path: root/Docking/Target/6y84.cif

data_6Y84
# 
_entry.id   6Y84 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.322 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6Y84         
WWPDB D_1292107053 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6Y84 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Owen, C.D.'            1  ? 
'Lukacik, P.'           2  ? 
'Strain-Damerell, C.M.' 3  ? 
'Douangamath, A.'       4  ? 
'Powell, A.J.'          5  ? 
'Fearon, D.'            6  ? 
'Brandao-Neto, J.'      7  ? 
'Crawshaw, A.D.'        8  ? 
'Aragao, D.'            9  ? 
'Williams, M.'          10 ? 
'Flaig, R.'             11 ? 
'Hall, D.'              12 ? 
'McAauley, K.'          13 ? 
'Stuart, D.I.'          14 ? 
'von Delft, F.'         15 ? 
'Walsh, M.A.'           16 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'COVID-19 main protease with unliganded active site' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Owen, C.D.'            1  ? 
primary 'Lukacik, P.'           2  ? 
primary 'Strain-Damerell, C.M.' 3  ? 
primary 'Douangamath, A.'       4  ? 
primary 'Powell, A.J.'          5  ? 
primary 'Fearon, D.'            6  ? 
primary 'Brandao-Neto, J.'      7  ? 
primary 'Crawshaw, A.D.'        8  ? 
primary 'Aragao, D.'            9  ? 
primary 'Williams, M.'          10 ? 
primary 'Flaig, R.'             11 ? 
primary 'Hall, D.'              12 ? 
primary 'McAauley, K.'          13 ? 
primary 'Stuart, D.I.'          14 ? 
primary 'von Delft, F.'         15 ? 
primary 'Walsh, M.A.'           16 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.160 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6Y84 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.812 
_cell.length_a_esd                 ? 
_cell.length_b                     52.949 
_cell.length_b_esd                 ? 
_cell.length_c                     44.631 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6Y84 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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 'Non-structural polyprotein 1ab' 33825.547 1   ? ? ? ? 
2 non-polymer syn 'DIMETHYL SULFOXIDE'             78.133    4   ? ? ? ? 
3 water       nat water                            18.015    391 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_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                    COVID-19 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    6Y84 
_struct_ref.pdbx_db_accession          6Y84 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6Y84 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             6Y84 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  306 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       306 
# 
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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'    117.146 
# 
_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                   6Y84 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            1.92 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         35.89 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;15% PEG 4000, 5% DMSO, 0.1M MES pH 6.5.
0.15 microlitre protein + 0.3 microlitre reservoir + 0.05 microlitre seed stock
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-24 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9126 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9126 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            17.330 
_reflns.entry_id                         6Y84 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.390 
_reflns.d_resolution_low                 54.930 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       50348 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             97.500 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.600 
_reflns.pdbx_Rmerge_I_obs                0.059 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            9.700 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             602 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.069 
_reflns.pdbx_Rpim_I_all                  0.034 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         179937 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.997 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
1.390 1.410  ? ? 4394 ? ? ? 2074 80.700 ? ? ? ? 0.929 ? ? ? ? ? ? ? ? 2.100 ? ? ? 0.800  1.141 0.650 ? 1 1 0.481 ? ? 
7.610 54.930 ? ? 1425 ? ? ? 339  99.800 ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 4.200 ? ? ? 32.500 0.025 0.012 ? 2 1 0.999 ? ? 
# 
_refine.aniso_B[1][1]                            -3.7809 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0422 
_refine.aniso_B[2][2]                            0.6978 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            3.0831 
_refine.B_iso_max                                97.940 
_refine.B_iso_mean                               21.0000 
_refine.B_iso_min                                10.280 
_refine.correlation_coeff_Fo_to_Fc               0.9630 
_refine.correlation_coeff_Fo_to_Fc_free          0.9560 
_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                                 6Y84 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.3900 
_refine.ls_d_res_low                             54.9300 
_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                     50331 
_refine.ls_number_reflns_R_free                  2498 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.5000 
_refine.ls_percent_reflns_R_free                 4.9600 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1790 
_refine.ls_R_factor_R_free                       0.2000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1779 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6LU7 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_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   0.0680 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.0710 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0740 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0690 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        6Y84 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.190 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.3900 
_refine_hist.d_res_low                        54.9300 
_refine_hist.number_atoms_solvent             391 
_refine_hist.number_atoms_total               2754 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       304 
_refine_hist.pdbx_B_iso_mean_ligand           33.83 
_refine_hist.pdbx_B_iso_mean_solvent          32.89 
_refine_hist.pdbx_number_atoms_protein        2347 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? ?      ? 909  ? t_dihedral_angle_d        2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_trig_c_planes           ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 466  ? t_gen_planes              5.000  HARMONIC     
'X-RAY DIFFRACTION' ? ?      ? 2628 ? t_it                      10.000 HARMONIC     
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_nbd                     ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_improper_torsion        ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_pseud_angle             ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 340  ? t_chiral_improper_torsion 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_sum_occupancies         ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_distance        ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_angle           ?      ?            
'X-RAY DIFFRACTION' ? ?      ? ?    ? t_utility_torsion         ?      ?            
'X-RAY DIFFRACTION' ? ?      ? 3017 ? t_ideal_dist_contact      4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 0.007  ? 2628 ? t_bond_d                  2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 0.980  ? 3595 ? t_angle_deg               2.000  HARMONIC     
'X-RAY DIFFRACTION' ? 3.920  ? ?    ? t_omega_torsion           ?      ?            
'X-RAY DIFFRACTION' ? 14.640 ? ?    ? t_other_torsion           ?      ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3900 
_refine_ls_shell.d_res_low                        1.4000 
_refine_ls_shell.number_reflns_all                1007 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             66 
_refine_ls_shell.number_reflns_R_work             941 
_refine_ls_shell.percent_reflns_obs               77.9900 
_refine_ls_shell.percent_reflns_R_free            6.5500 
_refine_ls_shell.R_factor_all                     0.2107 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2075 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2109 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6Y84 
_struct.title                        
'COVID-19 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, SARS-CoV-2)' 
_struct.pdbx_descriptor              'Non-structural polyprotein 1ab' 
_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        6Y84 
_struct_keywords.text            'protease, cysteine protease, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   '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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
# 
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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 LYS A 61  ? HIS A 64  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_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 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? 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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
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 LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
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 DMS 401 ? 8 'binding site for residue DMS A 401' 
AC2 Software A DMS 402 ? 2 'binding site for residue DMS A 402' 
AC3 Software A DMS 403 ? 6 'binding site for residue DMS A 403' 
AC4 Software A DMS 404 ? 5 'binding site for residue DMS A 404' 
# 
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 8 GLN A 74  ? GLN A 74  . ? 1_555 ? 
2  AC1 8 LEU A 75  ? LEU A 75  . ? 1_555 ? 
3  AC1 8 ARG A 76  ? ARG A 76  . ? 1_555 ? 
4  AC1 8 PHE A 223 ? PHE A 223 . ? 1_546 ? 
5  AC1 8 THR A 224 ? THR A 224 . ? 1_546 ? 
6  AC1 8 ASP A 263 ? ASP A 263 . ? 1_546 ? 
7  AC1 8 HOH F .   ? HOH A 570 . ? 1_546 ? 
8  AC1 8 HOH F .   ? HOH A 579 . ? 1_555 ? 
9  AC2 2 HIS A 64  ? HIS A 64  . ? 1_555 ? 
10 AC2 2 ASN A 65  ? ASN A 65  . ? 1_555 ? 
11 AC3 6 MET A 6   ? MET A 6   . ? 1_555 ? 
12 AC3 6 PHE A 8   ? PHE A 8   . ? 1_555 ? 
13 AC3 6 SER A 123 ? SER A 123 . ? 2_555 ? 
14 AC3 6 GLN A 127 ? GLN A 127 . ? 1_555 ? 
15 AC3 6 ASP A 295 ? ASP A 295 . ? 1_555 ? 
16 AC3 6 ARG A 298 ? ARG A 298 . ? 1_555 ? 
17 AC4 5 GLY A 15  ? GLY A 15  . ? 1_555 ? 
18 AC4 5 MET A 17  ? MET A 17  . ? 1_555 ? 
19 AC4 5 LYS A 97  ? LYS A 97  . ? 1_555 ? 
20 AC4 5 HOH F .   ? HOH A 620 . ? 1_555 ? 
21 AC4 5 HOH F .   ? HOH A 654 . ? 1_555 ? 
# 
_atom_sites.entry_id                    6Y84 
_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]   0.008864 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002073 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018886 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.023010 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   A SER A 1 1   ? -2.185 4.397   -17.079 0.50 26.55 ? 1   SER A N   1 
ATOM   2    N N   B SER A 1 1   ? -2.224 4.310   -17.137 0.50 25.36 ? 1   SER A N   1 
ATOM   3    C CA  A SER A 1 1   ? -2.021 5.695   -16.438 0.50 26.71 ? 1   SER A CA  1 
ATOM   4    C CA  B SER A 1 1   ? -1.882 5.526   -16.417 0.50 25.40 ? 1   SER A CA  1 
ATOM   5    C C   A SER A 1 1   ? -2.350 5.650   -14.945 0.50 25.98 ? 1   SER A C   1 
ATOM   6    C C   B SER A 1 1   ? -2.298 5.476   -14.933 0.50 24.98 ? 1   SER A C   1 
ATOM   7    O O   A SER A 1 1   ? -2.957 4.696   -14.446 0.50 25.86 ? 1   SER A O   1 
ATOM   8    O O   B SER A 1 1   ? -2.988 4.551   -14.492 0.50 24.74 ? 1   SER A O   1 
ATOM   9    C CB  A SER A 1 1   ? -2.819 6.777   -17.164 0.50 28.89 ? 1   SER A CB  1 
ATOM   10   C CB  B SER A 1 1   ? -2.440 6.757   -17.134 0.50 27.08 ? 1   SER A CB  1 
ATOM   11   O OG  A SER A 1 1   ? -2.052 7.417   -18.170 0.50 31.95 ? 1   SER A OG  1 
ATOM   12   O OG  B SER A 1 1   ? -3.797 7.000   -16.801 0.50 29.72 ? 1   SER A OG  1 
ATOM   13   N N   A GLY A 1 2   ? -1.917 6.679   -14.240 0.50 25.04 ? 2   GLY A N   1 
ATOM   14   N N   B GLY A 1 2   ? -1.852 6.467   -14.178 0.50 24.37 ? 2   GLY A N   1 
ATOM   15   C CA  A GLY A 1 2   ? -2.078 6.745   -12.803 0.50 24.62 ? 2   GLY A CA  1 
ATOM   16   C CA  B GLY A 1 2   ? -2.122 6.541   -12.756 0.50 24.27 ? 2   GLY A CA  1 
ATOM   17   C C   A GLY A 1 2   ? -0.786 6.340   -12.129 0.50 23.89 ? 2   GLY A C   1 
ATOM   18   C C   B GLY A 1 2   ? -0.877 6.134   -12.010 0.50 23.87 ? 2   GLY A C   1 
ATOM   19   O O   A GLY A 1 2   ? -0.004 5.553   -12.671 0.50 24.05 ? 2   GLY A O   1 
ATOM   20   O O   B GLY A 1 2   ? -0.206 5.169   -12.398 0.50 24.00 ? 2   GLY A O   1 
ATOM   21   N N   . PHE A 1 3   ? -0.560 6.863   -10.941 1.00 22.93 ? 3   PHE A N   1 
ATOM   22   C CA  . PHE A 1 3   ? 0.639  6.585   -10.184 1.00 22.04 ? 3   PHE A CA  1 
ATOM   23   C C   . PHE A 1 3   ? 0.290  6.604   -8.729  1.00 21.78 ? 3   PHE A C   1 
ATOM   24   O O   . PHE A 1 3   ? -0.157 7.619   -8.198  1.00 23.62 ? 3   PHE A O   1 
ATOM   25   C CB  . PHE A 1 3   ? 1.732  7.609   -10.538 1.00 21.01 ? 3   PHE A CB  1 
ATOM   26   C CG  . PHE A 1 3   ? 3.117  7.084   -10.258 1.00 21.05 ? 3   PHE A CG  1 
ATOM   27   C CD1 . PHE A 1 3   ? 3.724  6.190   -11.120 1.00 21.40 ? 3   PHE A CD1 1 
ATOM   28   C CD2 . PHE A 1 3   ? 3.799  7.464   -9.122  1.00 21.44 ? 3   PHE A CD2 1 
ATOM   29   C CE1 . PHE A 1 3   ? 4.993  5.696   -10.852 1.00 22.14 ? 3   PHE A CE1 1 
ATOM   30   C CE2 . PHE A 1 3   ? 5.075  6.985   -8.870  1.00 21.61 ? 3   PHE A CE2 1 
ATOM   31   C CZ  . PHE A 1 3   ? 5.652  6.081   -9.717  1.00 21.71 ? 3   PHE A CZ  1 
ATOM   32   N N   . ARG A 1 4   ? 0.443  5.457   -8.087  1.00 19.43 ? 4   ARG A N   1 
ATOM   33   C CA  . ARG A 1 4   ? 0.091  5.280   -6.693  1.00 18.12 ? 4   ARG A CA  1 
ATOM   34   C C   . ARG A 1 4   ? 1.257  4.818   -5.846  1.00 17.46 ? 4   ARG A C   1 
ATOM   35   O O   . ARG A 1 4   ? 2.173  4.183   -6.358  1.00 18.03 ? 4   ARG A O   1 
ATOM   36   C CB  . ARG A 1 4   ? -0.984 4.179   -6.615  1.00 19.34 ? 4   ARG A CB  1 
ATOM   37   C CG  . ARG A 1 4   ? -2.389 4.693   -6.846  1.00 22.46 ? 4   ARG A CG  1 
ATOM   38   C CD  . ARG A 1 4   ? -2.962 5.187   -5.525  1.00 25.30 ? 4   ARG A CD  1 
ATOM   39   N NE  . ARG A 1 4   ? -4.352 5.630   -5.666  1.00 28.96 ? 4   ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 4   ? -5.041 6.254   -4.713  1.00 31.07 ? 4   ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 4   ? -4.479 6.508   -3.538  1.00 31.07 ? 4   ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 4   ? -6.295 6.632   -4.932  1.00 28.97 ? 4   ARG A NH2 1 
ATOM   43   N N   A LYS A 1 5   ? 1.185  5.069   -4.531  0.50 16.58 ? 5   LYS A N   1 
ATOM   44   N N   B LYS A 1 5   ? 1.202  5.059   -4.523  0.50 16.76 ? 5   LYS A N   1 
ATOM   45   C CA  A LYS A 1 5   ? 2.185  4.556   -3.613  0.50 16.63 ? 5   LYS A CA  1 
ATOM   46   C CA  B LYS A 1 5   ? 2.235  4.584   -3.597  0.50 16.99 ? 5   LYS A CA  1 
ATOM   47   C C   A LYS A 1 5   ? 1.841  3.080   -3.508  0.50 17.04 ? 5   LYS A C   1 
ATOM   48   C C   B LYS A 1 5   ? 1.980  3.098   -3.369  0.50 17.63 ? 5   LYS A C   1 
ATOM   49   O O   A LYS A 1 5   ? 0.747  2.726   -3.077  0.50 17.39 ? 5   LYS A O   1 
ATOM   50   O O   B LYS A 1 5   ? 1.203  2.711   -2.496  0.50 18.57 ? 5   LYS A O   1 
ATOM   51   C CB  A LYS A 1 5   ? 2.120  5.253   -2.246  0.50 17.92 ? 5   LYS A CB  1 
ATOM   52   C CB  B LYS A 1 5   ? 2.196  5.363   -2.273  0.50 18.19 ? 5   LYS A CB  1 
ATOM   53   C CG  A LYS A 1 5   ? 3.300  4.911   -1.342  0.50 21.29 ? 5   LYS A CG  1 
ATOM   54   C CG  B LYS A 1 5   ? 3.332  5.005   -1.326  0.50 21.43 ? 5   LYS A CG  1 
ATOM   55   C CD  A LYS A 1 5   ? 4.637  5.388   -1.894  0.50 24.62 ? 5   LYS A CD  1 
ATOM   56   C CD  B LYS A 1 5   ? 4.694  5.391   -1.868  0.50 24.70 ? 5   LYS A CD  1 
ATOM   57   C CE  A LYS A 1 5   ? 4.810  6.884   -1.795  0.50 27.77 ? 5   LYS A CE  1 
ATOM   58   C CE  B LYS A 1 5   ? 4.925  6.879   -1.800  0.50 27.68 ? 5   LYS A CE  1 
ATOM   59   N NZ  A LYS A 1 5   ? 4.611  7.386   -0.415  0.50 29.14 ? 5   LYS A NZ  1 
ATOM   60   N NZ  B LYS A 1 5   ? 4.633  7.433   -0.457  0.50 28.93 ? 5   LYS A NZ  1 
ATOM   61   N N   . MET A 1 6   ? 2.663  2.273   -4.148  1.00 17.01 ? 6   MET A N   1 
ATOM   62   C CA  . MET A 1 6   ? 2.427  0.855   -4.239  1.00 17.12 ? 6   MET A CA  1 
ATOM   63   C C   . MET A 1 6   ? 3.367  0.015   -3.454  1.00 15.93 ? 6   MET A C   1 
ATOM   64   O O   . MET A 1 6   ? 4.570  0.202   -3.547  1.00 16.36 ? 6   MET A O   1 
ATOM   65   C CB  . MET A 1 6   ? 2.580  0.517   -5.725  1.00 19.42 ? 6   MET A CB  1 
ATOM   66   C CG  . MET A 1 6   ? 2.137  -0.836  -6.077  1.00 24.58 ? 6   MET A CG  1 
ATOM   67   S SD  . MET A 1 6   ? 2.195  -0.979  -7.868  1.00 31.98 ? 6   MET A SD  1 
ATOM   68   C CE  . MET A 1 6   ? 0.949  0.182   -8.339  1.00 27.76 ? 6   MET A CE  1 
ATOM   69   N N   . ALA A 1 7   ? 2.820  -0.956  -2.733  1.00 14.89 ? 7   ALA A N   1 
ATOM   70   C CA  . ALA A 1 7   ? 3.639  -1.900  -1.989  1.00 15.29 ? 7   ALA A CA  1 
ATOM   71   C C   . ALA A 1 7   ? 3.744  -3.190  -2.803  1.00 15.57 ? 7   ALA A C   1 
ATOM   72   O O   . ALA A 1 7   ? 2.963  -3.405  -3.734  1.00 16.04 ? 7   ALA A O   1 
ATOM   73   C CB  . ALA A 1 7   ? 3.006  -2.185  -0.630  1.00 15.59 ? 7   ALA A CB  1 
ATOM   74   N N   . PHE A 1 8   ? 4.742  -4.010  -2.521  1.00 15.58 ? 8   PHE A N   1 
ATOM   75   C CA  . PHE A 1 8   ? 4.868  -5.305  -3.172  1.00 16.87 ? 8   PHE A CA  1 
ATOM   76   C C   . PHE A 1 8   ? 3.750  -6.202  -2.661  1.00 16.69 ? 8   PHE A C   1 
ATOM   77   O O   . PHE A 1 8   ? 3.298  -6.088  -1.511  1.00 16.04 ? 8   PHE A O   1 
ATOM   78   C CB  . PHE A 1 8   ? 6.222  -5.940  -2.834  1.00 17.33 ? 8   PHE A CB  1 
ATOM   79   C CG  . PHE A 1 8   ? 7.358  -5.313  -3.588  1.00 19.06 ? 8   PHE A CG  1 
ATOM   80   C CD1 . PHE A 1 8   ? 7.607  -5.651  -4.907  1.00 20.90 ? 8   PHE A CD1 1 
ATOM   81   C CD2 . PHE A 1 8   ? 8.164  -4.366  -2.990  1.00 20.60 ? 8   PHE A CD2 1 
ATOM   82   C CE1 . PHE A 1 8   ? 8.640  -5.049  -5.607  1.00 22.00 ? 8   PHE A CE1 1 
ATOM   83   C CE2 . PHE A 1 8   ? 9.209  -3.787  -3.685  1.00 21.94 ? 8   PHE A CE2 1 
ATOM   84   C CZ  . PHE A 1 8   ? 9.433  -4.123  -4.991  1.00 22.08 ? 8   PHE A CZ  1 
ATOM   85   N N   . PRO A 1 9   ? 3.322  -7.176  -3.489  1.00 17.15 ? 9   PRO A N   1 
ATOM   86   C CA  . PRO A 1 9   ? 2.348  -8.173  -3.002  1.00 17.33 ? 9   PRO A CA  1 
ATOM   87   C C   . PRO A 1 9   ? 2.939  -8.881  -1.771  1.00 17.30 ? 9   PRO A C   1 
ATOM   88   O O   . PRO A 1 9   ? 4.125  -9.203  -1.771  1.00 19.22 ? 9   PRO A O   1 
ATOM   89   C CB  . PRO A 1 9   ? 2.198  -9.124  -4.195  1.00 19.02 ? 9   PRO A CB  1 
ATOM   90   C CG  . PRO A 1 9   ? 2.667  -8.338  -5.372  1.00 19.72 ? 9   PRO A CG  1 
ATOM   91   C CD  . PRO A 1 9   ? 3.768  -7.478  -4.860  1.00 17.41 ? 9   PRO A CD  1 
ATOM   92   N N   . SER A 1 10  ? 2.170  -8.982  -0.714  1.00 15.92 ? 10  SER A N   1 
ATOM   93   C CA  . SER A 1 10  ? 2.701  -9.448  0.569   1.00 15.16 ? 10  SER A CA  1 
ATOM   94   C C   . SER A 1 10  ? 2.612  -10.944 0.842   1.00 15.12 ? 10  SER A C   1 
ATOM   95   O O   . SER A 1 10  ? 3.100  -11.378 1.869   1.00 14.73 ? 10  SER A O   1 
ATOM   96   C CB  . SER A 1 10  ? 2.029  -8.690  1.705   1.00 15.91 ? 10  SER A CB  1 
ATOM   97   O OG  . SER A 1 10  ? 0.623  -8.864  1.658   1.00 17.96 ? 10  SER A OG  1 
ATOM   98   N N   . GLY A 1 11  ? 2.001  -11.708 -0.041  1.00 15.29 ? 11  GLY A N   1 
ATOM   99   C CA  . GLY A 1 11  ? 1.797  -13.135 0.179   1.00 15.09 ? 11  GLY A CA  1 
ATOM   100  C C   . GLY A 1 11  ? 3.008  -13.943 0.596   1.00 14.62 ? 11  GLY A C   1 
ATOM   101  O O   . GLY A 1 11  ? 2.943  -14.731 1.548   1.00 15.34 ? 11  GLY A O   1 
ATOM   102  N N   . LYS A 1 12  ? 4.126  -13.735 -0.106  1.00 13.99 ? 12  LYS A N   1 
ATOM   103  C CA  . LYS A 1 12  ? 5.345  -14.487 0.193   1.00 14.02 ? 12  LYS A CA  1 
ATOM   104  C C   . LYS A 1 12  ? 5.831  -14.217 1.613   1.00 14.16 ? 12  LYS A C   1 
ATOM   105  O O   . LYS A 1 12  ? 6.375  -15.110 2.261   1.00 14.81 ? 12  LYS A O   1 
ATOM   106  C CB  . LYS A 1 12  ? 6.449  -14.195 -0.821  1.00 15.54 ? 12  LYS A CB  1 
ATOM   107  C CG  . LYS A 1 12  ? 6.209  -14.833 -2.180  1.00 19.84 ? 12  LYS A CG  1 
ATOM   108  C CD  . LYS A 1 12  ? 7.166  -14.268 -3.223  1.00 25.38 ? 12  LYS A CD  1 
ATOM   109  C CE  . LYS A 1 12  ? 6.905  -14.864 -4.589  1.00 30.94 ? 12  LYS A CE  1 
ATOM   110  N NZ  . LYS A 1 12  ? 7.019  -16.342 -4.559  1.00 34.47 ? 12  LYS A NZ  1 
ATOM   111  N N   . VAL A 1 13  ? 5.605  -12.996 2.114   1.00 13.22 ? 13  VAL A N   1 
ATOM   112  C CA  . VAL A 1 13  ? 6.032  -12.646 3.468   1.00 12.21 ? 13  VAL A CA  1 
ATOM   113  C C   . VAL A 1 13  ? 5.000  -13.074 4.500   1.00 11.66 ? 13  VAL A C   1 
ATOM   114  O O   . VAL A 1 13  ? 5.364  -13.520 5.588   1.00 11.73 ? 13  VAL A O   1 
ATOM   115  C CB  . VAL A 1 13  ? 6.355  -11.145 3.551   1.00 13.09 ? 13  VAL A CB  1 
ATOM   116  C CG1 . VAL A 1 13  ? 6.822  -10.761 4.950   1.00 14.14 ? 13  VAL A CG1 1 
ATOM   117  C CG2 . VAL A 1 13  ? 7.411  -10.784 2.519   1.00 14.34 ? 13  VAL A CG2 1 
ATOM   118  N N   . GLU A 1 14  ? 3.701  -13.021 4.159   1.00 11.62 ? 14  GLU A N   1 
ATOM   119  C CA  . GLU A 1 14  ? 2.641  -13.473 5.068   1.00 11.63 ? 14  GLU A CA  1 
ATOM   120  C C   . GLU A 1 14  ? 2.876  -14.916 5.521   1.00 12.71 ? 14  GLU A C   1 
ATOM   121  O O   . GLU A 1 14  ? 2.716  -15.224 6.703   1.00 13.03 ? 14  GLU A O   1 
ATOM   122  C CB  . GLU A 1 14  ? 1.275  -13.399 4.373   1.00 12.59 ? 14  GLU A CB  1 
ATOM   123  C CG  . GLU A 1 14  ? 0.756  -11.988 4.211   1.00 15.46 ? 14  GLU A CG  1 
ATOM   124  C CD  . GLU A 1 14  ? -0.445 -11.950 3.292   1.00 18.75 ? 14  GLU A CD  1 
ATOM   125  O OE1 . GLU A 1 14  ? -1.417 -12.694 3.553   1.00 21.44 ? 14  GLU A OE1 1 
ATOM   126  O OE2 . GLU A 1 14  ? -0.390 -11.204 2.289   1.00 19.65 ? 14  GLU A OE2 1 
ATOM   127  N N   . GLY A 1 15  ? 3.357  -15.745 4.598   1.00 12.90 ? 15  GLY A N   1 
ATOM   128  C CA  . GLY A 1 15  ? 3.649  -17.145 4.878   1.00 12.73 ? 15  GLY A CA  1 
ATOM   129  C C   . GLY A 1 15  ? 4.818  -17.392 5.810   1.00 12.45 ? 15  GLY A C   1 
ATOM   130  O O   . GLY A 1 15  ? 5.068  -18.532 6.200   1.00 13.52 ? 15  GLY A O   1 
ATOM   131  N N   . CYS A 1 16  ? 5.547  -16.341 6.161   1.00 11.59 ? 16  CYS A N   1 
ATOM   132  C CA  . CYS A 1 16  ? 6.690  -16.411 7.064   1.00 11.47 ? 16  CYS A CA  1 
ATOM   133  C C   . CYS A 1 16  ? 6.412  -15.838 8.439   1.00 11.91 ? 16  CYS A C   1 
ATOM   134  O O   . CYS A 1 16  ? 7.299  -15.910 9.283   1.00 12.77 ? 16  CYS A O   1 
ATOM   135  C CB  . CYS A 1 16  ? 7.899  -15.722 6.446   1.00 12.44 ? 16  CYS A CB  1 
ATOM   136  S SG  . CYS A 1 16  ? 8.356  -16.342 4.810   1.00 15.98 ? 16  CYS A SG  1 
ATOM   137  N N   . MET A 1 17  ? 5.240  -15.226 8.673   1.00 11.61 ? 17  MET A N   1 
ATOM   138  C CA  . MET A 1 17  ? 5.017  -14.567 9.953   1.00 12.03 ? 17  MET A CA  1 
ATOM   139  C C   . MET A 1 17  ? 4.535  -15.499 11.022  1.00 12.33 ? 17  MET A C   1 
ATOM   140  O O   . MET A 1 17  ? 3.618  -16.266 10.806  1.00 12.97 ? 17  MET A O   1 
ATOM   141  C CB  . MET A 1 17  ? 4.077  -13.372 9.816   1.00 12.21 ? 17  MET A CB  1 
ATOM   142  C CG  . MET A 1 17  ? 4.535  -12.353 8.787   1.00 13.24 ? 17  MET A CG  1 
ATOM   143  S SD  . MET A 1 17  ? 6.217  -11.703 9.005   1.00 14.39 ? 17  MET A SD  1 
ATOM   144  C CE  . MET A 1 17  ? 6.158  -11.181 10.754  1.00 15.96 ? 17  MET A CE  1 
ATOM   145  N N   . VAL A 1 18  ? 5.186  -15.438 12.176  1.00 11.86 ? 18  VAL A N   1 
ATOM   146  C CA  . VAL A 1 18  ? 4.849  -16.234 13.343  1.00 12.74 ? 18  VAL A CA  1 
ATOM   147  C C   . VAL A 1 18  ? 4.775  -15.312 14.559  1.00 12.62 ? 18  VAL A C   1 
ATOM   148  O O   . VAL A 1 18  ? 5.220  -14.160 14.518  1.00 12.38 ? 18  VAL A O   1 
ATOM   149  C CB  . VAL A 1 18  ? 5.882  -17.373 13.576  1.00 13.97 ? 18  VAL A CB  1 
ATOM   150  C CG1 . VAL A 1 18  ? 5.917  -18.341 12.404  1.00 14.87 ? 18  VAL A CG1 1 
ATOM   151  C CG2 . VAL A 1 18  ? 7.262  -16.802 13.868  1.00 13.93 ? 18  VAL A CG2 1 
ATOM   152  N N   . GLN A 1 19  ? 4.185  -15.818 15.633  1.00 12.65 ? 19  GLN A N   1 
ATOM   153  C CA  . GLN A 1 19  ? 4.107  -15.113 16.896  1.00 13.10 ? 19  GLN A CA  1 
ATOM   154  C C   . GLN A 1 19  ? 5.221  -15.641 17.802  1.00 12.93 ? 19  GLN A C   1 
ATOM   155  O O   . GLN A 1 19  ? 5.433  -16.850 17.868  1.00 12.86 ? 19  GLN A O   1 
ATOM   156  C CB  . GLN A 1 19  ? 2.735  -15.376 17.520  1.00 14.90 ? 19  GLN A CB  1 
ATOM   157  C CG  . GLN A 1 19  ? 2.552  -14.741 18.881  1.00 18.61 ? 19  GLN A CG  1 
ATOM   158  C CD  . GLN A 1 19  ? 1.293  -15.237 19.530  1.00 24.25 ? 19  GLN A CD  1 
ATOM   159  O OE1 . GLN A 1 19  ? 1.285  -16.257 20.224  1.00 26.10 ? 19  GLN A OE1 1 
ATOM   160  N NE2 . GLN A 1 19  ? 0.206  -14.527 19.326  1.00 25.55 ? 19  GLN A NE2 1 
ATOM   161  N N   . VAL A 1 20  ? 5.940  -14.742 18.500  1.00 12.43 ? 20  VAL A N   1 
ATOM   162  C CA  . VAL A 1 20  ? 6.962  -15.171 19.450  1.00 13.22 ? 20  VAL A CA  1 
ATOM   163  C C   . VAL A 1 20  ? 6.631  -14.580 20.807  1.00 13.82 ? 20  VAL A C   1 
ATOM   164  O O   . VAL A 1 20  ? 6.435  -13.367 20.921  1.00 14.21 ? 20  VAL A O   1 
ATOM   165  C CB  . VAL A 1 20  ? 8.405  -14.806 19.036  1.00 13.47 ? 20  VAL A CB  1 
ATOM   166  C CG1 . VAL A 1 20  ? 9.408  -15.330 20.066  1.00 14.22 ? 20  VAL A CG1 1 
ATOM   167  C CG2 . VAL A 1 20  ? 8.731  -15.348 17.650  1.00 13.91 ? 20  VAL A CG2 1 
ATOM   168  N N   . THR A 1 21  ? 6.537  -15.429 21.823  1.00 14.34 ? 21  THR A N   1 
ATOM   169  C CA  . THR A 1 21  ? 6.264  -14.970 23.174  1.00 15.62 ? 21  THR A CA  1 
ATOM   170  C C   . THR A 1 21  ? 7.382  -15.417 24.085  1.00 16.58 ? 21  THR A C   1 
ATOM   171  O O   . THR A 1 21  ? 7.797  -16.567 24.035  1.00 16.63 ? 21  THR A O   1 
ATOM   172  C CB  . THR A 1 21  ? 4.920  -15.534 23.681  1.00 18.06 ? 21  THR A CB  1 
ATOM   173  O OG1 . THR A 1 21  ? 3.855  -15.130 22.823  1.00 19.40 ? 21  THR A OG1 1 
ATOM   174  C CG2 . THR A 1 21  ? 4.614  -15.109 25.110  1.00 19.50 ? 21  THR A CG2 1 
ATOM   175  N N   . CYS A 1 22  ? 7.882  -14.511 24.909  1.00 17.62 ? 22  CYS A N   1 
ATOM   176  C CA  . CYS A 1 22  ? 8.866  -14.862 25.915  1.00 19.68 ? 22  CYS A CA  1 
ATOM   177  C C   . CYS A 1 22  ? 8.353  -14.192 27.181  1.00 22.21 ? 22  CYS A C   1 
ATOM   178  O O   . CYS A 1 22  ? 8.185  -12.976 27.221  1.00 22.29 ? 22  CYS A O   1 
ATOM   179  C CB  . CYS A 1 22  ? 10.273 -14.403 25.535  1.00 19.81 ? 22  CYS A CB  1 
ATOM   180  S SG  . CYS A 1 22  ? 11.574 -15.049 26.614  1.00 26.04 ? 22  CYS A SG  1 
ATOM   181  N N   . GLY A 1 23  ? 7.977  -15.014 28.151  1.00 24.20 ? 23  GLY A N   1 
ATOM   182  C CA  . GLY A 1 23  ? 7.401  -14.541 29.403  1.00 25.86 ? 23  GLY A CA  1 
ATOM   183  C C   . GLY A 1 23  ? 6.078  -13.859 29.141  1.00 27.25 ? 23  GLY A C   1 
ATOM   184  O O   . GLY A 1 23  ? 5.164  -14.465 28.577  1.00 28.42 ? 23  GLY A O   1 
ATOM   185  N N   . THR A 1 24  ? 6.013  -12.564 29.424  1.00 27.33 ? 24  THR A N   1 
ATOM   186  C CA  . THR A 1 24  ? 4.800  -11.787 29.185  1.00 27.90 ? 24  THR A CA  1 
ATOM   187  C C   . THR A 1 24  ? 4.849  -10.946 27.898  1.00 26.48 ? 24  THR A C   1 
ATOM   188  O O   . THR A 1 24  ? 3.899  -10.223 27.618  1.00 27.56 ? 24  THR A O   1 
ATOM   189  C CB  . THR A 1 24  ? 4.514  -10.899 30.395  1.00 31.42 ? 24  THR A CB  1 
ATOM   190  O OG1 . THR A 1 24  ? 5.534  -9.903  30.499  1.00 33.89 ? 24  THR A OG1 1 
ATOM   191  C CG2 . THR A 1 24  ? 4.440  -11.691 31.681  1.00 32.45 ? 24  THR A CG2 1 
ATOM   192  N N   . THR A 1 25  ? 5.938  -11.023 27.128  1.00 24.11 ? 25  THR A N   1 
ATOM   193  C CA  . THR A 1 25  ? 6.082  -10.214 25.922  1.00 22.53 ? 25  THR A CA  1 
ATOM   194  C C   . THR A 1 25  ? 5.755  -11.009 24.671  1.00 21.00 ? 25  THR A C   1 
ATOM   195  O O   . THR A 1 25  ? 6.304  -12.083 24.490  1.00 21.49 ? 25  THR A O   1 
ATOM   196  C CB  . THR A 1 25  ? 7.503  -9.662  25.850  1.00 23.52 ? 25  THR A CB  1 
ATOM   197  O OG1 . THR A 1 25  ? 7.752  -8.858  27.011  1.00 24.80 ? 25  THR A OG1 1 
ATOM   198  C CG2 . THR A 1 25  ? 7.756  -8.862  24.584  1.00 23.98 ? 25  THR A CG2 1 
ATOM   199  N N   . THR A 1 26  ? 4.880  -10.486 23.817  1.00 19.91 ? 26  THR A N   1 
ATOM   200  C CA  . THR A 1 26  ? 4.539  -11.124 22.554  1.00 19.02 ? 26  THR A CA  1 
ATOM   201  C C   . THR A 1 26  ? 4.814  -10.164 21.401  1.00 17.49 ? 26  THR A C   1 
ATOM   202  O O   . THR A 1 26  ? 4.376  -9.013  21.413  1.00 18.04 ? 26  THR A O   1 
ATOM   203  C CB  . THR A 1 26  ? 3.074  -11.584 22.541  1.00 20.95 ? 26  THR A CB  1 
ATOM   204  O OG1 . THR A 1 26  ? 2.900  -12.636 23.488  1.00 22.53 ? 26  THR A OG1 1 
ATOM   205  C CG2 . THR A 1 26  ? 2.634  -12.069 21.182  1.00 21.72 ? 26  THR A CG2 1 
ATOM   206  N N   . LEU A 1 27  ? 5.539  -10.637 20.411  1.00 15.55 ? 27  LEU A N   1 
ATOM   207  C CA  . LEU A 1 27  ? 5.787  -9.858  19.200  1.00 14.34 ? 27  LEU A CA  1 
ATOM   208  C C   . LEU A 1 27  ? 5.841  -10.794 17.990  1.00 13.54 ? 27  LEU A C   1 
ATOM   209  O O   . LEU A 1 27  ? 5.400  -11.943 18.087  1.00 13.86 ? 27  LEU A O   1 
ATOM   210  C CB  . LEU A 1 27  ? 7.007  -8.909  19.344  1.00 13.99 ? 27  LEU A CB  1 
ATOM   211  C CG  . LEU A 1 27  ? 8.263  -9.503  19.968  1.00 14.11 ? 27  LEU A CG  1 
ATOM   212  C CD1 . LEU A 1 27  ? 8.801  -10.671 19.161  1.00 14.29 ? 27  LEU A CD1 1 
ATOM   213  C CD2 . LEU A 1 27  ? 9.349  -8.450  20.127  1.00 14.70 ? 27  LEU A CD2 1 
ATOM   214  N N   . ASN A 1 28  ? 6.313  -10.302 16.845  1.00 12.24 ? 28  ASN A N   1 
ATOM   215  C CA  . ASN A 1 28  ? 6.346  -11.091 15.631  1.00 11.92 ? 28  ASN A CA  1 
ATOM   216  C C   . ASN A 1 28  ? 7.714  -11.653 15.355  1.00 11.52 ? 28  ASN A C   1 
ATOM   217  O O   . ASN A 1 28  ? 8.725  -11.066 15.710  1.00 11.85 ? 28  ASN A O   1 
ATOM   218  C CB  . ASN A 1 28  ? 5.884  -10.259 14.427  1.00 13.05 ? 28  ASN A CB  1 
ATOM   219  C CG  . ASN A 1 28  ? 4.569  -9.595  14.702  1.00 15.18 ? 28  ASN A CG  1 
ATOM   220  O OD1 . ASN A 1 28  ? 3.512  -10.223 14.621  1.00 15.52 ? 28  ASN A OD1 1 
ATOM   221  N ND2 . ASN A 1 28  ? 4.620  -8.331  15.068  1.00 15.66 ? 28  ASN A ND2 1 
ATOM   222  N N   . GLY A 1 29  ? 7.713  -12.775 14.686  1.00 11.02 ? 29  GLY A N   1 
ATOM   223  C CA  . GLY A 1 29  ? 8.925  -13.411 14.219  1.00 11.06 ? 29  GLY A CA  1 
ATOM   224  C C   . GLY A 1 29  ? 8.812  -13.718 12.738  1.00 11.20 ? 29  GLY A C   1 
ATOM   225  O O   . GLY A 1 29  ? 7.714  -13.803 12.179  1.00 11.95 ? 29  GLY A O   1 
ATOM   226  N N   . LEU A 1 30  ? 9.956  -13.877 12.090  1.00 10.90 ? 30  LEU A N   1 
ATOM   227  C CA  . LEU A 1 30  ? 10.046 -14.190 10.667  1.00 10.82 ? 30  LEU A CA  1 
ATOM   228  C C   . LEU A 1 30  ? 10.616 -15.606 10.560  1.00 10.79 ? 30  LEU A C   1 
ATOM   229  O O   . LEU A 1 30  ? 11.740 -15.840 11.002  1.00 11.77 ? 30  LEU A O   1 
ATOM   230  C CB  . LEU A 1 30  ? 10.994 -13.195 9.995   1.00 10.42 ? 30  LEU A CB  1 
ATOM   231  C CG  . LEU A 1 30  ? 11.086 -13.328 8.477   1.00 11.21 ? 30  LEU A CG  1 
ATOM   232  C CD1 . LEU A 1 30  ? 9.784  -12.894 7.816   1.00 12.16 ? 30  LEU A CD1 1 
ATOM   233  C CD2 . LEU A 1 30  ? 12.245 -12.507 7.952   1.00 12.12 ? 30  LEU A CD2 1 
ATOM   234  N N   . TRP A 1 31  ? 9.866  -16.535 9.979   1.00 10.46 ? 31  TRP A N   1 
ATOM   235  C CA  . TRP A 1 31  ? 10.255 -17.943 9.908   1.00 10.74 ? 31  TRP A CA  1 
ATOM   236  C C   . TRP A 1 31  ? 10.711 -18.287 8.502   1.00 11.18 ? 31  TRP A C   1 
ATOM   237  O O   . TRP A 1 31  ? 9.923  -18.273 7.553   1.00 11.15 ? 31  TRP A O   1 
ATOM   238  C CB  . TRP A 1 31  ? 9.054  -18.777 10.353  1.00 11.08 ? 31  TRP A CB  1 
ATOM   239  C CG  . TRP A 1 31  ? 9.218  -20.262 10.334  1.00 11.19 ? 31  TRP A CG  1 
ATOM   240  C CD1 . TRP A 1 31  ? 10.371 -20.974 10.511  1.00 11.87 ? 31  TRP A CD1 1 
ATOM   241  C CD2 . TRP A 1 31  ? 8.153  -21.221 10.295  1.00 11.18 ? 31  TRP A CD2 1 
ATOM   242  N NE1 . TRP A 1 31  ? 10.090 -22.323 10.513  1.00 11.94 ? 31  TRP A NE1 1 
ATOM   243  C CE2 . TRP A 1 31  ? 8.734  -22.499 10.412  1.00 11.98 ? 31  TRP A CE2 1 
ATOM   244  C CE3 . TRP A 1 31  ? 6.763  -21.123 10.121  1.00 11.96 ? 31  TRP A CE3 1 
ATOM   245  C CZ2 . TRP A 1 31  ? 7.976  -23.673 10.353  1.00 12.16 ? 31  TRP A CZ2 1 
ATOM   246  C CZ3 . TRP A 1 31  ? 6.013  -22.284 10.075  1.00 12.27 ? 31  TRP A CZ3 1 
ATOM   247  C CH2 . TRP A 1 31  ? 6.621  -23.544 10.169  1.00 12.25 ? 31  TRP A CH2 1 
ATOM   248  N N   . LEU A 1 32  ? 12.025 -18.505 8.356   1.00 11.11 ? 32  LEU A N   1 
ATOM   249  C CA  . LEU A 1 32  ? 12.646 -18.808 7.060   1.00 12.05 ? 32  LEU A CA  1 
ATOM   250  C C   . LEU A 1 32  ? 13.464 -20.041 7.259   1.00 12.52 ? 32  LEU A C   1 
ATOM   251  O O   . LEU A 1 32  ? 14.277 -20.097 8.192   1.00 12.39 ? 32  LEU A O   1 
ATOM   252  C CB  . LEU A 1 32  ? 13.563 -17.678 6.627   1.00 12.45 ? 32  LEU A CB  1 
ATOM   253  C CG  . LEU A 1 32  ? 12.892 -16.342 6.393   1.00 13.71 ? 32  LEU A CG  1 
ATOM   254  C CD1 . LEU A 1 32  ? 13.907 -15.285 6.173   1.00 13.62 ? 32  LEU A CD1 1 
ATOM   255  C CD2 . LEU A 1 32  ? 11.959 -16.400 5.210   1.00 14.51 ? 32  LEU A CD2 1 
ATOM   256  N N   . ASP A 1 33  ? 13.193 -21.093 6.468   1.00 12.93 ? 33  ASP A N   1 
ATOM   257  C CA  . ASP A 1 33  ? 13.854 -22.381 6.675   1.00 13.70 ? 33  ASP A CA  1 
ATOM   258  C C   . ASP A 1 33  ? 13.561 -22.852 8.132   1.00 13.91 ? 33  ASP A C   1 
ATOM   259  O O   . ASP A 1 33  ? 12.412 -22.706 8.557   1.00 14.60 ? 33  ASP A O   1 
ATOM   260  C CB  . ASP A 1 33  ? 15.356 -22.306 6.311   1.00 16.27 ? 33  ASP A CB  1 
ATOM   261  C CG  . ASP A 1 33  ? 15.597 -21.887 4.883   1.00 21.63 ? 33  ASP A CG  1 
ATOM   262  O OD1 . ASP A 1 33  ? 14.817 -22.304 4.008   1.00 23.84 ? 33  ASP A OD1 1 
ATOM   263  O OD2 . ASP A 1 33  ? 16.574 -21.142 4.642   1.00 23.06 ? 33  ASP A OD2 1 
ATOM   264  N N   . ASP A 1 34  ? 14.549 -23.299 8.901   1.00 12.95 ? 34  ASP A N   1 
ATOM   265  C CA  . ASP A 1 34  ? 14.306 -23.727 10.265  1.00 12.62 ? 34  ASP A CA  1 
ATOM   266  C C   . ASP A 1 34  ? 14.745 -22.702 11.278  1.00 12.42 ? 34  ASP A C   1 
ATOM   267  O O   . ASP A 1 34  ? 15.104 -23.073 12.395  1.00 13.06 ? 34  ASP A O   1 
ATOM   268  C CB  . ASP A 1 34  ? 14.988 -25.077 10.522  1.00 13.51 ? 34  ASP A CB  1 
ATOM   269  C CG  . ASP A 1 34  ? 16.497 -25.078 10.331  1.00 17.85 ? 34  ASP A CG  1 
ATOM   270  O OD1 . ASP A 1 34  ? 17.037 -24.076 9.798   1.00 17.68 ? 34  ASP A OD1 1 
ATOM   271  O OD2 . ASP A 1 34  ? 17.138 -26.087 10.709  1.00 20.21 ? 34  ASP A OD2 1 
ATOM   272  N N   . VAL A 1 35  ? 14.689 -21.404 10.928  1.00 11.43 ? 35  VAL A N   1 
ATOM   273  C CA  . VAL A 1 35  ? 15.074 -20.358 11.868  1.00 12.04 ? 35  VAL A CA  1 
ATOM   274  C C   . VAL A 1 35  ? 13.987 -19.307 11.950  1.00 11.65 ? 35  VAL A C   1 
ATOM   275  O O   . VAL A 1 35  ? 13.400 -18.939 10.930  1.00 12.01 ? 35  VAL A O   1 
ATOM   276  C CB  . VAL A 1 35  ? 16.424 -19.702 11.481  1.00 13.42 ? 35  VAL A CB  1 
ATOM   277  C CG1 . VAL A 1 35  ? 16.824 -18.604 12.473  1.00 13.93 ? 35  VAL A CG1 1 
ATOM   278  C CG2 . VAL A 1 35  ? 17.519 -20.750 11.384  1.00 14.17 ? 35  VAL A CG2 1 
ATOM   279  N N   . VAL A 1 36  ? 13.699 -18.861 13.164  1.00 11.24 ? 36  VAL A N   1 
ATOM   280  C CA  . VAL A 1 36  ? 12.775 -17.774 13.408  1.00 11.41 ? 36  VAL A CA  1 
ATOM   281  C C   . VAL A 1 36  ? 13.589 -16.584 13.895  1.00 11.05 ? 36  VAL A C   1 
ATOM   282  O O   . VAL A 1 36  ? 14.339 -16.704 14.855  1.00 10.78 ? 36  VAL A O   1 
ATOM   283  C CB  . VAL A 1 36  ? 11.676 -18.169 14.404  1.00 12.20 ? 36  VAL A CB  1 
ATOM   284  C CG1 . VAL A 1 36  ? 10.833 -16.957 14.781  1.00 12.52 ? 36  VAL A CG1 1 
ATOM   285  C CG2 . VAL A 1 36  ? 10.810 -19.281 13.826  1.00 12.70 ? 36  VAL A CG2 1 
ATOM   286  N N   . TYR A 1 37  ? 13.465 -15.444 13.220  1.00 11.02 ? 37  TYR A N   1 
ATOM   287  C CA  . TYR A 1 37  ? 14.205 -14.229 13.566  1.00 10.75 ? 37  TYR A CA  1 
ATOM   288  C C   . TYR A 1 37  ? 13.256 -13.286 14.257  1.00 11.13 ? 37  TYR A C   1 
ATOM   289  O O   . TYR A 1 37  ? 12.130 -13.095 13.787  1.00 11.97 ? 37  TYR A O   1 
ATOM   290  C CB  . TYR A 1 37  ? 14.693 -13.529 12.285  1.00 10.59 ? 37  TYR A CB  1 
ATOM   291  C CG  . TYR A 1 37  ? 15.597 -14.400 11.453  1.00 11.51 ? 37  TYR A CG  1 
ATOM   292  C CD1 . TYR A 1 37  ? 15.076 -15.318 10.558  1.00 12.49 ? 37  TYR A CD1 1 
ATOM   293  C CD2 . TYR A 1 37  ? 16.974 -14.306 11.565  1.00 12.68 ? 37  TYR A CD2 1 
ATOM   294  C CE1 . TYR A 1 37  ? 15.904 -16.163 9.830   1.00 13.67 ? 37  TYR A CE1 1 
ATOM   295  C CE2 . TYR A 1 37  ? 17.814 -15.115 10.809  1.00 13.61 ? 37  TYR A CE2 1 
ATOM   296  C CZ  . TYR A 1 37  ? 17.275 -16.032 9.932   1.00 14.78 ? 37  TYR A CZ  1 
ATOM   297  O OH  . TYR A 1 37  ? 18.101 -16.885 9.229   1.00 17.25 ? 37  TYR A OH  1 
ATOM   298  N N   . CYS A 1 38  ? 13.677 -12.713 15.375  1.00 10.69 ? 38  CYS A N   1 
ATOM   299  C CA  . CYS A 1 38  ? 12.825 -11.757 16.071  1.00 10.98 ? 38  CYS A CA  1 
ATOM   300  C C   . CYS A 1 38  ? 13.672 -10.755 16.841  1.00 11.25 ? 38  CYS A C   1 
ATOM   301  O O   . CYS A 1 38  ? 14.846 -11.012 17.094  1.00 11.69 ? 38  CYS A O   1 
ATOM   302  C CB  . CYS A 1 38  ? 11.815 -12.484 16.958  1.00 11.60 ? 38  CYS A CB  1 
ATOM   303  S SG  . CYS A 1 38  ? 12.515 -13.143 18.487  1.00 13.48 ? 38  CYS A SG  1 
ATOM   304  N N   . PRO A 1 39  ? 13.111 -9.604  17.244  1.00 10.96 ? 39  PRO A N   1 
ATOM   305  C CA  . PRO A 1 39  ? 13.899 -8.651  18.033  1.00 10.74 ? 39  PRO A CA  1 
ATOM   306  C C   . PRO A 1 39  ? 14.331 -9.281  19.350  1.00 11.52 ? 39  PRO A C   1 
ATOM   307  O O   . PRO A 1 39  ? 13.544 -9.987  19.992  1.00 12.03 ? 39  PRO A O   1 
ATOM   308  C CB  . PRO A 1 39  ? 12.903 -7.512  18.282  1.00 11.14 ? 39  PRO A CB  1 
ATOM   309  C CG  . PRO A 1 39  ? 11.956 -7.602  17.126  1.00 11.48 ? 39  PRO A CG  1 
ATOM   310  C CD  . PRO A 1 39  ? 11.753 -9.084  16.998  1.00 10.66 ? 39  PRO A CD  1 
ATOM   311  N N   . ARG A 1 40  ? 15.581 -9.024  19.762  1.00 11.03 ? 40  ARG A N   1 
ATOM   312  C CA  . ARG A 1 40  ? 16.049 -9.593  21.020  1.00 11.30 ? 40  ARG A CA  1 
ATOM   313  C C   . ARG A 1 40  ? 15.284 -9.013  22.218  1.00 12.95 ? 40  ARG A C   1 
ATOM   314  O O   . ARG A 1 40  ? 15.228 -9.680  23.250  1.00 13.60 ? 40  ARG A O   1 
ATOM   315  C CB  . ARG A 1 40  ? 17.549 -9.444  21.184  1.00 11.64 ? 40  ARG A CB  1 
ATOM   316  C CG  . ARG A 1 40  ? 17.977 -8.012  21.332  1.00 12.88 ? 40  ARG A CG  1 
ATOM   317  C CD  . ARG A 1 40  ? 19.457 -7.968  21.572  1.00 13.12 ? 40  ARG A CD  1 
ATOM   318  N NE  . ARG A 1 40  ? 19.935 -6.599  21.666  1.00 14.21 ? 40  ARG A NE  1 
ATOM   319  C CZ  . ARG A 1 40  ? 21.174 -6.261  21.996  1.00 15.68 ? 40  ARG A CZ  1 
ATOM   320  N NH1 . ARG A 1 40  ? 22.082 -7.197  22.248  1.00 15.22 ? 40  ARG A NH1 1 
ATOM   321  N NH2 . ARG A 1 40  ? 21.519 -4.983  22.070  1.00 15.20 ? 40  ARG A NH2 1 
ATOM   322  N N   . HIS A 1 41  ? 14.628 -7.836  22.073  1.00 13.07 ? 41  HIS A N   1 
ATOM   323  C CA  . HIS A 1 41  ? 13.892 -7.269  23.196  1.00 13.76 ? 41  HIS A CA  1 
ATOM   324  C C   . HIS A 1 41  ? 12.612 -8.048  23.529  1.00 14.57 ? 41  HIS A C   1 
ATOM   325  O O   . HIS A 1 41  ? 11.970 -7.700  24.519  1.00 14.99 ? 41  HIS A O   1 
ATOM   326  C CB  . HIS A 1 41  ? 13.651 -5.754  23.097  1.00 14.02 ? 41  HIS A CB  1 
ATOM   327  C CG  . HIS A 1 41  ? 12.654 -5.295  22.083  1.00 16.36 ? 41  HIS A CG  1 
ATOM   328  N ND1 . HIS A 1 41  ? 11.296 -5.507  22.253  1.00 19.44 ? 41  HIS A ND1 1 
ATOM   329  C CD2 . HIS A 1 41  ? 12.838 -4.516  20.993  1.00 17.15 ? 41  HIS A CD2 1 
ATOM   330  C CE1 . HIS A 1 41  ? 10.708 -4.914  21.223  1.00 19.39 ? 41  HIS A CE1 1 
ATOM   331  N NE2 . HIS A 1 41  ? 11.596 -4.303  20.441  1.00 18.52 ? 41  HIS A NE2 1 
ATOM   332  N N   . VAL A 1 42  ? 12.320 -9.175  22.827  1.00 14.08 ? 42  VAL A N   1 
ATOM   333  C CA  . VAL A 1 42  ? 11.239 -10.064 23.272  1.00 14.58 ? 42  VAL A CA  1 
ATOM   334  C C   . VAL A 1 42  ? 11.547 -10.606 24.697  1.00 15.27 ? 42  VAL A C   1 
ATOM   335  O O   . VAL A 1 42  ? 10.628 -10.903 25.447  1.00 16.44 ? 42  VAL A O   1 
ATOM   336  C CB  . VAL A 1 42  ? 10.982 -11.221 22.276  1.00 14.96 ? 42  VAL A CB  1 
ATOM   337  C CG1 . VAL A 1 42  ? 12.125 -12.225 22.274  1.00 14.97 ? 42  VAL A CG1 1 
ATOM   338  C CG2 . VAL A 1 42  ? 9.651  -11.914 22.559  1.00 15.69 ? 42  VAL A CG2 1 
ATOM   339  N N   . ILE A 1 43  ? 12.839 -10.667 25.091  1.00 14.68 ? 43  ILE A N   1 
ATOM   340  C CA  . ILE A 1 43  ? 13.211 -11.149 26.424  1.00 15.70 ? 43  ILE A CA  1 
ATOM   341  C C   . ILE A 1 43  ? 13.082 -10.078 27.518  1.00 18.13 ? 43  ILE A C   1 
ATOM   342  O O   . ILE A 1 43  ? 13.347 -10.366 28.682  1.00 18.87 ? 43  ILE A O   1 
ATOM   343  C CB  . ILE A 1 43  ? 14.635 -11.767 26.406  1.00 15.42 ? 43  ILE A CB  1 
ATOM   344  C CG1 . ILE A 1 43  ? 15.718 -10.687 26.276  1.00 15.89 ? 43  ILE A CG1 1 
ATOM   345  C CG2 . ILE A 1 43  ? 14.757 -12.817 25.294  1.00 15.89 ? 43  ILE A CG2 1 
ATOM   346  C CD1 . ILE A 1 43  ? 17.155 -11.214 26.301  1.00 17.16 ? 43  ILE A CD1 1 
ATOM   347  N N   . CYS A 1 44  ? 12.700 -8.851  27.161  1.00 19.70 ? 44  CYS A N   1 
ATOM   348  C CA  . CYS A 1 44  ? 12.587 -7.761  28.109  1.00 22.56 ? 44  CYS A CA  1 
ATOM   349  C C   . CYS A 1 44  ? 11.166 -7.545  28.562  1.00 26.82 ? 44  CYS A C   1 
ATOM   350  O O   . CYS A 1 44  ? 10.221 -7.737  27.806  1.00 27.66 ? 44  CYS A O   1 
ATOM   351  C CB  . CYS A 1 44  ? 13.121 -6.476  27.485  1.00 22.30 ? 44  CYS A CB  1 
ATOM   352  S SG  . CYS A 1 44  ? 14.871 -6.530  27.050  1.00 22.16 ? 44  CYS A SG  1 
ATOM   353  N N   . THR A 1 45  ? 11.039 -7.011  29.755  1.00 29.51 ? 45  THR A N   1 
ATOM   354  C CA  . THR A 1 45  ? 9.787  -6.494  30.270  1.00 32.18 ? 45  THR A CA  1 
ATOM   355  C C   . THR A 1 45  ? 9.827  -4.970  29.895  1.00 34.36 ? 45  THR A C   1 
ATOM   356  O O   . THR A 1 45  ? 10.846 -4.488  29.368  1.00 34.59 ? 45  THR A O   1 
ATOM   357  C CB  . THR A 1 45  ? 9.740  -6.707  31.794  1.00 34.04 ? 45  THR A CB  1 
ATOM   358  O OG1 . THR A 1 45  ? 10.699 -5.849  32.419  1.00 35.60 ? 45  THR A OG1 1 
ATOM   359  C CG2 . THR A 1 45  ? 10.010 -8.155  32.194  1.00 34.58 ? 45  THR A CG2 1 
ATOM   360  N N   . SER A 1 46  ? 8.754  -4.205  30.188  1.00 35.48 ? 46  SER A N   1 
ATOM   361  C CA  . SER A 1 46  ? 8.778  -2.760  29.936  1.00 36.69 ? 46  SER A CA  1 
ATOM   362  C C   . SER A 1 46  ? 9.855  -2.090  30.824  1.00 37.23 ? 46  SER A C   1 
ATOM   363  O O   . SER A 1 46  ? 10.511 -1.144  30.383  1.00 37.54 ? 46  SER A O   1 
ATOM   364  C CB  . SER A 1 46  ? 7.409  -2.137  30.185  1.00 38.60 ? 46  SER A CB  1 
ATOM   365  O OG  . SER A 1 46  ? 7.293  -0.915  29.474  1.00 42.31 ? 46  SER A OG  1 
ATOM   366  N N   . GLU A 1 47  ? 10.064 -2.620  32.051  1.00 37.15 ? 47  GLU A N   1 
ATOM   367  C CA  . GLU A 1 47  ? 11.067 -2.151  33.007  1.00 37.30 ? 47  GLU A CA  1 
ATOM   368  C C   . GLU A 1 47  ? 12.485 -2.408  32.486  1.00 36.61 ? 47  GLU A C   1 
ATOM   369  O O   . GLU A 1 47  ? 13.323 -1.506  32.541  1.00 37.19 ? 47  GLU A O   1 
ATOM   370  C CB  . GLU A 1 47  ? 10.871 -2.832  34.379  1.00 40.16 ? 47  GLU A CB  1 
ATOM   371  C CG  . GLU A 1 47  ? 11.899 -2.401  35.412  1.00 46.08 ? 47  GLU A CG  1 
ATOM   372  C CD  . GLU A 1 47  ? 11.871 -3.137  36.739  1.00 53.53 ? 47  GLU A CD  1 
ATOM   373  O OE1 . GLU A 1 47  ? 11.167 -4.168  36.840  1.00 55.04 ? 47  GLU A OE1 1 
ATOM   374  O OE2 . GLU A 1 47  ? 12.559 -2.680  37.681  1.00 56.09 ? 47  GLU A OE2 1 
ATOM   375  N N   . ASP A 1 48  ? 12.752 -3.629  31.971  1.00 35.12 ? 48  ASP A N   1 
ATOM   376  C CA  . ASP A 1 48  ? 14.071 -3.994  31.442  1.00 34.07 ? 48  ASP A CA  1 
ATOM   377  C C   . ASP A 1 48  ? 14.517 -3.050  30.338  1.00 32.73 ? 48  ASP A C   1 
ATOM   378  O O   . ASP A 1 48  ? 15.695 -2.736  30.268  1.00 32.68 ? 48  ASP A O   1 
ATOM   379  C CB  . ASP A 1 48  ? 14.089 -5.430  30.884  1.00 35.22 ? 48  ASP A CB  1 
ATOM   380  C CG  . ASP A 1 48  ? 14.024 -6.544  31.907  1.00 39.53 ? 48  ASP A CG  1 
ATOM   381  O OD1 . ASP A 1 48  ? 14.540 -6.353  33.029  1.00 39.78 ? 48  ASP A OD1 1 
ATOM   382  O OD2 . ASP A 1 48  ? 13.467 -7.614  31.581  1.00 41.68 ? 48  ASP A OD2 1 
ATOM   383  N N   . MET A 1 49  ? 13.587 -2.587  29.486  1.00 31.75 ? 49  MET A N   1 
ATOM   384  C CA  . MET A 1 49  ? 13.915 -1.698  28.369  1.00 31.02 ? 49  MET A CA  1 
ATOM   385  C C   . MET A 1 49  ? 14.627 -0.405  28.761  1.00 30.28 ? 49  MET A C   1 
ATOM   386  O O   . MET A 1 49  ? 15.313 0.164   27.924  1.00 29.65 ? 49  MET A O   1 
ATOM   387  C CB  . MET A 1 49  ? 12.679 -1.384  27.513  1.00 31.35 ? 49  MET A CB  1 
ATOM   388  C CG  . MET A 1 49  ? 12.174 -2.572  26.724  1.00 32.65 ? 49  MET A CG  1 
ATOM   389  S SD  . MET A 1 49  ? 13.436 -3.315  25.650  1.00 33.34 ? 49  MET A SD  1 
ATOM   390  C CE  . MET A 1 49  ? 13.560 -2.060  24.368  1.00 27.71 ? 49  MET A CE  1 
ATOM   391  N N   . LEU A 1 50  ? 14.493 0.050   30.009  1.00 30.11 ? 50  LEU A N   1 
ATOM   392  C CA  . LEU A 1 50  ? 15.162 1.274   30.453  1.00 30.70 ? 50  LEU A CA  1 
ATOM   393  C C   . LEU A 1 50  ? 16.689 1.159   30.403  1.00 30.56 ? 50  LEU A C   1 
ATOM   394  O O   . LEU A 1 50  ? 17.345 2.089   29.955  1.00 31.26 ? 50  LEU A O   1 
ATOM   395  C CB  . LEU A 1 50  ? 14.682 1.683   31.851  1.00 31.34 ? 50  LEU A CB  1 
ATOM   396  C CG  . LEU A 1 50  ? 13.191 1.988   31.949  1.00 33.68 ? 50  LEU A CG  1 
ATOM   397  C CD1 . LEU A 1 50  ? 12.778 2.229   33.387  1.00 34.43 ? 50  LEU A CD1 1 
ATOM   398  C CD2 . LEU A 1 50  ? 12.806 3.173   31.059  1.00 34.52 ? 50  LEU A CD2 1 
ATOM   399  N N   . ASN A 1 51  ? 17.251 0.022   30.820  1.00 29.29 ? 51  ASN A N   1 
ATOM   400  C CA  . ASN A 1 51  ? 18.701 -0.204  30.771  1.00 28.56 ? 51  ASN A CA  1 
ATOM   401  C C   . ASN A 1 51  ? 18.964 -1.718  30.692  1.00 26.51 ? 51  ASN A C   1 
ATOM   402  O O   . ASN A 1 51  ? 19.400 -2.327  31.674  1.00 26.96 ? 51  ASN A O   1 
ATOM   403  C CB  . ASN A 1 51  ? 19.381 0.398   32.009  1.00 30.92 ? 51  ASN A CB  1 
ATOM   404  C CG  . ASN A 1 51  ? 20.892 0.388   31.942  1.00 35.07 ? 51  ASN A CG  1 
ATOM   405  O OD1 . ASN A 1 51  ? 21.493 0.225   30.873  1.00 36.86 ? 51  ASN A OD1 1 
ATOM   406  N ND2 . ASN A 1 51  ? 21.539 0.567   33.085  1.00 36.16 ? 51  ASN A ND2 1 
ATOM   407  N N   . PRO A 1 52  ? 18.640 -2.362  29.557  1.00 23.74 ? 52  PRO A N   1 
ATOM   408  C CA  . PRO A 1 52  ? 18.791 -3.824  29.494  1.00 22.58 ? 52  PRO A CA  1 
ATOM   409  C C   . PRO A 1 52  ? 20.203 -4.339  29.261  1.00 21.84 ? 52  PRO A C   1 
ATOM   410  O O   . PRO A 1 52  ? 20.938 -3.775  28.461  1.00 23.02 ? 52  PRO A O   1 
ATOM   411  C CB  . PRO A 1 52  ? 17.858 -4.228  28.347  1.00 23.00 ? 52  PRO A CB  1 
ATOM   412  C CG  . PRO A 1 52  ? 17.799 -3.012  27.462  1.00 23.84 ? 52  PRO A CG  1 
ATOM   413  C CD  . PRO A 1 52  ? 18.087 -1.804  28.306  1.00 23.00 ? 52  PRO A CD  1 
ATOM   414  N N   . ASN A 1 53  ? 20.579 -5.426  29.948  1.00 20.08 ? 53  ASN A N   1 
ATOM   415  C CA  . ASN A 1 53  ? 21.843 -6.098  29.676  1.00 19.44 ? 53  ASN A CA  1 
ATOM   416  C C   . ASN A 1 53  ? 21.378 -7.382  29.004  1.00 19.09 ? 53  ASN A C   1 
ATOM   417  O O   . ASN A 1 53  ? 20.976 -8.328  29.682  1.00 19.86 ? 53  ASN A O   1 
ATOM   418  C CB  . ASN A 1 53  ? 22.650 -6.418  30.934  1.00 20.41 ? 53  ASN A CB  1 
ATOM   419  C CG  . ASN A 1 53  ? 24.001 -6.990  30.569  1.00 23.36 ? 53  ASN A CG  1 
ATOM   420  O OD1 . ASN A 1 53  ? 24.112 -7.970  29.818  1.00 24.42 ? 53  ASN A OD1 1 
ATOM   421  N ND2 . ASN A 1 53  ? 25.063 -6.397  31.086  1.00 23.75 ? 53  ASN A ND2 1 
ATOM   422  N N   . TYR A 1 54  ? 21.348 -7.382  27.684  1.00 18.47 ? 54  TYR A N   1 
ATOM   423  C CA  . TYR A 1 54  ? 20.814 -8.489  26.923  1.00 17.26 ? 54  TYR A CA  1 
ATOM   424  C C   . TYR A 1 54  ? 21.500 -9.801  27.153  1.00 17.52 ? 54  TYR A C   1 
ATOM   425  O O   . TYR A 1 54  ? 20.800 -10.791 27.331  1.00 17.53 ? 54  TYR A O   1 
ATOM   426  C CB  . TYR A 1 54  ? 20.781 -8.147  25.448  1.00 15.88 ? 54  TYR A CB  1 
ATOM   427  C CG  . TYR A 1 54  ? 19.666 -7.180  25.141  1.00 15.71 ? 54  TYR A CG  1 
ATOM   428  C CD1 . TYR A 1 54  ? 18.353 -7.614  25.039  1.00 16.04 ? 54  TYR A CD1 1 
ATOM   429  C CD2 . TYR A 1 54  ? 19.916 -5.823  25.004  1.00 15.93 ? 54  TYR A CD2 1 
ATOM   430  C CE1 . TYR A 1 54  ? 17.320 -6.725  24.759  1.00 16.34 ? 54  TYR A CE1 1 
ATOM   431  C CE2 . TYR A 1 54  ? 18.897 -4.929  24.714  1.00 16.57 ? 54  TYR A CE2 1 
ATOM   432  C CZ  . TYR A 1 54  ? 17.596 -5.382  24.598  1.00 17.28 ? 54  TYR A CZ  1 
ATOM   433  O OH  . TYR A 1 54  ? 16.582 -4.489  24.330  1.00 18.46 ? 54  TYR A OH  1 
ATOM   434  N N   . GLU A 1 55  ? 22.849 -9.837  27.217  1.00 18.17 ? 55  GLU A N   1 
ATOM   435  C CA  . GLU A 1 55  ? 23.536 -11.110 27.478  1.00 18.88 ? 55  GLU A CA  1 
ATOM   436  C C   . GLU A 1 55  ? 23.132 -11.677 28.833  1.00 19.05 ? 55  GLU A C   1 
ATOM   437  O O   . GLU A 1 55  ? 22.911 -12.883 28.953  1.00 19.30 ? 55  GLU A O   1 
ATOM   438  C CB  . GLU A 1 55  ? 25.069 -10.991 27.409  1.00 22.09 ? 55  GLU A CB  1 
ATOM   439  C CG  . GLU A 1 55  ? 25.638 -10.894 26.003  1.00 27.99 ? 55  GLU A CG  1 
ATOM   440  C CD  . GLU A 1 55  ? 25.669 -12.141 25.133  1.00 34.81 ? 55  GLU A CD  1 
ATOM   441  O OE1 . GLU A 1 55  ? 25.127 -13.194 25.538  1.00 33.74 ? 55  GLU A OE1 1 
ATOM   442  O OE2 . GLU A 1 55  ? 26.209 -12.043 24.007  1.00 39.00 ? 55  GLU A OE2 1 
ATOM   443  N N   . ASP A 1 56  ? 22.991 -10.802 29.841  1.00 18.58 ? 56  ASP A N   1 
ATOM   444  C CA  . ASP A 1 56  ? 22.594 -11.263 31.171  1.00 18.89 ? 56  ASP A CA  1 
ATOM   445  C C   . ASP A 1 56  ? 21.151 -11.742 31.203  1.00 19.04 ? 56  ASP A C   1 
ATOM   446  O O   . ASP A 1 56  ? 20.872 -12.782 31.794  1.00 20.06 ? 56  ASP A O   1 
ATOM   447  C CB  . ASP A 1 56  ? 22.838 -10.181 32.232  1.00 20.13 ? 56  ASP A CB  1 
ATOM   448  C CG  . ASP A 1 56  ? 24.304 -9.937  32.525  1.00 23.92 ? 56  ASP A CG  1 
ATOM   449  O OD1 . ASP A 1 56  ? 25.133 -10.830 32.216  1.00 23.66 ? 56  ASP A OD1 1 
ATOM   450  O OD2 . ASP A 1 56  ? 24.630 -8.853  33.067  1.00 25.46 ? 56  ASP A OD2 1 
ATOM   451  N N   . LEU A 1 57  ? 20.235 -11.002 30.566  1.00 18.53 ? 57  LEU A N   1 
ATOM   452  C CA  . LEU A 1 57  ? 18.835 -11.405 30.531  1.00 18.71 ? 57  LEU A CA  1 
ATOM   453  C C   . LEU A 1 57  ? 18.663 -12.733 29.781  1.00 18.63 ? 57  LEU A C   1 
ATOM   454  O O   . LEU A 1 57  ? 17.847 -13.565 30.166  1.00 18.76 ? 57  LEU A O   1 
ATOM   455  C CB  . LEU A 1 57  ? 17.989 -10.323 29.851  1.00 19.11 ? 57  LEU A CB  1 
ATOM   456  C CG  . LEU A 1 57  ? 17.861 -9.013  30.615  1.00 21.19 ? 57  LEU A CG  1 
ATOM   457  C CD1 . LEU A 1 57  ? 17.170 -7.968  29.770  1.00 22.03 ? 57  LEU A CD1 1 
ATOM   458  C CD2 . LEU A 1 57  ? 17.084 -9.216  31.913  1.00 22.04 ? 57  LEU A CD2 1 
ATOM   459  N N   . LEU A 1 58  ? 19.446 -12.932 28.724  1.00 17.87 ? 58  LEU A N   1 
ATOM   460  C CA  . LEU A 1 58  ? 19.353 -14.126 27.908  1.00 18.31 ? 58  LEU A CA  1 
ATOM   461  C C   . LEU A 1 58  ? 19.824 -15.379 28.634  1.00 18.99 ? 58  LEU A C   1 
ATOM   462  O O   . LEU A 1 58  ? 19.291 -16.458 28.361  1.00 19.97 ? 58  LEU A O   1 
ATOM   463  C CB  . LEU A 1 58  ? 20.098 -13.912 26.579  1.00 18.33 ? 58  LEU A CB  1 
ATOM   464  C CG  . LEU A 1 58  ? 19.768 -14.878 25.447  1.00 19.20 ? 58  LEU A CG  1 
ATOM   465  C CD1 . LEU A 1 58  ? 18.284 -14.903 25.133  1.00 18.38 ? 58  LEU A CD1 1 
ATOM   466  C CD2 . LEU A 1 58  ? 20.620 -14.581 24.225  1.00 20.01 ? 58  LEU A CD2 1 
ATOM   467  N N   . ILE A 1 59  ? 20.748 -15.251 29.613  1.00 18.93 ? 59  ILE A N   1 
ATOM   468  C CA  . ILE A 1 59  ? 21.213 -16.402 30.410  1.00 20.28 ? 59  ILE A CA  1 
ATOM   469  C C   . ILE A 1 59  ? 20.039 -17.065 31.138  1.00 20.86 ? 59  ILE A C   1 
ATOM   470  O O   . ILE A 1 59  ? 20.042 -18.276 31.340  1.00 21.11 ? 59  ILE A O   1 
ATOM   471  C CB  . ILE A 1 59  ? 22.308 -15.997 31.439  1.00 22.03 ? 59  ILE A CB  1 
ATOM   472  C CG1 . ILE A 1 59  ? 23.587 -15.552 30.751  1.00 24.25 ? 59  ILE A CG1 1 
ATOM   473  C CG2 . ILE A 1 59  ? 22.606 -17.132 32.438  1.00 23.10 ? 59  ILE A CG2 1 
ATOM   474  C CD1 . ILE A 1 59  ? 24.600 -14.933 31.734  1.00 26.45 ? 59  ILE A CD1 1 
ATOM   475  N N   . ARG A 1 60  ? 19.043 -16.267 31.544  1.00 21.21 ? 60  ARG A N   1 
ATOM   476  C CA  . ARG A 1 60  ? 17.885 -16.790 32.250  1.00 22.07 ? 60  ARG A CA  1 
ATOM   477  C C   . ARG A 1 60  ? 16.844 -17.440 31.336  1.00 21.30 ? 60  ARG A C   1 
ATOM   478  O O   . ARG A 1 60  ? 15.812 -17.882 31.826  1.00 22.28 ? 60  ARG A O   1 
ATOM   479  C CB  . ARG A 1 60  ? 17.247 -15.694 33.120  1.00 24.65 ? 60  ARG A CB  1 
ATOM   480  C CG  . ARG A 1 60  ? 18.246 -14.947 33.999  1.00 29.44 ? 60  ARG A CG  1 
ATOM   481  C CD  . ARG A 1 60  ? 18.917 -15.852 35.008  1.00 33.62 ? 60  ARG A CD  1 
ATOM   482  N NE  . ARG A 1 60  ? 20.227 -15.335 35.399  1.00 37.98 ? 60  ARG A NE  1 
ATOM   483  C CZ  . ARG A 1 60  ? 21.142 -16.030 36.067  1.00 40.16 ? 60  ARG A CZ  1 
ATOM   484  N NH1 . ARG A 1 60  ? 22.307 -15.479 36.372  1.00 39.79 ? 60  ARG A NH1 1 
ATOM   485  N NH2 . ARG A 1 60  ? 20.898 -17.284 36.432  1.00 40.17 ? 60  ARG A NH2 1 
ATOM   486  N N   . LYS A 1 61  ? 17.089 -17.491 30.014  1.00 19.36 ? 61  LYS A N   1 
ATOM   487  C CA  . LYS A 1 61  ? 16.134 -18.067 29.078  1.00 18.81 ? 61  LYS A CA  1 
ATOM   488  C C   . LYS A 1 61  ? 16.645 -19.373 28.501  1.00 19.17 ? 61  LYS A C   1 
ATOM   489  O O   . LYS A 1 61  ? 17.832 -19.513 28.216  1.00 20.35 ? 61  LYS A O   1 
ATOM   490  C CB  . LYS A 1 61  ? 15.853 -17.072 27.936  1.00 19.82 ? 61  LYS A CB  1 
ATOM   491  C CG  . LYS A 1 61  ? 15.324 -15.717 28.401  1.00 22.51 ? 61  LYS A CG  1 
ATOM   492  C CD  . LYS A 1 61  ? 14.023 -15.821 29.196  1.00 26.00 ? 61  LYS A CD  1 
ATOM   493  C CE  . LYS A 1 61  ? 13.493 -14.456 29.568  1.00 29.36 ? 61  LYS A CE  1 
ATOM   494  N NZ  . LYS A 1 61  ? 12.260 -14.538 30.405  1.00 32.04 ? 61  LYS A NZ  1 
ATOM   495  N N   . SER A 1 62  ? 15.745 -20.338 28.359  1.00 17.84 ? 62  SER A N   1 
ATOM   496  C CA  . SER A 1 62  ? 16.030 -21.625 27.751  1.00 17.70 ? 62  SER A CA  1 
ATOM   497  C C   . SER A 1 62  ? 15.168 -21.747 26.476  1.00 16.11 ? 62  SER A C   1 
ATOM   498  O O   . SER A 1 62  ? 14.219 -20.985 26.286  1.00 15.44 ? 62  SER A O   1 
ATOM   499  C CB  . SER A 1 62  ? 15.673 -22.756 28.709  1.00 20.52 ? 62  SER A CB  1 
ATOM   500  O OG  . SER A 1 62  ? 16.454 -22.685 29.891  1.00 23.82 ? 62  SER A OG  1 
ATOM   501  N N   . ASN A 1 63  ? 15.466 -22.730 25.611  1.00 15.74 ? 63  ASN A N   1 
ATOM   502  C CA  . ASN A 1 63  ? 14.663 -22.963 24.399  1.00 15.24 ? 63  ASN A CA  1 
ATOM   503  C C   . ASN A 1 63  ? 13.166 -23.023 24.663  1.00 15.14 ? 63  ASN A C   1 
ATOM   504  O O   . ASN A 1 63  ? 12.399 -22.427 23.914  1.00 15.00 ? 63  ASN A O   1 
ATOM   505  C CB  . ASN A 1 63  ? 15.077 -24.261 23.732  1.00 15.61 ? 63  ASN A CB  1 
ATOM   506  C CG  . ASN A 1 63  ? 16.449 -24.203 23.162  1.00 17.36 ? 63  ASN A CG  1 
ATOM   507  O OD1 . ASN A 1 63  ? 16.926 -23.144 22.757  1.00 17.17 ? 63  ASN A OD1 1 
ATOM   508  N ND2 . ASN A 1 63  ? 17.110 -25.341 23.087  1.00 17.34 ? 63  ASN A ND2 1 
ATOM   509  N N   . HIS A 1 64  ? 12.750 -23.729 25.736  1.00 15.18 ? 64  HIS A N   1 
ATOM   510  C CA  . HIS A 1 64  ? 11.332 -23.876 26.064  1.00 15.34 ? 64  HIS A CA  1 
ATOM   511  C C   . HIS A 1 64  ? 10.643 -22.586 26.518  1.00 15.59 ? 64  HIS A C   1 
ATOM   512  O O   . HIS A 1 64  ? 9.414  -22.564 26.635  1.00 16.33 ? 64  HIS A O   1 
ATOM   513  C CB  . HIS A 1 64  ? 11.090 -25.001 27.087  1.00 16.13 ? 64  HIS A CB  1 
ATOM   514  C CG  . HIS A 1 64  ? 11.550 -24.698 28.481  1.00 17.26 ? 64  HIS A CG  1 
ATOM   515  N ND1 . HIS A 1 64  ? 12.805 -25.063 28.912  1.00 18.51 ? 64  HIS A ND1 1 
ATOM   516  C CD2 . HIS A 1 64  ? 10.890 -24.109 29.506  1.00 18.35 ? 64  HIS A CD2 1 
ATOM   517  C CE1 . HIS A 1 64  ? 12.887 -24.663 30.171  1.00 18.91 ? 64  HIS A CE1 1 
ATOM   518  N NE2 . HIS A 1 64  ? 11.768 -24.069 30.566  1.00 19.00 ? 64  HIS A NE2 1 
ATOM   519  N N   . ASN A 1 65  ? 11.413 -21.525 26.808  1.00 14.89 ? 65  ASN A N   1 
ATOM   520  C CA  . ASN A 1 65  ? 10.825 -20.244 27.197  1.00 15.45 ? 65  ASN A CA  1 
ATOM   521  C C   . ASN A 1 65  ? 10.364 -19.437 25.979  1.00 15.62 ? 65  ASN A C   1 
ATOM   522  O O   . ASN A 1 65  ? 9.615  -18.487 26.144  1.00 16.44 ? 65  ASN A O   1 
ATOM   523  C CB  . ASN A 1 65  ? 11.814 -19.399 27.993  1.00 16.32 ? 65  ASN A CB  1 
ATOM   524  C CG  . ASN A 1 65  ? 12.130 -19.936 29.354  1.00 20.06 ? 65  ASN A CG  1 
ATOM   525  O OD1 . ASN A 1 65  ? 13.288 -19.972 29.757  1.00 21.53 ? 65  ASN A OD1 1 
ATOM   526  N ND2 . ASN A 1 65  ? 11.113 -20.354 30.094  1.00 20.32 ? 65  ASN A ND2 1 
ATOM   527  N N   . PHE A 1 66  ? 10.834 -19.782 24.766  1.00 14.81 ? 66  PHE A N   1 
ATOM   528  C CA  . PHE A 1 66  ? 10.445 -19.072 23.556  1.00 14.55 ? 66  PHE A CA  1 
ATOM   529  C C   . PHE A 1 66  ? 9.285  -19.790 22.901  1.00 15.70 ? 66  PHE A C   1 
ATOM   530  O O   . PHE A 1 66  ? 9.473  -20.833 22.284  1.00 17.06 ? 66  PHE A O   1 
ATOM   531  C CB  . PHE A 1 66  ? 11.624 -18.973 22.581  1.00 13.81 ? 66  PHE A CB  1 
ATOM   532  C CG  . PHE A 1 66  ? 12.755 -18.158 23.140  1.00 14.30 ? 66  PHE A CG  1 
ATOM   533  C CD1 . PHE A 1 66  ? 12.739 -16.779 23.058  1.00 15.07 ? 66  PHE A CD1 1 
ATOM   534  C CD2 . PHE A 1 66  ? 13.840 -18.771 23.734  1.00 14.97 ? 66  PHE A CD2 1 
ATOM   535  C CE1 . PHE A 1 66  ? 13.791 -16.027 23.574  1.00 15.66 ? 66  PHE A CE1 1 
ATOM   536  C CE2 . PHE A 1 66  ? 14.884 -18.017 24.257  1.00 15.64 ? 66  PHE A CE2 1 
ATOM   537  C CZ  . PHE A 1 66  ? 14.840 -16.648 24.190  1.00 15.18 ? 66  PHE A CZ  1 
ATOM   538  N N   . LEU A 1 67  ? 8.095  -19.249 23.059  1.00 14.73 ? 67  LEU A N   1 
ATOM   539  C CA  . LEU A 1 67  ? 6.890  -19.851 22.496  1.00 15.02 ? 67  LEU A CA  1 
ATOM   540  C C   . LEU A 1 67  ? 6.660  -19.315 21.087  1.00 14.82 ? 67  LEU A C   1 
ATOM   541  O O   . LEU A 1 67  ? 6.407  -18.125 20.903  1.00 14.57 ? 67  LEU A O   1 
ATOM   542  C CB  . LEU A 1 67  ? 5.687  -19.563 23.389  1.00 16.22 ? 67  LEU A CB  1 
ATOM   543  C CG  . LEU A 1 67  ? 5.825  -20.012 24.845  1.00 19.15 ? 67  LEU A CG  1 
ATOM   544  C CD1 . LEU A 1 67  ? 4.603  -19.600 25.664  1.00 20.19 ? 67  LEU A CD1 1 
ATOM   545  C CD2 . LEU A 1 67  ? 6.082  -21.512 24.947  1.00 20.70 ? 67  LEU A CD2 1 
ATOM   546  N N   . VAL A 1 68  ? 6.797  -20.185 20.094  1.00 13.69 ? 68  VAL A N   1 
ATOM   547  C CA  . VAL A 1 68  ? 6.672  -19.779 18.702  1.00 13.84 ? 68  VAL A CA  1 
ATOM   548  C C   . VAL A 1 68  ? 5.478  -20.455 18.106  1.00 14.57 ? 68  VAL A C   1 
ATOM   549  O O   . VAL A 1 68  ? 5.380  -21.671 18.188  1.00 14.93 ? 68  VAL A O   1 
ATOM   550  C CB  . VAL A 1 68  ? 7.958  -20.136 17.936  1.00 14.82 ? 68  VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 68  ? 7.847  -19.711 16.467  1.00 14.89 ? 68  VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 68  ? 9.173  -19.485 18.597  1.00 15.58 ? 68  VAL A CG2 1 
ATOM   553  N N   . GLN A 1 69  ? 4.540  -19.672 17.571  1.00 14.79 ? 69  GLN A N   1 
ATOM   554  C CA  . GLN A 1 69  ? 3.320  -20.238 17.038  1.00 16.19 ? 69  GLN A CA  1 
ATOM   555  C C   . GLN A 1 69  ? 3.083  -19.685 15.636  1.00 17.21 ? 69  GLN A C   1 
ATOM   556  O O   . GLN A 1 69  ? 3.122  -18.475 15.425  1.00 16.72 ? 69  GLN A O   1 
ATOM   557  C CB  . GLN A 1 69  ? 2.170  -19.888 17.999  1.00 18.04 ? 69  GLN A CB  1 
ATOM   558  C CG  . GLN A 1 69  ? 0.888  -20.656 17.771  1.00 21.51 ? 69  GLN A CG  1 
ATOM   559  C CD  . GLN A 1 69  ? -0.161 -20.174 18.731  1.00 25.03 ? 69  GLN A CD  1 
ATOM   560  O OE1 . GLN A 1 69  ? 0.106  -19.927 19.909  1.00 25.84 ? 69  GLN A OE1 1 
ATOM   561  N NE2 . GLN A 1 69  ? -1.385 -20.021 18.241  1.00 26.21 ? 69  GLN A NE2 1 
ATOM   562  N N   . ALA A 1 70  ? 2.875  -20.594 14.677  1.00 19.00 ? 70  ALA A N   1 
ATOM   563  C CA  . ALA A 1 70  ? 2.620  -20.293 13.267  1.00 20.96 ? 70  ALA A CA  1 
ATOM   564  C C   . ALA A 1 70  ? 1.139  -20.600 13.043  1.00 23.17 ? 70  ALA A C   1 
ATOM   565  O O   . ALA A 1 70  ? 0.751  -21.762 13.002  1.00 23.52 ? 70  ALA A O   1 
ATOM   566  C CB  . ALA A 1 70  ? 3.471  -21.204 12.398  1.00 20.97 ? 70  ALA A CB  1 
ATOM   567  N N   . GLY A 1 71  ? 0.297  -19.573 13.046  1.00 24.68 ? 71  GLY A N   1 
ATOM   568  C CA  . GLY A 1 71  ? -1.148 -19.764 12.969  1.00 25.82 ? 71  GLY A CA  1 
ATOM   569  C C   . GLY A 1 71  ? -1.586 -20.403 14.272  1.00 26.30 ? 71  GLY A C   1 
ATOM   570  O O   . GLY A 1 71  ? -1.283 -19.875 15.340  1.00 27.29 ? 71  GLY A O   1 
ATOM   571  N N   A ASN A 1 72  ? -2.203 -21.577 14.195  0.50 25.88 ? 72  ASN A N   1 
ATOM   572  N N   B ASN A 1 72  ? -2.232 -21.574 14.208  0.50 26.13 ? 72  ASN A N   1 
ATOM   573  C CA  A ASN A 1 72  ? -2.607 -22.309 15.390  0.50 25.81 ? 72  ASN A CA  1 
ATOM   574  C CA  B ASN A 1 72  ? -2.637 -22.282 15.426  0.50 26.29 ? 72  ASN A CA  1 
ATOM   575  C C   A ASN A 1 72  ? -1.585 -23.402 15.775  0.50 25.30 ? 72  ASN A C   1 
ATOM   576  C C   B ASN A 1 72  ? -1.713 -23.458 15.794  0.50 25.45 ? 72  ASN A C   1 
ATOM   577  O O   A ASN A 1 72  ? -1.765 -24.044 16.810  0.50 25.73 ? 72  ASN A O   1 
ATOM   578  O O   B ASN A 1 72  ? -2.036 -24.222 16.705  0.50 25.81 ? 72  ASN A O   1 
ATOM   579  C CB  A ASN A 1 72  ? -3.990 -22.935 15.174  0.50 27.13 ? 72  ASN A CB  1 
ATOM   580  C CB  B ASN A 1 72  ? -4.102 -22.729 15.351  0.50 28.37 ? 72  ASN A CB  1 
ATOM   581  C CG  A ASN A 1 72  ? -4.706 -23.325 16.447  0.50 29.97 ? 72  ASN A CG  1 
ATOM   582  C CG  B ASN A 1 72  ? -4.444 -23.658 14.208  0.50 32.49 ? 72  ASN A CG  1 
ATOM   583  O OD1 A ASN A 1 72  ? -4.849 -22.526 17.378  0.50 30.90 ? 72  ASN A OD1 1 
ATOM   584  O OD1 B ASN A 1 72  ? -3.749 -24.647 13.927  0.50 34.05 ? 72  ASN A OD1 1 
ATOM   585  N ND2 A ASN A 1 72  ? -5.171 -24.566 16.514  0.50 30.55 ? 72  ASN A ND2 1 
ATOM   586  N ND2 B ASN A 1 72  ? -5.547 -23.372 13.532  0.50 33.10 ? 72  ASN A ND2 1 
ATOM   587  N N   A VAL A 1 73  ? -0.530 -23.633 14.956  0.75 24.08 ? 73  VAL A N   1 
ATOM   588  N N   B VAL A 1 73  ? -0.584 -23.618 15.080  0.25 23.95 ? 73  VAL A N   1 
ATOM   589  C CA  A VAL A 1 73  ? 0.414  -24.705 15.245  0.75 23.44 ? 73  VAL A CA  1 
ATOM   590  C CA  B VAL A 1 73  ? 0.344  -24.718 15.304  0.25 22.97 ? 73  VAL A CA  1 
ATOM   591  C C   A VAL A 1 73  ? 1.668  -24.214 15.976  0.75 21.47 ? 73  VAL A C   1 
ATOM   592  C C   B VAL A 1 73  ? 1.640  -24.244 15.966  0.25 21.72 ? 73  VAL A C   1 
ATOM   593  O O   A VAL A 1 73  ? 2.283  -23.222 15.597  0.75 20.54 ? 73  VAL A O   1 
ATOM   594  O O   B VAL A 1 73  ? 2.279  -23.304 15.502  0.25 21.51 ? 73  VAL A O   1 
ATOM   595  C CB  A VAL A 1 73  ? 0.763  -25.565 14.001  0.75 24.81 ? 73  VAL A CB  1 
ATOM   596  C CB  B VAL A 1 73  ? 0.577  -25.518 13.997  0.25 23.51 ? 73  VAL A CB  1 
ATOM   597  C CG1 A VAL A 1 73  ? 1.636  -24.807 13.009  0.75 25.84 ? 73  VAL A CG1 1 
ATOM   598  C CG1 B VAL A 1 73  ? 1.798  -26.431 14.097  0.25 24.00 ? 73  VAL A CG1 1 
ATOM   599  C CG2 A VAL A 1 73  ? 1.436  -26.868 14.414  0.75 25.38 ? 73  VAL A CG2 1 
ATOM   600  C CG2 B VAL A 1 73  ? -0.667 -26.320 13.638  0.25 23.85 ? 73  VAL A CG2 1 
ATOM   601  N N   . GLN A 1 74  ? 2.014  -24.909 17.059  1.00 20.75 ? 74  GLN A N   1 
ATOM   602  C CA  . GLN A 1 74  ? 3.186  -24.589 17.836  1.00 19.17 ? 74  GLN A CA  1 
ATOM   603  C C   . GLN A 1 74  ? 4.454  -25.134 17.203  1.00 18.22 ? 74  GLN A C   1 
ATOM   604  O O   . GLN A 1 74  ? 4.478  -26.264 16.693  1.00 18.47 ? 74  GLN A O   1 
ATOM   605  C CB  . GLN A 1 74  ? 3.034  -25.162 19.243  1.00 19.18 ? 74  GLN A CB  1 
ATOM   606  C CG  . GLN A 1 74  ? 3.779  -24.366 20.307  1.00 19.39 ? 74  GLN A CG  1 
ATOM   607  C CD  . GLN A 1 74  ? 3.183  -23.013 20.563  1.00 21.32 ? 74  GLN A CD  1 
ATOM   608  O OE1 . GLN A 1 74  ? 2.013  -22.747 20.265  1.00 21.97 ? 74  GLN A OE1 1 
ATOM   609  N NE2 . GLN A 1 74  ? 3.972  -22.133 21.159  1.00 21.51 ? 74  GLN A NE2 1 
ATOM   610  N N   . LEU A 1 75  ? 5.519  -24.334 17.242  1.00 17.05 ? 75  LEU A N   1 
ATOM   611  C CA  . LEU A 1 75  ? 6.809  -24.770 16.729  1.00 17.04 ? 75  LEU A CA  1 
ATOM   612  C C   . LEU A 1 75  ? 7.735  -25.145 17.865  1.00 16.56 ? 75  LEU A C   1 
ATOM   613  O O   . LEU A 1 75  ? 7.725  -24.505 18.912  1.00 17.40 ? 75  LEU A O   1 
ATOM   614  C CB  . LEU A 1 75  ? 7.454  -23.702 15.837  1.00 17.69 ? 75  LEU A CB  1 
ATOM   615  C CG  . LEU A 1 75  ? 6.621  -23.233 14.636  1.00 19.89 ? 75  LEU A CG  1 
ATOM   616  C CD1 . LEU A 1 75  ? 7.402  -22.256 13.792  1.00 20.45 ? 75  LEU A CD1 1 
ATOM   617  C CD2 . LEU A 1 75  ? 6.150  -24.405 13.778  1.00 21.66 ? 75  LEU A CD2 1 
ATOM   618  N N   . ARG A 1 76  ? 8.516  -26.197 17.669  1.00 14.98 ? 76  ARG A N   1 
ATOM   619  C CA  . ARG A 1 76  ? 9.440  -26.670 18.686  1.00 14.65 ? 76  ARG A CA  1 
ATOM   620  C C   . ARG A 1 76  ? 10.784 -25.974 18.535  1.00 15.18 ? 76  ARG A C   1 
ATOM   621  O O   . ARG A 1 76  ? 11.405 -26.099 17.487  1.00 16.02 ? 76  ARG A O   1 
ATOM   622  C CB  . ARG A 1 76  ? 9.611  -28.184 18.570  1.00 15.16 ? 76  ARG A CB  1 
ATOM   623  C CG  . ARG A 1 76  ? 10.429 -28.788 19.702  1.00 15.73 ? 76  ARG A CG  1 
ATOM   624  C CD  . ARG A 1 76  ? 10.493 -30.311 19.588  1.00 16.39 ? 76  ARG A CD  1 
ATOM   625  N NE  . ARG A 1 76  ? 9.152  -30.898 19.628  1.00 17.45 ? 76  ARG A NE  1 
ATOM   626  C CZ  . ARG A 1 76  ? 8.486  -31.179 20.744  1.00 18.47 ? 76  ARG A CZ  1 
ATOM   627  N NH1 . ARG A 1 76  ? 9.049  -30.980 21.932  1.00 17.24 ? 76  ARG A NH1 1 
ATOM   628  N NH2 . ARG A 1 76  ? 7.256  -31.675 20.681  1.00 18.11 ? 76  ARG A NH2 1 
ATOM   629  N N   . VAL A 1 77  ? 11.234 -25.254 19.574  1.00 14.60 ? 77  VAL A N   1 
ATOM   630  C CA  . VAL A 1 77  ? 12.504 -24.530 19.581  1.00 14.79 ? 77  VAL A CA  1 
ATOM   631  C C   . VAL A 1 77  ? 13.634 -25.433 20.060  1.00 15.27 ? 77  VAL A C   1 
ATOM   632  O O   . VAL A 1 77  ? 13.610 -25.910 21.200  1.00 15.58 ? 77  VAL A O   1 
ATOM   633  C CB  . VAL A 1 77  ? 12.396 -23.241 20.417  1.00 14.63 ? 77  VAL A CB  1 
ATOM   634  C CG1 . VAL A 1 77  ? 13.738 -22.496 20.457  1.00 15.23 ? 77  VAL A CG1 1 
ATOM   635  C CG2 . VAL A 1 77  ? 11.286 -22.353 19.859  1.00 15.19 ? 77  VAL A CG2 1 
ATOM   636  N N   . ILE A 1 78  ? 14.606 -25.704 19.183  1.00 14.95 ? 78  ILE A N   1 
ATOM   637  C CA  . ILE A 1 78  ? 15.726 -26.579 19.519  1.00 15.44 ? 78  ILE A CA  1 
ATOM   638  C C   . ILE A 1 78  ? 17.072 -25.865 19.681  1.00 15.44 ? 78  ILE A C   1 
ATOM   639  O O   . ILE A 1 78  ? 18.089 -26.513 19.933  1.00 16.12 ? 78  ILE A O   1 
ATOM   640  C CB  . ILE A 1 78  ? 15.821 -27.724 18.493  1.00 16.42 ? 78  ILE A CB  1 
ATOM   641  C CG1 . ILE A 1 78  ? 16.122 -27.179 17.085  1.00 17.67 ? 78  ILE A CG1 1 
ATOM   642  C CG2 . ILE A 1 78  ? 14.532 -28.525 18.490  1.00 16.90 ? 78  ILE A CG2 1 
ATOM   643  C CD1 . ILE A 1 78  ? 16.430 -28.295 16.044  1.00 18.94 ? 78  ILE A CD1 1 
ATOM   644  N N   . GLY A 1 79  ? 17.071 -24.547 19.607  1.00 15.03 ? 79  GLY A N   1 
ATOM   645  C CA  . GLY A 1 79  ? 18.273 -23.758 19.811  1.00 15.04 ? 79  GLY A CA  1 
ATOM   646  C C   . GLY A 1 79  ? 17.946 -22.286 19.759  1.00 15.10 ? 79  GLY A C   1 
ATOM   647  O O   . GLY A 1 79  ? 16.938 -21.896 19.168  1.00 14.94 ? 79  GLY A O   1 
ATOM   648  N N   . HIS A 1 80  ? 18.773 -21.465 20.388  1.00 14.85 ? 80  HIS A N   1 
ATOM   649  C CA  . HIS A 1 80  ? 18.582 -20.020 20.321  1.00 14.66 ? 80  HIS A CA  1 
ATOM   650  C C   . HIS A 1 80  ? 19.904 -19.333 20.423  1.00 15.30 ? 80  HIS A C   1 
ATOM   651  O O   . HIS A 1 80  ? 20.814 -19.802 21.123  1.00 15.86 ? 80  HIS A O   1 
ATOM   652  C CB  . HIS A 1 80  ? 17.588 -19.490 21.366  1.00 14.91 ? 80  HIS A CB  1 
ATOM   653  C CG  . HIS A 1 80  ? 18.070 -19.617 22.771  1.00 16.66 ? 80  HIS A CG  1 
ATOM   654  N ND1 . HIS A 1 80  ? 17.910 -20.787 23.482  1.00 17.48 ? 80  HIS A ND1 1 
ATOM   655  C CD2 . HIS A 1 80  ? 18.705 -18.716 23.556  1.00 17.84 ? 80  HIS A CD2 1 
ATOM   656  C CE1 . HIS A 1 80  ? 18.440 -20.563 24.674  1.00 18.30 ? 80  HIS A CE1 1 
ATOM   657  N NE2 . HIS A 1 80  ? 18.929 -19.326 24.760  1.00 18.47 ? 80  HIS A NE2 1 
ATOM   658  N N   . SER A 1 81  ? 20.031 -18.237 19.705  1.00 14.84 ? 81  SER A N   1 
ATOM   659  C CA  . SER A 1 81  ? 21.265 -17.465 19.755  1.00 14.86 ? 81  SER A CA  1 
ATOM   660  C C   . SER A 1 81  ? 20.972 -16.018 19.462  1.00 14.66 ? 81  SER A C   1 
ATOM   661  O O   . SER A 1 81  ? 19.970 -15.697 18.822  1.00 15.19 ? 81  SER A O   1 
ATOM   662  C CB  . SER A 1 81  ? 22.291 -18.011 18.768  1.00 16.73 ? 81  SER A CB  1 
ATOM   663  O OG  . SER A 1 81  ? 21.809 -17.919 17.441  1.00 20.31 ? 81  SER A OG  1 
ATOM   664  N N   A MET A 1 82  ? 21.828 -15.125 19.951  0.50 14.30 ? 82  MET A N   1 
ATOM   665  N N   B MET A 1 82  ? 21.839 -15.141 19.938  0.50 14.04 ? 82  MET A N   1 
ATOM   666  C CA  A MET A 1 82  ? 21.664 -13.700 19.723  0.50 14.74 ? 82  MET A CA  1 
ATOM   667  C CA  B MET A 1 82  ? 21.699 -13.721 19.712  0.50 14.21 ? 82  MET A CA  1 
ATOM   668  C C   A MET A 1 82  ? 22.712 -13.224 18.723  0.50 15.23 ? 82  MET A C   1 
ATOM   669  C C   B MET A 1 82  ? 22.718 -13.294 18.664  0.50 14.88 ? 82  MET A C   1 
ATOM   670  O O   A MET A 1 82  ? 23.905 -13.470 18.919  0.50 16.17 ? 82  MET A O   1 
ATOM   671  O O   B MET A 1 82  ? 23.890 -13.665 18.753  0.50 15.61 ? 82  MET A O   1 
ATOM   672  C CB  A MET A 1 82  ? 21.801 -12.929 21.041  0.50 15.23 ? 82  MET A CB  1 
ATOM   673  C CB  B MET A 1 82  ? 21.937 -12.966 21.026  0.50 14.18 ? 82  MET A CB  1 
ATOM   674  C CG  A MET A 1 82  ? 21.614 -11.442 20.874  0.50 17.47 ? 82  MET A CG  1 
ATOM   675  C CG  B MET A 1 82  ? 21.759 -11.474 20.898  0.50 15.64 ? 82  MET A CG  1 
ATOM   676  S SD  A MET A 1 82  ? 21.828 -10.548 22.424  0.50 20.86 ? 82  MET A SD  1 
ATOM   677  S SD  B MET A 1 82  ? 21.374 -10.707 22.484  0.50 15.97 ? 82  MET A SD  1 
ATOM   678  C CE  A MET A 1 82  ? 20.402 -11.108 23.302  0.50 20.46 ? 82  MET A CE  1 
ATOM   679  C CE  B MET A 1 82  ? 22.877 -11.090 23.413  0.50 12.42 ? 82  MET A CE  1 
ATOM   680  N N   . GLN A 1 83  ? 22.270 -12.561 17.647  1.00 15.01 ? 83  GLN A N   1 
ATOM   681  C CA  . GLN A 1 83  ? 23.164 -12.017 16.627  1.00 15.04 ? 83  GLN A CA  1 
ATOM   682  C C   . GLN A 1 83  ? 22.849 -10.536 16.608  1.00 13.84 ? 83  GLN A C   1 
ATOM   683  O O   . GLN A 1 83  ? 21.761 -10.157 16.187  1.00 14.15 ? 83  GLN A O   1 
ATOM   684  C CB  . GLN A 1 83  ? 22.915 -12.619 15.247  1.00 17.78 ? 83  GLN A CB  1 
ATOM   685  C CG  . GLN A 1 83  ? 23.871 -12.027 14.206  1.00 22.38 ? 83  GLN A CG  1 
ATOM   686  C CD  . GLN A 1 83  ? 23.630 -12.527 12.802  1.00 27.19 ? 83  GLN A CD  1 
ATOM   687  O OE1 . GLN A 1 83  ? 22.667 -13.246 12.515  1.00 27.58 ? 83  GLN A OE1 1 
ATOM   688  N NE2 . GLN A 1 83  ? 24.504 -12.142 11.883  1.00 28.65 ? 83  GLN A NE2 1 
ATOM   689  N N   . ASN A 1 84  ? 23.741 -9.705  17.152  1.00 13.13 ? 84  ASN A N   1 
ATOM   690  C CA  . ASN A 1 84  ? 23.516 -8.266  17.264  1.00 12.86 ? 84  ASN A CA  1 
ATOM   691  C C   . ASN A 1 84  ? 22.187 -8.003  18.043  1.00 12.30 ? 84  ASN A C   1 
ATOM   692  O O   . ASN A 1 84  ? 22.073 -8.505  19.170  1.00 13.18 ? 84  ASN A O   1 
ATOM   693  C CB  . ASN A 1 84  ? 23.643 -7.595  15.893  1.00 13.60 ? 84  ASN A CB  1 
ATOM   694  C CG  . ASN A 1 84  ? 24.979 -7.902  15.287  1.00 16.97 ? 84  ASN A CG  1 
ATOM   695  O OD1 . ASN A 1 84  ? 26.030 -7.659  15.897  1.00 18.65 ? 84  ASN A OD1 1 
ATOM   696  N ND2 . ASN A 1 84  ? 24.965 -8.478  14.103  1.00 17.35 ? 84  ASN A ND2 1 
ATOM   697  N N   . CYS A 1 85  ? 21.183 -7.327  17.448  1.00 11.65 ? 85  CYS A N   1 
ATOM   698  C CA  . CYS A 1 85  ? 19.935 -7.077  18.150  1.00 11.74 ? 85  CYS A CA  1 
ATOM   699  C C   . CYS A 1 85  ? 18.805 -8.021  17.785  1.00 11.93 ? 85  CYS A C   1 
ATOM   700  O O   . CYS A 1 85  ? 17.658 -7.743  18.135  1.00 12.25 ? 85  CYS A O   1 
ATOM   701  C CB  . CYS A 1 85  ? 19.518 -5.626  17.998  1.00 12.25 ? 85  CYS A CB  1 
ATOM   702  S SG  . CYS A 1 85  ? 20.771 -4.475  18.599  1.00 14.49 ? 85  CYS A SG  1 
ATOM   703  N N   . VAL A 1 86  ? 19.106 -9.142  17.124  1.00 11.92 ? 86  VAL A N   1 
ATOM   704  C CA  A VAL A 1 86  ? 18.063 -10.123 16.816  0.80 12.69 ? 86  VAL A CA  1 
ATOM   705  C CA  B VAL A 1 86  ? 18.084 -10.108 16.770  0.20 12.62 ? 86  VAL A CA  1 
ATOM   706  C C   . VAL A 1 86  ? 18.368 -11.466 17.447  1.00 13.31 ? 86  VAL A C   1 
ATOM   707  O O   . VAL A 1 86  ? 19.522 -11.792 17.744  1.00 13.89 ? 86  VAL A O   1 
ATOM   708  C CB  A VAL A 1 86  ? 17.715 -10.290 15.315  0.80 13.96 ? 86  VAL A CB  1 
ATOM   709  C CB  B VAL A 1 86  ? 17.964 -10.163 15.216  0.20 13.40 ? 86  VAL A CB  1 
ATOM   710  C CG1 A VAL A 1 86  ? 17.232 -8.980  14.704  0.80 14.98 ? 86  VAL A CG1 1 
ATOM   711  C CG1 B VAL A 1 86  ? 17.427 -11.492 14.704  0.20 13.91 ? 86  VAL A CG1 1 
ATOM   712  C CG2 A VAL A 1 86  ? 18.874 -10.884 14.538  0.80 14.71 ? 86  VAL A CG2 1 
ATOM   713  C CG2 B VAL A 1 86  ? 17.115 -9.007  14.699  0.20 14.01 ? 86  VAL A CG2 1 
ATOM   714  N N   . LEU A 1 87  ? 17.311 -12.214 17.743  1.00 12.95 ? 87  LEU A N   1 
ATOM   715  C CA  . LEU A 1 87  ? 17.437 -13.555 18.248  1.00 13.45 ? 87  LEU A CA  1 
ATOM   716  C C   . LEU A 1 87  ? 17.087 -14.460 17.060  1.00 12.81 ? 87  LEU A C   1 
ATOM   717  O O   . LEU A 1 87  ? 16.214 -14.148 16.232  1.00 12.84 ? 87  LEU A O   1 
ATOM   718  C CB  . LEU A 1 87  ? 16.456 -13.848 19.385  1.00 14.73 ? 87  LEU A CB  1 
ATOM   719  C CG  . LEU A 1 87  ? 16.676 -13.104 20.677  1.00 17.21 ? 87  LEU A CG  1 
ATOM   720  C CD1 . LEU A 1 87  ? 15.555 -13.409 21.659  1.00 17.72 ? 87  LEU A CD1 1 
ATOM   721  C CD2 . LEU A 1 87  ? 18.026 -13.431 21.279  1.00 19.12 ? 87  LEU A CD2 1 
ATOM   722  N N   . LYS A 1 88  ? 17.808 -15.569 16.962  1.00 12.70 ? 88  LYS A N   1 
ATOM   723  C CA  . LYS A 1 88  ? 17.600 -16.588 15.957  1.00 12.67 ? 88  LYS A CA  1 
ATOM   724  C C   . LYS A 1 88  ? 17.188 -17.806 16.736  1.00 12.90 ? 88  LYS A C   1 
ATOM   725  O O   . LYS A 1 88  ? 17.975 -18.321 17.525  1.00 13.84 ? 88  LYS A O   1 
ATOM   726  C CB  . LYS A 1 88  ? 18.899 -16.875 15.190  1.00 13.93 ? 88  LYS A CB  1 
ATOM   727  C CG  . LYS A 1 88  ? 19.258 -15.755 14.219  1.00 17.96 ? 88  LYS A CG  1 
ATOM   728  C CD  . LYS A 1 88  ? 20.490 -16.070 13.376  1.00 22.34 ? 88  LYS A CD  1 
ATOM   729  C CE  . LYS A 1 88  ? 21.738 -16.137 14.208  1.00 26.94 ? 88  LYS A CE  1 
ATOM   730  N NZ  . LYS A 1 88  ? 22.952 -15.999 13.363  1.00 28.94 ? 88  LYS A NZ  1 
ATOM   731  N N   . LEU A 1 89  ? 15.950 -18.220 16.574  1.00 12.44 ? 89  LEU A N   1 
ATOM   732  C CA  . LEU A 1 89  ? 15.403 -19.373 17.256  1.00 12.59 ? 89  LEU A CA  1 
ATOM   733  C C   . LEU A 1 89  ? 15.367 -20.511 16.264  1.00 12.94 ? 89  LEU A C   1 
ATOM   734  O O   . LEU A 1 89  ? 14.620 -20.459 15.287  1.00 13.54 ? 89  LEU A O   1 
ATOM   735  C CB  . LEU A 1 89  ? 13.982 -19.063 17.753  1.00 12.75 ? 89  LEU A CB  1 
ATOM   736  C CG  . LEU A 1 89  ? 13.831 -17.772 18.569  1.00 13.26 ? 89  LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 89  ? 12.360 -17.539 18.932  1.00 14.00 ? 89  LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 89  ? 14.701 -17.814 19.810  1.00 14.04 ? 89  LEU A CD2 1 
ATOM   739  N N   . LYS A 1 90  ? 16.203 -21.522 16.472  1.00 12.58 ? 90  LYS A N   1 
ATOM   740  C CA  . LYS A 1 90  ? 16.232 -22.674 15.595  1.00 13.10 ? 90  LYS A CA  1 
ATOM   741  C C   . LYS A 1 90  ? 15.051 -23.539 15.962  1.00 13.08 ? 90  LYS A C   1 
ATOM   742  O O   . LYS A 1 90  ? 14.830 -23.805 17.137  1.00 13.52 ? 90  LYS A O   1 
ATOM   743  C CB  . LYS A 1 90  ? 17.536 -23.458 15.769  1.00 15.25 ? 90  LYS A CB  1 
ATOM   744  C CG  . LYS A 1 90  ? 17.687 -24.519 14.697  1.00 19.98 ? 90  LYS A CG  1 
ATOM   745  C CD  . LYS A 1 90  ? 18.937 -25.357 14.862  1.00 26.70 ? 90  LYS A CD  1 
ATOM   746  C CE  . LYS A 1 90  ? 18.950 -26.460 13.827  1.00 31.95 ? 90  LYS A CE  1 
ATOM   747  N NZ  . LYS A 1 90  ? 20.250 -27.184 13.784  1.00 34.61 ? 90  LYS A NZ  1 
ATOM   748  N N   . VAL A 1 91  ? 14.239 -23.892 14.982  1.00 13.01 ? 91  VAL A N   1 
ATOM   749  C CA  . VAL A 1 91  ? 13.080 -24.738 15.204  1.00 13.59 ? 91  VAL A CA  1 
ATOM   750  C C   . VAL A 1 91  ? 13.290 -26.080 14.510  1.00 13.94 ? 91  VAL A C   1 
ATOM   751  O O   . VAL A 1 91  ? 14.153 -26.193 13.635  1.00 14.24 ? 91  VAL A O   1 
ATOM   752  C CB  . VAL A 1 91  ? 11.760 -24.046 14.810  1.00 13.54 ? 91  VAL A CB  1 
ATOM   753  C CG1 . VAL A 1 91  ? 11.470 -22.870 15.748  1.00 13.86 ? 91  VAL A CG1 1 
ATOM   754  C CG2 . VAL A 1 91  ? 11.792 -23.576 13.358  1.00 13.61 ? 91  VAL A CG2 1 
ATOM   755  N N   . ASP A 1 92  ? 12.510 -27.098 14.887  1.00 14.52 ? 92  ASP A N   1 
ATOM   756  C CA  . ASP A 1 92  ? 12.713 -28.432 14.308  1.00 15.39 ? 92  ASP A CA  1 
ATOM   757  C C   . ASP A 1 92  ? 12.040 -28.640 12.940  1.00 16.15 ? 92  ASP A C   1 
ATOM   758  O O   . ASP A 1 92  ? 12.151 -29.724 12.366  1.00 17.58 ? 92  ASP A O   1 
ATOM   759  C CB  . ASP A 1 92  ? 12.298 -29.535 15.300  1.00 16.92 ? 92  ASP A CB  1 
ATOM   760  C CG  . ASP A 1 92  ? 10.803 -29.782 15.434  1.00 21.75 ? 92  ASP A CG  1 
ATOM   761  O OD1 . ASP A 1 92  ? 10.011 -28.950 14.931  1.00 21.92 ? 92  ASP A OD1 1 
ATOM   762  O OD2 . ASP A 1 92  ? 10.423 -30.804 16.052  1.00 24.89 ? 92  ASP A OD2 1 
ATOM   763  N N   . THR A 1 93  ? 11.319 -27.629 12.442  1.00 15.46 ? 93  THR A N   1 
ATOM   764  C CA  . THR A 1 93  ? 10.601 -27.740 11.184  1.00 15.98 ? 93  THR A CA  1 
ATOM   765  C C   . THR A 1 93  ? 10.936 -26.576 10.273  1.00 15.60 ? 93  THR A C   1 
ATOM   766  O O   . THR A 1 93  ? 10.857 -25.414 10.682  1.00 15.87 ? 93  THR A O   1 
ATOM   767  C CB  . THR A 1 93  ? 9.091  -27.772 11.474  1.00 18.02 ? 93  THR A CB  1 
ATOM   768  O OG1 . THR A 1 93  ? 8.807  -28.909 12.282  1.00 19.65 ? 93  THR A OG1 1 
ATOM   769  C CG2 . THR A 1 93  ? 8.231  -27.818 10.214  1.00 18.56 ? 93  THR A CG2 1 
ATOM   770  N N   . ALA A 1 94  ? 11.321 -26.885 9.036   1.00 15.11 ? 94  ALA A N   1 
ATOM   771  C CA  . ALA A 1 94  ? 11.580 -25.846 8.051   1.00 15.27 ? 94  ALA A CA  1 
ATOM   772  C C   . ALA A 1 94  ? 10.227 -25.287 7.629   1.00 14.37 ? 94  ALA A C   1 
ATOM   773  O O   . ALA A 1 94  ? 9.266  -26.049 7.472   1.00 14.40 ? 94  ALA A O   1 
ATOM   774  C CB  . ALA A 1 94  ? 12.280 -26.436 6.838   1.00 15.99 ? 94  ALA A CB  1 
ATOM   775  N N   . ASN A 1 95  ? 10.133 -23.953 7.445   1.00 13.14 ? 95  ASN A N   1 
ATOM   776  C CA  . ASN A 1 95  ? 8.883  -23.366 6.989   1.00 12.83 ? 95  ASN A CA  1 
ATOM   777  C C   . ASN A 1 95  ? 8.594  -23.845 5.583   1.00 14.44 ? 95  ASN A C   1 
ATOM   778  O O   . ASN A 1 95  ? 9.373  -23.554 4.678   1.00 15.01 ? 95  ASN A O   1 
ATOM   779  C CB  . ASN A 1 95  ? 8.974  -21.836 7.015   1.00 11.70 ? 95  ASN A CB  1 
ATOM   780  C CG  . ASN A 1 95  ? 7.671  -21.166 6.662   1.00 12.68 ? 95  ASN A CG  1 
ATOM   781  O OD1 . ASN A 1 95  ? 6.665  -21.818 6.312   1.00 12.65 ? 95  ASN A OD1 1 
ATOM   782  N ND2 . ASN A 1 95  ? 7.654  -19.854 6.755   1.00 13.33 ? 95  ASN A ND2 1 
ATOM   783  N N   . PRO A 1 96  ? 7.498  -24.592 5.381   1.00 15.09 ? 96  PRO A N   1 
ATOM   784  C CA  . PRO A 1 96  ? 7.194  -25.071 4.022   1.00 15.91 ? 96  PRO A CA  1 
ATOM   785  C C   . PRO A 1 96  ? 6.869  -23.969 3.029   1.00 16.81 ? 96  PRO A C   1 
ATOM   786  O O   . PRO A 1 96  ? 6.955  -24.177 1.819   1.00 18.67 ? 96  PRO A O   1 
ATOM   787  C CB  . PRO A 1 96  ? 6.007  -26.020 4.234   1.00 16.85 ? 96  PRO A CB  1 
ATOM   788  C CG  . PRO A 1 96  ? 5.365  -25.537 5.452   1.00 17.21 ? 96  PRO A CG  1 
ATOM   789  C CD  . PRO A 1 96  ? 6.454  -24.999 6.343   1.00 15.27 ? 96  PRO A CD  1 
ATOM   790  N N   A LYS A 1 97  ? 6.497  -22.792 3.536   0.50 16.18 ? 97  LYS A N   1 
ATOM   791  N N   B LYS A 1 97  ? 6.498  -22.794 3.526   0.50 15.87 ? 97  LYS A N   1 
ATOM   792  C CA  A LYS A 1 97  ? 6.197  -21.633 2.715   0.50 16.25 ? 97  LYS A CA  1 
ATOM   793  C CA  B LYS A 1 97  ? 6.186  -21.657 2.678   0.50 15.62 ? 97  LYS A CA  1 
ATOM   794  C C   A LYS A 1 97  ? 7.398  -20.685 2.599   0.50 16.20 ? 97  LYS A C   1 
ATOM   795  C C   B LYS A 1 97  ? 7.397  -20.733 2.479   0.50 15.87 ? 97  LYS A C   1 
ATOM   796  O O   A LYS A 1 97  ? 7.196  -19.507 2.312   0.50 16.30 ? 97  LYS A O   1 
ATOM   797  O O   B LYS A 1 97  ? 7.210  -19.616 1.997   0.50 15.98 ? 97  LYS A O   1 
ATOM   798  C CB  A LYS A 1 97  ? 4.997  -20.876 3.290   0.50 17.71 ? 97  LYS A CB  1 
ATOM   799  C CB  B LYS A 1 97  ? 5.028  -20.859 3.292   0.50 16.13 ? 97  LYS A CB  1 
ATOM   800  C CG  A LYS A 1 97  ? 3.707  -21.681 3.258   0.50 21.36 ? 97  LYS A CG  1 
ATOM   801  C CG  B LYS A 1 97  ? 3.787  -21.702 3.563   0.50 18.13 ? 97  LYS A CG  1 
ATOM   802  C CD  A LYS A 1 97  ? 2.514  -20.817 3.626   0.50 25.21 ? 97  LYS A CD  1 
ATOM   803  C CD  B LYS A 1 97  ? 2.659  -20.874 4.168   0.50 20.47 ? 97  LYS A CD  1 
ATOM   804  C CE  A LYS A 1 97  ? 1.247  -21.628 3.735   0.50 28.84 ? 97  LYS A CE  1 
ATOM   805  C CE  B LYS A 1 97  ? 1.497  -21.748 4.586   0.50 23.28 ? 97  LYS A CE  1 
ATOM   806  N NZ  A LYS A 1 97  ? 1.311  -22.583 4.872   0.50 31.00 ? 97  LYS A NZ  1 
ATOM   807  N NZ  B LYS A 1 97  ? 0.450  -20.970 5.306   0.50 24.86 ? 97  LYS A NZ  1 
ATOM   808  N N   . THR A 1 98  ? 8.635  -21.173 2.838   1.00 15.64 ? 98  THR A N   1 
ATOM   809  C CA  . THR A 1 98  ? 9.819  -20.315 2.707   1.00 15.75 ? 98  THR A CA  1 
ATOM   810  C C   . THR A 1 98  ? 10.036 -19.955 1.256   1.00 17.30 ? 98  THR A C   1 
ATOM   811  O O   . THR A 1 98  ? 10.207 -20.836 0.419   1.00 18.89 ? 98  THR A O   1 
ATOM   812  C CB  . THR A 1 98  ? 11.098 -20.973 3.223   1.00 15.79 ? 98  THR A CB  1 
ATOM   813  O OG1 . THR A 1 98  ? 10.913 -21.371 4.576   1.00 14.95 ? 98  THR A OG1 1 
ATOM   814  C CG2 . THR A 1 98  ? 12.291 -20.020 3.161   1.00 16.33 ? 98  THR A CG2 1 
ATOM   815  N N   . PRO A 1 99  ? 9.971  -18.662 0.943   1.00 17.35 ? 99  PRO A N   1 
ATOM   816  C CA  . PRO A 1 99  ? 10.220 -18.251 -0.440  1.00 17.36 ? 99  PRO A CA  1 
ATOM   817  C C   . PRO A 1 99  ? 11.719 -18.183 -0.682  1.00 17.89 ? 99  PRO A C   1 
ATOM   818  O O   . PRO A 1 99  ? 12.539 -18.301 0.246   1.00 18.10 ? 99  PRO A O   1 
ATOM   819  C CB  . PRO A 1 99  ? 9.616  -16.844 -0.472  1.00 17.74 ? 99  PRO A CB  1 
ATOM   820  C CG  . PRO A 1 99  ? 9.944  -16.303 0.908   1.00 18.63 ? 99  PRO A CG  1 
ATOM   821  C CD  . PRO A 1 99  ? 9.806  -17.493 1.835   1.00 16.90 ? 99  PRO A CD  1 
ATOM   822  N N   . LYS A 1 100 ? 12.124 -17.929 -1.950  1.00 18.01 ? 100 LYS A N   1 
ATOM   823  C CA  . LYS A 1 100 ? 13.535 -17.625 -2.236  1.00 17.86 ? 100 LYS A CA  1 
ATOM   824  C C   . LYS A 1 100 ? 13.794 -16.281 -1.557  1.00 16.86 ? 100 LYS A C   1 
ATOM   825  O O   . LYS A 1 100 ? 12.915 -15.410 -1.609  1.00 17.12 ? 100 LYS A O   1 
ATOM   826  C CB  . LYS A 1 100 ? 13.781 -17.459 -3.727  1.00 20.30 ? 100 LYS A CB  1 
ATOM   827  C CG  . LYS A 1 100 ? 13.806 -18.781 -4.460  1.00 25.36 ? 100 LYS A CG  1 
ATOM   828  C CD  . LYS A 1 100 ? 13.957 -18.552 -5.942  1.00 30.62 ? 100 LYS A CD  1 
ATOM   829  C CE  . LYS A 1 100 ? 13.870 -19.846 -6.690  1.00 34.80 ? 100 LYS A CE  1 
ATOM   830  N NZ  . LYS A 1 100 ? 13.923 -19.616 -8.154  1.00 37.87 ? 100 LYS A NZ  1 
ATOM   831  N N   . TYR A 1 101 ? 14.880 -16.181 -0.805  1.00 16.48 ? 101 TYR A N   1 
ATOM   832  C CA  . TYR A 1 101 ? 15.128 -14.952 -0.066  1.00 16.55 ? 101 TYR A CA  1 
ATOM   833  C C   . TYR A 1 101 ? 16.581 -14.602 0.070   1.00 17.45 ? 101 TYR A C   1 
ATOM   834  O O   . TYR A 1 101 ? 17.465 -15.432 -0.117  1.00 18.21 ? 101 TYR A O   1 
ATOM   835  C CB  . TYR A 1 101 ? 14.446 -14.990 1.329   1.00 15.77 ? 101 TYR A CB  1 
ATOM   836  C CG  . TYR A 1 101 ? 15.146 -15.902 2.316   1.00 15.73 ? 101 TYR A CG  1 
ATOM   837  C CD1 . TYR A 1 101 ? 14.886 -17.261 2.336   1.00 15.94 ? 101 TYR A CD1 1 
ATOM   838  C CD2 . TYR A 1 101 ? 16.069 -15.402 3.228   1.00 16.30 ? 101 TYR A CD2 1 
ATOM   839  C CE1 . TYR A 1 101 ? 15.528 -18.107 3.223   1.00 17.03 ? 101 TYR A CE1 1 
ATOM   840  C CE2 . TYR A 1 101 ? 16.721 -16.242 4.126   1.00 16.87 ? 101 TYR A CE2 1 
ATOM   841  C CZ  . TYR A 1 101 ? 16.426 -17.592 4.137   1.00 18.00 ? 101 TYR A CZ  1 
ATOM   842  O OH  . TYR A 1 101 ? 17.050 -18.451 5.005   1.00 19.69 ? 101 TYR A OH  1 
ATOM   843  N N   . LYS A 1 102 ? 16.813 -13.342 0.419   1.00 17.07 ? 102 LYS A N   1 
ATOM   844  C CA  . LYS A 1 102 ? 18.117 -12.782 0.702   1.00 17.29 ? 102 LYS A CA  1 
ATOM   845  C C   . LYS A 1 102 ? 17.931 -11.785 1.830   1.00 17.01 ? 102 LYS A C   1 
ATOM   846  O O   . LYS A 1 102 ? 16.841 -11.228 2.005   1.00 17.36 ? 102 LYS A O   1 
ATOM   847  C CB  . LYS A 1 102 ? 18.666 -12.018 -0.521  1.00 19.57 ? 102 LYS A CB  1 
ATOM   848  C CG  . LYS A 1 102 ? 19.172 -12.891 -1.652  1.00 25.57 ? 102 LYS A CG  1 
ATOM   849  C CD  . LYS A 1 102 ? 19.560 -12.019 -2.838  1.00 30.51 ? 102 LYS A CD  1 
ATOM   850  C CE  . LYS A 1 102 ? 19.942 -12.850 -4.039  1.00 34.71 ? 102 LYS A CE  1 
ATOM   851  N NZ  . LYS A 1 102 ? 20.222 -11.998 -5.223  1.00 37.67 ? 102 LYS A NZ  1 
ATOM   852  N N   . PHE A 1 103 ? 18.997 -11.533 2.573   1.00 16.41 ? 103 PHE A N   1 
ATOM   853  C CA  . PHE A 1 103 ? 18.994 -10.484 3.584   1.00 16.22 ? 103 PHE A CA  1 
ATOM   854  C C   . PHE A 1 103 ? 19.847 -9.382  3.004   1.00 16.98 ? 103 PHE A C   1 
ATOM   855  O O   . PHE A 1 103 ? 20.994 -9.634  2.601   1.00 18.29 ? 103 PHE A O   1 
ATOM   856  C CB  . PHE A 1 103 ? 19.613 -10.957 4.902   1.00 15.69 ? 103 PHE A CB  1 
ATOM   857  C CG  . PHE A 1 103 ? 18.795 -11.943 5.708   1.00 15.24 ? 103 PHE A CG  1 
ATOM   858  C CD1 . PHE A 1 103 ? 17.445 -12.132 5.446   1.00 15.08 ? 103 PHE A CD1 1 
ATOM   859  C CD2 . PHE A 1 103 ? 19.352 -12.609 6.784   1.00 15.50 ? 103 PHE A CD2 1 
ATOM   860  C CE1 . PHE A 1 103 ? 16.690 -13.014 6.217   1.00 15.35 ? 103 PHE A CE1 1 
ATOM   861  C CE2 . PHE A 1 103 ? 18.597 -13.493 7.545   1.00 15.76 ? 103 PHE A CE2 1 
ATOM   862  C CZ  . PHE A 1 103 ? 17.267 -13.671 7.274   1.00 15.43 ? 103 PHE A CZ  1 
ATOM   863  N N   . VAL A 1 104 ? 19.279 -8.182  2.889   1.00 16.37 ? 104 VAL A N   1 
ATOM   864  C CA  . VAL A 1 104 ? 20.033 -7.044  2.376   1.00 17.50 ? 104 VAL A CA  1 
ATOM   865  C C   . VAL A 1 104 ? 19.980 -5.887  3.348   1.00 17.45 ? 104 VAL A C   1 
ATOM   866  O O   . VAL A 1 104 ? 18.977 -5.694  4.025   1.00 18.38 ? 104 VAL A O   1 
ATOM   867  C CB  . VAL A 1 104 ? 19.568 -6.605  0.972   1.00 19.51 ? 104 VAL A CB  1 
ATOM   868  C CG1 . VAL A 1 104 ? 19.602 -7.772  -0.011  1.00 20.51 ? 104 VAL A CG1 1 
ATOM   869  C CG2 . VAL A 1 104 ? 18.188 -5.980  1.030   1.00 21.03 ? 104 VAL A CG2 1 
ATOM   870  N N   . ARG A 1 105 ? 21.056 -5.114  3.423   1.00 15.80 ? 105 ARG A N   1 
ATOM   871  C CA  . ARG A 1 105 ? 21.085 -3.918  4.245   1.00 15.43 ? 105 ARG A CA  1 
ATOM   872  C C   . ARG A 1 105 ? 20.948 -2.766  3.265   1.00 16.07 ? 105 ARG A C   1 
ATOM   873  O O   . ARG A 1 105 ? 21.814 -2.585  2.403   1.00 16.45 ? 105 ARG A O   1 
ATOM   874  C CB  . ARG A 1 105 ? 22.391 -3.812  5.050   1.00 15.61 ? 105 ARG A CB  1 
ATOM   875  C CG  . ARG A 1 105 ? 22.422 -2.551  5.896   1.00 16.10 ? 105 ARG A CG  1 
ATOM   876  C CD  . ARG A 1 105 ? 23.630 -2.518  6.815   1.00 16.65 ? 105 ARG A CD  1 
ATOM   877  N NE  . ARG A 1 105 ? 23.615 -1.344  7.690   1.00 16.81 ? 105 ARG A NE  1 
ATOM   878  C CZ  . ARG A 1 105 ? 22.963 -1.276  8.847   1.00 17.76 ? 105 ARG A CZ  1 
ATOM   879  N NH1 . ARG A 1 105 ? 22.257 -2.313  9.283   1.00 15.50 ? 105 ARG A NH1 1 
ATOM   880  N NH2 . ARG A 1 105 ? 23.019 -0.174  9.580   1.00 16.68 ? 105 ARG A NH2 1 
ATOM   881  N N   . ILE A 1 106 ? 19.843 -2.020  3.359   1.00 16.34 ? 106 ILE A N   1 
ATOM   882  C CA  . ILE A 1 106 ? 19.591 -0.952  2.403   1.00 17.54 ? 106 ILE A CA  1 
ATOM   883  C C   . ILE A 1 106 ? 20.273 0.351   2.775   1.00 18.38 ? 106 ILE A C   1 
ATOM   884  O O   . ILE A 1 106 ? 20.686 0.548   3.914   1.00 18.30 ? 106 ILE A O   1 
ATOM   885  C CB  . ILE A 1 106 ? 18.079 -0.754  2.154   1.00 18.39 ? 106 ILE A CB  1 
ATOM   886  C CG1 . ILE A 1 106 ? 17.349 -0.412  3.456   1.00 18.46 ? 106 ILE A CG1 1 
ATOM   887  C CG2 . ILE A 1 106 ? 17.482 -1.941  1.420   1.00 19.36 ? 106 ILE A CG2 1 
ATOM   888  C CD1 . ILE A 1 106 ? 15.965 0.091   3.254   1.00 19.73 ? 106 ILE A CD1 1 
ATOM   889  N N   . GLN A 1 107 ? 20.428 1.226   1.782   1.00 19.23 ? 107 GLN A N   1 
ATOM   890  C CA  . GLN A 1 107 ? 20.997 2.545   1.964   1.00 19.73 ? 107 GLN A CA  1 
ATOM   891  C C   . GLN A 1 107 ? 19.865 3.537   2.207   1.00 18.47 ? 107 GLN A C   1 
ATOM   892  O O   . GLN A 1 107 ? 18.742 3.340   1.721   1.00 17.38 ? 107 GLN A O   1 
ATOM   893  C CB  . GLN A 1 107 ? 21.745 2.950   0.676   1.00 23.23 ? 107 GLN A CB  1 
ATOM   894  C CG  . GLN A 1 107 ? 22.876 1.997   0.305   1.00 29.27 ? 107 GLN A CG  1 
ATOM   895  C CD  . GLN A 1 107 ? 24.026 2.049   1.285   1.00 36.32 ? 107 GLN A CD  1 
ATOM   896  O OE1 . GLN A 1 107 ? 24.225 3.026   2.019   1.00 38.70 ? 107 GLN A OE1 1 
ATOM   897  N NE2 . GLN A 1 107 ? 24.829 0.996   1.300   1.00 37.97 ? 107 GLN A NE2 1 
ATOM   898  N N   . PRO A 1 108 ? 20.146 4.681   2.862   1.00 18.14 ? 108 PRO A N   1 
ATOM   899  C CA  . PRO A 1 108 ? 19.108 5.716   2.987   1.00 17.93 ? 108 PRO A CA  1 
ATOM   900  C C   . PRO A 1 108 ? 18.660 6.165   1.590   1.00 17.22 ? 108 PRO A C   1 
ATOM   901  O O   . PRO A 1 108 ? 19.462 6.189   0.647   1.00 17.68 ? 108 PRO A O   1 
ATOM   902  C CB  . PRO A 1 108 ? 19.811 6.845   3.755   1.00 19.73 ? 108 PRO A CB  1 
ATOM   903  C CG  . PRO A 1 108 ? 21.269 6.568   3.594   1.00 21.30 ? 108 PRO A CG  1 
ATOM   904  C CD  . PRO A 1 108 ? 21.423 5.100   3.467   1.00 19.01 ? 108 PRO A CD  1 
ATOM   905  N N   . GLY A 1 109 ? 17.382 6.434   1.449   1.00 15.99 ? 109 GLY A N   1 
ATOM   906  C CA  . GLY A 1 109 ? 16.807 6.791   0.158   1.00 16.21 ? 109 GLY A CA  1 
ATOM   907  C C   . GLY A 1 109 ? 16.074 5.638   -0.506  1.00 16.96 ? 109 GLY A C   1 
ATOM   908  O O   . GLY A 1 109 ? 15.191 5.862   -1.338  1.00 18.41 ? 109 GLY A O   1 
ATOM   909  N N   A GLN A 1 110 ? 16.422 4.397   -0.138  0.75 16.76 ? 110 GLN A N   1 
ATOM   910  N N   B GLN A 1 110 ? 16.445 4.390   -0.161  0.25 16.16 ? 110 GLN A N   1 
ATOM   911  C CA  A GLN A 1 110 ? 15.768 3.237   -0.714  0.75 16.95 ? 110 GLN A CA  1 
ATOM   912  C CA  B GLN A 1 110 ? 15.829 3.187   -0.717  0.25 15.84 ? 110 GLN A CA  1 
ATOM   913  C C   A GLN A 1 110 ? 14.440 2.952   -0.068  0.75 16.11 ? 110 GLN A C   1 
ATOM   914  C C   B GLN A 1 110 ? 14.470 2.926   -0.075  0.25 15.71 ? 110 GLN A C   1 
ATOM   915  O O   A GLN A 1 110 ? 14.240 3.191   1.125   0.75 16.11 ? 110 GLN A O   1 
ATOM   916  O O   B GLN A 1 110 ? 14.293 3.143   1.123   0.25 15.80 ? 110 GLN A O   1 
ATOM   917  C CB  A GLN A 1 110 ? 16.693 2.020   -0.709  0.75 19.14 ? 110 GLN A CB  1 
ATOM   918  C CB  B GLN A 1 110 ? 16.764 1.974   -0.537  0.25 16.49 ? 110 GLN A CB  1 
ATOM   919  C CG  A GLN A 1 110 ? 17.940 2.248   -1.555  0.75 23.45 ? 110 GLN A CG  1 
ATOM   920  C CG  B GLN A 1 110 ? 16.218 0.644   -1.057  0.25 17.81 ? 110 GLN A CG  1 
ATOM   921  C CD  A GLN A 1 110 ? 17.625 2.582   -2.992  0.75 30.28 ? 110 GLN A CD  1 
ATOM   922  C CD  B GLN A 1 110 ? 15.922 0.672   -2.535  0.25 19.23 ? 110 GLN A CD  1 
ATOM   923  O OE1 A GLN A 1 110 ? 17.015 1.792   -3.727  0.75 33.04 ? 110 GLN A OE1 1 
ATOM   924  O OE1 B GLN A 1 110 ? 16.709 1.161   -3.348  0.25 20.49 ? 110 GLN A OE1 1 
ATOM   925  N NE2 A GLN A 1 110 ? 18.015 3.774   -3.418  0.75 30.91 ? 110 GLN A NE2 1 
ATOM   926  N NE2 B GLN A 1 110 ? 14.760 0.153   -2.910  0.25 17.17 ? 110 GLN A NE2 1 
ATOM   927  N N   . THR A 1 111 ? 13.508 2.467   -0.876  1.00 15.42 ? 111 THR A N   1 
ATOM   928  C CA  . THR A 1 111 ? 12.177 2.177   -0.420  1.00 15.01 ? 111 THR A CA  1 
ATOM   929  C C   . THR A 1 111 ? 12.007 0.676   -0.190  1.00 14.44 ? 111 THR A C   1 
ATOM   930  O O   . THR A 1 111 ? 12.800 -0.137  -0.654  1.00 15.56 ? 111 THR A O   1 
ATOM   931  C CB  . THR A 1 111 ? 11.189 2.708   -1.461  1.00 15.57 ? 111 THR A CB  1 
ATOM   932  O OG1 . THR A 1 111 ? 11.488 2.051   -2.697  1.00 16.40 ? 111 THR A OG1 1 
ATOM   933  C CG2 . THR A 1 111 ? 11.297 4.211   -1.623  1.00 15.53 ? 111 THR A CG2 1 
ATOM   934  N N   . PHE A 1 112 ? 10.950 0.319   0.518   1.00 13.51 ? 112 PHE A N   1 
ATOM   935  C CA  . PHE A 1 112 ? 10.598 -1.063  0.784   1.00 13.06 ? 112 PHE A CA  1 
ATOM   936  C C   . PHE A 1 112 ? 9.173  -1.129  1.275   1.00 12.87 ? 112 PHE A C   1 
ATOM   937  O O   . PHE A 1 112 ? 8.617  -0.121  1.728   1.00 12.86 ? 112 PHE A O   1 
ATOM   938  C CB  . PHE A 1 112 ? 11.550 -1.690  1.813   1.00 13.30 ? 112 PHE A CB  1 
ATOM   939  C CG  . PHE A 1 112 ? 11.648 -0.996  3.149   1.00 13.25 ? 112 PHE A CG  1 
ATOM   940  C CD1 . PHE A 1 112 ? 12.527 0.058   3.340   1.00 14.26 ? 112 PHE A CD1 1 
ATOM   941  C CD2 . PHE A 1 112 ? 10.881 -1.409  4.218   1.00 13.58 ? 112 PHE A CD2 1 
ATOM   942  C CE1 . PHE A 1 112 ? 12.649 0.667   4.581   1.00 14.94 ? 112 PHE A CE1 1 
ATOM   943  C CE2 . PHE A 1 112 ? 11.024 -0.820  5.466   1.00 14.05 ? 112 PHE A CE2 1 
ATOM   944  C CZ  . PHE A 1 112 ? 11.895 0.226   5.637   1.00 14.59 ? 112 PHE A CZ  1 
ATOM   945  N N   . SER A 1 113 ? 8.584  -2.325  1.254   1.00 12.27 ? 113 SER A N   1 
ATOM   946  C CA  . SER A 1 113 ? 7.231  -2.520  1.754   1.00 12.47 ? 113 SER A CA  1 
ATOM   947  C C   . SER A 1 113 ? 7.324  -3.072  3.152   1.00 12.94 ? 113 SER A C   1 
ATOM   948  O O   . SER A 1 113 ? 8.199  -3.891  3.424   1.00 13.55 ? 113 SER A O   1 
ATOM   949  C CB  . SER A 1 113 ? 6.494  -3.535  0.894   1.00 13.09 ? 113 SER A CB  1 
ATOM   950  O OG  . SER A 1 113 ? 6.426  -3.026  -0.426  1.00 14.30 ? 113 SER A OG  1 
ATOM   951  N N   . VAL A 1 114 ? 6.388  -2.710  4.000   1.00 12.29 ? 114 VAL A N   1 
ATOM   952  C CA  . VAL A 1 114 ? 6.309  -3.243  5.354   1.00 12.81 ? 114 VAL A CA  1 
ATOM   953  C C   . VAL A 1 114 ? 5.016  -4.014  5.481   1.00 13.03 ? 114 VAL A C   1 
ATOM   954  O O   . VAL A 1 114 ? 3.956  -3.520  5.093   1.00 13.21 ? 114 VAL A O   1 
ATOM   955  C CB  . VAL A 1 114 ? 6.321  -2.096  6.393   1.00 12.98 ? 114 VAL A CB  1 
ATOM   956  C CG1 . VAL A 1 114 ? 5.995  -2.605  7.800   1.00 13.23 ? 114 VAL A CG1 1 
ATOM   957  C CG2 . VAL A 1 114 ? 7.642  -1.359  6.377   1.00 13.58 ? 114 VAL A CG2 1 
ATOM   958  N N   . LEU A 1 115 ? 5.084  -5.218  6.060   1.00 12.47 ? 115 LEU A N   1 
ATOM   959  C CA  . LEU A 1 115 ? 3.894  -5.974  6.346   1.00 12.54 ? 115 LEU A CA  1 
ATOM   960  C C   . LEU A 1 115 ? 3.703  -5.818  7.851   1.00 12.81 ? 115 LEU A C   1 
ATOM   961  O O   . LEU A 1 115 ? 4.403  -6.474  8.629   1.00 13.18 ? 115 LEU A O   1 
ATOM   962  C CB  . LEU A 1 115 ? 4.037  -7.458  5.964   1.00 12.90 ? 115 LEU A CB  1 
ATOM   963  C CG  . LEU A 1 115 ? 2.822  -8.307  6.284   1.00 14.50 ? 115 LEU A CG  1 
ATOM   964  C CD1 . LEU A 1 115 ? 1.620  -7.870  5.469   1.00 15.37 ? 115 LEU A CD1 1 
ATOM   965  C CD2 . LEU A 1 115 ? 3.100  -9.764  6.033   1.00 14.68 ? 115 LEU A CD2 1 
ATOM   966  N N   A ALA A 1 116 ? 2.831  -4.892  8.282   0.50 12.53 ? 116 ALA A N   1 
ATOM   967  N N   B ALA A 1 116 ? 2.781  -4.931  8.250   0.50 12.98 ? 116 ALA A N   1 
ATOM   968  C CA  A ALA A 1 116 ? 2.624  -4.675  9.718   0.50 13.17 ? 116 ALA A CA  1 
ATOM   969  C CA  B ALA A 1 116 ? 2.439  -4.683  9.648   0.50 14.18 ? 116 ALA A CA  1 
ATOM   970  C C   A ALA A 1 116 ? 1.810  -5.835  10.275  0.50 13.37 ? 116 ALA A C   1 
ATOM   971  C C   B ALA A 1 116 ? 1.816  -5.963  10.194  0.50 14.72 ? 116 ALA A C   1 
ATOM   972  O O   A ALA A 1 116 ? 0.739  -6.137  9.755   0.50 13.60 ? 116 ALA A O   1 
ATOM   973  O O   B ALA A 1 116 ? 0.984  -6.577  9.520   0.50 15.10 ? 116 ALA A O   1 
ATOM   974  C CB  A ALA A 1 116 ? 1.907  -3.354  9.963   0.50 13.83 ? 116 ALA A CB  1 
ATOM   975  C CB  B ALA A 1 116 ? 1.442  -3.535  9.736   0.50 14.78 ? 116 ALA A CB  1 
ATOM   976  N N   A CYS A 1 117 ? 2.327  -6.495  11.304  0.75 13.30 ? 117 CYS A N   1 
ATOM   977  N N   B CYS A 1 117 ? 2.247  -6.387  11.372  0.25 14.79 ? 117 CYS A N   1 
ATOM   978  C CA  A CYS A 1 117 ? 1.697  -7.643  11.954  0.75 13.87 ? 117 CYS A CA  1 
ATOM   979  C CA  B CYS A 1 117 ? 1.815  -7.651  11.942  0.25 15.40 ? 117 CYS A CA  1 
ATOM   980  C C   A CYS A 1 117 ? 1.506  -7.426  13.414  0.75 14.56 ? 117 CYS A C   1 
ATOM   981  C C   B CYS A 1 117 ? 1.597  -7.519  13.450  0.25 15.40 ? 117 CYS A C   1 
ATOM   982  O O   A CYS A 1 117 ? 2.265  -6.683  14.028  0.75 14.38 ? 117 CYS A O   1 
ATOM   983  O O   B CYS A 1 117 ? 2.357  -6.821  14.110  0.25 15.48 ? 117 CYS A O   1 
ATOM   984  C CB  A CYS A 1 117 ? 2.543  -8.892  11.752  0.75 14.43 ? 117 CYS A CB  1 
ATOM   985  C CB  B CYS A 1 117 ? 2.882  -8.701  11.636  0.25 16.62 ? 117 CYS A CB  1 
ATOM   986  S SG  A CYS A 1 117 ? 2.803  -9.323  10.034  0.75 14.59 ? 117 CYS A SG  1 
ATOM   987  S SG  B CYS A 1 117 ? 2.292  -10.412 11.656  0.25 20.52 ? 117 CYS A SG  1 
ATOM   988  N N   . TYR A 1 118 ? 0.570  -8.188  13.997  1.00 15.18 ? 118 TYR A N   1 
ATOM   989  C CA  . TYR A 1 118 ? 0.296  -8.220  15.447  1.00 16.61 ? 118 TYR A CA  1 
ATOM   990  C C   . TYR A 1 118 ? -0.002 -9.668  15.797  1.00 18.17 ? 118 TYR A C   1 
ATOM   991  O O   . TYR A 1 118 ? -0.763 -10.310 15.085  1.00 18.33 ? 118 TYR A O   1 
ATOM   992  C CB  . TYR A 1 118 ? -0.905 -7.330  15.835  1.00 17.19 ? 118 TYR A CB  1 
ATOM   993  C CG  . TYR A 1 118 ? -0.613 -5.889  15.531  1.00 17.88 ? 118 TYR A CG  1 
ATOM   994  C CD1 . TYR A 1 118 ? 0.120  -5.113  16.416  1.00 18.60 ? 118 TYR A CD1 1 
ATOM   995  C CD2 . TYR A 1 118 ? -0.904 -5.351  14.286  1.00 18.85 ? 118 TYR A CD2 1 
ATOM   996  C CE1 . TYR A 1 118 ? 0.471  -3.810  16.108  1.00 19.34 ? 118 TYR A CE1 1 
ATOM   997  C CE2 . TYR A 1 118 ? -0.509 -4.069  13.946  1.00 19.60 ? 118 TYR A CE2 1 
ATOM   998  C CZ  . TYR A 1 118 ? 0.167  -3.297  14.865  1.00 20.22 ? 118 TYR A CZ  1 
ATOM   999  O OH  . TYR A 1 118 ? 0.539  -2.027  14.526  1.00 21.79 ? 118 TYR A OH  1 
ATOM   1000 N N   . ASN A 1 119 ? 0.643  -10.210 16.842  1.00 18.87 ? 119 ASN A N   1 
ATOM   1001 C CA  . ASN A 1 119 ? 0.439  -11.600 17.254  1.00 20.10 ? 119 ASN A CA  1 
ATOM   1002 C C   . ASN A 1 119 ? 0.702  -12.594 16.117  1.00 19.55 ? 119 ASN A C   1 
ATOM   1003 O O   . ASN A 1 119 ? -0.008 -13.593 15.977  1.00 20.20 ? 119 ASN A O   1 
ATOM   1004 C CB  . ASN A 1 119 ? -0.981 -11.790 17.805  1.00 22.64 ? 119 ASN A CB  1 
ATOM   1005 C CG  . ASN A 1 119 ? -1.294 -10.896 18.970  1.00 27.97 ? 119 ASN A CG  1 
ATOM   1006 O OD1 . ASN A 1 119 ? -2.158 -10.021 18.891  1.00 30.85 ? 119 ASN A OD1 1 
ATOM   1007 N ND2 . ASN A 1 119 ? -0.591 -11.091 20.070  1.00 29.18 ? 119 ASN A ND2 1 
ATOM   1008 N N   . GLY A 1 120 ? 1.679  -12.285 15.272  1.00 18.20 ? 120 GLY A N   1 
ATOM   1009 C CA  . GLY A 1 120 ? 2.021  -13.141 14.143  1.00 17.98 ? 120 GLY A CA  1 
ATOM   1010 C C   . GLY A 1 120 ? 1.039  -13.089 12.987  1.00 18.05 ? 120 GLY A C   1 
ATOM   1011 O O   . GLY A 1 120 ? 1.168  -13.860 12.037  1.00 18.15 ? 120 GLY A O   1 
ATOM   1012 N N   . SER A 1 121 ? 0.031  -12.200 13.059  1.00 17.88 ? 121 SER A N   1 
ATOM   1013 C CA  . SER A 1 121 ? -0.988 -12.098 12.025  1.00 19.05 ? 121 SER A CA  1 
ATOM   1014 C C   . SER A 1 121 ? -0.884 -10.784 11.263  1.00 19.31 ? 121 SER A C   1 
ATOM   1015 O O   . SER A 1 121 ? -0.858 -9.709  11.855  1.00 18.83 ? 121 SER A O   1 
ATOM   1016 C CB  . SER A 1 121 ? -2.379 -12.227 12.637  1.00 21.46 ? 121 SER A CB  1 
ATOM   1017 O OG  . SER A 1 121 ? -2.553 -13.527 13.175  1.00 25.54 ? 121 SER A OG  1 
ATOM   1018 N N   . PRO A 1 122 ? -0.842 -10.855 9.929   1.00 20.18 ? 122 PRO A N   1 
ATOM   1019 C CA  . PRO A 1 122 ? -0.716 -9.623  9.136   1.00 20.36 ? 122 PRO A CA  1 
ATOM   1020 C C   . PRO A 1 122 ? -1.952 -8.725  9.210   1.00 20.01 ? 122 PRO A C   1 
ATOM   1021 O O   . PRO A 1 122 ? -3.095 -9.193  9.177   1.00 20.24 ? 122 PRO A O   1 
ATOM   1022 C CB  . PRO A 1 122 ? -0.453 -10.148 7.715   1.00 22.14 ? 122 PRO A CB  1 
ATOM   1023 C CG  . PRO A 1 122 ? 0.095  -11.574 7.925   1.00 22.93 ? 122 PRO A CG  1 
ATOM   1024 C CD  . PRO A 1 122 ? -0.761 -12.055 9.076   1.00 20.91 ? 122 PRO A CD  1 
ATOM   1025 N N   . SER A 1 123 ? -1.723 -7.421  9.339   1.00 19.28 ? 123 SER A N   1 
ATOM   1026 C CA  . SER A 1 123 ? -2.812 -6.455  9.398   1.00 19.98 ? 123 SER A CA  1 
ATOM   1027 C C   . SER A 1 123 ? -2.866 -5.587  8.166   1.00 19.22 ? 123 SER A C   1 
ATOM   1028 O O   . SER A 1 123 ? -3.958 -5.209  7.743   1.00 19.82 ? 123 SER A O   1 
ATOM   1029 C CB  . SER A 1 123 ? -2.716 -5.583  10.640  1.00 23.07 ? 123 SER A CB  1 
ATOM   1030 O OG  . SER A 1 123 ? -1.507 -4.852  10.632  1.00 27.68 ? 123 SER A OG  1 
ATOM   1031 N N   . GLY A 1 124 ? -1.705 -5.226  7.622   1.00 17.37 ? 124 GLY A N   1 
ATOM   1032 C CA  . GLY A 1 124 ? -1.677 -4.368  6.453   1.00 16.81 ? 124 GLY A CA  1 
ATOM   1033 C C   . GLY A 1 124 ? -0.319 -4.237  5.824   1.00 15.64 ? 124 GLY A C   1 
ATOM   1034 O O   . GLY A 1 124 ? 0.683  -4.635  6.408   1.00 14.83 ? 124 GLY A O   1 
ATOM   1035 N N   . VAL A 1 125 ? -0.281 -3.697  4.620   1.00 15.52 ? 125 VAL A N   1 
ATOM   1036 C CA  . VAL A 1 125 ? 0.955  -3.526  3.900   1.00 16.15 ? 125 VAL A CA  1 
ATOM   1037 C C   . VAL A 1 125 ? 1.037  -2.116  3.362   1.00 16.23 ? 125 VAL A C   1 
ATOM   1038 O O   . VAL A 1 125 ? 0.028  -1.552  2.933   1.00 16.69 ? 125 VAL A O   1 
ATOM   1039 C CB  . VAL A 1 125 ? 1.136  -4.627  2.825   1.00 18.52 ? 125 VAL A CB  1 
ATOM   1040 C CG1 . VAL A 1 125 ? 0.022  -4.589  1.791   1.00 20.02 ? 125 VAL A CG1 1 
ATOM   1041 C CG2 . VAL A 1 125 ? 2.511  -4.563  2.175   1.00 19.01 ? 125 VAL A CG2 1 
ATOM   1042 N N   . TYR A 1 126 ? 2.205  -1.514  3.481   1.00 16.20 ? 126 TYR A N   1 
ATOM   1043 C CA  . TYR A 1 126 ? 2.408  -0.148  3.015   1.00 16.17 ? 126 TYR A CA  1 
ATOM   1044 C C   . TYR A 1 126 ? 3.842  0.066   2.588   1.00 15.60 ? 126 TYR A C   1 
ATOM   1045 O O   . TYR A 1 126 ? 4.736  -0.688  2.960   1.00 15.94 ? 126 TYR A O   1 
ATOM   1046 C CB  . TYR A 1 126 ? 1.958  0.884   4.064   1.00 16.49 ? 126 TYR A CB  1 
ATOM   1047 C CG  . TYR A 1 126 ? 2.669  0.757   5.389   1.00 17.12 ? 126 TYR A CG  1 
ATOM   1048 C CD1 . TYR A 1 126 ? 3.901  1.356   5.601   1.00 17.77 ? 126 TYR A CD1 1 
ATOM   1049 C CD2 . TYR A 1 126 ? 2.115  0.027   6.430   1.00 18.46 ? 126 TYR A CD2 1 
ATOM   1050 C CE1 . TYR A 1 126 ? 4.560  1.241   6.817   1.00 18.59 ? 126 TYR A CE1 1 
ATOM   1051 C CE2 . TYR A 1 126 ? 2.758  -0.085  7.654   1.00 19.26 ? 126 TYR A CE2 1 
ATOM   1052 C CZ  . TYR A 1 126 ? 3.979  0.529   7.845   1.00 19.71 ? 126 TYR A CZ  1 
ATOM   1053 O OH  . TYR A 1 126 ? 4.608  0.427   9.064   1.00 22.38 ? 126 TYR A OH  1 
ATOM   1054 N N   A GLN A 1 127 ? 4.050  1.061   1.748   0.50 15.62 ? 127 GLN A N   1 
ATOM   1055 N N   B GLN A 1 127 ? 4.090  1.164   1.886   0.50 15.49 ? 127 GLN A N   1 
ATOM   1056 C CA  A GLN A 1 127 ? 5.336  1.360   1.175   0.50 15.80 ? 127 GLN A CA  1 
ATOM   1057 C CA  B GLN A 1 127 ? 5.413  1.506   1.423   0.50 15.72 ? 127 GLN A CA  1 
ATOM   1058 C C   A GLN A 1 127 ? 5.965  2.540   1.890   0.50 16.49 ? 127 GLN A C   1 
ATOM   1059 C C   B GLN A 1 127 ? 6.095  2.480   2.372   0.50 16.20 ? 127 GLN A C   1 
ATOM   1060 O O   A GLN A 1 127 ? 5.306  3.560   2.092   0.50 16.63 ? 127 GLN A O   1 
ATOM   1061 O O   B GLN A 1 127 ? 5.462  3.402   2.878   0.50 16.36 ? 127 GLN A O   1 
ATOM   1062 C CB  A GLN A 1 127 ? 5.117  1.674   -0.313  0.50 16.38 ? 127 GLN A CB  1 
ATOM   1063 C CB  B GLN A 1 127 ? 5.315  2.096   0.015   0.50 17.00 ? 127 GLN A CB  1 
ATOM   1064 C CG  A GLN A 1 127 ? 6.368  1.792   -1.131  0.50 18.09 ? 127 GLN A CG  1 
ATOM   1065 C CG  B GLN A 1 127 ? 6.631  2.112   -0.715  0.50 19.17 ? 127 GLN A CG  1 
ATOM   1066 C CD  A GLN A 1 127 ? 7.089  0.490   -1.349  0.50 18.85 ? 127 GLN A CD  1 
ATOM   1067 C CD  B GLN A 1 127 ? 7.033  0.761   -1.249  0.50 19.69 ? 127 GLN A CD  1 
ATOM   1068 O OE1 A GLN A 1 127 ? 6.666  -0.598  -0.912  0.50 18.45 ? 127 GLN A OE1 1 
ATOM   1069 O OE1 B GLN A 1 127 ? 6.501  -0.300  -0.868  0.50 20.09 ? 127 GLN A OE1 1 
ATOM   1070 N NE2 A GLN A 1 127 ? 8.210  0.583   -2.023  0.50 19.51 ? 127 GLN A NE2 1 
ATOM   1071 N NE2 B GLN A 1 127 ? 8.008  0.774   -2.125  0.50 19.03 ? 127 GLN A NE2 1 
ATOM   1072 N N   A CYS A 1 128 ? 7.225  2.400   2.294   0.50 16.47 ? 128 CYS A N   1 
ATOM   1073 N N   B CYS A 1 128 ? 7.382  2.261   2.606   0.50 16.43 ? 128 CYS A N   1 
ATOM   1074 C CA  A CYS A 1 128 ? 7.942  3.478   2.975   0.50 16.78 ? 128 CYS A CA  1 
ATOM   1075 C CA  B CYS A 1 128 ? 8.255  3.071   3.448   0.50 17.09 ? 128 CYS A CA  1 
ATOM   1076 C C   A CYS A 1 128 ? 9.416  3.592   2.486   0.50 16.85 ? 128 CYS A C   1 
ATOM   1077 C C   B CYS A 1 128 ? 9.557  3.356   2.718   0.50 17.04 ? 128 CYS A C   1 
ATOM   1078 O O   A CYS A 1 128 ? 9.746  3.008   1.463   0.50 16.70 ? 128 CYS A O   1 
ATOM   1079 O O   B CYS A 1 128 ? 9.936  2.632   1.810   0.50 16.87 ? 128 CYS A O   1 
ATOM   1080 C CB  A CYS A 1 128 ? 7.831  3.331   4.489   0.50 17.30 ? 128 CYS A CB  1 
ATOM   1081 C CB  B CYS A 1 128 ? 8.549  2.332   4.751   0.50 18.43 ? 128 CYS A CB  1 
ATOM   1082 S SG  A CYS A 1 128 ? 8.691  1.883   5.141   0.50 19.72 ? 128 CYS A SG  1 
ATOM   1083 S SG  B CYS A 1 128 ? 7.272  2.509   6.011   0.50 23.03 ? 128 CYS A SG  1 
ATOM   1084 N N   . ALA A 1 129 ? 10.286 4.364   3.171   1.00 17.09 ? 129 ALA A N   1 
ATOM   1085 C CA  . ALA A 1 129 ? 11.650 4.578   2.712   1.00 17.20 ? 129 ALA A CA  1 
ATOM   1086 C C   . ALA A 1 129 ? 12.538 4.679   3.922   1.00 16.36 ? 129 ALA A C   1 
ATOM   1087 O O   . ALA A 1 129 ? 12.115 5.142   4.987   1.00 17.23 ? 129 ALA A O   1 
ATOM   1088 C CB  . ALA A 1 129 ? 11.767 5.848   1.894   1.00 17.51 ? 129 ALA A CB  1 
ATOM   1089 N N   . MET A 1 130 ? 13.787 4.272   3.753   1.00 14.85 ? 130 MET A N   1 
ATOM   1090 C CA  . MET A 1 130 ? 14.793 4.474   4.787   1.00 14.43 ? 130 MET A CA  1 
ATOM   1091 C C   . MET A 1 130 ? 15.149 5.964   4.667   1.00 14.95 ? 130 MET A C   1 
ATOM   1092 O O   . MET A 1 130 ? 15.626 6.382   3.618   1.00 15.32 ? 130 MET A O   1 
ATOM   1093 C CB  . MET A 1 130 ? 16.023 3.600   4.511   1.00 14.88 ? 130 MET A CB  1 
ATOM   1094 C CG  . MET A 1 130 ? 17.144 3.773   5.526   1.00 16.66 ? 130 MET A CG  1 
ATOM   1095 S SD  . MET A 1 130 ? 16.663 3.502   7.255   1.00 17.10 ? 130 MET A SD  1 
ATOM   1096 C CE  . MET A 1 130 ? 15.931 1.868   7.146   1.00 15.89 ? 130 MET A CE  1 
ATOM   1097 N N   . ARG A 1 131 ? 14.805 6.763   5.672   1.00 14.67 ? 131 ARG A N   1 
ATOM   1098 C CA  . ARG A 1 131 ? 15.075 8.199   5.615   1.00 14.63 ? 131 ARG A CA  1 
ATOM   1099 C C   . ARG A 1 131 ? 16.579 8.470   5.700   1.00 15.11 ? 131 ARG A C   1 
ATOM   1100 O O   . ARG A 1 131 ? 17.321 7.663   6.261   1.00 15.31 ? 131 ARG A O   1 
ATOM   1101 C CB  . ARG A 1 131 ? 14.359 8.906   6.784   1.00 14.75 ? 131 ARG A CB  1 
ATOM   1102 C CG  . ARG A 1 131 ? 12.853 8.693   6.868   1.00 15.21 ? 131 ARG A CG  1 
ATOM   1103 C CD  . ARG A 1 131 ? 12.112 9.087   5.600   1.00 15.22 ? 131 ARG A CD  1 
ATOM   1104 N NE  . ARG A 1 131 ? 12.512 10.422  5.144   1.00 14.93 ? 131 ARG A NE  1 
ATOM   1105 C CZ  . ARG A 1 131 ? 12.205 10.925  3.951   1.00 14.97 ? 131 ARG A CZ  1 
ATOM   1106 N NH1 . ARG A 1 131 ? 11.460 10.230  3.101   1.00 14.04 ? 131 ARG A NH1 1 
ATOM   1107 N NH2 . ARG A 1 131 ? 12.629 12.136  3.606   1.00 14.38 ? 131 ARG A NH2 1 
ATOM   1108 N N   . PRO A 1 132 ? 17.057 9.636   5.226   1.00 15.38 ? 132 PRO A N   1 
ATOM   1109 C CA  . PRO A 1 132 ? 18.491 9.948   5.366   1.00 15.82 ? 132 PRO A CA  1 
ATOM   1110 C C   . PRO A 1 132 ? 18.982 9.985   6.832   1.00 16.21 ? 132 PRO A C   1 
ATOM   1111 O O   . PRO A 1 132 ? 20.180 9.803   7.070   1.00 17.50 ? 132 PRO A O   1 
ATOM   1112 C CB  . PRO A 1 132 ? 18.614 11.299  4.676   1.00 16.65 ? 132 PRO A CB  1 
ATOM   1113 C CG  . PRO A 1 132 ? 17.506 11.284  3.656   1.00 16.44 ? 132 PRO A CG  1 
ATOM   1114 C CD  . PRO A 1 132 ? 16.361 10.665  4.424   1.00 15.17 ? 132 PRO A CD  1 
ATOM   1115 N N   . ASN A 1 133 ? 18.087 10.206  7.816   1.00 14.91 ? 133 ASN A N   1 
ATOM   1116 C CA  . ASN A 1 133 ? 18.488 10.161  9.234   1.00 14.67 ? 133 ASN A CA  1 
ATOM   1117 C C   . ASN A 1 133 ? 18.338 8.731   9.835   1.00 14.76 ? 133 ASN A C   1 
ATOM   1118 O O   . ASN A 1 133 ? 18.393 8.562   11.050  1.00 14.97 ? 133 ASN A O   1 
ATOM   1119 C CB  . ASN A 1 133 ? 17.697 11.176  10.071  1.00 15.33 ? 133 ASN A CB  1 
ATOM   1120 C CG  . ASN A 1 133 ? 16.214 10.909  10.098  1.00 15.79 ? 133 ASN A CG  1 
ATOM   1121 O OD1 . ASN A 1 133 ? 15.728 9.883   9.605   1.00 15.06 ? 133 ASN A OD1 1 
ATOM   1122 N ND2 . ASN A 1 133 ? 15.454 11.831  10.669  1.00 16.61 ? 133 ASN A ND2 1 
ATOM   1123 N N   . PHE A 1 134 ? 18.104 7.718   8.982   1.00 14.43 ? 134 PHE A N   1 
ATOM   1124 C CA  . PHE A 1 134 ? 18.012 6.312   9.351   1.00 15.16 ? 134 PHE A CA  1 
ATOM   1125 C C   . PHE A 1 134 ? 16.803 5.931   10.198  1.00 15.02 ? 134 PHE A C   1 
ATOM   1126 O O   . PHE A 1 134 ? 16.792 4.877   10.839  1.00 15.26 ? 134 PHE A O   1 
ATOM   1127 C CB  . PHE A 1 134 ? 19.291 5.830   10.006  1.00 15.66 ? 134 PHE A CB  1 
ATOM   1128 C CG  . PHE A 1 134 ? 20.480 5.964   9.086   1.00 17.62 ? 134 PHE A CG  1 
ATOM   1129 C CD1 . PHE A 1 134 ? 20.732 5.016   8.114   1.00 19.31 ? 134 PHE A CD1 1 
ATOM   1130 C CD2 . PHE A 1 134 ? 21.369 7.012   9.226   1.00 19.06 ? 134 PHE A CD2 1 
ATOM   1131 C CE1 . PHE A 1 134 ? 21.843 5.131   7.281   1.00 20.53 ? 134 PHE A CE1 1 
ATOM   1132 C CE2 . PHE A 1 134 ? 22.476 7.120   8.396   1.00 20.32 ? 134 PHE A CE2 1 
ATOM   1133 C CZ  . PHE A 1 134 ? 22.710 6.176   7.437   1.00 20.35 ? 134 PHE A CZ  1 
ATOM   1134 N N   . THR A 1 135 ? 15.760 6.743   10.140  1.00 14.48 ? 135 THR A N   1 
ATOM   1135 C CA  . THR A 1 135 ? 14.475 6.389   10.724  1.00 14.62 ? 135 THR A CA  1 
ATOM   1136 C C   . THR A 1 135 ? 13.558 5.992   9.541   1.00 14.74 ? 135 THR A C   1 
ATOM   1137 O O   . THR A 1 135 ? 13.902 6.189   8.367   1.00 14.52 ? 135 THR A O   1 
ATOM   1138 C CB  . THR A 1 135 ? 13.860 7.611   11.436  1.00 15.36 ? 135 THR A CB  1 
ATOM   1139 O OG1 . THR A 1 135 ? 13.529 8.620   10.477  1.00 16.63 ? 135 THR A OG1 1 
ATOM   1140 C CG2 . THR A 1 135 ? 14.745 8.161   12.529  1.00 15.23 ? 135 THR A CG2 1 
ATOM   1141 N N   . ILE A 1 136 ? 12.395 5.430   9.852   1.00 14.48 ? 136 ILE A N   1 
ATOM   1142 C CA  . ILE A 1 136 ? 11.362 5.231   8.863   1.00 15.24 ? 136 ILE A CA  1 
ATOM   1143 C C   . ILE A 1 136 ? 10.103 5.840   9.436   1.00 15.66 ? 136 ILE A C   1 
ATOM   1144 O O   . ILE A 1 136 ? 9.949  5.927   10.654  1.00 15.42 ? 136 ILE A O   1 
ATOM   1145 C CB  . ILE A 1 136 ? 11.154 3.773   8.380   1.00 16.56 ? 136 ILE A CB  1 
ATOM   1146 C CG1 . ILE A 1 136 ? 10.532 2.890   9.459   1.00 17.44 ? 136 ILE A CG1 1 
ATOM   1147 C CG2 . ILE A 1 136 ? 12.448 3.165   7.826   1.00 17.63 ? 136 ILE A CG2 1 
ATOM   1148 C CD1 . ILE A 1 136 ? 9.987  1.590   8.900   1.00 18.35 ? 136 ILE A CD1 1 
ATOM   1149 N N   A LYS A 1 137 ? 9.196  6.293   8.569   0.50 16.39 ? 137 LYS A N   1 
ATOM   1150 N N   B LYS A 1 137 ? 9.209  6.274   8.558   0.50 16.47 ? 137 LYS A N   1 
ATOM   1151 C CA  A LYS A 1 137 ? 7.929  6.844   9.037   0.50 17.56 ? 137 LYS A CA  1 
ATOM   1152 C CA  B LYS A 1 137 ? 7.936  6.833   8.974   0.50 17.72 ? 137 LYS A CA  1 
ATOM   1153 C C   A LYS A 1 137 ? 6.887  5.782   8.750   0.50 17.91 ? 137 LYS A C   1 
ATOM   1154 C C   B LYS A 1 137 ? 6.920  5.736   8.717   0.50 17.94 ? 137 LYS A C   1 
ATOM   1155 O O   A LYS A 1 137 ? 6.343  5.738   7.658   0.50 18.13 ? 137 LYS A O   1 
ATOM   1156 O O   B LYS A 1 137 ? 6.413  5.631   7.608   0.50 18.10 ? 137 LYS A O   1 
ATOM   1157 C CB  A LYS A 1 137 ? 7.610  8.173   8.334   0.50 20.10 ? 137 LYS A CB  1 
ATOM   1158 C CB  B LYS A 1 137 ? 7.601  8.067   8.115   0.50 20.49 ? 137 LYS A CB  1 
ATOM   1159 C CG  A LYS A 1 137 ? 8.672  9.240   8.580   0.50 24.65 ? 137 LYS A CG  1 
ATOM   1160 C CG  B LYS A 1 137 ? 8.547  9.239   8.322   0.50 25.54 ? 137 LYS A CG  1 
ATOM   1161 C CD  A LYS A 1 137 ? 8.340  10.542  7.865   0.50 28.93 ? 137 LYS A CD  1 
ATOM   1162 C CD  B LYS A 1 137 ? 8.454  10.239  7.173   0.50 29.94 ? 137 LYS A CD  1 
ATOM   1163 C CE  A LYS A 1 137 ? 7.600  11.508  8.754   0.50 32.40 ? 137 LYS A CE  1 
ATOM   1164 C CE  B LYS A 1 137 ? 8.724  11.649  7.635   0.50 33.45 ? 137 LYS A CE  1 
ATOM   1165 N NZ  A LYS A 1 137 ? 8.483  12.051  9.819   0.50 34.48 ? 137 LYS A NZ  1 
ATOM   1166 N NZ  B LYS A 1 137 ? 9.352  12.475  6.565   0.50 34.98 ? 137 LYS A NZ  1 
ATOM   1167 N N   . GLY A 1 138 ? 6.673  4.891   9.709   1.00 17.84 ? 138 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 138 ? 5.745  3.780   9.550   1.00 18.27 ? 138 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 138 ? 4.449  3.921   10.307  1.00 17.75 ? 138 GLY A C   1 
ATOM   1170 O O   . GLY A 1 138 ? 4.066  5.022   10.697  1.00 18.35 ? 138 GLY A O   1 
ATOM   1171 N N   . SER A 1 139 ? 3.747  2.813   10.483  1.00 16.95 ? 139 SER A N   1 
ATOM   1172 C CA  . SER A 1 139 ? 2.511  2.779   11.237  1.00 17.34 ? 139 SER A CA  1 
ATOM   1173 C C   . SER A 1 139 ? 2.627  1.538   12.081  1.00 18.01 ? 139 SER A C   1 
ATOM   1174 O O   . SER A 1 139 ? 2.438  0.427   11.594  1.00 18.46 ? 139 SER A O   1 
ATOM   1175 C CB  . SER A 1 139 ? 1.310  2.717   10.300  1.00 18.70 ? 139 SER A CB  1 
ATOM   1176 O OG  . SER A 1 139 ? 0.131  2.477   11.049  1.00 23.01 ? 139 SER A OG  1 
ATOM   1177 N N   . PHE A 1 140 ? 3.090  1.719   13.311  1.00 17.22 ? 140 PHE A N   1 
ATOM   1178 C CA  . PHE A 1 140 ? 3.374  0.600   14.192  1.00 17.88 ? 140 PHE A CA  1 
ATOM   1179 C C   . PHE A 1 140 ? 2.824  0.838   15.576  1.00 20.15 ? 140 PHE A C   1 
ATOM   1180 O O   . PHE A 1 140 ? 3.184  1.818   16.205  1.00 21.50 ? 140 PHE A O   1 
ATOM   1181 C CB  . PHE A 1 140 ? 4.896  0.431   14.317  1.00 16.98 ? 140 PHE A CB  1 
ATOM   1182 C CG  . PHE A 1 140 ? 5.648  0.038   13.067  1.00 16.74 ? 140 PHE A CG  1 
ATOM   1183 C CD1 . PHE A 1 140 ? 5.592  -1.254  12.584  1.00 17.75 ? 140 PHE A CD1 1 
ATOM   1184 C CD2 . PHE A 1 140 ? 6.484  0.939   12.430  1.00 16.89 ? 140 PHE A CD2 1 
ATOM   1185 C CE1 . PHE A 1 140 ? 6.315  -1.619  11.454  1.00 17.58 ? 140 PHE A CE1 1 
ATOM   1186 C CE2 . PHE A 1 140 ? 7.224  0.564   11.320  1.00 17.58 ? 140 PHE A CE2 1 
ATOM   1187 C CZ  . PHE A 1 140 ? 7.144  -0.713  10.843  1.00 17.08 ? 140 PHE A CZ  1 
ATOM   1188 N N   . LEU A 1 141 ? 2.006  -0.071  16.069  1.00 20.53 ? 141 LEU A N   1 
ATOM   1189 C CA  . LEU A 1 141 ? 1.467  0.022   17.427  1.00 22.25 ? 141 LEU A CA  1 
ATOM   1190 C C   . LEU A 1 141 ? 2.194  -0.996  18.303  1.00 22.71 ? 141 LEU A C   1 
ATOM   1191 O O   . LEU A 1 141 ? 3.009  -1.765  17.799  1.00 22.61 ? 141 LEU A O   1 
ATOM   1192 C CB  . LEU A 1 141 ? -0.022 -0.321  17.412  1.00 23.61 ? 141 LEU A CB  1 
ATOM   1193 C CG  . LEU A 1 141 ? -0.880 0.558   16.561  1.00 26.86 ? 141 LEU A CG  1 
ATOM   1194 C CD1 . LEU A 1 141 ? -2.217 -0.070  16.370  1.00 28.11 ? 141 LEU A CD1 1 
ATOM   1195 C CD2 . LEU A 1 141 ? -1.000 1.953   17.161  1.00 27.94 ? 141 LEU A CD2 1 
ATOM   1196 N N   . ASN A 1 142 ? 1.876  -1.054  19.615  1.00 23.13 ? 142 ASN A N   1 
ATOM   1197 C CA  . ASN A 1 142 ? 2.473  -2.056  20.495  1.00 23.46 ? 142 ASN A CA  1 
ATOM   1198 C C   . ASN A 1 142 ? 2.080  -3.453  20.002  1.00 21.95 ? 142 ASN A C   1 
ATOM   1199 O O   . ASN A 1 142 ? 0.950  -3.667  19.566  1.00 22.17 ? 142 ASN A O   1 
ATOM   1200 C CB  . ASN A 1 142 ? 2.077  -1.814  21.953  1.00 26.50 ? 142 ASN A CB  1 
ATOM   1201 C CG  . ASN A 1 142 ? 2.744  -0.586  22.522  1.00 33.37 ? 142 ASN A CG  1 
ATOM   1202 O OD1 . ASN A 1 142 ? 3.924  -0.317  22.266  1.00 35.67 ? 142 ASN A OD1 1 
ATOM   1203 N ND2 . ASN A 1 142 ? 2.005  0.198   23.302  1.00 35.11 ? 142 ASN A ND2 1 
ATOM   1204 N N   . GLY A 1 143 ? 3.065  -4.323  19.913  1.00 20.23 ? 143 GLY A N   1 
ATOM   1205 C CA  . GLY A 1 143 ? 2.872  -5.658  19.374  1.00 18.71 ? 143 GLY A CA  1 
ATOM   1206 C C   . GLY A 1 143 ? 3.365  -5.788  17.939  1.00 16.65 ? 143 GLY A C   1 
ATOM   1207 O O   . GLY A 1 143 ? 3.442  -6.903  17.428  1.00 16.13 ? 143 GLY A O   1 
ATOM   1208 N N   . SER A 1 144 ? 3.691  -4.663  17.268  1.00 15.41 ? 144 SER A N   1 
ATOM   1209 C CA  . SER A 1 144 ? 4.151  -4.716  15.875  1.00 14.02 ? 144 SER A CA  1 
ATOM   1210 C C   . SER A 1 144 ? 5.623  -5.030  15.716  1.00 13.25 ? 144 SER A C   1 
ATOM   1211 O O   . SER A 1 144 ? 6.059  -5.283  14.594  1.00 12.34 ? 144 SER A O   1 
ATOM   1212 C CB  . SER A 1 144 ? 3.856  -3.411  15.150  1.00 14.75 ? 144 SER A CB  1 
ATOM   1213 O OG  . SER A 1 144 ? 4.555  -2.361  15.795  1.00 16.91 ? 144 SER A OG  1 
ATOM   1214 N N   . CYS A 1 145 ? 6.413  -5.035  16.803  1.00 13.27 ? 145 CYS A N   1 
ATOM   1215 C CA  . CYS A 1 145 ? 7.837  -5.364  16.678  1.00 13.16 ? 145 CYS A CA  1 
ATOM   1216 C C   . CYS A 1 145 ? 8.043  -6.722  16.046  1.00 12.44 ? 145 CYS A C   1 
ATOM   1217 O O   . CYS A 1 145 ? 7.218  -7.618  16.221  1.00 12.76 ? 145 CYS A O   1 
ATOM   1218 C CB  . CYS A 1 145 ? 8.549  -5.254  18.016  1.00 14.52 ? 145 CYS A CB  1 
ATOM   1219 S SG  . CYS A 1 145 ? 8.542  -3.580  18.699  1.00 19.18 ? 145 CYS A SG  1 
ATOM   1220 N N   . GLY A 1 146 ? 9.054  -6.812  15.211  1.00 11.62 ? 146 GLY A N   1 
ATOM   1221 C CA  . GLY A 1 146 ? 9.297  -8.040  14.474  1.00 11.65 ? 146 GLY A CA  1 
ATOM   1222 C C   . GLY A 1 146 ? 8.639  -8.028  13.111  1.00 11.50 ? 146 GLY A C   1 
ATOM   1223 O O   . GLY A 1 146 ? 8.938  -8.880  12.282  1.00 12.48 ? 146 GLY A O   1 
ATOM   1224 N N   . SER A 1 147 ? 7.753  -7.040  12.831  1.00 11.19 ? 147 SER A N   1 
ATOM   1225 C CA  . SER A 1 147 ? 7.204  -6.880  11.475  1.00 11.25 ? 147 SER A CA  1 
ATOM   1226 C C   . SER A 1 147 ? 8.385  -6.510  10.565  1.00 11.68 ? 147 SER A C   1 
ATOM   1227 O O   . SER A 1 147 ? 9.322  -5.827  11.010  1.00 11.33 ? 147 SER A O   1 
ATOM   1228 C CB  . SER A 1 147 ? 6.210  -5.723  11.428  1.00 12.25 ? 147 SER A CB  1 
ATOM   1229 O OG  . SER A 1 147 ? 5.054  -6.012  12.198  1.00 13.30 ? 147 SER A OG  1 
ATOM   1230 N N   . VAL A 1 148 ? 8.354  -6.970  9.308   1.00 11.17 ? 148 VAL A N   1 
ATOM   1231 C CA  . VAL A 1 148 ? 9.493  -6.779  8.444   1.00 11.78 ? 148 VAL A CA  1 
ATOM   1232 C C   . VAL A 1 148 ? 9.223  -5.923  7.220   1.00 12.04 ? 148 VAL A C   1 
ATOM   1233 O O   . VAL A 1 148 ? 8.088  -5.781  6.767   1.00 11.94 ? 148 VAL A O   1 
ATOM   1234 C CB  . VAL A 1 148 ? 10.129 -8.138  8.036   1.00 12.63 ? 148 VAL A CB  1 
ATOM   1235 C CG1 . VAL A 1 148 ? 10.607 -8.914  9.260   1.00 12.66 ? 148 VAL A CG1 1 
ATOM   1236 C CG2 . VAL A 1 148 ? 9.180  -8.973  7.195   1.00 13.55 ? 148 VAL A CG2 1 
ATOM   1237 N N   . GLY A 1 149 ? 10.312 -5.371  6.699   1.00 12.16 ? 149 GLY A N   1 
ATOM   1238 C CA  . GLY A 1 149 ? 10.362 -4.619  5.460   1.00 12.30 ? 149 GLY A CA  1 
ATOM   1239 C C   . GLY A 1 149 ? 11.095 -5.441  4.419   1.00 12.43 ? 149 GLY A C   1 
ATOM   1240 O O   . GLY A 1 149 ? 12.033 -6.187  4.731   1.00 12.20 ? 149 GLY A O   1 
ATOM   1241 N N   . PHE A 1 150 ? 10.650 -5.327  3.175   1.00 12.00 ? 150 PHE A N   1 
ATOM   1242 C CA  . PHE A 1 150 ? 11.198 -6.146  2.114   1.00 13.19 ? 150 PHE A CA  1 
ATOM   1243 C C   . PHE A 1 150 ? 10.981 -5.537  0.748   1.00 14.59 ? 150 PHE A C   1 
ATOM   1244 O O   . PHE A 1 150 ? 10.124 -4.675  0.576   1.00 14.07 ? 150 PHE A O   1 
ATOM   1245 C CB  . PHE A 1 150 ? 10.498 -7.529  2.164   1.00 13.42 ? 150 PHE A CB  1 
ATOM   1246 C CG  . PHE A 1 150 ? 8.997  -7.465  1.967   1.00 14.35 ? 150 PHE A CG  1 
ATOM   1247 C CD1 . PHE A 1 150 ? 8.154  -7.170  3.021   1.00 15.42 ? 150 PHE A CD1 1 
ATOM   1248 C CD2 . PHE A 1 150 ? 8.432  -7.691  0.721   1.00 15.45 ? 150 PHE A CD2 1 
ATOM   1249 C CE1 . PHE A 1 150 ? 6.783  -7.040  2.825   1.00 16.35 ? 150 PHE A CE1 1 
ATOM   1250 C CE2 . PHE A 1 150 ? 7.052  -7.611  0.541   1.00 16.30 ? 150 PHE A CE2 1 
ATOM   1251 C CZ  . PHE A 1 150 ? 6.239  -7.292  1.593   1.00 15.96 ? 150 PHE A CZ  1 
ATOM   1252 N N   . ASN A 1 151 ? 11.734 -6.041  -0.222  1.00 15.13 ? 151 ASN A N   1 
ATOM   1253 C CA  . ASN A 1 151 ? 11.561 -5.768  -1.644  1.00 16.70 ? 151 ASN A CA  1 
ATOM   1254 C C   . ASN A 1 151 ? 11.469 -7.132  -2.334  1.00 18.24 ? 151 ASN A C   1 
ATOM   1255 O O   . ASN A 1 151 ? 11.926 -8.137  -1.785  1.00 17.68 ? 151 ASN A O   1 
ATOM   1256 C CB  . ASN A 1 151 ? 12.736 -4.982  -2.203  1.00 17.55 ? 151 ASN A CB  1 
ATOM   1257 C CG  . ASN A 1 151 ? 12.678 -3.526  -1.848  1.00 21.16 ? 151 ASN A CG  1 
ATOM   1258 O OD1 . ASN A 1 151 ? 12.018 -2.729  -2.525  1.00 23.71 ? 151 ASN A OD1 1 
ATOM   1259 N ND2 . ASN A 1 151 ? 13.342 -3.149  -0.770  1.00 19.82 ? 151 ASN A ND2 1 
ATOM   1260 N N   . ILE A 1 152 ? 10.860 -7.188  -3.527  1.00 19.82 ? 152 ILE A N   1 
ATOM   1261 C CA  . ILE A 1 152 ? 10.779 -8.458  -4.255  1.00 22.59 ? 152 ILE A CA  1 
ATOM   1262 C C   . ILE A 1 152 ? 11.333 -8.271  -5.655  1.00 25.21 ? 152 ILE A C   1 
ATOM   1263 O O   . ILE A 1 152 ? 11.049 -7.265  -6.296  1.00 25.64 ? 152 ILE A O   1 
ATOM   1264 C CB  . ILE A 1 152 ? 9.350  -9.069  -4.286  1.00 23.47 ? 152 ILE A CB  1 
ATOM   1265 C CG1 . ILE A 1 152 ? 8.720  -9.144  -2.884  1.00 24.58 ? 152 ILE A CG1 1 
ATOM   1266 C CG2 . ILE A 1 152 ? 9.360  -10.453 -4.972  1.00 24.13 ? 152 ILE A CG2 1 
ATOM   1267 C CD1 . ILE A 1 152 ? 7.304  -9.608  -2.866  1.00 25.76 ? 152 ILE A CD1 1 
ATOM   1268 N N   . ASP A 1 153 ? 12.157 -9.211  -6.114  1.00 26.83 ? 153 ASP A N   1 
ATOM   1269 C CA  . ASP A 1 153 ? 12.655 -9.198  -7.484  1.00 28.74 ? 153 ASP A CA  1 
ATOM   1270 C C   . ASP A 1 153 ? 12.170 -10.512 -8.056  1.00 29.83 ? 153 ASP A C   1 
ATOM   1271 O O   . ASP A 1 153 ? 12.773 -11.548 -7.779  1.00 30.55 ? 153 ASP A O   1 
ATOM   1272 C CB  . ASP A 1 153 ? 14.184 -9.123  -7.546  1.00 31.89 ? 153 ASP A CB  1 
ATOM   1273 C CG  . ASP A 1 153 ? 14.688 -8.981  -8.971  1.00 40.02 ? 153 ASP A CG  1 
ATOM   1274 O OD1 . ASP A 1 153 ? 13.977 -8.356  -9.795  1.00 41.47 ? 153 ASP A OD1 1 
ATOM   1275 O OD2 . ASP A 1 153 ? 15.789 -9.501  -9.268  1.00 43.80 ? 153 ASP A OD2 1 
ATOM   1276 N N   . TYR A 1 154 ? 11.037 -10.469 -8.789  1.00 29.57 ? 154 TYR A N   1 
ATOM   1277 C CA  . TYR A 1 154 ? 10.327 -11.603 -9.381  1.00 30.13 ? 154 TYR A CA  1 
ATOM   1278 C C   . TYR A 1 154 ? 9.896  -12.627 -8.298  1.00 29.86 ? 154 TYR A C   1 
ATOM   1279 O O   . TYR A 1 154 ? 8.809  -12.476 -7.736  1.00 30.57 ? 154 TYR A O   1 
ATOM   1280 C CB  . TYR A 1 154 ? 11.081 -12.243 -10.574 0.50 30.31 ? 154 TYR A CB  1 
ATOM   1281 C CG  . TYR A 1 154 ? 10.357 -13.446 -11.143 0.50 31.41 ? 154 TYR A CG  1 
ATOM   1282 C CD1 . TYR A 1 154 ? 9.054  -13.341 -11.609 0.50 32.51 ? 154 TYR A CD1 1 
ATOM   1283 C CD2 . TYR A 1 154 ? 10.964 -14.693 -11.188 0.50 32.38 ? 154 TYR A CD2 1 
ATOM   1284 C CE1 . TYR A 1 154 ? 8.372  -14.447 -12.100 0.50 33.48 ? 154 TYR A CE1 1 
ATOM   1285 C CE2 . TYR A 1 154 ? 10.290 -15.808 -11.669 0.50 33.42 ? 154 TYR A CE2 1 
ATOM   1286 C CZ  . TYR A 1 154 ? 8.994  -15.680 -12.131 0.50 34.48 ? 154 TYR A CZ  1 
ATOM   1287 O OH  . TYR A 1 154 ? 8.328  -16.774 -12.627 0.50 36.31 ? 154 TYR A OH  1 
ATOM   1288 N N   . ASP A 1 155 ? 10.732 -13.629 -7.970  1.00 28.99 ? 155 ASP A N   1 
ATOM   1289 C CA  . ASP A 1 155 ? 10.368 -14.624 -6.961  1.00 28.27 ? 155 ASP A CA  1 
ATOM   1290 C C   . ASP A 1 155 ? 11.249 -14.600 -5.720  1.00 26.66 ? 155 ASP A C   1 
ATOM   1291 O O   . ASP A 1 155 ? 11.085 -15.455 -4.854  1.00 27.06 ? 155 ASP A O   1 
ATOM   1292 C CB  . ASP A 1 155 ? 10.346 -16.038 -7.566  1.00 30.93 ? 155 ASP A CB  1 
ATOM   1293 C CG  . ASP A 1 155 ? 11.673 -16.511 -8.140  1.00 36.67 ? 155 ASP A CG  1 
ATOM   1294 O OD1 . ASP A 1 155 ? 12.607 -15.683 -8.250  1.00 37.43 ? 155 ASP A OD1 1 
ATOM   1295 O OD2 . ASP A 1 155 ? 11.772 -17.708 -8.495  1.00 39.58 ? 155 ASP A OD2 1 
ATOM   1296 N N   . CYS A 1 156 ? 12.175 -13.637 -5.622  1.00 24.66 ? 156 CYS A N   1 
ATOM   1297 C CA  . CYS A 1 156 ? 13.076 -13.566 -4.484  1.00 23.25 ? 156 CYS A CA  1 
ATOM   1298 C C   . CYS A 1 156 ? 12.758 -12.398 -3.587  1.00 20.76 ? 156 CYS A C   1 
ATOM   1299 O O   . CYS A 1 156 ? 12.827 -11.248 -4.023  1.00 20.48 ? 156 CYS A O   1 
ATOM   1300 C CB  . CYS A 1 156 ? 14.525 -13.518 -4.955  1.00 24.48 ? 156 CYS A CB  1 
ATOM   1301 S SG  . CYS A 1 156 ? 15.738 -13.478 -3.610  1.00 27.04 ? 156 CYS A SG  1 
ATOM   1302 N N   . VAL A 1 157 ? 12.484 -12.680 -2.310  1.00 18.60 ? 157 VAL A N   1 
ATOM   1303 C CA  . VAL A 1 157 ? 12.218 -11.620 -1.344  1.00 17.05 ? 157 VAL A CA  1 
ATOM   1304 C C   . VAL A 1 157 ? 13.514 -11.180 -0.700  1.00 15.71 ? 157 VAL A C   1 
ATOM   1305 O O   . VAL A 1 157 ? 14.196 -11.995 -0.084  1.00 15.50 ? 157 VAL A O   1 
ATOM   1306 C CB  . VAL A 1 157 ? 11.247 -12.102 -0.243  1.00 17.28 ? 157 VAL A CB  1 
ATOM   1307 C CG1 . VAL A 1 157 ? 10.950 -10.990 0.757   1.00 17.60 ? 157 VAL A CG1 1 
ATOM   1308 C CG2 . VAL A 1 157 ? 9.958  -12.653 -0.847  1.00 18.06 ? 157 VAL A CG2 1 
ATOM   1309 N N   . SER A 1 158 ? 13.840 -9.894  -0.794  1.00 15.06 ? 158 SER A N   1 
ATOM   1310 C CA  . SER A 1 158 ? 15.008 -9.358  -0.111  1.00 14.90 ? 158 SER A CA  1 
ATOM   1311 C C   . SER A 1 158 ? 14.517 -8.654  1.138   1.00 14.32 ? 158 SER A C   1 
ATOM   1312 O O   . SER A 1 158 ? 13.944 -7.567  1.050   1.00 14.24 ? 158 SER A O   1 
ATOM   1313 C CB  . SER A 1 158 ? 15.755 -8.366  -0.997  1.00 17.17 ? 158 SER A CB  1 
ATOM   1314 O OG  . SER A 1 158 ? 16.436 -9.063  -2.024  1.00 20.62 ? 158 SER A OG  1 
ATOM   1315 N N   . PHE A 1 159 ? 14.725 -9.276  2.299   1.00 13.50 ? 159 PHE A N   1 
ATOM   1316 C CA  . PHE A 1 159 ? 14.327 -8.676  3.565   1.00 13.12 ? 159 PHE A CA  1 
ATOM   1317 C C   . PHE A 1 159 ? 15.366 -7.649  3.959   1.00 12.99 ? 159 PHE A C   1 
ATOM   1318 O O   . PHE A 1 159 ? 16.559 -7.954  3.983   1.00 13.40 ? 159 PHE A O   1 
ATOM   1319 C CB  . PHE A 1 159 ? 14.245 -9.749  4.654   1.00 12.61 ? 159 PHE A CB  1 
ATOM   1320 C CG  . PHE A 1 159 ? 13.131 -10.726 4.411   1.00 11.64 ? 159 PHE A CG  1 
ATOM   1321 C CD1 . PHE A 1 159 ? 11.819 -10.392 4.702   1.00 12.23 ? 159 PHE A CD1 1 
ATOM   1322 C CD2 . PHE A 1 159 ? 13.391 -11.978 3.887   1.00 11.94 ? 159 PHE A CD2 1 
ATOM   1323 C CE1 . PHE A 1 159 ? 10.793 -11.300 4.508   1.00 12.59 ? 159 PHE A CE1 1 
ATOM   1324 C CE2 . PHE A 1 159 ? 12.357 -12.881 3.669   1.00 12.59 ? 159 PHE A CE2 1 
ATOM   1325 C CZ  . PHE A 1 159 ? 11.064 -12.538 3.991   1.00 12.27 ? 159 PHE A CZ  1 
ATOM   1326 N N   . CYS A 1 160 ? 14.918 -6.444  4.317   1.00 12.93 ? 160 CYS A N   1 
ATOM   1327 C CA  . CYS A 1 160 ? 15.839 -5.365  4.668   1.00 13.50 ? 160 CYS A CA  1 
ATOM   1328 C C   . CYS A 1 160 ? 15.596 -4.739  6.011   1.00 13.22 ? 160 CYS A C   1 
ATOM   1329 O O   . CYS A 1 160 ? 16.451 -3.984  6.456   1.00 13.85 ? 160 CYS A O   1 
ATOM   1330 C CB  . CYS A 1 160 ? 15.838 -4.296  3.580   1.00 14.93 ? 160 CYS A CB  1 
ATOM   1331 S SG  . CYS A 1 160 ? 14.213 -3.572  3.272   1.00 15.19 ? 160 CYS A SG  1 
ATOM   1332 N N   . TYR A 1 161 ? 14.433 -4.952  6.614   1.00 12.04 ? 161 TYR A N   1 
ATOM   1333 C CA  . TYR A 1 161 ? 14.112 -4.270  7.849   1.00 11.92 ? 161 TYR A CA  1 
ATOM   1334 C C   . TYR A 1 161 ? 13.335 -5.134  8.797   1.00 11.21 ? 161 TYR A C   1 
ATOM   1335 O O   . TYR A 1 161 ? 12.520 -5.929  8.377   1.00 11.05 ? 161 TYR A O   1 
ATOM   1336 C CB  . TYR A 1 161 ? 13.272 -3.020  7.497   1.00 11.04 ? 161 TYR A CB  1 
ATOM   1337 C CG  . TYR A 1 161 ? 12.873 -2.174  8.686   1.00 11.13 ? 161 TYR A CG  1 
ATOM   1338 C CD1 . TYR A 1 161 ? 13.734 -1.221  9.206   1.00 12.22 ? 161 TYR A CD1 1 
ATOM   1339 C CD2 . TYR A 1 161 ? 11.614 -2.292  9.256   1.00 11.72 ? 161 TYR A CD2 1 
ATOM   1340 C CE1 . TYR A 1 161 ? 13.370 -0.445  10.303  1.00 12.77 ? 161 TYR A CE1 1 
ATOM   1341 C CE2 . TYR A 1 161 ? 11.245 -1.535  10.356  1.00 12.42 ? 161 TYR A CE2 1 
ATOM   1342 C CZ  . TYR A 1 161 ? 12.120 -0.604  10.873  1.00 12.57 ? 161 TYR A CZ  1 
ATOM   1343 O OH  . TYR A 1 161 ? 11.751 0.138   11.977  1.00 12.95 ? 161 TYR A OH  1 
ATOM   1344 N N   . MET A 1 162 ? 13.585 -4.974  10.085  1.00 10.28 ? 162 MET A N   1 
ATOM   1345 C CA  . MET A 1 162 ? 12.783 -5.594  11.126  1.00 10.68 ? 162 MET A CA  1 
ATOM   1346 C C   . MET A 1 162 ? 12.509 -4.476  12.131  1.00 10.72 ? 162 MET A C   1 
ATOM   1347 O O   . MET A 1 162 ? 13.429 -3.757  12.531  1.00 10.71 ? 162 MET A O   1 
ATOM   1348 C CB  . MET A 1 162 ? 13.469 -6.782  11.785  1.00 11.91 ? 162 MET A CB  1 
ATOM   1349 C CG  . MET A 1 162 ? 12.631 -7.332  12.936  1.00 12.92 ? 162 MET A CG  1 
ATOM   1350 S SD  . MET A 1 162 ? 13.162 -8.961  13.503  1.00 15.17 ? 162 MET A SD  1 
ATOM   1351 C CE  . MET A 1 162 ? 12.432 -9.997  12.218  1.00 16.30 ? 162 MET A CE  1 
ATOM   1352 N N   . HIS A 1 163 ? 11.245 -4.306  12.496  1.00 10.85 ? 163 HIS A N   1 
ATOM   1353 C CA  . HIS A 1 163 ? 10.862 -3.230  13.394  1.00 10.78 ? 163 HIS A CA  1 
ATOM   1354 C C   . HIS A 1 163 ? 11.218 -3.501  14.829  1.00 10.88 ? 163 HIS A C   1 
ATOM   1355 O O   . HIS A 1 163 ? 10.858 -4.554  15.333  1.00 11.36 ? 163 HIS A O   1 
ATOM   1356 C CB  . HIS A 1 163 ? 9.363  -2.967  13.299  1.00 11.80 ? 163 HIS A CB  1 
ATOM   1357 C CG  . HIS A 1 163 ? 8.995  -1.754  14.072  1.00 12.60 ? 163 HIS A CG  1 
ATOM   1358 N ND1 . HIS A 1 163 ? 9.637  -0.545  13.857  1.00 13.89 ? 163 HIS A ND1 1 
ATOM   1359 C CD2 . HIS A 1 163 ? 8.139  -1.619  15.105  1.00 13.61 ? 163 HIS A CD2 1 
ATOM   1360 C CE1 . HIS A 1 163 ? 9.124  0.289   14.740  1.00 14.58 ? 163 HIS A CE1 1 
ATOM   1361 N NE2 . HIS A 1 163 ? 8.222  -0.307  15.514  1.00 14.16 ? 163 HIS A NE2 1 
ATOM   1362 N N   . HIS A 1 164 ? 11.850 -2.524  15.504  1.00 10.72 ? 164 HIS A N   1 
ATOM   1363 C CA  . HIS A 1 164 ? 12.191 -2.691  16.911  1.00 12.02 ? 164 HIS A CA  1 
ATOM   1364 C C   . HIS A 1 164 ? 11.654 -1.626  17.827  1.00 13.54 ? 164 HIS A C   1 
ATOM   1365 O O   . HIS A 1 164 ? 11.296 -1.961  18.960  1.00 14.57 ? 164 HIS A O   1 
ATOM   1366 C CB  . HIS A 1 164 ? 13.720 -2.699  17.140  1.00 12.32 ? 164 HIS A CB  1 
ATOM   1367 C CG  . HIS A 1 164 ? 14.408 -3.927  16.654  1.00 11.31 ? 164 HIS A CG  1 
ATOM   1368 N ND1 . HIS A 1 164 ? 15.090 -4.762  17.524  1.00 11.61 ? 164 HIS A ND1 1 
ATOM   1369 C CD2 . HIS A 1 164 ? 14.549 -4.392  15.393  1.00 11.50 ? 164 HIS A CD2 1 
ATOM   1370 C CE1 . HIS A 1 164 ? 15.623 -5.706  16.765  1.00 11.94 ? 164 HIS A CE1 1 
ATOM   1371 N NE2 . HIS A 1 164 ? 15.308 -5.537  15.478  1.00 12.33 ? 164 HIS A NE2 1 
ATOM   1372 N N   A MET A 1 165 ? 11.586 -0.360  17.376  0.50 14.49 ? 165 MET A N   1 
ATOM   1373 N N   B MET A 1 165 ? 11.783 -0.326  17.439  0.50 13.59 ? 165 MET A N   1 
ATOM   1374 C CA  A MET A 1 165 ? 11.139 0.666   18.305  0.50 16.09 ? 165 MET A CA  1 
ATOM   1375 C CA  B MET A 1 165 ? 11.504 0.797   18.336  0.50 14.00 ? 165 MET A CA  1 
ATOM   1376 C C   A MET A 1 165 ? 10.595 1.912   17.722  0.50 15.90 ? 165 MET A C   1 
ATOM   1377 C C   B MET A 1 165 ? 10.702 1.944   17.739  0.50 14.88 ? 165 MET A C   1 
ATOM   1378 O O   A MET A 1 165 ? 10.776 2.215   16.550  0.50 15.72 ? 165 MET A O   1 
ATOM   1379 O O   B MET A 1 165 ? 10.842 2.241   16.560  0.50 14.65 ? 165 MET A O   1 
ATOM   1380 C CB  A MET A 1 165 ? 12.260 1.033   19.260  0.50 18.07 ? 165 MET A CB  1 
ATOM   1381 C CB  B MET A 1 165 ? 12.844 1.448   18.767  0.50 13.85 ? 165 MET A CB  1 
ATOM   1382 C CG  A MET A 1 165 ? 13.510 1.441   18.567  0.50 21.85 ? 165 MET A CG  1 
ATOM   1383 C CG  B MET A 1 165 ? 13.883 0.481   19.312  0.50 14.29 ? 165 MET A CG  1 
ATOM   1384 S SD  A MET A 1 165 ? 14.871 1.411   19.737  0.50 29.90 ? 165 MET A SD  1 
ATOM   1385 S SD  B MET A 1 165 ? 13.470 -0.155  20.945  0.50 15.29 ? 165 MET A SD  1 
ATOM   1386 C CE  A MET A 1 165 ? 14.286 0.130   20.907  0.50 30.34 ? 165 MET A CE  1 
ATOM   1387 C CE  B MET A 1 165 ? 13.829 1.249   21.920  0.50 19.00 ? 165 MET A CE  1 
ATOM   1388 N N   . GLU A 1 166 ? 9.962  2.669   18.591  1.00 16.13 ? 166 GLU A N   1 
ATOM   1389 C CA  . GLU A 1 166 ? 9.355  3.908   18.240  1.00 17.53 ? 166 GLU A CA  1 
ATOM   1390 C C   . GLU A 1 166 ? 10.049 4.945   19.115  1.00 19.53 ? 166 GLU A C   1 
ATOM   1391 O O   . GLU A 1 166 ? 10.099 4.793   20.337  1.00 20.14 ? 166 GLU A O   1 
ATOM   1392 C CB  . GLU A 1 166 ? 7.885  3.883   18.595  1.00 19.56 ? 166 GLU A CB  1 
ATOM   1393 C CG  . GLU A 1 166 ? 7.200  5.177   18.243  1.00 23.51 ? 166 GLU A CG  1 
ATOM   1394 C CD  . GLU A 1 166 ? 5.719  4.914   18.267  1.00 27.84 ? 166 GLU A CD  1 
ATOM   1395 O OE1 . GLU A 1 166 ? 5.148  4.841   19.378  1.00 29.33 ? 166 GLU A OE1 1 
ATOM   1396 O OE2 . GLU A 1 166 ? 5.144  4.697   17.176  1.00 27.18 ? 166 GLU A OE2 1 
ATOM   1397 N N   . LEU A 1 167 ? 10.596 5.973   18.494  1.00 20.80 ? 167 LEU A N   1 
ATOM   1398 C CA  . LEU A 1 167 ? 11.246 7.053   19.220  1.00 23.30 ? 167 LEU A CA  1 
ATOM   1399 C C   . LEU A 1 167 ? 10.170 7.948   19.834  1.00 25.62 ? 167 LEU A C   1 
ATOM   1400 O O   . LEU A 1 167 ? 9.054  8.016   19.312  1.00 25.54 ? 167 LEU A O   1 
ATOM   1401 C CB  . LEU A 1 167 ? 12.109 7.853   18.227  1.00 24.19 ? 167 LEU A CB  1 
ATOM   1402 C CG  . LEU A 1 167 ? 13.150 7.045   17.422  1.00 26.98 ? 167 LEU A CG  1 
ATOM   1403 C CD1 . LEU A 1 167 ? 14.029 7.967   16.621  1.00 28.28 ? 167 LEU A CD1 1 
ATOM   1404 C CD2 . LEU A 1 167 ? 14.022 6.155   18.327  1.00 27.79 ? 167 LEU A CD2 1 
ATOM   1405 N N   . PRO A 1 168 ? 10.502 8.716   20.885  1.00 27.44 ? 168 PRO A N   1 
ATOM   1406 C CA  . PRO A 1 168 ? 9.495  9.604   21.486  1.00 28.84 ? 168 PRO A CA  1 
ATOM   1407 C C   . PRO A 1 168 ? 8.854  10.601  20.525  1.00 30.15 ? 168 PRO A C   1 
ATOM   1408 O O   . PRO A 1 168 ? 7.806  11.147  20.853  1.00 31.65 ? 168 PRO A O   1 
ATOM   1409 C CB  . PRO A 1 168 ? 10.264 10.307  22.605  1.00 29.60 ? 168 PRO A CB  1 
ATOM   1410 C CG  . PRO A 1 168 ? 11.376 9.380   22.945  1.00 29.87 ? 168 PRO A CG  1 
ATOM   1411 C CD  . PRO A 1 168 ? 11.767 8.736   21.646  1.00 27.74 ? 168 PRO A CD  1 
ATOM   1412 N N   . THR A 1 169 ? 9.448  10.838  19.342  1.00 29.64 ? 169 THR A N   1 
ATOM   1413 C CA  . THR A 1 169 ? 8.869  11.743  18.351  1.00 29.70 ? 169 THR A CA  1 
ATOM   1414 C C   . THR A 1 169 ? 7.931  11.078  17.330  1.00 29.13 ? 169 THR A C   1 
ATOM   1415 O O   . THR A 1 169 ? 7.497  11.738  16.388  1.00 29.33 ? 169 THR A O   1 
ATOM   1416 C CB  . THR A 1 169 ? 9.946  12.533  17.623  1.00 31.65 ? 169 THR A CB  1 
ATOM   1417 O OG1 . THR A 1 169 ? 10.933 11.626  17.118  1.00 32.87 ? 169 THR A OG1 1 
ATOM   1418 C CG2 . THR A 1 169 ? 10.574 13.602  18.502  1.00 32.20 ? 169 THR A CG2 1 
ATOM   1419 N N   . GLY A 1 170 ? 7.618  9.799   17.517  1.00 28.09 ? 170 GLY A N   1 
ATOM   1420 C CA  . GLY A 1 170 ? 6.690  9.104   16.634  1.00 27.29 ? 170 GLY A CA  1 
ATOM   1421 C C   . GLY A 1 170 ? 7.276  8.478   15.392  1.00 25.98 ? 170 GLY A C   1 
ATOM   1422 O O   . GLY A 1 170 ? 6.531  7.969   14.548  1.00 26.76 ? 170 GLY A O   1 
ATOM   1423 N N   . VAL A 1 171 ? 8.602  8.553   15.235  1.00 23.64 ? 171 VAL A N   1 
ATOM   1424 C CA  . VAL A 1 171 ? 9.262  7.930   14.096  1.00 21.19 ? 171 VAL A CA  1 
ATOM   1425 C C   . VAL A 1 171 ? 9.803  6.561   14.543  1.00 17.38 ? 171 VAL A C   1 
ATOM   1426 O O   . VAL A 1 171 ? 9.847  6.266   15.735  1.00 17.18 ? 171 VAL A O   1 
ATOM   1427 C CB  . VAL A 1 171 ? 10.323 8.817   13.418  1.00 22.74 ? 171 VAL A CB  1 
ATOM   1428 C CG1 . VAL A 1 171 ? 9.690  10.084  12.853  1.00 23.85 ? 171 VAL A CG1 1 
ATOM   1429 C CG2 . VAL A 1 171 ? 11.443 9.141   14.386  1.00 23.08 ? 171 VAL A CG2 1 
ATOM   1430 N N   . HIS A 1 172 ? 10.166 5.722   13.586  1.00 15.44 ? 172 HIS A N   1 
ATOM   1431 C CA  . HIS A 1 172 ? 10.508 4.343   13.854  1.00 13.98 ? 172 HIS A CA  1 
ATOM   1432 C C   . HIS A 1 172 ? 11.940 3.965   13.543  1.00 13.47 ? 172 HIS A C   1 
ATOM   1433 O O   . HIS A 1 172 ? 12.551 4.481   12.612  1.00 13.64 ? 172 HIS A O   1 
ATOM   1434 C CB  . HIS A 1 172 ? 9.512  3.472   13.081  1.00 13.55 ? 172 HIS A CB  1 
ATOM   1435 C CG  . HIS A 1 172 ? 8.096  3.784   13.471  1.00 13.40 ? 172 HIS A CG  1 
ATOM   1436 N ND1 . HIS A 1 172 ? 7.228  4.426   12.601  1.00 14.72 ? 172 HIS A ND1 1 
ATOM   1437 C CD2 . HIS A 1 172 ? 7.501  3.693   14.686  1.00 14.40 ? 172 HIS A CD2 1 
ATOM   1438 C CE1 . HIS A 1 172 ? 6.107  4.609   13.283  1.00 15.27 ? 172 HIS A CE1 1 
ATOM   1439 N NE2 . HIS A 1 172 ? 6.228  4.194   14.544  1.00 15.66 ? 172 HIS A NE2 1 
ATOM   1440 N N   . ALA A 1 173 ? 12.452 3.012   14.322  1.00 12.95 ? 173 ALA A N   1 
ATOM   1441 C CA  . ALA A 1 173 ? 13.821 2.530   14.168  1.00 12.79 ? 173 ALA A CA  1 
ATOM   1442 C C   . ALA A 1 173 ? 13.843 1.028   14.231  1.00 12.27 ? 173 ALA A C   1 
ATOM   1443 O O   . ALA A 1 173 ? 13.033 0.406   14.916  1.00 12.33 ? 173 ALA A O   1 
ATOM   1444 C CB  . ALA A 1 173 ? 14.713 3.092   15.263  1.00 13.06 ? 173 ALA A CB  1 
ATOM   1445 N N   . GLY A 1 174 ? 14.761 0.447   13.481  1.00 11.78 ? 174 GLY A N   1 
ATOM   1446 C CA  . GLY A 1 174 ? 14.888 -0.994  13.445  1.00 11.54 ? 174 GLY A CA  1 
ATOM   1447 C C   . GLY A 1 174 ? 16.188 -1.435  12.847  1.00 11.18 ? 174 GLY A C   1 
ATOM   1448 O O   . GLY A 1 174 ? 17.097 -0.636  12.618  1.00 11.32 ? 174 GLY A O   1 
ATOM   1449 N N   . THR A 1 175 ? 16.261 -2.716  12.564  1.00 10.81 ? 175 THR A N   1 
ATOM   1450 C CA  . THR A 1 175 ? 17.491 -3.329  12.129  1.00 10.66 ? 175 THR A CA  1 
ATOM   1451 C C   . THR A 1 175 ? 17.367 -3.974  10.774  1.00 10.85 ? 175 THR A C   1 
ATOM   1452 O O   . THR A 1 175 ? 16.261 -4.147  10.274  1.00 11.09 ? 175 THR A O   1 
ATOM   1453 C CB  . THR A 1 175 ? 17.861 -4.455  13.166  1.00 11.46 ? 175 THR A CB  1 
ATOM   1454 O OG1 . THR A 1 175 ? 16.924 -5.534  13.087  1.00 11.86 ? 175 THR A OG1 1 
ATOM   1455 C CG2 . THR A 1 175 ? 17.958 -3.963  14.586  1.00 10.45 ? 175 THR A CG2 1 
ATOM   1456 N N   . ASP A 1 176 ? 18.499 -4.410  10.211  1.00 10.92 ? 176 ASP A N   1 
ATOM   1457 C CA  . ASP A 1 176 ? 18.444 -5.296  9.071   1.00 11.27 ? 176 ASP A CA  1 
ATOM   1458 C C   . ASP A 1 176 ? 18.223 -6.736  9.677   1.00 12.10 ? 176 ASP A C   1 
ATOM   1459 O O   . ASP A 1 176 ? 18.096 -6.893  10.907  1.00 12.09 ? 176 ASP A O   1 
ATOM   1460 C CB  . ASP A 1 176 ? 19.709 -5.176  8.218   1.00 12.43 ? 176 ASP A CB  1 
ATOM   1461 C CG  . ASP A 1 176 ? 20.997 -5.503  8.928   1.00 14.28 ? 176 ASP A CG  1 
ATOM   1462 O OD1 . ASP A 1 176 ? 20.945 -6.153  10.000  1.00 12.59 ? 176 ASP A OD1 1 
ATOM   1463 O OD2 . ASP A 1 176 ? 22.059 -5.109  8.421   1.00 16.57 ? 176 ASP A OD2 1 
ATOM   1464 N N   . LEU A 1 177 ? 18.214 -7.776  8.839   1.00 12.56 ? 177 LEU A N   1 
ATOM   1465 C CA  . LEU A 1 177 ? 17.977 -9.134  9.340   1.00 13.37 ? 177 LEU A CA  1 
ATOM   1466 C C   . LEU A 1 177 ? 19.229 -9.788  9.950   1.00 14.68 ? 177 LEU A C   1 
ATOM   1467 O O   . LEU A 1 177 ? 19.141 -10.901 10.466  1.00 15.23 ? 177 LEU A O   1 
ATOM   1468 C CB  . LEU A 1 177 ? 17.292 -10.027 8.318   1.00 13.37 ? 177 LEU A CB  1 
ATOM   1469 C CG  . LEU A 1 177 ? 15.764 -9.973  8.325   1.00 14.51 ? 177 LEU A CG  1 
ATOM   1470 C CD1 . LEU A 1 177 ? 15.215 -10.582 9.597   1.00 15.35 ? 177 LEU A CD1 1 
ATOM   1471 C CD2 . LEU A 1 177 ? 15.227 -8.547  8.101   1.00 15.65 ? 177 LEU A CD2 1 
ATOM   1472 N N   . GLU A 1 178 ? 20.370 -9.083  9.938   1.00 14.29 ? 178 GLU A N   1 
ATOM   1473 C CA  . GLU A 1 178 ? 21.541 -9.484  10.702  1.00 13.76 ? 178 GLU A CA  1 
ATOM   1474 C C   . GLU A 1 178 ? 21.486 -8.861  12.125  1.00 13.43 ? 178 GLU A C   1 
ATOM   1475 O O   . GLU A 1 178 ? 22.376 -9.100  12.928  1.00 13.86 ? 178 GLU A O   1 
ATOM   1476 C CB  . GLU A 1 178 ? 22.832 -9.097  9.978   1.00 15.67 ? 178 GLU A CB  1 
ATOM   1477 C CG  . GLU A 1 178 ? 22.961 -9.834  8.661   1.00 20.95 ? 178 GLU A CG  1 
ATOM   1478 C CD  . GLU A 1 178 ? 24.223 -9.546  7.877   1.00 29.38 ? 178 GLU A CD  1 
ATOM   1479 O OE1 . GLU A 1 178 ? 24.984 -8.632  8.273   1.00 29.50 ? 178 GLU A OE1 1 
ATOM   1480 O OE2 . GLU A 1 178 ? 24.452 -10.242 6.861   1.00 33.24 ? 178 GLU A OE2 1 
ATOM   1481 N N   . GLY A 1 179 ? 20.467 -8.044  12.419  1.00 13.13 ? 179 GLY A N   1 
ATOM   1482 C CA  . GLY A 1 179 ? 20.307 -7.465  13.737  1.00 12.66 ? 179 GLY A CA  1 
ATOM   1483 C C   . GLY A 1 179 ? 21.024 -6.160  13.973  1.00 12.23 ? 179 GLY A C   1 
ATOM   1484 O O   . GLY A 1 179 ? 21.067 -5.710  15.109  1.00 12.53 ? 179 GLY A O   1 
ATOM   1485 N N   . ASN A 1 180 ? 21.583 -5.550  12.928  1.00 11.78 ? 180 ASN A N   1 
ATOM   1486 C CA  . ASN A 1 180 ? 22.268 -4.273  13.077  1.00 12.01 ? 180 ASN A CA  1 
ATOM   1487 C C   . ASN A 1 180 ? 21.296 -3.149  12.821  1.00 11.40 ? 180 ASN A C   1 
ATOM   1488 O O   . ASN A 1 180 ? 20.701 -3.072  11.748  1.00 10.73 ? 180 ASN A O   1 
ATOM   1489 C CB  . ASN A 1 180 ? 23.447 -4.180  12.113  1.00 13.42 ? 180 ASN A CB  1 
ATOM   1490 C CG  . ASN A 1 180 ? 24.560 -5.117  12.483  1.00 16.66 ? 180 ASN A CG  1 
ATOM   1491 O OD1 . ASN A 1 180 ? 25.033 -5.908  11.663  1.00 18.84 ? 180 ASN A OD1 1 
ATOM   1492 N ND2 . ASN A 1 180 ? 24.992 -5.054  13.726  1.00 16.09 ? 180 ASN A ND2 1 
ATOM   1493 N N   . PHE A 1 181 ? 21.136 -2.246  13.795  1.00 11.37 ? 181 PHE A N   1 
ATOM   1494 C CA  . PHE A 1 181 ? 20.248 -1.104  13.610  1.00 11.91 ? 181 PHE A CA  1 
ATOM   1495 C C   . PHE A 1 181 ? 20.686 -0.235  12.452  1.00 12.38 ? 181 PHE A C   1 
ATOM   1496 O O   . PHE A 1 181 ? 21.881 -0.094  12.176  1.00 12.34 ? 181 PHE A O   1 
ATOM   1497 C CB  . PHE A 1 181 ? 20.201 -0.235  14.871  1.00 12.24 ? 181 PHE A CB  1 
ATOM   1498 C CG  . PHE A 1 181 ? 19.085 -0.590  15.813  1.00 12.39 ? 181 PHE A CG  1 
ATOM   1499 C CD1 . PHE A 1 181 ? 19.280 -1.514  16.825  1.00 12.74 ? 181 PHE A CD1 1 
ATOM   1500 C CD2 . PHE A 1 181 ? 17.854 0.039   15.721  1.00 12.69 ? 181 PHE A CD2 1 
ATOM   1501 C CE1 . PHE A 1 181 ? 18.258 -1.822  17.714  1.00 12.99 ? 181 PHE A CE1 1 
ATOM   1502 C CE2 . PHE A 1 181 ? 16.828 -0.277  16.600  1.00 13.19 ? 181 PHE A CE2 1 
ATOM   1503 C CZ  . PHE A 1 181 ? 17.031 -1.207  17.593  1.00 13.05 ? 181 PHE A CZ  1 
ATOM   1504 N N   . TYR A 1 182 ? 19.702 0.341   11.784  1.00 11.78 ? 182 TYR A N   1 
ATOM   1505 C CA  . TYR A 1 182 ? 19.973 1.380   10.817  1.00 12.63 ? 182 TYR A CA  1 
ATOM   1506 C C   . TYR A 1 182 ? 20.218 2.634   11.653  1.00 13.60 ? 182 TYR A C   1 
ATOM   1507 O O   . TYR A 1 182 ? 19.486 2.909   12.615  1.00 14.08 ? 182 TYR A O   1 
ATOM   1508 C CB  . TYR A 1 182 ? 18.765 1.574   9.929   1.00 12.36 ? 182 TYR A CB  1 
ATOM   1509 C CG  . TYR A 1 182 ? 18.689 0.495   8.878   1.00 12.38 ? 182 TYR A CG  1 
ATOM   1510 C CD1 . TYR A 1 182 ? 19.511 0.528   7.766   1.00 12.83 ? 182 TYR A CD1 1 
ATOM   1511 C CD2 . TYR A 1 182 ? 17.862 -0.604  9.045   1.00 12.57 ? 182 TYR A CD2 1 
ATOM   1512 C CE1 . TYR A 1 182 ? 19.456 -0.465  6.802   1.00 12.90 ? 182 TYR A CE1 1 
ATOM   1513 C CE2 . TYR A 1 182 ? 17.792 -1.601  8.089   1.00 12.93 ? 182 TYR A CE2 1 
ATOM   1514 C CZ  . TYR A 1 182 ? 18.601 -1.534  6.970   1.00 13.28 ? 182 TYR A CZ  1 
ATOM   1515 O OH  . TYR A 1 182 ? 18.538 -2.508  5.998   1.00 13.15 ? 182 TYR A OH  1 
ATOM   1516 N N   . GLY A 1 183 ? 21.282 3.338   11.320  1.00 13.88 ? 183 GLY A N   1 
ATOM   1517 C CA  . GLY A 1 183 ? 21.632 4.549   12.030  1.00 15.00 ? 183 GLY A CA  1 
ATOM   1518 C C   . GLY A 1 183 ? 22.167 4.279   13.408  1.00 15.58 ? 183 GLY A C   1 
ATOM   1519 O O   . GLY A 1 183 ? 22.626 3.178   13.716  1.00 15.49 ? 183 GLY A O   1 
ATOM   1520 N N   . PRO A 1 184 ? 22.081 5.295   14.261  1.00 15.71 ? 184 PRO A N   1 
ATOM   1521 C CA  . PRO A 1 184 ? 22.700 5.199   15.592  1.00 15.80 ? 184 PRO A CA  1 
ATOM   1522 C C   . PRO A 1 184 ? 21.818 4.666   16.712  1.00 15.71 ? 184 PRO A C   1 
ATOM   1523 O O   . PRO A 1 184 ? 22.202 4.708   17.880  1.00 16.85 ? 184 PRO A O   1 
ATOM   1524 C CB  . PRO A 1 184 ? 23.004 6.662   15.886  1.00 16.92 ? 184 PRO A CB  1 
ATOM   1525 C CG  . PRO A 1 184 ? 21.820 7.366   15.282  1.00 17.42 ? 184 PRO A CG  1 
ATOM   1526 C CD  . PRO A 1 184 ? 21.576 6.658   13.991  1.00 15.87 ? 184 PRO A CD  1 
ATOM   1527 N N   . PHE A 1 185 ? 20.626 4.205   16.356  1.00 15.02 ? 185 PHE A N   1 
ATOM   1528 C CA  . PHE A 1 185 ? 19.631 3.816   17.322  1.00 15.08 ? 185 PHE A CA  1 
ATOM   1529 C C   . PHE A 1 185 ? 19.972 2.543   18.048  1.00 15.67 ? 185 PHE A C   1 
ATOM   1530 O O   . PHE A 1 185 ? 20.717 1.701   17.548  1.00 15.41 ? 185 PHE A O   1 
ATOM   1531 C CB  . PHE A 1 185 ? 18.245 3.763   16.665  1.00 14.67 ? 185 PHE A CB  1 
ATOM   1532 C CG  . PHE A 1 185 ? 17.918 5.097   16.038  1.00 14.96 ? 185 PHE A CG  1 
ATOM   1533 C CD1 . PHE A 1 185 ? 17.777 6.231   16.819  1.00 15.71 ? 185 PHE A CD1 1 
ATOM   1534 C CD2 . PHE A 1 185 ? 17.856 5.235   14.665  1.00 15.58 ? 185 PHE A CD2 1 
ATOM   1535 C CE1 . PHE A 1 185 ? 17.550 7.473   16.232  1.00 15.86 ? 185 PHE A CE1 1 
ATOM   1536 C CE2 . PHE A 1 185 ? 17.627 6.471   14.088  1.00 15.63 ? 185 PHE A CE2 1 
ATOM   1537 C CZ  . PHE A 1 185 ? 17.450 7.580   14.874  1.00 15.37 ? 185 PHE A CZ  1 
ATOM   1538 N N   . VAL A 1 186 ? 19.484 2.448   19.269  1.00 16.07 ? 186 VAL A N   1 
ATOM   1539 C CA  . VAL A 1 186 ? 19.714 1.295   20.124  1.00 16.52 ? 186 VAL A CA  1 
ATOM   1540 C C   . VAL A 1 186 ? 18.408 0.767   20.679  1.00 16.78 ? 186 VAL A C   1 
ATOM   1541 O O   . VAL A 1 186 ? 17.436 1.513   20.778  1.00 17.71 ? 186 VAL A O   1 
ATOM   1542 C CB  . VAL A 1 186 ? 20.699 1.623   21.273  1.00 17.66 ? 186 VAL A CB  1 
ATOM   1543 C CG1 . VAL A 1 186 ? 22.088 1.924   20.725  1.00 18.92 ? 186 VAL A CG1 1 
ATOM   1544 C CG2 . VAL A 1 186 ? 20.188 2.782   22.130  1.00 18.38 ? 186 VAL A CG2 1 
ATOM   1545 N N   . ASP A 1 187 ? 18.386 -0.515  21.077  1.00 15.60 ? 187 ASP A N   1 
ATOM   1546 C CA  . ASP A 1 187 ? 17.180 -1.106  21.642  1.00 15.58 ? 187 ASP A CA  1 
ATOM   1547 C C   . ASP A 1 187 ? 17.101 -0.911  23.133  1.00 16.90 ? 187 ASP A C   1 
ATOM   1548 O O   . ASP A 1 187 ? 17.132 -1.857  23.916  1.00 16.91 ? 187 ASP A O   1 
ATOM   1549 C CB  . ASP A 1 187 ? 16.973 -2.565  21.246  1.00 15.08 ? 187 ASP A CB  1 
ATOM   1550 C CG  . ASP A 1 187 ? 18.169 -3.478  21.361  1.00 15.13 ? 187 ASP A CG  1 
ATOM   1551 O OD1 . ASP A 1 187 ? 19.244 -3.005  21.797  1.00 15.07 ? 187 ASP A OD1 1 
ATOM   1552 O OD2 . ASP A 1 187 ? 18.030 -4.666  21.026  1.00 14.64 ? 187 ASP A OD2 1 
ATOM   1553 N N   . ARG A 1 188 ? 16.993 0.352   23.513  1.00 18.27 ? 188 ARG A N   1 
ATOM   1554 C CA  . ARG A 1 188 ? 16.915 0.803   24.882  1.00 20.54 ? 188 ARG A CA  1 
ATOM   1555 C C   . ARG A 1 188 ? 15.979 2.000   24.892  1.00 22.19 ? 188 ARG A C   1 
ATOM   1556 O O   . ARG A 1 188 ? 16.006 2.826   23.979  1.00 21.85 ? 188 ARG A O   1 
ATOM   1557 C CB  . ARG A 1 188 ? 18.315 1.222   25.371  1.00 23.06 ? 188 ARG A CB  1 
ATOM   1558 C CG  . ARG A 1 188 ? 18.378 1.486   26.858  1.00 28.82 ? 188 ARG A CG  1 
ATOM   1559 C CD  . ARG A 1 188 ? 19.755 1.913   27.332  1.00 34.58 ? 188 ARG A CD  1 
ATOM   1560 N NE  . ARG A 1 188 ? 19.637 2.726   28.541  1.00 39.48 ? 188 ARG A NE  1 
ATOM   1561 C CZ  . ARG A 1 188 ? 20.650 3.073   29.325  1.00 42.92 ? 188 ARG A CZ  1 
ATOM   1562 N NH1 . ARG A 1 188 ? 21.884 2.678   29.040  1.00 43.29 ? 188 ARG A NH1 1 
ATOM   1563 N NH2 . ARG A 1 188 ? 20.434 3.803   30.412  1.00 43.34 ? 188 ARG A NH2 1 
ATOM   1564 N N   . GLN A 1 189 ? 15.143 2.089   25.912  1.00 24.10 ? 189 GLN A N   1 
ATOM   1565 C CA  . GLN A 1 189 ? 14.193 3.177   26.044  1.00 26.30 ? 189 GLN A CA  1 
ATOM   1566 C C   . GLN A 1 189 ? 14.930 4.350   26.661  1.00 28.13 ? 189 GLN A C   1 
ATOM   1567 O O   . GLN A 1 189 ? 14.955 4.501   27.883  1.00 28.84 ? 189 GLN A O   1 
ATOM   1568 C CB  . GLN A 1 189 ? 13.013 2.731   26.905  1.00 28.62 ? 189 GLN A CB  1 
ATOM   1569 C CG  . GLN A 1 189 ? 11.848 3.700   26.891  1.00 33.55 ? 189 GLN A CG  1 
ATOM   1570 C CD  . GLN A 1 189 ? 10.793 3.236   27.855  1.00 39.90 ? 189 GLN A CD  1 
ATOM   1571 O OE1 . GLN A 1 189 ? 10.375 2.071   27.855  1.00 41.94 ? 189 GLN A OE1 1 
ATOM   1572 N NE2 . GLN A 1 189 ? 10.354 4.137   28.711  1.00 40.98 ? 189 GLN A NE2 1 
ATOM   1573 N N   . THR A 1 190 ? 15.597 5.137   25.811  1.00 29.21 ? 190 THR A N   1 
ATOM   1574 C CA  . THR A 1 190 ? 16.412 6.287   26.208  1.00 30.97 ? 190 THR A CA  1 
ATOM   1575 C C   . THR A 1 190 ? 16.145 7.506   25.303  1.00 31.77 ? 190 THR A C   1 
ATOM   1576 O O   . THR A 1 190 ? 15.420 7.392   24.308  1.00 32.40 ? 190 THR A O   1 
ATOM   1577 C CB  . THR A 1 190 ? 17.915 5.902   26.162  1.00 33.71 ? 190 THR A CB  1 
ATOM   1578 O OG1 . THR A 1 190 ? 18.225 5.263   24.922  1.00 35.59 ? 190 THR A OG1 1 
ATOM   1579 C CG2 . THR A 1 190 ? 18.348 5.087   27.338  1.00 34.74 ? 190 THR A CG2 1 
ATOM   1580 N N   . ALA A 1 191 ? 16.753 8.667   25.625  1.00 31.73 ? 191 ALA A N   1 
ATOM   1581 C CA  . ALA A 1 191 ? 16.636 9.844   24.794  1.00 32.04 ? 191 ALA A CA  1 
ATOM   1582 C C   . ALA A 1 191 ? 17.438 9.584   23.530  1.00 32.03 ? 191 ALA A C   1 
ATOM   1583 O O   . ALA A 1 191 ? 18.667 9.639   23.539  1.00 33.57 ? 191 ALA A O   1 
ATOM   1584 C CB  . ALA A 1 191 ? 17.189 11.058  25.515  1.00 32.37 ? 191 ALA A CB  1 
ATOM   1585 N N   . GLN A 1 192 ? 16.744 9.214   22.473  1.00 30.11 ? 192 GLN A N   1 
ATOM   1586 C CA  . GLN A 1 192 ? 17.362 8.979   21.185  1.00 28.86 ? 192 GLN A CA  1 
ATOM   1587 C C   . GLN A 1 192 ? 16.641 9.910   20.261  1.00 28.78 ? 192 GLN A C   1 
ATOM   1588 O O   . GLN A 1 192 ? 15.459 9.689   19.992  1.00 30.27 ? 192 GLN A O   1 
ATOM   1589 C CB  . GLN A 1 192 ? 17.121 7.544   20.715  1.00 28.03 ? 192 GLN A CB  1 
ATOM   1590 C CG  . GLN A 1 192 ? 17.466 6.488   21.725  1.00 27.39 ? 192 GLN A CG  1 
ATOM   1591 C CD  . GLN A 1 192 ? 17.504 5.185   21.001  1.00 24.21 ? 192 GLN A CD  1 
ATOM   1592 O OE1 . GLN A 1 192 ? 18.318 5.000   20.097  1.00 22.45 ? 192 GLN A OE1 1 
ATOM   1593 N NE2 . GLN A 1 192 ? 16.608 4.276   21.359  1.00 23.00 ? 192 GLN A NE2 1 
ATOM   1594 N N   . ALA A 1 193 ? 17.306 10.977  19.816  1.00 27.11 ? 193 ALA A N   1 
ATOM   1595 C CA  . ALA A 1 193 ? 16.657 11.916  18.912  1.00 26.29 ? 193 ALA A CA  1 
ATOM   1596 C C   . ALA A 1 193 ? 17.154 11.718  17.499  1.00 25.22 ? 193 ALA A C   1 
ATOM   1597 O O   . ALA A 1 193 ? 18.320 11.376  17.282  1.00 25.57 ? 193 ALA A O   1 
ATOM   1598 C CB  . ALA A 1 193 ? 16.894 13.340  19.361  1.00 26.29 ? 193 ALA A CB  1 
ATOM   1599 N N   . ALA A 1 194 ? 16.261 11.895  16.535  1.00 23.81 ? 194 ALA A N   1 
ATOM   1600 C CA  . ALA A 1 194 ? 16.617 11.758  15.133  1.00 22.55 ? 194 ALA A CA  1 
ATOM   1601 C C   . ALA A 1 194 ? 17.257 13.041  14.614  1.00 20.69 ? 194 ALA A C   1 
ATOM   1602 O O   . ALA A 1 194 ? 16.939 14.141  15.065  1.00 20.78 ? 194 ALA A O   1 
ATOM   1603 C CB  . ALA A 1 194 ? 15.384 11.422  14.309  1.00 22.80 ? 194 ALA A CB  1 
ATOM   1604 N N   . GLY A 1 195 ? 18.140 12.891  13.641  1.00 18.81 ? 195 GLY A N   1 
ATOM   1605 C CA  . GLY A 1 195 ? 18.752 14.027  12.981  1.00 18.20 ? 195 GLY A CA  1 
ATOM   1606 C C   . GLY A 1 195 ? 17.782 14.641  11.989  1.00 17.45 ? 195 GLY A C   1 
ATOM   1607 O O   . GLY A 1 195 ? 16.600 14.274  11.937  1.00 17.25 ? 195 GLY A O   1 
ATOM   1608 N N   . THR A 1 196 ? 18.293 15.530  11.144  1.00 16.59 ? 196 THR A N   1 
ATOM   1609 C CA  . THR A 1 196 ? 17.483 16.239  10.165  1.00 16.96 ? 196 THR A CA  1 
ATOM   1610 C C   . THR A 1 196 ? 16.846 15.288  9.210   1.00 17.50 ? 196 THR A C   1 
ATOM   1611 O O   . THR A 1 196 ? 17.541 14.425  8.663   1.00 17.04 ? 196 THR A O   1 
ATOM   1612 C CB  . THR A 1 196 ? 18.339 17.238  9.386   1.00 18.41 ? 196 THR A CB  1 
ATOM   1613 O OG1 . THR A 1 196 ? 19.041 18.066  10.303  1.00 19.49 ? 196 THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 196 ? 17.516 18.113  8.465   1.00 19.24 ? 196 THR A CG2 1 
ATOM   1615 N N   . ASP A 1 197 ? 15.517 15.412  9.024   1.00 17.89 ? 197 ASP A N   1 
ATOM   1616 C CA  . ASP A 1 197 ? 14.850 14.565  8.047   1.00 18.28 ? 197 ASP A CA  1 
ATOM   1617 C C   . ASP A 1 197 ? 14.922 15.240  6.692   1.00 17.83 ? 197 ASP A C   1 
ATOM   1618 O O   . ASP A 1 197 ? 13.995 15.929  6.257   1.00 20.27 ? 197 ASP A O   1 
ATOM   1619 C CB  . ASP A 1 197 ? 13.431 14.139  8.441   1.00 20.37 ? 197 ASP A CB  1 
ATOM   1620 C CG  . ASP A 1 197 ? 12.899 12.932  7.682   1.00 23.82 ? 197 ASP A CG  1 
ATOM   1621 O OD1 . ASP A 1 197 ? 13.654 12.353  6.864   1.00 20.44 ? 197 ASP A OD1 1 
ATOM   1622 O OD2 . ASP A 1 197 ? 11.747 12.542  7.934   1.00 28.73 ? 197 ASP A OD2 1 
ATOM   1623 N N   A THR A 1 198 ? 16.073 15.084  6.036   0.50 16.35 ? 198 THR A N   1 
ATOM   1624 N N   B THR A 1 198 ? 16.027 14.973  6.021   0.50 16.18 ? 198 THR A N   1 
ATOM   1625 C CA  A THR A 1 198 ? 16.273 15.688  4.726   0.50 15.97 ? 198 THR A CA  1 
ATOM   1626 C CA  B THR A 1 198 ? 16.431 15.485  4.722   0.50 15.73 ? 198 THR A CA  1 
ATOM   1627 C C   A THR A 1 198 ? 15.435 14.991  3.669   0.50 15.27 ? 198 THR A C   1 
ATOM   1628 C C   B THR A 1 198 ? 15.577 14.886  3.597   0.50 15.16 ? 198 THR A C   1 
ATOM   1629 O O   A THR A 1 198 ? 14.972 13.861  3.855   0.50 15.28 ? 198 THR A O   1 
ATOM   1630 O O   B THR A 1 198 ? 15.248 13.702  3.663   0.50 15.19 ? 198 THR A O   1 
ATOM   1631 C CB  A THR A 1 198 ? 17.753 15.778  4.371   0.50 17.51 ? 198 THR A CB  1 
ATOM   1632 C CB  B THR A 1 198 ? 17.918 15.133  4.570   0.50 16.74 ? 198 THR A CB  1 
ATOM   1633 O OG1 A THR A 1 198 ? 18.310 14.471  4.399   0.50 18.42 ? 198 THR A OG1 1 
ATOM   1634 O OG1 B THR A 1 198 ? 18.659 15.683  5.672   0.50 17.41 ? 198 THR A OG1 1 
ATOM   1635 C CG2 A THR A 1 198 ? 18.524 16.703  5.296   0.50 17.78 ? 198 THR A CG2 1 
ATOM   1636 C CG2 B THR A 1 198 ? 18.499 15.622  3.285   0.50 17.17 ? 198 THR A CG2 1 
ATOM   1637 N N   . THR A 1 199 ? 15.201 15.692  2.578   1.00 14.19 ? 199 THR A N   1 
ATOM   1638 C CA  . THR A 1 199 ? 14.404 15.175  1.472   1.00 13.47 ? 199 THR A CA  1 
ATOM   1639 C C   . THR A 1 199 ? 15.302 14.448  0.475   1.00 12.86 ? 199 THR A C   1 
ATOM   1640 O O   . THR A 1 199 ? 16.404 14.913  0.194   1.00 13.34 ? 199 THR A O   1 
ATOM   1641 C CB  . THR A 1 199 ? 13.546 16.279  0.859   1.00 14.60 ? 199 THR A CB  1 
ATOM   1642 O OG1 . THR A 1 199 ? 12.711 16.839  1.874   1.00 15.22 ? 199 THR A OG1 1 
ATOM   1643 C CG2 . THR A 1 199 ? 12.667 15.765  -0.281  1.00 15.03 ? 199 THR A CG2 1 
ATOM   1644 N N   . ILE A 1 200 ? 14.861 13.264  -0.011  1.00 12.06 ? 200 ILE A N   1 
ATOM   1645 C CA  . ILE A 1 200 ? 15.633 12.442  -0.950  1.00 12.31 ? 200 ILE A CA  1 
ATOM   1646 C C   . ILE A 1 200 ? 15.432 12.991  -2.363  1.00 11.85 ? 200 ILE A C   1 
ATOM   1647 O O   . ILE A 1 200 ? 14.510 12.616  -3.089  1.00 11.58 ? 200 ILE A O   1 
ATOM   1648 C CB  . ILE A 1 200 ? 15.218 10.951  -0.852  1.00 12.52 ? 200 ILE A CB  1 
ATOM   1649 C CG1 . ILE A 1 200 ? 15.204 10.474  0.626   1.00 12.89 ? 200 ILE A CG1 1 
ATOM   1650 C CG2 . ILE A 1 200 ? 16.162 10.099  -1.689  1.00 12.93 ? 200 ILE A CG2 1 
ATOM   1651 C CD1 . ILE A 1 200 ? 14.183 9.365   0.910   1.00 14.24 ? 200 ILE A CD1 1 
ATOM   1652 N N   . THR A 1 201 ? 16.317 13.911  -2.732  1.00 11.75 ? 201 THR A N   1 
ATOM   1653 C CA  . THR A 1 201 ? 16.264 14.631  -3.995  1.00 12.03 ? 201 THR A CA  1 
ATOM   1654 C C   . THR A 1 201 ? 16.083 13.743  -5.217  1.00 12.46 ? 201 THR A C   1 
ATOM   1655 O O   . THR A 1 201 ? 15.218 14.024  -6.052  1.00 13.25 ? 201 THR A O   1 
ATOM   1656 C CB  . THR A 1 201 ? 17.526 15.476  -4.150  1.00 13.15 ? 201 THR A CB  1 
ATOM   1657 O OG1 . THR A 1 201 ? 17.749 16.207  -2.951  1.00 13.77 ? 201 THR A OG1 1 
ATOM   1658 C CG2 . THR A 1 201 ? 17.479 16.386  -5.360  1.00 14.00 ? 201 THR A CG2 1 
ATOM   1659 N N   . VAL A 1 202 ? 16.888 12.675  -5.341  1.00 11.54 ? 202 VAL A N   1 
ATOM   1660 C CA  . VAL A 1 202 ? 16.798 11.804  -6.519  1.00 12.15 ? 202 VAL A CA  1 
ATOM   1661 C C   . VAL A 1 202 ? 15.402 11.170  -6.634  1.00 12.21 ? 202 VAL A C   1 
ATOM   1662 O O   . VAL A 1 202 ? 14.899 10.999  -7.736  1.00 12.15 ? 202 VAL A O   1 
ATOM   1663 C CB  . VAL A 1 202 ? 17.929 10.751  -6.579  1.00 13.19 ? 202 VAL A CB  1 
ATOM   1664 C CG1 . VAL A 1 202 ? 17.770 9.698   -5.480  1.00 14.16 ? 202 VAL A CG1 1 
ATOM   1665 C CG2 . VAL A 1 202 ? 18.012 10.102  -7.959  1.00 14.05 ? 202 VAL A CG2 1 
ATOM   1666 N N   . ASN A 1 203 ? 14.756 10.889  -5.487  1.00 12.28 ? 203 ASN A N   1 
ATOM   1667 C CA  . ASN A 1 203 ? 13.419 10.315  -5.495  1.00 12.14 ? 203 ASN A CA  1 
ATOM   1668 C C   . ASN A 1 203 ? 12.385 11.343  -5.906  1.00 12.09 ? 203 ASN A C   1 
ATOM   1669 O O   . ASN A 1 203 ? 11.470 11.014  -6.664  1.00 12.27 ? 203 ASN A O   1 
ATOM   1670 C CB  . ASN A 1 203 ? 13.086 9.747   -4.116  1.00 12.23 ? 203 ASN A CB  1 
ATOM   1671 C CG  . ASN A 1 203 ? 13.839 8.482   -3.781  1.00 12.94 ? 203 ASN A CG  1 
ATOM   1672 O OD1 . ASN A 1 203 ? 14.704 8.031   -4.528  1.00 12.49 ? 203 ASN A OD1 1 
ATOM   1673 N ND2 . ASN A 1 203 ? 13.543 7.903   -2.603  1.00 12.93 ? 203 ASN A ND2 1 
ATOM   1674 N N   . VAL A 1 204 ? 12.549 12.612  -5.486  1.00 11.53 ? 204 VAL A N   1 
ATOM   1675 C CA  . VAL A 1 204 ? 11.614 13.665  -5.908  1.00 11.74 ? 204 VAL A CA  1 
ATOM   1676 C C   . VAL A 1 204 ? 11.696 13.853  -7.408  1.00 12.06 ? 204 VAL A C   1 
ATOM   1677 O O   . VAL A 1 204 ? 10.667 13.959  -8.069  1.00 12.65 ? 204 VAL A O   1 
ATOM   1678 C CB  . VAL A 1 204 ? 11.899 14.998  -5.193  1.00 12.37 ? 204 VAL A CB  1 
ATOM   1679 C CG1 . VAL A 1 204 ? 10.971 16.096  -5.711  1.00 12.86 ? 204 VAL A CG1 1 
ATOM   1680 C CG2 . VAL A 1 204 ? 11.731 14.836  -3.687  1.00 11.91 ? 204 VAL A CG2 1 
ATOM   1681 N N   . LEU A 1 205 ? 12.920 13.831  -7.961  1.00 11.62 ? 205 LEU A N   1 
ATOM   1682 C CA  . LEU A 1 205 ? 13.080 13.980  -9.409  1.00 11.61 ? 205 LEU A CA  1 
ATOM   1683 C C   . LEU A 1 205 ? 12.439 12.817  -10.129 1.00 12.03 ? 205 LEU A C   1 
ATOM   1684 O O   . LEU A 1 205 ? 11.742 13.024  -11.120 1.00 11.50 ? 205 LEU A O   1 
ATOM   1685 C CB  . LEU A 1 205 ? 14.560 14.080  -9.785  1.00 11.82 ? 205 LEU A CB  1 
ATOM   1686 C CG  . LEU A 1 205 ? 15.223 15.375  -9.349  1.00 12.51 ? 205 LEU A CG  1 
ATOM   1687 C CD1 . LEU A 1 205 ? 16.733 15.246  -9.360  1.00 13.36 ? 205 LEU A CD1 1 
ATOM   1688 C CD2 . LEU A 1 205 ? 14.733 16.542  -10.186 1.00 13.75 ? 205 LEU A CD2 1 
ATOM   1689 N N   . ALA A 1 206 ? 12.630 11.587  -9.620  1.00 12.01 ? 206 ALA A N   1 
ATOM   1690 C CA  . ALA A 1 206 ? 12.019 10.411  -10.254 1.00 12.58 ? 206 ALA A CA  1 
ATOM   1691 C C   . ALA A 1 206 ? 10.483 10.546  -10.260 1.00 13.06 ? 206 ALA A C   1 
ATOM   1692 O O   . ALA A 1 206 ? 9.841  10.284  -11.270 1.00 12.97 ? 206 ALA A O   1 
ATOM   1693 C CB  . ALA A 1 206 ? 12.426 9.154   -9.509  1.00 13.02 ? 206 ALA A CB  1 
ATOM   1694 N N   . TRP A 1 207 ? 9.924  11.046  -9.151  1.00 12.31 ? 207 TRP A N   1 
ATOM   1695 C CA  . TRP A 1 207 ? 8.484  11.237  -9.044  1.00 12.72 ? 207 TRP A CA  1 
ATOM   1696 C C   . TRP A 1 207 ? 7.993  12.353  -9.993  1.00 12.88 ? 207 TRP A C   1 
ATOM   1697 O O   . TRP A 1 207 ? 6.919  12.226  -10.565 1.00 13.64 ? 207 TRP A O   1 
ATOM   1698 C CB  . TRP A 1 207 ? 8.134  11.468  -7.574  1.00 13.10 ? 207 TRP A CB  1 
ATOM   1699 C CG  . TRP A 1 207 ? 6.764  11.990  -7.302  1.00 13.61 ? 207 TRP A CG  1 
ATOM   1700 C CD1 . TRP A 1 207 ? 5.613  11.271  -7.141  1.00 14.89 ? 207 TRP A CD1 1 
ATOM   1701 C CD2 . TRP A 1 207 ? 6.432  13.349  -7.037  1.00 13.53 ? 207 TRP A CD2 1 
ATOM   1702 N NE1 . TRP A 1 207 ? 4.581  12.114  -6.796  1.00 15.38 ? 207 TRP A NE1 1 
ATOM   1703 C CE2 . TRP A 1 207 ? 5.061  13.396  -6.721  1.00 14.69 ? 207 TRP A CE2 1 
ATOM   1704 C CE3 . TRP A 1 207 ? 7.177  14.530  -6.990  1.00 14.59 ? 207 TRP A CE3 1 
ATOM   1705 C CZ2 . TRP A 1 207 ? 4.421  14.585  -6.382  1.00 15.53 ? 207 TRP A CZ2 1 
ATOM   1706 C CZ3 . TRP A 1 207 ? 6.536  15.709  -6.670  1.00 15.61 ? 207 TRP A CZ3 1 
ATOM   1707 C CH2 . TRP A 1 207 ? 5.175  15.729  -6.384  1.00 15.54 ? 207 TRP A CH2 1 
ATOM   1708 N N   . LEU A 1 208 ? 8.814  13.381  -10.235 1.00 12.37 ? 208 LEU A N   1 
ATOM   1709 C CA  . LEU A 1 208 ? 8.452  14.412  -11.218 1.00 12.13 ? 208 LEU A CA  1 
ATOM   1710 C C   . LEU A 1 208 ? 8.433  13.799  -12.619 1.00 12.89 ? 208 LEU A C   1 
ATOM   1711 O O   . LEU A 1 208 ? 7.538  14.110  -13.409 1.00 13.49 ? 208 LEU A O   1 
ATOM   1712 C CB  . LEU A 1 208 ? 9.446  15.566  -11.142 1.00 11.68 ? 208 LEU A CB  1 
ATOM   1713 C CG  . LEU A 1 208 ? 9.330  16.445  -9.891  1.00 13.13 ? 208 LEU A CG  1 
ATOM   1714 C CD1 . LEU A 1 208 ? 10.419 17.506  -9.884  1.00 13.35 ? 208 LEU A CD1 1 
ATOM   1715 C CD2 . LEU A 1 208 ? 7.956  17.130  -9.824  1.00 13.49 ? 208 LEU A CD2 1 
ATOM   1716 N N   . TYR A 1 209 ? 9.367  12.870  -12.916 1.00 12.85 ? 209 TYR A N   1 
ATOM   1717 C CA  . TYR A 1 209 ? 9.341  12.143  -14.193 1.00 13.30 ? 209 TYR A CA  1 
ATOM   1718 C C   . TYR A 1 209 ? 8.069  11.310  -14.283 1.00 14.51 ? 209 TYR A C   1 
ATOM   1719 O O   . TYR A 1 209 ? 7.423  11.315  -15.316 1.00 15.06 ? 209 TYR A O   1 
ATOM   1720 C CB  . TYR A 1 209 ? 10.556 11.234  -14.364 1.00 12.99 ? 209 TYR A CB  1 
ATOM   1721 C CG  . TYR A 1 209 ? 11.758 11.992  -14.871 1.00 13.05 ? 209 TYR A CG  1 
ATOM   1722 C CD1 . TYR A 1 209 ? 11.814 12.446  -16.178 1.00 13.88 ? 209 TYR A CD1 1 
ATOM   1723 C CD2 . TYR A 1 209 ? 12.843 12.240  -14.048 1.00 13.62 ? 209 TYR A CD2 1 
ATOM   1724 C CE1 . TYR A 1 209 ? 12.907 13.155  -16.649 1.00 14.59 ? 209 TYR A CE1 1 
ATOM   1725 C CE2 . TYR A 1 209 ? 13.943 12.953  -14.506 1.00 14.55 ? 209 TYR A CE2 1 
ATOM   1726 C CZ  . TYR A 1 209 ? 13.975 13.397  -15.814 1.00 14.96 ? 209 TYR A CZ  1 
ATOM   1727 O OH  . TYR A 1 209 ? 15.049 14.115  -16.279 1.00 16.11 ? 209 TYR A OH  1 
ATOM   1728 N N   . ALA A 1 210 ? 7.680  10.629  -13.183 1.00 14.89 ? 210 ALA A N   1 
ATOM   1729 C CA  . ALA A 1 210 ? 6.429  9.851   -13.171 1.00 15.35 ? 210 ALA A CA  1 
ATOM   1730 C C   . ALA A 1 210 ? 5.231  10.755  -13.445 1.00 16.18 ? 210 ALA A C   1 
ATOM   1731 O O   . ALA A 1 210 ? 4.309  10.368  -14.163 1.00 16.64 ? 210 ALA A O   1 
ATOM   1732 C CB  . ALA A 1 210 ? 6.246  9.164   -11.820 1.00 15.41 ? 210 ALA A CB  1 
ATOM   1733 N N   . ALA A 1 211 ? 5.247  11.971  -12.900 1.00 15.83 ? 211 ALA A N   1 
ATOM   1734 C CA  . ALA A 1 211 ? 4.178  12.927  -13.105 1.00 15.93 ? 211 ALA A CA  1 
ATOM   1735 C C   . ALA A 1 211 ? 4.077  13.306  -14.578 1.00 16.27 ? 211 ALA A C   1 
ATOM   1736 O O   . ALA A 1 211 ? 2.978  13.279  -15.138 1.00 17.39 ? 211 ALA A O   1 
ATOM   1737 C CB  . ALA A 1 211 ? 4.407  14.152  -12.240 1.00 16.23 ? 211 ALA A CB  1 
ATOM   1738 N N   . VAL A 1 212 ? 5.210  13.588  -15.237 1.00 15.64 ? 212 VAL A N   1 
ATOM   1739 C CA  . VAL A 1 212 ? 5.187  13.927  -16.663 1.00 16.48 ? 212 VAL A CA  1 
ATOM   1740 C C   . VAL A 1 212 ? 4.654  12.777  -17.487 1.00 18.29 ? 212 VAL A C   1 
ATOM   1741 O O   . VAL A 1 212 ? 3.796  12.996  -18.351 1.00 19.31 ? 212 VAL A O   1 
ATOM   1742 C CB  . VAL A 1 212 ? 6.574  14.389  -17.150 1.00 16.59 ? 212 VAL A CB  1 
ATOM   1743 C CG1 . VAL A 1 212 ? 6.583  14.581  -18.668 1.00 16.85 ? 212 VAL A CG1 1 
ATOM   1744 C CG2 . VAL A 1 212 ? 6.969  15.674  -16.451 1.00 17.06 ? 212 VAL A CG2 1 
ATOM   1745 N N   . ILE A 1 213 ? 5.112  11.552  -17.202 1.00 19.03 ? 213 ILE A N   1 
ATOM   1746 C CA  . ILE A 1 213 ? 4.654  10.357  -17.930 1.00 20.91 ? 213 ILE A CA  1 
ATOM   1747 C C   . ILE A 1 213 ? 3.142  10.195  -17.791 1.00 23.56 ? 213 ILE A C   1 
ATOM   1748 O O   . ILE A 1 213 ? 2.457  9.941   -18.777 1.00 24.76 ? 213 ILE A O   1 
ATOM   1749 C CB  . ILE A 1 213 ? 5.416  9.109   -17.418 1.00 21.25 ? 213 ILE A CB  1 
ATOM   1750 C CG1 . ILE A 1 213 ? 6.904  9.189   -17.803 1.00 21.73 ? 213 ILE A CG1 1 
ATOM   1751 C CG2 . ILE A 1 213 ? 4.783  7.803   -17.918 1.00 21.99 ? 213 ILE A CG2 1 
ATOM   1752 C CD1 . ILE A 1 213 ? 7.788  8.246   -17.083 1.00 22.87 ? 213 ILE A CD1 1 
ATOM   1753 N N   . ASN A 1 214 ? 2.620  10.439  -16.588 1.00 24.22 ? 214 ASN A N   1 
ATOM   1754 C CA  . ASN A 1 214 ? 1.204  10.282  -16.300 1.00 26.05 ? 214 ASN A CA  1 
ATOM   1755 C C   . ASN A 1 214 ? 0.343  11.544  -16.522 1.00 27.69 ? 214 ASN A C   1 
ATOM   1756 O O   . ASN A 1 214 ? -0.799 11.581  -16.055 1.00 29.91 ? 214 ASN A O   1 
ATOM   1757 C CB  . ASN A 1 214 ? 1.016  9.716   -14.899 1.00 27.31 ? 214 ASN A CB  1 
ATOM   1758 C CG  . ASN A 1 214 ? 1.479  8.279   -14.822 1.00 30.24 ? 214 ASN A CG  1 
ATOM   1759 O OD1 . ASN A 1 214 ? 0.744  7.346   -15.163 1.00 32.47 ? 214 ASN A OD1 1 
ATOM   1760 N ND2 . ASN A 1 214 ? 2.714  8.047   -14.430 1.00 29.78 ? 214 ASN A ND2 1 
ATOM   1761 N N   . GLY A 1 215 ? 0.848  12.529  -17.260 1.00 26.51 ? 215 GLY A N   1 
ATOM   1762 C CA  . GLY A 1 215 ? 0.065  13.709  -17.623 1.00 26.05 ? 215 GLY A CA  1 
ATOM   1763 C C   . GLY A 1 215 ? 0.186  15.021  -16.870 1.00 24.55 ? 215 GLY A C   1 
ATOM   1764 O O   . GLY A 1 215 ? -0.239 16.059  -17.380 1.00 25.20 ? 215 GLY A O   1 
ATOM   1765 N N   A ASP A 1 216 ? 0.744  14.999  -15.654 0.50 23.04 ? 216 ASP A N   1 
ATOM   1766 N N   B ASP A 1 216 ? 0.748  14.992  -15.660 0.50 23.39 ? 216 ASP A N   1 
ATOM   1767 C CA  A ASP A 1 216 ? 0.891  16.222  -14.868 0.50 22.25 ? 216 ASP A CA  1 
ATOM   1768 C CA  B ASP A 1 216 ? 0.909  16.203  -14.862 0.50 22.94 ? 216 ASP A CA  1 
ATOM   1769 C C   A ASP A 1 216 ? 2.182  16.909  -15.280 0.50 22.70 ? 216 ASP A C   1 
ATOM   1770 C C   B ASP A 1 216 ? 2.192  16.893  -15.307 0.50 23.02 ? 216 ASP A C   1 
ATOM   1771 O O   A ASP A 1 216 ? 3.265  16.409  -14.988 0.50 23.46 ? 216 ASP A O   1 
ATOM   1772 O O   B ASP A 1 216 ? 3.280  16.379  -15.060 0.50 23.77 ? 216 ASP A O   1 
ATOM   1773 C CB  A ASP A 1 216 ? 0.863  15.910  -13.369 0.50 22.37 ? 216 ASP A CB  1 
ATOM   1774 C CB  B ASP A 1 216 ? 0.959  15.849  -13.368 0.50 24.09 ? 216 ASP A CB  1 
ATOM   1775 C CG  A ASP A 1 216 ? -0.442 15.298  -12.907 0.50 24.19 ? 216 ASP A CG  1 
ATOM   1776 C CG  B ASP A 1 216 ? -0.170 16.456  -12.563 0.50 27.89 ? 216 ASP A CG  1 
ATOM   1777 O OD1 A ASP A 1 216 ? -1.477 15.540  -13.561 0.50 24.19 ? 216 ASP A OD1 1 
ATOM   1778 O OD1 B ASP A 1 216 ? -0.595 17.580  -12.895 0.50 28.66 ? 216 ASP A OD1 1 
ATOM   1779 O OD2 A ASP A 1 216 ? -0.430 14.579  -11.889 0.50 25.07 ? 216 ASP A OD2 1 
ATOM   1780 O OD2 B ASP A 1 216 ? -0.618 15.812  -11.589 0.50 29.52 ? 216 ASP A OD2 1 
ATOM   1781 N N   . ARG A 1 217 ? 2.073  18.016  -16.019 1.00 21.99 ? 217 ARG A N   1 
ATOM   1782 C CA  . ARG A 1 217 ? 3.233  18.713  -16.564 1.00 20.81 ? 217 ARG A CA  1 
ATOM   1783 C C   . ARG A 1 217 ? 3.263  20.218  -16.299 1.00 19.92 ? 217 ARG A C   1 
ATOM   1784 O O   . ARG A 1 217 ? 4.105  20.898  -16.881 1.00 19.51 ? 217 ARG A O   1 
ATOM   1785 C CB  . ARG A 1 217 ? 3.252  18.535  -18.107 0.50 21.37 ? 217 ARG A CB  1 
ATOM   1786 C CG  . ARG A 1 217 ? 2.978  17.127  -18.645 0.50 23.57 ? 217 ARG A CG  1 
ATOM   1787 C CD  . ARG A 1 217 ? 2.523  17.152  -20.100 0.50 25.14 ? 217 ARG A CD  1 
ATOM   1788 N NE  . ARG A 1 217 ? 3.525  17.746  -20.981 0.50 25.70 ? 217 ARG A NE  1 
ATOM   1789 C CZ  . ARG A 1 217 ? 4.427  17.041  -21.650 0.50 25.29 ? 217 ARG A CZ  1 
ATOM   1790 N NH1 . ARG A 1 217 ? 5.318  17.652  -22.418 0.50 24.48 ? 217 ARG A NH1 1 
ATOM   1791 N NH2 . ARG A 1 217 ? 4.448  15.719  -21.555 0.50 23.66 ? 217 ARG A NH2 1 
ATOM   1792 N N   . TRP A 1 218 ? 2.347  20.759  -15.483 1.00 19.50 ? 218 TRP A N   1 
ATOM   1793 C CA  . TRP A 1 218 ? 2.290  22.214  -15.276 1.00 19.27 ? 218 TRP A CA  1 
ATOM   1794 C C   . TRP A 1 218 ? 3.589  22.829  -14.740 1.00 19.18 ? 218 TRP A C   1 
ATOM   1795 O O   . TRP A 1 218 ? 3.833  24.006  -14.958 1.00 19.69 ? 218 TRP A O   1 
ATOM   1796 C CB  . TRP A 1 218 ? 1.102  22.617  -14.384 1.00 19.08 ? 218 TRP A CB  1 
ATOM   1797 C CG  . TRP A 1 218 ? 1.172  22.070  -12.987 1.00 18.92 ? 218 TRP A CG  1 
ATOM   1798 C CD1 . TRP A 1 218 ? 0.547  20.956  -12.513 1.00 19.63 ? 218 TRP A CD1 1 
ATOM   1799 C CD2 . TRP A 1 218 ? 1.858  22.655  -11.864 1.00 19.21 ? 218 TRP A CD2 1 
ATOM   1800 N NE1 . TRP A 1 218 ? 0.866  20.766  -11.187 1.00 19.83 ? 218 TRP A NE1 1 
ATOM   1801 C CE2 . TRP A 1 218 ? 1.651  21.805  -10.761 1.00 19.68 ? 218 TRP A CE2 1 
ATOM   1802 C CE3 . TRP A 1 218 ? 2.647  23.803  -11.692 1.00 19.71 ? 218 TRP A CE3 1 
ATOM   1803 C CZ2 . TRP A 1 218 ? 2.230  22.048  -9.514  1.00 19.83 ? 218 TRP A CZ2 1 
ATOM   1804 C CZ3 . TRP A 1 218 ? 3.229  24.034  -10.460 1.00 20.19 ? 218 TRP A CZ3 1 
ATOM   1805 C CH2 . TRP A 1 218 ? 3.000  23.174  -9.383  1.00 20.04 ? 218 TRP A CH2 1 
ATOM   1806 N N   . PHE A 1 219 ? 4.383  22.040  -14.003 1.00 18.30 ? 219 PHE A N   1 
ATOM   1807 C CA  . PHE A 1 219 ? 5.624  22.483  -13.356 1.00 17.79 ? 219 PHE A CA  1 
ATOM   1808 C C   . PHE A 1 219 ? 6.842  22.530  -14.276 1.00 18.51 ? 219 PHE A C   1 
ATOM   1809 O O   . PHE A 1 219 ? 7.911  22.994  -13.861 1.00 18.69 ? 219 PHE A O   1 
ATOM   1810 C CB  . PHE A 1 219 ? 5.920  21.590  -12.136 1.00 16.65 ? 219 PHE A CB  1 
ATOM   1811 C CG  . PHE A 1 219 ? 5.997  20.133  -12.506 1.00 15.65 ? 219 PHE A CG  1 
ATOM   1812 C CD1 . PHE A 1 219 ? 7.163  19.591  -13.018 1.00 15.83 ? 219 PHE A CD1 1 
ATOM   1813 C CD2 . PHE A 1 219 ? 4.885  19.316  -12.400 1.00 15.39 ? 219 PHE A CD2 1 
ATOM   1814 C CE1 . PHE A 1 219 ? 7.210  18.266  -13.417 1.00 15.82 ? 219 PHE A CE1 1 
ATOM   1815 C CE2 . PHE A 1 219 ? 4.956  17.985  -12.749 1.00 15.80 ? 219 PHE A CE2 1 
ATOM   1816 C CZ  . PHE A 1 219 ? 6.103  17.475  -13.293 1.00 15.51 ? 219 PHE A CZ  1 
ATOM   1817 N N   . LEU A 1 220 ? 6.703  22.044  -15.520 1.00 18.09 ? 220 LEU A N   1 
ATOM   1818 C CA  . LEU A 1 220 ? 7.800  22.117  -16.472 1.00 19.03 ? 220 LEU A CA  1 
ATOM   1819 C C   . LEU A 1 220 ? 7.971  23.571  -16.859 1.00 20.12 ? 220 LEU A C   1 
ATOM   1820 O O   . LEU A 1 220 ? 6.988  24.309  -16.991 1.00 20.85 ? 220 LEU A O   1 
ATOM   1821 C CB  . LEU A 1 220 ? 7.525  21.266  -17.709 1.00 19.05 ? 220 LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 220 ? 7.424  19.768  -17.467 1.00 19.56 ? 220 LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 220 ? 7.122  19.044  -18.764 1.00 19.47 ? 220 LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 220 ? 8.694  19.212  -16.777 1.00 20.00 ? 220 LEU A CD2 1 
ATOM   1825 N N   . ASN A 1 221 ? 9.214  23.996  -16.965 1.00 20.10 ? 221 ASN A N   1 
ATOM   1826 C CA  . ASN A 1 221 ? 9.510  25.383  -17.252 1.00 20.10 ? 221 ASN A CA  1 
ATOM   1827 C C   . ASN A 1 221 ? 10.545 25.542  -18.362 1.00 19.74 ? 221 ASN A C   1 
ATOM   1828 O O   . ASN A 1 221 ? 11.001 24.563  -18.944 1.00 20.14 ? 221 ASN A O   1 
ATOM   1829 C CB  . ASN A 1 221 ? 9.905  26.097  -15.960 1.00 20.92 ? 221 ASN A CB  1 
ATOM   1830 C CG  . ASN A 1 221 ? 11.146 25.546  -15.329 1.00 23.14 ? 221 ASN A CG  1 
ATOM   1831 O OD1 . ASN A 1 221 ? 12.101 25.106  -15.998 1.00 22.57 ? 221 ASN A OD1 1 
ATOM   1832 N ND2 . ASN A 1 221 ? 11.167 25.582  -14.017 1.00 23.81 ? 221 ASN A ND2 1 
ATOM   1833 N N   . ARG A 1 222 ? 10.877 26.784  -18.683 1.00 18.88 ? 222 ARG A N   1 
ATOM   1834 C CA  . ARG A 1 222 ? 11.832 27.102  -19.726 1.00 18.93 ? 222 ARG A CA  1 
ATOM   1835 C C   . ARG A 1 222 ? 13.271 27.127  -19.238 1.00 18.41 ? 222 ARG A C   1 
ATOM   1836 O O   . ARG A 1 222 ? 14.134 27.579  -19.982 1.00 18.72 ? 222 ARG A O   1 
ATOM   1837 C CB  . ARG A 1 222 ? 11.491 28.498  -20.253 1.00 20.02 ? 222 ARG A CB  1 
ATOM   1838 C CG  . ARG A 1 222 ? 10.094 28.584  -20.823 1.00 23.44 ? 222 ARG A CG  1 
ATOM   1839 C CD  . ARG A 1 222 ? 9.746  29.989  -21.277 1.00 26.45 ? 222 ARG A CD  1 
ATOM   1840 N NE  . ARG A 1 222 ? 8.499  29.999  -22.037 1.00 28.59 ? 222 ARG A NE  1 
ATOM   1841 C CZ  . ARG A 1 222 ? 8.402  29.730  -23.335 1.00 31.63 ? 222 ARG A CZ  1 
ATOM   1842 N NH1 . ARG A 1 222 ? 9.488  29.449  -24.047 1.00 31.12 ? 222 ARG A NH1 1 
ATOM   1843 N NH2 . ARG A 1 222 ? 7.218  29.741  -23.933 1.00 31.84 ? 222 ARG A NH2 1 
ATOM   1844 N N   . PHE A 1 223 ? 13.552 26.663  -18.016 1.00 17.24 ? 223 PHE A N   1 
ATOM   1845 C CA  . PHE A 1 223 ? 14.877 26.810  -17.437 1.00 17.43 ? 223 PHE A CA  1 
ATOM   1846 C C   . PHE A 1 223 ? 15.704 25.551  -17.362 1.00 15.35 ? 223 PHE A C   1 
ATOM   1847 O O   . PHE A 1 223 ? 15.192 24.438  -17.466 1.00 15.55 ? 223 PHE A O   1 
ATOM   1848 C CB  . PHE A 1 223 ? 14.761 27.413  -16.009 1.00 18.71 ? 223 PHE A CB  1 
ATOM   1849 C CG  . PHE A 1 223 ? 13.758 28.531  -15.821 1.00 20.74 ? 223 PHE A CG  1 
ATOM   1850 C CD1 . PHE A 1 223 ? 13.624 29.530  -16.768 1.00 22.13 ? 223 PHE A CD1 1 
ATOM   1851 C CD2 . PHE A 1 223 ? 12.977 28.595  -14.684 1.00 22.23 ? 223 PHE A CD2 1 
ATOM   1852 C CE1 . PHE A 1 223 ? 12.696 30.547  -16.598 1.00 23.38 ? 223 PHE A CE1 1 
ATOM   1853 C CE2 . PHE A 1 223 ? 12.071 29.627  -14.501 1.00 23.56 ? 223 PHE A CE2 1 
ATOM   1854 C CZ  . PHE A 1 223 ? 11.935 30.596  -15.459 1.00 23.59 ? 223 PHE A CZ  1 
ATOM   1855 N N   . THR A 1 224 ? 17.002 25.743  -17.157 1.00 14.22 ? 224 THR A N   1 
ATOM   1856 C CA  . THR A 1 224 ? 17.923 24.681  -16.819 1.00 13.87 ? 224 THR A CA  1 
ATOM   1857 C C   . THR A 1 224 ? 18.777 25.156  -15.619 1.00 14.09 ? 224 THR A C   1 
ATOM   1858 O O   . THR A 1 224 ? 18.645 26.293  -15.133 1.00 14.76 ? 224 THR A O   1 
ATOM   1859 C CB  . THR A 1 224 ? 18.695 24.154  -18.032 1.00 14.52 ? 224 THR A CB  1 
ATOM   1860 O OG1 . THR A 1 224 ? 19.214 22.865  -17.666 1.00 14.05 ? 224 THR A OG1 1 
ATOM   1861 C CG2 . THR A 1 224 ? 19.849 25.052  -18.412 1.00 14.98 ? 224 THR A CG2 1 
ATOM   1862 N N   . THR A 1 225 ? 19.601 24.275  -15.099 1.00 13.19 ? 225 THR A N   1 
ATOM   1863 C CA  . THR A 1 225 ? 20.500 24.563  -14.003 1.00 13.50 ? 225 THR A CA  1 
ATOM   1864 C C   . THR A 1 225 ? 21.729 23.647  -14.160 1.00 13.55 ? 225 THR A C   1 
ATOM   1865 O O   . THR A 1 225 ? 21.844 22.918  -15.145 1.00 13.01 ? 225 THR A O   1 
ATOM   1866 C CB  . THR A 1 225 ? 19.759 24.407  -12.648 1.00 15.53 ? 225 THR A CB  1 
ATOM   1867 O OG1 . THR A 1 225 ? 20.659 24.812  -11.628 1.00 17.08 ? 225 THR A OG1 1 
ATOM   1868 C CG2 . THR A 1 225 ? 19.333 22.975  -12.374 1.00 16.36 ? 225 THR A CG2 1 
ATOM   1869 N N   . THR A 1 226 ? 22.671 23.746  -13.226 1.00 13.79 ? 226 THR A N   1 
ATOM   1870 C CA  . THR A 1 226 ? 23.834 22.885  -13.142 1.00 13.97 ? 226 THR A CA  1 
ATOM   1871 C C   . THR A 1 226 ? 23.718 22.116  -11.827 1.00 14.17 ? 226 THR A C   1 
ATOM   1872 O O   . THR A 1 226 ? 22.936 22.501  -10.957 1.00 13.64 ? 226 THR A O   1 
ATOM   1873 C CB  . THR A 1 226 ? 25.130 23.738  -13.146 1.00 16.08 ? 226 THR A CB  1 
ATOM   1874 O OG1 . THR A 1 226 ? 25.192 24.499  -11.938 1.00 16.64 ? 226 THR A OG1 1 
ATOM   1875 C CG2 . THR A 1 226 ? 25.245 24.618  -14.361 1.00 17.33 ? 226 THR A CG2 1 
ATOM   1876 N N   A LEU A 1 227 ? 24.519 21.061  -11.653 0.50 14.30 ? 227 LEU A N   1 
ATOM   1877 N N   B LEU A 1 227 ? 24.524 21.056  -11.640 0.50 14.01 ? 227 LEU A N   1 
ATOM   1878 C CA  A LEU A 1 227 ? 24.520 20.302  -10.408 0.50 15.27 ? 227 LEU A CA  1 
ATOM   1879 C CA  B LEU A 1 227 ? 24.508 20.322  -10.373 0.50 14.69 ? 227 LEU A CA  1 
ATOM   1880 C C   A LEU A 1 227 ? 24.897 21.190  -9.216  0.50 15.82 ? 227 LEU A C   1 
ATOM   1881 C C   B LEU A 1 227 ? 24.873 21.224  -9.206  0.50 15.51 ? 227 LEU A C   1 
ATOM   1882 O O   A LEU A 1 227 ? 24.223 21.149  -8.192  0.50 16.27 ? 227 LEU A O   1 
ATOM   1883 O O   B LEU A 1 227 ? 24.172 21.226  -8.197  0.50 15.90 ? 227 LEU A O   1 
ATOM   1884 C CB  A LEU A 1 227 ? 25.476 19.108  -10.535 0.50 15.64 ? 227 LEU A CB  1 
ATOM   1885 C CB  B LEU A 1 227 ? 25.440 19.112  -10.410 0.50 14.62 ? 227 LEU A CB  1 
ATOM   1886 C CG  A LEU A 1 227 ? 25.138 17.847  -9.735  0.50 17.11 ? 227 LEU A CG  1 
ATOM   1887 C CG  B LEU A 1 227 ? 24.906 17.875  -11.109 0.50 15.35 ? 227 LEU A CG  1 
ATOM   1888 C CD1 A LEU A 1 227 ? 23.676 17.439  -9.907  0.50 17.60 ? 227 LEU A CD1 1 
ATOM   1889 C CD1 B LEU A 1 227 ? 25.881 16.725  -10.955 0.50 15.25 ? 227 LEU A CD1 1 
ATOM   1890 C CD2 A LEU A 1 227 ? 26.019 16.702  -10.161 0.50 17.33 ? 227 LEU A CD2 1 
ATOM   1891 C CD2 B LEU A 1 227 ? 23.531 17.463  -10.562 0.50 15.94 ? 227 LEU A CD2 1 
ATOM   1892 N N   . ASN A 1 228 ? 25.916 22.051  -9.374  1.00 15.51 ? 228 ASN A N   1 
ATOM   1893 C CA  . ASN A 1 228 ? 26.326 22.950  -8.300  1.00 15.00 ? 228 ASN A CA  1 
ATOM   1894 C C   . ASN A 1 228 ? 25.286 24.033  -7.986  1.00 14.90 ? 228 ASN A C   1 
ATOM   1895 O O   . ASN A 1 228 ? 25.056 24.317  -6.813  1.00 15.98 ? 228 ASN A O   1 
ATOM   1896 C CB  . ASN A 1 228 ? 27.700 23.551  -8.581  1.00 15.85 ? 228 ASN A CB  1 
ATOM   1897 C CG  . ASN A 1 228 ? 28.840 22.550  -8.522  1.00 19.59 ? 228 ASN A CG  1 
ATOM   1898 O OD1 . ASN A 1 228 ? 29.929 22.794  -9.060  1.00 21.73 ? 228 ASN A OD1 1 
ATOM   1899 N ND2 . ASN A 1 228 ? 28.635 21.411  -7.881  1.00 20.10 ? 228 ASN A ND2 1 
ATOM   1900 N N   . ASP A 1 229 ? 24.638 24.604  -9.002  1.00 14.47 ? 229 ASP A N   1 
ATOM   1901 C CA  . ASP A 1 229 ? 23.626 25.638  -8.756  1.00 14.83 ? 229 ASP A CA  1 
ATOM   1902 C C   . ASP A 1 229 ? 22.417 25.008  -8.087  1.00 15.00 ? 229 ASP A C   1 
ATOM   1903 O O   . ASP A 1 229 ? 21.915 25.535  -7.090  1.00 15.74 ? 229 ASP A O   1 
ATOM   1904 C CB  . ASP A 1 229 ? 23.213 26.348  -10.049 1.00 17.00 ? 229 ASP A CB  1 
ATOM   1905 C CG  . ASP A 1 229 ? 22.101 27.337  -9.811  1.00 23.28 ? 229 ASP A CG  1 
ATOM   1906 O OD1 . ASP A 1 229 ? 22.347 28.337  -9.109  1.00 25.03 ? 229 ASP A OD1 1 
ATOM   1907 O OD2 . ASP A 1 229 ? 20.957 27.068  -10.265 1.00 24.97 ? 229 ASP A OD2 1 
ATOM   1908 N N   . PHE A 1 230 ? 21.979 23.838  -8.584  1.00 14.41 ? 230 PHE A N   1 
ATOM   1909 C CA  . PHE A 1 230 ? 20.850 23.142  -7.980  1.00 14.40 ? 230 PHE A CA  1 
ATOM   1910 C C   . PHE A 1 230 ? 21.151 22.818  -6.516  1.00 15.23 ? 230 PHE A C   1 
ATOM   1911 O O   . PHE A 1 230 ? 20.308 23.067  -5.661  1.00 16.01 ? 230 PHE A O   1 
ATOM   1912 C CB  . PHE A 1 230 ? 20.527 21.845  -8.745  1.00 13.67 ? 230 PHE A CB  1 
ATOM   1913 C CG  . PHE A 1 230 ? 19.422 21.092  -8.049  1.00 14.69 ? 230 PHE A CG  1 
ATOM   1914 C CD1 . PHE A 1 230 ? 18.100 21.467  -8.213  1.00 15.26 ? 230 PHE A CD1 1 
ATOM   1915 C CD2 . PHE A 1 230 ? 19.715 20.119  -7.106  1.00 15.80 ? 230 PHE A CD2 1 
ATOM   1916 C CE1 . PHE A 1 230 ? 17.088 20.834  -7.504  1.00 16.46 ? 230 PHE A CE1 1 
ATOM   1917 C CE2 . PHE A 1 230 ? 18.704 19.520  -6.370  1.00 16.25 ? 230 PHE A CE2 1 
ATOM   1918 C CZ  . PHE A 1 230 ? 17.399 19.868  -6.589  1.00 16.71 ? 230 PHE A CZ  1 
ATOM   1919 N N   . ASN A 1 231 ? 22.374 22.361  -6.232  1.00 15.00 ? 231 ASN A N   1 
ATOM   1920 C CA  . ASN A 1 231 ? 22.758 22.003  -4.873  1.00 15.46 ? 231 ASN A CA  1 
ATOM   1921 C C   . ASN A 1 231 ? 22.802 23.158  -3.914  1.00 16.96 ? 231 ASN A C   1 
ATOM   1922 O O   . ASN A 1 231 ? 22.591 22.932  -2.725  1.00 17.72 ? 231 ASN A O   1 
ATOM   1923 C CB  . ASN A 1 231 ? 24.050 21.215  -4.849  1.00 16.36 ? 231 ASN A CB  1 
ATOM   1924 C CG  . ASN A 1 231 ? 23.829 19.796  -5.314  1.00 18.15 ? 231 ASN A CG  1 
ATOM   1925 O OD1 . ASN A 1 231 ? 22.721 19.254  -5.242  1.00 18.68 ? 231 ASN A OD1 1 
ATOM   1926 N ND2 . ASN A 1 231 ? 24.868 19.145  -5.804  1.00 19.47 ? 231 ASN A ND2 1 
ATOM   1927 N N   . LEU A 1 232 ? 22.976 24.394  -4.396  1.00 17.68 ? 232 LEU A N   1 
ATOM   1928 C CA  . LEU A 1 232 ? 22.885 25.567  -3.519  1.00 19.22 ? 232 LEU A CA  1 
ATOM   1929 C C   . LEU A 1 232 ? 21.437 25.670  -3.002  1.00 19.67 ? 232 LEU A C   1 
ATOM   1930 O O   . LEU A 1 232 ? 21.223 25.880  -1.806  1.00 20.80 ? 232 LEU A O   1 
ATOM   1931 C CB  . LEU A 1 232 ? 23.257 26.842  -4.289  1.00 20.79 ? 232 LEU A CB  1 
ATOM   1932 C CG  . LEU A 1 232 ? 24.717 26.974  -4.677  1.00 23.66 ? 232 LEU A CG  1 
ATOM   1933 C CD1 . LEU A 1 232 ? 24.933 28.250  -5.452  1.00 24.78 ? 232 LEU A CD1 1 
ATOM   1934 C CD2 . LEU A 1 232 ? 25.615 26.984  -3.447  1.00 24.66 ? 232 LEU A CD2 1 
ATOM   1935 N N   . VAL A 1 233 ? 20.459 25.417  -3.886  1.00 18.99 ? 233 VAL A N   1 
ATOM   1936 C CA  . VAL A 1 233 ? 19.045 25.406  -3.533  1.00 18.83 ? 233 VAL A CA  1 
ATOM   1937 C C   . VAL A 1 233 ? 18.700 24.193  -2.684  1.00 18.78 ? 233 VAL A C   1 
ATOM   1938 O O   . VAL A 1 233 ? 18.008 24.331  -1.675  1.00 19.12 ? 233 VAL A O   1 
ATOM   1939 C CB  . VAL A 1 233 ? 18.177 25.464  -4.804  1.00 20.10 ? 233 VAL A CB  1 
ATOM   1940 C CG1 . VAL A 1 233 ? 16.694 25.454  -4.446  1.00 20.95 ? 233 VAL A CG1 1 
ATOM   1941 C CG2 . VAL A 1 233 ? 18.525 26.699  -5.624  1.00 20.92 ? 233 VAL A CG2 1 
ATOM   1942 N N   . ALA A 1 234 ? 19.239 23.018  -3.016  1.00 18.51 ? 234 ALA A N   1 
ATOM   1943 C CA  . ALA A 1 234 ? 18.996 21.802  -2.227  1.00 19.45 ? 234 ALA A CA  1 
ATOM   1944 C C   . ALA A 1 234 ? 19.449 22.000  -0.771  1.00 20.44 ? 234 ALA A C   1 
ATOM   1945 O O   . ALA A 1 234 ? 18.700 21.699  0.153   1.00 20.35 ? 234 ALA A O   1 
ATOM   1946 C CB  . ALA A 1 234 ? 19.732 20.621  -2.849  1.00 19.88 ? 234 ALA A CB  1 
ATOM   1947 N N   . MET A 1 235 ? 20.620 22.616  -0.569  1.00 20.53 ? 235 MET A N   1 
ATOM   1948 C CA  . MET A 1 235 ? 21.139 22.894  0.770   1.00 21.06 ? 235 MET A CA  1 
ATOM   1949 C C   . MET A 1 235 ? 20.163 23.771  1.556   1.00 19.75 ? 235 MET A C   1 
ATOM   1950 O O   . MET A 1 235 ? 19.813 23.447  2.691   1.00 19.72 ? 235 MET A O   1 
ATOM   1951 C CB  . MET A 1 235 ? 22.522 23.574  0.668   1.00 23.60 ? 235 MET A CB  1 
ATOM   1952 C CG  . MET A 1 235 ? 23.037 24.121  1.984   1.00 29.30 ? 235 MET A CG  1 
ATOM   1953 S SD  . MET A 1 235 ? 24.257 23.025  2.705   1.00 42.88 ? 235 MET A SD  1 
ATOM   1954 C CE  . MET A 1 235 ? 25.589 23.247  1.552   1.00 39.42 ? 235 MET A CE  1 
ATOM   1955 N N   . LYS A 1 236 ? 19.700 24.853  0.927   1.00 18.47 ? 236 LYS A N   1 
ATOM   1956 C CA  . LYS A 1 236 ? 18.792 25.785  1.563   1.00 17.97 ? 236 LYS A CA  1 
ATOM   1957 C C   . LYS A 1 236 ? 17.493 25.121  2.014   1.00 17.43 ? 236 LYS A C   1 
ATOM   1958 O O   . LYS A 1 236 ? 16.951 25.470  3.058   1.00 18.51 ? 236 LYS A O   1 
ATOM   1959 C CB  . LYS A 1 236 ? 18.530 26.978  0.623   1.00 20.89 ? 236 LYS A CB  1 
ATOM   1960 C CG  . LYS A 1 236 ? 17.528 27.986  1.164   1.00 26.53 ? 236 LYS A CG  1 
ATOM   1961 C CD  . LYS A 1 236 ? 17.172 29.030  0.127   1.00 33.01 ? 236 LYS A CD  1 
ATOM   1962 C CE  . LYS A 1 236 ? 15.990 29.854  0.572   1.00 37.50 ? 236 LYS A CE  1 
ATOM   1963 N NZ  . LYS A 1 236 ? 16.358 30.835  1.631   1.00 40.05 ? 236 LYS A NZ  1 
ATOM   1964 N N   . TYR A 1 237 ? 17.020 24.124  1.260   1.00 15.66 ? 237 TYR A N   1 
ATOM   1965 C CA  . TYR A 1 237 ? 15.746 23.472  1.564   1.00 14.78 ? 237 TYR A CA  1 
ATOM   1966 C C   . TYR A 1 237 ? 15.852 22.109  2.238   1.00 14.96 ? 237 TYR A C   1 
ATOM   1967 O O   . TYR A 1 237 ? 14.861 21.366  2.262   1.00 15.72 ? 237 TYR A O   1 
ATOM   1968 C CB  . TYR A 1 237 ? 14.899 23.373  0.286   1.00 14.56 ? 237 TYR A CB  1 
ATOM   1969 C CG  . TYR A 1 237 ? 14.367 24.728  -0.118  1.00 15.63 ? 237 TYR A CG  1 
ATOM   1970 C CD1 . TYR A 1 237 ? 13.223 25.245  0.467   1.00 16.68 ? 237 TYR A CD1 1 
ATOM   1971 C CD2 . TYR A 1 237 ? 15.067 25.534  -1.005  1.00 16.39 ? 237 TYR A CD2 1 
ATOM   1972 C CE1 . TYR A 1 237 ? 12.778 26.527  0.169   1.00 17.54 ? 237 TYR A CE1 1 
ATOM   1973 C CE2 . TYR A 1 237 ? 14.617 26.808  -1.333  1.00 16.88 ? 237 TYR A CE2 1 
ATOM   1974 C CZ  . TYR A 1 237 ? 13.486 27.312  -0.721  1.00 18.39 ? 237 TYR A CZ  1 
ATOM   1975 O OH  . TYR A 1 237 ? 13.013 28.560  -1.046  1.00 19.90 ? 237 TYR A OH  1 
ATOM   1976 N N   A ASN A 1 238 ? 17.029 21.783  2.777   0.50 14.71 ? 238 ASN A N   1 
ATOM   1977 N N   B ASN A 1 238 ? 17.031 21.780  2.788   0.50 14.49 ? 238 ASN A N   1 
ATOM   1978 C CA  A ASN A 1 238 ? 17.254 20.514  3.458   0.50 15.20 ? 238 ASN A CA  1 
ATOM   1979 C CA  B ASN A 1 238 ? 17.284 20.504  3.467   0.50 14.74 ? 238 ASN A CA  1 
ATOM   1980 C C   A ASN A 1 238 ? 16.986 19.323  2.549   0.50 14.96 ? 238 ASN A C   1 
ATOM   1981 C C   B ASN A 1 238 ? 17.054 19.295  2.568   0.50 14.80 ? 238 ASN A C   1 
ATOM   1982 O O   A ASN A 1 238 ? 16.317 18.373  2.941   0.50 15.04 ? 238 ASN A O   1 
ATOM   1983 O O   B ASN A 1 238 ? 16.509 18.281  3.000   0.50 14.95 ? 238 ASN A O   1 
ATOM   1984 C CB  A ASN A 1 238 ? 16.460 20.437  4.761   0.50 17.13 ? 238 ASN A CB  1 
ATOM   1985 C CB  B ASN A 1 238 ? 16.506 20.379  4.782   0.50 15.99 ? 238 ASN A CB  1 
ATOM   1986 C CG  A ASN A 1 238 ? 16.882 21.508  5.733   0.50 21.05 ? 238 ASN A CG  1 
ATOM   1987 C CG  B ASN A 1 238 ? 17.068 21.220  5.903   0.50 18.49 ? 238 ASN A CG  1 
ATOM   1988 O OD1 A ASN A 1 238 ? 16.104 22.393  6.115   0.50 22.39 ? 238 ASN A OD1 1 
ATOM   1989 O OD1 B ASN A 1 238 ? 18.118 21.861  5.772   0.50 18.96 ? 238 ASN A OD1 1 
ATOM   1990 N ND2 A ASN A 1 238 ? 18.142 21.469  6.126   0.50 21.55 ? 238 ASN A ND2 1 
ATOM   1991 N ND2 B ASN A 1 238 ? 16.368 21.244  7.026   0.50 19.10 ? 238 ASN A ND2 1 
ATOM   1992 N N   . TYR A 1 239 ? 17.462 19.417  1.309   1.00 14.63 ? 239 TYR A N   1 
ATOM   1993 C CA  . TYR A 1 239 ? 17.378 18.342  0.336   1.00 14.81 ? 239 TYR A CA  1 
ATOM   1994 C C   . TYR A 1 239 ? 18.779 17.746  0.260   1.00 15.52 ? 239 TYR A C   1 
ATOM   1995 O O   . TYR A 1 239 ? 19.769 18.452  0.460   1.00 16.11 ? 239 TYR A O   1 
ATOM   1996 C CB  . TYR A 1 239 ? 17.039 18.905  -1.050  1.00 14.64 ? 239 TYR A CB  1 
ATOM   1997 C CG  . TYR A 1 239 ? 15.569 18.840  -1.373  1.00 14.52 ? 239 TYR A CG  1 
ATOM   1998 C CD1 . TYR A 1 239 ? 14.637 19.491  -0.584  1.00 14.91 ? 239 TYR A CD1 1 
ATOM   1999 C CD2 . TYR A 1 239 ? 15.115 18.175  -2.502  1.00 14.55 ? 239 TYR A CD2 1 
ATOM   2000 C CE1 . TYR A 1 239 ? 13.281 19.426  -0.871  1.00 15.52 ? 239 TYR A CE1 1 
ATOM   2001 C CE2 . TYR A 1 239 ? 13.766 18.114  -2.809  1.00 15.01 ? 239 TYR A CE2 1 
ATOM   2002 C CZ  . TYR A 1 239 ? 12.850 18.743  -1.992  1.00 15.84 ? 239 TYR A CZ  1 
ATOM   2003 O OH  . TYR A 1 239 ? 11.509 18.631  -2.269  1.00 16.32 ? 239 TYR A OH  1 
ATOM   2004 N N   A GLU A 1 240 ? 18.870 16.448  -0.030  0.50 15.37 ? 240 GLU A N   1 
ATOM   2005 N N   B GLU A 1 240 ? 18.868 16.461  -0.067  0.50 15.60 ? 240 GLU A N   1 
ATOM   2006 C CA  A GLU A 1 240 ? 20.154 15.777  -0.186  0.50 16.23 ? 240 GLU A CA  1 
ATOM   2007 C CA  B GLU A 1 240 ? 20.151 15.796  -0.223  0.50 16.61 ? 240 GLU A CA  1 
ATOM   2008 C C   A GLU A 1 240 ? 20.879 16.322  -1.420  0.50 16.43 ? 240 GLU A C   1 
ATOM   2009 C C   B GLU A 1 240 ? 20.878 16.350  -1.428  0.50 16.61 ? 240 GLU A C   1 
ATOM   2010 O O   A GLU A 1 240 ? 20.244 16.585  -2.438  0.50 15.69 ? 240 GLU A O   1 
ATOM   2011 O O   B GLU A 1 240 ? 20.249 16.611  -2.453  0.50 15.86 ? 240 GLU A O   1 
ATOM   2012 C CB  A GLU A 1 240 ? 19.925 14.265  -0.355  0.50 18.78 ? 240 GLU A CB  1 
ATOM   2013 C CB  B GLU A 1 240 ? 19.929 14.302  -0.446  0.50 19.82 ? 240 GLU A CB  1 
ATOM   2014 C CG  A GLU A 1 240 ? 19.511 13.580  0.931   0.50 23.01 ? 240 GLU A CG  1 
ATOM   2015 C CG  B GLU A 1 240 ? 19.757 13.549  0.847   0.50 25.74 ? 240 GLU A CG  1 
ATOM   2016 C CD  A GLU A 1 240 ? 20.607 13.558  1.976   0.50 27.97 ? 240 GLU A CD  1 
ATOM   2017 C CD  B GLU A 1 240 ? 19.839 12.057  0.654   0.50 32.83 ? 240 GLU A CD  1 
ATOM   2018 O OE1 A GLU A 1 240 ? 21.558 12.757  1.825   0.50 28.30 ? 240 GLU A OE1 1 
ATOM   2019 O OE1 B GLU A 1 240 ? 19.029 11.520  -0.134  0.50 34.72 ? 240 GLU A OE1 1 
ATOM   2020 O OE2 A GLU A 1 240 ? 20.521 14.346  2.943   0.50 29.56 ? 240 GLU A OE2 1 
ATOM   2021 O OE2 B GLU A 1 240 ? 20.715 11.421  1.281   0.50 35.82 ? 240 GLU A OE2 1 
ATOM   2022 N N   . PRO A 1 241 ? 22.205 16.501  -1.358  1.00 17.14 ? 241 PRO A N   1 
ATOM   2023 C CA  . PRO A 1 241 ? 22.942 16.989  -2.541  1.00 18.08 ? 241 PRO A CA  1 
ATOM   2024 C C   . PRO A 1 241 ? 22.812 15.998  -3.698  1.00 17.98 ? 241 PRO A C   1 
ATOM   2025 O O   . PRO A 1 241 ? 22.874 14.796  -3.468  1.00 18.99 ? 241 PRO A O   1 
ATOM   2026 C CB  . PRO A 1 241 ? 24.400 17.037  -2.063  1.00 19.59 ? 241 PRO A CB  1 
ATOM   2027 C CG  . PRO A 1 241 ? 24.323 17.034  -0.568  1.00 19.93 ? 241 PRO A CG  1 
ATOM   2028 C CD  . PRO A 1 241 ? 23.111 16.247  -0.217  1.00 17.24 ? 241 PRO A CD  1 
ATOM   2029 N N   . LEU A 1 242 ? 22.540 16.485  -4.895  1.00 17.16 ? 242 LEU A N   1 
ATOM   2030 C CA  . LEU A 1 242 ? 22.418 15.624  -6.060  1.00 17.79 ? 242 LEU A CA  1 
ATOM   2031 C C   . LEU A 1 242 ? 23.822 15.392  -6.612  1.00 17.81 ? 242 LEU A C   1 
ATOM   2032 O O   . LEU A 1 242 ? 24.618 16.325  -6.735  1.00 17.96 ? 242 LEU A O   1 
ATOM   2033 C CB  . LEU A 1 242 ? 21.514 16.262  -7.115  1.00 18.10 ? 242 LEU A CB  1 
ATOM   2034 C CG  . LEU A 1 242 ? 20.945 15.279  -8.128  1.00 19.57 ? 242 LEU A CG  1 
ATOM   2035 C CD1 . LEU A 1 242 ? 19.885 14.396  -7.492  1.00 20.27 ? 242 LEU A CD1 1 
ATOM   2036 C CD2 . LEU A 1 242 ? 20.350 16.000  -9.280  1.00 19.83 ? 242 LEU A CD2 1 
ATOM   2037 N N   . THR A 1 243 ? 24.131 14.138  -6.881  1.00 18.16 ? 243 THR A N   1 
ATOM   2038 C CA  . THR A 1 243 ? 25.435 13.756  -7.399  1.00 18.67 ? 243 THR A CA  1 
ATOM   2039 C C   . THR A 1 243 ? 25.333 13.318  -8.861  1.00 19.12 ? 243 THR A C   1 
ATOM   2040 O O   . THR A 1 243 ? 24.223 13.074  -9.370  1.00 18.82 ? 243 THR A O   1 
ATOM   2041 C CB  . THR A 1 243 ? 26.018 12.618  -6.543  1.00 19.51 ? 243 THR A CB  1 
ATOM   2042 O OG1 . THR A 1 243 ? 25.257 11.425  -6.756  1.00 19.15 ? 243 THR A OG1 1 
ATOM   2043 C CG2 . THR A 1 243 ? 26.099 12.973  -5.073  1.00 20.65 ? 243 THR A CG2 1 
ATOM   2044 N N   . GLN A 1 244 ? 26.491 13.150  -9.526  1.00 19.36 ? 244 GLN A N   1 
ATOM   2045 C CA  . GLN A 1 244 ? 26.496 12.626  -10.886 1.00 19.60 ? 244 GLN A CA  1 
ATOM   2046 C C   . GLN A 1 244 ? 25.936 11.192  -10.896 1.00 19.31 ? 244 GLN A C   1 
ATOM   2047 O O   . GLN A 1 244 ? 25.228 10.841  -11.832 1.00 19.52 ? 244 GLN A O   1 
ATOM   2048 C CB  . GLN A 1 244 ? 27.908 12.662  -11.481 1.00 21.32 ? 244 GLN A CB  1 
ATOM   2049 C CG  . GLN A 1 244 ? 27.948 12.291  -12.963 1.00 24.67 ? 244 GLN A CG  1 
ATOM   2050 C CD  . GLN A 1 244 ? 27.099 13.215  -13.796 1.00 27.50 ? 244 GLN A CD  1 
ATOM   2051 O OE1 . GLN A 1 244 ? 27.194 14.445  -13.689 1.00 28.95 ? 244 GLN A OE1 1 
ATOM   2052 N NE2 . GLN A 1 244 ? 26.239 12.644  -14.629 1.00 26.25 ? 244 GLN A NE2 1 
ATOM   2053 N N   . ASP A 1 245 ? 26.150 10.409  -9.818  1.00 18.53 ? 245 ASP A N   1 
ATOM   2054 C CA  . ASP A 1 245 ? 25.574 9.066   -9.707  1.00 18.09 ? 245 ASP A CA  1 
ATOM   2055 C C   . ASP A 1 245 ? 24.045 9.134   -9.768  1.00 16.92 ? 245 ASP A C   1 
ATOM   2056 O O   . ASP A 1 245 ? 23.437 8.335   -10.466 1.00 17.01 ? 245 ASP A O   1 
ATOM   2057 C CB  . ASP A 1 245 ? 26.001 8.387   -8.399  1.00 20.87 ? 245 ASP A CB  1 
ATOM   2058 C CG  . ASP A 1 245 ? 27.274 7.574   -8.483  1.00 27.71 ? 245 ASP A CG  1 
ATOM   2059 O OD1 . ASP A 1 245 ? 28.003 7.709   -9.493  1.00 28.66 ? 245 ASP A OD1 1 
ATOM   2060 O OD2 . ASP A 1 245 ? 27.551 6.809   -7.530  1.00 30.69 ? 245 ASP A OD2 1 
ATOM   2061 N N   . HIS A 1 246 ? 23.429 10.114  -9.083  1.00 15.98 ? 246 HIS A N   1 
ATOM   2062 C CA  . HIS A 1 246 ? 21.969 10.269  -9.127  1.00 15.49 ? 246 HIS A CA  1 
ATOM   2063 C C   . HIS A 1 246 ? 21.504 10.639  -10.533 1.00 15.40 ? 246 HIS A C   1 
ATOM   2064 O O   . HIS A 1 246 ? 20.479 10.138  -10.994 1.00 15.05 ? 246 HIS A O   1 
ATOM   2065 C CB  . HIS A 1 246 ? 21.508 11.368  -8.176  1.00 15.78 ? 246 HIS A CB  1 
ATOM   2066 C CG  . HIS A 1 246 ? 21.770 11.078  -6.743  1.00 17.82 ? 246 HIS A CG  1 
ATOM   2067 N ND1 . HIS A 1 246 ? 22.203 12.070  -5.882  1.00 19.11 ? 246 HIS A ND1 1 
ATOM   2068 C CD2 . HIS A 1 246 ? 21.645 9.920   -6.061  1.00 19.14 ? 246 HIS A CD2 1 
ATOM   2069 C CE1 . HIS A 1 246 ? 22.337 11.483  -4.706  1.00 19.83 ? 246 HIS A CE1 1 
ATOM   2070 N NE2 . HIS A 1 246 ? 21.998 10.194  -4.760  1.00 20.16 ? 246 HIS A NE2 1 
ATOM   2071 N N   . VAL A 1 247 ? 22.246 11.522  -11.204 1.00 15.42 ? 247 VAL A N   1 
ATOM   2072 C CA  . VAL A 1 247 ? 21.930 11.926  -12.569 1.00 15.51 ? 247 VAL A CA  1 
ATOM   2073 C C   . VAL A 1 247 ? 21.958 10.715  -13.495 1.00 16.08 ? 247 VAL A C   1 
ATOM   2074 O O   . VAL A 1 247 ? 21.051 10.539  -14.308 1.00 16.35 ? 247 VAL A O   1 
ATOM   2075 C CB  . VAL A 1 247 ? 22.896 13.023  -13.073 1.00 16.23 ? 247 VAL A CB  1 
ATOM   2076 C CG1 . VAL A 1 247 ? 22.681 13.298  -14.560 1.00 17.00 ? 247 VAL A CG1 1 
ATOM   2077 C CG2 . VAL A 1 247 ? 22.733 14.297  -12.255 1.00 17.00 ? 247 VAL A CG2 1 
ATOM   2078 N N   . ASP A 1 248 ? 22.964 9.855   -13.327 1.00 16.47 ? 248 ASP A N   1 
ATOM   2079 C CA  . ASP A 1 248 ? 23.084 8.653   -14.146 1.00 17.07 ? 248 ASP A CA  1 
ATOM   2080 C C   . ASP A 1 248 ? 21.953 7.675   -13.877 1.00 17.14 ? 248 ASP A C   1 
ATOM   2081 O O   . ASP A 1 248 ? 21.438 7.067   -14.812 1.00 17.79 ? 248 ASP A O   1 
ATOM   2082 C CB  . ASP A 1 248 ? 24.433 7.972   -13.911 1.00 18.42 ? 248 ASP A CB  1 
ATOM   2083 C CG  . ASP A 1 248 ? 25.621 8.798   -14.361 1.00 21.95 ? 248 ASP A CG  1 
ATOM   2084 O OD1 . ASP A 1 248 ? 25.426 9.733   -15.170 1.00 22.47 ? 248 ASP A OD1 1 
ATOM   2085 O OD2 . ASP A 1 248 ? 26.742 8.511   -13.904 1.00 24.76 ? 248 ASP A OD2 1 
ATOM   2086 N N   . ILE A 1 249 ? 21.549 7.528   -12.614 1.00 16.87 ? 249 ILE A N   1 
ATOM   2087 C CA  . ILE A 1 249 ? 20.432 6.648   -12.257 1.00 17.46 ? 249 ILE A CA  1 
ATOM   2088 C C   . ILE A 1 249 ? 19.119 7.132   -12.904 1.00 16.76 ? 249 ILE A C   1 
ATOM   2089 O O   . ILE A 1 249 ? 18.263 6.320   -13.253 1.00 17.06 ? 249 ILE A O   1 
ATOM   2090 C CB  . ILE A 1 249 ? 20.323 6.530   -10.715 1.00 19.59 ? 249 ILE A CB  1 
ATOM   2091 C CG1 . ILE A 1 249 ? 21.526 5.765   -10.147 1.00 20.92 ? 249 ILE A CG1 1 
ATOM   2092 C CG2 . ILE A 1 249 ? 19.034 5.855   -10.297 1.00 21.07 ? 249 ILE A CG2 1 
ATOM   2093 C CD1 . ILE A 1 249 ? 21.709 5.942   -8.653  1.00 22.51 ? 249 ILE A CD1 1 
ATOM   2094 N N   . LEU A 1 250 ? 18.972 8.455   -13.087 1.00 15.50 ? 250 LEU A N   1 
ATOM   2095 C CA  . LEU A 1 250 ? 17.794 9.034   -13.730 1.00 15.60 ? 250 LEU A CA  1 
ATOM   2096 C C   . LEU A 1 250 ? 17.834 8.995   -15.268 1.00 16.87 ? 250 LEU A C   1 
ATOM   2097 O O   . LEU A 1 250 ? 16.844 9.354   -15.898 1.00 17.10 ? 250 LEU A O   1 
ATOM   2098 C CB  . LEU A 1 250 ? 17.591 10.474  -13.267 1.00 14.27 ? 250 LEU A CB  1 
ATOM   2099 C CG  . LEU A 1 250 ? 17.215 10.646  -11.808 1.00 14.27 ? 250 LEU A CG  1 
ATOM   2100 C CD1 . LEU A 1 250 ? 17.430 12.094  -11.372 1.00 14.67 ? 250 LEU A CD1 1 
ATOM   2101 C CD2 . LEU A 1 250 ? 15.762 10.236  -11.577 1.00 14.78 ? 250 LEU A CD2 1 
ATOM   2102 N N   . GLY A 1 251 ? 18.940 8.525   -15.843 1.00 17.02 ? 251 GLY A N   1 
ATOM   2103 C CA  . GLY A 1 251 ? 19.134 8.385   -17.284 1.00 18.15 ? 251 GLY A CA  1 
ATOM   2104 C C   . GLY A 1 251 ? 17.975 7.739   -18.021 1.00 19.09 ? 251 GLY A C   1 
ATOM   2105 O O   . GLY A 1 251 ? 17.410 8.357   -18.923 1.00 19.38 ? 251 GLY A O   1 
ATOM   2106 N N   . PRO A 1 252 ? 17.540 6.528   -17.623 1.00 19.11 ? 252 PRO A N   1 
ATOM   2107 C CA  . PRO A 1 252 ? 16.394 5.908   -18.309 1.00 19.24 ? 252 PRO A CA  1 
ATOM   2108 C C   . PRO A 1 252 ? 15.110 6.745   -18.294 1.00 18.83 ? 252 PRO A C   1 
ATOM   2109 O O   . PRO A 1 252 ? 14.431 6.798   -19.315 1.00 19.47 ? 252 PRO A O   1 
ATOM   2110 C CB  . PRO A 1 252 ? 16.246 4.562   -17.589 1.00 20.19 ? 252 PRO A CB  1 
ATOM   2111 C CG  . PRO A 1 252 ? 17.626 4.268   -17.093 1.00 20.99 ? 252 PRO A CG  1 
ATOM   2112 C CD  . PRO A 1 252 ? 18.109 5.617   -16.617 1.00 19.33 ? 252 PRO A CD  1 
ATOM   2113 N N   . LEU A 1 253 ? 14.785 7.429   -17.181 1.00 18.06 ? 253 LEU A N   1 
ATOM   2114 C CA  . LEU A 1 253 ? 13.586 8.275   -17.140 1.00 17.83 ? 253 LEU A CA  1 
ATOM   2115 C C   . LEU A 1 253 ? 13.741 9.519   -18.012 1.00 18.44 ? 253 LEU A C   1 
ATOM   2116 O O   . LEU A 1 253 ? 12.785 9.977   -18.635 1.00 19.17 ? 253 LEU A O   1 
ATOM   2117 C CB  . LEU A 1 253 ? 13.221 8.666   -15.706 1.00 17.36 ? 253 LEU A CB  1 
ATOM   2118 C CG  . LEU A 1 253 ? 12.642 7.523   -14.882 1.00 18.39 ? 253 LEU A CG  1 
ATOM   2119 C CD1 . LEU A 1 253 ? 12.522 7.914   -13.415 1.00 18.47 ? 253 LEU A CD1 1 
ATOM   2120 C CD2 . LEU A 1 253 ? 11.285 7.102   -15.419 1.00 19.76 ? 253 LEU A CD2 1 
ATOM   2121 N N   . SER A 1 254 ? 14.956 10.052  -18.077 1.00 18.35 ? 254 SER A N   1 
ATOM   2122 C CA  . SER A 1 254 ? 15.269 11.190  -18.918 1.00 18.83 ? 254 SER A CA  1 
ATOM   2123 C C   . SER A 1 254 ? 15.130 10.789  -20.399 1.00 19.74 ? 254 SER A C   1 
ATOM   2124 O O   . SER A 1 254 ? 14.617 11.567  -21.210 1.00 20.29 ? 254 SER A O   1 
ATOM   2125 C CB  . SER A 1 254 ? 16.703 11.640  -18.638 1.00 19.93 ? 254 SER A CB  1 
ATOM   2126 O OG  . SER A 1 254 ? 17.063 12.706  -19.494 1.00 22.09 ? 254 SER A OG  1 
ATOM   2127 N N   . ALA A 1 255 ? 15.585 9.585   -20.748 1.00 19.75 ? 255 ALA A N   1 
ATOM   2128 C CA  . ALA A 1 255 ? 15.515 9.100   -22.123 1.00 20.73 ? 255 ALA A CA  1 
ATOM   2129 C C   . ALA A 1 255 ? 14.080 8.868   -22.550 1.00 22.35 ? 255 ALA A C   1 
ATOM   2130 O O   . ALA A 1 255 ? 13.724 9.175   -23.692 1.00 22.53 ? 255 ALA A O   1 
ATOM   2131 C CB  . ALA A 1 255 ? 16.321 7.819   -22.267 1.00 20.66 ? 255 ALA A CB  1 
ATOM   2132 N N   . GLN A 1 256 ? 13.260 8.330   -21.643 1.00 22.99 ? 256 GLN A N   1 
ATOM   2133 C CA  . GLN A 1 256 ? 11.861 8.039   -21.931 1.00 24.03 ? 256 GLN A CA  1 
ATOM   2134 C C   . GLN A 1 256 ? 11.033 9.298   -22.174 1.00 23.74 ? 256 GLN A C   1 
ATOM   2135 O O   . GLN A 1 256 ? 10.254 9.350   -23.132 1.00 24.91 ? 256 GLN A O   1 
ATOM   2136 C CB  . GLN A 1 256 ? 11.252 7.200   -20.805 1.00 26.63 ? 256 GLN A CB  1 
ATOM   2137 C CG  . GLN A 1 256 ? 9.818  6.770   -21.073 1.00 31.24 ? 256 GLN A CG  1 
ATOM   2138 C CD  . GLN A 1 256 ? 9.199  6.054   -19.898 1.00 36.62 ? 256 GLN A CD  1 
ATOM   2139 O OE1 . GLN A 1 256 ? 9.885  5.560   -18.983 1.00 38.38 ? 256 GLN A OE1 1 
ATOM   2140 N NE2 . GLN A 1 256 ? 7.876  5.983   -19.902 1.00 37.67 ? 256 GLN A NE2 1 
ATOM   2141 N N   . THR A 1 257 ? 11.226 10.325  -21.350 1.00 21.63 ? 257 THR A N   1 
ATOM   2142 C CA  . THR A 1 257 ? 10.447 11.552  -21.456 1.00 20.74 ? 257 THR A CA  1 
ATOM   2143 C C   . THR A 1 257 ? 11.055 12.627  -22.354 1.00 20.66 ? 257 THR A C   1 
ATOM   2144 O O   . THR A 1 257 ? 10.367 13.578  -22.708 1.00 21.25 ? 257 THR A O   1 
ATOM   2145 C CB  . THR A 1 257 ? 10.244 12.132  -20.061 1.00 21.06 ? 257 THR A CB  1 
ATOM   2146 O OG1 . THR A 1 257 ? 11.535 12.470  -19.536 1.00 21.29 ? 257 THR A OG1 1 
ATOM   2147 C CG2 . THR A 1 257 ? 9.565  11.151  -19.127 1.00 21.27 ? 257 THR A CG2 1 
ATOM   2148 N N   . GLY A 1 258 ? 12.336 12.508  -22.660 1.00 19.65 ? 258 GLY A N   1 
ATOM   2149 C CA  . GLY A 1 258 ? 13.033 13.522  -23.440 1.00 19.47 ? 258 GLY A CA  1 
ATOM   2150 C C   . GLY A 1 258 ? 13.360 14.765  -22.637 1.00 18.75 ? 258 GLY A C   1 
ATOM   2151 O O   . GLY A 1 258 ? 13.782 15.770  -23.207 1.00 18.83 ? 258 GLY A O   1 
ATOM   2152 N N   . ILE A 1 259 ? 13.206 14.712  -21.284 1.00 17.30 ? 259 ILE A N   1 
ATOM   2153 C CA  . ILE A 1 259 ? 13.516 15.858  -20.450 1.00 17.01 ? 259 ILE A CA  1 
ATOM   2154 C C   . ILE A 1 259 ? 14.840 15.605  -19.784 1.00 16.46 ? 259 ILE A C   1 
ATOM   2155 O O   . ILE A 1 259 ? 14.980 14.653  -19.015 1.00 16.95 ? 259 ILE A O   1 
ATOM   2156 C CB  . ILE A 1 259 ? 12.396 16.138  -19.416 1.00 18.00 ? 259 ILE A CB  1 
ATOM   2157 C CG1 . ILE A 1 259 ? 11.064 16.389  -20.148 1.00 19.63 ? 259 ILE A CG1 1 
ATOM   2158 C CG2 . ILE A 1 259 ? 12.766 17.336  -18.557 1.00 18.35 ? 259 ILE A CG2 1 
ATOM   2159 C CD1 . ILE A 1 259 ? 9.876  16.454  -19.229 1.00 21.54 ? 259 ILE A CD1 1 
ATOM   2160 N N   . ALA A 1 260 ? 15.837 16.436  -20.095 1.00 15.60 ? 260 ALA A N   1 
ATOM   2161 C CA  . ALA A 1 260 ? 17.170 16.324  -19.512 1.00 15.26 ? 260 ALA A CA  1 
ATOM   2162 C C   . ALA A 1 260 ? 17.099 16.416  -17.996 1.00 14.60 ? 260 ALA A C   1 
ATOM   2163 O O   . ALA A 1 260 ? 16.278 17.168  -17.463 1.00 14.60 ? 260 ALA A O   1 
ATOM   2164 C CB  . ALA A 1 260 ? 18.067 17.431  -20.055 1.00 16.18 ? 260 ALA A CB  1 
ATOM   2165 N N   . VAL A 1 261 ? 17.925 15.638  -17.296 1.00 13.65 ? 261 VAL A N   1 
ATOM   2166 C CA  . VAL A 1 261 ? 17.923 15.636  -15.837 1.00 13.86 ? 261 VAL A CA  1 
ATOM   2167 C C   . VAL A 1 261 ? 18.078 17.028  -15.244 1.00 13.55 ? 261 VAL A C   1 
ATOM   2168 O O   . VAL A 1 261 ? 17.313 17.391  -14.351 1.00 14.19 ? 261 VAL A O   1 
ATOM   2169 C CB  . VAL A 1 261 ? 18.954 14.647  -15.258 1.00 15.10 ? 261 VAL A CB  1 
ATOM   2170 C CG1 . VAL A 1 261 ? 19.013 14.754  -13.744 1.00 14.97 ? 261 VAL A CG1 1 
ATOM   2171 C CG2 . VAL A 1 261 ? 18.624 13.214  -15.680 1.00 16.65 ? 261 VAL A CG2 1 
ATOM   2172 N N   . LEU A 1 262 ? 19.005 17.831  -15.794 1.00 13.28 ? 262 LEU A N   1 
ATOM   2173 C CA  . LEU A 1 262 ? 19.208 19.180  -15.273 1.00 13.56 ? 262 LEU A CA  1 
ATOM   2174 C C   . LEU A 1 262 ? 18.028 20.109  -15.552 1.00 13.51 ? 262 LEU A C   1 
ATOM   2175 O O   . LEU A 1 262 ? 17.795 21.025  -14.755 1.00 13.73 ? 262 LEU A O   1 
ATOM   2176 C CB  . LEU A 1 262 ? 20.526 19.768  -15.738 1.00 13.70 ? 262 LEU A CB  1 
ATOM   2177 C CG  . LEU A 1 262 ? 21.765 19.061  -15.162 1.00 15.11 ? 262 LEU A CG  1 
ATOM   2178 C CD1 . LEU A 1 262 ? 23.038 19.609  -15.783 1.00 15.85 ? 262 LEU A CD1 1 
ATOM   2179 C CD2 . LEU A 1 262 ? 21.832 19.171  -13.652 1.00 15.29 ? 262 LEU A CD2 1 
ATOM   2180 N N   . ASP A 1 263 ? 17.252 19.857  -16.630 1.00 13.50 ? 263 ASP A N   1 
ATOM   2181 C CA  . ASP A 1 263 ? 16.044 20.647  -16.866 1.00 13.09 ? 263 ASP A CA  1 
ATOM   2182 C C   . ASP A 1 263 ? 15.008 20.287  -15.786 1.00 14.28 ? 263 ASP A C   1 
ATOM   2183 O O   . ASP A 1 263 ? 14.352 21.181  -15.249 1.00 15.00 ? 263 ASP A O   1 
ATOM   2184 C CB  . ASP A 1 263 ? 15.460 20.397  -18.251 1.00 13.77 ? 263 ASP A CB  1 
ATOM   2185 C CG  . ASP A 1 263 ? 16.333 20.842  -19.408 1.00 14.89 ? 263 ASP A CG  1 
ATOM   2186 O OD1 . ASP A 1 263 ? 17.440 21.396  -19.156 1.00 14.07 ? 263 ASP A OD1 1 
ATOM   2187 O OD2 . ASP A 1 263 ? 15.912 20.661  -20.549 1.00 16.19 ? 263 ASP A OD2 1 
ATOM   2188 N N   . MET A 1 264 ? 14.883 18.991  -15.442 1.00 13.23 ? 264 MET A N   1 
ATOM   2189 C CA  . MET A 1 264 ? 13.973 18.598  -14.358 1.00 12.75 ? 264 MET A CA  1 
ATOM   2190 C C   . MET A 1 264 ? 14.443 19.193  -13.029 1.00 13.28 ? 264 MET A C   1 
ATOM   2191 O O   . MET A 1 264 ? 13.626 19.638  -12.230 1.00 14.09 ? 264 MET A O   1 
ATOM   2192 C CB  . MET A 1 264 ? 13.808 17.085  -14.252 1.00 13.83 ? 264 MET A CB  1 
ATOM   2193 C CG  . MET A 1 264 ? 12.620 16.710  -13.385 1.00 14.70 ? 264 MET A CG  1 
ATOM   2194 S SD  . MET A 1 264 ? 11.043 17.204  -14.145 1.00 16.49 ? 264 MET A SD  1 
ATOM   2195 C CE  . MET A 1 264 ? 10.741 15.784  -15.174 1.00 18.99 ? 264 MET A CE  1 
ATOM   2196 N N   . CYS A 1 265 ? 15.767 19.296  -12.823 1.00 12.88 ? 265 CYS A N   1 
ATOM   2197 C CA  . CYS A 1 265 ? 16.310 19.936  -11.623 1.00 13.13 ? 265 CYS A CA  1 
ATOM   2198 C C   . CYS A 1 265 ? 15.888 21.399  -11.572 1.00 13.37 ? 265 CYS A C   1 
ATOM   2199 O O   . CYS A 1 265 ? 15.599 21.895  -10.489 1.00 13.84 ? 265 CYS A O   1 
ATOM   2200 C CB  . CYS A 1 265 ? 17.828 19.815  -11.597 1.00 13.18 ? 265 CYS A CB  1 
ATOM   2201 S SG  . CYS A 1 265 ? 18.430 18.150  -11.239 1.00 13.95 ? 265 CYS A SG  1 
ATOM   2202 N N   . ALA A 1 266 ? 15.814 22.076  -12.734 1.00 13.18 ? 266 ALA A N   1 
ATOM   2203 C CA  . ALA A 1 266 ? 15.388 23.477  -12.773 1.00 14.34 ? 266 ALA A CA  1 
ATOM   2204 C C   . ALA A 1 266 ? 13.907 23.600  -12.453 1.00 15.13 ? 266 ALA A C   1 
ATOM   2205 O O   . ALA A 1 266 ? 13.510 24.582  -11.826 1.00 16.07 ? 266 ALA A O   1 
ATOM   2206 C CB  . ALA A 1 266 ? 15.692 24.101  -14.119 1.00 15.34 ? 266 ALA A CB  1 
ATOM   2207 N N   . SER A 1 267 ? 13.093 22.600  -12.841 1.00 14.73 ? 267 SER A N   1 
ATOM   2208 C CA  . SER A 1 267 ? 11.680 22.574  -12.475 1.00 15.16 ? 267 SER A CA  1 
ATOM   2209 C C   . SER A 1 267 ? 11.573 22.402  -10.957 1.00 14.35 ? 267 SER A C   1 
ATOM   2210 O O   . SER A 1 267 ? 10.788 23.086  -10.302 1.00 14.65 ? 267 SER A O   1 
ATOM   2211 C CB  . SER A 1 267 ? 10.953 21.421  -13.163 1.00 17.63 ? 267 SER A CB  1 
ATOM   2212 O OG  . SER A 1 267 ? 10.610 21.744  -14.499 1.00 21.64 ? 267 SER A OG  1 
ATOM   2213 N N   . LEU A 1 268 ? 12.371 21.488  -10.401 1.00 13.19 ? 268 LEU A N   1 
ATOM   2214 C CA  . LEU A 1 268 ? 12.359 21.248  -8.965  1.00 13.02 ? 268 LEU A CA  1 
ATOM   2215 C C   . LEU A 1 268 ? 12.836 22.482  -8.205  1.00 13.76 ? 268 LEU A C   1 
ATOM   2216 O O   . LEU A 1 268 ? 12.237 22.854  -7.203  1.00 13.46 ? 268 LEU A O   1 
ATOM   2217 C CB  . LEU A 1 268 ? 13.191 20.007  -8.611  1.00 12.54 ? 268 LEU A CB  1 
ATOM   2218 C CG  . LEU A 1 268 ? 13.338 19.701  -7.124  1.00 13.38 ? 268 LEU A CG  1 
ATOM   2219 C CD1 . LEU A 1 268 ? 11.961 19.546  -6.450  1.00 14.09 ? 268 LEU A CD1 1 
ATOM   2220 C CD2 . LEU A 1 268 ? 14.098 18.421  -6.934  1.00 13.76 ? 268 LEU A CD2 1 
ATOM   2221 N N   . LYS A 1 269 ? 13.869 23.160  -8.705  1.00 12.82 ? 269 LYS A N   1 
ATOM   2222 C CA  . LYS A 1 269 ? 14.363 24.389  -8.097  1.00 12.60 ? 269 LYS A CA  1 
ATOM   2223 C C   . LYS A 1 269 ? 13.255 25.446  -8.026  1.00 13.34 ? 269 LYS A C   1 
ATOM   2224 O O   . LYS A 1 269 ? 13.062 26.038  -6.976  1.00 13.99 ? 269 LYS A O   1 
ATOM   2225 C CB  . LYS A 1 269 ? 15.546 24.917  -8.911  1.00 13.63 ? 269 LYS A CB  1 
ATOM   2226 C CG  . LYS A 1 269 ? 16.062 26.292  -8.492  1.00 17.21 ? 269 LYS A CG  1 
ATOM   2227 C CD  . LYS A 1 269 ? 17.254 26.664  -9.357  1.00 20.23 ? 269 LYS A CD  1 
ATOM   2228 C CE  . LYS A 1 269 ? 17.557 28.150  -9.315  1.00 23.68 ? 269 LYS A CE  1 
ATOM   2229 N NZ  . LYS A 1 269 ? 18.553 28.518  -10.362 1.00 25.16 ? 269 LYS A NZ  1 
ATOM   2230 N N   . GLU A 1 270 ? 12.479 25.616  -9.107  1.00 13.60 ? 270 GLU A N   1 
ATOM   2231 C CA  . GLU A 1 270 ? 11.380 26.581  -9.098  1.00 14.67 ? 270 GLU A CA  1 
ATOM   2232 C C   . GLU A 1 270 ? 10.288 26.174  -8.115  1.00 15.62 ? 270 GLU A C   1 
ATOM   2233 O O   . GLU A 1 270 ? 9.749  27.026  -7.415  1.00 16.25 ? 270 GLU A O   1 
ATOM   2234 C CB  . GLU A 1 270 ? 10.813 26.806  -10.505 1.00 17.51 ? 270 GLU A CB  1 
ATOM   2235 C CG  . GLU A 1 270 ? 11.804 27.456  -11.453 1.00 24.81 ? 270 GLU A CG  1 
ATOM   2236 C CD  . GLU A 1 270 ? 12.368 28.793  -11.016 1.00 32.43 ? 270 GLU A CD  1 
ATOM   2237 O OE1 . GLU A 1 270 ? 11.568 29.730  -10.794 1.00 33.99 ? 270 GLU A OE1 1 
ATOM   2238 O OE2 . GLU A 1 270 ? 13.611 28.907  -10.900 1.00 33.71 ? 270 GLU A OE2 1 
ATOM   2239 N N   . LEU A 1 271 ? 9.974  24.877  -8.043  1.00 15.19 ? 271 LEU A N   1 
ATOM   2240 C CA  . LEU A 1 271 ? 8.984  24.384  -7.082  1.00 15.27 ? 271 LEU A CA  1 
ATOM   2241 C C   . LEU A 1 271 ? 9.434  24.628  -5.646  1.00 15.62 ? 271 LEU A C   1 
ATOM   2242 O O   . LEU A 1 271 ? 8.598  24.933  -4.792  1.00 17.11 ? 271 LEU A O   1 
ATOM   2243 C CB  . LEU A 1 271 ? 8.749  22.894  -7.289  1.00 15.27 ? 271 LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 271 ? 7.915  22.555  -8.510  1.00 16.49 ? 271 LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 271 ? 7.962  21.084  -8.777  1.00 16.95 ? 271 LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 271 ? 6.477  23.030  -8.321  1.00 17.56 ? 271 LEU A CD2 1 
ATOM   2247 N N   . LEU A 1 272 ? 10.737 24.490  -5.367  1.00 14.10 ? 272 LEU A N   1 
ATOM   2248 C CA  . LEU A 1 272 ? 11.233 24.723  -4.011  1.00 14.76 ? 272 LEU A CA  1 
ATOM   2249 C C   . LEU A 1 272 ? 11.164 26.195  -3.655  1.00 16.26 ? 272 LEU A C   1 
ATOM   2250 O O   . LEU A 1 272 ? 10.760 26.536  -2.543  1.00 17.01 ? 272 LEU A O   1 
ATOM   2251 C CB  . LEU A 1 272 ? 12.669 24.214  -3.869  1.00 14.74 ? 272 LEU A CB  1 
ATOM   2252 C CG  . LEU A 1 272 ? 12.797 22.705  -3.843  1.00 16.78 ? 272 LEU A CG  1 
ATOM   2253 C CD1 . LEU A 1 272 ? 14.257 22.274  -3.868  1.00 17.63 ? 272 LEU A CD1 1 
ATOM   2254 C CD2 . LEU A 1 272 ? 12.062 22.119  -2.657  1.00 18.76 ? 272 LEU A CD2 1 
ATOM   2255 N N   . GLN A 1 273 ? 11.531 27.061  -4.599  1.00 16.06 ? 273 GLN A N   1 
ATOM   2256 C CA  . GLN A 1 273 ? 11.587 28.499  -4.374  1.00 17.33 ? 273 GLN A CA  1 
ATOM   2257 C C   . GLN A 1 273 ? 10.240 29.180  -4.375  1.00 19.69 ? 273 GLN A C   1 
ATOM   2258 O O   . GLN A 1 273 ? 10.080 30.197  -3.708  1.00 20.97 ? 273 GLN A O   1 
ATOM   2259 C CB  . GLN A 1 273 ? 12.515 29.162  -5.409  1.00 17.71 ? 273 GLN A CB  1 
ATOM   2260 C CG  . GLN A 1 273 ? 13.968 28.758  -5.252  1.00 19.36 ? 273 GLN A CG  1 
ATOM   2261 C CD  . GLN A 1 273 ? 14.860 29.396  -6.286  1.00 22.80 ? 273 GLN A CD  1 
ATOM   2262 O OE1 . GLN A 1 273 ? 14.437 29.745  -7.391  1.00 24.43 ? 273 GLN A OE1 1 
ATOM   2263 N NE2 . GLN A 1 273 ? 16.125 29.546  -5.950  1.00 23.28 ? 273 GLN A NE2 1 
ATOM   2264 N N   . ASN A 1 274 ? 9.280  28.656  -5.133  1.00 20.29 ? 274 ASN A N   1 
ATOM   2265 C CA  . ASN A 1 274 ? 7.976  29.304  -5.249  1.00 21.83 ? 274 ASN A CA  1 
ATOM   2266 C C   . ASN A 1 274 ? 6.801  28.527  -4.690  1.00 22.69 ? 274 ASN A C   1 
ATOM   2267 O O   . ASN A 1 274 ? 5.697  29.063  -4.637  1.00 23.59 ? 274 ASN A O   1 
ATOM   2268 C CB  . ASN A 1 274 ? 7.716  29.658  -6.695  1.00 23.76 ? 274 ASN A CB  1 
ATOM   2269 C CG  . ASN A 1 274 ? 8.780  30.577  -7.217  1.00 29.54 ? 274 ASN A CG  1 
ATOM   2270 O OD1 . ASN A 1 274 ? 8.793  31.778  -6.927  1.00 32.28 ? 274 ASN A OD1 1 
ATOM   2271 N ND2 . ASN A 1 274 ? 9.721  30.023  -7.954  1.00 30.78 ? 274 ASN A ND2 1 
ATOM   2272 N N   . GLY A 1 275 ? 7.023  27.287  -4.285  1.00 22.59 ? 275 GLY A N   1 
ATOM   2273 C CA  . GLY A 1 275 ? 5.948  26.444  -3.791  1.00 22.92 ? 275 GLY A CA  1 
ATOM   2274 C C   . GLY A 1 275 ? 5.080  25.943  -4.929  1.00 23.41 ? 275 GLY A C   1 
ATOM   2275 O O   . GLY A 1 275 ? 5.379  26.177  -6.111  1.00 23.66 ? 275 GLY A O   1 
ATOM   2276 N N   A MET A 1 276 ? 3.995  25.255  -4.586  0.75 23.76 ? 276 MET A N   1 
ATOM   2277 N N   B MET A 1 276 ? 3.999  25.241  -4.587  0.25 23.17 ? 276 MET A N   1 
ATOM   2278 C CA  A MET A 1 276 ? 3.106  24.713  -5.607  0.75 24.64 ? 276 MET A CA  1 
ATOM   2279 C CA  B MET A 1 276 ? 3.087  24.717  -5.599  0.25 23.44 ? 276 MET A CA  1 
ATOM   2280 C C   A MET A 1 276 ? 1.887  25.618  -5.902  0.75 25.05 ? 276 MET A C   1 
ATOM   2281 C C   B MET A 1 276 ? 1.968  25.686  -5.984  0.25 24.43 ? 276 MET A C   1 
ATOM   2282 O O   A MET A 1 276 ? 1.113  25.299  -6.801  0.75 25.20 ? 276 MET A O   1 
ATOM   2283 O O   B MET A 1 276 ? 1.294  25.437  -6.974  0.25 24.50 ? 276 MET A O   1 
ATOM   2284 C CB  A MET A 1 276 ? 2.723  23.269  -5.272  0.75 25.92 ? 276 MET A CB  1 
ATOM   2285 C CB  B MET A 1 276 ? 2.506  23.358  -5.181  0.25 23.19 ? 276 MET A CB  1 
ATOM   2286 C CG  A MET A 1 276 ? 3.943  22.341  -5.362  0.75 28.07 ? 276 MET A CG  1 
ATOM   2287 C CG  B MET A 1 276 ? 3.463  22.203  -5.391  0.25 23.17 ? 276 MET A CG  1 
ATOM   2288 S SD  A MET A 1 276 ? 3.789  20.735  -4.570  0.75 35.78 ? 276 MET A SD  1 
ATOM   2289 S SD  B MET A 1 276 ? 2.590  20.634  -5.587  0.25 19.97 ? 276 MET A SD  1 
ATOM   2290 C CE  A MET A 1 276 ? 2.500  20.047  -5.545  0.75 30.19 ? 276 MET A CE  1 
ATOM   2291 C CE  B MET A 1 276 ? 3.918  19.512  -5.312  0.25 18.54 ? 276 MET A CE  1 
ATOM   2292 N N   . ASN A 1 277 ? 1.774  26.783  -5.227  1.00 24.94 ? 277 ASN A N   1 
ATOM   2293 C CA  . ASN A 1 277 ? 0.711  27.772  -5.473  1.00 25.60 ? 277 ASN A CA  1 
ATOM   2294 C C   . ASN A 1 277 ? -0.709 27.189  -5.412  1.00 25.41 ? 277 ASN A C   1 
ATOM   2295 O O   . ASN A 1 277 ? -1.567 27.570  -6.209  1.00 26.11 ? 277 ASN A O   1 
ATOM   2296 C CB  . ASN A 1 277 ? 0.942  28.527  -6.787  1.00 27.55 ? 277 ASN A CB  1 
ATOM   2297 C CG  . ASN A 1 277 ? 2.030  29.565  -6.712  1.00 32.36 ? 277 ASN A CG  1 
ATOM   2298 O OD1 . ASN A 1 277 ? 3.087  29.452  -7.353  1.00 34.44 ? 277 ASN A OD1 1 
ATOM   2299 N ND2 . ASN A 1 277 ? 1.795  30.607  -5.933  1.00 32.85 ? 277 ASN A ND2 1 
ATOM   2300 N N   . GLY A 1 278 ? -0.939 26.258  -4.495  1.00 24.04 ? 278 GLY A N   1 
ATOM   2301 C CA  . GLY A 1 278 ? -2.250 25.630  -4.362  1.00 23.26 ? 278 GLY A CA  1 
ATOM   2302 C C   . GLY A 1 278 ? -2.558 24.555  -5.391  1.00 22.48 ? 278 GLY A C   1 
ATOM   2303 O O   . GLY A 1 278 ? -3.689 24.070  -5.468  1.00 22.88 ? 278 GLY A O   1 
ATOM   2304 N N   A ARG A 1 279 ? -1.553 24.151  -6.167  0.50 21.95 ? 279 ARG A N   1 
ATOM   2305 N N   B ARG A 1 279 ? -1.550 24.164  -6.183  0.50 21.71 ? 279 ARG A N   1 
ATOM   2306 C CA  A ARG A 1 279 ? -1.722 23.116  -7.173  0.50 21.79 ? 279 ARG A CA  1 
ATOM   2307 C CA  B ARG A 1 279 ? -1.691 23.135  -7.207  0.50 21.30 ? 279 ARG A CA  1 
ATOM   2308 C C   A ARG A 1 279 ? -1.216 21.759  -6.668  0.50 21.02 ? 279 ARG A C   1 
ATOM   2309 C C   B ARG A 1 279 ? -1.203 21.769  -6.683  0.50 20.81 ? 279 ARG A C   1 
ATOM   2310 O O   A ARG A 1 279 ? -0.595 21.677  -5.602  0.50 20.83 ? 279 ARG A O   1 
ATOM   2311 O O   B ARG A 1 279 ? -0.560 21.694  -5.629  0.50 20.66 ? 279 ARG A O   1 
ATOM   2312 C CB  A ARG A 1 279 ? -1.035 23.533  -8.485  0.50 23.35 ? 279 ARG A CB  1 
ATOM   2313 C CB  B ARG A 1 279 ? -0.911 23.540  -8.475  0.50 22.14 ? 279 ARG A CB  1 
ATOM   2314 C CG  A ARG A 1 279 ? -1.623 24.814  -9.067  0.50 27.22 ? 279 ARG A CG  1 
ATOM   2315 C CG  B ARG A 1 279 ? -1.238 24.939  -9.002  0.50 24.89 ? 279 ARG A CG  1 
ATOM   2316 C CD  A ARG A 1 279 ? -1.199 25.050  -10.505 0.50 31.04 ? 279 ARG A CD  1 
ATOM   2317 C CD  B ARG A 1 279 ? -0.110 25.483  -9.868  0.50 27.42 ? 279 ARG A CD  1 
ATOM   2318 N NE  A ARG A 1 279 ? -1.606 23.954  -11.383 0.50 34.59 ? 279 ARG A NE  1 
ATOM   2319 N NE  B ARG A 1 279 ? -0.302 26.894  -10.206 0.50 30.09 ? 279 ARG A NE  1 
ATOM   2320 C CZ  A ARG A 1 279 ? -2.790 23.867  -11.981 0.50 37.85 ? 279 ARG A CZ  1 
ATOM   2321 C CZ  B ARG A 1 279 ? 0.680  27.785  -10.306 0.50 31.90 ? 279 ARG A CZ  1 
ATOM   2322 N NH1 A ARG A 1 279 ? -3.697 24.824  -11.819 0.50 37.97 ? 279 ARG A NH1 1 
ATOM   2323 N NH1 B ARG A 1 279 ? 1.940  27.424  -10.088 0.50 31.04 ? 279 ARG A NH1 1 
ATOM   2324 N NH2 A ARG A 1 279 ? -3.068 22.834  -12.764 0.50 38.37 ? 279 ARG A NH2 1 
ATOM   2325 N NH2 B ARG A 1 279 ? 0.413  29.041  -10.636 0.50 31.90 ? 279 ARG A NH2 1 
ATOM   2326 N N   . THR A 1 280 ? -1.531 20.684  -7.398  1.00 20.29 ? 280 THR A N   1 
ATOM   2327 C CA  . THR A 1 280 ? -1.107 19.344  -7.010  1.00 19.70 ? 280 THR A CA  1 
ATOM   2328 C C   . THR A 1 280 ? -0.346 18.658  -8.148  1.00 18.60 ? 280 THR A C   1 
ATOM   2329 O O   . THR A 1 280 ? -0.473 19.032  -9.320  1.00 18.37 ? 280 THR A O   1 
ATOM   2330 C CB  . THR A 1 280 ? -2.305 18.475  -6.574  1.00 21.75 ? 280 THR A CB  1 
ATOM   2331 O OG1 . THR A 1 280 ? -3.207 18.341  -7.675  1.00 22.42 ? 280 THR A OG1 1 
ATOM   2332 C CG2 . THR A 1 280 ? -3.016 19.017  -5.348  1.00 22.81 ? 280 THR A CG2 1 
ATOM   2333 N N   . ILE A 1 281 ? 0.475  17.669  -7.786  1.00 17.32 ? 281 ILE A N   1 
ATOM   2334 C CA  . ILE A 1 281 ? 1.241  16.844  -8.713  1.00 17.17 ? 281 ILE A CA  1 
ATOM   2335 C C   . ILE A 1 281 ? 0.971  15.413  -8.307  1.00 17.06 ? 281 ILE A C   1 
ATOM   2336 O O   . ILE A 1 281 ? 1.194  15.057  -7.152  1.00 16.72 ? 281 ILE A O   1 
ATOM   2337 C CB  . ILE A 1 281 ? 2.749  17.150  -8.631  1.00 17.81 ? 281 ILE A CB  1 
ATOM   2338 C CG1 . ILE A 1 281 ? 3.047  18.602  -9.014  1.00 18.05 ? 281 ILE A CG1 1 
ATOM   2339 C CG2 . ILE A 1 281 ? 3.527  16.160  -9.502  1.00 18.38 ? 281 ILE A CG2 1 
ATOM   2340 C CD1 . ILE A 1 281 ? 4.518  19.020  -8.861  1.00 18.34 ? 281 ILE A CD1 1 
ATOM   2341 N N   . LEU A 1 282 ? 0.390  14.603  -9.206  1.00 17.24 ? 282 LEU A N   1 
ATOM   2342 C CA  . LEU A 1 282 ? 0.041  13.212  -8.889  1.00 17.35 ? 282 LEU A CA  1 
ATOM   2343 C C   . LEU A 1 282 ? -0.763 13.066  -7.587  1.00 18.42 ? 282 LEU A C   1 
ATOM   2344 O O   . LEU A 1 282 ? -0.449 12.228  -6.754  1.00 19.49 ? 282 LEU A O   1 
ATOM   2345 C CB  . LEU A 1 282 ? 1.267  12.292  -8.890  1.00 16.82 ? 282 LEU A CB  1 
ATOM   2346 C CG  . LEU A 1 282 ? 1.936  12.047  -10.240 1.00 17.52 ? 282 LEU A CG  1 
ATOM   2347 C CD1 . LEU A 1 282 ? 3.136  11.159  -10.080 1.00 17.37 ? 282 LEU A CD1 1 
ATOM   2348 C CD2 . LEU A 1 282 ? 0.969  11.447  -11.235 1.00 18.50 ? 282 LEU A CD2 1 
ATOM   2349 N N   . GLY A 1 283 ? -1.725 13.970  -7.411  1.00 19.57 ? 283 GLY A N   1 
ATOM   2350 C CA  . GLY A 1 283 ? -2.606 13.998  -6.248  1.00 20.20 ? 283 GLY A CA  1 
ATOM   2351 C C   . GLY A 1 283 ? -1.975 14.425  -4.940  1.00 20.33 ? 283 GLY A C   1 
ATOM   2352 O O   . GLY A 1 283 ? -2.567 14.232  -3.877  1.00 21.64 ? 283 GLY A O   1 
ATOM   2353 N N   A SER A 1 284 ? -0.758 14.973  -4.996  0.75 19.07 ? 284 SER A N   1 
ATOM   2354 N N   B SER A 1 284 ? -0.757 14.979  -4.998  0.25 19.33 ? 284 SER A N   1 
ATOM   2355 C CA  A SER A 1 284 ? -0.061 15.413  -3.798  0.75 18.29 ? 284 SER A CA  1 
ATOM   2356 C CA  B SER A 1 284 ? -0.033 15.409  -3.809  0.25 18.82 ? 284 SER A CA  1 
ATOM   2357 C C   A SER A 1 284 ? 0.123  16.915  -3.823  0.75 18.11 ? 284 SER A C   1 
ATOM   2358 C C   B SER A 1 284 ? 0.197  16.911  -3.813  0.25 18.48 ? 284 SER A C   1 
ATOM   2359 O O   A SER A 1 284 ? 0.390  17.488  -4.872  0.75 17.64 ? 284 SER A O   1 
ATOM   2360 O O   B SER A 1 284 ? 0.554  17.481  -4.841  0.25 18.38 ? 284 SER A O   1 
ATOM   2361 C CB  A SER A 1 284 ? 1.311  14.752  -3.713  0.75 18.83 ? 284 SER A CB  1 
ATOM   2362 C CB  B SER A 1 284 ? 1.319  14.705  -3.725  0.25 19.61 ? 284 SER A CB  1 
ATOM   2363 O OG  A SER A 1 284 ? 2.022  15.192  -2.566  0.75 20.77 ? 284 SER A OG  1 
ATOM   2364 O OG  B SER A 1 284 ? 1.181  13.310  -3.519  0.25 21.27 ? 284 SER A OG  1 
ATOM   2365 N N   . ALA A 1 285 ? 0.040  17.547  -2.650  1.00 18.03 ? 285 ALA A N   1 
ATOM   2366 C CA  . ALA A 1 285 ? 0.290  18.982  -2.522  1.00 18.74 ? 285 ALA A CA  1 
ATOM   2367 C C   . ALA A 1 285 ? 1.728  19.259  -1.985  1.00 18.86 ? 285 ALA A C   1 
ATOM   2368 O O   . ALA A 1 285 ? 2.067  20.400  -1.676  1.00 20.19 ? 285 ALA A O   1 
ATOM   2369 C CB  . ALA A 1 285 ? -0.755 19.620  -1.623  1.00 19.27 ? 285 ALA A CB  1 
ATOM   2370 N N   . LEU A 1 286 ? 2.561  18.233  -1.874  1.00 17.88 ? 286 LEU A N   1 
ATOM   2371 C CA  . LEU A 1 286 ? 3.951  18.373  -1.497  1.00 18.08 ? 286 LEU A CA  1 
ATOM   2372 C C   . LEU A 1 286 ? 4.832  17.526  -2.431  1.00 17.12 ? 286 LEU A C   1 
ATOM   2373 O O   . LEU A 1 286 ? 4.316  16.735  -3.234  1.00 17.43 ? 286 LEU A O   1 
ATOM   2374 C CB  . LEU A 1 286 ? 4.191  18.099  -0.005  1.00 19.14 ? 286 LEU A CB  1 
ATOM   2375 C CG  . LEU A 1 286 ? 3.662  16.806  0.562   1.00 21.28 ? 286 LEU A CG  1 
ATOM   2376 C CD1 . LEU A 1 286 ? 4.491  15.630  0.105   1.00 22.70 ? 286 LEU A CD1 1 
ATOM   2377 C CD2 . LEU A 1 286 ? 3.721  16.839  2.088   1.00 22.17 ? 286 LEU A CD2 1 
ATOM   2378 N N   . LEU A 1 287 ? 6.135  17.757  -2.402  1.00 15.55 ? 287 LEU A N   1 
ATOM   2379 C CA  . LEU A 1 287 ? 7.059  17.031  -3.258  1.00 15.39 ? 287 LEU A CA  1 
ATOM   2380 C C   . LEU A 1 287 ? 7.339  15.664  -2.641  1.00 15.22 ? 287 LEU A C   1 
ATOM   2381 O O   . LEU A 1 287 ? 7.958  15.571  -1.591  1.00 16.81 ? 287 LEU A O   1 
ATOM   2382 C CB  . LEU A 1 287 ? 8.323  17.863  -3.459  1.00 16.06 ? 287 LEU A CB  1 
ATOM   2383 C CG  . LEU A 1 287 ? 8.026  19.223  -4.104  1.00 18.18 ? 287 LEU A CG  1 
ATOM   2384 C CD1 . LEU A 1 287 ? 9.204  20.138  -3.991  1.00 18.93 ? 287 LEU A CD1 1 
ATOM   2385 C CD2 . LEU A 1 287 ? 7.575  19.068  -5.566  1.00 19.33 ? 287 LEU A CD2 1 
ATOM   2386 N N   A GLU A 1 288 ? 6.855  14.602  -3.286  0.50 13.98 ? 288 GLU A N   1 
ATOM   2387 N N   B GLU A 1 288 ? 6.866  14.610  -3.293  0.50 14.00 ? 288 GLU A N   1 
ATOM   2388 C CA  A GLU A 1 288 ? 6.993  13.231  -2.776  0.50 13.48 ? 288 GLU A CA  1 
ATOM   2389 C CA  B GLU A 1 288 ? 6.991  13.233  -2.807  0.50 13.54 ? 288 GLU A CA  1 
ATOM   2390 C C   A GLU A 1 288 ? 8.376  12.638  -2.986  0.50 13.16 ? 288 GLU A C   1 
ATOM   2391 C C   B GLU A 1 288 ? 8.390  12.654  -2.992  0.50 13.22 ? 288 GLU A C   1 
ATOM   2392 O O   A GLU A 1 288 ? 8.883  12.653  -4.105  0.50 13.26 ? 288 GLU A O   1 
ATOM   2393 O O   B GLU A 1 288 ? 8.917  12.689  -4.102  0.50 13.37 ? 288 GLU A O   1 
ATOM   2394 C CB  A GLU A 1 288 ? 5.916  12.318  -3.382  0.50 14.44 ? 288 GLU A CB  1 
ATOM   2395 C CB  B GLU A 1 288 ? 5.938  12.358  -3.504  0.50 14.59 ? 288 GLU A CB  1 
ATOM   2396 C CG  A GLU A 1 288 ? 4.495  12.789  -3.115  0.50 16.46 ? 288 GLU A CG  1 
ATOM   2397 C CG  B GLU A 1 288 ? 6.026  10.881  -3.187  0.50 16.96 ? 288 GLU A CG  1 
ATOM   2398 C CD  A GLU A 1 288 ? 3.946  12.471  -1.736  0.50 20.85 ? 288 GLU A CD  1 
ATOM   2399 C CD  B GLU A 1 288 ? 5.638  10.508  -1.773  0.50 19.50 ? 288 GLU A CD  1 
ATOM   2400 O OE1 A GLU A 1 288 ? 4.624  11.747  -0.972  0.50 22.15 ? 288 GLU A OE1 1 
ATOM   2401 O OE1 B GLU A 1 288 ? 6.458  9.855   -1.089  0.50 16.00 ? 288 GLU A OE1 1 
ATOM   2402 O OE2 A GLU A 1 288 ? 2.824  12.931  -1.426  0.50 21.03 ? 288 GLU A OE2 1 
ATOM   2403 O OE2 B GLU A 1 288 ? 4.514  10.867  -1.350  0.50 22.07 ? 288 GLU A OE2 1 
ATOM   2404 N N   . ASP A 1 289 ? 8.971  12.078  -1.927  1.00 12.93 ? 289 ASP A N   1 
ATOM   2405 C CA  . ASP A 1 289 ? 10.310 11.516  -2.024  1.00 12.60 ? 289 ASP A CA  1 
ATOM   2406 C C   . ASP A 1 289 ? 10.423 10.047  -1.666  1.00 13.43 ? 289 ASP A C   1 
ATOM   2407 O O   . ASP A 1 289 ? 11.543 9.594   -1.414  1.00 13.88 ? 289 ASP A O   1 
ATOM   2408 C CB  . ASP A 1 289 ? 11.323 12.330  -1.215  1.00 12.56 ? 289 ASP A CB  1 
ATOM   2409 C CG  . ASP A 1 289 ? 11.288 12.143  0.274   1.00 14.92 ? 289 ASP A CG  1 
ATOM   2410 O OD1 . ASP A 1 289 ? 10.301 11.554  0.778   1.00 14.82 ? 289 ASP A OD1 1 
ATOM   2411 O OD2 . ASP A 1 289 ? 12.243 12.583  0.934   1.00 15.48 ? 289 ASP A OD2 1 
ATOM   2412 N N   . GLU A 1 290 ? 9.296  9.306   -1.633  1.00 13.33 ? 290 GLU A N   1 
ATOM   2413 C CA  . GLU A 1 290 ? 9.409  7.892   -1.299  1.00 13.90 ? 290 GLU A CA  1 
ATOM   2414 C C   . GLU A 1 290 ? 9.082  6.995   -2.504  1.00 14.27 ? 290 GLU A C   1 
ATOM   2415 O O   . GLU A 1 290 ? 8.544  5.902   -2.363  1.00 14.58 ? 290 GLU A O   1 
ATOM   2416 C CB  . GLU A 1 290 ? 8.658  7.524   -0.006  1.00 14.67 ? 290 GLU A CB  1 
ATOM   2417 C CG  . GLU A 1 290 ? 9.218  8.275   1.202   1.00 16.76 ? 290 GLU A CG  1 
ATOM   2418 C CD  . GLU A 1 290 ? 8.875  7.717   2.576   1.00 18.56 ? 290 GLU A CD  1 
ATOM   2419 O OE1 . GLU A 1 290 ? 7.986  6.840   2.655   1.00 16.60 ? 290 GLU A OE1 1 
ATOM   2420 O OE2 . GLU A 1 290 ? 9.511  8.133   3.572   1.00 19.92 ? 290 GLU A OE2 1 
ATOM   2421 N N   . PHE A 1 291 ? 9.510  7.433   -3.696  1.00 13.63 ? 291 PHE A N   1 
ATOM   2422 C CA  . PHE A 1 291 ? 9.546  6.589   -4.879  1.00 14.24 ? 291 PHE A CA  1 
ATOM   2423 C C   . PHE A 1 291 ? 10.925 6.730   -5.436  1.00 14.69 ? 291 PHE A C   1 
ATOM   2424 O O   . PHE A 1 291 ? 11.307 7.844   -5.781  1.00 15.37 ? 291 PHE A O   1 
ATOM   2425 C CB  . PHE A 1 291 ? 8.614  7.038   -5.997  1.00 14.36 ? 291 PHE A CB  1 
ATOM   2426 C CG  . PHE A 1 291 ? 7.153  6.969   -5.703  1.00 15.75 ? 291 PHE A CG  1 
ATOM   2427 C CD1 . PHE A 1 291 ? 6.458  5.787   -5.858  1.00 16.87 ? 291 PHE A CD1 1 
ATOM   2428 C CD2 . PHE A 1 291 ? 6.457  8.100   -5.333  1.00 17.27 ? 291 PHE A CD2 1 
ATOM   2429 C CE1 . PHE A 1 291 ? 5.089  5.746   -5.646  1.00 18.29 ? 291 PHE A CE1 1 
ATOM   2430 C CE2 . PHE A 1 291 ? 5.090  8.060   -5.145  1.00 18.48 ? 291 PHE A CE2 1 
ATOM   2431 C CZ  . PHE A 1 291 ? 4.414  6.885   -5.307  1.00 18.11 ? 291 PHE A CZ  1 
ATOM   2432 N N   . THR A 1 292 ? 11.657 5.637   -5.560  1.00 14.58 ? 292 THR A N   1 
ATOM   2433 C CA  . THR A 1 292 ? 12.980 5.663   -6.157  1.00 14.64 ? 292 THR A CA  1 
ATOM   2434 C C   . THR A 1 292 ? 12.849 5.681   -7.683  1.00 14.39 ? 292 THR A C   1 
ATOM   2435 O O   . THR A 1 292 ? 11.814 5.278   -8.228  1.00 14.19 ? 292 THR A O   1 
ATOM   2436 C CB  . THR A 1 292 ? 13.753 4.380   -5.771  1.00 15.84 ? 292 THR A CB  1 
ATOM   2437 O OG1 . THR A 1 292 ? 13.148 3.243   -6.396  1.00 17.07 ? 292 THR A OG1 1 
ATOM   2438 C CG2 . THR A 1 292 ? 13.836 4.168   -4.275  1.00 15.86 ? 292 THR A CG2 1 
ATOM   2439 N N   . PRO A 1 293 ? 13.938 5.984   -8.406  1.00 14.84 ? 293 PRO A N   1 
ATOM   2440 C CA  . PRO A 1 293 ? 13.897 5.872   -9.875  1.00 14.67 ? 293 PRO A CA  1 
ATOM   2441 C C   . PRO A 1 293 ? 13.499 4.455   -10.322 1.00 15.65 ? 293 PRO A C   1 
ATOM   2442 O O   . PRO A 1 293 ? 12.761 4.300   -11.296 1.00 16.06 ? 293 PRO A O   1 
ATOM   2443 C CB  . PRO A 1 293 ? 15.339 6.206   -10.275 1.00 15.78 ? 293 PRO A CB  1 
ATOM   2444 C CG  . PRO A 1 293 ? 15.801 7.141   -9.190  1.00 16.06 ? 293 PRO A CG  1 
ATOM   2445 C CD  . PRO A 1 293 ? 15.229 6.536   -7.942  1.00 14.54 ? 293 PRO A CD  1 
ATOM   2446 N N   . PHE A 1 294 ? 13.961 3.420   -9.593  1.00 16.05 ? 294 PHE A N   1 
ATOM   2447 C CA  A PHE A 1 294 ? 13.614 2.037   -9.947  0.60 17.63 ? 294 PHE A CA  1 
ATOM   2448 C CA  B PHE A 1 294 ? 13.625 2.042   -9.943  0.40 17.39 ? 294 PHE A CA  1 
ATOM   2449 C C   . PHE A 1 294 ? 12.129 1.806   -9.755  1.00 17.49 ? 294 PHE A C   1 
ATOM   2450 O O   . PHE A 1 294 ? 11.509 1.147   -10.587 1.00 18.53 ? 294 PHE A O   1 
ATOM   2451 C CB  A PHE A 1 294 ? 14.414 1.007   -9.126  0.60 18.71 ? 294 PHE A CB  1 
ATOM   2452 C CB  B PHE A 1 294 ? 14.457 1.057   -9.109  0.40 18.14 ? 294 PHE A CB  1 
ATOM   2453 C CG  A PHE A 1 294 ? 15.839 0.729   -9.559  0.60 20.73 ? 294 PHE A CG  1 
ATOM   2454 C CG  B PHE A 1 294 ? 14.453 -0.377  -9.584  0.40 19.78 ? 294 PHE A CG  1 
ATOM   2455 C CD1 A PHE A 1 294 ? 16.370 1.325   -10.689 0.60 22.07 ? 294 PHE A CD1 1 
ATOM   2456 C CD1 B PHE A 1 294 ? 14.237 -0.685  -10.916 0.40 21.21 ? 294 PHE A CD1 1 
ATOM   2457 C CD2 A PHE A 1 294 ? 16.668 -0.076  -8.794  0.60 22.36 ? 294 PHE A CD2 1 
ATOM   2458 C CD2 B PHE A 1 294 ? 14.733 -1.411  -8.711  0.40 21.02 ? 294 PHE A CD2 1 
ATOM   2459 C CE1 A PHE A 1 294 ? 17.685 1.092   -11.061 0.60 23.04 ? 294 PHE A CE1 1 
ATOM   2460 C CE1 B PHE A 1 294 ? 14.239 -2.002  -11.348 0.40 22.18 ? 294 PHE A CE1 1 
ATOM   2461 C CE2 A PHE A 1 294 ? 17.988 -0.290  -9.162  0.60 23.26 ? 294 PHE A CE2 1 
ATOM   2462 C CE2 B PHE A 1 294 ? 14.734 -2.729  -9.147  0.40 21.90 ? 294 PHE A CE2 1 
ATOM   2463 C CZ  A PHE A 1 294 ? 18.485 0.292   -10.294 0.60 23.11 ? 294 PHE A CZ  1 
ATOM   2464 C CZ  B PHE A 1 294 ? 14.485 -3.015  -10.461 0.40 21.80 ? 294 PHE A CZ  1 
ATOM   2465 N N   . ASP A 1 295 ? 11.540 2.357   -8.678  1.00 16.66 ? 295 ASP A N   1 
ATOM   2466 C CA  . ASP A 1 295 ? 10.103 2.218   -8.410  1.00 16.33 ? 295 ASP A CA  1 
ATOM   2467 C C   . ASP A 1 295 ? 9.308  2.848   -9.537  1.00 17.17 ? 295 ASP A C   1 
ATOM   2468 O O   . ASP A 1 295 ? 8.307  2.286   -9.970  1.00 18.29 ? 295 ASP A O   1 
ATOM   2469 C CB  . ASP A 1 295 ? 9.693  2.913   -7.106  1.00 17.12 ? 295 ASP A CB  1 
ATOM   2470 C CG  . ASP A 1 295 ? 10.224 2.304   -5.838  1.00 18.41 ? 295 ASP A CG  1 
ATOM   2471 O OD1 . ASP A 1 295 ? 10.556 1.095   -5.850  1.00 19.16 ? 295 ASP A OD1 1 
ATOM   2472 O OD2 . ASP A 1 295 ? 10.319 3.037   -4.827  1.00 18.01 ? 295 ASP A OD2 1 
ATOM   2473 N N   . VAL A 1 296 ? 9.741  4.040   -9.998  1.00 16.16 ? 296 VAL A N   1 
ATOM   2474 C CA  . VAL A 1 296 ? 9.047  4.738   -11.073 1.00 16.40 ? 296 VAL A CA  1 
ATOM   2475 C C   . VAL A 1 296 ? 9.068  3.925   -12.358 1.00 18.06 ? 296 VAL A C   1 
ATOM   2476 O O   . VAL A 1 296 ? 8.017  3.731   -12.959 1.00 19.14 ? 296 VAL A O   1 
ATOM   2477 C CB  . VAL A 1 296 ? 9.581  6.179   -11.258 1.00 16.18 ? 296 VAL A CB  1 
ATOM   2478 C CG1 . VAL A 1 296 ? 8.940  6.830   -12.468 1.00 16.59 ? 296 VAL A CG1 1 
ATOM   2479 C CG2 . VAL A 1 296 ? 9.293  7.003   -10.012 1.00 16.05 ? 296 VAL A CG2 1 
ATOM   2480 N N   . VAL A 1 297 ? 10.238 3.395   -12.748 1.00 18.39 ? 297 VAL A N   1 
ATOM   2481 C CA  . VAL A 1 297 ? 10.337 2.563   -13.952 1.00 19.89 ? 297 VAL A CA  1 
ATOM   2482 C C   . VAL A 1 297 ? 9.473  1.298   -13.807 1.00 20.88 ? 297 VAL A C   1 
ATOM   2483 O O   . VAL A 1 297 ? 8.737  0.942   -14.739 1.00 21.36 ? 297 VAL A O   1 
ATOM   2484 C CB  . VAL A 1 297 ? 11.811 2.192   -14.251 1.00 21.55 ? 297 VAL A CB  1 
ATOM   2485 C CG1 . VAL A 1 297 ? 11.910 1.180   -15.391 1.00 22.49 ? 297 VAL A CG1 1 
ATOM   2486 C CG2 . VAL A 1 297 ? 12.640 3.438   -14.563 1.00 22.68 ? 297 VAL A CG2 1 
ATOM   2487 N N   . ARG A 1 298 ? 9.549  0.644   -12.641 1.00 21.24 ? 298 ARG A N   1 
ATOM   2488 C CA  . ARG A 1 298 ? 8.807  -0.585  -12.372 1.00 22.55 ? 298 ARG A CA  1 
ATOM   2489 C C   . ARG A 1 298 ? 7.308  -0.361  -12.501 1.00 22.93 ? 298 ARG A C   1 
ATOM   2490 O O   . ARG A 1 298 ? 6.636  -1.115  -13.208 1.00 22.97 ? 298 ARG A O   1 
ATOM   2491 C CB  . ARG A 1 298 ? 9.156  -1.144  -10.976 1.00 25.03 ? 298 ARG A CB  1 
ATOM   2492 C CG  . ARG A 1 298 ? 8.689  -2.583  -10.744 1.00 29.79 ? 298 ARG A CG  1 
ATOM   2493 C CD  . ARG A 1 298 ? 8.979  -3.085  -9.331  1.00 34.67 ? 298 ARG A CD  1 
ATOM   2494 N NE  . ARG A 1 298 ? 10.404 -3.075  -8.999  1.00 39.16 ? 298 ARG A NE  1 
ATOM   2495 C CZ  . ARG A 1 298 ? 10.970 -2.244  -8.127  1.00 42.47 ? 298 ARG A CZ  1 
ATOM   2496 N NH1 . ARG A 1 298 ? 12.272 -2.306  -7.894  1.00 43.09 ? 298 ARG A NH1 1 
ATOM   2497 N NH2 . ARG A 1 298 ? 10.237 -1.347  -7.482  1.00 42.21 ? 298 ARG A NH2 1 
ATOM   2498 N N   . GLN A 1 299 ? 6.784  0.674   -11.846 1.00 23.07 ? 299 GLN A N   1 
ATOM   2499 C CA  . GLN A 1 299 ? 5.354  0.958   -11.884 1.00 23.81 ? 299 GLN A CA  1 
ATOM   2500 C C   . GLN A 1 299 ? 4.900  1.427   -13.238 1.00 25.68 ? 299 GLN A C   1 
ATOM   2501 O O   . GLN A 1 299 ? 3.853  0.988   -13.714 1.00 26.69 ? 299 GLN A O   1 
ATOM   2502 C CB  . GLN A 1 299 ? 4.957  1.970   -10.809 1.00 23.65 ? 299 GLN A CB  1 
ATOM   2503 C CG  . GLN A 1 299 ? 3.447  2.122   -10.708 1.00 23.14 ? 299 GLN A CG  1 
ATOM   2504 C CD  . GLN A 1 299 ? 2.957  2.977   -9.576  1.00 22.18 ? 299 GLN A CD  1 
ATOM   2505 O OE1 . GLN A 1 299 ? 1.844  3.497   -9.627  1.00 22.38 ? 299 GLN A OE1 1 
ATOM   2506 N NE2 . GLN A 1 299 ? 3.758  3.156   -8.534  1.00 20.10 ? 299 GLN A NE2 1 
ATOM   2507 N N   . CYS A 1 300 ? 5.691  2.286   -13.886 1.00 26.06 ? 300 CYS A N   1 
ATOM   2508 C CA  . CYS A 1 300 ? 5.337  2.786   -15.204 1.00 27.01 ? 300 CYS A CA  1 
ATOM   2509 C C   . CYS A 1 300 ? 5.445  1.714   -16.315 1.00 28.98 ? 300 CYS A C   1 
ATOM   2510 O O   . CYS A 1 300 ? 4.855  1.899   -17.375 1.00 29.26 ? 300 CYS A O   1 
ATOM   2511 C CB  . CYS A 1 300 ? 6.127  4.045   -15.545 1.00 26.34 ? 300 CYS A CB  1 
ATOM   2512 S SG  . CYS A 1 300 ? 5.721  5.471   -14.500 1.00 27.90 ? 300 CYS A SG  1 
ATOM   2513 N N   . SER A 1 301 ? 6.132  0.583   -16.063 1.00 30.28 ? 301 SER A N   1 
ATOM   2514 C CA  . SER A 1 301 ? 6.245  -0.481  -17.069 1.00 32.04 ? 301 SER A CA  1 
ATOM   2515 C C   . SER A 1 301 ? 5.465  -1.768  -16.734 1.00 33.71 ? 301 SER A C   1 
ATOM   2516 O O   . SER A 1 301 ? 5.292  -2.617  -17.604 1.00 34.43 ? 301 SER A O   1 
ATOM   2517 C CB  . SER A 1 301 ? 7.705  -0.806  -17.369 1.00 33.84 ? 301 SER A CB  1 
ATOM   2518 O OG  . SER A 1 301 ? 8.315  -1.500  -16.296 1.00 36.40 ? 301 SER A OG  1 
ATOM   2519 N N   . GLY A 1 302 ? 5.019  -1.910  -15.491 1.00 34.12 ? 302 GLY A N   1 
ATOM   2520 C CA  . GLY A 1 302 ? 4.222  -3.058  -15.071 1.00 35.05 ? 302 GLY A CA  1 
ATOM   2521 C C   . GLY A 1 302 ? 4.997  -4.334  -14.820 1.00 35.61 ? 302 GLY A C   1 
ATOM   2522 O O   . GLY A 1 302 ? 4.571  -5.413  -15.243 1.00 36.15 ? 302 GLY A O   1 
ATOM   2523 N N   . VAL A 1 303 ? 6.128  -4.228  -14.109 1.00 35.32 ? 303 VAL A N   1 
ATOM   2524 C CA  . VAL A 1 303 ? 6.954  -5.389  -13.780 1.00 35.32 ? 303 VAL A CA  1 
ATOM   2525 C C   . VAL A 1 303 ? 6.215  -6.275  -12.784 1.00 34.93 ? 303 VAL A C   1 
ATOM   2526 O O   . VAL A 1 303 ? 5.658  -5.767  -11.815 1.00 34.71 ? 303 VAL A O   1 
ATOM   2527 C CB  . VAL A 1 303 ? 8.320  -4.942  -13.211 1.00 36.13 ? 303 VAL A CB  1 
ATOM   2528 C CG1 . VAL A 1 303 ? 9.179  -6.136  -12.804 1.00 36.86 ? 303 VAL A CG1 1 
ATOM   2529 C CG2 . VAL A 1 303 ? 9.059  -4.069  -14.209 1.00 36.62 ? 303 VAL A CG2 1 
ATOM   2530 N N   A THR A 1 304 ? 6.200  -7.599  -13.004 0.50 34.73 ? 304 THR A N   1 
ATOM   2531 N N   B THR A 1 304 ? 6.201  -7.585  -13.044 0.50 34.72 ? 304 THR A N   1 
ATOM   2532 C CA  A THR A 1 304 ? 5.514  -8.516  -12.093 0.50 34.97 ? 304 THR A CA  1 
ATOM   2533 C CA  B THR A 1 304 ? 5.553  -8.566  -12.184 0.50 34.96 ? 304 THR A CA  1 
ATOM   2534 C C   A THR A 1 304 ? 6.476  -9.352  -11.246 0.50 35.09 ? 304 THR A C   1 
ATOM   2535 C C   B THR A 1 304 ? 6.556  -9.620  -11.706 0.50 35.18 ? 304 THR A C   1 
ATOM   2536 O O   A THR A 1 304 ? 6.038  -10.116 -10.384 0.50 34.91 ? 304 THR A O   1 
ATOM   2537 O O   B THR A 1 304 ? 7.751  -9.347  -11.597 0.50 35.09 ? 304 THR A O   1 
ATOM   2538 C CB  A THR A 1 304 ? 4.532  -9.384  -12.868 0.50 36.14 ? 304 THR A CB  1 
ATOM   2539 C CB  B THR A 1 304 ? 4.394  -9.205  -12.939 0.50 35.98 ? 304 THR A CB  1 
ATOM   2540 O OG1 A THR A 1 304 ? 5.255  -10.142 -13.839 0.50 37.13 ? 304 THR A OG1 1 
ATOM   2541 O OG1 B THR A 1 304 ? 4.903  -9.804  -14.134 0.50 36.92 ? 304 THR A OG1 1 
ATOM   2542 C CG2 A THR A 1 304 ? 3.471  -8.559  -13.555 0.50 36.53 ? 304 THR A CG2 1 
ATOM   2543 C CG2 B THR A 1 304 ? 3.329  -8.196  -13.297 0.50 36.25 ? 304 THR A CG2 1 
HETATM 2544 S S   . DMS B 2 .   ? 6.882  -28.125 21.472  1.00 20.06 ? 401 DMS A S   1 
HETATM 2545 O O   . DMS B 2 .   ? 7.674  -27.206 22.316  1.00 20.48 ? 401 DMS A O   1 
HETATM 2546 C C1  . DMS B 2 .   ? 5.955  -27.138 20.370  1.00 19.79 ? 401 DMS A C1  1 
HETATM 2547 C C2  . DMS B 2 .   ? 5.581  -28.752 22.497  1.00 19.86 ? 401 DMS A C2  1 
HETATM 2548 S S   . DMS C 2 .   ? 7.044  -21.256 28.847  1.00 48.64 ? 402 DMS A S   1 
HETATM 2549 O O   . DMS C 2 .   ? 6.922  -22.717 28.688  1.00 48.54 ? 402 DMS A O   1 
HETATM 2550 C C1  . DMS C 2 .   ? 5.390  -20.729 29.206  1.00 48.61 ? 402 DMS A C1  1 
HETATM 2551 C C2  . DMS C 2 .   ? 7.732  -21.050 30.463  1.00 48.75 ? 402 DMS A C2  1 
HETATM 2552 S S   . DMS D 2 .   ? 6.261  -1.076  -6.323  1.00 29.95 ? 403 DMS A S   1 
HETATM 2553 O O   . DMS D 2 .   ? 5.958  -2.533  -6.360  1.00 30.71 ? 403 DMS A O   1 
HETATM 2554 C C1  . DMS D 2 .   ? 7.022  -0.725  -7.858  1.00 30.37 ? 403 DMS A C1  1 
HETATM 2555 C C2  . DMS D 2 .   ? 7.596  -0.894  -5.175  1.00 30.14 ? 403 DMS A C2  1 
HETATM 2556 S S   . DMS E 2 .   ? 2.371  -18.855 7.984   1.00 36.23 ? 404 DMS A S   1 
HETATM 2557 O O   . DMS E 2 .   ? 1.975  -20.201 7.546   1.00 36.88 ? 404 DMS A O   1 
HETATM 2558 C C1  . DMS E 2 .   ? 3.628  -19.160 9.196   1.00 36.02 ? 404 DMS A C1  1 
HETATM 2559 C C2  . DMS E 2 .   ? 1.058  -18.333 9.062   1.00 36.25 ? 404 DMS A C2  1 
HETATM 2560 O O   . HOH F 3 .   ? 16.168 1.473   -5.859  1.00 46.52 ? 501 HOH A O   1 
HETATM 2561 O O   . HOH F 3 .   ? 14.078 -19.491 32.277  1.00 41.46 ? 502 HOH A O   1 
HETATM 2562 O O   . HOH F 3 .   ? 6.880  13.380  21.324  1.00 29.25 ? 503 HOH A O   1 
HETATM 2563 O O   . HOH F 3 .   ? 13.998 -10.881 31.006  1.00 35.36 ? 504 HOH A O   1 
HETATM 2564 O O   . HOH F 3 .   ? -0.912 17.057  -19.539 1.00 38.93 ? 505 HOH A O   1 
HETATM 2565 O O   . HOH F 3 .   ? -3.061 10.895  -16.794 1.00 40.86 ? 506 HOH A O   1 
HETATM 2566 O O   . HOH F 3 .   ? 6.044  5.803   1.306   1.00 24.97 ? 507 HOH A O   1 
HETATM 2567 O O   . HOH F 3 .   ? 2.799  4.893   20.226  1.00 34.61 ? 508 HOH A O   1 
HETATM 2568 O O   . HOH F 3 .   ? 24.406 -5.758  8.993   1.00 17.99 ? 509 HOH A O   1 
HETATM 2569 O O   . HOH F 3 .   ? 21.426 -20.287 30.771  1.00 23.30 ? 510 HOH A O   1 
HETATM 2570 O O   . HOH F 3 .   ? 11.397 31.677  -2.156  1.00 25.90 ? 511 HOH A O   1 
HETATM 2571 O O   . HOH F 3 .   ? 12.195 -27.051 22.943  1.00 19.83 ? 512 HOH A O   1 
HETATM 2572 O O   . HOH F 3 .   ? 19.756 10.134  -2.112  1.00 30.96 ? 513 HOH A O   1 
HETATM 2573 O O   . HOH F 3 .   ? 5.478  -17.689 1.918   1.00 19.67 ? 514 HOH A O   1 
HETATM 2574 O O   . HOH F 3 .   ? 8.621  24.377  -11.854 1.00 26.34 ? 515 HOH A O   1 
HETATM 2575 O O   . HOH F 3 .   ? 0.090  -17.755 15.613  1.00 35.61 ? 516 HOH A O   1 
HETATM 2576 O O   . HOH F 3 .   ? 9.022  -26.606 14.754  1.00 40.22 ? 517 HOH A O   1 
HETATM 2577 O O   . HOH F 3 .   ? 9.601  -23.263 23.053  1.00 21.34 ? 518 HOH A O   1 
HETATM 2578 O O   . HOH F 3 .   ? 7.168  -26.153 0.208   1.00 33.81 ? 519 HOH A O   1 
HETATM 2579 O O   . HOH F 3 .   ? 16.939 -5.562  33.520  1.00 37.83 ? 520 HOH A O   1 
HETATM 2580 O O   . HOH F 3 .   ? 8.175  -31.641 17.026  1.00 31.45 ? 521 HOH A O   1 
HETATM 2581 O O   . HOH F 3 .   ? 20.485 8.740   25.153  1.00 39.46 ? 522 HOH A O   1 
HETATM 2582 O O   . HOH F 3 .   ? 6.032  -8.497  8.633   1.00 14.96 ? 523 HOH A O   1 
HETATM 2583 O O   . HOH F 3 .   ? 13.232 10.946  19.529  1.00 48.19 ? 524 HOH A O   1 
HETATM 2584 O O   . HOH F 3 .   ? 3.638  22.182  -0.621  1.00 34.15 ? 525 HOH A O   1 
HETATM 2585 O O   . HOH F 3 .   ? 6.136  4.320   21.727  1.00 40.25 ? 526 HOH A O   1 
HETATM 2586 O O   . HOH F 3 .   ? 24.549 4.929   18.980  1.00 27.73 ? 527 HOH A O   1 
HETATM 2587 O O   . HOH F 3 .   ? 21.248 -12.985 34.361  1.00 37.99 ? 528 HOH A O   1 
HETATM 2588 O O   . HOH F 3 .   ? 4.472  26.774  -8.479  1.00 30.69 ? 529 HOH A O   1 
HETATM 2589 O O   . HOH F 3 .   ? 16.252 12.230  7.025   1.00 30.97 ? 530 HOH A O   1 
HETATM 2590 O O   . HOH F 3 .   ? 6.267  8.345   11.973  1.00 33.79 ? 531 HOH A O   1 
HETATM 2591 O O   . HOH F 3 .   ? 14.837 -9.578  -4.136  1.00 34.69 ? 532 HOH A O   1 
HETATM 2592 O O   . HOH F 3 .   ? 23.775 -14.714 27.189  1.00 19.51 ? 533 HOH A O   1 
HETATM 2593 O O   . HOH F 3 .   ? 12.117 31.027  -8.579  1.00 28.22 ? 534 HOH A O   1 
HETATM 2594 O O   . HOH F 3 .   ? 10.798 -24.784 2.844   1.00 18.90 ? 535 HOH A O   1 
HETATM 2595 O O   . HOH F 3 .   ? 18.416 -28.970 20.813  1.00 44.66 ? 536 HOH A O   1 
HETATM 2596 O O   . HOH F 3 .   ? 13.207 23.157  -18.628 1.00 23.28 ? 537 HOH A O   1 
HETATM 2597 O O   . HOH F 3 .   ? 1.305  22.918  -1.525  1.00 39.57 ? 538 HOH A O   1 
HETATM 2598 O O   . HOH F 3 .   ? 13.733 -16.538 32.742  1.00 42.72 ? 539 HOH A O   1 
HETATM 2599 O O   . HOH F 3 .   ? 20.769 -13.106 10.684  1.00 24.31 ? 540 HOH A O   1 
HETATM 2600 O O   . HOH F 3 .   ? 8.621  5.486   22.418  1.00 37.97 ? 541 HOH A O   1 
HETATM 2601 O O   . HOH F 3 .   ? 19.369 9.113   0.911   0.50 21.92 ? 542 HOH A O   1 
HETATM 2602 O O   . HOH F 3 .   ? 20.059 10.278  15.617  1.00 20.33 ? 543 HOH A O   1 
HETATM 2603 O O   . HOH F 3 .   ? 13.595 0.797   -5.476  1.00 24.59 ? 544 HOH A O   1 
HETATM 2604 O O   . HOH F 3 .   ? 15.233 18.533  -21.978 1.00 20.38 ? 545 HOH A O   1 
HETATM 2605 O O   . HOH F 3 .   ? 4.305  7.616   10.196  1.00 32.91 ? 546 HOH A O   1 
HETATM 2606 O O   . HOH F 3 .   ? 28.704 8.986   -11.711 1.00 37.15 ? 547 HOH A O   1 
HETATM 2607 O O   . HOH F 3 .   ? 20.309 -18.432 26.843  1.00 19.13 ? 548 HOH A O   1 
HETATM 2608 O O   . HOH F 3 .   ? -0.916 1.911   13.421  1.00 31.81 ? 549 HOH A O   1 
HETATM 2609 O O   . HOH F 3 .   ? 22.855 27.060  -0.065  1.00 31.20 ? 550 HOH A O   1 
HETATM 2610 O O   . HOH F 3 .   ? 14.655 26.081  4.261   1.00 21.96 ? 551 HOH A O   1 
HETATM 2611 O O   . HOH F 3 .   ? 3.751  4.190   -18.169 1.00 34.28 ? 552 HOH A O   1 
HETATM 2612 O O   . HOH F 3 .   ? 13.326 -24.508 3.825   1.00 22.78 ? 553 HOH A O   1 
HETATM 2613 O O   . HOH F 3 .   ? 27.169 26.220  -11.432 1.00 21.90 ? 554 HOH A O   1 
HETATM 2614 O O   . HOH F 3 .   ? 9.882  19.723  -0.456  1.00 21.00 ? 555 HOH A O   1 
HETATM 2615 O O   . HOH F 3 .   ? -3.265 28.392  -8.099  1.00 21.52 ? 556 HOH A O   1 
HETATM 2616 O O   . HOH F 3 .   ? 20.738 21.420  4.165   1.00 27.07 ? 557 HOH A O   1 
HETATM 2617 O O   . HOH F 3 .   ? 6.867  -23.050 20.986  1.00 15.42 ? 558 HOH A O   1 
HETATM 2618 O O   . HOH F 3 .   ? 8.877  28.045  -1.387  1.00 22.94 ? 559 HOH A O   1 
HETATM 2619 O O   . HOH F 3 .   ? 0.113  -1.132  12.039  1.00 27.87 ? 560 HOH A O   1 
HETATM 2620 O O   . HOH F 3 .   ? 2.365  -8.994  18.707  1.00 22.91 ? 561 HOH A O   1 
HETATM 2621 O O   . HOH F 3 .   ? 4.775  24.485  -18.488 1.00 38.08 ? 562 HOH A O   1 
HETATM 2622 O O   . HOH F 3 .   ? 11.512 21.778  -17.020 1.00 21.35 ? 563 HOH A O   1 
HETATM 2623 O O   . HOH F 3 .   ? -1.260 -19.317 22.131  1.00 37.41 ? 564 HOH A O   1 
HETATM 2624 O O   . HOH F 3 .   ? 23.016 1.706   15.920  1.00 19.55 ? 565 HOH A O   1 
HETATM 2625 O O   . HOH F 3 .   ? 22.194 19.573  0.676   1.00 26.37 ? 566 HOH A O   1 
HETATM 2626 O O   . HOH F 3 .   ? 8.161  -17.907 28.320  1.00 34.19 ? 567 HOH A O   1 
HETATM 2627 O O   . HOH F 3 .   ? 7.958  3.525   -3.456  1.00 17.12 ? 568 HOH A O   1 
HETATM 2628 O O   . HOH F 3 .   ? 15.855 -27.834 12.287  1.00 23.48 ? 569 HOH A O   1 
HETATM 2629 O O   . HOH F 3 .   ? 16.709 28.254  -20.308 1.00 19.84 ? 570 HOH A O   1 
HETATM 2630 O O   . HOH F 3 .   ? 8.450  15.959  1.017   1.00 29.83 ? 571 HOH A O   1 
HETATM 2631 O O   . HOH F 3 .   ? 9.777  6.249   5.698   1.00 15.43 ? 572 HOH A O   1 
HETATM 2632 O O   . HOH F 3 .   ? 17.679 -25.053 30.209  1.00 30.30 ? 573 HOH A O   1 
HETATM 2633 O O   . HOH F 3 .   ? -5.912 -4.357  9.377   1.00 39.55 ? 574 HOH A O   1 
HETATM 2634 O O   . HOH F 3 .   ? 25.363 9.442   -4.945  1.00 28.46 ? 575 HOH A O   1 
HETATM 2635 O O   . HOH F 3 .   ? 16.878 6.559   -3.938  1.00 17.95 ? 576 HOH A O   1 
HETATM 2636 O O   . HOH F 3 .   ? 12.105 -32.691 16.980  1.00 31.58 ? 577 HOH A O   1 
HETATM 2637 O O   . HOH F 3 .   ? 12.237 21.928  2.499   1.00 20.92 ? 578 HOH A O   1 
HETATM 2638 O O   . HOH F 3 .   ? 9.918  -25.725 22.117  1.00 14.76 ? 579 HOH A O   1 
HETATM 2639 O O   . HOH F 3 .   ? 21.216 28.768  -6.698  1.00 41.88 ? 580 HOH A O   1 
HETATM 2640 O O   . HOH F 3 .   ? 10.267 17.926  1.520   1.00 26.08 ? 581 HOH A O   1 
HETATM 2641 O O   . HOH F 3 .   ? 24.873 29.260  -8.891  1.00 23.50 ? 582 HOH A O   1 
HETATM 2642 O O   . HOH F 3 .   ? 18.869 10.206  13.140  1.00 19.66 ? 583 HOH A O   1 
HETATM 2643 O O   . HOH F 3 .   ? -1.740 -15.236 2.695   1.00 33.35 ? 584 HOH A O   1 
HETATM 2644 O O   . HOH F 3 .   ? 10.507 -0.544  -3.024  1.00 21.42 ? 585 HOH A O   1 
HETATM 2645 O O   . HOH F 3 .   ? 23.489 22.748  -17.286 1.00 16.05 ? 586 HOH A O   1 
HETATM 2646 O O   . HOH F 3 .   ? 13.322 21.382  -20.851 1.00 26.01 ? 587 HOH A O   1 
HETATM 2647 O O   . HOH F 3 .   ? 18.541 -8.076  -3.408  1.00 40.63 ? 588 HOH A O   1 
HETATM 2648 O O   . HOH F 3 .   ? 8.071  3.586   30.056  1.00 37.79 ? 589 HOH A O   1 
HETATM 2649 O O   . HOH F 3 .   ? -1.477 3.593   -1.801  1.00 42.67 ? 590 HOH A O   1 
HETATM 2650 O O   . HOH F 3 .   ? 3.602  22.218  -19.191 1.00 32.60 ? 591 HOH A O   1 
HETATM 2651 O O   . HOH F 3 .   ? 9.993  -17.767 -3.963  1.00 21.80 ? 592 HOH A O   1 
HETATM 2652 O O   . HOH F 3 .   ? 22.259 16.293  3.670   1.00 37.29 ? 593 HOH A O   1 
HETATM 2653 O O   . HOH F 3 .   ? 10.599 32.889  -5.240  1.00 50.44 ? 594 HOH A O   1 
HETATM 2654 O O   . HOH F 3 .   ? 13.521 12.427  17.221  1.00 36.62 ? 595 HOH A O   1 
HETATM 2655 O O   . HOH F 3 .   ? -3.864 -12.103 2.544   1.00 20.32 ? 596 HOH A O   1 
HETATM 2656 O O   . HOH F 3 .   ? 26.359 -5.686  17.729  1.00 34.04 ? 597 HOH A O   1 
HETATM 2657 O O   . HOH F 3 .   ? 0.896  -16.433 2.082   1.00 39.32 ? 598 HOH A O   1 
HETATM 2658 O O   . HOH F 3 .   ? 28.921 9.379   -15.273 1.00 32.13 ? 599 HOH A O   1 
HETATM 2659 O O   . HOH F 3 .   ? 24.011 13.123  -1.655  1.00 31.18 ? 600 HOH A O   1 
HETATM 2660 O O   . HOH F 3 .   ? 21.433 21.717  -18.735 1.00 17.60 ? 601 HOH A O   1 
HETATM 2661 O O   . HOH F 3 .   ? 1.773  1.863   0.024   1.00 26.63 ? 602 HOH A O   1 
HETATM 2662 O O   . HOH F 3 .   ? 7.494  -28.340 15.770  1.00 33.19 ? 603 HOH A O   1 
HETATM 2663 O O   . HOH F 3 .   ? 15.633 -5.640  20.179  1.00 12.60 ? 604 HOH A O   1 
HETATM 2664 O O   . HOH F 3 .   ? 22.115 9.845   5.153   1.00 29.86 ? 605 HOH A O   1 
HETATM 2665 O O   . HOH F 3 .   ? 24.327 -8.927  20.642  1.00 20.53 ? 606 HOH A O   1 
HETATM 2666 O O   . HOH F 3 .   ? 16.826 -18.849 7.693   1.00 18.59 ? 607 HOH A O   1 
HETATM 2667 O O   . HOH F 3 .   ? 28.679 18.724  -8.356  1.00 35.42 ? 608 HOH A O   1 
HETATM 2668 O O   . HOH F 3 .   ? 24.424 -0.652  12.999  1.00 27.63 ? 609 HOH A O   1 
HETATM 2669 O O   . HOH F 3 .   ? -0.724 22.828  -3.129  1.00 39.81 ? 610 HOH A O   1 
HETATM 2670 O O   . HOH F 3 .   ? 19.959 5.204   -1.851  1.00 27.89 ? 611 HOH A O   1 
HETATM 2671 O O   . HOH F 3 .   ? 15.062 26.996  -12.204 1.00 18.02 ? 612 HOH A O   1 
HETATM 2672 O O   . HOH F 3 .   ? 8.199  -28.395 6.565   1.00 25.90 ? 613 HOH A O   1 
HETATM 2673 O O   . HOH F 3 .   ? 7.788  -24.522 25.639  1.00 18.95 ? 614 HOH A O   1 
HETATM 2674 O O   . HOH F 3 .   ? 10.042 -5.817  25.008  1.00 36.65 ? 615 HOH A O   1 
HETATM 2675 O O   . HOH F 3 .   ? 22.116 2.055   5.700   1.00 36.41 ? 616 HOH A O   1 
HETATM 2676 O O   . HOH F 3 .   ? 3.693  -17.399 20.860  1.00 18.97 ? 617 HOH A O   1 
HETATM 2677 O O   . HOH F 3 .   ? 26.732 23.577  -4.772  1.00 19.11 ? 618 HOH A O   1 
HETATM 2678 O O   . HOH F 3 .   ? 9.585  10.091  -4.896  1.00 12.16 ? 619 HOH A O   1 
HETATM 2679 O O   . HOH F 3 .   ? 1.295  -21.833 9.645   1.00 55.13 ? 620 HOH A O   1 
HETATM 2680 O O   . HOH F 3 .   ? 22.839 -7.292  34.441  1.00 27.63 ? 621 HOH A O   1 
HETATM 2681 O O   . HOH F 3 .   ? 18.961 -27.689 9.426   1.00 43.04 ? 622 HOH A O   1 
HETATM 2682 O O   . HOH F 3 .   ? 21.521 10.599  -17.013 1.00 25.46 ? 623 HOH A O   1 
HETATM 2683 O O   . HOH F 3 .   ? 13.990 14.918  12.502  1.00 32.85 ? 624 HOH A O   1 
HETATM 2684 O O   . HOH F 3 .   ? 1.918  -11.990 25.974  1.00 35.35 ? 625 HOH A O   1 
HETATM 2685 O O   . HOH F 3 .   ? -4.038 -9.431  16.969  1.00 48.81 ? 626 HOH A O   1 
HETATM 2686 O O   . HOH F 3 .   ? 13.366 19.059  3.371   1.00 28.20 ? 627 HOH A O   1 
HETATM 2687 O O   . HOH F 3 .   ? 24.678 1.909   12.377  1.00 46.47 ? 628 HOH A O   1 
HETATM 2688 O O   . HOH F 3 .   ? 14.580 -25.790 26.928  1.00 17.27 ? 629 HOH A O   1 
HETATM 2689 O O   . HOH F 3 .   ? 15.757 -12.840 31.816  1.00 22.74 ? 630 HOH A O   1 
HETATM 2690 O O   . HOH F 3 .   ? 14.529 -20.206 0.077   1.00 29.75 ? 631 HOH A O   1 
HETATM 2691 O O   . HOH F 3 .   ? 10.744 -23.544 0.343   1.00 18.47 ? 632 HOH A O   1 
HETATM 2692 O O   . HOH F 3 .   ? 2.570  13.675  -20.732 1.00 43.65 ? 633 HOH A O   1 
HETATM 2693 O O   . HOH F 3 .   ? 5.372  -6.477  21.881  1.00 27.60 ? 634 HOH A O   1 
HETATM 2694 O O   . HOH F 3 .   ? 3.140  9.142   -21.338 1.00 30.01 ? 635 HOH A O   1 
HETATM 2695 O O   . HOH F 3 .   ? 19.977 -21.182 28.743  1.00 32.10 ? 636 HOH A O   1 
HETATM 2696 O O   . HOH F 3 .   ? 7.570  12.013  0.722   1.00 33.53 ? 637 HOH A O   1 
HETATM 2697 O O   . HOH F 3 .   ? 12.447 11.173  10.477  1.00 26.80 ? 638 HOH A O   1 
HETATM 2698 O O   . HOH F 3 .   ? 15.757 6.369   -14.440 1.00 24.76 ? 639 HOH A O   1 
HETATM 2699 O O   . HOH F 3 .   ? 17.547 27.500  -12.889 1.00 19.19 ? 640 HOH A O   1 
HETATM 2700 O O   . HOH F 3 .   ? 5.057  -17.229 28.359  1.00 47.39 ? 641 HOH A O   1 
HETATM 2701 O O   . HOH F 3 .   ? -2.486 12.802  -14.220 1.00 42.13 ? 642 HOH A O   1 
HETATM 2702 O O   . HOH F 3 .   ? -4.994 23.645  -3.052  1.00 32.21 ? 643 HOH A O   1 
HETATM 2703 O O   . HOH F 3 .   ? -0.389 -15.332 10.266  1.00 36.06 ? 644 HOH A O   1 
HETATM 2704 O O   . HOH F 3 .   ? 5.665  2.461   -4.750  1.00 17.90 ? 645 HOH A O   1 
HETATM 2705 O O   . HOH F 3 .   ? 5.266  -27.778 14.491  1.00 36.75 ? 646 HOH A O   1 
HETATM 2706 O O   . HOH F 3 .   ? 2.594  25.678  -16.824 1.00 30.95 ? 647 HOH A O   1 
HETATM 2707 O O   . HOH F 3 .   ? 22.547 8.950   -2.317  1.00 43.74 ? 648 HOH A O   1 
HETATM 2708 O O   . HOH F 3 .   ? 15.056 -5.071  0.319   1.00 20.13 ? 649 HOH A O   1 
HETATM 2709 O O   . HOH F 3 .   ? 18.804 -7.696  6.107   1.00 16.54 ? 650 HOH A O   1 
HETATM 2710 O O   . HOH F 3 .   ? 6.258  2.386   -7.542  1.00 22.14 ? 651 HOH A O   1 
HETATM 2711 O O   . HOH F 3 .   ? 25.440 -15.867 12.089  1.00 45.56 ? 652 HOH A O   1 
HETATM 2712 O O   . HOH F 3 .   ? 13.858 31.054  -2.000  1.00 31.40 ? 653 HOH A O   1 
HETATM 2713 O O   . HOH F 3 .   ? 3.992  -22.184 7.072   1.00 17.77 ? 654 HOH A O   1 
HETATM 2714 O O   . HOH F 3 .   ? 16.781 4.789   30.472  1.00 57.67 ? 655 HOH A O   1 
HETATM 2715 O O   . HOH F 3 .   ? 14.653 -22.055 31.952  1.00 32.65 ? 656 HOH A O   1 
HETATM 2716 O O   . HOH F 3 .   ? 13.879 4.396   -20.671 1.00 28.86 ? 657 HOH A O   1 
HETATM 2717 O O   . HOH F 3 .   ? 27.708 -4.709  14.373  1.00 45.60 ? 658 HOH A O   1 
HETATM 2718 O O   . HOH F 3 .   ? -2.375 19.163  -11.398 1.00 31.14 ? 659 HOH A O   1 
HETATM 2719 O O   . HOH F 3 .   ? 9.946  -10.999 28.175  1.00 34.34 ? 660 HOH A O   1 
HETATM 2720 O O   . HOH F 3 .   ? 16.584 2.526   12.374  1.00 14.44 ? 661 HOH A O   1 
HETATM 2721 O O   . HOH F 3 .   ? 7.870  23.887  -2.281  1.00 26.01 ? 662 HOH A O   1 
HETATM 2722 O O   . HOH F 3 .   ? 15.076 11.269  -25.013 1.00 30.97 ? 663 HOH A O   1 
HETATM 2723 O O   . HOH F 3 .   ? 12.776 -3.174  -5.257  1.00 33.42 ? 664 HOH A O   1 
HETATM 2724 O O   . HOH F 3 .   ? 17.673 16.856  14.835  1.00 35.96 ? 665 HOH A O   1 
HETATM 2725 O O   . HOH F 3 .   ? -5.618 24.316  -7.513  1.00 20.87 ? 666 HOH A O   1 
HETATM 2726 O O   . HOH F 3 .   ? 29.467 15.778  -12.676 1.00 32.03 ? 667 HOH A O   1 
HETATM 2727 O O   . HOH F 3 .   ? -2.615 16.225  -9.453  1.00 26.89 ? 668 HOH A O   1 
HETATM 2728 O O   . HOH F 3 .   ? 20.970 6.298   19.867  1.00 27.96 ? 669 HOH A O   1 
HETATM 2729 O O   . HOH F 3 .   ? 22.051 -18.298 38.812  1.00 31.27 ? 670 HOH A O   1 
HETATM 2730 O O   . HOH F 3 .   ? 22.550 7.382   -17.399 1.00 24.21 ? 671 HOH A O   1 
HETATM 2731 O O   . HOH F 3 .   ? 20.505 18.890  3.164   1.00 33.29 ? 672 HOH A O   1 
HETATM 2732 O O   . HOH F 3 .   ? 21.340 -1.629  20.448  1.00 16.34 ? 673 HOH A O   1 
HETATM 2733 O O   . HOH F 3 .   ? -0.741 -15.736 14.250  1.00 30.76 ? 674 HOH A O   1 
HETATM 2734 O O   . HOH F 3 .   ? 23.323 20.417  -1.600  1.00 29.58 ? 675 HOH A O   1 
HETATM 2735 O O   . HOH F 3 .   ? 1.456  8.663   -6.092  1.00 38.82 ? 676 HOH A O   1 
HETATM 2736 O O   . HOH F 3 .   ? 17.887 4.741   -6.103  1.00 34.71 ? 677 HOH A O   1 
HETATM 2737 O O   . HOH F 3 .   ? 14.269 5.280   22.766  1.00 24.58 ? 678 HOH A O   1 
HETATM 2738 O O   . HOH F 3 .   ? 27.355 20.815  -5.391  1.00 24.25 ? 679 HOH A O   1 
HETATM 2739 O O   . HOH F 3 .   ? 9.720  -1.209  21.229  1.00 30.93 ? 680 HOH A O   1 
HETATM 2740 O O   . HOH F 3 .   ? 2.024  11.322  -5.624  1.00 22.74 ? 681 HOH A O   1 
HETATM 2741 O O   . HOH F 3 .   ? 9.861  24.688  -0.545  1.00 22.75 ? 682 HOH A O   1 
HETATM 2742 O O   . HOH F 3 .   ? 20.486 -1.656  24.001  1.00 24.64 ? 683 HOH A O   1 
HETATM 2743 O O   . HOH F 3 .   ? 23.225 2.694   9.309   1.00 22.82 ? 684 HOH A O   1 
HETATM 2744 O O   . HOH F 3 .   ? 27.418 16.923  -6.933  1.00 31.40 ? 685 HOH A O   1 
HETATM 2745 O O   . HOH F 3 .   ? 16.157 -27.895 23.992  1.00 21.03 ? 686 HOH A O   1 
HETATM 2746 O O   . HOH F 3 .   ? 18.371 -16.308 -2.702  1.00 39.26 ? 687 HOH A O   1 
HETATM 2747 O O   . HOH F 3 .   ? 25.461 -11.702 20.577  1.00 40.43 ? 688 HOH A O   1 
HETATM 2748 O O   . HOH F 3 .   ? 22.395 -0.560  18.161  1.00 15.98 ? 689 HOH A O   1 
HETATM 2749 O O   . HOH F 3 .   ? 11.106 -22.190 32.650  1.00 28.72 ? 690 HOH A O   1 
HETATM 2750 O O   . HOH F 3 .   ? 13.906 15.879  -26.087 1.00 40.25 ? 691 HOH A O   1 
HETATM 2751 O O   . HOH F 3 .   ? 3.233  28.434  -3.275  1.00 28.74 ? 692 HOH A O   1 
HETATM 2752 O O   . HOH F 3 .   ? 22.874 -2.369  16.096  1.00 16.71 ? 693 HOH A O   1 
HETATM 2753 O O   . HOH F 3 .   ? 5.924  -4.719  19.944  1.00 29.98 ? 694 HOH A O   1 
HETATM 2754 O O   . HOH F 3 .   ? 13.872 17.335  10.417  1.00 36.01 ? 695 HOH A O   1 
HETATM 2755 O O   . HOH F 3 .   ? -3.730 23.139  -15.560 1.00 97.94 ? 696 HOH A O   1 
HETATM 2756 O O   . HOH F 3 .   ? 8.299  -10.717 30.288  1.00 47.50 ? 697 HOH A O   1 
HETATM 2757 O O   . HOH F 3 .   ? 21.543 -1.801  26.438  1.00 47.98 ? 698 HOH A O   1 
HETATM 2758 O O   . HOH F 3 .   ? 18.028 -23.973 26.108  1.00 19.47 ? 699 HOH A O   1 
HETATM 2759 O O   . HOH F 3 .   ? 12.908 18.528  -23.180 1.00 41.68 ? 700 HOH A O   1 
HETATM 2760 O O   . HOH F 3 .   ? 2.949  30.284  -11.274 1.00 37.62 ? 701 HOH A O   1 
HETATM 2761 O O   . HOH F 3 .   ? 20.081 -20.090 16.613  1.00 22.76 ? 702 HOH A O   1 
HETATM 2762 O O   . HOH F 3 .   ? 18.378 30.888  -7.178  1.00 34.12 ? 703 HOH A O   1 
HETATM 2763 O O   . HOH F 3 .   ? 5.351  -31.635 18.500  1.00 40.71 ? 704 HOH A O   1 
HETATM 2764 O O   . HOH F 3 .   ? 0.701  25.514  -2.225  1.00 36.15 ? 705 HOH A O   1 
HETATM 2765 O O   . HOH F 3 .   ? 25.191 16.426  -14.367 1.00 24.82 ? 706 HOH A O   1 
HETATM 2766 O O   . HOH F 3 .   ? 21.234 -13.358 2.280   1.00 27.41 ? 707 HOH A O   1 
HETATM 2767 O O   . HOH F 3 .   ? 7.239  19.679  -0.526  1.00 19.53 ? 708 HOH A O   1 
HETATM 2768 O O   . HOH F 3 .   ? 26.231 -10.821 18.148  1.00 29.32 ? 709 HOH A O   1 
HETATM 2769 O O   . HOH F 3 .   ? 18.272 24.759  5.918   1.00 42.75 ? 710 HOH A O   1 
HETATM 2770 O O   . HOH F 3 .   ? 23.954 -16.170 21.645  1.00 23.30 ? 711 HOH A O   1 
HETATM 2771 O O   . HOH F 3 .   ? 10.555 -16.892 30.368  1.00 33.54 ? 712 HOH A O   1 
HETATM 2772 O O   . HOH F 3 .   ? -3.214 21.063  -9.741  1.00 34.02 ? 713 HOH A O   1 
HETATM 2773 O O   . HOH F 3 .   ? -2.136 9.260   -10.450 1.00 40.46 ? 714 HOH A O   1 
HETATM 2774 O O   . HOH F 3 .   ? 11.910 -29.685 8.498   1.00 34.74 ? 715 HOH A O   1 
HETATM 2775 O O   . HOH F 3 .   ? 1.343  -16.891 12.512  1.00 27.31 ? 716 HOH A O   1 
HETATM 2776 O O   . HOH F 3 .   ? 13.914 19.690  7.284   1.00 37.82 ? 717 HOH A O   1 
HETATM 2777 O O   . HOH F 3 .   ? -0.234 16.076  -0.146  0.50 11.47 ? 718 HOH A O   1 
HETATM 2778 O O   . HOH F 3 .   ? 24.548 -7.687  26.198  1.00 36.32 ? 719 HOH A O   1 
HETATM 2779 O O   . HOH F 3 .   ? 18.171 27.334  4.952   1.00 53.03 ? 720 HOH A O   1 
HETATM 2780 O O   . HOH F 3 .   ? 11.863 12.861  14.635  1.00 54.98 ? 721 HOH A O   1 
HETATM 2781 O O   . HOH F 3 .   ? 19.214 -6.192  32.419  1.00 25.40 ? 722 HOH A O   1 
HETATM 2782 O O   . HOH F 3 .   ? -0.227 7.570   -3.969  1.00 37.09 ? 723 HOH A O   1 
HETATM 2783 O O   . HOH F 3 .   ? 19.243 12.398  -3.622  1.00 19.12 ? 724 HOH A O   1 
HETATM 2784 O O   . HOH F 3 .   ? 23.410 -6.008  1.926   1.00 25.91 ? 725 HOH A O   1 
HETATM 2785 O O   . HOH F 3 .   ? 7.624  -8.536  -15.424 1.00 46.55 ? 726 HOH A O   1 
HETATM 2786 O O   . HOH F 3 .   ? 23.169 -8.425  4.161   1.00 50.23 ? 727 HOH A O   1 
HETATM 2787 O O   . HOH F 3 .   ? 20.967 16.913  -17.778 1.00 17.97 ? 728 HOH A O   1 
HETATM 2788 O O   . HOH F 3 .   ? 3.435  -8.065  24.643  1.00 37.20 ? 729 HOH A O   1 
HETATM 2789 O O   . HOH F 3 .   ? 2.421  -19.701 21.721  1.00 19.80 ? 730 HOH A O   1 
HETATM 2790 O O   . HOH F 3 .   ? 20.354 -26.799 18.082  1.00 35.93 ? 731 HOH A O   1 
HETATM 2791 O O   . HOH F 3 .   ? 26.885 -9.220  10.443  1.00 44.15 ? 732 HOH A O   1 
HETATM 2792 O O   . HOH F 3 .   ? 1.564  -8.119  21.531  1.00 37.29 ? 733 HOH A O   1 
HETATM 2793 O O   . HOH F 3 .   ? 15.456 24.744  7.786   1.00 37.81 ? 734 HOH A O   1 
HETATM 2794 O O   . HOH F 3 .   ? 27.760 21.772  -11.674 1.00 17.55 ? 735 HOH A O   1 
HETATM 2795 O O   . HOH F 3 .   ? -5.506 20.181  -8.002  1.00 40.32 ? 736 HOH A O   1 
HETATM 2796 O O   . HOH F 3 .   ? 11.915 15.221  4.229   1.00 32.50 ? 737 HOH A O   1 
HETATM 2797 O O   . HOH F 3 .   ? 30.151 25.265  -10.687 1.00 30.25 ? 738 HOH A O   1 
HETATM 2798 O O   . HOH F 3 .   ? 20.827 -22.801 22.064  1.00 21.95 ? 739 HOH A O   1 
HETATM 2799 O O   . HOH F 3 .   ? 13.583 -14.012 33.010  1.00 38.07 ? 740 HOH A O   1 
HETATM 2800 O O   . HOH F 3 .   ? 0.455  1.284   20.771  1.00 47.74 ? 741 HOH A O   1 
HETATM 2801 O O   . HOH F 3 .   ? -0.514 19.449  -15.740 1.00 36.34 ? 742 HOH A O   1 
HETATM 2802 O O   . HOH F 3 .   ? 23.836 -4.507  23.876  1.00 50.45 ? 743 HOH A O   1 
HETATM 2803 O O   . HOH F 3 .   ? 3.878  20.684  -21.337 1.00 32.39 ? 744 HOH A O   1 
HETATM 2804 O O   . HOH F 3 .   ? 24.290 -15.929 16.833  1.00 38.93 ? 745 HOH A O   1 
HETATM 2805 O O   . HOH F 3 .   ? 23.201 -5.397  26.412  1.00 24.88 ? 746 HOH A O   1 
HETATM 2806 O O   . HOH F 3 .   ? 26.273 20.548  -14.032 1.00 22.96 ? 747 HOH A O   1 
HETATM 2807 O O   . HOH F 3 .   ? 2.975  2.530   24.921  1.00 30.68 ? 748 HOH A O   1 
HETATM 2808 O O   . HOH F 3 .   ? 10.919 -11.853 30.486  1.00 37.95 ? 749 HOH A O   1 
HETATM 2809 O O   . HOH F 3 .   ? 20.396 13.586  9.082   1.00 33.87 ? 750 HOH A O   1 
HETATM 2810 O O   . HOH F 3 .   ? 11.865 4.048   22.653  1.00 33.22 ? 751 HOH A O   1 
HETATM 2811 O O   . HOH F 3 .   ? 27.729 -7.194  12.023  1.00 36.54 ? 752 HOH A O   1 
HETATM 2812 O O   . HOH F 3 .   ? 17.618 22.329  9.554   1.00 40.97 ? 753 HOH A O   1 
HETATM 2813 O O   . HOH F 3 .   ? 8.941  -7.897  -8.369  1.00 32.94 ? 754 HOH A O   1 
HETATM 2814 O O   . HOH F 3 .   ? 11.761 -29.800 22.589  1.00 19.37 ? 755 HOH A O   1 
HETATM 2815 O O   . HOH F 3 .   ? 28.635 10.717  -8.101  1.00 30.16 ? 756 HOH A O   1 
HETATM 2816 O O   . HOH F 3 .   ? 9.498  1.361   21.295  1.00 24.46 ? 757 HOH A O   1 
HETATM 2817 O O   . HOH F 3 .   ? 9.182  28.999  -17.474 1.00 26.72 ? 758 HOH A O   1 
HETATM 2818 O O   . HOH F 3 .   ? 16.203 30.204  -2.976  1.00 42.95 ? 759 HOH A O   1 
HETATM 2819 O O   . HOH F 3 .   ? 11.088 -31.620 10.226  1.00 43.15 ? 760 HOH A O   1 
HETATM 2820 O O   . HOH F 3 .   ? 20.093 -25.462 22.433  1.00 26.03 ? 761 HOH A O   1 
HETATM 2821 O O   . HOH F 3 .   ? 28.829 14.538  -8.128  1.00 34.41 ? 762 HOH A O   1 
HETATM 2822 O O   . HOH F 3 .   ? 3.441  24.795  -1.613  1.00 34.84 ? 763 HOH A O   1 
HETATM 2823 O O   . HOH F 3 .   ? 20.202 14.527  -19.039 1.00 33.34 ? 764 HOH A O   1 
HETATM 2824 O O   . HOH F 3 .   ? 0.115  -27.182 17.907  1.00 30.24 ? 765 HOH A O   1 
HETATM 2825 O O   . HOH F 3 .   ? 1.044  -16.222 23.465  1.00 44.28 ? 766 HOH A O   1 
HETATM 2826 O O   . HOH F 3 .   ? -2.627 17.627  -15.519 1.00 60.97 ? 767 HOH A O   1 
HETATM 2827 O O   . HOH F 3 .   ? 16.474 3.496   -7.806  1.00 29.34 ? 768 HOH A O   1 
HETATM 2828 O O   . HOH F 3 .   ? 24.409 -4.330  16.668  1.00 28.43 ? 769 HOH A O   1 
HETATM 2829 O O   . HOH F 3 .   ? 16.789 -18.630 -0.780  1.00 27.06 ? 770 HOH A O   1 
HETATM 2830 O O   . HOH F 3 .   ? 25.012 13.875  -17.225 1.00 25.24 ? 771 HOH A O   1 
HETATM 2831 O O   . HOH F 3 .   ? 6.492  -8.329  -7.853  1.00 39.75 ? 772 HOH A O   1 
HETATM 2832 O O   . HOH F 3 .   ? 20.068 -0.155  -1.012  1.00 35.16 ? 773 HOH A O   1 
HETATM 2833 O O   . HOH F 3 .   ? -0.000 -0.407  -0.000  0.50 24.99 ? 774 HOH A O   1 
HETATM 2834 O O   . HOH F 3 .   ? 11.274 -2.559  -16.545 1.00 43.12 ? 775 HOH A O   1 
HETATM 2835 O O   . HOH F 3 .   ? -1.568 6.148   -2.378  1.00 39.83 ? 776 HOH A O   1 
HETATM 2836 O O   . HOH F 3 .   ? -4.782 26.408  -9.310  1.00 22.16 ? 777 HOH A O   1 
HETATM 2837 O O   . HOH F 3 .   ? 16.309 -2.605  -2.855  1.00 41.31 ? 778 HOH A O   1 
HETATM 2838 O O   . HOH F 3 .   ? 30.825 20.967  -5.604  1.00 39.69 ? 779 HOH A O   1 
HETATM 2839 O O   . HOH F 3 .   ? 15.578 -19.046 34.790  1.00 41.80 ? 780 HOH A O   1 
HETATM 2840 O O   . HOH F 3 .   ? -2.125 -3.200  18.826  1.00 41.36 ? 781 HOH A O   1 
HETATM 2841 O O   . HOH F 3 .   ? 23.956 -20.421 20.945  1.00 45.16 ? 782 HOH A O   1 
HETATM 2842 O O   . HOH F 3 .   ? 12.859 22.637  6.077   1.00 35.21 ? 783 HOH A O   1 
HETATM 2843 O O   . HOH F 3 .   ? 25.214 -7.886  22.805  1.00 37.18 ? 784 HOH A O   1 
HETATM 2844 O O   . HOH F 3 .   ? 6.955  -15.138 -8.159  1.00 53.30 ? 785 HOH A O   1 
HETATM 2845 O O   . HOH F 3 .   ? 26.675 27.198  -8.963  1.00 30.23 ? 786 HOH A O   1 
HETATM 2846 O O   . HOH F 3 .   ? 5.969  2.060   28.913  1.00 39.92 ? 787 HOH A O   1 
HETATM 2847 O O   . HOH F 3 .   ? 3.824  -29.082 18.300  1.00 39.98 ? 788 HOH A O   1 
HETATM 2848 O O   . HOH F 3 .   ? 5.982  -23.035 -1.144  1.00 38.34 ? 789 HOH A O   1 
HETATM 2849 O O   . HOH F 3 .   ? 2.922  -18.050 1.197   1.00 32.81 ? 790 HOH A O   1 
HETATM 2850 O O   . HOH F 3 .   ? 21.637 -7.541  6.163   1.00 28.51 ? 791 HOH A O   1 
HETATM 2851 O O   . HOH F 3 .   ? 20.695 25.668  5.052   1.00 48.77 ? 792 HOH A O   1 
HETATM 2852 O O   . HOH F 3 .   ? 21.965 -17.907 23.656  1.00 32.28 ? 793 HOH A O   1 
HETATM 2853 O O   . HOH F 3 .   ? 3.738  9.887   14.440  1.00 38.47 ? 794 HOH A O   1 
HETATM 2854 O O   . HOH F 3 .   ? 7.546  -34.937 19.762  1.00 35.53 ? 795 HOH A O   1 
HETATM 2855 O O   . HOH F 3 .   ? 19.252 -11.117 34.347  1.00 37.85 ? 796 HOH A O   1 
HETATM 2856 O O   . HOH F 3 .   ? 17.203 15.425  -23.516 1.00 36.42 ? 797 HOH A O   1 
HETATM 2857 O O   . HOH F 3 .   ? 25.973 23.296  -2.028  1.00 29.90 ? 798 HOH A O   1 
HETATM 2858 O O   . HOH F 3 .   ? 17.194 -10.402 -5.842  1.00 42.68 ? 799 HOH A O   1 
HETATM 2859 O O   . HOH F 3 .   ? 8.784  -4.353  26.547  1.00 44.39 ? 800 HOH A O   1 
HETATM 2860 O O   . HOH F 3 .   ? 17.638 -17.925 37.524  1.00 49.93 ? 801 HOH A O   1 
HETATM 2861 O O   . HOH F 3 .   ? 12.370 32.802  -12.287 1.00 44.37 ? 802 HOH A O   1 
HETATM 2862 O O   . HOH F 3 .   ? 2.872  -1.757  -11.757 1.00 38.02 ? 803 HOH A O   1 
HETATM 2863 O O   . HOH F 3 .   ? 20.613 4.079   -5.766  1.00 40.55 ? 804 HOH A O   1 
HETATM 2864 O O   . HOH F 3 .   ? 14.640 -29.204 9.936   1.00 30.84 ? 805 HOH A O   1 
HETATM 2865 O O   . HOH F 3 .   ? 17.978 -19.808 33.834  1.00 31.41 ? 806 HOH A O   1 
HETATM 2866 O O   . HOH F 3 .   ? 15.789 -25.802 6.748   1.00 34.39 ? 807 HOH A O   1 
HETATM 2867 O O   . HOH F 3 .   ? 5.765  11.051  11.864  1.00 47.77 ? 808 HOH A O   1 
HETATM 2868 O O   . HOH F 3 .   ? 20.630 8.871   18.299  1.00 34.56 ? 809 HOH A O   1 
HETATM 2869 O O   . HOH F 3 .   ? 28.704 24.207  -12.425 1.00 28.48 ? 810 HOH A O   1 
HETATM 2870 O O   . HOH F 3 .   ? 0.105  -17.197 4.667   1.00 37.28 ? 811 HOH A O   1 
HETATM 2871 O O   . HOH F 3 .   ? 22.401 -22.767 19.930  1.00 34.52 ? 812 HOH A O   1 
HETATM 2872 O O   . HOH F 3 .   ? 18.717 -18.428 1.379   1.00 41.70 ? 813 HOH A O   1 
HETATM 2873 O O   . HOH F 3 .   ? 17.792 -22.269 33.181  1.00 42.81 ? 814 HOH A O   1 
HETATM 2874 O O   . HOH F 3 .   ? 20.668 -22.530 17.546  1.00 24.89 ? 815 HOH A O   1 
HETATM 2875 O O   . HOH F 3 .   ? 7.721  -5.547  22.694  1.00 46.81 ? 816 HOH A O   1 
HETATM 2876 O O   . HOH F 3 .   ? 20.766 5.826   -19.089 1.00 39.70 ? 817 HOH A O   1 
HETATM 2877 O O   . HOH F 3 .   ? 28.111 9.358   -5.026  1.00 37.59 ? 818 HOH A O   1 
HETATM 2878 O O   . HOH F 3 .   ? 25.908 -14.886 15.182  1.00 37.07 ? 819 HOH A O   1 
HETATM 2879 O O   . HOH F 3 .   ? 14.701 -6.924  -4.448  1.00 39.83 ? 820 HOH A O   1 
HETATM 2880 O O   . HOH F 3 .   ? 21.178 6.636   -5.226  1.00 32.30 ? 821 HOH A O   1 
HETATM 2881 O O   . HOH F 3 .   ? 24.874 10.464  -2.477  1.00 28.16 ? 822 HOH A O   1 
HETATM 2882 O O   . HOH F 3 .   ? -2.947 28.034  -1.971  1.00 40.10 ? 823 HOH A O   1 
HETATM 2883 O O   . HOH F 3 .   ? 14.364 20.232  9.961   1.00 64.02 ? 824 HOH A O   1 
HETATM 2884 O O   . HOH F 3 .   ? 1.998  9.130   -3.466  1.00 43.88 ? 825 HOH A O   1 
HETATM 2885 O O   . HOH F 3 .   ? 11.115 20.848  -19.436 1.00 28.04 ? 826 HOH A O   1 
HETATM 2886 O O   . HOH F 3 .   ? 10.569 -34.359 21.224  1.00 30.05 ? 827 HOH A O   1 
HETATM 2887 O O   . HOH F 3 .   ? 7.992  2.820   22.784  1.00 30.45 ? 828 HOH A O   1 
HETATM 2888 O O   . HOH F 3 .   ? 23.890 6.960   -5.408  1.00 41.41 ? 829 HOH A O   1 
HETATM 2889 O O   . HOH F 3 .   ? -4.860 -11.927 5.027   1.00 34.53 ? 830 HOH A O   1 
HETATM 2890 O O   . HOH F 3 .   ? -5.504 22.417  -9.461  1.00 35.31 ? 831 HOH A O   1 
HETATM 2891 O O   . HOH F 3 .   ? 21.823 -25.766 20.312  1.00 35.08 ? 832 HOH A O   1 
HETATM 2892 O O   . HOH F 3 .   ? 24.913 4.376   10.687  1.00 37.92 ? 833 HOH A O   1 
HETATM 2893 O O   . HOH F 3 .   ? 1.269  20.703  -21.897 1.00 32.97 ? 834 HOH A O   1 
HETATM 2894 O O   . HOH F 3 .   ? 3.771  11.637  -21.977 1.00 31.92 ? 835 HOH A O   1 
HETATM 2895 O O   . HOH F 3 .   ? 12.626 24.742  -22.470 1.00 40.86 ? 836 HOH A O   1 
HETATM 2896 O O   . HOH F 3 .   ? 16.595 -4.924  -1.942  1.00 35.09 ? 837 HOH A O   1 
HETATM 2897 O O   . HOH F 3 .   ? 11.940 -2.105  -13.997 1.00 81.21 ? 838 HOH A O   1 
HETATM 2898 O O   . HOH F 3 .   ? 22.261 -14.167 8.754   1.00 42.15 ? 839 HOH A O   1 
HETATM 2899 O O   . HOH F 3 .   ? 25.901 3.885   16.892  1.00 35.17 ? 840 HOH A O   1 
HETATM 2900 O O   . HOH F 3 .   ? 6.955  0.869   24.448  1.00 37.90 ? 841 HOH A O   1 
HETATM 2901 O O   . HOH F 3 .   ? 19.400 7.494   -3.277  1.00 24.50 ? 842 HOH A O   1 
HETATM 2902 O O   . HOH F 3 .   ? 22.943 -1.301  22.523  1.00 28.74 ? 843 HOH A O   1 
HETATM 2903 O O   . HOH F 3 .   ? -4.289 9.192   -7.451  1.00 33.71 ? 844 HOH A O   1 
HETATM 2904 O O   . HOH F 3 .   ? 24.338 2.535   6.965   1.00 50.58 ? 845 HOH A O   1 
HETATM 2905 O O   . HOH F 3 .   ? 12.482 24.156  3.931   1.00 27.61 ? 846 HOH A O   1 
HETATM 2906 O O   . HOH F 3 .   ? 13.627 -27.685 25.198  1.00 17.11 ? 847 HOH A O   1 
HETATM 2907 O O   . HOH F 3 .   ? 21.105 -20.304 14.193  1.00 35.35 ? 848 HOH A O   1 
HETATM 2908 O O   . HOH F 3 .   ? 22.677 -16.948 26.065  1.00 22.28 ? 849 HOH A O   1 
HETATM 2909 O O   . HOH F 3 .   ? 8.193  2.892   -22.627 1.00 55.19 ? 850 HOH A O   1 
HETATM 2910 O O   . HOH F 3 .   ? 17.203 -26.064 27.384  1.00 25.61 ? 851 HOH A O   1 
HETATM 2911 O O   . HOH F 3 .   ? 6.147  21.871  -1.733  1.00 31.41 ? 852 HOH A O   1 
HETATM 2912 O O   . HOH F 3 .   ? 20.037 -8.416  33.885  1.00 27.89 ? 853 HOH A O   1 
HETATM 2913 O O   . HOH F 3 .   ? 15.046 17.762  14.001  1.00 56.06 ? 854 HOH A O   1 
HETATM 2914 O O   . HOH F 3 .   ? 25.051 -3.698  20.136  1.00 53.04 ? 855 HOH A O   1 
HETATM 2915 O O   . HOH F 3 .   ? 10.109 25.184  -23.031 1.00 38.82 ? 856 HOH A O   1 
HETATM 2916 O O   . HOH F 3 .   ? 27.648 -2.076  15.145  1.00 34.17 ? 857 HOH A O   1 
HETATM 2917 O O   . HOH F 3 .   ? 19.976 14.798  -21.747 1.00 35.44 ? 858 HOH A O   1 
HETATM 2918 O O   . HOH F 3 .   ? 11.374 -33.896 23.985  1.00 24.95 ? 859 HOH A O   1 
HETATM 2919 O O   . HOH F 3 .   ? 25.999 20.692  -1.475  1.00 31.16 ? 860 HOH A O   1 
HETATM 2920 O O   . HOH F 3 .   ? 8.111  -2.686  22.688  1.00 44.34 ? 861 HOH A O   1 
HETATM 2921 O O   . HOH F 3 .   ? 10.912 0.306   23.988  1.00 62.89 ? 862 HOH A O   1 
HETATM 2922 O O   . HOH F 3 .   ? 0.810  22.459  -19.140 1.00 42.26 ? 863 HOH A O   1 
HETATM 2923 O O   . HOH F 3 .   ? 9.569  31.573  -18.134 1.00 44.74 ? 864 HOH A O   1 
HETATM 2924 O O   . HOH F 3 .   ? 4.943  1.282   26.322  1.00 29.80 ? 865 HOH A O   1 
HETATM 2925 O O   . HOH F 3 .   ? 8.400  -28.634 3.942   1.00 32.60 ? 866 HOH A O   1 
HETATM 2926 O O   . HOH F 3 .   ? 13.703 12.434  22.929  1.00 44.31 ? 867 HOH A O   1 
HETATM 2927 O O   . HOH F 3 .   ? 10.378 -27.381 2.773   1.00 30.68 ? 868 HOH A O   1 
HETATM 2928 O O   . HOH F 3 .   ? 28.747 25.438  -4.710  1.00 33.95 ? 869 HOH A O   1 
HETATM 2929 O O   . HOH F 3 .   ? 16.308 -29.927 22.132  1.00 41.46 ? 870 HOH A O   1 
HETATM 2930 O O   . HOH F 3 .   ? 20.530 -15.652 4.907   1.00 37.96 ? 871 HOH A O   1 
HETATM 2931 O O   . HOH F 3 .   ? 1.363  -29.462 16.883  1.00 43.05 ? 872 HOH A O   1 
HETATM 2932 O O   . HOH F 3 .   ? 28.290 -3.921  16.901  1.00 33.06 ? 873 HOH A O   1 
HETATM 2933 O O   . HOH F 3 .   ? 21.119 -26.362 24.834  1.00 28.95 ? 874 HOH A O   1 
HETATM 2934 O O   . HOH F 3 .   ? 27.101 14.413  -1.879  1.00 33.91 ? 875 HOH A O   1 
HETATM 2935 O O   . HOH F 3 .   ? 25.873 21.448  -16.628 1.00 22.36 ? 876 HOH A O   1 
HETATM 2936 O O   . HOH F 3 .   ? 25.161 31.405  -7.246  1.00 39.01 ? 877 HOH A O   1 
HETATM 2937 O O   . HOH F 3 .   ? 25.157 -0.742  15.399  1.00 32.15 ? 878 HOH A O   1 
HETATM 2938 O O   . HOH F 3 .   ? 18.090 -7.289  35.812  1.00 56.43 ? 879 HOH A O   1 
HETATM 2939 O O   . HOH F 3 .   ? 16.073 13.714  23.421  1.00 31.52 ? 880 HOH A O   1 
HETATM 2940 O O   . HOH F 3 .   ? 21.892 0.520   24.913  1.00 47.37 ? 881 HOH A O   1 
HETATM 2941 O O   . HOH F 3 .   ? 10.432 22.183  0.548   1.00 21.18 ? 882 HOH A O   1 
HETATM 2942 O O   . HOH F 3 .   ? 16.365 -11.946 34.322  1.00 44.91 ? 883 HOH A O   1 
HETATM 2943 O O   . HOH F 3 .   ? 14.946 -32.152 15.788  1.00 37.75 ? 884 HOH A O   1 
HETATM 2944 O O   . HOH F 3 .   ? 21.901 12.848  -18.345 1.00 27.03 ? 885 HOH A O   1 
HETATM 2945 O O   . HOH F 3 .   ? 23.819 16.236  -16.712 1.00 22.25 ? 886 HOH A O   1 
HETATM 2946 O O   . HOH F 3 .   ? 24.099 18.963  2.615   1.00 30.17 ? 887 HOH A O   1 
HETATM 2947 O O   . HOH F 3 .   ? 13.977 -31.276 21.409  1.00 26.57 ? 888 HOH A O   1 
HETATM 2948 O O   . HOH F 3 .   ? 24.747 17.900  -18.867 1.00 37.61 ? 889 HOH A O   1 
HETATM 2949 O O   . HOH F 3 .   ? 26.570 31.349  -4.896  1.00 34.25 ? 890 HOH A O   1 
HETATM 2950 O O   . HOH F 3 .   ? 25.523 16.140  -20.792 1.00 39.96 ? 891 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A SER A 1   ? 0.3790 0.3658 0.2638 -0.1331 -0.1030 0.0674  1   SER A N   
2    N N   B SER A 1   ? 0.3647 0.3506 0.2482 -0.1342 -0.1039 0.0678  1   SER A N   
3    C CA  A SER A 1   ? 0.3697 0.3711 0.2741 -0.1239 -0.0975 0.0694  1   SER A CA  
4    C CA  B SER A 1   ? 0.3548 0.3538 0.2566 -0.1238 -0.0970 0.0677  1   SER A CA  
5    C C   A SER A 1   ? 0.3512 0.3620 0.2738 -0.1150 -0.0937 0.0712  1   SER A C   
6    C C   B SER A 1   ? 0.3399 0.3488 0.2604 -0.1153 -0.0938 0.0702  1   SER A C   
7    O O   A SER A 1   ? 0.3500 0.3592 0.2735 -0.1169 -0.0968 0.0737  1   SER A O   
8    O O   B SER A 1   ? 0.3368 0.3447 0.2586 -0.1178 -0.0975 0.0736  1   SER A O   
9    C CB  A SER A 1   ? 0.3908 0.4027 0.3042 -0.1293 -0.1027 0.0802  1   SER A CB  
10   C CB  B SER A 1   ? 0.3697 0.3791 0.2803 -0.1274 -0.1004 0.0766  1   SER A CB  
11   O OG  A SER A 1   ? 0.4343 0.4421 0.3375 -0.1310 -0.1009 0.0760  1   SER A OG  
12   O OG  B SER A 1   ? 0.3934 0.4150 0.3207 -0.1305 -0.1062 0.0898  1   SER A OG  
13   N N   A GLY A 2   ? 0.3321 0.3515 0.2678 -0.1055 -0.0870 0.0696  2   GLY A N   
14   N N   B GLY A 2   ? 0.3248 0.3424 0.2586 -0.1055 -0.0869 0.0684  2   GLY A N   
15   C CA  A GLY A 2   ? 0.3196 0.3459 0.2699 -0.0962 -0.0822 0.0700  2   GLY A CA  
16   C CA  B GLY A 2   ? 0.3159 0.3411 0.2651 -0.0967 -0.0827 0.0698  2   GLY A CA  
17   C C   A GLY A 2   ? 0.3152 0.3338 0.2586 -0.0888 -0.0752 0.0577  2   GLY A C   
18   C C   B GLY A 2   ? 0.3152 0.3333 0.2584 -0.0889 -0.0756 0.0578  2   GLY A C   
19   O O   A GLY A 2   ? 0.3266 0.3335 0.2538 -0.0916 -0.0748 0.0500  2   GLY A O   
20   O O   B GLY A 2   ? 0.3260 0.3323 0.2536 -0.0917 -0.0755 0.0505  2   GLY A O   
21   N N   . PHE A 3   ? 0.2972 0.3216 0.2523 -0.0793 -0.0695 0.0563  3   PHE A N   
22   C CA  . PHE A 3   ? 0.2893 0.3080 0.2403 -0.0721 -0.0633 0.0461  3   PHE A CA  
23   C C   . PHE A 3   ? 0.2801 0.3044 0.2431 -0.0646 -0.0601 0.0477  3   PHE A C   
24   O O   . PHE A 3   ? 0.2968 0.3290 0.2718 -0.0601 -0.0580 0.0527  3   PHE A O   
25   C CB  . PHE A 3   ? 0.2768 0.2952 0.2263 -0.0688 -0.0591 0.0409  3   PHE A CB  
26   C CG  . PHE A 3   ? 0.2827 0.2930 0.2240 -0.0645 -0.0542 0.0307  3   PHE A CG  
27   C CD1 . PHE A 3   ? 0.2957 0.2956 0.2219 -0.0689 -0.0544 0.0255  3   PHE A CD1 
28   C CD2 . PHE A 3   ? 0.2846 0.2969 0.2329 -0.0562 -0.0493 0.0269  3   PHE A CD2 
29   C CE1 . PHE A 3   ? 0.3093 0.3023 0.2298 -0.0646 -0.0492 0.0174  3   PHE A CE1 
30   C CE2 . PHE A 3   ? 0.2909 0.2968 0.2333 -0.0528 -0.0452 0.0189  3   PHE A CE2 
31   C CZ  . PHE A 3   ? 0.2995 0.2964 0.2291 -0.0566 -0.0449 0.0146  3   PHE A CZ  
32   N N   . ARG A 4   ? 0.2533 0.2727 0.2124 -0.0633 -0.0595 0.0440  4   ARG A N   
33   C CA  . ARG A 4   ? 0.2321 0.2556 0.2008 -0.0566 -0.0566 0.0454  4   ARG A CA  
34   C C   . ARG A 4   ? 0.2271 0.2449 0.1914 -0.0506 -0.0517 0.0360  4   ARG A C   
35   O O   . ARG A 4   ? 0.2404 0.2504 0.1940 -0.0527 -0.0512 0.0292  4   ARG A O   
36   C CB  . ARG A 4   ? 0.2469 0.2710 0.2168 -0.0613 -0.0615 0.0515  4   ARG A CB  
37   C CG  . ARG A 4   ? 0.2796 0.3131 0.2608 -0.0646 -0.0656 0.0640  4   ARG A CG  
38   C CD  . ARG A 4   ? 0.3081 0.3495 0.3037 -0.0561 -0.0610 0.0691  4   ARG A CD  
39   N NE  . ARG A 4   ? 0.3468 0.3979 0.3555 -0.0584 -0.0639 0.0826  4   ARG A NE  
40   C CZ  . ARG A 4   ? 0.3666 0.4250 0.3888 -0.0513 -0.0594 0.0896  4   ARG A CZ  
41   N NH1 . ARG A 4   ? 0.3673 0.4234 0.3900 -0.0420 -0.0523 0.0836  4   ARG A NH1 
42   N NH2 . ARG A 4   ? 0.3326 0.4003 0.3678 -0.0535 -0.0618 0.1030  4   ARG A NH2 
43   N N   A LYS A 5   ? 0.2120 0.2334 0.1844 -0.0433 -0.0480 0.0363  5   LYS A N   
44   N N   B LYS A 5   ? 0.2144 0.2357 0.1867 -0.0432 -0.0480 0.0362  5   LYS A N   
45   C CA  A LYS A 5   ? 0.2153 0.2320 0.1845 -0.0381 -0.0442 0.0287  5   LYS A CA  
46   C CA  B LYS A 5   ? 0.2199 0.2365 0.1890 -0.0379 -0.0441 0.0285  5   LYS A CA  
47   C C   A LYS A 5   ? 0.2227 0.2362 0.1884 -0.0413 -0.0467 0.0289  5   LYS A C   
48   C C   B LYS A 5   ? 0.2302 0.2435 0.1960 -0.0403 -0.0460 0.0280  5   LYS A C   
49   O O   A LYS A 5   ? 0.2236 0.2416 0.1956 -0.0420 -0.0489 0.0356  5   LYS A O   
50   O O   B LYS A 5   ? 0.2387 0.2557 0.2110 -0.0380 -0.0461 0.0322  5   LYS A O   
51   C CB  A LYS A 5   ? 0.2280 0.2480 0.2048 -0.0301 -0.0401 0.0295  5   LYS A CB  
52   C CB  B LYS A 5   ? 0.2315 0.2515 0.2083 -0.0300 -0.0399 0.0293  5   LYS A CB  
53   C CG  A LYS A 5   ? 0.2735 0.2887 0.2467 -0.0254 -0.0368 0.0217  5   LYS A CG  
54   C CG  B LYS A 5   ? 0.2752 0.2905 0.2486 -0.0252 -0.0367 0.0218  5   LYS A CG  
55   C CD  A LYS A 5   ? 0.3187 0.3300 0.2866 -0.0257 -0.0355 0.0155  5   LYS A CD  
56   C CD  B LYS A 5   ? 0.3199 0.3310 0.2877 -0.0255 -0.0354 0.0153  5   LYS A CD  
57   C CE  A LYS A 5   ? 0.3569 0.3701 0.3282 -0.0227 -0.0339 0.0162  5   LYS A CE  
58   C CE  B LYS A 5   ? 0.3559 0.3690 0.3270 -0.0227 -0.0339 0.0160  5   LYS A CE  
59   N NZ  A LYS A 5   ? 0.3728 0.3864 0.3481 -0.0165 -0.0312 0.0172  5   LYS A NZ  
60   N NZ  B LYS A 5   ? 0.3701 0.3837 0.3454 -0.0165 -0.0312 0.0172  5   LYS A NZ  
61   N N   . MET A 6   ? 0.2284 0.2341 0.1838 -0.0444 -0.0468 0.0227  6   MET A N   
62   C CA  . MET A 6   ? 0.2335 0.2339 0.1832 -0.0482 -0.0492 0.0221  6   MET A CA  
63   C C   . MET A 6   ? 0.2208 0.2164 0.1681 -0.0440 -0.0454 0.0155  6   MET A C   
64   O O   . MET A 6   ? 0.2287 0.2206 0.1722 -0.0415 -0.0417 0.0095  6   MET A O   
65   C CB  . MET A 6   ? 0.2693 0.2619 0.2066 -0.0561 -0.0522 0.0206  6   MET A CB  
66   C CG  . MET A 6   ? 0.3399 0.3251 0.2691 -0.0619 -0.0558 0.0208  6   MET A CG  
67   S SD  . MET A 6   ? 0.4425 0.4174 0.3551 -0.0716 -0.0596 0.0200  6   MET A SD  
68   C CE  . MET A 6   ? 0.3824 0.3682 0.3041 -0.0757 -0.0652 0.0303  6   MET A CE  
69   N N   . ALA A 7   ? 0.2066 0.2027 0.1567 -0.0436 -0.0466 0.0174  7   ALA A N   
70   C CA  . ALA A 7   ? 0.2137 0.2054 0.1620 -0.0401 -0.0434 0.0119  7   ALA A CA  
71   C C   . ALA A 7   ? 0.2240 0.2060 0.1616 -0.0459 -0.0451 0.0093  7   ALA A C   
72   O O   . ALA A 7   ? 0.2328 0.2119 0.1649 -0.0528 -0.0498 0.0128  7   ALA A O   
73   C CB  . ALA A 7   ? 0.2122 0.2101 0.1700 -0.0356 -0.0430 0.0154  7   ALA A CB  
74   N N   . PHE A 8   ? 0.2275 0.2033 0.1611 -0.0435 -0.0413 0.0035  8   PHE A N   
75   C CA  . PHE A 8   ? 0.2512 0.2159 0.1740 -0.0482 -0.0419 0.0008  8   PHE A CA  
76   C C   . PHE A 8   ? 0.2471 0.2136 0.1735 -0.0506 -0.0463 0.0055  8   PHE A C   
77   O O   . PHE A 8   ? 0.2320 0.2076 0.1699 -0.0462 -0.0464 0.0090  8   PHE A O   
78   C CB  . PHE A 8   ? 0.2598 0.2187 0.1802 -0.0438 -0.0357 -0.0056 8   PHE A CB  
79   C CG  . PHE A 8   ? 0.2847 0.2396 0.1998 -0.0426 -0.0313 -0.0096 8   PHE A CG  
80   C CD1 . PHE A 8   ? 0.3166 0.2600 0.2176 -0.0474 -0.0304 -0.0122 8   PHE A CD1 
81   C CD2 . PHE A 8   ? 0.2990 0.2610 0.2225 -0.0369 -0.0282 -0.0105 8   PHE A CD2 
82   C CE1 . PHE A 8   ? 0.3331 0.2732 0.2298 -0.0458 -0.0259 -0.0152 8   PHE A CE1 
83   C CE2 . PHE A 8   ? 0.3182 0.2773 0.2381 -0.0358 -0.0244 -0.0134 8   PHE A CE2 
84   C CZ  . PHE A 8   ? 0.3277 0.2764 0.2349 -0.0400 -0.0230 -0.0155 8   PHE A CZ  
85   N N   . PRO A 9   ? 0.2598 0.2165 0.1755 -0.0577 -0.0500 0.0058  9   PRO A N   
86   C CA  . PRO A 9   ? 0.2606 0.2180 0.1797 -0.0604 -0.0544 0.0103  9   PRO A CA  
87   C C   . PRO A 9   ? 0.2575 0.2167 0.1833 -0.0537 -0.0498 0.0072  9   PRO A C   
88   O O   . PRO A 9   ? 0.2854 0.2383 0.2066 -0.0505 -0.0442 0.0008  9   PRO A O   
89   C CB  . PRO A 9   ? 0.2926 0.2349 0.1951 -0.0690 -0.0579 0.0086  9   PRO A CB  
90   C CG  . PRO A 9   ? 0.3068 0.2437 0.1989 -0.0719 -0.0570 0.0060  9   PRO A CG  
91   C CD  . PRO A 9   ? 0.2731 0.2162 0.1721 -0.0635 -0.0498 0.0018  9   PRO A CD  
92   N N   . SER A 10  ? 0.2329 0.2016 0.1705 -0.0510 -0.0516 0.0125  10  SER A N   
93   C CA  . SER A 10  ? 0.2194 0.1919 0.1648 -0.0441 -0.0474 0.0103  10  SER A CA  
94   C C   . SER A 10  ? 0.2215 0.1881 0.1649 -0.0458 -0.0482 0.0097  10  SER A C   
95   O O   . SER A 10  ? 0.2135 0.1831 0.1632 -0.0404 -0.0448 0.0080  10  SER A O   
96   C CB  . SER A 10  ? 0.2200 0.2056 0.1788 -0.0388 -0.0475 0.0160  10  SER A CB  
97   O OG  . SER A 10  ? 0.2428 0.2330 0.2066 -0.0426 -0.0530 0.0242  10  SER A OG  
98   N N   . GLY A 11  ? 0.2295 0.1874 0.1641 -0.0534 -0.0530 0.0111  11  GLY A N   
99   C CA  . GLY A 11  ? 0.2298 0.1812 0.1622 -0.0558 -0.0546 0.0111  11  GLY A CA  
100  C C   . GLY A 11  ? 0.2268 0.1718 0.1570 -0.0512 -0.0480 0.0044  11  GLY A C   
101  O O   . GLY A 11  ? 0.2323 0.1805 0.1699 -0.0483 -0.0473 0.0055  11  GLY A O   
102  N N   . LYS A 12  ? 0.2248 0.1612 0.1455 -0.0504 -0.0428 -0.0020 12  LYS A N   
103  C CA  . LYS A 12  ? 0.2278 0.1579 0.1471 -0.0461 -0.0359 -0.0075 12  LYS A CA  
104  C C   . LYS A 12  ? 0.2202 0.1631 0.1547 -0.0382 -0.0326 -0.0068 12  LYS A C   
105  O O   . LYS A 12  ? 0.2276 0.1691 0.1658 -0.0351 -0.0292 -0.0082 12  LYS A O   
106  C CB  . LYS A 12  ? 0.2543 0.1739 0.1622 -0.0460 -0.0303 -0.0132 12  LYS A CB  
107  C CG  . LYS A 12  ? 0.3209 0.2229 0.2099 -0.0536 -0.0318 -0.0155 12  LYS A CG  
108  C CD  . LYS A 12  ? 0.3976 0.2910 0.2756 -0.0533 -0.0264 -0.0200 12  LYS A CD  
109  C CE  . LYS A 12  ? 0.4817 0.3558 0.3382 -0.0610 -0.0278 -0.0224 12  LYS A CE  
110  N NZ  . LYS A 12  ? 0.5337 0.3937 0.3822 -0.0623 -0.0255 -0.0248 12  LYS A NZ  
111  N N   . VAL A 13  ? 0.2016 0.1563 0.1443 -0.0351 -0.0337 -0.0041 13  VAL A N   
112  C CA  . VAL A 13  ? 0.1813 0.1466 0.1360 -0.0282 -0.0311 -0.0033 13  VAL A CA  
113  C C   . VAL A 13  ? 0.1687 0.1420 0.1324 -0.0272 -0.0345 0.0020  13  VAL A C   
114  O O   . VAL A 13  ? 0.1657 0.1433 0.1367 -0.0227 -0.0324 0.0021  13  VAL A O   
115  C CB  . VAL A 13  ? 0.1893 0.1613 0.1468 -0.0253 -0.0301 -0.0035 13  VAL A CB  
116  C CG1 . VAL A 13  ? 0.1965 0.1771 0.1637 -0.0189 -0.0280 -0.0028 13  VAL A CG1 
117  C CG2 . VAL A 13  ? 0.2103 0.1748 0.1597 -0.0262 -0.0265 -0.0082 13  VAL A CG2 
118  N N   . GLU A 14  ? 0.1675 0.1426 0.1312 -0.0315 -0.0400 0.0072  14  GLU A N   
119  C CA  . GLU A 14  ? 0.1621 0.1448 0.1350 -0.0306 -0.0432 0.0135  14  GLU A CA  
120  C C   . GLU A 14  ? 0.1768 0.1554 0.1508 -0.0305 -0.0424 0.0123  14  GLU A C   
121  O O   . GLU A 14  ? 0.1752 0.1613 0.1585 -0.0261 -0.0416 0.0149  14  GLU A O   
122  C CB  . GLU A 14  ? 0.1742 0.1577 0.1464 -0.0368 -0.0496 0.0200  14  GLU A CB  
123  C CG  . GLU A 14  ? 0.2071 0.1980 0.1825 -0.0359 -0.0505 0.0238  14  GLU A CG  
124  C CD  . GLU A 14  ? 0.2494 0.2399 0.2232 -0.0433 -0.0572 0.0303  14  GLU A CD  
125  O OE1 . GLU A 14  ? 0.2807 0.2738 0.2599 -0.0459 -0.0616 0.0368  14  GLU A OE1 
126  O OE2 . GLU A 14  ? 0.2641 0.2514 0.2313 -0.0469 -0.0584 0.0294  14  GLU A OE2 
127  N N   . GLY A 15  ? 0.1868 0.1528 0.1505 -0.0348 -0.0418 0.0079  15  GLY A N   
128  C CA  . GLY A 15  ? 0.1869 0.1467 0.1502 -0.0351 -0.0405 0.0063  15  GLY A CA  
129  C C   . GLY A 15  ? 0.1802 0.1431 0.1499 -0.0284 -0.0343 0.0031  15  GLY A C   
130  O O   . GLY A 15  ? 0.1941 0.1536 0.1659 -0.0278 -0.0328 0.0025  15  GLY A O   
131  N N   . CYS A 16  ? 0.1662 0.1350 0.1391 -0.0239 -0.0310 0.0014  16  CYS A N   
132  C CA  . CYS A 16  ? 0.1612 0.1338 0.1407 -0.0181 -0.0261 -0.0007 16  CYS A CA  
133  C C   . CYS A 16  ? 0.1592 0.1443 0.1489 -0.0133 -0.0270 0.0029  16  CYS A C   
134  O O   . CYS A 16  ? 0.1672 0.1557 0.1622 -0.0092 -0.0239 0.0020  16  CYS A O   
135  C CB  . CYS A 16  ? 0.1764 0.1450 0.1513 -0.0169 -0.0216 -0.0051 16  CYS A CB  
136  S SG  . CYS A 16  ? 0.2316 0.1834 0.1921 -0.0216 -0.0188 -0.0097 16  CYS A SG  
137  N N   . MET A 17  ? 0.1526 0.1440 0.1446 -0.0137 -0.0308 0.0074  17  MET A N   
138  C CA  . MET A 17  ? 0.1522 0.1534 0.1515 -0.0085 -0.0305 0.0105  17  MET A CA  
139  C C   . MET A 17  ? 0.1518 0.1579 0.1587 -0.0065 -0.0311 0.0143  17  MET A C   
140  O O   . MET A 17  ? 0.1596 0.1653 0.1680 -0.0094 -0.0341 0.0178  17  MET A O   
141  C CB  . MET A 17  ? 0.1531 0.1588 0.1521 -0.0085 -0.0326 0.0140  17  MET A CB  
142  C CG  . MET A 17  ? 0.1697 0.1714 0.1618 -0.0104 -0.0321 0.0106  17  MET A CG  
143  S SD  . MET A 17  ? 0.1856 0.1854 0.1757 -0.0071 -0.0278 0.0048  17  MET A SD  
144  C CE  . MET A 17  ? 0.2009 0.2086 0.1971 -0.0010 -0.0269 0.0074  17  MET A CE  
145  N N   . VAL A 18  ? 0.1429 0.1536 0.1543 -0.0018 -0.0287 0.0140  18  VAL A N   
146  C CA  . VAL A 18  ? 0.1498 0.1659 0.1684 0.0009  -0.0289 0.0176  18  VAL A CA  
147  C C   . VAL A 18  ? 0.1456 0.1680 0.1660 0.0060  -0.0278 0.0197  18  VAL A C   
148  O O   . VAL A 18  ? 0.1443 0.1657 0.1602 0.0072  -0.0267 0.0174  18  VAL A O   
149  C CB  . VAL A 18  ? 0.1652 0.1787 0.1868 0.0011  -0.0267 0.0150  18  VAL A CB  
150  C CG1 . VAL A 18  ? 0.1808 0.1855 0.1986 -0.0036 -0.0270 0.0128  18  VAL A CG1 
151  C CG2 . VAL A 18  ? 0.1651 0.1782 0.1858 0.0034  -0.0238 0.0115  18  VAL A CG2 
152  N N   . GLN A 19  ? 0.1422 0.1701 0.1683 0.0088  -0.0280 0.0241  19  GLN A N   
153  C CA  . GLN A 19  ? 0.1465 0.1786 0.1726 0.0138  -0.0264 0.0262  19  GLN A CA  
154  C C   . GLN A 19  ? 0.1436 0.1763 0.1715 0.0154  -0.0252 0.0242  19  GLN A C   
155  O O   . GLN A 19  ? 0.1405 0.1740 0.1740 0.0142  -0.0255 0.0247  19  GLN A O   
156  C CB  . GLN A 19  ? 0.1656 0.2034 0.1970 0.0161  -0.0268 0.0332  19  GLN A CB  
157  C CG  . GLN A 19  ? 0.2122 0.2528 0.2420 0.0218  -0.0243 0.0357  19  GLN A CG  
158  C CD  . GLN A 19  ? 0.2795 0.3260 0.3160 0.0245  -0.0240 0.0433  19  GLN A CD  
159  O OE1 . GLN A 19  ? 0.2999 0.3499 0.3420 0.0254  -0.0242 0.0455  19  GLN A OE1 
160  N NE2 . GLN A 19  ? 0.2951 0.3434 0.3321 0.0261  -0.0232 0.0481  19  GLN A NE2 
161  N N   . VAL A 20  ? 0.1391 0.1710 0.1624 0.0177  -0.0242 0.0225  20  VAL A N   
162  C CA  . VAL A 20  ? 0.1480 0.1811 0.1733 0.0187  -0.0239 0.0219  20  VAL A CA  
163  C C   . VAL A 20  ? 0.1564 0.1910 0.1775 0.0226  -0.0234 0.0245  20  VAL A C   
164  O O   . VAL A 20  ? 0.1651 0.1964 0.1783 0.0241  -0.0228 0.0238  20  VAL A O   
165  C CB  . VAL A 20  ? 0.1530 0.1826 0.1763 0.0167  -0.0238 0.0177  20  VAL A CB  
166  C CG1 . VAL A 20  ? 0.1603 0.1924 0.1876 0.0173  -0.0241 0.0188  20  VAL A CG1 
167  C CG2 . VAL A 20  ? 0.1588 0.1853 0.1843 0.0134  -0.0231 0.0150  20  VAL A CG2 
168  N N   . THR A 21  ? 0.1601 0.1987 0.1858 0.0244  -0.0234 0.0277  21  THR A N   
169  C CA  . THR A 21  ? 0.1782 0.2169 0.1984 0.0281  -0.0225 0.0302  21  THR A CA  
170  C C   . THR A 21  ? 0.1897 0.2293 0.2108 0.0274  -0.0239 0.0300  21  THR A C   
171  O O   . THR A 21  ? 0.1860 0.2296 0.2163 0.0258  -0.0245 0.0309  21  THR A O   
172  C CB  . THR A 21  ? 0.2060 0.2495 0.2307 0.0314  -0.0211 0.0358  21  THR A CB  
173  O OG1 . THR A 21  ? 0.2226 0.2663 0.2481 0.0316  -0.0204 0.0375  21  THR A OG1 
174  C CG2 . THR A 21  ? 0.2269 0.2694 0.2447 0.0358  -0.0192 0.0387  21  THR A CG2 
175  N N   . CYS A 22  ? 0.2077 0.2429 0.2189 0.0281  -0.0245 0.0292  22  CYS A N   
176  C CA  . CYS A 22  ? 0.2335 0.2695 0.2447 0.0270  -0.0266 0.0302  22  CYS A CA  
177  C C   . CYS A 22  ? 0.2710 0.3026 0.2700 0.0302  -0.0258 0.0320  22  CYS A C   
178  O O   . CYS A 22  ? 0.2785 0.3027 0.2655 0.0312  -0.0250 0.0301  22  CYS A O   
179  C CB  . CYS A 22  ? 0.2364 0.2697 0.2468 0.0230  -0.0292 0.0274  22  CYS A CB  
180  S SG  . CYS A 22  ? 0.3129 0.3491 0.3273 0.0205  -0.0326 0.0304  22  CYS A SG  
181  N N   . GLY A 23  ? 0.2938 0.3296 0.2959 0.0323  -0.0252 0.0360  23  GLY A N   
182  C CA  . GLY A 23  ? 0.3204 0.3516 0.3105 0.0360  -0.0235 0.0383  23  GLY A CA  
183  C C   . GLY A 23  ? 0.3405 0.3689 0.3258 0.0405  -0.0191 0.0393  23  GLY A C   
184  O O   . GLY A 23  ? 0.3496 0.3845 0.3455 0.0421  -0.0173 0.0419  23  GLY A O   
185  N N   . THR A 24  ? 0.3500 0.3684 0.3199 0.0420  -0.0176 0.0372  24  THR A N   
186  C CA  . THR A 24  ? 0.3600 0.3750 0.3251 0.0468  -0.0126 0.0387  24  THR A CA  
187  C C   . THR A 24  ? 0.3425 0.3554 0.3082 0.0448  -0.0129 0.0352  24  THR A C   
188  O O   . THR A 24  ? 0.3580 0.3683 0.3207 0.0484  -0.0090 0.0367  24  THR A O   
189  C CB  . THR A 24  ? 0.4144 0.4183 0.3611 0.0508  -0.0092 0.0394  24  THR A CB  
190  O OG1 . THR A 24  ? 0.4539 0.4472 0.3867 0.0473  -0.0122 0.0343  24  THR A OG1 
191  C CG2 . THR A 24  ? 0.4277 0.4329 0.3722 0.0528  -0.0086 0.0431  24  THR A CG2 
192  N N   . THR A 25  ? 0.3104 0.3248 0.2808 0.0395  -0.0172 0.0312  25  THR A N   
193  C CA  . THR A 25  ? 0.2916 0.3033 0.2612 0.0375  -0.0177 0.0277  25  THR A CA  
194  C C   . THR A 25  ? 0.2647 0.2846 0.2487 0.0354  -0.0183 0.0281  25  THR A C   
195  O O   . THR A 25  ? 0.2662 0.2913 0.2590 0.0329  -0.0204 0.0281  25  THR A O   
196  C CB  . THR A 25  ? 0.3080 0.3144 0.2715 0.0330  -0.0217 0.0233  25  THR A CB  
197  O OG1 . THR A 25  ? 0.3325 0.3293 0.2804 0.0341  -0.0218 0.0229  25  THR A OG1 
198  C CG2 . THR A 25  ? 0.3143 0.3188 0.2782 0.0307  -0.0223 0.0198  25  THR A CG2 
199  N N   . THR A 26  ? 0.2504 0.2704 0.2356 0.0365  -0.0163 0.0289  26  THR A N   
200  C CA  . THR A 26  ? 0.2337 0.2594 0.2297 0.0337  -0.0176 0.0293  26  THR A CA  
201  C C   . THR A 26  ? 0.2166 0.2386 0.2093 0.0312  -0.0182 0.0256  26  THR A C   
202  O O   . THR A 26  ? 0.2275 0.2450 0.2130 0.0334  -0.0162 0.0257  26  THR A O   
203  C CB  . THR A 26  ? 0.2539 0.2850 0.2569 0.0365  -0.0155 0.0355  26  THR A CB  
204  O OG1 . THR A 26  ? 0.2709 0.3065 0.2788 0.0383  -0.0153 0.0390  26  THR A OG1 
205  C CG2 . THR A 26  ? 0.2595 0.2945 0.2711 0.0327  -0.0176 0.0361  26  THR A CG2 
206  N N   . LEU A 27  ? 0.1900 0.2133 0.1877 0.0268  -0.0206 0.0225  27  LEU A N   
207  C CA  . LEU A 27  ? 0.1763 0.1967 0.1717 0.0241  -0.0212 0.0193  27  LEU A CA  
208  C C   . LEU A 27  ? 0.1629 0.1858 0.1657 0.0201  -0.0227 0.0183  27  LEU A C   
209  O O   . LEU A 27  ? 0.1637 0.1902 0.1728 0.0199  -0.0230 0.0208  27  LEU A O   
210  C CB  . LEU A 27  ? 0.1762 0.1911 0.1642 0.0230  -0.0222 0.0151  27  LEU A CB  
211  C CG  . LEU A 27  ? 0.1771 0.1923 0.1666 0.0215  -0.0240 0.0137  27  LEU A CG  
212  C CD1 . LEU A 27  ? 0.1749 0.1939 0.1740 0.0186  -0.0246 0.0130  27  LEU A CD1 
213  C CD2 . LEU A 27  ? 0.1888 0.1986 0.1711 0.0199  -0.0258 0.0109  27  LEU A CD2 
214  N N   . ASN A 28  ? 0.1481 0.1682 0.1488 0.0171  -0.0233 0.0150  28  ASN A N   
215  C CA  . ASN A 28  ? 0.1428 0.1628 0.1474 0.0132  -0.0242 0.0138  28  ASN A CA  
216  C C   . ASN A 28  ? 0.1380 0.1558 0.1440 0.0112  -0.0240 0.0101  28  ASN A C   
217  O O   . ASN A 28  ? 0.1433 0.1598 0.1471 0.0117  -0.0238 0.0082  28  ASN A O   
218  C CB  . ASN A 28  ? 0.1590 0.1768 0.1601 0.0110  -0.0247 0.0131  28  ASN A CB  
219  C CG  . ASN A 28  ? 0.1851 0.2055 0.1862 0.0134  -0.0244 0.0178  28  ASN A CG  
220  O OD1 . ASN A 28  ? 0.1866 0.2104 0.1926 0.0130  -0.0252 0.0224  28  ASN A OD1 
221  N ND2 . ASN A 28  ? 0.1936 0.2120 0.1895 0.0160  -0.0230 0.0173  28  ASN A ND2 
222  N N   . GLY A 29  ? 0.1306 0.1477 0.1402 0.0088  -0.0239 0.0097  29  GLY A N   
223  C CA  . GLY A 29  ? 0.1316 0.1457 0.1430 0.0071  -0.0224 0.0068  29  GLY A CA  
224  C C   . GLY A 29  ? 0.1363 0.1448 0.1445 0.0035  -0.0219 0.0046  29  GLY A C   
225  O O   . GLY A 29  ? 0.1468 0.1545 0.1528 0.0015  -0.0237 0.0059  29  GLY A O   
226  N N   . LEU A 30  ? 0.1341 0.1384 0.1416 0.0024  -0.0195 0.0016  30  LEU A N   
227  C CA  . LEU A 30  ? 0.1373 0.1342 0.1396 -0.0008 -0.0180 -0.0011 30  LEU A CA  
228  C C   . LEU A 30  ? 0.1373 0.1300 0.1426 -0.0011 -0.0150 -0.0017 30  LEU A C   
229  O O   . LEU A 30  ? 0.1475 0.1416 0.1582 0.0010  -0.0121 -0.0015 30  LEU A O   
230  C CB  . LEU A 30  ? 0.1341 0.1286 0.1331 -0.0010 -0.0162 -0.0037 30  LEU A CB  
231  C CG  . LEU A 30  ? 0.1495 0.1355 0.1410 -0.0042 -0.0143 -0.0065 30  LEU A CG  
232  C CD1 . LEU A 30  ? 0.1640 0.1487 0.1493 -0.0073 -0.0180 -0.0060 30  LEU A CD1 
233  C CD2 . LEU A 30  ? 0.1619 0.1464 0.1524 -0.0034 -0.0116 -0.0084 30  LEU A CD2 
234  N N   . TRP A 31  ? 0.1360 0.1233 0.1380 -0.0039 -0.0156 -0.0018 31  TRP A N   
235  C CA  . TRP A 31  ? 0.1406 0.1227 0.1448 -0.0042 -0.0127 -0.0022 31  TRP A CA  
236  C C   . TRP A 31  ? 0.1535 0.1230 0.1484 -0.0069 -0.0091 -0.0060 31  TRP A C   
237  O O   . TRP A 31  ? 0.1585 0.1212 0.1440 -0.0111 -0.0114 -0.0072 31  TRP A O   
238  C CB  . TRP A 31  ? 0.1435 0.1275 0.1500 -0.0056 -0.0164 0.0007  31  TRP A CB  
239  C CG  . TRP A 31  ? 0.1463 0.1244 0.1545 -0.0063 -0.0142 0.0006  31  TRP A CG  
240  C CD1 . TRP A 31  ? 0.1544 0.1298 0.1669 -0.0040 -0.0090 -0.0003 31  TRP A CD1 
241  C CD2 . TRP A 31  ? 0.1473 0.1227 0.1548 -0.0093 -0.0176 0.0027  31  TRP A CD2 
242  N NE1 . TRP A 31  ? 0.1567 0.1268 0.1702 -0.0052 -0.0083 0.0003  31  TRP A NE1 
243  C CE2 . TRP A 31  ? 0.1583 0.1284 0.1687 -0.0086 -0.0139 0.0021  31  TRP A CE2 
244  C CE3 . TRP A 31  ? 0.1574 0.1343 0.1627 -0.0126 -0.0234 0.0056  31  TRP A CE3 
245  C CZ2 . TRP A 31  ? 0.1623 0.1274 0.1721 -0.0115 -0.0162 0.0035  31  TRP A CZ2 
246  C CZ3 . TRP A 31  ? 0.1626 0.1355 0.1682 -0.0157 -0.0261 0.0078  31  TRP A CZ3 
247  C CH2 . TRP A 31  ? 0.1640 0.1305 0.1711 -0.0153 -0.0226 0.0063  31  TRP A CH2 
248  N N   . LEU A 32  ? 0.1528 0.1193 0.1501 -0.0046 -0.0033 -0.0072 32  LEU A N   
249  C CA  . LEU A 32  ? 0.1720 0.1257 0.1602 -0.0059 0.0020  -0.0106 32  LEU A CA  
250  C C   . LEU A 32  ? 0.1779 0.1269 0.1710 -0.0036 0.0080  -0.0101 32  LEU A C   
251  O O   . LEU A 32  ? 0.1695 0.1268 0.1746 0.0001  0.0099  -0.0072 32  LEU A O   
252  C CB  . LEU A 32  ? 0.1767 0.1319 0.1644 -0.0044 0.0045  -0.0115 32  LEU A CB  
253  C CG  . LEU A 32  ? 0.1925 0.1523 0.1759 -0.0062 -0.0006 -0.0120 32  LEU A CG  
254  C CD1 . LEU A 32  ? 0.1900 0.1524 0.1752 -0.0043 0.0018  -0.0122 32  LEU A CD1 
255  C CD2 . LEU A 32  ? 0.2102 0.1605 0.1805 -0.0111 -0.0028 -0.0142 32  LEU A CD2 
256  N N   . ASP A 33  ? 0.1908 0.1261 0.1746 -0.0061 0.0105  -0.0124 33  ASP A N   
257  C CA  . ASP A 33  ? 0.2009 0.1304 0.1891 -0.0038 0.0166  -0.0117 33  ASP A CA  
258  C C   . ASP A 33  ? 0.1946 0.1369 0.1970 -0.0019 0.0130  -0.0076 33  ASP A C   
259  O O   . ASP A 33  ? 0.2016 0.1493 0.2037 -0.0042 0.0060  -0.0065 33  ASP A O   
260  C CB  . ASP A 33  ? 0.2335 0.1598 0.2250 0.0003  0.0255  -0.0115 33  ASP A CB  
261  C CG  . ASP A 33  ? 0.3105 0.2238 0.2874 -0.0013 0.0295  -0.0153 33  ASP A CG  
262  O OD1 . ASP A 33  ? 0.3480 0.2480 0.3097 -0.0056 0.0283  -0.0188 33  ASP A OD1 
263  O OD2 . ASP A 33  ? 0.3265 0.2427 0.3068 0.0015  0.0337  -0.0145 33  ASP A OD2 
264  N N   . ASP A 34  ? 0.1764 0.1244 0.1914 0.0022  0.0173  -0.0046 34  ASP A N   
265  C CA  . ASP A 34  ? 0.1641 0.1238 0.1917 0.0038  0.0139  -0.0005 34  ASP A CA  
266  C C   . ASP A 34  ? 0.1535 0.1277 0.1907 0.0061  0.0110  0.0026  34  ASP A C   
267  O O   . ASP A 34  ? 0.1547 0.1379 0.2036 0.0083  0.0105  0.0066  34  ASP A O   
268  C CB  . ASP A 34  ? 0.1742 0.1298 0.2092 0.0061  0.0201  0.0014  34  ASP A CB  
269  C CG  . ASP A 34  ? 0.2272 0.1819 0.2691 0.0099  0.0282  0.0033  34  ASP A CG  
270  O OD1 . ASP A 34  ? 0.2261 0.1809 0.2648 0.0103  0.0295  0.0023  34  ASP A OD1 
271  O OD2 . ASP A 34  ? 0.2542 0.2083 0.3054 0.0125  0.0334  0.0063  34  ASP A OD2 
272  N N   . VAL A 35  ? 0.1421 0.1184 0.1739 0.0053  0.0084  0.0010  35  VAL A N   
273  C CA  . VAL A 35  ? 0.1436 0.1316 0.1821 0.0069  0.0051  0.0037  35  VAL A CA  
274  C C   . VAL A 35  ? 0.1399 0.1313 0.1715 0.0051  -0.0011 0.0023  35  VAL A C   
275  O O   . VAL A 35  ? 0.1499 0.1347 0.1716 0.0027  -0.0017 -0.0008 35  VAL A O   
276  C CB  . VAL A 35  ? 0.1601 0.1481 0.2015 0.0084  0.0091  0.0044  35  VAL A CB  
277  C CG1 . VAL A 35  ? 0.1611 0.1599 0.2082 0.0091  0.0045  0.0072  35  VAL A CG1 
278  C CG2 . VAL A 35  ? 0.1679 0.1529 0.2177 0.0107  0.0163  0.0069  35  VAL A CG2 
279  N N   . VAL A 36  ? 0.1299 0.1308 0.1664 0.0064  -0.0053 0.0050  36  VAL A N   
280  C CA  . VAL A 36  ? 0.1327 0.1371 0.1637 0.0058  -0.0101 0.0046  36  VAL A CA  
281  C C   . VAL A 36  ? 0.1263 0.1352 0.1584 0.0070  -0.0112 0.0053  36  VAL A C   
282  O O   . VAL A 36  ? 0.1188 0.1327 0.1579 0.0084  -0.0115 0.0082  36  VAL A O   
283  C CB  . VAL A 36  ? 0.1401 0.1500 0.1736 0.0065  -0.0136 0.0073  36  VAL A CB  
284  C CG1 . VAL A 36  ? 0.1445 0.1580 0.1732 0.0070  -0.0172 0.0078  36  VAL A CG1 
285  C CG2 . VAL A 36  ? 0.1485 0.1535 0.1807 0.0045  -0.0135 0.0070  36  VAL A CG2 
286  N N   . TYR A 37  ? 0.1289 0.1355 0.1541 0.0060  -0.0122 0.0030  37  TYR A N   
287  C CA  . TYR A 37  ? 0.1248 0.1341 0.1497 0.0065  -0.0137 0.0034  37  TYR A CA  
288  C C   . TYR A 37  ? 0.1305 0.1425 0.1501 0.0071  -0.0177 0.0037  37  TYR A C   
289  O O   . TYR A 37  ? 0.1433 0.1537 0.1579 0.0064  -0.0186 0.0027  37  TYR A O   
290  C CB  . TYR A 37  ? 0.1259 0.1303 0.1462 0.0052  -0.0117 0.0008  37  TYR A CB  
291  C CG  . TYR A 37  ? 0.1381 0.1378 0.1616 0.0052  -0.0062 0.0005  37  TYR A CG  
292  C CD1 . TYR A 37  ? 0.1543 0.1469 0.1734 0.0041  -0.0034 -0.0017 37  TYR A CD1 
293  C CD2 . TYR A 37  ? 0.1499 0.1515 0.1806 0.0063  -0.0038 0.0029  37  TYR A CD2 
294  C CE1 . TYR A 37  ? 0.1709 0.1572 0.1914 0.0046  0.0027  -0.0021 37  TYR A CE1 
295  C CE2 . TYR A 37  ? 0.1620 0.1589 0.1962 0.0072  0.0026  0.0034  37  TYR A CE2 
296  C CZ  . TYR A 37  ? 0.1816 0.1701 0.2098 0.0066  0.0062  0.0005  37  TYR A CZ  
297  O OH  . TYR A 37  ? 0.2143 0.1962 0.2448 0.0079  0.0135  0.0010  37  TYR A OH  
298  N N   . CYS A 38  ? 0.1233 0.1388 0.1439 0.0081  -0.0201 0.0056  38  CYS A N   
299  C CA  . CYS A 38  ? 0.1292 0.1452 0.1430 0.0092  -0.0229 0.0058  38  CYS A CA  
300  C C   . CYS A 38  ? 0.1335 0.1493 0.1447 0.0091  -0.0254 0.0065  38  CYS A C   
301  O O   . CYS A 38  ? 0.1367 0.1541 0.1535 0.0081  -0.0258 0.0082  38  CYS A O   
302  C CB  . CYS A 38  ? 0.1355 0.1545 0.1507 0.0110  -0.0234 0.0081  38  CYS A CB  
303  S SG  . CYS A 38  ? 0.1562 0.1794 0.1768 0.0121  -0.0247 0.0115  38  CYS A SG  
304  N N   . PRO A 39  ? 0.1337 0.1469 0.1360 0.0098  -0.0274 0.0058  39  PRO A N   
305  C CA  . PRO A 39  ? 0.1342 0.1442 0.1298 0.0092  -0.0309 0.0063  39  PRO A CA  
306  C C   . PRO A 39  ? 0.1415 0.1548 0.1415 0.0092  -0.0323 0.0095  39  PRO A C   
307  O O   . PRO A 39  ? 0.1469 0.1622 0.1478 0.0111  -0.0313 0.0107  39  PRO A O   
308  C CB  . PRO A 39  ? 0.1438 0.1499 0.1296 0.0112  -0.0305 0.0050  39  PRO A CB  
309  C CG  . PRO A 39  ? 0.1467 0.1541 0.1352 0.0113  -0.0279 0.0037  39  PRO A CG  
310  C CD  . PRO A 39  ? 0.1321 0.1439 0.1290 0.0113  -0.0265 0.0050  39  PRO A CD  
311  N N   . ARG A 40  ? 0.1347 0.1480 0.1365 0.0068  -0.0353 0.0114  40  ARG A N   
312  C CA  . ARG A 40  ? 0.1363 0.1522 0.1409 0.0061  -0.0378 0.0151  40  ARG A CA  
313  C C   . ARG A 40  ? 0.1631 0.1740 0.1549 0.0073  -0.0400 0.0150  40  ARG A C   
314  O O   . ARG A 40  ? 0.1704 0.1833 0.1629 0.0078  -0.0407 0.0175  40  ARG A O   
315  C CB  . ARG A 40  ? 0.1380 0.1555 0.1486 0.0025  -0.0411 0.0184  40  ARG A CB  
316  C CG  . ARG A 40  ? 0.1592 0.1704 0.1596 0.0001  -0.0455 0.0177  40  ARG A CG  
317  C CD  . ARG A 40  ? 0.1588 0.1727 0.1669 -0.0040 -0.0497 0.0227  40  ARG A CD  
318  N NE  . ARG A 40  ? 0.1780 0.1853 0.1766 -0.0069 -0.0543 0.0221  40  ARG A NE  
319  C CZ  . ARG A 40  ? 0.1952 0.2032 0.1976 -0.0113 -0.0597 0.0268  40  ARG A CZ  
320  N NH1 . ARG A 40  ? 0.1822 0.1977 0.1982 -0.0129 -0.0605 0.0328  40  ARG A NH1 
321  N NH2 . ARG A 40  ? 0.1947 0.1956 0.1873 -0.0143 -0.0643 0.0261  40  ARG A NH2 
322  N N   . HIS A 41  ? 0.1708 0.1750 0.1508 0.0084  -0.0397 0.0121  41  HIS A N   
323  C CA  . HIS A 41  ? 0.1863 0.1838 0.1525 0.0106  -0.0399 0.0119  41  HIS A CA  
324  C C   . HIS A 41  ? 0.1951 0.1958 0.1627 0.0149  -0.0359 0.0129  41  HIS A C   
325  O O   . HIS A 41  ? 0.2054 0.2012 0.1629 0.0172  -0.0354 0.0136  41  HIS A O   
326  C CB  . HIS A 41  ? 0.1972 0.1853 0.1502 0.0106  -0.0406 0.0091  41  HIS A CB  
327  C CG  . HIS A 41  ? 0.2270 0.2150 0.1798 0.0134  -0.0364 0.0069  41  HIS A CG  
328  N ND1 . HIS A 41  ? 0.2661 0.2548 0.2175 0.0176  -0.0323 0.0076  41  HIS A ND1 
329  C CD2 . HIS A 41  ? 0.2370 0.2239 0.1905 0.0124  -0.0360 0.0046  41  HIS A CD2 
330  C CE1 . HIS A 41  ? 0.2654 0.2539 0.2173 0.0188  -0.0298 0.0062  41  HIS A CE1 
331  N NE2 . HIS A 41  ? 0.2544 0.2419 0.2074 0.0157  -0.0320 0.0041  41  HIS A NE2 
332  N N   . VAL A 42  ? 0.1822 0.1906 0.1623 0.0156  -0.0336 0.0136  42  VAL A N   
333  C CA  . VAL A 42  ? 0.1859 0.1985 0.1696 0.0188  -0.0310 0.0159  42  VAL A CA  
334  C C   . VAL A 42  ? 0.1949 0.2082 0.1770 0.0189  -0.0329 0.0189  42  VAL A C   
335  O O   . VAL A 42  ? 0.2105 0.2241 0.1898 0.0221  -0.0310 0.0207  42  VAL A O   
336  C CB  . VAL A 42  ? 0.1841 0.2034 0.1807 0.0184  -0.0292 0.0161  42  VAL A CB  
337  C CG1 . VAL A 42  ? 0.1795 0.2032 0.1863 0.0160  -0.0303 0.0173  42  VAL A CG1 
338  C CG2 . VAL A 42  ? 0.1914 0.2140 0.1907 0.0215  -0.0268 0.0185  42  VAL A CG2 
339  N N   . ILE A 43  ? 0.1867 0.2004 0.1707 0.0153  -0.0367 0.0199  43  ILE A N   
340  C CA  . ILE A 43  ? 0.2001 0.2144 0.1822 0.0145  -0.0394 0.0234  43  ILE A CA  
341  C C   . ILE A 43  ? 0.2405 0.2444 0.2041 0.0146  -0.0414 0.0228  43  ILE A C   
342  O O   . ILE A 43  ? 0.2518 0.2544 0.2107 0.0138  -0.0437 0.0255  43  ILE A O   
343  C CB  . ILE A 43  ? 0.1911 0.2105 0.1842 0.0102  -0.0429 0.0260  43  ILE A CB  
344  C CG1 . ILE A 43  ? 0.2007 0.2149 0.1882 0.0061  -0.0472 0.0255  43  ILE A CG1 
345  C CG2 . ILE A 43  ? 0.1891 0.2162 0.1985 0.0106  -0.0396 0.0261  43  ILE A CG2 
346  C CD1 . ILE A 43  ? 0.2105 0.2308 0.2108 0.0020  -0.0504 0.0297  43  ILE A CD1 
347  N N   . CYS A 44  ? 0.2667 0.2625 0.2191 0.0156  -0.0403 0.0196  44  CYS A N   
348  C CA  . CYS A 44  ? 0.3137 0.2971 0.2464 0.0156  -0.0418 0.0188  44  CYS A CA  
349  C C   . CYS A 44  ? 0.3723 0.3510 0.2957 0.0217  -0.0360 0.0186  44  CYS A C   
350  O O   . CYS A 44  ? 0.3787 0.3624 0.3097 0.0251  -0.0317 0.0185  44  CYS A O   
351  C CB  . CYS A 44  ? 0.3157 0.2911 0.2403 0.0133  -0.0436 0.0155  44  CYS A CB  
352  S SG  . CYS A 44  ? 0.3091 0.2889 0.2438 0.0063  -0.0504 0.0168  44  CYS A SG  
353  N N   . THR A 45  ? 0.4158 0.3836 0.3217 0.0226  -0.0363 0.0189  45  THR A N   
354  C CA  . THR A 45  ? 0.4565 0.4164 0.3498 0.0287  -0.0301 0.0190  45  THR A CA  
355  C C   . THR A 45  ? 0.4930 0.4402 0.3723 0.0283  -0.0296 0.0152  45  THR A C   
356  O O   . THR A 45  ? 0.4961 0.4420 0.3762 0.0231  -0.0348 0.0130  45  THR A O   
357  C CB  . THR A 45  ? 0.4873 0.4397 0.3665 0.0295  -0.0304 0.0212  45  THR A CB  
358  O OG1 . THR A 45  ? 0.5172 0.4565 0.3790 0.0245  -0.0359 0.0193  45  THR A OG1 
359  C CG2 . THR A 45  ? 0.4854 0.4501 0.3785 0.0283  -0.0326 0.0250  45  THR A CG2 
360  N N   . SER A 46  ? 0.5146 0.4523 0.3813 0.0340  -0.0232 0.0150  46  SER A N   
361  C CA  . SER A 46  ? 0.5392 0.4636 0.3915 0.0340  -0.0223 0.0116  46  SER A CA  
362  C C   . SER A 46  ? 0.5572 0.4670 0.3904 0.0286  -0.0286 0.0095  46  SER A C   
363  O O   . SER A 46  ? 0.5653 0.4683 0.3928 0.0247  -0.0323 0.0065  46  SER A O   
364  C CB  . SER A 46  ? 0.5692 0.4857 0.4118 0.0418  -0.0133 0.0128  46  SER A CB  
365  O OG  . SER A 46  ? 0.6206 0.5295 0.4576 0.0423  -0.0115 0.0101  46  SER A OG  
366  N N   . GLU A 47  ? 0.5606 0.4662 0.3845 0.0278  -0.0303 0.0114  47  GLU A N   
367  C CA  . GLU A 47  ? 0.5733 0.4653 0.3785 0.0217  -0.0373 0.0104  47  GLU A CA  
368  C C   . GLU A 47  ? 0.5575 0.4580 0.3755 0.0133  -0.0468 0.0109  47  GLU A C   
369  O O   . GLU A 47  ? 0.5721 0.4620 0.3788 0.0078  -0.0527 0.0091  47  GLU A O   
370  C CB  . GLU A 47  ? 0.6141 0.5023 0.4093 0.0228  -0.0369 0.0133  47  GLU A CB  
371  C CG  . GLU A 47  ? 0.7008 0.5744 0.4757 0.0154  -0.0451 0.0130  47  GLU A CG  
372  C CD  . GLU A 47  ? 0.7996 0.6698 0.5645 0.0150  -0.0462 0.0161  47  GLU A CD  
373  O OE1 . GLU A 47  ? 0.8102 0.6928 0.5882 0.0202  -0.0412 0.0191  47  GLU A OE1 
374  O OE2 . GLU A 47  ? 0.8443 0.6991 0.5879 0.0092  -0.0525 0.0159  47  GLU A OE2 
375  N N   . ASP A 48  ? 0.5245 0.4437 0.3662 0.0125  -0.0481 0.0136  48  ASP A N   
376  C CA  . ASP A 48  ? 0.5032 0.4319 0.3596 0.0056  -0.0555 0.0152  48  ASP A CA  
377  C C   . ASP A 48  ? 0.4859 0.4129 0.3449 0.0034  -0.0570 0.0124  48  ASP A C   
378  O O   . ASP A 48  ? 0.4853 0.4111 0.3451 -0.0031 -0.0643 0.0134  48  ASP A O   
379  C CB  . ASP A 48  ? 0.5029 0.4508 0.3845 0.0067  -0.0541 0.0181  48  ASP A CB  
380  C CG  . ASP A 48  ? 0.5549 0.5080 0.4393 0.0072  -0.0546 0.0220  48  ASP A CG  
381  O OD1 . ASP A 48  ? 0.5653 0.5100 0.4362 0.0033  -0.0596 0.0238  48  ASP A OD1 
382  O OD2 . ASP A 48  ? 0.5728 0.5380 0.4728 0.0109  -0.0503 0.0236  48  ASP A OD2 
383  N N   . MET A 49  ? 0.4729 0.4001 0.3335 0.0086  -0.0505 0.0095  49  MET A N   
384  C CA  . MET A 49  ? 0.4625 0.3892 0.3268 0.0069  -0.0514 0.0069  49  MET A CA  
385  C C   . MET A 49  ? 0.4647 0.3753 0.3103 0.0022  -0.0568 0.0051  49  MET A C   
386  O O   . MET A 49  ? 0.4547 0.3665 0.3055 -0.0011 -0.0601 0.0043  49  MET A O   
387  C CB  . MET A 49  ? 0.4649 0.3936 0.3326 0.0132  -0.0435 0.0048  49  MET A CB  
388  C CG  . MET A 49  ? 0.4693 0.4140 0.3572 0.0161  -0.0398 0.0065  49  MET A CG  
389  S SD  . MET A 49  ? 0.4666 0.4249 0.3751 0.0107  -0.0446 0.0075  49  MET A SD  
390  C CE  . MET A 49  ? 0.3963 0.3518 0.3049 0.0097  -0.0444 0.0042  49  MET A CE  
391  N N   . LEU A 50  ? 0.4750 0.3702 0.2988 0.0018  -0.0579 0.0048  50  LEU A N   
392  C CA  . LEU A 50  ? 0.4951 0.3727 0.2988 -0.0035 -0.0638 0.0031  50  LEU A CA  
393  C C   . LEU A 50  ? 0.4892 0.3714 0.3007 -0.0125 -0.0744 0.0062  50  LEU A C   
394  O O   . LEU A 50  ? 0.5008 0.3775 0.3094 -0.0168 -0.0790 0.0053  50  LEU A O   
395  C CB  . LEU A 50  ? 0.5188 0.3769 0.2950 -0.0022 -0.0625 0.0021  50  LEU A CB  
396  C CG  . LEU A 50  ? 0.5538 0.4051 0.3208 0.0072  -0.0512 -0.0002 50  LEU A CG  
397  C CD1 . LEU A 50  ? 0.5787 0.4107 0.3185 0.0088  -0.0492 -0.0005 50  LEU A CD1 
398  C CD2 . LEU A 50  ? 0.5675 0.4125 0.3316 0.0097  -0.0473 -0.0035 50  LEU A CD2 
399  N N   . ASN A 51  ? 0.4655 0.3587 0.2886 -0.0153 -0.0781 0.0107  51  ASN A N   
400  C CA  . ASN A 51  ? 0.4505 0.3502 0.2843 -0.0236 -0.0877 0.0154  51  ASN A CA  
401  C C   . ASN A 51  ? 0.4106 0.3292 0.2674 -0.0231 -0.0871 0.0201  51  ASN A C   
402  O O   . ASN A 51  ? 0.4166 0.3359 0.2718 -0.0268 -0.0920 0.0243  51  ASN A O   
403  C CB  . ASN A 51  ? 0.4934 0.3764 0.3050 -0.0310 -0.0968 0.0172  51  ASN A CB  
404  C CG  . ASN A 51  ? 0.5408 0.4292 0.3627 -0.0404 -0.1077 0.0232  51  ASN A CG  
405  O OD1 . ASN A 51  ? 0.5517 0.4536 0.3951 -0.0411 -0.1081 0.0253  51  ASN A OD1 
406  N ND2 . ASN A 51  ? 0.5631 0.4408 0.3698 -0.0478 -0.1167 0.0266  51  ASN A ND2 
407  N N   . PRO A 52  ? 0.3637 0.2970 0.2411 -0.0183 -0.0808 0.0193  52  PRO A N   
408  C CA  . PRO A 52  ? 0.3370 0.2864 0.2345 -0.0171 -0.0792 0.0233  52  PRO A CA  
409  C C   . PRO A 52  ? 0.3183 0.2781 0.2333 -0.0231 -0.0854 0.0295  52  PRO A C   
410  O O   . PRO A 52  ? 0.3308 0.2919 0.2521 -0.0260 -0.0879 0.0301  52  PRO A O   
411  C CB  . PRO A 52  ? 0.3352 0.2934 0.2451 -0.0104 -0.0704 0.0200  52  PRO A CB  
412  C CG  . PRO A 52  ? 0.3498 0.3017 0.2544 -0.0104 -0.0698 0.0161  52  PRO A CG  
413  C CD  . PRO A 52  ? 0.3524 0.2872 0.2342 -0.0139 -0.0749 0.0150  52  PRO A CD  
414  N N   . ASN A 53  ? 0.2904 0.2581 0.2144 -0.0247 -0.0874 0.0346  53  ASN A N   
415  C CA  . ASN A 53  ? 0.2714 0.2513 0.2160 -0.0292 -0.0915 0.0417  53  ASN A CA  
416  C C   . ASN A 53  ? 0.2561 0.2495 0.2199 -0.0233 -0.0835 0.0415  53  ASN A C   
417  O O   . ASN A 53  ? 0.2636 0.2611 0.2298 -0.0214 -0.0818 0.0432  53  ASN A O   
418  C CB  . ASN A 53  ? 0.2848 0.2640 0.2268 -0.0357 -0.0999 0.0486  53  ASN A CB  
419  C CG  . ASN A 53  ? 0.3101 0.3024 0.2753 -0.0401 -0.1038 0.0571  53  ASN A CG  
420  O OD1 . ASN A 53  ? 0.3120 0.3174 0.2984 -0.0364 -0.0978 0.0589  53  ASN A OD1 
421  N ND2 . ASN A 53  ? 0.3174 0.3058 0.2792 -0.0483 -0.1136 0.0631  53  ASN A ND2 
422  N N   . TYR A 54  ? 0.2424 0.2414 0.2180 -0.0206 -0.0786 0.0394  54  TYR A N   
423  C CA  . TYR A 54  ? 0.2190 0.2277 0.2090 -0.0151 -0.0706 0.0380  54  TYR A CA  
424  C C   . TYR A 54  ? 0.2126 0.2325 0.2207 -0.0161 -0.0708 0.0446  54  TYR A C   
425  O O   . TYR A 54  ? 0.2098 0.2340 0.2224 -0.0125 -0.0664 0.0439  54  TYR A O   
426  C CB  . TYR A 54  ? 0.1991 0.2092 0.1952 -0.0128 -0.0659 0.0343  54  TYR A CB  
427  C CG  . TYR A 54  ? 0.2051 0.2062 0.1857 -0.0098 -0.0634 0.0275  54  TYR A CG  
428  C CD1 . TYR A 54  ? 0.2100 0.2115 0.1881 -0.0046 -0.0576 0.0238  54  TYR A CD1 
429  C CD2 . TYR A 54  ? 0.2146 0.2070 0.1837 -0.0123 -0.0670 0.0256  54  TYR A CD2 
430  C CE1 . TYR A 54  ? 0.2203 0.2145 0.1861 -0.0017 -0.0549 0.0189  54  TYR A CE1 
431  C CE2 . TYR A 54  ? 0.2297 0.2141 0.1858 -0.0093 -0.0641 0.0200  54  TYR A CE2 
432  C CZ  . TYR A 54  ? 0.2388 0.2243 0.1935 -0.0039 -0.0578 0.0169  54  TYR A CZ  
433  O OH  . TYR A 54  ? 0.2600 0.2383 0.2033 -0.0007 -0.0547 0.0126  54  TYR A OH  
434  N N   . GLU A 55  ? 0.2157 0.2401 0.2346 -0.0210 -0.0755 0.0513  55  GLU A N   
435  C CA  . GLU A 55  ? 0.2147 0.2503 0.2523 -0.0216 -0.0749 0.0585  55  GLU A CA  
436  C C   . GLU A 55  ? 0.2191 0.2544 0.2503 -0.0224 -0.0778 0.0605  55  GLU A C   
437  O O   . GLU A 55  ? 0.2158 0.2588 0.2585 -0.0196 -0.0739 0.0625  55  GLU A O   
438  C CB  . GLU A 55  ? 0.2489 0.2902 0.3003 -0.0271 -0.0801 0.0674  55  GLU A CB  
439  C CG  . GLU A 55  ? 0.3177 0.3632 0.3827 -0.0252 -0.0751 0.0679  55  GLU A CG  
440  C CD  . GLU A 55  ? 0.3953 0.4491 0.4783 -0.0201 -0.0658 0.0687  55  GLU A CD  
441  O OE1 . GLU A 55  ? 0.3796 0.4366 0.4658 -0.0173 -0.0623 0.0681  55  GLU A OE1 
442  O OE2 . GLU A 55  ? 0.4443 0.5004 0.5372 -0.0188 -0.0615 0.0697  55  GLU A OE2 
443  N N   . ASP A 56  ? 0.2230 0.2482 0.2347 -0.0260 -0.0845 0.0597  56  ASP A N   
444  C CA  . ASP A 56  ? 0.2304 0.2538 0.2334 -0.0269 -0.0872 0.0616  56  ASP A CA  
445  C C   . ASP A 56  ? 0.2346 0.2569 0.2318 -0.0198 -0.0798 0.0556  56  ASP A C   
446  O O   . ASP A 56  ? 0.2434 0.2719 0.2470 -0.0182 -0.0783 0.0583  56  ASP A O   
447  C CB  . ASP A 56  ? 0.2578 0.2683 0.2388 -0.0329 -0.0960 0.0623  56  ASP A CB  
448  C CG  . ASP A 56  ? 0.3026 0.3156 0.2907 -0.0413 -0.1053 0.0708  56  ASP A CG  
449  O OD1 . ASP A 56  ? 0.2869 0.3134 0.2985 -0.0422 -0.1049 0.0781  56  ASP A OD1 
450  O OD2 . ASP A 56  ? 0.3320 0.3330 0.3023 -0.0470 -0.1130 0.0709  56  ASP A OD2 
451  N N   . LEU A 57  ? 0.2342 0.2493 0.2205 -0.0158 -0.0754 0.0482  57  LEU A N   
452  C CA  . LEU A 57  ? 0.2381 0.2527 0.2202 -0.0093 -0.0686 0.0437  57  LEU A CA  
453  C C   . LEU A 57  ? 0.2260 0.2529 0.2289 -0.0057 -0.0628 0.0448  57  LEU A C   
454  O O   . LEU A 57  ? 0.2258 0.2561 0.2308 -0.0021 -0.0595 0.0449  57  LEU A O   
455  C CB  . LEU A 57  ? 0.2503 0.2561 0.2198 -0.0060 -0.0651 0.0369  57  LEU A CB  
456  C CG  . LEU A 57  ? 0.2895 0.2804 0.2353 -0.0081 -0.0690 0.0346  57  LEU A CG  
457  C CD1 . LEU A 57  ? 0.3054 0.2892 0.2426 -0.0049 -0.0650 0.0287  57  LEU A CD1 
458  C CD2 . LEU A 57  ? 0.3070 0.2920 0.2385 -0.0060 -0.0683 0.0350  57  LEU A CD2 
459  N N   . LEU A 58  ? 0.2097 0.2422 0.2272 -0.0068 -0.0616 0.0459  58  LEU A N   
460  C CA  . LEU A 58  ? 0.2064 0.2478 0.2414 -0.0036 -0.0557 0.0464  58  LEU A CA  
461  C C   . LEU A 58  ? 0.2077 0.2577 0.2561 -0.0045 -0.0564 0.0529  58  LEU A C   
462  O O   . LEU A 58  ? 0.2154 0.2705 0.2731 -0.0010 -0.0514 0.0525  58  LEU A O   
463  C CB  . LEU A 58  ? 0.2030 0.2459 0.2476 -0.0042 -0.0534 0.0458  58  LEU A CB  
464  C CG  . LEU A 58  ? 0.2085 0.2557 0.2651 -0.0005 -0.0460 0.0438  58  LEU A CG  
465  C CD1 . LEU A 58  ? 0.2022 0.2459 0.2502 0.0035  -0.0423 0.0379  58  LEU A CD1 
466  C CD2 . LEU A 58  ? 0.2163 0.2637 0.2805 -0.0013 -0.0438 0.0438  58  LEU A CD2 
467  N N   . ILE A 59  ? 0.2065 0.2578 0.2550 -0.0094 -0.0630 0.0590  59  ILE A N   
468  C CA  . ILE A 59  ? 0.2165 0.2764 0.2778 -0.0106 -0.0643 0.0661  59  ILE A CA  
469  C C   . ILE A 59  ? 0.2255 0.2857 0.2813 -0.0069 -0.0619 0.0643  59  ILE A C   
470  O O   . ILE A 59  ? 0.2214 0.2898 0.2908 -0.0055 -0.0597 0.0681  59  ILE A O   
471  C CB  . ILE A 59  ? 0.2392 0.2992 0.2986 -0.0174 -0.0732 0.0734  59  ILE A CB  
472  C CG1 . ILE A 59  ? 0.2630 0.3255 0.3329 -0.0213 -0.0757 0.0777  59  ILE A CG1 
473  C CG2 . ILE A 59  ? 0.2463 0.3149 0.3164 -0.0188 -0.0750 0.0808  59  ILE A CG2 
474  C CD1 . ILE A 59  ? 0.2926 0.3538 0.3584 -0.0292 -0.0861 0.0852  59  ILE A CD1 
475  N N   . ARG A 60  ? 0.2395 0.2907 0.2757 -0.0051 -0.0622 0.0591  60  ARG A N   
476  C CA  . ARG A 60  ? 0.2522 0.3034 0.2828 -0.0012 -0.0596 0.0581  60  ARG A CA  
477  C C   . ARG A 60  ? 0.2388 0.2934 0.2769 0.0044  -0.0524 0.0543  60  ARG A C   
478  O O   . ARG A 60  ? 0.2522 0.3074 0.2870 0.0080  -0.0500 0.0539  60  ARG A O   
479  C CB  . ARG A 60  ? 0.2970 0.3364 0.3034 -0.0011 -0.0620 0.0552  60  ARG A CB  
480  C CG  . ARG A 60  ? 0.3633 0.3965 0.3587 -0.0077 -0.0701 0.0585  60  ARG A CG  
481  C CD  . ARG A 60  ? 0.4112 0.4515 0.4147 -0.0112 -0.0745 0.0661  60  ARG A CD  
482  N NE  . ARG A 60  ? 0.4675 0.5059 0.4695 -0.0189 -0.0830 0.0711  60  ARG A NE  
483  C CZ  . ARG A 60  ? 0.4890 0.5351 0.5020 -0.0237 -0.0881 0.0793  60  ARG A CZ  
484  N NH1 . ARG A 60  ? 0.4853 0.5294 0.4970 -0.0313 -0.0964 0.0846  60  ARG A NH1 
485  N NH2 . ARG A 60  ? 0.4813 0.5375 0.5075 -0.0212 -0.0853 0.0830  60  ARG A NH2 
486  N N   . LYS A 61  ? 0.2107 0.2668 0.2580 0.0050  -0.0491 0.0517  61  LYS A N   
487  C CA  . LYS A 61  ? 0.2015 0.2591 0.2540 0.0092  -0.0432 0.0481  61  LYS A CA  
488  C C   . LYS A 61  ? 0.1973 0.2624 0.2687 0.0094  -0.0401 0.0509  61  LYS A C   
489  O O   . LYS A 61  ? 0.2081 0.2760 0.2892 0.0068  -0.0408 0.0540  61  LYS A O   
490  C CB  . LYS A 61  ? 0.2188 0.2701 0.2642 0.0098  -0.0414 0.0424  61  LYS A CB  
491  C CG  . LYS A 61  ? 0.2620 0.3046 0.2885 0.0101  -0.0435 0.0394  61  LYS A CG  
492  C CD  . LYS A 61  ? 0.3096 0.3507 0.3275 0.0139  -0.0418 0.0394  61  LYS A CD  
493  C CE  . LYS A 61  ? 0.3620 0.3928 0.3608 0.0150  -0.0423 0.0363  61  LYS A CE  
494  N NZ  . LYS A 61  ? 0.3994 0.4282 0.3897 0.0193  -0.0397 0.0373  61  LYS A NZ  
495  N N   . SER A 62  ? 0.1776 0.2457 0.2545 0.0125  -0.0365 0.0504  62  SER A N   
496  C CA  . SER A 62  ? 0.1690 0.2418 0.2617 0.0132  -0.0327 0.0521  62  SER A CA  
497  C C   . SER A 62  ? 0.1510 0.2194 0.2419 0.0152  -0.0285 0.0468  62  SER A C   
498  O O   . SER A 62  ? 0.1477 0.2118 0.2273 0.0164  -0.0288 0.0431  62  SER A O   
499  C CB  . SER A 62  ? 0.2000 0.2793 0.3004 0.0144  -0.0328 0.0566  62  SER A CB  
500  O OG  . SER A 62  ? 0.2401 0.3234 0.3417 0.0120  -0.0372 0.0620  62  SER A OG  
501  N N   . ASN A 63  ? 0.1426 0.2113 0.2442 0.0155  -0.0244 0.0467  63  ASN A N   
502  C CA  . ASN A 63  ? 0.1389 0.2022 0.2378 0.0164  -0.0210 0.0420  63  ASN A CA  
503  C C   . ASN A 63  ? 0.1396 0.2029 0.2325 0.0181  -0.0221 0.0410  63  ASN A C   
504  O O   . ASN A 63  ? 0.1422 0.2008 0.2270 0.0182  -0.0218 0.0372  63  ASN A O   
505  C CB  . ASN A 63  ? 0.1400 0.2028 0.2503 0.0167  -0.0165 0.0429  63  ASN A CB  
506  C CG  . ASN A 63  ? 0.1606 0.2220 0.2770 0.0158  -0.0136 0.0440  63  ASN A CG  
507  O OD1 . ASN A 63  ? 0.1610 0.2198 0.2717 0.0147  -0.0145 0.0422  63  ASN A OD1 
508  N ND2 . ASN A 63  ? 0.1556 0.2186 0.2845 0.0164  -0.0096 0.0474  63  ASN A ND2 
509  N N   . HIS A 64  ? 0.1366 0.2058 0.2344 0.0194  -0.0233 0.0450  64  HIS A N   
510  C CA  . HIS A 64  ? 0.1395 0.2098 0.2337 0.0214  -0.0239 0.0456  64  HIS A CA  
511  C C   . HIS A 64  ? 0.1476 0.2159 0.2288 0.0228  -0.0257 0.0445  64  HIS A C   
512  O O   . HIS A 64  ? 0.1578 0.2267 0.2361 0.0249  -0.0255 0.0453  64  HIS A O   
513  C CB  . HIS A 64  ? 0.1440 0.2214 0.2474 0.0228  -0.0243 0.0507  64  HIS A CB  
514  C CG  . HIS A 64  ? 0.1574 0.2393 0.2592 0.0231  -0.0269 0.0545  64  HIS A CG  
515  N ND1 . HIS A 64  ? 0.1694 0.2548 0.2790 0.0213  -0.0277 0.0575  64  HIS A ND1 
516  C CD2 . HIS A 64  ? 0.1738 0.2566 0.2667 0.0250  -0.0286 0.0562  64  HIS A CD2 
517  C CE1 . HIS A 64  ? 0.1754 0.2634 0.2797 0.0213  -0.0308 0.0606  64  HIS A CE1 
518  N NE2 . HIS A 64  ? 0.1810 0.2667 0.2742 0.0237  -0.0311 0.0595  64  HIS A NE2 
519  N N   . ASN A 65  ? 0.1421 0.2078 0.2157 0.0217  -0.0274 0.0433  65  ASN A N   
520  C CA  . ASN A 65  ? 0.1553 0.2168 0.2150 0.0231  -0.0285 0.0418  65  ASN A CA  
521  C C   . ASN A 65  ? 0.1613 0.2173 0.2150 0.0229  -0.0272 0.0373  65  ASN A C   
522  O O   . ASN A 65  ? 0.1761 0.2288 0.2198 0.0247  -0.0271 0.0365  65  ASN A O   
523  C CB  . ASN A 65  ? 0.1695 0.2287 0.2218 0.0213  -0.0315 0.0422  65  ASN A CB  
524  C CG  . ASN A 65  ? 0.2148 0.2782 0.2691 0.0212  -0.0336 0.0470  65  ASN A CG  
525  O OD1 . ASN A 65  ? 0.2319 0.2968 0.2893 0.0182  -0.0363 0.0491  65  ASN A OD1 
526  N ND2 . ASN A 65  ? 0.2177 0.2836 0.2708 0.0243  -0.0325 0.0495  65  ASN A ND2 
527  N N   . PHE A 66  ? 0.1497 0.2042 0.2089 0.0208  -0.0259 0.0348  66  PHE A N   
528  C CA  . PHE A 66  ? 0.1500 0.1993 0.2036 0.0201  -0.0250 0.0308  66  PHE A CA  
529  C C   . PHE A 66  ? 0.1633 0.2130 0.2202 0.0205  -0.0239 0.0311  66  PHE A C   
530  O O   . PHE A 66  ? 0.1783 0.2277 0.2423 0.0190  -0.0227 0.0309  66  PHE A O   
531  C CB  . PHE A 66  ? 0.1409 0.1871 0.1969 0.0175  -0.0240 0.0280  66  PHE A CB  
532  C CG  . PHE A 66  ? 0.1481 0.1940 0.2013 0.0164  -0.0260 0.0284  66  PHE A CG  
533  C CD1 . PHE A 66  ? 0.1628 0.2043 0.2053 0.0161  -0.0275 0.0261  66  PHE A CD1 
534  C CD2 . PHE A 66  ? 0.1524 0.2022 0.2140 0.0153  -0.0266 0.0318  66  PHE A CD2 
535  C CE1 . PHE A 66  ? 0.1717 0.2122 0.2112 0.0143  -0.0302 0.0269  66  PHE A CE1 
536  C CE2 . PHE A 66  ? 0.1617 0.2114 0.2212 0.0134  -0.0295 0.0333  66  PHE A CE2 
537  C CZ  . PHE A 66  ? 0.1615 0.2061 0.2093 0.0127  -0.0316 0.0307  66  PHE A CZ  
538  N N   . LEU A 67  ? 0.1528 0.2026 0.2045 0.0223  -0.0242 0.0323  67  LEU A N   
539  C CA  . LEU A 67  ? 0.1549 0.2058 0.2102 0.0223  -0.0241 0.0341  67  LEU A CA  
540  C C   . LEU A 67  ? 0.1556 0.2011 0.2063 0.0197  -0.0242 0.0307  67  LEU A C   
541  O O   . LEU A 67  ? 0.1556 0.1989 0.1989 0.0204  -0.0242 0.0295  67  LEU A O   
542  C CB  . LEU A 67  ? 0.1694 0.2240 0.2231 0.0259  -0.0240 0.0387  67  LEU A CB  
543  C CG  . LEU A 67  ? 0.2040 0.2634 0.2603 0.0286  -0.0238 0.0424  67  LEU A CG  
544  C CD1 . LEU A 67  ? 0.2174 0.2792 0.2706 0.0330  -0.0225 0.0471  67  LEU A CD1 
545  C CD2 . LEU A 67  ? 0.2184 0.2820 0.2861 0.0273  -0.0243 0.0444  67  LEU A CD2 
546  N N   . VAL A 68  ? 0.1411 0.1836 0.1954 0.0166  -0.0241 0.0291  68  VAL A N   
547  C CA  . VAL A 68  ? 0.1470 0.1832 0.1958 0.0135  -0.0243 0.0257  68  VAL A CA  
548  C C   . VAL A 68  ? 0.1559 0.1913 0.2065 0.0113  -0.0262 0.0282  68  VAL A C   
549  O O   . VAL A 68  ? 0.1585 0.1941 0.2148 0.0103  -0.0265 0.0298  68  VAL A O   
550  C CB  . VAL A 68  ? 0.1612 0.1918 0.2099 0.0114  -0.0221 0.0215  68  VAL A CB  
551  C CG1 . VAL A 68  ? 0.1670 0.1902 0.2084 0.0082  -0.0220 0.0178  68  VAL A CG1 
552  C CG2 . VAL A 68  ? 0.1702 0.2028 0.2190 0.0132  -0.0210 0.0205  68  VAL A CG2 
553  N N   . GLN A 69  ? 0.1602 0.1952 0.2065 0.0104  -0.0278 0.0294  69  GLN A N   
554  C CA  . GLN A 69  ? 0.1772 0.2122 0.2259 0.0077  -0.0307 0.0333  69  GLN A CA  
555  C C   . GLN A 69  ? 0.1946 0.2232 0.2361 0.0033  -0.0323 0.0309  69  GLN A C   
556  O O   . GLN A 69  ? 0.1901 0.2187 0.2267 0.0043  -0.0316 0.0296  69  GLN A O   
557  C CB  . GLN A 69  ? 0.1963 0.2396 0.2497 0.0114  -0.0313 0.0402  69  GLN A CB  
558  C CG  . GLN A 69  ? 0.2373 0.2833 0.2968 0.0091  -0.0347 0.0466  69  GLN A CG  
559  C CD  . GLN A 69  ? 0.2773 0.3317 0.3418 0.0139  -0.0339 0.0540  69  GLN A CD  
560  O OE1 . GLN A 69  ? 0.2862 0.3444 0.3514 0.0190  -0.0309 0.0547  69  GLN A OE1 
561  N NE2 . GLN A 69  ? 0.2905 0.3473 0.3582 0.0121  -0.0365 0.0602  69  GLN A NE2 
562  N N   . ALA A 70  ? 0.2201 0.2421 0.2599 -0.0017 -0.0344 0.0301  70  ALA A N   
563  C CA  . ALA A 70  ? 0.2502 0.2644 0.2818 -0.0071 -0.0366 0.0280  70  ALA A CA  
564  C C   . ALA A 70  ? 0.2762 0.2930 0.3110 -0.0104 -0.0418 0.0350  70  ALA A C   
565  O O   . ALA A 70  ? 0.2803 0.2952 0.3183 -0.0131 -0.0442 0.0374  70  ALA A O   
566  C CB  . ALA A 70  ? 0.2561 0.2590 0.2818 -0.0106 -0.0351 0.0226  70  ALA A CB  
567  N N   . GLY A 71  ? 0.2932 0.3155 0.3291 -0.0097 -0.0433 0.0393  71  GLY A N   
568  C CA  . GLY A 71  ? 0.3039 0.3312 0.3459 -0.0122 -0.0480 0.0480  71  GLY A CA  
569  C C   . GLY A 71  ? 0.3035 0.3394 0.3562 -0.0076 -0.0472 0.0536  71  GLY A C   
570  O O   . GLY A 71  ? 0.3133 0.3550 0.3687 -0.0011 -0.0430 0.0534  71  GLY A O   
571  N N   A ASN A 72  ? 0.2967 0.3324 0.3544 -0.0112 -0.0512 0.0581  72  ASN A N   
572  N N   B ASN A 72  ? 0.2996 0.3356 0.3576 -0.0112 -0.0512 0.0583  72  ASN A N   
573  C CA  A ASN A 72  ? 0.2894 0.3333 0.3579 -0.0072 -0.0506 0.0637  72  ASN A CA  
574  C CA  B ASN A 72  ? 0.2953 0.3396 0.3641 -0.0070 -0.0505 0.0639  72  ASN A CA  
575  C C   A ASN A 72  ? 0.2844 0.3241 0.3527 -0.0065 -0.0484 0.0581  72  ASN A C   
576  C C   B ASN A 72  ? 0.2858 0.3261 0.3550 -0.0067 -0.0489 0.0590  72  ASN A C   
577  O O   A ASN A 72  ? 0.2848 0.3311 0.3618 -0.0030 -0.0476 0.0620  72  ASN A O   
578  O O   B ASN A 72  ? 0.2853 0.3318 0.3635 -0.0041 -0.0489 0.0637  72  ASN A O   
579  C CB  A ASN A 72  ? 0.3023 0.3498 0.3786 -0.0113 -0.0566 0.0734  72  ASN A CB  
580  C CB  B ASN A 72  ? 0.3169 0.3666 0.3945 -0.0100 -0.0560 0.0746  72  ASN A CB  
581  C CG  A ASN A 72  ? 0.3301 0.3891 0.4194 -0.0061 -0.0557 0.0819  72  ASN A CG  
582  C CG  B ASN A 72  ? 0.3733 0.4141 0.4471 -0.0192 -0.0627 0.0749  72  ASN A CG  
583  O OD1 A ASN A 72  ? 0.3382 0.4048 0.4309 0.0010  -0.0511 0.0846  72  ASN A OD1 
584  O OD1 B ASN A 72  ? 0.3977 0.4295 0.4666 -0.0221 -0.0629 0.0691  72  ASN A OD1 
585  N ND2 A ASN A 72  ? 0.3352 0.3945 0.4310 -0.0093 -0.0598 0.0863  72  ASN A ND2 
586  N ND2 B ASN A 72  ? 0.3798 0.4222 0.4556 -0.0241 -0.0683 0.0824  72  ASN A ND2 
587  N N   A VAL A 73  ? 0.2756 0.3045 0.3347 -0.0096 -0.0471 0.0497  73  VAL A N   
588  N N   B VAL A 73  ? 0.2733 0.3034 0.3335 -0.0091 -0.0471 0.0504  73  VAL A N   
589  C CA  A VAL A 73  ? 0.2687 0.2933 0.3288 -0.0090 -0.0446 0.0455  73  VAL A CA  
590  C CA  B VAL A 73  ? 0.2623 0.2875 0.3231 -0.0089 -0.0448 0.0461  73  VAL A CA  
591  C C   A VAL A 73  ? 0.2429 0.2701 0.3030 -0.0034 -0.0389 0.0407  73  VAL A C   
592  C C   B VAL A 73  ? 0.2460 0.2730 0.3061 -0.0036 -0.0390 0.0408  73  VAL A C   
593  O O   A VAL A 73  ? 0.2341 0.2588 0.2876 -0.0027 -0.0367 0.0363  73  VAL A O   
594  O O   B VAL A 73  ? 0.2468 0.2705 0.2999 -0.0032 -0.0369 0.0361  73  VAL A O   
595  C CB  A VAL A 73  ? 0.2938 0.3038 0.3449 -0.0155 -0.0460 0.0407  73  VAL A CB  
596  C CB  B VAL A 73  ? 0.2769 0.2878 0.3287 -0.0159 -0.0468 0.0418  73  VAL A CB  
597  C CG1 A VAL A 73  ? 0.3138 0.3149 0.3532 -0.0169 -0.0432 0.0334  73  VAL A CG1 
598  C CG1 B VAL A 73  ? 0.2857 0.2897 0.3364 -0.0147 -0.0422 0.0361  73  VAL A CG1 
599  C CG2 A VAL A 73  ? 0.3009 0.3074 0.3558 -0.0147 -0.0435 0.0388  73  VAL A CG2 
600  C CG2 B VAL A 73  ? 0.2809 0.2903 0.3351 -0.0215 -0.0535 0.0482  73  VAL A CG2 
601  N N   . GLN A 74  ? 0.2292 0.2618 0.2972 0.0002  -0.0370 0.0423  74  GLN A N   
602  C CA  . GLN A 74  ? 0.2079 0.2433 0.2770 0.0046  -0.0327 0.0391  74  GLN A CA  
603  C C   . GLN A 74  ? 0.2000 0.2265 0.2658 0.0028  -0.0296 0.0331  74  GLN A C   
604  O O   . GLN A 74  ? 0.2053 0.2250 0.2715 -0.0002 -0.0298 0.0324  74  GLN A O   
605  C CB  . GLN A 74  ? 0.2017 0.2464 0.2807 0.0086  -0.0322 0.0440  74  GLN A CB  
606  C CG  . GLN A 74  ? 0.2025 0.2529 0.2815 0.0135  -0.0293 0.0433  74  GLN A CG  
607  C CD  . GLN A 74  ? 0.2277 0.2810 0.3015 0.0159  -0.0294 0.0447  74  GLN A CD  
608  O OE1 . GLN A 74  ? 0.2352 0.2901 0.3093 0.0154  -0.0314 0.0487  74  GLN A OE1 
609  N NE2 . GLN A 74  ? 0.2313 0.2853 0.3008 0.0187  -0.0273 0.0422  74  GLN A NE2 
610  N N   . LEU A 75  ? 0.1864 0.2124 0.2489 0.0049  -0.0264 0.0291  75  LEU A N   
611  C CA  . LEU A 75  ? 0.1892 0.2081 0.2503 0.0042  -0.0224 0.0246  75  LEU A CA  
612  C C   . LEU A 75  ? 0.1778 0.2034 0.2479 0.0079  -0.0199 0.0263  75  LEU A C   
613  O O   . LEU A 75  ? 0.1848 0.2187 0.2575 0.0108  -0.0208 0.0287  75  LEU A O   
614  C CB  . LEU A 75  ? 0.2020 0.2155 0.2545 0.0034  -0.0207 0.0199  75  LEU A CB  
615  C CG  . LEU A 75  ? 0.2354 0.2421 0.2782 -0.0007 -0.0233 0.0183  75  LEU A CG  
616  C CD1 . LEU A 75  ? 0.2468 0.2484 0.2818 -0.0012 -0.0210 0.0136  75  LEU A CD1 
617  C CD2 . LEU A 75  ? 0.2622 0.2593 0.3016 -0.0052 -0.0245 0.0178  75  LEU A CD2 
618  N N   . ARG A 76  ? 0.1580 0.1790 0.2321 0.0075  -0.0166 0.0253  76  ARG A N   
619  C CA  . ARG A 76  ? 0.1483 0.1758 0.2325 0.0104  -0.0142 0.0278  76  ARG A CA  
620  C C   . ARG A 76  ? 0.1556 0.1822 0.2391 0.0115  -0.0110 0.0257  76  ARG A C   
621  O O   . ARG A 76  ? 0.1705 0.1882 0.2501 0.0103  -0.0073 0.0224  76  ARG A O   
622  C CB  . ARG A 76  ? 0.1542 0.1774 0.2447 0.0098  -0.0118 0.0289  76  ARG A CB  
623  C CG  . ARG A 76  ? 0.1544 0.1859 0.2574 0.0127  -0.0099 0.0329  76  ARG A CG  
624  C CD  . ARG A 76  ? 0.1620 0.1890 0.2716 0.0122  -0.0073 0.0342  76  ARG A CD  
625  N NE  . ARG A 76  ? 0.1758 0.2025 0.2848 0.0104  -0.0115 0.0359  76  ARG A NE  
626  C CZ  . ARG A 76  ? 0.1826 0.2198 0.2994 0.0120  -0.0148 0.0409  76  ARG A CZ  
627  N NH1 . ARG A 76  ? 0.1608 0.2087 0.2855 0.0151  -0.0144 0.0443  76  ARG A NH1 
628  N NH2 . ARG A 76  ? 0.1781 0.2151 0.2948 0.0101  -0.0186 0.0432  76  ARG A NH2 
629  N N   . VAL A 77  ? 0.1442 0.1795 0.2310 0.0136  -0.0124 0.0281  77  VAL A N   
630  C CA  . VAL A 77  ? 0.1462 0.1822 0.2336 0.0142  -0.0106 0.0274  77  VAL A CA  
631  C C   . VAL A 77  ? 0.1473 0.1863 0.2465 0.0153  -0.0074 0.0309  77  VAL A C   
632  O O   . VAL A 77  ? 0.1462 0.1929 0.2530 0.0164  -0.0091 0.0352  77  VAL A O   
633  C CB  . VAL A 77  ? 0.1438 0.1855 0.2267 0.0150  -0.0144 0.0283  77  VAL A CB  
634  C CG1 . VAL A 77  ? 0.1508 0.1931 0.2347 0.0148  -0.0136 0.0284  77  VAL A CG1 
635  C CG2 . VAL A 77  ? 0.1555 0.1939 0.2278 0.0143  -0.0166 0.0254  77  VAL A CG2 
636  N N   . ILE A 78  ? 0.1447 0.1776 0.2457 0.0151  -0.0024 0.0296  78  ILE A N   
637  C CA  . ILE A 78  ? 0.1458 0.1813 0.2595 0.0165  0.0018  0.0339  78  ILE A CA  
638  C C   . ILE A 78  ? 0.1428 0.1822 0.2617 0.0169  0.0029  0.0366  78  ILE A C   
639  O O   . ILE A 78  ? 0.1463 0.1887 0.2773 0.0181  0.0065  0.0414  78  ILE A O   
640  C CB  . ILE A 78  ? 0.1617 0.1865 0.2757 0.0167  0.0081  0.0319  78  ILE A CB  
641  C CG1 . ILE A 78  ? 0.1846 0.1983 0.2883 0.0159  0.0119  0.0270  78  ILE A CG1 
642  C CG2 . ILE A 78  ? 0.1700 0.1918 0.2805 0.0156  0.0057  0.0305  78  ILE A CG2 
643  C CD1 . ILE A 78  ? 0.2057 0.2061 0.3078 0.0164  0.0196  0.0251  78  ILE A CD1 
644  N N   . GLY A 79  ? 0.1401 0.1801 0.2510 0.0159  -0.0006 0.0346  79  GLY A N   
645  C CA  . GLY A 79  ? 0.1374 0.1814 0.2527 0.0155  -0.0010 0.0377  79  GLY A CA  
646  C C   . GLY A 79  ? 0.1422 0.1855 0.2460 0.0141  -0.0057 0.0345  79  GLY A C   
647  O O   . GLY A 79  ? 0.1454 0.1836 0.2384 0.0138  -0.0065 0.0295  79  GLY A O   
648  N N   . HIS A 80  ? 0.1366 0.1849 0.2427 0.0130  -0.0091 0.0379  80  HIS A N   
649  C CA  . HIS A 80  ? 0.1385 0.1849 0.2335 0.0116  -0.0132 0.0350  80  HIS A CA  
650  C C   . HIS A 80  ? 0.1440 0.1931 0.2443 0.0101  -0.0145 0.0390  80  HIS A C   
651  O O   . HIS A 80  ? 0.1452 0.2003 0.2570 0.0095  -0.0151 0.0455  80  HIS A O   
652  C CB  . HIS A 80  ? 0.1439 0.1924 0.2301 0.0114  -0.0188 0.0341  80  HIS A CB  
653  C CG  . HIS A 80  ? 0.1623 0.2172 0.2534 0.0105  -0.0229 0.0397  80  HIS A CG  
654  N ND1 . HIS A 80  ? 0.1682 0.2281 0.2678 0.0115  -0.0222 0.0432  80  HIS A ND1 
655  C CD2 . HIS A 80  ? 0.1778 0.2344 0.2659 0.0082  -0.0280 0.0424  80  HIS A CD2 
656  C CE1 . HIS A 80  ? 0.1764 0.2412 0.2779 0.0098  -0.0268 0.0480  80  HIS A CE1 
657  N NE2 . HIS A 80  ? 0.1818 0.2442 0.2758 0.0076  -0.0306 0.0477  80  HIS A NE2 
658  N N   . SER A 81  ? 0.1420 0.1870 0.2347 0.0092  -0.0151 0.0359  81  SER A N   
659  C CA  . SER A 81  ? 0.1398 0.1873 0.2373 0.0074  -0.0171 0.0401  81  SER A CA  
660  C C   . SER A 81  ? 0.1430 0.1863 0.2279 0.0059  -0.0208 0.0359  81  SER A C   
661  O O   . SER A 81  ? 0.1548 0.1929 0.2294 0.0069  -0.0196 0.0299  81  SER A O   
662  C CB  . SER A 81  ? 0.1600 0.2070 0.2686 0.0087  -0.0103 0.0429  81  SER A CB  
663  O OG  . SER A 81  ? 0.2105 0.2497 0.3114 0.0102  -0.0053 0.0368  81  SER A OG  
664  N N   A MET A 82  ? 0.1375 0.1829 0.2230 0.0032  -0.0258 0.0397  82  MET A N   
665  N N   B MET A 82  ? 0.1341 0.1796 0.2199 0.0033  -0.0256 0.0397  82  MET A N   
666  C CA  A MET A 82  ? 0.1484 0.1893 0.2223 0.0016  -0.0295 0.0362  82  MET A CA  
667  C CA  B MET A 82  ? 0.1415 0.1826 0.2160 0.0016  -0.0294 0.0364  82  MET A CA  
668  C C   A MET A 82  ? 0.1526 0.1934 0.2328 0.0010  -0.0272 0.0382  82  MET A C   
669  C C   B MET A 82  ? 0.1480 0.1888 0.2288 0.0012  -0.0266 0.0382  82  MET A C   
670  O O   A MET A 82  ? 0.1586 0.2045 0.2514 -0.0002 -0.0274 0.0453  82  MET A O   
671  O O   B MET A 82  ? 0.1511 0.1969 0.2453 0.0005  -0.0257 0.0451  82  MET A O   
672  C CB  A MET A 82  ? 0.1567 0.1980 0.2242 -0.0015 -0.0375 0.0388  82  MET A CB  
673  C CB  B MET A 82  ? 0.1426 0.1844 0.2116 -0.0017 -0.0375 0.0395  82  MET A CB  
674  C CG  A MET A 82  ? 0.1915 0.2267 0.2458 -0.0031 -0.0413 0.0351  82  MET A CG  
675  C CG  B MET A 82  ? 0.1675 0.2033 0.2234 -0.0034 -0.0415 0.0359  82  MET A CG  
676  S SD  A MET A 82  ? 0.2388 0.2711 0.2825 -0.0073 -0.0506 0.0379  82  MET A SD  
677  S SD  B MET A 82  ? 0.1780 0.2095 0.2192 -0.0061 -0.0495 0.0362  82  MET A SD  
678  C CE  A MET A 82  ? 0.2376 0.2679 0.2717 -0.0043 -0.0496 0.0344  82  MET A CE  
679  C CE  B MET A 82  ? 0.1267 0.1648 0.1803 -0.0108 -0.0552 0.0463  82  MET A CE  
680  N N   . GLN A 83  ? 0.1542 0.1897 0.2265 0.0019  -0.0248 0.0327  83  GLN A N   
681  C CA  . GLN A 83  ? 0.1533 0.1881 0.2299 0.0016  -0.0223 0.0341  83  GLN A CA  
682  C C   . GLN A 83  ? 0.1433 0.1744 0.2080 -0.0004 -0.0275 0.0308  83  GLN A C   
683  O O   . GLN A 83  ? 0.1526 0.1789 0.2062 0.0006  -0.0269 0.0245  83  GLN A O   
684  C CB  . GLN A 83  ? 0.1894 0.2200 0.2662 0.0045  -0.0140 0.0304  83  GLN A CB  
685  C CG  . GLN A 83  ? 0.2466 0.2763 0.3275 0.0046  -0.0109 0.0324  83  GLN A CG  
686  C CD  . GLN A 83  ? 0.3106 0.3341 0.3886 0.0072  -0.0026 0.0284  83  GLN A CD  
687  O OE1 . GLN A 83  ? 0.3192 0.3381 0.3906 0.0083  0.0001  0.0235  83  GLN A OE1 
688  N NE2 . GLN A 83  ? 0.3279 0.3504 0.4102 0.0079  0.0015  0.0307  83  GLN A NE2 
689  N N   . ASN A 84  ? 0.1329 0.1659 0.1999 -0.0036 -0.0333 0.0354  84  ASN A N   
690  C CA  . ASN A 84  ? 0.1351 0.1634 0.1902 -0.0059 -0.0388 0.0327  84  ASN A CA  
691  C C   . ASN A 84  ? 0.1344 0.1580 0.1748 -0.0053 -0.0415 0.0273  84  ASN A C   
692  O O   . ASN A 84  ? 0.1453 0.1703 0.1853 -0.0060 -0.0442 0.0295  84  ASN A O   
693  C CB  . ASN A 84  ? 0.1455 0.1714 0.1997 -0.0050 -0.0352 0.0300  84  ASN A CB  
694  C CG  . ASN A 84  ? 0.1817 0.2124 0.2509 -0.0050 -0.0321 0.0365  84  ASN A CG  
695  O OD1 . ASN A 84  ? 0.1987 0.2336 0.2761 -0.0080 -0.0368 0.0437  84  ASN A OD1 
696  N ND2 . ASN A 84  ? 0.1855 0.2154 0.2584 -0.0019 -0.0241 0.0348  84  ASN A ND2 
697  N N   . CYS A 85  ? 0.1317 0.1500 0.1611 -0.0038 -0.0400 0.0211  85  CYS A N   
698  C CA  . CYS A 85  ? 0.1382 0.1524 0.1553 -0.0026 -0.0414 0.0172  85  CYS A CA  
699  C C   . CYS A 85  ? 0.1403 0.1555 0.1577 0.0007  -0.0364 0.0141  85  CYS A C   
700  O O   . CYS A 85  ? 0.1484 0.1605 0.1564 0.0022  -0.0366 0.0113  85  CYS A O   
701  C CB  . CYS A 85  ? 0.1510 0.1586 0.1558 -0.0033 -0.0439 0.0138  85  CYS A CB  
702  S SG  . CYS A 85  ? 0.1812 0.1858 0.1834 -0.0081 -0.0513 0.0176  85  CYS A SG  
703  N N   . VAL A 86  ? 0.1354 0.1543 0.1631 0.0017  -0.0318 0.0152  86  VAL A N   
704  C CA  A VAL A 86  ? 0.1452 0.1642 0.1728 0.0040  -0.0279 0.0128  86  VAL A CA  
705  C CA  B VAL A 86  ? 0.1442 0.1632 0.1719 0.0040  -0.0279 0.0127  86  VAL A CA  
706  C C   . VAL A 86  ? 0.1483 0.1718 0.1854 0.0047  -0.0267 0.0163  86  VAL A C   
707  O O   . VAL A 86  ? 0.1515 0.1785 0.1978 0.0036  -0.0272 0.0209  86  VAL A O   
708  C CB  A VAL A 86  ? 0.1624 0.1787 0.1895 0.0047  -0.0232 0.0093  86  VAL A CB  
709  C CB  B VAL A 86  ? 0.1550 0.1713 0.1828 0.0044  -0.0232 0.0096  86  VAL A CB  
710  C CG1 A VAL A 86  ? 0.1797 0.1922 0.1975 0.0041  -0.0245 0.0060  86  VAL A CG1 
711  C CG1 B VAL A 86  ? 0.1607 0.1764 0.1916 0.0057  -0.0188 0.0085  86  VAL A CG1 
712  C CG2 A VAL A 86  ? 0.1683 0.1855 0.2049 0.0046  -0.0191 0.0115  86  VAL A CG2 
713  C CG2 B VAL A 86  ? 0.1676 0.1800 0.1849 0.0042  -0.0245 0.0058  86  VAL A CG2 
714  N N   . LEU A 87  ? 0.1444 0.1682 0.1797 0.0063  -0.0256 0.0150  87  LEU A N   
715  C CA  . LEU A 87  ? 0.1464 0.1742 0.1906 0.0072  -0.0239 0.0179  87  LEU A CA  
716  C C   . LEU A 87  ? 0.1383 0.1635 0.1851 0.0082  -0.0185 0.0155  87  LEU A C   
717  O O   . LEU A 87  ? 0.1425 0.1635 0.1819 0.0082  -0.0176 0.0116  87  LEU A O   
718  C CB  . LEU A 87  ? 0.1632 0.1927 0.2037 0.0084  -0.0262 0.0185  87  LEU A CB  
719  C CG  . LEU A 87  ? 0.1963 0.2262 0.2314 0.0075  -0.0312 0.0207  87  LEU A CG  
720  C CD1 . LEU A 87  ? 0.2043 0.2347 0.2342 0.0095  -0.0320 0.0209  87  LEU A CD1 
721  C CD2 . LEU A 87  ? 0.2162 0.2502 0.2602 0.0053  -0.0333 0.0259  87  LEU A CD2 
722  N N   . LYS A 88  ? 0.1328 0.1598 0.1898 0.0087  -0.0150 0.0182  88  LYS A N   
723  C CA  . LYS A 88  ? 0.1334 0.1560 0.1921 0.0095  -0.0095 0.0163  88  LYS A CA  
724  C C   . LYS A 88  ? 0.1333 0.1590 0.1978 0.0105  -0.0093 0.0185  88  LYS A C   
725  O O   . LYS A 88  ? 0.1402 0.1711 0.2146 0.0109  -0.0093 0.0232  88  LYS A O   
726  C CB  . LYS A 88  ? 0.1473 0.1683 0.2136 0.0100  -0.0042 0.0184  88  LYS A CB  
727  C CG  . LYS A 88  ? 0.2015 0.2189 0.2621 0.0092  -0.0036 0.0161  88  LYS A CG  
728  C CD  . LYS A 88  ? 0.2553 0.2703 0.3230 0.0103  0.0028  0.0185  88  LYS A CD  
729  C CE  . LYS A 88  ? 0.3066 0.3292 0.3880 0.0106  0.0021  0.0258  88  LYS A CE  
730  N NZ  . LYS A 88  ? 0.3299 0.3515 0.4180 0.0116  0.0074  0.0291  88  LYS A NZ  
731  N N   . LEU A 89  ? 0.1301 0.1534 0.1893 0.0106  -0.0097 0.0159  89  LEU A N   
732  C CA  . LEU A 89  ? 0.1294 0.1554 0.1937 0.0114  -0.0098 0.0179  89  LEU A CA  
733  C C   . LEU A 89  ? 0.1356 0.1549 0.2012 0.0113  -0.0048 0.0163  89  LEU A C   
734  O O   . LEU A 89  ? 0.1483 0.1607 0.2054 0.0100  -0.0042 0.0125  89  LEU A O   
735  C CB  . LEU A 89  ? 0.1331 0.1607 0.1908 0.0116  -0.0137 0.0171  89  LEU A CB  
736  C CG  . LEU A 89  ? 0.1403 0.1710 0.1923 0.0120  -0.0178 0.0176  89  LEU A CG  
737  C CD1 . LEU A 89  ? 0.1515 0.1830 0.1976 0.0129  -0.0200 0.0174  89  LEU A CD1 
738  C CD2 . LEU A 89  ? 0.1466 0.1827 0.2044 0.0123  -0.0197 0.0217  89  LEU A CD2 
739  N N   . LYS A 90  ? 0.1274 0.1477 0.2030 0.0124  -0.0010 0.0194  90  LYS A N   
740  C CA  . LYS A 90  ? 0.1365 0.1485 0.2125 0.0126  0.0046  0.0179  90  LYS A CA  
741  C C   . LYS A 90  ? 0.1366 0.1485 0.2118 0.0120  0.0022  0.0178  90  LYS A C   
742  O O   . LYS A 90  ? 0.1371 0.1575 0.2191 0.0129  -0.0008 0.0213  90  LYS A O   
743  C CB  . LYS A 90  ? 0.1591 0.1726 0.2476 0.0146  0.0101  0.0223  90  LYS A CB  
744  C CG  . LYS A 90  ? 0.2237 0.2255 0.3100 0.0152  0.0174  0.0202  90  LYS A CG  
745  C CD  . LYS A 90  ? 0.3041 0.3069 0.4037 0.0179  0.0242  0.0252  90  LYS A CD  
746  C CE  . LYS A 90  ? 0.3769 0.3655 0.4717 0.0188  0.0320  0.0225  90  LYS A CE  
747  N NZ  . LYS A 90  ? 0.4068 0.3943 0.5138 0.0222  0.0407  0.0276  90  LYS A NZ  
748  N N   . VAL A 91  ? 0.1419 0.1445 0.2081 0.0102  0.0029  0.0140  91  VAL A N   
749  C CA  . VAL A 91  ? 0.1498 0.1516 0.2152 0.0089  0.0001  0.0144  91  VAL A CA  
750  C C   . VAL A 91  ? 0.1577 0.1489 0.2230 0.0084  0.0052  0.0133  91  VAL A C   
751  O O   . VAL A 91  ? 0.1654 0.1478 0.2276 0.0088  0.0111  0.0113  91  VAL A O   
752  C CB  . VAL A 91  ? 0.1528 0.1533 0.2083 0.0064  -0.0051 0.0124  91  VAL A CB  
753  C CG1 . VAL A 91  ? 0.1531 0.1640 0.2097 0.0079  -0.0093 0.0143  91  VAL A CG1 
754  C CG2 . VAL A 91  ? 0.1613 0.1508 0.2049 0.0039  -0.0033 0.0078  91  VAL A CG2 
755  N N   . ASP A 92  ? 0.1643 0.1553 0.2322 0.0075  0.0033  0.0149  92  ASP A N   
756  C CA  . ASP A 92  ? 0.1792 0.1588 0.2466 0.0069  0.0081  0.0140  92  ASP A CA  
757  C C   . ASP A 92  ? 0.1994 0.1631 0.2511 0.0028  0.0081  0.0092  92  ASP A C   
758  O O   . ASP A 92  ? 0.2231 0.1741 0.2708 0.0018  0.0121  0.0077  92  ASP A O   
759  C CB  . ASP A 92  ? 0.1931 0.1787 0.2710 0.0077  0.0064  0.0181  92  ASP A CB  
760  C CG  . ASP A 92  ? 0.2553 0.2417 0.3296 0.0047  -0.0003 0.0188  92  ASP A CG  
761  O OD1 . ASP A 92  ? 0.2611 0.2460 0.3260 0.0022  -0.0045 0.0169  92  ASP A OD1 
762  O OD2 . ASP A 92  ? 0.2915 0.2806 0.3734 0.0049  -0.0014 0.0220  92  ASP A OD2 
763  N N   . THR A 93  ? 0.1939 0.1574 0.2361 0.0001  0.0033  0.0071  93  THR A N   
764  C CA  . THR A 93  ? 0.2104 0.1596 0.2373 -0.0047 0.0018  0.0033  93  THR A CA  
765  C C   . THR A 93  ? 0.2101 0.1555 0.2272 -0.0055 0.0029  -0.0002 93  THR A C   
766  O O   . THR A 93  ? 0.2088 0.1651 0.2291 -0.0043 -0.0001 0.0009  93  THR A O   
767  C CB  . THR A 93  ? 0.2348 0.1888 0.2611 -0.0082 -0.0067 0.0059  93  THR A CB  
768  O OG1 . THR A 93  ? 0.2512 0.2085 0.2869 -0.0075 -0.0075 0.0093  93  THR A OG1 
769  C CG2 . THR A 93  ? 0.2512 0.1918 0.2621 -0.0145 -0.0103 0.0033  93  THR A CG2 
770  N N   . ALA A 94  ? 0.2136 0.1424 0.2181 -0.0075 0.0076  -0.0044 94  ALA A N   
771  C CA  . ALA A 94  ? 0.2209 0.1446 0.2147 -0.0087 0.0087  -0.0077 94  ALA A CA  
772  C C   . ALA A 94  ? 0.2124 0.1362 0.1976 -0.0140 0.0003  -0.0079 94  ALA A C   
773  O O   . ALA A 94  ? 0.2162 0.1342 0.1968 -0.0183 -0.0041 -0.0072 94  ALA A O   
774  C CB  . ALA A 94  ? 0.2408 0.1451 0.2218 -0.0095 0.0164  -0.0119 94  ALA A CB  
775  N N   . ASN A 95  ? 0.1950 0.1255 0.1786 -0.0141 -0.0022 -0.0083 95  ASN A N   
776  C CA  . ASN A 95  ? 0.1934 0.1243 0.1698 -0.0190 -0.0096 -0.0076 95  ASN A CA  
777  C C   . ASN A 95  ? 0.2259 0.1381 0.1848 -0.0249 -0.0097 -0.0111 95  ASN A C   
778  O O   . ASN A 95  ? 0.2395 0.1421 0.1889 -0.0248 -0.0045 -0.0150 95  ASN A O   
779  C CB  . ASN A 95  ? 0.1754 0.1158 0.1533 -0.0175 -0.0111 -0.0075 95  ASN A CB  
780  C CG  . ASN A 95  ? 0.1885 0.1314 0.1617 -0.0219 -0.0184 -0.0054 95  ASN A CG  
781  O OD1 . ASN A 95  ? 0.1915 0.1291 0.1601 -0.0268 -0.0232 -0.0037 95  ASN A OD1 
782  N ND2 . ASN A 95  ? 0.1933 0.1446 0.1685 -0.0204 -0.0197 -0.0048 95  ASN A ND2 
783  N N   . PRO A 96  ? 0.2378 0.1442 0.1916 -0.0304 -0.0156 -0.0095 96  PRO A N   
784  C CA  . PRO A 96  ? 0.2611 0.1476 0.1956 -0.0371 -0.0165 -0.0128 96  PRO A CA  
785  C C   . PRO A 96  ? 0.2771 0.1609 0.2007 -0.0411 -0.0196 -0.0140 96  PRO A C   
786  O O   . PRO A 96  ? 0.3125 0.1787 0.2182 -0.0458 -0.0185 -0.0178 96  PRO A O   
787  C CB  . PRO A 96  ? 0.2739 0.1579 0.2084 -0.0424 -0.0239 -0.0091 96  PRO A CB  
788  C CG  . PRO A 96  ? 0.2656 0.1705 0.2179 -0.0394 -0.0285 -0.0032 96  PRO A CG  
789  C CD  . PRO A 96  ? 0.2328 0.1500 0.1975 -0.0311 -0.0220 -0.0040 96  PRO A CD  
790  N N   A LYS A 97  ? 0.2603 0.1608 0.1938 -0.0391 -0.0232 -0.0109 97  LYS A N   
791  N N   B LYS A 97  ? 0.2564 0.1568 0.1898 -0.0392 -0.0232 -0.0109 97  LYS A N   
792  C CA  A LYS A 97  ? 0.2636 0.1643 0.1896 -0.0422 -0.0261 -0.0113 97  LYS A CA  
793  C CA  B LYS A 97  ? 0.2560 0.1561 0.1815 -0.0424 -0.0262 -0.0113 97  LYS A CA  
794  C C   A LYS A 97  ? 0.2614 0.1653 0.1889 -0.0368 -0.0193 -0.0146 97  LYS A C   
795  C C   B LYS A 97  ? 0.2585 0.1605 0.1841 -0.0374 -0.0192 -0.0149 97  LYS A C   
796  O O   A LYS A 97  ? 0.2606 0.1709 0.1879 -0.0373 -0.0216 -0.0138 97  LYS A O   
797  O O   B LYS A 97  ? 0.2598 0.1652 0.1823 -0.0387 -0.0213 -0.0148 97  LYS A O   
798  C CB  A LYS A 97  ? 0.2736 0.1897 0.2095 -0.0434 -0.0339 -0.0050 97  LYS A CB  
799  C CB  B LYS A 97  ? 0.2533 0.1698 0.1896 -0.0431 -0.0337 -0.0051 97  LYS A CB  
800  C CG  A LYS A 97  ? 0.3212 0.2347 0.2559 -0.0497 -0.0418 -0.0003 97  LYS A CG  
801  C CG  B LYS A 97  ? 0.2776 0.1946 0.2165 -0.0478 -0.0409 0.0002  97  LYS A CG  
802  C CD  A LYS A 97  ? 0.3618 0.2900 0.3060 -0.0508 -0.0487 0.0069  97  LYS A CD  
803  C CD  B LYS A 97  ? 0.2981 0.2314 0.2485 -0.0476 -0.0472 0.0074  97  LYS A CD  
804  C CE  A LYS A 97  ? 0.4069 0.3352 0.3536 -0.0564 -0.0565 0.0134  97  LYS A CE  
805  C CE  B LYS A 97  ? 0.3308 0.2666 0.2870 -0.0513 -0.0538 0.0139  97  LYS A CE  
806  N NZ  A LYS A 97  ? 0.4286 0.3624 0.3867 -0.0522 -0.0549 0.0151  97  LYS A NZ  
807  N NZ  B LYS A 97  ? 0.3407 0.2934 0.3103 -0.0497 -0.0582 0.0220  97  LYS A NZ  
808  N N   . THR A 98  ? 0.2547 0.1549 0.1848 -0.0317 -0.0110 -0.0174 98  THR A N   
809  C CA  . THR A 98  ? 0.2542 0.1576 0.1867 -0.0270 -0.0048 -0.0195 98  THR A CA  
810  C C   . THR A 98  ? 0.2842 0.1736 0.1997 -0.0305 -0.0026 -0.0232 98  THR A C   
811  O O   . THR A 98  ? 0.3148 0.1866 0.2165 -0.0332 0.0009  -0.0263 98  THR A O   
812  C CB  . THR A 98  ? 0.2523 0.1549 0.1925 -0.0210 0.0037  -0.0202 98  THR A CB  
813  O OG1 . THR A 98  ? 0.2326 0.1476 0.1878 -0.0181 0.0015  -0.0166 98  THR A OG1 
814  C CG2 . THR A 98  ? 0.2558 0.1638 0.2009 -0.0164 0.0090  -0.0207 98  THR A CG2 
815  N N   . PRO A 99  ? 0.2825 0.1788 0.1980 -0.0308 -0.0048 -0.0229 99  PRO A N   
816  C CA  . PRO A 99  ? 0.2921 0.1759 0.1916 -0.0340 -0.0026 -0.0262 99  PRO A CA  
817  C C   . PRO A 99  ? 0.3000 0.1796 0.2001 -0.0284 0.0075  -0.0286 99  PRO A C   
818  O O   . PRO A 99  ? 0.2949 0.1834 0.2093 -0.0225 0.0117  -0.0271 99  PRO A O   
819  C CB  . PRO A 99  ? 0.2916 0.1876 0.1950 -0.0354 -0.0086 -0.0239 99  PRO A CB  
820  C CG  . PRO A 99  ? 0.2906 0.2044 0.2130 -0.0291 -0.0083 -0.0211 99  PRO A CG  
821  C CD  . PRO A 99  ? 0.2660 0.1807 0.1953 -0.0276 -0.0083 -0.0197 99  PRO A CD  
822  N N   . LYS A 100 ? 0.3110 0.1775 0.1960 -0.0303 0.0116  -0.0318 100 LYS A N   
823  C CA  . LYS A 100 ? 0.3088 0.1736 0.1961 -0.0246 0.0211  -0.0328 100 LYS A CA  
824  C C   . LYS A 100 ? 0.2847 0.1688 0.1873 -0.0214 0.0182  -0.0300 100 LYS A C   
825  O O   . LYS A 100 ? 0.2856 0.1769 0.1878 -0.0249 0.0106  -0.0290 100 LYS A O   
826  C CB  . LYS A 100 ? 0.3518 0.2000 0.2196 -0.0274 0.0254  -0.0363 100 LYS A CB  
827  C CG  . LYS A 100 ? 0.4294 0.2549 0.2793 -0.0297 0.0305  -0.0396 100 LYS A CG  
828  C CD  . LYS A 100 ? 0.5093 0.3170 0.3371 -0.0332 0.0340  -0.0431 100 LYS A CD  
829  C CE  . LYS A 100 ? 0.5777 0.3601 0.3843 -0.0365 0.0383  -0.0468 100 LYS A CE  
830  N NZ  . LYS A 100 ? 0.6311 0.3946 0.4134 -0.0404 0.0413  -0.0503 100 LYS A NZ  
831  N N   . TYR A 101 ? 0.2722 0.1649 0.1891 -0.0152 0.0233  -0.0279 101 TYR A N   
832  C CA  . TYR A 101 ? 0.2629 0.1725 0.1935 -0.0127 0.0198  -0.0252 101 TYR A CA  
833  C C   . TYR A 101 ? 0.2697 0.1834 0.2099 -0.0073 0.0267  -0.0232 101 TYR A C   
834  O O   . TYR A 101 ? 0.2816 0.1879 0.2224 -0.0042 0.0348  -0.0229 101 TYR A O   
835  C CB  . TYR A 101 ? 0.2444 0.1674 0.1873 -0.0121 0.0131  -0.0225 101 TYR A CB  
836  C CG  . TYR A 101 ? 0.2390 0.1652 0.1934 -0.0080 0.0170  -0.0204 101 TYR A CG  
837  C CD1 . TYR A 101 ? 0.2457 0.1632 0.1967 -0.0088 0.0191  -0.0212 101 TYR A CD1 
838  C CD2 . TYR A 101 ? 0.2376 0.1754 0.2064 -0.0037 0.0181  -0.0172 101 TYR A CD2 
839  C CE1 . TYR A 101 ? 0.2546 0.1755 0.2170 -0.0049 0.0228  -0.0188 101 TYR A CE1 
840  C CE2 . TYR A 101 ? 0.2398 0.1813 0.2199 -0.0003 0.0212  -0.0144 101 TYR A CE2 
841  C CZ  . TYR A 101 ? 0.2577 0.1913 0.2351 -0.0008 0.0236  -0.0152 101 TYR A CZ  
842  O OH  . TYR A 101 ? 0.2740 0.2112 0.2629 0.0025  0.0269  -0.0122 101 TYR A OH  
843  N N   . LYS A 102 ? 0.2583 0.1839 0.2065 -0.0062 0.0232  -0.0213 102 LYS A N   
844  C CA  . LYS A 102 ? 0.2549 0.1875 0.2147 -0.0018 0.0273  -0.0181 102 LYS A CA  
845  C C   . LYS A 102 ? 0.2427 0.1902 0.2135 -0.0015 0.0200  -0.0157 102 LYS A C   
846  O O   . LYS A 102 ? 0.2472 0.1982 0.2143 -0.0044 0.0132  -0.0169 102 LYS A O   
847  C CB  . LYS A 102 ? 0.2879 0.2152 0.2405 -0.0019 0.0314  -0.0190 102 LYS A CB  
848  C CG  . LYS A 102 ? 0.3730 0.2843 0.3144 -0.0009 0.0408  -0.0209 102 LYS A CG  
849  C CD  . LYS A 102 ? 0.4398 0.3464 0.3730 -0.0013 0.0439  -0.0217 102 LYS A CD  
850  C CE  . LYS A 102 ? 0.5043 0.3923 0.4223 -0.0008 0.0534  -0.0241 102 LYS A CE  
851  N NZ  . LYS A 102 ? 0.5466 0.4297 0.4550 -0.0015 0.0561  -0.0250 102 LYS A NZ  
852  N N   . PHE A 103 ? 0.2279 0.1836 0.2119 0.0018  0.0214  -0.0118 103 PHE A N   
853  C CA  . PHE A 103 ? 0.2188 0.1863 0.2111 0.0019  0.0147  -0.0095 103 PHE A CA  
854  C C   . PHE A 103 ? 0.2271 0.1966 0.2214 0.0025  0.0161  -0.0080 103 PHE A C   
855  O O   . PHE A 103 ? 0.2426 0.2103 0.2420 0.0050  0.0225  -0.0052 103 PHE A O   
856  C CB  . PHE A 103 ? 0.2052 0.1803 0.2106 0.0041  0.0140  -0.0053 103 PHE A CB  
857  C CG  . PHE A 103 ? 0.1993 0.1748 0.2051 0.0038  0.0119  -0.0060 103 PHE A CG  
858  C CD1 . PHE A 103 ? 0.2018 0.1733 0.1978 0.0012  0.0087  -0.0095 103 PHE A CD1 
859  C CD2 . PHE A 103 ? 0.1970 0.1780 0.2139 0.0057  0.0123  -0.0022 103 PHE A CD2 
860  C CE1 . PHE A 103 ? 0.2043 0.1770 0.2018 0.0010  0.0065  -0.0093 103 PHE A CE1 
861  C CE2 . PHE A 103 ? 0.1998 0.1817 0.2174 0.0055  0.0102  -0.0025 103 PHE A CE2 
862  C CZ  . PHE A 103 ? 0.2000 0.1780 0.2082 0.0033  0.0073  -0.0060 103 PHE A CZ  
863  N N   . VAL A 104 ? 0.2197 0.1924 0.2100 0.0005  0.0107  -0.0093 104 VAL A N   
864  C CA  . VAL A 104 ? 0.2324 0.2076 0.2249 0.0008  0.0110  -0.0077 104 VAL A CA  
865  C C   . VAL A 104 ? 0.2271 0.2109 0.2250 0.0002  0.0039  -0.0060 104 VAL A C   
866  O O   . VAL A 104 ? 0.2392 0.2249 0.2341 -0.0010 -0.0012 -0.0076 104 VAL A O   
867  C CB  . VAL A 104 ? 0.2641 0.2325 0.2449 -0.0012 0.0127  -0.0110 104 VAL A CB  
868  C CG1 . VAL A 104 ? 0.2834 0.2403 0.2554 -0.0011 0.0197  -0.0131 104 VAL A CG1 
869  C CG2 . VAL A 104 ? 0.2852 0.2550 0.2590 -0.0044 0.0060  -0.0136 104 VAL A CG2 
870  N N   . ARG A 105 ? 0.2023 0.1904 0.2078 0.0010  0.0037  -0.0024 105 ARG A N   
871  C CA  . ARG A 105 ? 0.1946 0.1886 0.2031 -0.0001 -0.0031 -0.0009 105 ARG A CA  
872  C C   . ARG A 105 ? 0.2048 0.1975 0.2081 -0.0013 -0.0037 -0.0024 105 ARG A C   
873  O O   . ARG A 105 ? 0.2089 0.2009 0.2150 -0.0006 0.0004  -0.0004 105 ARG A O   
874  C CB  . ARG A 105 ? 0.1910 0.1905 0.2118 0.0007  -0.0042 0.0050  105 ARG A CB  
875  C CG  . ARG A 105 ? 0.1958 0.1989 0.2171 -0.0012 -0.0119 0.0062  105 ARG A CG  
876  C CD  . ARG A 105 ? 0.1972 0.2054 0.2298 -0.0016 -0.0147 0.0126  105 ARG A CD  
877  N NE  . ARG A 105 ? 0.1998 0.2089 0.2299 -0.0042 -0.0226 0.0133  105 ARG A NE  
878  C CZ  . ARG A 105 ? 0.2140 0.2221 0.2387 -0.0051 -0.0276 0.0117  105 ARG A CZ  
879  N NH1 . ARG A 105 ? 0.1863 0.1938 0.2090 -0.0038 -0.0257 0.0096  105 ARG A NH1 
880  N NH2 . ARG A 105 ? 0.2021 0.2088 0.2227 -0.0074 -0.0342 0.0122  105 ARG A NH2 
881  N N   . ILE A 106 ? 0.2107 0.2033 0.2069 -0.0030 -0.0083 -0.0053 106 ILE A N   
882  C CA  . ILE A 106 ? 0.2279 0.2195 0.2192 -0.0043 -0.0089 -0.0066 106 ILE A CA  
883  C C   . ILE A 106 ? 0.2356 0.2311 0.2318 -0.0047 -0.0128 -0.0040 106 ILE A C   
884  O O   . ILE A 106 ? 0.2320 0.2302 0.2331 -0.0046 -0.0166 -0.0018 106 ILE A O   
885  C CB  . ILE A 106 ? 0.2423 0.2319 0.2246 -0.0060 -0.0113 -0.0099 106 ILE A CB  
886  C CG1 . ILE A 106 ? 0.2423 0.2345 0.2247 -0.0057 -0.0162 -0.0099 106 ILE A CG1 
887  C CG2 . ILE A 106 ? 0.2585 0.2427 0.2345 -0.0068 -0.0076 -0.0122 106 ILE A CG2 
888  C CD1 . ILE A 106 ? 0.2607 0.2523 0.2368 -0.0069 -0.0185 -0.0114 106 ILE A CD1 
889  N N   . GLN A 107 ? 0.2470 0.2421 0.2414 -0.0055 -0.0122 -0.0041 107 GLN A N   
890  C CA  . GLN A 107 ? 0.2511 0.2492 0.2493 -0.0062 -0.0161 -0.0018 107 GLN A CA  
891  C C   . GLN A 107 ? 0.2377 0.2349 0.2291 -0.0075 -0.0206 -0.0044 107 GLN A C   
892  O O   . GLN A 107 ? 0.2268 0.2221 0.2116 -0.0080 -0.0196 -0.0072 107 GLN A O   
893  C CB  . GLN A 107 ? 0.2947 0.2930 0.2949 -0.0061 -0.0123 -0.0001 107 GLN A CB  
894  C CG  . GLN A 107 ? 0.3689 0.3673 0.3760 -0.0041 -0.0061 0.0033  107 GLN A CG  
895  C CD  . GLN A 107 ? 0.4527 0.4559 0.4716 -0.0036 -0.0086 0.0088  107 GLN A CD  
896  O OE1 . GLN A 107 ? 0.4809 0.4869 0.5026 -0.0053 -0.0152 0.0106  107 GLN A OE1 
897  N NE2 . GLN A 107 ? 0.4710 0.4747 0.4969 -0.0014 -0.0034 0.0122  107 GLN A NE2 
898  N N   . PRO A 108 ? 0.2328 0.2308 0.2256 -0.0082 -0.0254 -0.0030 108 PRO A N   
899  C CA  . PRO A 108 ? 0.2328 0.2291 0.2193 -0.0088 -0.0285 -0.0051 108 PRO A CA  
900  C C   . PRO A 108 ? 0.2246 0.2212 0.2084 -0.0096 -0.0261 -0.0061 108 PRO A C   
901  O O   . PRO A 108 ? 0.2289 0.2269 0.2161 -0.0099 -0.0235 -0.0046 108 PRO A O   
902  C CB  . PRO A 108 ? 0.2553 0.2507 0.2435 -0.0098 -0.0334 -0.0030 108 PRO A CB  
903  C CG  . PRO A 108 ? 0.2711 0.2697 0.2685 -0.0102 -0.0330 0.0010  108 PRO A CG  
904  C CD  . PRO A 108 ? 0.2406 0.2406 0.2409 -0.0088 -0.0284 0.0011  108 PRO A CD  
905  N N   . GLY A 109 ? 0.2113 0.2069 0.1895 -0.0099 -0.0266 -0.0079 109 GLY A N   
906  C CA  . GLY A 109 ? 0.2149 0.2110 0.1901 -0.0113 -0.0251 -0.0083 109 GLY A CA  
907  C C   . GLY A 109 ? 0.2262 0.2210 0.1971 -0.0123 -0.0223 -0.0097 109 GLY A C   
908  O O   . GLY A 109 ? 0.2460 0.2407 0.2128 -0.0141 -0.0223 -0.0099 109 GLY A O   
909  N N   A GLN A 110 ? 0.2239 0.2173 0.1955 -0.0114 -0.0202 -0.0104 110 GLN A N   
910  N N   B GLN A 110 ? 0.2164 0.2097 0.1880 -0.0114 -0.0201 -0.0104 110 GLN A N   
911  C CA  A GLN A 110 ? 0.2291 0.2196 0.1955 -0.0126 -0.0179 -0.0118 110 GLN A CA  
912  C CA  B GLN A 110 ? 0.2150 0.2054 0.1816 -0.0125 -0.0177 -0.0118 110 GLN A CA  
913  C C   A GLN A 110 ? 0.2190 0.2100 0.1832 -0.0129 -0.0203 -0.0120 110 GLN A C   
914  C C   B GLN A 110 ? 0.2140 0.2049 0.1782 -0.0129 -0.0202 -0.0120 110 GLN A C   
915  O O   A GLN A 110 ? 0.2176 0.2103 0.1844 -0.0110 -0.0224 -0.0114 110 GLN A O   
916  O O   B GLN A 110 ? 0.2136 0.2063 0.1806 -0.0110 -0.0223 -0.0114 110 GLN A O   
917  C CB  A GLN A 110 ? 0.2570 0.2450 0.2251 -0.0114 -0.0138 -0.0121 110 GLN A CB  
918  C CB  B GLN A 110 ? 0.2230 0.2113 0.1920 -0.0111 -0.0139 -0.0120 110 GLN A CB  
919  C CG  A GLN A 110 ? 0.3110 0.2983 0.2815 -0.0108 -0.0101 -0.0110 110 GLN A CG  
920  C CG  B GLN A 110 ? 0.2436 0.2268 0.2063 -0.0123 -0.0112 -0.0138 110 GLN A CG  
921  C CD  A GLN A 110 ? 0.4009 0.3852 0.3643 -0.0131 -0.0084 -0.0118 110 GLN A CD  
922  C CD  B GLN A 110 ? 0.2659 0.2445 0.2201 -0.0152 -0.0094 -0.0149 110 GLN A CD  
923  O OE1 A GLN A 110 ? 0.4405 0.4194 0.3954 -0.0150 -0.0065 -0.0137 110 GLN A OE1 
924  O OE1 B GLN A 110 ? 0.2822 0.2600 0.2362 -0.0150 -0.0068 -0.0144 110 GLN A OE1 
925  N NE2 A GLN A 110 ? 0.4069 0.3944 0.3730 -0.0133 -0.0095 -0.0103 110 GLN A NE2 
926  N NE2 B GLN A 110 ? 0.2433 0.2187 0.1903 -0.0181 -0.0110 -0.0158 110 GLN A NE2 
927  N N   . THR A 111 ? 0.2128 0.2018 0.1715 -0.0155 -0.0202 -0.0122 111 THR A N   
928  C CA  . THR A 111 ? 0.2075 0.1977 0.1651 -0.0162 -0.0225 -0.0111 111 THR A CA  
929  C C   . THR A 111 ? 0.2020 0.1891 0.1577 -0.0166 -0.0214 -0.0120 111 THR A C   
930  O O   . THR A 111 ? 0.2183 0.2012 0.1718 -0.0169 -0.0183 -0.0138 111 THR A O   
931  C CB  . THR A 111 ? 0.2156 0.2063 0.1695 -0.0197 -0.0243 -0.0094 111 THR A CB  
932  O OG1 . THR A 111 ? 0.2302 0.2157 0.1773 -0.0229 -0.0226 -0.0109 111 THR A OG1 
933  C CG2 . THR A 111 ? 0.2132 0.2071 0.1698 -0.0190 -0.0254 -0.0081 111 THR A CG2 
934  N N   . PHE A 112 ? 0.1891 0.1782 0.1460 -0.0163 -0.0234 -0.0104 112 PHE A N   
935  C CA  . PHE A 112 ? 0.1846 0.1713 0.1403 -0.0170 -0.0231 -0.0107 112 PHE A CA  
936  C C   . PHE A 112 ? 0.1805 0.1706 0.1378 -0.0175 -0.0261 -0.0074 112 PHE A C   
937  O O   . PHE A 112 ? 0.1779 0.1722 0.1383 -0.0158 -0.0274 -0.0050 112 PHE A O   
938  C CB  . PHE A 112 ? 0.1862 0.1730 0.1462 -0.0136 -0.0210 -0.0121 112 PHE A CB  
939  C CG  . PHE A 112 ? 0.1824 0.1736 0.1476 -0.0101 -0.0224 -0.0109 112 PHE A CG  
940  C CD1 . PHE A 112 ? 0.1942 0.1864 0.1613 -0.0087 -0.0225 -0.0112 112 PHE A CD1 
941  C CD2 . PHE A 112 ? 0.1852 0.1784 0.1524 -0.0084 -0.0236 -0.0094 112 PHE A CD2 
942  C CE1 . PHE A 112 ? 0.2015 0.1953 0.1709 -0.0061 -0.0241 -0.0105 112 PHE A CE1 
943  C CE2 . PHE A 112 ? 0.1897 0.1848 0.1592 -0.0052 -0.0244 -0.0086 112 PHE A CE2 
944  C CZ  . PHE A 112 ? 0.1967 0.1914 0.1664 -0.0043 -0.0248 -0.0094 112 PHE A CZ  
945  N N   . SER A 113 ? 0.1742 0.1622 0.1298 -0.0194 -0.0268 -0.0068 113 SER A N   
946  C CA  . SER A 113 ? 0.1744 0.1662 0.1331 -0.0198 -0.0296 -0.0025 113 SER A CA  
947  C C   . SER A 113 ? 0.1779 0.1720 0.1416 -0.0156 -0.0286 -0.0023 113 SER A C   
948  O O   . SER A 113 ? 0.1868 0.1781 0.1502 -0.0147 -0.0266 -0.0053 113 SER A O   
949  C CB  . SER A 113 ? 0.1853 0.1730 0.1390 -0.0252 -0.0320 -0.0012 113 SER A CB  
950  O OG  . SER A 113 ? 0.2038 0.1885 0.1513 -0.0296 -0.0333 -0.0013 113 SER A OG  
951  N N   . VAL A 114 ? 0.1666 0.1656 0.1348 -0.0132 -0.0296 0.0016  114 VAL A N   
952  C CA  . VAL A 114 ? 0.1711 0.1722 0.1433 -0.0093 -0.0287 0.0025  114 VAL A CA  
953  C C   . VAL A 114 ? 0.1720 0.1758 0.1472 -0.0107 -0.0308 0.0073  114 VAL A C   
954  O O   . VAL A 114 ? 0.1727 0.1794 0.1497 -0.0122 -0.0325 0.0121  114 VAL A O   
955  C CB  . VAL A 114 ? 0.1719 0.1753 0.1458 -0.0046 -0.0275 0.0034  114 VAL A CB  
956  C CG1 . VAL A 114 ? 0.1736 0.1787 0.1503 -0.0006 -0.0266 0.0052  114 VAL A CG1 
957  C CG2 . VAL A 114 ? 0.1813 0.1819 0.1527 -0.0037 -0.0264 -0.0007 114 VAL A CG2 
958  N N   . LEU A 115 ? 0.1646 0.1679 0.1415 -0.0102 -0.0306 0.0070  115 LEU A N   
959  C CA  . LEU A 115 ? 0.1630 0.1694 0.1439 -0.0111 -0.0327 0.0122  115 LEU A CA  
960  C C   . LEU A 115 ? 0.1635 0.1741 0.1492 -0.0051 -0.0306 0.0143  115 LEU A C   
961  O O   . LEU A 115 ? 0.1683 0.1779 0.1546 -0.0029 -0.0292 0.0116  115 LEU A O   
962  C CB  . LEU A 115 ? 0.1697 0.1718 0.1487 -0.0147 -0.0340 0.0106  115 LEU A CB  
963  C CG  . LEU A 115 ? 0.1872 0.1925 0.1710 -0.0160 -0.0368 0.0165  115 LEU A CG  
964  C CD1 . LEU A 115 ? 0.1973 0.2049 0.1819 -0.0202 -0.0406 0.0224  115 LEU A CD1 
965  C CD2 . LEU A 115 ? 0.1923 0.1921 0.1735 -0.0192 -0.0377 0.0142  115 LEU A CD2 
966  N N   A ALA A 116 ? 0.1576 0.1721 0.1462 -0.0022 -0.0299 0.0190  116 ALA A N   
967  N N   B ALA A 116 ? 0.1632 0.1778 0.1520 -0.0024 -0.0300 0.0193  116 ALA A N   
968  C CA  A ALA A 116 ? 0.1643 0.1809 0.1552 0.0039  -0.0271 0.0210  116 ALA A CA  
969  C CA  B ALA A 116 ? 0.1766 0.1938 0.1682 0.0036  -0.0274 0.0220  116 ALA A CA  
970  C C   A ALA A 116 ? 0.1638 0.1840 0.1603 0.0043  -0.0280 0.0257  116 ALA A C   
971  C C   B ALA A 116 ? 0.1808 0.2010 0.1775 0.0037  -0.0283 0.0256  116 ALA A C   
972  O O   A ALA A 116 ? 0.1640 0.1877 0.1651 0.0017  -0.0302 0.0314  116 ALA A O   
973  O O   B ALA A 116 ? 0.1837 0.2061 0.1839 -0.0002 -0.0313 0.0298  116 ALA A O   
974  C CB  A ALA A 116 ? 0.1721 0.1901 0.1635 0.0074  -0.0249 0.0250  116 ALA A CB  
975  C CB  B ALA A 116 ? 0.1826 0.2025 0.1765 0.0062  -0.0258 0.0276  116 ALA A CB  
976  N N   A CYS A 117 ? 0.1629 0.1828 0.1597 0.0071  -0.0266 0.0237  117 CYS A N   
977  N N   B CYS A 117 ? 0.1817 0.2018 0.1786 0.0076  -0.0264 0.0241  117 CYS A N   
978  C CA  A CYS A 117 ? 0.1670 0.1905 0.1694 0.0080  -0.0272 0.0278  117 CYS A CA  
979  C CA  B CYS A 117 ? 0.1867 0.2097 0.1886 0.0078  -0.0272 0.0270  117 CYS A CA  
980  C C   A CYS A 117 ? 0.1750 0.2001 0.1782 0.0142  -0.0240 0.0300  117 CYS A C   
981  C C   B CYS A 117 ? 0.1857 0.2107 0.1888 0.0141  -0.0240 0.0295  117 CYS A C   
982  O O   A CYS A 117 ? 0.1758 0.1973 0.1732 0.0170  -0.0218 0.0262  117 CYS A O   
983  O O   B CYS A 117 ? 0.1897 0.2112 0.1872 0.0170  -0.0219 0.0258  117 CYS A O   
984  C CB  A CYS A 117 ? 0.1751 0.1960 0.1771 0.0049  -0.0287 0.0233  117 CYS A CB  
985  C CB  B CYS A 117 ? 0.2039 0.2234 0.2040 0.0047  -0.0284 0.0214  117 CYS A CB  
986  S SG  A CYS A 117 ? 0.1800 0.1960 0.1782 -0.0024 -0.0317 0.0203  117 CYS A SG  
987  S SG  B CYS A 117 ? 0.2509 0.2722 0.2567 0.0020  -0.0309 0.0245  117 CYS A SG  
988  N N   . TYR A 118 ? 0.1791 0.2090 0.1887 0.0158  -0.0239 0.0360  118 TYR A N   
989  C CA  . TYR A 118 ? 0.1964 0.2278 0.2067 0.0219  -0.0205 0.0388  118 TYR A CA  
990  C C   . TYR A 118 ? 0.2126 0.2481 0.2297 0.0210  -0.0223 0.0416  118 TYR A C   
991  O O   . TYR A 118 ? 0.2115 0.2504 0.2348 0.0173  -0.0253 0.0459  118 TYR A O   
992  C CB  . TYR A 118 ? 0.2023 0.2361 0.2148 0.0267  -0.0169 0.0462  118 TYR A CB  
993  C CG  . TYR A 118 ? 0.2149 0.2438 0.2205 0.0279  -0.0148 0.0434  118 TYR A CG  
994  C CD1 . TYR A 118 ? 0.2294 0.2518 0.2255 0.0318  -0.0117 0.0390  118 TYR A CD1 
995  C CD2 . TYR A 118 ? 0.2263 0.2562 0.2337 0.0240  -0.0169 0.0444  118 TYR A CD2 
996  C CE1 . TYR A 118 ? 0.2428 0.2598 0.2321 0.0323  -0.0102 0.0360  118 TYR A CE1 
997  C CE2 . TYR A 118 ? 0.2393 0.2647 0.2406 0.0246  -0.0153 0.0412  118 TYR A CE2 
998  C CZ  . TYR A 118 ? 0.2523 0.2712 0.2448 0.0289  -0.0119 0.0371  118 TYR A CZ  
999  O OH  . TYR A 118 ? 0.2759 0.2898 0.2623 0.0292  -0.0107 0.0342  118 TYR A OH  
1000 N N   . ASN A 119 ? 0.2222 0.2571 0.2379 0.0235  -0.0211 0.0393  119 ASN A N   
1001 C CA  . ASN A 119 ? 0.2341 0.2729 0.2567 0.0229  -0.0226 0.0418  119 ASN A CA  
1002 C C   . ASN A 119 ? 0.2266 0.2644 0.2519 0.0164  -0.0266 0.0395  119 ASN A C   
1003 O O   . ASN A 119 ? 0.2314 0.2726 0.2635 0.0144  -0.0290 0.0439  119 ASN A O   
1004 C CB  . ASN A 119 ? 0.2617 0.3068 0.2918 0.0263  -0.0213 0.0512  119 ASN A CB  
1005 C CG  . ASN A 119 ? 0.3308 0.3751 0.3568 0.0333  -0.0160 0.0538  119 ASN A CG  
1006 O OD1 . ASN A 119 ? 0.3668 0.4120 0.3934 0.0362  -0.0133 0.0588  119 ASN A OD1 
1007 N ND2 . ASN A 119 ? 0.3485 0.3905 0.3698 0.0362  -0.0143 0.0508  119 ASN A ND2 
1008 N N   . GLY A 120 ? 0.2131 0.2457 0.2328 0.0131  -0.0274 0.0329  120 GLY A N   
1009 C CA  . GLY A 120 ? 0.2116 0.2406 0.2310 0.0073  -0.0301 0.0300  120 GLY A CA  
1010 C C   . GLY A 120 ? 0.2124 0.2411 0.2323 0.0027  -0.0334 0.0335  120 GLY A C   
1011 O O   . GLY A 120 ? 0.2158 0.2400 0.2337 -0.0027 -0.0360 0.0316  120 GLY A O   
1012 N N   . SER A 121 ? 0.2081 0.2410 0.2303 0.0045  -0.0332 0.0393  121 SER A N   
1013 C CA  . SER A 121 ? 0.2219 0.2559 0.2461 -0.0002 -0.0369 0.0444  121 SER A CA  
1014 C C   . SER A 121 ? 0.2273 0.2595 0.2467 -0.0010 -0.0363 0.0428  121 SER A C   
1015 O O   . SER A 121 ? 0.2210 0.2548 0.2397 0.0040  -0.0327 0.0432  121 SER A O   
1016 C CB  . SER A 121 ? 0.2465 0.2885 0.2805 0.0022  -0.0374 0.0548  121 SER A CB  
1017 O OG  . SER A 121 ? 0.2958 0.3397 0.3349 0.0018  -0.0389 0.0568  121 SER A OG  
1018 N N   . PRO A 122 ? 0.2413 0.2691 0.2563 -0.0075 -0.0399 0.0411  122 PRO A N   
1019 C CA  . PRO A 122 ? 0.2456 0.2719 0.2562 -0.0087 -0.0395 0.0397  122 PRO A CA  
1020 C C   . PRO A 122 ? 0.2367 0.2697 0.2538 -0.0069 -0.0395 0.0485  122 PRO A C   
1021 O O   . PRO A 122 ? 0.2354 0.2734 0.2600 -0.0088 -0.0424 0.0570  122 PRO A O   
1022 C CB  . PRO A 122 ? 0.2727 0.2920 0.2764 -0.0165 -0.0436 0.0364  122 PRO A CB  
1023 C CG  . PRO A 122 ? 0.2849 0.2995 0.2868 -0.0178 -0.0438 0.0324  122 PRO A CG  
1024 C CD  . PRO A 122 ? 0.2534 0.2757 0.2652 -0.0142 -0.0439 0.0393  122 PRO A CD  
1025 N N   . SER A 123 ? 0.2282 0.2613 0.2432 -0.0032 -0.0360 0.0472  123 SER A N   
1026 C CA  . SER A 123 ? 0.2331 0.2718 0.2542 -0.0008 -0.0348 0.0555  123 SER A CA  
1027 C C   . SER A 123 ? 0.2247 0.2623 0.2433 -0.0052 -0.0369 0.0555  123 SER A C   
1028 O O   . SER A 123 ? 0.2283 0.2711 0.2537 -0.0068 -0.0386 0.0643  123 SER A O   
1029 C CB  . SER A 123 ? 0.2721 0.3113 0.2931 0.0077  -0.0283 0.0556  123 SER A CB  
1030 O OG  . SER A 123 ? 0.3356 0.3686 0.3475 0.0089  -0.0263 0.0467  123 SER A OG  
1031 N N   . GLY A 124 ? 0.2063 0.2377 0.2159 -0.0069 -0.0366 0.0466  124 GLY A N   
1032 C CA  . GLY A 124 ? 0.2006 0.2308 0.2073 -0.0109 -0.0383 0.0464  124 GLY A CA  
1033 C C   . GLY A 124 ? 0.1914 0.2145 0.1884 -0.0130 -0.0381 0.0366  124 GLY A C   
1034 O O   . GLY A 124 ? 0.1835 0.2030 0.1769 -0.0105 -0.0358 0.0302  124 GLY A O   
1035 N N   . VAL A 125 ? 0.1915 0.2130 0.1850 -0.0177 -0.0403 0.0362  125 VAL A N   
1036 C CA  . VAL A 125 ? 0.2046 0.2196 0.1894 -0.0198 -0.0398 0.0280  125 VAL A CA  
1037 C C   . VAL A 125 ? 0.2054 0.2216 0.1896 -0.0194 -0.0388 0.0283  125 VAL A C   
1038 O O   . VAL A 125 ? 0.2082 0.2289 0.1970 -0.0211 -0.0406 0.0352  125 VAL A O   
1039 C CB  . VAL A 125 ? 0.2389 0.2477 0.2169 -0.0270 -0.0434 0.0256  125 VAL A CB  
1040 C CG1 . VAL A 125 ? 0.2575 0.2676 0.2356 -0.0337 -0.0487 0.0322  125 VAL A CG1 
1041 C CG2 . VAL A 125 ? 0.2505 0.2520 0.2196 -0.0278 -0.0413 0.0171  125 VAL A CG2 
1042 N N   . TYR A 126 ? 0.2076 0.2204 0.1874 -0.0167 -0.0359 0.0217  126 TYR A N   
1043 C CA  . TYR A 126 ? 0.2073 0.2207 0.1864 -0.0161 -0.0349 0.0215  126 TYR A CA  
1044 C C   . TYR A 126 ? 0.2039 0.2122 0.1767 -0.0165 -0.0336 0.0139  126 TYR A C   
1045 O O   . TYR A 126 ? 0.2102 0.2149 0.1804 -0.0156 -0.0324 0.0092  126 TYR A O   
1046 C CB  . TYR A 126 ? 0.2086 0.2252 0.1926 -0.0098 -0.0316 0.0249  126 TYR A CB  
1047 C CG  . TYR A 126 ? 0.2180 0.2320 0.2004 -0.0043 -0.0285 0.0209  126 TYR A CG  
1048 C CD1 . TYR A 126 ? 0.2293 0.2390 0.2069 -0.0027 -0.0271 0.0147  126 TYR A CD1 
1049 C CD2 . TYR A 126 ? 0.2334 0.2491 0.2190 -0.0013 -0.0275 0.0237  126 TYR A CD2 
1050 C CE1 . TYR A 126 ? 0.2413 0.2482 0.2168 0.0014  -0.0252 0.0117  126 TYR A CE1 
1051 C CE2 . TYR A 126 ? 0.2452 0.2581 0.2283 0.0033  -0.0250 0.0202  126 TYR A CE2 
1052 C CZ  . TYR A 126 ? 0.2542 0.2625 0.2320 0.0043  -0.0241 0.0143  126 TYR A CZ  
1053 O OH  . TYR A 126 ? 0.2901 0.2953 0.2649 0.0080  -0.0226 0.0116  126 TYR A OH  
1054 N N   A GLN A 127 ? 0.2048 0.2129 0.1759 -0.0181 -0.0338 0.0136  127 GLN A N   
1055 N N   B GLN A 127 ? 0.2029 0.2111 0.1743 -0.0174 -0.0334 0.0134  127 GLN A N   
1056 C CA  A GLN A 127 ? 0.2100 0.2140 0.1761 -0.0189 -0.0326 0.0078  127 GLN A CA  
1057 C CA  B GLN A 127 ? 0.2088 0.2131 0.1755 -0.0177 -0.0321 0.0075  127 GLN A CA  
1058 C C   A GLN A 127 ? 0.2180 0.2225 0.1858 -0.0142 -0.0304 0.0061  127 GLN A C   
1059 C C   B GLN A 127 ? 0.2144 0.2186 0.1826 -0.0125 -0.0297 0.0055  127 GLN A C   
1060 O O   A GLN A 127 ? 0.2180 0.2252 0.1888 -0.0123 -0.0300 0.0097  127 GLN A O   
1061 O O   B GLN A 127 ? 0.2147 0.2211 0.1858 -0.0097 -0.0289 0.0088  127 GLN A O   
1062 C CB  A GLN A 127 ? 0.2189 0.2223 0.1814 -0.0245 -0.0349 0.0091  127 GLN A CB  
1063 C CB  B GLN A 127 ? 0.2260 0.2301 0.1899 -0.0223 -0.0338 0.0085  127 GLN A CB  
1064 C CG  A GLN A 127 ? 0.2441 0.2428 0.2006 -0.0261 -0.0336 0.0039  127 GLN A CG  
1065 C CG  B GLN A 127 ? 0.2569 0.2563 0.2152 -0.0236 -0.0324 0.0030  127 GLN A CG  
1066 C CD  A GLN A 127 ? 0.2576 0.2501 0.2085 -0.0274 -0.0323 -0.0004 127 GLN A CD  
1067 C CD  B GLN A 127 ? 0.2674 0.2610 0.2195 -0.0268 -0.0323 0.0000  127 GLN A CD  
1068 O OE1 A GLN A 127 ? 0.2529 0.2441 0.2039 -0.0277 -0.0329 0.0001  127 GLN A OE1 
1069 O OE1 B GLN A 127 ? 0.2729 0.2655 0.2250 -0.0275 -0.0333 0.0010  127 GLN A OE1 
1070 N NE2 A GLN A 127 ? 0.2689 0.2572 0.2154 -0.0278 -0.0299 -0.0043 127 GLN A NE2 
1071 N NE2 B GLN A 127 ? 0.2625 0.2514 0.2090 -0.0283 -0.0305 -0.0036 127 GLN A NE2 
1072 N N   A CYS A 128 ? 0.2195 0.2209 0.1853 -0.0124 -0.0288 0.0013  128 CYS A N   
1073 N N   B CYS A 128 ? 0.2191 0.2201 0.1851 -0.0114 -0.0285 0.0006  128 CYS A N   
1074 C CA  A CYS A 128 ? 0.2236 0.2241 0.1898 -0.0089 -0.0277 -0.0004 128 CYS A CA  
1075 C CA  B CYS A 128 ? 0.2279 0.2275 0.1941 -0.0078 -0.0273 -0.0016 128 CYS A CA  
1076 C C   A CYS A 128 ? 0.2259 0.2239 0.1904 -0.0099 -0.0272 -0.0044 128 CYS A C   
1077 C C   B CYS A 128 ? 0.2284 0.2260 0.1930 -0.0094 -0.0270 -0.0049 128 CYS A C   
1078 O O   A CYS A 128 ? 0.2252 0.2219 0.1876 -0.0130 -0.0269 -0.0057 128 CYS A O   
1079 O O   B CYS A 128 ? 0.2274 0.2236 0.1902 -0.0123 -0.0266 -0.0063 128 CYS A O   
1080 C CB  A CYS A 128 ? 0.2301 0.2299 0.1972 -0.0046 -0.0267 -0.0001 128 CYS A CB  
1081 C CB  B CYS A 128 ? 0.2450 0.2435 0.2118 -0.0049 -0.0266 -0.0027 128 CYS A CB  
1082 S SG  A CYS A 128 ? 0.2613 0.2596 0.2283 -0.0042 -0.0265 -0.0031 128 CYS A SG  
1083 S SG  B CYS A 128 ? 0.3024 0.3023 0.2705 -0.0008 -0.0258 0.0013  128 CYS A SG  
1084 N N   . ALA A 129 ? 0.2293 0.2258 0.1942 -0.0075 -0.0270 -0.0059 129 ALA A N   
1085 C CA  . ALA A 129 ? 0.2310 0.2263 0.1962 -0.0084 -0.0268 -0.0082 129 ALA A CA  
1086 C C   . ALA A 129 ? 0.2206 0.2142 0.1869 -0.0061 -0.0274 -0.0091 129 ALA A C   
1087 O O   . ALA A 129 ? 0.2327 0.2246 0.1972 -0.0039 -0.0283 -0.0085 129 ALA A O   
1088 C CB  . ALA A 129 ? 0.2348 0.2306 0.1999 -0.0096 -0.0273 -0.0076 129 ALA A CB  
1089 N N   . MET A 130 ? 0.2008 0.1942 0.1694 -0.0068 -0.0270 -0.0101 130 MET A N   
1090 C CA  . MET A 130 ? 0.1952 0.1873 0.1656 -0.0057 -0.0286 -0.0099 130 MET A CA  
1091 C C   . MET A 130 ? 0.2025 0.1933 0.1720 -0.0061 -0.0307 -0.0095 130 MET A C   
1092 O O   . MET A 130 ? 0.2061 0.1984 0.1776 -0.0075 -0.0301 -0.0092 130 MET A O   
1093 C CB  . MET A 130 ? 0.1989 0.1922 0.1742 -0.0063 -0.0271 -0.0096 130 MET A CB  
1094 C CG  . MET A 130 ? 0.2203 0.2135 0.1991 -0.0060 -0.0295 -0.0081 130 MET A CG  
1095 S SD  . MET A 130 ? 0.2278 0.2187 0.2031 -0.0045 -0.0322 -0.0081 130 MET A SD  
1096 C CE  . MET A 130 ? 0.2113 0.2043 0.1880 -0.0035 -0.0287 -0.0088 130 MET A CE  
1097 N N   . ARG A 131 ? 0.2015 0.1887 0.1670 -0.0048 -0.0327 -0.0094 131 ARG A N   
1098 C CA  . ARG A 131 ? 0.2027 0.1870 0.1662 -0.0053 -0.0347 -0.0091 131 ARG A CA  
1099 C C   . ARG A 131 ? 0.2077 0.1917 0.1747 -0.0072 -0.0374 -0.0082 131 ARG A C   
1100 O O   . ARG A 131 ? 0.2090 0.1938 0.1788 -0.0075 -0.0383 -0.0074 131 ARG A O   
1101 C CB  . ARG A 131 ? 0.2088 0.1867 0.1650 -0.0032 -0.0355 -0.0094 131 ARG A CB  
1102 C CG  . ARG A 131 ? 0.2152 0.1936 0.1693 -0.0008 -0.0325 -0.0088 131 ARG A CG  
1103 C CD  . ARG A 131 ? 0.2128 0.1956 0.1700 -0.0015 -0.0307 -0.0075 131 ARG A CD  
1104 N NE  . ARG A 131 ? 0.2100 0.1907 0.1667 -0.0024 -0.0319 -0.0075 131 ARG A NE  
1105 C CZ  . ARG A 131 ? 0.2081 0.1926 0.1680 -0.0038 -0.0312 -0.0063 131 ARG A CZ  
1106 N NH1 . ARG A 131 ? 0.1936 0.1834 0.1563 -0.0048 -0.0297 -0.0050 131 ARG A NH1 
1107 N NH2 . ARG A 131 ? 0.2013 0.1839 0.1611 -0.0045 -0.0325 -0.0061 131 ARG A NH2 
1108 N N   . PRO A 132 ? 0.2112 0.1942 0.1788 -0.0085 -0.0393 -0.0075 132 PRO A N   
1109 C CA  . PRO A 132 ? 0.2154 0.1985 0.1874 -0.0105 -0.0426 -0.0054 132 PRO A CA  
1110 C C   . PRO A 132 ? 0.2233 0.2010 0.1915 -0.0113 -0.0469 -0.0047 132 PRO A C   
1111 O O   . PRO A 132 ? 0.2373 0.2166 0.2109 -0.0134 -0.0498 -0.0019 132 PRO A O   
1112 C CB  . PRO A 132 ? 0.2262 0.2083 0.1981 -0.0116 -0.0440 -0.0048 132 PRO A CB  
1113 C CG  . PRO A 132 ? 0.2227 0.2079 0.1941 -0.0105 -0.0399 -0.0061 132 PRO A CG  
1114 C CD  . PRO A 132 ? 0.2092 0.1921 0.1752 -0.0084 -0.0383 -0.0077 132 PRO A CD  
1115 N N   . ASN A 133 ? 0.2123 0.1833 0.1710 -0.0098 -0.0473 -0.0067 133 ASN A N   
1116 C CA  . ASN A 133 ? 0.2134 0.1779 0.1661 -0.0109 -0.0513 -0.0062 133 ASN A CA  
1117 C C   . ASN A 133 ? 0.2127 0.1806 0.1674 -0.0096 -0.0496 -0.0062 133 ASN A C   
1118 O O   . ASN A 133 ? 0.2193 0.1818 0.1678 -0.0099 -0.0521 -0.0061 133 ASN A O   
1119 C CB  . ASN A 133 ? 0.2299 0.1833 0.1694 -0.0097 -0.0521 -0.0083 133 ASN A CB  
1120 C CG  . ASN A 133 ? 0.2370 0.1903 0.1728 -0.0056 -0.0467 -0.0100 133 ASN A CG  
1121 O OD1 . ASN A 133 ? 0.2231 0.1841 0.1651 -0.0041 -0.0433 -0.0099 133 ASN A OD1 
1122 N ND2 . ASN A 133 ? 0.2540 0.1978 0.1793 -0.0036 -0.0456 -0.0112 133 ASN A ND2 
1123 N N   . PHE A 134 ? 0.2034 0.1791 0.1657 -0.0083 -0.0454 -0.0063 134 PHE A N   
1124 C CA  . PHE A 134 ? 0.2103 0.1897 0.1760 -0.0072 -0.0434 -0.0060 134 PHE A CA  
1125 C C   . PHE A 134 ? 0.2120 0.1882 0.1706 -0.0047 -0.0419 -0.0077 134 PHE A C   
1126 O O   . PHE A 134 ? 0.2138 0.1918 0.1740 -0.0040 -0.0414 -0.0072 134 PHE A O   
1127 C CB  . PHE A 134 ? 0.2145 0.1952 0.1854 -0.0093 -0.0468 -0.0029 134 PHE A CB  
1128 C CG  . PHE A 134 ? 0.2344 0.2200 0.2151 -0.0112 -0.0470 0.0000  134 PHE A CG  
1129 C CD1 . PHE A 134 ? 0.2511 0.2428 0.2400 -0.0101 -0.0422 0.0008  134 PHE A CD1 
1130 C CD2 . PHE A 134 ? 0.2532 0.2365 0.2344 -0.0140 -0.0520 0.0026  134 PHE A CD2 
1131 C CE1 . PHE A 134 ? 0.2621 0.2578 0.2600 -0.0110 -0.0413 0.0042  134 PHE A CE1 
1132 C CE2 . PHE A 134 ? 0.2640 0.2525 0.2556 -0.0153 -0.0519 0.0064  134 PHE A CE2 
1133 C CZ  . PHE A 134 ? 0.2594 0.2543 0.2595 -0.0135 -0.0462 0.0073  134 PHE A CZ  
1134 N N   . THR A 135 ? 0.2087 0.1810 0.1607 -0.0029 -0.0404 -0.0091 135 THR A N   
1135 C CA  . THR A 135 ? 0.2126 0.1833 0.1598 0.0002  -0.0376 -0.0096 135 THR A CA  
1136 C C   . THR A 135 ? 0.2102 0.1872 0.1627 0.0010  -0.0340 -0.0095 135 THR A C   
1137 O O   . THR A 135 ? 0.2047 0.1852 0.1617 -0.0008 -0.0337 -0.0095 135 THR A O   
1138 C CB  . THR A 135 ? 0.2285 0.1900 0.1652 0.0020  -0.0376 -0.0102 135 THR A CB  
1139 O OG1 . THR A 135 ? 0.2442 0.2059 0.1817 0.0019  -0.0365 -0.0103 135 THR A OG1 
1140 C CG2 . THR A 135 ? 0.2325 0.1852 0.1610 0.0002  -0.0420 -0.0105 135 THR A CG2 
1141 N N   . ILE A 136 ? 0.2069 0.1849 0.1584 0.0034  -0.0314 -0.0087 136 ILE A N   
1142 C CA  . ILE A 136 ? 0.2138 0.1964 0.1688 0.0036  -0.0290 -0.0076 136 ILE A CA  
1143 C C   . ILE A 136 ? 0.2215 0.2012 0.1722 0.0069  -0.0267 -0.0057 136 ILE A C   
1144 O O   . ILE A 136 ? 0.2221 0.1966 0.1672 0.0095  -0.0262 -0.0057 136 ILE A O   
1145 C CB  . ILE A 136 ? 0.2269 0.2151 0.1873 0.0025  -0.0280 -0.0073 136 ILE A CB  
1146 C CG1 . ILE A 136 ? 0.2382 0.2265 0.1980 0.0048  -0.0272 -0.0061 136 ILE A CG1 
1147 C CG2 . ILE A 136 ? 0.2386 0.2284 0.2029 0.0000  -0.0288 -0.0088 136 ILE A CG2 
1148 C CD1 . ILE A 136 ? 0.2465 0.2396 0.2111 0.0037  -0.0262 -0.0052 136 ILE A CD1 
1149 N N   A LYS A 137 ? 0.2290 0.2116 0.1822 0.0070  -0.0251 -0.0036 137 LYS A N   
1150 N N   B LYS A 137 ? 0.2299 0.2126 0.1832 0.0069  -0.0252 -0.0037 137 LYS A N   
1151 C CA  A LYS A 137 ? 0.2450 0.2258 0.1963 0.0107  -0.0221 -0.0004 137 LYS A CA  
1152 C CA  B LYS A 137 ? 0.2468 0.2279 0.1985 0.0105  -0.0222 -0.0004 137 LYS A CA  
1153 C C   A LYS A 137 ? 0.2452 0.2327 0.2025 0.0107  -0.0210 0.0030  137 LYS A C   
1154 C C   B LYS A 137 ? 0.2455 0.2332 0.2030 0.0105  -0.0211 0.0029  137 LYS A C   
1155 O O   A LYS A 137 ? 0.2446 0.2372 0.2069 0.0083  -0.0214 0.0052  137 LYS A O   
1156 O O   B LYS A 137 ? 0.2441 0.2371 0.2066 0.0080  -0.0216 0.0050  137 LYS A O   
1157 C CB  A LYS A 137 ? 0.2776 0.2572 0.2288 0.0108  -0.0211 0.0009  137 LYS A CB  
1158 C CB  B LYS A 137 ? 0.2817 0.2627 0.2342 0.0101  -0.0214 0.0010  137 LYS A CB  
1159 C CG  A LYS A 137 ? 0.3396 0.3121 0.2850 0.0101  -0.0229 -0.0023 137 LYS A CG  
1160 C CG  B LYS A 137 ? 0.3499 0.3238 0.2966 0.0098  -0.0227 -0.0018 137 LYS A CG  
1161 C CD  A LYS A 137 ? 0.3939 0.3654 0.3399 0.0102  -0.0218 -0.0008 137 LYS A CD  
1162 C CD  B LYS A 137 ? 0.4039 0.3799 0.3538 0.0082  -0.0228 -0.0007 137 LYS A CD  
1163 C CE  A LYS A 137 ? 0.4429 0.4061 0.3822 0.0148  -0.0181 0.0008  137 LYS A CE  
1164 C CE  B LYS A 137 ? 0.4534 0.4206 0.3967 0.0098  -0.0225 -0.0017 137 LYS A CE  
1165 N NZ  A LYS A 137 ? 0.4766 0.4283 0.4051 0.0152  -0.0197 -0.0028 137 LYS A NZ  
1166 N NZ  B LYS A 137 ? 0.4711 0.4404 0.4176 0.0067  -0.0246 -0.0024 137 LYS A NZ  
1167 N N   . GLY A 138 ? 0.2446 0.2319 0.2013 0.0127  -0.0202 0.0035  138 GLY A N   
1168 C CA  . GLY A 138 ? 0.2460 0.2394 0.2086 0.0125  -0.0198 0.0070  138 GLY A CA  
1169 C C   . GLY A 138 ? 0.2391 0.2328 0.2027 0.0170  -0.0163 0.0123  138 GLY A C   
1170 O O   . GLY A 138 ? 0.2492 0.2386 0.2092 0.0205  -0.0133 0.0139  138 GLY A O   
1171 N N   . SER A 139 ? 0.2255 0.2242 0.1942 0.0172  -0.0163 0.0156  139 SER A N   
1172 C CA  . SER A 139 ? 0.2291 0.2292 0.2003 0.0218  -0.0127 0.0217  139 SER A CA  
1173 C C   . SER A 139 ? 0.2372 0.2384 0.2089 0.0226  -0.0132 0.0213  139 SER A C   
1174 O O   . SER A 139 ? 0.2391 0.2458 0.2167 0.0194  -0.0158 0.0224  139 SER A O   
1175 C CB  . SER A 139 ? 0.2409 0.2483 0.2211 0.0202  -0.0129 0.0287  139 SER A CB  
1176 O OG  . SER A 139 ? 0.2930 0.3033 0.2779 0.0245  -0.0096 0.0358  139 SER A OG  
1177 N N   . PHE A 140 ? 0.2317 0.2266 0.1959 0.0262  -0.0113 0.0188  140 PHE A N   
1178 C CA  . PHE A 140 ? 0.2400 0.2355 0.2040 0.0268  -0.0120 0.0179  140 PHE A CA  
1179 C C   . PHE A 140 ? 0.2721 0.2629 0.2306 0.0328  -0.0076 0.0206  140 PHE A C   
1180 O O   . PHE A 140 ? 0.2955 0.2774 0.2439 0.0353  -0.0056 0.0183  140 PHE A O   
1181 C CB  . PHE A 140 ? 0.2313 0.2232 0.1906 0.0238  -0.0153 0.0113  140 PHE A CB  
1182 C CG  . PHE A 140 ? 0.2256 0.2211 0.1894 0.0184  -0.0188 0.0083  140 PHE A CG  
1183 C CD1 . PHE A 140 ? 0.2344 0.2352 0.2047 0.0157  -0.0205 0.0088  140 PHE A CD1 
1184 C CD2 . PHE A 140 ? 0.2295 0.2219 0.1902 0.0162  -0.0202 0.0049  140 PHE A CD2 
1185 C CE1 . PHE A 140 ? 0.2311 0.2331 0.2036 0.0112  -0.0227 0.0059  140 PHE A CE1 
1186 C CE2 . PHE A 140 ? 0.2363 0.2312 0.2005 0.0118  -0.0225 0.0024  140 PHE A CE2 
1187 C CZ  . PHE A 140 ? 0.2268 0.2259 0.1962 0.0095  -0.0234 0.0027  140 PHE A CZ  
1188 N N   . LEU A 141 ? 0.2734 0.2692 0.2374 0.0351  -0.0061 0.0253  141 LEU A N   
1189 C CA  . LEU A 141 ? 0.2985 0.2898 0.2571 0.0412  -0.0013 0.0283  141 LEU A CA  
1190 C C   . LEU A 141 ? 0.3053 0.2961 0.2613 0.0405  -0.0035 0.0254  141 LEU A C   
1191 O O   . LEU A 141 ? 0.3014 0.2961 0.2616 0.0356  -0.0082 0.0219  141 LEU A O   
1192 C CB  . LEU A 141 ? 0.3101 0.3085 0.2785 0.0446  0.0022  0.0372  141 LEU A CB  
1193 C CG  . LEU A 141 ? 0.3488 0.3495 0.3224 0.0453  0.0044  0.0422  141 LEU A CG  
1194 C CD1 . LEU A 141 ? 0.3570 0.3675 0.3437 0.0466  0.0057  0.0518  141 LEU A CD1 
1195 C CD2 . LEU A 141 ? 0.3693 0.3596 0.3325 0.0508  0.0105  0.0421  141 LEU A CD2 
1196 N N   . ASN A 142 ? 0.3145 0.3005 0.2638 0.0455  0.0003  0.0273  142 ASN A N   
1197 C CA  . ASN A 142 ? 0.3191 0.3055 0.2668 0.0448  -0.0019 0.0255  142 ASN A CA  
1198 C C   . ASN A 142 ? 0.2914 0.2895 0.2533 0.0425  -0.0043 0.0287  142 ASN A C   
1199 O O   . ASN A 142 ? 0.2891 0.2935 0.2599 0.0439  -0.0025 0.0346  142 ASN A O   
1200 C CB  . ASN A 142 ? 0.3638 0.3423 0.3007 0.0507  0.0031  0.0276  142 ASN A CB  
1201 C CG  . ASN A 142 ? 0.4614 0.4256 0.3811 0.0514  0.0040  0.0230  142 ASN A CG  
1202 O OD1 . ASN A 142 ? 0.4930 0.4539 0.4085 0.0465  -0.0011 0.0174  142 ASN A OD1 
1203 N ND2 . ASN A 142 ? 0.4901 0.4448 0.3992 0.0576  0.0107  0.0256  142 ASN A ND2 
1204 N N   . GLY A 143 ? 0.2679 0.2684 0.2323 0.0383  -0.0087 0.0248  143 GLY A N   
1205 C CA  . GLY A 143 ? 0.2418 0.2512 0.2180 0.0354  -0.0114 0.0266  143 GLY A CA  
1206 C C   . GLY A 143 ? 0.2132 0.2251 0.1943 0.0298  -0.0149 0.0234  143 GLY A C   
1207 O O   . GLY A 143 ? 0.2026 0.2193 0.1911 0.0266  -0.0173 0.0235  143 GLY A O   
1208 N N   . SER A 144 ? 0.2005 0.2082 0.1767 0.0286  -0.0150 0.0207  144 SER A N   
1209 C CA  . SER A 144 ? 0.1811 0.1906 0.1609 0.0235  -0.0179 0.0178  144 SER A CA  
1210 C C   . SER A 144 ? 0.1726 0.1799 0.1508 0.0202  -0.0204 0.0123  144 SER A C   
1211 O O   . SER A 144 ? 0.1598 0.1682 0.1408 0.0163  -0.0220 0.0101  144 SER A O   
1212 C CB  . SER A 144 ? 0.1922 0.1992 0.1689 0.0234  -0.0170 0.0179  144 SER A CB  
1213 O OG  . SER A 144 ? 0.2250 0.2249 0.1925 0.0253  -0.0159 0.0147  144 SER A OG  
1214 N N   . CYS A 145 ? 0.1754 0.1797 0.1493 0.0216  -0.0206 0.0107  145 CYS A N   
1215 C CA  . CYS A 145 ? 0.1740 0.1774 0.1484 0.0185  -0.0230 0.0069  145 CYS A CA  
1216 C C   . CYS A 145 ? 0.1604 0.1686 0.1434 0.0158  -0.0237 0.0069  145 CYS A C   
1217 O O   . CYS A 145 ? 0.1619 0.1736 0.1494 0.0167  -0.0232 0.0096  145 CYS A O   
1218 C CB  . CYS A 145 ? 0.1941 0.1942 0.1633 0.0197  -0.0239 0.0066  145 CYS A CB  
1219 S SG  . CYS A 145 ? 0.2609 0.2515 0.2164 0.0219  -0.0233 0.0055  145 CYS A SG  
1220 N N   . GLY A 146 ? 0.1498 0.1572 0.1345 0.0128  -0.0246 0.0039  146 GLY A N   
1221 C CA  . GLY A 146 ? 0.1474 0.1568 0.1383 0.0104  -0.0244 0.0034  146 GLY A CA  
1222 C C   . GLY A 146 ? 0.1458 0.1546 0.1365 0.0080  -0.0242 0.0030  146 GLY A C   
1223 O O   . GLY A 146 ? 0.1578 0.1655 0.1507 0.0055  -0.0237 0.0017  146 GLY A O   
1224 N N   . SER A 147 ? 0.1431 0.1517 0.1305 0.0086  -0.0243 0.0043  147 SER A N   
1225 C CA  . SER A 147 ? 0.1443 0.1522 0.1310 0.0055  -0.0249 0.0043  147 SER A CA  
1226 C C   . SER A 147 ? 0.1516 0.1561 0.1359 0.0031  -0.0246 0.0002  147 SER A C   
1227 O O   . SER A 147 ? 0.1480 0.1514 0.1310 0.0044  -0.0243 -0.0015 147 SER A O   
1228 C CB  . SER A 147 ? 0.1573 0.1662 0.1420 0.0069  -0.0249 0.0071  147 SER A CB  
1229 O OG  . SER A 147 ? 0.1685 0.1807 0.1562 0.0096  -0.0244 0.0120  147 SER A OG  
1230 N N   . VAL A 148 ? 0.1463 0.1485 0.1295 -0.0004 -0.0246 -0.0010 148 VAL A N   
1231 C CA  . VAL A 148 ? 0.1560 0.1546 0.1370 -0.0022 -0.0233 -0.0044 148 VAL A CA  
1232 C C   . VAL A 148 ? 0.1614 0.1581 0.1381 -0.0047 -0.0239 -0.0051 148 VAL A C   
1233 O O   . VAL A 148 ? 0.1603 0.1578 0.1356 -0.0065 -0.0256 -0.0028 148 VAL A O   
1234 C CB  . VAL A 148 ? 0.1675 0.1627 0.1497 -0.0036 -0.0213 -0.0060 148 VAL A CB  
1235 C CG1 . VAL A 148 ? 0.1651 0.1630 0.1529 -0.0010 -0.0206 -0.0050 148 VAL A CG1 
1236 C CG2 . VAL A 148 ? 0.1812 0.1732 0.1603 -0.0071 -0.0223 -0.0055 148 VAL A CG2 
1237 N N   . GLY A 149 ? 0.1641 0.1587 0.1394 -0.0051 -0.0225 -0.0076 149 GLY A N   
1238 C CA  . GLY A 149 ? 0.1680 0.1602 0.1390 -0.0076 -0.0224 -0.0087 149 GLY A CA  
1239 C C   . GLY A 149 ? 0.1725 0.1592 0.1405 -0.0098 -0.0198 -0.0111 149 GLY A C   
1240 O O   . GLY A 149 ? 0.1692 0.1545 0.1400 -0.0084 -0.0172 -0.0121 149 GLY A O   
1241 N N   . PHE A 150 ? 0.1703 0.1533 0.1322 -0.0134 -0.0202 -0.0117 150 PHE A N   
1242 C CA  . PHE A 150 ? 0.1901 0.1652 0.1460 -0.0157 -0.0172 -0.0141 150 PHE A CA  
1243 C C   . PHE A 150 ? 0.2117 0.1828 0.1599 -0.0193 -0.0176 -0.0148 150 PHE A C   
1244 O O   . PHE A 150 ? 0.2039 0.1788 0.1519 -0.0209 -0.0211 -0.0128 150 PHE A O   
1245 C CB  . PHE A 150 ? 0.1951 0.1662 0.1486 -0.0177 -0.0178 -0.0138 150 PHE A CB  
1246 C CG  . PHE A 150 ? 0.2071 0.1797 0.1583 -0.0212 -0.0228 -0.0110 150 PHE A CG  
1247 C CD1 . PHE A 150 ? 0.2157 0.1963 0.1740 -0.0192 -0.0256 -0.0074 150 PHE A CD1 
1248 C CD2 . PHE A 150 ? 0.2264 0.1922 0.1683 -0.0267 -0.0246 -0.0111 150 PHE A CD2 
1249 C CE1 . PHE A 150 ? 0.2266 0.2097 0.1848 -0.0220 -0.0297 -0.0033 150 PHE A CE1 
1250 C CE2 . PHE A 150 ? 0.2366 0.2048 0.1780 -0.0305 -0.0299 -0.0070 150 PHE A CE2 
1251 C CZ  . PHE A 150 ? 0.2261 0.2036 0.1767 -0.0279 -0.0322 -0.0028 150 PHE A CZ  
1252 N N   . ASN A 151 ? 0.2234 0.1864 0.1650 -0.0206 -0.0137 -0.0174 151 ASN A N   
1253 C CA  . ASN A 151 ? 0.2490 0.2054 0.1802 -0.0247 -0.0136 -0.0185 151 ASN A CA  
1254 C C   . ASN A 151 ? 0.2759 0.2203 0.1967 -0.0277 -0.0115 -0.0205 151 ASN A C   
1255 O O   . ASN A 151 ? 0.2690 0.2107 0.1922 -0.0254 -0.0083 -0.0215 151 ASN A O   
1256 C CB  . ASN A 151 ? 0.2598 0.2158 0.1913 -0.0227 -0.0096 -0.0196 151 ASN A CB  
1257 C CG  . ASN A 151 ? 0.3002 0.2653 0.2385 -0.0214 -0.0125 -0.0177 151 ASN A CG  
1258 O OD1 . ASN A 151 ? 0.3333 0.2995 0.2679 -0.0243 -0.0154 -0.0168 151 ASN A OD1 
1259 N ND2 . ASN A 151 ? 0.2779 0.2494 0.2257 -0.0172 -0.0122 -0.0169 151 ASN A ND2 
1260 N N   . ILE A 152 ? 0.3027 0.2392 0.2112 -0.0333 -0.0133 -0.0211 152 ILE A N   
1261 C CA  . ILE A 152 ? 0.3469 0.2691 0.2424 -0.0368 -0.0114 -0.0235 152 ILE A CA  
1262 C C   . ILE A 152 ? 0.3883 0.2993 0.2701 -0.0391 -0.0075 -0.0260 152 ILE A C   
1263 O O   . ILE A 152 ? 0.3936 0.3075 0.2730 -0.0415 -0.0102 -0.0249 152 ILE A O   
1264 C CB  . ILE A 152 ? 0.3603 0.2802 0.2511 -0.0428 -0.0184 -0.0213 152 ILE A CB  
1265 C CG1 . ILE A 152 ? 0.3656 0.2977 0.2707 -0.0401 -0.0221 -0.0178 152 ILE A CG1 
1266 C CG2 . ILE A 152 ? 0.3794 0.2822 0.2552 -0.0466 -0.0163 -0.0242 152 ILE A CG2 
1267 C CD1 . ILE A 152 ? 0.3812 0.3132 0.2845 -0.0455 -0.0290 -0.0141 152 ILE A CD1 
1268 N N   . ASP A 153 ? 0.4161 0.3142 0.2891 -0.0379 -0.0005 -0.0292 153 ASP A N   
1269 C CA  . ASP A 153 ? 0.4501 0.3347 0.3071 -0.0400 0.0042  -0.0317 153 ASP A CA  
1270 C C   . ASP A 153 ? 0.4755 0.3426 0.3155 -0.0448 0.0044  -0.0342 153 ASP A C   
1271 O O   . ASP A 153 ? 0.4875 0.3468 0.3264 -0.0416 0.0105  -0.0360 153 ASP A O   
1272 C CB  . ASP A 153 ? 0.4891 0.3723 0.3503 -0.0332 0.0141  -0.0327 153 ASP A CB  
1273 C CG  . ASP A 153 ? 0.6021 0.4717 0.4468 -0.0348 0.0196  -0.0349 153 ASP A CG  
1274 O OD1 . ASP A 153 ? 0.6244 0.4920 0.4593 -0.0404 0.0145  -0.0348 153 ASP A OD1 
1275 O OD2 . ASP A 153 ? 0.6541 0.5147 0.4955 -0.0303 0.0293  -0.0361 153 ASP A OD2 
1276 N N   . TYR A 154 ? 0.4783 0.3395 0.3057 -0.0529 -0.0029 -0.0336 154 TYR A N   
1277 C CA  . TYR A 154 ? 0.4970 0.3411 0.3065 -0.0599 -0.0057 -0.0351 154 TYR A CA  
1278 C C   . TYR A 154 ? 0.4899 0.3367 0.3080 -0.0589 -0.0080 -0.0341 154 TYR A C   
1279 O O   . TYR A 154 ? 0.4925 0.3498 0.3191 -0.0620 -0.0165 -0.0302 154 TYR A O   
1280 C CB  . TYR A 154 ? 0.5145 0.3358 0.3015 -0.0610 0.0024  -0.0398 154 TYR A CB  
1281 C CG  . TYR A 154 ? 0.5418 0.3431 0.3083 -0.0686 -0.0009 -0.0418 154 TYR A CG  
1282 C CD1 . TYR A 154 ? 0.5593 0.3587 0.3171 -0.0784 -0.0120 -0.0392 154 TYR A CD1 
1283 C CD2 . TYR A 154 ? 0.5632 0.3475 0.3196 -0.0663 0.0070  -0.0455 154 TYR A CD2 
1284 C CE1 . TYR A 154 ? 0.5842 0.3648 0.3230 -0.0863 -0.0162 -0.0403 154 TYR A CE1 
1285 C CE2 . TYR A 154 ? 0.5893 0.3541 0.3262 -0.0736 0.0036  -0.0474 154 TYR A CE2 
1286 C CZ  . TYR A 154 ? 0.6066 0.3693 0.3342 -0.0840 -0.0084 -0.0449 154 TYR A CZ  
1287 O OH  . TYR A 154 ? 0.6433 0.3857 0.3507 -0.0922 -0.0128 -0.0463 154 TYR A OH  
1288 N N   . ASP A 155 ? 0.4819 0.3204 0.2992 -0.0543 -0.0001 -0.0370 155 ASP A N   
1289 C CA  . ASP A 155 ? 0.4692 0.3101 0.2947 -0.0533 -0.0020 -0.0360 155 ASP A CA  
1290 C C   . ASP A 155 ? 0.4375 0.2920 0.2834 -0.0445 0.0033  -0.0350 155 ASP A C   
1291 O O   . ASP A 155 ? 0.4396 0.2961 0.2927 -0.0429 0.0028  -0.0342 155 ASP A O   
1292 C CB  . ASP A 155 ? 0.5167 0.3350 0.3233 -0.0570 0.0010  -0.0394 155 ASP A CB  
1293 C CG  . ASP A 155 ? 0.5979 0.4010 0.3946 -0.0521 0.0136  -0.0436 155 ASP A CG  
1294 O OD1 . ASP A 155 ? 0.6029 0.4128 0.4064 -0.0465 0.0196  -0.0435 155 ASP A OD1 
1295 O OD2 . ASP A 155 ? 0.6460 0.4298 0.4281 -0.0537 0.0176  -0.0465 155 ASP A OD2 
1296 N N   . CYS A 156 ? 0.4061 0.2698 0.2611 -0.0390 0.0078  -0.0346 156 CYS A N   
1297 C CA  . CYS A 156 ? 0.3780 0.2540 0.2516 -0.0314 0.0122  -0.0330 156 CYS A CA  
1298 C C   . CYS A 156 ? 0.3346 0.2300 0.2241 -0.0297 0.0062  -0.0297 156 CYS A C   
1299 O O   . CYS A 156 ? 0.3294 0.2298 0.2191 -0.0301 0.0050  -0.0292 156 CYS A O   
1300 C CB  . CYS A 156 ? 0.3957 0.2659 0.2683 -0.0262 0.0226  -0.0343 156 CYS A CB  
1301 S SG  . CYS A 156 ? 0.4155 0.3003 0.3114 -0.0177 0.0276  -0.0310 156 CYS A SG  
1302 N N   . VAL A 157 ? 0.2993 0.2052 0.2021 -0.0273 0.0034  -0.0275 157 VAL A N   
1303 C CA  . VAL A 157 ? 0.2695 0.1921 0.1862 -0.0250 -0.0013 -0.0245 157 VAL A CA  
1304 C C   . VAL A 157 ? 0.2462 0.1761 0.1745 -0.0190 0.0035  -0.0237 157 VAL A C   
1305 O O   . VAL A 157 ? 0.2416 0.1712 0.1762 -0.0156 0.0077  -0.0233 157 VAL A O   
1306 C CB  . VAL A 157 ? 0.2674 0.1973 0.1918 -0.0254 -0.0067 -0.0219 157 VAL A CB  
1307 C CG1 . VAL A 157 ? 0.2624 0.2074 0.1989 -0.0227 -0.0108 -0.0189 157 VAL A CG1 
1308 C CG2 . VAL A 157 ? 0.2831 0.2058 0.1974 -0.0319 -0.0121 -0.0214 157 VAL A CG2 
1309 N N   . SER A 158 ? 0.2344 0.1714 0.1665 -0.0178 0.0025  -0.0229 158 SER A N   
1310 C CA  . SER A 158 ? 0.2258 0.1707 0.1698 -0.0129 0.0054  -0.0212 158 SER A CA  
1311 C C   . SER A 158 ? 0.2111 0.1683 0.1649 -0.0118 -0.0005 -0.0189 158 SER A C   
1312 O O   . SER A 158 ? 0.2087 0.1705 0.1618 -0.0132 -0.0047 -0.0183 158 SER A O   
1313 C CB  . SER A 158 ? 0.2555 0.1997 0.1973 -0.0125 0.0081  -0.0214 158 SER A CB  
1314 O OG  . SER A 158 ? 0.3059 0.2382 0.2392 -0.0122 0.0154  -0.0230 158 SER A OG  
1315 N N   . PHE A 159 ? 0.1963 0.1580 0.1587 -0.0092 -0.0006 -0.0174 159 PHE A N   
1316 C CA  . PHE A 159 ? 0.1856 0.1572 0.1557 -0.0078 -0.0055 -0.0152 159 PHE A CA  
1317 C C   . PHE A 159 ? 0.1799 0.1570 0.1566 -0.0054 -0.0052 -0.0138 159 PHE A C   
1318 O O   . PHE A 159 ? 0.1835 0.1603 0.1655 -0.0034 -0.0012 -0.0127 159 PHE A O   
1319 C CB  . PHE A 159 ? 0.1763 0.1503 0.1525 -0.0061 -0.0055 -0.0139 159 PHE A CB  
1320 C CG  . PHE A 159 ? 0.1674 0.1367 0.1381 -0.0086 -0.0069 -0.0146 159 PHE A CG  
1321 C CD1 . PHE A 159 ? 0.1742 0.1471 0.1436 -0.0104 -0.0121 -0.0133 159 PHE A CD1 
1322 C CD2 . PHE A 159 ? 0.1754 0.1360 0.1424 -0.0094 -0.0028 -0.0160 159 PHE A CD2 
1323 C CE1 . PHE A 159 ? 0.1811 0.1504 0.1468 -0.0132 -0.0142 -0.0128 159 PHE A CE1 
1324 C CE2 . PHE A 159 ? 0.1872 0.1425 0.1485 -0.0125 -0.0050 -0.0164 159 PHE A CE2 
1325 C CZ  . PHE A 159 ? 0.1816 0.1420 0.1428 -0.0146 -0.0111 -0.0145 159 PHE A CZ  
1326 N N   . CYS A 160 ? 0.1774 0.1596 0.1544 -0.0056 -0.0096 -0.0132 160 CYS A N   
1327 C CA  . CYS A 160 ? 0.1816 0.1679 0.1634 -0.0042 -0.0104 -0.0118 160 CYS A CA  
1328 C C   . CYS A 160 ? 0.1752 0.1668 0.1604 -0.0030 -0.0148 -0.0103 160 CYS A C   
1329 O O   . CYS A 160 ? 0.1811 0.1751 0.1700 -0.0023 -0.0161 -0.0089 160 CYS A O   
1330 C CB  . CYS A 160 ? 0.2017 0.1866 0.1789 -0.0058 -0.0105 -0.0128 160 CYS A CB  
1331 S SG  . CYS A 160 ? 0.2072 0.1925 0.1776 -0.0081 -0.0147 -0.0136 160 CYS A SG  
1332 N N   . TYR A 161 ? 0.1606 0.1533 0.1436 -0.0029 -0.0171 -0.0103 161 TYR A N   
1333 C CA  . TYR A 161 ? 0.1578 0.1535 0.1414 -0.0014 -0.0205 -0.0090 161 TYR A CA  
1334 C C   . TYR A 161 ? 0.1479 0.1452 0.1326 -0.0001 -0.0212 -0.0080 161 TYR A C   
1335 O O   . TYR A 161 ? 0.1466 0.1431 0.1302 -0.0010 -0.0204 -0.0081 161 TYR A O   
1336 C CB  . TYR A 161 ? 0.1484 0.1439 0.1270 -0.0019 -0.0224 -0.0094 161 TYR A CB  
1337 C CG  . TYR A 161 ? 0.1499 0.1462 0.1268 0.0001  -0.0248 -0.0083 161 TYR A CG  
1338 C CD1 . TYR A 161 ? 0.1642 0.1594 0.1405 0.0004  -0.0266 -0.0082 161 TYR A CD1 
1339 C CD2 . TYR A 161 ? 0.1577 0.1549 0.1328 0.0015  -0.0253 -0.0070 161 TYR A CD2 
1340 C CE1 . TYR A 161 ? 0.1733 0.1666 0.1453 0.0020  -0.0286 -0.0076 161 TYR A CE1 
1341 C CE2 . TYR A 161 ? 0.1680 0.1641 0.1399 0.0039  -0.0263 -0.0060 161 TYR A CE2 
1342 C CZ  . TYR A 161 ? 0.1717 0.1649 0.1409 0.0041  -0.0279 -0.0067 161 TYR A CZ  
1343 O OH  . TYR A 161 ? 0.1797 0.1693 0.1430 0.0063  -0.0287 -0.0061 161 TYR A OH  
1344 N N   . MET A 162 ? 0.1349 0.1341 0.1214 0.0016  -0.0230 -0.0066 162 MET A N   
1345 C CA  . MET A 162 ? 0.1393 0.1402 0.1261 0.0032  -0.0238 -0.0051 162 MET A CA  
1346 C C   . MET A 162 ? 0.1416 0.1418 0.1238 0.0049  -0.0260 -0.0044 162 MET A C   
1347 O O   . MET A 162 ? 0.1424 0.1411 0.1235 0.0045  -0.0277 -0.0045 162 MET A O   
1348 C CB  . MET A 162 ? 0.1523 0.1551 0.1451 0.0037  -0.0230 -0.0039 162 MET A CB  
1349 C CG  . MET A 162 ? 0.1644 0.1693 0.1574 0.0056  -0.0240 -0.0021 162 MET A CG  
1350 S SD  . MET A 162 ? 0.1893 0.1969 0.1903 0.0060  -0.0227 -0.0004 162 MET A SD  
1351 C CE  . MET A 162 ? 0.2042 0.2095 0.2055 0.0044  -0.0201 -0.0018 162 MET A CE  
1352 N N   . HIS A 163 ? 0.1442 0.1446 0.1233 0.0066  -0.0259 -0.0033 163 HIS A N   
1353 C CA  . HIS A 163 ? 0.1463 0.1439 0.1192 0.0088  -0.0267 -0.0027 163 HIS A CA  
1354 C C   . HIS A 163 ? 0.1486 0.1451 0.1197 0.0103  -0.0278 -0.0017 163 HIS A C   
1355 O O   . HIS A 163 ? 0.1525 0.1519 0.1271 0.0113  -0.0271 -0.0001 163 HIS A O   
1356 C CB  . HIS A 163 ? 0.1596 0.1579 0.1309 0.0107  -0.0252 -0.0006 163 HIS A CB  
1357 C CG  . HIS A 163 ? 0.1737 0.1674 0.1376 0.0134  -0.0246 -0.0001 163 HIS A CG  
1358 N ND1 . HIS A 163 ? 0.1932 0.1824 0.1522 0.0125  -0.0257 -0.0021 163 HIS A ND1 
1359 C CD2 . HIS A 163 ? 0.1884 0.1803 0.1484 0.0172  -0.0229 0.0023  163 HIS A CD2 
1360 C CE1 . HIS A 163 ? 0.2062 0.1900 0.1576 0.0155  -0.0245 -0.0012 163 HIS A CE1 
1361 N NE2 . HIS A 163 ? 0.2005 0.1855 0.1519 0.0186  -0.0224 0.0014  163 HIS A NE2 
1362 N N   . HIS A 164 ? 0.1504 0.1420 0.1151 0.0102  -0.0297 -0.0023 164 HIS A N   
1363 C CA  . HIS A 164 ? 0.1691 0.1581 0.1297 0.0109  -0.0315 -0.0012 164 HIS A CA  
1364 C C   . HIS A 164 ? 0.1951 0.1761 0.1434 0.0131  -0.0314 -0.0013 164 HIS A C   
1365 O O   . HIS A 164 ? 0.2104 0.1892 0.1541 0.0150  -0.0310 -0.0001 164 HIS A O   
1366 C CB  . HIS A 164 ? 0.1722 0.1610 0.1352 0.0075  -0.0351 -0.0010 164 HIS A CB  
1367 C CG  . HIS A 164 ? 0.1532 0.1487 0.1278 0.0062  -0.0345 0.0001  164 HIS A CG  
1368 N ND1 . HIS A 164 ? 0.1547 0.1526 0.1337 0.0053  -0.0361 0.0025  164 HIS A ND1 
1369 C CD2 . HIS A 164 ? 0.1520 0.1510 0.1338 0.0054  -0.0321 -0.0006 164 HIS A CD2 
1370 C CE1 . HIS A 164 ? 0.1538 0.1568 0.1431 0.0046  -0.0342 0.0033  164 HIS A CE1 
1371 N NE2 . HIS A 164 ? 0.1584 0.1614 0.1487 0.0047  -0.0316 0.0011  164 HIS A NE2 
1372 N N   A MET A 165 ? 0.2107 0.1865 0.1532 0.0126  -0.0317 -0.0029 165 MET A N   
1373 N N   B MET A 165 ? 0.1993 0.1751 0.1418 0.0126  -0.0317 -0.0029 165 MET A N   
1374 C CA  A MET A 165 ? 0.2385 0.2048 0.1679 0.0154  -0.0305 -0.0030 165 MET A CA  
1375 C CA  B MET A 165 ? 0.2125 0.1782 0.1414 0.0148  -0.0313 -0.0032 165 MET A CA  
1376 C C   A MET A 165 ? 0.2389 0.2011 0.1640 0.0169  -0.0281 -0.0037 165 MET A C   
1377 C C   B MET A 165 ? 0.2261 0.1882 0.1511 0.0168  -0.0283 -0.0038 165 MET A C   
1378 O O   A MET A 165 ? 0.2340 0.1991 0.1642 0.0146  -0.0292 -0.0048 165 MET A O   
1379 O O   B MET A 165 ? 0.2205 0.1856 0.1506 0.0147  -0.0292 -0.0048 165 MET A O   
1380 C CB  A MET A 165 ? 0.2700 0.2275 0.1892 0.0129  -0.0348 -0.0039 165 MET A CB  
1381 C CB  B MET A 165 ? 0.2153 0.1739 0.1371 0.0111  -0.0364 -0.0044 165 MET A CB  
1382 C CG  A MET A 165 ? 0.3156 0.2749 0.2397 0.0085  -0.0389 -0.0047 165 MET A CG  
1383 C CG  B MET A 165 ? 0.2179 0.1802 0.1450 0.0075  -0.0407 -0.0030 165 MET A CG  
1384 S SD  A MET A 165 ? 0.4189 0.3763 0.3410 0.0048  -0.0446 -0.0030 165 MET A SD  
1385 S SD  B MET A 165 ? 0.2343 0.1928 0.1536 0.0091  -0.0411 -0.0013 165 MET A SD  
1386 C CE  A MET A 165 ? 0.4248 0.3833 0.3446 0.0084  -0.0417 -0.0014 165 MET A CE  
1387 C CE  B MET A 165 ? 0.2937 0.2357 0.1926 0.0073  -0.0447 -0.0026 165 MET A CE  
1388 N N   . GLU A 166 ? 0.2493 0.2015 0.1619 0.0199  -0.0262 -0.0036 166 GLU A N   
1389 C CA  . GLU A 166 ? 0.2711 0.2172 0.1777 0.0221  -0.0233 -0.0039 166 GLU A CA  
1390 C C   . GLU A 166 ? 0.3063 0.2383 0.1974 0.0209  -0.0257 -0.0062 166 GLU A C   
1391 O O   . GLU A 166 ? 0.3201 0.2445 0.2007 0.0219  -0.0259 -0.0061 166 GLU A O   
1392 C CB  . GLU A 166 ? 0.2977 0.2430 0.2027 0.0279  -0.0169 -0.0007 166 GLU A CB  
1393 C CG  . GLU A 166 ? 0.3512 0.2905 0.2515 0.0306  -0.0131 -0.0001 166 GLU A CG  
1394 C CD  . GLU A 166 ? 0.4030 0.3466 0.3083 0.0360  -0.0068 0.0049  166 GLU A CD  
1395 O OE1 . GLU A 166 ? 0.4265 0.3640 0.3240 0.0405  -0.0028 0.0068  166 GLU A OE1 
1396 O OE2 . GLU A 166 ? 0.3872 0.3407 0.3047 0.0354  -0.0062 0.0075  166 GLU A OE2 
1397 N N   . LEU A 167 ? 0.3244 0.2526 0.2134 0.0184  -0.0279 -0.0079 167 LEU A N   
1398 C CA  . LEU A 167 ? 0.3661 0.2796 0.2395 0.0166  -0.0309 -0.0100 167 LEU A CA  
1399 C C   . LEU A 167 ? 0.4043 0.3052 0.2639 0.0220  -0.0247 -0.0099 167 LEU A C   
1400 O O   . LEU A 167 ? 0.3997 0.3053 0.2653 0.0264  -0.0187 -0.0078 167 LEU A O   
1401 C CB  . LEU A 167 ? 0.3754 0.2902 0.2534 0.0124  -0.0348 -0.0113 167 LEU A CB  
1402 C CG  . LEU A 167 ? 0.4016 0.3291 0.2946 0.0079  -0.0394 -0.0107 167 LEU A CG  
1403 C CD1 . LEU A 167 ? 0.4176 0.3442 0.3127 0.0040  -0.0432 -0.0114 167 LEU A CD1 
1404 C CD2 . LEU A 167 ? 0.4117 0.3399 0.3045 0.0050  -0.0439 -0.0097 167 LEU A CD2 
1405 N N   . PRO A 168 ? 0.4393 0.3232 0.2800 0.0214  -0.0261 -0.0117 168 PRO A N   
1406 C CA  . PRO A 168 ? 0.4669 0.3364 0.2926 0.0271  -0.0190 -0.0117 168 PRO A CA  
1407 C C   . PRO A 168 ? 0.4820 0.3517 0.3119 0.0298  -0.0144 -0.0111 168 PRO A C   
1408 O O   . PRO A 168 ? 0.5059 0.3678 0.3287 0.0360  -0.0067 -0.0095 168 PRO A O   
1409 C CB  . PRO A 168 ? 0.4906 0.3403 0.2940 0.0240  -0.0231 -0.0145 168 PRO A CB  
1410 C CG  . PRO A 168 ? 0.4903 0.3464 0.2981 0.0179  -0.0313 -0.0145 168 PRO A CG  
1411 C CD  . PRO A 168 ? 0.4489 0.3251 0.2801 0.0155  -0.0339 -0.0133 168 PRO A CD  
1412 N N   . THR A 169 ? 0.4686 0.3473 0.3103 0.0257  -0.0187 -0.0118 169 THR A N   
1413 C CA  . THR A 169 ? 0.4668 0.3475 0.3142 0.0278  -0.0149 -0.0108 169 THR A CA  
1414 C C   . THR A 169 ? 0.4478 0.3455 0.3136 0.0302  -0.0111 -0.0070 169 THR A C   
1415 O O   . THR A 169 ? 0.4469 0.3484 0.3194 0.0311  -0.0089 -0.0055 169 THR A O   
1416 C CB  . THR A 169 ? 0.4914 0.3711 0.3402 0.0222  -0.0211 -0.0131 169 THR A CB  
1417 O OG1 . THR A 169 ? 0.4986 0.3909 0.3595 0.0169  -0.0276 -0.0134 169 THR A OG1 
1418 C CG2 . THR A 169 ? 0.5117 0.3714 0.3405 0.0203  -0.0239 -0.0159 169 THR A CG2 
1419 N N   . GLY A 170 ? 0.4288 0.3363 0.3024 0.0310  -0.0107 -0.0052 170 GLY A N   
1420 C CA  . GLY A 170 ? 0.4084 0.3306 0.2979 0.0327  -0.0078 -0.0012 170 GLY A CA  
1421 C C   . GLY A 170 ? 0.3825 0.3184 0.2863 0.0276  -0.0126 -0.0018 170 GLY A C   
1422 O O   . GLY A 170 ? 0.3849 0.3314 0.3003 0.0280  -0.0110 0.0014  170 GLY A O   
1423 N N   . VAL A 171 ? 0.3537 0.2884 0.2562 0.0226  -0.0185 -0.0054 171 VAL A N   
1424 C CA  . VAL A 171 ? 0.3148 0.2609 0.2295 0.0182  -0.0223 -0.0060 171 VAL A CA  
1425 C C   . VAL A 171 ? 0.2636 0.2147 0.1821 0.0166  -0.0248 -0.0064 171 VAL A C   
1426 O O   . VAL A 171 ? 0.2655 0.2109 0.1765 0.0180  -0.0248 -0.0066 171 VAL A O   
1427 C CB  . VAL A 171 ? 0.3351 0.2792 0.2497 0.0143  -0.0262 -0.0082 171 VAL A CB  
1428 C CG1 . VAL A 171 ? 0.3511 0.2915 0.2636 0.0161  -0.0234 -0.0074 171 VAL A CG1 
1429 C CG2 . VAL A 171 ? 0.3457 0.2805 0.2507 0.0118  -0.0307 -0.0104 171 VAL A CG2 
1430 N N   . HIS A 172 ? 0.2320 0.1932 0.1615 0.0137  -0.0265 -0.0064 172 HIS A N   
1431 C CA  . HIS A 172 ? 0.2098 0.1766 0.1447 0.0127  -0.0277 -0.0062 172 HIS A CA  
1432 C C   . HIS A 172 ? 0.2010 0.1704 0.1405 0.0086  -0.0317 -0.0076 172 HIS A C   
1433 O O   . HIS A 172 ? 0.2016 0.1725 0.1443 0.0062  -0.0330 -0.0084 172 HIS A O   
1434 C CB  . HIS A 172 ? 0.1986 0.1740 0.1423 0.0134  -0.0251 -0.0041 172 HIS A CB  
1435 C CG  . HIS A 172 ? 0.1979 0.1719 0.1392 0.0177  -0.0211 -0.0010 172 HIS A CG  
1436 N ND1 . HIS A 172 ? 0.2129 0.1892 0.1572 0.0184  -0.0190 0.0013  172 HIS A ND1 
1437 C CD2 . HIS A 172 ? 0.2140 0.1836 0.1495 0.0216  -0.0186 0.0006  172 HIS A CD2 
1438 C CE1 . HIS A 172 ? 0.2212 0.1955 0.1633 0.0229  -0.0150 0.0048  172 HIS A CE1 
1439 N NE2 . HIS A 172 ? 0.2297 0.1995 0.1659 0.0252  -0.0143 0.0044  172 HIS A NE2 
1440 N N   . ALA A 173 ? 0.1934 0.1642 0.1343 0.0080  -0.0331 -0.0072 173 ALA A N   
1441 C CA  . ALA A 173 ? 0.1885 0.1623 0.1353 0.0046  -0.0364 -0.0072 173 ALA A CA  
1442 C C   . ALA A 173 ? 0.1771 0.1575 0.1317 0.0048  -0.0352 -0.0061 173 ALA A C   
1443 O O   . ALA A 173 ? 0.1781 0.1590 0.1312 0.0072  -0.0336 -0.0053 173 ALA A O   
1444 C CB  . ALA A 173 ? 0.1967 0.1635 0.1362 0.0027  -0.0408 -0.0069 173 ALA A CB  
1445 N N   . GLY A 174 ? 0.1663 0.1516 0.1295 0.0026  -0.0356 -0.0057 174 GLY A N   
1446 C CA  . GLY A 174 ? 0.1590 0.1496 0.1298 0.0028  -0.0340 -0.0047 174 GLY A CA  
1447 C C   . GLY A 174 ? 0.1505 0.1445 0.1298 0.0006  -0.0341 -0.0036 174 GLY A C   
1448 O O   . GLY A 174 ? 0.1524 0.1453 0.1323 -0.0012 -0.0363 -0.0029 174 GLY A O   
1449 N N   . THR A 175 ? 0.1423 0.1401 0.1283 0.0010  -0.0314 -0.0030 175 THR A N   
1450 C CA  . THR A 175 ? 0.1365 0.1372 0.1314 -0.0001 -0.0302 -0.0010 175 THR A CA  
1451 C C   . THR A 175 ? 0.1378 0.1390 0.1355 0.0001  -0.0256 -0.0025 175 THR A C   
1452 O O   . THR A 175 ? 0.1427 0.1426 0.1360 0.0006  -0.0241 -0.0047 175 THR A O   
1453 C CB  . THR A 175 ? 0.1438 0.1473 0.1442 0.0003  -0.0307 0.0017  175 THR A CB  
1454 O OG1 . THR A 175 ? 0.1485 0.1530 0.1492 0.0019  -0.0277 0.0004  175 THR A OG1 
1455 C CG2 . THR A 175 ? 0.1331 0.1350 0.1289 -0.0004 -0.0355 0.0032  175 THR A CG2 
1456 N N   . ASP A 176 ? 0.1357 0.1384 0.1409 -0.0003 -0.0231 -0.0006 176 ASP A N   
1457 C CA  . ASP A 176 ? 0.1402 0.1414 0.1467 0.0002  -0.0177 -0.0019 176 ASP A CA  
1458 C C   . ASP A 176 ? 0.1491 0.1512 0.1593 0.0014  -0.0159 -0.0011 176 ASP A C   
1459 O O   . ASP A 176 ? 0.1476 0.1524 0.1594 0.0017  -0.0190 0.0005  176 ASP A O   
1460 C CB  . ASP A 176 ? 0.1529 0.1542 0.1652 0.0002  -0.0144 0.0002  176 ASP A CB  
1461 C CG  . ASP A 176 ? 0.1714 0.1768 0.1944 0.0005  -0.0146 0.0055  176 ASP A CG  
1462 O OD1 . ASP A 176 ? 0.1481 0.1558 0.1743 0.0008  -0.0165 0.0072  176 ASP A OD1 
1463 O OD2 . ASP A 176 ? 0.1979 0.2047 0.2269 0.0004  -0.0132 0.0086  176 ASP A OD2 
1464 N N   . LEU A 177 ? 0.1557 0.1549 0.1667 0.0018  -0.0108 -0.0021 177 LEU A N   
1465 C CA  . LEU A 177 ? 0.1647 0.1641 0.1791 0.0028  -0.0091 -0.0014 177 LEU A CA  
1466 C C   . LEU A 177 ? 0.1765 0.1794 0.2020 0.0040  -0.0071 0.0031  177 LEU A C   
1467 O O   . LEU A 177 ? 0.1817 0.1855 0.2115 0.0049  -0.0057 0.0043  177 LEU A O   
1468 C CB  . LEU A 177 ? 0.1687 0.1618 0.1774 0.0023  -0.0052 -0.0044 177 LEU A CB  
1469 C CG  . LEU A 177 ? 0.1860 0.1781 0.1872 0.0009  -0.0085 -0.0067 177 LEU A CG  
1470 C CD1 . LEU A 177 ? 0.1940 0.1903 0.1990 0.0020  -0.0110 -0.0050 177 LEU A CD1 
1471 C CD2 . LEU A 177 ? 0.2019 0.1950 0.1976 -0.0001 -0.0120 -0.0078 177 LEU A CD2 
1472 N N   . GLU A 178 ? 0.1687 0.1743 0.1999 0.0038  -0.0076 0.0064  178 GLU A N   
1473 C CA  . GLU A 178 ? 0.1564 0.1671 0.1995 0.0043  -0.0076 0.0123  178 GLU A CA  
1474 C C   . GLU A 178 ? 0.1508 0.1657 0.1938 0.0026  -0.0152 0.0143  178 GLU A C   
1475 O O   . GLU A 178 ? 0.1516 0.1712 0.2037 0.0020  -0.0171 0.0198  178 GLU A O   
1476 C CB  . GLU A 178 ? 0.1777 0.1894 0.2282 0.0047  -0.0044 0.0162  178 GLU A CB  
1477 C CG  . GLU A 178 ? 0.2469 0.2527 0.2963 0.0068  0.0043  0.0145  178 GLU A CG  
1478 C CD  . GLU A 178 ? 0.3511 0.3573 0.4079 0.0081  0.0092  0.0189  178 GLU A CD  
1479 O OE1 . GLU A 178 ? 0.3485 0.3603 0.4119 0.0068  0.0049  0.0235  178 GLU A OE1 
1480 O OE2 . GLU A 178 ? 0.4024 0.4025 0.4580 0.0103  0.0175  0.0182  178 GLU A OE2 
1481 N N   . GLY A 179 ? 0.1512 0.1640 0.1836 0.0018  -0.0194 0.0105  179 GLY A N   
1482 C CA  . GLY A 179 ? 0.1460 0.1601 0.1751 0.0006  -0.0257 0.0117  179 GLY A CA  
1483 C C   . GLY A 179 ? 0.1411 0.1548 0.1686 -0.0018 -0.0306 0.0136  179 GLY A C   
1484 O O   . GLY A 179 ? 0.1464 0.1596 0.1702 -0.0034 -0.0361 0.0151  179 GLY A O   
1485 N N   . ASN A 180 ? 0.1351 0.1482 0.1645 -0.0022 -0.0289 0.0137  180 ASN A N   
1486 C CA  . ASN A 180 ? 0.1386 0.1510 0.1668 -0.0047 -0.0339 0.0158  180 ASN A CA  
1487 C C   . ASN A 180 ? 0.1367 0.1440 0.1525 -0.0048 -0.0357 0.0106  180 ASN A C   
1488 O O   . ASN A 180 ? 0.1297 0.1355 0.1425 -0.0035 -0.0318 0.0071  180 ASN A O   
1489 C CB  . ASN A 180 ? 0.1521 0.1674 0.1905 -0.0049 -0.0310 0.0197  180 ASN A CB  
1490 C CG  . ASN A 180 ? 0.1866 0.2074 0.2390 -0.0049 -0.0296 0.0267  180 ASN A CG  
1491 O OD1 . ASN A 180 ? 0.2108 0.2333 0.2715 -0.0025 -0.0227 0.0285  180 ASN A OD1 
1492 N ND2 . ASN A 180 ? 0.1778 0.2009 0.2326 -0.0074 -0.0358 0.0310  180 ASN A ND2 
1493 N N   . PHE A 181 ? 0.1401 0.1438 0.1479 -0.0066 -0.0415 0.0105  181 PHE A N   
1494 C CA  . PHE A 181 ? 0.1528 0.1509 0.1490 -0.0063 -0.0427 0.0062  181 PHE A CA  
1495 C C   . PHE A 181 ? 0.1580 0.1562 0.1561 -0.0071 -0.0419 0.0060  181 PHE A C   
1496 O O   . PHE A 181 ? 0.1538 0.1548 0.1602 -0.0089 -0.0430 0.0100  181 PHE A O   
1497 C CB  . PHE A 181 ? 0.1623 0.1544 0.1484 -0.0081 -0.0487 0.0065  181 PHE A CB  
1498 C CG  . PHE A 181 ? 0.1681 0.1570 0.1456 -0.0060 -0.0481 0.0043  181 PHE A CG  
1499 C CD1 . PHE A 181 ? 0.1711 0.1620 0.1510 -0.0062 -0.0494 0.0068  181 PHE A CD1 
1500 C CD2 . PHE A 181 ? 0.1768 0.1609 0.1444 -0.0036 -0.0461 0.0005  181 PHE A CD2 
1501 C CE1 . PHE A 181 ? 0.1778 0.1658 0.1498 -0.0040 -0.0486 0.0052  181 PHE A CE1 
1502 C CE2 . PHE A 181 ? 0.1865 0.1678 0.1470 -0.0011 -0.0449 -0.0005 181 PHE A CE2 
1503 C CZ  . PHE A 181 ? 0.1834 0.1666 0.1458 -0.0012 -0.0461 0.0017  181 PHE A CZ  
1504 N N   . TYR A 182 ? 0.1537 0.1491 0.1449 -0.0058 -0.0398 0.0019  182 TYR A N   
1505 C CA  . TYR A 182 ? 0.1648 0.1594 0.1557 -0.0067 -0.0400 0.0014  182 TYR A CA  
1506 C C   . TYR A 182 ? 0.1812 0.1704 0.1651 -0.0089 -0.0460 0.0020  182 TYR A C   
1507 O O   . TYR A 182 ? 0.1923 0.1761 0.1665 -0.0083 -0.0478 0.0002  182 TYR A O   
1508 C CB  . TYR A 182 ? 0.1636 0.1569 0.1491 -0.0050 -0.0364 -0.0026 182 TYR A CB  
1509 C CG  . TYR A 182 ? 0.1610 0.1576 0.1518 -0.0041 -0.0312 -0.0031 182 TYR A CG  
1510 C CD1 . TYR A 182 ? 0.1643 0.1626 0.1605 -0.0046 -0.0286 -0.0020 182 TYR A CD1 
1511 C CD2 . TYR A 182 ? 0.1635 0.1606 0.1534 -0.0027 -0.0287 -0.0044 182 TYR A CD2 
1512 C CE1 . TYR A 182 ? 0.1644 0.1631 0.1626 -0.0038 -0.0232 -0.0028 182 TYR A CE1 
1513 C CE2 . TYR A 182 ? 0.1670 0.1648 0.1595 -0.0023 -0.0242 -0.0052 182 TYR A CE2 
1514 C CZ  . TYR A 182 ? 0.1702 0.1681 0.1661 -0.0029 -0.0212 -0.0046 182 TYR A CZ  
1515 O OH  . TYR A 182 ? 0.1692 0.1653 0.1651 -0.0025 -0.0162 -0.0057 182 TYR A OH  
1516 N N   . GLY A 183 ? 0.1830 0.1729 0.1714 -0.0113 -0.0488 0.0049  183 GLY A N   
1517 C CA  . GLY A 183 ? 0.2017 0.1853 0.1830 -0.0142 -0.0551 0.0058  183 GLY A CA  
1518 C C   . GLY A 183 ? 0.2106 0.1916 0.1898 -0.0167 -0.0605 0.0087  183 GLY A C   
1519 O O   . GLY A 183 ? 0.2050 0.1914 0.1923 -0.0166 -0.0597 0.0118  183 GLY A O   
1520 N N   . PRO A 184 ? 0.2194 0.1910 0.1864 -0.0190 -0.0659 0.0079  184 PRO A N   
1521 C CA  . PRO A 184 ? 0.2234 0.1908 0.1861 -0.0227 -0.0724 0.0112  184 PRO A CA  
1522 C C   . PRO A 184 ? 0.2274 0.1897 0.1796 -0.0209 -0.0716 0.0086  184 PRO A C   
1523 O O   . PRO A 184 ? 0.2463 0.2028 0.1912 -0.0241 -0.0773 0.0107  184 PRO A O   
1524 C CB  . PRO A 184 ? 0.2447 0.2017 0.1965 -0.0264 -0.0787 0.0110  184 PRO A CB  
1525 C CG  . PRO A 184 ? 0.2552 0.2077 0.1988 -0.0224 -0.0734 0.0051  184 PRO A CG  
1526 C CD  . PRO A 184 ? 0.2274 0.1912 0.1842 -0.0190 -0.0667 0.0046  184 PRO A CD  
1527 N N   . PHE A 185 ? 0.2187 0.1827 0.1693 -0.0159 -0.0649 0.0045  185 PHE A N   
1528 C CA  . PHE A 185 ? 0.2245 0.1836 0.1649 -0.0134 -0.0632 0.0022  185 PHE A CA  
1529 C C   . PHE A 185 ? 0.2280 0.1925 0.1746 -0.0138 -0.0639 0.0052  185 PHE A C   
1530 O O   . PHE A 185 ? 0.2167 0.1908 0.1780 -0.0146 -0.0631 0.0084  185 PHE A O   
1531 C CB  . PHE A 185 ? 0.2196 0.1798 0.1582 -0.0083 -0.0562 -0.0017 185 PHE A CB  
1532 C CG  . PHE A 185 ? 0.2271 0.1816 0.1595 -0.0080 -0.0557 -0.0041 185 PHE A CG  
1533 C CD1 . PHE A 185 ? 0.2458 0.1877 0.1632 -0.0089 -0.0586 -0.0054 185 PHE A CD1 
1534 C CD2 . PHE A 185 ? 0.2299 0.1909 0.1710 -0.0072 -0.0527 -0.0047 185 PHE A CD2 
1535 C CE1 . PHE A 185 ? 0.2512 0.1878 0.1637 -0.0087 -0.0581 -0.0071 185 PHE A CE1 
1536 C CE2 . PHE A 185 ? 0.2336 0.1901 0.1701 -0.0073 -0.0526 -0.0062 185 PHE A CE2 
1537 C CZ  . PHE A 185 ? 0.2389 0.1835 0.1617 -0.0078 -0.0552 -0.0074 185 PHE A CZ  
1538 N N   . VAL A 186 ? 0.2393 0.1970 0.1744 -0.0134 -0.0652 0.0045  186 VAL A N   
1539 C CA  . VAL A 186 ? 0.2422 0.2041 0.1814 -0.0139 -0.0663 0.0074  186 VAL A CA  
1540 C C   . VAL A 186 ? 0.2486 0.2085 0.1806 -0.0092 -0.0614 0.0047  186 VAL A C   
1541 O O   . VAL A 186 ? 0.2669 0.2189 0.1870 -0.0063 -0.0588 0.0013  186 VAL A O   
1542 C CB  . VAL A 186 ? 0.2610 0.2167 0.1934 -0.0196 -0.0747 0.0112  186 VAL A CB  
1543 C CG1 . VAL A 186 ? 0.2715 0.2320 0.2153 -0.0245 -0.0797 0.0160  186 VAL A CG1 
1544 C CG2 . VAL A 186 ? 0.2830 0.2224 0.1930 -0.0204 -0.0773 0.0080  186 VAL A CG2 
1545 N N   . ASP A 187 ? 0.2285 0.1956 0.1684 -0.0081 -0.0601 0.0069  187 ASP A N   
1546 C CA  . ASP A 187 ? 0.2303 0.1966 0.1651 -0.0037 -0.0557 0.0053  187 ASP A CA  
1547 C C   . ASP A 187 ? 0.2549 0.2120 0.1752 -0.0047 -0.0590 0.0061  187 ASP A C   
1548 O O   . ASP A 187 ? 0.2531 0.2136 0.1759 -0.0047 -0.0597 0.0085  187 ASP A O   
1549 C CB  . ASP A 187 ? 0.2152 0.1930 0.1649 -0.0016 -0.0519 0.0067  187 ASP A CB  
1550 C CG  . ASP A 187 ? 0.2089 0.1944 0.1717 -0.0048 -0.0548 0.0111  187 ASP A CG  
1551 O OD1 . ASP A 187 ? 0.2092 0.1923 0.1709 -0.0092 -0.0606 0.0141  187 ASP A OD1 
1552 O OD2 . ASP A 187 ? 0.1961 0.1897 0.1704 -0.0029 -0.0512 0.0121  187 ASP A OD2 
1553 N N   . ARG A 188 ? 0.2821 0.2263 0.1859 -0.0057 -0.0611 0.0040  188 ARG A N   
1554 C CA  . ARG A 188 ? 0.3215 0.2525 0.2064 -0.0070 -0.0642 0.0040  188 ARG A CA  
1555 C C   . ARG A 188 ? 0.3521 0.2702 0.2206 -0.0035 -0.0603 0.0000  188 ARG A C   
1556 O O   . ARG A 188 ? 0.3475 0.2648 0.2178 -0.0036 -0.0596 -0.0019 188 ARG A O   
1557 C CB  . ARG A 188 ? 0.3562 0.2825 0.2376 -0.0146 -0.0735 0.0070  188 ARG A CB  
1558 C CG  . ARG A 188 ? 0.4405 0.3529 0.3017 -0.0173 -0.0780 0.0076  188 ARG A CG  
1559 C CD  . ARG A 188 ? 0.5164 0.4237 0.3738 -0.0260 -0.0885 0.0114  188 ARG A CD  
1560 N NE  . ARG A 188 ? 0.5940 0.4813 0.4246 -0.0288 -0.0924 0.0099  188 ARG A NE  
1561 C CZ  . ARG A 188 ? 0.6437 0.5225 0.4646 -0.0369 -0.1024 0.0134  188 ARG A CZ  
1562 N NH1 . ARG A 188 ? 0.6388 0.5290 0.4771 -0.0431 -0.1096 0.0195  188 ARG A NH1 
1563 N NH2 . ARG A 188 ? 0.6649 0.5232 0.4584 -0.0392 -0.1053 0.0113  188 ARG A NH2 
1564 N N   . GLN A 189 ? 0.3850 0.2930 0.2379 -0.0002 -0.0573 -0.0009 189 GLN A N   
1565 C CA  . GLN A 189 ? 0.4227 0.3172 0.2593 0.0041  -0.0522 -0.0040 189 GLN A CA  
1566 C C   . GLN A 189 ? 0.4583 0.3352 0.2753 -0.0010 -0.0582 -0.0054 189 GLN A C   
1567 O O   . GLN A 189 ? 0.4780 0.3414 0.2765 -0.0022 -0.0601 -0.0054 189 GLN A O   
1568 C CB  . GLN A 189 ? 0.4560 0.3469 0.2846 0.0103  -0.0454 -0.0036 189 GLN A CB  
1569 C CG  . GLN A 189 ? 0.5266 0.4059 0.3421 0.0164  -0.0378 -0.0056 189 GLN A CG  
1570 C CD  . GLN A 189 ? 0.6110 0.4864 0.4185 0.0225  -0.0312 -0.0040 189 GLN A CD  
1571 O OE1 . GLN A 189 ? 0.6280 0.5166 0.4490 0.0248  -0.0292 -0.0013 189 GLN A OE1 
1572 N NE2 . GLN A 189 ? 0.6387 0.4950 0.4234 0.0254  -0.0275 -0.0054 189 GLN A NE2 
1573 N N   . THR A 190 ? 0.4705 0.3476 0.2918 -0.0045 -0.0618 -0.0063 190 THR A N   
1574 C CA  . THR A 190 ? 0.5034 0.3648 0.3086 -0.0104 -0.0687 -0.0071 190 THR A CA  
1575 C C   . THR A 190 ? 0.5160 0.3722 0.3190 -0.0089 -0.0662 -0.0100 190 THR A C   
1576 O O   . THR A 190 ? 0.5161 0.3828 0.3322 -0.0039 -0.0597 -0.0107 190 THR A O   
1577 C CB  . THR A 190 ? 0.5318 0.4010 0.3480 -0.0186 -0.0788 -0.0031 190 THR A CB  
1578 O OG1 . THR A 190 ? 0.5408 0.4293 0.3822 -0.0179 -0.0774 -0.0014 190 THR A OG1 
1579 C CG2 . THR A 190 ? 0.5465 0.4150 0.3586 -0.0220 -0.0835 0.0001  190 THR A CG2 
1580 N N   . ALA A 191 ? 0.5262 0.3663 0.3131 -0.0138 -0.0719 -0.0112 191 ALA A N   
1581 C CA  . ALA A 191 ? 0.5322 0.3675 0.3178 -0.0132 -0.0705 -0.0134 191 ALA A CA  
1582 C C   . ALA A 191 ? 0.5178 0.3715 0.3276 -0.0162 -0.0740 -0.0110 191 ALA A C   
1583 O O   . ALA A 191 ? 0.5351 0.3910 0.3496 -0.0232 -0.0828 -0.0080 191 ALA A O   
1584 C CB  . ALA A 191 ? 0.5515 0.3644 0.3138 -0.0185 -0.0768 -0.0149 191 ALA A CB  
1585 N N   . GLN A 192 ? 0.4838 0.3510 0.3093 -0.0110 -0.0671 -0.0115 192 GLN A N   
1586 C CA  . GLN A 192 ? 0.4556 0.3388 0.3022 -0.0128 -0.0686 -0.0098 192 GLN A CA  
1587 C C   . GLN A 192 ? 0.4553 0.3366 0.3017 -0.0092 -0.0634 -0.0122 192 GLN A C   
1588 O O   . GLN A 192 ? 0.4729 0.3568 0.3204 -0.0031 -0.0556 -0.0134 192 GLN A O   
1589 C CB  . GLN A 192 ? 0.4330 0.3339 0.2979 -0.0100 -0.0647 -0.0081 192 GLN A CB  
1590 C CG  . GLN A 192 ? 0.4245 0.3272 0.2891 -0.0117 -0.0676 -0.0057 192 GLN A CG  
1591 C CD  . GLN A 192 ? 0.3715 0.2920 0.2566 -0.0101 -0.0647 -0.0038 192 GLN A CD  
1592 O OE1 . GLN A 192 ? 0.3411 0.2712 0.2406 -0.0125 -0.0666 -0.0019 192 GLN A OE1 
1593 N NE2 . GLN A 192 ? 0.3545 0.2788 0.2407 -0.0057 -0.0597 -0.0041 192 GLN A NE2 
1594 N N   . ALA A 193 ? 0.4362 0.3127 0.2810 -0.0129 -0.0677 -0.0124 193 ALA A N   
1595 C CA  . ALA A 193 ? 0.4262 0.3013 0.2715 -0.0096 -0.0629 -0.0143 193 ALA A CA  
1596 C C   . ALA A 193 ? 0.4005 0.2918 0.2661 -0.0109 -0.0634 -0.0126 193 ALA A C   
1597 O O   . ALA A 193 ? 0.3993 0.2976 0.2745 -0.0157 -0.0693 -0.0099 193 ALA A O   
1598 C CB  . ALA A 193 ? 0.4384 0.2947 0.2658 -0.0122 -0.0662 -0.0160 193 ALA A CB  
1599 N N   . ALA A 194 ? 0.3784 0.2757 0.2506 -0.0066 -0.0571 -0.0136 194 ALA A N   
1600 C CA  . ALA A 194 ? 0.3522 0.2633 0.2414 -0.0076 -0.0568 -0.0123 194 ALA A CA  
1601 C C   . ALA A 194 ? 0.3308 0.2368 0.2184 -0.0108 -0.0606 -0.0122 194 ALA A C   
1602 O O   . ALA A 194 ? 0.3411 0.2333 0.2150 -0.0104 -0.0607 -0.0139 194 ALA A O   
1603 C CB  . ALA A 194 ? 0.3502 0.2696 0.2465 -0.0025 -0.0493 -0.0129 194 ALA A CB  
1604 N N   . GLY A 195 ? 0.2987 0.2156 0.2004 -0.0136 -0.0632 -0.0100 195 GLY A N   
1605 C CA  . GLY A 195 ? 0.2911 0.2060 0.1945 -0.0164 -0.0665 -0.0092 195 GLY A CA  
1606 C C   . GLY A 195 ? 0.2800 0.1973 0.1857 -0.0127 -0.0606 -0.0108 195 GLY A C   
1607 O O   . GLY A 195 ? 0.2772 0.1964 0.1819 -0.0082 -0.0544 -0.0122 195 GLY A O   
1608 N N   . THR A 196 ? 0.2668 0.1859 0.1776 -0.0148 -0.0627 -0.0097 196 THR A N   
1609 C CA  . THR A 196 ? 0.2699 0.1913 0.1834 -0.0121 -0.0581 -0.0105 196 THR A CA  
1610 C C   . THR A 196 ? 0.2685 0.2034 0.1931 -0.0095 -0.0527 -0.0101 196 THR A C   
1611 O O   . THR A 196 ? 0.2559 0.2007 0.1909 -0.0111 -0.0536 -0.0087 196 THR A O   
1612 C CB  . THR A 196 ? 0.2861 0.2086 0.2049 -0.0155 -0.0621 -0.0088 196 THR A CB  
1613 O OG1 . THR A 196 ? 0.3079 0.2169 0.2157 -0.0191 -0.0684 -0.0087 196 THR A OG1 
1614 C CG2 . THR A 196 ? 0.2955 0.2193 0.2161 -0.0131 -0.0578 -0.0092 196 THR A CG2 
1615 N N   . ASP A 197 ? 0.2743 0.2089 0.1966 -0.0054 -0.0470 -0.0110 197 ASP A N   
1616 C CA  . ASP A 197 ? 0.2719 0.2186 0.2041 -0.0038 -0.0428 -0.0102 197 ASP A CA  
1617 C C   . ASP A 197 ? 0.2617 0.2144 0.2013 -0.0050 -0.0423 -0.0090 197 ASP A C   
1618 O O   . ASP A 197 ? 0.2930 0.2452 0.2321 -0.0030 -0.0392 -0.0083 197 ASP A O   
1619 C CB  . ASP A 197 ? 0.2997 0.2457 0.2285 0.0004  -0.0377 -0.0102 197 ASP A CB  
1620 C CG  . ASP A 197 ? 0.3365 0.2940 0.2744 0.0008  -0.0350 -0.0091 197 ASP A CG  
1621 O OD1 . ASP A 197 ? 0.2888 0.2537 0.2342 -0.0018 -0.0366 -0.0090 197 ASP A OD1 
1622 O OD2 . ASP A 197 ? 0.3987 0.3570 0.3357 0.0038  -0.0313 -0.0081 197 ASP A OD2 
1623 N N   A THR A 198 ? 0.2387 0.1970 0.1855 -0.0081 -0.0454 -0.0081 198 THR A N   
1624 N N   B THR A 198 ? 0.2362 0.1952 0.1834 -0.0080 -0.0451 -0.0081 198 THR A N   
1625 C CA  A THR A 198 ? 0.2296 0.1938 0.1834 -0.0094 -0.0450 -0.0068 198 THR A CA  
1626 C CA  B THR A 198 ? 0.2258 0.1911 0.1806 -0.0097 -0.0452 -0.0067 198 THR A CA  
1627 C C   A THR A 198 ? 0.2161 0.1890 0.1751 -0.0084 -0.0407 -0.0063 198 THR A C   
1628 C C   B THR A 198 ? 0.2140 0.1880 0.1741 -0.0088 -0.0409 -0.0063 198 THR A C   
1629 O O   A THR A 198 ? 0.2153 0.1908 0.1743 -0.0073 -0.0386 -0.0069 198 THR A O   
1630 O O   B THR A 198 ? 0.2128 0.1903 0.1740 -0.0081 -0.0390 -0.0068 198 THR A O   
1631 C CB  A THR A 198 ? 0.2460 0.2133 0.2061 -0.0126 -0.0489 -0.0051 198 THR A CB  
1632 C CB  B THR A 198 ? 0.2355 0.2043 0.1965 -0.0126 -0.0488 -0.0051 198 THR A CB  
1633 O OG1 A THR A 198 ? 0.2540 0.2270 0.2191 -0.0130 -0.0483 -0.0046 198 THR A OG1 
1634 O OG1 B THR A 198 ? 0.2486 0.2088 0.2041 -0.0145 -0.0540 -0.0048 198 THR A OG1 
1635 C CG2 A THR A 198 ? 0.2543 0.2123 0.2089 -0.0148 -0.0545 -0.0046 198 THR A CG2 
1636 C CG2 B THR A 198 ? 0.2360 0.2113 0.2051 -0.0142 -0.0487 -0.0032 198 THR A CG2 
1637 N N   . THR A 199 ? 0.1998 0.1767 0.1627 -0.0091 -0.0398 -0.0051 199 THR A N   
1638 C CA  . THR A 199 ? 0.1870 0.1712 0.1538 -0.0093 -0.0367 -0.0041 199 THR A CA  
1639 C C   . THR A 199 ? 0.1754 0.1658 0.1475 -0.0115 -0.0366 -0.0039 199 THR A C   
1640 O O   . THR A 199 ? 0.1801 0.1711 0.1555 -0.0128 -0.0384 -0.0031 199 THR A O   
1641 C CB  . THR A 199 ? 0.2008 0.1857 0.1684 -0.0089 -0.0355 -0.0022 199 THR A CB  
1642 O OG1 . THR A 199 ? 0.2126 0.1907 0.1749 -0.0059 -0.0342 -0.0021 199 THR A OG1 
1643 C CG2 . THR A 199 ? 0.2025 0.1949 0.1736 -0.0100 -0.0333 -0.0004 199 THR A CG2 
1644 N N   . ILE A 200 ? 0.1639 0.1580 0.1363 -0.0118 -0.0342 -0.0043 200 ILE A N   
1645 C CA  . ILE A 200 ? 0.1650 0.1627 0.1402 -0.0134 -0.0327 -0.0044 200 ILE A CA  
1646 C C   . ILE A 200 ? 0.1575 0.1587 0.1338 -0.0153 -0.0318 -0.0030 200 ILE A C   
1647 O O   . ILE A 200 ? 0.1543 0.1573 0.1284 -0.0166 -0.0304 -0.0027 200 ILE A O   
1648 C CB  . ILE A 200 ? 0.1682 0.1662 0.1412 -0.0132 -0.0306 -0.0057 200 ILE A CB  
1649 C CG1 . ILE A 200 ? 0.1744 0.1693 0.1460 -0.0112 -0.0317 -0.0067 200 ILE A CG1 
1650 C CG2 . ILE A 200 ? 0.1724 0.1717 0.1471 -0.0142 -0.0282 -0.0059 200 ILE A CG2 
1651 C CD1 . ILE A 200 ? 0.1923 0.1873 0.1614 -0.0105 -0.0302 -0.0073 200 ILE A CD1 
1652 N N   . THR A 201 ? 0.1548 0.1570 0.1348 -0.0158 -0.0329 -0.0018 201 THR A N   
1653 C CA  . THR A 201 ? 0.1566 0.1622 0.1383 -0.0175 -0.0324 -0.0001 201 THR A CA  
1654 C C   . THR A 201 ? 0.1622 0.1698 0.1412 -0.0193 -0.0294 -0.0002 201 THR A C   
1655 O O   . THR A 201 ? 0.1723 0.1817 0.1493 -0.0212 -0.0293 0.0008  201 THR A O   
1656 C CB  . THR A 201 ? 0.1688 0.1753 0.1557 -0.0177 -0.0339 0.0016  201 THR A CB  
1657 O OG1 . THR A 201 ? 0.1778 0.1802 0.1650 -0.0168 -0.0373 0.0015  201 THR A OG1 
1658 C CG2 . THR A 201 ? 0.1775 0.1876 0.1668 -0.0192 -0.0336 0.0037  201 THR A CG2 
1659 N N   . VAL A 202 ? 0.1512 0.1577 0.1297 -0.0189 -0.0270 -0.0012 202 VAL A N   
1660 C CA  . VAL A 202 ? 0.1608 0.1665 0.1342 -0.0206 -0.0235 -0.0018 202 VAL A CA  
1661 C C   . VAL A 202 ? 0.1642 0.1685 0.1313 -0.0225 -0.0241 -0.0028 202 VAL A C   
1662 O O   . VAL A 202 ? 0.1653 0.1690 0.1273 -0.0253 -0.0233 -0.0023 202 VAL A O   
1663 C CB  . VAL A 202 ? 0.1747 0.1781 0.1485 -0.0192 -0.0197 -0.0024 202 VAL A CB  
1664 C CG1 . VAL A 202 ? 0.1879 0.1889 0.1611 -0.0177 -0.0196 -0.0042 202 VAL A CG1 
1665 C CG2 . VAL A 202 ? 0.1887 0.1892 0.1558 -0.0207 -0.0153 -0.0028 202 VAL A CG2 
1666 N N   . ASN A 203 ? 0.1651 0.1688 0.1328 -0.0211 -0.0257 -0.0035 203 ASN A N   
1667 C CA  . ASN A 203 ? 0.1648 0.1681 0.1284 -0.0228 -0.0266 -0.0032 203 ASN A CA  
1668 C C   . ASN A 203 ? 0.1626 0.1693 0.1276 -0.0244 -0.0287 -0.0002 203 ASN A C   
1669 O O   . ASN A 203 ? 0.1657 0.1731 0.1272 -0.0277 -0.0295 0.0015  203 ASN A O   
1670 C CB  . ASN A 203 ? 0.1660 0.1681 0.1308 -0.0203 -0.0272 -0.0042 203 ASN A CB  
1671 C CG  . ASN A 203 ? 0.1764 0.1755 0.1397 -0.0193 -0.0251 -0.0065 203 ASN A CG  
1672 O OD1 . ASN A 203 ? 0.1717 0.1691 0.1335 -0.0200 -0.0225 -0.0074 203 ASN A OD1 
1673 N ND2 . ASN A 203 ? 0.1763 0.1746 0.1404 -0.0173 -0.0256 -0.0072 203 ASN A ND2 
1674 N N   . VAL A 204 ? 0.1532 0.1617 0.1232 -0.0225 -0.0298 0.0010  204 VAL A N   
1675 C CA  . VAL A 204 ? 0.1539 0.1657 0.1264 -0.0236 -0.0311 0.0045  204 VAL A CA  
1676 C C   . VAL A 204 ? 0.1578 0.1719 0.1285 -0.0274 -0.0312 0.0060  204 VAL A C   
1677 O O   . VAL A 204 ? 0.1647 0.1814 0.1347 -0.0304 -0.0325 0.0092  204 VAL A O   
1678 C CB  . VAL A 204 ? 0.1605 0.1719 0.1374 -0.0207 -0.0318 0.0051  204 VAL A CB  
1679 C CG1 . VAL A 204 ? 0.1644 0.1793 0.1447 -0.0216 -0.0324 0.0092  204 VAL A CG1 
1680 C CG2 . VAL A 204 ? 0.1563 0.1636 0.1325 -0.0172 -0.0317 0.0037  204 VAL A CG2 
1681 N N   . LEU A 205 ? 0.1529 0.1659 0.1227 -0.0275 -0.0297 0.0042  205 LEU A N   
1682 C CA  . LEU A 205 ? 0.1534 0.1676 0.1201 -0.0309 -0.0291 0.0055  205 LEU A CA  
1683 C C   . LEU A 205 ? 0.1627 0.1739 0.1206 -0.0346 -0.0288 0.0051  205 LEU A C   
1684 O O   . LEU A 205 ? 0.1567 0.1691 0.1112 -0.0388 -0.0304 0.0076  205 LEU A O   
1685 C CB  . LEU A 205 ? 0.1561 0.1693 0.1238 -0.0295 -0.0266 0.0043  205 LEU A CB  
1686 C CG  . LEU A 205 ? 0.1609 0.1772 0.1370 -0.0272 -0.0280 0.0057  205 LEU A CG  
1687 C CD1 . LEU A 205 ? 0.1710 0.1866 0.1501 -0.0253 -0.0259 0.0052  205 LEU A CD1 
1688 C CD2 . LEU A 205 ? 0.1744 0.1949 0.1530 -0.0293 -0.0295 0.0089  205 LEU A CD2 
1689 N N   . ALA A 206 ? 0.1654 0.1719 0.1192 -0.0337 -0.0273 0.0021  206 ALA A N   
1690 C CA  . ALA A 206 ? 0.1774 0.1791 0.1214 -0.0376 -0.0273 0.0015  206 ALA A CA  
1691 C C   . ALA A 206 ? 0.1821 0.1871 0.1269 -0.0409 -0.0315 0.0053  206 ALA A C   
1692 O O   . ALA A 206 ? 0.1838 0.1872 0.1217 -0.0462 -0.0334 0.0073  206 ALA A O   
1693 C CB  . ALA A 206 ? 0.1854 0.1822 0.1269 -0.0354 -0.0251 -0.0019 206 ALA A CB  
1694 N N   . TRP A 207 ? 0.1684 0.1778 0.1215 -0.0378 -0.0327 0.0070  207 TRP A N   
1695 C CA  . TRP A 207 ? 0.1712 0.1846 0.1275 -0.0399 -0.0358 0.0120  207 TRP A CA  
1696 C C   . TRP A 207 ? 0.1705 0.1890 0.1298 -0.0430 -0.0378 0.0168  207 TRP A C   
1697 O O   . TRP A 207 ? 0.1798 0.2004 0.1382 -0.0476 -0.0409 0.0215  207 TRP A O   
1698 C CB  . TRP A 207 ? 0.1730 0.1883 0.1366 -0.0347 -0.0352 0.0125  207 TRP A CB  
1699 C CG  . TRP A 207 ? 0.1756 0.1960 0.1455 -0.0349 -0.0368 0.0187  207 TRP A CG  
1700 C CD1 . TRP A 207 ? 0.1911 0.2131 0.1617 -0.0369 -0.0387 0.0226  207 TRP A CD1 
1701 C CD2 . TRP A 207 ? 0.1708 0.1951 0.1482 -0.0323 -0.0362 0.0222  207 TRP A CD2 
1702 N NE1 . TRP A 207 ? 0.1926 0.2200 0.1718 -0.0353 -0.0388 0.0290  207 TRP A NE1 
1703 C CE2 . TRP A 207 ? 0.1823 0.2106 0.1652 -0.0322 -0.0369 0.0286  207 TRP A CE2 
1704 C CE3 . TRP A 207 ? 0.1833 0.2076 0.1635 -0.0297 -0.0349 0.0208  207 TRP A CE3 
1705 C CZ2 . TRP A 207 ? 0.1891 0.2210 0.1800 -0.0292 -0.0355 0.0335  207 TRP A CZ2 
1706 C CZ3 . TRP A 207 ? 0.1929 0.2200 0.1800 -0.0272 -0.0341 0.0251  207 TRP A CZ3 
1707 C CH2 . TRP A 207 ? 0.1892 0.2198 0.1814 -0.0268 -0.0340 0.0314  207 TRP A CH2 
1708 N N   . LEU A 208 ? 0.1624 0.1825 0.1250 -0.0411 -0.0364 0.0160  208 LEU A N   
1709 C CA  . LEU A 208 ? 0.1569 0.1818 0.1222 -0.0441 -0.0381 0.0204  208 LEU A CA  
1710 C C   . LEU A 208 ? 0.1709 0.1928 0.1260 -0.0504 -0.0394 0.0206  208 LEU A C   
1711 O O   . LEU A 208 ? 0.1774 0.2027 0.1324 -0.0554 -0.0427 0.0258  208 LEU A O   
1712 C CB  . LEU A 208 ? 0.1490 0.1754 0.1195 -0.0407 -0.0363 0.0191  208 LEU A CB  
1713 C CG  . LEU A 208 ? 0.1641 0.1919 0.1430 -0.0354 -0.0357 0.0196  208 LEU A CG  
1714 C CD1 . LEU A 208 ? 0.1654 0.1935 0.1482 -0.0330 -0.0348 0.0182  208 LEU A CD1 
1715 C CD2 . LEU A 208 ? 0.1647 0.1975 0.1502 -0.0360 -0.0369 0.0260  208 LEU A CD2 
1716 N N   . TYR A 209 ? 0.1759 0.1907 0.1216 -0.0505 -0.0369 0.0155  209 TYR A N   
1717 C CA  . TYR A 209 ? 0.1880 0.1968 0.1206 -0.0564 -0.0375 0.0150  209 TYR A CA  
1718 C C   . TYR A 209 ? 0.2056 0.2126 0.1332 -0.0617 -0.0417 0.0179  209 TYR A C   
1719 O O   . TYR A 209 ? 0.2150 0.2212 0.1362 -0.0682 -0.0452 0.0215  209 TYR A O   
1720 C CB  . TYR A 209 ? 0.1901 0.1901 0.1135 -0.0545 -0.0327 0.0093  209 TYR A CB  
1721 C CG  . TYR A 209 ? 0.1898 0.1909 0.1153 -0.0518 -0.0291 0.0083  209 TYR A CG  
1722 C CD1 . TYR A 209 ? 0.2026 0.2029 0.1217 -0.0557 -0.0292 0.0102  209 TYR A CD1 
1723 C CD2 . TYR A 209 ? 0.1937 0.1964 0.1272 -0.0457 -0.0258 0.0060  209 TYR A CD2 
1724 C CE1 . TYR A 209 ? 0.2103 0.2121 0.1321 -0.0531 -0.0257 0.0100  209 TYR A CE1 
1725 C CE2 . TYR A 209 ? 0.2039 0.2083 0.1406 -0.0434 -0.0229 0.0063  209 TYR A CE2 
1726 C CZ  . TYR A 209 ? 0.2111 0.2151 0.1421 -0.0469 -0.0226 0.0082  209 TYR A CZ  
1727 O OH  . TYR A 209 ? 0.2235 0.2299 0.1587 -0.0445 -0.0196 0.0092  209 TYR A OH  
1728 N N   . ALA A 210 ? 0.2094 0.2161 0.1404 -0.0591 -0.0418 0.0170  210 ALA A N   
1729 C CA  . ALA A 210 ? 0.2163 0.2224 0.1447 -0.0640 -0.0463 0.0208  210 ALA A CA  
1730 C C   . ALA A 210 ? 0.2209 0.2359 0.1579 -0.0673 -0.0507 0.0291  210 ALA A C   
1731 O O   . ALA A 210 ? 0.2286 0.2430 0.1608 -0.0745 -0.0557 0.0340  210 ALA A O   
1732 C CB  . ALA A 210 ? 0.2153 0.2215 0.1488 -0.0595 -0.0452 0.0192  210 ALA A CB  
1733 N N   . ALA A 211 ? 0.2098 0.2324 0.1593 -0.0624 -0.0491 0.0314  211 ALA A N   
1734 C CA  . ALA A 211 ? 0.2048 0.2362 0.1643 -0.0643 -0.0520 0.0398  211 ALA A CA  
1735 C C   . ALA A 211 ? 0.2108 0.2428 0.1647 -0.0714 -0.0553 0.0430  211 ALA A C   
1736 O O   . ALA A 211 ? 0.2234 0.2590 0.1784 -0.0777 -0.0603 0.0504  211 ALA A O   
1737 C CB  . ALA A 211 ? 0.2027 0.2395 0.1745 -0.0571 -0.0485 0.0402  211 ALA A CB  
1738 N N   . VAL A 212 ? 0.2063 0.2345 0.1535 -0.0709 -0.0527 0.0380  212 VAL A N   
1739 C CA  . VAL A 212 ? 0.2194 0.2472 0.1595 -0.0775 -0.0554 0.0407  212 VAL A CA  
1740 C C   . VAL A 212 ? 0.2499 0.2699 0.1751 -0.0858 -0.0596 0.0415  212 VAL A C   
1741 O O   . VAL A 212 ? 0.2625 0.2852 0.1860 -0.0933 -0.0650 0.0483  212 VAL A O   
1742 C CB  . VAL A 212 ? 0.2233 0.2480 0.1591 -0.0745 -0.0509 0.0353  212 VAL A CB  
1743 C CG1 . VAL A 212 ? 0.2307 0.2533 0.1563 -0.0815 -0.0532 0.0376  212 VAL A CG1 
1744 C CG2 . VAL A 212 ? 0.2217 0.2542 0.1723 -0.0679 -0.0483 0.0360  212 VAL A CG2 
1745 N N   . ILE A 213 ? 0.2661 0.2762 0.1805 -0.0851 -0.0576 0.0352  213 ILE A N   
1746 C CA  . ILE A 213 ? 0.2989 0.2988 0.1967 -0.0932 -0.0615 0.0351  213 ILE A CA  
1747 C C   . ILE A 213 ? 0.3284 0.3341 0.2324 -0.0989 -0.0688 0.0438  213 ILE A C   
1748 O O   . ILE A 213 ? 0.3478 0.3505 0.2427 -0.1081 -0.0749 0.0486  213 ILE A O   
1749 C CB  . ILE A 213 ? 0.3102 0.2991 0.1982 -0.0898 -0.0572 0.0270  213 ILE A CB  
1750 C CG1 . ILE A 213 ? 0.3208 0.3032 0.2015 -0.0853 -0.0501 0.0200  213 ILE A CG1 
1751 C CG2 . ILE A 213 ? 0.3287 0.3063 0.2006 -0.0978 -0.0616 0.0272  213 ILE A CG2 
1752 C CD1 . ILE A 213 ? 0.3387 0.3140 0.2162 -0.0797 -0.0445 0.0132  213 ILE A CD1 
1753 N N   . ASN A 214 ? 0.3286 0.3431 0.2488 -0.0934 -0.0681 0.0468  214 ASN A N   
1754 C CA  . ASN A 214 ? 0.3465 0.3677 0.2756 -0.0973 -0.0738 0.0560  214 ASN A CA  
1755 C C   . ASN A 214 ? 0.3578 0.3920 0.3022 -0.0985 -0.0764 0.0662  214 ASN A C   
1756 O O   . ASN A 214 ? 0.3792 0.4213 0.3358 -0.0992 -0.0794 0.0750  214 ASN A O   
1757 C CB  . ASN A 214 ? 0.3592 0.3819 0.2964 -0.0909 -0.0712 0.0545  214 ASN A CB  
1758 C CG  . ASN A 214 ? 0.4054 0.4159 0.3279 -0.0923 -0.0708 0.0474  214 ASN A CG  
1759 O OD1 . ASN A 214 ? 0.4375 0.4434 0.3529 -0.0994 -0.0763 0.0505  214 ASN A OD1 
1760 N ND2 . ASN A 214 ? 0.4032 0.4076 0.3206 -0.0863 -0.0645 0.0381  214 ASN A ND2 
1761 N N   . GLY A 215 ? 0.3423 0.3787 0.2864 -0.0988 -0.0753 0.0660  215 GLY A N   
1762 C CA  . GLY A 215 ? 0.3281 0.3761 0.2856 -0.1007 -0.0778 0.0759  215 GLY A CA  
1763 C C   . GLY A 215 ? 0.3001 0.3575 0.2753 -0.0920 -0.0726 0.0778  215 GLY A C   
1764 O O   . GLY A 215 ? 0.3024 0.3681 0.2871 -0.0937 -0.0741 0.0852  215 GLY A O   
1765 N N   A ASP A 216 ? 0.2803 0.3359 0.2594 -0.0829 -0.0667 0.0714  216 ASP A N   
1766 N N   B ASP A 216 ? 0.2847 0.3402 0.2637 -0.0830 -0.0668 0.0714  216 ASP A N   
1767 C CA  A ASP A 216 ? 0.2635 0.3253 0.2567 -0.0747 -0.0618 0.0725  216 ASP A CA  
1768 C CA  B ASP A 216 ? 0.2724 0.3339 0.2653 -0.0747 -0.0617 0.0722  216 ASP A CA  
1769 C C   A ASP A 216 ? 0.2716 0.3305 0.2605 -0.0722 -0.0585 0.0655  216 ASP A C   
1770 C C   B ASP A 216 ? 0.2758 0.3346 0.2642 -0.0724 -0.0587 0.0654  216 ASP A C   
1771 O O   A ASP A 216 ? 0.2864 0.3380 0.2669 -0.0689 -0.0555 0.0565  216 ASP A O   
1772 O O   B ASP A 216 ? 0.2909 0.3421 0.2703 -0.0696 -0.0558 0.0564  216 ASP A O   
1773 C CB  A ASP A 216 ? 0.2639 0.3240 0.2621 -0.0669 -0.0575 0.0695  216 ASP A CB  
1774 C CB  B ASP A 216 ? 0.2863 0.3457 0.2833 -0.0669 -0.0574 0.0686  216 ASP A CB  
1775 C CG  A ASP A 216 ? 0.2835 0.3475 0.2882 -0.0685 -0.0600 0.0774  216 ASP A CG  
1776 C CG  B ASP A 216 ? 0.3267 0.3938 0.3393 -0.0629 -0.0559 0.0775  216 ASP A CG  
1777 O OD1 A ASP A 216 ? 0.2790 0.3500 0.2902 -0.0743 -0.0644 0.0877  216 ASP A OD1 
1778 O OD1 B ASP A 216 ? 0.3309 0.4047 0.3535 -0.0626 -0.0554 0.0842  216 ASP A OD1 
1779 O OD2 A ASP A 216 ? 0.2960 0.3567 0.3001 -0.0642 -0.0577 0.0741  216 ASP A OD2 
1780 O OD2 B ASP A 216 ? 0.3469 0.4129 0.3618 -0.0597 -0.0546 0.0781  216 ASP A OD2 
1781 N N   . ARG A 217 ? 0.2585 0.3236 0.2534 -0.0740 -0.0594 0.0705  217 ARG A N   
1782 C CA  . ARG A 217 ? 0.2453 0.3087 0.2367 -0.0726 -0.0572 0.0655  217 ARG A CA  
1783 C C   . ARG A 217 ? 0.2271 0.2973 0.2323 -0.0678 -0.0545 0.0689  217 ARG A C   
1784 O O   . ARG A 217 ? 0.2224 0.2927 0.2263 -0.0675 -0.0535 0.0665  217 ARG A O   
1785 C CB  . ARG A 217 ? 0.2559 0.3186 0.2373 -0.0814 -0.0615 0.0677  217 ARG A CB  
1786 C CG  . ARG A 217 ? 0.2916 0.3465 0.2575 -0.0885 -0.0654 0.0663  217 ARG A CG  
1787 C CD  . ARG A 217 ? 0.3143 0.3693 0.2718 -0.0984 -0.0710 0.0717  217 ARG A CD  
1788 N NE  . ARG A 217 ? 0.3240 0.3770 0.2753 -0.0983 -0.0686 0.0679  217 ARG A NE  
1789 C CZ  . ARG A 217 ? 0.3284 0.3705 0.2620 -0.1002 -0.0669 0.0609  217 ARG A CZ  
1790 N NH1 . ARG A 217 ? 0.3197 0.3610 0.2493 -0.0996 -0.0642 0.0587  217 ARG A NH1 
1791 N NH2 . ARG A 217 ? 0.3159 0.3476 0.2355 -0.1029 -0.0676 0.0567  217 ARG A NH2 
1792 N N   . TRP A 218 ? 0.2159 0.2912 0.2339 -0.0640 -0.0532 0.0750  218 TRP A N   
1793 C CA  . TRP A 218 ? 0.2071 0.2875 0.2374 -0.0597 -0.0503 0.0788  218 TRP A CA  
1794 C C   . TRP A 218 ? 0.2084 0.2834 0.2369 -0.0535 -0.0463 0.0704  218 TRP A C   
1795 O O   . TRP A 218 ? 0.2116 0.2896 0.2469 -0.0518 -0.0450 0.0724  218 TRP A O   
1796 C CB  . TRP A 218 ? 0.1990 0.2837 0.2422 -0.0556 -0.0480 0.0866  218 TRP A CB  
1797 C CG  . TRP A 218 ? 0.1998 0.2781 0.2409 -0.0491 -0.0442 0.0816  218 TRP A CG  
1798 C CD1 . TRP A 218 ? 0.2098 0.2871 0.2488 -0.0499 -0.0453 0.0828  218 TRP A CD1 
1799 C CD2 . TRP A 218 ? 0.2055 0.2774 0.2468 -0.0410 -0.0390 0.0754  218 TRP A CD2 
1800 N NE1 . TRP A 218 ? 0.2152 0.2860 0.2523 -0.0426 -0.0408 0.0770  218 TRP A NE1 
1801 C CE2 . TRP A 218 ? 0.2142 0.2813 0.2523 -0.0373 -0.0370 0.0726  218 TRP A CE2 
1802 C CE3 . TRP A 218 ? 0.2123 0.2814 0.2553 -0.0370 -0.0363 0.0720  218 TRP A CE3 
1803 C CZ2 . TRP A 218 ? 0.2196 0.2788 0.2549 -0.0302 -0.0327 0.0663  218 TRP A CZ2 
1804 C CZ3 . TRP A 218 ? 0.2220 0.2828 0.2621 -0.0302 -0.0323 0.0658  218 TRP A CZ3 
1805 C CH2 . TRP A 218 ? 0.2233 0.2790 0.2592 -0.0270 -0.0306 0.0631  218 TRP A CH2 
1806 N N   . PHE A 219 ? 0.2026 0.2700 0.2228 -0.0503 -0.0446 0.0619  219 PHE A N   
1807 C CA  . PHE A 219 ? 0.1985 0.2603 0.2170 -0.0448 -0.0415 0.0545  219 PHE A CA  
1808 C C   . PHE A 219 ? 0.2102 0.2707 0.2225 -0.0472 -0.0423 0.0502  219 PHE A C   
1809 O O   . PHE A 219 ? 0.2134 0.2706 0.2260 -0.0434 -0.0405 0.0455  219 PHE A O   
1810 C CB  . PHE A 219 ? 0.1881 0.2429 0.2014 -0.0407 -0.0396 0.0485  219 PHE A CB  
1811 C CG  . PHE A 219 ? 0.1796 0.2318 0.1831 -0.0447 -0.0415 0.0455  219 PHE A CG  
1812 C CD1 . PHE A 219 ? 0.1862 0.2342 0.1810 -0.0461 -0.0414 0.0395  219 PHE A CD1 
1813 C CD2 . PHE A 219 ? 0.1759 0.2296 0.1791 -0.0472 -0.0432 0.0495  219 PHE A CD2 
1814 C CE1 . PHE A 219 ? 0.1908 0.2348 0.1755 -0.0497 -0.0425 0.0369  219 PHE A CE1 
1815 C CE2 . PHE A 219 ? 0.1857 0.2356 0.1790 -0.0512 -0.0452 0.0467  219 PHE A CE2 
1816 C CZ  . PHE A 219 ? 0.1871 0.2316 0.1705 -0.0526 -0.0447 0.0402  219 PHE A CZ  
1817 N N   . LEU A 220 ? 0.2060 0.2687 0.2125 -0.0536 -0.0450 0.0522  220 LEU A N   
1818 C CA  . LEU A 220 ? 0.2204 0.2817 0.2208 -0.0556 -0.0448 0.0490  220 LEU A CA  
1819 C C   . LEU A 220 ? 0.2291 0.2963 0.2392 -0.0547 -0.0447 0.0528  220 LEU A C   
1820 O O   . LEU A 220 ? 0.2333 0.3066 0.2522 -0.0558 -0.0460 0.0597  220 LEU A O   
1821 C CB  . LEU A 220 ? 0.2247 0.2850 0.2142 -0.0629 -0.0475 0.0503  220 LEU A CB  
1822 C CG  . LEU A 220 ? 0.2373 0.2904 0.2156 -0.0645 -0.0477 0.0463  220 LEU A CG  
1823 C CD1 . LEU A 220 ? 0.2414 0.2915 0.2069 -0.0725 -0.0507 0.0479  220 LEU A CD1 
1824 C CD2 . LEU A 220 ? 0.2467 0.2928 0.2205 -0.0591 -0.0436 0.0381  220 LEU A CD2 
1825 N N   . ASN A 221 ? 0.2295 0.2950 0.2392 -0.0523 -0.0430 0.0490  221 ASN A N   
1826 C CA  . ASN A 221 ? 0.2248 0.2950 0.2438 -0.0510 -0.0429 0.0521  221 ASN A CA  
1827 C C   . ASN A 221 ? 0.2211 0.2925 0.2365 -0.0531 -0.0427 0.0511  221 ASN A C   
1828 O O   . ASN A 221 ? 0.2310 0.2986 0.2357 -0.0554 -0.0421 0.0482  221 ASN A O   
1829 C CB  . ASN A 221 ? 0.2341 0.3011 0.2598 -0.0448 -0.0412 0.0496  221 ASN A CB  
1830 C CG  . ASN A 221 ? 0.2661 0.3267 0.2866 -0.0417 -0.0398 0.0428  221 ASN A CG  
1831 O OD1 . ASN A 221 ? 0.2607 0.3206 0.2763 -0.0430 -0.0393 0.0405  221 ASN A OD1 
1832 N ND2 . ASN A 221 ? 0.2758 0.3312 0.2975 -0.0375 -0.0390 0.0400  221 ASN A ND2 
1833 N N   . ARG A 222 ? 0.2057 0.2819 0.2299 -0.0522 -0.0429 0.0542  222 ARG A N   
1834 C CA  . ARG A 222 ? 0.2060 0.2843 0.2288 -0.0537 -0.0424 0.0545  222 ARG A CA  
1835 C C   . ARG A 222 ? 0.2006 0.2750 0.2238 -0.0493 -0.0403 0.0498  222 ARG A C   
1836 O O   . ARG A 222 ? 0.2032 0.2802 0.2280 -0.0496 -0.0395 0.0510  222 ARG A O   
1837 C CB  . ARG A 222 ? 0.2137 0.2997 0.2475 -0.0546 -0.0439 0.0607  222 ARG A CB  
1838 C CG  . ARG A 222 ? 0.2546 0.3462 0.2899 -0.0595 -0.0463 0.0672  222 ARG A CG  
1839 C CD  . ARG A 222 ? 0.2858 0.3854 0.3336 -0.0601 -0.0474 0.0740  222 ARG A CD  
1840 N NE  . ARG A 222 ? 0.3103 0.4163 0.3597 -0.0658 -0.0502 0.0815  222 ARG A NE  
1841 C CZ  . ARG A 222 ? 0.3500 0.4591 0.3926 -0.0722 -0.0526 0.0845  222 ARG A CZ  
1842 N NH1 . ARG A 222 ? 0.3476 0.4538 0.3813 -0.0730 -0.0515 0.0807  222 ARG A NH1 
1843 N NH2 . ARG A 222 ? 0.3501 0.4649 0.3946 -0.0780 -0.0560 0.0921  222 ARG A NH2 
1844 N N   . PHE A 223 ? 0.1880 0.2567 0.2104 -0.0456 -0.0395 0.0453  223 PHE A N   
1845 C CA  . PHE A 223 ? 0.1905 0.2561 0.2156 -0.0418 -0.0384 0.0423  223 PHE A CA  
1846 C C   . PHE A 223 ? 0.1685 0.2292 0.1855 -0.0409 -0.0360 0.0381  223 PHE A C   
1847 O O   . PHE A 223 ? 0.1751 0.2326 0.1831 -0.0425 -0.0350 0.0360  223 PHE A O   
1848 C CB  . PHE A 223 ? 0.2060 0.2680 0.2368 -0.0381 -0.0397 0.0409  223 PHE A CB  
1849 C CG  . PHE A 223 ? 0.2286 0.2930 0.2664 -0.0380 -0.0409 0.0447  223 PHE A CG  
1850 C CD1 . PHE A 223 ? 0.2419 0.3129 0.2861 -0.0400 -0.0417 0.0496  223 PHE A CD1 
1851 C CD2 . PHE A 223 ? 0.2490 0.3088 0.2870 -0.0355 -0.0406 0.0437  223 PHE A CD2 
1852 C CE1 . PHE A 223 ? 0.2545 0.3277 0.3060 -0.0396 -0.0421 0.0538  223 PHE A CE1 
1853 C CE2 . PHE A 223 ? 0.2631 0.3243 0.3077 -0.0346 -0.0405 0.0478  223 PHE A CE2 
1854 C CZ  . PHE A 223 ? 0.2589 0.3269 0.3106 -0.0367 -0.0412 0.0529  223 PHE A CZ  
1855 N N   . THR A 224 ? 0.1530 0.2131 0.1741 -0.0383 -0.0350 0.0374  224 THR A N   
1856 C CA  . THR A 224 ? 0.1516 0.2071 0.1683 -0.0362 -0.0324 0.0342  224 THR A CA  
1857 C C   . THR A 224 ? 0.1523 0.2060 0.1769 -0.0330 -0.0344 0.0335  224 THR A C   
1858 O O   . THR A 224 ? 0.1582 0.2130 0.1898 -0.0326 -0.0376 0.0351  224 THR A O   
1859 C CB  . THR A 224 ? 0.1613 0.2174 0.1731 -0.0369 -0.0284 0.0352  224 THR A CB  
1860 O OG1 . THR A 224 ? 0.1594 0.2096 0.1648 -0.0351 -0.0251 0.0318  224 THR A OG1 
1861 C CG2 . THR A 224 ? 0.1625 0.2231 0.1837 -0.0353 -0.0280 0.0390  224 THR A CG2 
1862 N N   . THR A 225 ? 0.1427 0.1930 0.1656 -0.0310 -0.0327 0.0314  225 THR A N   
1863 C CA  . THR A 225 ? 0.1450 0.1933 0.1745 -0.0289 -0.0350 0.0314  225 THR A CA  
1864 C C   . THR A 225 ? 0.1455 0.1935 0.1756 -0.0272 -0.0316 0.0321  225 THR A C   
1865 O O   . THR A 225 ? 0.1403 0.1888 0.1651 -0.0273 -0.0269 0.0323  225 THR A O   
1866 C CB  . THR A 225 ? 0.1737 0.2164 0.2000 -0.0281 -0.0375 0.0279  225 THR A CB  
1867 O OG1 . THR A 225 ? 0.1926 0.2324 0.2239 -0.0269 -0.0407 0.0283  225 THR A OG1 
1868 C CG2 . THR A 225 ? 0.1881 0.2273 0.2060 -0.0277 -0.0349 0.0242  225 THR A CG2 
1869 N N   . THR A 226 ? 0.1469 0.1936 0.1834 -0.0257 -0.0339 0.0332  226 THR A N   
1870 C CA  . THR A 226 ? 0.1483 0.1950 0.1876 -0.0238 -0.0308 0.0348  226 THR A CA  
1871 C C   . THR A 226 ? 0.1535 0.1950 0.1898 -0.0231 -0.0325 0.0314  226 THR A C   
1872 O O   . THR A 226 ? 0.1489 0.1869 0.1823 -0.0239 -0.0365 0.0286  226 THR A O   
1873 C CB  . THR A 226 ? 0.1692 0.2204 0.2212 -0.0234 -0.0332 0.0409  226 THR A CB  
1874 O OG1 . THR A 226 ? 0.1760 0.2243 0.2318 -0.0246 -0.0401 0.0409  226 THR A OG1 
1875 C CG2 . THR A 226 ? 0.1819 0.2387 0.2379 -0.0240 -0.0320 0.0448  226 THR A CG2 
1876 N N   A LEU A 227 ? 0.1551 0.1958 0.1924 -0.0213 -0.0291 0.0321  227 LEU A N   
1877 N N   B LEU A 227 ? 0.1515 0.1922 0.1888 -0.0213 -0.0291 0.0321  227 LEU A N   
1878 C CA  A LEU A 227 ? 0.1694 0.2059 0.2049 -0.0206 -0.0308 0.0296  227 LEU A CA  
1879 C CA  B LEU A 227 ? 0.1621 0.1985 0.1977 -0.0207 -0.0310 0.0295  227 LEU A CA  
1880 C C   A LEU A 227 ? 0.1749 0.2099 0.2162 -0.0218 -0.0380 0.0311  227 LEU A C   
1881 C C   B LEU A 227 ? 0.1711 0.2060 0.2123 -0.0219 -0.0382 0.0311  227 LEU A C   
1882 O O   A LEU A 227 ? 0.1842 0.2140 0.2200 -0.0224 -0.0412 0.0274  227 LEU A O   
1883 O O   B LEU A 227 ? 0.1795 0.2093 0.2152 -0.0225 -0.0414 0.0273  227 LEU A O   
1884 C CB  A LEU A 227 ? 0.1732 0.2100 0.2112 -0.0183 -0.0254 0.0317  227 LEU A CB  
1885 C CB  B LEU A 227 ? 0.1603 0.1969 0.1982 -0.0184 -0.0260 0.0314  227 LEU A CB  
1886 C CG  A LEU A 227 ? 0.1952 0.2274 0.2273 -0.0174 -0.0240 0.0278  227 LEU A CG  
1887 C CG  B LEU A 227 ? 0.1740 0.2074 0.2019 -0.0174 -0.0192 0.0279  227 LEU A CG  
1888 C CD1 A LEU A 227 ? 0.2069 0.2351 0.2268 -0.0185 -0.0232 0.0217  227 LEU A CD1 
1889 C CD1 B LEU A 227 ? 0.1720 0.2045 0.2030 -0.0146 -0.0141 0.0300  227 LEU A CD1 
1890 C CD2 A LEU A 227 ? 0.1975 0.2297 0.2314 -0.0147 -0.0170 0.0301  227 LEU A CD2 
1891 C CD2 B LEU A 227 ? 0.1864 0.2153 0.2040 -0.0187 -0.0211 0.0218  227 LEU A CD2 
1892 N N   . ASN A 228 ? 0.1664 0.2052 0.2179 -0.0225 -0.0408 0.0368  228 ASN A N   
1893 C CA  . ASN A 228 ? 0.1596 0.1953 0.2151 -0.0245 -0.0486 0.0386  228 ASN A CA  
1894 C C   . ASN A 228 ? 0.1620 0.1930 0.2114 -0.0260 -0.0525 0.0350  228 ASN A C   
1895 O O   . ASN A 228 ? 0.1794 0.2032 0.2243 -0.0271 -0.0572 0.0328  228 ASN A O   
1896 C CB  . ASN A 228 ? 0.1641 0.2053 0.2327 -0.0253 -0.0510 0.0464  228 ASN A CB  
1897 C CG  . ASN A 228 ? 0.2077 0.2526 0.2841 -0.0237 -0.0480 0.0514  228 ASN A CG  
1898 O OD1 . ASN A 228 ? 0.2288 0.2799 0.3169 -0.0233 -0.0473 0.0588  228 ASN A OD1 
1899 N ND2 . ASN A 228 ? 0.2169 0.2585 0.2882 -0.0226 -0.0459 0.0482  228 ASN A ND2 
1900 N N   . ASP A 229 ? 0.1556 0.1898 0.2042 -0.0260 -0.0501 0.0347  229 ASP A N   
1901 C CA  . ASP A 229 ? 0.1631 0.1932 0.2073 -0.0269 -0.0529 0.0323  229 ASP A CA  
1902 C C   . ASP A 229 ? 0.1704 0.1950 0.2044 -0.0259 -0.0513 0.0267  229 ASP A C   
1903 O O   . ASP A 229 ? 0.1840 0.2011 0.2132 -0.0261 -0.0544 0.0245  229 ASP A O   
1904 C CB  . ASP A 229 ? 0.1876 0.2237 0.2347 -0.0273 -0.0507 0.0342  229 ASP A CB  
1905 C CG  . ASP A 229 ? 0.2696 0.3018 0.3131 -0.0278 -0.0525 0.0323  229 ASP A CG  
1906 O OD1 . ASP A 229 ? 0.2930 0.3199 0.3380 -0.0287 -0.0572 0.0331  229 ASP A OD1 
1907 O OD2 . ASP A 229 ? 0.2923 0.3257 0.3308 -0.0273 -0.0492 0.0302  229 ASP A OD2 
1908 N N   . PHE A 230 ? 0.1635 0.1907 0.1935 -0.0249 -0.0463 0.0247  230 PHE A N   
1909 C CA  . PHE A 230 ? 0.1676 0.1905 0.1891 -0.0240 -0.0449 0.0203  230 PHE A CA  
1910 C C   . PHE A 230 ? 0.1813 0.1975 0.2000 -0.0235 -0.0479 0.0184  230 PHE A C   
1911 O O   . PHE A 230 ? 0.1952 0.2052 0.2080 -0.0229 -0.0491 0.0157  230 PHE A O   
1912 C CB  . PHE A 230 ? 0.1586 0.1845 0.1762 -0.0236 -0.0398 0.0189  230 PHE A CB  
1913 C CG  . PHE A 230 ? 0.1754 0.1973 0.1855 -0.0229 -0.0389 0.0150  230 PHE A CG  
1914 C CD1 . PHE A 230 ? 0.1837 0.2056 0.1905 -0.0233 -0.0387 0.0144  230 PHE A CD1 
1915 C CD2 . PHE A 230 ? 0.1914 0.2097 0.1991 -0.0218 -0.0389 0.0129  230 PHE A CD2 
1916 C CE1 . PHE A 230 ? 0.2018 0.2204 0.2030 -0.0225 -0.0380 0.0119  230 PHE A CE1 
1917 C CE2 . PHE A 230 ? 0.2005 0.2151 0.2019 -0.0210 -0.0385 0.0099  230 PHE A CE2 
1918 C CZ  . PHE A 230 ? 0.2073 0.2221 0.2056 -0.0212 -0.0379 0.0095  230 PHE A CZ  
1919 N N   . ASN A 231 ? 0.1764 0.1935 0.1998 -0.0237 -0.0491 0.0205  231 ASN A N   
1920 C CA  . ASN A 231 ? 0.1851 0.1963 0.2061 -0.0239 -0.0525 0.0195  231 ASN A CA  
1921 C C   . ASN A 231 ? 0.2076 0.2110 0.2259 -0.0255 -0.0585 0.0195  231 ASN A C   
1922 O O   . ASN A 231 ? 0.2219 0.2178 0.2334 -0.0255 -0.0607 0.0170  231 ASN A O   
1923 C CB  . ASN A 231 ? 0.1929 0.2078 0.2210 -0.0240 -0.0523 0.0231  231 ASN A CB  
1924 C CG  . ASN A 231 ? 0.2152 0.2331 0.2414 -0.0220 -0.0461 0.0213  231 ASN A CG  
1925 O OD1 . ASN A 231 ? 0.2253 0.2409 0.2436 -0.0211 -0.0436 0.0169  231 ASN A OD1 
1926 N ND2 . ASN A 231 ? 0.2279 0.2506 0.2612 -0.0211 -0.0431 0.0250  231 ASN A ND2 
1927 N N   . LEU A 232 ? 0.2152 0.2191 0.2374 -0.0267 -0.0609 0.0220  232 LEU A N   
1928 C CA  . LEU A 232 ? 0.2396 0.2337 0.2569 -0.0283 -0.0662 0.0214  232 LEU A CA  
1929 C C   . LEU A 232 ? 0.2511 0.2382 0.2580 -0.0261 -0.0634 0.0166  232 LEU A C   
1930 O O   . LEU A 232 ? 0.2721 0.2482 0.2700 -0.0262 -0.0658 0.0142  232 LEU A O   
1931 C CB  . LEU A 232 ? 0.2564 0.2531 0.2805 -0.0298 -0.0684 0.0250  232 LEU A CB  
1932 C CG  . LEU A 232 ? 0.2869 0.2897 0.3222 -0.0320 -0.0719 0.0310  232 LEU A CG  
1933 C CD1 . LEU A 232 ? 0.2982 0.3035 0.3398 -0.0333 -0.0739 0.0345  232 LEU A CD1 
1934 C CD2 . LEU A 232 ? 0.3027 0.2980 0.3364 -0.0349 -0.0789 0.0327  232 LEU A CD2 
1935 N N   . VAL A 233 ? 0.2402 0.2334 0.2479 -0.0243 -0.0580 0.0157  233 VAL A N   
1936 C CA  . VAL A 233 ? 0.2420 0.2309 0.2424 -0.0220 -0.0547 0.0128  233 VAL A CA  
1937 C C   . VAL A 233 ? 0.2444 0.2304 0.2386 -0.0206 -0.0531 0.0097  233 VAL A C   
1938 O O   . VAL A 233 ? 0.2544 0.2316 0.2405 -0.0190 -0.0528 0.0074  233 VAL A O   
1939 C CB  . VAL A 233 ? 0.2538 0.2514 0.2584 -0.0214 -0.0505 0.0142  233 VAL A CB  
1940 C CG1 . VAL A 233 ? 0.2676 0.2618 0.2668 -0.0191 -0.0471 0.0128  233 VAL A CG1 
1941 C CG2 . VAL A 233 ? 0.2610 0.2616 0.2722 -0.0228 -0.0521 0.0175  233 VAL A CG2 
1942 N N   . ALA A 234 ? 0.2379 0.2302 0.2354 -0.0209 -0.0520 0.0099  234 ALA A N   
1943 C CA  . ALA A 234 ? 0.2521 0.2423 0.2446 -0.0197 -0.0506 0.0073  234 ALA A CA  
1944 C C   . ALA A 234 ? 0.2700 0.2501 0.2564 -0.0201 -0.0549 0.0061  234 ALA A C   
1945 O O   . ALA A 234 ? 0.2737 0.2472 0.2521 -0.0185 -0.0538 0.0034  234 ALA A O   
1946 C CB  . ALA A 234 ? 0.2534 0.2510 0.2511 -0.0201 -0.0488 0.0082  234 ALA A CB  
1947 N N   . MET A 235 ? 0.2708 0.2489 0.2605 -0.0227 -0.0599 0.0085  235 MET A N   
1948 C CA  . MET A 235 ? 0.2833 0.2506 0.2661 -0.0244 -0.0653 0.0080  235 MET A CA  
1949 C C   . MET A 235 ? 0.2748 0.2297 0.2458 -0.0231 -0.0651 0.0050  235 MET A C   
1950 O O   . MET A 235 ? 0.2808 0.2267 0.2418 -0.0223 -0.0654 0.0024  235 MET A O   
1951 C CB  . MET A 235 ? 0.3132 0.2810 0.3027 -0.0282 -0.0716 0.0124  235 MET A CB  
1952 C CG  . MET A 235 ? 0.3926 0.3474 0.3734 -0.0313 -0.0786 0.0124  235 MET A CG  
1953 S SD  . MET A 235 ? 0.5622 0.5196 0.5473 -0.0340 -0.0831 0.0157  235 MET A SD  
1954 C CE  . MET A 235 ? 0.5082 0.4783 0.5112 -0.0362 -0.0851 0.0231  235 MET A CE  
1955 N N   . LYS A 236 ? 0.2583 0.2127 0.2306 -0.0226 -0.0639 0.0057  236 LYS A N   
1956 C CA  . LYS A 236 ? 0.2595 0.2016 0.2215 -0.0208 -0.0625 0.0036  236 LYS A CA  
1957 C C   . LYS A 236 ? 0.2555 0.1957 0.2112 -0.0167 -0.0566 0.0010  236 LYS A C   
1958 O O   . LYS A 236 ? 0.2773 0.2045 0.2214 -0.0149 -0.0556 -0.0012 236 LYS A O   
1959 C CB  . LYS A 236 ? 0.2939 0.2384 0.2613 -0.0207 -0.0616 0.0056  236 LYS A CB  
1960 C CG  . LYS A 236 ? 0.3727 0.3048 0.3307 -0.0180 -0.0586 0.0042  236 LYS A CG  
1961 C CD  . LYS A 236 ? 0.4508 0.3874 0.4161 -0.0177 -0.0569 0.0068  236 LYS A CD  
1962 C CE  . LYS A 236 ? 0.5137 0.4397 0.4715 -0.0139 -0.0519 0.0061  236 LYS A CE  
1963 N NZ  . LYS A 236 ? 0.5567 0.4634 0.5015 -0.0148 -0.0550 0.0042  236 LYS A NZ  
1964 N N   . TYR A 237 ? 0.2267 0.1790 0.1895 -0.0153 -0.0527 0.0015  237 TYR A N   
1965 C CA  . TYR A 237 ? 0.2168 0.1692 0.1758 -0.0118 -0.0474 0.0002  237 TYR A CA  
1966 C C   . TYR A 237 ? 0.2196 0.1729 0.1759 -0.0114 -0.0473 -0.0016 237 TYR A C   
1967 O O   . TYR A 237 ? 0.2282 0.1848 0.1841 -0.0089 -0.0431 -0.0019 237 TYR A O   
1968 C CB  . TYR A 237 ? 0.2073 0.1712 0.1748 -0.0110 -0.0433 0.0026  237 TYR A CB  
1969 C CG  . TYR A 237 ? 0.2211 0.1826 0.1900 -0.0101 -0.0420 0.0047  237 TYR A CG  
1970 C CD1 . TYR A 237 ? 0.2387 0.1928 0.2023 -0.0065 -0.0377 0.0051  237 TYR A CD1 
1971 C CD2 . TYR A 237 ? 0.2272 0.1928 0.2027 -0.0126 -0.0446 0.0066  237 TYR A CD2 
1972 C CE1 . TYR A 237 ? 0.2503 0.2010 0.2152 -0.0053 -0.0360 0.0073  237 TYR A CE1 
1973 C CE2 . TYR A 237 ? 0.2339 0.1968 0.2108 -0.0118 -0.0434 0.0086  237 TYR A CE2 
1974 C CZ  . TYR A 237 ? 0.2574 0.2123 0.2289 -0.0082 -0.0391 0.0089  237 TYR A CZ  
1975 O OH  . TYR A 237 ? 0.2769 0.2289 0.2504 -0.0070 -0.0372 0.0114  237 TYR A OH  
1976 N N   A ASN A 238 ? 0.2175 0.1685 0.1729 -0.0140 -0.0520 -0.0021 238 ASN A N   
1977 N N   B ASN A 238 ? 0.2148 0.1657 0.1700 -0.0140 -0.0520 -0.0021 238 ASN A N   
1978 C CA  A ASN A 238 ? 0.2240 0.1759 0.1775 -0.0138 -0.0523 -0.0033 238 ASN A CA  
1979 C CA  B ASN A 238 ? 0.2182 0.1701 0.1718 -0.0139 -0.0524 -0.0033 238 ASN A CA  
1980 C C   A ASN A 238 ? 0.2143 0.1785 0.1758 -0.0131 -0.0487 -0.0028 238 ASN A C   
1981 C C   B ASN A 238 ? 0.2122 0.1765 0.1739 -0.0133 -0.0489 -0.0028 238 ASN A C   
1982 O O   A ASN A 238 ? 0.2159 0.1809 0.1749 -0.0112 -0.0459 -0.0041 238 ASN A O   
1983 O O   B ASN A 238 ? 0.2144 0.1796 0.1739 -0.0117 -0.0466 -0.0041 238 ASN A O   
1984 C CB  A ASN A 238 ? 0.2562 0.1969 0.1976 -0.0112 -0.0506 -0.0057 238 ASN A CB  
1985 C CB  B ASN A 238 ? 0.2416 0.1827 0.1832 -0.0114 -0.0508 -0.0057 238 ASN A CB  
1986 C CG  A ASN A 238 ? 0.3145 0.2403 0.2451 -0.0126 -0.0546 -0.0066 238 ASN A CG  
1987 C CG  B ASN A 238 ? 0.2820 0.2082 0.2124 -0.0131 -0.0554 -0.0067 238 ASN A CG  
1988 O OD1 A ASN A 238 ? 0.3377 0.2533 0.2598 -0.0103 -0.0521 -0.0075 238 ASN A OD1 
1989 O OD1 B ASN A 238 ? 0.2879 0.2122 0.2202 -0.0168 -0.0609 -0.0053 238 ASN A OD1 
1990 N ND2 A ASN A 238 ? 0.3215 0.2452 0.2521 -0.0167 -0.0611 -0.0058 238 ASN A ND2 
1991 N ND2 B ASN A 238 ? 0.2978 0.2124 0.2157 -0.0105 -0.0534 -0.0089 238 ASN A ND2 
1992 N N   . TYR A 239 ? 0.2042 0.1771 0.1744 -0.0147 -0.0485 -0.0008 239 TYR A N   
1993 C CA  . TYR A 239 ? 0.2014 0.1840 0.1775 -0.0147 -0.0454 -0.0004 239 TYR A CA  
1994 C C   . TYR A 239 ? 0.2074 0.1933 0.1890 -0.0165 -0.0474 0.0010  239 TYR A C   
1995 O O   . TYR A 239 ? 0.2147 0.1986 0.1987 -0.0183 -0.0514 0.0029  239 TYR A O   
1996 C CB  . TYR A 239 ? 0.1953 0.1844 0.1764 -0.0154 -0.0435 0.0014  239 TYR A CB  
1997 C CG  . TYR A 239 ? 0.1940 0.1846 0.1730 -0.0140 -0.0401 0.0013  239 TYR A CG  
1998 C CD1 . TYR A 239 ? 0.2026 0.1870 0.1769 -0.0118 -0.0394 0.0012  239 TYR A CD1 
1999 C CD2 . TYR A 239 ? 0.1911 0.1889 0.1728 -0.0151 -0.0376 0.0022  239 TYR A CD2 
2000 C CE1 . TYR A 239 ? 0.2095 0.1964 0.1839 -0.0104 -0.0361 0.0026  239 TYR A CE1 
2001 C CE2 . TYR A 239 ? 0.1965 0.1964 0.1773 -0.0146 -0.0355 0.0034  239 TYR A CE2 
2002 C CZ  . TYR A 239 ? 0.2094 0.2047 0.1877 -0.0121 -0.0347 0.0041  239 TYR A CZ  
2003 O OH  . TYR A 239 ? 0.2142 0.2126 0.1936 -0.0115 -0.0324 0.0067  239 TYR A OH  
2004 N N   A GLU A 240 ? 0.2031 0.1938 0.1870 -0.0160 -0.0446 0.0006  240 GLU A N   
2005 N N   B GLU A 240 ? 0.2060 0.1969 0.1900 -0.0160 -0.0446 0.0006  240 GLU A N   
2006 C CA  A GLU A 240 ? 0.2106 0.2050 0.2009 -0.0169 -0.0451 0.0028  240 GLU A CA  
2007 C CA  B GLU A 240 ? 0.2154 0.2099 0.2058 -0.0169 -0.0450 0.0028  240 GLU A CA  
2008 C C   A GLU A 240 ? 0.2090 0.2088 0.2064 -0.0180 -0.0444 0.0058  240 GLU A C   
2009 C C   B GLU A 240 ? 0.2113 0.2111 0.2087 -0.0180 -0.0444 0.0058  240 GLU A C   
2010 O O   A GLU A 240 ? 0.1989 0.2015 0.1956 -0.0179 -0.0417 0.0053  240 GLU A O   
2011 O O   B GLU A 240 ? 0.2011 0.2037 0.1979 -0.0179 -0.0417 0.0053  240 GLU A O   
2012 C CB  A GLU A 240 ? 0.2421 0.2394 0.2322 -0.0157 -0.0409 0.0014  240 GLU A CB  
2013 C CB  B GLU A 240 ? 0.2550 0.2526 0.2454 -0.0157 -0.0408 0.0015  240 GLU A CB  
2014 C CG  A GLU A 240 ? 0.2988 0.2918 0.2839 -0.0147 -0.0418 -0.0006 240 GLU A CG  
2015 C CG  B GLU A 240 ? 0.3326 0.3262 0.3190 -0.0149 -0.0418 -0.0001 240 GLU A CG  
2016 C CD  A GLU A 240 ? 0.3616 0.3521 0.3489 -0.0158 -0.0460 0.0013  240 GLU A CD  
2017 C CD  B GLU A 240 ? 0.4209 0.4175 0.4091 -0.0139 -0.0381 -0.0006 240 GLU A CD  
2018 O OE1 A GLU A 240 ? 0.3622 0.3567 0.3563 -0.0160 -0.0451 0.0038  240 GLU A OE1 
2019 O OE1 B GLU A 240 ? 0.4450 0.4433 0.4308 -0.0135 -0.0343 -0.0022 240 GLU A OE1 
2020 O OE2 A GLU A 240 ? 0.3858 0.3697 0.3677 -0.0165 -0.0502 0.0008  240 GLU A OE2 
2021 O OE2 B GLU A 240 ? 0.4574 0.4543 0.4493 -0.0140 -0.0390 0.0010  240 GLU A OE2 
2022 N N   . PRO A 241 ? 0.2153 0.2168 0.2193 -0.0191 -0.0466 0.0092  241 PRO A N   
2023 C CA  . PRO A 241 ? 0.2227 0.2298 0.2344 -0.0196 -0.0454 0.0129  241 PRO A CA  
2024 C C   . PRO A 241 ? 0.2198 0.2315 0.2320 -0.0182 -0.0387 0.0124  241 PRO A C   
2025 O O   . PRO A 241 ? 0.2329 0.2443 0.2441 -0.0171 -0.0359 0.0115  241 PRO A O   
2026 C CB  . PRO A 241 ? 0.2383 0.2473 0.2589 -0.0208 -0.0485 0.0182  241 PRO A CB  
2027 C CG  . PRO A 241 ? 0.2465 0.2487 0.2620 -0.0222 -0.0542 0.0169  241 PRO A CG  
2028 C CD  . PRO A 241 ? 0.2168 0.2155 0.2229 -0.0203 -0.0511 0.0114  241 PRO A CD  
2029 N N   . LEU A 242 ? 0.2081 0.2229 0.2211 -0.0185 -0.0365 0.0132  242 LEU A N   
2030 C CA  . LEU A 242 ? 0.2160 0.2329 0.2268 -0.0176 -0.0302 0.0127  242 LEU A CA  
2031 C C   . LEU A 242 ? 0.2124 0.2329 0.2316 -0.0165 -0.0271 0.0175  242 LEU A C   
2032 O O   . LEU A 242 ? 0.2108 0.2343 0.2374 -0.0171 -0.0297 0.0215  242 LEU A O   
2033 C CB  . LEU A 242 ? 0.2211 0.2391 0.2274 -0.0188 -0.0292 0.0115  242 LEU A CB  
2034 C CG  . LEU A 242 ? 0.2425 0.2597 0.2415 -0.0191 -0.0240 0.0096  242 LEU A CG  
2035 C CD1 . LEU A 242 ? 0.2550 0.2685 0.2468 -0.0192 -0.0238 0.0058  242 LEU A CD1 
2036 C CD2 . LEU A 242 ? 0.2458 0.2652 0.2423 -0.0210 -0.0238 0.0103  242 LEU A CD2 
2037 N N   . THR A 243 ? 0.2176 0.2371 0.2353 -0.0148 -0.0216 0.0171  243 THR A N   
2038 C CA  . THR A 243 ? 0.2205 0.2427 0.2461 -0.0129 -0.0169 0.0223  243 THR A CA  
2039 C C   . THR A 243 ? 0.2288 0.2496 0.2482 -0.0118 -0.0094 0.0215  243 THR A C   
2040 O O   . THR A 243 ? 0.2298 0.2470 0.2382 -0.0132 -0.0085 0.0168  243 THR A O   
2041 C CB  . THR A 243 ? 0.2302 0.2515 0.2595 -0.0111 -0.0150 0.0234  243 THR A CB  
2042 O OG1 . THR A 243 ? 0.2306 0.2470 0.2500 -0.0103 -0.0103 0.0186  243 THR A OG1 
2043 C CG2 . THR A 243 ? 0.2434 0.2647 0.2764 -0.0127 -0.0225 0.0239  243 THR A CG2 
2044 N N   . GLN A 244 ? 0.2287 0.2517 0.2550 -0.0095 -0.0042 0.0267  244 GLN A N   
2045 C CA  . GLN A 244 ? 0.2356 0.2551 0.2540 -0.0081 0.0041  0.0261  244 GLN A CA  
2046 C C   . GLN A 244 ? 0.2382 0.2500 0.2454 -0.0073 0.0089  0.0213  244 GLN A C   
2047 O O   . GLN A 244 ? 0.2468 0.2530 0.2417 -0.0083 0.0125  0.0179  244 GLN A O   
2048 C CB  . GLN A 244 ? 0.2529 0.2757 0.2816 -0.0048 0.0101  0.0335  244 GLN A CB  
2049 C CG  . GLN A 244 ? 0.3001 0.3180 0.3193 -0.0031 0.0191  0.0332  244 GLN A CG  
2050 C CD  . GLN A 244 ? 0.3381 0.3566 0.3501 -0.0062 0.0161  0.0309  244 GLN A CD  
2051 O OE1 . GLN A 244 ? 0.3514 0.3767 0.3719 -0.0076 0.0105  0.0337  244 GLN A OE1 
2052 N NE2 . GLN A 244 ? 0.3302 0.3412 0.3261 -0.0076 0.0196  0.0259  244 GLN A NE2 
2053 N N   . ASP A 245 ? 0.2271 0.2384 0.2386 -0.0060 0.0086  0.0214  245 ASP A N   
2054 C CA  . ASP A 245 ? 0.2274 0.2313 0.2287 -0.0056 0.0124  0.0166  245 ASP A CA  
2055 C C   . ASP A 245 ? 0.2178 0.2185 0.2068 -0.0093 0.0079  0.0104  245 ASP A C   
2056 O O   . ASP A 245 ? 0.2251 0.2189 0.2021 -0.0101 0.0116  0.0070  245 ASP A O   
2057 C CB  . ASP A 245 ? 0.2592 0.2649 0.2687 -0.0042 0.0107  0.0180  245 ASP A CB  
2058 C CG  . ASP A 245 ? 0.3428 0.3489 0.3613 -0.0002 0.0180  0.0237  245 ASP A CG  
2059 O OD1 . ASP A 245 ? 0.3544 0.3601 0.3744 0.0020  0.0244  0.0273  245 ASP A OD1 
2060 O OD2 . ASP A 245 ? 0.3785 0.3852 0.4024 0.0008  0.0174  0.0248  245 ASP A OD2 
2061 N N   . HIS A 246 ? 0.2032 0.2084 0.1955 -0.0114 0.0000  0.0096  246 HIS A N   
2062 C CA  . HIS A 246 ? 0.2009 0.2041 0.1837 -0.0146 -0.0039 0.0052  246 HIS A CA  
2063 C C   . HIS A 246 ? 0.2030 0.2044 0.1775 -0.0167 -0.0019 0.0047  246 HIS A C   
2064 O O   . HIS A 246 ? 0.2037 0.2007 0.1676 -0.0192 -0.0020 0.0017  246 HIS A O   
2065 C CB  . HIS A 246 ? 0.2012 0.2089 0.1896 -0.0157 -0.0114 0.0055  246 HIS A CB  
2066 C CG  . HIS A 246 ? 0.2251 0.2332 0.2186 -0.0144 -0.0143 0.0054  246 HIS A CG  
2067 N ND1 . HIS A 246 ? 0.2381 0.2491 0.2389 -0.0146 -0.0197 0.0075  246 HIS A ND1 
2068 C CD2 . HIS A 246 ? 0.2434 0.2488 0.2352 -0.0134 -0.0129 0.0037  246 HIS A CD2 
2069 C CE1 . HIS A 246 ? 0.2470 0.2568 0.2495 -0.0138 -0.0215 0.0070  246 HIS A CE1 
2070 N NE2 . HIS A 246 ? 0.2537 0.2608 0.2516 -0.0129 -0.0174 0.0048  246 HIS A NE2 
2071 N N   . VAL A 247 ? 0.2002 0.2054 0.1801 -0.0161 -0.0010 0.0083  247 VAL A N   
2072 C CA  . VAL A 247 ? 0.2044 0.2082 0.1767 -0.0182 0.0010  0.0085  247 VAL A CA  
2073 C C   . VAL A 247 ? 0.2190 0.2136 0.1784 -0.0181 0.0082  0.0065  247 VAL A C   
2074 O O   . VAL A 247 ? 0.2279 0.2181 0.1753 -0.0215 0.0078  0.0042  247 VAL A O   
2075 C CB  . VAL A 247 ? 0.2085 0.2181 0.1902 -0.0168 0.0018  0.0134  247 VAL A CB  
2076 C CG1 . VAL A 247 ? 0.2220 0.2293 0.1947 -0.0186 0.0050  0.0137  247 VAL A CG1 
2077 C CG2 . VAL A 247 ? 0.2124 0.2290 0.2044 -0.0177 -0.0057 0.0150  247 VAL A CG2 
2078 N N   . ASP A 248 ? 0.2240 0.2157 0.1861 -0.0143 0.0144  0.0078  248 ASP A N   
2079 C CA  . ASP A 248 ? 0.2398 0.2205 0.1885 -0.0134 0.0226  0.0058  248 ASP A CA  
2080 C C   . ASP A 248 ? 0.2470 0.2205 0.1838 -0.0164 0.0205  0.0006  248 ASP A C   
2081 O O   . ASP A 248 ? 0.2636 0.2275 0.1848 -0.0189 0.0234  -0.0021 248 ASP A O   
2082 C CB  . ASP A 248 ? 0.2546 0.2342 0.2111 -0.0081 0.0302  0.0092  248 ASP A CB  
2083 C CG  . ASP A 248 ? 0.2938 0.2793 0.2610 -0.0051 0.0336  0.0155  248 ASP A CG  
2084 O OD1 . ASP A 248 ? 0.3003 0.2881 0.2652 -0.0070 0.0318  0.0162  248 ASP A OD1 
2085 O OD2 . ASP A 248 ? 0.3247 0.3128 0.3031 -0.0010 0.0376  0.0200  248 ASP A OD2 
2086 N N   . ILE A 249 ? 0.2398 0.2176 0.1835 -0.0165 0.0152  -0.0006 249 ILE A N   
2087 C CA  . ILE A 249 ? 0.2522 0.2245 0.1865 -0.0193 0.0126  -0.0048 249 ILE A CA  
2088 C C   . ILE A 249 ? 0.2467 0.2183 0.1717 -0.0247 0.0074  -0.0062 249 ILE A C   
2089 O O   . ILE A 249 ? 0.2569 0.2212 0.1701 -0.0279 0.0069  -0.0089 249 ILE A O   
2090 C CB  . ILE A 249 ? 0.2738 0.2517 0.2187 -0.0177 0.0083  -0.0049 249 ILE A CB  
2091 C CG1 . ILE A 249 ? 0.2886 0.2655 0.2407 -0.0132 0.0136  -0.0033 249 ILE A CG1 
2092 C CG2 . ILE A 249 ? 0.2960 0.2709 0.2335 -0.0209 0.0042  -0.0082 249 ILE A CG2 
2093 C CD1 . ILE A 249 ? 0.3018 0.2864 0.2672 -0.0115 0.0089  -0.0017 249 ILE A CD1 
2094 N N   . LEU A 250 ? 0.2261 0.2054 0.1573 -0.0259 0.0032  -0.0039 250 LEU A N   
2095 C CA  . LEU A 250 ? 0.2291 0.2096 0.1540 -0.0310 -0.0018 -0.0037 250 LEU A CA  
2096 C C   . LEU A 250 ? 0.2518 0.2255 0.1636 -0.0339 0.0017  -0.0036 250 LEU A C   
2097 O O   . LEU A 250 ? 0.2569 0.2306 0.1623 -0.0388 -0.0024 -0.0030 250 LEU A O   
2098 C CB  . LEU A 250 ? 0.2045 0.1956 0.1420 -0.0306 -0.0071 -0.0010 250 LEU A CB  
2099 C CG  . LEU A 250 ? 0.1998 0.1957 0.1467 -0.0288 -0.0113 -0.0014 250 LEU A CG  
2100 C CD1 . LEU A 250 ? 0.1986 0.2022 0.1567 -0.0275 -0.0148 0.0013  250 LEU A CD1 
2101 C CD2 . LEU A 250 ? 0.2085 0.2031 0.1500 -0.0320 -0.0152 -0.0024 250 LEU A CD2 
2102 N N   . GLY A 251 ? 0.2570 0.2248 0.1650 -0.0307 0.0094  -0.0036 251 GLY A N   
2103 C CA  . GLY A 251 ? 0.2790 0.2382 0.1725 -0.0327 0.0142  -0.0036 251 GLY A CA  
2104 C C   . GLY A 251 ? 0.3006 0.2497 0.1753 -0.0393 0.0116  -0.0062 251 GLY A C   
2105 O O   . GLY A 251 ? 0.3064 0.2557 0.1743 -0.0440 0.0085  -0.0049 251 GLY A O   
2106 N N   . PRO A 252 ? 0.3063 0.2471 0.1729 -0.0404 0.0118  -0.0095 252 PRO A N   
2107 C CA  . PRO A 252 ? 0.3173 0.2481 0.1658 -0.0477 0.0081  -0.0113 252 PRO A CA  
2108 C C   . PRO A 252 ? 0.3076 0.2475 0.1604 -0.0534 -0.0017 -0.0086 252 PRO A C   
2109 O O   . PRO A 252 ? 0.3219 0.2563 0.1613 -0.0599 -0.0047 -0.0078 252 PRO A O   
2110 C CB  . PRO A 252 ? 0.3331 0.2562 0.1776 -0.0468 0.0095  -0.0146 252 PRO A CB  
2111 C CG  . PRO A 252 ? 0.3405 0.2637 0.1935 -0.0389 0.0180  -0.0148 252 PRO A CG  
2112 C CD  . PRO A 252 ? 0.3076 0.2467 0.1802 -0.0356 0.0156  -0.0111 252 PRO A CD  
2113 N N   . LEU A 253 ? 0.2874 0.2407 0.1582 -0.0512 -0.0065 -0.0066 253 LEU A N   
2114 C CA  . LEU A 253 ? 0.2797 0.2418 0.1560 -0.0557 -0.0145 -0.0031 253 LEU A CA  
2115 C C   . LEU A 253 ? 0.2847 0.2525 0.1635 -0.0570 -0.0153 0.0001  253 LEU A C   
2116 O O   . LEU A 253 ? 0.2944 0.2644 0.1698 -0.0629 -0.0206 0.0032  253 LEU A O   
2117 C CB  . LEU A 253 ? 0.2645 0.2373 0.1577 -0.0522 -0.0181 -0.0020 253 LEU A CB  
2118 C CG  . LEU A 253 ? 0.2797 0.2484 0.1705 -0.0525 -0.0193 -0.0040 253 LEU A CG  
2119 C CD1 . LEU A 253 ? 0.2723 0.2503 0.1790 -0.0479 -0.0212 -0.0033 253 LEU A CD1 
2120 C CD2 . LEU A 253 ? 0.3014 0.2666 0.1826 -0.0600 -0.0251 -0.0021 253 LEU A CD2 
2121 N N   . SER A 254 ? 0.2804 0.2509 0.1657 -0.0518 -0.0101 0.0001  254 SER A N   
2122 C CA  . SER A 254 ? 0.2840 0.2596 0.1720 -0.0525 -0.0100 0.0032  254 SER A CA  
2123 C C   . SER A 254 ? 0.3057 0.2704 0.1738 -0.0578 -0.0082 0.0029  254 SER A C   
2124 O O   . SER A 254 ? 0.3123 0.2805 0.1782 -0.0624 -0.0119 0.0061  254 SER A O   
2125 C CB  . SER A 254 ? 0.2930 0.2724 0.1917 -0.0456 -0.0043 0.0035  254 SER A CB  
2126 O OG  . SER A 254 ? 0.3179 0.3022 0.2193 -0.0461 -0.0039 0.0068  254 SER A OG  
2127 N N   . ALA A 255 ? 0.3155 0.2664 0.1685 -0.0573 -0.0023 -0.0008 255 ALA A N   
2128 C CA  . ALA A 255 ? 0.3400 0.2771 0.1707 -0.0623 0.0002  -0.0017 255 ALA A CA  
2129 C C   . ALA A 255 ? 0.3655 0.2991 0.1848 -0.0715 -0.0082 -0.0007 255 ALA A C   
2130 O O   . ALA A 255 ? 0.3732 0.3025 0.1802 -0.0774 -0.0103 0.0012  255 ALA A O   
2131 C CB  . ALA A 255 ? 0.3488 0.2704 0.1658 -0.0590 0.0091  -0.0060 255 ALA A CB  
2132 N N   . GLN A 256 ? 0.3714 0.3069 0.1952 -0.0729 -0.0131 -0.0013 256 GLN A N   
2133 C CA  . GLN A 256 ? 0.3882 0.3212 0.2036 -0.0818 -0.0217 0.0009  256 GLN A CA  
2134 C C   . GLN A 256 ? 0.3764 0.3230 0.2027 -0.0857 -0.0289 0.0071  256 GLN A C   
2135 O O   . GLN A 256 ? 0.3964 0.3390 0.2109 -0.0941 -0.0342 0.0102  256 GLN A O   
2136 C CB  . GLN A 256 ? 0.4192 0.3527 0.2398 -0.0813 -0.0246 -0.0004 256 GLN A CB  
2137 C CG  . GLN A 256 ? 0.4812 0.4119 0.2938 -0.0905 -0.0335 0.0028  256 GLN A CG  
2138 C CD  . GLN A 256 ? 0.5459 0.4792 0.3663 -0.0894 -0.0364 0.0025  256 GLN A CD  
2139 O OE1 . GLN A 256 ? 0.5664 0.4991 0.3928 -0.0825 -0.0312 -0.0015 256 GLN A OE1 
2140 N NE2 . GLN A 256 ? 0.5577 0.4944 0.3791 -0.0964 -0.0450 0.0075  256 GLN A NE2 
2141 N N   . THR A 257 ? 0.3374 0.2991 0.1853 -0.0801 -0.0291 0.0093  257 THR A N   
2142 C CA  . THR A 257 ? 0.3177 0.2924 0.1780 -0.0828 -0.0352 0.0154  257 THR A CA  
2143 C C   . THR A 257 ? 0.3148 0.2937 0.1766 -0.0824 -0.0332 0.0176  257 THR A C   
2144 O O   . THR A 257 ? 0.3169 0.3048 0.1857 -0.0860 -0.0382 0.0231  257 THR A O   
2145 C CB  . THR A 257 ? 0.3105 0.2976 0.1920 -0.0770 -0.0364 0.0167  257 THR A CB  
2146 O OG1 . THR A 257 ? 0.3100 0.2992 0.1997 -0.0691 -0.0302 0.0135  257 THR A OG1 
2147 C CG2 . THR A 257 ? 0.3140 0.2985 0.1956 -0.0772 -0.0386 0.0155  257 THR A CG2 
2148 N N   . GLY A 258 ? 0.3055 0.2787 0.1625 -0.0777 -0.0256 0.0140  258 GLY A N   
2149 C CA  . GLY A 258 ? 0.3007 0.2784 0.1606 -0.0763 -0.0230 0.0162  258 GLY A CA  
2150 C C   . GLY A 258 ? 0.2790 0.2716 0.1619 -0.0707 -0.0237 0.0188  258 GLY A C   
2151 O O   . GLY A 258 ? 0.2760 0.2747 0.1645 -0.0699 -0.0229 0.0217  258 GLY A O   
2152 N N   . ILE A 259 ? 0.2544 0.2524 0.1504 -0.0664 -0.0249 0.0176  259 ILE A N   
2153 C CA  . ILE A 259 ? 0.2404 0.2499 0.1558 -0.0614 -0.0257 0.0196  259 ILE A CA  
2154 C C   . ILE A 259 ? 0.2324 0.2402 0.1529 -0.0544 -0.0200 0.0163  259 ILE A C   
2155 O O   . ILE A 259 ? 0.2410 0.2438 0.1594 -0.0521 -0.0183 0.0128  259 ILE A O   
2156 C CB  . ILE A 259 ? 0.2472 0.2634 0.1733 -0.0617 -0.0310 0.0216  259 ILE A CB  
2157 C CG1 . ILE A 259 ? 0.2679 0.2870 0.1908 -0.0690 -0.0367 0.0267  259 ILE A CG1 
2158 C CG2 . ILE A 259 ? 0.2428 0.2682 0.1863 -0.0565 -0.0312 0.0231  259 ILE A CG2 
2159 C CD1 . ILE A 259 ? 0.2874 0.3119 0.2193 -0.0695 -0.0411 0.0296  259 ILE A CD1 
2160 N N   . ALA A 260 ? 0.2177 0.2297 0.1452 -0.0512 -0.0172 0.0179  260 ALA A N   
2161 C CA  . ALA A 260 ? 0.2111 0.2229 0.1457 -0.0449 -0.0123 0.0165  260 ALA A CA  
2162 C C   . ALA A 260 ? 0.1974 0.2133 0.1439 -0.0416 -0.0150 0.0154  260 ALA A C   
2163 O O   . ALA A 260 ? 0.1930 0.2148 0.1470 -0.0426 -0.0201 0.0169  260 ALA A O   
2164 C CB  . ALA A 260 ? 0.2178 0.2359 0.1611 -0.0428 -0.0106 0.0202  260 ALA A CB  
2165 N N   . VAL A 261 ? 0.1862 0.1984 0.1340 -0.0375 -0.0114 0.0130  261 VAL A N   
2166 C CA  . VAL A 261 ? 0.1849 0.1997 0.1422 -0.0346 -0.0140 0.0118  261 VAL A CA  
2167 C C   . VAL A 261 ? 0.1738 0.1965 0.1447 -0.0331 -0.0179 0.0145  261 VAL A C   
2168 O O   . VAL A 261 ? 0.1797 0.2045 0.1548 -0.0332 -0.0219 0.0141  261 VAL A O   
2169 C CB  . VAL A 261 ? 0.2018 0.2123 0.1596 -0.0306 -0.0094 0.0099  261 VAL A CB  
2170 C CG1 . VAL A 261 ? 0.1959 0.2093 0.1635 -0.0281 -0.0127 0.0092  261 VAL A CG1 
2171 C CG2 . VAL A 261 ? 0.2294 0.2303 0.1728 -0.0321 -0.0058 0.0066  261 VAL A CG2 
2172 N N   . LEU A 262 ? 0.1670 0.1935 0.1440 -0.0319 -0.0165 0.0175  262 LEU A N   
2173 C CA  . LEU A 262 ? 0.1643 0.1971 0.1536 -0.0308 -0.0205 0.0201  262 LEU A CA  
2174 C C   . LEU A 262 ? 0.1622 0.1988 0.1522 -0.0338 -0.0245 0.0217  262 LEU A C   
2175 O O   . LEU A 262 ? 0.1616 0.2008 0.1595 -0.0329 -0.0281 0.0226  262 LEU A O   
2176 C CB  . LEU A 262 ? 0.1625 0.1988 0.1594 -0.0288 -0.0184 0.0237  262 LEU A CB  
2177 C CG  . LEU A 262 ? 0.1797 0.2140 0.1806 -0.0252 -0.0152 0.0239  262 LEU A CG  
2178 C CD1 . LEU A 262 ? 0.1849 0.2233 0.1941 -0.0233 -0.0126 0.0290  262 LEU A CD1 
2179 C CD2 . LEU A 262 ? 0.1798 0.2139 0.1872 -0.0239 -0.0195 0.0228  262 LEU A CD2 
2180 N N   . ASP A 263 ? 0.1652 0.2012 0.1467 -0.0376 -0.0240 0.0223  263 ASP A N   
2181 C CA  . ASP A 263 ? 0.1578 0.1982 0.1413 -0.0407 -0.0279 0.0249  263 ASP A CA  
2182 C C   . ASP A 263 ? 0.1734 0.2122 0.1570 -0.0405 -0.0304 0.0233  263 ASP A C   
2183 O O   . ASP A 263 ? 0.1790 0.2213 0.1698 -0.0400 -0.0331 0.0254  263 ASP A O   
2184 C CB  . ASP A 263 ? 0.1698 0.2097 0.1437 -0.0457 -0.0277 0.0267  263 ASP A CB  
2185 C CG  . ASP A 263 ? 0.1838 0.2253 0.1567 -0.0461 -0.0250 0.0288  263 ASP A CG  
2186 O OD1 . ASP A 263 ? 0.1696 0.2137 0.1512 -0.0423 -0.0234 0.0296  263 ASP A OD1 
2187 O OD2 . ASP A 263 ? 0.2039 0.2440 0.1674 -0.0504 -0.0248 0.0302  263 ASP A OD2 
2188 N N   . MET A 264 ? 0.1646 0.1978 0.1403 -0.0405 -0.0289 0.0199  264 MET A N   
2189 C CA  . MET A 264 ? 0.1588 0.1907 0.1351 -0.0398 -0.0309 0.0187  264 MET A CA  
2190 C C   . MET A 264 ? 0.1625 0.1947 0.1475 -0.0352 -0.0315 0.0177  264 MET A C   
2191 O O   . MET A 264 ? 0.1712 0.2041 0.1599 -0.0342 -0.0334 0.0186  264 MET A O   
2192 C CB  . MET A 264 ? 0.1777 0.2035 0.1444 -0.0407 -0.0293 0.0155  264 MET A CB  
2193 C CG  . MET A 264 ? 0.1885 0.2142 0.1558 -0.0409 -0.0317 0.0157  264 MET A CG  
2194 S SD  . MET A 264 ? 0.2095 0.2401 0.1771 -0.0463 -0.0356 0.0214  264 MET A SD  
2195 C CE  . MET A 264 ? 0.2483 0.2724 0.2007 -0.0520 -0.0357 0.0202  264 MET A CE  
2196 N N   . CYS A 265 ? 0.1567 0.1879 0.1448 -0.0327 -0.0301 0.0165  265 CYS A N   
2197 C CA  . CYS A 265 ? 0.1578 0.1883 0.1529 -0.0294 -0.0318 0.0160  265 CYS A CA  
2198 C C   . CYS A 265 ? 0.1576 0.1912 0.1591 -0.0295 -0.0343 0.0189  265 CYS A C   
2199 O O   . CYS A 265 ? 0.1637 0.1946 0.1675 -0.0276 -0.0360 0.0183  265 CYS A O   
2200 C CB  . CYS A 265 ? 0.1574 0.1875 0.1559 -0.0276 -0.0304 0.0160  265 CYS A CB  
2201 S SG  . CYS A 265 ? 0.1704 0.1959 0.1636 -0.0262 -0.0268 0.0129  265 CYS A SG  
2202 N N   . ALA A 266 ? 0.1530 0.1913 0.1565 -0.0317 -0.0343 0.0220  266 ALA A N   
2203 C CA  . ALA A 266 ? 0.1644 0.2059 0.1747 -0.0318 -0.0364 0.0252  266 ALA A CA  
2204 C C   . ALA A 266 ? 0.1744 0.2162 0.1842 -0.0323 -0.0370 0.0266  266 ALA A C   
2205 O O   . ALA A 266 ? 0.1850 0.2259 0.1996 -0.0305 -0.0379 0.0280  266 ALA A O   
2206 C CB  . ALA A 266 ? 0.1742 0.2213 0.1873 -0.0342 -0.0362 0.0287  266 ALA A CB  
2207 N N   . SER A 267 ? 0.1711 0.2133 0.1750 -0.0346 -0.0364 0.0266  267 SER A N   
2208 C CA  . SER A 267 ? 0.1762 0.2192 0.1808 -0.0350 -0.0370 0.0290  267 SER A CA  
2209 C C   . SER A 267 ? 0.1678 0.2053 0.1723 -0.0308 -0.0364 0.0261  267 SER A C   
2210 O O   . SER A 267 ? 0.1705 0.2073 0.1788 -0.0287 -0.0360 0.0283  267 SER A O   
2211 C CB  . SER A 267 ? 0.2095 0.2533 0.2072 -0.0390 -0.0373 0.0297  267 SER A CB  
2212 O OG  . SER A 267 ? 0.2588 0.3075 0.2561 -0.0436 -0.0386 0.0337  267 SER A OG  
2213 N N   . LEU A 268 ? 0.1561 0.1892 0.1560 -0.0295 -0.0358 0.0216  268 LEU A N   
2214 C CA  . LEU A 268 ? 0.1563 0.1837 0.1548 -0.0260 -0.0354 0.0188  268 LEU A CA  
2215 C C   . LEU A 268 ? 0.1657 0.1895 0.1678 -0.0233 -0.0363 0.0187  268 LEU A C   
2216 O O   . LEU A 268 ? 0.1637 0.1828 0.1651 -0.0206 -0.0357 0.0187  268 LEU A O   
2217 C CB  . LEU A 268 ? 0.1529 0.1770 0.1465 -0.0255 -0.0348 0.0147  268 LEU A CB  
2218 C CG  . LEU A 268 ? 0.1661 0.1844 0.1579 -0.0223 -0.0349 0.0118  268 LEU A CG  
2219 C CD1 . LEU A 268 ? 0.1760 0.1930 0.1665 -0.0209 -0.0341 0.0130  268 LEU A CD1 
2220 C CD2 . LEU A 268 ? 0.1727 0.1891 0.1609 -0.0223 -0.0341 0.0087  268 LEU A CD2 
2221 N N   . LYS A 269 ? 0.1523 0.1773 0.1577 -0.0241 -0.0375 0.0191  269 LYS A N   
2222 C CA  . LYS A 269 ? 0.1498 0.1707 0.1582 -0.0225 -0.0392 0.0194  269 LYS A CA  
2223 C C   . LYS A 269 ? 0.1584 0.1790 0.1695 -0.0214 -0.0383 0.0224  269 LYS A C   
2224 O O   . LYS A 269 ? 0.1699 0.1828 0.1789 -0.0188 -0.0381 0.0215  269 LYS A O   
2225 C CB  . LYS A 269 ? 0.1600 0.1846 0.1732 -0.0242 -0.0407 0.0208  269 LYS A CB  
2226 C CG  . LYS A 269 ? 0.2053 0.2261 0.2223 -0.0235 -0.0433 0.0219  269 LYS A CG  
2227 C CD  . LYS A 269 ? 0.2400 0.2659 0.2629 -0.0252 -0.0448 0.0241  269 LYS A CD  
2228 C CE  . LYS A 269 ? 0.2824 0.3067 0.3105 -0.0255 -0.0474 0.0265  269 LYS A CE  
2229 N NZ  . LYS A 269 ? 0.2965 0.3278 0.3318 -0.0272 -0.0484 0.0298  269 LYS A NZ  
2230 N N   . GLU A 270 ? 0.1579 0.1859 0.1729 -0.0234 -0.0374 0.0264  270 GLU A N   
2231 C CA  . GLU A 270 ? 0.1697 0.1985 0.1891 -0.0223 -0.0360 0.0306  270 GLU A CA  
2232 C C   . GLU A 270 ? 0.1841 0.2088 0.2007 -0.0194 -0.0335 0.0309  270 GLU A C   
2233 O O   . GLU A 270 ? 0.1935 0.2128 0.2111 -0.0162 -0.0315 0.0324  270 GLU A O   
2234 C CB  . GLU A 270 ? 0.2006 0.2393 0.2255 -0.0258 -0.0363 0.0358  270 GLU A CB  
2235 C CG  . GLU A 270 ? 0.2905 0.3331 0.3190 -0.0280 -0.0381 0.0365  270 GLU A CG  
2236 C CD  . GLU A 270 ? 0.3871 0.4255 0.4198 -0.0259 -0.0388 0.0367  270 GLU A CD  
2237 O OE1 . GLU A 270 ? 0.4059 0.4431 0.4426 -0.0243 -0.0375 0.0400  270 GLU A OE1 
2238 O OE2 . GLU A 270 ? 0.4043 0.4403 0.4364 -0.0260 -0.0407 0.0342  270 GLU A OE2 
2239 N N   . LEU A 271 ? 0.1794 0.2056 0.1921 -0.0203 -0.0333 0.0295  271 LEU A N   
2240 C CA  . LEU A 271 ? 0.1824 0.2050 0.1928 -0.0174 -0.0309 0.0300  271 LEU A CA  
2241 C C   . LEU A 271 ? 0.1924 0.2041 0.1972 -0.0133 -0.0299 0.0258  271 LEU A C   
2242 O O   . LEU A 271 ? 0.2133 0.2197 0.2169 -0.0095 -0.0268 0.0273  271 LEU A O   
2243 C CB  . LEU A 271 ? 0.1825 0.2083 0.1894 -0.0196 -0.0316 0.0289  271 LEU A CB  
2244 C CG  . LEU A 271 ? 0.1939 0.2284 0.2042 -0.0240 -0.0327 0.0340  271 LEU A CG  
2245 C CD1 . LEU A 271 ? 0.2015 0.2366 0.2060 -0.0269 -0.0339 0.0316  271 LEU A CD1 
2246 C CD2 . LEU A 271 ? 0.2042 0.2418 0.2211 -0.0226 -0.0308 0.0409  271 LEU A CD2 
2247 N N   . LEU A 272 ? 0.1758 0.1833 0.1766 -0.0139 -0.0325 0.0211  272 LEU A N   
2248 C CA  . LEU A 272 ? 0.1901 0.1864 0.1843 -0.0111 -0.0327 0.0173  272 LEU A CA  
2249 C C   . LEU A 272 ? 0.2116 0.2007 0.2057 -0.0091 -0.0319 0.0186  272 LEU A C   
2250 O O   . LEU A 272 ? 0.2267 0.2053 0.2144 -0.0057 -0.0297 0.0175  272 LEU A O   
2251 C CB  . LEU A 272 ? 0.1912 0.1860 0.1829 -0.0130 -0.0362 0.0135  272 LEU A CB  
2252 C CG  . LEU A 272 ? 0.2166 0.2148 0.2063 -0.0139 -0.0361 0.0114  272 LEU A CG  
2253 C CD1 . LEU A 272 ? 0.2272 0.2256 0.2170 -0.0157 -0.0389 0.0091  272 LEU A CD1 
2254 C CD2 . LEU A 272 ? 0.2454 0.2379 0.2294 -0.0109 -0.0341 0.0099  272 LEU A CD2 
2255 N N   . GLN A 273 ? 0.2054 0.1992 0.2057 -0.0112 -0.0335 0.0209  273 GLN A N   
2256 C CA  . GLN A 273 ? 0.2237 0.2105 0.2243 -0.0099 -0.0332 0.0221  273 GLN A CA  
2257 C C   . GLN A 273 ? 0.2527 0.2390 0.2565 -0.0068 -0.0283 0.0266  273 GLN A C   
2258 O O   . GLN A 273 ? 0.2737 0.2493 0.2739 -0.0040 -0.0263 0.0267  273 GLN A O   
2259 C CB  . GLN A 273 ? 0.2243 0.2171 0.2315 -0.0133 -0.0367 0.0234  273 GLN A CB  
2260 C CG  . GLN A 273 ? 0.2464 0.2378 0.2515 -0.0156 -0.0413 0.0202  273 GLN A CG  
2261 C CD  . GLN A 273 ? 0.2852 0.2832 0.2979 -0.0185 -0.0442 0.0225  273 GLN A CD  
2262 O OE1 . GLN A 273 ? 0.3006 0.3075 0.3202 -0.0196 -0.0430 0.0261  273 GLN A OE1 
2263 N NE2 . GLN A 273 ? 0.2929 0.2871 0.3048 -0.0200 -0.0483 0.0211  273 GLN A NE2 
2264 N N   . ASN A 274 ? 0.2545 0.2516 0.2649 -0.0075 -0.0264 0.0309  274 ASN A N   
2265 C CA  . ASN A 274 ? 0.2714 0.2704 0.2878 -0.0049 -0.0218 0.0371  274 ASN A CA  
2266 C C   . ASN A 274 ? 0.2823 0.2817 0.2981 -0.0020 -0.0178 0.0397  274 ASN A C   
2267 O O   . ASN A 274 ? 0.2916 0.2917 0.3129 0.0010  -0.0132 0.0457  274 ASN A O   
2268 C CB  . ASN A 274 ? 0.2879 0.2999 0.3149 -0.0086 -0.0232 0.0426  274 ASN A CB  
2269 C CG  . ASN A 274 ? 0.3608 0.3720 0.3895 -0.0106 -0.0263 0.0411  274 ASN A CG  
2270 O OD1 . ASN A 274 ? 0.3974 0.4019 0.4271 -0.0083 -0.0247 0.0422  274 ASN A OD1 
2271 N ND2 . ASN A 274 ? 0.3745 0.3917 0.4032 -0.0146 -0.0305 0.0387  274 ASN A ND2 
2272 N N   . GLY A 275 ? 0.2828 0.2823 0.2932 -0.0028 -0.0193 0.0359  275 GLY A N   
2273 C CA  . GLY A 275 ? 0.2865 0.2874 0.2970 -0.0005 -0.0161 0.0386  275 GLY A CA  
2274 C C   . GLY A 275 ? 0.2849 0.2996 0.3049 -0.0041 -0.0171 0.0452  275 GLY A C   
2275 O O   . GLY A 275 ? 0.2838 0.3064 0.3087 -0.0085 -0.0203 0.0469  275 GLY A O   
2276 N N   A MET A 276 ? 0.2877 0.3051 0.3100 -0.0024 -0.0146 0.0494  276 MET A N   
2277 N N   B MET A 276 ? 0.2802 0.2977 0.3025 -0.0025 -0.0147 0.0494  276 MET A N   
2278 C CA  A MET A 276 ? 0.2918 0.3217 0.3226 -0.0067 -0.0165 0.0565  276 MET A CA  
2279 C CA  B MET A 276 ? 0.2766 0.3065 0.3075 -0.0066 -0.0165 0.0566  276 MET A CA  
2280 C C   A MET A 276 ? 0.2913 0.3266 0.3338 -0.0049 -0.0128 0.0668  276 MET A C   
2281 C C   B MET A 276 ? 0.2834 0.3188 0.3259 -0.0052 -0.0132 0.0666  276 MET A C   
2282 O O   A MET A 276 ? 0.2868 0.3330 0.3374 -0.0092 -0.0151 0.0741  276 MET A O   
2283 O O   B MET A 276 ? 0.2781 0.3245 0.3285 -0.0099 -0.0158 0.0734  276 MET A O   
2284 C CB  A MET A 276 ? 0.3085 0.3402 0.3362 -0.0077 -0.0176 0.0558  276 MET A CB  
2285 C CB  B MET A 276 ? 0.2735 0.3053 0.3025 -0.0070 -0.0168 0.0572  276 MET A CB  
2286 C CG  A MET A 276 ? 0.3395 0.3688 0.3581 -0.0109 -0.0218 0.0471  276 MET A CG  
2287 C CG  B MET A 276 ? 0.2760 0.3074 0.2968 -0.0110 -0.0214 0.0498  276 MET A CG  
2288 S SD  A MET A 276 ? 0.4400 0.4671 0.4525 -0.0105 -0.0223 0.0438  276 MET A SD  
2289 S SD  B MET A 276 ? 0.2332 0.2709 0.2548 -0.0145 -0.0237 0.0531  276 MET A SD  
2290 C CE  A MET A 276 ? 0.3629 0.4010 0.3831 -0.0152 -0.0244 0.0528  276 MET A CE  
2291 C CE  B MET A 276 ? 0.2208 0.2526 0.2310 -0.0159 -0.0263 0.0426  276 MET A CE  
2292 N N   . ASN A 277 ? 0.2923 0.3197 0.3354 0.0008  -0.0075 0.0678  277 ASN A N   
2293 C CA  . ASN A 277 ? 0.2954 0.3270 0.3503 0.0034  -0.0029 0.0778  277 ASN A CA  
2294 C C   . ASN A 277 ? 0.2873 0.3268 0.3515 0.0043  -0.0004 0.0878  277 ASN A C   
2295 O O   . ASN A 277 ? 0.2883 0.3383 0.3654 0.0022  -0.0004 0.0980  277 ASN A O   
2296 C CB  . ASN A 277 ? 0.3146 0.3549 0.3771 -0.0016 -0.0066 0.0811  277 ASN A CB  
2297 C CG  . ASN A 277 ? 0.3801 0.4120 0.4375 -0.0004 -0.0067 0.0749  277 ASN A CG  
2298 O OD1 . ASN A 277 ? 0.4070 0.4407 0.4607 -0.0050 -0.0120 0.0694  277 ASN A OD1 
2299 N ND2 . ASN A 277 ? 0.3897 0.4116 0.4467 0.0058  -0.0005 0.0760  277 ASN A ND2 
2300 N N   . GLY A 278 ? 0.2732 0.3084 0.3318 0.0070  0.0013  0.0856  278 GLY A N   
2301 C CA  . GLY A 278 ? 0.2576 0.3004 0.3255 0.0080  0.0034  0.0955  278 GLY A CA  
2302 C C   . GLY A 278 ? 0.2420 0.2976 0.3147 -0.0003 -0.0042 0.0992  278 GLY A C   
2303 O O   . GLY A 278 ? 0.2411 0.3048 0.3234 -0.0011 -0.0039 0.1091  278 GLY A O   
2304 N N   A ARG A 279 ? 0.2374 0.2940 0.3026 -0.0066 -0.0109 0.0916  279 ARG A N   
2305 N N   B ARG A 279 ? 0.2343 0.2909 0.2996 -0.0067 -0.0110 0.0916  279 ARG A N   
2306 C CA  A ARG A 279 ? 0.2322 0.2977 0.2981 -0.0149 -0.0181 0.0936  279 ARG A CA  
2307 C CA  B ARG A 279 ? 0.2260 0.2915 0.2918 -0.0151 -0.0183 0.0935  279 ARG A CA  
2308 C C   A ARG A 279 ? 0.2276 0.2883 0.2826 -0.0159 -0.0206 0.0856  279 ARG A C   
2309 C C   B ARG A 279 ? 0.2250 0.2857 0.2799 -0.0160 -0.0206 0.0856  279 ARG A C   
2310 O O   A ARG A 279 ? 0.2311 0.2822 0.2782 -0.0106 -0.0172 0.0780  279 ARG A O   
2311 O O   B ARG A 279 ? 0.2290 0.2801 0.2759 -0.0107 -0.0173 0.0778  279 ARG A O   
2312 C CB  A ARG A 279 ? 0.2510 0.3206 0.3158 -0.0214 -0.0232 0.0918  279 ARG A CB  
2313 C CB  B ARG A 279 ? 0.2362 0.3051 0.2999 -0.0213 -0.0233 0.0907  279 ARG A CB  
2314 C CG  A ARG A 279 ? 0.2938 0.3698 0.3709 -0.0211 -0.0214 0.1010  279 ARG A CG  
2315 C CG  B ARG A 279 ? 0.2661 0.3395 0.3403 -0.0205 -0.0212 0.0976  279 ARG A CG  
2316 C CD  A ARG A 279 ? 0.3399 0.4224 0.4173 -0.0287 -0.0273 0.1016  279 ARG A CD  
2317 C CD  B ARG A 279 ? 0.2998 0.3726 0.3693 -0.0240 -0.0245 0.0916  279 ARG A CD  
2318 N NE  A ARG A 279 ? 0.3833 0.4723 0.4588 -0.0371 -0.0340 0.1049  279 ARG A NE  
2319 N NE  B ARG A 279 ? 0.3295 0.4052 0.4085 -0.0223 -0.0219 0.0973  279 ARG A NE  
2320 C CZ  A ARG A 279 ? 0.4179 0.5167 0.5037 -0.0417 -0.0368 0.1170  279 ARG A CZ  
2321 C CZ  B ARG A 279 ? 0.3550 0.4260 0.4310 -0.0209 -0.0213 0.0917  279 ARG A CZ  
2322 N NH1 A ARG A 279 ? 0.4125 0.5171 0.5131 -0.0382 -0.0327 0.1276  279 ARG A NH1 
2323 N NH1 B ARG A 279 ? 0.3504 0.4141 0.4149 -0.0210 -0.0232 0.0809  279 ARG A NH1 
2324 N NH2 A ARG A 279 ? 0.4248 0.5272 0.5060 -0.0501 -0.0437 0.1190  279 ARG A NH2 
2325 N NH2 B ARG A 279 ? 0.3509 0.4248 0.4364 -0.0195 -0.0189 0.0976  279 ARG A NH2 
2326 N N   . THR A 280 ? 0.2166 0.2832 0.2709 -0.0228 -0.0264 0.0879  280 THR A N   
2327 C CA  . THR A 280 ? 0.2139 0.2762 0.2585 -0.0242 -0.0287 0.0810  280 THR A CA  
2328 C C   . THR A 280 ? 0.2026 0.2653 0.2386 -0.0320 -0.0349 0.0758  280 THR A C   
2329 O O   . THR A 280 ? 0.1972 0.2652 0.2356 -0.0377 -0.0384 0.0798  280 THR A O   
2330 C CB  . THR A 280 ? 0.2364 0.3030 0.2869 -0.0242 -0.0288 0.0887  280 THR A CB  
2331 O OG1 . THR A 280 ? 0.2391 0.3154 0.2973 -0.0315 -0.0340 0.0988  280 THR A OG1 
2332 C CG2 . THR A 280 ? 0.2482 0.3129 0.3057 -0.0154 -0.0213 0.0936  280 THR A CG2 
2333 N N   . ILE A 281 ? 0.1921 0.2483 0.2175 -0.0321 -0.0358 0.0669  281 ILE A N   
2334 C CA  . ILE A 281 ? 0.1942 0.2484 0.2097 -0.0384 -0.0402 0.0613  281 ILE A CA  
2335 C C   . ILE A 281 ? 0.1954 0.2471 0.2059 -0.0398 -0.0418 0.0598  281 ILE A C   
2336 O O   . ILE A 281 ? 0.1929 0.2404 0.2021 -0.0344 -0.0387 0.0558  281 ILE A O   
2337 C CB  . ILE A 281 ? 0.2069 0.2547 0.2150 -0.0359 -0.0385 0.0514  281 ILE A CB  
2338 C CG1 . ILE A 281 ? 0.2075 0.2576 0.2209 -0.0346 -0.0371 0.0531  281 ILE A CG1 
2339 C CG2 . ILE A 281 ? 0.2187 0.2634 0.2162 -0.0414 -0.0415 0.0459  281 ILE A CG2 
2340 C CD1 . ILE A 281 ? 0.2148 0.2592 0.2228 -0.0321 -0.0358 0.0447  281 ILE A CD1 
2341 N N   . LEU A 282 ? 0.1976 0.2518 0.2056 -0.0474 -0.0470 0.0638  282 LEU A N   
2342 C CA  . LEU A 282 ? 0.2014 0.2530 0.2048 -0.0495 -0.0492 0.0632  282 LEU A CA  
2343 C C   . LEU A 282 ? 0.2114 0.2652 0.2233 -0.0435 -0.0461 0.0674  282 LEU A C   
2344 O O   . LEU A 282 ? 0.2279 0.2771 0.2354 -0.0406 -0.0446 0.0622  282 LEU A O   
2345 C CB  . LEU A 282 ? 0.2020 0.2448 0.1923 -0.0498 -0.0488 0.0523  282 LEU A CB  
2346 C CG  . LEU A 282 ? 0.2157 0.2547 0.1952 -0.0564 -0.0518 0.0488  282 LEU A CG  
2347 C CD1 . LEU A 282 ? 0.2203 0.2506 0.1889 -0.0551 -0.0497 0.0390  282 LEU A CD1 
2348 C CD2 . LEU A 282 ? 0.2288 0.2691 0.2051 -0.0654 -0.0580 0.0555  282 LEU A CD2 
2349 N N   . GLY A 283 ? 0.2195 0.2802 0.2437 -0.0412 -0.0443 0.0767  283 GLY A N   
2350 C CA  . GLY A 283 ? 0.2237 0.2868 0.2570 -0.0349 -0.0402 0.0826  283 GLY A CA  
2351 C C   . GLY A 283 ? 0.2283 0.2848 0.2593 -0.0257 -0.0334 0.0759  283 GLY A C   
2352 O O   . GLY A 283 ? 0.2436 0.2998 0.2788 -0.0202 -0.0296 0.0791  283 GLY A O   
2353 N N   A SER A 284 ? 0.2168 0.2675 0.2403 -0.0242 -0.0321 0.0668  284 SER A N   
2354 N N   B SER A 284 ? 0.2200 0.2707 0.2436 -0.0242 -0.0321 0.0669  284 SER A N   
2355 C CA  A SER A 284 ? 0.2108 0.2539 0.2303 -0.0166 -0.0269 0.0603  284 SER A CA  
2356 C CA  B SER A 284 ? 0.2176 0.2606 0.2369 -0.0167 -0.0270 0.0601  284 SER A CA  
2357 C C   A SER A 284 ? 0.2077 0.2497 0.2305 -0.0132 -0.0236 0.0613  284 SER A C   
2358 C C   B SER A 284 ? 0.2128 0.2543 0.2350 -0.0132 -0.0236 0.0607  284 SER A C   
2359 O O   A SER A 284 ? 0.2003 0.2455 0.2245 -0.0173 -0.0261 0.0621  284 SER A O   
2360 O O   B SER A 284 ? 0.2104 0.2546 0.2333 -0.0172 -0.0261 0.0607  284 SER A O   
2361 C CB  A SER A 284 ? 0.2234 0.2600 0.2319 -0.0177 -0.0285 0.0493  284 SER A CB  
2362 C CB  B SER A 284 ? 0.2334 0.2699 0.2416 -0.0179 -0.0287 0.0492  284 SER A CB  
2363 O OG  A SER A 284 ? 0.2520 0.2810 0.2562 -0.0114 -0.0246 0.0435  284 SER A OG  
2364 O OG  B SER A 284 ? 0.2558 0.2918 0.2605 -0.0199 -0.0308 0.0477  284 SER A OG  
2365 N N   . ALA A 285 ? 0.2088 0.2447 0.2314 -0.0058 -0.0178 0.0607  285 ALA A N   
2366 C CA  . ALA A 285 ? 0.2189 0.2508 0.2425 -0.0020 -0.0141 0.0606  285 ALA A CA  
2367 C C   . ALA A 285 ? 0.2274 0.2492 0.2400 -0.0003 -0.0142 0.0498  285 ALA A C   
2368 O O   . ALA A 285 ? 0.2469 0.2625 0.2578 0.0030  -0.0114 0.0483  285 ALA A O   
2369 C CB  . ALA A 285 ? 0.2244 0.2542 0.2537 0.0051  -0.0071 0.0676  285 ALA A CB  
2370 N N   . LEU A 286 ? 0.2180 0.2377 0.2235 -0.0026 -0.0174 0.0429  286 LEU A N   
2371 C CA  . LEU A 286 ? 0.2259 0.2381 0.2229 -0.0022 -0.0186 0.0342  286 LEU A CA  
2372 C C   . LEU A 286 ? 0.2134 0.2293 0.2079 -0.0080 -0.0234 0.0299  286 LEU A C   
2373 O O   . LEU A 286 ? 0.2143 0.2366 0.2113 -0.0123 -0.0257 0.0329  286 LEU A O   
2374 C CB  . LEU A 286 ? 0.2449 0.2477 0.2345 0.0028  -0.0159 0.0300  286 LEU A CB  
2375 C CG  . LEU A 286 ? 0.2717 0.2762 0.2607 0.0035  -0.0156 0.0307  286 LEU A CG  
2376 C CD1 . LEU A 286 ? 0.2898 0.2969 0.2759 -0.0012 -0.0201 0.0258  286 LEU A CD1 
2377 C CD2 . LEU A 286 ? 0.2887 0.2833 0.2704 0.0092  -0.0120 0.0279  286 LEU A CD2 
2378 N N   . LEU A 287 ? 0.1966 0.2080 0.1863 -0.0085 -0.0248 0.0238  287 LEU A N   
2379 C CA  . LEU A 287 ? 0.1945 0.2084 0.1818 -0.0129 -0.0280 0.0201  287 LEU A CA  
2380 C C   . LEU A 287 ? 0.1947 0.2063 0.1774 -0.0127 -0.0283 0.0165  287 LEU A C   
2381 O O   . LEU A 287 ? 0.2180 0.2238 0.1970 -0.0098 -0.0277 0.0127  287 LEU A O   
2382 C CB  . LEU A 287 ? 0.2044 0.2153 0.1904 -0.0131 -0.0290 0.0166  287 LEU A CB  
2383 C CG  . LEU A 287 ? 0.2287 0.2422 0.2198 -0.0134 -0.0287 0.0204  287 LEU A CG  
2384 C CD1 . LEU A 287 ? 0.2400 0.2492 0.2299 -0.0128 -0.0297 0.0172  287 LEU A CD1 
2385 C CD2 . LEU A 287 ? 0.2392 0.2611 0.2341 -0.0183 -0.0304 0.0244  287 LEU A CD2 
2386 N N   A GLU A 288 ? 0.1777 0.1933 0.1603 -0.0162 -0.0297 0.0179  288 GLU A N   
2387 N N   B GLU A 288 ? 0.1778 0.1935 0.1605 -0.0162 -0.0297 0.0179  288 GLU A N   
2388 C CA  A GLU A 288 ? 0.1732 0.1869 0.1521 -0.0162 -0.0299 0.0150  288 GLU A CA  
2389 C CA  B GLU A 288 ? 0.1739 0.1877 0.1528 -0.0164 -0.0299 0.0151  288 GLU A CA  
2390 C C   A GLU A 288 ? 0.1716 0.1824 0.1461 -0.0175 -0.0305 0.0093  288 GLU A C   
2391 C C   B GLU A 288 ? 0.1723 0.1831 0.1468 -0.0175 -0.0305 0.0093  288 GLU A C   
2392 O O   A GLU A 288 ? 0.1728 0.1850 0.1461 -0.0209 -0.0314 0.0087  288 GLU A O   
2393 O O   B GLU A 288 ? 0.1742 0.1863 0.1476 -0.0208 -0.0314 0.0086  288 GLU A O   
2394 C CB  A GLU A 288 ? 0.1836 0.2015 0.1635 -0.0199 -0.0314 0.0192  288 GLU A CB  
2395 C CB  B GLU A 288 ? 0.1855 0.2036 0.1653 -0.0203 -0.0316 0.0192  288 GLU A CB  
2396 C CG  A GLU A 288 ? 0.2056 0.2277 0.1921 -0.0185 -0.0306 0.0266  288 GLU A CG  
2397 C CG  B GLU A 288 ? 0.2176 0.2336 0.1934 -0.0213 -0.0322 0.0166  288 GLU A CG  
2398 C CD  A GLU A 288 ? 0.2616 0.2815 0.2492 -0.0134 -0.0280 0.0276  288 GLU A CD  
2399 C CD  B GLU A 288 ? 0.2499 0.2642 0.2269 -0.0166 -0.0304 0.0167  288 GLU A CD  
2400 O OE1 A GLU A 288 ? 0.2810 0.2966 0.2640 -0.0115 -0.0275 0.0224  288 GLU A OE1 
2401 O OE1 B GLU A 288 ? 0.2080 0.2184 0.1815 -0.0149 -0.0297 0.0118  288 GLU A OE1 
2402 O OE2 A GLU A 288 ? 0.2609 0.2838 0.2546 -0.0111 -0.0261 0.0343  288 GLU A OE2 
2403 O OE2 B GLU A 288 ? 0.2800 0.2969 0.2618 -0.0145 -0.0293 0.0222  288 GLU A OE2 
2404 N N   . ASP A 289 ? 0.1707 0.1775 0.1429 -0.0148 -0.0298 0.0058  289 ASP A N   
2405 C CA  . ASP A 289 ? 0.1681 0.1727 0.1380 -0.0155 -0.0300 0.0016  289 ASP A CA  
2406 C C   . ASP A 289 ? 0.1799 0.1831 0.1473 -0.0156 -0.0295 -0.0004 289 ASP A C   
2407 O O   . ASP A 289 ? 0.1866 0.1876 0.1533 -0.0150 -0.0290 -0.0033 289 ASP A O   
2408 C CB  . ASP A 289 ? 0.1686 0.1696 0.1389 -0.0129 -0.0303 -0.0004 289 ASP A CB  
2409 C CG  . ASP A 289 ? 0.2007 0.1974 0.1689 -0.0096 -0.0302 -0.0016 289 ASP A CG  
2410 O OD1 . ASP A 289 ? 0.1995 0.1965 0.1670 -0.0083 -0.0291 -0.0004 289 ASP A OD1 
2411 O OD2 . ASP A 289 ? 0.2094 0.2023 0.1766 -0.0086 -0.0313 -0.0034 289 ASP A OD2 
2412 N N   . GLU A 290 ? 0.1783 0.1828 0.1452 -0.0165 -0.0297 0.0017  290 GLU A N   
2413 C CA  . GLU A 290 ? 0.1869 0.1897 0.1516 -0.0168 -0.0293 -0.0002 290 GLU A CA  
2414 C C   . GLU A 290 ? 0.1929 0.1955 0.1537 -0.0215 -0.0299 0.0002  290 GLU A C   
2415 O O   . GLU A 290 ? 0.1977 0.1993 0.1568 -0.0227 -0.0304 0.0005  290 GLU A O   
2416 C CB  . GLU A 290 ? 0.1961 0.1989 0.1623 -0.0136 -0.0289 0.0010  290 GLU A CB  
2417 C CG  . GLU A 290 ? 0.2235 0.2234 0.1899 -0.0094 -0.0282 -0.0005 290 GLU A CG  
2418 C CD  . GLU A 290 ? 0.2471 0.2452 0.2128 -0.0061 -0.0274 -0.0005 290 GLU A CD  
2419 O OE1 . GLU A 290 ? 0.2213 0.2215 0.1880 -0.0064 -0.0272 0.0016  290 GLU A OE1 
2420 O OE2 . GLU A 290 ? 0.2664 0.2605 0.2300 -0.0035 -0.0273 -0.0023 290 GLU A OE2 
2421 N N   . PHE A 291 ? 0.1857 0.1881 0.1443 -0.0244 -0.0300 -0.0001 291 PHE A N   
2422 C CA  . PHE A 291 ? 0.1967 0.1958 0.1484 -0.0288 -0.0300 -0.0010 291 PHE A CA  
2423 C C   . PHE A 291 ? 0.2040 0.2004 0.1537 -0.0282 -0.0273 -0.0041 291 PHE A C   
2424 O O   . PHE A 291 ? 0.2109 0.2098 0.1633 -0.0278 -0.0274 -0.0032 291 PHE A O   
2425 C CB  . PHE A 291 ? 0.1984 0.1994 0.1479 -0.0337 -0.0326 0.0028  291 PHE A CB  
2426 C CG  . PHE A 291 ? 0.2136 0.2184 0.1665 -0.0352 -0.0355 0.0079  291 PHE A CG  
2427 C CD1 . PHE A 291 ? 0.2299 0.2323 0.1787 -0.0387 -0.0375 0.0090  291 PHE A CD1 
2428 C CD2 . PHE A 291 ? 0.2284 0.2390 0.1890 -0.0331 -0.0361 0.0122  291 PHE A CD2 
2429 C CE1 . PHE A 291 ? 0.2449 0.2518 0.1984 -0.0404 -0.0406 0.0152  291 PHE A CE1 
2430 C CE2 . PHE A 291 ? 0.2408 0.2556 0.2059 -0.0343 -0.0383 0.0184  291 PHE A CE2 
2431 C CZ  . PHE A 291 ? 0.2375 0.2511 0.1997 -0.0380 -0.0407 0.0202  291 PHE A CZ  
2432 N N   . THR A 292 ? 0.2058 0.1971 0.1510 -0.0281 -0.0247 -0.0071 292 THR A N   
2433 C CA  . THR A 292 ? 0.2080 0.1966 0.1518 -0.0272 -0.0211 -0.0090 292 THR A CA  
2434 C C   . THR A 292 ? 0.2090 0.1937 0.1441 -0.0315 -0.0204 -0.0088 292 THR A C   
2435 O O   . THR A 292 ? 0.2094 0.1919 0.1380 -0.0358 -0.0229 -0.0077 292 THR A O   
2436 C CB  . THR A 292 ? 0.2254 0.2090 0.1675 -0.0252 -0.0175 -0.0115 292 THR A CB  
2437 O OG1 . THR A 292 ? 0.2463 0.2233 0.1789 -0.0286 -0.0170 -0.0126 292 THR A OG1 
2438 C CG2 . THR A 292 ? 0.2222 0.2088 0.1715 -0.0217 -0.0184 -0.0116 292 THR A CG2 
2439 N N   . PRO A 293 ? 0.2156 0.1986 0.1496 -0.0306 -0.0169 -0.0094 293 PRO A N   
2440 C CA  . PRO A 293 ? 0.2189 0.1964 0.1422 -0.0345 -0.0154 -0.0096 293 PRO A CA  
2441 C C   . PRO A 293 ? 0.2387 0.2063 0.1496 -0.0376 -0.0141 -0.0118 293 PRO A C   
2442 O O   . PRO A 293 ? 0.2490 0.2119 0.1493 -0.0430 -0.0162 -0.0112 293 PRO A O   
2443 C CB  . PRO A 293 ? 0.2324 0.2092 0.1581 -0.0312 -0.0103 -0.0099 293 PRO A CB  
2444 C CG  . PRO A 293 ? 0.2285 0.2138 0.1679 -0.0274 -0.0122 -0.0083 293 PRO A CG  
2445 C CD  . PRO A 293 ? 0.2079 0.1941 0.1504 -0.0263 -0.0145 -0.0092 293 PRO A CD  
2446 N N   . PHE A 294 ? 0.2447 0.2087 0.1564 -0.0347 -0.0111 -0.0139 294 PHE A N   
2447 C CA  A PHE A 294 ? 0.2722 0.2257 0.1719 -0.0374 -0.0097 -0.0162 294 PHE A CA  
2448 C CA  B PHE A 294 ? 0.2692 0.2227 0.1690 -0.0374 -0.0096 -0.0162 294 PHE A CA  
2449 C C   . PHE A 294 ? 0.2707 0.2255 0.1683 -0.0420 -0.0162 -0.0146 294 PHE A C   
2450 O O   . PHE A 294 ? 0.2910 0.2372 0.1757 -0.0475 -0.0177 -0.0150 294 PHE A O   
2451 C CB  A PHE A 294 ? 0.2858 0.2362 0.1888 -0.0329 -0.0050 -0.0182 294 PHE A CB  
2452 C CB  B PHE A 294 ? 0.2783 0.2291 0.1819 -0.0327 -0.0049 -0.0181 294 PHE A CB  
2453 C CG  A PHE A 294 ? 0.3135 0.2587 0.2155 -0.0291 0.0029  -0.0192 294 PHE A CG  
2454 C CG  B PHE A 294 ? 0.3077 0.2455 0.1983 -0.0345 -0.0013 -0.0209 294 PHE A CG  
2455 C CD1 A PHE A 294 ? 0.3332 0.2756 0.2298 -0.0297 0.0061  -0.0187 294 PHE A CD1 
2456 C CD1 B PHE A 294 ? 0.3351 0.2616 0.2092 -0.0392 0.0000  -0.0222 294 PHE A CD1 
2457 C CD2 A PHE A 294 ? 0.3325 0.2768 0.2404 -0.0247 0.0074  -0.0197 294 PHE A CD2 
2458 C CD2 B PHE A 294 ? 0.3229 0.2587 0.2170 -0.0316 0.0011  -0.0221 294 PHE A CD2 
2459 C CE1 A PHE A 294 ? 0.3467 0.2849 0.2437 -0.0255 0.0141  -0.0185 294 PHE A CE1 
2460 C CE1 B PHE A 294 ? 0.3569 0.2690 0.2170 -0.0411 0.0034  -0.0250 294 PHE A CE1 
2461 C CE2 A PHE A 294 ? 0.3446 0.2853 0.2539 -0.0207 0.0151  -0.0191 294 PHE A CE2 
2462 C CE2 B PHE A 294 ? 0.3424 0.2652 0.2243 -0.0331 0.0047  -0.0246 294 PHE A CE2 
2463 C CZ  A PHE A 294 ? 0.3455 0.2831 0.2493 -0.0209 0.0187  -0.0184 294 PHE A CZ  
2464 C CZ  B PHE A 294 ? 0.3512 0.2615 0.2156 -0.0379 0.0059  -0.0263 294 PHE A CZ  
2465 N N   . ASP A 295 ? 0.2529 0.2177 0.1624 -0.0401 -0.0201 -0.0122 295 ASP A N   
2466 C CA  . ASP A 295 ? 0.2476 0.2153 0.1577 -0.0437 -0.0259 -0.0092 295 ASP A CA  
2467 C C   . ASP A 295 ? 0.2600 0.2280 0.1646 -0.0496 -0.0298 -0.0060 295 ASP A C   
2468 O O   . ASP A 295 ? 0.2774 0.2420 0.1754 -0.0553 -0.0340 -0.0039 295 ASP A O   
2469 C CB  . ASP A 295 ? 0.2495 0.2275 0.1733 -0.0396 -0.0279 -0.0067 295 ASP A CB  
2470 C CG  . ASP A 295 ? 0.2638 0.2425 0.1933 -0.0346 -0.0256 -0.0088 295 ASP A CG  
2471 O OD1 . ASP A 295 ? 0.2773 0.2493 0.2015 -0.0349 -0.0234 -0.0113 295 ASP A OD1 
2472 O OD2 . ASP A 295 ? 0.2535 0.2386 0.1922 -0.0306 -0.0260 -0.0078 295 ASP A OD2 
2473 N N   . VAL A 296 ? 0.2445 0.2169 0.1525 -0.0487 -0.0290 -0.0051 296 VAL A N   
2474 C CA  . VAL A 296 ? 0.2485 0.2222 0.1524 -0.0542 -0.0327 -0.0016 296 VAL A CA  
2475 C C   . VAL A 296 ? 0.2792 0.2410 0.1658 -0.0602 -0.0325 -0.0033 296 VAL A C   
2476 O O   . VAL A 296 ? 0.2957 0.2555 0.1759 -0.0670 -0.0378 0.0000  296 VAL A O   
2477 C CB  . VAL A 296 ? 0.2406 0.2216 0.1524 -0.0515 -0.0316 -0.0003 296 VAL A CB  
2478 C CG1 . VAL A 296 ? 0.2471 0.2291 0.1541 -0.0575 -0.0351 0.0035  296 VAL A CG1 
2479 C CG2 . VAL A 296 ? 0.2309 0.2216 0.1572 -0.0468 -0.0328 0.0019  296 VAL A CG2 
2480 N N   . VAL A 297 ? 0.2892 0.2421 0.1676 -0.0579 -0.0263 -0.0080 297 VAL A N   
2481 C CA  . VAL A 297 ? 0.3194 0.2578 0.1784 -0.0631 -0.0248 -0.0103 297 VAL A CA  
2482 C C   . VAL A 297 ? 0.3375 0.2679 0.1878 -0.0677 -0.0283 -0.0106 297 VAL A C   
2483 O O   . VAL A 297 ? 0.3512 0.2732 0.1873 -0.0755 -0.0325 -0.0093 297 VAL A O   
2484 C CB  . VAL A 297 ? 0.3451 0.2753 0.1985 -0.0581 -0.0158 -0.0147 297 VAL A CB  
2485 C CG1 . VAL A 297 ? 0.3705 0.2827 0.2015 -0.0628 -0.0129 -0.0176 297 VAL A CG1 
2486 C CG2 . VAL A 297 ? 0.3543 0.2919 0.2157 -0.0545 -0.0128 -0.0135 297 VAL A CG2 
2487 N N   . ARG A 298 ? 0.3385 0.2714 0.1970 -0.0634 -0.0271 -0.0119 298 ARG A N   
2488 C CA  . ARG A 298 ? 0.3595 0.2855 0.2117 -0.0670 -0.0301 -0.0122 298 ARG A CA  
2489 C C   . ARG A 298 ? 0.3621 0.2932 0.2158 -0.0738 -0.0391 -0.0063 298 ARG A C   
2490 O O   . ARG A 298 ? 0.3706 0.2916 0.2105 -0.0814 -0.0433 -0.0054 298 ARG A O   
2491 C CB  . ARG A 298 ? 0.3855 0.3161 0.2494 -0.0605 -0.0274 -0.0137 298 ARG A CB  
2492 C CG  . ARG A 298 ? 0.4514 0.3728 0.3077 -0.0632 -0.0286 -0.0150 298 ARG A CG  
2493 C CD  . ARG A 298 ? 0.5071 0.4343 0.3760 -0.0568 -0.0263 -0.0159 298 ARG A CD  
2494 N NE  . ARG A 298 ? 0.5627 0.4894 0.4357 -0.0499 -0.0184 -0.0195 298 ARG A NE  
2495 C CZ  . ARG A 298 ? 0.5959 0.5340 0.4836 -0.0439 -0.0169 -0.0186 298 ARG A CZ  
2496 N NH1 . ARG A 298 ? 0.6028 0.5401 0.4942 -0.0386 -0.0104 -0.0208 298 ARG A NH1 
2497 N NH2 . ARG A 298 ? 0.5851 0.5349 0.4837 -0.0434 -0.0218 -0.0151 298 ARG A NH2 
2498 N N   . GLN A 299 ? 0.3535 0.2995 0.2235 -0.0715 -0.0421 -0.0016 299 GLN A N   
2499 C CA  . GLN A 299 ? 0.3590 0.3118 0.2339 -0.0770 -0.0499 0.0056  299 GLN A CA  
2500 C C   . GLN A 299 ? 0.3870 0.3366 0.2520 -0.0848 -0.0542 0.0088  299 GLN A C   
2501 O O   . GLN A 299 ? 0.4029 0.3494 0.2619 -0.0928 -0.0611 0.0134  299 GLN A O   
2502 C CB  . GLN A 299 ? 0.3452 0.3136 0.2398 -0.0713 -0.0503 0.0098  299 GLN A CB  
2503 C CG  . GLN A 299 ? 0.3338 0.3097 0.2356 -0.0760 -0.0573 0.0184  299 GLN A CG  
2504 C CD  . GLN A 299 ? 0.3113 0.3003 0.2311 -0.0699 -0.0567 0.0229  299 GLN A CD  
2505 O OE1 . GLN A 299 ? 0.3085 0.3054 0.2364 -0.0726 -0.0610 0.0310  299 GLN A OE1 
2506 N NE2 . GLN A 299 ? 0.2821 0.2734 0.2084 -0.0618 -0.0513 0.0185  299 GLN A NE2 
2507 N N   . CYS A 300 ? 0.3924 0.3424 0.2554 -0.0831 -0.0507 0.0068  300 CYS A N   
2508 C CA  . CYS A 300 ? 0.4087 0.3556 0.2619 -0.0905 -0.0545 0.0098  300 CYS A CA  
2509 C C   . CYS A 300 ? 0.4480 0.3763 0.2769 -0.0979 -0.0552 0.0065  300 CYS A C   
2510 O O   . CYS A 300 ? 0.4564 0.3806 0.2748 -0.1063 -0.0607 0.0101  300 CYS A O   
2511 C CB  . CYS A 300 ? 0.3963 0.3494 0.2550 -0.0864 -0.0505 0.0091  300 CYS A CB  
2512 S SG  . CYS A 300 ? 0.4013 0.3739 0.2849 -0.0804 -0.0515 0.0145  300 CYS A SG  
2513 N N   . SER A 301 ? 0.4716 0.3880 0.2911 -0.0951 -0.0500 0.0001  301 SER A N   
2514 C CA  . SER A 301 ? 0.5089 0.4050 0.3035 -0.1017 -0.0498 -0.0035 301 SER A CA  
2515 C C   . SER A 301 ? 0.5350 0.4229 0.3229 -0.1066 -0.0546 -0.0031 301 SER A C   
2516 O O   . SER A 301 ? 0.5574 0.4275 0.3234 -0.1139 -0.0565 -0.0050 301 SER A O   
2517 C CB  . SER A 301 ? 0.5388 0.4236 0.3234 -0.0957 -0.0391 -0.0109 301 SER A CB  
2518 O OG  . SER A 301 ? 0.5687 0.4535 0.3609 -0.0883 -0.0335 -0.0146 301 SER A OG  
2519 N N   . GLY A 302 ? 0.5305 0.4300 0.3361 -0.1026 -0.0563 -0.0006 302 GLY A N   
2520 C CA  . GLY A 302 ? 0.5449 0.4392 0.3475 -0.1069 -0.0613 0.0010  302 GLY A CA  
2521 C C   . GLY A 302 ? 0.5606 0.4402 0.3523 -0.1038 -0.0550 -0.0062 302 GLY A C   
2522 O O   . GLY A 302 ? 0.5777 0.4425 0.3534 -0.1106 -0.0585 -0.0070 302 GLY A O   
2523 N N   . VAL A 303 ? 0.5526 0.4361 0.3534 -0.0937 -0.0459 -0.0110 303 VAL A N   
2524 C CA  . VAL A 303 ? 0.5589 0.4304 0.3526 -0.0896 -0.0389 -0.0171 303 VAL A CA  
2525 C C   . VAL A 303 ? 0.5504 0.4249 0.3518 -0.0901 -0.0431 -0.0151 303 VAL A C   
2526 O O   . VAL A 303 ? 0.5357 0.4270 0.3563 -0.0873 -0.0466 -0.0105 303 VAL A O   
2527 C CB  . VAL A 303 ? 0.5633 0.4412 0.3684 -0.0789 -0.0291 -0.0207 303 VAL A CB  
2528 C CG1 . VAL A 303 ? 0.5777 0.4448 0.3782 -0.0742 -0.0215 -0.0257 303 VAL A CG1 
2529 C CG2 . VAL A 303 ? 0.5724 0.4479 0.3709 -0.0782 -0.0248 -0.0220 303 VAL A CG2 
2530 N N   A THR A 304 ? 0.5584 0.4163 0.3449 -0.0934 -0.0424 -0.0183 304 THR A N   
2531 N N   B THR A 304 ? 0.5585 0.4161 0.3445 -0.0936 -0.0424 -0.0183 304 THR A N   
2532 C CA  A THR A 304 ? 0.5583 0.4185 0.3519 -0.0940 -0.0464 -0.0162 304 THR A CA  
2533 C CA  B THR A 304 ? 0.5595 0.4178 0.3510 -0.0944 -0.0461 -0.0167 304 THR A CA  
2534 C C   A THR A 304 ? 0.5592 0.4165 0.3575 -0.0859 -0.0379 -0.0212 304 THR A C   
2535 C C   B THR A 304 ? 0.5665 0.4152 0.3551 -0.0881 -0.0372 -0.0228 304 THR A C   
2536 O O   A THR A 304 ? 0.5537 0.4136 0.3592 -0.0853 -0.0403 -0.0199 304 THR A O   
2537 O O   B THR A 304 ? 0.5641 0.4134 0.3558 -0.0806 -0.0281 -0.0266 304 THR A O   
2538 C CB  A THR A 304 ? 0.5841 0.4294 0.3596 -0.1053 -0.0545 -0.0143 304 THR A CB  
2539 C CB  B THR A 304 ? 0.5814 0.4283 0.3575 -0.1062 -0.0558 -0.0133 304 THR A CB  
2540 O OG1 A THR A 304 ? 0.6127 0.4346 0.3633 -0.1078 -0.0490 -0.0209 304 THR A OG1 
2541 O OG1 B THR A 304 ? 0.6100 0.4336 0.3593 -0.1110 -0.0526 -0.0187 304 THR A OG1 
2542 C CG2 A THR A 304 ? 0.5871 0.4386 0.3622 -0.1137 -0.0643 -0.0073 304 THR A CG2 
2543 C CG2 B THR A 304 ? 0.5784 0.4376 0.3615 -0.1123 -0.0651 -0.0054 304 THR A CG2 
2544 S S   . DMS B .   ? 0.2030 0.2530 0.3059 0.0142  -0.0223 0.0422  401 DMS A S   
2545 O O   . DMS B .   ? 0.2067 0.2623 0.3090 0.0170  -0.0213 0.0422  401 DMS A O   
2546 C C1  . DMS B .   ? 0.2054 0.2497 0.2971 0.0117  -0.0247 0.0398  401 DMS A C1  
2547 C C2  . DMS B .   ? 0.1948 0.2540 0.3057 0.0159  -0.0255 0.0493  401 DMS A C2  
2548 S S   . DMS C .   ? 0.5726 0.6429 0.6328 0.0331  -0.0250 0.0516  402 DMS A S   
2549 O O   . DMS C .   ? 0.5645 0.6411 0.6389 0.0324  -0.0251 0.0544  402 DMS A O   
2550 C C1  . DMS C .   ? 0.5741 0.6444 0.6284 0.0381  -0.0224 0.0551  402 DMS A C1  
2551 C C2  . DMS C .   ? 0.5761 0.6466 0.6296 0.0338  -0.0265 0.0540  402 DMS A C2  
2552 S S   . DMS D .   ? 0.4191 0.3868 0.3321 -0.0512 -0.0390 -0.0011 403 DMS A S   
2553 O O   . DMS D .   ? 0.4341 0.3934 0.3396 -0.0547 -0.0404 -0.0021 403 DMS A O   
2554 C C1  . DMS D .   ? 0.4314 0.3907 0.3317 -0.0546 -0.0369 -0.0043 403 DMS A C1  
2555 C C2  . DMS D .   ? 0.4176 0.3886 0.3391 -0.0424 -0.0329 -0.0054 403 DMS A C2  
2556 S S   . DMS E .   ? 0.4677 0.4488 0.4601 -0.0274 -0.0432 0.0179  404 DMS A S   
2557 O O   . DMS E .   ? 0.4800 0.4523 0.4688 -0.0326 -0.0462 0.0186  404 DMS A O   
2558 C C1  . DMS E .   ? 0.4613 0.4467 0.4607 -0.0200 -0.0367 0.0144  404 DMS A C1  
2559 C C2  . DMS E .   ? 0.4585 0.4549 0.4639 -0.0243 -0.0465 0.0272  404 DMS A C2  
# 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP 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 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 DMS 1   401 401 DMS DMS A . 
C 2 DMS 1   402 501 DMS DMS A . 
D 2 DMS 1   403 601 DMS DMS A . 
E 2 DMS 1   404 701 DMS DMS A . 
F 3 HOH 1   501 374 HOH HOH A . 
F 3 HOH 2   502 340 HOH HOH A . 
F 3 HOH 3   503 119 HOH HOH A . 
F 3 HOH 4   504 199 HOH HOH A . 
F 3 HOH 5   505 165 HOH HOH A . 
F 3 HOH 6   506 275 HOH HOH A . 
F 3 HOH 7   507 112 HOH HOH A . 
F 3 HOH 8   508 162 HOH HOH A . 
F 3 HOH 9   509 66  HOH HOH A . 
F 3 HOH 10  510 25  HOH HOH A . 
F 3 HOH 11  511 132 HOH HOH A . 
F 3 HOH 12  512 35  HOH HOH A . 
F 3 HOH 13  513 345 HOH HOH A . 
F 3 HOH 14  514 29  HOH HOH A . 
F 3 HOH 15  515 99  HOH HOH A . 
F 3 HOH 16  516 129 HOH HOH A . 
F 3 HOH 17  517 212 HOH HOH A . 
F 3 HOH 18  518 93  HOH HOH A . 
F 3 HOH 19  519 327 HOH HOH A . 
F 3 HOH 20  520 120 HOH HOH A . 
F 3 HOH 21  521 155 HOH HOH A . 
F 3 HOH 22  522 373 HOH HOH A . 
F 3 HOH 23  523 9   HOH HOH A . 
F 3 HOH 24  524 335 HOH HOH A . 
F 3 HOH 25  525 243 HOH HOH A . 
F 3 HOH 26  526 358 HOH HOH A . 
F 3 HOH 27  527 97  HOH HOH A . 
F 3 HOH 28  528 264 HOH HOH A . 
F 3 HOH 29  529 137 HOH HOH A . 
F 3 HOH 30  530 352 HOH HOH A . 
F 3 HOH 31  531 151 HOH HOH A . 
F 3 HOH 32  532 256 HOH HOH A . 
F 3 HOH 33  533 48  HOH HOH A . 
F 3 HOH 34  534 107 HOH HOH A . 
F 3 HOH 35  535 40  HOH HOH A . 
F 3 HOH 36  536 313 HOH HOH A . 
F 3 HOH 37  537 34  HOH HOH A . 
F 3 HOH 38  538 277 HOH HOH A . 
F 3 HOH 39  539 332 HOH HOH A . 
F 3 HOH 40  540 73  HOH HOH A . 
F 3 HOH 41  541 198 HOH HOH A . 
F 3 HOH 42  542 251 HOH HOH A . 
F 3 HOH 43  543 38  HOH HOH A . 
F 3 HOH 44  544 55  HOH HOH A . 
F 3 HOH 45  545 63  HOH HOH A . 
F 3 HOH 46  546 247 HOH HOH A . 
F 3 HOH 47  547 248 HOH HOH A . 
F 3 HOH 48  548 44  HOH HOH A . 
F 3 HOH 49  549 178 HOH HOH A . 
F 3 HOH 50  550 154 HOH HOH A . 
F 3 HOH 51  551 76  HOH HOH A . 
F 3 HOH 52  552 242 HOH HOH A . 
F 3 HOH 53  553 67  HOH HOH A . 
F 3 HOH 54  554 104 HOH HOH A . 
F 3 HOH 55  555 30  HOH HOH A . 
F 3 HOH 56  556 157 HOH HOH A . 
F 3 HOH 57  557 33  HOH HOH A . 
F 3 HOH 58  558 1   HOH HOH A . 
F 3 HOH 59  559 80  HOH HOH A . 
F 3 HOH 60  560 77  HOH HOH A . 
F 3 HOH 61  561 53  HOH HOH A . 
F 3 HOH 62  562 179 HOH HOH A . 
F 3 HOH 63  563 56  HOH HOH A . 
F 3 HOH 64  564 319 HOH HOH A . 
F 3 HOH 65  565 21  HOH HOH A . 
F 3 HOH 66  566 181 HOH HOH A . 
F 3 HOH 67  567 208 HOH HOH A . 
F 3 HOH 68  568 3   HOH HOH A . 
F 3 HOH 69  569 45  HOH HOH A . 
F 3 HOH 70  570 82  HOH HOH A . 
F 3 HOH 71  571 183 HOH HOH A . 
F 3 HOH 72  572 20  HOH HOH A . 
F 3 HOH 73  573 182 HOH HOH A . 
F 3 HOH 74  574 390 HOH HOH A . 
F 3 HOH 75  575 177 HOH HOH A . 
F 3 HOH 76  576 24  HOH HOH A . 
F 3 HOH 77  577 244 HOH HOH A . 
F 3 HOH 78  578 116 HOH HOH A . 
F 3 HOH 79  579 7   HOH HOH A . 
F 3 HOH 80  580 241 HOH HOH A . 
F 3 HOH 81  581 159 HOH HOH A . 
F 3 HOH 82  582 347 HOH HOH A . 
F 3 HOH 83  583 113 HOH HOH A . 
F 3 HOH 84  584 142 HOH HOH A . 
F 3 HOH 85  585 12  HOH HOH A . 
F 3 HOH 86  586 10  HOH HOH A . 
F 3 HOH 87  587 186 HOH HOH A . 
F 3 HOH 88  588 266 HOH HOH A . 
F 3 HOH 89  589 349 HOH HOH A . 
F 3 HOH 90  590 175 HOH HOH A . 
F 3 HOH 91  591 184 HOH HOH A . 
F 3 HOH 92  592 42  HOH HOH A . 
F 3 HOH 93  593 294 HOH HOH A . 
F 3 HOH 94  594 304 HOH HOH A . 
F 3 HOH 95  595 274 HOH HOH A . 
F 3 HOH 96  596 26  HOH HOH A . 
F 3 HOH 97  597 169 HOH HOH A . 
F 3 HOH 98  598 368 HOH HOH A . 
F 3 HOH 99  599 189 HOH HOH A . 
F 3 HOH 100 600 105 HOH HOH A . 
F 3 HOH 101 601 19  HOH HOH A . 
F 3 HOH 102 602 259 HOH HOH A . 
F 3 HOH 103 603 357 HOH HOH A . 
F 3 HOH 104 604 6   HOH HOH A . 
F 3 HOH 105 605 170 HOH HOH A . 
F 3 HOH 106 606 58  HOH HOH A . 
F 3 HOH 107 607 65  HOH HOH A . 
F 3 HOH 108 608 361 HOH HOH A . 
F 3 HOH 109 609 94  HOH HOH A . 
F 3 HOH 110 610 236 HOH HOH A . 
F 3 HOH 111 611 163 HOH HOH A . 
F 3 HOH 112 612 86  HOH HOH A . 
F 3 HOH 113 613 31  HOH HOH A . 
F 3 HOH 114 614 27  HOH HOH A . 
F 3 HOH 115 615 326 HOH HOH A . 
F 3 HOH 116 616 306 HOH HOH A . 
F 3 HOH 117 617 43  HOH HOH A . 
F 3 HOH 118 618 92  HOH HOH A . 
F 3 HOH 119 619 4   HOH HOH A . 
F 3 HOH 120 620 272 HOH HOH A . 
F 3 HOH 121 621 168 HOH HOH A . 
F 3 HOH 122 622 342 HOH HOH A . 
F 3 HOH 123 623 117 HOH HOH A . 
F 3 HOH 124 624 263 HOH HOH A . 
F 3 HOH 125 625 289 HOH HOH A . 
F 3 HOH 126 626 171 HOH HOH A . 
F 3 HOH 127 627 69  HOH HOH A . 
F 3 HOH 128 628 269 HOH HOH A . 
F 3 HOH 129 629 5   HOH HOH A . 
F 3 HOH 130 630 68  HOH HOH A . 
F 3 HOH 131 631 87  HOH HOH A . 
F 3 HOH 132 632 89  HOH HOH A . 
F 3 HOH 133 633 351 HOH HOH A . 
F 3 HOH 134 634 172 HOH HOH A . 
F 3 HOH 135 635 230 HOH HOH A . 
F 3 HOH 136 636 54  HOH HOH A . 
F 3 HOH 137 637 118 HOH HOH A . 
F 3 HOH 138 638 60  HOH HOH A . 
F 3 HOH 139 639 106 HOH HOH A . 
F 3 HOH 140 640 79  HOH HOH A . 
F 3 HOH 141 641 185 HOH HOH A . 
F 3 HOH 142 642 381 HOH HOH A . 
F 3 HOH 143 643 298 HOH HOH A . 
F 3 HOH 144 644 295 HOH HOH A . 
F 3 HOH 145 645 17  HOH HOH A . 
F 3 HOH 146 646 164 HOH HOH A . 
F 3 HOH 147 647 204 HOH HOH A . 
F 3 HOH 148 648 310 HOH HOH A . 
F 3 HOH 149 649 11  HOH HOH A . 
F 3 HOH 150 650 15  HOH HOH A . 
F 3 HOH 151 651 28  HOH HOH A . 
F 3 HOH 152 652 392 HOH HOH A . 
F 3 HOH 153 653 246 HOH HOH A . 
F 3 HOH 154 654 37  HOH HOH A . 
F 3 HOH 155 655 309 HOH HOH A . 
F 3 HOH 156 656 200 HOH HOH A . 
F 3 HOH 157 657 130 HOH HOH A . 
F 3 HOH 158 658 285 HOH HOH A . 
F 3 HOH 159 659 83  HOH HOH A . 
F 3 HOH 160 660 102 HOH HOH A . 
F 3 HOH 161 661 62  HOH HOH A . 
F 3 HOH 162 662 101 HOH HOH A . 
F 3 HOH 163 663 176 HOH HOH A . 
F 3 HOH 164 664 325 HOH HOH A . 
F 3 HOH 165 665 234 HOH HOH A . 
F 3 HOH 166 666 52  HOH HOH A . 
F 3 HOH 167 667 88  HOH HOH A . 
F 3 HOH 168 668 72  HOH HOH A . 
F 3 HOH 169 669 128 HOH HOH A . 
F 3 HOH 170 670 228 HOH HOH A . 
F 3 HOH 171 671 145 HOH HOH A . 
F 3 HOH 172 672 173 HOH HOH A . 
F 3 HOH 173 673 18  HOH HOH A . 
F 3 HOH 174 674 125 HOH HOH A . 
F 3 HOH 175 675 152 HOH HOH A . 
F 3 HOH 176 676 299 HOH HOH A . 
F 3 HOH 177 677 240 HOH HOH A . 
F 3 HOH 178 678 111 HOH HOH A . 
F 3 HOH 179 679 61  HOH HOH A . 
F 3 HOH 180 680 203 HOH HOH A . 
F 3 HOH 181 681 100 HOH HOH A . 
F 3 HOH 182 682 156 HOH HOH A . 
F 3 HOH 183 683 71  HOH HOH A . 
F 3 HOH 184 684 59  HOH HOH A . 
F 3 HOH 185 685 133 HOH HOH A . 
F 3 HOH 186 686 64  HOH HOH A . 
F 3 HOH 187 687 127 HOH HOH A . 
F 3 HOH 188 688 386 HOH HOH A . 
F 3 HOH 189 689 14  HOH HOH A . 
F 3 HOH 190 690 78  HOH HOH A . 
F 3 HOH 191 691 344 HOH HOH A . 
F 3 HOH 192 692 131 HOH HOH A . 
F 3 HOH 193 693 2   HOH HOH A . 
F 3 HOH 194 694 135 HOH HOH A . 
F 3 HOH 195 695 239 HOH HOH A . 
F 3 HOH 196 696 276 HOH HOH A . 
F 3 HOH 197 697 328 HOH HOH A . 
F 3 HOH 198 698 213 HOH HOH A . 
F 3 HOH 199 699 32  HOH HOH A . 
F 3 HOH 200 700 360 HOH HOH A . 
F 3 HOH 201 701 201 HOH HOH A . 
F 3 HOH 202 702 136 HOH HOH A . 
F 3 HOH 203 703 153 HOH HOH A . 
F 3 HOH 204 704 379 HOH HOH A . 
F 3 HOH 205 705 166 HOH HOH A . 
F 3 HOH 206 706 84  HOH HOH A . 
F 3 HOH 207 707 75  HOH HOH A . 
F 3 HOH 208 708 231 HOH HOH A . 
F 3 HOH 209 709 187 HOH HOH A . 
F 3 HOH 210 710 290 HOH HOH A . 
F 3 HOH 211 711 96  HOH HOH A . 
F 3 HOH 212 712 211 HOH HOH A . 
F 3 HOH 213 713 150 HOH HOH A . 
F 3 HOH 214 714 267 HOH HOH A . 
F 3 HOH 215 715 260 HOH HOH A . 
F 3 HOH 216 716 103 HOH HOH A . 
F 3 HOH 217 717 232 HOH HOH A . 
F 3 HOH 218 718 8   HOH HOH A . 
F 3 HOH 219 719 126 HOH HOH A . 
F 3 HOH 220 720 330 HOH HOH A . 
F 3 HOH 221 721 385 HOH HOH A . 
F 3 HOH 222 722 188 HOH HOH A . 
F 3 HOH 223 723 217 HOH HOH A . 
F 3 HOH 224 724 47  HOH HOH A . 
F 3 HOH 225 725 81  HOH HOH A . 
F 3 HOH 226 726 329 HOH HOH A . 
F 3 HOH 227 727 388 HOH HOH A . 
F 3 HOH 228 728 51  HOH HOH A . 
F 3 HOH 229 729 95  HOH HOH A . 
F 3 HOH 230 730 13  HOH HOH A . 
F 3 HOH 231 731 197 HOH HOH A . 
F 3 HOH 232 732 296 HOH HOH A . 
F 3 HOH 233 733 235 HOH HOH A . 
F 3 HOH 234 734 148 HOH HOH A . 
F 3 HOH 235 735 22  HOH HOH A . 
F 3 HOH 236 736 268 HOH HOH A . 
F 3 HOH 237 737 193 HOH HOH A . 
F 3 HOH 238 738 261 HOH HOH A . 
F 3 HOH 239 739 23  HOH HOH A . 
F 3 HOH 240 740 308 HOH HOH A . 
F 3 HOH 241 741 265 HOH HOH A . 
F 3 HOH 242 742 146 HOH HOH A . 
F 3 HOH 243 743 339 HOH HOH A . 
F 3 HOH 244 744 252 HOH HOH A . 
F 3 HOH 245 745 262 HOH HOH A . 
F 3 HOH 246 746 16  HOH HOH A . 
F 3 HOH 247 747 57  HOH HOH A . 
F 3 HOH 248 748 143 HOH HOH A . 
F 3 HOH 249 749 206 HOH HOH A . 
F 3 HOH 250 750 139 HOH HOH A . 
F 3 HOH 251 751 297 HOH HOH A . 
F 3 HOH 252 752 123 HOH HOH A . 
F 3 HOH 253 753 286 HOH HOH A . 
F 3 HOH 254 754 237 HOH HOH A . 
F 3 HOH 255 755 219 HOH HOH A . 
F 3 HOH 256 756 109 HOH HOH A . 
F 3 HOH 257 757 36  HOH HOH A . 
F 3 HOH 258 758 144 HOH HOH A . 
F 3 HOH 259 759 312 HOH HOH A . 
F 3 HOH 260 760 291 HOH HOH A . 
F 3 HOH 261 761 110 HOH HOH A . 
F 3 HOH 262 762 233 HOH HOH A . 
F 3 HOH 263 763 245 HOH HOH A . 
F 3 HOH 264 764 149 HOH HOH A . 
F 3 HOH 265 765 194 HOH HOH A . 
F 3 HOH 266 766 370 HOH HOH A . 
F 3 HOH 267 767 389 HOH HOH A . 
F 3 HOH 268 768 39  HOH HOH A . 
F 3 HOH 269 769 91  HOH HOH A . 
F 3 HOH 270 770 138 HOH HOH A . 
F 3 HOH 271 771 50  HOH HOH A . 
F 3 HOH 272 772 140 HOH HOH A . 
F 3 HOH 273 773 46  HOH HOH A . 
F 3 HOH 274 774 250 HOH HOH A . 
F 3 HOH 275 775 270 HOH HOH A . 
F 3 HOH 276 776 353 HOH HOH A . 
F 3 HOH 277 777 249 HOH HOH A . 
F 3 HOH 278 778 322 HOH HOH A . 
F 3 HOH 279 779 336 HOH HOH A . 
F 3 HOH 280 780 192 HOH HOH A . 
F 3 HOH 281 781 315 HOH HOH A . 
F 3 HOH 282 782 377 HOH HOH A . 
F 3 HOH 283 783 284 HOH HOH A . 
F 3 HOH 284 784 300 HOH HOH A . 
F 3 HOH 285 785 320 HOH HOH A . 
F 3 HOH 286 786 121 HOH HOH A . 
F 3 HOH 287 787 271 HOH HOH A . 
F 3 HOH 288 788 371 HOH HOH A . 
F 3 HOH 289 789 257 HOH HOH A . 
F 3 HOH 290 790 318 HOH HOH A . 
F 3 HOH 291 791 74  HOH HOH A . 
F 3 HOH 292 792 341 HOH HOH A . 
F 3 HOH 293 793 238 HOH HOH A . 
F 3 HOH 294 794 365 HOH HOH A . 
F 3 HOH 295 795 215 HOH HOH A . 
F 3 HOH 296 796 366 HOH HOH A . 
F 3 HOH 297 797 356 HOH HOH A . 
F 3 HOH 298 798 214 HOH HOH A . 
F 3 HOH 299 799 311 HOH HOH A . 
F 3 HOH 300 800 331 HOH HOH A . 
F 3 HOH 301 801 307 HOH HOH A . 
F 3 HOH 302 802 387 HOH HOH A . 
F 3 HOH 303 803 280 HOH HOH A . 
F 3 HOH 304 804 305 HOH HOH A . 
F 3 HOH 305 805 167 HOH HOH A . 
F 3 HOH 306 806 220 HOH HOH A . 
F 3 HOH 307 807 255 HOH HOH A . 
F 3 HOH 308 808 314 HOH HOH A . 
F 3 HOH 309 809 202 HOH HOH A . 
F 3 HOH 310 810 191 HOH HOH A . 
F 3 HOH 311 811 303 HOH HOH A . 
F 3 HOH 312 812 346 HOH HOH A . 
F 3 HOH 313 813 334 HOH HOH A . 
F 3 HOH 314 814 364 HOH HOH A . 
F 3 HOH 315 815 221 HOH HOH A . 
F 3 HOH 316 816 378 HOH HOH A . 
F 3 HOH 317 817 287 HOH HOH A . 
F 3 HOH 318 818 293 HOH HOH A . 
F 3 HOH 319 819 362 HOH HOH A . 
F 3 HOH 320 820 384 HOH HOH A . 
F 3 HOH 321 821 273 HOH HOH A . 
F 3 HOH 322 822 174 HOH HOH A . 
F 3 HOH 323 823 301 HOH HOH A . 
F 3 HOH 324 824 317 HOH HOH A . 
F 3 HOH 325 825 372 HOH HOH A . 
F 3 HOH 326 826 180 HOH HOH A . 
F 3 HOH 327 827 253 HOH HOH A . 
F 3 HOH 328 828 161 HOH HOH A . 
F 3 HOH 329 829 288 HOH HOH A . 
F 3 HOH 330 830 190 HOH HOH A . 
F 3 HOH 331 831 355 HOH HOH A . 
F 3 HOH 332 832 278 HOH HOH A . 
F 3 HOH 333 833 391 HOH HOH A . 
F 3 HOH 334 834 226 HOH HOH A . 
F 3 HOH 335 835 258 HOH HOH A . 
F 3 HOH 336 836 227 HOH HOH A . 
F 3 HOH 337 837 147 HOH HOH A . 
F 3 HOH 338 838 323 HOH HOH A . 
F 3 HOH 339 839 369 HOH HOH A . 
F 3 HOH 340 840 354 HOH HOH A . 
F 3 HOH 341 841 205 HOH HOH A . 
F 3 HOH 342 842 108 HOH HOH A . 
F 3 HOH 343 843 122 HOH HOH A . 
F 3 HOH 344 844 229 HOH HOH A . 
F 3 HOH 345 845 363 HOH HOH A . 
F 3 HOH 346 846 158 HOH HOH A . 
F 3 HOH 347 847 90  HOH HOH A . 
F 3 HOH 348 848 210 HOH HOH A . 
F 3 HOH 349 849 49  HOH HOH A . 
F 3 HOH 350 850 338 HOH HOH A . 
F 3 HOH 351 851 124 HOH HOH A . 
F 3 HOH 352 852 218 HOH HOH A . 
F 3 HOH 353 853 160 HOH HOH A . 
F 3 HOH 354 854 333 HOH HOH A . 
F 3 HOH 355 855 223 HOH HOH A . 
F 3 HOH 356 856 207 HOH HOH A . 
F 3 HOH 357 857 343 HOH HOH A . 
F 3 HOH 358 858 282 HOH HOH A . 
F 3 HOH 359 859 41  HOH HOH A . 
F 3 HOH 360 860 225 HOH HOH A . 
F 3 HOH 361 861 383 HOH HOH A . 
F 3 HOH 362 862 216 HOH HOH A . 
F 3 HOH 363 863 337 HOH HOH A . 
F 3 HOH 364 864 380 HOH HOH A . 
F 3 HOH 365 865 254 HOH HOH A . 
F 3 HOH 366 866 292 HOH HOH A . 
F 3 HOH 367 867 376 HOH HOH A . 
F 3 HOH 368 868 70  HOH HOH A . 
F 3 HOH 369 869 209 HOH HOH A . 
F 3 HOH 370 870 134 HOH HOH A . 
F 3 HOH 371 871 281 HOH HOH A . 
F 3 HOH 372 872 382 HOH HOH A . 
F 3 HOH 373 873 350 HOH HOH A . 
F 3 HOH 374 874 141 HOH HOH A . 
F 3 HOH 375 875 195 HOH HOH A . 
F 3 HOH 376 876 114 HOH HOH A . 
F 3 HOH 377 877 316 HOH HOH A . 
F 3 HOH 378 878 359 HOH HOH A . 
F 3 HOH 379 879 324 HOH HOH A . 
F 3 HOH 380 880 279 HOH HOH A . 
F 3 HOH 381 881 367 HOH HOH A . 
F 3 HOH 382 882 98  HOH HOH A . 
F 3 HOH 383 883 375 HOH HOH A . 
F 3 HOH 384 884 302 HOH HOH A . 
F 3 HOH 385 885 348 HOH HOH A . 
F 3 HOH 386 886 115 HOH HOH A . 
F 3 HOH 387 887 196 HOH HOH A . 
F 3 HOH 388 888 224 HOH HOH A . 
F 3 HOH 389 889 222 HOH HOH A . 
F 3 HOH 390 890 283 HOH HOH A . 
F 3 HOH 391 891 321 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
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)' 4410  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  25910 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     774 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2020-03-11 
# 
_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_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         11.7561 
_pdbx_refine_tls.origin_y         0.8392 
_pdbx_refine_tls.origin_z         4.6891 
_pdbx_refine_tls.T[1][1]          -0.0121 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0060 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0248 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0177 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0095 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0441 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.3373 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.1417 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0841 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9615 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.7793 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.4899 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0543 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0192 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0247 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0315 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0611 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0331 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0069 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0231 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0068 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     304 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
_pdbx_phasing_MR.entry_id                     6Y84 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                ? 
_pdbx_phasing_MR.R_factor                     ? 
_pdbx_phasing_MR.R_rigid_body                 0.468 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          54.910 
_pdbx_phasing_MR.d_res_low_rotation           1.740 
_pdbx_phasing_MR.d_res_high_translation       ? 
_pdbx_phasing_MR.d_res_low_translation        ? 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_phasing.method   MR 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4   1 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .       2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? BUSTER      ? ? ? .       3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25    4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? DIALS       ? ? ? .       5 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? .       6 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .       7 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 7.0.078 8 
# 
_pdbx_entry_details.entry_id                 6Y84 
_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         ? 
# 
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 ASP A 33  ? ? 57.52   -132.67 
2 1 ASN A 51  ? ? -154.49 69.76   
3 1 ASN A 84  ? ? 56.10   -119.94 
4 1 TYR A 154 ? ? 58.72   -89.93  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 889 ? 6.51 . 
2 1 O ? A HOH 890 ? 6.68 . 
3 1 O ? A HOH 891 ? 7.12 . 
# 
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 PHE 305 ? A PHE 305 
2 1 Y 1 A GLN 306 ? A GLN 306 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE' DMS 
3 water                HOH 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 homology         ? 
2 1 'gel filtration' ? 
#