data_7KJR
# 
_entry.id   7KJR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.337 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   7KJR         
WWPDB D_1000252579 
EMDB  EMD-22898    
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  'Cryo-EM structure of SARS-CoV-2 ORF3a' 6XDC      unspecified            
EMDB 'Cryo-EM structure of SARS-CoV-2 ORF3a' EMD-22898 'associated EM volume' 
EMDB 'Cryo-EM structure of SARS-CoV-2 ORF3a' EMD-22136 'other EM volume'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7KJR 
_pdbx_database_status.recvd_initial_deposition_date   2020-10-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kern, D.M.'    1 0000-0001-8529-9045 
'Hoel, C.M.'    2 0000-0002-1344-0780 
'Kotecha, A.'   3 0000-0002-4480-5439 
'Brohawn, S.G.' 4 0000-0001-6768-3406 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cryo-EM structure of the SARS-CoV-2 3a ion channel in lipid nanodiscs.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2020.06.17.156554 
_citation.pdbx_database_id_PubMed   32587976 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kern, D.M.'    1 0000-0001-8529-9045 
primary 'Sorum, B.'     2 0000-0001-6742-1094 
primary 'Hoel, C.M.'    3 0000-0002-1344-0780 
primary 'Sridharan, S.' 4 ?                   
primary 'Remis, J.P.'   5 ?                   
primary 'Toso, D.B.'    6 ?                   
primary 'Brohawn, S.G.' 7 0000-0001-6768-3406 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7KJR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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             ? 
# 
_symmetry.entry_id                         7KJR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'ORF3a protein'                               32165.902 2   ? ? ?                     ? 
2 polymer     man 'Apolipoprotein A-I'                          24647.678 2   ? ? 'UNP residues 79-267' ? 
3 non-polymer syn 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine 749.073   2   ? ? ?                     ? 
4 water       nat water                                         18.015    122 ? ? ?                     ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Accessory protein 3a,Protein U274,Protein X1,ORF3a,Protein 3a' 
2 'ApoA-I,Apolipoprotein A1,MSPE3D1'                              
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFV
CNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPY
NSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEP
EEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPLSNSLEVLFQ
;
;MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFV
CNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPY
NSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEP
EEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPLSNSLEVLFQ
;
A,B ? 
2 'polypeptide(L)' no no 
;HHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEME
LYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYH
AKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
;
;HHHHHHHDYDIPTTENLYFQGSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEME
LYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYH
AKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
;
C,D ? 
# 
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   ASP n 
1 3   LEU n 
1 4   PHE n 
1 5   MET n 
1 6   ARG n 
1 7   ILE n 
1 8   PHE n 
1 9   THR n 
1 10  ILE n 
1 11  GLY n 
1 12  THR n 
1 13  VAL n 
1 14  THR n 
1 15  LEU n 
1 16  LYS n 
1 17  GLN n 
1 18  GLY n 
1 19  GLU n 
1 20  ILE n 
1 21  LYS n 
1 22  ASP n 
1 23  ALA n 
1 24  THR n 
1 25  PRO n 
1 26  SER n 
1 27  ASP n 
1 28  PHE n 
1 29  VAL n 
1 30  ARG n 
1 31  ALA n 
1 32  THR n 
1 33  ALA n 
1 34  THR n 
1 35  ILE n 
1 36  PRO n 
1 37  ILE n 
1 38  GLN n 
1 39  ALA n 
1 40  SER n 
1 41  LEU n 
1 42  PRO n 
1 43  PHE n 
1 44  GLY n 
1 45  TRP n 
1 46  LEU n 
1 47  ILE n 
1 48  VAL n 
1 49  GLY n 
1 50  VAL n 
1 51  ALA n 
1 52  LEU n 
1 53  LEU n 
1 54  ALA n 
1 55  VAL n 
1 56  PHE n 
1 57  GLN n 
1 58  SER n 
1 59  ALA n 
1 60  SER n 
1 61  LYS n 
1 62  ILE n 
1 63  ILE n 
1 64  THR n 
1 65  LEU n 
1 66  LYS n 
1 67  LYS n 
1 68  ARG n 
1 69  TRP n 
1 70  GLN n 
1 71  LEU n 
1 72  ALA n 
1 73  LEU n 
1 74  SER n 
1 75  LYS n 
1 76  GLY n 
1 77  VAL n 
1 78  HIS n 
1 79  PHE n 
1 80  VAL n 
1 81  CYS n 
1 82  ASN n 
1 83  LEU n 
1 84  LEU n 
1 85  LEU n 
1 86  LEU n 
1 87  PHE n 
1 88  VAL n 
1 89  THR n 
1 90  VAL n 
1 91  TYR n 
1 92  SER n 
1 93  HIS n 
1 94  LEU n 
1 95  LEU n 
1 96  LEU n 
1 97  VAL n 
1 98  ALA n 
1 99  ALA n 
1 100 GLY n 
1 101 LEU n 
1 102 GLU n 
1 103 ALA n 
1 104 PRO n 
1 105 PHE n 
1 106 LEU n 
1 107 TYR n 
1 108 LEU n 
1 109 TYR n 
1 110 ALA n 
1 111 LEU n 
1 112 VAL n 
1 113 TYR n 
1 114 PHE n 
1 115 LEU n 
1 116 GLN n 
1 117 SER n 
1 118 ILE n 
1 119 ASN n 
1 120 PHE n 
1 121 VAL n 
1 122 ARG n 
1 123 ILE n 
1 124 ILE n 
1 125 MET n 
1 126 ARG n 
1 127 LEU n 
1 128 TRP n 
1 129 LEU n 
1 130 CYS n 
1 131 TRP n 
1 132 LYS n 
1 133 CYS n 
1 134 ARG n 
1 135 SER n 
1 136 LYS n 
1 137 ASN n 
1 138 PRO n 
1 139 LEU n 
1 140 LEU n 
1 141 TYR n 
1 142 ASP n 
1 143 ALA n 
1 144 ASN n 
1 145 TYR n 
1 146 PHE n 
1 147 LEU n 
1 148 CYS n 
1 149 TRP n 
1 150 HIS n 
1 151 THR n 
1 152 ASN n 
1 153 CYS n 
1 154 TYR n 
1 155 ASP n 
1 156 TYR n 
1 157 CYS n 
1 158 ILE n 
1 159 PRO n 
1 160 TYR n 
1 161 ASN n 
1 162 SER n 
1 163 VAL n 
1 164 THR n 
1 165 SER n 
1 166 SER n 
1 167 ILE n 
1 168 VAL n 
1 169 ILE n 
1 170 THR n 
1 171 SER n 
1 172 GLY n 
1 173 ASP n 
1 174 GLY n 
1 175 THR n 
1 176 THR n 
1 177 SER n 
1 178 PRO n 
1 179 ILE n 
1 180 SER n 
1 181 GLU n 
1 182 HIS n 
1 183 ASP n 
1 184 TYR n 
1 185 GLN n 
1 186 ILE n 
1 187 GLY n 
1 188 GLY n 
1 189 TYR n 
1 190 THR n 
1 191 GLU n 
1 192 LYS n 
1 193 TRP n 
1 194 GLU n 
1 195 SER n 
1 196 GLY n 
1 197 VAL n 
1 198 LYS n 
1 199 ASP n 
1 200 CYS n 
1 201 VAL n 
1 202 VAL n 
1 203 LEU n 
1 204 HIS n 
1 205 SER n 
1 206 TYR n 
1 207 PHE n 
1 208 THR n 
1 209 SER n 
1 210 ASP n 
1 211 TYR n 
1 212 TYR n 
1 213 GLN n 
1 214 LEU n 
1 215 TYR n 
1 216 SER n 
1 217 THR n 
1 218 GLN n 
1 219 LEU n 
1 220 SER n 
1 221 THR n 
1 222 ASP n 
1 223 THR n 
1 224 GLY n 
1 225 VAL n 
1 226 GLU n 
1 227 HIS n 
1 228 VAL n 
1 229 THR n 
1 230 PHE n 
1 231 PHE n 
1 232 ILE n 
1 233 TYR n 
1 234 ASN n 
1 235 LYS n 
1 236 ILE n 
1 237 VAL n 
1 238 ASP n 
1 239 GLU n 
1 240 PRO n 
1 241 GLU n 
1 242 GLU n 
1 243 HIS n 
1 244 VAL n 
1 245 GLN n 
1 246 ILE n 
1 247 HIS n 
1 248 THR n 
1 249 ILE n 
1 250 ASP n 
1 251 GLY n 
1 252 SER n 
1 253 SER n 
1 254 GLY n 
1 255 VAL n 
1 256 VAL n 
1 257 ASN n 
1 258 PRO n 
1 259 VAL n 
1 260 MET n 
1 261 GLU n 
1 262 PRO n 
1 263 ILE n 
1 264 TYR n 
1 265 ASP n 
1 266 GLU n 
1 267 PRO n 
1 268 THR n 
1 269 THR n 
1 270 THR n 
1 271 THR n 
1 272 SER n 
1 273 VAL n 
1 274 PRO n 
1 275 LEU n 
1 276 SER n 
1 277 ASN n 
1 278 SER n 
1 279 LEU n 
1 280 GLU n 
1 281 VAL n 
1 282 LEU n 
1 283 PHE n 
1 284 GLN n 
2 1   HIS n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   ASP n 
2 9   TYR n 
2 10  ASP n 
2 11  ILE n 
2 12  PRO n 
2 13  THR n 
2 14  THR n 
2 15  GLU n 
2 16  ASN n 
2 17  LEU n 
2 18  TYR n 
2 19  PHE n 
2 20  GLN n 
2 21  GLY n 
2 22  SER n 
2 23  THR n 
2 24  PHE n 
2 25  SER n 
2 26  LYS n 
2 27  LEU n 
2 28  ARG n 
2 29  GLU n 
2 30  GLN n 
2 31  LEU n 
2 32  GLY n 
2 33  PRO n 
2 34  VAL n 
2 35  THR n 
2 36  GLN n 
2 37  GLU n 
2 38  PHE n 
2 39  TRP n 
2 40  ASP n 
2 41  ASN n 
2 42  LEU n 
2 43  GLU n 
2 44  LYS n 
2 45  GLU n 
2 46  THR n 
2 47  GLU n 
2 48  GLY n 
2 49  LEU n 
2 50  ARG n 
2 51  GLN n 
2 52  GLU n 
2 53  MET n 
2 54  SER n 
2 55  LYS n 
2 56  ASP n 
2 57  LEU n 
2 58  GLU n 
2 59  GLU n 
2 60  VAL n 
2 61  LYS n 
2 62  ALA n 
2 63  LYS n 
2 64  VAL n 
2 65  GLN n 
2 66  PRO n 
2 67  TYR n 
2 68  LEU n 
2 69  ASP n 
2 70  ASP n 
2 71  PHE n 
2 72  GLN n 
2 73  LYS n 
2 74  LYS n 
2 75  TRP n 
2 76  GLN n 
2 77  GLU n 
2 78  GLU n 
2 79  MET n 
2 80  GLU n 
2 81  LEU n 
2 82  TYR n 
2 83  ARG n 
2 84  GLN n 
2 85  LYS n 
2 86  VAL n 
2 87  GLU n 
2 88  PRO n 
2 89  LEU n 
2 90  ARG n 
2 91  ALA n 
2 92  GLU n 
2 93  LEU n 
2 94  GLN n 
2 95  GLU n 
2 96  GLY n 
2 97  ALA n 
2 98  ARG n 
2 99  GLN n 
2 100 LYS n 
2 101 LEU n 
2 102 HIS n 
2 103 GLU n 
2 104 LEU n 
2 105 GLN n 
2 106 GLU n 
2 107 LYS n 
2 108 LEU n 
2 109 SER n 
2 110 PRO n 
2 111 LEU n 
2 112 GLY n 
2 113 GLU n 
2 114 GLU n 
2 115 MET n 
2 116 ARG n 
2 117 ASP n 
2 118 ARG n 
2 119 ALA n 
2 120 ARG n 
2 121 ALA n 
2 122 HIS n 
2 123 VAL n 
2 124 ASP n 
2 125 ALA n 
2 126 LEU n 
2 127 ARG n 
2 128 THR n 
2 129 HIS n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 TYR n 
2 134 SER n 
2 135 ASP n 
2 136 GLU n 
2 137 LEU n 
2 138 ARG n 
2 139 GLN n 
2 140 ARG n 
2 141 LEU n 
2 142 ALA n 
2 143 ALA n 
2 144 ARG n 
2 145 LEU n 
2 146 GLU n 
2 147 ALA n 
2 148 LEU n 
2 149 LYS n 
2 150 GLU n 
2 151 ASN n 
2 152 GLY n 
2 153 GLY n 
2 154 ALA n 
2 155 ARG n 
2 156 LEU n 
2 157 ALA n 
2 158 GLU n 
2 159 TYR n 
2 160 HIS n 
2 161 ALA n 
2 162 LYS n 
2 163 ALA n 
2 164 THR n 
2 165 GLU n 
2 166 HIS n 
2 167 LEU n 
2 168 SER n 
2 169 THR n 
2 170 LEU n 
2 171 SER n 
2 172 GLU n 
2 173 LYS n 
2 174 ALA n 
2 175 LYS n 
2 176 PRO n 
2 177 ALA n 
2 178 LEU n 
2 179 GLU n 
2 180 ASP n 
2 181 LEU n 
2 182 ARG n 
2 183 GLN n 
2 184 GLY n 
2 185 LEU n 
2 186 LEU n 
2 187 PRO n 
2 188 VAL n 
2 189 LEU n 
2 190 GLU n 
2 191 SER n 
2 192 PHE n 
2 193 LYS n 
2 194 VAL n 
2 195 SER n 
2 196 PHE n 
2 197 LEU n 
2 198 SER n 
2 199 ALA n 
2 200 LEU n 
2 201 GLU n 
2 202 GLU n 
2 203 TYR n 
2 204 THR n 
2 205 LYS n 
2 206 LYS n 
2 207 LEU n 
2 208 ASN n 
2 209 THR n 
2 210 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 284 2019-nCoV ? 3a    ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? 
? ? ? ? ? 'fall armyworm' 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 210 Human     ? APOA1 ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? 
? ? ? ? ? ?               'Escherichia coli'      562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP AP3A_SARS2  P0DTC3 ? 1 
;MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFV
CNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPY
NSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEP
EEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL
;
1  
2 UNP APOA1_HUMAN P02647 ? 2 
;STFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKL
HELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDL
RQGLLPVLESFKVSFLSALEEYTKKLNTQ
;
79 
# 
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 7KJR A 1  ? 275 ? P0DTC3 1  ? 275 ? 1  275 
2 1 7KJR B 1  ? 275 ? P0DTC3 1  ? 275 ? 1  275 
3 2 7KJR C 22 ? 210 ? P02647 79 ? 267 ? 23 211 
4 2 7KJR D 22 ? 210 ? P02647 79 ? 267 ? 23 211 
# 
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 7KJR SER A 276 ? UNP P0DTC3 ? ? 'expression tag' 276 1  
1 7KJR ASN A 277 ? UNP P0DTC3 ? ? 'expression tag' 277 2  
1 7KJR SER A 278 ? UNP P0DTC3 ? ? 'expression tag' 278 3  
1 7KJR LEU A 279 ? UNP P0DTC3 ? ? 'expression tag' 279 4  
1 7KJR GLU A 280 ? UNP P0DTC3 ? ? 'expression tag' 280 5  
1 7KJR VAL A 281 ? UNP P0DTC3 ? ? 'expression tag' 281 6  
1 7KJR LEU A 282 ? UNP P0DTC3 ? ? 'expression tag' 282 7  
1 7KJR PHE A 283 ? UNP P0DTC3 ? ? 'expression tag' 283 8  
1 7KJR GLN A 284 ? UNP P0DTC3 ? ? 'expression tag' 284 9  
2 7KJR SER B 276 ? UNP P0DTC3 ? ? 'expression tag' 276 10 
2 7KJR ASN B 277 ? UNP P0DTC3 ? ? 'expression tag' 277 11 
2 7KJR SER B 278 ? UNP P0DTC3 ? ? 'expression tag' 278 12 
2 7KJR LEU B 279 ? UNP P0DTC3 ? ? 'expression tag' 279 13 
2 7KJR GLU B 280 ? UNP P0DTC3 ? ? 'expression tag' 280 14 
2 7KJR VAL B 281 ? UNP P0DTC3 ? ? 'expression tag' 281 15 
2 7KJR LEU B 282 ? UNP P0DTC3 ? ? 'expression tag' 282 16 
2 7KJR PHE B 283 ? UNP P0DTC3 ? ? 'expression tag' 283 17 
2 7KJR GLN B 284 ? UNP P0DTC3 ? ? 'expression tag' 284 18 
3 7KJR HIS C 1   ? UNP P02647 ? ? 'expression tag' 2   19 
3 7KJR HIS C 2   ? UNP P02647 ? ? 'expression tag' 3   20 
3 7KJR HIS C 3   ? UNP P02647 ? ? 'expression tag' 4   21 
3 7KJR HIS C 4   ? UNP P02647 ? ? 'expression tag' 5   22 
3 7KJR HIS C 5   ? UNP P02647 ? ? 'expression tag' 6   23 
3 7KJR HIS C 6   ? UNP P02647 ? ? 'expression tag' 7   24 
3 7KJR HIS C 7   ? UNP P02647 ? ? 'expression tag' 8   25 
3 7KJR ASP C 8   ? UNP P02647 ? ? 'expression tag' 9   26 
3 7KJR TYR C 9   ? UNP P02647 ? ? 'expression tag' 10  27 
3 7KJR ASP C 10  ? UNP P02647 ? ? 'expression tag' 11  28 
3 7KJR ILE C 11  ? UNP P02647 ? ? 'expression tag' 12  29 
3 7KJR PRO C 12  ? UNP P02647 ? ? 'expression tag' 13  30 
3 7KJR THR C 13  ? UNP P02647 ? ? 'expression tag' 14  31 
3 7KJR THR C 14  ? UNP P02647 ? ? 'expression tag' 15  32 
3 7KJR GLU C 15  ? UNP P02647 ? ? 'expression tag' 16  33 
3 7KJR ASN C 16  ? UNP P02647 ? ? 'expression tag' 17  34 
3 7KJR LEU C 17  ? UNP P02647 ? ? 'expression tag' 18  35 
3 7KJR TYR C 18  ? UNP P02647 ? ? 'expression tag' 19  36 
3 7KJR PHE C 19  ? UNP P02647 ? ? 'expression tag' 20  37 
3 7KJR GLN C 20  ? UNP P02647 ? ? 'expression tag' 21  38 
3 7KJR GLY C 21  ? UNP P02647 ? ? 'expression tag' 22  39 
4 7KJR HIS D 1   ? UNP P02647 ? ? 'expression tag' 2   40 
4 7KJR HIS D 2   ? UNP P02647 ? ? 'expression tag' 3   41 
4 7KJR HIS D 3   ? UNP P02647 ? ? 'expression tag' 4   42 
4 7KJR HIS D 4   ? UNP P02647 ? ? 'expression tag' 5   43 
4 7KJR HIS D 5   ? UNP P02647 ? ? 'expression tag' 6   44 
4 7KJR HIS D 6   ? UNP P02647 ? ? 'expression tag' 7   45 
4 7KJR HIS D 7   ? UNP P02647 ? ? 'expression tag' 8   46 
4 7KJR ASP D 8   ? UNP P02647 ? ? 'expression tag' 9   47 
4 7KJR TYR D 9   ? UNP P02647 ? ? 'expression tag' 10  48 
4 7KJR ASP D 10  ? UNP P02647 ? ? 'expression tag' 11  49 
4 7KJR ILE D 11  ? UNP P02647 ? ? 'expression tag' 12  50 
4 7KJR PRO D 12  ? UNP P02647 ? ? 'expression tag' 13  51 
4 7KJR THR D 13  ? UNP P02647 ? ? 'expression tag' 14  52 
4 7KJR THR D 14  ? UNP P02647 ? ? 'expression tag' 15  53 
4 7KJR GLU D 15  ? UNP P02647 ? ? 'expression tag' 16  54 
4 7KJR ASN D 16  ? UNP P02647 ? ? 'expression tag' 17  55 
4 7KJR LEU D 17  ? UNP P02647 ? ? 'expression tag' 18  56 
4 7KJR TYR D 18  ? UNP P02647 ? ? 'expression tag' 19  57 
4 7KJR PHE D 19  ? UNP P02647 ? ? 'expression tag' 20  58 
4 7KJR GLN D 20  ? UNP P02647 ? ? 'expression tag' 21  59 
4 7KJR GLY D 21  ? UNP P02647 ? ? 'expression tag' 22  60 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                      ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ?    'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                      ?    'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                                     ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                       ?    'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                     ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                         ?    'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                    ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                       ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                        ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                    ?    'C5 H11 N O2 S'    149.211 
PEE non-polymer         . 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine DOPE 'C41 H83 N O8 P 1' 749.073 
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 
# 
_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                   7KJR 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.33 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7KJR 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_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                            . 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                           ? 
_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                    ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.0053 ? 3818 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.7083 ? 5186 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 0.0464 ? 576  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.0049 ? 626  ? f_plane_restr      ? ? 
'ELECTRON MICROSCOPY' ? 8.6355 ? 502  ? f_dihedral_angle_d ? ? 
# 
_struct.entry_id                     7KJR 
_struct.title                        'Cryo-EM structure of SARS-CoV-2 ORF3a' 
_struct.pdbx_descriptor              'Protein 3a, Apolipoprotein A-I' 
_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        7KJR 
_struct_keywords.text            'SARS-CoV-2, coronavirus, transport protein, viral protein, viroporin, membrane protein' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
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 PHE A 43  ? LYS A 61  ? PHE A 43  LYS A 61  1 ? 19 
HELX_P HELX_P2  AA2 LYS A 67  ? GLY A 100 ? LYS A 67  GLY A 100 1 ? 34 
HELX_P HELX_P3  AA3 GLU A 102 ? PRO A 104 ? GLU A 102 PRO A 104 5 ? 3  
HELX_P HELX_P4  AA4 PHE A 105 ? ARG A 134 ? PHE A 105 ARG A 134 1 ? 30 
HELX_P HELX_P5  AA5 LYS A 136 ? TYR A 141 ? LYS A 136 TYR A 141 1 ? 6  
HELX_P HELX_P6  AA6 LEU A 219 ? GLY A 224 ? LEU A 219 GLY A 224 1 ? 6  
HELX_P HELX_P7  AA7 PHE B 43  ? LYS B 61  ? PHE B 43  LYS B 61  1 ? 19 
HELX_P HELX_P8  AA8 LYS B 67  ? GLY B 100 ? LYS B 67  GLY B 100 1 ? 34 
HELX_P HELX_P9  AA9 GLU B 102 ? PRO B 104 ? GLU B 102 PRO B 104 5 ? 3  
HELX_P HELX_P10 AB1 PHE B 105 ? ARG B 134 ? PHE B 105 ARG B 134 1 ? 30 
HELX_P HELX_P11 AB2 LYS B 136 ? TYR B 141 ? LYS B 136 TYR B 141 1 ? 6  
HELX_P HELX_P12 AB3 LEU B 219 ? GLY B 224 ? LEU B 219 GLY B 224 1 ? 6  
HELX_P HELX_P13 AB4 SER C 25  ? SER C 54  ? SER C 26  SER C 55  1 ? 30 
HELX_P HELX_P14 AB5 SER D 25  ? THR D 46  ? SER D 26  THR D 47  1 ? 22 
HELX_P HELX_P15 AB6 THR D 46  ? SER D 54  ? THR D 47  SER D 55  1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 155 ? TYR A 160 ? ASP A 155 TYR A 160 
AA1 2 TYR A 145 ? HIS A 150 ? TYR A 145 HIS A 150 
AA1 3 CYS A 200 ? HIS A 204 ? CYS A 200 HIS A 204 
AA1 4 SER A 209 ? GLN A 218 ? SER A 209 GLN A 218 
AA1 5 VAL A 228 ? LYS A 235 ? VAL A 228 LYS A 235 
AA1 6 SER A 166 ? GLY A 172 ? SER A 166 GLY A 172 
AA1 7 ASP A 183 ? ILE A 186 ? ASP A 183 ILE A 186 
AA1 8 TYR A 189 ? LYS A 192 ? TYR A 189 LYS A 192 
AA2 1 ASP B 155 ? TYR B 160 ? ASP B 155 TYR B 160 
AA2 2 TYR B 145 ? HIS B 150 ? TYR B 145 HIS B 150 
AA2 3 CYS B 200 ? HIS B 204 ? CYS B 200 HIS B 204 
AA2 4 SER B 209 ? GLN B 218 ? SER B 209 GLN B 218 
AA2 5 VAL B 228 ? LYS B 235 ? VAL B 228 LYS B 235 
AA2 6 SER B 166 ? GLY B 172 ? SER B 166 GLY B 172 
AA2 7 ASP B 183 ? ILE B 186 ? ASP B 183 ILE B 186 
AA2 8 TYR B 189 ? LYS B 192 ? TYR B 189 LYS B 192 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 158 ? O ILE A 158 N LEU A 147 ? N LEU A 147 
AA1 2 3 N CYS A 148 ? N CYS A 148 O VAL A 202 ? O VAL A 202 
AA1 3 4 N LEU A 203 ? N LEU A 203 O ASP A 210 ? O ASP A 210 
AA1 4 5 N GLN A 218 ? N GLN A 218 O PHE A 230 ? O PHE A 230 
AA1 5 6 O PHE A 231 ? O PHE A 231 N ILE A 169 ? N ILE A 169 
AA1 6 7 N THR A 170 ? N THR A 170 O GLN A 185 ? O GLN A 185 
AA1 7 8 N TYR A 184 ? N TYR A 184 O GLU A 191 ? O GLU A 191 
AA2 1 2 O ILE B 158 ? O ILE B 158 N LEU B 147 ? N LEU B 147 
AA2 2 3 N CYS B 148 ? N CYS B 148 O VAL B 202 ? O VAL B 202 
AA2 3 4 N LEU B 203 ? N LEU B 203 O ASP B 210 ? O ASP B 210 
AA2 4 5 N GLN B 218 ? N GLN B 218 O PHE B 230 ? O PHE B 230 
AA2 5 6 O PHE B 231 ? O PHE B 231 N ILE B 169 ? N ILE B 169 
AA2 6 7 N THR B 170 ? N THR B 170 O GLN B 185 ? O GLN B 185 
AA2 7 8 N TYR B 184 ? N TYR B 184 O GLU B 191 ? O GLU B 191 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A PEE 301 ? 9 'binding site for residue PEE A 301' 
AC2 Software B PEE 301 ? 9 'binding site for residue PEE B 301' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 9 LYS A 61  ? LYS A 61  . ? 1_555 ? 
2  AC1 9 ILE A 62  ? ILE A 62  . ? 1_555 ? 
3  AC1 9 ILE A 63  ? ILE A 63  . ? 1_555 ? 
4  AC1 9 THR A 64  ? THR A 64  . ? 1_555 ? 
5  AC1 9 HOH G .   ? HOH A 402 . ? 1_555 ? 
6  AC1 9 ARG B 122 ? ARG B 122 . ? 1_555 ? 
7  AC1 9 TYR B 206 ? TYR B 206 . ? 1_555 ? 
8  AC1 9 THR C 35  ? THR C 36  . ? 1_555 ? 
9  AC1 9 TRP C 39  ? TRP C 40  . ? 1_555 ? 
10 AC2 9 ARG A 122 ? ARG A 122 . ? 1_555 ? 
11 AC2 9 TYR A 206 ? TYR A 206 . ? 1_555 ? 
12 AC2 9 LYS B 61  ? LYS B 61  . ? 1_555 ? 
13 AC2 9 ILE B 62  ? ILE B 62  . ? 1_555 ? 
14 AC2 9 ILE B 63  ? ILE B 63  . ? 1_555 ? 
15 AC2 9 THR B 64  ? THR B 64  . ? 1_555 ? 
16 AC2 9 HOH H .   ? HOH B 404 . ? 1_555 ? 
17 AC2 9 THR D 35  ? THR D 36  . ? 1_555 ? 
18 AC2 9 TRP D 39  ? TRP D 40  . ? 1_555 ? 
# 
_atom_sites.entry_id                    7KJR 
_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.fract_transf_matrix[1][1]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 40  ? 121.48700 105.33800 74.45500  1.000 57.61869 ? 40  SER A N   1 
ATOM   2    C CA  . SER A 1 40  ? 120.33400 106.06000 74.97900  1.000 57.61869 ? 40  SER A CA  1 
ATOM   3    C C   . SER A 1 40  ? 119.83100 105.43200 76.27100  1.000 57.61869 ? 40  SER A C   1 
ATOM   4    O O   . SER A 1 40  ? 120.02900 104.24200 76.51600  1.000 57.61869 ? 40  SER A O   1 
ATOM   5    C CB  . SER A 1 40  ? 119.20800 106.09900 73.94600  1.000 57.61869 ? 40  SER A CB  1 
ATOM   6    O OG  . SER A 1 40  ? 119.59300 106.83800 72.80100  1.000 57.61869 ? 40  SER A OG  1 
ATOM   7    N N   . LEU A 1 41  ? 119.17800 106.24500 77.09500  1.000 50.63587 ? 41  LEU A N   1 
ATOM   8    C CA  . LEU A 1 41  ? 118.57400 105.79400 78.34200  1.000 50.63587 ? 41  LEU A CA  1 
ATOM   9    C C   . LEU A 1 41  ? 117.07100 105.67900 78.13600  1.000 50.63587 ? 41  LEU A C   1 
ATOM   10   O O   . LEU A 1 41  ? 116.40500 106.70200 77.91000  1.000 50.63587 ? 41  LEU A O   1 
ATOM   11   C CB  . LEU A 1 41  ? 118.88900 106.76000 79.48500  1.000 50.63587 ? 41  LEU A CB  1 
ATOM   12   C CG  . LEU A 1 41  ? 120.09900 106.46200 80.37100  1.000 50.63587 ? 41  LEU A CG  1 
ATOM   13   C CD1 . LEU A 1 41  ? 121.38500 106.45700 79.57700  1.000 50.63587 ? 41  LEU A CD1 1 
ATOM   14   C CD2 . LEU A 1 41  ? 120.17500 107.49100 81.47800  1.000 50.63587 ? 41  LEU A CD2 1 
ATOM   15   N N   . PRO A 1 42  ? 116.50100 104.47900 78.17500  1.000 47.90362 ? 42  PRO A N   1 
ATOM   16   C CA  . PRO A 1 42  ? 115.06200 104.33600 77.93700  1.000 47.90362 ? 42  PRO A CA  1 
ATOM   17   C C   . PRO A 1 42  ? 114.23100 104.93000 79.06400  1.000 47.90362 ? 42  PRO A C   1 
ATOM   18   O O   . PRO A 1 42  ? 114.62500 104.95400 80.23100  1.000 47.90362 ? 42  PRO A O   1 
ATOM   19   C CB  . PRO A 1 42  ? 114.86200 102.82000 77.84000  1.000 47.90362 ? 42  PRO A CB  1 
ATOM   20   C CG  . PRO A 1 42  ? 116.03500 102.23100 78.51600  1.000 47.90362 ? 42  PRO A CG  1 
ATOM   21   C CD  . PRO A 1 42  ? 117.16900 103.18700 78.38900  1.000 47.90362 ? 42  PRO A CD  1 
ATOM   22   N N   . PHE A 1 43  ? 113.04800 105.41400 78.68400  1.000 47.52460 ? 43  PHE A N   1 
ATOM   23   C CA  . PHE A 1 43  ? 112.14900 106.06300 79.63000  1.000 47.52460 ? 43  PHE A CA  1 
ATOM   24   C C   . PHE A 1 43  ? 111.49800 105.06600 80.58100  1.000 47.52460 ? 43  PHE A C   1 
ATOM   25   O O   . PHE A 1 43  ? 111.02500 105.46700 81.64600  1.000 47.52460 ? 43  PHE A O   1 
ATOM   26   C CB  . PHE A 1 43  ? 111.05000 106.83700 78.88900  1.000 47.52460 ? 43  PHE A CB  1 
ATOM   27   C CG  . PHE A 1 43  ? 111.52000 108.10100 78.18900  1.000 47.52460 ? 43  PHE A CG  1 
ATOM   28   C CD1 . PHE A 1 43  ? 112.86200 108.35400 77.95100  1.000 47.52460 ? 43  PHE A CD1 1 
ATOM   29   C CD2 . PHE A 1 43  ? 110.59200 109.02000 77.73100  1.000 47.52460 ? 43  PHE A CD2 1 
ATOM   30   C CE1 . PHE A 1 43  ? 113.26700 109.50300 77.29700  1.000 47.52460 ? 43  PHE A CE1 1 
ATOM   31   C CE2 . PHE A 1 43  ? 110.99400 110.17000 77.07700  1.000 47.52460 ? 43  PHE A CE2 1 
ATOM   32   C CZ  . PHE A 1 43  ? 112.33200 110.41000 76.86200  1.000 47.52460 ? 43  PHE A CZ  1 
ATOM   33   N N   . GLY A 1 44  ? 111.46600 103.78200 80.21900  1.000 44.11117 ? 44  GLY A N   1 
ATOM   34   C CA  . GLY A 1 44  ? 110.72900 102.81000 81.00800  1.000 44.11117 ? 44  GLY A CA  1 
ATOM   35   C C   . GLY A 1 44  ? 111.36000 102.49600 82.35000  1.000 44.11117 ? 44  GLY A C   1 
ATOM   36   O O   . GLY A 1 44  ? 110.66400 102.08400 83.28400  1.000 44.11117 ? 44  GLY A O   1 
ATOM   37   N N   . TRP A 1 45  ? 112.67800 102.67500 82.46900  1.000 43.94786 ? 45  TRP A N   1 
ATOM   38   C CA  . TRP A 1 45  ? 113.31700 102.48000 83.76500  1.000 43.94786 ? 45  TRP A CA  1 
ATOM   39   C C   . TRP A 1 45  ? 112.87500 103.52600 84.77300  1.000 43.94786 ? 45  TRP A C   1 
ATOM   40   O O   . TRP A 1 45  ? 112.81700 103.23400 85.96900  1.000 43.94786 ? 45  TRP A O   1 
ATOM   41   C CB  . TRP A 1 45  ? 114.83900 102.48100 83.63400  1.000 43.94786 ? 45  TRP A CB  1 
ATOM   42   C CG  . TRP A 1 45  ? 115.37400 101.27900 82.94200  1.000 43.94786 ? 45  TRP A CG  1 
ATOM   43   C CD1 . TRP A 1 45  ? 116.03300 101.24400 81.75600  1.000 43.94786 ? 45  TRP A CD1 1 
ATOM   44   C CD2 . TRP A 1 45  ? 115.29300 99.92400  83.39700  1.000 43.94786 ? 45  TRP A CD2 1 
ATOM   45   N NE1 . TRP A 1 45  ? 116.37100 99.95400  81.43700  1.000 43.94786 ? 45  TRP A NE1 1 
ATOM   46   C CE2 . TRP A 1 45  ? 115.92700 99.12300  82.43000  1.000 43.94786 ? 45  TRP A CE2 1 
ATOM   47   C CE3 . TRP A 1 45  ? 114.74800 99.31000  84.53000  1.000 43.94786 ? 45  TRP A CE3 1 
ATOM   48   C CZ2 . TRP A 1 45  ? 116.03100 97.73900  82.56000  1.000 43.94786 ? 45  TRP A CZ2 1 
ATOM   49   C CZ3 . TRP A 1 45  ? 114.85000 97.94100  84.65600  1.000 43.94786 ? 45  TRP A CZ3 1 
ATOM   50   C CH2 . TRP A 1 45  ? 115.48800 97.16900  83.67800  1.000 43.94786 ? 45  TRP A CH2 1 
ATOM   51   N N   . LEU A 1 46  ? 112.54900 104.73600 84.31600  1.000 38.97767 ? 46  LEU A N   1 
ATOM   52   C CA  . LEU A 1 46  ? 111.98200 105.73000 85.21800  1.000 38.97767 ? 46  LEU A CA  1 
ATOM   53   C C   . LEU A 1 46  ? 110.64300 105.26300 85.77600  1.000 38.97767 ? 46  LEU A C   1 
ATOM   54   O O   . LEU A 1 46  ? 110.37800 105.41500 86.97100  1.000 38.97767 ? 46  LEU A O   1 
ATOM   55   C CB  . LEU A 1 46  ? 111.83400 107.07100 84.50400  1.000 38.97767 ? 46  LEU A CB  1 
ATOM   56   C CG  . LEU A 1 46  ? 111.31800 108.20300 85.39100  1.000 38.97767 ? 46  LEU A CG  1 
ATOM   57   C CD1 . LEU A 1 46  ? 112.28800 108.45600 86.53200  1.000 38.97767 ? 46  LEU A CD1 1 
ATOM   58   C CD2 . LEU A 1 46  ? 111.08700 109.46900 84.58800  1.000 38.97767 ? 46  LEU A CD2 1 
ATOM   59   N N   . ILE A 1 47  ? 109.80300 104.66200 84.93100  1.000 38.88313 ? 47  ILE A N   1 
ATOM   60   C CA  . ILE A 1 47  ? 108.51600 104.14200 85.38200  1.000 38.88313 ? 47  ILE A CA  1 
ATOM   61   C C   . ILE A 1 47  ? 108.70700 102.97300 86.34600  1.000 38.88313 ? 47  ILE A C   1 
ATOM   62   O O   . ILE A 1 47  ? 108.01700 102.88000 87.36800  1.000 38.88313 ? 47  ILE A O   1 
ATOM   63   C CB  . ILE A 1 47  ? 107.65100 103.75800 84.16600  1.000 38.88313 ? 47  ILE A CB  1 
ATOM   64   C CG1 . ILE A 1 47  ? 107.13900 105.01800 83.46400  1.000 38.88313 ? 47  ILE A CG1 1 
ATOM   65   C CG2 . ILE A 1 47  ? 106.49000 102.86700 84.57300  1.000 38.88313 ? 47  ILE A CG2 1 
ATOM   66   C CD1 . ILE A 1 47  ? 106.12000 104.75700 82.39000  1.000 38.88313 ? 47  ILE A CD1 1 
ATOM   67   N N   . VAL A 1 48  ? 109.64300 102.07100 86.04400  1.000 38.78911 ? 48  VAL A N   1 
ATOM   68   C CA  . VAL A 1 48  ? 109.91200 100.94500 86.94000  1.000 38.78911 ? 48  VAL A CA  1 
ATOM   69   C C   . VAL A 1 48  ? 110.41200 101.43900 88.29500  1.000 38.78911 ? 48  VAL A C   1 
ATOM   70   O O   . VAL A 1 48  ? 109.97400 100.95900 89.35200  1.000 38.78911 ? 48  VAL A O   1 
ATOM   71   C CB  . VAL A 1 48  ? 110.90900 99.97000  86.28300  1.000 38.78911 ? 48  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 48  ? 111.35800 98.91000  87.26900  1.000 38.78911 ? 48  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 48  ? 110.28700 99.32000  85.06300  1.000 38.78911 ? 48  VAL A CG2 1 
ATOM   74   N N   . GLY A 1 49  ? 111.32000 102.41800 88.28400  1.000 36.76780 ? 49  GLY A N   1 
ATOM   75   C CA  . GLY A 1 49  ? 111.80200 102.99100 89.52700  1.000 36.76780 ? 49  GLY A CA  1 
ATOM   76   C C   . GLY A 1 49  ? 110.71500 103.69600 90.31300  1.000 36.76780 ? 49  GLY A C   1 
ATOM   77   O O   . GLY A 1 49  ? 110.67100 103.60300 91.53800  1.000 36.76780 ? 49  GLY A O   1 
ATOM   78   N N   . VAL A 1 50  ? 109.82100 104.40400 89.61900  1.000 35.95894 ? 50  VAL A N   1 
ATOM   79   C CA  . VAL A 1 50  ? 108.71200 105.07600 90.29100  1.000 35.95894 ? 50  VAL A CA  1 
ATOM   80   C C   . VAL A 1 50  ? 107.78100 104.05600 90.93300  1.000 35.95894 ? 50  VAL A C   1 
ATOM   81   O O   . VAL A 1 50  ? 107.32300 104.24100 92.06300  1.000 35.95894 ? 50  VAL A O   1 
ATOM   82   C CB  . VAL A 1 50  ? 107.96600 105.99200 89.30100  1.000 35.95894 ? 50  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 50  ? 106.57500 106.33000 89.80300  1.000 35.95894 ? 50  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 50  ? 108.75500 107.25500 89.06800  1.000 35.95894 ? 50  VAL A CG2 1 
ATOM   85   N N   . ALA A 1 51  ? 107.49800 102.96200 90.22700  1.000 37.27432 ? 51  ALA A N   1 
ATOM   86   C CA  . ALA A 1 51  ? 106.61800 101.93500 90.77200  1.000 37.27432 ? 51  ALA A CA  1 
ATOM   87   C C   . ALA A 1 51  ? 107.22600 101.27200 92.00500  1.000 37.27432 ? 51  ALA A C   1 
ATOM   88   O O   . ALA A 1 51  ? 106.53700 101.06600 93.01300  1.000 37.27432 ? 51  ALA A O   1 
ATOM   89   C CB  . ALA A 1 51  ? 106.30800 100.90100 89.69200  1.000 37.27432 ? 51  ALA A CB  1 
ATOM   90   N N   . LEU A 1 52  ? 108.52400 100.95700 91.95400  1.000 36.73039 ? 52  LEU A N   1 
ATOM   91   C CA  . LEU A 1 52  ? 109.18400 100.36600 93.11500  1.000 36.73039 ? 52  LEU A CA  1 
ATOM   92   C C   . LEU A 1 52  ? 109.26100 101.34900 94.27900  1.000 36.73039 ? 52  LEU A C   1 
ATOM   93   O O   . LEU A 1 52  ? 109.05000 100.96600 95.43800  1.000 36.73039 ? 52  LEU A O   1 
ATOM   94   C CB  . LEU A 1 52  ? 110.57700 99.87400  92.73000  1.000 36.73039 ? 52  LEU A CB  1 
ATOM   95   C CG  . LEU A 1 52  ? 110.58300 98.56800  91.94000  1.000 36.73039 ? 52  LEU A CG  1 
ATOM   96   C CD1 . LEU A 1 52  ? 111.96200 98.27200  91.39300  1.000 36.73039 ? 52  LEU A CD1 1 
ATOM   97   C CD2 . LEU A 1 52  ? 110.08900 97.43000  92.81500  1.000 36.73039 ? 52  LEU A CD2 1 
ATOM   98   N N   . LEU A 1 53  ? 109.55800 102.61900 93.98800  1.000 37.07118 ? 53  LEU A N   1 
ATOM   99   C CA  . LEU A 1 53  ? 109.58000 103.64700 95.02000  1.000 37.07118 ? 53  LEU A CA  1 
ATOM   100  C C   . LEU A 1 53  ? 108.21400 103.80700 95.66900  1.000 37.07118 ? 53  LEU A C   1 
ATOM   101  O O   . LEU A 1 53  ? 108.11900 103.96000 96.88800  1.000 37.07118 ? 53  LEU A O   1 
ATOM   102  C CB  . LEU A 1 53  ? 110.04600 104.97300 94.42200  1.000 37.07118 ? 53  LEU A CB  1 
ATOM   103  C CG  . LEU A 1 53  ? 109.96300 106.21000 95.31600  1.000 37.07118 ? 53  LEU A CG  1 
ATOM   104  C CD1 . LEU A 1 53  ? 110.96200 106.11500 96.45100  1.000 37.07118 ? 53  LEU A CD1 1 
ATOM   105  C CD2 . LEU A 1 53  ? 110.18500 107.47400 94.51000  1.000 37.07118 ? 53  LEU A CD2 1 
ATOM   106  N N   . ALA A 1 54  ? 107.14700 103.77400 94.86800  1.000 37.16335 ? 54  ALA A N   1 
ATOM   107  C CA  . ALA A 1 54  ? 105.79800 103.86300 95.41100  1.000 37.16335 ? 54  ALA A CA  1 
ATOM   108  C C   . ALA A 1 54  ? 105.48400 102.67500 96.30800  1.000 37.16335 ? 54  ALA A C   1 
ATOM   109  O O   . ALA A 1 54  ? 104.91500 102.84900 97.39100  1.000 37.16335 ? 54  ALA A O   1 
ATOM   110  C CB  . ALA A 1 54  ? 104.77800 103.96200 94.27900  1.000 37.16335 ? 54  ALA A CB  1 
ATOM   111  N N   . VAL A 1 55  ? 105.87200 101.46600 95.88200  1.000 37.60241 ? 55  VAL A N   1 
ATOM   112  C CA  . VAL A 1 55  ? 105.65600 100.27400 96.70200  1.000 37.60241 ? 55  VAL A CA  1 
ATOM   113  C C   . VAL A 1 55  ? 106.34000 100.43000 98.05300  1.000 37.60241 ? 55  VAL A C   1 
ATOM   114  O O   . VAL A 1 55  ? 105.71900 100.26000 99.11000  1.000 37.60241 ? 55  VAL A O   1 
ATOM   115  C CB  . VAL A 1 55  ? 106.15900 99.01300  95.97500  1.000 37.60241 ? 55  VAL A CB  1 
ATOM   116  C CG1 . VAL A 1 55  ? 106.24600 97.84100  96.94400  1.000 37.60241 ? 55  VAL A CG1 1 
ATOM   117  C CG2 . VAL A 1 55  ? 105.27200 98.65900  94.81700  1.000 37.60241 ? 55  VAL A CG2 1 
ATOM   118  N N   . PHE A 1 56  ? 107.61800 100.80500 98.03600  1.000 39.16325 ? 56  PHE A N   1 
ATOM   119  C CA  . PHE A 1 56  ? 108.38200 100.84300 99.27700  1.000 39.16325 ? 56  PHE A CA  1 
ATOM   120  C C   . PHE A 1 56  ? 107.96900 102.00400 100.17300 1.000 39.16325 ? 56  PHE A C   1 
ATOM   121  O O   . PHE A 1 56  ? 107.91700 101.84100 101.39400 1.000 39.16325 ? 56  PHE A O   1 
ATOM   122  C CB  . PHE A 1 56  ? 109.87400 100.87900 98.96500  1.000 39.16325 ? 56  PHE A CB  1 
ATOM   123  C CG  . PHE A 1 56  ? 110.46600 99.52100  98.75100  1.000 39.16325 ? 56  PHE A CG  1 
ATOM   124  C CD1 . PHE A 1 56  ? 110.98100 98.80200  99.81300  1.000 39.16325 ? 56  PHE A CD1 1 
ATOM   125  C CD2 . PHE A 1 56  ? 110.47600 98.94700  97.49300  1.000 39.16325 ? 56  PHE A CD2 1 
ATOM   126  C CE1 . PHE A 1 56  ? 111.51300 97.54300  99.62000  1.000 39.16325 ? 56  PHE A CE1 1 
ATOM   127  C CE2 . PHE A 1 56  ? 111.00300 97.69200  97.29400  1.000 39.16325 ? 56  PHE A CE2 1 
ATOM   128  C CZ  . PHE A 1 56  ? 111.52400 96.98800  98.35900  1.000 39.16325 ? 56  PHE A CZ  1 
ATOM   129  N N   . GLN A 1 57  ? 107.65700 103.17000 99.59900  1.000 41.06627 ? 57  GLN A N   1 
ATOM   130  C CA  . GLN A 1 57  ? 107.17300 104.29800 100.39200 1.000 41.06627 ? 57  GLN A CA  1 
ATOM   131  C C   . GLN A 1 57  ? 105.82700 103.98700 101.03700 1.000 41.06627 ? 57  GLN A C   1 
ATOM   132  O O   . GLN A 1 57  ? 105.60800 104.28000 102.22200 1.000 41.06627 ? 57  GLN A O   1 
ATOM   133  C CB  . GLN A 1 57  ? 107.06700 105.53900 99.50800  1.000 41.06627 ? 57  GLN A CB  1 
ATOM   134  C CG  . GLN A 1 57  ? 108.18600 106.53800 99.68000  1.000 41.06627 ? 57  GLN A CG  1 
ATOM   135  C CD  . GLN A 1 57  ? 108.26200 107.09000 101.08500 1.000 41.06627 ? 57  GLN A CD  1 
ATOM   136  O OE1 . GLN A 1 57  ? 107.31700 107.70500 101.57300 1.000 41.06627 ? 57  GLN A OE1 1 
ATOM   137  N NE2 . GLN A 1 57  ? 109.38700 106.86900 101.74600 1.000 41.06627 ? 57  GLN A NE2 1 
ATOM   138  N N   . SER A 1 58  ? 104.91300 103.38600 100.27000 1.000 39.54871 ? 58  SER A N   1 
ATOM   139  C CA  . SER A 1 58  ? 103.61000 103.03100 100.81100 1.000 39.54871 ? 58  SER A CA  1 
ATOM   140  C C   . SER A 1 58  ? 103.73500 101.97700 101.90100 1.000 39.54871 ? 58  SER A C   1 
ATOM   141  O O   . SER A 1 58  ? 102.99100 102.00700 102.88600 1.000 39.54871 ? 58  SER A O   1 
ATOM   142  C CB  . SER A 1 58  ? 102.69900 102.54300 99.68700  1.000 39.54871 ? 58  SER A CB  1 
ATOM   143  O OG  . SER A 1 58  ? 102.74600 103.41700 98.58000  1.000 39.54871 ? 58  SER A OG  1 
ATOM   144  N N   . ALA A 1 59  ? 104.66800 101.03600 101.74300 1.000 40.40976 ? 59  ALA A N   1 
ATOM   145  C CA  . ALA A 1 59  ? 104.89800 100.05300 102.79600 1.000 40.40976 ? 59  ALA A CA  1 
ATOM   146  C C   . ALA A 1 59  ? 105.50800 100.69900 104.03400 1.000 40.40976 ? 59  ALA A C   1 
ATOM   147  O O   . ALA A 1 59  ? 105.16900 100.32600 105.16100 1.000 40.40976 ? 59  ALA A O   1 
ATOM   148  C CB  . ALA A 1 59  ? 105.78800 98.92600  102.27900 1.000 40.40976 ? 59  ALA A CB  1 
ATOM   149  N N   . SER A 1 60  ? 106.40500 101.67000 103.84600 1.000 42.06541 ? 60  SER A N   1 
ATOM   150  C CA  . SER A 1 60  ? 107.02500 102.33700 104.98500 1.000 42.06541 ? 60  SER A CA  1 
ATOM   151  C C   . SER A 1 60  ? 106.01900 103.16500 105.76800 1.000 42.06541 ? 60  SER A C   1 
ATOM   152  O O   . SER A 1 60  ? 106.19400 103.37200 106.97300 1.000 42.06541 ? 60  SER A O   1 
ATOM   153  C CB  . SER A 1 60  ? 108.17800 103.22600 104.52100 1.000 42.06541 ? 60  SER A CB  1 
ATOM   154  O OG  . SER A 1 60  ? 107.70200 104.43900 103.97100 1.000 42.06541 ? 60  SER A OG  1 
ATOM   155  N N   . LYS A 1 61  ? 104.97000 103.65500 105.10700 1.000 44.52379 ? 61  LYS A N   1 
ATOM   156  C CA  . LYS A 1 61  ? 103.96300 104.42500 105.83100 1.000 44.52379 ? 61  LYS A CA  1 
ATOM   157  C C   . LYS A 1 61  ? 103.15800 103.60100 106.83500 1.000 44.52379 ? 61  LYS A C   1 
ATOM   158  O O   . LYS A 1 61  ? 102.53200 104.19300 107.71800 1.000 44.52379 ? 61  LYS A O   1 
ATOM   159  C CB  . LYS A 1 61  ? 102.99400 105.10000 104.85700 1.000 44.52379 ? 61  LYS A CB  1 
ATOM   160  C CG  . LYS A 1 61  ? 103.62500 106.15000 103.96700 1.000 44.52379 ? 61  LYS A CG  1 
ATOM   161  C CD  . LYS A 1 61  ? 103.75800 107.47600 104.68900 1.000 44.52379 ? 61  LYS A CD  1 
ATOM   162  C CE  . LYS A 1 61  ? 102.51400 108.33500 104.51600 1.000 44.52379 ? 61  LYS A CE  1 
ATOM   163  N NZ  . LYS A 1 61  ? 102.56200 109.56300 105.35700 1.000 44.52379 ? 61  LYS A NZ  1 
ATOM   164  N N   . ILE A 1 62  ? 103.15000 102.27100 106.74000 1.000 43.93679 ? 62  ILE A N   1 
ATOM   165  C CA  . ILE A 1 62  ? 102.19500 101.48300 107.51600 1.000 43.93679 ? 62  ILE A CA  1 
ATOM   166  C C   . ILE A 1 62  ? 102.84400 100.37700 108.34100 1.000 43.93679 ? 62  ILE A C   1 
ATOM   167  O O   . ILE A 1 62  ? 102.19300 99.37900  108.66100 1.000 43.93679 ? 62  ILE A O   1 
ATOM   168  C CB  . ILE A 1 62  ? 101.11700 100.88100 106.59600 1.000 43.93679 ? 62  ILE A CB  1 
ATOM   169  C CG1 . ILE A 1 62  ? 101.76500 100.06400 105.47800 1.000 43.93679 ? 62  ILE A CG1 1 
ATOM   170  C CG2 . ILE A 1 62  ? 100.20500 101.96900 106.03800 1.000 43.93679 ? 62  ILE A CG2 1 
ATOM   171  C CD1 . ILE A 1 62  ? 100.77400 99.42300  104.55800 1.000 43.93679 ? 62  ILE A CD1 1 
ATOM   172  N N   . ILE A 1 63  ? 104.10900 100.53500 108.70700 1.000 45.59661 ? 63  ILE A N   1 
ATOM   173  C CA  . ILE A 1 63  ? 104.77700 99.57400  109.58200 1.000 45.59661 ? 63  ILE A CA  1 
ATOM   174  C C   . ILE A 1 63  ? 104.70100 100.08600 111.01500 1.000 45.59661 ? 63  ILE A C   1 
ATOM   175  O O   . ILE A 1 63  ? 105.24500 101.14900 111.32700 1.000 45.59661 ? 63  ILE A O   1 
ATOM   176  C CB  . ILE A 1 63  ? 106.23400 99.34600  109.15400 1.000 45.59661 ? 63  ILE A CB  1 
ATOM   177  C CG1 . ILE A 1 63  ? 106.29400 98.70200  107.77000 1.000 45.59661 ? 63  ILE A CG1 1 
ATOM   178  C CG2 . ILE A 1 63  ? 106.96400 98.48100  110.17000 1.000 45.59661 ? 63  ILE A CG2 1 
ATOM   179  C CD1 . ILE A 1 63  ? 107.62500 98.87200  107.07600 1.000 45.59661 ? 63  ILE A CD1 1 
ATOM   180  N N   . THR A 1 64  ? 104.03500 99.33000  111.88700 1.000 48.32962 ? 64  THR A N   1 
ATOM   181  C CA  . THR A 1 64  ? 103.94500 99.70500  113.29400 1.000 48.32962 ? 64  THR A CA  1 
ATOM   182  C C   . THR A 1 64  ? 105.31400 99.62700  113.95700 1.000 48.32962 ? 64  THR A C   1 
ATOM   183  O O   . THR A 1 64  ? 106.08000 98.69400  113.71200 1.000 48.32962 ? 64  THR A O   1 
ATOM   184  C CB  . THR A 1 64  ? 102.95800 98.80600  114.03700 1.000 48.32962 ? 64  THR A CB  1 
ATOM   185  O OG1 . THR A 1 64  ? 103.49200 97.48200  114.13900 1.000 48.32962 ? 64  THR A OG1 1 
ATOM   186  C CG2 . THR A 1 64  ? 101.64100 98.75700  113.31500 1.000 48.32962 ? 64  THR A CG2 1 
ATOM   187  N N   . LEU A 1 65  ? 105.63100 100.63100 114.76900 1.000 45.52174 ? 65  LEU A N   1 
ATOM   188  C CA  . LEU A 1 65  ? 106.91800 100.69700 115.45600 1.000 45.52174 ? 65  LEU A CA  1 
ATOM   189  C C   . LEU A 1 65  ? 106.75700 100.31900 116.92700 1.000 45.52174 ? 65  LEU A C   1 
ATOM   190  O O   . LEU A 1 65  ? 106.80800 101.15600 117.82500 1.000 45.52174 ? 65  LEU A O   1 
ATOM   191  C CB  . LEU A 1 65  ? 107.52100 102.08800 115.30200 1.000 45.52174 ? 65  LEU A CB  1 
ATOM   192  C CG  . LEU A 1 65  ? 107.59500 102.59000 113.86300 1.000 45.52174 ? 65  LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 65  ? 108.18600 103.98300 113.80400 1.000 45.52174 ? 65  LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 65  ? 108.39400 101.62300 113.03100 1.000 45.52174 ? 65  LEU A CD2 1 
ATOM   195  N N   . LYS A 1 66  ? 106.58000 99.02400  117.17100 1.000 46.49987 ? 66  LYS A N   1 
ATOM   196  C CA  . LYS A 1 66  ? 106.45400 98.52600  118.53500 1.000 46.49987 ? 66  LYS A CA  1 
ATOM   197  C C   . LYS A 1 66  ? 107.60100 97.61800  118.94800 1.000 46.49987 ? 66  LYS A C   1 
ATOM   198  O O   . LYS A 1 66  ? 108.28700 97.90300  119.93200 1.000 46.49987 ? 66  LYS A O   1 
ATOM   199  C CB  . LYS A 1 66  ? 105.11700 97.79700  118.70900 1.000 46.49987 ? 66  LYS A CB  1 
ATOM   200  C CG  . LYS A 1 66  ? 103.92900 98.65400  118.35200 1.000 46.49987 ? 66  LYS A CG  1 
ATOM   201  C CD  . LYS A 1 66  ? 102.65400 98.13500  118.96800 1.000 46.49987 ? 66  LYS A CD  1 
ATOM   202  C CE  . LYS A 1 66  ? 101.55900 99.17700  118.89100 1.000 46.49987 ? 66  LYS A CE  1 
ATOM   203  N NZ  . LYS A 1 66  ? 100.61800 99.07200  120.02800 1.000 46.49987 ? 66  LYS A NZ  1 
ATOM   204  N N   . LYS A 1 67  ? 107.84400 96.54200  118.21600 1.000 50.04904 ? 67  LYS A N   1 
ATOM   205  C CA  . LYS A 1 67  ? 108.92500 95.62200  118.53000 1.000 50.04904 ? 67  LYS A CA  1 
ATOM   206  C C   . LYS A 1 67  ? 110.18900 96.00900  117.77400 1.000 50.04904 ? 67  LYS A C   1 
ATOM   207  O O   . LYS A 1 67  ? 110.15000 96.75900  116.79700 1.000 50.04904 ? 67  LYS A O   1 
ATOM   208  C CB  . LYS A 1 67  ? 108.51600 94.18500  118.21100 1.000 50.04904 ? 67  LYS A CB  1 
ATOM   209  C CG  . LYS A 1 67  ? 107.11100 93.86800  118.67800 1.000 50.04904 ? 67  LYS A CG  1 
ATOM   210  C CD  . LYS A 1 67  ? 106.79600 92.39600  118.59400 1.000 50.04904 ? 67  LYS A CD  1 
ATOM   211  C CE  . LYS A 1 67  ? 105.30400 92.17500  118.38900 1.000 50.04904 ? 67  LYS A CE  1 
ATOM   212  N NZ  . LYS A 1 67  ? 104.99500 91.59600  117.04700 1.000 50.04904 ? 67  LYS A NZ  1 
ATOM   213  N N   . ARG A 1 68  ? 111.32200 95.49700  118.26000 1.000 46.80743 ? 68  ARG A N   1 
ATOM   214  C CA  . ARG A 1 68  ? 112.61700 95.90800  117.72900 1.000 46.80743 ? 68  ARG A CA  1 
ATOM   215  C C   . ARG A 1 68  ? 112.80200 95.46000  116.28600 1.000 46.80743 ? 68  ARG A C   1 
ATOM   216  O O   . ARG A 1 68  ? 113.41200 96.17500  115.48100 1.000 46.80743 ? 68  ARG A O   1 
ATOM   217  C CB  . ARG A 1 68  ? 113.74100 95.35800  118.60400 1.000 46.80743 ? 68  ARG A CB  1 
ATOM   218  C CG  . ARG A 1 68  ? 114.86500 96.34100  118.83200 1.000 46.80743 ? 68  ARG A CG  1 
ATOM   219  C CD  . ARG A 1 68  ? 115.70200 95.97400  120.04100 1.000 46.80743 ? 68  ARG A CD  1 
ATOM   220  N NE  . ARG A 1 68  ? 117.05400 96.51500  119.95500 1.000 46.80743 ? 68  ARG A NE  1 
ATOM   221  C CZ  . ARG A 1 68  ? 118.03700 95.96400  119.25000 1.000 46.80743 ? 68  ARG A CZ  1 
ATOM   222  N NH1 . ARG A 1 68  ? 117.82600 94.84600  118.57000 1.000 46.80743 ? 68  ARG A NH1 1 
ATOM   223  N NH2 . ARG A 1 68  ? 119.23600 96.52800  119.22900 1.000 46.80743 ? 68  ARG A NH2 1 
ATOM   224  N N   . TRP A 1 69  ? 112.28900 94.27700  115.94300 1.000 52.00850 ? 69  TRP A N   1 
ATOM   225  C CA  . TRP A 1 69  ? 112.39800 93.80500  114.57200 1.000 52.00850 ? 69  TRP A CA  1 
ATOM   226  C C   . TRP A 1 69  ? 111.56800 94.65700  113.62300 1.000 52.00850 ? 69  TRP A C   1 
ATOM   227  O O   . TRP A 1 69  ? 111.97200 94.87100  112.47700 1.000 52.00850 ? 69  TRP A O   1 
ATOM   228  C CB  . TRP A 1 69  ? 112.00500 92.32900  114.49000 1.000 52.00850 ? 69  TRP A CB  1 
ATOM   229  C CG  . TRP A 1 69  ? 110.54700 92.04400  114.60000 1.000 52.00850 ? 69  TRP A CG  1 
ATOM   230  C CD1 . TRP A 1 69  ? 109.85500 91.76100  115.73500 1.000 52.00850 ? 69  TRP A CD1 1 
ATOM   231  C CD2 . TRP A 1 69  ? 109.59900 91.99500  113.52900 1.000 52.00850 ? 69  TRP A CD2 1 
ATOM   232  N NE1 . TRP A 1 69  ? 108.53200 91.55200  115.44400 1.000 52.00850 ? 69  TRP A NE1 1 
ATOM   233  C CE2 . TRP A 1 69  ? 108.34900 91.68700  114.09400 1.000 52.00850 ? 69  TRP A CE2 1 
ATOM   234  C CE3 . TRP A 1 69  ? 109.68400 92.19200  112.14900 1.000 52.00850 ? 69  TRP A CE3 1 
ATOM   235  C CZ2 . TRP A 1 69  ? 107.19500 91.57100  113.32800 1.000 52.00850 ? 69  TRP A CZ2 1 
ATOM   236  C CZ3 . TRP A 1 69  ? 108.53900 92.07100  111.39200 1.000 52.00850 ? 69  TRP A CZ3 1 
ATOM   237  C CH2 . TRP A 1 69  ? 107.31200 91.76200  111.98200 1.000 52.00850 ? 69  TRP A CH2 1 
ATOM   238  N N   . GLN A 1 70  ? 110.43300 95.18300  114.08700 1.000 47.08246 ? 70  GLN A N   1 
ATOM   239  C CA  . GLN A 1 70  ? 109.66700 96.11600  113.26900 1.000 47.08246 ? 70  GLN A CA  1 
ATOM   240  C C   . GLN A 1 70  ? 110.41600 97.42900  113.07300 1.000 47.08246 ? 70  GLN A C   1 
ATOM   241  O O   . GLN A 1 70  ? 110.34300 98.03200  111.99900 1.000 47.08246 ? 70  GLN A O   1 
ATOM   242  C CB  . GLN A 1 70  ? 108.29800 96.36500  113.89300 1.000 47.08246 ? 70  GLN A CB  1 
ATOM   243  C CG  . GLN A 1 70  ? 107.48900 95.11000  114.12300 1.000 47.08246 ? 70  GLN A CG  1 
ATOM   244  C CD  . GLN A 1 70  ? 106.23800 95.36500  114.92900 1.000 47.08246 ? 70  GLN A CD  1 
ATOM   245  O OE1 . GLN A 1 70  ? 106.24400 96.15200  115.86900 1.000 47.08246 ? 70  GLN A OE1 1 
ATOM   246  N NE2 . GLN A 1 70  ? 105.15700 94.69800  114.56600 1.000 47.08246 ? 70  GLN A NE2 1 
ATOM   247  N N   . LEU A 1 71  ? 111.14500 97.88500  114.09500 1.000 41.51675 ? 71  LEU A N   1 
ATOM   248  C CA  . LEU A 1 71  ? 111.95400 99.09100  113.94600 1.000 41.51675 ? 71  LEU A CA  1 
ATOM   249  C C   . LEU A 1 71  ? 113.07400 98.88300  112.93500 1.000 41.51675 ? 71  LEU A C   1 
ATOM   250  O O   . LEU A 1 71  ? 113.33300 99.75400  112.09500 1.000 41.51675 ? 71  LEU A O   1 
ATOM   251  C CB  . LEU A 1 71  ? 112.52800 99.51300  115.29800 1.000 41.51675 ? 71  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 71  ? 111.52900 99.85600  116.40200 1.000 41.51675 ? 71  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 71  ? 112.18400 99.73600  117.76300 1.000 41.51675 ? 71  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 71  ? 110.97500 101.24600 116.20000 1.000 41.51675 ? 71  LEU A CD2 1 
ATOM   255  N N   . ALA A 1 72  ? 113.74400 97.73000  113.00000 1.000 39.97349 ? 72  ALA A N   1 
ATOM   256  C CA  . ALA A 1 72  ? 114.79000 97.42700  112.02900 1.000 39.97349 ? 72  ALA A CA  1 
ATOM   257  C C   . ALA A 1 72  ? 114.21700 97.30600  110.62200 1.000 39.97349 ? 72  ALA A C   1 
ATOM   258  O O   . ALA A 1 72  ? 114.82200 97.78500  109.65500 1.000 39.97349 ? 72  ALA A O   1 
ATOM   259  C CB  . ALA A 1 72  ? 115.52600 96.15000  112.42700 1.000 39.97349 ? 72  ALA A CB  1 
ATOM   260  N N   . LEU A 1 73  ? 113.04600 96.67700  110.49200 1.000 38.66469 ? 73  LEU A N   1 
ATOM   261  C CA  . LEU A 1 73  ? 112.39600 96.55900  109.19300 1.000 38.66469 ? 73  LEU A CA  1 
ATOM   262  C C   . LEU A 1 73  ? 112.03300 97.92400  108.62700 1.000 38.66469 ? 73  LEU A C   1 
ATOM   263  O O   . LEU A 1 73  ? 112.25000 98.18700  107.44100 1.000 38.66469 ? 73  LEU A O   1 
ATOM   264  C CB  . LEU A 1 73  ? 111.15000 95.68400  109.31200 1.000 38.66469 ? 73  LEU A CB  1 
ATOM   265  C CG  . LEU A 1 73  ? 110.27700 95.58500  108.06400 1.000 38.66469 ? 73  LEU A CG  1 
ATOM   266  C CD1 . LEU A 1 73  ? 110.98400 94.78500  106.98300 1.000 38.66469 ? 73  LEU A CD1 1 
ATOM   267  C CD2 . LEU A 1 73  ? 108.93600 94.97100  108.39900 1.000 38.66469 ? 73  LEU A CD2 1 
ATOM   268  N N   . SER A 1 74  ? 111.49300 98.80700  109.46800 1.000 39.29948 ? 74  SER A N   1 
ATOM   269  C CA  . SER A 1 74  ? 111.12500 100.14500 109.02400 1.000 39.29948 ? 74  SER A CA  1 
ATOM   270  C C   . SER A 1 74  ? 112.34700 100.94700 108.59800 1.000 39.29948 ? 74  SER A C   1 
ATOM   271  O O   . SER A 1 74  ? 112.30600 101.65800 107.58800 1.000 39.29948 ? 74  SER A O   1 
ATOM   272  C CB  . SER A 1 74  ? 110.36900 100.86100 110.13800 1.000 39.29948 ? 74  SER A CB  1 
ATOM   273  O OG  . SER A 1 74  ? 109.96800 102.15700 109.74800 1.000 39.29948 ? 74  SER A OG  1 
ATOM   274  N N   . LYS A 1 75  ? 113.44600 100.83900 109.34900 1.000 38.70198 ? 75  LYS A N   1 
ATOM   275  C CA  . LYS A 1 75  ? 114.67200 101.53100 108.96400 1.000 38.70198 ? 75  LYS A CA  1 
ATOM   276  C C   . LYS A 1 75  ? 115.23800 101.00100 107.65200 1.000 38.70198 ? 75  LYS A C   1 
ATOM   277  O O   . LYS A 1 75  ? 115.68500 101.79000 106.81200 1.000 38.70198 ? 75  LYS A O   1 
ATOM   278  C CB  . LYS A 1 75  ? 115.71500 101.41400 110.07600 1.000 38.70198 ? 75  LYS A CB  1 
ATOM   279  C CG  . LYS A 1 75  ? 115.50800 102.36100 111.24500 1.000 38.70198 ? 75  LYS A CG  1 
ATOM   280  C CD  . LYS A 1 75  ? 114.92100 103.69000 110.80800 1.000 38.70198 ? 75  LYS A CD  1 
ATOM   281  C CE  . LYS A 1 75  ? 114.15400 104.36100 111.92800 1.000 38.70198 ? 75  LYS A CE  1 
ATOM   282  N NZ  . LYS A 1 75  ? 114.99700 105.31300 112.69700 1.000 38.70198 ? 75  LYS A NZ  1 
ATOM   283  N N   . GLY A 1 76  ? 115.22100 99.68200  107.45400 1.000 38.09626 ? 76  GLY A N   1 
ATOM   284  C CA  . GLY A 1 76  ? 115.69000 99.13000  106.19400 1.000 38.09626 ? 76  GLY A CA  1 
ATOM   285  C C   . GLY A 1 76  ? 114.82700 99.53600  105.01500 1.000 38.09626 ? 76  GLY A C   1 
ATOM   286  O O   . GLY A 1 76  ? 115.33900 99.83400  103.93100 1.000 38.09626 ? 76  GLY A O   1 
ATOM   287  N N   . VAL A 1 77  ? 113.50900 99.56700  105.21300 1.000 38.63271 ? 77  VAL A N   1 
ATOM   288  C CA  . VAL A 1 77  ? 112.60500 99.98200  104.14900 1.000 38.63271 ? 77  VAL A CA  1 
ATOM   289  C C   . VAL A 1 77  ? 112.80600 101.45700 103.82400 1.000 38.63271 ? 77  VAL A C   1 
ATOM   290  O O   . VAL A 1 77  ? 112.77800 101.85100 102.65700 1.000 38.63271 ? 77  VAL A O   1 
ATOM   291  C CB  . VAL A 1 77  ? 111.14800 99.66000  104.53300 1.000 38.63271 ? 77  VAL A CB  1 
ATOM   292  C CG1 . VAL A 1 77  ? 110.17200 100.32600 103.58700 1.000 38.63271 ? 77  VAL A CG1 1 
ATOM   293  C CG2 . VAL A 1 77  ? 110.92300 98.16300  104.51700 1.000 38.63271 ? 77  VAL A CG2 1 
ATOM   294  N N   . HIS A 1 78  ? 113.05300 102.28600 104.84200 1.000 40.47710 ? 78  HIS A N   1 
ATOM   295  C CA  . HIS A 1 78  ? 113.34200 103.69700 104.60100 1.000 40.47710 ? 78  HIS A CA  1 
ATOM   296  C C   . HIS A 1 78  ? 114.65700 103.88100 103.85200 1.000 40.47710 ? 78  HIS A C   1 
ATOM   297  O O   . HIS A 1 78  ? 114.77000 104.76500 102.99300 1.000 40.47710 ? 78  HIS A O   1 
ATOM   298  C CB  . HIS A 1 78  ? 113.36700 104.45600 105.92300 1.000 40.47710 ? 78  HIS A CB  1 
ATOM   299  C CG  . HIS A 1 78  ? 112.00700 104.76600 106.46100 1.000 40.47710 ? 78  HIS A CG  1 
ATOM   300  N ND1 . HIS A 1 78  ? 111.64500 104.50400 107.76300 1.000 40.47710 ? 78  HIS A ND1 1 
ATOM   301  C CD2 . HIS A 1 78  ? 110.92100 105.32000 105.87300 1.000 40.47710 ? 78  HIS A CD2 1 
ATOM   302  C CE1 . HIS A 1 78  ? 110.39300 104.87700 107.95200 1.000 40.47710 ? 78  HIS A CE1 1 
ATOM   303  N NE2 . HIS A 1 78  ? 109.93200 105.37800 106.82200 1.000 40.47710 ? 78  HIS A NE2 1 
ATOM   304  N N   . PHE A 1 79  ? 115.66100 103.06200 104.16700 1.000 39.77112 ? 79  PHE A N   1 
ATOM   305  C CA  . PHE A 1 79  ? 116.92100 103.11500 103.43200 1.000 39.77112 ? 79  PHE A CA  1 
ATOM   306  C C   . PHE A 1 79  ? 116.72600 102.74600 101.96400 1.000 39.77112 ? 79  PHE A C   1 
ATOM   307  O O   . PHE A 1 79  ? 117.26600 103.41000 101.06700 1.000 39.77112 ? 79  PHE A O   1 
ATOM   308  C CB  . PHE A 1 79  ? 117.93900 102.18600 104.09200 1.000 39.77112 ? 79  PHE A CB  1 
ATOM   309  C CG  . PHE A 1 79  ? 119.30600 102.26500 103.49300 1.000 39.77112 ? 79  PHE A CG  1 
ATOM   310  C CD1 . PHE A 1 79  ? 120.06600 103.41400 103.62000 1.000 39.77112 ? 79  PHE A CD1 1 
ATOM   311  C CD2 . PHE A 1 79  ? 119.83200 101.19300 102.79900 1.000 39.77112 ? 79  PHE A CD2 1 
ATOM   312  C CE1 . PHE A 1 79  ? 121.32500 103.48900 103.06700 1.000 39.77112 ? 79  PHE A CE1 1 
ATOM   313  C CE2 . PHE A 1 79  ? 121.09100 101.26300 102.24700 1.000 39.77112 ? 79  PHE A CE2 1 
ATOM   314  C CZ  . PHE A 1 79  ? 121.83800 102.41300 102.38000 1.000 39.77112 ? 79  PHE A CZ  1 
ATOM   315  N N   . VAL A 1 80  ? 115.94300 101.69700 101.70200 1.000 39.46629 ? 80  VAL A N   1 
ATOM   316  C CA  . VAL A 1 80  ? 115.64700 101.30800 100.32400 1.000 39.46629 ? 80  VAL A CA  1 
ATOM   317  C C   . VAL A 1 80  ? 114.84900 102.40300 99.61700  1.000 39.46629 ? 80  VAL A C   1 
ATOM   318  O O   . VAL A 1 80  ? 115.06500 102.68000 98.43000  1.000 39.46629 ? 80  VAL A O   1 
ATOM   319  C CB  . VAL A 1 80  ? 114.91400 99.95300  100.30300 1.000 39.46629 ? 80  VAL A CB  1 
ATOM   320  C CG1 . VAL A 1 80  ? 114.40400 99.62200  98.90800  1.000 39.46629 ? 80  VAL A CG1 1 
ATOM   321  C CG2 . VAL A 1 80  ? 115.83400 98.85800  100.79500 1.000 39.46629 ? 80  VAL A CG2 1 
ATOM   322  N N   . CYS A 1 81  ? 113.93200 103.05100 100.34000 1.000 40.06953 ? 81  CYS A N   1 
ATOM   323  C CA  . CYS A 1 81  ? 113.16400 104.15900 99.78000  1.000 40.06953 ? 81  CYS A CA  1 
ATOM   324  C C   . CYS A 1 81  ? 114.06900 105.30200 99.36100  1.000 40.06953 ? 81  CYS A C   1 
ATOM   325  O O   . CYS A 1 81  ? 113.89100 105.88200 98.28700  1.000 40.06953 ? 81  CYS A O   1 
ATOM   326  C CB  . CYS A 1 81  ? 112.14600 104.67300 100.79600 1.000 40.06953 ? 81  CYS A CB  1 
ATOM   327  S SG  . CYS A 1 81  ? 110.73100 103.64100 101.06900 1.000 40.06953 ? 81  CYS A SG  1 
ATOM   328  N N   . ASN A 1 82  ? 115.03600 105.65100 100.20900 1.000 39.88859 ? 82  ASN A N   1 
ATOM   329  C CA  . ASN A 1 82  ? 115.94000 106.74200 99.87700  1.000 39.88859 ? 82  ASN A CA  1 
ATOM   330  C C   . ASN A 1 82  ? 116.83300 106.38500 98.69600  1.000 39.88859 ? 82  ASN A C   1 
ATOM   331  O O   . ASN A 1 82  ? 117.11500 107.23800 97.84800  1.000 39.88859 ? 82  ASN A O   1 
ATOM   332  C CB  . ASN A 1 82  ? 116.77700 107.12200 101.09200 1.000 39.88859 ? 82  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 82  ? 117.49600 108.43600 100.90400 1.000 39.88859 ? 82  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 82  ? 116.90700 109.50100 101.05300 1.000 39.88859 ? 82  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 82  ? 118.77500 108.36700 100.56200 1.000 39.88859 ? 82  ASN A ND2 1 
ATOM   336  N N   . LEU A 1 83  ? 117.28300 105.12900 98.62100  1.000 38.87893 ? 83  LEU A N   1 
ATOM   337  C CA  . LEU A 1 83  ? 118.06700 104.70100 97.46400  1.000 38.87893 ? 83  LEU A CA  1 
ATOM   338  C C   . LEU A 1 83  ? 117.25100 104.78200 96.17700  1.000 38.87893 ? 83  LEU A C   1 
ATOM   339  O O   . LEU A 1 83  ? 117.74700 105.25100 95.14700  1.000 38.87893 ? 83  LEU A O   1 
ATOM   340  C CB  . LEU A 1 83  ? 118.59000 103.28400 97.68000  1.000 38.87893 ? 83  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 83  ? 119.64900 103.10900 98.76900  1.000 38.87893 ? 83  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 83  ? 120.12100 101.67300 98.81200  1.000 38.87893 ? 83  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 83  ? 120.81800 104.05100 98.55400  1.000 38.87893 ? 83  LEU A CD2 1 
ATOM   344  N N   . LEU A 1 84  ? 115.98900 104.35000 96.22400  1.000 37.46457 ? 84  LEU A N   1 
ATOM   345  C CA  . LEU A 1 84  ? 115.12300 104.43500 95.05100  1.000 37.46457 ? 84  LEU A CA  1 
ATOM   346  C C   . LEU A 1 84  ? 114.83800 105.88200 94.66700  1.000 37.46457 ? 84  LEU A C   1 
ATOM   347  O O   . LEU A 1 84  ? 114.74400 106.20400 93.47800  1.000 37.46457 ? 84  LEU A O   1 
ATOM   348  C CB  . LEU A 1 84  ? 113.82000 103.68600 95.30900  1.000 37.46457 ? 84  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 84  ? 113.90200 102.16400 95.23700  1.000 37.46457 ? 84  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 84  ? 112.64000 101.54100 95.78900  1.000 37.46457 ? 84  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 84  ? 114.14600 101.72000 93.81400  1.000 37.46457 ? 84  LEU A CD2 1 
ATOM   352  N N   . LEU A 1 85  ? 114.67400 106.76000 95.66000  1.000 37.36691 ? 85  LEU A N   1 
ATOM   353  C CA  . LEU A 1 85  ? 114.45500 108.17500 95.38200  1.000 37.36691 ? 85  LEU A CA  1 
ATOM   354  C C   . LEU A 1 85  ? 115.67000 108.79800 94.71200  1.000 37.36691 ? 85  LEU A C   1 
ATOM   355  O O   . LEU A 1 85  ? 115.53400 109.58100 93.76400  1.000 37.36691 ? 85  LEU A O   1 
ATOM   356  C CB  . LEU A 1 85  ? 114.12300 108.92100 96.67300  1.000 37.36691 ? 85  LEU A CB  1 
ATOM   357  C CG  . LEU A 1 85  ? 113.75300 110.38700 96.47000  1.000 37.36691 ? 85  LEU A CG  1 
ATOM   358  C CD1 . LEU A 1 85  ? 112.32400 110.50400 95.96100  1.000 37.36691 ? 85  LEU A CD1 1 
ATOM   359  C CD2 . LEU A 1 85  ? 113.95300 111.18500 97.74200  1.000 37.36691 ? 85  LEU A CD2 1 
ATOM   360  N N   . LEU A 1 86  ? 116.86700 108.45600 95.19200  1.000 37.27940 ? 86  LEU A N   1 
ATOM   361  C CA  . LEU A 1 86  ? 118.08500 108.90400 94.53000  1.000 37.27940 ? 86  LEU A CA  1 
ATOM   362  C C   . LEU A 1 86  ? 118.14900 108.39200 93.10100  1.000 37.27940 ? 86  LEU A C   1 
ATOM   363  O O   . LEU A 1 86  ? 118.52400 109.13500 92.18600  1.000 37.27940 ? 86  LEU A O   1 
ATOM   364  C CB  . LEU A 1 86  ? 119.31000 108.44600 95.31400  1.000 37.27940 ? 86  LEU A CB  1 
ATOM   365  C CG  . LEU A 1 86  ? 119.64000 109.22000 96.58700  1.000 37.27940 ? 86  LEU A CG  1 
ATOM   366  C CD1 . LEU A 1 86  ? 120.65400 108.45600 97.41800  1.000 37.27940 ? 86  LEU A CD1 1 
ATOM   367  C CD2 . LEU A 1 86  ? 120.16700 110.59800 96.23300  1.000 37.27940 ? 86  LEU A CD2 1 
ATOM   368  N N   . PHE A 1 87  ? 117.76900 107.12900 92.88800  1.000 36.21480 ? 87  PHE A N   1 
ATOM   369  C CA  . PHE A 1 87  ? 117.78100 106.57300 91.54000  1.000 36.21480 ? 87  PHE A CA  1 
ATOM   370  C C   . PHE A 1 87  ? 116.83900 107.33300 90.61200  1.000 36.21480 ? 87  PHE A C   1 
ATOM   371  O O   . PHE A 1 87  ? 117.22400 107.69800 89.50000  1.000 36.21480 ? 87  PHE A O   1 
ATOM   372  C CB  . PHE A 1 87  ? 117.41000 105.09100 91.54800  1.000 36.21480 ? 87  PHE A CB  1 
ATOM   373  C CG  . PHE A 1 87  ? 117.12000 104.55300 90.17800  1.000 36.21480 ? 87  PHE A CG  1 
ATOM   374  C CD1 . PHE A 1 87  ? 118.15300 104.30700 89.29000  1.000 36.21480 ? 87  PHE A CD1 1 
ATOM   375  C CD2 . PHE A 1 87  ? 115.81900 104.33100 89.76000  1.000 36.21480 ? 87  PHE A CD2 1 
ATOM   376  C CE1 . PHE A 1 87  ? 117.89500 103.83800 88.02300  1.000 36.21480 ? 87  PHE A CE1 1 
ATOM   377  C CE2 . PHE A 1 87  ? 115.55900 103.86200 88.49300  1.000 36.21480 ? 87  PHE A CE2 1 
ATOM   378  C CZ  . PHE A 1 87  ? 116.59800 103.61400 87.62400  1.000 36.21480 ? 87  PHE A CZ  1 
ATOM   379  N N   . VAL A 1 88  ? 115.59300 107.56000 91.03900  1.000 35.56824 ? 88  VAL A N   1 
ATOM   380  C CA  . VAL A 1 88  ? 114.64100 108.19900 90.13300  1.000 35.56824 ? 88  VAL A CA  1 
ATOM   381  C C   . VAL A 1 88  ? 115.02100 109.65000 89.89000  1.000 35.56824 ? 88  VAL A C   1 
ATOM   382  O O   . VAL A 1 88  ? 114.86700 110.14700 88.77100  1.000 35.56824 ? 88  VAL A O   1 
ATOM   383  C CB  . VAL A 1 88  ? 113.18000 108.07000 90.61800  1.000 35.56824 ? 88  VAL A CB  1 
ATOM   384  C CG1 . VAL A 1 88  ? 112.69900 106.63000 90.49700  1.000 35.56824 ? 88  VAL A CG1 1 
ATOM   385  C CG2 . VAL A 1 88  ? 112.99700 108.59700 92.02400  1.000 35.56824 ? 88  VAL A CG2 1 
ATOM   386  N N   . THR A 1 89  ? 115.56500 110.33800 90.90100  1.000 36.19862 ? 89  THR A N   1 
ATOM   387  C CA  . THR A 1 89  ? 116.01700 111.71100 90.70400  1.000 36.19862 ? 89  THR A CA  1 
ATOM   388  C C   . THR A 1 89  ? 117.15700 111.78300 89.69700  1.000 36.19862 ? 89  THR A C   1 
ATOM   389  O O   . THR A 1 89  ? 117.09600 112.54800 88.72700  1.000 36.19862 ? 89  THR A O   1 
ATOM   390  C CB  . THR A 1 89  ? 116.45800 112.31600 92.03400  1.000 36.19862 ? 89  THR A CB  1 
ATOM   391  O OG1 . THR A 1 89  ? 115.50300 112.00100 93.05000  1.000 36.19862 ? 89  THR A OG1 1 
ATOM   392  C CG2 . THR A 1 89  ? 116.58000 113.80800 91.89900  1.000 36.19862 ? 89  THR A CG2 1 
ATOM   393  N N   . VAL A 1 90  ? 118.20500 110.98100 89.91100  1.000 35.89770 ? 90  VAL A N   1 
ATOM   394  C CA  . VAL A 1 90  ? 119.37000 111.01600 89.03300  1.000 35.89770 ? 90  VAL A CA  1 
ATOM   395  C C   . VAL A 1 90  ? 118.99400 110.56400 87.62800  1.000 35.89770 ? 90  VAL A C   1 
ATOM   396  O O   . VAL A 1 90  ? 119.42600 111.15800 86.63500  1.000 35.89770 ? 90  VAL A O   1 
ATOM   397  C CB  . VAL A 1 90  ? 120.50800 110.16400 89.62800  1.000 35.89770 ? 90  VAL A CB  1 
ATOM   398  C CG1 . VAL A 1 90  ? 121.62500 109.96100 88.62300  1.000 35.89770 ? 90  VAL A CG1 1 
ATOM   399  C CG2 . VAL A 1 90  ? 121.04100 110.80600 90.88900  1.000 35.89770 ? 90  VAL A CG2 1 
ATOM   400  N N   . TYR A 1 91  ? 118.15600 109.53000 87.52300  1.000 37.93933 ? 91  TYR A N   1 
ATOM   401  C CA  . TYR A 1 91  ? 117.77200 109.00200 86.22200  1.000 37.93933 ? 91  TYR A CA  1 
ATOM   402  C C   . TYR A 1 91  ? 116.89400 109.97500 85.45000  1.000 37.93933 ? 91  TYR A C   1 
ATOM   403  O O   . TYR A 1 91  ? 117.04700 110.11600 84.23400  1.000 37.93933 ? 91  TYR A O   1 
ATOM   404  C CB  . TYR A 1 91  ? 117.05800 107.66600 86.39200  1.000 37.93933 ? 91  TYR A CB  1 
ATOM   405  C CG  . TYR A 1 91  ? 117.01300 106.86800 85.12200  1.000 37.93933 ? 91  TYR A CG  1 
ATOM   406  C CD1 . TYR A 1 91  ? 115.88100 106.86400 84.32200  1.000 37.93933 ? 91  TYR A CD1 1 
ATOM   407  C CD2 . TYR A 1 91  ? 118.11100 106.13600 84.70900  1.000 37.93933 ? 91  TYR A CD2 1 
ATOM   408  C CE1 . TYR A 1 91  ? 115.84400 106.14200 83.15500  1.000 37.93933 ? 91  TYR A CE1 1 
ATOM   409  C CE2 . TYR A 1 91  ? 118.08200 105.41000 83.54800  1.000 37.93933 ? 91  TYR A CE2 1 
ATOM   410  C CZ  . TYR A 1 91  ? 116.94900 105.41500 82.77400  1.000 37.93933 ? 91  TYR A CZ  1 
ATOM   411  O OH  . TYR A 1 91  ? 116.92600 104.68900 81.61500  1.000 37.93933 ? 91  TYR A OH  1 
ATOM   412  N N   . SER A 1 92  ? 115.96100 110.65000 86.12700  1.000 37.87424 ? 92  SER A N   1 
ATOM   413  C CA  . SER A 1 92  ? 115.15600 111.64800 85.43800  1.000 37.87424 ? 92  SER A CA  1 
ATOM   414  C C   . SER A 1 92  ? 115.99300 112.85500 85.04300  1.000 37.87424 ? 92  SER A C   1 
ATOM   415  O O   . SER A 1 92  ? 115.75300 113.45500 83.99100  1.000 37.87424 ? 92  SER A O   1 
ATOM   416  C CB  . SER A 1 92  ? 113.97100 112.06400 86.30900  1.000 37.87424 ? 92  SER A CB  1 
ATOM   417  O OG  . SER A 1 92  ? 114.39300 112.76000 87.46200  1.000 37.87424 ? 92  SER A OG  1 
ATOM   418  N N   . HIS A 1 93  ? 116.99000 113.20900 85.85800  1.000 39.13101 ? 93  HIS A N   1 
ATOM   419  C CA  . HIS A 1 93  ? 117.91300 114.27300 85.48200  1.000 39.13101 ? 93  HIS A CA  1 
ATOM   420  C C   . HIS A 1 93  ? 118.73100 113.88100 84.25600  1.000 39.13101 ? 93  HIS A C   1 
ATOM   421  O O   . HIS A 1 93  ? 118.98400 114.70900 83.37600  1.000 39.13101 ? 93  HIS A O   1 
ATOM   422  C CB  . HIS A 1 93  ? 118.81300 114.60600 86.67300  1.000 39.13101 ? 93  HIS A CB  1 
ATOM   423  C CG  . HIS A 1 93  ? 119.69100 115.79900 86.46500  1.000 39.13101 ? 93  HIS A CG  1 
ATOM   424  N ND1 . HIS A 1 93  ? 120.75700 116.08400 87.28600  1.000 39.13101 ? 93  HIS A ND1 1 
ATOM   425  C CD2 . HIS A 1 93  ? 119.66000 116.78100 85.53500  1.000 39.13101 ? 93  HIS A CD2 1 
ATOM   426  C CE1 . HIS A 1 93  ? 121.35000 117.18600 86.86800  1.000 39.13101 ? 93  HIS A CE1 1 
ATOM   427  N NE2 . HIS A 1 93  ? 120.70500 117.62800 85.80500  1.000 39.13101 ? 93  HIS A NE2 1 
ATOM   428  N N   . LEU A 1 94  ? 119.13400 112.61200 84.17100  1.000 39.83479 ? 94  LEU A N   1 
ATOM   429  C CA  . LEU A 1 94  ? 119.84400 112.12800 82.99000  1.000 39.83479 ? 94  LEU A CA  1 
ATOM   430  C C   . LEU A 1 94  ? 118.94200 112.11300 81.76200  1.000 39.83479 ? 94  LEU A C   1 
ATOM   431  O O   . LEU A 1 94  ? 119.39600 112.40800 80.65200  1.000 39.83479 ? 94  LEU A O   1 
ATOM   432  C CB  . LEU A 1 94  ? 120.40800 110.73600 83.24800  1.000 39.83479 ? 94  LEU A CB  1 
ATOM   433  C CG  . LEU A 1 94  ? 121.59400 110.62900 84.19600  1.000 39.83479 ? 94  LEU A CG  1 
ATOM   434  C CD1 . LEU A 1 94  ? 121.82900 109.18400 84.56400  1.000 39.83479 ? 94  LEU A CD1 1 
ATOM   435  C CD2 . LEU A 1 94  ? 122.82300 111.23100 83.56800  1.000 39.83479 ? 94  LEU A CD2 1 
ATOM   436  N N   . LEU A 1 95  ? 117.66800 111.75900 81.94000  1.000 42.57524 ? 95  LEU A N   1 
ATOM   437  C CA  . LEU A 1 95  ? 116.70600 111.83100 80.84400  1.000 42.57524 ? 95  LEU A CA  1 
ATOM   438  C C   . LEU A 1 95  ? 116.54900 113.26100 80.34500  1.000 42.57524 ? 95  LEU A C   1 
ATOM   439  O O   . LEU A 1 95  ? 116.49300 113.50300 79.13400  1.000 42.57524 ? 95  LEU A O   1 
ATOM   440  C CB  . LEU A 1 95  ? 115.35500 111.27500 81.29500  1.000 42.57524 ? 95  LEU A CB  1 
ATOM   441  C CG  . LEU A 1 95  ? 115.18100 109.76000 81.39200  1.000 42.57524 ? 95  LEU A CG  1 
ATOM   442  C CD1 . LEU A 1 95  ? 113.72600 109.41300 81.65200  1.000 42.57524 ? 95  LEU A CD1 1 
ATOM   443  C CD2 . LEU A 1 95  ? 115.67300 109.07800 80.13300  1.000 42.57524 ? 95  LEU A CD2 1 
ATOM   444  N N   . LEU A 1 96  ? 116.48000 114.22200 81.26900  1.000 45.28787 ? 96  LEU A N   1 
ATOM   445  C CA  . LEU A 1 96  ? 116.40300 115.63000 80.88900  1.000 45.28787 ? 96  LEU A CA  1 
ATOM   446  C C   . LEU A 1 96  ? 117.65800 116.08600 80.15400  1.000 45.28787 ? 96  LEU A C   1 
ATOM   447  O O   . LEU A 1 96  ? 117.57300 116.83300 79.17500  1.000 45.28787 ? 96  LEU A O   1 
ATOM   448  C CB  . LEU A 1 96  ? 116.17600 116.49200 82.12700  1.000 45.28787 ? 96  LEU A CB  1 
ATOM   449  C CG  . LEU A 1 96  ? 114.73400 116.57900 82.61600  1.000 45.28787 ? 96  LEU A CG  1 
ATOM   450  C CD1 . LEU A 1 96  ? 114.67400 117.33500 83.91600  1.000 45.28787 ? 96  LEU A CD1 1 
ATOM   451  C CD2 . LEU A 1 96  ? 113.85300 117.23300 81.57200  1.000 45.28787 ? 96  LEU A CD2 1 
ATOM   452  N N   . VAL A 1 97  ? 118.83000 115.66300 80.62200  1.000 47.15390 ? 97  VAL A N   1 
ATOM   453  C CA  . VAL A 1 97  ? 120.08000 116.09300 80.00200  1.000 47.15390 ? 97  VAL A CA  1 
ATOM   454  C C   . VAL A 1 97  ? 120.21500 115.50100 78.60400  1.000 47.15390 ? 97  VAL A C   1 
ATOM   455  O O   . VAL A 1 97  ? 120.59300 116.19500 77.65300  1.000 47.15390 ? 97  VAL A O   1 
ATOM   456  C CB  . VAL A 1 97  ? 121.27300 115.72400 80.90300  1.000 47.15390 ? 97  VAL A CB  1 
ATOM   457  C CG1 . VAL A 1 97  ? 122.58400 115.82800 80.14400  1.000 47.15390 ? 97  VAL A CG1 1 
ATOM   458  C CG2 . VAL A 1 97  ? 121.29700 116.62400 82.12000  1.000 47.15390 ? 97  VAL A CG2 1 
ATOM   459  N N   . ALA A 1 98  ? 119.88500 114.21400 78.45300  1.000 47.33582 ? 98  ALA A N   1 
ATOM   460  C CA  . ALA A 1 98  ? 119.89300 113.58300 77.13900  1.000 47.33582 ? 98  ALA A CA  1 
ATOM   461  C C   . ALA A 1 98  ? 118.85400 114.19700 76.21300  1.000 47.33582 ? 98  ALA A C   1 
ATOM   462  O O   . ALA A 1 98  ? 119.05700 114.23100 74.99500  1.000 47.33582 ? 98  ALA A O   1 
ATOM   463  C CB  . ALA A 1 98  ? 119.65200 112.08300 77.27500  1.000 47.33582 ? 98  ALA A CB  1 
ATOM   464  N N   . ALA A 1 99  ? 117.74000 114.67800 76.76500  1.000 49.80951 ? 99  ALA A N   1 
ATOM   465  C CA  . ALA A 1 99  ? 116.75600 115.37600 75.94700  1.000 49.80951 ? 99  ALA A CA  1 
ATOM   466  C C   . ALA A 1 99  ? 117.21900 116.78500 75.60300  1.000 49.80951 ? 99  ALA A C   1 
ATOM   467  O O   . ALA A 1 99  ? 116.94500 117.28200 74.50600  1.000 49.80951 ? 99  ALA A O   1 
ATOM   468  C CB  . ALA A 1 99  ? 115.41100 115.40900 76.66800  1.000 49.80951 ? 99  ALA A CB  1 
ATOM   469  N N   . GLY A 1 100 ? 117.92800 117.43800 76.51600  1.000 52.97576 ? 100 GLY A N   1 
ATOM   470  C CA  . GLY A 1 100 ? 118.34400 118.81300 76.33600  1.000 52.97576 ? 100 GLY A CA  1 
ATOM   471  C C   . GLY A 1 100 ? 117.51000 119.84400 77.06400  1.000 52.97576 ? 100 GLY A C   1 
ATOM   472  O O   . GLY A 1 100 ? 117.73200 121.04200 76.86500  1.000 52.97576 ? 100 GLY A O   1 
ATOM   473  N N   . LEU A 1 101 ? 116.56200 119.42000 77.90100  1.000 53.86398 ? 101 LEU A N   1 
ATOM   474  C CA  . LEU A 1 101 ? 115.65100 120.32300 78.59300  1.000 53.86398 ? 101 LEU A CA  1 
ATOM   475  C C   . LEU A 1 101 ? 115.94100 120.40800 80.08600  1.000 53.86398 ? 101 LEU A C   1 
ATOM   476  O O   . LEU A 1 101 ? 115.03600 120.68900 80.87500  1.000 53.86398 ? 101 LEU A O   1 
ATOM   477  C CB  . LEU A 1 101 ? 114.19000 119.91500 78.37100  1.000 53.86398 ? 101 LEU A CB  1 
ATOM   478  C CG  . LEU A 1 101 ? 113.52500 119.84300 76.98600  1.000 53.86398 ? 101 LEU A CG  1 
ATOM   479  C CD1 . LEU A 1 101 ? 113.61200 121.19400 76.28400  1.000 53.86398 ? 101 LEU A CD1 1 
ATOM   480  C CD2 . LEU A 1 101 ? 114.02600 118.72300 76.08300  1.000 53.86398 ? 101 LEU A CD2 1 
ATOM   481  N N   . GLU A 1 102 ? 117.18500 120.17100 80.48900  1.000 55.03924 ? 102 GLU A N   1 
ATOM   482  C CA  . GLU A 1 102 ? 117.53100 120.18400 81.90200  1.000 55.03924 ? 102 GLU A CA  1 
ATOM   483  C C   . GLU A 1 102 ? 117.54900 121.58600 82.50200  1.000 55.03924 ? 102 GLU A C   1 
ATOM   484  O O   . GLU A 1 102 ? 117.25300 121.72500 83.69100  1.000 55.03924 ? 102 GLU A O   1 
ATOM   485  C CB  . GLU A 1 102 ? 118.88700 119.50100 82.10800  1.000 55.03924 ? 102 GLU A CB  1 
ATOM   486  C CG  . GLU A 1 102 ? 120.08800 120.27200 81.56700  1.000 55.03924 ? 102 GLU A CG  1 
ATOM   487  C CD  . GLU A 1 102 ? 120.27400 120.10800 80.06600  1.000 55.03924 ? 102 GLU A CD  1 
ATOM   488  O OE1 . GLU A 1 102 ? 119.49300 119.36400 79.44400  1.000 55.03924 ? 102 GLU A OE1 1 
ATOM   489  O OE2 . GLU A 1 102 ? 121.19500 120.73400 79.50600  1.000 55.03924 ? 102 GLU A OE2 1 
ATOM   490  N N   . ALA A 1 103 ? 117.84000 122.61800 81.69900  1.000 54.81414 ? 103 ALA A N   1 
ATOM   491  C CA  . ALA A 1 103 ? 118.12500 123.95300 82.23000  1.000 54.81414 ? 103 ALA A CA  1 
ATOM   492  C C   . ALA A 1 103 ? 117.01100 124.55700 83.08400  1.000 54.81414 ? 103 ALA A C   1 
ATOM   493  O O   . ALA A 1 103 ? 117.33400 125.17200 84.11500  1.000 54.81414 ? 103 ALA A O   1 
ATOM   494  C CB  . ALA A 1 103 ? 118.51500 124.89000 81.08200  1.000 54.81414 ? 103 ALA A CB  1 
ATOM   495  N N   . PRO A 1 104 ? 115.71600 124.44200 82.75200  1.000 54.32321 ? 104 PRO A N   1 
ATOM   496  C CA  . PRO A 1 104 ? 114.69500 124.92200 83.70300  1.000 54.32321 ? 104 PRO A CA  1 
ATOM   497  C C   . PRO A 1 104 ? 114.52200 124.04200 84.93800  1.000 54.32321 ? 104 PRO A C   1 
ATOM   498  O O   . PRO A 1 104 ? 113.58800 124.28600 85.71200  1.000 54.32321 ? 104 PRO A O   1 
ATOM   499  C CB  . PRO A 1 104 ? 113.41100 124.94800 82.86600  1.000 54.32321 ? 104 PRO A CB  1 
ATOM   500  C CG  . PRO A 1 104 ? 113.65300 124.02700 81.75600  1.000 54.32321 ? 104 PRO A CG  1 
ATOM   501  C CD  . PRO A 1 104 ? 115.10200 124.09800 81.45200  1.000 54.32321 ? 104 PRO A CD  1 
ATOM   502  N N   . PHE A 1 105 ? 115.36700 123.03400 85.14500  1.000 51.80039 ? 105 PHE A N   1 
ATOM   503  C CA  . PHE A 1 105 ? 115.28500 122.16800 86.31200  1.000 51.80039 ? 105 PHE A CA  1 
ATOM   504  C C   . PHE A 1 105 ? 116.58800 122.09000 87.09400  1.000 51.80039 ? 105 PHE A C   1 
ATOM   505  O O   . PHE A 1 105 ? 116.67300 121.30000 88.04200  1.000 51.80039 ? 105 PHE A O   1 
ATOM   506  C CB  . PHE A 1 105 ? 114.85200 120.75700 85.89700  1.000 51.80039 ? 105 PHE A CB  1 
ATOM   507  C CG  . PHE A 1 105 ? 113.57700 120.72300 85.11500  1.000 51.80039 ? 105 PHE A CG  1 
ATOM   508  C CD1 . PHE A 1 105 ? 113.59400 120.72500 83.73200  1.000 51.80039 ? 105 PHE A CD1 1 
ATOM   509  C CD2 . PHE A 1 105 ? 112.35700 120.68800 85.76300  1.000 51.80039 ? 105 PHE A CD2 1 
ATOM   510  C CE1 . PHE A 1 105 ? 112.42400 120.69400 83.01300  1.000 51.80039 ? 105 PHE A CE1 1 
ATOM   511  C CE2 . PHE A 1 105 ? 111.18200 120.65800 85.04600  1.000 51.80039 ? 105 PHE A CE2 1 
ATOM   512  C CZ  . PHE A 1 105 ? 111.21700 120.66000 83.67000  1.000 51.80039 ? 105 PHE A CZ  1 
ATOM   513  N N   . LEU A 1 106 ? 117.60100 122.87700 86.71800  1.000 50.43847 ? 106 LEU A N   1 
ATOM   514  C CA  . LEU A 1 106 ? 118.87600 122.84700 87.42900  1.000 50.43847 ? 106 LEU A CA  1 
ATOM   515  C C   . LEU A 1 106 ? 118.71800 123.23600 88.89100  1.000 50.43847 ? 106 LEU A C   1 
ATOM   516  O O   . LEU A 1 106 ? 119.31800 122.60600 89.76500  1.000 50.43847 ? 106 LEU A O   1 
ATOM   517  C CB  . LEU A 1 106 ? 119.89800 123.76200 86.75200  1.000 50.43847 ? 106 LEU A CB  1 
ATOM   518  C CG  . LEU A 1 106 ? 120.86000 123.18700 85.71000  1.000 50.43847 ? 106 LEU A CG  1 
ATOM   519  C CD1 . LEU A 1 106 ? 122.00200 122.49100 86.42700  1.000 50.43847 ? 106 LEU A CD1 1 
ATOM   520  C CD2 . LEU A 1 106 ? 120.19200 122.21800 84.77900  1.000 50.43847 ? 106 LEU A CD2 1 
ATOM   521  N N   . TYR A 1 107 ? 117.91700 124.26500 89.17700  1.000 48.02069 ? 107 TYR A N   1 
ATOM   522  C CA  . TYR A 1 107 ? 117.73500 124.69100 90.56100  1.000 48.02069 ? 107 TYR A CA  1 
ATOM   523  C C   . TYR A 1 107 ? 117.05200 123.60800 91.38600  1.000 48.02069 ? 107 TYR A C   1 
ATOM   524  O O   . TYR A 1 107 ? 117.44800 123.34400 92.52500  1.000 48.02069 ? 107 TYR A O   1 
ATOM   525  C CB  . TYR A 1 107 ? 116.95400 126.00800 90.61100  1.000 48.02069 ? 107 TYR A CB  1 
ATOM   526  C CG  . TYR A 1 107 ? 115.46500 125.88600 90.37400  1.000 48.02069 ? 107 TYR A CG  1 
ATOM   527  C CD1 . TYR A 1 107 ? 114.56700 125.88200 91.43800  1.000 48.02069 ? 107 TYR A CD1 1 
ATOM   528  C CD2 . TYR A 1 107 ? 114.95500 125.76400 89.08600  1.000 48.02069 ? 107 TYR A CD2 1 
ATOM   529  C CE1 . TYR A 1 107 ? 113.20600 125.76800 91.22200  1.000 48.02069 ? 107 TYR A CE1 1 
ATOM   530  C CE2 . TYR A 1 107 ? 113.59900 125.64900 88.86400  1.000 48.02069 ? 107 TYR A CE2 1 
ATOM   531  C CZ  . TYR A 1 107 ? 112.73000 125.65200 89.93400  1.000 48.02069 ? 107 TYR A CZ  1 
ATOM   532  O OH  . TYR A 1 107 ? 111.37800 125.53700 89.71100  1.000 48.02069 ? 107 TYR A OH  1 
ATOM   533  N N   . LEU A 1 108 ? 116.05400 122.93800 90.80700  1.000 43.17964 ? 108 LEU A N   1 
ATOM   534  C CA  . LEU A 1 108 ? 115.33900 121.88600 91.52000  1.000 43.17964 ? 108 LEU A CA  1 
ATOM   535  C C   . LEU A 1 108 ? 116.24400 120.69100 91.79500  1.000 43.17964 ? 108 LEU A C   1 
ATOM   536  O O   . LEU A 1 108 ? 116.25500 120.14500 92.90500  1.000 43.17964 ? 108 LEU A O   1 
ATOM   537  C CB  . LEU A 1 108 ? 114.11500 121.46700 90.70900  1.000 43.17964 ? 108 LEU A CB  1 
ATOM   538  C CG  . LEU A 1 108 ? 112.84000 121.09500 91.45700  1.000 43.17964 ? 108 LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 108 ? 112.41800 122.22300 92.37900  1.000 43.17964 ? 108 LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 108 ? 111.74500 120.79300 90.46000  1.000 43.17964 ? 108 LEU A CD2 1 
ATOM   541  N N   . TYR A 1 109 ? 117.03400 120.28500 90.80000  1.000 40.19823 ? 109 TYR A N   1 
ATOM   542  C CA  . TYR A 1 109 ? 117.88500 119.11500 90.98800  1.000 40.19823 ? 109 TYR A CA  1 
ATOM   543  C C   . TYR A 1 109 ? 119.05400 119.42200 91.91300  1.000 40.19823 ? 109 TYR A C   1 
ATOM   544  O O   . TYR A 1 109 ? 119.44000 118.58100 92.73200  1.000 40.19823 ? 109 TYR A O   1 
ATOM   545  C CB  . TYR A 1 109 ? 118.36300 118.58700 89.63800  1.000 40.19823 ? 109 TYR A CB  1 
ATOM   546  C CG  . TYR A 1 109 ? 117.32600 117.71900 88.98100  1.000 40.19823 ? 109 TYR A CG  1 
ATOM   547  C CD1 . TYR A 1 109 ? 117.08800 116.43300 89.43600  1.000 40.19823 ? 109 TYR A CD1 1 
ATOM   548  C CD2 . TYR A 1 109 ? 116.56000 118.19400 87.92900  1.000 40.19823 ? 109 TYR A CD2 1 
ATOM   549  C CE1 . TYR A 1 109 ? 116.12700 115.64200 88.85200  1.000 40.19823 ? 109 TYR A CE1 1 
ATOM   550  C CE2 . TYR A 1 109 ? 115.59600 117.40800 87.34000  1.000 40.19823 ? 109 TYR A CE2 1 
ATOM   551  C CZ  . TYR A 1 109 ? 115.38700 116.13300 87.80300  1.000 40.19823 ? 109 TYR A CZ  1 
ATOM   552  O OH  . TYR A 1 109 ? 114.43300 115.34100 87.22000  1.000 40.19823 ? 109 TYR A OH  1 
ATOM   553  N N   . ALA A 1 110 ? 119.60800 120.63300 91.82000  1.000 38.96825 ? 110 ALA A N   1 
ATOM   554  C CA  . ALA A 1 110 ? 120.62900 121.07000 92.76400  1.000 38.96825 ? 110 ALA A CA  1 
ATOM   555  C C   . ALA A 1 110 ? 120.08000 121.11000 94.18200  1.000 38.96825 ? 110 ALA A C   1 
ATOM   556  O O   . ALA A 1 110 ? 120.77400 120.74400 95.13600  1.000 38.96825 ? 110 ALA A O   1 
ATOM   557  C CB  . ALA A 1 110 ? 121.16200 122.44100 92.35200  1.000 38.96825 ? 110 ALA A CB  1 
ATOM   558  N N   . LEU A 1 111 ? 118.82600 121.54300 94.33800  1.000 38.70361 ? 111 LEU A N   1 
ATOM   559  C CA  . LEU A 1 111 ? 118.19100 121.53100 95.65000  1.000 38.70361 ? 111 LEU A CA  1 
ATOM   560  C C   . LEU A 1 111 ? 118.05100 120.11000 96.18500  1.000 38.70361 ? 111 LEU A C   1 
ATOM   561  O O   . LEU A 1 111 ? 118.31700 119.85700 97.36500  1.000 38.70361 ? 111 LEU A O   1 
ATOM   562  C CB  . LEU A 1 111 ? 116.83000 122.22100 95.57400  1.000 38.70361 ? 111 LEU A CB  1 
ATOM   563  C CG  . LEU A 1 111 ? 116.02900 122.32400 96.86900  1.000 38.70361 ? 111 LEU A CG  1 
ATOM   564  C CD1 . LEU A 1 111 ? 116.84400 123.00100 97.95700  1.000 38.70361 ? 111 LEU A CD1 1 
ATOM   565  C CD2 . LEU A 1 111 ? 114.74600 123.07800 96.62200  1.000 38.70361 ? 111 LEU A CD2 1 
ATOM   566  N N   . VAL A 1 112 ? 117.64700 119.16700 95.32500  1.000 36.71357 ? 112 VAL A N   1 
ATOM   567  C CA  . VAL A 1 112 ? 117.53900 117.77000 95.75200  1.000 36.71357 ? 112 VAL A CA  1 
ATOM   568  C C   . VAL A 1 112 ? 118.89400 117.24300 96.20100  1.000 36.71357 ? 112 VAL A C   1 
ATOM   569  O O   . VAL A 1 112 ? 119.01100 116.58900 97.24300  1.000 36.71357 ? 112 VAL A O   1 
ATOM   570  C CB  . VAL A 1 112 ? 116.96300 116.88600 94.63100  1.000 36.71357 ? 112 VAL A CB  1 
ATOM   571  C CG1 . VAL A 1 112 ? 116.98200 115.43200 95.06400  1.000 36.71357 ? 112 VAL A CG1 1 
ATOM   572  C CG2 . VAL A 1 112 ? 115.57000 117.28700 94.29400  1.000 36.71357 ? 112 VAL A CG2 1 
ATOM   573  N N   . TYR A 1 113 ? 119.93700 117.51900 95.41700  1.000 36.36656 ? 113 TYR A N   1 
ATOM   574  C CA  . TYR A 1 113 ? 121.25800 116.99300 95.73900  1.000 36.36656 ? 113 TYR A CA  1 
ATOM   575  C C   . TYR A 1 113 ? 121.80400 117.61700 97.01600  1.000 36.36656 ? 113 TYR A C   1 
ATOM   576  O O   . TYR A 1 113 ? 122.46300 116.94100 97.81200  1.000 36.36656 ? 113 TYR A O   1 
ATOM   577  C CB  . TYR A 1 113 ? 122.21200 117.20900 94.56600  1.000 36.36656 ? 113 TYR A CB  1 
ATOM   578  C CG  . TYR A 1 113 ? 121.77900 116.50100 93.30800  1.000 36.36656 ? 113 TYR A CG  1 
ATOM   579  C CD1 . TYR A 1 113 ? 121.11500 115.28200 93.37000  1.000 36.36656 ? 113 TYR A CD1 1 
ATOM   580  C CD2 . TYR A 1 113 ? 122.02900 117.04700 92.05800  1.000 36.36656 ? 113 TYR A CD2 1 
ATOM   581  C CE1 . TYR A 1 113 ? 120.70800 114.63500 92.22800  1.000 36.36656 ? 113 TYR A CE1 1 
ATOM   582  C CE2 . TYR A 1 113 ? 121.62500 116.40500 90.91100  1.000 36.36656 ? 113 TYR A CE2 1 
ATOM   583  C CZ  . TYR A 1 113 ? 120.96700 115.19800 91.00100  1.000 36.36656 ? 113 TYR A CZ  1 
ATOM   584  O OH  . TYR A 1 113 ? 120.56800 114.55100 89.86000  1.000 36.36656 ? 113 TYR A OH  1 
ATOM   585  N N   . PHE A 1 114 ? 121.50600 118.89500 97.24800  1.000 37.57555 ? 114 PHE A N   1 
ATOM   586  C CA  . PHE A 1 114 ? 121.92700 119.55600 98.47900  1.000 37.57555 ? 114 PHE A CA  1 
ATOM   587  C C   . PHE A 1 114 ? 121.22300 118.96600 99.69800  1.000 37.57555 ? 114 PHE A C   1 
ATOM   588  O O   . PHE A 1 114 ? 121.85700 118.68400 100.72600 1.000 37.57555 ? 114 PHE A O   1 
ATOM   589  C CB  . PHE A 1 114 ? 121.66200 121.05600 98.35600  1.000 37.57555 ? 114 PHE A CB  1 
ATOM   590  C CG  . PHE A 1 114 ? 121.94400 121.82900 99.60100  1.000 37.57555 ? 114 PHE A CG  1 
ATOM   591  C CD1 . PHE A 1 114 ? 120.91200 122.39000 100.32600 1.000 37.57555 ? 114 PHE A CD1 1 
ATOM   592  C CD2 . PHE A 1 114 ? 123.24100 122.00400 100.04500 1.000 37.57555 ? 114 PHE A CD2 1 
ATOM   593  C CE1 . PHE A 1 114 ? 121.16800 123.11200 101.47000 1.000 37.57555 ? 114 PHE A CE1 1 
ATOM   594  C CE2 . PHE A 1 114 ? 123.50300 122.72100 101.19300 1.000 37.57555 ? 114 PHE A CE2 1 
ATOM   595  C CZ  . PHE A 1 114 ? 122.46600 123.27400 101.90600 1.000 37.57555 ? 114 PHE A CZ  1 
ATOM   596  N N   . LEU A 1 115 ? 119.90900 118.75200 99.59600  1.000 37.68230 ? 115 LEU A N   1 
ATOM   597  C CA  . LEU A 1 115 ? 119.17800 118.17200 100.71800 1.000 37.68230 ? 115 LEU A CA  1 
ATOM   598  C C   . LEU A 1 115 ? 119.61000 116.73100 100.97300 1.000 37.68230 ? 115 LEU A C   1 
ATOM   599  O O   . LEU A 1 115 ? 119.66500 116.28500 102.12400 1.000 37.68230 ? 115 LEU A O   1 
ATOM   600  C CB  . LEU A 1 115 ? 117.67300 118.25300 100.46900 1.000 37.68230 ? 115 LEU A CB  1 
ATOM   601  C CG  . LEU A 1 115 ? 117.05100 119.63900 100.26400 1.000 37.68230 ? 115 LEU A CG  1 
ATOM   602  C CD1 . LEU A 1 115 ? 115.59300 119.52900 99.86700  1.000 37.68230 ? 115 LEU A CD1 1 
ATOM   603  C CD2 . LEU A 1 115 ? 117.21200 120.52600 101.48200 1.000 37.68230 ? 115 LEU A CD2 1 
ATOM   604  N N   . GLN A 1 116 ? 119.94500 115.99300 99.91300  1.000 38.20323 ? 116 GLN A N   1 
ATOM   605  C CA  . GLN A 1 116 ? 120.40700 114.62000 100.08300 1.000 38.20323 ? 116 GLN A CA  1 
ATOM   606  C C   . GLN A 1 116 ? 121.80600 114.57500 100.68500 1.000 38.20323 ? 116 GLN A C   1 
ATOM   607  O O   . GLN A 1 116 ? 122.13100 113.65500 101.43800 1.000 38.20323 ? 116 GLN A O   1 
ATOM   608  C CB  . GLN A 1 116 ? 120.36800 113.88400 98.74600  1.000 38.20323 ? 116 GLN A CB  1 
ATOM   609  C CG  . GLN A 1 116 ? 118.98300 113.43000 98.34600  1.000 38.20323 ? 116 GLN A CG  1 
ATOM   610  C CD  . GLN A 1 116 ? 118.41800 112.39100 99.28400  1.000 38.20323 ? 116 GLN A CD  1 
ATOM   611  O OE1 . GLN A 1 116 ? 119.08700 111.41900 99.62600  1.000 38.20323 ? 116 GLN A OE1 1 
ATOM   612  N NE2 . GLN A 1 116 ? 117.17900 112.58800 99.70600  1.000 38.20323 ? 116 GLN A NE2 1 
ATOM   613  N N   . SER A 1 117 ? 122.64700 115.56100 100.36600 1.000 37.81575 ? 117 SER A N   1 
ATOM   614  C CA  . SER A 1 117 ? 123.93700 115.68200 101.03800 1.000 37.81575 ? 117 SER A CA  1 
ATOM   615  C C   . SER A 1 117 ? 123.75200 115.93900 102.52900 1.000 37.81575 ? 117 SER A C   1 
ATOM   616  O O   . SER A 1 117 ? 124.46600 115.37000 103.36700 1.000 37.81575 ? 117 SER A O   1 
ATOM   617  C CB  . SER A 1 117 ? 124.75700 116.80000 100.39900 1.000 37.81575 ? 117 SER A CB  1 
ATOM   618  O OG  . SER A 1 117 ? 125.48700 116.32000 99.29100  1.000 37.81575 ? 117 SER A OG  1 
ATOM   619  N N   . ILE A 1 118 ? 122.79100 116.80000 102.87400 1.000 38.07588 ? 118 ILE A N   1 
ATOM   620  C CA  . ILE A 1 118 ? 122.48400 117.04300 104.28300 1.000 38.07588 ? 118 ILE A CA  1 
ATOM   621  C C   . ILE A 1 118 ? 122.00800 115.76100 104.95700 1.000 38.07588 ? 118 ILE A C   1 
ATOM   622  O O   . ILE A 1 118 ? 122.38700 115.46000 106.09400 1.000 38.07588 ? 118 ILE A O   1 
ATOM   623  C CB  . ILE A 1 118 ? 121.45200 118.17900 104.41800 1.000 38.07588 ? 118 ILE A CB  1 
ATOM   624  C CG1 . ILE A 1 118 ? 122.06000 119.50100 103.96100 1.000 38.07588 ? 118 ILE A CG1 1 
ATOM   625  C CG2 . ILE A 1 118 ? 120.96900 118.30800 105.84900 1.000 38.07588 ? 118 ILE A CG2 1 
ATOM   626  C CD1 . ILE A 1 118 ? 121.09800 120.64600 104.00800 1.000 38.07588 ? 118 ILE A CD1 1 
ATOM   627  N N   . ASN A 1 119 ? 121.17800 114.98200 104.26300 1.000 38.82168 ? 119 ASN A N   1 
ATOM   628  C CA  . ASN A 1 119 ? 120.69200 113.72500 104.82500 1.000 38.82168 ? 119 ASN A CA  1 
ATOM   629  C C   . ASN A 1 119 ? 121.82100 112.71400 105.00600 1.000 38.82168 ? 119 ASN A C   1 
ATOM   630  O O   . ASN A 1 119 ? 121.82500 111.94300 105.97300 1.000 38.82168 ? 119 ASN A O   1 
ATOM   631  C CB  . ASN A 1 119 ? 119.59300 113.15400 103.93800 1.000 38.82168 ? 119 ASN A CB  1 
ATOM   632  C CG  . ASN A 1 119 ? 119.01900 111.87100 104.48000 1.000 38.82168 ? 119 ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 119 ? 118.49700 111.83300 105.58700 1.000 38.82168 ? 119 ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 119 ? 119.10600 110.81000 103.69600 1.000 38.82168 ? 119 ASN A ND2 1 
ATOM   635  N N   . PHE A 1 120 ? 122.78100 112.69800 104.08100 1.000 37.81955 ? 120 PHE A N   1 
ATOM   636  C CA  . PHE A 1 120 ? 123.95700 111.84900 104.23200 1.000 37.81955 ? 120 PHE A CA  1 
ATOM   637  C C   . PHE A 1 120 ? 124.75900 112.23300 105.47100 1.000 37.81955 ? 120 PHE A C   1 
ATOM   638  O O   . PHE A 1 120 ? 125.19400 111.36500 106.24000 1.000 37.81955 ? 120 PHE A O   1 
ATOM   639  C CB  . PHE A 1 120 ? 124.82400 111.94100 102.97900 1.000 37.81955 ? 120 PHE A CB  1 
ATOM   640  C CG  . PHE A 1 120 ? 126.09500 111.15000 103.06500 1.000 37.81955 ? 120 PHE A CG  1 
ATOM   641  C CD1 . PHE A 1 120 ? 126.06800 109.76700 103.04100 1.000 37.81955 ? 120 PHE A CD1 1 
ATOM   642  C CD2 . PHE A 1 120 ? 127.31500 111.79100 103.18000 1.000 37.81955 ? 120 PHE A CD2 1 
ATOM   643  C CE1 . PHE A 1 120 ? 127.23700 109.03700 103.12200 1.000 37.81955 ? 120 PHE A CE1 1 
ATOM   644  C CE2 . PHE A 1 120 ? 128.48600 111.06700 103.26200 1.000 37.81955 ? 120 PHE A CE2 1 
ATOM   645  C CZ  . PHE A 1 120 ? 128.44700 109.68800 103.23300 1.000 37.81955 ? 120 PHE A CZ  1 
ATOM   646  N N   . VAL A 1 121 ? 124.96100 113.53800 105.67900 1.000 37.70209 ? 121 VAL A N   1 
ATOM   647  C CA  . VAL A 1 121 ? 125.65100 114.00600 106.88000 1.000 37.70209 ? 121 VAL A CA  1 
ATOM   648  C C   . VAL A 1 121 ? 124.87400 113.61100 108.13400 1.000 37.70209 ? 121 VAL A C   1 
ATOM   649  O O   . VAL A 1 121 ? 125.46000 113.22300 109.15100 1.000 37.70209 ? 121 VAL A O   1 
ATOM   650  C CB  . VAL A 1 121 ? 125.88200 115.52700 106.80400 1.000 37.70209 ? 121 VAL A CB  1 
ATOM   651  C CG1 . VAL A 1 121 ? 126.44300 116.06000 108.10800 1.000 37.70209 ? 121 VAL A CG1 1 
ATOM   652  C CG2 . VAL A 1 121 ? 126.82000 115.85400 105.66600 1.000 37.70209 ? 121 VAL A CG2 1 
ATOM   653  N N   . ARG A 1 122 ? 123.54400 113.68500 108.07100 1.000 40.99010 ? 122 ARG A N   1 
ATOM   654  C CA  . ARG A 1 122 ? 122.71500 113.29500 109.20700 1.000 40.99010 ? 122 ARG A CA  1 
ATOM   655  C C   . ARG A 1 122 ? 122.85200 111.80800 109.51700 1.000 40.99010 ? 122 ARG A C   1 
ATOM   656  O O   . ARG A 1 122 ? 122.87300 111.41000 110.68500 1.000 40.99010 ? 122 ARG A O   1 
ATOM   657  C CB  . ARG A 1 122 ? 121.25700 113.65200 108.93100 1.000 40.99010 ? 122 ARG A CB  1 
ATOM   658  C CG  . ARG A 1 122 ? 120.30100 113.25700 110.03200 1.000 40.99010 ? 122 ARG A CG  1 
ATOM   659  C CD  . ARG A 1 122 ? 118.87200 113.27100 109.54800 1.000 40.99010 ? 122 ARG A CD  1 
ATOM   660  N NE  . ARG A 1 122 ? 118.62800 112.25700 108.52900 1.000 40.99010 ? 122 ARG A NE  1 
ATOM   661  C CZ  . ARG A 1 122 ? 118.33000 110.99000 108.79200 1.000 40.99010 ? 122 ARG A CZ  1 
ATOM   662  N NH1 . ARG A 1 122 ? 118.24400 110.57500 110.04600 1.000 40.99010 ? 122 ARG A NH1 1 
ATOM   663  N NH2 . ARG A 1 122 ? 118.12000 110.13800 107.80200 1.000 40.99010 ? 122 ARG A NH2 1 
ATOM   664  N N   . ILE A 1 123 ? 122.93700 110.97200 108.48200 1.000 38.91934 ? 123 ILE A N   1 
ATOM   665  C CA  . ILE A 1 123 ? 123.11700 109.53700 108.69100 1.000 38.91934 ? 123 ILE A CA  1 
ATOM   666  C C   . ILE A 1 123 ? 124.48700 109.25300 109.30200 1.000 38.91934 ? 123 ILE A C   1 
ATOM   667  O O   . ILE A 1 123 ? 124.63000 108.38400 110.17300 1.000 38.91934 ? 123 ILE A O   1 
ATOM   668  C CB  . ILE A 1 123 ? 122.89900 108.78100 107.36600 1.000 38.91934 ? 123 ILE A CB  1 
ATOM   669  C CG1 . ILE A 1 123 ? 121.40400 108.62300 107.09400 1.000 38.91934 ? 123 ILE A CG1 1 
ATOM   670  C CG2 . ILE A 1 123 ? 123.56200 107.41600 107.38100 1.000 38.91934 ? 123 ILE A CG2 1 
ATOM   671  C CD1 . ILE A 1 123 ? 121.07900 108.31000 105.65900 1.000 38.91934 ? 123 ILE A CD1 1 
ATOM   672  N N   . ILE A 1 124 ? 125.50900 110.00000 108.87500 1.000 38.73273 ? 124 ILE A N   1 
ATOM   673  C CA  . ILE A 1 124 ? 126.83500 109.86200 109.47800 1.000 38.73273 ? 124 ILE A CA  1 
ATOM   674  C C   . ILE A 1 124 ? 126.79200 110.23900 110.95700 1.000 38.73273 ? 124 ILE A C   1 
ATOM   675  O O   . ILE A 1 124 ? 127.37900 109.56000 111.80800 1.000 38.73273 ? 124 ILE A O   1 
ATOM   676  C CB  . ILE A 1 124 ? 127.87200 110.70600 108.71200 1.000 38.73273 ? 124 ILE A CB  1 
ATOM   677  C CG1 . ILE A 1 124 ? 128.01600 110.21800 107.27000 1.000 38.73273 ? 124 ILE A CG1 1 
ATOM   678  C CG2 . ILE A 1 124 ? 129.22000 110.67600 109.41000 1.000 38.73273 ? 124 ILE A CG2 1 
ATOM   679  C CD1 . ILE A 1 124 ? 128.30600 108.74800 107.14600 1.000 38.73273 ? 124 ILE A CD1 1 
ATOM   680  N N   . MET A 1 125 ? 126.09300 111.32900 111.28400 1.000 41.36569 ? 125 MET A N   1 
ATOM   681  C CA  . MET A 1 125 ? 125.97200 111.73300 112.68300 1.000 41.36569 ? 125 MET A CA  1 
ATOM   682  C C   . MET A 1 125 ? 125.18300 110.71200 113.49500 1.000 41.36569 ? 125 MET A C   1 
ATOM   683  O O   . MET A 1 125 ? 125.47200 110.49500 114.67400 1.000 41.36569 ? 125 MET A O   1 
ATOM   684  C CB  . MET A 1 125 ? 125.33100 113.11600 112.79600 1.000 41.36569 ? 125 MET A CB  1 
ATOM   685  C CG  . MET A 1 125 ? 126.12000 114.23500 112.14100 1.000 41.36569 ? 125 MET A CG  1 
ATOM   686  S SD  . MET A 1 125 ? 127.57700 114.83400 113.03300 1.000 41.36569 ? 125 MET A SD  1 
ATOM   687  C CE  . MET A 1 125 ? 127.22200 114.40600 114.74400 1.000 41.36569 ? 125 MET A CE  1 
ATOM   688  N N   . ARG A 1 126 ? 124.18800 110.07300 112.88000 1.000 36.50458 ? 126 ARG A N   1 
ATOM   689  C CA  . ARG A 1 126 ? 123.45500 109.00900 113.55700 1.000 36.50458 ? 126 ARG A CA  1 
ATOM   690  C C   . ARG A 1 126 ? 124.35400 107.81200 113.85200 1.000 36.50458 ? 126 ARG A C   1 
ATOM   691  O O   . ARG A 1 126 ? 124.27500 107.21500 114.93200 1.000 36.50458 ? 126 ARG A O   1 
ATOM   692  C CB  . ARG A 1 126 ? 122.25600 108.58700 112.71300 1.000 36.50458 ? 126 ARG A CB  1 
ATOM   693  C CG  . ARG A 1 126 ? 121.06900 108.11400 113.51600 1.000 36.50458 ? 126 ARG A CG  1 
ATOM   694  C CD  . ARG A 1 126 ? 120.42800 109.25600 114.27400 1.000 36.50458 ? 126 ARG A CD  1 
ATOM   695  N NE  . ARG A 1 126 ? 119.36400 108.79800 115.15800 1.000 36.50458 ? 126 ARG A NE  1 
ATOM   696  C CZ  . ARG A 1 126 ? 118.66200 109.58900 115.95900 1.000 36.50458 ? 126 ARG A CZ  1 
ATOM   697  N NH1 . ARG A 1 126 ? 118.90500 110.88700 115.99300 1.000 36.50458 ? 126 ARG A NH1 1 
ATOM   698  N NH2 . ARG A 1 126 ? 117.71200 109.07800 116.72100 1.000 36.50458 ? 126 ARG A NH2 1 
ATOM   699  N N   . LEU A 1 127 ? 125.21800 107.45000 112.90100 1.000 36.90352 ? 127 LEU A N   1 
ATOM   700  C CA  . LEU A 1 127 ? 126.16700 106.36500 113.13700 1.000 36.90352 ? 127 LEU A CA  1 
ATOM   701  C C   . LEU A 1 127 ? 127.16000 106.72900 114.23200 1.000 36.90352 ? 127 LEU A C   1 
ATOM   702  O O   . LEU A 1 127 ? 127.55300 105.87900 115.04000 1.000 36.90352 ? 127 LEU A O   1 
ATOM   703  C CB  . LEU A 1 127 ? 126.90700 106.01900 111.84700 1.000 36.90352 ? 127 LEU A CB  1 
ATOM   704  C CG  . LEU A 1 127 ? 126.07200 105.33600 110.76800 1.000 36.90352 ? 127 LEU A CG  1 
ATOM   705  C CD1 . LEU A 1 127 ? 126.86700 105.21000 109.48600 1.000 36.90352 ? 127 LEU A CD1 1 
ATOM   706  C CD2 . LEU A 1 127 ? 125.59500 103.98100 111.24600 1.000 36.90352 ? 127 LEU A CD2 1 
ATOM   707  N N   . TRP A 1 128 ? 127.57500 107.99200 114.27500 1.000 40.80127 ? 128 TRP A N   1 
ATOM   708  C CA  . TRP A 1 128 ? 128.49500 108.41800 115.32000 1.000 40.80127 ? 128 TRP A CA  1 
ATOM   709  C C   . TRP A 1 128 ? 127.80700 108.44400 116.68200 1.000 40.80127 ? 128 TRP A C   1 
ATOM   710  O O   . TRP A 1 128 ? 128.44300 108.20600 117.71400 1.000 40.80127 ? 128 TRP A O   1 
ATOM   711  C CB  . TRP A 1 128 ? 129.07800 109.78500 114.97200 1.000 40.80127 ? 128 TRP A CB  1 
ATOM   712  C CG  . TRP A 1 128 ? 130.06500 110.24300 115.96500 1.000 40.80127 ? 128 TRP A CG  1 
ATOM   713  C CD1 . TRP A 1 128 ? 131.39900 109.97100 115.96700 1.000 40.80127 ? 128 TRP A CD1 1 
ATOM   714  C CD2 . TRP A 1 128 ? 129.81900 111.05400 117.11100 1.000 40.80127 ? 128 TRP A CD2 1 
ATOM   715  N NE1 . TRP A 1 128 ? 131.99900 110.55700 117.04700 1.000 40.80127 ? 128 TRP A NE1 1 
ATOM   716  C CE2 . TRP A 1 128 ? 131.05000 111.22900 117.76600 1.000 40.80127 ? 128 TRP A CE2 1 
ATOM   717  C CE3 . TRP A 1 128 ? 128.67600 111.64400 117.65200 1.000 40.80127 ? 128 TRP A CE3 1 
ATOM   718  C CZ2 . TRP A 1 128 ? 131.17300 111.97100 118.92600 1.000 40.80127 ? 128 TRP A CZ2 1 
ATOM   719  C CZ3 . TRP A 1 128 ? 128.80100 112.37600 118.80300 1.000 40.80127 ? 128 TRP A CZ3 1 
ATOM   720  C CH2 . TRP A 1 128 ? 130.04200 112.53500 119.42800 1.000 40.80127 ? 128 TRP A CH2 1 
ATOM   721  N N   . LEU A 1 129 ? 126.50900 108.75300 116.70400 1.000 36.45152 ? 129 LEU A N   1 
ATOM   722  C CA  . LEU A 1 129 ? 125.73300 108.65800 117.93500 1.000 36.45152 ? 129 LEU A CA  1 
ATOM   723  C C   . LEU A 1 129 ? 125.61000 107.21200 118.39000 1.000 36.45152 ? 129 LEU A C   1 
ATOM   724  O O   . LEU A 1 129 ? 125.63300 106.92800 119.59100 1.000 36.45152 ? 129 LEU A O   1 
ATOM   725  C CB  . LEU A 1 129 ? 124.35300 109.28000 117.73000 1.000 36.45152 ? 129 LEU A CB  1 
ATOM   726  C CG  . LEU A 1 129 ? 123.51300 109.66000 118.95000 1.000 36.45152 ? 129 LEU A CG  1 
ATOM   727  C CD1 . LEU A 1 129 ? 124.31400 110.49100 119.93100 1.000 36.45152 ? 129 LEU A CD1 1 
ATOM   728  C CD2 . LEU A 1 129 ? 122.26200 110.40200 118.50900 1.000 36.45152 ? 129 LEU A CD2 1 
ATOM   729  N N   . CYS A 1 130 ? 125.46700 106.28700 117.44100 1.000 35.02414 ? 130 CYS A N   1 
ATOM   730  C CA  . CYS A 1 130 ? 125.50500 104.86800 117.77600 1.000 35.02414 ? 130 CYS A CA  1 
ATOM   731  C C   . CYS A 1 130 ? 126.84200 104.47000 118.37900 1.000 35.02414 ? 130 CYS A C   1 
ATOM   732  O O   . CYS A 1 130 ? 126.88300 103.70300 119.34500 1.000 35.02414 ? 130 CYS A O   1 
ATOM   733  C CB  . CYS A 1 130 ? 125.21900 104.01800 116.54000 1.000 35.02414 ? 130 CYS A CB  1 
ATOM   734  S SG  . CYS A 1 130 ? 123.51000 104.01100 116.04600 1.000 35.02414 ? 130 CYS A SG  1 
ATOM   735  N N   . TRP A 1 131 ? 127.94000 104.96600 117.81400 1.000 35.21376 ? 131 TRP A N   1 
ATOM   736  C CA  . TRP A 1 131 ? 129.25800 104.69500 118.37600 1.000 35.21376 ? 131 TRP A CA  1 
ATOM   737  C C   . TRP A 1 131 ? 129.40600 105.27600 119.78100 1.000 35.21376 ? 131 TRP A C   1 
ATOM   738  O O   . TRP A 1 131 ? 129.95200 104.61800 120.67200 1.000 35.21376 ? 131 TRP A O   1 
ATOM   739  C CB  . TRP A 1 131 ? 130.34800 105.24900 117.45700 1.000 35.21376 ? 131 TRP A CB  1 
ATOM   740  C CG  . TRP A 1 131 ? 131.70200 105.25600 118.08500 1.000 35.21376 ? 131 TRP A CG  1 
ATOM   741  C CD1 . TRP A 1 131 ? 132.60600 104.24200 118.07900 1.000 35.21376 ? 131 TRP A CD1 1 
ATOM   742  C CD2 . TRP A 1 131 ? 132.30900 106.32900 118.81000 1.000 35.21376 ? 131 TRP A CD2 1 
ATOM   743  N NE1 . TRP A 1 131 ? 133.73600 104.61000 118.75800 1.000 35.21376 ? 131 TRP A NE1 1 
ATOM   744  C CE2 . TRP A 1 131 ? 133.57700 105.88700 119.22200 1.000 35.21376 ? 131 TRP A CE2 1 
ATOM   745  C CE3 . TRP A 1 131 ? 131.89900 107.61900 119.15800 1.000 35.21376 ? 131 TRP A CE3 1 
ATOM   746  C CZ2 . TRP A 1 131 ? 134.44300 106.68900 119.95500 1.000 35.21376 ? 131 TRP A CZ2 1 
ATOM   747  C CZ3 . TRP A 1 131 ? 132.75400 108.40900 119.89100 1.000 35.21376 ? 131 TRP A CZ3 1 
ATOM   748  C CH2 . TRP A 1 131 ? 134.01400 107.94500 120.28000 1.000 35.21376 ? 131 TRP A CH2 1 
ATOM   749  N N   . LYS A 1 132 ? 128.93900 106.50600 119.99000 1.000 36.61718 ? 132 LYS A N   1 
ATOM   750  C CA  . LYS A 1 132 ? 129.07700 107.14000 121.29600 1.000 36.61718 ? 132 LYS A CA  1 
ATOM   751  C C   . LYS A 1 132 ? 128.19800 106.46600 122.34300 1.000 36.61718 ? 132 LYS A C   1 
ATOM   752  O O   . LYS A 1 132 ? 128.62900 106.25700 123.48200 1.000 36.61718 ? 132 LYS A O   1 
ATOM   753  C CB  . LYS A 1 132 ? 128.73900 108.62600 121.20000 1.000 36.61718 ? 132 LYS A CB  1 
ATOM   754  C CG  . LYS A 1 132 ? 128.93900 109.34200 122.50100 1.000 36.61718 ? 132 LYS A CG  1 
ATOM   755  C CD  . LYS A 1 132 ? 127.92000 110.43200 122.69100 1.000 36.61718 ? 132 LYS A CD  1 
ATOM   756  C CE  . LYS A 1 132 ? 128.42400 111.80900 122.32900 1.000 36.61718 ? 132 LYS A CE  1 
ATOM   757  N NZ  . LYS A 1 132 ? 127.31000 112.77800 122.13600 1.000 36.61718 ? 132 LYS A NZ  1 
ATOM   758  N N   . CYS A 1 133 ? 126.96900 106.11500 121.97800 1.000 35.80336 ? 133 CYS A N   1 
ATOM   759  C CA  . CYS A 1 133 ? 126.06900 105.43400 122.89500 1.000 35.80336 ? 133 CYS A CA  1 
ATOM   760  C C   . CYS A 1 133 ? 126.40400 103.96100 123.07200 1.000 35.80336 ? 133 CYS A C   1 
ATOM   761  O O   . CYS A 1 133 ? 125.80800 103.31900 123.94200 1.000 35.80336 ? 133 CYS A O   1 
ATOM   762  C CB  . CYS A 1 133 ? 124.62100 105.57900 122.42100 1.000 35.80336 ? 133 CYS A CB  1 
ATOM   763  S SG  . CYS A 1 133 ? 124.02000 107.28100 122.34500 1.000 35.80336 ? 133 CYS A SG  1 
ATOM   764  N N   . ARG A 1 134 ? 127.34400 103.42900 122.28500 1.000 36.40386 ? 134 ARG A N   1 
ATOM   765  C CA  . ARG A 1 134 ? 127.71800 102.01100 122.29100 1.000 36.40386 ? 134 ARG A CA  1 
ATOM   766  C C   . ARG A 1 134 ? 126.49900 101.11600 122.09400 1.000 36.40386 ? 134 ARG A C   1 
ATOM   767  O O   . ARG A 1 134 ? 126.35300 100.07300 122.72900 1.000 36.40386 ? 134 ARG A O   1 
ATOM   768  C CB  . ARG A 1 134 ? 128.47700 101.63700 123.56700 1.000 36.40386 ? 134 ARG A CB  1 
ATOM   769  C CG  . ARG A 1 134 ? 129.45000 102.69500 124.04700 1.000 36.40386 ? 134 ARG A CG  1 
ATOM   770  C CD  . ARG A 1 134 ? 130.88400 102.22900 123.93600 1.000 36.40386 ? 134 ARG A CD  1 
ATOM   771  N NE  . ARG A 1 134 ? 131.09500 100.94100 124.58600 1.000 36.40386 ? 134 ARG A NE  1 
ATOM   772  C CZ  . ARG A 1 134 ? 131.42700 100.79200 125.86400 1.000 36.40386 ? 134 ARG A CZ  1 
ATOM   773  N NH1 . ARG A 1 134 ? 131.58100 101.85600 126.64000 1.000 36.40386 ? 134 ARG A NH1 1 
ATOM   774  N NH2 . ARG A 1 134 ? 131.59800 99.57900  126.36700 1.000 36.40386 ? 134 ARG A NH2 1 
ATOM   775  N N   . SER A 1 135 ? 125.61700 101.53200 121.19100 1.000 33.47925 ? 135 SER A N   1 
ATOM   776  C CA  . SER A 1 135 ? 124.33600 100.87800 121.00200 1.000 33.47925 ? 135 SER A CA  1 
ATOM   777  C C   . SER A 1 135 ? 123.86600 101.10800 119.57500 1.000 33.47925 ? 135 SER A C   1 
ATOM   778  O O   . SER A 1 135 ? 124.28500 102.05400 118.91200 1.000 33.47925 ? 135 SER A O   1 
ATOM   779  C CB  . SER A 1 135 ? 123.29700 101.40200 122.00200 1.000 33.47925 ? 135 SER A CB  1 
ATOM   780  O OG  . SER A 1 135 ? 121.99600 100.96700 121.67200 1.000 33.47925 ? 135 SER A OG  1 
ATOM   781  N N   . LYS A 1 136 ? 122.98000 100.23400 119.11300 1.000 36.00359 ? 136 LYS A N   1 
ATOM   782  C CA  . LYS A 1 136 ? 122.33700 100.40600 117.81900 1.000 36.00359 ? 136 LYS A CA  1 
ATOM   783  C C   . LYS A 1 136 ? 121.02900 101.17700 117.90900 1.000 36.00359 ? 136 LYS A C   1 
ATOM   784  O O   . LYS A 1 136 ? 120.41800 101.44400 116.87200 1.000 36.00359 ? 136 LYS A O   1 
ATOM   785  C CB  . LYS A 1 136 ? 122.07700 99.04300  117.17300 1.000 36.00359 ? 136 LYS A CB  1 
ATOM   786  C CG  . LYS A 1 136 ? 123.22700 98.53500  116.32200 1.000 36.00359 ? 136 LYS A CG  1 
ATOM   787  C CD  . LYS A 1 136 ? 123.35100 97.00800  116.32000 1.000 36.00359 ? 136 LYS A CD  1 
ATOM   788  C CE  . LYS A 1 136 ? 122.12200 96.29900  116.88200 1.000 36.00359 ? 136 LYS A CE  1 
ATOM   789  N NZ  . LYS A 1 136 ? 122.34800 94.83800  117.03400 1.000 36.00359 ? 136 LYS A NZ  1 
ATOM   790  N N   . ASN A 1 137 ? 120.59500 101.52900 119.11800 1.000 34.17025 ? 137 ASN A N   1 
ATOM   791  C CA  . ASN A 1 137 ? 119.32100 102.22200 119.29900 1.000 34.17025 ? 137 ASN A CA  1 
ATOM   792  C C   . ASN A 1 137 ? 119.19600 103.55700 118.56700 1.000 34.17025 ? 137 ASN A C   1 
ATOM   793  O O   . ASN A 1 137 ? 118.08200 103.85500 118.10500 1.000 34.17025 ? 137 ASN A O   1 
ATOM   794  C CB  . ASN A 1 137 ? 119.04600 102.39700 120.79700 1.000 34.17025 ? 137 ASN A CB  1 
ATOM   795  C CG  . ASN A 1 137 ? 118.53000 101.13000 121.43900 1.000 34.17025 ? 137 ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 137 ? 118.17200 100.18000 120.75100 1.000 34.17025 ? 137 ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 137 ? 118.50100 101.10500 122.75900 1.000 34.17025 ? 137 ASN A ND2 1 
ATOM   798  N N   . PRO A 1 138 ? 120.22600 104.41300 118.45900 1.000 33.50411 ? 138 PRO A N   1 
ATOM   799  C CA  . PRO A 1 138 ? 120.05300 105.62200 117.63500 1.000 33.50411 ? 138 PRO A CA  1 
ATOM   800  C C   . PRO A 1 138 ? 119.71500 105.34600 116.18000 1.000 33.50411 ? 138 PRO A C   1 
ATOM   801  O O   . PRO A 1 138 ? 119.07300 106.18700 115.54400 1.000 33.50411 ? 138 PRO A O   1 
ATOM   802  C CB  . PRO A 1 138 ? 121.40000 106.33600 117.78500 1.000 33.50411 ? 138 PRO A CB  1 
ATOM   803  C CG  . PRO A 1 138 ? 121.87400 105.92100 119.10000 1.000 33.50411 ? 138 PRO A CG  1 
ATOM   804  C CD  . PRO A 1 138 ? 121.48100 104.49400 119.23100 1.000 33.50411 ? 138 PRO A CD  1 
ATOM   805  N N   . LEU A 1 139 ? 120.11600 104.20200 115.62800 1.000 35.80070 ? 139 LEU A N   1 
ATOM   806  C CA  . LEU A 1 139 ? 119.65400 103.83800 114.29300 1.000 35.80070 ? 139 LEU A CA  1 
ATOM   807  C C   . LEU A 1 139 ? 118.19200 103.41700 114.30900 1.000 35.80070 ? 139 LEU A C   1 
ATOM   808  O O   . LEU A 1 139 ? 117.43300 103.76200 113.39900 1.000 35.80070 ? 139 LEU A O   1 
ATOM   809  C CB  . LEU A 1 139 ? 120.51800 102.72100 113.71500 1.000 35.80070 ? 139 LEU A CB  1 
ATOM   810  C CG  . LEU A 1 139 ? 121.82700 103.14100 113.05800 1.000 35.80070 ? 139 LEU A CG  1 
ATOM   811  C CD1 . LEU A 1 139 ? 122.56300 101.92600 112.52200 1.000 35.80070 ? 139 LEU A CD1 1 
ATOM   812  C CD2 . LEU A 1 139 ? 121.57900 104.16200 111.96500 1.000 35.80070 ? 139 LEU A CD2 1 
ATOM   813  N N   . LEU A 1 140 ? 117.77600 102.68100 115.33700 1.000 36.60278 ? 140 LEU A N   1 
ATOM   814  C CA  . LEU A 1 140 ? 116.42300 102.14600 115.38200 1.000 36.60278 ? 140 LEU A CA  1 
ATOM   815  C C   . LEU A 1 140 ? 115.38300 103.19800 115.74000 1.000 36.60278 ? 140 LEU A C   1 
ATOM   816  O O   . LEU A 1 140 ? 114.23700 103.09800 115.29800 1.000 36.60278 ? 140 LEU A O   1 
ATOM   817  C CB  . LEU A 1 140 ? 116.35700 100.99100 116.37700 1.000 36.60278 ? 140 LEU A CB  1 
ATOM   818  C CG  . LEU A 1 140 ? 117.25300 99.80200  116.05500 1.000 36.60278 ? 140 LEU A CG  1 
ATOM   819  C CD1 . LEU A 1 140 ? 117.20800 98.79500  117.18200 1.000 36.60278 ? 140 LEU A CD1 1 
ATOM   820  C CD2 . LEU A 1 140 ? 116.82700 99.16700  114.74700 1.000 36.60278 ? 140 LEU A CD2 1 
ATOM   821  N N   . TYR A 1 141 ? 115.75000 104.19900 116.53100 1.000 33.76791 ? 141 TYR A N   1 
ATOM   822  C CA  . TYR A 1 141 ? 114.80900 105.17800 117.04700 1.000 33.76791 ? 141 TYR A CA  1 
ATOM   823  C C   . TYR A 1 141 ? 115.11000 106.56100 116.49100 1.000 33.76791 ? 141 TYR A C   1 
ATOM   824  O O   . TYR A 1 141 ? 116.26600 106.91500 116.25300 1.000 33.76791 ? 141 TYR A O   1 
ATOM   825  C CB  . TYR A 1 141 ? 114.85000 105.23000 118.57400 1.000 33.76791 ? 141 TYR A CB  1 
ATOM   826  C CG  . TYR A 1 141 ? 114.37300 103.97200 119.24600 1.000 33.76791 ? 141 TYR A CG  1 
ATOM   827  C CD1 . TYR A 1 141 ? 113.02200 103.71200 119.38600 1.000 33.76791 ? 141 TYR A CD1 1 
ATOM   828  C CD2 . TYR A 1 141 ? 115.27500 103.05100 119.75700 1.000 33.76791 ? 141 TYR A CD2 1 
ATOM   829  C CE1 . TYR A 1 141 ? 112.58200 102.57200 120.00300 1.000 33.76791 ? 141 TYR A CE1 1 
ATOM   830  C CE2 . TYR A 1 141 ? 114.84200 101.90700 120.37800 1.000 33.76791 ? 141 TYR A CE2 1 
ATOM   831  C CZ  . TYR A 1 141 ? 113.49300 101.67400 120.50100 1.000 33.76791 ? 141 TYR A CZ  1 
ATOM   832  O OH  . TYR A 1 141 ? 113.04900 100.53400 121.11700 1.000 33.76791 ? 141 TYR A OH  1 
ATOM   833  N N   . ASP A 1 142 ? 114.05500 107.34700 116.31000 1.000 38.88093 ? 142 ASP A N   1 
ATOM   834  C CA  . ASP A 1 142 ? 114.15800 108.69700 115.77900 1.000 38.88093 ? 142 ASP A CA  1 
ATOM   835  C C   . ASP A 1 142 ? 114.22100 109.76100 116.86600 1.000 38.88093 ? 142 ASP A C   1 
ATOM   836  O O   . ASP A 1 142 ? 114.03300 110.94200 116.56500 1.000 38.88093 ? 142 ASP A O   1 
ATOM   837  C CB  . ASP A 1 142 ? 112.97900 108.98600 114.84700 1.000 38.88093 ? 142 ASP A CB  1 
ATOM   838  C CG  . ASP A 1 142 ? 113.13200 108.32900 113.48900 1.000 38.88093 ? 142 ASP A CG  1 
ATOM   839  O OD1 . ASP A 1 142 ? 114.25900 107.92400 113.14200 1.000 38.88093 ? 142 ASP A OD1 1 
ATOM   840  O OD2 . ASP A 1 142 ? 112.12100 108.21700 112.76600 1.000 38.88093 ? 142 ASP A OD2 1 
ATOM   841  N N   . ALA A 1 143 ? 114.49300 109.37300 118.11000 1.000 33.66595 ? 143 ALA A N   1 
ATOM   842  C CA  . ALA A 1 143 ? 114.43900 110.30300 119.22800 1.000 33.66595 ? 143 ALA A CA  1 
ATOM   843  C C   . ALA A 1 143 ? 115.53700 111.35400 119.13700 1.000 33.66595 ? 143 ALA A C   1 
ATOM   844  O O   . ALA A 1 143 ? 116.59900 111.13500 118.55200 1.000 33.66595 ? 143 ALA A O   1 
ATOM   845  C CB  . ALA A 1 143 ? 114.55700 109.55000 120.54900 1.000 33.66595 ? 143 ALA A CB  1 
ATOM   846  N N   . ASN A 1 144 ? 115.26200 112.51600 119.72600 1.000 35.12785 ? 144 ASN A N   1 
ATOM   847  C CA  . ASN A 1 144 ? 116.23800 113.59500 119.73000 1.000 35.12785 ? 144 ASN A CA  1 
ATOM   848  C C   . ASN A 1 144 ? 117.38900 113.30700 120.68300 1.000 35.12785 ? 144 ASN A C   1 
ATOM   849  O O   . ASN A 1 144 ? 118.50700 113.78100 120.46400 1.000 35.12785 ? 144 ASN A O   1 
ATOM   850  C CB  . ASN A 1 144 ? 115.55800 114.91200 120.10400 1.000 35.12785 ? 144 ASN A CB  1 
ATOM   851  C CG  . ASN A 1 144 ? 114.59400 115.39800 119.04200 1.000 35.12785 ? 144 ASN A CG  1 
ATOM   852  O OD1 . ASN A 1 144 ? 113.41000 115.58900 119.30600 1.000 35.12785 ? 144 ASN A OD1 1 
ATOM   853  N ND2 . ASN A 1 144 ? 115.09600 115.59100 117.83100 1.000 35.12785 ? 144 ASN A ND2 1 
ATOM   854  N N   . TYR A 1 145 ? 117.13800 112.54300 121.74200 1.000 29.67532 ? 145 TYR A N   1 
ATOM   855  C CA  . TYR A 1 145 ? 118.13200 112.29900 122.77300 1.000 29.67532 ? 145 TYR A CA  1 
ATOM   856  C C   . TYR A 1 145 ? 118.10300 110.83400 123.16600 1.000 29.67532 ? 145 TYR A C   1 
ATOM   857  O O   . TYR A 1 145 ? 117.13000 110.12100 122.92200 1.000 29.67532 ? 145 TYR A O   1 
ATOM   858  C CB  . TYR A 1 145 ? 117.89400 113.17800 124.00700 1.000 29.67532 ? 145 TYR A CB  1 
ATOM   859  C CG  . TYR A 1 145 ? 118.02100 114.64900 123.72300 1.000 29.67532 ? 145 TYR A CG  1 
ATOM   860  C CD1 . TYR A 1 145 ? 116.93200 115.38800 123.29400 1.000 29.67532 ? 145 TYR A CD1 1 
ATOM   861  C CD2 . TYR A 1 145 ? 119.23000 115.29700 123.87300 1.000 29.67532 ? 145 TYR A CD2 1 
ATOM   862  C CE1 . TYR A 1 145 ? 117.04700 116.72500 123.01500 1.000 29.67532 ? 145 TYR A CE1 1 
ATOM   863  C CE2 . TYR A 1 145 ? 119.35200 116.63400 123.60200 1.000 29.67532 ? 145 TYR A CE2 1 
ATOM   864  C CZ  . TYR A 1 145 ? 118.25900 117.34500 123.17600 1.000 29.67532 ? 145 TYR A CZ  1 
ATOM   865  O OH  . TYR A 1 145 ? 118.38800 118.68400 122.91100 1.000 29.67532 ? 145 TYR A OH  1 
ATOM   866  N N   . PHE A 1 146 ? 119.18800 110.39300 123.78700 1.000 27.48973 ? 146 PHE A N   1 
ATOM   867  C CA  . PHE A 1 146 ? 119.27500 109.03200 124.29600 1.000 27.48973 ? 146 PHE A CA  1 
ATOM   868  C C   . PHE A 1 146 ? 119.90500 109.06100 125.67600 1.000 27.48973 ? 146 PHE A C   1 
ATOM   869  O O   . PHE A 1 146 ? 121.00500 109.58800 125.84500 1.000 27.48973 ? 146 PHE A O   1 
ATOM   870  C CB  . PHE A 1 146 ? 120.06700 108.13800 123.33700 1.000 27.48973 ? 146 PHE A CB  1 
ATOM   871  C CG  . PHE A 1 146 ? 119.32500 107.82500 122.07700 1.000 27.48973 ? 146 PHE A CG  1 
ATOM   872  C CD1 . PHE A 1 146 ? 118.47300 106.74100 122.01700 1.000 27.48973 ? 146 PHE A CD1 1 
ATOM   873  C CD2 . PHE A 1 146 ? 119.44100 108.64400 120.96700 1.000 27.48973 ? 146 PHE A CD2 1 
ATOM   874  C CE1 . PHE A 1 146 ? 117.77400 106.46100 120.87200 1.000 27.48973 ? 146 PHE A CE1 1 
ATOM   875  C CE2 . PHE A 1 146 ? 118.73500 108.37100 119.82400 1.000 27.48973 ? 146 PHE A CE2 1 
ATOM   876  C CZ  . PHE A 1 146 ? 117.89800 107.28100 119.77800 1.000 27.48973 ? 146 PHE A CZ  1 
ATOM   877  N N   . LEU A 1 147 ? 119.19400 108.52500 126.65900 1.000 26.37938 ? 147 LEU A N   1 
ATOM   878  C CA  . LEU A 1 147 ? 119.72500 108.39500 128.00500 1.000 26.37938 ? 147 LEU A CA  1 
ATOM   879  C C   . LEU A 1 147 ? 120.51800 107.10300 128.10300 1.000 26.37938 ? 147 LEU A C   1 
ATOM   880  O O   . LEU A 1 147 ? 119.98900 106.02200 127.84400 1.000 26.37938 ? 147 LEU A O   1 
ATOM   881  C CB  . LEU A 1 147 ? 118.61200 108.41200 129.04700 1.000 26.37938 ? 147 LEU A CB  1 
ATOM   882  C CG  . LEU A 1 147 ? 119.28600 108.50400 130.41600 1.000 26.37938 ? 147 LEU A CG  1 
ATOM   883  C CD1 . LEU A 1 147 ? 119.70300 109.93100 130.71300 1.000 26.37938 ? 147 LEU A CD1 1 
ATOM   884  C CD2 . LEU A 1 147 ? 118.45200 107.93200 131.51800 1.000 26.37938 ? 147 LEU A CD2 1 
ATOM   885  N N   . CYS A 1 148 ? 121.77500 107.21500 128.49500 1.000 29.09865 ? 148 CYS A N   1 
ATOM   886  C CA  . CYS A 1 148 ? 122.72400 106.12800 128.40700 1.000 29.09865 ? 148 CYS A CA  1 
ATOM   887  C C   . CYS A 1 148 ? 123.46100 105.97800 129.72300 1.000 29.09865 ? 148 CYS A C   1 
ATOM   888  O O   . CYS A 1 148 ? 123.69900 106.95300 130.44400 1.000 29.09865 ? 148 CYS A O   1 
ATOM   889  C CB  . CYS A 1 148 ? 123.73000 106.36900 127.28100 1.000 29.09865 ? 148 CYS A CB  1 
ATOM   890  S SG  . CYS A 1 148 ? 122.97100 106.69600 125.68900 1.000 29.09865 ? 148 CYS A SG  1 
ATOM   891  N N   . TRP A 1 149 ? 123.80500 104.73400 130.03000 1.000 26.70445 ? 149 TRP A N   1 
ATOM   892  C CA  . TRP A 1 149 ? 124.79600 104.49400 131.06900 1.000 26.70445 ? 149 TRP A CA  1 
ATOM   893  C C   . TRP A 1 149 ? 125.47600 103.16200 130.81400 1.000 26.70445 ? 149 TRP A C   1 
ATOM   894  O O   . TRP A 1 149 ? 124.93700 102.29100 130.13300 1.000 26.70445 ? 149 TRP A O   1 
ATOM   895  C CB  . TRP A 1 149 ? 124.19900 104.55600 132.48600 1.000 26.70445 ? 149 TRP A CB  1 
ATOM   896  C CG  . TRP A 1 149 ? 123.35100 103.40400 132.91900 1.000 26.70445 ? 149 TRP A CG  1 
ATOM   897  C CD1 . TRP A 1 149 ? 123.74600 102.33300 133.65600 1.000 26.70445 ? 149 TRP A CD1 1 
ATOM   898  C CD2 . TRP A 1 149 ? 121.95100 103.23300 132.68200 1.000 26.70445 ? 149 TRP A CD2 1 
ATOM   899  N NE1 . TRP A 1 149 ? 122.68800 101.49600 133.87900 1.000 26.70445 ? 149 TRP A NE1 1 
ATOM   900  C CE2 . TRP A 1 149 ? 121.57100 102.02500 133.29200 1.000 26.70445 ? 149 TRP A CE2 1 
ATOM   901  C CE3 . TRP A 1 149 ? 120.98400 103.98100 132.00900 1.000 26.70445 ? 149 TRP A CE3 1 
ATOM   902  C CZ2 . TRP A 1 149 ? 120.26700 101.54500 133.24700 1.000 26.70445 ? 149 TRP A CZ2 1 
ATOM   903  C CZ3 . TRP A 1 149 ? 119.69500 103.50400 131.96400 1.000 26.70445 ? 149 TRP A CZ3 1 
ATOM   904  C CH2 . TRP A 1 149 ? 119.34500 102.29700 132.57800 1.000 26.70445 ? 149 TRP A CH2 1 
ATOM   905  N N   . HIS A 1 150 ? 126.67200 103.02300 131.36500 1.000 32.06579 ? 150 HIS A N   1 
ATOM   906  C CA  . HIS A 1 150 ? 127.54300 101.89900 131.07200 1.000 32.06579 ? 150 HIS A CA  1 
ATOM   907  C C   . HIS A 1 150 ? 127.64600 100.97800 132.27800 1.000 32.06579 ? 150 HIS A C   1 
ATOM   908  O O   . HIS A 1 150 ? 127.92400 101.43000 133.39200 1.000 32.06579 ? 150 HIS A O   1 
ATOM   909  C CB  . HIS A 1 150 ? 128.93500 102.38400 130.67100 1.000 32.06579 ? 150 HIS A CB  1 
ATOM   910  C CG  . HIS A 1 150 ? 129.96500 101.30100 130.65600 1.000 32.06579 ? 150 HIS A CG  1 
ATOM   911  N ND1 . HIS A 1 150 ? 130.13300 100.45200 129.58400 1.000 32.06579 ? 150 HIS A ND1 1 
ATOM   912  C CD2 . HIS A 1 150 ? 130.86800 100.91500 131.58700 1.000 32.06579 ? 150 HIS A CD2 1 
ATOM   913  C CE1 . HIS A 1 150 ? 131.10300 99.59900  129.85100 1.000 32.06579 ? 150 HIS A CE1 1 
ATOM   914  N NE2 . HIS A 1 150 ? 131.56300 99.85600  131.06100 1.000 32.06579 ? 150 HIS A NE2 1 
ATOM   915  N N   . THR A 1 151 ? 127.42800 99.69400  132.04800 1.000 35.12634 ? 151 THR A N   1 
ATOM   916  C CA  . THR A 1 151 ? 127.78600 98.65000  132.99300 1.000 35.12634 ? 151 THR A CA  1 
ATOM   917  C C   . THR A 1 151 ? 128.74300 97.69000  132.30200 1.000 35.12634 ? 151 THR A C   1 
ATOM   918  O O   . THR A 1 151 ? 128.95400 97.76300  131.09000 1.000 35.12634 ? 151 THR A O   1 
ATOM   919  C CB  . THR A 1 151 ? 126.54500 97.91600  133.51800 1.000 35.12634 ? 151 THR A CB  1 
ATOM   920  O OG1 . THR A 1 151 ? 125.79800 97.37800  132.42200 1.000 35.12634 ? 151 THR A OG1 1 
ATOM   921  C CG2 . THR A 1 151 ? 125.66400 98.86800  134.29900 1.000 35.12634 ? 151 THR A CG2 1 
ATOM   922  N N   . ASN A 1 152 ? 129.33900 96.79500  133.09100 1.000 40.21307 ? 152 ASN A N   1 
ATOM   923  C CA  . ASN A 1 152 ? 130.32400 95.86500  132.54500 1.000 40.21307 ? 152 ASN A CA  1 
ATOM   924  C C   . ASN A 1 152 ? 129.72400 94.92800  131.50500 1.000 40.21307 ? 152 ASN A C   1 
ATOM   925  O O   . ASN A 1 152 ? 130.40400 94.56100  130.54200 1.000 40.21307 ? 152 ASN A O   1 
ATOM   926  C CB  . ASN A 1 152 ? 130.96600 95.05200  133.66400 1.000 40.21307 ? 152 ASN A CB  1 
ATOM   927  C CG  . ASN A 1 152 ? 131.61800 95.91700  134.71000 1.000 40.21307 ? 152 ASN A CG  1 
ATOM   928  O OD1 . ASN A 1 152 ? 132.10900 97.00400  134.41200 1.000 40.21307 ? 152 ASN A OD1 1 
ATOM   929  N ND2 . ASN A 1 152 ? 131.63600 95.43800  135.94600 1.000 40.21307 ? 152 ASN A ND2 1 
ATOM   930  N N   . CYS A 1 153 ? 128.46700 94.52700  131.67300 1.000 41.51150 ? 153 CYS A N   1 
ATOM   931  C CA  . CYS A 1 153 ? 127.86400 93.56800  130.76000 1.000 41.51150 ? 153 CYS A CA  1 
ATOM   932  C C   . CYS A 1 153 ? 126.91600 94.19900  129.75100 1.000 41.51150 ? 153 CYS A C   1 
ATOM   933  O O   . CYS A 1 153 ? 126.51400 93.51900  128.80300 1.000 41.51150 ? 153 CYS A O   1 
ATOM   934  C CB  . CYS A 1 153 ? 127.11500 92.47900  131.54200 1.000 41.51150 ? 153 CYS A CB  1 
ATOM   935  S SG  . CYS A 1 153 ? 125.70300 93.05600  132.49500 1.000 41.51150 ? 153 CYS A SG  1 
ATOM   936  N N   . TYR A 1 154 ? 126.55000 95.46500  129.91800 1.000 34.77847 ? 154 TYR A N   1 
ATOM   937  C CA  . TYR A 1 154 ? 125.58900 96.06600  129.00700 1.000 34.77847 ? 154 TYR A CA  1 
ATOM   938  C C   . TYR A 1 154 ? 125.77100 97.57600  128.97500 1.000 34.77847 ? 154 TYR A C   1 
ATOM   939  O O   . TYR A 1 154 ? 126.18600 98.18600  129.96000 1.000 34.77847 ? 154 TYR A O   1 
ATOM   940  C CB  . TYR A 1 154 ? 124.15200 95.71900  129.40600 1.000 34.77847 ? 154 TYR A CB  1 
ATOM   941  C CG  . TYR A 1 154 ? 123.16200 95.94300  128.29800 1.000 34.77847 ? 154 TYR A CG  1 
ATOM   942  C CD1 . TYR A 1 154 ? 122.31000 97.03500  128.31600 1.000 34.77847 ? 154 TYR A CD1 1 
ATOM   943  C CD2 . TYR A 1 154 ? 123.08600 95.06600  127.22500 1.000 34.77847 ? 154 TYR A CD2 1 
ATOM   944  C CE1 . TYR A 1 154 ? 121.41000 97.24600  127.30200 1.000 34.77847 ? 154 TYR A CE1 1 
ATOM   945  C CE2 . TYR A 1 154 ? 122.18900 95.26900  126.20500 1.000 34.77847 ? 154 TYR A CE2 1 
ATOM   946  C CZ  . TYR A 1 154 ? 121.35400 96.36000  126.24700 1.000 34.77847 ? 154 TYR A CZ  1 
ATOM   947  O OH  . TYR A 1 154 ? 120.45700 96.56600  125.23100 1.000 34.77847 ? 154 TYR A OH  1 
ATOM   948  N N   . ASP A 1 155 ? 125.44500 98.16600  127.83000 1.000 33.75025 ? 155 ASP A N   1 
ATOM   949  C CA  . ASP A 1 155 ? 125.39800 99.61400  127.66500 1.000 33.75025 ? 155 ASP A CA  1 
ATOM   950  C C   . ASP A 1 155 ? 123.95800 100.00700 127.37000 1.000 33.75025 ? 155 ASP A C   1 
ATOM   951  O O   . ASP A 1 155 ? 123.41000 99.63600  126.32900 1.000 33.75025 ? 155 ASP A O   1 
ATOM   952  C CB  . ASP A 1 155 ? 126.34300 100.07100 126.55700 1.000 33.75025 ? 155 ASP A CB  1 
ATOM   953  C CG  . ASP A 1 155 ? 127.79400 100.01900 126.97800 1.000 33.75025 ? 155 ASP A CG  1 
ATOM   954  O OD1 . ASP A 1 155 ? 128.57500 99.28000  126.35400 1.000 33.75025 ? 155 ASP A OD1 1 
ATOM   955  O OD2 . ASP A 1 155 ? 128.15200 100.70400 127.95200 1.000 33.75025 ? 155 ASP A OD2 1 
ATOM   956  N N   . TYR A 1 156 ? 123.34500 100.74500 128.28700 1.000 29.51729 ? 156 TYR A N   1 
ATOM   957  C CA  . TYR A 1 156 ? 121.94500 101.11200 128.15700 1.000 29.51729 ? 156 TYR A CA  1 
ATOM   958  C C   . TYR A 1 156 ? 121.80100 102.41600 127.39500 1.000 29.51729 ? 156 TYR A C   1 
ATOM   959  O O   . TYR A 1 156 ? 122.53400 103.37800 127.64700 1.000 29.51729 ? 156 TYR A O   1 
ATOM   960  C CB  . TYR A 1 156 ? 121.29500 101.25000 129.53100 1.000 29.51729 ? 156 TYR A CB  1 
ATOM   961  C CG  . TYR A 1 156 ? 121.20500 99.96100  130.29200 1.000 29.51729 ? 156 TYR A CG  1 
ATOM   962  C CD1 . TYR A 1 156 ? 122.22800 99.56200  131.13400 1.000 29.51729 ? 156 TYR A CD1 1 
ATOM   963  C CD2 . TYR A 1 156 ? 120.09900 99.13700  130.16400 1.000 29.51729 ? 156 TYR A CD2 1 
ATOM   964  C CE1 . TYR A 1 156 ? 122.15000 98.38900  131.83300 1.000 29.51729 ? 156 TYR A CE1 1 
ATOM   965  C CE2 . TYR A 1 156 ? 120.01400 97.95700  130.85800 1.000 29.51729 ? 156 TYR A CE2 1 
ATOM   966  C CZ  . TYR A 1 156 ? 121.04400 97.58800  131.68800 1.000 29.51729 ? 156 TYR A CZ  1 
ATOM   967  O OH  . TYR A 1 156 ? 120.97000 96.41600  132.38300 1.000 29.51729 ? 156 TYR A OH  1 
ATOM   968  N N   . CYS A 1 157 ? 120.81300 102.44700 126.49800 1.000 30.33211 ? 157 CYS A N   1 
ATOM   969  C CA  . CYS A 1 157 ? 120.56600 103.57900 125.60800 1.000 30.33211 ? 157 CYS A CA  1 
ATOM   970  C C   . CYS A 1 157 ? 119.06300 103.62300 125.33700 1.000 30.33211 ? 157 CYS A C   1 
ATOM   971  O O   . CYS A 1 157 ? 118.55000 102.83500 124.54000 1.000 30.33211 ? 157 CYS A O   1 
ATOM   972  C CB  . CYS A 1 157 ? 121.37300 103.43400 124.32400 1.000 30.33211 ? 157 CYS A CB  1 
ATOM   973  S SG  . CYS A 1 157 ? 121.10300 104.68800 123.07400 1.000 30.33211 ? 157 CYS A SG  1 
ATOM   974  N N   . ILE A 1 158 ? 118.37100 104.53800 125.99600 1.000 26.40051 ? 158 ILE A N   1 
ATOM   975  C CA  . ILE A 1 158 ? 116.91200 104.62100 125.97500 1.000 26.40051 ? 158 ILE A CA  1 
ATOM   976  C C   . ILE A 1 158 ? 116.51600 105.91300 125.27400 1.000 26.40051 ? 158 ILE A C   1 
ATOM   977  O O   . ILE A 1 158 ? 117.06500 106.96700 125.59800 1.000 26.40051 ? 158 ILE A O   1 
ATOM   978  C CB  . ILE A 1 158 ? 116.32000 104.57000 127.39700 1.000 26.40051 ? 158 ILE A CB  1 
ATOM   979  C CG1 . ILE A 1 158 ? 116.75600 103.28800 128.10500 1.000 26.40051 ? 158 ILE A CG1 1 
ATOM   980  C CG2 . ILE A 1 158 ? 114.80400 104.68800 127.37000 1.000 26.40051 ? 158 ILE A CG2 1 
ATOM   981  C CD1 . ILE A 1 158 ? 116.32000 103.20700 129.53900 1.000 26.40051 ? 158 ILE A CD1 1 
ATOM   982  N N   . PRO A 1 159 ? 115.58900 105.87800 124.31600 1.000 25.56481 ? 159 PRO A N   1 
ATOM   983  C CA  . PRO A 1 159 ? 115.15000 107.11700 123.66100 1.000 25.56481 ? 159 PRO A CA  1 
ATOM   984  C C   . PRO A 1 159 ? 114.51900 108.10000 124.63900 1.000 25.56481 ? 159 PRO A C   1 
ATOM   985  O O   . PRO A 1 159 ? 113.83700 107.71500 125.58800 1.000 25.56481 ? 159 PRO A O   1 
ATOM   986  C CB  . PRO A 1 159 ? 114.12200 106.62800 122.63400 1.000 25.56481 ? 159 PRO A CB  1 
ATOM   987  C CG  . PRO A 1 159 ? 114.36000 105.19700 122.48500 1.000 25.56481 ? 159 PRO A CG  1 
ATOM   988  C CD  . PRO A 1 159 ? 114.94300 104.68800 123.74200 1.000 25.56481 ? 159 PRO A CD  1 
ATOM   989  N N   . TYR A 1 160 ? 114.75000 109.38700 124.38700 1.000 24.26380 ? 160 TYR A N   1 
ATOM   990  C CA  . TYR A 1 160 ? 114.24700 110.45700 125.23400 1.000 24.26380 ? 160 TYR A CA  1 
ATOM   991  C C   . TYR A 1 160 ? 114.08500 111.71000 124.38300 1.000 24.26380 ? 160 TYR A C   1 
ATOM   992  O O   . TYR A 1 160 ? 114.83200 111.92500 123.42700 1.000 24.26380 ? 160 TYR A O   1 
ATOM   993  C CB  . TYR A 1 160 ? 115.19200 110.70900 126.41300 1.000 24.26380 ? 160 TYR A CB  1 
ATOM   994  C CG  . TYR A 1 160 ? 114.55200 111.36200 127.61300 1.000 24.26380 ? 160 TYR A CG  1 
ATOM   995  C CD1 . TYR A 1 160 ? 114.86600 112.66400 127.96200 1.000 24.26380 ? 160 TYR A CD1 1 
ATOM   996  C CD2 . TYR A 1 160 ? 113.64800 110.67400 128.40700 1.000 24.26380 ? 160 TYR A CD2 1 
ATOM   997  C CE1 . TYR A 1 160 ? 114.29500 113.26300 129.05800 1.000 24.26380 ? 160 TYR A CE1 1 
ATOM   998  C CE2 . TYR A 1 160 ? 113.07500 111.27100 129.50600 1.000 24.26380 ? 160 TYR A CE2 1 
ATOM   999  C CZ  . TYR A 1 160 ? 113.40200 112.56500 129.82600 1.000 24.26380 ? 160 TYR A CZ  1 
ATOM   1000 O OH  . TYR A 1 160 ? 112.83500 113.17200 130.91500 1.000 24.26380 ? 160 TYR A OH  1 
ATOM   1001 N N   . ASN A 1 161 ? 113.11100 112.54500 124.74400 1.000 27.93691 ? 161 ASN A N   1 
ATOM   1002 C CA  . ASN A 1 161 ? 112.67400 113.59900 123.83500 1.000 27.93691 ? 161 ASN A CA  1 
ATOM   1003 C C   . ASN A 1 161 ? 113.41200 114.92400 124.00600 1.000 27.93691 ? 161 ASN A C   1 
ATOM   1004 O O   . ASN A 1 161 ? 113.69300 115.59300 123.00900 1.000 27.93691 ? 161 ASN A O   1 
ATOM   1005 C CB  . ASN A 1 161 ? 111.17100 113.83600 123.97700 1.000 27.93691 ? 161 ASN A CB  1 
ATOM   1006 C CG  . ASN A 1 161 ? 110.64400 114.83000 122.96200 1.000 27.93691 ? 161 ASN A CG  1 
ATOM   1007 O OD1 . ASN A 1 161 ? 110.66400 114.57300 121.76300 1.000 27.93691 ? 161 ASN A OD1 1 
ATOM   1008 N ND2 . ASN A 1 161 ? 110.18500 115.97600 123.43700 1.000 27.93691 ? 161 ASN A ND2 1 
ATOM   1009 N N   . SER A 1 162 ? 113.72200 115.34200 125.23000 1.000 27.97825 ? 162 SER A N   1 
ATOM   1010 C CA  . SER A 1 162 ? 114.30700 116.66300 125.42000 1.000 27.97825 ? 162 SER A CA  1 
ATOM   1011 C C   . SER A 1 162 ? 115.15500 116.67800 126.68100 1.000 27.97825 ? 162 SER A C   1 
ATOM   1012 O O   . SER A 1 162 ? 115.07300 115.78100 127.51600 1.000 27.97825 ? 162 SER A O   1 
ATOM   1013 C CB  . SER A 1 162 ? 113.23000 117.75300 125.49000 1.000 27.97825 ? 162 SER A CB  1 
ATOM   1014 O OG  . SER A 1 162 ? 112.39100 117.58600 126.61600 1.000 27.97825 ? 162 SER A OG  1 
ATOM   1015 N N   . VAL A 1 163 ? 115.97500 117.71600 126.81300 1.000 28.48718 ? 163 VAL A N   1 
ATOM   1016 C CA  . VAL A 1 163 ? 116.79200 117.89900 128.00800 1.000 28.48718 ? 163 VAL A CA  1 
ATOM   1017 C C   . VAL A 1 163 ? 115.89700 118.44400 129.11400 1.000 28.48718 ? 163 VAL A C   1 
ATOM   1018 O O   . VAL A 1 163 ? 115.50600 119.61100 129.09200 1.000 28.48718 ? 163 VAL A O   1 
ATOM   1019 C CB  . VAL A 1 163 ? 117.97800 118.83300 127.75000 1.000 28.48718 ? 163 VAL A CB  1 
ATOM   1020 C CG1 . VAL A 1 163 ? 118.85200 118.92100 128.97900 1.000 28.48718 ? 163 VAL A CG1 1 
ATOM   1021 C CG2 . VAL A 1 163 ? 118.77900 118.35900 126.57300 1.000 28.48718 ? 163 VAL A CG2 1 
ATOM   1022 N N   . THR A 1 164 ? 115.57400 117.60200 130.08400 1.000 28.24127 ? 164 THR A N   1 
ATOM   1023 C CA  . THR A 1 164 ? 114.78000 117.99400 131.23400 1.000 28.24127 ? 164 THR A CA  1 
ATOM   1024 C C   . THR A 1 164 ? 115.69300 118.17300 132.43900 1.000 28.24127 ? 164 THR A C   1 
ATOM   1025 O O   . THR A 1 164 ? 116.85200 117.75700 132.43100 1.000 28.24127 ? 164 THR A O   1 
ATOM   1026 C CB  . THR A 1 164 ? 113.69000 116.95800 131.53300 1.000 28.24127 ? 164 THR A CB  1 
ATOM   1027 O OG1 . THR A 1 164 ? 114.28900 115.67100 131.71000 1.000 28.24127 ? 164 THR A OG1 1 
ATOM   1028 C CG2 . THR A 1 164 ? 112.69600 116.88700 130.39000 1.000 28.24127 ? 164 THR A CG2 1 
ATOM   1029 N N   . SER A 1 165 ? 115.16600 118.82000 133.47400 1.000 28.80191 ? 165 SER A N   1 
ATOM   1030 C CA  . SER A 1 165 ? 115.94800 119.01300 134.68700 1.000 28.80191 ? 165 SER A CA  1 
ATOM   1031 C C   . SER A 1 165 ? 116.00400 117.75800 135.54400 1.000 28.80191 ? 165 SER A C   1 
ATOM   1032 O O   . SER A 1 165 ? 116.87300 117.65100 136.41200 1.000 28.80191 ? 165 SER A O   1 
ATOM   1033 C CB  . SER A 1 165 ? 115.38600 120.18000 135.50000 1.000 28.80191 ? 165 SER A CB  1 
ATOM   1034 O OG  . SER A 1 165 ? 114.11600 119.87400 136.03600 1.000 28.80191 ? 165 SER A OG  1 
ATOM   1035 N N   . SER A 1 166 ? 115.10500 116.81000 135.31300 1.000 27.44724 ? 166 SER A N   1 
ATOM   1036 C CA  . SER A 1 166 ? 115.11000 115.54300 136.01800 1.000 27.44724 ? 166 SER A CA  1 
ATOM   1037 C C   . SER A 1 166 ? 114.74400 114.44500 135.03800 1.000 27.44724 ? 166 SER A C   1 
ATOM   1038 O O   . SER A 1 166 ? 114.13900 114.69100 133.99400 1.000 27.44724 ? 166 SER A O   1 
ATOM   1039 C CB  . SER A 1 166 ? 114.13900 115.53800 137.20400 1.000 27.44724 ? 166 SER A CB  1 
ATOM   1040 O OG  . SER A 1 166 ? 112.81300 115.76200 136.77300 1.000 27.44724 ? 166 SER A OG  1 
ATOM   1041 N N   . ILE A 1 167 ? 115.13300 113.22600 135.38300 1.000 24.81016 ? 167 ILE A N   1 
ATOM   1042 C CA  . ILE A 1 167 ? 114.79100 112.04000 134.60900 1.000 24.81016 ? 167 ILE A CA  1 
ATOM   1043 C C   . ILE A 1 167 ? 114.39300 110.94100 135.58200 1.000 24.81016 ? 167 ILE A C   1 
ATOM   1044 O O   . ILE A 1 167 ? 115.06800 110.72200 136.58900 1.000 24.81016 ? 167 ILE A O   1 
ATOM   1045 C CB  . ILE A 1 167 ? 115.95500 111.60000 133.69500 1.000 24.81016 ? 167 ILE A CB  1 
ATOM   1046 C CG1 . ILE A 1 167 ? 116.00900 112.49800 132.45800 1.000 24.81016 ? 167 ILE A CG1 1 
ATOM   1047 C CG2 . ILE A 1 167 ? 115.82100 110.14500 133.27500 1.000 24.81016 ? 167 ILE A CG2 1 
ATOM   1048 C CD1 . ILE A 1 167 ? 117.27900 112.43300 131.70100 1.000 24.81016 ? 167 ILE A CD1 1 
ATOM   1049 N N   . VAL A 1 168 ? 113.29200 110.25800 135.29800 1.000 23.19999 ? 168 VAL A N   1 
ATOM   1050 C CA  . VAL A 1 168 ? 112.84600 109.13500 136.11000 1.000 23.19999 ? 168 VAL A CA  1 
ATOM   1051 C C   . VAL A 1 168 ? 113.03300 107.86400 135.30300 1.000 23.19999 ? 168 VAL A C   1 
ATOM   1052 O O   . VAL A 1 168 ? 112.50100 107.73700 134.19500 1.000 23.19999 ? 168 VAL A O   1 
ATOM   1053 C CB  . VAL A 1 168 ? 111.38800 109.29300 136.56200 1.000 23.19999 ? 168 VAL A CB  1 
ATOM   1054 C CG1 . VAL A 1 168 ? 110.97100 108.10100 137.40300 1.000 23.19999 ? 168 VAL A CG1 1 
ATOM   1055 C CG2 . VAL A 1 168 ? 111.23000 110.56400 137.34000 1.000 23.19999 ? 168 VAL A CG2 1 
ATOM   1056 N N   . ILE A 1 169 ? 113.79000 106.92800 135.85500 1.000 24.04064 ? 169 ILE A N   1 
ATOM   1057 C CA  . ILE A 1 169 ? 113.92100 105.59300 135.29600 1.000 24.04064 ? 169 ILE A CA  1 
ATOM   1058 C C   . ILE A 1 169 ? 113.06900 104.66400 136.14300 1.000 24.04064 ? 169 ILE A C   1 
ATOM   1059 O O   . ILE A 1 169 ? 113.23600 104.59400 137.36400 1.000 24.04064 ? 169 ILE A O   1 
ATOM   1060 C CB  . ILE A 1 169 ? 115.38600 105.13500 135.25800 1.000 24.04064 ? 169 ILE A CB  1 
ATOM   1061 C CG1 . ILE A 1 169 ? 116.23800 106.15000 134.49500 1.000 24.04064 ? 169 ILE A CG1 1 
ATOM   1062 C CG2 . ILE A 1 169 ? 115.49700 103.75900 134.62400 1.000 24.04064 ? 169 ILE A CG2 1 
ATOM   1063 C CD1 . ILE A 1 169 ? 117.69900 105.82000 134.46400 1.000 24.04064 ? 169 ILE A CD1 1 
ATOM   1064 N N   . THR A 1 170 ? 112.14500 103.96000 135.50700 1.000 26.45503 ? 170 THR A N   1 
ATOM   1065 C CA  . THR A 1 170 ? 111.28900 103.00200 136.18000 1.000 26.45503 ? 170 THR A CA  1 
ATOM   1066 C C   . THR A 1 170 ? 111.88800 101.61500 136.00700 1.000 26.45503 ? 170 THR A C   1 
ATOM   1067 O O   . THR A 1 170 ? 112.25400 101.23200 134.89800 1.000 26.45503 ? 170 THR A O   1 
ATOM   1068 C CB  . THR A 1 170 ? 109.87400 103.06000 135.60300 1.000 26.45503 ? 170 THR A CB  1 
ATOM   1069 O OG1 . THR A 1 170 ? 109.32400 104.36300 135.81500 1.000 26.45503 ? 170 THR A OG1 1 
ATOM   1070 C CG2 . THR A 1 170 ? 108.99000 102.03900 136.24400 1.000 26.45503 ? 170 THR A CG2 1 
ATOM   1071 N N   . SER A 1 171 ? 112.00500 100.86900 137.09700 1.000 32.29061 ? 171 SER A N   1 
ATOM   1072 C CA  . SER A 1 171 ? 112.54700 99.51800  137.04100 1.000 32.29061 ? 171 SER A CA  1 
ATOM   1073 C C   . SER A 1 171 ? 111.48000 98.55500  137.53400 1.000 32.29061 ? 171 SER A C   1 
ATOM   1074 O O   . SER A 1 171 ? 111.01000 98.66900  138.66900 1.000 32.29061 ? 171 SER A O   1 
ATOM   1075 C CB  . SER A 1 171 ? 113.82400 99.39700  137.86700 1.000 32.29061 ? 171 SER A CB  1 
ATOM   1076 O OG  . SER A 1 171 ? 114.17100 98.03900  138.05500 1.000 32.29061 ? 171 SER A OG  1 
ATOM   1077 N N   . GLY A 1 172 ? 111.09900 97.61300  136.68100 1.000 40.27270 ? 172 GLY A N   1 
ATOM   1078 C CA  . GLY A 1 172 ? 110.16900 96.56100  137.05500 1.000 40.27270 ? 172 GLY A CA  1 
ATOM   1079 C C   . GLY A 1 172 ? 110.89100 95.22700  137.13100 1.000 40.27270 ? 172 GLY A C   1 
ATOM   1080 O O   . GLY A 1 172 ? 111.71800 94.91100  136.27800 1.000 40.27270 ? 172 GLY A O   1 
ATOM   1081 N N   . ASP A 1 173 ? 110.57800 94.45300  138.16700 1.000 46.29251 ? 173 ASP A N   1 
ATOM   1082 C CA  . ASP A 1 173 ? 111.20800 93.15500  138.34600 1.000 46.29251 ? 173 ASP A CA  1 
ATOM   1083 C C   . ASP A 1 173 ? 110.47300 92.08300  137.54000 1.000 46.29251 ? 173 ASP A C   1 
ATOM   1084 O O   . ASP A 1 173 ? 109.62900 92.37100  136.68900 1.000 46.29251 ? 173 ASP A O   1 
ATOM   1085 C CB  . ASP A 1 173 ? 111.30100 92.80500  139.83400 1.000 46.29251 ? 173 ASP A CB  1 
ATOM   1086 C CG  . ASP A 1 173 ? 109.95700 92.85400  140.55600 1.000 46.29251 ? 173 ASP A CG  1 
ATOM   1087 O OD1 . ASP A 1 173 ? 109.96000 93.16100  141.76500 1.000 46.29251 ? 173 ASP A OD1 1 
ATOM   1088 O OD2 . ASP A 1 173 ? 108.90500 92.57900  139.94500 1.000 46.29251 ? 173 ASP A OD2 1 
ATOM   1089 N N   . GLY A 1 174 ? 110.80200 90.82600  137.81200 1.000 49.74248 ? 174 GLY A N   1 
ATOM   1090 C CA  . GLY A 1 174 ? 110.13600 89.71200  137.16300 1.000 49.74248 ? 174 GLY A CA  1 
ATOM   1091 C C   . GLY A 1 174 ? 108.74900 89.43600  137.71500 1.000 49.74248 ? 174 GLY A C   1 
ATOM   1092 O O   . GLY A 1 174 ? 108.58500 89.13000  138.89600 1.000 49.74248 ? 174 GLY A O   1 
ATOM   1093 N N   . GLU A 1 181 ? 108.83200 91.55500  131.68900 1.000 47.49790 ? 181 GLU A N   1 
ATOM   1094 C CA  . GLU A 1 181 ? 110.04900 91.08100  132.33500 1.000 47.49790 ? 181 GLU A CA  1 
ATOM   1095 C C   . GLU A 1 181 ? 110.70400 92.17400  133.16200 1.000 47.49790 ? 181 GLU A C   1 
ATOM   1096 O O   . GLU A 1 181 ? 110.20700 93.29400  133.23300 1.000 47.49790 ? 181 GLU A O   1 
ATOM   1097 C CB  . GLU A 1 181 ? 111.04000 90.56000  131.29300 1.000 47.49790 ? 181 GLU A CB  1 
ATOM   1098 C CG  . GLU A 1 181 ? 111.46900 91.59600  130.26700 1.000 47.49790 ? 181 GLU A CG  1 
ATOM   1099 C CD  . GLU A 1 181 ? 112.24100 90.98300  129.11300 1.000 47.49790 ? 181 GLU A CD  1 
ATOM   1100 O OE1 . GLU A 1 181 ? 112.73700 89.84700  129.26600 1.000 47.49790 ? 181 GLU A OE1 1 
ATOM   1101 O OE2 . GLU A 1 181 ? 112.35800 91.63700  128.05500 1.000 47.49790 ? 181 GLU A OE2 1 
ATOM   1102 N N   . HIS A 1 182 ? 111.82100 91.82400  133.79300 1.000 40.53937 ? 182 HIS A N   1 
ATOM   1103 C CA  . HIS A 1 182 ? 112.64100 92.79700  134.49900 1.000 40.53937 ? 182 HIS A CA  1 
ATOM   1104 C C   . HIS A 1 182 ? 113.22300 93.78600  133.49600 1.000 40.53937 ? 182 HIS A C   1 
ATOM   1105 O O   . HIS A 1 182 ? 113.95100 93.39400  132.58200 1.000 40.53937 ? 182 HIS A O   1 
ATOM   1106 C CB  . HIS A 1 182 ? 113.75000 92.06900  135.25600 1.000 40.53937 ? 182 HIS A CB  1 
ATOM   1107 C CG  . HIS A 1 182 ? 114.35300 92.85600  136.37400 1.000 40.53937 ? 182 HIS A CG  1 
ATOM   1108 N ND1 . HIS A 1 182 ? 113.96900 94.14400  136.67600 1.000 40.53937 ? 182 HIS A ND1 1 
ATOM   1109 C CD2 . HIS A 1 182 ? 115.31500 92.53100  137.26900 1.000 40.53937 ? 182 HIS A CD2 1 
ATOM   1110 C CE1 . HIS A 1 182 ? 114.66900 94.57900  137.70700 1.000 40.53937 ? 182 HIS A CE1 1 
ATOM   1111 N NE2 . HIS A 1 182 ? 115.49400 93.62000  138.08600 1.000 40.53937 ? 182 HIS A NE2 1 
ATOM   1112 N N   . ASP A 1 183 ? 112.89300 95.06500  133.64800 1.000 36.86201 ? 183 ASP A N   1 
ATOM   1113 C CA  . ASP A 1 183 ? 113.26100 96.03400  132.62600 1.000 36.86201 ? 183 ASP A CA  1 
ATOM   1114 C C   . ASP A 1 183 ? 113.37400 97.42800  133.22800 1.000 36.86201 ? 183 ASP A C   1 
ATOM   1115 O O   . ASP A 1 183 ? 112.82800 97.72300  134.29300 1.000 36.86201 ? 183 ASP A O   1 
ATOM   1116 C CB  . ASP A 1 183 ? 112.24800 96.03000  131.47800 1.000 36.86201 ? 183 ASP A CB  1 
ATOM   1117 C CG  . ASP A 1 183 ? 110.93800 96.69100  131.85500 1.000 36.86201 ? 183 ASP A CG  1 
ATOM   1118 O OD1 . ASP A 1 183 ? 110.34200 96.30200  132.88100 1.000 36.86201 ? 183 ASP A OD1 1 
ATOM   1119 O OD2 . ASP A 1 183 ? 110.50400 97.61000  131.13400 1.000 36.86201 ? 183 ASP A OD2 1 
ATOM   1120 N N   . TYR A 1 184 ? 114.10400 98.27900  132.51300 1.000 29.13685 ? 184 TYR A N   1 
ATOM   1121 C CA  . TYR A 1 184 ? 114.14400 99.71500  132.72300 1.000 29.13685 ? 184 TYR A CA  1 
ATOM   1122 C C   . TYR A 1 184 ? 113.25100 100.38800 131.69300 1.000 29.13685 ? 184 TYR A C   1 
ATOM   1123 O O   . TYR A 1 184 ? 113.15300 99.94200  130.55100 1.000 29.13685 ? 184 TYR A O   1 
ATOM   1124 C CB  . TYR A 1 184 ? 115.56200 100.26300 132.59100 1.000 29.13685 ? 184 TYR A CB  1 
ATOM   1125 C CG  . TYR A 1 184 ? 116.52300 99.75000  133.62300 1.000 29.13685 ? 184 TYR A CG  1 
ATOM   1126 C CD1 . TYR A 1 184 ? 117.53700 98.87200  133.27400 1.000 29.13685 ? 184 TYR A CD1 1 
ATOM   1127 C CD2 . TYR A 1 184 ? 116.42600 100.15100 134.94400 1.000 29.13685 ? 184 TYR A CD2 1 
ATOM   1128 C CE1 . TYR A 1 184 ? 118.42300 98.40700  134.21200 1.000 29.13685 ? 184 TYR A CE1 1 
ATOM   1129 C CE2 . TYR A 1 184 ? 117.30400 99.68800  135.88700 1.000 29.13685 ? 184 TYR A CE2 1 
ATOM   1130 C CZ  . TYR A 1 184 ? 118.30300 98.81900  135.51800 1.000 29.13685 ? 184 TYR A CZ  1 
ATOM   1131 O OH  . TYR A 1 184 ? 119.18100 98.35400  136.45900 1.000 29.13685 ? 184 TYR A OH  1 
ATOM   1132 N N   . GLN A 1 185 ? 112.60400 101.47000 132.10300 1.000 25.98195 ? 185 GLN A N   1 
ATOM   1133 C CA  . GLN A 1 185 ? 111.58500 102.09300 131.27600 1.000 25.98195 ? 185 GLN A CA  1 
ATOM   1134 C C   . GLN A 1 185 ? 111.59800 103.59300 131.50900 1.000 25.98195 ? 185 GLN A C   1 
ATOM   1135 O O   . GLN A 1 185 ? 111.61200 104.04800 132.65500 1.000 25.98195 ? 185 GLN A O   1 
ATOM   1136 C CB  . GLN A 1 185 ? 110.20600 101.49900 131.58700 1.000 25.98195 ? 185 GLN A CB  1 
ATOM   1137 C CG  . GLN A 1 185 ? 109.05000 102.10200 130.81300 1.000 25.98195 ? 185 GLN A CG  1 
ATOM   1138 C CD  . GLN A 1 185 ? 108.32300 103.18100 131.59100 1.000 25.98195 ? 185 GLN A CD  1 
ATOM   1139 O OE1 . GLN A 1 185 ? 108.32300 104.34000 131.20300 1.000 25.98195 ? 185 GLN A OE1 1 
ATOM   1140 N NE2 . GLN A 1 185 ? 107.70500 102.79900 132.69500 1.000 25.98195 ? 185 GLN A NE2 1 
ATOM   1141 N N   . ILE A 1 186 ? 111.64500 104.35300 130.41800 1.000 24.02153 ? 186 ILE A N   1 
ATOM   1142 C CA  . ILE A 1 186 ? 111.39600 105.79000 130.43600 1.000 24.02153 ? 186 ILE A CA  1 
ATOM   1143 C C   . ILE A 1 186 ? 110.47900 106.12400 129.27200 1.000 24.02153 ? 186 ILE A C   1 
ATOM   1144 O O   . ILE A 1 186 ? 110.76800 105.75600 128.12900 1.000 24.02153 ? 186 ILE A O   1 
ATOM   1145 C CB  . ILE A 1 186 ? 112.68400 106.63400 130.34000 1.000 24.02153 ? 186 ILE A CB  1 
ATOM   1146 C CG1 . ILE A 1 186 ? 113.80500 106.07600 131.21200 1.000 24.02153 ? 186 ILE A CG1 1 
ATOM   1147 C CG2 . ILE A 1 186 ? 112.39500 108.05500 130.75200 1.000 24.02153 ? 186 ILE A CG2 1 
ATOM   1148 C CD1 . ILE A 1 186 ? 115.13800 106.66900 130.90300 1.000 24.02153 ? 186 ILE A CD1 1 
ATOM   1149 N N   . GLY A 1 187 ? 109.38700 106.83000 129.55800 1.000 24.36672 ? 187 GLY A N   1 
ATOM   1150 C CA  . GLY A 1 187 ? 108.45000 107.23500 128.52800 1.000 24.36672 ? 187 GLY A CA  1 
ATOM   1151 C C   . GLY A 1 187 ? 107.79500 106.09700 127.78600 1.000 24.36672 ? 187 GLY A C   1 
ATOM   1152 O O   . GLY A 1 187 ? 107.37200 106.27500 126.64500 1.000 24.36672 ? 187 GLY A O   1 
ATOM   1153 N N   . GLY A 1 188 ? 107.69600 104.92600 128.40400 1.000 24.95745 ? 188 GLY A N   1 
ATOM   1154 C CA  . GLY A 1 188 ? 107.21100 103.74400 127.74000 1.000 24.95745 ? 188 GLY A CA  1 
ATOM   1155 C C   . GLY A 1 188 ? 108.25100 102.99300 126.93900 1.000 24.95745 ? 188 GLY A C   1 
ATOM   1156 O O   . GLY A 1 188 ? 107.94500 101.91800 126.41900 1.000 24.95745 ? 188 GLY A O   1 
ATOM   1157 N N   . TYR A 1 189 ? 109.46400 103.52200 126.82000 1.000 27.46811 ? 189 TYR A N   1 
ATOM   1158 C CA  . TYR A 1 189 ? 110.55900 102.82300 126.16400 1.000 27.46811 ? 189 TYR A CA  1 
ATOM   1159 C C   . TYR A 1 189 ? 111.27300 101.93700 127.17000 1.000 27.46811 ? 189 TYR A C   1 
ATOM   1160 O O   . TYR A 1 189 ? 111.53400 102.35100 128.30100 1.000 27.46811 ? 189 TYR A O   1 
ATOM   1161 C CB  . TYR A 1 189 ? 111.54700 103.80600 125.54100 1.000 27.46811 ? 189 TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 189 ? 111.00800 104.54800 124.35000 1.000 27.46811 ? 189 TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 189 ? 110.98100 103.95600 123.09800 1.000 27.46811 ? 189 TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 189 ? 110.52700 105.84100 124.47600 1.000 27.46811 ? 189 TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 189 ? 110.49500 104.63100 122.00600 1.000 27.46811 ? 189 TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 189 ? 110.03600 106.52300 123.39100 1.000 27.46811 ? 189 TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 189 ? 110.02100 105.91200 122.15800 1.000 27.46811 ? 189 TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 189 ? 109.53300 106.59100 121.07300 1.000 27.46811 ? 189 TYR A OH  1 
ATOM   1169 N N   . THR A 1 190 ? 111.61000 100.72900 126.74000 1.000 31.69660 ? 190 THR A N   1 
ATOM   1170 C CA  . THR A 1 190 ? 112.02400 99.65400  127.62600 1.000 31.69660 ? 190 THR A CA  1 
ATOM   1171 C C   . THR A 1 190 ? 113.35700 99.07300  127.17500 1.000 31.69660 ? 190 THR A C   1 
ATOM   1172 O O   . THR A 1 190 ? 113.58500 98.87200  125.98100 1.000 31.69660 ? 190 THR A O   1 
ATOM   1173 C CB  . THR A 1 190 ? 110.92800 98.56400  127.66400 1.000 31.69660 ? 190 THR A CB  1 
ATOM   1174 O OG1 . THR A 1 190 ? 109.89400 98.94800  128.57700 1.000 31.69660 ? 190 THR A OG1 1 
ATOM   1175 C CG2 . THR A 1 190 ? 111.47900 97.20800  128.05700 1.000 31.69660 ? 190 THR A CG2 1 
ATOM   1176 N N   . GLU A 1 191 ? 114.24400 98.83400  128.13800 1.000 34.61983 ? 191 GLU A N   1 
ATOM   1177 C CA  . GLU A 1 191 ? 115.44300 98.03400  127.93900 1.000 34.61983 ? 191 GLU A CA  1 
ATOM   1178 C C   . GLU A 1 191 ? 115.44800 96.88900  128.93800 1.000 34.61983 ? 191 GLU A C   1 
ATOM   1179 O O   . GLU A 1 191 ? 115.09700 97.07100  130.10300 1.000 34.61983 ? 191 GLU A O   1 
ATOM   1180 C CB  . GLU A 1 191 ? 116.72400 98.86400  128.08900 1.000 34.61983 ? 191 GLU A CB  1 
ATOM   1181 C CG  . GLU A 1 191 ? 116.98700 99.78800  126.92000 1.000 34.61983 ? 191 GLU A CG  1 
ATOM   1182 C CD  . GLU A 1 191 ? 118.34800 99.57400  126.28900 1.000 34.61983 ? 191 GLU A CD  1 
ATOM   1183 O OE1 . GLU A 1 191 ? 119.23800 100.41800 126.48800 1.000 34.61983 ? 191 GLU A OE1 1 
ATOM   1184 O OE2 . GLU A 1 191 ? 118.52700 98.55700  125.59100 1.000 34.61983 ? 191 GLU A OE2 1 
ATOM   1185 N N   . LYS A 1 192 ? 115.83200 95.70700  128.46400 1.000 36.22174 ? 192 LYS A N   1 
ATOM   1186 C CA  . LYS A 1 192 ? 115.92800 94.52600  129.31200 1.000 36.22174 ? 192 LYS A CA  1 
ATOM   1187 C C   . LYS A 1 192 ? 116.95600 94.76100  130.41400 1.000 36.22174 ? 192 LYS A C   1 
ATOM   1188 O O   . LYS A 1 192 ? 118.04200 95.28600  130.16900 1.000 36.22174 ? 192 LYS A O   1 
ATOM   1189 C CB  . LYS A 1 192 ? 116.32000 93.32000  128.45300 1.000 36.22174 ? 192 LYS A CB  1 
ATOM   1190 C CG  . LYS A 1 192 ? 116.39800 91.93500  129.10300 1.000 36.22174 ? 192 LYS A CG  1 
ATOM   1191 C CD  . LYS A 1 192 ? 115.43500 91.72500  130.25800 1.000 36.22174 ? 192 LYS A CD  1 
ATOM   1192 C CE  . LYS A 1 192 ? 115.97400 90.71000  131.25100 1.000 36.22174 ? 192 LYS A CE  1 
ATOM   1193 N NZ  . LYS A 1 192 ? 115.28700 90.77000  132.56500 1.000 36.22174 ? 192 LYS A NZ  1 
ATOM   1194 N N   . TRP A 1 193 ? 116.59400 94.39300  131.63600 1.000 33.83315 ? 193 TRP A N   1 
ATOM   1195 C CA  . TRP A 1 193 ? 117.52000 94.47300  132.75600 1.000 33.83315 ? 193 TRP A CA  1 
ATOM   1196 C C   . TRP A 1 193 ? 118.67800 93.49900  132.56800 1.000 33.83315 ? 193 TRP A C   1 
ATOM   1197 O O   . TRP A 1 193 ? 118.47200 92.31200  132.31400 1.000 33.83315 ? 193 TRP A O   1 
ATOM   1198 C CB  . TRP A 1 193 ? 116.78000 94.17100  134.05900 1.000 33.83315 ? 193 TRP A CB  1 
ATOM   1199 C CG  . TRP A 1 193 ? 117.54400 94.49200  135.30500 1.000 33.83315 ? 193 TRP A CG  1 
ATOM   1200 C CD1 . TRP A 1 193 ? 117.42600 95.61200  136.06300 1.000 33.83315 ? 193 TRP A CD1 1 
ATOM   1201 C CD2 . TRP A 1 193 ? 118.51900 93.66900  135.95600 1.000 33.83315 ? 193 TRP A CD2 1 
ATOM   1202 N NE1 . TRP A 1 193 ? 118.27300 95.55000  137.13700 1.000 33.83315 ? 193 TRP A NE1 1 
ATOM   1203 C CE2 . TRP A 1 193 ? 118.95500 94.36500  137.09500 1.000 33.83315 ? 193 TRP A CE2 1 
ATOM   1204 C CE3 . TRP A 1 193 ? 119.06800 92.41500  135.68400 1.000 33.83315 ? 193 TRP A CE3 1 
ATOM   1205 C CZ2 . TRP A 1 193 ? 119.91500 93.85200  137.95900 1.000 33.83315 ? 193 TRP A CZ2 1 
ATOM   1206 C CZ3 . TRP A 1 193 ? 120.02200 91.90900  136.53900 1.000 33.83315 ? 193 TRP A CZ3 1 
ATOM   1207 C CH2 . TRP A 1 193 ? 120.43700 92.62500  137.66200 1.000 33.83315 ? 193 TRP A CH2 1 
ATOM   1208 N N   . GLU A 1 194 ? 119.89800 94.00000  132.70700 1.000 35.30156 ? 194 GLU A N   1 
ATOM   1209 C CA  . GLU A 1 194 ? 121.08600 93.15500  132.73900 1.000 35.30156 ? 194 GLU A CA  1 
ATOM   1210 C C   . GLU A 1 194 ? 121.97200 93.42000  133.93800 1.000 35.30156 ? 194 GLU A C   1 
ATOM   1211 O O   . GLU A 1 194 ? 122.84800 92.59700  134.22500 1.000 35.30156 ? 194 GLU A O   1 
ATOM   1212 C CB  . GLU A 1 194 ? 121.92400 93.34000  131.46200 1.000 35.30156 ? 194 GLU A CB  1 
ATOM   1213 C CG  . GLU A 1 194 ? 121.22000 93.05700  130.13000 1.000 35.30156 ? 194 GLU A CG  1 
ATOM   1214 C CD  . GLU A 1 194 ? 120.67900 91.63500  129.96300 1.000 35.30156 ? 194 GLU A CD  1 
ATOM   1215 O OE1 . GLU A 1 194 ? 120.95600 90.74500  130.79300 1.000 35.30156 ? 194 GLU A OE1 1 
ATOM   1216 O OE2 . GLU A 1 194 ? 119.95500 91.40600  128.97400 1.000 35.30156 ? 194 GLU A OE2 1 
ATOM   1217 N N   . SER A 1 195 ? 121.76000 94.51700  134.65500 1.000 33.37485 ? 195 SER A N   1 
ATOM   1218 C CA  . SER A 1 195 ? 122.63400 94.98400  135.72000 1.000 33.37485 ? 195 SER A CA  1 
ATOM   1219 C C   . SER A 1 195 ? 121.94400 96.15700  136.40000 1.000 33.37485 ? 195 SER A C   1 
ATOM   1220 O O   . SER A 1 195 ? 120.87500 96.60100  135.97600 1.000 33.37485 ? 195 SER A O   1 
ATOM   1221 C CB  . SER A 1 195 ? 124.00200 95.38600  135.17400 1.000 33.37485 ? 195 SER A CB  1 
ATOM   1222 O OG  . SER A 1 195 ? 123.84200 96.16500  134.01000 1.000 33.37485 ? 195 SER A OG  1 
ATOM   1223 N N   . GLY A 1 196 ? 122.58000 96.66500  137.44600 1.000 32.65559 ? 196 GLY A N   1 
ATOM   1224 C CA  . GLY A 1 196 ? 121.98800 97.71800  138.24200 1.000 32.65559 ? 196 GLY A CA  1 
ATOM   1225 C C   . GLY A 1 196 ? 122.11300 99.09300  137.61400 1.000 32.65559 ? 196 GLY A C   1 
ATOM   1226 O O   . GLY A 1 196 ? 122.70500 99.29300  136.55400 1.000 32.65559 ? 196 GLY A O   1 
ATOM   1227 N N   . VAL A 1 197 ? 121.51300 100.06300 138.30000 1.000 32.26269 ? 197 VAL A N   1 
ATOM   1228 C CA  . VAL A 1 197 ? 121.60400 101.45700 137.88900 1.000 32.26269 ? 197 VAL A CA  1 
ATOM   1229 C C   . VAL A 1 197 ? 122.96200 102.02400 138.28500 1.000 32.26269 ? 197 VAL A C   1 
ATOM   1230 O O   . VAL A 1 197 ? 123.65100 101.51400 139.17000 1.000 32.26269 ? 197 VAL A O   1 
ATOM   1231 C CB  . VAL A 1 197 ? 120.46000 102.29500 138.49400 1.000 32.26269 ? 197 VAL A CB  1 
ATOM   1232 C CG1 . VAL A 1 197 ? 119.12200 101.82100 137.99700 1.000 32.26269 ? 197 VAL A CG1 1 
ATOM   1233 C CG2 . VAL A 1 197 ? 120.50900 102.25100 140.00900 1.000 32.26269 ? 197 VAL A CG2 1 
ATOM   1234 N N   . LYS A 1 198 ? 123.34400 103.10400 137.62000 1.000 33.63846 ? 198 LYS A N   1 
ATOM   1235 C CA  . LYS A 1 198 ? 124.52500 103.86700 137.98600 1.000 33.63846 ? 198 LYS A CA  1 
ATOM   1236 C C   . LYS A 1 198 ? 124.11400 105.16400 138.67200 1.000 33.63846 ? 198 LYS A C   1 
ATOM   1237 O O   . LYS A 1 198 ? 122.99500 105.65400 138.51600 1.000 33.63846 ? 198 LYS A O   1 
ATOM   1238 C CB  . LYS A 1 198 ? 125.38700 104.15800 136.75400 1.000 33.63846 ? 198 LYS A CB  1 
ATOM   1239 C CG  . LYS A 1 198 ? 126.11300 102.94500 136.21900 1.000 33.63846 ? 198 LYS A CG  1 
ATOM   1240 C CD  . LYS A 1 198 ? 126.98400 102.31600 137.28800 1.000 33.63846 ? 198 LYS A CD  1 
ATOM   1241 C CE  . LYS A 1 198 ? 127.87800 101.23600 136.71500 1.000 33.63846 ? 198 LYS A CE  1 
ATOM   1242 N NZ  . LYS A 1 198 ? 129.11100 101.80300 136.10700 1.000 33.63846 ? 198 LYS A NZ  1 
ATOM   1243 N N   . ASP A 1 199 ? 125.04400 105.71900 139.44700 1.000 35.47202 ? 199 ASP A N   1 
ATOM   1244 C CA  . ASP A 1 199 ? 124.78900 106.98300 140.12300 1.000 35.47202 ? 199 ASP A CA  1 
ATOM   1245 C C   . ASP A 1 199 ? 124.79400 108.16200 139.16300 1.000 35.47202 ? 199 ASP A C   1 
ATOM   1246 O O   . ASP A 1 199 ? 124.28400 109.23000 139.51200 1.000 35.47202 ? 199 ASP A O   1 
ATOM   1247 C CB  . ASP A 1 199 ? 125.82300 107.20400 141.22300 1.000 35.47202 ? 199 ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 199 ? 125.59700 106.30800 142.41700 1.000 35.47202 ? 199 ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 199 ? 124.47700 105.77500 142.55600 1.000 35.47202 ? 199 ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 199 ? 126.53900 106.13000 143.21700 1.000 35.47202 ? 199 ASP A OD2 1 
ATOM   1251 N N   . CYS A 1 200 ? 125.35900 107.99600 137.97100 1.000 35.20511 ? 200 CYS A N   1 
ATOM   1252 C CA  . CYS A 1 200 ? 125.38200 109.05000 136.96700 1.000 35.20511 ? 200 CYS A CA  1 
ATOM   1253 C C   . CYS A 1 200 ? 124.96900 108.45800 135.63100 1.000 35.20511 ? 200 CYS A C   1 
ATOM   1254 O O   . CYS A 1 200 ? 125.51500 107.43800 135.20600 1.000 35.20511 ? 200 CYS A O   1 
ATOM   1255 C CB  . CYS A 1 200 ? 126.77000 109.69000 136.86700 1.000 35.20511 ? 200 CYS A CB  1 
ATOM   1256 S SG  . CYS A 1 200 ? 126.83300 111.18000 135.84600 1.000 35.20511 ? 200 CYS A SG  1 
ATOM   1257 N N   . VAL A 1 201 ? 124.00800 109.09600 134.97600 1.000 28.39083 ? 201 VAL A N   1 
ATOM   1258 C CA  . VAL A 1 201 ? 123.62000 108.74300 133.61700 1.000 28.39083 ? 201 VAL A CA  1 
ATOM   1259 C C   . VAL A 1 201 ? 123.85800 109.95800 132.73200 1.000 28.39083 ? 201 VAL A C   1 
ATOM   1260 O O   . VAL A 1 201 ? 124.07600 111.06900 133.21400 1.000 28.39083 ? 201 VAL A O   1 
ATOM   1261 C CB  . VAL A 1 201 ? 122.15800 108.26200 133.53000 1.000 28.39083 ? 201 VAL A CB  1 
ATOM   1262 C CG1 . VAL A 1 201 ? 121.97600 106.98700 134.32700 1.000 28.39083 ? 201 VAL A CG1 1 
ATOM   1263 C CG2 . VAL A 1 201 ? 121.21500 109.33600 134.01500 1.000 28.39083 ? 201 VAL A CG2 1 
ATOM   1264 N N   . VAL A 1 202 ? 123.84300 109.74800 131.41900 1.000 28.66332 ? 202 VAL A N   1 
ATOM   1265 C CA  . VAL A 1 202 ? 124.14900 110.83600 130.49800 1.000 28.66332 ? 202 VAL A CA  1 
ATOM   1266 C C   . VAL A 1 202 ? 123.14300 110.84600 129.35400 1.000 28.66332 ? 202 VAL A C   1 
ATOM   1267 O O   . VAL A 1 202 ? 122.85100 109.80700 128.76100 1.000 28.66332 ? 202 VAL A O   1 
ATOM   1268 C CB  . VAL A 1 202 ? 125.60200 110.75400 129.98100 1.000 28.66332 ? 202 VAL A CB  1 
ATOM   1269 C CG1 . VAL A 1 202 ? 125.90800 109.39700 129.36000 1.000 28.66332 ? 202 VAL A CG1 1 
ATOM   1270 C CG2 . VAL A 1 202 ? 125.89700 111.89300 129.02100 1.000 28.66332 ? 202 VAL A CG2 1 
ATOM   1271 N N   . LEU A 1 203 ? 122.60600 112.02000 129.05800 1.000 28.27066 ? 203 LEU A N   1 
ATOM   1272 C CA  . LEU A 1 203 ? 121.73900 112.23400 127.91200 1.000 28.27066 ? 203 LEU A CA  1 
ATOM   1273 C C   . LEU A 1 203 ? 122.58900 112.73000 126.75000 1.000 28.27066 ? 203 LEU A C   1 
ATOM   1274 O O   . LEU A 1 203 ? 123.23800 113.77500 126.85400 1.000 28.27066 ? 203 LEU A O   1 
ATOM   1275 C CB  . LEU A 1 203 ? 120.64600 113.24100 128.26300 1.000 28.27066 ? 203 LEU A CB  1 
ATOM   1276 C CG  . LEU A 1 203 ? 119.34700 113.25700 127.46200 1.000 28.27066 ? 203 LEU A CG  1 
ATOM   1277 C CD1 . LEU A 1 203 ? 118.58100 111.95800 127.61700 1.000 28.27066 ? 203 LEU A CD1 1 
ATOM   1278 C CD2 . LEU A 1 203 ? 118.50100 114.44300 127.89400 1.000 28.27066 ? 203 LEU A CD2 1 
ATOM   1279 N N   . HIS A 1 204 ? 122.58800 111.98000 125.65500 1.000 30.85524 ? 204 HIS A N   1 
ATOM   1280 C CA  . HIS A 1 204 ? 123.36600 112.29000 124.46800 1.000 30.85524 ? 204 HIS A CA  1 
ATOM   1281 C C   . HIS A 1 204 ? 122.46100 112.74500 123.33300 1.000 30.85524 ? 204 HIS A C   1 
ATOM   1282 O O   . HIS A 1 204 ? 121.37800 112.19800 123.12000 1.000 30.85524 ? 204 HIS A O   1 
ATOM   1283 C CB  . HIS A 1 204 ? 124.16200 111.07600 123.98800 1.000 30.85524 ? 204 HIS A CB  1 
ATOM   1284 C CG  . HIS A 1 204 ? 125.32900 110.72400 124.85300 1.000 30.85524 ? 204 HIS A CG  1 
ATOM   1285 N ND1 . HIS A 1 204 ? 126.27300 111.64700 125.24300 1.000 30.85524 ? 204 HIS A ND1 1 
ATOM   1286 C CD2 . HIS A 1 204 ? 125.72600 109.53800 125.37000 1.000 30.85524 ? 204 HIS A CD2 1 
ATOM   1287 C CE1 . HIS A 1 204 ? 127.19500 111.04700 125.97300 1.000 30.85524 ? 204 HIS A CE1 1 
ATOM   1288 N NE2 . HIS A 1 204 ? 126.88400 109.76700 126.06700 1.000 30.85524 ? 204 HIS A NE2 1 
ATOM   1289 N N   . SER A 1 205 ? 122.92900 113.75100 122.60000 1.000 36.92194 ? 205 SER A N   1 
ATOM   1290 C CA  . SER A 1 205 ? 122.39500 114.09900 121.29300 1.000 36.92194 ? 205 SER A CA  1 
ATOM   1291 C C   . SER A 1 205 ? 123.55700 114.14100 120.31400 1.000 36.92194 ? 205 SER A C   1 
ATOM   1292 O O   . SER A 1 205 ? 124.66400 113.69300 120.62200 1.000 36.92194 ? 205 SER A O   1 
ATOM   1293 C CB  . SER A 1 205 ? 121.63700 115.42800 121.31900 1.000 36.92194 ? 205 SER A CB  1 
ATOM   1294 O OG  . SER A 1 205 ? 122.49500 116.51600 121.59300 1.000 36.92194 ? 205 SER A OG  1 
ATOM   1295 N N   . TYR A 1 206 ? 123.29100 114.67600 119.11900 1.000 42.55383 ? 206 TYR A N   1 
ATOM   1296 C CA  . TYR A 1 206 ? 124.34500 114.86600 118.12500 1.000 42.55383 ? 206 TYR A CA  1 
ATOM   1297 C C   . TYR A 1 206 ? 125.47300 115.73200 118.66600 1.000 42.55383 ? 206 TYR A C   1 
ATOM   1298 O O   . TYR A 1 206 ? 126.65100 115.40400 118.50100 1.000 42.55383 ? 206 TYR A O   1 
ATOM   1299 C CB  . TYR A 1 206 ? 123.77700 115.51800 116.86600 1.000 42.55383 ? 206 TYR A CB  1 
ATOM   1300 C CG  . TYR A 1 206 ? 122.85800 114.66800 116.03100 1.000 42.55383 ? 206 TYR A CG  1 
ATOM   1301 C CD1 . TYR A 1 206 ? 123.14200 113.33700 115.77000 1.000 42.55383 ? 206 TYR A CD1 1 
ATOM   1302 C CD2 . TYR A 1 206 ? 121.70900 115.21200 115.48300 1.000 42.55383 ? 206 TYR A CD2 1 
ATOM   1303 C CE1 . TYR A 1 206 ? 122.29600 112.57300 114.99600 1.000 42.55383 ? 206 TYR A CE1 1 
ATOM   1304 C CE2 . TYR A 1 206 ? 120.86200 114.46000 114.71300 1.000 42.55383 ? 206 TYR A CE2 1 
ATOM   1305 C CZ  . TYR A 1 206 ? 121.15800 113.14400 114.46900 1.000 42.55383 ? 206 TYR A CZ  1 
ATOM   1306 O OH  . TYR A 1 206 ? 120.30100 112.40600 113.69500 1.000 42.55383 ? 206 TYR A OH  1 
ATOM   1307 N N   . PHE A 1 207 ? 125.13100 116.83500 119.32900 1.000 47.02366 ? 207 PHE A N   1 
ATOM   1308 C CA  . PHE A 1 207 ? 126.10800 117.84400 119.69800 1.000 47.02366 ? 207 PHE A CA  1 
ATOM   1309 C C   . PHE A 1 207 ? 126.23200 118.08900 121.19200 1.000 47.02366 ? 207 PHE A C   1 
ATOM   1310 O O   . PHE A 1 207 ? 127.18700 118.75300 121.60700 1.000 47.02366 ? 207 PHE A O   1 
ATOM   1311 C CB  . PHE A 1 207 ? 125.77500 119.17000 119.00000 1.000 47.02366 ? 207 PHE A CB  1 
ATOM   1312 C CG  . PHE A 1 207 ? 125.44800 119.01100 117.54800 1.000 47.02366 ? 207 PHE A CG  1 
ATOM   1313 C CD1 . PHE A 1 207 ? 124.16500 119.22800 117.08600 1.000 47.02366 ? 207 PHE A CD1 1 
ATOM   1314 C CD2 . PHE A 1 207 ? 126.42100 118.61700 116.64900 1.000 47.02366 ? 207 PHE A CD2 1 
ATOM   1315 C CE1 . PHE A 1 207 ? 123.86400 119.07100 115.75200 1.000 47.02366 ? 207 PHE A CE1 1 
ATOM   1316 C CE2 . PHE A 1 207 ? 126.12400 118.45800 115.32000 1.000 47.02366 ? 207 PHE A CE2 1 
ATOM   1317 C CZ  . PHE A 1 207 ? 124.84600 118.68400 114.86900 1.000 47.02366 ? 207 PHE A CZ  1 
ATOM   1318 N N   . THR A 1 208 ? 125.31800 117.57500 122.01100 1.000 39.44602 ? 208 THR A N   1 
ATOM   1319 C CA  . THR A 1 208 ? 125.29600 117.88100 123.43200 1.000 39.44602 ? 208 THR A CA  1 
ATOM   1320 C C   . THR A 1 208 ? 125.34400 116.60300 124.25500 1.000 39.44602 ? 208 THR A C   1 
ATOM   1321 O O   . THR A 1 208 ? 124.96500 115.52600 123.79200 1.000 39.44602 ? 208 THR A O   1 
ATOM   1322 C CB  . THR A 1 208 ? 124.04400 118.68900 123.82500 1.000 39.44602 ? 208 THR A CB  1 
ATOM   1323 O OG1 . THR A 1 208 ? 122.87700 117.87100 123.68500 1.000 39.44602 ? 208 THR A OG1 1 
ATOM   1324 C CG2 . THR A 1 208 ? 123.89600 119.92300 122.95500 1.000 39.44602 ? 208 THR A CG2 1 
ATOM   1325 N N   . SER A 1 209 ? 125.83200 116.74100 125.48400 1.000 35.57888 ? 209 SER A N   1 
ATOM   1326 C CA  . SER A 1 209 ? 125.77100 115.69600 126.49500 1.000 35.57888 ? 209 SER A CA  1 
ATOM   1327 C C   . SER A 1 209 ? 125.47900 116.34700 127.83600 1.000 35.57888 ? 209 SER A C   1 
ATOM   1328 O O   . SER A 1 209 ? 126.18800 117.26700 128.25000 1.000 35.57888 ? 209 SER A O   1 
ATOM   1329 C CB  . SER A 1 209 ? 127.07200 114.89700 126.56300 1.000 35.57888 ? 209 SER A CB  1 
ATOM   1330 O OG  . SER A 1 209 ? 127.25800 114.13100 125.39000 1.000 35.57888 ? 209 SER A OG  1 
ATOM   1331 N N   . ASP A 1 210 ? 124.44000 115.87300 128.50800 1.000 33.15853 ? 210 ASP A N   1 
ATOM   1332 C CA  . ASP A 1 210 ? 124.05400 116.39000 129.81200 1.000 33.15853 ? 210 ASP A CA  1 
ATOM   1333 C C   . ASP A 1 210 ? 124.08700 115.26300 130.83100 1.000 33.15853 ? 210 ASP A C   1 
ATOM   1334 O O   . ASP A 1 210 ? 123.59000 114.17200 130.57200 1.000 33.15853 ? 210 ASP A O   1 
ATOM   1335 C CB  . ASP A 1 210 ? 122.66400 117.02800 129.76000 1.000 33.15853 ? 210 ASP A CB  1 
ATOM   1336 C CG  . ASP A 1 210 ? 122.63600 118.28600 128.91600 1.000 33.15853 ? 210 ASP A CG  1 
ATOM   1337 O OD1 . ASP A 1 210 ? 122.18200 118.22000 127.75600 1.000 33.15853 ? 210 ASP A OD1 1 
ATOM   1338 O OD2 . ASP A 1 210 ? 123.08000 119.34300 129.40600 1.000 33.15853 ? 210 ASP A OD2 1 
ATOM   1339 N N   . TYR A 1 211 ? 124.66800 115.52200 131.99200 1.000 32.18925 ? 211 TYR A N   1 
ATOM   1340 C CA  . TYR A 1 211 ? 124.86000 114.48700 132.99600 1.000 32.18925 ? 211 TYR A CA  1 
ATOM   1341 C C   . TYR A 1 211 ? 123.83600 114.62500 134.11200 1.000 32.18925 ? 211 TYR A C   1 
ATOM   1342 O O   . TYR A 1 211 ? 123.46300 115.73600 134.49500 1.000 32.18925 ? 211 TYR A O   1 
ATOM   1343 C CB  . TYR A 1 211 ? 126.28200 114.52500 133.55600 1.000 32.18925 ? 211 TYR A CB  1 
ATOM   1344 C CG  . TYR A 1 211 ? 127.30700 114.10700 132.53400 1.000 32.18925 ? 211 TYR A CG  1 
ATOM   1345 C CD1 . TYR A 1 211 ? 127.78100 112.80700 132.49800 1.000 32.18925 ? 211 TYR A CD1 1 
ATOM   1346 C CD2 . TYR A 1 211 ? 127.78400 115.00400 131.58800 1.000 32.18925 ? 211 TYR A CD2 1 
ATOM   1347 C CE1 . TYR A 1 211 ? 128.70800 112.41400 131.56200 1.000 32.18925 ? 211 TYR A CE1 1 
ATOM   1348 C CE2 . TYR A 1 211 ? 128.70600 114.61900 130.64800 1.000 32.18925 ? 211 TYR A CE2 1 
ATOM   1349 C CZ  . TYR A 1 211 ? 129.16700 113.32400 130.64000 1.000 32.18925 ? 211 TYR A CZ  1 
ATOM   1350 O OH  . TYR A 1 211 ? 130.09200 112.93600 129.70500 1.000 32.18925 ? 211 TYR A OH  1 
ATOM   1351 N N   . TYR A 1 212 ? 123.37400 113.48500 134.61200 1.000 28.82555 ? 212 TYR A N   1 
ATOM   1352 C CA  . TYR A 1 212 ? 122.34700 113.42100 135.63700 1.000 28.82555 ? 212 TYR A CA  1 
ATOM   1353 C C   . TYR A 1 212 ? 122.86300 112.57400 136.78600 1.000 28.82555 ? 212 TYR A C   1 
ATOM   1354 O O   . TYR A 1 212 ? 123.44600 111.50800 136.56500 1.000 28.82555 ? 212 TYR A O   1 
ATOM   1355 C CB  . TYR A 1 212 ? 121.04100 112.83800 135.08300 1.000 28.82555 ? 212 TYR A CB  1 
ATOM   1356 C CG  . TYR A 1 212 ? 120.32000 113.74500 134.11000 1.000 28.82555 ? 212 TYR A CG  1 
ATOM   1357 C CD1 . TYR A 1 212 ? 119.18800 114.44600 134.49500 1.000 28.82555 ? 212 TYR A CD1 1 
ATOM   1358 C CD2 . TYR A 1 212 ? 120.77100 113.89600 132.80600 1.000 28.82555 ? 212 TYR A CD2 1 
ATOM   1359 C CE1 . TYR A 1 212 ? 118.53100 115.27500 133.61400 1.000 28.82555 ? 212 TYR A CE1 1 
ATOM   1360 C CE2 . TYR A 1 212 ? 120.12600 114.72300 131.92100 1.000 28.82555 ? 212 TYR A CE2 1 
ATOM   1361 C CZ  . TYR A 1 212 ? 119.00800 115.41000 132.32700 1.000 28.82555 ? 212 TYR A CZ  1 
ATOM   1362 O OH  . TYR A 1 212 ? 118.36300 116.22800 131.44000 1.000 28.82555 ? 212 TYR A OH  1 
ATOM   1363 N N   . GLN A 1 213 ? 122.64700 113.05400 138.00200 1.000 30.88550 ? 213 GLN A N   1 
ATOM   1364 C CA  . GLN A 1 213 ? 123.07900 112.39600 139.22200 1.000 30.88550 ? 213 GLN A CA  1 
ATOM   1365 C C   . GLN A 1 213 ? 121.86900 111.79600 139.92400 1.000 30.88550 ? 213 GLN A C   1 
ATOM   1366 O O   . GLN A 1 213 ? 120.82200 112.43800 140.02400 1.000 30.88550 ? 213 GLN A O   1 
ATOM   1367 C CB  . GLN A 1 213 ? 123.79700 113.39400 140.13500 1.000 30.88550 ? 213 GLN A CB  1 
ATOM   1368 C CG  . GLN A 1 213 ? 124.07800 112.91000 141.54300 1.000 30.88550 ? 213 GLN A CG  1 
ATOM   1369 C CD  . GLN A 1 213 ? 125.13900 111.83800 141.59400 1.000 30.88550 ? 213 GLN A CD  1 
ATOM   1370 O OE1 . GLN A 1 213 ? 126.14100 111.90500 140.88400 1.000 30.88550 ? 213 GLN A OE1 1 
ATOM   1371 N NE2 . GLN A 1 213 ? 124.92700 110.83500 142.44000 1.000 30.88550 ? 213 GLN A NE2 1 
ATOM   1372 N N   . LEU A 1 214 ? 122.01000 110.56200 140.39900 1.000 29.02749 ? 214 LEU A N   1 
ATOM   1373 C CA  . LEU A 1 214 ? 120.92500 109.89600 141.10700 1.000 29.02749 ? 214 LEU A CA  1 
ATOM   1374 C C   . LEU A 1 214 ? 120.68700 110.57000 142.45200 1.000 29.02749 ? 214 LEU A C   1 
ATOM   1375 O O   . LEU A 1 214 ? 121.57900 110.60400 143.30300 1.000 29.02749 ? 214 LEU A O   1 
ATOM   1376 C CB  . LEU A 1 214 ? 121.24800 108.41800 141.30100 1.000 29.02749 ? 214 LEU A CB  1 
ATOM   1377 C CG  . LEU A 1 214 ? 120.18200 107.61400 142.05000 1.000 29.02749 ? 214 LEU A CG  1 
ATOM   1378 C CD1 . LEU A 1 214 ? 118.89600 107.55200 141.24800 1.000 29.02749 ? 214 LEU A CD1 1 
ATOM   1379 C CD2 . LEU A 1 214 ? 120.68200 106.22600 142.38900 1.000 29.02749 ? 214 LEU A CD2 1 
ATOM   1380 N N   . TYR A 1 215 ? 119.48600 111.11100 142.64300 1.000 32.84508 ? 215 TYR A N   1 
ATOM   1381 C CA  . TYR A 1 215 ? 119.12700 111.82400 143.85800 1.000 32.84508 ? 215 TYR A CA  1 
ATOM   1382 C C   . TYR A 1 215 ? 118.26400 111.01600 144.80700 1.000 32.84508 ? 215 TYR A C   1 
ATOM   1383 O O   . TYR A 1 215 ? 118.35500 111.21500 146.01700 1.000 32.84508 ? 215 TYR A O   1 
ATOM   1384 C CB  . TYR A 1 215 ? 118.37900 113.11400 143.51100 1.000 32.84508 ? 215 TYR A CB  1 
ATOM   1385 C CG  . TYR A 1 215 ? 119.24800 114.34100 143.47500 1.000 32.84508 ? 215 TYR A CG  1 
ATOM   1386 C CD1 . TYR A 1 215 ? 118.79700 115.54800 143.98600 1.000 32.84508 ? 215 TYR A CD1 1 
ATOM   1387 C CD2 . TYR A 1 215 ? 120.51900 114.29500 142.92500 1.000 32.84508 ? 215 TYR A CD2 1 
ATOM   1388 C CE1 . TYR A 1 215 ? 119.59100 116.67300 143.95000 1.000 32.84508 ? 215 TYR A CE1 1 
ATOM   1389 C CE2 . TYR A 1 215 ? 121.31800 115.41000 142.88500 1.000 32.84508 ? 215 TYR A CE2 1 
ATOM   1390 C CZ  . TYR A 1 215 ? 120.85100 116.59700 143.39800 1.000 32.84508 ? 215 TYR A CZ  1 
ATOM   1391 O OH  . TYR A 1 215 ? 121.64900 117.71100 143.35600 1.000 32.84508 ? 215 TYR A OH  1 
ATOM   1392 N N   . SER A 1 216 ? 117.43400 110.11500 144.29300 1.000 32.79082 ? 216 SER A N   1 
ATOM   1393 C CA  . SER A 1 216 ? 116.44000 109.45300 145.11700 1.000 32.79082 ? 216 SER A CA  1 
ATOM   1394 C C   . SER A 1 216 ? 116.06300 108.12100 144.49100 1.000 32.79082 ? 216 SER A C   1 
ATOM   1395 O O   . SER A 1 216 ? 116.05300 107.97200 143.26900 1.000 32.79082 ? 216 SER A O   1 
ATOM   1396 C CB  . SER A 1 216 ? 115.19700 110.33500 145.29000 1.000 32.79082 ? 216 SER A CB  1 
ATOM   1397 O OG  . SER A 1 216 ? 114.26200 109.73600 146.16100 1.000 32.79082 ? 216 SER A OG  1 
ATOM   1398 N N   . THR A 1 217 ? 115.74900 107.15600 145.34800 1.000 33.59834 ? 217 THR A N   1 
ATOM   1399 C CA  . THR A 1 217 ? 115.28800 105.83300 144.94200 1.000 33.59834 ? 217 THR A CA  1 
ATOM   1400 C C   . THR A 1 217 ? 113.96500 105.56800 145.64800 1.000 33.59834 ? 217 THR A C   1 
ATOM   1401 O O   . THR A 1 217 ? 113.92800 105.44300 146.87500 1.000 33.59834 ? 217 THR A O   1 
ATOM   1402 C CB  . THR A 1 217 ? 116.32000 104.75800 145.28500 1.000 33.59834 ? 217 THR A CB  1 
ATOM   1403 O OG1 . THR A 1 217 ? 117.57500 105.08800 144.68000 1.000 33.59834 ? 217 THR A OG1 1 
ATOM   1404 C CG2 . THR A 1 217 ? 115.86700 103.40500 144.79100 1.000 33.59834 ? 217 THR A CG2 1 
ATOM   1405 N N   . GLN A 1 218 ? 112.88600 105.48600 144.88000 1.000 34.65995 ? 218 GLN A N   1 
ATOM   1406 C CA  . GLN A 1 218 ? 111.55400 105.30500 145.43900 1.000 34.65995 ? 218 GLN A CA  1 
ATOM   1407 C C   . GLN A 1 218 ? 111.18600 103.82800 145.40000 1.000 34.65995 ? 218 GLN A C   1 
ATOM   1408 O O   . GLN A 1 218 ? 111.09300 103.23400 144.32200 1.000 34.65995 ? 218 GLN A O   1 
ATOM   1409 C CB  . GLN A 1 218 ? 110.52300 106.13200 144.67200 1.000 34.65995 ? 218 GLN A CB  1 
ATOM   1410 C CG  . GLN A 1 218 ? 110.82400 107.62200 144.57000 1.000 34.65995 ? 218 GLN A CG  1 
ATOM   1411 C CD  . GLN A 1 218 ? 111.11900 108.26200 145.90600 1.000 34.65995 ? 218 GLN A CD  1 
ATOM   1412 O OE1 . GLN A 1 218 ? 112.14200 108.91700 146.07900 1.000 34.65995 ? 218 GLN A OE1 1 
ATOM   1413 N NE2 . GLN A 1 218 ? 110.22100 108.07900 146.85900 1.000 34.65995 ? 218 GLN A NE2 1 
ATOM   1414 N N   . LEU A 1 219 ? 110.96400 103.24400 146.56900 1.000 37.39633 ? 219 LEU A N   1 
ATOM   1415 C CA  . LEU A 1 219 ? 110.57200 101.85000 146.69100 1.000 37.39633 ? 219 LEU A CA  1 
ATOM   1416 C C   . LEU A 1 219 ? 109.06100 101.73300 146.84500 1.000 37.39633 ? 219 LEU A C   1 
ATOM   1417 O O   . LEU A 1 219 ? 108.35000 102.72000 147.03500 1.000 37.39633 ? 219 LEU A O   1 
ATOM   1418 C CB  . LEU A 1 219 ? 111.28700 101.19700 147.87400 1.000 37.39633 ? 219 LEU A CB  1 
ATOM   1419 C CG  . LEU A 1 219 ? 112.80700 101.11300 147.74100 1.000 37.39633 ? 219 LEU A CG  1 
ATOM   1420 C CD1 . LEU A 1 219 ? 113.41200 100.48300 148.97700 1.000 37.39633 ? 219 LEU A CD1 1 
ATOM   1421 C CD2 . LEU A 1 219 ? 113.18700 100.33700 146.49800 1.000 37.39633 ? 219 LEU A CD2 1 
ATOM   1422 N N   . SER A 1 220 ? 108.57300 100.49300 146.75700 1.000 39.72717 ? 220 SER A N   1 
ATOM   1423 C CA  . SER A 1 220 ? 107.14100 100.22900 146.85400 1.000 39.72717 ? 220 SER A CA  1 
ATOM   1424 C C   . SER A 1 220 ? 106.55500 100.66000 148.19100 1.000 39.72717 ? 220 SER A C   1 
ATOM   1425 O O   . SER A 1 220 ? 105.36300 100.97200 148.25800 1.000 39.72717 ? 220 SER A O   1 
ATOM   1426 C CB  . SER A 1 220 ? 106.86900 98.74600  146.62400 1.000 39.72717 ? 220 SER A CB  1 
ATOM   1427 O OG  . SER A 1 220 ? 107.41500 98.32000  145.39200 1.000 39.72717 ? 220 SER A OG  1 
ATOM   1428 N N   . THR A 1 221 ? 107.36200 100.68700 149.25200 1.000 43.34708 ? 221 THR A N   1 
ATOM   1429 C CA  . THR A 1 221 ? 106.89600 101.22500 150.52200 1.000 43.34708 ? 221 THR A CA  1 
ATOM   1430 C C   . THR A 1 221 ? 106.77600 102.74100 150.48600 1.000 43.34708 ? 221 THR A C   1 
ATOM   1431 O O   . THR A 1 221 ? 106.04100 103.31900 151.29200 1.000 43.34708 ? 221 THR A O   1 
ATOM   1432 C CB  . THR A 1 221 ? 107.83300 100.79900 151.65000 1.000 43.34708 ? 221 THR A CB  1 
ATOM   1433 O OG1 . THR A 1 221 ? 109.19300 100.98000 151.23900 1.000 43.34708 ? 221 THR A OG1 1 
ATOM   1434 C CG2 . THR A 1 221 ? 107.60600 99.34000  151.99700 1.000 43.34708 ? 221 THR A CG2 1 
ATOM   1435 N N   . ASP A 1 222 ? 107.48500 103.39800 149.56800 1.000 43.04732 ? 222 ASP A N   1 
ATOM   1436 C CA  . ASP A 1 222 ? 107.39200 104.84900 149.45500 1.000 43.04732 ? 222 ASP A CA  1 
ATOM   1437 C C   . ASP A 1 222 ? 106.21800 105.26300 148.57800 1.000 43.04732 ? 222 ASP A C   1 
ATOM   1438 O O   . ASP A 1 222 ? 105.61400 106.31900 148.79600 1.000 43.04732 ? 222 ASP A O   1 
ATOM   1439 C CB  . ASP A 1 222 ? 108.69300 105.41500 148.88500 1.000 43.04732 ? 222 ASP A CB  1 
ATOM   1440 C CG  . ASP A 1 222 ? 109.89000 105.11600 149.75400 1.000 43.04732 ? 222 ASP A CG  1 
ATOM   1441 O OD1 . ASP A 1 222 ? 109.70200 104.86400 150.96300 1.000 43.04732 ? 222 ASP A OD1 1 
ATOM   1442 O OD2 . ASP A 1 222 ? 111.01900 105.11200 149.22200 1.000 43.04732 ? 222 ASP A OD2 1 
ATOM   1443 N N   . THR A 1 223 ? 105.88900 104.45300 147.57400 1.000 37.34691 ? 223 THR A N   1 
ATOM   1444 C CA  . THR A 1 223 ? 104.94500 104.83900 146.53700 1.000 37.34691 ? 223 THR A CA  1 
ATOM   1445 C C   . THR A 1 223 ? 103.65000 104.04800 146.54900 1.000 37.34691 ? 223 THR A C   1 
ATOM   1446 O O   . THR A 1 223 ? 102.62600 104.56700 146.10400 1.000 37.34691 ? 223 THR A O   1 
ATOM   1447 C CB  . THR A 1 223 ? 105.59000 104.69500 145.15100 1.000 37.34691 ? 223 THR A CB  1 
ATOM   1448 O OG1 . THR A 1 223 ? 105.78400 103.31000 144.85000 1.000 37.34691 ? 223 THR A OG1 1 
ATOM   1449 C CG2 . THR A 1 223 ? 106.92800 105.39700 145.11100 1.000 37.34691 ? 223 THR A CG2 1 
ATOM   1450 N N   . GLY A 1 224 ? 103.66600 102.81100 147.04000 1.000 38.27994 ? 224 GLY A N   1 
ATOM   1451 C CA  . GLY A 1 224 ? 102.50900 101.95200 146.98800 1.000 38.27994 ? 224 GLY A CA  1 
ATOM   1452 C C   . GLY A 1 224 ? 102.40200 101.10600 145.74100 1.000 38.27994 ? 224 GLY A C   1 
ATOM   1453 O O   . GLY A 1 224 ? 101.53900 100.22400 145.68500 1.000 38.27994 ? 224 GLY A O   1 
ATOM   1454 N N   . VAL A 1 225 ? 103.25000 101.33600 144.74600 1.000 37.35710 ? 225 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 225 ? 103.24000 100.55500 143.51700 1.000 37.35710 ? 225 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 225 ? 104.13500 99.34100  143.73600 1.000 37.35710 ? 225 VAL A C   1 
ATOM   1457 O O   . VAL A 1 225 ? 105.35700 99.46900  143.82600 1.000 37.35710 ? 225 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 225 ? 103.70900 101.38800 142.31900 1.000 37.35710 ? 225 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 225 ? 103.58200 100.58900 141.03800 1.000 37.35710 ? 225 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 225 ? 102.92200 102.67200 142.22900 1.000 37.35710 ? 225 VAL A CG2 1 
ATOM   1461 N N   . GLU A 1 226 ? 103.52600 98.16200  143.81400 1.000 41.29645 ? 226 GLU A N   1 
ATOM   1462 C CA  . GLU A 1 226 ? 104.27400 96.95000  144.10700 1.000 41.29645 ? 226 GLU A CA  1 
ATOM   1463 C C   . GLU A 1 226 ? 105.12200 96.52500  142.91700 1.000 41.29645 ? 226 GLU A C   1 
ATOM   1464 O O   . GLU A 1 226 ? 104.73400 96.70900  141.76000 1.000 41.29645 ? 226 GLU A O   1 
ATOM   1465 C CB  . GLU A 1 226 ? 103.32500 95.81600  144.50200 1.000 41.29645 ? 226 GLU A CB  1 
ATOM   1466 C CG  . GLU A 1 226 ? 102.13200 96.15400  145.42200 1.000 41.29645 ? 226 GLU A CG  1 
ATOM   1467 C CD  . GLU A 1 226 ? 102.47100 96.75800  146.79700 1.000 41.29645 ? 226 GLU A CD  1 
ATOM   1468 O OE1 . GLU A 1 226 ? 101.76500 96.39300  147.76000 1.000 41.29645 ? 226 GLU A OE1 1 
ATOM   1469 O OE2 . GLU A 1 226 ? 103.38000 97.60300  146.94500 1.000 41.29645 ? 226 GLU A OE2 1 
ATOM   1470 N N   . HIS A 1 227 ? 106.29300 95.96200  143.22300 1.000 41.16450 ? 227 HIS A N   1 
ATOM   1471 C CA  . HIS A 1 227 ? 107.23700 95.38500  142.26900 1.000 41.16450 ? 227 HIS A CA  1 
ATOM   1472 C C   . HIS A 1 227 ? 107.83900 96.41900  141.32900 1.000 41.16450 ? 227 HIS A C   1 
ATOM   1473 O O   . HIS A 1 227 ? 108.33800 96.06200  140.26100 1.000 41.16450 ? 227 HIS A O   1 
ATOM   1474 C CB  . HIS A 1 227 ? 106.59700 94.25900  141.44700 1.000 41.16450 ? 227 HIS A CB  1 
ATOM   1475 C CG  . HIS A 1 227 ? 105.89900 93.22400  142.27100 1.000 41.16450 ? 227 HIS A CG  1 
ATOM   1476 N ND1 . HIS A 1 227 ? 106.15200 93.04400  143.61300 1.000 41.16450 ? 227 HIS A ND1 1 
ATOM   1477 C CD2 . HIS A 1 227 ? 104.93600 92.33000  141.94700 1.000 41.16450 ? 227 HIS A CD2 1 
ATOM   1478 C CE1 . HIS A 1 227 ? 105.38600 92.07500  144.07700 1.000 41.16450 ? 227 HIS A CE1 1 
ATOM   1479 N NE2 . HIS A 1 227 ? 104.63800 91.62500  143.08700 1.000 41.16450 ? 227 HIS A NE2 1 
ATOM   1480 N N   . VAL A 1 228 ? 107.80200 97.69700  141.69000 1.000 32.54132 ? 228 VAL A N   1 
ATOM   1481 C CA  . VAL A 1 228 ? 108.32900 98.76400  140.85000 1.000 32.54132 ? 228 VAL A CA  1 
ATOM   1482 C C   . VAL A 1 228 ? 109.21300 99.66800  141.69800 1.000 32.54132 ? 228 VAL A C   1 
ATOM   1483 O O   . VAL A 1 228 ? 108.84900 100.03500 142.81900 1.000 32.54132 ? 228 VAL A O   1 
ATOM   1484 C CB  . VAL A 1 228 ? 107.20000 99.57600  140.17600 1.000 32.54132 ? 228 VAL A CB  1 
ATOM   1485 C CG1 . VAL A 1 228 ? 107.77600 100.65300 139.31300 1.000 32.54132 ? 228 VAL A CG1 1 
ATOM   1486 C CG2 . VAL A 1 228 ? 106.30900 98.68100  139.33300 1.000 32.54132 ? 228 VAL A CG2 1 
ATOM   1487 N N   . THR A 1 229 ? 110.37900 100.01800 141.16400 1.000 29.14758 ? 229 THR A N   1 
ATOM   1488 C CA  . THR A 1 229 ? 111.27700 100.99100 141.76500 1.000 29.14758 ? 229 THR A CA  1 
ATOM   1489 C C   . THR A 1 229 ? 111.37200 102.19800 140.84200 1.000 29.14758 ? 229 THR A C   1 
ATOM   1490 O O   . THR A 1 229 ? 111.31900 102.05500 139.62100 1.000 29.14758 ? 229 THR A O   1 
ATOM   1491 C CB  . THR A 1 229 ? 112.67100 100.38200 142.00300 1.000 29.14758 ? 229 THR A CB  1 
ATOM   1492 O OG1 . THR A 1 229 ? 112.54100 99.15100  142.71900 1.000 29.14758 ? 229 THR A OG1 1 
ATOM   1493 C CG2 . THR A 1 229 ? 113.54800 101.31300 142.81200 1.000 29.14758 ? 229 THR A CG2 1 
ATOM   1494 N N   . PHE A 1 230 ? 111.49600 103.38800 141.41600 1.000 27.24041 ? 230 PHE A N   1 
ATOM   1495 C CA  . PHE A 1 230 ? 111.68700 104.60800 140.64300 1.000 27.24041 ? 230 PHE A CA  1 
ATOM   1496 C C   . PHE A 1 230 ? 113.01200 105.24900 141.02800 1.000 27.24041 ? 230 PHE A C   1 
ATOM   1497 O O   . PHE A 1 230 ? 113.22800 105.58300 142.19500 1.000 27.24041 ? 230 PHE A O   1 
ATOM   1498 C CB  . PHE A 1 230 ? 110.52900 105.58000 140.85800 1.000 27.24041 ? 230 PHE A CB  1 
ATOM   1499 C CG  . PHE A 1 230 ? 109.19600 105.00900 140.50200 1.000 27.24041 ? 230 PHE A CG  1 
ATOM   1500 C CD1 . PHE A 1 230 ? 108.77000 104.98800 139.18800 1.000 27.24041 ? 230 PHE A CD1 1 
ATOM   1501 C CD2 . PHE A 1 230 ? 108.36800 104.48700 141.47700 1.000 27.24041 ? 230 PHE A CD2 1 
ATOM   1502 C CE1 . PHE A 1 230 ? 107.55200 104.45700 138.85700 1.000 27.24041 ? 230 PHE A CE1 1 
ATOM   1503 C CE2 . PHE A 1 230 ? 107.14800 103.96000 141.14600 1.000 27.24041 ? 230 PHE A CE2 1 
ATOM   1504 C CZ  . PHE A 1 230 ? 106.73800 103.95000 139.83500 1.000 27.24041 ? 230 PHE A CZ  1 
ATOM   1505 N N   . PHE A 1 231 ? 113.89100 105.41700 140.04900 1.000 26.02467 ? 231 PHE A N   1 
ATOM   1506 C CA  . PHE A 1 231 ? 115.17100 106.08000 140.23600 1.000 26.02467 ? 231 PHE A CA  1 
ATOM   1507 C C   . PHE A 1 231 ? 115.06300 107.48400 139.66600 1.000 26.02467 ? 231 PHE A C   1 
ATOM   1508 O O   . PHE A 1 231 ? 114.77100 107.65600 138.48000 1.000 26.02467 ? 231 PHE A O   1 
ATOM   1509 C CB  . PHE A 1 231 ? 116.29600 105.30000 139.55600 1.000 26.02467 ? 231 PHE A CB  1 
ATOM   1510 C CG  . PHE A 1 231 ? 116.43100 103.89000 140.04100 1.000 26.02467 ? 231 PHE A CG  1 
ATOM   1511 C CD1 . PHE A 1 231 ? 117.14500 103.60700 141.18900 1.000 26.02467 ? 231 PHE A CD1 1 
ATOM   1512 C CD2 . PHE A 1 231 ? 115.83900 102.84800 139.35400 1.000 26.02467 ? 231 PHE A CD2 1 
ATOM   1513 C CE1 . PHE A 1 231 ? 117.26900 102.31200 141.63900 1.000 26.02467 ? 231 PHE A CE1 1 
ATOM   1514 C CE2 . PHE A 1 231 ? 115.96300 101.55600 139.79900 1.000 26.02467 ? 231 PHE A CE2 1 
ATOM   1515 C CZ  . PHE A 1 231 ? 116.67800 101.28600 140.94300 1.000 26.02467 ? 231 PHE A CZ  1 
ATOM   1516 N N   . ILE A 1 232 ? 115.29200 108.48000 140.50700 1.000 26.67108 ? 232 ILE A N   1 
ATOM   1517 C CA  . ILE A 1 232 ? 115.08600 109.87500 140.15100 1.000 26.67108 ? 232 ILE A CA  1 
ATOM   1518 C C   . ILE A 1 232 ? 116.45100 110.53000 140.02600 1.000 26.67108 ? 232 ILE A C   1 
ATOM   1519 O O   . ILE A 1 232 ? 117.27000 110.45100 140.94600 1.000 26.67108 ? 232 ILE A O   1 
ATOM   1520 C CB  . ILE A 1 232 ? 114.20000 110.58800 141.18200 1.000 26.67108 ? 232 ILE A CB  1 
ATOM   1521 C CG1 . ILE A 1 232 ? 112.83400 109.90300 141.23800 1.000 26.67108 ? 232 ILE A CG1 1 
ATOM   1522 C CG2 . ILE A 1 232 ? 114.06100 112.05600 140.84800 1.000 26.67108 ? 232 ILE A CG2 1 
ATOM   1523 C CD1 . ILE A 1 232 ? 111.88700 110.49300 142.23500 1.000 26.67108 ? 232 ILE A CD1 1 
ATOM   1524 N N   . TYR A 1 233 ? 116.70300 111.15500 138.88200 1.000 26.92686 ? 233 TYR A N   1 
ATOM   1525 C CA  . TYR A 1 233 ? 117.98400 111.76100 138.56400 1.000 26.92686 ? 233 TYR A CA  1 
ATOM   1526 C C   . TYR A 1 233 ? 117.79000 113.25400 138.38600 1.000 26.92686 ? 233 TYR A C   1 
ATOM   1527 O O   . TYR A 1 233 ? 116.89200 113.68200 137.65900 1.000 26.92686 ? 233 TYR A O   1 
ATOM   1528 C CB  . TYR A 1 233 ? 118.58000 111.16900 137.28600 1.000 26.92686 ? 233 TYR A CB  1 
ATOM   1529 C CG  . TYR A 1 233 ? 119.09800 109.76400 137.42600 1.000 26.92686 ? 233 TYR A CG  1 
ATOM   1530 C CD1 . TYR A 1 233 ? 120.45400 109.52000 137.56200 1.000 26.92686 ? 233 TYR A CD1 1 
ATOM   1531 C CD2 . TYR A 1 233 ? 118.23300 108.67900 137.40300 1.000 26.92686 ? 233 TYR A CD2 1 
ATOM   1532 C CE1 . TYR A 1 233 ? 120.93300 108.24100 137.68500 1.000 26.92686 ? 233 TYR A CE1 1 
ATOM   1533 C CE2 . TYR A 1 233 ? 118.70400 107.39800 137.52500 1.000 26.92686 ? 233 TYR A CE2 1 
ATOM   1534 C CZ  . TYR A 1 233 ? 120.05500 107.18400 137.66600 1.000 26.92686 ? 233 TYR A CZ  1 
ATOM   1535 O OH  . TYR A 1 233 ? 120.53100 105.90800 137.79000 1.000 26.92686 ? 233 TYR A OH  1 
ATOM   1536 N N   . ASN A 1 234 ? 118.63600 114.03100 139.04000 1.000 31.12756 ? 234 ASN A N   1 
ATOM   1537 C CA  . ASN A 1 234 ? 118.65300 115.47500 138.90400 1.000 31.12756 ? 234 ASN A CA  1 
ATOM   1538 C C   . ASN A 1 234 ? 119.77900 115.88000 137.96400 1.000 31.12756 ? 234 ASN A C   1 
ATOM   1539 O O   . ASN A 1 234 ? 120.88200 115.33700 138.03700 1.000 31.12756 ? 234 ASN A O   1 
ATOM   1540 C CB  . ASN A 1 234 ? 118.83500 116.14100 140.26800 1.000 31.12756 ? 234 ASN A CB  1 
ATOM   1541 C CG  . ASN A 1 234 ? 118.58400 117.62600 140.22500 1.000 31.12756 ? 234 ASN A CG  1 
ATOM   1542 O OD1 . ASN A 1 234 ? 117.61500 118.08300 139.63300 1.000 31.12756 ? 234 ASN A OD1 1 
ATOM   1543 N ND2 . ASN A 1 234 ? 119.47400 118.39000 140.83100 1.000 31.12756 ? 234 ASN A ND2 1 
ATOM   1544 N N   . LYS A 1 235 ? 119.49200 116.82800 137.07700 1.000 32.38229 ? 235 LYS A N   1 
ATOM   1545 C CA  . LYS A 1 235 ? 120.48900 117.29200 136.12000 1.000 32.38229 ? 235 LYS A CA  1 
ATOM   1546 C C   . LYS A 1 235 ? 121.63900 117.98800 136.83200 1.000 32.38229 ? 235 LYS A C   1 
ATOM   1547 O O   . LYS A 1 235 ? 121.42700 118.85300 137.68400 1.000 32.38229 ? 235 LYS A O   1 
ATOM   1548 C CB  . LYS A 1 235 ? 119.85200 118.23900 135.10600 1.000 32.38229 ? 235 LYS A CB  1 
ATOM   1549 C CG  . LYS A 1 235 ? 120.74500 118.57700 133.93500 1.000 32.38229 ? 235 LYS A CG  1 
ATOM   1550 C CD  . LYS A 1 235 ? 119.95400 119.16000 132.78900 1.000 32.38229 ? 235 LYS A CD  1 
ATOM   1551 C CE  . LYS A 1 235 ? 120.55000 120.46100 132.31400 1.000 32.38229 ? 235 LYS A CE  1 
ATOM   1552 N NZ  . LYS A 1 235 ? 121.82900 120.25300 131.59300 1.000 32.38229 ? 235 LYS A NZ  1 
ATOM   1553 N N   . ILE A 1 236 ? 122.85900 117.60600 136.47800 1.000 36.18802 ? 236 ILE A N   1 
ATOM   1554 C CA  . ILE A 1 236 ? 124.05500 118.21300 137.04700 1.000 36.18802 ? 236 ILE A CA  1 
ATOM   1555 C C   . ILE A 1 236 ? 124.30100 119.53900 136.33900 1.000 36.18802 ? 236 ILE A C   1 
ATOM   1556 O O   . ILE A 1 236 ? 124.31600 119.60600 135.10700 1.000 36.18802 ? 236 ILE A O   1 
ATOM   1557 C CB  . ILE A 1 236 ? 125.26500 117.27600 136.91500 1.000 36.18802 ? 236 ILE A CB  1 
ATOM   1558 C CG1 . ILE A 1 236 ? 125.04400 116.00700 137.73600 1.000 36.18802 ? 236 ILE A CG1 1 
ATOM   1559 C CG2 . ILE A 1 236 ? 126.53200 117.97000 137.36600 1.000 36.18802 ? 236 ILE A CG2 1 
ATOM   1560 C CD1 . ILE A 1 236 ? 125.94400 114.86600 137.35000 1.000 36.18802 ? 236 ILE A CD1 1 
ATOM   1561 N N   . VAL A 1 237 ? 124.48000 120.59900 137.11600 1.000 46.92163 ? 237 VAL A N   1 
ATOM   1562 C CA  . VAL A 1 237 ? 124.70700 121.93700 136.58700 1.000 46.92163 ? 237 VAL A CA  1 
ATOM   1563 C C   . VAL A 1 237 ? 126.11100 122.37100 136.98200 1.000 46.92163 ? 237 VAL A C   1 
ATOM   1564 O O   . VAL A 1 237 ? 126.55100 122.13600 138.11400 1.000 46.92163 ? 237 VAL A O   1 
ATOM   1565 C CB  . VAL A 1 237 ? 123.64100 122.93000 137.07500 1.000 46.92163 ? 237 VAL A CB  1 
ATOM   1566 C CG1 . VAL A 1 237 ? 122.31300 122.62600 136.41400 1.000 46.92163 ? 237 VAL A CG1 1 
ATOM   1567 C CG2 . VAL A 1 237 ? 123.49100 122.86300 138.57800 1.000 46.92163 ? 237 VAL A CG2 1 
ATOM   1568 N N   . ASP A 1 238 ? 126.82400 122.97300 136.03700 1.000 60.04004 ? 238 ASP A N   1 
ATOM   1569 C CA  . ASP A 1 238 ? 128.19200 123.41800 136.27200 1.000 60.04004 ? 238 ASP A CA  1 
ATOM   1570 C C   . ASP A 1 238 ? 128.48200 124.72400 135.54000 1.000 60.04004 ? 238 ASP A C   1 
ATOM   1571 O O   . ASP A 1 238 ? 129.08000 125.64200 136.10300 1.000 60.04004 ? 238 ASP A O   1 
ATOM   1572 C CB  . ASP A 1 238 ? 129.18300 122.33800 135.83700 1.000 60.04004 ? 238 ASP A CB  1 
ATOM   1573 C CG  . ASP A 1 238 ? 128.98200 121.91300 134.39800 1.000 60.04004 ? 238 ASP A CG  1 
ATOM   1574 O OD1 . ASP A 1 238 ? 127.83700 122.00300 133.90900 1.000 60.04004 ? 238 ASP A OD1 1 
ATOM   1575 O OD2 . ASP A 1 238 ? 129.96700 121.49000 133.75700 1.000 60.04004 ? 238 ASP A OD2 1 
ATOM   1576 N N   . SER B 1 40  ? 98.82000  111.66400 74.14700  1.000 58.23855 ? 40  SER B N   1 
ATOM   1577 C CA  . SER B 1 40  ? 97.72100  112.25800 74.89700  1.000 58.23855 ? 40  SER B CA  1 
ATOM   1578 C C   . SER B 1 40  ? 98.21200  112.80400 76.23400  1.000 58.23855 ? 40  SER B C   1 
ATOM   1579 O O   . SER B 1 40  ? 97.99900  113.97400 76.55000  1.000 58.23855 ? 40  SER B O   1 
ATOM   1580 C CB  . SER B 1 40  ? 96.60400  111.23400 75.11500  1.000 58.23855 ? 40  SER B CB  1 
ATOM   1581 O OG  . SER B 1 40  ? 97.05800  110.12900 75.87800  1.000 58.23855 ? 40  SER B OG  1 
ATOM   1582 N N   . LEU B 1 41  ? 98.86700  111.94900 77.01600  1.000 51.28418 ? 41  LEU B N   1 
ATOM   1583 C CA  . LEU B 1 41  ? 99.47200  112.35500 78.27800  1.000 51.28418 ? 41  LEU B CA  1 
ATOM   1584 C C   . LEU B 1 41  ? 100.97800 112.45400 78.11500  1.000 51.28418 ? 41  LEU B C   1 
ATOM   1585 O O   . LEU B 1 41  ? 101.63700 111.42700 77.90100  1.000 51.28418 ? 41  LEU B O   1 
ATOM   1586 C CB  . LEU B 1 41  ? 99.13300  111.36000 79.38400  1.000 51.28418 ? 41  LEU B CB  1 
ATOM   1587 C CG  . LEU B 1 41  ? 97.95000  111.68900 80.29600  1.000 51.28418 ? 41  LEU B CG  1 
ATOM   1588 C CD1 . LEU B 1 41  ? 96.64900  111.71900 79.52500  1.000 51.28418 ? 41  LEU B CD1 1 
ATOM   1589 C CD2 . LEU B 1 41  ? 97.87200  110.67100 81.41400  1.000 51.28418 ? 41  LEU B CD2 1 
ATOM   1590 N N   . PRO B 1 42  ? 101.54700 113.65600 78.17800  1.000 48.04913 ? 42  PRO B N   1 
ATOM   1591 C CA  . PRO B 1 42  ? 102.99100 113.80300 77.96100  1.000 48.04913 ? 42  PRO B CA  1 
ATOM   1592 C C   . PRO B 1 42  ? 103.80800 113.14200 79.06100  1.000 48.04913 ? 42  PRO B C   1 
ATOM   1593 O O   . PRO B 1 42  ? 103.42900 113.13600 80.23400  1.000 48.04913 ? 42  PRO B O   1 
ATOM   1594 C CB  . PRO B 1 42  ? 103.20300 115.32100 77.95100  1.000 48.04913 ? 42  PRO B CB  1 
ATOM   1595 C CG  . PRO B 1 42  ? 101.95800 115.91200 78.48900  1.000 48.04913 ? 42  PRO B CG  1 
ATOM   1596 C CD  . PRO B 1 42  ? 100.85400 114.94600 78.29400  1.000 48.04913 ? 42  PRO B CD  1 
ATOM   1597 N N   . PHE B 1 43  ? 104.95200 112.58800 78.66400  1.000 47.71052 ? 43  PHE B N   1 
ATOM   1598 C CA  . PHE B 1 43  ? 105.87400 111.95800 79.59600  1.000 47.71052 ? 43  PHE B CA  1 
ATOM   1599 C C   . PHE B 1 43  ? 106.56600 112.95300 80.51500  1.000 47.71052 ? 43  PHE B C   1 
ATOM   1600 O O   . PHE B 1 43  ? 107.06200 112.55200 81.57000  1.000 47.71052 ? 43  PHE B O   1 
ATOM   1601 C CB  . PHE B 1 43  ? 106.95200 111.16400 78.84300  1.000 47.71052 ? 43  PHE B CB  1 
ATOM   1602 C CG  . PHE B 1 43  ? 106.44900 109.90700 78.17400  1.000 47.71052 ? 43  PHE B CG  1 
ATOM   1603 C CD1 . PHE B 1 43  ? 106.90600 108.67000 78.58300  1.000 47.71052 ? 43  PHE B CD1 1 
ATOM   1604 C CD2 . PHE B 1 43  ? 105.55200 109.96300 77.11800  1.000 47.71052 ? 43  PHE B CD2 1 
ATOM   1605 C CE1 . PHE B 1 43  ? 106.46200 107.51100 77.96900  1.000 47.71052 ? 43  PHE B CE1 1 
ATOM   1606 C CE2 . PHE B 1 43  ? 105.10400 108.80700 76.50500  1.000 47.71052 ? 43  PHE B CE2 1 
ATOM   1607 C CZ  . PHE B 1 43  ? 105.56200 107.58300 76.93000  1.000 47.71052 ? 43  PHE B CZ  1 
ATOM   1608 N N   . GLY B 1 44  ? 106.59700 114.23000 80.15200  1.000 44.10159 ? 44  GLY B N   1 
ATOM   1609 C CA  . GLY B 1 44  ? 107.29700 115.23800 80.91000  1.000 44.10159 ? 44  GLY B CA  1 
ATOM   1610 C C   . GLY B 1 44  ? 106.67500 115.61800 82.23000  1.000 44.10159 ? 44  GLY B C   1 
ATOM   1611 O O   . GLY B 1 44  ? 107.37600 116.15600 83.09100  1.000 44.10159 ? 44  GLY B O   1 
ATOM   1612 N N   . TRP B 1 45  ? 105.38000 115.35900 82.42600  1.000 43.71632 ? 45  TRP B N   1 
ATOM   1613 C CA  . TRP B 1 45  ? 104.78300 115.61100 83.73100  1.000 43.71632 ? 45  TRP B CA  1 
ATOM   1614 C C   . TRP B 1 45  ? 105.23400 114.58300 84.75400  1.000 43.71632 ? 45  TRP B C   1 
ATOM   1615 O O   . TRP B 1 45  ? 105.26600 114.87800 85.95200  1.000 43.71632 ? 45  TRP B O   1 
ATOM   1616 C CB  . TRP B 1 45  ? 103.25900 115.63100 83.63500  1.000 43.71632 ? 45  TRP B CB  1 
ATOM   1617 C CG  . TRP B 1 45  ? 102.73000 116.83800 82.94800  1.000 43.71632 ? 45  TRP B CG  1 
ATOM   1618 C CD1 . TRP B 1 45  ? 102.09400 116.88100 81.74900  1.000 43.71632 ? 45  TRP B CD1 1 
ATOM   1619 C CD2 . TRP B 1 45  ? 102.80700 118.18900 83.41100  1.000 43.71632 ? 45  TRP B CD2 1 
ATOM   1620 N NE1 . TRP B 1 45  ? 101.75900 118.17300 81.43400  1.000 43.71632 ? 45  TRP B NE1 1 
ATOM   1621 C CE2 . TRP B 1 45  ? 102.18800 118.99800 82.44000  1.000 43.71632 ? 45  TRP B CE2 1 
ATOM   1622 C CE3 . TRP B 1 45  ? 103.33400 118.79500 84.55600  1.000 43.71632 ? 45  TRP B CE3 1 
ATOM   1623 C CZ2 . TRP B 1 45  ? 102.08100 120.38000 82.57800  1.000 43.71632 ? 45  TRP B CZ2 1 
ATOM   1624 C CZ3 . TRP B 1 45  ? 103.22900 120.16400 84.69000  1.000 43.71632 ? 45  TRP B CZ3 1 
ATOM   1625 C CH2 . TRP B 1 45  ? 102.60600 120.94200 83.70700  1.000 43.71632 ? 45  TRP B CH2 1 
ATOM   1626 N N   . LEU B 1 46  ? 105.58400 113.37700 84.30500  1.000 38.63334 ? 46  LEU B N   1 
ATOM   1627 C CA  . LEU B 1 46  ? 106.14200 112.38600 85.21500  1.000 38.63334 ? 46  LEU B CA  1 
ATOM   1628 C C   . LEU B 1 46  ? 107.47700 112.85200 85.78200  1.000 38.63334 ? 46  LEU B C   1 
ATOM   1629 O O   . LEU B 1 46  ? 107.73800 112.68900 86.97700  1.000 38.63334 ? 46  LEU B O   1 
ATOM   1630 C CB  . LEU B 1 46  ? 106.29200 111.04200 84.50500  1.000 38.63334 ? 46  LEU B CB  1 
ATOM   1631 C CG  . LEU B 1 46  ? 106.78300 109.90400 85.39900  1.000 38.63334 ? 46  LEU B CG  1 
ATOM   1632 C CD1 . LEU B 1 46  ? 105.79600 109.66100 86.52600  1.000 38.63334 ? 46  LEU B CD1 1 
ATOM   1633 C CD2 . LEU B 1 46  ? 107.01100 108.63700 84.59700  1.000 38.63334 ? 46  LEU B CD2 1 
ATOM   1634 N N   . ILE B 1 47  ? 108.32300 113.45800 84.94600  1.000 38.33366 ? 47  ILE B N   1 
ATOM   1635 C CA  . ILE B 1 47  ? 109.61000 113.96800 85.41000  1.000 38.33366 ? 47  ILE B CA  1 
ATOM   1636 C C   . ILE B 1 47  ? 109.42000 115.13700 86.37500  1.000 38.33366 ? 47  ILE B C   1 
ATOM   1637 O O   . ILE B 1 47  ? 110.10600 115.22600 87.39800  1.000 38.33366 ? 47  ILE B O   1 
ATOM   1638 C CB  . ILE B 1 47  ? 110.49400 114.34700 84.20500  1.000 38.33366 ? 47  ILE B CB  1 
ATOM   1639 C CG1 . ILE B 1 47  ? 111.05600 113.08800 83.54300  1.000 38.33366 ? 47  ILE B CG1 1 
ATOM   1640 C CG2 . ILE B 1 47  ? 111.62700 115.26900 84.61100  1.000 38.33366 ? 47  ILE B CG2 1 
ATOM   1641 C CD1 . ILE B 1 47  ? 111.84400 113.35500 82.29200  1.000 38.33366 ? 47  ILE B CD1 1 
ATOM   1642 N N   . VAL B 1 48  ? 108.48600 116.04200 86.07500  1.000 38.43929 ? 48  VAL B N   1 
ATOM   1643 C CA  . VAL B 1 48  ? 108.21300 117.16700 86.96800  1.000 38.43929 ? 48  VAL B CA  1 
ATOM   1644 C C   . VAL B 1 48  ? 107.69500 116.66600 88.31400  1.000 38.43929 ? 48  VAL B C   1 
ATOM   1645 O O   . VAL B 1 48  ? 108.11300 117.14100 89.38000  1.000 38.43929 ? 48  VAL B O   1 
ATOM   1646 C CB  . VAL B 1 48  ? 107.22400 118.14600 86.30700  1.000 38.43929 ? 48  VAL B CB  1 
ATOM   1647 C CG1 . VAL B 1 48  ? 106.79600 119.22300 87.28200  1.000 38.43929 ? 48  VAL B CG1 1 
ATOM   1648 C CG2 . VAL B 1 48  ? 107.84600 118.77100 85.07400  1.000 38.43929 ? 48  VAL B CG2 1 
ATOM   1649 N N   . GLY B 1 49  ? 106.79100 115.68500 88.27900  1.000 36.70420 ? 49  GLY B N   1 
ATOM   1650 C CA  . GLY B 1 49  ? 106.29700 115.09500 89.50900  1.000 36.70420 ? 49  GLY B CA  1 
ATOM   1651 C C   . GLY B 1 49  ? 107.38300 114.40200 90.30800  1.000 36.70420 ? 49  GLY B C   1 
ATOM   1652 O O   . GLY B 1 49  ? 107.42300 114.50800 91.53200  1.000 36.70420 ? 49  GLY B O   1 
ATOM   1653 N N   . VAL B 1 50  ? 108.28400 113.69300 89.62400  1.000 35.91328 ? 50  VAL B N   1 
ATOM   1654 C CA  . VAL B 1 50  ? 109.38900 113.02100 90.30300  1.000 35.91328 ? 50  VAL B CA  1 
ATOM   1655 C C   . VAL B 1 50  ? 110.31700 114.04000 90.94900  1.000 35.91328 ? 50  VAL B C   1 
ATOM   1656 O O   . VAL B 1 50  ? 110.77200 113.85400 92.08000  1.000 35.91328 ? 50  VAL B O   1 
ATOM   1657 C CB  . VAL B 1 50  ? 110.13900 112.10400 89.31600  1.000 35.91328 ? 50  VAL B CB  1 
ATOM   1658 C CG1 . VAL B 1 50  ? 111.53200 111.77300 89.81800  1.000 35.91328 ? 50  VAL B CG1 1 
ATOM   1659 C CG2 . VAL B 1 50  ? 109.35300 110.83900 89.08200  1.000 35.91328 ? 50  VAL B CG2 1 
ATOM   1660 N N   . ALA B 1 51  ? 110.60400 115.13400 90.24600  1.000 37.05782 ? 51  ALA B N   1 
ATOM   1661 C CA  . ALA B 1 51  ? 111.48700 116.15900 90.78900  1.000 37.05782 ? 51  ALA B CA  1 
ATOM   1662 C C   . ALA B 1 51  ? 110.87800 116.82700 92.01900  1.000 37.05782 ? 51  ALA B C   1 
ATOM   1663 O O   . ALA B 1 51  ? 111.56600 117.03700 93.02700  1.000 37.05782 ? 51  ALA B O   1 
ATOM   1664 C CB  . ALA B 1 51  ? 111.80500 117.18800 89.70800  1.000 37.05782 ? 51  ALA B CB  1 
ATOM   1665 N N   . LEU B 1 52  ? 109.58100 117.14600 91.96400  1.000 36.83078 ? 52  LEU B N   1 
ATOM   1666 C CA  . LEU B 1 52  ? 108.91900 117.73800 93.12400  1.000 36.83078 ? 52  LEU B CA  1 
ATOM   1667 C C   . LEU B 1 52  ? 108.83900 116.75400 94.28700  1.000 36.83078 ? 52  LEU B C   1 
ATOM   1668 O O   . LEU B 1 52  ? 109.04900 117.13600 95.44600  1.000 36.83078 ? 52  LEU B O   1 
ATOM   1669 C CB  . LEU B 1 52  ? 107.52700 118.23000 92.73500  1.000 36.83078 ? 52  LEU B CB  1 
ATOM   1670 C CG  . LEU B 1 52  ? 107.52100 119.53300 91.94200  1.000 36.83078 ? 52  LEU B CG  1 
ATOM   1671 C CD1 . LEU B 1 52  ? 106.14200 119.82900 91.39400  1.000 36.83078 ? 52  LEU B CD1 1 
ATOM   1672 C CD2 . LEU B 1 52  ? 108.01500 120.67300 92.81400  1.000 36.83078 ? 52  LEU B CD2 1 
ATOM   1673 N N   . LEU B 1 53  ? 108.54100 115.48500 93.99400  1.000 37.22098 ? 53  LEU B N   1 
ATOM   1674 C CA  . LEU B 1 53  ? 108.51300 114.46000 95.02900  1.000 37.22098 ? 53  LEU B CA  1 
ATOM   1675 C C   . LEU B 1 53  ? 109.87900 114.29400 95.67800  1.000 37.22098 ? 53  LEU B C   1 
ATOM   1676 O O   . LEU B 1 53  ? 109.97300 114.14000 96.89700  1.000 37.22098 ? 53  LEU B O   1 
ATOM   1677 C CB  . LEU B 1 53  ? 108.03800 113.13500 94.43600  1.000 37.22098 ? 53  LEU B CB  1 
ATOM   1678 C CG  . LEU B 1 53  ? 108.14700 111.89600 95.32400  1.000 37.22098 ? 53  LEU B CG  1 
ATOM   1679 C CD1 . LEU B 1 53  ? 107.12800 111.95800 96.44200  1.000 37.22098 ? 53  LEU B CD1 1 
ATOM   1680 C CD2 . LEU B 1 53  ? 107.97200 110.63100 94.51000  1.000 37.22098 ? 53  LEU B CD2 1 
ATOM   1681 N N   . ALA B 1 54  ? 110.94600 114.32600 94.87800  1.000 37.23975 ? 54  ALA B N   1 
ATOM   1682 C CA  . ALA B 1 54  ? 112.29600 114.23700 95.42000  1.000 37.23975 ? 54  ALA B CA  1 
ATOM   1683 C C   . ALA B 1 54  ? 112.61100 115.42500 96.31600  1.000 37.23975 ? 54  ALA B C   1 
ATOM   1684 O O   . ALA B 1 54  ? 113.18500 115.25200 97.39700  1.000 37.23975 ? 54  ALA B O   1 
ATOM   1685 C CB  . ALA B 1 54  ? 113.31400 114.13600 94.28800  1.000 37.23975 ? 54  ALA B CB  1 
ATOM   1686 N N   . VAL B 1 55  ? 112.22200 116.63400 95.89100  1.000 37.59109 ? 55  VAL B N   1 
ATOM   1687 C CA  . VAL B 1 55  ? 112.43700 117.82600 96.71200  1.000 37.59109 ? 55  VAL B CA  1 
ATOM   1688 C C   . VAL B 1 55  ? 111.75500 117.66700 98.06300  1.000 37.59109 ? 55  VAL B C   1 
ATOM   1689 O O   . VAL B 1 55  ? 112.37600 117.84000 99.11900  1.000 37.59109 ? 55  VAL B O   1 
ATOM   1690 C CB  . VAL B 1 55  ? 111.92900 119.08600 95.98800  1.000 37.59109 ? 55  VAL B CB  1 
ATOM   1691 C CG1 . VAL B 1 55  ? 111.83700 120.25600 96.95900  1.000 37.59109 ? 55  VAL B CG1 1 
ATOM   1692 C CG2 . VAL B 1 55  ? 112.81500 119.44600 94.83400  1.000 37.59109 ? 55  VAL B CG2 1 
ATOM   1693 N N   . PHE B 1 56  ? 110.47800 117.28800 98.04700  1.000 39.13132 ? 56  PHE B N   1 
ATOM   1694 C CA  . PHE B 1 56  ? 109.71100 117.26100 99.28700  1.000 39.13132 ? 56  PHE B CA  1 
ATOM   1695 C C   . PHE B 1 56  ? 110.12600 116.10100 100.18500 1.000 39.13132 ? 56  PHE B C   1 
ATOM   1696 O O   . PHE B 1 56  ? 110.18300 116.25800 101.40700 1.000 39.13132 ? 56  PHE B O   1 
ATOM   1697 C CB  . PHE B 1 56  ? 108.21900 117.22500 98.97200  1.000 39.13132 ? 56  PHE B CB  1 
ATOM   1698 C CG  . PHE B 1 56  ? 107.63000 118.58300 98.75400  1.000 39.13132 ? 56  PHE B CG  1 
ATOM   1699 C CD1 . PHE B 1 56  ? 107.11400 119.30600 99.81400  1.000 39.13132 ? 56  PHE B CD1 1 
ATOM   1700 C CD2 . PHE B 1 56  ? 107.62300 119.15400 97.49400  1.000 39.13132 ? 56  PHE B CD2 1 
ATOM   1701 C CE1 . PHE B 1 56  ? 106.58400 120.56500 99.61600  1.000 39.13132 ? 56  PHE B CE1 1 
ATOM   1702 C CE2 . PHE B 1 56  ? 107.09800 120.41000 97.29100  1.000 39.13132 ? 56  PHE B CE2 1 
ATOM   1703 C CZ  . PHE B 1 56  ? 106.57700 121.11700 98.35300  1.000 39.13132 ? 56  PHE B CZ  1 
ATOM   1704 N N   . GLN B 1 57  ? 110.43800 114.93800 99.60500  1.000 41.23767 ? 57  GLN B N   1 
ATOM   1705 C CA  . GLN B 1 57  ? 110.92700 113.80900 100.39300 1.000 41.23767 ? 57  GLN B CA  1 
ATOM   1706 C C   . GLN B 1 57  ? 112.27400 114.11600 101.03600 1.000 41.23767 ? 57  GLN B C   1 
ATOM   1707 O O   . GLN B 1 57  ? 112.48900 113.81900 102.22200 1.000 41.23767 ? 57  GLN B O   1 
ATOM   1708 C CB  . GLN B 1 57  ? 111.03300 112.57100 99.50700  1.000 41.23767 ? 57  GLN B CB  1 
ATOM   1709 C CG  . GLN B 1 57  ? 109.91700 111.56700 99.67900  1.000 41.23767 ? 57  GLN B CG  1 
ATOM   1710 C CD  . GLN B 1 57  ? 109.84500 111.01300 101.08300 1.000 41.23767 ? 57  GLN B CD  1 
ATOM   1711 O OE1 . GLN B 1 57  ? 110.79100 110.39900 101.56800 1.000 41.23767 ? 57  GLN B OE1 1 
ATOM   1712 N NE2 . GLN B 1 57  ? 108.72000 111.23100 101.74600 1.000 41.23767 ? 57  GLN B NE2 1 
ATOM   1713 N N   . SER B 1 58  ? 113.19000 114.71700 100.27300 1.000 39.58947 ? 58  SER B N   1 
ATOM   1714 C CA  . SER B 1 58  ? 114.49200 115.07300 100.81400 1.000 39.58947 ? 58  SER B CA  1 
ATOM   1715 C C   . SER B 1 58  ? 114.36500 116.12400 101.90800 1.000 39.58947 ? 58  SER B C   1 
ATOM   1716 O O   . SER B 1 58  ? 115.10500 116.08700 102.89500 1.000 39.58947 ? 58  SER B O   1 
ATOM   1717 C CB  . SER B 1 58  ? 115.40200 115.56600 99.69200  1.000 39.58947 ? 58  SER B CB  1 
ATOM   1718 O OG  . SER B 1 58  ? 115.39400 114.66900 98.60200  1.000 39.58947 ? 58  SER B OG  1 
ATOM   1719 N N   . ALA B 1 59  ? 113.43800 117.07100 101.74800 1.000 40.52151 ? 59  ALA B N   1 
ATOM   1720 C CA  . ALA B 1 59  ? 113.20500 118.05200 102.80200 1.000 40.52151 ? 59  ALA B CA  1 
ATOM   1721 C C   . ALA B 1 59  ? 112.59900 117.40300 104.04100 1.000 40.52151 ? 59  ALA B C   1 
ATOM   1722 O O   . ALA B 1 59  ? 112.94200 117.77300 105.16800 1.000 40.52151 ? 59  ALA B O   1 
ATOM   1723 C CB  . ALA B 1 59  ? 112.31000 119.17500 102.28700 1.000 40.52151 ? 59  ALA B CB  1 
ATOM   1724 N N   . SER B 1 60  ? 111.70200 116.43300 103.85400 1.000 42.15472 ? 60  SER B N   1 
ATOM   1725 C CA  . SER B 1 60  ? 111.08300 115.76500 104.99300 1.000 42.15472 ? 60  SER B CA  1 
ATOM   1726 C C   . SER B 1 60  ? 112.08800 114.93200 105.77200 1.000 42.15472 ? 60  SER B C   1 
ATOM   1727 O O   . SER B 1 60  ? 111.91500 114.72300 106.97600 1.000 42.15472 ? 60  SER B O   1 
ATOM   1728 C CB  . SER B 1 60  ? 109.92500 114.88100 104.53100 1.000 42.15472 ? 60  SER B CB  1 
ATOM   1729 O OG  . SER B 1 60  ? 110.39600 113.67100 103.97100 1.000 42.15472 ? 60  SER B OG  1 
ATOM   1730 N N   . LYS B 1 61  ? 113.13300 114.43900 105.10700 1.000 44.75978 ? 61  LYS B N   1 
ATOM   1731 C CA  . LYS B 1 61  ? 114.13900 113.66400 105.82700 1.000 44.75978 ? 61  LYS B CA  1 
ATOM   1732 C C   . LYS B 1 61  ? 114.94600 114.48200 106.83400 1.000 44.75978 ? 61  LYS B C   1 
ATOM   1733 O O   . LYS B 1 61  ? 115.56700 113.88500 107.71800 1.000 44.75978 ? 61  LYS B O   1 
ATOM   1734 C CB  . LYS B 1 61  ? 115.10500 112.98900 104.85100 1.000 44.75978 ? 61  LYS B CB  1 
ATOM   1735 C CG  . LYS B 1 61  ? 114.47100 111.94400 103.95800 1.000 44.75978 ? 61  LYS B CG  1 
ATOM   1736 C CD  . LYS B 1 61  ? 114.33600 110.61900 104.67900 1.000 44.75978 ? 61  LYS B CD  1 
ATOM   1737 C CE  . LYS B 1 61  ? 115.57900 109.75900 104.50300 1.000 44.75978 ? 61  LYS B CE  1 
ATOM   1738 N NZ  . LYS B 1 61  ? 115.53300 108.53000 105.34200 1.000 44.75978 ? 61  LYS B NZ  1 
ATOM   1739 N N   . ILE B 1 62  ? 114.96400 115.81100 106.74000 1.000 44.44254 ? 62  ILE B N   1 
ATOM   1740 C CA  . ILE B 1 62  ? 115.91800 116.59800 107.51000 1.000 44.44254 ? 62  ILE B CA  1 
ATOM   1741 C C   . ILE B 1 62  ? 115.24800 117.70400 108.32800 1.000 44.44254 ? 62  ILE B C   1 
ATOM   1742 O O   . ILE B 1 62  ? 115.88400 118.69300 108.64700 1.000 44.44254 ? 62  ILE B O   1 
ATOM   1743 C CB  . ILE B 1 62  ? 117.01400 117.18400 106.60100 1.000 44.44254 ? 62  ILE B CB  1 
ATOM   1744 C CG1 . ILE B 1 62  ? 116.38700 117.98500 105.46200 1.000 44.44254 ? 62  ILE B CG1 1 
ATOM   1745 C CG2 . ILE B 1 62  ? 117.93100 116.08600 106.07200 1.000 44.44254 ? 62  ILE B CG2 1 
ATOM   1746 C CD1 . ILE B 1 62  ? 117.38300 118.76800 104.67300 1.000 44.44254 ? 62  ILE B CD1 1 
ATOM   1747 N N   . ILE B 1 63  ? 113.98100 117.55300 108.68600 1.000 46.02183 ? 63  ILE B N   1 
ATOM   1748 C CA  . ILE B 1 63  ? 113.31400 118.51700 109.55700 1.000 46.02183 ? 63  ILE B CA  1 
ATOM   1749 C C   . ILE B 1 63  ? 113.39300 118.00900 110.99100 1.000 46.02183 ? 63  ILE B C   1 
ATOM   1750 O O   . ILE B 1 63  ? 112.84600 116.94900 111.30800 1.000 46.02183 ? 63  ILE B O   1 
ATOM   1751 C CB  . ILE B 1 63  ? 111.85500 118.74200 109.13300 1.000 46.02183 ? 63  ILE B CB  1 
ATOM   1752 C CG1 . ILE B 1 63  ? 111.79000 119.39000 107.75100 1.000 46.02183 ? 63  ILE B CG1 1 
ATOM   1753 C CG2 . ILE B 1 63  ? 111.12600 119.60300 110.15200 1.000 46.02183 ? 63  ILE B CG2 1 
ATOM   1754 C CD1 . ILE B 1 63  ? 110.45200 119.22800 107.06700 1.000 46.02183 ? 63  ILE B CD1 1 
ATOM   1755 N N   . THR B 1 64  ? 114.06800 118.76300 111.85800 1.000 48.76573 ? 64  THR B N   1 
ATOM   1756 C CA  . THR B 1 64  ? 114.15400 118.38800 113.26400 1.000 48.76573 ? 64  THR B CA  1 
ATOM   1757 C C   . THR B 1 64  ? 112.78800 118.47600 113.92900 1.000 48.76573 ? 64  THR B C   1 
ATOM   1758 O O   . THR B 1 64  ? 112.02600 119.41500 113.69800 1.000 48.76573 ? 64  THR B O   1 
ATOM   1759 C CB  . THR B 1 64  ? 115.14600 119.27900 114.01000 1.000 48.76573 ? 64  THR B CB  1 
ATOM   1760 O OG1 . THR B 1 64  ? 114.60900 120.60000 114.13900 1.000 48.76573 ? 64  THR B OG1 1 
ATOM   1761 C CG2 . THR B 1 64  ? 116.45500 119.34300 113.27700 1.000 48.76573 ? 64  THR B CG2 1 
ATOM   1762 N N   . LEU B 1 65  ? 112.46900 117.46700 114.73500 1.000 45.64901 ? 65  LEU B N   1 
ATOM   1763 C CA  . LEU B 1 65  ? 111.18800 117.41400 115.42500 1.000 45.64901 ? 65  LEU B CA  1 
ATOM   1764 C C   . LEU B 1 65  ? 111.30500 117.84800 116.87800 1.000 45.64901 ? 65  LEU B C   1 
ATOM   1765 O O   . LEU B 1 65  ? 111.06800 117.04600 117.78500 1.000 45.64901 ? 65  LEU B O   1 
ATOM   1766 C CB  . LEU B 1 65  ? 110.60500 116.00400 115.33900 1.000 45.64901 ? 65  LEU B CB  1 
ATOM   1767 C CG  . LEU B 1 65  ? 110.50700 115.43600 113.92500 1.000 45.64901 ? 65  LEU B CG  1 
ATOM   1768 C CD1 . LEU B 1 65  ? 109.86000 114.06500 113.93700 1.000 45.64901 ? 65  LEU B CD1 1 
ATOM   1769 C CD2 . LEU B 1 65  ? 109.74100 116.38700 113.03500 1.000 45.64901 ? 65  LEU B CD2 1 
ATOM   1770 N N   . LYS B 1 66  ? 111.67000 119.10400 117.12000 1.000 46.62451 ? 66  LYS B N   1 
ATOM   1771 C CA  . LYS B 1 66  ? 111.76500 119.58000 118.49400 1.000 46.62451 ? 66  LYS B CA  1 
ATOM   1772 C C   . LYS B 1 66  ? 110.56600 120.43100 118.89800 1.000 46.62451 ? 66  LYS B C   1 
ATOM   1773 O O   . LYS B 1 66  ? 109.86000 120.09400 119.85100 1.000 46.62451 ? 66  LYS B O   1 
ATOM   1774 C CB  . LYS B 1 66  ? 113.06500 120.36100 118.68900 1.000 46.62451 ? 66  LYS B CB  1 
ATOM   1775 C CG  . LYS B 1 66  ? 114.29900 119.49500 118.62400 1.000 46.62451 ? 66  LYS B CG  1 
ATOM   1776 C CD  . LYS B 1 66  ? 115.55300 120.31500 118.81200 1.000 46.62451 ? 66  LYS B CD  1 
ATOM   1777 C CE  . LYS B 1 66  ? 116.79300 119.45000 118.71300 1.000 46.62451 ? 66  LYS B CE  1 
ATOM   1778 N NZ  . LYS B 1 66  ? 116.84200 118.44800 119.80100 1.000 46.62451 ? 66  LYS B NZ  1 
ATOM   1779 N N   . LYS B 1 67  ? 110.31300 121.51700 118.18200 1.000 50.07618 ? 67  LYS B N   1 
ATOM   1780 C CA  . LYS B 1 67  ? 109.23100 122.42800 118.51900 1.000 50.07618 ? 67  LYS B CA  1 
ATOM   1781 C C   . LYS B 1 67  ? 107.95600 122.05500 117.77400 1.000 50.07618 ? 67  LYS B C   1 
ATOM   1782 O O   . LYS B 1 67  ? 107.96500 121.28300 116.81400 1.000 50.07618 ? 67  LYS B O   1 
ATOM   1783 C CB  . LYS B 1 67  ? 109.63900 123.87200 118.22700 1.000 50.07618 ? 67  LYS B CB  1 
ATOM   1784 C CG  . LYS B 1 67  ? 110.96900 124.23900 118.85100 1.000 50.07618 ? 67  LYS B CG  1 
ATOM   1785 C CD  . LYS B 1 67  ? 111.33200 125.68200 118.61300 1.000 50.07618 ? 67  LYS B CD  1 
ATOM   1786 C CE  . LYS B 1 67  ? 112.82800 125.84100 118.38300 1.000 50.07618 ? 67  LYS B CE  1 
ATOM   1787 N NZ  . LYS B 1 67  ? 113.13400 126.49300 117.07300 1.000 50.07618 ? 67  LYS B NZ  1 
ATOM   1788 N N   . ARG B 1 68  ? 106.84200 122.61400 118.25000 1.000 46.50866 ? 68  ARG B N   1 
ATOM   1789 C CA  . ARG B 1 68  ? 105.52500 122.23100 117.75400 1.000 46.50866 ? 68  ARG B CA  1 
ATOM   1790 C C   . ARG B 1 68  ? 105.33300 122.64500 116.30100 1.000 46.50866 ? 68  ARG B C   1 
ATOM   1791 O O   . ARG B 1 68  ? 104.72800 121.91300 115.50600 1.000 46.50866 ? 68  ARG B O   1 
ATOM   1792 C CB  . ARG B 1 68  ? 104.44600 122.85600 118.63300 1.000 46.50866 ? 68  ARG B CB  1 
ATOM   1793 C CG  . ARG B 1 68  ? 103.12700 122.13600 118.60800 1.000 46.50866 ? 68  ARG B CG  1 
ATOM   1794 C CD  . ARG B 1 68  ? 102.03900 122.99600 119.23500 1.000 46.50866 ? 68  ARG B CD  1 
ATOM   1795 N NE  . ARG B 1 68  ? 100.72000 122.36600 119.25600 1.000 46.50866 ? 68  ARG B NE  1 
ATOM   1796 C CZ  . ARG B 1 68  ? 100.39700 121.28100 119.95700 1.000 46.50866 ? 68  ARG B CZ  1 
ATOM   1797 N NH1 . ARG B 1 68  ? 101.28600 120.68200 120.74100 1.000 46.50866 ? 68  ARG B NH1 1 
ATOM   1798 N NH2 . ARG B 1 68  ? 99.16200  120.80300 119.88900 1.000 46.50866 ? 68  ARG B NH2 1 
ATOM   1799 N N   . TRP B 1 69  ? 105.82700 123.83100 115.94100 1.000 52.01988 ? 69  TRP B N   1 
ATOM   1800 C CA  . TRP B 1 69  ? 105.70300 124.29100 114.56700 1.000 52.01988 ? 69  TRP B CA  1 
ATOM   1801 C C   . TRP B 1 69  ? 106.53500 123.44100 113.62000 1.000 52.01988 ? 69  TRP B C   1 
ATOM   1802 O O   . TRP B 1 69  ? 106.13400 123.22700 112.47400 1.000 52.01988 ? 69  TRP B O   1 
ATOM   1803 C CB  . TRP B 1 69  ? 106.08300 125.76900 114.46900 1.000 52.01988 ? 69  TRP B CB  1 
ATOM   1804 C CG  . TRP B 1 69  ? 107.53900 126.06100 114.58900 1.000 52.01988 ? 69  TRP B CG  1 
ATOM   1805 C CD1 . TRP B 1 69  ? 108.22300 126.35100 115.72800 1.000 52.01988 ? 69  TRP B CD1 1 
ATOM   1806 C CD2 . TRP B 1 69  ? 108.49500 126.10800 113.52500 1.000 52.01988 ? 69  TRP B CD2 1 
ATOM   1807 N NE1 . TRP B 1 69  ? 109.54600 126.56200 115.44500 1.000 52.01988 ? 69  TRP B NE1 1 
ATOM   1808 C CE2 . TRP B 1 69  ? 109.74000 126.42200 114.09700 1.000 52.01988 ? 69  TRP B CE2 1 
ATOM   1809 C CE3 . TRP B 1 69  ? 108.42000 125.90500 112.14400 1.000 52.01988 ? 69  TRP B CE3 1 
ATOM   1810 C CZ2 . TRP B 1 69  ? 110.89900 126.53900 113.33900 1.000 52.01988 ? 69  TRP B CZ2 1 
ATOM   1811 C CZ3 . TRP B 1 69  ? 109.57100 126.02600 111.39500 1.000 52.01988 ? 69  TRP B CZ3 1 
ATOM   1812 C CH2 . TRP B 1 69  ? 110.79300 126.34200 111.99300 1.000 52.01988 ? 69  TRP B CH2 1 
ATOM   1813 N N   . GLN B 1 70  ? 107.67000 122.91600 114.08700 1.000 47.03760 ? 70  GLN B N   1 
ATOM   1814 C CA  . GLN B 1 70  ? 108.43900 121.98500 113.27000 1.000 47.03760 ? 70  GLN B CA  1 
ATOM   1815 C C   . GLN B 1 70  ? 107.69100 120.67300 113.07100 1.000 47.03760 ? 70  GLN B C   1 
ATOM   1816 O O   . GLN B 1 70  ? 107.76200 120.07500 111.99400 1.000 47.03760 ? 70  GLN B O   1 
ATOM   1817 C CB  . GLN B 1 70  ? 109.80600 121.73800 113.90000 1.000 47.03760 ? 70  GLN B CB  1 
ATOM   1818 C CG  . GLN B 1 70  ? 110.61100 122.99400 114.13700 1.000 47.03760 ? 70  GLN B CG  1 
ATOM   1819 C CD  . GLN B 1 70  ? 111.87100 122.73500 114.92500 1.000 47.03760 ? 70  GLN B CD  1 
ATOM   1820 O OE1 . GLN B 1 70  ? 111.86100 121.99700 115.90400 1.000 47.03760 ? 70  GLN B OE1 1 
ATOM   1821 N NE2 . GLN B 1 70  ? 112.96500 123.34400 114.50500 1.000 47.03760 ? 70  GLN B NE2 1 
ATOM   1822 N N   . LEU B 1 71  ? 106.96800 120.21000 114.09300 1.000 41.37942 ? 71  LEU B N   1 
ATOM   1823 C CA  . LEU B 1 71  ? 106.16000 119.00400 113.94000 1.000 41.37942 ? 71  LEU B CA  1 
ATOM   1824 C C   . LEU B 1 71  ? 105.03800 119.21600 112.93300 1.000 41.37942 ? 71  LEU B C   1 
ATOM   1825 O O   . LEU B 1 71  ? 104.78200 118.35100 112.08400 1.000 41.37942 ? 71  LEU B O   1 
ATOM   1826 C CB  . LEU B 1 71  ? 105.58900 118.57500 115.29100 1.000 41.37942 ? 71  LEU B CB  1 
ATOM   1827 C CG  . LEU B 1 71  ? 106.58900 118.22700 116.39200 1.000 41.37942 ? 71  LEU B CG  1 
ATOM   1828 C CD1 . LEU B 1 71  ? 105.94000 118.36000 117.75500 1.000 41.37942 ? 71  LEU B CD1 1 
ATOM   1829 C CD2 . LEU B 1 71  ? 107.13000 116.83100 116.19500 1.000 41.37942 ? 71  LEU B CD2 1 
ATOM   1830 N N   . ALA B 1 72  ? 104.36100 120.36500 113.01000 1.000 40.04386 ? 72  ALA B N   1 
ATOM   1831 C CA  . ALA B 1 72  ? 103.31400 120.67100 112.04100 1.000 40.04386 ? 72  ALA B CA  1 
ATOM   1832 C C   . ALA B 1 72  ? 103.88300 120.79200 110.63200 1.000 40.04386 ? 72  ALA B C   1 
ATOM   1833 O O   . ALA B 1 72  ? 103.28000 120.30100 109.67000 1.000 40.04386 ? 72  ALA B O   1 
ATOM   1834 C CB  . ALA B 1 72  ? 102.58200 121.95000 112.44100 1.000 40.04386 ? 72  ALA B CB  1 
ATOM   1835 N N   . LEU B 1 73  ? 105.05000 121.42700 110.49700 1.000 39.03704 ? 73  LEU B N   1 
ATOM   1836 C CA  . LEU B 1 73  ? 105.69600 121.54900 109.19500 1.000 39.03704 ? 73  LEU B CA  1 
ATOM   1837 C C   . LEU B 1 73  ? 106.06300 120.18700 108.62700 1.000 39.03704 ? 73  LEU B C   1 
ATOM   1838 O O   . LEU B 1 73  ? 105.84700 119.92600 107.44000 1.000 39.03704 ? 73  LEU B O   1 
ATOM   1839 C CB  . LEU B 1 73  ? 106.93900 122.42900 109.31200 1.000 39.03704 ? 73  LEU B CB  1 
ATOM   1840 C CG  . LEU B 1 73  ? 107.81200 122.52600 108.06300 1.000 39.03704 ? 73  LEU B CG  1 
ATOM   1841 C CD1 . LEU B 1 73  ? 107.10600 123.32500 106.98100 1.000 39.03704 ? 73  LEU B CD1 1 
ATOM   1842 C CD2 . LEU B 1 73  ? 109.15500 123.13800 108.39800 1.000 39.03704 ? 73  LEU B CD2 1 
ATOM   1843 N N   . SER B 1 74  ? 106.60800 119.30400 109.46500 1.000 39.40277 ? 74  SER B N   1 
ATOM   1844 C CA  . SER B 1 74  ? 106.99500 117.97600 109.00900 1.000 39.40277 ? 74  SER B CA  1 
ATOM   1845 C C   . SER B 1 74  ? 105.78300 117.15800 108.58300 1.000 39.40277 ? 74  SER B C   1 
ATOM   1846 O O   . SER B 1 74  ? 105.83300 116.45000 107.57100 1.000 39.40277 ? 74  SER B O   1 
ATOM   1847 C CB  . SER B 1 74  ? 107.77500 117.26300 110.10800 1.000 39.40277 ? 74  SER B CB  1 
ATOM   1848 O OG  . SER B 1 74  ? 107.80900 115.86800 109.89600 1.000 39.40277 ? 74  SER B OG  1 
ATOM   1849 N N   . LYS B 1 75  ? 104.68000 117.25000 109.33100 1.000 39.22934 ? 75  LYS B N   1 
ATOM   1850 C CA  . LYS B 1 75  ? 103.47500 116.52500 108.93700 1.000 39.22934 ? 75  LYS B CA  1 
ATOM   1851 C C   . LYS B 1 75  ? 102.88100 117.07500 107.64600 1.000 39.22934 ? 75  LYS B C   1 
ATOM   1852 O O   . LYS B 1 75  ? 102.40800 116.30700 106.80100 1.000 39.22934 ? 75  LYS B O   1 
ATOM   1853 C CB  . LYS B 1 75  ? 102.44000 116.55200 110.06000 1.000 39.22934 ? 75  LYS B CB  1 
ATOM   1854 C CG  . LYS B 1 75  ? 102.88200 115.82300 111.30400 1.000 39.22934 ? 75  LYS B CG  1 
ATOM   1855 C CD  . LYS B 1 75  ? 102.84100 114.32800 111.09000 1.000 39.22934 ? 75  LYS B CD  1 
ATOM   1856 C CE  . LYS B 1 75  ? 103.96100 113.63800 111.83200 1.000 39.22934 ? 75  LYS B CE  1 
ATOM   1857 N NZ  . LYS B 1 75  ? 103.47400 112.45700 112.59100 1.000 39.22934 ? 75  LYS B NZ  1 
ATOM   1858 N N   . GLY B 1 76  ? 102.89800 118.39700 107.46900 1.000 38.80830 ? 76  GLY B N   1 
ATOM   1859 C CA  . GLY B 1 76  ? 102.42400 118.96700 106.21800 1.000 38.80830 ? 76  GLY B CA  1 
ATOM   1860 C C   . GLY B 1 76  ? 103.27700 118.56400 105.02900 1.000 38.80830 ? 76  GLY B C   1 
ATOM   1861 O O   . GLY B 1 76  ? 102.75600 118.26600 103.94900 1.000 38.80830 ? 76  GLY B O   1 
ATOM   1862 N N   . VAL B 1 77  ? 104.59600 118.53500 105.21700 1.000 38.81783 ? 77  VAL B N   1 
ATOM   1863 C CA  . VAL B 1 77  ? 105.49500 118.12100 104.14700 1.000 38.81783 ? 77  VAL B CA  1 
ATOM   1864 C C   . VAL B 1 77  ? 105.29200 116.64700 103.82200 1.000 38.81783 ? 77  VAL B C   1 
ATOM   1865 O O   . VAL B 1 77  ? 105.31800 116.25400 102.65400 1.000 38.81783 ? 77  VAL B O   1 
ATOM   1866 C CB  . VAL B 1 77  ? 106.95400 118.44200 104.52700 1.000 38.81783 ? 77  VAL B CB  1 
ATOM   1867 C CG1 . VAL B 1 77  ? 107.92700 117.77400 103.57900 1.000 38.81783 ? 77  VAL B CG1 1 
ATOM   1868 C CG2 . VAL B 1 77  ? 107.17900 119.94000 104.51200 1.000 38.81783 ? 77  VAL B CG2 1 
ATOM   1869 N N   . HIS B 1 78  ? 105.04600 115.81700 104.83900 1.000 40.70036 ? 78  HIS B N   1 
ATOM   1870 C CA  . HIS B 1 78  ? 104.75800 114.40500 104.59800 1.000 40.70036 ? 78  HIS B CA  1 
ATOM   1871 C C   . HIS B 1 78  ? 103.44200 114.22000 103.84900 1.000 40.70036 ? 78  HIS B C   1 
ATOM   1872 O O   . HIS B 1 78  ? 103.32900 113.33600 102.99100 1.000 40.70036 ? 78  HIS B O   1 
ATOM   1873 C CB  . HIS B 1 78  ? 104.73300 113.64600 105.92000 1.000 40.70036 ? 78  HIS B CB  1 
ATOM   1874 C CG  . HIS B 1 78  ? 106.09300 113.33500 106.45700 1.000 40.70036 ? 78  HIS B CG  1 
ATOM   1875 N ND1 . HIS B 1 78  ? 106.46000 113.60800 107.75500 1.000 40.70036 ? 78  HIS B ND1 1 
ATOM   1876 C CD2 . HIS B 1 78  ? 107.17400 112.77100 105.87100 1.000 40.70036 ? 78  HIS B CD2 1 
ATOM   1877 C CE1 . HIS B 1 78  ? 107.71100 113.23100 107.94500 1.000 40.70036 ? 78  HIS B CE1 1 
ATOM   1878 N NE2 . HIS B 1 78  ? 108.16600 112.71800 106.81800 1.000 40.70036 ? 78  HIS B NE2 1 
ATOM   1879 N N   . PHE B 1 79  ? 102.43600 115.03600 104.16600 1.000 39.96660 ? 79  PHE B N   1 
ATOM   1880 C CA  . PHE B 1 79  ? 101.17700 114.98700 103.43000 1.000 39.96660 ? 79  PHE B CA  1 
ATOM   1881 C C   . PHE B 1 79  ? 101.37400 115.35700 101.96300 1.000 39.96660 ? 79  PHE B C   1 
ATOM   1882 O O   . PHE B 1 79  ? 100.83600 114.69300 101.06500 1.000 39.96660 ? 79  PHE B O   1 
ATOM   1883 C CB  . PHE B 1 79  ? 100.16000 115.91700 104.09000 1.000 39.96660 ? 79  PHE B CB  1 
ATOM   1884 C CG  . PHE B 1 79  ? 98.79800  115.85500 103.47700 1.000 39.96660 ? 79  PHE B CG  1 
ATOM   1885 C CD1 . PHE B 1 79  ? 98.01800  114.72000 103.60400 1.000 39.96660 ? 79  PHE B CD1 1 
ATOM   1886 C CD2 . PHE B 1 79  ? 98.29800  116.93000 102.76700 1.000 39.96660 ? 79  PHE B CD2 1 
ATOM   1887 C CE1 . PHE B 1 79  ? 96.76300  114.66100 103.03800 1.000 39.96660 ? 79  PHE B CE1 1 
ATOM   1888 C CE2 . PHE B 1 79  ? 97.04400  116.87600 102.20100 1.000 39.96660 ? 79  PHE B CE2 1 
ATOM   1889 C CZ  . PHE B 1 79  ? 96.27700  115.74000 102.33600 1.000 39.96660 ? 79  PHE B CZ  1 
ATOM   1890 N N   . VAL B 1 80  ? 102.15200 116.41000 101.70300 1.000 39.40420 ? 80  VAL B N   1 
ATOM   1891 C CA  . VAL B 1 80  ? 102.45400 116.79800 100.32600 1.000 39.40420 ? 80  VAL B CA  1 
ATOM   1892 C C   . VAL B 1 80  ? 103.24600 115.70000 99.61900  1.000 39.40420 ? 80  VAL B C   1 
ATOM   1893 O O   . VAL B 1 80  ? 103.02700 115.42100 98.43300  1.000 39.40420 ? 80  VAL B O   1 
ATOM   1894 C CB  . VAL B 1 80  ? 103.19400 118.14900 100.30700 1.000 39.40420 ? 80  VAL B CB  1 
ATOM   1895 C CG1 . VAL B 1 80  ? 103.70400 118.47800 98.91200  1.000 39.40420 ? 80  VAL B CG1 1 
ATOM   1896 C CG2 . VAL B 1 80  ? 102.28200 119.24800 100.80300 1.000 39.40420 ? 80  VAL B CG2 1 
ATOM   1897 N N   . CYS B 1 81  ? 104.16600 115.05100 100.34000 1.000 40.04680 ? 81  CYS B N   1 
ATOM   1898 C CA  . CYS B 1 81  ? 104.93400 113.94400 99.77800  1.000 40.04680 ? 81  CYS B CA  1 
ATOM   1899 C C   . CYS B 1 81  ? 104.02900 112.80000 99.36000  1.000 40.04680 ? 81  CYS B C   1 
ATOM   1900 O O   . CYS B 1 81  ? 104.20800 112.22200 98.28500  1.000 40.04680 ? 81  CYS B O   1 
ATOM   1901 C CB  . CYS B 1 81  ? 105.95200 113.42900 100.79400 1.000 40.04680 ? 81  CYS B CB  1 
ATOM   1902 S SG  . CYS B 1 81  ? 107.36500 114.46200 101.07100 1.000 40.04680 ? 81  CYS B SG  1 
ATOM   1903 N N   . ASN B 1 82  ? 103.06500 112.44900 100.20900 1.000 39.99079 ? 82  ASN B N   1 
ATOM   1904 C CA  . ASN B 1 82  ? 102.16200 111.35500 99.87700  1.000 39.99079 ? 82  ASN B CA  1 
ATOM   1905 C C   . ASN B 1 82  ? 101.26600 111.71300 98.69800  1.000 39.99079 ? 82  ASN B C   1 
ATOM   1906 O O   . ASN B 1 82  ? 100.98400 110.86000 97.84900  1.000 39.99079 ? 82  ASN B O   1 
ATOM   1907 C CB  . ASN B 1 82  ? 101.32900 110.97100 101.09300 1.000 39.99079 ? 82  ASN B CB  1 
ATOM   1908 C CG  . ASN B 1 82  ? 100.59900 109.66500 100.89800 1.000 39.99079 ? 82  ASN B CG  1 
ATOM   1909 O OD1 . ASN B 1 82  ? 101.17700 108.59400 101.05300 1.000 39.99079 ? 82  ASN B OD1 1 
ATOM   1910 N ND2 . ASN B 1 82  ? 99.32400  109.74500 100.54400 1.000 39.99079 ? 82  ASN B ND2 1 
ATOM   1911 N N   . LEU B 1 83  ? 100.81600 112.96800 98.62400  1.000 39.11037 ? 83  LEU B N   1 
ATOM   1912 C CA  . LEU B 1 83  ? 100.03100 113.39800 97.47000  1.000 39.11037 ? 83  LEU B CA  1 
ATOM   1913 C C   . LEU B 1 83  ? 100.84400 113.31900 96.18100  1.000 39.11037 ? 83  LEU B C   1 
ATOM   1914 O O   . LEU B 1 83  ? 100.34700 112.84900 95.15100  1.000 39.11037 ? 83  LEU B O   1 
ATOM   1915 C CB  . LEU B 1 83  ? 99.51000  114.81600 97.69300  1.000 39.11037 ? 83  LEU B CB  1 
ATOM   1916 C CG  . LEU B 1 83  ? 98.43300  114.98900 98.76700  1.000 39.11037 ? 83  LEU B CG  1 
ATOM   1917 C CD1 . LEU B 1 83  ? 97.82500  116.37000 98.68700  1.000 39.11037 ? 83  LEU B CD1 1 
ATOM   1918 C CD2 . LEU B 1 83  ? 97.35700  113.92500 98.64800  1.000 39.11037 ? 83  LEU B CD2 1 
ATOM   1919 N N   . LEU B 1 84  ? 102.10600 113.75100 96.22600  1.000 37.68699 ? 84  LEU B N   1 
ATOM   1920 C CA  . LEU B 1 84  ? 102.97100 113.66600 95.05300  1.000 37.68699 ? 84  LEU B CA  1 
ATOM   1921 C C   . LEU B 1 84  ? 103.25700 112.21900 94.66700  1.000 37.68699 ? 84  LEU B C   1 
ATOM   1922 O O   . LEU B 1 84  ? 103.35000 111.89700 93.47800  1.000 37.68699 ? 84  LEU B O   1 
ATOM   1923 C CB  . LEU B 1 84  ? 104.27400 114.41600 95.31000  1.000 37.68699 ? 84  LEU B CB  1 
ATOM   1924 C CG  . LEU B 1 84  ? 104.19300 115.93700 95.23700  1.000 37.68699 ? 84  LEU B CG  1 
ATOM   1925 C CD1 . LEU B 1 84  ? 105.45600 116.56000 95.79100  1.000 37.68699 ? 84  LEU B CD1 1 
ATOM   1926 C CD2 . LEU B 1 84  ? 103.95200 116.38100 93.81300  1.000 37.68699 ? 84  LEU B CD2 1 
ATOM   1927 N N   . LEU B 1 85  ? 103.42300 111.34100 95.66000  1.000 37.21820 ? 85  LEU B N   1 
ATOM   1928 C CA  . LEU B 1 85  ? 103.64200 109.92600 95.38200  1.000 37.21820 ? 85  LEU B CA  1 
ATOM   1929 C C   . LEU B 1 85  ? 102.42800 109.30300 94.71200  1.000 37.21820 ? 85  LEU B C   1 
ATOM   1930 O O   . LEU B 1 85  ? 102.56400 108.51800 93.76500  1.000 37.21820 ? 85  LEU B O   1 
ATOM   1931 C CB  . LEU B 1 85  ? 103.97500 109.18100 96.67200  1.000 37.21820 ? 85  LEU B CB  1 
ATOM   1932 C CG  . LEU B 1 85  ? 104.34400 107.71400 96.47000  1.000 37.21820 ? 85  LEU B CG  1 
ATOM   1933 C CD1 . LEU B 1 85  ? 105.77100 107.59600 95.95700  1.000 37.21820 ? 85  LEU B CD1 1 
ATOM   1934 C CD2 . LEU B 1 85  ? 104.14700 106.91700 97.74400  1.000 37.21820 ? 85  LEU B CD2 1 
ATOM   1935 N N   . LEU B 1 86  ? 101.23100 109.64500 95.19200  1.000 37.33207 ? 86  LEU B N   1 
ATOM   1936 C CA  . LEU B 1 86  ? 100.01300 109.19800 94.53000  1.000 37.33207 ? 86  LEU B CA  1 
ATOM   1937 C C   . LEU B 1 86  ? 99.95000  109.70900 93.10000  1.000 37.33207 ? 86  LEU B C   1 
ATOM   1938 O O   . LEU B 1 86  ? 99.57600  108.96500 92.18600  1.000 37.33207 ? 86  LEU B O   1 
ATOM   1939 C CB  . LEU B 1 86  ? 98.78800  109.65900 95.31300  1.000 37.33207 ? 86  LEU B CB  1 
ATOM   1940 C CG  . LEU B 1 86  ? 98.45400  108.88200 96.58300  1.000 37.33207 ? 86  LEU B CG  1 
ATOM   1941 C CD1 . LEU B 1 86  ? 97.44400  109.64800 97.41800  1.000 37.33207 ? 86  LEU B CD1 1 
ATOM   1942 C CD2 . LEU B 1 86  ? 97.92000  107.51000 96.22100  1.000 37.33207 ? 86  LEU B CD2 1 
ATOM   1943 N N   . PHE B 1 87  ? 100.33100 110.97200 92.88700  1.000 36.13749 ? 87  PHE B N   1 
ATOM   1944 C CA  . PHE B 1 87  ? 100.32100 111.52600 91.53800  1.000 36.13749 ? 87  PHE B CA  1 
ATOM   1945 C C   . PHE B 1 87  ? 101.26100 110.76500 90.61100  1.000 36.13749 ? 87  PHE B C   1 
ATOM   1946 O O   . PHE B 1 87  ? 100.87600 110.39900 89.49900  1.000 36.13749 ? 87  PHE B O   1 
ATOM   1947 C CB  . PHE B 1 87  ? 100.69300 113.00800 91.54700  1.000 36.13749 ? 87  PHE B CB  1 
ATOM   1948 C CG  . PHE B 1 87  ? 100.98200 113.54600 90.17600  1.000 36.13749 ? 87  PHE B CG  1 
ATOM   1949 C CD1 . PHE B 1 87  ? 99.94800  113.79400 89.29000  1.000 36.13749 ? 87  PHE B CD1 1 
ATOM   1950 C CD2 . PHE B 1 87  ? 102.28200 113.76700 89.75500  1.000 36.13749 ? 87  PHE B CD2 1 
ATOM   1951 C CE1 . PHE B 1 87  ? 100.20400 114.26300 88.02300  1.000 36.13749 ? 87  PHE B CE1 1 
ATOM   1952 C CE2 . PHE B 1 87  ? 102.54200 114.23600 88.48800  1.000 36.13749 ? 87  PHE B CE2 1 
ATOM   1953 C CZ  . PHE B 1 87  ? 101.50100 114.48600 87.62200  1.000 36.13749 ? 87  PHE B CZ  1 
ATOM   1954 N N   . VAL B 1 88  ? 102.50700 110.53600 91.03900  1.000 35.62467 ? 88  VAL B N   1 
ATOM   1955 C CA  . VAL B 1 88  ? 103.45900 109.89600 90.13300  1.000 35.62467 ? 88  VAL B CA  1 
ATOM   1956 C C   . VAL B 1 88  ? 103.07800 108.44400 89.89000  1.000 35.62467 ? 88  VAL B C   1 
ATOM   1957 O O   . VAL B 1 88  ? 103.23400 107.94600 88.77200  1.000 35.62467 ? 88  VAL B O   1 
ATOM   1958 C CB  . VAL B 1 88  ? 104.92000 110.02400 90.61800  1.000 35.62467 ? 88  VAL B CB  1 
ATOM   1959 C CG1 . VAL B 1 88  ? 105.40200 111.46400 90.49400  1.000 35.62467 ? 88  VAL B CG1 1 
ATOM   1960 C CG2 . VAL B 1 88  ? 105.10100 109.50200 92.02600  1.000 35.62467 ? 88  VAL B CG2 1 
ATOM   1961 N N   . THR B 1 89  ? 102.53500 107.75700 90.90200  1.000 36.13931 ? 89  THR B N   1 
ATOM   1962 C CA  . THR B 1 89  ? 102.08100 106.38400 90.70700  1.000 36.13931 ? 89  THR B CA  1 
ATOM   1963 C C   . THR B 1 89  ? 100.94200 106.31300 89.69900  1.000 36.13931 ? 89  THR B C   1 
ATOM   1964 O O   . THR B 1 89  ? 101.00500 105.54800 88.72800  1.000 36.13931 ? 89  THR B O   1 
ATOM   1965 C CB  . THR B 1 89  ? 101.63800 105.78200 92.03900  1.000 36.13931 ? 89  THR B CB  1 
ATOM   1966 O OG1 . THR B 1 89  ? 102.58900 106.10800 93.05600  1.000 36.13931 ? 89  THR B OG1 1 
ATOM   1967 C CG2 . THR B 1 89  ? 101.52300 104.28700 91.91700  1.000 36.13931 ? 89  THR B CG2 1 
ATOM   1968 N N   . VAL B 1 90  ? 99.89500  107.11600 89.91000  1.000 35.84484 ? 90  VAL B N   1 
ATOM   1969 C CA  . VAL B 1 90  ? 98.73100  107.08300 89.03100  1.000 35.84484 ? 90  VAL B CA  1 
ATOM   1970 C C   . VAL B 1 90  ? 99.10900  107.53400 87.62700  1.000 35.84484 ? 90  VAL B C   1 
ATOM   1971 O O   . VAL B 1 90  ? 98.67600  106.94000 86.63300  1.000 35.84484 ? 90  VAL B O   1 
ATOM   1972 C CB  . VAL B 1 90  ? 97.59300  107.93700 89.62500  1.000 35.84484 ? 90  VAL B CB  1 
ATOM   1973 C CG1 . VAL B 1 90  ? 96.47700  108.13900 88.62000  1.000 35.84484 ? 90  VAL B CG1 1 
ATOM   1974 C CG2 . VAL B 1 90  ? 97.06000  107.29600 90.88700  1.000 35.84484 ? 90  VAL B CG2 1 
ATOM   1975 N N   . TYR B 1 91  ? 99.94700  108.56600 87.52100  1.000 37.70626 ? 91  TYR B N   1 
ATOM   1976 C CA  . TYR B 1 91  ? 100.33000 109.09500 86.21900  1.000 37.70626 ? 91  TYR B CA  1 
ATOM   1977 C C   . TYR B 1 91  ? 101.20800 108.12200 85.44600  1.000 37.70626 ? 91  TYR B C   1 
ATOM   1978 O O   . TYR B 1 91  ? 101.05300 107.98100 84.23000  1.000 37.70626 ? 91  TYR B O   1 
ATOM   1979 C CB  . TYR B 1 91  ? 101.04200 110.43200 86.38900  1.000 37.70626 ? 91  TYR B CB  1 
ATOM   1980 C CG  . TYR B 1 91  ? 101.08400 111.23100 85.11900  1.000 37.70626 ? 91  TYR B CG  1 
ATOM   1981 C CD1 . TYR B 1 91  ? 99.98300  111.96000 84.70800  1.000 37.70626 ? 91  TYR B CD1 1 
ATOM   1982 C CD2 . TYR B 1 91  ? 102.21500 111.23900 84.31800  1.000 37.70626 ? 91  TYR B CD2 1 
ATOM   1983 C CE1 . TYR B 1 91  ? 100.00900 112.68600 83.54700  1.000 37.70626 ? 91  TYR B CE1 1 
ATOM   1984 C CE2 . TYR B 1 91  ? 102.24900 111.96100 83.15200  1.000 37.70626 ? 91  TYR B CE2 1 
ATOM   1985 C CZ  . TYR B 1 91  ? 101.14200 112.68500 82.77200  1.000 37.70626 ? 91  TYR B CZ  1 
ATOM   1986 O OH  . TYR B 1 91  ? 101.16200 113.41200 81.61300  1.000 37.70626 ? 91  TYR B OH  1 
ATOM   1987 N N   . SER B 1 92  ? 102.14100 107.44700 86.12200  1.000 37.72491 ? 92  SER B N   1 
ATOM   1988 C CA  . SER B 1 92  ? 102.94500 106.44700 85.43300  1.000 37.72491 ? 92  SER B CA  1 
ATOM   1989 C C   . SER B 1 92  ? 102.10600 105.24200 85.03900  1.000 37.72491 ? 92  SER B C   1 
ATOM   1990 O O   . SER B 1 92  ? 102.34400 104.64200 83.98500  1.000 37.72491 ? 92  SER B O   1 
ATOM   1991 C CB  . SER B 1 92  ? 104.13000 106.03000 86.30300  1.000 37.72491 ? 92  SER B CB  1 
ATOM   1992 O OG  . SER B 1 92  ? 103.70700 105.34700 87.46300  1.000 37.72491 ? 92  SER B OG  1 
ATOM   1993 N N   . HIS B 1 93  ? 101.11000 104.88800 85.85500  1.000 39.04881 ? 93  HIS B N   1 
ATOM   1994 C CA  . HIS B 1 93  ? 100.18000 103.83000 85.47800  1.000 39.04881 ? 93  HIS B CA  1 
ATOM   1995 C C   . HIS B 1 93  ? 99.36900  104.22700 84.24800  1.000 39.04881 ? 93  HIS B C   1 
ATOM   1996 O O   . HIS B 1 93  ? 99.11600  103.40000 83.36800  1.000 39.04881 ? 93  HIS B O   1 
ATOM   1997 C CB  . HIS B 1 93  ? 99.27300  103.50800 86.66600  1.000 39.04881 ? 93  HIS B CB  1 
ATOM   1998 C CG  . HIS B 1 93  ? 98.40100  102.30900 86.46800  1.000 39.04881 ? 93  HIS B CG  1 
ATOM   1999 N ND1 . HIS B 1 93  ? 97.37100  101.99600 87.32300  1.000 39.04881 ? 93  HIS B ND1 1 
ATOM   2000 C CD2 . HIS B 1 93  ? 98.40800  101.34500 85.51900  1.000 39.04881 ? 93  HIS B CD2 1 
ATOM   2001 C CE1 . HIS B 1 93  ? 96.77400  100.89500 86.90600  1.000 39.04881 ? 93  HIS B CE1 1 
ATOM   2002 N NE2 . HIS B 1 93  ? 97.38300  100.48100 85.81100  1.000 39.04881 ? 93  HIS B NE2 1 
ATOM   2003 N N   . LEU B 1 94  ? 98.97100  105.49700 84.16400  1.000 39.70166 ? 94  LEU B N   1 
ATOM   2004 C CA  . LEU B 1 94  ? 98.26300  105.98500 82.98400  1.000 39.70166 ? 94  LEU B CA  1 
ATOM   2005 C C   . LEU B 1 94  ? 99.16200  105.99200 81.75300  1.000 39.70166 ? 94  LEU B C   1 
ATOM   2006 O O   . LEU B 1 94  ? 98.70400  105.69700 80.64600  1.000 39.70166 ? 94  LEU B O   1 
ATOM   2007 C CB  . LEU B 1 94  ? 97.71000  107.38200 83.24200  1.000 39.70166 ? 94  LEU B CB  1 
ATOM   2008 C CG  . LEU B 1 94  ? 96.52000  107.48900 84.18600  1.000 39.70166 ? 94  LEU B CG  1 
ATOM   2009 C CD1 . LEU B 1 94  ? 96.27100  108.93700 84.53700  1.000 39.70166 ? 94  LEU B CD1 1 
ATOM   2010 C CD2 . LEU B 1 94  ? 95.29800  106.86900 83.56300  1.000 39.70166 ? 94  LEU B CD2 1 
ATOM   2011 N N   . LEU B 1 95  ? 100.43800 106.34200 81.92700  1.000 42.38255 ? 95  LEU B N   1 
ATOM   2012 C CA  . LEU B 1 95  ? 101.39500 106.26000 80.82700  1.000 42.38255 ? 95  LEU B CA  1 
ATOM   2013 C C   . LEU B 1 95  ? 101.54600 104.82700 80.33300  1.000 42.38255 ? 95  LEU B C   1 
ATOM   2014 O O   . LEU B 1 95  ? 101.59500 104.58100 79.12200  1.000 42.38255 ? 95  LEU B O   1 
ATOM   2015 C CB  . LEU B 1 95  ? 102.75000 106.81600 81.26400  1.000 42.38255 ? 95  LEU B CB  1 
ATOM   2016 C CG  . LEU B 1 95  ? 102.91700 108.32900 81.39600  1.000 42.38255 ? 95  LEU B CG  1 
ATOM   2017 C CD1 . LEU B 1 95  ? 104.36400 108.67100 81.69900  1.000 42.38255 ? 95  LEU B CD1 1 
ATOM   2018 C CD2 . LEU B 1 95  ? 102.46100 109.03400 80.13400  1.000 42.38255 ? 95  LEU B CD2 1 
ATOM   2019 N N   . LEU B 1 96  ? 101.61800 103.86900 81.25900  1.000 45.04576 ? 96  LEU B N   1 
ATOM   2020 C CA  . LEU B 1 96  ? 101.69200 102.46100 80.88000  1.000 45.04576 ? 96  LEU B CA  1 
ATOM   2021 C C   . LEU B 1 96  ? 100.43500 102.00500 80.15100  1.000 45.04576 ? 96  LEU B C   1 
ATOM   2022 O O   . LEU B 1 96  ? 100.51500 101.25100 79.17600  1.000 45.04576 ? 96  LEU B O   1 
ATOM   2023 C CB  . LEU B 1 96  ? 101.92600 101.59800 82.11700  1.000 45.04576 ? 96  LEU B CB  1 
ATOM   2024 C CG  . LEU B 1 96  ? 103.37000 101.51200 82.60000  1.000 45.04576 ? 96  LEU B CG  1 
ATOM   2025 C CD1 . LEU B 1 96  ? 103.44000 100.76200 83.90300  1.000 45.04576 ? 96  LEU B CD1 1 
ATOM   2026 C CD2 . LEU B 1 96  ? 104.24600 100.85500 81.55300  1.000 45.04576 ? 96  LEU B CD2 1 
ATOM   2027 N N   . VAL B 1 97  ? 99.26500  102.43700 80.61700  1.000 46.83880 ? 97  VAL B N   1 
ATOM   2028 C CA  . VAL B 1 97  ? 98.01500  102.02200 79.98800  1.000 46.83880 ? 97  VAL B CA  1 
ATOM   2029 C C   . VAL B 1 97  ? 97.89200  102.61800 78.59000  1.000 46.83880 ? 97  VAL B C   1 
ATOM   2030 O O   . VAL B 1 97  ? 97.50700  101.92700 77.64000  1.000 46.83880 ? 97  VAL B O   1 
ATOM   2031 C CB  . VAL B 1 97  ? 96.82200  102.40000 80.88600  1.000 46.83880 ? 97  VAL B CB  1 
ATOM   2032 C CG1 . VAL B 1 97  ? 95.51200  102.29400 80.12700  1.000 46.83880 ? 97  VAL B CG1 1 
ATOM   2033 C CG2 . VAL B 1 97  ? 96.79400  101.50900 82.11000  1.000 46.83880 ? 97  VAL B CG2 1 
ATOM   2034 N N   . ALA B 1 98  ? 98.23800  103.89900 78.43800  1.000 47.14291 ? 98  ALA B N   1 
ATOM   2035 C CA  . ALA B 1 98  ? 98.21900  104.53300 77.12400  1.000 47.14291 ? 98  ALA B CA  1 
ATOM   2036 C C   . ALA B 1 98  ? 99.24500  103.90700 76.19100  1.000 47.14291 ? 98  ALA B C   1 
ATOM   2037 O O   . ALA B 1 98  ? 99.04600  103.87300 74.97200  1.000 47.14291 ? 98  ALA B O   1 
ATOM   2038 C CB  . ALA B 1 98  ? 98.47000  106.03200 77.26200  1.000 47.14291 ? 98  ALA B CB  1 
ATOM   2039 N N   . ALA B 1 99  ? 100.35200 103.41100 76.74400  1.000 49.33841 ? 99  ALA B N   1 
ATOM   2040 C CA  . ALA B 1 99  ? 101.32500 102.69800 75.92500  1.000 49.33841 ? 99  ALA B CA  1 
ATOM   2041 C C   . ALA B 1 99  ? 100.83900 101.29700 75.57800  1.000 49.33841 ? 99  ALA B C   1 
ATOM   2042 O O   . ALA B 1 99  ? 101.10000 100.80100 74.47700  1.000 49.33841 ? 99  ALA B O   1 
ATOM   2043 C CB  . ALA B 1 99  ? 102.66900 102.63700 76.64600  1.000 49.33841 ? 99  ALA B CB  1 
ATOM   2044 N N   . GLY B 1 100 ? 100.12900 100.64900 76.49500  1.000 52.21790 ? 100 GLY B N   1 
ATOM   2045 C CA  . GLY B 1 100 ? 99.71400  99.27300  76.32500  1.000 52.21790 ? 100 GLY B CA  1 
ATOM   2046 C C   . GLY B 1 100 ? 100.54400 98.25400  77.07700  1.000 52.21790 ? 100 GLY B C   1 
ATOM   2047 O O   . GLY B 1 100 ? 100.32300 97.05200  76.90100  1.000 52.21790 ? 100 GLY B O   1 
ATOM   2048 N N   . LEU B 1 101 ? 101.48700 98.69200  77.90900  1.000 52.91694 ? 101 LEU B N   1 
ATOM   2049 C CA  . LEU B 1 101 ? 102.39700 97.80300  78.61600  1.000 52.91694 ? 101 LEU B CA  1 
ATOM   2050 C C   . LEU B 1 101 ? 102.07500 97.69200  80.09700  1.000 52.91694 ? 101 LEU B C   1 
ATOM   2051 O O   . LEU B 1 101 ? 102.97200 97.41900  80.89800  1.000 52.91694 ? 101 LEU B O   1 
ATOM   2052 C CB  . LEU B 1 101 ? 103.85200 98.26000  78.44000  1.000 52.91694 ? 101 LEU B CB  1 
ATOM   2053 C CG  . LEU B 1 101 ? 104.58600 98.29500  77.08800  1.000 52.91694 ? 101 LEU B CG  1 
ATOM   2054 C CD1 . LEU B 1 101 ? 104.71700 96.88200  76.52900  1.000 52.91694 ? 101 LEU B CD1 1 
ATOM   2055 C CD2 . LEU B 1 101 ? 104.00700 99.24800  76.04400  1.000 52.91694 ? 101 LEU B CD2 1 
ATOM   2056 N N   . GLU B 1 102 ? 100.81400 97.88600  80.47800  1.000 54.15411 ? 102 GLU B N   1 
ATOM   2057 C CA  . GLU B 1 102 ? 100.47400 97.95900  81.89300  1.000 54.15411 ? 102 GLU B CA  1 
ATOM   2058 C C   . GLU B 1 102 ? 100.49900 96.59100  82.56800  1.000 54.15411 ? 102 GLU B C   1 
ATOM   2059 O O   . GLU B 1 102 ? 100.81000 96.51100  83.76100  1.000 54.15411 ? 102 GLU B O   1 
ATOM   2060 C CB  . GLU B 1 102 ? 99.10700  98.62400  82.06500  1.000 54.15411 ? 102 GLU B CB  1 
ATOM   2061 C CG  . GLU B 1 102 ? 97.92400  97.80700  81.55800  1.000 54.15411 ? 102 GLU B CG  1 
ATOM   2062 C CD  . GLU B 1 102 ? 97.72900  97.91600  80.05400  1.000 54.15411 ? 102 GLU B CD  1 
ATOM   2063 O OE1 . GLU B 1 102 ? 98.48400  98.66500  79.40600  1.000 54.15411 ? 102 GLU B OE1 1 
ATOM   2064 O OE2 . GLU B 1 102 ? 96.82900  97.24000  79.51800  1.000 54.15411 ? 102 GLU B OE2 1 
ATOM   2065 N N   . ALA B 1 103 ? 100.21400 95.51400  81.82700  1.000 54.25201 ? 103 ALA B N   1 
ATOM   2066 C CA  . ALA B 1 103 ? 99.93700  94.21000  82.43800  1.000 54.25201 ? 103 ALA B CA  1 
ATOM   2067 C C   . ALA B 1 103 ? 101.06200 93.66700  83.31700  1.000 54.25201 ? 103 ALA B C   1 
ATOM   2068 O O   . ALA B 1 103 ? 100.79000 93.37100  84.49400  1.000 54.25201 ? 103 ALA B O   1 
ATOM   2069 C CB  . ALA B 1 103 ? 99.53900  93.20400  81.34800  1.000 54.25201 ? 103 ALA B CB  1 
ATOM   2070 N N   . PRO B 1 104 ? 102.33100 93.59100  82.88300  1.000 53.90604 ? 104 PRO B N   1 
ATOM   2071 C CA  . PRO B 1 104 ? 103.37200 93.08900  83.79600  1.000 53.90604 ? 104 PRO B CA  1 
ATOM   2072 C C   . PRO B 1 104 ? 103.67000 94.01100  84.96900  1.000 53.90604 ? 104 PRO B C   1 
ATOM   2073 O O   . PRO B 1 104 ? 104.60500 93.73500  85.72800  1.000 53.90604 ? 104 PRO B O   1 
ATOM   2074 C CB  . PRO B 1 104 ? 104.59600 92.95300  82.88400  1.000 53.90604 ? 104 PRO B CB  1 
ATOM   2075 C CG  . PRO B 1 104 ? 104.39200 93.97700  81.86000  1.000 53.90604 ? 104 PRO B CG  1 
ATOM   2076 C CD  . PRO B 1 104 ? 102.92800 93.95500  81.57900  1.000 53.90604 ? 104 PRO B CD  1 
ATOM   2077 N N   . PHE B 1 105 ? 102.92000 95.09700  85.13400  1.000 51.52469 ? 105 PHE B N   1 
ATOM   2078 C CA  . PHE B 1 105 ? 103.05300 95.97500  86.28000  1.000 51.52469 ? 105 PHE B CA  1 
ATOM   2079 C C   . PHE B 1 105 ? 101.78700 96.06000  87.11700  1.000 51.52469 ? 105 PHE B C   1 
ATOM   2080 O O   . PHE B 1 105 ? 101.82400 96.68400  88.18500  1.000 51.52469 ? 105 PHE B O   1 
ATOM   2081 C CB  . PHE B 1 105 ? 103.46200 97.38200  85.82500  1.000 51.52469 ? 105 PHE B CB  1 
ATOM   2082 C CG  . PHE B 1 105 ? 104.72400 97.40900  85.02200  1.000 51.52469 ? 105 PHE B CG  1 
ATOM   2083 C CD1 . PHE B 1 105 ? 104.68400 97.41200  83.64000  1.000 51.52469 ? 105 PHE B CD1 1 
ATOM   2084 C CD2 . PHE B 1 105 ? 105.95400 97.41800  85.65000  1.000 51.52469 ? 105 PHE B CD2 1 
ATOM   2085 C CE1 . PHE B 1 105 ? 105.84100 97.43200  82.90300  1.000 51.52469 ? 105 PHE B CE1 1 
ATOM   2086 C CE2 . PHE B 1 105 ? 107.11700 97.43800  84.91600  1.000 51.52469 ? 105 PHE B CE2 1 
ATOM   2087 C CZ  . PHE B 1 105 ? 107.06000 97.44500  83.54000  1.000 51.52469 ? 105 PHE B CZ  1 
ATOM   2088 N N   . LEU B 1 106 ? 100.68000 95.43600  86.68100  1.000 49.61620 ? 106 LEU B N   1 
ATOM   2089 C CA  . LEU B 1 106 ? 99.42000  95.57200  87.41400  1.000 49.61620 ? 106 LEU B CA  1 
ATOM   2090 C C   . LEU B 1 106 ? 99.53000  95.10300  88.85900  1.000 49.61620 ? 106 LEU B C   1 
ATOM   2091 O O   . LEU B 1 106 ? 99.10500  95.82700  89.76800  1.000 49.61620 ? 106 LEU B O   1 
ATOM   2092 C CB  . LEU B 1 106 ? 98.29600  94.81400  86.70500  1.000 49.61620 ? 106 LEU B CB  1 
ATOM   2093 C CG  . LEU B 1 106 ? 97.91200  95.22600  85.28800  1.000 49.61620 ? 106 LEU B CG  1 
ATOM   2094 C CD1 . LEU B 1 106 ? 96.51400  94.73800  84.97700  1.000 49.61620 ? 106 LEU B CD1 1 
ATOM   2095 C CD2 . LEU B 1 106 ? 97.95100  96.73700  85.16600  1.000 49.61620 ? 106 LEU B CD2 1 
ATOM   2096 N N   . TYR B 1 107 ? 100.14500 93.93700  89.08800  1.000 48.45685 ? 107 TYR B N   1 
ATOM   2097 C CA  . TYR B 1 107 ? 100.32400 93.43200  90.44600  1.000 48.45685 ? 107 TYR B CA  1 
ATOM   2098 C C   . TYR B 1 107 ? 101.10400 94.41600  91.30600  1.000 48.45685 ? 107 TYR B C   1 
ATOM   2099 O O   . TYR B 1 107 ? 100.86900 94.51000  92.51400  1.000 48.45685 ? 107 TYR B O   1 
ATOM   2100 C CB  . TYR B 1 107 ? 101.02800 92.07500  90.41800  1.000 48.45685 ? 107 TYR B CB  1 
ATOM   2101 C CG  . TYR B 1 107 ? 102.52700 92.16200  90.23300  1.000 48.45685 ? 107 TYR B CG  1 
ATOM   2102 C CD1 . TYR B 1 107 ? 103.39400 91.98500  91.30700  1.000 48.45685 ? 107 TYR B CD1 1 
ATOM   2103 C CD2 . TYR B 1 107 ? 103.07700 92.43100  88.98400  1.000 48.45685 ? 107 TYR B CD2 1 
ATOM   2104 C CE1 . TYR B 1 107 ? 104.76400 92.07100  91.14000  1.000 48.45685 ? 107 TYR B CE1 1 
ATOM   2105 C CE2 . TYR B 1 107 ? 104.44300 92.51800  88.81000  1.000 48.45685 ? 107 TYR B CE2 1 
ATOM   2106 C CZ  . TYR B 1 107 ? 105.28100 92.33500  89.88900  1.000 48.45685 ? 107 TYR B CZ  1 
ATOM   2107 O OH  . TYR B 1 107 ? 106.64100 92.42100  89.71500  1.000 48.45685 ? 107 TYR B OH  1 
ATOM   2108 N N   . LEU B 1 108 ? 102.03400 95.15600  90.70300  1.000 43.76126 ? 108 LEU B N   1 
ATOM   2109 C CA  . LEU B 1 108 ? 102.73100 96.19100  91.45000  1.000 43.76126 ? 108 LEU B CA  1 
ATOM   2110 C C   . LEU B 1 108 ? 101.78900 97.33500  91.79100  1.000 43.76126 ? 108 LEU B C   1 
ATOM   2111 O O   . LEU B 1 108 ? 101.67000 97.72300  92.95900  1.000 43.76126 ? 108 LEU B O   1 
ATOM   2112 C CB  . LEU B 1 108 ? 103.92700 96.69000  90.64400  1.000 43.76126 ? 108 LEU B CB  1 
ATOM   2113 C CG  . LEU B 1 108 ? 105.21200 97.01900  91.39600  1.000 43.76126 ? 108 LEU B CG  1 
ATOM   2114 C CD1 . LEU B 1 108 ? 105.60100 95.87900  92.31800  1.000 43.76126 ? 108 LEU B CD1 1 
ATOM   2115 C CD2 . LEU B 1 108 ? 106.31900 97.29100  90.40300  1.000 43.76126 ? 108 LEU B CD2 1 
ATOM   2116 N N   . TYR B 1 109 ? 101.05400 97.83600  90.79200  1.000 40.13907 ? 109 TYR B N   1 
ATOM   2117 C CA  . TYR B 1 109 ? 100.25600 99.03800  90.99600  1.000 40.13907 ? 109 TYR B CA  1 
ATOM   2118 C C   . TYR B 1 109 ? 99.10000  98.77300  91.94300  1.000 40.13907 ? 109 TYR B C   1 
ATOM   2119 O O   . TYR B 1 109 ? 98.86700  99.55600  92.87100  1.000 40.13907 ? 109 TYR B O   1 
ATOM   2120 C CB  . TYR B 1 109 ? 99.76000  99.57300  89.65600  1.000 40.13907 ? 109 TYR B CB  1 
ATOM   2121 C CG  . TYR B 1 109 ? 100.79600 100.41700 88.98000  1.000 40.13907 ? 109 TYR B CG  1 
ATOM   2122 C CD1 . TYR B 1 109 ? 101.05800 101.70200 89.42100  1.000 40.13907 ? 109 TYR B CD1 1 
ATOM   2123 C CD2 . TYR B 1 109 ? 101.54300 99.91900  87.92400  1.000 40.13907 ? 109 TYR B CD2 1 
ATOM   2124 C CE1 . TYR B 1 109 ? 102.02000 102.47500 88.81900  1.000 40.13907 ? 109 TYR B CE1 1 
ATOM   2125 C CE2 . TYR B 1 109 ? 102.50800 100.68600 87.31600  1.000 40.13907 ? 109 TYR B CE2 1 
ATOM   2126 C CZ  . TYR B 1 109 ? 102.74100 101.96300 87.76600  1.000 40.13907 ? 109 TYR B CZ  1 
ATOM   2127 O OH  . TYR B 1 109 ? 103.69800 102.73800 87.16500  1.000 40.13907 ? 109 TYR B OH  1 
ATOM   2128 N N   . ALA B 1 110 ? 98.40900  97.64600  91.74500  1.000 38.96101 ? 110 ALA B N   1 
ATOM   2129 C CA  . ALA B 1 110 ? 97.41600  97.18700  92.70600  1.000 38.96101 ? 110 ALA B CA  1 
ATOM   2130 C C   . ALA B 1 110 ? 97.99100  97.16200  94.11100  1.000 38.96101 ? 110 ALA B C   1 
ATOM   2131 O O   . ALA B 1 110 ? 97.38400  97.71000  95.04100  1.000 38.96101 ? 110 ALA B O   1 
ATOM   2132 C CB  . ALA B 1 110 ? 96.90900  95.80000  92.31400  1.000 38.96101 ? 110 ALA B CB  1 
ATOM   2133 N N   . LEU B 1 111 ? 99.20700  96.61600  94.25800  1.000 38.60687 ? 111 LEU B N   1 
ATOM   2134 C CA  . LEU B 1 111 ? 99.85800  96.59000  95.56000  1.000 38.60687 ? 111 LEU B CA  1 
ATOM   2135 C C   . LEU B 1 111 ? 99.97100  97.99100  96.13700  1.000 38.60687 ? 111 LEU B C   1 
ATOM   2136 O O   . LEU B 1 111 ? 99.51700  98.23100  97.26400  1.000 38.60687 ? 111 LEU B O   1 
ATOM   2137 C CB  . LEU B 1 111 ? 101.23500 95.93700  95.45100  1.000 38.60687 ? 111 LEU B CB  1 
ATOM   2138 C CG  . LEU B 1 111 ? 102.03400 95.77700  96.74400  1.000 38.60687 ? 111 LEU B CG  1 
ATOM   2139 C CD1 . LEU B 1 111 ? 101.20500 95.10000  97.82400  1.000 38.60687 ? 111 LEU B CD1 1 
ATOM   2140 C CD2 . LEU B 1 111 ? 103.29800 94.99700  96.48100  1.000 38.60687 ? 111 LEU B CD2 1 
ATOM   2141 N N   . VAL B 1 112 ? 100.46400 98.94600  95.33400  1.000 36.54303 ? 112 VAL B N   1 
ATOM   2142 C CA  . VAL B 1 112 ? 100.57700 100.32800 95.79500  1.000 36.54303 ? 112 VAL B CA  1 
ATOM   2143 C C   . VAL B 1 112 ? 99.22500  100.82600 96.26100  1.000 36.54303 ? 112 VAL B C   1 
ATOM   2144 O O   . VAL B 1 112 ? 99.07700  101.29900 97.39700  1.000 36.54303 ? 112 VAL B O   1 
ATOM   2145 C CB  . VAL B 1 112 ? 101.13300 101.23900 94.68500  1.000 36.54303 ? 112 VAL B CB  1 
ATOM   2146 C CG1 . VAL B 1 112 ? 101.06900 102.69000 95.13100  1.000 36.54303 ? 112 VAL B CG1 1 
ATOM   2147 C CG2 . VAL B 1 112 ? 102.53300 100.86600 94.33300  1.000 36.54303 ? 112 VAL B CG2 1 
ATOM   2148 N N   . TYR B 1 113 ? 98.20000  100.62000 95.42800  1.000 36.11422 ? 113 TYR B N   1 
ATOM   2149 C CA  . TYR B 1 113 ? 96.88300  101.13100 95.76000  1.000 36.11422 ? 113 TYR B CA  1 
ATOM   2150 C C   . TYR B 1 113 ? 96.38400  100.49600 97.03800  1.000 36.11422 ? 113 TYR B C   1 
ATOM   2151 O O   . TYR B 1 113 ? 95.93000  101.21200 97.94000  1.000 36.11422 ? 113 TYR B O   1 
ATOM   2152 C CB  . TYR B 1 113 ? 95.91900  100.89400 94.60000  1.000 36.11422 ? 113 TYR B CB  1 
ATOM   2153 C CG  . TYR B 1 113 ? 96.33900  101.59400 93.33400  1.000 36.11422 ? 113 TYR B CG  1 
ATOM   2154 C CD1 . TYR B 1 113 ? 96.96100  102.83500 93.38000  1.000 36.11422 ? 113 TYR B CD1 1 
ATOM   2155 C CD2 . TYR B 1 113 ? 96.13000  101.01300 92.09300  1.000 36.11422 ? 113 TYR B CD2 1 
ATOM   2156 C CE1 . TYR B 1 113 ? 97.35900  103.47400 92.23100  1.000 36.11422 ? 113 TYR B CE1 1 
ATOM   2157 C CE2 . TYR B 1 113 ? 96.52400  101.64800 90.93900  1.000 36.11422 ? 113 TYR B CE2 1 
ATOM   2158 C CZ  . TYR B 1 113 ? 97.13700  102.87900 91.01300  1.000 36.11422 ? 113 TYR B CZ  1 
ATOM   2159 O OH  . TYR B 1 113 ? 97.52800  103.51800 89.86400  1.000 36.11422 ? 113 TYR B OH  1 
ATOM   2160 N N   . PHE B 1 114 ? 96.60600  99.18700  97.18500  1.000 37.29479 ? 114 PHE B N   1 
ATOM   2161 C CA  . PHE B 1 114 ? 96.19000  98.50400  98.39900  1.000 37.29479 ? 114 PHE B CA  1 
ATOM   2162 C C   . PHE B 1 114 ? 96.87900  99.11300  99.60700  1.000 37.29479 ? 114 PHE B C   1 
ATOM   2163 O O   . PHE B 1 114 ? 96.21400  99.52200  100.56800 1.000 37.29479 ? 114 PHE B O   1 
ATOM   2164 C CB  . PHE B 1 114 ? 96.48400  97.01000  98.28100  1.000 37.29479 ? 114 PHE B CB  1 
ATOM   2165 C CG  . PHE B 1 114 ? 96.22200  96.23900  99.53500  1.000 37.29479 ? 114 PHE B CG  1 
ATOM   2166 C CD1 . PHE B 1 114 ? 97.26900  95.79000  100.31500 1.000 37.29479 ? 114 PHE B CD1 1 
ATOM   2167 C CD2 . PHE B 1 114 ? 94.92800  95.97500  99.94300  1.000 37.29479 ? 114 PHE B CD2 1 
ATOM   2168 C CE1 . PHE B 1 114 ? 97.03100  95.07600  101.46700 1.000 37.29479 ? 114 PHE B CE1 1 
ATOM   2169 C CE2 . PHE B 1 114 ? 94.68400  95.26700  101.10100 1.000 37.29479 ? 114 PHE B CE2 1 
ATOM   2170 C CZ  . PHE B 1 114 ? 95.73500  94.81900  101.86400 1.000 37.29479 ? 114 PHE B CZ  1 
ATOM   2171 N N   . LEU B 1 115 ? 98.19900  99.30100  99.51600  1.000 37.40857 ? 115 LEU B N   1 
ATOM   2172 C CA  . LEU B 1 115 ? 98.91500  99.88500  100.63800 1.000 37.40857 ? 115 LEU B CA  1 
ATOM   2173 C C   . LEU B 1 115 ? 98.43300  101.30000 100.90500 1.000 37.40857 ? 115 LEU B C   1 
ATOM   2174 O O   . LEU B 1 115 ? 98.20400  101.66200 102.06600 1.000 37.40857 ? 115 LEU B O   1 
ATOM   2175 C CB  . LEU B 1 115 ? 100.42000 99.85500  100.38400 1.000 37.40857 ? 115 LEU B CB  1 
ATOM   2176 C CG  . LEU B 1 115 ? 101.05600 98.48300  100.14300 1.000 37.40857 ? 115 LEU B CG  1 
ATOM   2177 C CD1 . LEU B 1 115 ? 102.50500 98.61700  99.72200  1.000 37.40857 ? 115 LEU B CD1 1 
ATOM   2178 C CD2 . LEU B 1 115 ? 100.93400 97.59300  101.36300 1.000 37.40857 ? 115 LEU B CD2 1 
ATOM   2179 N N   . GLN B 1 116 ? 98.17800  102.07100 99.84300  1.000 37.54971 ? 116 GLN B N   1 
ATOM   2180 C CA  . GLN B 1 116 ? 97.71500  103.43400 100.04800 1.000 37.54971 ? 116 GLN B CA  1 
ATOM   2181 C C   . GLN B 1 116 ? 96.34900  103.44200 100.70400 1.000 37.54971 ? 116 GLN B C   1 
ATOM   2182 O O   . GLN B 1 116 ? 96.09900  104.27400 101.58500 1.000 37.54971 ? 116 GLN B O   1 
ATOM   2183 C CB  . GLN B 1 116 ? 97.69900  104.19900 98.72900  1.000 37.54971 ? 116 GLN B CB  1 
ATOM   2184 C CG  . GLN B 1 116 ? 99.07000  104.66400 98.29700  1.000 37.54971 ? 116 GLN B CG  1 
ATOM   2185 C CD  . GLN B 1 116 ? 99.65900  105.68500 99.24300  1.000 37.54971 ? 116 GLN B CD  1 
ATOM   2186 O OE1 . GLN B 1 116 ? 99.00900  106.66600 99.59900  1.000 37.54971 ? 116 GLN B OE1 1 
ATOM   2187 N NE2 . GLN B 1 116 ? 100.89600 105.46200 99.65600  1.000 37.54971 ? 116 GLN B NE2 1 
ATOM   2188 N N   . SER B 1 117 ? 95.49800  102.47100 100.35100 1.000 37.13269 ? 117 SER B N   1 
ATOM   2189 C CA  . SER B 1 117 ? 94.20600  102.35700 101.01200 1.000 37.13269 ? 117 SER B CA  1 
ATOM   2190 C C   . SER B 1 117 ? 94.38800  102.18100 102.50800 1.000 37.13269 ? 117 SER B C   1 
ATOM   2191 O O   . SER B 1 117 ? 93.76000  102.89400 103.30100 1.000 37.13269 ? 117 SER B O   1 
ATOM   2192 C CB  . SER B 1 117 ? 93.40900  101.19500 100.42500 1.000 37.13269 ? 117 SER B CB  1 
ATOM   2193 O OG  . SER B 1 117 ? 92.68100  101.61000 99.28900  1.000 37.13269 ? 117 SER B OG  1 
ATOM   2194 N N   . ILE B 1 118 ? 95.32200  101.30800 102.90300 1.000 37.57778 ? 118 ILE B N   1 
ATOM   2195 C CA  . ILE B 1 118 ? 95.58100  101.09300 104.32100 1.000 37.57778 ? 118 ILE B CA  1 
ATOM   2196 C C   . ILE B 1 118 ? 96.02600  102.39200 104.96500 1.000 37.57778 ? 118 ILE B C   1 
ATOM   2197 O O   . ILE B 1 118 ? 95.52400  102.77800 106.02900 1.000 37.57778 ? 118 ILE B O   1 
ATOM   2198 C CB  . ILE B 1 118 ? 96.61700  99.97000  104.51400 1.000 37.57778 ? 118 ILE B CB  1 
ATOM   2199 C CG1 . ILE B 1 118 ? 96.01800  98.62700  104.10800 1.000 37.57778 ? 118 ILE B CG1 1 
ATOM   2200 C CG2 . ILE B 1 118 ? 97.08700  99.91100  105.95100 1.000 37.57778 ? 118 ILE B CG2 1 
ATOM   2201 C CD1 . ILE B 1 118 ? 97.03300  97.53800  103.98400 1.000 37.57778 ? 118 ILE B CD1 1 
ATOM   2202 N N   . ASN B 1 119 ? 96.90000  103.13200 104.27600 1.000 38.18246 ? 119 ASN B N   1 
ATOM   2203 C CA  . ASN B 1 119 ? 97.38500  104.39000 104.82000 1.000 38.18246 ? 119 ASN B CA  1 
ATOM   2204 C C   . ASN B 1 119 ? 96.23700  105.36700 105.00900 1.000 38.18246 ? 119 ASN B C   1 
ATOM   2205 O O   . ASN B 1 119 ? 96.15000  106.03100 106.05000 1.000 38.18246 ? 119 ASN B O   1 
ATOM   2206 C CB  . ASN B 1 119 ? 98.45800  104.97200 103.90900 1.000 38.18246 ? 119 ASN B CB  1 
ATOM   2207 C CG  . ASN B 1 119 ? 99.03900  106.25500 104.44300 1.000 38.18246 ? 119 ASN B CG  1 
ATOM   2208 O OD1 . ASN B 1 119 ? 99.60000  106.28600 105.53200 1.000 38.18246 ? 119 ASN B OD1 1 
ATOM   2209 N ND2 . ASN B 1 119 ? 98.91600  107.32300 103.67300 1.000 38.18246 ? 119 ASN B ND2 1 
ATOM   2210 N N   . PHE B 1 120 ? 95.30200  105.39300 104.05200 1.000 37.53136 ? 120 PHE B N   1 
ATOM   2211 C CA  . PHE B 1 120 ? 94.13200  106.24300 104.19300 1.000 37.53136 ? 120 PHE B CA  1 
ATOM   2212 C C   . PHE B 1 120 ? 93.36200  105.88300 105.45300 1.000 37.53136 ? 120 PHE B C   1 
ATOM   2213 O O   . PHE B 1 120 ? 93.06900  106.76000 106.27800 1.000 37.53136 ? 120 PHE B O   1 
ATOM   2214 C CB  . PHE B 1 120 ? 93.24500  106.12200 102.95700 1.000 37.53136 ? 120 PHE B CB  1 
ATOM   2215 C CG  . PHE B 1 120 ? 91.95300  106.87500 103.06200 1.000 37.53136 ? 120 PHE B CG  1 
ATOM   2216 C CD1 . PHE B 1 120 ? 91.94000  108.25800 103.01600 1.000 37.53136 ? 120 PHE B CD1 1 
ATOM   2217 C CD2 . PHE B 1 120 ? 90.75400  106.20200 103.20900 1.000 37.53136 ? 120 PHE B CD2 1 
ATOM   2218 C CE1 . PHE B 1 120 ? 90.75400  108.95700 103.11100 1.000 37.53136 ? 120 PHE B CE1 1 
ATOM   2219 C CE2 . PHE B 1 120 ? 89.56500  106.89400 103.30400 1.000 37.53136 ? 120 PHE B CE2 1 
ATOM   2220 C CZ  . PHE B 1 120 ? 89.56500  108.27400 103.25400 1.000 37.53136 ? 120 PHE B CZ  1 
ATOM   2221 N N   . VAL B 1 121 ? 93.13100  104.58200 105.66700 1.000 37.26314 ? 121 VAL B N   1 
ATOM   2222 C CA  . VAL B 1 121 ? 92.43300  104.13700 106.86600 1.000 37.26314 ? 121 VAL B CA  1 
ATOM   2223 C C   . VAL B 1 121 ? 93.20500  104.56500 108.10100 1.000 37.26314 ? 121 VAL B C   1 
ATOM   2224 O O   . VAL B 1 121 ? 92.62600  105.10200 109.05500 1.000 37.26314 ? 121 VAL B O   1 
ATOM   2225 C CB  . VAL B 1 121 ? 92.21400  102.61300 106.82900 1.000 37.26314 ? 121 VAL B CB  1 
ATOM   2226 C CG1 . VAL B 1 121 ? 91.66400  102.12000 108.15200 1.000 37.26314 ? 121 VAL B CG1 1 
ATOM   2227 C CG2 . VAL B 1 121 ? 91.27500  102.24800 105.70300 1.000 37.26314 ? 121 VAL B CG2 1 
ATOM   2228 N N   . ARG B 1 122 ? 94.53500  104.43100 108.05400 1.000 40.44898 ? 122 ARG B N   1 
ATOM   2229 C CA  . ARG B 1 122 ? 95.35200  104.80600 109.19800 1.000 40.44898 ? 122 ARG B CA  1 
ATOM   2230 C C   . ARG B 1 122 ? 95.18100  106.28100 109.51500 1.000 40.44898 ? 122 ARG B C   1 
ATOM   2231 O O   . ARG B 1 122 ? 94.97800  106.65000 110.67900 1.000 40.44898 ? 122 ARG B O   1 
ATOM   2232 C CB  . ARG B 1 122 ? 96.81600  104.47100 108.92900 1.000 40.44898 ? 122 ARG B CB  1 
ATOM   2233 C CG  . ARG B 1 122 ? 97.76900  104.97200 109.98600 1.000 40.44898 ? 122 ARG B CG  1 
ATOM   2234 C CD  . ARG B 1 122 ? 99.20000  104.91100 109.50600 1.000 40.44898 ? 122 ARG B CD  1 
ATOM   2235 N NE  . ARG B 1 122 ? 99.48800  105.92800 108.50100 1.000 40.44898 ? 122 ARG B NE  1 
ATOM   2236 C CZ  . ARG B 1 122 ? 99.79800  107.18800 108.78000 1.000 40.44898 ? 122 ARG B CZ  1 
ATOM   2237 N NH1 . ARG B 1 122 ? 99.85800  107.59600 110.03800 1.000 40.44898 ? 122 ARG B NH1 1 
ATOM   2238 N NH2 . ARG B 1 122 ? 100.04800 108.04200 107.80000 1.000 40.44898 ? 122 ARG B NH2 1 
ATOM   2239 N N   . ILE B 1 123 ? 95.15000  107.12300 108.47600 1.000 38.82102 ? 123 ILE B N   1 
ATOM   2240 C CA  . ILE B 1 123 ? 94.98700  108.55500 108.69300 1.000 38.82102 ? 123 ILE B CA  1 
ATOM   2241 C C   . ILE B 1 123 ? 93.64700  108.82500 109.35500 1.000 38.82102 ? 123 ILE B C   1 
ATOM   2242 O O   . ILE B 1 123 ? 93.56300  109.59100 110.32400 1.000 38.82102 ? 123 ILE B O   1 
ATOM   2243 C CB  . ILE B 1 123 ? 95.14700  109.31900 107.36600 1.000 38.82102 ? 123 ILE B CB  1 
ATOM   2244 C CG1 . ILE B 1 123 ? 96.62700  109.45500 107.01800 1.000 38.82102 ? 123 ILE B CG1 1 
ATOM   2245 C CG2 . ILE B 1 123 ? 94.51000  110.69200 107.44700 1.000 38.82102 ? 123 ILE B CG2 1 
ATOM   2246 C CD1 . ILE B 1 123 ? 96.88200  109.88900 105.60100 1.000 38.82102 ? 123 ILE B CD1 1 
ATOM   2247 N N   . ILE B 1 124 ? 92.60200  108.11600 108.91000 1.000 38.33494 ? 124 ILE B N   1 
ATOM   2248 C CA  . ILE B 1 124 ? 91.28600  108.26700 109.51700 1.000 38.33494 ? 124 ILE B CA  1 
ATOM   2249 C C   . ILE B 1 124 ? 91.35500  107.91800 110.99300 1.000 38.33494 ? 124 ILE B C   1 
ATOM   2250 O O   . ILE B 1 124 ? 90.89700  108.69000 111.84600 1.000 38.33494 ? 124 ILE B O   1 
ATOM   2251 C CB  . ILE B 1 124 ? 90.24500  107.40200 108.77900 1.000 38.33494 ? 124 ILE B CB  1 
ATOM   2252 C CG1 . ILE B 1 124 ? 90.06700  107.86600 107.33200 1.000 38.33494 ? 124 ILE B CG1 1 
ATOM   2253 C CG2 . ILE B 1 124 ? 88.91300  107.43100 109.50700 1.000 38.33494 ? 124 ILE B CG2 1 
ATOM   2254 C CD1 . ILE B 1 124 ? 89.95700  109.36100 107.16400 1.000 38.33494 ? 124 ILE B CD1 1 
ATOM   2255 N N   . MET B 1 125 ? 92.01700  106.80100 111.32100 1.000 40.70622 ? 125 MET B N   1 
ATOM   2256 C CA  . MET B 1 125 ? 92.13800  106.41200 112.72000 1.000 40.70622 ? 125 MET B CA  1 
ATOM   2257 C C   . MET B 1 125 ? 92.89500  107.46600 113.50400 1.000 40.70622 ? 125 MET B C   1 
ATOM   2258 O O   . MET B 1 125 ? 92.49100  107.82300 114.61800 1.000 40.70622 ? 125 MET B O   1 
ATOM   2259 C CB  . MET B 1 125 ? 92.81400  105.04700 112.84800 1.000 40.70622 ? 125 MET B CB  1 
ATOM   2260 C CG  . MET B 1 125 ? 92.12700  103.93300 112.08400 1.000 40.70622 ? 125 MET B CG  1 
ATOM   2261 S SD  . MET B 1 125 ? 90.64900  103.23400 112.86100 1.000 40.70622 ? 125 MET B SD  1 
ATOM   2262 C CE  . MET B 1 125 ? 90.86500  103.63800 114.60100 1.000 40.70622 ? 125 MET B CE  1 
ATOM   2263 N N   . ARG B 1 126 ? 93.93600  108.04000 112.89500 1.000 36.43597 ? 126 ARG B N   1 
ATOM   2264 C CA  . ARG B 1 126 ? 94.67900  109.09700 113.56100 1.000 36.43597 ? 126 ARG B CA  1 
ATOM   2265 C C   . ARG B 1 126 ? 93.77000  110.27500 113.86900 1.000 36.43597 ? 126 ARG B C   1 
ATOM   2266 O O   . ARG B 1 126 ? 93.75100  110.76600 115.00500 1.000 36.43597 ? 126 ARG B O   1 
ATOM   2267 C CB  . ARG B 1 126 ? 95.86400  109.52800 112.70200 1.000 36.43597 ? 126 ARG B CB  1 
ATOM   2268 C CG  . ARG B 1 126 ? 97.05000  110.00600 113.50000 1.000 36.43597 ? 126 ARG B CG  1 
ATOM   2269 C CD  . ARG B 1 126 ? 97.68300  108.86500 114.26800 1.000 36.43597 ? 126 ARG B CD  1 
ATOM   2270 N NE  . ARG B 1 126 ? 98.74700  109.32000 115.15200 1.000 36.43597 ? 126 ARG B NE  1 
ATOM   2271 C CZ  . ARG B 1 126 ? 99.44600  108.52600 115.95300 1.000 36.43597 ? 126 ARG B CZ  1 
ATOM   2272 N NH1 . ARG B 1 126 ? 99.19900  107.22800 115.98500 1.000 36.43597 ? 126 ARG B NH1 1 
ATOM   2273 N NH2 . ARG B 1 126 ? 100.39600 109.03200 116.71700 1.000 36.43597 ? 126 ARG B NH2 1 
ATOM   2274 N N   . LEU B 1 127 ? 92.93300  110.66300 112.90000 1.000 36.92870 ? 127 LEU B N   1 
ATOM   2275 C CA  . LEU B 1 127 ? 91.99900  111.75400 113.13300 1.000 36.92870 ? 127 LEU B CA  1 
ATOM   2276 C C   . LEU B 1 127 ? 91.03000  111.39400 114.24000 1.000 36.92870 ? 127 LEU B C   1 
ATOM   2277 O O   . LEU B 1 127 ? 90.73600  112.22100 115.11100 1.000 36.92870 ? 127 LEU B O   1 
ATOM   2278 C CB  . LEU B 1 127 ? 91.24200  112.09400 111.85200 1.000 36.92870 ? 127 LEU B CB  1 
ATOM   2279 C CG  . LEU B 1 127 ? 92.06500  112.78900 110.77200 1.000 36.92870 ? 127 LEU B CG  1 
ATOM   2280 C CD1 . LEU B 1 127 ? 91.28900  112.85100 109.47400 1.000 36.92870 ? 127 LEU B CD1 1 
ATOM   2281 C CD2 . LEU B 1 127 ? 92.47200  114.17300 111.23100 1.000 36.92870 ? 127 LEU B CD2 1 
ATOM   2282 N N   . TRP B 1 128 ? 90.58300  110.14000 114.26100 1.000 40.67555 ? 128 TRP B N   1 
ATOM   2283 C CA  . TRP B 1 128 ? 89.64800  109.73300 115.29300 1.000 40.67555 ? 128 TRP B CA  1 
ATOM   2284 C C   . TRP B 1 128 ? 90.33200  109.72800 116.65200 1.000 40.67555 ? 128 TRP B C   1 
ATOM   2285 O O   . TRP B 1 128 ? 89.71300  110.07500 117.66600 1.000 40.67555 ? 128 TRP B O   1 
ATOM   2286 C CB  . TRP B 1 128 ? 89.05800  108.37000 114.94500 1.000 40.67555 ? 128 TRP B CB  1 
ATOM   2287 C CG  . TRP B 1 128 ? 88.08500  107.89600 115.93700 1.000 40.67555 ? 128 TRP B CG  1 
ATOM   2288 C CD1 . TRP B 1 128 ? 86.75400  108.17900 115.96800 1.000 40.67555 ? 128 TRP B CD1 1 
ATOM   2289 C CD2 . TRP B 1 128 ? 88.33700  107.03200 117.04000 1.000 40.67555 ? 128 TRP B CD2 1 
ATOM   2290 N NE1 . TRP B 1 128 ? 86.16400  107.56200 117.03500 1.000 40.67555 ? 128 TRP B NE1 1 
ATOM   2291 C CE2 . TRP B 1 128 ? 87.11500  106.84800 117.71000 1.000 40.67555 ? 128 TRP B CE2 1 
ATOM   2292 C CE3 . TRP B 1 128 ? 89.48000  106.40400 117.53600 1.000 40.67555 ? 128 TRP B CE3 1 
ATOM   2293 C CZ2 . TRP B 1 128 ? 87.00000  106.06100 118.83900 1.000 40.67555 ? 128 TRP B CZ2 1 
ATOM   2294 C CZ3 . TRP B 1 128 ? 89.36300  105.62600 118.65700 1.000 40.67555 ? 128 TRP B CZ3 1 
ATOM   2295 C CH2 . TRP B 1 128 ? 88.13000  105.45700 119.29400 1.000 40.67555 ? 128 TRP B CH2 1 
ATOM   2296 N N   . LEU B 1 129 ? 91.62700  109.39500 116.67800 1.000 36.37962 ? 129 LEU B N   1 
ATOM   2297 C CA  . LEU B 1 129 ? 92.38200  109.49400 117.91800 1.000 36.37962 ? 129 LEU B CA  1 
ATOM   2298 C C   . LEU B 1 129 ? 92.43400  110.93900 118.38500 1.000 36.37962 ? 129 LEU B C   1 
ATOM   2299 O O   . LEU B 1 129 ? 92.26900  111.22000 119.57800 1.000 36.37962 ? 129 LEU B O   1 
ATOM   2300 C CB  . LEU B 1 129 ? 93.78500  108.92000 117.72400 1.000 36.37962 ? 129 LEU B CB  1 
ATOM   2301 C CG  . LEU B 1 129 ? 94.61100  108.53000 118.95000 1.000 36.37962 ? 129 LEU B CG  1 
ATOM   2302 C CD1 . LEU B 1 129 ? 93.82900  107.61400 119.86900 1.000 36.37962 ? 129 LEU B CD1 1 
ATOM   2303 C CD2 . LEU B 1 129 ? 95.89600  107.85900 118.50100 1.000 36.37962 ? 129 LEU B CD2 1 
ATOM   2304 N N   . CYS B 1 130 ? 92.58400  111.87100 117.43900 1.000 35.23629 ? 130 CYS B N   1 
ATOM   2305 C CA  . CYS B 1 130 ? 92.52400  113.28600 117.77400 1.000 35.23629 ? 130 CYS B CA  1 
ATOM   2306 C C   . CYS B 1 130 ? 91.17000  113.65200 118.35200 1.000 35.23629 ? 130 CYS B C   1 
ATOM   2307 O O   . CYS B 1 130 ? 91.07800  114.49100 119.25400 1.000 35.23629 ? 130 CYS B O   1 
ATOM   2308 C CB  . CYS B 1 130 ? 92.82700  114.13400 116.54200 1.000 35.23629 ? 130 CYS B CB  1 
ATOM   2309 S SG  . CYS B 1 130 ? 94.54700  114.13800 116.09200 1.000 35.23629 ? 130 CYS B SG  1 
ATOM   2310 N N   . TRP B 1 131 ? 90.10700  113.03000 117.85000 1.000 35.20792 ? 131 TRP B N   1 
ATOM   2311 C CA  . TRP B 1 131 ? 88.79700  113.28000 118.42500 1.000 35.20792 ? 131 TRP B CA  1 
ATOM   2312 C C   . TRP B 1 131 ? 88.69200  112.67000 119.81600 1.000 35.20792 ? 131 TRP B C   1 
ATOM   2313 O O   . TRP B 1 131 ? 88.05500  113.24500 120.70400 1.000 35.20792 ? 131 TRP B O   1 
ATOM   2314 C CB  . TRP B 1 131 ? 87.70700  112.73600 117.50300 1.000 35.20792 ? 131 TRP B CB  1 
ATOM   2315 C CG  . TRP B 1 131 ? 86.35800  112.74300 118.12200 1.000 35.20792 ? 131 TRP B CG  1 
ATOM   2316 C CD1 . TRP B 1 131 ? 85.45900  113.75900 118.10300 1.000 35.20792 ? 131 TRP B CD1 1 
ATOM   2317 C CD2 . TRP B 1 131 ? 85.75000  111.68100 118.85700 1.000 35.20792 ? 131 TRP B CD2 1 
ATOM   2318 N NE1 . TRP B 1 131 ? 84.32600  113.40200 118.78200 1.000 35.20792 ? 131 TRP B NE1 1 
ATOM   2319 C CE2 . TRP B 1 131 ? 84.48000  112.12800 119.25800 1.000 35.20792 ? 131 TRP B CE2 1 
ATOM   2320 C CE3 . TRP B 1 131 ? 86.15800  110.39600 119.22000 1.000 35.20792 ? 131 TRP B CE3 1 
ATOM   2321 C CZ2 . TRP B 1 131 ? 83.61200  111.33600 119.99800 1.000 35.20792 ? 131 TRP B CZ2 1 
ATOM   2322 C CZ3 . TRP B 1 131 ? 85.30100  109.61300 119.95600 1.000 35.20792 ? 131 TRP B CZ3 1 
ATOM   2323 C CH2 . TRP B 1 131 ? 84.04000  110.08300 120.33700 1.000 35.20792 ? 131 TRP B CH2 1 
ATOM   2324 N N   . LYS B 1 132 ? 89.31200  111.50900 120.02800 1.000 36.87145 ? 132 LYS B N   1 
ATOM   2325 C CA  . LYS B 1 132 ? 89.16500  110.84200 121.31500 1.000 36.87145 ? 132 LYS B CA  1 
ATOM   2326 C C   . LYS B 1 132 ? 90.01000  111.52400 122.38100 1.000 36.87145 ? 132 LYS B C   1 
ATOM   2327 O O   . LYS B 1 132 ? 89.59800  111.64100 123.53900 1.000 36.87145 ? 132 LYS B O   1 
ATOM   2328 C CB  . LYS B 1 132 ? 89.53700  109.36700 121.19300 1.000 36.87145 ? 132 LYS B CB  1 
ATOM   2329 C CG  . LYS B 1 132 ? 89.17600  108.57700 122.41500 1.000 36.87145 ? 132 LYS B CG  1 
ATOM   2330 C CD  . LYS B 1 132 ? 90.19500  107.49700 122.66400 1.000 36.87145 ? 132 LYS B CD  1 
ATOM   2331 C CE  . LYS B 1 132 ? 89.78700  106.14200 122.15600 1.000 36.87145 ? 132 LYS B CE  1 
ATOM   2332 N NZ  . LYS B 1 132 ? 90.88200  105.14200 122.26500 1.000 36.87145 ? 132 LYS B NZ  1 
ATOM   2333 N N   . CYS B 1 133 ? 91.19400  111.98600 122.00300 1.000 36.01234 ? 133 CYS B N   1 
ATOM   2334 C CA  . CYS B 1 133 ? 92.08600  112.67700 122.91900 1.000 36.01234 ? 133 CYS B CA  1 
ATOM   2335 C C   . CYS B 1 133 ? 91.73100  114.14500 123.09800 1.000 36.01234 ? 133 CYS B C   1 
ATOM   2336 O O   . CYS B 1 133 ? 92.32000  114.79500 123.96600 1.000 36.01234 ? 133 CYS B O   1 
ATOM   2337 C CB  . CYS B 1 133 ? 93.53100  112.54600 122.43400 1.000 36.01234 ? 133 CYS B CB  1 
ATOM   2338 S SG  . CYS B 1 133 ? 94.11800  110.84300 122.30600 1.000 36.01234 ? 133 CYS B SG  1 
ATOM   2339 N N   . ARG B 1 134 ? 90.77700  114.66200 122.31700 1.000 36.38415 ? 134 ARG B N   1 
ATOM   2340 C CA  . ARG B 1 134 ? 90.39100  116.07700 122.31700 1.000 36.38415 ? 134 ARG B CA  1 
ATOM   2341 C C   . ARG B 1 134 ? 91.60200  116.98100 122.10400 1.000 36.38415 ? 134 ARG B C   1 
ATOM   2342 O O   . ARG B 1 134 ? 91.74400  118.02800 122.73200 1.000 36.38415 ? 134 ARG B O   1 
ATOM   2343 C CB  . ARG B 1 134 ? 89.64200  116.45300 123.59700 1.000 36.38415 ? 134 ARG B CB  1 
ATOM   2344 C CG  . ARG B 1 134 ? 88.65800  115.40400 124.07200 1.000 36.38415 ? 134 ARG B CG  1 
ATOM   2345 C CD  . ARG B 1 134 ? 87.22800  115.85800 123.88400 1.000 36.38415 ? 134 ARG B CD  1 
ATOM   2346 N NE  . ARG B 1 134 ? 86.96900  117.14100 124.52800 1.000 36.38415 ? 134 ARG B NE  1 
ATOM   2347 C CZ  . ARG B 1 134 ? 86.68300  117.29100 125.81800 1.000 36.38415 ? 134 ARG B CZ  1 
ATOM   2348 N NH1 . ARG B 1 134 ? 86.61700  116.23300 126.61500 1.000 36.38415 ? 134 ARG B NH1 1 
ATOM   2349 N NH2 . ARG B 1 134 ? 86.46400  118.50100 126.31100 1.000 36.38415 ? 134 ARG B NH2 1 
ATOM   2350 N N   . SER B 1 135 ? 92.47800  116.57000 121.19500 1.000 33.74436 ? 135 SER B N   1 
ATOM   2351 C CA  . SER B 1 135 ? 93.75900  117.22800 121.00400 1.000 33.74436 ? 135 SER B CA  1 
ATOM   2352 C C   . SER B 1 135 ? 94.22600  116.99000 119.57800 1.000 33.74436 ? 135 SER B C   1 
ATOM   2353 O O   . SER B 1 135 ? 93.79400  116.04800 118.91800 1.000 33.74436 ? 135 SER B O   1 
ATOM   2354 C CB  . SER B 1 135 ? 94.79800  116.70900 122.00600 1.000 33.74436 ? 135 SER B CB  1 
ATOM   2355 O OG  . SER B 1 135 ? 96.09500  117.16500 121.68800 1.000 33.74436 ? 135 SER B OG  1 
ATOM   2356 N N   . LYS B 1 136 ? 95.12500  117.85200 119.11500 1.000 36.16170 ? 136 LYS B N   1 
ATOM   2357 C CA  . LYS B 1 136 ? 95.76200  117.69100 117.81800 1.000 36.16170 ? 136 LYS B CA  1 
ATOM   2358 C C   . LYS B 1 136 ? 97.07600  116.93000 117.90700 1.000 36.16170 ? 136 LYS B C   1 
ATOM   2359 O O   . LYS B 1 136 ? 97.70100  116.67400 116.87600 1.000 36.16170 ? 136 LYS B O   1 
ATOM   2360 C CB  . LYS B 1 136 ? 95.99400  119.05600 117.17100 1.000 36.16170 ? 136 LYS B CB  1 
ATOM   2361 C CG  . LYS B 1 136 ? 94.83400  119.54200 116.32000 1.000 36.16170 ? 136 LYS B CG  1 
ATOM   2362 C CD  . LYS B 1 136 ? 94.67500  121.06500 116.32400 1.000 36.16170 ? 136 LYS B CD  1 
ATOM   2363 C CE  . LYS B 1 136 ? 95.89700  121.80100 116.86500 1.000 36.16170 ? 136 LYS B CE  1 
ATOM   2364 N NZ  . LYS B 1 136 ? 95.63500  123.25400 117.04000 1.000 36.16170 ? 136 LYS B NZ  1 
ATOM   2365 N N   . ASN B 1 137 ? 97.50400  116.57100 119.11600 1.000 34.95935 ? 137 ASN B N   1 
ATOM   2366 C CA  . ASN B 1 137 ? 98.77600  115.87700 119.29900 1.000 34.95935 ? 137 ASN B CA  1 
ATOM   2367 C C   . ASN B 1 137 ? 98.90000  114.54200 118.56600 1.000 34.95935 ? 137 ASN B C   1 
ATOM   2368 O O   . ASN B 1 137 ? 100.01400 114.24000 118.10800 1.000 34.95935 ? 137 ASN B O   1 
ATOM   2369 C CB  . ASN B 1 137 ? 99.05000  115.70100 120.79700 1.000 34.95935 ? 137 ASN B CB  1 
ATOM   2370 C CG  . ASN B 1 137 ? 99.55600  116.97000 121.44200 1.000 34.95935 ? 137 ASN B CG  1 
ATOM   2371 O OD1 . ASN B 1 137 ? 99.89300  117.92900 120.75800 1.000 34.95935 ? 137 ASN B OD1 1 
ATOM   2372 N ND2 . ASN B 1 137 ? 99.59900  116.98600 122.76200 1.000 34.95935 ? 137 ASN B ND2 1 
ATOM   2373 N N   . PRO B 1 138 ? 97.86600  113.68900 118.45500 1.000 33.53315 ? 138 PRO B N   1 
ATOM   2374 C CA  . PRO B 1 138 ? 98.03900  112.48000 117.63000 1.000 33.53315 ? 138 PRO B CA  1 
ATOM   2375 C C   . PRO B 1 138 ? 98.38400  112.75700 116.17600 1.000 33.53315 ? 138 PRO B C   1 
ATOM   2376 O O   . PRO B 1 138 ? 99.03400  111.92300 115.54100 1.000 33.53315 ? 138 PRO B O   1 
ATOM   2377 C CB  . PRO B 1 138 ? 96.69100  111.76800 117.77800 1.000 33.53315 ? 138 PRO B CB  1 
ATOM   2378 C CG  . PRO B 1 138 ? 96.21900  112.17900 119.09500 1.000 33.53315 ? 138 PRO B CG  1 
ATOM   2379 C CD  . PRO B 1 138 ? 96.61300  113.60500 119.23100 1.000 33.53315 ? 138 PRO B CD  1 
ATOM   2380 N N   . LEU B 1 139 ? 97.97800  113.90100 115.62600 1.000 35.74063 ? 139 LEU B N   1 
ATOM   2381 C CA  . LEU B 1 139 ? 98.44300  114.26900 114.29300 1.000 35.74063 ? 139 LEU B CA  1 
ATOM   2382 C C   . LEU B 1 139 ? 99.90600  114.68800 114.31300 1.000 35.74063 ? 139 LEU B C   1 
ATOM   2383 O O   . LEU B 1 139 ? 100.65900 114.36500 113.39100 1.000 35.74063 ? 139 LEU B O   1 
ATOM   2384 C CB  . LEU B 1 139 ? 97.58400  115.39000 113.71300 1.000 35.74063 ? 139 LEU B CB  1 
ATOM   2385 C CG  . LEU B 1 139 ? 96.23200  115.00700 113.12500 1.000 35.74063 ? 139 LEU B CG  1 
ATOM   2386 C CD1 . LEU B 1 139 ? 95.59400  116.20200 112.43900 1.000 35.74063 ? 139 LEU B CD1 1 
ATOM   2387 C CD2 . LEU B 1 139 ? 96.36100  113.83100 112.17400 1.000 35.74063 ? 139 LEU B CD2 1 
ATOM   2388 N N   . LEU B 1 140 ? 100.32700 115.40200 115.35300 1.000 36.59278 ? 140 LEU B N   1 
ATOM   2389 C CA  . LEU B 1 140 ? 101.67800 115.94700 115.38900 1.000 36.59278 ? 140 LEU B CA  1 
ATOM   2390 C C   . LEU B 1 140 ? 102.71800 114.88600 115.73100 1.000 36.59278 ? 140 LEU B C   1 
ATOM   2391 O O   . LEU B 1 140 ? 103.85700 114.95600 115.26300 1.000 36.59278 ? 140 LEU B O   1 
ATOM   2392 C CB  . LEU B 1 140 ? 101.74200 117.10000 116.38500 1.000 36.59278 ? 140 LEU B CB  1 
ATOM   2393 C CG  . LEU B 1 140 ? 100.85600 118.28800 116.03200 1.000 36.59278 ? 140 LEU B CG  1 
ATOM   2394 C CD1 . LEU B 1 140 ? 100.88600 119.30300 117.14500 1.000 36.59278 ? 140 LEU B CD1 1 
ATOM   2395 C CD2 . LEU B 1 140 ? 101.30800 118.90800 114.72600 1.000 36.59278 ? 140 LEU B CD2 1 
ATOM   2396 N N   . TYR B 1 141 ? 102.35300 113.90600 116.54600 1.000 33.98897 ? 141 TYR B N   1 
ATOM   2397 C CA  . TYR B 1 141 ? 103.29600 112.91900 117.04700 1.000 33.98897 ? 141 TYR B CA  1 
ATOM   2398 C C   . TYR B 1 141 ? 102.99300 111.53700 116.48800 1.000 33.98897 ? 141 TYR B C   1 
ATOM   2399 O O   . TYR B 1 141 ? 101.83900 111.18600 116.24100 1.000 33.98897 ? 141 TYR B O   1 
ATOM   2400 C CB  . TYR B 1 141 ? 103.27000 112.86300 118.57300 1.000 33.98897 ? 141 TYR B CB  1 
ATOM   2401 C CG  . TYR B 1 141 ? 103.73100 114.12600 119.24500 1.000 33.98897 ? 141 TYR B CG  1 
ATOM   2402 C CD1 . TYR B 1 141 ? 105.07900 114.39600 119.39600 1.000 33.98897 ? 141 TYR B CD1 1 
ATOM   2403 C CD2 . TYR B 1 141 ? 102.81900 115.04100 119.74700 1.000 33.98897 ? 141 TYR B CD2 1 
ATOM   2404 C CE1 . TYR B 1 141 ? 105.50600 115.54100 120.01400 1.000 33.98897 ? 141 TYR B CE1 1 
ATOM   2405 C CE2 . TYR B 1 141 ? 103.23800 116.19000 120.36900 1.000 33.98897 ? 141 TYR B CE2 1 
ATOM   2406 C CZ  . TYR B 1 141 ? 104.58500 116.43300 120.50200 1.000 33.98897 ? 141 TYR B CZ  1 
ATOM   2407 O OH  . TYR B 1 141 ? 105.01600 117.57700 121.12000 1.000 33.98897 ? 141 TYR B OH  1 
ATOM   2408 N N   . ASP B 1 142 ? 104.04700 110.74700 116.31400 1.000 38.88252 ? 142 ASP B N   1 
ATOM   2409 C CA  . ASP B 1 142 ? 103.94300 109.39500 115.78500 1.000 38.88252 ? 142 ASP B CA  1 
ATOM   2410 C C   . ASP B 1 142 ? 103.87100 108.33400 116.87500 1.000 38.88252 ? 142 ASP B C   1 
ATOM   2411 O O   . ASP B 1 142 ? 104.05300 107.15100 116.57500 1.000 38.88252 ? 142 ASP B O   1 
ATOM   2412 C CB  . ASP B 1 142 ? 105.12600 109.09600 114.86200 1.000 38.88252 ? 142 ASP B CB  1 
ATOM   2413 C CG  . ASP B 1 142 ? 105.00700 109.78100 113.51700 1.000 38.88252 ? 142 ASP B CG  1 
ATOM   2414 O OD1 . ASP B 1 142 ? 103.88000 109.87600 112.99200 1.000 38.88252 ? 142 ASP B OD1 1 
ATOM   2415 O OD2 . ASP B 1 142 ? 106.04400 110.21900 112.97900 1.000 38.88252 ? 142 ASP B OD2 1 
ATOM   2416 N N   . ALA B 1 143 ? 103.60100 108.72500 118.11700 1.000 33.48119 ? 143 ALA B N   1 
ATOM   2417 C CA  . ALA B 1 143 ? 103.65400 107.79500 119.23600 1.000 33.48119 ? 143 ALA B CA  1 
ATOM   2418 C C   . ALA B 1 143 ? 102.55600 106.74400 119.14300 1.000 33.48119 ? 143 ALA B C   1 
ATOM   2419 O O   . ALA B 1 143 ? 101.49500 106.96300 118.55800 1.000 33.48119 ? 143 ALA B O   1 
ATOM   2420 C CB  . ALA B 1 143 ? 103.53400 108.54800 120.55700 1.000 33.48119 ? 143 ALA B CB  1 
ATOM   2421 N N   . ASN B 1 144 ? 102.83200 105.58200 119.73000 1.000 34.79581 ? 144 ASN B N   1 
ATOM   2422 C CA  . ASN B 1 144 ? 101.85700 104.50100 119.73200 1.000 34.79581 ? 144 ASN B CA  1 
ATOM   2423 C C   . ASN B 1 144 ? 100.70600 104.78900 120.68500 1.000 34.79581 ? 144 ASN B C   1 
ATOM   2424 O O   . ASN B 1 144 ? 99.58700  104.31700 120.46400 1.000 34.79581 ? 144 ASN B O   1 
ATOM   2425 C CB  . ASN B 1 144 ? 102.53800 103.18500 120.10700 1.000 34.79581 ? 144 ASN B CB  1 
ATOM   2426 C CG  . ASN B 1 144 ? 103.50400 102.70100 119.04600 1.000 34.79581 ? 144 ASN B CG  1 
ATOM   2427 O OD1 . ASN B 1 144 ? 104.68800 102.51200 119.31100 1.000 34.79581 ? 144 ASN B OD1 1 
ATOM   2428 N ND2 . ASN B 1 144 ? 103.00400 102.50700 117.83400 1.000 34.79581 ? 144 ASN B ND2 1 
ATOM   2429 N N   . TYR B 1 145 ? 100.95700 105.55100 121.74500 1.000 29.54588 ? 145 TYR B N   1 
ATOM   2430 C CA  . TYR B 1 145 ? 99.96200  105.79600 122.77500 1.000 29.54588 ? 145 TYR B CA  1 
ATOM   2431 C C   . TYR B 1 145 ? 99.99300  107.26100 123.16700 1.000 29.54588 ? 145 TYR B C   1 
ATOM   2432 O O   . TYR B 1 145 ? 100.96700 107.97300 122.92500 1.000 29.54588 ? 145 TYR B O   1 
ATOM   2433 C CB  . TYR B 1 145 ? 100.19700 104.91700 124.00900 1.000 29.54588 ? 145 TYR B CB  1 
ATOM   2434 C CG  . TYR B 1 145 ? 100.07300 103.44600 123.72300 1.000 29.54588 ? 145 TYR B CG  1 
ATOM   2435 C CD1 . TYR B 1 145 ? 101.16500 102.70900 123.29900 1.000 29.54588 ? 145 TYR B CD1 1 
ATOM   2436 C CD2 . TYR B 1 145 ? 98.86300  102.79700 123.86500 1.000 29.54588 ? 145 TYR B CD2 1 
ATOM   2437 C CE1 . TYR B 1 145 ? 101.05300 101.37200 123.01900 1.000 29.54588 ? 145 TYR B CE1 1 
ATOM   2438 C CE2 . TYR B 1 145 ? 98.74400  101.46000 123.59300 1.000 29.54588 ? 145 TYR B CE2 1 
ATOM   2439 C CZ  . TYR B 1 145 ? 99.84000  100.75000 123.17200 1.000 29.54588 ? 145 TYR B CZ  1 
ATOM   2440 O OH  . TYR B 1 145 ? 99.71400  99.41200  122.90500 1.000 29.54588 ? 145 TYR B OH  1 
ATOM   2441 N N   . PHE B 1 146 ? 98.90700  107.70500 123.78600 1.000 27.37880 ? 146 PHE B N   1 
ATOM   2442 C CA  . PHE B 1 146 ? 98.82400  109.06600 124.29500 1.000 27.37880 ? 146 PHE B CA  1 
ATOM   2443 C C   . PHE B 1 146 ? 98.19400  109.03800 125.67500 1.000 27.37880 ? 146 PHE B C   1 
ATOM   2444 O O   . PHE B 1 146 ? 97.09500  108.51000 125.84600 1.000 27.37880 ? 146 PHE B O   1 
ATOM   2445 C CB  . PHE B 1 146 ? 98.03200  109.96000 123.33700 1.000 27.37880 ? 146 PHE B CB  1 
ATOM   2446 C CG  . PHE B 1 146 ? 98.77300  110.27100 122.07500 1.000 27.37880 ? 146 PHE B CG  1 
ATOM   2447 C CD1 . PHE B 1 146 ? 99.62800  111.35300 122.01300 1.000 27.37880 ? 146 PHE B CD1 1 
ATOM   2448 C CD2 . PHE B 1 146 ? 98.65400  109.45300 120.96500 1.000 27.37880 ? 146 PHE B CD2 1 
ATOM   2449 C CE1 . PHE B 1 146 ? 100.32600 111.63100 120.86700 1.000 27.37880 ? 146 PHE B CE1 1 
ATOM   2450 C CE2 . PHE B 1 146 ? 99.35700  109.72300 119.82100 1.000 27.37880 ? 146 PHE B CE2 1 
ATOM   2451 C CZ  . PHE B 1 146 ? 100.19800 110.81100 119.77300 1.000 27.37880 ? 146 PHE B CZ  1 
ATOM   2452 N N   . LEU B 1 147 ? 98.90600  109.57600 126.65700 1.000 26.15354 ? 147 LEU B N   1 
ATOM   2453 C CA  . LEU B 1 147 ? 98.37500  109.70600 128.00300 1.000 26.15354 ? 147 LEU B CA  1 
ATOM   2454 C C   . LEU B 1 147 ? 97.58200  110.99800 128.10100 1.000 26.15354 ? 147 LEU B C   1 
ATOM   2455 O O   . LEU B 1 147 ? 98.11100  112.07900 127.84100 1.000 26.15354 ? 147 LEU B O   1 
ATOM   2456 C CB  . LEU B 1 147 ? 99.48900  109.68900 129.04500 1.000 26.15354 ? 147 LEU B CB  1 
ATOM   2457 C CG  . LEU B 1 147 ? 98.81600  109.59800 130.41500 1.000 26.15354 ? 147 LEU B CG  1 
ATOM   2458 C CD1 . LEU B 1 147 ? 98.37600  108.17700 130.70200 1.000 26.15354 ? 147 LEU B CD1 1 
ATOM   2459 C CD2 . LEU B 1 147 ? 99.66200  110.14600 131.52000 1.000 26.15354 ? 147 LEU B CD2 1 
ATOM   2460 N N   . CYS B 1 148 ? 96.32600  110.88500 128.49400 1.000 28.64157 ? 148 CYS B N   1 
ATOM   2461 C CA  . CYS B 1 148 ? 95.37600  111.97100 128.40500 1.000 28.64157 ? 148 CYS B CA  1 
ATOM   2462 C C   . CYS B 1 148 ? 94.63900  112.12200 129.72100 1.000 28.64157 ? 148 CYS B C   1 
ATOM   2463 O O   . CYS B 1 148 ? 94.40300  111.14700 130.44200 1.000 28.64157 ? 148 CYS B O   1 
ATOM   2464 C CB  . CYS B 1 148 ? 94.36900  111.72800 127.27900 1.000 28.64157 ? 148 CYS B CB  1 
ATOM   2465 S SG  . CYS B 1 148 ? 95.12600  111.39800 125.68500 1.000 28.64157 ? 148 CYS B SG  1 
ATOM   2466 N N   . TRP B 1 149 ? 94.29600  113.36500 130.02800 1.000 26.36151 ? 149 TRP B N   1 
ATOM   2467 C CA  . TRP B 1 149 ? 93.30500  113.60400 131.06800 1.000 26.36151 ? 149 TRP B CA  1 
ATOM   2468 C C   . TRP B 1 149 ? 92.62500  114.93600 130.81300 1.000 26.36151 ? 149 TRP B C   1 
ATOM   2469 O O   . TRP B 1 149 ? 93.16300  115.80900 130.13300 1.000 26.36151 ? 149 TRP B O   1 
ATOM   2470 C CB  . TRP B 1 149 ? 93.90100  113.54200 132.48500 1.000 26.36151 ? 149 TRP B CB  1 
ATOM   2471 C CG  . TRP B 1 149 ? 94.74800  114.69500 132.91900 1.000 26.36151 ? 149 TRP B CG  1 
ATOM   2472 C CD1 . TRP B 1 149 ? 94.35300  115.76500 133.65700 1.000 26.36151 ? 149 TRP B CD1 1 
ATOM   2473 C CD2 . TRP B 1 149 ? 96.14800  114.86700 132.68200 1.000 26.36151 ? 149 TRP B CD2 1 
ATOM   2474 N NE1 . TRP B 1 149 ? 95.41000  116.60300 133.88000 1.000 26.36151 ? 149 TRP B NE1 1 
ATOM   2475 C CE2 . TRP B 1 149 ? 96.52700  116.07400 133.29400 1.000 26.36151 ? 149 TRP B CE2 1 
ATOM   2476 C CE3 . TRP B 1 149 ? 97.11600  114.12000 132.00800 1.000 26.36151 ? 149 TRP B CE3 1 
ATOM   2477 C CZ2 . TRP B 1 149 ? 97.83100  116.55500 133.24900 1.000 26.36151 ? 149 TRP B CZ2 1 
ATOM   2478 C CZ3 . TRP B 1 149 ? 98.40500  114.59700 131.96400 1.000 26.36151 ? 149 TRP B CZ3 1 
ATOM   2479 C CH2 . TRP B 1 149 ? 98.75300  115.80400 132.57900 1.000 26.36151 ? 149 TRP B CH2 1 
ATOM   2480 N N   . HIS B 1 150 ? 91.42800  115.07500 131.36400 1.000 31.12612 ? 150 HIS B N   1 
ATOM   2481 C CA  . HIS B 1 150 ? 90.55800  116.19900 131.07100 1.000 31.12612 ? 150 HIS B CA  1 
ATOM   2482 C C   . HIS B 1 150 ? 90.45700  117.12100 132.27600 1.000 31.12612 ? 150 HIS B C   1 
ATOM   2483 O O   . HIS B 1 150 ? 90.18100  116.67100 133.39000 1.000 31.12612 ? 150 HIS B O   1 
ATOM   2484 C CB  . HIS B 1 150 ? 89.16500  115.71500 130.67300 1.000 31.12612 ? 150 HIS B CB  1 
ATOM   2485 C CG  . HIS B 1 150 ? 88.13600  116.79900 130.65900 1.000 31.12612 ? 150 HIS B CG  1 
ATOM   2486 N ND1 . HIS B 1 150 ? 87.96700  117.64700 129.58700 1.000 31.12612 ? 150 HIS B ND1 1 
ATOM   2487 C CD2 . HIS B 1 150 ? 87.23400  117.18500 131.59100 1.000 31.12612 ? 150 HIS B CD2 1 
ATOM   2488 C CE1 . HIS B 1 150 ? 86.99700  118.50100 129.85500 1.000 31.12612 ? 150 HIS B CE1 1 
ATOM   2489 N NE2 . HIS B 1 150 ? 86.53900  118.24500 131.06600 1.000 31.12612 ? 150 HIS B NE2 1 
ATOM   2490 N N   . THR B 1 151 ? 90.67500  118.40600 132.04500 1.000 34.10876 ? 151 THR B N   1 
ATOM   2491 C CA  . THR B 1 151 ? 90.32300  119.44900 132.99100 1.000 34.10876 ? 151 THR B CA  1 
ATOM   2492 C C   . THR B 1 151 ? 89.36200  120.40900 132.30600 1.000 34.10876 ? 151 THR B C   1 
ATOM   2493 O O   . THR B 1 151 ? 89.14600  120.34000 131.09500 1.000 34.10876 ? 151 THR B O   1 
ATOM   2494 C CB  . THR B 1 151 ? 91.56500  120.18400 133.51000 1.000 34.10876 ? 151 THR B CB  1 
ATOM   2495 O OG1 . THR B 1 151 ? 92.31200  120.71300 132.41000 1.000 34.10876 ? 151 THR B OG1 1 
ATOM   2496 C CG2 . THR B 1 151 ? 92.44500  119.23500 134.29600 1.000 34.10876 ? 151 THR B CG2 1 
ATOM   2497 N N   . ASN B 1 152 ? 88.77000  121.30300 133.09900 1.000 39.36257 ? 152 ASN B N   1 
ATOM   2498 C CA  . ASN B 1 152 ? 87.77500  122.22900 132.56400 1.000 39.36257 ? 152 ASN B CA  1 
ATOM   2499 C C   . ASN B 1 152 ? 88.36100  123.17200 131.52100 1.000 39.36257 ? 152 ASN B C   1 
ATOM   2500 O O   . ASN B 1 152 ? 87.66300  123.55700 130.57900 1.000 39.36257 ? 152 ASN B O   1 
ATOM   2501 C CB  . ASN B 1 152 ? 87.14100  123.03600 133.69200 1.000 39.36257 ? 152 ASN B CB  1 
ATOM   2502 C CG  . ASN B 1 152 ? 86.43400  122.16900 134.69900 1.000 39.36257 ? 152 ASN B CG  1 
ATOM   2503 O OD1 . ASN B 1 152 ? 85.91000  121.10900 134.36300 1.000 39.36257 ? 152 ASN B OD1 1 
ATOM   2504 N ND2 . ASN B 1 152 ? 86.40700  122.61600 135.94700 1.000 39.36257 ? 152 ASN B ND2 1 
ATOM   2505 N N   . CYS B 1 153 ? 89.62600  123.55800 131.66300 1.000 40.77063 ? 153 CYS B N   1 
ATOM   2506 C CA  . CYS B 1 153 ? 90.22800  124.52200 130.75600 1.000 40.77063 ? 153 CYS B CA  1 
ATOM   2507 C C   . CYS B 1 153 ? 91.17800  123.89500 129.74800 1.000 40.77063 ? 153 CYS B C   1 
ATOM   2508 O O   . CYS B 1 153 ? 91.58300  124.57500 128.80100 1.000 40.77063 ? 153 CYS B O   1 
ATOM   2509 C CB  . CYS B 1 153 ? 90.96500  125.61200 131.54500 1.000 40.77063 ? 153 CYS B CB  1 
ATOM   2510 S SG  . CYS B 1 153 ? 92.38600  125.04400 132.49000 1.000 40.77063 ? 153 CYS B SG  1 
ATOM   2511 N N   . TYR B 1 154 ? 91.54700  122.62900 129.91400 1.000 34.15615 ? 154 TYR B N   1 
ATOM   2512 C CA  . TYR B 1 154 ? 92.51000  122.02900 129.00500 1.000 34.15615 ? 154 TYR B CA  1 
ATOM   2513 C C   . TYR B 1 154 ? 92.32900  120.52000 128.97400 1.000 34.15615 ? 154 TYR B C   1 
ATOM   2514 O O   . TYR B 1 154 ? 91.92000  119.90900 129.96100 1.000 34.15615 ? 154 TYR B O   1 
ATOM   2515 C CB  . TYR B 1 154 ? 93.94500  122.37900 129.40600 1.000 34.15615 ? 154 TYR B CB  1 
ATOM   2516 C CG  . TYR B 1 154 ? 94.93600  122.15700 128.29900 1.000 34.15615 ? 154 TYR B CG  1 
ATOM   2517 C CD1 . TYR B 1 154 ? 95.78800  121.06500 128.31600 1.000 34.15615 ? 154 TYR B CD1 1 
ATOM   2518 C CD2 . TYR B 1 154 ? 95.01300  123.03500 127.22700 1.000 34.15615 ? 154 TYR B CD2 1 
ATOM   2519 C CE1 . TYR B 1 154 ? 96.68900  120.85600 127.30200 1.000 34.15615 ? 154 TYR B CE1 1 
ATOM   2520 C CE2 . TYR B 1 154 ? 95.91000  122.83500 126.20700 1.000 34.15615 ? 154 TYR B CE2 1 
ATOM   2521 C CZ  . TYR B 1 154 ? 96.74500  121.74400 126.24800 1.000 34.15615 ? 154 TYR B CZ  1 
ATOM   2522 O OH  . TYR B 1 154 ? 97.64200  121.53900 125.23200 1.000 34.15615 ? 154 TYR B OH  1 
ATOM   2523 N N   . ASP B 1 155 ? 92.64700  119.93000 127.82700 1.000 33.15033 ? 155 ASP B N   1 
ATOM   2524 C CA  . ASP B 1 155 ? 92.69700  118.48300 127.66300 1.000 33.15033 ? 155 ASP B CA  1 
ATOM   2525 C C   . ASP B 1 155 ? 94.13800  118.09200 127.36700 1.000 33.15033 ? 155 ASP B C   1 
ATOM   2526 O O   . ASP B 1 155 ? 94.68500  118.46500 126.32600 1.000 33.15033 ? 155 ASP B O   1 
ATOM   2527 C CB  . ASP B 1 155 ? 91.75100  118.02200 126.55700 1.000 33.15033 ? 155 ASP B CB  1 
ATOM   2528 C CG  . ASP B 1 155 ? 90.30000  118.08100 126.97900 1.000 33.15033 ? 155 ASP B CG  1 
ATOM   2529 O OD1 . ASP B 1 155 ? 89.52300  118.82500 126.35600 1.000 33.15033 ? 155 ASP B OD1 1 
ATOM   2530 O OD2 . ASP B 1 155 ? 89.94000  117.39600 127.95200 1.000 33.15033 ? 155 ASP B OD2 1 
ATOM   2531 N N   . TYR B 1 156 ? 94.75100  117.35100 128.28100 1.000 29.07736 ? 156 TYR B N   1 
ATOM   2532 C CA  . TYR B 1 156 ? 96.15200  116.98500 128.15500 1.000 29.07736 ? 156 TYR B CA  1 
ATOM   2533 C C   . TYR B 1 156 ? 96.29600  115.68300 127.39100 1.000 29.07736 ? 156 TYR B C   1 
ATOM   2534 O O   . TYR B 1 156 ? 95.56600  114.71900 127.64300 1.000 29.07736 ? 156 TYR B O   1 
ATOM   2535 C CB  . TYR B 1 156 ? 96.79500  116.84200 129.53100 1.000 29.07736 ? 156 TYR B CB  1 
ATOM   2536 C CG  . TYR B 1 156 ? 96.87600  118.12800 130.29700 1.000 29.07736 ? 156 TYR B CG  1 
ATOM   2537 C CD1 . TYR B 1 156 ? 95.84700  118.52400 131.13300 1.000 29.07736 ? 156 TYR B CD1 1 
ATOM   2538 C CD2 . TYR B 1 156 ? 97.97900  118.95300 130.17900 1.000 29.07736 ? 156 TYR B CD2 1 
ATOM   2539 C CE1 . TYR B 1 156 ? 95.92100  119.69700 131.83500 1.000 29.07736 ? 156 TYR B CE1 1 
ATOM   2540 C CE2 . TYR B 1 156 ? 98.06000  120.13100 130.87000 1.000 29.07736 ? 156 TYR B CE2 1 
ATOM   2541 C CZ  . TYR B 1 156 ? 97.02700  120.49800 131.69500 1.000 29.07736 ? 156 TYR B CZ  1 
ATOM   2542 O OH  . TYR B 1 156 ? 97.10000  121.66900 132.39100 1.000 29.07736 ? 156 TYR B OH  1 
ATOM   2543 N N   . CYS B 1 157 ? 97.28200  115.65500 126.49100 1.000 29.96542 ? 157 CYS B N   1 
ATOM   2544 C CA  . CYS B 1 157 ? 97.53200  114.52300 125.60200 1.000 29.96542 ? 157 CYS B CA  1 
ATOM   2545 C C   . CYS B 1 157 ? 99.03500  114.48100 125.33400 1.000 29.96542 ? 157 CYS B C   1 
ATOM   2546 O O   . CYS B 1 157 ? 99.55000  115.27800 124.54700 1.000 29.96542 ? 157 CYS B O   1 
ATOM   2547 C CB  . CYS B 1 157 ? 96.72700  114.66400 124.31700 1.000 29.96542 ? 157 CYS B CB  1 
ATOM   2548 S SG  . CYS B 1 157 ? 97.00900  113.41200 123.06900 1.000 29.96542 ? 157 CYS B SG  1 
ATOM   2549 N N   . ILE B 1 158 ? 99.72800  113.55400 125.98600 1.000 26.15336 ? 158 ILE B N   1 
ATOM   2550 C CA  . ILE B 1 158 ? 101.18300 113.48100 125.97400 1.000 26.15336 ? 158 ILE B CA  1 
ATOM   2551 C C   . ILE B 1 158 ? 101.58400 112.18900 125.27600 1.000 26.15336 ? 158 ILE B C   1 
ATOM   2552 O O   . ILE B 1 158 ? 101.04000 111.13500 125.59800 1.000 26.15336 ? 158 ILE B O   1 
ATOM   2553 C CB  . ILE B 1 158 ? 101.78000 113.53300 127.39200 1.000 26.15336 ? 158 ILE B CB  1 
ATOM   2554 C CG1 . ILE B 1 158 ? 101.34800 114.81700 128.09800 1.000 26.15336 ? 158 ILE B CG1 1 
ATOM   2555 C CG2 . ILE B 1 158 ? 103.29600 113.41300 127.36100 1.000 26.15336 ? 158 ILE B CG2 1 
ATOM   2556 C CD1 . ILE B 1 158 ? 101.78000 114.89700 129.53300 1.000 26.15336 ? 158 ILE B CD1 1 
ATOM   2557 N N   . PRO B 1 159 ? 102.51000 112.22200 124.31700 1.000 25.45506 ? 159 PRO B N   1 
ATOM   2558 C CA  . PRO B 1 159 ? 102.94900 110.98200 123.66200 1.000 25.45506 ? 159 PRO B CA  1 
ATOM   2559 C C   . PRO B 1 159 ? 103.58000 109.99800 124.63900 1.000 25.45506 ? 159 PRO B C   1 
ATOM   2560 O O   . PRO B 1 159 ? 104.26200 110.38300 125.58900 1.000 25.45506 ? 159 PRO B O   1 
ATOM   2561 C CB  . PRO B 1 159 ? 103.97600 111.47100 122.63400 1.000 25.45506 ? 159 PRO B CB  1 
ATOM   2562 C CG  . PRO B 1 159 ? 103.73700 112.90100 122.48400 1.000 25.45506 ? 159 PRO B CG  1 
ATOM   2563 C CD  . PRO B 1 159 ? 103.15300 113.41200 123.73900 1.000 25.45506 ? 159 PRO B CD  1 
ATOM   2564 N N   . TYR B 1 160 ? 103.35000 108.71200 124.38600 1.000 24.06599 ? 160 TYR B N   1 
ATOM   2565 C CA  . TYR B 1 160 ? 103.85200 107.64100 125.23200 1.000 24.06599 ? 160 TYR B CA  1 
ATOM   2566 C C   . TYR B 1 160 ? 104.01400 106.38800 124.38100 1.000 24.06599 ? 160 TYR B C   1 
ATOM   2567 O O   . TYR B 1 160 ? 103.26700 106.17400 123.42500 1.000 24.06599 ? 160 TYR B O   1 
ATOM   2568 C CB  . TYR B 1 160 ? 102.90800 107.38900 126.41200 1.000 24.06599 ? 160 TYR B CB  1 
ATOM   2569 C CG  . TYR B 1 160 ? 103.54900 106.73700 127.61100 1.000 24.06599 ? 160 TYR B CG  1 
ATOM   2570 C CD1 . TYR B 1 160 ? 103.23400 105.43700 127.96300 1.000 24.06599 ? 160 TYR B CD1 1 
ATOM   2571 C CD2 . TYR B 1 160 ? 104.45400 107.42600 128.40400 1.000 24.06599 ? 160 TYR B CD2 1 
ATOM   2572 C CE1 . TYR B 1 160 ? 103.80600 104.83700 129.05800 1.000 24.06599 ? 160 TYR B CE1 1 
ATOM   2573 C CE2 . TYR B 1 160 ? 105.02700 106.83000 129.50400 1.000 24.06599 ? 160 TYR B CE2 1 
ATOM   2574 C CZ  . TYR B 1 160 ? 104.69900 105.53500 129.82500 1.000 24.06599 ? 160 TYR B CZ  1 
ATOM   2575 O OH  . TYR B 1 160 ? 105.26600 104.92900 130.91400 1.000 24.06599 ? 160 TYR B OH  1 
ATOM   2576 N N   . ASN B 1 161 ? 104.98600 105.55100 124.74300 1.000 27.72217 ? 161 ASN B N   1 
ATOM   2577 C CA  . ASN B 1 161 ? 105.42400 104.49800 123.83400 1.000 27.72217 ? 161 ASN B CA  1 
ATOM   2578 C C   . ASN B 1 161 ? 104.68800 103.17200 124.00400 1.000 27.72217 ? 161 ASN B C   1 
ATOM   2579 O O   . ASN B 1 161 ? 104.40200 102.50700 123.00500 1.000 27.72217 ? 161 ASN B O   1 
ATOM   2580 C CB  . ASN B 1 161 ? 106.92800 104.26200 123.97800 1.000 27.72217 ? 161 ASN B CB  1 
ATOM   2581 C CG  . ASN B 1 161 ? 107.45600 103.27000 122.96100 1.000 27.72217 ? 161 ASN B CG  1 
ATOM   2582 O OD1 . ASN B 1 161 ? 107.44100 103.53200 121.76300 1.000 27.72217 ? 161 ASN B OD1 1 
ATOM   2583 N ND2 . ASN B 1 161 ? 107.91200 102.12200 123.43400 1.000 27.72217 ? 161 ASN B ND2 1 
ATOM   2584 N N   . SER B 1 162 ? 104.38500 102.74600 125.22600 1.000 27.82860 ? 162 SER B N   1 
ATOM   2585 C CA  . SER B 1 162 ? 103.79600 101.42800 125.41800 1.000 27.82860 ? 162 SER B CA  1 
ATOM   2586 C C   . SER B 1 162 ? 102.93200 101.42600 126.66900 1.000 27.82860 ? 162 SER B C   1 
ATOM   2587 O O   . SER B 1 162 ? 102.96900 102.35300 127.47400 1.000 27.82860 ? 162 SER B O   1 
ATOM   2588 C CB  . SER B 1 162 ? 104.87400 100.33900 125.50400 1.000 27.82860 ? 162 SER B CB  1 
ATOM   2589 O OG  . SER B 1 162 ? 105.72900 100.53800 126.61100 1.000 27.82860 ? 162 SER B OG  1 
ATOM   2590 N N   . VAL B 1 163 ? 102.14500 100.36400 126.82600 1.000 28.18635 ? 163 VAL B N   1 
ATOM   2591 C CA  . VAL B 1 163 ? 101.30800 100.19300 128.01200 1.000 28.18635 ? 163 VAL B CA  1 
ATOM   2592 C C   . VAL B 1 163 ? 102.20200 99.65600  129.12500 1.000 28.18635 ? 163 VAL B C   1 
ATOM   2593 O O   . VAL B 1 163 ? 102.59700 98.49200  129.11300 1.000 28.18635 ? 163 VAL B O   1 
ATOM   2594 C CB  . VAL B 1 163 ? 100.12000 99.26600  127.75100 1.000 28.18635 ? 163 VAL B CB  1 
ATOM   2595 C CG1 . VAL B 1 163 ? 99.24200  99.18200  128.97900 1.000 28.18635 ? 163 VAL B CG1 1 
ATOM   2596 C CG2 . VAL B 1 163 ? 99.32400  99.74600  126.57200 1.000 28.18635 ? 163 VAL B CG2 1 
ATOM   2597 N N   . THR B 1 164 ? 102.52000 100.50300 130.09100 1.000 27.78806 ? 164 THR B N   1 
ATOM   2598 C CA  . THR B 1 164 ? 103.31300 100.11200 131.24400 1.000 27.78806 ? 164 THR B CA  1 
ATOM   2599 C C   . THR B 1 164 ? 102.40300 99.92700  132.45000 1.000 27.78806 ? 164 THR B C   1 
ATOM   2600 O O   . THR B 1 164 ? 101.24100 100.33200 132.44700 1.000 27.78806 ? 164 THR B O   1 
ATOM   2601 C CB  . THR B 1 164 ? 104.39500 101.15400 131.54100 1.000 27.78806 ? 164 THR B CB  1 
ATOM   2602 O OG1 . THR B 1 164 ? 103.79100 102.44300 131.68600 1.000 27.78806 ? 164 THR B OG1 1 
ATOM   2603 C CG2 . THR B 1 164 ? 105.40400 101.20900 130.41000 1.000 27.78806 ? 164 THR B CG2 1 
ATOM   2604 N N   . SER B 1 165 ? 102.94100 99.28400  133.48500 1.000 28.50095 ? 165 SER B N   1 
ATOM   2605 C CA  . SER B 1 165 ? 102.14800 99.06900  134.69000 1.000 28.50095 ? 165 SER B CA  1 
ATOM   2606 C C   . SER B 1 165 ? 102.08200 100.32700 135.54500 1.000 28.50095 ? 165 SER B C   1 
ATOM   2607 O O   . SER B 1 165 ? 101.21600 100.44100 136.41600 1.000 28.50095 ? 165 SER B O   1 
ATOM   2608 C CB  . SER B 1 165 ? 102.71300 97.89900  135.49200 1.000 28.50095 ? 165 SER B CB  1 
ATOM   2609 O OG  . SER B 1 165 ? 103.96200 98.22000  136.06700 1.000 28.50095 ? 165 SER B OG  1 
ATOM   2610 N N   . SER B 1 166 ? 102.97800 101.27400 135.30900 1.000 27.33530 ? 166 SER B N   1 
ATOM   2611 C CA  . SER B 1 166 ? 102.98700 102.54100 136.01400 1.000 27.33530 ? 166 SER B CA  1 
ATOM   2612 C C   . SER B 1 166 ? 103.36200 103.64200 135.03900 1.000 27.33530 ? 166 SER B C   1 
ATOM   2613 O O   . SER B 1 166 ? 103.96900 103.39900 133.99700 1.000 27.33530 ? 166 SER B O   1 
ATOM   2614 C CB  . SER B 1 166 ? 103.96100 102.52900 137.19700 1.000 27.33530 ? 166 SER B CB  1 
ATOM   2615 O OG  . SER B 1 166 ? 105.30000 102.50400 136.75100 1.000 27.33530 ? 166 SER B OG  1 
ATOM   2616 N N   . ILE B 1 167 ? 102.97200 104.86200 135.38700 1.000 24.80693 ? 167 ILE B N   1 
ATOM   2617 C CA  . ILE B 1 167 ? 103.31000 106.04800 134.61100 1.000 24.80693 ? 167 ILE B CA  1 
ATOM   2618 C C   . ILE B 1 167 ? 103.70800 107.15000 135.58100 1.000 24.80693 ? 167 ILE B C   1 
ATOM   2619 O O   . ILE B 1 167 ? 103.03500 107.36700 136.59000 1.000 24.80693 ? 167 ILE B O   1 
ATOM   2620 C CB  . ILE B 1 167 ? 102.14000 106.48400 133.70100 1.000 24.80693 ? 167 ILE B CB  1 
ATOM   2621 C CG1 . ILE B 1 167 ? 102.05600 105.55900 132.48500 1.000 24.80693 ? 167 ILE B CG1 1 
ATOM   2622 C CG2 . ILE B 1 167 ? 102.29200 107.92800 133.24800 1.000 24.80693 ? 167 ILE B CG2 1 
ATOM   2623 C CD1 . ILE B 1 167 ? 100.82100 105.69900 131.68200 1.000 24.80693 ? 167 ILE B CD1 1 
ATOM   2624 N N   . VAL B 1 168 ? 104.80500 107.83700 135.29300 1.000 23.34756 ? 168 VAL B N   1 
ATOM   2625 C CA  . VAL B 1 168 ? 105.25100 108.95900 136.10500 1.000 23.34756 ? 168 VAL B CA  1 
ATOM   2626 C C   . VAL B 1 168 ? 105.06500 110.23200 135.29900 1.000 23.34756 ? 168 VAL B C   1 
ATOM   2627 O O   . VAL B 1 168 ? 105.59400 110.35700 134.19000 1.000 23.34756 ? 168 VAL B O   1 
ATOM   2628 C CB  . VAL B 1 168 ? 106.70900 108.80200 136.55800 1.000 23.34756 ? 168 VAL B CB  1 
ATOM   2629 C CG1 . VAL B 1 168 ? 107.12500 109.99100 137.40300 1.000 23.34756 ? 168 VAL B CG1 1 
ATOM   2630 C CG2 . VAL B 1 168 ? 106.86900 107.52900 137.33100 1.000 23.34756 ? 168 VAL B CG2 1 
ATOM   2631 N N   . ILE B 1 169 ? 104.31200 111.17000 135.85400 1.000 24.01820 ? 169 ILE B N   1 
ATOM   2632 C CA  . ILE B 1 169 ? 104.18200 112.50500 135.29500 1.000 24.01820 ? 169 ILE B CA  1 
ATOM   2633 C C   . ILE B 1 169 ? 105.03400 113.43500 136.14200 1.000 24.01820 ? 169 ILE B C   1 
ATOM   2634 O O   . ILE B 1 169 ? 104.86700 113.50400 137.36300 1.000 24.01820 ? 169 ILE B O   1 
ATOM   2635 C CB  . ILE B 1 169 ? 102.71700 112.96300 135.25600 1.000 24.01820 ? 169 ILE B CB  1 
ATOM   2636 C CG1 . ILE B 1 169 ? 101.86500 111.94600 134.49500 1.000 24.01820 ? 169 ILE B CG1 1 
ATOM   2637 C CG2 . ILE B 1 169 ? 102.60600 114.33700 134.61900 1.000 24.01820 ? 169 ILE B CG2 1 
ATOM   2638 C CD1 . ILE B 1 169 ? 100.40500 112.27600 134.46100 1.000 24.01820 ? 169 ILE B CD1 1 
ATOM   2639 N N   . THR B 1 170 ? 105.95700 114.14000 135.50600 1.000 26.61166 ? 170 THR B N   1 
ATOM   2640 C CA  . THR B 1 170 ? 106.81200 115.09900 136.18100 1.000 26.61166 ? 170 THR B CA  1 
ATOM   2641 C C   . THR B 1 170 ? 106.21100 116.48600 136.01000 1.000 26.61166 ? 170 THR B C   1 
ATOM   2642 O O   . THR B 1 170 ? 105.82600 116.86200 134.90500 1.000 26.61166 ? 170 THR B O   1 
ATOM   2643 C CB  . THR B 1 170 ? 108.22700 115.04400 135.60400 1.000 26.61166 ? 170 THR B CB  1 
ATOM   2644 O OG1 . THR B 1 170 ? 108.77300 113.73700 135.80300 1.000 26.61166 ? 170 THR B OG1 1 
ATOM   2645 C CG2 . THR B 1 170 ? 109.11400 116.05500 136.25600 1.000 26.61166 ? 170 THR B CG2 1 
ATOM   2646 N N   . SER B 1 171 ? 106.11400 117.23700 137.09800 1.000 32.33071 ? 171 SER B N   1 
ATOM   2647 C CA  . SER B 1 171 ? 105.57000 118.58800 137.04900 1.000 32.33071 ? 171 SER B CA  1 
ATOM   2648 C C   . SER B 1 171 ? 106.63800 119.55400 137.53600 1.000 32.33071 ? 171 SER B C   1 
ATOM   2649 O O   . SER B 1 171 ? 107.11800 119.43800 138.66700 1.000 32.33071 ? 171 SER B O   1 
ATOM   2650 C CB  . SER B 1 171 ? 104.29900 118.70500 137.88500 1.000 32.33071 ? 171 SER B CB  1 
ATOM   2651 O OG  . SER B 1 171 ? 103.87500 120.05200 137.96400 1.000 32.33071 ? 171 SER B OG  1 
ATOM   2652 N N   . GLY B 1 172 ? 107.00700 120.50100 136.68400 1.000 40.47479 ? 172 GLY B N   1 
ATOM   2653 C CA  . GLY B 1 172 ? 107.93200 121.55800 137.05300 1.000 40.47479 ? 172 GLY B CA  1 
ATOM   2654 C C   . GLY B 1 172 ? 107.20600 122.89100 137.11100 1.000 40.47479 ? 172 GLY B C   1 
ATOM   2655 O O   . GLY B 1 172 ? 106.37700 123.19300 136.25400 1.000 40.47479 ? 172 GLY B O   1 
ATOM   2656 N N   . ASP B 1 173 ? 107.51800 123.68100 138.13400 1.000 46.23732 ? 173 ASP B N   1 
ATOM   2657 C CA  . ASP B 1 173 ? 106.86900 124.97300 138.31500 1.000 46.23732 ? 173 ASP B CA  1 
ATOM   2658 C C   . ASP B 1 173 ? 107.60700 126.04400 137.51100 1.000 46.23732 ? 173 ASP B C   1 
ATOM   2659 O O   . ASP B 1 173 ? 108.46700 125.75200 136.67600 1.000 46.23732 ? 173 ASP B O   1 
ATOM   2660 C CB  . ASP B 1 173 ? 106.76900 125.31200 139.80200 1.000 46.23732 ? 173 ASP B CB  1 
ATOM   2661 C CG  . ASP B 1 173 ? 108.10100 125.21100 140.52900 1.000 46.23732 ? 173 ASP B CG  1 
ATOM   2662 O OD1 . ASP B 1 173 ? 108.08600 125.11800 141.77300 1.000 46.23732 ? 173 ASP B OD1 1 
ATOM   2663 O OD2 . ASP B 1 173 ? 109.15900 125.23300 139.87200 1.000 46.23732 ? 173 ASP B OD2 1 
ATOM   2664 N N   . GLY B 1 174 ? 107.27500 127.30500 137.75800 1.000 50.03450 ? 174 GLY B N   1 
ATOM   2665 C CA  . GLY B 1 174 ? 107.94900 128.40900 137.10000 1.000 50.03450 ? 174 GLY B CA  1 
ATOM   2666 C C   . GLY B 1 174 ? 109.34300 128.67100 137.63900 1.000 50.03450 ? 174 GLY B C   1 
ATOM   2667 O O   . GLY B 1 174 ? 109.52200 128.96900 138.82100 1.000 50.03450 ? 174 GLY B O   1 
ATOM   2668 N N   . GLU B 1 181 ? 109.52300 127.12300 132.58500 1.000 51.43352 ? 181 GLU B N   1 
ATOM   2669 C CA  . GLU B 1 181 ? 108.07900 127.13300 132.38800 1.000 51.43352 ? 181 GLU B CA  1 
ATOM   2670 C C   . GLU B 1 181 ? 107.39400 125.99500 133.13400 1.000 51.43352 ? 181 GLU B C   1 
ATOM   2671 O O   . GLU B 1 181 ? 107.87700 124.86700 133.14200 1.000 51.43352 ? 181 GLU B O   1 
ATOM   2672 C CB  . GLU B 1 181 ? 107.74500 127.06200 130.89600 1.000 51.43352 ? 181 GLU B CB  1 
ATOM   2673 C CG  . GLU B 1 181 ? 108.68100 126.18200 130.08600 1.000 51.43352 ? 181 GLU B CG  1 
ATOM   2674 C CD  . GLU B 1 181 ? 108.47400 126.33100 128.58800 1.000 51.43352 ? 181 GLU B CD  1 
ATOM   2675 O OE1 . GLU B 1 181 ? 107.37100 126.74700 128.17600 1.000 51.43352 ? 181 GLU B OE1 1 
ATOM   2676 O OE2 . GLU B 1 181 ? 109.41600 126.03400 127.82200 1.000 51.43352 ? 181 GLU B OE2 1 
ATOM   2677 N N   . HIS B 1 182 ? 106.27000 126.32000 133.76700 1.000 40.90885 ? 182 HIS B N   1 
ATOM   2678 C CA  . HIS B 1 182 ? 105.45400 125.33000 134.45500 1.000 40.90885 ? 182 HIS B CA  1 
ATOM   2679 C C   . HIS B 1 182 ? 104.88600 124.33800 133.44600 1.000 40.90885 ? 182 HIS B C   1 
ATOM   2680 O O   . HIS B 1 182 ? 104.18400 124.72900 132.51000 1.000 40.90885 ? 182 HIS B O   1 
ATOM   2681 C CB  . HIS B 1 182 ? 104.33100 126.04100 135.20800 1.000 40.90885 ? 182 HIS B CB  1 
ATOM   2682 C CG  . HIS B 1 182 ? 103.74900 125.25400 136.33900 1.000 40.90885 ? 182 HIS B CG  1 
ATOM   2683 N ND1 . HIS B 1 182 ? 104.13800 123.96700 136.63400 1.000 40.90885 ? 182 HIS B ND1 1 
ATOM   2684 C CD2 . HIS B 1 182 ? 102.80400 125.58000 137.25100 1.000 40.90885 ? 182 HIS B CD2 1 
ATOM   2685 C CE1 . HIS B 1 182 ? 103.45800 123.53300 137.67800 1.000 40.90885 ? 182 HIS B CE1 1 
ATOM   2686 N NE2 . HIS B 1 182 ? 102.64000 124.49200 138.07200 1.000 40.90885 ? 182 HIS B NE2 1 
ATOM   2687 N N   . ASP B 1 183 ? 105.19300 123.05500 133.62400 1.000 37.16755 ? 183 ASP B N   1 
ATOM   2688 C CA  . ASP B 1 183 ? 104.82500 122.07000 132.61600 1.000 37.16755 ? 183 ASP B CA  1 
ATOM   2689 C C   . ASP B 1 183 ? 104.72400 120.68200 133.23500 1.000 37.16755 ? 183 ASP B C   1 
ATOM   2690 O O   . ASP B 1 183 ? 105.28700 120.40000 134.29500 1.000 37.16755 ? 183 ASP B O   1 
ATOM   2691 C CB  . ASP B 1 183 ? 105.83100 122.06500 131.46200 1.000 37.16755 ? 183 ASP B CB  1 
ATOM   2692 C CG  . ASP B 1 183 ? 107.14500 121.41000 131.83700 1.000 37.16755 ? 183 ASP B CG  1 
ATOM   2693 O OD1 . ASP B 1 183 ? 107.72700 121.78400 132.87600 1.000 37.16755 ? 183 ASP B OD1 1 
ATOM   2694 O OD2 . ASP B 1 183 ? 107.59600 120.51000 131.10300 1.000 37.16755 ? 183 ASP B OD2 1 
ATOM   2695 N N   . TYR B 1 184 ? 103.98400 119.82200 132.54200 1.000 29.17813 ? 184 TYR B N   1 
ATOM   2696 C CA  . TYR B 1 184 ? 103.96200 118.38500 132.75100 1.000 29.17813 ? 184 TYR B CA  1 
ATOM   2697 C C   . TYR B 1 184 ? 104.86000 117.72700 131.71500 1.000 29.17813 ? 184 TYR B C   1 
ATOM   2698 O O   . TYR B 1 184 ? 104.97100 118.19600 130.58400 1.000 29.17813 ? 184 TYR B O   1 
ATOM   2699 C CB  . TYR B 1 184 ? 102.55000 117.82100 132.62200 1.000 29.17813 ? 184 TYR B CB  1 
ATOM   2700 C CG  . TYR B 1 184 ? 101.58000 118.34200 133.64300 1.000 29.17813 ? 184 TYR B CG  1 
ATOM   2701 C CD1 . TYR B 1 184 ? 100.57600 119.22800 133.28200 1.000 29.17813 ? 184 TYR B CD1 1 
ATOM   2702 C CD2 . TYR B 1 184 ? 101.66000 117.94300 134.96500 1.000 29.17813 ? 184 TYR B CD2 1 
ATOM   2703 C CE1 . TYR B 1 184 ? 99.68300  119.70100 134.20900 1.000 29.17813 ? 184 TYR B CE1 1 
ATOM   2704 C CE2 . TYR B 1 184 ? 100.77500 118.41400 135.89800 1.000 29.17813 ? 184 TYR B CE2 1 
ATOM   2705 C CZ  . TYR B 1 184 ? 99.78700  119.28900 135.51700 1.000 29.17813 ? 184 TYR B CZ  1 
ATOM   2706 O OH  . TYR B 1 184 ? 98.90200  119.76100 136.44900 1.000 29.17813 ? 184 TYR B OH  1 
ATOM   2707 N N   . GLN B 1 185 ? 105.50000 116.63500 132.10700 1.000 26.08644 ? 185 GLN B N   1 
ATOM   2708 C CA  . GLN B 1 185 ? 106.51800 116.01200 131.27600 1.000 26.08644 ? 185 GLN B CA  1 
ATOM   2709 C C   . GLN B 1 185 ? 106.49700 114.51100 131.50400 1.000 26.08644 ? 185 GLN B C   1 
ATOM   2710 O O   . GLN B 1 185 ? 106.47400 114.05400 132.64900 1.000 26.08644 ? 185 GLN B O   1 
ATOM   2711 C CB  . GLN B 1 185 ? 107.89900 116.59900 131.58800 1.000 26.08644 ? 185 GLN B CB  1 
ATOM   2712 C CG  . GLN B 1 185 ? 109.05000 115.99500 130.81000 1.000 26.08644 ? 185 GLN B CG  1 
ATOM   2713 C CD  . GLN B 1 185 ? 109.77700 114.91600 131.58700 1.000 26.08644 ? 185 GLN B CD  1 
ATOM   2714 O OE1 . GLN B 1 185 ? 109.77700 113.75700 131.19800 1.000 26.08644 ? 185 GLN B OE1 1 
ATOM   2715 N NE2 . GLN B 1 185 ? 110.39400 115.29600 132.69200 1.000 26.08644 ? 185 GLN B NE2 1 
ATOM   2716 N N   . ILE B 1 186 ? 106.45700 113.75100 130.41300 1.000 23.90782 ? 186 ILE B N   1 
ATOM   2717 C CA  . ILE B 1 186 ? 106.70300 112.31300 130.43400 1.000 23.90782 ? 186 ILE B CA  1 
ATOM   2718 C C   . ILE B 1 186 ? 107.62000 111.97400 129.27200 1.000 23.90782 ? 186 ILE B C   1 
ATOM   2719 O O   . ILE B 1 186 ? 107.33300 112.34000 128.12800 1.000 23.90782 ? 186 ILE B O   1 
ATOM   2720 C CB  . ILE B 1 186 ? 105.41400 111.47000 130.34000 1.000 23.90782 ? 186 ILE B CB  1 
ATOM   2721 C CG1 . ILE B 1 186 ? 104.29500 112.02600 131.21500 1.000 23.90782 ? 186 ILE B CG1 1 
ATOM   2722 C CG2 . ILE B 1 186 ? 105.70300 110.04800 130.74900 1.000 23.90782 ? 186 ILE B CG2 1 
ATOM   2723 C CD1 . ILE B 1 186 ? 102.95900 111.44400 130.89900 1.000 23.90782 ? 186 ILE B CD1 1 
ATOM   2724 N N   . GLY B 1 187 ? 108.71000 111.26600 129.56100 1.000 23.84358 ? 187 GLY B N   1 
ATOM   2725 C CA  . GLY B 1 187 ? 109.64800 110.85900 128.53200 1.000 23.84358 ? 187 GLY B CA  1 
ATOM   2726 C C   . GLY B 1 187 ? 110.30600 111.99700 127.79200 1.000 23.84358 ? 187 GLY B C   1 
ATOM   2727 O O   . GLY B 1 187 ? 110.72600 111.82100 126.65000 1.000 23.84358 ? 187 GLY B O   1 
ATOM   2728 N N   . GLY B 1 188 ? 110.40700 113.16600 128.41300 1.000 24.85434 ? 188 GLY B N   1 
ATOM   2729 C CA  . GLY B 1 188 ? 110.89600 114.34800 127.75100 1.000 24.85434 ? 188 GLY B CA  1 
ATOM   2730 C C   . GLY B 1 188 ? 109.85900 115.09600 126.94400 1.000 24.85434 ? 188 GLY B C   1 
ATOM   2731 O O   . GLY B 1 188 ? 110.16600 116.17200 126.42400 1.000 24.85434 ? 188 GLY B O   1 
ATOM   2732 N N   . TYR B 1 189 ? 108.64700 114.56600 126.82000 1.000 27.37428 ? 189 TYR B N   1 
ATOM   2733 C CA  . TYR B 1 189 ? 107.55700 115.25900 126.14900 1.000 27.37428 ? 189 TYR B CA  1 
ATOM   2734 C C   . TYR B 1 189 ? 106.84800 116.15900 127.14600 1.000 27.37428 ? 189 TYR B C   1 
ATOM   2735 O O   . TYR B 1 189 ? 106.54800 115.73800 128.26600 1.000 27.37428 ? 189 TYR B O   1 
ATOM   2736 C CB  . TYR B 1 189 ? 106.56800 114.27200 125.53400 1.000 27.37428 ? 189 TYR B CB  1 
ATOM   2737 C CG  . TYR B 1 189 ? 107.10200 113.53900 124.33900 1.000 27.37428 ? 189 TYR B CG  1 
ATOM   2738 C CD1 . TYR B 1 189 ? 107.12600 114.13900 123.08900 1.000 27.37428 ? 189 TYR B CD1 1 
ATOM   2739 C CD2 . TYR B 1 189 ? 107.58500 112.24500 124.45500 1.000 27.37428 ? 189 TYR B CD2 1 
ATOM   2740 C CE1 . TYR B 1 189 ? 107.60800 113.47000 121.99200 1.000 27.37428 ? 189 TYR B CE1 1 
ATOM   2741 C CE2 . TYR B 1 189 ? 108.07200 111.57000 123.36500 1.000 27.37428 ? 189 TYR B CE2 1 
ATOM   2742 C CZ  . TYR B 1 189 ? 108.08400 112.18800 122.13600 1.000 27.37428 ? 189 TYR B CZ  1 
ATOM   2743 O OH  . TYR B 1 189 ? 108.56900 111.51600 121.04700 1.000 27.37428 ? 189 TYR B OH  1 
ATOM   2744 N N   . THR B 1 190 ? 106.56500 117.38300 126.72300 1.000 31.44228 ? 190 THR B N   1 
ATOM   2745 C CA  . THR B 1 190 ? 106.14500 118.45800 127.60500 1.000 31.44228 ? 190 THR B CA  1 
ATOM   2746 C C   . THR B 1 190 ? 104.79900 119.01500 127.16200 1.000 31.44228 ? 190 THR B C   1 
ATOM   2747 O O   . THR B 1 190 ? 104.56100 119.22800 125.97100 1.000 31.44228 ? 190 THR B O   1 
ATOM   2748 C CB  . THR B 1 190 ? 107.22000 119.56200 127.62800 1.000 31.44228 ? 190 THR B CB  1 
ATOM   2749 O OG1 . THR B 1 190 ? 108.26400 119.19800 128.53800 1.000 31.44228 ? 190 THR B OG1 1 
ATOM   2750 C CG2 . THR B 1 190 ? 106.64800 120.90900 128.02200 1.000 31.44228 ? 190 THR B CG2 1 
ATOM   2751 N N   . GLU B 1 191 ? 103.91600 119.21900 128.13100 1.000 33.95051 ? 191 GLU B N   1 
ATOM   2752 C CA  . GLU B 1 191 ? 102.65900 119.92500 127.95600 1.000 33.95051 ? 191 GLU B CA  1 
ATOM   2753 C C   . GLU B 1 191 ? 102.64500 121.08600 128.93600 1.000 33.95051 ? 191 GLU B C   1 
ATOM   2754 O O   . GLU B 1 191 ? 102.96900 120.90800 130.11000 1.000 33.95051 ? 191 GLU B O   1 
ATOM   2755 C CB  . GLU B 1 191 ? 101.47000 119.00500 128.22100 1.000 33.95051 ? 191 GLU B CB  1 
ATOM   2756 C CG  . GLU B 1 191 ? 100.19300 119.39200 127.52500 1.000 33.95051 ? 191 GLU B CG  1 
ATOM   2757 C CD  . GLU B 1 191 ? 99.90200  118.51300 126.33100 1.000 33.95051 ? 191 GLU B CD  1 
ATOM   2758 O OE1 . GLU B 1 191 ? 98.80700  118.63700 125.75000 1.000 33.95051 ? 191 GLU B OE1 1 
ATOM   2759 O OE2 . GLU B 1 191 ? 100.76900 117.68900 125.98000 1.000 33.95051 ? 191 GLU B OE2 1 
ATOM   2760 N N   . LYS B 1 192 ? 102.27700 122.27100 128.46500 1.000 34.87661 ? 192 LYS B N   1 
ATOM   2761 C CA  . LYS B 1 192 ? 102.27200 123.43500 129.33900 1.000 34.87661 ? 192 LYS B CA  1 
ATOM   2762 C C   . LYS B 1 192 ? 101.19100 123.30300 130.40600 1.000 34.87661 ? 192 LYS B C   1 
ATOM   2763 O O   . LYS B 1 192 ? 100.08800 122.82500 130.14200 1.000 34.87661 ? 192 LYS B O   1 
ATOM   2764 C CB  . LYS B 1 192 ? 102.06800 124.71100 128.52500 1.000 34.87661 ? 192 LYS B CB  1 
ATOM   2765 C CG  . LYS B 1 192 ? 101.96400 125.97100 129.35700 1.000 34.87661 ? 192 LYS B CG  1 
ATOM   2766 C CD  . LYS B 1 192 ? 101.16700 127.03900 128.65400 1.000 34.87661 ? 192 LYS B CD  1 
ATOM   2767 C CE  . LYS B 1 192 ? 101.85700 128.38700 128.72900 1.000 34.87661 ? 192 LYS B CE  1 
ATOM   2768 N NZ  . LYS B 1 192 ? 101.31400 129.21500 129.83600 1.000 34.87661 ? 192 LYS B NZ  1 
ATOM   2769 N N   . TRP B 1 193 ? 101.52900 123.70900 131.62500 1.000 33.49499 ? 193 TRP B N   1 
ATOM   2770 C CA  . TRP B 1 193 ? 100.59400 123.64100 132.73800 1.000 33.49499 ? 193 TRP B CA  1 
ATOM   2771 C C   . TRP B 1 193 ? 99.43600  124.61300 132.54100 1.000 33.49499 ? 193 TRP B C   1 
ATOM   2772 O O   . TRP B 1 193 ? 99.64200  125.80000 132.28200 1.000 33.49499 ? 193 TRP B O   1 
ATOM   2773 C CB  . TRP B 1 193 ? 101.32700 123.95000 134.04400 1.000 33.49499 ? 193 TRP B CB  1 
ATOM   2774 C CG  . TRP B 1 193 ? 100.56600 123.61800 135.29100 1.000 33.49499 ? 193 TRP B CG  1 
ATOM   2775 C CD1 . TRP B 1 193 ? 100.69000 122.49600 136.04300 1.000 33.49499 ? 193 TRP B CD1 1 
ATOM   2776 C CD2 . TRP B 1 193 ? 99.58900  124.43400 135.94900 1.000 33.49499 ? 193 TRP B CD2 1 
ATOM   2777 N NE1 . TRP B 1 193 ? 99.84500  122.54900 137.12000 1.000 33.49499 ? 193 TRP B NE1 1 
ATOM   2778 C CE2 . TRP B 1 193 ? 99.15700  123.73100 137.08500 1.000 33.49499 ? 193 TRP B CE2 1 
ATOM   2779 C CE3 . TRP B 1 193 ? 99.03200  125.68700 135.68200 1.000 33.49499 ? 193 TRP B CE3 1 
ATOM   2780 C CZ2 . TRP B 1 193 ? 98.19700  124.23600 137.95300 1.000 33.49499 ? 193 TRP B CZ2 1 
ATOM   2781 C CZ3 . TRP B 1 193 ? 98.07800  126.18400 136.54100 1.000 33.49499 ? 193 TRP B CZ3 1 
ATOM   2782 C CH2 . TRP B 1 193 ? 97.66900  125.46100 137.66200 1.000 33.49499 ? 193 TRP B CH2 1 
ATOM   2783 N N   . GLU B 1 194 ? 98.21500  124.10300 132.67700 1.000 35.20920 ? 194 GLU B N   1 
ATOM   2784 C CA  . GLU B 1 194 ? 97.01300  124.93100 132.73600 1.000 35.20920 ? 194 GLU B CA  1 
ATOM   2785 C C   . GLU B 1 194 ? 96.16500  124.67000 133.96400 1.000 35.20920 ? 194 GLU B C   1 
ATOM   2786 O O   . GLU B 1 194 ? 95.31800  125.50600 134.29000 1.000 35.20920 ? 194 GLU B O   1 
ATOM   2787 C CB  . GLU B 1 194 ? 96.13500  124.71300 131.49300 1.000 35.20920 ? 194 GLU B CB  1 
ATOM   2788 C CG  . GLU B 1 194 ? 96.73900  125.02300 130.12200 1.000 35.20920 ? 194 GLU B CG  1 
ATOM   2789 C CD  . GLU B 1 194 ? 97.34900  126.41600 129.96300 1.000 35.20920 ? 194 GLU B CD  1 
ATOM   2790 O OE1 . GLU B 1 194 ? 97.11500  127.32100 130.79100 1.000 35.20920 ? 194 GLU B OE1 1 
ATOM   2791 O OE2 . GLU B 1 194 ? 98.06000  126.61300 128.96200 1.000 35.20920 ? 194 GLU B OE2 1 
ATOM   2792 N N   . SER B 1 195 ? 96.37400  123.56000 134.66500 1.000 33.28462 ? 195 SER B N   1 
ATOM   2793 C CA  . SER B 1 195 ? 95.50500  123.10900 135.73900 1.000 33.28462 ? 195 SER B CA  1 
ATOM   2794 C C   . SER B 1 195 ? 96.17500  121.92700 136.42000 1.000 33.28462 ? 195 SER B C   1 
ATOM   2795 O O   . SER B 1 195 ? 97.23800  121.46700 136.00300 1.000 33.28462 ? 195 SER B O   1 
ATOM   2796 C CB  . SER B 1 195 ? 94.12300  122.73200 135.20700 1.000 33.28462 ? 195 SER B CB  1 
ATOM   2797 O OG  . SER B 1 195 ? 94.25300  121.95600 134.03700 1.000 33.28462 ? 195 SER B OG  1 
ATOM   2798 N N   . GLY B 1 196 ? 95.52700  121.42900 137.46400 1.000 32.63372 ? 196 GLY B N   1 
ATOM   2799 C CA  . GLY B 1 196 ? 96.10200  120.37300 138.26700 1.000 32.63372 ? 196 GLY B CA  1 
ATOM   2800 C C   . GLY B 1 196 ? 95.98600  119.00100 137.63400 1.000 32.63372 ? 196 GLY B C   1 
ATOM   2801 O O   . GLY B 1 196 ? 95.39300  118.80100 136.57400 1.000 32.63372 ? 196 GLY B O   1 
ATOM   2802 N N   . VAL B 1 197 ? 96.59500  118.03100 138.31300 1.000 31.93374 ? 197 VAL B N   1 
ATOM   2803 C CA  . VAL B 1 197 ? 96.50300  116.63800 137.90200 1.000 31.93374 ? 197 VAL B CA  1 
ATOM   2804 C C   . VAL B 1 197 ? 95.14300  116.07400 138.29700 1.000 31.93374 ? 197 VAL B C   1 
ATOM   2805 O O   . VAL B 1 197 ? 94.45300  116.58900 139.17600 1.000 31.93374 ? 197 VAL B O   1 
ATOM   2806 C CB  . VAL B 1 197 ? 97.64300  115.79700 138.51100 1.000 31.93374 ? 197 VAL B CB  1 
ATOM   2807 C CG1 . VAL B 1 197 ? 98.98200  116.23800 137.98100 1.000 31.93374 ? 197 VAL B CG1 1 
ATOM   2808 C CG2 . VAL B 1 197 ? 97.61600  115.87800 140.02400 1.000 31.93374 ? 197 VAL B CG2 1 
ATOM   2809 N N   . LYS B 1 198 ? 94.76300  114.99100 137.63700 1.000 32.87681 ? 198 LYS B N   1 
ATOM   2810 C CA  . LYS B 1 198 ? 93.58300  114.22500 137.99800 1.000 32.87681 ? 198 LYS B CA  1 
ATOM   2811 C C   . LYS B 1 198 ? 93.99900  112.92700 138.67500 1.000 32.87681 ? 198 LYS B C   1 
ATOM   2812 O O   . LYS B 1 198 ? 95.11200  112.43100 138.49400 1.000 32.87681 ? 198 LYS B O   1 
ATOM   2813 C CB  . LYS B 1 198 ? 92.71900  113.93500 136.76500 1.000 32.87681 ? 198 LYS B CB  1 
ATOM   2814 C CG  . LYS B 1 198 ? 91.99500  115.14800 136.23400 1.000 32.87681 ? 198 LYS B CG  1 
ATOM   2815 C CD  . LYS B 1 198 ? 90.97900  115.65000 137.23900 1.000 32.87681 ? 198 LYS B CD  1 
ATOM   2816 C CE  . LYS B 1 198 ? 90.22300  116.85000 136.71100 1.000 32.87681 ? 198 LYS B CE  1 
ATOM   2817 N NZ  . LYS B 1 198 ? 88.96400  116.43700 136.03600 1.000 32.87681 ? 198 LYS B NZ  1 
ATOM   2818 N N   . ASP B 1 199 ? 93.08400  112.38100 139.47100 1.000 35.14513 ? 199 ASP B N   1 
ATOM   2819 C CA  . ASP B 1 199 ? 93.31800  111.10600 140.13000 1.000 35.14513 ? 199 ASP B CA  1 
ATOM   2820 C C   . ASP B 1 199 ? 93.30300  109.93000 139.16600 1.000 35.14513 ? 199 ASP B C   1 
ATOM   2821 O O   . ASP B 1 199 ? 93.79600  108.85600 139.51900 1.000 35.14513 ? 199 ASP B O   1 
ATOM   2822 C CB  . ASP B 1 199 ? 92.27700  110.88400 141.22500 1.000 35.14513 ? 199 ASP B CB  1 
ATOM   2823 C CG  . ASP B 1 199 ? 92.48000  111.79600 142.41000 1.000 35.14513 ? 199 ASP B CG  1 
ATOM   2824 O OD1 . ASP B 1 199 ? 93.59700  112.33300 142.56100 1.000 35.14513 ? 199 ASP B OD1 1 
ATOM   2825 O OD2 . ASP B 1 199 ? 91.52500  111.98300 143.19200 1.000 35.14513 ? 199 ASP B OD2 1 
ATOM   2826 N N   . CYS B 1 200 ? 92.75000  110.10300 137.96900 1.000 34.82278 ? 200 CYS B N   1 
ATOM   2827 C CA  . CYS B 1 200 ? 92.71700  109.05000 136.96600 1.000 34.82278 ? 200 CYS B CA  1 
ATOM   2828 C C   . CYS B 1 200 ? 93.12600  109.64000 135.62700 1.000 34.82278 ? 200 CYS B C   1 
ATOM   2829 O O   . CYS B 1 200 ? 92.57300  110.65600 135.20000 1.000 34.82278 ? 200 CYS B O   1 
ATOM   2830 C CB  . CYS B 1 200 ? 91.32800  108.41400 136.87200 1.000 34.82278 ? 200 CYS B CB  1 
ATOM   2831 S SG  . CYS B 1 200 ? 91.25900  106.91600 135.86300 1.000 34.82278 ? 200 CYS B SG  1 
ATOM   2832 N N   . VAL B 1 201 ? 94.09200  109.00500 134.97300 1.000 28.15478 ? 201 VAL B N   1 
ATOM   2833 C CA  . VAL B 1 201 ? 94.48300  109.35900 133.61500 1.000 28.15478 ? 201 VAL B CA  1 
ATOM   2834 C C   . VAL B 1 201 ? 94.24500  108.14300 132.73200 1.000 28.15478 ? 201 VAL B C   1 
ATOM   2835 O O   . VAL B 1 201 ? 94.02600  107.03500 133.21900 1.000 28.15478 ? 201 VAL B O   1 
ATOM   2836 C CB  . VAL B 1 201 ? 95.94600  109.83600 133.52700 1.000 28.15478 ? 201 VAL B CB  1 
ATOM   2837 C CG1 . VAL B 1 201 ? 96.13000  111.11400 134.31700 1.000 28.15478 ? 201 VAL B CG1 1 
ATOM   2838 C CG2 . VAL B 1 201 ? 96.88500  108.76200 134.01900 1.000 28.15478 ? 201 VAL B CG2 1 
ATOM   2839 N N   . VAL B 1 202 ? 94.26100  108.35100 131.41900 1.000 28.48841 ? 202 VAL B N   1 
ATOM   2840 C CA  . VAL B 1 202 ? 93.95500  107.26200 130.50000 1.000 28.48841 ? 202 VAL B CA  1 
ATOM   2841 C C   . VAL B 1 202 ? 94.96000  107.25400 129.35400 1.000 28.48841 ? 202 VAL B C   1 
ATOM   2842 O O   . VAL B 1 202 ? 95.25000  108.29300 128.76000 1.000 28.48841 ? 202 VAL B O   1 
ATOM   2843 C CB  . VAL B 1 202 ? 92.50100  107.34100 129.98400 1.000 28.48841 ? 202 VAL B CB  1 
ATOM   2844 C CG1 . VAL B 1 202 ? 92.19200  108.69800 129.36300 1.000 28.48841 ? 202 VAL B CG1 1 
ATOM   2845 C CG2 . VAL B 1 202 ? 92.20600  106.20100 129.02600 1.000 28.48841 ? 202 VAL B CG2 1 
ATOM   2846 N N   . LEU B 1 203 ? 95.49900  106.08100 129.05800 1.000 28.11460 ? 203 LEU B N   1 
ATOM   2847 C CA  . LEU B 1 203 ? 96.36100  105.86700 127.90900 1.000 28.11460 ? 203 LEU B CA  1 
ATOM   2848 C C   . LEU B 1 203 ? 95.50600  105.37100 126.74900 1.000 28.11460 ? 203 LEU B C   1 
ATOM   2849 O O   . LEU B 1 203 ? 94.85200  104.33000 126.85800 1.000 28.11460 ? 203 LEU B O   1 
ATOM   2850 C CB  . LEU B 1 203 ? 97.45500  104.85900 128.25500 1.000 28.11460 ? 203 LEU B CB  1 
ATOM   2851 C CG  . LEU B 1 203 ? 98.75500  104.84600 127.45700 1.000 28.11460 ? 203 LEU B CG  1 
ATOM   2852 C CD1 . LEU B 1 203 ? 99.52200  106.14200 127.62400 1.000 28.11460 ? 203 LEU B CD1 1 
ATOM   2853 C CD2 . LEU B 1 203 ? 99.59900  103.65800 127.88500 1.000 28.11460 ? 203 LEU B CD2 1 
ATOM   2854 N N   . HIS B 1 204 ? 95.51000  106.11800 125.65100 1.000 30.76395 ? 204 HIS B N   1 
ATOM   2855 C CA  . HIS B 1 204 ? 94.72600  105.80700 124.46700 1.000 30.76395 ? 204 HIS B CA  1 
ATOM   2856 C C   . HIS B 1 204 ? 95.62800  105.34800 123.33200 1.000 30.76395 ? 204 HIS B C   1 
ATOM   2857 O O   . HIS B 1 204 ? 96.70800  105.90500 123.11900 1.000 30.76395 ? 204 HIS B O   1 
ATOM   2858 C CB  . HIS B 1 204 ? 93.93200  107.02200 123.98600 1.000 30.76395 ? 204 HIS B CB  1 
ATOM   2859 C CG  . HIS B 1 204 ? 92.77600  107.38900 124.85900 1.000 30.76395 ? 204 HIS B CG  1 
ATOM   2860 N ND1 . HIS B 1 204 ? 91.82500  106.47800 125.26200 1.000 30.76395 ? 204 HIS B ND1 1 
ATOM   2861 C CD2 . HIS B 1 204 ? 92.39400  108.58200 125.37000 1.000 30.76395 ? 204 HIS B CD2 1 
ATOM   2862 C CE1 . HIS B 1 204 ? 90.91400  107.09200 125.99300 1.000 30.76395 ? 204 HIS B CE1 1 
ATOM   2863 N NE2 . HIS B 1 204 ? 91.23800  108.36800 126.07700 1.000 30.76395 ? 204 HIS B NE2 1 
ATOM   2864 N N   . SER B 1 205 ? 95.17000  104.33400 122.60300 1.000 36.82969 ? 205 SER B N   1 
ATOM   2865 C CA  . SER B 1 205 ? 95.70600  104.01000 121.28800 1.000 36.82969 ? 205 SER B CA  1 
ATOM   2866 C C   . SER B 1 205 ? 94.55400  103.95600 120.29700 1.000 36.82969 ? 205 SER B C   1 
ATOM   2867 O O   . SER B 1 205 ? 93.44800  104.40400 120.61300 1.000 36.82969 ? 205 SER B O   1 
ATOM   2868 C CB  . SER B 1 205 ? 96.46800  102.68800 121.29600 1.000 36.82969 ? 205 SER B CB  1 
ATOM   2869 O OG  . SER B 1 205 ? 95.67500  101.63000 121.79100 1.000 36.82969 ? 205 SER B OG  1 
ATOM   2870 N N   . TYR B 1 206 ? 94.81000  103.42600 119.09800 1.000 42.62040 ? 206 TYR B N   1 
ATOM   2871 C CA  . TYR B 1 206 ? 93.75000  103.23700 118.11000 1.000 42.62040 ? 206 TYR B CA  1 
ATOM   2872 C C   . TYR B 1 206 ? 92.62800  102.36800 118.66000 1.000 42.62040 ? 206 TYR B C   1 
ATOM   2873 O O   . TYR B 1 206 ? 91.44600  102.68500 118.50100 1.000 42.62040 ? 206 TYR B O   1 
ATOM   2874 C CB  . TYR B 1 206 ? 94.31300  102.59300 116.84600 1.000 42.62040 ? 206 TYR B CB  1 
ATOM   2875 C CG  . TYR B 1 206 ? 95.24200  103.44300 116.02100 1.000 42.62040 ? 206 TYR B CG  1 
ATOM   2876 C CD1 . TYR B 1 206 ? 94.95700  104.77200 115.75300 1.000 42.62040 ? 206 TYR B CD1 1 
ATOM   2877 C CD2 . TYR B 1 206 ? 96.39700  102.90000 115.48600 1.000 42.62040 ? 206 TYR B CD2 1 
ATOM   2878 C CE1 . TYR B 1 206 ? 95.81100  105.53700 114.98800 1.000 42.62040 ? 206 TYR B CE1 1 
ATOM   2879 C CE2 . TYR B 1 206 ? 97.25100  103.65200 114.72400 1.000 42.62040 ? 206 TYR B CE2 1 
ATOM   2880 C CZ  . TYR B 1 206 ? 96.95600  104.96700 114.47400 1.000 42.62040 ? 206 TYR B CZ  1 
ATOM   2881 O OH  . TYR B 1 206 ? 97.81900  105.70700 113.70800 1.000 42.62040 ? 206 TYR B OH  1 
ATOM   2882 N N   . PHE B 1 207 ? 92.98300  101.26800 119.32400 1.000 46.85688 ? 207 PHE B N   1 
ATOM   2883 C CA  . PHE B 1 207 ? 92.01700  100.24700 119.69000 1.000 46.85688 ? 207 PHE B CA  1 
ATOM   2884 C C   . PHE B 1 207 ? 91.88500  100.00000 121.18300 1.000 46.85688 ? 207 PHE B C   1 
ATOM   2885 O O   . PHE B 1 207 ? 90.92500  99.34100  121.59100 1.000 46.85688 ? 207 PHE B O   1 
ATOM   2886 C CB  . PHE B 1 207 ? 92.37000  98.92200  118.99900 1.000 46.85688 ? 207 PHE B CB  1 
ATOM   2887 C CG  . PHE B 1 207 ? 92.67500  99.07800  117.54200 1.000 46.85688 ? 207 PHE B CG  1 
ATOM   2888 C CD1 . PHE B 1 207 ? 93.95300  98.87200  117.06300 1.000 46.85688 ? 207 PHE B CD1 1 
ATOM   2889 C CD2 . PHE B 1 207 ? 91.68500  99.45800  116.65400 1.000 46.85688 ? 207 PHE B CD2 1 
ATOM   2890 C CE1 . PHE B 1 207 ? 94.23400  99.02700  115.72400 1.000 46.85688 ? 207 PHE B CE1 1 
ATOM   2891 C CE2 . PHE B 1 207 ? 91.96100  99.61400  115.32000 1.000 46.85688 ? 207 PHE B CE2 1 
ATOM   2892 C CZ  . PHE B 1 207 ? 93.23700  99.39900  114.85300 1.000 46.85688 ? 207 PHE B CZ  1 
ATOM   2893 N N   . THR B 1 208 ? 92.79700  100.50800 122.00600 1.000 39.17506 ? 208 THR B N   1 
ATOM   2894 C CA  . THR B 1 208 ? 92.81300  100.20400 123.42800 1.000 39.17506 ? 208 THR B CA  1 
ATOM   2895 C C   . THR B 1 208 ? 92.74400  101.47800 124.25600 1.000 39.17506 ? 208 THR B C   1 
ATOM   2896 O O   . THR B 1 208 ? 93.08600  102.56700 123.78900 1.000 39.17506 ? 208 THR B O   1 
ATOM   2897 C CB  . THR B 1 208 ? 94.07000  99.41300  123.82100 1.000 39.17506 ? 208 THR B CB  1 
ATOM   2898 O OG1 . THR B 1 208 ? 95.23600  100.21300 123.59200 1.000 39.17506 ? 208 THR B OG1 1 
ATOM   2899 C CG2 . THR B 1 208 ? 94.17900  98.13600  123.01200 1.000 39.17506 ? 208 THR B CG2 1 
ATOM   2900 N N   . SER B 1 209 ? 92.28400  101.32400 125.49400 1.000 35.08015 ? 209 SER B N   1 
ATOM   2901 C CA  . SER B 1 209 ? 92.31400  102.37800 126.49600 1.000 35.08015 ? 209 SER B CA  1 
ATOM   2902 C C   . SER B 1 209 ? 92.61100  101.74300 127.84300 1.000 35.08015 ? 209 SER B C   1 
ATOM   2903 O O   . SER B 1 209 ? 91.90200  100.82800 128.26800 1.000 35.08015 ? 209 SER B O   1 
ATOM   2904 C CB  . SER B 1 209 ? 90.99200  103.14500 126.55000 1.000 35.08015 ? 209 SER B CB  1 
ATOM   2905 O OG  . SER B 1 209 ? 90.87500  104.03400 125.45800 1.000 35.08015 ? 209 SER B OG  1 
ATOM   2906 N N   . ASP B 1 210 ? 93.65400  102.22100 128.50600 1.000 33.03247 ? 210 ASP B N   1 
ATOM   2907 C CA  . ASP B 1 210 ? 94.04800  101.71000 129.81000 1.000 33.03247 ? 210 ASP B CA  1 
ATOM   2908 C C   . ASP B 1 210 ? 94.01300  102.83800 130.82800 1.000 33.03247 ? 210 ASP B C   1 
ATOM   2909 O O   . ASP B 1 210 ? 94.51000  103.92900 130.56800 1.000 33.03247 ? 210 ASP B O   1 
ATOM   2910 C CB  . ASP B 1 210 ? 95.44000  101.07700 129.75400 1.000 33.03247 ? 210 ASP B CB  1 
ATOM   2911 C CG  . ASP B 1 210 ? 95.46900  99.81600  128.91500 1.000 33.03247 ? 210 ASP B CG  1 
ATOM   2912 O OD1 . ASP B 1 210 ? 95.01700  98.76400  129.40600 1.000 33.03247 ? 210 ASP B OD1 1 
ATOM   2913 O OD2 . ASP B 1 210 ? 95.93500  99.87500  127.75900 1.000 33.03247 ? 210 ASP B OD2 1 
ATOM   2914 N N   . TYR B 1 211 ? 93.43400  102.57900 131.99000 1.000 32.17740 ? 211 TYR B N   1 
ATOM   2915 C CA  . TYR B 1 211 ? 93.24200  103.61300 132.99500 1.000 32.17740 ? 211 TYR B CA  1 
ATOM   2916 C C   . TYR B 1 211 ? 94.26500  103.47400 134.11100 1.000 32.17740 ? 211 TYR B C   1 
ATOM   2917 O O   . TYR B 1 211 ? 94.63700  102.36400 134.49500 1.000 32.17740 ? 211 TYR B O   1 
ATOM   2918 C CB  . TYR B 1 211 ? 91.82000  103.57300 133.55400 1.000 32.17740 ? 211 TYR B CB  1 
ATOM   2919 C CG  . TYR B 1 211 ? 90.79500  103.99200 132.53300 1.000 32.17740 ? 211 TYR B CG  1 
ATOM   2920 C CD1 . TYR B 1 211 ? 90.32000  105.29200 132.49800 1.000 32.17740 ? 211 TYR B CD1 1 
ATOM   2921 C CD2 . TYR B 1 211 ? 90.31600  103.09600 131.58700 1.000 32.17740 ? 211 TYR B CD2 1 
ATOM   2922 C CE1 . TYR B 1 211 ? 89.39400  105.68600 131.56200 1.000 32.17740 ? 211 TYR B CE1 1 
ATOM   2923 C CE2 . TYR B 1 211 ? 89.39400  103.48100 130.64700 1.000 32.17740 ? 211 TYR B CE2 1 
ATOM   2924 C CZ  . TYR B 1 211 ? 88.93400  104.77600 130.64000 1.000 32.17740 ? 211 TYR B CZ  1 
ATOM   2925 O OH  . TYR B 1 211 ? 88.00900  105.16500 129.70500 1.000 32.17740 ? 211 TYR B OH  1 
ATOM   2926 N N   . TYR B 1 212 ? 94.72900  104.61500 134.61000 1.000 28.78915 ? 212 TYR B N   1 
ATOM   2927 C CA  . TYR B 1 212 ? 95.75400  104.67800 135.63700 1.000 28.78915 ? 212 TYR B CA  1 
ATOM   2928 C C   . TYR B 1 212 ? 95.23700  105.52500 136.78500 1.000 28.78915 ? 212 TYR B C   1 
ATOM   2929 O O   . TYR B 1 212 ? 94.65500  106.59200 136.56300 1.000 28.78915 ? 212 TYR B O   1 
ATOM   2930 C CB  . TYR B 1 212 ? 97.06100  105.26100 135.08600 1.000 28.78915 ? 212 TYR B CB  1 
ATOM   2931 C CG  . TYR B 1 212 ? 97.78200  104.35600 134.11100 1.000 28.78915 ? 212 TYR B CG  1 
ATOM   2932 C CD1 . TYR B 1 212 ? 98.91600  103.65700 134.49400 1.000 28.78915 ? 212 TYR B CD1 1 
ATOM   2933 C CD2 . TYR B 1 212 ? 97.33100  104.20700 132.80700 1.000 28.78915 ? 212 TYR B CD2 1 
ATOM   2934 C CE1 . TYR B 1 212 ? 99.57400  102.83100 133.61100 1.000 28.78915 ? 212 TYR B CE1 1 
ATOM   2935 C CE2 . TYR B 1 212 ? 97.97600  103.38200 131.92100 1.000 28.78915 ? 212 TYR B CE2 1 
ATOM   2936 C CZ  . TYR B 1 212 ? 99.09600  102.69700 132.32500 1.000 28.78915 ? 212 TYR B CZ  1 
ATOM   2937 O OH  . TYR B 1 212 ? 99.74100  101.88100 131.43600 1.000 28.78915 ? 212 TYR B OH  1 
ATOM   2938 N N   . GLN B 1 213 ? 95.45200  105.04600 138.00100 1.000 30.80199 ? 213 GLN B N   1 
ATOM   2939 C CA  . GLN B 1 213 ? 95.02100  105.70400 139.22100 1.000 30.80199 ? 213 GLN B CA  1 
ATOM   2940 C C   . GLN B 1 213 ? 96.23200  106.30200 139.92300 1.000 30.80199 ? 213 GLN B C   1 
ATOM   2941 O O   . GLN B 1 213 ? 97.27800  105.65900 140.02300 1.000 30.80199 ? 213 GLN B O   1 
ATOM   2942 C CB  . GLN B 1 213 ? 94.30200  104.70700 140.13500 1.000 30.80199 ? 213 GLN B CB  1 
ATOM   2943 C CG  . GLN B 1 213 ? 94.02100  105.19400 141.54100 1.000 30.80199 ? 213 GLN B CG  1 
ATOM   2944 C CD  . GLN B 1 213 ? 92.95300  106.26000 141.59100 1.000 30.80199 ? 213 GLN B CD  1 
ATOM   2945 O OE1 . GLN B 1 213 ? 91.96500  106.20000 140.86100 1.000 30.80199 ? 213 GLN B OE1 1 
ATOM   2946 N NE2 . GLN B 1 213 ? 93.14600  107.25100 142.45500 1.000 30.80199 ? 213 GLN B NE2 1 
ATOM   2947 N N   . LEU B 1 214 ? 96.09100  107.53700 140.39800 1.000 29.20607 ? 214 LEU B N   1 
ATOM   2948 C CA  . LEU B 1 214 ? 97.17700  108.20200 141.10700 1.000 29.20607 ? 214 LEU B CA  1 
ATOM   2949 C C   . LEU B 1 214 ? 97.41500  107.52700 142.45200 1.000 29.20607 ? 214 LEU B C   1 
ATOM   2950 O O   . LEU B 1 214 ? 96.52300  107.49500 143.30400 1.000 29.20607 ? 214 LEU B O   1 
ATOM   2951 C CB  . LEU B 1 214 ? 96.85500  109.68000 141.30200 1.000 29.20607 ? 214 LEU B CB  1 
ATOM   2952 C CG  . LEU B 1 214 ? 97.91900  110.48600 142.05100 1.000 29.20607 ? 214 LEU B CG  1 
ATOM   2953 C CD1 . LEU B 1 214 ? 99.20500  110.54700 141.25000 1.000 29.20607 ? 214 LEU B CD1 1 
ATOM   2954 C CD2 . LEU B 1 214 ? 97.41800  111.87400 142.38700 1.000 29.20607 ? 214 LEU B CD2 1 
ATOM   2955 N N   . TYR B 1 215 ? 98.61500  106.98600 142.64400 1.000 33.27668 ? 215 TYR B N   1 
ATOM   2956 C CA  . TYR B 1 215 ? 98.97400  106.27600 143.86000 1.000 33.27668 ? 215 TYR B CA  1 
ATOM   2957 C C   . TYR B 1 215 ? 99.83600  107.08500 144.80800 1.000 33.27668 ? 215 TYR B C   1 
ATOM   2958 O O   . TYR B 1 215 ? 99.74400  106.89000 146.01800 1.000 33.27668 ? 215 TYR B O   1 
ATOM   2959 C CB  . TYR B 1 215 ? 99.72200  104.98400 143.51800 1.000 33.27668 ? 215 TYR B CB  1 
ATOM   2960 C CG  . TYR B 1 215 ? 98.85100  103.75800 143.47900 1.000 33.27668 ? 215 TYR B CG  1 
ATOM   2961 C CD1 . TYR B 1 215 ? 99.30200  102.54900 143.98400 1.000 33.27668 ? 215 TYR B CD1 1 
ATOM   2962 C CD2 . TYR B 1 215 ? 97.57900  103.80700 142.93000 1.000 33.27668 ? 215 TYR B CD2 1 
ATOM   2963 C CE1 . TYR B 1 215 ? 98.50800  101.42500 143.94600 1.000 33.27668 ? 215 TYR B CE1 1 
ATOM   2964 C CE2 . TYR B 1 215 ? 96.78000  102.69200 142.88800 1.000 33.27668 ? 215 TYR B CE2 1 
ATOM   2965 C CZ  . TYR B 1 215 ? 97.24700  101.50400 143.39600 1.000 33.27668 ? 215 TYR B CZ  1 
ATOM   2966 O OH  . TYR B 1 215 ? 96.44800  100.39000 143.35100 1.000 33.27668 ? 215 TYR B OH  1 
ATOM   2967 N N   . SER B 1 216 ? 100.66700 107.98500 144.29200 1.000 33.10364 ? 216 SER B N   1 
ATOM   2968 C CA  . SER B 1 216 ? 101.66100 108.64700 145.11600 1.000 33.10364 ? 216 SER B CA  1 
ATOM   2969 C C   . SER B 1 216 ? 102.03900 109.97900 144.49000 1.000 33.10364 ? 216 SER B C   1 
ATOM   2970 O O   . SER B 1 216 ? 102.05000 110.12800 143.26700 1.000 33.10364 ? 216 SER B O   1 
ATOM   2971 C CB  . SER B 1 216 ? 102.90400 107.76500 145.28900 1.000 33.10364 ? 216 SER B CB  1 
ATOM   2972 O OG  . SER B 1 216 ? 103.84100 108.36400 146.15800 1.000 33.10364 ? 216 SER B OG  1 
ATOM   2973 N N   . THR B 1 217 ? 102.35000 110.94500 145.34700 1.000 33.78234 ? 217 THR B N   1 
ATOM   2974 C CA  . THR B 1 217 ? 102.81100 112.26800 144.94100 1.000 33.78234 ? 217 THR B CA  1 
ATOM   2975 C C   . THR B 1 217 ? 104.13400 112.53200 145.64700 1.000 33.78234 ? 217 THR B C   1 
ATOM   2976 O O   . THR B 1 217 ? 104.17100 112.65700 146.87400 1.000 33.78234 ? 217 THR B O   1 
ATOM   2977 C CB  . THR B 1 217 ? 101.78000 113.34300 145.28400 1.000 33.78234 ? 217 THR B CB  1 
ATOM   2978 O OG1 . THR B 1 217 ? 100.52600 113.01500 144.67700 1.000 33.78234 ? 217 THR B OG1 1 
ATOM   2979 C CG2 . THR B 1 217 ? 102.23600 114.69700 144.79200 1.000 33.78234 ? 217 THR B CG2 1 
ATOM   2980 N N   . GLN B 1 218 ? 105.21400 112.61500 144.87900 1.000 34.72376 ? 218 GLN B N   1 
ATOM   2981 C CA  . GLN B 1 218 ? 106.54600 112.79400 145.43900 1.000 34.72376 ? 218 GLN B CA  1 
ATOM   2982 C C   . GLN B 1 218 ? 106.91500 114.27100 145.40000 1.000 34.72376 ? 218 GLN B C   1 
ATOM   2983 O O   . GLN B 1 218 ? 107.00600 114.86600 144.32300 1.000 34.72376 ? 218 GLN B O   1 
ATOM   2984 C CB  . GLN B 1 218 ? 107.57500 111.96600 144.67200 1.000 34.72376 ? 218 GLN B CB  1 
ATOM   2985 C CG  . GLN B 1 218 ? 107.27100 110.47700 144.57200 1.000 34.72376 ? 218 GLN B CG  1 
ATOM   2986 C CD  . GLN B 1 218 ? 106.98600 109.83600 145.90900 1.000 34.72376 ? 218 GLN B CD  1 
ATOM   2987 O OE1 . GLN B 1 218 ? 105.96600 109.17700 146.08700 1.000 34.72376 ? 218 GLN B OE1 1 
ATOM   2988 N NE2 . GLN B 1 218 ? 107.88700 110.02400 146.85800 1.000 34.72376 ? 218 GLN B NE2 1 
ATOM   2989 N N   . LEU B 1 219 ? 107.13800 114.85400 146.56900 1.000 37.50730 ? 219 LEU B N   1 
ATOM   2990 C CA  . LEU B 1 219 ? 107.52800 116.24900 146.69100 1.000 37.50730 ? 219 LEU B CA  1 
ATOM   2991 C C   . LEU B 1 219 ? 109.04000 116.36800 146.84100 1.000 37.50730 ? 219 LEU B C   1 
ATOM   2992 O O   . LEU B 1 219 ? 109.75500 115.38100 147.01400 1.000 37.50730 ? 219 LEU B O   1 
ATOM   2993 C CB  . LEU B 1 219 ? 106.81400 116.89900 147.87600 1.000 37.50730 ? 219 LEU B CB  1 
ATOM   2994 C CG  . LEU B 1 219 ? 105.29500 116.98500 147.74100 1.000 37.50730 ? 219 LEU B CG  1 
ATOM   2995 C CD1 . LEU B 1 219 ? 104.68800 117.61900 148.97500 1.000 37.50730 ? 219 LEU B CD1 1 
ATOM   2996 C CD2 . LEU B 1 219 ? 104.91700 117.76000 146.49600 1.000 37.50730 ? 219 LEU B CD2 1 
ATOM   2997 N N   . SER B 1 220 ? 109.52200 117.61200 146.77100 1.000 40.03113 ? 220 SER B N   1 
ATOM   2998 C CA  . SER B 1 220 ? 110.95600 117.87200 146.85400 1.000 40.03113 ? 220 SER B CA  1 
ATOM   2999 C C   . SER B 1 220 ? 111.54200 117.43200 148.18900 1.000 40.03113 ? 220 SER B C   1 
ATOM   3000 O O   . SER B 1 220 ? 112.73200 117.11300 148.26800 1.000 40.03113 ? 220 SER B O   1 
ATOM   3001 C CB  . SER B 1 220 ? 111.23100 119.35400 146.62100 1.000 40.03113 ? 220 SER B CB  1 
ATOM   3002 O OG  . SER B 1 220 ? 110.69100 119.77600 145.38500 1.000 40.03113 ? 220 SER B OG  1 
ATOM   3003 N N   . THR B 1 221 ? 110.72800 117.40700 149.24600 1.000 43.69804 ? 221 THR B N   1 
ATOM   3004 C CA  . THR B 1 221 ? 111.19600 116.87700 150.52000 1.000 43.69804 ? 221 THR B CA  1 
ATOM   3005 C C   . THR B 1 221 ? 111.32400 115.36100 150.48300 1.000 43.69804 ? 221 THR B C   1 
ATOM   3006 O O   . THR B 1 221 ? 112.06300 114.78400 151.28700 1.000 43.69804 ? 221 THR B O   1 
ATOM   3007 C CB  . THR B 1 221 ? 110.25600 117.30300 151.64500 1.000 43.69804 ? 221 THR B CB  1 
ATOM   3008 O OG1 . THR B 1 221 ? 108.89700 117.13100 151.22600 1.000 43.69804 ? 221 THR B OG1 1 
ATOM   3009 C CG2 . THR B 1 221 ? 110.48800 118.75900 151.99900 1.000 43.69804 ? 221 THR B CG2 1 
ATOM   3010 N N   . ASP B 1 222 ? 110.61700 114.70200 149.56600 1.000 42.95759 ? 222 ASP B N   1 
ATOM   3011 C CA  . ASP B 1 222 ? 110.71400 113.25200 149.45100 1.000 42.95759 ? 222 ASP B CA  1 
ATOM   3012 C C   . ASP B 1 222 ? 111.89500 112.84700 148.57900 1.000 42.95759 ? 222 ASP B C   1 
ATOM   3013 O O   . ASP B 1 222 ? 112.52400 111.80900 148.80900 1.000 42.95759 ? 222 ASP B O   1 
ATOM   3014 C CB  . ASP B 1 222 ? 109.41600 112.68500 148.87500 1.000 42.95759 ? 222 ASP B CB  1 
ATOM   3015 C CG  . ASP B 1 222 ? 108.21500 112.98000 149.74000 1.000 42.95759 ? 222 ASP B CG  1 
ATOM   3016 O OD1 . ASP B 1 222 ? 108.39600 113.22200 150.95200 1.000 42.95759 ? 222 ASP B OD1 1 
ATOM   3017 O OD2 . ASP B 1 222 ? 107.08800 112.99200 149.20100 1.000 42.95759 ? 222 ASP B OD2 1 
ATOM   3018 N N   . THR B 1 223 ? 112.20100 113.65000 147.56100 1.000 37.29286 ? 223 THR B N   1 
ATOM   3019 C CA  . THR B 1 223 ? 113.14700 113.25800 146.52800 1.000 37.29286 ? 223 THR B CA  1 
ATOM   3020 C C   . THR B 1 223 ? 114.44500 114.05000 146.54900 1.000 37.29286 ? 223 THR B C   1 
ATOM   3021 O O   . THR B 1 223 ? 115.47300 113.52800 146.10900 1.000 37.29286 ? 223 THR B O   1 
ATOM   3022 C CB  . THR B 1 223 ? 112.50500 113.40200 145.14100 1.000 37.29286 ? 223 THR B CB  1 
ATOM   3023 O OG1 . THR B 1 223 ? 112.31600 114.78800 144.83900 1.000 37.29286 ? 223 THR B OG1 1 
ATOM   3024 C CG2 . THR B 1 223 ? 111.16600 112.70500 145.10100 1.000 37.29286 ? 223 THR B CG2 1 
ATOM   3025 N N   . GLY B 1 224 ? 114.42600 115.28600 147.04100 1.000 38.37740 ? 224 GLY B N   1 
ATOM   3026 C CA  . GLY B 1 224 ? 115.58400 116.14500 146.99400 1.000 38.37740 ? 224 GLY B CA  1 
ATOM   3027 C C   . GLY B 1 224 ? 115.69600 116.98900 145.74600 1.000 38.37740 ? 224 GLY B C   1 
ATOM   3028 O O   . GLY B 1 224 ? 116.56000 117.87000 145.69100 1.000 38.37740 ? 224 GLY B O   1 
ATOM   3029 N N   . VAL B 1 225 ? 114.85100 116.75800 144.74800 1.000 37.57340 ? 225 VAL B N   1 
ATOM   3030 C CA  . VAL B 1 225 ? 114.86400 117.53900 143.51900 1.000 37.57340 ? 225 VAL B CA  1 
ATOM   3031 C C   . VAL B 1 225 ? 113.97400 118.75700 143.73900 1.000 37.57340 ? 225 VAL B C   1 
ATOM   3032 O O   . VAL B 1 225 ? 112.75100 118.63300 143.83400 1.000 37.57340 ? 225 VAL B O   1 
ATOM   3033 C CB  . VAL B 1 225 ? 114.39000 116.71000 142.32000 1.000 37.57340 ? 225 VAL B CB  1 
ATOM   3034 C CG1 . VAL B 1 225 ? 114.53400 117.50400 141.03700 1.000 37.57340 ? 225 VAL B CG1 1 
ATOM   3035 C CG2 . VAL B 1 225 ? 115.16400 115.41600 142.23800 1.000 37.57340 ? 225 VAL B CG2 1 
ATOM   3036 N N   . GLU B 1 226 ? 114.58700 119.93300 143.81400 1.000 41.46862 ? 226 GLU B N   1 
ATOM   3037 C CA  . GLU B 1 226 ? 113.84400 121.14900 144.10900 1.000 41.46862 ? 226 GLU B CA  1 
ATOM   3038 C C   . GLU B 1 226 ? 112.99200 121.57300 142.92300 1.000 41.46862 ? 226 GLU B C   1 
ATOM   3039 O O   . GLU B 1 226 ? 113.37300 121.38500 141.76500 1.000 41.46862 ? 226 GLU B O   1 
ATOM   3040 C CB  . GLU B 1 226 ? 114.80100 122.28100 144.49500 1.000 41.46862 ? 226 GLU B CB  1 
ATOM   3041 C CG  . GLU B 1 226 ? 115.93900 122.01000 145.52200 1.000 41.46862 ? 226 GLU B CG  1 
ATOM   3042 C CD  . GLU B 1 226 ? 115.58800 121.26100 146.83100 1.000 41.46862 ? 226 GLU B CD  1 
ATOM   3043 O OE1 . GLU B 1 226 ? 116.36500 121.43900 147.79200 1.000 41.46862 ? 226 GLU B OE1 1 
ATOM   3044 O OE2 . GLU B 1 226 ? 114.60000 120.50600 146.94600 1.000 41.46862 ? 226 GLU B OE2 1 
ATOM   3045 N N   . HIS B 1 227 ? 111.82100 122.13500 143.23400 1.000 41.20200 ? 227 HIS B N   1 
ATOM   3046 C CA  . HIS B 1 227 ? 110.88300 122.72200 142.27700 1.000 41.20200 ? 227 HIS B CA  1 
ATOM   3047 C C   . HIS B 1 227 ? 110.27400 121.69000 141.33700 1.000 41.20200 ? 227 HIS B C   1 
ATOM   3048 O O   . HIS B 1 227 ? 109.77700 122.04500 140.26700 1.000 41.20200 ? 227 HIS B O   1 
ATOM   3049 C CB  . HIS B 1 227 ? 111.53900 123.84400 141.46000 1.000 41.20200 ? 227 HIS B CB  1 
ATOM   3050 C CG  . HIS B 1 227 ? 112.22300 124.88100 142.29200 1.000 41.20200 ? 227 HIS B CG  1 
ATOM   3051 N ND1 . HIS B 1 227 ? 111.94500 125.06900 143.62800 1.000 41.20200 ? 227 HIS B ND1 1 
ATOM   3052 C CD2 . HIS B 1 227 ? 113.19300 125.77100 141.98100 1.000 41.20200 ? 227 HIS B CD2 1 
ATOM   3053 C CE1 . HIS B 1 227 ? 112.70500 126.03900 144.10100 1.000 41.20200 ? 227 HIS B CE1 1 
ATOM   3054 N NE2 . HIS B 1 227 ? 113.47200 126.48200 143.12200 1.000 41.20200 ? 227 HIS B NE2 1 
ATOM   3055 N N   . VAL B 1 228 ? 110.30200 120.41200 141.70200 1.000 32.91706 ? 228 VAL B N   1 
ATOM   3056 C CA  . VAL B 1 228 ? 109.77600 119.34500 140.86100 1.000 32.91706 ? 228 VAL B CA  1 
ATOM   3057 C C   . VAL B 1 228 ? 108.89100 118.43900 141.70500 1.000 32.91706 ? 228 VAL B C   1 
ATOM   3058 O O   . VAL B 1 228 ? 109.25100 118.07400 142.82800 1.000 32.91706 ? 228 VAL B O   1 
ATOM   3059 C CB  . VAL B 1 228 ? 110.90600 118.53300 140.18700 1.000 32.91706 ? 228 VAL B CB  1 
ATOM   3060 C CG1 . VAL B 1 228 ? 110.33100 117.45600 139.32200 1.000 32.91706 ? 228 VAL B CG1 1 
ATOM   3061 C CG2 . VAL B 1 228 ? 111.79900 119.42700 139.34400 1.000 32.91706 ? 228 VAL B CG2 1 
ATOM   3062 N N   . THR B 1 229 ? 107.72700 118.08600 141.16700 1.000 29.50779 ? 229 THR B N   1 
ATOM   3063 C CA  . THR B 1 229 ? 106.82800 117.11200 141.76500 1.000 29.50779 ? 229 THR B CA  1 
ATOM   3064 C C   . THR B 1 229 ? 106.73300 115.90500 140.84200 1.000 29.50779 ? 229 THR B C   1 
ATOM   3065 O O   . THR B 1 229 ? 106.78900 116.04800 139.62100 1.000 29.50779 ? 229 THR B O   1 
ATOM   3066 C CB  . THR B 1 229 ? 105.43300 117.72300 142.00000 1.000 29.50779 ? 229 THR B CB  1 
ATOM   3067 O OG1 . THR B 1 229 ? 105.56200 118.95100 142.71900 1.000 29.50779 ? 229 THR B OG1 1 
ATOM   3068 C CG2 . THR B 1 229 ? 104.55300 116.79000 142.80500 1.000 29.50779 ? 229 THR B CG2 1 
ATOM   3069 N N   . PHE B 1 230 ? 106.60700 114.71500 141.41600 1.000 27.28454 ? 230 PHE B N   1 
ATOM   3070 C CA  . PHE B 1 230 ? 106.41500 113.49500 140.64400 1.000 27.28454 ? 230 PHE B CA  1 
ATOM   3071 C C   . PHE B 1 230 ? 105.09000 112.85400 141.02900 1.000 27.28454 ? 230 PHE B C   1 
ATOM   3072 O O   . PHE B 1 230 ? 104.87300 112.52100 142.19600 1.000 27.28454 ? 230 PHE B O   1 
ATOM   3073 C CB  . PHE B 1 230 ? 107.57300 112.52300 140.86000 1.000 27.28454 ? 230 PHE B CB  1 
ATOM   3074 C CG  . PHE B 1 230 ? 108.90600 113.09300 140.50300 1.000 27.28454 ? 230 PHE B CG  1 
ATOM   3075 C CD1 . PHE B 1 230 ? 109.33100 113.11300 139.18900 1.000 27.28454 ? 230 PHE B CD1 1 
ATOM   3076 C CD2 . PHE B 1 230 ? 109.73300 113.61800 141.47700 1.000 27.28454 ? 230 PHE B CD2 1 
ATOM   3077 C CE1 . PHE B 1 230 ? 110.54900 113.64400 138.85700 1.000 27.28454 ? 230 PHE B CE1 1 
ATOM   3078 C CE2 . PHE B 1 230 ? 110.95200 114.14500 141.14500 1.000 27.28454 ? 230 PHE B CE2 1 
ATOM   3079 C CZ  . PHE B 1 230 ? 111.36200 114.15300 139.83400 1.000 27.28454 ? 230 PHE B CZ  1 
ATOM   3080 N N   . PHE B 1 231 ? 104.21200 112.68500 140.04900 1.000 26.08027 ? 231 PHE B N   1 
ATOM   3081 C CA  . PHE B 1 231 ? 102.93100 112.02200 140.23700 1.000 26.08027 ? 231 PHE B CA  1 
ATOM   3082 C C   . PHE B 1 231 ? 103.03900 110.61700 139.66700 1.000 26.08027 ? 231 PHE B C   1 
ATOM   3083 O O   . PHE B 1 231 ? 103.33000 110.44400 138.48100 1.000 26.08027 ? 231 PHE B O   1 
ATOM   3084 C CB  . PHE B 1 231 ? 101.80600 112.80100 139.55600 1.000 26.08027 ? 231 PHE B CB  1 
ATOM   3085 C CG  . PHE B 1 231 ? 101.67300 114.21200 140.03900 1.000 26.08027 ? 231 PHE B CG  1 
ATOM   3086 C CD1 . PHE B 1 231 ? 100.96200 114.49700 141.18900 1.000 26.08027 ? 231 PHE B CD1 1 
ATOM   3087 C CD2 . PHE B 1 231 ? 102.26300 115.25300 139.34900 1.000 26.08027 ? 231 PHE B CD2 1 
ATOM   3088 C CE1 . PHE B 1 231 ? 100.84000 115.79200 141.63700 1.000 26.08027 ? 231 PHE B CE1 1 
ATOM   3089 C CE2 . PHE B 1 231 ? 102.14000 116.54600 139.79200 1.000 26.08027 ? 231 PHE B CE2 1 
ATOM   3090 C CZ  . PHE B 1 231 ? 101.42800 116.81700 140.93800 1.000 26.08027 ? 231 PHE B CZ  1 
ATOM   3091 N N   . ILE B 1 232 ? 102.80900 109.62200 140.50800 1.000 27.02028 ? 232 ILE B N   1 
ATOM   3092 C CA  . ILE B 1 232 ? 103.01500 108.22600 140.15300 1.000 27.02028 ? 232 ILE B CA  1 
ATOM   3093 C C   . ILE B 1 232 ? 101.65000 107.57200 140.02800 1.000 27.02028 ? 232 ILE B C   1 
ATOM   3094 O O   . ILE B 1 232 ? 100.83200 107.64900 140.94800 1.000 27.02028 ? 232 ILE B O   1 
ATOM   3095 C CB  . ILE B 1 232 ? 103.90100 107.51300 141.18400 1.000 27.02028 ? 232 ILE B CB  1 
ATOM   3096 C CG1 . ILE B 1 232 ? 105.26600 108.19800 141.24200 1.000 27.02028 ? 232 ILE B CG1 1 
ATOM   3097 C CG2 . ILE B 1 232 ? 104.03900 106.04600 140.85000 1.000 27.02028 ? 232 ILE B CG2 1 
ATOM   3098 C CD1 . ILE B 1 232 ? 106.21500 107.60400 142.23400 1.000 27.02028 ? 232 ILE B CD1 1 
ATOM   3099 N N   . TYR B 1 233 ? 101.39800 106.94900 138.88300 1.000 26.89423 ? 233 TYR B N   1 
ATOM   3100 C CA  . TYR B 1 233 ? 100.11800 106.34000 138.56600 1.000 26.89423 ? 233 TYR B CA  1 
ATOM   3101 C C   . TYR B 1 233 ? 100.31400 104.84700 138.38900 1.000 26.89423 ? 233 TYR B C   1 
ATOM   3102 O O   . TYR B 1 233 ? 101.21200 104.41800 137.66300 1.000 26.89423 ? 233 TYR B O   1 
ATOM   3103 C CB  . TYR B 1 233 ? 99.52300  106.93200 137.28800 1.000 26.89423 ? 233 TYR B CB  1 
ATOM   3104 C CG  . TYR B 1 233 ? 99.00400  108.33600 137.42700 1.000 26.89423 ? 233 TYR B CG  1 
ATOM   3105 C CD1 . TYR B 1 233 ? 97.64800  108.58000 137.56400 1.000 26.89423 ? 233 TYR B CD1 1 
ATOM   3106 C CD2 . TYR B 1 233 ? 99.86800  109.42200 137.40300 1.000 26.89423 ? 233 TYR B CD2 1 
ATOM   3107 C CE1 . TYR B 1 233 ? 97.16800  109.85900 137.68600 1.000 26.89423 ? 233 TYR B CE1 1 
ATOM   3108 C CE2 . TYR B 1 233 ? 99.39600  110.70300 137.52400 1.000 26.89423 ? 233 TYR B CE2 1 
ATOM   3109 C CZ  . TYR B 1 233 ? 98.04500  110.91700 137.66500 1.000 26.89423 ? 233 TYR B CZ  1 
ATOM   3110 O OH  . TYR B 1 233 ? 97.56800  112.19200 137.78800 1.000 26.89423 ? 233 TYR B OH  1 
ATOM   3111 N N   . ASN B 1 234 ? 99.46800  104.06900 139.04400 1.000 31.22110 ? 234 ASN B N   1 
ATOM   3112 C CA  . ASN B 1 234 ? 99.45100  102.62400 138.91300 1.000 31.22110 ? 234 ASN B CA  1 
ATOM   3113 C C   . ASN B 1 234 ? 98.32500  102.22300 137.97100 1.000 31.22110 ? 234 ASN B C   1 
ATOM   3114 O O   . ASN B 1 234 ? 97.22300  102.76600 138.04600 1.000 31.22110 ? 234 ASN B O   1 
ATOM   3115 C CB  . ASN B 1 234 ? 99.26500  101.95900 140.27800 1.000 31.22110 ? 234 ASN B CB  1 
ATOM   3116 C CG  . ASN B 1 234 ? 99.49200  100.47100 140.23200 1.000 31.22110 ? 234 ASN B CG  1 
ATOM   3117 O OD1 . ASN B 1 234 ? 100.47700 100.00200 139.67500 1.000 31.22110 ? 234 ASN B OD1 1 
ATOM   3118 N ND2 . ASN B 1 234 ? 98.56600  99.71600  140.79400 1.000 31.22110 ? 234 ASN B ND2 1 
ATOM   3119 N N   . LYS B 1 235 ? 98.61100  101.27800 137.08100 1.000 32.27907 ? 235 LYS B N   1 
ATOM   3120 C CA  . LYS B 1 235 ? 97.61400  100.81700 136.12400 1.000 32.27907 ? 235 LYS B CA  1 
ATOM   3121 C C   . LYS B 1 235 ? 96.46600  100.11800 136.83500 1.000 32.27907 ? 235 LYS B C   1 
ATOM   3122 O O   . LYS B 1 235 ? 96.68100  99.24500  137.67900 1.000 32.27907 ? 235 LYS B O   1 
ATOM   3123 C CB  . LYS B 1 235 ? 98.24900  99.87400  135.10600 1.000 32.27907 ? 235 LYS B CB  1 
ATOM   3124 C CG  . LYS B 1 235 ? 97.35500  99.53500  133.93600 1.000 32.27907 ? 235 LYS B CG  1 
ATOM   3125 C CD  . LYS B 1 235 ? 98.14500  98.95200  132.78900 1.000 32.27907 ? 235 LYS B CD  1 
ATOM   3126 C CE  . LYS B 1 235 ? 97.55300  97.65000  132.31400 1.000 32.27907 ? 235 LYS B CE  1 
ATOM   3127 N NZ  . LYS B 1 235 ? 96.27300  97.85400  131.59300 1.000 32.27907 ? 235 LYS B NZ  1 
ATOM   3128 N N   . ILE B 1 236 ? 95.24700  100.50500 136.49300 1.000 36.06047 ? 236 ILE B N   1 
ATOM   3129 C CA  . ILE B 1 236 ? 94.05800  99.87100  137.04300 1.000 36.06047 ? 236 ILE B CA  1 
ATOM   3130 C C   . ILE B 1 236 ? 93.83100  98.55500  136.31400 1.000 36.06047 ? 236 ILE B C   1 
ATOM   3131 O O   . ILE B 1 236 ? 93.78300  98.51200  135.08100 1.000 36.06047 ? 236 ILE B O   1 
ATOM   3132 C CB  . ILE B 1 236 ? 92.84000  100.80000 136.91800 1.000 36.06047 ? 236 ILE B CB  1 
ATOM   3133 C CG1 . ILE B 1 236 ? 93.06400  102.08000 137.72100 1.000 36.06047 ? 236 ILE B CG1 1 
ATOM   3134 C CG2 . ILE B 1 236 ? 91.58500  100.10000 137.39200 1.000 36.06047 ? 236 ILE B CG2 1 
ATOM   3135 C CD1 . ILE B 1 236 ? 92.14300  103.20800 137.34600 1.000 36.06047 ? 236 ILE B CD1 1 
ATOM   3136 N N   . VAL B 1 237 ? 93.70700  97.47500  137.07300 1.000 46.26520 ? 237 VAL B N   1 
ATOM   3137 C CA  . VAL B 1 237 ? 93.53200  96.14300  136.51200 1.000 46.26520 ? 237 VAL B CA  1 
ATOM   3138 C C   . VAL B 1 237 ? 92.06900  95.75100  136.65400 1.000 46.26520 ? 237 VAL B C   1 
ATOM   3139 O O   . VAL B 1 237 ? 91.46700  95.92000  137.72100 1.000 46.26520 ? 237 VAL B O   1 
ATOM   3140 C CB  . VAL B 1 237 ? 94.46600  95.12200  137.17900 1.000 46.26520 ? 237 VAL B CB  1 
ATOM   3141 C CG1 . VAL B 1 237 ? 95.87900  95.32000  136.68000 1.000 46.26520 ? 237 VAL B CG1 1 
ATOM   3142 C CG2 . VAL B 1 237 ? 94.42900  95.26100  138.68600 1.000 46.26520 ? 237 VAL B CG2 1 
ATOM   3143 N N   . ASP B 1 238 ? 91.49000  95.25600  135.56600 1.000 57.60959 ? 238 ASP B N   1 
ATOM   3144 C CA  . ASP B 1 238 ? 90.08300  94.88600  135.54000 1.000 57.60959 ? 238 ASP B CA  1 
ATOM   3145 C C   . ASP B 1 238 ? 89.90000  93.44300  135.08400 1.000 57.60959 ? 238 ASP B C   1 
ATOM   3146 O O   . ASP B 1 238 ? 89.99900  92.51200  135.88300 1.000 57.60959 ? 238 ASP B O   1 
ATOM   3147 C CB  . ASP B 1 238 ? 89.30300  95.83200  134.62700 1.000 57.60959 ? 238 ASP B CB  1 
ATOM   3148 C CG  . ASP B 1 238 ? 90.05800  96.16800  133.35600 1.000 57.60959 ? 238 ASP B CG  1 
ATOM   3149 O OD1 . ASP B 1 238 ? 91.23400  95.76800  133.23500 1.000 57.60959 ? 238 ASP B OD1 1 
ATOM   3150 O OD2 . ASP B 1 238 ? 89.47300  96.83400  132.47700 1.000 57.60959 ? 238 ASP B OD2 1 
ATOM   3151 N N   . PHE C 2 24  ? 81.16500  103.08600 113.29500 1.000 61.74300 ? 25  PHE C N   1 
ATOM   3152 C CA  . PHE C 2 24  ? 82.61500  103.22900 113.30000 1.000 61.74300 ? 25  PHE C CA  1 
ATOM   3153 C C   . PHE C 2 24  ? 83.22300  102.31400 114.35900 1.000 61.74300 ? 25  PHE C C   1 
ATOM   3154 O O   . PHE C 2 24  ? 84.34000  101.82400 114.19500 1.000 61.74300 ? 25  PHE C O   1 
ATOM   3155 C CB  . PHE C 2 24  ? 83.01200  104.69400 113.54500 1.000 61.74300 ? 25  PHE C CB  1 
ATOM   3156 C CG  . PHE C 2 24  ? 84.50100  104.93900 113.55200 1.000 61.74300 ? 25  PHE C CG  1 
ATOM   3157 C CD1 . PHE C 2 24  ? 85.15200  105.32500 112.39200 1.000 61.74300 ? 25  PHE C CD1 1 
ATOM   3158 C CD2 . PHE C 2 24  ? 85.24300  104.82000 114.72000 1.000 61.74300 ? 25  PHE C CD2 1 
ATOM   3159 C CE1 . PHE C 2 24  ? 86.51200  105.55500 112.38900 1.000 61.74300 ? 25  PHE C CE1 1 
ATOM   3160 C CE2 . PHE C 2 24  ? 86.60000  105.04300 114.71700 1.000 61.74300 ? 25  PHE C CE2 1 
ATOM   3161 C CZ  . PHE C 2 24  ? 87.23500  105.41500 113.55200 1.000 61.74300 ? 25  PHE C CZ  1 
ATOM   3162 N N   . SER C 2 25  ? 82.48300  102.09600 115.44800 1.000 69.14012 ? 26  SER C N   1 
ATOM   3163 C CA  . SER C 2 25  ? 82.99500  101.28400 116.54900 1.000 69.14012 ? 26  SER C CA  1 
ATOM   3164 C C   . SER C 2 25  ? 83.19600  99.83600  116.12100 1.000 69.14012 ? 26  SER C C   1 
ATOM   3165 O O   . SER C 2 25  ? 84.18800  99.19600  116.49400 1.000 69.14012 ? 26  SER C O   1 
ATOM   3166 C CB  . SER C 2 25  ? 82.04700  101.36500 117.74400 1.000 69.14012 ? 26  SER C CB  1 
ATOM   3167 O OG  . SER C 2 25  ? 82.56800  100.65300 118.85300 1.000 69.14012 ? 26  SER C OG  1 
ATOM   3168 N N   . LYS C 2 26  ? 82.25600  99.30100  115.33900 1.000 71.21229 ? 27  LYS C N   1 
ATOM   3169 C CA  . LYS C 2 26  ? 82.36100  97.92900  114.85600 1.000 71.21229 ? 27  LYS C CA  1 
ATOM   3170 C C   . LYS C 2 26  ? 83.58500  97.75700  113.96400 1.000 71.21229 ? 27  LYS C C   1 
ATOM   3171 O O   . LYS C 2 26  ? 84.31500  96.76700  114.07000 1.000 71.21229 ? 27  LYS C O   1 
ATOM   3172 C CB  . LYS C 2 26  ? 81.08400  97.54800  114.10500 1.000 71.21229 ? 27  LYS C CB  1 
ATOM   3173 C CG  . LYS C 2 26  ? 79.80700  97.82200  114.88100 1.000 71.21229 ? 27  LYS C CG  1 
ATOM   3174 C CD  . LYS C 2 26  ? 78.57500  97.47100  114.06400 1.000 71.21229 ? 27  LYS C CD  1 
ATOM   3175 C CE  . LYS C 2 26  ? 77.30000  97.74500  114.84400 1.000 71.21229 ? 27  LYS C CE  1 
ATOM   3176 N NZ  . LYS C 2 26  ? 76.08300  97.41800  114.05100 1.000 71.21229 ? 27  LYS C NZ  1 
ATOM   3177 N N   . LEU C 2 27  ? 83.83000  98.73200  113.08700 1.000 68.12306 ? 28  LEU C N   1 
ATOM   3178 C CA  . LEU C 2 27  ? 84.99800  98.66800  112.21700 1.000 68.12306 ? 28  LEU C CA  1 
ATOM   3179 C C   . LEU C 2 27  ? 86.29600  98.72500  113.01200 1.000 68.12306 ? 28  LEU C C   1 
ATOM   3180 O O   . LEU C 2 27  ? 87.25000  98.02300  112.67700 1.000 68.12306 ? 28  LEU C O   1 
ATOM   3181 C CB  . LEU C 2 27  ? 84.95100  99.80100  111.19300 1.000 68.12306 ? 28  LEU C CB  1 
ATOM   3182 C CG  . LEU C 2 27  ? 84.21300  99.50100  109.88800 1.000 68.12306 ? 28  LEU C CG  1 
ATOM   3183 C CD1 . LEU C 2 27  ? 83.60200  100.77100 109.31800 1.000 68.12306 ? 28  LEU C CD1 1 
ATOM   3184 C CD2 . LEU C 2 27  ? 85.14600  98.84900  108.88100 1.000 68.12306 ? 28  LEU C CD2 1 
ATOM   3185 N N   . ARG C 2 28  ? 86.34500  99.53800  114.06700 1.000 60.93581 ? 29  ARG C N   1 
ATOM   3186 C CA  . ARG C 2 28  ? 87.52800  99.60300  114.92200 1.000 60.93581 ? 29  ARG C CA  1 
ATOM   3187 C C   . ARG C 2 28  ? 87.75900  98.27900  115.64700 1.000 60.93581 ? 29  ARG C C   1 
ATOM   3188 O O   . ARG C 2 28  ? 88.89700  97.79100  115.74300 1.000 60.93581 ? 29  ARG C O   1 
ATOM   3189 C CB  . ARG C 2 28  ? 87.35400  100.76500 115.90200 1.000 60.93581 ? 29  ARG C CB  1 
ATOM   3190 C CG  . ARG C 2 28  ? 88.26400  100.81700 117.11700 1.000 60.93581 ? 29  ARG C CG  1 
ATOM   3191 C CD  . ARG C 2 28  ? 88.11900  102.19900 117.74400 1.000 60.93581 ? 29  ARG C CD  1 
ATOM   3192 N NE  . ARG C 2 28  ? 87.61700  102.15600 119.11500 1.000 60.93581 ? 29  ARG C NE  1 
ATOM   3193 C CZ  . ARG C 2 28  ? 88.37400  102.27800 120.19900 1.000 60.93581 ? 29  ARG C CZ  1 
ATOM   3194 N NH1 . ARG C 2 28  ? 89.67400  102.49300 120.08200 1.000 60.93581 ? 29  ARG C NH1 1 
ATOM   3195 N NH2 . ARG C 2 28  ? 87.82000  102.22800 121.40200 1.000 60.93581 ? 29  ARG C NH2 1 
ATOM   3196 N N   . GLU C 2 29  ? 86.67600  97.67500  116.14800 1.000 70.37682 ? 30  GLU C N   1 
ATOM   3197 C CA  . GLU C 2 29  ? 86.77600  96.37700  116.80800 1.000 70.37682 ? 30  GLU C CA  1 
ATOM   3198 C C   . GLU C 2 29  ? 87.22100  95.28800  115.83900 1.000 70.37682 ? 30  GLU C C   1 
ATOM   3199 O O   . GLU C 2 29  ? 87.90100  94.33700  116.23700 1.000 70.37682 ? 30  GLU C O   1 
ATOM   3200 C CB  . GLU C 2 29  ? 85.43700  96.00900  117.44500 1.000 70.37682 ? 30  GLU C CB  1 
ATOM   3201 C CG  . GLU C 2 29  ? 85.05700  96.87200  118.63200 1.000 70.37682 ? 30  GLU C CG  1 
ATOM   3202 C CD  . GLU C 2 29  ? 83.61400  96.68000  119.05300 1.000 70.37682 ? 30  GLU C CD  1 
ATOM   3203 O OE1 . GLU C 2 29  ? 82.87800  95.96100  118.34600 1.000 70.37682 ? 30  GLU C OE1 1 
ATOM   3204 O OE2 . GLU C 2 29  ? 83.21500  97.25000  120.09000 1.000 70.37682 ? 30  GLU C OE2 1 
ATOM   3205 N N   . GLN C 2 30  ? 86.82100  95.39000  114.57200 1.000 68.91385 ? 31  GLN C N   1 
ATOM   3206 C CA  . GLN C 2 30  ? 87.32200  94.46600  113.55800 1.000 68.91385 ? 31  GLN C CA  1 
ATOM   3207 C C   . GLN C 2 30  ? 88.79100  94.72800  113.23500 1.000 68.91385 ? 31  GLN C C   1 
ATOM   3208 O O   . GLN C 2 30  ? 89.56500  93.79500  112.99900 1.000 68.91385 ? 31  GLN C O   1 
ATOM   3209 C CB  . GLN C 2 30  ? 86.46300  94.55000  112.29100 1.000 68.91385 ? 31  GLN C CB  1 
ATOM   3210 C CG  . GLN C 2 30  ? 85.26200  93.58700  112.20800 1.000 68.91385 ? 31  GLN C CG  1 
ATOM   3211 C CD  . GLN C 2 30  ? 84.34200  93.59000  113.42000 1.000 68.91385 ? 31  GLN C CD  1 
ATOM   3212 O OE1 . GLN C 2 30  ? 83.32200  94.27700  113.43100 1.000 68.91385 ? 31  GLN C OE1 1 
ATOM   3213 N NE2 . GLN C 2 30  ? 84.67200  92.78300  114.42400 1.000 68.91385 ? 31  GLN C NE2 1 
ATOM   3214 N N   . LEU C 2 31  ? 89.19000  96.00100  113.21500 1.000 64.22327 ? 32  LEU C N   1 
ATOM   3215 C CA  . LEU C 2 31  ? 90.52300  96.35800  112.73800 1.000 64.22327 ? 32  LEU C CA  1 
ATOM   3216 C C   . LEU C 2 31  ? 91.60700  95.99500  113.74200 1.000 64.22327 ? 32  LEU C C   1 
ATOM   3217 O O   . LEU C 2 31  ? 92.72700  95.65000  113.34700 1.000 64.22327 ? 32  LEU C O   1 
ATOM   3218 C CB  . LEU C 2 31  ? 90.58700  97.85000  112.41600 1.000 64.22327 ? 32  LEU C CB  1 
ATOM   3219 C CG  . LEU C 2 31  ? 90.01900  98.30700  111.07500 1.000 64.22327 ? 32  LEU C CG  1 
ATOM   3220 C CD1 . LEU C 2 31  ? 90.33100  99.77500  110.84800 1.000 64.22327 ? 32  LEU C CD1 1 
ATOM   3221 C CD2 . LEU C 2 31  ? 90.56400  97.45200  109.94400 1.000 64.22327 ? 32  LEU C CD2 1 
ATOM   3222 N N   . GLY C 2 32  ? 91.31100  96.10200  115.03700 1.000 63.46884 ? 33  GLY C N   1 
ATOM   3223 C CA  . GLY C 2 32  ? 92.31000  95.87700  116.06400 1.000 63.46884 ? 33  GLY C CA  1 
ATOM   3224 C C   . GLY C 2 32  ? 93.01600  94.52700  116.03100 1.000 63.46884 ? 33  GLY C C   1 
ATOM   3225 O O   . GLY C 2 32  ? 94.22600  94.42700  115.75700 1.000 63.46884 ? 33  GLY C O   1 
ATOM   3226 N N   . PRO C 2 33  ? 92.26700  93.45700  116.32800 1.000 67.34073 ? 34  PRO C N   1 
ATOM   3227 C CA  . PRO C 2 33  ? 92.88200  92.12000  116.33300 1.000 67.34073 ? 34  PRO C CA  1 
ATOM   3228 C C   . PRO C 2 33  ? 93.40600  91.68200  114.98000 1.000 67.34073 ? 34  PRO C C   1 
ATOM   3229 O O   . PRO C 2 33  ? 94.34000  90.87700  114.93000 1.000 67.34073 ? 34  PRO C O   1 
ATOM   3230 C CB  . PRO C 2 33  ? 91.74200  91.21600  116.82300 1.000 67.34073 ? 34  PRO C CB  1 
ATOM   3231 C CG  . PRO C 2 33  ? 90.83400  92.12700  117.56500 1.000 67.34073 ? 34  PRO C CG  1 
ATOM   3232 C CD  . PRO C 2 33  ? 90.88100  93.41600  116.81700 1.000 67.34073 ? 34  PRO C CD  1 
ATOM   3233 N N   . VAL C 2 34  ? 92.83800  92.18600  113.88300 1.000 66.77027 ? 35  VAL C N   1 
ATOM   3234 C CA  . VAL C 2 34  ? 93.34100  91.83800  112.55500 1.000 66.77027 ? 35  VAL C CA  1 
ATOM   3235 C C   . VAL C 2 34  ? 94.77000  92.34400  112.38000 1.000 66.77027 ? 35  VAL C C   1 
ATOM   3236 O O   . VAL C 2 34  ? 95.66500  91.60100  111.95800 1.000 66.77027 ? 35  VAL C O   1 
ATOM   3237 C CB  . VAL C 2 34  ? 92.39900  92.39200  111.46900 1.000 66.77027 ? 35  VAL C CB  1 
ATOM   3238 C CG1 . VAL C 2 34  ? 93.13400  92.59400  110.15400 1.000 66.77027 ? 35  VAL C CG1 1 
ATOM   3239 C CG2 . VAL C 2 34  ? 91.21500  91.46500  111.28200 1.000 66.77027 ? 35  VAL C CG2 1 
ATOM   3240 N N   . THR C 2 35  ? 95.00700  93.60800  112.74400 1.000 64.72894 ? 36  THR C N   1 
ATOM   3241 C CA  . THR C 2 35  ? 96.34800  94.18200  112.68200 1.000 64.72894 ? 36  THR C CA  1 
ATOM   3242 C C   . THR C 2 35  ? 97.30300  93.44900  113.61800 1.000 64.72894 ? 36  THR C C   1 
ATOM   3243 O O   . THR C 2 35  ? 98.44000  93.11600  113.23800 1.000 64.72894 ? 36  THR C O   1 
ATOM   3244 C CB  . THR C 2 35  ? 96.28000  95.67000  113.03900 1.000 64.72894 ? 36  THR C CB  1 
ATOM   3245 O OG1 . THR C 2 35  ? 95.40600  96.34500  112.12700 1.000 64.72894 ? 36  THR C OG1 1 
ATOM   3246 C CG2 . THR C 2 35  ? 97.65400  96.30900  112.98000 1.000 64.72894 ? 36  THR C CG2 1 
ATOM   3247 N N   . GLN C 2 36  ? 96.84600  93.17500  114.84600 1.000 67.57734 ? 37  GLN C N   1 
ATOM   3248 C CA  . GLN C 2 36  ? 97.70300  92.49300  115.81300 1.000 67.57734 ? 37  GLN C CA  1 
ATOM   3249 C C   . GLN C 2 36  ? 98.09100  91.09900  115.33300 1.000 67.57734 ? 37  GLN C C   1 
ATOM   3250 O O   . GLN C 2 36  ? 99.26200  90.70800  115.42000 1.000 67.57734 ? 37  GLN C O   1 
ATOM   3251 C CB  . GLN C 2 36  ? 97.00200  92.41500  117.17200 1.000 67.57734 ? 37  GLN C CB  1 
ATOM   3252 C CG  . GLN C 2 36  ? 97.79900  91.92000  118.42200 1.000 67.57734 ? 37  GLN C CG  1 
ATOM   3253 C CD  . GLN C 2 36  ? 99.22000  92.48200  118.66500 1.000 67.57734 ? 37  GLN C CD  1 
ATOM   3254 O OE1 . GLN C 2 36  ? 99.88700  93.03400  117.79100 1.000 67.57734 ? 37  GLN C OE1 1 
ATOM   3255 N NE2 . GLN C 2 36  ? 99.67600  92.32500  119.90100 1.000 67.57734 ? 37  GLN C NE2 1 
ATOM   3256 N N   . GLU C 2 37  ? 97.12900  90.34800  114.79600 1.000 68.72263 ? 38  GLU C N   1 
ATOM   3257 C CA  . GLU C 2 37  ? 97.40200  88.98800  114.35400 1.000 68.72263 ? 38  GLU C CA  1 
ATOM   3258 C C   . GLU C 2 37  ? 98.25800  88.98700  113.09700 1.000 68.72263 ? 38  GLU C C   1 
ATOM   3259 O O   . GLU C 2 37  ? 99.07000  88.08000  112.89600 1.000 68.72263 ? 38  GLU C O   1 
ATOM   3260 C CB  . GLU C 2 37  ? 96.08700  88.22900  114.14000 1.000 68.72263 ? 38  GLU C CB  1 
ATOM   3261 C CG  . GLU C 2 37  ? 95.65100  88.04700  112.69100 1.000 68.72263 ? 38  GLU C CG  1 
ATOM   3262 C CD  . GLU C 2 37  ? 94.26200  87.45600  112.56200 1.000 68.72263 ? 38  GLU C CD  1 
ATOM   3263 O OE1 . GLU C 2 37  ? 93.63400  87.64500  111.49900 1.000 68.72263 ? 38  GLU C OE1 1 
ATOM   3264 O OE2 . GLU C 2 37  ? 93.79800  86.80500  113.52100 1.000 68.72263 ? 38  GLU C OE2 1 
ATOM   3265 N N   . PHE C 2 38  ? 98.11500  90.01300  112.24700 1.000 63.19134 ? 39  PHE C N   1 
ATOM   3266 C CA  . PHE C 2 38  ? 98.99200  90.10900  111.08700 1.000 63.19134 ? 39  PHE C CA  1 
ATOM   3267 C C   . PHE C 2 38  ? 100.43800 90.29800  111.51200 1.000 63.19134 ? 39  PHE C C   1 
ATOM   3268 O O   . PHE C 2 38  ? 101.34000 89.63600  110.98500 1.000 63.19134 ? 39  PHE C O   1 
ATOM   3269 C CB  . PHE C 2 38  ? 98.56200  91.25500  110.17200 1.000 63.19134 ? 39  PHE C CB  1 
ATOM   3270 C CG  . PHE C 2 38  ? 99.62600  91.66400  109.19200 1.000 63.19134 ? 39  PHE C CG  1 
ATOM   3271 C CD1 . PHE C 2 38  ? 99.88800  90.88800  108.07500 1.000 63.19134 ? 39  PHE C CD1 1 
ATOM   3272 C CD2 . PHE C 2 38  ? 100.37500 92.81400  109.39300 1.000 63.19134 ? 39  PHE C CD2 1 
ATOM   3273 C CE1 . PHE C 2 38  ? 100.87100 91.25100  107.17600 1.000 63.19134 ? 39  PHE C CE1 1 
ATOM   3274 C CE2 . PHE C 2 38  ? 101.36000 93.17800  108.50000 1.000 63.19134 ? 39  PHE C CE2 1 
ATOM   3275 C CZ  . PHE C 2 38  ? 101.60700 92.39700  107.38800 1.000 63.19134 ? 39  PHE C CZ  1 
ATOM   3276 N N   . TRP C 2 39  ? 100.68200 91.19400  112.47000 1.000 60.07895 ? 40  TRP C N   1 
ATOM   3277 C CA  . TRP C 2 39  ? 102.06400 91.42700  112.87400 1.000 60.07895 ? 40  TRP C CA  1 
ATOM   3278 C C   . TRP C 2 39  ? 102.62800 90.23400  113.64000 1.000 60.07895 ? 40  TRP C C   1 
ATOM   3279 O O   . TRP C 2 39  ? 103.80700 89.89000  113.48200 1.000 60.07895 ? 40  TRP C O   1 
ATOM   3280 C CB  . TRP C 2 39  ? 102.16700 92.71800  113.68100 1.000 60.07895 ? 40  TRP C CB  1 
ATOM   3281 C CG  . TRP C 2 39  ? 102.05600 93.92100  112.80200 1.000 60.07895 ? 40  TRP C CG  1 
ATOM   3282 C CD1 . TRP C 2 39  ? 101.03300 94.81900  112.76900 1.000 60.07895 ? 40  TRP C CD1 1 
ATOM   3283 C CD2 . TRP C 2 39  ? 102.98900 94.34000  111.79900 1.000 60.07895 ? 40  TRP C CD2 1 
ATOM   3284 N NE1 . TRP C 2 39  ? 101.27600 95.77800  111.82000 1.000 60.07895 ? 40  TRP C NE1 1 
ATOM   3285 C CE2 . TRP C 2 39  ? 102.47100 95.50700  111.21000 1.000 60.07895 ? 40  TRP C CE2 1 
ATOM   3286 C CE3 . TRP C 2 39  ? 104.21800 93.84600  111.34900 1.000 60.07895 ? 40  TRP C CE3 1 
ATOM   3287 C CZ2 . TRP C 2 39  ? 103.13600 96.18900  110.19500 1.000 60.07895 ? 40  TRP C CZ2 1 
ATOM   3288 C CZ3 . TRP C 2 39  ? 104.87400 94.52200  110.34200 1.000 60.07895 ? 40  TRP C CZ3 1 
ATOM   3289 C CH2 . TRP C 2 39  ? 104.33200 95.68000  109.77500 1.000 60.07895 ? 40  TRP C CH2 1 
ATOM   3290 N N   . ASP C 2 40  ? 101.79200 89.56400  114.44000 1.000 68.74390 ? 41  ASP C N   1 
ATOM   3291 C CA  . ASP C 2 40  ? 102.22900 88.34500  115.11500 1.000 68.74390 ? 41  ASP C CA  1 
ATOM   3292 C C   . ASP C 2 40  ? 102.58300 87.24900  114.11700 1.000 68.74390 ? 41  ASP C C   1 
ATOM   3293 O O   . ASP C 2 40  ? 103.61100 86.57500  114.26200 1.000 68.74390 ? 41  ASP C O   1 
ATOM   3294 C CB  . ASP C 2 40  ? 101.14400 87.86100  116.07500 1.000 68.74390 ? 41  ASP C CB  1 
ATOM   3295 C CG  . ASP C 2 40  ? 100.91900 88.81500  117.22900 1.000 68.74390 ? 41  ASP C CG  1 
ATOM   3296 O OD1 . ASP C 2 40  ? 101.78400 89.68200  117.46600 1.000 68.74390 ? 41  ASP C OD1 1 
ATOM   3297 O OD2 . ASP C 2 40  ? 99.87400  88.69500  117.90200 1.000 68.74390 ? 41  ASP C OD2 1 
ATOM   3298 N N   . ASN C 2 41  ? 101.75200 87.06300  113.08900 1.000 69.68303 ? 42  ASN C N   1 
ATOM   3299 C CA  . ASN C 2 41  ? 102.02100 86.04100  112.08400 1.000 69.68303 ? 42  ASN C CA  1 
ATOM   3300 C C   . ASN C 2 41  ? 103.27600 86.36800  111.28800 1.000 69.68303 ? 42  ASN C C   1 
ATOM   3301 O O   . ASN C 2 41  ? 104.06900 85.47600  110.97400 1.000 69.68303 ? 42  ASN C O   1 
ATOM   3302 C CB  . ASN C 2 41  ? 100.81500 85.88500  111.15700 1.000 69.68303 ? 42  ASN C CB  1 
ATOM   3303 C CG  . ASN C 2 41  ? 99.64400  85.19500  111.82900 1.000 69.68303 ? 42  ASN C CG  1 
ATOM   3304 O OD1 . ASN C 2 41  ? 99.72100  84.81800  112.99700 1.000 69.68303 ? 42  ASN C OD1 1 
ATOM   3305 N ND2 . ASN C 2 41  ? 98.54500  85.04300  111.10000 1.000 69.68303 ? 42  ASN C ND2 1 
ATOM   3306 N N   . LEU C 2 42  ? 103.47300 87.64700  110.95400 1.000 69.13523 ? 43  LEU C N   1 
ATOM   3307 C CA  . LEU C 2 42  ? 104.68600 88.04500  110.24800 1.000 69.13523 ? 43  LEU C CA  1 
ATOM   3308 C C   . LEU C 2 42  ? 105.92100 87.77200  111.09300 1.000 69.13523 ? 43  LEU C C   1 
ATOM   3309 O O   . LEU C 2 42  ? 106.95000 87.32200  110.57300 1.000 69.13523 ? 43  LEU C O   1 
ATOM   3310 C CB  . LEU C 2 42  ? 104.61500 89.52000  109.85900 1.000 69.13523 ? 43  LEU C CB  1 
ATOM   3311 C CG  . LEU C 2 42  ? 105.64100 89.99200  108.82700 1.000 69.13523 ? 43  LEU C CG  1 
ATOM   3312 C CD1 . LEU C 2 42  ? 105.61600 89.10400  107.59600 1.000 69.13523 ? 43  LEU C CD1 1 
ATOM   3313 C CD2 . LEU C 2 42  ? 105.40800 91.44300  108.44900 1.000 69.13523 ? 43  LEU C CD2 1 
ATOM   3314 N N   . GLU C 2 43  ? 105.82800 88.01200  112.40300 1.000 70.23163 ? 44  GLU C N   1 
ATOM   3315 C CA  . GLU C 2 43  ? 106.93000 87.67000  113.29600 1.000 70.23163 ? 44  GLU C CA  1 
ATOM   3316 C C   . GLU C 2 43  ? 107.20200 86.16800  113.29500 1.000 70.23163 ? 44  GLU C C   1 
ATOM   3317 O O   . GLU C 2 43  ? 108.36300 85.74100  113.25700 1.000 70.23163 ? 44  GLU C O   1 
ATOM   3318 C CB  . GLU C 2 43  ? 106.62200 88.15900  114.70800 1.000 70.23163 ? 44  GLU C CB  1 
ATOM   3319 C CG  . GLU C 2 43  ? 107.75100 87.95600  115.69700 1.000 70.23163 ? 44  GLU C CG  1 
ATOM   3320 C CD  . GLU C 2 43  ? 107.56900 88.78600  116.94300 1.000 70.23163 ? 44  GLU C CD  1 
ATOM   3321 O OE1 . GLU C 2 43  ? 106.60000 89.56700  116.98600 1.000 70.23163 ? 44  GLU C OE1 1 
ATOM   3322 O OE2 . GLU C 2 43  ? 108.39000 88.66600  117.87500 1.000 70.23163 ? 44  GLU C OE2 1 
ATOM   3323 N N   . LYS C 2 44  ? 106.14300 85.35200  113.33000 1.000 74.43528 ? 45  LYS C N   1 
ATOM   3324 C CA  . LYS C 2 44  ? 106.32800 83.90000  113.30500 1.000 74.43528 ? 45  LYS C CA  1 
ATOM   3325 C C   . LYS C 2 44  ? 107.01200 83.43600  112.02000 1.000 74.43528 ? 45  LYS C C   1 
ATOM   3326 O O   . LYS C 2 44  ? 107.93900 82.62000  112.06100 1.000 74.43528 ? 45  LYS C O   1 
ATOM   3327 C CB  . LYS C 2 44  ? 104.99000 83.17800  113.48400 1.000 74.43528 ? 45  LYS C CB  1 
ATOM   3328 C CG  . LYS C 2 44  ? 104.22500 83.50400  114.76100 1.000 74.43528 ? 45  LYS C CG  1 
ATOM   3329 C CD  . LYS C 2 44  ? 105.13900 83.58200  115.97400 1.000 74.43528 ? 45  LYS C CD  1 
ATOM   3330 C CE  . LYS C 2 44  ? 104.67400 84.64200  116.96000 1.000 74.43528 ? 45  LYS C CE  1 
ATOM   3331 N NZ  . LYS C 2 44  ? 104.57600 85.98900  116.33900 1.000 74.43528 ? 45  LYS C NZ  1 
ATOM   3332 N N   . GLU C 2 45  ? 106.57600 83.94900  110.86600 1.000 78.08239 ? 46  GLU C N   1 
ATOM   3333 C CA  . GLU C 2 45  ? 107.16000 83.47900  109.61000 1.000 78.08239 ? 46  GLU C CA  1 
ATOM   3334 C C   . GLU C 2 45  ? 108.54300 84.07300  109.35900 1.000 78.08239 ? 46  GLU C C   1 
ATOM   3335 O O   . GLU C 2 45  ? 109.31700 83.52700  108.56500 1.000 78.08239 ? 46  GLU C O   1 
ATOM   3336 C CB  . GLU C 2 45  ? 106.23900 83.76000  108.41900 1.000 78.08239 ? 46  GLU C CB  1 
ATOM   3337 C CG  . GLU C 2 45  ? 104.76100 83.58000  108.67000 1.000 78.08239 ? 46  GLU C CG  1 
ATOM   3338 C CD  . GLU C 2 45  ? 104.29100 82.16300  108.41300 1.000 78.08239 ? 46  GLU C CD  1 
ATOM   3339 O OE1 . GLU C 2 45  ? 103.43800 81.97200  107.52100 1.000 78.08239 ? 46  GLU C OE1 1 
ATOM   3340 O OE2 . GLU C 2 45  ? 104.77000 81.24000  109.10400 1.000 78.08239 ? 46  GLU C OE2 1 
ATOM   3341 N N   . THR C 2 46  ? 108.87900 85.18400  110.01100 1.000 80.37485 ? 47  THR C N   1 
ATOM   3342 C CA  . THR C 2 46  ? 110.19700 85.77100  109.80100 1.000 80.37485 ? 47  THR C CA  1 
ATOM   3343 C C   . THR C 2 46  ? 111.17600 85.52500  110.94500 1.000 80.37485 ? 47  THR C C   1 
ATOM   3344 O O   . THR C 2 46  ? 112.27700 86.08000  110.90900 1.000 80.37485 ? 47  THR C O   1 
ATOM   3345 C CB  . THR C 2 46  ? 110.07500 87.28100  109.56000 1.000 80.37485 ? 47  THR C CB  1 
ATOM   3346 O OG1 . THR C 2 46  ? 109.41900 87.89900  110.67400 1.000 80.37485 ? 47  THR C OG1 1 
ATOM   3347 C CG2 . THR C 2 46  ? 109.29300 87.55800  108.28300 1.000 80.37485 ? 47  THR C CG2 1 
ATOM   3348 N N   . GLU C 2 47  ? 110.80300 84.73400  111.95800 1.000 85.73022 ? 48  GLU C N   1 
ATOM   3349 C CA  . GLU C 2 47  ? 111.70400 84.48500  113.08500 1.000 85.73022 ? 48  GLU C CA  1 
ATOM   3350 C C   . GLU C 2 47  ? 113.02200 83.85500  112.64200 1.000 85.73022 ? 48  GLU C C   1 
ATOM   3351 O O   . GLU C 2 47  ? 114.10200 84.30300  113.05000 1.000 85.73022 ? 48  GLU C O   1 
ATOM   3352 C CB  . GLU C 2 47  ? 111.01200 83.59400  114.11700 1.000 85.73022 ? 48  GLU C CB  1 
ATOM   3353 C CG  . GLU C 2 47  ? 111.87900 83.22600  115.31100 1.000 85.73022 ? 48  GLU C CG  1 
ATOM   3354 C CD  . GLU C 2 47  ? 112.09100 84.38200  116.27100 1.000 85.73022 ? 48  GLU C CD  1 
ATOM   3355 O OE1 . GLU C 2 47  ? 111.30800 85.35300  116.22600 1.000 85.73022 ? 48  GLU C OE1 1 
ATOM   3356 O OE2 . GLU C 2 47  ? 113.04200 84.31700  117.07800 1.000 85.73022 ? 48  GLU C OE2 1 
ATOM   3357 N N   . GLY C 2 48  ? 112.95600 82.81700  111.80600 1.000 89.26041 ? 49  GLY C N   1 
ATOM   3358 C CA  . GLY C 2 48  ? 114.17500 82.15200  111.36900 1.000 89.26041 ? 49  GLY C CA  1 
ATOM   3359 C C   . GLY C 2 48  ? 115.06600 83.04600  110.52800 1.000 89.26041 ? 49  GLY C C   1 
ATOM   3360 O O   . GLY C 2 48  ? 116.28700 83.06600  110.70200 1.000 89.26041 ? 49  GLY C O   1 
ATOM   3361 N N   . LEU C 2 49  ? 114.46700 83.81000  109.61300 1.000 90.06938 ? 50  LEU C N   1 
ATOM   3362 C CA  . LEU C 2 49  ? 115.24700 84.71500  108.77600 1.000 90.06938 ? 50  LEU C CA  1 
ATOM   3363 C C   . LEU C 2 49  ? 115.88100 85.82800  109.60600 1.000 90.06938 ? 50  LEU C C   1 
ATOM   3364 O O   . LEU C 2 49  ? 117.03400 86.21200  109.36900 1.000 90.06938 ? 50  LEU C O   1 
ATOM   3365 C CB  . LEU C 2 49  ? 114.35400 85.28900  107.67800 1.000 90.06938 ? 50  LEU C CB  1 
ATOM   3366 C CG  . LEU C 2 49  ? 114.95900 86.25000  106.65800 1.000 90.06938 ? 50  LEU C CG  1 
ATOM   3367 C CD1 . LEU C 2 49  ? 115.99400 85.54300  105.80000 1.000 90.06938 ? 50  LEU C CD1 1 
ATOM   3368 C CD2 . LEU C 2 49  ? 113.86700 86.86200  105.80000 1.000 90.06938 ? 50  LEU C CD2 1 
ATOM   3369 N N   . ARG C 2 50  ? 115.15400 86.34100  110.60300 1.000 84.24308 ? 51  ARG C N   1 
ATOM   3370 C CA  . ARG C 2 50  ? 115.70400 87.38800  111.45600 1.000 84.24308 ? 51  ARG C CA  1 
ATOM   3371 C C   . ARG C 2 50  ? 116.81700 86.84500  112.34000 1.000 84.24308 ? 51  ARG C C   1 
ATOM   3372 O O   . ARG C 2 50  ? 117.75400 87.57300  112.69000 1.000 84.24308 ? 51  ARG C O   1 
ATOM   3373 C CB  . ARG C 2 50  ? 114.59700 88.00800  112.30400 1.000 84.24308 ? 51  ARG C CB  1 
ATOM   3374 C CG  . ARG C 2 50  ? 113.67200 88.91200  111.51900 1.000 84.24308 ? 51  ARG C CG  1 
ATOM   3375 C CD  . ARG C 2 50  ? 112.60500 89.50200  112.40900 1.000 84.24308 ? 51  ARG C CD  1 
ATOM   3376 N NE  . ARG C 2 50  ? 111.71900 88.49000  112.97100 1.000 84.24308 ? 51  ARG C NE  1 
ATOM   3377 C CZ  . ARG C 2 50  ? 111.65600 88.19000  114.26300 1.000 84.24308 ? 51  ARG C CZ  1 
ATOM   3378 N NH1 . ARG C 2 50  ? 112.42800 88.82500  115.13200 1.000 84.24308 ? 51  ARG C NH1 1 
ATOM   3379 N NH2 . ARG C 2 50  ? 110.81900 87.25800  114.68900 1.000 84.24308 ? 51  ARG C NH2 1 
ATOM   3380 N N   . GLN C 2 51  ? 116.72300 85.57100  112.72500 1.000 93.21906 ? 52  GLN C N   1 
ATOM   3381 C CA  . GLN C 2 51  ? 117.85700 84.91500  113.36500 1.000 93.21906 ? 52  GLN C CA  1 
ATOM   3382 C C   . GLN C 2 51  ? 119.03300 84.81000  112.40300 1.000 93.21906 ? 52  GLN C C   1 
ATOM   3383 O O   . GLN C 2 51  ? 120.19400 84.93100  112.81100 1.000 93.21906 ? 52  GLN C O   1 
ATOM   3384 C CB  . GLN C 2 51  ? 117.45300 83.52900  113.86600 1.000 93.21906 ? 52  GLN C CB  1 
ATOM   3385 C CG  . GLN C 2 51  ? 117.80700 83.26300  115.31800 1.000 93.21906 ? 52  GLN C CG  1 
ATOM   3386 C CD  . GLN C 2 51  ? 117.08600 84.19700  116.26800 1.000 93.21906 ? 52  GLN C CD  1 
ATOM   3387 O OE1 . GLN C 2 51  ? 115.85700 84.22900  116.30800 1.000 93.21906 ? 52  GLN C OE1 1 
ATOM   3388 N NE2 . GLN C 2 51  ? 117.84800 84.96300  117.04000 1.000 93.21906 ? 52  GLN C NE2 1 
ATOM   3389 N N   . GLU C 2 52  ? 118.74600 84.57600  111.11900 1.000 94.51533 ? 53  GLU C N   1 
ATOM   3390 C CA  . GLU C 2 52  ? 119.81000 84.46500  110.12400 1.000 94.51533 ? 53  GLU C CA  1 
ATOM   3391 C C   . GLU C 2 52  ? 120.55100 85.78600  109.93900 1.000 94.51533 ? 53  GLU C C   1 
ATOM   3392 O O   . GLU C 2 52  ? 121.76800 85.79300  109.72500 1.000 94.51533 ? 53  GLU C O   1 
ATOM   3393 C CB  . GLU C 2 52  ? 119.24800 83.96900  108.79100 1.000 94.51533 ? 53  GLU C CB  1 
ATOM   3394 C CG  . GLU C 2 52  ? 118.87400 82.49700  108.78800 1.000 94.51533 ? 53  GLU C CG  1 
ATOM   3395 C CD  . GLU C 2 52  ? 118.12100 82.08800  107.53800 1.000 94.51533 ? 53  GLU C CD  1 
ATOM   3396 O OE1 . GLU C 2 52  ? 117.95500 82.93600  106.63600 1.000 94.51533 ? 53  GLU C OE1 1 
ATOM   3397 O OE2 . GLU C 2 52  ? 117.69600 80.91600  107.45700 1.000 94.51533 ? 53  GLU C OE2 1 
ATOM   3398 N N   . MET C 2 53  ? 119.83800 86.92100  109.99400 1.000 96.23865 ? 54  MET C N   1 
ATOM   3399 C CA  . MET C 2 53  ? 120.56700 88.19100  109.95800 1.000 96.23865 ? 54  MET C CA  1 
ATOM   3400 C C   . MET C 2 53  ? 121.43200 88.39100  111.19700 1.000 96.23865 ? 54  MET C C   1 
ATOM   3401 O O   . MET C 2 53  ? 122.54400 88.92200  111.09200 1.000 96.23865 ? 54  MET C O   1 
ATOM   3402 C CB  . MET C 2 53  ? 119.65300 89.41400  109.80500 1.000 96.23865 ? 54  MET C CB  1 
ATOM   3403 C CG  . MET C 2 53  ? 119.19800 89.75100  108.38700 1.000 96.23865 ? 54  MET C CG  1 
ATOM   3404 S SD  . MET C 2 53  ? 117.56000 90.50800  108.26700 1.000 96.23865 ? 54  MET C SD  1 
ATOM   3405 C CE  . MET C 2 53  ? 116.46100 89.11300  108.26500 1.000 96.23865 ? 54  MET C CE  1 
ATOM   3406 N N   . SER C 2 54  ? 120.94900 87.99300  112.36800 1.000 97.23649 ? 55  SER C N   1 
ATOM   3407 C CA  . SER C 2 54  ? 121.69900 88.19200  113.60300 1.000 97.23649 ? 55  SER C CA  1 
ATOM   3408 C C   . SER C 2 54  ? 122.86700 87.21500  113.70600 1.000 97.23649 ? 55  SER C C   1 
ATOM   3409 O O   . SER C 2 54  ? 122.71800 86.10400  114.21500 1.000 97.23649 ? 55  SER C O   1 
ATOM   3410 C CB  . SER C 2 54  ? 120.78300 88.04400  114.81700 1.000 97.23649 ? 55  SER C CB  1 
ATOM   3411 O OG  . SER C 2 54  ? 120.29600 86.71800  114.92600 1.000 97.23649 ? 55  SER C OG  1 
ATOM   3412 N N   . PHE D 2 24  ? 136.96200 114.88600 112.94000 1.000 61.43775 ? 25  PHE D N   1 
ATOM   3413 C CA  . PHE D 2 24  ? 135.51500 114.78700 113.08000 1.000 61.43775 ? 25  PHE D CA  1 
ATOM   3414 C C   . PHE D 2 24  ? 135.05800 115.67500 114.23000 1.000 61.43775 ? 25  PHE D C   1 
ATOM   3415 O O   . PHE D 2 24  ? 133.93600 116.18100 114.22700 1.000 61.43775 ? 25  PHE D O   1 
ATOM   3416 C CB  . PHE D 2 24  ? 135.09100 113.32600 113.30800 1.000 61.43775 ? 25  PHE D CB  1 
ATOM   3417 C CG  . PHE D 2 24  ? 133.60100 113.12800 113.44300 1.000 61.43775 ? 25  PHE D CG  1 
ATOM   3418 C CD1 . PHE D 2 24  ? 132.83900 112.78700 112.33700 1.000 61.43775 ? 25  PHE D CD1 1 
ATOM   3419 C CD2 . PHE D 2 24  ? 132.96600 113.24500 114.67300 1.000 61.43775 ? 25  PHE D CD2 1 
ATOM   3420 C CE1 . PHE D 2 24  ? 131.47700 112.60100 112.44800 1.000 61.43775 ? 25  PHE D CE1 1 
ATOM   3421 C CE2 . PHE D 2 24  ? 131.60700 113.06900 114.78300 1.000 61.43775 ? 25  PHE D CE2 1 
ATOM   3422 C CZ  . PHE D 2 24  ? 130.86300 112.73900 113.67200 1.000 61.43775 ? 25  PHE D CZ  1 
ATOM   3423 N N   . SER D 2 25  ? 135.94000 115.85500 115.21600 1.000 68.36961 ? 26  SER D N   1 
ATOM   3424 C CA  . SER D 2 25  ? 135.58100 116.61700 116.40800 1.000 68.36961 ? 26  SER D CA  1 
ATOM   3425 C C   . SER D 2 25  ? 135.31300 118.07900 116.07800 1.000 68.36961 ? 26  SER D C   1 
ATOM   3426 O O   . SER D 2 25  ? 134.39600 118.69000 116.63800 1.000 68.36961 ? 26  SER D O   1 
ATOM   3427 C CB  . SER D 2 25  ? 136.68700 116.49900 117.45600 1.000 68.36961 ? 26  SER D CB  1 
ATOM   3428 O OG  . SER D 2 25  ? 136.15600 116.57300 118.76700 1.000 68.36961 ? 26  SER D OG  1 
ATOM   3429 N N   . LYS D 2 26  ? 136.11100 118.66000 115.18000 1.000 70.37761 ? 27  LYS D N   1 
ATOM   3430 C CA  . LYS D 2 26  ? 135.93600 120.06100 114.81200 1.000 70.37761 ? 27  LYS D CA  1 
ATOM   3431 C C   . LYS D 2 26  ? 134.62700 120.27600 114.06000 1.000 70.37761 ? 27  LYS D C   1 
ATOM   3432 O O   . LYS D 2 26  ? 133.86800 121.20600 114.35200 1.000 70.37761 ? 27  LYS D O   1 
ATOM   3433 C CB  . LYS D 2 26  ? 137.12500 120.52600 113.96900 1.000 70.37761 ? 27  LYS D CB  1 
ATOM   3434 C CG  . LYS D 2 26  ? 138.47700 120.32000 114.63100 1.000 70.37761 ? 27  LYS D CG  1 
ATOM   3435 C CD  . LYS D 2 26  ? 139.60800 120.74500 113.70900 1.000 70.37761 ? 27  LYS D CD  1 
ATOM   3436 C CE  . LYS D 2 26  ? 140.96400 120.52800 114.35900 1.000 70.37761 ? 27  LYS D CE  1 
ATOM   3437 N NZ  . LYS D 2 26  ? 142.08000 120.92000 113.45500 1.000 70.37761 ? 27  LYS D NZ  1 
ATOM   3438 N N   . LEU D 2 27  ? 134.34600 119.40800 113.08500 1.000 67.25294 ? 28  LEU D N   1 
ATOM   3439 C CA  . LEU D 2 27  ? 133.14700 119.56700 112.27100 1.000 67.25294 ? 28  LEU D CA  1 
ATOM   3440 C C   . LEU D 2 27  ? 131.87800 119.33100 113.08000 1.000 67.25294 ? 28  LEU D C   1 
ATOM   3441 O O   . LEU D 2 27  ? 130.84800 119.95500 112.80500 1.000 67.25294 ? 28  LEU D O   1 
ATOM   3442 C CB  . LEU D 2 27  ? 133.20400 118.62200 111.07200 1.000 67.25294 ? 28  LEU D CB  1 
ATOM   3443 C CG  . LEU D 2 27  ? 132.27600 118.94400 109.90100 1.000 67.25294 ? 28  LEU D CG  1 
ATOM   3444 C CD1 . LEU D 2 27  ? 133.05200 118.94100 108.59500 1.000 67.25294 ? 28  LEU D CD1 1 
ATOM   3445 C CD2 . LEU D 2 27  ? 131.12800 117.95200 109.84400 1.000 67.25294 ? 28  LEU D CD2 1 
ATOM   3446 N N   . ARG D 2 28  ? 131.93300 118.44900 114.07900 1.000 61.13067 ? 29  ARG D N   1 
ATOM   3447 C CA  . ARG D 2 28  ? 130.78700 118.25400 114.96200 1.000 61.13067 ? 29  ARG D CA  1 
ATOM   3448 C C   . ARG D 2 28  ? 130.46900 119.52100 115.74600 1.000 61.13067 ? 29  ARG D C   1 
ATOM   3449 O O   . ARG D 2 28  ? 129.30100 119.90600 115.87100 1.000 61.13067 ? 29  ARG D O   1 
ATOM   3450 C CB  . ARG D 2 28  ? 131.05600 117.08500 115.90700 1.000 61.13067 ? 29  ARG D CB  1 
ATOM   3451 C CG  . ARG D 2 28  ? 130.05900 116.93400 117.04400 1.000 61.13067 ? 29  ARG D CG  1 
ATOM   3452 C CD  . ARG D 2 28  ? 130.26900 115.60700 117.74300 1.000 61.13067 ? 29  ARG D CD  1 
ATOM   3453 N NE  . ARG D 2 28  ? 130.64400 115.76900 119.14500 1.000 61.13067 ? 29  ARG D NE  1 
ATOM   3454 C CZ  . ARG D 2 28  ? 129.78900 115.75600 120.16100 1.000 61.13067 ? 29  ARG D CZ  1 
ATOM   3455 N NH1 . ARG D 2 28  ? 128.49700 115.57300 119.94100 1.000 61.13067 ? 29  ARG D NH1 1 
ATOM   3456 N NH2 . ARG D 2 28  ? 130.23100 115.90500 121.40100 1.000 61.13067 ? 29  ARG D NH2 1 
ATOM   3457 N N   . GLU D 2 29  ? 131.49600 120.19200 116.26900 1.000 68.64943 ? 30  GLU D N   1 
ATOM   3458 C CA  . GLU D 2 29  ? 131.27300 121.45000 116.97200 1.000 68.64943 ? 30  GLU D CA  1 
ATOM   3459 C C   . GLU D 2 29  ? 130.86100 122.56300 116.01400 1.000 68.64943 ? 30  GLU D C   1 
ATOM   3460 O O   . GLU D 2 29  ? 130.18900 123.51600 116.42000 1.000 68.64943 ? 30  GLU D O   1 
ATOM   3461 C CB  . GLU D 2 29  ? 132.52800 121.84600 117.75000 1.000 68.64943 ? 30  GLU D CB  1 
ATOM   3462 C CG  . GLU D 2 29  ? 132.69600 121.18100 119.12300 1.000 68.64943 ? 30  GLU D CG  1 
ATOM   3463 C CD  . GLU D 2 29  ? 131.38400 120.93400 119.86200 1.000 68.64943 ? 30  GLU D CD  1 
ATOM   3464 O OE1 . GLU D 2 29  ? 130.99400 121.79600 120.67800 1.000 68.64943 ? 30  GLU D OE1 1 
ATOM   3465 O OE2 . GLU D 2 29  ? 130.76700 119.86200 119.67100 1.000 68.64943 ? 30  GLU D OE2 1 
ATOM   3466 N N   . GLN D 2 30  ? 131.27200 122.46800 114.74900 1.000 68.36414 ? 31  GLN D N   1 
ATOM   3467 C CA  . GLN D 2 30  ? 130.83200 123.43700 113.74900 1.000 68.36414 ? 31  GLN D CA  1 
ATOM   3468 C C   . GLN D 2 30  ? 129.35200 123.26400 113.41400 1.000 68.36414 ? 31  GLN D C   1 
ATOM   3469 O O   . GLN D 2 30  ? 128.63500 124.24600 113.19500 1.000 68.36414 ? 31  GLN D O   1 
ATOM   3470 C CB  . GLN D 2 30  ? 131.68300 123.31200 112.48300 1.000 68.36414 ? 31  GLN D CB  1 
ATOM   3471 C CG  . GLN D 2 30  ? 132.76100 124.38100 112.31200 1.000 68.36414 ? 31  GLN D CG  1 
ATOM   3472 C CD  . GLN D 2 30  ? 133.77800 124.41300 113.43600 1.000 68.36414 ? 31  GLN D CD  1 
ATOM   3473 O OE1 . GLN D 2 30  ? 134.77500 123.69300 113.40400 1.000 68.36414 ? 31  GLN D OE1 1 
ATOM   3474 N NE2 . GLN D 2 30  ? 133.54100 125.26300 114.42800 1.000 68.36414 ? 31  GLN D NE2 1 
ATOM   3475 N N   . LEU D 2 31  ? 128.88000 122.01500 113.36300 1.000 64.32692 ? 32  LEU D N   1 
ATOM   3476 C CA  . LEU D 2 31  ? 127.54700 121.74200 112.83100 1.000 64.32692 ? 32  LEU D CA  1 
ATOM   3477 C C   . LEU D 2 31  ? 126.44100 122.17200 113.78800 1.000 64.32692 ? 32  LEU D C   1 
ATOM   3478 O O   . LEU D 2 31  ? 125.35300 122.56100 113.34600 1.000 64.32692 ? 32  LEU D O   1 
ATOM   3479 C CB  . LEU D 2 31  ? 127.40700 120.25700 112.50600 1.000 64.32692 ? 32  LEU D CB  1 
ATOM   3480 C CG  . LEU D 2 31  ? 128.00200 119.76100 111.19200 1.000 64.32692 ? 32  LEU D CG  1 
ATOM   3481 C CD1 . LEU D 2 31  ? 127.61000 118.31300 110.96300 1.000 64.32692 ? 32  LEU D CD1 1 
ATOM   3482 C CD2 . LEU D 2 31  ? 127.55200 120.63800 110.03700 1.000 64.32692 ? 32  LEU D CD2 1 
ATOM   3483 N N   . GLY D 2 32  ? 126.68700 122.08900 115.09300 1.000 63.97523 ? 33  GLY D N   1 
ATOM   3484 C CA  . GLY D 2 32  ? 125.67000 122.32400 116.09600 1.000 63.97523 ? 33  GLY D CA  1 
ATOM   3485 C C   . GLY D 2 32  ? 125.02300 123.69800 116.07000 1.000 63.97523 ? 33  GLY D C   1 
ATOM   3486 O O   . GLY D 2 32  ? 123.81000 123.83500 115.84600 1.000 63.97523 ? 33  GLY D O   1 
ATOM   3487 N N   . PRO D 2 33  ? 125.81700 124.74500 116.32900 1.000 67.66480 ? 34  PRO D N   1 
ATOM   3488 C CA  . PRO D 2 33  ? 125.25300 126.10500 116.29600 1.000 67.66480 ? 34  PRO D CA  1 
ATOM   3489 C C   . PRO D 2 33  ? 124.70000 126.49800 114.94100 1.000 67.66480 ? 34  PRO D C   1 
ATOM   3490 O O   . PRO D 2 33  ? 123.74900 127.28200 114.88500 1.000 67.66480 ? 34  PRO D O   1 
ATOM   3491 C CB  . PRO D 2 33  ? 126.44200 126.98500 116.70600 1.000 67.66480 ? 34  PRO D CB  1 
ATOM   3492 C CG  . PRO D 2 33  ? 127.33600 126.07700 117.46500 1.000 67.66480 ? 34  PRO D CG  1 
ATOM   3493 C CD  . PRO D 2 33  ? 127.21700 124.75400 116.78500 1.000 67.66480 ? 34  PRO D CD  1 
ATOM   3494 N N   . VAL D 2 34  ? 125.26100 125.97200 113.85000 1.000 67.05193 ? 35  VAL D N   1 
ATOM   3495 C CA  . VAL D 2 34  ? 124.74300 126.28000 112.51800 1.000 67.05193 ? 35  VAL D CA  1 
ATOM   3496 C C   . VAL D 2 34  ? 123.31300 125.77300 112.36800 1.000 67.05193 ? 35  VAL D C   1 
ATOM   3497 O O   . VAL D 2 34  ? 122.41500 126.51600 111.94800 1.000 67.05193 ? 35  VAL D O   1 
ATOM   3498 C CB  . VAL D 2 34  ? 125.67600 125.69100 111.44300 1.000 67.05193 ? 35  VAL D CB  1 
ATOM   3499 C CG1 . VAL D 2 34  ? 124.96000 125.57300 110.11000 1.000 67.05193 ? 35  VAL D CG1 1 
ATOM   3500 C CG2 . VAL D 2 34  ? 126.92400 126.54000 111.30800 1.000 67.05193 ? 35  VAL D CG2 1 
ATOM   3501 N N   . THR D 2 35  ? 123.07700 124.51100 112.73900 1.000 65.02879 ? 36  THR D N   1 
ATOM   3502 C CA  . THR D 2 35  ? 121.73600 123.93600 112.68400 1.000 65.02879 ? 36  THR D CA  1 
ATOM   3503 C C   . THR D 2 35  ? 120.77800 124.67600 113.61200 1.000 65.02879 ? 36  THR D C   1 
ATOM   3504 O O   . THR D 2 35  ? 119.64400 125.00800 113.22700 1.000 65.02879 ? 36  THR D O   1 
ATOM   3505 C CB  . THR D 2 35  ? 121.80500 122.45200 113.05400 1.000 65.02879 ? 36  THR D CB  1 
ATOM   3506 O OG1 . THR D 2 35  ? 122.66500 121.76700 112.13600 1.000 65.02879 ? 36  THR D OG1 1 
ATOM   3507 C CG2 . THR D 2 35  ? 120.43000 121.81400 113.01900 1.000 65.02879 ? 36  THR D CG2 1 
ATOM   3508 N N   . GLN D 2 36  ? 121.23100 124.95900 114.83900 1.000 67.63702 ? 37  GLN D N   1 
ATOM   3509 C CA  . GLN D 2 36  ? 120.37300 125.63400 115.80800 1.000 67.63702 ? 37  GLN D CA  1 
ATOM   3510 C C   . GLN D 2 36  ? 119.98800 127.02900 115.33500 1.000 67.63702 ? 37  GLN D C   1 
ATOM   3511 O O   . GLN D 2 36  ? 118.81900 127.42200 115.42800 1.000 67.63702 ? 37  GLN D O   1 
ATOM   3512 C CB  . GLN D 2 36  ? 121.06900 125.70500 117.17000 1.000 67.63702 ? 37  GLN D CB  1 
ATOM   3513 C CG  . GLN D 2 36  ? 120.19000 125.98800 118.41900 1.000 67.63702 ? 37  GLN D CG  1 
ATOM   3514 C CD  . GLN D 2 36  ? 118.81200 125.30600 118.48000 1.000 67.63702 ? 37  GLN D CD  1 
ATOM   3515 O OE1 . GLN D 2 36  ? 118.62000 124.26800 117.85100 1.000 67.63702 ? 37  GLN D OE1 1 
ATOM   3516 N NE2 . GLN D 2 36  ? 117.82700 125.95500 119.09700 1.000 67.63702 ? 37  GLN D NE2 1 
ATOM   3517 N N   . GLU D 2 37  ? 120.95000 127.78400 114.80000 1.000 68.44418 ? 38  GLU D N   1 
ATOM   3518 C CA  . GLU D 2 37  ? 120.66400 129.13400 114.34200 1.000 68.44418 ? 38  GLU D CA  1 
ATOM   3519 C C   . GLU D 2 37  ? 119.82100 129.12600 113.07600 1.000 68.44418 ? 38  GLU D C   1 
ATOM   3520 O O   . GLU D 2 37  ? 119.01100 130.03500 112.88100 1.000 68.44418 ? 38  GLU D O   1 
ATOM   3521 C CB  . GLU D 2 37  ? 121.96900 129.91400 114.13900 1.000 68.44418 ? 38  GLU D CB  1 
ATOM   3522 C CG  . GLU D 2 37  ? 122.49900 129.97000 112.71200 1.000 68.44418 ? 38  GLU D CG  1 
ATOM   3523 C CD  . GLU D 2 37  ? 123.97200 130.32000 112.64300 1.000 68.44418 ? 38  GLU D CD  1 
ATOM   3524 O OE1 . GLU D 2 37  ? 124.50600 130.42600 111.51900 1.000 68.44418 ? 38  GLU D OE1 1 
ATOM   3525 O OE2 . GLU D 2 37  ? 124.59600 130.48600 113.71200 1.000 68.44418 ? 38  GLU D OE2 1 
ATOM   3526 N N   . PHE D 2 38  ? 119.96600 128.10500 112.22300 1.000 63.22405 ? 39  PHE D N   1 
ATOM   3527 C CA  . PHE D 2 38  ? 119.08900 128.00600 111.06400 1.000 63.22405 ? 39  PHE D CA  1 
ATOM   3528 C C   . PHE D 2 38  ? 117.64500 127.81100 111.49700 1.000 63.22405 ? 39  PHE D C   1 
ATOM   3529 O O   . PHE D 2 38  ? 116.73200 128.46000 110.97200 1.000 63.22405 ? 39  PHE D O   1 
ATOM   3530 C CB  . PHE D 2 38  ? 119.52400 126.86300 110.14700 1.000 63.22405 ? 39  PHE D CB  1 
ATOM   3531 C CG  . PHE D 2 38  ? 118.45800 126.43700 109.17700 1.000 63.22405 ? 39  PHE D CG  1 
ATOM   3532 C CD1 . PHE D 2 38  ? 118.18100 127.20300 108.05600 1.000 63.22405 ? 39  PHE D CD1 1 
ATOM   3533 C CD2 . PHE D 2 38  ? 117.71900 125.28300 109.39300 1.000 63.22405 ? 39  PHE D CD2 1 
ATOM   3534 C CE1 . PHE D 2 38  ? 117.19400 126.82500 107.16700 1.000 63.22405 ? 39  PHE D CE1 1 
ATOM   3535 C CE2 . PHE D 2 38  ? 116.73100 124.90400 108.51000 1.000 63.22405 ? 39  PHE D CE2 1 
ATOM   3536 C CZ  . PHE D 2 38  ? 116.47000 125.67400 107.39300 1.000 63.22405 ? 39  PHE D CZ  1 
ATOM   3537 N N   . TRP D 2 39  ? 117.41600 126.91900 112.46200 1.000 60.16582 ? 40  TRP D N   1 
ATOM   3538 C CA  . TRP D 2 39  ? 116.04000 126.67800 112.88400 1.000 60.16582 ? 40  TRP D CA  1 
ATOM   3539 C C   . TRP D 2 39  ? 115.48000 127.86500 113.66000 1.000 60.16582 ? 40  TRP D C   1 
ATOM   3540 O O   . TRP D 2 39  ? 114.29200 128.18700 113.53400 1.000 60.16582 ? 40  TRP D O   1 
ATOM   3541 C CB  . TRP D 2 39  ? 115.95500 125.38400 113.68800 1.000 60.16582 ? 40  TRP D CB  1 
ATOM   3542 C CG  . TRP D 2 39  ? 116.06000 124.18300 112.80600 1.000 60.16582 ? 40  TRP D CG  1 
ATOM   3543 C CD1 . TRP D 2 39  ? 117.08100 123.28400 112.76600 1.000 60.16582 ? 40  TRP D CD1 1 
ATOM   3544 C CD2 . TRP D 2 39  ? 115.12100 123.76700 111.80800 1.000 60.16582 ? 40  TRP D CD2 1 
ATOM   3545 N NE1 . TRP D 2 39  ? 116.83300 122.32700 111.81700 1.000 60.16582 ? 40  TRP D NE1 1 
ATOM   3546 C CE2 . TRP D 2 39  ? 115.63400 122.60000 111.21400 1.000 60.16582 ? 40  TRP D CE2 1 
ATOM   3547 C CE3 . TRP D 2 39  ? 113.89000 124.26400 111.36500 1.000 60.16582 ? 40  TRP D CE3 1 
ATOM   3548 C CZ2 . TRP D 2 39  ? 114.96300 121.92100 110.20100 1.000 60.16582 ? 40  TRP D CZ2 1 
ATOM   3549 C CZ3 . TRP D 2 39  ? 113.22700 123.59000 110.36000 1.000 60.16582 ? 40  TRP D CZ3 1 
ATOM   3550 C CH2 . TRP D 2 39  ? 113.76500 122.43200 109.78800 1.000 60.16582 ? 40  TRP D CH2 1 
ATOM   3551 N N   . ASP D 2 40  ? 116.32500 128.55100 114.43400 1.000 68.68587 ? 41  ASP D N   1 
ATOM   3552 C CA  . ASP D 2 40  ? 115.89000 129.76900 115.11300 1.000 68.68587 ? 41  ASP D CA  1 
ATOM   3553 C C   . ASP D 2 40  ? 115.51200 130.86000 114.11700 1.000 68.68587 ? 41  ASP D C   1 
ATOM   3554 O O   . ASP D 2 40  ? 114.49200 131.53800 114.28600 1.000 68.68587 ? 41  ASP D O   1 
ATOM   3555 C CB  . ASP D 2 40  ? 116.98700 130.26300 116.05400 1.000 68.68587 ? 41  ASP D CB  1 
ATOM   3556 C CG  . ASP D 2 40  ? 117.20400 129.33700 117.23200 1.000 68.68587 ? 41  ASP D CG  1 
ATOM   3557 O OD1 . ASP D 2 40  ? 116.30200 128.52800 117.53100 1.000 68.68587 ? 41  ASP D OD1 1 
ATOM   3558 O OD2 . ASP D 2 40  ? 118.28000 129.41800 117.85900 1.000 68.68587 ? 41  ASP D OD2 1 
ATOM   3559 N N   . ASN D 2 41  ? 116.31600 131.04000 113.06600 1.000 69.89688 ? 42  ASN D N   1 
ATOM   3560 C CA  . ASN D 2 41  ? 116.00000 132.04100 112.05300 1.000 69.89688 ? 42  ASN D CA  1 
ATOM   3561 C C   . ASN D 2 41  ? 114.73000 131.68000 111.29500 1.000 69.89688 ? 42  ASN D C   1 
ATOM   3562 O O   . ASN D 2 41  ? 113.89600 132.55000 111.02500 1.000 69.89688 ? 42  ASN D O   1 
ATOM   3563 C CB  . ASN D 2 41  ? 117.17100 132.21300 111.08500 1.000 69.89688 ? 42  ASN D CB  1 
ATOM   3564 C CG  . ASN D 2 41  ? 118.39600 132.83600 111.73600 1.000 69.89688 ? 42  ASN D CG  1 
ATOM   3565 O OD1 . ASN D 2 41  ? 118.39600 133.10500 112.93600 1.000 69.89688 ? 42  ASN D OD1 1 
ATOM   3566 N ND2 . ASN D 2 41  ? 119.45500 133.03400 110.96000 1.000 69.89688 ? 42  ASN D ND2 1 
ATOM   3567 N N   . LEU D 2 42  ? 114.56100 130.39900 110.95300 1.000 68.71246 ? 43  LEU D N   1 
ATOM   3568 C CA  . LEU D 2 42  ? 113.34900 129.97300 110.26100 1.000 68.71246 ? 43  LEU D CA  1 
ATOM   3569 C C   . LEU D 2 42  ? 112.12200 130.15600 111.14300 1.000 68.71246 ? 43  LEU D C   1 
ATOM   3570 O O   . LEU D 2 42  ? 111.01900 130.40300 110.64100 1.000 68.71246 ? 43  LEU D O   1 
ATOM   3571 C CB  . LEU D 2 42  ? 113.47900 128.51800 109.81300 1.000 68.71246 ? 43  LEU D CB  1 
ATOM   3572 C CG  . LEU D 2 42  ? 112.43800 128.02700 108.80500 1.000 68.71246 ? 43  LEU D CG  1 
ATOM   3573 C CD1 . LEU D 2 42  ? 112.38100 128.94800 107.60100 1.000 68.71246 ? 43  LEU D CD1 1 
ATOM   3574 C CD2 . LEU D 2 42  ? 112.72000 126.59800 108.37900 1.000 68.71246 ? 43  LEU D CD2 1 
ATOM   3575 N N   . GLU D 2 43  ? 112.29100 130.03500 112.46000 1.000 70.43652 ? 44  GLU D N   1 
ATOM   3576 C CA  . GLU D 2 43  ? 111.21000 130.39000 113.37100 1.000 70.43652 ? 44  GLU D CA  1 
ATOM   3577 C C   . GLU D 2 43  ? 110.93200 131.88800 113.33900 1.000 70.43652 ? 44  GLU D C   1 
ATOM   3578 O O   . GLU D 2 43  ? 109.77200 132.31100 113.38700 1.000 70.43652 ? 44  GLU D O   1 
ATOM   3579 C CB  . GLU D 2 43  ? 111.55200 129.94400 114.79000 1.000 70.43652 ? 44  GLU D CB  1 
ATOM   3580 C CG  . GLU D 2 43  ? 110.43400 130.16300 115.79000 1.000 70.43652 ? 44  GLU D CG  1 
ATOM   3581 C CD  . GLU D 2 43  ? 110.57800 129.28200 117.00300 1.000 70.43652 ? 44  GLU D CD  1 
ATOM   3582 O OE1 . GLU D 2 43  ? 111.51700 128.46600 117.01800 1.000 70.43652 ? 44  GLU D OE1 1 
ATOM   3583 O OE2 . GLU D 2 43  ? 109.75900 129.40000 117.93800 1.000 70.43652 ? 44  GLU D OE2 1 
ATOM   3584 N N   . LYS D 2 44  ? 111.98700 132.70500 113.27300 1.000 74.72382 ? 45  LYS D N   1 
ATOM   3585 C CA  . LYS D 2 44  ? 111.80500 134.15600 113.29400 1.000 74.72382 ? 45  LYS D CA  1 
ATOM   3586 C C   . LYS D 2 44  ? 111.06600 134.65500 112.05400 1.000 74.72382 ? 45  LYS D C   1 
ATOM   3587 O O   . LYS D 2 44  ? 110.09200 135.40700 112.16200 1.000 74.72382 ? 45  LYS D O   1 
ATOM   3588 C CB  . LYS D 2 44  ? 113.15700 134.86000 113.42400 1.000 74.72382 ? 45  LYS D CB  1 
ATOM   3589 C CG  . LYS D 2 44  ? 113.86700 134.67100 114.76000 1.000 74.72382 ? 45  LYS D CG  1 
ATOM   3590 C CD  . LYS D 2 44  ? 112.89500 134.58500 115.92500 1.000 74.72382 ? 45  LYS D CD  1 
ATOM   3591 C CE  . LYS D 2 44  ? 113.39800 133.62600 116.99100 1.000 74.72382 ? 45  LYS D CE  1 
ATOM   3592 N NZ  . LYS D 2 44  ? 113.42200 132.21900 116.50800 1.000 74.72382 ? 45  LYS D NZ  1 
ATOM   3593 N N   . GLU D 2 45  ? 111.51000 134.24300 110.86200 1.000 78.93381 ? 46  GLU D N   1 
ATOM   3594 C CA  . GLU D 2 45  ? 110.94900 134.81700 109.64000 1.000 78.93381 ? 46  GLU D CA  1 
ATOM   3595 C C   . GLU D 2 45  ? 109.54900 134.28700 109.34500 1.000 78.93381 ? 46  GLU D C   1 
ATOM   3596 O O   . GLU D 2 45  ? 108.81500 134.87800 108.54500 1.000 78.93381 ? 46  GLU D O   1 
ATOM   3597 C CB  . GLU D 2 45  ? 111.87300 134.56900 108.44600 1.000 78.93381 ? 46  GLU D CB  1 
ATOM   3598 C CG  . GLU D 2 45  ? 113.35200 134.60100 108.76000 1.000 78.93381 ? 46  GLU D CG  1 
ATOM   3599 C CD  . GLU D 2 45  ? 114.17800 135.17500 107.62700 1.000 78.93381 ? 46  GLU D CD  1 
ATOM   3600 O OE1 . GLU D 2 45  ? 114.91200 134.40200 106.97500 1.000 78.93381 ? 46  GLU D OE1 1 
ATOM   3601 O OE2 . GLU D 2 45  ? 114.09600 136.39700 107.38800 1.000 78.93381 ? 46  GLU D OE2 1 
ATOM   3602 N N   . THR D 2 46  ? 109.15900 133.17900 109.96900 1.000 81.16627 ? 47  THR D N   1 
ATOM   3603 C CA  . THR D 2 46  ? 107.85200 132.58800 109.71500 1.000 81.16627 ? 47  THR D CA  1 
ATOM   3604 C C   . THR D 2 46  ? 106.87000 132.76000 110.87100 1.000 81.16627 ? 47  THR D C   1 
ATOM   3605 O O   . THR D 2 46  ? 105.83700 132.08500 110.88300 1.000 81.16627 ? 47  THR D O   1 
ATOM   3606 C CB  . THR D 2 46  ? 107.99800 131.10000 109.38600 1.000 81.16627 ? 47  THR D CB  1 
ATOM   3607 O OG1 . THR D 2 46  ? 108.59000 130.41400 110.49700 1.000 81.16627 ? 47  THR D OG1 1 
ATOM   3608 C CG2 . THR D 2 46  ? 108.86400 130.91200 108.14900 1.000 81.16627 ? 47  THR D CG2 1 
ATOM   3609 N N   . GLU D 2 47  ? 107.16000 133.63800 111.83400 1.000 86.26338 ? 48  GLU D N   1 
ATOM   3610 C CA  . GLU D 2 47  ? 106.28300 133.78200 112.99500 1.000 86.26338 ? 48  GLU D CA  1 
ATOM   3611 C C   . GLU D 2 47  ? 104.91500 134.33200 112.60300 1.000 86.26338 ? 48  GLU D C   1 
ATOM   3612 O O   . GLU D 2 47  ? 103.87800 133.81600 113.03700 1.000 86.26338 ? 48  GLU D O   1 
ATOM   3613 C CB  . GLU D 2 47  ? 106.94200 134.68400 114.03900 1.000 86.26338 ? 48  GLU D CB  1 
ATOM   3614 C CG  . GLU D 2 47  ? 106.10800 134.90000 115.29100 1.000 86.26338 ? 48  GLU D CG  1 
ATOM   3615 C CD  . GLU D 2 47  ? 106.08100 133.68700 116.20100 1.000 86.26338 ? 48  GLU D CD  1 
ATOM   3616 O OE1 . GLU D 2 47  ? 106.96300 132.81300 116.06300 1.000 86.26338 ? 48  GLU D OE1 1 
ATOM   3617 O OE2 . GLU D 2 47  ? 105.17800 133.60900 117.05900 1.000 86.26338 ? 48  GLU D OE2 1 
ATOM   3618 N N   . GLY D 2 48  ? 104.89500 135.37700 111.77200 1.000 90.04056 ? 49  GLY D N   1 
ATOM   3619 C CA  . GLY D 2 48  ? 103.62800 135.97000 111.37000 1.000 90.04056 ? 49  GLY D CA  1 
ATOM   3620 C C   . GLY D 2 48  ? 102.78700 135.04100 110.51800 1.000 90.04056 ? 49  GLY D C   1 
ATOM   3621 O O   . GLY D 2 48  ? 101.56700 134.96700 110.68000 1.000 90.04056 ? 49  GLY D O   1 
ATOM   3622 N N   . LEU D 2 49  ? 103.42600 134.31400 109.60100 1.000 90.49936 ? 50  LEU D N   1 
ATOM   3623 C CA  . LEU D 2 49  ? 102.69700 133.36000 108.77000 1.000 90.49936 ? 50  LEU D CA  1 
ATOM   3624 C C   . LEU D 2 49  ? 102.11600 132.22600 109.61000 1.000 90.49936 ? 50  LEU D C   1 
ATOM   3625 O O   . LEU D 2 49  ? 100.95100 131.84400 109.43200 1.000 90.49936 ? 50  LEU D O   1 
ATOM   3626 C CB  . LEU D 2 49  ? 103.62700 132.82300 107.68300 1.000 90.49936 ? 50  LEU D CB  1 
ATOM   3627 C CG  . LEU D 2 49  ? 103.08700 131.85000 106.63800 1.000 90.49936 ? 50  LEU D CG  1 
ATOM   3628 C CD1 . LEU D 2 49  ? 102.05000 132.52500 105.75700 1.000 90.49936 ? 50  LEU D CD1 1 
ATOM   3629 C CD2 . LEU D 2 49  ? 104.22400 131.28600 105.80300 1.000 90.49936 ? 50  LEU D CD2 1 
ATOM   3630 N N   . ARG D 2 50  ? 102.89800 131.70300 110.55800 1.000 84.44606 ? 51  ARG D N   1 
ATOM   3631 C CA  . ARG D 2 50  ? 102.40400 130.63700 111.42500 1.000 84.44606 ? 51  ARG D CA  1 
ATOM   3632 C C   . ARG D 2 50  ? 101.29000 131.13900 112.33100 1.000 84.44606 ? 51  ARG D C   1 
ATOM   3633 O O   . ARG D 2 50  ? 100.39900 130.37200 112.71600 1.000 84.44606 ? 51  ARG D O   1 
ATOM   3634 C CB  . ARG D 2 50  ? 103.55100 130.06200 112.25200 1.000 84.44606 ? 51  ARG D CB  1 
ATOM   3635 C CG  . ARG D 2 50  ? 104.52600 129.22800 111.44800 1.000 84.44606 ? 51  ARG D CG  1 
ATOM   3636 C CD  . ARG D 2 50  ? 105.57400 128.62000 112.34900 1.000 84.44606 ? 51  ARG D CD  1 
ATOM   3637 N NE  . ARG D 2 50  ? 106.50600 129.62500 112.84400 1.000 84.44606 ? 51  ARG D NE  1 
ATOM   3638 C CZ  . ARG D 2 50  ? 106.58900 130.00100 114.11500 1.000 84.44606 ? 51  ARG D CZ  1 
ATOM   3639 N NH1 . ARG D 2 50  ? 105.80100 129.44900 115.02500 1.000 84.44606 ? 51  ARG D NH1 1 
ATOM   3640 N NH2 . ARG D 2 50  ? 107.46400 130.92500 114.47700 1.000 84.44606 ? 51  ARG D NH2 1 
ATOM   3641 N N   . GLN D 2 51  ? 101.32900 132.42300 112.69200 1.000 93.61258 ? 52  GLN D N   1 
ATOM   3642 C CA  . GLN D 2 51  ? 100.17700 133.03400 113.34600 1.000 93.61258 ? 52  GLN D CA  1 
ATOM   3643 C C   . GLN D 2 51  ? 98.98000  133.07500 112.40400 1.000 93.61258 ? 52  GLN D C   1 
ATOM   3644 O O   . GLN D 2 51  ? 97.83400  132.90700 112.83500 1.000 93.61258 ? 52  GLN D O   1 
ATOM   3645 C CB  . GLN D 2 51  ? 100.52800 134.44300 113.82500 1.000 93.61258 ? 52  GLN D CB  1 
ATOM   3646 C CG  . GLN D 2 51  ? 100.19700 134.70500 115.28300 1.000 93.61258 ? 52  GLN D CG  1 
ATOM   3647 C CD  . GLN D 2 51  ? 100.98600 133.81700 116.22200 1.000 93.61258 ? 52  GLN D CD  1 
ATOM   3648 O OE1 . GLN D 2 51  ? 102.21600 133.85100 116.23700 1.000 93.61258 ? 52  GLN D OE1 1 
ATOM   3649 N NE2 . GLN D 2 51  ? 100.28300 133.01300 117.01100 1.000 93.61258 ? 52  GLN D NE2 1 
ATOM   3650 N N   . GLU D 2 52  ? 99.23200  133.30900 111.11200 1.000 95.40911 ? 53  GLU D N   1 
ATOM   3651 C CA  . GLU D 2 52  ? 98.14500  133.40300 110.14100 1.000 95.40911 ? 53  GLU D CA  1 
ATOM   3652 C C   . GLU D 2 52  ? 97.42900  132.06700 109.96200 1.000 95.40911 ? 53  GLU D C   1 
ATOM   3653 O O   . GLU D 2 52  ? 96.20800  132.03800 109.76800 1.000 95.40911 ? 53  GLU D O   1 
ATOM   3654 C CB  . GLU D 2 52  ? 98.66300  133.92700 108.80100 1.000 95.40911 ? 53  GLU D CB  1 
ATOM   3655 C CG  . GLU D 2 52  ? 98.92100  135.42400 108.78400 1.000 95.40911 ? 53  GLU D CG  1 
ATOM   3656 C CD  . GLU D 2 52  ? 99.69000  135.87000 107.55700 1.000 95.40911 ? 53  GLU D CD  1 
ATOM   3657 O OE1 . GLU D 2 52  ? 99.62100  135.17000 106.52400 1.000 95.40911 ? 53  GLU D OE1 1 
ATOM   3658 O OE2 . GLU D 2 52  ? 100.36200 136.92000 107.62400 1.000 95.40911 ? 53  GLU D OE2 1 
ATOM   3659 N N   . MET D 2 53  ? 98.16300  130.94400 109.99800 1.000 96.74629 ? 54  MET D N   1 
ATOM   3660 C CA  . MET D 2 53  ? 97.43800  129.66900 110.04500 1.000 96.74629 ? 54  MET D CA  1 
ATOM   3661 C C   . MET D 2 53  ? 96.62200  129.51800 111.32500 1.000 96.74629 ? 54  MET D C   1 
ATOM   3662 O O   . MET D 2 53  ? 95.48400  129.03800 111.27400 1.000 96.74629 ? 54  MET D O   1 
ATOM   3663 C CB  . MET D 2 53  ? 98.33600  128.43100 109.90300 1.000 96.74629 ? 54  MET D CB  1 
ATOM   3664 C CG  . MET D 2 53  ? 98.73100  128.00700 108.48600 1.000 96.74629 ? 54  MET D CG  1 
ATOM   3665 S SD  . MET D 2 53  ? 100.44800 127.52600 108.19600 1.000 96.74629 ? 54  MET D SD  1 
ATOM   3666 C CE  . MET D 2 53  ? 101.29200 129.07800 108.08900 1.000 96.74629 ? 54  MET D CE  1 
ATOM   3667 N N   . SER D 2 54  ? 97.17300  129.90600 112.46800 1.000 97.53025 ? 55  SER D N   1 
ATOM   3668 C CA  . SER D 2 54  ? 96.47500  129.73200 113.73800 1.000 97.53025 ? 55  SER D CA  1 
ATOM   3669 C C   . SER D 2 54  ? 95.35300  130.75300 113.90200 1.000 97.53025 ? 55  SER D C   1 
ATOM   3670 O O   . SER D 2 54  ? 95.58100  131.87800 114.34600 1.000 97.53025 ? 55  SER D O   1 
ATOM   3671 C CB  . SER D 2 54  ? 97.45500  129.83600 114.90700 1.000 97.53025 ? 55  SER D CB  1 
ATOM   3672 O OG  . SER D 2 54  ? 97.93600  131.16100 115.04900 1.000 97.53025 ? 55  SER D OG  1 
HETATM 3673 C C2  . PEE E 3 .   ? 99.16500  100.61000 111.18100 1.000 51.72036 ? 301 PEE A C2  1 
HETATM 3674 C C1  . PEE E 3 .   ? 100.33700 101.57600 111.31200 1.000 51.72036 ? 301 PEE A C1  1 
HETATM 3675 N N   . PEE E 3 .   ? 104.63500 105.55000 112.16900 1.000 51.72036 ? 301 PEE A N   1 
HETATM 3676 C C3  . PEE E 3 .   ? 97.83500  101.35700 111.35700 1.000 51.72036 ? 301 PEE A C3  1 
HETATM 3677 C C4  . PEE E 3 .   ? 103.30000 103.66400 111.34600 1.000 51.72036 ? 301 PEE A C4  1 
HETATM 3678 C C5  . PEE E 3 .   ? 103.84300 105.05000 110.98200 1.000 51.72036 ? 301 PEE A C5  1 
HETATM 3679 C C10 . PEE E 3 .   ? 99.13600  98.61100  109.94400 1.000 51.72036 ? 301 PEE A C10 1 
HETATM 3680 C C11 . PEE E 3 .   ? 98.45700  97.92900  108.79900 1.000 51.72036 ? 301 PEE A C11 1 
HETATM 3681 C C12 . PEE E 3 .   ? 98.42900  96.42500  109.07400 1.000 51.72036 ? 301 PEE A C12 1 
HETATM 3682 C C13 . PEE E 3 .   ? 97.53700  95.71300  108.07400 1.000 51.72036 ? 301 PEE A C13 1 
HETATM 3683 C C30 . PEE E 3 .   ? 95.65800  100.93200 110.57800 1.000 51.72036 ? 301 PEE A C30 1 
HETATM 3684 C C31 . PEE E 3 .   ? 94.75800  100.49900 109.44900 1.000 51.72036 ? 301 PEE A C31 1 
HETATM 3685 C C32 . PEE E 3 .   ? 94.54500  98.98900  109.53400 1.000 51.72036 ? 301 PEE A C32 1 
HETATM 3686 C C33 . PEE E 3 .   ? 93.78800  98.47400  108.32300 1.000 51.72036 ? 301 PEE A C33 1 
HETATM 3687 O O4  . PEE E 3 .   ? 99.63700  98.01700  110.87400 1.000 51.72036 ? 301 PEE A O4  1 
HETATM 3688 O O5  . PEE E 3 .   ? 95.26400  101.17400 111.70900 1.000 51.72036 ? 301 PEE A O5  1 
HETATM 3689 O O2  . PEE E 3 .   ? 99.16800  99.96600  109.91900 1.000 51.72036 ? 301 PEE A O2  1 
HETATM 3690 O O3  . PEE E 3 .   ? 96.97200  101.05300 110.26900 1.000 51.72036 ? 301 PEE A O3  1 
HETATM 3691 O O1P . PEE E 3 .   ? 102.28400 103.23400 113.73300 1.000 51.72036 ? 301 PEE A O1P 1 
HETATM 3692 O O2P . PEE E 3 .   ? 100.15200 104.64100 112.96000 1.000 51.72036 ? 301 PEE A O2P 1 
HETATM 3693 O O3P . PEE E 3 .   ? 100.32600 102.10900 112.58900 1.000 51.72036 ? 301 PEE A O3P 1 
HETATM 3694 O O4P . PEE E 3 .   ? 101.93700 103.74000 111.31900 1.000 51.72036 ? 301 PEE A O4P 1 
HETATM 3695 P P   . PEE E 3 .   ? 101.12200 103.52200 112.87400 1.000 51.72036 ? 301 PEE A P   1 
HETATM 3696 C C2  . PEE F 3 .   ? 118.94200 117.51400 111.15500 1.000 52.34633 ? 301 PEE B C2  1 
HETATM 3697 C C1  . PEE F 3 .   ? 117.78700 116.52300 111.27700 1.000 52.34633 ? 301 PEE B C1  1 
HETATM 3698 N N   . PEE F 3 .   ? 113.46400 112.62200 112.23900 1.000 52.34633 ? 301 PEE B N   1 
HETATM 3699 C C3  . PEE F 3 .   ? 120.29000 116.80000 111.34500 1.000 52.34633 ? 301 PEE B C3  1 
HETATM 3700 C C4  . PEE F 3 .   ? 114.81400 114.44800 111.30900 1.000 52.34633 ? 301 PEE B C4  1 
HETATM 3701 C C5  . PEE F 3 .   ? 114.26700 113.04300 111.02900 1.000 52.34633 ? 301 PEE B C5  1 
HETATM 3702 C C10 . PEE F 3 .   ? 118.94500 119.51300 109.91600 1.000 52.34633 ? 301 PEE B C10 1 
HETATM 3703 C C11 . PEE F 3 .   ? 119.52800 120.20700 108.72500 1.000 52.34633 ? 301 PEE B C11 1 
HETATM 3704 C C12 . PEE F 3 .   ? 119.68700 121.69100 109.05500 1.000 52.34633 ? 301 PEE B C12 1 
HETATM 3705 C C13 . PEE F 3 .   ? 120.58500 122.37400 108.04000 1.000 52.34633 ? 301 PEE B C13 1 
HETATM 3706 C C30 . PEE F 3 .   ? 122.37800 117.47600 110.50100 1.000 52.34633 ? 301 PEE B C30 1 
HETATM 3707 C C31 . PEE F 3 .   ? 122.74700 118.83200 109.94900 1.000 52.34633 ? 301 PEE B C31 1 
HETATM 3708 C C32 . PEE F 3 .   ? 124.08700 118.72700 109.23400 1.000 52.34633 ? 301 PEE B C32 1 
HETATM 3709 C C33 . PEE F 3 .   ? 124.28900 119.87900 108.26800 1.000 52.34633 ? 301 PEE B C33 1 
HETATM 3710 O O4  . PEE F 3 .   ? 118.50100 120.10000 110.87900 1.000 52.34633 ? 301 PEE B O4  1 
HETATM 3711 O O5  . PEE F 3 .   ? 123.12900 116.78000 111.16700 1.000 52.34633 ? 301 PEE B O5  1 
HETATM 3712 O O2  . PEE F 3 .   ? 118.93500 118.15800 109.89200 1.000 52.34633 ? 301 PEE B O2  1 
HETATM 3713 O O3  . PEE F 3 .   ? 121.12400 117.04700 110.21900 1.000 52.34633 ? 301 PEE B O3  1 
HETATM 3714 O O1P . PEE F 3 .   ? 115.80400 114.90700 113.70500 1.000 52.34633 ? 301 PEE B O1P 1 
HETATM 3715 O O2P . PEE F 3 .   ? 117.94400 113.49000 112.97800 1.000 52.34633 ? 301 PEE B O2P 1 
HETATM 3716 O O3P . PEE F 3 .   ? 117.77400 116.01600 112.56500 1.000 52.34633 ? 301 PEE B O3P 1 
HETATM 3717 O O4P . PEE F 3 .   ? 116.17700 114.36300 111.30300 1.000 52.34633 ? 301 PEE B O4P 1 
HETATM 3718 P P   . PEE F 3 .   ? 116.97500 114.60700 112.86300 1.000 52.34633 ? 301 PEE B P   1 
HETATM 3719 O O   . HOH G 4 .   ? 111.12100 107.03600 103.27600 1.000 44.72474 ? 401 HOH A O   1 
HETATM 3720 O O   . HOH G 4 .   ? 103.96100 102.48400 115.16800 1.000 45.97150 ? 402 HOH A O   1 
HETATM 3721 O O   . HOH G 4 .   ? 108.05900 102.07800 143.83900 1.000 33.07210 ? 403 HOH A O   1 
HETATM 3722 O O   . HOH G 4 .   ? 110.93800 103.89200 111.33800 1.000 42.67190 ? 404 HOH A O   1 
HETATM 3723 O O   . HOH G 4 .   ? 100.80500 103.32200 102.48700 1.000 40.85325 ? 405 HOH A O   1 
HETATM 3724 O O   . HOH G 4 .   ? 106.83900 104.68700 135.19200 1.000 24.48979 ? 406 HOH A O   1 
HETATM 3725 O O   . HOH G 4 .   ? 124.56600 92.20700  136.12800 1.000 36.29079 ? 407 HOH A O   1 
HETATM 3726 O O   . HOH G 4 .   ? 112.06200 117.85700 135.42800 1.000 29.17486 ? 408 HOH A O   1 
HETATM 3727 O O   . HOH G 4 .   ? 124.89900 118.50100 132.78600 1.000 37.97376 ? 409 HOH A O   1 
HETATM 3728 O O   . HOH G 4 .   ? 110.35800 106.26000 133.77100 1.000 22.31120 ? 410 HOH A O   1 
HETATM 3729 O O   . HOH G 4 .   ? 107.43000 102.76100 109.35900 1.000 44.22026 ? 411 HOH A O   1 
HETATM 3730 O O   . HOH G 4 .   ? 111.57900 108.24300 126.84700 1.000 24.94216 ? 412 HOH A O   1 
HETATM 3731 O O   . HOH G 4 .   ? 107.59600 108.36400 125.04400 1.000 27.87629 ? 413 HOH A O   1 
HETATM 3732 O O   . HOH G 4 .   ? 122.13600 116.32000 125.77000 1.000 31.47665 ? 414 HOH A O   1 
HETATM 3733 O O   . HOH G 4 .   ? 125.13900 103.41900 126.59900 1.000 29.45249 ? 415 HOH A O   1 
HETATM 3734 O O   . HOH G 4 .   ? 108.80000 102.34300 119.29600 1.000 36.24461 ? 416 HOH A O   1 
HETATM 3735 O O   . HOH G 4 .   ? 127.22400 103.34900 127.78000 1.000 33.37250 ? 417 HOH A O   1 
HETATM 3736 O O   . HOH G 4 .   ? 121.14200 104.02800 135.79200 1.000 29.64638 ? 418 HOH A O   1 
HETATM 3737 O O   . HOH G 4 .   ? 112.19600 112.47200 120.68200 1.000 33.87097 ? 419 HOH A O   1 
HETATM 3738 O O   . HOH G 4 .   ? 110.33500 98.77800  144.87700 1.000 36.36613 ? 420 HOH A O   1 
HETATM 3739 O O   . HOH G 4 .   ? 117.13300 107.04900 113.41200 1.000 36.59508 ? 421 HOH A O   1 
HETATM 3740 O O   . HOH G 4 .   ? 111.83700 111.54000 133.04200 1.000 23.71062 ? 422 HOH A O   1 
HETATM 3741 O O   . HOH G 4 .   ? 117.14300 123.30000 78.61500  1.000 57.89506 ? 423 HOH A O   1 
HETATM 3742 O O   . HOH G 4 .   ? 113.43200 101.23200 123.92500 1.000 32.63249 ? 424 HOH A O   1 
HETATM 3743 O O   . HOH G 4 .   ? 120.14000 113.81400 118.03400 1.000 42.03422 ? 425 HOH A O   1 
HETATM 3744 O O   . HOH G 4 .   ? 110.20400 99.85800  124.31700 1.000 33.24449 ? 426 HOH A O   1 
HETATM 3745 O O   . HOH G 4 .   ? 112.76400 120.33600 132.73200 1.000 32.06756 ? 427 HOH A O   1 
HETATM 3746 O O   . HOH G 4 .   ? 108.72000 107.73400 132.28700 1.000 26.03789 ? 428 HOH A O   1 
HETATM 3747 O O   . HOH G 4 .   ? 100.96000 97.72400  142.41400 1.000 39.88264 ? 429 HOH A O   1 
HETATM 3748 O O   . HOH G 4 .   ? 115.79500 119.95500 124.88700 1.000 33.45541 ? 430 HOH A O   1 
HETATM 3749 O O   . HOH G 4 .   ? 113.29500 118.39400 122.12300 1.000 34.61834 ? 431 HOH A O   1 
HETATM 3750 O O   . HOH G 4 .   ? 121.23600 99.59900  124.20300 1.000 35.66427 ? 432 HOH A O   1 
HETATM 3751 O O   . HOH G 4 .   ? 109.83800 99.01700  134.01400 1.000 31.18546 ? 433 HOH A O   1 
HETATM 3752 O O   . HOH G 4 .   ? 128.29800 97.89200  123.71000 1.000 42.56353 ? 434 HOH A O   1 
HETATM 3753 O O   . HOH G 4 .   ? 112.02900 119.90300 128.48800 1.000 34.33930 ? 435 HOH A O   1 
HETATM 3754 O O   . HOH G 4 .   ? 104.67300 109.04400 101.05200 1.000 42.05266 ? 436 HOH A O   1 
HETATM 3755 O O   . HOH G 4 .   ? 113.38000 107.43100 103.23400 1.000 43.31214 ? 437 HOH A O   1 
HETATM 3756 O O   . HOH G 4 .   ? 127.95200 105.40200 132.72800 1.000 32.38662 ? 438 HOH A O   1 
HETATM 3757 O O   . HOH G 4 .   ? 107.56000 98.31100  131.02400 1.000 34.21119 ? 439 HOH A O   1 
HETATM 3758 O O   . HOH G 4 .   ? 107.59600 99.78900  133.04000 1.000 30.58179 ? 440 HOH A O   1 
HETATM 3759 O O   . HOH G 4 .   ? 124.08000 119.95500 140.07600 1.000 41.03680 ? 441 HOH A O   1 
HETATM 3760 O O   . HOH G 4 .   ? 129.18900 96.85700  128.13100 1.000 36.09872 ? 442 HOH A O   1 
HETATM 3761 O O   . HOH G 4 .   ? 111.26400 106.03400 116.32000 1.000 42.40202 ? 443 HOH A O   1 
HETATM 3762 O O   . HOH G 4 .   ? 125.73800 96.29900  125.38800 1.000 39.30564 ? 444 HOH A O   1 
HETATM 3763 O O   . HOH G 4 .   ? 116.72700 107.25400 148.30800 1.000 41.56933 ? 445 HOH A O   1 
HETATM 3764 O O   . HOH G 4 .   ? 111.95800 107.38700 119.27000 1.000 32.37243 ? 446 HOH A O   1 
HETATM 3765 O O   . HOH G 4 .   ? 127.37600 94.56800  134.63400 1.000 38.69914 ? 447 HOH A O   1 
HETATM 3766 O O   . HOH G 4 .   ? 109.63600 100.67300 120.71300 1.000 37.91825 ? 448 HOH A O   1 
HETATM 3767 O O   . HOH G 4 .   ? 103.11900 94.53000  117.01700 1.000 52.42237 ? 449 HOH A O   1 
HETATM 3768 O O   . HOH G 4 .   ? 117.58300 114.00400 116.54300 1.000 41.13156 ? 450 HOH A O   1 
HETATM 3769 O O   . HOH G 4 .   ? 115.59300 101.47800 124.51700 1.000 35.68843 ? 451 HOH A O   1 
HETATM 3770 O O   . HOH G 4 .   ? 114.69600 117.98800 90.89700  1.000 44.24560 ? 452 HOH A O   1 
HETATM 3771 O O   . HOH G 4 .   ? 99.73100  110.56500 103.96500 1.000 46.25416 ? 453 HOH A O   1 
HETATM 3772 O O   . HOH G 4 .   ? 122.82700 117.04700 140.31100 1.000 36.43685 ? 454 HOH A O   1 
HETATM 3773 O O   . HOH G 4 .   ? 111.49300 108.02400 99.17500  1.000 42.74305 ? 455 HOH A O   1 
HETATM 3774 O O   . HOH G 4 .   ? 117.00000 111.94900 96.05700  1.000 40.89033 ? 456 HOH A O   1 
HETATM 3775 O O   . HOH G 4 .   ? 109.37000 104.53900 118.33500 1.000 38.43616 ? 457 HOH A O   1 
HETATM 3776 O O   . HOH G 4 .   ? 118.50100 120.68200 137.50600 1.000 32.23650 ? 458 HOH A O   1 
HETATM 3777 O O   . HOH G 4 .   ? 106.59200 108.20300 122.47300 1.000 28.32135 ? 459 HOH A O   1 
HETATM 3778 O O   . HOH G 4 .   ? 127.22600 105.78600 128.94100 1.000 31.12949 ? 460 HOH A O   1 
HETATM 3779 O O   . HOH G 4 .   ? 109.05000 109.05000 97.76900  1.000 46.64548 ? 461 HOH A O   1 
HETATM 3780 O O   . HOH H 4 .   ? 102.44000 116.67000 124.77900 1.000 34.13235 ? 401 HOH B O   1 
HETATM 3781 O O   . HOH H 4 .   ? 106.99800 111.03800 103.28500 1.000 45.91669 ? 402 HOH B O   1 
HETATM 3782 O O   . HOH H 4 .   ? 107.17700 114.20000 111.37700 1.000 42.84988 ? 403 HOH B O   1 
HETATM 3783 O O   . HOH H 4 .   ? 114.13900 115.62200 115.16600 1.000 46.76381 ? 404 HOH B O   1 
HETATM 3784 O O   . HOH H 4 .   ? 110.04200 116.02300 143.83800 1.000 33.26353 ? 405 HOH B O   1 
HETATM 3785 O O   . HOH H 4 .   ? 96.86400  118.50100 124.20300 1.000 35.27942 ? 406 HOH B O   1 
HETATM 3786 O O   . HOH H 4 .   ? 93.55700  125.90900 136.09300 1.000 36.45014 ? 407 HOH B O   1 
HETATM 3787 O O   . HOH H 4 .   ? 117.30000 114.81700 102.47000 1.000 41.22354 ? 408 HOH B O   1 
HETATM 3788 O O   . HOH H 4 .   ? 111.26000 113.41200 135.19100 1.000 24.76617 ? 409 HOH B O   1 
HETATM 3789 O O   . HOH H 4 .   ? 93.19300  99.59900  132.78900 1.000 39.46380 ? 410 HOH B O   1 
HETATM 3790 O O   . HOH H 4 .   ? 106.51600 109.86100 126.84400 1.000 24.85784 ? 411 HOH B O   1 
HETATM 3791 O O   . HOH H 4 .   ? 110.50400 109.73600 125.04400 1.000 28.66349 ? 412 HOH B O   1 
HETATM 3792 O O   . HOH H 4 .   ? 107.74100 111.83900 133.77100 1.000 22.10732 ? 413 HOH B O   1 
HETATM 3793 O O   . HOH H 4 .   ? 109.30200 115.76200 119.29900 1.000 37.74214 ? 414 HOH B O   1 
HETATM 3794 O O   . HOH H 4 .   ? 92.97300  114.68600 126.58500 1.000 29.12811 ? 415 HOH B O   1 
HETATM 3795 O O   . HOH H 4 .   ? 106.03800 100.24300 135.42800 1.000 29.09553 ? 416 HOH B O   1 
HETATM 3796 O O   . HOH H 4 .   ? 95.96400  101.78400 125.77100 1.000 31.62663 ? 417 HOH B O   1 
HETATM 3797 O O   . HOH H 4 .   ? 110.66800 115.33700 109.35900 1.000 45.06218 ? 418 HOH B O   1 
HETATM 3798 O O   . HOH H 4 .   ? 96.96100  114.07500 135.79500 1.000 29.06266 ? 419 HOH B O   1 
HETATM 3799 O O   . HOH H 4 .   ? 90.87600  114.75200 127.77900 1.000 32.10743 ? 420 HOH B O   1 
HETATM 3800 O O   . HOH H 4 .   ? 105.90500 105.62800 120.68200 1.000 33.34773 ? 421 HOH B O   1 
HETATM 3801 O O   . HOH H 4 .   ? 107.75800 119.31700 144.87400 1.000 36.67390 ? 422 HOH B O   1 
HETATM 3802 O O   . HOH H 4 .   ? 106.26100 106.56000 133.04100 1.000 23.99263 ? 423 HOH B O   1 
HETATM 3803 O O   . HOH H 4 .   ? 107.89300 118.24200 124.31700 1.000 33.33026 ? 424 HOH B O   1 
HETATM 3804 O O   . HOH H 4 .   ? 97.96700  104.29300 118.02800 1.000 40.65523 ? 425 HOH B O   1 
HETATM 3805 O O   . HOH H 4 .   ? 105.33300 97.75900  132.73300 1.000 31.80898 ? 426 HOH B O   1 
HETATM 3806 O O   . HOH H 4 .   ? 117.13800 120.38000 142.41300 1.000 39.73735 ? 427 HOH B O   1 
HETATM 3807 O O   . HOH H 4 .   ? 109.37900 110.36500 132.28700 1.000 25.60324 ? 428 HOH B O   1 
HETATM 3808 O O   . HOH H 4 .   ? 102.31300 98.14500  124.88900 1.000 34.62833 ? 429 HOH B O   1 
HETATM 3809 O O   . HOH H 4 .   ? 104.80400 99.71200  122.12000 1.000 35.17076 ? 430 HOH B O   1 
HETATM 3810 O O   . HOH H 4 .   ? 100.97300 111.05800 113.41200 1.000 36.19751 ? 431 HOH B O   1 
HETATM 3811 O O   . HOH H 4 .   ? 108.26100 119.08900 134.01500 1.000 30.90621 ? 432 HOH B O   1 
HETATM 3812 O O   . HOH H 4 .   ? 104.55800 116.84100 123.96900 1.000 32.32548 ? 433 HOH B O   1 
HETATM 3813 O O   . HOH H 4 .   ? 89.80600  120.20600 123.71600 1.000 42.05809 ? 434 HOH B O   1 
HETATM 3814 O O   . HOH H 4 .   ? 113.42800 109.05600 101.05300 1.000 42.88625 ? 435 HOH B O   1 
HETATM 3815 O O   . HOH H 4 .   ? 104.73400 110.67300 103.23300 1.000 43.11897 ? 436 HOH B O   1 
HETATM 3816 O O   . HOH H 4 .   ? 90.14800  112.70000 132.73400 1.000 34.31338 ? 437 HOH B O   1 
HETATM 3817 O O   . HOH H 4 .   ? 110.50400 118.30000 133.04100 1.000 31.24676 ? 438 HOH B O   1 
HETATM 3818 O O   . HOH H 4 .   ? 110.53700 119.80000 131.01100 1.000 34.74358 ? 439 HOH B O   1 
HETATM 3819 O O   . HOH H 4 .   ? 106.07600 98.19000  128.49800 1.000 34.70221 ? 440 HOH B O   1 
HETATM 3820 O O   . HOH H 4 .   ? 100.95500 94.83800  78.93600  1.000 56.45116 ? 441 HOH B O   1 
HETATM 3821 O O   . HOH H 4 .   ? 88.91100  121.24500 128.13000 1.000 35.12723 ? 442 HOH B O   1 
HETATM 3822 O O   . HOH H 4 .   ? 92.37700  121.77800 125.37200 1.000 38.15541 ? 443 HOH B O   1 
HETATM 3823 O O   . HOH H 4 .   ? 106.83500 112.06700 116.32000 1.000 42.46219 ? 444 HOH B O   1 
HETATM 3824 O O   . HOH H 4 .   ? 106.14200 110.72100 119.27300 1.000 32.63806 ? 445 HOH B O   1 
HETATM 3825 O O   . HOH H 4 .   ? 101.37800 110.85400 148.30800 1.000 42.17099 ? 446 HOH B O   1 
HETATM 3826 O O   . HOH H 4 .   ? 108.46200 117.42800 120.71800 1.000 38.20873 ? 447 HOH B O   1 
HETATM 3827 O O   . HOH H 4 .   ? 90.72400  123.53100 134.63400 1.000 37.57413 ? 448 HOH B O   1 
HETATM 3828 O O   . HOH H 4 .   ? 93.89900  98.15200  140.19000 1.000 42.10206 ? 449 HOH B O   1 
HETATM 3829 O O   . HOH H 4 .   ? 114.94500 123.57500 117.03000 1.000 53.06115 ? 450 HOH B O   1 
HETATM 3830 O O   . HOH H 4 .   ? 100.51400 104.09300 116.54400 1.000 40.92189 ? 451 HOH B O   1 
HETATM 3831 O O   . HOH H 4 .   ? 118.32300 107.47900 103.98800 1.000 45.49943 ? 452 HOH B O   1 
HETATM 3832 O O   . HOH H 4 .   ? 103.42500 100.12500 90.90400  1.000 44.43645 ? 453 HOH B O   1 
HETATM 3833 O O   . HOH H 4 .   ? 95.28100  101.05300 140.31100 1.000 36.69476 ? 454 HOH B O   1 
HETATM 3834 O O   . HOH H 4 .   ? 106.60700 110.07300 99.18000  1.000 43.06003 ? 455 HOH B O   1 
HETATM 3835 O O   . HOH H 4 .   ? 101.10400 106.15100 96.05900  1.000 40.69110 ? 456 HOH B O   1 
HETATM 3836 O O   . HOH H 4 .   ? 108.72500 113.55200 118.33300 1.000 38.73351 ? 457 HOH B O   1 
HETATM 3837 O O   . HOH H 4 .   ? 99.59900  97.41900  137.50500 1.000 33.17294 ? 458 HOH B O   1 
HETATM 3838 O O   . HOH H 4 .   ? 109.05000 109.05000 104.43300 1.000 45.08840 ? 459 HOH B O   1 
HETATM 3839 O O   . HOH H 4 .   ? 111.50800 109.89800 122.47300 1.000 28.72319 ? 460 HOH B O   1 
HETATM 3840 O O   . HOH H 4 .   ? 90.87500  112.31700 128.93800 1.000 31.61517 ? 461 HOH B O   1 
# 
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   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   MET 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   ILE 7   7   ?   ?   ?   A . n 
A 1 8   PHE 8   8   ?   ?   ?   A . n 
A 1 9   THR 9   9   ?   ?   ?   A . n 
A 1 10  ILE 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  THR 12  12  ?   ?   ?   A . n 
A 1 13  VAL 13  13  ?   ?   ?   A . n 
A 1 14  THR 14  14  ?   ?   ?   A . n 
A 1 15  LEU 15  15  ?   ?   ?   A . n 
A 1 16  LYS 16  16  ?   ?   ?   A . n 
A 1 17  GLN 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  GLU 19  19  ?   ?   ?   A . n 
A 1 20  ILE 20  20  ?   ?   ?   A . n 
A 1 21  LYS 21  21  ?   ?   ?   A . n 
A 1 22  ASP 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  THR 24  24  ?   ?   ?   A . n 
A 1 25  PRO 25  25  ?   ?   ?   A . n 
A 1 26  SER 26  26  ?   ?   ?   A . n 
A 1 27  ASP 27  27  ?   ?   ?   A . n 
A 1 28  PHE 28  28  ?   ?   ?   A . n 
A 1 29  VAL 29  29  ?   ?   ?   A . n 
A 1 30  ARG 30  30  ?   ?   ?   A . n 
A 1 31  ALA 31  31  ?   ?   ?   A . n 
A 1 32  THR 32  32  ?   ?   ?   A . n 
A 1 33  ALA 33  33  ?   ?   ?   A . n 
A 1 34  THR 34  34  ?   ?   ?   A . n 
A 1 35  ILE 35  35  ?   ?   ?   A . n 
A 1 36  PRO 36  36  ?   ?   ?   A . n 
A 1 37  ILE 37  37  ?   ?   ?   A . n 
A 1 38  GLN 38  38  ?   ?   ?   A . n 
A 1 39  ALA 39  39  ?   ?   ?   A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  TRP 45  45  45  TRP TRP A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  TRP 69  69  69  TRP TRP A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 TRP 128 128 128 TRP TRP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 CYS 130 130 130 CYS CYS A . n 
A 1 131 TRP 131 131 131 TRP TRP A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 PRO 138 138 138 PRO PRO A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 TYR 141 141 141 TYR TYR A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 CYS 148 148 148 CYS CYS A . n 
A 1 149 TRP 149 149 149 TRP TRP A . n 
A 1 150 HIS 150 150 150 HIS HIS A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 CYS 157 157 157 CYS CYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 ?   ?   ?   A . n 
A 1 176 THR 176 176 ?   ?   ?   A . n 
A 1 177 SER 177 177 ?   ?   ?   A . n 
A 1 178 PRO 178 178 ?   ?   ?   A . n 
A 1 179 ILE 179 179 ?   ?   ?   A . n 
A 1 180 SER 180 180 ?   ?   ?   A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 HIS 182 182 182 HIS HIS A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 GLN 185 185 185 GLN GLN A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 LYS 192 192 192 LYS LYS A . n 
A 1 193 TRP 193 193 193 TRP TRP A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 CYS 200 200 200 CYS CYS A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 GLN 213 213 213 GLN GLN A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 HIS 227 227 227 HIS HIS A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 TYR 233 233 233 TYR TYR A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLU 239 239 ?   ?   ?   A . n 
A 1 240 PRO 240 240 ?   ?   ?   A . n 
A 1 241 GLU 241 241 ?   ?   ?   A . n 
A 1 242 GLU 242 242 ?   ?   ?   A . n 
A 1 243 HIS 243 243 ?   ?   ?   A . n 
A 1 244 VAL 244 244 ?   ?   ?   A . n 
A 1 245 GLN 245 245 ?   ?   ?   A . n 
A 1 246 ILE 246 246 ?   ?   ?   A . n 
A 1 247 HIS 247 247 ?   ?   ?   A . n 
A 1 248 THR 248 248 ?   ?   ?   A . n 
A 1 249 ILE 249 249 ?   ?   ?   A . n 
A 1 250 ASP 250 250 ?   ?   ?   A . n 
A 1 251 GLY 251 251 ?   ?   ?   A . n 
A 1 252 SER 252 252 ?   ?   ?   A . n 
A 1 253 SER 253 253 ?   ?   ?   A . n 
A 1 254 GLY 254 254 ?   ?   ?   A . n 
A 1 255 VAL 255 255 ?   ?   ?   A . n 
A 1 256 VAL 256 256 ?   ?   ?   A . n 
A 1 257 ASN 257 257 ?   ?   ?   A . n 
A 1 258 PRO 258 258 ?   ?   ?   A . n 
A 1 259 VAL 259 259 ?   ?   ?   A . n 
A 1 260 MET 260 260 ?   ?   ?   A . n 
A 1 261 GLU 261 261 ?   ?   ?   A . n 
A 1 262 PRO 262 262 ?   ?   ?   A . n 
A 1 263 ILE 263 263 ?   ?   ?   A . n 
A 1 264 TYR 264 264 ?   ?   ?   A . n 
A 1 265 ASP 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 PRO 267 267 ?   ?   ?   A . n 
A 1 268 THR 268 268 ?   ?   ?   A . n 
A 1 269 THR 269 269 ?   ?   ?   A . n 
A 1 270 THR 270 270 ?   ?   ?   A . n 
A 1 271 THR 271 271 ?   ?   ?   A . n 
A 1 272 SER 272 272 ?   ?   ?   A . n 
A 1 273 VAL 273 273 ?   ?   ?   A . n 
A 1 274 PRO 274 274 ?   ?   ?   A . n 
A 1 275 LEU 275 275 ?   ?   ?   A . n 
A 1 276 SER 276 276 ?   ?   ?   A . n 
A 1 277 ASN 277 277 ?   ?   ?   A . n 
A 1 278 SER 278 278 ?   ?   ?   A . n 
A 1 279 LEU 279 279 ?   ?   ?   A . n 
A 1 280 GLU 280 280 ?   ?   ?   A . n 
A 1 281 VAL 281 281 ?   ?   ?   A . n 
A 1 282 LEU 282 282 ?   ?   ?   A . n 
A 1 283 PHE 283 283 ?   ?   ?   A . n 
A 1 284 GLN 284 284 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   PHE 4   4   ?   ?   ?   B . n 
B 1 5   MET 5   5   ?   ?   ?   B . n 
B 1 6   ARG 6   6   ?   ?   ?   B . n 
B 1 7   ILE 7   7   ?   ?   ?   B . n 
B 1 8   PHE 8   8   ?   ?   ?   B . n 
B 1 9   THR 9   9   ?   ?   ?   B . n 
B 1 10  ILE 10  10  ?   ?   ?   B . n 
B 1 11  GLY 11  11  ?   ?   ?   B . n 
B 1 12  THR 12  12  ?   ?   ?   B . n 
B 1 13  VAL 13  13  ?   ?   ?   B . n 
B 1 14  THR 14  14  ?   ?   ?   B . n 
B 1 15  LEU 15  15  ?   ?   ?   B . n 
B 1 16  LYS 16  16  ?   ?   ?   B . n 
B 1 17  GLN 17  17  ?   ?   ?   B . n 
B 1 18  GLY 18  18  ?   ?   ?   B . n 
B 1 19  GLU 19  19  ?   ?   ?   B . n 
B 1 20  ILE 20  20  ?   ?   ?   B . n 
B 1 21  LYS 21  21  ?   ?   ?   B . n 
B 1 22  ASP 22  22  ?   ?   ?   B . n 
B 1 23  ALA 23  23  ?   ?   ?   B . n 
B 1 24  THR 24  24  ?   ?   ?   B . n 
B 1 25  PRO 25  25  ?   ?   ?   B . n 
B 1 26  SER 26  26  ?   ?   ?   B . n 
B 1 27  ASP 27  27  ?   ?   ?   B . n 
B 1 28  PHE 28  28  ?   ?   ?   B . n 
B 1 29  VAL 29  29  ?   ?   ?   B . n 
B 1 30  ARG 30  30  ?   ?   ?   B . n 
B 1 31  ALA 31  31  ?   ?   ?   B . n 
B 1 32  THR 32  32  ?   ?   ?   B . n 
B 1 33  ALA 33  33  ?   ?   ?   B . n 
B 1 34  THR 34  34  ?   ?   ?   B . n 
B 1 35  ILE 35  35  ?   ?   ?   B . n 
B 1 36  PRO 36  36  ?   ?   ?   B . n 
B 1 37  ILE 37  37  ?   ?   ?   B . n 
B 1 38  GLN 38  38  ?   ?   ?   B . n 
B 1 39  ALA 39  39  ?   ?   ?   B . n 
B 1 40  SER 40  40  40  SER SER B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  TRP 45  45  45  TRP TRP B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  PHE 56  56  56  PHE PHE B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  LYS 66  66  66  LYS LYS B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  TRP 69  69  69  TRP TRP B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  HIS 78  78  78  HIS HIS B . n 
B 1 79  PHE 79  79  79  PHE PHE B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  ASN 82  82  82  ASN ASN B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  THR 89  89  89  THR THR B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  SER 92  92  92  SER SER B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 TYR 109 109 109 TYR TYR B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 MET 125 125 125 MET MET B . n 
B 1 126 ARG 126 126 126 ARG ARG B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 TRP 128 128 128 TRP TRP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 CYS 130 130 130 CYS CYS B . n 
B 1 131 TRP 131 131 131 TRP TRP B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 CYS 133 133 133 CYS CYS B . n 
B 1 134 ARG 134 134 134 ARG ARG B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 ASN 137 137 137 ASN ASN B . n 
B 1 138 PRO 138 138 138 PRO PRO B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 TYR 141 141 141 TYR TYR B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 TYR 145 145 145 TYR TYR B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 CYS 148 148 148 CYS CYS B . n 
B 1 149 TRP 149 149 149 TRP TRP B . n 
B 1 150 HIS 150 150 150 HIS HIS B . n 
B 1 151 THR 151 151 151 THR THR B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 CYS 153 153 153 CYS CYS B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 TYR 156 156 156 TYR TYR B . n 
B 1 157 CYS 157 157 157 CYS CYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 TYR 160 160 160 TYR TYR B . n 
B 1 161 ASN 161 161 161 ASN ASN B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 VAL 163 163 163 VAL VAL B . n 
B 1 164 THR 164 164 164 THR THR B . n 
B 1 165 SER 165 165 165 SER SER B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 ASP 173 173 173 ASP ASP B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 ?   ?   ?   B . n 
B 1 176 THR 176 176 ?   ?   ?   B . n 
B 1 177 SER 177 177 ?   ?   ?   B . n 
B 1 178 PRO 178 178 ?   ?   ?   B . n 
B 1 179 ILE 179 179 ?   ?   ?   B . n 
B 1 180 SER 180 180 ?   ?   ?   B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 HIS 182 182 182 HIS HIS B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 TYR 184 184 184 TYR TYR B . n 
B 1 185 GLN 185 185 185 GLN GLN B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 TYR 189 189 189 TYR TYR B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 GLU 191 191 191 GLU GLU B . n 
B 1 192 LYS 192 192 192 LYS LYS B . n 
B 1 193 TRP 193 193 193 TRP TRP B . n 
B 1 194 GLU 194 194 194 GLU GLU B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 CYS 200 200 200 CYS CYS B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 HIS 204 204 204 HIS HIS B . n 
B 1 205 SER 205 205 205 SER SER B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 PHE 207 207 207 PHE PHE B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 TYR 212 212 212 TYR TYR B . n 
B 1 213 GLN 213 213 213 GLN GLN B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 THR 217 217 217 THR THR B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 THR 221 221 221 THR THR B . n 
B 1 222 ASP 222 222 222 ASP ASP B . n 
B 1 223 THR 223 223 223 THR THR B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 HIS 227 227 227 HIS HIS B . n 
B 1 228 VAL 228 228 228 VAL VAL B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 PHE 231 231 231 PHE PHE B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 TYR 233 233 233 TYR TYR B . n 
B 1 234 ASN 234 234 234 ASN ASN B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 ILE 236 236 236 ILE ILE B . n 
B 1 237 VAL 237 237 237 VAL VAL B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 GLU 239 239 ?   ?   ?   B . n 
B 1 240 PRO 240 240 ?   ?   ?   B . n 
B 1 241 GLU 241 241 ?   ?   ?   B . n 
B 1 242 GLU 242 242 ?   ?   ?   B . n 
B 1 243 HIS 243 243 ?   ?   ?   B . n 
B 1 244 VAL 244 244 ?   ?   ?   B . n 
B 1 245 GLN 245 245 ?   ?   ?   B . n 
B 1 246 ILE 246 246 ?   ?   ?   B . n 
B 1 247 HIS 247 247 ?   ?   ?   B . n 
B 1 248 THR 248 248 ?   ?   ?   B . n 
B 1 249 ILE 249 249 ?   ?   ?   B . n 
B 1 250 ASP 250 250 ?   ?   ?   B . n 
B 1 251 GLY 251 251 ?   ?   ?   B . n 
B 1 252 SER 252 252 ?   ?   ?   B . n 
B 1 253 SER 253 253 ?   ?   ?   B . n 
B 1 254 GLY 254 254 ?   ?   ?   B . n 
B 1 255 VAL 255 255 ?   ?   ?   B . n 
B 1 256 VAL 256 256 ?   ?   ?   B . n 
B 1 257 ASN 257 257 ?   ?   ?   B . n 
B 1 258 PRO 258 258 ?   ?   ?   B . n 
B 1 259 VAL 259 259 ?   ?   ?   B . n 
B 1 260 MET 260 260 ?   ?   ?   B . n 
B 1 261 GLU 261 261 ?   ?   ?   B . n 
B 1 262 PRO 262 262 ?   ?   ?   B . n 
B 1 263 ILE 263 263 ?   ?   ?   B . n 
B 1 264 TYR 264 264 ?   ?   ?   B . n 
B 1 265 ASP 265 265 ?   ?   ?   B . n 
B 1 266 GLU 266 266 ?   ?   ?   B . n 
B 1 267 PRO 267 267 ?   ?   ?   B . n 
B 1 268 THR 268 268 ?   ?   ?   B . n 
B 1 269 THR 269 269 ?   ?   ?   B . n 
B 1 270 THR 270 270 ?   ?   ?   B . n 
B 1 271 THR 271 271 ?   ?   ?   B . n 
B 1 272 SER 272 272 ?   ?   ?   B . n 
B 1 273 VAL 273 273 ?   ?   ?   B . n 
B 1 274 PRO 274 274 ?   ?   ?   B . n 
B 1 275 LEU 275 275 ?   ?   ?   B . n 
B 1 276 SER 276 276 ?   ?   ?   B . n 
B 1 277 ASN 277 277 ?   ?   ?   B . n 
B 1 278 SER 278 278 ?   ?   ?   B . n 
B 1 279 LEU 279 279 ?   ?   ?   B . n 
B 1 280 GLU 280 280 ?   ?   ?   B . n 
B 1 281 VAL 281 281 ?   ?   ?   B . n 
B 1 282 LEU 282 282 ?   ?   ?   B . n 
B 1 283 PHE 283 283 ?   ?   ?   B . n 
B 1 284 GLN 284 284 ?   ?   ?   B . n 
C 2 1   HIS 1   2   ?   ?   ?   C . n 
C 2 2   HIS 2   3   ?   ?   ?   C . n 
C 2 3   HIS 3   4   ?   ?   ?   C . n 
C 2 4   HIS 4   5   ?   ?   ?   C . n 
C 2 5   HIS 5   6   ?   ?   ?   C . n 
C 2 6   HIS 6   7   ?   ?   ?   C . n 
C 2 7   HIS 7   8   ?   ?   ?   C . n 
C 2 8   ASP 8   9   ?   ?   ?   C . n 
C 2 9   TYR 9   10  ?   ?   ?   C . n 
C 2 10  ASP 10  11  ?   ?   ?   C . n 
C 2 11  ILE 11  12  ?   ?   ?   C . n 
C 2 12  PRO 12  13  ?   ?   ?   C . n 
C 2 13  THR 13  14  ?   ?   ?   C . n 
C 2 14  THR 14  15  ?   ?   ?   C . n 
C 2 15  GLU 15  16  ?   ?   ?   C . n 
C 2 16  ASN 16  17  ?   ?   ?   C . n 
C 2 17  LEU 17  18  ?   ?   ?   C . n 
C 2 18  TYR 18  19  ?   ?   ?   C . n 
C 2 19  PHE 19  20  ?   ?   ?   C . n 
C 2 20  GLN 20  21  ?   ?   ?   C . n 
C 2 21  GLY 21  22  ?   ?   ?   C . n 
C 2 22  SER 22  23  ?   ?   ?   C . n 
C 2 23  THR 23  24  ?   ?   ?   C . n 
C 2 24  PHE 24  25  25  PHE PHE C . n 
C 2 25  SER 25  26  26  SER SER C . n 
C 2 26  LYS 26  27  27  LYS LYS C . n 
C 2 27  LEU 27  28  28  LEU LEU C . n 
C 2 28  ARG 28  29  29  ARG ARG C . n 
C 2 29  GLU 29  30  30  GLU GLU C . n 
C 2 30  GLN 30  31  31  GLN GLN C . n 
C 2 31  LEU 31  32  32  LEU LEU C . n 
C 2 32  GLY 32  33  33  GLY GLY C . n 
C 2 33  PRO 33  34  34  PRO PRO C . n 
C 2 34  VAL 34  35  35  VAL VAL C . n 
C 2 35  THR 35  36  36  THR THR C . n 
C 2 36  GLN 36  37  37  GLN GLN C . n 
C 2 37  GLU 37  38  38  GLU GLU C . n 
C 2 38  PHE 38  39  39  PHE PHE C . n 
C 2 39  TRP 39  40  40  TRP TRP C . n 
C 2 40  ASP 40  41  41  ASP ASP C . n 
C 2 41  ASN 41  42  42  ASN ASN C . n 
C 2 42  LEU 42  43  43  LEU LEU C . n 
C 2 43  GLU 43  44  44  GLU GLU C . n 
C 2 44  LYS 44  45  45  LYS LYS C . n 
C 2 45  GLU 45  46  46  GLU GLU C . n 
C 2 46  THR 46  47  47  THR THR C . n 
C 2 47  GLU 47  48  48  GLU GLU C . n 
C 2 48  GLY 48  49  49  GLY GLY C . n 
C 2 49  LEU 49  50  50  LEU LEU C . n 
C 2 50  ARG 50  51  51  ARG ARG C . n 
C 2 51  GLN 51  52  52  GLN GLN C . n 
C 2 52  GLU 52  53  53  GLU GLU C . n 
C 2 53  MET 53  54  54  MET MET C . n 
C 2 54  SER 54  55  55  SER SER C . n 
C 2 55  LYS 55  56  ?   ?   ?   C . n 
C 2 56  ASP 56  57  ?   ?   ?   C . n 
C 2 57  LEU 57  58  ?   ?   ?   C . n 
C 2 58  GLU 58  59  ?   ?   ?   C . n 
C 2 59  GLU 59  60  ?   ?   ?   C . n 
C 2 60  VAL 60  61  ?   ?   ?   C . n 
C 2 61  LYS 61  62  ?   ?   ?   C . n 
C 2 62  ALA 62  63  ?   ?   ?   C . n 
C 2 63  LYS 63  64  ?   ?   ?   C . n 
C 2 64  VAL 64  65  ?   ?   ?   C . n 
C 2 65  GLN 65  66  ?   ?   ?   C . n 
C 2 66  PRO 66  67  ?   ?   ?   C . n 
C 2 67  TYR 67  68  ?   ?   ?   C . n 
C 2 68  LEU 68  69  ?   ?   ?   C . n 
C 2 69  ASP 69  70  ?   ?   ?   C . n 
C 2 70  ASP 70  71  ?   ?   ?   C . n 
C 2 71  PHE 71  72  ?   ?   ?   C . n 
C 2 72  GLN 72  73  ?   ?   ?   C . n 
C 2 73  LYS 73  74  ?   ?   ?   C . n 
C 2 74  LYS 74  75  ?   ?   ?   C . n 
C 2 75  TRP 75  76  ?   ?   ?   C . n 
C 2 76  GLN 76  77  ?   ?   ?   C . n 
C 2 77  GLU 77  78  ?   ?   ?   C . n 
C 2 78  GLU 78  79  ?   ?   ?   C . n 
C 2 79  MET 79  80  ?   ?   ?   C . n 
C 2 80  GLU 80  81  ?   ?   ?   C . n 
C 2 81  LEU 81  82  ?   ?   ?   C . n 
C 2 82  TYR 82  83  ?   ?   ?   C . n 
C 2 83  ARG 83  84  ?   ?   ?   C . n 
C 2 84  GLN 84  85  ?   ?   ?   C . n 
C 2 85  LYS 85  86  ?   ?   ?   C . n 
C 2 86  VAL 86  87  ?   ?   ?   C . n 
C 2 87  GLU 87  88  ?   ?   ?   C . n 
C 2 88  PRO 88  89  ?   ?   ?   C . n 
C 2 89  LEU 89  90  ?   ?   ?   C . n 
C 2 90  ARG 90  91  ?   ?   ?   C . n 
C 2 91  ALA 91  92  ?   ?   ?   C . n 
C 2 92  GLU 92  93  ?   ?   ?   C . n 
C 2 93  LEU 93  94  ?   ?   ?   C . n 
C 2 94  GLN 94  95  ?   ?   ?   C . n 
C 2 95  GLU 95  96  ?   ?   ?   C . n 
C 2 96  GLY 96  97  ?   ?   ?   C . n 
C 2 97  ALA 97  98  ?   ?   ?   C . n 
C 2 98  ARG 98  99  ?   ?   ?   C . n 
C 2 99  GLN 99  100 ?   ?   ?   C . n 
C 2 100 LYS 100 101 ?   ?   ?   C . n 
C 2 101 LEU 101 102 ?   ?   ?   C . n 
C 2 102 HIS 102 103 ?   ?   ?   C . n 
C 2 103 GLU 103 104 ?   ?   ?   C . n 
C 2 104 LEU 104 105 ?   ?   ?   C . n 
C 2 105 GLN 105 106 ?   ?   ?   C . n 
C 2 106 GLU 106 107 ?   ?   ?   C . n 
C 2 107 LYS 107 108 ?   ?   ?   C . n 
C 2 108 LEU 108 109 ?   ?   ?   C . n 
C 2 109 SER 109 110 ?   ?   ?   C . n 
C 2 110 PRO 110 111 ?   ?   ?   C . n 
C 2 111 LEU 111 112 ?   ?   ?   C . n 
C 2 112 GLY 112 113 ?   ?   ?   C . n 
C 2 113 GLU 113 114 ?   ?   ?   C . n 
C 2 114 GLU 114 115 ?   ?   ?   C . n 
C 2 115 MET 115 116 ?   ?   ?   C . n 
C 2 116 ARG 116 117 ?   ?   ?   C . n 
C 2 117 ASP 117 118 ?   ?   ?   C . n 
C 2 118 ARG 118 119 ?   ?   ?   C . n 
C 2 119 ALA 119 120 ?   ?   ?   C . n 
C 2 120 ARG 120 121 ?   ?   ?   C . n 
C 2 121 ALA 121 122 ?   ?   ?   C . n 
C 2 122 HIS 122 123 ?   ?   ?   C . n 
C 2 123 VAL 123 124 ?   ?   ?   C . n 
C 2 124 ASP 124 125 ?   ?   ?   C . n 
C 2 125 ALA 125 126 ?   ?   ?   C . n 
C 2 126 LEU 126 127 ?   ?   ?   C . n 
C 2 127 ARG 127 128 ?   ?   ?   C . n 
C 2 128 THR 128 129 ?   ?   ?   C . n 
C 2 129 HIS 129 130 ?   ?   ?   C . n 
C 2 130 LEU 130 131 ?   ?   ?   C . n 
C 2 131 ALA 131 132 ?   ?   ?   C . n 
C 2 132 PRO 132 133 ?   ?   ?   C . n 
C 2 133 TYR 133 134 ?   ?   ?   C . n 
C 2 134 SER 134 135 ?   ?   ?   C . n 
C 2 135 ASP 135 136 ?   ?   ?   C . n 
C 2 136 GLU 136 137 ?   ?   ?   C . n 
C 2 137 LEU 137 138 ?   ?   ?   C . n 
C 2 138 ARG 138 139 ?   ?   ?   C . n 
C 2 139 GLN 139 140 ?   ?   ?   C . n 
C 2 140 ARG 140 141 ?   ?   ?   C . n 
C 2 141 LEU 141 142 ?   ?   ?   C . n 
C 2 142 ALA 142 143 ?   ?   ?   C . n 
C 2 143 ALA 143 144 ?   ?   ?   C . n 
C 2 144 ARG 144 145 ?   ?   ?   C . n 
C 2 145 LEU 145 146 ?   ?   ?   C . n 
C 2 146 GLU 146 147 ?   ?   ?   C . n 
C 2 147 ALA 147 148 ?   ?   ?   C . n 
C 2 148 LEU 148 149 ?   ?   ?   C . n 
C 2 149 LYS 149 150 ?   ?   ?   C . n 
C 2 150 GLU 150 151 ?   ?   ?   C . n 
C 2 151 ASN 151 152 ?   ?   ?   C . n 
C 2 152 GLY 152 153 ?   ?   ?   C . n 
C 2 153 GLY 153 154 ?   ?   ?   C . n 
C 2 154 ALA 154 155 ?   ?   ?   C . n 
C 2 155 ARG 155 156 ?   ?   ?   C . n 
C 2 156 LEU 156 157 ?   ?   ?   C . n 
C 2 157 ALA 157 158 ?   ?   ?   C . n 
C 2 158 GLU 158 159 ?   ?   ?   C . n 
C 2 159 TYR 159 160 ?   ?   ?   C . n 
C 2 160 HIS 160 161 ?   ?   ?   C . n 
C 2 161 ALA 161 162 ?   ?   ?   C . n 
C 2 162 LYS 162 163 ?   ?   ?   C . n 
C 2 163 ALA 163 164 ?   ?   ?   C . n 
C 2 164 THR 164 165 ?   ?   ?   C . n 
C 2 165 GLU 165 166 ?   ?   ?   C . n 
C 2 166 HIS 166 167 ?   ?   ?   C . n 
C 2 167 LEU 167 168 ?   ?   ?   C . n 
C 2 168 SER 168 169 ?   ?   ?   C . n 
C 2 169 THR 169 170 ?   ?   ?   C . n 
C 2 170 LEU 170 171 ?   ?   ?   C . n 
C 2 171 SER 171 172 ?   ?   ?   C . n 
C 2 172 GLU 172 173 ?   ?   ?   C . n 
C 2 173 LYS 173 174 ?   ?   ?   C . n 
C 2 174 ALA 174 175 ?   ?   ?   C . n 
C 2 175 LYS 175 176 ?   ?   ?   C . n 
C 2 176 PRO 176 177 ?   ?   ?   C . n 
C 2 177 ALA 177 178 ?   ?   ?   C . n 
C 2 178 LEU 178 179 ?   ?   ?   C . n 
C 2 179 GLU 179 180 ?   ?   ?   C . n 
C 2 180 ASP 180 181 ?   ?   ?   C . n 
C 2 181 LEU 181 182 ?   ?   ?   C . n 
C 2 182 ARG 182 183 ?   ?   ?   C . n 
C 2 183 GLN 183 184 ?   ?   ?   C . n 
C 2 184 GLY 184 185 ?   ?   ?   C . n 
C 2 185 LEU 185 186 ?   ?   ?   C . n 
C 2 186 LEU 186 187 ?   ?   ?   C . n 
C 2 187 PRO 187 188 ?   ?   ?   C . n 
C 2 188 VAL 188 189 ?   ?   ?   C . n 
C 2 189 LEU 189 190 ?   ?   ?   C . n 
C 2 190 GLU 190 191 ?   ?   ?   C . n 
C 2 191 SER 191 192 ?   ?   ?   C . n 
C 2 192 PHE 192 193 ?   ?   ?   C . n 
C 2 193 LYS 193 194 ?   ?   ?   C . n 
C 2 194 VAL 194 195 ?   ?   ?   C . n 
C 2 195 SER 195 196 ?   ?   ?   C . n 
C 2 196 PHE 196 197 ?   ?   ?   C . n 
C 2 197 LEU 197 198 ?   ?   ?   C . n 
C 2 198 SER 198 199 ?   ?   ?   C . n 
C 2 199 ALA 199 200 ?   ?   ?   C . n 
C 2 200 LEU 200 201 ?   ?   ?   C . n 
C 2 201 GLU 201 202 ?   ?   ?   C . n 
C 2 202 GLU 202 203 ?   ?   ?   C . n 
C 2 203 TYR 203 204 ?   ?   ?   C . n 
C 2 204 THR 204 205 ?   ?   ?   C . n 
C 2 205 LYS 205 206 ?   ?   ?   C . n 
C 2 206 LYS 206 207 ?   ?   ?   C . n 
C 2 207 LEU 207 208 ?   ?   ?   C . n 
C 2 208 ASN 208 209 ?   ?   ?   C . n 
C 2 209 THR 209 210 ?   ?   ?   C . n 
C 2 210 GLN 210 211 ?   ?   ?   C . n 
D 2 1   HIS 1   2   ?   ?   ?   D . n 
D 2 2   HIS 2   3   ?   ?   ?   D . n 
D 2 3   HIS 3   4   ?   ?   ?   D . n 
D 2 4   HIS 4   5   ?   ?   ?   D . n 
D 2 5   HIS 5   6   ?   ?   ?   D . n 
D 2 6   HIS 6   7   ?   ?   ?   D . n 
D 2 7   HIS 7   8   ?   ?   ?   D . n 
D 2 8   ASP 8   9   ?   ?   ?   D . n 
D 2 9   TYR 9   10  ?   ?   ?   D . n 
D 2 10  ASP 10  11  ?   ?   ?   D . n 
D 2 11  ILE 11  12  ?   ?   ?   D . n 
D 2 12  PRO 12  13  ?   ?   ?   D . n 
D 2 13  THR 13  14  ?   ?   ?   D . n 
D 2 14  THR 14  15  ?   ?   ?   D . n 
D 2 15  GLU 15  16  ?   ?   ?   D . n 
D 2 16  ASN 16  17  ?   ?   ?   D . n 
D 2 17  LEU 17  18  ?   ?   ?   D . n 
D 2 18  TYR 18  19  ?   ?   ?   D . n 
D 2 19  PHE 19  20  ?   ?   ?   D . n 
D 2 20  GLN 20  21  ?   ?   ?   D . n 
D 2 21  GLY 21  22  ?   ?   ?   D . n 
D 2 22  SER 22  23  ?   ?   ?   D . n 
D 2 23  THR 23  24  ?   ?   ?   D . n 
D 2 24  PHE 24  25  25  PHE PHE D . n 
D 2 25  SER 25  26  26  SER SER D . n 
D 2 26  LYS 26  27  27  LYS LYS D . n 
D 2 27  LEU 27  28  28  LEU LEU D . n 
D 2 28  ARG 28  29  29  ARG ARG D . n 
D 2 29  GLU 29  30  30  GLU GLU D . n 
D 2 30  GLN 30  31  31  GLN GLN D . n 
D 2 31  LEU 31  32  32  LEU LEU D . n 
D 2 32  GLY 32  33  33  GLY GLY D . n 
D 2 33  PRO 33  34  34  PRO PRO D . n 
D 2 34  VAL 34  35  35  VAL VAL D . n 
D 2 35  THR 35  36  36  THR THR D . n 
D 2 36  GLN 36  37  37  GLN GLN D . n 
D 2 37  GLU 37  38  38  GLU GLU D . n 
D 2 38  PHE 38  39  39  PHE PHE D . n 
D 2 39  TRP 39  40  40  TRP TRP D . n 
D 2 40  ASP 40  41  41  ASP ASP D . n 
D 2 41  ASN 41  42  42  ASN ASN D . n 
D 2 42  LEU 42  43  43  LEU LEU D . n 
D 2 43  GLU 43  44  44  GLU GLU D . n 
D 2 44  LYS 44  45  45  LYS LYS D . n 
D 2 45  GLU 45  46  46  GLU GLU D . n 
D 2 46  THR 46  47  47  THR THR D . n 
D 2 47  GLU 47  48  48  GLU GLU D . n 
D 2 48  GLY 48  49  49  GLY GLY D . n 
D 2 49  LEU 49  50  50  LEU LEU D . n 
D 2 50  ARG 50  51  51  ARG ARG D . n 
D 2 51  GLN 51  52  52  GLN GLN D . n 
D 2 52  GLU 52  53  53  GLU GLU D . n 
D 2 53  MET 53  54  54  MET MET D . n 
D 2 54  SER 54  55  55  SER SER D . n 
D 2 55  LYS 55  56  ?   ?   ?   D . n 
D 2 56  ASP 56  57  ?   ?   ?   D . n 
D 2 57  LEU 57  58  ?   ?   ?   D . n 
D 2 58  GLU 58  59  ?   ?   ?   D . n 
D 2 59  GLU 59  60  ?   ?   ?   D . n 
D 2 60  VAL 60  61  ?   ?   ?   D . n 
D 2 61  LYS 61  62  ?   ?   ?   D . n 
D 2 62  ALA 62  63  ?   ?   ?   D . n 
D 2 63  LYS 63  64  ?   ?   ?   D . n 
D 2 64  VAL 64  65  ?   ?   ?   D . n 
D 2 65  GLN 65  66  ?   ?   ?   D . n 
D 2 66  PRO 66  67  ?   ?   ?   D . n 
D 2 67  TYR 67  68  ?   ?   ?   D . n 
D 2 68  LEU 68  69  ?   ?   ?   D . n 
D 2 69  ASP 69  70  ?   ?   ?   D . n 
D 2 70  ASP 70  71  ?   ?   ?   D . n 
D 2 71  PHE 71  72  ?   ?   ?   D . n 
D 2 72  GLN 72  73  ?   ?   ?   D . n 
D 2 73  LYS 73  74  ?   ?   ?   D . n 
D 2 74  LYS 74  75  ?   ?   ?   D . n 
D 2 75  TRP 75  76  ?   ?   ?   D . n 
D 2 76  GLN 76  77  ?   ?   ?   D . n 
D 2 77  GLU 77  78  ?   ?   ?   D . n 
D 2 78  GLU 78  79  ?   ?   ?   D . n 
D 2 79  MET 79  80  ?   ?   ?   D . n 
D 2 80  GLU 80  81  ?   ?   ?   D . n 
D 2 81  LEU 81  82  ?   ?   ?   D . n 
D 2 82  TYR 82  83  ?   ?   ?   D . n 
D 2 83  ARG 83  84  ?   ?   ?   D . n 
D 2 84  GLN 84  85  ?   ?   ?   D . n 
D 2 85  LYS 85  86  ?   ?   ?   D . n 
D 2 86  VAL 86  87  ?   ?   ?   D . n 
D 2 87  GLU 87  88  ?   ?   ?   D . n 
D 2 88  PRO 88  89  ?   ?   ?   D . n 
D 2 89  LEU 89  90  ?   ?   ?   D . n 
D 2 90  ARG 90  91  ?   ?   ?   D . n 
D 2 91  ALA 91  92  ?   ?   ?   D . n 
D 2 92  GLU 92  93  ?   ?   ?   D . n 
D 2 93  LEU 93  94  ?   ?   ?   D . n 
D 2 94  GLN 94  95  ?   ?   ?   D . n 
D 2 95  GLU 95  96  ?   ?   ?   D . n 
D 2 96  GLY 96  97  ?   ?   ?   D . n 
D 2 97  ALA 97  98  ?   ?   ?   D . n 
D 2 98  ARG 98  99  ?   ?   ?   D . n 
D 2 99  GLN 99  100 ?   ?   ?   D . n 
D 2 100 LYS 100 101 ?   ?   ?   D . n 
D 2 101 LEU 101 102 ?   ?   ?   D . n 
D 2 102 HIS 102 103 ?   ?   ?   D . n 
D 2 103 GLU 103 104 ?   ?   ?   D . n 
D 2 104 LEU 104 105 ?   ?   ?   D . n 
D 2 105 GLN 105 106 ?   ?   ?   D . n 
D 2 106 GLU 106 107 ?   ?   ?   D . n 
D 2 107 LYS 107 108 ?   ?   ?   D . n 
D 2 108 LEU 108 109 ?   ?   ?   D . n 
D 2 109 SER 109 110 ?   ?   ?   D . n 
D 2 110 PRO 110 111 ?   ?   ?   D . n 
D 2 111 LEU 111 112 ?   ?   ?   D . n 
D 2 112 GLY 112 113 ?   ?   ?   D . n 
D 2 113 GLU 113 114 ?   ?   ?   D . n 
D 2 114 GLU 114 115 ?   ?   ?   D . n 
D 2 115 MET 115 116 ?   ?   ?   D . n 
D 2 116 ARG 116 117 ?   ?   ?   D . n 
D 2 117 ASP 117 118 ?   ?   ?   D . n 
D 2 118 ARG 118 119 ?   ?   ?   D . n 
D 2 119 ALA 119 120 ?   ?   ?   D . n 
D 2 120 ARG 120 121 ?   ?   ?   D . n 
D 2 121 ALA 121 122 ?   ?   ?   D . n 
D 2 122 HIS 122 123 ?   ?   ?   D . n 
D 2 123 VAL 123 124 ?   ?   ?   D . n 
D 2 124 ASP 124 125 ?   ?   ?   D . n 
D 2 125 ALA 125 126 ?   ?   ?   D . n 
D 2 126 LEU 126 127 ?   ?   ?   D . n 
D 2 127 ARG 127 128 ?   ?   ?   D . n 
D 2 128 THR 128 129 ?   ?   ?   D . n 
D 2 129 HIS 129 130 ?   ?   ?   D . n 
D 2 130 LEU 130 131 ?   ?   ?   D . n 
D 2 131 ALA 131 132 ?   ?   ?   D . n 
D 2 132 PRO 132 133 ?   ?   ?   D . n 
D 2 133 TYR 133 134 ?   ?   ?   D . n 
D 2 134 SER 134 135 ?   ?   ?   D . n 
D 2 135 ASP 135 136 ?   ?   ?   D . n 
D 2 136 GLU 136 137 ?   ?   ?   D . n 
D 2 137 LEU 137 138 ?   ?   ?   D . n 
D 2 138 ARG 138 139 ?   ?   ?   D . n 
D 2 139 GLN 139 140 ?   ?   ?   D . n 
D 2 140 ARG 140 141 ?   ?   ?   D . n 
D 2 141 LEU 141 142 ?   ?   ?   D . n 
D 2 142 ALA 142 143 ?   ?   ?   D . n 
D 2 143 ALA 143 144 ?   ?   ?   D . n 
D 2 144 ARG 144 145 ?   ?   ?   D . n 
D 2 145 LEU 145 146 ?   ?   ?   D . n 
D 2 146 GLU 146 147 ?   ?   ?   D . n 
D 2 147 ALA 147 148 ?   ?   ?   D . n 
D 2 148 LEU 148 149 ?   ?   ?   D . n 
D 2 149 LYS 149 150 ?   ?   ?   D . n 
D 2 150 GLU 150 151 ?   ?   ?   D . n 
D 2 151 ASN 151 152 ?   ?   ?   D . n 
D 2 152 GLY 152 153 ?   ?   ?   D . n 
D 2 153 GLY 153 154 ?   ?   ?   D . n 
D 2 154 ALA 154 155 ?   ?   ?   D . n 
D 2 155 ARG 155 156 ?   ?   ?   D . n 
D 2 156 LEU 156 157 ?   ?   ?   D . n 
D 2 157 ALA 157 158 ?   ?   ?   D . n 
D 2 158 GLU 158 159 ?   ?   ?   D . n 
D 2 159 TYR 159 160 ?   ?   ?   D . n 
D 2 160 HIS 160 161 ?   ?   ?   D . n 
D 2 161 ALA 161 162 ?   ?   ?   D . n 
D 2 162 LYS 162 163 ?   ?   ?   D . n 
D 2 163 ALA 163 164 ?   ?   ?   D . n 
D 2 164 THR 164 165 ?   ?   ?   D . n 
D 2 165 GLU 165 166 ?   ?   ?   D . n 
D 2 166 HIS 166 167 ?   ?   ?   D . n 
D 2 167 LEU 167 168 ?   ?   ?   D . n 
D 2 168 SER 168 169 ?   ?   ?   D . n 
D 2 169 THR 169 170 ?   ?   ?   D . n 
D 2 170 LEU 170 171 ?   ?   ?   D . n 
D 2 171 SER 171 172 ?   ?   ?   D . n 
D 2 172 GLU 172 173 ?   ?   ?   D . n 
D 2 173 LYS 173 174 ?   ?   ?   D . n 
D 2 174 ALA 174 175 ?   ?   ?   D . n 
D 2 175 LYS 175 176 ?   ?   ?   D . n 
D 2 176 PRO 176 177 ?   ?   ?   D . n 
D 2 177 ALA 177 178 ?   ?   ?   D . n 
D 2 178 LEU 178 179 ?   ?   ?   D . n 
D 2 179 GLU 179 180 ?   ?   ?   D . n 
D 2 180 ASP 180 181 ?   ?   ?   D . n 
D 2 181 LEU 181 182 ?   ?   ?   D . n 
D 2 182 ARG 182 183 ?   ?   ?   D . n 
D 2 183 GLN 183 184 ?   ?   ?   D . n 
D 2 184 GLY 184 185 ?   ?   ?   D . n 
D 2 185 LEU 185 186 ?   ?   ?   D . n 
D 2 186 LEU 186 187 ?   ?   ?   D . n 
D 2 187 PRO 187 188 ?   ?   ?   D . n 
D 2 188 VAL 188 189 ?   ?   ?   D . n 
D 2 189 LEU 189 190 ?   ?   ?   D . n 
D 2 190 GLU 190 191 ?   ?   ?   D . n 
D 2 191 SER 191 192 ?   ?   ?   D . n 
D 2 192 PHE 192 193 ?   ?   ?   D . n 
D 2 193 LYS 193 194 ?   ?   ?   D . n 
D 2 194 VAL 194 195 ?   ?   ?   D . n 
D 2 195 SER 195 196 ?   ?   ?   D . n 
D 2 196 PHE 196 197 ?   ?   ?   D . n 
D 2 197 LEU 197 198 ?   ?   ?   D . n 
D 2 198 SER 198 199 ?   ?   ?   D . n 
D 2 199 ALA 199 200 ?   ?   ?   D . n 
D 2 200 LEU 200 201 ?   ?   ?   D . n 
D 2 201 GLU 201 202 ?   ?   ?   D . n 
D 2 202 GLU 202 203 ?   ?   ?   D . n 
D 2 203 TYR 203 204 ?   ?   ?   D . n 
D 2 204 THR 204 205 ?   ?   ?   D . n 
D 2 205 LYS 205 206 ?   ?   ?   D . n 
D 2 206 LYS 206 207 ?   ?   ?   D . n 
D 2 207 LEU 207 208 ?   ?   ?   D . n 
D 2 208 ASN 208 209 ?   ?   ?   D . n 
D 2 209 THR 209 210 ?   ?   ?   D . n 
D 2 210 GLN 210 211 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 PEE 1  301 301 PEE PEE A . 
F 3 PEE 1  301 301 PEE PEE B . 
G 4 HOH 1  401 66  HOH HOH A . 
G 4 HOH 2  402 72  HOH HOH A . 
G 4 HOH 3  403 97  HOH HOH A . 
G 4 HOH 4  404 79  HOH HOH A . 
G 4 HOH 5  405 3   HOH HOH A . 
G 4 HOH 6  406 24  HOH HOH A . 
G 4 HOH 7  407 136 HOH HOH A . 
G 4 HOH 8  408 27  HOH HOH A . 
G 4 HOH 9  409 99  HOH HOH A . 
G 4 HOH 10 410 25  HOH HOH A . 
G 4 HOH 11 411 71  HOH HOH A . 
G 4 HOH 12 412 11  HOH HOH A . 
G 4 HOH 13 413 8   HOH HOH A . 
G 4 HOH 14 414 34  HOH HOH A . 
G 4 HOH 15 415 58  HOH HOH A . 
G 4 HOH 16 416 5   HOH HOH A . 
G 4 HOH 17 417 89  HOH HOH A . 
G 4 HOH 18 418 92  HOH HOH A . 
G 4 HOH 19 419 15  HOH HOH A . 
G 4 HOH 20 420 98  HOH HOH A . 
G 4 HOH 21 421 84  HOH HOH A . 
G 4 HOH 22 422 19  HOH HOH A . 
G 4 HOH 23 423 81  HOH HOH A . 
G 4 HOH 24 424 43  HOH HOH A . 
G 4 HOH 25 425 33  HOH HOH A . 
G 4 HOH 26 426 42  HOH HOH A . 
G 4 HOH 27 427 94  HOH HOH A . 
G 4 HOH 28 428 22  HOH HOH A . 
G 4 HOH 29 429 113 HOH HOH A . 
G 4 HOH 30 430 95  HOH HOH A . 
G 4 HOH 31 431 121 HOH HOH A . 
G 4 HOH 32 432 57  HOH HOH A . 
G 4 HOH 33 433 40  HOH HOH A . 
G 4 HOH 34 434 88  HOH HOH A . 
G 4 HOH 35 435 31  HOH HOH A . 
G 4 HOH 36 436 1   HOH HOH A . 
G 4 HOH 37 437 70  HOH HOH A . 
G 4 HOH 38 438 96  HOH HOH A . 
G 4 HOH 39 439 38  HOH HOH A . 
G 4 HOH 40 440 39  HOH HOH A . 
G 4 HOH 41 441 124 HOH HOH A . 
G 4 HOH 42 442 55  HOH HOH A . 
G 4 HOH 43 443 91  HOH HOH A . 
G 4 HOH 44 444 93  HOH HOH A . 
G 4 HOH 45 445 37  HOH HOH A . 
G 4 HOH 46 446 13  HOH HOH A . 
G 4 HOH 47 447 56  HOH HOH A . 
G 4 HOH 48 448 4   HOH HOH A . 
G 4 HOH 49 449 76  HOH HOH A . 
G 4 HOH 50 450 32  HOH HOH A . 
G 4 HOH 51 451 118 HOH HOH A . 
G 4 HOH 52 452 62  HOH HOH A . 
G 4 HOH 53 453 130 HOH HOH A . 
G 4 HOH 54 454 123 HOH HOH A . 
G 4 HOH 55 455 63  HOH HOH A . 
G 4 HOH 56 456 80  HOH HOH A . 
G 4 HOH 57 457 117 HOH HOH A . 
G 4 HOH 58 458 112 HOH HOH A . 
G 4 HOH 59 459 7   HOH HOH A . 
G 4 HOH 60 460 122 HOH HOH A . 
G 4 HOH 61 461 68  HOH HOH A . 
H 4 HOH 1  401 120 HOH HOH B . 
H 4 HOH 2  402 65  HOH HOH B . 
H 4 HOH 3  403 114 HOH HOH B . 
H 4 HOH 4  404 73  HOH HOH B . 
H 4 HOH 5  405 36  HOH HOH B . 
H 4 HOH 6  406 102 HOH HOH B . 
H 4 HOH 7  407 109 HOH HOH B . 
H 4 HOH 8  408 82  HOH HOH B . 
H 4 HOH 9  409 26  HOH HOH B . 
H 4 HOH 10 410 135 HOH HOH B . 
H 4 HOH 11 411 9   HOH HOH B . 
H 4 HOH 12 412 10  HOH HOH B . 
H 4 HOH 13 413 21  HOH HOH B . 
H 4 HOH 14 414 16  HOH HOH B . 
H 4 HOH 15 415 105 HOH HOH B . 
H 4 HOH 16 416 41  HOH HOH B . 
H 4 HOH 17 417 48  HOH HOH B . 
H 4 HOH 18 418 74  HOH HOH B . 
H 4 HOH 19 419 50  HOH HOH B . 
H 4 HOH 20 420 106 HOH HOH B . 
H 4 HOH 21 421 6   HOH HOH B . 
H 4 HOH 22 422 35  HOH HOH B . 
H 4 HOH 23 423 23  HOH HOH B . 
H 4 HOH 24 424 18  HOH HOH B . 
H 4 HOH 25 425 46  HOH HOH B . 
H 4 HOH 26 426 108 HOH HOH B . 
H 4 HOH 27 427 111 HOH HOH B . 
H 4 HOH 28 428 20  HOH HOH B . 
H 4 HOH 29 429 134 HOH HOH B . 
H 4 HOH 30 430 45  HOH HOH B . 
H 4 HOH 31 431 90  HOH HOH B . 
H 4 HOH 32 432 29  HOH HOH B . 
H 4 HOH 33 433 119 HOH HOH B . 
H 4 HOH 34 434 101 HOH HOH B . 
H 4 HOH 35 435 2   HOH HOH B . 
H 4 HOH 36 436 69  HOH HOH B . 
H 4 HOH 37 437 104 HOH HOH B . 
H 4 HOH 38 438 28  HOH HOH B . 
H 4 HOH 39 439 30  HOH HOH B . 
H 4 HOH 40 440 44  HOH HOH B . 
H 4 HOH 41 441 100 HOH HOH B . 
H 4 HOH 42 442 126 HOH HOH B . 
H 4 HOH 43 443 103 HOH HOH B . 
H 4 HOH 44 444 115 HOH HOH B . 
H 4 HOH 45 445 14  HOH HOH B . 
H 4 HOH 46 446 110 HOH HOH B . 
H 4 HOH 47 447 17  HOH HOH B . 
H 4 HOH 48 448 107 HOH HOH B . 
H 4 HOH 49 449 52  HOH HOH B . 
H 4 HOH 50 450 128 HOH HOH B . 
H 4 HOH 51 451 47  HOH HOH B . 
H 4 HOH 52 452 83  HOH HOH B . 
H 4 HOH 53 453 61  HOH HOH B . 
H 4 HOH 54 454 51  HOH HOH B . 
H 4 HOH 55 455 64  HOH HOH B . 
H 4 HOH 56 456 129 HOH HOH B . 
H 4 HOH 57 457 116 HOH HOH B . 
H 4 HOH 58 458 53  HOH HOH B . 
H 4 HOH 59 459 67  HOH HOH B . 
H 4 HOH 60 460 12  HOH HOH B . 
H 4 HOH 61 461 49  HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9370  ? 
1 MORE         -82   ? 
1 'SSA (A^2)'  22010 ? 
# 
_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   ? 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2020-11-18 
2 'Structure model' 1 1 2021-01-27 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' entity          
2 2 'Structure model' entity_name_com 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_entity.pdbx_description' 
2 2 'Structure model' '_entity_name_com.name'    
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement ? ? 'Paul D. Adams' pdadams@lbl.gov ? ? ? ? Python/C++ https://www.phenix-online.org/ ? phenix.real_space_refine ? ? 
program 1.18.2_3874 1 
? refinement ? ? 'Paul D. Adams' pdadams@lbl.gov ? ? ? ? Python/C++ https://www.phenix-online.org/ ? PHENIX                   ? ? 
program 1.18.2_3874 2 
# 
_pdbx_entry_details.entry_id                 7KJR 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
_em_3d_fitting.entry_id          7KJR 
_em_3d_fitting.id                1 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_protocol      ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.method            ? 
# 
_em_3d_reconstruction.entry_id                    7KJR 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.num_class_averages          1 
_em_3d_reconstruction.num_particles               91218 
_em_3d_reconstruction.resolution                  2.08 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.symmetry_type               POINT 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.magnification_calibration   ? 
# 
_em_buffer.id            1 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.details              ? 
_em_entity_assembly.name                 'SARS-CoV-2 protein 3A in lipid nanodiscs' 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.entity_id_list       1,2 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
# 
_em_imaging.id                              1 
_em_imaging.entry_id                        7KJR 
_em_imaging.accelerating_voltage            300 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.cryogen                         ? 
_em_imaging.details                         ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_max             ? 
_em_imaging.nominal_defocus_min             ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.specimen_id                     1 
_em_imaging.citation_id                     ? 
_em_imaging.date                            ? 
_em_imaging.temperature                     ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.astigmatism                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.specimen_holder_type            ? 
# 
_em_sample_support.id               1 
_em_sample_support.specimen_id      1 
_em_sample_support.details          ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.method           ? 
_em_sample_support.film_material    ? 
# 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.chamber_temperature   277 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.details               
;1 blot force 
5 second wait time
3 second blot time
;
_em_vitrification.humidity              100 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.entry_id              7KJR 
_em_vitrification.citation_id           ? 
_em_vitrification.method                ? 
_em_vitrification.temp                  ? 
_em_vitrification.time_resolved_state   ? 
# 
_em_experiment.entry_id                7KJR 
_em_experiment.id                      1 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.entity_assembly_id      1 
# 
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 LEU A 65  ? ? -103.90 74.51   
2 1 SER A 205 ? ? -126.86 -168.47 
3 1 LEU B 65  ? ? -100.74 63.72   
4 1 PRO B 104 ? ? -68.05  5.42    
5 1 SER B 205 ? ? -126.39 -167.57 
# 
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 N 1 A PEE 301 ? C14 ? E PEE 1 C14 
2  1 N 1 A PEE 301 ? C15 ? E PEE 1 C15 
3  1 N 1 A PEE 301 ? C16 ? E PEE 1 C16 
4  1 N 1 A PEE 301 ? C17 ? E PEE 1 C17 
5  1 N 1 A PEE 301 ? C18 ? E PEE 1 C18 
6  1 N 1 A PEE 301 ? C19 ? E PEE 1 C19 
7  1 N 1 A PEE 301 ? C20 ? E PEE 1 C20 
8  1 N 1 A PEE 301 ? C21 ? E PEE 1 C21 
9  1 N 1 A PEE 301 ? C22 ? E PEE 1 C22 
10 1 N 1 A PEE 301 ? C23 ? E PEE 1 C23 
11 1 N 1 A PEE 301 ? C24 ? E PEE 1 C24 
12 1 N 1 A PEE 301 ? C25 ? E PEE 1 C25 
13 1 N 1 A PEE 301 ? C26 ? E PEE 1 C26 
14 1 N 1 A PEE 301 ? C27 ? E PEE 1 C27 
15 1 N 1 A PEE 301 ? C34 ? E PEE 1 C34 
16 1 N 1 A PEE 301 ? C35 ? E PEE 1 C35 
17 1 N 1 A PEE 301 ? C36 ? E PEE 1 C36 
18 1 N 1 A PEE 301 ? C37 ? E PEE 1 C37 
19 1 N 1 A PEE 301 ? C38 ? E PEE 1 C38 
20 1 N 1 A PEE 301 ? C39 ? E PEE 1 C39 
21 1 N 1 A PEE 301 ? C40 ? E PEE 1 C40 
22 1 N 1 A PEE 301 ? C41 ? E PEE 1 C41 
23 1 N 1 A PEE 301 ? C42 ? E PEE 1 C42 
24 1 N 1 A PEE 301 ? C43 ? E PEE 1 C43 
25 1 N 1 A PEE 301 ? C44 ? E PEE 1 C44 
26 1 N 1 A PEE 301 ? C45 ? E PEE 1 C45 
27 1 N 1 A PEE 301 ? C46 ? E PEE 1 C46 
28 1 N 1 A PEE 301 ? C47 ? E PEE 1 C47 
29 1 N 1 B PEE 301 ? C14 ? F PEE 1 C14 
30 1 N 1 B PEE 301 ? C15 ? F PEE 1 C15 
31 1 N 1 B PEE 301 ? C16 ? F PEE 1 C16 
32 1 N 1 B PEE 301 ? C17 ? F PEE 1 C17 
33 1 N 1 B PEE 301 ? C18 ? F PEE 1 C18 
34 1 N 1 B PEE 301 ? C19 ? F PEE 1 C19 
35 1 N 1 B PEE 301 ? C20 ? F PEE 1 C20 
36 1 N 1 B PEE 301 ? C21 ? F PEE 1 C21 
37 1 N 1 B PEE 301 ? C22 ? F PEE 1 C22 
38 1 N 1 B PEE 301 ? C23 ? F PEE 1 C23 
39 1 N 1 B PEE 301 ? C24 ? F PEE 1 C24 
40 1 N 1 B PEE 301 ? C25 ? F PEE 1 C25 
41 1 N 1 B PEE 301 ? C26 ? F PEE 1 C26 
42 1 N 1 B PEE 301 ? C27 ? F PEE 1 C27 
43 1 N 1 B PEE 301 ? C34 ? F PEE 1 C34 
44 1 N 1 B PEE 301 ? C35 ? F PEE 1 C35 
45 1 N 1 B PEE 301 ? C36 ? F PEE 1 C36 
46 1 N 1 B PEE 301 ? C37 ? F PEE 1 C37 
47 1 N 1 B PEE 301 ? C38 ? F PEE 1 C38 
48 1 N 1 B PEE 301 ? C39 ? F PEE 1 C39 
49 1 N 1 B PEE 301 ? C40 ? F PEE 1 C40 
50 1 N 1 B PEE 301 ? C41 ? F PEE 1 C41 
51 1 N 1 B PEE 301 ? C42 ? F PEE 1 C42 
52 1 N 1 B PEE 301 ? C43 ? F PEE 1 C43 
53 1 N 1 B PEE 301 ? C44 ? F PEE 1 C44 
54 1 N 1 B PEE 301 ? C45 ? F PEE 1 C45 
55 1 N 1 B PEE 301 ? C46 ? F PEE 1 C46 
56 1 N 1 B PEE 301 ? C47 ? F PEE 1 C47 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ASP 2   ? A ASP 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A PHE 4   ? A PHE 4   
5   1 Y 1 A MET 5   ? A MET 5   
6   1 Y 1 A ARG 6   ? A ARG 6   
7   1 Y 1 A ILE 7   ? A ILE 7   
8   1 Y 1 A PHE 8   ? A PHE 8   
9   1 Y 1 A THR 9   ? A THR 9   
10  1 Y 1 A ILE 10  ? A ILE 10  
11  1 Y 1 A GLY 11  ? A GLY 11  
12  1 Y 1 A THR 12  ? A THR 12  
13  1 Y 1 A VAL 13  ? A VAL 13  
14  1 Y 1 A THR 14  ? A THR 14  
15  1 Y 1 A LEU 15  ? A LEU 15  
16  1 Y 1 A LYS 16  ? A LYS 16  
17  1 Y 1 A GLN 17  ? A GLN 17  
18  1 Y 1 A GLY 18  ? A GLY 18  
19  1 Y 1 A GLU 19  ? A GLU 19  
20  1 Y 1 A ILE 20  ? A ILE 20  
21  1 Y 1 A LYS 21  ? A LYS 21  
22  1 Y 1 A ASP 22  ? A ASP 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A THR 24  ? A THR 24  
25  1 Y 1 A PRO 25  ? A PRO 25  
26  1 Y 1 A SER 26  ? A SER 26  
27  1 Y 1 A ASP 27  ? A ASP 27  
28  1 Y 1 A PHE 28  ? A PHE 28  
29  1 Y 1 A VAL 29  ? A VAL 29  
30  1 Y 1 A ARG 30  ? A ARG 30  
31  1 Y 1 A ALA 31  ? A ALA 31  
32  1 Y 1 A THR 32  ? A THR 32  
33  1 Y 1 A ALA 33  ? A ALA 33  
34  1 Y 1 A THR 34  ? A THR 34  
35  1 Y 1 A ILE 35  ? A ILE 35  
36  1 Y 1 A PRO 36  ? A PRO 36  
37  1 Y 1 A ILE 37  ? A ILE 37  
38  1 Y 1 A GLN 38  ? A GLN 38  
39  1 Y 1 A ALA 39  ? A ALA 39  
40  1 Y 1 A THR 175 ? A THR 175 
41  1 Y 1 A THR 176 ? A THR 176 
42  1 Y 1 A SER 177 ? A SER 177 
43  1 Y 1 A PRO 178 ? A PRO 178 
44  1 Y 1 A ILE 179 ? A ILE 179 
45  1 Y 1 A SER 180 ? A SER 180 
46  1 Y 1 A GLU 239 ? A GLU 239 
47  1 Y 1 A PRO 240 ? A PRO 240 
48  1 Y 1 A GLU 241 ? A GLU 241 
49  1 Y 1 A GLU 242 ? A GLU 242 
50  1 Y 1 A HIS 243 ? A HIS 243 
51  1 Y 1 A VAL 244 ? A VAL 244 
52  1 Y 1 A GLN 245 ? A GLN 245 
53  1 Y 1 A ILE 246 ? A ILE 246 
54  1 Y 1 A HIS 247 ? A HIS 247 
55  1 Y 1 A THR 248 ? A THR 248 
56  1 Y 1 A ILE 249 ? A ILE 249 
57  1 Y 1 A ASP 250 ? A ASP 250 
58  1 Y 1 A GLY 251 ? A GLY 251 
59  1 Y 1 A SER 252 ? A SER 252 
60  1 Y 1 A SER 253 ? A SER 253 
61  1 Y 1 A GLY 254 ? A GLY 254 
62  1 Y 1 A VAL 255 ? A VAL 255 
63  1 Y 1 A VAL 256 ? A VAL 256 
64  1 Y 1 A ASN 257 ? A ASN 257 
65  1 Y 1 A PRO 258 ? A PRO 258 
66  1 Y 1 A VAL 259 ? A VAL 259 
67  1 Y 1 A MET 260 ? A MET 260 
68  1 Y 1 A GLU 261 ? A GLU 261 
69  1 Y 1 A PRO 262 ? A PRO 262 
70  1 Y 1 A ILE 263 ? A ILE 263 
71  1 Y 1 A TYR 264 ? A TYR 264 
72  1 Y 1 A ASP 265 ? A ASP 265 
73  1 Y 1 A GLU 266 ? A GLU 266 
74  1 Y 1 A PRO 267 ? A PRO 267 
75  1 Y 1 A THR 268 ? A THR 268 
76  1 Y 1 A THR 269 ? A THR 269 
77  1 Y 1 A THR 270 ? A THR 270 
78  1 Y 1 A THR 271 ? A THR 271 
79  1 Y 1 A SER 272 ? A SER 272 
80  1 Y 1 A VAL 273 ? A VAL 273 
81  1 Y 1 A PRO 274 ? A PRO 274 
82  1 Y 1 A LEU 275 ? A LEU 275 
83  1 Y 1 A SER 276 ? A SER 276 
84  1 Y 1 A ASN 277 ? A ASN 277 
85  1 Y 1 A SER 278 ? A SER 278 
86  1 Y 1 A LEU 279 ? A LEU 279 
87  1 Y 1 A GLU 280 ? A GLU 280 
88  1 Y 1 A VAL 281 ? A VAL 281 
89  1 Y 1 A LEU 282 ? A LEU 282 
90  1 Y 1 A PHE 283 ? A PHE 283 
91  1 Y 1 A GLN 284 ? A GLN 284 
92  1 Y 1 B MET 1   ? B MET 1   
93  1 Y 1 B ASP 2   ? B ASP 2   
94  1 Y 1 B LEU 3   ? B LEU 3   
95  1 Y 1 B PHE 4   ? B PHE 4   
96  1 Y 1 B MET 5   ? B MET 5   
97  1 Y 1 B ARG 6   ? B ARG 6   
98  1 Y 1 B ILE 7   ? B ILE 7   
99  1 Y 1 B PHE 8   ? B PHE 8   
100 1 Y 1 B THR 9   ? B THR 9   
101 1 Y 1 B ILE 10  ? B ILE 10  
102 1 Y 1 B GLY 11  ? B GLY 11  
103 1 Y 1 B THR 12  ? B THR 12  
104 1 Y 1 B VAL 13  ? B VAL 13  
105 1 Y 1 B THR 14  ? B THR 14  
106 1 Y 1 B LEU 15  ? B LEU 15  
107 1 Y 1 B LYS 16  ? B LYS 16  
108 1 Y 1 B GLN 17  ? B GLN 17  
109 1 Y 1 B GLY 18  ? B GLY 18  
110 1 Y 1 B GLU 19  ? B GLU 19  
111 1 Y 1 B ILE 20  ? B ILE 20  
112 1 Y 1 B LYS 21  ? B LYS 21  
113 1 Y 1 B ASP 22  ? B ASP 22  
114 1 Y 1 B ALA 23  ? B ALA 23  
115 1 Y 1 B THR 24  ? B THR 24  
116 1 Y 1 B PRO 25  ? B PRO 25  
117 1 Y 1 B SER 26  ? B SER 26  
118 1 Y 1 B ASP 27  ? B ASP 27  
119 1 Y 1 B PHE 28  ? B PHE 28  
120 1 Y 1 B VAL 29  ? B VAL 29  
121 1 Y 1 B ARG 30  ? B ARG 30  
122 1 Y 1 B ALA 31  ? B ALA 31  
123 1 Y 1 B THR 32  ? B THR 32  
124 1 Y 1 B ALA 33  ? B ALA 33  
125 1 Y 1 B THR 34  ? B THR 34  
126 1 Y 1 B ILE 35  ? B ILE 35  
127 1 Y 1 B PRO 36  ? B PRO 36  
128 1 Y 1 B ILE 37  ? B ILE 37  
129 1 Y 1 B GLN 38  ? B GLN 38  
130 1 Y 1 B ALA 39  ? B ALA 39  
131 1 Y 1 B THR 175 ? B THR 175 
132 1 Y 1 B THR 176 ? B THR 176 
133 1 Y 1 B SER 177 ? B SER 177 
134 1 Y 1 B PRO 178 ? B PRO 178 
135 1 Y 1 B ILE 179 ? B ILE 179 
136 1 Y 1 B SER 180 ? B SER 180 
137 1 Y 1 B GLU 239 ? B GLU 239 
138 1 Y 1 B PRO 240 ? B PRO 240 
139 1 Y 1 B GLU 241 ? B GLU 241 
140 1 Y 1 B GLU 242 ? B GLU 242 
141 1 Y 1 B HIS 243 ? B HIS 243 
142 1 Y 1 B VAL 244 ? B VAL 244 
143 1 Y 1 B GLN 245 ? B GLN 245 
144 1 Y 1 B ILE 246 ? B ILE 246 
145 1 Y 1 B HIS 247 ? B HIS 247 
146 1 Y 1 B THR 248 ? B THR 248 
147 1 Y 1 B ILE 249 ? B ILE 249 
148 1 Y 1 B ASP 250 ? B ASP 250 
149 1 Y 1 B GLY 251 ? B GLY 251 
150 1 Y 1 B SER 252 ? B SER 252 
151 1 Y 1 B SER 253 ? B SER 253 
152 1 Y 1 B GLY 254 ? B GLY 254 
153 1 Y 1 B VAL 255 ? B VAL 255 
154 1 Y 1 B VAL 256 ? B VAL 256 
155 1 Y 1 B ASN 257 ? B ASN 257 
156 1 Y 1 B PRO 258 ? B PRO 258 
157 1 Y 1 B VAL 259 ? B VAL 259 
158 1 Y 1 B MET 260 ? B MET 260 
159 1 Y 1 B GLU 261 ? B GLU 261 
160 1 Y 1 B PRO 262 ? B PRO 262 
161 1 Y 1 B ILE 263 ? B ILE 263 
162 1 Y 1 B TYR 264 ? B TYR 264 
163 1 Y 1 B ASP 265 ? B ASP 265 
164 1 Y 1 B GLU 266 ? B GLU 266 
165 1 Y 1 B PRO 267 ? B PRO 267 
166 1 Y 1 B THR 268 ? B THR 268 
167 1 Y 1 B THR 269 ? B THR 269 
168 1 Y 1 B THR 270 ? B THR 270 
169 1 Y 1 B THR 271 ? B THR 271 
170 1 Y 1 B SER 272 ? B SER 272 
171 1 Y 1 B VAL 273 ? B VAL 273 
172 1 Y 1 B PRO 274 ? B PRO 274 
173 1 Y 1 B LEU 275 ? B LEU 275 
174 1 Y 1 B SER 276 ? B SER 276 
175 1 Y 1 B ASN 277 ? B ASN 277 
176 1 Y 1 B SER 278 ? B SER 278 
177 1 Y 1 B LEU 279 ? B LEU 279 
178 1 Y 1 B GLU 280 ? B GLU 280 
179 1 Y 1 B VAL 281 ? B VAL 281 
180 1 Y 1 B LEU 282 ? B LEU 282 
181 1 Y 1 B PHE 283 ? B PHE 283 
182 1 Y 1 B GLN 284 ? B GLN 284 
183 1 Y 1 C HIS 2   ? C HIS 1   
184 1 Y 1 C HIS 3   ? C HIS 2   
185 1 Y 1 C HIS 4   ? C HIS 3   
186 1 Y 1 C HIS 5   ? C HIS 4   
187 1 Y 1 C HIS 6   ? C HIS 5   
188 1 Y 1 C HIS 7   ? C HIS 6   
189 1 Y 1 C HIS 8   ? C HIS 7   
190 1 Y 1 C ASP 9   ? C ASP 8   
191 1 Y 1 C TYR 10  ? C TYR 9   
192 1 Y 1 C ASP 11  ? C ASP 10  
193 1 Y 1 C ILE 12  ? C ILE 11  
194 1 Y 1 C PRO 13  ? C PRO 12  
195 1 Y 1 C THR 14  ? C THR 13  
196 1 Y 1 C THR 15  ? C THR 14  
197 1 Y 1 C GLU 16  ? C GLU 15  
198 1 Y 1 C ASN 17  ? C ASN 16  
199 1 Y 1 C LEU 18  ? C LEU 17  
200 1 Y 1 C TYR 19  ? C TYR 18  
201 1 Y 1 C PHE 20  ? C PHE 19  
202 1 Y 1 C GLN 21  ? C GLN 20  
203 1 Y 1 C GLY 22  ? C GLY 21  
204 1 Y 1 C SER 23  ? C SER 22  
205 1 Y 1 C THR 24  ? C THR 23  
206 1 Y 1 C LYS 56  ? C LYS 55  
207 1 Y 1 C ASP 57  ? C ASP 56  
208 1 Y 1 C LEU 58  ? C LEU 57  
209 1 Y 1 C GLU 59  ? C GLU 58  
210 1 Y 1 C GLU 60  ? C GLU 59  
211 1 Y 1 C VAL 61  ? C VAL 60  
212 1 Y 1 C LYS 62  ? C LYS 61  
213 1 Y 1 C ALA 63  ? C ALA 62  
214 1 Y 1 C LYS 64  ? C LYS 63  
215 1 Y 1 C VAL 65  ? C VAL 64  
216 1 Y 1 C GLN 66  ? C GLN 65  
217 1 Y 1 C PRO 67  ? C PRO 66  
218 1 Y 1 C TYR 68  ? C TYR 67  
219 1 Y 1 C LEU 69  ? C LEU 68  
220 1 Y 1 C ASP 70  ? C ASP 69  
221 1 Y 1 C ASP 71  ? C ASP 70  
222 1 Y 1 C PHE 72  ? C PHE 71  
223 1 Y 1 C GLN 73  ? C GLN 72  
224 1 Y 1 C LYS 74  ? C LYS 73  
225 1 Y 1 C LYS 75  ? C LYS 74  
226 1 Y 1 C TRP 76  ? C TRP 75  
227 1 Y 1 C GLN 77  ? C GLN 76  
228 1 Y 1 C GLU 78  ? C GLU 77  
229 1 Y 1 C GLU 79  ? C GLU 78  
230 1 Y 1 C MET 80  ? C MET 79  
231 1 Y 1 C GLU 81  ? C GLU 80  
232 1 Y 1 C LEU 82  ? C LEU 81  
233 1 Y 1 C TYR 83  ? C TYR 82  
234 1 Y 1 C ARG 84  ? C ARG 83  
235 1 Y 1 C GLN 85  ? C GLN 84  
236 1 Y 1 C LYS 86  ? C LYS 85  
237 1 Y 1 C VAL 87  ? C VAL 86  
238 1 Y 1 C GLU 88  ? C GLU 87  
239 1 Y 1 C PRO 89  ? C PRO 88  
240 1 Y 1 C LEU 90  ? C LEU 89  
241 1 Y 1 C ARG 91  ? C ARG 90  
242 1 Y 1 C ALA 92  ? C ALA 91  
243 1 Y 1 C GLU 93  ? C GLU 92  
244 1 Y 1 C LEU 94  ? C LEU 93  
245 1 Y 1 C GLN 95  ? C GLN 94  
246 1 Y 1 C GLU 96  ? C GLU 95  
247 1 Y 1 C GLY 97  ? C GLY 96  
248 1 Y 1 C ALA 98  ? C ALA 97  
249 1 Y 1 C ARG 99  ? C ARG 98  
250 1 Y 1 C GLN 100 ? C GLN 99  
251 1 Y 1 C LYS 101 ? C LYS 100 
252 1 Y 1 C LEU 102 ? C LEU 101 
253 1 Y 1 C HIS 103 ? C HIS 102 
254 1 Y 1 C GLU 104 ? C GLU 103 
255 1 Y 1 C LEU 105 ? C LEU 104 
256 1 Y 1 C GLN 106 ? C GLN 105 
257 1 Y 1 C GLU 107 ? C GLU 106 
258 1 Y 1 C LYS 108 ? C LYS 107 
259 1 Y 1 C LEU 109 ? C LEU 108 
260 1 Y 1 C SER 110 ? C SER 109 
261 1 Y 1 C PRO 111 ? C PRO 110 
262 1 Y 1 C LEU 112 ? C LEU 111 
263 1 Y 1 C GLY 113 ? C GLY 112 
264 1 Y 1 C GLU 114 ? C GLU 113 
265 1 Y 1 C GLU 115 ? C GLU 114 
266 1 Y 1 C MET 116 ? C MET 115 
267 1 Y 1 C ARG 117 ? C ARG 116 
268 1 Y 1 C ASP 118 ? C ASP 117 
269 1 Y 1 C ARG 119 ? C ARG 118 
270 1 Y 1 C ALA 120 ? C ALA 119 
271 1 Y 1 C ARG 121 ? C ARG 120 
272 1 Y 1 C ALA 122 ? C ALA 121 
273 1 Y 1 C HIS 123 ? C HIS 122 
274 1 Y 1 C VAL 124 ? C VAL 123 
275 1 Y 1 C ASP 125 ? C ASP 124 
276 1 Y 1 C ALA 126 ? C ALA 125 
277 1 Y 1 C LEU 127 ? C LEU 126 
278 1 Y 1 C ARG 128 ? C ARG 127 
279 1 Y 1 C THR 129 ? C THR 128 
280 1 Y 1 C HIS 130 ? C HIS 129 
281 1 Y 1 C LEU 131 ? C LEU 130 
282 1 Y 1 C ALA 132 ? C ALA 131 
283 1 Y 1 C PRO 133 ? C PRO 132 
284 1 Y 1 C TYR 134 ? C TYR 133 
285 1 Y 1 C SER 135 ? C SER 134 
286 1 Y 1 C ASP 136 ? C ASP 135 
287 1 Y 1 C GLU 137 ? C GLU 136 
288 1 Y 1 C LEU 138 ? C LEU 137 
289 1 Y 1 C ARG 139 ? C ARG 138 
290 1 Y 1 C GLN 140 ? C GLN 139 
291 1 Y 1 C ARG 141 ? C ARG 140 
292 1 Y 1 C LEU 142 ? C LEU 141 
293 1 Y 1 C ALA 143 ? C ALA 142 
294 1 Y 1 C ALA 144 ? C ALA 143 
295 1 Y 1 C ARG 145 ? C ARG 144 
296 1 Y 1 C LEU 146 ? C LEU 145 
297 1 Y 1 C GLU 147 ? C GLU 146 
298 1 Y 1 C ALA 148 ? C ALA 147 
299 1 Y 1 C LEU 149 ? C LEU 148 
300 1 Y 1 C LYS 150 ? C LYS 149 
301 1 Y 1 C GLU 151 ? C GLU 150 
302 1 Y 1 C ASN 152 ? C ASN 151 
303 1 Y 1 C GLY 153 ? C GLY 152 
304 1 Y 1 C GLY 154 ? C GLY 153 
305 1 Y 1 C ALA 155 ? C ALA 154 
306 1 Y 1 C ARG 156 ? C ARG 155 
307 1 Y 1 C LEU 157 ? C LEU 156 
308 1 Y 1 C ALA 158 ? C ALA 157 
309 1 Y 1 C GLU 159 ? C GLU 158 
310 1 Y 1 C TYR 160 ? C TYR 159 
311 1 Y 1 C HIS 161 ? C HIS 160 
312 1 Y 1 C ALA 162 ? C ALA 161 
313 1 Y 1 C LYS 163 ? C LYS 162 
314 1 Y 1 C ALA 164 ? C ALA 163 
315 1 Y 1 C THR 165 ? C THR 164 
316 1 Y 1 C GLU 166 ? C GLU 165 
317 1 Y 1 C HIS 167 ? C HIS 166 
318 1 Y 1 C LEU 168 ? C LEU 167 
319 1 Y 1 C SER 169 ? C SER 168 
320 1 Y 1 C THR 170 ? C THR 169 
321 1 Y 1 C LEU 171 ? C LEU 170 
322 1 Y 1 C SER 172 ? C SER 171 
323 1 Y 1 C GLU 173 ? C GLU 172 
324 1 Y 1 C LYS 174 ? C LYS 173 
325 1 Y 1 C ALA 175 ? C ALA 174 
326 1 Y 1 C LYS 176 ? C LYS 175 
327 1 Y 1 C PRO 177 ? C PRO 176 
328 1 Y 1 C ALA 178 ? C ALA 177 
329 1 Y 1 C LEU 179 ? C LEU 178 
330 1 Y 1 C GLU 180 ? C GLU 179 
331 1 Y 1 C ASP 181 ? C ASP 180 
332 1 Y 1 C LEU 182 ? C LEU 181 
333 1 Y 1 C ARG 183 ? C ARG 182 
334 1 Y 1 C GLN 184 ? C GLN 183 
335 1 Y 1 C GLY 185 ? C GLY 184 
336 1 Y 1 C LEU 186 ? C LEU 185 
337 1 Y 1 C LEU 187 ? C LEU 186 
338 1 Y 1 C PRO 188 ? C PRO 187 
339 1 Y 1 C VAL 189 ? C VAL 188 
340 1 Y 1 C LEU 190 ? C LEU 189 
341 1 Y 1 C GLU 191 ? C GLU 190 
342 1 Y 1 C SER 192 ? C SER 191 
343 1 Y 1 C PHE 193 ? C PHE 192 
344 1 Y 1 C LYS 194 ? C LYS 193 
345 1 Y 1 C VAL 195 ? C VAL 194 
346 1 Y 1 C SER 196 ? C SER 195 
347 1 Y 1 C PHE 197 ? C PHE 196 
348 1 Y 1 C LEU 198 ? C LEU 197 
349 1 Y 1 C SER 199 ? C SER 198 
350 1 Y 1 C ALA 200 ? C ALA 199 
351 1 Y 1 C LEU 201 ? C LEU 200 
352 1 Y 1 C GLU 202 ? C GLU 201 
353 1 Y 1 C GLU 203 ? C GLU 202 
354 1 Y 1 C TYR 204 ? C TYR 203 
355 1 Y 1 C THR 205 ? C THR 204 
356 1 Y 1 C LYS 206 ? C LYS 205 
357 1 Y 1 C LYS 207 ? C LYS 206 
358 1 Y 1 C LEU 208 ? C LEU 207 
359 1 Y 1 C ASN 209 ? C ASN 208 
360 1 Y 1 C THR 210 ? C THR 209 
361 1 Y 1 C GLN 211 ? C GLN 210 
362 1 Y 1 D HIS 2   ? D HIS 1   
363 1 Y 1 D HIS 3   ? D HIS 2   
364 1 Y 1 D HIS 4   ? D HIS 3   
365 1 Y 1 D HIS 5   ? D HIS 4   
366 1 Y 1 D HIS 6   ? D HIS 5   
367 1 Y 1 D HIS 7   ? D HIS 6   
368 1 Y 1 D HIS 8   ? D HIS 7   
369 1 Y 1 D ASP 9   ? D ASP 8   
370 1 Y 1 D TYR 10  ? D TYR 9   
371 1 Y 1 D ASP 11  ? D ASP 10  
372 1 Y 1 D ILE 12  ? D ILE 11  
373 1 Y 1 D PRO 13  ? D PRO 12  
374 1 Y 1 D THR 14  ? D THR 13  
375 1 Y 1 D THR 15  ? D THR 14  
376 1 Y 1 D GLU 16  ? D GLU 15  
377 1 Y 1 D ASN 17  ? D ASN 16  
378 1 Y 1 D LEU 18  ? D LEU 17  
379 1 Y 1 D TYR 19  ? D TYR 18  
380 1 Y 1 D PHE 20  ? D PHE 19  
381 1 Y 1 D GLN 21  ? D GLN 20  
382 1 Y 1 D GLY 22  ? D GLY 21  
383 1 Y 1 D SER 23  ? D SER 22  
384 1 Y 1 D THR 24  ? D THR 23  
385 1 Y 1 D LYS 56  ? D LYS 55  
386 1 Y 1 D ASP 57  ? D ASP 56  
387 1 Y 1 D LEU 58  ? D LEU 57  
388 1 Y 1 D GLU 59  ? D GLU 58  
389 1 Y 1 D GLU 60  ? D GLU 59  
390 1 Y 1 D VAL 61  ? D VAL 60  
391 1 Y 1 D LYS 62  ? D LYS 61  
392 1 Y 1 D ALA 63  ? D ALA 62  
393 1 Y 1 D LYS 64  ? D LYS 63  
394 1 Y 1 D VAL 65  ? D VAL 64  
395 1 Y 1 D GLN 66  ? D GLN 65  
396 1 Y 1 D PRO 67  ? D PRO 66  
397 1 Y 1 D TYR 68  ? D TYR 67  
398 1 Y 1 D LEU 69  ? D LEU 68  
399 1 Y 1 D ASP 70  ? D ASP 69  
400 1 Y 1 D ASP 71  ? D ASP 70  
401 1 Y 1 D PHE 72  ? D PHE 71  
402 1 Y 1 D GLN 73  ? D GLN 72  
403 1 Y 1 D LYS 74  ? D LYS 73  
404 1 Y 1 D LYS 75  ? D LYS 74  
405 1 Y 1 D TRP 76  ? D TRP 75  
406 1 Y 1 D GLN 77  ? D GLN 76  
407 1 Y 1 D GLU 78  ? D GLU 77  
408 1 Y 1 D GLU 79  ? D GLU 78  
409 1 Y 1 D MET 80  ? D MET 79  
410 1 Y 1 D GLU 81  ? D GLU 80  
411 1 Y 1 D LEU 82  ? D LEU 81  
412 1 Y 1 D TYR 83  ? D TYR 82  
413 1 Y 1 D ARG 84  ? D ARG 83  
414 1 Y 1 D GLN 85  ? D GLN 84  
415 1 Y 1 D LYS 86  ? D LYS 85  
416 1 Y 1 D VAL 87  ? D VAL 86  
417 1 Y 1 D GLU 88  ? D GLU 87  
418 1 Y 1 D PRO 89  ? D PRO 88  
419 1 Y 1 D LEU 90  ? D LEU 89  
420 1 Y 1 D ARG 91  ? D ARG 90  
421 1 Y 1 D ALA 92  ? D ALA 91  
422 1 Y 1 D GLU 93  ? D GLU 92  
423 1 Y 1 D LEU 94  ? D LEU 93  
424 1 Y 1 D GLN 95  ? D GLN 94  
425 1 Y 1 D GLU 96  ? D GLU 95  
426 1 Y 1 D GLY 97  ? D GLY 96  
427 1 Y 1 D ALA 98  ? D ALA 97  
428 1 Y 1 D ARG 99  ? D ARG 98  
429 1 Y 1 D GLN 100 ? D GLN 99  
430 1 Y 1 D LYS 101 ? D LYS 100 
431 1 Y 1 D LEU 102 ? D LEU 101 
432 1 Y 1 D HIS 103 ? D HIS 102 
433 1 Y 1 D GLU 104 ? D GLU 103 
434 1 Y 1 D LEU 105 ? D LEU 104 
435 1 Y 1 D GLN 106 ? D GLN 105 
436 1 Y 1 D GLU 107 ? D GLU 106 
437 1 Y 1 D LYS 108 ? D LYS 107 
438 1 Y 1 D LEU 109 ? D LEU 108 
439 1 Y 1 D SER 110 ? D SER 109 
440 1 Y 1 D PRO 111 ? D PRO 110 
441 1 Y 1 D LEU 112 ? D LEU 111 
442 1 Y 1 D GLY 113 ? D GLY 112 
443 1 Y 1 D GLU 114 ? D GLU 113 
444 1 Y 1 D GLU 115 ? D GLU 114 
445 1 Y 1 D MET 116 ? D MET 115 
446 1 Y 1 D ARG 117 ? D ARG 116 
447 1 Y 1 D ASP 118 ? D ASP 117 
448 1 Y 1 D ARG 119 ? D ARG 118 
449 1 Y 1 D ALA 120 ? D ALA 119 
450 1 Y 1 D ARG 121 ? D ARG 120 
451 1 Y 1 D ALA 122 ? D ALA 121 
452 1 Y 1 D HIS 123 ? D HIS 122 
453 1 Y 1 D VAL 124 ? D VAL 123 
454 1 Y 1 D ASP 125 ? D ASP 124 
455 1 Y 1 D ALA 126 ? D ALA 125 
456 1 Y 1 D LEU 127 ? D LEU 126 
457 1 Y 1 D ARG 128 ? D ARG 127 
458 1 Y 1 D THR 129 ? D THR 128 
459 1 Y 1 D HIS 130 ? D HIS 129 
460 1 Y 1 D LEU 131 ? D LEU 130 
461 1 Y 1 D ALA 132 ? D ALA 131 
462 1 Y 1 D PRO 133 ? D PRO 132 
463 1 Y 1 D TYR 134 ? D TYR 133 
464 1 Y 1 D SER 135 ? D SER 134 
465 1 Y 1 D ASP 136 ? D ASP 135 
466 1 Y 1 D GLU 137 ? D GLU 136 
467 1 Y 1 D LEU 138 ? D LEU 137 
468 1 Y 1 D ARG 139 ? D ARG 138 
469 1 Y 1 D GLN 140 ? D GLN 139 
470 1 Y 1 D ARG 141 ? D ARG 140 
471 1 Y 1 D LEU 142 ? D LEU 141 
472 1 Y 1 D ALA 143 ? D ALA 142 
473 1 Y 1 D ALA 144 ? D ALA 143 
474 1 Y 1 D ARG 145 ? D ARG 144 
475 1 Y 1 D LEU 146 ? D LEU 145 
476 1 Y 1 D GLU 147 ? D GLU 146 
477 1 Y 1 D ALA 148 ? D ALA 147 
478 1 Y 1 D LEU 149 ? D LEU 148 
479 1 Y 1 D LYS 150 ? D LYS 149 
480 1 Y 1 D GLU 151 ? D GLU 150 
481 1 Y 1 D ASN 152 ? D ASN 151 
482 1 Y 1 D GLY 153 ? D GLY 152 
483 1 Y 1 D GLY 154 ? D GLY 153 
484 1 Y 1 D ALA 155 ? D ALA 154 
485 1 Y 1 D ARG 156 ? D ARG 155 
486 1 Y 1 D LEU 157 ? D LEU 156 
487 1 Y 1 D ALA 158 ? D ALA 157 
488 1 Y 1 D GLU 159 ? D GLU 158 
489 1 Y 1 D TYR 160 ? D TYR 159 
490 1 Y 1 D HIS 161 ? D HIS 160 
491 1 Y 1 D ALA 162 ? D ALA 161 
492 1 Y 1 D LYS 163 ? D LYS 162 
493 1 Y 1 D ALA 164 ? D ALA 163 
494 1 Y 1 D THR 165 ? D THR 164 
495 1 Y 1 D GLU 166 ? D GLU 165 
496 1 Y 1 D HIS 167 ? D HIS 166 
497 1 Y 1 D LEU 168 ? D LEU 167 
498 1 Y 1 D SER 169 ? D SER 168 
499 1 Y 1 D THR 170 ? D THR 169 
500 1 Y 1 D LEU 171 ? D LEU 170 
501 1 Y 1 D SER 172 ? D SER 171 
502 1 Y 1 D GLU 173 ? D GLU 172 
503 1 Y 1 D LYS 174 ? D LYS 173 
504 1 Y 1 D ALA 175 ? D ALA 174 
505 1 Y 1 D LYS 176 ? D LYS 175 
506 1 Y 1 D PRO 177 ? D PRO 176 
507 1 Y 1 D ALA 178 ? D ALA 177 
508 1 Y 1 D LEU 179 ? D LEU 178 
509 1 Y 1 D GLU 180 ? D GLU 179 
510 1 Y 1 D ASP 181 ? D ASP 180 
511 1 Y 1 D LEU 182 ? D LEU 181 
512 1 Y 1 D ARG 183 ? D ARG 182 
513 1 Y 1 D GLN 184 ? D GLN 183 
514 1 Y 1 D GLY 185 ? D GLY 184 
515 1 Y 1 D LEU 186 ? D LEU 185 
516 1 Y 1 D LEU 187 ? D LEU 186 
517 1 Y 1 D PRO 188 ? D PRO 187 
518 1 Y 1 D VAL 189 ? D VAL 188 
519 1 Y 1 D LEU 190 ? D LEU 189 
520 1 Y 1 D GLU 191 ? D GLU 190 
521 1 Y 1 D SER 192 ? D SER 191 
522 1 Y 1 D PHE 193 ? D PHE 192 
523 1 Y 1 D LYS 194 ? D LYS 193 
524 1 Y 1 D VAL 195 ? D VAL 194 
525 1 Y 1 D SER 196 ? D SER 195 
526 1 Y 1 D PHE 197 ? D PHE 196 
527 1 Y 1 D LEU 198 ? D LEU 197 
528 1 Y 1 D SER 199 ? D SER 198 
529 1 Y 1 D ALA 200 ? D ALA 199 
530 1 Y 1 D LEU 201 ? D LEU 200 
531 1 Y 1 D GLU 202 ? D GLU 201 
532 1 Y 1 D GLU 203 ? D GLU 202 
533 1 Y 1 D TYR 204 ? D TYR 203 
534 1 Y 1 D THR 205 ? D THR 204 
535 1 Y 1 D LYS 206 ? D LYS 205 
536 1 Y 1 D LYS 207 ? D LYS 206 
537 1 Y 1 D LEU 208 ? D LEU 207 
538 1 Y 1 D ASN 209 ? D ASN 208 
539 1 Y 1 D THR 210 ? D THR 209 
540 1 Y 1 D GLN 211 ? D GLN 210 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.name 
1 1 20  mM C8H18N2O4S HEPES                
1 2 150 mM KCl        'Potassium Chloride' 
# 
_em_ctf_correction.id                       1 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
_em_ctf_correction.details                  ? 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.062 
# 
_em_entity_assembly_naturalsource.id                   1 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.ncbi_tax_id          2697049 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organism             'Severe acute respiratory syndrome coronavirus 2' 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
# 
_em_entity_assembly_recombinant.id                   1 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
_em_image_processing.details              ? 
# 
_em_image_recording.id                            1 
_em_image_recording.imaging_id                    1 
_em_image_recording.avg_electron_dose_per_image   50 
_em_image_recording.average_exposure_time         ? 
_em_image_recording.details                       ? 
_em_image_recording.detector_mode                 ? 
_em_image_recording.film_or_detector_model        'FEI FALCON IV (4k x 4k)' 
_em_image_recording.num_diffraction_images        ? 
_em_image_recording.num_grids_imaged              ? 
_em_image_recording.num_real_images               ? 
# 
loop_
_em_software.id 
_em_software.category 
_em_software.details 
_em_software.name 
_em_software.version 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
1  'PARTICLE SELECTION'       ? ?      ?               1 ? ? 
2  'IMAGE ACQUISITION'        ? ?      ?               ? ? 1 
3  MASKING                    ? ?      ?               ? ? ? 
4  'CTF CORRECTION'           ? ?      ?               1 ? ? 
5  'LAYERLINE INDEXING'       ? ?      ?               ? ? ? 
6  'DIFFRACTION INDEXING'     ? ?      ?               ? ? ? 
7  'MODEL FITTING'            ? ?      ?               ? 1 ? 
8  OTHER                      ? ?      ?               ? ? ? 
9  'INITIAL EULER ASSIGNMENT' ? ?      ?               1 ? ? 
10 'FINAL EULER ASSIGNMENT'   ? ?      ?               1 ? ? 
11 CLASSIFICATION             ? ?      ?               1 ? ? 
12 RECONSTRUCTION             ? ?      ?               1 ? ? 
13 'MODEL REFINEMENT'         ? PHENIX 1.18.2-3874-000 ? 1 ? 
# 
_em_specimen.id                      1 
_em_specimen.experiment_id           1 
_em_specimen.concentration           1.1 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM123496 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM128263 2 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-Dioleoyl-sn-glycero-3-phosphoethanolamine PEE 
4 water                                         HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
