data_9FPW
# 
_entry.id   9FPW 
# 
_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   9FPW         pdb_00009fpw 10.2210/pdb9fpw/pdb 
WWPDB D_1292139315 ?            ?                   
# 
_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                        9FPW 
_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-(2-phenylethylsulfanyl)-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-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' 351.440   2   ?       ? ?                               
? 
4 non-polymer syn 'SODIUM ION'                                            22.990    1   ?       ? ?                               
? 
5 water       nat water                                                   18.015    312 ?       ? ?                               
? 
# 
_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-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' A1IEN 
4 'SODIUM ION'                                            NA    
5 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 
A1IEN non-polymer         . 'methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' ? 'C16 H17 N O4 S2' 351.440 
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 
NA    non-polymer         . 'SODIUM ION'                                            ? 'Na 1'            22.990  
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 262 262 262 PHE PHE A . n 
B 1 263 HIS 263 263 263 HIS HIS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IEN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IEN 
_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 A1IEN 1   302 1   A1IEN JA4 B . 
E 2 ZN    1   301 2   ZN    ZN  A . 
F 3 A1IEN 1   302 2   A1IEN JA4 A . 
G 4 NA    1   303 1   NA    NA  A . 
H 5 HOH   1   401 270 HOH   HOH B . 
H 5 HOH   2   402 237 HOH   HOH B . 
H 5 HOH   3   403 231 HOH   HOH B . 
H 5 HOH   4   404 29  HOH   HOH B . 
H 5 HOH   5   405 36  HOH   HOH B . 
H 5 HOH   6   406 248 HOH   HOH B . 
H 5 HOH   7   407 47  HOH   HOH B . 
H 5 HOH   8   408 215 HOH   HOH B . 
H 5 HOH   9   409 62  HOH   HOH B . 
H 5 HOH   10  410 72  HOH   HOH B . 
H 5 HOH   11  411 5   HOH   HOH B . 
H 5 HOH   12  412 196 HOH   HOH B . 
H 5 HOH   13  413 106 HOH   HOH B . 
H 5 HOH   14  414 9   HOH   HOH B . 
H 5 HOH   15  415 220 HOH   HOH B . 
H 5 HOH   16  416 14  HOH   HOH B . 
H 5 HOH   17  417 42  HOH   HOH B . 
H 5 HOH   18  418 191 HOH   HOH B . 
H 5 HOH   19  419 143 HOH   HOH B . 
H 5 HOH   20  420 125 HOH   HOH B . 
H 5 HOH   21  421 101 HOH   HOH B . 
H 5 HOH   22  422 250 HOH   HOH B . 
H 5 HOH   23  423 7   HOH   HOH B . 
H 5 HOH   24  424 144 HOH   HOH B . 
H 5 HOH   25  425 278 HOH   HOH B . 
H 5 HOH   26  426 301 HOH   HOH B . 
H 5 HOH   27  427 165 HOH   HOH B . 
H 5 HOH   28  428 45  HOH   HOH B . 
H 5 HOH   29  429 148 HOH   HOH B . 
H 5 HOH   30  430 137 HOH   HOH B . 
H 5 HOH   31  431 186 HOH   HOH B . 
H 5 HOH   32  432 302 HOH   HOH B . 
H 5 HOH   33  433 110 HOH   HOH B . 
H 5 HOH   34  434 244 HOH   HOH B . 
H 5 HOH   35  435 12  HOH   HOH B . 
H 5 HOH   36  436 17  HOH   HOH B . 
H 5 HOH   37  437 274 HOH   HOH B . 
H 5 HOH   38  438 128 HOH   HOH B . 
H 5 HOH   39  439 211 HOH   HOH B . 
H 5 HOH   40  440 188 HOH   HOH B . 
H 5 HOH   41  441 4   HOH   HOH B . 
H 5 HOH   42  442 221 HOH   HOH B . 
H 5 HOH   43  443 39  HOH   HOH B . 
H 5 HOH   44  444 2   HOH   HOH B . 
H 5 HOH   45  445 33  HOH   HOH B . 
H 5 HOH   46  446 216 HOH   HOH B . 
H 5 HOH   47  447 118 HOH   HOH B . 
H 5 HOH   48  448 83  HOH   HOH B . 
H 5 HOH   49  449 80  HOH   HOH B . 
H 5 HOH   50  450 138 HOH   HOH B . 
H 5 HOH   51  451 85  HOH   HOH B . 
H 5 HOH   52  452 58  HOH   HOH B . 
H 5 HOH   53  453 117 HOH   HOH B . 
H 5 HOH   54  454 279 HOH   HOH B . 
H 5 HOH   55  455 156 HOH   HOH B . 
H 5 HOH   56  456 57  HOH   HOH B . 
H 5 HOH   57  457 11  HOH   HOH B . 
H 5 HOH   58  458 78  HOH   HOH B . 
H 5 HOH   59  459 95  HOH   HOH B . 
H 5 HOH   60  460 152 HOH   HOH B . 
H 5 HOH   61  461 8   HOH   HOH B . 
H 5 HOH   62  462 16  HOH   HOH B . 
H 5 HOH   63  463 116 HOH   HOH B . 
H 5 HOH   64  464 43  HOH   HOH B . 
H 5 HOH   65  465 114 HOH   HOH B . 
H 5 HOH   66  466 184 HOH   HOH B . 
H 5 HOH   67  467 88  HOH   HOH B . 
H 5 HOH   68  468 97  HOH   HOH B . 
H 5 HOH   69  469 307 HOH   HOH B . 
H 5 HOH   70  470 201 HOH   HOH B . 
H 5 HOH   71  471 210 HOH   HOH B . 
H 5 HOH   72  472 46  HOH   HOH B . 
H 5 HOH   73  473 169 HOH   HOH B . 
H 5 HOH   74  474 32  HOH   HOH B . 
H 5 HOH   75  475 218 HOH   HOH B . 
H 5 HOH   76  476 49  HOH   HOH B . 
H 5 HOH   77  477 93  HOH   HOH B . 
H 5 HOH   78  478 77  HOH   HOH B . 
H 5 HOH   79  479 266 HOH   HOH B . 
H 5 HOH   80  480 228 HOH   HOH B . 
H 5 HOH   81  481 44  HOH   HOH B . 
H 5 HOH   82  482 10  HOH   HOH B . 
H 5 HOH   83  483 87  HOH   HOH B . 
H 5 HOH   84  484 30  HOH   HOH B . 
H 5 HOH   85  485 82  HOH   HOH B . 
H 5 HOH   86  486 145 HOH   HOH B . 
H 5 HOH   87  487 113 HOH   HOH B . 
H 5 HOH   88  488 26  HOH   HOH B . 
H 5 HOH   89  489 67  HOH   HOH B . 
H 5 HOH   90  490 161 HOH   HOH B . 
H 5 HOH   91  491 280 HOH   HOH B . 
H 5 HOH   92  492 64  HOH   HOH B . 
H 5 HOH   93  493 166 HOH   HOH B . 
H 5 HOH   94  494 183 HOH   HOH B . 
H 5 HOH   95  495 86  HOH   HOH B . 
H 5 HOH   96  496 151 HOH   HOH B . 
H 5 HOH   97  497 99  HOH   HOH B . 
H 5 HOH   98  498 277 HOH   HOH B . 
H 5 HOH   99  499 243 HOH   HOH B . 
H 5 HOH   100 500 162 HOH   HOH B . 
H 5 HOH   101 501 127 HOH   HOH B . 
H 5 HOH   102 502 136 HOH   HOH B . 
H 5 HOH   103 503 13  HOH   HOH B . 
H 5 HOH   104 504 171 HOH   HOH B . 
H 5 HOH   105 505 214 HOH   HOH B . 
H 5 HOH   106 506 103 HOH   HOH B . 
H 5 HOH   107 507 175 HOH   HOH B . 
H 5 HOH   108 508 79  HOH   HOH B . 
H 5 HOH   109 509 150 HOH   HOH B . 
H 5 HOH   110 510 157 HOH   HOH B . 
H 5 HOH   111 511 132 HOH   HOH B . 
H 5 HOH   112 512 287 HOH   HOH B . 
H 5 HOH   113 513 252 HOH   HOH B . 
H 5 HOH   114 514 91  HOH   HOH B . 
H 5 HOH   115 515 119 HOH   HOH B . 
H 5 HOH   116 516 90  HOH   HOH B . 
H 5 HOH   117 517 263 HOH   HOH B . 
H 5 HOH   118 518 109 HOH   HOH B . 
H 5 HOH   119 519 226 HOH   HOH B . 
H 5 HOH   120 520 306 HOH   HOH B . 
H 5 HOH   121 521 260 HOH   HOH B . 
H 5 HOH   122 522 203 HOH   HOH B . 
H 5 HOH   123 523 275 HOH   HOH B . 
H 5 HOH   124 524 194 HOH   HOH B . 
H 5 HOH   125 525 249 HOH   HOH B . 
H 5 HOH   126 526 311 HOH   HOH B . 
H 5 HOH   127 527 170 HOH   HOH B . 
H 5 HOH   128 528 163 HOH   HOH B . 
H 5 HOH   129 529 70  HOH   HOH B . 
H 5 HOH   130 530 73  HOH   HOH B . 
H 5 HOH   131 531 285 HOH   HOH B . 
H 5 HOH   132 532 262 HOH   HOH B . 
H 5 HOH   133 533 230 HOH   HOH B . 
H 5 HOH   134 534 179 HOH   HOH B . 
H 5 HOH   135 535 227 HOH   HOH B . 
H 5 HOH   136 536 271 HOH   HOH B . 
H 5 HOH   137 537 120 HOH   HOH B . 
H 5 HOH   138 538 289 HOH   HOH B . 
H 5 HOH   139 539 256 HOH   HOH B . 
H 5 HOH   140 540 178 HOH   HOH B . 
H 5 HOH   141 541 268 HOH   HOH B . 
H 5 HOH   142 542 292 HOH   HOH B . 
H 5 HOH   143 543 135 HOH   HOH B . 
H 5 HOH   144 544 308 HOH   HOH B . 
H 5 HOH   145 545 310 HOH   HOH B . 
H 5 HOH   146 546 219 HOH   HOH B . 
H 5 HOH   147 547 258 HOH   HOH B . 
H 5 HOH   148 548 65  HOH   HOH B . 
H 5 HOH   149 549 245 HOH   HOH B . 
H 5 HOH   150 550 304 HOH   HOH B . 
H 5 HOH   151 551 159 HOH   HOH B . 
H 5 HOH   152 552 229 HOH   HOH B . 
H 5 HOH   153 553 255 HOH   HOH B . 
H 5 HOH   154 554 286 HOH   HOH B . 
H 5 HOH   155 555 242 HOH   HOH B . 
H 5 HOH   156 556 298 HOH   HOH B . 
H 5 HOH   157 557 309 HOH   HOH B . 
H 5 HOH   158 558 272 HOH   HOH B . 
H 5 HOH   159 559 303 HOH   HOH B . 
I 5 HOH   1   401 213 HOH   HOH A . 
I 5 HOH   2   402 205 HOH   HOH A . 
I 5 HOH   3   403 105 HOH   HOH A . 
I 5 HOH   4   404 247 HOH   HOH A . 
I 5 HOH   5   405 94  HOH   HOH A . 
I 5 HOH   6   406 209 HOH   HOH A . 
I 5 HOH   7   407 158 HOH   HOH A . 
I 5 HOH   8   408 160 HOH   HOH A . 
I 5 HOH   9   409 217 HOH   HOH A . 
I 5 HOH   10  410 34  HOH   HOH A . 
I 5 HOH   11  411 172 HOH   HOH A . 
I 5 HOH   12  412 112 HOH   HOH A . 
I 5 HOH   13  413 190 HOH   HOH A . 
I 5 HOH   14  414 50  HOH   HOH A . 
I 5 HOH   15  415 312 HOH   HOH A . 
I 5 HOH   16  416 197 HOH   HOH A . 
I 5 HOH   17  417 291 HOH   HOH A . 
I 5 HOH   18  418 121 HOH   HOH A . 
I 5 HOH   19  419 56  HOH   HOH A . 
I 5 HOH   20  420 276 HOH   HOH A . 
I 5 HOH   21  421 204 HOH   HOH A . 
I 5 HOH   22  422 20  HOH   HOH A . 
I 5 HOH   23  423 23  HOH   HOH A . 
I 5 HOH   24  424 155 HOH   HOH A . 
I 5 HOH   25  425 281 HOH   HOH A . 
I 5 HOH   26  426 180 HOH   HOH A . 
I 5 HOH   27  427 115 HOH   HOH A . 
I 5 HOH   28  428 25  HOH   HOH A . 
I 5 HOH   29  429 3   HOH   HOH A . 
I 5 HOH   30  430 69  HOH   HOH A . 
I 5 HOH   31  431 224 HOH   HOH A . 
I 5 HOH   32  432 235 HOH   HOH A . 
I 5 HOH   33  433 71  HOH   HOH A . 
I 5 HOH   34  434 75  HOH   HOH A . 
I 5 HOH   35  435 140 HOH   HOH A . 
I 5 HOH   36  436 51  HOH   HOH A . 
I 5 HOH   37  437 305 HOH   HOH A . 
I 5 HOH   38  438 1   HOH   HOH A . 
I 5 HOH   39  439 41  HOH   HOH A . 
I 5 HOH   40  440 233 HOH   HOH A . 
I 5 HOH   41  441 269 HOH   HOH A . 
I 5 HOH   42  442 123 HOH   HOH A . 
I 5 HOH   43  443 53  HOH   HOH A . 
I 5 HOH   44  444 18  HOH   HOH A . 
I 5 HOH   45  445 129 HOH   HOH A . 
I 5 HOH   46  446 104 HOH   HOH A . 
I 5 HOH   47  447 6   HOH   HOH A . 
I 5 HOH   48  448 59  HOH   HOH A . 
I 5 HOH   49  449 76  HOH   HOH A . 
I 5 HOH   50  450 66  HOH   HOH A . 
I 5 HOH   51  451 300 HOH   HOH A . 
I 5 HOH   52  452 126 HOH   HOH A . 
I 5 HOH   53  453 48  HOH   HOH A . 
I 5 HOH   54  454 185 HOH   HOH A . 
I 5 HOH   55  455 19  HOH   HOH A . 
I 5 HOH   56  456 96  HOH   HOH A . 
I 5 HOH   57  457 193 HOH   HOH A . 
I 5 HOH   58  458 60  HOH   HOH A . 
I 5 HOH   59  459 139 HOH   HOH A . 
I 5 HOH   60  460 130 HOH   HOH A . 
I 5 HOH   61  461 28  HOH   HOH A . 
I 5 HOH   62  462 122 HOH   HOH A . 
I 5 HOH   63  463 108 HOH   HOH A . 
I 5 HOH   64  464 238 HOH   HOH A . 
I 5 HOH   65  465 264 HOH   HOH A . 
I 5 HOH   66  466 22  HOH   HOH A . 
I 5 HOH   67  467 192 HOH   HOH A . 
I 5 HOH   68  468 187 HOH   HOH A . 
I 5 HOH   69  469 84  HOH   HOH A . 
I 5 HOH   70  470 273 HOH   HOH A . 
I 5 HOH   71  471 92  HOH   HOH A . 
I 5 HOH   72  472 149 HOH   HOH A . 
I 5 HOH   73  473 232 HOH   HOH A . 
I 5 HOH   74  474 81  HOH   HOH A . 
I 5 HOH   75  475 54  HOH   HOH A . 
I 5 HOH   76  476 223 HOH   HOH A . 
I 5 HOH   77  477 98  HOH   HOH A . 
I 5 HOH   78  478 239 HOH   HOH A . 
I 5 HOH   79  479 181 HOH   HOH A . 
I 5 HOH   80  480 195 HOH   HOH A . 
I 5 HOH   81  481 176 HOH   HOH A . 
I 5 HOH   82  482 246 HOH   HOH A . 
I 5 HOH   83  483 299 HOH   HOH A . 
I 5 HOH   84  484 111 HOH   HOH A . 
I 5 HOH   85  485 208 HOH   HOH A . 
I 5 HOH   86  486 294 HOH   HOH A . 
I 5 HOH   87  487 40  HOH   HOH A . 
I 5 HOH   88  488 296 HOH   HOH A . 
I 5 HOH   89  489 257 HOH   HOH A . 
I 5 HOH   90  490 68  HOH   HOH A . 
I 5 HOH   91  491 240 HOH   HOH A . 
I 5 HOH   92  492 15  HOH   HOH A . 
I 5 HOH   93  493 282 HOH   HOH A . 
I 5 HOH   94  494 284 HOH   HOH A . 
I 5 HOH   95  495 27  HOH   HOH A . 
I 5 HOH   96  496 142 HOH   HOH A . 
I 5 HOH   97  497 38  HOH   HOH A . 
I 5 HOH   98  498 153 HOH   HOH A . 
I 5 HOH   99  499 251 HOH   HOH A . 
I 5 HOH   100 500 200 HOH   HOH A . 
I 5 HOH   101 501 173 HOH   HOH A . 
I 5 HOH   102 502 107 HOH   HOH A . 
I 5 HOH   103 503 253 HOH   HOH A . 
I 5 HOH   104 504 259 HOH   HOH A . 
I 5 HOH   105 505 202 HOH   HOH A . 
I 5 HOH   106 506 31  HOH   HOH A . 
I 5 HOH   107 507 154 HOH   HOH A . 
I 5 HOH   108 508 37  HOH   HOH A . 
I 5 HOH   109 509 283 HOH   HOH A . 
I 5 HOH   110 510 63  HOH   HOH A . 
I 5 HOH   111 511 225 HOH   HOH A . 
I 5 HOH   112 512 35  HOH   HOH A . 
I 5 HOH   113 513 265 HOH   HOH A . 
I 5 HOH   114 514 100 HOH   HOH A . 
I 5 HOH   115 515 147 HOH   HOH A . 
I 5 HOH   116 516 131 HOH   HOH A . 
I 5 HOH   117 517 146 HOH   HOH A . 
I 5 HOH   118 518 61  HOH   HOH A . 
I 5 HOH   119 519 297 HOH   HOH A . 
I 5 HOH   120 520 102 HOH   HOH A . 
I 5 HOH   121 521 267 HOH   HOH A . 
I 5 HOH   122 522 52  HOH   HOH A . 
I 5 HOH   123 523 89  HOH   HOH A . 
I 5 HOH   124 524 141 HOH   HOH A . 
I 5 HOH   125 525 55  HOH   HOH A . 
I 5 HOH   126 526 241 HOH   HOH A . 
I 5 HOH   127 527 24  HOH   HOH A . 
I 5 HOH   128 528 124 HOH   HOH A . 
I 5 HOH   129 529 133 HOH   HOH A . 
I 5 HOH   130 530 74  HOH   HOH A . 
I 5 HOH   131 531 134 HOH   HOH A . 
I 5 HOH   132 532 288 HOH   HOH A . 
I 5 HOH   133 533 21  HOH   HOH A . 
I 5 HOH   134 534 199 HOH   HOH A . 
I 5 HOH   135 535 198 HOH   HOH A . 
I 5 HOH   136 536 207 HOH   HOH A . 
I 5 HOH   137 537 261 HOH   HOH A . 
I 5 HOH   138 538 177 HOH   HOH A . 
I 5 HOH   139 539 182 HOH   HOH A . 
I 5 HOH   140 540 293 HOH   HOH A . 
I 5 HOH   141 541 234 HOH   HOH A . 
I 5 HOH   142 542 189 HOH   HOH A . 
I 5 HOH   143 543 295 HOH   HOH A . 
I 5 HOH   144 544 290 HOH   HOH A . 
I 5 HOH   145 545 174 HOH   HOH A . 
I 5 HOH   146 546 212 HOH   HOH A . 
I 5 HOH   147 547 164 HOH   HOH A . 
I 5 HOH   148 548 206 HOH   HOH A . 
I 5 HOH   149 549 222 HOH   HOH A . 
I 5 HOH   150 550 167 HOH   HOH A . 
I 5 HOH   151 551 168 HOH   HOH A . 
I 5 HOH   152 552 254 HOH   HOH A . 
I 5 HOH   153 553 236 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 GLU 11  ? CD  ? A GLU 11  CD  
2  1 Y 1 B GLU 11  ? OE1 ? A GLU 11  OE1 
3  1 Y 1 B GLU 11  ? OE2 ? A GLU 11  OE2 
4  1 Y 1 B ILE 16  ? CD1 ? A ILE 16  CD1 
5  1 Y 1 B LYS 174 ? CE  ? A LYS 174 CE  
6  1 Y 1 B LYS 174 ? NZ  ? A LYS 174 NZ  
7  1 Y 1 A GLU 11  ? CG  ? B GLU 11  CG  
8  1 Y 1 A GLU 11  ? CD  ? B GLU 11  CD  
9  1 Y 1 A GLU 11  ? OE1 ? B GLU 11  OE1 
10 1 Y 1 A GLU 11  ? OE2 ? B GLU 11  OE2 
11 1 Y 1 A LYS 38  ? CD  ? B LYS 38  CD  
12 1 Y 1 A LYS 38  ? CE  ? B LYS 38  CE  
13 1 Y 1 A LYS 38  ? NZ  ? B LYS 38  NZ  
14 1 Y 1 A LYS 41  ? CD  ? B LYS 41  CD  
15 1 Y 1 A LYS 41  ? CE  ? B LYS 41  CE  
16 1 Y 1 A LYS 41  ? NZ  ? B LYS 41  NZ  
17 1 Y 1 A GLU 236 ? CG  ? B GLU 236 CG  
18 1 Y 1 A GLU 236 ? CD  ? B GLU 236 CD  
19 1 Y 1 A GLU 236 ? OE1 ? B GLU 236 OE1 
20 1 Y 1 A GLU 236 ? OE2 ? B GLU 236 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? '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                     9FPW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.466 
_cell.length_a_esd                 ? 
_cell.length_b                     58.389 
_cell.length_b_esd                 ? 
_cell.length_c                     160.687 
_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                         9FPW 
_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                   9FPW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.9 
_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         2017-12-19 
_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                                       9FPW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.900 
_reflns.d_resolution_low                               160.687 
_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                                     42102 
_reflns.number_obs                                     42102 
_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                                13.100 
_reflns.pdbx_netI_over_av_sigmaI                       3.800 
_reflns.pdbx_netI_over_sigmaI                          13.000 
_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                                0.122 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       552165 
_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                                0.116 
_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 
1.900 2.000   ? 2.000 81128 ? ? ? 6051 ? ? ? ? ? ? ? ? ? ? ? 13.400 ? ? 7.600  0.331 0.091 ? 1  1 ? ? ? 100.000 ? 0.312 0.312 ? ? 
? ? ? ? ? ? 
2.000 2.120   ? 2.600 73292 ? ? ? 5746 ? ? ? ? ? ? ? ? ? ? ? 12.800 ? ? 8.900  0.246 0.070 ? 2  1 ? ? ? 100.000 ? 0.232 0.232 ? ? 
? ? ? ? ? ? 
2.120 2.270   ? 3.200 70459 ? ? ? 5357 ? ? ? ? ? ? ? ? ? ? ? 13.200 ? ? 10.300 0.203 0.057 ? 3  1 ? ? ? 100.000 ? 0.191 0.191 ? ? 
? ? ? ? ? ? 
2.270 2.450   ? 3.500 68711 ? ? ? 5059 ? ? ? ? ? ? ? ? ? ? ? 13.600 ? ? 11.700 0.174 0.048 ? 4  1 ? ? ? 100.000 ? 0.164 0.164 ? ? 
? ? ? ? ? ? 
2.450 2.690   ? 3.600 61207 ? ? ? 4649 ? ? ? ? ? ? ? ? ? ? ? 13.200 ? ? 12.800 0.159 0.044 ? 5  1 ? ? ? 100.000 ? 0.150 0.150 ? ? 
? ? ? ? ? ? 
2.690 3.000   ? 4.400 55035 ? ? ? 4228 ? ? ? ? ? ? ? ? ? ? ? 13.000 ? ? 15.000 0.141 0.039 ? 6  1 ? ? ? 100.000 ? 0.133 0.133 ? ? 
? ? ? ? ? ? 
3.000 3.470   ? 4.800 51340 ? ? ? 3770 ? ? ? ? ? ? ? ? ? ? ? 13.600 ? ? 18.200 0.130 0.036 ? 7  1 ? ? ? 100.000 ? 0.124 0.124 ? ? 
? ? ? ? ? ? 
3.470 4.250   ? 5.800 39815 ? ? ? 3212 ? ? ? ? ? ? ? ? ? ? ? 12.400 ? ? 19.800 0.109 0.031 ? 8  1 ? ? ? 100.000 ? 0.103 0.103 ? ? 
? ? ? ? ? ? 
4.250 6.010   ? 7.400 33630 ? ? ? 2524 ? ? ? ? ? ? ? ? ? ? ? 13.300 ? ? 21.000 0.086 0.024 ? 9  1 ? ? ? 100.000 ? 0.082 0.082 ? ? 
? ? ? ? ? ? 
6.010 160.687 ? 7.400 17548 ? ? ? 1506 ? ? ? ? ? ? ? ? ? ? ? 11.700 ? ? 18.800 0.073 0.021 ? 10 1 ? ? ? 100.000 ? 0.068 0.068 ? ? 
? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.9200 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.8300 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -1.7600 
_refine.B_iso_max                                88.880 
_refine.B_iso_mean                               25.8660 
_refine.B_iso_min                                10.690 
_refine.correlation_coeff_Fo_to_Fc               0.9470 
_refine.correlation_coeff_Fo_to_Fc_free          0.9230 
_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                                 9FPW 
_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                            1.9000 
_refine.ls_d_res_low                             40.2100 
_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                     37845 
_refine.ls_number_reflns_R_free                  4131 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8500 
_refine.ls_percent_reflns_R_free                 9.8000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1928 
_refine.ls_R_factor_R_free                       0.2329 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1883 
_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                       0.1760 
_refine.pdbx_overall_ESU_R_Free                  0.1580 
_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                       1.9000 
_refine_hist.d_res_low                        40.2100 
_refine_hist.number_atoms_solvent             312 
_refine_hist.number_atoms_total               4457 
_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       517 
_refine_hist.pdbx_B_iso_mean_ligand           34.71 
_refine_hist.pdbx_B_iso_mean_solvent          32.54 
_refine_hist.pdbx_number_atoms_protein        4096 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_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' ? 0.008  0.012  4304 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.567  1.644  5870 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.291  5.000  523  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.152 22.744 215  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 15.034 15.000 678  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.287 15.000 20   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.118  0.200  539  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  3374 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.9000 
_refine_ls_shell.d_res_low                        1.9490 
_refine_ls_shell.number_reflns_all                3038 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             283 
_refine_ls_shell.number_reflns_R_work             2755 
_refine_ls_shell.percent_reflns_obs               99.7700 
_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                  0.2030 
_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                  0.2540 
# 
_struct.entry_id                     9FPW 
_struct.title                        
'Crystal structure of carbonic anhydrase XIII with methyl 4-(2-phenylethylsulfanyl)-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        9FPW 
_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 5 ? 
I N N 5 ? 
# 
_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 9FPW B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 9FPW 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 9FPW MET B 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 1 
2 9FPW 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,H   
2 1 B,E,F,G,I 
# 
_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  ? ILE A 16  ? GLY B 14  ILE B 16  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 17  ? PHE A 22  ? HIS B 17  PHE B 22  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 23  ? GLY A 27  ? PRO B 23  GLY B 27  5 ? 5  
HELX_P HELX_P4  AA4 LYS A 36  ? VAL A 40  ? LYS B 36  VAL B 40  5 ? 5  
HELX_P HELX_P5  AA5 SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 156 ? GLN A 158 ? ASN B 156 GLN B 158 5 ? 3  
HELX_P HELX_P7  AA7 LEU A 159 ? ASP A 164 ? LEU B 159 ASP B 164 1 ? 6  
HELX_P HELX_P8  AA8 THR A 165 ? LYS A 170 ? THR B 165 LYS B 170 5 ? 6  
HELX_P HELX_P9  AA9 ASP A 182 ? LEU A 187 ? ASP B 182 LEU B 187 5 ? 6  
HELX_P HELX_P10 AB1 SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9  
HELX_P HELX_P11 AB2 GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8  
HELX_P HELX_P12 AB3 PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6  
HELX_P HELX_P13 AB4 LYS B 36  ? VAL B 40  ? LYS A 36  VAL A 40  5 ? 5  
HELX_P HELX_P14 AB5 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6  
HELX_P HELX_P15 AB6 ASN B 156 ? GLN B 158 ? ASN A 156 GLN A 158 5 ? 3  
HELX_P HELX_P16 AB7 LEU B 159 ? ASP B 164 ? LEU A 159 ASP A 164 1 ? 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 ? SER B 230 ? SER A 221 SER A 230 1 ? 10 
# 
_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 ? ? ? ? ? ? ? 2.054 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN    . ZN  ? ? B HIS 98  B ZN    301 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc3  metalc ? ? A SER 101 O   ? ? ? 1_555 G NA    . NA  ? ? B SER 101 A NA    303 4_555 ? ? ? ? ? ? ? 2.547 ? ? 
metalc4  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN    . ZN  ? ? B HIS 121 B ZN    301 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D A1IEN . S7  ? ? B ZN  301 B A1IEN 302 1_555 ? ? ? ? ? ? ? 2.959 ? ? 
metalc6  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D A1IEN . N10 ? ? B ZN  301 B A1IEN 302 1_555 ? ? ? ? ? ? ? 1.762 ? ? 
metalc7  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc8  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 98  A ZN    301 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc9  metalc ? ? B HIS 121 ND1 ? ? ? 1_555 E ZN    . ZN  ? ? A HIS 121 A ZN    301 1_555 ? ? ? ? ? ? ? 1.928 ? ? 
metalc10 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F A1IEN . N10 ? ? A ZN  301 A A1IEN 302 1_555 ? ? ? ? ? ? ? 1.894 ? ? 
metalc11 metalc ? ? G NA  .   NA  ? ? ? 1_555 I HOH   . O   ? ? A NA  303 A HOH   415 1_555 ? ? ? ? ? ? ? 2.826 ? ? 
metalc12 metalc ? ? G NA  .   NA  ? ? ? 1_555 I HOH   . O   ? ? A NA  303 A HOH   438 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
# 
_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_555 103.8 ? 
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_555 117.2 ? 
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 93.4  ? 
4  NE2 ? A HIS   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D A1IEN .   ? B A1IEN 302 ? 1_555 89.2  ? 
5  NE2 ? A HIS   98  ? B HIS   98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D A1IEN .   ? B A1IEN 302 ? 1_555 135.9 ? 
6  ND1 ? A HIS   121 ? B HIS   121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D A1IEN .   ? B A1IEN 302 ? 1_555 118.0 ? 
7  NE2 ? A HIS   96  ? B HIS   96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D A1IEN .   ? B A1IEN 302 ? 1_555 117.6 ? 
8  NE2 ? A HIS   98  ? B HIS   98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D A1IEN .   ? B A1IEN 302 ? 1_555 107.6 ? 
9  ND1 ? A HIS   121 ? B HIS   121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D A1IEN .   ? B A1IEN 302 ? 1_555 113.2 ? 
10 S7  ? D A1IEN .   ? B A1IEN 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D A1IEN .   ? B A1IEN 302 ? 1_555 33.6  ? 
11 O   ? A SER   101 ? B SER   101 ? 1_555 NA ? G NA . ? A NA 303 ? 4_555 O   ? I HOH   .   ? A HOH   415 ? 1_555 87.9  ? 
12 O   ? A SER   101 ? B SER   101 ? 1_555 NA ? G NA . ? A NA 303 ? 4_555 O   ? I HOH   .   ? A HOH   438 ? 1_555 83.4  ? 
13 O   ? I HOH   .   ? A HOH   415 ? 1_555 NA ? G NA . ? A NA 303 ? 4_555 O   ? I HOH   .   ? A HOH   438 ? 1_555 5.5   ? 
14 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_555 100.8 ? 
15 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_555 118.0 ? 
16 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_555 101.5 ? 
17 NE2 ? B HIS   96  ? A HIS   96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F A1IEN .   ? A A1IEN 302 ? 1_555 115.7 ? 
18 NE2 ? B HIS   98  ? A HIS   98  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F A1IEN .   ? A A1IEN 302 ? 1_555 105.0 ? 
19 ND1 ? B HIS   121 ? A HIS   121 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N10 ? F A1IEN .   ? A A1IEN 302 ? 1_555 112.8 ? 
# 
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 0.76  
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 8.84  
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -3.93 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 7.94  
# 
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  TYR A 90  ? TRP A 99  ? TYR B 90  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  TYR A 90  ? TRP A 99  ? TYR B 90  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  ARG B 47  ? LYS B 52  ? ARG A 47  LYS A 52  
AA6 2  VAL B 80  ? GLY B 84  ? VAL A 80  GLY A 84  
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 TRP A 194 ? N TRP B 194 O VAL A 213 ? O VAL B 213 
AA2 4 5  O ILE A 212 ? O ILE B 212 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 LYS A 59  ? N LYS B 59  
AA2 9 10 N ILE A 61  ? N ILE B 61  O THR A 176 ? O THR B 176 
AA3 1 2  N LYS A 52  ? N LYS B 52  O VAL A 80  ? O VAL B 80  
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 TRP B 194 ? N TRP A 194 O VAL B 213 ? O VAL A 213 
AA5 4 5  O ILE B 212 ? O ILE A 212 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 GLN B 151 ? N GLN A 151 O ILE B 218 ? O ILE A 218 
# 
_pdbx_entry_details.entry_id                   9FPW 
_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 ASN B 77  ? ? -102.02 40.42 
2 1 HIS B 105 ? ? -153.09 63.99 
3 1 ASN B 246 ? ? -152.34 39.22 
4 1 ASP A 74  ? ? -117.96 52.57 
5 1 ASN A 246 ? ? -146.63 39.90 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    5 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    6 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -127.28 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       559 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.28 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
# 
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 
A1IEN C13  C  N N 1   
A1IEN C20  C  N N 2   
A1IEN C12  C  N N 3   
A1IEN C16  C  Y N 4   
A1IEN O22  O  N N 5   
A1IEN C23  C  N N 6   
A1IEN O21  O  N N 7   
A1IEN C2   C  Y N 8   
A1IEN C3   C  Y N 9   
A1IEN C4   C  Y N 10  
A1IEN C5   C  Y N 11  
A1IEN C6   C  Y N 12  
A1IEN S7   S  N N 13  
A1IEN O9   O  N N 14  
A1IEN N10  N  N N 15  
A1IEN O8   O  N N 16  
A1IEN C1   C  Y N 17  
A1IEN S11  S  N N 18  
A1IEN C14  C  Y N 19  
A1IEN C18  C  Y N 20  
A1IEN C19  C  Y N 21  
A1IEN C17  C  Y N 22  
A1IEN C15  C  Y N 23  
A1IEN H1   H  N N 24  
A1IEN H2   H  N N 25  
A1IEN H3   H  N N 26  
A1IEN H4   H  N N 27  
A1IEN H5   H  N N 28  
A1IEN H6   H  N N 29  
A1IEN H7   H  N N 30  
A1IEN H8   H  N N 31  
A1IEN H9   H  N N 32  
A1IEN H10  H  N N 33  
A1IEN H11  H  N N 34  
A1IEN H12  H  N N 35  
A1IEN H13  H  N N 36  
A1IEN H14  H  N N 37  
A1IEN H15  H  N N 38  
A1IEN H16  H  N N 39  
A1IEN H17  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
HIS   N    N  N N 177 
HIS   CA   C  N S 178 
HIS   C    C  N N 179 
HIS   O    O  N N 180 
HIS   CB   C  N N 181 
HIS   CG   C  Y N 182 
HIS   ND1  N  Y N 183 
HIS   CD2  C  Y N 184 
HIS   CE1  C  Y N 185 
HIS   NE2  N  Y N 186 
HIS   OXT  O  N N 187 
HIS   H    H  N N 188 
HIS   H2   H  N N 189 
HIS   HA   H  N N 190 
HIS   HB2  H  N N 191 
HIS   HB3  H  N N 192 
HIS   HD1  H  N N 193 
HIS   HD2  H  N N 194 
HIS   HE1  H  N N 195 
HIS   HE2  H  N N 196 
HIS   HXT  H  N N 197 
HOH   O    O  N N 198 
HOH   H1   H  N N 199 
HOH   H2   H  N N 200 
ILE   N    N  N N 201 
ILE   CA   C  N S 202 
ILE   C    C  N N 203 
ILE   O    O  N N 204 
ILE   CB   C  N S 205 
ILE   CG1  C  N N 206 
ILE   CG2  C  N N 207 
ILE   CD1  C  N N 208 
ILE   OXT  O  N N 209 
ILE   H    H  N N 210 
ILE   H2   H  N N 211 
ILE   HA   H  N N 212 
ILE   HB   H  N N 213 
ILE   HG12 H  N N 214 
ILE   HG13 H  N N 215 
ILE   HG21 H  N N 216 
ILE   HG22 H  N N 217 
ILE   HG23 H  N N 218 
ILE   HD11 H  N N 219 
ILE   HD12 H  N N 220 
ILE   HD13 H  N N 221 
ILE   HXT  H  N N 222 
LEU   N    N  N N 223 
LEU   CA   C  N S 224 
LEU   C    C  N N 225 
LEU   O    O  N N 226 
LEU   CB   C  N N 227 
LEU   CG   C  N N 228 
LEU   CD1  C  N N 229 
LEU   CD2  C  N N 230 
LEU   OXT  O  N N 231 
LEU   H    H  N N 232 
LEU   H2   H  N N 233 
LEU   HA   H  N N 234 
LEU   HB2  H  N N 235 
LEU   HB3  H  N N 236 
LEU   HG   H  N N 237 
LEU   HD11 H  N N 238 
LEU   HD12 H  N N 239 
LEU   HD13 H  N N 240 
LEU   HD21 H  N N 241 
LEU   HD22 H  N N 242 
LEU   HD23 H  N N 243 
LEU   HXT  H  N N 244 
LYS   N    N  N N 245 
LYS   CA   C  N S 246 
LYS   C    C  N N 247 
LYS   O    O  N N 248 
LYS   CB   C  N N 249 
LYS   CG   C  N N 250 
LYS   CD   C  N N 251 
LYS   CE   C  N N 252 
LYS   NZ   N  N N 253 
LYS   OXT  O  N N 254 
LYS   H    H  N N 255 
LYS   H2   H  N N 256 
LYS   HA   H  N N 257 
LYS   HB2  H  N N 258 
LYS   HB3  H  N N 259 
LYS   HG2  H  N N 260 
LYS   HG3  H  N N 261 
LYS   HD2  H  N N 262 
LYS   HD3  H  N N 263 
LYS   HE2  H  N N 264 
LYS   HE3  H  N N 265 
LYS   HZ1  H  N N 266 
LYS   HZ2  H  N N 267 
LYS   HZ3  H  N N 268 
LYS   HXT  H  N N 269 
MET   N    N  N N 270 
MET   CA   C  N S 271 
MET   C    C  N N 272 
MET   O    O  N N 273 
MET   CB   C  N N 274 
MET   CG   C  N N 275 
MET   SD   S  N N 276 
MET   CE   C  N N 277 
MET   OXT  O  N N 278 
MET   H    H  N N 279 
MET   H2   H  N N 280 
MET   HA   H  N N 281 
MET   HB2  H  N N 282 
MET   HB3  H  N N 283 
MET   HG2  H  N N 284 
MET   HG3  H  N N 285 
MET   HE1  H  N N 286 
MET   HE2  H  N N 287 
MET   HE3  H  N N 288 
MET   HXT  H  N N 289 
NA    NA   NA N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TRP   N    N  N N 362 
TRP   CA   C  N S 363 
TRP   C    C  N N 364 
TRP   O    O  N N 365 
TRP   CB   C  N N 366 
TRP   CG   C  Y N 367 
TRP   CD1  C  Y N 368 
TRP   CD2  C  Y N 369 
TRP   NE1  N  Y N 370 
TRP   CE2  C  Y N 371 
TRP   CE3  C  Y N 372 
TRP   CZ2  C  Y N 373 
TRP   CZ3  C  Y N 374 
TRP   CH2  C  Y N 375 
TRP   OXT  O  N N 376 
TRP   H    H  N N 377 
TRP   H2   H  N N 378 
TRP   HA   H  N N 379 
TRP   HB2  H  N N 380 
TRP   HB3  H  N N 381 
TRP   HD1  H  N N 382 
TRP   HE1  H  N N 383 
TRP   HE3  H  N N 384 
TRP   HZ2  H  N N 385 
TRP   HZ3  H  N N 386 
TRP   HH2  H  N N 387 
TRP   HXT  H  N N 388 
TYR   N    N  N N 389 
TYR   CA   C  N S 390 
TYR   C    C  N N 391 
TYR   O    O  N N 392 
TYR   CB   C  N N 393 
TYR   CG   C  Y N 394 
TYR   CD1  C  Y N 395 
TYR   CD2  C  Y N 396 
TYR   CE1  C  Y N 397 
TYR   CE2  C  Y N 398 
TYR   CZ   C  Y N 399 
TYR   OH   O  N N 400 
TYR   OXT  O  N N 401 
TYR   H    H  N N 402 
TYR   H2   H  N N 403 
TYR   HA   H  N N 404 
TYR   HB2  H  N N 405 
TYR   HB3  H  N N 406 
TYR   HD1  H  N N 407 
TYR   HD2  H  N N 408 
TYR   HE1  H  N N 409 
TYR   HE2  H  N N 410 
TYR   HH   H  N N 411 
TYR   HXT  H  N N 412 
VAL   N    N  N N 413 
VAL   CA   C  N S 414 
VAL   C    C  N N 415 
VAL   O    O  N N 416 
VAL   CB   C  N N 417 
VAL   CG1  C  N N 418 
VAL   CG2  C  N N 419 
VAL   OXT  O  N N 420 
VAL   H    H  N N 421 
VAL   H2   H  N N 422 
VAL   HA   H  N N 423 
VAL   HB   H  N N 424 
VAL   HG11 H  N N 425 
VAL   HG12 H  N N 426 
VAL   HG13 H  N N 427 
VAL   HG21 H  N N 428 
VAL   HG22 H  N N 429 
VAL   HG23 H  N N 430 
VAL   HXT  H  N N 431 
ZN    ZN   ZN N N 432 
# 
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 
A1IEN O21 C20  doub N N 1   
A1IEN C20 O22  sing N N 2   
A1IEN C20 C2   sing N N 3   
A1IEN C23 O22  sing N N 4   
A1IEN C3  C2   doub Y N 5   
A1IEN C3  C4   sing Y N 6   
A1IEN C2  C1   sing Y N 7   
A1IEN C4  C5   doub Y N 8   
A1IEN C19 C18  doub Y N 9   
A1IEN C19 C17  sing Y N 10  
A1IEN C18 C14  sing Y N 11  
A1IEN C17 C16  doub Y N 12  
A1IEN C1  C6   doub Y N 13  
A1IEN C5  C6   sing Y N 14  
A1IEN C5  S11  sing N N 15  
A1IEN C14 C13  sing N N 16  
A1IEN C14 C15  doub Y N 17  
A1IEN C12 C13  sing N N 18  
A1IEN C12 S11  sing N N 19  
A1IEN C6  S7   sing N N 20  
A1IEN C16 C15  sing Y N 21  
A1IEN S7  N10  sing N N 22  
A1IEN S7  O9   doub N N 23  
A1IEN S7  O8   doub N N 24  
A1IEN C13 H1   sing N N 25  
A1IEN C13 H2   sing N N 26  
A1IEN C12 H3   sing N N 27  
A1IEN C12 H4   sing N N 28  
A1IEN C16 H5   sing N N 29  
A1IEN C23 H6   sing N N 30  
A1IEN C23 H7   sing N N 31  
A1IEN C23 H8   sing N N 32  
A1IEN C3  H9   sing N N 33  
A1IEN C4  H10  sing N N 34  
A1IEN N10 H11  sing N N 35  
A1IEN N10 H12  sing N N 36  
A1IEN C1  H13  sing N N 37  
A1IEN C18 H14  sing N N 38  
A1IEN C19 H15  sing N N 39  
A1IEN C17 H16  sing N N 40  
A1IEN C15 H17  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
_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   6G5U 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FPW 
_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]   0.018029 
_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]   0.017127 
_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]   0.006223 
_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  
NA 
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   ? 28.408  -13.496 -11.959 1.00 50.35 ? 6   SER   B N   1 
ATOM   2    C  CA  . SER   A 1 6   ? 27.701  -12.315 -12.540 1.00 48.31 ? 6   SER   B CA  1 
ATOM   3    C  C   . SER   A 1 6   ? 27.925  -11.077 -11.673 1.00 42.48 ? 6   SER   B C   1 
ATOM   4    O  O   . SER   A 1 6   ? 28.042  -11.175 -10.457 1.00 42.72 ? 6   SER   B O   1 
ATOM   5    C  CB  . SER   A 1 6   ? 26.228  -12.591 -12.729 1.00 53.57 ? 6   SER   B CB  1 
ATOM   6    O  OG  . SER   A 1 6   ? 25.910  -12.712 -14.109 1.00 59.61 ? 6   SER   B OG  1 
ATOM   7    N  N   . TRP   A 1 7   ? 27.939  -9.911  -12.322 1.00 36.17 ? 7   TRP   B N   1 
ATOM   8    C  CA  . TRP   A 1 7   ? 28.238  -8.640  -11.688 1.00 30.17 ? 7   TRP   B CA  1 
ATOM   9    C  C   . TRP   A 1 7   ? 27.178  -8.265  -10.653 1.00 29.10 ? 7   TRP   B C   1 
ATOM   10   O  O   . TRP   A 1 7   ? 26.037  -8.710  -10.735 1.00 26.43 ? 7   TRP   B O   1 
ATOM   11   C  CB  . TRP   A 1 7   ? 28.368  -7.564  -12.766 1.00 29.30 ? 7   TRP   B CB  1 
ATOM   12   C  CG  . TRP   A 1 7   ? 27.075  -7.166  -13.414 1.00 29.34 ? 7   TRP   B CG  1 
ATOM   13   C  CD1 . TRP   A 1 7   ? 26.505  -7.723  -14.524 1.00 29.65 ? 7   TRP   B CD1 1 
ATOM   14   C  CD2 . TRP   A 1 7   ? 26.192  -6.099  -12.996 1.00 27.95 ? 7   TRP   B CD2 1 
ATOM   15   N  NE1 . TRP   A 1 7   ? 25.327  -7.083  -14.821 1.00 31.20 ? 7   TRP   B NE1 1 
ATOM   16   C  CE2 . TRP   A 1 7   ? 25.117  -6.073  -13.912 1.00 28.51 ? 7   TRP   B CE2 1 
ATOM   17   C  CE3 . TRP   A 1 7   ? 26.202  -5.175  -11.938 1.00 26.79 ? 7   TRP   B CE3 1 
ATOM   18   C  CZ2 . TRP   A 1 7   ? 24.055  -5.172  -13.782 1.00 29.61 ? 7   TRP   B CZ2 1 
ATOM   19   C  CZ3 . TRP   A 1 7   ? 25.171  -4.260  -11.831 1.00 25.17 ? 7   TRP   B CZ3 1 
ATOM   20   C  CH2 . TRP   A 1 7   ? 24.113  -4.264  -12.742 1.00 26.83 ? 7   TRP   B CH2 1 
ATOM   21   N  N   . GLY   A 1 8   ? 27.565  -7.398  -9.700  1.00 26.25 ? 8   GLY   B N   1 
ATOM   22   C  CA  . GLY   A 1 8   ? 26.678  -6.944  -8.632  1.00 22.97 ? 8   GLY   B CA  1 
ATOM   23   C  C   . GLY   A 1 8   ? 27.321  -5.783  -7.872  1.00 20.44 ? 8   GLY   B C   1 
ATOM   24   O  O   . GLY   A 1 8   ? 28.087  -5.039  -8.470  1.00 20.43 ? 8   GLY   B O   1 
ATOM   25   N  N   . TYR   A 1 9   ? 27.011  -5.640  -6.566  1.00 18.84 ? 9   TYR   B N   1 
ATOM   26   C  CA  . TYR   A 1 9   ? 27.533  -4.544  -5.766  1.00 21.22 ? 9   TYR   B CA  1 
ATOM   27   C  C   . TYR   A 1 9   ? 28.152  -5.065  -4.466  1.00 25.13 ? 9   TYR   B C   1 
ATOM   28   O  O   . TYR   A 1 9   ? 28.303  -4.321  -3.495  1.00 23.40 ? 9   TYR   B O   1 
ATOM   29   C  CB  . TYR   A 1 9   ? 26.394  -3.573  -5.465  1.00 21.83 ? 9   TYR   B CB  1 
ATOM   30   C  CG  . TYR   A 1 9   ? 25.871  -2.879  -6.696  1.00 19.95 ? 9   TYR   B CG  1 
ATOM   31   C  CD1 . TYR   A 1 9   ? 26.470  -1.720  -7.170  1.00 19.43 ? 9   TYR   B CD1 1 
ATOM   32   C  CD2 . TYR   A 1 9   ? 24.768  -3.385  -7.371  1.00 20.17 ? 9   TYR   B CD2 1 
ATOM   33   C  CE1 . TYR   A 1 9   ? 25.955  -1.088  -8.296  1.00 18.97 ? 9   TYR   B CE1 1 
ATOM   34   C  CE2 . TYR   A 1 9   ? 24.223  -2.745  -8.476  1.00 19.45 ? 9   TYR   B CE2 1 
ATOM   35   C  CZ  . TYR   A 1 9   ? 24.849  -1.606  -8.943  1.00 17.84 ? 9   TYR   B CZ  1 
ATOM   36   O  OH  . TYR   A 1 9   ? 24.345  -0.963  -10.032 1.00 18.22 ? 9   TYR   B OH  1 
ATOM   37   N  N   . ARG   A 1 10  ? 28.518  -6.350  -4.465  1.00 24.15 ? 10  ARG   B N   1 
ATOM   38   C  CA  . ARG   A 1 10  ? 29.116  -6.975  -3.289  1.00 29.21 ? 10  ARG   B CA  1 
ATOM   39   C  C   . ARG   A 1 10  ? 30.640  -6.940  -3.419  1.00 30.39 ? 10  ARG   B C   1 
ATOM   40   O  O   . ARG   A 1 10  ? 31.176  -6.526  -4.444  1.00 30.96 ? 10  ARG   B O   1 
ATOM   41   C  CB  . ARG   A 1 10  ? 28.576  -8.399  -3.097  1.00 28.36 ? 10  ARG   B CB  1 
ATOM   42   C  CG  . ARG   A 1 10  ? 27.056  -8.488  -3.039  1.00 33.09 ? 10  ARG   B CG  1 
ATOM   43   C  CD  . ARG   A 1 10  ? 26.527  -9.904  -3.162  1.00 37.96 ? 10  ARG   B CD  1 
ATOM   44   N  NE  . ARG   A 1 10  ? 26.674  -10.681 -1.941  1.00 42.34 ? 10  ARG   B NE  1 
ATOM   45   C  CZ  . ARG   A 1 10  ? 26.259  -11.940 -1.792  1.00 44.11 ? 10  ARG   B CZ  1 
ATOM   46   N  NH1 . ARG   A 1 10  ? 25.654  -12.581 -2.784  1.00 41.82 ? 10  ARG   B NH1 1 
ATOM   47   N  NH2 . ARG   A 1 10  ? 26.448  -12.552 -0.637  1.00 48.19 ? 10  ARG   B NH2 1 
ATOM   48   N  N   . GLU   A 1 11  ? 31.352  -7.421  -2.388  1.00 34.28 ? 11  GLU   B N   1 
ATOM   49   C  CA  . GLU   A 1 11  ? 32.803  -7.263  -2.343  1.00 37.02 ? 11  GLU   B CA  1 
ATOM   50   C  C   . GLU   A 1 11  ? 33.463  -7.820  -3.604  1.00 34.15 ? 11  GLU   B C   1 
ATOM   51   O  O   . GLU   A 1 11  ? 34.339  -7.185  -4.195  1.00 34.32 ? 11  GLU   B O   1 
ATOM   52   C  CB  . GLU   A 1 11  ? 33.423  -7.923  -1.104  1.00 37.43 ? 11  GLU   B CB  1 
ATOM   53   C  CG  . GLU   A 1 11  ? 34.830  -7.407  -0.819  1.00 40.21 ? 11  GLU   B CG  1 
ATOM   54   N  N   . HIS   A 1 12  ? 33.043  -9.021  -3.998  1.00 36.98 ? 12  HIS   B N   1 
ATOM   55   C  CA  . HIS   A 1 12  ? 33.780  -9.768  -4.997  1.00 38.53 ? 12  HIS   B CA  1 
ATOM   56   C  C   . HIS   A 1 12  ? 33.304  -9.440  -6.404  1.00 34.88 ? 12  HIS   B C   1 
ATOM   57   O  O   . HIS   A 1 12  ? 34.033  -9.711  -7.342  1.00 32.45 ? 12  HIS   B O   1 
ATOM   58   C  CB  . HIS   A 1 12  ? 33.705  -11.278 -4.722  1.00 46.36 ? 12  HIS   B CB  1 
ATOM   59   C  CG  . HIS   A 1 12  ? 34.695  -11.778 -3.720  1.00 54.48 ? 12  HIS   B CG  1 
ATOM   60   N  ND1 . HIS   A 1 12  ? 36.006  -11.325 -3.675  1.00 58.46 ? 12  HIS   B ND1 1 
ATOM   61   C  CD2 . HIS   A 1 12  ? 34.590  -12.725 -2.762  1.00 60.58 ? 12  HIS   B CD2 1 
ATOM   62   C  CE1 . HIS   A 1 12  ? 36.656  -11.957 -2.717  1.00 64.29 ? 12  HIS   B CE1 1 
ATOM   63   N  NE2 . HIS   A 1 12  ? 35.806  -12.821 -2.139  1.00 67.10 ? 12  HIS   B NE2 1 
ATOM   64   N  N   . ASN   A 1 13  ? 32.077  -8.911  -6.554  1.00 32.65 ? 13  ASN   B N   1 
ATOM   65   C  CA  . ASN   A 1 13  ? 31.513  -8.709  -7.885  1.00 28.93 ? 13  ASN   B CA  1 
ATOM   66   C  C   . ASN   A 1 13  ? 31.194  -7.233  -8.156  1.00 28.32 ? 13  ASN   B C   1 
ATOM   67   O  O   . ASN   A 1 13  ? 30.566  -6.923  -9.169  1.00 26.58 ? 13  ASN   B O   1 
ATOM   68   C  CB  . ASN   A 1 13  ? 30.315  -9.633  -8.153  1.00 29.15 ? 13  ASN   B CB  1 
ATOM   69   C  CG  . ASN   A 1 13  ? 29.100  -9.313  -7.305  1.00 32.24 ? 13  ASN   B CG  1 
ATOM   70   O  OD1 . ASN   A 1 13  ? 29.121  -8.392  -6.487  1.00 34.20 ? 13  ASN   B OD1 1 
ATOM   71   N  ND2 . ASN   A 1 13  ? 28.037  -10.086 -7.468  1.00 32.97 ? 13  ASN   B ND2 1 
ATOM   72   N  N   . GLY   A 1 14  ? 31.676  -6.337  -7.286  1.00 26.90 ? 14  GLY   B N   1 
ATOM   73   C  CA  . GLY   A 1 14  ? 31.225  -4.948  -7.229  1.00 28.56 ? 14  GLY   B CA  1 
ATOM   74   C  C   . GLY   A 1 14  ? 31.935  -4.005  -8.207  1.00 26.54 ? 14  GLY   B C   1 
ATOM   75   O  O   . GLY   A 1 14  ? 32.847  -4.390  -8.941  1.00 24.94 ? 14  GLY   B O   1 
ATOM   76   N  N   . PRO   A 1 15  ? 31.524  -2.716  -8.251  1.00 24.13 ? 15  PRO   B N   1 
ATOM   77   C  CA  . PRO   A 1 15  ? 32.071  -1.766  -9.215  1.00 23.82 ? 15  PRO   B CA  1 
ATOM   78   C  C   . PRO   A 1 15  ? 33.563  -1.867  -9.519  1.00 25.84 ? 15  PRO   B C   1 
ATOM   79   O  O   . PRO   A 1 15  ? 33.960  -1.748  -10.677 1.00 23.08 ? 15  PRO   B O   1 
ATOM   80   C  CB  . PRO   A 1 15  ? 31.627  -0.418  -8.613  1.00 20.95 ? 15  PRO   B CB  1 
ATOM   81   C  CG  . PRO   A 1 15  ? 30.248  -0.762  -8.114  1.00 20.10 ? 15  PRO   B CG  1 
ATOM   82   C  CD  . PRO   A 1 15  ? 30.439  -2.126  -7.438  1.00 23.85 ? 15  PRO   B CD  1 
ATOM   83   N  N   . ILE   A 1 16  ? 34.387  -2.093  -8.488  1.00 26.26 ? 16  ILE   B N   1 
ATOM   84   C  CA  . ILE   A 1 16  ? 35.824  -2.030  -8.708  1.00 30.01 ? 16  ILE   B CA  1 
ATOM   85   C  C   . ILE   A 1 16  ? 36.280  -3.196  -9.592  1.00 28.46 ? 16  ILE   B C   1 
ATOM   86   O  O   . ILE   A 1 16  ? 37.329  -3.117  -10.219 1.00 30.02 ? 16  ILE   B O   1 
ATOM   87   C  CB  . ILE   A 1 16  ? 36.598  -1.907  -7.375  1.00 31.31 ? 16  ILE   B CB  1 
ATOM   88   C  CG1 . ILE   A 1 16  ? 37.982  -1.287  -7.571  1.00 40.14 ? 16  ILE   B CG1 1 
ATOM   89   C  CG2 . ILE   A 1 16  ? 36.672  -3.230  -6.629  1.00 33.49 ? 16  ILE   B CG2 1 
ATOM   90   N  N   . HIS   A 1 17  ? 35.451  -4.241  -9.695  1.00 31.85 ? 17  HIS   B N   1 
ATOM   91   C  CA  . HIS   A 1 17  ? 35.787  -5.460  -10.420 1.00 31.75 ? 17  HIS   B CA  1 
ATOM   92   C  C   . HIS   A 1 17  ? 35.102  -5.540  -11.786 1.00 34.59 ? 17  HIS   B C   1 
ATOM   93   O  O   . HIS   A 1 17  ? 35.321  -6.494  -12.528 1.00 35.91 ? 17  HIS   B O   1 
ATOM   94   C  CB  . HIS   A 1 17  ? 35.390  -6.698  -9.599  1.00 34.28 ? 17  HIS   B CB  1 
ATOM   95   C  CG  . HIS   A 1 17  ? 36.137  -6.794  -8.316  1.00 38.95 ? 17  HIS   B CG  1 
ATOM   96   N  ND1 . HIS   A 1 17  ? 37.497  -6.979  -8.277  1.00 40.17 ? 17  HIS   B ND1 1 
ATOM   97   C  CD2 . HIS   A 1 17  ? 35.730  -6.690  -7.034  1.00 41.98 ? 17  HIS   B CD2 1 
ATOM   98   C  CE1 . HIS   A 1 17  ? 37.903  -6.996  -7.025  1.00 43.73 ? 17  HIS   B CE1 1 
ATOM   99   N  NE2 . HIS   A 1 17  ? 36.839  -6.821  -6.247  1.00 46.23 ? 17  HIS   B NE2 1 
ATOM   100  N  N   . TRP   A 1 18  ? 34.238  -4.571  -12.116 1.00 30.53 ? 18  TRP   B N   1 
ATOM   101  C  CA  . TRP   A 1 18  ? 33.439  -4.687  -13.323 1.00 27.29 ? 18  TRP   B CA  1 
ATOM   102  C  C   . TRP   A 1 18  ? 34.323  -4.745  -14.568 1.00 29.08 ? 18  TRP   B C   1 
ATOM   103  O  O   . TRP   A 1 18  ? 33.961  -5.364  -15.583 1.00 31.80 ? 18  TRP   B O   1 
ATOM   104  C  CB  . TRP   A 1 18  ? 32.475  -3.500  -13.405 1.00 24.95 ? 18  TRP   B CB  1 
ATOM   105  C  CG  . TRP   A 1 18  ? 31.328  -3.610  -12.461 1.00 21.40 ? 18  TRP   B CG  1 
ATOM   106  C  CD1 . TRP   A 1 18  ? 30.996  -4.674  -11.677 1.00 18.91 ? 18  TRP   B CD1 1 
ATOM   107  C  CD2 . TRP   A 1 18  ? 30.291  -2.628  -12.267 1.00 21.51 ? 18  TRP   B CD2 1 
ATOM   108  N  NE1 . TRP   A 1 18  ? 29.845  -4.417  -10.991 1.00 21.29 ? 18  TRP   B NE1 1 
ATOM   109  C  CE2 . TRP   A 1 18  ? 29.393  -3.166  -11.322 1.00 21.22 ? 18  TRP   B CE2 1 
ATOM   110  C  CE3 . TRP   A 1 18  ? 30.094  -1.329  -12.746 1.00 22.02 ? 18  TRP   B CE3 1 
ATOM   111  C  CZ2 . TRP   A 1 18  ? 28.280  -2.458  -10.848 1.00 23.24 ? 18  TRP   B CZ2 1 
ATOM   112  C  CZ3 . TRP   A 1 18  ? 28.992  -0.629  -12.290 1.00 21.96 ? 18  TRP   B CZ3 1 
ATOM   113  C  CH2 . TRP   A 1 18  ? 28.096  -1.189  -11.362 1.00 23.55 ? 18  TRP   B CH2 1 
ATOM   114  N  N   . LYS   A 1 19  ? 35.459  -4.050  -14.486 1.00 31.86 ? 19  LYS   B N   1 
ATOM   115  C  CA  . LYS   A 1 19  ? 36.373  -3.870  -15.600 1.00 35.25 ? 19  LYS   B CA  1 
ATOM   116  C  C   . LYS   A 1 19  ? 37.033  -5.181  -16.013 1.00 38.93 ? 19  LYS   B C   1 
ATOM   117  O  O   . LYS   A 1 19  ? 37.592  -5.245  -17.100 1.00 43.71 ? 19  LYS   B O   1 
ATOM   118  C  CB  . LYS   A 1 19  ? 37.492  -2.913  -15.206 1.00 36.28 ? 19  LYS   B CB  1 
ATOM   119  C  CG  . LYS   A 1 19  ? 38.502  -3.484  -14.215 1.00 38.15 ? 19  LYS   B CG  1 
ATOM   120  C  CD  . LYS   A 1 19  ? 39.829  -2.786  -14.335 1.00 40.59 ? 19  LYS   B CD  1 
ATOM   121  C  CE  . LYS   A 1 19  ? 40.041  -1.702  -13.300 1.00 48.64 ? 19  LYS   B CE  1 
ATOM   122  N  NZ  . LYS   A 1 19  ? 41.449  -1.235  -13.295 1.00 45.32 ? 19  LYS   B NZ  1 
ATOM   123  N  N   . GLU   A 1 20  ? 36.998  -6.199  -15.143 1.00 45.41 ? 20  GLU   B N   1 
ATOM   124  C  CA  . GLU   A 1 20  ? 37.530  -7.517  -15.472 1.00 52.37 ? 20  GLU   B CA  1 
ATOM   125  C  C   . GLU   A 1 20  ? 36.695  -8.131  -16.598 1.00 54.84 ? 20  GLU   B C   1 
ATOM   126  O  O   . GLU   A 1 20  ? 37.257  -8.662  -17.554 1.00 52.79 ? 20  GLU   B O   1 
ATOM   127  C  CB  . GLU   A 1 20  ? 37.610  -8.429  -14.236 1.00 51.80 ? 20  GLU   B CB  1 
ATOM   128  C  CG  . GLU   A 1 20  ? 38.439  -7.848  -13.086 1.00 51.89 ? 20  GLU   B CG  1 
ATOM   129  C  CD  . GLU   A 1 20  ? 38.230  -8.453  -11.698 1.00 50.09 ? 20  GLU   B CD  1 
ATOM   130  O  OE1 . GLU   A 1 20  ? 37.599  -9.524  -11.608 1.00 47.43 ? 20  GLU   B OE1 1 
ATOM   131  O  OE2 . GLU   A 1 20  ? 38.701  -7.849  -10.700 1.00 46.76 ? 20  GLU   B OE2 1 
ATOM   132  N  N   . PHE   A 1 21  ? 35.361  -8.009  -16.480 1.00 53.34 ? 21  PHE   B N   1 
ATOM   133  C  CA  . PHE   A 1 21  ? 34.395  -8.595  -17.399 1.00 50.12 ? 21  PHE   B CA  1 
ATOM   134  C  C   . PHE   A 1 21  ? 33.970  -7.599  -18.487 1.00 50.03 ? 21  PHE   B C   1 
ATOM   135  O  O   . PHE   A 1 21  ? 33.622  -8.006  -19.594 1.00 46.46 ? 21  PHE   B O   1 
ATOM   136  C  CB  . PHE   A 1 21  ? 33.172  -9.107  -16.628 1.00 66.43 ? 21  PHE   B CB  1 
ATOM   137  C  CG  . PHE   A 1 21  ? 33.170  -10.547 -16.155 1.00 74.24 ? 21  PHE   B CG  1 
ATOM   138  C  CD1 . PHE   A 1 21  ? 34.338  -11.296 -16.074 1.00 77.15 ? 21  PHE   B CD1 1 
ATOM   139  C  CD2 . PHE   A 1 21  ? 31.982  -11.144 -15.743 1.00 75.48 ? 21  PHE   B CD2 1 
ATOM   140  C  CE1 . PHE   A 1 21  ? 34.310  -12.609 -15.622 1.00 80.12 ? 21  PHE   B CE1 1 
ATOM   141  C  CE2 . PHE   A 1 21  ? 31.955  -12.455 -15.288 1.00 77.93 ? 21  PHE   B CE2 1 
ATOM   142  C  CZ  . PHE   A 1 21  ? 33.121  -13.186 -15.227 1.00 76.62 ? 21  PHE   B CZ  1 
ATOM   143  N  N   . PHE   A 1 22  ? 33.950  -6.295  -18.173 1.00 40.81 ? 22  PHE   B N   1 
ATOM   144  C  CA  . PHE   A 1 22  ? 33.485  -5.288  -19.118 1.00 37.25 ? 22  PHE   B CA  1 
ATOM   145  C  C   . PHE   A 1 22  ? 34.541  -4.206  -19.274 1.00 38.17 ? 22  PHE   B C   1 
ATOM   146  O  O   . PHE   A 1 22  ? 34.504  -3.207  -18.567 1.00 41.52 ? 22  PHE   B O   1 
ATOM   147  C  CB  . PHE   A 1 22  ? 32.145  -4.688  -18.683 1.00 32.35 ? 22  PHE   B CB  1 
ATOM   148  C  CG  . PHE   A 1 22  ? 31.051  -5.704  -18.477 1.00 32.58 ? 22  PHE   B CG  1 
ATOM   149  C  CD1 . PHE   A 1 22  ? 30.248  -6.108  -19.537 1.00 29.73 ? 22  PHE   B CD1 1 
ATOM   150  C  CD2 . PHE   A 1 22  ? 30.859  -6.284  -17.235 1.00 29.35 ? 22  PHE   B CD2 1 
ATOM   151  C  CE1 . PHE   A 1 22  ? 29.265  -7.067  -19.355 1.00 32.43 ? 22  PHE   B CE1 1 
ATOM   152  C  CE2 . PHE   A 1 22  ? 29.864  -7.232  -17.042 1.00 33.23 ? 22  PHE   B CE2 1 
ATOM   153  C  CZ  . PHE   A 1 22  ? 29.060  -7.614  -18.103 1.00 36.25 ? 22  PHE   B CZ  1 
ATOM   154  N  N   . PRO   A 1 23  ? 35.503  -4.393  -20.202 1.00 40.12 ? 23  PRO   B N   1 
ATOM   155  C  CA  . PRO   A 1 23  ? 36.616  -3.464  -20.414 1.00 38.52 ? 23  PRO   B CA  1 
ATOM   156  C  C   . PRO   A 1 23  ? 36.302  -1.974  -20.531 1.00 39.70 ? 23  PRO   B C   1 
ATOM   157  O  O   . PRO   A 1 23  ? 37.139  -1.146  -20.176 1.00 34.10 ? 23  PRO   B O   1 
ATOM   158  C  CB  . PRO   A 1 23  ? 37.132  -3.899  -21.792 1.00 39.47 ? 23  PRO   B CB  1 
ATOM   159  C  CG  . PRO   A 1 23  ? 36.895  -5.382  -21.804 1.00 40.39 ? 23  PRO   B CG  1 
ATOM   160  C  CD  . PRO   A 1 23  ? 35.569  -5.557  -21.103 1.00 42.36 ? 23  PRO   B CD  1 
ATOM   161  N  N   . ILE   A 1 24  ? 35.124  -1.637  -21.082 1.00 34.07 ? 24  ILE   B N   1 
ATOM   162  C  CA  . ILE   A 1 24  ? 34.795  -0.237  -21.304 1.00 34.10 ? 24  ILE   B CA  1 
ATOM   163  C  C   . ILE   A 1 24  ? 34.607  0.481   -19.960 1.00 30.80 ? 24  ILE   B C   1 
ATOM   164  O  O   . ILE   A 1 24  ? 34.435  1.700   -19.930 1.00 29.08 ? 24  ILE   B O   1 
ATOM   165  C  CB  . ILE   A 1 24  ? 33.563  -0.100  -22.225 1.00 33.64 ? 24  ILE   B CB  1 
ATOM   166  C  CG1 . ILE   A 1 24  ? 33.395  1.327   -22.753 1.00 35.39 ? 24  ILE   B CG1 1 
ATOM   167  C  CG2 . ILE   A 1 24  ? 32.312  -0.582  -21.522 1.00 31.60 ? 24  ILE   B CG2 1 
ATOM   168  C  CD1 . ILE   A 1 24  ? 34.477  1.771   -23.715 1.00 38.30 ? 24  ILE   B CD1 1 
ATOM   169  N  N   . ALA   A 1 25  ? 34.607  -0.284  -18.859 1.00 28.63 ? 25  ALA   B N   1 
ATOM   170  C  CA  . ALA   A 1 25  ? 34.595  0.285   -17.517 1.00 34.53 ? 25  ALA   B CA  1 
ATOM   171  C  C   . ALA   A 1 25  ? 35.680  1.348   -17.343 1.00 35.47 ? 25  ALA   B C   1 
ATOM   172  O  O   . ALA   A 1 25  ? 35.497  2.276   -16.555 1.00 34.12 ? 25  ALA   B O   1 
ATOM   173  C  CB  . ALA   A 1 25  ? 34.688  -0.789  -16.468 1.00 29.26 ? 25  ALA   B CB  1 
ATOM   174  N  N   . ASP   A 1 26  ? 36.769  1.237   -18.122 1.00 40.25 ? 26  ASP   B N   1 
ATOM   175  C  CA  . ASP   A 1 26  ? 37.916  2.127   -18.016 1.00 42.42 ? 26  ASP   B CA  1 
ATOM   176  C  C   . ASP   A 1 26  ? 37.930  3.173   -19.130 1.00 40.08 ? 26  ASP   B C   1 
ATOM   177  O  O   . ASP   A 1 26  ? 38.958  3.823   -19.335 1.00 37.39 ? 26  ASP   B O   1 
ATOM   178  C  CB  . ASP   A 1 26  ? 39.234  1.346   -18.025 1.00 52.81 ? 26  ASP   B CB  1 
ATOM   179  C  CG  . ASP   A 1 26  ? 39.611  0.773   -16.669 1.00 63.50 ? 26  ASP   B CG  1 
ATOM   180  O  OD1 . ASP   A 1 26  ? 39.280  1.415   -15.646 1.00 65.20 ? 26  ASP   B OD1 1 
ATOM   181  O  OD2 . ASP   A 1 26  ? 40.232  -0.313  -16.641 1.00 71.60 ? 26  ASP   B OD2 1 
ATOM   182  N  N   . GLY   A 1 27  ? 36.783  3.375   -19.799 1.00 38.54 ? 27  GLY   B N   1 
ATOM   183  C  CA  . GLY   A 1 27  ? 36.679  4.265   -20.957 1.00 34.31 ? 27  GLY   B CA  1 
ATOM   184  C  C   . GLY   A 1 27  ? 36.774  5.748   -20.597 1.00 35.51 ? 27  GLY   B C   1 
ATOM   185  O  O   . GLY   A 1 27  ? 36.863  6.100   -19.419 1.00 36.02 ? 27  GLY   B O   1 
ATOM   186  N  N   . ASP   A 1 28  ? 36.750  6.613   -21.625 1.00 32.87 ? 28  ASP   B N   1 
ATOM   187  C  CA  . ASP   A 1 28  ? 36.885  8.053   -21.443 1.00 31.64 ? 28  ASP   B CA  1 
ATOM   188  C  C   . ASP   A 1 28  ? 35.524  8.738   -21.300 1.00 27.71 ? 28  ASP   B C   1 
ATOM   189  O  O   . ASP   A 1 28  ? 35.472  9.942   -21.081 1.00 25.94 ? 28  ASP   B O   1 
ATOM   190  C  CB  . ASP   A 1 28  ? 37.686  8.705   -22.575 1.00 41.72 ? 28  ASP   B CB  1 
ATOM   191  C  CG  . ASP   A 1 28  ? 39.164  8.331   -22.619 1.00 51.13 ? 28  ASP   B CG  1 
ATOM   192  O  OD1 . ASP   A 1 28  ? 39.478  7.122   -22.490 1.00 52.09 ? 28  ASP   B OD1 1 
ATOM   193  O  OD2 . ASP   A 1 28  ? 39.998  9.254   -22.794 1.00 56.31 ? 28  ASP   B OD2 1 
ATOM   194  N  N   . GLN   A 1 29  ? 34.416  7.989   -21.403 1.00 25.28 ? 29  GLN   B N   1 
ATOM   195  C  CA  . GLN   A 1 29  ? 33.131  8.648   -21.195 1.00 24.79 ? 29  GLN   B CA  1 
ATOM   196  C  C   . GLN   A 1 29  ? 32.253  7.861   -20.224 1.00 21.91 ? 29  GLN   B C   1 
ATOM   197  O  O   . GLN   A 1 29  ? 31.132  7.455   -20.568 1.00 20.00 ? 29  GLN   B O   1 
ATOM   198  C  CB  . GLN   A 1 29  ? 32.453  8.969   -22.525 1.00 25.48 ? 29  GLN   B CB  1 
ATOM   199  C  CG  . GLN   A 1 29  ? 33.248  9.992   -23.348 1.00 34.81 ? 29  GLN   B CG  1 
ATOM   200  C  CD  . GLN   A 1 29  ? 32.388  10.817  -24.276 1.00 36.72 ? 29  GLN   B CD  1 
ATOM   201  O  OE1 . GLN   A 1 29  ? 31.388  10.327  -24.812 1.00 35.06 ? 29  GLN   B OE1 1 
ATOM   202  N  NE2 . GLN   A 1 29  ? 32.763  12.079  -24.451 1.00 35.84 ? 29  GLN   B NE2 1 
ATOM   203  N  N   . GLN   A 1 30  ? 32.783  7.624   -19.019 1.00 19.75 ? 30  GLN   B N   1 
ATOM   204  C  CA  . GLN   A 1 30  ? 32.091  6.799   -18.032 1.00 18.33 ? 30  GLN   B CA  1 
ATOM   205  C  C   . GLN   A 1 30  ? 31.264  7.666   -17.084 1.00 16.68 ? 30  GLN   B C   1 
ATOM   206  O  O   . GLN   A 1 30  ? 31.598  8.820   -16.833 1.00 17.81 ? 30  GLN   B O   1 
ATOM   207  C  CB  . GLN   A 1 30  ? 33.057  5.855   -17.297 1.00 18.53 ? 30  GLN   B CB  1 
ATOM   208  C  CG  . GLN   A 1 30  ? 33.561  4.681   -18.147 1.00 17.06 ? 30  GLN   B CG  1 
ATOM   209  C  CD  . GLN   A 1 30  ? 32.471  3.696   -18.478 1.00 17.08 ? 30  GLN   B CD  1 
ATOM   210  O  OE1 . GLN   A 1 30  ? 31.965  2.997   -17.617 1.00 19.72 ? 30  GLN   B OE1 1 
ATOM   211  N  NE2 . GLN   A 1 30  ? 32.101  3.618   -19.747 1.00 18.94 ? 30  GLN   B NE2 1 
ATOM   212  N  N   . SER   A 1 31  ? 30.185  7.075   -16.548 1.00 16.80 ? 31  SER   B N   1 
ATOM   213  C  CA  . SER   A 1 31  ? 29.237  7.753   -15.670 1.00 16.82 ? 31  SER   B CA  1 
ATOM   214  C  C   . SER   A 1 31  ? 29.096  6.922   -14.403 1.00 16.43 ? 31  SER   B C   1 
ATOM   215  O  O   . SER   A 1 31  ? 29.355  5.715   -14.479 1.00 17.19 ? 31  SER   B O   1 
ATOM   216  C  CB  . SER   A 1 31  ? 27.898  7.862   -16.388 1.00 16.64 ? 31  SER   B CB  1 
ATOM   217  O  OG  . SER   A 1 31  ? 28.005  8.838   -17.408 1.00 18.72 ? 31  SER   B OG  1 
ATOM   218  N  N   . PRO   A 1 32  ? 28.690  7.477   -13.221 1.00 16.53 ? 32  PRO   B N   1 
ATOM   219  C  CA  . PRO   A 1 32  ? 28.334  8.898   -13.035 1.00 15.36 ? 32  PRO   B CA  1 
ATOM   220  C  C   . PRO   A 1 32  ? 29.570  9.758   -12.794 1.00 16.65 ? 32  PRO   B C   1 
ATOM   221  O  O   . PRO   A 1 32  ? 30.694  9.249   -12.822 1.00 17.62 ? 32  PRO   B O   1 
ATOM   222  C  CB  . PRO   A 1 32  ? 27.474  8.859   -11.753 1.00 15.49 ? 32  PRO   B CB  1 
ATOM   223  C  CG  . PRO   A 1 32  ? 28.162  7.737   -10.937 1.00 14.54 ? 32  PRO   B CG  1 
ATOM   224  C  CD  . PRO   A 1 32  ? 28.467  6.690   -11.991 1.00 14.88 ? 32  PRO   B CD  1 
ATOM   225  N  N   . ILE   A 1 33  ? 29.358  11.051  -12.541 1.00 17.47 ? 33  ILE   B N   1 
ATOM   226  C  CA  . ILE   A 1 33  ? 30.464  11.968  -12.288 1.00 19.77 ? 33  ILE   B CA  1 
ATOM   227  C  C   . ILE   A 1 33  ? 30.141  12.874  -11.098 1.00 20.63 ? 33  ILE   B C   1 
ATOM   228  O  O   . ILE   A 1 33  ? 29.002  12.979  -10.658 1.00 21.06 ? 33  ILE   B O   1 
ATOM   229  C  CB  . ILE   A 1 33  ? 30.764  12.860  -13.516 1.00 20.14 ? 33  ILE   B CB  1 
ATOM   230  C  CG1 . ILE   A 1 33  ? 29.524  13.667  -13.941 1.00 17.97 ? 33  ILE   B CG1 1 
ATOM   231  C  CG2 . ILE   A 1 33  ? 31.353  12.062  -14.671 1.00 22.57 ? 33  ILE   B CG2 1 
ATOM   232  C  CD1 . ILE   A 1 33  ? 29.850  14.848  -14.802 1.00 19.59 ? 33  ILE   B CD1 1 
ATOM   233  N  N   . GLU   A 1 34  ? 31.176  13.597  -10.649 1.00 21.33 ? 34  GLU   B N   1 
ATOM   234  C  CA  . GLU   A 1 34  ? 31.047  14.726  -9.749  1.00 23.35 ? 34  GLU   B CA  1 
ATOM   235  C  C   . GLU   A 1 34  ? 30.694  15.967  -10.559 1.00 22.66 ? 34  GLU   B C   1 
ATOM   236  O  O   . GLU   A 1 34  ? 31.375  16.290  -11.537 1.00 21.78 ? 34  GLU   B O   1 
ATOM   237  C  CB  . GLU   A 1 34  ? 32.386  14.926  -9.029  1.00 28.55 ? 34  GLU   B CB  1 
ATOM   238  C  CG  . GLU   A 1 34  ? 32.362  16.105  -8.072  1.00 35.21 ? 34  GLU   B CG  1 
ATOM   239  C  CD  . GLU   A 1 34  ? 31.658  15.845  -6.747  1.00 35.90 ? 34  GLU   B CD  1 
ATOM   240  O  OE1 . GLU   A 1 34  ? 32.018  14.841  -6.075  1.00 39.06 ? 34  GLU   B OE1 1 
ATOM   241  O  OE2 . GLU   A 1 34  ? 30.761  16.652  -6.385  1.00 36.35 ? 34  GLU   B OE2 1 
ATOM   242  N  N   . ILE   A 1 35  ? 29.609  16.649  -10.172 1.00 22.06 ? 35  ILE   B N   1 
ATOM   243  C  CA  . ILE   A 1 35  ? 29.211  17.862  -10.861 1.00 22.14 ? 35  ILE   B CA  1 
ATOM   244  C  C   . ILE   A 1 35  ? 29.693  18.998  -9.975  1.00 23.57 ? 35  ILE   B C   1 
ATOM   245  O  O   . ILE   A 1 35  ? 29.173  19.170  -8.874  1.00 23.47 ? 35  ILE   B O   1 
ATOM   246  C  CB  . ILE   A 1 35  ? 27.681  17.921  -11.048 1.00 23.80 ? 35  ILE   B CB  1 
ATOM   247  C  CG1 . ILE   A 1 35  ? 27.157  16.756  -11.885 1.00 23.05 ? 35  ILE   B CG1 1 
ATOM   248  C  CG2 . ILE   A 1 35  ? 27.248  19.260  -11.638 1.00 22.69 ? 35  ILE   B CG2 1 
ATOM   249  C  CD1 . ILE   A 1 35  ? 25.629  16.641  -11.916 1.00 24.75 ? 35  ILE   B CD1 1 
ATOM   250  N  N   . LYS   A 1 36  ? 30.719  19.724  -10.432 1.00 25.43 ? 36  LYS   B N   1 
ATOM   251  C  CA  . LYS   A 1 36  ? 31.176  20.891  -9.694  1.00 24.71 ? 36  LYS   B CA  1 
ATOM   252  C  C   . LYS   A 1 36  ? 30.541  22.130  -10.312 1.00 26.57 ? 36  LYS   B C   1 
ATOM   253  O  O   . LYS   A 1 36  ? 30.971  22.575  -11.371 1.00 25.79 ? 36  LYS   B O   1 
ATOM   254  C  CB  . LYS   A 1 36  ? 32.696  21.035  -9.714  1.00 25.79 ? 36  LYS   B CB  1 
ATOM   255  C  CG  . LYS   A 1 36  ? 33.471  19.881  -9.092  1.00 29.97 ? 36  LYS   B CG  1 
ATOM   256  C  CD  . LYS   A 1 36  ? 34.956  20.181  -9.133  1.00 30.92 ? 36  LYS   B CD  1 
ATOM   257  C  CE  . LYS   A 1 36  ? 35.808  19.289  -8.260  1.00 35.26 ? 36  LYS   B CE  1 
ATOM   258  N  NZ  . LYS   A 1 36  ? 37.190  19.215  -8.797  1.00 31.40 ? 36  LYS   B NZ  1 
ATOM   259  N  N   . THR   A 1 37  ? 29.587  22.714  -9.585  1.00 29.85 ? 37  THR   B N   1 
ATOM   260  C  CA  . THR   A 1 37  ? 28.680  23.720  -10.118 1.00 32.34 ? 37  THR   B CA  1 
ATOM   261  C  C   . THR   A 1 37  ? 29.432  24.942  -10.633 1.00 37.04 ? 37  THR   B C   1 
ATOM   262  O  O   . THR   A 1 37  ? 29.047  25.513  -11.654 1.00 35.42 ? 37  THR   B O   1 
ATOM   263  C  CB  . THR   A 1 37  ? 27.606  24.102  -9.095  1.00 35.77 ? 37  THR   B CB  1 
ATOM   264  O  OG1 . THR   A 1 37  ? 28.280  24.452  -7.891  1.00 38.13 ? 37  THR   B OG1 1 
ATOM   265  C  CG2 . THR   A 1 37  ? 26.634  22.978  -8.826  1.00 38.71 ? 37  THR   B CG2 1 
ATOM   266  N  N   . LYS   A 1 38  ? 30.513  25.327  -9.945  1.00 34.62 ? 38  LYS   B N   1 
ATOM   267  C  CA  . LYS   A 1 38  ? 31.250  26.527  -10.308 1.00 39.16 ? 38  LYS   B CA  1 
ATOM   268  C  C   . LYS   A 1 38  ? 32.060  26.298  -11.590 1.00 40.85 ? 38  LYS   B C   1 
ATOM   269  O  O   . LYS   A 1 38  ? 32.519  27.267  -12.199 1.00 40.09 ? 38  LYS   B O   1 
ATOM   270  C  CB  . LYS   A 1 38  ? 32.070  27.032  -9.116  1.00 38.46 ? 38  LYS   B CB  1 
ATOM   271  C  CG  . LYS   A 1 38  ? 31.298  27.892  -8.121  1.00 44.09 ? 38  LYS   B CG  1 
ATOM   272  C  CD  . LYS   A 1 38  ? 31.673  29.376  -8.168  1.00 49.82 ? 38  LYS   B CD  1 
ATOM   273  C  CE  . LYS   A 1 38  ? 30.517  30.331  -7.948  1.00 48.83 ? 38  LYS   B CE  1 
ATOM   274  N  NZ  . LYS   A 1 38  ? 29.983  30.273  -6.565  1.00 50.92 ? 38  LYS   B NZ  1 
ATOM   275  N  N   . GLU   A 1 39  ? 32.208  25.030  -12.026 1.00 35.34 ? 39  GLU   B N   1 
ATOM   276  C  CA  . GLU   A 1 39  ? 32.966  24.770  -13.242 1.00 37.32 ? 39  GLU   B CA  1 
ATOM   277  C  C   . GLU   A 1 39  ? 32.063  24.520  -14.444 1.00 36.20 ? 39  GLU   B C   1 
ATOM   278  O  O   . GLU   A 1 39  ? 32.541  24.504  -15.575 1.00 40.95 ? 39  GLU   B O   1 
ATOM   279  C  CB  . GLU   A 1 39  ? 33.966  23.622  -13.092 1.00 44.46 ? 39  GLU   B CB  1 
ATOM   280  C  CG  . GLU   A 1 39  ? 35.361  24.106  -12.719 1.00 48.83 ? 39  GLU   B CG  1 
ATOM   281  C  CD  . GLU   A 1 39  ? 35.422  24.679  -11.314 1.00 53.99 ? 39  GLU   B CD  1 
ATOM   282  O  OE1 . GLU   A 1 39  ? 35.176  23.910  -10.369 1.00 58.48 ? 39  GLU   B OE1 1 
ATOM   283  O  OE2 . GLU   A 1 39  ? 35.699  25.892  -11.167 1.00 60.18 ? 39  GLU   B OE2 1 
ATOM   284  N  N   . VAL   A 1 40  ? 30.779  24.275  -14.199 1.00 34.29 ? 40  VAL   B N   1 
ATOM   285  C  CA  . VAL   A 1 40  ? 29.857  23.941  -15.277 1.00 34.01 ? 40  VAL   B CA  1 
ATOM   286  C  C   . VAL   A 1 40  ? 29.600  25.217  -16.074 1.00 35.67 ? 40  VAL   B C   1 
ATOM   287  O  O   . VAL   A 1 40  ? 29.578  26.306  -15.505 1.00 40.54 ? 40  VAL   B O   1 
ATOM   288  C  CB  . VAL   A 1 40  ? 28.557  23.344  -14.700 1.00 31.73 ? 40  VAL   B CB  1 
ATOM   289  C  CG1 . VAL   A 1 40  ? 27.476  23.150  -15.747 1.00 34.52 ? 40  VAL   B CG1 1 
ATOM   290  C  CG2 . VAL   A 1 40  ? 28.820  22.051  -13.947 1.00 33.19 ? 40  VAL   B CG2 1 
ATOM   291  N  N   . LYS   A 1 41  ? 29.400  25.091  -17.387 1.00 37.06 ? 41  LYS   B N   1 
ATOM   292  C  CA  . LYS   A 1 41  ? 29.118  26.294  -18.152 1.00 38.30 ? 41  LYS   B CA  1 
ATOM   293  C  C   . LYS   A 1 41  ? 27.651  26.345  -18.576 1.00 34.80 ? 41  LYS   B C   1 
ATOM   294  O  O   . LYS   A 1 41  ? 27.093  25.373  -19.094 1.00 28.27 ? 41  LYS   B O   1 
ATOM   295  C  CB  . LYS   A 1 41  ? 30.094  26.453  -19.322 1.00 43.87 ? 41  LYS   B CB  1 
ATOM   296  C  CG  . LYS   A 1 41  ? 30.664  27.857  -19.506 1.00 52.66 ? 41  LYS   B CG  1 
ATOM   297  C  CD  . LYS   A 1 41  ? 30.525  28.763  -18.292 1.00 55.01 ? 41  LYS   B CD  1 
ATOM   298  C  CE  . LYS   A 1 41  ? 29.348  29.716  -18.391 1.00 57.06 ? 41  LYS   B CE  1 
ATOM   299  N  NZ  . LYS   A 1 41  ? 28.561  29.748  -17.134 1.00 50.55 ? 41  LYS   B NZ  1 
ATOM   300  N  N   . TYR   A 1 42  ? 27.058  27.521  -18.375 1.00 33.54 ? 42  TYR   B N   1 
ATOM   301  C  CA  . TYR   A 1 42  ? 25.737  27.821  -18.890 1.00 34.62 ? 42  TYR   B CA  1 
ATOM   302  C  C   . TYR   A 1 42  ? 25.781  27.878  -20.417 1.00 32.49 ? 42  TYR   B C   1 
ATOM   303  O  O   . TYR   A 1 42  ? 26.594  28.605  -20.981 1.00 32.07 ? 42  TYR   B O   1 
ATOM   304  C  CB  . TYR   A 1 42  ? 25.206  29.114  -18.262 1.00 38.44 ? 42  TYR   B CB  1 
ATOM   305  C  CG  . TYR   A 1 42  ? 24.009  29.674  -18.988 1.00 38.67 ? 42  TYR   B CG  1 
ATOM   306  C  CD1 . TYR   A 1 42  ? 22.817  28.971  -19.023 1.00 36.47 ? 42  TYR   B CD1 1 
ATOM   307  C  CD2 . TYR   A 1 42  ? 24.076  30.882  -19.674 1.00 41.75 ? 42  TYR   B CD2 1 
ATOM   308  C  CE1 . TYR   A 1 42  ? 21.712  29.461  -19.698 1.00 42.22 ? 42  TYR   B CE1 1 
ATOM   309  C  CE2 . TYR   A 1 42  ? 22.974  31.400  -20.339 1.00 43.27 ? 42  TYR   B CE2 1 
ATOM   310  C  CZ  . TYR   A 1 42  ? 21.786  30.681  -20.352 1.00 45.21 ? 42  TYR   B CZ  1 
ATOM   311  O  OH  . TYR   A 1 42  ? 20.687  31.155  -21.007 1.00 43.20 ? 42  TYR   B OH  1 
ATOM   312  N  N   . ASP   A 1 43  ? 24.918  27.089  -21.081 1.00 28.25 ? 43  ASP   B N   1 
ATOM   313  C  CA  . ASP   A 1 43  ? 24.855  27.087  -22.537 1.00 28.70 ? 43  ASP   B CA  1 
ATOM   314  C  C   . ASP   A 1 43  ? 23.473  27.558  -22.990 1.00 30.92 ? 43  ASP   B C   1 
ATOM   315  O  O   . ASP   A 1 43  ? 22.494  26.801  -22.965 1.00 30.33 ? 43  ASP   B O   1 
ATOM   316  C  CB  . ASP   A 1 43  ? 25.249  25.728  -23.124 1.00 29.33 ? 43  ASP   B CB  1 
ATOM   317  C  CG  . ASP   A 1 43  ? 25.401  25.691  -24.638 1.00 32.66 ? 43  ASP   B CG  1 
ATOM   318  O  OD1 . ASP   A 1 43  ? 25.011  26.680  -25.307 1.00 38.02 ? 43  ASP   B OD1 1 
ATOM   319  O  OD2 . ASP   A 1 43  ? 25.867  24.661  -25.149 1.00 32.24 ? 43  ASP   B OD2 1 
ATOM   320  N  N   . SER   A 1 44  ? 23.425  28.800  -23.478 1.00 31.37 ? 44  SER   B N   1 
ATOM   321  C  CA  . SER   A 1 44  ? 22.222  29.447  -23.981 1.00 33.62 ? 44  SER   B CA  1 
ATOM   322  C  C   . SER   A 1 44  ? 21.678  28.737  -25.226 1.00 36.61 ? 44  SER   B C   1 
ATOM   323  O  O   . SER   A 1 44  ? 20.561  29.005  -25.656 1.00 44.78 ? 44  SER   B O   1 
ATOM   324  C  CB  . SER   A 1 44  ? 22.512  30.902  -24.292 1.00 35.72 ? 44  SER   B CB  1 
ATOM   325  O  OG  . SER   A 1 44  ? 22.948  30.988  -25.642 1.00 35.81 ? 44  SER   B OG  1 
ATOM   326  N  N   . SER   A 1 45  ? 22.448  27.818  -25.811 1.00 36.09 ? 45  SER   B N   1 
ATOM   327  C  CA  . SER   A 1 45  ? 21.975  27.087  -26.968 1.00 32.74 ? 45  SER   B CA  1 
ATOM   328  C  C   . SER   A 1 45  ? 21.196  25.830  -26.558 1.00 35.80 ? 45  SER   B C   1 
ATOM   329  O  O   . SER   A 1 45  ? 20.569  25.213  -27.421 1.00 34.19 ? 45  SER   B O   1 
ATOM   330  C  CB  . SER   A 1 45  ? 23.109  26.779  -27.918 1.00 39.43 ? 45  SER   B CB  1 
ATOM   331  O  OG  . SER   A 1 45  ? 23.494  25.408  -27.860 1.00 38.32 ? 45  SER   B OG  1 
ATOM   332  N  N   . LEU   A 1 46  ? 21.264  25.430  -25.265 1.00 29.35 ? 46  LEU   B N   1 
ATOM   333  C  CA  . LEU   A 1 46  ? 20.486  24.303  -24.754 1.00 26.12 ? 46  LEU   B CA  1 
ATOM   334  C  C   . LEU   A 1 46  ? 18.998  24.662  -24.810 1.00 27.73 ? 46  LEU   B C   1 
ATOM   335  O  O   . LEU   A 1 46  ? 18.641  25.832  -24.743 1.00 26.55 ? 46  LEU   B O   1 
ATOM   336  C  CB  . LEU   A 1 46  ? 20.918  23.965  -23.320 1.00 21.91 ? 46  LEU   B CB  1 
ATOM   337  C  CG  . LEU   A 1 46  ? 22.226  23.169  -23.161 1.00 21.68 ? 46  LEU   B CG  1 
ATOM   338  C  CD1 . LEU   A 1 46  ? 22.583  23.022  -21.666 1.00 18.85 ? 46  LEU   B CD1 1 
ATOM   339  C  CD2 . LEU   A 1 46  ? 22.114  21.780  -23.789 1.00 20.95 ? 46  LEU   B CD2 1 
ATOM   340  N  N   . ARG   A 1 47  ? 18.134  23.649  -24.950 1.00 27.33 ? 47  ARG   B N   1 
ATOM   341  C  CA  . ARG   A 1 47  ? 16.704  23.908  -25.011 1.00 25.30 ? 47  ARG   B CA  1 
ATOM   342  C  C   . ARG   A 1 47  ? 16.006  23.361  -23.763 1.00 23.23 ? 47  ARG   B C   1 
ATOM   343  O  O   . ARG   A 1 47  ? 16.503  22.452  -23.099 1.00 23.33 ? 47  ARG   B O   1 
ATOM   344  C  CB  . ARG   A 1 47  ? 16.103  23.338  -26.299 1.00 27.51 ? 47  ARG   B CB  1 
ATOM   345  C  CG  . ARG   A 1 47  ? 16.561  24.067  -27.563 1.00 34.56 ? 47  ARG   B CG  1 
ATOM   346  C  CD  . ARG   A 1 47  ? 15.898  23.275  -28.689 1.00 40.64 ? 47  ARG   B CD  1 
ATOM   347  N  NE  . ARG   A 1 47  ? 16.105  23.656  -30.082 1.00 48.21 ? 47  ARG   B NE  1 
ATOM   348  C  CZ  . ARG   A 1 47  ? 16.037  22.771  -31.076 1.00 49.83 ? 47  ARG   B CZ  1 
ATOM   349  N  NH1 . ARG   A 1 47  ? 15.766  21.495  -30.807 1.00 51.45 ? 47  ARG   B NH1 1 
ATOM   350  N  NH2 . ARG   A 1 47  ? 16.252  23.157  -32.321 1.00 49.89 ? 47  ARG   B NH2 1 
ATOM   351  N  N   . PRO   A 1 48  ? 14.801  23.884  -23.451 1.00 21.21 ? 48  PRO   B N   1 
ATOM   352  C  CA  . PRO   A 1 48  ? 13.984  23.381  -22.343 1.00 20.22 ? 48  PRO   B CA  1 
ATOM   353  C  C   . PRO   A 1 48  ? 13.572  21.930  -22.577 1.00 17.66 ? 48  PRO   B C   1 
ATOM   354  O  O   . PRO   A 1 48  ? 13.424  21.507  -23.723 1.00 17.08 ? 48  PRO   B O   1 
ATOM   355  C  CB  . PRO   A 1 48  ? 12.709  24.235  -22.419 1.00 21.08 ? 48  PRO   B CB  1 
ATOM   356  C  CG  . PRO   A 1 48  ? 13.128  25.483  -23.158 1.00 25.26 ? 48  PRO   B CG  1 
ATOM   357  C  CD  . PRO   A 1 48  ? 14.192  25.041  -24.144 1.00 21.21 ? 48  PRO   B CD  1 
ATOM   358  N  N   . LEU   A 1 49  ? 13.492  21.160  -21.483 1.00 16.92 ? 49  LEU   B N   1 
ATOM   359  C  CA  . LEU   A 1 49  ? 12.963  19.810  -21.557 1.00 19.00 ? 49  LEU   B CA  1 
ATOM   360  C  C   . LEU   A 1 49  ? 11.462  19.884  -21.825 1.00 19.88 ? 49  LEU   B C   1 
ATOM   361  O  O   . LEU   A 1 49  ? 10.756  20.723  -21.258 1.00 19.07 ? 49  LEU   B O   1 
ATOM   362  C  CB  . LEU   A 1 49  ? 13.267  19.083  -20.243 1.00 18.81 ? 49  LEU   B CB  1 
ATOM   363  C  CG  . LEU   A 1 49  ? 14.746  18.853  -19.915 1.00 19.87 ? 49  LEU   B CG  1 
ATOM   364  C  CD1 . LEU   A 1 49  ? 14.888  18.191  -18.555 1.00 19.49 ? 49  LEU   B CD1 1 
ATOM   365  C  CD2 . LEU   A 1 49  ? 15.408  17.978  -20.970 1.00 23.58 ? 49  LEU   B CD2 1 
ATOM   366  N  N   . SER   A 1 50  ? 10.999  18.996  -22.707 1.00 19.79 ? 50  SER   B N   1 
ATOM   367  C  CA  . SER   A 1 50  ? 9.588   18.868  -22.999 1.00 21.24 ? 50  SER   B CA  1 
ATOM   368  C  C   . SER   A 1 50  ? 9.244   17.400  -22.796 1.00 20.70 ? 50  SER   B C   1 
ATOM   369  O  O   . SER   A 1 50  ? 9.820   16.553  -23.479 1.00 20.05 ? 50  SER   B O   1 
ATOM   370  C  CB  . SER   A 1 50  ? 9.354   19.321  -24.415 1.00 23.22 ? 50  SER   B CB  1 
ATOM   371  O  OG  . SER   A 1 50  ? 8.065   18.942  -24.890 1.00 27.11 ? 50  SER   B OG  1 
ATOM   372  N  N   . ILE   A 1 51  ? 8.379   17.104  -21.818 1.00 21.78 ? 51  ILE   B N   1 
ATOM   373  C  CA  . ILE   A 1 51  ? 8.146   15.722  -21.407 1.00 22.26 ? 51  ILE   B CA  1 
ATOM   374  C  C   . ILE   A 1 51  ? 6.671   15.390  -21.560 1.00 24.07 ? 51  ILE   B C   1 
ATOM   375  O  O   . ILE   A 1 51  ? 5.825   16.159  -21.112 1.00 22.26 ? 51  ILE   B O   1 
ATOM   376  C  CB  . ILE   A 1 51  ? 8.585   15.531  -19.936 1.00 25.47 ? 51  ILE   B CB  1 
ATOM   377  C  CG1 . ILE   A 1 51  ? 10.083  15.814  -19.795 1.00 25.36 ? 51  ILE   B CG1 1 
ATOM   378  C  CG2 . ILE   A 1 51  ? 8.197   14.128  -19.473 1.00 25.10 ? 51  ILE   B CG2 1 
ATOM   379  C  CD1 . ILE   A 1 51  ? 10.587  16.011  -18.398 1.00 28.00 ? 51  ILE   B CD1 1 
ATOM   380  N  N   . LYS   A 1 52  ? 6.378   14.211  -22.124 1.00 24.65 ? 52  LYS   B N   1 
ATOM   381  C  CA  . LYS   A 1 52  ? 5.026   13.706  -22.082 1.00 26.40 ? 52  LYS   B CA  1 
ATOM   382  C  C   . LYS   A 1 52  ? 5.098   12.231  -21.708 1.00 25.97 ? 52  LYS   B C   1 
ATOM   383  O  O   . LYS   A 1 52  ? 5.667   11.446  -22.472 1.00 22.20 ? 52  LYS   B O   1 
ATOM   384  C  CB  . LYS   A 1 52  ? 4.356   13.872  -23.448 1.00 32.37 ? 52  LYS   B CB  1 
ATOM   385  C  CG  . LYS   A 1 52  ? 2.981   13.222  -23.550 1.00 36.68 ? 52  LYS   B CG  1 
ATOM   386  C  CD  . LYS   A 1 52  ? 2.555   12.939  -24.980 1.00 38.56 ? 52  LYS   B CD  1 
ATOM   387  C  CE  . LYS   A 1 52  ? 1.115   12.475  -25.073 1.00 38.61 ? 52  LYS   B CE  1 
ATOM   388  N  NZ  . LYS   A 1 52  ? 0.970   11.062  -24.653 1.00 34.28 ? 52  LYS   B NZ  1 
ATOM   389  N  N   . TYR   A 1 53  ? 4.560   11.897  -20.521 1.00 23.73 ? 53  TYR   B N   1 
ATOM   390  C  CA  . TYR   A 1 53  ? 4.584   10.544  -19.984 1.00 23.07 ? 53  TYR   B CA  1 
ATOM   391  C  C   . TYR   A 1 53  ? 3.149   10.092  -19.728 1.00 25.32 ? 53  TYR   B C   1 
ATOM   392  O  O   . TYR   A 1 53  ? 2.524   10.572  -18.792 1.00 27.06 ? 53  TYR   B O   1 
ATOM   393  C  CB  . TYR   A 1 53  ? 5.370   10.470  -18.665 1.00 23.71 ? 53  TYR   B CB  1 
ATOM   394  C  CG  . TYR   A 1 53  ? 6.862   10.701  -18.727 1.00 21.39 ? 53  TYR   B CG  1 
ATOM   395  C  CD1 . TYR   A 1 53  ? 7.597   10.368  -19.859 1.00 21.24 ? 53  TYR   B CD1 1 
ATOM   396  C  CD2 . TYR   A 1 53  ? 7.561   11.165  -17.614 1.00 20.36 ? 53  TYR   B CD2 1 
ATOM   397  C  CE1 . TYR   A 1 53  ? 8.975   10.546  -19.910 1.00 19.88 ? 53  TYR   B CE1 1 
ATOM   398  C  CE2 . TYR   A 1 53  ? 8.938   11.331  -17.649 1.00 20.19 ? 53  TYR   B CE2 1 
ATOM   399  C  CZ  . TYR   A 1 53  ? 9.647   11.036  -18.806 1.00 18.75 ? 53  TYR   B CZ  1 
ATOM   400  O  OH  . TYR   A 1 53  ? 10.996  11.203  -18.873 1.00 19.42 ? 53  TYR   B OH  1 
ATOM   401  N  N   . ASP   A 1 54  ? 2.651   9.177   -20.573 1.00 23.23 ? 54  ASP   B N   1 
ATOM   402  C  CA  . ASP   A 1 54  ? 1.303   8.629   -20.471 1.00 23.88 ? 54  ASP   B CA  1 
ATOM   403  C  C   . ASP   A 1 54  ? 1.250   7.659   -19.293 1.00 23.31 ? 54  ASP   B C   1 
ATOM   404  O  O   . ASP   A 1 54  ? 2.020   6.699   -19.264 1.00 21.56 ? 54  ASP   B O   1 
ATOM   405  C  CB  . ASP   A 1 54  ? 0.950   7.869   -21.760 1.00 25.57 ? 54  ASP   B CB  1 
ATOM   406  C  CG  . ASP   A 1 54  ? -0.524  7.506   -21.919 1.00 30.64 ? 54  ASP   B CG  1 
ATOM   407  O  OD1 . ASP   A 1 54  ? -1.117  6.904   -20.974 1.00 28.06 ? 54  ASP   B OD1 1 
ATOM   408  O  OD2 . ASP   A 1 54  ? -1.082  7.850   -22.990 1.00 35.70 ? 54  ASP   B OD2 1 
ATOM   409  N  N   . PRO   A 1 55  ? 0.325   7.823   -18.316 1.00 23.51 ? 55  PRO   B N   1 
ATOM   410  C  CA  . PRO   A 1 55  ? 0.239   6.891   -17.187 1.00 23.11 ? 55  PRO   B CA  1 
ATOM   411  C  C   . PRO   A 1 55  ? -0.146  5.475   -17.636 1.00 23.20 ? 55  PRO   B C   1 
ATOM   412  O  O   . PRO   A 1 55  ? 0.168   4.525   -16.923 1.00 24.49 ? 55  PRO   B O   1 
ATOM   413  C  CB  . PRO   A 1 55  ? -0.843  7.444   -16.247 1.00 25.68 ? 55  PRO   B CB  1 
ATOM   414  C  CG  . PRO   A 1 55  ? -1.233  8.797   -16.821 1.00 27.25 ? 55  PRO   B CG  1 
ATOM   415  C  CD  . PRO   A 1 55  ? -0.670  8.911   -18.229 1.00 27.25 ? 55  PRO   B CD  1 
ATOM   416  N  N   . SER   A 1 56  ? -0.763  5.327   -18.821 1.00 25.18 ? 56  SER   B N   1 
ATOM   417  C  CA  . SER   A 1 56  ? -1.051  3.990   -19.347 1.00 28.00 ? 56  SER   B CA  1 
ATOM   418  C  C   . SER   A 1 56  ? 0.168   3.284   -19.943 1.00 25.17 ? 56  SER   B C   1 
ATOM   419  O  O   . SER   A 1 56  ? 0.072   2.124   -20.340 1.00 27.13 ? 56  SER   B O   1 
ATOM   420  C  CB  . SER   A 1 56  ? -2.232  3.952   -20.291 1.00 31.72 ? 56  SER   B CB  1 
ATOM   421  O  OG  . SER   A 1 56  ? -1.970  4.698   -21.467 1.00 37.48 ? 56  SER   B OG  1 
ATOM   422  N  N   . SER   A 1 57  ? 1.331   3.944   -19.976 1.00 21.91 ? 57  SER   B N   1 
ATOM   423  C  CA  . SER   A 1 57  ? 2.495   3.312   -20.582 1.00 20.98 ? 57  SER   B CA  1 
ATOM   424  C  C   . SER   A 1 57  ? 3.118   2.222   -19.702 1.00 21.37 ? 57  SER   B C   1 
ATOM   425  O  O   . SER   A 1 57  ? 3.649   1.239   -20.237 1.00 22.42 ? 57  SER   B O   1 
ATOM   426  C  CB  . SER   A 1 57  ? 3.538   4.344   -20.956 1.00 21.74 ? 57  SER   B CB  1 
ATOM   427  O  OG  . SER   A 1 57  ? 3.110   5.079   -22.103 1.00 20.67 ? 57  SER   B OG  1 
ATOM   428  N  N   . ALA   A 1 58  ? 3.115   2.420   -18.375 1.00 17.51 ? 58  ALA   B N   1 
ATOM   429  C  CA  . ALA   A 1 58  ? 3.763   1.483   -17.454 1.00 19.11 ? 58  ALA   B CA  1 
ATOM   430  C  C   . ALA   A 1 58  ? 3.026   0.149   -17.503 1.00 17.40 ? 58  ALA   B C   1 
ATOM   431  O  O   . ALA   A 1 58  ? 1.800   0.149   -17.541 1.00 18.05 ? 58  ALA   B O   1 
ATOM   432  C  CB  . ALA   A 1 58  ? 3.716   2.019   -16.046 1.00 18.89 ? 58  ALA   B CB  1 
ATOM   433  N  N   . LYS   A 1 59  ? 3.761   -0.973  -17.472 1.00 17.66 ? 59  LYS   B N   1 
ATOM   434  C  CA  . LYS   A 1 59  ? 3.086   -2.266  -17.528 1.00 17.96 ? 59  LYS   B CA  1 
ATOM   435  C  C   . LYS   A 1 59  ? 3.423   -3.209  -16.369 1.00 19.05 ? 59  LYS   B C   1 
ATOM   436  O  O   . LYS   A 1 59  ? 2.523   -3.923  -15.883 1.00 19.29 ? 59  LYS   B O   1 
ATOM   437  C  CB  . LYS   A 1 59  ? 3.393   -2.963  -18.848 1.00 17.80 ? 59  LYS   B CB  1 
ATOM   438  C  CG  . LYS   A 1 59  ? 2.888   -2.195  -20.066 1.00 18.29 ? 59  LYS   B CG  1 
ATOM   439  C  CD  . LYS   A 1 59  ? 1.384   -1.996  -20.162 1.00 20.38 ? 59  LYS   B CD  1 
ATOM   440  C  CE  . LYS   A 1 59  ? 1.071   -1.268  -21.450 1.00 21.98 ? 59  LYS   B CE  1 
ATOM   441  N  NZ  . LYS   A 1 59  ? 0.023   -0.247  -21.294 1.00 27.64 ? 59  LYS   B NZ  1 
ATOM   442  N  N   . ILE   A 1 60  ? 4.708   -3.249  -15.990 1.00 17.66 ? 60  ILE   B N   1 
ATOM   443  C  CA  . ILE   A 1 60  ? 5.286   -4.293  -15.158 1.00 20.19 ? 60  ILE   B CA  1 
ATOM   444  C  C   . ILE   A 1 60  ? 6.302   -3.651  -14.210 1.00 18.75 ? 60  ILE   B C   1 
ATOM   445  O  O   . ILE   A 1 60  ? 7.025   -2.738  -14.611 1.00 20.82 ? 60  ILE   B O   1 
ATOM   446  C  CB  . ILE   A 1 60  ? 5.901   -5.400  -16.062 1.00 23.77 ? 60  ILE   B CB  1 
ATOM   447  C  CG1 . ILE   A 1 60  ? 4.810   -6.274  -16.701 1.00 30.68 ? 60  ILE   B CG1 1 
ATOM   448  C  CG2 . ILE   A 1 60  ? 6.880   -6.272  -15.311 1.00 26.71 ? 60  ILE   B CG2 1 
ATOM   449  C  CD1 . ILE   A 1 60  ? 5.165   -6.841  -18.073 1.00 29.51 ? 60  ILE   B CD1 1 
ATOM   450  N  N   . ILE   A 1 61  ? 6.319   -4.095  -12.947 1.00 16.97 ? 61  ILE   B N   1 
ATOM   451  C  CA  . ILE   A 1 61  ? 7.444   -3.810  -12.063 1.00 17.05 ? 61  ILE   B CA  1 
ATOM   452  C  C   . ILE   A 1 61  ? 8.132   -5.128  -11.730 1.00 18.31 ? 61  ILE   B C   1 
ATOM   453  O  O   . ILE   A 1 61  ? 7.445   -6.137  -11.482 1.00 18.39 ? 61  ILE   B O   1 
ATOM   454  C  CB  . ILE   A 1 61  ? 7.037   -2.984  -10.828 1.00 17.64 ? 61  ILE   B CB  1 
ATOM   455  C  CG1 . ILE   A 1 61  ? 8.236   -2.315  -10.147 1.00 20.04 ? 61  ILE   B CG1 1 
ATOM   456  C  CG2 . ILE   A 1 61  ? 6.172   -3.755  -9.818  1.00 18.16 ? 61  ILE   B CG2 1 
ATOM   457  C  CD1 . ILE   A 1 61  ? 7.817   -1.233  -9.157  1.00 20.12 ? 61  ILE   B CD1 1 
ATOM   458  N  N   . SER   A 1 62  ? 9.464   -5.103  -11.738 1.00 18.81 ? 62  SER   B N   1 
ATOM   459  C  CA  . SER   A 1 62  ? 10.230  -6.319  -11.485 1.00 20.80 ? 62  SER   B CA  1 
ATOM   460  C  C   . SER   A 1 62  ? 11.469  -6.043  -10.651 1.00 20.14 ? 62  SER   B C   1 
ATOM   461  O  O   . SER   A 1 62  ? 11.926  -4.915  -10.545 1.00 17.36 ? 62  SER   B O   1 
ATOM   462  C  CB  . SER   A 1 62  ? 10.578  -7.071  -12.746 1.00 24.66 ? 62  SER   B CB  1 
ATOM   463  O  OG  . SER   A 1 62  ? 11.280  -6.249  -13.647 1.00 30.24 ? 62  SER   B OG  1 
ATOM   464  N  N   . ASN   A 1 63  ? 11.967  -7.106  -10.020 1.00 19.23 ? 63  ASN   B N   1 
ATOM   465  C  CA  . ASN   A 1 63  ? 13.268  -7.080  -9.367  1.00 21.85 ? 63  ASN   B CA  1 
ATOM   466  C  C   . ASN   A 1 63  ? 14.277  -7.693  -10.338 1.00 21.60 ? 63  ASN   B C   1 
ATOM   467  O  O   . ASN   A 1 63  ? 14.222  -8.907  -10.575 1.00 21.60 ? 63  ASN   B O   1 
ATOM   468  C  CB  . ASN   A 1 63  ? 13.197  -7.828  -8.020  1.00 20.35 ? 63  ASN   B CB  1 
ATOM   469  C  CG  . ASN   A 1 63  ? 14.482  -7.813  -7.222  1.00 20.48 ? 63  ASN   B CG  1 
ATOM   470  O  OD1 . ASN   A 1 63  ? 15.499  -7.319  -7.702  1.00 23.42 ? 63  ASN   B OD1 1 
ATOM   471  N  ND2 . ASN   A 1 63  ? 14.449  -8.361  -6.004  1.00 23.86 ? 63  ASN   B ND2 1 
ATOM   472  N  N   . SER   A 1 64  ? 15.199  -6.862  -10.854 1.00 21.11 ? 64  SER   B N   1 
ATOM   473  C  CA  . SER   A 1 64  ? 16.269  -7.331  -11.728 1.00 22.65 ? 64  SER   B CA  1 
ATOM   474  C  C   . SER   A 1 64  ? 17.392  -8.002  -10.939 1.00 23.15 ? 64  SER   B C   1 
ATOM   475  O  O   . SER   A 1 64  ? 18.294  -8.570  -11.552 1.00 27.41 ? 64  SER   B O   1 
ATOM   476  C  CB  . SER   A 1 64  ? 16.867  -6.179  -12.518 1.00 23.41 ? 64  SER   B CB  1 
ATOM   477  O  OG  . SER   A 1 64  ? 17.625  -5.371  -11.633 1.00 21.28 ? 64  SER   B OG  1 
ATOM   478  N  N   . GLY   A 1 65  ? 17.397  -7.851  -9.609  1.00 21.98 ? 65  GLY   B N   1 
ATOM   479  C  CA  . GLY   A 1 65  ? 18.539  -8.254  -8.805  1.00 22.00 ? 65  GLY   B CA  1 
ATOM   480  C  C   . GLY   A 1 65  ? 19.498  -7.099  -8.544  1.00 23.13 ? 65  GLY   B C   1 
ATOM   481  O  O   . GLY   A 1 65  ? 20.359  -7.229  -7.676  1.00 23.01 ? 65  GLY   B O   1 
ATOM   482  N  N   . HIS   A 1 66  ? 19.325  -5.992  -9.298  1.00 22.38 ? 66  HIS   B N   1 
ATOM   483  C  CA  . HIS   A 1 66  ? 20.162  -4.796  -9.230  1.00 20.53 ? 66  HIS   B CA  1 
ATOM   484  C  C   . HIS   A 1 66  ? 19.368  -3.524  -8.862  1.00 20.28 ? 66  HIS   B C   1 
ATOM   485  O  O   . HIS   A 1 66  ? 19.970  -2.534  -8.453  1.00 20.10 ? 66  HIS   B O   1 
ATOM   486  C  CB  . HIS   A 1 66  ? 20.863  -4.556  -10.561 1.00 23.73 ? 66  HIS   B CB  1 
ATOM   487  C  CG  . HIS   A 1 66  ? 21.476  -5.777  -11.146 1.00 25.47 ? 66  HIS   B CG  1 
ATOM   488  N  ND1 . HIS   A 1 66  ? 22.559  -6.398  -10.563 1.00 27.99 ? 66  HIS   B ND1 1 
ATOM   489  C  CD2 . HIS   A 1 66  ? 21.181  -6.479  -12.261 1.00 27.65 ? 66  HIS   B CD2 1 
ATOM   490  C  CE1 . HIS   A 1 66  ? 22.904  -7.458  -11.287 1.00 27.02 ? 66  HIS   B CE1 1 
ATOM   491  N  NE2 . HIS   A 1 66  ? 22.081  -7.527  -12.338 1.00 27.79 ? 66  HIS   B NE2 1 
ATOM   492  N  N   . SER   A 1 67  ? 18.039  -3.549  -9.010  1.00 17.33 ? 67  SER   B N   1 
ATOM   493  C  CA  . SER   A 1 67  ? 17.139  -2.477  -8.604  1.00 17.69 ? 67  SER   B CA  1 
ATOM   494  C  C   . SER   A 1 67  ? 15.738  -3.015  -8.810  1.00 19.85 ? 67  SER   B C   1 
ATOM   495  O  O   . SER   A 1 67  ? 15.612  -4.179  -9.167  1.00 20.74 ? 67  SER   B O   1 
ATOM   496  C  CB  . SER   A 1 67  ? 17.382  -1.193  -9.396  1.00 16.30 ? 67  SER   B CB  1 
ATOM   497  O  OG  . SER   A 1 67  ? 16.660  -0.112  -8.789  1.00 17.60 ? 67  SER   B OG  1 
ATOM   498  N  N   . PHE   A 1 68  ? 14.694  -2.236  -8.510  1.00 19.87 ? 68  PHE   B N   1 
ATOM   499  C  CA  . PHE   A 1 68  ? 13.445  -2.523  -9.181  1.00 21.75 ? 68  PHE   B CA  1 
ATOM   500  C  C   . PHE   A 1 68  ? 13.528  -1.886  -10.571 1.00 22.98 ? 68  PHE   B C   1 
ATOM   501  O  O   . PHE   A 1 68  ? 14.260  -0.927  -10.773 1.00 21.40 ? 68  PHE   B O   1 
ATOM   502  C  CB  . PHE   A 1 68  ? 12.247  -2.003  -8.378  1.00 22.70 ? 68  PHE   B CB  1 
ATOM   503  C  CG  . PHE   A 1 68  ? 12.126  -0.498  -8.397  1.00 24.92 ? 68  PHE   B CG  1 
ATOM   504  C  CD1 . PHE   A 1 68  ? 11.476  0.152   -9.446  1.00 26.76 ? 68  PHE   B CD1 1 
ATOM   505  C  CD2 . PHE   A 1 68  ? 12.674  0.270   -7.376  1.00 27.50 ? 68  PHE   B CD2 1 
ATOM   506  C  CE1 . PHE   A 1 68  ? 11.390  1.543   -9.469  1.00 27.88 ? 68  PHE   B CE1 1 
ATOM   507  C  CE2 . PHE   A 1 68  ? 12.576  1.659   -7.396  1.00 25.08 ? 68  PHE   B CE2 1 
ATOM   508  C  CZ  . PHE   A 1 68  ? 11.949  2.286   -8.446  1.00 24.15 ? 68  PHE   B CZ  1 
ATOM   509  N  N   . ASN   A 1 69  ? 12.693  -2.364  -11.490 1.00 21.41 ? 69  ASN   B N   1 
ATOM   510  C  CA  . ASN   A 1 69  ? 12.599  -1.880  -12.864 1.00 23.84 ? 69  ASN   B CA  1 
ATOM   511  C  C   . ASN   A 1 69  ? 11.124  -1.738  -13.225 1.00 23.19 ? 69  ASN   B C   1 
ATOM   512  O  O   . ASN   A 1 69  ? 10.379  -2.724  -13.193 1.00 23.47 ? 69  ASN   B O   1 
ATOM   513  C  CB  . ASN   A 1 69  ? 13.170  -2.909  -13.840 1.00 34.12 ? 69  ASN   B CB  1 
ATOM   514  C  CG  . ASN   A 1 69  ? 14.593  -2.601  -14.240 1.00 43.49 ? 69  ASN   B CG  1 
ATOM   515  O  OD1 . ASN   A 1 69  ? 15.331  -1.950  -13.496 1.00 47.12 ? 69  ASN   B OD1 1 
ATOM   516  N  ND2 . ASN   A 1 69  ? 14.982  -3.055  -15.421 1.00 50.57 ? 69  ASN   B ND2 1 
ATOM   517  N  N   . VAL   A 1 70  ? 10.670  -0.506  -13.476 1.00 19.04 ? 70  VAL   B N   1 
ATOM   518  C  CA  . VAL   A 1 70  ? 9.335   -0.353  -14.047 1.00 18.09 ? 70  VAL   B CA  1 
ATOM   519  C  C   . VAL   A 1 70  ? 9.506   -0.358  -15.570 1.00 19.08 ? 70  VAL   B C   1 
ATOM   520  O  O   . VAL   A 1 70  ? 10.288  0.433   -16.110 1.00 15.77 ? 70  VAL   B O   1 
ATOM   521  C  CB  . VAL   A 1 70  ? 8.644   0.945   -13.558 1.00 18.31 ? 70  VAL   B CB  1 
ATOM   522  C  CG1 . VAL   A 1 70  ? 7.289   1.187   -14.237 1.00 17.84 ? 70  VAL   B CG1 1 
ATOM   523  C  CG2 . VAL   A 1 70  ? 8.499   0.937   -12.040 1.00 19.26 ? 70  VAL   B CG2 1 
ATOM   524  N  N   . ASP   A 1 71  ? 8.807   -1.287  -16.251 1.00 20.34 ? 71  ASP   B N   1 
ATOM   525  C  CA  . ASP   A 1 71  ? 8.904   -1.438  -17.699 1.00 23.40 ? 71  ASP   B CA  1 
ATOM   526  C  C   . ASP   A 1 71  ? 7.687   -0.778  -18.356 1.00 22.81 ? 71  ASP   B C   1 
ATOM   527  O  O   . ASP   A 1 71  ? 6.565   -0.900  -17.860 1.00 23.36 ? 71  ASP   B O   1 
ATOM   528  C  CB  . ASP   A 1 71  ? 9.071   -2.907  -18.119 1.00 28.95 ? 71  ASP   B CB  1 
ATOM   529  C  CG  . ASP   A 1 71  ? 10.464  -3.513  -17.902 1.00 37.31 ? 71  ASP   B CG  1 
ATOM   530  O  OD1 . ASP   A 1 71  ? 11.441  -2.749  -17.654 1.00 40.93 ? 71  ASP   B OD1 1 
ATOM   531  O  OD2 . ASP   A 1 71  ? 10.580  -4.761  -17.986 1.00 43.96 ? 71  ASP   B OD2 1 
ATOM   532  N  N   . PHE   A 1 72  ? 7.942   -0.042  -19.450 1.00 22.04 ? 72  PHE   B N   1 
ATOM   533  C  CA  . PHE   A 1 72  ? 6.940   0.714   -20.184 1.00 24.06 ? 72  PHE   B CA  1 
ATOM   534  C  C   . PHE   A 1 72  ? 6.824   0.152   -21.606 1.00 24.21 ? 72  PHE   B C   1 
ATOM   535  O  O   . PHE   A 1 72  ? 7.817   -0.244  -22.215 1.00 23.50 ? 72  PHE   B O   1 
ATOM   536  C  CB  . PHE   A 1 72  ? 7.335   2.198   -20.267 1.00 21.28 ? 72  PHE   B CB  1 
ATOM   537  C  CG  . PHE   A 1 72  ? 7.421   2.871   -18.912 1.00 22.37 ? 72  PHE   B CG  1 
ATOM   538  C  CD1 . PHE   A 1 72  ? 8.563   2.736   -18.117 1.00 20.37 ? 72  PHE   B CD1 1 
ATOM   539  C  CD2 . PHE   A 1 72  ? 6.350   3.615   -18.420 1.00 20.39 ? 72  PHE   B CD2 1 
ATOM   540  C  CE1 . PHE   A 1 72  ? 8.624   3.356   -16.876 1.00 20.71 ? 72  PHE   B CE1 1 
ATOM   541  C  CE2 . PHE   A 1 72  ? 6.421   4.239   -17.179 1.00 21.71 ? 72  PHE   B CE2 1 
ATOM   542  C  CZ  . PHE   A 1 72  ? 7.553   4.094   -16.403 1.00 20.11 ? 72  PHE   B CZ  1 
ATOM   543  N  N   . ASP   A 1 73  ? 5.602   0.165   -22.142 1.00 23.57 ? 73  ASP   B N   1 
ATOM   544  C  CA  . ASP   A 1 73  ? 5.346   -0.240  -23.519 1.00 22.72 ? 73  ASP   B CA  1 
ATOM   545  C  C   . ASP   A 1 73  ? 5.973   0.801   -24.447 1.00 22.63 ? 73  ASP   B C   1 
ATOM   546  O  O   . ASP   A 1 73  ? 5.494   1.940   -24.495 1.00 23.96 ? 73  ASP   B O   1 
ATOM   547  C  CB  . ASP   A 1 73  ? 3.835   -0.377  -23.744 1.00 23.41 ? 73  ASP   B CB  1 
ATOM   548  C  CG  . ASP   A 1 73  ? 3.457   -0.739  -25.180 1.00 26.23 ? 73  ASP   B CG  1 
ATOM   549  O  OD1 . ASP   A 1 73  ? 4.353   -0.977  -25.960 1.00 26.86 ? 73  ASP   B OD1 1 
ATOM   550  O  OD2 . ASP   A 1 73  ? 2.260   -0.792  -25.486 1.00 26.76 ? 73  ASP   B OD2 1 
ATOM   551  N  N   . ASP   A 1 74  ? 7.077   0.433   -25.110 1.00 21.69 ? 74  ASP   B N   1 
ATOM   552  C  CA  . ASP   A 1 74  ? 7.766   1.318   -26.053 1.00 22.40 ? 74  ASP   B CA  1 
ATOM   553  C  C   . ASP   A 1 74  ? 7.513   0.869   -27.498 1.00 21.70 ? 74  ASP   B C   1 
ATOM   554  O  O   . ASP   A 1 74  ? 8.363   1.082   -28.356 1.00 21.93 ? 74  ASP   B O   1 
ATOM   555  C  CB  . ASP   A 1 74  ? 9.263   1.454   -25.746 1.00 21.45 ? 74  ASP   B CB  1 
ATOM   556  C  CG  . ASP   A 1 74  ? 10.018  0.139   -25.960 1.00 28.39 ? 74  ASP   B CG  1 
ATOM   557  O  OD1 . ASP   A 1 74  ? 9.346   -0.919  -26.073 1.00 24.72 ? 74  ASP   B OD1 1 
ATOM   558  O  OD2 . ASP   A 1 74  ? 11.262  0.170   -26.021 1.00 26.63 ? 74  ASP   B OD2 1 
ATOM   559  N  N   . THR   A 1 75  ? 6.327   0.297   -27.762 1.00 23.12 ? 75  THR   B N   1 
ATOM   560  C  CA  . THR   A 1 75  ? 5.808   0.018   -29.101 1.00 28.97 ? 75  THR   B CA  1 
ATOM   561  C  C   . THR   A 1 75  ? 5.653   1.298   -29.920 1.00 32.24 ? 75  THR   B C   1 
ATOM   562  O  O   . THR   A 1 75  ? 6.032   1.321   -31.092 1.00 31.96 ? 75  THR   B O   1 
ATOM   563  C  CB  . THR   A 1 75  ? 4.366   -0.518  -29.064 1.00 34.10 ? 75  THR   B CB  1 
ATOM   564  O  OG1 . THR   A 1 75  ? 4.332   -1.705  -28.273 1.00 29.63 ? 75  THR   B OG1 1 
ATOM   565  C  CG2 . THR   A 1 75  ? 3.808   -0.841  -30.439 1.00 35.67 ? 75  THR   B CG2 1 
ATOM   566  N  N   . GLU   A 1 76  ? 5.057   2.343   -29.324 1.00 34.06 ? 76  GLU   B N   1 
ATOM   567  C  CA  . GLU   A 1 76  ? 4.945   3.608   -30.046 1.00 36.40 ? 76  GLU   B CA  1 
ATOM   568  C  C   . GLU   A 1 76  ? 5.321   4.776   -29.135 1.00 31.64 ? 76  GLU   B C   1 
ATOM   569  O  O   . GLU   A 1 76  ? 5.986   4.572   -28.123 1.00 31.60 ? 76  GLU   B O   1 
ATOM   570  C  CB  . GLU   A 1 76  ? 3.634   3.726   -30.850 1.00 42.33 ? 76  GLU   B CB  1 
ATOM   571  C  CG  . GLU   A 1 76  ? 2.381   3.999   -30.025 1.00 43.98 ? 76  GLU   B CG  1 
ATOM   572  C  CD  . GLU   A 1 76  ? 1.052   3.691   -30.711 1.00 49.31 ? 76  GLU   B CD  1 
ATOM   573  O  OE1 . GLU   A 1 76  ? 1.058   3.375   -31.924 1.00 44.59 ? 76  GLU   B OE1 1 
ATOM   574  O  OE2 . GLU   A 1 76  ? 0.002   3.740   -30.022 1.00 47.24 ? 76  GLU   B OE2 1 
ATOM   575  N  N   . ASN   A 1 77  ? 4.955   5.992   -29.562 1.00 30.16 ? 77  ASN   B N   1 
ATOM   576  C  CA  . ASN   A 1 77  ? 5.424   7.251   -29.009 1.00 29.38 ? 77  ASN   B CA  1 
ATOM   577  C  C   . ASN   A 1 77  ? 4.418   7.929   -28.079 1.00 28.74 ? 77  ASN   B C   1 
ATOM   578  O  O   . ASN   A 1 77  ? 4.353   9.158   -28.041 1.00 27.92 ? 77  ASN   B O   1 
ATOM   579  C  CB  . ASN   A 1 77  ? 5.736   8.275   -30.099 1.00 29.70 ? 77  ASN   B CB  1 
ATOM   580  C  CG  . ASN   A 1 77  ? 7.199   8.304   -30.441 1.00 25.81 ? 77  ASN   B CG  1 
ATOM   581  O  OD1 . ASN   A 1 77  ? 7.999   7.537   -29.893 1.00 21.83 ? 77  ASN   B OD1 1 
ATOM   582  N  ND2 . ASN   A 1 77  ? 7.537   9.161   -31.370 1.00 26.13 ? 77  ASN   B ND2 1 
ATOM   583  N  N   . LYS   A 1 78  ? 3.726   7.158   -27.232 1.00 27.29 ? 78  LYS   B N   1 
ATOM   584  C  CA  . LYS   A 1 78  ? 2.850   7.762   -26.237 1.00 28.49 ? 78  LYS   B CA  1 
ATOM   585  C  C   . LYS   A 1 78  ? 3.661   8.483   -25.151 1.00 24.61 ? 78  LYS   B C   1 
ATOM   586  O  O   . LYS   A 1 78  ? 3.206   9.465   -24.556 1.00 23.67 ? 78  LYS   B O   1 
ATOM   587  C  CB  . LYS   A 1 78  ? 1.953   6.693   -25.599 1.00 34.16 ? 78  LYS   B CB  1 
ATOM   588  C  CG  . LYS   A 1 78  ? 0.825   6.166   -26.480 1.00 39.93 ? 78  LYS   B CG  1 
ATOM   589  C  CD  . LYS   A 1 78  ? 0.229   4.858   -25.982 1.00 42.70 ? 78  LYS   B CD  1 
ATOM   590  C  CE  . LYS   A 1 78  ? -0.647  4.177   -27.021 1.00 49.72 ? 78  LYS   B CE  1 
ATOM   591  N  NZ  . LYS   A 1 78  ? -0.588  2.696   -26.947 1.00 49.10 ? 78  LYS   B NZ  1 
ATOM   592  N  N   . SER   A 1 79  ? 4.849   7.962   -24.832 1.00 19.32 ? 79  SER   B N   1 
ATOM   593  C  CA  . SER   A 1 79  ? 5.647   8.536   -23.748 1.00 17.98 ? 79  SER   B CA  1 
ATOM   594  C  C   . SER   A 1 79  ? 7.057   8.894   -24.227 1.00 16.85 ? 79  SER   B C   1 
ATOM   595  O  O   . SER   A 1 79  ? 7.834   7.995   -24.579 1.00 13.89 ? 79  SER   B O   1 
ATOM   596  C  CB  . SER   A 1 79  ? 5.718   7.573   -22.577 1.00 18.79 ? 79  SER   B CB  1 
ATOM   597  O  OG  . SER   A 1 79  ? 4.456   7.426   -21.941 1.00 17.89 ? 79  SER   B OG  1 
ATOM   598  N  N   . VAL   A 1 80  ? 7.389   10.197  -24.216 1.00 17.30 ? 80  VAL   B N   1 
ATOM   599  C  CA  . VAL   A 1 80  ? 8.581   10.706  -24.898 1.00 18.34 ? 80  VAL   B CA  1 
ATOM   600  C  C   . VAL   A 1 80  ? 9.208   11.858  -24.108 1.00 17.67 ? 80  VAL   B C   1 
ATOM   601  O  O   . VAL   A 1 80  ? 8.534   12.578  -23.368 1.00 16.48 ? 80  VAL   B O   1 
ATOM   602  C  CB  . VAL   A 1 80  ? 8.341   11.170  -26.356 1.00 19.41 ? 80  VAL   B CB  1 
ATOM   603  C  CG1 . VAL   A 1 80  ? 7.790   10.086  -27.279 1.00 18.34 ? 80  VAL   B CG1 1 
ATOM   604  C  CG2 . VAL   A 1 80  ? 7.521   12.457  -26.460 1.00 21.04 ? 80  VAL   B CG2 1 
ATOM   605  N  N   . LEU   A 1 81  ? 10.513  12.005  -24.334 1.00 16.14 ? 81  LEU   B N   1 
ATOM   606  C  CA  . LEU   A 1 81  ? 11.307  13.160  -23.930 1.00 18.07 ? 81  LEU   B CA  1 
ATOM   607  C  C   . LEU   A 1 81  ? 11.852  13.845  -25.178 1.00 18.88 ? 81  LEU   B C   1 
ATOM   608  O  O   . LEU   A 1 81  ? 12.421  13.185  -26.053 1.00 19.85 ? 81  LEU   B O   1 
ATOM   609  C  CB  . LEU   A 1 81  ? 12.476  12.629  -23.075 1.00 18.75 ? 81  LEU   B CB  1 
ATOM   610  C  CG  . LEU   A 1 81  ? 13.514  13.657  -22.624 1.00 19.62 ? 81  LEU   B CG  1 
ATOM   611  C  CD1 . LEU   A 1 81  ? 12.874  14.646  -21.671 1.00 18.97 ? 81  LEU   B CD1 1 
ATOM   612  C  CD2 . LEU   A 1 81  ? 14.691  12.960  -21.956 1.00 22.06 ? 81  LEU   B CD2 1 
ATOM   613  N  N   . ARG   A 1 82  ? 11.719  15.183  -25.221 1.00 18.80 ? 82  ARG   B N   1 
ATOM   614  C  CA  . ARG   A 1 82  ? 12.128  16.010  -26.340 1.00 22.40 ? 82  ARG   B CA  1 
ATOM   615  C  C   . ARG   A 1 82  ? 12.852  17.205  -25.717 1.00 20.20 ? 82  ARG   B C   1 
ATOM   616  O  O   . ARG   A 1 82  ? 12.757  17.428  -24.524 1.00 18.71 ? 82  ARG   B O   1 
ATOM   617  C  CB  . ARG   A 1 82  ? 10.911  16.529  -27.144 1.00 25.27 ? 82  ARG   B CB  1 
ATOM   618  C  CG  . ARG   A 1 82  ? 9.736   15.559  -27.245 1.00 32.84 ? 82  ARG   B CG  1 
ATOM   619  C  CD  . ARG   A 1 82  ? 8.331   16.062  -27.582 1.00 37.34 ? 82  ARG   B CD  1 
ATOM   620  N  NE  . ARG   A 1 82  ? 7.634   16.690  -26.458 1.00 38.95 ? 82  ARG   B NE  1 
ATOM   621  C  CZ  . ARG   A 1 82  ? 6.327   16.616  -26.199 1.00 37.68 ? 82  ARG   B CZ  1 
ATOM   622  N  NH1 . ARG   A 1 82  ? 5.522   15.889  -26.963 1.00 30.65 ? 82  ARG   B NH1 1 
ATOM   623  N  NH2 . ARG   A 1 82  ? 5.838   17.264  -25.151 1.00 34.37 ? 82  ARG   B NH2 1 
ATOM   624  N  N   . GLY   A 1 83  ? 13.615  17.945  -26.517 1.00 21.95 ? 83  GLY   B N   1 
ATOM   625  C  CA  . GLY   A 1 83  ? 14.200  19.172  -26.001 1.00 19.67 ? 83  GLY   B CA  1 
ATOM   626  C  C   . GLY   A 1 83  ? 15.499  18.897  -25.272 1.00 21.28 ? 83  GLY   B C   1 
ATOM   627  O  O   . GLY   A 1 83  ? 16.181  17.891  -25.526 1.00 22.48 ? 83  GLY   B O   1 
ATOM   628  N  N   . GLY   A 1 84  ? 15.792  19.758  -24.304 1.00 22.24 ? 84  GLY   B N   1 
ATOM   629  C  CA  . GLY   A 1 84  ? 17.064  19.656  -23.626 1.00 23.43 ? 84  GLY   B CA  1 
ATOM   630  C  C   . GLY   A 1 84  ? 18.198  19.694  -24.642 1.00 22.28 ? 84  GLY   B C   1 
ATOM   631  O  O   . GLY   A 1 84  ? 18.196  20.507  -25.570 1.00 24.69 ? 84  GLY   B O   1 
ATOM   632  N  N   . PRO   A 1 85  ? 19.222  18.829  -24.456 1.00 22.63 ? 85  PRO   B N   1 
ATOM   633  C  CA  . PRO   A 1 85  ? 20.350  18.737  -25.389 1.00 22.42 ? 85  PRO   B CA  1 
ATOM   634  C  C   . PRO   A 1 85  ? 20.102  17.822  -26.583 1.00 20.41 ? 85  PRO   B C   1 
ATOM   635  O  O   . PRO   A 1 85  ? 20.988  17.647  -27.408 1.00 25.44 ? 85  PRO   B O   1 
ATOM   636  C  CB  . PRO   A 1 85  ? 21.443  18.086  -24.502 1.00 20.11 ? 85  PRO   B CB  1 
ATOM   637  C  CG  . PRO   A 1 85  ? 20.672  17.211  -23.532 1.00 18.49 ? 85  PRO   B CG  1 
ATOM   638  C  CD  . PRO   A 1 85  ? 19.387  17.967  -23.265 1.00 20.06 ? 85  PRO   B CD  1 
ATOM   639  N  N   . LEU   A 1 86  ? 18.919  17.194  -26.626 1.00 20.46 ? 86  LEU   B N   1 
ATOM   640  C  CA  . LEU   A 1 86  ? 18.614  16.112  -27.548 1.00 19.78 ? 86  LEU   B CA  1 
ATOM   641  C  C   . LEU   A 1 86  ? 18.196  16.646  -28.932 1.00 21.27 ? 86  LEU   B C   1 
ATOM   642  O  O   . LEU   A 1 86  ? 17.503  17.658  -29.069 1.00 19.44 ? 86  LEU   B O   1 
ATOM   643  C  CB  . LEU   A 1 86  ? 17.512  15.249  -26.917 1.00 17.97 ? 86  LEU   B CB  1 
ATOM   644  C  CG  . LEU   A 1 86  ? 17.825  14.694  -25.515 1.00 17.68 ? 86  LEU   B CG  1 
ATOM   645  C  CD1 . LEU   A 1 86  ? 16.597  13.997  -24.917 1.00 19.56 ? 86  LEU   B CD1 1 
ATOM   646  C  CD2 . LEU   A 1 86  ? 18.974  13.689  -25.568 1.00 16.65 ? 86  LEU   B CD2 1 
ATOM   647  N  N   . THR   A 1 87  ? 18.605  15.928  -29.972 1.00 20.57 ? 87  THR   B N   1 
ATOM   648  C  CA  . THR   A 1 87  ? 17.989  16.103  -31.276 1.00 23.03 ? 87  THR   B CA  1 
ATOM   649  C  C   . THR   A 1 87  ? 16.896  15.044  -31.446 1.00 24.95 ? 87  THR   B C   1 
ATOM   650  O  O   . THR   A 1 87  ? 17.173  13.837  -31.369 1.00 24.22 ? 87  THR   B O   1 
ATOM   651  C  CB  . THR   A 1 87  ? 19.057  15.972  -32.368 1.00 26.66 ? 87  THR   B CB  1 
ATOM   652  O  OG1 . THR   A 1 87  ? 20.049  16.966  -32.084 1.00 27.47 ? 87  THR   B OG1 1 
ATOM   653  C  CG2 . THR   A 1 87  ? 18.491  16.160  -33.762 1.00 31.78 ? 87  THR   B CG2 1 
ATOM   654  N  N   . GLY   A 1 88  ? 15.668  15.486  -31.732 1.00 22.31 ? 88  GLY   B N   1 
ATOM   655  C  CA  . GLY   A 1 88  ? 14.581  14.552  -32.015 1.00 27.45 ? 88  GLY   B CA  1 
ATOM   656  C  C   . GLY   A 1 88  ? 13.918  13.978  -30.753 1.00 26.59 ? 88  GLY   B C   1 
ATOM   657  O  O   . GLY   A 1 88  ? 14.005  14.560  -29.671 1.00 25.58 ? 88  GLY   B O   1 
ATOM   658  N  N   . SER   A 1 89  ? 13.244  12.823  -30.890 1.00 23.16 ? 89  SER   B N   1 
ATOM   659  C  CA  . SER   A 1 89  ? 12.357  12.354  -29.836 1.00 21.42 ? 89  SER   B CA  1 
ATOM   660  C  C   . SER   A 1 89  ? 12.903  11.069  -29.215 1.00 19.33 ? 89  SER   B C   1 
ATOM   661  O  O   . SER   A 1 89  ? 13.289  10.165  -29.933 1.00 20.14 ? 89  SER   B O   1 
ATOM   662  C  CB  . SER   A 1 89  ? 10.965  12.144  -30.395 1.00 23.01 ? 89  SER   B CB  1 
ATOM   663  O  OG  . SER   A 1 89  ? 10.120  11.571  -29.421 1.00 25.19 ? 89  SER   B OG  1 
ATOM   664  N  N   . TYR   A 1 90  ? 12.954  10.997  -27.885 1.00 16.88 ? 90  TYR   B N   1 
ATOM   665  C  CA  . TYR   A 1 90  ? 13.449  9.797   -27.226 1.00 17.63 ? 90  TYR   B CA  1 
ATOM   666  C  C   . TYR   A 1 90  ? 12.302  9.132   -26.472 1.00 17.84 ? 90  TYR   B C   1 
ATOM   667  O  O   . TYR   A 1 90  ? 11.550  9.791   -25.760 1.00 18.90 ? 90  TYR   B O   1 
ATOM   668  C  CB  . TYR   A 1 90  ? 14.637  10.091  -26.305 1.00 17.56 ? 90  TYR   B CB  1 
ATOM   669  C  CG  . TYR   A 1 90  ? 15.966  10.392  -26.969 1.00 17.56 ? 90  TYR   B CG  1 
ATOM   670  C  CD1 . TYR   A 1 90  ? 16.124  11.471  -27.830 1.00 19.42 ? 90  TYR   B CD1 1 
ATOM   671  C  CD2 . TYR   A 1 90  ? 17.099  9.640   -26.672 1.00 17.54 ? 90  TYR   B CD2 1 
ATOM   672  C  CE1 . TYR   A 1 90  ? 17.349  11.763  -28.428 1.00 19.06 ? 90  TYR   B CE1 1 
ATOM   673  C  CE2 . TYR   A 1 90  ? 18.336  9.925   -27.249 1.00 18.62 ? 90  TYR   B CE2 1 
ATOM   674  C  CZ  . TYR   A 1 90  ? 18.463  10.990  -28.130 1.00 19.84 ? 90  TYR   B CZ  1 
ATOM   675  O  OH  . TYR   A 1 90  ? 19.658  11.301  -28.724 1.00 18.05 ? 90  TYR   B OH  1 
ATOM   676  N  N   . ARG   A 1 91  ? 12.154  7.826   -26.694 1.00 15.82 ? 91  ARG   B N   1 
ATOM   677  C  CA  . ARG   A 1 91  ? 10.990  7.096   -26.233 1.00 15.38 ? 91  ARG   B CA  1 
ATOM   678  C  C   . ARG   A 1 91  ? 11.321  6.453   -24.880 1.00 15.53 ? 91  ARG   B C   1 
ATOM   679  O  O   . ARG   A 1 91  ? 12.383  5.819   -24.731 1.00 14.51 ? 91  ARG   B O   1 
ATOM   680  C  CB  . ARG   A 1 91  ? 10.691  6.038   -27.301 1.00 15.50 ? 91  ARG   B CB  1 
ATOM   681  C  CG  . ARG   A 1 91  ? 9.440   5.223   -27.029 1.00 18.14 ? 91  ARG   B CG  1 
ATOM   682  C  CD  . ARG   A 1 91  ? 9.047   4.331   -28.207 1.00 17.78 ? 91  ARG   B CD  1 
ATOM   683  N  NE  . ARG   A 1 91  ? 8.916   5.027   -29.492 1.00 18.07 ? 91  ARG   B NE  1 
ATOM   684  C  CZ  . ARG   A 1 91  ? 8.859   4.391   -30.669 1.00 20.50 ? 91  ARG   B CZ  1 
ATOM   685  N  NH1 . ARG   A 1 91  ? 8.855   3.069   -30.691 1.00 18.29 ? 91  ARG   B NH1 1 
ATOM   686  N  NH2 . ARG   A 1 91  ? 8.759   5.059   -31.806 1.00 21.47 ? 91  ARG   B NH2 1 
ATOM   687  N  N   . LEU   A 1 92  ? 10.381  6.577   -23.932 1.00 17.06 ? 92  LEU   B N   1 
ATOM   688  C  CA  . LEU   A 1 92  ? 10.479  6.014   -22.580 1.00 17.04 ? 92  LEU   B CA  1 
ATOM   689  C  C   . LEU   A 1 92  ? 10.545  4.492   -22.612 1.00 19.30 ? 92  LEU   B C   1 
ATOM   690  O  O   . LEU   A 1 92  ? 9.665   3.835   -23.185 1.00 20.63 ? 92  LEU   B O   1 
ATOM   691  C  CB  . LEU   A 1 92  ? 9.245   6.461   -21.792 1.00 15.55 ? 92  LEU   B CB  1 
ATOM   692  C  CG  . LEU   A 1 92  ? 9.168   6.001   -20.336 1.00 17.01 ? 92  LEU   B CG  1 
ATOM   693  C  CD1 . LEU   A 1 92  ? 10.392  6.443   -19.523 1.00 16.11 ? 92  LEU   B CD1 1 
ATOM   694  C  CD2 . LEU   A 1 92  ? 7.863   6.463   -19.683 1.00 16.63 ? 92  LEU   B CD2 1 
ATOM   695  N  N   . ARG   A 1 93  ? 11.530  3.949   -21.887 1.00 17.80 ? 93  ARG   B N   1 
ATOM   696  C  CA  . ARG   A 1 93  ? 11.757  2.515   -21.843 1.00 19.87 ? 93  ARG   B CA  1 
ATOM   697  C  C   . ARG   A 1 93  ? 11.560  1.980   -20.415 1.00 17.62 ? 93  ARG   B C   1 
ATOM   698  O  O   . ARG   A 1 93  ? 10.815  1.015   -20.216 1.00 16.63 ? 93  ARG   B O   1 
ATOM   699  C  CB  . ARG   A 1 93  ? 13.146  2.210   -22.430 1.00 22.58 ? 93  ARG   B CB  1 
ATOM   700  C  CG  . ARG   A 1 93  ? 13.629  0.784   -22.202 1.00 26.32 ? 93  ARG   B CG  1 
ATOM   701  C  CD  . ARG   A 1 93  ? 12.956  -0.181  -23.148 1.00 29.51 ? 93  ARG   B CD  1 
ATOM   702  N  NE  . ARG   A 1 93  ? 13.562  -1.521  -23.160 1.00 30.42 ? 93  ARG   B NE  1 
ATOM   703  C  CZ  . ARG   A 1 93  ? 13.294  -2.450  -24.079 1.00 34.33 ? 93  ARG   B CZ  1 
ATOM   704  N  NH1 . ARG   A 1 93  ? 12.438  -2.193  -25.063 1.00 29.08 ? 93  ARG   B NH1 1 
ATOM   705  N  NH2 . ARG   A 1 93  ? 13.883  -3.635  -24.008 1.00 32.59 ? 93  ARG   B NH2 1 
ATOM   706  N  N   . GLN   A 1 94  ? 12.242  2.578   -19.433 1.00 15.65 ? 94  GLN   B N   1 
ATOM   707  C  CA  . GLN   A 1 94  ? 12.287  2.004   -18.090 1.00 16.81 ? 94  GLN   B CA  1 
ATOM   708  C  C   . GLN   A 1 94  ? 12.665  3.033   -17.019 1.00 16.17 ? 94  GLN   B C   1 
ATOM   709  O  O   . GLN   A 1 94  ? 13.260  4.073   -17.306 1.00 15.04 ? 94  GLN   B O   1 
ATOM   710  C  CB  . GLN   A 1 94  ? 13.173  0.733   -18.101 1.00 22.13 ? 94  GLN   B CB  1 
ATOM   711  C  CG  . GLN   A 1 94  ? 14.677  0.968   -18.138 1.00 27.76 ? 94  GLN   B CG  1 
ATOM   712  C  CD  . GLN   A 1 94  ? 15.284  0.935   -16.744 1.00 32.60 ? 94  GLN   B CD  1 
ATOM   713  O  OE1 . GLN   A 1 94  ? 15.121  1.862   -15.967 1.00 34.36 ? 94  GLN   B OE1 1 
ATOM   714  N  NE2 . GLN   A 1 94  ? 15.993  -0.130  -16.399 1.00 33.87 ? 94  GLN   B NE2 1 
ATOM   715  N  N   . VAL   A 1 95  ? 12.275  2.748   -15.770 1.00 14.76 ? 95  VAL   B N   1 
ATOM   716  C  CA  . VAL   A 1 95  ? 12.636  3.551   -14.605 1.00 14.63 ? 95  VAL   B CA  1 
ATOM   717  C  C   . VAL   A 1 95  ? 13.218  2.600   -13.566 1.00 15.41 ? 95  VAL   B C   1 
ATOM   718  O  O   . VAL   A 1 95  ? 12.682  1.501   -13.369 1.00 16.69 ? 95  VAL   B O   1 
ATOM   719  C  CB  . VAL   A 1 95  ? 11.396  4.283   -14.045 1.00 15.83 ? 95  VAL   B CB  1 
ATOM   720  C  CG1 . VAL   A 1 95  ? 11.637  4.907   -12.675 1.00 17.67 ? 95  VAL   B CG1 1 
ATOM   721  C  CG2 . VAL   A 1 95  ? 10.921  5.361   -15.033 1.00 16.01 ? 95  VAL   B CG2 1 
ATOM   722  N  N   . HIS   A 1 96  ? 14.306  3.030   -12.911 1.00 14.79 ? 96  HIS   B N   1 
ATOM   723  C  CA  . HIS   A 1 96  ? 14.843  2.323   -11.760 1.00 14.39 ? 96  HIS   B CA  1 
ATOM   724  C  C   . HIS   A 1 96  ? 15.410  3.353   -10.782 1.00 15.77 ? 96  HIS   B C   1 
ATOM   725  O  O   . HIS   A 1 96  ? 15.353  4.545   -11.065 1.00 15.63 ? 96  HIS   B O   1 
ATOM   726  C  CB  . HIS   A 1 96  ? 15.885  1.296   -12.235 1.00 13.91 ? 96  HIS   B CB  1 
ATOM   727  C  CG  . HIS   A 1 96  ? 17.022  1.937   -12.937 1.00 14.36 ? 96  HIS   B CG  1 
ATOM   728  N  ND1 . HIS   A 1 96  ? 17.059  2.069   -14.300 1.00 15.83 ? 96  HIS   B ND1 1 
ATOM   729  C  CD2 . HIS   A 1 96  ? 18.168  2.484   -12.461 1.00 15.88 ? 96  HIS   B CD2 1 
ATOM   730  C  CE1 . HIS   A 1 96  ? 18.166  2.707   -14.657 1.00 15.89 ? 96  HIS   B CE1 1 
ATOM   731  N  NE2 . HIS   A 1 96  ? 18.889  2.931   -13.539 1.00 15.12 ? 96  HIS   B NE2 1 
ATOM   732  N  N   . LEU   A 1 97  ? 15.903  2.892   -9.622  1.00 15.39 ? 97  LEU   B N   1 
ATOM   733  C  CA  . LEU   A 1 97  ? 16.413  3.766   -8.567  1.00 16.71 ? 97  LEU   B CA  1 
ATOM   734  C  C   . LEU   A 1 97  ? 17.769  3.249   -8.077  1.00 17.28 ? 97  LEU   B C   1 
ATOM   735  O  O   . LEU   A 1 97  ? 18.018  2.040   -8.087  1.00 18.03 ? 97  LEU   B O   1 
ATOM   736  C  CB  . LEU   A 1 97  ? 15.389  3.700   -7.429  1.00 17.49 ? 97  LEU   B CB  1 
ATOM   737  C  CG  . LEU   A 1 97  ? 15.627  4.669   -6.270  1.00 18.56 ? 97  LEU   B CG  1 
ATOM   738  C  CD1 . LEU   A 1 97  ? 15.360  6.097   -6.722  1.00 18.49 ? 97  LEU   B CD1 1 
ATOM   739  C  CD2 . LEU   A 1 97  ? 14.698  4.305   -5.122  1.00 18.10 ? 97  LEU   B CD2 1 
ATOM   740  N  N   . HIS   A 1 98  ? 18.649  4.167   -7.666  1.00 16.18 ? 98  HIS   B N   1 
ATOM   741  C  CA  . HIS   A 1 98  ? 19.868  3.793   -6.973  1.00 16.31 ? 98  HIS   B CA  1 
ATOM   742  C  C   . HIS   A 1 98  ? 19.845  4.388   -5.562  1.00 16.13 ? 98  HIS   B C   1 
ATOM   743  O  O   . HIS   A 1 98  ? 19.312  5.479   -5.332  1.00 15.80 ? 98  HIS   B O   1 
ATOM   744  C  CB  . HIS   A 1 98  ? 21.088  4.372   -7.703  1.00 15.90 ? 98  HIS   B CB  1 
ATOM   745  C  CG  . HIS   A 1 98  ? 21.204  3.922   -9.111  1.00 18.05 ? 98  HIS   B CG  1 
ATOM   746  N  ND1 . HIS   A 1 98  ? 21.939  2.803   -9.484  1.00 17.06 ? 98  HIS   B ND1 1 
ATOM   747  C  CD2 . HIS   A 1 98  ? 20.661  4.442   -10.231 1.00 15.31 ? 98  HIS   B CD2 1 
ATOM   748  C  CE1 . HIS   A 1 98  ? 21.859  2.695   -10.803 1.00 18.73 ? 98  HIS   B CE1 1 
ATOM   749  N  NE2 . HIS   A 1 98  ? 21.110  3.716   -11.273 1.00 17.29 ? 98  HIS   B NE2 1 
ATOM   750  N  N   . TRP   A 1 99  ? 20.463  3.666   -4.627  1.00 15.23 ? 99  TRP   B N   1 
ATOM   751  C  CA  . TRP   A 1 99  ? 20.577  4.059   -3.234  1.00 15.16 ? 99  TRP   B CA  1 
ATOM   752  C  C   . TRP   A 1 99  ? 21.889  3.484   -2.692  1.00 16.43 ? 99  TRP   B C   1 
ATOM   753  O  O   . TRP   A 1 99  ? 22.623  2.760   -3.392  1.00 16.83 ? 99  TRP   B O   1 
ATOM   754  C  CB  . TRP   A 1 99  ? 19.332  3.577   -2.461  1.00 15.25 ? 99  TRP   B CB  1 
ATOM   755  C  CG  . TRP   A 1 99  ? 19.139  2.084   -2.514  1.00 14.65 ? 99  TRP   B CG  1 
ATOM   756  C  CD1 . TRP   A 1 99  ? 19.788  1.154   -1.746  1.00 16.77 ? 99  TRP   B CD1 1 
ATOM   757  C  CD2 . TRP   A 1 99  ? 18.270  1.338   -3.392  1.00 14.28 ? 99  TRP   B CD2 1 
ATOM   758  N  NE1 . TRP   A 1 99  ? 19.367  -0.116  -2.069  1.00 15.62 ? 99  TRP   B NE1 1 
ATOM   759  C  CE2 . TRP   A 1 99  ? 18.464  -0.030  -3.097  1.00 13.63 ? 99  TRP   B CE2 1 
ATOM   760  C  CE3 . TRP   A 1 99  ? 17.398  1.677   -4.450  1.00 13.18 ? 99  TRP   B CE3 1 
ATOM   761  C  CZ2 . TRP   A 1 99  ? 17.765  -1.035  -3.756  1.00 14.05 ? 99  TRP   B CZ2 1 
ATOM   762  C  CZ3 . TRP   A 1 99  ? 16.699  0.675   -5.094  1.00 13.56 ? 99  TRP   B CZ3 1 
ATOM   763  C  CH2 . TRP   A 1 99  ? 16.883  -0.667  -4.756  1.00 14.94 ? 99  TRP   B CH2 1 
ATOM   764  N  N   . GLY   A 1 100 ? 22.212  3.861   -1.453  1.00 16.79 ? 100 GLY   B N   1 
ATOM   765  C  CA  . GLY   A 1 100 ? 23.355  3.300   -0.760  1.00 15.64 ? 100 GLY   B CA  1 
ATOM   766  C  C   . GLY   A 1 100 ? 22.891  2.715   0.571   1.00 18.13 ? 100 GLY   B C   1 
ATOM   767  O  O   . GLY   A 1 100 ? 21.685  2.676   0.837   1.00 17.57 ? 100 GLY   B O   1 
ATOM   768  N  N   . SER   A 1 101 ? 23.845  2.245   1.390   1.00 17.99 ? 101 SER   B N   1 
ATOM   769  C  CA  . SER   A 1 101 ? 23.482  1.630   2.664   1.00 20.09 ? 101 SER   B CA  1 
ATOM   770  C  C   . SER   A 1 101 ? 23.153  2.718   3.692   1.00 20.02 ? 101 SER   B C   1 
ATOM   771  O  O   . SER   A 1 101 ? 22.474  2.435   4.663   1.00 20.33 ? 101 SER   B O   1 
ATOM   772  C  CB  . SER   A 1 101 ? 24.581  0.708   3.139   1.00 19.79 ? 101 SER   B CB  1 
ATOM   773  O  OG  . SER   A 1 101 ? 25.688  1.494   3.534   1.00 23.05 ? 101 SER   B OG  1 
ATOM   774  N  N   . ALA   A 1 102 ? 23.594  3.961   3.442   1.00 21.84 ? 102 ALA   B N   1 
ATOM   775  C  CA  . ALA   A 1 102 ? 23.330  5.087   4.330   1.00 22.03 ? 102 ALA   B CA  1 
ATOM   776  C  C   . ALA   A 1 102 ? 22.567  6.188   3.594   1.00 20.81 ? 102 ALA   B C   1 
ATOM   777  O  O   . ALA   A 1 102 ? 22.824  6.442   2.421   1.00 19.77 ? 102 ALA   B O   1 
ATOM   778  C  CB  . ALA   A 1 102 ? 24.642  5.628   4.870   1.00 21.05 ? 102 ALA   B CB  1 
ATOM   779  N  N   . ASP   A 1 103 ? 21.671  6.880   4.309   1.00 18.60 ? 103 ASP   B N   1 
ATOM   780  C  CA  . ASP   A 1 103 ? 20.863  7.955   3.734   1.00 22.48 ? 103 ASP   B CA  1 
ATOM   781  C  C   . ASP   A 1 103 ? 21.658  9.197   3.287   1.00 24.80 ? 103 ASP   B C   1 
ATOM   782  O  O   . ASP   A 1 103 ? 21.090  10.082  2.633   1.00 24.17 ? 103 ASP   B O   1 
ATOM   783  C  CB  . ASP   A 1 103 ? 19.718  8.334   4.687   1.00 25.27 ? 103 ASP   B CB  1 
ATOM   784  C  CG  . ASP   A 1 103 ? 18.667  7.228   4.797   1.00 27.04 ? 103 ASP   B CG  1 
ATOM   785  O  OD1 . ASP   A 1 103 ? 18.825  6.196   4.143   1.00 29.57 ? 103 ASP   B OD1 1 
ATOM   786  O  OD2 . ASP   A 1 103 ? 17.701  7.405   5.538   1.00 30.61 ? 103 ASP   B OD2 1 
ATOM   787  N  N   . ASP   A 1 104 ? 22.947  9.323   3.622   1.00 25.40 ? 104 ASP   B N   1 
ATOM   788  C  CA  . ASP   A 1 104 ? 23.655  10.535  3.208   1.00 31.61 ? 104 ASP   B CA  1 
ATOM   789  C  C   . ASP   A 1 104 ? 24.630  10.247  2.054   1.00 31.35 ? 104 ASP   B C   1 
ATOM   790  O  O   . ASP   A 1 104 ? 25.478  11.077  1.709   1.00 30.10 ? 104 ASP   B O   1 
ATOM   791  C  CB  . ASP   A 1 104 ? 24.317  11.238  4.407   1.00 34.00 ? 104 ASP   B CB  1 
ATOM   792  C  CG  . ASP   A 1 104 ? 25.352  10.343  5.069   1.00 38.80 ? 104 ASP   B CG  1 
ATOM   793  O  OD1 . ASP   A 1 104 ? 25.201  9.113   4.955   1.00 37.95 ? 104 ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   A 1 104 ? 26.308  10.868  5.675   1.00 44.03 ? 104 ASP   B OD2 1 
ATOM   795  N  N   . HIS   A 1 105 ? 24.535  9.039   1.484   1.00 28.48 ? 105 HIS   B N   1 
ATOM   796  C  CA  . HIS   A 1 105 ? 25.475  8.599   0.466   1.00 29.76 ? 105 HIS   B CA  1 
ATOM   797  C  C   . HIS   A 1 105 ? 24.835  7.571   -0.461  1.00 27.12 ? 105 HIS   B C   1 
ATOM   798  O  O   . HIS   A 1 105 ? 25.311  6.437   -0.533  1.00 28.24 ? 105 HIS   B O   1 
ATOM   799  C  CB  . HIS   A 1 105 ? 26.726  8.016   1.133   1.00 33.33 ? 105 HIS   B CB  1 
ATOM   800  C  CG  . HIS   A 1 105 ? 27.968  8.173   0.329   1.00 36.72 ? 105 HIS   B CG  1 
ATOM   801  N  ND1 . HIS   A 1 105 ? 28.598  7.103   -0.277  1.00 40.07 ? 105 HIS   B ND1 1 
ATOM   802  C  CD2 . HIS   A 1 105 ? 28.708  9.270   0.041   1.00 41.49 ? 105 HIS   B CD2 1 
ATOM   803  C  CE1 . HIS   A 1 105 ? 29.683  7.526   -0.904  1.00 41.32 ? 105 HIS   B CE1 1 
ATOM   804  N  NE2 . HIS   A 1 105 ? 29.772  8.860   -0.723  1.00 45.30 ? 105 HIS   B NE2 1 
ATOM   805  N  N   . GLY   A 1 106 ? 23.801  7.984   -1.208  1.00 23.95 ? 106 GLY   B N   1 
ATOM   806  C  CA  . GLY   A 1 106 ? 23.075  7.025   -2.019  1.00 24.13 ? 106 GLY   B CA  1 
ATOM   807  C  C   . GLY   A 1 106 ? 23.029  7.338   -3.509  1.00 23.57 ? 106 GLY   B C   1 
ATOM   808  O  O   . GLY   A 1 106 ? 22.748  6.442   -4.302  1.00 24.76 ? 106 GLY   B O   1 
ATOM   809  N  N   . SER   A 1 107 ? 23.272  8.597   -3.905  1.00 22.03 ? 107 SER   B N   1 
ATOM   810  C  CA  . SER   A 1 107 ? 23.087  8.970   -5.307  1.00 19.98 ? 107 SER   B CA  1 
ATOM   811  C  C   . SER   A 1 107 ? 24.302  8.561   -6.143  1.00 19.45 ? 107 SER   B C   1 
ATOM   812  O  O   . SER   A 1 107 ? 25.369  8.288   -5.602  1.00 20.32 ? 107 SER   B O   1 
ATOM   813  C  CB  . SER   A 1 107 ? 22.711  10.435  -5.477  1.00 19.11 ? 107 SER   B CB  1 
ATOM   814  O  OG  . SER   A 1 107 ? 23.712  11.292  -4.939  1.00 19.86 ? 107 SER   B OG  1 
ATOM   815  N  N   . GLU   A 1 108 ? 24.151  8.476   -7.475  1.00 17.93 ? 108 GLU   B N   1 
ATOM   816  C  CA  . GLU   A 1 108 ? 25.314  8.172   -8.295  1.00 16.82 ? 108 GLU   B CA  1 
ATOM   817  C  C   . GLU   A 1 108 ? 26.058  9.470   -8.618  1.00 17.23 ? 108 GLU   B C   1 
ATOM   818  O  O   . GLU   A 1 108 ? 27.258  9.577   -8.375  1.00 16.22 ? 108 GLU   B O   1 
ATOM   819  C  CB  . GLU   A 1 108 ? 24.858  7.420   -9.535  1.00 19.84 ? 108 GLU   B CB  1 
ATOM   820  C  CG  . GLU   A 1 108 ? 24.274  6.052   -9.185  1.00 20.60 ? 108 GLU   B CG  1 
ATOM   821  C  CD  . GLU   A 1 108 ? 24.405  5.014   -10.282 1.00 22.48 ? 108 GLU   B CD  1 
ATOM   822  O  OE1 . GLU   A 1 108 ? 23.940  5.311   -11.394 1.00 21.64 ? 108 GLU   B OE1 1 
ATOM   823  O  OE2 . GLU   A 1 108 ? 24.977  3.906   -10.019 1.00 20.55 ? 108 GLU   B OE2 1 
ATOM   824  N  N   . HIS   A 1 109 ? 25.335  10.457  -9.149  1.00 17.08 ? 109 HIS   B N   1 
ATOM   825  C  CA  . HIS   A 1 109 ? 25.869  11.801  -9.354  1.00 17.50 ? 109 HIS   B CA  1 
ATOM   826  C  C   . HIS   A 1 109 ? 26.010  12.496  -8.001  1.00 18.57 ? 109 HIS   B C   1 
ATOM   827  O  O   . HIS   A 1 109 ? 25.174  12.315  -7.124  1.00 18.24 ? 109 HIS   B O   1 
ATOM   828  C  CB  . HIS   A 1 109 ? 25.004  12.605  -10.365 1.00 15.90 ? 109 HIS   B CB  1 
ATOM   829  C  CG  . HIS   A 1 109 ? 25.093  12.024  -11.741 1.00 17.38 ? 109 HIS   B CG  1 
ATOM   830  N  ND1 . HIS   A 1 109 ? 24.251  10.984  -12.171 1.00 17.34 ? 109 HIS   B ND1 1 
ATOM   831  C  CD2 . HIS   A 1 109 ? 25.961  12.246  -12.756 1.00 16.11 ? 109 HIS   B CD2 1 
ATOM   832  C  CE1 . HIS   A 1 109 ? 24.606  10.603  -13.383 1.00 18.95 ? 109 HIS   B CE1 1 
ATOM   833  N  NE2 . HIS   A 1 109 ? 25.651  11.359  -13.770 1.00 18.67 ? 109 HIS   B NE2 1 
ATOM   834  N  N   . ILE   A 1 110 ? 27.050  13.340  -7.870  1.00 17.95 ? 110 ILE   B N   1 
ATOM   835  C  CA  . ILE   A 1 110 ? 27.355  14.033  -6.635  1.00 19.39 ? 110 ILE   B CA  1 
ATOM   836  C  C   . ILE   A 1 110 ? 27.475  15.513  -7.003  1.00 18.52 ? 110 ILE   B C   1 
ATOM   837  O  O   . ILE   A 1 110 ? 28.093  15.837  -8.009  1.00 22.70 ? 110 ILE   B O   1 
ATOM   838  C  CB  . ILE   A 1 110 ? 28.650  13.437  -6.025  1.00 19.96 ? 110 ILE   B CB  1 
ATOM   839  C  CG1 . ILE   A 1 110 ? 28.485  11.923  -5.824  1.00 22.03 ? 110 ILE   B CG1 1 
ATOM   840  C  CG2 . ILE   A 1 110 ? 29.039  14.092  -4.708  1.00 18.75 ? 110 ILE   B CG2 1 
ATOM   841  C  CD1 . ILE   A 1 110 ? 29.722  11.255  -5.319  1.00 23.53 ? 110 ILE   B CD1 1 
ATOM   842  N  N   . VAL   A 1 111 ? 26.820  16.387  -6.245  1.00 19.41 ? 111 VAL   B N   1 
ATOM   843  C  CA  . VAL   A 1 111 ? 26.824  17.804  -6.585  1.00 20.63 ? 111 VAL   B CA  1 
ATOM   844  C  C   . VAL   A 1 111 ? 27.588  18.559  -5.497  1.00 22.06 ? 111 VAL   B C   1 
ATOM   845  O  O   . VAL   A 1 111 ? 27.084  18.706  -4.375  1.00 22.42 ? 111 VAL   B O   1 
ATOM   846  C  CB  . VAL   A 1 111 ? 25.392  18.366  -6.715  1.00 21.20 ? 111 VAL   B CB  1 
ATOM   847  C  CG1 . VAL   A 1 111 ? 25.424  19.834  -7.145  1.00 20.90 ? 111 VAL   B CG1 1 
ATOM   848  C  CG2 . VAL   A 1 111 ? 24.535  17.528  -7.669  1.00 20.85 ? 111 VAL   B CG2 1 
ATOM   849  N  N   . ASP   A 1 112 ? 28.778  19.052  -5.857  1.00 24.45 ? 112 ASP   B N   1 
ATOM   850  C  CA  . ASP   A 1 112 ? 29.655  19.822  -4.976  1.00 26.12 ? 112 ASP   B CA  1 
ATOM   851  C  C   . ASP   A 1 112 ? 29.904  19.045  -3.684  1.00 25.63 ? 112 ASP   B C   1 
ATOM   852  O  O   . ASP   A 1 112 ? 29.829  19.593  -2.586  1.00 24.67 ? 112 ASP   B O   1 
ATOM   853  C  CB  . ASP   A 1 112 ? 29.099  21.218  -4.681  1.00 29.21 ? 112 ASP   B CB  1 
ATOM   854  C  CG  . ASP   A 1 112 ? 29.039  22.101  -5.910  1.00 32.54 ? 112 ASP   B CG  1 
ATOM   855  O  OD1 . ASP   A 1 112 ? 30.017  22.102  -6.721  1.00 32.64 ? 112 ASP   B OD1 1 
ATOM   856  O  OD2 . ASP   A 1 112 ? 28.034  22.817  -6.026  1.00 40.75 ? 112 ASP   B OD2 1 
ATOM   857  N  N   . GLY   A 1 113 ? 30.181  17.750  -3.851  1.00 23.56 ? 113 GLY   B N   1 
ATOM   858  C  CA  . GLY   A 1 113 ? 30.488  16.867  -2.743  1.00 22.71 ? 113 GLY   B CA  1 
ATOM   859  C  C   . GLY   A 1 113 ? 29.237  16.265  -2.106  1.00 23.50 ? 113 GLY   B C   1 
ATOM   860  O  O   . GLY   A 1 113 ? 29.344  15.342  -1.295  1.00 25.34 ? 113 GLY   B O   1 
ATOM   861  N  N   . VAL   A 1 114 ? 28.052  16.768  -2.473  1.00 22.96 ? 114 VAL   B N   1 
ATOM   862  C  CA  . VAL   A 1 114 ? 26.852  16.348  -1.756  1.00 23.16 ? 114 VAL   B CA  1 
ATOM   863  C  C   . VAL   A 1 114 ? 26.245  15.148  -2.466  1.00 22.49 ? 114 VAL   B C   1 
ATOM   864  O  O   . VAL   A 1 114 ? 25.925  15.244  -3.642  1.00 21.49 ? 114 VAL   B O   1 
ATOM   865  C  CB  . VAL   A 1 114 ? 25.798  17.464  -1.647  1.00 22.92 ? 114 VAL   B CB  1 
ATOM   866  C  CG1 . VAL   A 1 114 ? 24.508  16.953  -1.017  1.00 25.33 ? 114 VAL   B CG1 1 
ATOM   867  C  CG2 . VAL   A 1 114 ? 26.322  18.682  -0.912  1.00 22.52 ? 114 VAL   B CG2 1 
ATOM   868  N  N   . SER   A 1 115 ? 26.107  14.035  -1.739  1.00 24.80 ? 115 SER   B N   1 
ATOM   869  C  CA  . SER   A 1 115 ? 25.380  12.866  -2.199  1.00 26.10 ? 115 SER   B CA  1 
ATOM   870  C  C   . SER   A 1 115 ? 23.986  12.893  -1.619  1.00 27.69 ? 115 SER   B C   1 
ATOM   871  O  O   . SER   A 1 115 ? 23.800  13.211  -0.442  1.00 31.60 ? 115 SER   B O   1 
ATOM   872  C  CB  . SER   A 1 115 ? 26.046  11.581  -1.793  1.00 27.97 ? 115 SER   B CB  1 
ATOM   873  O  OG  . SER   A 1 115 ? 27.363  11.567  -2.279  1.00 35.89 ? 115 SER   B OG  1 
ATOM   874  N  N   . TYR   A 1 116 ? 23.021  12.561  -2.473  1.00 23.91 ? 116 TYR   B N   1 
ATOM   875  C  CA  . TYR   A 1 116 ? 21.631  12.571  -2.081  1.00 22.63 ? 116 TYR   B CA  1 
ATOM   876  C  C   . TYR   A 1 116 ? 21.357  11.189  -1.505  1.00 19.40 ? 116 TYR   B C   1 
ATOM   877  O  O   . TYR   A 1 116 ? 22.213  10.312  -1.606  1.00 21.58 ? 116 TYR   B O   1 
ATOM   878  C  CB  . TYR   A 1 116 ? 20.787  12.990  -3.296  1.00 20.69 ? 116 TYR   B CB  1 
ATOM   879  C  CG  . TYR   A 1 116 ? 20.928  14.463  -3.567  1.00 22.37 ? 116 TYR   B CG  1 
ATOM   880  C  CD1 . TYR   A 1 116 ? 20.159  15.351  -2.833  1.00 25.45 ? 116 TYR   B CD1 1 
ATOM   881  C  CD2 . TYR   A 1 116 ? 21.837  14.979  -4.488  1.00 23.30 ? 116 TYR   B CD2 1 
ATOM   882  C  CE1 . TYR   A 1 116 ? 20.264  16.722  -2.995  1.00 28.74 ? 116 TYR   B CE1 1 
ATOM   883  C  CE2 . TYR   A 1 116 ? 21.945  16.361  -4.675  1.00 26.92 ? 116 TYR   B CE2 1 
ATOM   884  C  CZ  . TYR   A 1 116 ? 21.172  17.230  -3.902  1.00 28.67 ? 116 TYR   B CZ  1 
ATOM   885  O  OH  . TYR   A 1 116 ? 21.174  18.591  -4.001  1.00 32.89 ? 116 TYR   B OH  1 
ATOM   886  N  N   . ALA   A 1 117 ? 20.179  11.027  -0.892  1.00 17.51 ? 117 ALA   B N   1 
ATOM   887  C  CA  . ALA   A 1 117 ? 19.718  9.742   -0.367  1.00 17.24 ? 117 ALA   B CA  1 
ATOM   888  C  C   . ALA   A 1 117 ? 19.576  8.717   -1.487  1.00 17.08 ? 117 ALA   B C   1 
ATOM   889  O  O   . ALA   A 1 117 ? 19.793  7.521   -1.280  1.00 17.88 ? 117 ALA   B O   1 
ATOM   890  C  CB  . ALA   A 1 117 ? 18.418  9.924   0.373   1.00 17.34 ? 117 ALA   B CB  1 
ATOM   891  N  N   . ALA   A 1 118 ? 19.185  9.167   -2.687  1.00 15.57 ? 118 ALA   B N   1 
ATOM   892  C  CA  . ALA   A 1 118 ? 18.940  8.189   -3.742  1.00 13.61 ? 118 ALA   B CA  1 
ATOM   893  C  C   . ALA   A 1 118 ? 18.843  8.919   -5.078  1.00 13.48 ? 118 ALA   B C   1 
ATOM   894  O  O   . ALA   A 1 118 ? 18.835  10.152  -5.091  1.00 14.17 ? 118 ALA   B O   1 
ATOM   895  C  CB  . ALA   A 1 118 ? 17.686  7.373   -3.476  1.00 12.84 ? 118 ALA   B CB  1 
ATOM   896  N  N   . GLU   A 1 119 ? 18.722  8.164   -6.180  1.00 14.13 ? 119 GLU   B N   1 
ATOM   897  C  CA  . GLU   A 1 119 ? 18.675  8.796   -7.493  1.00 15.41 ? 119 GLU   B CA  1 
ATOM   898  C  C   . GLU   A 1 119 ? 17.810  7.941   -8.410  1.00 16.54 ? 119 GLU   B C   1 
ATOM   899  O  O   . GLU   A 1 119 ? 18.140  6.776   -8.636  1.00 16.99 ? 119 GLU   B O   1 
ATOM   900  C  CB  . GLU   A 1 119 ? 20.105  8.989   -8.032  1.00 16.36 ? 119 GLU   B CB  1 
ATOM   901  C  CG  . GLU   A 1 119 ? 20.230  9.776   -9.340  1.00 19.47 ? 119 GLU   B CG  1 
ATOM   902  C  CD  . GLU   A 1 119 ? 21.664  10.073  -9.809  1.00 21.43 ? 119 GLU   B CD  1 
ATOM   903  O  OE1 . GLU   A 1 119 ? 22.496  10.270  -8.943  1.00 22.71 ? 119 GLU   B OE1 1 
ATOM   904  O  OE2 . GLU   A 1 119 ? 21.949  10.093  -11.069 1.00 21.60 ? 119 GLU   B OE2 1 
ATOM   905  N  N   . LEU   A 1 120 ? 16.756  8.555   -8.970  1.00 15.17 ? 120 LEU   B N   1 
ATOM   906  C  CA  . LEU   A 1 120 ? 15.849  7.910   -9.918  1.00 17.21 ? 120 LEU   B CA  1 
ATOM   907  C  C   . LEU   A 1 120 ? 16.366  8.161   -11.333 1.00 16.56 ? 120 LEU   B C   1 
ATOM   908  O  O   . LEU   A 1 120 ? 16.793  9.282   -11.629 1.00 15.98 ? 120 LEU   B O   1 
ATOM   909  C  CB  . LEU   A 1 120 ? 14.449  8.514   -9.723  1.00 17.63 ? 120 LEU   B CB  1 
ATOM   910  C  CG  . LEU   A 1 120 ? 13.311  7.860   -10.498 1.00 21.08 ? 120 LEU   B CG  1 
ATOM   911  C  CD1 . LEU   A 1 120 ? 12.789  6.660   -9.710  1.00 18.58 ? 120 LEU   B CD1 1 
ATOM   912  C  CD2 . LEU   A 1 120 ? 12.208  8.893   -10.773 1.00 20.56 ? 120 LEU   B CD2 1 
ATOM   913  N  N   . HIS   A 1 121 ? 16.442  7.086   -12.153 1.00 16.21 ? 121 HIS   B N   1 
ATOM   914  C  CA  . HIS   A 1 121 ? 16.872  7.164   -13.545 1.00 14.79 ? 121 HIS   B CA  1 
ATOM   915  C  C   . HIS   A 1 121 ? 15.713  6.802   -14.451 1.00 15.30 ? 121 HIS   B C   1 
ATOM   916  O  O   . HIS   A 1 121 ? 15.096  5.755   -14.255 1.00 15.34 ? 121 HIS   B O   1 
ATOM   917  C  CB  . HIS   A 1 121 ? 18.063  6.247   -13.847 1.00 15.74 ? 121 HIS   B CB  1 
ATOM   918  C  CG  . HIS   A 1 121 ? 19.326  6.766   -13.278 1.00 15.96 ? 121 HIS   B CG  1 
ATOM   919  N  ND1 . HIS   A 1 121 ? 20.422  5.978   -13.075 1.00 15.76 ? 121 HIS   B ND1 1 
ATOM   920  C  CD2 . HIS   A 1 121 ? 19.633  8.007   -12.845 1.00 15.76 ? 121 HIS   B CD2 1 
ATOM   921  C  CE1 . HIS   A 1 121 ? 21.394  6.721   -12.531 1.00 16.51 ? 121 HIS   B CE1 1 
ATOM   922  N  NE2 . HIS   A 1 121 ? 20.896  7.963   -12.347 1.00 16.23 ? 121 HIS   B NE2 1 
ATOM   923  N  N   . VAL   A 1 122 ? 15.400  7.703   -15.395 1.00 14.16 ? 122 VAL   B N   1 
ATOM   924  C  CA  . VAL   A 1 122 ? 14.354  7.460   -16.382 1.00 14.59 ? 122 VAL   B CA  1 
ATOM   925  C  C   . VAL   A 1 122 ? 15.061  7.256   -17.726 1.00 14.71 ? 122 VAL   B C   1 
ATOM   926  O  O   . VAL   A 1 122 ? 15.738  8.143   -18.211 1.00 13.33 ? 122 VAL   B O   1 
ATOM   927  C  CB  . VAL   A 1 122 ? 13.342  8.633   -16.438 1.00 14.44 ? 122 VAL   B CB  1 
ATOM   928  C  CG1 . VAL   A 1 122 ? 12.152  8.277   -17.318 1.00 15.40 ? 122 VAL   B CG1 1 
ATOM   929  C  CG2 . VAL   A 1 122 ? 12.864  9.060   -15.049 1.00 14.88 ? 122 VAL   B CG2 1 
ATOM   930  N  N   . VAL   A 1 123 ? 14.982  6.047   -18.291 1.00 14.54 ? 123 VAL   B N   1 
ATOM   931  C  CA  . VAL   A 1 123 ? 15.804  5.666   -19.433 1.00 14.62 ? 123 VAL   B CA  1 
ATOM   932  C  C   . VAL   A 1 123 ? 14.997  5.765   -20.738 1.00 14.54 ? 123 VAL   B C   1 
ATOM   933  O  O   . VAL   A 1 123 ? 13.898  5.214   -20.854 1.00 15.55 ? 123 VAL   B O   1 
ATOM   934  C  CB  . VAL   A 1 123 ? 16.375  4.246   -19.254 1.00 16.49 ? 123 VAL   B CB  1 
ATOM   935  C  CG1 . VAL   A 1 123 ? 17.102  3.778   -20.509 1.00 15.60 ? 123 VAL   B CG1 1 
ATOM   936  C  CG2 . VAL   A 1 123 ? 17.272  4.115   -18.008 1.00 16.23 ? 123 VAL   B CG2 1 
ATOM   937  N  N   . HIS   A 1 124 ? 15.552  6.451   -21.728 1.00 13.87 ? 124 HIS   B N   1 
ATOM   938  C  CA  . HIS   A 1 124 ? 14.864  6.628   -23.007 1.00 14.50 ? 124 HIS   B CA  1 
ATOM   939  C  C   . HIS   A 1 124 ? 15.799  6.309   -24.176 1.00 14.71 ? 124 HIS   B C   1 
ATOM   940  O  O   . HIS   A 1 124 ? 17.013  6.419   -24.027 1.00 14.67 ? 124 HIS   B O   1 
ATOM   941  C  CB  . HIS   A 1 124 ? 14.443  8.091   -23.237 1.00 14.51 ? 124 HIS   B CB  1 
ATOM   942  C  CG  . HIS   A 1 124 ? 13.778  8.801   -22.116 1.00 14.85 ? 124 HIS   B CG  1 
ATOM   943  N  ND1 . HIS   A 1 124 ? 14.435  9.111   -20.956 1.00 16.06 ? 124 HIS   B ND1 1 
ATOM   944  C  CD2 . HIS   A 1 124 ? 12.537  9.340   -22.005 1.00 14.08 ? 124 HIS   B CD2 1 
ATOM   945  C  CE1 . HIS   A 1 124 ? 13.615  9.753   -20.145 1.00 14.77 ? 124 HIS   B CE1 1 
ATOM   946  N  NE2 . HIS   A 1 124 ? 12.447  9.873   -20.747 1.00 14.43 ? 124 HIS   B NE2 1 
ATOM   947  N  N   . TRP   A 1 125 ? 15.235  5.979   -25.364 1.00 14.94 ? 125 TRP   B N   1 
ATOM   948  C  CA  . TRP   A 1 125 ? 16.029  5.711   -26.564 1.00 15.67 ? 125 TRP   B CA  1 
ATOM   949  C  C   . TRP   A 1 125 ? 15.531  6.489   -27.792 1.00 16.16 ? 125 TRP   B C   1 
ATOM   950  O  O   . TRP   A 1 125 ? 14.357  6.831   -27.934 1.00 16.35 ? 125 TRP   B O   1 
ATOM   951  C  CB  . TRP   A 1 125 ? 16.133  4.212   -26.889 1.00 14.61 ? 125 TRP   B CB  1 
ATOM   952  C  CG  . TRP   A 1 125 ? 14.808  3.544   -27.131 1.00 17.13 ? 125 TRP   B CG  1 
ATOM   953  C  CD1 . TRP   A 1 125 ? 13.942  3.062   -26.191 1.00 18.24 ? 125 TRP   B CD1 1 
ATOM   954  C  CD2 . TRP   A 1 125 ? 14.232  3.189   -28.400 1.00 18.74 ? 125 TRP   B CD2 1 
ATOM   955  N  NE1 . TRP   A 1 125 ? 12.865  2.448   -26.783 1.00 18.97 ? 125 TRP   B NE1 1 
ATOM   956  C  CE2 . TRP   A 1 125 ? 12.998  2.548   -28.136 1.00 19.63 ? 125 TRP   B CE2 1 
ATOM   957  C  CE3 . TRP   A 1 125 ? 14.608  3.400   -29.734 1.00 19.34 ? 125 TRP   B CE3 1 
ATOM   958  C  CZ2 . TRP   A 1 125 ? 12.173  2.055   -29.153 1.00 20.26 ? 125 TRP   B CZ2 1 
ATOM   959  C  CZ3 . TRP   A 1 125 ? 13.797  2.903   -30.734 1.00 19.22 ? 125 TRP   B CZ3 1 
ATOM   960  C  CH2 . TRP   A 1 125 ? 12.584  2.275   -30.447 1.00 19.29 ? 125 TRP   B CH2 1 
ATOM   961  N  N   . ASN   A 1 126 ? 16.464  6.706   -28.710 1.00 16.69 ? 126 ASN   B N   1 
ATOM   962  C  CA  . ASN   A 1 126 ? 16.306  7.574   -29.855 1.00 18.55 ? 126 ASN   B CA  1 
ATOM   963  C  C   . ASN   A 1 126 ? 15.602  6.816   -30.983 1.00 18.43 ? 126 ASN   B C   1 
ATOM   964  O  O   . ASN   A 1 126 ? 16.268  6.253   -31.845 1.00 17.38 ? 126 ASN   B O   1 
ATOM   965  C  CB  . ASN   A 1 126 ? 17.672  8.071   -30.308 1.00 19.52 ? 126 ASN   B CB  1 
ATOM   966  C  CG  . ASN   A 1 126 ? 17.610  9.126   -31.380 1.00 22.60 ? 126 ASN   B CG  1 
ATOM   967  O  OD1 . ASN   A 1 126 ? 16.562  9.322   -31.982 1.00 24.79 ? 126 ASN   B OD1 1 
ATOM   968  N  ND2 . ASN   A 1 126 ? 18.720  9.825   -31.601 1.00 19.91 ? 126 ASN   B ND2 1 
ATOM   969  N  N   . SER   A 1 127 ? 14.272  6.926   -31.000 1.00 19.61 ? 127 SER   B N   1 
ATOM   970  C  CA  . SER   A 1 127 ? 13.397  6.238   -31.942 1.00 20.73 ? 127 SER   B CA  1 
ATOM   971  C  C   . SER   A 1 127 ? 13.358  6.975   -33.279 1.00 20.72 ? 127 SER   B C   1 
ATOM   972  O  O   . SER   A 1 127 ? 12.950  6.390   -34.269 1.00 21.62 ? 127 SER   B O   1 
ATOM   973  C  CB  . SER   A 1 127 ? 12.003  5.960   -31.364 1.00 21.00 ? 127 SER   B CB  1 
ATOM   974  O  OG  . SER   A 1 127 ? 11.328  7.151   -30.983 1.00 23.12 ? 127 SER   B OG  1 
ATOM   975  N  N   . ASP   A 1 128 ? 13.835  8.223   -33.304 1.00 21.10 ? 128 ASP   B N   1 
ATOM   976  C  CA  . ASP   A 1 128 ? 13.947  8.997   -34.527 1.00 24.00 ? 128 ASP   B CA  1 
ATOM   977  C  C   . ASP   A 1 128 ? 15.109  8.515   -35.391 1.00 24.46 ? 128 ASP   B C   1 
ATOM   978  O  O   . ASP   A 1 128 ? 15.107  8.770   -36.586 1.00 24.32 ? 128 ASP   B O   1 
ATOM   979  C  CB  . ASP   A 1 128 ? 14.018  10.504  -34.257 1.00 27.94 ? 128 ASP   B CB  1 
ATOM   980  C  CG  . ASP   A 1 128 ? 12.655  11.071  -33.885 1.00 32.21 ? 128 ASP   B CG  1 
ATOM   981  O  OD1 . ASP   A 1 128 ? 11.695  10.275  -33.754 1.00 36.94 ? 128 ASP   B OD1 1 
ATOM   982  O  OD2 . ASP   A 1 128 ? 12.557  12.290  -33.725 1.00 32.31 ? 128 ASP   B OD2 1 
ATOM   983  N  N   . LYS   A 1 129 ? 16.081  7.792   -34.808 1.00 20.30 ? 129 LYS   B N   1 
ATOM   984  C  CA  . LYS   A 1 129 ? 17.253  7.399   -35.558 1.00 23.00 ? 129 LYS   B CA  1 
ATOM   985  C  C   . LYS   A 1 129 ? 17.458  5.894   -35.555 1.00 21.45 ? 129 LYS   B C   1 
ATOM   986  O  O   . LYS   A 1 129 ? 18.057  5.393   -36.497 1.00 23.01 ? 129 LYS   B O   1 
ATOM   987  C  CB  . LYS   A 1 129 ? 18.524  8.049   -35.005 1.00 25.74 ? 129 LYS   B CB  1 
ATOM   988  C  CG  . LYS   A 1 129 ? 18.880  9.393   -35.616 1.00 30.85 ? 129 LYS   B CG  1 
ATOM   989  C  CD  . LYS   A 1 129 ? 20.243  9.888   -35.180 1.00 29.61 ? 129 LYS   B CD  1 
ATOM   990  C  CE  . LYS   A 1 129 ? 21.362  9.507   -36.124 1.00 34.17 ? 129 LYS   B CE  1 
ATOM   991  N  NZ  . LYS   A 1 129 ? 22.682  9.936   -35.609 1.00 30.23 ? 129 LYS   B NZ  1 
ATOM   992  N  N   . TYR   A 1 130 ? 17.001  5.183   -34.502 1.00 19.69 ? 130 TYR   B N   1 
ATOM   993  C  CA  . TYR   A 1 130 ? 17.260  3.756   -34.353 1.00 18.71 ? 130 TYR   B CA  1 
ATOM   994  C  C   . TYR   A 1 130 ? 15.968  2.961   -34.328 1.00 18.58 ? 130 TYR   B C   1 
ATOM   995  O  O   . TYR   A 1 130 ? 14.950  3.457   -33.870 1.00 19.90 ? 130 TYR   B O   1 
ATOM   996  C  CB  . TYR   A 1 130 ? 18.133  3.485   -33.117 1.00 19.04 ? 130 TYR   B CB  1 
ATOM   997  C  CG  . TYR   A 1 130 ? 19.388  4.311   -33.228 1.00 21.24 ? 130 TYR   B CG  1 
ATOM   998  C  CD1 . TYR   A 1 130 ? 20.288  4.063   -34.256 1.00 23.06 ? 130 TYR   B CD1 1 
ATOM   999  C  CD2 . TYR   A 1 130 ? 19.596  5.426   -32.445 1.00 21.46 ? 130 TYR   B CD2 1 
ATOM   1000 C  CE1 . TYR   A 1 130 ? 21.414  4.849   -34.451 1.00 27.44 ? 130 TYR   B CE1 1 
ATOM   1001 C  CE2 . TYR   A 1 130 ? 20.720  6.219   -32.619 1.00 24.66 ? 130 TYR   B CE2 1 
ATOM   1002 C  CZ  . TYR   A 1 130 ? 21.632  5.934   -33.622 1.00 26.81 ? 130 TYR   B CZ  1 
ATOM   1003 O  OH  . TYR   A 1 130 ? 22.739  6.711   -33.818 1.00 25.73 ? 130 TYR   B OH  1 
ATOM   1004 N  N   . PRO   A 1 131 ? 15.958  1.726   -34.853 1.00 19.27 ? 131 PRO   B N   1 
ATOM   1005 C  CA  . PRO   A 1 131 ? 14.730  0.916   -34.849 1.00 22.93 ? 131 PRO   B CA  1 
ATOM   1006 C  C   . PRO   A 1 131 ? 14.289  0.321   -33.500 1.00 22.76 ? 131 PRO   B C   1 
ATOM   1007 O  O   . PRO   A 1 131 ? 13.131  -0.087  -33.327 1.00 23.34 ? 131 PRO   B O   1 
ATOM   1008 C  CB  . PRO   A 1 131 ? 15.080  -0.190  -35.861 1.00 21.66 ? 131 PRO   B CB  1 
ATOM   1009 C  CG  . PRO   A 1 131 ? 16.569  -0.365  -35.677 1.00 23.14 ? 131 PRO   B CG  1 
ATOM   1010 C  CD  . PRO   A 1 131 ? 17.096  1.050   -35.493 1.00 20.52 ? 131 PRO   B CD  1 
ATOM   1011 N  N   . SER   A 1 132 ? 15.219  0.191   -32.547 1.00 23.91 ? 132 SER   B N   1 
ATOM   1012 C  CA  . SER   A 1 132 ? 14.926  -0.510  -31.305 1.00 20.78 ? 132 SER   B CA  1 
ATOM   1013 C  C   . SER   A 1 132 ? 15.864  -0.008  -30.210 1.00 21.43 ? 132 SER   B C   1 
ATOM   1014 O  O   . SER   A 1 132 ? 16.934  0.521   -30.504 1.00 22.07 ? 132 SER   B O   1 
ATOM   1015 C  CB  . SER   A 1 132 ? 15.111  -1.997  -31.512 1.00 21.18 ? 132 SER   B CB  1 
ATOM   1016 O  OG  . SER   A 1 132 ? 16.500  -2.294  -31.526 1.00 23.47 ? 132 SER   B OG  1 
ATOM   1017 N  N   . PHE   A 1 133 ? 15.460  -0.216  -28.948 1.00 20.79 ? 133 PHE   B N   1 
ATOM   1018 C  CA  . PHE   A 1 133 ? 16.301  0.109   -27.802 1.00 21.54 ? 133 PHE   B CA  1 
ATOM   1019 C  C   . PHE   A 1 133 ? 17.678  -0.552  -27.956 1.00 22.74 ? 133 PHE   B C   1 
ATOM   1020 O  O   . PHE   A 1 133 ? 18.702  0.102   -27.783 1.00 22.71 ? 133 PHE   B O   1 
ATOM   1021 C  CB  . PHE   A 1 133 ? 15.593  -0.249  -26.486 1.00 21.01 ? 133 PHE   B CB  1 
ATOM   1022 C  CG  . PHE   A 1 133 ? 16.494  -0.131  -25.279 1.00 22.07 ? 133 PHE   B CG  1 
ATOM   1023 C  CD1 . PHE   A 1 133 ? 16.650  1.081   -24.640 1.00 23.66 ? 133 PHE   B CD1 1 
ATOM   1024 C  CD2 . PHE   A 1 133 ? 17.229  -1.221  -24.823 1.00 26.56 ? 133 PHE   B CD2 1 
ATOM   1025 C  CE1 . PHE   A 1 133 ? 17.512  1.216   -23.565 1.00 26.53 ? 133 PHE   B CE1 1 
ATOM   1026 C  CE2 . PHE   A 1 133 ? 18.083  -1.095  -23.734 1.00 28.41 ? 133 PHE   B CE2 1 
ATOM   1027 C  CZ  . PHE   A 1 133 ? 18.239  0.130   -23.121 1.00 29.50 ? 133 PHE   B CZ  1 
ATOM   1028 N  N   . VAL   A 1 134 ? 17.695  -1.841  -28.330 1.00 23.69 ? 134 VAL   B N   1 
ATOM   1029 C  CA  . VAL   A 1 134 ? 18.931  -2.609  -28.448 1.00 27.73 ? 134 VAL   B CA  1 
ATOM   1030 C  C   . VAL   A 1 134 ? 19.902  -1.957  -29.433 1.00 29.54 ? 134 VAL   B C   1 
ATOM   1031 O  O   . VAL   A 1 134 ? 21.098  -1.864  -29.129 1.00 30.49 ? 134 VAL   B O   1 
ATOM   1032 C  CB  . VAL   A 1 134 ? 18.643  -4.074  -28.839 1.00 29.30 ? 134 VAL   B CB  1 
ATOM   1033 C  CG1 . VAL   A 1 134 ? 19.893  -4.939  -28.782 1.00 36.68 ? 134 VAL   B CG1 1 
ATOM   1034 C  CG2 . VAL   A 1 134 ? 17.582  -4.674  -27.943 1.00 32.38 ? 134 VAL   B CG2 1 
ATOM   1035 N  N   . GLU   A 1 135 ? 19.414  -1.537  -30.621 1.00 25.55 ? 135 GLU   B N   1 
ATOM   1036 C  CA  . GLU   A 1 135 ? 20.293  -0.906  -31.599 1.00 26.20 ? 135 GLU   B CA  1 
ATOM   1037 C  C   . GLU   A 1 135 ? 20.746  0.468   -31.093 1.00 26.08 ? 135 GLU   B C   1 
ATOM   1038 O  O   . GLU   A 1 135 ? 21.907  0.840   -31.293 1.00 25.83 ? 135 GLU   B O   1 
ATOM   1039 C  CB  . GLU   A 1 135 ? 19.663  -0.760  -32.998 1.00 28.36 ? 135 GLU   B CB  1 
ATOM   1040 C  CG  . GLU   A 1 135 ? 19.376  -2.071  -33.736 1.00 31.89 ? 135 GLU   B CG  1 
ATOM   1041 C  CD  . GLU   A 1 135 ? 20.594  -2.896  -34.138 1.00 38.03 ? 135 GLU   B CD  1 
ATOM   1042 O  OE1 . GLU   A 1 135 ? 20.427  -4.122  -34.345 1.00 44.68 ? 135 GLU   B OE1 1 
ATOM   1043 O  OE2 . GLU   A 1 135 ? 21.712  -2.317  -34.268 1.00 39.91 ? 135 GLU   B OE2 1 
ATOM   1044 N  N   . ALA   A 1 136 ? 19.825  1.230   -30.470 1.00 23.26 ? 136 ALA   B N   1 
ATOM   1045 C  CA  . ALA   A 1 136 ? 20.147  2.559   -29.936 1.00 21.90 ? 136 ALA   B CA  1 
ATOM   1046 C  C   . ALA   A 1 136 ? 21.199  2.487   -28.814 1.00 22.45 ? 136 ALA   B C   1 
ATOM   1047 O  O   . ALA   A 1 136 ? 22.046  3.369   -28.663 1.00 20.04 ? 136 ALA   B O   1 
ATOM   1048 C  CB  . ALA   A 1 136 ? 18.892  3.249   -29.442 1.00 20.65 ? 136 ALA   B CB  1 
ATOM   1049 N  N   . ALA   A 1 137 ? 21.126  1.427   -28.011 1.00 23.28 ? 137 ALA   B N   1 
ATOM   1050 C  CA  . ALA   A 1 137 ? 21.987  1.312   -26.842 1.00 25.68 ? 137 ALA   B CA  1 
ATOM   1051 C  C   . ALA   A 1 137 ? 23.470  1.329   -27.228 1.00 29.04 ? 137 ALA   B C   1 
ATOM   1052 O  O   . ALA   A 1 137 ? 24.294  1.593   -26.365 1.00 27.59 ? 137 ALA   B O   1 
ATOM   1053 C  CB  . ALA   A 1 137 ? 21.661  0.034   -26.125 1.00 24.68 ? 137 ALA   B CB  1 
ATOM   1054 N  N   . HIS   A 1 138 ? 23.790  1.030   -28.505 1.00 30.93 ? 138 HIS   B N   1 
ATOM   1055 C  CA  . HIS   A 1 138 ? 25.153  0.870   -29.014 1.00 34.36 ? 138 HIS   B CA  1 
ATOM   1056 C  C   . HIS   A 1 138 ? 25.650  2.073   -29.814 1.00 33.98 ? 138 HIS   B C   1 
ATOM   1057 O  O   . HIS   A 1 138 ? 26.678  1.985   -30.490 1.00 33.98 ? 138 HIS   B O   1 
ATOM   1058 C  CB  . HIS   A 1 138 ? 25.262  -0.403  -29.866 1.00 36.76 ? 138 HIS   B CB  1 
ATOM   1059 C  CG  . HIS   A 1 138 ? 25.145  -1.620  -29.027 1.00 39.75 ? 138 HIS   B CG  1 
ATOM   1060 N  ND1 . HIS   A 1 138 ? 26.236  -2.174  -28.394 1.00 44.47 ? 138 HIS   B ND1 1 
ATOM   1061 C  CD2 . HIS   A 1 138 ? 24.069  -2.348  -28.655 1.00 43.82 ? 138 HIS   B CD2 1 
ATOM   1062 C  CE1 . HIS   A 1 138 ? 25.846  -3.223  -27.690 1.00 44.22 ? 138 HIS   B CE1 1 
ATOM   1063 N  NE2 . HIS   A 1 138 ? 24.516  -3.350  -27.832 1.00 47.40 ? 138 HIS   B NE2 1 
ATOM   1064 N  N   . GLU   A 1 139 ? 24.922  3.191   -29.770 1.00 30.50 ? 139 GLU   B N   1 
ATOM   1065 C  CA  . GLU   A 1 139 ? 25.332  4.364   -30.531 1.00 29.91 ? 139 GLU   B CA  1 
ATOM   1066 C  C   . GLU   A 1 139 ? 25.531  5.528   -29.570 1.00 28.84 ? 139 GLU   B C   1 
ATOM   1067 O  O   . GLU   A 1 139 ? 24.801  5.607   -28.587 1.00 25.82 ? 139 GLU   B O   1 
ATOM   1068 C  CB  . GLU   A 1 139 ? 24.210  4.789   -31.483 1.00 37.68 ? 139 GLU   B CB  1 
ATOM   1069 C  CG  . GLU   A 1 139 ? 23.767  3.675   -32.415 1.00 42.29 ? 139 GLU   B CG  1 
ATOM   1070 C  CD  . GLU   A 1 139 ? 24.835  3.325   -33.436 1.00 43.74 ? 139 GLU   B CD  1 
ATOM   1071 O  OE1 . GLU   A 1 139 ? 24.693  2.277   -34.099 1.00 51.00 ? 139 GLU   B OE1 1 
ATOM   1072 O  OE2 . GLU   A 1 139 ? 25.813  4.100   -33.557 1.00 49.59 ? 139 GLU   B OE2 1 
ATOM   1073 N  N   . PRO   A 1 140 ? 26.446  6.486   -29.861 1.00 27.54 ? 140 PRO   B N   1 
ATOM   1074 C  CA  . PRO   A 1 140 ? 26.749  7.577   -28.939 1.00 26.50 ? 140 PRO   B CA  1 
ATOM   1075 C  C   . PRO   A 1 140 ? 25.566  8.502   -28.662 1.00 27.12 ? 140 PRO   B C   1 
ATOM   1076 O  O   . PRO   A 1 140 ? 25.532  9.193   -27.637 1.00 27.31 ? 140 PRO   B O   1 
ATOM   1077 C  CB  . PRO   A 1 140 ? 27.817  8.419   -29.668 1.00 28.03 ? 140 PRO   B CB  1 
ATOM   1078 C  CG  . PRO   A 1 140 ? 28.375  7.517   -30.735 1.00 28.88 ? 140 PRO   B CG  1 
ATOM   1079 C  CD  . PRO   A 1 140 ? 27.250  6.566   -31.097 1.00 29.46 ? 140 PRO   B CD  1 
ATOM   1080 N  N   . ASP   A 1 141 ? 24.624  8.556   -29.604 1.00 23.60 ? 141 ASP   B N   1 
ATOM   1081 C  CA  . ASP   A 1 141 ? 23.459  9.404   -29.428 1.00 21.60 ? 141 ASP   B CA  1 
ATOM   1082 C  C   . ASP   A 1 141 ? 22.233  8.514   -29.213 1.00 20.51 ? 141 ASP   B C   1 
ATOM   1083 O  O   . ASP   A 1 141 ? 21.098  8.960   -29.383 1.00 23.16 ? 141 ASP   B O   1 
ATOM   1084 C  CB  . ASP   A 1 141 ? 23.295  10.354  -30.618 1.00 25.99 ? 141 ASP   B CB  1 
ATOM   1085 C  CG  . ASP   A 1 141 ? 23.080  9.646   -31.950 1.00 28.09 ? 141 ASP   B CG  1 
ATOM   1086 O  OD1 . ASP   A 1 141 ? 23.405  8.423   -32.061 1.00 29.80 ? 141 ASP   B OD1 1 
ATOM   1087 O  OD2 . ASP   A 1 141 ? 22.577  10.298  -32.875 1.00 32.70 ? 141 ASP   B OD2 1 
ATOM   1088 N  N   . GLY   A 1 142 ? 22.456  7.284   -28.755 1.00 19.21 ? 142 GLY   B N   1 
ATOM   1089 C  CA  . GLY   A 1 142 ? 21.368  6.297   -28.693 1.00 19.30 ? 142 GLY   B CA  1 
ATOM   1090 C  C   . GLY   A 1 142 ? 20.381  6.507   -27.538 1.00 18.90 ? 142 GLY   B C   1 
ATOM   1091 O  O   . GLY   A 1 142 ? 19.167  6.296   -27.707 1.00 19.74 ? 142 GLY   B O   1 
ATOM   1092 N  N   . LEU   A 1 143 ? 20.896  6.865   -26.347 1.00 18.45 ? 143 LEU   B N   1 
ATOM   1093 C  CA  . LEU   A 1 143 ? 20.098  6.786   -25.127 1.00 17.21 ? 143 LEU   B CA  1 
ATOM   1094 C  C   . LEU   A 1 143 ? 20.105  8.137   -24.425 1.00 16.50 ? 143 LEU   B C   1 
ATOM   1095 O  O   . LEU   A 1 143 ? 21.045  8.910   -24.558 1.00 17.22 ? 143 LEU   B O   1 
ATOM   1096 C  CB  . LEU   A 1 143 ? 20.677  5.723   -24.180 1.00 16.29 ? 143 LEU   B CB  1 
ATOM   1097 C  CG  . LEU   A 1 143 ? 20.758  4.261   -24.641 1.00 19.93 ? 143 LEU   B CG  1 
ATOM   1098 C  CD1 . LEU   A 1 143 ? 21.204  3.351   -23.491 1.00 19.60 ? 143 LEU   B CD1 1 
ATOM   1099 C  CD2 . LEU   A 1 143 ? 19.460  3.726   -25.252 1.00 18.51 ? 143 LEU   B CD2 1 
ATOM   1100 N  N   . ALA   A 1 144 ? 19.034  8.422   -23.677 1.00 16.33 ? 144 ALA   B N   1 
ATOM   1101 C  CA  . ALA   A 1 144 ? 19.015  9.608   -22.836 1.00 16.79 ? 144 ALA   B CA  1 
ATOM   1102 C  C   . ALA   A 1 144 ? 18.480  9.198   -21.468 1.00 16.35 ? 144 ALA   B C   1 
ATOM   1103 O  O   . ALA   A 1 144 ? 17.479  8.468   -21.354 1.00 14.77 ? 144 ALA   B O   1 
ATOM   1104 C  CB  . ALA   A 1 144 ? 18.191  10.710  -23.465 1.00 16.97 ? 144 ALA   B CB  1 
ATOM   1105 N  N   . VAL   A 1 145 ? 19.214  9.564   -20.418 1.00 14.84 ? 145 VAL   B N   1 
ATOM   1106 C  CA  . VAL   A 1 145 ? 18.711  9.171   -19.116 1.00 13.97 ? 145 VAL   B CA  1 
ATOM   1107 C  C   . VAL   A 1 145 ? 18.500  10.449  -18.321 1.00 15.78 ? 145 VAL   B C   1 
ATOM   1108 O  O   . VAL   A 1 145 ? 19.413  11.287  -18.237 1.00 14.16 ? 145 VAL   B O   1 
ATOM   1109 C  CB  . VAL   A 1 145 ? 19.663  8.219   -18.368 1.00 15.63 ? 145 VAL   B CB  1 
ATOM   1110 C  CG1 . VAL   A 1 145 ? 19.072  7.828   -17.013 1.00 17.37 ? 145 VAL   B CG1 1 
ATOM   1111 C  CG2 . VAL   A 1 145 ? 19.981  6.964   -19.187 1.00 15.35 ? 145 VAL   B CG2 1 
ATOM   1112 N  N   . LEU   A 1 146 ? 17.268  10.602  -17.814 1.00 16.20 ? 146 LEU   B N   1 
ATOM   1113 C  CA  . LEU   A 1 146 ? 16.929  11.708  -16.919 1.00 16.05 ? 146 LEU   B CA  1 
ATOM   1114 C  C   . LEU   A 1 146 ? 17.203  11.248  -15.486 1.00 15.95 ? 146 LEU   B C   1 
ATOM   1115 O  O   . LEU   A 1 146 ? 16.699  10.205  -15.087 1.00 18.49 ? 146 LEU   B O   1 
ATOM   1116 C  CB  . LEU   A 1 146 ? 15.446  12.048  -17.163 1.00 17.75 ? 146 LEU   B CB  1 
ATOM   1117 C  CG  . LEU   A 1 146 ? 14.849  13.196  -16.374 1.00 22.37 ? 146 LEU   B CG  1 
ATOM   1118 C  CD1 . LEU   A 1 146 ? 15.496  14.472  -16.858 1.00 23.39 ? 146 LEU   B CD1 1 
ATOM   1119 C  CD2 . LEU   A 1 146 ? 13.349  13.300  -16.665 1.00 23.84 ? 146 LEU   B CD2 1 
ATOM   1120 N  N   . GLY   A 1 147 ? 18.019  12.007  -14.742 1.00 15.34 ? 147 GLY   B N   1 
ATOM   1121 C  CA  . GLY   A 1 147 ? 18.315  11.725  -13.354 1.00 17.13 ? 147 GLY   B CA  1 
ATOM   1122 C  C   . GLY   A 1 147 ? 17.587  12.663  -12.397 1.00 18.03 ? 147 GLY   B C   1 
ATOM   1123 O  O   . GLY   A 1 147 ? 17.594  13.875  -12.600 1.00 17.86 ? 147 GLY   B O   1 
ATOM   1124 N  N   . VAL   A 1 148 ? 16.941  12.090  -11.371 1.00 17.49 ? 148 VAL   B N   1 
ATOM   1125 C  CA  . VAL   A 1 148 ? 16.267  12.900  -10.366 1.00 17.35 ? 148 VAL   B CA  1 
ATOM   1126 C  C   . VAL   A 1 148 ? 16.835  12.500  -9.014  1.00 17.50 ? 148 VAL   B C   1 
ATOM   1127 O  O   . VAL   A 1 148 ? 16.798  11.321  -8.645  1.00 18.03 ? 148 VAL   B O   1 
ATOM   1128 C  CB  . VAL   A 1 148 ? 14.736  12.697  -10.398 1.00 18.82 ? 148 VAL   B CB  1 
ATOM   1129 C  CG1 . VAL   A 1 148 ? 13.995  13.432  -9.277  1.00 16.10 ? 148 VAL   B CG1 1 
ATOM   1130 C  CG2 . VAL   A 1 148 ? 14.157  13.024  -11.767 1.00 18.46 ? 148 VAL   B CG2 1 
ATOM   1131 N  N   . PHE   A 1 149 ? 17.345  13.481  -8.258  1.00 16.18 ? 149 PHE   B N   1 
ATOM   1132 C  CA  . PHE   A 1 149 ? 17.771  13.196  -6.888  1.00 15.74 ? 149 PHE   B CA  1 
ATOM   1133 C  C   . PHE   A 1 149 ? 16.594  13.128  -5.918  1.00 15.70 ? 149 PHE   B C   1 
ATOM   1134 O  O   . PHE   A 1 149 ? 15.613  13.879  -6.036  1.00 16.44 ? 149 PHE   B O   1 
ATOM   1135 C  CB  . PHE   A 1 149 ? 18.705  14.298  -6.386  1.00 16.64 ? 149 PHE   B CB  1 
ATOM   1136 C  CG  . PHE   A 1 149 ? 19.940  14.474  -7.228  1.00 16.22 ? 149 PHE   B CG  1 
ATOM   1137 C  CD1 . PHE   A 1 149 ? 20.864  13.444  -7.359  1.00 14.83 ? 149 PHE   B CD1 1 
ATOM   1138 C  CD2 . PHE   A 1 149 ? 20.178  15.677  -7.875  1.00 16.29 ? 149 PHE   B CD2 1 
ATOM   1139 C  CE1 . PHE   A 1 149 ? 22.023  13.646  -8.098  1.00 16.38 ? 149 PHE   B CE1 1 
ATOM   1140 C  CE2 . PHE   A 1 149 ? 21.331  15.862  -8.635  1.00 15.44 ? 149 PHE   B CE2 1 
ATOM   1141 C  CZ  . PHE   A 1 149 ? 22.252  14.848  -8.725  1.00 15.21 ? 149 PHE   B CZ  1 
ATOM   1142 N  N   . LEU   A 1 150 ? 16.733  12.249  -4.910  1.00 16.30 ? 150 LEU   B N   1 
ATOM   1143 C  CA  . LEU   A 1 150 ? 15.798  12.131  -3.798  1.00 15.52 ? 150 LEU   B CA  1 
ATOM   1144 C  C   . LEU   A 1 150 ? 16.552  12.556  -2.534  1.00 17.71 ? 150 LEU   B C   1 
ATOM   1145 O  O   . LEU   A 1 150 ? 17.657  12.060  -2.279  1.00 19.91 ? 150 LEU   B O   1 
ATOM   1146 C  CB  . LEU   A 1 150 ? 15.322  10.675  -3.673  1.00 17.24 ? 150 LEU   B CB  1 
ATOM   1147 C  CG  . LEU   A 1 150 ? 14.365  10.158  -4.759  1.00 18.03 ? 150 LEU   B CG  1 
ATOM   1148 C  CD1 . LEU   A 1 150 ? 15.149  9.773   -6.003  1.00 19.13 ? 150 LEU   B CD1 1 
ATOM   1149 C  CD2 . LEU   A 1 150 ? 13.593  8.934   -4.250  1.00 18.96 ? 150 LEU   B CD2 1 
ATOM   1150 N  N   . GLN   A 1 151 ? 15.969  13.493  -1.768  1.00 17.63 ? 151 GLN   B N   1 
ATOM   1151 C  CA  . GLN   A 1 151 ? 16.484  13.911  -0.466  1.00 20.06 ? 151 GLN   B CA  1 
ATOM   1152 C  C   . GLN   A 1 151 ? 15.545  13.471  0.664   1.00 19.75 ? 151 GLN   B C   1 
ATOM   1153 O  O   . GLN   A 1 151 ? 14.319  13.468  0.500   1.00 18.00 ? 151 GLN   B O   1 
ATOM   1154 C  CB  . GLN   A 1 151 ? 16.724  15.433  -0.409  1.00 22.69 ? 151 GLN   B CB  1 
ATOM   1155 C  CG  . GLN   A 1 151 ? 15.533  16.235  -0.900  1.00 25.89 ? 151 GLN   B CG  1 
ATOM   1156 C  CD  . GLN   A 1 151 ? 15.513  17.708  -0.542  1.00 34.53 ? 151 GLN   B CD  1 
ATOM   1157 O  OE1 . GLN   A 1 151 ? 16.548  18.366  -0.416  1.00 33.19 ? 151 GLN   B OE1 1 
ATOM   1158 N  NE2 . GLN   A 1 151 ? 14.304  18.239  -0.391  1.00 37.62 ? 151 GLN   B NE2 1 
ATOM   1159 N  N   . ILE   A 1 152 ? 16.135  13.153  1.829   1.00 18.61 ? 152 ILE   B N   1 
ATOM   1160 C  CA  . ILE   A 1 152 ? 15.387  12.743  3.012   1.00 22.59 ? 152 ILE   B CA  1 
ATOM   1161 C  C   . ILE   A 1 152 ? 14.523  13.906  3.487   1.00 24.91 ? 152 ILE   B C   1 
ATOM   1162 O  O   . ILE   A 1 152 ? 14.984  15.039  3.599   1.00 23.04 ? 152 ILE   B O   1 
ATOM   1163 C  CB  . ILE   A 1 152 ? 16.283  12.225  4.156   1.00 24.14 ? 152 ILE   B CB  1 
ATOM   1164 C  CG1 . ILE   A 1 152 ? 16.972  10.908  3.777   1.00 23.65 ? 152 ILE   B CG1 1 
ATOM   1165 C  CG2 . ILE   A 1 152 ? 15.469  12.077  5.444   1.00 25.72 ? 152 ILE   B CG2 1 
ATOM   1166 C  CD1 . ILE   A 1 152 ? 16.010  9.732   3.589   1.00 22.41 ? 152 ILE   B CD1 1 
ATOM   1167 N  N   . GLY   A 1 153 ? 13.246  13.607  3.712   1.00 25.34 ? 153 GLY   B N   1 
ATOM   1168 C  CA  . GLY   A 1 153 ? 12.330  14.565  4.314   1.00 27.83 ? 153 GLY   B CA  1 
ATOM   1169 C  C   . GLY   A 1 153 ? 10.989  13.896  4.605   1.00 27.56 ? 153 GLY   B C   1 
ATOM   1170 O  O   . GLY   A 1 153 ? 10.938  12.751  5.040   1.00 25.34 ? 153 GLY   B O   1 
ATOM   1171 N  N   . GLU   A 1 154 ? 9.920   14.632  4.333   1.00 26.52 ? 154 GLU   B N   1 
ATOM   1172 C  CA  . GLU   A 1 154 ? 8.554   14.180  4.457   1.00 28.76 ? 154 GLU   B CA  1 
ATOM   1173 C  C   . GLU   A 1 154 ? 8.341   12.996  3.509   1.00 24.04 ? 154 GLU   B C   1 
ATOM   1174 O  O   . GLU   A 1 154 ? 8.935   12.943  2.423   1.00 24.31 ? 154 GLU   B O   1 
ATOM   1175 C  CB  . GLU   A 1 154 ? 7.655   15.375  4.124   1.00 36.53 ? 154 GLU   B CB  1 
ATOM   1176 C  CG  . GLU   A 1 154 ? 8.149   16.709  4.707   1.00 46.79 ? 154 GLU   B CG  1 
ATOM   1177 C  CD  . GLU   A 1 154 ? 9.257   17.555  4.046   1.00 59.98 ? 154 GLU   B CD  1 
ATOM   1178 O  OE1 . GLU   A 1 154 ? 10.073  17.024  3.223   1.00 49.35 ? 154 GLU   B OE1 1 
ATOM   1179 O  OE2 . GLU   A 1 154 ? 9.322   18.781  4.363   1.00 60.25 ? 154 GLU   B OE2 1 
ATOM   1180 N  N   . PRO   A 1 155 ? 7.450   12.032  3.846   1.00 22.96 ? 155 PRO   B N   1 
ATOM   1181 C  CA  . PRO   A 1 155 ? 7.176   10.910  2.952   1.00 22.25 ? 155 PRO   B CA  1 
ATOM   1182 C  C   . PRO   A 1 155 ? 6.574   11.462  1.658   1.00 23.37 ? 155 PRO   B C   1 
ATOM   1183 O  O   . PRO   A 1 155 ? 5.876   12.480  1.672   1.00 20.28 ? 155 PRO   B O   1 
ATOM   1184 C  CB  . PRO   A 1 155 ? 6.045   10.119  3.651   1.00 22.52 ? 155 PRO   B CB  1 
ATOM   1185 C  CG  . PRO   A 1 155 ? 6.104   10.551  5.091   1.00 22.72 ? 155 PRO   B CG  1 
ATOM   1186 C  CD  . PRO   A 1 155 ? 6.604   11.987  5.049   1.00 21.98 ? 155 PRO   B CD  1 
ATOM   1187 N  N   . ASN   A 1 156 ? 6.786   10.723  0.573   1.00 22.78 ? 156 ASN   B N   1 
ATOM   1188 C  CA  . ASN   A 1 156 ? 6.380   11.182  -0.742  1.00 23.14 ? 156 ASN   B CA  1 
ATOM   1189 C  C   . ASN   A 1 156 ? 5.246   10.270  -1.183  1.00 23.83 ? 156 ASN   B C   1 
ATOM   1190 O  O   . ASN   A 1 156 ? 5.479   9.086   -1.420  1.00 21.50 ? 156 ASN   B O   1 
ATOM   1191 C  CB  . ASN   A 1 156 ? 7.556   11.091  -1.719  1.00 22.75 ? 156 ASN   B CB  1 
ATOM   1192 C  CG  . ASN   A 1 156 ? 7.299   11.771  -3.052  1.00 22.00 ? 156 ASN   B CG  1 
ATOM   1193 O  OD1 . ASN   A 1 156 ? 6.156   11.862  -3.479  1.00 18.95 ? 156 ASN   B OD1 1 
ATOM   1194 N  ND2 . ASN   A 1 156 ? 8.343   12.276  -3.685  1.00 20.20 ? 156 ASN   B ND2 1 
ATOM   1195 N  N   . SER   A 1 157 ? 4.034   10.832  -1.286  1.00 21.87 ? 157 SER   B N   1 
ATOM   1196 C  CA  . SER   A 1 157 ? 2.884   10.020  -1.649  1.00 23.72 ? 157 SER   B CA  1 
ATOM   1197 C  C   . SER   A 1 157 ? 3.004   9.471   -3.075  1.00 25.20 ? 157 SER   B C   1 
ATOM   1198 O  O   . SER   A 1 157 ? 2.425   8.424   -3.376  1.00 26.36 ? 157 SER   B O   1 
ATOM   1199 C  CB  . SER   A 1 157 ? 1.577   10.766  -1.426  1.00 25.39 ? 157 SER   B CB  1 
ATOM   1200 O  OG  . SER   A 1 157 ? 1.526   11.891  -2.291  1.00 27.41 ? 157 SER   B OG  1 
ATOM   1201 N  N   . GLN   A 1 158 ? 3.806   10.115  -3.929  1.00 22.29 ? 158 GLN   B N   1 
ATOM   1202 C  CA  . GLN   A 1 158 ? 3.979   9.651   -5.306  1.00 25.24 ? 158 GLN   B CA  1 
ATOM   1203 C  C   . GLN   A 1 158 ? 4.830   8.379   -5.375  1.00 25.51 ? 158 GLN   B C   1 
ATOM   1204 O  O   . GLN   A 1 158 ? 4.885   7.756   -6.438  1.00 24.07 ? 158 GLN   B O   1 
ATOM   1205 C  CB  . GLN   A 1 158 ? 4.645   10.699  -6.201  1.00 27.18 ? 158 GLN   B CB  1 
ATOM   1206 C  CG  . GLN   A 1 158 ? 3.865   12.005  -6.356  1.00 30.90 ? 158 GLN   B CG  1 
ATOM   1207 C  CD  . GLN   A 1 158 ? 2.431   11.869  -6.825  1.00 32.67 ? 158 GLN   B CD  1 
ATOM   1208 O  OE1 . GLN   A 1 158 ? 1.583   12.711  -6.518  1.00 35.84 ? 158 GLN   B OE1 1 
ATOM   1209 N  NE2 . GLN   A 1 158 ? 2.142   10.830  -7.599  1.00 28.80 ? 158 GLN   B NE2 1 
ATOM   1210 N  N   . LEU   A 1 159 ? 5.490   8.005   -4.261  1.00 22.12 ? 159 LEU   B N   1 
ATOM   1211 C  CA  . LEU   A 1 159 ? 6.256   6.759   -4.207  1.00 22.06 ? 159 LEU   B CA  1 
ATOM   1212 C  C   . LEU   A 1 159 ? 5.457   5.620   -3.572  1.00 23.03 ? 159 LEU   B C   1 
ATOM   1213 O  O   . LEU   A 1 159 ? 5.920   4.487   -3.612  1.00 23.88 ? 159 LEU   B O   1 
ATOM   1214 C  CB  . LEU   A 1 159 ? 7.545   6.968   -3.405  1.00 22.82 ? 159 LEU   B CB  1 
ATOM   1215 C  CG  . LEU   A 1 159 ? 8.575   7.926   -3.999  1.00 25.75 ? 159 LEU   B CG  1 
ATOM   1216 C  CD1 . LEU   A 1 159 ? 9.642   8.255   -2.965  1.00 24.80 ? 159 LEU   B CD1 1 
ATOM   1217 C  CD2 . LEU   A 1 159 ? 9.227   7.348   -5.263  1.00 25.08 ? 159 LEU   B CD2 1 
ATOM   1218 N  N   . GLN   A 1 160 ? 4.277   5.898   -3.006  1.00 21.76 ? 160 GLN   B N   1 
ATOM   1219 C  CA  . GLN   A 1 160 ? 3.457   4.865   -2.379  1.00 26.60 ? 160 GLN   B CA  1 
ATOM   1220 C  C   . GLN   A 1 160 ? 3.145   3.725   -3.349  1.00 26.95 ? 160 GLN   B C   1 
ATOM   1221 O  O   . GLN   A 1 160 ? 3.158   2.550   -2.963  1.00 27.03 ? 160 GLN   B O   1 
ATOM   1222 C  CB  . GLN   A 1 160 ? 2.134   5.436   -1.847  1.00 30.84 ? 160 GLN   B CB  1 
ATOM   1223 C  CG  . GLN   A 1 160 ? 1.362   4.460   -0.958  1.00 35.12 ? 160 GLN   B CG  1 
ATOM   1224 C  CD  . GLN   A 1 160 ? 1.984   4.295   0.409   1.00 42.60 ? 160 GLN   B CD  1 
ATOM   1225 O  OE1 . GLN   A 1 160 ? 2.359   5.275   1.058   1.00 46.17 ? 160 GLN   B OE1 1 
ATOM   1226 N  NE2 . GLN   A 1 160 ? 2.110   3.050   0.856   1.00 38.90 ? 160 GLN   B NE2 1 
ATOM   1227 N  N   . LYS   A 1 161 ? 2.838   4.063   -4.609  1.00 25.77 ? 161 LYS   B N   1 
ATOM   1228 C  CA  . LYS   A 1 161 ? 2.462   3.037   -5.570  1.00 24.49 ? 161 LYS   B CA  1 
ATOM   1229 C  C   . LYS   A 1 161 ? 3.596   2.020   -5.714  1.00 23.64 ? 161 LYS   B C   1 
ATOM   1230 O  O   . LYS   A 1 161 ? 3.354   0.810   -5.765  1.00 21.43 ? 161 LYS   B O   1 
ATOM   1231 C  CB  . LYS   A 1 161 ? 2.070   3.653   -6.917  1.00 26.53 ? 161 LYS   B CB  1 
ATOM   1232 C  CG  . LYS   A 1 161 ? 1.361   2.695   -7.868  1.00 30.19 ? 161 LYS   B CG  1 
ATOM   1233 C  CD  . LYS   A 1 161 ? 1.174   3.221   -9.279  1.00 30.24 ? 161 LYS   B CD  1 
ATOM   1234 C  CE  . LYS   A 1 161 ? 0.768   2.128   -10.245 1.00 34.56 ? 161 LYS   B CE  1 
ATOM   1235 N  NZ  . LYS   A 1 161 ? -0.493  1.442   -9.849  1.00 30.59 ? 161 LYS   B NZ  1 
ATOM   1236 N  N   . ILE   A 1 162 ? 4.830   2.516   -5.757  1.00 20.08 ? 162 ILE   B N   1 
ATOM   1237 C  CA  . ILE   A 1 162 ? 5.993   1.663   -5.917  1.00 21.13 ? 162 ILE   B CA  1 
ATOM   1238 C  C   . ILE   A 1 162 ? 6.229   0.889   -4.629  1.00 22.52 ? 162 ILE   B C   1 
ATOM   1239 O  O   . ILE   A 1 162 ? 6.420   -0.333  -4.654  1.00 21.26 ? 162 ILE   B O   1 
ATOM   1240 C  CB  . ILE   A 1 162 ? 7.240   2.467   -6.345  1.00 20.38 ? 162 ILE   B CB  1 
ATOM   1241 C  CG1 . ILE   A 1 162 ? 7.051   3.080   -7.738  1.00 22.61 ? 162 ILE   B CG1 1 
ATOM   1242 C  CG2 . ILE   A 1 162 ? 8.503   1.588   -6.277  1.00 22.27 ? 162 ILE   B CG2 1 
ATOM   1243 C  CD1 . ILE   A 1 162 ? 8.171   4.023   -8.207  1.00 20.14 ? 162 ILE   B CD1 1 
ATOM   1244 N  N   . THR   A 1 163 ? 6.268   1.606   -3.502  1.00 21.79 ? 163 THR   B N   1 
ATOM   1245 C  CA  . THR   A 1 163 ? 6.648   0.925   -2.268  1.00 21.34 ? 163 THR   B CA  1 
ATOM   1246 C  C   . THR   A 1 163 ? 5.674   -0.210  -1.929  1.00 22.04 ? 163 THR   B C   1 
ATOM   1247 O  O   . THR   A 1 163 ? 6.101   -1.255  -1.423  1.00 21.27 ? 163 THR   B O   1 
ATOM   1248 C  CB  . THR   A 1 163 ? 6.919   1.899   -1.110  1.00 21.47 ? 163 THR   B CB  1 
ATOM   1249 O  OG1 . THR   A 1 163 ? 5.725   2.560   -0.707  1.00 24.31 ? 163 THR   B OG1 1 
ATOM   1250 C  CG2 . THR   A 1 163 ? 7.971   2.945   -1.413  1.00 20.28 ? 163 THR   B CG2 1 
ATOM   1251 N  N   . ASP   A 1 164 ? 4.376   -0.009  -2.184  1.00 22.69 ? 164 ASP   B N   1 
ATOM   1252 C  CA  . ASP   A 1 164 ? 3.360   -1.035  -1.940  1.00 26.92 ? 164 ASP   B CA  1 
ATOM   1253 C  C   . ASP   A 1 164 ? 3.641   -2.332  -2.708  1.00 27.45 ? 164 ASP   B C   1 
ATOM   1254 O  O   . ASP   A 1 164 ? 3.130   -3.384  -2.316  1.00 26.43 ? 164 ASP   B O   1 
ATOM   1255 C  CB  . ASP   A 1 164 ? 1.945   -0.549  -2.281  1.00 30.06 ? 164 ASP   B CB  1 
ATOM   1256 C  CG  . ASP   A 1 164 ? 1.360   0.442   -1.281  1.00 36.04 ? 164 ASP   B CG  1 
ATOM   1257 O  OD1 . ASP   A 1 164 ? 1.924   0.549   -0.176  1.00 36.41 ? 164 ASP   B OD1 1 
ATOM   1258 O  OD2 . ASP   A 1 164 ? 0.336   1.110   -1.618  1.00 40.74 ? 164 ASP   B OD2 1 
ATOM   1259 N  N   . THR   A 1 165 ? 4.451   -2.286  -3.783  1.00 25.18 ? 165 THR   B N   1 
ATOM   1260 C  CA  . THR   A 1 165 ? 4.648   -3.496  -4.579  1.00 24.87 ? 165 THR   B CA  1 
ATOM   1261 C  C   . THR   A 1 165 ? 5.868   -4.295  -4.127  1.00 23.75 ? 165 THR   B C   1 
ATOM   1262 O  O   . THR   A 1 165 ? 6.078   -5.424  -4.582  1.00 22.62 ? 165 THR   B O   1 
ATOM   1263 C  CB  . THR   A 1 165 ? 4.826   -3.243  -6.082  1.00 26.08 ? 165 THR   B CB  1 
ATOM   1264 O  OG1 . THR   A 1 165 ? 6.096   -2.618  -6.277  1.00 26.61 ? 165 THR   B OG1 1 
ATOM   1265 C  CG2 . THR   A 1 165 ? 3.693   -2.450  -6.706  1.00 29.91 ? 165 THR   B CG2 1 
ATOM   1266 N  N   . LEU   A 1 166 ? 6.684   -3.728  -3.242  1.00 20.63 ? 166 LEU   B N   1 
ATOM   1267 C  CA  . LEU   A 1 166 ? 8.027   -4.257  -3.077  1.00 24.22 ? 166 LEU   B CA  1 
ATOM   1268 C  C   . LEU   A 1 166 ? 8.029   -5.631  -2.390  1.00 24.86 ? 166 LEU   B C   1 
ATOM   1269 O  O   . LEU   A 1 166 ? 8.945   -6.407  -2.583  1.00 24.38 ? 166 LEU   B O   1 
ATOM   1270 C  CB  . LEU   A 1 166 ? 8.897   -3.252  -2.316  1.00 24.73 ? 166 LEU   B CB  1 
ATOM   1271 C  CG  . LEU   A 1 166 ? 9.181   -1.907  -3.006  1.00 26.26 ? 166 LEU   B CG  1 
ATOM   1272 C  CD1 . LEU   A 1 166 ? 9.998   -1.021  -2.066  1.00 24.59 ? 166 LEU   B CD1 1 
ATOM   1273 C  CD2 . LEU   A 1 166 ? 9.917   -2.072  -4.334  1.00 27.48 ? 166 LEU   B CD2 1 
ATOM   1274 N  N   . ASP   A 1 167 ? 7.029   -5.924  -1.561  1.00 31.19 ? 167 ASP   B N   1 
ATOM   1275 C  CA  . ASP   A 1 167 ? 6.948   -7.230  -0.920  1.00 35.46 ? 167 ASP   B CA  1 
ATOM   1276 C  C   . ASP   A 1 167 ? 6.769   -8.310  -1.989  1.00 32.87 ? 167 ASP   B C   1 
ATOM   1277 O  O   . ASP   A 1 167 ? 7.489   -9.305  -2.015  1.00 35.41 ? 167 ASP   B O   1 
ATOM   1278 C  CB  . ASP   A 1 167 ? 5.835   -7.283  0.131   1.00 42.37 ? 167 ASP   B CB  1 
ATOM   1279 C  CG  . ASP   A 1 167 ? 6.206   -6.641  1.456   1.00 48.52 ? 167 ASP   B CG  1 
ATOM   1280 O  OD1 . ASP   A 1 167 ? 7.410   -6.520  1.741   1.00 51.23 ? 167 ASP   B OD1 1 
ATOM   1281 O  OD2 . ASP   A 1 167 ? 5.281   -6.277  2.200   1.00 55.76 ? 167 ASP   B OD2 1 
ATOM   1282 N  N   . SER   A 1 168 ? 5.853   -8.069  -2.919  1.00 30.79 ? 168 SER   B N   1 
ATOM   1283 C  CA  . SER   A 1 168 ? 5.544   -9.027  -3.970  1.00 30.66 ? 168 SER   B CA  1 
ATOM   1284 C  C   . SER   A 1 168 ? 6.744   -9.308  -4.889  1.00 29.59 ? 168 SER   B C   1 
ATOM   1285 O  O   . SER   A 1 168 ? 6.710   -10.252 -5.666  1.00 27.08 ? 168 SER   B O   1 
ATOM   1286 C  CB  . SER   A 1 168 ? 4.332   -8.567  -4.750  1.00 30.76 ? 168 SER   B CB  1 
ATOM   1287 O  OG  . SER   A 1 168 ? 4.700   -7.559  -5.683  1.00 31.99 ? 168 SER   B OG  1 
ATOM   1288 N  N   . ILE   A 1 169 ? 7.817   -8.503  -4.832  1.00 26.61 ? 169 ILE   B N   1 
ATOM   1289 C  CA  . ILE   A 1 169 ? 8.940   -8.721  -5.732  1.00 23.61 ? 169 ILE   B CA  1 
ATOM   1290 C  C   . ILE   A 1 169 ? 10.248  -8.841  -4.940  1.00 23.22 ? 169 ILE   B C   1 
ATOM   1291 O  O   . ILE   A 1 169 ? 11.277  -8.371  -5.405  1.00 20.19 ? 169 ILE   B O   1 
ATOM   1292 C  CB  . ILE   A 1 169 ? 9.081   -7.596  -6.807  1.00 26.85 ? 169 ILE   B CB  1 
ATOM   1293 C  CG1 . ILE   A 1 169 ? 9.361   -6.218  -6.193  1.00 22.20 ? 169 ILE   B CG1 1 
ATOM   1294 C  CG2 . ILE   A 1 169 ? 7.918   -7.564  -7.796  1.00 27.97 ? 169 ILE   B CG2 1 
ATOM   1295 C  CD1 . ILE   A 1 169 ? 9.869   -5.154  -7.200  1.00 25.94 ? 169 ILE   B CD1 1 
ATOM   1296 N  N   A LYS   A 1 170 ? 10.192  -9.464  -3.752  0.50 25.60 ? 170 LYS   B N   1 
ATOM   1297 N  N   B LYS   A 1 170 ? 10.219  -9.467  -3.757  0.50 25.55 ? 170 LYS   B N   1 
ATOM   1298 C  CA  A LYS   A 1 170 ? 11.342  -9.562  -2.861  0.50 26.64 ? 170 LYS   B CA  1 
ATOM   1299 C  CA  B LYS   A 1 170 ? 11.423  -9.448  -2.940  0.50 26.61 ? 170 LYS   B CA  1 
ATOM   1300 C  C   A LYS   A 1 170 ? 12.504  -10.221 -3.600  0.50 25.58 ? 170 LYS   B C   1 
ATOM   1301 C  C   B LYS   A 1 170 ? 12.550  -10.219 -3.624  0.50 25.54 ? 170 LYS   B C   1 
ATOM   1302 O  O   A LYS   A 1 170 ? 13.615  -9.701  -3.608  0.50 24.17 ? 170 LYS   B O   1 
ATOM   1303 O  O   B LYS   A 1 170 ? 13.688  -9.762  -3.628  0.50 24.28 ? 170 LYS   B O   1 
ATOM   1304 C  CB  A LYS   A 1 170 ? 10.982  -10.346 -1.591  0.50 27.44 ? 170 LYS   B CB  1 
ATOM   1305 C  CB  B LYS   A 1 170 ? 11.176  -9.810  -1.472  0.50 27.19 ? 170 LYS   B CB  1 
ATOM   1306 C  CG  A LYS   A 1 170 ? 11.668  -9.904  -0.301  0.50 30.56 ? 170 LYS   B CG  1 
ATOM   1307 C  CG  B LYS   A 1 170 ? 12.208  -9.226  -0.513  0.50 30.02 ? 170 LYS   B CG  1 
ATOM   1308 C  CD  A LYS   A 1 170 ? 10.896  -8.830  0.476   0.50 30.57 ? 170 LYS   B CD  1 
ATOM   1309 C  CD  B LYS   A 1 170 ? 11.623  -8.563  0.736   0.50 30.26 ? 170 LYS   B CD  1 
ATOM   1310 C  CE  A LYS   A 1 170 ? 11.237  -8.744  1.955   0.50 29.95 ? 170 LYS   B CE  1 
ATOM   1311 C  CE  B LYS   A 1 170 ? 10.520  -7.551  0.481   0.50 28.94 ? 170 LYS   B CE  1 
ATOM   1312 N  NZ  A LYS   A 1 170 ? 12.695  -8.851  2.226   0.50 25.74 ? 170 LYS   B NZ  1 
ATOM   1313 N  NZ  B LYS   A 1 170 ? 10.908  -6.521  -0.511  0.50 23.16 ? 170 LYS   B NZ  1 
ATOM   1314 N  N   . GLU   A 1 171 ? 12.221  -11.363 -4.232  1.00 26.15 ? 171 GLU   B N   1 
ATOM   1315 C  CA  . GLU   A 1 171 ? 13.243  -12.191 -4.853  1.00 30.51 ? 171 GLU   B CA  1 
ATOM   1316 C  C   . GLU   A 1 171 ? 13.569  -11.693 -6.260  1.00 29.37 ? 171 GLU   B C   1 
ATOM   1317 O  O   . GLU   A 1 171 ? 12.678  -11.247 -7.006  1.00 26.64 ? 171 GLU   B O   1 
ATOM   1318 C  CB  . GLU   A 1 171 ? 12.789  -13.657 -4.884  1.00 37.40 ? 171 GLU   B CB  1 
ATOM   1319 C  CG  . GLU   A 1 171 ? 12.384  -14.214 -3.517  1.00 43.42 ? 171 GLU   B CG  1 
ATOM   1320 C  CD  . GLU   A 1 171 ? 11.051  -13.748 -2.934  1.00 54.78 ? 171 GLU   B CD  1 
ATOM   1321 O  OE1 . GLU   A 1 171 ? 10.903  -13.820 -1.669  1.00 56.39 ? 171 GLU   B OE1 1 
ATOM   1322 O  OE2 . GLU   A 1 171 ? 10.156  -13.299 -3.727  1.00 47.34 ? 171 GLU   B OE2 1 
ATOM   1323 N  N   . LYS   A 1 172 ? 14.853  -11.836 -6.626  1.00 26.64 ? 172 LYS   B N   1 
ATOM   1324 C  CA  . LYS   A 1 172 ? 15.341  -11.479 -7.950  1.00 26.47 ? 172 LYS   B CA  1 
ATOM   1325 C  C   . LYS   A 1 172 ? 14.568  -12.267 -9.000  1.00 27.05 ? 172 LYS   B C   1 
ATOM   1326 O  O   . LYS   A 1 172 ? 14.386  -13.471 -8.836  1.00 23.32 ? 172 LYS   B O   1 
ATOM   1327 C  CB  . LYS   A 1 172 ? 16.836  -11.790 -8.085  1.00 26.78 ? 172 LYS   B CB  1 
ATOM   1328 C  CG  . LYS   A 1 172 ? 17.338  -11.908 -9.519  1.00 26.36 ? 172 LYS   B CG  1 
ATOM   1329 C  CD  . LYS   A 1 172 ? 18.847  -12.002 -9.639  1.00 28.76 ? 172 LYS   B CD  1 
ATOM   1330 C  CE  . LYS   A 1 172 ? 19.337  -11.922 -11.065 1.00 32.92 ? 172 LYS   B CE  1 
ATOM   1331 N  NZ  . LYS   A 1 172 ? 20.762  -12.323 -11.125 1.00 40.89 ? 172 LYS   B NZ  1 
ATOM   1332 N  N   . GLY   A 1 173 ? 14.089  -11.571 -10.047 1.00 25.73 ? 173 GLY   B N   1 
ATOM   1333 C  CA  . GLY   A 1 173 ? 13.279  -12.211 -11.074 1.00 27.60 ? 173 GLY   B CA  1 
ATOM   1334 C  C   . GLY   A 1 173 ? 11.773  -12.029 -10.912 1.00 27.41 ? 173 GLY   B C   1 
ATOM   1335 O  O   . GLY   A 1 173 ? 11.048  -12.123 -11.899 1.00 35.61 ? 173 GLY   B O   1 
ATOM   1336 N  N   . LYS   A 1 174 ? 11.286  -11.790 -9.689  1.00 26.64 ? 174 LYS   B N   1 
ATOM   1337 C  CA  . LYS   A 1 174 ? 9.851   -11.639 -9.491  1.00 26.27 ? 174 LYS   B CA  1 
ATOM   1338 C  C   . LYS   A 1 174 ? 9.380   -10.390 -10.238 1.00 25.21 ? 174 LYS   B C   1 
ATOM   1339 O  O   . LYS   A 1 174 ? 10.133  -9.408  -10.350 1.00 22.49 ? 174 LYS   B O   1 
ATOM   1340 C  CB  . LYS   A 1 174 ? 9.482   -11.530 -8.009  1.00 27.75 ? 174 LYS   B CB  1 
ATOM   1341 C  CG  . LYS   A 1 174 ? 9.636   -12.799 -7.172  1.00 34.49 ? 174 LYS   B CG  1 
ATOM   1342 C  CD  . LYS   A 1 174 ? 8.615   -13.880 -7.477  1.00 37.44 ? 174 LYS   B CD  1 
ATOM   1343 N  N   . GLN   A 1 175 ? 8.155   -10.471 -10.760 1.00 23.31 ? 175 GLN   B N   1 
ATOM   1344 C  CA  . GLN   A 1 175 ? 7.524   -9.379  -11.481 1.00 27.92 ? 175 GLN   B CA  1 
ATOM   1345 C  C   . GLN   A 1 175 ? 6.024   -9.381  -11.210 1.00 30.60 ? 175 GLN   B C   1 
ATOM   1346 O  O   . GLN   A 1 175 ? 5.446   -10.423 -10.893 1.00 28.06 ? 175 GLN   B O   1 
ATOM   1347 C  CB  . GLN   A 1 175 ? 7.952   -9.336  -12.952 1.00 33.43 ? 175 GLN   B CB  1 
ATOM   1348 C  CG  . GLN   A 1 175 ? 7.364   -10.412 -13.845 1.00 41.19 ? 175 GLN   B CG  1 
ATOM   1349 C  CD  . GLN   A 1 175 ? 7.954   -10.314 -15.234 1.00 47.56 ? 175 GLN   B CD  1 
ATOM   1350 O  OE1 . GLN   A 1 175 ? 7.308   -10.635 -16.228 1.00 56.06 ? 175 GLN   B OE1 1 
ATOM   1351 N  NE2 . GLN   A 1 175 ? 9.191   -9.842  -15.321 1.00 51.02 ? 175 GLN   B NE2 1 
ATOM   1352 N  N   . THR   A 1 176 ? 5.431   -8.185  -11.288 1.00 26.24 ? 176 THR   B N   1 
ATOM   1353 C  CA  . THR   A 1 176 ? 4.044   -7.934  -10.942 1.00 28.71 ? 176 THR   B CA  1 
ATOM   1354 C  C   . THR   A 1 176 ? 3.494   -6.896  -11.915 1.00 24.26 ? 176 THR   B C   1 
ATOM   1355 O  O   . THR   A 1 176 ? 4.212   -5.981  -12.353 1.00 19.47 ? 176 THR   B O   1 
ATOM   1356 C  CB  . THR   A 1 176 ? 3.903   -7.409  -9.505  1.00 29.73 ? 176 THR   B CB  1 
ATOM   1357 O  OG1 . THR   A 1 176 ? 4.404   -8.437  -8.651  1.00 39.74 ? 176 THR   B OG1 1 
ATOM   1358 C  CG2 . THR   A 1 176 ? 2.473   -7.098  -9.120  1.00 31.88 ? 176 THR   B CG2 1 
ATOM   1359 N  N   . ARG   A 1 177 ? 2.230   -7.076  -12.294 1.00 21.52 ? 177 ARG   B N   1 
ATOM   1360 C  CA  . ARG   A 1 177 ? 1.664   -6.073  -13.197 1.00 23.31 ? 177 ARG   B CA  1 
ATOM   1361 C  C   . ARG   A 1 177 ? 1.556   -4.737  -12.463 1.00 21.48 ? 177 ARG   B C   1 
ATOM   1362 O  O   . ARG   A 1 177 ? 1.305   -4.710  -11.263 1.00 19.93 ? 177 ARG   B O   1 
ATOM   1363 C  CB  . ARG   A 1 177 ? 0.363   -6.576  -13.819 1.00 23.84 ? 177 ARG   B CB  1 
ATOM   1364 C  CG  . ARG   A 1 177 ? 0.639   -7.708  -14.807 1.00 23.47 ? 177 ARG   B CG  1 
ATOM   1365 C  CD  . ARG   A 1 177 ? -0.681  -8.238  -15.292 1.00 25.04 ? 177 ARG   B CD  1 
ATOM   1366 N  NE  . ARG   A 1 177 ? -1.210  -7.248  -16.220 1.00 26.46 ? 177 ARG   B NE  1 
ATOM   1367 C  CZ  . ARG   A 1 177 ? -2.313  -7.393  -16.939 1.00 28.13 ? 177 ARG   B CZ  1 
ATOM   1368 N  NH1 . ARG   A 1 177 ? -3.003  -8.525  -16.849 1.00 22.10 ? 177 ARG   B NH1 1 
ATOM   1369 N  NH2 . ARG   A 1 177 ? -2.689  -6.415  -17.756 1.00 27.14 ? 177 ARG   B NH2 1 
ATOM   1370 N  N   . PHE   A 1 178 ? 1.757   -3.630  -13.195 1.00 22.38 ? 178 PHE   B N   1 
ATOM   1371 C  CA  . PHE   A 1 178 ? 1.928   -2.324  -12.585 1.00 21.36 ? 178 PHE   B CA  1 
ATOM   1372 C  C   . PHE   A 1 178 ? 1.560   -1.294  -13.640 1.00 20.62 ? 178 PHE   B C   1 
ATOM   1373 O  O   . PHE   A 1 178 ? 2.347   -1.072  -14.550 1.00 21.93 ? 178 PHE   B O   1 
ATOM   1374 C  CB  . PHE   A 1 178 ? 3.407   -2.096  -12.233 1.00 21.65 ? 178 PHE   B CB  1 
ATOM   1375 C  CG  . PHE   A 1 178 ? 3.732   -0.847  -11.434 1.00 21.50 ? 178 PHE   B CG  1 
ATOM   1376 C  CD1 . PHE   A 1 178 ? 3.633   -0.835  -10.049 1.00 23.17 ? 178 PHE   B CD1 1 
ATOM   1377 C  CD2 . PHE   A 1 178 ? 4.198   0.304   -12.056 1.00 23.00 ? 178 PHE   B CD2 1 
ATOM   1378 C  CE1 . PHE   A 1 178 ? 3.960   0.298   -9.310  1.00 23.42 ? 178 PHE   B CE1 1 
ATOM   1379 C  CE2 . PHE   A 1 178 ? 4.508   1.444   -11.326 1.00 22.45 ? 178 PHE   B CE2 1 
ATOM   1380 C  CZ  . PHE   A 1 178 ? 4.414   1.437   -9.950  1.00 22.60 ? 178 PHE   B CZ  1 
ATOM   1381 N  N   . THR   A 1 179 ? 0.359   -0.708  -13.534 1.00 22.95 ? 179 THR   B N   1 
ATOM   1382 C  CA  . THR   A 1 179 ? -0.074  0.225   -14.569 1.00 25.65 ? 179 THR   B CA  1 
ATOM   1383 C  C   . THR   A 1 179 ? -0.764  1.428   -13.935 1.00 25.55 ? 179 THR   B C   1 
ATOM   1384 O  O   . THR   A 1 179 ? -0.887  1.506   -12.715 1.00 26.35 ? 179 THR   B O   1 
ATOM   1385 C  CB  . THR   A 1 179 ? -0.914  -0.451  -15.666 1.00 31.77 ? 179 THR   B CB  1 
ATOM   1386 O  OG1 . THR   A 1 179 ? -0.890  0.379   -16.839 1.00 39.75 ? 179 THR   B OG1 1 
ATOM   1387 C  CG2 . THR   A 1 179 ? -2.340  -0.698  -15.226 1.00 35.98 ? 179 THR   B CG2 1 
ATOM   1388 N  N   . ASN   A 1 180 ? -1.174  2.387   -14.770 1.00 25.31 ? 180 ASN   B N   1 
ATOM   1389 C  CA  . ASN   A 1 180 ? -1.717  3.642   -14.261 1.00 25.64 ? 180 ASN   B CA  1 
ATOM   1390 C  C   . ASN   A 1 180 ? -0.692  4.310   -13.342 1.00 24.86 ? 180 ASN   B C   1 
ATOM   1391 O  O   . ASN   A 1 180 ? -1.009  4.670   -12.206 1.00 26.72 ? 180 ASN   B O   1 
ATOM   1392 C  CB  . ASN   A 1 180 ? -3.052  3.474   -13.525 1.00 29.17 ? 180 ASN   B CB  1 
ATOM   1393 C  CG  . ASN   A 1 180 ? -3.775  4.800   -13.384 1.00 34.59 ? 180 ASN   B CG  1 
ATOM   1394 O  OD1 . ASN   A 1 180 ? -3.546  5.711   -14.176 1.00 34.07 ? 180 ASN   B OD1 1 
ATOM   1395 N  ND2 . ASN   A 1 180 ? -4.615  4.936   -12.363 1.00 37.90 ? 180 ASN   B ND2 1 
ATOM   1396 N  N   . PHE   A 1 181 ? 0.521   4.515   -13.868 1.00 22.51 ? 181 PHE   B N   1 
ATOM   1397 C  CA  . PHE   A 1 181 ? 1.612   5.087   -13.100 1.00 22.27 ? 181 PHE   B CA  1 
ATOM   1398 C  C   . PHE   A 1 181 ? 1.942   6.472   -13.632 1.00 22.25 ? 181 PHE   B C   1 
ATOM   1399 O  O   . PHE   A 1 181 ? 2.520   6.598   -14.706 1.00 24.70 ? 181 PHE   B O   1 
ATOM   1400 C  CB  . PHE   A 1 181 ? 2.852   4.193   -13.203 1.00 21.90 ? 181 PHE   B CB  1 
ATOM   1401 C  CG  . PHE   A 1 181 ? 4.122   4.760   -12.608 1.00 21.79 ? 181 PHE   B CG  1 
ATOM   1402 C  CD1 . PHE   A 1 181 ? 4.120   5.373   -11.368 1.00 22.81 ? 181 PHE   B CD1 1 
ATOM   1403 C  CD2 . PHE   A 1 181 ? 5.334   4.637   -13.280 1.00 23.13 ? 181 PHE   B CD2 1 
ATOM   1404 C  CE1 . PHE   A 1 181 ? 5.290   5.880   -10.810 1.00 21.32 ? 181 PHE   B CE1 1 
ATOM   1405 C  CE2 . PHE   A 1 181 ? 6.511   5.117   -12.713 1.00 23.25 ? 181 PHE   B CE2 1 
ATOM   1406 C  CZ  . PHE   A 1 181 ? 6.483   5.741   -11.477 1.00 23.20 ? 181 PHE   B CZ  1 
ATOM   1407 N  N   . ASP   A 1 182 ? 1.594   7.502   -12.854 1.00 23.25 ? 182 ASP   B N   1 
ATOM   1408 C  CA  . ASP   A 1 182 ? 1.788   8.877   -13.285 1.00 24.12 ? 182 ASP   B CA  1 
ATOM   1409 C  C   . ASP   A 1 182 ? 3.207   9.336   -12.940 1.00 22.77 ? 182 ASP   B C   1 
ATOM   1410 O  O   . ASP   A 1 182 ? 3.419   10.013  -11.938 1.00 24.73 ? 182 ASP   B O   1 
ATOM   1411 C  CB  . ASP   A 1 182 ? 0.667   9.754   -12.722 1.00 25.98 ? 182 ASP   B CB  1 
ATOM   1412 C  CG  . ASP   A 1 182 ? 0.730   11.228  -13.132 1.00 33.47 ? 182 ASP   B CG  1 
ATOM   1413 O  OD1 . ASP   A 1 182 ? 1.312   11.523  -14.186 1.00 35.87 ? 182 ASP   B OD1 1 
ATOM   1414 O  OD2 . ASP   A 1 182 ? 0.156   12.072  -12.393 1.00 31.78 ? 182 ASP   B OD2 1 
ATOM   1415 N  N   . LEU   A 1 183 ? 4.181   8.942   -13.777 1.00 19.46 ? 183 LEU   B N   1 
ATOM   1416 C  CA  . LEU   A 1 183 ? 5.593   9.289   -13.619 1.00 20.00 ? 183 LEU   B CA  1 
ATOM   1417 C  C   . LEU   A 1 183 ? 5.790   10.804  -13.676 1.00 20.20 ? 183 LEU   B C   1 
ATOM   1418 O  O   . LEU   A 1 183 ? 6.697   11.318  -13.049 1.00 20.84 ? 183 LEU   B O   1 
ATOM   1419 C  CB  . LEU   A 1 183 ? 6.384   8.635   -14.757 1.00 20.22 ? 183 LEU   B CB  1 
ATOM   1420 C  CG  . LEU   A 1 183 ? 7.890   8.915   -14.806 1.00 19.62 ? 183 LEU   B CG  1 
ATOM   1421 C  CD1 . LEU   A 1 183 ? 8.598   8.505   -13.512 1.00 17.65 ? 183 LEU   B CD1 1 
ATOM   1422 C  CD2 . LEU   A 1 183 ? 8.521   8.206   -15.994 1.00 19.76 ? 183 LEU   B CD2 1 
ATOM   1423 N  N   . LEU   A 1 184 ? 4.965   11.524  -14.448 1.00 19.49 ? 184 LEU   B N   1 
ATOM   1424 C  CA  . LEU   A 1 184 ? 5.115   12.977  -14.533 1.00 21.05 ? 184 LEU   B CA  1 
ATOM   1425 C  C   . LEU   A 1 184 ? 5.016   13.601  -13.139 1.00 18.57 ? 184 LEU   B C   1 
ATOM   1426 O  O   . LEU   A 1 184 ? 5.770   14.520  -12.810 1.00 19.02 ? 184 LEU   B O   1 
ATOM   1427 C  CB  . LEU   A 1 184 ? 4.067   13.560  -15.508 1.00 21.70 ? 184 LEU   B CB  1 
ATOM   1428 C  CG  . LEU   A 1 184 ? 4.068   15.087  -15.614 1.00 26.28 ? 184 LEU   B CG  1 
ATOM   1429 C  CD1 . LEU   A 1 184 ? 5.298   15.582  -16.365 1.00 24.45 ? 184 LEU   B CD1 1 
ATOM   1430 C  CD2 . LEU   A 1 184 ? 2.784   15.612  -16.268 1.00 25.54 ? 184 LEU   B CD2 1 
ATOM   1431 N  N   . SER   A 1 185 ? 4.076   13.116  -12.314 1.00 19.09 ? 185 SER   B N   1 
ATOM   1432 C  CA  . SER   A 1 185 ? 3.797   13.716  -11.020 1.00 21.17 ? 185 SER   B CA  1 
ATOM   1433 C  C   . SER   A 1 185 ? 4.914   13.449  -10.007 1.00 21.85 ? 185 SER   B C   1 
ATOM   1434 O  O   . SER   A 1 185 ? 4.977   14.105  -8.980  1.00 23.16 ? 185 SER   B O   1 
ATOM   1435 C  CB  . SER   A 1 185 ? 2.463   13.263  -10.475 1.00 23.60 ? 185 SER   B CB  1 
ATOM   1436 O  OG  . SER   A 1 185 ? 1.417   13.773  -11.291 1.00 27.72 ? 185 SER   B OG  1 
ATOM   1437 N  N   . LEU   A 1 186 ? 5.772   12.465  -10.279 1.00 21.66 ? 186 LEU   B N   1 
ATOM   1438 C  CA  . LEU   A 1 186 ? 6.938   12.163  -9.457  1.00 22.23 ? 186 LEU   B CA  1 
ATOM   1439 C  C   . LEU   A 1 186 ? 8.072   13.153  -9.681  1.00 23.49 ? 186 LEU   B C   1 
ATOM   1440 O  O   . LEU   A 1 186 ? 8.874   13.345  -8.761  1.00 26.16 ? 186 LEU   B O   1 
ATOM   1441 C  CB  . LEU   A 1 186 ? 7.419   10.760  -9.806  1.00 23.57 ? 186 LEU   B CB  1 
ATOM   1442 C  CG  . LEU   A 1 186 ? 8.411   10.096  -8.861  1.00 27.93 ? 186 LEU   B CG  1 
ATOM   1443 C  CD1 . LEU   A 1 186 ? 8.093   10.366  -7.377  1.00 27.61 ? 186 LEU   B CD1 1 
ATOM   1444 C  CD2 . LEU   A 1 186 ? 8.424   8.600   -9.149  1.00 27.33 ? 186 LEU   B CD2 1 
ATOM   1445 N  N   . LEU   A 1 187 ? 8.176   13.752  -10.885 1.00 22.39 ? 187 LEU   B N   1 
ATOM   1446 C  CA  . LEU   A 1 187 ? 9.268   14.682  -11.167 1.00 21.83 ? 187 LEU   B CA  1 
ATOM   1447 C  C   . LEU   A 1 187 ? 9.143   15.949  -10.322 1.00 21.39 ? 187 LEU   B C   1 
ATOM   1448 O  O   . LEU   A 1 187 ? 8.047   16.341  -9.926  1.00 23.52 ? 187 LEU   B O   1 
ATOM   1449 C  CB  . LEU   A 1 187 ? 9.289   15.098  -12.642 1.00 25.55 ? 187 LEU   B CB  1 
ATOM   1450 C  CG  . LEU   A 1 187 ? 9.381   13.977  -13.667 1.00 28.50 ? 187 LEU   B CG  1 
ATOM   1451 C  CD1 . LEU   A 1 187 ? 9.197   14.548  -15.073 1.00 31.68 ? 187 LEU   B CD1 1 
ATOM   1452 C  CD2 . LEU   A 1 187 ? 10.704  13.235  -13.538 1.00 27.86 ? 187 LEU   B CD2 1 
ATOM   1453 N  N   . PRO   A 1 188 ? 10.251  16.681  -10.082 1.00 21.41 ? 188 PRO   B N   1 
ATOM   1454 C  CA  . PRO   A 1 188 ? 10.182  17.957  -9.364  1.00 23.70 ? 188 PRO   B CA  1 
ATOM   1455 C  C   . PRO   A 1 188 ? 9.439   19.011  -10.187 1.00 26.30 ? 188 PRO   B C   1 
ATOM   1456 O  O   . PRO   A 1 188 ? 9.290   18.860  -11.396 1.00 27.03 ? 188 PRO   B O   1 
ATOM   1457 C  CB  . PRO   A 1 188 ? 11.648  18.388  -9.200  1.00 21.84 ? 188 PRO   B CB  1 
ATOM   1458 C  CG  . PRO   A 1 188 ? 12.395  17.598  -10.266 1.00 21.86 ? 188 PRO   B CG  1 
ATOM   1459 C  CD  . PRO   A 1 188 ? 11.634  16.295  -10.436 1.00 22.73 ? 188 PRO   B CD  1 
ATOM   1460 N  N   . PRO   A 1 189 ? 8.955   20.118  -9.575  1.00 31.51 ? 189 PRO   B N   1 
ATOM   1461 C  CA  . PRO   A 1 189 ? 8.220   21.137  -10.328 1.00 29.97 ? 189 PRO   B CA  1 
ATOM   1462 C  C   . PRO   A 1 189 ? 9.086   21.904  -11.336 1.00 32.42 ? 189 PRO   B C   1 
ATOM   1463 O  O   . PRO   A 1 189 ? 8.553   22.408  -12.332 1.00 28.44 ? 189 PRO   B O   1 
ATOM   1464 C  CB  . PRO   A 1 189 ? 7.668   22.058  -9.214  1.00 31.23 ? 189 PRO   B CB  1 
ATOM   1465 C  CG  . PRO   A 1 189 ? 8.630   21.893  -8.085  1.00 29.16 ? 189 PRO   B CG  1 
ATOM   1466 C  CD  . PRO   A 1 189 ? 9.061   20.440  -8.142  1.00 29.18 ? 189 PRO   B CD  1 
ATOM   1467 N  N   . SER   A 1 190 ? 10.411  21.945  -11.089 1.00 26.72 ? 190 SER   B N   1 
ATOM   1468 C  CA  . SER   A 1 190 ? 11.377  22.672  -11.921 1.00 25.34 ? 190 SER   B CA  1 
ATOM   1469 C  C   . SER   A 1 190 ? 12.242  21.704  -12.731 1.00 21.27 ? 190 SER   B C   1 
ATOM   1470 O  O   . SER   A 1 190 ? 12.805  20.765  -12.173 1.00 20.19 ? 190 SER   B O   1 
ATOM   1471 C  CB  . SER   A 1 190 ? 12.218  23.625  -11.091 1.00 29.47 ? 190 SER   B CB  1 
ATOM   1472 O  OG  . SER   A 1 190 ? 13.399  24.000  -11.805 1.00 34.97 ? 190 SER   B OG  1 
ATOM   1473 N  N   . TRP   A 1 191 ? 12.343  21.946  -14.044 1.00 18.67 ? 191 TRP   B N   1 
ATOM   1474 C  CA  . TRP   A 1 191 ? 13.076  21.060  -14.934 1.00 20.00 ? 191 TRP   B CA  1 
ATOM   1475 C  C   . TRP   A 1 191 ? 14.418  21.649  -15.387 1.00 18.00 ? 191 TRP   B C   1 
ATOM   1476 O  O   . TRP   A 1 191 ? 14.955  21.251  -16.432 1.00 20.50 ? 191 TRP   B O   1 
ATOM   1477 C  CB  . TRP   A 1 191 ? 12.164  20.681  -16.107 1.00 21.08 ? 191 TRP   B CB  1 
ATOM   1478 C  CG  . TRP   A 1 191 ? 10.929  19.911  -15.715 1.00 23.74 ? 191 TRP   B CG  1 
ATOM   1479 C  CD1 . TRP   A 1 191 ? 10.641  19.330  -14.507 1.00 22.70 ? 191 TRP   B CD1 1 
ATOM   1480 C  CD2 . TRP   A 1 191 ? 9.825   19.583  -16.580 1.00 23.58 ? 191 TRP   B CD2 1 
ATOM   1481 N  NE1 . TRP   A 1 191 ? 9.441   18.662  -14.576 1.00 22.91 ? 191 TRP   B NE1 1 
ATOM   1482 C  CE2 . TRP   A 1 191 ? 8.917   18.803  -15.828 1.00 24.13 ? 191 TRP   B CE2 1 
ATOM   1483 C  CE3 . TRP   A 1 191 ? 9.536   19.835  -17.924 1.00 23.83 ? 191 TRP   B CE3 1 
ATOM   1484 C  CZ2 . TRP   A 1 191 ? 7.712   18.336  -16.368 1.00 28.19 ? 191 TRP   B CZ2 1 
ATOM   1485 C  CZ3 . TRP   A 1 191 ? 8.362   19.345  -18.467 1.00 25.90 ? 191 TRP   B CZ3 1 
ATOM   1486 C  CH2 . TRP   A 1 191 ? 7.455   18.617  -17.699 1.00 25.07 ? 191 TRP   B CH2 1 
ATOM   1487 N  N   . ASP   A 1 192 ? 15.020  22.538  -14.585 1.00 18.11 ? 192 ASP   B N   1 
ATOM   1488 C  CA  . ASP   A 1 192 ? 16.367  23.009  -14.886 1.00 18.49 ? 192 ASP   B CA  1 
ATOM   1489 C  C   . ASP   A 1 192 ? 17.351  21.840  -14.733 1.00 18.66 ? 192 ASP   B C   1 
ATOM   1490 O  O   . ASP   A 1 192 ? 17.174  21.024  -13.828 1.00 16.12 ? 192 ASP   B O   1 
ATOM   1491 C  CB  . ASP   A 1 192 ? 16.851  24.107  -13.934 1.00 21.76 ? 192 ASP   B CB  1 
ATOM   1492 C  CG  . ASP   A 1 192 ? 16.085  25.441  -13.947 1.00 33.69 ? 192 ASP   B CG  1 
ATOM   1493 O  OD1 . ASP   A 1 192 ? 15.296  25.723  -14.906 1.00 34.65 ? 192 ASP   B OD1 1 
ATOM   1494 O  OD2 . ASP   A 1 192 ? 16.306  26.228  -12.992 1.00 41.61 ? 192 ASP   B OD2 1 
ATOM   1495 N  N   . TYR   A 1 193 ? 18.386  21.782  -15.590 1.00 18.02 ? 193 TYR   B N   1 
ATOM   1496 C  CA  . TYR   A 1 193 ? 19.225  20.584  -15.601 1.00 17.20 ? 193 TYR   B CA  1 
ATOM   1497 C  C   . TYR   A 1 193 ? 20.682  20.885  -15.935 1.00 16.15 ? 193 TYR   B C   1 
ATOM   1498 O  O   . TYR   A 1 193 ? 21.013  21.966  -16.435 1.00 18.42 ? 193 TYR   B O   1 
ATOM   1499 C  CB  . TYR   A 1 193 ? 18.655  19.570  -16.608 1.00 15.55 ? 193 TYR   B CB  1 
ATOM   1500 C  CG  . TYR   A 1 193 ? 18.663  20.060  -18.036 1.00 16.14 ? 193 TYR   B CG  1 
ATOM   1501 C  CD1 . TYR   A 1 193 ? 19.770  19.875  -18.853 1.00 15.74 ? 193 TYR   B CD1 1 
ATOM   1502 C  CD2 . TYR   A 1 193 ? 17.607  20.834  -18.527 1.00 17.88 ? 193 TYR   B CD2 1 
ATOM   1503 C  CE1 . TYR   A 1 193 ? 19.775  20.349  -20.159 1.00 18.35 ? 193 TYR   B CE1 1 
ATOM   1504 C  CE2 . TYR   A 1 193 ? 17.607  21.326  -19.826 1.00 16.11 ? 193 TYR   B CE2 1 
ATOM   1505 C  CZ  . TYR   A 1 193 ? 18.707  21.102  -20.635 1.00 18.14 ? 193 TYR   B CZ  1 
ATOM   1506 O  OH  . TYR   A 1 193 ? 18.761  21.577  -21.912 1.00 18.35 ? 193 TYR   B OH  1 
ATOM   1507 N  N   . TRP   A 1 194 ? 21.526  19.858  -15.696 1.00 16.31 ? 194 TRP   B N   1 
ATOM   1508 C  CA  . TRP   A 1 194 ? 22.895  19.756  -16.165 1.00 17.04 ? 194 TRP   B CA  1 
ATOM   1509 C  C   . TRP   A 1 194 ? 22.937  18.611  -17.164 1.00 15.65 ? 194 TRP   B C   1 
ATOM   1510 O  O   . TRP   A 1 194 ? 22.185  17.639  -17.012 1.00 15.09 ? 194 TRP   B O   1 
ATOM   1511 C  CB  . TRP   A 1 194 ? 23.906  19.483  -15.025 1.00 17.97 ? 194 TRP   B CB  1 
ATOM   1512 C  CG  . TRP   A 1 194 ? 23.984  20.509  -13.939 1.00 18.83 ? 194 TRP   B CG  1 
ATOM   1513 C  CD1 . TRP   A 1 194 ? 24.557  21.748  -14.031 1.00 21.26 ? 194 TRP   B CD1 1 
ATOM   1514 C  CD2 . TRP   A 1 194 ? 23.514  20.381  -12.579 1.00 19.48 ? 194 TRP   B CD2 1 
ATOM   1515 N  NE1 . TRP   A 1 194 ? 24.462  22.408  -12.834 1.00 21.27 ? 194 TRP   B NE1 1 
ATOM   1516 C  CE2 . TRP   A 1 194 ? 23.818  21.600  -11.925 1.00 21.61 ? 194 TRP   B CE2 1 
ATOM   1517 C  CE3 . TRP   A 1 194 ? 22.860  19.368  -11.851 1.00 19.69 ? 194 TRP   B CE3 1 
ATOM   1518 C  CZ2 . TRP   A 1 194 ? 23.504  21.823  -10.574 1.00 20.98 ? 194 TRP   B CZ2 1 
ATOM   1519 C  CZ3 . TRP   A 1 194 ? 22.544  19.587  -10.525 1.00 22.00 ? 194 TRP   B CZ3 1 
ATOM   1520 C  CH2 . TRP   A 1 194 ? 22.880  20.798  -9.888  1.00 20.94 ? 194 TRP   B CH2 1 
ATOM   1521 N  N   . THR   A 1 195 ? 23.852  18.700  -18.131 1.00 14.81 ? 195 THR   B N   1 
ATOM   1522 C  CA  . THR   A 1 195 ? 23.974  17.647  -19.140 1.00 17.17 ? 195 THR   B CA  1 
ATOM   1523 C  C   . THR   A 1 195 ? 25.445  17.379  -19.475 1.00 16.94 ? 195 THR   B C   1 
ATOM   1524 O  O   . THR   A 1 195 ? 26.285  18.275  -19.414 1.00 17.79 ? 195 THR   B O   1 
ATOM   1525 C  CB  . THR   A 1 195 ? 23.114  17.975  -20.380 1.00 17.16 ? 195 THR   B CB  1 
ATOM   1526 O  OG1 . THR   A 1 195 ? 23.229  16.871  -21.277 1.00 18.69 ? 195 THR   B OG1 1 
ATOM   1527 C  CG2 . THR   A 1 195 ? 23.567  19.214  -21.133 1.00 17.66 ? 195 THR   B CG2 1 
ATOM   1528 N  N   . TYR   A 1 196 ? 25.744  16.133  -19.858 1.00 17.27 ? 196 TYR   B N   1 
ATOM   1529 C  CA  . TYR   A 1 196 ? 27.088  15.742  -20.268 1.00 16.22 ? 196 TYR   B CA  1 
ATOM   1530 C  C   . TYR   A 1 196 ? 26.974  14.389  -20.967 1.00 17.88 ? 196 TYR   B C   1 
ATOM   1531 O  O   . TYR   A 1 196 ? 26.036  13.625  -20.693 1.00 15.91 ? 196 TYR   B O   1 
ATOM   1532 C  CB  . TYR   A 1 196 ? 28.031  15.689  -19.051 1.00 16.74 ? 196 TYR   B CB  1 
ATOM   1533 C  CG  . TYR   A 1 196 ? 27.845  14.484  -18.160 1.00 16.96 ? 196 TYR   B CG  1 
ATOM   1534 C  CD1 . TYR   A 1 196 ? 26.864  14.449  -17.170 1.00 16.34 ? 196 TYR   B CD1 1 
ATOM   1535 C  CD2 . TYR   A 1 196 ? 28.640  13.364  -18.326 1.00 16.91 ? 196 TYR   B CD2 1 
ATOM   1536 C  CE1 . TYR   A 1 196 ? 26.675  13.317  -16.383 1.00 15.41 ? 196 TYR   B CE1 1 
ATOM   1537 C  CE2 . TYR   A 1 196 ? 28.472  12.237  -17.543 1.00 16.76 ? 196 TYR   B CE2 1 
ATOM   1538 C  CZ  . TYR   A 1 196 ? 27.499  12.215  -16.561 1.00 16.33 ? 196 TYR   B CZ  1 
ATOM   1539 O  OH  . TYR   A 1 196 ? 27.341  11.078  -15.815 1.00 16.47 ? 196 TYR   B OH  1 
ATOM   1540 N  N   . PRO   A 1 197 ? 27.917  14.044  -21.875 1.00 16.58 ? 197 PRO   B N   1 
ATOM   1541 C  CA  . PRO   A 1 197 ? 27.907  12.732  -22.526 1.00 17.98 ? 197 PRO   B CA  1 
ATOM   1542 C  C   . PRO   A 1 197 ? 28.549  11.663  -21.638 1.00 18.19 ? 197 PRO   B C   1 
ATOM   1543 O  O   . PRO   A 1 197 ? 29.605  11.912  -21.085 1.00 17.94 ? 197 PRO   B O   1 
ATOM   1544 C  CB  . PRO   A 1 197 ? 28.761  12.994  -23.785 1.00 16.98 ? 197 PRO   B CB  1 
ATOM   1545 C  CG  . PRO   A 1 197 ? 29.784  14.029  -23.318 1.00 17.31 ? 197 PRO   B CG  1 
ATOM   1546 C  CD  . PRO   A 1 197 ? 28.976  14.938  -22.406 1.00 17.60 ? 197 PRO   B CD  1 
ATOM   1547 N  N   . GLY   A 1 198 ? 27.932  10.469  -21.537 1.00 18.50 ? 198 GLY   B N   1 
ATOM   1548 C  CA  . GLY   A 1 198 ? 28.406  9.465   -20.594 1.00 16.68 ? 198 GLY   B CA  1 
ATOM   1549 C  C   . GLY   A 1 198 ? 27.960  8.055   -20.972 1.00 16.63 ? 198 GLY   B C   1 
ATOM   1550 O  O   . GLY   A 1 198 ? 27.803  7.746   -22.148 1.00 17.09 ? 198 GLY   B O   1 
ATOM   1551 N  N   . SER   A 1 199 ? 27.723  7.230   -19.961 1.00 17.05 ? 199 SER   B N   1 
ATOM   1552 C  CA  . SER   A 1 199 ? 27.559  5.800   -20.142 1.00 16.78 ? 199 SER   B CA  1 
ATOM   1553 C  C   . SER   A 1 199 ? 26.406  5.303   -19.297 1.00 17.52 ? 199 SER   B C   1 
ATOM   1554 O  O   . SER   A 1 199 ? 25.965  5.983   -18.371 1.00 15.99 ? 199 SER   B O   1 
ATOM   1555 C  CB  . SER   A 1 199 ? 28.862  5.105   -19.737 1.00 16.67 ? 199 SER   B CB  1 
ATOM   1556 O  OG  . SER   A 1 199 ? 29.009  5.026   -18.302 1.00 17.84 ? 199 SER   B OG  1 
ATOM   1557 N  N   . LEU   A 1 200 ? 25.983  4.057   -19.565 1.00 16.89 ? 200 LEU   B N   1 
ATOM   1558 C  CA  . LEU   A 1 200 ? 25.288  3.274   -18.569 1.00 18.55 ? 200 LEU   B CA  1 
ATOM   1559 C  C   . LEU   A 1 200 ? 26.131  3.279   -17.299 1.00 18.07 ? 200 LEU   B C   1 
ATOM   1560 O  O   . LEU   A 1 200 ? 27.352  3.344   -17.378 1.00 18.59 ? 200 LEU   B O   1 
ATOM   1561 C  CB  . LEU   A 1 200 ? 25.179  1.836   -19.092 1.00 20.61 ? 200 LEU   B CB  1 
ATOM   1562 C  CG  . LEU   A 1 200 ? 23.934  1.459   -19.888 1.00 25.52 ? 200 LEU   B CG  1 
ATOM   1563 C  CD1 . LEU   A 1 200 ? 23.127  2.637   -20.406 1.00 21.08 ? 200 LEU   B CD1 1 
ATOM   1564 C  CD2 . LEU   A 1 200 ? 24.242  0.419   -20.948 1.00 22.84 ? 200 LEU   B CD2 1 
ATOM   1565 N  N   . THR   A 1 201 ? 25.483  3.197   -16.127 1.00 16.41 ? 201 THR   B N   1 
ATOM   1566 C  CA  . THR   A 1 201 ? 26.253  3.047   -14.888 1.00 18.33 ? 201 THR   B CA  1 
ATOM   1567 C  C   . THR   A 1 201 ? 26.246  1.607   -14.362 1.00 18.31 ? 201 THR   B C   1 
ATOM   1568 O  O   . THR   A 1 201 ? 26.714  1.338   -13.243 1.00 21.16 ? 201 THR   B O   1 
ATOM   1569 C  CB  . THR   A 1 201 ? 25.790  4.019   -13.801 1.00 17.50 ? 201 THR   B CB  1 
ATOM   1570 O  OG1 . THR   A 1 201 ? 24.504  3.543   -13.401 1.00 18.33 ? 201 THR   B OG1 1 
ATOM   1571 C  CG2 . THR   A 1 201 ? 25.824  5.459   -14.280 1.00 16.36 ? 201 THR   B CG2 1 
ATOM   1572 N  N   . VAL   A 1 202 ? 25.674  0.699   -15.153 1.00 17.77 ? 202 VAL   B N   1 
ATOM   1573 C  CA  . VAL   A 1 202 ? 25.712  -0.726  -14.861 1.00 19.76 ? 202 VAL   B CA  1 
ATOM   1574 C  C   . VAL   A 1 202 ? 26.271  -1.413  -16.101 1.00 20.12 ? 202 VAL   B C   1 
ATOM   1575 O  O   . VAL   A 1 202 ? 26.138  -0.896  -17.203 1.00 19.63 ? 202 VAL   B O   1 
ATOM   1576 C  CB  . VAL   A 1 202 ? 24.325  -1.309  -14.544 1.00 19.96 ? 202 VAL   B CB  1 
ATOM   1577 C  CG1 . VAL   A 1 202 ? 23.735  -0.729  -13.270 1.00 20.44 ? 202 VAL   B CG1 1 
ATOM   1578 C  CG2 . VAL   A 1 202 ? 23.364  -1.143  -15.732 1.00 19.35 ? 202 VAL   B CG2 1 
ATOM   1579 N  N   . PRO   A 1 203 ? 26.930  -2.585  -15.984 1.00 22.98 ? 203 PRO   B N   1 
ATOM   1580 C  CA  . PRO   A 1 203 ? 27.343  -3.313  -17.186 1.00 23.71 ? 203 PRO   B CA  1 
ATOM   1581 C  C   . PRO   A 1 203 ? 26.096  -3.502  -18.052 1.00 24.12 ? 203 PRO   B C   1 
ATOM   1582 O  O   . PRO   A 1 203 ? 25.013  -3.736  -17.528 1.00 20.36 ? 203 PRO   B O   1 
ATOM   1583 C  CB  . PRO   A 1 203 ? 27.854  -4.652  -16.611 1.00 25.35 ? 203 PRO   B CB  1 
ATOM   1584 C  CG  . PRO   A 1 203 ? 28.324  -4.299  -15.210 1.00 22.24 ? 203 PRO   B CG  1 
ATOM   1585 C  CD  . PRO   A 1 203 ? 27.344  -3.233  -14.737 1.00 22.36 ? 203 PRO   B CD  1 
ATOM   1586 N  N   . PRO   A 1 204 ? 26.180  -3.415  -19.406 1.00 28.12 ? 204 PRO   B N   1 
ATOM   1587 C  CA  . PRO   A 1 204 ? 27.458  -3.330  -20.121 1.00 28.20 ? 204 PRO   B CA  1 
ATOM   1588 C  C   . PRO   A 1 204 ? 28.214  -1.999  -20.240 1.00 26.59 ? 204 PRO   B C   1 
ATOM   1589 O  O   . PRO   A 1 204 ? 29.207  -1.917  -20.971 1.00 21.64 ? 204 PRO   B O   1 
ATOM   1590 C  CB  . PRO   A 1 204 ? 27.080  -3.847  -21.520 1.00 28.67 ? 204 PRO   B CB  1 
ATOM   1591 C  CG  . PRO   A 1 204 ? 25.624  -3.413  -21.702 1.00 30.34 ? 204 PRO   B CG  1 
ATOM   1592 C  CD  . PRO   A 1 204 ? 25.020  -3.454  -20.314 1.00 29.03 ? 204 PRO   B CD  1 
ATOM   1593 N  N   . LEU   A 1 205 ? 27.763  -0.949  -19.531 1.00 23.23 ? 205 LEU   B N   1 
ATOM   1594 C  CA  . LEU   A 1 205 ? 28.588  0.249   -19.339 1.00 21.08 ? 205 LEU   B CA  1 
ATOM   1595 C  C   . LEU   A 1 205 ? 28.803  0.999   -20.648 1.00 19.37 ? 205 LEU   B C   1 
ATOM   1596 O  O   . LEU   A 1 205 ? 29.753  1.772   -20.775 1.00 22.45 ? 205 LEU   B O   1 
ATOM   1597 C  CB  . LEU   A 1 205 ? 29.923  -0.111  -18.656 1.00 21.38 ? 205 LEU   B CB  1 
ATOM   1598 C  CG  . LEU   A 1 205 ? 29.819  -0.694  -17.240 1.00 22.42 ? 205 LEU   B CG  1 
ATOM   1599 C  CD1 . LEU   A 1 205 ? 31.171  -1.194  -16.729 1.00 25.06 ? 205 LEU   B CD1 1 
ATOM   1600 C  CD2 . LEU   A 1 205 ? 29.270  0.358   -16.275 1.00 21.02 ? 205 LEU   B CD2 1 
ATOM   1601 N  N   . LEU   A 1 206 ? 27.886  0.798   -21.612 1.00 20.86 ? 206 LEU   B N   1 
ATOM   1602 C  CA  . LEU   A 1 206 ? 28.003  1.384   -22.951 1.00 22.67 ? 206 LEU   B CA  1 
ATOM   1603 C  C   . LEU   A 1 206 ? 27.966  2.908   -22.903 1.00 22.52 ? 206 LEU   B C   1 
ATOM   1604 O  O   . LEU   A 1 206 ? 27.157  3.472   -22.168 1.00 21.10 ? 206 LEU   B O   1 
ATOM   1605 C  CB  . LEU   A 1 206 ? 26.876  0.872   -23.853 1.00 22.80 ? 206 LEU   B CB  1 
ATOM   1606 C  CG  . LEU   A 1 206 ? 26.865  -0.641  -24.064 1.00 24.38 ? 206 LEU   B CG  1 
ATOM   1607 C  CD1 . LEU   A 1 206 ? 25.569  -1.081  -24.733 1.00 25.56 ? 206 LEU   B CD1 1 
ATOM   1608 C  CD2 . LEU   A 1 206 ? 28.074  -1.083  -24.858 1.00 27.40 ? 206 LEU   B CD2 1 
ATOM   1609 N  N   . GLU   A 1 207 ? 28.816  3.550   -23.720 1.00 21.49 ? 207 GLU   B N   1 
ATOM   1610 C  CA  . GLU   A 1 207 ? 28.960  5.000   -23.737 1.00 22.40 ? 207 GLU   B CA  1 
ATOM   1611 C  C   . GLU   A 1 207 ? 28.025  5.598   -24.789 1.00 24.74 ? 207 GLU   B C   1 
ATOM   1612 O  O   . GLU   A 1 207 ? 28.451  6.152   -25.811 1.00 25.04 ? 207 GLU   B O   1 
ATOM   1613 C  CB  . GLU   A 1 207 ? 30.425  5.385   -23.963 1.00 25.52 ? 207 GLU   B CB  1 
ATOM   1614 C  CG  . GLU   A 1 207 ? 31.345  4.745   -22.917 1.00 28.48 ? 207 GLU   B CG  1 
ATOM   1615 C  CD  . GLU   A 1 207 ? 32.806  5.155   -23.008 1.00 34.50 ? 207 GLU   B CD  1 
ATOM   1616 O  OE1 . GLU   A 1 207 ? 33.212  5.542   -24.135 1.00 34.45 ? 207 GLU   B OE1 1 
ATOM   1617 O  OE2 . GLU   A 1 207 ? 33.540  5.110   -21.941 1.00 30.55 ? 207 GLU   B OE2 1 
ATOM   1618 N  N   . SER   A 1 208 ? 26.725  5.444   -24.546 1.00 22.95 ? 208 SER   B N   1 
ATOM   1619 C  CA  . SER   A 1 208 ? 25.699  5.811   -25.515 1.00 21.32 ? 208 SER   B CA  1 
ATOM   1620 C  C   . SER   A 1 208 ? 24.679  6.758   -24.880 1.00 19.48 ? 208 SER   B C   1 
ATOM   1621 O  O   . SER   A 1 208 ? 23.578  6.912   -25.392 1.00 18.73 ? 208 SER   B O   1 
ATOM   1622 C  CB  . SER   A 1 208 ? 25.006  4.565   -25.961 1.00 23.89 ? 208 SER   B CB  1 
ATOM   1623 O  OG  . SER   A 1 208 ? 24.619  3.791   -24.840 1.00 25.86 ? 208 SER   B OG  1 
ATOM   1624 N  N   . VAL   A 1 209 ? 25.033  7.353   -23.740 1.00 19.20 ? 209 VAL   B N   1 
ATOM   1625 C  CA  . VAL   A 1 209 ? 24.036  8.059   -22.949 1.00 18.25 ? 209 VAL   B CA  1 
ATOM   1626 C  C   . VAL   A 1 209 ? 24.301  9.568   -22.961 1.00 17.78 ? 209 VAL   B C   1 
ATOM   1627 O  O   . VAL   A 1 209 ? 25.390  10.010  -22.632 1.00 17.75 ? 209 VAL   B O   1 
ATOM   1628 C  CB  . VAL   A 1 209 ? 23.964  7.518   -21.502 1.00 19.46 ? 209 VAL   B CB  1 
ATOM   1629 C  CG1 . VAL   A 1 209 ? 22.991  8.357   -20.666 1.00 17.27 ? 209 VAL   B CG1 1 
ATOM   1630 C  CG2 . VAL   A 1 209 ? 23.579  6.027   -21.471 1.00 17.81 ? 209 VAL   B CG2 1 
ATOM   1631 N  N   . THR   A 1 210 ? 23.240  10.346  -23.227 1.00 17.69 ? 210 THR   B N   1 
ATOM   1632 C  CA  . THR   A 1 210 ? 23.221  11.762  -22.932 1.00 16.68 ? 210 THR   B CA  1 
ATOM   1633 C  C   . THR   A 1 210 ? 22.508  11.897  -21.592 1.00 16.67 ? 210 THR   B C   1 
ATOM   1634 O  O   . THR   A 1 210 ? 21.318  11.543  -21.499 1.00 16.16 ? 210 THR   B O   1 
ATOM   1635 C  CB  . THR   A 1 210 ? 22.442  12.536  -24.002 1.00 19.09 ? 210 THR   B CB  1 
ATOM   1636 O  OG1 . THR   A 1 210 ? 22.979  12.301  -25.305 1.00 17.97 ? 210 THR   B OG1 1 
ATOM   1637 C  CG2 . THR   A 1 210 ? 22.374  14.021  -23.721 1.00 16.64 ? 210 THR   B CG2 1 
ATOM   1638 N  N   . TRP   A 1 211 ? 23.279  12.291  -20.567 1.00 13.94 ? 211 TRP   B N   1 
ATOM   1639 C  CA  . TRP   A 1 211 ? 22.759  12.471  -19.220 1.00 16.13 ? 211 TRP   B CA  1 
ATOM   1640 C  C   . TRP   A 1 211 ? 22.100  13.841  -19.095 1.00 15.88 ? 211 TRP   B C   1 
ATOM   1641 O  O   . TRP   A 1 211 ? 22.694  14.840  -19.455 1.00 16.61 ? 211 TRP   B O   1 
ATOM   1642 C  CB  . TRP   A 1 211 ? 23.864  12.353  -18.173 1.00 14.50 ? 211 TRP   B CB  1 
ATOM   1643 C  CG  . TRP   A 1 211 ? 24.188  10.916  -17.920 1.00 14.87 ? 211 TRP   B CG  1 
ATOM   1644 C  CD1 . TRP   A 1 211 ? 25.152  10.148  -18.512 1.00 15.18 ? 211 TRP   B CD1 1 
ATOM   1645 C  CD2 . TRP   A 1 211 ? 23.445  10.049  -17.059 1.00 16.17 ? 211 TRP   B CD2 1 
ATOM   1646 N  NE1 . TRP   A 1 211 ? 25.073  8.852   -18.042 1.00 16.21 ? 211 TRP   B NE1 1 
ATOM   1647 C  CE2 . TRP   A 1 211 ? 24.052  8.776   -17.128 1.00 15.72 ? 211 TRP   B CE2 1 
ATOM   1648 C  CE3 . TRP   A 1 211 ? 22.349  10.245  -16.206 1.00 15.80 ? 211 TRP   B CE3 1 
ATOM   1649 C  CZ2 . TRP   A 1 211 ? 23.572  7.687   -16.405 1.00 17.00 ? 211 TRP   B CZ2 1 
ATOM   1650 C  CZ3 . TRP   A 1 211 ? 21.893  9.170   -15.473 1.00 15.65 ? 211 TRP   B CZ3 1 
ATOM   1651 C  CH2 . TRP   A 1 211 ? 22.482  7.909   -15.590 1.00 15.95 ? 211 TRP   B CH2 1 
ATOM   1652 N  N   . ILE   A 1 212 ? 20.895  13.844  -18.538 1.00 15.60 ? 212 ILE   B N   1 
ATOM   1653 C  CA  . ILE   A 1 212 ? 20.161  15.052  -18.163 1.00 15.31 ? 212 ILE   B CA  1 
ATOM   1654 C  C   . ILE   A 1 212 ? 19.869  14.934  -16.657 1.00 14.90 ? 212 ILE   B C   1 
ATOM   1655 O  O   . ILE   A 1 212 ? 19.010  14.163  -16.228 1.00 16.85 ? 212 ILE   B O   1 
ATOM   1656 C  CB  . ILE   A 1 212 ? 18.893  15.156  -19.037 1.00 14.28 ? 212 ILE   B CB  1 
ATOM   1657 C  CG1 . ILE   A 1 212 ? 19.249  15.213  -20.535 1.00 16.92 ? 212 ILE   B CG1 1 
ATOM   1658 C  CG2 . ILE   A 1 212 ? 18.018  16.331  -18.587 1.00 14.97 ? 212 ILE   B CG2 1 
ATOM   1659 C  CD1 . ILE   A 1 212 ? 18.102  14.868  -21.498 1.00 15.93 ? 212 ILE   B CD1 1 
ATOM   1660 N  N   . VAL   A 1 213 ? 20.605  15.689  -15.845 1.00 15.06 ? 213 VAL   B N   1 
ATOM   1661 C  CA  . VAL   A 1 213 ? 20.472  15.596  -14.395 1.00 17.23 ? 213 VAL   B CA  1 
ATOM   1662 C  C   . VAL   A 1 213 ? 19.717  16.806  -13.872 1.00 16.89 ? 213 VAL   B C   1 
ATOM   1663 O  O   . VAL   A 1 213 ? 20.226  17.920  -14.009 1.00 15.68 ? 213 VAL   B O   1 
ATOM   1664 C  CB  . VAL   A 1 213 ? 21.852  15.471  -13.732 1.00 16.88 ? 213 VAL   B CB  1 
ATOM   1665 C  CG1 . VAL   A 1 213 ? 21.746  15.359  -12.200 1.00 15.93 ? 213 VAL   B CG1 1 
ATOM   1666 C  CG2 . VAL   A 1 213 ? 22.541  14.229  -14.303 1.00 17.22 ? 213 VAL   B CG2 1 
ATOM   1667 N  N   . LEU   A 1 214 ? 18.535  16.556  -13.282 1.00 16.71 ? 214 LEU   B N   1 
ATOM   1668 C  CA  . LEU   A 1 214 ? 17.713  17.639  -12.735 1.00 17.71 ? 214 LEU   B CA  1 
ATOM   1669 C  C   . LEU   A 1 214 ? 18.350  18.199  -11.474 1.00 18.07 ? 214 LEU   B C   1 
ATOM   1670 O  O   . LEU   A 1 214 ? 18.809  17.468  -10.606 1.00 19.19 ? 214 LEU   B O   1 
ATOM   1671 C  CB  . LEU   A 1 214 ? 16.261  17.197  -12.459 1.00 17.68 ? 214 LEU   B CB  1 
ATOM   1672 C  CG  . LEU   A 1 214 ? 15.474  16.719  -13.682 1.00 19.39 ? 214 LEU   B CG  1 
ATOM   1673 C  CD1 . LEU   A 1 214 ? 14.001  16.555  -13.335 1.00 22.60 ? 214 LEU   B CD1 1 
ATOM   1674 C  CD2 . LEU   A 1 214 ? 15.627  17.650  -14.884 1.00 17.85 ? 214 LEU   B CD2 1 
ATOM   1675 N  N   . LYS   A 1 215 ? 18.384  19.533  -11.394 1.00 20.11 ? 215 LYS   B N   1 
ATOM   1676 C  CA  . LYS   A 1 215 ? 18.954  20.205  -10.238 1.00 19.94 ? 215 LYS   B CA  1 
ATOM   1677 C  C   . LYS   A 1 215 ? 18.092  20.001  -8.982  1.00 19.39 ? 215 LYS   B C   1 
ATOM   1678 O  O   . LYS   A 1 215 ? 18.628  19.738  -7.897  1.00 19.96 ? 215 LYS   B O   1 
ATOM   1679 C  CB  . LYS   A 1 215 ? 19.137  21.698  -10.527 1.00 21.95 ? 215 LYS   B CB  1 
ATOM   1680 C  CG  . LYS   A 1 215 ? 19.679  22.488  -9.338  1.00 28.55 ? 215 LYS   B CG  1 
ATOM   1681 C  CD  . LYS   A 1 215 ? 20.019  23.930  -9.655  1.00 33.09 ? 215 LYS   B CD  1 
ATOM   1682 C  CE  . LYS   A 1 215 ? 20.072  24.795  -8.406  1.00 39.09 ? 215 LYS   B CE  1 
ATOM   1683 N  NZ  . LYS   A 1 215 ? 20.838  26.041  -8.667  1.00 39.02 ? 215 LYS   B NZ  1 
ATOM   1684 N  N   . GLN   A 1 216 ? 16.765  20.099  -9.122  1.00 19.03 ? 216 GLN   B N   1 
ATOM   1685 C  CA  . GLN   A 1 216 ? 15.883  20.151  -7.952  1.00 19.36 ? 216 GLN   B CA  1 
ATOM   1686 C  C   . GLN   A 1 216 ? 15.570  18.729  -7.467  1.00 17.60 ? 216 GLN   B C   1 
ATOM   1687 O  O   . GLN   A 1 216 ? 15.069  17.918  -8.245  1.00 18.63 ? 216 GLN   B O   1 
ATOM   1688 C  CB  . GLN   A 1 216 ? 14.546  20.799  -8.320  1.00 18.59 ? 216 GLN   B CB  1 
ATOM   1689 C  CG  . GLN   A 1 216 ? 13.580  20.830  -7.147  1.00 21.94 ? 216 GLN   B CG  1 
ATOM   1690 C  CD  . GLN   A 1 216 ? 12.466  21.839  -7.314  1.00 24.71 ? 216 GLN   B CD  1 
ATOM   1691 O  OE1 . GLN   A 1 216 ? 12.171  22.625  -6.418  1.00 32.61 ? 216 GLN   B OE1 1 
ATOM   1692 N  NE2 . GLN   A 1 216 ? 11.789  21.779  -8.439  1.00 22.47 ? 216 GLN   B NE2 1 
ATOM   1693 N  N   . PRO   A 1 217 ? 15.853  18.352  -6.195  1.00 18.32 ? 217 PRO   B N   1 
ATOM   1694 C  CA  . PRO   A 1 217 ? 15.510  17.002  -5.714  1.00 18.54 ? 217 PRO   B CA  1 
ATOM   1695 C  C   . PRO   A 1 217 ? 14.029  16.877  -5.350  1.00 17.33 ? 217 PRO   B C   1 
ATOM   1696 O  O   . PRO   A 1 217 ? 13.318  17.890  -5.273  1.00 15.52 ? 217 PRO   B O   1 
ATOM   1697 C  CB  . PRO   A 1 217 ? 16.389  16.822  -4.466  1.00 16.83 ? 217 PRO   B CB  1 
ATOM   1698 C  CG  . PRO   A 1 217 ? 16.571  18.268  -3.954  1.00 21.06 ? 217 PRO   B CG  1 
ATOM   1699 C  CD  . PRO   A 1 217 ? 16.629  19.127  -5.205  1.00 18.79 ? 217 PRO   B CD  1 
ATOM   1700 N  N   . ILE   A 1 218 ? 13.571  15.633  -5.204  1.00 17.39 ? 218 ILE   B N   1 
ATOM   1701 C  CA  . ILE   A 1 218 ? 12.248  15.323  -4.647  1.00 18.22 ? 218 ILE   B CA  1 
ATOM   1702 C  C   . ILE   A 1 218 ? 12.476  14.667  -3.286  1.00 19.01 ? 218 ILE   B C   1 
ATOM   1703 O  O   . ILE   A 1 218 ? 13.588  14.206  -2.986  1.00 19.78 ? 218 ILE   B O   1 
ATOM   1704 C  CB  . ILE   A 1 218 ? 11.449  14.399  -5.582  1.00 18.89 ? 218 ILE   B CB  1 
ATOM   1705 C  CG1 . ILE   A 1 218 ? 12.130  13.041  -5.760  1.00 18.81 ? 218 ILE   B CG1 1 
ATOM   1706 C  CG2 . ILE   A 1 218 ? 11.193  15.063  -6.926  1.00 22.28 ? 218 ILE   B CG2 1 
ATOM   1707 C  CD1 . ILE   A 1 218 ? 11.259  12.025  -6.487  1.00 18.87 ? 218 ILE   B CD1 1 
ATOM   1708 N  N   A ASN   A 1 219 ? 11.417  14.622  -2.468  0.50 18.08 ? 219 ASN   B N   1 
ATOM   1709 N  N   B ASN   A 1 219 ? 11.407  14.603  -2.477  0.50 18.68 ? 219 ASN   B N   1 
ATOM   1710 C  CA  A ASN   A 1 219 ? 11.534  14.097  -1.123  0.50 18.63 ? 219 ASN   B CA  1 
ATOM   1711 C  CA  B ASN   A 1 219 ? 11.487  14.087  -1.123  0.50 19.66 ? 219 ASN   B CA  1 
ATOM   1712 C  C   A ASN   A 1 219 ? 11.305  12.583  -1.108  0.50 18.32 ? 219 ASN   B C   1 
ATOM   1713 C  C   B ASN   A 1 219 ? 11.259  12.574  -1.086  0.50 19.05 ? 219 ASN   B C   1 
ATOM   1714 O  O   A ASN   A 1 219 ? 10.673  12.029  -2.007  0.50 17.85 ? 219 ASN   B O   1 
ATOM   1715 O  O   B ASN   A 1 219 ? 10.548  12.013  -1.918  0.50 18.86 ? 219 ASN   B O   1 
ATOM   1716 C  CB  A ASN   A 1 219 ? 10.617  14.857  -0.158  0.50 19.68 ? 219 ASN   B CB  1 
ATOM   1717 C  CB  B ASN   A 1 219 ? 10.444  14.742  -0.216  0.50 21.50 ? 219 ASN   B CB  1 
ATOM   1718 C  CG  A ASN   A 1 219 ? 9.195   14.986  -0.665  0.50 20.62 ? 219 ASN   B CG  1 
ATOM   1719 C  CG  B ASN   A 1 219 ? 10.596  16.240  -0.088  0.50 23.29 ? 219 ASN   B CG  1 
ATOM   1720 O  OD1 A ASN   A 1 219 ? 8.940   15.665  -1.664  0.50 22.66 ? 219 ASN   B OD1 1 
ATOM   1721 O  OD1 B ASN   A 1 219 ? 11.695  16.743  0.129   0.50 24.41 ? 219 ASN   B OD1 1 
ATOM   1722 N  ND2 A ASN   A 1 219 ? 8.255   14.375  0.044   0.50 21.00 ? 219 ASN   B ND2 1 
ATOM   1723 N  ND2 B ASN   A 1 219 ? 9.486   16.957  -0.195  0.50 25.36 ? 219 ASN   B ND2 1 
ATOM   1724 N  N   . ILE   A 1 220 ? 11.861  11.932  -0.078  1.00 18.92 ? 220 ILE   B N   1 
ATOM   1725 C  CA  . ILE   A 1 220 ? 11.572  10.555  0.306   1.00 17.44 ? 220 ILE   B CA  1 
ATOM   1726 C  C   . ILE   A 1 220 ? 11.767  10.480  1.824   1.00 17.11 ? 220 ILE   B C   1 
ATOM   1727 O  O   . ILE   A 1 220 ? 12.646  11.151  2.368   1.00 19.11 ? 220 ILE   B O   1 
ATOM   1728 C  CB  . ILE   A 1 220 ? 12.495  9.548   -0.423  1.00 17.82 ? 220 ILE   B CB  1 
ATOM   1729 C  CG1 . ILE   A 1 220 ? 12.119  8.097   -0.111  1.00 17.33 ? 220 ILE   B CG1 1 
ATOM   1730 C  CG2 . ILE   A 1 220 ? 13.965  9.782   -0.110  1.00 17.44 ? 220 ILE   B CG2 1 
ATOM   1731 C  CD1 . ILE   A 1 220 ? 12.685  7.089   -1.112  1.00 19.12 ? 220 ILE   B CD1 1 
ATOM   1732 N  N   . SER   A 1 221 ? 10.971  9.656   2.519   1.00 17.10 ? 221 SER   B N   1 
ATOM   1733 C  CA  . SER   A 1 221 ? 11.208  9.440   3.938   1.00 18.29 ? 221 SER   B CA  1 
ATOM   1734 C  C   . SER   A 1 221 ? 12.262  8.361   4.144   1.00 19.29 ? 221 SER   B C   1 
ATOM   1735 O  O   . SER   A 1 221 ? 12.523  7.566   3.251   1.00 18.79 ? 221 SER   B O   1 
ATOM   1736 C  CB  . SER   A 1 221 ? 9.940   9.160   4.730   1.00 17.89 ? 221 SER   B CB  1 
ATOM   1737 O  OG  . SER   A 1 221 ? 9.472   7.857   4.459   1.00 17.60 ? 221 SER   B OG  1 
ATOM   1738 N  N   . SER   A 1 222 ? 12.887  8.363   5.333   1.00 21.38 ? 222 SER   B N   1 
ATOM   1739 C  CA  . SER   A 1 222 ? 13.839  7.316   5.690   1.00 20.42 ? 222 SER   B CA  1 
ATOM   1740 C  C   . SER   A 1 222 ? 13.155  5.969   5.600   1.00 19.16 ? 222 SER   B C   1 
ATOM   1741 O  O   . SER   A 1 222 ? 13.805  4.998   5.247   1.00 20.47 ? 222 SER   B O   1 
ATOM   1742 C  CB  . SER   A 1 222 ? 14.333  7.452   7.109   1.00 21.99 ? 222 SER   B CB  1 
ATOM   1743 O  OG  . SER   A 1 222 ? 15.152  8.590   7.224   1.00 31.78 ? 222 SER   B OG  1 
ATOM   1744 N  N   . GLN   A 1 223 ? 11.908  5.902   6.071   1.00 19.12 ? 223 GLN   B N   1 
ATOM   1745 C  CA  . GLN   A 1 223 ? 11.221  4.621   6.150   1.00 21.64 ? 223 GLN   B CA  1 
ATOM   1746 C  C   . GLN   A 1 223 ? 10.918  4.118   4.731   1.00 20.78 ? 223 GLN   B C   1 
ATOM   1747 O  O   . GLN   A 1 223 ? 10.954  2.913   4.487   1.00 20.64 ? 223 GLN   B O   1 
ATOM   1748 C  CB  . GLN   A 1 223 ? 9.967   4.703   7.030   1.00 26.83 ? 223 GLN   B CB  1 
ATOM   1749 C  CG  . GLN   A 1 223 ? 10.237  4.979   8.512   1.00 27.74 ? 223 GLN   B CG  1 
ATOM   1750 C  CD  . GLN   A 1 223 ? 10.502  6.442   8.792   1.00 32.09 ? 223 GLN   B CD  1 
ATOM   1751 O  OE1 . GLN   A 1 223 ? 10.870  6.826   9.907   1.00 33.06 ? 223 GLN   B OE1 1 
ATOM   1752 N  NE2 . GLN   A 1 223 ? 10.242  7.289   7.799   1.00 25.64 ? 223 GLN   B NE2 1 
ATOM   1753 N  N   . GLN   A 1 224 ? 10.599  5.043   3.799   1.00 18.31 ? 224 GLN   B N   1 
ATOM   1754 C  CA  . GLN   A 1 224 ? 10.336  4.674   2.413   1.00 17.58 ? 224 GLN   B CA  1 
ATOM   1755 C  C   . GLN   A 1 224 ? 11.589  4.097   1.755   1.00 19.03 ? 224 GLN   B C   1 
ATOM   1756 O  O   . GLN   A 1 224 ? 11.499  3.074   1.077   1.00 19.45 ? 224 GLN   B O   1 
ATOM   1757 C  CB  . GLN   A 1 224 ? 9.824   5.860   1.595   1.00 17.87 ? 224 GLN   B CB  1 
ATOM   1758 C  CG  . GLN   A 1 224 ? 8.346   6.143   1.826   1.00 20.20 ? 224 GLN   B CG  1 
ATOM   1759 C  CD  . GLN   A 1 224 ? 7.893   7.359   1.061   1.00 19.07 ? 224 GLN   B CD  1 
ATOM   1760 O  OE1 . GLN   A 1 224 ? 8.562   8.376   1.054   1.00 21.37 ? 224 GLN   B OE1 1 
ATOM   1761 N  NE2 . GLN   A 1 224 ? 6.717   7.280   0.471   1.00 17.91 ? 224 GLN   B NE2 1 
ATOM   1762 N  N   . LEU   A 1 225 ? 12.740  4.772   1.944   1.00 18.37 ? 225 LEU   B N   1 
ATOM   1763 C  CA  . LEU   A 1 225 ? 13.994  4.337   1.357   1.00 20.58 ? 225 LEU   B CA  1 
ATOM   1764 C  C   . LEU   A 1 225 ? 14.423  2.978   1.919   1.00 21.49 ? 225 LEU   B C   1 
ATOM   1765 O  O   . LEU   A 1 225 ? 14.885  2.118   1.160   1.00 24.17 ? 225 LEU   B O   1 
ATOM   1766 C  CB  . LEU   A 1 225 ? 15.039  5.419   1.616   1.00 20.67 ? 225 LEU   B CB  1 
ATOM   1767 C  CG  . LEU   A 1 225 ? 16.397  5.238   0.942   1.00 21.65 ? 225 LEU   B CG  1 
ATOM   1768 C  CD1 . LEU   A 1 225 ? 16.272  5.090   -0.567  1.00 21.81 ? 225 LEU   B CD1 1 
ATOM   1769 C  CD2 . LEU   A 1 225 ? 17.263  6.443   1.268   1.00 23.86 ? 225 LEU   B CD2 1 
ATOM   1770 N  N   . ALA   A 1 226 ? 14.260  2.766   3.237   1.00 21.32 ? 226 ALA   B N   1 
ATOM   1771 C  CA  . ALA   A 1 226 ? 14.647  1.491   3.837   1.00 21.00 ? 226 ALA   B CA  1 
ATOM   1772 C  C   . ALA   A 1 226 ? 13.948  0.332   3.141   1.00 21.13 ? 226 ALA   B C   1 
ATOM   1773 O  O   . ALA   A 1 226 ? 14.526  -0.752  3.049   1.00 20.38 ? 226 ALA   B O   1 
ATOM   1774 C  CB  . ALA   A 1 226 ? 14.422  1.452   5.360   1.00 20.48 ? 226 ALA   B CB  1 
ATOM   1775 N  N   . LYS   A 1 227 ? 12.718  0.539   2.664   1.00 20.88 ? 227 LYS   B N   1 
ATOM   1776 C  CA  . LYS   A 1 227 ? 11.975  -0.540  2.025   1.00 24.18 ? 227 LYS   B CA  1 
ATOM   1777 C  C   . LYS   A 1 227 ? 12.714  -1.092  0.798   1.00 23.15 ? 227 LYS   B C   1 
ATOM   1778 O  O   . LYS   A 1 227 ? 12.646  -2.282  0.540   1.00 20.30 ? 227 LYS   B O   1 
ATOM   1779 C  CB  . LYS   A 1 227 ? 10.511  -0.192  1.739   1.00 26.66 ? 227 LYS   B CB  1 
ATOM   1780 C  CG  . LYS   A 1 227 ? 9.562   -0.543  2.883   1.00 36.49 ? 227 LYS   B CG  1 
ATOM   1781 C  CD  . LYS   A 1 227 ? 8.075   -0.357  2.607   1.00 43.19 ? 227 LYS   B CD  1 
ATOM   1782 C  CE  . LYS   A 1 227 ? 7.459   -1.418  1.720   1.00 40.07 ? 227 LYS   B CE  1 
ATOM   1783 N  NZ  . LYS   A 1 227 ? 7.812   -2.793  2.164   1.00 42.51 ? 227 LYS   B NZ  1 
ATOM   1784 N  N   . PHE   A 1 228 ? 13.438  -0.236  0.067   1.00 18.92 ? 228 PHE   B N   1 
ATOM   1785 C  CA  . PHE   A 1 228 ? 14.172  -0.660  -1.108  1.00 19.18 ? 228 PHE   B CA  1 
ATOM   1786 C  C   . PHE   A 1 228 ? 15.293  -1.624  -0.744  1.00 19.36 ? 228 PHE   B C   1 
ATOM   1787 O  O   . PHE   A 1 228 ? 15.570  -2.534  -1.501  1.00 19.17 ? 228 PHE   B O   1 
ATOM   1788 C  CB  . PHE   A 1 228 ? 14.700  0.553   -1.889  1.00 18.34 ? 228 PHE   B CB  1 
ATOM   1789 C  CG  . PHE   A 1 228 ? 13.558  1.317   -2.518  1.00 20.62 ? 228 PHE   B CG  1 
ATOM   1790 C  CD1 . PHE   A 1 228 ? 12.925  0.848   -3.663  1.00 20.06 ? 228 PHE   B CD1 1 
ATOM   1791 C  CD2 . PHE   A 1 228 ? 13.090  2.490   -1.947  1.00 20.56 ? 228 PHE   B CD2 1 
ATOM   1792 C  CE1 . PHE   A 1 228 ? 11.860  1.544   -4.226  1.00 21.19 ? 228 PHE   B CE1 1 
ATOM   1793 C  CE2 . PHE   A 1 228 ? 12.007  3.166   -2.491  1.00 21.05 ? 228 PHE   B CE2 1 
ATOM   1794 C  CZ  . PHE   A 1 228 ? 11.395  2.697   -3.633  1.00 22.04 ? 228 PHE   B CZ  1 
ATOM   1795 N  N   . ARG   A 1 229 ? 15.936  -1.414  0.405   1.00 20.08 ? 229 ARG   B N   1 
ATOM   1796 C  CA  . ARG   A 1 229 ? 17.114  -2.198  0.739   1.00 19.95 ? 229 ARG   B CA  1 
ATOM   1797 C  C   . ARG   A 1 229 ? 16.662  -3.586  1.163   1.00 20.46 ? 229 ARG   B C   1 
ATOM   1798 O  O   . ARG   A 1 229 ? 17.495  -4.440  1.372   1.00 24.15 ? 229 ARG   B O   1 
ATOM   1799 C  CB  . ARG   A 1 229 ? 17.850  -1.576  1.922   1.00 19.50 ? 229 ARG   B CB  1 
ATOM   1800 C  CG  . ARG   A 1 229 ? 18.360  -0.169  1.655   1.00 19.52 ? 229 ARG   B CG  1 
ATOM   1801 C  CD  . ARG   A 1 229 ? 19.309  0.244   2.773   1.00 19.02 ? 229 ARG   B CD  1 
ATOM   1802 N  NE  . ARG   A 1 229 ? 19.653  1.628   2.559   1.00 18.28 ? 229 ARG   B NE  1 
ATOM   1803 C  CZ  . ARG   A 1 229 ? 19.020  2.689   3.030   1.00 17.25 ? 229 ARG   B CZ  1 
ATOM   1804 N  NH1 . ARG   A 1 229 ? 18.011  2.578   3.873   1.00 18.01 ? 229 ARG   B NH1 1 
ATOM   1805 N  NH2 . ARG   A 1 229 ? 19.447  3.895   2.692   1.00 20.33 ? 229 ARG   B NH2 1 
ATOM   1806 N  N   . SER   A 1 230 ? 15.345  -3.780  1.315   1.00 22.19 ? 230 SER   B N   1 
ATOM   1807 C  CA  . SER   A 1 230 ? 14.784  -5.093  1.623   1.00 23.33 ? 230 SER   B CA  1 
ATOM   1808 C  C   . SER   A 1 230 ? 14.637  -5.990  0.414   1.00 22.88 ? 230 SER   B C   1 
ATOM   1809 O  O   . SER   A 1 230 ? 14.297  -7.165  0.588   1.00 24.56 ? 230 SER   B O   1 
ATOM   1810 C  CB  . SER   A 1 230 ? 13.491  -4.994  2.353   1.00 24.77 ? 230 SER   B CB  1 
ATOM   1811 O  OG  . SER   A 1 230 ? 13.779  -5.092  3.729   1.00 32.47 ? 230 SER   B OG  1 
ATOM   1812 N  N   . LEU   A 1 231 ? 14.890  -5.455  -0.788  1.00 21.98 ? 231 LEU   B N   1 
ATOM   1813 C  CA  . LEU   A 1 231 ? 14.920  -6.287  -1.984  1.00 22.51 ? 231 LEU   B CA  1 
ATOM   1814 C  C   . LEU   A 1 231 ? 16.140  -7.205  -1.936  1.00 23.14 ? 231 LEU   B C   1 
ATOM   1815 O  O   . LEU   A 1 231 ? 17.181  -6.799  -1.429  1.00 23.32 ? 231 LEU   B O   1 
ATOM   1816 C  CB  . LEU   A 1 231 ? 14.996  -5.405  -3.234  1.00 20.88 ? 231 LEU   B CB  1 
ATOM   1817 C  CG  . LEU   A 1 231 ? 13.739  -4.589  -3.539  1.00 22.87 ? 231 LEU   B CG  1 
ATOM   1818 C  CD1 . LEU   A 1 231 ? 14.017  -3.639  -4.691  1.00 19.92 ? 231 LEU   B CD1 1 
ATOM   1819 C  CD2 . LEU   A 1 231 ? 12.572  -5.508  -3.871  1.00 21.07 ? 231 LEU   B CD2 1 
ATOM   1820 N  N   . LEU   A 1 232 ? 16.008  -8.414  -2.516  1.00 22.41 ? 232 LEU   B N   1 
ATOM   1821 C  CA  . LEU   A 1 232 ? 17.128  -9.348  -2.628  1.00 24.90 ? 232 LEU   B CA  1 
ATOM   1822 C  C   . LEU   A 1 232 ? 17.867  -9.191  -3.955  1.00 25.01 ? 232 LEU   B C   1 
ATOM   1823 O  O   . LEU   A 1 232 ? 17.289  -8.869  -4.984  1.00 28.25 ? 232 LEU   B O   1 
ATOM   1824 C  CB  . LEU   A 1 232 ? 16.641  -10.793 -2.440  1.00 24.26 ? 232 LEU   B CB  1 
ATOM   1825 C  CG  . LEU   A 1 232 ? 15.938  -11.066 -1.106  1.00 24.62 ? 232 LEU   B CG  1 
ATOM   1826 C  CD1 . LEU   A 1 232 ? 15.413  -12.497 -1.047  1.00 26.01 ? 232 LEU   B CD1 1 
ATOM   1827 C  CD2 . LEU   A 1 232 ? 16.858  -10.764 0.068   1.00 24.62 ? 232 LEU   B CD2 1 
ATOM   1828 N  N   . CYS   A 1 233 ? 19.188  -9.399  -3.922  1.00 28.27 ? 233 CYS   B N   1 
ATOM   1829 C  CA  . CYS   A 1 233 ? 19.939  -9.525  -5.163  1.00 25.52 ? 233 CYS   B CA  1 
ATOM   1830 C  C   . CYS   A 1 233 ? 20.062  -10.998 -5.563  1.00 25.84 ? 233 CYS   B C   1 
ATOM   1831 O  O   . CYS   A 1 233 ? 20.789  -11.344 -6.488  1.00 26.76 ? 233 CYS   B O   1 
ATOM   1832 C  CB  . CYS   A 1 233 ? 21.316  -8.881  -5.053  1.00 25.59 ? 233 CYS   B CB  1 
ATOM   1833 S  SG  . CYS   A 1 233 ? 22.380  -9.644  -3.797  1.00 29.53 ? 233 CYS   B SG  1 
ATOM   1834 N  N   . THR   A 1 234 ? 19.298  -11.867 -4.912  1.00 26.80 ? 234 THR   B N   1 
ATOM   1835 C  CA  . THR   A 1 234 ? 19.391  -13.283 -5.223  1.00 27.02 ? 234 THR   B CA  1 
ATOM   1836 C  C   . THR   A 1 234 ? 18.005  -13.805 -5.610  1.00 30.46 ? 234 THR   B C   1 
ATOM   1837 O  O   . THR   A 1 234 ? 16.985  -13.266 -5.150  1.00 28.71 ? 234 THR   B O   1 
ATOM   1838 C  CB  . THR   A 1 234 ? 19.978  -14.038 -4.019  1.00 28.43 ? 234 THR   B CB  1 
ATOM   1839 O  OG1 . THR   A 1 234 ? 19.216  -13.590 -2.897  1.00 32.53 ? 234 THR   B OG1 1 
ATOM   1840 C  CG2 . THR   A 1 234 ? 21.444  -13.754 -3.776  1.00 28.82 ? 234 THR   B CG2 1 
ATOM   1841 N  N   . ALA   A 1 235 ? 17.988  -14.904 -6.392  1.00 30.25 ? 235 ALA   B N   1 
ATOM   1842 C  CA  . ALA   A 1 235 ? 16.773  -15.566 -6.849  1.00 32.04 ? 235 ALA   B CA  1 
ATOM   1843 C  C   . ALA   A 1 235 ? 16.233  -16.569 -5.821  1.00 37.74 ? 235 ALA   B C   1 
ATOM   1844 O  O   . ALA   A 1 235 ? 16.921  -16.944 -4.863  1.00 31.31 ? 235 ALA   B O   1 
ATOM   1845 C  CB  . ALA   A 1 235 ? 17.026  -16.253 -8.171  1.00 32.98 ? 235 ALA   B CB  1 
ATOM   1846 N  N   . GLU   A 1 236 ? 14.974  -16.989 -6.042  1.00 37.97 ? 236 GLU   B N   1 
ATOM   1847 C  CA  . GLU   A 1 236 ? 14.298  -18.001 -5.245  1.00 44.45 ? 236 GLU   B CA  1 
ATOM   1848 C  C   . GLU   A 1 236 ? 15.157  -19.265 -5.191  1.00 48.53 ? 236 GLU   B C   1 
ATOM   1849 O  O   . GLU   A 1 236 ? 15.731  -19.679 -6.206  1.00 45.04 ? 236 GLU   B O   1 
ATOM   1850 C  CB  . GLU   A 1 236 ? 12.938  -18.306 -5.877  1.00 53.85 ? 236 GLU   B CB  1 
ATOM   1851 C  CG  . GLU   A 1 236 ? 12.054  -19.219 -5.041  1.00 59.23 ? 236 GLU   B CG  1 
ATOM   1852 C  CD  . GLU   A 1 236 ? 11.330  -18.532 -3.892  1.00 61.86 ? 236 GLU   B CD  1 
ATOM   1853 O  OE1 . GLU   A 1 236 ? 11.984  -18.264 -2.857  1.00 69.11 ? 236 GLU   B OE1 1 
ATOM   1854 O  OE2 . GLU   A 1 236 ? 10.108  -18.270 -4.031  1.00 61.72 ? 236 GLU   B OE2 1 
ATOM   1855 N  N   . GLY   A 1 237 ? 15.250  -19.855 -3.991  1.00 50.13 ? 237 GLY   B N   1 
ATOM   1856 C  CA  . GLY   A 1 237 ? 16.028  -21.066 -3.775  1.00 57.89 ? 237 GLY   B CA  1 
ATOM   1857 C  C   . GLY   A 1 237 ? 17.514  -20.848 -4.051  1.00 62.46 ? 237 GLY   B C   1 
ATOM   1858 O  O   . GLY   A 1 237 ? 18.111  -21.559 -4.857  1.00 68.68 ? 237 GLY   B O   1 
ATOM   1859 N  N   . GLU   A 1 238 ? 18.080  -19.850 -3.358  1.00 59.57 ? 238 GLU   B N   1 
ATOM   1860 C  CA  . GLU   A 1 238 ? 19.459  -19.399 -3.476  1.00 54.79 ? 238 GLU   B CA  1 
ATOM   1861 C  C   . GLU   A 1 238 ? 19.750  -18.596 -2.208  1.00 49.15 ? 238 GLU   B C   1 
ATOM   1862 O  O   . GLU   A 1 238 ? 18.855  -17.919 -1.709  1.00 43.92 ? 238 GLU   B O   1 
ATOM   1863 C  CB  . GLU   A 1 238 ? 19.599  -18.555 -4.749  1.00 58.80 ? 238 GLU   B CB  1 
ATOM   1864 C  CG  . GLU   A 1 238 ? 21.019  -18.360 -5.250  1.00 66.42 ? 238 GLU   B CG  1 
ATOM   1865 C  CD  . GLU   A 1 238 ? 21.159  -17.205 -6.232  1.00 71.57 ? 238 GLU   B CD  1 
ATOM   1866 O  OE1 . GLU   A 1 238 ? 22.219  -16.545 -6.218  1.00 70.90 ? 238 GLU   B OE1 1 
ATOM   1867 O  OE2 . GLU   A 1 238 ? 20.202  -16.955 -7.000  1.00 74.48 ? 238 GLU   B OE2 1 
ATOM   1868 N  N   . ALA   A 1 239 ? 20.971  -18.718 -1.663  1.00 46.11 ? 239 ALA   B N   1 
ATOM   1869 C  CA  . ALA   A 1 239 ? 21.353  -18.080 -0.408  1.00 41.49 ? 239 ALA   B CA  1 
ATOM   1870 C  C   . ALA   A 1 239 ? 21.034  -16.581 -0.473  1.00 39.07 ? 239 ALA   B C   1 
ATOM   1871 O  O   . ALA   A 1 239 ? 21.528  -15.910 -1.365  1.00 38.82 ? 239 ALA   B O   1 
ATOM   1872 C  CB  . ALA   A 1 239 ? 22.829  -18.307 -0.174  1.00 38.51 ? 239 ALA   B CB  1 
ATOM   1873 N  N   . ALA   A 1 240 ? 20.222  -16.074 0.469   1.00 36.71 ? 240 ALA   B N   1 
ATOM   1874 C  CA  . ALA   A 1 240 ? 19.695  -14.711 0.451   1.00 35.79 ? 240 ALA   B CA  1 
ATOM   1875 C  C   . ALA   A 1 240 ? 20.794  -13.678 0.702   1.00 32.38 ? 240 ALA   B C   1 
ATOM   1876 O  O   . ALA   A 1 240 ? 21.617  -13.819 1.609   1.00 30.35 ? 240 ALA   B O   1 
ATOM   1877 C  CB  . ALA   A 1 240 ? 18.597  -14.579 1.474   1.00 34.56 ? 240 ALA   B CB  1 
ATOM   1878 N  N   . ALA   A 1 241 ? 20.814  -12.637 -0.129  1.00 26.76 ? 241 ALA   B N   1 
ATOM   1879 C  CA  . ALA   A 1 241 ? 21.661  -11.474 0.099   1.00 24.54 ? 241 ALA   B CA  1 
ATOM   1880 C  C   . ALA   A 1 241 ? 20.839  -10.233 -0.248  1.00 22.67 ? 241 ALA   B C   1 
ATOM   1881 O  O   . ALA   A 1 241 ? 20.068  -10.287 -1.183  1.00 19.67 ? 241 ALA   B O   1 
ATOM   1882 C  CB  . ALA   A 1 241 ? 22.865  -11.557 -0.796  1.00 25.59 ? 241 ALA   B CB  1 
ATOM   1883 N  N   . PHE   A 1 242 ? 20.986  -9.143  0.513   1.00 22.64 ? 242 PHE   B N   1 
ATOM   1884 C  CA  . PHE   A 1 242 ? 20.062  -8.024  0.363   1.00 22.28 ? 242 PHE   B CA  1 
ATOM   1885 C  C   . PHE   A 1 242 ? 20.730  -6.954  -0.493  1.00 21.77 ? 242 PHE   B C   1 
ATOM   1886 O  O   . PHE   A 1 242 ? 21.945  -6.816  -0.466  1.00 21.77 ? 242 PHE   B O   1 
ATOM   1887 C  CB  . PHE   A 1 242 ? 19.699  -7.428  1.724   1.00 20.82 ? 242 PHE   B CB  1 
ATOM   1888 C  CG  . PHE   A 1 242 ? 18.745  -8.243  2.560   1.00 26.35 ? 242 PHE   B CG  1 
ATOM   1889 C  CD1 . PHE   A 1 242 ? 17.375  -8.111  2.401   1.00 25.29 ? 242 PHE   B CD1 1 
ATOM   1890 C  CD2 . PHE   A 1 242 ? 19.219  -9.124  3.527   1.00 25.15 ? 242 PHE   B CD2 1 
ATOM   1891 C  CE1 . PHE   A 1 242 ? 16.480  -8.834  3.178   1.00 29.29 ? 242 PHE   B CE1 1 
ATOM   1892 C  CE2 . PHE   A 1 242 ? 18.320  -9.849  4.298   1.00 28.57 ? 242 PHE   B CE2 1 
ATOM   1893 C  CZ  . PHE   A 1 242 ? 16.956  -9.708  4.125   1.00 28.87 ? 242 PHE   B CZ  1 
ATOM   1894 N  N   . LEU   A 1 243 ? 19.924  -6.158  -1.213  1.00 19.22 ? 243 LEU   B N   1 
ATOM   1895 C  CA  . LEU   A 1 243 ? 20.439  -5.123  -2.090  1.00 21.11 ? 243 LEU   B CA  1 
ATOM   1896 C  C   . LEU   A 1 243 ? 20.492  -3.814  -1.296  1.00 20.25 ? 243 LEU   B C   1 
ATOM   1897 O  O   . LEU   A 1 243 ? 19.680  -2.897  -1.481  1.00 21.01 ? 243 LEU   B O   1 
ATOM   1898 C  CB  . LEU   A 1 243 ? 19.457  -5.053  -3.267  1.00 21.01 ? 243 LEU   B CB  1 
ATOM   1899 C  CG  . LEU   A 1 243 ? 19.902  -4.307  -4.514  1.00 25.52 ? 243 LEU   B CG  1 
ATOM   1900 C  CD1 . LEU   A 1 243 ? 21.216  -4.834  -5.101  1.00 24.92 ? 243 LEU   B CD1 1 
ATOM   1901 C  CD2 . LEU   A 1 243 ? 18.784  -4.346  -5.545  1.00 25.41 ? 243 LEU   B CD2 1 
ATOM   1902 N  N   . VAL   A 1 244 ? 21.448  -3.755  -0.371  1.00 20.50 ? 244 VAL   B N   1 
ATOM   1903 C  CA  . VAL   A 1 244 ? 21.523  -2.655  0.568   1.00 19.23 ? 244 VAL   B CA  1 
ATOM   1904 C  C   . VAL   A 1 244 ? 22.071  -1.426  -0.133  1.00 19.00 ? 244 VAL   B C   1 
ATOM   1905 O  O   . VAL   A 1 244 ? 21.847  -0.331  0.363   1.00 19.22 ? 244 VAL   B O   1 
ATOM   1906 C  CB  . VAL   A 1 244 ? 22.313  -2.992  1.857   1.00 21.79 ? 244 VAL   B CB  1 
ATOM   1907 C  CG1 . VAL   A 1 244 ? 21.688  -4.139  2.654   1.00 21.10 ? 244 VAL   B CG1 1 
ATOM   1908 C  CG2 . VAL   A 1 244 ? 23.793  -3.223  1.601   1.00 19.15 ? 244 VAL   B CG2 1 
ATOM   1909 N  N   . SER   A 1 245 ? 22.774  -1.612  -1.267  1.00 18.45 ? 245 SER   B N   1 
ATOM   1910 C  CA  . SER   A 1 245 ? 23.483  -0.551  -1.972  1.00 19.38 ? 245 SER   B CA  1 
ATOM   1911 C  C   . SER   A 1 245 ? 23.604  -0.909  -3.456  1.00 20.44 ? 245 SER   B C   1 
ATOM   1912 O  O   . SER   A 1 245 ? 23.867  -2.050  -3.779  1.00 20.33 ? 245 SER   B O   1 
ATOM   1913 C  CB  . SER   A 1 245 ? 24.856  -0.339  -1.373  1.00 21.31 ? 245 SER   B CB  1 
ATOM   1914 O  OG  . SER   A 1 245 ? 25.454  0.839   -1.890  1.00 20.42 ? 245 SER   B OG  1 
ATOM   1915 N  N   . ASN   A 1 246 ? 23.398  0.055   -4.373  1.00 18.71 ? 246 ASN   B N   1 
ATOM   1916 C  CA  . ASN   A 1 246 ? 23.425  -0.260  -5.801  1.00 18.71 ? 246 ASN   B CA  1 
ATOM   1917 C  C   . ASN   A 1 246 ? 23.845  0.948   -6.630  1.00 20.34 ? 246 ASN   B C   1 
ATOM   1918 O  O   . ASN   A 1 246 ? 23.294  1.164   -7.698  1.00 20.25 ? 246 ASN   B O   1 
ATOM   1919 C  CB  . ASN   A 1 246 ? 22.094  -0.833  -6.302  1.00 17.58 ? 246 ASN   B CB  1 
ATOM   1920 C  CG  . ASN   A 1 246 ? 20.910  0.124   -6.210  1.00 17.86 ? 246 ASN   B CG  1 
ATOM   1921 O  OD1 . ASN   A 1 246 ? 20.999  1.187   -5.588  1.00 16.91 ? 246 ASN   B OD1 1 
ATOM   1922 N  ND2 . ASN   A 1 246 ? 19.793  -0.239  -6.841  1.00 16.12 ? 246 ASN   B ND2 1 
ATOM   1923 N  N   . HIS   A 1 247 ? 24.814  1.724   -6.135  1.00 19.68 ? 247 HIS   B N   1 
ATOM   1924 C  CA  . HIS   A 1 247 ? 25.301  2.895   -6.844  1.00 19.79 ? 247 HIS   B CA  1 
ATOM   1925 C  C   . HIS   A 1 247 ? 26.779  2.715   -7.178  1.00 20.11 ? 247 HIS   B C   1 
ATOM   1926 O  O   . HIS   A 1 247 ? 27.532  2.109   -6.414  1.00 22.13 ? 247 HIS   B O   1 
ATOM   1927 C  CB  . HIS   A 1 247 ? 25.031  4.168   -6.028  1.00 19.42 ? 247 HIS   B CB  1 
ATOM   1928 C  CG  . HIS   A 1 247 ? 25.815  4.289   -4.759  1.00 23.71 ? 247 HIS   B CG  1 
ATOM   1929 N  ND1 . HIS   A 1 247 ? 25.460  3.635   -3.585  1.00 25.14 ? 247 HIS   B ND1 1 
ATOM   1930 C  CD2 . HIS   A 1 247 ? 26.943  4.970   -4.484  1.00 25.38 ? 247 HIS   B CD2 1 
ATOM   1931 C  CE1 . HIS   A 1 247 ? 26.318  3.942   -2.631  1.00 25.97 ? 247 HIS   B CE1 1 
ATOM   1932 N  NE2 . HIS   A 1 247 ? 27.228  4.761   -3.156  1.00 29.85 ? 247 HIS   B NE2 1 
ATOM   1933 N  N   . ARG   A 1 248 ? 27.168  3.211   -8.356  1.00 19.32 ? 248 ARG   B N   1 
ATOM   1934 C  CA  . ARG   A 1 248 ? 28.537  3.158   -8.828  1.00 20.00 ? 248 ARG   B CA  1 
ATOM   1935 C  C   . ARG   A 1 248 ? 29.254  4.427   -8.386  1.00 21.52 ? 248 ARG   B C   1 
ATOM   1936 O  O   . ARG   A 1 248 ? 28.652  5.497   -8.453  1.00 19.00 ? 248 ARG   B O   1 
ATOM   1937 C  CB  . ARG   A 1 248 ? 28.553  3.096   -10.359 1.00 21.23 ? 248 ARG   B CB  1 
ATOM   1938 C  CG  . ARG   A 1 248 ? 29.948  2.931   -10.936 1.00 21.29 ? 248 ARG   B CG  1 
ATOM   1939 C  CD  . ARG   A 1 248 ? 29.989  3.159   -12.427 1.00 21.75 ? 248 ARG   B CD  1 
ATOM   1940 N  NE  . ARG   A 1 248 ? 31.177  2.560   -13.031 1.00 20.32 ? 248 ARG   B NE  1 
ATOM   1941 C  CZ  . ARG   A 1 248 ? 31.573  2.771   -14.294 1.00 22.24 ? 248 ARG   B CZ  1 
ATOM   1942 N  NH1 . ARG   A 1 248 ? 30.876  3.558   -15.091 1.00 19.49 ? 248 ARG   B NH1 1 
ATOM   1943 N  NH2 . ARG   A 1 248 ? 32.659  2.178   -14.759 1.00 22.89 ? 248 ARG   B NH2 1 
ATOM   1944 N  N   . PRO   A 1 249 ? 30.530  4.335   -7.938  1.00 21.44 ? 249 PRO   B N   1 
ATOM   1945 C  CA  . PRO   A 1 249 ? 31.303  5.506   -7.516  1.00 22.87 ? 249 PRO   B CA  1 
ATOM   1946 C  C   . PRO   A 1 249 ? 31.485  6.426   -8.714  1.00 23.65 ? 249 PRO   B C   1 
ATOM   1947 O  O   . PRO   A 1 249 ? 31.369  5.988   -9.863  1.00 20.79 ? 249 PRO   B O   1 
ATOM   1948 C  CB  . PRO   A 1 249 ? 32.698  4.936   -7.153  1.00 23.65 ? 249 PRO   B CB  1 
ATOM   1949 C  CG  . PRO   A 1 249 ? 32.472  3.460   -6.922  1.00 25.00 ? 249 PRO   B CG  1 
ATOM   1950 C  CD  . PRO   A 1 249 ? 31.286  3.077   -7.778  1.00 23.74 ? 249 PRO   B CD  1 
ATOM   1951 N  N   . PRO   A 1 250 ? 31.813  7.722   -8.501  1.00 24.14 ? 250 PRO   B N   1 
ATOM   1952 C  CA  . PRO   A 1 250 ? 31.964  8.638   -9.632  1.00 24.13 ? 250 PRO   B CA  1 
ATOM   1953 C  C   . PRO   A 1 250 ? 33.220  8.319   -10.442 1.00 23.96 ? 250 PRO   B C   1 
ATOM   1954 O  O   . PRO   A 1 250 ? 34.176  7.758   -9.909  1.00 23.04 ? 250 PRO   B O   1 
ATOM   1955 C  CB  . PRO   A 1 250 ? 32.043  10.017  -8.960  1.00 27.63 ? 250 PRO   B CB  1 
ATOM   1956 C  CG  . PRO   A 1 250 ? 32.509  9.760   -7.523  1.00 27.59 ? 250 PRO   B CG  1 
ATOM   1957 C  CD  . PRO   A 1 250 ? 32.086  8.345   -7.183  1.00 24.25 ? 250 PRO   B CD  1 
ATOM   1958 N  N   . GLN   A 1 251 ? 33.207  8.660   -11.739 1.00 22.84 ? 251 GLN   B N   1 
ATOM   1959 C  CA  . GLN   A 1 251 ? 34.255  8.271   -12.678 1.00 22.27 ? 251 GLN   B CA  1 
ATOM   1960 C  C   . GLN   A 1 251 ? 34.955  9.521   -13.193 1.00 22.59 ? 251 GLN   B C   1 
ATOM   1961 O  O   . GLN   A 1 251 ? 34.372  10.595  -13.192 1.00 22.65 ? 251 GLN   B O   1 
ATOM   1962 C  CB  . GLN   A 1 251 ? 33.663  7.473   -13.842 1.00 21.58 ? 251 GLN   B CB  1 
ATOM   1963 C  CG  . GLN   A 1 251 ? 32.901  6.248   -13.386 1.00 23.28 ? 251 GLN   B CG  1 
ATOM   1964 C  CD  . GLN   A 1 251 ? 33.732  5.250   -12.616 1.00 25.04 ? 251 GLN   B CD  1 
ATOM   1965 O  OE1 . GLN   A 1 251 ? 33.313  4.752   -11.574 1.00 28.13 ? 251 GLN   B OE1 1 
ATOM   1966 N  NE2 . GLN   A 1 251 ? 34.911  4.945   -13.121 1.00 26.48 ? 251 GLN   B NE2 1 
ATOM   1967 N  N   . PRO   A 1 252 ? 36.207  9.448   -13.685 1.00 24.74 ? 252 PRO   B N   1 
ATOM   1968 C  CA  . PRO   A 1 252 ? 36.908  10.660  -14.104 1.00 25.90 ? 252 PRO   B CA  1 
ATOM   1969 C  C   . PRO   A 1 252 ? 36.269  11.320  -15.335 1.00 26.02 ? 252 PRO   B C   1 
ATOM   1970 O  O   . PRO   A 1 252 ? 35.810  10.635  -16.256 1.00 22.33 ? 252 PRO   B O   1 
ATOM   1971 C  CB  . PRO   A 1 252 ? 38.357  10.207  -14.356 1.00 27.70 ? 252 PRO   B CB  1 
ATOM   1972 C  CG  . PRO   A 1 252 ? 38.341  8.706   -14.411 1.00 25.64 ? 252 PRO   B CG  1 
ATOM   1973 C  CD  . PRO   A 1 252 ? 37.006  8.225   -13.875 1.00 27.58 ? 252 PRO   B CD  1 
ATOM   1974 N  N   . LEU   A 1 253 ? 36.232  12.661  -15.309 1.00 25.81 ? 253 LEU   B N   1 
ATOM   1975 C  CA  . LEU   A 1 253 ? 35.565  13.489  -16.304 1.00 28.78 ? 253 LEU   B CA  1 
ATOM   1976 C  C   . LEU   A 1 253 ? 36.274  13.392  -17.658 1.00 28.90 ? 253 LEU   B C   1 
ATOM   1977 O  O   . LEU   A 1 253 ? 35.640  13.434  -18.731 1.00 22.78 ? 253 LEU   B O   1 
ATOM   1978 C  CB  . LEU   A 1 253 ? 35.540  14.918  -15.742 1.00 29.46 ? 253 LEU   B CB  1 
ATOM   1979 C  CG  . LEU   A 1 253 ? 34.611  15.932  -16.414 1.00 31.20 ? 253 LEU   B CG  1 
ATOM   1980 C  CD1 . LEU   A 1 253 ? 33.212  15.381  -16.649 1.00 30.34 ? 253 LEU   B CD1 1 
ATOM   1981 C  CD2 . LEU   A 1 253 ? 34.538  17.220  -15.598 1.00 34.80 ? 253 LEU   B CD2 1 
ATOM   1982 N  N   . LYS   A 1 254 ? 37.609  13.276  -17.588 1.00 29.74 ? 254 LYS   B N   1 
ATOM   1983 C  CA  . LYS   A 1 254 ? 38.481  13.148  -18.746 1.00 27.17 ? 254 LYS   B CA  1 
ATOM   1984 C  C   . LYS   A 1 254 ? 38.152  14.196  -19.810 1.00 27.02 ? 254 LYS   B C   1 
ATOM   1985 O  O   . LYS   A 1 254 ? 38.108  13.888  -20.999 1.00 27.11 ? 254 LYS   B O   1 
ATOM   1986 C  CB  . LYS   A 1 254 ? 38.411  11.723  -19.297 1.00 30.35 ? 254 LYS   B CB  1 
ATOM   1987 C  CG  . LYS   A 1 254 ? 38.874  10.606  -18.370 1.00 33.86 ? 254 LYS   B CG  1 
ATOM   1988 C  CD  . LYS   A 1 254 ? 40.343  10.341  -18.420 1.00 37.94 ? 254 LYS   B CD  1 
ATOM   1989 C  CE  . LYS   A 1 254 ? 40.673  8.910   -18.047 1.00 45.79 ? 254 LYS   B CE  1 
ATOM   1990 N  NZ  . LYS   A 1 254 ? 39.872  7.948   -18.847 1.00 51.83 ? 254 LYS   B NZ  1 
ATOM   1991 N  N   . GLY   A 1 255 ? 37.905  15.443  -19.393 1.00 26.16 ? 255 GLY   B N   1 
ATOM   1992 C  CA  . GLY   A 1 255 ? 37.880  16.545  -20.345 1.00 27.39 ? 255 GLY   B CA  1 
ATOM   1993 C  C   . GLY   A 1 255 ? 36.526  16.804  -21.011 1.00 28.87 ? 255 GLY   B C   1 
ATOM   1994 O  O   . GLY   A 1 255 ? 36.406  17.693  -21.857 1.00 27.88 ? 255 GLY   B O   1 
ATOM   1995 N  N   . ARG   A 1 256 ? 35.504  16.039  -20.618 1.00 23.98 ? 256 ARG   B N   1 
ATOM   1996 C  CA  . ARG   A 1 256 ? 34.147  16.243  -21.104 1.00 22.90 ? 256 ARG   B CA  1 
ATOM   1997 C  C   . ARG   A 1 256 ? 33.614  17.544  -20.531 1.00 23.36 ? 256 ARG   B C   1 
ATOM   1998 O  O   . ARG   A 1 256 ? 34.056  17.993  -19.480 1.00 26.55 ? 256 ARG   B O   1 
ATOM   1999 C  CB  . ARG   A 1 256 ? 33.247  15.110  -20.608 1.00 21.33 ? 256 ARG   B CB  1 
ATOM   2000 C  CG  . ARG   A 1 256 ? 33.445  13.798  -21.338 1.00 23.06 ? 256 ARG   B CG  1 
ATOM   2001 C  CD  . ARG   A 1 256 ? 32.624  12.730  -20.665 1.00 23.09 ? 256 ARG   B CD  1 
ATOM   2002 N  NE  . ARG   A 1 256 ? 33.220  12.215  -19.430 1.00 20.33 ? 256 ARG   B NE  1 
ATOM   2003 C  CZ  . ARG   A 1 256 ? 32.630  11.312  -18.673 1.00 22.04 ? 256 ARG   B CZ  1 
ATOM   2004 N  NH1 . ARG   A 1 256 ? 31.427  10.849  -19.010 1.00 19.36 ? 256 ARG   B NH1 1 
ATOM   2005 N  NH2 . ARG   A 1 256 ? 33.251  10.854  -17.594 1.00 21.53 ? 256 ARG   B NH2 1 
ATOM   2006 N  N   . LYS   A 1 257 ? 32.659  18.154  -21.231 1.00 25.67 ? 257 LYS   B N   1 
ATOM   2007 C  CA  . LYS   A 1 257 ? 32.109  19.424  -20.795 1.00 24.97 ? 257 LYS   B CA  1 
ATOM   2008 C  C   . LYS   A 1 257 ? 30.743  19.169  -20.169 1.00 22.24 ? 257 LYS   B C   1 
ATOM   2009 O  O   . LYS   A 1 257 ? 29.904  18.515  -20.792 1.00 23.46 ? 257 LYS   B O   1 
ATOM   2010 C  CB  . LYS   A 1 257 ? 31.961  20.355  -22.001 1.00 28.88 ? 257 LYS   B CB  1 
ATOM   2011 C  CG  . LYS   A 1 257 ? 31.350  21.707  -21.662 1.00 35.05 ? 257 LYS   B CG  1 
ATOM   2012 C  CD  . LYS   A 1 257 ? 30.864  22.482  -22.878 1.00 37.95 ? 257 LYS   B CD  1 
ATOM   2013 C  CE  . LYS   A 1 257 ? 31.744  23.666  -23.213 1.00 47.26 ? 257 LYS   B CE  1 
ATOM   2014 N  NZ  . LYS   A 1 257 ? 31.182  24.439  -24.348 1.00 51.59 ? 257 LYS   B NZ  1 
ATOM   2015 N  N   . VAL   A 1 258 ? 30.563  19.613  -18.916 1.00 22.63 ? 258 VAL   B N   1 
ATOM   2016 C  CA  . VAL   A 1 258 ? 29.258  19.554  -18.267 1.00 23.54 ? 258 VAL   B CA  1 
ATOM   2017 C  C   . VAL   A 1 258 ? 28.575  20.902  -18.492 1.00 22.39 ? 258 VAL   B C   1 
ATOM   2018 O  O   . VAL   A 1 258 ? 29.164  21.948  -18.226 1.00 21.07 ? 258 VAL   B O   1 
ATOM   2019 C  CB  . VAL   A 1 258 ? 29.385  19.241  -16.762 1.00 24.01 ? 258 VAL   B CB  1 
ATOM   2020 C  CG1 . VAL   A 1 258 ? 28.018  19.079  -16.112 1.00 27.76 ? 258 VAL   B CG1 1 
ATOM   2021 C  CG2 . VAL   A 1 258 ? 30.230  18.002  -16.518 1.00 26.58 ? 258 VAL   B CG2 1 
ATOM   2022 N  N   . ARG   A 1 259 ? 27.346  20.888  -19.010 1.00 19.38 ? 259 ARG   B N   1 
ATOM   2023 C  CA  . ARG   A 1 259 ? 26.695  22.156  -19.318 1.00 20.60 ? 259 ARG   B CA  1 
ATOM   2024 C  C   . ARG   A 1 259 ? 25.443  22.318  -18.465 1.00 21.45 ? 259 ARG   B C   1 
ATOM   2025 O  O   . ARG   A 1 259 ? 24.875  21.320  -18.002 1.00 20.79 ? 259 ARG   B O   1 
ATOM   2026 C  CB  . ARG   A 1 259 ? 26.328  22.228  -20.808 1.00 19.77 ? 259 ARG   B CB  1 
ATOM   2027 C  CG  . ARG   A 1 259 ? 27.501  21.974  -21.740 1.00 18.72 ? 259 ARG   B CG  1 
ATOM   2028 C  CD  . ARG   A 1 259 ? 27.023  22.073  -23.188 1.00 21.24 ? 259 ARG   B CD  1 
ATOM   2029 N  NE  . ARG   A 1 259 ? 26.364  20.824  -23.577 1.00 23.08 ? 259 ARG   B NE  1 
ATOM   2030 C  CZ  . ARG   A 1 259 ? 25.500  20.670  -24.570 1.00 24.53 ? 259 ARG   B CZ  1 
ATOM   2031 N  NH1 . ARG   A 1 259 ? 25.109  21.716  -25.292 1.00 23.13 ? 259 ARG   B NH1 1 
ATOM   2032 N  NH2 . ARG   A 1 259 ? 25.006  19.463  -24.803 1.00 22.30 ? 259 ARG   B NH2 1 
ATOM   2033 N  N   . ALA   A 1 260 ? 25.051  23.583  -18.259 1.00 20.47 ? 260 ALA   B N   1 
ATOM   2034 C  CA  . ALA   A 1 260 ? 23.857  23.928  -17.501 1.00 23.18 ? 260 ALA   B CA  1 
ATOM   2035 C  C   . ALA   A 1 260 ? 22.841  24.646  -18.393 1.00 22.27 ? 260 ALA   B C   1 
ATOM   2036 O  O   . ALA   A 1 260 ? 23.217  25.412  -19.277 1.00 21.92 ? 260 ALA   B O   1 
ATOM   2037 C  CB  . ALA   A 1 260 ? 24.222  24.721  -16.258 1.00 21.65 ? 260 ALA   B CB  1 
ATOM   2038 N  N   . SER   A 1 261 ? 21.543  24.342  -18.171 1.00 23.11 ? 261 SER   B N   1 
ATOM   2039 C  CA  . SER   A 1 261 ? 20.420  24.895  -18.922 1.00 23.77 ? 261 SER   B CA  1 
ATOM   2040 C  C   . SER   A 1 261 ? 20.040  26.255  -18.355 1.00 26.59 ? 261 SER   B C   1 
ATOM   2041 O  O   . SER   A 1 261 ? 19.156  26.907  -18.905 1.00 26.17 ? 261 SER   B O   1 
ATOM   2042 C  CB  . SER   A 1 261 ? 19.179  24.015  -18.848 1.00 20.95 ? 261 SER   B CB  1 
ATOM   2043 O  OG  . SER   A 1 261 ? 18.670  23.991  -17.502 1.00 20.13 ? 261 SER   B OG  1 
ATOM   2044 N  N   . PHE   A 1 262 ? 20.658  26.625  -17.233 1.00 29.49 ? 262 PHE   B N   1 
ATOM   2045 C  CA  . PHE   A 1 262 ? 20.245  27.783  -16.451 1.00 31.67 ? 262 PHE   B CA  1 
ATOM   2046 C  C   . PHE   A 1 262 ? 21.482  28.541  -15.975 1.00 35.73 ? 262 PHE   B C   1 
ATOM   2047 O  O   . PHE   A 1 262 ? 22.554  27.964  -15.838 1.00 29.97 ? 262 PHE   B O   1 
ATOM   2048 C  CB  . PHE   A 1 262 ? 19.485  27.341  -15.194 1.00 27.58 ? 262 PHE   B CB  1 
ATOM   2049 C  CG  . PHE   A 1 262 ? 20.308  26.494  -14.257 1.00 29.90 ? 262 PHE   B CG  1 
ATOM   2050 C  CD1 . PHE   A 1 262 ? 20.447  25.130  -14.474 1.00 28.67 ? 262 PHE   B CD1 1 
ATOM   2051 C  CD2 . PHE   A 1 262 ? 20.962  27.057  -13.170 1.00 28.64 ? 262 PHE   B CD2 1 
ATOM   2052 C  CE1 . PHE   A 1 262 ? 21.233  24.356  -13.634 1.00 28.40 ? 262 PHE   B CE1 1 
ATOM   2053 C  CE2 . PHE   A 1 262 ? 21.747  26.282  -12.327 1.00 30.39 ? 262 PHE   B CE2 1 
ATOM   2054 C  CZ  . PHE   A 1 262 ? 21.880  24.933  -12.557 1.00 30.67 ? 262 PHE   B CZ  1 
ATOM   2055 N  N   . HIS   A 1 263 ? 21.283  29.829  -15.685 1.00 47.82 ? 263 HIS   B N   1 
ATOM   2056 C  CA  . HIS   A 1 263 ? 22.268  30.683  -15.037 1.00 60.65 ? 263 HIS   B CA  1 
ATOM   2057 C  C   . HIS   A 1 263 ? 21.558  31.523  -13.967 1.00 70.03 ? 263 HIS   B C   1 
ATOM   2058 O  O   . HIS   A 1 263 ? 22.217  32.175  -13.155 1.00 76.57 ? 263 HIS   B O   1 
ATOM   2059 C  CB  . HIS   A 1 263 ? 23.014  31.555  -16.068 1.00 66.18 ? 263 HIS   B CB  1 
ATOM   2060 C  CG  . HIS   A 1 263 ? 22.248  32.730  -16.592 1.00 73.85 ? 263 HIS   B CG  1 
ATOM   2061 N  ND1 . HIS   A 1 263 ? 20.978  32.614  -17.142 1.00 78.67 ? 263 HIS   B ND1 1 
ATOM   2062 C  CD2 . HIS   A 1 263 ? 22.576  34.039  -16.684 1.00 79.04 ? 263 HIS   B CD2 1 
ATOM   2063 C  CE1 . HIS   A 1 263 ? 20.552  33.803  -17.524 1.00 78.13 ? 263 HIS   B CE1 1 
ATOM   2064 N  NE2 . HIS   A 1 263 ? 21.516  34.696  -17.254 1.00 83.25 ? 263 HIS   B NE2 1 
ATOM   2065 O  OXT . HIS   A 1 263 ? 20.317  31.568  -13.894 1.00 72.64 ? 263 HIS   B OXT 1 
ATOM   2066 N  N   . LEU   B 1 5   ? -25.676 45.037  -27.149 1.00 61.81 ? 5   LEU   A N   1 
ATOM   2067 C  CA  . LEU   B 1 5   ? -24.189 44.986  -27.039 1.00 64.59 ? 5   LEU   A CA  1 
ATOM   2068 C  C   . LEU   B 1 5   ? -23.600 44.072  -28.116 1.00 64.69 ? 5   LEU   A C   1 
ATOM   2069 O  O   . LEU   B 1 5   ? -23.022 44.566  -29.087 1.00 69.58 ? 5   LEU   A O   1 
ATOM   2070 C  CB  . LEU   B 1 5   ? -23.816 44.495  -25.633 1.00 64.84 ? 5   LEU   A CB  1 
ATOM   2071 C  CG  . LEU   B 1 5   ? -22.327 44.484  -25.287 1.00 60.12 ? 5   LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   B 1 5   ? -21.994 45.612  -24.335 1.00 55.96 ? 5   LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   B 1 5   ? -21.940 43.158  -24.653 1.00 58.44 ? 5   LEU   A CD2 1 
ATOM   2074 N  N   . SER   B 1 6   ? -23.868 42.758  -27.985 1.00 56.80 ? 6   SER   A N   1 
ATOM   2075 C  CA  . SER   B 1 6   ? -22.840 41.717  -27.986 1.00 47.33 ? 6   SER   A CA  1 
ATOM   2076 C  C   . SER   B 1 6   ? -21.790 41.763  -29.097 1.00 42.21 ? 6   SER   A C   1 
ATOM   2077 O  O   . SER   B 1 6   ? -22.075 41.797  -30.291 1.00 46.47 ? 6   SER   A O   1 
ATOM   2078 C  CB  . SER   B 1 6   ? -23.315 40.342  -27.641 1.00 49.78 ? 6   SER   A CB  1 
ATOM   2079 O  OG  . SER   B 1 6   ? -22.831 40.019  -26.337 1.00 45.31 ? 6   SER   A OG  1 
ATOM   2080 N  N   . TRP   B 1 7   ? -20.544 41.684  -28.637 1.00 31.07 ? 7   TRP   A N   1 
ATOM   2081 C  CA  . TRP   B 1 7   ? -19.384 41.975  -29.448 1.00 26.85 ? 7   TRP   A CA  1 
ATOM   2082 C  C   . TRP   B 1 7   ? -19.034 40.737  -30.270 1.00 23.50 ? 7   TRP   A C   1 
ATOM   2083 O  O   . TRP   B 1 7   ? -19.370 39.610  -29.900 1.00 22.75 ? 7   TRP   A O   1 
ATOM   2084 C  CB  . TRP   B 1 7   ? -18.244 42.424  -28.527 1.00 24.98 ? 7   TRP   A CB  1 
ATOM   2085 C  CG  . TRP   B 1 7   ? -17.820 41.346  -27.575 1.00 24.32 ? 7   TRP   A CG  1 
ATOM   2086 C  CD1 . TRP   B 1 7   ? -18.342 41.059  -26.346 1.00 24.03 ? 7   TRP   A CD1 1 
ATOM   2087 C  CD2 . TRP   B 1 7   ? -16.820 40.345  -27.828 1.00 22.70 ? 7   TRP   A CD2 1 
ATOM   2088 N  NE1 . TRP   B 1 7   ? -17.696 39.978  -25.790 1.00 24.25 ? 7   TRP   A NE1 1 
ATOM   2089 C  CE2 . TRP   B 1 7   ? -16.759 39.518  -26.677 1.00 23.90 ? 7   TRP   A CE2 1 
ATOM   2090 C  CE3 . TRP   B 1 7   ? -15.964 40.091  -28.907 1.00 22.35 ? 7   TRP   A CE3 1 
ATOM   2091 C  CZ2 . TRP   B 1 7   ? -15.864 38.453  -26.575 1.00 22.87 ? 7   TRP   A CZ2 1 
ATOM   2092 C  CZ3 . TRP   B 1 7   ? -15.073 39.036  -28.804 1.00 22.18 ? 7   TRP   A CZ3 1 
ATOM   2093 C  CH2 . TRP   B 1 7   ? -15.039 38.222  -27.663 1.00 22.29 ? 7   TRP   A CH2 1 
ATOM   2094 N  N   . GLY   B 1 8   ? -18.298 40.959  -31.356 1.00 23.55 ? 8   GLY   A N   1 
ATOM   2095 C  CA  . GLY   B 1 8   ? -17.704 39.855  -32.101 1.00 21.42 ? 8   GLY   A CA  1 
ATOM   2096 C  C   . GLY   B 1 8   ? -16.691 40.400  -33.087 1.00 21.14 ? 8   GLY   A C   1 
ATOM   2097 O  O   . GLY   B 1 8   ? -15.996 41.355  -32.735 1.00 19.04 ? 8   GLY   A O   1 
ATOM   2098 N  N   . TYR   B 1 9   ? -16.647 39.815  -34.302 1.00 20.29 ? 9   TYR   A N   1 
ATOM   2099 C  CA  . TYR   B 1 9   ? -15.665 40.244  -35.287 1.00 21.05 ? 9   TYR   A CA  1 
ATOM   2100 C  C   . TYR   B 1 9   ? -16.306 40.673  -36.607 1.00 22.51 ? 9   TYR   A C   1 
ATOM   2101 O  O   . TYR   B 1 9   ? -15.596 40.896  -37.584 1.00 23.73 ? 9   TYR   A O   1 
ATOM   2102 C  CB  . TYR   B 1 9   ? -14.630 39.133  -35.478 1.00 19.61 ? 9   TYR   A CB  1 
ATOM   2103 C  CG  . TYR   B 1 9   ? -13.849 38.849  -34.214 1.00 18.28 ? 9   TYR   A CG  1 
ATOM   2104 C  CD1 . TYR   B 1 9   ? -12.728 39.594  -33.919 1.00 18.32 ? 9   TYR   A CD1 1 
ATOM   2105 C  CD2 . TYR   B 1 9   ? -14.228 37.858  -33.312 1.00 20.22 ? 9   TYR   A CD2 1 
ATOM   2106 C  CE1 . TYR   B 1 9   ? -11.994 39.389  -32.761 1.00 18.39 ? 9   TYR   A CE1 1 
ATOM   2107 C  CE2 . TYR   B 1 9   ? -13.486 37.610  -32.153 1.00 19.82 ? 9   TYR   A CE2 1 
ATOM   2108 C  CZ  . TYR   B 1 9   ? -12.367 38.392  -31.874 1.00 18.79 ? 9   TYR   A CZ  1 
ATOM   2109 O  OH  . TYR   B 1 9   ? -11.541 38.187  -30.799 1.00 18.46 ? 9   TYR   A OH  1 
ATOM   2110 N  N   . ARG   B 1 10  ? -17.641 40.762  -36.628 1.00 27.68 ? 10  ARG   A N   1 
ATOM   2111 C  CA  . ARG   B 1 10  ? -18.431 41.069  -37.816 1.00 31.29 ? 10  ARG   A CA  1 
ATOM   2112 C  C   . ARG   B 1 10  ? -18.427 42.587  -37.990 1.00 34.87 ? 10  ARG   A C   1 
ATOM   2113 O  O   . ARG   B 1 10  ? -17.785 43.284  -37.218 1.00 35.78 ? 10  ARG   A O   1 
ATOM   2114 C  CB  . ARG   B 1 10  ? -19.832 40.446  -37.690 1.00 33.10 ? 10  ARG   A CB  1 
ATOM   2115 C  CG  . ARG   B 1 10  ? -19.801 38.924  -37.581 1.00 38.48 ? 10  ARG   A CG  1 
ATOM   2116 C  CD  . ARG   B 1 10  ? -21.124 38.196  -37.393 1.00 45.37 ? 10  ARG   A CD  1 
ATOM   2117 N  NE  . ARG   B 1 10  ? -22.005 38.400  -38.542 1.00 52.14 ? 10  ARG   A NE  1 
ATOM   2118 C  CZ  . ARG   B 1 10  ? -23.293 38.050  -38.601 1.00 55.81 ? 10  ARG   A CZ  1 
ATOM   2119 N  NH1 . ARG   B 1 10  ? -23.882 37.452  -37.571 1.00 50.45 ? 10  ARG   A NH1 1 
ATOM   2120 N  NH2 . ARG   B 1 10  ? -23.980 38.297  -39.705 1.00 50.33 ? 10  ARG   A NH2 1 
ATOM   2121 N  N   . GLU   B 1 11  ? -19.145 43.113  -38.993 1.00 37.37 ? 11  GLU   A N   1 
ATOM   2122 C  CA  . GLU   B 1 11  ? -19.078 44.538  -39.311 1.00 36.85 ? 11  GLU   A CA  1 
ATOM   2123 C  C   . GLU   B 1 11  ? -19.646 45.395  -38.179 1.00 34.80 ? 11  GLU   A C   1 
ATOM   2124 O  O   . GLU   B 1 11  ? -19.045 46.401  -37.789 1.00 32.01 ? 11  GLU   A O   1 
ATOM   2125 C  CB  . GLU   B 1 11  ? -19.823 44.855  -40.615 1.00 43.27 ? 11  GLU   A CB  1 
ATOM   2126 N  N   . HIS   B 1 12  ? -20.809 45.005  -37.652 0.50 28.22 ? 12  HIS   A N   1 
ATOM   2127 C  CA  . HIS   B 1 12  ? -21.478 45.886  -36.712 0.50 28.17 ? 12  HIS   A CA  1 
ATOM   2128 C  C   . HIS   B 1 12  ? -21.028 45.677  -35.261 0.50 27.55 ? 12  HIS   A C   1 
ATOM   2129 O  O   . HIS   B 1 12  ? -21.351 46.487  -34.408 0.50 23.13 ? 12  HIS   A O   1 
ATOM   2130 C  CB  . HIS   B 1 12  ? -22.991 45.877  -36.970 0.50 29.94 ? 12  HIS   A CB  1 
ATOM   2131 C  CG  . HIS   B 1 12  ? -23.314 46.469  -38.303 0.50 33.48 ? 12  HIS   A CG  1 
ATOM   2132 N  ND1 . HIS   B 1 12  ? -22.602 47.539  -38.823 0.50 35.29 ? 12  HIS   A ND1 1 
ATOM   2133 C  CD2 . HIS   B 1 12  ? -24.236 46.143  -39.234 0.50 34.32 ? 12  HIS   A CD2 1 
ATOM   2134 C  CE1 . HIS   B 1 12  ? -23.075 47.847  -40.016 0.50 35.52 ? 12  HIS   A CE1 1 
ATOM   2135 N  NE2 . HIS   B 1 12  ? -24.084 47.011  -40.285 0.50 34.96 ? 12  HIS   A NE2 1 
ATOM   2136 N  N   . ASN   B 1 13  ? -20.233 44.632  -34.978 1.00 29.13 ? 13  ASN   A N   1 
ATOM   2137 C  CA  . ASN   B 1 13  ? -19.918 44.282  -33.593 1.00 27.72 ? 13  ASN   A CA  1 
ATOM   2138 C  C   . ASN   B 1 13  ? -18.417 44.059  -33.395 1.00 27.38 ? 13  ASN   A C   1 
ATOM   2139 O  O   . ASN   B 1 13  ? -18.008 43.530  -32.360 1.00 28.58 ? 13  ASN   A O   1 
ATOM   2140 C  CB  . ASN   B 1 13  ? -20.749 43.079  -33.131 1.00 27.33 ? 13  ASN   A CB  1 
ATOM   2141 C  CG  . ASN   B 1 13  ? -20.358 41.761  -33.770 1.00 25.74 ? 13  ASN   A CG  1 
ATOM   2142 O  OD1 . ASN   B 1 13  ? -19.463 41.698  -34.619 1.00 26.38 ? 13  ASN   A OD1 1 
ATOM   2143 N  ND2 . ASN   B 1 13  ? -21.007 40.689  -33.335 1.00 31.40 ? 13  ASN   A ND2 1 
ATOM   2144 N  N   . GLY   B 1 14  ? -17.606 44.488  -34.367 1.00 26.96 ? 14  GLY   A N   1 
ATOM   2145 C  CA  . GLY   B 1 14  ? -16.216 44.062  -34.444 1.00 27.58 ? 14  GLY   A CA  1 
ATOM   2146 C  C   . GLY   B 1 14  ? -15.266 45.038  -33.756 1.00 22.35 ? 14  GLY   A C   1 
ATOM   2147 O  O   . GLY   B 1 14  ? -15.691 46.084  -33.288 1.00 28.30 ? 14  GLY   A O   1 
ATOM   2148 N  N   . PRO   B 1 15  ? -13.951 44.721  -33.669 1.00 25.47 ? 15  PRO   A N   1 
ATOM   2149 C  CA  . PRO   B 1 15  ? -12.971 45.553  -32.964 1.00 23.95 ? 15  PRO   A CA  1 
ATOM   2150 C  C   . PRO   B 1 15  ? -13.086 47.084  -32.950 1.00 28.52 ? 15  PRO   A C   1 
ATOM   2151 O  O   . PRO   B 1 15  ? -12.926 47.688  -31.890 1.00 27.20 ? 15  PRO   A O   1 
ATOM   2152 C  CB  . PRO   B 1 15  ? -11.634 45.093  -33.539 1.00 23.95 ? 15  PRO   A CB  1 
ATOM   2153 C  CG  . PRO   B 1 15  ? -11.868 43.620  -33.894 1.00 23.58 ? 15  PRO   A CG  1 
ATOM   2154 C  CD  . PRO   B 1 15  ? -13.344 43.500  -34.235 1.00 23.22 ? 15  PRO   A CD  1 
ATOM   2155 N  N   . ILE   B 1 16  ? -13.345 47.715  -34.109 1.00 32.26 ? 16  ILE   A N   1 
ATOM   2156 C  CA  . ILE   B 1 16  ? -13.522 49.170  -34.181 1.00 36.82 ? 16  ILE   A CA  1 
ATOM   2157 C  C   . ILE   B 1 16  ? -14.641 49.632  -33.238 1.00 36.28 ? 16  ILE   A C   1 
ATOM   2158 O  O   . ILE   B 1 16  ? -14.610 50.757  -32.736 1.00 37.85 ? 16  ILE   A O   1 
ATOM   2159 C  CB  . ILE   B 1 16  ? -13.754 49.650  -35.647 1.00 41.13 ? 16  ILE   A CB  1 
ATOM   2160 C  CG1 . ILE   B 1 16  ? -13.487 51.149  -35.854 1.00 45.21 ? 16  ILE   A CG1 1 
ATOM   2161 C  CG2 . ILE   B 1 16  ? -15.152 49.302  -36.138 1.00 42.53 ? 16  ILE   A CG2 1 
ATOM   2162 C  CD1 . ILE   B 1 16  ? -12.048 51.512  -36.192 1.00 50.56 ? 16  ILE   A CD1 1 
ATOM   2163 N  N   . HIS   B 1 17  ? -15.647 48.770  -33.009 1.00 34.76 ? 17  HIS   A N   1 
ATOM   2164 C  CA  . HIS   B 1 17  ? -16.847 49.165  -32.283 1.00 34.39 ? 17  HIS   A CA  1 
ATOM   2165 C  C   . HIS   B 1 17  ? -16.713 48.933  -30.778 1.00 31.26 ? 17  HIS   A C   1 
ATOM   2166 O  O   . HIS   B 1 17  ? -17.487 49.480  -29.990 1.00 27.98 ? 17  HIS   A O   1 
ATOM   2167 C  CB  . HIS   B 1 17  ? -18.095 48.469  -32.867 1.00 38.04 ? 17  HIS   A CB  1 
ATOM   2168 C  CG  . HIS   B 1 17  ? -18.504 49.029  -34.194 1.00 49.81 ? 17  HIS   A CG  1 
ATOM   2169 N  ND1 . HIS   B 1 17  ? -18.944 50.339  -34.346 1.00 51.94 ? 17  HIS   A ND1 1 
ATOM   2170 C  CD2 . HIS   B 1 17  ? -18.526 48.482  -35.430 1.00 50.66 ? 17  HIS   A CD2 1 
ATOM   2171 C  CE1 . HIS   B 1 17  ? -19.218 50.566  -35.614 1.00 54.11 ? 17  HIS   A CE1 1 
ATOM   2172 N  NE2 . HIS   B 1 17  ? -18.968 49.441  -36.299 1.00 53.42 ? 17  HIS   A NE2 1 
ATOM   2173 N  N   . TRP   B 1 18  ? -15.734 48.104  -30.369 1.00 27.61 ? 18  TRP   A N   1 
ATOM   2174 C  CA  . TRP   B 1 18  ? -15.644 47.673  -28.978 1.00 23.28 ? 18  TRP   A CA  1 
ATOM   2175 C  C   . TRP   B 1 18  ? -15.558 48.848  -27.998 1.00 24.13 ? 18  TRP   A C   1 
ATOM   2176 O  O   . TRP   B 1 18  ? -16.047 48.746  -26.876 1.00 24.16 ? 18  TRP   A O   1 
ATOM   2177 C  CB  . TRP   B 1 18  ? -14.452 46.727  -28.797 1.00 21.23 ? 18  TRP   A CB  1 
ATOM   2178 C  CG  . TRP   B 1 18  ? -14.575 45.436  -29.540 1.00 19.93 ? 18  TRP   A CG  1 
ATOM   2179 C  CD1 . TRP   B 1 18  ? -15.687 44.930  -30.151 1.00 18.85 ? 18  TRP   A CD1 1 
ATOM   2180 C  CD2 . TRP   B 1 18  ? -13.543 44.434  -29.671 1.00 18.12 ? 18  TRP   A CD2 1 
ATOM   2181 N  NE1 . TRP   B 1 18  ? -15.412 43.680  -30.660 1.00 18.44 ? 18  TRP   A NE1 1 
ATOM   2182 C  CE2 . TRP   B 1 18  ? -14.112 43.347  -30.366 1.00 18.48 ? 18  TRP   A CE2 1 
ATOM   2183 C  CE3 . TRP   B 1 18  ? -12.203 44.353  -29.262 1.00 19.56 ? 18  TRP   A CE3 1 
ATOM   2184 C  CZ2 . TRP   B 1 18  ? -13.371 42.208  -30.693 1.00 16.06 ? 18  TRP   A CZ2 1 
ATOM   2185 C  CZ3 . TRP   B 1 18  ? -11.477 43.210  -29.559 1.00 17.47 ? 18  TRP   A CZ3 1 
ATOM   2186 C  CH2 . TRP   B 1 18  ? -12.058 42.161  -30.269 1.00 16.62 ? 18  TRP   A CH2 1 
ATOM   2187 N  N   . LYS   B 1 19  ? -14.910 49.943  -28.415 1.00 30.06 ? 19  LYS   A N   1 
ATOM   2188 C  CA  . LYS   B 1 19  ? -14.659 51.118  -27.582 1.00 31.87 ? 19  LYS   A CA  1 
ATOM   2189 C  C   . LYS   B 1 19  ? -15.964 51.766  -27.117 1.00 35.24 ? 19  LYS   A C   1 
ATOM   2190 O  O   . LYS   B 1 19  ? -16.016 52.377  -26.048 1.00 33.99 ? 19  LYS   A O   1 
ATOM   2191 C  CB  . LYS   B 1 19  ? -13.849 52.146  -28.374 1.00 34.70 ? 19  LYS   A CB  1 
ATOM   2192 C  CG  . LYS   B 1 19  ? -14.507 52.684  -29.641 1.00 40.38 ? 19  LYS   A CG  1 
ATOM   2193 C  CD  . LYS   B 1 19  ? -13.767 53.863  -30.284 1.00 46.92 ? 19  LYS   A CD  1 
ATOM   2194 C  CE  . LYS   B 1 19  ? -12.369 53.547  -30.788 1.00 49.25 ? 19  LYS   A CE  1 
ATOM   2195 N  NZ  . LYS   B 1 19  ? -12.344 52.693  -32.004 1.00 46.03 ? 19  LYS   A NZ  1 
ATOM   2196 N  N   . GLU   B 1 20  ? -17.025 51.604  -27.912 1.00 38.08 ? 20  GLU   A N   1 
ATOM   2197 C  CA  . GLU   B 1 20  ? -18.315 52.206  -27.600 1.00 42.31 ? 20  GLU   A CA  1 
ATOM   2198 C  C   . GLU   B 1 20  ? -18.870 51.639  -26.297 1.00 43.88 ? 20  GLU   A C   1 
ATOM   2199 O  O   . GLU   B 1 20  ? -19.662 52.295  -25.619 1.00 43.57 ? 20  GLU   A O   1 
ATOM   2200 C  CB  . GLU   B 1 20  ? -19.309 51.951  -28.732 1.00 48.24 ? 20  GLU   A CB  1 
ATOM   2201 C  CG  . GLU   B 1 20  ? -19.026 52.791  -29.964 1.00 48.79 ? 20  GLU   A CG  1 
ATOM   2202 C  CD  . GLU   B 1 20  ? -19.590 52.227  -31.257 1.00 55.29 ? 20  GLU   A CD  1 
ATOM   2203 O  OE1 . GLU   B 1 20  ? -20.626 51.512  -31.202 1.00 55.78 ? 20  GLU   A OE1 1 
ATOM   2204 O  OE2 . GLU   B 1 20  ? -18.989 52.496  -32.321 1.00 56.79 ? 20  GLU   A OE2 1 
ATOM   2205 N  N   . PHE   B 1 21  ? -18.452 50.416  -25.951 1.00 37.42 ? 21  PHE   A N   1 
ATOM   2206 C  CA  . PHE   B 1 21  ? -18.982 49.779  -24.762 1.00 36.56 ? 21  PHE   A CA  1 
ATOM   2207 C  C   . PHE   B 1 21  ? -17.876 49.451  -23.747 1.00 35.23 ? 21  PHE   A C   1 
ATOM   2208 O  O   . PHE   B 1 21  ? -18.177 49.169  -22.588 1.00 35.50 ? 21  PHE   A O   1 
ATOM   2209 C  CB  . PHE   B 1 21  ? -19.820 48.560  -25.159 1.00 43.19 ? 21  PHE   A CB  1 
ATOM   2210 C  CG  . PHE   B 1 21  ? -21.184 48.857  -25.742 1.00 49.89 ? 21  PHE   A CG  1 
ATOM   2211 C  CD1 . PHE   B 1 21  ? -21.350 49.097  -27.102 1.00 51.90 ? 21  PHE   A CD1 1 
ATOM   2212 C  CD2 . PHE   B 1 21  ? -22.316 48.875  -24.932 1.00 53.90 ? 21  PHE   A CD2 1 
ATOM   2213 C  CE1 . PHE   B 1 21  ? -22.608 49.357  -27.634 1.00 53.69 ? 21  PHE   A CE1 1 
ATOM   2214 C  CE2 . PHE   B 1 21  ? -23.575 49.119  -25.465 1.00 55.48 ? 21  PHE   A CE2 1 
ATOM   2215 C  CZ  . PHE   B 1 21  ? -23.718 49.364  -26.817 1.00 54.27 ? 21  PHE   A CZ  1 
ATOM   2216 N  N   . PHE   B 1 22  ? -16.606 49.430  -24.187 1.00 30.72 ? 22  PHE   A N   1 
ATOM   2217 C  CA  . PHE   B 1 22  ? -15.479 49.118  -23.314 1.00 30.78 ? 22  PHE   A CA  1 
ATOM   2218 C  C   . PHE   B 1 22  ? -14.395 50.171  -23.534 1.00 33.17 ? 22  PHE   A C   1 
ATOM   2219 O  O   . PHE   B 1 22  ? -13.525 49.999  -24.386 1.00 32.68 ? 22  PHE   A O   1 
ATOM   2220 C  CB  . PHE   B 1 22  ? -14.943 47.701  -23.580 1.00 28.79 ? 22  PHE   A CB  1 
ATOM   2221 C  CG  . PHE   B 1 22  ? -15.993 46.623  -23.524 1.00 27.76 ? 22  PHE   A CG  1 
ATOM   2222 C  CD1 . PHE   B 1 22  ? -16.313 46.008  -22.331 1.00 28.53 ? 22  PHE   A CD1 1 
ATOM   2223 C  CD2 . PHE   B 1 22  ? -16.687 46.247  -24.668 1.00 30.20 ? 22  PHE   A CD2 1 
ATOM   2224 C  CE1 . PHE   B 1 22  ? -17.305 45.041  -22.293 1.00 29.94 ? 22  PHE   A CE1 1 
ATOM   2225 C  CE2 . PHE   B 1 22  ? -17.673 45.274  -24.627 1.00 30.54 ? 22  PHE   A CE2 1 
ATOM   2226 C  CZ  . PHE   B 1 22  ? -17.985 44.676  -23.430 1.00 27.97 ? 22  PHE   A CZ  1 
ATOM   2227 N  N   . PRO   B 1 23  ? -14.420 51.309  -22.802 1.00 36.06 ? 23  PRO   A N   1 
ATOM   2228 C  CA  . PRO   B 1 23  ? -13.565 52.451  -23.148 1.00 35.47 ? 23  PRO   A CA  1 
ATOM   2229 C  C   . PRO   B 1 23  ? -12.075 52.185  -22.928 1.00 29.87 ? 23  PRO   A C   1 
ATOM   2230 O  O   . PRO   B 1 23  ? -11.226 52.916  -23.433 1.00 33.78 ? 23  PRO   A O   1 
ATOM   2231 C  CB  . PRO   B 1 23  ? -14.051 53.588  -22.222 1.00 34.22 ? 23  PRO   A CB  1 
ATOM   2232 C  CG  . PRO   B 1 23  ? -14.782 52.896  -21.086 1.00 37.55 ? 23  PRO   A CG  1 
ATOM   2233 C  CD  . PRO   B 1 23  ? -15.222 51.534  -21.589 1.00 35.96 ? 23  PRO   A CD  1 
ATOM   2234 N  N   . ILE   B 1 24  ? -11.760 51.143  -22.162 1.00 29.17 ? 24  ILE   A N   1 
ATOM   2235 C  CA  . ILE   B 1 24  ? -10.372 50.773  -21.943 1.00 28.66 ? 24  ILE   A CA  1 
ATOM   2236 C  C   . ILE   B 1 24  ? -9.753  50.293  -23.261 1.00 28.65 ? 24  ILE   A C   1 
ATOM   2237 O  O   . ILE   B 1 24  ? -8.523  50.149  -23.349 1.00 26.34 ? 24  ILE   A O   1 
ATOM   2238 C  CB  . ILE   B 1 24  ? -10.255 49.742  -20.801 1.00 28.90 ? 24  ILE   A CB  1 
ATOM   2239 C  CG1 . ILE   B 1 24  ? -8.853  49.684  -20.169 1.00 29.95 ? 24  ILE   A CG1 1 
ATOM   2240 C  CG2 . ILE   B 1 24  ? -10.711 48.368  -21.289 1.00 28.22 ? 24  ILE   A CG2 1 
ATOM   2241 C  CD1 . ILE   B 1 24  ? -8.372  50.957  -19.519 1.00 31.91 ? 24  ILE   A CD1 1 
ATOM   2242 N  N   . ALA   B 1 25  ? -10.599 50.077  -24.293 1.00 28.30 ? 25  ALA   A N   1 
ATOM   2243 C  CA  . ALA   B 1 25  ? -10.134 49.756  -25.637 1.00 27.96 ? 25  ALA   A CA  1 
ATOM   2244 C  C   . ALA   B 1 25  ? -9.086  50.760  -26.088 1.00 28.75 ? 25  ALA   A C   1 
ATOM   2245 O  O   . ALA   B 1 25  ? -8.192  50.388  -26.854 1.00 27.59 ? 25  ALA   A O   1 
ATOM   2246 C  CB  . ALA   B 1 25  ? -11.263 49.687  -26.638 1.00 28.52 ? 25  ALA   A CB  1 
ATOM   2247 N  N   . ASP   B 1 26  ? -9.215  52.019  -25.632 1.00 28.46 ? 26  ASP   A N   1 
ATOM   2248 C  CA  . ASP   B 1 26  ? -8.256  53.045  -26.018 1.00 32.01 ? 26  ASP   A CA  1 
ATOM   2249 C  C   . ASP   B 1 26  ? -7.267  53.328  -24.884 1.00 32.13 ? 26  ASP   A C   1 
ATOM   2250 O  O   . ASP   B 1 26  ? -6.694  54.413  -24.849 1.00 33.17 ? 26  ASP   A O   1 
ATOM   2251 C  CB  . ASP   B 1 26  ? -8.951  54.335  -26.488 1.00 37.91 ? 26  ASP   A CB  1 
ATOM   2252 C  CG  . ASP   B 1 26  ? -9.629  54.250  -27.850 1.00 47.29 ? 26  ASP   A CG  1 
ATOM   2253 O  OD1 . ASP   B 1 26  ? -9.260  53.354  -28.661 1.00 48.19 ? 26  ASP   A OD1 1 
ATOM   2254 O  OD2 . ASP   B 1 26  ? -10.528 55.089  -28.100 1.00 59.92 ? 26  ASP   A OD2 1 
ATOM   2255 N  N   . GLY   B 1 27  ? -7.058  52.354  -23.976 1.00 29.94 ? 27  GLY   A N   1 
ATOM   2256 C  CA  . GLY   B 1 27  ? -6.151  52.492  -22.840 1.00 26.43 ? 27  GLY   A CA  1 
ATOM   2257 C  C   . GLY   B 1 27  ? -4.663  52.534  -23.220 1.00 24.55 ? 27  GLY   A C   1 
ATOM   2258 O  O   . GLY   B 1 27  ? -4.302  52.546  -24.389 1.00 26.32 ? 27  GLY   A O   1 
ATOM   2259 N  N   . ASP   B 1 28  ? -3.812  52.564  -22.186 1.00 24.78 ? 28  ASP   A N   1 
ATOM   2260 C  CA  . ASP   B 1 28  ? -2.371  52.751  -22.263 1.00 23.27 ? 28  ASP   A CA  1 
ATOM   2261 C  C   . ASP   B 1 28  ? -1.650  51.405  -22.263 1.00 21.70 ? 28  ASP   A C   1 
ATOM   2262 O  O   . ASP   B 1 28  ? -0.456  51.343  -22.567 1.00 19.82 ? 28  ASP   A O   1 
ATOM   2263 C  CB  . ASP   B 1 28  ? -1.888  53.490  -21.020 1.00 26.38 ? 28  ASP   A CB  1 
ATOM   2264 C  CG  . ASP   B 1 28  ? -2.239  54.968  -21.110 1.00 29.57 ? 28  ASP   A CG  1 
ATOM   2265 O  OD1 . ASP   B 1 28  ? -2.479  55.441  -22.253 1.00 34.14 ? 28  ASP   A OD1 1 
ATOM   2266 O  OD2 . ASP   B 1 28  ? -2.308  55.612  -20.051 1.00 31.79 ? 28  ASP   A OD2 1 
ATOM   2267 N  N   . GLN   B 1 29  ? -2.380  50.328  -21.939 1.00 18.82 ? 29  GLN   A N   1 
ATOM   2268 C  CA  . GLN   B 1 29  ? -1.719  49.029  -21.886 1.00 18.66 ? 29  GLN   A CA  1 
ATOM   2269 C  C   . GLN   B 1 29  ? -2.563  48.003  -22.636 1.00 18.90 ? 29  GLN   A C   1 
ATOM   2270 O  O   . GLN   B 1 29  ? -2.808  46.906  -22.119 1.00 20.32 ? 29  GLN   A O   1 
ATOM   2271 C  CB  . GLN   B 1 29  ? -1.456  48.601  -20.431 1.00 22.46 ? 29  GLN   A CB  1 
ATOM   2272 C  CG  . GLN   B 1 29  ? -0.420  49.461  -19.676 1.00 24.45 ? 29  GLN   A CG  1 
ATOM   2273 C  CD  . GLN   B 1 29  ? 0.337   48.817  -18.532 1.00 28.09 ? 29  GLN   A CD  1 
ATOM   2274 O  OE1 . GLN   B 1 29  ? -0.064  47.785  -17.975 1.00 24.46 ? 29  GLN   A OE1 1 
ATOM   2275 N  NE2 . GLN   B 1 29  ? 1.440   49.450  -18.141 1.00 26.75 ? 29  GLN   A NE2 1 
ATOM   2276 N  N   . GLN   B 1 30  ? -2.939  48.326  -23.885 1.00 17.37 ? 30  GLN   A N   1 
ATOM   2277 C  CA  . GLN   B 1 30  ? -3.752  47.438  -24.703 1.00 17.19 ? 30  GLN   A CA  1 
ATOM   2278 C  C   . GLN   B 1 30  ? -2.881  46.490  -25.524 1.00 16.64 ? 30  GLN   A C   1 
ATOM   2279 O  O   . GLN   B 1 30  ? -1.720  46.780  -25.847 1.00 17.92 ? 30  GLN   A O   1 
ATOM   2280 C  CB  . GLN   B 1 30  ? -4.747  48.234  -25.562 1.00 16.98 ? 30  GLN   A CB  1 
ATOM   2281 C  CG  . GLN   B 1 30  ? -5.835  48.900  -24.714 1.00 17.13 ? 30  GLN   A CG  1 
ATOM   2282 C  CD  . GLN   B 1 30  ? -6.788  47.869  -24.159 1.00 17.32 ? 30  GLN   A CD  1 
ATOM   2283 O  OE1 . GLN   B 1 30  ? -7.559  47.275  -24.893 1.00 19.14 ? 30  GLN   A OE1 1 
ATOM   2284 N  NE2 . GLN   B 1 30  ? -6.726  47.614  -22.861 1.00 18.23 ? 30  GLN   A NE2 1 
ATOM   2285 N  N   . SER   B 1 31  ? -3.471  45.328  -25.823 1.00 16.87 ? 31  SER   A N   1 
ATOM   2286 C  CA  . SER   B 1 31  ? -2.838  44.249  -26.559 1.00 16.87 ? 31  SER   A CA  1 
ATOM   2287 C  C   . SER   B 1 31  ? -3.743  43.896  -27.727 1.00 16.91 ? 31  SER   A C   1 
ATOM   2288 O  O   . SER   B 1 31  ? -4.939  44.129  -27.675 1.00 17.19 ? 31  SER   A O   1 
ATOM   2289 C  CB  . SER   B 1 31  ? -2.663  43.008  -25.684 1.00 15.93 ? 31  SER   A CB  1 
ATOM   2290 O  OG  . SER   B 1 31  ? -1.694  43.248  -24.689 1.00 15.95 ? 31  SER   A OG  1 
ATOM   2291 N  N   . PRO   B 1 32  ? -3.245  43.252  -28.798 1.00 16.65 ? 32  PRO   A N   1 
ATOM   2292 C  CA  . PRO   B 1 32  ? -1.826  42.933  -28.946 1.00 16.50 ? 32  PRO   A CA  1 
ATOM   2293 C  C   . PRO   B 1 32  ? -1.005  44.146  -29.394 1.00 17.14 ? 32  PRO   A C   1 
ATOM   2294 O  O   . PRO   B 1 32  ? -1.534  45.247  -29.468 1.00 16.70 ? 32  PRO   A O   1 
ATOM   2295 C  CB  . PRO   B 1 32  ? -1.874  41.953  -30.122 1.00 15.12 ? 32  PRO   A CB  1 
ATOM   2296 C  CG  . PRO   B 1 32  ? -3.032  42.440  -30.986 1.00 13.48 ? 32  PRO   A CG  1 
ATOM   2297 C  CD  . PRO   B 1 32  ? -4.061  42.885  -29.973 1.00 15.27 ? 32  PRO   A CD  1 
ATOM   2298 N  N   . ILE   B 1 33  ? 0.265   43.920  -29.756 1.00 17.65 ? 33  ILE   A N   1 
ATOM   2299 C  CA  . ILE   B 1 33  ? 1.171   45.015  -30.110 1.00 18.91 ? 33  ILE   A CA  1 
ATOM   2300 C  C   . ILE   B 1 33  ? 2.023   44.586  -31.295 1.00 19.06 ? 33  ILE   A C   1 
ATOM   2301 O  O   . ILE   B 1 33  ? 2.065   43.403  -31.650 1.00 18.10 ? 33  ILE   A O   1 
ATOM   2302 C  CB  . ILE   B 1 33  ? 2.095   45.459  -28.943 1.00 18.38 ? 33  ILE   A CB  1 
ATOM   2303 C  CG1 . ILE   B 1 33  ? 3.019   44.327  -28.462 1.00 18.80 ? 33  ILE   A CG1 1 
ATOM   2304 C  CG2 . ILE   B 1 33  ? 1.316   46.125  -27.808 1.00 17.60 ? 33  ILE   A CG2 1 
ATOM   2305 C  CD1 . ILE   B 1 33  ? 4.119   44.759  -27.492 1.00 18.85 ? 33  ILE   A CD1 1 
ATOM   2306 N  N   . GLU   B 1 34  ? 2.743   45.572  -31.843 1.00 19.40 ? 34  GLU   A N   1 
ATOM   2307 C  CA  . GLU   B 1 34  ? 3.815   45.349  -32.790 1.00 21.47 ? 34  GLU   A CA  1 
ATOM   2308 C  C   . GLU   B 1 34  ? 5.117   45.290  -32.002 1.00 22.30 ? 34  GLU   A C   1 
ATOM   2309 O  O   . GLU   B 1 34  ? 5.410   46.164  -31.182 1.00 22.63 ? 34  GLU   A O   1 
ATOM   2310 C  CB  . GLU   B 1 34  ? 3.944   46.527  -33.773 1.00 23.88 ? 34  GLU   A CB  1 
ATOM   2311 C  CG  . GLU   B 1 34  ? 2.738   46.688  -34.687 1.00 27.87 ? 34  GLU   A CG  1 
ATOM   2312 C  CD  . GLU   B 1 34  ? 3.028   47.585  -35.887 1.00 34.05 ? 34  GLU   A CD  1 
ATOM   2313 O  OE1 . GLU   B 1 34  ? 3.648   47.079  -36.915 1.00 33.01 ? 34  GLU   A OE1 1 
ATOM   2314 O  OE2 . GLU   B 1 34  ? 2.673   48.790  -35.787 1.00 25.91 ? 34  GLU   A OE2 1 
ATOM   2315 N  N   . ILE   B 1 35  ? 5.916   44.275  -32.320 1.00 21.10 ? 35  ILE   A N   1 
ATOM   2316 C  CA  . ILE   B 1 35  ? 7.191   44.090  -31.655 1.00 22.48 ? 35  ILE   A CA  1 
ATOM   2317 C  C   . ILE   B 1 35  ? 8.273   44.470  -32.658 1.00 21.79 ? 35  ILE   A C   1 
ATOM   2318 O  O   . ILE   B 1 35  ? 8.411   43.801  -33.666 1.00 22.20 ? 35  ILE   A O   1 
ATOM   2319 C  CB  . ILE   B 1 35  ? 7.322   42.629  -31.155 1.00 22.75 ? 35  ILE   A CB  1 
ATOM   2320 C  CG1 . ILE   B 1 35  ? 6.319   42.351  -30.023 1.00 22.43 ? 35  ILE   A CG1 1 
ATOM   2321 C  CG2 . ILE   B 1 35  ? 8.746   42.340  -30.722 1.00 21.56 ? 35  ILE   A CG2 1 
ATOM   2322 C  CD1 . ILE   B 1 35  ? 6.063   40.879  -29.787 1.00 20.44 ? 35  ILE   A CD1 1 
ATOM   2323 N  N   . LYS   B 1 36  ? 8.972   45.568  -32.366 1.00 24.27 ? 36  LYS   A N   1 
ATOM   2324 C  CA  . LYS   B 1 36  ? 10.095  46.066  -33.148 1.00 26.89 ? 36  LYS   A CA  1 
ATOM   2325 C  C   . LYS   B 1 36  ? 11.385  45.570  -32.502 1.00 26.15 ? 36  LYS   A C   1 
ATOM   2326 O  O   . LYS   B 1 36  ? 11.869  46.155  -31.531 1.00 26.54 ? 36  LYS   A O   1 
ATOM   2327 C  CB  . LYS   B 1 36  ? 10.038  47.604  -33.148 1.00 30.42 ? 36  LYS   A CB  1 
ATOM   2328 C  CG  . LYS   B 1 36  ? 11.119  48.312  -33.967 1.00 33.40 ? 36  LYS   A CG  1 
ATOM   2329 C  CD  . LYS   B 1 36  ? 10.990  49.837  -34.013 1.00 36.96 ? 36  LYS   A CD  1 
ATOM   2330 C  CE  . LYS   B 1 36  ? 9.837   50.300  -34.890 1.00 37.70 ? 36  LYS   A CE  1 
ATOM   2331 N  NZ  . LYS   B 1 36  ? 9.898   51.751  -35.221 1.00 33.08 ? 36  LYS   A NZ  1 
ATOM   2332 N  N   . THR   B 1 37  ? 11.951  44.501  -33.066 1.00 28.22 ? 37  THR   A N   1 
ATOM   2333 C  CA  . THR   B 1 37  ? 12.990  43.741  -32.384 1.00 31.24 ? 37  THR   A CA  1 
ATOM   2334 C  C   . THR   B 1 37  ? 14.224  44.580  -32.045 1.00 37.70 ? 37  THR   A C   1 
ATOM   2335 O  O   . THR   B 1 37  ? 14.906  44.311  -31.060 1.00 39.16 ? 37  THR   A O   1 
ATOM   2336 C  CB  . THR   B 1 37  ? 13.335  42.446  -33.127 1.00 30.20 ? 37  THR   A CB  1 
ATOM   2337 O  OG1 . THR   B 1 37  ? 13.837  42.695  -34.442 1.00 31.85 ? 37  THR   A OG1 1 
ATOM   2338 C  CG2 . THR   B 1 37  ? 12.162  41.500  -33.184 1.00 28.39 ? 37  THR   A CG2 1 
ATOM   2339 N  N   . LYS   B 1 38  ? 14.539  45.595  -32.852 1.00 39.15 ? 38  LYS   A N   1 
ATOM   2340 C  CA  . LYS   B 1 38  ? 15.810  46.255  -32.602 1.00 42.99 ? 38  LYS   A CA  1 
ATOM   2341 C  C   . LYS   B 1 38  ? 15.657  47.330  -31.524 1.00 43.80 ? 38  LYS   A C   1 
ATOM   2342 O  O   . LYS   B 1 38  ? 16.649  47.939  -31.139 1.00 46.52 ? 38  LYS   A O   1 
ATOM   2343 C  CB  . LYS   B 1 38  ? 16.510  46.677  -33.904 1.00 47.04 ? 38  LYS   A CB  1 
ATOM   2344 C  CG  . LYS   B 1 38  ? 15.869  47.834  -34.657 1.00 42.19 ? 38  LYS   A CG  1 
ATOM   2345 N  N   . GLU   B 1 39  ? 14.448  47.532  -30.980 1.00 41.83 ? 39  GLU   A N   1 
ATOM   2346 C  CA  . GLU   B 1 39  ? 14.355  48.415  -29.820 1.00 46.11 ? 39  GLU   A CA  1 
ATOM   2347 C  C   . GLU   B 1 39  ? 14.040  47.648  -28.528 1.00 42.74 ? 39  GLU   A C   1 
ATOM   2348 O  O   . GLU   B 1 39  ? 13.814  48.245  -27.479 1.00 41.69 ? 39  GLU   A O   1 
ATOM   2349 C  CB  . GLU   B 1 39  ? 13.468  49.640  -30.084 1.00 55.30 ? 39  GLU   A CB  1 
ATOM   2350 C  CG  . GLU   B 1 39  ? 14.087  50.636  -31.066 1.00 66.90 ? 39  GLU   A CG  1 
ATOM   2351 C  CD  . GLU   B 1 39  ? 15.300  51.463  -30.640 1.00 72.27 ? 39  GLU   A CD  1 
ATOM   2352 O  OE1 . GLU   B 1 39  ? 15.238  52.709  -30.786 1.00 72.13 ? 39  GLU   A OE1 1 
ATOM   2353 O  OE2 . GLU   B 1 39  ? 16.323  50.873  -30.197 1.00 71.66 ? 39  GLU   A OE2 1 
ATOM   2354 N  N   . VAL   B 1 40  ? 14.057  46.313  -28.599 1.00 35.10 ? 40  VAL   A N   1 
ATOM   2355 C  CA  . VAL   B 1 40  ? 13.789  45.477  -27.443 1.00 32.84 ? 40  VAL   A CA  1 
ATOM   2356 C  C   . VAL   B 1 40  ? 15.106  45.203  -26.730 1.00 32.31 ? 40  VAL   A C   1 
ATOM   2357 O  O   . VAL   B 1 40  ? 16.071  44.813  -27.376 1.00 33.86 ? 40  VAL   A O   1 
ATOM   2358 C  CB  . VAL   B 1 40  ? 13.131  44.160  -27.886 1.00 31.88 ? 40  VAL   A CB  1 
ATOM   2359 C  CG1 . VAL   B 1 40  ? 13.109  43.148  -26.756 1.00 33.26 ? 40  VAL   A CG1 1 
ATOM   2360 C  CG2 . VAL   B 1 40  ? 11.732  44.401  -28.436 1.00 32.08 ? 40  VAL   A CG2 1 
ATOM   2361 N  N   . LYS   B 1 41  ? 15.111  45.342  -25.399 1.00 34.06 ? 41  LYS   A N   1 
ATOM   2362 C  CA  . LYS   B 1 41  ? 16.302  45.110  -24.592 1.00 34.35 ? 41  LYS   A CA  1 
ATOM   2363 C  C   . LYS   B 1 41  ? 16.262  43.700  -24.007 1.00 30.40 ? 41  LYS   A C   1 
ATOM   2364 O  O   . LYS   B 1 41  ? 15.246  43.292  -23.448 1.00 24.41 ? 41  LYS   A O   1 
ATOM   2365 C  CB  . LYS   B 1 41  ? 16.350  46.078  -23.400 1.00 36.34 ? 41  LYS   A CB  1 
ATOM   2366 C  CG  . LYS   B 1 41  ? 16.953  47.455  -23.674 1.00 36.78 ? 41  LYS   A CG  1 
ATOM   2367 N  N   . TYR   B 1 42  ? 17.392  42.987  -24.098 1.00 26.86 ? 42  TYR   A N   1 
ATOM   2368 C  CA  . TYR   B 1 42  ? 17.581  41.782  -23.309 1.00 28.98 ? 42  TYR   A CA  1 
ATOM   2369 C  C   . TYR   B 1 42  ? 17.621  42.172  -21.831 1.00 28.06 ? 42  TYR   A C   1 
ATOM   2370 O  O   . TYR   B 1 42  ? 18.305  43.120  -21.463 1.00 25.20 ? 42  TYR   A O   1 
ATOM   2371 C  CB  . TYR   B 1 42  ? 18.859  41.066  -23.744 1.00 26.70 ? 42  TYR   A CB  1 
ATOM   2372 C  CG  . TYR   B 1 42  ? 19.349  40.030  -22.763 1.00 27.24 ? 42  TYR   A CG  1 
ATOM   2373 C  CD1 . TYR   B 1 42  ? 18.612  38.877  -22.517 1.00 26.44 ? 42  TYR   A CD1 1 
ATOM   2374 C  CD2 . TYR   B 1 42  ? 20.566  40.177  -22.102 1.00 28.88 ? 42  TYR   A CD2 1 
ATOM   2375 C  CE1 . TYR   B 1 42  ? 19.045  37.904  -21.637 1.00 27.36 ? 42  TYR   A CE1 1 
ATOM   2376 C  CE2 . TYR   B 1 42  ? 21.021  39.204  -21.220 1.00 32.03 ? 42  TYR   A CE2 1 
ATOM   2377 C  CZ  . TYR   B 1 42  ? 20.259  38.068  -20.989 1.00 32.21 ? 42  TYR   A CZ  1 
ATOM   2378 O  OH  . TYR   B 1 42  ? 20.687  37.115  -20.114 1.00 33.64 ? 42  TYR   A OH  1 
ATOM   2379 N  N   . ASP   B 1 43  ? 16.888  41.433  -20.989 1.00 25.64 ? 43  ASP   A N   1 
ATOM   2380 C  CA  . ASP   B 1 43  ? 16.855  41.680  -19.552 1.00 29.14 ? 43  ASP   A CA  1 
ATOM   2381 C  C   . ASP   B 1 43  ? 17.395  40.461  -18.797 1.00 28.58 ? 43  ASP   A C   1 
ATOM   2382 O  O   . ASP   B 1 43  ? 16.741  39.412  -18.744 1.00 22.94 ? 43  ASP   A O   1 
ATOM   2383 C  CB  . ASP   B 1 43  ? 15.455  42.076  -19.062 1.00 28.61 ? 43  ASP   A CB  1 
ATOM   2384 C  CG  . ASP   B 1 43  ? 15.380  42.428  -17.582 1.00 33.02 ? 43  ASP   A CG  1 
ATOM   2385 O  OD1 . ASP   B 1 43  ? 16.365  42.171  -16.857 1.00 32.01 ? 43  ASP   A OD1 1 
ATOM   2386 O  OD2 . ASP   B 1 43  ? 14.339  42.988  -17.164 1.00 34.15 ? 43  ASP   A OD2 1 
ATOM   2387 N  N   . SER   B 1 44  ? 18.555  40.638  -18.139 1.00 27.13 ? 44  SER   A N   1 
ATOM   2388 C  CA  . SER   B 1 44  ? 19.252  39.511  -17.527 1.00 31.20 ? 44  SER   A CA  1 
ATOM   2389 C  C   . SER   B 1 44  ? 18.645  39.154  -16.172 1.00 29.34 ? 44  SER   A C   1 
ATOM   2390 O  O   . SER   B 1 44  ? 18.975  38.114  -15.609 1.00 36.71 ? 44  SER   A O   1 
ATOM   2391 C  CB  . SER   B 1 44  ? 20.732  39.778  -17.409 1.00 35.66 ? 44  SER   A CB  1 
ATOM   2392 O  OG  . SER   B 1 44  ? 20.933  40.929  -16.607 1.00 37.12 ? 44  SER   A OG  1 
ATOM   2393 N  N   . SER   B 1 45  ? 17.715  39.989  -15.687 1.00 28.88 ? 45  SER   A N   1 
ATOM   2394 C  CA  . SER   B 1 45  ? 17.007  39.728  -14.448 1.00 28.09 ? 45  SER   A CA  1 
ATOM   2395 C  C   . SER   B 1 45  ? 15.837  38.751  -14.644 1.00 31.36 ? 45  SER   A C   1 
ATOM   2396 O  O   . SER   B 1 45  ? 15.295  38.237  -13.671 1.00 30.45 ? 45  SER   A O   1 
ATOM   2397 C  CB  . SER   B 1 45  ? 16.586  41.020  -13.788 1.00 31.40 ? 45  SER   A CB  1 
ATOM   2398 O  OG  . SER   B 1 45  ? 15.411  41.546  -14.384 1.00 29.35 ? 45  SER   A OG  1 
ATOM   2399 N  N   . LEU   B 1 46  ? 15.458  38.462  -15.899 1.00 28.04 ? 46  LEU   A N   1 
ATOM   2400 C  CA  . LEU   B 1 46  ? 14.438  37.448  -16.138 1.00 28.15 ? 46  LEU   A CA  1 
ATOM   2401 C  C   . LEU   B 1 46  ? 14.974  36.091  -15.692 1.00 30.40 ? 46  LEU   A C   1 
ATOM   2402 O  O   . LEU   B 1 46  ? 16.103  35.746  -16.028 1.00 29.71 ? 46  LEU   A O   1 
ATOM   2403 C  CB  . LEU   B 1 46  ? 14.097  37.430  -17.630 1.00 23.09 ? 46  LEU   A CB  1 
ATOM   2404 C  CG  . LEU   B 1 46  ? 13.376  38.673  -18.150 1.00 21.37 ? 46  LEU   A CG  1 
ATOM   2405 C  CD1 . LEU   B 1 46  ? 13.327  38.644  -19.680 1.00 20.82 ? 46  LEU   A CD1 1 
ATOM   2406 C  CD2 . LEU   B 1 46  ? 11.967  38.744  -17.564 1.00 24.77 ? 46  LEU   A CD2 1 
ATOM   2407 N  N   . ARG   B 1 47  ? 14.149  35.344  -14.939 1.00 28.98 ? 47  ARG   A N   1 
ATOM   2408 C  CA  . ARG   B 1 47  ? 14.479  34.019  -14.433 1.00 29.71 ? 47  ARG   A CA  1 
ATOM   2409 C  C   . ARG   B 1 47  ? 14.148  32.970  -15.491 1.00 28.16 ? 47  ARG   A C   1 
ATOM   2410 O  O   . ARG   B 1 47  ? 13.362  33.224  -16.405 1.00 26.47 ? 47  ARG   A O   1 
ATOM   2411 C  CB  . ARG   B 1 47  ? 13.695  33.714  -13.142 1.00 30.99 ? 47  ARG   A CB  1 
ATOM   2412 C  CG  . ARG   B 1 47  ? 13.989  34.631  -11.956 1.00 40.30 ? 47  ARG   A CG  1 
ATOM   2413 C  CD  . ARG   B 1 47  ? 15.444  34.713  -11.506 1.00 45.50 ? 47  ARG   A CD  1 
ATOM   2414 N  NE  . ARG   B 1 47  ? 15.994  33.392  -11.200 1.00 61.87 ? 47  ARG   A NE  1 
ATOM   2415 C  CZ  . ARG   B 1 47  ? 17.219  32.960  -11.516 1.00 66.30 ? 47  ARG   A CZ  1 
ATOM   2416 N  NH1 . ARG   B 1 47  ? 17.586  31.731  -11.191 1.00 65.80 ? 47  ARG   A NH1 1 
ATOM   2417 N  NH2 . ARG   B 1 47  ? 18.062  33.741  -12.172 1.00 67.07 ? 47  ARG   A NH2 1 
ATOM   2418 N  N   . PRO   B 1 48  ? 14.709  31.739  -15.414 1.00 27.16 ? 48  PRO   A N   1 
ATOM   2419 C  CA  . PRO   B 1 48  ? 14.350  30.700  -16.381 1.00 27.60 ? 48  PRO   A CA  1 
ATOM   2420 C  C   . PRO   B 1 48  ? 12.831  30.521  -16.418 1.00 26.03 ? 48  PRO   A C   1 
ATOM   2421 O  O   . PRO   B 1 48  ? 12.161  30.593  -15.399 1.00 21.48 ? 48  PRO   A O   1 
ATOM   2422 C  CB  . PRO   B 1 48  ? 15.041  29.452  -15.811 1.00 29.94 ? 48  PRO   A CB  1 
ATOM   2423 C  CG  . PRO   B 1 48  ? 16.227  30.017  -15.057 1.00 27.45 ? 48  PRO   A CG  1 
ATOM   2424 C  CD  . PRO   B 1 48  ? 15.692  31.279  -14.409 1.00 28.50 ? 48  PRO   A CD  1 
ATOM   2425 N  N   . LEU   B 1 49  ? 12.275  30.341  -17.611 1.00 23.51 ? 49  LEU   A N   1 
ATOM   2426 C  CA  . LEU   B 1 49  ? 10.838  30.187  -17.684 1.00 25.71 ? 49  LEU   A CA  1 
ATOM   2427 C  C   . LEU   B 1 49  ? 10.520  28.709  -17.477 1.00 27.00 ? 49  LEU   A C   1 
ATOM   2428 O  O   . LEU   B 1 49  ? 11.111  27.875  -18.178 1.00 26.57 ? 49  LEU   A O   1 
ATOM   2429 C  CB  . LEU   B 1 49  ? 10.399  30.642  -19.072 1.00 22.79 ? 49  LEU   A CB  1 
ATOM   2430 C  CG  . LEU   B 1 49  ? 8.894   30.731  -19.286 1.00 23.61 ? 49  LEU   A CG  1 
ATOM   2431 C  CD1 . LEU   B 1 49  ? 8.342   31.965  -18.617 1.00 20.63 ? 49  LEU   A CD1 1 
ATOM   2432 C  CD2 . LEU   B 1 49  ? 8.608   30.748  -20.786 1.00 24.43 ? 49  LEU   A CD2 1 
ATOM   2433 N  N   . SER   B 1 50  ? 9.601   28.422  -16.532 1.00 23.67 ? 50  SER   A N   1 
ATOM   2434 C  CA  . SER   B 1 50  ? 9.219   27.052  -16.188 1.00 21.01 ? 50  SER   A CA  1 
ATOM   2435 C  C   . SER   B 1 50  ? 7.797   26.768  -16.674 1.00 22.78 ? 50  SER   A C   1 
ATOM   2436 O  O   . SER   B 1 50  ? 6.853   27.462  -16.286 1.00 18.16 ? 50  SER   A O   1 
ATOM   2437 C  CB  . SER   B 1 50  ? 9.391   26.831  -14.693 1.00 24.61 ? 50  SER   A CB  1 
ATOM   2438 O  OG  . SER   B 1 50  ? 8.856   25.588  -14.230 1.00 21.30 ? 50  SER   A OG  1 
ATOM   2439 N  N   . ILE   B 1 51  ? 7.650   25.741  -17.526 1.00 19.92 ? 51  ILE   A N   1 
ATOM   2440 C  CA  . ILE   B 1 51  ? 6.331   25.395  -18.023 1.00 21.99 ? 51  ILE   A CA  1 
ATOM   2441 C  C   . ILE   B 1 51  ? 6.109   23.924  -17.717 1.00 26.06 ? 51  ILE   A C   1 
ATOM   2442 O  O   . ILE   B 1 51  ? 6.847   23.092  -18.209 1.00 25.21 ? 51  ILE   A O   1 
ATOM   2443 C  CB  . ILE   B 1 51  ? 6.163   25.706  -19.537 1.00 22.10 ? 51  ILE   A CB  1 
ATOM   2444 C  CG1 . ILE   B 1 51  ? 6.559   27.142  -19.896 1.00 22.33 ? 51  ILE   A CG1 1 
ATOM   2445 C  CG2 . ILE   B 1 51  ? 4.744   25.422  -20.011 1.00 22.09 ? 51  ILE   A CG2 1 
ATOM   2446 C  CD1 . ILE   B 1 51  ? 6.376   27.491  -21.394 1.00 20.79 ? 51  ILE   A CD1 1 
ATOM   2447 N  N   . LYS   B 1 52  ? 5.068   23.620  -16.939 1.00 26.15 ? 52  LYS   A N   1 
ATOM   2448 C  CA  . LYS   B 1 52  ? 4.742   22.240  -16.620 1.00 28.28 ? 52  LYS   A CA  1 
ATOM   2449 C  C   . LYS   B 1 52  ? 3.257   22.063  -16.904 1.00 24.26 ? 52  LYS   A C   1 
ATOM   2450 O  O   . LYS   B 1 52  ? 2.437   22.669  -16.199 1.00 24.30 ? 52  LYS   A O   1 
ATOM   2451 C  CB  . LYS   B 1 52  ? 5.028   21.954  -15.141 1.00 31.18 ? 52  LYS   A CB  1 
ATOM   2452 C  CG  . LYS   B 1 52  ? 4.896   20.492  -14.691 1.00 41.32 ? 52  LYS   A CG  1 
ATOM   2453 C  CD  . LYS   B 1 52  ? 4.666   20.322  -13.184 1.00 44.93 ? 52  LYS   A CD  1 
ATOM   2454 C  CE  . LYS   B 1 52  ? 4.274   18.924  -12.723 1.00 46.74 ? 52  LYS   A CE  1 
ATOM   2455 N  NZ  . LYS   B 1 52  ? 2.898   18.533  -13.132 1.00 43.87 ? 52  LYS   A NZ  1 
ATOM   2456 N  N   . TYR   B 1 53  ? 2.938   21.312  -17.962 1.00 19.60 ? 53  TYR   A N   1 
ATOM   2457 C  CA  . TYR   B 1 53  ? 1.544   21.055  -18.283 1.00 17.61 ? 53  TYR   A CA  1 
ATOM   2458 C  C   . TYR   B 1 53  ? 1.289   19.554  -18.271 1.00 18.64 ? 53  TYR   A C   1 
ATOM   2459 O  O   . TYR   B 1 53  ? 1.988   18.784  -18.923 1.00 18.16 ? 53  TYR   A O   1 
ATOM   2460 C  CB  . TYR   B 1 53  ? 1.144   21.596  -19.653 1.00 15.17 ? 53  TYR   A CB  1 
ATOM   2461 C  CG  . TYR   B 1 53  ? 1.251   23.083  -19.869 1.00 13.77 ? 53  TYR   A CG  1 
ATOM   2462 C  CD1 . TYR   B 1 53  ? 0.954   23.998  -18.870 1.00 13.06 ? 53  TYR   A CD1 1 
ATOM   2463 C  CD2 . TYR   B 1 53  ? 1.603   23.566  -21.116 1.00 12.80 ? 53  TYR   A CD2 1 
ATOM   2464 C  CE1 . TYR   B 1 53  ? 1.039   25.362  -19.112 1.00 12.88 ? 53  TYR   A CE1 1 
ATOM   2465 C  CE2 . TYR   B 1 53  ? 1.681   24.923  -21.373 1.00 12.06 ? 53  TYR   A CE2 1 
ATOM   2466 C  CZ  . TYR   B 1 53  ? 1.398   25.822  -20.365 1.00 11.86 ? 53  TYR   A CZ  1 
ATOM   2467 O  OH  . TYR   B 1 53  ? 1.514   27.150  -20.627 1.00 10.69 ? 53  TYR   A OH  1 
ATOM   2468 N  N   . ASP   B 1 54  ? 0.254   19.173  -17.528 1.00 21.12 ? 54  ASP   A N   1 
ATOM   2469 C  CA  . ASP   B 1 54  ? -0.131  17.780  -17.338 1.00 22.57 ? 54  ASP   A CA  1 
ATOM   2470 C  C   . ASP   B 1 54  ? -1.251  17.441  -18.317 1.00 20.54 ? 54  ASP   A C   1 
ATOM   2471 O  O   . ASP   B 1 54  ? -2.267  18.114  -18.323 1.00 19.29 ? 54  ASP   A O   1 
ATOM   2472 C  CB  . ASP   B 1 54  ? -0.595  17.599  -15.896 1.00 25.51 ? 54  ASP   A CB  1 
ATOM   2473 C  CG  . ASP   B 1 54  ? -0.843  16.166  -15.483 1.00 28.63 ? 54  ASP   A CG  1 
ATOM   2474 O  OD1 . ASP   B 1 54  ? -1.365  15.387  -16.299 1.00 28.61 ? 54  ASP   A OD1 1 
ATOM   2475 O  OD2 . ASP   B 1 54  ? -0.586  15.880  -14.318 1.00 32.37 ? 54  ASP   A OD2 1 
ATOM   2476 N  N   . PRO   B 1 55  ? -1.112  16.443  -19.217 1.00 22.47 ? 55  PRO   A N   1 
ATOM   2477 C  CA  . PRO   B 1 55  ? -2.206  16.101  -20.142 1.00 23.36 ? 55  PRO   A CA  1 
ATOM   2478 C  C   . PRO   B 1 55  ? -3.558  15.759  -19.515 1.00 25.27 ? 55  PRO   A C   1 
ATOM   2479 O  O   . PRO   B 1 55  ? -4.588  15.880  -20.184 1.00 25.70 ? 55  PRO   A O   1 
ATOM   2480 C  CB  . PRO   B 1 55  ? -1.645  14.886  -20.908 1.00 24.57 ? 55  PRO   A CB  1 
ATOM   2481 C  CG  . PRO   B 1 55  ? -0.146  15.127  -20.875 1.00 25.61 ? 55  PRO   A CG  1 
ATOM   2482 C  CD  . PRO   B 1 55  ? 0.106   15.636  -19.464 1.00 22.18 ? 55  PRO   A CD  1 
ATOM   2483 N  N   . SER   B 1 56  ? -3.570  15.390  -18.223 1.00 23.16 ? 56  SER   A N   1 
ATOM   2484 C  CA  . SER   B 1 56  ? -4.825  15.029  -17.581 1.00 25.44 ? 56  SER   A CA  1 
ATOM   2485 C  C   . SER   B 1 56  ? -5.592  16.269  -17.109 1.00 25.49 ? 56  SER   A C   1 
ATOM   2486 O  O   . SER   B 1 56  ? -6.716  16.145  -16.634 1.00 25.75 ? 56  SER   A O   1 
ATOM   2487 C  CB  . SER   B 1 56  ? -4.616  14.060  -16.439 1.00 30.31 ? 56  SER   A CB  1 
ATOM   2488 O  OG  . SER   B 1 56  ? -3.842  14.651  -15.404 1.00 30.90 ? 56  SER   A OG  1 
ATOM   2489 N  N   . SER   B 1 57  ? -4.989  17.459  -17.228 1.00 21.49 ? 57  SER   A N   1 
ATOM   2490 C  CA  . SER   B 1 57  ? -5.658  18.685  -16.803 1.00 22.08 ? 57  SER   A CA  1 
ATOM   2491 C  C   . SER   B 1 57  ? -6.794  19.091  -17.759 1.00 20.90 ? 57  SER   A C   1 
ATOM   2492 O  O   . SER   B 1 57  ? -7.733  19.781  -17.339 1.00 23.23 ? 57  SER   A O   1 
ATOM   2493 C  CB  . SER   B 1 57  ? -4.656  19.823  -16.684 1.00 21.40 ? 57  SER   A CB  1 
ATOM   2494 O  OG  . SER   B 1 57  ? -3.796  19.604  -15.574 1.00 25.85 ? 57  SER   A OG  1 
ATOM   2495 N  N   . ALA   B 1 58  ? -6.707  18.726  -19.045 1.00 20.87 ? 58  ALA   A N   1 
ATOM   2496 C  CA  . ALA   B 1 58  ? -7.683  19.191  -20.028 1.00 19.13 ? 58  ALA   A CA  1 
ATOM   2497 C  C   . ALA   B 1 58  ? -9.016  18.496  -19.748 1.00 21.33 ? 58  ALA   A C   1 
ATOM   2498 O  O   . ALA   B 1 58  ? -9.010  17.304  -19.415 1.00 20.80 ? 58  ALA   A O   1 
ATOM   2499 C  CB  . ALA   B 1 58  ? -7.201  18.895  -21.433 1.00 20.33 ? 58  ALA   A CB  1 
ATOM   2500 N  N   . LYS   B 1 59  ? -10.138 19.216  -19.922 1.00 19.92 ? 59  LYS   A N   1 
ATOM   2501 C  CA  . LYS   B 1 59  ? -11.451 18.654  -19.636 1.00 22.12 ? 59  LYS   A CA  1 
ATOM   2502 C  C   . LYS   B 1 59  ? -12.352 18.609  -20.868 1.00 21.56 ? 59  LYS   A C   1 
ATOM   2503 O  O   . LYS   B 1 59  ? -12.897 17.550  -21.215 1.00 19.20 ? 59  LYS   A O   1 
ATOM   2504 C  CB  . LYS   B 1 59  ? -12.118 19.395  -18.471 1.00 25.13 ? 59  LYS   A CB  1 
ATOM   2505 C  CG  . LYS   B 1 59  ? -11.430 19.134  -17.137 1.00 32.07 ? 59  LYS   A CG  1 
ATOM   2506 C  CD  . LYS   B 1 59  ? -10.994 17.673  -16.977 1.00 38.64 ? 59  LYS   A CD  1 
ATOM   2507 C  CE  . LYS   B 1 59  ? -10.384 17.345  -15.624 1.00 42.12 ? 59  LYS   A CE  1 
ATOM   2508 N  NZ  . LYS   B 1 59  ? -9.347  16.292  -15.735 1.00 37.43 ? 59  LYS   A NZ  1 
ATOM   2509 N  N   . ILE   B 1 60  ? -12.600 19.790  -21.442 1.00 20.11 ? 60  ILE   A N   1 
ATOM   2510 C  CA  . ILE   B 1 60  ? -13.565 19.940  -22.517 1.00 21.58 ? 60  ILE   A CA  1 
ATOM   2511 C  C   . ILE   B 1 60  ? -13.044 20.925  -23.552 1.00 18.89 ? 60  ILE   A C   1 
ATOM   2512 O  O   . ILE   B 1 60  ? -12.202 21.783  -23.252 1.00 17.51 ? 60  ILE   A O   1 
ATOM   2513 C  CB  . ILE   B 1 60  ? -14.947 20.396  -21.996 1.00 26.56 ? 60  ILE   A CB  1 
ATOM   2514 C  CG1 . ILE   B 1 60  ? -14.896 21.766  -21.328 1.00 26.95 ? 60  ILE   A CG1 1 
ATOM   2515 C  CG2 . ILE   B 1 60  ? -15.543 19.353  -21.064 1.00 27.45 ? 60  ILE   A CG2 1 
ATOM   2516 C  CD1 . ILE   B 1 60  ? -16.269 22.376  -21.132 1.00 32.68 ? 60  ILE   A CD1 1 
ATOM   2517 N  N   . ILE   B 1 61  ? -13.542 20.747  -24.776 1.00 17.74 ? 61  ILE   A N   1 
ATOM   2518 C  CA  . ILE   B 1 61  ? -13.391 21.760  -25.799 1.00 17.45 ? 61  ILE   A CA  1 
ATOM   2519 C  C   . ILE   B 1 61  ? -14.785 22.210  -26.192 1.00 17.96 ? 61  ILE   A C   1 
ATOM   2520 O  O   . ILE   B 1 61  ? -15.739 21.415  -26.308 1.00 17.00 ? 61  ILE   A O   1 
ATOM   2521 C  CB  . ILE   B 1 61  ? -12.574 21.258  -27.004 1.00 17.89 ? 61  ILE   A CB  1 
ATOM   2522 C  CG1 . ILE   B 1 61  ? -12.103 22.418  -27.884 1.00 16.65 ? 61  ILE   A CG1 1 
ATOM   2523 C  CG2 . ILE   B 1 61  ? -13.333 20.193  -27.794 1.00 16.18 ? 61  ILE   A CG2 1 
ATOM   2524 C  CD1 . ILE   B 1 61  ? -11.211 21.999  -29.039 1.00 17.11 ? 61  ILE   A CD1 1 
ATOM   2525 N  N   . SER   B 1 62  ? -14.889 23.512  -26.390 1.00 17.86 ? 62  SER   A N   1 
ATOM   2526 C  CA  . SER   B 1 62  ? -16.180 24.066  -26.744 1.00 19.04 ? 62  SER   A CA  1 
ATOM   2527 C  C   . SER   B 1 62  ? -16.027 25.226  -27.730 1.00 20.39 ? 62  SER   A C   1 
ATOM   2528 O  O   . SER   B 1 62  ? -14.930 25.774  -27.885 1.00 19.44 ? 62  SER   A O   1 
ATOM   2529 C  CB  . SER   B 1 62  ? -16.889 24.502  -25.524 1.00 20.09 ? 62  SER   A CB  1 
ATOM   2530 O  OG  . SER   B 1 62  ? -16.289 25.667  -25.001 1.00 23.74 ? 62  SER   A OG  1 
ATOM   2531 N  N   . ASN   B 1 63  ? -17.144 25.546  -28.399 1.00 18.59 ? 63  ASN   A N   1 
ATOM   2532 C  CA  . ASN   B 1 63  ? -17.239 26.694  -29.280 1.00 20.23 ? 63  ASN   A CA  1 
ATOM   2533 C  C   . ASN   B 1 63  ? -17.811 27.847  -28.470 1.00 22.17 ? 63  ASN   A C   1 
ATOM   2534 O  O   . ASN   B 1 63  ? -18.997 27.873  -28.130 1.00 22.01 ? 63  ASN   A O   1 
ATOM   2535 C  CB  . ASN   B 1 63  ? -18.046 26.386  -30.554 1.00 20.44 ? 63  ASN   A CB  1 
ATOM   2536 C  CG  . ASN   B 1 63  ? -18.137 27.549  -31.530 1.00 22.39 ? 63  ASN   A CG  1 
ATOM   2537 O  OD1 . ASN   B 1 63  ? -17.855 28.694  -31.182 1.00 22.23 ? 63  ASN   A OD1 1 
ATOM   2538 N  ND2 . ASN   B 1 63  ? -18.536 27.264  -32.760 1.00 24.20 ? 63  ASN   A ND2 1 
ATOM   2539 N  N   . SER   B 1 64  ? -16.953 28.828  -28.201 1.00 22.00 ? 64  SER   A N   1 
ATOM   2540 C  CA  . SER   B 1 64  ? -17.337 29.974  -27.412 1.00 20.19 ? 64  SER   A CA  1 
ATOM   2541 C  C   . SER   B 1 64  ? -18.125 30.983  -28.256 1.00 23.05 ? 64  SER   A C   1 
ATOM   2542 O  O   . SER   B 1 64  ? -18.682 31.929  -27.699 1.00 23.81 ? 64  SER   A O   1 
ATOM   2543 C  CB  . SER   B 1 64  ? -16.084 30.613  -26.840 1.00 22.04 ? 64  SER   A CB  1 
ATOM   2544 O  OG  . SER   B 1 64  ? -15.381 31.347  -27.844 1.00 20.75 ? 64  SER   A OG  1 
ATOM   2545 N  N   . GLY   B 1 65  ? -18.109 30.820  -29.590 1.00 18.79 ? 65  GLY   A N   1 
ATOM   2546 C  CA  . GLY   B 1 65  ? -18.648 31.797  -30.520 1.00 22.10 ? 65  GLY   A CA  1 
ATOM   2547 C  C   . GLY   B 1 65  ? -17.568 32.741  -31.047 1.00 21.78 ? 65  GLY   A C   1 
ATOM   2548 O  O   . GLY   B 1 65  ? -17.772 33.427  -32.053 1.00 20.91 ? 65  GLY   A O   1 
ATOM   2549 N  N   . HIS   B 1 66  ? -16.403 32.709  -30.400 1.00 18.62 ? 66  HIS   A N   1 
ATOM   2550 C  CA  . HIS   B 1 66  ? -15.298 33.597  -30.749 1.00 20.07 ? 66  HIS   A CA  1 
ATOM   2551 C  C   . HIS   B 1 66  ? -14.053 32.798  -31.139 1.00 19.21 ? 66  HIS   A C   1 
ATOM   2552 O  O   . HIS   B 1 66  ? -13.174 33.352  -31.790 1.00 20.34 ? 66  HIS   A O   1 
ATOM   2553 C  CB  . HIS   B 1 66  ? -14.953 34.508  -29.565 1.00 21.07 ? 66  HIS   A CB  1 
ATOM   2554 C  CG  . HIS   B 1 66  ? -16.138 35.236  -29.017 1.00 22.73 ? 66  HIS   A CG  1 
ATOM   2555 N  ND1 . HIS   B 1 66  ? -16.673 34.958  -27.767 1.00 24.23 ? 66  HIS   A ND1 1 
ATOM   2556 C  CD2 . HIS   B 1 66  ? -16.902 36.220  -29.555 1.00 23.32 ? 66  HIS   A CD2 1 
ATOM   2557 C  CE1 . HIS   B 1 66  ? -17.722 35.754  -27.562 1.00 24.48 ? 66  HIS   A CE1 1 
ATOM   2558 N  NE2 . HIS   B 1 66  ? -17.895 36.526  -28.659 1.00 23.96 ? 66  HIS   A NE2 1 
ATOM   2559 N  N   . SER   B 1 67  ? -13.914 31.567  -30.616 1.00 17.08 ? 67  SER   A N   1 
ATOM   2560 C  CA  . SER   B 1 67  ? -12.846 30.663  -31.024 1.00 17.99 ? 67  SER   A CA  1 
ATOM   2561 C  C   . SER   B 1 67  ? -13.245 29.288  -30.507 1.00 17.98 ? 67  SER   A C   1 
ATOM   2562 O  O   . SER   B 1 67  ? -14.295 29.174  -29.902 1.00 18.11 ? 67  SER   A O   1 
ATOM   2563 C  CB  . SER   B 1 67  ? -11.502 31.068  -30.424 1.00 17.37 ? 67  SER   A CB  1 
ATOM   2564 O  OG  . SER   B 1 67  ? -10.505 30.091  -30.738 1.00 19.14 ? 67  SER   A OG  1 
ATOM   2565 N  N   . PHE   B 1 68  ? -12.398 28.268  -30.672 1.00 17.89 ? 68  PHE   A N   1 
ATOM   2566 C  CA  . PHE   B 1 68  ? -12.576 27.132  -29.777 1.00 18.96 ? 68  PHE   A CA  1 
ATOM   2567 C  C   . PHE   B 1 68  ? -11.984 27.492  -28.409 1.00 20.37 ? 68  PHE   A C   1 
ATOM   2568 O  O   . PHE   B 1 68  ? -11.160 28.393  -28.292 1.00 22.63 ? 68  PHE   A O   1 
ATOM   2569 C  CB  . PHE   B 1 68  ? -11.915 25.867  -30.335 1.00 19.88 ? 68  PHE   A CB  1 
ATOM   2570 C  CG  . PHE   B 1 68  ? -10.407 25.884  -30.331 1.00 18.71 ? 68  PHE   A CG  1 
ATOM   2571 C  CD1 . PHE   B 1 68  ? -9.691  25.609  -29.173 1.00 19.67 ? 68  PHE   A CD1 1 
ATOM   2572 C  CD2 . PHE   B 1 68  ? -9.700  26.156  -31.495 1.00 19.30 ? 68  PHE   A CD2 1 
ATOM   2573 C  CE1 . PHE   B 1 68  ? -8.302  25.627  -29.178 1.00 20.31 ? 68  PHE   A CE1 1 
ATOM   2574 C  CE2 . PHE   B 1 68  ? -8.309  26.175  -31.501 1.00 18.51 ? 68  PHE   A CE2 1 
ATOM   2575 C  CZ  . PHE   B 1 68  ? -7.619  25.906  -30.342 1.00 20.81 ? 68  PHE   A CZ  1 
ATOM   2576 N  N   . ASN   B 1 69  ? -12.372 26.755  -27.370 1.00 17.22 ? 69  ASN   A N   1 
ATOM   2577 C  CA  . ASN   B 1 69  ? -11.936 27.027  -26.015 1.00 17.91 ? 69  ASN   A CA  1 
ATOM   2578 C  C   . ASN   B 1 69  ? -11.647 25.670  -25.386 1.00 17.68 ? 69  ASN   A C   1 
ATOM   2579 O  O   . ASN   B 1 69  ? -12.574 24.879  -25.242 1.00 17.64 ? 69  ASN   A O   1 
ATOM   2580 C  CB  . ASN   B 1 69  ? -13.101 27.741  -25.331 1.00 24.50 ? 69  ASN   A CB  1 
ATOM   2581 C  CG  . ASN   B 1 69  ? -12.889 28.172  -23.898 1.00 34.97 ? 69  ASN   A CG  1 
ATOM   2582 O  OD1 . ASN   B 1 69  ? -12.687 29.352  -23.618 1.00 44.13 ? 69  ASN   A OD1 1 
ATOM   2583 N  ND2 . ASN   B 1 69  ? -13.048 27.245  -22.975 1.00 36.26 ? 69  ASN   A ND2 1 
ATOM   2584 N  N   . VAL   B 1 70  ? -10.381 25.347  -25.126 1.00 16.19 ? 70  VAL   A N   1 
ATOM   2585 C  CA  . VAL   B 1 70  ? -10.095 24.165  -24.300 1.00 17.67 ? 70  VAL   A CA  1 
ATOM   2586 C  C   . VAL   B 1 70  ? -10.051 24.624  -22.850 1.00 18.47 ? 70  VAL   A C   1 
ATOM   2587 O  O   . VAL   B 1 70  ? -9.252  25.513  -22.536 1.00 18.66 ? 70  VAL   A O   1 
ATOM   2588 C  CB  . VAL   B 1 70  ? -8.769  23.488  -24.666 1.00 17.56 ? 70  VAL   A CB  1 
ATOM   2589 C  CG1 . VAL   B 1 70  ? -8.479  22.306  -23.748 1.00 19.01 ? 70  VAL   A CG1 1 
ATOM   2590 C  CG2 . VAL   B 1 70  ? -8.736  23.097  -26.146 1.00 18.94 ? 70  VAL   A CG2 1 
ATOM   2591 N  N   . ASP   B 1 71  ? -10.912 24.027  -22.005 1.00 17.53 ? 71  ASP   A N   1 
ATOM   2592 C  CA  . ASP   B 1 71  ? -10.924 24.334  -20.577 1.00 20.66 ? 71  ASP   A CA  1 
ATOM   2593 C  C   . ASP   B 1 71  ? -10.094 23.294  -19.827 1.00 21.11 ? 71  ASP   A C   1 
ATOM   2594 O  O   . ASP   B 1 71  ? -10.173 22.091  -20.130 1.00 20.23 ? 71  ASP   A O   1 
ATOM   2595 C  CB  . ASP   B 1 71  ? -12.338 24.255  -20.016 1.00 24.62 ? 71  ASP   A CB  1 
ATOM   2596 C  CG  . ASP   B 1 71  ? -13.202 25.480  -20.281 1.00 32.92 ? 71  ASP   A CG  1 
ATOM   2597 O  OD1 . ASP   B 1 71  ? -12.661 26.593  -20.300 1.00 37.78 ? 71  ASP   A OD1 1 
ATOM   2598 O  OD2 . ASP   B 1 71  ? -14.436 25.308  -20.428 1.00 39.97 ? 71  ASP   A OD2 1 
ATOM   2599 N  N   . PHE   B 1 72  ? -9.325  23.774  -18.838 1.00 20.25 ? 72  PHE   A N   1 
ATOM   2600 C  CA  . PHE   B 1 72  ? -8.526  22.896  -17.989 1.00 21.60 ? 72  PHE   A CA  1 
ATOM   2601 C  C   . PHE   B 1 72  ? -9.036  22.947  -16.552 1.00 22.83 ? 72  PHE   A C   1 
ATOM   2602 O  O   . PHE   B 1 72  ? -9.519  23.985  -16.105 1.00 22.60 ? 72  PHE   A O   1 
ATOM   2603 C  CB  . PHE   B 1 72  ? -7.047  23.292  -18.059 1.00 19.87 ? 72  PHE   A CB  1 
ATOM   2604 C  CG  . PHE   B 1 72  ? -6.468  23.151  -19.444 1.00 18.35 ? 72  PHE   A CG  1 
ATOM   2605 C  CD1 . PHE   B 1 72  ? -6.684  24.130  -20.408 1.00 19.22 ? 72  PHE   A CD1 1 
ATOM   2606 C  CD2 . PHE   B 1 72  ? -5.723  22.027  -19.798 1.00 17.97 ? 72  PHE   A CD2 1 
ATOM   2607 C  CE1 . PHE   B 1 72  ? -6.149  24.028  -21.688 1.00 17.86 ? 72  PHE   A CE1 1 
ATOM   2608 C  CE2 . PHE   B 1 72  ? -5.194  21.929  -21.080 1.00 18.00 ? 72  PHE   A CE2 1 
ATOM   2609 C  CZ  . PHE   B 1 72  ? -5.420  22.908  -22.028 1.00 17.16 ? 72  PHE   A CZ  1 
ATOM   2610 N  N   . ASP   B 1 73  ? -8.917  21.812  -15.847 1.00 23.93 ? 73  ASP   A N   1 
ATOM   2611 C  CA  . ASP   B 1 73  ? -9.107  21.766  -14.409 1.00 26.43 ? 73  ASP   A CA  1 
ATOM   2612 C  C   . ASP   B 1 73  ? -8.068  22.680  -13.769 1.00 25.53 ? 73  ASP   A C   1 
ATOM   2613 O  O   . ASP   B 1 73  ? -6.875  22.394  -13.857 1.00 23.10 ? 73  ASP   A O   1 
ATOM   2614 C  CB  . ASP   B 1 73  ? -8.953  20.326  -13.918 1.00 31.69 ? 73  ASP   A CB  1 
ATOM   2615 C  CG  . ASP   B 1 73  ? -9.237  20.184  -12.431 1.00 41.17 ? 73  ASP   A CG  1 
ATOM   2616 O  OD1 . ASP   B 1 73  ? -8.756  21.054  -11.662 1.00 39.20 ? 73  ASP   A OD1 1 
ATOM   2617 O  OD2 . ASP   B 1 73  ? -9.938  19.199  -12.049 1.00 43.95 ? 73  ASP   A OD2 1 
ATOM   2618 N  N   . ASP   B 1 74  ? -8.531  23.765  -13.130 1.00 21.58 ? 74  ASP   A N   1 
ATOM   2619 C  CA  . ASP   B 1 74  ? -7.626  24.731  -12.532 1.00 24.86 ? 74  ASP   A CA  1 
ATOM   2620 C  C   . ASP   B 1 74  ? -7.841  24.804  -11.010 1.00 28.21 ? 74  ASP   A C   1 
ATOM   2621 O  O   . ASP   B 1 74  ? -8.027  25.903  -10.442 1.00 26.03 ? 74  ASP   A O   1 
ATOM   2622 C  CB  . ASP   B 1 74  ? -7.773  26.096  -13.207 1.00 24.08 ? 74  ASP   A CB  1 
ATOM   2623 C  CG  . ASP   B 1 74  ? -9.124  26.704  -12.892 1.00 26.25 ? 74  ASP   A CG  1 
ATOM   2624 O  OD1 . ASP   B 1 74  ? -10.021 25.946  -12.367 1.00 25.03 ? 74  ASP   A OD1 1 
ATOM   2625 O  OD2 . ASP   B 1 74  ? -9.265  27.935  -13.125 1.00 23.66 ? 74  ASP   A OD2 1 
ATOM   2626 N  N   . THR   B 1 75  ? -7.794  23.623  -10.362 1.00 26.07 ? 75  THR   A N   1 
ATOM   2627 C  CA  . THR   B 1 75  ? -7.992  23.494  -8.916  1.00 29.33 ? 75  THR   A CA  1 
ATOM   2628 C  C   . THR   B 1 75  ? -6.700  23.065  -8.228  1.00 28.24 ? 75  THR   A C   1 
ATOM   2629 O  O   . THR   B 1 75  ? -6.619  23.097  -6.995  1.00 29.03 ? 75  THR   A O   1 
ATOM   2630 C  CB  . THR   B 1 75  ? -9.127  22.509  -8.577  1.00 29.65 ? 75  THR   A CB  1 
ATOM   2631 O  OG1 . THR   B 1 75  ? -8.672  21.188  -8.899  1.00 27.83 ? 75  THR   A OG1 1 
ATOM   2632 C  CG2 . THR   B 1 75  ? -10.436 22.836  -9.271  1.00 29.20 ? 75  THR   A CG2 1 
ATOM   2633 N  N   . GLU   B 1 76  ? -5.707  22.641  -9.029  1.00 27.21 ? 76  GLU   A N   1 
ATOM   2634 C  CA  . GLU   B 1 76  ? -4.421  22.200  -8.514  1.00 27.82 ? 76  GLU   A CA  1 
ATOM   2635 C  C   . GLU   B 1 76  ? -3.278  22.802  -9.314  1.00 24.09 ? 76  GLU   A C   1 
ATOM   2636 O  O   . GLU   B 1 76  ? -3.504  23.433  -10.342 1.00 26.23 ? 76  GLU   A O   1 
ATOM   2637 C  CB  . GLU   B 1 76  ? -4.324  20.674  -8.562  1.00 33.17 ? 76  GLU   A CB  1 
ATOM   2638 C  CG  . GLU   B 1 76  ? -4.865  20.073  -7.289  1.00 41.33 ? 76  GLU   A CG  1 
ATOM   2639 C  CD  . GLU   B 1 76  ? -5.550  18.739  -7.475  1.00 51.92 ? 76  GLU   A CD  1 
ATOM   2640 O  OE1 . GLU   B 1 76  ? -4.828  17.748  -7.732  1.00 59.54 ? 76  GLU   A OE1 1 
ATOM   2641 O  OE2 . GLU   B 1 76  ? -6.799  18.703  -7.375  1.00 59.54 ? 76  GLU   A OE2 1 
ATOM   2642 N  N   . ASN   B 1 77  ? -2.051  22.539  -8.864  1.00 22.27 ? 77  ASN   A N   1 
ATOM   2643 C  CA  . ASN   B 1 77  ? -0.863  23.108  -9.491  1.00 22.30 ? 77  ASN   A CA  1 
ATOM   2644 C  C   . ASN   B 1 77  ? -0.131  22.088  -10.358 1.00 22.40 ? 77  ASN   A C   1 
ATOM   2645 O  O   . ASN   B 1 77  ? 1.087   22.156  -10.477 1.00 24.11 ? 77  ASN   A O   1 
ATOM   2646 C  CB  . ASN   B 1 77  ? 0.025   23.830  -8.479  1.00 22.85 ? 77  ASN   A CB  1 
ATOM   2647 C  CG  . ASN   B 1 77  ? -0.599  25.143  -8.052  1.00 25.18 ? 77  ASN   A CG  1 
ATOM   2648 O  OD1 . ASN   B 1 77  ? -1.442  25.695  -8.765  1.00 24.29 ? 77  ASN   A OD1 1 
ATOM   2649 N  ND2 . ASN   B 1 77  ? -0.173  25.665  -6.912  1.00 24.89 ? 77  ASN   A ND2 1 
ATOM   2650 N  N   . LYS   B 1 78  ? -0.897  21.201  -11.008 1.00 22.86 ? 78  LYS   A N   1 
ATOM   2651 C  CA  . LYS   B 1 78  ? -0.343  20.205  -11.913 1.00 24.29 ? 78  LYS   A CA  1 
ATOM   2652 C  C   . LYS   B 1 78  ? 0.032   20.858  -13.246 1.00 21.13 ? 78  LYS   A C   1 
ATOM   2653 O  O   . LYS   B 1 78  ? 0.892   20.326  -13.929 1.00 21.45 ? 78  LYS   A O   1 
ATOM   2654 C  CB  . LYS   B 1 78  ? -1.364  19.095  -12.202 1.00 29.00 ? 78  LYS   A CB  1 
ATOM   2655 C  CG  . LYS   B 1 78  ? -1.605  18.089  -11.079 1.00 33.99 ? 78  LYS   A CG  1 
ATOM   2656 C  CD  . LYS   B 1 78  ? -2.506  16.930  -11.502 1.00 37.74 ? 78  LYS   A CD  1 
ATOM   2657 C  CE  . LYS   B 1 78  ? -2.483  15.756  -10.536 1.00 45.12 ? 78  LYS   A CE  1 
ATOM   2658 N  NZ  . LYS   B 1 78  ? -3.439  14.691  -10.933 1.00 48.39 ? 78  LYS   A NZ  1 
ATOM   2659 N  N   . SER   B 1 79  ? -0.644  21.962  -13.643 1.00 18.84 ? 79  SER   A N   1 
ATOM   2660 C  CA  . SER   B 1 79  ? -0.329  22.641  -14.906 1.00 17.57 ? 79  SER   A CA  1 
ATOM   2661 C  C   . SER   B 1 79  ? -0.126  24.129  -14.629 1.00 17.86 ? 79  SER   A C   1 
ATOM   2662 O  O   . SER   B 1 79  ? -1.092  24.833  -14.381 1.00 14.58 ? 79  SER   A O   1 
ATOM   2663 C  CB  . SER   B 1 79  ? -1.411  22.470  -15.953 1.00 19.73 ? 79  SER   A CB  1 
ATOM   2664 O  OG  . SER   B 1 79  ? -1.505  21.132  -16.415 1.00 18.41 ? 79  SER   A OG  1 
ATOM   2665 N  N   . VAL   B 1 80  ? 1.138   24.564  -14.608 1.00 18.34 ? 80  VAL   A N   1 
ATOM   2666 C  CA  . VAL   B 1 80  ? 1.476   25.875  -14.075 1.00 19.11 ? 80  VAL   A CA  1 
ATOM   2667 C  C   . VAL   B 1 80  ? 2.609   26.480  -14.893 1.00 20.16 ? 80  VAL   A C   1 
ATOM   2668 O  O   . VAL   B 1 80  ? 3.464   25.775  -15.437 1.00 24.76 ? 80  VAL   A O   1 
ATOM   2669 C  CB  . VAL   B 1 80  ? 1.827   25.878  -12.572 1.00 22.22 ? 80  VAL   A CB  1 
ATOM   2670 C  CG1 . VAL   B 1 80  ? 0.747   25.259  -11.701 1.00 20.96 ? 80  VAL   A CG1 1 
ATOM   2671 C  CG2 . VAL   B 1 80  ? 3.190   25.268  -12.271 1.00 23.12 ? 80  VAL   A CG2 1 
ATOM   2672 N  N   . LEU   B 1 81  ? 2.608   27.811  -14.937 1.00 18.12 ? 81  LEU   A N   1 
ATOM   2673 C  CA  . LEU   B 1 81  ? 3.650   28.598  -15.574 1.00 18.85 ? 81  LEU   A CA  1 
ATOM   2674 C  C   . LEU   B 1 81  ? 4.298   29.438  -14.475 1.00 20.34 ? 81  LEU   A C   1 
ATOM   2675 O  O   . LEU   B 1 81  ? 3.607   30.036  -13.659 1.00 16.99 ? 81  LEU   A O   1 
ATOM   2676 C  CB  . LEU   B 1 81  ? 2.971   29.483  -16.631 1.00 20.85 ? 81  LEU   A CB  1 
ATOM   2677 C  CG  . LEU   B 1 81  ? 3.838   30.563  -17.271 1.00 21.77 ? 81  LEU   A CG  1 
ATOM   2678 C  CD1 . LEU   B 1 81  ? 4.933   29.937  -18.121 1.00 22.48 ? 81  LEU   A CD1 1 
ATOM   2679 C  CD2 . LEU   B 1 81  ? 2.974   31.488  -18.118 1.00 23.00 ? 81  LEU   A CD2 1 
ATOM   2680 N  N   . ARG   B 1 82  ? 5.635   29.443  -14.431 1.00 21.09 ? 82  ARG   A N   1 
ATOM   2681 C  CA  . ARG   B 1 82  ? 6.362   30.123  -13.375 1.00 22.22 ? 82  ARG   A CA  1 
ATOM   2682 C  C   . ARG   B 1 82  ? 7.625   30.675  -14.015 1.00 20.47 ? 82  ARG   A C   1 
ATOM   2683 O  O   . ARG   B 1 82  ? 8.029   30.217  -15.091 1.00 18.24 ? 82  ARG   A O   1 
ATOM   2684 C  CB  . ARG   B 1 82  ? 6.805   29.141  -12.274 1.00 24.94 ? 82  ARG   A CB  1 
ATOM   2685 C  CG  . ARG   B 1 82  ? 5.680   28.602  -11.395 1.00 29.78 ? 82  ARG   A CG  1 
ATOM   2686 C  CD  . ARG   B 1 82  ? 6.046   27.418  -10.502 1.00 33.97 ? 82  ARG   A CD  1 
ATOM   2687 N  NE  . ARG   B 1 82  ? 6.341   26.217  -11.284 1.00 45.66 ? 82  ARG   A NE  1 
ATOM   2688 C  CZ  . ARG   B 1 82  ? 6.015   24.958  -10.946 1.00 49.52 ? 82  ARG   A CZ  1 
ATOM   2689 N  NH1 . ARG   B 1 82  ? 5.372   24.725  -9.805  1.00 44.52 ? 82  ARG   A NH1 1 
ATOM   2690 N  NH2 . ARG   B 1 82  ? 6.312   23.951  -11.769 1.00 37.97 ? 82  ARG   A NH2 1 
ATOM   2691 N  N   . GLY   B 1 83  ? 8.248   31.628  -13.321 1.00 20.50 ? 83  GLY   A N   1 
ATOM   2692 C  CA  . GLY   B 1 83  ? 9.548   32.122  -13.739 1.00 19.01 ? 83  GLY   A CA  1 
ATOM   2693 C  C   . GLY   B 1 83  ? 9.415   33.199  -14.803 1.00 21.16 ? 83  GLY   A C   1 
ATOM   2694 O  O   . GLY   B 1 83  ? 8.374   33.845  -14.896 1.00 17.57 ? 83  GLY   A O   1 
ATOM   2695 N  N   . GLY   B 1 84  ? 10.475  33.359  -15.617 1.00 22.28 ? 84  GLY   A N   1 
ATOM   2696 C  CA  . GLY   B 1 84  ? 10.527  34.442  -16.584 1.00 19.78 ? 84  GLY   A CA  1 
ATOM   2697 C  C   . GLY   B 1 84  ? 10.283  35.758  -15.864 1.00 21.50 ? 84  GLY   A C   1 
ATOM   2698 O  O   . GLY   B 1 84  ? 10.977  36.090  -14.902 1.00 22.59 ? 84  GLY   A O   1 
ATOM   2699 N  N   . PRO   B 1 85  ? 9.288   36.544  -16.300 1.00 20.83 ? 85  PRO   A N   1 
ATOM   2700 C  CA  . PRO   B 1 85  ? 8.977   37.817  -15.629 1.00 20.21 ? 85  PRO   A CA  1 
ATOM   2701 C  C   . PRO   B 1 85  ? 8.031   37.699  -14.432 1.00 21.99 ? 85  PRO   A C   1 
ATOM   2702 O  O   . PRO   B 1 85  ? 7.714   38.713  -13.797 1.00 20.74 ? 85  PRO   A O   1 
ATOM   2703 C  CB  . PRO   B 1 85  ? 8.240   38.549  -16.748 1.00 20.04 ? 85  PRO   A CB  1 
ATOM   2704 C  CG  . PRO   B 1 85  ? 7.484   37.431  -17.465 1.00 21.10 ? 85  PRO   A CG  1 
ATOM   2705 C  CD  . PRO   B 1 85  ? 8.450   36.257  -17.484 1.00 21.43 ? 85  PRO   A CD  1 
ATOM   2706 N  N   . LEU   B 1 86  ? 7.552   36.462  -14.155 1.00 20.99 ? 86  LEU   A N   1 
ATOM   2707 C  CA  . LEU   B 1 86  ? 6.419   36.270  -13.256 1.00 21.49 ? 86  LEU   A CA  1 
ATOM   2708 C  C   . LEU   B 1 86  ? 6.848   36.194  -11.785 1.00 21.83 ? 86  LEU   A C   1 
ATOM   2709 O  O   . LEU   B 1 86  ? 7.802   35.495  -11.465 1.00 23.39 ? 86  LEU   A O   1 
ATOM   2710 C  CB  . LEU   B 1 86  ? 5.703   34.967  -13.663 1.00 18.15 ? 86  LEU   A CB  1 
ATOM   2711 C  CG  . LEU   B 1 86  ? 5.130   34.950  -15.087 1.00 18.91 ? 86  LEU   A CG  1 
ATOM   2712 C  CD1 . LEU   B 1 86  ? 4.586   33.572  -15.444 1.00 17.72 ? 86  LEU   A CD1 1 
ATOM   2713 C  CD2 . LEU   B 1 86  ? 4.016   35.983  -15.212 1.00 15.90 ? 86  LEU   A CD2 1 
ATOM   2714 N  N   . THR   B 1 87  ? 6.052   36.791  -10.878 1.00 20.44 ? 87  THR   A N   1 
ATOM   2715 C  CA  . THR   B 1 87  ? 6.196   36.542  -9.437  1.00 23.35 ? 87  THR   A CA  1 
ATOM   2716 C  C   . THR   B 1 87  ? 5.101   35.588  -8.955  1.00 22.76 ? 87  THR   A C   1 
ATOM   2717 O  O   . THR   B 1 87  ? 3.911   35.889  -9.078  1.00 24.11 ? 87  THR   A O   1 
ATOM   2718 C  CB  . THR   B 1 87  ? 6.114   37.836  -8.613  1.00 25.66 ? 87  THR   A CB  1 
ATOM   2719 O  OG1 . THR   B 1 87  ? 7.107   38.725  -9.141  1.00 27.37 ? 87  THR   A OG1 1 
ATOM   2720 C  CG2 . THR   B 1 87  ? 6.373   37.599  -7.132  1.00 27.76 ? 87  THR   A CG2 1 
ATOM   2721 N  N   . GLY   B 1 88  ? 5.505   34.412  -8.466  1.00 24.72 ? 88  GLY   A N   1 
ATOM   2722 C  CA  . GLY   B 1 88  ? 4.559   33.369  -8.085  1.00 25.58 ? 88  GLY   A CA  1 
ATOM   2723 C  C   . GLY   B 1 88  ? 4.141   32.424  -9.225  1.00 25.14 ? 88  GLY   A C   1 
ATOM   2724 O  O   . GLY   B 1 88  ? 4.729   32.379  -10.308 1.00 21.54 ? 88  GLY   A O   1 
ATOM   2725 N  N   . SER   B 1 89  ? 3.075   31.669  -8.952  1.00 22.96 ? 89  SER   A N   1 
ATOM   2726 C  CA  . SER   B 1 89  ? 2.677   30.538  -9.764  1.00 21.58 ? 89  SER   A CA  1 
ATOM   2727 C  C   . SER   B 1 89  ? 1.398   30.888  -10.527 1.00 21.01 ? 89  SER   A C   1 
ATOM   2728 O  O   . SER   B 1 89  ? 0.418   31.320  -9.922  1.00 19.50 ? 89  SER   A O   1 
ATOM   2729 C  CB  . SER   B 1 89  ? 2.486   29.343  -8.857  1.00 23.45 ? 89  SER   A CB  1 
ATOM   2730 O  OG  . SER   B 1 89  ? 2.172   28.190  -9.634  1.00 28.97 ? 89  SER   A OG  1 
ATOM   2731 N  N   . TYR   B 1 90  ? 1.406   30.694  -11.856 1.00 18.14 ? 90  TYR   A N   1 
ATOM   2732 C  CA  . TYR   B 1 90  ? 0.231   31.015  -12.652 1.00 16.31 ? 90  TYR   A CA  1 
ATOM   2733 C  C   . TYR   B 1 90  ? -0.366  29.708  -13.154 1.00 16.39 ? 90  TYR   A C   1 
ATOM   2734 O  O   . TYR   B 1 90  ? 0.305   28.918  -13.829 1.00 17.68 ? 90  TYR   A O   1 
ATOM   2735 C  CB  . TYR   B 1 90  ? 0.593   31.987  -13.776 1.00 15.56 ? 90  TYR   A CB  1 
ATOM   2736 C  CG  . TYR   B 1 90  ? 0.846   33.397  -13.288 1.00 15.57 ? 90  TYR   A CG  1 
ATOM   2737 C  CD1 . TYR   B 1 90  ? 1.949   33.717  -12.503 1.00 15.03 ? 90  TYR   A CD1 1 
ATOM   2738 C  CD2 . TYR   B 1 90  ? -0.048  34.407  -13.608 1.00 15.21 ? 90  TYR   A CD2 1 
ATOM   2739 C  CE1 . TYR   B 1 90  ? 2.144   35.010  -12.027 1.00 17.32 ? 90  TYR   A CE1 1 
ATOM   2740 C  CE2 . TYR   B 1 90  ? 0.139   35.709  -13.148 1.00 15.92 ? 90  TYR   A CE2 1 
ATOM   2741 C  CZ  . TYR   B 1 90  ? 1.242   36.017  -12.368 1.00 17.21 ? 90  TYR   A CZ  1 
ATOM   2742 O  OH  . TYR   B 1 90  ? 1.416   37.309  -11.934 1.00 19.38 ? 90  TYR   A OH  1 
ATOM   2743 N  N   . ARG   B 1 91  ? -1.627  29.480  -12.788 1.00 16.21 ? 91  ARG   A N   1 
ATOM   2744 C  CA  . ARG   B 1 91  ? -2.297  28.222  -13.102 1.00 16.82 ? 91  ARG   A CA  1 
ATOM   2745 C  C   . ARG   B 1 91  ? -2.936  28.230  -14.498 1.00 16.72 ? 91  ARG   A C   1 
ATOM   2746 O  O   . ARG   B 1 91  ? -3.692  29.145  -14.847 1.00 14.76 ? 91  ARG   A O   1 
ATOM   2747 C  CB  . ARG   B 1 91  ? -3.345  27.928  -12.021 1.00 16.94 ? 91  ARG   A CB  1 
ATOM   2748 C  CG  . ARG   B 1 91  ? -3.959  26.540  -12.120 1.00 16.16 ? 91  ARG   A CG  1 
ATOM   2749 C  CD  . ARG   B 1 91  ? -4.833  26.258  -10.881 1.00 17.54 ? 91  ARG   A CD  1 
ATOM   2750 N  NE  . ARG   B 1 91  ? -4.111  26.334  -9.630  1.00 16.09 ? 91  ARG   A NE  1 
ATOM   2751 C  CZ  . ARG   B 1 91  ? -4.651  26.565  -8.417  1.00 18.64 ? 91  ARG   A CZ  1 
ATOM   2752 N  NH1 . ARG   B 1 91  ? -5.953  26.757  -8.291  1.00 16.73 ? 91  ARG   A NH1 1 
ATOM   2753 N  NH2 . ARG   B 1 91  ? -3.870  26.628  -7.346  1.00 16.96 ? 91  ARG   A NH2 1 
ATOM   2754 N  N   . LEU   B 1 92  ? -2.716  27.134  -15.246 1.00 15.40 ? 92  LEU   A N   1 
ATOM   2755 C  CA  . LEU   B 1 92  ? -3.344  26.977  -16.553 1.00 16.32 ? 92  LEU   A CA  1 
ATOM   2756 C  C   . LEU   B 1 92  ? -4.876  26.951  -16.441 1.00 17.99 ? 92  LEU   A C   1 
ATOM   2757 O  O   . LEU   B 1 92  ? -5.448  26.172  -15.683 1.00 16.99 ? 92  LEU   A O   1 
ATOM   2758 C  CB  . LEU   B 1 92  ? -2.789  25.727  -17.250 1.00 16.00 ? 92  LEU   A CB  1 
ATOM   2759 C  CG  . LEU   B 1 92  ? -3.455  25.350  -18.578 1.00 17.92 ? 92  LEU   A CG  1 
ATOM   2760 C  CD1 . LEU   B 1 92  ? -3.170  26.398  -19.658 1.00 19.01 ? 92  LEU   A CD1 1 
ATOM   2761 C  CD2 . LEU   B 1 92  ? -2.980  23.985  -19.060 1.00 16.93 ? 92  LEU   A CD2 1 
ATOM   2762 N  N   . ARG   B 1 93  ? -5.552  27.693  -17.321 1.00 16.02 ? 93  ARG   A N   1 
ATOM   2763 C  CA  . ARG   B 1 93  ? -7.004  27.772  -17.253 1.00 19.46 ? 93  ARG   A CA  1 
ATOM   2764 C  C   . ARG   B 1 93  ? -7.639  27.450  -18.613 1.00 18.24 ? 93  ARG   A C   1 
ATOM   2765 O  O   . ARG   B 1 93  ? -8.645  26.711  -18.678 1.00 19.12 ? 93  ARG   A O   1 
ATOM   2766 C  CB  . ARG   B 1 93  ? -7.435  29.121  -16.658 1.00 18.40 ? 93  ARG   A CB  1 
ATOM   2767 C  CG  . ARG   B 1 93  ? -8.940  29.403  -16.675 1.00 23.12 ? 93  ARG   A CG  1 
ATOM   2768 C  CD  . ARG   B 1 93  ? -9.857  28.325  -16.098 1.00 30.11 ? 93  ARG   A CD  1 
ATOM   2769 N  NE  . ARG   B 1 93  ? -11.324 28.454  -16.192 1.00 35.58 ? 93  ARG   A NE  1 
ATOM   2770 C  CZ  . ARG   B 1 93  ? -12.067 27.972  -17.197 1.00 37.09 ? 93  ARG   A CZ  1 
ATOM   2771 N  NH1 . ARG   B 1 93  ? -11.487 27.388  -18.233 1.00 33.36 ? 93  ARG   A NH1 1 
ATOM   2772 N  NH2 . ARG   B 1 93  ? -13.385 28.083  -17.176 1.00 38.54 ? 93  ARG   A NH2 1 
ATOM   2773 N  N   . GLN   B 1 94  ? -7.076  28.022  -19.701 1.00 16.95 ? 94  GLN   A N   1 
ATOM   2774 C  CA  . GLN   B 1 94  ? -7.707  27.894  -21.014 1.00 17.21 ? 94  GLN   A CA  1 
ATOM   2775 C  C   . GLN   B 1 94  ? -6.742  28.132  -22.186 1.00 15.83 ? 94  GLN   A C   1 
ATOM   2776 O  O   . GLN   B 1 94  ? -5.748  28.864  -22.065 1.00 14.93 ? 94  GLN   A O   1 
ATOM   2777 C  CB  . GLN   B 1 94  ? -8.983  28.746  -21.108 1.00 20.75 ? 94  GLN   A CB  1 
ATOM   2778 C  CG  . GLN   B 1 94  ? -8.805  30.183  -21.578 1.00 29.41 ? 94  GLN   A CG  1 
ATOM   2779 C  CD  . GLN   B 1 94  ? -9.118  30.389  -23.045 1.00 29.93 ? 94  GLN   A CD  1 
ATOM   2780 O  OE1 . GLN   B 1 94  ? -8.301  30.103  -23.888 1.00 30.95 ? 94  GLN   A OE1 1 
ATOM   2781 N  NE2 . GLN   B 1 94  ? -10.297 30.899  -23.375 1.00 39.58 ? 94  GLN   A NE2 1 
ATOM   2782 N  N   . VAL   B 1 95  ? -7.068  27.500  -23.325 1.00 14.87 ? 95  VAL   A N   1 
ATOM   2783 C  CA  . VAL   B 1 95  ? -6.350  27.620  -24.597 1.00 15.47 ? 95  VAL   A CA  1 
ATOM   2784 C  C   . VAL   B 1 95  ? -7.351  27.952  -25.702 1.00 15.15 ? 95  VAL   A C   1 
ATOM   2785 O  O   . VAL   B 1 95  ? -8.407  27.303  -25.806 1.00 14.66 ? 95  VAL   A O   1 
ATOM   2786 C  CB  . VAL   B 1 95  ? -5.575  26.341  -24.967 1.00 16.54 ? 95  VAL   A CB  1 
ATOM   2787 C  CG1 . VAL   B 1 95  ? -4.989  26.381  -26.395 1.00 17.09 ? 95  VAL   A CG1 1 
ATOM   2788 C  CG2 . VAL   B 1 95  ? -4.464  26.076  -23.971 1.00 16.48 ? 95  VAL   A CG2 1 
ATOM   2789 N  N   . HIS   B 1 96  ? -6.959  28.898  -26.568 1.00 12.94 ? 96  HIS   A N   1 
ATOM   2790 C  CA  . HIS   B 1 96  ? -7.725  29.212  -27.771 1.00 13.38 ? 96  HIS   A CA  1 
ATOM   2791 C  C   . HIS   B 1 96  ? -6.775  29.681  -28.887 1.00 14.07 ? 96  HIS   A C   1 
ATOM   2792 O  O   . HIS   B 1 96  ? -5.555  29.828  -28.696 1.00 14.20 ? 96  HIS   A O   1 
ATOM   2793 C  CB  . HIS   B 1 96  ? -8.814  30.272  -27.452 1.00 11.93 ? 96  HIS   A CB  1 
ATOM   2794 C  CG  . HIS   B 1 96  ? -8.178  31.543  -26.991 1.00 12.03 ? 96  HIS   A CG  1 
ATOM   2795 N  ND1 . HIS   B 1 96  ? -7.917  31.770  -25.665 1.00 12.33 ? 96  HIS   A ND1 1 
ATOM   2796 C  CD2 . HIS   B 1 96  ? -7.723  32.629  -27.672 1.00 13.65 ? 96  HIS   A CD2 1 
ATOM   2797 C  CE1 . HIS   B 1 96  ? -7.310  32.953  -25.525 1.00 14.86 ? 96  HIS   A CE1 1 
ATOM   2798 N  NE2 . HIS   B 1 96  ? -7.192  33.508  -26.757 1.00 13.85 ? 96  HIS   A NE2 1 
ATOM   2799 N  N   . LEU   B 1 97  ? -7.348  29.927  -30.069 1.00 14.54 ? 97  LEU   A N   1 
ATOM   2800 C  CA  . LEU   B 1 97  ? -6.586  30.300  -31.256 1.00 15.82 ? 97  LEU   A CA  1 
ATOM   2801 C  C   . LEU   B 1 97  ? -7.200  31.542  -31.900 1.00 16.56 ? 97  LEU   A C   1 
ATOM   2802 O  O   . LEU   B 1 97  ? -8.418  31.684  -31.944 1.00 17.22 ? 97  LEU   A O   1 
ATOM   2803 C  CB  . LEU   B 1 97  ? -6.627  29.104  -32.217 1.00 16.09 ? 97  LEU   A CB  1 
ATOM   2804 C  CG  . LEU   B 1 97  ? -5.731  29.144  -33.459 1.00 18.26 ? 97  LEU   A CG  1 
ATOM   2805 C  CD1 . LEU   B 1 97  ? -4.250  29.109  -33.102 1.00 16.34 ? 97  LEU   A CD1 1 
ATOM   2806 C  CD2 . LEU   B 1 97  ? -6.056  27.965  -34.368 1.00 17.55 ? 97  LEU   A CD2 1 
ATOM   2807 N  N   . HIS   B 1 98  ? -6.337  32.427  -32.420 1.00 14.31 ? 98  HIS   A N   1 
ATOM   2808 C  CA  . HIS   B 1 98  ? -6.764  33.464  -33.347 1.00 14.06 ? 98  HIS   A CA  1 
ATOM   2809 C  C   . HIS   B 1 98  ? -6.233  33.210  -34.766 1.00 14.84 ? 98  HIS   A C   1 
ATOM   2810 O  O   . HIS   B 1 98  ? -5.138  32.696  -34.971 1.00 15.68 ? 98  HIS   A O   1 
ATOM   2811 C  CB  . HIS   B 1 98  ? -6.180  34.782  -32.850 1.00 13.01 ? 98  HIS   A CB  1 
ATOM   2812 C  CG  . HIS   B 1 98  ? -6.607  35.102  -31.461 1.00 14.64 ? 98  HIS   A CG  1 
ATOM   2813 N  ND1 . HIS   B 1 98  ? -7.704  35.910  -31.191 1.00 15.72 ? 98  HIS   A ND1 1 
ATOM   2814 C  CD2 . HIS   B 1 98  ? -6.078  34.759  -30.266 1.00 14.44 ? 98  HIS   A CD2 1 
ATOM   2815 C  CE1 . HIS   B 1 98  ? -7.805  36.084  -29.888 1.00 13.85 ? 98  HIS   A CE1 1 
ATOM   2816 N  NE2 . HIS   B 1 98  ? -6.819  35.400  -29.305 1.00 14.31 ? 98  HIS   A NE2 1 
ATOM   2817 N  N   . TRP   B 1 99  ? -7.024  33.599  -35.758 1.00 14.21 ? 99  TRP   A N   1 
ATOM   2818 C  CA  . TRP   B 1 99  ? -6.698  33.478  -37.166 1.00 15.57 ? 99  TRP   A CA  1 
ATOM   2819 C  C   . TRP   B 1 99  ? -7.395  34.621  -37.891 1.00 15.98 ? 99  TRP   A C   1 
ATOM   2820 O  O   . TRP   B 1 99  ? -8.156  35.404  -37.286 1.00 16.49 ? 99  TRP   A O   1 
ATOM   2821 C  CB  . TRP   B 1 99  ? -7.159  32.103  -37.713 1.00 17.00 ? 99  TRP   A CB  1 
ATOM   2822 C  CG  . TRP   B 1 99  ? -8.628  31.850  -37.549 1.00 17.11 ? 99  TRP   A CG  1 
ATOM   2823 C  CD1 . TRP   B 1 99  ? -9.623  32.241  -38.405 1.00 18.13 ? 99  TRP   A CD1 1 
ATOM   2824 C  CD2 . TRP   B 1 99  ? -9.284  31.111  -36.495 1.00 16.68 ? 99  TRP   A CD2 1 
ATOM   2825 N  NE1 . TRP   B 1 99  ? -10.845 31.824  -37.942 1.00 17.76 ? 99  TRP   A NE1 1 
ATOM   2826 C  CE2 . TRP   B 1 99  ? -10.673 31.158  -36.756 1.00 17.35 ? 99  TRP   A CE2 1 
ATOM   2827 C  CE3 . TRP   B 1 99  ? -8.839  30.457  -35.336 1.00 16.14 ? 99  TRP   A CE3 1 
ATOM   2828 C  CZ2 . TRP   B 1 99  ? -11.615 30.538  -35.931 1.00 16.62 ? 99  TRP   A CZ2 1 
ATOM   2829 C  CZ3 . TRP   B 1 99  ? -9.771  29.839  -34.522 1.00 17.75 ? 99  TRP   A CZ3 1 
ATOM   2830 C  CH2 . TRP   B 1 99  ? -11.140 29.877  -34.816 1.00 17.79 ? 99  TRP   A CH2 1 
ATOM   2831 N  N   . GLY   B 1 100 ? -7.080  34.716  -39.186 1.00 16.61 ? 100 GLY   A N   1 
ATOM   2832 C  CA  . GLY   B 1 100 ? -7.605  35.723  -40.079 1.00 17.49 ? 100 GLY   A CA  1 
ATOM   2833 C  C   . GLY   B 1 100 ? -8.338  35.060  -41.239 1.00 18.12 ? 100 GLY   A C   1 
ATOM   2834 O  O   . GLY   B 1 100 ? -8.351  33.836  -41.362 1.00 17.05 ? 100 GLY   A O   1 
ATOM   2835 N  N   . SER   B 1 101 ? -8.938  35.884  -42.100 1.00 17.88 ? 101 SER   A N   1 
ATOM   2836 C  CA  . SER   B 1 101 ? -9.729  35.323  -43.187 1.00 20.51 ? 101 SER   A CA  1 
ATOM   2837 C  C   . SER   B 1 101 ? -8.838  34.897  -44.360 1.00 19.34 ? 101 SER   A C   1 
ATOM   2838 O  O   . SER   B 1 101 ? -9.319  34.227  -45.276 1.00 21.59 ? 101 SER   A O   1 
ATOM   2839 C  CB  . SER   B 1 101 ? -10.764 36.305  -43.631 1.00 19.70 ? 101 SER   A CB  1 
ATOM   2840 O  OG  . SER   B 1 101 ? -10.097 37.370  -44.288 1.00 24.42 ? 101 SER   A OG  1 
ATOM   2841 N  N   . ALA   B 1 102 ? -7.562  35.306  -44.337 1.00 19.21 ? 102 ALA   A N   1 
ATOM   2842 C  CA  . ALA   B 1 102 ? -6.564  34.770  -45.252 1.00 22.70 ? 102 ALA   A CA  1 
ATOM   2843 C  C   . ALA   B 1 102 ? -5.316  34.330  -44.476 1.00 22.61 ? 102 ALA   A C   1 
ATOM   2844 O  O   . ALA   B 1 102 ? -5.038  34.832  -43.382 1.00 20.19 ? 102 ALA   A O   1 
ATOM   2845 C  CB  . ALA   B 1 102 ? -6.235  35.788  -46.328 1.00 20.81 ? 102 ALA   A CB  1 
ATOM   2846 N  N   . ASP   B 1 103 ? -4.532  33.433  -45.093 1.00 22.26 ? 103 ASP   A N   1 
ATOM   2847 C  CA  . ASP   B 1 103 ? -3.370  32.837  -44.447 1.00 24.99 ? 103 ASP   A CA  1 
ATOM   2848 C  C   . ASP   B 1 103 ? -2.264  33.871  -44.192 1.00 25.98 ? 103 ASP   A C   1 
ATOM   2849 O  O   . ASP   B 1 103 ? -1.400  33.654  -43.342 1.00 23.82 ? 103 ASP   A O   1 
ATOM   2850 C  CB  . ASP   B 1 103 ? -2.799  31.700  -45.303 1.00 25.83 ? 103 ASP   A CB  1 
ATOM   2851 C  CG  . ASP   B 1 103 ? -3.674  30.452  -45.397 1.00 29.83 ? 103 ASP   A CG  1 
ATOM   2852 O  OD1 . ASP   B 1 103 ? -4.645  30.345  -44.629 1.00 31.05 ? 103 ASP   A OD1 1 
ATOM   2853 O  OD2 . ASP   B 1 103 ? -3.403  29.602  -46.294 1.00 31.76 ? 103 ASP   A OD2 1 
ATOM   2854 N  N   . ASP   B 1 104 ? -2.241  34.977  -44.940 1.00 26.91 ? 104 ASP   A N   1 
ATOM   2855 C  CA  . ASP   B 1 104 ? -1.089  35.878  -44.864 1.00 31.66 ? 104 ASP   A CA  1 
ATOM   2856 C  C   . ASP   B 1 104 ? -1.144  36.866  -43.687 1.00 33.53 ? 104 ASP   A C   1 
ATOM   2857 O  O   . ASP   B 1 104 ? -0.150  37.555  -43.431 1.00 36.42 ? 104 ASP   A O   1 
ATOM   2858 C  CB  . ASP   B 1 104 ? -0.846  36.584  -46.195 1.00 37.07 ? 104 ASP   A CB  1 
ATOM   2859 C  CG  . ASP   B 1 104 ? -2.110  37.235  -46.713 1.00 44.87 ? 104 ASP   A CG  1 
ATOM   2860 O  OD1 . ASP   B 1 104 ? -2.502  38.269  -46.139 1.00 50.08 ? 104 ASP   A OD1 1 
ATOM   2861 O  OD2 . ASP   B 1 104 ? -2.708  36.677  -47.664 1.00 50.12 ? 104 ASP   A OD2 1 
ATOM   2862 N  N   . HIS   B 1 105 ? -2.290  36.985  -42.992 1.00 29.81 ? 105 HIS   A N   1 
ATOM   2863 C  CA  . HIS   B 1 105 ? -2.345  37.746  -41.746 1.00 33.49 ? 105 HIS   A CA  1 
ATOM   2864 C  C   . HIS   B 1 105 ? -3.461  37.278  -40.804 1.00 33.41 ? 105 HIS   A C   1 
ATOM   2865 O  O   . HIS   B 1 105 ? -4.638  37.582  -40.993 1.00 36.57 ? 105 HIS   A O   1 
ATOM   2866 C  CB  . HIS   B 1 105 ? -2.352  39.270  -41.976 1.00 40.35 ? 105 HIS   A CB  1 
ATOM   2867 C  CG  . HIS   B 1 105 ? -3.656  39.854  -42.391 1.00 48.67 ? 105 HIS   A CG  1 
ATOM   2868 N  ND1 . HIS   B 1 105 ? -3.941  40.158  -43.713 1.00 54.54 ? 105 HIS   A ND1 1 
ATOM   2869 C  CD2 . HIS   B 1 105 ? -4.730  40.251  -41.669 1.00 56.66 ? 105 HIS   A CD2 1 
ATOM   2870 C  CE1 . HIS   B 1 105 ? -5.149  40.689  -43.790 1.00 61.11 ? 105 HIS   A CE1 1 
ATOM   2871 N  NE2 . HIS   B 1 105 ? -5.663  40.741  -42.544 1.00 60.89 ? 105 HIS   A NE2 1 
ATOM   2872 N  N   . GLY   B 1 106 ? -3.066  36.630  -39.712 1.00 30.40 ? 106 GLY   A N   1 
ATOM   2873 C  CA  . GLY   B 1 106 ? -4.045  36.157  -38.744 1.00 29.26 ? 106 GLY   A CA  1 
ATOM   2874 C  C   . GLY   B 1 106 ? -3.543  36.233  -37.305 1.00 25.94 ? 106 GLY   A C   1 
ATOM   2875 O  O   . GLY   B 1 106 ? -4.324  36.050  -36.366 1.00 27.44 ? 106 GLY   A O   1 
ATOM   2876 N  N   . SER   B 1 107 ? -2.241  36.491  -37.129 1.00 21.53 ? 107 SER   A N   1 
ATOM   2877 C  CA  . SER   B 1 107 ? -1.730  36.582  -35.766 1.00 19.87 ? 107 SER   A CA  1 
ATOM   2878 C  C   . SER   B 1 107 ? -2.169  37.898  -35.123 1.00 20.79 ? 107 SER   A C   1 
ATOM   2879 O  O   . SER   B 1 107 ? -2.593  38.833  -35.799 1.00 21.86 ? 107 SER   A O   1 
ATOM   2880 C  CB  . SER   B 1 107 ? -0.236  36.348  -35.674 1.00 17.98 ? 107 SER   A CB  1 
ATOM   2881 O  OG  . SER   B 1 107 ? 0.485   37.347  -36.384 1.00 18.26 ? 107 SER   A OG  1 
ATOM   2882 N  N   . GLU   B 1 108 ? -2.202  37.920  -33.791 1.00 18.35 ? 108 GLU   A N   1 
ATOM   2883 C  CA  . GLU   B 1 108 ? -2.552  39.155  -33.106 1.00 19.33 ? 108 GLU   A CA  1 
ATOM   2884 C  C   . GLU   B 1 108 ? -1.313  40.024  -32.965 1.00 17.67 ? 108 GLU   A C   1 
ATOM   2885 O  O   . GLU   B 1 108 ? -1.327  41.185  -33.346 1.00 16.26 ? 108 GLU   A O   1 
ATOM   2886 C  CB  . GLU   B 1 108 ? -3.139  38.811  -31.743 1.00 20.56 ? 108 GLU   A CB  1 
ATOM   2887 C  CG  . GLU   B 1 108 ? -4.505  38.206  -31.970 1.00 23.09 ? 108 GLU   A CG  1 
ATOM   2888 C  CD  . GLU   B 1 108 ? -5.488  38.571  -30.902 1.00 21.75 ? 108 GLU   A CD  1 
ATOM   2889 O  OE1 . GLU   B 1 108 ? -5.160  38.301  -29.734 1.00 22.02 ? 108 GLU   A OE1 1 
ATOM   2890 O  OE2 . GLU   B 1 108 ? -6.606  39.031  -31.262 1.00 22.51 ? 108 GLU   A OE2 1 
ATOM   2891 N  N   . HIS   B 1 109 ? -0.246  39.442  -32.415 1.00 16.61 ? 109 HIS   A N   1 
ATOM   2892 C  CA  . HIS   B 1 109 ? 1.023   40.174  -32.399 1.00 18.88 ? 109 HIS   A CA  1 
ATOM   2893 C  C   . HIS   B 1 109 ? 1.644   40.163  -33.803 1.00 17.99 ? 109 HIS   A C   1 
ATOM   2894 O  O   . HIS   B 1 109 ? 1.390   39.239  -34.575 1.00 16.98 ? 109 HIS   A O   1 
ATOM   2895 C  CB  . HIS   B 1 109 ? 1.959   39.587  -31.337 1.00 17.59 ? 109 HIS   A CB  1 
ATOM   2896 C  CG  . HIS   B 1 109 ? 1.457   39.808  -29.960 1.00 19.09 ? 109 HIS   A CG  1 
ATOM   2897 N  ND1 . HIS   B 1 109 ? 0.507   38.975  -29.371 1.00 18.99 ? 109 HIS   A ND1 1 
ATOM   2898 C  CD2 . HIS   B 1 109 ? 1.740   40.768  -29.062 1.00 16.89 ? 109 HIS   A CD2 1 
ATOM   2899 C  CE1 . HIS   B 1 109 ? 0.221   39.433  -28.170 1.00 18.74 ? 109 HIS   A CE1 1 
ATOM   2900 N  NE2 . HIS   B 1 109 ? 0.966   40.531  -27.968 1.00 19.08 ? 109 HIS   A NE2 1 
ATOM   2901 N  N   . ILE   B 1 110 ? 2.432   41.209  -34.123 1.00 18.38 ? 110 ILE   A N   1 
ATOM   2902 C  CA  . ILE   B 1 110 ? 3.151   41.384  -35.387 1.00 20.54 ? 110 ILE   A CA  1 
ATOM   2903 C  C   . ILE   B 1 110 ? 4.610   41.735  -35.073 1.00 19.40 ? 110 ILE   A C   1 
ATOM   2904 O  O   . ILE   B 1 110 ? 4.868   42.687  -34.343 1.00 24.76 ? 110 ILE   A O   1 
ATOM   2905 C  CB  . ILE   B 1 110 ? 2.507   42.471  -36.289 1.00 22.12 ? 110 ILE   A CB  1 
ATOM   2906 C  CG1 . ILE   B 1 110 ? 1.036   42.197  -36.641 1.00 25.47 ? 110 ILE   A CG1 1 
ATOM   2907 C  CG2 . ILE   B 1 110 ? 3.334   42.679  -37.550 1.00 23.29 ? 110 ILE   A CG2 1 
ATOM   2908 C  CD1 . ILE   B 1 110 ? 0.378   43.284  -37.520 1.00 26.32 ? 110 ILE   A CD1 1 
ATOM   2909 N  N   . VAL   B 1 111 ? 5.561   40.977  -35.650 1.00 19.97 ? 111 VAL   A N   1 
ATOM   2910 C  CA  . VAL   B 1 111 ? 6.982   41.091  -35.375 1.00 22.04 ? 111 VAL   A CA  1 
ATOM   2911 C  C   . VAL   B 1 111 ? 7.705   41.709  -36.575 1.00 26.63 ? 111 VAL   A C   1 
ATOM   2912 O  O   . VAL   B 1 111 ? 7.808   41.083  -37.632 1.00 25.13 ? 111 VAL   A O   1 
ATOM   2913 C  CB  . VAL   B 1 111 ? 7.572   39.696  -35.088 1.00 25.37 ? 111 VAL   A CB  1 
ATOM   2914 C  CG1 . VAL   B 1 111 ? 9.049   39.788  -34.708 1.00 25.55 ? 111 VAL   A CG1 1 
ATOM   2915 C  CG2 . VAL   B 1 111 ? 6.754   38.973  -34.014 1.00 22.08 ? 111 VAL   A CG2 1 
ATOM   2916 N  N   . ASP   B 1 112 ? 8.222   42.923  -36.391 1.00 25.30 ? 112 ASP   A N   1 
ATOM   2917 C  CA  . ASP   B 1 112 ? 8.928   43.635  -37.451 1.00 27.76 ? 112 ASP   A CA  1 
ATOM   2918 C  C   . ASP   B 1 112 ? 8.107   43.672  -38.742 1.00 27.67 ? 112 ASP   A C   1 
ATOM   2919 O  O   . ASP   B 1 112 ? 8.660   43.536  -39.843 1.00 29.89 ? 112 ASP   A O   1 
ATOM   2920 C  CB  . ASP   B 1 112 ? 10.312  43.030  -37.698 1.00 28.56 ? 112 ASP   A CB  1 
ATOM   2921 C  CG  . ASP   B 1 112 ? 11.301  43.279  -36.571 1.00 30.57 ? 112 ASP   A CG  1 
ATOM   2922 O  OD1 . ASP   B 1 112 ? 11.230  44.362  -35.933 1.00 30.90 ? 112 ASP   A OD1 1 
ATOM   2923 O  OD2 . ASP   B 1 112 ? 12.133  42.377  -36.328 1.00 32.78 ? 112 ASP   A OD2 1 
ATOM   2924 N  N   . GLY   B 1 113 ? 6.796   43.878  -38.596 1.00 24.41 ? 113 GLY   A N   1 
ATOM   2925 C  CA  . GLY   B 1 113 ? 5.881   44.024  -39.718 1.00 24.58 ? 113 GLY   A CA  1 
ATOM   2926 C  C   . GLY   B 1 113 ? 5.404   42.682  -40.267 1.00 25.76 ? 113 GLY   A C   1 
ATOM   2927 O  O   . GLY   B 1 113 ? 4.582   42.654  -41.176 1.00 27.64 ? 113 GLY   A O   1 
ATOM   2928 N  N   . VAL   B 1 114 ? 5.912   41.575  -39.706 1.00 26.54 ? 114 VAL   A N   1 
ATOM   2929 C  CA  . VAL   B 1 114 ? 5.583   40.253  -40.216 1.00 27.15 ? 114 VAL   A CA  1 
ATOM   2930 C  C   . VAL   B 1 114 ? 4.430   39.654  -39.407 1.00 25.82 ? 114 VAL   A C   1 
ATOM   2931 O  O   . VAL   B 1 114 ? 4.525   39.508  -38.178 1.00 24.25 ? 114 VAL   A O   1 
ATOM   2932 C  CB  . VAL   B 1 114 ? 6.810   39.313  -40.234 1.00 29.89 ? 114 VAL   A CB  1 
ATOM   2933 C  CG1 . VAL   B 1 114 ? 6.430   37.902  -40.682 1.00 32.91 ? 114 VAL   A CG1 1 
ATOM   2934 C  CG2 . VAL   B 1 114 ? 7.952   39.867  -41.090 1.00 31.28 ? 114 VAL   A CG2 1 
ATOM   2935 N  N   . SER   B 1 115 ? 3.351   39.307  -40.122 1.00 23.20 ? 115 SER   A N   1 
ATOM   2936 C  CA  . SER   B 1 115 ? 2.224   38.618  -39.521 1.00 24.07 ? 115 SER   A CA  1 
ATOM   2937 C  C   . SER   B 1 115 ? 2.411   37.122  -39.719 1.00 23.35 ? 115 SER   A C   1 
ATOM   2938 O  O   . SER   B 1 115 ? 2.974   36.708  -40.721 1.00 22.75 ? 115 SER   A O   1 
ATOM   2939 C  CB  . SER   B 1 115 ? 0.919   39.062  -40.108 1.00 25.23 ? 115 SER   A CB  1 
ATOM   2940 O  OG  . SER   B 1 115 ? 0.626   40.382  -39.715 1.00 30.02 ? 115 SER   A OG  1 
ATOM   2941 N  N   . TYR   B 1 116 ? 1.917   36.323  -38.772 1.00 20.67 ? 116 TYR   A N   1 
ATOM   2942 C  CA  . TYR   B 1 116 ? 1.820   34.887  -38.971 1.00 18.98 ? 116 TYR   A CA  1 
ATOM   2943 C  C   . TYR   B 1 116 ? 0.381   34.525  -39.342 1.00 19.60 ? 116 TYR   A C   1 
ATOM   2944 O  O   . TYR   B 1 116 ? -0.491  35.380  -39.364 1.00 17.85 ? 116 TYR   A O   1 
ATOM   2945 C  CB  . TYR   B 1 116 ? 2.360   34.158  -37.733 1.00 21.33 ? 116 TYR   A CB  1 
ATOM   2946 C  CG  . TYR   B 1 116 ? 3.828   34.440  -37.526 1.00 22.52 ? 116 TYR   A CG  1 
ATOM   2947 C  CD1 . TYR   B 1 116 ? 4.780   33.716  -38.231 1.00 24.79 ? 116 TYR   A CD1 1 
ATOM   2948 C  CD2 . TYR   B 1 116 ? 4.262   35.453  -36.686 1.00 22.62 ? 116 TYR   A CD2 1 
ATOM   2949 C  CE1 . TYR   B 1 116 ? 6.138   33.953  -38.089 1.00 24.33 ? 116 TYR   A CE1 1 
ATOM   2950 C  CE2 . TYR   B 1 116 ? 5.622   35.698  -36.522 1.00 27.61 ? 116 TYR   A CE2 1 
ATOM   2951 C  CZ  . TYR   B 1 116 ? 6.553   34.951  -37.230 1.00 27.38 ? 116 TYR   A CZ  1 
ATOM   2952 O  OH  . TYR   B 1 116 ? 7.892   35.158  -37.133 1.00 30.84 ? 116 TYR   A OH  1 
ATOM   2953 N  N   . ALA   B 1 117 ? 0.159   33.254  -39.687 1.00 17.15 ? 117 ALA   A N   1 
ATOM   2954 C  CA  . ALA   B 1 117 ? -1.154  32.795  -40.122 1.00 17.44 ? 117 ALA   A CA  1 
ATOM   2955 C  C   . ALA   B 1 117 ? -2.140  32.697  -38.952 1.00 16.85 ? 117 ALA   A C   1 
ATOM   2956 O  O   . ALA   B 1 117 ? -3.351  32.849  -39.131 1.00 19.76 ? 117 ALA   A O   1 
ATOM   2957 C  CB  . ALA   B 1 117 ? -1.002  31.445  -40.805 1.00 19.31 ? 117 ALA   A CB  1 
ATOM   2958 N  N   . ALA   B 1 118 ? -1.630  32.431  -37.738 1.00 16.50 ? 118 ALA   A N   1 
ATOM   2959 C  CA  . ALA   B 1 118 ? -2.474  32.307  -36.563 1.00 15.28 ? 118 ALA   A CA  1 
ATOM   2960 C  C   . ALA   B 1 118 ? -1.616  32.487  -35.320 1.00 15.26 ? 118 ALA   A C   1 
ATOM   2961 O  O   . ALA   B 1 118 ? -0.391  32.514  -35.434 1.00 15.47 ? 118 ALA   A O   1 
ATOM   2962 C  CB  . ALA   B 1 118 ? -3.200  30.974  -36.539 1.00 14.90 ? 118 ALA   A CB  1 
ATOM   2963 N  N   . GLU   B 1 119 ? -2.283  32.539  -34.149 1.00 14.35 ? 119 GLU   A N   1 
ATOM   2964 C  CA  . GLU   B 1 119 ? -1.595  32.654  -32.868 1.00 16.62 ? 119 GLU   A CA  1 
ATOM   2965 C  C   . GLU   B 1 119 ? -2.373  31.892  -31.790 1.00 15.06 ? 119 GLU   A C   1 
ATOM   2966 O  O   . GLU   B 1 119 ? -3.555  32.125  -31.588 1.00 15.16 ? 119 GLU   A O   1 
ATOM   2967 C  CB  . GLU   B 1 119 ? -1.434  34.146  -32.557 1.00 17.79 ? 119 GLU   A CB  1 
ATOM   2968 C  CG  . GLU   B 1 119 ? -0.571  34.474  -31.341 1.00 20.60 ? 119 GLU   A CG  1 
ATOM   2969 C  CD  . GLU   B 1 119 ? -0.392  35.985  -31.151 1.00 21.80 ? 119 GLU   A CD  1 
ATOM   2970 O  OE1 . GLU   B 1 119 ? -0.269  36.702  -32.174 1.00 24.38 ? 119 GLU   A OE1 1 
ATOM   2971 O  OE2 . GLU   B 1 119 ? -0.424  36.464  -29.992 1.00 22.58 ? 119 GLU   A OE2 1 
ATOM   2972 N  N   . LEU   B 1 120 ? -1.702  30.959  -31.113 1.00 14.50 ? 120 LEU   A N   1 
ATOM   2973 C  CA  . LEU   B 1 120 ? -2.286  30.206  -30.014 1.00 15.99 ? 120 LEU   A CA  1 
ATOM   2974 C  C   . LEU   B 1 120 ? -2.022  30.976  -28.715 1.00 16.44 ? 120 LEU   A C   1 
ATOM   2975 O  O   . LEU   B 1 120 ? -0.897  31.406  -28.483 1.00 14.36 ? 120 LEU   A O   1 
ATOM   2976 C  CB  . LEU   B 1 120 ? -1.571  28.845  -30.003 1.00 18.35 ? 120 LEU   A CB  1 
ATOM   2977 C  CG  . LEU   B 1 120 ? -2.157  27.776  -29.084 1.00 21.19 ? 120 LEU   A CG  1 
ATOM   2978 C  CD1 . LEU   B 1 120 ? -3.442  27.216  -29.660 1.00 19.96 ? 120 LEU   A CD1 1 
ATOM   2979 C  CD2 . LEU   B 1 120 ? -1.118  26.668  -28.876 1.00 21.93 ? 120 LEU   A CD2 1 
ATOM   2980 N  N   . HIS   B 1 121 ? -3.072  31.157  -27.881 1.00 14.79 ? 121 HIS   A N   1 
ATOM   2981 C  CA  . HIS   B 1 121 ? -2.952  31.735  -26.559 1.00 14.48 ? 121 HIS   A CA  1 
ATOM   2982 C  C   . HIS   B 1 121 ? -3.235  30.684  -25.498 1.00 14.65 ? 121 HIS   A C   1 
ATOM   2983 O  O   . HIS   B 1 121 ? -4.205  29.921  -25.616 1.00 15.79 ? 121 HIS   A O   1 
ATOM   2984 C  CB  . HIS   B 1 121 ? -3.902  32.951  -26.405 1.00 14.88 ? 121 HIS   A CB  1 
ATOM   2985 C  CG  . HIS   B 1 121 ? -3.485  34.131  -27.230 1.00 16.92 ? 121 HIS   A CG  1 
ATOM   2986 N  ND1 . HIS   B 1 121 ? -4.319  35.226  -27.466 1.00 17.70 ? 121 HIS   A ND1 1 
ATOM   2987 C  CD2 . HIS   B 1 121 ? -2.322  34.395  -27.860 1.00 17.23 ? 121 HIS   A CD2 1 
ATOM   2988 C  CE1 . HIS   B 1 121 ? -3.661  36.114  -28.211 1.00 17.02 ? 121 HIS   A CE1 1 
ATOM   2989 N  NE2 . HIS   B 1 121 ? -2.448  35.629  -28.474 1.00 16.12 ? 121 HIS   A NE2 1 
ATOM   2990 N  N   . VAL   B 1 122 ? -2.362  30.662  -24.481 1.00 15.48 ? 122 VAL   A N   1 
ATOM   2991 C  CA  . VAL   B 1 122 ? -2.466  29.782  -23.326 1.00 13.29 ? 122 VAL   A CA  1 
ATOM   2992 C  C   . VAL   B 1 122 ? -2.628  30.706  -22.125 1.00 12.91 ? 122 VAL   A C   1 
ATOM   2993 O  O   . VAL   B 1 122 ? -1.715  31.489  -21.847 1.00 12.37 ? 122 VAL   A O   1 
ATOM   2994 C  CB  . VAL   B 1 122 ? -1.241  28.865  -23.159 1.00 13.16 ? 122 VAL   A CB  1 
ATOM   2995 C  CG1 . VAL   B 1 122 ? -1.485  27.838  -22.046 1.00 13.54 ? 122 VAL   A CG1 1 
ATOM   2996 C  CG2 . VAL   B 1 122 ? -0.935  28.142  -24.456 1.00 14.84 ? 122 VAL   A CG2 1 
ATOM   2997 N  N   . VAL   B 1 123 ? -3.804  30.639  -21.485 1.00 11.76 ? 123 VAL   A N   1 
ATOM   2998 C  CA  . VAL   B 1 123 ? -4.170  31.666  -20.512 1.00 13.62 ? 123 VAL   A CA  1 
ATOM   2999 C  C   . VAL   B 1 123 ? -4.014  31.092  -19.103 1.00 13.73 ? 123 VAL   A C   1 
ATOM   3000 O  O   . VAL   B 1 123 ? -4.543  30.009  -18.829 1.00 14.03 ? 123 VAL   A O   1 
ATOM   3001 C  CB  . VAL   B 1 123 ? -5.625  32.116  -20.716 1.00 13.80 ? 123 VAL   A CB  1 
ATOM   3002 C  CG1 . VAL   B 1 123 ? -6.035  33.145  -19.672 1.00 15.04 ? 123 VAL   A CG1 1 
ATOM   3003 C  CG2 . VAL   B 1 123 ? -5.868  32.613  -22.149 1.00 13.98 ? 123 VAL   A CG2 1 
ATOM   3004 N  N   . HIS   B 1 124 ? -3.320  31.826  -18.226 1.00 13.41 ? 124 HIS   A N   1 
ATOM   3005 C  CA  . HIS   B 1 124 ? -3.043  31.385  -16.863 1.00 15.38 ? 124 HIS   A CA  1 
ATOM   3006 C  C   . HIS   B 1 124 ? -3.484  32.455  -15.879 1.00 16.67 ? 124 HIS   A C   1 
ATOM   3007 O  O   . HIS   B 1 124 ? -3.492  33.624  -16.247 1.00 16.57 ? 124 HIS   A O   1 
ATOM   3008 C  CB  . HIS   B 1 124 ? -1.529  31.178  -16.651 1.00 13.90 ? 124 HIS   A CB  1 
ATOM   3009 C  CG  . HIS   B 1 124 ? -0.878  30.394  -17.739 1.00 13.83 ? 124 HIS   A CG  1 
ATOM   3010 N  ND1 . HIS   B 1 124 ? -0.693  30.911  -19.006 1.00 14.52 ? 124 HIS   A ND1 1 
ATOM   3011 C  CD2 . HIS   B 1 124 ? -0.381  29.131  -17.778 1.00 14.94 ? 124 HIS   A CD2 1 
ATOM   3012 C  CE1 . HIS   B 1 124 ? -0.082  30.002  -19.773 1.00 16.10 ? 124 HIS   A CE1 1 
ATOM   3013 N  NE2 . HIS   B 1 124 ? 0.139   28.922  -19.040 1.00 13.84 ? 124 HIS   A NE2 1 
ATOM   3014 N  N   . TRP   B 1 125 ? -3.717  32.072  -14.607 1.00 16.29 ? 125 TRP   A N   1 
ATOM   3015 C  CA  . TRP   B 1 125 ? -4.093  33.048  -13.579 1.00 16.65 ? 125 TRP   A CA  1 
ATOM   3016 C  C   . TRP   B 1 125 ? -3.326  32.796  -12.273 1.00 15.78 ? 125 TRP   A C   1 
ATOM   3017 O  O   . TRP   B 1 125 ? -2.943  31.671  -11.952 1.00 15.97 ? 125 TRP   A O   1 
ATOM   3018 C  CB  . TRP   B 1 125 ? -5.612  33.101  -13.353 1.00 16.38 ? 125 TRP   A CB  1 
ATOM   3019 C  CG  . TRP   B 1 125 ? -6.226  31.807  -12.892 1.00 16.40 ? 125 TRP   A CG  1 
ATOM   3020 C  CD1 . TRP   B 1 125 ? -6.624  30.769  -13.683 1.00 17.66 ? 125 TRP   A CD1 1 
ATOM   3021 C  CD2 . TRP   B 1 125 ? -6.555  31.419  -11.539 1.00 16.65 ? 125 TRP   A CD2 1 
ATOM   3022 N  NE1 . TRP   B 1 125 ? -7.173  29.758  -12.917 1.00 15.93 ? 125 TRP   A NE1 1 
ATOM   3023 C  CE2 . TRP   B 1 125 ? -7.114  30.124  -11.596 1.00 16.68 ? 125 TRP   A CE2 1 
ATOM   3024 C  CE3 . TRP   B 1 125 ? -6.402  32.024  -10.271 1.00 17.57 ? 125 TRP   A CE3 1 
ATOM   3025 C  CZ2 . TRP   B 1 125 ? -7.575  29.452  -10.445 1.00 16.86 ? 125 TRP   A CZ2 1 
ATOM   3026 C  CZ3 . TRP   B 1 125 ? -6.848  31.364  -9.144  1.00 15.67 ? 125 TRP   A CZ3 1 
ATOM   3027 C  CH2 . TRP   B 1 125 ? -7.392  30.074  -9.227  1.00 16.48 ? 125 TRP   A CH2 1 
ATOM   3028 N  N   . ASN   B 1 126 ? -3.048  33.880  -11.554 1.00 15.93 ? 126 ASN   A N   1 
ATOM   3029 C  CA  . ASN   B 1 126 ? -2.172  33.890  -10.395 1.00 17.36 ? 126 ASN   A CA  1 
ATOM   3030 C  C   . ASN   B 1 126 ? -2.919  33.302  -9.188  1.00 17.33 ? 126 ASN   A C   1 
ATOM   3031 O  O   . ASN   B 1 126 ? -3.725  33.976  -8.539  1.00 18.72 ? 126 ASN   A O   1 
ATOM   3032 C  CB  . ASN   B 1 126 ? -1.661  35.320  -10.167 1.00 20.06 ? 126 ASN   A CB  1 
ATOM   3033 C  CG  . ASN   B 1 126 ? -0.781  35.509  -8.949  1.00 23.90 ? 126 ASN   A CG  1 
ATOM   3034 O  OD1 . ASN   B 1 126 ? -0.693  34.629  -8.084  1.00 25.76 ? 126 ASN   A OD1 1 
ATOM   3035 N  ND2 . ASN   B 1 126 ? -0.154  36.674  -8.855  1.00 22.68 ? 126 ASN   A ND2 1 
ATOM   3036 N  N   . SER   B 1 127 ? -2.654  32.027  -8.878  1.00 17.93 ? 127 SER   A N   1 
ATOM   3037 C  CA  . SER   B 1 127 ? -3.421  31.338  -7.849  1.00 18.32 ? 127 SER   A CA  1 
ATOM   3038 C  C   . SER   B 1 127 ? -2.763  31.501  -6.468  1.00 22.59 ? 127 SER   A C   1 
ATOM   3039 O  O   . SER   B 1 127 ? -3.335  31.130  -5.429  1.00 21.08 ? 127 SER   A O   1 
ATOM   3040 C  CB  . SER   B 1 127 ? -3.594  29.891  -8.265  1.00 20.18 ? 127 SER   A CB  1 
ATOM   3041 O  OG  . SER   B 1 127 ? -2.308  29.281  -8.332  1.00 23.95 ? 127 SER   A OG  1 
ATOM   3042 N  N   . ASP   B 1 128 ? -1.578  32.128  -6.446  1.00 19.77 ? 128 ASP   A N   1 
ATOM   3043 C  CA  . ASP   B 1 128 ? -0.917  32.486  -5.209  1.00 24.09 ? 128 ASP   A CA  1 
ATOM   3044 C  C   . ASP   B 1 128 ? -1.584  33.700  -4.557  1.00 24.87 ? 128 ASP   A C   1 
ATOM   3045 O  O   . ASP   B 1 128 ? -1.479  33.812  -3.339  1.00 24.07 ? 128 ASP   A O   1 
ATOM   3046 C  CB  . ASP   B 1 128 ? 0.587   32.734  -5.389  1.00 26.45 ? 128 ASP   A CB  1 
ATOM   3047 C  CG  . ASP   B 1 128 ? 1.395   31.465  -5.641  1.00 29.31 ? 128 ASP   A CG  1 
ATOM   3048 O  OD1 . ASP   B 1 128 ? 0.836   30.345  -5.489  1.00 27.55 ? 128 ASP   A OD1 1 
ATOM   3049 O  OD2 . ASP   B 1 128 ? 2.565   31.603  -6.034  1.00 30.66 ? 128 ASP   A OD2 1 
ATOM   3050 N  N   . LYS   B 1 129 ? -2.312  34.546  -5.320  1.00 21.63 ? 129 LYS   A N   1 
ATOM   3051 C  CA  . LYS   B 1 129 ? -2.900  35.770  -4.752  1.00 20.78 ? 129 LYS   A CA  1 
ATOM   3052 C  C   . LYS   B 1 129 ? -4.422  35.851  -4.869  1.00 20.88 ? 129 LYS   A C   1 
ATOM   3053 O  O   . LYS   B 1 129 ? -5.059  36.607  -4.111  1.00 19.16 ? 129 LYS   A O   1 
ATOM   3054 C  CB  . LYS   B 1 129 ? -2.325  37.024  -5.413  1.00 23.90 ? 129 LYS   A CB  1 
ATOM   3055 C  CG  . LYS   B 1 129 ? -0.831  37.245  -5.186  1.00 26.98 ? 129 LYS   A CG  1 
ATOM   3056 C  CD  . LYS   B 1 129 ? -0.371  38.611  -5.644  1.00 30.74 ? 129 LYS   A CD  1 
ATOM   3057 C  CE  . LYS   B 1 129 ? -1.048  39.758  -4.921  1.00 31.62 ? 129 LYS   A CE  1 
ATOM   3058 N  NZ  . LYS   B 1 129 ? -0.702  41.075  -5.524  1.00 33.94 ? 129 LYS   A NZ  1 
ATOM   3059 N  N   . TYR   B 1 130 ? -5.007  35.121  -5.835  1.00 17.74 ? 130 TYR   A N   1 
ATOM   3060 C  CA  . TYR   B 1 130 ? -6.406  35.336  -6.174  1.00 20.33 ? 130 TYR   A CA  1 
ATOM   3061 C  C   . TYR   B 1 130 ? -7.150  34.019  -6.096  1.00 20.26 ? 130 TYR   A C   1 
ATOM   3062 O  O   . TYR   B 1 130 ? -6.527  32.970  -6.248  1.00 19.63 ? 130 TYR   A O   1 
ATOM   3063 C  CB  . TYR   B 1 130 ? -6.555  36.028  -7.537  1.00 20.07 ? 130 TYR   A CB  1 
ATOM   3064 C  CG  . TYR   B 1 130 ? -5.755  37.309  -7.554  1.00 21.52 ? 130 TYR   A CG  1 
ATOM   3065 C  CD1 . TYR   B 1 130 ? -6.097  38.358  -6.712  1.00 22.96 ? 130 TYR   A CD1 1 
ATOM   3066 C  CD2 . TYR   B 1 130 ? -4.623  37.436  -8.337  1.00 21.42 ? 130 TYR   A CD2 1 
ATOM   3067 C  CE1 . TYR   B 1 130 ? -5.328  39.512  -6.668  1.00 23.31 ? 130 TYR   A CE1 1 
ATOM   3068 C  CE2 . TYR   B 1 130 ? -3.847  38.584  -8.324  1.00 21.45 ? 130 TYR   A CE2 1 
ATOM   3069 C  CZ  . TYR   B 1 130 ? -4.212  39.625  -7.481  1.00 23.21 ? 130 TYR   A CZ  1 
ATOM   3070 O  OH  . TYR   B 1 130 ? -3.465  40.768  -7.427  1.00 21.99 ? 130 TYR   A OH  1 
ATOM   3071 N  N   . PRO   B 1 131 ? -8.464  34.034  -5.798  1.00 21.20 ? 131 PRO   A N   1 
ATOM   3072 C  CA  . PRO   B 1 131 ? -9.218  32.782  -5.674  1.00 23.03 ? 131 PRO   A CA  1 
ATOM   3073 C  C   . PRO   B 1 131 ? -9.717  32.139  -6.959  1.00 23.84 ? 131 PRO   A C   1 
ATOM   3074 O  O   . PRO   B 1 131 ? -10.083 30.955  -6.962  1.00 24.11 ? 131 PRO   A O   1 
ATOM   3075 C  CB  . PRO   B 1 131 ? -10.427 33.200  -4.824  1.00 22.42 ? 131 PRO   A CB  1 
ATOM   3076 C  CG  . PRO   B 1 131 ? -10.658 34.653  -5.206  1.00 22.03 ? 131 PRO   A CG  1 
ATOM   3077 C  CD  . PRO   B 1 131 ? -9.254  35.211  -5.382  1.00 21.75 ? 131 PRO   A CD  1 
ATOM   3078 N  N   . SER   B 1 132 ? -9.738  32.915  -8.050  1.00 20.74 ? 132 SER   A N   1 
ATOM   3079 C  CA  . SER   B 1 132 ? -10.406 32.460  -9.251  1.00 21.66 ? 132 SER   A CA  1 
ATOM   3080 C  C   . SER   B 1 132 ? -9.787  33.195  -10.420 1.00 21.01 ? 132 SER   A C   1 
ATOM   3081 O  O   . SER   B 1 132 ? -9.246  34.285  -10.209 1.00 20.80 ? 132 SER   A O   1 
ATOM   3082 C  CB  . SER   B 1 132 ? -11.877 32.801  -9.180  1.00 21.27 ? 132 SER   A CB  1 
ATOM   3083 O  OG  . SER   B 1 132 ? -12.023 34.203  -9.016  1.00 24.06 ? 132 SER   A OG  1 
ATOM   3084 N  N   . PHE   B 1 133 ? -9.970  32.626  -11.621 1.00 20.62 ? 133 PHE   A N   1 
ATOM   3085 C  CA  . PHE   B 1 133 ? -9.681  33.359  -12.845 1.00 21.65 ? 133 PHE   A CA  1 
ATOM   3086 C  C   . PHE   B 1 133 ? -10.406 34.713  -12.834 1.00 21.05 ? 133 PHE   A C   1 
ATOM   3087 O  O   . PHE   B 1 133 ? -9.815  35.766  -13.104 1.00 21.82 ? 133 PHE   A O   1 
ATOM   3088 C  CB  . PHE   B 1 133 ? -10.025 32.542  -14.094 1.00 25.38 ? 133 PHE   A CB  1 
ATOM   3089 C  CG  . PHE   B 1 133 ? -9.787  33.363  -15.335 1.00 28.53 ? 133 PHE   A CG  1 
ATOM   3090 C  CD1 . PHE   B 1 133 ? -10.743 34.266  -15.780 1.00 28.43 ? 133 PHE   A CD1 1 
ATOM   3091 C  CD2 . PHE   B 1 133 ? -8.564  33.322  -15.982 1.00 27.48 ? 133 PHE   A CD2 1 
ATOM   3092 C  CE1 . PHE   B 1 133 ? -10.501 35.084  -16.874 1.00 35.04 ? 133 PHE   A CE1 1 
ATOM   3093 C  CE2 . PHE   B 1 133 ? -8.339  34.121  -17.096 1.00 32.25 ? 133 PHE   A CE2 1 
ATOM   3094 C  CZ  . PHE   B 1 133 ? -9.291  35.011  -17.530 1.00 33.43 ? 133 PHE   A CZ  1 
ATOM   3095 N  N   . VAL   B 1 134 ? -11.688 34.697  -12.465 1.00 22.22 ? 134 VAL   A N   1 
ATOM   3096 C  CA  . VAL   B 1 134 ? -12.474 35.913  -12.633 1.00 26.60 ? 134 VAL   A CA  1 
ATOM   3097 C  C   . VAL   B 1 134 ? -11.907 37.052  -11.792 1.00 27.16 ? 134 VAL   A C   1 
ATOM   3098 O  O   . VAL   B 1 134 ? -11.852 38.195  -12.257 1.00 30.74 ? 134 VAL   A O   1 
ATOM   3099 C  CB  . VAL   B 1 134 ? -13.992 35.719  -12.435 1.00 30.76 ? 134 VAL   A CB  1 
ATOM   3100 C  CG1 . VAL   B 1 134 ? -14.612 34.965  -13.604 1.00 34.16 ? 134 VAL   A CG1 1 
ATOM   3101 C  CG2 . VAL   B 1 134 ? -14.315 35.018  -11.139 1.00 33.30 ? 134 VAL   A CG2 1 
ATOM   3102 N  N   A GLU   B 1 135 ? -11.464 36.761  -10.562 0.50 24.55 ? 135 GLU   A N   1 
ATOM   3103 N  N   B GLU   B 1 135 ? -11.508 36.732  -10.555 0.50 25.16 ? 135 GLU   A N   1 
ATOM   3104 C  CA  A GLU   B 1 135 ? -10.980 37.851  -9.731  0.50 24.99 ? 135 GLU   A CA  1 
ATOM   3105 C  CA  B GLU   B 1 135 ? -10.971 37.736  -9.656  0.50 26.02 ? 135 GLU   A CA  1 
ATOM   3106 C  C   A GLU   B 1 135 ? -9.546  38.240  -10.094 0.50 22.33 ? 135 GLU   A C   1 
ATOM   3107 C  C   B GLU   B 1 135 ? -9.624  38.222  -10.193 0.50 22.80 ? 135 GLU   A C   1 
ATOM   3108 O  O   A GLU   B 1 135 ? -9.162  39.395  -9.933  0.50 21.29 ? 135 GLU   A O   1 
ATOM   3109 O  O   B GLU   B 1 135 ? -9.411  39.423  -10.301 0.50 21.53 ? 135 GLU   A O   1 
ATOM   3110 C  CB  A GLU   B 1 135 ? -11.192 37.597  -8.236  0.50 27.25 ? 135 GLU   A CB  1 
ATOM   3111 C  CB  B GLU   B 1 135 ? -10.920 37.212  -8.216  0.50 29.04 ? 135 GLU   A CB  1 
ATOM   3112 C  CG  A GLU   B 1 135 ? -11.284 38.903  -7.457  0.50 29.58 ? 135 GLU   A CG  1 
ATOM   3113 C  CG  B GLU   B 1 135 ? -11.672 38.084  -7.219  0.50 35.21 ? 135 GLU   A CG  1 
ATOM   3114 C  CD  A GLU   B 1 135 ? -9.943  39.607  -7.435  0.50 29.28 ? 135 GLU   A CD  1 
ATOM   3115 C  CD  B GLU   B 1 135 ? -13.172 38.224  -7.425  0.50 35.61 ? 135 GLU   A CD  1 
ATOM   3116 O  OE1 A GLU   B 1 135 ? -8.922  38.885  -7.324  0.50 31.53 ? 135 GLU   A OE1 1 
ATOM   3117 O  OE1 B GLU   B 1 135 ? -13.668 37.774  -8.478  0.50 38.59 ? 135 GLU   A OE1 1 
ATOM   3118 O  OE2 A GLU   B 1 135 ? -9.909  40.849  -7.557  0.50 24.29 ? 135 GLU   A OE2 1 
ATOM   3119 O  OE2 B GLU   B 1 135 ? -13.844 38.767  -6.529  0.50 36.14 ? 135 GLU   A OE2 1 
ATOM   3120 N  N   . ALA   B 1 136 ? -8.756  37.274  -10.580 1.00 20.23 ? 136 ALA   A N   1 
ATOM   3121 C  CA  . ALA   B 1 136 ? -7.421  37.558  -11.085 1.00 20.49 ? 136 ALA   A CA  1 
ATOM   3122 C  C   . ALA   B 1 136 ? -7.481  38.522  -12.280 1.00 18.81 ? 136 ALA   A C   1 
ATOM   3123 O  O   . ALA   B 1 136 ? -6.607  39.380  -12.427 1.00 22.91 ? 136 ALA   A O   1 
ATOM   3124 C  CB  . ALA   B 1 136 ? -6.725  36.254  -11.452 1.00 16.78 ? 136 ALA   A CB  1 
ATOM   3125 N  N   . ALA   B 1 137 ? -8.490  38.364  -13.150 1.00 21.01 ? 137 ALA   A N   1 
ATOM   3126 C  CA  . ALA   B 1 137 ? -8.583  39.171  -14.362 1.00 23.48 ? 137 ALA   A CA  1 
ATOM   3127 C  C   . ALA   B 1 137 ? -8.739  40.666  -14.068 1.00 25.18 ? 137 ALA   A C   1 
ATOM   3128 O  O   . ALA   B 1 137 ? -8.622  41.445  -15.005 1.00 27.39 ? 137 ALA   A O   1 
ATOM   3129 C  CB  . ALA   B 1 137 ? -9.676  38.702  -15.278 1.00 22.53 ? 137 ALA   A CB  1 
ATOM   3130 N  N   . HIS   B 1 138 ? -9.005  41.056  -12.809 1.00 26.42 ? 138 HIS   A N   1 
ATOM   3131 C  CA  . HIS   B 1 138 ? -9.205  42.470  -12.466 1.00 28.72 ? 138 HIS   A CA  1 
ATOM   3132 C  C   . HIS   B 1 138 ? -7.991  43.101  -11.793 1.00 30.29 ? 138 HIS   A C   1 
ATOM   3133 O  O   . HIS   B 1 138 ? -8.088  44.213  -11.268 1.00 28.33 ? 138 HIS   A O   1 
ATOM   3134 C  CB  . HIS   B 1 138 ? -10.436 42.659  -11.575 1.00 28.49 ? 138 HIS   A CB  1 
ATOM   3135 C  CG  . HIS   B 1 138 ? -11.688 42.435  -12.341 1.00 34.80 ? 138 HIS   A CG  1 
ATOM   3136 N  ND1 . HIS   B 1 138 ? -12.334 43.460  -13.029 1.00 36.70 ? 138 HIS   A ND1 1 
ATOM   3137 C  CD2 . HIS   B 1 138 ? -12.391 41.309  -12.581 1.00 34.41 ? 138 HIS   A CD2 1 
ATOM   3138 C  CE1 . HIS   B 1 138 ? -13.384 42.971  -13.650 1.00 34.54 ? 138 HIS   A CE1 1 
ATOM   3139 N  NE2 . HIS   B 1 138 ? -13.444 41.657  -13.384 1.00 37.39 ? 138 HIS   A NE2 1 
ATOM   3140 N  N   . GLU   B 1 139 ? -6.863  42.382  -11.769 1.00 26.46 ? 139 GLU   A N   1 
ATOM   3141 C  CA  . GLU   B 1 139 ? -5.665  42.876  -11.112 1.00 28.31 ? 139 GLU   A CA  1 
ATOM   3142 C  C   . GLU   B 1 139 ? -4.481  42.894  -12.082 1.00 28.69 ? 139 GLU   A C   1 
ATOM   3143 O  O   . GLU   B 1 139 ? -4.293  41.941  -12.843 1.00 26.73 ? 139 GLU   A O   1 
ATOM   3144 C  CB  . GLU   B 1 139 ? -5.332  41.925  -9.959  1.00 34.21 ? 139 GLU   A CB  1 
ATOM   3145 C  CG  . GLU   B 1 139 ? -6.476  41.753  -8.975  1.00 38.95 ? 139 GLU   A CG  1 
ATOM   3146 C  CD  . GLU   B 1 139 ? -6.746  42.886  -7.994  1.00 42.27 ? 139 GLU   A CD  1 
ATOM   3147 O  OE1 . GLU   B 1 139 ? -6.269  44.030  -8.215  1.00 43.58 ? 139 GLU   A OE1 1 
ATOM   3148 O  OE2 . GLU   B 1 139 ? -7.457  42.620  -6.998  1.00 57.20 ? 139 GLU   A OE2 1 
ATOM   3149 N  N   . PRO   B 1 140 ? -3.593  43.922  -12.012 1.00 26.64 ? 140 PRO   A N   1 
ATOM   3150 C  CA  . PRO   B 1 140 ? -2.447  44.031  -12.914 1.00 23.71 ? 140 PRO   A CA  1 
ATOM   3151 C  C   . PRO   B 1 140 ? -1.561  42.788  -12.958 1.00 24.30 ? 140 PRO   A C   1 
ATOM   3152 O  O   . PRO   B 1 140 ? -1.055  42.422  -14.013 1.00 24.62 ? 140 PRO   A O   1 
ATOM   3153 C  CB  . PRO   B 1 140 ? -1.682  45.284  -12.438 1.00 25.69 ? 140 PRO   A CB  1 
ATOM   3154 C  CG  . PRO   B 1 140 ? -2.313  45.681  -11.115 1.00 28.52 ? 140 PRO   A CG  1 
ATOM   3155 C  CD  . PRO   B 1 140 ? -3.705  45.081  -11.109 1.00 27.73 ? 140 PRO   A CD  1 
ATOM   3156 N  N   . ASP   B 1 141 ? -1.419  42.108  -11.815 1.00 21.24 ? 141 ASP   A N   1 
ATOM   3157 C  CA  . ASP   B 1 141 ? -0.583  40.923  -11.774 1.00 21.67 ? 141 ASP   A CA  1 
ATOM   3158 C  C   . ASP   B 1 141 ? -1.461  39.676  -11.863 1.00 19.37 ? 141 ASP   A C   1 
ATOM   3159 O  O   . ASP   B 1 141 ? -1.017  38.601  -11.497 1.00 22.97 ? 141 ASP   A O   1 
ATOM   3160 C  CB  . ASP   B 1 141 ? 0.313   40.955  -10.538 1.00 22.77 ? 141 ASP   A CB  1 
ATOM   3161 C  CG  . ASP   B 1 141 ? -0.470  41.000  -9.232  1.00 27.44 ? 141 ASP   A CG  1 
ATOM   3162 O  OD1 . ASP   B 1 141 ? -1.699  41.292  -9.262  1.00 28.72 ? 141 ASP   A OD1 1 
ATOM   3163 O  OD2 . ASP   B 1 141 ? 0.139   40.696  -8.200  1.00 29.13 ? 141 ASP   A OD2 1 
ATOM   3164 N  N   . GLY   B 1 142 ? -2.677  39.811  -12.395 1.00 18.55 ? 142 GLY   A N   1 
ATOM   3165 C  CA  . GLY   B 1 142 ? -3.648  38.718  -12.319 1.00 17.86 ? 142 GLY   A CA  1 
ATOM   3166 C  C   . GLY   B 1 142 ? -3.374  37.572  -13.306 1.00 17.74 ? 142 GLY   A C   1 
ATOM   3167 O  O   . GLY   B 1 142 ? -3.542  36.393  -12.958 1.00 15.03 ? 142 GLY   A O   1 
ATOM   3168 N  N   . LEU   B 1 143 ? -3.013  37.922  -14.549 1.00 17.13 ? 143 LEU   A N   1 
ATOM   3169 C  CA  . LEU   B 1 143 ? -3.050  36.907  -15.609 1.00 15.76 ? 143 LEU   A CA  1 
ATOM   3170 C  C   . LEU   B 1 143 ? -1.720  36.888  -16.357 1.00 15.84 ? 143 LEU   A C   1 
ATOM   3171 O  O   . LEU   B 1 143 ? -1.005  37.888  -16.405 1.00 14.51 ? 143 LEU   A O   1 
ATOM   3172 C  CB  . LEU   B 1 143 ? -4.194  37.236  -16.575 1.00 15.94 ? 143 LEU   A CB  1 
ATOM   3173 C  CG  . LEU   B 1 143 ? -5.612  37.409  -16.018 1.00 14.50 ? 143 LEU   A CG  1 
ATOM   3174 C  CD1 . LEU   B 1 143 ? -6.535  37.700  -17.184 1.00 15.57 ? 143 LEU   A CD1 1 
ATOM   3175 C  CD2 . LEU   B 1 143 ? -6.118  36.120  -15.365 1.00 16.45 ? 143 LEU   A CD2 1 
ATOM   3176 N  N   . ALA   B 1 144 ? -1.400  35.723  -16.925 1.00 14.48 ? 144 ALA   A N   1 
ATOM   3177 C  CA  . ALA   B 1 144 ? -0.238  35.518  -17.773 1.00 15.24 ? 144 ALA   A CA  1 
ATOM   3178 C  C   . ALA   B 1 144 ? -0.703  34.739  -18.998 1.00 15.24 ? 144 ALA   A C   1 
ATOM   3179 O  O   . ALA   B 1 144 ? -1.431  33.725  -18.885 1.00 14.35 ? 144 ALA   A O   1 
ATOM   3180 C  CB  . ALA   B 1 144 ? 0.858   34.798  -17.019 1.00 14.59 ? 144 ALA   A CB  1 
ATOM   3181 N  N   . VAL   B 1 145 ? -0.372  35.281  -20.171 1.00 15.52 ? 145 VAL   A N   1 
ATOM   3182 C  CA  . VAL   B 1 145 ? -0.775  34.639  -21.412 1.00 14.29 ? 145 VAL   A CA  1 
ATOM   3183 C  C   . VAL   B 1 145 ? 0.480   34.356  -22.226 1.00 16.11 ? 145 VAL   A C   1 
ATOM   3184 O  O   . VAL   B 1 145 ? 1.325   35.241  -22.477 1.00 13.33 ? 145 VAL   A O   1 
ATOM   3185 C  CB  . VAL   B 1 145 ? -1.857  35.404  -22.194 1.00 14.04 ? 145 VAL   A CB  1 
ATOM   3186 C  CG1 . VAL   B 1 145 ? -2.269  34.644  -23.465 1.00 13.59 ? 145 VAL   A CG1 1 
ATOM   3187 C  CG2 . VAL   B 1 145 ? -3.094  35.678  -21.319 1.00 13.93 ? 145 VAL   A CG2 1 
ATOM   3188 N  N   . LEU   B 1 146 ? 0.603   33.074  -22.580 1.00 14.98 ? 146 LEU   A N   1 
ATOM   3189 C  CA  . LEU   B 1 146 ? 1.677   32.628  -23.440 1.00 17.78 ? 146 LEU   A CA  1 
ATOM   3190 C  C   . LEU   B 1 146 ? 1.124   32.655  -24.867 1.00 15.41 ? 146 LEU   A C   1 
ATOM   3191 O  O   . LEU   B 1 146 ? 0.050   32.101  -25.120 1.00 15.68 ? 146 LEU   A O   1 
ATOM   3192 C  CB  . LEU   B 1 146 ? 1.972   31.189  -23.025 1.00 20.68 ? 146 LEU   A CB  1 
ATOM   3193 C  CG  . LEU   B 1 146 ? 3.413   30.752  -22.796 1.00 28.81 ? 146 LEU   A CG  1 
ATOM   3194 C  CD1 . LEU   B 1 146 ? 3.566   29.290  -23.207 1.00 33.67 ? 146 LEU   A CD1 1 
ATOM   3195 C  CD2 . LEU   B 1 146 ? 4.409   31.609  -23.532 1.00 30.91 ? 146 LEU   A CD2 1 
ATOM   3196 N  N   . GLY   B 1 147 ? 1.864   33.278  -25.794 1.00 16.02 ? 147 GLY   A N   1 
ATOM   3197 C  CA  . GLY   B 1 147 ? 1.509   33.331  -27.209 1.00 16.38 ? 147 GLY   A CA  1 
ATOM   3198 C  C   . GLY   B 1 147 ? 2.514   32.535  -28.059 1.00 18.00 ? 147 GLY   A C   1 
ATOM   3199 O  O   . GLY   B 1 147 ? 3.724   32.644  -27.877 1.00 16.95 ? 147 GLY   A O   1 
ATOM   3200 N  N   . VAL   B 1 148 ? 1.980   31.726  -28.980 1.00 16.01 ? 148 VAL   A N   1 
ATOM   3201 C  CA  . VAL   B 1 148 ? 2.750   30.940  -29.922 1.00 16.30 ? 148 VAL   A CA  1 
ATOM   3202 C  C   . VAL   B 1 148 ? 2.241   31.273  -31.322 1.00 16.29 ? 148 VAL   A C   1 
ATOM   3203 O  O   . VAL   B 1 148 ? 1.047   31.147  -31.600 1.00 16.31 ? 148 VAL   A O   1 
ATOM   3204 C  CB  . VAL   B 1 148 ? 2.564   29.434  -29.619 1.00 17.99 ? 148 VAL   A CB  1 
ATOM   3205 C  CG1 . VAL   B 1 148 ? 3.400   28.585  -30.567 1.00 18.99 ? 148 VAL   A CG1 1 
ATOM   3206 C  CG2 . VAL   B 1 148 ? 2.910   29.099  -28.172 1.00 19.97 ? 148 VAL   A CG2 1 
ATOM   3207 N  N   . PHE   B 1 149 ? 3.144   31.662  -32.219 1.00 16.14 ? 149 PHE   A N   1 
ATOM   3208 C  CA  . PHE   B 1 149 ? 2.754   31.944  -33.594 1.00 15.49 ? 149 PHE   A CA  1 
ATOM   3209 C  C   . PHE   B 1 149 ? 2.694   30.655  -34.404 1.00 15.23 ? 149 PHE   A C   1 
ATOM   3210 O  O   . PHE   B 1 149 ? 3.535   29.775  -34.224 1.00 16.65 ? 149 PHE   A O   1 
ATOM   3211 C  CB  . PHE   B 1 149 ? 3.841   32.775  -34.269 1.00 13.98 ? 149 PHE   A CB  1 
ATOM   3212 C  CG  . PHE   B 1 149 ? 3.970   34.163  -33.698 1.00 15.81 ? 149 PHE   A CG  1 
ATOM   3213 C  CD1 . PHE   B 1 149 ? 2.885   35.026  -33.689 1.00 14.93 ? 149 PHE   A CD1 1 
ATOM   3214 C  CD2 . PHE   B 1 149 ? 5.178   34.585  -33.164 1.00 15.63 ? 149 PHE   A CD2 1 
ATOM   3215 C  CE1 . PHE   B 1 149 ? 3.037   36.311  -33.186 1.00 16.70 ? 149 PHE   A CE1 1 
ATOM   3216 C  CE2 . PHE   B 1 149 ? 5.316   35.861  -32.618 1.00 17.53 ? 149 PHE   A CE2 1 
ATOM   3217 C  CZ  . PHE   B 1 149 ? 4.230   36.706  -32.630 1.00 15.36 ? 149 PHE   A CZ  1 
ATOM   3218 N  N   . LEU   B 1 150 ? 1.769   30.600  -35.356 1.00 14.85 ? 150 LEU   A N   1 
ATOM   3219 C  CA  . LEU   B 1 150 ? 1.722   29.487  -36.300 1.00 17.22 ? 150 LEU   A CA  1 
ATOM   3220 C  C   . LEU   B 1 150 ? 2.002   30.049  -37.694 1.00 17.48 ? 150 LEU   A C   1 
ATOM   3221 O  O   . LEU   B 1 150 ? 1.371   31.031  -38.106 1.00 18.45 ? 150 LEU   A O   1 
ATOM   3222 C  CB  . LEU   B 1 150 ? 0.353   28.797  -36.248 1.00 16.71 ? 150 LEU   A CB  1 
ATOM   3223 C  CG  . LEU   B 1 150 ? -0.008  28.062  -34.957 1.00 18.12 ? 150 LEU   A CG  1 
ATOM   3224 C  CD1 . LEU   B 1 150 ? -0.407  29.039  -33.864 1.00 19.17 ? 150 LEU   A CD1 1 
ATOM   3225 C  CD2 . LEU   B 1 150 ? -1.154  27.087  -35.209 1.00 21.01 ? 150 LEU   A CD2 1 
ATOM   3226 N  N   . GLN   B 1 151 ? 2.960   29.437  -38.396 1.00 17.58 ? 151 GLN   A N   1 
ATOM   3227 C  CA  . GLN   B 1 151 ? 3.270   29.867  -39.753 1.00 20.06 ? 151 GLN   A CA  1 
ATOM   3228 C  C   . GLN   B 1 151 ? 2.798   28.758  -40.692 1.00 21.01 ? 151 GLN   A C   1 
ATOM   3229 O  O   . GLN   B 1 151 ? 2.751   27.588  -40.286 1.00 20.53 ? 151 GLN   A O   1 
ATOM   3230 C  CB  . GLN   B 1 151 ? 4.777   30.122  -39.871 1.00 19.78 ? 151 GLN   A CB  1 
ATOM   3231 C  CG  . GLN   B 1 151 ? 5.589   28.861  -39.564 1.00 22.25 ? 151 GLN   A CG  1 
ATOM   3232 C  CD  . GLN   B 1 151 ? 7.096   28.957  -39.708 1.00 27.88 ? 151 GLN   A CD  1 
ATOM   3233 O  OE1 . GLN   B 1 151 ? 7.656   30.041  -39.838 1.00 25.52 ? 151 GLN   A OE1 1 
ATOM   3234 N  NE2 . GLN   B 1 151 ? 7.763   27.804  -39.666 1.00 28.38 ? 151 GLN   A NE2 1 
ATOM   3235 N  N   . ILE   B 1 152 ? 2.435   29.128  -41.932 1.00 20.84 ? 152 ILE   A N   1 
ATOM   3236 C  CA  . ILE   B 1 152 ? 2.032   28.143  -42.929 1.00 21.80 ? 152 ILE   A CA  1 
ATOM   3237 C  C   . ILE   B 1 152 ? 3.228   27.250  -43.227 1.00 22.08 ? 152 ILE   A C   1 
ATOM   3238 O  O   . ILE   B 1 152 ? 4.332   27.744  -43.425 1.00 21.81 ? 152 ILE   A O   1 
ATOM   3239 C  CB  . ILE   B 1 152 ? 1.541   28.803  -44.236 1.00 22.48 ? 152 ILE   A CB  1 
ATOM   3240 C  CG1 . ILE   B 1 152 ? 0.287   29.661  -44.037 1.00 22.29 ? 152 ILE   A CG1 1 
ATOM   3241 C  CG2 . ILE   B 1 152 ? 1.344   27.736  -45.304 1.00 22.48 ? 152 ILE   A CG2 1 
ATOM   3242 C  CD1 . ILE   B 1 152 ? -0.904  28.945  -43.430 1.00 21.85 ? 152 ILE   A CD1 1 
ATOM   3243 N  N   . GLY   B 1 153 ? 3.002   25.936  -43.244 1.00 20.91 ? 153 GLY   A N   1 
ATOM   3244 C  CA  . GLY   B 1 153 ? 4.091   25.016  -43.520 1.00 21.25 ? 153 GLY   A CA  1 
ATOM   3245 C  C   . GLY   B 1 153 ? 3.489   23.638  -43.721 1.00 22.88 ? 153 GLY   A C   1 
ATOM   3246 O  O   . GLY   B 1 153 ? 2.280   23.496  -43.954 1.00 23.51 ? 153 GLY   A O   1 
ATOM   3247 N  N   . GLU   B 1 154 ? 4.313   22.611  -43.591 1.00 24.22 ? 154 GLU   A N   1 
ATOM   3248 C  CA  . GLU   B 1 154 ? 3.744   21.280  -43.723 1.00 26.50 ? 154 GLU   A CA  1 
ATOM   3249 C  C   . GLU   B 1 154 ? 2.793   21.040  -42.546 1.00 25.21 ? 154 GLU   A C   1 
ATOM   3250 O  O   . GLU   B 1 154 ? 2.941   21.639  -41.473 1.00 24.94 ? 154 GLU   A O   1 
ATOM   3251 C  CB  . GLU   B 1 154 ? 4.878   20.276  -43.939 1.00 30.96 ? 154 GLU   A CB  1 
ATOM   3252 C  CG  . GLU   B 1 154 ? 5.494   20.397  -45.341 1.00 33.90 ? 154 GLU   A CG  1 
ATOM   3253 C  CD  . GLU   B 1 154 ? 6.964   20.014  -45.467 1.00 39.47 ? 154 GLU   A CD  1 
ATOM   3254 O  OE1 . GLU   B 1 154 ? 7.574   19.676  -44.415 1.00 40.43 ? 154 GLU   A OE1 1 
ATOM   3255 O  OE2 . GLU   B 1 154 ? 7.518   20.073  -46.613 1.00 38.26 ? 154 GLU   A OE2 1 
ATOM   3256 N  N   . PRO   B 1 155 ? 1.755   20.184  -42.686 1.00 26.25 ? 155 PRO   A N   1 
ATOM   3257 C  CA  . PRO   B 1 155 ? 0.804   19.970  -41.592 1.00 25.30 ? 155 PRO   A CA  1 
ATOM   3258 C  C   . PRO   B 1 155 ? 1.398   19.519  -40.257 1.00 24.06 ? 155 PRO   A C   1 
ATOM   3259 O  O   . PRO   B 1 155 ? 2.359   18.748  -40.205 1.00 24.05 ? 155 PRO   A O   1 
ATOM   3260 C  CB  . PRO   B 1 155 ? -0.190  18.943  -42.160 1.00 25.97 ? 155 PRO   A CB  1 
ATOM   3261 C  CG  . PRO   B 1 155 ? 0.595   18.261  -43.274 1.00 24.81 ? 155 PRO   A CG  1 
ATOM   3262 C  CD  . PRO   B 1 155 ? 1.417   19.388  -43.886 1.00 24.80 ? 155 PRO   A CD  1 
ATOM   3263 N  N   . ASN   B 1 156 ? 0.793   20.012  -39.172 1.00 21.09 ? 156 ASN   A N   1 
ATOM   3264 C  CA  . ASN   B 1 156 ? 1.275   19.787  -37.809 1.00 20.34 ? 156 ASN   A CA  1 
ATOM   3265 C  C   . ASN   B 1 156 ? 0.468   18.654  -37.185 1.00 19.03 ? 156 ASN   A C   1 
ATOM   3266 O  O   . ASN   B 1 156 ? -0.712  18.806  -36.860 1.00 16.47 ? 156 ASN   A O   1 
ATOM   3267 C  CB  . ASN   B 1 156 ? 1.093   21.037  -36.950 1.00 19.85 ? 156 ASN   A CB  1 
ATOM   3268 C  CG  . ASN   B 1 156 ? 1.884   20.972  -35.662 1.00 22.00 ? 156 ASN   A CG  1 
ATOM   3269 O  OD1 . ASN   B 1 156 ? 2.087   19.888  -35.101 1.00 19.91 ? 156 ASN   A OD1 1 
ATOM   3270 N  ND2 . ASN   B 1 156 ? 2.358   22.126  -35.207 1.00 19.70 ? 156 ASN   A ND2 1 
ATOM   3271 N  N   . SER   B 1 157 ? 1.097   17.495  -36.998 1.00 19.80 ? 157 SER   A N   1 
ATOM   3272 C  CA  . SER   B 1 157 ? 0.318   16.375  -36.502 1.00 23.04 ? 157 SER   A CA  1 
ATOM   3273 C  C   . SER   B 1 157 ? -0.167  16.619  -35.071 1.00 24.88 ? 157 SER   A C   1 
ATOM   3274 O  O   . SER   B 1 157 ? -1.071  15.930  -34.587 1.00 27.30 ? 157 SER   A O   1 
ATOM   3275 C  CB  . SER   B 1 157 ? 1.101   15.077  -36.652 1.00 28.35 ? 157 SER   A CB  1 
ATOM   3276 O  OG  . SER   B 1 157 ? 2.292   15.154  -35.905 1.00 34.40 ? 157 SER   A OG  1 
ATOM   3277 N  N   . GLN   B 1 158 ? 0.398   17.630  -34.398 1.00 24.19 ? 158 GLN   A N   1 
ATOM   3278 C  CA  . GLN   B 1 158 ? -0.009  17.890  -33.022 1.00 26.43 ? 158 GLN   A CA  1 
ATOM   3279 C  C   . GLN   B 1 158 ? -1.308  18.689  -32.931 1.00 26.25 ? 158 GLN   A C   1 
ATOM   3280 O  O   . GLN   B 1 158 ? -1.805  18.897  -31.823 1.00 26.86 ? 158 GLN   A O   1 
ATOM   3281 C  CB  . GLN   B 1 158 ? 1.111   18.540  -32.210 1.00 25.27 ? 158 GLN   A CB  1 
ATOM   3282 C  CG  . GLN   B 1 158 ? 2.351   17.668  -32.062 1.00 31.98 ? 158 GLN   A CG  1 
ATOM   3283 C  CD  . GLN   B 1 158 ? 2.083   16.286  -31.506 1.00 32.44 ? 158 GLN   A CD  1 
ATOM   3284 O  OE1 . GLN   B 1 158 ? 2.441   15.281  -32.113 1.00 40.70 ? 158 GLN   A OE1 1 
ATOM   3285 N  NE2 . GLN   B 1 158 ? 1.442   16.210  -30.350 1.00 32.78 ? 158 GLN   A NE2 1 
ATOM   3286 N  N   . LEU   B 1 159 ? -1.869  19.108  -34.074 1.00 22.09 ? 159 LEU   A N   1 
ATOM   3287 C  CA  . LEU   B 1 159 ? -3.128  19.839  -34.068 1.00 22.85 ? 159 LEU   A CA  1 
ATOM   3288 C  C   . LEU   B 1 159 ? -4.283  18.886  -34.382 1.00 26.19 ? 159 LEU   A C   1 
ATOM   3289 O  O   . LEU   B 1 159 ? -5.443  19.288  -34.361 1.00 25.73 ? 159 LEU   A O   1 
ATOM   3290 C  CB  . LEU   B 1 159 ? -3.062  20.957  -35.112 1.00 23.10 ? 159 LEU   A CB  1 
ATOM   3291 C  CG  . LEU   B 1 159 ? -2.090  22.119  -34.872 1.00 24.61 ? 159 LEU   A CG  1 
ATOM   3292 C  CD1 . LEU   B 1 159 ? -1.961  23.001  -36.136 1.00 22.64 ? 159 LEU   A CD1 1 
ATOM   3293 C  CD2 . LEU   B 1 159 ? -2.542  22.984  -33.704 1.00 26.50 ? 159 LEU   A CD2 1 
ATOM   3294 N  N   . GLN   B 1 160 ? -3.974  17.611  -34.647 1.00 26.22 ? 160 GLN   A N   1 
ATOM   3295 C  CA  . GLN   B 1 160 ? -5.029  16.666  -35.013 1.00 27.75 ? 160 GLN   A CA  1 
ATOM   3296 C  C   . GLN   B 1 160 ? -6.077  16.509  -33.902 1.00 26.00 ? 160 GLN   A C   1 
ATOM   3297 O  O   . GLN   B 1 160 ? -7.269  16.390  -34.214 1.00 23.44 ? 160 GLN   A O   1 
ATOM   3298 C  CB  . GLN   B 1 160 ? -4.480  15.297  -35.458 1.00 27.24 ? 160 GLN   A CB  1 
ATOM   3299 C  CG  . GLN   B 1 160 ? -5.577  14.365  -36.003 1.00 30.16 ? 160 GLN   A CG  1 
ATOM   3300 C  CD  . GLN   B 1 160 ? -5.318  12.877  -35.905 1.00 34.80 ? 160 GLN   A CD  1 
ATOM   3301 O  OE1 . GLN   B 1 160 ? -6.243  12.066  -35.867 1.00 44.06 ? 160 GLN   A OE1 1 
ATOM   3302 N  NE2 . GLN   B 1 160 ? -4.058  12.488  -35.885 1.00 28.53 ? 160 GLN   A NE2 1 
ATOM   3303 N  N   . LYS   B 1 161 ? -5.639  16.452  -32.625 1.00 24.54 ? 161 LYS   A N   1 
ATOM   3304 C  CA  . LYS   B 1 161 ? -6.588  16.252  -31.537 1.00 25.20 ? 161 LYS   A CA  1 
ATOM   3305 C  C   . LYS   B 1 161 ? -7.654  17.352  -31.540 1.00 24.08 ? 161 LYS   A C   1 
ATOM   3306 O  O   . LYS   B 1 161 ? -8.846  17.079  -31.357 1.00 23.90 ? 161 LYS   A O   1 
ATOM   3307 C  CB  . LYS   B 1 161 ? -5.893  16.079  -30.181 1.00 29.56 ? 161 LYS   A CB  1 
ATOM   3308 C  CG  . LYS   B 1 161 ? -6.727  15.361  -29.121 1.00 29.98 ? 161 LYS   A CG  1 
ATOM   3309 C  CD  . LYS   B 1 161 ? -6.119  15.355  -27.737 1.00 30.80 ? 161 LYS   A CD  1 
ATOM   3310 C  CE  . LYS   B 1 161 ? -7.115  15.051  -26.637 1.00 28.83 ? 161 LYS   A CE  1 
ATOM   3311 N  NZ  . LYS   B 1 161 ? -7.658  13.676  -26.735 1.00 30.70 ? 161 LYS   A NZ  1 
ATOM   3312 N  N   . ILE   B 1 162 ? -7.233  18.584  -31.833 1.00 20.45 ? 162 ILE   A N   1 
ATOM   3313 C  CA  . ILE   B 1 162 ? -8.160  19.701  -31.928 1.00 20.64 ? 162 ILE   A CA  1 
ATOM   3314 C  C   . ILE   B 1 162 ? -9.000  19.638  -33.211 1.00 21.93 ? 162 ILE   A C   1 
ATOM   3315 O  O   . ILE   B 1 162 ? -10.221 19.837  -33.142 1.00 22.64 ? 162 ILE   A O   1 
ATOM   3316 C  CB  . ILE   B 1 162 ? -7.418  21.047  -31.811 1.00 19.38 ? 162 ILE   A CB  1 
ATOM   3317 C  CG1 . ILE   B 1 162 ? -6.754  21.209  -30.437 1.00 21.89 ? 162 ILE   A CG1 1 
ATOM   3318 C  CG2 . ILE   B 1 162 ? -8.413  22.178  -32.056 1.00 19.20 ? 162 ILE   A CG2 1 
ATOM   3319 C  CD1 . ILE   B 1 162 ? -5.729  22.355  -30.333 1.00 21.85 ? 162 ILE   A CD1 1 
ATOM   3320 N  N   . THR   B 1 163 ? -8.361  19.428  -34.385 1.00 21.72 ? 163 THR   A N   1 
ATOM   3321 C  CA  . THR   B 1 163 ? -9.073  19.554  -35.662 1.00 21.87 ? 163 THR   A CA  1 
ATOM   3322 C  C   . THR   B 1 163 ? -10.158 18.476  -35.775 1.00 22.98 ? 163 THR   A C   1 
ATOM   3323 O  O   . THR   B 1 163 ? -11.203 18.712  -36.382 1.00 23.44 ? 163 THR   A O   1 
ATOM   3324 C  CB  . THR   B 1 163 ? -8.175  19.598  -36.913 1.00 20.73 ? 163 THR   A CB  1 
ATOM   3325 O  OG1 . THR   B 1 163 ? -7.455  18.372  -37.100 1.00 20.72 ? 163 THR   A OG1 1 
ATOM   3326 C  CG2 . THR   B 1 163 ? -7.193  20.763  -36.937 1.00 21.70 ? 163 THR   A CG2 1 
ATOM   3327 N  N   . ASP   B 1 164 ? -9.897  17.318  -35.161 1.00 24.77 ? 164 ASP   A N   1 
ATOM   3328 C  CA  . ASP   B 1 164 ? -10.821 16.193  -35.152 1.00 28.60 ? 164 ASP   A CA  1 
ATOM   3329 C  C   . ASP   B 1 164 ? -12.115 16.509  -34.398 1.00 29.30 ? 164 ASP   A C   1 
ATOM   3330 O  O   . ASP   B 1 164 ? -13.113 15.812  -34.584 1.00 29.38 ? 164 ASP   A O   1 
ATOM   3331 C  CB  . ASP   B 1 164 ? -10.148 14.957  -34.552 1.00 33.88 ? 164 ASP   A CB  1 
ATOM   3332 C  CG  . ASP   B 1 164 ? -9.405  14.091  -35.562 1.00 42.97 ? 164 ASP   A CG  1 
ATOM   3333 O  OD1 . ASP   B 1 164 ? -9.650  14.264  -36.774 1.00 50.76 ? 164 ASP   A OD1 1 
ATOM   3334 O  OD2 . ASP   B 1 164 ? -8.591  13.227  -35.123 1.00 41.65 ? 164 ASP   A OD2 1 
ATOM   3335 N  N   . THR   B 1 165 ? -12.124 17.543  -33.542 1.00 26.09 ? 165 THR   A N   1 
ATOM   3336 C  CA  . THR   B 1 165 ? -13.315 17.840  -32.748 1.00 27.50 ? 165 THR   A CA  1 
ATOM   3337 C  C   . THR   B 1 165 ? -14.165 18.953  -33.386 1.00 26.37 ? 165 THR   A C   1 
ATOM   3338 O  O   . THR   B 1 165 ? -15.261 19.241  -32.910 1.00 22.80 ? 165 THR   A O   1 
ATOM   3339 C  CB  . THR   B 1 165 ? -12.977 18.338  -31.327 1.00 26.13 ? 165 THR   A CB  1 
ATOM   3340 O  OG1 . THR   B 1 165 ? -12.377 19.621  -31.508 1.00 27.68 ? 165 THR   A OG1 1 
ATOM   3341 C  CG2 . THR   B 1 165 ? -12.063 17.426  -30.532 1.00 26.26 ? 165 THR   A CG2 1 
ATOM   3342 N  N   . LEU   B 1 166 ? -13.661 19.618  -34.429 1.00 24.73 ? 166 LEU   A N   1 
ATOM   3343 C  CA  . LEU   B 1 166 ? -14.306 20.860  -34.865 1.00 26.63 ? 166 LEU   A CA  1 
ATOM   3344 C  C   . LEU   B 1 166 ? -15.696 20.588  -35.456 1.00 27.21 ? 166 LEU   A C   1 
ATOM   3345 O  O   . LEU   B 1 166 ? -16.573 21.449  -35.378 1.00 23.95 ? 166 LEU   A O   1 
ATOM   3346 C  CB  . LEU   B 1 166 ? -13.415 21.615  -35.865 1.00 26.38 ? 166 LEU   A CB  1 
ATOM   3347 C  CG  . LEU   B 1 166 ? -12.051 22.068  -35.329 1.00 29.40 ? 166 LEU   A CG  1 
ATOM   3348 C  CD1 . LEU   B 1 166 ? -11.210 22.711  -36.433 1.00 27.26 ? 166 LEU   A CD1 1 
ATOM   3349 C  CD2 . LEU   B 1 166 ? -12.191 23.016  -34.140 1.00 27.72 ? 166 LEU   A CD2 1 
ATOM   3350 N  N   . ASP   B 1 167 ? -15.894 19.398  -36.045 1.00 29.95 ? 167 ASP   A N   1 
ATOM   3351 C  CA  . ASP   B 1 167 ? -17.200 19.008  -36.582 1.00 35.86 ? 167 ASP   A CA  1 
ATOM   3352 C  C   . ASP   B 1 167 ? -18.237 18.950  -35.458 1.00 32.06 ? 167 ASP   A C   1 
ATOM   3353 O  O   . ASP   B 1 167 ? -19.338 19.466  -35.613 1.00 30.42 ? 167 ASP   A O   1 
ATOM   3354 C  CB  . ASP   B 1 167 ? -17.181 17.664  -37.329 1.00 40.42 ? 167 ASP   A CB  1 
ATOM   3355 C  CG  . ASP   B 1 167 ? -17.356 17.761  -38.836 1.00 50.62 ? 167 ASP   A CG  1 
ATOM   3356 O  OD1 . ASP   B 1 167 ? -16.469 18.355  -39.495 1.00 52.00 ? 167 ASP   A OD1 1 
ATOM   3357 O  OD2 . ASP   B 1 167 ? -18.372 17.227  -39.349 1.00 56.92 ? 167 ASP   A OD2 1 
ATOM   3358 N  N   . SER   B 1 168 ? -17.866 18.364  -34.309 1.00 29.87 ? 168 SER   A N   1 
ATOM   3359 C  CA  . SER   B 1 168 ? -18.792 18.257  -33.185 1.00 31.06 ? 168 SER   A CA  1 
ATOM   3360 C  C   . SER   B 1 168 ? -19.056 19.590  -32.462 1.00 28.68 ? 168 SER   A C   1 
ATOM   3361 O  O   . SER   B 1 168 ? -20.007 19.659  -31.677 1.00 27.38 ? 168 SER   A O   1 
ATOM   3362 C  CB  . SER   B 1 168 ? -18.326 17.223  -32.197 1.00 32.56 ? 168 SER   A CB  1 
ATOM   3363 O  OG  . SER   B 1 168 ? -17.250 17.766  -31.448 1.00 32.04 ? 168 SER   A OG  1 
ATOM   3364 N  N   . ILE   B 1 169 ? -18.237 20.639  -32.681 1.00 24.35 ? 169 ILE   A N   1 
ATOM   3365 C  CA  . ILE   B 1 169 ? -18.497 21.914  -32.002 1.00 25.39 ? 169 ILE   A CA  1 
ATOM   3366 C  C   . ILE   B 1 169 ? -18.771 23.047  -33.000 1.00 23.74 ? 169 ILE   A C   1 
ATOM   3367 O  O   . ILE   B 1 169 ? -18.384 24.200  -32.789 1.00 22.13 ? 169 ILE   A O   1 
ATOM   3368 C  CB  . ILE   B 1 169 ? -17.370 22.284  -31.011 1.00 23.05 ? 169 ILE   A CB  1 
ATOM   3369 C  CG1 . ILE   B 1 169 ? -16.005 22.400  -31.697 1.00 25.38 ? 169 ILE   A CG1 1 
ATOM   3370 C  CG2 . ILE   B 1 169 ? -17.347 21.306  -29.838 1.00 24.52 ? 169 ILE   A CG2 1 
ATOM   3371 C  CD1 . ILE   B 1 169 ? -14.982 23.205  -30.902 1.00 24.17 ? 169 ILE   A CD1 1 
ATOM   3372 N  N   . LYS   B 1 170 ? -19.420 22.723  -34.117 1.00 24.69 ? 170 LYS   A N   1 
ATOM   3373 C  CA  . LYS   B 1 170 ? -19.542 23.711  -35.189 1.00 27.14 ? 170 LYS   A CA  1 
ATOM   3374 C  C   . LYS   B 1 170 ? -20.296 24.950  -34.695 1.00 25.53 ? 170 LYS   A C   1 
ATOM   3375 O  O   . LYS   B 1 170 ? -19.917 26.083  -34.997 1.00 25.24 ? 170 LYS   A O   1 
ATOM   3376 C  CB  . LYS   B 1 170 ? -20.225 23.079  -36.412 1.00 33.50 ? 170 LYS   A CB  1 
ATOM   3377 C  CG  . LYS   B 1 170 ? -20.631 24.078  -37.492 1.00 36.23 ? 170 LYS   A CG  1 
ATOM   3378 C  CD  . LYS   B 1 170 ? -21.044 23.463  -38.804 1.00 36.85 ? 170 LYS   A CD  1 
ATOM   3379 C  CE  . LYS   B 1 170 ? -20.980 24.480  -39.933 1.00 41.88 ? 170 LYS   A CE  1 
ATOM   3380 N  NZ  . LYS   B 1 170 ? -19.618 24.598  -40.520 1.00 35.76 ? 170 LYS   A NZ  1 
ATOM   3381 N  N   . GLU   B 1 171 ? -21.357 24.723  -33.908 1.00 25.26 ? 171 GLU   A N   1 
ATOM   3382 C  CA  . GLU   B 1 171 ? -22.222 25.800  -33.453 1.00 27.37 ? 171 GLU   A CA  1 
ATOM   3383 C  C   . GLU   B 1 171 ? -21.758 26.317  -32.090 1.00 25.85 ? 171 GLU   A C   1 
ATOM   3384 O  O   . GLU   B 1 171 ? -21.318 25.550  -31.237 1.00 25.16 ? 171 GLU   A O   1 
ATOM   3385 C  CB  . GLU   B 1 171 ? -23.686 25.351  -33.404 1.00 33.93 ? 171 GLU   A CB  1 
ATOM   3386 C  CG  . GLU   B 1 171 ? -24.242 24.882  -34.748 1.00 37.80 ? 171 GLU   A CG  1 
ATOM   3387 C  CD  . GLU   B 1 171 ? -23.984 23.432  -35.134 1.00 48.46 ? 171 GLU   A CD  1 
ATOM   3388 O  OE1 . GLU   B 1 171 ? -24.312 23.063  -36.289 1.00 50.72 ? 171 GLU   A OE1 1 
ATOM   3389 O  OE2 . GLU   B 1 171 ? -23.459 22.661  -34.280 1.00 52.96 ? 171 GLU   A OE2 1 
ATOM   3390 N  N   . LYS   B 1 172 ? -21.902 27.633  -31.893 1.00 23.57 ? 172 LYS   A N   1 
ATOM   3391 C  CA  . LYS   B 1 172 ? -21.632 28.279  -30.617 1.00 25.42 ? 172 LYS   A CA  1 
ATOM   3392 C  C   . LYS   B 1 172 ? -22.367 27.569  -29.473 1.00 26.92 ? 172 LYS   A C   1 
ATOM   3393 O  O   . LYS   B 1 172 ? -23.563 27.303  -29.578 1.00 25.27 ? 172 LYS   A O   1 
ATOM   3394 C  CB  . LYS   B 1 172 ? -22.114 29.721  -30.713 1.00 25.80 ? 172 LYS   A CB  1 
ATOM   3395 C  CG  . LYS   B 1 172 ? -21.924 30.548  -29.458 1.00 27.78 ? 172 LYS   A CG  1 
ATOM   3396 C  CD  . LYS   B 1 172 ? -22.535 31.931  -29.538 1.00 27.29 ? 172 LYS   A CD  1 
ATOM   3397 C  CE  . LYS   B 1 172 ? -22.240 32.699  -28.258 1.00 30.97 ? 172 LYS   A CE  1 
ATOM   3398 N  NZ  . LYS   B 1 172 ? -22.486 34.154  -28.416 1.00 33.02 ? 172 LYS   A NZ  1 
ATOM   3399 N  N   . GLY   B 1 173 ? -21.636 27.261  -28.391 1.00 25.42 ? 173 GLY   A N   1 
ATOM   3400 C  CA  . GLY   B 1 173 ? -22.185 26.659  -27.182 1.00 25.58 ? 173 GLY   A CA  1 
ATOM   3401 C  C   . GLY   B 1 173 ? -22.027 25.136  -27.151 1.00 27.86 ? 173 GLY   A C   1 
ATOM   3402 O  O   . GLY   B 1 173 ? -22.226 24.521  -26.119 1.00 23.95 ? 173 GLY   A O   1 
ATOM   3403 N  N   . LYS   B 1 174 ? -21.680 24.517  -28.285 1.00 25.03 ? 174 LYS   A N   1 
ATOM   3404 C  CA  . LYS   B 1 174 ? -21.450 23.085  -28.313 1.00 23.17 ? 174 LYS   A CA  1 
ATOM   3405 C  C   . LYS   B 1 174 ? -20.124 22.771  -27.622 1.00 22.62 ? 174 LYS   A C   1 
ATOM   3406 O  O   . LYS   B 1 174 ? -19.198 23.591  -27.633 1.00 20.74 ? 174 LYS   A O   1 
ATOM   3407 C  CB  . LYS   B 1 174 ? -21.473 22.563  -29.747 1.00 26.01 ? 174 LYS   A CB  1 
ATOM   3408 C  CG  . LYS   B 1 174 ? -22.829 22.656  -30.447 1.00 31.24 ? 174 LYS   A CG  1 
ATOM   3409 C  CD  . LYS   B 1 174 ? -23.709 21.445  -30.206 1.00 37.57 ? 174 LYS   A CD  1 
ATOM   3410 C  CE  . LYS   B 1 174 ? -23.383 20.258  -31.094 1.00 43.41 ? 174 LYS   A CE  1 
ATOM   3411 N  NZ  . LYS   B 1 174 ? -24.000 20.394  -32.439 1.00 46.18 ? 174 LYS   A NZ  1 
ATOM   3412 N  N   . GLN   B 1 175 ? -20.048 21.582  -27.009 1.00 20.61 ? 175 GLN   A N   1 
ATOM   3413 C  CA  . GLN   B 1 175 ? -18.840 21.172  -26.306 1.00 19.72 ? 175 GLN   A CA  1 
ATOM   3414 C  C   . GLN   B 1 175 ? -18.641 19.671  -26.466 1.00 23.35 ? 175 GLN   A C   1 
ATOM   3415 O  O   . GLN   B 1 175 ? -19.620 18.946  -26.692 1.00 21.40 ? 175 GLN   A O   1 
ATOM   3416 C  CB  . GLN   B 1 175 ? -18.876 21.612  -24.836 1.00 20.48 ? 175 GLN   A CB  1 
ATOM   3417 C  CG  . GLN   B 1 175 ? -19.846 20.821  -23.972 1.00 23.24 ? 175 GLN   A CG  1 
ATOM   3418 C  CD  . GLN   B 1 175 ? -19.814 21.272  -22.537 1.00 25.15 ? 175 GLN   A CD  1 
ATOM   3419 O  OE1 . GLN   B 1 175 ? -19.526 20.506  -21.627 1.00 27.22 ? 175 GLN   A OE1 1 
ATOM   3420 N  NE2 . GLN   B 1 175 ? -20.074 22.541  -22.320 1.00 22.37 ? 175 GLN   A NE2 1 
ATOM   3421 N  N   . THR   B 1 176 ? -17.385 19.212  -26.356 1.00 22.91 ? 176 THR   A N   1 
ATOM   3422 C  CA  . THR   B 1 176 ? -17.144 17.779  -26.216 1.00 28.48 ? 176 THR   A CA  1 
ATOM   3423 C  C   . THR   B 1 176 ? -16.036 17.476  -25.216 1.00 26.68 ? 176 THR   A C   1 
ATOM   3424 O  O   . THR   B 1 176 ? -15.209 18.338  -24.886 1.00 22.35 ? 176 THR   A O   1 
ATOM   3425 C  CB  . THR   B 1 176 ? -16.645 17.038  -27.472 1.00 34.12 ? 176 THR   A CB  1 
ATOM   3426 O  OG1 . THR   B 1 176 ? -16.099 17.905  -28.468 1.00 38.19 ? 176 THR   A OG1 1 
ATOM   3427 C  CG2 . THR   B 1 176 ? -17.654 16.064  -28.035 1.00 36.99 ? 176 THR   A CG2 1 
ATOM   3428 N  N   . ARG   B 1 177 ? -16.018 16.206  -24.776 1.00 24.11 ? 177 ARG   A N   1 
ATOM   3429 C  CA  . ARG   B 1 177 ? -14.972 15.731  -23.894 1.00 25.60 ? 177 ARG   A CA  1 
ATOM   3430 C  C   . ARG   B 1 177 ? -13.637 16.017  -24.573 1.00 23.79 ? 177 ARG   A C   1 
ATOM   3431 O  O   . ARG   B 1 177 ? -13.501 15.769  -25.760 1.00 22.94 ? 177 ARG   A O   1 
ATOM   3432 C  CB  . ARG   B 1 177 ? -15.083 14.206  -23.728 1.00 26.63 ? 177 ARG   A CB  1 
ATOM   3433 C  CG  . ARG   B 1 177 ? -14.069 13.642  -22.744 1.00 30.12 ? 177 ARG   A CG  1 
ATOM   3434 C  CD  . ARG   B 1 177 ? -14.591 12.384  -22.073 1.00 33.22 ? 177 ARG   A CD  1 
ATOM   3435 N  NE  . ARG   B 1 177 ? -13.573 11.540  -21.470 1.00 37.62 ? 177 ARG   A NE  1 
ATOM   3436 C  CZ  . ARG   B 1 177 ? -12.990 11.730  -20.284 1.00 42.14 ? 177 ARG   A CZ  1 
ATOM   3437 N  NH1 . ARG   B 1 177 ? -13.296 12.778  -19.519 1.00 37.81 ? 177 ARG   A NH1 1 
ATOM   3438 N  NH2 . ARG   B 1 177 ? -12.088 10.850  -19.877 1.00 39.44 ? 177 ARG   A NH2 1 
ATOM   3439 N  N   . PHE   B 1 178 ? -12.648 16.502  -23.819 1.00 22.00 ? 178 PHE   A N   1 
ATOM   3440 C  CA  . PHE   B 1 178 ? -11.334 16.710  -24.401 1.00 20.69 ? 178 PHE   A CA  1 
ATOM   3441 C  C   . PHE   B 1 178 ? -10.265 16.454  -23.339 1.00 20.41 ? 178 PHE   A C   1 
ATOM   3442 O  O   . PHE   B 1 178 ? -9.981  17.342  -22.560 1.00 18.86 ? 178 PHE   A O   1 
ATOM   3443 C  CB  . PHE   B 1 178 ? -11.266 18.142  -24.965 1.00 20.22 ? 178 PHE   A CB  1 
ATOM   3444 C  CG  . PHE   B 1 178 ? -10.108 18.413  -25.902 1.00 18.20 ? 178 PHE   A CG  1 
ATOM   3445 C  CD1 . PHE   B 1 178 ? -10.179 18.041  -27.232 1.00 17.97 ? 178 PHE   A CD1 1 
ATOM   3446 C  CD2 . PHE   B 1 178 ? -8.957  19.043  -25.452 1.00 18.92 ? 178 PHE   A CD2 1 
ATOM   3447 C  CE1 . PHE   B 1 178 ? -9.126  18.313  -28.097 1.00 18.15 ? 178 PHE   A CE1 1 
ATOM   3448 C  CE2 . PHE   B 1 178 ? -7.910  19.313  -26.318 1.00 17.19 ? 178 PHE   A CE2 1 
ATOM   3449 C  CZ  . PHE   B 1 178 ? -7.999  18.956  -27.642 1.00 17.15 ? 178 PHE   A CZ  1 
ATOM   3450 N  N   . THR   B 1 179 ? -9.645  15.262  -23.278 1.00 21.57 ? 179 THR   A N   1 
ATOM   3451 C  CA  . THR   B 1 179 ? -8.610  15.151  -22.252 1.00 24.04 ? 179 THR   A CA  1 
ATOM   3452 C  C   . THR   B 1 179 ? -7.406  14.386  -22.785 1.00 23.63 ? 179 THR   A C   1 
ATOM   3453 O  O   . THR   B 1 179 ? -7.422  13.952  -23.935 1.00 26.09 ? 179 THR   A O   1 
ATOM   3454 C  CB  . THR   B 1 179 ? -9.122  14.673  -20.877 1.00 31.19 ? 179 THR   A CB  1 
ATOM   3455 O  OG1 . THR   B 1 179 ? -8.026  14.734  -19.932 1.00 31.21 ? 179 THR   A OG1 1 
ATOM   3456 C  CG2 . THR   B 1 179 ? -9.748  13.291  -20.969 1.00 31.69 ? 179 THR   A CG2 1 
ATOM   3457 N  N   . ASN   B 1 180 ? -6.392  14.207  -21.932 0.50 19.49 ? 180 ASN   A N   1 
ATOM   3458 C  CA  . ASN   B 1 180 ? -5.112  13.679  -22.371 0.50 19.18 ? 180 ASN   A CA  1 
ATOM   3459 C  C   . ASN   B 1 180 ? -4.587  14.510  -23.540 0.50 19.11 ? 180 ASN   A C   1 
ATOM   3460 O  O   . ASN   B 1 180 ? -4.232  13.998  -24.598 0.50 16.69 ? 180 ASN   A O   1 
ATOM   3461 C  CB  . ASN   B 1 180 ? -5.176  12.186  -22.687 0.50 20.67 ? 180 ASN   A CB  1 
ATOM   3462 C  CG  . ASN   B 1 180 ? -4.000  11.480  -22.051 0.50 23.74 ? 180 ASN   A CG  1 
ATOM   3463 O  OD1 . ASN   B 1 180 ? -2.858  11.853  -22.283 0.50 22.65 ? 180 ASN   A OD1 1 
ATOM   3464 N  ND2 . ASN   B 1 180 ? -4.278  10.490  -21.215 0.50 27.58 ? 180 ASN   A ND2 1 
ATOM   3465 N  N   . PHE   B 1 181 ? -4.548  15.822  -23.325 1.00 20.97 ? 181 PHE   A N   1 
ATOM   3466 C  CA  . PHE   B 1 181 ? -4.089  16.763  -24.339 1.00 22.46 ? 181 PHE   A CA  1 
ATOM   3467 C  C   . PHE   B 1 181 ? -2.646  17.163  -24.029 1.00 22.28 ? 181 PHE   A C   1 
ATOM   3468 O  O   . PHE   B 1 181 ? -2.366  17.686  -22.951 1.00 21.94 ? 181 PHE   A O   1 
ATOM   3469 C  CB  . PHE   B 1 181 ? -5.015  17.985  -24.350 1.00 22.12 ? 181 PHE   A CB  1 
ATOM   3470 C  CG  . PHE   B 1 181 ? -4.626  19.143  -25.239 1.00 21.97 ? 181 PHE   A CG  1 
ATOM   3471 C  CD1 . PHE   B 1 181 ? -4.176  18.946  -26.536 1.00 23.85 ? 181 PHE   A CD1 1 
ATOM   3472 C  CD2 . PHE   B 1 181 ? -4.798  20.444  -24.794 1.00 22.02 ? 181 PHE   A CD2 1 
ATOM   3473 C  CE1 . PHE   B 1 181 ? -3.868  20.023  -27.354 1.00 22.58 ? 181 PHE   A CE1 1 
ATOM   3474 C  CE2 . PHE   B 1 181 ? -4.484  21.523  -25.610 1.00 21.65 ? 181 PHE   A CE2 1 
ATOM   3475 C  CZ  . PHE   B 1 181 ? -4.030  21.312  -26.895 1.00 23.32 ? 181 PHE   A CZ  1 
ATOM   3476 N  N   . ASP   B 1 182 ? -1.755  16.889  -24.997 1.00 22.29 ? 182 ASP   A N   1 
ATOM   3477 C  CA  . ASP   B 1 182 ? -0.319  17.105  -24.912 1.00 26.16 ? 182 ASP   A CA  1 
ATOM   3478 C  C   . ASP   B 1 182 ? -0.040  18.546  -25.329 1.00 23.33 ? 182 ASP   A C   1 
ATOM   3479 O  O   . ASP   B 1 182 ? 0.434   18.788  -26.431 1.00 25.18 ? 182 ASP   A O   1 
ATOM   3480 C  CB  . ASP   B 1 182 ? 0.448   16.172  -25.866 1.00 28.53 ? 182 ASP   A CB  1 
ATOM   3481 C  CG  . ASP   B 1 182 ? 1.976   16.307  -25.830 1.00 32.38 ? 182 ASP   A CG  1 
ATOM   3482 O  OD1 . ASP   B 1 182 ? 2.499   17.132  -25.037 1.00 34.79 ? 182 ASP   A OD1 1 
ATOM   3483 O  OD2 . ASP   B 1 182 ? 2.654   15.565  -26.588 1.00 35.01 ? 182 ASP   A OD2 1 
ATOM   3484 N  N   . LEU   B 1 183 ? -0.419  19.484  -24.464 1.00 23.22 ? 183 LEU   A N   1 
ATOM   3485 C  CA  . LEU   B 1 183 ? -0.282  20.900  -24.786 1.00 21.47 ? 183 LEU   A CA  1 
ATOM   3486 C  C   . LEU   B 1 183 ? 1.201   21.285  -24.939 1.00 21.58 ? 183 LEU   A C   1 
ATOM   3487 O  O   . LEU   B 1 183 ? 1.544   22.074  -25.810 1.00 20.11 ? 183 LEU   A O   1 
ATOM   3488 C  CB  . LEU   B 1 183 ? -1.021  21.728  -23.733 1.00 17.37 ? 183 LEU   A CB  1 
ATOM   3489 C  CG  . LEU   B 1 183 ? -0.906  23.247  -23.915 1.00 18.24 ? 183 LEU   A CG  1 
ATOM   3490 C  CD1 . LEU   B 1 183 ? -1.504  23.729  -25.243 1.00 18.06 ? 183 LEU   A CD1 1 
ATOM   3491 C  CD2 . LEU   B 1 183 ? -1.505  23.970  -22.725 1.00 20.73 ? 183 LEU   A CD2 1 
ATOM   3492 N  N   . LEU   B 1 184 ? 2.121   20.663  -24.190 1.00 21.48 ? 184 LEU   A N   1 
ATOM   3493 C  CA  . LEU   B 1 184 ? 3.523   21.025  -24.411 1.00 24.73 ? 184 LEU   A CA  1 
ATOM   3494 C  C   . LEU   B 1 184 ? 3.960   20.766  -25.857 1.00 24.25 ? 184 LEU   A C   1 
ATOM   3495 O  O   . LEU   B 1 184 ? 4.831   21.458  -26.354 1.00 21.49 ? 184 LEU   A O   1 
ATOM   3496 C  CB  . LEU   B 1 184 ? 4.458   20.300  -23.431 1.00 25.44 ? 184 LEU   A CB  1 
ATOM   3497 C  CG  . LEU   B 1 184 ? 4.417   20.805  -21.988 1.00 31.06 ? 184 LEU   A CG  1 
ATOM   3498 C  CD1 . LEU   B 1 184 ? 4.982   19.740  -21.026 1.00 31.31 ? 184 LEU   A CD1 1 
ATOM   3499 C  CD2 . LEU   B 1 184 ? 5.178   22.124  -21.865 1.00 26.65 ? 184 LEU   A CD2 1 
ATOM   3500 N  N   . SER   B 1 185 ? 3.376   19.772  -26.539 1.00 23.60 ? 185 SER   A N   1 
ATOM   3501 C  CA  . SER   B 1 185 ? 3.820   19.472  -27.895 1.00 25.73 ? 185 SER   A CA  1 
ATOM   3502 C  C   . SER   B 1 185 ? 3.475   20.559  -28.920 1.00 27.05 ? 185 SER   A C   1 
ATOM   3503 O  O   . SER   B 1 185 ? 3.931   20.477  -30.056 1.00 25.36 ? 185 SER   A O   1 
ATOM   3504 C  CB  . SER   B 1 185 ? 3.350   18.112  -28.356 1.00 32.09 ? 185 SER   A CB  1 
ATOM   3505 O  OG  . SER   B 1 185 ? 1.979   18.164  -28.725 1.00 35.02 ? 185 SER   A OG  1 
ATOM   3506 N  N   . LEU   B 1 186 ? 2.646   21.545  -28.544 1.00 23.60 ? 186 LEU   A N   1 
ATOM   3507 C  CA  . LEU   B 1 186 ? 2.345   22.689  -29.390 1.00 23.28 ? 186 LEU   A CA  1 
ATOM   3508 C  C   . LEU   B 1 186 ? 3.258   23.867  -29.069 1.00 25.23 ? 186 LEU   A C   1 
ATOM   3509 O  O   . LEU   B 1 186 ? 3.012   24.994  -29.518 1.00 28.90 ? 186 LEU   A O   1 
ATOM   3510 C  CB  . LEU   B 1 186 ? 0.884   23.102  -29.166 1.00 21.12 ? 186 LEU   A CB  1 
ATOM   3511 C  CG  . LEU   B 1 186 ? -0.147  22.149  -29.771 1.00 22.30 ? 186 LEU   A CG  1 
ATOM   3512 C  CD1 . LEU   B 1 186 ? -1.563  22.596  -29.430 1.00 23.14 ? 186 LEU   A CD1 1 
ATOM   3513 C  CD2 . LEU   B 1 186 ? 0.066   22.034  -31.286 1.00 22.46 ? 186 LEU   A CD2 1 
ATOM   3514 N  N   . LEU   B 1 187 ? 4.276   23.646  -28.237 1.00 22.01 ? 187 LEU   A N   1 
ATOM   3515 C  CA  . LEU   B 1 187 ? 5.242   24.717  -28.075 1.00 21.65 ? 187 LEU   A CA  1 
ATOM   3516 C  C   . LEU   B 1 187 ? 6.413   24.451  -29.008 1.00 19.50 ? 187 LEU   A C   1 
ATOM   3517 O  O   . LEU   B 1 187 ? 6.730   23.293  -29.286 1.00 16.92 ? 187 LEU   A O   1 
ATOM   3518 C  CB  . LEU   B 1 187 ? 5.737   24.792  -26.624 1.00 21.89 ? 187 LEU   A CB  1 
ATOM   3519 C  CG  . LEU   B 1 187 ? 4.681   25.141  -25.588 1.00 21.91 ? 187 LEU   A CG  1 
ATOM   3520 C  CD1 . LEU   B 1 187 ? 5.285   25.182  -24.184 1.00 23.16 ? 187 LEU   A CD1 1 
ATOM   3521 C  CD2 . LEU   B 1 187 ? 4.015   26.455  -25.914 1.00 23.39 ? 187 LEU   A CD2 1 
ATOM   3522 N  N   . PRO   B 1 188 ? 7.109   25.505  -29.489 1.00 19.88 ? 188 PRO   A N   1 
ATOM   3523 C  CA  . PRO   B 1 188 ? 8.279   25.327  -30.355 1.00 18.14 ? 188 PRO   A CA  1 
ATOM   3524 C  C   . PRO   B 1 188 ? 9.438   24.796  -29.511 1.00 19.31 ? 188 PRO   A C   1 
ATOM   3525 O  O   . PRO   B 1 188 ? 9.360   24.807  -28.284 1.00 17.26 ? 188 PRO   A O   1 
ATOM   3526 C  CB  . PRO   B 1 188 ? 8.598   26.761  -30.824 1.00 17.97 ? 188 PRO   A CB  1 
ATOM   3527 C  CG  . PRO   B 1 188 ? 8.113   27.592  -29.661 1.00 18.21 ? 188 PRO   A CG  1 
ATOM   3528 C  CD  . PRO   B 1 188 ? 6.809   26.932  -29.234 1.00 18.43 ? 188 PRO   A CD  1 
ATOM   3529 N  N   . PRO   B 1 189 ? 10.514  24.248  -30.122 1.00 18.69 ? 189 PRO   A N   1 
ATOM   3530 C  CA  . PRO   B 1 189 ? 11.677  23.787  -29.350 1.00 20.53 ? 189 PRO   A CA  1 
ATOM   3531 C  C   . PRO   B 1 189 ? 12.356  24.835  -28.473 1.00 19.25 ? 189 PRO   A C   1 
ATOM   3532 O  O   . PRO   B 1 189 ? 12.733  24.494  -27.360 1.00 19.87 ? 189 PRO   A O   1 
ATOM   3533 C  CB  . PRO   B 1 189 ? 12.667  23.314  -30.411 1.00 20.39 ? 189 PRO   A CB  1 
ATOM   3534 C  CG  . PRO   B 1 189 ? 11.743  22.835  -31.509 1.00 21.45 ? 189 PRO   A CG  1 
ATOM   3535 C  CD  . PRO   B 1 189 ? 10.593  23.838  -31.526 1.00 19.50 ? 189 PRO   A CD  1 
ATOM   3536 N  N   . SER   B 1 190 ? 12.470  26.085  -28.949 1.00 18.50 ? 190 SER   A N   1 
ATOM   3537 C  CA  . SER   B 1 190 ? 13.051  27.155  -28.141 1.00 18.11 ? 190 SER   A CA  1 
ATOM   3538 C  C   . SER   B 1 190 ? 11.925  27.959  -27.506 1.00 18.28 ? 190 SER   A C   1 
ATOM   3539 O  O   . SER   B 1 190 ? 10.925  28.259  -28.166 1.00 18.27 ? 190 SER   A O   1 
ATOM   3540 C  CB  . SER   B 1 190 ? 13.928  28.090  -28.937 1.00 20.34 ? 190 SER   A CB  1 
ATOM   3541 O  OG  . SER   B 1 190 ? 14.315  29.235  -28.142 1.00 19.39 ? 190 SER   A OG  1 
ATOM   3542 N  N   . TRP   B 1 191 ? 12.101  28.269  -26.221 1.00 16.37 ? 191 TRP   A N   1 
ATOM   3543 C  CA  . TRP   B 1 191 ? 11.163  29.125  -25.506 1.00 17.60 ? 191 TRP   A CA  1 
ATOM   3544 C  C   . TRP   B 1 191 ? 11.697  30.547  -25.334 1.00 17.45 ? 191 TRP   A C   1 
ATOM   3545 O  O   . TRP   B 1 191 ? 11.209  31.254  -24.464 1.00 18.96 ? 191 TRP   A O   1 
ATOM   3546 C  CB  . TRP   B 1 191 ? 10.705  28.554  -24.152 1.00 15.33 ? 191 TRP   A CB  1 
ATOM   3547 C  CG  . TRP   B 1 191 ? 10.090  27.186  -24.171 1.00 16.71 ? 191 TRP   A CG  1 
ATOM   3548 C  CD1 . TRP   B 1 191 ? 9.676   26.452  -25.248 1.00 17.67 ? 191 TRP   A CD1 1 
ATOM   3549 C  CD2 . TRP   B 1 191 ? 9.824   26.373  -23.011 1.00 18.48 ? 191 TRP   A CD2 1 
ATOM   3550 N  NE1 . TRP   B 1 191 ? 9.184   25.235  -24.833 1.00 16.90 ? 191 TRP   A NE1 1 
ATOM   3551 C  CE2 . TRP   B 1 191 ? 9.278   25.156  -23.471 1.00 17.65 ? 191 TRP   A CE2 1 
ATOM   3552 C  CE3 . TRP   B 1 191 ? 10.044  26.539  -21.634 1.00 18.80 ? 191 TRP   A CE3 1 
ATOM   3553 C  CZ2 . TRP   B 1 191 ? 8.929   24.120  -22.596 1.00 18.75 ? 191 TRP   A CZ2 1 
ATOM   3554 C  CZ3 . TRP   B 1 191 ? 9.700   25.516  -20.770 1.00 21.08 ? 191 TRP   A CZ3 1 
ATOM   3555 C  CH2 . TRP   B 1 191 ? 9.160   24.316  -21.251 1.00 17.22 ? 191 TRP   A CH2 1 
ATOM   3556 N  N   . ASP   B 1 192 ? 12.633  30.989  -26.173 1.00 18.94 ? 192 ASP   A N   1 
ATOM   3557 C  CA  . ASP   B 1 192 ? 13.002  32.400  -26.084 1.00 19.04 ? 192 ASP   A CA  1 
ATOM   3558 C  C   . ASP   B 1 192 ? 11.780  33.247  -26.457 1.00 16.93 ? 192 ASP   A C   1 
ATOM   3559 O  O   . ASP   B 1 192 ? 10.972  32.848  -27.311 1.00 13.72 ? 192 ASP   A O   1 
ATOM   3560 C  CB  . ASP   B 1 192 ? 14.123  32.759  -27.044 1.00 24.61 ? 192 ASP   A CB  1 
ATOM   3561 C  CG  . ASP   B 1 192 ? 15.408  31.957  -26.838 1.00 27.89 ? 192 ASP   A CG  1 
ATOM   3562 O  OD1 . ASP   B 1 192 ? 15.639  31.471  -25.733 1.00 32.04 ? 192 ASP   A OD1 1 
ATOM   3563 O  OD2 . ASP   B 1 192 ? 16.155  31.854  -27.808 1.00 33.62 ? 192 ASP   A OD2 1 
ATOM   3564 N  N   . TYR   B 1 193 ? 11.652  34.402  -25.798 1.00 15.60 ? 193 TYR   A N   1 
ATOM   3565 C  CA  . TYR   B 1 193 ? 10.365  35.085  -25.780 1.00 15.34 ? 193 TYR   A CA  1 
ATOM   3566 C  C   . TYR   B 1 193 ? 10.567  36.569  -25.535 1.00 16.17 ? 193 TYR   A C   1 
ATOM   3567 O  O   . TYR   B 1 193 ? 11.621  36.962  -25.054 1.00 15.47 ? 193 TYR   A O   1 
ATOM   3568 C  CB  . TYR   B 1 193 ? 9.445   34.493  -24.698 1.00 14.48 ? 193 TYR   A CB  1 
ATOM   3569 C  CG  . TYR   B 1 193 ? 9.927   34.718  -23.284 1.00 15.10 ? 193 TYR   A CG  1 
ATOM   3570 C  CD1 . TYR   B 1 193 ? 9.646   35.888  -22.608 1.00 14.83 ? 193 TYR   A CD1 1 
ATOM   3571 C  CD2 . TYR   B 1 193 ? 10.707  33.757  -22.652 1.00 15.81 ? 193 TYR   A CD2 1 
ATOM   3572 C  CE1 . TYR   B 1 193 ? 10.099  36.096  -21.313 1.00 18.42 ? 193 TYR   A CE1 1 
ATOM   3573 C  CE2 . TYR   B 1 193 ? 11.154  33.938  -21.353 1.00 16.59 ? 193 TYR   A CE2 1 
ATOM   3574 C  CZ  . TYR   B 1 193 ? 10.873  35.124  -20.697 1.00 17.81 ? 193 TYR   A CZ  1 
ATOM   3575 O  OH  . TYR   B 1 193 ? 11.364  35.327  -19.448 1.00 18.70 ? 193 TYR   A OH  1 
ATOM   3576 N  N   . TRP   B 1 194 ? 9.544   37.348  -25.913 1.00 15.95 ? 194 TRP   A N   1 
ATOM   3577 C  CA  . TRP   B 1 194 ? 9.392   38.751  -25.541 1.00 16.22 ? 194 TRP   A CA  1 
ATOM   3578 C  C   . TRP   B 1 194 ? 8.297   38.876  -24.483 1.00 16.84 ? 194 TRP   A C   1 
ATOM   3579 O  O   . TRP   B 1 194 ? 7.317   38.111  -24.478 1.00 16.71 ? 194 TRP   A O   1 
ATOM   3580 C  CB  . TRP   B 1 194 ? 9.014   39.569  -26.777 1.00 15.83 ? 194 TRP   A CB  1 
ATOM   3581 C  CG  . TRP   B 1 194 ? 10.031  39.532  -27.872 1.00 17.81 ? 194 TRP   A CG  1 
ATOM   3582 C  CD1 . TRP   B 1 194 ? 11.275  40.110  -27.872 1.00 17.79 ? 194 TRP   A CD1 1 
ATOM   3583 C  CD2 . TRP   B 1 194 ? 9.886   38.868  -29.138 1.00 18.04 ? 194 TRP   A CD2 1 
ATOM   3584 N  NE1 . TRP   B 1 194 ? 11.887  39.879  -29.081 1.00 19.96 ? 194 TRP   A NE1 1 
ATOM   3585 C  CE2 . TRP   B 1 194 ? 11.076  39.098  -29.863 1.00 19.00 ? 194 TRP   A CE2 1 
ATOM   3586 C  CE3 . TRP   B 1 194 ? 8.870   38.095  -29.720 1.00 19.22 ? 194 TRP   A CE3 1 
ATOM   3587 C  CZ2 . TRP   B 1 194 ? 11.283  38.584  -31.138 1.00 21.07 ? 194 TRP   A CZ2 1 
ATOM   3588 C  CZ3 . TRP   B 1 194 ? 9.062   37.614  -31.002 1.00 23.08 ? 194 TRP   A CZ3 1 
ATOM   3589 C  CH2 . TRP   B 1 194 ? 10.265  37.835  -31.692 1.00 22.80 ? 194 TRP   A CH2 1 
ATOM   3590 N  N   . THR   B 1 195 ? 8.426   39.857  -23.582 1.00 14.77 ? 195 THR   A N   1 
ATOM   3591 C  CA  . THR   B 1 195 ? 7.407   39.981  -22.549 1.00 16.74 ? 195 THR   A CA  1 
ATOM   3592 C  C   . THR   B 1 195 ? 7.076   41.460  -22.380 1.00 16.65 ? 195 THR   A C   1 
ATOM   3593 O  O   . THR   B 1 195 ? 7.957   42.314  -22.482 1.00 17.69 ? 195 THR   A O   1 
ATOM   3594 C  CB  . THR   B 1 195 ? 7.822   39.308  -21.212 1.00 16.07 ? 195 THR   A CB  1 
ATOM   3595 O  OG1 . THR   B 1 195 ? 6.728   39.526  -20.324 1.00 18.23 ? 195 THR   A OG1 1 
ATOM   3596 C  CG2 . THR   B 1 195 ? 9.068   39.916  -20.607 1.00 16.38 ? 195 THR   A CG2 1 
ATOM   3597 N  N   . TYR   B 1 196 ? 5.802   41.767  -22.145 1.00 15.94 ? 196 TYR   A N   1 
ATOM   3598 C  CA  . TYR   B 1 196 ? 5.437   43.157  -21.901 1.00 15.84 ? 196 TYR   A CA  1 
ATOM   3599 C  C   . TYR   B 1 196 ? 4.123   43.150  -21.126 1.00 15.77 ? 196 TYR   A C   1 
ATOM   3600 O  O   . TYR   B 1 196 ? 3.386   42.142  -21.156 1.00 16.21 ? 196 TYR   A O   1 
ATOM   3601 C  CB  . TYR   B 1 196 ? 5.288   43.918  -23.229 1.00 16.09 ? 196 TYR   A CB  1 
ATOM   3602 C  CG  . TYR   B 1 196 ? 4.059   43.534  -24.011 1.00 15.63 ? 196 TYR   A CG  1 
ATOM   3603 C  CD1 . TYR   B 1 196 ? 4.017   42.379  -24.778 1.00 14.78 ? 196 TYR   A CD1 1 
ATOM   3604 C  CD2 . TYR   B 1 196 ? 2.913   44.312  -23.944 1.00 14.71 ? 196 TYR   A CD2 1 
ATOM   3605 C  CE1 . TYR   B 1 196 ? 2.872   41.988  -25.469 1.00 15.76 ? 196 TYR   A CE1 1 
ATOM   3606 C  CE2 . TYR   B 1 196 ? 1.783   43.952  -24.660 1.00 14.91 ? 196 TYR   A CE2 1 
ATOM   3607 C  CZ  . TYR   B 1 196 ? 1.741   42.788  -25.403 1.00 15.25 ? 196 TYR   A CZ  1 
ATOM   3608 O  OH  . TYR   B 1 196 ? 0.608   42.421  -26.085 1.00 14.30 ? 196 TYR   A OH  1 
ATOM   3609 N  N   . PRO   B 1 197 ? 3.766   44.257  -20.445 1.00 16.25 ? 197 PRO   A N   1 
ATOM   3610 C  CA  . PRO   B 1 197 ? 2.459   44.370  -19.803 1.00 15.69 ? 197 PRO   A CA  1 
ATOM   3611 C  C   . PRO   B 1 197 ? 1.334   44.791  -20.735 1.00 16.58 ? 197 PRO   A C   1 
ATOM   3612 O  O   . PRO   B 1 197 ? 1.456   45.768  -21.482 1.00 17.27 ? 197 PRO   A O   1 
ATOM   3613 C  CB  . PRO   B 1 197 ? 2.711   45.460  -18.730 1.00 16.53 ? 197 PRO   A CB  1 
ATOM   3614 C  CG  . PRO   B 1 197 ? 3.687   46.393  -19.438 1.00 16.17 ? 197 PRO   A CG  1 
ATOM   3615 C  CD  . PRO   B 1 197 ? 4.618   45.443  -20.184 1.00 16.76 ? 197 PRO   A CD  1 
ATOM   3616 N  N   . GLY   B 1 198 ? 0.212   44.082  -20.649 1.00 14.03 ? 198 GLY   A N   1 
ATOM   3617 C  CA  . GLY   B 1 198 ? -0.848  44.333  -21.610 1.00 16.39 ? 198 GLY   A CA  1 
ATOM   3618 C  C   . GLY   B 1 198 ? -2.226  43.918  -21.110 1.00 14.17 ? 198 GLY   A C   1 
ATOM   3619 O  O   . GLY   B 1 198 ? -2.491  44.018  -19.923 1.00 15.31 ? 198 GLY   A O   1 
ATOM   3620 N  N   . SER   B 1 199 ? -3.085  43.479  -22.043 1.00 14.96 ? 199 SER   A N   1 
ATOM   3621 C  CA  . SER   B 1 199 ? -4.493  43.284  -21.769 1.00 15.06 ? 199 SER   A CA  1 
ATOM   3622 C  C   . SER   B 1 199 ? -4.995  41.972  -22.364 1.00 13.98 ? 199 SER   A C   1 
ATOM   3623 O  O   . SER   B 1 199 ? -4.343  41.357  -23.206 1.00 14.35 ? 199 SER   A O   1 
ATOM   3624 C  CB  . SER   B 1 199 ? -5.313  44.480  -22.261 1.00 13.74 ? 199 SER   A CB  1 
ATOM   3625 O  OG  . SER   B 1 199 ? -5.531  44.418  -23.683 1.00 16.30 ? 199 SER   A OG  1 
ATOM   3626 N  N   . LEU   B 1 200 ? -6.215  41.600  -21.977 1.00 15.89 ? 200 LEU   A N   1 
ATOM   3627 C  CA  . LEU   B 1 200 ? -7.028  40.723  -22.817 1.00 17.25 ? 200 LEU   A CA  1 
ATOM   3628 C  C   . LEU   B 1 200 ? -7.171  41.373  -24.212 1.00 17.40 ? 200 LEU   A C   1 
ATOM   3629 O  O   . LEU   B 1 200 ? -7.216  42.593  -24.341 1.00 16.16 ? 200 LEU   A O   1 
ATOM   3630 C  CB  . LEU   B 1 200 ? -8.424  40.603  -22.187 1.00 20.11 ? 200 LEU   A CB  1 
ATOM   3631 C  CG  . LEU   B 1 200 ? -8.719  39.560  -21.105 1.00 24.29 ? 200 LEU   A CG  1 
ATOM   3632 C  CD1 . LEU   B 1 200 ? -7.528  38.893  -20.425 1.00 23.86 ? 200 LEU   A CD1 1 
ATOM   3633 C  CD2 . LEU   B 1 200 ? -9.793  40.002  -20.148 1.00 24.31 ? 200 LEU   A CD2 1 
ATOM   3634 N  N   . THR   B 1 201 ? -7.257  40.564  -25.274 1.00 15.26 ? 201 THR   A N   1 
ATOM   3635 C  CA  . THR   B 1 201 ? -7.448  41.121  -26.614 1.00 16.41 ? 201 THR   A CA  1 
ATOM   3636 C  C   . THR   B 1 201 ? -8.909  41.017  -27.061 1.00 16.26 ? 201 THR   A C   1 
ATOM   3637 O  O   . THR   B 1 201 ? -9.201  41.237  -28.241 1.00 18.18 ? 201 THR   A O   1 
ATOM   3638 C  CB  . THR   B 1 201 ? -6.478  40.495  -27.626 1.00 15.88 ? 201 THR   A CB  1 
ATOM   3639 O  OG1 . THR   B 1 201 ? -6.940  39.175  -27.904 1.00 15.69 ? 201 THR   A OG1 1 
ATOM   3640 C  CG2 . THR   B 1 201 ? -5.052  40.446  -27.128 1.00 17.77 ? 201 THR   A CG2 1 
ATOM   3641 N  N   . VAL   B 1 202 ? -9.801  40.629  -26.138 1.00 16.34 ? 202 VAL   A N   1 
ATOM   3642 C  CA  . VAL   B 1 202 ? -11.246 40.577  -26.325 1.00 18.42 ? 202 VAL   A CA  1 
ATOM   3643 C  C   . VAL   B 1 202 ? -11.890 41.357  -25.195 1.00 18.29 ? 202 VAL   A C   1 
ATOM   3644 O  O   . VAL   B 1 202 ? -11.354 41.397  -24.076 1.00 18.72 ? 202 VAL   A O   1 
ATOM   3645 C  CB  . VAL   B 1 202 ? -11.835 39.142  -26.340 1.00 17.51 ? 202 VAL   A CB  1 
ATOM   3646 C  CG1 . VAL   B 1 202 ? -11.298 38.311  -27.521 1.00 18.21 ? 202 VAL   A CG1 1 
ATOM   3647 C  CG2 . VAL   B 1 202 ? -11.669 38.414  -25.012 1.00 19.32 ? 202 VAL   A CG2 1 
ATOM   3648 N  N   . PRO   B 1 203 ? -13.100 41.918  -25.425 1.00 20.32 ? 203 PRO   A N   1 
ATOM   3649 C  CA  . PRO   B 1 203 ? -13.891 42.480  -24.326 1.00 19.77 ? 203 PRO   A CA  1 
ATOM   3650 C  C   . PRO   B 1 203 ? -13.958 41.483  -23.168 1.00 21.19 ? 203 PRO   A C   1 
ATOM   3651 O  O   . PRO   B 1 203 ? -14.131 40.282  -23.396 1.00 20.15 ? 203 PRO   A O   1 
ATOM   3652 C  CB  . PRO   B 1 203 ? -15.263 42.681  -25.002 1.00 19.05 ? 203 PRO   A CB  1 
ATOM   3653 C  CG  . PRO   B 1 203 ? -14.867 43.034  -26.437 1.00 20.08 ? 203 PRO   A CG  1 
ATOM   3654 C  CD  . PRO   B 1 203 ? -13.796 41.990  -26.728 1.00 18.77 ? 203 PRO   A CD  1 
ATOM   3655 N  N   . PRO   B 1 204 ? -13.786 41.913  -21.888 1.00 24.02 ? 204 PRO   A N   1 
ATOM   3656 C  CA  . PRO   B 1 204 ? -13.699 43.333  -21.506 1.00 21.63 ? 204 PRO   A CA  1 
ATOM   3657 C  C   . PRO   B 1 204 ? -12.352 44.076  -21.605 1.00 23.10 ? 204 PRO   A C   1 
ATOM   3658 O  O   . PRO   B 1 204 ? -12.213 45.190  -21.087 1.00 20.96 ? 204 PRO   A O   1 
ATOM   3659 C  CB  . PRO   B 1 204 ? -14.191 43.291  -20.030 1.00 24.03 ? 204 PRO   A CB  1 
ATOM   3660 C  CG  . PRO   B 1 204 ? -13.769 41.918  -19.505 1.00 24.61 ? 204 PRO   A CG  1 
ATOM   3661 C  CD  . PRO   B 1 204 ? -13.686 41.014  -20.725 1.00 24.12 ? 204 PRO   A CD  1 
ATOM   3662 N  N   . LEU   B 1 205 ? -11.325 43.466  -22.219 1.00 19.36 ? 205 LEU   A N   1 
ATOM   3663 C  CA  . LEU   B 1 205 ? -10.101 44.192  -22.583 1.00 19.40 ? 205 LEU   A CA  1 
ATOM   3664 C  C   . LEU   B 1 205 ? -9.301  44.660  -21.358 1.00 19.08 ? 205 LEU   A C   1 
ATOM   3665 O  O   . LEU   B 1 205 ? -8.563  45.636  -21.429 1.00 18.13 ? 205 LEU   A O   1 
ATOM   3666 C  CB  . LEU   B 1 205 ? -10.496 45.380  -23.473 1.00 20.86 ? 205 LEU   A CB  1 
ATOM   3667 C  CG  . LEU   B 1 205 ? -10.999 44.994  -24.864 1.00 20.07 ? 205 LEU   A CG  1 
ATOM   3668 C  CD1 . LEU   B 1 205 ? -11.664 46.176  -25.549 1.00 21.57 ? 205 LEU   A CD1 1 
ATOM   3669 C  CD2 . LEU   B 1 205 ? -9.871  44.450  -25.738 1.00 21.57 ? 205 LEU   A CD2 1 
ATOM   3670 N  N   . LEU   B 1 206 ? -9.384  43.923  -20.240 1.00 19.24 ? 206 LEU   A N   1 
ATOM   3671 C  CA  . LEU   B 1 206 ? -8.810  44.328  -18.957 1.00 19.25 ? 206 LEU   A CA  1 
ATOM   3672 C  C   . LEU   B 1 206 ? -7.279  44.316  -18.986 1.00 19.61 ? 206 LEU   A C   1 
ATOM   3673 O  O   . LEU   B 1 206 ? -6.656  43.377  -19.490 1.00 17.16 ? 206 LEU   A O   1 
ATOM   3674 C  CB  . LEU   B 1 206 ? -9.324  43.371  -17.869 1.00 20.86 ? 206 LEU   A CB  1 
ATOM   3675 C  CG  . LEU   B 1 206 ? -10.842 43.344  -17.688 1.00 23.39 ? 206 LEU   A CG  1 
ATOM   3676 C  CD1 . LEU   B 1 206 ? -11.267 42.120  -16.886 1.00 24.99 ? 206 LEU   A CD1 1 
ATOM   3677 C  CD2 . LEU   B 1 206 ? -11.316 44.614  -17.004 1.00 24.84 ? 206 LEU   A CD2 1 
ATOM   3678 N  N   . GLU   B 1 207 ? -6.665  45.327  -18.356 1.00 18.75 ? 207 GLU   A N   1 
ATOM   3679 C  CA  . GLU   B 1 207 ? -5.206  45.466  -18.348 1.00 18.66 ? 207 GLU   A CA  1 
ATOM   3680 C  C   . GLU   B 1 207 ? -4.599  44.692  -17.181 1.00 16.71 ? 207 GLU   A C   1 
ATOM   3681 O  O   . GLU   B 1 207 ? -4.155  45.275  -16.195 1.00 17.45 ? 207 GLU   A O   1 
ATOM   3682 C  CB  . GLU   B 1 207 ? -4.816  46.958  -18.445 1.00 18.42 ? 207 GLU   A CB  1 
ATOM   3683 C  CG  . GLU   B 1 207 ? -5.304  47.546  -19.759 1.00 18.01 ? 207 GLU   A CG  1 
ATOM   3684 C  CD  . GLU   B 1 207 ? -5.152  49.052  -19.957 1.00 20.93 ? 207 GLU   A CD  1 
ATOM   3685 O  OE1 . GLU   B 1 207 ? -5.034  49.731  -18.937 1.00 20.68 ? 207 GLU   A OE1 1 
ATOM   3686 O  OE2 . GLU   B 1 207 ? -5.126  49.520  -21.141 1.00 21.80 ? 207 GLU   A OE2 1 
ATOM   3687 N  N   . SER   B 1 208 ? -4.629  43.355  -17.291 1.00 17.77 ? 208 SER   A N   1 
ATOM   3688 C  CA  . SER   B 1 208 ? -4.277  42.429  -16.223 1.00 18.00 ? 208 SER   A CA  1 
ATOM   3689 C  C   . SER   B 1 208 ? -3.250  41.368  -16.646 1.00 17.73 ? 208 SER   A C   1 
ATOM   3690 O  O   . SER   B 1 208 ? -2.955  40.481  -15.845 1.00 19.47 ? 208 SER   A O   1 
ATOM   3691 C  CB  . SER   B 1 208 ? -5.535  41.745  -15.681 1.00 21.53 ? 208 SER   A CB  1 
ATOM   3692 O  OG  . SER   B 1 208 ? -6.256  41.112  -16.733 1.00 22.29 ? 208 SER   A OG  1 
ATOM   3693 N  N   . VAL   B 1 209 ? -2.692  41.482  -17.868 1.00 16.07 ? 209 VAL   A N   1 
ATOM   3694 C  CA  . VAL   B 1 209 ? -1.974  40.391  -18.509 1.00 17.59 ? 209 VAL   A CA  1 
ATOM   3695 C  C   . VAL   B 1 209 ? -0.480  40.705  -18.570 1.00 17.79 ? 209 VAL   A C   1 
ATOM   3696 O  O   . VAL   B 1 209 ? -0.061  41.710  -19.128 1.00 17.99 ? 209 VAL   A O   1 
ATOM   3697 C  CB  . VAL   B 1 209 ? -2.504  40.097  -19.941 1.00 15.62 ? 209 VAL   A CB  1 
ATOM   3698 C  CG1 . VAL   B 1 209 ? -1.699  38.982  -20.585 1.00 15.30 ? 209 VAL   A CG1 1 
ATOM   3699 C  CG2 . VAL   B 1 209 ? -3.993  39.730  -19.953 1.00 17.02 ? 209 VAL   A CG2 1 
ATOM   3700 N  N   . THR   B 1 210 ? 0.340   39.771  -18.094 1.00 16.71 ? 210 THR   A N   1 
ATOM   3701 C  CA  . THR   B 1 210 ? 1.743   39.711  -18.480 1.00 16.07 ? 210 THR   A CA  1 
ATOM   3702 C  C   . THR   B 1 210 ? 1.836   38.812  -19.710 1.00 16.19 ? 210 THR   A C   1 
ATOM   3703 O  O   . THR   B 1 210 ? 1.560   37.602  -19.601 1.00 14.71 ? 210 THR   A O   1 
ATOM   3704 C  CB  . THR   B 1 210 ? 2.566   39.115  -17.315 1.00 17.49 ? 210 THR   A CB  1 
ATOM   3705 O  OG1 . THR   B 1 210 ? 2.401   39.984  -16.190 1.00 16.68 ? 210 THR   A OG1 1 
ATOM   3706 C  CG2 . THR   B 1 210 ? 4.044   38.943  -17.615 1.00 15.64 ? 210 THR   A CG2 1 
ATOM   3707 N  N   . TRP   B 1 211 ? 2.193   39.397  -20.861 1.00 14.90 ? 211 TRP   A N   1 
ATOM   3708 C  CA  . TRP   B 1 211 ? 2.361   38.671  -22.124 1.00 14.69 ? 211 TRP   A CA  1 
ATOM   3709 C  C   . TRP   B 1 211 ? 3.753   38.035  -22.211 1.00 15.70 ? 211 TRP   A C   1 
ATOM   3710 O  O   . TRP   B 1 211 ? 4.763   38.659  -21.922 1.00 17.16 ? 211 TRP   A O   1 
ATOM   3711 C  CB  . TRP   B 1 211 ? 2.074   39.588  -23.330 1.00 14.31 ? 211 TRP   A CB  1 
ATOM   3712 C  CG  . TRP   B 1 211 ? 0.612   39.791  -23.557 1.00 14.31 ? 211 TRP   A CG  1 
ATOM   3713 C  CD1 . TRP   B 1 211 ? -0.184  40.805  -23.085 1.00 15.04 ? 211 TRP   A CD1 1 
ATOM   3714 C  CD2 . TRP   B 1 211 ? -0.256  38.870  -24.245 1.00 14.19 ? 211 TRP   A CD2 1 
ATOM   3715 N  NE1 . TRP   B 1 211 ? -1.482  40.588  -23.449 1.00 14.63 ? 211 TRP   A NE1 1 
ATOM   3716 C  CE2 . TRP   B 1 211 ? -1.552  39.422  -24.184 1.00 14.46 ? 211 TRP   A CE2 1 
ATOM   3717 C  CE3 . TRP   B 1 211 ? -0.035  37.666  -24.955 1.00 14.89 ? 211 TRP   A CE3 1 
ATOM   3718 C  CZ2 . TRP   B 1 211 ? -2.641  38.794  -24.784 1.00 15.51 ? 211 TRP   A CZ2 1 
ATOM   3719 C  CZ3 . TRP   B 1 211 ? -1.120  37.048  -25.552 1.00 14.32 ? 211 TRP   A CZ3 1 
ATOM   3720 C  CH2 . TRP   B 1 211 ? -2.404  37.590  -25.418 1.00 16.15 ? 211 TRP   A CH2 1 
ATOM   3721 N  N   . ILE   B 1 212 ? 3.782   36.765  -22.608 1.00 14.16 ? 212 ILE   A N   1 
ATOM   3722 C  CA  . ILE   B 1 212 ? 4.985   36.032  -22.913 1.00 15.09 ? 212 ILE   A CA  1 
ATOM   3723 C  C   . ILE   B 1 212 ? 4.792   35.492  -24.320 1.00 15.72 ? 212 ILE   A C   1 
ATOM   3724 O  O   . ILE   B 1 212 ? 3.976   34.591  -24.567 1.00 16.76 ? 212 ILE   A O   1 
ATOM   3725 C  CB  . ILE   B 1 212 ? 5.261   34.947  -21.836 1.00 15.57 ? 212 ILE   A CB  1 
ATOM   3726 C  CG1 . ILE   B 1 212 ? 5.343   35.600  -20.447 1.00 17.62 ? 212 ILE   A CG1 1 
ATOM   3727 C  CG2 . ILE   B 1 212 ? 6.518   34.126  -22.193 1.00 16.74 ? 212 ILE   A CG2 1 
ATOM   3728 C  CD1 . ILE   B 1 212 ? 5.202   34.660  -19.268 1.00 19.66 ? 212 ILE   A CD1 1 
ATOM   3729 N  N   . VAL   B 1 213 ? 5.444   36.157  -25.272 1.00 14.96 ? 213 VAL   A N   1 
ATOM   3730 C  CA  . VAL   B 1 213 ? 5.256   35.795  -26.674 1.00 15.30 ? 213 VAL   A CA  1 
ATOM   3731 C  C   . VAL   B 1 213 ? 6.522   35.073  -27.154 1.00 15.60 ? 213 VAL   A C   1 
ATOM   3732 O  O   . VAL   B 1 213 ? 7.609   35.640  -27.101 1.00 14.09 ? 213 VAL   A O   1 
ATOM   3733 C  CB  . VAL   B 1 213 ? 4.974   37.051  -27.513 1.00 15.46 ? 213 VAL   A CB  1 
ATOM   3734 C  CG1 . VAL   B 1 213 ? 4.843   36.752  -29.010 1.00 16.29 ? 213 VAL   A CG1 1 
ATOM   3735 C  CG2 . VAL   B 1 213 ? 3.742   37.801  -26.993 1.00 18.10 ? 213 VAL   A CG2 1 
ATOM   3736 N  N   . LEU   B 1 214 ? 6.362   33.834  -27.638 1.00 13.86 ? 214 LEU   A N   1 
ATOM   3737 C  CA  . LEU   B 1 214 ? 7.519   33.055  -28.059 1.00 14.85 ? 214 LEU   A CA  1 
ATOM   3738 C  C   . LEU   B 1 214 ? 7.950   33.474  -29.458 1.00 16.08 ? 214 LEU   A C   1 
ATOM   3739 O  O   . LEU   B 1 214 ? 7.119   33.673  -30.343 1.00 15.23 ? 214 LEU   A O   1 
ATOM   3740 C  CB  . LEU   B 1 214 ? 7.204   31.554  -28.021 1.00 17.32 ? 214 LEU   A CB  1 
ATOM   3741 C  CG  . LEU   B 1 214 ? 7.301   30.891  -26.632 1.00 21.09 ? 214 LEU   A CG  1 
ATOM   3742 C  CD1 . LEU   B 1 214 ? 6.604   31.680  -25.548 1.00 22.30 ? 214 LEU   A CD1 1 
ATOM   3743 C  CD2 . LEU   B 1 214 ? 6.773   29.460  -26.652 1.00 22.05 ? 214 LEU   A CD2 1 
ATOM   3744 N  N   . LYS   B 1 215 ? 9.277   33.577  -29.637 1.00 16.06 ? 215 LYS   A N   1 
ATOM   3745 C  CA  . LYS   B 1 215 ? 9.841   33.998  -30.912 1.00 18.20 ? 215 LYS   A CA  1 
ATOM   3746 C  C   . LYS   B 1 215 ? 9.635   32.936  -31.996 1.00 16.99 ? 215 LYS   A C   1 
ATOM   3747 O  O   . LYS   B 1 215 ? 9.366   33.262  -33.148 1.00 16.45 ? 215 LYS   A O   1 
ATOM   3748 C  CB  . LYS   B 1 215 ? 11.325  34.333  -30.740 1.00 18.30 ? 215 LYS   A CB  1 
ATOM   3749 C  CG  . LYS   B 1 215 ? 12.083  34.557  -32.053 1.00 21.57 ? 215 LYS   A CG  1 
ATOM   3750 C  CD  . LYS   B 1 215 ? 13.527  34.975  -31.832 1.00 26.21 ? 215 LYS   A CD  1 
ATOM   3751 C  CE  . LYS   B 1 215 ? 14.286  35.222  -33.124 1.00 29.78 ? 215 LYS   A CE  1 
ATOM   3752 N  NZ  . LYS   B 1 215 ? 15.469  36.083  -32.889 1.00 32.81 ? 215 LYS   A NZ  1 
ATOM   3753 N  N   . GLN   B 1 216 ? 9.822   31.666  -31.651 1.00 17.29 ? 216 GLN   A N   1 
ATOM   3754 C  CA  . GLN   B 1 216 ? 9.870   30.638  -32.678 1.00 17.21 ? 216 GLN   A CA  1 
ATOM   3755 C  C   . GLN   B 1 216 ? 8.455   30.121  -32.978 1.00 18.35 ? 216 GLN   A C   1 
ATOM   3756 O  O   . GLN   B 1 216 ? 7.757   29.604  -32.093 1.00 15.55 ? 216 GLN   A O   1 
ATOM   3757 C  CB  . GLN   B 1 216 ? 10.748  29.460  -32.228 1.00 17.78 ? 216 GLN   A CB  1 
ATOM   3758 C  CG  . GLN   B 1 216 ? 10.754  28.310  -33.227 1.00 18.23 ? 216 GLN   A CG  1 
ATOM   3759 C  CD  . GLN   B 1 216 ? 11.797  27.266  -32.903 1.00 20.63 ? 216 GLN   A CD  1 
ATOM   3760 O  OE1 . GLN   B 1 216 ? 12.220  27.153  -31.756 1.00 21.57 ? 216 GLN   A OE1 1 
ATOM   3761 N  NE2 . GLN   B 1 216 ? 12.197  26.475  -33.899 1.00 21.11 ? 216 GLN   A NE2 1 
ATOM   3762 N  N   . PRO   B 1 217 ? 8.016   30.217  -34.251 1.00 17.58 ? 217 PRO   A N   1 
ATOM   3763 C  CA  . PRO   B 1 217 ? 6.706   29.714  -34.674 1.00 16.96 ? 217 PRO   A CA  1 
ATOM   3764 C  C   . PRO   B 1 217 ? 6.617   28.196  -34.743 1.00 17.81 ? 217 PRO   A C   1 
ATOM   3765 O  O   . PRO   B 1 217 ? 7.634   27.507  -34.825 1.00 17.98 ? 217 PRO   A O   1 
ATOM   3766 C  CB  . PRO   B 1 217 ? 6.549   30.251  -36.101 1.00 20.12 ? 217 PRO   A CB  1 
ATOM   3767 C  CG  . PRO   B 1 217 ? 7.969   30.529  -36.555 1.00 19.34 ? 217 PRO   A CG  1 
ATOM   3768 C  CD  . PRO   B 1 217 ? 8.752   30.919  -35.320 1.00 17.65 ? 217 PRO   A CD  1 
ATOM   3769 N  N   . ILE   B 1 218 ? 5.387   27.681  -34.703 1.00 18.04 ? 218 ILE   A N   1 
ATOM   3770 C  CA  . ILE   B 1 218 ? 5.161   26.287  -35.063 1.00 18.76 ? 218 ILE   A CA  1 
ATOM   3771 C  C   . ILE   B 1 218 ? 4.460   26.261  -36.418 1.00 19.31 ? 218 ILE   A C   1 
ATOM   3772 O  O   . ILE   B 1 218 ? 4.059   27.296  -36.911 1.00 17.44 ? 218 ILE   A O   1 
ATOM   3773 C  CB  . ILE   B 1 218 ? 4.346   25.552  -33.977 1.00 18.29 ? 218 ILE   A CB  1 
ATOM   3774 C  CG1 . ILE   B 1 218 ? 2.938   26.150  -33.819 1.00 17.92 ? 218 ILE   A CG1 1 
ATOM   3775 C  CG2 . ILE   B 1 218 ? 5.110   25.539  -32.654 1.00 20.37 ? 218 ILE   A CG2 1 
ATOM   3776 C  CD1 . ILE   B 1 218 ? 1.988   25.323  -32.944 1.00 18.15 ? 218 ILE   A CD1 1 
ATOM   3777 N  N   . ASN   B 1 219 ? 4.285   25.063  -37.002 1.00 17.54 ? 219 ASN   A N   1 
ATOM   3778 C  CA  . ASN   B 1 219 ? 3.714   24.971  -38.333 1.00 19.91 ? 219 ASN   A CA  1 
ATOM   3779 C  C   . ASN   B 1 219 ? 2.209   24.672  -38.249 1.00 18.62 ? 219 ASN   A C   1 
ATOM   3780 O  O   . ASN   B 1 219 ? 1.758   23.973  -37.326 1.00 18.82 ? 219 ASN   A O   1 
ATOM   3781 C  CB  . ASN   B 1 219 ? 4.372   23.818  -39.116 1.00 23.80 ? 219 ASN   A CB  1 
ATOM   3782 C  CG  . ASN   B 1 219 ? 5.807   24.072  -39.552 1.00 29.63 ? 219 ASN   A CG  1 
ATOM   3783 O  OD1 . ASN   B 1 219 ? 6.575   23.123  -39.761 1.00 33.97 ? 219 ASN   A OD1 1 
ATOM   3784 N  ND2 . ASN   B 1 219 ? 6.175   25.328  -39.742 1.00 29.39 ? 219 ASN   A ND2 1 
ATOM   3785 N  N   . ILE   B 1 220 ? 1.455   25.153  -39.258 1.00 16.88 ? 220 ILE   A N   1 
ATOM   3786 C  CA  . ILE   B 1 220 ? 0.098   24.685  -39.560 1.00 18.18 ? 220 ILE   A CA  1 
ATOM   3787 C  C   . ILE   B 1 220 ? -0.063  24.696  -41.089 1.00 18.38 ? 220 ILE   A C   1 
ATOM   3788 O  O   . ILE   B 1 220 ? 0.491   25.571  -41.750 1.00 18.10 ? 220 ILE   A O   1 
ATOM   3789 C  CB  . ILE   B 1 220 ? -0.967  25.559  -38.864 1.00 16.88 ? 220 ILE   A CB  1 
ATOM   3790 C  CG1 . ILE   B 1 220 ? -2.393  25.046  -39.087 1.00 16.84 ? 220 ILE   A CG1 1 
ATOM   3791 C  CG2 . ILE   B 1 220 ? -0.830  27.007  -39.286 1.00 16.81 ? 220 ILE   A CG2 1 
ATOM   3792 C  CD1 . ILE   B 1 220 ? -3.448  25.765  -38.245 1.00 17.87 ? 220 ILE   A CD1 1 
ATOM   3793 N  N   . SER   B 1 221 ? -0.810  23.737  -41.659 1.00 16.91 ? 221 SER   A N   1 
ATOM   3794 C  CA  . SER   B 1 221 ? -1.044  23.802  -43.101 1.00 18.63 ? 221 SER   A CA  1 
ATOM   3795 C  C   . SER   B 1 221 ? -2.257  24.687  -43.395 1.00 18.08 ? 221 SER   A C   1 
ATOM   3796 O  O   . SER   B 1 221 ? -3.069  24.924  -42.508 1.00 17.94 ? 221 SER   A O   1 
ATOM   3797 C  CB  . SER   B 1 221 ? -1.210  22.428  -43.708 1.00 19.09 ? 221 SER   A CB  1 
ATOM   3798 O  OG  . SER   B 1 221 ? -2.511  21.935  -43.412 1.00 20.12 ? 221 SER   A OG  1 
ATOM   3799 N  N   A SER   B 1 222 ? -2.346  25.194  -44.635 0.50 18.23 ? 222 SER   A N   1 
ATOM   3800 N  N   B SER   B 1 222 ? -2.346  25.174  -44.644 0.50 17.36 ? 222 SER   A N   1 
ATOM   3801 C  CA  A SER   B 1 222 ? -3.497  25.972  -45.076 0.50 18.40 ? 222 SER   A CA  1 
ATOM   3802 C  CA  B SER   B 1 222 ? -3.470  25.964  -45.132 0.50 17.12 ? 222 SER   A CA  1 
ATOM   3803 C  C   A SER   B 1 222 ? -4.775  25.165  -44.872 0.50 18.56 ? 222 SER   A C   1 
ATOM   3804 C  C   B SER   B 1 222 ? -4.777  25.187  -44.971 0.50 17.86 ? 222 SER   A C   1 
ATOM   3805 O  O   A SER   B 1 222 ? -5.784  25.698  -44.431 0.50 18.55 ? 222 SER   A O   1 
ATOM   3806 O  O   B SER   B 1 222 ? -5.814  25.762  -44.666 0.50 18.12 ? 222 SER   A O   1 
ATOM   3807 C  CB  A SER   B 1 222 ? -3.349  26.401  -46.524 0.50 19.10 ? 222 SER   A CB  1 
ATOM   3808 C  CB  B SER   B 1 222 ? -3.244  26.367  -46.583 0.50 16.46 ? 222 SER   A CB  1 
ATOM   3809 O  OG  A SER   B 1 222 ? -2.340  27.388  -46.647 0.50 21.30 ? 222 SER   A OG  1 
ATOM   3810 O  OG  B SER   B 1 222 ? -4.335  27.126  -47.073 0.50 15.83 ? 222 SER   A OG  1 
ATOM   3811 N  N   . GLN   B 1 223 ? -4.725  23.870  -45.204 1.00 19.08 ? 223 GLN   A N   1 
ATOM   3812 C  CA  . GLN   B 1 223 ? -5.898  23.022  -45.061 1.00 19.35 ? 223 GLN   A CA  1 
ATOM   3813 C  C   . GLN   B 1 223 ? -6.298  22.890  -43.593 1.00 20.32 ? 223 GLN   A C   1 
ATOM   3814 O  O   . GLN   B 1 223 ? -7.493  22.937  -43.295 1.00 22.17 ? 223 GLN   A O   1 
ATOM   3815 C  CB  . GLN   B 1 223 ? -5.680  21.656  -45.725 1.00 22.17 ? 223 GLN   A CB  1 
ATOM   3816 C  CG  . GLN   B 1 223 ? -5.806  21.726  -47.240 1.00 26.86 ? 223 GLN   A CG  1 
ATOM   3817 C  CD  . GLN   B 1 223 ? -5.937  20.335  -47.812 1.00 31.89 ? 223 GLN   A CD  1 
ATOM   3818 O  OE1 . GLN   B 1 223 ? -6.742  19.522  -47.341 1.00 32.35 ? 223 GLN   A OE1 1 
ATOM   3819 N  NE2 . GLN   B 1 223 ? -5.103  20.036  -48.794 1.00 29.72 ? 223 GLN   A NE2 1 
ATOM   3820 N  N   . GLN   B 1 224 ? -5.323  22.705  -42.674 1.00 19.05 ? 224 GLN   A N   1 
ATOM   3821 C  CA  . GLN   B 1 224 ? -5.678  22.623  -41.259 1.00 18.70 ? 224 GLN   A CA  1 
ATOM   3822 C  C   . GLN   B 1 224 ? -6.353  23.918  -40.820 1.00 19.92 ? 224 GLN   A C   1 
ATOM   3823 O  O   . GLN   B 1 224 ? -7.392  23.917  -40.152 1.00 22.44 ? 224 GLN   A O   1 
ATOM   3824 C  CB  . GLN   B 1 224 ? -4.442  22.392  -40.392 1.00 17.53 ? 224 GLN   A CB  1 
ATOM   3825 C  CG  . GLN   B 1 224 ? -3.883  20.992  -40.613 1.00 18.88 ? 224 GLN   A CG  1 
ATOM   3826 C  CD  . GLN   B 1 224 ? -2.674  20.775  -39.738 1.00 20.78 ? 224 GLN   A CD  1 
ATOM   3827 O  OE1 . GLN   B 1 224 ? -1.665  21.491  -39.830 1.00 19.44 ? 224 GLN   A OE1 1 
ATOM   3828 N  NE2 . GLN   B 1 224 ? -2.784  19.773  -38.878 1.00 20.35 ? 224 GLN   A NE2 1 
ATOM   3829 N  N   . LEU   B 1 225 ? -5.754  25.034  -41.222 1.00 18.77 ? 225 LEU   A N   1 
ATOM   3830 C  CA  . LEU   B 1 225 ? -6.233  26.308  -40.733 1.00 20.19 ? 225 LEU   A CA  1 
ATOM   3831 C  C   . LEU   B 1 225 ? -7.624  26.635  -41.272 1.00 20.22 ? 225 LEU   A C   1 
ATOM   3832 O  O   . LEU   B 1 225 ? -8.418  27.244  -40.564 1.00 20.55 ? 225 LEU   A O   1 
ATOM   3833 C  CB  . LEU   B 1 225 ? -5.192  27.355  -41.123 1.00 19.42 ? 225 LEU   A CB  1 
ATOM   3834 C  CG  . LEU   B 1 225 ? -5.437  28.771  -40.645 1.00 22.00 ? 225 LEU   A CG  1 
ATOM   3835 C  CD1 . LEU   B 1 225 ? -5.658  28.811  -39.116 1.00 18.93 ? 225 LEU   A CD1 1 
ATOM   3836 C  CD2 . LEU   B 1 225 ? -4.211  29.586  -41.044 1.00 21.19 ? 225 LEU   A CD2 1 
ATOM   3837 N  N   . ALA   B 1 226 ? -7.913  26.282  -42.534 1.00 21.23 ? 226 ALA   A N   1 
ATOM   3838 C  CA  . ALA   B 1 226 ? -9.230  26.521  -43.115 1.00 21.42 ? 226 ALA   A CA  1 
ATOM   3839 C  C   . ALA   B 1 226 ? -10.339 25.824  -42.329 1.00 22.89 ? 226 ALA   A C   1 
ATOM   3840 O  O   . ALA   B 1 226 ? -11.475 26.315  -42.308 1.00 21.60 ? 226 ALA   A O   1 
ATOM   3841 C  CB  . ALA   B 1 226 ? -9.273  26.120  -44.580 1.00 20.98 ? 226 ALA   A CB  1 
ATOM   3842 N  N   . LYS   B 1 227 ? -10.023 24.683  -41.691 1.00 18.79 ? 227 LYS   A N   1 
ATOM   3843 C  CA  . LYS   B 1 227 ? -11.042 24.003  -40.895 1.00 22.09 ? 227 LYS   A CA  1 
ATOM   3844 C  C   . LYS   B 1 227 ? -11.561 24.891  -39.762 1.00 21.13 ? 227 LYS   A C   1 
ATOM   3845 O  O   . LYS   B 1 227 ? -12.700 24.711  -39.348 1.00 22.87 ? 227 LYS   A O   1 
ATOM   3846 C  CB  . LYS   B 1 227 ? -10.521 22.684  -40.304 1.00 27.92 ? 227 LYS   A CB  1 
ATOM   3847 C  CG  . LYS   B 1 227 ? -10.122 21.646  -41.346 1.00 35.86 ? 227 LYS   A CG  1 
ATOM   3848 C  CD  . LYS   B 1 227 ? -9.638  20.303  -40.790 1.00 40.04 ? 227 LYS   A CD  1 
ATOM   3849 C  CE  . LYS   B 1 227 ? -10.727 19.251  -40.681 1.00 47.10 ? 227 LYS   A CE  1 
ATOM   3850 N  NZ  . LYS   B 1 227 ? -10.172 17.873  -40.757 1.00 51.14 ? 227 LYS   A NZ  1 
ATOM   3851 N  N   . PHE   B 1 228 ? -10.750 25.841  -39.257 1.00 19.07 ? 228 PHE   A N   1 
ATOM   3852 C  CA  . PHE   B 1 228 ? -11.173 26.652  -38.115 1.00 19.05 ? 228 PHE   A CA  1 
ATOM   3853 C  C   . PHE   B 1 228 ? -12.171 27.695  -38.580 1.00 18.69 ? 228 PHE   A C   1 
ATOM   3854 O  O   . PHE   B 1 228 ? -13.022 28.148  -37.806 1.00 18.86 ? 228 PHE   A O   1 
ATOM   3855 C  CB  . PHE   B 1 228 ? -10.008 27.321  -37.363 1.00 16.27 ? 228 PHE   A CB  1 
ATOM   3856 C  CG  . PHE   B 1 228 ? -9.148  26.325  -36.615 1.00 17.63 ? 228 PHE   A CG  1 
ATOM   3857 C  CD1 . PHE   B 1 228 ? -9.517  25.840  -35.364 1.00 17.27 ? 228 PHE   A CD1 1 
ATOM   3858 C  CD2 . PHE   B 1 228 ? -7.996  25.816  -37.193 1.00 18.69 ? 228 PHE   A CD2 1 
ATOM   3859 C  CE1 . PHE   B 1 228 ? -8.770  24.861  -34.706 1.00 17.25 ? 228 PHE   A CE1 1 
ATOM   3860 C  CE2 . PHE   B 1 228 ? -7.222  24.869  -36.517 1.00 19.17 ? 228 PHE   A CE2 1 
ATOM   3861 C  CZ  . PHE   B 1 228 ? -7.616  24.377  -35.287 1.00 19.19 ? 228 PHE   A CZ  1 
ATOM   3862 N  N   . ARG   B 1 229 ? -12.061 28.068  -39.853 1.00 18.93 ? 229 ARG   A N   1 
ATOM   3863 C  CA  . ARG   B 1 229 ? -12.906 29.151  -40.366 1.00 20.52 ? 229 ARG   A CA  1 
ATOM   3864 C  C   . ARG   B 1 229 ? -14.337 28.673  -40.617 1.00 23.19 ? 229 ARG   A C   1 
ATOM   3865 O  O   . ARG   B 1 229 ? -15.249 29.493  -40.833 1.00 22.14 ? 229 ARG   A O   1 
ATOM   3866 C  CB  . ARG   B 1 229 ? -12.334 29.755  -41.646 1.00 21.08 ? 229 ARG   A CB  1 
ATOM   3867 C  CG  . ARG   B 1 229 ? -10.956 30.381  -41.488 1.00 19.95 ? 229 ARG   A CG  1 
ATOM   3868 C  CD  . ARG   B 1 229 ? -10.641 31.290  -42.671 1.00 19.99 ? 229 ARG   A CD  1 
ATOM   3869 N  NE  . ARG   B 1 229 ? -9.214  31.614  -42.597 1.00 19.90 ? 229 ARG   A NE  1 
ATOM   3870 C  CZ  . ARG   B 1 229 ? -8.216  30.978  -43.200 1.00 18.66 ? 229 ARG   A CZ  1 
ATOM   3871 N  NH1 . ARG   B 1 229 ? -8.441  29.968  -44.033 1.00 20.71 ? 229 ARG   A NH1 1 
ATOM   3872 N  NH2 . ARG   B 1 229 ? -6.976  31.391  -42.987 1.00 19.10 ? 229 ARG   A NH2 1 
ATOM   3873 N  N   . SER   B 1 230 ? -14.534 27.346  -40.583 1.00 23.02 ? 230 SER   A N   1 
ATOM   3874 C  CA  . SER   B 1 230 ? -15.882 26.804  -40.734 1.00 26.28 ? 230 SER   A CA  1 
ATOM   3875 C  C   . SER   B 1 230 ? -16.662 26.676  -39.412 1.00 25.47 ? 230 SER   A C   1 
ATOM   3876 O  O   . SER   B 1 230 ? -17.842 26.330  -39.434 1.00 26.36 ? 230 SER   A O   1 
ATOM   3877 C  CB  . SER   B 1 230 ? -15.898 25.555  -41.605 1.00 29.95 ? 230 SER   A CB  1 
ATOM   3878 O  OG  . SER   B 1 230 ? -15.578 24.404  -40.844 1.00 34.48 ? 230 SER   A OG  1 
ATOM   3879 N  N   . LEU   B 1 231 ? -16.062 27.051  -38.266 1.00 22.05 ? 231 LEU   A N   1 
ATOM   3880 C  CA  . LEU   B 1 231 ? -16.805 27.194  -37.020 1.00 19.79 ? 231 LEU   A CA  1 
ATOM   3881 C  C   . LEU   B 1 231 ? -17.764 28.367  -37.181 1.00 20.06 ? 231 LEU   A C   1 
ATOM   3882 O  O   . LEU   B 1 231 ? -17.427 29.328  -37.867 1.00 20.88 ? 231 LEU   A O   1 
ATOM   3883 C  CB  . LEU   B 1 231 ? -15.852 27.506  -35.861 1.00 17.88 ? 231 LEU   A CB  1 
ATOM   3884 C  CG  . LEU   B 1 231 ? -14.857 26.415  -35.506 1.00 17.10 ? 231 LEU   A CG  1 
ATOM   3885 C  CD1 . LEU   B 1 231 ? -13.827 26.990  -34.561 1.00 16.37 ? 231 LEU   A CD1 1 
ATOM   3886 C  CD2 . LEU   B 1 231 ? -15.595 25.242  -34.849 1.00 18.60 ? 231 LEU   A CD2 1 
ATOM   3887 N  N   . LEU   B 1 232 ? -18.921 28.301  -36.514 1.00 21.31 ? 232 LEU   A N   1 
ATOM   3888 C  CA  . LEU   B 1 232 ? -19.900 29.387  -36.548 1.00 21.33 ? 232 LEU   A CA  1 
ATOM   3889 C  C   . LEU   B 1 232 ? -19.791 30.253  -35.303 1.00 23.12 ? 232 LEU   A C   1 
ATOM   3890 O  O   . LEU   B 1 232 ? -19.455 29.774  -34.213 1.00 23.78 ? 232 LEU   A O   1 
ATOM   3891 C  CB  . LEU   B 1 232 ? -21.333 28.834  -36.631 1.00 22.39 ? 232 LEU   A CB  1 
ATOM   3892 C  CG  . LEU   B 1 232 ? -21.637 27.824  -37.745 1.00 23.33 ? 232 LEU   A CG  1 
ATOM   3893 C  CD1 . LEU   B 1 232 ? -23.030 27.217  -37.576 1.00 25.07 ? 232 LEU   A CD1 1 
ATOM   3894 C  CD2 . LEU   B 1 232 ? -21.488 28.459  -39.124 1.00 24.42 ? 232 LEU   A CD2 1 
ATOM   3895 N  N   . CYS   B 1 233 ? -20.114 31.544  -35.475 1.00 22.50 ? 233 CYS   A N   1 
ATOM   3896 C  CA  . CYS   B 1 233 ? -20.213 32.441  -34.340 1.00 24.11 ? 233 CYS   A CA  1 
ATOM   3897 C  C   . CYS   B 1 233 ? -21.660 32.500  -33.847 1.00 24.78 ? 233 CYS   A C   1 
ATOM   3898 O  O   . CYS   B 1 233 ? -22.003 33.365  -33.054 1.00 25.43 ? 233 CYS   A O   1 
ATOM   3899 C  CB  . CYS   B 1 233 ? -19.667 33.827  -34.674 1.00 26.38 ? 233 CYS   A CB  1 
ATOM   3900 S  SG  . CYS   B 1 233 ? -20.482 34.621  -36.092 1.00 30.76 ? 233 CYS   A SG  1 
ATOM   3901 N  N   . THR   B 1 234 ? -22.488 31.553  -34.301 1.00 26.13 ? 234 THR   A N   1 
ATOM   3902 C  CA  . THR   B 1 234 ? -23.928 31.583  -34.086 1.00 29.55 ? 234 THR   A CA  1 
ATOM   3903 C  C   . THR   B 1 234 ? -24.388 30.264  -33.462 1.00 32.76 ? 234 THR   A C   1 
ATOM   3904 O  O   . THR   B 1 234 ? -23.803 29.209  -33.699 1.00 27.75 ? 234 THR   A O   1 
ATOM   3905 C  CB  . THR   B 1 234 ? -24.662 31.828  -35.421 1.00 32.23 ? 234 THR   A CB  1 
ATOM   3906 O  OG1 . THR   B 1 234 ? -24.193 30.908  -36.418 1.00 25.47 ? 234 THR   A OG1 1 
ATOM   3907 C  CG2 . THR   B 1 234 ? -24.474 33.233  -35.949 1.00 27.55 ? 234 THR   A CG2 1 
ATOM   3908 N  N   . ALA   B 1 235 ? -25.434 30.349  -32.639 1.00 35.71 ? 235 ALA   A N   1 
ATOM   3909 C  CA  . ALA   B 1 235 ? -25.975 29.189  -31.947 1.00 42.63 ? 235 ALA   A CA  1 
ATOM   3910 C  C   . ALA   B 1 235 ? -26.877 28.382  -32.883 1.00 41.44 ? 235 ALA   A C   1 
ATOM   3911 O  O   . ALA   B 1 235 ? -27.347 28.902  -33.896 1.00 44.86 ? 235 ALA   A O   1 
ATOM   3912 C  CB  . ALA   B 1 235 ? -26.732 29.668  -30.725 1.00 43.28 ? 235 ALA   A CB  1 
ATOM   3913 N  N   . GLU   B 1 236 ? -27.120 27.113  -32.520 1.00 50.15 ? 236 GLU   A N   1 
ATOM   3914 C  CA  . GLU   B 1 236 ? -28.120 26.265  -33.158 1.00 58.12 ? 236 GLU   A CA  1 
ATOM   3915 C  C   . GLU   B 1 236 ? -29.485 26.952  -33.103 1.00 59.41 ? 236 GLU   A C   1 
ATOM   3916 O  O   . GLU   B 1 236 ? -29.921 27.405  -32.045 1.00 59.85 ? 236 GLU   A O   1 
ATOM   3917 C  CB  . GLU   B 1 236 ? -28.175 24.886  -32.493 1.00 62.16 ? 236 GLU   A CB  1 
ATOM   3918 N  N   . GLY   B 1 237 ? -30.138 27.035  -34.268 1.00 64.72 ? 237 GLY   A N   1 
ATOM   3919 C  CA  . GLY   B 1 237 ? -31.411 27.725  -34.398 1.00 67.14 ? 237 GLY   A CA  1 
ATOM   3920 C  C   . GLY   B 1 237 ? -31.271 29.096  -35.057 1.00 69.87 ? 237 GLY   A C   1 
ATOM   3921 O  O   . GLY   B 1 237 ? -32.237 29.615  -35.614 1.00 66.97 ? 237 GLY   A O   1 
ATOM   3922 N  N   . GLU   B 1 238 ? -30.061 29.670  -34.995 1.00 70.25 ? 238 GLU   A N   1 
ATOM   3923 C  CA  . GLU   B 1 238 ? -29.833 31.028  -35.461 1.00 61.75 ? 238 GLU   A CA  1 
ATOM   3924 C  C   . GLU   B 1 238 ? -29.311 30.998  -36.897 1.00 55.70 ? 238 GLU   A C   1 
ATOM   3925 O  O   . GLU   B 1 238 ? -28.703 30.020  -37.329 1.00 53.24 ? 238 GLU   A O   1 
ATOM   3926 C  CB  . GLU   B 1 238 ? -28.899 31.761  -34.495 1.00 68.98 ? 238 GLU   A CB  1 
ATOM   3927 C  CG  . GLU   B 1 238 ? -29.272 33.214  -34.256 1.00 75.39 ? 238 GLU   A CG  1 
ATOM   3928 C  CD  . GLU   B 1 238 ? -28.185 34.057  -33.602 1.00 85.14 ? 238 GLU   A CD  1 
ATOM   3929 O  OE1 . GLU   B 1 238 ? -27.485 33.540  -32.701 1.00 88.69 ? 238 GLU   A OE1 1 
ATOM   3930 O  OE2 . GLU   B 1 238 ? -28.028 35.229  -34.002 1.00 88.88 ? 238 GLU   A OE2 1 
ATOM   3931 N  N   . ALA   B 1 239 ? -29.587 32.084  -37.628 1.00 50.62 ? 239 ALA   A N   1 
ATOM   3932 C  CA  . ALA   B 1 239 ? -29.036 32.360  -38.948 1.00 47.59 ? 239 ALA   A CA  1 
ATOM   3933 C  C   . ALA   B 1 239 ? -27.510 32.275  -38.901 1.00 40.43 ? 239 ALA   A C   1 
ATOM   3934 O  O   . ALA   B 1 239 ? -26.867 33.066  -38.223 1.00 42.19 ? 239 ALA   A O   1 
ATOM   3935 C  CB  . ALA   B 1 239 ? -29.480 33.736  -39.401 1.00 42.82 ? 239 ALA   A CB  1 
ATOM   3936 N  N   . ALA   B 1 240 ? -26.955 31.346  -39.677 1.00 36.43 ? 240 ALA   A N   1 
ATOM   3937 C  CA  . ALA   B 1 240 ? -25.552 30.977  -39.588 1.00 35.99 ? 240 ALA   A CA  1 
ATOM   3938 C  C   . ALA   B 1 240 ? -24.642 32.118  -40.052 1.00 33.76 ? 240 ALA   A C   1 
ATOM   3939 O  O   . ALA   B 1 240 ? -24.814 32.676  -41.130 1.00 29.86 ? 240 ALA   A O   1 
ATOM   3940 C  CB  . ALA   B 1 240 ? -25.320 29.719  -40.384 1.00 36.50 ? 240 ALA   A CB  1 
ATOM   3941 N  N   . ALA   B 1 241 ? -23.630 32.423  -39.231 1.00 29.52 ? 241 ALA   A N   1 
ATOM   3942 C  CA  . ALA   B 1 241 ? -22.489 33.203  -39.673 1.00 24.35 ? 241 ALA   A CA  1 
ATOM   3943 C  C   . ALA   B 1 241 ? -21.194 32.521  -39.216 1.00 23.66 ? 241 ALA   A C   1 
ATOM   3944 O  O   . ALA   B 1 241 ? -21.151 31.900  -38.149 1.00 23.05 ? 241 ALA   A O   1 
ATOM   3945 C  CB  . ALA   B 1 241 ? -22.603 34.610  -39.167 1.00 25.34 ? 241 ALA   A CB  1 
ATOM   3946 N  N   . PHE   B 1 242 ? -20.156 32.631  -40.054 1.00 21.88 ? 242 PHE   A N   1 
ATOM   3947 C  CA  . PHE   B 1 242 ? -18.924 31.858  -39.913 1.00 22.66 ? 242 PHE   A CA  1 
ATOM   3948 C  C   . PHE   B 1 242 ? -17.865 32.691  -39.204 1.00 24.82 ? 242 PHE   A C   1 
ATOM   3949 O  O   . PHE   B 1 242 ? -17.834 33.915  -39.382 1.00 21.81 ? 242 PHE   A O   1 
ATOM   3950 C  CB  . PHE   B 1 242 ? -18.358 31.497  -41.290 1.00 24.28 ? 242 PHE   A CB  1 
ATOM   3951 C  CG  . PHE   B 1 242 ? -19.183 30.471  -42.013 1.00 26.16 ? 242 PHE   A CG  1 
ATOM   3952 C  CD1 . PHE   B 1 242 ? -19.023 29.122  -41.751 1.00 25.93 ? 242 PHE   A CD1 1 
ATOM   3953 C  CD2 . PHE   B 1 242 ? -20.135 30.870  -42.938 1.00 26.39 ? 242 PHE   A CD2 1 
ATOM   3954 C  CE1 . PHE   B 1 242 ? -19.809 28.180  -42.407 1.00 27.68 ? 242 PHE   A CE1 1 
ATOM   3955 C  CE2 . PHE   B 1 242 ? -20.920 29.929  -43.584 1.00 25.78 ? 242 PHE   A CE2 1 
ATOM   3956 C  CZ  . PHE   B 1 242 ? -20.758 28.591  -43.316 1.00 25.52 ? 242 PHE   A CZ  1 
ATOM   3957 N  N   . LEU   B 1 243 ? -16.986 32.008  -38.439 1.00 23.36 ? 243 LEU   A N   1 
ATOM   3958 C  CA  . LEU   B 1 243 ? -15.900 32.686  -37.737 1.00 23.72 ? 243 LEU   A CA  1 
ATOM   3959 C  C   . LEU   B 1 243 ? -14.653 32.697  -38.646 1.00 22.13 ? 243 LEU   A C   1 
ATOM   3960 O  O   . LEU   B 1 243 ? -13.687 31.955  -38.442 1.00 21.50 ? 243 LEU   A O   1 
ATOM   3961 C  CB  . LEU   B 1 243 ? -15.699 31.916  -36.414 1.00 23.37 ? 243 LEU   A CB  1 
ATOM   3962 C  CG  . LEU   B 1 243 ? -14.755 32.476  -35.347 1.00 25.90 ? 243 LEU   A CG  1 
ATOM   3963 C  CD1 . LEU   B 1 243 ? -15.235 33.827  -34.841 1.00 25.32 ? 243 LEU   A CD1 1 
ATOM   3964 C  CD2 . LEU   B 1 243 ? -14.679 31.505  -34.162 1.00 25.79 ? 243 LEU   A CD2 1 
ATOM   3965 N  N   . VAL   B 1 244 ? -14.669 33.528  -39.698 1.00 21.22 ? 244 VAL   A N   1 
ATOM   3966 C  CA  . VAL   B 1 244 ? -13.598 33.505  -40.686 1.00 21.52 ? 244 VAL   A CA  1 
ATOM   3967 C  C   . VAL   B 1 244 ? -12.397 34.263  -40.131 1.00 21.65 ? 244 VAL   A C   1 
ATOM   3968 O  O   . VAL   B 1 244 ? -11.293 34.106  -40.634 1.00 21.52 ? 244 VAL   A O   1 
ATOM   3969 C  CB  . VAL   B 1 244 ? -14.003 34.038  -42.084 1.00 21.87 ? 244 VAL   A CB  1 
ATOM   3970 C  CG1 . VAL   B 1 244 ? -15.059 33.137  -42.703 1.00 22.93 ? 244 VAL   A CG1 1 
ATOM   3971 C  CG2 . VAL   B 1 244 ? -14.526 35.462  -42.000 1.00 22.15 ? 244 VAL   A CG2 1 
ATOM   3972 N  N   . SER   B 1 245 ? -12.625 35.083  -39.100 1.00 19.99 ? 245 SER   A N   1 
ATOM   3973 C  CA  . SER   B 1 245 ? -11.538 35.900  -38.553 1.00 19.16 ? 245 SER   A CA  1 
ATOM   3974 C  C   . SER   B 1 245 ? -11.863 36.263  -37.103 1.00 19.25 ? 245 SER   A C   1 
ATOM   3975 O  O   . SER   B 1 245 ? -13.004 36.629  -36.823 1.00 17.75 ? 245 SER   A O   1 
ATOM   3976 C  CB  . SER   B 1 245 ? -11.398 37.150  -39.360 1.00 21.02 ? 245 SER   A CB  1 
ATOM   3977 O  OG  . SER   B 1 245 ? -10.259 37.872  -38.952 1.00 19.68 ? 245 SER   A OG  1 
ATOM   3978 N  N   . ASN   B 1 246 ? -10.870 36.186  -36.194 1.00 16.79 ? 246 ASN   A N   1 
ATOM   3979 C  CA  . ASN   B 1 246 ? -11.120 36.526  -34.799 1.00 16.88 ? 246 ASN   A CA  1 
ATOM   3980 C  C   . ASN   B 1 246 ? -9.880  37.156  -34.172 1.00 18.12 ? 246 ASN   A C   1 
ATOM   3981 O  O   . ASN   B 1 246 ? -9.574  36.883  -33.018 1.00 17.64 ? 246 ASN   A O   1 
ATOM   3982 C  CB  . ASN   B 1 246 ? -11.554 35.316  -33.963 1.00 15.93 ? 246 ASN   A CB  1 
ATOM   3983 C  CG  . ASN   B 1 246 ? -10.559 34.165  -34.012 1.00 15.77 ? 246 ASN   A CG  1 
ATOM   3984 O  OD1 . ASN   B 1 246 ? -9.535  34.258  -34.679 1.00 15.72 ? 246 ASN   A OD1 1 
ATOM   3985 N  ND2 . ASN   B 1 246 ? -10.893 33.042  -33.385 1.00 14.73 ? 246 ASN   A ND2 1 
ATOM   3986 N  N   . HIS   B 1 247 ? -9.166  38.019  -34.911 1.00 18.03 ? 247 HIS   A N   1 
ATOM   3987 C  CA  . HIS   B 1 247 ? -8.010  38.663  -34.306 1.00 17.34 ? 247 HIS   A CA  1 
ATOM   3988 C  C   . HIS   B 1 247 ? -8.270  40.157  -34.211 1.00 19.94 ? 247 HIS   A C   1 
ATOM   3989 O  O   . HIS   B 1 247 ? -8.940  40.727  -35.059 1.00 22.30 ? 247 HIS   A O   1 
ATOM   3990 C  CB  . HIS   B 1 247 ? -6.702  38.384  -35.076 1.00 20.31 ? 247 HIS   A CB  1 
ATOM   3991 C  CG  . HIS   B 1 247 ? -6.695  38.848  -36.501 1.00 23.16 ? 247 HIS   A CG  1 
ATOM   3992 N  ND1 . HIS   B 1 247 ? -6.013  40.006  -36.919 1.00 25.53 ? 247 HIS   A ND1 1 
ATOM   3993 C  CD2 . HIS   B 1 247 ? -7.320  38.363  -37.598 1.00 23.12 ? 247 HIS   A CD2 1 
ATOM   3994 C  CE1 . HIS   B 1 247 ? -6.208  40.190  -38.222 1.00 25.01 ? 247 HIS   A CE1 1 
ATOM   3995 N  NE2 . HIS   B 1 247 ? -7.013  39.198  -38.661 1.00 27.05 ? 247 HIS   A NE2 1 
ATOM   3996 N  N   . ARG   B 1 248 ? -7.697  40.774  -33.185 1.00 19.68 ? 248 ARG   A N   1 
ATOM   3997 C  CA  . ARG   B 1 248 ? -7.760  42.207  -32.975 1.00 20.02 ? 248 ARG   A CA  1 
ATOM   3998 C  C   . ARG   B 1 248 ? -6.479  42.835  -33.514 1.00 21.00 ? 248 ARG   A C   1 
ATOM   3999 O  O   . ARG   B 1 248 ? -5.404  42.275  -33.291 1.00 21.85 ? 248 ARG   A O   1 
ATOM   4000 C  CB  . ARG   B 1 248 ? -7.841  42.480  -31.475 1.00 18.61 ? 248 ARG   A CB  1 
ATOM   4001 C  CG  . ARG   B 1 248 ? -7.934  43.966  -31.131 1.00 19.22 ? 248 ARG   A CG  1 
ATOM   4002 C  CD  . ARG   B 1 248 ? -7.678  44.294  -29.667 1.00 18.70 ? 248 ARG   A CD  1 
ATOM   4003 N  NE  . ARG   B 1 248 ? -8.242  45.625  -29.355 1.00 21.00 ? 248 ARG   A NE  1 
ATOM   4004 C  CZ  . ARG   B 1 248 ? -7.973  46.346  -28.270 1.00 19.54 ? 248 ARG   A CZ  1 
ATOM   4005 N  NH1 . ARG   B 1 248 ? -7.122  45.898  -27.358 1.00 17.17 ? 248 ARG   A NH1 1 
ATOM   4006 N  NH2 . ARG   B 1 248 ? -8.584  47.513  -28.096 1.00 20.51 ? 248 ARG   A NH2 1 
ATOM   4007 N  N   . PRO   B 1 249 ? -6.543  44.005  -34.195 1.00 20.89 ? 249 PRO   A N   1 
ATOM   4008 C  CA  . PRO   B 1 249 ? -5.343  44.651  -34.736 1.00 20.91 ? 249 PRO   A CA  1 
ATOM   4009 C  C   . PRO   B 1 249 ? -4.451  45.099  -33.587 1.00 20.97 ? 249 PRO   A C   1 
ATOM   4010 O  O   . PRO   B 1 249 ? -4.963  45.414  -32.516 1.00 22.23 ? 249 PRO   A O   1 
ATOM   4011 C  CB  . PRO   B 1 249 ? -5.878  45.934  -35.410 1.00 20.71 ? 249 PRO   A CB  1 
ATOM   4012 C  CG  . PRO   B 1 249 ? -7.334  45.619  -35.677 1.00 24.89 ? 249 PRO   A CG  1 
ATOM   4013 C  CD  . PRO   B 1 249 ? -7.776  44.767  -34.495 1.00 22.37 ? 249 PRO   A CD  1 
ATOM   4014 N  N   . PRO   B 1 250 ? -3.107  45.175  -33.777 1.00 21.32 ? 250 PRO   A N   1 
ATOM   4015 C  CA  . PRO   B 1 250 ? -2.213  45.710  -32.748 1.00 20.96 ? 250 PRO   A CA  1 
ATOM   4016 C  C   . PRO   B 1 250 ? -2.592  47.127  -32.348 1.00 19.53 ? 250 PRO   A C   1 
ATOM   4017 O  O   . PRO   B 1 250 ? -3.013  47.912  -33.197 1.00 21.08 ? 250 PRO   A O   1 
ATOM   4018 C  CB  . PRO   B 1 250 ? -0.810  45.692  -33.368 1.00 19.30 ? 250 PRO   A CB  1 
ATOM   4019 C  CG  . PRO   B 1 250 ? -0.938  44.634  -34.473 1.00 22.61 ? 250 PRO   A CG  1 
ATOM   4020 C  CD  . PRO   B 1 250 ? -2.372  44.701  -34.964 1.00 21.52 ? 250 PRO   A CD  1 
ATOM   4021 N  N   . GLN   B 1 251 ? -2.302  47.436  -31.081 1.00 19.42 ? 251 GLN   A N   1 
ATOM   4022 C  CA  . GLN   B 1 251 ? -2.609  48.695  -30.410 1.00 19.03 ? 251 GLN   A CA  1 
ATOM   4023 C  C   . GLN   B 1 251 ? -1.293  49.389  -30.079 1.00 19.18 ? 251 GLN   A C   1 
ATOM   4024 O  O   . GLN   B 1 251 ? -0.264  48.725  -29.972 1.00 20.96 ? 251 GLN   A O   1 
ATOM   4025 C  CB  . GLN   B 1 251 ? -3.456  48.413  -29.161 1.00 18.76 ? 251 GLN   A CB  1 
ATOM   4026 C  CG  . GLN   B 1 251 ? -4.746  47.664  -29.484 1.00 20.06 ? 251 GLN   A CG  1 
ATOM   4027 C  CD  . GLN   B 1 251 ? -5.571  48.346  -30.547 1.00 25.45 ? 251 GLN   A CD  1 
ATOM   4028 O  OE1 . GLN   B 1 251 ? -6.005  47.729  -31.521 1.00 27.54 ? 251 GLN   A OE1 1 
ATOM   4029 N  NE2 . GLN   B 1 251 ? -5.825  49.632  -30.347 1.00 23.83 ? 251 GLN   A NE2 1 
ATOM   4030 N  N   . PRO   B 1 252 ? -1.273  50.723  -29.869 1.00 20.18 ? 252 PRO   A N   1 
ATOM   4031 C  CA  . PRO   B 1 252 ? -0.016  51.459  -29.670 1.00 18.54 ? 252 PRO   A CA  1 
ATOM   4032 C  C   . PRO   B 1 252 ? 0.657   51.125  -28.337 1.00 20.13 ? 252 PRO   A C   1 
ATOM   4033 O  O   . PRO   B 1 252 ? -0.018  50.926  -27.336 1.00 17.79 ? 252 PRO   A O   1 
ATOM   4034 C  CB  . PRO   B 1 252 ? -0.451  52.929  -29.587 1.00 19.50 ? 252 PRO   A CB  1 
ATOM   4035 C  CG  . PRO   B 1 252 ? -1.884  52.951  -30.075 1.00 21.40 ? 252 PRO   A CG  1 
ATOM   4036 C  CD  . PRO   B 1 252 ? -2.458  51.587  -29.781 1.00 19.67 ? 252 PRO   A CD  1 
ATOM   4037 N  N   . LEU   B 1 253 ? 1.997   51.088  -28.327 1.00 19.47 ? 253 LEU   A N   1 
ATOM   4038 C  CA  . LEU   B 1 253 ? 2.783   50.791  -27.138 1.00 21.38 ? 253 LEU   A CA  1 
ATOM   4039 C  C   . LEU   B 1 253 ? 2.582   51.873  -26.073 1.00 22.37 ? 253 LEU   A C   1 
ATOM   4040 O  O   . LEU   B 1 253 ? 2.528   51.598  -24.882 1.00 17.78 ? 253 LEU   A O   1 
ATOM   4041 C  CB  . LEU   B 1 253 ? 4.260   50.714  -27.543 1.00 24.94 ? 253 LEU   A CB  1 
ATOM   4042 C  CG  . LEU   B 1 253 ? 4.771   49.318  -27.897 1.00 28.68 ? 253 LEU   A CG  1 
ATOM   4043 C  CD1 . LEU   B 1 253 ? 6.254   49.387  -28.260 1.00 30.96 ? 253 LEU   A CD1 1 
ATOM   4044 C  CD2 . LEU   B 1 253 ? 4.527   48.329  -26.752 1.00 26.86 ? 253 LEU   A CD2 1 
ATOM   4045 N  N   . LYS   B 1 254 ? 2.493   53.129  -26.501 1.00 22.36 ? 254 LYS   A N   1 
ATOM   4046 C  CA  . LYS   B 1 254 ? 2.230   54.190  -25.535 1.00 25.76 ? 254 LYS   A CA  1 
ATOM   4047 C  C   . LYS   B 1 254 ? 3.233   54.179  -24.369 1.00 24.02 ? 254 LYS   A C   1 
ATOM   4048 O  O   . LYS   B 1 254 ? 2.861   54.426  -23.235 1.00 23.34 ? 254 LYS   A O   1 
ATOM   4049 C  CB  . LYS   B 1 254 ? 0.794   54.068  -25.024 1.00 27.58 ? 254 LYS   A CB  1 
ATOM   4050 C  CG  . LYS   B 1 254 ? -0.245  54.551  -26.019 1.00 32.71 ? 254 LYS   A CG  1 
ATOM   4051 C  CD  . LYS   B 1 254 ? -1.512  55.002  -25.339 1.00 38.54 ? 254 LYS   A CD  1 
ATOM   4052 C  CE  . LYS   B 1 254 ? -2.020  56.280  -25.962 1.00 48.05 ? 254 LYS   A CE  1 
ATOM   4053 N  NZ  . LYS   B 1 254 ? -2.136  56.120  -27.432 1.00 49.98 ? 254 LYS   A NZ  1 
ATOM   4054 N  N   . GLY   B 1 255 ? 4.504   53.903  -24.655 1.00 22.29 ? 255 GLY   A N   1 
ATOM   4055 C  CA  . GLY   B 1 255 ? 5.558   54.148  -23.676 1.00 23.33 ? 255 GLY   A CA  1 
ATOM   4056 C  C   . GLY   B 1 255 ? 6.023   52.849  -23.033 1.00 24.26 ? 255 GLY   A C   1 
ATOM   4057 O  O   . GLY   B 1 255 ? 7.004   52.836  -22.303 1.00 22.45 ? 255 GLY   A O   1 
ATOM   4058 N  N   . ARG   B 1 256 ? 5.311   51.746  -23.306 1.00 19.52 ? 256 ARG   A N   1 
ATOM   4059 C  CA  . ARG   B 1 256 ? 5.658   50.491  -22.646 1.00 19.73 ? 256 ARG   A CA  1 
ATOM   4060 C  C   . ARG   B 1 256 ? 6.950   49.944  -23.261 1.00 22.41 ? 256 ARG   A C   1 
ATOM   4061 O  O   . ARG   B 1 256 ? 7.263   50.238  -24.415 1.00 23.30 ? 256 ARG   A O   1 
ATOM   4062 C  CB  . ARG   B 1 256 ? 4.523   49.464  -22.808 1.00 18.04 ? 256 ARG   A CB  1 
ATOM   4063 C  CG  . ARG   B 1 256 ? 3.302   49.688  -21.921 1.00 18.60 ? 256 ARG   A CG  1 
ATOM   4064 C  CD  . ARG   B 1 256 ? 2.221   48.694  -22.370 1.00 17.87 ? 256 ARG   A CD  1 
ATOM   4065 N  NE  . ARG   B 1 256 ? 1.576   49.048  -23.636 1.00 16.77 ? 256 ARG   A NE  1 
ATOM   4066 C  CZ  . ARG   B 1 256 ? 0.699   48.292  -24.272 1.00 17.68 ? 256 ARG   A CZ  1 
ATOM   4067 N  NH1 . ARG   B 1 256 ? 0.409   47.089  -23.791 1.00 14.86 ? 256 ARG   A NH1 1 
ATOM   4068 N  NH2 . ARG   B 1 256 ? 0.130   48.747  -25.383 1.00 16.28 ? 256 ARG   A NH2 1 
ATOM   4069 N  N   . LYS   B 1 257 ? 7.675   49.114  -22.503 1.00 21.81 ? 257 LYS   A N   1 
ATOM   4070 C  CA  . LYS   B 1 257 ? 8.916   48.541  -22.990 1.00 23.26 ? 257 LYS   A CA  1 
ATOM   4071 C  C   . LYS   B 1 257 ? 8.766   47.029  -23.091 1.00 22.76 ? 257 LYS   A C   1 
ATOM   4072 O  O   . LYS   B 1 257 ? 8.146   46.389  -22.230 1.00 20.66 ? 257 LYS   A O   1 
ATOM   4073 C  CB  . LYS   B 1 257 ? 10.116  48.949  -22.136 1.00 28.02 ? 257 LYS   A CB  1 
ATOM   4074 C  CG  . LYS   B 1 257 ? 10.610  50.373  -22.407 1.00 30.35 ? 257 LYS   A CG  1 
ATOM   4075 C  CD  . LYS   B 1 257 ? 11.591  50.863  -21.361 1.00 36.30 ? 257 LYS   A CD  1 
ATOM   4076 C  CE  . LYS   B 1 257 ? 11.718  52.373  -21.313 1.00 37.90 ? 257 LYS   A CE  1 
ATOM   4077 N  NZ  . LYS   B 1 257 ? 12.716  52.811  -20.304 1.00 42.50 ? 257 LYS   A NZ  1 
ATOM   4078 N  N   . VAL   B 1 258 ? 9.223   46.510  -24.232 1.00 20.27 ? 258 VAL   A N   1 
ATOM   4079 C  CA  . VAL   B 1 258 ? 9.148   45.076  -24.466 1.00 20.26 ? 258 VAL   A CA  1 
ATOM   4080 C  C   . VAL   B 1 258 ? 10.532  44.545  -24.119 1.00 20.75 ? 258 VAL   A C   1 
ATOM   4081 O  O   . VAL   B 1 258 ? 11.500  45.195  -24.482 1.00 20.04 ? 258 VAL   A O   1 
ATOM   4082 C  CB  . VAL   B 1 258 ? 8.805   44.805  -25.940 1.00 20.66 ? 258 VAL   A CB  1 
ATOM   4083 C  CG1 . VAL   B 1 258 ? 8.755   43.304  -26.191 1.00 19.35 ? 258 VAL   A CG1 1 
ATOM   4084 C  CG2 . VAL   B 1 258 ? 7.484   45.472  -26.338 1.00 19.15 ? 258 VAL   A CG2 1 
ATOM   4085 N  N   . ARG   B 1 259 ? 10.634  43.432  -23.373 1.00 18.37 ? 259 ARG   A N   1 
ATOM   4086 C  CA  . ARG   B 1 259 ? 11.946  42.921  -22.999 1.00 17.77 ? 259 ARG   A CA  1 
ATOM   4087 C  C   . ARG   B 1 259 ? 12.108  41.544  -23.616 1.00 18.83 ? 259 ARG   A C   1 
ATOM   4088 O  O   . ARG   B 1 259 ? 11.104  40.892  -23.871 1.00 16.69 ? 259 ARG   A O   1 
ATOM   4089 C  CB  . ARG   B 1 259 ? 12.024  42.717  -21.486 1.00 19.71 ? 259 ARG   A CB  1 
ATOM   4090 C  CG  . ARG   B 1 259 ? 12.039  44.021  -20.703 1.00 21.10 ? 259 ARG   A CG  1 
ATOM   4091 C  CD  . ARG   B 1 259 ? 11.926  43.751  -19.211 1.00 24.84 ? 259 ARG   A CD  1 
ATOM   4092 N  NE  . ARG   B 1 259 ? 10.636  43.232  -18.774 1.00 23.65 ? 259 ARG   A NE  1 
ATOM   4093 C  CZ  . ARG   B 1 259 ? 10.428  42.593  -17.627 1.00 23.26 ? 259 ARG   A CZ  1 
ATOM   4094 N  NH1 . ARG   B 1 259 ? 11.433  42.337  -16.809 1.00 24.86 ? 259 ARG   A NH1 1 
ATOM   4095 N  NH2 . ARG   B 1 259 ? 9.215   42.192  -17.296 1.00 25.27 ? 259 ARG   A NH2 1 
ATOM   4096 N  N   . ALA   B 1 260 ? 13.363  41.121  -23.808 1.00 18.34 ? 260 ALA   A N   1 
ATOM   4097 C  CA  . ALA   B 1 260 ? 13.690  39.835  -24.420 1.00 18.92 ? 260 ALA   A CA  1 
ATOM   4098 C  C   . ALA   B 1 260 ? 14.409  38.963  -23.388 1.00 18.14 ? 260 ALA   A C   1 
ATOM   4099 O  O   . ALA   B 1 260 ? 15.217  39.455  -22.586 1.00 17.11 ? 260 ALA   A O   1 
ATOM   4100 C  CB  . ALA   B 1 260 ? 14.529  40.040  -25.667 1.00 19.29 ? 260 ALA   A CB  1 
ATOM   4101 N  N   . SER   B 1 261 ? 14.095  37.662  -23.430 1.00 17.13 ? 261 SER   A N   1 
ATOM   4102 C  CA  . SER   B 1 261 ? 14.721  36.671  -22.581 1.00 18.96 ? 261 SER   A CA  1 
ATOM   4103 C  C   . SER   B 1 261 ? 16.056  36.236  -23.173 1.00 20.07 ? 261 SER   A C   1 
ATOM   4104 O  O   . SER   B 1 261 ? 16.734  35.398  -22.586 1.00 21.66 ? 261 SER   A O   1 
ATOM   4105 C  CB  . SER   B 1 261 ? 13.814  35.448  -22.506 1.00 17.95 ? 261 SER   A CB  1 
ATOM   4106 O  OG  . SER   B 1 261 ? 13.886  34.744  -23.747 1.00 15.61 ? 261 SER   A OG  1 
ATOM   4107 N  N   . PHE   B 1 262 ? 16.382  36.732  -24.371 1.00 20.70 ? 262 PHE   A N   1 
ATOM   4108 C  CA  . PHE   B 1 262 ? 17.512  36.195  -25.103 1.00 24.00 ? 262 PHE   A CA  1 
ATOM   4109 C  C   . PHE   B 1 262 ? 18.268  37.368  -25.715 1.00 27.85 ? 262 PHE   A C   1 
ATOM   4110 O  O   . PHE   B 1 262 ? 17.711  38.462  -25.884 1.00 23.36 ? 262 PHE   A O   1 
ATOM   4111 C  CB  . PHE   B 1 262 ? 17.042  35.240  -26.209 1.00 23.41 ? 262 PHE   A CB  1 
ATOM   4112 C  CG  . PHE   B 1 262 ? 16.141  35.928  -27.201 1.00 24.33 ? 262 PHE   A CG  1 
ATOM   4113 C  CD1 . PHE   B 1 262 ? 14.812  36.189  -26.888 1.00 22.66 ? 262 PHE   A CD1 1 
ATOM   4114 C  CD2 . PHE   B 1 262 ? 16.632  36.371  -28.421 1.00 25.19 ? 262 PHE   A CD2 1 
ATOM   4115 C  CE1 . PHE   B 1 262 ? 13.983  36.825  -27.807 1.00 22.76 ? 262 PHE   A CE1 1 
ATOM   4116 C  CE2 . PHE   B 1 262 ? 15.809  37.030  -29.322 1.00 24.55 ? 262 PHE   A CE2 1 
ATOM   4117 C  CZ  . PHE   B 1 262 ? 14.484  37.256  -29.017 1.00 26.16 ? 262 PHE   A CZ  1 
ATOM   4118 N  N   . HIS   B 1 263 ? 19.543  37.105  -26.012 1.00 34.16 ? 263 HIS   A N   1 
ATOM   4119 C  CA  . HIS   B 1 263 ? 20.312  37.947  -26.914 1.00 45.13 ? 263 HIS   A CA  1 
ATOM   4120 C  C   . HIS   B 1 263 ? 20.989  37.048  -27.956 1.00 52.08 ? 263 HIS   A C   1 
ATOM   4121 O  O   . HIS   B 1 263 ? 21.994  36.393  -27.678 1.00 53.86 ? 263 HIS   A O   1 
ATOM   4122 C  CB  . HIS   B 1 263 ? 21.246  38.917  -26.159 1.00 48.06 ? 263 HIS   A CB  1 
ATOM   4123 C  CG  . HIS   B 1 263 ? 22.087  38.351  -25.054 1.00 52.76 ? 263 HIS   A CG  1 
ATOM   4124 N  ND1 . HIS   B 1 263 ? 22.826  39.174  -24.208 1.00 57.66 ? 263 HIS   A ND1 1 
ATOM   4125 C  CD2 . HIS   B 1 263 ? 22.319  37.084  -24.634 1.00 57.50 ? 263 HIS   A CD2 1 
ATOM   4126 C  CE1 . HIS   B 1 263 ? 23.474  38.435  -23.324 1.00 63.27 ? 263 HIS   A CE1 1 
ATOM   4127 N  NE2 . HIS   B 1 263 ? 23.173  37.145  -23.561 1.00 58.01 ? 263 HIS   A NE2 1 
ATOM   4128 O  OXT . HIS   B 1 263 ? 20.519  36.953  -29.095 1.00 56.57 ? 263 HIS   A OXT 1 
HETATM 4129 ZN ZN  . ZN    C 2 .   ? 20.613  4.019   -13.292 1.00 17.32 ? 301 ZN    B ZN  1 
HETATM 4130 C  C13 . A1IEN D 3 .   ? 20.823  -1.347  -19.199 1.00 46.10 ? 302 A1IEN B C13 1 
HETATM 4131 C  C20 . A1IEN D 3 .   ? 20.182  -0.776  -12.577 1.00 32.89 ? 302 A1IEN B C20 1 
HETATM 4132 C  C12 . A1IEN D 3 .   ? 19.714  -0.299  -19.321 1.00 41.28 ? 302 A1IEN B C12 1 
HETATM 4133 C  C16 . A1IEN D 3 .   ? 21.550  -4.314  -21.542 1.00 53.73 ? 302 A1IEN B C16 1 
HETATM 4134 O  O22 . A1IEN D 3 .   ? 20.763  -0.027  -11.589 1.00 31.25 ? 302 A1IEN B O22 1 
HETATM 4135 C  C23 . A1IEN D 3 .   ? 21.325  -0.554  -10.411 1.00 26.31 ? 302 A1IEN B C23 1 
HETATM 4136 O  O21 . A1IEN D 3 .   ? 19.624  -1.833  -12.273 1.00 37.13 ? 302 A1IEN B O21 1 
HETATM 4137 C  C2  . A1IEN D 3 .   ? 20.144  -0.322  -13.988 1.00 34.66 ? 302 A1IEN B C2  1 
HETATM 4138 C  C3  . A1IEN D 3 .   ? 19.448  -1.059  -14.983 1.00 32.33 ? 302 A1IEN B C3  1 
HETATM 4139 C  C4  . A1IEN D 3 .   ? 19.411  -0.601  -16.313 1.00 34.79 ? 302 A1IEN B C4  1 
HETATM 4140 C  C5  . A1IEN D 3 .   ? 20.043  0.623   -16.679 1.00 34.94 ? 302 A1IEN B C5  1 
HETATM 4141 C  C6  . A1IEN D 3 .   ? 20.731  1.387   -15.688 1.00 31.78 ? 302 A1IEN B C6  1 
HETATM 4142 S  S7  . A1IEN D 3 .   ? 21.580  2.998   -15.895 1.00 29.64 ? 302 A1IEN B S7  1 
HETATM 4143 O  O9  . A1IEN D 3 .   ? 20.607  4.088   -16.421 1.00 26.15 ? 302 A1IEN B O9  1 
HETATM 4144 N  N10 . A1IEN D 3 .   ? 22.012  3.561   -14.261 1.00 27.78 ? 302 A1IEN B N10 1 
HETATM 4145 O  O8  . A1IEN D 3 .   ? 22.837  3.014   -16.691 1.00 24.32 ? 302 A1IEN B O8  1 
HETATM 4146 C  C1  . A1IEN D 3 .   ? 20.753  0.900   -14.362 1.00 34.31 ? 302 A1IEN B C1  1 
HETATM 4147 S  S11 . A1IEN D 3 .   ? 19.999  1.248   -18.352 1.00 38.55 ? 302 A1IEN B S11 1 
HETATM 4148 C  C14 . A1IEN D 3 .   ? 21.080  -2.146  -20.461 1.00 51.73 ? 302 A1IEN B C14 1 
HETATM 4149 C  C18 . A1IEN D 3 .   ? 21.145  -1.528  -21.735 1.00 53.42 ? 302 A1IEN B C18 1 
HETATM 4150 C  C19 . A1IEN D 3 .   ? 21.408  -2.295  -22.894 1.00 55.64 ? 302 A1IEN B C19 1 
HETATM 4151 C  C17 . A1IEN D 3 .   ? 21.607  -3.684  -22.794 1.00 55.84 ? 302 A1IEN B C17 1 
HETATM 4152 C  C15 . A1IEN D 3 .   ? 21.291  -3.548  -20.382 1.00 57.51 ? 302 A1IEN B C15 1 
HETATM 4153 ZN ZN  . ZN    E 2 .   ? -6.240  35.253  -27.308 1.00 16.05 ? 301 ZN    A ZN  1 
HETATM 4154 C  C13 . A1IEN F 3 .   ? -11.059 34.232  -20.693 1.00 43.39 ? 302 A1IEN A C13 1 
HETATM 4155 C  C20 . A1IEN F 3 .   ? -11.099 34.422  -27.780 1.00 25.67 ? 302 A1IEN A C20 1 
HETATM 4156 C  C12 . A1IEN F 3 .   ? -9.730  33.986  -21.349 1.00 36.51 ? 302 A1IEN A C12 1 
HETATM 4157 C  C16 . A1IEN F 3 .   ? -13.308 31.122  -20.498 1.00 56.09 ? 302 A1IEN A C16 1 
HETATM 4158 O  O22 . A1IEN F 3 .   ? -10.482 35.072  -28.775 1.00 24.09 ? 302 A1IEN A O22 1 
HETATM 4159 C  C23 . A1IEN F 3 .   ? -11.002 35.043  -30.073 1.00 21.71 ? 302 A1IEN A C23 1 
HETATM 4160 O  O21 . A1IEN F 3 .   ? -11.923 33.540  -28.098 1.00 24.90 ? 302 A1IEN A O21 1 
HETATM 4161 C  C2  . A1IEN F 3 .   ? -10.644 34.689  -26.389 1.00 23.70 ? 302 A1IEN A C2  1 
HETATM 4162 C  C3  . A1IEN F 3 .   ? -11.329 34.188  -25.286 1.00 24.50 ? 302 A1IEN A C3  1 
HETATM 4163 C  C4  . A1IEN F 3 .   ? -10.851 34.420  -24.000 1.00 24.73 ? 302 A1IEN A C4  1 
HETATM 4164 C  C5  . A1IEN F 3 .   ? -9.662  35.154  -23.793 1.00 26.37 ? 302 A1IEN A C5  1 
HETATM 4165 C  C6  . A1IEN F 3 .   ? -8.935  35.643  -24.916 1.00 21.53 ? 302 A1IEN A C6  1 
HETATM 4166 S  S7  . A1IEN F 3 .   ? -7.362  36.575  -24.825 1.00 22.01 ? 302 A1IEN A S7  1 
HETATM 4167 O  O9  . A1IEN F 3 .   ? -6.280  35.781  -24.120 1.00 20.94 ? 302 A1IEN A O9  1 
HETATM 4168 N  N10 . A1IEN F 3 .   ? -6.886  36.835  -26.492 1.00 19.82 ? 302 A1IEN A N10 1 
HETATM 4169 O  O8  . A1IEN F 3 .   ? -7.558  37.961  -24.192 1.00 20.21 ? 302 A1IEN A O8  1 
HETATM 4170 C  C1  . A1IEN F 3 .   ? -9.450  35.400  -26.180 1.00 22.07 ? 302 A1IEN A C1  1 
HETATM 4171 S  S11 . A1IEN F 3 .   ? -8.980  35.455  -22.176 1.00 27.82 ? 302 A1IEN A S11 1 
HETATM 4172 C  C14 . A1IEN F 3 .   ? -11.640 32.915  -20.227 1.00 50.67 ? 302 A1IEN A C14 1 
HETATM 4173 C  C18 . A1IEN F 3 .   ? -11.112 32.254  -19.089 1.00 49.16 ? 302 A1IEN A C18 1 
HETATM 4174 C  C19 . A1IEN F 3 .   ? -11.693 31.050  -18.660 1.00 50.62 ? 302 A1IEN A C19 1 
HETATM 4175 C  C17 . A1IEN F 3 .   ? -12.776 30.475  -19.369 1.00 53.93 ? 302 A1IEN A C17 1 
HETATM 4176 C  C15 . A1IEN F 3 .   ? -12.741 32.344  -20.920 1.00 54.90 ? 302 A1IEN A C15 1 
HETATM 4177 NA NA  . NA    G 4 .   ? -6.941  28.229  -5.887  1.00 30.11 ? 303 NA    A NA  1 
HETATM 4178 O  O   . HOH   H 5 .   ? 1.060   12.416  -18.867 1.00 48.95 ? 401 HOH   B O   1 
HETATM 4179 O  O   . HOH   H 5 .   ? 17.215  -2.973  -12.458 1.00 32.56 ? 402 HOH   B O   1 
HETATM 4180 O  O   . HOH   H 5 .   ? 25.830  22.774  -5.114  1.00 42.54 ? 403 HOH   B O   1 
HETATM 4181 O  O   . HOH   H 5 .   ? 29.238  12.679  -1.227  1.00 30.18 ? 404 HOH   B O   1 
HETATM 4182 O  O   . HOH   H 5 .   ? 24.560  -9.629  -12.522 1.00 39.09 ? 405 HOH   B O   1 
HETATM 4183 O  O   . HOH   H 5 .   ? 30.358  7.221   -27.028 1.00 29.54 ? 406 HOH   B O   1 
HETATM 4184 O  O   . HOH   H 5 .   ? 5.880   5.332   -25.718 1.00 20.71 ? 407 HOH   B O   1 
HETATM 4185 O  O   . HOH   H 5 .   ? 36.107  4.477   -15.462 1.00 34.39 ? 408 HOH   B O   1 
HETATM 4186 O  O   . HOH   H 5 .   ? 9.800   -4.718  -15.046 1.00 29.31 ? 409 HOH   B O   1 
HETATM 4187 O  O   . HOH   H 5 .   ? 14.472  17.018  -29.179 1.00 27.35 ? 410 HOH   B O   1 
HETATM 4188 O  O   . HOH   H 5 .   ? 17.069  19.959  -28.046 1.00 24.06 ? 411 HOH   B O   1 
HETATM 4189 O  O   . HOH   H 5 .   ? 22.494  10.085  -26.490 1.00 31.72 ? 412 HOH   B O   1 
HETATM 4190 O  O   . HOH   H 5 .   ? 6.028   2.662   -33.274 1.00 38.74 ? 413 HOH   B O   1 
HETATM 4191 O  O   . HOH   H 5 .   ? -1.789  13.682  -12.852 1.00 39.41 ? 414 HOH   B O   1 
HETATM 4192 O  O   . HOH   H 5 .   ? 23.101  0.296   -33.703 1.00 30.39 ? 415 HOH   B O   1 
HETATM 4193 O  O   . HOH   H 5 .   ? 25.280  1.334   -10.737 1.00 20.84 ? 416 HOH   B O   1 
HETATM 4194 O  O   . HOH   H 5 .   ? 3.278   3.412   -24.065 1.00 26.07 ? 417 HOH   B O   1 
HETATM 4195 O  O   . HOH   H 5 .   ? 15.672  23.651  -10.633 1.00 28.91 ? 418 HOH   B O   1 
HETATM 4196 O  O   . HOH   H 5 .   ? 26.761  8.190   6.798   1.00 30.40 ? 419 HOH   B O   1 
HETATM 4197 O  O   . HOH   H 5 .   ? 10.349  8.994   -29.254 1.00 20.24 ? 420 HOH   B O   1 
HETATM 4198 O  O   . HOH   H 5 .   ? 28.677  7.700   -7.073  1.00 23.98 ? 421 HOH   B O   1 
HETATM 4199 O  O   . HOH   H 5 .   ? 3.687   16.190  -8.112  1.00 32.62 ? 422 HOH   B O   1 
HETATM 4200 O  O   . HOH   H 5 .   ? 2.730   10.376  -16.206 1.00 22.62 ? 423 HOH   B O   1 
HETATM 4201 O  O   . HOH   H 5 .   ? 1.039   -0.399  -5.618  1.00 28.43 ? 424 HOH   B O   1 
HETATM 4202 O  O   . HOH   H 5 .   ? -3.629  7.592   -20.720 1.00 36.51 ? 425 HOH   B O   1 
HETATM 4203 O  O   . HOH   H 5 .   ? 37.905  6.411   -17.033 1.00 44.72 ? 426 HOH   B O   1 
HETATM 4204 O  O   . HOH   H 5 .   ? 23.928  -15.969 -2.425  1.00 51.13 ? 427 HOH   B O   1 
HETATM 4205 O  O   . HOH   H 5 .   ? -1.026  11.290  -10.170 1.00 32.49 ? 428 HOH   B O   1 
HETATM 4206 O  O   . HOH   H 5 .   ? 12.854  25.944  -15.876 1.00 34.53 ? 429 HOH   B O   1 
HETATM 4207 O  O   . HOH   H 5 .   ? 10.657  1.152   6.430   1.00 26.08 ? 430 HOH   B O   1 
HETATM 4208 O  O   . HOH   H 5 .   ? 20.479  13.709  -29.436 1.00 25.28 ? 431 HOH   B O   1 
HETATM 4209 O  O   . HOH   H 5 .   ? 29.163  21.402  -0.776  1.00 47.12 ? 432 HOH   B O   1 
HETATM 4210 O  O   . HOH   H 5 .   ? 21.812  16.882  -29.805 1.00 35.43 ? 433 HOH   B O   1 
HETATM 4211 O  O   . HOH   H 5 .   ? 30.473  -3.396  -22.775 1.00 35.94 ? 434 HOH   B O   1 
HETATM 4212 O  O   . HOH   H 5 .   ? 3.642   -5.991  -2.364  1.00 30.46 ? 435 HOH   B O   1 
HETATM 4213 O  O   . HOH   H 5 .   ? 16.830  16.135  -9.138  1.00 17.06 ? 436 HOH   B O   1 
HETATM 4214 O  O   . HOH   H 5 .   ? -0.037  -0.748  -8.399  1.00 32.70 ? 437 HOH   B O   1 
HETATM 4215 O  O   . HOH   H 5 .   ? 27.158  10.512  -25.981 1.00 27.93 ? 438 HOH   B O   1 
HETATM 4216 O  O   . HOH   H 5 .   ? 24.351  -4.114  -2.150  1.00 25.90 ? 439 HOH   B O   1 
HETATM 4217 O  O   . HOH   H 5 .   ? 21.122  19.704  -6.928  1.00 22.63 ? 440 HOH   B O   1 
HETATM 4218 O  O   . HOH   H 5 .   ? 0.599   -4.997  -17.421 1.00 28.71 ? 441 HOH   B O   1 
HETATM 4219 O  O   . HOH   H 5 .   ? -0.723  1.076   -4.089  1.00 36.47 ? 442 HOH   B O   1 
HETATM 4220 O  O   . HOH   H 5 .   ? 3.420   16.767  -20.059 1.00 34.31 ? 443 HOH   B O   1 
HETATM 4221 O  O   . HOH   H 5 .   ? 15.443  20.959  -11.644 1.00 18.46 ? 444 HOH   B O   1 
HETATM 4222 O  O   . HOH   H 5 .   ? 12.167  -2.243  -20.206 1.00 42.60 ? 445 HOH   B O   1 
HETATM 4223 O  O   . HOH   H 5 .   ? 0.672   -9.211  -11.733 1.00 31.19 ? 446 HOH   B O   1 
HETATM 4224 O  O   . HOH   H 5 .   ? 9.952   8.043   -33.134 1.00 25.40 ? 447 HOH   B O   1 
HETATM 4225 O  O   . HOH   H 5 .   ? 4.569   0.742   0.958   1.00 31.29 ? 448 HOH   B O   1 
HETATM 4226 O  O   . HOH   H 5 .   ? 5.400   4.901   0.698   1.00 27.70 ? 449 HOH   B O   1 
HETATM 4227 O  O   . HOH   H 5 .   ? 16.715  25.898  -17.311 1.00 28.08 ? 450 HOH   B O   1 
HETATM 4228 O  O   . HOH   H 5 .   ? 20.798  5.722   0.526   1.00 20.19 ? 451 HOH   B O   1 
HETATM 4229 O  O   . HOH   H 5 .   ? 26.890  0.342   -4.172  1.00 27.97 ? 452 HOH   B O   1 
HETATM 4230 O  O   . HOH   H 5 .   ? 35.955  5.644   -24.098 1.00 36.59 ? 453 HOH   B O   1 
HETATM 4231 O  O   . HOH   H 5 .   ? -2.828  0.695   -18.758 1.00 48.35 ? 454 HOH   B O   1 
HETATM 4232 O  O   . HOH   H 5 .   ? 15.070  18.021  -32.611 1.00 37.23 ? 455 HOH   B O   1 
HETATM 4233 O  O   . HOH   H 5 .   ? 28.884  9.090   -24.296 1.00 23.36 ? 456 HOH   B O   1 
HETATM 4234 O  O   . HOH   H 5 .   ? 16.549  4.755   5.182   1.00 23.02 ? 457 HOH   B O   1 
HETATM 4235 O  O   . HOH   H 5 .   ? 11.407  22.588  -19.333 1.00 22.60 ? 458 HOH   B O   1 
HETATM 4236 O  O   . HOH   H 5 .   ? 1.783   6.720   -5.448  1.00 25.73 ? 459 HOH   B O   1 
HETATM 4237 O  O   . HOH   H 5 .   ? 32.726  21.097  -18.046 1.00 31.59 ? 460 HOH   B O   1 
HETATM 4238 O  O   . HOH   H 5 .   ? 31.724  24.112  -7.560  1.00 25.29 ? 461 HOH   B O   1 
HETATM 4239 O  O   . HOH   H 5 .   ? 3.736   13.531  -0.736  1.00 24.73 ? 462 HOH   B O   1 
HETATM 4240 O  O   . HOH   H 5 .   ? 17.289  -15.536 -2.470  1.00 30.05 ? 463 HOH   B O   1 
HETATM 4241 O  O   . HOH   H 5 .   ? 26.547  2.199   0.269   1.00 30.81 ? 464 HOH   B O   1 
HETATM 4242 O  O   . HOH   H 5 .   ? 25.705  12.833  -25.308 1.00 20.16 ? 465 HOH   B O   1 
HETATM 4243 O  O   . HOH   H 5 .   ? 10.857  0.989   -34.512 1.00 34.54 ? 466 HOH   B O   1 
HETATM 4244 O  O   . HOH   H 5 .   ? 23.195  19.331  -27.237 1.00 34.47 ? 467 HOH   B O   1 
HETATM 4245 O  O   . HOH   H 5 .   ? 27.733  18.633  -22.534 1.00 23.12 ? 468 HOH   B O   1 
HETATM 4246 O  O   . HOH   H 5 .   ? 35.458  7.547   -7.444  1.00 39.44 ? 469 HOH   B O   1 
HETATM 4247 O  O   . HOH   H 5 .   ? 7.540   20.813  -26.893 1.00 28.54 ? 470 HOH   B O   1 
HETATM 4248 O  O   . HOH   H 5 .   ? -0.091  9.518   -8.667  1.00 34.17 ? 471 HOH   B O   1 
HETATM 4249 O  O   . HOH   H 5 .   ? 33.764  12.714  -11.461 1.00 22.86 ? 472 HOH   B O   1 
HETATM 4250 O  O   . HOH   H 5 .   ? 39.828  13.270  -15.870 1.00 41.36 ? 473 HOH   B O   1 
HETATM 4251 O  O   . HOH   H 5 .   ? 14.146  22.407  -18.859 1.00 19.14 ? 474 HOH   B O   1 
HETATM 4252 O  O   . HOH   H 5 .   ? 33.414  -2.466  -5.881  1.00 31.09 ? 475 HOH   B O   1 
HETATM 4253 O  O   . HOH   H 5 .   ? 6.886   4.200   -23.482 1.00 19.23 ? 476 HOH   B O   1 
HETATM 4254 O  O   . HOH   H 5 .   ? 23.127  -6.692  -7.579  1.00 28.03 ? 477 HOH   B O   1 
HETATM 4255 O  O   . HOH   H 5 .   ? 26.770  8.554   -3.162  1.00 28.74 ? 478 HOH   B O   1 
HETATM 4256 O  O   . HOH   H 5 .   ? 25.300  25.006  -12.101 1.00 35.69 ? 479 HOH   B O   1 
HETATM 4257 O  O   . HOH   H 5 .   ? 26.638  13.630  1.293   1.00 37.90 ? 480 HOH   B O   1 
HETATM 4258 O  O   . HOH   H 5 .   ? 11.958  22.059  -26.090 1.00 20.90 ? 481 HOH   B O   1 
HETATM 4259 O  O   . HOH   H 5 .   ? 7.769   13.908  -6.206  1.00 21.97 ? 482 HOH   B O   1 
HETATM 4260 O  O   . HOH   H 5 .   ? 0.724   7.074   -10.177 1.00 27.27 ? 483 HOH   B O   1 
HETATM 4261 O  O   . HOH   H 5 .   ? 33.121  0.819   -11.884 1.00 23.18 ? 484 HOH   B O   1 
HETATM 4262 O  O   . HOH   H 5 .   ? -1.244  -1.371  -11.271 1.00 31.70 ? 485 HOH   B O   1 
HETATM 4263 O  O   . HOH   H 5 .   ? 32.039  18.708  -12.902 1.00 30.40 ? 486 HOH   B O   1 
HETATM 4264 O  O   . HOH   H 5 .   ? 25.872  4.780   1.742   1.00 24.70 ? 487 HOH   B O   1 
HETATM 4265 O  O   . HOH   H 5 .   ? 25.504  17.185  -23.010 1.00 22.77 ? 488 HOH   B O   1 
HETATM 4266 O  O   . HOH   H 5 .   ? 35.370  8.291   -17.932 1.00 28.25 ? 489 HOH   B O   1 
HETATM 4267 O  O   . HOH   H 5 .   ? 2.650   -10.674 -8.112  1.00 54.00 ? 490 HOH   B O   1 
HETATM 4268 O  O   . HOH   H 5 .   ? -3.565  5.075   -17.000 1.00 36.53 ? 491 HOH   B O   1 
HETATM 4269 O  O   . HOH   H 5 .   ? 3.146   5.097   -17.101 1.00 25.26 ? 492 HOH   B O   1 
HETATM 4270 O  O   . HOH   H 5 .   ? 7.061   -0.854  -32.713 1.00 31.32 ? 493 HOH   B O   1 
HETATM 4271 O  O   . HOH   H 5 .   ? 3.034   14.129  -19.450 1.00 23.82 ? 494 HOH   B O   1 
HETATM 4272 O  O   . HOH   H 5 .   ? 25.374  -9.988  -6.286  1.00 38.67 ? 495 HOH   B O   1 
HETATM 4273 O  O   . HOH   H 5 .   ? 18.990  13.697  1.545   1.00 31.92 ? 496 HOH   B O   1 
HETATM 4274 O  O   . HOH   H 5 .   ? 35.972  -1.708  -12.814 1.00 28.34 ? 497 HOH   B O   1 
HETATM 4275 O  O   . HOH   H 5 .   ? 5.704   -4.139  -27.414 1.00 48.00 ? 498 HOH   B O   1 
HETATM 4276 O  O   . HOH   H 5 .   ? 22.295  14.445  -27.192 1.00 30.68 ? 499 HOH   B O   1 
HETATM 4277 O  O   . HOH   H 5 .   ? 31.773  16.861  -23.716 1.00 28.24 ? 500 HOH   B O   1 
HETATM 4278 O  O   . HOH   H 5 .   ? 2.867   6.818   -8.370  1.00 27.93 ? 501 HOH   B O   1 
HETATM 4279 O  O   . HOH   H 5 .   ? 12.156  10.575  7.139   1.00 29.94 ? 502 HOH   B O   1 
HETATM 4280 O  O   . HOH   H 5 .   ? 11.940  3.676   -34.841 1.00 23.72 ? 503 HOH   B O   1 
HETATM 4281 O  O   . HOH   H 5 .   ? 34.766  -10.288 -21.084 1.00 34.34 ? 504 HOH   B O   1 
HETATM 4282 O  O   . HOH   H 5 .   ? 30.989  -11.048 -3.338  1.00 39.01 ? 505 HOH   B O   1 
HETATM 4283 O  O   . HOH   H 5 .   ? 20.695  5.135   -37.830 1.00 29.81 ? 506 HOH   B O   1 
HETATM 4284 O  O   . HOH   H 5 .   ? 24.664  -7.182  -5.579  1.00 27.87 ? 507 HOH   B O   1 
HETATM 4285 O  O   . HOH   H 5 .   ? 30.440  1.926   -25.649 1.00 26.25 ? 508 HOH   B O   1 
HETATM 4286 O  O   . HOH   H 5 .   ? 15.170  -2.068  -20.686 1.00 38.61 ? 509 HOH   B O   1 
HETATM 4287 O  O   . HOH   H 5 .   ? 12.752  -1.398  -28.389 1.00 27.82 ? 510 HOH   B O   1 
HETATM 4288 O  O   . HOH   H 5 .   ? 37.351  14.045  -12.885 1.00 30.97 ? 511 HOH   B O   1 
HETATM 4289 O  O   . HOH   H 5 .   ? 8.546   2.342   -33.597 1.00 38.14 ? 512 HOH   B O   1 
HETATM 4290 O  O   . HOH   H 5 .   ? 18.354  -4.141  -36.560 1.00 47.38 ? 513 HOH   B O   1 
HETATM 4291 O  O   . HOH   H 5 .   ? 10.385  18.657  -5.468  1.00 37.56 ? 514 HOH   B O   1 
HETATM 4292 O  O   . HOH   H 5 .   ? 3.034   2.897   -27.126 1.00 49.21 ? 515 HOH   B O   1 
HETATM 4293 O  O   . HOH   H 5 .   ? 28.758  -0.469  -28.580 1.00 41.31 ? 516 HOH   B O   1 
HETATM 4294 O  O   . HOH   H 5 .   ? 37.446  -6.027  -3.353  1.00 42.85 ? 517 HOH   B O   1 
HETATM 4295 O  O   . HOH   H 5 .   ? 21.855  -10.094 -9.288  1.00 24.03 ? 518 HOH   B O   1 
HETATM 4296 O  O   . HOH   H 5 .   ? 26.033  30.310  -24.243 1.00 40.66 ? 519 HOH   B O   1 
HETATM 4297 O  O   . HOH   H 5 .   ? 23.914  25.317  -9.322  1.00 41.36 ? 520 HOH   B O   1 
HETATM 4298 O  O   . HOH   H 5 .   ? 28.474  4.206   -28.421 1.00 41.84 ? 521 HOH   B O   1 
HETATM 4299 O  O   . HOH   H 5 .   ? 23.951  -6.558  -3.032  1.00 31.28 ? 522 HOH   B O   1 
HETATM 4300 O  O   . HOH   H 5 .   ? 36.764  0.643   -13.666 1.00 39.24 ? 523 HOH   B O   1 
HETATM 4301 O  O   . HOH   H 5 .   ? -3.358  -0.203  -11.340 1.00 43.60 ? 524 HOH   B O   1 
HETATM 4302 O  O   . HOH   H 5 .   ? 14.813  -3.556  -28.181 1.00 41.61 ? 525 HOH   B O   1 
HETATM 4303 O  O   . HOH   H 5 .   ? 16.924  25.762  -21.159 1.00 35.70 ? 526 HOH   B O   1 
HETATM 4304 O  O   . HOH   H 5 .   ? 29.064  3.746   -0.007  1.00 44.88 ? 527 HOH   B O   1 
HETATM 4305 O  O   . HOH   H 5 .   ? 1.624   -6.240  -5.040  1.00 40.18 ? 528 HOH   B O   1 
HETATM 4306 O  O   . HOH   H 5 .   ? 2.013   -3.987  0.851   1.00 46.99 ? 529 HOH   B O   1 
HETATM 4307 O  O   . HOH   H 5 .   ? 13.162  19.560  -29.615 1.00 34.68 ? 530 HOH   B O   1 
HETATM 4308 O  O   . HOH   H 5 .   ? 13.166  19.768  -32.356 1.00 37.84 ? 531 HOH   B O   1 
HETATM 4309 O  O   . HOH   H 5 .   ? 4.508   6.561   3.482   1.00 54.88 ? 532 HOH   B O   1 
HETATM 4310 O  O   . HOH   H 5 .   ? 24.136  16.169  -27.170 1.00 30.07 ? 533 HOH   B O   1 
HETATM 4311 O  O   . HOH   H 5 .   ? 32.423  -8.408  -11.986 1.00 34.77 ? 534 HOH   B O   1 
HETATM 4312 O  O   . HOH   H 5 .   ? 30.547  25.314  -5.313  1.00 55.12 ? 535 HOH   B O   1 
HETATM 4313 O  O   . HOH   H 5 .   ? 17.530  3.135   7.375   1.00 49.62 ? 536 HOH   B O   1 
HETATM 4314 O  O   . HOH   H 5 .   ? 11.232  20.192  -27.977 1.00 28.88 ? 537 HOH   B O   1 
HETATM 4315 O  O   . HOH   H 5 .   ? 20.123  29.784  -29.137 1.00 39.80 ? 538 HOH   B O   1 
HETATM 4316 O  O   . HOH   H 5 .   ? -3.559  4.463   -29.996 1.00 46.50 ? 539 HOH   B O   1 
HETATM 4317 O  O   . HOH   H 5 .   ? 9.466   -0.419  -31.531 1.00 42.40 ? 540 HOH   B O   1 
HETATM 4318 O  O   . HOH   H 5 .   ? 14.136  3.991   8.811   1.00 36.25 ? 541 HOH   B O   1 
HETATM 4319 O  O   . HOH   H 5 .   ? 21.455  -4.157  -25.828 1.00 45.07 ? 542 HOH   B O   1 
HETATM 4320 O  O   . HOH   H 5 .   ? 29.537  17.945  -24.478 1.00 30.35 ? 543 HOH   B O   1 
HETATM 4321 O  O   . HOH   H 5 .   ? 42.550  -4.323  -15.140 1.00 46.74 ? 544 HOH   B O   1 
HETATM 4322 O  O   . HOH   H 5 .   ? 20.785  21.345  -28.225 1.00 50.14 ? 545 HOH   B O   1 
HETATM 4323 O  O   . HOH   H 5 .   ? -0.954  3.821   -4.620  1.00 41.02 ? 546 HOH   B O   1 
HETATM 4324 O  O   . HOH   H 5 .   ? 7.070   3.004   4.323   1.00 48.91 ? 547 HOH   B O   1 
HETATM 4325 O  O   . HOH   H 5 .   ? 26.045  15.245  -25.126 1.00 23.76 ? 548 HOH   B O   1 
HETATM 4326 O  O   . HOH   H 5 .   ? 32.619  12.889  -2.634  1.00 36.91 ? 549 HOH   B O   1 
HETATM 4327 O  O   . HOH   H 5 .   ? 5.592   -5.045  -30.149 1.00 30.35 ? 550 HOH   B O   1 
HETATM 4328 O  O   . HOH   H 5 .   ? 32.856  20.452  -15.584 1.00 58.44 ? 551 HOH   B O   1 
HETATM 4329 O  O   . HOH   H 5 .   ? 22.124  21.884  -6.224  1.00 38.68 ? 552 HOH   B O   1 
HETATM 4330 O  O   . HOH   H 5 .   ? 23.795  23.751  -7.003  1.00 32.08 ? 553 HOH   B O   1 
HETATM 4331 O  O   . HOH   H 5 .   ? 28.212  33.984  -7.153  1.00 50.55 ? 554 HOH   B O   1 
HETATM 4332 O  O   . HOH   H 5 .   ? 15.065  25.124  -19.303 1.00 30.25 ? 555 HOH   B O   1 
HETATM 4333 O  O   . HOH   H 5 .   ? 12.417  1.947   8.573   1.00 33.10 ? 556 HOH   B O   1 
HETATM 4334 O  O   . HOH   H 5 .   ? 40.831  -4.844  -6.130  1.00 49.16 ? 557 HOH   B O   1 
HETATM 4335 O  O   . HOH   H 5 .   ? 28.238  16.266  -26.142 1.00 26.73 ? 558 HOH   B O   1 
HETATM 4336 O  O   . HOH   H 5 .   ? 38.988  2.246   -4.892  1.00 44.00 ? 559 HOH   B O   1 
HETATM 4337 O  O   . HOH   I 5 .   ? -14.569 22.822  -39.565 1.00 33.00 ? 401 HOH   A O   1 
HETATM 4338 O  O   . HOH   I 5 .   ? -13.283 25.783  -43.847 1.00 36.02 ? 402 HOH   A O   1 
HETATM 4339 O  O   . HOH   I 5 .   ? 13.091  46.938  -23.776 1.00 32.68 ? 403 HOH   A O   1 
HETATM 4340 O  O   . HOH   I 5 .   ? -14.369 34.548  -8.317  1.00 40.66 ? 404 HOH   A O   1 
HETATM 4341 O  O   . HOH   I 5 .   ? -4.975  23.641  -14.834 1.00 22.96 ? 405 HOH   A O   1 
HETATM 4342 O  O   . HOH   I 5 .   ? -8.498  16.338  -38.090 1.00 35.01 ? 406 HOH   A O   1 
HETATM 4343 O  O   . HOH   I 5 .   ? 15.490  32.699  -23.560 1.00 33.76 ? 407 HOH   A O   1 
HETATM 4344 O  O   . HOH   I 5 .   ? 18.238  35.657  -13.769 1.00 51.70 ? 408 HOH   A O   1 
HETATM 4345 O  O   . HOH   I 5 .   ? 2.492   39.836  -8.057  1.00 32.86 ? 409 HOH   A O   1 
HETATM 4346 O  O   . HOH   I 5 .   ? -4.916  52.211  -19.302 1.00 26.40 ? 410 HOH   A O   1 
HETATM 4347 O  O   . HOH   I 5 .   ? -1.628  54.595  -17.854 1.00 35.48 ? 411 HOH   A O   1 
HETATM 4348 O  O   . HOH   I 5 .   ? -12.867 49.793  -30.513 1.00 29.10 ? 412 HOH   A O   1 
HETATM 4349 O  O   . HOH   I 5 .   ? 2.262   37.053  -7.575  1.00 34.48 ? 413 HOH   A O   1 
HETATM 4350 O  O   . HOH   I 5 .   ? -1.174  28.318  -6.281  1.00 28.05 ? 414 HOH   A O   1 
HETATM 4351 O  O   . HOH   I 5 .   ? -9.736  28.607  -6.071  1.00 25.50 ? 415 HOH   A O   1 
HETATM 4352 O  O   . HOH   I 5 .   ? 1.551   49.599  -33.656 1.00 28.78 ? 416 HOH   A O   1 
HETATM 4353 O  O   . HOH   I 5 .   ? -4.612  53.133  -26.868 1.00 44.43 ? 417 HOH   A O   1 
HETATM 4354 O  O   . HOH   I 5 .   ? 1.451   52.789  -21.608 1.00 26.72 ? 418 HOH   A O   1 
HETATM 4355 O  O   . HOH   I 5 .   ? -6.252  28.340  -44.878 1.00 25.83 ? 419 HOH   A O   1 
HETATM 4356 O  O   . HOH   I 5 .   ? 17.452  36.304  -18.160 1.00 33.75 ? 420 HOH   A O   1 
HETATM 4357 O  O   . HOH   I 5 .   ? -12.489 31.216  -27.076 1.00 35.97 ? 421 HOH   A O   1 
HETATM 4358 O  O   . HOH   I 5 .   ? -3.192  22.740  -12.832 1.00 21.17 ? 422 HOH   A O   1 
HETATM 4359 O  O   . HOH   I 5 .   ? 7.238   32.832  -10.891 1.00 19.91 ? 423 HOH   A O   1 
HETATM 4360 O  O   . HOH   I 5 .   ? -15.228 36.531  -38.199 1.00 27.46 ? 424 HOH   A O   1 
HETATM 4361 O  O   . HOH   I 5 .   ? 10.136  30.649  -39.252 1.00 34.82 ? 425 HOH   A O   1 
HETATM 4362 O  O   . HOH   I 5 .   ? -17.911 37.566  -34.777 1.00 23.44 ? 426 HOH   A O   1 
HETATM 4363 O  O   . HOH   I 5 .   ? 2.576   42.574  -16.570 1.00 25.79 ? 427 HOH   A O   1 
HETATM 4364 O  O   . HOH   I 5 .   ? -17.374 35.979  -32.545 1.00 23.25 ? 428 HOH   A O   1 
HETATM 4365 O  O   . HOH   I 5 .   ? 5.874   31.597  -31.415 1.00 14.39 ? 429 HOH   A O   1 
HETATM 4366 O  O   . HOH   I 5 .   ? -1.283  45.430  -18.000 1.00 24.02 ? 430 HOH   A O   1 
HETATM 4367 O  O   . HOH   I 5 .   ? 14.910  38.613  -32.303 1.00 29.40 ? 431 HOH   A O   1 
HETATM 4368 O  O   . HOH   I 5 .   ? -5.813  51.068  -27.821 1.00 37.20 ? 432 HOH   A O   1 
HETATM 4369 O  O   . HOH   I 5 .   ? -0.563  28.107  -9.962  1.00 21.71 ? 433 HOH   A O   1 
HETATM 4370 O  O   . HOH   I 5 .   ? -5.210  33.214  -41.000 1.00 15.29 ? 434 HOH   A O   1 
HETATM 4371 O  O   . HOH   I 5 .   ? -8.818  16.788  -11.919 1.00 45.40 ? 435 HOH   A O   1 
HETATM 4372 O  O   . HOH   I 5 .   ? -9.203  39.374  -30.334 1.00 18.51 ? 436 HOH   A O   1 
HETATM 4373 O  O   . HOH   I 5 .   ? -13.212 47.020  -19.424 1.00 31.64 ? 437 HOH   A O   1 
HETATM 4374 O  O   . HOH   I 5 .   ? -5.924  30.503  -5.279  1.00 21.49 ? 438 HOH   A O   1 
HETATM 4375 O  O   . HOH   I 5 .   ? 13.558  33.853  -19.066 1.00 24.10 ? 439 HOH   A O   1 
HETATM 4376 O  O   . HOH   I 5 .   ? -26.056 28.993  -36.574 1.00 35.56 ? 440 HOH   A O   1 
HETATM 4377 O  O   . HOH   I 5 .   ? 1.921   23.294  -46.600 1.00 28.95 ? 441 HOH   A O   1 
HETATM 4378 O  O   . HOH   I 5 .   ? -4.596  39.321  -47.435 1.00 40.30 ? 442 HOH   A O   1 
HETATM 4379 O  O   . HOH   I 5 .   ? -4.620  38.625  -2.403  1.00 27.13 ? 443 HOH   A O   1 
HETATM 4380 O  O   . HOH   I 5 .   ? 10.965  30.778  -29.081 1.00 18.92 ? 444 HOH   A O   1 
HETATM 4381 O  O   . HOH   I 5 .   ? -9.836  14.630  -30.899 1.00 30.46 ? 445 HOH   A O   1 
HETATM 4382 O  O   . HOH   I 5 .   ? -13.601 17.827  -37.222 1.00 35.16 ? 446 HOH   A O   1 
HETATM 4383 O  O   . HOH   I 5 .   ? 0.079   39.716  -14.746 1.00 22.53 ? 447 HOH   A O   1 
HETATM 4384 O  O   . HOH   I 5 .   ? 2.669   54.509  -28.813 1.00 25.95 ? 448 HOH   A O   1 
HETATM 4385 O  O   . HOH   I 5 .   ? 10.489  35.148  -12.410 1.00 28.78 ? 449 HOH   A O   1 
HETATM 4386 O  O   . HOH   I 5 .   ? 2.132   48.316  -31.167 1.00 18.71 ? 450 HOH   A O   1 
HETATM 4387 O  O   . HOH   I 5 .   ? 13.428  27.103  -19.357 1.00 37.79 ? 451 HOH   A O   1 
HETATM 4388 O  O   . HOH   I 5 .   ? 8.970   35.637  -34.402 1.00 26.68 ? 452 HOH   A O   1 
HETATM 4389 O  O   . HOH   I 5 .   ? -5.176  18.157  -38.566 1.00 25.33 ? 453 HOH   A O   1 
HETATM 4390 O  O   . HOH   I 5 .   ? -10.991 30.102  -11.731 1.00 24.12 ? 454 HOH   A O   1 
HETATM 4391 O  O   . HOH   I 5 .   ? 6.061   25.592  -13.938 1.00 24.89 ? 455 HOH   A O   1 
HETATM 4392 O  O   . HOH   I 5 .   ? -15.754 16.504  -34.714 1.00 33.69 ? 456 HOH   A O   1 
HETATM 4393 O  O   . HOH   I 5 .   ? 1.964   51.904  -19.230 1.00 25.72 ? 457 HOH   A O   1 
HETATM 4394 O  O   . HOH   I 5 .   ? 3.951   38.335  -11.775 1.00 19.36 ? 458 HOH   A O   1 
HETATM 4395 O  O   . HOH   I 5 .   ? 11.023  24.220  -15.200 1.00 36.58 ? 459 HOH   A O   1 
HETATM 4396 O  O   . HOH   I 5 .   ? -6.466  37.733  -43.029 1.00 32.22 ? 460 HOH   A O   1 
HETATM 4397 O  O   . HOH   I 5 .   ? -2.667  47.443  -15.414 1.00 22.12 ? 461 HOH   A O   1 
HETATM 4398 O  O   . HOH   I 5 .   ? -0.691  12.727  -16.445 1.00 36.06 ? 462 HOH   A O   1 
HETATM 4399 O  O   . HOH   I 5 .   ? -20.744 38.012  -33.938 1.00 28.15 ? 463 HOH   A O   1 
HETATM 4400 O  O   . HOH   I 5 .   ? -3.754  41.330  -35.598 1.00 39.44 ? 464 HOH   A O   1 
HETATM 4401 O  O   . HOH   I 5 .   ? -8.436  12.784  -32.392 1.00 47.70 ? 465 HOH   A O   1 
HETATM 4402 O  O   . HOH   I 5 .   ? -14.153 15.886  -19.389 1.00 28.70 ? 466 HOH   A O   1 
HETATM 4403 O  O   . HOH   I 5 .   ? 1.803   42.307  -41.325 1.00 31.09 ? 467 HOH   A O   1 
HETATM 4404 O  O   . HOH   I 5 .   ? -9.886  19.258  -7.318  1.00 28.35 ? 468 HOH   A O   1 
HETATM 4405 O  O   . HOH   I 5 .   ? -14.480 24.602  -23.176 1.00 29.24 ? 469 HOH   A O   1 
HETATM 4406 O  O   . HOH   I 5 .   ? 6.769   48.880  -19.872 1.00 38.69 ? 470 HOH   A O   1 
HETATM 4407 O  O   . HOH   I 5 .   ? -10.825 39.776  -36.892 1.00 25.62 ? 471 HOH   A O   1 
HETATM 4408 O  O   . HOH   I 5 .   ? -1.343  17.949  -29.225 1.00 36.60 ? 472 HOH   A O   1 
HETATM 4409 O  O   . HOH   I 5 .   ? 7.767   47.312  -30.177 1.00 29.26 ? 473 HOH   A O   1 
HETATM 4410 O  O   . HOH   I 5 .   ? 8.421   44.303  -20.127 1.00 26.65 ? 474 HOH   A O   1 
HETATM 4411 O  O   . HOH   I 5 .   ? -8.314  47.125  -16.948 1.00 23.13 ? 475 HOH   A O   1 
HETATM 4412 O  O   . HOH   I 5 .   ? 19.894  43.076  -18.595 1.00 41.87 ? 476 HOH   A O   1 
HETATM 4413 O  O   . HOH   I 5 .   ? 9.108   22.659  -26.476 1.00 25.14 ? 477 HOH   A O   1 
HETATM 4414 O  O   . HOH   I 5 .   ? 9.722   25.821  -11.551 1.00 47.17 ? 478 HOH   A O   1 
HETATM 4415 O  O   . HOH   I 5 .   ? 0.066   43.983  -16.085 1.00 23.23 ? 479 HOH   A O   1 
HETATM 4416 O  O   . HOH   I 5 .   ? -6.535  49.493  -16.547 1.00 31.05 ? 480 HOH   A O   1 
HETATM 4417 O  O   . HOH   I 5 .   ? -20.687 18.115  -29.182 1.00 41.47 ? 481 HOH   A O   1 
HETATM 4418 O  O   . HOH   I 5 .   ? 12.448  29.485  -12.804 1.00 44.11 ? 482 HOH   A O   1 
HETATM 4419 O  O   . HOH   I 5 .   ? 6.130   48.342  -37.472 1.00 36.29 ? 483 HOH   A O   1 
HETATM 4420 O  O   . HOH   I 5 .   ? 3.494   45.169  -41.931 1.00 38.78 ? 484 HOH   A O   1 
HETATM 4421 O  O   . HOH   I 5 .   ? 13.514  46.059  -35.469 1.00 35.54 ? 485 HOH   A O   1 
HETATM 4422 O  O   . HOH   I 5 .   ? -14.292 37.483  -22.827 1.00 36.46 ? 486 HOH   A O   1 
HETATM 4423 O  O   . HOH   I 5 .   ? -2.431  50.709  -25.541 1.00 19.51 ? 487 HOH   A O   1 
HETATM 4424 O  O   . HOH   I 5 .   ? -20.195 38.097  -27.607 1.00 39.68 ? 488 HOH   A O   1 
HETATM 4425 O  O   . HOH   I 5 .   ? -18.584 35.995  -41.217 1.00 34.64 ? 489 HOH   A O   1 
HETATM 4426 O  O   . HOH   I 5 .   ? 6.772   42.056  -18.952 1.00 19.66 ? 490 HOH   A O   1 
HETATM 4427 O  O   . HOH   I 5 .   ? 0.519   46.648  -15.383 1.00 26.95 ? 491 HOH   A O   1 
HETATM 4428 O  O   . HOH   I 5 .   ? -3.218  10.108  -37.317 1.00 30.64 ? 492 HOH   A O   1 
HETATM 4429 O  O   . HOH   I 5 .   ? -10.099 47.176  -30.958 1.00 27.44 ? 493 HOH   A O   1 
HETATM 4430 O  O   . HOH   I 5 .   ? 3.895   33.821  -4.707  1.00 30.86 ? 494 HOH   A O   1 
HETATM 4431 O  O   . HOH   I 5 .   ? 5.791   22.678  -36.291 1.00 21.20 ? 495 HOH   A O   1 
HETATM 4432 O  O   . HOH   I 5 .   ? 14.522  40.650  -30.054 1.00 28.49 ? 496 HOH   A O   1 
HETATM 4433 O  O   . HOH   I 5 .   ? 9.750   23.723  -17.662 1.00 20.78 ? 497 HOH   A O   1 
HETATM 4434 O  O   . HOH   I 5 .   ? 4.021   22.060  -32.810 1.00 23.42 ? 498 HOH   A O   1 
HETATM 4435 O  O   . HOH   I 5 .   ? 10.446  48.195  -26.286 1.00 33.16 ? 499 HOH   A O   1 
HETATM 4436 O  O   . HOH   I 5 .   ? -1.113  50.137  -33.238 1.00 28.14 ? 500 HOH   A O   1 
HETATM 4437 O  O   . HOH   I 5 .   ? 10.011  27.122  -36.488 1.00 28.60 ? 501 HOH   A O   1 
HETATM 4438 O  O   . HOH   I 5 .   ? -2.699  15.661  -27.481 1.00 27.96 ? 502 HOH   A O   1 
HETATM 4439 O  O   . HOH   I 5 .   ? 1.350   34.376  -42.626 1.00 31.85 ? 503 HOH   A O   1 
HETATM 4440 O  O   . HOH   I 5 .   ? -16.896 22.957  -37.880 1.00 35.81 ? 504 HOH   A O   1 
HETATM 4441 O  O   . HOH   I 5 .   ? -20.605 34.731  -30.602 1.00 34.21 ? 505 HOH   A O   1 
HETATM 4442 O  O   . HOH   I 5 .   ? 8.586   24.870  -33.930 1.00 22.84 ? 506 HOH   A O   1 
HETATM 4443 O  O   . HOH   I 5 .   ? -10.885 45.987  -13.456 1.00 41.62 ? 507 HOH   A O   1 
HETATM 4444 O  O   . HOH   I 5 .   ? -2.151  39.679  -38.593 1.00 24.44 ? 508 HOH   A O   1 
HETATM 4445 O  O   . HOH   I 5 .   ? 15.040  26.262  -31.877 1.00 35.12 ? 509 HOH   A O   1 
HETATM 4446 O  O   . HOH   I 5 .   ? 14.455  28.503  -24.421 1.00 26.13 ? 510 HOH   A O   1 
HETATM 4447 O  O   . HOH   I 5 .   ? 4.362   39.832  -13.953 1.00 27.24 ? 511 HOH   A O   1 
HETATM 4448 O  O   . HOH   I 5 .   ? 5.747   45.052  -36.060 1.00 27.87 ? 512 HOH   A O   1 
HETATM 4449 O  O   . HOH   I 5 .   ? 1.418   18.721  -22.022 1.00 33.66 ? 513 HOH   A O   1 
HETATM 4450 O  O   . HOH   I 5 .   ? 3.405   52.255  -30.699 1.00 31.19 ? 514 HOH   A O   1 
HETATM 4451 O  O   . HOH   I 5 .   ? -2.822  15.649  -31.963 1.00 25.83 ? 515 HOH   A O   1 
HETATM 4452 O  O   . HOH   I 5 .   ? 16.058  34.754  -19.722 1.00 27.33 ? 516 HOH   A O   1 
HETATM 4453 O  O   . HOH   I 5 .   ? -9.041  38.852  -41.568 1.00 37.90 ? 517 HOH   A O   1 
HETATM 4454 O  O   . HOH   I 5 .   ? -0.245  24.709  -46.767 1.00 23.16 ? 518 HOH   A O   1 
HETATM 4455 O  O   . HOH   I 5 .   ? -11.254 28.975  -8.941  1.00 31.71 ? 519 HOH   A O   1 
HETATM 4456 O  O   . HOH   I 5 .   ? 7.219   23.518  -43.661 1.00 38.56 ? 520 HOH   A O   1 
HETATM 4457 O  O   . HOH   I 5 .   ? 6.646   18.520  -41.750 1.00 33.00 ? 521 HOH   A O   1 
HETATM 4458 O  O   . HOH   I 5 .   ? -1.675  12.857  -34.014 1.00 53.40 ? 522 HOH   A O   1 
HETATM 4459 O  O   . HOH   I 5 .   ? -22.790 20.341  -26.473 1.00 27.72 ? 523 HOH   A O   1 
HETATM 4460 O  O   . HOH   I 5 .   ? 0.173   27.185  -48.425 1.00 35.02 ? 524 HOH   A O   1 
HETATM 4461 O  O   . HOH   I 5 .   ? -9.100  54.601  -21.948 1.00 40.95 ? 525 HOH   A O   1 
HETATM 4462 O  O   . HOH   I 5 .   ? -10.571 13.243  -25.452 1.00 36.18 ? 526 HOH   A O   1 
HETATM 4463 O  O   . HOH   I 5 .   ? 2.529   32.236  -42.024 1.00 25.50 ? 527 HOH   A O   1 
HETATM 4464 O  O   . HOH   I 5 .   ? -7.325  17.792  -44.821 1.00 42.18 ? 528 HOH   A O   1 
HETATM 4465 O  O   . HOH   I 5 .   ? -10.419 13.987  -28.199 1.00 33.00 ? 529 HOH   A O   1 
HETATM 4466 O  O   . HOH   I 5 .   ? 20.122  34.103  -25.233 1.00 32.40 ? 530 HOH   A O   1 
HETATM 4467 O  O   . HOH   I 5 .   ? -13.573 46.172  -36.875 1.00 26.33 ? 531 HOH   A O   1 
HETATM 4468 O  O   . HOH   I 5 .   ? 13.829  31.389  -20.186 1.00 38.02 ? 532 HOH   A O   1 
HETATM 4469 O  O   . HOH   I 5 .   ? -2.417  22.722  -47.132 1.00 21.47 ? 533 HOH   A O   1 
HETATM 4470 O  O   . HOH   I 5 .   ? -17.695 36.170  -37.063 1.00 31.03 ? 534 HOH   A O   1 
HETATM 4471 O  O   . HOH   I 5 .   ? 13.375  31.243  -30.599 1.00 28.06 ? 535 HOH   A O   1 
HETATM 4472 O  O   . HOH   I 5 .   ? -8.673  10.994  -24.750 1.00 43.24 ? 536 HOH   A O   1 
HETATM 4473 O  O   . HOH   I 5 .   ? -32.255 29.357  -39.126 1.00 37.61 ? 537 HOH   A O   1 
HETATM 4474 O  O   . HOH   I 5 .   ? -6.674  18.546  -40.650 1.00 46.93 ? 538 HOH   A O   1 
HETATM 4475 O  O   . HOH   I 5 .   ? -19.648 45.810  -30.154 1.00 30.16 ? 539 HOH   A O   1 
HETATM 4476 O  O   . HOH   I 5 .   ? 21.852  43.554  -22.059 1.00 44.39 ? 540 HOH   A O   1 
HETATM 4477 O  O   . HOH   I 5 .   ? 9.503   25.039  -38.098 1.00 39.85 ? 541 HOH   A O   1 
HETATM 4478 O  O   . HOH   I 5 .   ? -17.895 41.165  -22.371 1.00 45.22 ? 542 HOH   A O   1 
HETATM 4479 O  O   . HOH   I 5 .   ? -20.964 30.376  -25.324 1.00 57.12 ? 543 HOH   A O   1 
HETATM 4480 O  O   . HOH   I 5 .   ? -12.268 13.600  -31.783 1.00 42.62 ? 544 HOH   A O   1 
HETATM 4481 O  O   . HOH   I 5 .   ? 5.124   43.182  -17.160 1.00 22.44 ? 545 HOH   A O   1 
HETATM 4482 O  O   . HOH   I 5 .   ? 3.999   24.229  -47.183 1.00 27.66 ? 546 HOH   A O   1 
HETATM 4483 O  O   . HOH   I 5 .   ? 10.406  23.222  -35.104 1.00 37.04 ? 547 HOH   A O   1 
HETATM 4484 O  O   . HOH   I 5 .   ? 10.284  28.766  -11.546 1.00 32.60 ? 548 HOH   A O   1 
HETATM 4485 O  O   . HOH   I 5 .   ? 11.308  36.620  -35.156 1.00 32.11 ? 549 HOH   A O   1 
HETATM 4486 O  O   . HOH   I 5 .   ? 6.935   22.721  -33.660 1.00 36.51 ? 550 HOH   A O   1 
HETATM 4487 O  O   . HOH   I 5 .   ? -10.970 47.953  -17.168 1.00 30.49 ? 551 HOH   A O   1 
HETATM 4488 O  O   . HOH   I 5 .   ? -20.538 43.701  -43.736 1.00 56.29 ? 552 HOH   A O   1 
HETATM 4489 O  O   . HOH   I 5 .   ? 12.879  47.697  -20.106 1.00 37.51 ? 553 HOH   A O   1 
# 
