 196 TYR   A CD2 1 
ATOM   3626 C  CE1 . TYR   B 1 196 ? -24.912 -43.020 25.056 1.00 12.04 ? 196 TYR   A CE1 1 
ATOM   3627 C  CE2 . TYR   B 1 196 ? -26.148 -44.840 24.116 1.00 12.72 ? 196 TYR   A CE2 1 
ATOM   3628 C  CZ  . TYR   B 1 196 ? -26.096 -43.718 24.927 1.00 12.24 ? 196 TYR   A CZ  1 
ATOM   3629 O  OH  . TYR   B 1 196 ? -27.202 -43.308 25.629 1.00 13.30 ? 196 TYR   A OH  1 
ATOM   3630 N  N   . PRO   B 1 197 ? -24.230 -45.230 19.912 1.00 13.06 ? 197 PRO   A N   1 
ATOM   3631 C  CA  . PRO   B 1 197 ? -25.534 -45.201 19.240 1.00 13.54 ? 197 PRO   A CA  1 
ATOM   3632 C  C   . PRO   B 1 197 ? -26.654 -45.599 20.201 1.00 14.69 ? 197 PRO   A C   1 
ATOM   3633 O  O   . PRO   B 1 197 ? -26.563 -46.621 20.877 1.00 13.96 ? 197 PRO   A O   1 
ATOM   3634 C  CB  . PRO   B 1 197 ? -25.363 -46.238 18.112 1.00 16.46 ? 197 PRO   A CB  1 
ATOM   3635 C  CG  . PRO   B 1 197 ? -24.375 -47.255 18.738 1.00 15.18 ? 197 PRO   A CG  1 
ATOM   3636 C  CD  . PRO   B 1 197 ? -23.440 -46.448 19.631 1.00 15.60 ? 197 PRO   A CD  1 
ATOM   3637 N  N   . GLY   B 1 198 ? -27.738 -44.813 20.214 1.00 12.98 ? 198 GLY   A N   1 
ATOM   3638 C  CA  . GLY   B 1 198 ? -28.811 -45.143 21.142 1.00 13.96 ? 198 GLY   A CA  1 
ATOM   3639 C  C   . GLY   B 1 198 ? -30.159 -44.624 20.647 1.00 12.41 ? 198 GLY   A C   1 
ATOM   3640 O  O   . GLY   B 1 198 ? -30.427 -44.689 19.441 1.00 12.83 ? 198 GLY   A O   1 
ATOM   3641 N  N   . SER   B 1 199 ? -30.985 -44.173 21.600 1.00 11.90 ? 199 SER   A N   1 
ATOM   3642 C  CA  . SER   B 1 199 ? -32.391 -43.961 21.310 1.00 10.83 ? 199 SER   A CA  1 
ATOM   3643 C  C   . SER   B 1 199 ? -32.862 -42.648 21.918 1.00 10.68 ? 199 SER   A C   1 
ATOM   3644 O  O   . SER   B 1 199 ? -32.246 -42.086 22.838 1.00 11.00 ? 199 SER   A O   1 
ATOM   3645 C  CB  . SER   B 1 199 ? -33.208 -45.157 21.861 1.00 11.66 ? 199 SER   A CB  1 
ATOM   3646 O  OG  . SER   B 1 199 ? -33.322 -45.123 23.288 1.00 11.12 ? 199 SER   A OG  1 
ATOM   3647 N  N   . LEU   B 1 200 ? -34.093 -42.291 21.545 1.00 11.85 ? 200 LEU   A N   1 
ATOM   3648 C  CA  . LEU   B 1 200 ? -34.825 -41.350 22.386 1.00 12.62 ? 200 LEU   A CA  1 
ATOM   3649 C  C   . LEU   B 1 200 ? -34.976 -41.984 23.776 1.00 12.95 ? 200 LEU   A C   1 
ATOM   3650 O  O   . LEU   B 1 200 ? -35.177 -43.208 23.889 1.00 12.69 ? 200 LEU   A O   1 
ATOM   3651 C  CB  . LEU   B 1 200 ? -36.218 -41.108 21.771 1.00 13.32 ? 200 LEU   A CB  1 
ATOM   3652 C  CG  . LEU   B 1 200 ? -36.187 -40.536 20.334 1.00 15.03 ? 200 LEU   A CG  1 
ATOM   3653 C  CD1 . LEU   B 1 200 ? -37.653 -40.367 19.903 1.00 18.65 ? 200 LEU   A CD1 1 
ATOM   3654 C  CD2 . LEU   B 1 200 ? -35.479 -39.191 20.383 1.00 15.30 ? 200 LEU   A CD2 1 
ATOM   3655 N  N   . THR   B 1 201 ? -34.971 -41.140 24.825 1.00 11.33 ? 201 THR   A N   1 
ATOM   3656 C  CA  . THR   B 1 201 ? -35.173 -41.646 26.197 1.00 10.66 ? 201 THR   A CA  1 
ATOM   3657 C  C   . THR   B 1 201 ? -36.620 -41.484 26.674 1.00 11.32 ? 201 THR   A C   1 
ATOM   3658 O  O   . THR   B 1 201 ? -36.935 -41.727 27.855 1.00 11.07 ? 201 THR   A O   1 
ATOM   3659 C  CB  . THR   B 1 201 ? -34.172 -41.092 27.218 1.00 12.23 ? 201 THR   A CB  1 
ATOM   3660 O  OG1 . THR   B 1 201 ? -34.578 -39.751 27.513 1.00 11.66 ? 201 THR   A OG1 1 
ATOM   3661 C  CG2 . THR   B 1 201 ? -32.713 -41.270 26.813 1.00 13.83 ? 201 THR   A CG2 1 
ATOM   3662 N  N   . VAL   B 1 202 ? -37.486 -41.025 25.760 1.00 12.62 ? 202 VAL   A N   1 
ATOM   3663 C  CA  . VAL   B 1 202 ? -38.936 -40.956 26.009 1.00 12.86 ? 202 VAL   A CA  1 
ATOM   3664 C  C   . VAL   B 1 202 ? -39.641 -41.725 24.896 1.00 14.68 ? 202 VAL   A C   1 
ATOM   3665 O  O   . VAL   B 1 202 ? -39.098 -41.844 23.786 1.00 14.50 ? 202 VAL   A O   1 
ATOM   3666 C  CB  . VAL   B 1 202 ? -39.449 -39.502 26.055 1.00 14.13 ? 202 VAL   A CB  1 
ATOM   3667 C  CG1 . VAL   B 1 202 ? -38.923 -38.788 27.326 1.00 13.88 ? 202 VAL   A CG1 1 
ATOM   3668 C  CG2 . VAL   B 1 202 ? -39.124 -38.754 24.769 1.00 13.07 ? 202 VAL   A CG2 1 
ATOM   3669 N  N   . PRO   B 1 203 ? -40.887 -42.213 25.142 1.00 14.15 ? 203 PRO   A N   1 
ATOM   3670 C  CA  . PRO   B 1 203 ? -41.696 -42.801 24.055 1.00 14.97 ? 203 PRO   A CA  1 
ATOM   3671 C  C   . PRO   B 1 203 ? -41.693 -41.824 22.885 1.00 14.31 ? 203 PRO   A C   1 
ATOM   3672 O  O   . PRO   B 1 203 ? -41.887 -40.600 23.074 1.00 14.82 ? 203 PRO   A O   1 
ATOM   3673 C  CB  . PRO   B 1 203 ? -43.056 -42.877 24.745 1.00 13.64 ? 203 PRO   A CB  1 
ATOM   3674 C  CG  . PRO   B 1 203 ? -42.618 -43.322 26.155 1.00 14.42 ? 203 PRO   A CG  1 
ATOM   3675 C  CD  . PRO   B 1 203 ? -41.538 -42.283 26.457 1.00 12.84 ? 203 PRO   A CD  1 
ATOM   3676 N  N   . PRO   B 1 204 ? -41.599 -42.293 21.613 1.00 14.94 ? 204 PRO   A N   1 
ATOM   3677 C  CA  . PRO   B 1 204 ? -41.581 -43.722 21.258 1.00 15.24 ? 204 PRO   A CA  1 
ATOM   3678 C  C   . PRO   B 1 204 ? -40.257 -44.483 21.247 1.00 15.75 ? 204 PRO   A C   1 
ATOM   3679 O  O   . PRO   B 1 204 ? -40.210 -45.611 20.716 1.00 18.65 ? 204 PRO   A O   1 
ATOM   3680 C  CB  . PRO   B 1 204 ? -42.090 -43.652 19.780 1.00 16.08 ? 204 PRO   A CB  1 
ATOM   3681 C  CG  . PRO   B 1 204 ? -41.543 -42.343 19.274 1.00 15.84 ? 204 PRO   A CG  1 
ATOM   3682 C  CD  . PRO   B 1 204 ? -41.683 -41.385 20.435 1.00 16.49 ? 204 PRO   A CD  1 
ATOM   3683 N  N   . LEU   B 1 205 ? -39.188 -43.926 21.859 1.00 14.52 ? 205 LEU   A N   1 
ATOM   3684 C  CA  . LEU   B 1 205 ? -37.957 -44.691 22.151 1.00 13.12 ? 205 LEU   A CA  1 
ATOM   3685 C  C   . LEU   B 1 205 ? -37.204 -45.133 20.896 1.00 13.44 ? 205 LEU   A C   1 
ATOM   3686 O  O   . LEU   B 1 205 ? -36.503 -46.157 20.927 1.00 13.52 ? 205 LEU   A O   1 
ATOM   3687 C  CB  . LEU   B 1 205 ? -38.214 -45.866 23.116 1.00 14.56 ? 205 LEU   A CB  1 
ATOM   3688 C  CG  . LEU   B 1 205 ? -38.894 -45.464 24.430 1.00 12.25 ? 205 LEU   A CG  1 
ATOM   3689 C  CD1 . LEU   B 1 205 ? -39.473 -46.686 25.125 1.00 15.21 ? 205 LEU   A CD1 1 
ATOM   3690 C  CD2 . LEU   B 1 205 ? -37.897 -44.705 25.347 1.00 15.32 ? 205 LEU   A CD2 1 
ATOM   3691 N  N   . LEU   B 1 206 ? -37.372 -44.389 19.791 1.00 13.95 ? 206 LEU   A N   1 
ATOM   3692 C  CA  . LEU   B 1 206 ? -36.824 -44.763 18.495 1.00 14.50 ? 206 LEU   A CA  1 
ATOM   3693 C  C   . LEU   B 1 206 ? -35.307 -44.785 18.529 1.00 12.72 ? 206 LEU   A C   1 
ATOM   3694 O  O   . LEU   B 1 206 ? -34.678 -43.919 19.147 1.00 13.23 ? 206 LEU   A O   1 
ATOM   3695 C  CB  . LEU   B 1 206 ? -37.289 -43.764 17.410 1.00 15.80 ? 206 LEU   A CB  1 
ATOM   3696 C  CG  . LEU   B 1 206 ? -38.813 -43.817 17.186 1.00 17.28 ? 206 LEU   A CG  1 
ATOM   3697 C  CD1 . LEU   B 1 206 ? -39.256 -42.593 16.394 1.00 18.89 ? 206 LEU   A CD1 1 
ATOM   3698 C  CD2 . LEU   B 1 206 ? -39.199 -45.124 16.499 1.00 23.12 ? 206 LEU   A CD2 1 
ATOM   3699 N  N   . GLU   B 1 207 ? -34.739 -45.817 17.850 1.00 13.29 ? 207 GLU   A N   1 
ATOM   3700 C  CA  . GLU   B 1 207 ? -33.292 -45.998 17.877 1.00 13.61 ? 207 GLU   A CA  1 
ATOM   3701 C  C   . GLU   B 1 207 ? -32.663 -45.238 16.723 1.00 14.33 ? 207 GLU   A C   1 
ATOM   3702 O  O   . GLU   B 1 207 ? -32.217 -45.857 15.733 1.00 16.71 ? 207 GLU   A O   1 
ATOM   3703 C  CB  . GLU   B 1 207 ? -32.962 -47.503 17.920 1.00 14.41 ? 207 GLU   A CB  1 
ATOM   3704 C  CG  . GLU   B 1 207 ? -33.473 -48.130 19.236 1.00 14.57 ? 207 GLU   A CG  1 
ATOM   3705 C  CD  . GLU   B 1 207 ? -33.281 -49.643 19.386 1.00 15.60 ? 207 GLU   A CD  1 
ATOM   3706 O  OE1 . GLU   B 1 207 ? -33.174 -50.329 18.350 1.00 18.42 ? 207 GLU   A OE1 1 
ATOM   3707 O  OE2 . GLU   B 1 207 ? -33.240 -50.121 20.537 1.00 15.01 ? 207 GLU   A OE2 1 
ATOM   3708 N  N   . SER   B 1 208 ? -32.652 -43.895 16.859 1.00 13.14 ? 208 SER   A N   1 
ATOM   3709 C  CA  . SER   B 1 208 ? -32.233 -43.051 15.745 1.00 13.87 ? 208 SER   A CA  1 
ATOM   3710 C  C   . SER   B 1 208 ? -31.224 -42.012 16.243 1.00 13.80 ? 208 SER   A C   1 
ATOM   3711 O  O   . SER   B 1 208 ? -30.878 -41.078 15.524 1.00 14.89 ? 208 SER   A O   1 
ATOM   3712 C  CB  . SER   B 1 208 ? -33.431 -42.330 15.160 1.00 16.14 ? 208 SER   A CB  1 
ATOM   3713 O  OG  . SER   B 1 208 ? -34.120 -41.735 16.264 1.00 18.98 ? 208 SER   A OG  1 
ATOM   3714 N  N   . VAL   B 1 209 ? -30.650 -42.226 17.442 1.00 13.82 ? 209 VAL   A N   1 
ATOM   3715 C  CA  . VAL   B 1 209 ? -29.874 -41.155 18.071 1.00 12.52 ? 209 VAL   A CA  1 
ATOM   3716 C  C   . VAL   B 1 209 ? -28.384 -41.495 18.153 1.00 13.94 ? 209 VAL   A C   1 
ATOM   3717 O  O   . VAL   B 1 209 ? -28.010 -42.556 18.665 1.00 16.13 ? 209 VAL   A O   1 
ATOM   3718 C  CB  . VAL   B 1 209 ? -30.366 -40.785 19.505 1.00 12.42 ? 209 VAL   A CB  1 
ATOM   3719 C  CG1 . VAL   B 1 209 ? -29.521 -39.641 20.042 1.00 12.92 ? 209 VAL   A CG1 1 
ATOM   3720 C  CG2 . VAL   B 1 209 ? -31.852 -40.314 19.520 1.00 12.60 ? 209 VAL   A CG2 1 
ATOM   3721 N  N   . THR   B 1 210 ? -27.554 -40.574 17.655 1.00 12.08 ? 210 THR   A N   1 
ATOM   3722 C  CA  . THR   B 1 210 ? -26.125 -40.557 17.976 1.00 12.84 ? 210 THR   A CA  1 
ATOM   3723 C  C   . THR   B 1 210 ? -25.943 -39.675 19.209 1.00 12.60 ? 210 THR   A C   1 
ATOM   3724 O  O   . THR   B 1 210 ? -26.178 -38.474 19.169 1.00 12.88 ? 210 THR   A O   1 
ATOM   3725 C  CB  . THR   B 1 210 ? -25.289 -40.040 16.797 1.00 13.59 ? 210 THR   A CB  1 
ATOM   3726 O  OG1 . THR   B 1 210 ? -25.487 -40.905 15.661 1.00 15.40 ? 210 THR   A OG1 1 
ATOM   3727 C  CG2 . THR   B 1 210 ? -23.825 -39.899 17.176 1.00 15.81 ? 210 THR   A CG2 1 
ATOM   3728 N  N   . TRP   B 1 211 ? -25.609 -40.320 20.350 1.00 11.63 ? 211 TRP   A N   1 
ATOM   3729 C  CA  . TRP   B 1 211 ? -25.471 -39.595 21.611 1.00 11.55 ? 211 TRP   A CA  1 
ATOM   3730 C  C   . TRP   B 1 211 ? -24.074 -39.022 21.730 1.00 12.42 ? 211 TRP   A C   1 
ATOM   3731 O  O   . TRP   B 1 211 ? -23.117 -39.725 21.448 1.00 15.45 ? 211 TRP   A O   1 
ATOM   3732 C  CB  . TRP   B 1 211 ? -25.708 -40.588 22.792 1.00 11.64 ? 211 TRP   A CB  1 
ATOM   3733 C  CG  . TRP   B 1 211 ? -27.186 -40.708 23.045 1.00 11.63 ? 211 TRP   A CG  1 
ATOM   3734 C  CD1 . TRP   B 1 211 ? -28.067 -41.638 22.564 1.00 12.77 ? 211 TRP   A CD1 1 
ATOM   3735 C  CD2 . TRP   B 1 211 ? -27.958 -39.771 23.812 1.00 11.79 ? 211 TRP   A CD2 1 
ATOM   3736 N  NE1 . TRP   B 1 211 ? -29.338 -41.303 22.955 1.00 12.47 ? 211 TRP   A NE1 1 
ATOM   3737 C  CE2 . TRP   B 1 211 ? -29.297 -40.176 23.737 1.00 11.98 ? 211 TRP   A CE2 1 
ATOM   3738 C  CE3 . TRP   B 1 211 ? -27.639 -38.598 24.516 1.00 13.42 ? 211 TRP   A CE3 1 
ATOM   3739 C  CZ2 . TRP   B 1 211 ? -30.329 -39.466 24.379 1.00 12.23 ? 211 TRP   A CZ2 1 
ATOM   3740 C  CZ3 . TRP   B 1 211 ? -28.644 -37.870 25.120 1.00 12.73 ? 211 TRP   A CZ3 1 
ATOM   3741 C  CH2 . TRP   B 1 211 ? -29.963 -38.315 25.073 1.00 13.30 ? 211 TRP   A CH2 1 
ATOM   3742 N  N   . ILE   B 1 212 ? -23.972 -37.761 22.163 1.00 11.56 ? 212 ILE   A N   1 
ATOM   3743 C  CA  . ILE   B 1 212 ? -22.695 -37.114 22.423 1.00 11.88 ? 212 ILE   A CA  1 
ATOM   3744 C  C   . ILE   B 1 212 ? -22.830 -36.551 23.840 1.00 12.83 ? 212 ILE   A C   1 
ATOM   3745 O  O   . ILE   B 1 212 ? -23.528 -35.559 24.056 1.00 13.21 ? 212 ILE   A O   1 
ATOM   3746 C  CB  . ILE   B 1 212 ? -22.442 -36.005 21.355 1.00 14.60 ? 212 ILE   A CB  1 
ATOM   3747 C  CG1 . ILE   B 1 212 ? -22.368 -36.606 19.945 1.00 16.03 ? 212 ILE   A CG1 1 
ATOM   3748 C  CG2 . ILE   B 1 212 ? -21.170 -35.241 21.685 1.00 14.51 ? 212 ILE   A CG2 1 
ATOM   3749 C  CD1 . ILE   B 1 212 ? -22.498 -35.567 18.799 1.00 17.31 ? 212 ILE   A CD1 1 
ATOM   3750 N  N   . VAL   B 1 213 ? -22.149 -37.172 24.812 1.00 12.97 ? 213 VAL   A N   1 
ATOM   3751 C  CA  . VAL   B 1 213 ? -22.314 -36.751 26.202 1.00 12.67 ? 213 VAL   A CA  1 
ATOM   3752 C  C   . VAL   B 1 213 ? -21.033 -36.071 26.650 1.00 13.63 ? 213 VAL   A C   1 
ATOM   3753 O  O   . VAL   B 1 213 ? -19.980 -36.713 26.630 1.00 13.07 ? 213 VAL   A O   1 
ATOM   3754 C  CB  . VAL   B 1 213 ? -22.628 -37.994 27.073 1.00 12.84 ? 213 VAL   A CB  1 
ATOM   3755 C  CG1 . VAL   B 1 213 ? -22.693 -37.695 28.559 1.00 14.66 ? 213 VAL   A CG1 1 
ATOM   3756 C  CG2 . VAL   B 1 213 ? -23.961 -38.640 26.676 1.00 13.79 ? 213 VAL   A CG2 1 
ATOM   3757 N  N   . LEU   B 1 214 ? -21.131 -34.805 27.059 1.00 13.63 ? 214 LEU   A N   1 
ATOM   3758 C  CA  . LEU   B 1 214 ? -19.939 -34.051 27.470 1.00 13.79 ? 214 LEU   A CA  1 
ATOM   3759 C  C   . LEU   B 1 214 ? -19.463 -34.525 28.848 1.00 13.94 ? 214 LEU   A C   1 
ATOM   3760 O  O   . LEU   B 1 214 ? -20.256 -34.811 29.741 1.00 14.48 ? 214 LEU   A O   1 
ATOM   3761 C  CB  . LEU   B 1 214 ? -20.250 -32.548 27.500 1.00 14.18 ? 214 LEU   A CB  1 
ATOM   3762 C  CG  . LEU   B 1 214 ? -20.634 -31.959 26.138 1.00 17.06 ? 214 LEU   A CG  1 
ATOM   3763 C  CD1 . LEU   B 1 214 ? -20.543 -30.439 26.184 1.00 19.25 ? 214 LEU   A CD1 1 
ATOM   3764 C  CD2 . LEU   B 1 214 ? -19.765 -32.474 25.002 1.00 22.29 ? 214 LEU   A CD2 1 
ATOM   3765 N  N   A LYS   B 1 215 ? -18.133 -34.623 29.020 0.50 13.43 ? 215 LYS   A N   1 
ATOM   3766 N  N   B LYS   B 1 215 ? -18.134 -34.596 29.012 0.50 12.56 ? 215 LYS   A N   1 
ATOM   3767 C  CA  A LYS   B 1 215 ? -17.583 -35.136 30.272 0.50 15.82 ? 215 LYS   A CA  1 
ATOM   3768 C  CA  B LYS   B 1 215 ? -17.552 -35.128 30.237 0.50 14.22 ? 215 LYS   A CA  1 
ATOM   3769 C  C   A LYS   B 1 215 ? -17.662 -34.113 31.401 0.50 15.35 ? 215 LYS   A C   1 
ATOM   3770 C  C   B LYS   B 1 215 ? -17.604 -34.127 31.387 0.50 14.30 ? 215 LYS   A C   1 
ATOM   3771 O  O   A LYS   B 1 215 ? -17.923 -34.484 32.556 0.50 17.66 ? 215 LYS   A O   1 
ATOM   3772 O  O   B LYS   B 1 215 ? -17.795 -34.536 32.543 0.50 17.01 ? 215 LYS   A O   1 
ATOM   3773 C  CB  A LYS   B 1 215 ? -16.132 -35.608 30.107 0.50 17.08 ? 215 LYS   A CB  1 
ATOM   3774 C  CB  B LYS   B 1 215 ? -16.101 -35.541 29.974 0.50 13.55 ? 215 LYS   A CB  1 
ATOM   3775 C  CG  A LYS   B 1 215 ? -15.432 -35.949 31.420 0.50 18.85 ? 215 LYS   A CG  1 
ATOM   3776 C  CG  B LYS   B 1 215 ? -15.898 -36.489 28.802 0.50 13.38 ? 215 LYS   A CG  1 
ATOM   3777 C  CD  A LYS   B 1 215 ? -13.941 -36.214 31.296 0.50 23.17 ? 215 LYS   A CD  1 
ATOM   3778 C  CD  B LYS   B 1 215 ? -14.445 -36.982 28.709 0.50 14.30 ? 215 LYS   A CD  1 
ATOM   3779 C  CE  A LYS   B 1 215 ? -13.146 -35.742 32.506 0.50 23.45 ? 215 LYS   A CE  1 
ATOM   3780 C  CE  B LYS   B 1 215 ? -14.184 -37.880 27.510 0.50 14.10 ? 215 LYS   A CE  1 
ATOM   3781 N  NZ  A LYS   B 1 215 ? -12.199 -36.800 32.929 0.50 27.97 ? 215 LYS   A NZ  1 
ATOM   3782 N  NZ  B LYS   B 1 215 ? -12.950 -38.666 27.724 0.50 16.25 ? 215 LYS   A NZ  1 
ATOM   3783 N  N   . GLN   B 1 216 ? -17.467 -32.832 31.081 1.00 14.58 ? 216 GLN   A N   1 
ATOM   3784 C  CA  . GLN   B 1 216 ? -17.411 -31.790 32.098 1.00 13.20 ? 216 GLN   A CA  1 
ATOM   3785 C  C   . GLN   B 1 216 ? -18.790 -31.256 32.481 1.00 15.13 ? 216 GLN   A C   1 
ATOM   3786 O  O   . GLN   B 1 216 ? -19.537 -30.758 31.630 1.00 15.36 ? 216 GLN   A O   1 
ATOM   3787 C  CB  . GLN   B 1 216 ? -16.526 -30.625 31.626 1.00 15.63 ? 216 GLN   A CB  1 
ATOM   3788 C  CG  . GLN   B 1 216 ? -16.391 -29.531 32.706 1.00 16.28 ? 216 GLN   A CG  1 
ATOM   3789 C  CD  . GLN   B 1 216 ? -15.451 -28.403 32.340 1.00 20.18 ? 216 GLN   A CD  1 
ATOM   3790 O  OE1 . GLN   B 1 216 ? -14.996 -28.290 31.186 1.00 21.29 ? 216 GLN   A OE1 1 
ATOM   3791 N  NE2 . GLN   B 1 216 ? -15.110 -27.608 33.357 1.00 21.40 ? 216 GLN   A NE2 1 
ATOM   3792 N  N   . PRO   B 1 217 ? -19.191 -31.287 33.768 1.00 16.15 ? 217 PRO   A N   1 
ATOM   3793 C  CA  . PRO   B 1 217 ? -20.492 -30.732 34.158 1.00 16.67 ? 217 PRO   A CA  1 
ATOM   3794 C  C   . PRO   B 1 217 ? -20.543 -29.214 34.300 1.00 17.33 ? 217 PRO   A C   1 
ATOM   3795 O  O   . PRO   B 1 217 ? -19.483 -28.556 34.365 1.00 17.70 ? 217 PRO   A O   1 
ATOM   3796 C  CB  . PRO   B 1 217 ? -20.710 -31.318 35.552 1.00 18.66 ? 217 PRO   A CB  1 
ATOM   3797 C  CG  . PRO   B 1 217 ? -19.276 -31.373 36.039 1.00 20.39 ? 217 PRO   A CG  1 
ATOM   3798 C  CD  . PRO   B 1 217 ? -18.534 -32.002 34.882 1.00 18.77 ? 217 PRO   A CD  1 
ATOM   3799 N  N   . ILE   B 1 218 ? -21.783 -28.686 34.331 1.00 14.31 ? 218 ILE   A N   1 
ATOM   3800 C  CA  . ILE   B 1 218 ? -22.008 -27.272 34.651 1.00 14.98 ? 218 ILE   A CA  1 
ATOM   3801 C  C   . ILE   B 1 218 ? -22.694 -27.234 36.008 1.00 16.02 ? 218 ILE   A C   1 
ATOM   3802 O  O   . ILE   B 1 218 ? -23.122 -28.278 36.485 1.00 17.07 ? 218 ILE   A O   1 
ATOM   3803 C  CB  . ILE   B 1 218 ? -22.837 -26.514 33.595 1.00 14.51 ? 218 ILE   A CB  1 
ATOM   3804 C  CG1 . ILE   B 1 218 ? -24.314 -26.957 33.517 1.00 16.33 ? 218 ILE   A CG1 1 
ATOM   3805 C  CG2 . ILE   B 1 218 ? -22.190 -26.542 32.221 1.00 16.23 ? 218 ILE   A CG2 1 
ATOM   3806 C  CD1 . ILE   B 1 218 ? -25.172 -26.010 32.613 1.00 16.36 ? 218 ILE   A CD1 1 
ATOM   3807 N  N   . ASN   B 1 219 ? -22.769 -26.077 36.664 1.00 14.73 ? 219 ASN   A N   1 
ATOM   3808 C  CA  . ASN   B 1 219 ? -23.374 -26.088 38.002 1.00 15.27 ? 219 ASN   A CA  1 
ATOM   3809 C  C   . ASN   B 1 219 ? -24.857 -25.704 37.979 1.00 15.48 ? 219 ASN   A C   1 
ATOM   3810 O  O   . ASN   B 1 219 ? -25.314 -24.974 37.098 1.00 16.47 ? 219 ASN   A O   1 
ATOM   3811 C  CB  . ASN   B 1 219 ? -22.792 -24.987 38.890 1.00 18.29 ? 219 ASN   A CB  1 
ATOM   3812 C  CG  . ASN   B 1 219 ? -21.374 -25.245 39.370 1.00 24.84 ? 219 ASN   A CG  1 
ATOM   3813 O  OD1 . ASN   B 1 219 ? -20.670 -24.301 39.761 1.00 37.01 ? 219 ASN   A OD1 1 
ATOM   3814 N  ND2 . ASN   B 1 219 ? -20.932 -26.484 39.386 1.00 22.85 ? 219 ASN   A ND2 1 
ATOM   3815 N  N   . ILE   B 1 220 ? -25.570 -26.120 39.044 1.00 14.44 ? 220 ILE   A N   1 
ATOM   3816 C  CA  . ILE   B 1 220 ? -26.915 -25.601 39.351 1.00 14.20 ? 220 ILE   A CA  1 
ATOM   3817 C  C   . ILE   B 1 220 ? -27.043 -25.596 40.880 1.00 14.69 ? 220 ILE   A C   1 
ATOM   3818 O  O   . ILE   B 1 220 ? -26.533 -26.517 41.504 1.00 14.78 ? 220 ILE   A O   1 
ATOM   3819 C  CB  . ILE   B 1 220 ? -28.029 -26.477 38.699 1.00 13.46 ? 220 ILE   A CB  1 
ATOM   3820 C  CG1 . ILE   B 1 220 ? -29.420 -25.879 38.946 1.00 14.04 ? 220 ILE   A CG1 1 
ATOM   3821 C  CG2 . ILE   B 1 220 ? -28.009 -27.920 39.175 1.00 15.19 ? 220 ILE   A CG2 1 
ATOM   3822 C  CD1 . ILE   B 1 220 ? -30.498 -26.329 37.932 1.00 16.11 ? 220 ILE   A CD1 1 
ATOM   3823 N  N   . SER   B 1 221 ? -27.778 -24.630 41.489 1.00 14.39 ? 221 SER   A N   1 
ATOM   3824 C  CA  . SER   B 1 221 ? -28.008 -24.768 42.926 1.00 14.84 ? 221 SER   A CA  1 
ATOM   3825 C  C   . SER   B 1 221 ? -29.218 -25.679 43.211 1.00 15.35 ? 221 SER   A C   1 
ATOM   3826 O  O   . SER   B 1 221 ? -30.088 -25.877 42.333 1.00 17.52 ? 221 SER   A O   1 
ATOM   3827 C  CB  . SER   B 1 221 ? -28.209 -23.413 43.610 1.00 14.14 ? 221 SER   A CB  1 
ATOM   3828 O  OG  . SER   B 1 221 ? -29.462 -22.854 43.234 1.00 16.48 ? 221 SER   A OG  1 
ATOM   3829 N  N   . SER   B 1 222 ? -29.328 -26.137 44.480 1.00 15.20 ? 222 SER   A N   1 
ATOM   3830 C  CA  . SER   B 1 222 ? -30.515 -26.899 44.868 1.00 16.04 ? 222 SER   A CA  1 
ATOM   3831 C  C   . SER   B 1 222 ? -31.792 -26.097 44.655 1.00 15.74 ? 222 SER   A C   1 
ATOM   3832 O  O   . SER   B 1 222 ? -32.804 -26.667 44.206 1.00 15.70 ? 222 SER   A O   1 
ATOM   3833 C  CB  . SER   B 1 222 ? -30.476 -27.444 46.313 1.00 18.24 ? 222 SER   A CB  1 
ATOM   3834 O  OG  . SER   B 1 222 ? -29.416 -28.385 46.427 1.00 23.34 ? 222 SER   A OG  1 
ATOM   3835 N  N   . GLN   B 1 223 ? -31.769 -24.817 45.053 1.00 15.71 ? 223 GLN   A N   1 
ATOM   3836 C  CA  . GLN   B 1 223 ? -32.943 -23.974 44.919 1.00 14.85 ? 223 GLN   A CA  1 
ATOM   3837 C  C   . GLN   B 1 223 ? -33.353 -23.803 43.451 1.00 15.71 ? 223 GLN   A C   1 
ATOM   3838 O  O   . GLN   B 1 223 ? -34.548 -23.815 43.173 1.00 16.46 ? 223 GLN   A O   1 
ATOM   3839 C  CB  . GLN   B 1 223 ? -32.753 -22.640 45.656 1.00 16.86 ? 223 GLN   A CB  1 
ATOM   3840 C  CG  . GLN   B 1 223 ? -32.945 -22.768 47.158 1.00 21.22 ? 223 GLN   A CG  1 
ATOM   3841 C  CD  . GLN   B 1 223 ? -33.078 -21.394 47.811 1.00 24.16 ? 223 GLN   A CD  1 
ATOM   3842 O  OE1 . GLN   B 1 223 ? -33.796 -20.518 47.318 1.00 28.87 ? 223 GLN   A OE1 1 
ATOM   3843 N  NE2 . GLN   B 1 223 ? -32.306 -21.160 48.869 1.00 27.02 ? 223 GLN   A NE2 1 
ATOM   3844 N  N   . GLN   B 1 224 ? -32.372 -23.622 42.548 1.00 16.62 ? 224 GLN   A N   1 
ATOM   3845 C  CA  . GLN   B 1 224 ? -32.706 -23.483 41.127 1.00 14.96 ? 224 GLN   A CA  1 
ATOM   3846 C  C   . GLN   B 1 224 ? -33.364 -24.775 40.658 1.00 15.68 ? 224 GLN   A C   1 
ATOM   3847 O  O   . GLN   B 1 224 ? -34.417 -24.742 39.986 1.00 16.90 ? 224 GLN   A O   1 
ATOM   3848 C  CB  . GLN   B 1 224 ? -31.427 -23.227 40.317 1.00 15.27 ? 224 GLN   A CB  1 
ATOM   3849 C  CG  . GLN   B 1 224 ? -30.969 -21.778 40.391 1.00 14.50 ? 224 GLN   A CG  1 
ATOM   3850 C  CD  . GLN   B 1 224 ? -29.729 -21.599 39.550 1.00 17.45 ? 224 GLN   A CD  1 
ATOM   3851 O  OE1 . GLN   B 1 224 ? -28.760 -22.363 39.695 1.00 16.87 ? 224 GLN   A OE1 1 
ATOM   3852 N  NE2 . GLN   B 1 224 ? -29.763 -20.584 38.677 1.00 16.99 ? 224 GLN   A NE2 1 
ATOM   3853 N  N   . LEU   B 1 225 ? -32.768 -25.910 41.020 1.00 13.95 ? 225 LEU   A N   1 
ATOM   3854 C  CA  . LEU   B 1 225 ? -33.271 -27.181 40.490 1.00 15.07 ? 225 LEU   A CA  1 
ATOM   3855 C  C   . LEU   B 1 225 ? -34.674 -27.476 41.044 1.00 16.79 ? 225 LEU   A C   1 
ATOM   3856 O  O   . LEU   B 1 225 ? -35.531 -27.993 40.330 1.00 16.46 ? 225 LEU   A O   1 
ATOM   3857 C  CB  . LEU   B 1 225 ? -32.315 -28.329 40.835 1.00 16.75 ? 225 LEU   A CB  1 
ATOM   3858 C  CG  . LEU   B 1 225 ? -32.616 -29.729 40.265 1.00 18.14 ? 225 LEU   A CG  1 
ATOM   3859 C  CD1 . LEU   B 1 225 ? -32.828 -29.728 38.734 1.00 18.42 ? 225 LEU   A CD1 1 
ATOM   3860 C  CD2 . LEU   B 1 225 ? -31.499 -30.705 40.639 1.00 19.24 ? 225 LEU   A CD2 1 
ATOM   3861 N  N   . ALA   B 1 226 ? -34.960 -27.093 42.309 1.00 16.52 ? 226 ALA   A N   1 
ATOM   3862 C  CA  . ALA   B 1 226 ? -36.283 -27.339 42.870 1.00 17.14 ? 226 ALA   A CA  1 
ATOM   3863 C  C   . ALA   B 1 226 ? -37.381 -26.611 42.113 1.00 17.61 ? 226 ALA   A C   1 
ATOM   3864 O  O   . ALA   B 1 226 ? -38.529 -27.058 42.176 1.00 18.98 ? 226 ALA   A O   1 
ATOM   3865 C  CB  . ALA   B 1 226 ? -36.332 -26.916 44.333 1.00 17.99 ? 226 ALA   A CB  1 
ATOM   3866 N  N   . LYS   B 1 227 ? -37.057 -25.493 41.456 1.00 16.05 ? 227 LYS   A N   1 
ATOM   3867 C  CA  . LYS   B 1 227 ? -38.050 -24.726 40.712 1.00 18.38 ? 227 LYS   A CA  1 
ATOM   3868 C  C   . LYS   B 1 227 ? -38.643 -25.593 39.599 1.00 18.25 ? 227 LYS   A C   1 
ATOM   3869 O  O   . LYS   B 1 227 ? -39.847 -25.517 39.334 1.00 20.53 ? 227 LYS   A O   1 
ATOM   3870 C  CB  . LYS   B 1 227 ? -37.425 -23.447 40.131 1.00 19.69 ? 227 LYS   A CB  1 
ATOM   3871 C  CG  . LYS   B 1 227 ? -37.130 -22.353 41.145 1.00 25.16 ? 227 LYS   A CG  1 
ATOM   3872 C  CD  . LYS   B 1 227 ? -36.561 -21.102 40.508 1.00 31.85 ? 227 LYS   A CD  1 
ATOM   3873 N  N   . PHE   B 1 228 ? -37.812 -26.422 38.955 1.00 15.77 ? 228 PHE   A N   1 
ATOM   3874 C  CA  . PHE   B 1 228 ? -38.303 -27.312 37.882 1.00 15.32 ? 228 PHE   A CA  1 
ATOM   3875 C  C   . PHE   B 1 228 ? -39.332 -28.336 38.373 1.00 15.67 ? 228 PHE   A C   1 
ATOM   3876 O  O   . PHE   B 1 228 ? -40.284 -28.693 37.655 1.00 15.41 ? 228 PHE   A O   1 
ATOM   3877 C  CB  . PHE   B 1 228 ? -37.139 -28.021 37.163 1.00 14.62 ? 228 PHE   A CB  1 
ATOM   3878 C  CG  . PHE   B 1 228 ? -36.284 -26.991 36.448 1.00 14.86 ? 228 PHE   A CG  1 
ATOM   3879 C  CD1 . PHE   B 1 228 ? -36.688 -26.488 35.216 1.00 16.59 ? 228 PHE   A CD1 1 
ATOM   3880 C  CD2 . PHE   B 1 228 ? -35.098 -26.513 36.987 1.00 17.00 ? 228 PHE   A CD2 1 
ATOM   3881 C  CE1 . PHE   B 1 228 ? -35.966 -25.496 34.566 1.00 15.38 ? 228 PHE   A CE1 1 
ATOM   3882 C  CE2 . PHE   B 1 228 ? -34.358 -25.542 36.317 1.00 19.32 ? 228 PHE   A CE2 1 
ATOM   3883 C  CZ  . PHE   B 1 228 ? -34.763 -25.061 35.087 1.00 17.23 ? 228 PHE   A CZ  1 
ATOM   3884 N  N   . ARG   B 1 229 ? -39.154 -28.789 39.634 1.00 15.84 ? 229 ARG   A N   1 
ATOM   3885 C  CA  . ARG   B 1 229 ? -40.054 -29.829 40.114 1.00 15.42 ? 229 ARG   A CA  1 
ATOM   3886 C  C   . ARG   B 1 229 ? -41.465 -29.306 40.390 1.00 18.07 ? 229 ARG   A C   1 
ATOM   3887 O  O   . ARG   B 1 229 ? -42.364 -30.135 40.663 1.00 17.80 ? 229 ARG   A O   1 
ATOM   3888 C  CB  . ARG   B 1 229 ? -39.463 -30.410 41.410 1.00 16.19 ? 229 ARG   A CB  1 
ATOM   3889 C  CG  . ARG   B 1 229 ? -38.096 -31.067 41.247 1.00 14.98 ? 229 ARG   A CG  1 
ATOM   3890 C  CD  . ARG   B 1 229 ? -37.763 -32.032 42.419 1.00 14.14 ? 229 ARG   A CD  1 
ATOM   3891 N  NE  . ARG   B 1 229 ? -36.373 -32.467 42.388 1.00 13.85 ? 229 ARG   A NE  1 
ATOM   3892 C  CZ  . ARG   B 1 229 ? -35.336 -31.809 42.877 1.00 15.30 ? 229 ARG   A CZ  1 
ATOM   3893 N  NH1 . ARG   B 1 229 ? -35.545 -30.777 43.707 1.00 16.38 ? 229 ARG   A NH1 1 
ATOM   3894 N  NH2 . ARG   B 1 229 ? -34.113 -32.316 42.744 1.00 15.43 ? 229 ARG   A NH2 1 
ATOM   3895 N  N   . SER   B 1 230 ? -41.642 -27.975 40.412 1.00 17.87 ? 230 SER   A N   1 
ATOM   3896 C  CA  . SER   B 1 230 ? -42.976 -27.397 40.586 1.00 21.84 ? 230 SER   A CA  1 
ATOM   3897 C  C   . SER   B 1 230 ? -43.780 -27.289 39.289 1.00 19.75 ? 230 SER   A C   1 
ATOM   3898 O  O   . SER   B 1 230 ? -44.944 -26.895 39.315 1.00 20.57 ? 230 SER   A O   1 
ATOM   3899 C  CB  . SER   B 1 230 ? -42.885 -26.073 41.329 1.00 26.70 ? 230 SER   A CB  1 
ATOM   3900 O  OG  . SER   B 1 230 ? -42.844 -26.365 42.727 1.00 31.61 ? 230 SER   A OG  1 
ATOM   3901 N  N   . LEU   B 1 231 ? -43.166 -27.601 38.136 1.00 18.25 ? 231 LEU   A N   1 
ATOM   3902 C  CA  . LEU   B 1 231 ? -43.964 -27.711 36.921 1.00 18.21 ? 231 LEU   A CA  1 
ATOM   3903 C  C   . LEU   B 1 231 ? -44.993 -28.833 37.068 1.00 18.32 ? 231 LEU   A C   1 
ATOM   3904 O  O   . LEU   B 1 231 ? -44.748 -29.835 37.758 1.00 16.40 ? 231 LEU   A O   1 
ATOM   3905 C  CB  . LEU   B 1 231 ? -43.044 -28.021 35.732 1.00 16.90 ? 231 LEU   A CB  1 
ATOM   3906 C  CG  . LEU   B 1 231 ? -42.102 -26.896 35.343 1.00 17.03 ? 231 LEU   A CG  1 
ATOM   3907 C  CD1 . LEU   B 1 231 ? -41.095 -27.426 34.349 1.00 16.89 ? 231 LEU   A CD1 1 
ATOM   3908 C  CD2 . LEU   B 1 231 ? -42.914 -25.710 34.751 1.00 17.38 ? 231 LEU   A CD2 1 
ATOM   3909 N  N   . LEU   B 1 232 ? -46.163 -28.687 36.410 1.00 16.31 ? 232 LEU   A N   1 
ATOM   3910 C  CA  . LEU   B 1 232 ? -47.154 -29.749 36.451 1.00 16.07 ? 232 LEU   A CA  1 
ATOM   3911 C  C   . LEU   B 1 232 ? -47.068 -30.652 35.225 1.00 16.77 ? 232 LEU   A C   1 
ATOM   3912 O  O   . LEU   B 1 232 ? -46.685 -30.199 34.135 1.00 18.50 ? 232 LEU   A O   1 
ATOM   3913 C  CB  . LEU   B 1 232 ? -48.555 -29.128 36.564 1.00 18.34 ? 232 LEU   A CB  1 
ATOM   3914 C  CG  . LEU   B 1 232 ? -48.722 -28.173 37.743 1.00 19.76 ? 232 LEU   A CG  1 
ATOM   3915 C  CD1 . LEU   B 1 232 ? -50.160 -27.623 37.745 1.00 23.11 ? 232 LEU   A CD1 1 
ATOM   3916 C  CD2 . LEU   B 1 232 ? -48.501 -28.941 39.030 1.00 21.42 ? 232 LEU   A CD2 1 
ATOM   3917 N  N   . CYS   B 1 233 ? -47.485 -31.906 35.355 1.00 17.57 ? 233 CYS   A N   1 
ATOM   3918 C  CA  . CYS   B 1 233 ? -47.663 -32.785 34.222 1.00 16.99 ? 233 CYS   A CA  1 
ATOM   3919 C  C   . CYS   B 1 233 ? -49.122 -32.811 33.785 1.00 21.17 ? 233 CYS   A C   1 
ATOM   3920 O  O   . CYS   B 1 233 ? -49.482 -33.656 32.959 1.00 23.24 ? 233 CYS   A O   1 
ATOM   3921 C  CB  . CYS   B 1 233 ? -47.138 -34.209 34.435 1.00 18.64 ? 233 CYS   A CB  1 
ATOM   3922 S  SG  . CYS   B 1 233 ? -47.873 -35.083 35.859 1.00 24.03 ? 233 CYS   A SG  1 
ATOM   3923 N  N   . THR   B 1 234 ? -49.907 -31.886 34.342 1.00 18.91 ? 234 THR   A N   1 
ATOM   3924 C  CA  . THR   B 1 234 ? -51.333 -31.826 34.065 1.00 21.59 ? 234 THR   A CA  1 
ATOM   3925 C  C   . THR   B 1 234 ? -51.677 -30.457 33.492 1.00 24.12 ? 234 THR   A C   1 
ATOM   3926 O  O   . THR   B 1 234 ? -51.004 -29.449 33.760 1.00 22.66 ? 234 THR   A O   1 
ATOM   3927 C  CB  . THR   B 1 234 ? -52.084 -32.135 35.367 1.00 21.93 ? 234 THR   A CB  1 
ATOM   3928 O  OG1 . THR   B 1 234 ? -51.580 -31.241 36.370 1.00 21.33 ? 234 THR   A OG1 1 
ATOM   3929 C  CG2 . THR   B 1 234 ? -51.917 -33.582 35.755 1.00 23.25 ? 234 THR   A CG2 1 
ATOM   3930 N  N   . ALA   B 1 235 ? -52.753 -30.452 32.693 1.00 27.60 ? 235 ALA   A N   1 
ATOM   3931 C  CA  . ALA   B 1 235 ? -53.248 -29.229 32.080 1.00 30.96 ? 235 ALA   A CA  1 
ATOM   3932 C  C   . ALA   B 1 235 ? -54.119 -28.462 33.079 1.00 31.49 ? 235 ALA   A C   1 
ATOM   3933 O  O   . ALA   B 1 235 ? -54.506 -28.996 34.108 1.00 32.04 ? 235 ALA   A O   1 
ATOM   3934 C  CB  . ALA   B 1 235 ? -53.994 -29.587 30.809 1.00 31.88 ? 235 ALA   A CB  1 
ATOM   3935 N  N   . GLU   B 1 236 ? -54.367 -27.179 32.802 1.00 32.42 ? 236 GLU   A N   1 
ATOM   3936 C  CA  . GLU   B 1 236 ? -55.246 -26.335 33.605 1.00 43.67 ? 236 GLU   A CA  1 
ATOM   3937 C  C   . GLU   B 1 236 ? -56.618 -27.007 33.685 1.00 43.26 ? 236 GLU   A C   1 
ATOM   3938 O  O   . GLU   B 1 236 ? -57.071 -27.602 32.708 1.00 43.45 ? 236 GLU   A O   1 
ATOM   3939 C  CB  . GLU   B 1 236 ? -55.334 -24.942 32.971 1.00 49.25 ? 236 GLU   A CB  1 
ATOM   3940 C  CG  . GLU   B 1 236 ? -55.613 -23.813 33.953 1.00 58.05 ? 236 GLU   A CG  1 
ATOM   3941 C  CD  . GLU   B 1 236 ? -55.302 -22.414 33.433 1.00 64.98 ? 236 GLU   A CD  1 
ATOM   3942 O  OE1 . GLU   B 1 236 ? -54.510 -21.715 34.095 1.00 66.98 ? 236 GLU   A OE1 1 
ATOM   3943 O  OE2 . GLU   B 1 236 ? -55.837 -22.022 32.363 1.00 65.09 ? 236 GLU   A OE2 1 
ATOM   3944 N  N   . GLY   B 1 237 ? -57.216 -26.986 34.883 1.00 55.44 ? 237 GLY   A N   1 
ATOM   3945 C  CA  . GLY   B 1 237 ? -58.515 -27.599 35.122 1.00 55.56 ? 237 GLY   A CA  1 
ATOM   3946 C  C   . GLY   B 1 237 ? -58.453 -29.079 35.508 1.00 57.95 ? 237 GLY   A C   1 
ATOM   3947 O  O   . GLY   B 1 237 ? -59.441 -29.620 36.000 1.00 64.24 ? 237 GLY   A O   1 
ATOM   3948 N  N   . GLU   B 1 238 ? -57.317 -29.740 35.259 1.00 48.08 ? 238 GLU   A N   1 
ATOM   3949 C  CA  . GLU   B 1 238 ? -57.122 -31.111 35.696 1.00 41.63 ? 238 GLU   A CA  1 
ATOM   3950 C  C   . GLU   B 1 238 ? -56.647 -31.080 37.145 1.00 40.12 ? 238 GLU   A C   1 
ATOM   3951 O  O   . GLU   B 1 238 ? -56.031 -30.111 37.578 1.00 35.12 ? 238 GLU   A O   1 
ATOM   3952 C  CB  . GLU   B 1 238 ? -56.032 -31.777 34.864 1.00 55.18 ? 238 GLU   A CB  1 
ATOM   3953 C  CG  . GLU   B 1 238 ? -56.515 -32.514 33.625 1.00 61.77 ? 238 GLU   A CG  1 
ATOM   3954 C  CD  . GLU   B 1 238 ? -55.424 -33.391 33.016 1.00 69.24 ? 238 GLU   A CD  1 
ATOM   3955 O  OE1 . GLU   B 1 238 ? -54.340 -32.848 32.616 1.00 56.58 ? 238 GLU   A OE1 1 
ATOM   3956 O  OE2 . GLU   B 1 238 ? -55.640 -34.624 32.962 1.00 71.55 ? 238 GLU   A OE2 1 
ATOM   3957 N  N   . ALA   B 1 239 ? -56.947 -32.135 37.903 1.00 35.39 ? 239 ALA   A N   1 
ATOM   3958 C  CA  . ALA   B 1 239 ? -56.392 -32.264 39.237 1.00 33.21 ? 239 ALA   A CA  1 
ATOM   3959 C  C   . ALA   B 1 239 ? -54.864 -32.270 39.069 1.00 29.53 ? 239 ALA   A C   1 
ATOM   3960 O  O   . ALA   B 1 239 ? -54.356 -33.039 38.262 1.00 33.99 ? 239 ALA   A O   1 
ATOM   3961 C  CB  . ALA   B 1 239 ? -56.885 -33.544 39.873 1.00 35.84 ? 239 ALA   A CB  1 
ATOM   3962 N  N   . ALA   B 1 240 ? -54.190 -31.406 39.838 1.00 31.17 ? 240 ALA   A N   1 
ATOM   3963 C  CA  . ALA   B 1 240 ? -52.763 -31.080 39.716 1.00 27.36 ? 240 ALA   A CA  1 
ATOM   3964 C  C   . ALA   B 1 240 ? -51.906 -32.295 40.067 1.00 26.26 ? 240 ALA   A C   1 
ATOM   3965 O  O   . ALA   B 1 240 ? -52.123 -32.916 41.113 1.00 28.01 ? 240 ALA   A O   1 
ATOM   3966 C  CB  . ALA   B 1 240 ? -52.423 -29.923 40.636 1.00 30.94 ? 240 ALA   A CB  1 
ATOM   3967 N  N   . ALA   B 1 241 ? -50.923 -32.632 39.203 1.00 20.19 ? 241 ALA   A N   1 
ATOM   3968 C  CA  . ALA   B 1 241 ? -49.860 -33.565 39.570 1.00 17.17 ? 241 ALA   A CA  1 
ATOM   3969 C  C   . ALA   B 1 241 ? -48.539 -32.937 39.122 1.00 17.62 ? 241 ALA   A C   1 
ATOM   3970 O  O   . ALA   B 1 241 ? -48.524 -32.293 38.088 1.00 18.80 ? 241 ALA   A O   1 
ATOM   3971 C  CB  . ALA   B 1 241 ? -50.039 -34.874 38.920 1.00 19.24 ? 241 ALA   A CB  1 
ATOM   3972 N  N   . PHE   B 1 242 ? -47.484 -33.119 39.931 1.00 17.48 ? 242 PHE   A N   1 
ATOM   3973 C  CA  . PHE   B 1 242 ? -46.233 -32.411 39.712 1.00 16.73 ? 242 PHE   A CA  1 
ATOM   3974 C  C   . PHE   B 1 242 ? -45.198 -33.299 39.024 1.00 17.05 ? 242 PHE   A C   1 
ATOM   3975 O  O   . PHE   B 1 242 ? -45.132 -34.524 39.213 1.00 20.25 ? 242 PHE   A O   1 
ATOM   3976 C  CB  . PHE   B 1 242 ? -45.621 -32.008 41.056 1.00 18.09 ? 242 PHE   A CB  1 
ATOM   3977 C  CG  . PHE   B 1 242 ? -46.421 -30.963 41.771 1.00 17.21 ? 242 PHE   A CG  1 
ATOM   3978 C  CD1 . PHE   B 1 242 ? -46.232 -29.612 41.519 1.00 18.66 ? 242 PHE   A CD1 1 
ATOM   3979 C  CD2 . PHE   B 1 242 ? -47.427 -31.367 42.658 1.00 19.40 ? 242 PHE   A CD2 1 
ATOM   3980 C  CE1 . PHE   B 1 242 ? -46.979 -28.659 42.201 1.00 23.31 ? 242 PHE   A CE1 1 
ATOM   3981 C  CE2 . PHE   B 1 242 ? -48.181 -30.397 43.313 1.00 25.18 ? 242 PHE   A CE2 1 
ATOM   3982 C  CZ  . PHE   B 1 242 ? -47.956 -29.056 43.078 1.00 24.14 ? 242 PHE   A CZ  1 
ATOM   3983 N  N   . LEU   B 1 243 ? -44.324 -32.616 38.276 1.00 16.43 ? 243 LEU   A N   1 
ATOM   3984 C  CA  . LEU   B 1 243 ? -43.269 -33.299 37.532 1.00 16.42 ? 243 LEU   A CA  1 
ATOM   3985 C  C   . LEU   B 1 243 ? -42.010 -33.299 38.396 1.00 15.06 ? 243 LEU   A C   1 
ATOM   3986 O  O   . LEU   B 1 243 ? -41.032 -32.608 38.101 1.00 15.42 ? 243 LEU   A O   1 
ATOM   3987 C  CB  . LEU   B 1 243 ? -43.090 -32.454 36.257 1.00 17.16 ? 243 LEU   A CB  1 
ATOM   3988 C  CG  . LEU   B 1 243 ? -42.175 -33.040 35.185 1.00 18.38 ? 243 LEU   A CG  1 
ATOM   3989 C  CD1 . LEU   B 1 243 ? -42.675 -34.418 34.725 1.00 17.36 ? 243 LEU   A CD1 1 
ATOM   3990 C  CD2 . LEU   B 1 243 ? -42.140 -32.069 33.998 1.00 21.39 ? 243 LEU   A CD2 1 
ATOM   3991 N  N   . VAL   B 1 244 ? -42.031 -34.090 39.496 1.00 14.10 ? 244 VAL   A N   1 
ATOM   3992 C  CA  . VAL   B 1 244 ? -40.917 -34.054 40.438 1.00 14.23 ? 244 VAL   A CA  1 
ATOM   3993 C  C   . VAL   B 1 244 ? -39.767 -34.900 39.908 1.00 12.58 ? 244 VAL   A C   1 
ATOM   3994 O  O   . VAL   B 1 244 ? -38.647 -34.698 40.392 1.00 13.55 ? 244 VAL   A O   1 
ATOM   3995 C  CB  . VAL   B 1 244 ? -41.257 -34.513 41.873 1.00 18.40 ? 244 VAL   A CB  1 
ATOM   3996 C  CG1 . VAL   B 1 244 ? -42.311 -33.616 42.467 1.00 19.84 ? 244 VAL   A CG1 1 
ATOM   3997 C  CG2 . VAL   B 1 244 ? -41.713 -35.970 41.903 1.00 19.02 ? 244 VAL   A CG2 1 
ATOM   3998 N  N   . SER   B 1 245 ? -40.036 -35.796 38.938 1.00 13.16 ? 245 SER   A N   1 
ATOM   3999 C  CA  . SER   B 1 245 ? -38.953 -36.631 38.384 1.00 13.33 ? 245 SER   A CA  1 
ATOM   4000 C  C   . SER   B 1 245 ? -39.264 -37.005 36.927 1.00 12.19 ? 245 SER   A C   1 
ATOM   4001 O  O   . SER   B 1 245 ? -40.409 -37.311 36.606 1.00 14.66 ? 245 SER   A O   1 
ATOM   4002 C  CB  . SER   B 1 245 ? -38.738 -37.875 39.224 1.00 16.17 ? 245 SER   A CB  1 
ATOM   4003 O  OG  . SER   B 1 245 ? -37.681 -38.739 38.760 1.00 17.48 ? 245 SER   A OG  1 
ATOM   4004 N  N   . ASN   B 1 246 ? -38.272 -36.893 36.038 1.00 12.03 ? 246 ASN   A N   1 
ATOM   4005 C  CA  . ASN   B 1 246 ? -38.561 -37.139 34.644 1.00 11.86 ? 246 ASN   A CA  1 
ATOM   4006 C  C   . ASN   B 1 246 ? -37.353 -37.775 33.936 1.00 11.33 ? 246 ASN   A C   1 
ATOM   4007 O  O   . ASN   B 1 246 ? -37.120 -37.489 32.759 1.00 13.89 ? 246 ASN   A O   1 
ATOM   4008 C  CB  . ASN   B 1 246 ? -39.050 -35.871 33.952 1.00 12.08 ? 246 ASN   A CB  1 
ATOM   4009 C  CG  . ASN   B 1 246 ? -37.970 -34.808 33.876 1.00 12.87 ? 246 ASN   A CG  1 
ATOM   4010 O  OD1 . ASN   B 1 246 ? -36.917 -34.957 34.503 1.00 13.44 ? 246 ASN   A OD1 1 
ATOM   4011 N  ND2 . ASN   B 1 246 ? -38.227 -33.746 33.109 1.00 13.17 ? 246 ASN   A ND2 1 
ATOM   4012 N  N   . HIS   B 1 247 ? -36.642 -38.694 34.607 1.00 11.13 ? 247 HIS   A N   1 
ATOM   4013 C  CA  . HIS   B 1 247 ? -35.511 -39.396 33.987 1.00 12.16 ? 247 HIS   A CA  1 
ATOM   4014 C  C   . HIS   B 1 247 ? -35.844 -40.888 33.859 1.00 13.31 ? 247 HIS   A C   1 
ATOM   4015 O  O   . HIS   B 1 247 ? -36.410 -41.489 34.771 1.00 17.33 ? 247 HIS   A O   1 
ATOM   4016 C  CB  . HIS   B 1 247 ? -34.208 -39.187 34.798 1.00 13.43 ? 247 HIS   A CB  1 
ATOM   4017 C  CG  . HIS   B 1 247 ? -34.247 -39.705 36.212 1.00 14.97 ? 247 HIS   A CG  1 
ATOM   4018 N  ND1 . HIS   B 1 247 ? -33.555 -40.852 36.614 1.00 19.81 ? 247 HIS   A ND1 1 
ATOM   4019 C  CD2 . HIS   B 1 247 ? -34.878 -39.246 37.311 1.00 15.54 ? 247 HIS   A CD2 1 
ATOM   4020 C  CE1 . HIS   B 1 247 ? -33.790 -41.082 37.907 1.00 21.04 ? 247 HIS   A CE1 1 
ATOM   4021 N  NE2 . HIS   B 1 247 ? -34.603 -40.144 38.350 1.00 18.03 ? 247 HIS   A NE2 1 
ATOM   4022 N  N   . ARG   B 1 248 ? -35.326 -41.493 32.787 1.00 13.25 ? 248 ARG   A N   1 
ATOM   4023 C  CA  . ARG   B 1 248 ? -35.434 -42.926 32.539 1.00 12.33 ? 248 ARG   A CA  1 
ATOM   4024 C  C   . ARG   B 1 248 ? -34.166 -43.569 33.091 1.00 13.45 ? 248 ARG   A C   1 
ATOM   4025 O  O   . ARG   B 1 248 ? -33.041 -43.068 32.919 1.00 15.30 ? 248 ARG   A O   1 
ATOM   4026 C  CB  . ARG   B 1 248 ? -35.531 -43.132 31.009 1.00 12.72 ? 248 ARG   A CB  1 
ATOM   4027 C  CG  . ARG   B 1 248 ? -35.740 -44.620 30.701 1.00 12.02 ? 248 ARG   A CG  1 
ATOM   4028 C  CD  . ARG   B 1 248 ? -35.666 -44.920 29.210 1.00 13.83 ? 248 ARG   A CD  1 
ATOM   4029 N  NE  . ARG   B 1 248 ? -36.204 -46.282 28.933 1.00 15.50 ? 248 ARG   A NE  1 
ATOM   4030 C  CZ  . ARG   B 1 248 ? -35.978 -46.983 27.812 1.00 14.02 ? 248 ARG   A CZ  1 
ATOM   4031 N  NH1 . ARG   B 1 248 ? -35.152 -46.539 26.876 1.00 14.86 ? 248 ARG   A NH1 1 
ATOM   4032 N  NH2 . ARG   B 1 248 ? -36.597 -48.144 27.652 1.00 16.07 ? 248 ARG   A NH2 1 
ATOM   4033 N  N   . PRO   B 1 249 ? -34.297 -44.692 33.839 1.00 14.23 ? 249 PRO   A N   1 
ATOM   4034 C  CA  . PRO   B 1 249 ? -33.100 -45.389 34.318 1.00 16.11 ? 249 PRO   A CA  1 
ATOM   4035 C  C   . PRO   B 1 249 ? -32.262 -45.868 33.139 1.00 15.88 ? 249 PRO   A C   1 
ATOM   4036 O  O   . PRO   B 1 249 ? -32.781 -46.120 32.035 1.00 16.13 ? 249 PRO   A O   1 
ATOM   4037 C  CB  . PRO   B 1 249 ? -33.677 -46.630 35.017 1.00 19.83 ? 249 PRO   A CB  1 
ATOM   4038 C  CG  . PRO   B 1 249 ? -35.071 -46.182 35.453 1.00 19.38 ? 249 PRO   A CG  1 
ATOM   4039 C  CD  . PRO   B 1 249 ? -35.559 -45.300 34.295 1.00 16.98 ? 249 PRO   A CD  1 
ATOM   4040 N  N   . PRO   B 1 250 ? -30.935 -46.007 33.340 1.00 15.34 ? 250 PRO   A N   1 
ATOM   4041 C  CA  . PRO   B 1 250 ? -30.036 -46.598 32.346 1.00 16.43 ? 250 PRO   A CA  1 
ATOM   4042 C  C   . PRO   B 1 250 ? -30.465 -48.001 31.926 1.00 14.65 ? 250 PRO   A C   1 
ATOM   4043 O  O   . PRO   B 1 250 ? -30.953 -48.801 32.748 1.00 16.78 ? 250 PRO   A O   1 
ATOM   4044 C  CB  . PRO   B 1 250 ? -28.652 -46.604 33.042 1.00 19.58 ? 250 PRO   A CB  1 
ATOM   4045 C  CG  . PRO   B 1 250 ? -28.763 -45.526 34.090 1.00 21.41 ? 250 PRO   A CG  1 
ATOM   4046 C  CD  . PRO   B 1 250 ? -30.219 -45.538 34.534 1.00 20.21 ? 250 PRO   A CD  1 
ATOM   4047 N  N   . GLN   B 1 251 ? -30.296 -48.245 30.636 1.00 12.89 ? 251 GLN   A N   1 
ATOM   4048 C  CA  . GLN   B 1 251 ? -30.620 -49.513 29.994 1.00 14.36 ? 251 GLN   A CA  1 
ATOM   4049 C  C   . GLN   B 1 251 ? -29.317 -50.240 29.647 1.00 16.30 ? 251 GLN   A C   1 
ATOM   4050 O  O   . GLN   B 1 251 ? -28.271 -49.623 29.580 1.00 14.91 ? 251 GLN   A O   1 
ATOM   4051 C  CB  . GLN   B 1 251 ? -31.360 -49.236 28.686 1.00 16.67 ? 251 GLN   A CB  1 
ATOM   4052 C  CG  . GLN   B 1 251 ? -32.646 -48.427 28.939 1.00 17.51 ? 251 GLN   A CG  1 
ATOM   4053 C  CD  . GLN   B 1 251 ? -33.559 -49.051 29.978 1.00 21.21 ? 251 GLN   A CD  1 
ATOM   4054 O  OE1 . GLN   B 1 251 ? -33.955 -48.435 30.980 1.00 21.92 ? 251 GLN   A OE1 1 
ATOM   4055 N  NE2 . GLN   B 1 251 ? -33.890 -50.322 29.777 1.00 17.14 ? 251 GLN   A NE2 1 
ATOM   4056 N  N   . PRO   B 1 252 ? -29.328 -51.581 29.434 1.00 16.36 ? 252 PRO   A N   1 
ATOM   4057 C  CA  . PRO   B 1 252 ? -28.045 -52.288 29.271 1.00 17.37 ? 252 PRO   A CA  1 
ATOM   4058 C  C   . PRO   B 1 252 ? -27.335 -51.939 27.955 1.00 18.22 ? 252 PRO   A C   1 
ATOM   4059 O  O   . PRO   B 1 252 ? -27.977 -51.691 26.926 1.00 16.46 ? 252 PRO   A O   1 
ATOM   4060 C  CB  . PRO   B 1 252 ? -28.460 -53.773 29.321 1.00 18.62 ? 252 PRO   A CB  1 
ATOM   4061 C  CG  . PRO   B 1 252 ? -29.896 -53.798 29.848 1.00 20.85 ? 252 PRO   A CG  1 
ATOM   4062 C  CD  . PRO   B 1 252 ? -30.520 -52.444 29.541 1.00 19.85 ? 252 PRO   A CD  1 
ATOM   4063 N  N   . LEU   B 1 253 ? -26.000 -51.958 27.958 1.00 18.66 ? 253 LEU   A N   1 
ATOM   4064 C  CA  . LEU   B 1 253 ? -25.232 -51.576 26.773 1.00 18.30 ? 253 LEU   A CA  1 
ATOM   4065 C  C   . LEU   B 1 253 ? -25.403 -52.596 25.634 1.00 17.35 ? 253 LEU   A C   1 
ATOM   4066 O  O   . LEU   B 1 253 ? -25.337 -52.241 24.452 1.00 18.58 ? 253 LEU   A O   1 
ATOM   4067 C  CB  . LEU   B 1 253 ? -23.733 -51.430 27.141 1.00 22.39 ? 253 LEU   A CB  1 
ATOM   4068 C  CG  . LEU   B 1 253 ? -23.105 -50.026 27.242 1.00 33.05 ? 253 LEU   A CG  1 
ATOM   4069 C  CD1 . LEU   B 1 253 ? -21.591 -50.150 27.381 1.00 35.84 ? 253 LEU   A CD1 1 
ATOM   4070 C  CD2 . LEU   B 1 253 ? -23.421 -49.108 26.053 1.00 25.25 ? 253 LEU   A CD2 1 
ATOM   4071 N  N   . LYS   B 1 254 ? -25.625 -53.875 25.952 1.00 17.16 ? 254 LYS   A N   1 
ATOM   4072 C  CA  . LYS   B 1 254 ? -25.917 -54.869 24.919 1.00 18.14 ? 254 LYS   A CA  1 
ATOM   4073 C  C   . LYS   B 1 254 ? -24.844 -54.887 23.828 1.00 18.61 ? 254 LYS   A C   1 
ATOM   4074 O  O   . LYS   B 1 254 ? -25.134 -54.907 22.630 1.00 21.26 ? 254 LYS   A O   1 
ATOM   4075 C  CB  . LYS   B 1 254 ? -27.359 -54.727 24.397 1.00 19.85 ? 254 LYS   A CB  1 
ATOM   4076 C  CG  . LYS   B 1 254 ? -28.383 -55.144 25.450 1.00 22.46 ? 254 LYS   A CG  1 
ATOM   4077 C  CD  . LYS   B 1 254 ? -29.735 -55.323 24.835 1.00 25.57 ? 254 LYS   A CD  1 
ATOM   4078 C  CE  . LYS   B 1 254 ? -30.814 -55.370 25.906 1.00 27.34 ? 254 LYS   A CE  1 
ATOM   4079 N  NZ  . LYS   B 1 254 ? -32.193 -55.590 25.367 1.00 29.91 ? 254 LYS   A NZ  1 
ATOM   4080 N  N   . GLY   B 1 255 ? -23.560 -54.834 24.226 1.00 18.44 ? 255 GLY   A N   1 
ATOM   4081 C  CA  . GLY   B 1 255 ? -22.545 -54.989 23.176 1.00 18.46 ? 255 GLY   A CA  1 
ATOM   4082 C  C   . GLY   B 1 255 ? -22.024 -53.699 22.514 1.00 18.44 ? 255 GLY   A C   1 
ATOM   4083 O  O   . GLY   B 1 255 ? -20.986 -53.705 21.840 1.00 20.83 ? 255 GLY   A O   1 
ATOM   4084 N  N   . ARG   B 1 256 ? -22.737 -52.570 22.664 1.00 18.31 ? 256 ARG   A N   1 
ATOM   4085 C  CA  . ARG   B 1 256 ? -22.220 -51.312 22.123 1.00 17.12 ? 256 ARG   A CA  1 
ATOM   4086 C  C   . ARG   B 1 256 ? -20.939 -50.885 22.836 1.00 20.38 ? 256 ARG   A C   1 
ATOM   4087 O  O   . ARG   B 1 256 ? -20.789 -51.125 24.034 1.00 23.78 ? 256 ARG   A O   1 
ATOM   4088 C  CB  . ARG   B 1 256 ? -23.292 -50.221 22.292 1.00 17.46 ? 256 ARG   A CB  1 
ATOM   4089 C  CG  . ARG   B 1 256 ? -24.528 -50.506 21.459 1.00 15.91 ? 256 ARG   A CG  1 
ATOM   4090 C  CD  . ARG   B 1 256 ? -25.650 -49.526 21.829 1.00 15.88 ? 256 ARG   A CD  1 
ATOM   4091 N  NE  . ARG   B 1 256 ? -26.260 -49.867 23.105 1.00 14.26 ? 256 ARG   A NE  1 
ATOM   4092 C  CZ  . ARG   B 1 256 ? -27.222 -49.141 23.695 1.00 14.49 ? 256 ARG   A CZ  1 
ATOM   4093 N  NH1 . ARG   B 1 256 ? -27.607 -47.988 23.170 1.00 13.60 ? 256 ARG   A NH1 1 
ATOM   4094 N  NH2 . ARG   B 1 256 ? -27.753 -49.540 24.838 1.00 14.00 ? 256 ARG   A NH2 1 
ATOM   4095 N  N   . LYS   B 1 257 ? -20.110 -50.094 22.151 1.00 21.02 ? 257 LYS   A N   1 
ATOM   4096 C  CA  . LYS   B 1 257 ? -18.962 -49.495 22.824 1.00 23.45 ? 257 LYS   A CA  1 
ATOM   4097 C  C   . LYS   B 1 257 ? -19.121 -47.984 22.896 1.00 21.36 ? 257 LYS   A C   1 
ATOM   4098 O  O   . LYS   B 1 257 ? -19.613 -47.335 21.964 1.00 26.58 ? 257 LYS   A O   1 
ATOM   4099 C  CB  . LYS   B 1 257 ? -17.647 -49.852 22.133 1.00 31.84 ? 257 LYS   A CB  1 
ATOM   4100 C  CG  . LYS   B 1 257 ? -17.379 -51.351 22.082 1.00 36.05 ? 257 LYS   A CG  1 
ATOM   4101 C  CD  . LYS   B 1 257 ? -15.938 -51.712 21.823 1.00 38.15 ? 257 LYS   A CD  1 
ATOM   4102 C  CE  . LYS   B 1 257 ? -15.785 -53.178 21.472 1.00 40.50 ? 257 LYS   A CE  1 
ATOM   4103 N  NZ  . LYS   B 1 257 ? -14.538 -53.391 20.698 1.00 47.64 ? 257 LYS   A NZ  1 
ATOM   4104 N  N   . VAL   B 1 258 ? -18.743 -47.464 24.045 1.00 19.02 ? 258 VAL   A N   1 
ATOM   4105 C  CA  . VAL   B 1 258 ? -18.719 -46.042 24.231 1.00 16.72 ? 258 VAL   A CA  1 
ATOM   4106 C  C   . VAL   B 1 258 ? -17.352 -45.589 23.755 1.00 18.20 ? 258 VAL   A C   1 
ATOM   4107 O  O   . VAL   B 1 258 ? -16.360 -46.177 24.169 1.00 21.00 ? 258 VAL   A O   1 
ATOM   4108 C  CB  . VAL   B 1 258 ? -18.959 -45.671 25.683 1.00 16.34 ? 258 VAL   A CB  1 
ATOM   4109 C  CG1 . VAL   B 1 258 ? -18.863 -44.171 25.821 1.00 16.88 ? 258 VAL   A CG1 1 
ATOM   4110 C  CG2 . VAL   B 1 258 ? -20.332 -46.171 26.117 1.00 18.42 ? 258 VAL   A CG2 1 
ATOM   4111 N  N   . ARG   B 1 259 ? -17.342 -44.630 22.826 1.00 15.96 ? 259 ARG   A N   1 
ATOM   4112 C  CA  . ARG   B 1 259 ? -16.078 -44.155 22.268 1.00 16.84 ? 259 ARG   A CA  1 
ATOM   4113 C  C   . ARG   B 1 259 ? -15.758 -42.757 22.773 1.00 18.26 ? 259 ARG   A C   1 
ATOM   4114 O  O   . ARG   B 1 259 ? -16.636 -41.966 23.094 1.00 17.10 ? 259 ARG   A O   1 
ATOM   4115 C  CB  . ARG   B 1 259 ? -16.048 -44.177 20.728 1.00 17.10 ? 259 ARG   A CB  1 
ATOM   4116 C  CG  . ARG   B 1 259 ? -16.201 -45.576 20.131 1.00 20.26 ? 259 ARG   A CG  1 
ATOM   4117 C  CD  . ARG   B 1 259 ? -16.106 -45.436 18.610 1.00 22.93 ? 259 ARG   A CD  1 
ATOM   4118 N  NE  . ARG   B 1 259 ? -17.313 -44.814 18.039 1.00 23.66 ? 259 ARG   A NE  1 
ATOM   4119 C  CZ  . ARG   B 1 259 ? -17.373 -44.036 16.949 1.00 27.19 ? 259 ARG   A CZ  1 
ATOM   4120 N  NH1 . ARG   B 1 259 ? -16.288 -43.774 16.229 1.00 27.93 ? 259 ARG   A NH1 1 
ATOM   4121 N  NH2 . ARG   B 1 259 ? -18.545 -43.547 16.563 1.00 23.16 ? 259 ARG   A NH2 1 
ATOM   4122 N  N   . ALA   B 1 260 ? -14.454 -42.457 22.843 1.00 17.28 ? 260 ALA   A N   1 
ATOM   4123 C  CA  . ALA   B 1 260 ? -14.087 -41.077 23.115 1.00 20.30 ? 260 ALA   A CA  1 
ATOM   4124 C  C   . ALA   B 1 260 ? -13.021 -40.562 22.172 1.00 24.74 ? 260 ALA   A C   1 
ATOM   4125 O  O   . ALA   B 1 260 ? -12.373 -41.334 21.469 1.00 23.76 ? 260 ALA   A O   1 
ATOM   4126 C  CB  . ALA   B 1 260 ? -13.639 -40.897 24.500 1.00 19.72 ? 260 ALA   A CB  1 
ATOM   4127 N  N   . SER   B 1 261 ? -12.854 -39.239 22.345 1.00 37.64 ? 261 SER   A N   1 
ATOM   4128 C  CA  . SER   B 1 261 ? -12.187 -38.253 21.514 1.00 51.93 ? 261 SER   A CA  1 
ATOM   4129 C  C   . SER   B 1 261 ? -10.814 -37.946 22.117 1.00 54.95 ? 261 SER   A C   1 
ATOM   4130 O  O   . SER   B 1 261 ? -10.807 -37.249 23.165 1.00 67.84 ? 261 SER   A O   1 
ATOM   4131 C  CB  . SER   B 1 261 ? -13.039 -36.986 21.475 1.00 47.09 ? 261 SER   A CB  1 
ATOM   4132 O  OG  . SER   B 1 261 ? -13.794 -36.801 22.685 1.00 33.56 ? 261 SER   A OG  1 
HETATM 4133 ZN ZN  . ZN    C 2 .   ? -6.878  -4.165  13.470 1.00 12.95 ? 301 ZN    B ZN  1 
HETATM 4134 C  C1  . A1IEL D 3 .   ? -7.348  -0.045  14.224 1.00 28.91 ? 302 A1IEL B C1  1 
HETATM 4135 C  C2  . A1IEL D 3 .   ? -6.705  -1.238  14.534 1.00 29.49 ? 302 A1IEL B C2  1 
HETATM 4136 C  C3  . A1IEL D 3 .   ? -6.814  -1.758  15.856 1.00 29.32 ? 302 A1IEL B C3  1 
HETATM 4137 C  C4  . A1IEL D 3 .   ? -7.603  -1.011  16.806 1.00 32.49 ? 302 A1IEL B C4  1 
HETATM 4138 C  C5  . A1IEL D 3 .   ? -8.234  0.236   16.478 1.00 30.22 ? 302 A1IEL B C5  1 
HETATM 4139 C  C6  . A1IEL D 3 .   ? -8.133  0.701   15.169 1.00 30.08 ? 302 A1IEL B C6  1 
HETATM 4140 C  C9  . A1IEL D 3 .   ? -6.161  0.689   10.738 1.00 16.38 ? 302 A1IEL B C9  1 
HETATM 4141 C  C16 . A1IEL D 3 .   ? -8.741  -0.434  19.275 1.00 41.24 ? 302 A1IEL B C16 1 
HETATM 4142 C  C20 . A1IEL D 3 .   ? -6.623  1.025   19.535 1.00 52.70 ? 302 A1IEL B C20 1 
HETATM 4143 O  O14 . A1IEL D 3 .   ? -4.783  -3.283  16.896 1.00 23.21 ? 302 A1IEL B O14 1 
HETATM 4144 S  S11 . A1IEL D 3 .   ? -5.987  -3.361  16.099 1.00 32.26 ? 302 A1IEL B S11 1 
HETATM 4145 O  O12 . A1IEL D 3 .   ? -6.898  -4.533  16.334 1.00 28.87 ? 302 A1IEL B O12 1 
HETATM 4146 N  N13 . A1IEL D 3 .   ? -5.404  -3.593  14.405 1.00 27.93 ? 302 A1IEL B N13 1 
HETATM 4147 C  C7  . A1IEL D 3 .   ? -7.224  0.489   12.920 1.00 27.57 ? 302 A1IEL B C7  1 
HETATM 4148 O  O10 . A1IEL D 3 .   ? -7.647  1.615   12.833 1.00 35.40 ? 302 A1IEL B O10 1 
HETATM 4149 O  O8  . A1IEL D 3 .   ? -6.601  -0.120  11.870 1.00 31.76 ? 302 A1IEL B O8  1 
HETATM 4150 S  S15 . A1IEL D 3 .   ? -7.760  -1.739  18.417 1.00 36.80 ? 302 A1IEL B S15 1 
HETATM 4151 C  C17 . A1IEL D 3 .   ? -7.999  0.784   19.786 1.00 49.73 ? 302 A1IEL B C17 1 
HETATM 4152 C  C21 . A1IEL D 3 .   ? -5.988  2.183   20.028 1.00 57.90 ? 302 A1IEL B C21 1 
HETATM 4153 C  C22 . A1IEL D 3 .   ? -6.724  3.118   20.772 1.00 60.71 ? 302 A1IEL B C22 1 
HETATM 4154 C  C19 . A1IEL D 3 .   ? -8.095  2.890   21.019 1.00 57.63 ? 302 A1IEL B C19 1 
HETATM 4155 C  C18 . A1IEL D 3 .   ? -8.736  1.737   20.527 1.00 52.96 ? 302 A1IEL B C18 1 
HETATM 4156 ZN ZN  . ZN    E 2 .   ? -33.827 -35.941 26.942 1.00 12.47 ? 301 ZN    A ZN  1 
HETATM 4157 C  C1  . A1IEL F 3 .   ? -38.025 -35.267 26.100 1.00 20.77 ? 302 A1IEL A C1  1 
HETATM 4158 C  C2  . A1IEL F 3 .   ? -36.873 -36.062 25.946 1.00 21.84 ? 302 A1IEL A C2  1 
HETATM 4159 C  C3  . A1IEL F 3 .   ? -36.346 -36.221 24.638 1.00 19.99 ? 302 A1IEL A C3  1 
HETATM 4160 C  C4  . A1IEL F 3 .   ? -37.035 -35.607 23.552 1.00 26.93 ? 302 A1IEL A C4  1 
HETATM 4161 C  C5  . A1IEL F 3 .   ? -38.194 -34.827 23.731 1.00 23.22 ? 302 A1IEL A C5  1 
HETATM 4162 C  C6  . A1IEL F 3 .   ? -38.682 -34.668 25.020 1.00 23.34 ? 302 A1IEL A C6  1 
HETATM 4163 C  C9  . A1IEL F 3 .   ? -38.643 -35.872 29.759 1.00 20.57 ? 302 A1IEL A C9  1 
HETATM 4164 C  C16 . A1IEL F 3 .   ? -37.692 -34.960 20.914 1.00 32.55 ? 302 A1IEL A C16 1 
HETATM 4165 C  C20 . A1IEL F 3 .   ? -39.265 -37.011 21.281 1.00 33.48 ? 302 A1IEL A C20 1 
HETATM 4166 O  O14 . A1IEL F 3 .   ? -35.110 -38.480 23.912 1.00 21.43 ? 302 A1IEL A O14 1 
HETATM 4167 S  S11 . A1IEL F 3 .   ? -34.814 -37.175 24.486 1.00 25.92 ? 302 A1IEL A S11 1 
HETATM 4168 O  O12 . A1IEL F 3 .   ? -33.715 -36.392 23.831 1.00 25.16 ? 302 A1IEL A O12 1 
HETATM 4169 N  N13 . A1IEL F 3 .   ? -34.358 -37.371 26.169 1.00 23.29 ? 302 A1IEL A N13 1 
HETATM 4170 C  C7  . A1IEL F 3 .   ? -38.566 -35.063 27.436 1.00 22.03 ? 302 A1IEL A C7  1 
HETATM 4171 O  O10 . A1IEL F 3 .   ? -39.573 -34.386 27.603 1.00 28.02 ? 302 A1IEL A O10 1 
HETATM 4172 O  O8  . A1IEL F 3 .   ? -37.998 -35.689 28.496 1.00 28.08 ? 302 A1IEL A O8  1 
HETATM 4173 S  S15 . A1IEL F 3 .   ? -36.368 -35.810 21.915 1.00 26.29 ? 302 A1IEL A S15 1 
HETATM 4174 C  C17 . A1IEL F 3 .   ? -39.016 -35.717 20.739 1.00 35.63 ? 302 A1IEL A C17 1 
HETATM 4175 C  C21 . A1IEL F 3 .   ? -40.512 -37.660 21.091 1.00 36.23 ? 302 A1IEL A C21 1 
HETATM 4176 C  C22 . A1IEL F 3 .   ? -41.543 -37.018 20.351 1.00 42.79 ? 302 A1IEL A C22 1 
HETATM 4177 C  C19 . A1IEL F 3 .   ? -41.309 -35.724 19.823 1.00 41.31 ? 302 A1IEL A C19 1 
HETATM 4178 C  C18 . A1IEL F 3 .   ? -40.064 -35.096 20.021 1.00 35.84 ? 302 A1IEL A C18 1 
HETATM 4179 O  O   . HOH   G 4 .   ? -28.435 -11.874 9.853  1.00 41.62 ? 401 HOH   B O   1 
HETATM 4180 O  O   . HOH   G 4 .   ? -31.143 -8.446  20.304 1.00 31.84 ? 402 HOH   B O   1 
HETATM 4181 O  O   . HOH   G 4 .   ? -26.700 -13.223 18.893 1.00 27.55 ? 403 HOH   B O   1 
HETATM 4182 O  O   . HOH   G 4 .   ? -10.646 -26.085 16.680 1.00 37.47 ? 404 HOH   B O   1 
HETATM 4183 O  O   . HOH   G 4 .   ? 3.421   -16.812 6.402  1.00 21.53 ? 405 HOH   B O   1 
HETATM 4184 O  O   . HOH   G 4 .   ? -10.125 2.694   13.136 1.00 34.37 ? 406 HOH   B O   1 
HETATM 4185 O  O   . HOH   G 4 .   ? -0.416  -8.138  3.377  1.00 30.87 ? 407 HOH   B O   1 
HETATM 4186 O  O   . HOH   G 4 .   ? -0.602  -7.428  -6.522 1.00 35.13 ? 408 HOH   B O   1 
HETATM 4187 O  O   . HOH   G 4 .   ? -27.445 -12.481 21.781 1.00 45.67 ? 409 HOH   B O   1 
HETATM 4188 O  O   . HOH   G 4 .   ? 8.728   -4.993  15.701 1.00 28.20 ? 410 HOH   B O   1 
HETATM 4189 O  O   . HOH   G 4 .   ? -23.920 -17.587 20.056 1.00 30.56 ? 411 HOH   B O   1 
HETATM 4190 O  O   . HOH   G 4 .   ? 8.283   -5.895  24.521 1.00 32.50 ? 412 HOH   B O   1 
HETATM 4191 O  O   . HOH   G 4 .   ? 1.323   -9.551  24.489 1.00 19.19 ? 413 HOH   B O   1 
HETATM 4192 O  O   . HOH   G 4 .   ? -21.696 -14.974 0.267  1.00 53.69 ? 414 HOH   B O   1 
HETATM 4193 O  O   . HOH   G 4 .   ? 8.426   1.288   12.608 1.00 29.47 ? 415 HOH   B O   1 
HETATM 4194 O  O   . HOH   G 4 .   ? 5.359   -7.602  26.274 1.00 42.26 ? 416 HOH   B O   1 
HETATM 4195 O  O   . HOH   G 4 .   ? 2.844   2.562   23.413 1.00 28.91 ? 417 HOH   B O   1 
HETATM 4196 O  O   . HOH   G 4 .   ? 8.994   -12.329 22.595 1.00 31.04 ? 418 HOH   B O   1 
HETATM 4197 O  O   . HOH   G 4 .   ? -21.763 -6.282  25.667 1.00 18.83 ? 419 HOH   B O   1 
HETATM 4198 O  O   . HOH   G 4 .   ? -26.995 5.614   9.553  1.00 29.28 ? 420 HOH   B O   1 
HETATM 4199 O  O   . HOH   G 4 .   ? -16.536 -18.977 5.128  1.00 39.26 ? 421 HOH   B O   1 
HETATM 4200 O  O   . HOH   G 4 .   ? -3.340  4.498   2.705  1.00 19.99 ? 422 HOH   B O   1 
HETATM 4201 O  O   . HOH   G 4 .   ? -4.833  -10.676 26.441 1.00 20.45 ? 423 HOH   B O   1 
HETATM 4202 O  O   . HOH   G 4 .   ? -3.389  8.412   0.640  1.00 34.78 ? 424 HOH   B O   1 
HETATM 4203 O  O   . HOH   G 4 .   ? 1.943   -26.472 23.436 1.00 52.79 ? 425 HOH   B O   1 
HETATM 4204 O  O   . HOH   G 4 .   ? -17.342 -10.150 29.208 1.00 19.16 ? 426 HOH   B O   1 
HETATM 4205 O  O   . HOH   G 4 .   ? -22.864 -0.522  -0.684 1.00 35.24 ? 427 HOH   B O   1 
HETATM 4206 O  O   . HOH   G 4 .   ? -25.570 -6.757  5.389  1.00 35.27 ? 428 HOH   B O   1 
HETATM 4207 O  O   . HOH   G 4 .   ? -29.103 -14.535 12.755 1.00 37.78 ? 429 HOH   B O   1 
HETATM 4208 O  O   . HOH   G 4 .   ? -1.646  -4.334  -1.500 1.00 21.07 ? 430 HOH   B O   1 
HETATM 4209 O  O   . HOH   G 4 .   ? -10.346 -20.909 27.745 1.00 22.18 ? 431 HOH   B O   1 
HETATM 4210 O  O   . HOH   G 4 .   ? -24.252 -14.848 19.206 1.00 25.86 ? 432 HOH   B O   1 
HETATM 4211 O  O   . HOH   G 4 .   ? -21.981 -4.618  -0.532 1.00 32.04 ? 433 HOH   B O   1 
HETATM 4212 O  O   . HOH   G 4 .   ? -16.752 -0.548  -5.962 1.00 31.59 ? 434 HOH   B O   1 
HETATM 4213 O  O   . HOH   G 4 .   ? -2.231  -1.464  11.058 1.00 14.59 ? 435 HOH   B O   1 
HETATM 4214 O  O   . HOH   G 4 .   ? -17.601 -9.196  33.138 1.00 22.50 ? 436 HOH   B O   1 
HETATM 4215 O  O   . HOH   G 4 .   ? -13.901 -20.349 3.258  1.00 32.63 ? 437 HOH   B O   1 
HETATM 4216 O  O   . HOH   G 4 .   ? -23.991 6.146   2.748  1.00 32.13 ? 438 HOH   B O   1 
HETATM 4217 O  O   . HOH   G 4 .   ? -28.003 -0.981  24.249 1.00 32.39 ? 439 HOH   B O   1 
HETATM 4218 O  O   . HOH   G 4 .   ? -12.957 -18.145 28.876 1.00 17.11 ? 440 HOH   B O   1 
HETATM 4219 O  O   . HOH   G 4 .   ? -20.172 -6.760  -5.614 1.00 21.42 ? 441 HOH   B O   1 
HETATM 4220 O  O   . HOH   G 4 .   ? -0.403  -12.671 -5.744 1.00 47.01 ? 442 HOH   B O   1 
HETATM 4221 O  O   . HOH   G 4 .   ? -4.606  -0.522  33.490 1.00 30.90 ? 443 HOH   B O   1 
HETATM 4222 O  O   . HOH   G 4 .   ? 1.346   -7.789  7.122  1.00 19.15 ? 444 HOH   B O   1 
HETATM 4223 O  O   . HOH   G 4 .   ? -24.663 -4.295  24.028 1.00 25.55 ? 445 HOH   B O   1 
HETATM 4224 O  O   . HOH   G 4 .   ? -21.024 -0.349  32.674 1.00 26.60 ? 446 HOH   B O   1 
HETATM 4225 O  O   . HOH   G 4 .   ? -17.922 4.359   15.667 1.00 30.37 ? 447 HOH   B O   1 
HETATM 4226 O  O   . HOH   G 4 .   ? -16.937 10.570  15.047 1.00 40.58 ? 448 HOH   B O   1 
HETATM 4227 O  O   . HOH   G 4 .   ? 3.954   -15.440 -0.886 1.00 26.49 ? 449 HOH   B O   1 
HETATM 4228 O  O   . HOH   G 4 .   ? 2.848   -7.825  27.340 1.00 27.33 ? 450 HOH   B O   1 
HETATM 4229 O  O   . HOH   G 4 .   ? -28.167 -1.103  4.213  1.00 38.23 ? 451 HOH   B O   1 
HETATM 4230 O  O   . HOH   G 4 .   ? 6.372   -15.759 12.504 1.00 30.63 ? 452 HOH   B O   1 
HETATM 4231 O  O   . HOH   G 4 .   ? -8.581  -27.254 9.291  1.00 42.33 ? 453 HOH   B O   1 
HETATM 4232 O  O   . HOH   G 4 .   ? 6.439   -12.775 11.560 1.00 22.06 ? 454 HOH   B O   1 
HETATM 4233 O  O   . HOH   G 4 .   ? -14.648 15.787  9.226  1.00 25.37 ? 455 HOH   B O   1 
HETATM 4234 O  O   . HOH   G 4 .   ? -6.848  -0.303  -5.760 1.00 17.19 ? 456 HOH   B O   1 
HETATM 4235 O  O   . HOH   G 4 .   ? -16.835 -1.989  34.400 1.00 29.58 ? 457 HOH   B O   1 
HETATM 4236 O  O   . HOH   G 4 .   ? 3.931   -24.272 7.068  1.00 24.07 ? 458 HOH   B O   1 
HETATM 4237 O  O   . HOH   G 4 .   ? 0.392   -19.028 22.353 1.00 18.46 ? 459 HOH   B O   1 
HETATM 4238 O  O   . HOH   G 4 .   ? -10.942 -4.332  -5.098 1.00 24.06 ? 460 HOH   B O   1 
HETATM 4239 O  O   . HOH   G 4 .   ? -5.179  -12.226 -1.628 1.00 36.67 ? 461 HOH   B O   1 
HETATM 4240 O  O   . HOH   G 4 .   ? 10.854  2.166   18.655 1.00 32.11 ? 462 HOH   B O   1 
HETATM 4241 O  O   . HOH   G 4 .   ? -3.272  9.998   9.641  1.00 40.93 ? 463 HOH   B O   1 
HETATM 4242 O  O   . HOH   G 4 .   ? 10.342  -6.510  17.205 1.00 38.14 ? 464 HOH   B O   1 
HETATM 4243 O  O   . HOH   G 4 .   ? -7.042  -14.563 29.296 1.00 17.25 ? 465 HOH   B O   1 
HETATM 4244 O  O   . HOH   G 4 .   ? -28.646 -5.877  33.730 1.00 32.57 ? 466 HOH   B O   1 
HETATM 4245 O  O   . HOH   G 4 .   ? -16.574 -15.427 33.531 1.00 40.45 ? 467 HOH   B O   1 
HETATM 4246 O  O   . HOH   G 4 .   ? -19.438 -13.966 6.015  1.00 19.96 ? 468 HOH   B O   1 
HETATM 4247 O  O   . HOH   G 4 .   ? -23.931 -9.391  9.196  1.00 35.73 ? 469 HOH   B O   1 
HETATM 4248 O  O   . HOH   G 4 .   ? -7.230  -5.919  37.853 1.00 26.49 ? 470 HOH   B O   1 
HETATM 4249 O  O   . HOH   G 4 .   ? -0.648  -0.122  4.492  1.00 20.14 ? 471 HOH   B O   1 
HETATM 4250 O  O   . HOH   G 4 .   ? -1.794  -13.244 25.270 1.00 19.67 ? 472 HOH   B O   1 
HETATM 4251 O  O   . HOH   G 4 .   ? -10.379 -16.244 8.869  1.00 14.04 ? 473 HOH   B O   1 
HETATM 4252 O  O   . HOH   G 4 .   ? 8.609   -1.608  13.913 1.00 39.73 ? 474 HOH   B O   1 
HETATM 4253 O  O   . HOH   G 4 .   ? -21.564 -3.763  33.515 1.00 29.24 ? 475 HOH   B O   1 
HETATM 4254 O  O   . HOH   G 4 .   ? -11.769 -21.308 11.265 1.00 18.06 ? 476 HOH   B O   1 
HETATM 4255 O  O   . HOH   G 4 .   ? -5.177  -15.009 27.103 1.00 22.31 ? 477 HOH   B O   1 
HETATM 4256 O  O   . HOH   G 4 .   ? -14.771 -10.938 38.088 1.00 31.11 ? 478 HOH   B O   1 
HETATM 4257 O  O   . HOH   G 4 .   ? -10.474 15.927  3.241  1.00 26.08 ? 479 HOH   B O   1 
HETATM 4258 O  O   . HOH   G 4 .   ? -24.480 -5.824  17.043 1.00 25.10 ? 480 HOH   B O   1 
HETATM 4259 O  O   . HOH   G 4 .   ? 4.600   -17.320 23.585 1.00 30.71 ? 481 HOH   B O   1 
HETATM 4260 O  O   . HOH   G 4 .   ? -26.730 -7.597  9.959  1.00 32.89 ? 482 HOH   B O   1 
HETATM 4261 O  O   . HOH   G 4 .   ? -5.742  -17.876 29.850 1.00 23.11 ? 483 HOH   B O   1 
HETATM 4262 O  O   . HOH   G 4 .   ? -16.913 -16.986 -3.288 1.00 37.05 ? 484 HOH   B O   1 
HETATM 4263 O  O   . HOH   G 4 .   ? -9.160  -13.249 33.167 1.00 32.16 ? 485 HOH   B O   1 
HETATM 4264 O  O   . HOH   G 4 .   ? -0.353  -11.034 26.115 1.00 21.12 ? 486 HOH   B O   1 
HETATM 4265 O  O   . HOH   G 4 .   ? -25.493 2.555   28.594 1.00 29.85 ? 487 HOH   B O   1 
HETATM 4266 O  O   . HOH   G 4 .   ? -15.578 1.448   20.649 1.00 35.79 ? 488 HOH   B O   1 
HETATM 4267 O  O   . HOH   G 4 .   ? -6.549  -5.389  -0.428 1.00 11.96 ? 489 HOH   B O   1 
HETATM 4268 O  O   . HOH   G 4 .   ? -12.448 -19.011 32.462 1.00 31.09 ? 490 HOH   B O   1 
HETATM 4269 O  O   . HOH   G 4 .   ? -15.848 -25.091 7.441  1.00 41.21 ? 491 HOH   B O   1 
HETATM 4270 O  O   . HOH   G 4 .   ? -24.767 -11.040 15.882 1.00 25.72 ? 492 HOH   B O   1 
HETATM 4271 O  O   . HOH   G 4 .   ? -15.347 -23.140 25.579 1.00 17.48 ? 493 HOH   B O   1 
HETATM 4272 O  O   . HOH   G 4 .   ? -14.871 9.048   -1.612 1.00 33.30 ? 494 HOH   B O   1 
HETATM 4273 O  O   . HOH   G 4 .   ? -5.919  10.093  9.672  1.00 25.12 ? 495 HOH   B O   1 
HETATM 4274 O  O   . HOH   G 4 .   ? -19.773 5.671   19.411 1.00 35.55 ? 496 HOH   B O   1 
HETATM 4275 O  O   . HOH   G 4 .   ? -20.838 -5.141  23.426 1.00 16.86 ? 497 HOH   B O   1 
HETATM 4276 O  O   . HOH   G 4 .   ? -22.076 3.996   0.578  1.00 30.23 ? 498 HOH   B O   1 
HETATM 4277 O  O   . HOH   G 4 .   ? -17.600 0.849   21.920 1.00 36.38 ? 499 HOH   B O   1 
HETATM 4278 O  O   . HOH   G 4 .   ? -3.983  -19.655 27.087 1.00 23.45 ? 500 HOH   B O   1 
HETATM 4279 O  O   . HOH   G 4 .   ? -15.768 -23.303 18.903 1.00 19.18 ? 501 HOH   B O   1 
HETATM 4280 O  O   . HOH   G 4 .   ? -32.071 -2.750  18.500 1.00 44.54 ? 502 HOH   B O   1 
HETATM 4281 O  O   . HOH   G 4 .   ? -4.543  6.686   8.267  1.00 18.27 ? 503 HOH   B O   1 
HETATM 4282 O  O   . HOH   G 4 .   ? -30.562 -7.334  23.989 1.00 38.98 ? 504 HOH   B O   1 
HETATM 4283 O  O   . HOH   G 4 .   ? 5.642   -1.003  12.031 1.00 18.95 ? 505 HOH   B O   1 
HETATM 4284 O  O   . HOH   G 4 .   ? 1.252   -21.405 0.512  1.00 29.79 ? 506 HOH   B O   1 
HETATM 4285 O  O   . HOH   G 4 .   ? 10.338  -13.924 13.121 1.00 30.35 ? 507 HOH   B O   1 
HETATM 4286 O  O   . HOH   G 4 .   ? -2.329  -27.722 13.280 1.00 33.37 ? 508 HOH   B O   1 
HETATM 4287 O  O   . HOH   G 4 .   ? -26.638 0.401   6.006  1.00 27.78 ? 509 HOH   B O   1 
HETATM 4288 O  O   . HOH   G 4 .   ? -13.052 -23.036 18.460 1.00 16.41 ? 510 HOH   B O   1 
HETATM 4289 O  O   . HOH   G 4 .   ? -13.555 3.183   -4.651 1.00 36.49 ? 511 HOH   B O   1 
HETATM 4290 O  O   . HOH   G 4 .   ? -23.476 -19.631 -3.578 1.00 39.77 ? 512 HOH   B O   1 
HETATM 4291 O  O   . HOH   G 4 .   ? -5.870  -19.698 6.618  1.00 26.17 ? 513 HOH   B O   1 
HETATM 4292 O  O   . HOH   G 4 .   ? -1.611  15.628  1.146  1.00 43.47 ? 514 HOH   B O   1 
HETATM 4293 O  O   . HOH   G 4 .   ? -4.981  20.180  3.986  1.00 59.40 ? 515 HOH   B O   1 
HETATM 4294 O  O   . HOH   G 4 .   ? 6.526   -24.302 7.320  1.00 30.37 ? 516 HOH   B O   1 
HETATM 4295 O  O   . HOH   G 4 .   ? -18.861 -3.366  33.527 1.00 41.66 ? 517 HOH   B O   1 
HETATM 4296 O  O   . HOH   G 4 .   ? -27.783 0.634   8.635  1.00 34.90 ? 518 HOH   B O   1 
HETATM 4297 O  O   . HOH   G 4 .   ? -16.323 -24.742 14.748 1.00 29.47 ? 519 HOH   B O   1 
HETATM 4298 O  O   . HOH   G 4 .   ? 11.859  -16.707 17.282 1.00 36.54 ? 520 HOH   B O   1 
HETATM 4299 O  O   . HOH   G 4 .   ? -5.563  13.503  8.854  1.00 41.10 ? 521 HOH   B O   1 
HETATM 4300 O  O   . HOH   G 4 .   ? -2.823  7.323   6.249  1.00 21.58 ? 522 HOH   B O   1 
HETATM 4301 O  O   . HOH   G 4 .   ? -24.062 -4.387  26.959 1.00 30.06 ? 523 HOH   B O   1 
HETATM 4302 O  O   . HOH   G 4 .   ? -1.967  -17.629 22.903 1.00 15.24 ? 524 HOH   B O   1 
HETATM 4303 O  O   . HOH   G 4 .   ? 7.825   -8.464  17.983 1.00 21.47 ? 525 HOH   B O   1 
HETATM 4304 O  O   . HOH   G 4 .   ? -14.305 -26.627 15.521 1.00 41.36 ? 526 HOH   B O   1 
HETATM 4305 O  O   . HOH   G 4 .   ? -15.924 -4.737  34.921 1.00 19.74 ? 527 HOH   B O   1 
HETATM 4306 O  O   . HOH   G 4 .   ? -15.285 -10.123 -7.028 1.00 25.15 ? 528 HOH   B O   1 
HETATM 4307 O  O   . HOH   G 4 .   ? -20.974 8.480   19.261 1.00 32.98 ? 529 HOH   B O   1 
HETATM 4308 O  O   . HOH   G 4 .   ? 5.645   2.356   6.022  1.00 30.43 ? 530 HOH   B O   1 
HETATM 4309 O  O   . HOH   G 4 .   ? -27.047 4.613   18.013 1.00 22.77 ? 531 HOH   B O   1 
HETATM 4310 O  O   . HOH   G 4 .   ? -16.846 7.096   1.224  1.00 38.21 ? 532 HOH   B O   1 
HETATM 4311 O  O   . HOH   G 4 .   ? -12.490 1.430   21.009 1.00 40.14 ? 533 HOH   B O   1 
HETATM 4312 O  O   . HOH   G 4 .   ? 5.547   -21.360 17.635 1.00 30.00 ? 534 HOH   B O   1 
HETATM 4313 O  O   . HOH   G 4 .   ? 8.045   -7.108  7.483  1.00 30.97 ? 535 HOH   B O   1 
HETATM 4314 O  O   . HOH   G 4 .   ? -14.970 0.490   28.506 1.00 22.86 ? 536 HOH   B O   1 
HETATM 4315 O  O   . HOH   G 4 .   ? -3.274  9.949   13.313 1.00 38.53 ? 537 HOH   B O   1 
HETATM 4316 O  O   . HOH   G 4 .   ? -0.512  -13.502 -1.220 1.00 34.82 ? 538 HOH   B O   1 
HETATM 4317 O  O   . HOH   G 4 .   ? -4.719  12.696  -2.659 1.00 32.25 ? 539 HOH   B O   1 
HETATM 4318 O  O   . HOH   G 4 .   ? 2.689   -2.401  26.007 1.00 21.74 ? 540 HOH   B O   1 
HETATM 4319 O  O   . HOH   G 4 .   ? -20.942 12.948  11.646 1.00 30.94 ? 541 HOH   B O   1 
HETATM 4320 O  O   . HOH   G 4 .   ? -1.276  -30.997 22.986 1.00 38.58 ? 542 HOH   B O   1 
HETATM 4321 O  O   . HOH   G 4 .   ? -2.184  9.924   6.927  1.00 29.02 ? 543 HOH   B O   1 
HETATM 4322 O  O   . HOH   G 4 .   ? -15.481 4.902   25.681 1.00 48.61 ? 544 HOH   B O   1 
HETATM 4323 O  O   . HOH   G 4 .   ? -28.513 1.105   11.100 1.00 33.40 ? 545 HOH   B O   1 
HETATM 4324 O  O   . HOH   G 4 .   ? 12.541  -13.347 15.804 1.00 31.10 ? 546 HOH   B O   1 
HETATM 4325 O  O   . HOH   G 4 .   ? 5.473   3.048   22.837 1.00 27.22 ? 547 HOH   B O   1 
HETATM 4326 O  O   . HOH   G 4 .   ? 5.070   -4.215  26.714 1.00 36.89 ? 548 HOH   B O   1 
HETATM 4327 O  O   . HOH   G 4 .   ? -0.837  4.406   1.543  1.00 30.29 ? 549 HOH   B O   1 
HETATM 4328 O  O   . HOH   G 4 .   ? -27.839 -9.803  8.778  1.00 47.98 ? 550 HOH   B O   1 
HETATM 4329 O  O   . HOH   G 4 .   ? -11.070 -24.158 9.868  1.00 37.25 ? 551 HOH   B O   1 
HETATM 4330 O  O   . HOH   G 4 .   ? -8.261  -31.499 15.568 1.00 35.79 ? 552 HOH   B O   1 
HETATM 4331 O  O   . HOH   G 4 .   ? 7.569   -2.582  10.652 1.00 34.56 ? 553 HOH   B O   1 
HETATM 4332 O  O   . HOH   G 4 .   ? -1.841  -25.385 11.708 1.00 28.56 ? 554 HOH   B O   1 
HETATM 4333 O  O   . HOH   G 4 .   ? -4.399  -22.961 27.113 1.00 41.98 ? 555 HOH   B O   1 
HETATM 4334 O  O   . HOH   G 4 .   ? -27.167 9.124   12.344 1.00 25.59 ? 556 HOH   B O   1 
HETATM 4335 O  O   . HOH   G 4 .   ? -25.325 -16.858 -1.172 1.00 31.38 ? 557 HOH   B O   1 
HETATM 4336 O  O   . HOH   G 4 .   ? 0.617   -4.664  28.507 1.00 35.99 ? 558 HOH   B O   1 
HETATM 4337 O  O   . HOH   G 4 .   ? -24.864 -7.007  8.201  1.00 35.98 ? 559 HOH   B O   1 
HETATM 4338 O  O   . HOH   G 4 .   ? 4.374   -19.134 12.922 1.00 30.18 ? 560 HOH   B O   1 
HETATM 4339 O  O   . HOH   G 4 .   ? -3.439  -25.639 9.153  1.00 34.46 ? 561 HOH   B O   1 
HETATM 4340 O  O   . HOH   G 4 .   ? -12.915 2.594   28.267 1.00 29.43 ? 562 HOH   B O   1 
HETATM 4341 O  O   . HOH   G 4 .   ? -17.359 8.112   -1.079 1.00 40.23 ? 563 HOH   B O   1 
HETATM 4342 O  O   . HOH   G 4 .   ? -7.246  -16.367 -0.863 1.00 44.21 ? 564 HOH   B O   1 
HETATM 4343 O  O   . HOH   G 4 .   ? 4.994   -22.231 4.297  1.00 33.53 ? 565 HOH   B O   1 
HETATM 4344 O  O   . HOH   G 4 .   ? -7.873  -13.393 -1.093 1.00 35.57 ? 566 HOH   B O   1 
HETATM 4345 O  O   . HOH   G 4 .   ? 9.781   -9.753  10.699 1.00 43.67 ? 567 HOH   B O   1 
HETATM 4346 O  O   . HOH   G 4 .   ? 3.180   11.579  4.728  1.00 43.91 ? 568 HOH   B O   1 
HETATM 4347 O  O   . HOH   G 4 .   ? -27.029 -3.274  24.088 1.00 46.96 ? 569 HOH   B O   1 
HETATM 4348 O  O   . HOH   G 4 .   ? -11.211 -24.333 30.910 1.00 35.94 ? 570 HOH   B O   1 
HETATM 4349 O  O   . HOH   G 4 .   ? 1.766   -12.306 27.226 1.00 34.94 ? 571 HOH   B O   1 
HETATM 4350 O  O   . HOH   G 4 .   ? -16.788 0.546   31.023 1.00 43.53 ? 572 HOH   B O   1 
HETATM 4351 O  O   . HOH   G 4 .   ? -24.566 9.037   15.410 1.00 50.90 ? 573 HOH   B O   1 
HETATM 4352 O  O   . HOH   G 4 .   ? -7.069  -22.168 27.833 1.00 50.34 ? 574 HOH   B O   1 
HETATM 4353 O  O   . HOH   G 4 .   ? -3.658  6.861   3.696  1.00 21.79 ? 575 HOH   B O   1 
HETATM 4354 O  O   . HOH   G 4 .   ? -9.917  -2.634  -7.231 1.00 34.31 ? 576 HOH   B O   1 
HETATM 4355 O  O   . HOH   G 4 .   ? 0.949   -8.727  -7.654 1.00 48.06 ? 577 HOH   B O   1 
HETATM 4356 O  O   . HOH   G 4 .   ? -3.337  -16.949 26.950 1.00 24.88 ? 578 HOH   B O   1 
HETATM 4357 O  O   . HOH   G 4 .   ? -0.433  -28.699 9.683  1.00 38.91 ? 579 HOH   B O   1 
HETATM 4358 O  O   . HOH   G 4 .   ? -15.956 -21.226 27.616 1.00 23.21 ? 580 HOH   B O   1 
HETATM 4359 O  O   . HOH   G 4 .   ? 4.921   8.637   12.253 1.00 37.81 ? 581 HOH   B O   1 
HETATM 4360 O  O   . HOH   G 4 .   ? 0.720   -2.425  27.771 1.00 36.89 ? 582 HOH   B O   1 
HETATM 4361 O  O   . HOH   G 4 .   ? 3.218   -5.216  4.051  1.00 41.49 ? 583 HOH   B O   1 
HETATM 4362 O  O   . HOH   G 4 .   ? 1.970   -7.508  4.607  1.00 23.94 ? 584 HOH   B O   1 
HETATM 4363 O  O   . HOH   G 4 .   ? -26.183 5.485   6.599  1.00 38.69 ? 585 HOH   B O   1 
HETATM 4364 O  O   . HOH   G 4 .   ? -14.272 -20.481 29.530 1.00 23.61 ? 586 HOH   B O   1 
HETATM 4365 O  O   . HOH   G 4 .   ? -26.318 -9.673  30.095 1.00 46.89 ? 587 HOH   B O   1 
HETATM 4366 O  O   . HOH   G 4 .   ? -11.753 -25.486 18.849 1.00 43.26 ? 588 HOH   B O   1 
HETATM 4367 O  O   . HOH   G 4 .   ? 2.054   -18.597 24.473 1.00 23.41 ? 589 HOH   B O   1 
HETATM 4368 O  O   . HOH   G 4 .   ? -1.833  -13.340 29.139 1.00 48.47 ? 590 HOH   B O   1 
HETATM 4369 O  O   . HOH   G 4 .   ? -11.921 -21.929 29.666 1.00 35.35 ? 591 HOH   B O   1 
HETATM 4370 O  O   . HOH   G 4 .   ? -13.165 -14.714 -7.811 1.00 52.21 ? 592 HOH   B O   1 
HETATM 4371 O  O   . HOH   G 4 .   ? -1.325  -12.791 32.560 1.00 40.63 ? 593 HOH   B O   1 
HETATM 4372 O  O   . HOH   G 4 .   ? -1.450  -15.919 25.148 1.00 20.28 ? 594 HOH   B O   1 
HETATM 4373 O  O   . HOH   G 4 .   ? -18.747 -13.448 -8.425 1.00 45.23 ? 595 HOH   B O   1 
HETATM 4374 O  O   . HOH   G 4 .   ? 2.341   -21.026 25.737 1.00 36.42 ? 596 HOH   B O   1 
HETATM 4375 O  O   . HOH   G 4 .   ? -5.032  -22.011 6.020  1.00 32.23 ? 597 HOH   B O   1 
HETATM 4376 O  O   . HOH   G 4 .   ? -24.704 10.445  1.548  1.00 39.82 ? 598 HOH   B O   1 
HETATM 4377 O  O   . HOH   G 4 .   ? -20.641 -2.806  -4.176 1.00 40.30 ? 599 HOH   B O   1 
HETATM 4378 O  O   . HOH   G 4 .   ? -13.011 16.184  1.792  1.00 33.08 ? 600 HOH   B O   1 
HETATM 4379 O  O   . HOH   G 4 .   ? -27.817 0.580   29.018 1.00 31.14 ? 601 HOH   B O   1 
HETATM 4380 O  O   . HOH   G 4 .   ? 2.992   11.481  16.052 1.00 47.56 ? 602 HOH   B O   1 
HETATM 4381 O  O   . HOH   G 4 .   ? -16.156 3.158   32.041 1.00 44.56 ? 603 HOH   B O   1 
HETATM 4382 O  O   . HOH   G 4 .   ? -10.525 -13.777 35.446 1.00 31.36 ? 604 HOH   B O   1 
HETATM 4383 O  O   . HOH   G 4 .   ? 2.543   -14.754 27.210 1.00 31.09 ? 605 HOH   B O   1 
HETATM 4384 O  O   . HOH   G 4 .   ? 14.446  -10.408 14.899 1.00 45.44 ? 606 HOH   B O   1 
HETATM 4385 O  O   . HOH   G 4 .   ? -35.075 3.139   18.036 1.00 33.80 ? 607 HOH   B O   1 
HETATM 4386 O  O   . HOH   G 4 .   ? 14.170  9.842   14.715 1.00 39.19 ? 608 HOH   B O   1 
HETATM 4387 O  O   . HOH   G 4 .   ? 0.879   -16.637 26.162 1.00 25.65 ? 609 HOH   B O   1 
HETATM 4388 O  O   . HOH   G 4 .   ? -5.884  2.623   24.025 1.00 50.55 ? 610 HOH   B O   1 
HETATM 4389 O  O   . HOH   G 4 .   ? 6.844   -2.439  27.926 1.00 39.47 ? 611 HOH   B O   1 
HETATM 4390 O  O   . HOH   H 4 .   ? -25.370 -15.015 28.181 1.00 34.24 ? 401 HOH   A O   1 
HETATM 4391 O  O   . HOH   H 4 .   ? -43.606 -15.168 38.365 1.00 40.36 ? 402 HOH   A O   1 
HETATM 4392 O  O   . HOH   H 4 .   ? -30.173 -13.184 26.170 1.00 45.68 ? 403 HOH   A O   1 
HETATM 4393 O  O   . HOH   H 4 .   ? -40.433 -32.179 26.942 1.00 32.77 ? 404 HOH   A O   1 
HETATM 4394 O  O   . HOH   H 4 .   ? -43.985 -28.502 24.268 1.00 39.85 ? 405 HOH   A O   1 
HETATM 4395 O  O   . HOH   H 4 .   ? -32.068 -56.818 22.938 1.00 36.00 ? 406 HOH   A O   1 
HETATM 4396 O  O   . HOH   H 4 .   ? -22.870 -30.727 5.367  1.00 35.62 ? 407 HOH   A O   1 
HETATM 4397 O  O   . HOH   H 4 .   ? -38.282 -54.429 22.920 1.00 39.08 ? 408 HOH   A O   1 
HETATM 4398 O  O   . HOH   H 4 .   ? -48.946 -54.563 25.834 1.00 43.62 ? 409 HOH   A O   1 
HETATM 4399 O  O   . HOH   H 4 .   ? -30.562 -37.271 48.540 1.00 38.37 ? 410 HOH   A O   1 
HETATM 4400 O  O   . HOH   H 4 .   ? -34.585 -19.121 45.295 1.00 28.65 ? 411 HOH   A O   1 
HETATM 4401 O  O   . HOH   H 4 .   ? -40.340 -26.146 43.781 1.00 33.39 ? 412 HOH   A O   1 
HETATM 4402 O  O   . HOH   H 4 .   ? -27.856 -28.607 9.650  1.00 18.24 ? 413 HOH   A O   1 
HETATM 4403 O  O   . HOH   H 4 .   ? -25.282 -40.463 7.507  1.00 32.29 ? 414 HOH   A O   1 
HETATM 4404 O  O   . HOH   H 4 .   ? -35.256 -13.595 17.712 1.00 39.52 ? 415 HOH   A O   1 
HETATM 4405 O  O   . HOH   H 4 .   ? -37.146 -19.762 7.344  1.00 31.74 ? 416 HOH   A O   1 
HETATM 4406 O  O   . HOH   H 4 .   ? -26.398 -50.320 33.278 1.00 23.58 ? 417 HOH   A O   1 
HETATM 4407 O  O   . HOH   H 4 .   ? -25.102 -24.443 46.250 1.00 23.71 ? 418 HOH   A O   1 
HETATM 4408 O  O   . HOH   H 4 .   ? -30.325 -11.227 37.561 1.00 35.04 ? 419 HOH   A O   1 
HETATM 4409 O  O   . HOH   H 4 .   ? -35.116 -13.428 32.454 1.00 38.98 ? 420 HOH   A O   1 
HETATM 4410 O  O   . HOH   H 4 .   ? -36.830 -39.968 30.071 1.00 13.68 ? 421 HOH   A O   1 
HETATM 4411 O  O   . HOH   H 4 .   ? -23.694 -34.303 4.271  1.00 27.23 ? 422 HOH   A O   1 
HETATM 4412 O  O   . HOH   H 4 .   ? -27.776 -40.608 14.423 1.00 17.03 ? 423 HOH   A O   1 
HETATM 4413 O  O   . HOH   H 4 .   ? -14.296 -47.094 35.204 1.00 29.39 ? 424 HOH   A O   1 
HETATM 4414 O  O   . HOH   H 4 .   ? -44.813 -36.506 32.393 1.00 18.60 ? 425 HOH   A O   1 
HETATM 4415 O  O   . HOH   H 4 .   ? -28.196 -13.486 16.396 1.00 35.33 ? 426 HOH   A O   1 
HETATM 4416 O  O   . HOH   H 4 .   ? -29.295 -46.152 17.439 1.00 19.73 ? 427 HOH   A O   1 
HETATM 4417 O  O   . HOH   H 4 .   ? -20.341 -40.858 10.714 1.00 29.41 ? 428 HOH   A O   1 
HETATM 4418 O  O   . HOH   H 4 .   ? -33.305 -29.320 44.834 1.00 18.75 ? 429 HOH   A O   1 
HETATM 4419 O  O   . HOH   H 4 .   ? -42.245 -34.773 7.841  1.00 33.01 ? 430 HOH   A O   1 
HETATM 4420 O  O   . HOH   H 4 .   ? -31.508 -42.359 34.966 1.00 20.47 ? 431 HOH   A O   1 
HETATM 4421 O  O   . HOH   H 4 .   ? -34.202 -51.498 27.392 1.00 32.40 ? 432 HOH   A O   1 
HETATM 4422 O  O   . HOH   H 4 .   ? -30.156 -59.052 18.952 1.00 31.26 ? 433 HOH   A O   1 
HETATM 4423 O  O   . HOH   H 4 .   ? -41.647 -24.884 23.075 1.00 23.64 ? 434 HOH   A O   1 
HETATM 4424 O  O   . HOH   H 4 .   ? -32.244 -24.186 14.636 1.00 17.36 ? 435 HOH   A O   1 
HETATM 4425 O  O   . HOH   H 4 .   ? -17.225 -36.261 12.046 1.00 23.73 ? 436 HOH   A O   1 
HETATM 4426 O  O   . HOH   H 4 .   ? -14.022 -28.160 18.971 1.00 31.12 ? 437 HOH   A O   1 
HETATM 4427 O  O   . HOH   H 4 .   ? -53.393 -29.277 36.613 1.00 31.60 ? 438 HOH   A O   1 
HETATM 4428 O  O   . HOH   H 4 .   ? -36.754 -15.084 30.893 1.00 23.19 ? 439 HOH   A O   1 
HETATM 4429 O  O   . HOH   H 4 .   ? -32.303 -20.522 13.048 1.00 37.49 ? 440 HOH   A O   1 
HETATM 4430 O  O   . HOH   H 4 .   ? -17.232 -32.222 38.791 1.00 39.63 ? 441 HOH   A O   1 
HETATM 4431 O  O   . HOH   H 4 .   ? -20.055 -28.304 43.036 1.00 34.24 ? 442 HOH   A O   1 
HETATM 4432 O  O   . HOH   H 4 .   ? -25.935 -43.207 40.876 1.00 29.03 ? 443 HOH   A O   1 
HETATM 4433 O  O   . HOH   H 4 .   ? -30.696 -23.145 12.646 1.00 18.22 ? 444 HOH   A O   1 
HETATM 4434 O  O   . HOH   H 4 .   ? -26.556 -53.423 20.875 1.00 24.52 ? 445 HOH   A O   1 
HETATM 4435 O  O   . HOH   H 4 .   ? -41.829 -14.687 27.572 1.00 30.56 ? 446 HOH   A O   1 
HETATM 4436 O  O   . HOH   H 4 .   ? -32.652 -53.120 26.374 1.00 35.30 ? 447 HOH   A O   1 
HETATM 4437 O  O   . HOH   H 4 .   ? -42.833 -16.666 34.548 1.00 25.20 ? 448 HOH   A O   1 
HETATM 4438 O  O   . HOH   H 4 .   ? -40.622 -50.410 30.036 1.00 24.87 ? 449 HOH   A O   1 
HETATM 4439 O  O   . HOH   H 4 .   ? -33.567 -30.973 4.816  1.00 17.56 ? 450 HOH   A O   1 
HETATM 4440 O  O   . HOH   H 4 .   ? -36.846 -14.160 28.274 1.00 27.15 ? 451 HOH   A O   1 
HETATM 4441 O  O   . HOH   H 4 .   ? -28.161 -30.830 47.668 1.00 30.81 ? 452 HOH   A O   1 
HETATM 4442 O  O   . HOH   H 4 .   ? -25.307 -43.562 16.191 1.00 23.79 ? 453 HOH   A O   1 
HETATM 4443 O  O   . HOH   H 4 .   ? -35.760 -17.057 38.200 1.00 27.26 ? 454 HOH   A O   1 
HETATM 4444 O  O   . HOH   H 4 .   ? -20.104 -24.233 42.873 1.00 44.27 ? 455 HOH   A O   1 
HETATM 4445 O  O   . HOH   H 4 .   ? -22.007 -31.385 43.735 1.00 40.64 ? 456 HOH   A O   1 
HETATM 4446 O  O   . HOH   H 4 .   ? -40.663 -18.293 37.154 1.00 27.29 ? 457 HOH   A O   1 
HETATM 4447 O  O   . HOH   H 4 .   ? -32.163 -18.980 38.430 1.00 26.35 ? 458 HOH   A O   1 
HETATM 4448 O  O   . HOH   H 4 .   ? -30.637 -47.962 15.027 1.00 24.18 ? 459 HOH   A O   1 
HETATM 4449 O  O   . HOH   H 4 .   ? -32.215 -39.048 1.882  1.00 18.28 ? 460 HOH   A O   1 
HETATM 4450 O  O   . HOH   H 4 .   ? -32.490 -34.199 40.762 1.00 13.79 ? 461 HOH   A O   1 
HETATM 4451 O  O   . HOH   H 4 .   ? -42.676 -37.277 38.133 1.00 20.05 ? 462 HOH   A O   1 
HETATM 4452 O  O   . HOH   H 4 .   ? -29.532 -40.618 38.012 1.00 19.44 ? 463 HOH   A O   1 
HETATM 4453 O  O   . HOH   H 4 .   ? -24.058 -26.587 8.033  1.00 32.15 ? 464 HOH   A O   1 
HETATM 4454 O  O   . HOH   H 4 .   ? -53.027 -25.978 30.442 1.00 32.76 ? 465 HOH   A O   1 
HETATM 4455 O  O   . HOH   H 4 .   ? -54.151 -33.092 42.957 1.00 39.32 ? 466 HOH   A O   1 
HETATM 4456 O  O   . HOH   H 4 .   ? -28.494 -28.953 5.831  1.00 17.22 ? 467 HOH   A O   1 
HETATM 4457 O  O   . HOH   H 4 .   ? -46.762 -33.271 25.083 1.00 41.74 ? 468 HOH   A O   1 
HETATM 4458 O  O   . HOH   H 4 .   ? -41.495 -32.816 23.301 1.00 44.04 ? 469 HOH   A O   1 
HETATM 4459 O  O   . HOH   H 4 .   ? -20.260 -33.696 10.627 1.00 19.94 ? 470 HOH   A O   1 
HETATM 4460 O  O   . HOH   H 4 .   ? -16.429 -31.895 28.472 1.00 15.77 ? 471 HOH   A O   1 
HETATM 4461 O  O   . HOH   H 4 .   ? -19.580 -21.785 26.744 1.00 31.04 ? 472 HOH   A O   1 
HETATM 4462 O  O   . HOH   H 4 .   ? -25.814 -49.341 30.798 1.00 19.57 ? 473 HOH   A O   1 
HETATM 4463 O  O   . HOH   H 4 .   ? -25.439 -28.713 3.917  1.00 35.55 ? 474 HOH   A O   1 
HETATM 4464 O  O   . HOH   H 4 .   ? -27.617 -47.592 14.888 1.00 34.05 ? 475 HOH   A O   1 
HETATM 4465 O  O   . HOH   H 4 .   ? -29.351 -20.317 20.944 1.00 40.12 ? 476 HOH   A O   1 
HETATM 4466 O  O   . HOH   H 4 .   ? -22.838 -18.379 41.867 1.00 34.94 ? 477 HOH   A O   1 
HETATM 4467 O  O   . HOH   H 4 .   ? -23.873 -39.235 11.212 1.00 19.63 ? 478 HOH   A O   1 
HETATM 4468 O  O   . HOH   H 4 .   ? -37.043 -28.790 5.777  1.00 17.61 ? 479 HOH   A O   1 
HETATM 4469 O  O   . HOH   H 4 .   ? -21.551 -32.535 30.863 1.00 15.62 ? 480 HOH   A O   1 
HETATM 4470 O  O   . HOH   H 4 .   ? -38.213 -40.602 36.767 1.00 21.70 ? 481 HOH   A O   1 
HETATM 4471 O  O   . HOH   H 4 .   ? -33.212 -53.084 18.741 1.00 19.15 ? 482 HOH   A O   1 
HETATM 4472 O  O   . HOH   H 4 .   ? -18.367 -36.856 33.970 1.00 21.98 ? 483 HOH   A O   1 
HETATM 4473 O  O   . HOH   H 4 .   ? -9.900  -38.788 17.639 1.00 35.71 ? 484 HOH   A O   1 
HETATM 4474 O  O   . HOH   H 4 .   ? -17.210 -28.550 35.981 1.00 29.62 ? 485 HOH   A O   1 
HETATM 4475 O  O   . HOH   H 4 .   ? -41.136 -16.067 19.306 1.00 21.18 ? 486 HOH   A O   1 
HETATM 4476 O  O   . HOH   H 4 .   ? -28.479 -18.952 28.948 1.00 42.56 ? 487 HOH   A O   1 
HETATM 4477 O  O   . HOH   H 4 .   ? -18.526 -25.997 33.704 1.00 24.03 ? 488 HOH   A O   1 
HETATM 4478 O  O   . HOH   H 4 .   ? -22.293 -20.272 34.289 1.00 36.51 ? 489 HOH   A O   1 
HETATM 4479 O  O   . HOH   H 4 .   ? -47.858 -18.546 29.254 1.00 30.04 ? 490 HOH   A O   1 
HETATM 4480 O  O   . HOH   H 4 .   ? -26.008 -35.486 42.228 1.00 24.72 ? 491 HOH   A O   1 
HETATM 4481 O  O   . HOH   H 4 .   ? -29.070 -50.888 33.041 1.00 24.30 ? 492 HOH   A O   1 
HETATM 4482 O  O   . HOH   H 4 .   ? -17.609 -24.360 17.231 1.00 18.93 ? 493 HOH   A O   1 
HETATM 4483 O  O   . HOH   H 4 .   ? -29.607 -16.624 27.530 1.00 24.80 ? 494 HOH   A O   1 
HETATM 4484 O  O   . HOH   H 4 .   ? -25.292 -37.802 6.858  1.00 25.41 ? 495 HOH   A O   1 
HETATM 4485 O  O   . HOH   H 4 .   ? -38.048 -47.877 30.595 1.00 21.14 ? 496 HOH   A O   1 
HETATM 4486 O  O   . HOH   H 4 .   ? -32.573 -40.223 47.048 1.00 24.51 ? 497 HOH   A O   1 
HETATM 4487 O  O   . HOH   H 4 .   ? -21.288 -23.811 35.838 1.00 27.16 ? 498 HOH   A O   1 
HETATM 4488 O  O   . HOH   H 4 .   ? -18.103 -23.735 26.023 1.00 21.51 ? 499 HOH   A O   1 
HETATM 4489 O  O   . HOH   H 4 .   ? -21.706 -49.285 37.324 1.00 36.41 ? 500 HOH   A O   1 
HETATM 4490 O  O   . HOH   H 4 .   ? -23.557 -40.807 13.583 1.00 29.63 ? 501 HOH   A O   1 
HETATM 4491 O  O   . HOH   H 4 .   ? -17.785 -40.329 37.740 1.00 38.78 ? 502 HOH   A O   1 
HETATM 4492 O  O   . HOH   H 4 .   ? -25.615 -16.955 12.384 1.00 37.07 ? 503 HOH   A O   1 
HETATM 4493 O  O   . HOH   H 4 .   ? -35.005 -50.244 16.173 1.00 22.04 ? 504 HOH   A O   1 
HETATM 4494 O  O   . HOH   H 4 .   ? -27.770 -44.912 15.521 1.00 20.64 ? 505 HOH   A O   1 
HETATM 4495 O  O   . HOH   H 4 .   ? -19.223 -34.694 7.399  1.00 34.42 ? 506 HOH   A O   1 
HETATM 4496 O  O   . HOH   H 4 .   ? -33.851 -38.719 42.644 1.00 28.52 ? 507 HOH   A O   1 
HETATM 4497 O  O   . HOH   H 4 .   ? -39.102 -46.266 12.835 1.00 33.57 ? 508 HOH   A O   1 
HETATM 4498 O  O   . HOH   H 4 .   ? -29.938 -16.142 32.163 1.00 28.72 ? 509 HOH   A O   1 
HETATM 4499 O  O   . HOH   H 4 .   ? -22.167 -46.015 35.617 1.00 25.52 ? 510 HOH   A O   1 
HETATM 4500 O  O   . HOH   H 4 .   ? -41.925 -23.542 39.337 1.00 38.83 ? 511 HOH   A O   1 
HETATM 4501 O  O   . HOH   H 4 .   ? -48.030 -37.705 31.460 1.00 43.92 ? 512 HOH   A O   1 
HETATM 4502 O  O   . HOH   H 4 .   ? -27.241 -27.884 48.230 1.00 23.81 ? 513 HOH   A O   1 
HETATM 4503 O  O   . HOH   H 4 .   ? -37.374 -13.788 25.274 1.00 25.79 ? 514 HOH   A O   1 
HETATM 4504 O  O   . HOH   H 4 .   ? -19.680 -45.681 19.423 1.00 33.18 ? 515 HOH   A O   1 
HETATM 4505 O  O   . HOH   H 4 .   ? -47.694 -25.166 23.631 1.00 36.25 ? 516 HOH   A O   1 
HETATM 4506 O  O   . HOH   H 4 .   ? -41.997 -47.784 20.107 1.00 31.48 ? 517 HOH   A O   1 
HETATM 4507 O  O   . HOH   H 4 .   ? -15.894 -42.175 13.693 1.00 39.57 ? 518 HOH   A O   1 
HETATM 4508 O  O   . HOH   H 4 .   ? -40.535 -13.567 18.891 1.00 31.58 ? 519 HOH   A O   1 
HETATM 4509 O  O   . HOH   H 4 .   ? -15.537 -52.402 36.302 1.00 39.70 ? 520 HOH   A O   1 
HETATM 4510 O  O   . HOH   H 4 .   ? -48.240 -35.129 30.796 1.00 30.25 ? 521 HOH   A O   1 
HETATM 4511 O  O   . HOH   H 4 .   ? -14.023 -39.800 10.327 1.00 32.19 ? 522 HOH   A O   1 
HETATM 4512 O  O   . HOH   H 4 .   ? -46.881 -47.523 20.168 1.00 37.63 ? 523 HOH   A O   1 
HETATM 4513 O  O   . HOH   H 4 .   ? -30.684 -12.712 18.804 1.00 36.29 ? 524 HOH   A O   1 
HETATM 4514 O  O   . HOH   H 4 .   ? -41.300 -46.705 36.325 1.00 34.14 ? 525 HOH   A O   1 
HETATM 4515 O  O   . HOH   H 4 .   ? -13.220 -41.622 29.508 1.00 29.56 ? 526 HOH   A O   1 
HETATM 4516 O  O   . HOH   H 4 .   ? -27.357 -25.636 46.583 1.00 21.36 ? 527 HOH   A O   1 
HETATM 4517 O  O   . HOH   H 4 .   ? -45.645 -37.857 34.573 1.00 20.66 ? 528 HOH   A O   1 
HETATM 4518 O  O   . HOH   H 4 .   ? -36.440 -47.781 16.478 1.00 21.99 ? 529 HOH   A O   1 
HETATM 4519 O  O   . HOH   H 4 .   ? -12.787 -29.367 23.918 1.00 23.69 ? 530 HOH   A O   1 
HETATM 4520 O  O   . HOH   H 4 .   ? -33.971 -46.144 13.386 1.00 39.31 ? 531 HOH   A O   1 
HETATM 4521 O  O   . HOH   H 4 .   ? -17.555 -49.123 26.168 1.00 23.47 ? 532 HOH   A O   1 
HETATM 4522 O  O   . HOH   H 4 .   ? -48.010 -38.254 27.540 1.00 34.59 ? 533 HOH   A O   1 
HETATM 4523 O  O   . HOH   H 4 .   ? -38.434 -30.302 11.201 1.00 18.79 ? 534 HOH   A O   1 
HETATM 4524 O  O   . HOH   H 4 .   ? -45.949 -36.784 40.922 1.00 36.50 ? 535 HOH   A O   1 
HETATM 4525 O  O   . HOH   H 4 .   ? -24.586 -46.129 41.701 1.00 29.03 ? 536 HOH   A O   1 
HETATM 4526 O  O   . HOH   H 4 .   ? -24.499 -33.154 41.669 1.00 29.36 ? 537 HOH   A O   1 
HETATM 4527 O  O   . HOH   H 4 .   ? -21.312 -26.150 13.481 1.00 25.24 ? 538 HOH   A O   1 
HETATM 4528 O  O   . HOH   H 4 .   ? -21.080 -43.220 18.395 1.00 22.19 ? 539 HOH   A O   1 
HETATM 4529 O  O   . HOH   H 4 .   ? -23.081 -22.764 32.647 1.00 21.57 ? 540 HOH   A O   1 
HETATM 4530 O  O   . HOH   H 4 .   ? -9.304  -47.554 23.553 1.00 40.98 ? 541 HOH   A O   1 
HETATM 4531 O  O   . HOH   H 4 .   ? -36.104 -39.815 41.032 1.00 26.93 ? 542 HOH   A O   1 
HETATM 4532 O  O   . HOH   H 4 .   ? -12.184 -27.300 31.056 1.00 38.51 ? 543 HOH   A O   1 
HETATM 4533 O  O   . HOH   H 4 .   ? -49.883 -20.624 26.474 1.00 27.55 ? 544 HOH   A O   1 
HETATM 4534 O  O   . HOH   H 4 .   ? -25.624 -19.433 21.990 1.00 28.03 ? 545 HOH   A O   1 
HETATM 4535 O  O   . HOH   H 4 .   ? -37.981 -51.179 29.098 1.00 36.75 ? 546 HOH   A O   1 
HETATM 4536 O  O   . HOH   H 4 .   ? -30.381 -51.398 25.156 1.00 21.47 ? 547 HOH   A O   1 
HETATM 4537 O  O   . HOH   H 4 .   ? -45.427 -14.816 25.154 1.00 37.66 ? 548 HOH   A O   1 
HETATM 4538 O  O   . HOH   H 4 .   ? -48.269 -38.265 34.000 1.00 24.82 ? 549 HOH   A O   1 
HETATM 4539 O  O   . HOH   H 4 .   ? -24.635 -53.109 30.386 1.00 24.63 ? 550 HOH   A O   1 
HETATM 4540 O  O   . HOH   H 4 .   ? -18.845 -53.813 32.550 1.00 30.67 ? 551 HOH   A O   1 
HETATM 4541 O  O   . HOH   H 4 .   ? -8.399  -42.564 12.043 1.00 35.01 ? 552 HOH   A O   1 
HETATM 4542 O  O   . HOH   H 4 .   ? -12.863 -25.541 33.061 1.00 39.86 ? 553 HOH   A O   1 
HETATM 4543 O  O   . HOH   H 4 .   ? -45.049 -36.738 37.077 1.00 25.33 ? 554 HOH   A O   1 
HETATM 4544 O  O   . HOH   H 4 .   ? -14.777 -31.855 20.969 1.00 23.48 ? 555 HOH   A O   1 
HETATM 4545 O  O   . HOH   H 4 .   ? -22.240 -54.864 27.012 1.00 28.74 ? 556 HOH   A O   1 
HETATM 4546 O  O   . HOH   H 4 .   ? -38.664 -26.620 17.117 1.00 37.33 ? 557 HOH   A O   1 
HETATM 4547 O  O   . HOH   H 4 .   ? -40.548 -32.216 11.987 1.00 25.52 ? 558 HOH   A O   1 
HETATM 4548 O  O   . HOH   H 4 .   ? -40.711 -20.728 39.734 1.00 40.95 ? 559 HOH   A O   1 
HETATM 4549 O  O   . HOH   H 4 .   ? -46.907 -41.480 41.282 1.00 35.77 ? 560 HOH   A O   1 
HETATM 4550 O  O   . HOH   H 4 .   ? -52.920 -44.512 27.058 1.00 42.81 ? 561 HOH   A O   1 
HETATM 4551 O  O   . HOH   H 4 .   ? -50.015 -43.175 38.765 1.00 36.80 ? 562 HOH   A O   1 
HETATM 4552 O  O   . HOH   H 4 .   ? -8.012  -40.172 11.234 1.00 42.58 ? 563 HOH   A O   1 
HETATM 4553 O  O   . HOH   H 4 .   ? -24.673 -26.774 5.290  1.00 41.35 ? 564 HOH   A O   1 
HETATM 4554 O  O   . HOH   H 4 .   ? -18.093 -47.500 28.601 1.00 33.17 ? 565 HOH   A O   1 
HETATM 4555 O  O   . HOH   H 4 .   ? -29.510 -23.908 47.048 1.00 19.64 ? 566 HOH   A O   1 
HETATM 4556 O  O   . HOH   H 4 .   ? -42.677 -39.005 39.544 1.00 37.36 ? 567 HOH   A O   1 
HETATM 4557 O  O   . HOH   H 4 .   ? -41.582 -49.698 18.634 1.00 35.43 ? 568 HOH   A O   1 
HETATM 4558 O  O   . HOH   H 4 .   ? -39.025 -29.435 8.564  1.00 26.87 ? 569 HOH   A O   1 
HETATM 4559 O  O   . HOH   H 4 .   ? -51.497 -37.906 37.254 1.00 38.99 ? 570 HOH   A O   1 
HETATM 4560 O  O   . HOH   H 4 .   ? -20.445 -19.323 41.583 1.00 36.32 ? 571 HOH   A O   1 
HETATM 4561 O  O   . HOH   H 4 .   ? -34.541 -17.068 13.194 1.00 42.40 ? 572 HOH   A O   1 
HETATM 4562 O  O   . HOH   H 4 .   ? -33.863 -54.610 28.863 1.00 50.38 ? 573 HOH   A O   1 
HETATM 4563 O  O   . HOH   H 4 .   ? -23.643 -13.015 32.212 1.00 50.62 ? 574 HOH   A O   1 
HETATM 4564 O  O   . HOH   H 4 .   ? -13.899 -32.491 29.964 1.00 28.69 ? 575 HOH   A O   1 
HETATM 4565 O  O   . HOH   H 4 .   ? -34.559 -40.066 44.792 1.00 38.90 ? 576 HOH   A O   1 
HETATM 4566 O  O   . HOH   H 4 .   ? -50.386 -42.958 36.530 1.00 33.88 ? 577 HOH   A O   1 
HETATM 4567 O  O   . HOH   H 4 .   ? -22.259 -35.296 41.382 1.00 41.81 ? 578 HOH   A O   1 
HETATM 4568 O  O   . HOH   H 4 .   ? -33.313 -10.504 25.676 1.00 39.33 ? 579 HOH   A O   1 
HETATM 4569 O  O   . HOH   H 4 .   ? -47.701 -46.304 30.178 1.00 31.62 ? 580 HOH   A O   1 
HETATM 4570 O  O   . HOH   H 4 .   ? -32.466 -13.531 32.398 1.00 44.38 ? 581 HOH   A O   1 
HETATM 4571 O  O   . HOH   H 4 .   ? -21.065 -48.425 39.386 1.00 41.53 ? 582 HOH   A O   1 
HETATM 4572 O  O   . HOH   H 4 .   ? -22.379 -21.657 37.926 1.00 49.06 ? 583 HOH   A O   1 
HETATM 4573 O  O   . HOH   H 4 .   ? -16.489 -24.515 34.740 1.00 37.51 ? 584 HOH   A O   1 
HETATM 4574 O  O   . HOH   H 4 .   ? -33.493 -26.416 47.896 1.00 29.00 ? 585 HOH   A O   1 
HETATM 4575 O  O   . HOH   H 4 .   ? -32.997 -24.549 50.264 1.00 35.79 ? 586 HOH   A O   1 
HETATM 4576 O  O   . HOH   H 4 .   ? -36.333 -46.180 14.064 1.00 40.94 ? 587 HOH   A O   1 
HETATM 4577 O  O   . HOH   H 4 .   ? -39.250 -14.294 31.620 1.00 35.20 ? 588 HOH   A O   1 
HETATM 4578 O  O   . HOH   H 4 .   ? -19.654 -20.226 29.079 1.00 44.78 ? 589 HOH   A O   1 
HETATM 4579 O  O   . HOH   H 4 .   ? -42.306 -34.935 24.218 1.00 48.79 ? 590 HOH   A O   1 
HETATM 4580 O  O   . HOH   H 4 .   ? -19.108 -32.188 8.737  1.00 41.88 ? 591 HOH   A O   1 
HETATM 4581 O  O   . HOH   H 4 .   ? -40.220 -22.209 16.500 1.00 44.36 ? 592 HOH   A O   1 
HETATM 4582 O  O   . HOH   H 4 .   ? -21.007 -30.215 7.635  1.00 38.30 ? 593 HOH   A O   1 
HETATM 4583 O  O   . HOH   H 4 .   ? -22.971 -25.699 47.107 1.00 42.81 ? 594 HOH   A O   1 
HETATM 4584 O  O   . HOH   H 4 .   ? -45.678 -41.307 21.764 1.00 59.84 ? 595 HOH   A O   1 
HETATM 4585 O  O   . HOH   H 4 .   ? -42.720 -46.239 14.873 1.00 45.53 ? 596 HOH   A O   1 
HETATM 4586 O  O   . HOH   H 4 .   ? -9.079  -33.730 10.106 1.00 62.67 ? 597 HOH   A O   1 
HETATM 4587 O  O   . HOH   H 4 .   ? -22.624 -44.021 16.359 1.00 28.78 ? 598 HOH   A O   1 
HETATM 4588 O  O   . HOH   H 4 .   ? -28.307 -16.842 39.856 1.00 43.09 ? 599 HOH   A O   1 
HETATM 4589 O  O   . HOH   H 4 .   ? -41.349 -14.954 30.552 1.00 45.27 ? 600 HOH   A O   1 
HETATM 4590 O  O   . HOH   H 4 .   ? -51.555 -37.904 30.515 1.00 48.83 ? 601 HOH   A O   1 
HETATM 4591 O  O   . HOH   H 4 .   ? -16.003 -37.777 34.876 1.00 28.68 ? 602 HOH   A O   1 
HETATM 4592 O  O   . HOH   H 4 .   ? -20.443 -23.565 33.241 1.00 41.65 ? 603 HOH   A O   1 
HETATM 4593 O  O   . HOH   H 4 .   ? -24.795 -43.436 12.001 1.00 43.16 ? 604 HOH   A O   1 
HETATM 4594 O  O   . HOH   H 4 .   ? -32.024 -10.857 15.478 1.00 39.66 ? 605 HOH   A O   1 
HETATM 4595 O  O   . HOH   H 4 .   ? -23.438 -30.535 47.248 1.00 42.21 ? 606 HOH   A O   1 
HETATM 4596 O  O   . HOH   H 4 .   ? -36.396 -52.434 15.694 1.00 45.83 ? 607 HOH   A O   1 
HETATM 4597 O  O   . HOH   H 4 .   ? -12.939 -29.555 21.096 1.00 39.24 ? 608 HOH   A O   1 
# 
