data_3NSS # _entry.id 3NSS # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3NSS RCSB RCSB060234 WWPDB D_1000060234 # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 3BEQ _pdbx_database_related.details '1918 Human N1 Neuraminidase' _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3NSS _pdbx_database_status.recvd_initial_deposition_date 2010-07-02 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Li, Q.' 1 'Qi, J.X.' 2 'Zhang, W.' 3 'Vavricka, C.J.' 4 'Shi, Y.' 5 'Gao, G.F.' 6 # _citation.id primary _citation.title 'The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site' _citation.journal_abbrev Nat.Struct.Mol.Biol. _citation.journal_volume 17 _citation.page_first 1266 _citation.page_last 1268 _citation.year 2010 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1545-9993 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 20852645 _citation.pdbx_database_id_DOI 10.1038/nsmb.1909 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Li, Q.' 1 primary 'Qi, J.X.' 2 primary 'Zhang, W.' 3 primary 'Vavricka, C.J.' 4 primary 'Shi, Y.' 5 primary 'Wei, J.H.' 6 primary 'Feng, E.G.' 7 primary 'Shen, J.S.' 8 primary 'Chen, J.L.' 9 primary 'Liu, D.' 10 primary 'He, J.H.' 11 primary 'Yan, J.H.' 12 primary 'Liu, H.' 13 primary 'Jiang, H.L.' 14 primary 'Teng, M.K.' 15 primary 'Li, X.B.' 16 primary 'Gao, G.F.' 17 # _cell.entry_id 3NSS _cell.length_a 118.537 _cell.length_b 137.857 _cell.length_c 118.512 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3NSS _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 _symmetry.space_group_name_Hall ? # 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 Neuraminidase 42727.629 2 ? ? 'UNP residues 82-469' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 5 ? ? ? ? 5 non-polymer syn 'ACETATE ION' 59.044 4 ? ? ? ? 6 water nat water 18.015 889 ? ? ? ? # _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 ;SVKLAGNSSLCPVSGWAIYSKDNSVRIGSKGDVFVIREPFISCSPLECRTFFLTQGALLNDKHSNGTIKDRSPYRTLMSC PIGEVPSPYNSRFESVAWSASACHDGINWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTV MTDGPSNGQASYKIFRIEKGKIVKSVEMNAPNYHYEECSCYPDSSEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGI FGDNPRPNDKTGSCGPVSSNGANGVKGFSFKYGNGVWIGRTKSISSRNGFEMIWDPNGWTGTDNNFSIKQDIVGINEWSG YSGSFVQHPELTGLDCIRPCFWVELIRGRPKENTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK ; _entity_poly.pdbx_seq_one_letter_code_can ;SVKLAGNSSLCPVSGWAIYSKDNSVRIGSKGDVFVIREPFISCSPLECRTFFLTQGALLNDKHSNGTIKDRSPYRTLMSC PIGEVPSPYNSRFESVAWSASACHDGINWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTV MTDGPSNGQASYKIFRIEKGKIVKSVEMNAPNYHYEECSCYPDSSEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGI FGDNPRPNDKTGSCGPVSSNGANGVKGFSFKYGNGVWIGRTKSISSRNGFEMIWDPNGWTGTDNNFSIKQDIVGINEWSG YSGSFVQHPELTGLDCIRPCFWVELIRGRPKENTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK ; _entity_poly.pdbx_strand_id A,B _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 VAL n 1 3 LYS n 1 4 LEU n 1 5 ALA n 1 6 GLY n 1 7 ASN n 1 8 SER n 1 9 SER n 1 10 LEU n 1 11 CYS n 1 12 PRO n 1 13 VAL n 1 14 SER n 1 15 GLY n 1 16 TRP n 1 17 ALA n 1 18 ILE n 1 19 TYR n 1 20 SER n 1 21 LYS n 1 22 ASP n 1 23 ASN n 1 24 SER n 1 25 VAL n 1 26 ARG n 1 27 ILE n 1 28 GLY n 1 29 SER n 1 30 LYS n 1 31 GLY n 1 32 ASP n 1 33 VAL n 1 34 PHE n 1 35 VAL n 1 36 ILE n 1 37 ARG n 1 38 GLU n 1 39 PRO n 1 40 PHE n 1 41 ILE n 1 42 SER n 1 43 CYS n 1 44 SER n 1 45 PRO n 1 46 LEU n 1 47 GLU n 1 48 CYS n 1 49 ARG n 1 50 THR n 1 51 PHE n 1 52 PHE n 1 53 LEU n 1 54 THR n 1 55 GLN n 1 56 GLY n 1 57 ALA n 1 58 LEU n 1 59 LEU n 1 60 ASN n 1 61 ASP n 1 62 LYS n 1 63 HIS n 1 64 SER n 1 65 ASN n 1 66 GLY n 1 67 THR n 1 68 ILE n 1 69 LYS n 1 70 ASP n 1 71 ARG n 1 72 SER n 1 73 PRO n 1 74 TYR n 1 75 ARG n 1 76 THR n 1 77 LEU n 1 78 MET n 1 79 SER n 1 80 CYS n 1 81 PRO n 1 82 ILE n 1 83 GLY n 1 84 GLU n 1 85 VAL n 1 86 PRO n 1 87 SER n 1 88 PRO n 1 89 TYR n 1 90 ASN n 1 91 SER n 1 92 ARG n 1 93 PHE n 1 94 GLU n 1 95 SER n 1 96 VAL n 1 97 ALA n 1 98 TRP n 1 99 SER n 1 100 ALA n 1 101 SER n 1 102 ALA n 1 103 CYS n 1 104 HIS n 1 105 ASP n 1 106 GLY n 1 107 ILE n 1 108 ASN n 1 109 TRP n 1 110 LEU n 1 111 THR n 1 112 ILE n 1 113 GLY n 1 114 ILE n 1 115 SER n 1 116 GLY n 1 117 PRO n 1 118 ASP n 1 119 ASN n 1 120 GLY n 1 121 ALA n 1 122 VAL n 1 123 ALA n 1 124 VAL n 1 125 LEU n 1 126 LYS n 1 127 TYR n 1 128 ASN n 1 129 GLY n 1 130 ILE n 1 131 ILE n 1 132 THR n 1 133 ASP n 1 134 THR n 1 135 ILE n 1 136 LYS n 1 137 SER n 1 138 TRP n 1 139 ARG n 1 140 ASN n 1 141 ASN n 1 142 ILE n 1 143 LEU n 1 144 ARG n 1 145 THR n 1 146 GLN n 1 147 GLU n 1 148 SER n 1 149 GLU n 1 150 CYS n 1 151 ALA n 1 152 CYS n 1 153 VAL n 1 154 ASN n 1 155 GLY n 1 156 SER n 1 157 CYS n 1 158 PHE n 1 159 THR n 1 160 VAL n 1 161 MET n 1 162 THR n 1 163 ASP n 1 164 GLY n 1 165 PRO n 1 166 SER n 1 167 ASN n 1 168 GLY n 1 169 GLN n 1 170 ALA n 1 171 SER n 1 172 TYR n 1 173 LYS n 1 174 ILE n 1 175 PHE n 1 176 ARG n 1 177 ILE n 1 178 GLU n 1 179 LYS n 1 180 GLY n 1 181 LYS n 1 182 ILE n 1 183 VAL n 1 184 LYS n 1 185 SER n 1 186 VAL n 1 187 GLU n 1 188 MET n 1 189 ASN n 1 190 ALA n 1 191 PRO n 1 192 ASN n 1 193 TYR n 1 194 HIS n 1 195 TYR n 1 196 GLU n 1 197 GLU n 1 198 CYS n 1 199 SER n 1 200 CYS n 1 201 TYR n 1 202 PRO n 1 203 ASP n 1 204 SER n 1 205 SER n 1 206 GLU n 1 207 ILE n 1 208 THR n 1 209 CYS n 1 210 VAL n 1 211 CYS n 1 212 ARG n 1 213 ASP n 1 214 ASN n 1 215 TRP n 1 216 HIS n 1 217 GLY n 1 218 SER n 1 219 ASN n 1 220 ARG n 1 221 PRO n 1 222 TRP n 1 223 VAL n 1 224 SER n 1 225 PHE n 1 226 ASN n 1 227 GLN n 1 228 ASN n 1 229 LEU n 1 230 GLU n 1 231 TYR n 1 232 GLN n 1 233 ILE n 1 234 GLY n 1 235 TYR n 1 236 ILE n 1 237 CYS n 1 238 SER n 1 239 GLY n 1 240 ILE n 1 241 PHE n 1 242 GLY n 1 243 ASP n 1 244 ASN n 1 245 PRO n 1 246 ARG n 1 247 PRO n 1 248 ASN n 1 249 ASP n 1 250 LYS n 1 251 THR n 1 252 GLY n 1 253 SER n 1 254 CYS n 1 255 GLY n 1 256 PRO n 1 257 VAL n 1 258 SER n 1 259 SER n 1 260 ASN n 1 261 GLY n 1 262 ALA n 1 263 ASN n 1 264 GLY n 1 265 VAL n 1 266 LYS n 1 267 GLY n 1 268 PHE n 1 269 SER n 1 270 PHE n 1 271 LYS n 1 272 TYR n 1 273 GLY n 1 274 ASN n 1 275 GLY n 1 276 VAL n 1 277 TRP n 1 278 ILE n 1 279 GLY n 1 280 ARG n 1 281 THR n 1 282 LYS n 1 283 SER n 1 284 ILE n 1 285 SER n 1 286 SER n 1 287 ARG n 1 288 ASN n 1 289 GLY n 1 290 PHE n 1 291 GLU n 1 292 MET n 1 293 ILE n 1 294 TRP n 1 295 ASP n 1 296 PRO n 1 297 ASN n 1 298 GLY n 1 299 TRP n 1 300 THR n 1 301 GLY n 1 302 THR n 1 303 ASP n 1 304 ASN n 1 305 ASN n 1 306 PHE n 1 307 SER n 1 308 ILE n 1 309 LYS n 1 310 GLN n 1 311 ASP n 1 312 ILE n 1 313 VAL n 1 314 GLY n 1 315 ILE n 1 316 ASN n 1 317 GLU n 1 318 TRP n 1 319 SER n 1 320 GLY n 1 321 TYR n 1 322 SER n 1 323 GLY n 1 324 SER n 1 325 PHE n 1 326 VAL n 1 327 GLN n 1 328 HIS n 1 329 PRO n 1 330 GLU n 1 331 LEU n 1 332 THR n 1 333 GLY n 1 334 LEU n 1 335 ASP n 1 336 CYS n 1 337 ILE n 1 338 ARG n 1 339 PRO n 1 340 CYS n 1 341 PHE n 1 342 TRP n 1 343 VAL n 1 344 GLU n 1 345 LEU n 1 346 ILE n 1 347 ARG n 1 348 GLY n 1 349 ARG n 1 350 PRO n 1 351 LYS n 1 352 GLU n 1 353 ASN n 1 354 THR n 1 355 ILE n 1 356 TRP n 1 357 THR n 1 358 SER n 1 359 GLY n 1 360 SER n 1 361 SER n 1 362 ILE n 1 363 SER n 1 364 PHE n 1 365 CYS n 1 366 GLY n 1 367 VAL n 1 368 ASN n 1 369 SER n 1 370 ASP n 1 371 THR n 1 372 VAL n 1 373 GLY n 1 374 TRP n 1 375 SER n 1 376 TRP n 1 377 PRO n 1 378 ASP n 1 379 GLY n 1 380 ALA n 1 381 GLU n 1 382 LEU n 1 383 PRO n 1 384 PHE n 1 385 THR n 1 386 ILE n 1 387 ASP n 1 388 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene NA _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'A/California/04/2009 H1N1' _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 'Influenza A virus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 641501 _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 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _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 SF9 _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 Baculovirus _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pAcGP67-B _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code C3W5S3_I09A0 _struct_ref.pdbx_db_accession C3W5S3 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;SVKLAGNSSLCPVSGWAIYSKDNSVRIGSKGDVFVIREPFISCSPLECRTFFLTQGALLNDKHSNGTIKDRSPYRTLMSC PIGEVPSPYNSRFESVAWSASACHDGINWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTV MTDGPSNGQASYKIFRIEKGKIVKSVEMNAPNYHYEECSCYPDSSEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGI FGDNPRPNDKTGSCGPVSSNGANGVKGFSFKYGNGVWIGRTKSISSRNGFEMIWDPNGWTGTDNNFSIKQDIVGINEWSG YSGSFVQHPELTGLDCIRPCFWVELIRGRPKENTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK ; _struct_ref.pdbx_align_begin 82 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3NSS A 1 ? 388 ? C3W5S3 82 ? 469 ? 82 470 2 1 3NSS B 1 ? 388 ? C3W5S3 82 ? 469 ? 82 470 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 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.entry_id 3NSS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.83 _exptl_crystal.density_percent_sol 56.58 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 291 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_details ;0.16M calcium acetate hydrate, 0.08M sodium cacodylate trihydrate, 14.4% polyethylene glycol 8000, 20% glycerol , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K ; _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2010-01-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9793 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRF BEAMLINE BL17U' _diffrn_source.pdbx_synchrotron_site SSRF _diffrn_source.pdbx_synchrotron_beamline BL17U _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9793 # _reflns.entry_id 3NSS _reflns.observed_criterion_sigma_I 4 _reflns.observed_criterion_sigma_F 2.0 _reflns.d_resolution_low 50 _reflns.d_resolution_high 1.9 _reflns.number_obs 75980 _reflns.number_all 75980 _reflns.percent_possible_obs 100 _reflns.pdbx_Rmerge_I_obs 0.163 _reflns.pdbx_Rsym_value 0.163 _reflns.pdbx_netI_over_sigmaI 14.4 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 8.3 _reflns.R_free_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.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.entry_id 3NSS _refine.ls_number_reflns_obs 73349 _refine.ls_number_reflns_all 73349 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.10 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 31.977 _refine.ls_d_res_high 1.902 _refine.ls_percent_reflns_obs 96.30 _refine.ls_R_factor_obs 0.1706 _refine.ls_R_factor_all 0.1719 _refine.ls_R_factor_R_work 0.1693 _refine.ls_R_factor_R_free 0.1955 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.03 _refine.ls_number_reflns_R_free 3688 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] -1.1145 _refine.aniso_B[2][2] 3.3061 _refine.aniso_B[3][3] -2.1917 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] -0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.367 _refine.solvent_model_param_bsol 42.027 _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.19 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5982 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 113 _refine_hist.number_atoms_solvent 889 _refine_hist.number_atoms_total 6984 _refine_hist.d_res_high 1.902 _refine_hist.d_res_low 31.977 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.003 ? ? 6275 'X-RAY DIFFRACTION' ? f_angle_d 0.810 ? ? 8512 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 19.513 ? ? 2229 'X-RAY DIFFRACTION' ? f_chiral_restr 0.055 ? ? 903 'X-RAY DIFFRACTION' ? f_plane_restr 0.003 ? ? 1103 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.redundancy_reflns_obs 'X-RAY DIFFRACTION' . 1.9023 1.9273 2333 0.1947 85.00 0.2576 . . 117 . . . . 'X-RAY DIFFRACTION' . 1.9273 1.9537 2514 0.1769 91.00 0.2158 . . 125 . . . . 'X-RAY DIFFRACTION' . 1.9537 1.9816 2545 0.1773 93.00 0.1995 . . 151 . . . . 'X-RAY DIFFRACTION' . 1.9816 2.0112 2595 0.1713 93.00 0.2081 . . 115 . . . . 'X-RAY DIFFRACTION' . 2.0112 2.0426 2603 0.1677 94.00 0.2204 . . 145 . . . . 'X-RAY DIFFRACTION' . 2.0426 2.0761 2587 0.1566 94.00 0.2131 . . 134 . . . . 'X-RAY DIFFRACTION' . 2.0761 2.1119 2620 0.1554 95.00 0.2035 . . 145 . . . . 'X-RAY DIFFRACTION' . 2.1119 2.1503 2618 0.1521 95.00 0.2061 . . 137 . . . . 'X-RAY DIFFRACTION' . 2.1503 2.1916 2670 0.1611 96.00 0.1867 . . 126 . . . . 'X-RAY DIFFRACTION' . 2.1916 2.2363 2660 0.1619 96.00 0.1769 . . 139 . . . . 'X-RAY DIFFRACTION' . 2.2363 2.2849 2640 0.1701 96.00 0.1965 . . 143 . . . . 'X-RAY DIFFRACTION' . 2.2849 2.3381 2715 0.1753 97.00 0.2129 . . 121 . . . . 'X-RAY DIFFRACTION' . 2.3381 2.3965 2662 0.1697 97.00 0.1853 . . 137 . . . . 'X-RAY DIFFRACTION' . 2.3965 2.4613 2684 0.1711 97.00 0.1990 . . 145 . . . . 'X-RAY DIFFRACTION' . 2.4613 2.5337 2664 0.1741 97.00 0.2101 . . 151 . . . . 'X-RAY DIFFRACTION' . 2.5337 2.6155 2691 0.1775 97.00 0.1998 . . 156 . . . . 'X-RAY DIFFRACTION' . 2.6155 2.7089 2721 0.1823 98.00 0.2182 . . 129 . . . . 'X-RAY DIFFRACTION' . 2.7089 2.8173 2762 0.1744 98.00 0.2064 . . 133 . . . . 'X-RAY DIFFRACTION' . 2.8173 2.9454 2719 0.1707 98.00 0.1950 . . 146 . . . . 'X-RAY DIFFRACTION' . 2.9454 3.1006 2756 0.1647 99.00 0.1973 . . 151 . . . . 'X-RAY DIFFRACTION' . 3.1006 3.2947 2773 0.1545 99.00 0.1737 . . 165 . . . . 'X-RAY DIFFRACTION' . 3.2947 3.5487 2765 0.1492 99.00 0.1524 . . 145 . . . . 'X-RAY DIFFRACTION' . 3.5487 3.9053 2784 0.1542 99.00 0.1888 . . 149 . . . . 'X-RAY DIFFRACTION' . 3.9053 4.4691 2780 0.1484 100.00 0.1631 . . 187 . . . . 'X-RAY DIFFRACTION' . 4.4691 5.6256 2845 0.1650 99.00 0.1769 . . 153 . . . . 'X-RAY DIFFRACTION' . 5.6256 31.9820 2955 0.2244 100.00 0.2332 . . 143 . . . . # _struct.entry_id 3NSS _struct.title 'The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active sites' _struct.pdbx_descriptor Neuraminidase _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3NSS _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text '6-BLADED BETA-PROPELLER, HYDROLASE, Calcium Binding, Glycosylation' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 2 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 5 ? L N N 5 ? M N N 5 ? N N N 2 ? O N N 2 ? P N N 4 ? Q N N 4 ? R N N 5 ? S N N 6 ? T N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # 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 1 ASN A 23 ? SER A 29 ? ASN A 104 SER A 110 1 ? 7 HELX_P HELX_P2 2 ASP A 61 ? ASN A 65 ? ASP A 142 ASN A 146 5 ? 5 HELX_P HELX_P3 3 HIS A 328 A GLY A 333 ? HIS A 412 GLY A 414 1 ? 6 HELX_P HELX_P4 4 ASN B 23 ? SER B 29 ? ASN B 104 SER B 110 1 ? 7 HELX_P HELX_P5 5 ASP B 61 ? ASN B 65 ? ASP B 142 ASN B 146 5 ? 5 HELX_P HELX_P6 6 HIS B 328 A GLY B 333 ? HIS B 412 GLY B 414 1 ? 6 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 11 SG ? ? ? 1_555 A CYS 336 SG ? ? A CYS 92 A CYS 417 1_555 ? ? ? ? ? ? ? 2.033 ? disulf2 disulf ? ? A CYS 43 SG ? ? ? 1_555 A CYS 48 SG ? ? A CYS 124 A CYS 129 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 103 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 183 A CYS 230 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? A CYS 152 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 232 A CYS 237 1_555 ? ? ? ? ? ? ? 2.055 ? disulf5 disulf ? ? A CYS 198 SG ? ? ? 1_555 A CYS 211 SG ? ? A CYS 278 A CYS 291 1_555 ? ? ? ? ? ? ? 2.041 ? disulf6 disulf ? ? A CYS 200 SG ? ? ? 1_555 A CYS 209 SG ? ? A CYS 280 A CYS 289 1_555 ? ? ? ? ? ? ? 2.034 ? disulf7 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 254 SG ? ? A CYS 318 A CYS 336 1_555 ? ? ? ? ? ? ? 2.035 ? disulf8 disulf ? ? A CYS 340 SG ? ? ? 1_555 A CYS 365 SG ? ? A CYS 421 A CYS 447 1_555 ? ? ? ? ? ? ? 2.042 ? disulf9 disulf ? ? B CYS 11 SG ? ? ? 1_555 B CYS 336 SG ? ? B CYS 92 B CYS 417 1_555 ? ? ? ? ? ? ? 2.034 ? disulf10 disulf ? ? B CYS 43 SG ? ? ? 1_555 B CYS 48 SG ? ? B CYS 124 B CYS 129 1_555 ? ? ? ? ? ? ? 2.045 ? disulf11 disulf ? ? B CYS 103 SG ? ? ? 1_555 B CYS 150 SG ? ? B CYS 183 B CYS 230 1_555 ? ? ? ? ? ? ? 2.038 ? disulf12 disulf ? ? B CYS 152 SG ? ? ? 1_555 B CYS 157 SG ? ? B CYS 232 B CYS 237 1_555 ? ? ? ? ? ? ? 2.035 ? disulf13 disulf ? ? B CYS 198 SG ? ? ? 1_555 B CYS 211 SG ? ? B CYS 278 B CYS 291 1_555 ? ? ? ? ? ? ? 2.044 ? disulf14 disulf ? ? B CYS 200 SG ? ? ? 1_555 B CYS 209 SG ? ? B CYS 280 B CYS 289 1_555 ? ? ? ? ? ? ? 2.033 ? disulf15 disulf ? ? B CYS 237 SG ? ? ? 1_555 B CYS 254 SG ? ? B CYS 318 B CYS 336 1_555 ? ? ? ? ? ? ? 2.037 ? disulf16 disulf ? ? B CYS 340 SG ? ? ? 1_555 B CYS 365 SG ? ? B CYS 421 B CYS 447 1_555 ? ? ? ? ? ? ? 2.070 ? covale1 covale ? ? D NAG . O4 ? ? ? 1_555 E MAN . C1 ? ? A NAG 502 A MAN 503 1_555 ? ? ? ? ? ? ? 1.436 ? covale2 covale ? ? B ASN 65 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 146 B NAG 501 1_555 ? ? ? ? ? ? ? 1.436 ? covale3 covale ? ? B ASN 7 ND2 ? ? ? 1_555 O NAG . C1 ? ? B ASN 88 B NAG 502 1_555 ? ? ? ? ? ? ? 1.438 ? covale4 covale ? ? E MAN . O3 ? ? ? 1_555 F MAN . C1 ? ? A MAN 503 A MAN 504 1_555 ? ? ? ? ? ? ? 1.439 ? covale5 covale ? ? A ASN 7 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 88 A NAG 505 1_555 ? ? ? ? ? ? ? 1.441 ? covale6 covale ? ? A ASN 65 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 146 A NAG 501 1_555 ? ? ? ? ? ? ? 1.442 ? covale7 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.443 ? metalc1 metalc ? ? B ASP 295 OD1 ? ? ? 1_555 Q CA . CA ? ? B ASP 379 B CA 602 1_555 ? ? ? ? ? ? ? 2.455 ? metalc2 metalc ? ? B ASN 263 O ? ? ? 1_555 P CA . CA ? ? B ASN 347 B CA 601 1_555 ? ? ? ? ? ? ? 2.456 ? metalc3 metalc ? ? A ASN 263 O ? ? ? 1_555 H CA . CA ? ? A ASN 347 A CA 601 1_555 ? ? ? ? ? ? ? 2.464 ? metalc4 metalc ? ? B ASP 213 O ? ? ? 1_555 P CA . CA ? ? B ASP 293 B CA 601 1_555 ? ? ? ? ? ? ? 2.482 ? metalc5 metalc ? ? A ASP 213 O ? ? ? 1_555 H CA . CA ? ? A ASP 293 A CA 601 1_555 ? ? ? ? ? ? ? 2.493 ? metalc6 metalc ? ? B ASN 297 OD1 ? ? ? 1_555 Q CA . CA ? ? B ASN 381 B CA 602 1_555 ? ? ? ? ? ? ? 2.496 ? metalc7 metalc ? ? A ASN 297 OD1 ? ? ? 1_555 I CA . CA ? ? A ASN 381 A CA 602 1_555 ? ? ? ? ? ? ? 2.498 ? metalc8 metalc ? ? A ASP 295 OD1 ? ? ? 1_555 I CA . CA ? ? A ASP 379 A CA 602 1_555 ? ? ? ? ? ? ? 2.501 ? metalc9 metalc ? ? B ASP 243 OD2 ? ? ? 1_555 P CA . CA ? ? B ASP 324 B CA 601 1_555 ? ? ? ? ? ? ? 2.506 ? metalc10 metalc ? ? A ASP 243 OD2 ? ? ? 1_555 H CA . CA ? ? A ASP 324 A CA 601 1_555 ? ? ? ? ? ? ? 2.522 ? metalc11 metalc ? ? A GLY 261 O ? ? ? 1_555 H CA . CA ? ? A GLY 345 A CA 601 1_555 ? ? ? ? ? ? ? 2.541 ? metalc12 metalc ? ? B GLY 217 O ? ? ? 1_555 P CA . CA ? ? B GLY 297 B CA 601 1_555 ? ? ? ? ? ? ? 2.552 ? metalc13 metalc ? ? B GLY 261 O ? ? ? 1_555 P CA . CA ? ? B GLY 345 B CA 601 1_555 ? ? ? ? ? ? ? 2.561 ? metalc14 metalc ? ? A GLY 217 O ? ? ? 1_555 H CA . CA ? ? A GLY 297 A CA 601 1_555 ? ? ? ? ? ? ? 2.590 ? metalc15 metalc ? ? A ASN 305 O ? ? ? 1_555 I CA . CA ? ? A ASN 389 A CA 602 1_555 ? ? ? ? ? ? ? 2.601 ? metalc16 metalc ? ? B ASN 305 O ? ? ? 1_555 Q CA . CA ? ? B ASN 389 B CA 602 1_555 ? ? ? ? ? ? ? 2.606 ? metalc17 metalc ? ? B ASP 303 OD1 ? ? ? 1_555 Q CA . CA ? ? B ASP 387 B CA 602 1_555 ? ? ? ? ? ? ? 2.614 ? metalc18 metalc ? ? A ASP 303 OD1 ? ? ? 1_555 I CA . CA ? ? A ASP 387 A CA 602 1_555 ? ? ? ? ? ? ? 2.633 ? metalc19 metalc ? ? B ASP 295 OD2 ? ? ? 1_555 Q CA . CA ? ? B ASP 379 B CA 602 1_555 ? ? ? ? ? ? ? 2.995 ? metalc20 metalc ? ? A ASP 295 OD2 ? ? ? 1_555 I CA . CA ? ? A ASP 379 A CA 602 1_555 ? ? ? ? ? ? ? 3.143 ? metalc21 metalc ? ? J CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 603 B HOH 903 1_555 ? ? ? ? ? ? ? 2.477 ? metalc22 metalc ? ? I CA . CA ? ? ? 1_555 S HOH . O ? ? A CA 602 A HOH 565 1_555 ? ? ? ? ? ? ? 2.587 ? metalc23 metalc ? ? J CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 603 B HOH 905 1_555 ? ? ? ? ? ? ? 2.592 ? metalc24 metalc ? ? H CA . CA ? ? ? 1_555 S HOH . O ? ? A CA 601 A HOH 476 1_555 ? ? ? ? ? ? ? 2.603 ? metalc25 metalc ? ? P CA . CA ? ? ? 1_555 T HOH . O ? ? B CA 601 B HOH 3 1_555 ? ? ? ? ? ? ? 2.613 ? metalc26 metalc ? ? I CA . CA ? ? ? 1_555 S HOH . O ? ? A CA 602 A HOH 493 1_555 ? ? ? ? ? ? ? 2.625 ? metalc27 metalc ? ? J CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 603 B HOH 902 1_555 ? ? ? ? ? ? ? 2.653 ? metalc28 metalc ? ? Q CA . CA ? ? ? 1_555 T HOH . O ? ? B CA 602 B HOH 56 1_555 ? ? ? ? ? ? ? 2.828 ? metalc29 metalc ? ? Q CA . CA ? ? ? 1_555 T HOH . O ? ? B CA 602 B HOH 575 1_555 ? ? ? ? ? ? ? 2.900 ? metalc30 metalc ? ? J CA . CA ? ? ? 1_555 T HOH . O ? ? A CA 603 B HOH 488 1_555 ? ? ? ? ? ? ? 2.903 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 244 A . ? ASN 325 A PRO 245 A ? PRO 326 A 1 4.73 2 ARG 349 A . ? ARG 430 A PRO 350 A ? PRO 431 A 1 0.97 3 LEU 382 A . ? LEU 464 A PRO 383 A ? PRO 465 A 1 0.01 4 ASN 244 B . ? ASN 325 B PRO 245 B ? PRO 326 B 1 4.52 5 ARG 349 B . ? ARG 430 B PRO 350 B ? PRO 431 B 1 2.12 6 LEU 382 B . ? LEU 464 B PRO 383 B ? PRO 465 B 1 -0.50 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? H ? 4 ? I ? 4 ? J ? 4 ? K ? 4 ? L ? 4 ? # 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 A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel K 3 4 ? anti-parallel L 1 2 ? anti-parallel L 2 3 ? anti-parallel L 3 4 ? 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 A 1 GLY A 15 ? LYS A 21 ? GLY A 96 LYS A 102 A 2 THR A 357 ? VAL A 367 ? THR A 439 VAL A 449 A 3 ARG A 338 ? GLY A 348 ? ARG A 419 GLY A 429 A 4 SER A 322 ? GLN A 327 ? SER A 407 GLN A 412 B 1 PHE A 34 ? CYS A 43 ? PHE A 115 CYS A 124 B 2 CYS A 48 ? LEU A 58 ? CYS A 129 LEU A 139 B 3 THR A 76 ? PRO A 81 ? THR A 157 PRO A 162 B 4 ARG A 92 ? VAL A 96 ? ARG A 172 VAL A 176 C 1 SER A 99 ? HIS A 104 ? SER A 179 HIS A 184 C 2 TRP A 109 ? SER A 115 ? TRP A 189 SER A 195 C 3 VAL A 122 ? TYR A 127 ? VAL A 202 TYR A 207 C 4 ILE A 130 ? LYS A 136 ? ILE A 210 LYS A 216 D 1 ALA A 151 ? VAL A 153 ? ALA A 231 VAL A 233 D 2 SER A 156 ? ASP A 163 ? SER A 236 ASP A 243 D 3 SER A 171 ? GLU A 178 ? SER A 251 GLU A 258 D 4 LYS A 181 ? GLU A 187 ? LYS A 261 GLU A 267 E 1 GLU A 196 ? ASP A 203 ? GLU A 276 ASP A 283 E 2 GLU A 206 ? ARG A 212 ? GLU A 286 ARG A 292 E 3 PRO A 221 ? PHE A 225 ? PRO A 301 PHE A 305 E 4 TYR A 231 ? TYR A 235 ? TYR A 312 TYR A 316 F 1 SER A 269 ? TYR A 272 ? SER A 353 TYR A 356 F 2 GLY A 275 ? ARG A 280 ? GLY A 359 ARG A 364 F 3 ASN A 288 ? ASP A 295 ? ASN A 372 ASP A 379 F 4 ILE A 308 ? TRP A 318 ? ILE A 392 TRP A 403 G 1 GLY B 15 ? LYS B 21 ? GLY B 96 LYS B 102 G 2 THR B 357 ? VAL B 367 ? THR B 439 VAL B 449 G 3 ARG B 338 ? GLY B 348 ? ARG B 419 GLY B 429 G 4 SER B 322 ? GLN B 327 ? SER B 407 GLN B 412 H 1 PHE B 34 ? CYS B 43 ? PHE B 115 CYS B 124 H 2 CYS B 48 ? LEU B 58 ? CYS B 129 LEU B 139 H 3 THR B 76 ? PRO B 81 ? THR B 157 PRO B 162 H 4 ARG B 92 ? VAL B 96 ? ARG B 172 VAL B 176 I 1 SER B 99 ? HIS B 104 ? SER B 179 HIS B 184 I 2 TRP B 109 ? SER B 115 ? TRP B 189 SER B 195 I 3 VAL B 122 ? TYR B 127 ? VAL B 202 TYR B 207 I 4 ILE B 130 ? LYS B 136 ? ILE B 210 LYS B 216 J 1 ALA B 151 ? VAL B 153 ? ALA B 231 VAL B 233 J 2 SER B 156 ? ASP B 163 ? SER B 236 ASP B 243 J 3 SER B 171 ? GLU B 178 ? SER B 251 GLU B 258 J 4 LYS B 181 ? GLU B 187 ? LYS B 261 GLU B 267 K 1 GLU B 196 ? ASP B 203 ? GLU B 276 ASP B 283 K 2 GLU B 206 ? ARG B 212 ? GLU B 286 ARG B 292 K 3 PRO B 221 ? PHE B 225 ? PRO B 301 PHE B 305 K 4 TYR B 231 ? TYR B 235 ? TYR B 312 TYR B 316 L 1 SER B 269 ? TYR B 272 ? SER B 353 TYR B 356 L 2 GLY B 275 ? ARG B 280 ? GLY B 359 ARG B 364 L 3 ASN B 288 ? ASP B 295 ? ASN B 372 ASP B 379 L 4 ILE B 308 ? TRP B 318 ? ILE B 392 TRP B 403 # 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 A 1 2 N TYR A 19 ? N TYR A 100 O SER A 363 ? O SER A 445 A 2 3 O SER A 358 ? O SER A 440 N ARG A 347 ? N ARG A 428 A 3 4 O CYS A 340 ? O CYS A 421 N PHE A 325 ? N PHE A 410 B 1 2 N PHE A 40 ? N PHE A 121 O PHE A 51 ? O PHE A 132 B 2 3 N THR A 50 ? N THR A 131 O CYS A 80 ? O CYS A 161 B 3 4 N LEU A 77 ? N LEU A 158 O SER A 95 ? O SER A 175 C 1 2 N CYS A 103 ? N CYS A 183 O LEU A 110 ? O LEU A 190 C 2 3 N GLY A 113 ? N GLY A 193 O VAL A 124 ? O VAL A 204 C 3 4 N LEU A 125 ? N LEU A 205 O THR A 132 ? O THR A 212 D 1 2 N VAL A 153 ? N VAL A 233 O SER A 156 ? O SER A 236 D 2 3 N CYS A 157 ? N CYS A 237 O ILE A 177 ? O ILE A 257 D 3 4 N ARG A 176 ? N ARG A 256 O LYS A 184 ? O LYS A 264 E 1 2 N SER A 199 ? N SER A 279 O VAL A 210 ? O VAL A 290 E 2 3 N ILE A 207 ? N ILE A 287 O PHE A 225 ? O PHE A 305 E 3 4 N TRP A 222 ? N TRP A 302 O GLY A 234 ? O GLY A 315 F 1 2 N PHE A 270 ? N PHE A 354 O TRP A 277 ? O TRP A 361 F 2 3 N ILE A 278 ? N ILE A 362 O ILE A 293 ? O ILE A 377 F 3 4 N MET A 292 ? N MET A 376 O GLN A 310 ? O GLN A 395 G 1 2 N TYR B 19 ? N TYR B 100 O SER B 363 ? O SER B 445 G 2 3 O SER B 358 ? O SER B 440 N ARG B 347 ? N ARG B 428 G 3 4 O CYS B 340 ? O CYS B 421 N PHE B 325 ? N PHE B 410 H 1 2 N PHE B 40 ? N PHE B 121 O PHE B 51 ? O PHE B 132 H 2 3 N THR B 50 ? N THR B 131 O CYS B 80 ? O CYS B 161 H 3 4 N LEU B 77 ? N LEU B 158 O SER B 95 ? O SER B 175 I 1 2 N SER B 101 ? N SER B 181 O ILE B 112 ? O ILE B 192 I 2 3 N GLY B 113 ? N GLY B 193 O VAL B 124 ? O VAL B 204 I 3 4 N ALA B 123 ? N ALA B 203 O ILE B 135 ? O ILE B 215 J 1 2 N VAL B 153 ? N VAL B 233 O SER B 156 ? O SER B 236 J 2 3 N CYS B 157 ? N CYS B 237 O ILE B 177 ? O ILE B 257 J 3 4 N ARG B 176 ? N ARG B 256 O LYS B 184 ? O LYS B 264 K 1 2 N SER B 199 ? N SER B 279 O VAL B 210 ? O VAL B 290 K 2 3 N ILE B 207 ? N ILE B 287 O PHE B 225 ? O PHE B 305 K 3 4 N TRP B 222 ? N TRP B 302 O GLY B 234 ? O GLY B 315 L 1 2 N PHE B 270 ? N PHE B 354 O TRP B 277 ? O TRP B 361 L 2 3 N ILE B 278 ? N ILE B 362 O ILE B 293 ? O ILE B 377 L 3 4 N MET B 292 ? N MET B 376 O GLN B 310 ? O GLN B 395 # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 501' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 502' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN A 503' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MAN A 504' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 505' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 601' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 602' AC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE CA A 603' AC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACT A 1' BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE ACT A 471' BC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE ACT A 472' BC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 501' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 502' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA B 601' BC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA B 602' BC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE ACT B 1' # 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 5 ASN A 65 ? ASN A 146 . ? 1_555 ? 2 AC1 5 NAG D . ? NAG A 502 . ? 1_555 ? 3 AC1 5 HOH S . ? HOH A 617 . ? 1_555 ? 4 AC1 5 HOH S . ? HOH A 834 . ? 1_555 ? 5 AC1 5 HOH S . ? HOH A 891 . ? 1_555 ? 6 AC2 3 NAG C . ? NAG A 501 . ? 1_555 ? 7 AC2 3 MAN E . ? MAN A 503 . ? 1_555 ? 8 AC2 3 ASN B 248 ? ASN B 329 . ? 2_554 ? 9 AC3 3 NAG D . ? NAG A 502 . ? 1_555 ? 10 AC3 3 MAN F . ? MAN A 504 . ? 1_555 ? 11 AC3 3 HOH T . ? HOH B 683 . ? 2_554 ? 12 AC4 6 MAN E . ? MAN A 503 . ? 1_555 ? 13 AC4 6 ARG B 246 ? ARG B 327 . ? 2_554 ? 14 AC4 6 ASP B 249 ? ASP B 330 . ? 2_554 ? 15 AC4 6 ARG B 280 ? ARG B 364 . ? 2_554 ? 16 AC4 6 LYS B 282 ? LYS B 366 . ? 2_554 ? 17 AC4 6 GLU B 291 ? GLU B 375 . ? 2_554 ? 18 AC5 6 ALA A 5 ? ALA A 86 . ? 1_555 ? 19 AC5 6 ASN A 7 ? ASN A 88 . ? 1_555 ? 20 AC5 6 HOH S . ? HOH A 718 . ? 1_555 ? 21 AC5 6 HOH S . ? HOH A 745 . ? 1_555 ? 22 AC5 6 HOH S . ? HOH A 768 . ? 1_555 ? 23 AC5 6 HOH S . ? HOH A 843 . ? 1_555 ? 24 AC6 6 ASP A 213 ? ASP A 293 . ? 1_555 ? 25 AC6 6 GLY A 217 ? GLY A 297 . ? 1_555 ? 26 AC6 6 ASP A 243 ? ASP A 324 . ? 1_555 ? 27 AC6 6 GLY A 261 ? GLY A 345 . ? 1_555 ? 28 AC6 6 ASN A 263 ? ASN A 347 . ? 1_555 ? 29 AC6 6 HOH S . ? HOH A 476 . ? 1_555 ? 30 AC7 6 ASP A 295 ? ASP A 379 . ? 1_555 ? 31 AC7 6 ASN A 297 ? ASN A 381 . ? 1_555 ? 32 AC7 6 ASP A 303 ? ASP A 387 . ? 1_555 ? 33 AC7 6 ASN A 305 ? ASN A 389 . ? 1_555 ? 34 AC7 6 HOH S . ? HOH A 493 . ? 1_555 ? 35 AC7 6 HOH S . ? HOH A 565 . ? 1_555 ? 36 AC8 8 HOH T . ? HOH B 488 . ? 1_555 ? 37 AC8 8 HOH T . ? HOH B 488 . ? 3_555 ? 38 AC8 8 HOH T . ? HOH B 902 . ? 3_555 ? 39 AC8 8 HOH T . ? HOH B 902 . ? 1_555 ? 40 AC8 8 HOH T . ? HOH B 903 . ? 1_555 ? 41 AC8 8 HOH T . ? HOH B 903 . ? 3_555 ? 42 AC8 8 HOH T . ? HOH B 905 . ? 3_555 ? 43 AC8 8 HOH T . ? HOH B 905 . ? 1_555 ? 44 AC9 5 HOH S . ? HOH A 53 . ? 1_555 ? 45 AC9 5 GLU A 196 ? GLU A 276 . ? 1_555 ? 46 AC9 5 GLU A 197 ? GLU A 277 . ? 1_555 ? 47 AC9 5 ARG A 212 ? ARG A 292 . ? 1_555 ? 48 AC9 5 HOH S . ? HOH A 888 . ? 1_555 ? 49 BC1 3 VAL A 13 ? VAL A 94 . ? 1_555 ? 50 BC1 3 TRP A 277 ? TRP A 361 . ? 1_555 ? 51 BC1 3 HOH S . ? HOH A 798 . ? 1_555 ? 52 BC2 2 ASN A 192 ? ASN A 272 . ? 1_555 ? 53 BC2 2 HOH S . ? HOH A 875 . ? 1_555 ? 54 BC3 2 ASN B 65 ? ASN B 146 . ? 1_555 ? 55 BC3 2 HOH T . ? HOH B 872 . ? 1_555 ? 56 BC4 2 ASN B 7 ? ASN B 88 . ? 1_555 ? 57 BC4 2 HOH T . ? HOH B 565 . ? 1_555 ? 58 BC5 6 HOH T . ? HOH B 3 . ? 1_555 ? 59 BC5 6 ASP B 213 ? ASP B 293 . ? 1_555 ? 60 BC5 6 GLY B 217 ? GLY B 297 . ? 1_555 ? 61 BC5 6 ASP B 243 ? ASP B 324 . ? 1_555 ? 62 BC5 6 GLY B 261 ? GLY B 345 . ? 1_555 ? 63 BC5 6 ASN B 263 ? ASN B 347 . ? 1_555 ? 64 BC6 6 HOH T . ? HOH B 56 . ? 1_555 ? 65 BC6 6 ASP B 295 ? ASP B 379 . ? 1_555 ? 66 BC6 6 ASN B 297 ? ASN B 381 . ? 1_555 ? 67 BC6 6 ASP B 303 ? ASP B 387 . ? 1_555 ? 68 BC6 6 ASN B 305 ? ASN B 389 . ? 1_555 ? 69 BC6 6 HOH T . ? HOH B 575 . ? 1_555 ? 70 BC7 2 VAL B 13 ? VAL B 94 . ? 1_555 ? 71 BC7 2 TRP B 277 ? TRP B 361 . ? 1_555 ? # _database_PDB_matrix.entry_id 3NSS _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3NSS _atom_sites.fract_transf_matrix[1][1] 0.008436 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.007254 _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] 0.008438 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA 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 . SER A 1 1 ? 12.209 46.355 27.734 1.00 47.70 ? 82 SER A N 1 ATOM 2 C CA . SER A 1 1 ? 13.284 45.427 27.397 1.00 32.82 ? 82 SER A CA 1 ATOM 3 C C . SER A 1 1 ? 14.591 46.166 27.122 1.00 28.96 ? 82 SER A C 1 ATOM 4 O O . SER A 1 1 ? 14.648 47.044 26.263 1.00 31.78 ? 82 SER A O 1 ATOM 5 C CB . SER A 1 1 ? 12.894 44.571 26.189 1.00 29.27 ? 82 SER A CB 1 ATOM 6 O OG . SER A 1 1 ? 11.798 43.728 26.495 1.00 33.45 ? 82 SER A OG 1 ATOM 7 N N . VAL A 1 2 ? 15.636 45.803 27.859 1.00 20.49 ? 83 VAL A N 1 ATOM 8 C CA . VAL A 1 2 ? 16.946 46.422 27.707 1.00 17.44 ? 83 VAL A CA 1 ATOM 9 C C . VAL A 1 2 ? 18.021 45.345 27.596 1.00 17.82 ? 83 VAL A C 1 ATOM 10 O O . VAL A 1 2 ? 17.975 44.338 28.299 1.00 14.45 ? 83 VAL A O 1 ATOM 11 C CB . VAL A 1 2 ? 17.274 47.335 28.905 1.00 19.58 ? 83 VAL A CB 1 ATOM 12 C CG1 . VAL A 1 2 ? 18.621 48.008 28.708 1.00 20.21 ? 83 VAL A CG1 1 ATOM 13 C CG2 . VAL A 1 2 ? 16.177 48.373 29.099 1.00 31.25 ? 83 VAL A CG2 1 ATOM 14 N N . LYS A 1 3 ? 18.990 45.553 26.713 1.00 15.59 ? 84 LYS A N 1 ATOM 15 C CA . LYS A 1 3 ? 20.048 44.569 26.527 1.00 15.47 ? 84 LYS A CA 1 ATOM 16 C C . LYS A 1 3 ? 20.928 44.457 27.769 1.00 16.58 ? 84 LYS A C 1 ATOM 17 O O . LYS A 1 3 ? 21.112 45.426 28.506 1.00 14.85 ? 84 LYS A O 1 ATOM 18 C CB . LYS A 1 3 ? 20.887 44.911 25.297 1.00 19.66 ? 84 LYS A CB 1 ATOM 19 C CG . LYS A 1 3 ? 21.298 46.367 25.235 1.00 26.40 ? 84 LYS A CG 1 ATOM 20 C CD . LYS A 1 3 ? 21.805 46.750 23.854 1.00 32.71 ? 84 LYS A CD 1 ATOM 21 C CE . LYS A 1 3 ? 21.742 48.257 23.657 1.00 42.25 ? 84 LYS A CE 1 ATOM 22 N NZ . LYS A 1 3 ? 22.366 48.685 22.376 1.00 45.92 ? 84 LYS A NZ 1 ATOM 23 N N . LEU A 1 4 ? 21.460 43.262 27.996 1.00 10.83 ? 85 LEU A N 1 ATOM 24 C CA . LEU A 1 4 ? 22.331 43.009 29.135 1.00 12.46 ? 85 LEU A CA 1 ATOM 25 C C . LEU A 1 4 ? 23.648 43.765 28.987 1.00 13.38 ? 85 LEU A C 1 ATOM 26 O O . LEU A 1 4 ? 24.243 43.789 27.909 1.00 14.02 ? 85 LEU A O 1 ATOM 27 C CB . LEU A 1 4 ? 22.595 41.508 29.267 1.00 7.89 ? 85 LEU A CB 1 ATOM 28 C CG . LEU A 1 4 ? 21.353 40.621 29.369 1.00 12.42 ? 85 LEU A CG 1 ATOM 29 C CD1 . LEU A 1 4 ? 21.746 39.148 29.357 1.00 10.46 ? 85 LEU A CD1 1 ATOM 30 C CD2 . LEU A 1 4 ? 20.544 40.960 30.617 1.00 11.05 ? 85 LEU A CD2 1 ATOM 31 N N . ALA A 1 5 ? 24.097 44.387 30.072 1.00 10.74 ? 86 ALA A N 1 ATOM 32 C CA . ALA A 1 5 ? 25.340 45.146 30.052 1.00 10.65 ? 86 ALA A CA 1 ATOM 33 C C . ALA A 1 5 ? 26.550 44.225 29.934 1.00 11.64 ? 86 ALA A C 1 ATOM 34 O O . ALA A 1 5 ? 27.358 44.359 29.014 1.00 14.32 ? 86 ALA A O 1 ATOM 35 C CB . ALA A 1 5 ? 25.451 46.014 31.298 1.00 12.97 ? 86 ALA A CB 1 ATOM 36 N N . GLY A 1 6 ? 26.666 43.291 30.873 1.00 7.90 ? 87 GLY A N 1 ATOM 37 C CA . GLY A 1 6 ? 27.767 42.348 30.888 1.00 10.57 ? 87 GLY A CA 1 ATOM 38 C C . GLY A 1 6 ? 29.096 42.988 31.244 1.00 12.11 ? 87 GLY A C 1 ATOM 39 O O . GLY A 1 6 ? 30.155 42.438 30.939 1.00 8.57 ? 87 GLY A O 1 ATOM 40 N N . ASN A 1 7 ? 29.044 44.145 31.899 1.00 9.02 ? 88 ASN A N 1 ATOM 41 C CA . ASN A 1 7 ? 30.258 44.903 32.197 1.00 9.32 ? 88 ASN A CA 1 ATOM 42 C C . ASN A 1 7 ? 30.761 44.790 33.639 1.00 13.79 ? 88 ASN A C 1 ATOM 43 O O . ASN A 1 7 ? 31.819 45.326 33.976 1.00 13.24 ? 88 ASN A O 1 ATOM 44 C CB . ASN A 1 7 ? 30.099 46.373 31.790 1.00 13.12 ? 88 ASN A CB 1 ATOM 45 C CG . ASN A 1 7 ? 29.007 47.088 32.565 1.00 19.87 ? 88 ASN A CG 1 ATOM 46 O OD1 . ASN A 1 7 ? 28.134 46.461 33.168 1.00 15.03 ? 88 ASN A OD1 1 ATOM 47 N ND2 . ASN A 1 7 ? 29.051 48.419 32.545 1.00 23.98 ? 88 ASN A ND2 1 ATOM 48 N N . SER A 1 8 ? 30.010 44.090 34.484 1.00 13.59 ? 89 SER A N 1 ATOM 49 C CA . SER A 1 8 ? 30.425 43.887 35.869 1.00 10.82 ? 89 SER A CA 1 ATOM 50 C C . SER A 1 8 ? 31.281 42.630 36.007 1.00 12.94 ? 89 SER A C 1 ATOM 51 O O . SER A 1 8 ? 31.376 41.828 35.078 1.00 10.44 ? 89 SER A O 1 ATOM 52 C CB . SER A 1 8 ? 29.208 43.817 36.799 1.00 10.74 ? 89 SER A CB 1 ATOM 53 O OG . SER A 1 8 ? 28.436 42.655 36.548 1.00 12.78 ? 89 SER A OG 1 ATOM 54 N N . SER A 1 9 ? 31.907 42.467 37.168 1.00 8.97 ? 90 SER A N 1 ATOM 55 C CA . SER A 1 9 ? 32.773 41.321 37.416 1.00 9.56 ? 90 SER A CA 1 ATOM 56 C C . SER A 1 9 ? 31.974 40.114 37.891 1.00 13.58 ? 90 SER A C 1 ATOM 57 O O . SER A 1 9 ? 30.827 40.249 38.318 1.00 11.86 ? 90 SER A O 1 ATOM 58 C CB . SER A 1 9 ? 33.833 41.674 38.462 1.00 13.67 ? 90 SER A CB 1 ATOM 59 O OG . SER A 1 9 ? 34.596 42.795 38.051 1.00 27.80 ? 90 SER A OG 1 ATOM 60 N N . LEU A 1 10 ? 32.584 38.935 37.809 1.00 14.25 ? 91 LEU A N 1 ATOM 61 C CA . LEU A 1 10 ? 31.999 37.734 38.392 1.00 19.06 ? 91 LEU A CA 1 ATOM 62 C C . LEU A 1 10 ? 31.897 37.903 39.899 1.00 16.31 ? 91 LEU A C 1 ATOM 63 O O . LEU A 1 10 ? 32.798 38.458 40.530 1.00 19.23 ? 91 LEU A O 1 ATOM 64 C CB . LEU A 1 10 ? 32.861 36.507 38.091 1.00 15.74 ? 91 LEU A CB 1 ATOM 65 C CG . LEU A 1 10 ? 32.588 35.659 36.852 1.00 18.84 ? 91 LEU A CG 1 ATOM 66 C CD1 . LEU A 1 10 ? 33.488 34.432 36.871 1.00 14.78 ? 91 LEU A CD1 1 ATOM 67 C CD2 . LEU A 1 10 ? 31.127 35.246 36.781 1.00 13.68 ? 91 LEU A CD2 1 ATOM 68 N N . CYS A 1 11 ? 30.802 37.424 40.477 1.00 12.72 ? 92 CYS A N 1 ATOM 69 C CA . CYS A 1 11 ? 30.649 37.437 41.926 1.00 17.91 ? 92 CYS A CA 1 ATOM 70 C C . CYS A 1 11 ? 31.598 36.420 42.544 1.00 18.35 ? 92 CYS A C 1 ATOM 71 O O . CYS A 1 11 ? 31.530 35.233 42.228 1.00 16.01 ? 92 CYS A O 1 ATOM 72 C CB . CYS A 1 11 ? 29.212 37.092 42.326 1.00 15.97 ? 92 CYS A CB 1 ATOM 73 S SG . CYS A 1 11 ? 27.927 38.165 41.641 1.00 24.22 ? 92 CYS A SG 1 ATOM 74 N N . PRO A 1 12 ? 32.502 36.879 43.419 1.00 24.28 ? 93 PRO A N 1 ATOM 75 C CA . PRO A 1 12 ? 33.300 35.905 44.167 1.00 23.26 ? 93 PRO A CA 1 ATOM 76 C C . PRO A 1 12 ? 32.369 35.058 45.026 1.00 21.18 ? 93 PRO A C 1 ATOM 77 O O . PRO A 1 12 ? 31.425 35.597 45.601 1.00 21.77 ? 93 PRO A O 1 ATOM 78 C CB . PRO A 1 12 ? 34.189 36.786 45.050 1.00 31.06 ? 93 PRO A CB 1 ATOM 79 C CG . PRO A 1 12 ? 34.250 38.101 44.339 1.00 36.09 ? 93 PRO A CG 1 ATOM 80 C CD . PRO A 1 12 ? 32.903 38.267 43.701 1.00 30.71 ? 93 PRO A CD 1 ATOM 81 N N . VAL A 1 13 ? 32.618 33.755 45.098 1.00 15.10 ? 94 VAL A N 1 ATOM 82 C CA . VAL A 1 13 ? 31.747 32.861 45.853 1.00 12.38 ? 94 VAL A CA 1 ATOM 83 C C . VAL A 1 13 ? 32.547 31.899 46.723 1.00 11.68 ? 94 VAL A C 1 ATOM 84 O O . VAL A 1 13 ? 33.674 31.535 46.390 1.00 11.84 ? 94 VAL A O 1 ATOM 85 C CB . VAL A 1 13 ? 30.822 32.057 44.922 1.00 10.93 ? 94 VAL A CB 1 ATOM 86 C CG1 . VAL A 1 13 ? 29.966 32.997 44.085 1.00 16.68 ? 94 VAL A CG1 1 ATOM 87 C CG2 . VAL A 1 13 ? 31.634 31.136 44.031 1.00 13.29 ? 94 VAL A CG2 1 ATOM 88 N N . SER A 1 14 ? 31.959 31.489 47.842 1.00 12.48 ? 95 SER A N 1 ATOM 89 C CA . SER A 1 14 ? 32.640 30.588 48.764 1.00 10.30 ? 95 SER A CA 1 ATOM 90 C C . SER A 1 14 ? 32.109 29.162 48.659 1.00 11.71 ? 95 SER A C 1 ATOM 91 O O . SER A 1 14 ? 32.743 28.217 49.127 1.00 10.22 ? 95 SER A O 1 ATOM 92 C CB . SER A 1 14 ? 32.516 31.099 50.204 1.00 13.13 ? 95 SER A CB 1 ATOM 93 O OG . SER A 1 14 ? 31.159 31.175 50.604 1.00 15.00 ? 95 SER A OG 1 ATOM 94 N N . GLY A 1 15 ? 30.946 29.010 48.033 1.00 11.12 ? 96 GLY A N 1 ATOM 95 C CA . GLY A 1 15 ? 30.317 27.710 47.918 1.00 7.54 ? 96 GLY A CA 1 ATOM 96 C C . GLY A 1 15 ? 29.133 27.705 46.972 1.00 7.79 ? 96 GLY A C 1 ATOM 97 O O . GLY A 1 15 ? 28.757 28.739 46.419 1.00 8.22 ? 96 GLY A O 1 ATOM 98 N N . TRP A 1 16 ? 28.533 26.533 46.797 1.00 8.59 ? 97 TRP A N 1 ATOM 99 C CA . TRP A 1 16 ? 27.476 26.360 45.812 1.00 7.88 ? 97 TRP A CA 1 ATOM 100 C C . TRP A 1 16 ? 26.199 25.809 46.437 1.00 7.75 ? 97 TRP A C 1 ATOM 101 O O . TRP A 1 16 ? 26.215 24.773 47.104 1.00 7.11 ? 97 TRP A O 1 ATOM 102 C CB . TRP A 1 16 ? 27.972 25.455 44.687 1.00 6.65 ? 97 TRP A CB 1 ATOM 103 C CG . TRP A 1 16 ? 29.280 25.931 44.140 1.00 6.83 ? 97 TRP A CG 1 ATOM 104 C CD1 . TRP A 1 16 ? 30.526 25.602 44.590 1.00 6.75 ? 97 TRP A CD1 1 ATOM 105 C CD2 . TRP A 1 16 ? 29.473 26.855 43.064 1.00 8.08 ? 97 TRP A CD2 1 ATOM 106 N NE1 . TRP A 1 16 ? 31.483 26.254 43.851 1.00 10.05 ? 97 TRP A NE1 1 ATOM 107 C CE2 . TRP A 1 16 ? 30.862 27.029 42.907 1.00 8.22 ? 97 TRP A CE2 1 ATOM 108 C CE3 . TRP A 1 16 ? 28.605 27.547 42.213 1.00 6.67 ? 97 TRP A CE3 1 ATOM 109 C CZ2 . TRP A 1 16 ? 31.402 27.868 41.935 1.00 5.72 ? 97 TRP A CZ2 1 ATOM 110 C CZ3 . TRP A 1 16 ? 29.145 28.375 41.248 1.00 7.41 ? 97 TRP A CZ3 1 ATOM 111 C CH2 . TRP A 1 16 ? 30.529 28.530 41.117 1.00 6.19 ? 97 TRP A CH2 1 ATOM 112 N N . ALA A 1 17 ? 25.097 26.521 46.216 1.00 7.00 ? 98 ALA A N 1 ATOM 113 C CA . ALA A 1 17 ? 23.796 26.148 46.763 1.00 6.03 ? 98 ALA A CA 1 ATOM 114 C C . ALA A 1 17 ? 22.957 25.502 45.671 1.00 6.42 ? 98 ALA A C 1 ATOM 115 O O . ALA A 1 17 ? 22.925 25.991 44.544 1.00 7.15 ? 98 ALA A O 1 ATOM 116 C CB . ALA A 1 17 ? 23.088 27.375 47.308 1.00 7.73 ? 98 ALA A CB 1 ATOM 117 N N . ILE A 1 18 ? 22.280 24.407 45.998 1.00 7.13 ? 99 ILE A N 1 ATOM 118 C CA . ILE A 1 18 ? 21.511 23.683 44.991 1.00 6.18 ? 99 ILE A CA 1 ATOM 119 C C . ILE A 1 18 ? 20.336 24.514 44.483 1.00 7.67 ? 99 ILE A C 1 ATOM 120 O O . ILE A 1 18 ? 19.597 25.121 45.263 1.00 6.16 ? 99 ILE A O 1 ATOM 121 C CB . ILE A 1 18 ? 21.045 22.291 45.480 1.00 6.98 ? 99 ILE A CB 1 ATOM 122 C CG1 . ILE A 1 18 ? 20.567 21.452 44.289 1.00 7.71 ? 99 ILE A CG1 1 ATOM 123 C CG2 . ILE A 1 18 ? 19.970 22.418 46.553 1.00 8.44 ? 99 ILE A CG2 1 ATOM 124 C CD1 . ILE A 1 18 ? 20.443 19.979 44.580 1.00 9.10 ? 99 ILE A CD1 1 ATOM 125 N N . TYR A 1 19 ? 20.181 24.534 43.164 1.00 5.38 ? 100 TYR A N 1 ATOM 126 C CA . TYR A 1 19 ? 19.228 25.415 42.504 1.00 4.88 ? 100 TYR A CA 1 ATOM 127 C C . TYR A 1 19 ? 18.070 24.630 41.895 1.00 7.31 ? 100 TYR A C 1 ATOM 128 O O . TYR A 1 19 ? 16.913 25.007 42.061 1.00 6.57 ? 100 TYR A O 1 ATOM 129 C CB . TYR A 1 19 ? 19.948 26.234 41.428 1.00 6.89 ? 100 TYR A CB 1 ATOM 130 C CG . TYR A 1 19 ? 19.128 27.348 40.821 1.00 9.61 ? 100 TYR A CG 1 ATOM 131 C CD1 . TYR A 1 19 ? 18.479 28.277 41.624 1.00 12.18 ? 100 TYR A CD1 1 ATOM 132 C CD2 . TYR A 1 19 ? 19.025 27.489 39.442 1.00 14.21 ? 100 TYR A CD2 1 ATOM 133 C CE1 . TYR A 1 19 ? 17.734 29.302 41.073 1.00 13.69 ? 100 TYR A CE1 1 ATOM 134 C CE2 . TYR A 1 19 ? 18.284 28.512 38.882 1.00 13.39 ? 100 TYR A CE2 1 ATOM 135 C CZ . TYR A 1 19 ? 17.643 29.416 39.703 1.00 16.59 ? 100 TYR A CZ 1 ATOM 136 O OH . TYR A 1 19 ? 16.907 30.439 39.151 1.00 22.50 ? 100 TYR A OH 1 ATOM 137 N N . SER A 1 20 ? 18.376 23.539 41.196 1.00 5.46 ? 101 SER A N 1 ATOM 138 C CA . SER A 1 20 ? 17.323 22.721 40.593 1.00 7.00 ? 101 SER A CA 1 ATOM 139 C C . SER A 1 20 ? 17.682 21.238 40.469 1.00 6.99 ? 101 SER A C 1 ATOM 140 O O . SER A 1 20 ? 18.855 20.864 40.483 1.00 7.55 ? 101 SER A O 1 ATOM 141 C CB . SER A 1 20 ? 16.932 23.272 39.216 1.00 8.54 ? 101 SER A CB 1 ATOM 142 O OG . SER A 1 20 ? 17.949 23.032 38.257 1.00 11.40 ? 101 SER A OG 1 ATOM 143 N N . LYS A 1 21 ? 16.650 20.407 40.360 1.00 4.10 ? 102 LYS A N 1 ATOM 144 C CA . LYS A 1 21 ? 16.794 18.987 40.045 1.00 10.17 ? 102 LYS A CA 1 ATOM 145 C C . LYS A 1 21 ? 15.496 18.521 39.390 1.00 10.07 ? 102 LYS A C 1 ATOM 146 O O . LYS A 1 21 ? 14.417 18.737 39.937 1.00 8.95 ? 102 LYS A O 1 ATOM 147 C CB . LYS A 1 21 ? 17.065 18.167 41.307 1.00 6.81 ? 102 LYS A CB 1 ATOM 148 C CG . LYS A 1 21 ? 17.364 16.696 41.030 1.00 6.87 ? 102 LYS A CG 1 ATOM 149 C CD . LYS A 1 21 ? 17.618 15.925 42.320 1.00 9.65 ? 102 LYS A CD 1 ATOM 150 C CE . LYS A 1 21 ? 18.390 14.638 42.058 1.00 9.02 ? 102 LYS A CE 1 ATOM 151 N NZ . LYS A 1 21 ? 17.707 13.751 41.077 1.00 12.03 ? 102 LYS A NZ 1 ATOM 152 N N . ASP A 1 22 ? 15.588 17.886 38.225 1.00 8.81 ? 103 ASP A N 1 ATOM 153 C CA . ASP A 1 22 ? 14.376 17.550 37.475 1.00 11.36 ? 103 ASP A CA 1 ATOM 154 C C . ASP A 1 22 ? 13.878 16.107 37.629 1.00 9.48 ? 103 ASP A C 1 ATOM 155 O O . ASP A 1 22 ? 12.717 15.823 37.336 1.00 10.28 ? 103 ASP A O 1 ATOM 156 C CB . ASP A 1 22 ? 14.517 17.928 35.993 1.00 10.03 ? 103 ASP A CB 1 ATOM 157 C CG . ASP A 1 22 ? 15.724 17.286 35.333 1.00 13.56 ? 103 ASP A CG 1 ATOM 158 O OD1 . ASP A 1 22 ? 16.226 16.267 35.852 1.00 12.35 ? 103 ASP A OD1 1 ATOM 159 O OD2 . ASP A 1 22 ? 16.167 17.801 34.283 1.00 20.44 ? 103 ASP A OD2 1 ATOM 160 N N . ASN A 1 23 ? 14.741 15.205 38.089 1.00 8.10 ? 104 ASN A N 1 ATOM 161 C CA . ASN A 1 23 ? 14.351 13.805 38.269 1.00 9.15 ? 104 ASN A CA 1 ATOM 162 C C . ASN A 1 23 ? 13.773 13.200 36.990 1.00 7.43 ? 104 ASN A C 1 ATOM 163 O O . ASN A 1 23 ? 12.880 12.355 37.039 1.00 6.53 ? 104 ASN A O 1 ATOM 164 C CB . ASN A 1 23 ? 13.329 13.672 39.405 1.00 7.81 ? 104 ASN A CB 1 ATOM 165 C CG . ASN A 1 23 ? 13.936 13.926 40.772 1.00 9.03 ? 104 ASN A CG 1 ATOM 166 O OD1 . ASN A 1 23 ? 14.971 13.362 41.117 1.00 6.99 ? 104 ASN A OD1 1 ATOM 167 N ND2 . ASN A 1 23 ? 13.283 14.771 41.564 1.00 10.75 ? 104 ASN A ND2 1 ATOM 168 N N . SER A 1 24 ? 14.297 13.634 35.848 1.00 6.42 ? 105 SER A N 1 ATOM 169 C CA . SER A 1 24 ? 13.726 13.288 34.548 1.00 9.22 ? 105 SER A CA 1 ATOM 170 C C . SER A 1 24 ? 13.601 11.788 34.283 1.00 8.48 ? 105 SER A C 1 ATOM 171 O O . SER A 1 24 ? 12.565 11.321 33.806 1.00 10.95 ? 105 SER A O 1 ATOM 172 C CB . SER A 1 24 ? 14.534 13.946 33.427 1.00 9.84 ? 105 SER A CB 1 ATOM 173 O OG . SER A 1 24 ? 14.470 15.358 33.528 1.00 16.32 ? 105 SER A OG 1 ATOM 174 N N . VAL A 1 25 ? 14.654 11.036 34.579 1.00 6.66 ? 106 VAL A N 1 ATOM 175 C CA . VAL A 1 25 ? 14.664 9.609 34.273 1.00 7.27 ? 106 VAL A CA 1 ATOM 176 C C . VAL A 1 25 ? 13.732 8.819 35.194 1.00 6.01 ? 106 VAL A C 1 ATOM 177 O O . VAL A 1 25 ? 13.024 7.919 34.745 1.00 8.94 ? 106 VAL A O 1 ATOM 178 C CB . VAL A 1 25 ? 16.091 9.029 34.309 1.00 7.77 ? 106 VAL A CB 1 ATOM 179 C CG1 . VAL A 1 25 ? 16.080 7.572 33.881 1.00 8.97 ? 106 VAL A CG1 1 ATOM 180 C CG2 . VAL A 1 25 ? 17.009 9.836 33.402 1.00 11.17 ? 106 VAL A CG2 1 ATOM 181 N N . ARG A 1 26 ? 13.727 9.162 36.479 1.00 6.57 ? 107 ARG A N 1 ATOM 182 C CA . ARG A 1 26 ? 12.810 8.533 37.425 1.00 5.63 ? 107 ARG A CA 1 ATOM 183 C C . ARG A 1 26 ? 11.365 8.713 36.972 1.00 7.80 ? 107 ARG A C 1 ATOM 184 O O . ARG A 1 26 ? 10.585 7.762 36.936 1.00 8.41 ? 107 ARG A O 1 ATOM 185 C CB . ARG A 1 26 ? 12.995 9.122 38.826 1.00 4.72 ? 107 ARG A CB 1 ATOM 186 C CG . ARG A 1 26 ? 14.243 8.634 39.543 1.00 7.83 ? 107 ARG A CG 1 ATOM 187 C CD . ARG A 1 26 ? 14.556 9.483 40.764 1.00 6.03 ? 107 ARG A CD 1 ATOM 188 N NE . ARG A 1 26 ? 13.485 9.466 41.759 1.00 6.60 ? 107 ARG A NE 1 ATOM 189 C CZ . ARG A 1 26 ? 13.389 8.570 42.737 1.00 10.56 ? 107 ARG A CZ 1 ATOM 190 N NH1 . ARG A 1 26 ? 14.294 7.607 42.849 1.00 8.92 ? 107 ARG A NH1 1 ATOM 191 N NH2 . ARG A 1 26 ? 12.386 8.636 43.603 1.00 7.10 ? 107 ARG A NH2 1 ATOM 192 N N . ILE A 1 27 ? 11.016 9.943 36.619 1.00 4.73 ? 108 ILE A N 1 ATOM 193 C CA . ILE A 1 27 ? 9.657 10.265 36.209 1.00 5.77 ? 108 ILE A CA 1 ATOM 194 C C . ILE A 1 27 ? 9.321 9.644 34.854 1.00 7.19 ? 108 ILE A C 1 ATOM 195 O O . ILE A 1 27 ? 8.198 9.191 34.632 1.00 8.28 ? 108 ILE A O 1 ATOM 196 C CB . ILE A 1 27 ? 9.444 11.791 36.187 1.00 5.83 ? 108 ILE A CB 1 ATOM 197 C CG1 . ILE A 1 27 ? 9.537 12.336 37.617 1.00 8.07 ? 108 ILE A CG1 1 ATOM 198 C CG2 . ILE A 1 27 ? 8.108 12.145 35.544 1.00 5.89 ? 108 ILE A CG2 1 ATOM 199 C CD1 . ILE A 1 27 ? 9.581 13.845 37.711 1.00 14.59 ? 108 ILE A CD1 1 ATOM 200 N N . GLY A 1 28 ? 10.308 9.604 33.964 1.00 6.35 ? 109 GLY A N 1 ATOM 201 C CA . GLY A 1 28 ? 10.127 9.062 32.628 1.00 10.03 ? 109 GLY A CA 1 ATOM 202 C C . GLY A 1 28 ? 9.835 7.574 32.595 1.00 10.83 ? 109 GLY A C 1 ATOM 203 O O . GLY A 1 28 ? 9.455 7.032 31.556 1.00 11.99 ? 109 GLY A O 1 ATOM 204 N N . SER A 1 29 ? 10.020 6.908 33.730 1.00 10.62 ? 110 SER A N 1 ATOM 205 C CA . SER A 1 29 ? 9.700 5.492 33.845 1.00 10.90 ? 110 SER A CA 1 ATOM 206 C C . SER A 1 29 ? 8.224 5.256 33.525 1.00 14.00 ? 110 SER A C 1 ATOM 207 O O . SER A 1 29 ? 7.865 4.242 32.926 1.00 17.25 ? 110 SER A O 1 ATOM 208 C CB . SER A 1 29 ? 10.033 4.981 35.249 1.00 14.85 ? 110 SER A CB 1 ATOM 209 O OG . SER A 1 29 ? 9.795 3.588 35.363 1.00 18.70 ? 110 SER A OG 1 ATOM 210 N N . LYS A 1 30 ? 7.374 6.198 33.924 1.00 11.27 ? 111 LYS A N 1 ATOM 211 C CA . LYS A 1 30 ? 5.945 6.110 33.632 1.00 12.57 ? 111 LYS A CA 1 ATOM 212 C C . LYS A 1 30 ? 5.450 7.278 32.785 1.00 14.53 ? 111 LYS A C 1 ATOM 213 O O . LYS A 1 30 ? 4.670 7.091 31.851 1.00 14.54 ? 111 LYS A O 1 ATOM 214 C CB . LYS A 1 30 ? 5.118 6.033 34.919 1.00 12.52 ? 111 LYS A CB 1 ATOM 215 C CG . LYS A 1 30 ? 3.620 6.126 34.652 1.00 12.49 ? 111 LYS A CG 1 ATOM 216 C CD . LYS A 1 30 ? 2.778 6.081 35.914 1.00 16.84 ? 111 LYS A CD 1 ATOM 217 C CE . LYS A 1 30 ? 1.301 6.260 35.568 1.00 15.59 ? 111 LYS A CE 1 ATOM 218 N NZ . LYS A 1 30 ? 0.417 6.262 36.764 1.00 24.14 ? 111 LYS A NZ 1 ATOM 219 N N . GLY A 1 31 ? 5.899 8.483 33.122 1.00 7.29 ? 112 GLY A N 1 ATOM 220 C CA . GLY A 1 31 ? 5.457 9.684 32.435 1.00 9.78 ? 112 GLY A CA 1 ATOM 221 C C . GLY A 1 31 ? 6.001 9.801 31.025 1.00 10.21 ? 112 GLY A C 1 ATOM 222 O O . GLY A 1 31 ? 6.870 9.033 30.618 1.00 12.85 ? 112 GLY A O 1 ATOM 223 N N . ASP A 1 32 ? 5.483 10.769 30.276 1.00 9.83 ? 113 ASP A N 1 ATOM 224 C CA . ASP A 1 32 ? 5.930 11.001 28.910 1.00 9.86 ? 113 ASP A CA 1 ATOM 225 C C . ASP A 1 32 ? 7.070 12.009 28.896 1.00 8.40 ? 113 ASP A C 1 ATOM 226 O O . ASP A 1 32 ? 6.854 13.222 28.846 1.00 8.77 ? 113 ASP A O 1 ATOM 227 C CB . ASP A 1 32 ? 4.766 11.474 28.040 1.00 11.11 ? 113 ASP A CB 1 ATOM 228 C CG . ASP A 1 32 ? 3.707 10.402 27.862 1.00 10.47 ? 113 ASP A CG 1 ATOM 229 O OD1 . ASP A 1 32 ? 4.036 9.208 28.023 1.00 11.85 ? 113 ASP A OD1 1 ATOM 230 O OD2 . ASP A 1 32 ? 2.549 10.750 27.561 1.00 14.15 ? 113 ASP A OD2 1 ATOM 231 N N . VAL A 1 33 ? 8.289 11.486 28.951 1.00 5.69 ? 114 VAL A N 1 ATOM 232 C CA . VAL A 1 33 ? 9.481 12.304 29.082 1.00 4.55 ? 114 VAL A CA 1 ATOM 233 C C . VAL A 1 33 ? 10.433 12.015 27.929 1.00 4.72 ? 114 VAL A C 1 ATOM 234 O O . VAL A 1 33 ? 10.710 10.855 27.622 1.00 5.42 ? 114 VAL A O 1 ATOM 235 C CB . VAL A 1 33 ? 10.187 12.020 30.424 1.00 5.55 ? 114 VAL A CB 1 ATOM 236 C CG1 . VAL A 1 33 ? 11.479 12.821 30.544 1.00 5.31 ? 114 VAL A CG1 1 ATOM 237 C CG2 . VAL A 1 33 ? 9.248 12.323 31.583 1.00 7.51 ? 114 VAL A CG2 1 ATOM 238 N N . PHE A 1 34 ? 10.917 13.071 27.283 1.00 5.50 ? 115 PHE A N 1 ATOM 239 C CA . PHE A 1 34 ? 11.843 12.928 26.166 1.00 5.77 ? 115 PHE A CA 1 ATOM 240 C C . PHE A 1 34 ? 13.109 12.192 26.577 1.00 7.82 ? 115 PHE A C 1 ATOM 241 O O . PHE A 1 34 ? 13.613 12.369 27.689 1.00 4.88 ? 115 PHE A O 1 ATOM 242 C CB . PHE A 1 34 ? 12.255 14.298 25.619 1.00 7.52 ? 115 PHE A CB 1 ATOM 243 C CG . PHE A 1 34 ? 11.224 14.947 24.737 1.00 7.40 ? 115 PHE A CG 1 ATOM 244 C CD1 . PHE A 1 34 ? 10.832 14.353 23.548 1.00 11.19 ? 115 PHE A CD1 1 ATOM 245 C CD2 . PHE A 1 34 ? 10.678 16.172 25.078 1.00 8.50 ? 115 PHE A CD2 1 ATOM 246 C CE1 . PHE A 1 34 ? 9.892 14.958 22.729 1.00 11.47 ? 115 PHE A CE1 1 ATOM 247 C CE2 . PHE A 1 34 ? 9.738 16.785 24.262 1.00 8.37 ? 115 PHE A CE2 1 ATOM 248 C CZ . PHE A 1 34 ? 9.346 16.178 23.088 1.00 5.88 ? 115 PHE A CZ 1 ATOM 249 N N . VAL A 1 35 ? 13.622 11.367 25.671 1.00 8.66 ? 116 VAL A N 1 ATOM 250 C CA . VAL A 1 35 ? 14.991 10.900 25.780 1.00 7.49 ? 116 VAL A CA 1 ATOM 251 C C . VAL A 1 35 ? 15.853 12.086 25.380 1.00 9.35 ? 116 VAL A C 1 ATOM 252 O O . VAL A 1 35 ? 15.693 12.633 24.290 1.00 9.09 ? 116 VAL A O 1 ATOM 253 C CB . VAL A 1 35 ? 15.277 9.730 24.826 1.00 9.55 ? 116 VAL A CB 1 ATOM 254 C CG1 . VAL A 1 35 ? 16.745 9.336 24.900 1.00 10.32 ? 116 VAL A CG1 1 ATOM 255 C CG2 . VAL A 1 35 ? 14.382 8.545 25.155 1.00 10.17 ? 116 VAL A CG2 1 ATOM 256 N N . ILE A 1 36 ? 16.746 12.506 26.267 1.00 6.07 ? 117 ILE A N 1 ATOM 257 C CA . ILE A 1 36 ? 17.564 13.677 25.990 1.00 9.24 ? 117 ILE A CA 1 ATOM 258 C C . ILE A 1 36 ? 19.018 13.469 26.365 1.00 11.64 ? 117 ILE A C 1 ATOM 259 O O . ILE A 1 36 ? 19.364 12.551 27.106 1.00 14.18 ? 117 ILE A O 1 ATOM 260 C CB . ILE A 1 36 ? 17.076 14.908 26.772 1.00 7.44 ? 117 ILE A CB 1 ATOM 261 C CG1 . ILE A 1 36 ? 17.426 14.758 28.255 1.00 11.35 ? 117 ILE A CG1 1 ATOM 262 C CG2 . ILE A 1 36 ? 15.579 15.115 26.580 1.00 10.09 ? 117 ILE A CG2 1 ATOM 263 C CD1 . ILE A 1 36 ? 17.357 16.051 29.032 1.00 20.30 ? 117 ILE A CD1 1 ATOM 264 N N . ARG A 1 37 ? 19.863 14.341 25.837 1.00 7.77 ? 118 ARG A N 1 ATOM 265 C CA . ARG A 1 37 ? 21.227 14.479 26.313 1.00 9.81 ? 118 ARG A CA 1 ATOM 266 C C . ARG A 1 37 ? 21.665 15.913 26.080 1.00 12.18 ? 118 ARG A C 1 ATOM 267 O O . ARG A 1 37 ? 20.938 16.700 25.470 1.00 12.06 ? 118 ARG A O 1 ATOM 268 C CB . ARG A 1 37 ? 22.168 13.495 25.617 1.00 13.05 ? 118 ARG A CB 1 ATOM 269 C CG . ARG A 1 37 ? 22.324 12.170 26.352 1.00 11.77 ? 118 ARG A CG 1 ATOM 270 C CD . ARG A 1 37 ? 23.763 11.693 26.311 1.00 16.14 ? 118 ARG A CD 1 ATOM 271 N NE . ARG A 1 37 ? 24.672 12.670 26.902 1.00 13.02 ? 118 ARG A NE 1 ATOM 272 C CZ . ARG A 1 37 ? 25.964 12.759 26.609 1.00 12.56 ? 118 ARG A CZ 1 ATOM 273 N NH1 . ARG A 1 37 ? 26.504 11.933 25.723 1.00 16.72 ? 118 ARG A NH1 1 ATOM 274 N NH2 . ARG A 1 37 ? 26.716 13.681 27.194 1.00 8.87 ? 118 ARG A NH2 1 ATOM 275 N N . GLU A 1 38 ? 22.846 16.256 26.575 1.00 14.90 ? 119 GLU A N 1 ATOM 276 C CA . GLU A 1 38 ? 23.373 17.601 26.407 1.00 16.33 ? 119 GLU A CA 1 ATOM 277 C C . GLU A 1 38 ? 22.386 18.665 26.886 1.00 13.57 ? 119 GLU A C 1 ATOM 278 O O . GLU A 1 38 ? 22.056 19.592 26.145 1.00 15.29 ? 119 GLU A O 1 ATOM 279 C CB . GLU A 1 38 ? 23.748 17.851 24.942 1.00 15.25 ? 119 GLU A CB 1 ATOM 280 C CG . GLU A 1 38 ? 24.906 16.996 24.426 1.00 21.66 ? 119 GLU A CG 1 ATOM 281 C CD . GLU A 1 38 ? 24.465 15.641 23.890 1.00 25.94 ? 119 GLU A CD 1 ATOM 282 O OE1 . GLU A 1 38 ? 25.256 14.679 23.985 1.00 23.70 ? 119 GLU A OE1 1 ATOM 283 O OE2 . GLU A 1 38 ? 23.334 15.535 23.369 1.00 20.46 ? 119 GLU A OE2 1 ATOM 284 N N . PRO A 1 39 ? 21.905 18.538 28.130 1.00 13.21 ? 120 PRO A N 1 ATOM 285 C CA . PRO A 1 39 ? 21.057 19.618 28.628 1.00 14.15 ? 120 PRO A CA 1 ATOM 286 C C . PRO A 1 39 ? 21.944 20.788 29.019 1.00 17.64 ? 120 PRO A C 1 ATOM 287 O O . PRO A 1 39 ? 23.117 20.586 29.330 1.00 19.84 ? 120 PRO A O 1 ATOM 288 C CB . PRO A 1 39 ? 20.426 19.005 29.875 1.00 18.20 ? 120 PRO A CB 1 ATOM 289 C CG . PRO A 1 39 ? 21.472 18.061 30.382 1.00 15.62 ? 120 PRO A CG 1 ATOM 290 C CD . PRO A 1 39 ? 22.198 17.535 29.170 1.00 13.96 ? 120 PRO A CD 1 ATOM 291 N N . PHE A 1 40 ? 21.406 21.998 28.978 1.00 6.00 ? 121 PHE A N 1 ATOM 292 C CA . PHE A 1 40 ? 22.121 23.142 29.520 1.00 6.00 ? 121 PHE A CA 1 ATOM 293 C C . PHE A 1 40 ? 21.138 24.219 29.938 1.00 8.11 ? 121 PHE A C 1 ATOM 294 O O . PHE A 1 40 ? 20.010 24.262 29.452 1.00 10.30 ? 121 PHE A O 1 ATOM 295 C CB . PHE A 1 40 ? 23.176 23.677 28.539 1.00 6.10 ? 121 PHE A CB 1 ATOM 296 C CG . PHE A 1 40 ? 22.611 24.255 27.266 1.00 3.97 ? 121 PHE A CG 1 ATOM 297 C CD1 . PHE A 1 40 ? 22.240 25.588 27.198 1.00 5.73 ? 121 PHE A CD1 1 ATOM 298 C CD2 . PHE A 1 40 ? 22.493 23.476 26.127 1.00 7.87 ? 121 PHE A CD2 1 ATOM 299 C CE1 . PHE A 1 40 ? 21.741 26.128 26.028 1.00 5.04 ? 121 PHE A CE1 1 ATOM 300 C CE2 . PHE A 1 40 ? 21.995 24.012 24.951 1.00 6.27 ? 121 PHE A CE2 1 ATOM 301 C CZ . PHE A 1 40 ? 21.620 25.341 24.904 1.00 3.41 ? 121 PHE A CZ 1 ATOM 302 N N . ILE A 1 41 ? 21.563 25.075 30.857 1.00 4.98 ? 122 ILE A N 1 ATOM 303 C CA . ILE A 1 41 ? 20.695 26.128 31.354 1.00 5.26 ? 122 ILE A CA 1 ATOM 304 C C . ILE A 1 41 ? 21.124 27.485 30.815 1.00 5.84 ? 122 ILE A C 1 ATOM 305 O O . ILE A 1 41 ? 22.309 27.733 30.602 1.00 5.05 ? 122 ILE A O 1 ATOM 306 C CB . ILE A 1 41 ? 20.678 26.148 32.891 1.00 6.11 ? 122 ILE A CB 1 ATOM 307 C CG1 . ILE A 1 41 ? 20.043 24.857 33.415 1.00 6.08 ? 122 ILE A CG1 1 ATOM 308 C CG2 . ILE A 1 41 ? 19.931 27.371 33.413 1.00 4.95 ? 122 ILE A CG2 1 ATOM 309 C CD1 . ILE A 1 41 ? 20.213 24.660 34.898 1.00 11.94 ? 122 ILE A CD1 1 ATOM 310 N N . SER A 1 42 ? 20.145 28.349 30.577 1.00 8.14 ? 123 SER A N 1 ATOM 311 C CA . SER A 1 42 ? 20.407 29.719 30.161 1.00 10.04 ? 123 SER A CA 1 ATOM 312 C C . SER A 1 42 ? 19.275 30.612 30.661 1.00 7.40 ? 123 SER A C 1 ATOM 313 O O . SER A 1 42 ? 18.127 30.177 30.745 1.00 8.28 ? 123 SER A O 1 ATOM 314 C CB . SER A 1 42 ? 20.536 29.803 28.640 1.00 10.46 ? 123 SER A CB 1 ATOM 315 O OG . SER A 1 42 ? 21.124 31.032 28.249 1.00 11.04 ? 123 SER A OG 1 ATOM 316 N N . CYS A 1 43 ? 19.600 31.857 30.992 1.00 7.36 ? 124 CYS A N 1 ATOM 317 C CA . CYS A 1 43 ? 18.635 32.747 31.631 1.00 10.99 ? 124 CYS A CA 1 ATOM 318 C C . CYS A 1 43 ? 18.359 34.012 30.822 1.00 11.96 ? 124 CYS A C 1 ATOM 319 O O . CYS A 1 43 ? 19.204 34.484 30.063 1.00 9.81 ? 124 CYS A O 1 ATOM 320 C CB . CYS A 1 43 ? 19.108 33.126 33.041 1.00 11.36 ? 124 CYS A CB 1 ATOM 321 S SG . CYS A 1 43 ? 19.373 31.730 34.171 1.00 15.19 ? 124 CYS A SG 1 ATOM 322 N N . SER A 1 44 ? 17.156 34.546 30.987 1.00 15.15 ? 125 SER A N 1 ATOM 323 C CA . SER A 1 44 ? 16.809 35.846 30.439 1.00 16.28 ? 125 SER A CA 1 ATOM 324 C C . SER A 1 44 ? 16.749 36.826 31.603 1.00 16.35 ? 125 SER A C 1 ATOM 325 O O . SER A 1 44 ? 17.055 36.458 32.739 1.00 17.17 ? 125 SER A O 1 ATOM 326 C CB . SER A 1 44 ? 15.458 35.778 29.723 1.00 17.47 ? 125 SER A CB 1 ATOM 327 O OG . SER A 1 44 ? 14.403 35.566 30.643 1.00 19.88 ? 125 SER A OG 1 ATOM 328 N N . PRO A 1 45 ? 16.376 38.085 31.334 1.00 16.03 ? 126 PRO A N 1 ATOM 329 C CA . PRO A 1 45 ? 16.186 38.998 32.464 1.00 15.80 ? 126 PRO A CA 1 ATOM 330 C C . PRO A 1 45 ? 14.958 38.629 33.293 1.00 16.25 ? 126 PRO A C 1 ATOM 331 O O . PRO A 1 45 ? 14.723 39.233 34.340 1.00 19.38 ? 126 PRO A O 1 ATOM 332 C CB . PRO A 1 45 ? 15.974 40.356 31.786 1.00 21.51 ? 126 PRO A CB 1 ATOM 333 C CG . PRO A 1 45 ? 16.599 40.213 30.438 1.00 17.53 ? 126 PRO A CG 1 ATOM 334 C CD . PRO A 1 45 ? 16.354 38.792 30.042 1.00 15.40 ? 126 PRO A CD 1 ATOM 335 N N . LEU A 1 46 ? 14.190 37.645 32.835 1.00 21.89 ? 127 LEU A N 1 ATOM 336 C CA . LEU A 1 46 ? 12.944 37.282 33.503 1.00 24.61 ? 127 LEU A CA 1 ATOM 337 C C . LEU A 1 46 ? 12.924 35.859 34.065 1.00 25.31 ? 127 LEU A C 1 ATOM 338 O O . LEU A 1 46 ? 12.350 35.617 35.127 1.00 23.84 ? 127 LEU A O 1 ATOM 339 C CB . LEU A 1 46 ? 11.754 37.487 32.561 1.00 24.08 ? 127 LEU A CB 1 ATOM 340 C CG . LEU A 1 46 ? 11.468 38.935 32.160 1.00 31.12 ? 127 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 46 ? 10.355 39.001 31.125 1.00 33.17 ? 127 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 46 ? 11.121 39.771 33.383 1.00 29.80 ? 127 LEU A CD2 1 ATOM 343 N N . GLU A 1 47 ? 13.539 34.917 33.357 1.00 17.61 ? 128 GLU A N 1 ATOM 344 C CA . GLU A 1 47 ? 13.473 33.516 33.772 1.00 18.58 ? 128 GLU A CA 1 ATOM 345 C C . GLU A 1 47 ? 14.690 32.703 33.347 1.00 16.49 ? 128 GLU A C 1 ATOM 346 O O . GLU A 1 47 ? 15.519 33.162 32.565 1.00 15.36 ? 128 GLU A O 1 ATOM 347 C CB . GLU A 1 47 ? 12.208 32.857 33.217 1.00 21.25 ? 128 GLU A CB 1 ATOM 348 C CG . GLU A 1 47 ? 12.212 32.693 31.705 1.00 24.33 ? 128 GLU A CG 1 ATOM 349 C CD . GLU A 1 47 ? 11.048 31.860 31.204 1.00 33.69 ? 128 GLU A CD 1 ATOM 350 O OE1 . GLU A 1 47 ? 10.229 31.418 32.037 1.00 39.89 ? 128 GLU A OE1 1 ATOM 351 O OE2 . GLU A 1 47 ? 10.954 31.646 29.978 1.00 27.97 ? 128 GLU A OE2 1 ATOM 352 N N . CYS A 1 48 ? 14.784 31.489 33.876 1.00 9.11 ? 129 CYS A N 1 ATOM 353 C CA . CYS A 1 48 ? 15.838 30.560 33.495 1.00 11.10 ? 129 CYS A CA 1 ATOM 354 C C . CYS A 1 48 ? 15.204 29.323 32.880 1.00 8.61 ? 129 CYS A C 1 ATOM 355 O O . CYS A 1 48 ? 14.202 28.814 33.382 1.00 10.50 ? 129 CYS A O 1 ATOM 356 C CB . CYS A 1 48 ? 16.689 30.174 34.709 1.00 16.63 ? 129 CYS A CB 1 ATOM 357 S SG . CYS A 1 48 ? 17.729 31.510 35.365 1.00 20.27 ? 129 CYS A SG 1 ATOM 358 N N . ARG A 1 49 ? 15.786 28.844 31.788 1.00 7.82 ? 130 ARG A N 1 ATOM 359 C CA . ARG A 1 49 ? 15.230 27.702 31.077 1.00 7.36 ? 130 ARG A CA 1 ATOM 360 C C . ARG A 1 49 ? 16.264 26.603 30.891 1.00 7.79 ? 130 ARG A C 1 ATOM 361 O O . ARG A 1 49 ? 17.464 26.870 30.818 1.00 8.99 ? 130 ARG A O 1 ATOM 362 C CB . ARG A 1 49 ? 14.695 28.135 29.710 1.00 8.54 ? 130 ARG A CB 1 ATOM 363 C CG . ARG A 1 49 ? 13.642 29.228 29.768 1.00 11.19 ? 130 ARG A CG 1 ATOM 364 C CD . ARG A 1 49 ? 13.100 29.539 28.383 1.00 13.97 ? 130 ARG A CD 1 ATOM 365 N NE . ARG A 1 49 ? 12.476 28.371 27.766 1.00 12.30 ? 130 ARG A NE 1 ATOM 366 C CZ . ARG A 1 49 ? 11.244 27.952 28.038 1.00 11.93 ? 130 ARG A CZ 1 ATOM 367 N NH1 . ARG A 1 49 ? 10.500 28.602 28.922 1.00 16.66 ? 130 ARG A NH1 1 ATOM 368 N NH2 . ARG A 1 49 ? 10.756 26.880 27.428 1.00 10.33 ? 130 ARG A NH2 1 ATOM 369 N N . THR A 1 50 ? 15.789 25.366 30.812 1.00 7.33 ? 131 THR A N 1 ATOM 370 C CA . THR A 1 50 ? 16.649 24.240 30.485 1.00 10.24 ? 131 THR A CA 1 ATOM 371 C C . THR A 1 50 ? 16.513 23.915 29.004 1.00 7.78 ? 131 THR A C 1 ATOM 372 O O . THR A 1 50 ? 15.424 23.599 28.529 1.00 6.36 ? 131 THR A O 1 ATOM 373 C CB . THR A 1 50 ? 16.281 22.984 31.295 1.00 12.71 ? 131 THR A CB 1 ATOM 374 O OG1 . THR A 1 50 ? 16.494 23.229 32.689 1.00 18.93 ? 131 THR A OG1 1 ATOM 375 C CG2 . THR A 1 50 ? 17.136 21.806 30.860 1.00 13.27 ? 131 THR A CG2 1 ATOM 376 N N . PHE A 1 51 ? 17.618 24.007 28.276 1.00 5.20 ? 132 PHE A N 1 ATOM 377 C CA . PHE A 1 51 ? 17.647 23.592 26.882 1.00 5.33 ? 132 PHE A CA 1 ATOM 378 C C . PHE A 1 51 ? 18.175 22.165 26.822 1.00 7.41 ? 132 PHE A C 1 ATOM 379 O O . PHE A 1 51 ? 18.888 21.727 27.722 1.00 7.97 ? 132 PHE A O 1 ATOM 380 C CB . PHE A 1 51 ? 18.535 24.531 26.063 1.00 4.99 ? 132 PHE A CB 1 ATOM 381 C CG . PHE A 1 51 ? 17.960 25.910 25.888 1.00 4.92 ? 132 PHE A CG 1 ATOM 382 C CD1 . PHE A 1 51 ? 18.061 26.850 26.898 1.00 6.65 ? 132 PHE A CD1 1 ATOM 383 C CD2 . PHE A 1 51 ? 17.317 26.262 24.711 1.00 5.96 ? 132 PHE A CD2 1 ATOM 384 C CE1 . PHE A 1 51 ? 17.528 28.120 26.741 1.00 10.08 ? 132 PHE A CE1 1 ATOM 385 C CE2 . PHE A 1 51 ? 16.782 27.527 24.547 1.00 9.64 ? 132 PHE A CE2 1 ATOM 386 C CZ . PHE A 1 51 ? 16.889 28.458 25.563 1.00 8.08 ? 132 PHE A CZ 1 ATOM 387 N N . PHE A 1 52 ? 17.823 21.438 25.769 1.00 5.72 ? 133 PHE A N 1 ATOM 388 C CA . PHE A 1 52 ? 18.250 20.050 25.640 1.00 6.80 ? 133 PHE A CA 1 ATOM 389 C C . PHE A 1 52 ? 18.088 19.539 24.218 1.00 8.18 ? 133 PHE A C 1 ATOM 390 O O . PHE A 1 52 ? 17.267 20.047 23.453 1.00 6.37 ? 133 PHE A O 1 ATOM 391 C CB . PHE A 1 52 ? 17.473 19.154 26.609 1.00 4.58 ? 133 PHE A CB 1 ATOM 392 C CG . PHE A 1 52 ? 15.980 19.314 26.522 1.00 8.19 ? 133 PHE A CG 1 ATOM 393 C CD1 . PHE A 1 52 ? 15.317 20.214 27.340 1.00 10.02 ? 133 PHE A CD1 1 ATOM 394 C CD2 . PHE A 1 52 ? 15.240 18.560 25.627 1.00 8.89 ? 133 PHE A CD2 1 ATOM 395 C CE1 . PHE A 1 52 ? 13.944 20.366 27.263 1.00 6.93 ? 133 PHE A CE1 1 ATOM 396 C CE2 . PHE A 1 52 ? 13.864 18.704 25.546 1.00 11.95 ? 133 PHE A CE2 1 ATOM 397 C CZ . PHE A 1 52 ? 13.218 19.610 26.364 1.00 10.83 ? 133 PHE A CZ 1 ATOM 398 N N . LEU A 1 53 ? 18.883 18.532 23.870 1.00 4.77 ? 134 LEU A N 1 ATOM 399 C CA . LEU A 1 53 ? 18.753 17.869 22.582 1.00 5.86 ? 134 LEU A CA 1 ATOM 400 C C . LEU A 1 53 ? 17.972 16.576 22.750 1.00 8.51 ? 134 LEU A C 1 ATOM 401 O O . LEU A 1 53 ? 18.430 15.647 23.417 1.00 7.64 ? 134 LEU A O 1 ATOM 402 C CB . LEU A 1 53 ? 20.129 17.571 21.982 1.00 7.24 ? 134 LEU A CB 1 ATOM 403 C CG . LEU A 1 53 ? 20.968 18.778 21.565 1.00 7.48 ? 134 LEU A CG 1 ATOM 404 C CD1 . LEU A 1 53 ? 22.272 18.319 20.923 1.00 10.44 ? 134 LEU A CD1 1 ATOM 405 C CD2 . LEU A 1 53 ? 20.181 19.670 20.615 1.00 5.92 ? 134 LEU A CD2 1 ATOM 406 N N . THR A 1 54 ? 16.784 16.527 22.158 1.00 9.71 ? 135 THR A N 1 ATOM 407 C CA . THR A 1 54 ? 15.972 15.322 22.186 1.00 10.51 ? 135 THR A CA 1 ATOM 408 C C . THR A 1 54 ? 16.478 14.344 21.139 1.00 13.90 ? 135 THR A C 1 ATOM 409 O O . THR A 1 54 ? 17.278 14.700 20.274 1.00 14.95 ? 135 THR A O 1 ATOM 410 C CB . THR A 1 54 ? 14.494 15.620 21.866 1.00 10.62 ? 135 THR A CB 1 ATOM 411 O OG1 . THR A 1 54 ? 14.362 15.934 20.474 1.00 14.97 ? 135 THR A OG1 1 ATOM 412 C CG2 . THR A 1 54 ? 13.986 16.785 22.696 1.00 12.96 ? 135 THR A CG2 1 ATOM 413 N N . GLN A 1 55 ? 16.001 13.109 21.225 1.00 12.26 ? 136 GLN A N 1 ATOM 414 C CA . GLN A 1 55 ? 16.276 12.105 20.212 1.00 14.57 ? 136 GLN A CA 1 ATOM 415 C C . GLN A 1 55 ? 15.001 11.858 19.414 1.00 14.73 ? 136 GLN A C 1 ATOM 416 O O . GLN A 1 55 ? 14.906 10.894 18.657 1.00 17.14 ? 136 GLN A O 1 ATOM 417 C CB . GLN A 1 55 ? 16.748 10.805 20.869 1.00 14.20 ? 136 GLN A CB 1 ATOM 418 C CG . GLN A 1 55 ? 18.103 10.903 21.558 1.00 15.15 ? 136 GLN A CG 1 ATOM 419 C CD . GLN A 1 55 ? 19.261 10.853 20.577 1.00 23.28 ? 136 GLN A CD 1 ATOM 420 O OE1 . GLN A 1 55 ? 19.061 10.864 19.362 1.00 18.25 ? 136 GLN A OE1 1 ATOM 421 N NE2 . GLN A 1 55 ? 20.481 10.791 21.102 1.00 19.13 ? 136 GLN A NE2 1 ATOM 422 N N . GLY A 1 56 ? 14.020 12.737 19.596 1.00 8.61 ? 137 GLY A N 1 ATOM 423 C CA . GLY A 1 56 ? 12.729 12.587 18.950 1.00 9.54 ? 137 GLY A CA 1 ATOM 424 C C . GLY A 1 56 ? 12.009 11.340 19.426 1.00 11.71 ? 137 GLY A C 1 ATOM 425 O O . GLY A 1 56 ? 11.283 10.700 18.663 1.00 9.29 ? 137 GLY A O 1 ATOM 426 N N . ALA A 1 57 ? 12.212 10.995 20.694 1.00 3.72 ? 138 ALA A N 1 ATOM 427 C CA . ALA A 1 57 ? 11.619 9.793 21.270 1.00 10.82 ? 138 ALA A CA 1 ATOM 428 C C . ALA A 1 57 ? 11.406 9.947 22.773 1.00 7.14 ? 138 ALA A C 1 ATOM 429 O O . ALA A 1 57 ? 11.990 10.827 23.405 1.00 5.93 ? 138 ALA A O 1 ATOM 430 C CB . ALA A 1 57 ? 12.495 8.581 20.980 1.00 8.11 ? 138 ALA A CB 1 ATOM 431 N N . LEU A 1 58 ? 10.570 9.083 23.341 1.00 6.56 ? 139 LEU A N 1 ATOM 432 C CA . LEU A 1 58 ? 10.278 9.133 24.768 1.00 6.71 ? 139 LEU A CA 1 ATOM 433 C C . LEU A 1 58 ? 10.907 7.960 25.512 1.00 8.05 ? 139 LEU A C 1 ATOM 434 O O . LEU A 1 58 ? 11.138 6.898 24.935 1.00 8.14 ? 139 LEU A O 1 ATOM 435 C CB . LEU A 1 58 ? 8.767 9.132 25.004 1.00 5.89 ? 139 LEU A CB 1 ATOM 436 C CG . LEU A 1 58 ? 7.965 10.252 24.340 1.00 4.93 ? 139 LEU A CG 1 ATOM 437 C CD1 . LEU A 1 58 ? 6.497 10.149 24.724 1.00 9.28 ? 139 LEU A CD1 1 ATOM 438 C CD2 . LEU A 1 58 ? 8.525 11.614 24.725 1.00 5.12 ? 139 LEU A CD2 1 ATOM 439 N N . LEU A 1 59 ? 11.176 8.159 26.798 1.00 8.58 ? 140 LEU A N 1 ATOM 440 C CA . LEU A 1 59 ? 11.706 7.094 27.643 1.00 9.39 ? 140 LEU A CA 1 ATOM 441 C C . LEU A 1 59 ? 10.725 5.929 27.737 1.00 10.32 ? 140 LEU A C 1 ATOM 442 O O . LEU A 1 59 ? 9.509 6.127 27.756 1.00 9.53 ? 140 LEU A O 1 ATOM 443 C CB . LEU A 1 59 ? 12.013 7.620 29.044 1.00 8.97 ? 140 LEU A CB 1 ATOM 444 C CG . LEU A 1 59 ? 13.266 8.480 29.210 1.00 11.31 ? 140 LEU A CG 1 ATOM 445 C CD1 . LEU A 1 59 ? 13.259 9.175 30.565 1.00 12.50 ? 140 LEU A CD1 1 ATOM 446 C CD2 . LEU A 1 59 ? 14.518 7.635 29.041 1.00 11.37 ? 140 LEU A CD2 1 ATOM 447 N N . ASN A 1 60 ? 11.269 4.718 27.797 1.00 8.65 ? 141 ASN A N 1 ATOM 448 C CA . ASN A 1 60 ? 10.470 3.504 27.932 1.00 10.02 ? 141 ASN A CA 1 ATOM 449 C C . ASN A 1 60 ? 9.606 3.203 26.708 1.00 10.82 ? 141 ASN A C 1 ATOM 450 O O . ASN A 1 60 ? 8.628 2.459 26.794 1.00 15.59 ? 141 ASN A O 1 ATOM 451 C CB . ASN A 1 60 ? 9.617 3.550 29.204 1.00 11.35 ? 141 ASN A CB 1 ATOM 452 C CG . ASN A 1 60 ? 9.803 2.322 30.071 1.00 15.21 ? 141 ASN A CG 1 ATOM 453 O OD1 . ASN A 1 60 ? 10.524 1.393 29.703 1.00 12.04 ? 141 ASN A OD1 1 ATOM 454 N ND2 . ASN A 1 60 ? 9.156 2.311 31.231 1.00 16.64 ? 141 ASN A ND2 1 ATOM 455 N N . ASP A 1 61 ? 9.973 3.788 25.572 1.00 10.53 ? 142 ASP A N 1 ATOM 456 C CA . ASP A 1 61 ? 9.345 3.456 24.297 1.00 12.17 ? 142 ASP A CA 1 ATOM 457 C C . ASP A 1 61 ? 10.389 2.880 23.346 1.00 10.62 ? 142 ASP A C 1 ATOM 458 O O . ASP A 1 61 ? 11.581 3.148 23.487 1.00 10.04 ? 142 ASP A O 1 ATOM 459 C CB . ASP A 1 61 ? 8.684 4.684 23.672 1.00 10.46 ? 142 ASP A CB 1 ATOM 460 C CG . ASP A 1 61 ? 8.114 4.398 22.294 1.00 12.17 ? 142 ASP A CG 1 ATOM 461 O OD1 . ASP A 1 61 ? 7.017 3.807 22.211 1.00 13.13 ? 142 ASP A OD1 1 ATOM 462 O OD2 . ASP A 1 61 ? 8.765 4.760 21.292 1.00 11.70 ? 142 ASP A OD2 1 ATOM 463 N N . LYS A 1 62 ? 9.942 2.095 22.372 1.00 10.76 ? 143 LYS A N 1 ATOM 464 C CA . LYS A 1 62 ? 10.868 1.407 21.479 1.00 10.65 ? 143 LYS A CA 1 ATOM 465 C C . LYS A 1 62 ? 11.746 2.356 20.663 1.00 10.16 ? 143 LYS A C 1 ATOM 466 O O . LYS A 1 62 ? 12.851 1.993 20.266 1.00 11.52 ? 143 LYS A O 1 ATOM 467 C CB . LYS A 1 62 ? 10.122 0.439 20.554 1.00 13.13 ? 143 LYS A CB 1 ATOM 468 C CG . LYS A 1 62 ? 9.231 1.104 19.517 1.00 11.83 ? 143 LYS A CG 1 ATOM 469 C CD . LYS A 1 62 ? 8.597 0.059 18.610 1.00 16.08 ? 143 LYS A CD 1 ATOM 470 C CE . LYS A 1 62 ? 7.773 0.699 17.506 1.00 15.92 ? 143 LYS A CE 1 ATOM 471 N NZ . LYS A 1 62 ? 7.252 -0.324 16.559 1.00 17.99 ? 143 LYS A NZ 1 ATOM 472 N N . HIS A 1 63 ? 11.264 3.569 20.417 1.00 8.24 ? 144 HIS A N 1 ATOM 473 C CA . HIS A 1 63 ? 12.016 4.517 19.596 1.00 9.71 ? 144 HIS A CA 1 ATOM 474 C C . HIS A 1 63 ? 13.237 5.087 20.317 1.00 7.93 ? 144 HIS A C 1 ATOM 475 O O . HIS A 1 63 ? 14.044 5.792 19.717 1.00 7.51 ? 144 HIS A O 1 ATOM 476 C CB . HIS A 1 63 ? 11.110 5.637 19.075 1.00 7.22 ? 144 HIS A CB 1 ATOM 477 C CG . HIS A 1 63 ? 10.109 5.175 18.064 1.00 8.60 ? 144 HIS A CG 1 ATOM 478 N ND1 . HIS A 1 63 ? 8.841 4.761 18.404 1.00 8.47 ? 144 HIS A ND1 1 ATOM 479 C CD2 . HIS A 1 63 ? 10.198 5.041 16.716 1.00 8.42 ? 144 HIS A CD2 1 ATOM 480 C CE1 . HIS A 1 63 ? 8.186 4.401 17.313 1.00 9.79 ? 144 HIS A CE1 1 ATOM 481 N NE2 . HIS A 1 63 ? 8.991 4.563 16.277 1.00 9.93 ? 144 HIS A NE2 1 ATOM 482 N N . SER A 1 64 ? 13.372 4.774 21.601 1.00 10.06 ? 145 SER A N 1 ATOM 483 C CA . SER A 1 64 ? 14.554 5.172 22.357 1.00 11.77 ? 145 SER A CA 1 ATOM 484 C C . SER A 1 64 ? 15.715 4.223 22.073 1.00 12.31 ? 145 SER A C 1 ATOM 485 O O . SER A 1 64 ? 16.821 4.413 22.576 1.00 10.98 ? 145 SER A O 1 ATOM 486 C CB . SER A 1 64 ? 14.251 5.204 23.858 1.00 8.92 ? 145 SER A CB 1 ATOM 487 O OG . SER A 1 64 ? 13.953 3.909 24.350 1.00 10.95 ? 145 SER A OG 1 ATOM 488 N N . ASN A 1 65 ? 15.451 3.200 21.263 1.00 7.94 ? 146 ASN A N 1 ATOM 489 C CA . ASN A 1 65 ? 16.456 2.203 20.902 1.00 13.05 ? 146 ASN A CA 1 ATOM 490 C C . ASN A 1 65 ? 17.621 2.837 20.150 1.00 17.31 ? 146 ASN A C 1 ATOM 491 O O . ASN A 1 65 ? 17.416 3.563 19.175 1.00 17.25 ? 146 ASN A O 1 ATOM 492 C CB . ASN A 1 65 ? 15.815 1.109 20.040 1.00 13.57 ? 146 ASN A CB 1 ATOM 493 C CG . ASN A 1 65 ? 16.510 -0.239 20.169 1.00 18.09 ? 146 ASN A CG 1 ATOM 494 O OD1 . ASN A 1 65 ? 17.666 -0.326 20.587 1.00 12.58 ? 146 ASN A OD1 1 ATOM 495 N ND2 . ASN A 1 65 ? 15.794 -1.303 19.800 1.00 20.69 ? 146 ASN A ND2 1 ATOM 496 N N . GLY A 1 66 ? 18.839 2.570 20.612 1.00 19.77 ? 147 GLY A N 1 ATOM 497 C CA . GLY A 1 66 ? 20.038 3.030 19.932 1.00 21.48 ? 147 GLY A CA 1 ATOM 498 C C . GLY A 1 66 ? 20.339 4.507 20.105 1.00 23.72 ? 147 GLY A C 1 ATOM 499 O O . GLY A 1 66 ? 21.085 5.091 19.316 1.00 19.01 ? 147 GLY A O 1 ATOM 500 N N . THR A 1 67 ? 19.770 5.115 21.141 1.00 13.52 ? 148 THR A N 1 ATOM 501 C CA . THR A 1 67 ? 19.950 6.546 21.375 1.00 17.10 ? 148 THR A CA 1 ATOM 502 C C . THR A 1 67 ? 21.321 6.905 21.951 1.00 18.04 ? 148 THR A C 1 ATOM 503 O O . THR A 1 67 ? 21.536 8.029 22.406 1.00 19.65 ? 148 THR A O 1 ATOM 504 C CB . THR A 1 67 ? 18.834 7.136 22.267 1.00 14.32 ? 148 THR A CB 1 ATOM 505 O OG1 . THR A 1 67 ? 18.584 6.262 23.375 1.00 11.67 ? 148 THR A OG1 1 ATOM 506 C CG2 . THR A 1 67 ? 17.548 7.313 21.468 1.00 15.73 ? 148 THR A CG2 1 ATOM 507 N N . ILE A 1 68 ? 22.247 5.953 21.927 1.00 18.20 ? 149 ILE A N 1 ATOM 508 C CA . ILE A 1 68 ? 23.631 6.245 22.274 1.00 18.43 ? 149 ILE A CA 1 ATOM 509 C C . ILE A 1 68 ? 24.256 7.050 21.141 1.00 23.60 ? 149 ILE A C 1 ATOM 510 O O . ILE A 1 68 ? 25.287 7.700 21.316 1.00 27.55 ? 149 ILE A O 1 ATOM 511 C CB . ILE A 1 68 ? 24.447 4.957 22.507 1.00 22.71 ? 149 ILE A CB 1 ATOM 512 C CG1 . ILE A 1 68 ? 25.832 5.296 23.067 1.00 25.83 ? 149 ILE A CG1 1 ATOM 513 C CG2 . ILE A 1 68 ? 24.559 4.154 21.219 1.00 22.38 ? 149 ILE A CG2 1 ATOM 514 C CD1 . ILE A 1 68 ? 26.668 4.088 23.408 1.00 28.18 ? 149 ILE A CD1 1 ATOM 515 N N . LYS A 1 69 ? 23.610 7.008 19.980 1.00 25.91 ? 150 LYS A N 1 ATOM 516 C CA . LYS A 1 69 ? 24.081 7.716 18.793 1.00 26.69 ? 150 LYS A CA 1 ATOM 517 C C . LYS A 1 69 ? 23.933 9.228 18.966 1.00 29.16 ? 150 LYS A C 1 ATOM 518 O O . LYS A 1 69 ? 22.908 9.708 19.453 1.00 25.30 ? 150 LYS A O 1 ATOM 519 C CB . LYS A 1 69 ? 23.307 7.238 17.561 1.00 30.46 ? 150 LYS A CB 1 ATOM 520 C CG . LYS A 1 69 ? 23.778 7.819 16.240 1.00 31.23 ? 150 LYS A CG 1 ATOM 521 C CD . LYS A 1 69 ? 22.945 7.265 15.098 1.00 36.38 ? 150 LYS A CD 1 ATOM 522 C CE . LYS A 1 69 ? 23.308 7.916 13.779 1.00 41.90 ? 150 LYS A CE 1 ATOM 523 N NZ . LYS A 1 69 ? 22.093 8.246 12.977 1.00 39.94 ? 150 LYS A NZ 1 ATOM 524 N N . ASP A 1 70 ? 24.957 9.973 18.559 1.00 21.72 ? 151 ASP A N 1 ATOM 525 C CA . ASP A 1 70 ? 24.998 11.415 18.792 1.00 24.14 ? 151 ASP A CA 1 ATOM 526 C C . ASP A 1 70 ? 24.220 12.240 17.766 1.00 21.93 ? 151 ASP A C 1 ATOM 527 O O . ASP A 1 70 ? 23.575 13.226 18.121 1.00 18.20 ? 151 ASP A O 1 ATOM 528 C CB . ASP A 1 70 ? 26.449 11.901 18.852 1.00 28.01 ? 151 ASP A CB 1 ATOM 529 C CG . ASP A 1 70 ? 27.177 11.415 20.092 1.00 33.19 ? 151 ASP A CG 1 ATOM 530 O OD1 . ASP A 1 70 ? 26.549 11.369 21.172 1.00 26.23 ? 151 ASP A OD1 1 ATOM 531 O OD2 . ASP A 1 70 ? 28.379 11.089 19.987 1.00 36.19 ? 151 ASP A OD2 1 ATOM 532 N N . ARG A 1 71 ? 24.285 11.843 16.499 1.00 14.55 ? 152 ARG A N 1 ATOM 533 C CA . ARG A 1 71 ? 23.718 12.654 15.425 1.00 12.64 ? 152 ARG A CA 1 ATOM 534 C C . ARG A 1 71 ? 22.677 11.903 14.598 1.00 18.40 ? 152 ARG A C 1 ATOM 535 O O . ARG A 1 71 ? 22.835 10.720 14.307 1.00 18.37 ? 152 ARG A O 1 ATOM 536 C CB . ARG A 1 71 ? 24.835 13.184 14.518 1.00 17.23 ? 152 ARG A CB 1 ATOM 537 C CG . ARG A 1 71 ? 25.933 13.925 15.275 1.00 10.73 ? 152 ARG A CG 1 ATOM 538 C CD . ARG A 1 71 ? 27.026 14.441 14.346 1.00 11.94 ? 152 ARG A CD 1 ATOM 539 N NE . ARG A 1 71 ? 27.700 13.363 13.626 1.00 12.97 ? 152 ARG A NE 1 ATOM 540 C CZ . ARG A 1 71 ? 28.637 12.580 14.154 1.00 18.78 ? 152 ARG A CZ 1 ATOM 541 N NH1 . ARG A 1 71 ? 29.009 12.743 15.417 1.00 15.87 ? 152 ARG A NH1 1 ATOM 542 N NH2 . ARG A 1 71 ? 29.197 11.628 13.422 1.00 15.85 ? 152 ARG A NH2 1 ATOM 543 N N . SER A 1 72 ? 21.613 12.607 14.225 1.00 10.92 ? 153 SER A N 1 ATOM 544 C CA . SER A 1 72 ? 20.551 12.044 13.400 1.00 10.74 ? 153 SER A CA 1 ATOM 545 C C . SER A 1 72 ? 19.622 13.171 12.966 1.00 10.11 ? 153 SER A C 1 ATOM 546 O O . SER A 1 72 ? 19.649 14.255 13.549 1.00 8.11 ? 153 SER A O 1 ATOM 547 C CB . SER A 1 72 ? 19.759 10.989 14.176 1.00 12.21 ? 153 SER A CB 1 ATOM 548 O OG . SER A 1 72 ? 18.754 11.590 14.974 1.00 12.88 ? 153 SER A OG 1 ATOM 549 N N . PRO A 1 73 ? 18.801 12.924 11.936 1.00 9.63 ? 154 PRO A N 1 ATOM 550 C CA . PRO A 1 73 ? 17.863 13.949 11.468 1.00 8.58 ? 154 PRO A CA 1 ATOM 551 C C . PRO A 1 73 ? 16.680 14.137 12.417 1.00 8.72 ? 154 PRO A C 1 ATOM 552 O O . PRO A 1 73 ? 15.851 15.017 12.182 1.00 9.48 ? 154 PRO A O 1 ATOM 553 C CB . PRO A 1 73 ? 17.380 13.394 10.123 1.00 9.97 ? 154 PRO A CB 1 ATOM 554 C CG . PRO A 1 73 ? 17.579 11.918 10.226 1.00 11.62 ? 154 PRO A CG 1 ATOM 555 C CD . PRO A 1 73 ? 18.790 11.721 11.084 1.00 11.13 ? 154 PRO A CD 1 ATOM 556 N N . TYR A 1 74 ? 16.608 13.333 13.474 1.00 7.02 ? 155 TYR A N 1 ATOM 557 C CA . TYR A 1 74 ? 15.470 13.387 14.389 1.00 8.91 ? 155 TYR A CA 1 ATOM 558 C C . TYR A 1 74 ? 15.720 14.260 15.614 1.00 10.15 ? 155 TYR A C 1 ATOM 559 O O . TYR A 1 74 ? 14.778 14.660 16.296 1.00 9.48 ? 155 TYR A O 1 ATOM 560 C CB . TYR A 1 74 ? 15.073 11.978 14.837 1.00 10.34 ? 155 TYR A CB 1 ATOM 561 C CG . TYR A 1 74 ? 15.039 10.986 13.704 1.00 11.51 ? 155 TYR A CG 1 ATOM 562 C CD1 . TYR A 1 74 ? 14.140 11.137 12.656 1.00 9.38 ? 155 TYR A CD1 1 ATOM 563 C CD2 . TYR A 1 74 ? 15.908 9.905 13.674 1.00 15.18 ? 155 TYR A CD2 1 ATOM 564 C CE1 . TYR A 1 74 ? 14.108 10.239 11.610 1.00 11.20 ? 155 TYR A CE1 1 ATOM 565 C CE2 . TYR A 1 74 ? 15.881 8.998 12.631 1.00 14.32 ? 155 TYR A CE2 1 ATOM 566 C CZ . TYR A 1 74 ? 14.979 9.170 11.603 1.00 15.39 ? 155 TYR A CZ 1 ATOM 567 O OH . TYR A 1 74 ? 14.947 8.273 10.562 1.00 16.21 ? 155 TYR A OH 1 ATOM 568 N N . ARG A 1 75 ? 16.985 14.552 15.898 1.00 7.16 ? 156 ARG A N 1 ATOM 569 C CA . ARG A 1 75 ? 17.315 15.324 17.090 1.00 9.50 ? 156 ARG A CA 1 ATOM 570 C C . ARG A 1 75 ? 16.882 16.776 16.942 1.00 6.20 ? 156 ARG A C 1 ATOM 571 O O . ARG A 1 75 ? 17.052 17.383 15.884 1.00 6.98 ? 156 ARG A O 1 ATOM 572 C CB . ARG A 1 75 ? 18.811 15.235 17.414 1.00 10.00 ? 156 ARG A CB 1 ATOM 573 C CG . ARG A 1 75 ? 19.307 13.815 17.625 1.00 13.35 ? 156 ARG A CG 1 ATOM 574 C CD . ARG A 1 75 ? 20.562 13.780 18.482 1.00 13.60 ? 156 ARG A CD 1 ATOM 575 N NE . ARG A 1 75 ? 20.267 14.054 19.886 1.00 12.88 ? 156 ARG A NE 1 ATOM 576 C CZ . ARG A 1 75 ? 21.176 14.053 20.854 1.00 17.35 ? 156 ARG A CZ 1 ATOM 577 N NH1 . ARG A 1 75 ? 22.446 13.794 20.574 1.00 13.96 ? 156 ARG A NH1 1 ATOM 578 N NH2 . ARG A 1 75 ? 20.816 14.312 22.104 1.00 16.98 ? 156 ARG A NH2 1 ATOM 579 N N . THR A 1 76 ? 16.307 17.324 18.007 1.00 7.12 ? 157 THR A N 1 ATOM 580 C CA . THR A 1 76 ? 15.865 18.710 18.000 1.00 6.21 ? 157 THR A CA 1 ATOM 581 C C . THR A 1 76 ? 16.231 19.413 19.299 1.00 8.96 ? 157 THR A C 1 ATOM 582 O O . THR A 1 76 ? 16.260 18.802 20.369 1.00 9.52 ? 157 THR A O 1 ATOM 583 C CB . THR A 1 76 ? 14.342 18.823 17.779 1.00 11.51 ? 157 THR A CB 1 ATOM 584 O OG1 . THR A 1 76 ? 13.650 18.145 18.834 1.00 12.65 ? 157 THR A OG1 1 ATOM 585 C CG2 . THR A 1 76 ? 13.947 18.216 16.437 1.00 9.07 ? 157 THR A CG2 1 ATOM 586 N N . LEU A 1 77 ? 16.520 20.703 19.193 1.00 6.62 ? 158 LEU A N 1 ATOM 587 C CA . LEU A 1 77 ? 16.750 21.530 20.365 1.00 6.00 ? 158 LEU A CA 1 ATOM 588 C C . LEU A 1 77 ? 15.412 22.018 20.898 1.00 6.93 ? 158 LEU A C 1 ATOM 589 O O . LEU A 1 77 ? 14.633 22.630 20.170 1.00 6.83 ? 158 LEU A O 1 ATOM 590 C CB . LEU A 1 77 ? 17.630 22.727 20.008 1.00 6.64 ? 158 LEU A CB 1 ATOM 591 C CG . LEU A 1 77 ? 17.910 23.699 21.155 1.00 6.10 ? 158 LEU A CG 1 ATOM 592 C CD1 . LEU A 1 77 ? 18.824 23.050 22.185 1.00 5.29 ? 158 LEU A CD1 1 ATOM 593 C CD2 . LEU A 1 77 ? 18.514 24.990 20.627 1.00 7.88 ? 158 LEU A CD2 1 ATOM 594 N N . MET A 1 78 ? 15.142 21.734 22.167 1.00 7.92 ? 159 MET A N 1 ATOM 595 C CA . MET A 1 78 ? 13.926 22.212 22.812 1.00 8.41 ? 159 MET A CA 1 ATOM 596 C C . MET A 1 78 ? 14.273 22.801 24.172 1.00 7.41 ? 159 MET A C 1 ATOM 597 O O . MET A 1 78 ? 15.413 22.696 24.622 1.00 7.01 ? 159 MET A O 1 ATOM 598 C CB . MET A 1 78 ? 12.905 21.079 22.949 1.00 9.06 ? 159 MET A CB 1 ATOM 599 C CG . MET A 1 78 ? 12.568 20.400 21.623 1.00 12.60 ? 159 MET A CG 1 ATOM 600 S SD . MET A 1 78 ? 11.168 19.269 21.721 1.00 20.34 ? 159 MET A SD 1 ATOM 601 C CE . MET A 1 78 ? 9.821 20.420 21.977 1.00 13.92 ? 159 MET A CE 1 ATOM 602 N N . SER A 1 79 ? 13.301 23.436 24.819 1.00 4.45 ? 160 SER A N 1 ATOM 603 C CA . SER A 1 79 ? 13.537 24.010 26.137 1.00 4.96 ? 160 SER A CA 1 ATOM 604 C C . SER A 1 79 ? 12.294 23.944 27.011 1.00 6.05 ? 160 SER A C 1 ATOM 605 O O . SER A 1 79 ? 11.171 23.914 26.515 1.00 4.90 ? 160 SER A O 1 ATOM 606 C CB . SER A 1 79 ? 14.016 25.460 26.025 1.00 5.33 ? 160 SER A CB 1 ATOM 607 O OG . SER A 1 79 ? 12.968 26.319 25.612 1.00 8.52 ? 160 SER A OG 1 ATOM 608 N N . CYS A 1 80 ? 12.507 23.923 28.320 1.00 8.41 ? 161 CYS A N 1 ATOM 609 C CA . CYS A 1 80 ? 11.408 23.966 29.272 1.00 10.16 ? 161 CYS A CA 1 ATOM 610 C C . CYS A 1 80 ? 11.858 24.740 30.504 1.00 10.55 ? 161 CYS A C 1 ATOM 611 O O . CYS A 1 80 ? 13.049 24.981 30.683 1.00 8.40 ? 161 CYS A O 1 ATOM 612 C CB . CYS A 1 80 ? 10.969 22.548 29.650 1.00 10.06 ? 161 CYS A CB 1 ATOM 613 S SG . CYS A 1 80 ? 12.234 21.568 30.492 1.00 14.06 ? 161 CYS A SG 1 ATOM 614 N N . PRO A 1 81 ? 10.906 25.146 31.355 1.00 10.71 ? 162 PRO A N 1 ATOM 615 C CA . PRO A 1 81 ? 11.290 25.841 32.587 1.00 8.34 ? 162 PRO A CA 1 ATOM 616 C C . PRO A 1 81 ? 12.262 24.996 33.399 1.00 7.84 ? 162 PRO A C 1 ATOM 617 O O . PRO A 1 81 ? 12.159 23.770 33.391 1.00 6.88 ? 162 PRO A O 1 ATOM 618 C CB . PRO A 1 81 ? 9.962 25.987 33.329 1.00 12.09 ? 162 PRO A CB 1 ATOM 619 C CG . PRO A 1 81 ? 8.927 25.993 32.237 1.00 14.57 ? 162 PRO A CG 1 ATOM 620 C CD . PRO A 1 81 ? 9.445 25.041 31.202 1.00 9.66 ? 162 PRO A CD 1 ATOM 621 N N . ILE A 1 82 ? 13.195 25.642 34.087 1.00 11.16 ? 163 ILE A N 1 ATOM 622 C CA . ILE A 1 82 ? 14.194 24.917 34.861 1.00 10.92 ? 163 ILE A CA 1 ATOM 623 C C . ILE A 1 82 ? 13.544 24.082 35.960 1.00 11.62 ? 163 ILE A C 1 ATOM 624 O O . ILE A 1 82 ? 12.605 24.530 36.618 1.00 9.43 ? 163 ILE A O 1 ATOM 625 C CB . ILE A 1 82 ? 15.244 25.875 35.469 1.00 12.77 ? 163 ILE A CB 1 ATOM 626 C CG1 . ILE A 1 82 ? 16.497 25.102 35.875 1.00 14.95 ? 163 ILE A CG1 1 ATOM 627 C CG2 . ILE A 1 82 ? 14.675 26.638 36.643 1.00 12.07 ? 163 ILE A CG2 1 ATOM 628 C CD1 . ILE A 1 82 ? 17.555 25.964 36.510 1.00 17.11 ? 163 ILE A CD1 1 ATOM 629 N N . GLY A 1 83 ? 14.030 22.858 36.137 1.00 6.74 ? 164 GLY A N 1 ATOM 630 C CA . GLY A 1 83 ? 13.538 21.998 37.198 1.00 9.34 ? 164 GLY A CA 1 ATOM 631 C C . GLY A 1 83 ? 12.384 21.103 36.784 1.00 9.77 ? 164 GLY A C 1 ATOM 632 O O . GLY A 1 83 ? 12.036 20.164 37.498 1.00 13.24 ? 164 GLY A O 1 ATOM 633 N N . GLU A 1 84 ? 11.784 21.398 35.634 1.00 10.04 ? 165 GLU A N 1 ATOM 634 C CA . GLU A 1 84 ? 10.689 20.584 35.118 1.00 10.64 ? 165 GLU A CA 1 ATOM 635 C C . GLU A 1 84 ? 11.226 19.497 34.195 1.00 11.82 ? 165 GLU A C 1 ATOM 636 O O . GLU A 1 84 ? 12.259 19.679 33.552 1.00 10.35 ? 165 GLU A O 1 ATOM 637 C CB . GLU A 1 84 ? 9.673 21.452 34.370 1.00 10.93 ? 165 GLU A CB 1 ATOM 638 C CG . GLU A 1 84 ? 9.021 22.531 35.221 1.00 13.23 ? 165 GLU A CG 1 ATOM 639 C CD . GLU A 1 84 ? 7.921 23.271 34.482 1.00 16.36 ? 165 GLU A CD 1 ATOM 640 O OE1 . GLU A 1 84 ? 7.426 22.744 33.463 1.00 20.70 ? 165 GLU A OE1 1 ATOM 641 O OE2 . GLU A 1 84 ? 7.549 24.380 34.919 1.00 16.25 ? 165 GLU A OE2 1 ATOM 642 N N . VAL A 1 85 ? 10.533 18.365 34.133 1.00 9.20 ? 166 VAL A N 1 ATOM 643 C CA . VAL A 1 85 ? 10.942 17.297 33.228 1.00 9.10 ? 166 VAL A CA 1 ATOM 644 C C . VAL A 1 85 ? 10.684 17.712 31.785 1.00 8.46 ? 166 VAL A C 1 ATOM 645 O O . VAL A 1 85 ? 9.683 18.365 31.491 1.00 9.59 ? 166 VAL A O 1 ATOM 646 C CB . VAL A 1 85 ? 10.213 15.968 33.517 1.00 8.05 ? 166 VAL A CB 1 ATOM 647 C CG1 . VAL A 1 85 ? 10.519 15.490 34.926 1.00 9.52 ? 166 VAL A CG1 1 ATOM 648 C CG2 . VAL A 1 85 ? 8.713 16.119 33.302 1.00 12.28 ? 166 VAL A CG2 1 ATOM 649 N N . PRO A 1 86 ? 11.606 17.352 30.882 1.00 8.55 ? 167 PRO A N 1 ATOM 650 C CA . PRO A 1 86 ? 11.458 17.643 29.453 1.00 8.91 ? 167 PRO A CA 1 ATOM 651 C C . PRO A 1 86 ? 10.389 16.754 28.826 1.00 8.58 ? 167 PRO A C 1 ATOM 652 O O . PRO A 1 86 ? 10.652 15.596 28.509 1.00 10.50 ? 167 PRO A O 1 ATOM 653 C CB . PRO A 1 86 ? 12.837 17.296 28.884 1.00 9.84 ? 167 PRO A CB 1 ATOM 654 C CG . PRO A 1 86 ? 13.389 16.285 29.830 1.00 10.78 ? 167 PRO A CG 1 ATOM 655 C CD . PRO A 1 86 ? 12.895 16.706 31.185 1.00 8.76 ? 167 PRO A CD 1 ATOM 656 N N . SER A 1 87 ? 9.189 17.298 28.660 1.00 8.83 ? 168 SER A N 1 ATOM 657 C CA . SER A 1 87 ? 8.076 16.541 28.104 1.00 9.03 ? 168 SER A CA 1 ATOM 658 C C . SER A 1 87 ? 7.520 17.239 26.872 1.00 8.59 ? 168 SER A C 1 ATOM 659 O O . SER A 1 87 ? 7.643 18.454 26.738 1.00 8.43 ? 168 SER A O 1 ATOM 660 C CB . SER A 1 87 ? 6.976 16.384 29.156 1.00 11.01 ? 168 SER A CB 1 ATOM 661 O OG . SER A 1 87 ? 5.819 15.790 28.601 1.00 13.87 ? 168 SER A OG 1 ATOM 662 N N . PRO A 1 88 ? 6.910 16.470 25.959 1.00 10.04 ? 169 PRO A N 1 ATOM 663 C CA . PRO A 1 88 ? 6.259 17.076 24.795 1.00 10.74 ? 169 PRO A CA 1 ATOM 664 C C . PRO A 1 88 ? 5.125 18.011 25.205 1.00 14.09 ? 169 PRO A C 1 ATOM 665 O O . PRO A 1 88 ? 4.671 18.807 24.384 1.00 12.72 ? 169 PRO A O 1 ATOM 666 C CB . PRO A 1 88 ? 5.690 15.869 24.032 1.00 9.90 ? 169 PRO A CB 1 ATOM 667 C CG . PRO A 1 88 ? 5.761 14.712 24.988 1.00 10.57 ? 169 PRO A CG 1 ATOM 668 C CD . PRO A 1 88 ? 6.918 15.000 25.885 1.00 8.78 ? 169 PRO A CD 1 ATOM 669 N N . TYR A 1 89 A 4.682 17.923 26.457 1.00 9.86 ? 169 TYR A N 1 ATOM 670 C CA . TYR A 1 89 A 3.535 18.708 26.907 1.00 9.76 ? 169 TYR A CA 1 ATOM 671 C C . TYR A 1 89 A 3.925 20.017 27.592 1.00 13.92 ? 169 TYR A C 1 ATOM 672 O O . TYR A 1 89 A 3.072 20.868 27.841 1.00 12.05 ? 169 TYR A O 1 ATOM 673 C CB . TYR A 1 89 A 2.637 17.883 27.835 1.00 11.97 ? 169 TYR A CB 1 ATOM 674 C CG . TYR A 1 89 A 2.375 16.473 27.354 1.00 8.39 ? 169 TYR A CG 1 ATOM 675 C CD1 . TYR A 1 89 A 2.063 16.215 26.025 1.00 11.71 ? 169 TYR A CD1 1 ATOM 676 C CD2 . TYR A 1 89 A 2.427 15.400 28.233 1.00 12.19 ? 169 TYR A CD2 1 ATOM 677 C CE1 . TYR A 1 89 A 1.824 14.924 25.584 1.00 10.49 ? 169 TYR A CE1 1 ATOM 678 C CE2 . TYR A 1 89 A 2.185 14.108 27.804 1.00 12.31 ? 169 TYR A CE2 1 ATOM 679 C CZ . TYR A 1 89 A 1.886 13.876 26.479 1.00 10.71 ? 169 TYR A CZ 1 ATOM 680 O OH . TYR A 1 89 A 1.647 12.591 26.050 1.00 12.23 ? 169 TYR A OH 1 ATOM 681 N N . ASN A 1 90 ? 5.207 20.184 27.898 1.00 10.43 ? 170 ASN A N 1 ATOM 682 C CA . ASN A 1 90 ? 5.654 21.412 28.547 1.00 12.00 ? 170 ASN A CA 1 ATOM 683 C C . ASN A 1 90 ? 6.878 22.032 27.884 1.00 11.34 ? 170 ASN A C 1 ATOM 684 O O . ASN A 1 90 ? 7.415 23.025 28.372 1.00 15.40 ? 170 ASN A O 1 ATOM 685 C CB . ASN A 1 90 ? 5.938 21.167 30.030 1.00 15.12 ? 170 ASN A CB 1 ATOM 686 C CG . ASN A 1 90 ? 7.261 20.470 30.258 1.00 15.91 ? 170 ASN A CG 1 ATOM 687 O OD1 . ASN A 1 90 ? 7.718 19.696 29.418 1.00 15.62 ? 170 ASN A OD1 1 ATOM 688 N ND2 . ASN A 1 90 ? 7.888 20.744 31.398 1.00 18.51 ? 170 ASN A ND2 1 ATOM 689 N N . SER A 1 91 ? 7.314 21.449 26.771 1.00 10.43 ? 171 SER A N 1 ATOM 690 C CA . SER A 1 91 ? 8.539 21.894 26.110 1.00 10.54 ? 171 SER A CA 1 ATOM 691 C C . SER A 1 91 ? 8.290 22.764 24.881 1.00 11.67 ? 171 SER A C 1 ATOM 692 O O . SER A 1 91 ? 7.386 22.504 24.086 1.00 12.73 ? 171 SER A O 1 ATOM 693 C CB . SER A 1 91 ? 9.416 20.696 25.738 1.00 12.56 ? 171 SER A CB 1 ATOM 694 O OG . SER A 1 91 ? 9.886 20.040 26.902 1.00 13.06 ? 171 SER A OG 1 ATOM 695 N N . ARG A 1 92 ? 9.105 23.801 24.735 1.00 7.97 ? 172 ARG A N 1 ATOM 696 C CA . ARG A 1 92 ? 9.027 24.688 23.582 1.00 11.24 ? 172 ARG A CA 1 ATOM 697 C C . ARG A 1 92 ? 10.018 24.237 22.511 1.00 9.58 ? 172 ARG A C 1 ATOM 698 O O . ARG A 1 92 ? 11.168 23.928 22.815 1.00 9.31 ? 172 ARG A O 1 ATOM 699 C CB . ARG A 1 92 ? 9.327 26.126 24.013 1.00 12.64 ? 172 ARG A CB 1 ATOM 700 C CG . ARG A 1 92 ? 9.314 27.143 22.887 1.00 25.35 ? 172 ARG A CG 1 ATOM 701 C CD . ARG A 1 92 ? 8.880 28.508 23.399 1.00 36.78 ? 172 ARG A CD 1 ATOM 702 N NE . ARG A 1 92 ? 9.965 29.241 24.044 1.00 32.40 ? 172 ARG A NE 1 ATOM 703 C CZ . ARG A 1 92 ? 9.807 30.039 25.097 1.00 37.73 ? 172 ARG A CZ 1 ATOM 704 N NH1 . ARG A 1 92 ? 8.609 30.199 25.644 1.00 37.16 ? 172 ARG A NH1 1 ATOM 705 N NH2 . ARG A 1 92 ? 10.850 30.673 25.613 1.00 28.21 ? 172 ARG A NH2 1 ATOM 706 N N . PHE A 1 93 ? 9.574 24.192 21.259 1.00 7.47 ? 173 PHE A N 1 ATOM 707 C CA . PHE A 1 93 ? 10.475 23.835 20.169 1.00 8.87 ? 173 PHE A CA 1 ATOM 708 C C . PHE A 1 93 ? 11.400 25.000 19.826 1.00 7.18 ? 173 PHE A C 1 ATOM 709 O O . PHE A 1 93 ? 10.953 26.140 19.705 1.00 8.56 ? 173 PHE A O 1 ATOM 710 C CB . PHE A 1 93 ? 9.700 23.402 18.925 1.00 8.81 ? 173 PHE A CB 1 ATOM 711 C CG . PHE A 1 93 ? 10.581 23.127 17.743 1.00 6.13 ? 173 PHE A CG 1 ATOM 712 C CD1 . PHE A 1 93 ? 11.190 21.893 17.590 1.00 8.87 ? 173 PHE A CD1 1 ATOM 713 C CD2 . PHE A 1 93 ? 10.821 24.112 16.798 1.00 6.18 ? 173 PHE A CD2 1 ATOM 714 C CE1 . PHE A 1 93 ? 12.014 21.641 16.509 1.00 8.81 ? 173 PHE A CE1 1 ATOM 715 C CE2 . PHE A 1 93 ? 11.644 23.864 15.716 1.00 6.60 ? 173 PHE A CE2 1 ATOM 716 C CZ . PHE A 1 93 ? 12.240 22.629 15.573 1.00 6.10 ? 173 PHE A CZ 1 ATOM 717 N N . GLU A 1 94 ? 12.688 24.711 19.665 1.00 7.74 ? 174 GLU A N 1 ATOM 718 C CA . GLU A 1 94 ? 13.660 25.750 19.335 1.00 7.26 ? 174 GLU A CA 1 ATOM 719 C C . GLU A 1 94 ? 14.211 25.591 17.917 1.00 7.67 ? 174 GLU A C 1 ATOM 720 O O . GLU A 1 94 ? 14.138 26.516 17.109 1.00 9.90 ? 174 GLU A O 1 ATOM 721 C CB . GLU A 1 94 ? 14.804 25.768 20.354 1.00 9.24 ? 174 GLU A CB 1 ATOM 722 C CG . GLU A 1 94 ? 14.352 25.946 21.804 1.00 7.02 ? 174 GLU A CG 1 ATOM 723 C CD . GLU A 1 94 ? 13.806 27.335 22.092 1.00 12.65 ? 174 GLU A CD 1 ATOM 724 O OE1 . GLU A 1 94 ? 13.848 28.198 21.189 1.00 12.56 ? 174 GLU A OE1 1 ATOM 725 O OE2 . GLU A 1 94 ? 13.337 27.567 23.228 1.00 13.36 ? 174 GLU A OE2 1 ATOM 726 N N . SER A 1 95 ? 14.749 24.414 17.613 1.00 5.62 ? 175 SER A N 1 ATOM 727 C CA . SER A 1 95 ? 15.402 24.196 16.325 1.00 8.21 ? 175 SER A CA 1 ATOM 728 C C . SER A 1 95 ? 15.684 22.719 16.078 1.00 7.71 ? 175 SER A C 1 ATOM 729 O O . SER A 1 95 ? 15.735 21.928 17.015 1.00 6.51 ? 175 SER A O 1 ATOM 730 C CB . SER A 1 95 ? 16.714 24.987 16.278 1.00 12.00 ? 175 SER A CB 1 ATOM 731 O OG . SER A 1 95 ? 17.402 24.783 15.058 1.00 20.23 ? 175 SER A OG 1 ATOM 732 N N . VAL A 1 96 ? 15.853 22.345 14.813 1.00 6.52 ? 176 VAL A N 1 ATOM 733 C CA . VAL A 1 96 ? 16.302 21.000 14.477 1.00 5.64 ? 176 VAL A CA 1 ATOM 734 C C . VAL A 1 96 ? 17.818 20.986 14.617 1.00 6.14 ? 176 VAL A C 1 ATOM 735 O O . VAL A 1 96 ? 18.503 21.798 13.997 1.00 8.77 ? 176 VAL A O 1 ATOM 736 C CB . VAL A 1 96 ? 15.921 20.613 13.036 1.00 6.89 ? 176 VAL A CB 1 ATOM 737 C CG1 . VAL A 1 96 ? 16.366 19.190 12.735 1.00 6.19 ? 176 VAL A CG1 1 ATOM 738 C CG2 . VAL A 1 96 ? 14.418 20.767 12.820 1.00 6.48 ? 176 VAL A CG2 1 ATOM 739 N N . ALA A 1 97 ? 18.349 20.080 15.433 1.00 7.33 ? 177 ALA A N 1 ATOM 740 C CA . ALA A 1 97 ? 19.768 20.151 15.774 1.00 8.46 ? 177 ALA A CA 1 ATOM 741 C C . ALA A 1 97 ? 20.321 18.906 16.461 1.00 7.05 ? 177 ALA A C 1 ATOM 742 O O . ALA A 1 97 ? 19.660 18.308 17.312 1.00 7.44 ? 177 ALA A O 1 ATOM 743 C CB . ALA A 1 97 ? 20.023 21.377 16.651 1.00 7.50 ? 177 ALA A CB 1 ATOM 744 N N . TRP A 1 98 ? 21.541 18.525 16.086 1.00 3.92 ? 178 TRP A N 1 ATOM 745 C CA . TRP A 1 98 ? 22.292 17.525 16.843 1.00 5.73 ? 178 TRP A CA 1 ATOM 746 C C . TRP A 1 98 ? 23.500 18.142 17.557 1.00 6.01 ? 178 TRP A C 1 ATOM 747 O O . TRP A 1 98 ? 24.300 17.438 18.173 1.00 6.58 ? 178 TRP A O 1 ATOM 748 C CB . TRP A 1 98 ? 22.694 16.314 15.985 1.00 8.21 ? 178 TRP A CB 1 ATOM 749 C CG . TRP A 1 98 ? 23.224 16.603 14.599 1.00 7.40 ? 178 TRP A CG 1 ATOM 750 C CD1 . TRP A 1 98 ? 22.584 16.367 13.414 1.00 6.82 ? 178 TRP A CD1 1 ATOM 751 C CD2 . TRP A 1 98 ? 24.512 17.137 14.256 1.00 4.76 ? 178 TRP A CD2 1 ATOM 752 N NE1 . TRP A 1 98 ? 23.386 16.732 12.360 1.00 8.58 ? 178 TRP A NE1 1 ATOM 753 C CE2 . TRP A 1 98 ? 24.574 17.209 12.849 1.00 8.70 ? 178 TRP A CE2 1 ATOM 754 C CE3 . TRP A 1 98 ? 25.613 17.572 15.003 1.00 6.86 ? 178 TRP A CE3 1 ATOM 755 C CZ2 . TRP A 1 98 ? 25.692 17.696 12.173 1.00 6.78 ? 178 TRP A CZ2 1 ATOM 756 C CZ3 . TRP A 1 98 ? 26.726 18.053 14.328 1.00 8.20 ? 178 TRP A CZ3 1 ATOM 757 C CH2 . TRP A 1 98 ? 26.755 18.112 12.927 1.00 6.25 ? 178 TRP A CH2 1 ATOM 758 N N . SER A 1 99 ? 23.609 19.463 17.464 1.00 6.01 ? 179 SER A N 1 ATOM 759 C CA . SER A 1 99 ? 24.574 20.244 18.233 1.00 7.72 ? 179 SER A CA 1 ATOM 760 C C . SER A 1 99 ? 24.008 21.652 18.358 1.00 7.70 ? 179 SER A C 1 ATOM 761 O O . SER A 1 99 ? 23.447 22.179 17.400 1.00 9.77 ? 179 SER A O 1 ATOM 762 C CB . SER A 1 99 ? 25.935 20.279 17.538 1.00 7.86 ? 179 SER A CB 1 ATOM 763 O OG . SER A 1 99 ? 26.884 20.994 18.311 1.00 7.99 ? 179 SER A OG 1 ATOM 764 N N . ALA A 1 100 ? 24.139 22.266 19.529 1.00 7.71 ? 180 ALA A N 1 ATOM 765 C CA . ALA A 1 100 ? 23.434 23.523 19.753 1.00 6.20 ? 180 ALA A CA 1 ATOM 766 C C . ALA A 1 100 ? 24.038 24.456 20.797 1.00 9.92 ? 180 ALA A C 1 ATOM 767 O O . ALA A 1 100 ? 24.941 24.091 21.551 1.00 7.75 ? 180 ALA A O 1 ATOM 768 C CB . ALA A 1 100 ? 21.967 23.244 20.085 1.00 8.55 ? 180 ALA A CB 1 ATOM 769 N N . SER A 1 101 ? 23.513 25.677 20.813 1.00 7.85 ? 181 SER A N 1 ATOM 770 C CA . SER A 1 101 ? 23.810 26.662 21.840 1.00 7.55 ? 181 SER A CA 1 ATOM 771 C C . SER A 1 101 ? 22.654 27.654 21.859 1.00 5.90 ? 181 SER A C 1 ATOM 772 O O . SER A 1 101 ? 21.883 27.727 20.903 1.00 8.03 ? 181 SER A O 1 ATOM 773 C CB . SER A 1 101 ? 25.123 27.385 21.536 1.00 10.42 ? 181 SER A CB 1 ATOM 774 O OG . SER A 1 101 ? 25.357 28.421 22.476 1.00 12.39 ? 181 SER A OG 1 ATOM 775 N N . ALA A 1 102 ? 22.529 28.409 22.943 1.00 2.46 ? 182 ALA A N 1 ATOM 776 C CA . ALA A 1 102 ? 21.474 29.409 23.058 1.00 2.88 ? 182 ALA A CA 1 ATOM 777 C C . ALA A 1 102 ? 21.810 30.413 24.153 1.00 6.33 ? 182 ALA A C 1 ATOM 778 O O . ALA A 1 102 ? 22.544 30.095 25.087 1.00 6.09 ? 182 ALA A O 1 ATOM 779 C CB . ALA A 1 102 ? 20.132 28.741 23.348 1.00 5.88 ? 182 ALA A CB 1 ATOM 780 N N . CYS A 1 103 ? 21.265 31.621 24.033 1.00 6.23 ? 183 CYS A N 1 ATOM 781 C CA . CYS A 1 103 ? 21.457 32.661 25.041 1.00 8.87 ? 183 CYS A CA 1 ATOM 782 C C . CYS A 1 103 ? 20.542 33.854 24.780 1.00 8.84 ? 183 CYS A C 1 ATOM 783 O O . CYS A 1 103 ? 20.044 34.032 23.670 1.00 10.14 ? 183 CYS A O 1 ATOM 784 C CB . CYS A 1 103 ? 22.919 33.113 25.088 1.00 8.12 ? 183 CYS A CB 1 ATOM 785 S SG . CYS A 1 103 ? 23.602 33.603 23.487 1.00 13.24 ? 183 CYS A SG 1 ATOM 786 N N . HIS A 1 104 ? 20.325 34.663 25.812 1.00 4.47 ? 184 HIS A N 1 ATOM 787 C CA . HIS A 1 104 ? 19.416 35.805 25.736 1.00 4.82 ? 184 HIS A CA 1 ATOM 788 C C . HIS A 1 104 ? 20.220 37.098 25.858 1.00 6.63 ? 184 HIS A C 1 ATOM 789 O O . HIS A 1 104 ? 21.034 37.237 26.767 1.00 9.36 ? 184 HIS A O 1 ATOM 790 C CB . HIS A 1 104 ? 18.393 35.716 26.874 1.00 4.69 ? 184 HIS A CB 1 ATOM 791 C CG . HIS A 1 104 ? 17.126 36.468 26.618 1.00 4.33 ? 184 HIS A CG 1 ATOM 792 N ND1 . HIS A 1 104 ? 17.027 37.834 26.758 1.00 5.62 ? 184 HIS A ND1 1 ATOM 793 C CD2 . HIS A 1 104 ? 15.893 36.038 26.247 1.00 5.41 ? 184 HIS A CD2 1 ATOM 794 C CE1 . HIS A 1 104 ? 15.794 38.218 26.473 1.00 5.48 ? 184 HIS A CE1 1 ATOM 795 N NE2 . HIS A 1 104 ? 15.089 37.145 26.159 1.00 5.27 ? 184 HIS A NE2 1 ATOM 796 N N . ASP A 1 105 ? 19.998 38.046 24.952 1.00 4.98 ? 185 ASP A N 1 ATOM 797 C CA . ASP A 1 105 ? 20.774 39.288 24.967 1.00 9.08 ? 185 ASP A CA 1 ATOM 798 C C . ASP A 1 105 ? 20.104 40.394 25.781 1.00 9.03 ? 185 ASP A C 1 ATOM 799 O O . ASP A 1 105 ? 20.569 41.534 25.793 1.00 9.86 ? 185 ASP A O 1 ATOM 800 C CB . ASP A 1 105 ? 21.051 39.783 23.542 1.00 8.69 ? 185 ASP A CB 1 ATOM 801 C CG . ASP A 1 105 ? 19.790 40.240 22.825 1.00 8.29 ? 185 ASP A CG 1 ATOM 802 O OD1 . ASP A 1 105 ? 18.686 40.064 23.379 1.00 9.28 ? 185 ASP A OD1 1 ATOM 803 O OD2 . ASP A 1 105 ? 19.904 40.777 21.704 1.00 10.36 ? 185 ASP A OD2 1 ATOM 804 N N . GLY A 1 106 ? 19.016 40.050 26.461 1.00 5.87 ? 186 GLY A N 1 ATOM 805 C CA . GLY A 1 106 ? 18.253 41.023 27.221 1.00 8.10 ? 186 GLY A CA 1 ATOM 806 C C . GLY A 1 106 ? 16.949 41.379 26.535 1.00 11.21 ? 186 GLY A C 1 ATOM 807 O O . GLY A 1 106 ? 15.987 41.784 27.187 1.00 13.73 ? 186 GLY A O 1 ATOM 808 N N . ILE A 1 107 ? 16.921 41.223 25.214 1.00 10.55 ? 187 ILE A N 1 ATOM 809 C CA . ILE A 1 107 ? 15.734 41.524 24.420 1.00 10.55 ? 187 ILE A CA 1 ATOM 810 C C . ILE A 1 107 ? 15.049 40.250 23.935 1.00 11.74 ? 187 ILE A C 1 ATOM 811 O O . ILE A 1 107 ? 13.855 40.050 24.161 1.00 12.57 ? 187 ILE A O 1 ATOM 812 C CB . ILE A 1 107 ? 16.077 42.386 23.187 1.00 14.34 ? 187 ILE A CB 1 ATOM 813 C CG1 . ILE A 1 107 ? 16.901 43.608 23.595 1.00 18.66 ? 187 ILE A CG1 1 ATOM 814 C CG2 . ILE A 1 107 ? 14.805 42.802 22.459 1.00 14.35 ? 187 ILE A CG2 1 ATOM 815 C CD1 . ILE A 1 107 ? 16.211 44.499 24.595 1.00 20.52 ? 187 ILE A CD1 1 ATOM 816 N N . ASN A 1 108 ? 15.808 39.392 23.261 1.00 7.21 ? 188 ASN A N 1 ATOM 817 C CA . ASN A 1 108 ? 15.260 38.156 22.712 1.00 6.66 ? 188 ASN A CA 1 ATOM 818 C C . ASN A 1 108 ? 16.219 36.981 22.839 1.00 6.50 ? 188 ASN A C 1 ATOM 819 O O . ASN A 1 108 ? 17.405 37.159 23.118 1.00 5.68 ? 188 ASN A O 1 ATOM 820 C CB . ASN A 1 108 ? 14.882 38.336 21.239 1.00 8.51 ? 188 ASN A CB 1 ATOM 821 C CG . ASN A 1 108 ? 13.637 39.181 21.052 1.00 11.24 ? 188 ASN A CG 1 ATOM 822 O OD1 . ASN A 1 108 ? 13.669 40.211 20.378 1.00 19.03 ? 188 ASN A OD1 1 ATOM 823 N ND2 . ASN A 1 108 ? 12.531 38.746 21.642 1.00 10.43 ? 188 ASN A ND2 1 ATOM 824 N N . TRP A 1 109 ? 15.686 35.782 22.622 1.00 7.25 ? 189 TRP A N 1 ATOM 825 C CA . TRP A 1 109 ? 16.478 34.562 22.628 1.00 7.58 ? 189 TRP A CA 1 ATOM 826 C C . TRP A 1 109 ? 17.209 34.376 21.308 1.00 7.98 ? 189 TRP A C 1 ATOM 827 O O . TRP A 1 109 ? 16.639 34.569 20.231 1.00 7.78 ? 189 TRP A O 1 ATOM 828 C CB . TRP A 1 109 ? 15.588 33.338 22.877 1.00 6.39 ? 189 TRP A CB 1 ATOM 829 C CG . TRP A 1 109 ? 15.178 33.146 24.304 1.00 8.73 ? 189 TRP A CG 1 ATOM 830 C CD1 . TRP A 1 109 ? 13.950 33.394 24.846 1.00 8.97 ? 189 TRP A CD1 1 ATOM 831 C CD2 . TRP A 1 109 ? 15.996 32.652 25.373 1.00 6.23 ? 189 TRP A CD2 1 ATOM 832 N NE1 . TRP A 1 109 ? 13.953 33.090 26.187 1.00 10.27 ? 189 TRP A NE1 1 ATOM 833 C CE2 . TRP A 1 109 ? 15.198 32.634 26.535 1.00 7.85 ? 189 TRP A CE2 1 ATOM 834 C CE3 . TRP A 1 109 ? 17.326 32.231 25.462 1.00 5.39 ? 189 TRP A CE3 1 ATOM 835 C CZ2 . TRP A 1 109 ? 15.687 32.209 27.770 1.00 13.08 ? 189 TRP A CZ2 1 ATOM 836 C CZ3 . TRP A 1 109 ? 17.809 31.808 26.689 1.00 7.83 ? 189 TRP A CZ3 1 ATOM 837 C CH2 . TRP A 1 109 ? 16.991 31.801 27.825 1.00 8.29 ? 189 TRP A CH2 1 ATOM 838 N N . LEU A 1 110 ? 18.477 34.001 21.402 1.00 8.28 ? 190 LEU A N 1 ATOM 839 C CA . LEU A 1 110 ? 19.224 33.532 20.250 1.00 7.33 ? 190 LEU A CA 1 ATOM 840 C C . LEU A 1 110 ? 19.403 32.030 20.402 1.00 5.70 ? 190 LEU A C 1 ATOM 841 O O . LEU A 1 110 ? 19.804 31.551 21.465 1.00 5.69 ? 190 LEU A O 1 ATOM 842 C CB . LEU A 1 110 ? 20.590 34.215 20.180 1.00 7.10 ? 190 LEU A CB 1 ATOM 843 C CG . LEU A 1 110 ? 21.605 33.593 19.218 1.00 8.86 ? 190 LEU A CG 1 ATOM 844 C CD1 . LEU A 1 110 ? 21.143 33.736 17.773 1.00 6.99 ? 190 LEU A CD1 1 ATOM 845 C CD2 . LEU A 1 110 ? 22.982 34.216 19.411 1.00 9.41 ? 190 LEU A CD2 1 ATOM 846 N N . THR A 1 111 ? 19.083 31.280 19.355 1.00 6.70 ? 191 THR A N 1 ATOM 847 C CA . THR A 1 111 ? 19.354 29.851 19.358 1.00 5.77 ? 191 THR A CA 1 ATOM 848 C C . THR A 1 111 ? 20.199 29.479 18.146 1.00 8.03 ? 191 THR A C 1 ATOM 849 O O . THR A 1 111 ? 20.046 30.055 17.069 1.00 7.90 ? 191 THR A O 1 ATOM 850 C CB . THR A 1 111 ? 18.063 29.000 19.405 1.00 9.92 ? 191 THR A CB 1 ATOM 851 O OG1 . THR A 1 111 ? 17.271 29.244 18.236 1.00 9.13 ? 191 THR A OG1 1 ATOM 852 C CG2 . THR A 1 111 ? 17.246 29.337 20.647 1.00 6.68 ? 191 THR A CG2 1 ATOM 853 N N . ILE A 1 112 ? 21.111 28.535 18.343 1.00 6.25 ? 192 ILE A N 1 ATOM 854 C CA . ILE A 1 112 ? 21.964 28.042 17.269 1.00 6.36 ? 192 ILE A CA 1 ATOM 855 C C . ILE A 1 112 ? 21.826 26.530 17.193 1.00 6.60 ? 192 ILE A C 1 ATOM 856 O O . ILE A 1 112 ? 22.186 25.824 18.131 1.00 9.31 ? 192 ILE A O 1 ATOM 857 C CB . ILE A 1 112 ? 23.439 28.403 17.516 1.00 6.87 ? 192 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 112 ? 23.594 29.915 17.697 1.00 8.45 ? 192 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 112 ? 24.308 27.908 16.373 1.00 8.64 ? 192 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 112 ? 24.994 30.343 18.084 1.00 11.52 ? 192 ILE A CD1 1 ATOM 861 N N . GLY A 1 113 ? 21.292 26.036 16.080 1.00 5.02 ? 193 GLY A N 1 ATOM 862 C CA . GLY A 1 113 ? 21.073 24.610 15.915 1.00 4.36 ? 193 GLY A CA 1 ATOM 863 C C . GLY A 1 113 ? 21.728 24.068 14.661 1.00 5.24 ? 193 GLY A C 1 ATOM 864 O O . GLY A 1 113 ? 21.421 24.509 13.553 1.00 4.44 ? 193 GLY A O 1 ATOM 865 N N . ILE A 1 114 ? 22.632 23.109 14.839 1.00 3.96 ? 194 ILE A N 1 ATOM 866 C CA . ILE A 1 114 ? 23.354 22.506 13.725 1.00 4.12 ? 194 ILE A CA 1 ATOM 867 C C . ILE A 1 114 ? 22.733 21.175 13.317 1.00 6.11 ? 194 ILE A C 1 ATOM 868 O O . ILE A 1 114 ? 22.533 20.291 14.147 1.00 5.58 ? 194 ILE A O 1 ATOM 869 C CB . ILE A 1 114 ? 24.839 22.269 14.075 1.00 6.18 ? 194 ILE A CB 1 ATOM 870 C CG1 . ILE A 1 114 ? 25.514 23.586 14.466 1.00 5.22 ? 194 ILE A CG1 1 ATOM 871 C CG2 . ILE A 1 114 ? 25.565 21.616 12.906 1.00 9.23 ? 194 ILE A CG2 1 ATOM 872 C CD1 . ILE A 1 114 ? 26.902 23.420 15.058 1.00 5.84 ? 194 ILE A CD1 1 ATOM 873 N N . SER A 1 115 ? 22.434 21.037 12.030 1.00 6.71 ? 195 SER A N 1 ATOM 874 C CA . SER A 1 115 ? 21.919 19.784 11.496 1.00 7.63 ? 195 SER A CA 1 ATOM 875 C C . SER A 1 115 ? 22.500 19.550 10.106 1.00 8.38 ? 195 SER A C 1 ATOM 876 O O . SER A 1 115 ? 23.282 20.362 9.608 1.00 9.46 ? 195 SER A O 1 ATOM 877 C CB . SER A 1 115 ? 20.390 19.805 11.447 1.00 7.39 ? 195 SER A CB 1 ATOM 878 O OG . SER A 1 115 ? 19.869 18.502 11.250 1.00 8.07 ? 195 SER A OG 1 ATOM 879 N N . GLY A 1 116 ? 22.122 18.441 9.481 1.00 8.25 ? 196 GLY A N 1 ATOM 880 C CA . GLY A 1 116 ? 22.651 18.099 8.173 1.00 10.66 ? 196 GLY A CA 1 ATOM 881 C C . GLY A 1 116 ? 23.693 16.998 8.249 1.00 10.49 ? 196 GLY A C 1 ATOM 882 O O . GLY A 1 116 ? 23.946 16.452 9.324 1.00 9.22 ? 196 GLY A O 1 ATOM 883 N N . PRO A 1 117 ? 24.310 16.669 7.105 1.00 9.52 ? 197 PRO A N 1 ATOM 884 C CA . PRO A 1 117 ? 25.284 15.576 7.004 1.00 9.01 ? 197 PRO A CA 1 ATOM 885 C C . PRO A 1 117 ? 26.628 15.938 7.628 1.00 11.40 ? 197 PRO A C 1 ATOM 886 O O . PRO A 1 117 ? 26.959 17.118 7.746 1.00 8.64 ? 197 PRO A O 1 ATOM 887 C CB . PRO A 1 117 ? 25.440 15.401 5.494 1.00 8.52 ? 197 PRO A CB 1 ATOM 888 C CG . PRO A 1 117 ? 25.195 16.764 4.947 1.00 13.06 ? 197 PRO A CG 1 ATOM 889 C CD . PRO A 1 117 ? 24.112 17.351 5.813 1.00 6.95 ? 197 PRO A CD 1 ATOM 890 N N . ASP A 1 118 ? 27.395 14.922 8.012 1.00 11.53 ? 198 ASP A N 1 ATOM 891 C CA . ASP A 1 118 ? 28.701 15.128 8.631 1.00 14.85 ? 198 ASP A CA 1 ATOM 892 C C . ASP A 1 118 ? 29.652 15.937 7.752 1.00 14.61 ? 198 ASP A C 1 ATOM 893 O O . ASP A 1 118 ? 30.527 16.636 8.261 1.00 13.89 ? 198 ASP A O 1 ATOM 894 C CB . ASP A 1 118 ? 29.349 13.785 8.987 1.00 13.48 ? 198 ASP A CB 1 ATOM 895 C CG . ASP A 1 118 ? 28.702 13.120 10.188 1.00 20.51 ? 198 ASP A CG 1 ATOM 896 O OD1 . ASP A 1 118 ? 27.781 13.717 10.787 1.00 18.49 ? 198 ASP A OD1 1 ATOM 897 O OD2 . ASP A 1 118 ? 29.121 11.997 10.539 1.00 22.50 ? 198 ASP A OD2 1 ATOM 898 N N . ASN A 1 119 ? 29.483 15.844 6.436 1.00 10.31 ? 199 ASN A N 1 ATOM 899 C CA . ASN A 1 119 ? 30.409 16.493 5.510 1.00 11.27 ? 199 ASN A CA 1 ATOM 900 C C . ASN A 1 119 ? 29.962 17.871 5.019 1.00 14.54 ? 199 ASN A C 1 ATOM 901 O O . ASN A 1 119 ? 30.599 18.460 4.146 1.00 13.05 ? 199 ASN A O 1 ATOM 902 C CB . ASN A 1 119 ? 30.715 15.579 4.317 1.00 15.53 ? 199 ASN A CB 1 ATOM 903 C CG . ASN A 1 119 ? 29.527 15.410 3.387 1.00 24.36 ? 199 ASN A CG 1 ATOM 904 O OD1 . ASN A 1 119 ? 28.427 15.884 3.668 1.00 16.17 ? 199 ASN A OD1 1 ATOM 905 N ND2 . ASN A 1 119 ? 29.748 14.730 2.267 1.00 26.15 ? 199 ASN A ND2 1 ATOM 906 N N . GLY A 1 120 ? 28.872 18.385 5.576 1.00 9.18 ? 200 GLY A N 1 ATOM 907 C CA . GLY A 1 120 ? 28.380 19.693 5.181 1.00 10.17 ? 200 GLY A CA 1 ATOM 908 C C . GLY A 1 120 ? 27.284 20.228 6.084 1.00 8.57 ? 200 GLY A C 1 ATOM 909 O O . GLY A 1 120 ? 26.276 20.751 5.606 1.00 8.07 ? 200 GLY A O 1 ATOM 910 N N . ALA A 1 121 ? 27.486 20.105 7.391 1.00 7.53 ? 201 ALA A N 1 ATOM 911 C CA . ALA A 1 121 ? 26.487 20.531 8.365 1.00 6.86 ? 201 ALA A CA 1 ATOM 912 C C . ALA A 1 121 ? 26.264 22.039 8.308 1.00 7.44 ? 201 ALA A C 1 ATOM 913 O O . ALA A 1 121 ? 27.168 22.798 7.961 1.00 6.75 ? 201 ALA A O 1 ATOM 914 C CB . ALA A 1 121 ? 26.898 20.107 9.767 1.00 7.80 ? 201 ALA A CB 1 ATOM 915 N N . VAL A 1 122 ? 25.054 22.463 8.656 1.00 5.18 ? 202 VAL A N 1 ATOM 916 C CA . VAL A 1 122 ? 24.699 23.876 8.636 1.00 5.90 ? 202 VAL A CA 1 ATOM 917 C C . VAL A 1 122 ? 24.113 24.319 9.968 1.00 6.98 ? 202 VAL A C 1 ATOM 918 O O . VAL A 1 122 ? 23.172 23.711 10.478 1.00 6.86 ? 202 VAL A O 1 ATOM 919 C CB . VAL A 1 122 ? 23.682 24.186 7.521 1.00 8.31 ? 202 VAL A CB 1 ATOM 920 C CG1 . VAL A 1 122 ? 23.127 25.602 7.681 1.00 6.53 ? 202 VAL A CG1 1 ATOM 921 C CG2 . VAL A 1 122 ? 24.327 24.010 6.154 1.00 5.33 ? 202 VAL A CG2 1 ATOM 922 N N . ALA A 1 123 ? 24.680 25.379 10.531 1.00 8.69 ? 203 ALA A N 1 ATOM 923 C CA . ALA A 1 123 ? 24.146 25.970 11.748 1.00 7.78 ? 203 ALA A CA 1 ATOM 924 C C . ALA A 1 123 ? 23.062 26.975 11.384 1.00 6.20 ? 203 ALA A C 1 ATOM 925 O O . ALA A 1 123 ? 23.300 27.905 10.617 1.00 7.21 ? 203 ALA A O 1 ATOM 926 C CB . ALA A 1 123 ? 25.254 26.647 12.540 1.00 6.70 ? 203 ALA A CB 1 ATOM 927 N N . VAL A 1 124 ? 21.866 26.775 11.921 1.00 5.01 ? 204 VAL A N 1 ATOM 928 C CA . VAL A 1 124 ? 20.772 27.706 11.694 1.00 5.40 ? 204 VAL A CA 1 ATOM 929 C C . VAL A 1 124 ? 20.622 28.608 12.912 1.00 5.56 ? 204 VAL A C 1 ATOM 930 O O . VAL A 1 124 ? 20.406 28.127 14.021 1.00 5.07 ? 204 VAL A O 1 ATOM 931 C CB . VAL A 1 124 ? 19.449 26.963 11.424 1.00 3.63 ? 204 VAL A CB 1 ATOM 932 C CG1 . VAL A 1 124 ? 18.290 27.947 11.338 1.00 7.78 ? 204 VAL A CG1 1 ATOM 933 C CG2 . VAL A 1 124 ? 19.556 26.141 10.143 1.00 4.94 ? 204 VAL A CG2 1 ATOM 934 N N . LEU A 1 125 ? 20.758 29.914 12.703 1.00 4.41 ? 205 LEU A N 1 ATOM 935 C CA . LEU A 1 125 ? 20.612 30.879 13.787 1.00 5.51 ? 205 LEU A CA 1 ATOM 936 C C . LEU A 1 125 ? 19.213 31.479 13.796 1.00 6.92 ? 205 LEU A C 1 ATOM 937 O O . LEU A 1 125 ? 18.714 31.930 12.764 1.00 6.46 ? 205 LEU A O 1 ATOM 938 C CB . LEU A 1 125 ? 21.656 31.995 13.674 1.00 6.22 ? 205 LEU A CB 1 ATOM 939 C CG . LEU A 1 125 ? 23.109 31.640 14.006 1.00 7.28 ? 205 LEU A CG 1 ATOM 940 C CD1 . LEU A 1 125 ? 23.697 30.698 12.967 1.00 11.00 ? 205 LEU A CD1 1 ATOM 941 C CD2 . LEU A 1 125 ? 23.958 32.901 14.121 1.00 9.18 ? 205 LEU A CD2 1 ATOM 942 N N . LYS A 1 126 ? 18.583 31.478 14.966 1.00 5.50 ? 206 LYS A N 1 ATOM 943 C CA . LYS A 1 126 ? 17.268 32.083 15.132 1.00 5.14 ? 206 LYS A CA 1 ATOM 944 C C . LYS A 1 126 ? 17.308 33.172 16.195 1.00 5.18 ? 206 LYS A C 1 ATOM 945 O O . LYS A 1 126 ? 17.957 33.021 17.229 1.00 5.37 ? 206 LYS A O 1 ATOM 946 C CB . LYS A 1 126 ? 16.223 31.033 15.518 1.00 5.64 ? 206 LYS A CB 1 ATOM 947 C CG . LYS A 1 126 ? 15.899 30.023 14.431 1.00 8.10 ? 206 LYS A CG 1 ATOM 948 C CD . LYS A 1 126 ? 14.884 29.008 14.939 1.00 10.39 ? 206 LYS A CD 1 ATOM 949 C CE . LYS A 1 126 ? 14.543 27.975 13.878 1.00 9.20 ? 206 LYS A CE 1 ATOM 950 N NZ . LYS A 1 126 ? 13.504 27.020 14.360 1.00 9.88 ? 206 LYS A NZ 1 ATOM 951 N N . TYR A 1 127 ? 16.615 34.271 15.926 1.00 5.33 ? 207 TYR A N 1 ATOM 952 C CA . TYR A 1 127 ? 16.472 35.347 16.893 1.00 3.56 ? 207 TYR A CA 1 ATOM 953 C C . TYR A 1 127 ? 14.982 35.564 17.100 1.00 6.07 ? 207 TYR A C 1 ATOM 954 O O . TYR A 1 127 ? 14.263 35.888 16.159 1.00 6.18 ? 207 TYR A O 1 ATOM 955 C CB . TYR A 1 127 ? 17.140 36.621 16.375 1.00 5.16 ? 207 TYR A CB 1 ATOM 956 C CG . TYR A 1 127 ? 17.279 37.722 17.404 1.00 8.24 ? 207 TYR A CG 1 ATOM 957 C CD1 . TYR A 1 127 ? 18.129 37.577 18.496 1.00 9.83 ? 207 TYR A CD1 1 ATOM 958 C CD2 . TYR A 1 127 ? 16.579 38.915 17.275 1.00 10.08 ? 207 TYR A CD2 1 ATOM 959 C CE1 . TYR A 1 127 ? 18.263 38.583 19.439 1.00 7.48 ? 207 TYR A CE1 1 ATOM 960 C CE2 . TYR A 1 127 ? 16.712 39.929 18.212 1.00 9.28 ? 207 TYR A CE2 1 ATOM 961 C CZ . TYR A 1 127 ? 17.556 39.757 19.288 1.00 8.30 ? 207 TYR A CZ 1 ATOM 962 O OH . TYR A 1 127 ? 17.692 40.761 20.221 1.00 9.48 ? 207 TYR A OH 1 ATOM 963 N N . ASN A 1 128 ? 14.523 35.364 18.331 1.00 5.46 ? 208 ASN A N 1 ATOM 964 C CA . ASN A 1 128 ? 13.095 35.378 18.632 1.00 8.89 ? 208 ASN A CA 1 ATOM 965 C C . ASN A 1 128 ? 12.328 34.369 17.778 1.00 6.28 ? 208 ASN A C 1 ATOM 966 O O . ASN A 1 128 ? 11.206 34.629 17.347 1.00 8.25 ? 208 ASN A O 1 ATOM 967 C CB . ASN A 1 128 ? 12.508 36.782 18.459 1.00 11.03 ? 208 ASN A CB 1 ATOM 968 C CG . ASN A 1 128 ? 11.130 36.917 19.082 1.00 16.29 ? 208 ASN A CG 1 ATOM 969 O OD1 . ASN A 1 128 ? 10.769 36.163 19.984 1.00 13.07 ? 208 ASN A OD1 1 ATOM 970 N ND2 . ASN A 1 128 ? 10.355 37.884 18.604 1.00 20.84 ? 208 ASN A ND2 1 ATOM 971 N N . GLY A 1 129 ? 12.948 33.220 17.525 1.00 9.45 ? 209 GLY A N 1 ATOM 972 C CA . GLY A 1 129 ? 12.292 32.140 16.808 1.00 12.41 ? 209 GLY A CA 1 ATOM 973 C C . GLY A 1 129 ? 12.233 32.298 15.298 1.00 12.15 ? 209 GLY A C 1 ATOM 974 O O . GLY A 1 129 ? 11.632 31.473 14.611 1.00 12.67 ? 209 GLY A O 1 ATOM 975 N N . ILE A 1 130 ? 12.848 33.357 14.782 1.00 4.18 ? 210 ILE A N 1 ATOM 976 C CA . ILE A 1 130 ? 12.881 33.609 13.341 1.00 5.97 ? 210 ILE A CA 1 ATOM 977 C C . ILE A 1 130 ? 14.290 33.373 12.801 1.00 6.45 ? 210 ILE A C 1 ATOM 978 O O . ILE A 1 130 ? 15.262 33.855 13.377 1.00 6.29 ? 210 ILE A O 1 ATOM 979 C CB . ILE A 1 130 ? 12.473 35.064 13.020 1.00 10.55 ? 210 ILE A CB 1 ATOM 980 C CG1 . ILE A 1 130 ? 11.070 35.369 13.562 1.00 10.55 ? 210 ILE A CG1 1 ATOM 981 C CG2 . ILE A 1 130 ? 12.562 35.336 11.520 1.00 7.98 ? 210 ILE A CG2 1 ATOM 982 C CD1 . ILE A 1 130 ? 9.963 34.539 12.928 1.00 10.45 ? 210 ILE A CD1 1 ATOM 983 N N . ILE A 1 131 ? 14.411 32.637 11.699 1.00 6.05 ? 211 ILE A N 1 ATOM 984 C CA . ILE A 1 131 ? 15.735 32.396 11.122 1.00 7.61 ? 211 ILE A CA 1 ATOM 985 C C . ILE A 1 131 ? 16.384 33.703 10.671 1.00 7.07 ? 211 ILE A C 1 ATOM 986 O O . ILE A 1 131 ? 15.791 34.481 9.922 1.00 10.15 ? 211 ILE A O 1 ATOM 987 C CB . ILE A 1 131 ? 15.695 31.407 9.946 1.00 7.86 ? 211 ILE A CB 1 ATOM 988 C CG1 . ILE A 1 131 ? 15.255 30.024 10.427 1.00 3.08 ? 211 ILE A CG1 1 ATOM 989 C CG2 . ILE A 1 131 ? 17.068 31.314 9.284 1.00 6.45 ? 211 ILE A CG2 1 ATOM 990 C CD1 . ILE A 1 131 ? 15.229 28.979 9.324 1.00 9.18 ? 211 ILE A CD1 1 ATOM 991 N N . THR A 1 132 ? 17.608 33.938 11.128 1.00 6.12 ? 212 THR A N 1 ATOM 992 C CA . THR A 1 132 ? 18.280 35.203 10.859 1.00 8.06 ? 212 THR A CA 1 ATOM 993 C C . THR A 1 132 ? 19.610 35.020 10.135 1.00 10.73 ? 212 THR A C 1 ATOM 994 O O . THR A 1 132 ? 20.142 35.964 9.560 1.00 10.89 ? 212 THR A O 1 ATOM 995 C CB . THR A 1 132 ? 18.515 35.997 12.158 1.00 7.05 ? 212 THR A CB 1 ATOM 996 O OG1 . THR A 1 132 ? 19.022 35.118 13.170 1.00 6.79 ? 212 THR A OG1 1 ATOM 997 C CG2 . THR A 1 132 ? 17.212 36.620 12.645 1.00 9.57 ? 212 THR A CG2 1 ATOM 998 N N . ASP A 1 133 ? 20.147 33.808 10.162 1.00 8.87 ? 213 ASP A N 1 ATOM 999 C CA . ASP A 1 133 ? 21.436 33.560 9.534 1.00 7.77 ? 213 ASP A CA 1 ATOM 1000 C C . ASP A 1 133 ? 21.752 32.077 9.523 1.00 8.72 ? 213 ASP A C 1 ATOM 1001 O O . ASP A 1 133 ? 21.117 31.289 10.224 1.00 6.66 ? 213 ASP A O 1 ATOM 1002 C CB . ASP A 1 133 ? 22.541 34.314 10.279 1.00 10.05 ? 213 ASP A CB 1 ATOM 1003 C CG . ASP A 1 133 ? 23.640 34.810 9.356 1.00 13.21 ? 213 ASP A CG 1 ATOM 1004 O OD1 . ASP A 1 133 ? 23.703 34.358 8.191 1.00 12.80 ? 213 ASP A OD1 1 ATOM 1005 O OD2 . ASP A 1 133 ? 24.442 35.660 9.799 1.00 14.91 ? 213 ASP A OD2 1 ATOM 1006 N N . THR A 1 134 ? 22.733 31.701 8.713 1.00 6.63 ? 214 THR A N 1 ATOM 1007 C CA . THR A 1 134 ? 23.250 30.345 8.720 1.00 8.57 ? 214 THR A CA 1 ATOM 1008 C C . THR A 1 134 ? 24.762 30.393 8.563 1.00 9.74 ? 214 THR A C 1 ATOM 1009 O O . THR A 1 134 ? 25.318 31.386 8.094 1.00 12.33 ? 214 THR A O 1 ATOM 1010 C CB . THR A 1 134 ? 22.659 29.491 7.577 1.00 10.40 ? 214 THR A CB 1 ATOM 1011 O OG1 . THR A 1 134 ? 23.061 30.031 6.313 1.00 10.13 ? 214 THR A OG1 1 ATOM 1012 C CG2 . THR A 1 134 ? 21.135 29.454 7.653 1.00 8.57 ? 214 THR A CG2 1 ATOM 1013 N N . ILE A 1 135 ? 25.427 29.320 8.965 1.00 7.67 ? 215 ILE A N 1 ATOM 1014 C CA . ILE A 1 135 ? 26.852 29.182 8.710 1.00 10.87 ? 215 ILE A CA 1 ATOM 1015 C C . ILE A 1 135 ? 27.149 27.719 8.415 1.00 10.67 ? 215 ILE A C 1 ATOM 1016 O O . ILE A 1 135 ? 26.742 26.829 9.160 1.00 11.33 ? 215 ILE A O 1 ATOM 1017 C CB . ILE A 1 135 ? 27.705 29.726 9.882 1.00 15.22 ? 215 ILE A CB 1 ATOM 1018 C CG1 . ILE A 1 135 ? 29.201 29.609 9.570 1.00 16.47 ? 215 ILE A CG1 1 ATOM 1019 C CG2 . ILE A 1 135 ? 27.370 29.006 11.174 1.00 14.22 ? 215 ILE A CG2 1 ATOM 1020 C CD1 . ILE A 1 135 ? 29.817 28.293 9.997 1.00 16.51 ? 215 ILE A CD1 1 ATOM 1021 N N . LYS A 1 136 ? 27.838 27.472 7.307 1.00 8.92 ? 216 LYS A N 1 ATOM 1022 C CA . LYS A 1 136 ? 28.073 26.107 6.860 1.00 9.72 ? 216 LYS A CA 1 ATOM 1023 C C . LYS A 1 136 ? 29.474 25.621 7.212 1.00 7.72 ? 216 LYS A C 1 ATOM 1024 O O . LYS A 1 136 ? 30.416 26.410 7.298 1.00 9.58 ? 216 LYS A O 1 ATOM 1025 C CB . LYS A 1 136 ? 27.828 25.987 5.354 1.00 12.68 ? 216 LYS A CB 1 ATOM 1026 C CG . LYS A 1 136 ? 27.860 24.561 4.834 1.00 9.40 ? 216 LYS A CG 1 ATOM 1027 C CD . LYS A 1 136 ? 27.310 24.478 3.421 1.00 13.09 ? 216 LYS A CD 1 ATOM 1028 C CE . LYS A 1 136 ? 27.207 23.033 2.958 1.00 15.81 ? 216 LYS A CE 1 ATOM 1029 N NZ . LYS A 1 136 ? 26.596 22.939 1.602 1.00 24.78 ? 216 LYS A NZ 1 ATOM 1030 N N . SER A 1 137 ? 29.587 24.315 7.428 1.00 9.20 ? 217 SER A N 1 ATOM 1031 C CA . SER A 1 137 ? 30.859 23.656 7.690 1.00 7.32 ? 217 SER A CA 1 ATOM 1032 C C . SER A 1 137 ? 31.928 24.161 6.726 1.00 12.11 ? 217 SER A C 1 ATOM 1033 O O . SER A 1 137 ? 31.692 24.240 5.519 1.00 8.37 ? 217 SER A O 1 ATOM 1034 C CB . SER A 1 137 ? 30.679 22.143 7.538 1.00 7.34 ? 217 SER A CB 1 ATOM 1035 O OG . SER A 1 137 ? 31.882 21.435 7.765 1.00 8.32 ? 217 SER A OG 1 ATOM 1036 N N . TRP A 1 138 ? 33.095 24.516 7.260 1.00 7.61 ? 218 TRP A N 1 ATOM 1037 C CA . TRP A 1 138 ? 34.196 25.000 6.429 1.00 9.18 ? 218 TRP A CA 1 ATOM 1038 C C . TRP A 1 138 ? 35.327 23.977 6.306 1.00 10.15 ? 218 TRP A C 1 ATOM 1039 O O . TRP A 1 138 ? 36.250 24.158 5.513 1.00 12.62 ? 218 TRP A O 1 ATOM 1040 C CB . TRP A 1 138 ? 34.736 26.338 6.952 1.00 9.16 ? 218 TRP A CB 1 ATOM 1041 C CG . TRP A 1 138 ? 35.364 26.252 8.311 1.00 10.52 ? 218 TRP A CG 1 ATOM 1042 C CD1 . TRP A 1 138 ? 36.678 26.021 8.593 1.00 8.88 ? 218 TRP A CD1 1 ATOM 1043 C CD2 . TRP A 1 138 ? 34.703 26.398 9.573 1.00 10.07 ? 218 TRP A CD2 1 ATOM 1044 N NE1 . TRP A 1 138 ? 36.878 26.012 9.952 1.00 11.17 ? 218 TRP A NE1 1 ATOM 1045 C CE2 . TRP A 1 138 ? 35.680 26.242 10.577 1.00 10.17 ? 218 TRP A CE2 1 ATOM 1046 C CE3 . TRP A 1 138 ? 33.380 26.644 9.952 1.00 11.26 ? 218 TRP A CE3 1 ATOM 1047 C CZ2 . TRP A 1 138 ? 35.377 26.322 11.934 1.00 11.34 ? 218 TRP A CZ2 1 ATOM 1048 C CZ3 . TRP A 1 138 ? 33.081 26.727 11.302 1.00 11.00 ? 218 TRP A CZ3 1 ATOM 1049 C CH2 . TRP A 1 138 ? 34.074 26.565 12.275 1.00 7.83 ? 218 TRP A CH2 1 ATOM 1050 N N . ARG A 1 139 ? 35.249 22.905 7.089 1.00 10.00 ? 219 ARG A N 1 ATOM 1051 C CA . ARG A 1 139 ? 36.210 21.808 6.990 1.00 12.19 ? 219 ARG A CA 1 ATOM 1052 C C . ARG A 1 139 ? 35.539 20.495 6.587 1.00 11.08 ? 219 ARG A C 1 ATOM 1053 O O . ARG A 1 139 ? 36.203 19.467 6.451 1.00 12.20 ? 219 ARG A O 1 ATOM 1054 C CB . ARG A 1 139 ? 36.962 21.620 8.310 1.00 9.28 ? 219 ARG A CB 1 ATOM 1055 C CG . ARG A 1 139 ? 37.917 22.751 8.651 1.00 12.46 ? 219 ARG A CG 1 ATOM 1056 C CD . ARG A 1 139 ? 39.062 22.833 7.651 1.00 23.12 ? 219 ARG A CD 1 ATOM 1057 N NE . ARG A 1 139 ? 40.027 23.866 8.017 1.00 22.40 ? 219 ARG A NE 1 ATOM 1058 C CZ . ARG A 1 139 ? 41.131 23.643 8.724 1.00 28.79 ? 219 ARG A CZ 1 ATOM 1059 N NH1 . ARG A 1 139 ? 41.417 22.417 9.142 1.00 30.49 ? 219 ARG A NH1 1 ATOM 1060 N NH2 . ARG A 1 139 ? 41.951 24.646 9.011 1.00 28.48 ? 219 ARG A NH2 1 ATOM 1061 N N . ASN A 1 140 ? 34.223 20.530 6.406 1.00 10.88 ? 220 ASN A N 1 ATOM 1062 C CA . ASN A 1 140 ? 33.477 19.348 5.979 1.00 13.54 ? 220 ASN A CA 1 ATOM 1063 C C . ASN A 1 140 ? 33.680 18.148 6.899 1.00 12.29 ? 220 ASN A C 1 ATOM 1064 O O . ASN A 1 140 ? 33.716 17.004 6.442 1.00 10.94 ? 220 ASN A O 1 ATOM 1065 C CB . ASN A 1 140 ? 33.855 18.967 4.544 1.00 12.91 ? 220 ASN A CB 1 ATOM 1066 C CG . ASN A 1 140 ? 33.572 20.077 3.551 1.00 19.34 ? 220 ASN A CG 1 ATOM 1067 O OD1 . ASN A 1 140 ? 32.885 21.048 3.864 1.00 20.02 ? 220 ASN A OD1 1 ATOM 1068 N ND2 . ASN A 1 140 ? 34.102 19.935 2.341 1.00 29.66 ? 220 ASN A ND2 1 ATOM 1069 N N . ASN A 1 141 ? 33.810 18.409 8.195 1.00 10.77 ? 221 ASN A N 1 ATOM 1070 C CA . ASN A 1 141 ? 34.028 17.340 9.163 1.00 8.50 ? 221 ASN A CA 1 ATOM 1071 C C . ASN A 1 141 ? 33.329 17.613 10.494 1.00 10.28 ? 221 ASN A C 1 ATOM 1072 O O . ASN A 1 141 ? 33.972 17.929 11.495 1.00 8.84 ? 221 ASN A O 1 ATOM 1073 C CB . ASN A 1 141 ? 35.527 17.108 9.377 1.00 11.98 ? 221 ASN A CB 1 ATOM 1074 C CG . ASN A 1 141 ? 35.823 15.808 10.110 1.00 17.94 ? 221 ASN A CG 1 ATOM 1075 O OD1 . ASN A 1 141 ? 34.913 15.065 10.479 1.00 14.40 ? 221 ASN A OD1 1 ATOM 1076 N ND2 . ASN A 1 141 ? 37.105 15.530 10.322 1.00 16.64 ? 221 ASN A ND2 1 ATOM 1077 N N . ILE A 1 142 ? 32.005 17.493 10.484 1.00 10.28 ? 222 ILE A N 1 ATOM 1078 C CA . ILE A 1 142 ? 31.186 17.625 11.688 1.00 8.00 ? 222 ILE A CA 1 ATOM 1079 C C . ILE A 1 142 ? 31.319 18.980 12.383 1.00 8.64 ? 222 ILE A C 1 ATOM 1080 O O . ILE A 1 142 ? 31.900 19.080 13.464 1.00 9.70 ? 222 ILE A O 1 ATOM 1081 C CB . ILE A 1 142 ? 31.476 16.502 12.705 1.00 7.96 ? 222 ILE A CB 1 ATOM 1082 C CG1 . ILE A 1 142 ? 31.496 15.142 12.005 1.00 13.42 ? 222 ILE A CG1 1 ATOM 1083 C CG2 . ILE A 1 142 ? 30.434 16.514 13.820 1.00 9.85 ? 222 ILE A CG2 1 ATOM 1084 C CD1 . ILE A 1 142 ? 31.771 13.977 12.934 1.00 14.08 ? 222 ILE A CD1 1 ATOM 1085 N N . LEU A 1 143 ? 30.774 20.017 11.757 1.00 6.64 ? 223 LEU A N 1 ATOM 1086 C CA . LEU A 1 143 ? 30.646 21.316 12.404 1.00 8.07 ? 223 LEU A CA 1 ATOM 1087 C C . LEU A 1 143 ? 29.902 21.133 13.721 1.00 6.92 ? 223 LEU A C 1 ATOM 1088 O O . LEU A 1 143 ? 28.851 20.497 13.757 1.00 6.20 ? 223 LEU A O 1 ATOM 1089 C CB . LEU A 1 143 ? 29.877 22.283 11.504 1.00 7.56 ? 223 LEU A CB 1 ATOM 1090 C CG . LEU A 1 143 ? 29.577 23.668 12.080 1.00 9.21 ? 223 LEU A CG 1 ATOM 1091 C CD1 . LEU A 1 143 ? 30.866 24.437 12.336 1.00 5.33 ? 223 LEU A CD1 1 ATOM 1092 C CD2 . LEU A 1 143 ? 28.664 24.444 11.141 1.00 9.02 ? 223 LEU A CD2 1 ATOM 1093 N N . ARG A 1 144 ? 30.446 21.685 14.801 1.00 4.80 ? 224 ARG A N 1 ATOM 1094 C CA . ARG A 1 144 ? 29.872 21.469 16.128 1.00 8.47 ? 224 ARG A CA 1 ATOM 1095 C C . ARG A 1 144 ? 30.127 22.645 17.068 1.00 6.90 ? 224 ARG A C 1 ATOM 1096 O O . ARG A 1 144 ? 31.065 23.415 16.867 1.00 7.08 ? 224 ARG A O 1 ATOM 1097 C CB . ARG A 1 144 ? 30.398 20.160 16.729 1.00 9.65 ? 224 ARG A CB 1 ATOM 1098 C CG . ARG A 1 144 ? 31.918 20.006 16.693 1.00 7.08 ? 224 ARG A CG 1 ATOM 1099 C CD . ARG A 1 144 ? 32.320 18.542 16.848 1.00 8.15 ? 224 ARG A CD 1 ATOM 1100 N NE . ARG A 1 144 ? 33.757 18.369 17.057 1.00 7.49 ? 224 ARG A NE 1 ATOM 1101 C CZ . ARG A 1 144 ? 34.650 18.261 16.078 1.00 11.86 ? 224 ARG A CZ 1 ATOM 1102 N NH1 . ARG A 1 144 ? 34.261 18.314 14.809 1.00 8.24 ? 224 ARG A NH1 1 ATOM 1103 N NH2 . ARG A 1 144 ? 35.935 18.105 16.367 1.00 10.20 ? 224 ARG A NH2 1 ATOM 1104 N N . THR A 1 145 ? 29.288 22.787 18.090 1.00 7.97 ? 225 THR A N 1 ATOM 1105 C CA . THR A 1 145 ? 29.369 23.952 18.968 1.00 5.16 ? 225 THR A CA 1 ATOM 1106 C C . THR A 1 145 ? 29.312 23.605 20.466 1.00 6.49 ? 225 THR A C 1 ATOM 1107 O O . THR A 1 145 ? 29.617 22.479 20.861 1.00 6.39 ? 225 THR A O 1 ATOM 1108 C CB . THR A 1 145 ? 28.323 25.034 18.572 1.00 5.39 ? 225 THR A CB 1 ATOM 1109 O OG1 . THR A 1 145 ? 28.565 26.247 19.300 1.00 8.39 ? 225 THR A OG1 1 ATOM 1110 C CG2 . THR A 1 145 ? 26.897 24.547 18.814 1.00 6.17 ? 225 THR A CG2 1 ATOM 1111 N N . GLN A 1 146 ? 28.923 24.576 21.288 1.00 6.99 ? 226 GLN A N 1 ATOM 1112 C CA . GLN A 1 146 ? 29.124 24.509 22.741 1.00 7.18 ? 226 GLN A CA 1 ATOM 1113 C C . GLN A 1 146 ? 28.391 23.398 23.493 1.00 7.28 ? 226 GLN A C 1 ATOM 1114 O O . GLN A 1 146 ? 28.956 22.772 24.391 1.00 6.97 ? 226 GLN A O 1 ATOM 1115 C CB . GLN A 1 146 ? 28.736 25.841 23.381 1.00 6.79 ? 226 GLN A CB 1 ATOM 1116 C CG . GLN A 1 146 ? 29.559 27.032 22.946 1.00 6.12 ? 226 GLN A CG 1 ATOM 1117 C CD . GLN A 1 146 ? 29.128 28.297 23.660 1.00 9.66 ? 226 GLN A CD 1 ATOM 1118 O OE1 . GLN A 1 146 ? 28.607 29.227 23.044 1.00 14.62 ? 226 GLN A OE1 1 ATOM 1119 N NE2 . GLN A 1 146 ? 29.322 28.329 24.973 1.00 7.63 ? 226 GLN A NE2 1 ATOM 1120 N N . GLU A 1 147 ? 27.128 23.179 23.148 1.00 6.65 ? 227 GLU A N 1 ATOM 1121 C CA . GLU A 1 147 ? 26.230 22.365 23.968 1.00 6.04 ? 227 GLU A CA 1 ATOM 1122 C C . GLU A 1 147 ? 26.022 23.016 25.339 1.00 8.93 ? 227 GLU A C 1 ATOM 1123 O O . GLU A 1 147 ? 25.672 22.347 26.314 1.00 9.87 ? 227 GLU A O 1 ATOM 1124 C CB . GLU A 1 147 ? 26.740 20.927 24.128 1.00 12.18 ? 227 GLU A CB 1 ATOM 1125 C CG . GLU A 1 147 ? 27.488 20.359 22.926 1.00 11.72 ? 227 GLU A CG 1 ATOM 1126 C CD . GLU A 1 147 ? 26.647 20.283 21.663 1.00 15.45 ? 227 GLU A CD 1 ATOM 1127 O OE1 . GLU A 1 147 ? 25.464 20.683 21.693 1.00 13.26 ? 227 GLU A OE1 1 ATOM 1128 O OE2 . GLU A 1 147 ? 27.179 19.817 20.633 1.00 16.28 ? 227 GLU A OE2 1 ATOM 1129 N N . SER A 1 148 ? 26.264 24.322 25.408 1.00 7.15 ? 228 SER A N 1 ATOM 1130 C CA . SER A 1 148 ? 25.857 25.130 26.557 1.00 8.37 ? 228 SER A CA 1 ATOM 1131 C C . SER A 1 148 ? 25.572 26.552 26.085 1.00 8.34 ? 228 SER A C 1 ATOM 1132 O O . SER A 1 148 ? 25.615 26.830 24.886 1.00 10.50 ? 228 SER A O 1 ATOM 1133 C CB . SER A 1 148 ? 26.894 25.097 27.689 1.00 10.43 ? 228 SER A CB 1 ATOM 1134 O OG . SER A 1 148 ? 28.168 25.545 27.265 1.00 10.10 ? 228 SER A OG 1 ATOM 1135 N N . GLU A 1 149 ? 25.276 27.451 27.016 1.00 6.20 ? 229 GLU A N 1 ATOM 1136 C CA . GLU A 1 149 ? 24.832 28.791 26.646 1.00 6.64 ? 229 GLU A CA 1 ATOM 1137 C C . GLU A 1 149 ? 25.944 29.639 26.037 1.00 6.92 ? 229 GLU A C 1 ATOM 1138 O O . GLU A 1 149 ? 27.097 29.569 26.467 1.00 8.47 ? 229 GLU A O 1 ATOM 1139 C CB . GLU A 1 149 ? 24.233 29.518 27.851 1.00 5.86 ? 229 GLU A CB 1 ATOM 1140 C CG . GLU A 1 149 ? 25.262 30.029 28.851 1.00 8.46 ? 229 GLU A CG 1 ATOM 1141 C CD . GLU A 1 149 ? 24.661 30.970 29.876 1.00 13.92 ? 229 GLU A CD 1 ATOM 1142 O OE1 . GLU A 1 149 ? 23.446 31.246 29.790 1.00 10.82 ? 229 GLU A OE1 1 ATOM 1143 O OE2 . GLU A 1 149 ? 25.401 31.440 30.767 1.00 10.10 ? 229 GLU A OE2 1 ATOM 1144 N N . CYS A 1 150 ? 25.591 30.434 25.030 1.00 7.34 ? 230 CYS A N 1 ATOM 1145 C CA . CYS A 1 150 ? 26.501 31.454 24.525 1.00 10.40 ? 230 CYS A CA 1 ATOM 1146 C C . CYS A 1 150 ? 26.563 32.604 25.533 1.00 12.20 ? 230 CYS A C 1 ATOM 1147 O O . CYS A 1 150 ? 25.806 32.625 26.506 1.00 10.17 ? 230 CYS A O 1 ATOM 1148 C CB . CYS A 1 150 ? 26.091 31.940 23.124 1.00 10.14 ? 230 CYS A CB 1 ATOM 1149 S SG . CYS A 1 150 ? 24.315 31.864 22.704 1.00 13.35 ? 230 CYS A SG 1 ATOM 1150 N N . ALA A 1 151 ? 27.471 33.548 25.314 1.00 8.06 ? 231 ALA A N 1 ATOM 1151 C CA . ALA A 1 151 ? 27.662 34.641 26.262 1.00 8.47 ? 231 ALA A CA 1 ATOM 1152 C C . ALA A 1 151 ? 27.359 35.986 25.612 1.00 9.46 ? 231 ALA A C 1 ATOM 1153 O O . ALA A 1 151 ? 27.760 36.235 24.479 1.00 5.50 ? 231 ALA A O 1 ATOM 1154 C CB . ALA A 1 151 ? 29.076 34.619 26.813 1.00 11.32 ? 231 ALA A CB 1 ATOM 1155 N N . CYS A 1 152 ? 26.651 36.850 26.336 1.00 9.51 ? 232 CYS A N 1 ATOM 1156 C CA . CYS A 1 152 ? 26.203 38.122 25.778 1.00 8.42 ? 232 CYS A CA 1 ATOM 1157 C C . CYS A 1 152 ? 26.769 39.330 26.521 1.00 10.10 ? 232 CYS A C 1 ATOM 1158 O O . CYS A 1 152 ? 26.832 39.351 27.751 1.00 12.23 ? 232 CYS A O 1 ATOM 1159 C CB . CYS A 1 152 ? 24.674 38.190 25.747 1.00 11.89 ? 232 CYS A CB 1 ATOM 1160 S SG . CYS A 1 152 ? 23.889 36.946 24.697 1.00 19.03 ? 232 CYS A SG 1 ATOM 1161 N N . VAL A 1 153 ? 27.179 40.332 25.750 1.00 7.01 ? 233 VAL A N 1 ATOM 1162 C CA . VAL A 1 153 ? 27.685 41.586 26.286 1.00 10.82 ? 233 VAL A CA 1 ATOM 1163 C C . VAL A 1 153 ? 27.209 42.738 25.413 1.00 13.63 ? 233 VAL A C 1 ATOM 1164 O O . VAL A 1 153 ? 27.512 42.788 24.222 1.00 7.49 ? 233 VAL A O 1 ATOM 1165 C CB . VAL A 1 153 ? 29.226 41.614 26.326 1.00 13.65 ? 233 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 153 ? 29.715 43.006 26.706 1.00 11.13 ? 233 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 153 ? 29.763 40.572 27.294 1.00 9.35 ? 233 VAL A CG2 1 ATOM 1168 N N . ASN A 1 154 ? 26.450 43.649 26.012 1.00 8.18 ? 234 ASN A N 1 ATOM 1169 C CA . ASN A 1 154 ? 25.968 44.851 25.334 1.00 12.60 ? 234 ASN A CA 1 ATOM 1170 C C . ASN A 1 154 ? 25.392 44.639 23.933 1.00 9.79 ? 234 ASN A C 1 ATOM 1171 O O . ASN A 1 154 ? 25.777 45.326 22.988 1.00 8.90 ? 234 ASN A O 1 ATOM 1172 C CB . ASN A 1 154 ? 27.065 45.916 25.282 1.00 12.91 ? 234 ASN A CB 1 ATOM 1173 C CG . ASN A 1 154 ? 26.519 47.292 24.967 1.00 12.77 ? 234 ASN A CG 1 ATOM 1174 O OD1 . ASN A 1 154 ? 25.415 47.642 25.382 1.00 25.99 ? 234 ASN A OD1 1 ATOM 1175 N ND2 . ASN A 1 154 ? 27.285 48.078 24.225 1.00 16.90 ? 234 ASN A ND2 1 ATOM 1176 N N . GLY A 1 155 ? 24.468 43.695 23.802 1.00 9.58 ? 235 GLY A N 1 ATOM 1177 C CA . GLY A 1 155 ? 23.767 43.498 22.545 1.00 13.30 ? 235 GLY A CA 1 ATOM 1178 C C . GLY A 1 155 ? 24.455 42.563 21.569 1.00 13.51 ? 235 GLY A C 1 ATOM 1179 O O . GLY A 1 155 ? 23.914 42.260 20.504 1.00 13.73 ? 235 GLY A O 1 ATOM 1180 N N . SER A 1 156 ? 25.656 42.115 21.916 1.00 7.11 ? 236 SER A N 1 ATOM 1181 C CA . SER A 1 156 ? 26.351 41.128 21.102 1.00 9.70 ? 236 SER A CA 1 ATOM 1182 C C . SER A 1 156 ? 26.486 39.826 21.873 1.00 12.32 ? 236 SER A C 1 ATOM 1183 O O . SER A 1 156 ? 26.784 39.833 23.066 1.00 8.90 ? 236 SER A O 1 ATOM 1184 C CB . SER A 1 156 ? 27.734 41.636 20.687 1.00 12.47 ? 236 SER A CB 1 ATOM 1185 O OG . SER A 1 156 ? 27.638 42.827 19.927 1.00 16.39 ? 236 SER A OG 1 ATOM 1186 N N . CYS A 1 157 ? 26.260 38.711 21.187 1.00 8.22 ? 237 CYS A N 1 ATOM 1187 C CA . CYS A 1 157 ? 26.433 37.394 21.784 1.00 9.34 ? 237 CYS A CA 1 ATOM 1188 C C . CYS A 1 157 ? 27.564 36.648 21.082 1.00 7.14 ? 237 CYS A C 1 ATOM 1189 O O . CYS A 1 157 ? 27.776 36.811 19.885 1.00 9.56 ? 237 CYS A O 1 ATOM 1190 C CB . CYS A 1 157 ? 25.131 36.595 21.720 1.00 10.85 ? 237 CYS A CB 1 ATOM 1191 S SG . CYS A 1 157 ? 23.781 37.309 22.677 1.00 19.36 ? 237 CYS A SG 1 ATOM 1192 N N . PHE A 1 158 ? 28.284 35.827 21.836 1.00 6.11 ? 238 PHE A N 1 ATOM 1193 C CA . PHE A 1 158 ? 29.490 35.195 21.327 1.00 7.80 ? 238 PHE A CA 1 ATOM 1194 C C . PHE A 1 158 ? 29.453 33.689 21.531 1.00 7.83 ? 238 PHE A C 1 ATOM 1195 O O . PHE A 1 158 ? 28.932 33.199 22.533 1.00 8.89 ? 238 PHE A O 1 ATOM 1196 C CB . PHE A 1 158 ? 30.719 35.791 22.017 1.00 7.25 ? 238 PHE A CB 1 ATOM 1197 C CG . PHE A 1 158 ? 30.810 37.287 21.901 1.00 6.40 ? 238 PHE A CG 1 ATOM 1198 C CD1 . PHE A 1 158 ? 30.130 38.108 22.788 1.00 6.86 ? 238 PHE A CD1 1 ATOM 1199 C CD2 . PHE A 1 158 ? 31.576 37.872 20.904 1.00 5.92 ? 238 PHE A CD2 1 ATOM 1200 C CE1 . PHE A 1 158 ? 30.209 39.486 22.680 1.00 6.40 ? 238 PHE A CE1 1 ATOM 1201 C CE2 . PHE A 1 158 ? 31.662 39.248 20.791 1.00 8.60 ? 238 PHE A CE2 1 ATOM 1202 C CZ . PHE A 1 158 ? 30.979 40.057 21.679 1.00 7.35 ? 238 PHE A CZ 1 ATOM 1203 N N . THR A 1 159 ? 30.005 32.957 20.571 1.00 7.40 ? 239 THR A N 1 ATOM 1204 C CA . THR A 1 159 ? 30.082 31.507 20.674 1.00 6.95 ? 239 THR A CA 1 ATOM 1205 C C . THR A 1 159 ? 31.320 30.992 19.951 1.00 9.34 ? 239 THR A C 1 ATOM 1206 O O . THR A 1 159 ? 31.979 31.731 19.223 1.00 9.61 ? 239 THR A O 1 ATOM 1207 C CB . THR A 1 159 ? 28.824 30.827 20.098 1.00 12.54 ? 239 THR A CB 1 ATOM 1208 O OG1 . THR A 1 159 ? 28.829 29.435 20.439 1.00 12.28 ? 239 THR A OG1 1 ATOM 1209 C CG2 . THR A 1 159 ? 28.771 30.979 18.586 1.00 10.94 ? 239 THR A CG2 1 ATOM 1210 N N . VAL A 1 160 ? 31.638 29.722 20.170 1.00 11.00 ? 240 VAL A N 1 ATOM 1211 C CA . VAL A 1 160 ? 32.768 29.091 19.509 1.00 8.98 ? 240 VAL A CA 1 ATOM 1212 C C . VAL A 1 160 ? 32.301 27.820 18.808 1.00 8.97 ? 240 VAL A C 1 ATOM 1213 O O . VAL A 1 160 ? 31.471 27.080 19.336 1.00 7.54 ? 240 VAL A O 1 ATOM 1214 C CB . VAL A 1 160 ? 33.877 28.740 20.515 1.00 12.71 ? 240 VAL A CB 1 ATOM 1215 C CG1 . VAL A 1 160 ? 34.407 30.002 21.189 1.00 10.67 ? 240 VAL A CG1 1 ATOM 1216 C CG2 . VAL A 1 160 ? 33.342 27.787 21.550 1.00 18.63 ? 240 VAL A CG2 1 ATOM 1217 N N . MET A 1 161 ? 32.820 27.582 17.609 1.00 7.11 ? 241 MET A N 1 ATOM 1218 C CA . MET A 1 161 ? 32.489 26.373 16.867 1.00 5.98 ? 241 MET A CA 1 ATOM 1219 C C . MET A 1 161 ? 33.753 25.664 16.409 1.00 5.96 ? 241 MET A C 1 ATOM 1220 O O . MET A 1 161 ? 34.788 26.294 16.197 1.00 6.65 ? 241 MET A O 1 ATOM 1221 C CB . MET A 1 161 ? 31.615 26.690 15.651 1.00 5.86 ? 241 MET A CB 1 ATOM 1222 C CG . MET A 1 161 ? 30.301 27.368 15.975 1.00 7.15 ? 241 MET A CG 1 ATOM 1223 S SD . MET A 1 161 ? 29.181 27.363 14.560 1.00 14.49 ? 241 MET A SD 1 ATOM 1224 C CE . MET A 1 161 ? 27.867 28.412 15.176 1.00 23.22 ? 241 MET A CE 1 ATOM 1225 N N . THR A 1 162 ? 33.651 24.350 16.250 1.00 6.93 ? 242 THR A N 1 ATOM 1226 C CA . THR A 1 162 ? 34.773 23.530 15.819 1.00 6.85 ? 242 THR A CA 1 ATOM 1227 C C . THR A 1 162 ? 34.387 22.744 14.572 1.00 7.48 ? 242 THR A C 1 ATOM 1228 O O . THR A 1 162 ? 33.238 22.336 14.415 1.00 6.77 ? 242 THR A O 1 ATOM 1229 C CB . THR A 1 162 ? 35.195 22.548 16.928 1.00 6.50 ? 242 THR A CB 1 ATOM 1230 O OG1 . THR A 1 162 ? 35.546 23.283 18.107 1.00 8.06 ? 242 THR A OG1 1 ATOM 1231 C CG2 . THR A 1 162 ? 36.381 21.698 16.488 1.00 5.99 ? 242 THR A CG2 1 ATOM 1232 N N . ASP A 1 163 ? 35.353 22.548 13.684 1.00 6.86 ? 243 ASP A N 1 ATOM 1233 C CA . ASP A 1 163 ? 35.154 21.752 12.484 1.00 6.72 ? 243 ASP A CA 1 ATOM 1234 C C . ASP A 1 163 ? 36.464 21.024 12.212 1.00 7.17 ? 243 ASP A C 1 ATOM 1235 O O . ASP A 1 163 ? 37.526 21.644 12.187 1.00 6.95 ? 243 ASP A O 1 ATOM 1236 C CB . ASP A 1 163 ? 34.779 22.653 11.306 1.00 6.72 ? 243 ASP A CB 1 ATOM 1237 C CG . ASP A 1 163 ? 34.125 21.891 10.168 1.00 10.10 ? 243 ASP A CG 1 ATOM 1238 O OD1 . ASP A 1 163 ? 34.204 20.644 10.152 1.00 9.56 ? 243 ASP A OD1 1 ATOM 1239 O OD2 . ASP A 1 163 ? 33.531 22.544 9.284 1.00 9.01 ? 243 ASP A OD2 1 ATOM 1240 N N . GLY A 1 164 ? 36.391 19.709 12.037 1.00 8.19 ? 244 GLY A N 1 ATOM 1241 C CA . GLY A 1 164 ? 37.586 18.903 11.854 1.00 7.84 ? 244 GLY A CA 1 ATOM 1242 C C . GLY A 1 164 ? 37.628 17.705 12.785 1.00 9.46 ? 244 GLY A C 1 ATOM 1243 O O . GLY A 1 164 ? 36.660 17.431 13.492 1.00 10.83 ? 244 GLY A O 1 ATOM 1244 N N . PRO A 1 165 ? 38.758 16.982 12.789 1.00 11.17 ? 245 PRO A N 1 ATOM 1245 C CA . PRO A 1 165 ? 38.927 15.749 13.569 1.00 10.32 ? 245 PRO A CA 1 ATOM 1246 C C . PRO A 1 165 ? 38.700 15.951 15.065 1.00 10.70 ? 245 PRO A C 1 ATOM 1247 O O . PRO A 1 165 ? 38.991 17.023 15.597 1.00 7.81 ? 245 PRO A O 1 ATOM 1248 C CB . PRO A 1 165 ? 40.391 15.375 13.317 1.00 9.93 ? 245 PRO A CB 1 ATOM 1249 C CG . PRO A 1 165 ? 40.727 16.011 12.016 1.00 16.40 ? 245 PRO A CG 1 ATOM 1250 C CD . PRO A 1 165 ? 39.952 17.296 11.986 1.00 10.82 ? 245 PRO A CD 1 ATOM 1251 N N . SER A 1 166 ? 38.188 14.921 15.731 1.00 11.59 ? 246 SER A N 1 ATOM 1252 C CA . SER A 1 166 ? 38.031 14.946 17.180 1.00 12.07 ? 246 SER A CA 1 ATOM 1253 C C . SER A 1 166 ? 39.186 14.206 17.853 1.00 15.06 ? 246 SER A C 1 ATOM 1254 O O . SER A 1 166 ? 39.238 14.096 19.079 1.00 14.66 ? 246 SER A O 1 ATOM 1255 C CB . SER A 1 166 ? 36.694 14.325 17.589 1.00 15.78 ? 246 SER A CB 1 ATOM 1256 O OG . SER A 1 166 ? 36.588 12.990 17.125 1.00 18.73 ? 246 SER A OG 1 ATOM 1257 N N . ASN A 1 167 ? 40.110 13.702 17.039 1.00 11.26 ? 247 ASN A N 1 ATOM 1258 C CA . ASN A 1 167 ? 41.270 12.971 17.540 1.00 13.81 ? 247 ASN A CA 1 ATOM 1259 C C . ASN A 1 167 ? 42.574 13.519 16.972 1.00 17.22 ? 247 ASN A C 1 ATOM 1260 O O . ASN A 1 167 ? 43.562 12.796 16.839 1.00 14.42 ? 247 ASN A O 1 ATOM 1261 C CB . ASN A 1 167 ? 41.149 11.481 17.216 1.00 17.09 ? 247 ASN A CB 1 ATOM 1262 C CG . ASN A 1 167 ? 41.208 11.202 15.727 1.00 21.43 ? 247 ASN A CG 1 ATOM 1263 O OD1 . ASN A 1 167 ? 41.008 12.099 14.907 1.00 12.29 ? 247 ASN A OD1 1 ATOM 1264 N ND2 . ASN A 1 167 ? 41.485 9.953 15.368 1.00 19.96 ? 247 ASN A ND2 1 ATOM 1265 N N . GLY A 1 168 ? 42.567 14.803 16.631 1.00 9.72 ? 248 GLY A N 1 ATOM 1266 C CA . GLY A 1 168 ? 43.738 15.455 16.080 1.00 12.09 ? 248 GLY A CA 1 ATOM 1267 C C . GLY A 1 168 ? 43.491 16.937 15.900 1.00 10.17 ? 248 GLY A C 1 ATOM 1268 O O . GLY A 1 168 ? 42.462 17.457 16.332 1.00 9.20 ? 248 GLY A O 1 ATOM 1269 N N . GLN A 1 169 ? 44.432 17.621 15.259 1.00 11.47 ? 249 GLN A N 1 ATOM 1270 C CA . GLN A 1 169 ? 44.300 19.054 15.025 1.00 12.14 ? 249 GLN A CA 1 ATOM 1271 C C . GLN A 1 169 ? 43.015 19.372 14.266 1.00 11.38 ? 249 GLN A C 1 ATOM 1272 O O . GLN A 1 169 ? 42.732 18.771 13.230 1.00 11.04 ? 249 GLN A O 1 ATOM 1273 C CB . GLN A 1 169 ? 45.501 19.583 14.241 1.00 11.69 ? 249 GLN A CB 1 ATOM 1274 C CG . GLN A 1 169 ? 45.477 21.090 14.026 1.00 10.57 ? 249 GLN A CG 1 ATOM 1275 C CD . GLN A 1 169 ? 45.800 21.861 15.293 1.00 13.79 ? 249 GLN A CD 1 ATOM 1276 O OE1 . GLN A 1 169 ? 46.861 21.678 15.890 1.00 10.12 ? 249 GLN A OE1 1 ATOM 1277 N NE2 . GLN A 1 169 ? 44.885 22.731 15.710 1.00 10.16 ? 249 GLN A NE2 1 ATOM 1278 N N . ALA A 1 170 ? 42.243 20.320 14.785 1.00 8.85 ? 250 ALA A N 1 ATOM 1279 C CA . ALA A 1 170 ? 41.030 20.773 14.117 1.00 7.82 ? 250 ALA A CA 1 ATOM 1280 C C . ALA A 1 170 ? 41.042 22.290 13.948 1.00 11.31 ? 250 ALA A C 1 ATOM 1281 O O . ALA A 1 170 ? 42.052 22.945 14.212 1.00 10.47 ? 250 ALA A O 1 ATOM 1282 C CB . ALA A 1 170 ? 39.793 20.327 14.890 1.00 7.58 ? 250 ALA A CB 1 ATOM 1283 N N . SER A 1 171 ? 39.916 22.839 13.504 1.00 5.63 ? 251 SER A N 1 ATOM 1284 C CA . SER A 1 171 ? 39.789 24.271 13.267 1.00 6.97 ? 251 SER A CA 1 ATOM 1285 C C . SER A 1 171 ? 38.745 24.866 14.208 1.00 7.93 ? 251 SER A C 1 ATOM 1286 O O . SER A 1 171 ? 37.659 24.309 14.372 1.00 7.06 ? 251 SER A O 1 ATOM 1287 C CB . SER A 1 171 ? 39.404 24.534 11.807 1.00 9.84 ? 251 SER A CB 1 ATOM 1288 O OG . SER A 1 171 ? 39.233 25.919 11.559 1.00 11.82 ? 251 SER A OG 1 ATOM 1289 N N . TYR A 1 172 ? 39.081 25.996 14.825 1.00 7.10 ? 252 TYR A N 1 ATOM 1290 C CA . TYR A 1 172 ? 38.235 26.600 15.850 1.00 7.19 ? 252 TYR A CA 1 ATOM 1291 C C . TYR A 1 172 ? 37.971 28.064 15.522 1.00 7.88 ? 252 TYR A C 1 ATOM 1292 O O . TYR A 1 172 ? 38.903 28.821 15.262 1.00 8.52 ? 252 TYR A O 1 ATOM 1293 C CB . TYR A 1 172 ? 38.909 26.465 17.221 1.00 6.11 ? 252 TYR A CB 1 ATOM 1294 C CG . TYR A 1 172 ? 39.776 25.232 17.308 1.00 8.62 ? 252 TYR A CG 1 ATOM 1295 C CD1 . TYR A 1 172 ? 39.209 23.967 17.376 1.00 5.32 ? 252 TYR A CD1 1 ATOM 1296 C CD2 . TYR A 1 172 ? 41.161 25.329 17.291 1.00 8.95 ? 252 TYR A CD2 1 ATOM 1297 C CE1 . TYR A 1 172 ? 39.992 22.835 17.433 1.00 6.18 ? 252 TYR A CE1 1 ATOM 1298 C CE2 . TYR A 1 172 ? 41.955 24.199 17.351 1.00 6.84 ? 252 TYR A CE2 1 ATOM 1299 C CZ . TYR A 1 172 ? 41.364 22.955 17.421 1.00 7.82 ? 252 TYR A CZ 1 ATOM 1300 O OH . TYR A 1 172 ? 42.145 21.824 17.477 1.00 8.45 ? 252 TYR A OH 1 ATOM 1301 N N . LYS A 1 173 ? 36.700 28.458 15.524 1.00 4.98 ? 253 LYS A N 1 ATOM 1302 C CA . LYS A 1 173 ? 36.323 29.830 15.196 1.00 4.26 ? 253 LYS A CA 1 ATOM 1303 C C . LYS A 1 173 ? 35.459 30.476 16.273 1.00 8.89 ? 253 LYS A C 1 ATOM 1304 O O . LYS A 1 173 ? 34.606 29.823 16.871 1.00 5.21 ? 253 LYS A O 1 ATOM 1305 C CB . LYS A 1 173 ? 35.582 29.885 13.857 1.00 5.12 ? 253 LYS A CB 1 ATOM 1306 C CG . LYS A 1 173 ? 36.459 29.672 12.635 1.00 7.19 ? 253 LYS A CG 1 ATOM 1307 C CD . LYS A 1 173 ? 35.652 29.864 11.358 1.00 10.94 ? 253 LYS A CD 1 ATOM 1308 C CE . LYS A 1 173 ? 36.511 29.679 10.117 1.00 17.16 ? 253 LYS A CE 1 ATOM 1309 N NZ . LYS A 1 173 ? 35.732 29.929 8.872 1.00 18.96 ? 253 LYS A NZ 1 ATOM 1310 N N . ILE A 1 174 ? 35.688 31.766 16.504 1.00 8.28 ? 254 ILE A N 1 ATOM 1311 C CA . ILE A 1 174 ? 34.887 32.549 17.434 1.00 7.86 ? 254 ILE A CA 1 ATOM 1312 C C . ILE A 1 174 ? 33.936 33.438 16.648 1.00 9.54 ? 254 ILE A C 1 ATOM 1313 O O . ILE A 1 174 ? 34.321 34.022 15.635 1.00 8.43 ? 254 ILE A O 1 ATOM 1314 C CB . ILE A 1 174 ? 35.765 33.452 18.316 1.00 9.47 ? 254 ILE A CB 1 ATOM 1315 C CG1 . ILE A 1 174 ? 36.905 32.650 18.946 1.00 8.01 ? 254 ILE A CG1 1 ATOM 1316 C CG2 . ILE A 1 174 ? 34.920 34.132 19.385 1.00 9.98 ? 254 ILE A CG2 1 ATOM 1317 C CD1 . ILE A 1 174 ? 37.929 33.510 19.669 1.00 12.01 ? 254 ILE A CD1 1 ATOM 1318 N N . PHE A 1 175 ? 32.697 33.548 17.113 1.00 7.57 ? 255 PHE A N 1 ATOM 1319 C CA . PHE A 1 175 ? 31.694 34.326 16.397 1.00 8.95 ? 255 PHE A CA 1 ATOM 1320 C C . PHE A 1 175 ? 31.108 35.451 17.242 1.00 9.97 ? 255 PHE A C 1 ATOM 1321 O O . PHE A 1 175 ? 30.859 35.279 18.433 1.00 9.29 ? 255 PHE A O 1 ATOM 1322 C CB . PHE A 1 175 ? 30.567 33.415 15.909 1.00 7.92 ? 255 PHE A CB 1 ATOM 1323 C CG . PHE A 1 175 ? 31.002 32.407 14.886 1.00 9.46 ? 255 PHE A CG 1 ATOM 1324 C CD1 . PHE A 1 175 ? 30.875 32.677 13.533 1.00 7.66 ? 255 PHE A CD1 1 ATOM 1325 C CD2 . PHE A 1 175 ? 31.537 31.189 15.275 1.00 9.21 ? 255 PHE A CD2 1 ATOM 1326 C CE1 . PHE A 1 175 ? 31.270 31.748 12.585 1.00 13.80 ? 255 PHE A CE1 1 ATOM 1327 C CE2 . PHE A 1 175 ? 31.936 30.257 14.333 1.00 8.17 ? 255 PHE A CE2 1 ATOM 1328 C CZ . PHE A 1 175 ? 31.802 30.538 12.985 1.00 11.45 ? 255 PHE A CZ 1 ATOM 1329 N N . ARG A 1 176 ? 30.900 36.604 16.614 1.00 7.94 ? 256 ARG A N 1 ATOM 1330 C CA . ARG A 1 176 ? 30.162 37.693 17.236 1.00 5.62 ? 256 ARG A CA 1 ATOM 1331 C C . ARG A 1 176 ? 28.828 37.837 16.516 1.00 7.26 ? 256 ARG A C 1 ATOM 1332 O O . ARG A 1 176 ? 28.782 38.021 15.298 1.00 7.77 ? 256 ARG A O 1 ATOM 1333 C CB . ARG A 1 176 ? 30.947 39.003 17.174 1.00 8.61 ? 256 ARG A CB 1 ATOM 1334 C CG . ARG A 1 176 ? 30.184 40.202 17.715 1.00 8.15 ? 256 ARG A CG 1 ATOM 1335 C CD . ARG A 1 176 ? 31.019 41.474 17.655 1.00 12.31 ? 256 ARG A CD 1 ATOM 1336 N NE . ARG A 1 176 ? 30.222 42.659 17.966 1.00 16.45 ? 256 ARG A NE 1 ATOM 1337 C CZ . ARG A 1 176 ? 30.731 43.851 18.263 1.00 23.43 ? 256 ARG A CZ 1 ATOM 1338 N NH1 . ARG A 1 176 ? 32.046 44.026 18.303 1.00 18.14 ? 256 ARG A NH1 1 ATOM 1339 N NH2 . ARG A 1 176 ? 29.924 44.869 18.530 1.00 22.76 ? 256 ARG A NH2 1 ATOM 1340 N N . ILE A 1 177 ? 27.745 37.744 17.275 1.00 7.84 ? 257 ILE A N 1 ATOM 1341 C CA . ILE A 1 177 ? 26.408 37.729 16.705 1.00 6.99 ? 257 ILE A CA 1 ATOM 1342 C C . ILE A 1 177 ? 25.558 38.853 17.283 1.00 9.44 ? 257 ILE A C 1 ATOM 1343 O O . ILE A 1 177 ? 25.520 39.050 18.496 1.00 8.50 ? 257 ILE A O 1 ATOM 1344 C CB . ILE A 1 177 ? 25.729 36.374 16.975 1.00 5.97 ? 257 ILE A CB 1 ATOM 1345 C CG1 . ILE A 1 177 ? 26.597 35.239 16.420 1.00 8.25 ? 257 ILE A CG1 1 ATOM 1346 C CG2 . ILE A 1 177 ? 24.329 36.343 16.375 1.00 7.38 ? 257 ILE A CG2 1 ATOM 1347 C CD1 . ILE A 1 177 ? 26.304 33.881 17.021 1.00 7.69 ? 257 ILE A CD1 1 ATOM 1348 N N . GLU A 1 178 ? 24.883 39.596 16.413 1.00 6.67 ? 258 GLU A N 1 ATOM 1349 C CA . GLU A 1 178 ? 23.998 40.666 16.860 1.00 5.77 ? 258 GLU A CA 1 ATOM 1350 C C . GLU A 1 178 ? 22.613 40.506 16.248 1.00 7.05 ? 258 GLU A C 1 ATOM 1351 O O . GLU A 1 178 ? 22.465 40.490 15.027 1.00 9.61 ? 258 GLU A O 1 ATOM 1352 C CB . GLU A 1 178 ? 24.583 42.034 16.505 1.00 9.75 ? 258 GLU A CB 1 ATOM 1353 C CG . GLU A 1 178 ? 25.921 42.315 17.173 1.00 15.03 ? 258 GLU A CG 1 ATOM 1354 C CD . GLU A 1 178 ? 26.521 43.641 16.750 1.00 23.79 ? 258 GLU A CD 1 ATOM 1355 O OE1 . GLU A 1 178 ? 25.791 44.475 16.174 1.00 26.60 ? 258 GLU A OE1 1 ATOM 1356 O OE2 . GLU A 1 178 ? 27.726 43.850 16.999 1.00 23.40 ? 258 GLU A OE2 1 ATOM 1357 N N . LYS A 1 179 ? 21.604 40.386 17.105 1.00 8.64 ? 259 LYS A N 1 ATOM 1358 C CA . LYS A 1 179 ? 20.235 40.143 16.659 1.00 9.69 ? 259 LYS A CA 1 ATOM 1359 C C . LYS A 1 179 ? 20.159 38.957 15.699 1.00 8.83 ? 259 LYS A C 1 ATOM 1360 O O . LYS A 1 179 ? 19.425 38.987 14.710 1.00 7.41 ? 259 LYS A O 1 ATOM 1361 C CB . LYS A 1 179 ? 19.642 41.400 16.019 1.00 11.51 ? 259 LYS A CB 1 ATOM 1362 C CG . LYS A 1 179 ? 19.518 42.572 16.982 1.00 16.59 ? 259 LYS A CG 1 ATOM 1363 C CD . LYS A 1 179 ? 18.904 43.784 16.309 1.00 24.93 ? 259 LYS A CD 1 ATOM 1364 C CE . LYS A 1 179 ? 18.664 44.901 17.310 1.00 30.85 ? 259 LYS A CE 1 ATOM 1365 N NZ . LYS A 1 179 ? 17.787 44.453 18.428 1.00 41.65 ? 259 LYS A NZ 1 ATOM 1366 N N . GLY A 1 180 ? 20.926 37.913 15.998 1.00 6.49 ? 260 GLY A N 1 ATOM 1367 C CA . GLY A 1 180 ? 20.884 36.688 15.222 1.00 4.97 ? 260 GLY A CA 1 ATOM 1368 C C . GLY A 1 180 ? 21.700 36.720 13.943 1.00 9.45 ? 260 GLY A C 1 ATOM 1369 O O . GLY A 1 180 ? 21.713 35.750 13.186 1.00 9.47 ? 260 GLY A O 1 ATOM 1370 N N . LYS A 1 181 ? 22.386 37.832 13.702 1.00 6.30 ? 261 LYS A N 1 ATOM 1371 C CA . LYS A 1 181 ? 23.208 37.978 12.505 1.00 7.62 ? 261 LYS A CA 1 ATOM 1372 C C . LYS A 1 181 ? 24.689 37.939 12.859 1.00 6.51 ? 261 LYS A C 1 ATOM 1373 O O . LYS A 1 181 ? 25.139 38.666 13.742 1.00 6.97 ? 261 LYS A O 1 ATOM 1374 C CB . LYS A 1 181 ? 22.892 39.301 11.806 1.00 14.76 ? 261 LYS A CB 1 ATOM 1375 C CG . LYS A 1 181 ? 21.427 39.490 11.434 1.00 17.49 ? 261 LYS A CG 1 ATOM 1376 C CD . LYS A 1 181 ? 21.065 38.717 10.175 1.00 23.85 ? 261 LYS A CD 1 ATOM 1377 C CE . LYS A 1 181 ? 19.621 38.979 9.765 1.00 22.59 ? 261 LYS A CE 1 ATOM 1378 N NZ . LYS A 1 181 ? 19.238 38.248 8.522 1.00 24.77 ? 261 LYS A NZ 1 ATOM 1379 N N . ILE A 1 182 ? 25.451 37.096 12.170 1.00 6.88 ? 262 ILE A N 1 ATOM 1380 C CA . ILE A 1 182 ? 26.895 37.067 12.371 1.00 7.46 ? 262 ILE A CA 1 ATOM 1381 C C . ILE A 1 182 ? 27.502 38.347 11.808 1.00 13.96 ? 262 ILE A C 1 ATOM 1382 O O . ILE A 1 182 ? 27.381 38.628 10.614 1.00 11.54 ? 262 ILE A O 1 ATOM 1383 C CB . ILE A 1 182 ? 27.541 35.842 11.701 1.00 10.51 ? 262 ILE A CB 1 ATOM 1384 C CG1 . ILE A 1 182 ? 26.951 34.556 12.282 1.00 12.09 ? 262 ILE A CG1 1 ATOM 1385 C CG2 . ILE A 1 182 ? 29.054 35.866 11.891 1.00 9.78 ? 262 ILE A CG2 1 ATOM 1386 C CD1 . ILE A 1 182 ? 27.404 33.300 11.578 1.00 17.05 ? 262 ILE A CD1 1 ATOM 1387 N N . VAL A 1 183 ? 28.135 39.132 12.674 1.00 6.35 ? 263 VAL A N 1 ATOM 1388 C CA . VAL A 1 183 ? 28.727 40.397 12.253 1.00 8.25 ? 263 VAL A CA 1 ATOM 1389 C C . VAL A 1 183 ? 30.246 40.305 12.172 1.00 13.39 ? 263 VAL A C 1 ATOM 1390 O O . VAL A 1 183 ? 30.892 41.141 11.544 1.00 9.57 ? 263 VAL A O 1 ATOM 1391 C CB . VAL A 1 183 ? 28.327 41.560 13.184 1.00 11.16 ? 263 VAL A CB 1 ATOM 1392 C CG1 . VAL A 1 183 ? 26.830 41.824 13.088 1.00 15.21 ? 263 VAL A CG1 1 ATOM 1393 C CG2 . VAL A 1 183 ? 28.733 41.262 14.620 1.00 11.74 ? 263 VAL A CG2 1 ATOM 1394 N N . LYS A 1 184 ? 30.809 39.284 12.809 1.00 8.97 ? 264 LYS A N 1 ATOM 1395 C CA . LYS A 1 184 ? 32.248 39.063 12.753 1.00 11.94 ? 264 LYS A CA 1 ATOM 1396 C C . LYS A 1 184 ? 32.616 37.662 13.222 1.00 9.91 ? 264 LYS A C 1 ATOM 1397 O O . LYS A 1 184 ? 31.962 37.095 14.100 1.00 8.43 ? 264 LYS A O 1 ATOM 1398 C CB . LYS A 1 184 ? 32.992 40.109 13.588 1.00 12.45 ? 264 LYS A CB 1 ATOM 1399 C CG . LYS A 1 184 ? 34.498 40.128 13.354 1.00 12.85 ? 264 LYS A CG 1 ATOM 1400 C CD . LYS A 1 184 ? 35.194 41.150 14.239 1.00 16.88 ? 264 LYS A CD 1 ATOM 1401 C CE . LYS A 1 184 ? 36.672 41.262 13.883 1.00 17.49 ? 264 LYS A CE 1 ATOM 1402 N NZ . LYS A 1 184 ? 37.402 42.214 14.767 1.00 19.16 ? 264 LYS A NZ 1 ATOM 1403 N N . SER A 1 185 ? 33.659 37.105 12.619 1.00 4.95 ? 265 SER A N 1 ATOM 1404 C CA . SER A 1 185 ? 34.211 35.831 13.056 1.00 8.46 ? 265 SER A CA 1 ATOM 1405 C C . SER A 1 185 ? 35.715 35.826 12.840 1.00 10.24 ? 265 SER A C 1 ATOM 1406 O O . SER A 1 185 ? 36.238 36.587 12.026 1.00 11.42 ? 265 SER A O 1 ATOM 1407 C CB . SER A 1 185 ? 33.564 34.661 12.311 1.00 8.24 ? 265 SER A CB 1 ATOM 1408 O OG . SER A 1 185 ? 33.880 34.683 10.929 1.00 9.74 ? 265 SER A OG 1 ATOM 1409 N N . VAL A 1 186 ? 36.409 34.969 13.578 1.00 8.65 ? 266 VAL A N 1 ATOM 1410 C CA . VAL A 1 186 ? 37.850 34.839 13.432 1.00 11.95 ? 266 VAL A CA 1 ATOM 1411 C C . VAL A 1 186 ? 38.272 33.413 13.752 1.00 11.15 ? 266 VAL A C 1 ATOM 1412 O O . VAL A 1 186 ? 37.753 32.799 14.685 1.00 10.35 ? 266 VAL A O 1 ATOM 1413 C CB . VAL A 1 186 ? 38.599 35.823 14.352 1.00 11.36 ? 266 VAL A CB 1 ATOM 1414 C CG1 . VAL A 1 186 ? 38.259 35.558 15.811 1.00 15.00 ? 266 VAL A CG1 1 ATOM 1415 C CG2 . VAL A 1 186 ? 40.102 35.731 14.124 1.00 15.61 ? 266 VAL A CG2 1 ATOM 1416 N N . GLU A 1 187 ? 39.197 32.872 12.966 1.00 10.76 ? 267 GLU A N 1 ATOM 1417 C CA . GLU A 1 187 ? 39.719 31.548 13.266 1.00 11.38 ? 267 GLU A CA 1 ATOM 1418 C C . GLU A 1 187 ? 40.868 31.646 14.256 1.00 13.28 ? 267 GLU A C 1 ATOM 1419 O O . GLU A 1 187 ? 41.795 32.433 14.072 1.00 10.81 ? 267 GLU A O 1 ATOM 1420 C CB . GLU A 1 187 ? 40.173 30.808 12.008 1.00 10.96 ? 267 GLU A CB 1 ATOM 1421 C CG . GLU A 1 187 ? 40.822 29.471 12.334 1.00 12.83 ? 267 GLU A CG 1 ATOM 1422 C CD . GLU A 1 187 ? 41.055 28.596 11.121 1.00 18.72 ? 267 GLU A CD 1 ATOM 1423 O OE1 . GLU A 1 187 ? 40.852 29.069 9.983 1.00 20.52 ? 267 GLU A OE1 1 ATOM 1424 O OE2 . GLU A 1 187 ? 41.446 27.426 11.313 1.00 13.72 ? 267 GLU A OE2 1 ATOM 1425 N N . MET A 1 188 ? 40.797 30.845 15.311 1.00 9.32 ? 268 MET A N 1 ATOM 1426 C CA . MET A 1 188 ? 41.846 30.831 16.318 1.00 8.38 ? 268 MET A CA 1 ATOM 1427 C C . MET A 1 188 ? 43.110 30.175 15.772 1.00 9.32 ? 268 MET A C 1 ATOM 1428 O O . MET A 1 188 ? 43.069 29.068 15.239 1.00 9.33 ? 268 MET A O 1 ATOM 1429 C CB . MET A 1 188 ? 41.364 30.105 17.571 1.00 7.88 ? 268 MET A CB 1 ATOM 1430 C CG . MET A 1 188 ? 40.255 30.837 18.310 1.00 6.22 ? 268 MET A CG 1 ATOM 1431 S SD . MET A 1 188 ? 39.245 29.748 19.325 1.00 11.54 ? 268 MET A SD 1 ATOM 1432 C CE . MET A 1 188 ? 40.493 28.976 20.353 1.00 9.43 ? 268 MET A CE 1 ATOM 1433 N N . ASN A 1 189 ? 44.229 30.879 15.898 1.00 9.98 ? 269 ASN A N 1 ATOM 1434 C CA . ASN A 1 189 ? 45.531 30.334 15.541 1.00 8.44 ? 269 ASN A CA 1 ATOM 1435 C C . ASN A 1 189 ? 46.058 29.517 16.718 1.00 9.74 ? 269 ASN A C 1 ATOM 1436 O O . ASN A 1 189 ? 46.783 30.032 17.566 1.00 8.08 ? 269 ASN A O 1 ATOM 1437 C CB . ASN A 1 189 ? 46.493 31.474 15.193 1.00 7.67 ? 269 ASN A CB 1 ATOM 1438 C CG . ASN A 1 189 ? 47.867 30.980 14.769 1.00 12.15 ? 269 ASN A CG 1 ATOM 1439 O OD1 . ASN A 1 189 ? 47.990 30.008 14.024 1.00 8.28 ? 269 ASN A OD1 1 ATOM 1440 N ND2 . ASN A 1 189 ? 48.908 31.659 15.238 1.00 8.00 ? 269 ASN A ND2 1 ATOM 1441 N N . ALA A 1 190 ? 45.674 28.245 16.779 1.00 8.81 ? 270 ALA A N 1 ATOM 1442 C CA . ALA A 1 190 ? 45.990 27.416 17.938 1.00 6.45 ? 270 ALA A CA 1 ATOM 1443 C C . ALA A 1 190 ? 46.534 26.038 17.564 1.00 9.14 ? 270 ALA A C 1 ATOM 1444 O O . ALA A 1 190 ? 45.884 25.022 17.813 1.00 4.28 ? 270 ALA A O 1 ATOM 1445 C CB . ALA A 1 190 ? 44.757 27.273 18.830 1.00 7.72 ? 270 ALA A CB 1 ATOM 1446 N N . PRO A 1 191 ? 47.730 25.998 16.958 1.00 13.36 ? 271 PRO A N 1 ATOM 1447 C CA . PRO A 1 191 ? 48.360 24.708 16.659 1.00 12.43 ? 271 PRO A CA 1 ATOM 1448 C C . PRO A 1 191 ? 48.683 23.935 17.936 1.00 11.37 ? 271 PRO A C 1 ATOM 1449 O O . PRO A 1 191 ? 49.129 24.527 18.918 1.00 10.38 ? 271 PRO A O 1 ATOM 1450 C CB . PRO A 1 191 ? 49.654 25.099 15.929 1.00 13.49 ? 271 PRO A CB 1 ATOM 1451 C CG . PRO A 1 191 ? 49.854 26.554 16.210 1.00 17.22 ? 271 PRO A CG 1 ATOM 1452 C CD . PRO A 1 191 ? 48.490 27.133 16.410 1.00 12.76 ? 271 PRO A CD 1 ATOM 1453 N N . ASN A 1 192 ? 48.447 22.627 17.907 1.00 10.36 ? 272 ASN A N 1 ATOM 1454 C CA . ASN A 1 192 ? 48.677 21.741 19.045 1.00 9.50 ? 272 ASN A CA 1 ATOM 1455 C C . ASN A 1 192 ? 47.630 21.887 20.151 1.00 11.38 ? 272 ASN A C 1 ATOM 1456 O O . ASN A 1 192 ? 47.723 21.235 21.191 1.00 12.56 ? 272 ASN A O 1 ATOM 1457 C CB . ASN A 1 192 ? 50.091 21.913 19.613 1.00 13.29 ? 272 ASN A CB 1 ATOM 1458 C CG . ASN A 1 192 ? 50.618 20.641 20.250 1.00 19.48 ? 272 ASN A CG 1 ATOM 1459 O OD1 . ASN A 1 192 ? 50.525 19.560 19.668 1.00 21.60 ? 272 ASN A OD1 1 ATOM 1460 N ND2 . ASN A 1 192 ? 51.180 20.764 21.447 1.00 20.63 ? 272 ASN A ND2 1 ATOM 1461 N N . TYR A 1 193 ? 46.646 22.752 19.921 1.00 12.51 ? 273 TYR A N 1 ATOM 1462 C CA . TYR A 1 193 ? 45.501 22.899 20.816 1.00 11.88 ? 273 TYR A CA 1 ATOM 1463 C C . TYR A 1 193 ? 44.315 22.119 20.262 1.00 10.16 ? 273 TYR A C 1 ATOM 1464 O O . TYR A 1 193 ? 44.243 21.859 19.062 1.00 7.27 ? 273 TYR A O 1 ATOM 1465 C CB . TYR A 1 193 ? 45.087 24.369 20.920 1.00 9.37 ? 273 TYR A CB 1 ATOM 1466 C CG . TYR A 1 193 ? 45.941 25.236 21.817 1.00 12.79 ? 273 TYR A CG 1 ATOM 1467 C CD1 . TYR A 1 193 ? 47.240 25.574 21.464 1.00 16.63 ? 273 TYR A CD1 1 ATOM 1468 C CD2 . TYR A 1 193 ? 45.432 25.749 23.003 1.00 14.24 ? 273 TYR A CD2 1 ATOM 1469 C CE1 . TYR A 1 193 ? 48.015 26.378 22.278 1.00 20.44 ? 273 TYR A CE1 1 ATOM 1470 C CE2 . TYR A 1 193 ? 46.197 26.554 23.822 1.00 11.63 ? 273 TYR A CE2 1 ATOM 1471 C CZ . TYR A 1 193 ? 47.488 26.866 23.455 1.00 17.63 ? 273 TYR A CZ 1 ATOM 1472 O OH . TYR A 1 193 ? 48.255 27.668 24.268 1.00 22.47 ? 273 TYR A OH 1 ATOM 1473 N N . HIS A 1 194 ? 43.373 21.768 21.134 1.00 8.54 ? 274 HIS A N 1 ATOM 1474 C CA . HIS A 1 194 ? 42.110 21.180 20.697 1.00 7.90 ? 274 HIS A CA 1 ATOM 1475 C C . HIS A 1 194 ? 40.959 21.741 21.530 1.00 9.01 ? 274 HIS A C 1 ATOM 1476 O O . HIS A 1 194 ? 40.995 21.694 22.760 1.00 7.24 ? 274 HIS A O 1 ATOM 1477 C CB . HIS A 1 194 ? 42.155 19.652 20.793 1.00 9.47 ? 274 HIS A CB 1 ATOM 1478 C CG . HIS A 1 194 ? 41.123 18.962 19.957 1.00 9.57 ? 274 HIS A CG 1 ATOM 1479 N ND1 . HIS A 1 194 ? 40.019 18.337 20.495 1.00 10.93 ? 274 HIS A ND1 1 ATOM 1480 C CD2 . HIS A 1 194 ? 41.023 18.807 18.613 1.00 7.57 ? 274 HIS A CD2 1 ATOM 1481 C CE1 . HIS A 1 194 ? 39.286 17.822 19.523 1.00 11.29 ? 274 HIS A CE1 1 ATOM 1482 N NE2 . HIS A 1 194 ? 39.875 18.096 18.371 1.00 12.63 ? 274 HIS A NE2 1 ATOM 1483 N N . TYR A 1 195 ? 39.948 22.281 20.855 1.00 6.20 ? 275 TYR A N 1 ATOM 1484 C CA . TYR A 1 195 ? 38.797 22.882 21.526 1.00 6.90 ? 275 TYR A CA 1 ATOM 1485 C C . TYR A 1 195 ? 37.491 22.219 21.114 1.00 7.69 ? 275 TYR A C 1 ATOM 1486 O O . TYR A 1 195 ? 37.161 22.160 19.929 1.00 6.44 ? 275 TYR A O 1 ATOM 1487 C CB . TYR A 1 195 ? 38.697 24.376 21.206 1.00 4.79 ? 275 TYR A CB 1 ATOM 1488 C CG . TYR A 1 195 ? 39.776 25.231 21.827 1.00 8.12 ? 275 TYR A CG 1 ATOM 1489 C CD1 . TYR A 1 195 ? 40.997 25.411 21.191 1.00 9.70 ? 275 TYR A CD1 1 ATOM 1490 C CD2 . TYR A 1 195 ? 39.571 25.867 23.045 1.00 8.14 ? 275 TYR A CD2 1 ATOM 1491 C CE1 . TYR A 1 195 ? 41.986 26.196 21.750 1.00 8.30 ? 275 TYR A CE1 1 ATOM 1492 C CE2 . TYR A 1 195 ? 40.558 26.655 23.613 1.00 6.54 ? 275 TYR A CE2 1 ATOM 1493 C CZ . TYR A 1 195 ? 41.762 26.815 22.958 1.00 9.29 ? 275 TYR A CZ 1 ATOM 1494 O OH . TYR A 1 195 ? 42.750 27.594 23.511 1.00 9.58 ? 275 TYR A OH 1 ATOM 1495 N N . GLU A 1 196 ? 36.746 21.733 22.099 1.00 7.74 ? 276 GLU A N 1 ATOM 1496 C CA . GLU A 1 196 ? 35.407 21.218 21.860 1.00 9.87 ? 276 GLU A CA 1 ATOM 1497 C C . GLU A 1 196 ? 34.475 21.596 23.005 1.00 8.02 ? 276 GLU A C 1 ATOM 1498 O O . GLU A 1 196 ? 34.915 21.768 24.144 1.00 8.45 ? 276 GLU A O 1 ATOM 1499 C CB . GLU A 1 196 ? 35.432 19.697 21.681 1.00 13.18 ? 276 GLU A CB 1 ATOM 1500 C CG . GLU A 1 196 ? 36.053 19.239 20.371 1.00 21.34 ? 276 GLU A CG 1 ATOM 1501 C CD . GLU A 1 196 ? 35.929 17.747 20.159 1.00 22.55 ? 276 GLU A CD 1 ATOM 1502 O OE1 . GLU A 1 196 ? 35.674 17.025 21.145 1.00 28.59 ? 276 GLU A OE1 1 ATOM 1503 O OE2 . GLU A 1 196 ? 36.088 17.294 19.007 1.00 17.98 ? 276 GLU A OE2 1 ATOM 1504 N N . GLU A 1 197 ? 33.193 21.741 22.688 1.00 7.70 ? 277 GLU A N 1 ATOM 1505 C CA . GLU A 1 197 ? 32.154 21.926 23.700 1.00 7.85 ? 277 GLU A CA 1 ATOM 1506 C C . GLU A 1 197 ? 32.502 22.968 24.763 1.00 8.11 ? 277 GLU A C 1 ATOM 1507 O O . GLU A 1 197 ? 32.460 22.684 25.962 1.00 9.15 ? 277 GLU A O 1 ATOM 1508 C CB . GLU A 1 197 ? 31.838 20.580 24.357 1.00 8.50 ? 277 GLU A CB 1 ATOM 1509 C CG . GLU A 1 197 ? 31.411 19.517 23.355 1.00 11.46 ? 277 GLU A CG 1 ATOM 1510 C CD . GLU A 1 197 ? 31.321 18.131 23.959 1.00 14.63 ? 277 GLU A CD 1 ATOM 1511 O OE1 . GLU A 1 197 ? 31.977 17.879 24.990 1.00 11.04 ? 277 GLU A OE1 1 ATOM 1512 O OE2 . GLU A 1 197 ? 30.597 17.288 23.391 1.00 14.26 ? 277 GLU A OE2 1 ATOM 1513 N N . CYS A 1 198 ? 32.829 24.179 24.325 1.00 6.91 ? 278 CYS A N 1 ATOM 1514 C CA . CYS A 1 198 ? 33.256 25.228 25.249 1.00 7.01 ? 278 CYS A CA 1 ATOM 1515 C C . CYS A 1 198 ? 32.137 25.717 26.164 1.00 6.73 ? 278 CYS A C 1 ATOM 1516 O O . CYS A 1 198 ? 30.995 25.891 25.734 1.00 6.84 ? 278 CYS A O 1 ATOM 1517 C CB . CYS A 1 198 ? 33.835 26.419 24.485 1.00 10.72 ? 278 CYS A CB 1 ATOM 1518 S SG . CYS A 1 198 ? 35.340 26.064 23.558 1.00 14.14 ? 278 CYS A SG 1 ATOM 1519 N N . SER A 1 199 ? 32.480 25.932 27.430 1.00 9.51 ? 279 SER A N 1 ATOM 1520 C CA . SER A 1 199 ? 31.590 26.598 28.370 1.00 8.35 ? 279 SER A CA 1 ATOM 1521 C C . SER A 1 199 ? 32.053 28.044 28.505 1.00 8.36 ? 279 SER A C 1 ATOM 1522 O O . SER A 1 199 ? 33.126 28.303 29.049 1.00 10.35 ? 279 SER A O 1 ATOM 1523 C CB . SER A 1 199 ? 31.623 25.901 29.730 1.00 8.67 ? 279 SER A CB 1 ATOM 1524 O OG . SER A 1 199 ? 31.154 24.567 29.633 1.00 13.54 ? 279 SER A OG 1 ATOM 1525 N N . CYS A 1 200 ? 31.253 28.977 27.994 1.00 7.79 ? 280 CYS A N 1 ATOM 1526 C CA . CYS A 1 200 ? 31.640 30.388 27.938 1.00 7.74 ? 280 CYS A CA 1 ATOM 1527 C C . CYS A 1 200 ? 30.755 31.272 28.813 1.00 10.56 ? 280 CYS A C 1 ATOM 1528 O O . CYS A 1 200 ? 29.543 31.077 28.887 1.00 11.32 ? 280 CYS A O 1 ATOM 1529 C CB . CYS A 1 200 ? 31.583 30.901 26.496 1.00 10.85 ? 280 CYS A CB 1 ATOM 1530 S SG . CYS A 1 200 ? 32.553 29.954 25.299 1.00 12.33 ? 280 CYS A SG 1 ATOM 1531 N N . TYR A 1 201 ? 31.368 32.257 29.460 1.00 5.74 ? 281 TYR A N 1 ATOM 1532 C CA . TYR A 1 201 ? 30.635 33.210 30.284 1.00 7.30 ? 281 TYR A CA 1 ATOM 1533 C C . TYR A 1 201 ? 31.243 34.598 30.135 1.00 7.60 ? 281 TYR A C 1 ATOM 1534 O O . TYR A 1 201 ? 32.421 34.727 29.798 1.00 7.31 ? 281 TYR A O 1 ATOM 1535 C CB . TYR A 1 201 ? 30.654 32.782 31.756 1.00 7.71 ? 281 TYR A CB 1 ATOM 1536 C CG . TYR A 1 201 ? 32.035 32.762 32.368 1.00 7.88 ? 281 TYR A CG 1 ATOM 1537 C CD1 . TYR A 1 201 ? 32.778 31.592 32.408 1.00 7.75 ? 281 TYR A CD1 1 ATOM 1538 C CD2 . TYR A 1 201 ? 32.600 33.916 32.902 1.00 6.10 ? 281 TYR A CD2 1 ATOM 1539 C CE1 . TYR A 1 201 ? 34.044 31.568 32.958 1.00 9.93 ? 281 TYR A CE1 1 ATOM 1540 C CE2 . TYR A 1 201 ? 33.868 33.899 33.456 1.00 9.27 ? 281 TYR A CE2 1 ATOM 1541 C CZ . TYR A 1 201 ? 34.584 32.720 33.482 1.00 9.46 ? 281 TYR A CZ 1 ATOM 1542 O OH . TYR A 1 201 ? 35.846 32.691 34.031 1.00 9.83 ? 281 TYR A OH 1 ATOM 1543 N N . PRO A 1 202 ? 30.436 35.643 30.382 1.00 8.92 ? 282 PRO A N 1 ATOM 1544 C CA . PRO A 1 202 ? 30.910 37.027 30.353 1.00 4.51 ? 282 PRO A CA 1 ATOM 1545 C C . PRO A 1 202 ? 31.445 37.469 31.710 1.00 7.55 ? 282 PRO A C 1 ATOM 1546 O O . PRO A 1 202 ? 30.961 37.026 32.754 1.00 7.71 ? 282 PRO A O 1 ATOM 1547 C CB . PRO A 1 202 ? 29.644 37.817 30.030 1.00 4.93 ? 282 PRO A CB 1 ATOM 1548 C CG . PRO A 1 202 ? 28.525 36.997 30.595 1.00 8.66 ? 282 PRO A CG 1 ATOM 1549 C CD . PRO A 1 202 ? 28.998 35.561 30.701 1.00 8.77 ? 282 PRO A CD 1 ATOM 1550 N N . ASP A 1 203 ? 32.432 38.354 31.685 1.00 4.95 ? 283 ASP A N 1 ATOM 1551 C CA . ASP A 1 203 ? 33.039 38.868 32.905 1.00 8.90 ? 283 ASP A CA 1 ATOM 1552 C C . ASP A 1 203 ? 33.757 40.168 32.562 1.00 10.55 ? 283 ASP A C 1 ATOM 1553 O O . ASP A 1 203 ? 34.718 40.164 31.794 1.00 10.34 ? 283 ASP A O 1 ATOM 1554 C CB . ASP A 1 203 ? 34.026 37.839 33.466 1.00 7.44 ? 283 ASP A CB 1 ATOM 1555 C CG . ASP A 1 203 ? 34.703 38.300 34.747 1.00 16.07 ? 283 ASP A CG 1 ATOM 1556 O OD1 . ASP A 1 203 ? 34.367 39.385 35.273 1.00 15.72 ? 283 ASP A OD1 1 ATOM 1557 O OD2 . ASP A 1 203 ? 35.583 37.564 35.237 1.00 18.02 ? 283 ASP A OD2 1 ATOM 1558 N N . SER A 1 204 ? 33.276 41.278 33.114 1.00 9.25 ? 284 SER A N 1 ATOM 1559 C CA . SER A 1 204 ? 33.887 42.586 32.874 1.00 10.87 ? 284 SER A CA 1 ATOM 1560 C C . SER A 1 204 ? 33.997 42.908 31.381 1.00 9.68 ? 284 SER A C 1 ATOM 1561 O O . SER A 1 204 ? 35.054 43.315 30.902 1.00 3.42 ? 284 SER A O 1 ATOM 1562 C CB . SER A 1 204 ? 35.269 42.668 33.535 1.00 12.12 ? 284 SER A CB 1 ATOM 1563 O OG . SER A 1 204 ? 35.174 42.478 34.937 1.00 16.53 ? 284 SER A OG 1 ATOM 1564 N N . SER A 1 205 ? 32.897 42.714 30.659 1.00 8.25 ? 285 SER A N 1 ATOM 1565 C CA . SER A 1 205 ? 32.809 43.062 29.238 1.00 11.96 ? 285 SER A CA 1 ATOM 1566 C C . SER A 1 205 ? 33.588 42.128 28.311 1.00 11.73 ? 285 SER A C 1 ATOM 1567 O O . SER A 1 205 ? 33.606 42.328 27.096 1.00 13.37 ? 285 SER A O 1 ATOM 1568 C CB . SER A 1 205 ? 33.240 44.514 29.004 1.00 14.77 ? 285 SER A CB 1 ATOM 1569 O OG . SER A 1 205 ? 32.379 45.422 29.668 1.00 13.10 ? 285 SER A OG 1 ATOM 1570 N N . GLU A 1 206 ? 34.233 41.113 28.876 1.00 8.07 ? 286 GLU A N 1 ATOM 1571 C CA . GLU A 1 206 ? 34.969 40.155 28.058 1.00 11.86 ? 286 GLU A CA 1 ATOM 1572 C C . GLU A 1 206 ? 34.460 38.731 28.263 1.00 10.24 ? 286 GLU A C 1 ATOM 1573 O O . GLU A 1 206 ? 33.782 38.440 29.246 1.00 8.78 ? 286 GLU A O 1 ATOM 1574 C CB . GLU A 1 206 ? 36.473 40.247 28.329 1.00 13.93 ? 286 GLU A CB 1 ATOM 1575 C CG . GLU A 1 206 ? 37.061 41.613 28.006 1.00 15.16 ? 286 GLU A CG 1 ATOM 1576 C CD . GLU A 1 206 ? 38.567 41.666 28.170 1.00 33.63 ? 286 GLU A CD 1 ATOM 1577 O OE1 . GLU A 1 206 ? 39.200 40.593 28.257 1.00 35.63 ? 286 GLU A OE1 1 ATOM 1578 O OE2 . GLU A 1 206 ? 39.120 42.786 28.208 1.00 41.39 ? 286 GLU A OE2 1 ATOM 1579 N N . ILE A 1 207 ? 34.784 37.850 27.324 1.00 6.65 ? 287 ILE A N 1 ATOM 1580 C CA . ILE A 1 207 ? 34.308 36.475 27.380 1.00 5.96 ? 287 ILE A CA 1 ATOM 1581 C C . ILE A 1 207 ? 35.434 35.509 27.726 1.00 6.07 ? 287 ILE A C 1 ATOM 1582 O O . ILE A 1 207 ? 36.536 35.607 27.189 1.00 9.76 ? 287 ILE A O 1 ATOM 1583 C CB . ILE A 1 207 ? 33.675 36.044 26.041 1.00 6.37 ? 287 ILE A CB 1 ATOM 1584 C CG1 . ILE A 1 207 ? 32.648 37.079 25.578 1.00 6.70 ? 287 ILE A CG1 1 ATOM 1585 C CG2 . ILE A 1 207 ? 33.035 34.668 26.169 1.00 5.36 ? 287 ILE A CG2 1 ATOM 1586 C CD1 . ILE A 1 207 ? 31.508 37.275 26.551 1.00 10.68 ? 287 ILE A CD1 1 ATOM 1587 N N . THR A 1 208 ? 35.149 34.580 28.631 1.00 7.45 ? 288 THR A N 1 ATOM 1588 C CA . THR A 1 208 ? 36.088 33.519 28.967 1.00 9.69 ? 288 THR A CA 1 ATOM 1589 C C . THR A 1 208 ? 35.440 32.169 28.677 1.00 8.03 ? 288 THR A C 1 ATOM 1590 O O . THR A 1 208 ? 34.296 31.934 29.064 1.00 7.27 ? 288 THR A O 1 ATOM 1591 C CB . THR A 1 208 ? 36.497 33.578 30.453 1.00 12.90 ? 288 THR A CB 1 ATOM 1592 O OG1 . THR A 1 208 ? 37.111 34.842 30.732 1.00 11.78 ? 288 THR A OG1 1 ATOM 1593 C CG2 . THR A 1 208 ? 37.471 32.462 30.784 1.00 11.60 ? 288 THR A CG2 1 ATOM 1594 N N . CYS A 1 209 ? 36.168 31.294 27.987 1.00 6.54 ? 289 CYS A N 1 ATOM 1595 C CA . CYS A 1 209 ? 35.666 29.965 27.648 1.00 7.24 ? 289 CYS A CA 1 ATOM 1596 C C . CYS A 1 209 ? 36.603 28.874 28.152 1.00 9.73 ? 289 CYS A C 1 ATOM 1597 O O . CYS A 1 209 ? 37.803 28.924 27.902 1.00 8.76 ? 289 CYS A O 1 ATOM 1598 C CB . CYS A 1 209 ? 35.523 29.809 26.131 1.00 9.65 ? 289 CYS A CB 1 ATOM 1599 S SG . CYS A 1 209 ? 34.346 30.914 25.330 1.00 12.32 ? 289 CYS A SG 1 ATOM 1600 N N . VAL A 1 210 ? 36.050 27.888 28.852 1.00 6.78 ? 290 VAL A N 1 ATOM 1601 C CA . VAL A 1 210 ? 36.807 26.703 29.243 1.00 5.17 ? 290 VAL A CA 1 ATOM 1602 C C . VAL A 1 210 ? 36.217 25.503 28.511 1.00 8.02 ? 290 VAL A C 1 ATOM 1603 O O . VAL A 1 210 ? 35.006 25.286 28.535 1.00 4.55 ? 290 VAL A O 1 ATOM 1604 C CB . VAL A 1 210 ? 36.776 26.476 30.768 1.00 5.28 ? 290 VAL A CB 1 ATOM 1605 C CG1 . VAL A 1 210 ? 37.530 25.206 31.135 1.00 5.92 ? 290 VAL A CG1 1 ATOM 1606 C CG2 . VAL A 1 210 ? 37.370 27.677 31.490 1.00 6.47 ? 290 VAL A CG2 1 ATOM 1607 N N . CYS A 1 211 ? 37.076 24.730 27.856 1.00 7.45 ? 291 CYS A N 1 ATOM 1608 C CA . CYS A 1 211 ? 36.613 23.761 26.869 1.00 6.39 ? 291 CYS A CA 1 ATOM 1609 C C . CYS A 1 211 ? 37.166 22.350 27.079 1.00 6.17 ? 291 CYS A C 1 ATOM 1610 O O . CYS A 1 211 ? 37.728 22.033 28.128 1.00 7.36 ? 291 CYS A O 1 ATOM 1611 C CB . CYS A 1 211 ? 36.948 24.268 25.463 1.00 7.06 ? 291 CYS A CB 1 ATOM 1612 S SG . CYS A 1 211 ? 36.546 26.024 25.204 1.00 12.17 ? 291 CYS A SG 1 ATOM 1613 N N . ARG A 1 212 ? 36.984 21.508 26.068 1.00 5.15 ? 292 ARG A N 1 ATOM 1614 C CA . ARG A 1 212 ? 37.382 20.105 26.123 1.00 5.16 ? 292 ARG A CA 1 ATOM 1615 C C . ARG A 1 212 ? 38.394 19.780 25.027 1.00 6.24 ? 292 ARG A C 1 ATOM 1616 O O . ARG A 1 212 ? 38.120 19.970 23.845 1.00 7.25 ? 292 ARG A O 1 ATOM 1617 C CB . ARG A 1 212 ? 36.145 19.213 25.973 1.00 4.75 ? 292 ARG A CB 1 ATOM 1618 C CG . ARG A 1 212 ? 36.416 17.758 25.587 1.00 6.83 ? 292 ARG A CG 1 ATOM 1619 C CD . ARG A 1 212 ? 35.094 17.030 25.336 1.00 9.42 ? 292 ARG A CD 1 ATOM 1620 N NE . ARG A 1 212 ? 35.262 15.644 24.899 1.00 8.36 ? 292 ARG A NE 1 ATOM 1621 C CZ . ARG A 1 212 ? 34.256 14.782 24.762 1.00 13.17 ? 292 ARG A CZ 1 ATOM 1622 N NH1 . ARG A 1 212 ? 33.014 15.163 25.030 1.00 7.17 ? 292 ARG A NH1 1 ATOM 1623 N NH2 . ARG A 1 212 ? 34.487 13.538 24.362 1.00 12.13 ? 292 ARG A NH2 1 ATOM 1624 N N . ASP A 1 213 ? 39.566 19.300 25.431 1.00 7.52 ? 293 ASP A N 1 ATOM 1625 C CA . ASP A 1 213 ? 40.581 18.833 24.489 1.00 7.33 ? 293 ASP A CA 1 ATOM 1626 C C . ASP A 1 213 ? 40.411 17.334 24.302 1.00 8.17 ? 293 ASP A C 1 ATOM 1627 O O . ASP A 1 213 ? 40.771 16.564 25.176 1.00 8.41 ? 293 ASP A O 1 ATOM 1628 C CB . ASP A 1 213 ? 41.983 19.150 25.027 1.00 6.34 ? 293 ASP A CB 1 ATOM 1629 C CG . ASP A 1 213 ? 43.101 18.554 24.174 1.00 9.15 ? 293 ASP A CG 1 ATOM 1630 O OD1 . ASP A 1 213 ? 42.855 17.585 23.429 1.00 9.11 ? 293 ASP A OD1 1 ATOM 1631 O OD2 . ASP A 1 213 ? 44.242 19.055 24.261 1.00 9.58 ? 293 ASP A OD2 1 ATOM 1632 N N . ASN A 1 214 ? 39.860 16.918 23.167 1.00 7.26 ? 294 ASN A N 1 ATOM 1633 C CA . ASN A 1 214 ? 39.579 15.504 22.936 1.00 8.12 ? 294 ASN A CA 1 ATOM 1634 C C . ASN A 1 214 ? 40.761 14.782 22.296 1.00 11.00 ? 294 ASN A C 1 ATOM 1635 O O . ASN A 1 214 ? 40.729 13.570 22.087 1.00 11.27 ? 294 ASN A O 1 ATOM 1636 C CB . ASN A 1 214 ? 38.339 15.346 22.054 1.00 8.80 ? 294 ASN A CB 1 ATOM 1637 C CG . ASN A 1 214 ? 37.599 14.052 22.319 1.00 12.95 ? 294 ASN A CG 1 ATOM 1638 O OD1 . ASN A 1 214 ? 37.161 13.794 23.441 1.00 12.46 ? 294 ASN A OD1 1 ATOM 1639 N ND2 . ASN A 1 214 ? 37.446 13.233 21.285 1.00 12.60 ? 294 ASN A ND2 1 ATOM 1640 N N . TRP A 1 215 ? 41.806 15.545 22.004 1.00 7.86 ? 295 TRP A N 1 ATOM 1641 C CA . TRP A 1 215 ? 42.947 15.058 21.241 1.00 8.32 ? 295 TRP A CA 1 ATOM 1642 C C . TRP A 1 215 ? 44.065 14.518 22.132 1.00 10.35 ? 295 TRP A C 1 ATOM 1643 O O . TRP A 1 215 ? 44.399 13.335 22.065 1.00 8.08 ? 295 TRP A O 1 ATOM 1644 C CB . TRP A 1 215 ? 43.461 16.190 20.346 1.00 10.28 ? 295 TRP A CB 1 ATOM 1645 C CG . TRP A 1 215 ? 44.713 15.895 19.580 1.00 9.43 ? 295 TRP A CG 1 ATOM 1646 C CD1 . TRP A 1 215 ? 45.301 14.677 19.388 1.00 12.79 ? 295 TRP A CD1 1 ATOM 1647 C CD2 . TRP A 1 215 ? 45.527 16.847 18.887 1.00 8.80 ? 295 TRP A CD2 1 ATOM 1648 N NE1 . TRP A 1 215 ? 46.437 14.816 18.623 1.00 11.48 ? 295 TRP A NE1 1 ATOM 1649 C CE2 . TRP A 1 215 ? 46.596 16.139 18.305 1.00 8.34 ? 295 TRP A CE2 1 ATOM 1650 C CE3 . TRP A 1 215 ? 45.456 18.233 18.707 1.00 6.67 ? 295 TRP A CE3 1 ATOM 1651 C CZ2 . TRP A 1 215 ? 47.585 16.770 17.553 1.00 11.29 ? 295 TRP A CZ2 1 ATOM 1652 C CZ3 . TRP A 1 215 ? 46.438 18.856 17.963 1.00 9.61 ? 295 TRP A CZ3 1 ATOM 1653 C CH2 . TRP A 1 215 ? 47.488 18.125 17.393 1.00 9.81 ? 295 TRP A CH2 1 ATOM 1654 N N . HIS A 1 216 ? 44.639 15.377 22.969 1.00 9.72 ? 296 HIS A N 1 ATOM 1655 C CA . HIS A 1 216 ? 45.801 14.976 23.760 1.00 9.94 ? 296 HIS A CA 1 ATOM 1656 C C . HIS A 1 216 ? 46.015 15.709 25.083 1.00 10.06 ? 296 HIS A C 1 ATOM 1657 O O . HIS A 1 216 ? 47.137 15.776 25.584 1.00 8.73 ? 296 HIS A O 1 ATOM 1658 C CB . HIS A 1 216 ? 47.063 15.010 22.891 1.00 8.97 ? 296 HIS A CB 1 ATOM 1659 C CG . HIS A 1 216 ? 47.352 16.352 22.291 1.00 12.12 ? 296 HIS A CG 1 ATOM 1660 N ND1 . HIS A 1 216 ? 48.305 16.542 21.315 1.00 10.64 ? 296 HIS A ND1 1 ATOM 1661 C CD2 . HIS A 1 216 ? 46.809 17.572 22.528 1.00 8.81 ? 296 HIS A CD2 1 ATOM 1662 C CE1 . HIS A 1 216 ? 48.342 17.820 20.978 1.00 9.13 ? 296 HIS A CE1 1 ATOM 1663 N NE2 . HIS A 1 216 ? 47.443 18.465 21.700 1.00 13.16 ? 296 HIS A NE2 1 ATOM 1664 N N . GLY A 1 217 ? 44.945 16.251 25.653 1.00 9.65 ? 297 GLY A N 1 ATOM 1665 C CA . GLY A 1 217 ? 45.059 16.950 26.921 1.00 8.84 ? 297 GLY A CA 1 ATOM 1666 C C . GLY A 1 217 ? 44.087 16.528 28.004 1.00 12.62 ? 297 GLY A C 1 ATOM 1667 O O . GLY A 1 217 ? 42.883 16.492 27.774 1.00 8.47 ? 297 GLY A O 1 ATOM 1668 N N . SER A 1 218 ? 44.609 16.213 29.187 1.00 10.71 ? 298 SER A N 1 ATOM 1669 C CA . SER A 1 218 ? 43.770 15.819 30.317 1.00 11.10 ? 298 SER A CA 1 ATOM 1670 C C . SER A 1 218 ? 43.448 17.012 31.216 1.00 9.72 ? 298 SER A C 1 ATOM 1671 O O . SER A 1 218 ? 42.646 16.907 32.147 1.00 10.24 ? 298 SER A O 1 ATOM 1672 C CB . SER A 1 218 ? 44.428 14.697 31.120 1.00 11.72 ? 298 SER A CB 1 ATOM 1673 O OG . SER A 1 218 ? 45.752 15.038 31.484 1.00 16.33 ? 298 SER A OG 1 ATOM 1674 N N . ASN A 1 219 ? 44.095 18.140 30.943 1.00 8.61 ? 299 ASN A N 1 ATOM 1675 C CA . ASN A 1 219 ? 43.671 19.420 31.497 1.00 10.75 ? 299 ASN A CA 1 ATOM 1676 C C . ASN A 1 219 ? 42.816 20.136 30.456 1.00 9.03 ? 299 ASN A C 1 ATOM 1677 O O . ASN A 1 219 ? 42.781 19.726 29.299 1.00 9.79 ? 299 ASN A O 1 ATOM 1678 C CB . ASN A 1 219 ? 44.874 20.277 31.910 1.00 9.06 ? 299 ASN A CB 1 ATOM 1679 C CG . ASN A 1 219 ? 45.890 20.447 30.790 1.00 9.36 ? 299 ASN A CG 1 ATOM 1680 O OD1 . ASN A 1 219 ? 45.950 19.646 29.858 1.00 7.34 ? 299 ASN A OD1 1 ATOM 1681 N ND2 . ASN A 1 219 ? 46.701 21.493 30.885 1.00 9.68 ? 299 ASN A ND2 1 ATOM 1682 N N . ARG A 1 220 ? 42.119 21.193 30.859 1.00 9.63 ? 300 ARG A N 1 ATOM 1683 C CA . ARG A 1 220 ? 41.214 21.882 29.942 1.00 8.60 ? 300 ARG A CA 1 ATOM 1684 C C . ARG A 1 220 ? 41.851 23.095 29.279 1.00 6.05 ? 300 ARG A C 1 ATOM 1685 O O . ARG A 1 220 ? 42.533 23.881 29.935 1.00 7.20 ? 300 ARG A O 1 ATOM 1686 C CB . ARG A 1 220 ? 39.928 22.299 30.660 1.00 7.87 ? 300 ARG A CB 1 ATOM 1687 C CG . ARG A 1 220 ? 39.132 21.132 31.211 1.00 6.83 ? 300 ARG A CG 1 ATOM 1688 C CD . ARG A 1 220 ? 37.694 21.524 31.523 1.00 7.34 ? 300 ARG A CD 1 ATOM 1689 N NE . ARG A 1 220 ? 36.925 20.356 31.936 1.00 5.95 ? 300 ARG A NE 1 ATOM 1690 C CZ . ARG A 1 220 ? 36.388 19.485 31.090 1.00 6.41 ? 300 ARG A CZ 1 ATOM 1691 N NH1 . ARG A 1 220 ? 36.521 19.661 29.780 1.00 5.87 ? 300 ARG A NH1 1 ATOM 1692 N NH2 . ARG A 1 220 ? 35.715 18.440 31.551 1.00 6.45 ? 300 ARG A NH2 1 ATOM 1693 N N . PRO A 1 221 ? 41.626 23.249 27.967 1.00 6.76 ? 301 PRO A N 1 ATOM 1694 C CA . PRO A 1 221 ? 42.073 24.442 27.249 1.00 8.10 ? 301 PRO A CA 1 ATOM 1695 C C . PRO A 1 221 ? 41.107 25.591 27.502 1.00 7.60 ? 301 PRO A C 1 ATOM 1696 O O . PRO A 1 221 ? 39.944 25.351 27.823 1.00 6.84 ? 301 PRO A O 1 ATOM 1697 C CB . PRO A 1 221 ? 41.994 24.009 25.786 1.00 5.78 ? 301 PRO A CB 1 ATOM 1698 C CG . PRO A 1 221 ? 40.874 23.029 25.758 1.00 7.00 ? 301 PRO A CG 1 ATOM 1699 C CD . PRO A 1 221 ? 40.906 22.310 27.088 1.00 6.11 ? 301 PRO A CD 1 ATOM 1700 N N . TRP A 1 222 ? 41.586 26.822 27.372 1.00 5.81 ? 302 TRP A N 1 ATOM 1701 C CA . TRP A 1 222 ? 40.713 27.981 27.489 1.00 7.67 ? 302 TRP A CA 1 ATOM 1702 C C . TRP A 1 222 ? 40.996 28.990 26.389 1.00 8.54 ? 302 TRP A C 1 ATOM 1703 O O . TRP A 1 222 ? 42.065 28.981 25.776 1.00 7.40 ? 302 TRP A O 1 ATOM 1704 C CB . TRP A 1 222 ? 40.828 28.639 28.872 1.00 6.17 ? 302 TRP A CB 1 ATOM 1705 C CG . TRP A 1 222 ? 42.210 29.106 29.238 1.00 6.68 ? 302 TRP A CG 1 ATOM 1706 C CD1 . TRP A 1 222 ? 43.129 28.433 29.993 1.00 7.52 ? 302 TRP A CD1 1 ATOM 1707 C CD2 . TRP A 1 222 ? 42.825 30.352 28.879 1.00 7.05 ? 302 TRP A CD2 1 ATOM 1708 N NE1 . TRP A 1 222 ? 44.276 29.178 30.119 1.00 7.19 ? 302 TRP A NE1 1 ATOM 1709 C CE2 . TRP A 1 222 ? 44.116 30.360 29.446 1.00 7.13 ? 302 TRP A CE2 1 ATOM 1710 C CE3 . TRP A 1 222 ? 42.411 31.460 28.131 1.00 6.51 ? 302 TRP A CE3 1 ATOM 1711 C CZ2 . TRP A 1 222 ? 44.996 31.430 29.288 1.00 8.34 ? 302 TRP A CZ2 1 ATOM 1712 C CZ3 . TRP A 1 222 ? 43.288 32.523 27.974 1.00 9.15 ? 302 TRP A CZ3 1 ATOM 1713 C CH2 . TRP A 1 222 ? 44.565 32.500 28.552 1.00 11.03 ? 302 TRP A CH2 1 ATOM 1714 N N . VAL A 1 223 ? 40.013 29.842 26.128 1.00 8.84 ? 303 VAL A N 1 ATOM 1715 C CA . VAL A 1 223 ? 40.183 30.966 25.220 1.00 7.20 ? 303 VAL A CA 1 ATOM 1716 C C . VAL A 1 223 ? 39.382 32.134 25.769 1.00 6.86 ? 303 VAL A C 1 ATOM 1717 O O . VAL A 1 223 ? 38.237 31.966 26.191 1.00 6.93 ? 303 VAL A O 1 ATOM 1718 C CB . VAL A 1 223 ? 39.724 30.628 23.778 1.00 5.93 ? 303 VAL A CB 1 ATOM 1719 C CG1 . VAL A 1 223 ? 38.298 30.100 23.773 1.00 6.23 ? 303 VAL A CG1 1 ATOM 1720 C CG2 . VAL A 1 223 ? 39.851 31.850 22.872 1.00 5.57 ? 303 VAL A CG2 1 ATOM 1721 N N . SER A 1 224 ? 39.996 33.310 25.805 1.00 6.77 ? 304 SER A N 1 ATOM 1722 C CA . SER A 1 224 ? 39.294 34.511 26.237 1.00 7.31 ? 304 SER A CA 1 ATOM 1723 C C . SER A 1 224 ? 39.432 35.590 25.174 1.00 9.75 ? 304 SER A C 1 ATOM 1724 O O . SER A 1 224 ? 40.425 35.632 24.448 1.00 8.55 ? 304 SER A O 1 ATOM 1725 C CB . SER A 1 224 ? 39.819 35.002 27.591 1.00 11.27 ? 304 SER A CB 1 ATOM 1726 O OG . SER A 1 224 ? 41.184 35.374 27.514 1.00 18.24 ? 304 SER A OG 1 ATOM 1727 N N . PHE A 1 225 ? 38.430 36.457 25.075 1.00 5.29 ? 305 PHE A N 1 ATOM 1728 C CA . PHE A 1 225 ? 38.435 37.494 24.051 1.00 9.06 ? 305 PHE A CA 1 ATOM 1729 C C . PHE A 1 225 ? 37.539 38.673 24.409 1.00 8.57 ? 305 PHE A C 1 ATOM 1730 O O . PHE A 1 225 ? 36.598 38.537 25.193 1.00 7.57 ? 305 PHE A O 1 ATOM 1731 C CB . PHE A 1 225 ? 38.021 36.907 22.695 1.00 4.79 ? 305 PHE A CB 1 ATOM 1732 C CG . PHE A 1 225 ? 36.747 36.102 22.740 1.00 4.92 ? 305 PHE A CG 1 ATOM 1733 C CD1 . PHE A 1 225 ? 35.523 36.698 22.480 1.00 7.01 ? 305 PHE A CD1 1 ATOM 1734 C CD2 . PHE A 1 225 ? 36.775 34.747 23.036 1.00 6.16 ? 305 PHE A CD2 1 ATOM 1735 C CE1 . PHE A 1 225 ? 34.348 35.959 22.519 1.00 5.41 ? 305 PHE A CE1 1 ATOM 1736 C CE2 . PHE A 1 225 ? 35.604 34.001 23.077 1.00 6.17 ? 305 PHE A CE2 1 ATOM 1737 C CZ . PHE A 1 225 ? 34.390 34.608 22.814 1.00 5.06 ? 305 PHE A CZ 1 ATOM 1738 N N . ASN A 1 226 ? 37.844 39.834 23.837 1.00 7.42 ? 306 ASN A N 1 ATOM 1739 C CA . ASN A 1 226 ? 36.983 40.997 23.992 1.00 11.02 ? 306 ASN A CA 1 ATOM 1740 C C . ASN A 1 226 ? 35.911 41.033 22.906 1.00 6.90 ? 306 ASN A C 1 ATOM 1741 O O . ASN A 1 226 ? 35.808 40.109 22.099 1.00 6.79 ? 306 ASN A O 1 ATOM 1742 C CB . ASN A 1 226 ? 37.795 42.299 24.024 1.00 8.82 ? 306 ASN A CB 1 ATOM 1743 C CG . ASN A 1 226 ? 38.637 42.506 22.776 1.00 14.43 ? 306 ASN A CG 1 ATOM 1744 O OD1 . ASN A 1 226 ? 38.297 42.036 21.690 1.00 8.04 ? 306 ASN A OD1 1 ATOM 1745 N ND2 . ASN A 1 226 ? 39.742 43.230 22.927 1.00 10.95 ? 306 ASN A ND2 1 ATOM 1746 N N . GLN A 1 227 ? 35.113 42.093 22.889 1.00 7.98 ? 308 GLN A N 1 ATOM 1747 C CA . GLN A 1 227 ? 34.013 42.199 21.935 1.00 9.71 ? 308 GLN A CA 1 ATOM 1748 C C . GLN A 1 227 ? 34.485 42.286 20.483 1.00 12.23 ? 308 GLN A C 1 ATOM 1749 O O . GLN A 1 227 ? 33.729 41.978 19.559 1.00 11.36 ? 308 GLN A O 1 ATOM 1750 C CB . GLN A 1 227 ? 33.115 43.386 22.283 1.00 10.89 ? 308 GLN A CB 1 ATOM 1751 C CG . GLN A 1 227 ? 32.410 43.239 23.623 1.00 9.05 ? 308 GLN A CG 1 ATOM 1752 C CD . GLN A 1 227 ? 31.760 44.525 24.080 1.00 11.09 ? 308 GLN A CD 1 ATOM 1753 O OE1 . GLN A 1 227 ? 30.816 45.013 23.460 1.00 16.41 ? 308 GLN A OE1 1 ATOM 1754 N NE2 . GLN A 1 227 ? 32.266 45.085 25.172 1.00 17.86 ? 308 GLN A NE2 1 ATOM 1755 N N . ASN A 1 228 ? 35.732 42.701 20.282 1.00 7.40 ? 309 ASN A N 1 ATOM 1756 C CA . ASN A 1 228 ? 36.292 42.780 18.935 1.00 8.34 ? 309 ASN A CA 1 ATOM 1757 C C . ASN A 1 228 ? 36.938 41.468 18.490 1.00 8.39 ? 309 ASN A C 1 ATOM 1758 O O . ASN A 1 228 ? 37.528 41.388 17.413 1.00 11.37 ? 309 ASN A O 1 ATOM 1759 C CB . ASN A 1 228 ? 37.284 43.942 18.823 1.00 11.29 ? 309 ASN A CB 1 ATOM 1760 C CG . ASN A 1 228 ? 36.592 45.291 18.694 1.00 24.97 ? 309 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 228 ? 35.372 45.366 18.548 1.00 28.06 ? 309 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 228 ? 37.373 46.364 18.743 1.00 34.10 ? 309 ASN A ND2 1 ATOM 1763 N N . LEU A 1 229 ? 36.814 40.446 19.330 1.00 7.06 ? 310 LEU A N 1 ATOM 1764 C CA . LEU A 1 229 ? 37.327 39.107 19.043 1.00 9.36 ? 310 LEU A CA 1 ATOM 1765 C C . LEU A 1 229 ? 38.854 39.015 19.090 1.00 8.28 ? 310 LEU A C 1 ATOM 1766 O O . LEU A 1 229 ? 39.446 38.102 18.517 1.00 10.00 ? 310 LEU A O 1 ATOM 1767 C CB . LEU A 1 229 ? 36.795 38.581 17.704 1.00 8.68 ? 310 LEU A CB 1 ATOM 1768 C CG . LEU A 1 229 ? 35.272 38.527 17.568 1.00 8.77 ? 310 LEU A CG 1 ATOM 1769 C CD1 . LEU A 1 229 ? 34.872 37.753 16.322 1.00 9.77 ? 310 LEU A CD1 1 ATOM 1770 C CD2 . LEU A 1 229 ? 34.642 37.910 18.814 1.00 8.04 ? 310 LEU A CD2 1 ATOM 1771 N N . GLU A 1 230 ? 39.482 39.969 19.767 1.00 6.75 ? 311 GLU A N 1 ATOM 1772 C CA . GLU A 1 230 ? 40.906 39.880 20.062 1.00 9.68 ? 311 GLU A CA 1 ATOM 1773 C C . GLU A 1 230 ? 41.081 38.888 21.205 1.00 8.45 ? 311 GLU A C 1 ATOM 1774 O O . GLU A 1 230 ? 40.612 39.126 22.317 1.00 11.37 ? 311 GLU A O 1 ATOM 1775 C CB . GLU A 1 230 ? 41.459 41.260 20.426 1.00 8.97 ? 311 GLU A CB 1 ATOM 1776 C CG . GLU A 1 230 ? 41.357 42.261 19.276 1.00 14.61 ? 311 GLU A CG 1 ATOM 1777 C CD . GLU A 1 230 ? 41.661 43.692 19.688 1.00 22.47 ? 311 GLU A CD 1 ATOM 1778 O OE1 . GLU A 1 230 ? 41.515 44.018 20.884 1.00 20.24 ? 311 GLU A OE1 1 ATOM 1779 O OE2 . GLU A 1 230 ? 42.039 44.495 18.807 1.00 22.78 ? 311 GLU A OE2 1 ATOM 1780 N N . TYR A 1 231 ? 41.740 37.766 20.929 1.00 5.84 ? 312 TYR A N 1 ATOM 1781 C CA . TYR A 1 231 ? 41.723 36.635 21.856 1.00 7.74 ? 312 TYR A CA 1 ATOM 1782 C C . TYR A 1 231 ? 43.082 36.254 22.443 1.00 11.02 ? 312 TYR A C 1 ATOM 1783 O O . TYR A 1 231 ? 44.135 36.633 21.927 1.00 7.78 ? 312 TYR A O 1 ATOM 1784 C CB . TYR A 1 231 ? 41.114 35.405 21.172 1.00 5.68 ? 312 TYR A CB 1 ATOM 1785 C CG . TYR A 1 231 ? 41.951 34.883 20.018 1.00 7.46 ? 312 TYR A CG 1 ATOM 1786 C CD1 . TYR A 1 231 ? 43.040 34.049 20.247 1.00 6.69 ? 312 TYR A CD1 1 ATOM 1787 C CD2 . TYR A 1 231 ? 41.655 35.228 18.707 1.00 5.63 ? 312 TYR A CD2 1 ATOM 1788 C CE1 . TYR A 1 231 ? 43.811 33.578 19.202 1.00 7.01 ? 312 TYR A CE1 1 ATOM 1789 C CE2 . TYR A 1 231 ? 42.424 34.760 17.653 1.00 8.81 ? 312 TYR A CE2 1 ATOM 1790 C CZ . TYR A 1 231 ? 43.499 33.935 17.908 1.00 6.49 ? 312 TYR A CZ 1 ATOM 1791 O OH . TYR A 1 231 ? 44.267 33.465 16.865 1.00 8.80 ? 312 TYR A OH 1 ATOM 1792 N N . GLN A 1 232 ? 43.031 35.497 23.535 1.00 5.37 ? 313 GLN A N 1 ATOM 1793 C CA . GLN A 1 232 ? 44.199 34.830 24.097 1.00 9.24 ? 313 GLN A CA 1 ATOM 1794 C C . GLN A 1 232 ? 43.831 33.373 24.347 1.00 7.62 ? 313 GLN A C 1 ATOM 1795 O O . GLN A 1 232 ? 42.660 33.057 24.569 1.00 6.14 ? 313 GLN A O 1 ATOM 1796 C CB . GLN A 1 232 ? 44.626 35.488 25.410 1.00 11.62 ? 313 GLN A CB 1 ATOM 1797 C CG . GLN A 1 232 ? 45.043 36.939 25.277 1.00 18.95 ? 313 GLN A CG 1 ATOM 1798 C CD . GLN A 1 232 ? 45.465 37.540 26.603 1.00 31.18 ? 313 GLN A CD 1 ATOM 1799 O OE1 . GLN A 1 232 ? 44.666 37.644 27.533 1.00 35.23 ? 313 GLN A OE1 1 ATOM 1800 N NE2 . GLN A 1 232 ? 46.728 37.941 26.695 1.00 36.96 ? 313 GLN A NE2 1 ATOM 1801 N N . ILE A 1 233 ? 44.823 32.488 24.308 1.00 7.07 ? 314 ILE A N 1 ATOM 1802 C CA . ILE A 1 233 ? 44.584 31.063 24.517 1.00 4.89 ? 314 ILE A CA 1 ATOM 1803 C C . ILE A 1 233 ? 45.576 30.450 25.501 1.00 9.90 ? 314 ILE A C 1 ATOM 1804 O O . ILE A 1 233 ? 46.664 30.983 25.719 1.00 6.61 ? 314 ILE A O 1 ATOM 1805 C CB . ILE A 1 233 ? 44.659 30.270 23.197 1.00 7.34 ? 314 ILE A CB 1 ATOM 1806 C CG1 . ILE A 1 233 ? 46.005 30.510 22.509 1.00 9.68 ? 314 ILE A CG1 1 ATOM 1807 C CG2 . ILE A 1 233 ? 43.503 30.646 22.279 1.00 9.94 ? 314 ILE A CG2 1 ATOM 1808 C CD1 . ILE A 1 233 ? 46.198 29.699 21.245 1.00 13.77 ? 314 ILE A CD1 1 ATOM 1809 N N . GLY A 1 234 ? 45.191 29.323 26.090 1.00 9.44 ? 315 GLY A N 1 ATOM 1810 C CA . GLY A 1 234 ? 46.055 28.599 27.003 1.00 11.24 ? 315 GLY A CA 1 ATOM 1811 C C . GLY A 1 234 ? 45.389 27.346 27.534 1.00 9.80 ? 315 GLY A C 1 ATOM 1812 O O . GLY A 1 234 ? 44.323 26.949 27.062 1.00 11.05 ? 315 GLY A O 1 ATOM 1813 N N . TYR A 1 235 ? 46.032 26.716 28.512 1.00 7.07 ? 316 TYR A N 1 ATOM 1814 C CA . TYR A 1 235 ? 45.461 25.578 29.221 1.00 8.59 ? 316 TYR A CA 1 ATOM 1815 C C . TYR A 1 235 ? 45.490 25.878 30.710 1.00 7.97 ? 316 TYR A C 1 ATOM 1816 O O . TYR A 1 235 ? 46.378 26.587 31.186 1.00 9.51 ? 316 TYR A O 1 ATOM 1817 C CB . TYR A 1 235 ? 46.268 24.306 28.946 1.00 9.37 ? 316 TYR A CB 1 ATOM 1818 C CG . TYR A 1 235 ? 45.883 23.581 27.676 1.00 9.27 ? 316 TYR A CG 1 ATOM 1819 C CD1 . TYR A 1 235 ? 46.296 24.046 26.435 1.00 10.35 ? 316 TYR A CD1 1 ATOM 1820 C CD2 . TYR A 1 235 ? 45.113 22.426 27.720 1.00 9.61 ? 316 TYR A CD2 1 ATOM 1821 C CE1 . TYR A 1 235 ? 45.947 23.386 25.271 1.00 10.44 ? 316 TYR A CE1 1 ATOM 1822 C CE2 . TYR A 1 235 ? 44.758 21.756 26.560 1.00 7.01 ? 316 TYR A CE2 1 ATOM 1823 C CZ . TYR A 1 235 ? 45.179 22.241 25.339 1.00 9.94 ? 316 TYR A CZ 1 ATOM 1824 O OH . TYR A 1 235 ? 44.828 21.582 24.183 1.00 8.37 ? 316 TYR A OH 1 ATOM 1825 N N . ILE A 1 236 ? 44.523 25.342 31.447 1.00 5.14 ? 317 ILE A N 1 ATOM 1826 C CA . ILE A 1 236 ? 44.523 25.488 32.896 1.00 5.85 ? 317 ILE A CA 1 ATOM 1827 C C . ILE A 1 236 ? 45.723 24.744 33.484 1.00 6.02 ? 317 ILE A C 1 ATOM 1828 O O . ILE A 1 236 ? 45.911 23.553 33.235 1.00 6.23 ? 317 ILE A O 1 ATOM 1829 C CB . ILE A 1 236 ? 43.205 24.992 33.517 1.00 6.74 ? 317 ILE A CB 1 ATOM 1830 C CG1 . ILE A 1 236 ? 42.030 25.803 32.959 1.00 7.26 ? 317 ILE A CG1 1 ATOM 1831 C CG2 . ILE A 1 236 ? 43.261 25.097 35.036 1.00 6.96 ? 317 ILE A CG2 1 ATOM 1832 C CD1 . ILE A 1 236 ? 40.669 25.362 33.461 1.00 4.55 ? 317 ILE A CD1 1 ATOM 1833 N N . CYS A 1 237 ? 46.535 25.458 34.258 1.00 7.88 ? 318 CYS A N 1 ATOM 1834 C CA . CYS A 1 237 ? 47.831 24.948 34.705 1.00 9.14 ? 318 CYS A CA 1 ATOM 1835 C C . CYS A 1 237 ? 47.762 23.990 35.895 1.00 11.73 ? 318 CYS A C 1 ATOM 1836 O O . CYS A 1 237 ? 48.689 23.212 36.124 1.00 11.69 ? 318 CYS A O 1 ATOM 1837 C CB . CYS A 1 237 ? 48.767 26.113 35.041 1.00 10.88 ? 318 CYS A CB 1 ATOM 1838 S SG . CYS A 1 237 ? 49.137 27.206 33.646 1.00 15.65 ? 318 CYS A SG 1 ATOM 1839 N N . SER A 1 238 ? 46.667 24.050 36.645 1.00 8.85 ? 319 SER A N 1 ATOM 1840 C CA . SER A 1 238 ? 46.542 23.286 37.884 1.00 9.71 ? 319 SER A CA 1 ATOM 1841 C C . SER A 1 238 ? 46.819 21.793 37.718 1.00 12.05 ? 319 SER A C 1 ATOM 1842 O O . SER A 1 238 ? 46.411 21.178 36.732 1.00 8.98 ? 319 SER A O 1 ATOM 1843 C CB . SER A 1 238 ? 45.153 23.484 38.495 1.00 12.61 ? 319 SER A CB 1 ATOM 1844 O OG . SER A 1 238 ? 45.005 22.718 39.678 1.00 11.34 ? 319 SER A OG 1 ATOM 1845 N N . GLY A 1 239 ? 47.509 21.220 38.700 1.00 12.30 ? 320 GLY A N 1 ATOM 1846 C CA . GLY A 1 239 ? 47.742 19.788 38.744 1.00 11.66 ? 320 GLY A CA 1 ATOM 1847 C C . GLY A 1 239 ? 46.478 19.049 39.143 1.00 16.66 ? 320 GLY A C 1 ATOM 1848 O O . GLY A 1 239 ? 46.430 17.816 39.145 1.00 13.47 ? 320 GLY A O 1 ATOM 1849 N N . ILE A 1 240 ? 45.452 19.815 39.504 1.00 9.77 ? 321 ILE A N 1 ATOM 1850 C CA . ILE A 1 240 ? 44.121 19.267 39.717 1.00 12.09 ? 321 ILE A CA 1 ATOM 1851 C C . ILE A 1 240 ? 43.452 19.147 38.350 1.00 10.45 ? 321 ILE A C 1 ATOM 1852 O O . ILE A 1 240 ? 42.704 20.035 37.947 1.00 12.61 ? 321 ILE A O 1 ATOM 1853 C CB . ILE A 1 240 ? 43.267 20.193 40.605 1.00 11.21 ? 321 ILE A CB 1 ATOM 1854 C CG1 . ILE A 1 240 ? 44.011 20.543 41.896 1.00 15.51 ? 321 ILE A CG1 1 ATOM 1855 C CG2 . ILE A 1 240 ? 41.925 19.546 40.905 1.00 9.87 ? 321 ILE A CG2 1 ATOM 1856 C CD1 . ILE A 1 240 ? 44.122 19.404 42.850 1.00 18.27 ? 321 ILE A CD1 1 ATOM 1857 N N . PHE A 1 241 ? 43.738 18.061 37.633 1.00 9.89 ? 322 PHE A N 1 ATOM 1858 C CA . PHE A 1 241 ? 43.268 17.897 36.256 1.00 12.27 ? 322 PHE A CA 1 ATOM 1859 C C . PHE A 1 241 ? 41.741 17.860 36.180 1.00 10.88 ? 322 PHE A C 1 ATOM 1860 O O . PHE A 1 241 ? 41.086 17.210 36.996 1.00 10.94 ? 322 PHE A O 1 ATOM 1861 C CB . PHE A 1 241 ? 43.878 16.643 35.626 1.00 11.42 ? 322 PHE A CB 1 ATOM 1862 C CG . PHE A 1 241 ? 45.378 16.568 35.755 1.00 12.88 ? 322 PHE A CG 1 ATOM 1863 C CD1 . PHE A 1 241 ? 46.185 17.562 35.219 1.00 11.56 ? 322 PHE A CD1 1 ATOM 1864 C CD2 . PHE A 1 241 ? 45.981 15.500 36.404 1.00 12.91 ? 322 PHE A CD2 1 ATOM 1865 C CE1 . PHE A 1 241 ? 47.565 17.494 35.336 1.00 11.16 ? 322 PHE A CE1 1 ATOM 1866 C CE2 . PHE A 1 241 ? 47.358 15.427 36.522 1.00 16.30 ? 322 PHE A CE2 1 ATOM 1867 C CZ . PHE A 1 241 ? 48.150 16.425 35.986 1.00 14.45 ? 322 PHE A CZ 1 ATOM 1868 N N . GLY A 1 242 ? 41.184 18.553 35.191 1.00 9.24 ? 323 GLY A N 1 ATOM 1869 C CA . GLY A 1 242 ? 39.750 18.764 35.127 1.00 9.08 ? 323 GLY A CA 1 ATOM 1870 C C . GLY A 1 242 ? 38.982 17.873 34.170 1.00 8.37 ? 323 GLY A C 1 ATOM 1871 O O . GLY A 1 242 ? 37.768 17.726 34.301 1.00 9.99 ? 323 GLY A O 1 ATOM 1872 N N . ASP A 1 243 ? 39.673 17.278 33.205 1.00 6.09 ? 324 ASP A N 1 ATOM 1873 C CA . ASP A 1 243 ? 38.993 16.468 32.201 1.00 7.71 ? 324 ASP A CA 1 ATOM 1874 C C . ASP A 1 243 ? 38.726 15.053 32.709 1.00 10.32 ? 324 ASP A C 1 ATOM 1875 O O . ASP A 1 243 ? 39.137 14.686 33.809 1.00 9.43 ? 324 ASP A O 1 ATOM 1876 C CB . ASP A 1 243 ? 39.796 16.427 30.897 1.00 9.39 ? 324 ASP A CB 1 ATOM 1877 C CG . ASP A 1 243 ? 38.919 16.208 29.673 1.00 13.21 ? 324 ASP A CG 1 ATOM 1878 O OD1 . ASP A 1 243 ? 37.693 16.032 29.825 1.00 6.64 ? 324 ASP A OD1 1 ATOM 1879 O OD2 . ASP A 1 243 ? 39.458 16.224 28.550 1.00 8.50 ? 324 ASP A OD2 1 ATOM 1880 N N . ASN A 1 244 ? 38.015 14.277 31.898 1.00 10.53 ? 325 ASN A N 1 ATOM 1881 C CA . ASN A 1 244 ? 37.754 12.873 32.174 1.00 10.73 ? 325 ASN A CA 1 ATOM 1882 C C . ASN A 1 244 ? 37.728 12.121 30.851 1.00 11.95 ? 325 ASN A C 1 ATOM 1883 O O . ASN A 1 244 ? 36.917 12.429 29.981 1.00 11.24 ? 325 ASN A O 1 ATOM 1884 C CB . ASN A 1 244 ? 36.418 12.705 32.899 1.00 10.13 ? 325 ASN A CB 1 ATOM 1885 C CG . ASN A 1 244 ? 36.113 11.256 33.229 1.00 14.27 ? 325 ASN A CG 1 ATOM 1886 O OD1 . ASN A 1 244 ? 35.497 10.542 32.438 1.00 16.26 ? 325 ASN A OD1 1 ATOM 1887 N ND2 . ASN A 1 244 ? 36.544 10.814 34.404 1.00 13.12 ? 325 ASN A ND2 1 ATOM 1888 N N . PRO A 1 245 ? 38.615 11.127 30.691 1.00 12.38 ? 326 PRO A N 1 ATOM 1889 C CA . PRO A 1 245 ? 39.546 10.631 31.710 1.00 12.91 ? 326 PRO A CA 1 ATOM 1890 C C . PRO A 1 245 ? 40.721 11.569 31.974 1.00 13.50 ? 326 PRO A C 1 ATOM 1891 O O . PRO A 1 245 ? 40.851 12.614 31.335 1.00 9.90 ? 326 PRO A O 1 ATOM 1892 C CB . PRO A 1 245 ? 40.058 9.328 31.094 1.00 14.07 ? 326 PRO A CB 1 ATOM 1893 C CG . PRO A 1 245 ? 40.007 9.580 29.633 1.00 16.68 ? 326 PRO A CG 1 ATOM 1894 C CD . PRO A 1 245 ? 38.765 10.403 29.417 1.00 14.44 ? 326 PRO A CD 1 ATOM 1895 N N . ARG A 1 246 ? 41.571 11.176 32.917 1.00 7.63 ? 327 ARG A N 1 ATOM 1896 C CA . ARG A 1 246 ? 42.710 11.980 33.335 1.00 8.36 ? 327 ARG A CA 1 ATOM 1897 C C . ARG A 1 246 ? 43.601 11.130 34.233 1.00 10.90 ? 327 ARG A C 1 ATOM 1898 O O . ARG A 1 246 ? 43.187 10.068 34.694 1.00 11.13 ? 327 ARG A O 1 ATOM 1899 C CB . ARG A 1 246 ? 42.235 13.210 34.110 1.00 9.32 ? 327 ARG A CB 1 ATOM 1900 C CG . ARG A 1 246 ? 41.517 12.872 35.408 1.00 8.76 ? 327 ARG A CG 1 ATOM 1901 C CD . ARG A 1 246 ? 41.147 14.116 36.204 1.00 7.35 ? 327 ARG A CD 1 ATOM 1902 N NE . ARG A 1 246 ? 40.512 13.766 37.472 1.00 6.47 ? 327 ARG A NE 1 ATOM 1903 C CZ . ARG A 1 246 ? 39.199 13.744 37.675 1.00 7.89 ? 327 ARG A CZ 1 ATOM 1904 N NH1 . ARG A 1 246 ? 38.365 14.069 36.694 1.00 6.92 ? 327 ARG A NH1 1 ATOM 1905 N NH2 . ARG A 1 246 ? 38.719 13.404 38.864 1.00 5.88 ? 327 ARG A NH2 1 ATOM 1906 N N . PRO A 1 247 ? 44.834 11.590 34.481 1.00 10.61 ? 328 PRO A N 1 ATOM 1907 C CA . PRO A 1 247 ? 45.704 10.907 35.442 1.00 12.37 ? 328 PRO A CA 1 ATOM 1908 C C . PRO A 1 247 ? 45.316 11.293 36.860 1.00 13.24 ? 328 PRO A C 1 ATOM 1909 O O . PRO A 1 247 ? 44.513 12.208 37.043 1.00 10.39 ? 328 PRO A O 1 ATOM 1910 C CB . PRO A 1 247 ? 47.093 11.485 35.135 1.00 12.56 ? 328 PRO A CB 1 ATOM 1911 C CG . PRO A 1 247 ? 46.950 12.253 33.854 1.00 15.68 ? 328 PRO A CG 1 ATOM 1912 C CD . PRO A 1 247 ? 45.528 12.689 33.796 1.00 12.77 ? 328 PRO A CD 1 ATOM 1913 N N . ASN A 1 248 ? 45.880 10.611 37.851 1.00 12.40 ? 329 ASN A N 1 ATOM 1914 C CA . ASN A 1 248 ? 45.767 11.070 39.229 1.00 15.01 ? 329 ASN A CA 1 ATOM 1915 C C . ASN A 1 248 ? 46.449 12.426 39.366 1.00 13.77 ? 329 ASN A C 1 ATOM 1916 O O . ASN A 1 248 ? 47.397 12.721 38.641 1.00 15.95 ? 329 ASN A O 1 ATOM 1917 C CB . ASN A 1 248 ? 46.393 10.060 40.190 1.00 16.03 ? 329 ASN A CB 1 ATOM 1918 C CG . ASN A 1 248 ? 45.532 8.826 40.382 1.00 23.28 ? 329 ASN A CG 1 ATOM 1919 O OD1 . ASN A 1 248 ? 44.370 8.923 40.775 1.00 19.27 ? 329 ASN A OD1 1 ATOM 1920 N ND2 . ASN A 1 248 ? 46.102 7.657 40.112 1.00 22.57 ? 329 ASN A ND2 1 ATOM 1921 N N . ASP A 1 249 ? 45.967 13.250 40.291 1.00 13.64 ? 330 ASP A N 1 ATOM 1922 C CA . ASP A 1 249 ? 46.512 14.593 40.476 1.00 12.34 ? 330 ASP A CA 1 ATOM 1923 C C . ASP A 1 249 ? 48.019 14.577 40.725 1.00 20.52 ? 330 ASP A C 1 ATOM 1924 O O . ASP A 1 249 ? 48.518 13.783 41.519 1.00 16.50 ? 330 ASP A O 1 ATOM 1925 C CB . ASP A 1 249 ? 45.799 15.312 41.622 1.00 14.08 ? 330 ASP A CB 1 ATOM 1926 C CG . ASP A 1 249 ? 44.346 15.612 41.308 1.00 16.02 ? 330 ASP A CG 1 ATOM 1927 O OD1 . ASP A 1 249 ? 43.979 15.597 40.114 1.00 13.73 ? 330 ASP A OD1 1 ATOM 1928 O OD2 . ASP A 1 249 ? 43.571 15.870 42.255 1.00 15.41 ? 330 ASP A OD2 1 ATOM 1929 N N . LYS A 1 250 ? 48.736 15.459 40.037 1.00 18.56 ? 331 LYS A N 1 ATOM 1930 C CA . LYS A 1 250 ? 50.179 15.587 40.212 1.00 20.34 ? 331 LYS A CA 1 ATOM 1931 C C . LYS A 1 250 ? 50.527 16.959 39.643 1.00 21.48 ? 331 LYS A C 1 ATOM 1932 O O . LYS A 1 250 ? 49.661 17.824 39.523 1.00 24.87 ? 331 LYS A O 1 ATOM 1933 C CB . LYS A 1 250 ? 50.920 14.546 39.371 1.00 19.32 ? 331 LYS A CB 1 ATOM 1934 C CG . LYS A 1 250 ? 50.499 14.504 37.910 1.00 23.50 ? 331 LYS A CG 1 ATOM 1935 C CD . LYS A 1 250 ? 51.248 13.419 37.149 1.00 33.82 ? 331 LYS A CD 1 ATOM 1936 C CE . LYS A 1 250 ? 50.736 13.290 35.721 1.00 40.22 ? 331 LYS A CE 1 ATOM 1937 N NZ . LYS A 1 250 ? 51.379 12.156 34.997 1.00 42.33 ? 331 LYS A NZ 1 ATOM 1938 N N . THR A 1 251 ? 51.796 17.161 39.302 1.00 18.34 ? 332 THR A N 1 ATOM 1939 C CA . THR A 1 251 ? 52.208 18.393 38.643 1.00 14.80 ? 332 THR A CA 1 ATOM 1940 C C . THR A 1 251 ? 51.582 18.666 37.281 1.00 15.19 ? 332 THR A C 1 ATOM 1941 O O . THR A 1 251 ? 51.681 17.845 36.372 1.00 17.05 ? 332 THR A O 1 ATOM 1942 C CB . THR A 1 251 ? 53.741 18.457 38.525 1.00 21.60 ? 332 THR A CB 1 ATOM 1943 O OG1 . THR A 1 251 ? 54.326 18.341 39.827 1.00 23.87 ? 332 THR A OG1 1 ATOM 1944 C CG2 . THR A 1 251 ? 54.168 19.776 37.901 1.00 16.80 ? 332 THR A CG2 1 ATOM 1945 N N . GLY A 1 252 ? 50.934 19.818 37.150 1.00 15.65 ? 333 GLY A N 1 ATOM 1946 C CA . GLY A 1 252 ? 50.234 20.162 35.926 1.00 14.42 ? 333 GLY A CA 1 ATOM 1947 C C . GLY A 1 252 ? 51.111 20.825 34.882 1.00 16.18 ? 333 GLY A C 1 ATOM 1948 O O . GLY A 1 252 ? 52.335 20.869 35.012 1.00 15.08 ? 333 GLY A O 1 ATOM 1949 N N . SER A 1 253 ? 50.473 21.341 33.839 1.00 14.24 ? 335 SER A N 1 ATOM 1950 C CA . SER A 1 253 ? 51.181 22.000 32.751 1.00 15.27 ? 335 SER A CA 1 ATOM 1951 C C . SER A 1 253 ? 50.328 23.110 32.155 1.00 14.65 ? 335 SER A C 1 ATOM 1952 O O . SER A 1 253 ? 49.102 23.008 32.118 1.00 14.46 ? 335 SER A O 1 ATOM 1953 C CB . SER A 1 253 ? 51.547 20.985 31.667 1.00 15.98 ? 335 SER A CB 1 ATOM 1954 O OG . SER A 1 253 ? 52.087 21.628 30.526 1.00 20.61 ? 335 SER A OG 1 ATOM 1955 N N . CYS A 1 254 ? 50.977 24.173 31.692 1.00 14.98 ? 336 CYS A N 1 ATOM 1956 C CA . CYS A 1 254 ? 50.262 25.260 31.036 1.00 19.30 ? 336 CYS A CA 1 ATOM 1957 C C . CYS A 1 254 ? 50.023 24.931 29.565 1.00 14.59 ? 336 CYS A C 1 ATOM 1958 O O . CYS A 1 254 ? 49.473 25.735 28.814 1.00 16.91 ? 336 CYS A O 1 ATOM 1959 C CB . CYS A 1 254 ? 51.011 26.583 31.201 1.00 18.47 ? 336 CYS A CB 1 ATOM 1960 S SG . CYS A 1 254 ? 51.035 27.185 32.912 1.00 37.63 ? 336 CYS A SG 1 ATOM 1961 N N . GLY A 1 255 ? 50.442 23.733 29.169 1.00 15.32 ? 339 GLY A N 1 ATOM 1962 C CA . GLY A 1 255 ? 50.130 23.194 27.858 1.00 16.19 ? 339 GLY A CA 1 ATOM 1963 C C . GLY A 1 255 ? 49.312 21.928 28.030 1.00 14.44 ? 339 GLY A C 1 ATOM 1964 O O . GLY A 1 255 ? 48.991 21.550 29.156 1.00 13.47 ? 339 GLY A O 1 ATOM 1965 N N . PRO A 1 256 ? 48.966 21.263 26.917 1.00 12.25 ? 340 PRO A N 1 ATOM 1966 C CA . PRO A 1 256 ? 48.158 20.039 27.001 1.00 11.95 ? 340 PRO A CA 1 ATOM 1967 C C . PRO A 1 256 ? 48.885 18.907 27.726 1.00 11.56 ? 340 PRO A C 1 ATOM 1968 O O . PRO A 1 256 ? 50.005 18.555 27.358 1.00 11.16 ? 340 PRO A O 1 ATOM 1969 C CB . PRO A 1 256 ? 47.925 19.664 25.531 1.00 10.73 ? 340 PRO A CB 1 ATOM 1970 C CG . PRO A 1 256 ? 48.955 20.412 24.758 1.00 12.85 ? 340 PRO A CG 1 ATOM 1971 C CD . PRO A 1 256 ? 49.236 21.661 25.525 1.00 10.29 ? 340 PRO A CD 1 ATOM 1972 N N . VAL A 1 257 ? 48.250 18.353 28.754 1.00 13.36 ? 341 VAL A N 1 ATOM 1973 C CA . VAL A 1 257 ? 48.799 17.209 29.472 1.00 11.85 ? 341 VAL A CA 1 ATOM 1974 C C . VAL A 1 257 ? 48.459 15.921 28.724 1.00 15.88 ? 341 VAL A C 1 ATOM 1975 O O . VAL A 1 257 ? 47.304 15.499 28.692 1.00 13.48 ? 341 VAL A O 1 ATOM 1976 C CB . VAL A 1 257 ? 48.250 17.133 30.910 1.00 15.49 ? 341 VAL A CB 1 ATOM 1977 C CG1 . VAL A 1 257 ? 48.735 15.867 31.603 1.00 15.72 ? 341 VAL A CG1 1 ATOM 1978 C CG2 . VAL A 1 257 ? 48.655 18.372 31.697 1.00 9.39 ? 341 VAL A CG2 1 ATOM 1979 N N . SER A 1 258 ? 49.472 15.300 28.127 1.00 12.11 ? 342 SER A N 1 ATOM 1980 C CA . SER A 1 258 ? 49.261 14.155 27.244 1.00 13.35 ? 342 SER A CA 1 ATOM 1981 C C . SER A 1 258 ? 48.762 12.894 27.954 1.00 13.05 ? 342 SER A C 1 ATOM 1982 O O . SER A 1 258 ? 48.005 12.110 27.378 1.00 13.01 ? 342 SER A O 1 ATOM 1983 C CB . SER A 1 258 ? 50.537 13.847 26.451 1.00 19.21 ? 342 SER A CB 1 ATOM 1984 O OG . SER A 1 258 ? 51.625 13.580 27.319 1.00 20.15 ? 342 SER A OG 1 ATOM 1985 N N . SER A 1 259 ? 49.186 12.694 29.197 1.00 13.36 ? 343 SER A N 1 ATOM 1986 C CA . SER A 1 259 ? 48.779 11.513 29.952 1.00 12.99 ? 343 SER A CA 1 ATOM 1987 C C . SER A 1 259 ? 47.257 11.411 30.046 1.00 15.38 ? 343 SER A C 1 ATOM 1988 O O . SER A 1 259 ? 46.602 12.308 30.577 1.00 12.66 ? 343 SER A O 1 ATOM 1989 C CB . SER A 1 259 ? 49.392 11.538 31.355 1.00 20.64 ? 343 SER A CB 1 ATOM 1990 O OG . SER A 1 259 ? 48.982 10.413 32.108 1.00 22.99 ? 343 SER A OG 1 ATOM 1991 N N . ASN A 1 260 ? 46.700 10.317 29.530 1.00 12.02 ? 344 ASN A N 1 ATOM 1992 C CA . ASN A 1 260 ? 45.251 10.117 29.514 1.00 14.15 ? 344 ASN A CA 1 ATOM 1993 C C . ASN A 1 260 ? 44.517 11.251 28.801 1.00 13.28 ? 344 ASN A C 1 ATOM 1994 O O . ASN A 1 260 ? 43.356 11.534 29.100 1.00 11.42 ? 344 ASN A O 1 ATOM 1995 C CB . ASN A 1 260 ? 44.708 9.976 30.938 1.00 13.42 ? 344 ASN A CB 1 ATOM 1996 C CG . ASN A 1 260 ? 45.326 8.812 31.686 1.00 18.29 ? 344 ASN A CG 1 ATOM 1997 O OD1 . ASN A 1 260 ? 46.251 8.990 32.478 1.00 21.21 ? 344 ASN A OD1 1 ATOM 1998 N ND2 . ASN A 1 260 ? 44.812 7.613 31.443 1.00 20.27 ? 344 ASN A ND2 1 ATOM 1999 N N . GLY A 1 261 ? 45.198 11.889 27.856 1.00 13.52 ? 345 GLY A N 1 ATOM 2000 C CA . GLY A 1 261 ? 44.675 13.072 27.198 1.00 13.81 ? 345 GLY A CA 1 ATOM 2001 C C . GLY A 1 261 ? 43.637 12.813 26.123 1.00 14.93 ? 345 GLY A C 1 ATOM 2002 O O . GLY A 1 261 ? 42.845 13.693 25.805 1.00 10.16 ? 345 GLY A O 1 ATOM 2003 N N . ALA A 1 262 ? 43.640 11.618 25.545 1.00 10.96 ? 346 ALA A N 1 ATOM 2004 C CA . ALA A 1 262 ? 42.648 11.284 24.525 1.00 13.20 ? 346 ALA A CA 1 ATOM 2005 C C . ALA A 1 262 ? 41.262 11.183 25.157 1.00 10.53 ? 346 ALA A C 1 ATOM 2006 O O . ALA A 1 262 ? 41.142 10.914 26.349 1.00 9.29 ? 346 ALA A O 1 ATOM 2007 C CB . ALA A 1 262 ? 43.015 9.988 23.831 1.00 15.10 ? 346 ALA A CB 1 ATOM 2008 N N . ASN A 1 263 ? 40.224 11.400 24.351 1.00 11.55 ? 347 ASN A N 1 ATOM 2009 C CA . ASN A 1 263 ? 38.840 11.365 24.822 1.00 13.07 ? 347 ASN A CA 1 ATOM 2010 C C . ASN A 1 263 ? 38.580 12.540 25.759 1.00 13.41 ? 347 ASN A C 1 ATOM 2011 O O . ASN A 1 263 ? 39.389 13.450 25.830 1.00 9.21 ? 347 ASN A O 1 ATOM 2012 C CB . ASN A 1 263 ? 38.536 10.032 25.511 1.00 14.48 ? 347 ASN A CB 1 ATOM 2013 C CG . ASN A 1 263 ? 37.054 9.702 25.524 1.00 27.39 ? 347 ASN A CG 1 ATOM 2014 O OD1 . ASN A 1 263 ? 36.217 10.518 25.138 1.00 24.14 ? 347 ASN A OD1 1 ATOM 2015 N ND2 . ASN A 1 263 ? 36.725 8.493 25.962 1.00 33.56 ? 347 ASN A ND2 1 ATOM 2016 N N . GLY A 1 264 ? 37.457 12.533 26.469 1.00 7.33 ? 348 GLY A N 1 ATOM 2017 C CA . GLY A 1 264 ? 37.160 13.619 27.386 1.00 7.56 ? 348 GLY A CA 1 ATOM 2018 C C . GLY A 1 264 ? 35.685 13.772 27.704 1.00 5.98 ? 348 GLY A C 1 ATOM 2019 O O . GLY A 1 264 ? 34.875 12.903 27.385 1.00 6.55 ? 348 GLY A O 1 ATOM 2020 N N . VAL A 1 265 ? 35.342 14.883 28.347 1.00 8.02 ? 349 VAL A N 1 ATOM 2021 C CA . VAL A 1 265 ? 33.953 15.192 28.670 1.00 6.93 ? 349 VAL A CA 1 ATOM 2022 C C . VAL A 1 265 ? 33.773 16.708 28.704 1.00 7.42 ? 349 VAL A C 1 ATOM 2023 O O . VAL A 1 265 ? 34.697 17.438 29.062 1.00 6.54 ? 349 VAL A O 1 ATOM 2024 C CB . VAL A 1 265 ? 33.532 14.577 30.028 1.00 7.32 ? 349 VAL A CB 1 ATOM 2025 C CG1 . VAL A 1 265 ? 34.276 15.244 31.180 1.00 6.64 ? 349 VAL A CG1 1 ATOM 2026 C CG2 . VAL A 1 265 ? 32.022 14.680 30.228 1.00 7.13 ? 349 VAL A CG2 1 ATOM 2027 N N . LYS A 1 266 ? 32.597 17.189 28.313 1.00 7.72 ? 350 LYS A N 1 ATOM 2028 C CA . LYS A 1 266 ? 32.325 18.618 28.416 1.00 5.98 ? 350 LYS A CA 1 ATOM 2029 C C . LYS A 1 266 ? 32.371 19.040 29.876 1.00 6.72 ? 350 LYS A C 1 ATOM 2030 O O . LYS A 1 266 ? 31.822 18.359 30.741 1.00 5.76 ? 350 LYS A O 1 ATOM 2031 C CB . LYS A 1 266 ? 30.965 18.983 27.818 1.00 7.41 ? 350 LYS A CB 1 ATOM 2032 C CG . LYS A 1 266 ? 30.604 20.455 28.012 1.00 5.85 ? 350 LYS A CG 1 ATOM 2033 C CD . LYS A 1 266 ? 29.240 20.794 27.429 1.00 8.12 ? 350 LYS A CD 1 ATOM 2034 C CE . LYS A 1 266 ? 28.841 22.225 27.764 1.00 7.48 ? 350 LYS A CE 1 ATOM 2035 N NZ . LYS A 1 266 ? 29.761 23.234 27.165 1.00 4.54 ? 350 LYS A NZ 1 ATOM 2036 N N . GLY A 1 267 ? 33.029 20.163 30.139 1.00 5.45 ? 351 GLY A N 1 ATOM 2037 C CA . GLY A 1 267 ? 33.139 20.694 31.483 1.00 8.23 ? 351 GLY A CA 1 ATOM 2038 C C . GLY A 1 267 ? 33.257 22.206 31.483 1.00 6.61 ? 351 GLY A C 1 ATOM 2039 O O . GLY A 1 267 ? 33.039 22.860 30.461 1.00 8.57 ? 351 GLY A O 1 ATOM 2040 N N . PHE A 1 268 ? 33.615 22.762 32.635 1.00 6.65 ? 352 PHE A N 1 ATOM 2041 C CA . PHE A 1 268 ? 33.699 24.202 32.802 1.00 5.82 ? 352 PHE A CA 1 ATOM 2042 C C . PHE A 1 268 ? 34.646 24.524 33.951 1.00 7.23 ? 352 PHE A C 1 ATOM 2043 O O . PHE A 1 268 ? 35.044 23.641 34.709 1.00 9.21 ? 352 PHE A O 1 ATOM 2044 C CB . PHE A 1 268 ? 32.317 24.762 33.139 1.00 6.23 ? 352 PHE A CB 1 ATOM 2045 C CG . PHE A 1 268 ? 31.868 24.436 34.535 1.00 7.20 ? 352 PHE A CG 1 ATOM 2046 C CD1 . PHE A 1 268 ? 31.223 23.241 34.808 1.00 6.26 ? 352 PHE A CD1 1 ATOM 2047 C CD2 . PHE A 1 268 ? 32.119 25.312 35.579 1.00 7.94 ? 352 PHE A CD2 1 ATOM 2048 C CE1 . PHE A 1 268 ? 30.823 22.933 36.097 1.00 6.70 ? 352 PHE A CE1 1 ATOM 2049 C CE2 . PHE A 1 268 ? 31.724 25.008 36.870 1.00 8.47 ? 352 PHE A CE2 1 ATOM 2050 C CZ . PHE A 1 268 ? 31.075 23.818 37.128 1.00 6.36 ? 352 PHE A CZ 1 ATOM 2051 N N . SER A 1 269 ? 34.993 25.799 34.074 1.00 4.94 ? 353 SER A N 1 ATOM 2052 C CA . SER A 1 269 ? 35.727 26.311 35.225 1.00 8.65 ? 353 SER A CA 1 ATOM 2053 C C . SER A 1 269 ? 35.530 27.819 35.288 1.00 7.92 ? 353 SER A C 1 ATOM 2054 O O . SER A 1 269 ? 35.317 28.455 34.257 1.00 6.55 ? 353 SER A O 1 ATOM 2055 C CB . SER A 1 269 ? 37.217 25.974 35.122 1.00 6.74 ? 353 SER A CB 1 ATOM 2056 O OG . SER A 1 269 ? 37.439 24.588 35.315 1.00 9.09 ? 353 SER A OG 1 ATOM 2057 N N . PHE A 1 270 ? 35.589 28.386 36.491 1.00 6.22 ? 354 PHE A N 1 ATOM 2058 C CA . PHE A 1 270 ? 35.461 29.831 36.660 1.00 6.33 ? 354 PHE A CA 1 ATOM 2059 C C . PHE A 1 270 ? 36.783 30.465 37.094 1.00 8.47 ? 354 PHE A C 1 ATOM 2060 O O . PHE A 1 270 ? 37.356 30.090 38.114 1.00 7.03 ? 354 PHE A O 1 ATOM 2061 C CB . PHE A 1 270 ? 34.359 30.174 37.668 1.00 7.24 ? 354 PHE A CB 1 ATOM 2062 C CG . PHE A 1 270 ? 32.967 29.877 37.177 1.00 7.05 ? 354 PHE A CG 1 ATOM 2063 C CD1 . PHE A 1 270 ? 32.405 30.625 36.155 1.00 7.53 ? 354 PHE A CD1 1 ATOM 2064 C CD2 . PHE A 1 270 ? 32.214 28.864 37.751 1.00 6.60 ? 354 PHE A CD2 1 ATOM 2065 C CE1 . PHE A 1 270 ? 31.121 30.359 35.704 1.00 8.41 ? 354 PHE A CE1 1 ATOM 2066 C CE2 . PHE A 1 270 ? 30.931 28.592 37.306 1.00 5.87 ? 354 PHE A CE2 1 ATOM 2067 C CZ . PHE A 1 270 ? 30.383 29.341 36.283 1.00 6.90 ? 354 PHE A CZ 1 ATOM 2068 N N . LYS A 1 271 ? 37.249 31.437 36.316 1.00 5.35 ? 355 LYS A N 1 ATOM 2069 C CA . LYS A 1 271 ? 38.508 32.118 36.589 1.00 4.90 ? 355 LYS A CA 1 ATOM 2070 C C . LYS A 1 271 ? 38.321 33.321 37.515 1.00 8.00 ? 355 LYS A C 1 ATOM 2071 O O . LYS A 1 271 ? 37.462 34.172 37.280 1.00 9.28 ? 355 LYS A O 1 ATOM 2072 C CB . LYS A 1 271 ? 39.152 32.571 35.274 1.00 7.91 ? 355 LYS A CB 1 ATOM 2073 C CG . LYS A 1 271 ? 40.452 33.346 35.436 1.00 7.79 ? 355 LYS A CG 1 ATOM 2074 C CD . LYS A 1 271 ? 40.973 33.826 34.088 1.00 11.02 ? 355 LYS A CD 1 ATOM 2075 C CE . LYS A 1 271 ? 42.357 34.462 34.203 1.00 13.59 ? 355 LYS A CE 1 ATOM 2076 N NZ . LYS A 1 271 ? 42.350 35.731 34.980 1.00 9.98 ? 355 LYS A NZ 1 ATOM 2077 N N . TYR A 1 272 ? 39.129 33.375 38.570 1.00 5.59 ? 356 TYR A N 1 ATOM 2078 C CA . TYR A 1 272 ? 39.192 34.537 39.450 1.00 9.65 ? 356 TYR A CA 1 ATOM 2079 C C . TYR A 1 272 ? 40.654 34.912 39.665 1.00 8.58 ? 356 TYR A C 1 ATOM 2080 O O . TYR A 1 272 ? 41.325 34.343 40.527 1.00 6.09 ? 356 TYR A O 1 ATOM 2081 C CB . TYR A 1 272 ? 38.542 34.238 40.801 1.00 10.61 ? 356 TYR A CB 1 ATOM 2082 C CG . TYR A 1 272 ? 37.040 34.070 40.754 1.00 10.19 ? 356 TYR A CG 1 ATOM 2083 C CD1 . TYR A 1 272 ? 36.472 32.836 40.475 1.00 6.66 ? 356 TYR A CD1 1 ATOM 2084 C CD2 . TYR A 1 272 ? 36.193 35.143 41.000 1.00 10.00 ? 356 TYR A CD2 1 ATOM 2085 C CE1 . TYR A 1 272 ? 35.099 32.674 40.434 1.00 6.43 ? 356 TYR A CE1 1 ATOM 2086 C CE2 . TYR A 1 272 ? 34.818 34.992 40.964 1.00 12.38 ? 356 TYR A CE2 1 ATOM 2087 C CZ . TYR A 1 272 ? 34.278 33.753 40.680 1.00 11.19 ? 356 TYR A CZ 1 ATOM 2088 O OH . TYR A 1 272 ? 32.912 33.587 40.644 1.00 12.73 ? 356 TYR A OH 1 ATOM 2089 N N . GLY A 1 273 ? 41.148 35.865 38.882 1.00 13.40 ? 357 GLY A N 1 ATOM 2090 C CA . GLY A 1 273 ? 42.558 36.210 38.923 1.00 14.28 ? 357 GLY A CA 1 ATOM 2091 C C . GLY A 1 273 ? 43.400 35.002 38.559 1.00 8.97 ? 357 GLY A C 1 ATOM 2092 O O . GLY A 1 273 ? 43.208 34.408 37.499 1.00 10.82 ? 357 GLY A O 1 ATOM 2093 N N . ASN A 1 274 ? 44.330 34.630 39.434 1.00 6.14 ? 358 ASN A N 1 ATOM 2094 C CA . ASN A 1 274 ? 45.148 33.440 39.207 1.00 7.01 ? 358 ASN A CA 1 ATOM 2095 C C . ASN A 1 274 ? 44.471 32.177 39.726 1.00 7.87 ? 358 ASN A C 1 ATOM 2096 O O . ASN A 1 274 ? 44.979 31.070 39.543 1.00 9.18 ? 358 ASN A O 1 ATOM 2097 C CB . ASN A 1 274 ? 46.530 33.594 39.850 1.00 9.56 ? 358 ASN A CB 1 ATOM 2098 C CG . ASN A 1 274 ? 47.335 34.717 39.234 1.00 13.47 ? 358 ASN A CG 1 ATOM 2099 O OD1 . ASN A 1 274 ? 47.202 35.877 39.623 1.00 14.11 ? 358 ASN A OD1 1 ATOM 2100 N ND2 . ASN A 1 274 ? 48.180 34.378 38.265 1.00 13.98 ? 358 ASN A ND2 1 ATOM 2101 N N . GLY A 1 275 ? 43.323 32.352 40.374 1.00 7.58 ? 359 GLY A N 1 ATOM 2102 C CA . GLY A 1 275 ? 42.592 31.241 40.955 1.00 6.81 ? 359 GLY A CA 1 ATOM 2103 C C . GLY A 1 275 ? 41.529 30.679 40.030 1.00 9.57 ? 359 GLY A C 1 ATOM 2104 O O . GLY A 1 275 ? 41.202 31.274 38.999 1.00 5.66 ? 359 GLY A O 1 ATOM 2105 N N . VAL A 1 276 ? 40.985 29.525 40.398 1.00 7.76 ? 360 VAL A N 1 ATOM 2106 C CA . VAL A 1 276 ? 39.992 28.868 39.561 1.00 4.13 ? 360 VAL A CA 1 ATOM 2107 C C . VAL A 1 276 ? 39.059 27.973 40.373 1.00 8.84 ? 360 VAL A C 1 ATOM 2108 O O . VAL A 1 276 ? 39.502 27.237 41.255 1.00 8.20 ? 360 VAL A O 1 ATOM 2109 C CB . VAL A 1 276 ? 40.672 28.037 38.452 1.00 6.37 ? 360 VAL A CB 1 ATOM 2110 C CG1 . VAL A 1 276 ? 41.561 26.962 39.058 1.00 6.68 ? 360 VAL A CG1 1 ATOM 2111 C CG2 . VAL A 1 276 ? 39.630 27.419 37.522 1.00 7.85 ? 360 VAL A CG2 1 ATOM 2112 N N . TRP A 1 277 ? 37.762 28.067 40.087 1.00 9.68 ? 361 TRP A N 1 ATOM 2113 C CA . TRP A 1 277 ? 36.793 27.099 40.584 1.00 9.23 ? 361 TRP A CA 1 ATOM 2114 C C . TRP A 1 277 ? 36.664 25.987 39.552 1.00 8.44 ? 361 TRP A C 1 ATOM 2115 O O . TRP A 1 277 ? 36.179 26.213 38.442 1.00 8.46 ? 361 TRP A O 1 ATOM 2116 C CB . TRP A 1 277 ? 35.426 27.750 40.801 1.00 8.59 ? 361 TRP A CB 1 ATOM 2117 C CG . TRP A 1 277 ? 35.191 28.277 42.184 1.00 7.73 ? 361 TRP A CG 1 ATOM 2118 C CD1 . TRP A 1 277 ? 35.154 29.587 42.566 1.00 7.38 ? 361 TRP A CD1 1 ATOM 2119 C CD2 . TRP A 1 277 ? 34.939 27.507 43.369 1.00 6.37 ? 361 TRP A CD2 1 ATOM 2120 N NE1 . TRP A 1 277 ? 34.899 29.681 43.912 1.00 9.11 ? 361 TRP A NE1 1 ATOM 2121 C CE2 . TRP A 1 277 ? 34.765 28.418 44.429 1.00 6.90 ? 361 TRP A CE2 1 ATOM 2122 C CE3 . TRP A 1 277 ? 34.849 26.136 43.635 1.00 7.11 ? 361 TRP A CE3 1 ATOM 2123 C CZ2 . TRP A 1 277 ? 34.504 28.006 45.734 1.00 7.67 ? 361 TRP A CZ2 1 ATOM 2124 C CZ3 . TRP A 1 277 ? 34.588 25.728 44.932 1.00 8.37 ? 361 TRP A CZ3 1 ATOM 2125 C CH2 . TRP A 1 277 ? 34.419 26.660 45.965 1.00 11.13 ? 361 TRP A CH2 1 ATOM 2126 N N . ILE A 1 278 ? 37.109 24.791 39.918 1.00 7.89 ? 362 ILE A N 1 ATOM 2127 C CA . ILE A 1 278 ? 37.104 23.657 39.007 1.00 8.93 ? 362 ILE A CA 1 ATOM 2128 C C . ILE A 1 278 ? 35.968 22.698 39.332 1.00 9.69 ? 362 ILE A C 1 ATOM 2129 O O . ILE A 1 278 ? 35.844 22.234 40.462 1.00 9.79 ? 362 ILE A O 1 ATOM 2130 C CB . ILE A 1 278 ? 38.437 22.882 39.079 1.00 9.56 ? 362 ILE A CB 1 ATOM 2131 C CG1 . ILE A 1 278 ? 39.586 23.745 38.558 1.00 11.63 ? 362 ILE A CG1 1 ATOM 2132 C CG2 . ILE A 1 278 ? 38.348 21.585 38.289 1.00 10.11 ? 362 ILE A CG2 1 ATOM 2133 C CD1 . ILE A 1 278 ? 40.957 23.138 38.786 1.00 16.51 ? 362 ILE A CD1 1 ATOM 2134 N N . GLY A 1 279 ? 35.132 22.418 38.338 1.00 8.08 ? 363 GLY A N 1 ATOM 2135 C CA . GLY A 1 279 ? 34.132 21.374 38.454 1.00 7.50 ? 363 GLY A CA 1 ATOM 2136 C C . GLY A 1 279 ? 34.614 20.160 37.685 1.00 8.15 ? 363 GLY A C 1 ATOM 2137 O O . GLY A 1 279 ? 35.039 20.285 36.538 1.00 9.98 ? 363 GLY A O 1 ATOM 2138 N N . ARG A 1 280 ? 34.573 18.988 38.310 1.00 5.30 ? 364 ARG A N 1 ATOM 2139 C CA . ARG A 1 280 ? 35.037 17.776 37.642 1.00 7.11 ? 364 ARG A CA 1 ATOM 2140 C C . ARG A 1 280 ? 34.411 16.518 38.226 1.00 8.05 ? 364 ARG A C 1 ATOM 2141 O O . ARG A 1 280 ? 33.842 16.541 39.317 1.00 5.86 ? 364 ARG A O 1 ATOM 2142 C CB . ARG A 1 280 ? 36.565 17.664 37.720 1.00 6.23 ? 364 ARG A CB 1 ATOM 2143 C CG . ARG A 1 280 ? 37.093 17.329 39.111 1.00 8.93 ? 364 ARG A CG 1 ATOM 2144 C CD . ARG A 1 280 ? 38.600 17.075 39.092 1.00 7.84 ? 364 ARG A CD 1 ATOM 2145 N NE . ARG A 1 280 ? 39.104 16.656 40.400 1.00 7.07 ? 364 ARG A NE 1 ATOM 2146 C CZ . ARG A 1 280 ? 40.372 16.341 40.648 1.00 9.90 ? 364 ARG A CZ 1 ATOM 2147 N NH1 . ARG A 1 280 ? 41.274 16.399 39.676 1.00 8.76 ? 364 ARG A NH1 1 ATOM 2148 N NH2 . ARG A 1 280 ? 40.738 15.970 41.868 1.00 11.04 ? 364 ARG A NH2 1 ATOM 2149 N N . THR A 1 281 ? 34.523 15.419 37.488 1.00 10.39 ? 365 THR A N 1 ATOM 2150 C CA . THR A 1 281 ? 34.096 14.121 37.987 1.00 10.52 ? 365 THR A CA 1 ATOM 2151 C C . THR A 1 281 ? 35.002 13.703 39.135 1.00 10.27 ? 365 THR A C 1 ATOM 2152 O O . THR A 1 281 ? 36.105 14.228 39.284 1.00 11.02 ? 365 THR A O 1 ATOM 2153 C CB . THR A 1 281 ? 34.172 13.042 36.893 1.00 12.23 ? 365 THR A CB 1 ATOM 2154 O OG1 . THR A 1 281 ? 35.539 12.844 36.511 1.00 11.76 ? 365 THR A OG1 1 ATOM 2155 C CG2 . THR A 1 281 ? 33.358 13.450 35.674 1.00 10.04 ? 365 THR A CG2 1 ATOM 2156 N N . LYS A 1 282 ? 34.535 12.761 39.947 1.00 10.62 ? 366 LYS A N 1 ATOM 2157 C CA . LYS A 1 282 ? 35.348 12.228 41.034 1.00 11.82 ? 366 LYS A CA 1 ATOM 2158 C C . LYS A 1 282 ? 36.238 11.086 40.551 1.00 12.07 ? 366 LYS A C 1 ATOM 2159 O O . LYS A 1 282 ? 37.355 10.915 41.037 1.00 14.30 ? 366 LYS A O 1 ATOM 2160 C CB . LYS A 1 282 ? 34.469 11.771 42.202 1.00 10.60 ? 366 LYS A CB 1 ATOM 2161 C CG . LYS A 1 282 ? 33.881 12.918 43.016 1.00 11.32 ? 366 LYS A CG 1 ATOM 2162 C CD . LYS A 1 282 ? 33.125 12.403 44.232 1.00 10.43 ? 366 LYS A CD 1 ATOM 2163 C CE . LYS A 1 282 ? 32.736 13.536 45.174 1.00 11.01 ? 366 LYS A CE 1 ATOM 2164 N NZ . LYS A 1 282 ? 33.934 14.167 45.807 1.00 12.97 ? 366 LYS A NZ 1 ATOM 2165 N N . SER A 1 283 ? 35.741 10.313 39.591 1.00 8.36 ? 367 SER A N 1 ATOM 2166 C CA . SER A 1 283 ? 36.520 9.233 38.992 1.00 12.55 ? 367 SER A CA 1 ATOM 2167 C C . SER A 1 283 ? 37.456 9.771 37.918 1.00 11.42 ? 367 SER A C 1 ATOM 2168 O O . SER A 1 283 ? 37.108 10.699 37.192 1.00 9.35 ? 367 SER A O 1 ATOM 2169 C CB . SER A 1 283 ? 35.597 8.179 38.380 1.00 12.90 ? 367 SER A CB 1 ATOM 2170 O OG . SER A 1 283 ? 36.326 7.285 37.556 1.00 15.41 ? 367 SER A OG 1 ATOM 2171 N N . ILE A 1 284 ? 38.645 9.187 37.815 1.00 13.49 ? 368 ILE A N 1 ATOM 2172 C CA . ILE A 1 284 ? 39.610 9.620 36.812 1.00 14.61 ? 368 ILE A CA 1 ATOM 2173 C C . ILE A 1 284 ? 39.440 8.864 35.498 1.00 11.83 ? 368 ILE A C 1 ATOM 2174 O O . ILE A 1 284 ? 40.038 9.227 34.485 1.00 13.74 ? 368 ILE A O 1 ATOM 2175 C CB . ILE A 1 284 ? 41.062 9.445 37.300 1.00 15.39 ? 368 ILE A CB 1 ATOM 2176 C CG1 . ILE A 1 284 ? 41.408 7.960 37.434 1.00 15.16 ? 368 ILE A CG1 1 ATOM 2177 C CG2 . ILE A 1 284 ? 41.281 10.182 38.616 1.00 14.61 ? 368 ILE A CG2 1 ATOM 2178 C CD1 . ILE A 1 284 ? 42.874 7.700 37.742 1.00 20.66 ? 368 ILE A CD1 1 ATOM 2179 N N . SER A 1 285 ? 38.620 7.817 35.512 1.00 11.10 ? 369 SER A N 1 ATOM 2180 C CA . SER A 1 285 ? 38.500 6.938 34.351 1.00 12.12 ? 369 SER A CA 1 ATOM 2181 C C . SER A 1 285 ? 37.093 6.896 33.758 1.00 18.07 ? 369 SER A C 1 ATOM 2182 O O . SER A 1 285 ? 36.920 6.622 32.569 1.00 14.80 ? 369 SER A O 1 ATOM 2183 C CB . SER A 1 285 ? 38.957 5.520 34.706 1.00 17.67 ? 369 SER A CB 1 ATOM 2184 O OG . SER A 1 285 ? 38.157 4.969 35.739 1.00 20.80 ? 369 SER A OG 1 ATOM 2185 N N . SER A 1 286 ? 36.090 7.165 34.586 1.00 14.35 ? 370 SER A N 1 ATOM 2186 C CA . SER A 1 286 ? 34.706 7.079 34.143 1.00 13.74 ? 370 SER A CA 1 ATOM 2187 C C . SER A 1 286 ? 33.920 8.323 34.542 1.00 11.18 ? 370 SER A C 1 ATOM 2188 O O . SER A 1 286 ? 34.348 9.091 35.402 1.00 11.10 ? 370 SER A O 1 ATOM 2189 C CB . SER A 1 286 ? 34.046 5.827 34.723 1.00 18.68 ? 370 SER A CB 1 ATOM 2190 O OG . SER A 1 286 ? 32.750 5.635 34.185 1.00 32.88 ? 370 SER A OG 1 ATOM 2191 N N . ARG A 1 287 ? 32.768 8.518 33.910 1.00 10.83 ? 371 ARG A N 1 ATOM 2192 C CA . ARG A 1 287 ? 31.922 9.666 34.211 1.00 11.63 ? 371 ARG A CA 1 ATOM 2193 C C . ARG A 1 287 ? 31.083 9.406 35.461 1.00 10.49 ? 371 ARG A C 1 ATOM 2194 O O . ARG A 1 287 ? 29.864 9.226 35.392 1.00 10.00 ? 371 ARG A O 1 ATOM 2195 C CB . ARG A 1 287 ? 31.051 10.020 33.003 1.00 8.81 ? 371 ARG A CB 1 ATOM 2196 C CG . ARG A 1 287 ? 31.876 10.472 31.801 1.00 7.10 ? 371 ARG A CG 1 ATOM 2197 C CD . ARG A 1 287 ? 31.039 10.658 30.544 1.00 10.88 ? 371 ARG A CD 1 ATOM 2198 N NE . ARG A 1 287 ? 31.848 11.182 29.445 1.00 8.33 ? 371 ARG A NE 1 ATOM 2199 C CZ . ARG A 1 287 ? 31.371 11.508 28.247 1.00 11.04 ? 371 ARG A CZ 1 ATOM 2200 N NH1 . ARG A 1 287 ? 30.081 11.361 27.981 1.00 8.88 ? 371 ARG A NH1 1 ATOM 2201 N NH2 . ARG A 1 287 ? 32.187 11.982 27.314 1.00 7.94 ? 371 ARG A NH2 1 ATOM 2202 N N . ASN A 1 288 ? 31.762 9.383 36.605 1.00 12.60 ? 372 ASN A N 1 ATOM 2203 C CA . ASN A 1 288 ? 31.125 9.138 37.892 1.00 10.55 ? 372 ASN A CA 1 ATOM 2204 C C . ASN A 1 288 ? 31.495 10.196 38.921 1.00 10.12 ? 372 ASN A C 1 ATOM 2205 O O . ASN A 1 288 ? 32.645 10.635 38.990 1.00 8.30 ? 372 ASN A O 1 ATOM 2206 C CB . ASN A 1 288 ? 31.503 7.754 38.424 1.00 14.45 ? 372 ASN A CB 1 ATOM 2207 C CG . ASN A 1 288 ? 30.856 6.632 37.641 1.00 20.14 ? 372 ASN A CG 1 ATOM 2208 O OD1 . ASN A 1 288 ? 29.748 6.197 37.958 1.00 23.06 ? 372 ASN A OD1 1 ATOM 2209 N ND2 . ASN A 1 288 ? 31.544 6.154 36.614 1.00 18.95 ? 372 ASN A ND2 1 ATOM 2210 N N . GLY A 1 289 ? 30.510 10.601 39.716 1.00 7.62 ? 373 GLY A N 1 ATOM 2211 C CA . GLY A 1 289 ? 30.723 11.579 40.766 1.00 7.10 ? 373 GLY A CA 1 ATOM 2212 C C . GLY A 1 289 ? 30.941 12.978 40.226 1.00 7.73 ? 373 GLY A C 1 ATOM 2213 O O . GLY A 1 289 ? 31.151 13.170 39.028 1.00 7.49 ? 373 GLY A O 1 ATOM 2214 N N . PHE A 1 290 ? 30.881 13.962 41.115 1.00 7.30 ? 374 PHE A N 1 ATOM 2215 C CA . PHE A 1 290 ? 31.171 15.336 40.736 1.00 6.31 ? 374 PHE A CA 1 ATOM 2216 C C . PHE A 1 290 ? 31.524 16.160 41.965 1.00 6.25 ? 374 PHE A C 1 ATOM 2217 O O . PHE A 1 290 ? 30.982 15.943 43.048 1.00 5.81 ? 374 PHE A O 1 ATOM 2218 C CB . PHE A 1 290 ? 29.991 15.966 39.992 1.00 5.07 ? 374 PHE A CB 1 ATOM 2219 C CG . PHE A 1 290 ? 30.381 17.133 39.129 1.00 6.06 ? 374 PHE A CG 1 ATOM 2220 C CD1 . PHE A 1 290 ? 30.848 16.931 37.840 1.00 5.96 ? 374 PHE A CD1 1 ATOM 2221 C CD2 . PHE A 1 290 ? 30.292 18.429 39.610 1.00 5.63 ? 374 PHE A CD2 1 ATOM 2222 C CE1 . PHE A 1 290 ? 31.214 17.999 37.043 1.00 7.25 ? 374 PHE A CE1 1 ATOM 2223 C CE2 . PHE A 1 290 ? 30.657 19.505 38.817 1.00 6.36 ? 374 PHE A CE2 1 ATOM 2224 C CZ . PHE A 1 290 ? 31.119 19.291 37.533 1.00 6.41 ? 374 PHE A CZ 1 ATOM 2225 N N . GLU A 1 291 ? 32.441 17.104 41.789 1.00 6.09 ? 375 GLU A N 1 ATOM 2226 C CA . GLU A 1 291 ? 32.921 17.914 42.900 1.00 7.67 ? 375 GLU A CA 1 ATOM 2227 C C . GLU A 1 291 ? 33.336 19.294 42.415 1.00 6.89 ? 375 GLU A C 1 ATOM 2228 O O . GLU A 1 291 ? 33.737 19.462 41.263 1.00 7.36 ? 375 GLU A O 1 ATOM 2229 C CB . GLU A 1 291 ? 34.103 17.225 43.591 1.00 7.50 ? 375 GLU A CB 1 ATOM 2230 C CG . GLU A 1 291 ? 35.313 17.004 42.687 1.00 11.01 ? 375 GLU A CG 1 ATOM 2231 C CD . GLU A 1 291 ? 36.360 16.104 43.320 1.00 16.03 ? 375 GLU A CD 1 ATOM 2232 O OE1 . GLU A 1 291 ? 36.106 15.579 44.424 1.00 13.51 ? 375 GLU A OE1 1 ATOM 2233 O OE2 . GLU A 1 291 ? 37.434 15.915 42.711 1.00 13.54 ? 375 GLU A OE2 1 ATOM 2234 N N . MET A 1 292 ? 33.223 20.281 43.298 1.00 6.04 ? 376 MET A N 1 ATOM 2235 C CA . MET A 1 292 ? 33.699 21.628 43.015 1.00 6.58 ? 376 MET A CA 1 ATOM 2236 C C . MET A 1 292 ? 34.935 21.903 43.856 1.00 11.27 ? 376 MET A C 1 ATOM 2237 O O . MET A 1 292 ? 34.927 21.693 45.067 1.00 8.95 ? 376 MET A O 1 ATOM 2238 C CB . MET A 1 292 ? 32.616 22.665 43.318 1.00 8.09 ? 376 MET A CB 1 ATOM 2239 C CG . MET A 1 292 ? 31.419 22.617 42.375 1.00 8.41 ? 376 MET A CG 1 ATOM 2240 S SD . MET A 1 292 ? 31.879 22.935 40.657 1.00 11.15 ? 376 MET A SD 1 ATOM 2241 C CE . MET A 1 292 ? 32.382 24.654 40.739 1.00 7.57 ? 376 MET A CE 1 ATOM 2242 N N . ILE A 1 293 ? 35.998 22.367 43.210 1.00 7.08 ? 377 ILE A N 1 ATOM 2243 C CA . ILE A 1 293 ? 37.256 22.611 43.901 1.00 8.36 ? 377 ILE A CA 1 ATOM 2244 C C . ILE A 1 293 ? 37.737 24.039 43.692 1.00 10.11 ? 377 ILE A C 1 ATOM 2245 O O . ILE A 1 293 ? 37.848 24.502 42.558 1.00 7.32 ? 377 ILE A O 1 ATOM 2246 C CB . ILE A 1 293 ? 38.350 21.643 43.423 1.00 9.01 ? 377 ILE A CB 1 ATOM 2247 C CG1 . ILE A 1 293 ? 37.968 20.201 43.762 1.00 11.19 ? 377 ILE A CG1 1 ATOM 2248 C CG2 . ILE A 1 293 ? 39.695 22.009 44.040 1.00 9.06 ? 377 ILE A CG2 1 ATOM 2249 C CD1 . ILE A 1 293 ? 38.929 19.170 43.224 1.00 16.85 ? 377 ILE A CD1 1 ATOM 2250 N N . TRP A 1 294 ? 38.010 24.735 44.791 1.00 6.55 ? 378 TRP A N 1 ATOM 2251 C CA . TRP A 1 294 ? 38.591 26.070 44.719 1.00 8.57 ? 378 TRP A CA 1 ATOM 2252 C C . TRP A 1 294 ? 40.107 25.992 44.831 1.00 9.00 ? 378 TRP A C 1 ATOM 2253 O O . TRP A 1 294 ? 40.649 25.570 45.854 1.00 11.04 ? 378 TRP A O 1 ATOM 2254 C CB . TRP A 1 294 ? 38.023 26.984 45.807 1.00 9.01 ? 378 TRP A CB 1 ATOM 2255 C CG . TRP A 1 294 ? 38.775 28.283 45.957 1.00 10.06 ? 378 TRP A CG 1 ATOM 2256 C CD1 . TRP A 1 294 ? 39.413 28.734 47.077 1.00 13.39 ? 378 TRP A CD1 1 ATOM 2257 C CD2 . TRP A 1 294 ? 38.970 29.289 44.952 1.00 10.34 ? 378 TRP A CD2 1 ATOM 2258 N NE1 . TRP A 1 294 ? 39.989 29.958 46.833 1.00 11.94 ? 378 TRP A NE1 1 ATOM 2259 C CE2 . TRP A 1 294 ? 39.732 30.321 45.537 1.00 13.45 ? 378 TRP A CE2 1 ATOM 2260 C CE3 . TRP A 1 294 ? 38.573 29.418 43.617 1.00 9.06 ? 378 TRP A CE3 1 ATOM 2261 C CZ2 . TRP A 1 294 ? 40.105 31.466 44.834 1.00 13.47 ? 378 TRP A CZ2 1 ATOM 2262 C CZ3 . TRP A 1 294 ? 38.945 30.557 42.919 1.00 9.37 ? 378 TRP A CZ3 1 ATOM 2263 C CH2 . TRP A 1 294 ? 39.704 31.564 43.529 1.00 11.24 ? 378 TRP A CH2 1 ATOM 2264 N N . ASP A 1 295 ? 40.783 26.397 43.764 1.00 8.79 ? 379 ASP A N 1 ATOM 2265 C CA . ASP A 1 295 ? 42.237 26.380 43.721 1.00 8.86 ? 379 ASP A CA 1 ATOM 2266 C C . ASP A 1 295 ? 42.763 27.792 43.466 1.00 8.28 ? 379 ASP A C 1 ATOM 2267 O O . ASP A 1 295 ? 42.810 28.245 42.325 1.00 5.80 ? 379 ASP A O 1 ATOM 2268 C CB . ASP A 1 295 ? 42.715 25.418 42.637 1.00 7.82 ? 379 ASP A CB 1 ATOM 2269 C CG . ASP A 1 295 ? 44.217 25.313 42.583 1.00 12.65 ? 379 ASP A CG 1 ATOM 2270 O OD1 . ASP A 1 295 ? 44.874 26.081 43.312 1.00 11.36 ? 379 ASP A OD1 1 ATOM 2271 O OD2 . ASP A 1 295 ? 44.736 24.472 41.821 1.00 15.95 ? 379 ASP A OD2 1 ATOM 2272 N N . PRO A 1 296 ? 43.170 28.487 44.540 1.00 9.49 ? 380 PRO A N 1 ATOM 2273 C CA . PRO A 1 296 ? 43.498 29.921 44.533 1.00 10.62 ? 380 PRO A CA 1 ATOM 2274 C C . PRO A 1 296 ? 44.611 30.345 43.566 1.00 7.65 ? 380 PRO A C 1 ATOM 2275 O O . PRO A 1 296 ? 44.718 31.535 43.272 1.00 10.66 ? 380 PRO A O 1 ATOM 2276 C CB . PRO A 1 296 ? 43.918 30.199 45.984 1.00 12.00 ? 380 PRO A CB 1 ATOM 2277 C CG . PRO A 1 296 ? 44.203 28.859 46.579 1.00 14.98 ? 380 PRO A CG 1 ATOM 2278 C CD . PRO A 1 296 ? 43.297 27.902 45.885 1.00 11.84 ? 380 PRO A CD 1 ATOM 2279 N N . ASN A 1 297 ? 45.429 29.412 43.091 1.00 6.55 ? 381 ASN A N 1 ATOM 2280 C CA . ASN A 1 297 ? 46.418 29.749 42.066 1.00 8.99 ? 381 ASN A CA 1 ATOM 2281 C C . ASN A 1 297 ? 46.433 28.732 40.929 1.00 10.82 ? 381 ASN A C 1 ATOM 2282 O O . ASN A 1 297 ? 47.434 28.582 40.230 1.00 12.32 ? 381 ASN A O 1 ATOM 2283 C CB . ASN A 1 297 ? 47.817 29.886 42.671 1.00 10.42 ? 381 ASN A CB 1 ATOM 2284 C CG . ASN A 1 297 ? 48.423 28.550 43.035 1.00 14.52 ? 381 ASN A CG 1 ATOM 2285 O OD1 . ASN A 1 297 ? 47.713 27.561 43.167 1.00 10.06 ? 381 ASN A OD1 1 ATOM 2286 N ND2 . ASN A 1 297 ? 49.739 28.513 43.201 1.00 22.68 ? 381 ASN A ND2 1 ATOM 2287 N N . GLY A 1 298 ? 45.311 28.044 40.744 1.00 7.06 ? 382 GLY A N 1 ATOM 2288 C CA . GLY A 1 298 ? 45.228 26.958 39.785 1.00 8.32 ? 382 GLY A CA 1 ATOM 2289 C C . GLY A 1 298 ? 45.139 27.356 38.323 1.00 8.04 ? 382 GLY A C 1 ATOM 2290 O O . GLY A 1 298 ? 45.348 26.523 37.445 1.00 7.77 ? 382 GLY A O 1 ATOM 2291 N N . TRP A 1 299 ? 44.823 28.615 38.041 1.00 8.01 ? 383 TRP A N 1 ATOM 2292 C CA . TRP A 1 299 ? 44.748 29.044 36.648 1.00 7.68 ? 383 TRP A CA 1 ATOM 2293 C C . TRP A 1 299 ? 46.138 29.068 36.021 1.00 12.55 ? 383 TRP A C 1 ATOM 2294 O O . TRP A 1 299 ? 46.313 28.684 34.863 1.00 10.38 ? 383 TRP A O 1 ATOM 2295 C CB . TRP A 1 299 ? 44.085 30.415 36.520 1.00 9.48 ? 383 TRP A CB 1 ATOM 2296 C CG . TRP A 1 299 ? 43.714 30.759 35.103 1.00 9.83 ? 383 TRP A CG 1 ATOM 2297 C CD1 . TRP A 1 299 ? 44.429 31.529 34.229 1.00 8.44 ? 383 TRP A CD1 1 ATOM 2298 C CD2 . TRP A 1 299 ? 42.540 30.336 34.398 1.00 8.65 ? 383 TRP A CD2 1 ATOM 2299 N NE1 . TRP A 1 299 ? 43.768 31.614 33.025 1.00 12.34 ? 383 TRP A NE1 1 ATOM 2300 C CE2 . TRP A 1 299 ? 42.607 30.889 33.103 1.00 11.15 ? 383 TRP A CE2 1 ATOM 2301 C CE3 . TRP A 1 299 ? 41.437 29.545 34.738 1.00 7.76 ? 383 TRP A CE3 1 ATOM 2302 C CZ2 . TRP A 1 299 ? 41.613 30.678 32.148 1.00 8.55 ? 383 TRP A CZ2 1 ATOM 2303 C CZ3 . TRP A 1 299 ? 40.451 29.335 33.786 1.00 13.40 ? 383 TRP A CZ3 1 ATOM 2304 C CH2 . TRP A 1 299 ? 40.547 29.900 32.508 1.00 10.40 ? 383 TRP A CH2 1 ATOM 2305 N N . THR A 1 300 ? 47.125 29.503 36.799 1.00 9.45 ? 384 THR A N 1 ATOM 2306 C CA . THR A 1 300 ? 48.482 29.681 36.290 1.00 11.05 ? 384 THR A CA 1 ATOM 2307 C C . THR A 1 300 ? 49.533 28.846 37.024 1.00 16.04 ? 384 THR A C 1 ATOM 2308 O O . THR A 1 300 ? 50.674 28.745 36.570 1.00 15.37 ? 384 THR A O 1 ATOM 2309 C CB . THR A 1 300 ? 48.906 31.161 36.357 1.00 16.01 ? 384 THR A CB 1 ATOM 2310 O OG1 . THR A 1 300 ? 48.772 31.633 37.704 1.00 14.09 ? 384 THR A OG1 1 ATOM 2311 C CG2 . THR A 1 300 ? 48.035 32.008 35.443 1.00 12.89 ? 384 THR A CG2 1 ATOM 2312 N N . GLY A 1 301 ? 49.154 28.258 38.156 1.00 9.15 ? 385 GLY A N 1 ATOM 2313 C CA . GLY A 1 301 ? 50.073 27.459 38.951 1.00 12.49 ? 385 GLY A CA 1 ATOM 2314 C C . GLY A 1 301 ? 49.906 25.969 38.712 1.00 13.80 ? 385 GLY A C 1 ATOM 2315 O O . GLY A 1 301 ? 48.791 25.489 38.518 1.00 11.16 ? 385 GLY A O 1 ATOM 2316 N N . THR A 1 302 ? 51.012 25.231 38.746 1.00 10.92 ? 386 THR A N 1 ATOM 2317 C CA . THR A 1 302 ? 50.999 23.825 38.341 1.00 13.54 ? 386 THR A CA 1 ATOM 2318 C C . THR A 1 302 ? 50.948 22.813 39.487 1.00 17.90 ? 386 THR A C 1 ATOM 2319 O O . THR A 1 302 ? 50.900 21.606 39.247 1.00 15.78 ? 386 THR A O 1 ATOM 2320 C CB . THR A 1 302 ? 52.205 23.490 37.438 1.00 15.00 ? 386 THR A CB 1 ATOM 2321 O OG1 . THR A 1 302 ? 53.421 23.778 38.138 1.00 12.51 ? 386 THR A OG1 1 ATOM 2322 C CG2 . THR A 1 302 ? 52.154 24.309 36.157 1.00 15.69 ? 386 THR A CG2 1 ATOM 2323 N N . ASP A 1 303 ? 50.961 23.290 40.727 1.00 17.11 ? 387 ASP A N 1 ATOM 2324 C CA . ASP A 1 303 ? 50.899 22.380 41.865 1.00 19.49 ? 387 ASP A CA 1 ATOM 2325 C C . ASP A 1 303 ? 49.502 21.776 41.994 1.00 16.05 ? 387 ASP A C 1 ATOM 2326 O O . ASP A 1 303 ? 48.572 22.198 41.306 1.00 14.37 ? 387 ASP A O 1 ATOM 2327 C CB . ASP A 1 303 ? 51.311 23.088 43.158 1.00 16.78 ? 387 ASP A CB 1 ATOM 2328 C CG . ASP A 1 303 ? 50.285 24.099 43.622 1.00 18.82 ? 387 ASP A CG 1 ATOM 2329 O OD1 . ASP A 1 303 ? 49.274 23.678 44.217 1.00 20.60 ? 387 ASP A OD1 1 ATOM 2330 O OD2 . ASP A 1 303 ? 50.490 25.310 43.404 1.00 16.95 ? 387 ASP A OD2 1 ATOM 2331 N N . ASN A 1 304 ? 49.360 20.781 42.865 1.00 16.56 ? 388 ASN A N 1 ATOM 2332 C CA . ASN A 1 304 ? 48.074 20.115 43.053 1.00 17.71 ? 388 ASN A CA 1 ATOM 2333 C C . ASN A 1 304 ? 47.439 20.385 44.415 1.00 18.80 ? 388 ASN A C 1 ATOM 2334 O O . ASN A 1 304 ? 46.604 19.612 44.882 1.00 18.16 ? 388 ASN A O 1 ATOM 2335 C CB . ASN A 1 304 ? 48.196 18.606 42.816 1.00 17.40 ? 388 ASN A CB 1 ATOM 2336 C CG . ASN A 1 304 ? 49.166 17.939 43.772 1.00 28.67 ? 388 ASN A CG 1 ATOM 2337 O OD1 . ASN A 1 304 ? 49.838 18.604 44.560 1.00 34.22 ? 388 ASN A OD1 1 ATOM 2338 N ND2 . ASN A 1 304 ? 49.242 16.615 43.707 1.00 26.45 ? 388 ASN A ND2 1 ATOM 2339 N N . ASN A 1 305 ? 47.839 21.480 45.049 1.00 12.91 ? 389 ASN A N 1 ATOM 2340 C CA . ASN A 1 305 ? 47.232 21.884 46.310 1.00 13.16 ? 389 ASN A CA 1 ATOM 2341 C C . ASN A 1 305 ? 45.959 22.678 46.041 1.00 15.79 ? 389 ASN A C 1 ATOM 2342 O O . ASN A 1 305 ? 45.875 23.395 45.053 1.00 14.17 ? 389 ASN A O 1 ATOM 2343 C CB . ASN A 1 305 ? 48.212 22.723 47.129 1.00 17.10 ? 389 ASN A CB 1 ATOM 2344 C CG . ASN A 1 305 ? 49.509 21.986 47.423 1.00 23.04 ? 389 ASN A CG 1 ATOM 2345 O OD1 . ASN A 1 305 ? 50.517 22.598 47.774 1.00 36.92 ? 389 ASN A OD1 1 ATOM 2346 N ND2 . ASN A 1 305 ? 49.489 20.667 47.275 1.00 27.13 ? 389 ASN A ND2 1 ATOM 2347 N N . PHE A 1 306 ? 44.963 22.537 46.907 1.00 12.11 ? 390 PHE A N 1 ATOM 2348 C CA . PHE A 1 306 ? 43.733 23.313 46.775 1.00 11.21 ? 390 PHE A CA 1 ATOM 2349 C C . PHE A 1 306 ? 43.179 23.682 48.148 1.00 15.15 ? 390 PHE A C 1 ATOM 2350 O O . PHE A 1 306 ? 43.589 23.114 49.157 1.00 13.61 ? 390 PHE A O 1 ATOM 2351 C CB . PHE A 1 306 ? 42.693 22.551 45.951 1.00 14.74 ? 390 PHE A CB 1 ATOM 2352 C CG . PHE A 1 306 ? 42.324 21.217 46.528 1.00 12.50 ? 390 PHE A CG 1 ATOM 2353 C CD1 . PHE A 1 306 ? 41.276 21.102 47.427 1.00 13.88 ? 390 PHE A CD1 1 ATOM 2354 C CD2 . PHE A 1 306 ? 43.026 20.076 46.173 1.00 17.62 ? 390 PHE A CD2 1 ATOM 2355 C CE1 . PHE A 1 306 ? 40.935 19.875 47.961 1.00 17.90 ? 390 PHE A CE1 1 ATOM 2356 C CE2 . PHE A 1 306 ? 42.689 18.845 46.703 1.00 20.28 ? 390 PHE A CE2 1 ATOM 2357 C CZ . PHE A 1 306 ? 41.641 18.745 47.599 1.00 19.18 ? 390 PHE A CZ 1 ATOM 2358 N N . SER A 1 307 ? 42.245 24.629 48.181 1.00 11.11 ? 391 SER A N 1 ATOM 2359 C CA . SER A 1 307 ? 41.755 25.177 49.443 1.00 8.99 ? 391 SER A CA 1 ATOM 2360 C C . SER A 1 307 ? 40.368 24.680 49.847 1.00 14.98 ? 391 SER A C 1 ATOM 2361 O O . SER A 1 307 ? 40.094 24.489 51.033 1.00 16.37 ? 391 SER A O 1 ATOM 2362 C CB . SER A 1 307 ? 41.754 26.705 49.392 1.00 11.75 ? 391 SER A CB 1 ATOM 2363 O OG . SER A 1 307 ? 43.067 27.203 49.202 1.00 17.94 ? 391 SER A OG 1 ATOM 2364 N N . ILE A 1 308 ? 39.491 24.486 48.867 1.00 12.08 ? 392 ILE A N 1 ATOM 2365 C CA . ILE A 1 308 ? 38.122 24.072 49.150 1.00 12.62 ? 392 ILE A CA 1 ATOM 2366 C C . ILE A 1 308 ? 37.673 22.961 48.215 1.00 14.00 ? 392 ILE A C 1 ATOM 2367 O O . ILE A 1 308 ? 37.948 23.000 47.015 1.00 12.25 ? 392 ILE A O 1 ATOM 2368 C CB . ILE A 1 308 ? 37.132 25.245 48.995 1.00 15.88 ? 392 ILE A CB 1 ATOM 2369 C CG1 . ILE A 1 308 ? 37.577 26.446 49.829 1.00 20.12 ? 392 ILE A CG1 1 ATOM 2370 C CG2 . ILE A 1 308 ? 35.721 24.814 49.382 1.00 17.80 ? 392 ILE A CG2 1 ATOM 2371 C CD1 . ILE A 1 308 ? 36.689 27.659 49.660 1.00 17.57 ? 392 ILE A CD1 1 ATOM 2372 N N . LYS A 1 309 ? 36.986 21.968 48.769 1.00 8.82 ? 394 LYS A N 1 ATOM 2373 C CA . LYS A 1 309 ? 36.313 20.963 47.958 1.00 9.73 ? 394 LYS A CA 1 ATOM 2374 C C . LYS A 1 309 ? 34.883 20.772 48.447 1.00 12.68 ? 394 LYS A C 1 ATOM 2375 O O . LYS A 1 309 ? 34.645 20.620 49.645 1.00 12.43 ? 394 LYS A O 1 ATOM 2376 C CB . LYS A 1 309 ? 37.060 19.626 47.987 1.00 13.18 ? 394 LYS A CB 1 ATOM 2377 C CG . LYS A 1 309 ? 36.286 18.504 47.305 1.00 15.01 ? 394 LYS A CG 1 ATOM 2378 C CD . LYS A 1 309 ? 36.983 17.156 47.424 1.00 21.87 ? 394 LYS A CD 1 ATOM 2379 C CE . LYS A 1 309 ? 38.129 17.036 46.441 1.00 23.04 ? 394 LYS A CE 1 ATOM 2380 N NZ . LYS A 1 309 ? 38.519 15.615 46.230 1.00 33.84 ? 394 LYS A NZ 1 ATOM 2381 N N . GLN A 1 310 ? 33.933 20.793 47.519 1.00 10.29 ? 395 GLN A N 1 ATOM 2382 C CA . GLN A 1 310 ? 32.535 20.556 47.857 1.00 8.91 ? 395 GLN A CA 1 ATOM 2383 C C . GLN A 1 310 ? 31.973 19.415 47.019 1.00 10.44 ? 395 GLN A C 1 ATOM 2384 O O . GLN A 1 310 ? 32.004 19.465 45.786 1.00 8.04 ? 395 GLN A O 1 ATOM 2385 C CB . GLN A 1 310 ? 31.704 21.826 47.643 1.00 11.01 ? 395 GLN A CB 1 ATOM 2386 C CG . GLN A 1 310 ? 30.237 21.673 48.028 1.00 6.96 ? 395 GLN A CG 1 ATOM 2387 C CD . GLN A 1 310 ? 29.411 22.910 47.721 1.00 11.46 ? 395 GLN A CD 1 ATOM 2388 O OE1 . GLN A 1 310 ? 29.950 23.998 47.509 1.00 9.81 ? 395 GLN A OE1 1 ATOM 2389 N NE2 . GLN A 1 310 ? 28.094 22.749 47.701 1.00 10.60 ? 395 GLN A NE2 1 ATOM 2390 N N . ASP A 1 311 ? 31.463 18.387 47.692 1.00 8.98 ? 396 ASP A N 1 ATOM 2391 C CA . ASP A 1 311 ? 30.863 17.241 47.014 1.00 9.23 ? 396 ASP A CA 1 ATOM 2392 C C . ASP A 1 311 ? 29.531 17.612 46.367 1.00 8.37 ? 396 ASP A C 1 ATOM 2393 O O . ASP A 1 311 ? 28.718 18.327 46.959 1.00 7.76 ? 396 ASP A O 1 ATOM 2394 C CB . ASP A 1 311 ? 30.655 16.085 47.992 1.00 11.65 ? 396 ASP A CB 1 ATOM 2395 C CG . ASP A 1 311 ? 31.958 15.473 48.459 1.00 17.34 ? 396 ASP A CG 1 ATOM 2396 O OD1 . ASP A 1 311 ? 33.008 15.760 47.846 1.00 16.71 ? 396 ASP A OD1 1 ATOM 2397 O OD2 . ASP A 1 311 ? 31.928 14.701 49.440 1.00 27.67 ? 396 ASP A OD2 1 ATOM 2398 N N . ILE A 1 312 ? 29.315 17.111 45.155 1.00 6.74 ? 397 ILE A N 1 ATOM 2399 C CA . ILE A 1 312 ? 28.095 17.383 44.404 1.00 6.79 ? 397 ILE A CA 1 ATOM 2400 C C . ILE A 1 312 ? 27.370 16.084 44.056 1.00 7.86 ? 397 ILE A C 1 ATOM 2401 O O . ILE A 1 312 ? 26.155 15.972 44.229 1.00 6.53 ? 397 ILE A O 1 ATOM 2402 C CB . ILE A 1 312 ? 28.404 18.154 43.110 1.00 6.61 ? 397 ILE A CB 1 ATOM 2403 C CG1 . ILE A 1 312 ? 29.094 19.482 43.437 1.00 6.22 ? 397 ILE A CG1 1 ATOM 2404 C CG2 . ILE A 1 312 ? 27.130 18.388 42.312 1.00 6.68 ? 397 ILE A CG2 1 ATOM 2405 C CD1 . ILE A 1 312 ? 28.224 20.451 44.213 1.00 8.16 ? 397 ILE A CD1 1 ATOM 2406 N N . VAL A 1 313 ? 28.128 15.112 43.555 1.00 6.27 ? 398 VAL A N 1 ATOM 2407 C CA . VAL A 1 313 ? 27.608 13.783 43.253 1.00 6.45 ? 398 VAL A CA 1 ATOM 2408 C C . VAL A 1 313 ? 28.607 12.736 43.743 1.00 7.21 ? 398 VAL A C 1 ATOM 2409 O O . VAL A 1 313 ? 29.804 12.851 43.486 1.00 6.97 ? 398 VAL A O 1 ATOM 2410 C CB . VAL A 1 313 ? 27.370 13.597 41.737 1.00 5.30 ? 398 VAL A CB 1 ATOM 2411 C CG1 . VAL A 1 313 ? 27.000 12.152 41.424 1.00 7.99 ? 398 VAL A CG1 1 ATOM 2412 C CG2 . VAL A 1 313 ? 26.290 14.553 41.241 1.00 7.40 ? 398 VAL A CG2 1 ATOM 2413 N N . GLY A 1 314 ? 28.116 11.725 44.455 1.00 6.28 ? 399 GLY A N 1 ATOM 2414 C CA . GLY A 1 314 ? 28.970 10.688 45.012 1.00 9.02 ? 399 GLY A CA 1 ATOM 2415 C C . GLY A 1 314 ? 29.764 9.933 43.962 1.00 9.57 ? 399 GLY A C 1 ATOM 2416 O O . GLY A 1 314 ? 29.332 9.807 42.819 1.00 8.23 ? 399 GLY A O 1 ATOM 2417 N N . ILE A 1 315 ? 30.926 9.414 44.350 1.00 10.85 ? 400 ILE A N 1 ATOM 2418 C CA . ILE A 1 315 ? 31.821 8.763 43.396 1.00 12.26 ? 400 ILE A CA 1 ATOM 2419 C C . ILE A 1 315 ? 31.211 7.510 42.761 1.00 14.96 ? 400 ILE A C 1 ATOM 2420 O O . ILE A 1 315 ? 31.572 7.135 41.646 1.00 18.16 ? 400 ILE A O 1 ATOM 2421 C CB . ILE A 1 315 ? 33.179 8.406 44.036 1.00 16.01 ? 400 ILE A CB 1 ATOM 2422 C CG1 . ILE A 1 315 ? 34.185 7.996 42.956 1.00 20.66 ? 400 ILE A CG1 1 ATOM 2423 C CG2 . ILE A 1 315 ? 33.006 7.311 45.077 1.00 18.01 ? 400 ILE A CG2 1 ATOM 2424 C CD1 . ILE A 1 315 ? 35.574 7.713 43.487 1.00 28.49 ? 400 ILE A CD1 1 ATOM 2425 N N . ASN A 1 316 ? 30.287 6.871 43.472 1.00 12.92 ? 401 ASN A N 1 ATOM 2426 C CA . ASN A 1 316 ? 29.633 5.667 42.968 1.00 20.50 ? 401 ASN A CA 1 ATOM 2427 C C . ASN A 1 316 ? 28.378 5.970 42.153 1.00 19.45 ? 401 ASN A C 1 ATOM 2428 O O . ASN A 1 316 ? 27.649 5.058 41.765 1.00 21.96 ? 401 ASN A O 1 ATOM 2429 C CB . ASN A 1 316 ? 29.278 4.727 44.122 1.00 26.38 ? 401 ASN A CB 1 ATOM 2430 C CG . ASN A 1 316 ? 30.501 4.168 44.820 1.00 31.86 ? 401 ASN A CG 1 ATOM 2431 O OD1 . ASN A 1 316 ? 30.492 3.952 46.032 1.00 39.52 ? 401 ASN A OD1 1 ATOM 2432 N ND2 . ASN A 1 316 ? 31.563 3.933 44.058 1.00 29.05 ? 401 ASN A ND2 1 ATOM 2433 N N . GLU A 1 317 ? 28.127 7.250 41.900 1.00 12.62 ? 402 GLU A N 1 ATOM 2434 C CA . GLU A 1 317 ? 26.938 7.664 41.162 1.00 9.77 ? 402 GLU A CA 1 ATOM 2435 C C . GLU A 1 317 ? 27.307 8.224 39.790 1.00 11.81 ? 402 GLU A C 1 ATOM 2436 O O . GLU A 1 317 ? 28.386 8.787 39.609 1.00 10.08 ? 402 GLU A O 1 ATOM 2437 C CB . GLU A 1 317 ? 26.154 8.710 41.957 1.00 10.78 ? 402 GLU A CB 1 ATOM 2438 C CG . GLU A 1 317 ? 25.838 8.301 43.389 1.00 19.74 ? 402 GLU A CG 1 ATOM 2439 C CD . GLU A 1 317 ? 24.790 7.209 43.477 1.00 26.26 ? 402 GLU A CD 1 ATOM 2440 O OE1 . GLU A 1 317 ? 24.099 6.959 42.466 1.00 26.18 ? 402 GLU A OE1 1 ATOM 2441 O OE2 . GLU A 1 317 ? 24.651 6.604 44.562 1.00 43.60 ? 402 GLU A OE2 1 ATOM 2442 N N . TRP A 1 318 ? 26.401 8.075 38.830 1.00 9.68 ? 403 TRP A N 1 ATOM 2443 C CA . TRP A 1 318 ? 26.653 8.519 37.463 1.00 8.54 ? 403 TRP A CA 1 ATOM 2444 C C . TRP A 1 318 ? 26.598 10.038 37.329 1.00 9.01 ? 403 TRP A C 1 ATOM 2445 O O . TRP A 1 318 ? 25.705 10.686 37.876 1.00 10.33 ? 403 TRP A O 1 ATOM 2446 C CB . TRP A 1 318 ? 25.641 7.883 36.507 1.00 13.31 ? 403 TRP A CB 1 ATOM 2447 C CG . TRP A 1 318 ? 25.566 6.394 36.637 1.00 16.03 ? 403 TRP A CG 1 ATOM 2448 C CD1 . TRP A 1 318 ? 24.565 5.670 37.216 1.00 19.17 ? 403 TRP A CD1 1 ATOM 2449 C CD2 . TRP A 1 318 ? 26.542 5.446 36.192 1.00 18.75 ? 403 TRP A CD2 1 ATOM 2450 N NE1 . TRP A 1 318 ? 24.855 4.328 37.152 1.00 21.19 ? 403 TRP A NE1 1 ATOM 2451 C CE2 . TRP A 1 318 ? 26.064 4.165 36.529 1.00 20.30 ? 403 TRP A CE2 1 ATOM 2452 C CE3 . TRP A 1 318 ? 27.773 5.557 35.540 1.00 20.55 ? 403 TRP A CE3 1 ATOM 2453 C CZ2 . TRP A 1 318 ? 26.774 3.003 36.235 1.00 23.30 ? 403 TRP A CZ2 1 ATOM 2454 C CZ3 . TRP A 1 318 ? 28.476 4.402 35.250 1.00 31.13 ? 403 TRP A CZ3 1 ATOM 2455 C CH2 . TRP A 1 318 ? 27.975 3.143 35.597 1.00 23.76 ? 403 TRP A CH2 1 ATOM 2456 N N . SER A 1 319 ? 27.560 10.602 36.606 1.00 8.16 ? 404 SER A N 1 ATOM 2457 C CA . SER A 1 319 ? 27.502 12.013 36.234 1.00 7.42 ? 404 SER A CA 1 ATOM 2458 C C . SER A 1 319 ? 27.693 12.062 34.717 1.00 10.03 ? 404 SER A C 1 ATOM 2459 O O . SER A 1 319 ? 27.424 11.080 34.027 1.00 8.39 ? 404 SER A O 1 ATOM 2460 C CB . SER A 1 319 ? 28.625 12.819 36.900 1.00 9.13 ? 404 SER A CB 1 ATOM 2461 O OG . SER A 1 319 ? 29.904 12.283 36.614 1.00 10.92 ? 404 SER A OG 1 ATOM 2462 N N . GLY A 1 320 ? 28.158 13.193 34.197 1.00 5.43 ? 405 GLY A N 1 ATOM 2463 C CA . GLY A 1 320 ? 28.334 13.338 32.762 1.00 6.75 ? 405 GLY A CA 1 ATOM 2464 C C . GLY A 1 320 ? 28.791 14.734 32.390 1.00 6.79 ? 405 GLY A C 1 ATOM 2465 O O . GLY A 1 320 ? 29.680 15.294 33.027 1.00 5.56 ? 405 GLY A O 1 ATOM 2466 N N . TYR A 1 321 ? 28.186 15.295 31.347 1.00 6.71 ? 406 TYR A N 1 ATOM 2467 C CA . TYR A 1 321 ? 28.510 16.653 30.928 1.00 7.34 ? 406 TYR A CA 1 ATOM 2468 C C . TYR A 1 321 ? 28.215 17.647 32.043 1.00 7.29 ? 406 TYR A C 1 ATOM 2469 O O . TYR A 1 321 ? 27.328 17.428 32.868 1.00 6.83 ? 406 TYR A O 1 ATOM 2470 C CB . TYR A 1 321 ? 27.714 17.038 29.677 1.00 7.91 ? 406 TYR A CB 1 ATOM 2471 C CG . TYR A 1 321 ? 28.313 16.558 28.372 1.00 8.23 ? 406 TYR A CG 1 ATOM 2472 C CD1 . TYR A 1 321 ? 29.205 15.493 28.339 1.00 7.59 ? 406 TYR A CD1 1 ATOM 2473 C CD2 . TYR A 1 321 ? 27.978 17.169 27.169 1.00 6.69 ? 406 TYR A CD2 1 ATOM 2474 C CE1 . TYR A 1 321 ? 29.754 15.055 27.141 1.00 9.11 ? 406 TYR A CE1 1 ATOM 2475 C CE2 . TYR A 1 321 ? 28.517 16.740 25.972 1.00 9.79 ? 406 TYR A CE2 1 ATOM 2476 C CZ . TYR A 1 321 ? 29.404 15.683 25.963 1.00 10.47 ? 406 TYR A CZ 1 ATOM 2477 O OH . TYR A 1 321 ? 29.940 15.256 24.769 1.00 10.41 ? 406 TYR A OH 1 ATOM 2478 N N . SER A 1 322 ? 28.972 18.737 32.067 1.00 5.41 ? 407 SER A N 1 ATOM 2479 C CA . SER A 1 322 ? 28.669 19.856 32.947 1.00 6.09 ? 407 SER A CA 1 ATOM 2480 C C . SER A 1 322 ? 28.997 21.156 32.226 1.00 5.82 ? 407 SER A C 1 ATOM 2481 O O . SER A 1 322 ? 29.803 21.174 31.296 1.00 8.10 ? 407 SER A O 1 ATOM 2482 C CB . SER A 1 322 ? 29.444 19.753 34.266 1.00 4.84 ? 407 SER A CB 1 ATOM 2483 O OG . SER A 1 322 ? 30.841 19.721 34.042 1.00 6.54 ? 407 SER A OG 1 ATOM 2484 N N . GLY A 1 323 ? 28.366 22.243 32.644 1.00 4.80 ? 408 GLY A N 1 ATOM 2485 C CA . GLY A 1 323 ? 28.581 23.516 31.988 1.00 6.20 ? 408 GLY A CA 1 ATOM 2486 C C . GLY A 1 323 ? 28.250 24.696 32.871 1.00 7.19 ? 408 GLY A C 1 ATOM 2487 O O . GLY A 1 323 ? 27.509 24.579 33.847 1.00 7.42 ? 408 GLY A O 1 ATOM 2488 N N . SER A 1 324 ? 28.804 25.847 32.519 1.00 6.03 ? 409 SER A N 1 ATOM 2489 C CA . SER A 1 324 ? 28.538 27.064 33.260 1.00 5.93 ? 409 SER A CA 1 ATOM 2490 C C . SER A 1 324 ? 27.276 27.736 32.742 1.00 6.91 ? 409 SER A C 1 ATOM 2491 O O . SER A 1 324 ? 26.869 27.528 31.597 1.00 7.26 ? 409 SER A O 1 ATOM 2492 C CB . SER A 1 324 ? 29.720 28.024 33.125 1.00 9.25 ? 409 SER A CB 1 ATOM 2493 O OG . SER A 1 324 ? 29.920 28.381 31.767 1.00 11.81 ? 409 SER A OG 1 ATOM 2494 N N . PHE A 1 325 ? 26.641 28.516 33.605 1.00 7.76 ? 410 PHE A N 1 ATOM 2495 C CA . PHE A 1 325 ? 25.667 29.509 33.170 1.00 8.24 ? 410 PHE A CA 1 ATOM 2496 C C . PHE A 1 325 ? 25.660 30.637 34.183 1.00 7.50 ? 410 PHE A C 1 ATOM 2497 O O . PHE A 1 325 ? 26.022 30.439 35.343 1.00 12.32 ? 410 PHE A O 1 ATOM 2498 C CB . PHE A 1 325 ? 24.267 28.915 32.936 1.00 6.81 ? 410 PHE A CB 1 ATOM 2499 C CG . PHE A 1 325 ? 23.537 28.502 34.190 1.00 8.58 ? 410 PHE A CG 1 ATOM 2500 C CD1 . PHE A 1 325 ? 23.769 27.265 34.772 1.00 7.58 ? 410 PHE A CD1 1 ATOM 2501 C CD2 . PHE A 1 325 ? 22.579 29.331 34.754 1.00 6.57 ? 410 PHE A CD2 1 ATOM 2502 C CE1 . PHE A 1 325 ? 23.083 26.875 35.910 1.00 7.60 ? 410 PHE A CE1 1 ATOM 2503 C CE2 . PHE A 1 325 ? 21.887 28.949 35.892 1.00 9.58 ? 410 PHE A CE2 1 ATOM 2504 C CZ . PHE A 1 325 ? 22.140 27.716 36.472 1.00 7.05 ? 410 PHE A CZ 1 ATOM 2505 N N . VAL A 1 326 ? 25.282 31.829 33.745 1.00 8.12 ? 411 VAL A N 1 ATOM 2506 C CA . VAL A 1 326 ? 25.348 32.982 34.626 1.00 6.96 ? 411 VAL A CA 1 ATOM 2507 C C . VAL A 1 326 ? 23.991 33.638 34.806 1.00 12.03 ? 411 VAL A C 1 ATOM 2508 O O . VAL A 1 326 ? 23.079 33.448 34.000 1.00 8.34 ? 411 VAL A O 1 ATOM 2509 C CB . VAL A 1 326 ? 26.365 34.025 34.115 1.00 9.80 ? 411 VAL A CB 1 ATOM 2510 C CG1 . VAL A 1 326 ? 27.767 33.441 34.132 1.00 6.87 ? 411 VAL A CG1 1 ATOM 2511 C CG2 . VAL A 1 326 ? 25.992 34.496 32.713 1.00 8.47 ? 411 VAL A CG2 1 ATOM 2512 N N . GLN A 1 327 ? 23.862 34.392 35.891 1.00 6.14 ? 412 GLN A N 1 ATOM 2513 C CA . GLN A 1 327 ? 22.698 35.227 36.108 1.00 4.36 ? 412 GLN A CA 1 ATOM 2514 C C . GLN A 1 327 ? 23.160 36.674 36.170 1.00 7.57 ? 412 GLN A C 1 ATOM 2515 O O . GLN A 1 327 ? 23.974 37.043 37.018 1.00 4.68 ? 412 GLN A O 1 ATOM 2516 C CB . GLN A 1 327 ? 21.959 34.818 37.386 1.00 5.38 ? 412 GLN A CB 1 ATOM 2517 C CG . GLN A 1 327 ? 21.400 33.402 37.322 1.00 5.57 ? 412 GLN A CG 1 ATOM 2518 C CD . GLN A 1 327 ? 20.519 33.052 38.505 1.00 7.29 ? 412 GLN A CD 1 ATOM 2519 O OE1 . GLN A 1 327 ? 20.769 33.481 39.631 1.00 6.66 ? 412 GLN A OE1 1 ATOM 2520 N NE2 . GLN A 1 327 ? 19.485 32.257 38.254 1.00 10.66 ? 412 GLN A NE2 1 ATOM 2521 N N . HIS A 1 328 A 22.652 37.484 35.247 1.00 8.13 ? 412 HIS A N 1 ATOM 2522 C CA . HIS A 1 328 A 23.062 38.875 35.140 1.00 8.13 ? 412 HIS A CA 1 ATOM 2523 C C . HIS A 1 328 A 22.353 39.728 36.185 1.00 6.86 ? 412 HIS A C 1 ATOM 2524 O O . HIS A 1 328 A 21.254 39.393 36.624 1.00 7.88 ? 412 HIS A O 1 ATOM 2525 C CB . HIS A 1 328 A 22.762 39.410 33.739 1.00 8.02 ? 412 HIS A CB 1 ATOM 2526 C CG . HIS A 1 328 A 23.697 38.909 32.682 1.00 10.21 ? 412 HIS A CG 1 ATOM 2527 N ND1 . HIS A 1 328 A 24.674 39.699 32.118 1.00 9.85 ? 412 HIS A ND1 1 ATOM 2528 C CD2 . HIS A 1 328 A 23.800 37.698 32.080 1.00 7.76 ? 412 HIS A CD2 1 ATOM 2529 C CE1 . HIS A 1 328 A 25.340 39.000 31.215 1.00 12.16 ? 412 HIS A CE1 1 ATOM 2530 N NE2 . HIS A 1 328 A 24.829 37.782 31.175 1.00 9.67 ? 412 HIS A NE2 1 ATOM 2531 N N . PRO A 1 329 B 22.987 40.836 36.590 1.00 4.48 ? 412 PRO A N 1 ATOM 2532 C CA . PRO A 1 329 B 22.393 41.774 37.548 1.00 6.81 ? 412 PRO A CA 1 ATOM 2533 C C . PRO A 1 329 B 21.002 42.223 37.115 1.00 10.78 ? 412 PRO A C 1 ATOM 2534 O O . PRO A 1 329 B 20.162 42.513 37.968 1.00 12.16 ? 412 PRO A O 1 ATOM 2535 C CB . PRO A 1 329 B 23.364 42.956 37.518 1.00 10.10 ? 412 PRO A CB 1 ATOM 2536 C CG . PRO A 1 329 B 24.670 42.347 37.157 1.00 11.25 ? 412 PRO A CG 1 ATOM 2537 C CD . PRO A 1 329 B 24.359 41.222 36.215 1.00 6.84 ? 412 PRO A CD 1 ATOM 2538 N N . GLU A 1 330 C 20.764 42.278 35.807 1.00 11.19 ? 412 GLU A N 1 ATOM 2539 C CA . GLU A 1 330 C 19.447 42.632 35.286 1.00 12.00 ? 412 GLU A CA 1 ATOM 2540 C C . GLU A 1 330 C 18.384 41.659 35.794 1.00 17.90 ? 412 GLU A C 1 ATOM 2541 O O . GLU A 1 330 C 17.210 42.004 35.898 1.00 19.31 ? 412 GLU A O 1 ATOM 2542 C CB . GLU A 1 330 C 19.449 42.656 33.753 1.00 15.71 ? 412 GLU A CB 1 ATOM 2543 C CG . GLU A 1 330 C 20.136 43.869 33.126 1.00 20.04 ? 412 GLU A CG 1 ATOM 2544 C CD . GLU A 1 330 C 21.642 43.705 32.995 1.00 14.81 ? 412 GLU A CD 1 ATOM 2545 O OE1 . GLU A 1 330 C 22.181 42.682 33.466 1.00 12.91 ? 412 GLU A OE1 1 ATOM 2546 O OE2 . GLU A 1 330 C 22.288 44.603 32.413 1.00 12.19 ? 412 GLU A OE2 1 ATOM 2547 N N . LEU A 1 331 D 18.802 40.439 36.110 1.00 10.59 ? 412 LEU A N 1 ATOM 2548 C CA . LEU A 1 331 D 17.879 39.430 36.617 1.00 10.15 ? 412 LEU A CA 1 ATOM 2549 C C . LEU A 1 331 D 17.855 39.382 38.146 1.00 12.29 ? 412 LEU A C 1 ATOM 2550 O O . LEU A 1 331 D 16.793 39.255 38.752 1.00 10.94 ? 412 LEU A O 1 ATOM 2551 C CB . LEU A 1 331 D 18.243 38.052 36.056 1.00 11.06 ? 412 LEU A CB 1 ATOM 2552 C CG . LEU A 1 331 D 17.550 36.832 36.665 1.00 8.70 ? 412 LEU A CG 1 ATOM 2553 C CD1 . LEU A 1 331 D 16.074 36.789 36.290 1.00 13.98 ? 412 LEU A CD1 1 ATOM 2554 C CD2 . LEU A 1 331 D 18.249 35.559 36.224 1.00 13.11 ? 412 LEU A CD2 1 ATOM 2555 N N . THR A 1 332 ? 19.027 39.499 38.763 1.00 7.50 ? 413 THR A N 1 ATOM 2556 C CA . THR A 1 332 ? 19.165 39.276 40.202 1.00 8.85 ? 413 THR A CA 1 ATOM 2557 C C . THR A 1 332 ? 19.047 40.539 41.050 1.00 13.59 ? 413 THR A C 1 ATOM 2558 O O . THR A 1 332 ? 18.652 40.476 42.215 1.00 16.30 ? 413 THR A O 1 ATOM 2559 C CB . THR A 1 332 ? 20.526 38.655 40.529 1.00 11.83 ? 413 THR A CB 1 ATOM 2560 O OG1 . THR A 1 332 ? 21.559 39.592 40.198 1.00 10.04 ? 413 THR A OG1 1 ATOM 2561 C CG2 . THR A 1 332 ? 20.729 37.371 39.742 1.00 10.53 ? 413 THR A CG2 1 ATOM 2562 N N . GLY A 1 333 ? 19.418 41.679 40.479 1.00 12.03 ? 414 GLY A N 1 ATOM 2563 C CA . GLY A 1 333 ? 19.470 42.915 41.237 1.00 13.86 ? 414 GLY A CA 1 ATOM 2564 C C . GLY A 1 333 ? 20.785 43.078 41.979 1.00 18.21 ? 414 GLY A C 1 ATOM 2565 O O . GLY A 1 333 ? 20.964 44.026 42.744 1.00 16.08 ? 414 GLY A O 1 ATOM 2566 N N . LEU A 1 334 ? 21.707 42.145 41.761 1.00 12.82 ? 415 LEU A N 1 ATOM 2567 C CA . LEU A 1 334 ? 23.046 42.243 42.332 1.00 13.59 ? 415 LEU A CA 1 ATOM 2568 C C . LEU A 1 334 ? 23.881 43.236 41.531 1.00 15.57 ? 415 LEU A C 1 ATOM 2569 O O . LEU A 1 334 ? 23.426 43.757 40.515 1.00 15.38 ? 415 LEU A O 1 ATOM 2570 C CB . LEU A 1 334 ? 23.728 40.873 42.340 1.00 9.74 ? 415 LEU A CB 1 ATOM 2571 C CG . LEU A 1 334 ? 23.039 39.782 43.165 1.00 19.99 ? 415 LEU A CG 1 ATOM 2572 C CD1 . LEU A 1 334 ? 23.668 38.421 42.901 1.00 16.17 ? 415 LEU A CD1 1 ATOM 2573 C CD2 . LEU A 1 334 ? 23.086 40.123 44.647 1.00 21.94 ? 415 LEU A CD2 1 ATOM 2574 N N . ASP A 1 335 ? 25.099 43.501 41.993 1.00 13.03 ? 416 ASP A N 1 ATOM 2575 C CA . ASP A 1 335 ? 25.995 44.416 41.290 1.00 23.90 ? 416 ASP A CA 1 ATOM 2576 C C . ASP A 1 335 ? 27.138 43.661 40.617 1.00 18.49 ? 416 ASP A C 1 ATOM 2577 O O . ASP A 1 335 ? 28.179 44.236 40.299 1.00 20.38 ? 416 ASP A O 1 ATOM 2578 C CB . ASP A 1 335 ? 26.539 45.486 42.243 1.00 23.23 ? 416 ASP A CB 1 ATOM 2579 C CG . ASP A 1 335 ? 27.328 44.897 43.397 1.00 35.82 ? 416 ASP A CG 1 ATOM 2580 O OD1 . ASP A 1 335 ? 27.665 43.695 43.346 1.00 39.89 ? 416 ASP A OD1 1 ATOM 2581 O OD2 . ASP A 1 335 ? 27.617 45.641 44.359 1.00 45.87 ? 416 ASP A OD2 1 ATOM 2582 N N . CYS A 1 336 ? 26.930 42.367 40.404 1.00 16.41 ? 417 CYS A N 1 ATOM 2583 C CA . CYS A 1 336 ? 27.933 41.517 39.778 1.00 11.78 ? 417 CYS A CA 1 ATOM 2584 C C . CYS A 1 336 ? 27.255 40.367 39.042 1.00 11.60 ? 417 CYS A C 1 ATOM 2585 O O . CYS A 1 336 ? 26.067 40.110 39.231 1.00 10.80 ? 417 CYS A O 1 ATOM 2586 C CB . CYS A 1 336 ? 28.895 40.967 40.829 1.00 11.88 ? 417 CYS A CB 1 ATOM 2587 S SG . CYS A 1 336 ? 28.074 40.115 42.196 1.00 23.23 ? 417 CYS A SG 1 ATOM 2588 N N . ILE A 1 337 ? 28.015 39.682 38.198 1.00 9.50 ? 418 ILE A N 1 ATOM 2589 C CA . ILE A 1 337 ? 27.490 38.545 37.456 1.00 8.27 ? 418 ILE A CA 1 ATOM 2590 C C . ILE A 1 337 ? 27.661 37.280 38.286 1.00 8.76 ? 418 ILE A C 1 ATOM 2591 O O . ILE A 1 337 ? 28.775 36.935 38.685 1.00 9.26 ? 418 ILE A O 1 ATOM 2592 C CB . ILE A 1 337 ? 28.200 38.397 36.099 1.00 8.75 ? 418 ILE A CB 1 ATOM 2593 C CG1 . ILE A 1 337 ? 27.980 39.655 35.255 1.00 8.38 ? 418 ILE A CG1 1 ATOM 2594 C CG2 . ILE A 1 337 ? 27.707 37.157 35.368 1.00 9.54 ? 418 ILE A CG2 1 ATOM 2595 C CD1 . ILE A 1 337 ? 28.673 39.626 33.903 1.00 10.51 ? 418 ILE A CD1 1 ATOM 2596 N N . ARG A 1 338 ? 26.552 36.599 38.563 1.00 7.45 ? 419 ARG A N 1 ATOM 2597 C CA . ARG A 1 338 ? 26.589 35.413 39.413 1.00 11.71 ? 419 ARG A CA 1 ATOM 2598 C C . ARG A 1 338 ? 26.846 34.134 38.626 1.00 7.13 ? 419 ARG A C 1 ATOM 2599 O O . ARG A 1 338 ? 26.129 33.830 37.672 1.00 8.15 ? 419 ARG A O 1 ATOM 2600 C CB . ARG A 1 338 ? 25.294 35.271 40.216 1.00 9.79 ? 419 ARG A CB 1 ATOM 2601 C CG . ARG A 1 338 ? 25.103 33.877 40.794 1.00 10.60 ? 419 ARG A CG 1 ATOM 2602 C CD . ARG A 1 338 ? 23.751 33.732 41.467 1.00 12.71 ? 419 ARG A CD 1 ATOM 2603 N NE . ARG A 1 338 ? 23.786 34.156 42.861 1.00 18.80 ? 419 ARG A NE 1 ATOM 2604 C CZ . ARG A 1 338 ? 22.710 34.267 43.631 1.00 18.14 ? 419 ARG A CZ 1 ATOM 2605 N NH1 . ARG A 1 338 ? 21.511 33.994 43.135 1.00 13.70 ? 419 ARG A NH1 1 ATOM 2606 N NH2 . ARG A 1 338 ? 22.833 34.656 44.893 1.00 20.17 ? 419 ARG A NH2 1 ATOM 2607 N N . PRO A 1 339 ? 27.870 33.372 39.040 1.00 10.36 ? 420 PRO A N 1 ATOM 2608 C CA . PRO A 1 339 ? 28.225 32.105 38.397 1.00 8.75 ? 420 PRO A CA 1 ATOM 2609 C C . PRO A 1 339 ? 27.315 30.988 38.880 1.00 7.55 ? 420 PRO A C 1 ATOM 2610 O O . PRO A 1 339 ? 27.062 30.883 40.078 1.00 9.95 ? 420 PRO A O 1 ATOM 2611 C CB . PRO A 1 339 ? 29.651 31.836 38.902 1.00 10.36 ? 420 PRO A CB 1 ATOM 2612 C CG . PRO A 1 339 ? 30.011 32.999 39.805 1.00 17.13 ? 420 PRO A CG 1 ATOM 2613 C CD . PRO A 1 339 ? 28.733 33.653 40.196 1.00 9.16 ? 420 PRO A CD 1 ATOM 2614 N N . CYS A 1 340 ? 26.828 30.171 37.954 1.00 4.51 ? 421 CYS A N 1 ATOM 2615 C CA . CYS A 1 340 ? 26.079 28.970 38.291 1.00 5.75 ? 421 CYS A CA 1 ATOM 2616 C C . CYS A 1 340 ? 26.615 27.847 37.417 1.00 7.48 ? 421 CYS A C 1 ATOM 2617 O O . CYS A 1 340 ? 27.388 28.096 36.489 1.00 5.75 ? 421 CYS A O 1 ATOM 2618 C CB . CYS A 1 340 ? 24.582 29.162 38.021 1.00 4.90 ? 421 CYS A CB 1 ATOM 2619 S SG . CYS A 1 340 ? 23.780 30.546 38.877 1.00 8.58 ? 421 CYS A SG 1 ATOM 2620 N N . PHE A 1 341 ? 26.211 26.615 37.702 1.00 3.73 ? 422 PHE A N 1 ATOM 2621 C CA . PHE A 1 341 ? 26.568 25.497 36.831 1.00 6.00 ? 422 PHE A CA 1 ATOM 2622 C C . PHE A 1 341 ? 25.513 24.401 36.857 1.00 5.94 ? 422 PHE A C 1 ATOM 2623 O O . PHE A 1 341 ? 24.724 24.303 37.796 1.00 6.26 ? 422 PHE A O 1 ATOM 2624 C CB . PHE A 1 341 ? 27.958 24.931 37.168 1.00 4.05 ? 422 PHE A CB 1 ATOM 2625 C CG . PHE A 1 341 ? 28.013 24.145 38.454 1.00 6.37 ? 422 PHE A CG 1 ATOM 2626 C CD1 . PHE A 1 341 ? 28.329 24.769 39.652 1.00 6.43 ? 422 PHE A CD1 1 ATOM 2627 C CD2 . PHE A 1 341 ? 27.764 22.782 38.462 1.00 8.52 ? 422 PHE A CD2 1 ATOM 2628 C CE1 . PHE A 1 341 ? 28.385 24.048 40.836 1.00 6.69 ? 422 PHE A CE1 1 ATOM 2629 C CE2 . PHE A 1 341 ? 27.817 22.055 39.645 1.00 7.59 ? 422 PHE A CE2 1 ATOM 2630 C CZ . PHE A 1 341 ? 28.128 22.689 40.831 1.00 6.64 ? 422 PHE A CZ 1 ATOM 2631 N N . TRP A 1 342 ? 25.496 23.592 35.806 1.00 2.51 ? 423 TRP A N 1 ATOM 2632 C CA . TRP A 1 342 ? 24.595 22.454 35.731 1.00 5.26 ? 423 TRP A CA 1 ATOM 2633 C C . TRP A 1 342 ? 25.401 21.182 35.523 1.00 4.70 ? 423 TRP A C 1 ATOM 2634 O O . TRP A 1 342 ? 26.524 21.223 35.008 1.00 2.97 ? 423 TRP A O 1 ATOM 2635 C CB . TRP A 1 342 ? 23.586 22.635 34.591 1.00 5.74 ? 423 TRP A CB 1 ATOM 2636 C CG . TRP A 1 342 ? 24.226 22.920 33.264 1.00 5.69 ? 423 TRP A CG 1 ATOM 2637 C CD1 . TRP A 1 342 ? 24.406 24.146 32.687 1.00 6.01 ? 423 TRP A CD1 1 ATOM 2638 C CD2 . TRP A 1 342 ? 24.779 21.963 32.352 1.00 7.44 ? 423 TRP A CD2 1 ATOM 2639 N NE1 . TRP A 1 342 ? 25.034 24.010 31.473 1.00 6.23 ? 423 TRP A NE1 1 ATOM 2640 C CE2 . TRP A 1 342 ? 25.272 22.680 31.243 1.00 6.91 ? 423 TRP A CE2 1 ATOM 2641 C CE3 . TRP A 1 342 ? 24.897 20.569 32.362 1.00 6.13 ? 423 TRP A CE3 1 ATOM 2642 C CZ2 . TRP A 1 342 ? 25.877 22.051 30.157 1.00 7.55 ? 423 TRP A CZ2 1 ATOM 2643 C CZ3 . TRP A 1 342 ? 25.501 19.946 31.283 1.00 5.20 ? 423 TRP A CZ3 1 ATOM 2644 C CH2 . TRP A 1 342 ? 25.983 20.688 30.195 1.00 8.47 ? 423 TRP A CH2 1 ATOM 2645 N N . VAL A 1 343 ? 24.830 20.055 35.935 1.00 2.16 ? 424 VAL A N 1 ATOM 2646 C CA . VAL A 1 343 ? 25.453 18.759 35.712 1.00 4.25 ? 424 VAL A CA 1 ATOM 2647 C C . VAL A 1 343 ? 24.456 17.791 35.089 1.00 6.87 ? 424 VAL A C 1 ATOM 2648 O O . VAL A 1 343 ? 23.327 17.657 35.563 1.00 6.39 ? 424 VAL A O 1 ATOM 2649 C CB . VAL A 1 343 ? 25.998 18.149 37.020 1.00 4.80 ? 424 VAL A CB 1 ATOM 2650 C CG1 . VAL A 1 343 ? 26.737 16.847 36.726 1.00 7.68 ? 424 VAL A CG1 1 ATOM 2651 C CG2 . VAL A 1 343 ? 26.913 19.135 37.724 1.00 5.64 ? 424 VAL A CG2 1 ATOM 2652 N N . GLU A 1 344 ? 24.884 17.129 34.019 1.00 6.56 ? 425 GLU A N 1 ATOM 2653 C CA . GLU A 1 344 ? 24.087 16.101 33.366 1.00 8.30 ? 425 GLU A CA 1 ATOM 2654 C C . GLU A 1 344 ? 24.399 14.753 34.001 1.00 7.08 ? 425 GLU A C 1 ATOM 2655 O O . GLU A 1 344 ? 25.563 14.372 34.127 1.00 8.29 ? 425 GLU A O 1 ATOM 2656 C CB . GLU A 1 344 ? 24.406 16.062 31.869 1.00 7.11 ? 425 GLU A CB 1 ATOM 2657 C CG . GLU A 1 344 ? 23.677 14.985 31.081 1.00 8.64 ? 425 GLU A CG 1 ATOM 2658 C CD . GLU A 1 344 ? 24.323 14.726 29.729 1.00 11.51 ? 425 GLU A CD 1 ATOM 2659 O OE1 . GLU A 1 344 ? 25.570 14.710 29.662 1.00 10.95 ? 425 GLU A OE1 1 ATOM 2660 O OE2 . GLU A 1 344 ? 23.589 14.537 28.735 1.00 10.05 ? 425 GLU A OE2 1 ATOM 2661 N N . LEU A 1 345 ? 23.358 14.041 34.414 1.00 6.04 ? 426 LEU A N 1 ATOM 2662 C CA . LEU A 1 345 ? 23.527 12.725 35.013 1.00 5.92 ? 426 LEU A CA 1 ATOM 2663 C C . LEU A 1 345 ? 23.104 11.663 34.006 1.00 8.21 ? 426 LEU A C 1 ATOM 2664 O O . LEU A 1 345 ? 21.916 11.375 33.858 1.00 7.84 ? 426 LEU A O 1 ATOM 2665 C CB . LEU A 1 345 ? 22.703 12.617 36.298 1.00 6.08 ? 426 LEU A CB 1 ATOM 2666 C CG . LEU A 1 345 ? 22.860 13.795 37.264 1.00 7.85 ? 426 LEU A CG 1 ATOM 2667 C CD1 . LEU A 1 345 ? 21.982 13.619 38.495 1.00 9.31 ? 426 LEU A CD1 1 ATOM 2668 C CD2 . LEU A 1 345 ? 24.319 13.979 37.667 1.00 8.37 ? 426 LEU A CD2 1 ATOM 2669 N N . ILE A 1 346 ? 24.084 11.090 33.313 1.00 5.96 ? 427 ILE A N 1 ATOM 2670 C CA . ILE A 1 346 ? 23.820 10.164 32.212 1.00 8.14 ? 427 ILE A CA 1 ATOM 2671 C C . ILE A 1 346 ? 23.480 8.754 32.685 1.00 9.49 ? 427 ILE A C 1 ATOM 2672 O O . ILE A 1 346 ? 24.234 8.147 33.446 1.00 7.58 ? 427 ILE A O 1 ATOM 2673 C CB . ILE A 1 346 ? 25.027 10.083 31.255 1.00 7.64 ? 427 ILE A CB 1 ATOM 2674 C CG1 . ILE A 1 346 ? 25.393 11.477 30.741 1.00 8.07 ? 427 ILE A CG1 1 ATOM 2675 C CG2 . ILE A 1 346 ? 24.729 9.140 30.097 1.00 8.57 ? 427 ILE A CG2 1 ATOM 2676 C CD1 . ILE A 1 346 ? 26.683 11.518 29.942 1.00 10.49 ? 427 ILE A CD1 1 ATOM 2677 N N . ARG A 1 347 ? 22.344 8.238 32.221 1.00 9.61 ? 428 ARG A N 1 ATOM 2678 C CA . ARG A 1 347 ? 21.938 6.869 32.517 1.00 9.62 ? 428 ARG A CA 1 ATOM 2679 C C . ARG A 1 347 ? 21.803 6.068 31.224 1.00 11.23 ? 428 ARG A C 1 ATOM 2680 O O . ARG A 1 347 ? 21.440 6.614 30.181 1.00 9.86 ? 428 ARG A O 1 ATOM 2681 C CB . ARG A 1 347 ? 20.609 6.851 33.276 1.00 10.56 ? 428 ARG A CB 1 ATOM 2682 C CG . ARG A 1 347 ? 20.621 7.620 34.594 1.00 9.76 ? 428 ARG A CG 1 ATOM 2683 C CD . ARG A 1 347 ? 21.717 7.119 35.524 1.00 10.70 ? 428 ARG A CD 1 ATOM 2684 N NE . ARG A 1 347 ? 21.605 5.688 35.801 1.00 9.05 ? 428 ARG A NE 1 ATOM 2685 C CZ . ARG A 1 347 ? 20.871 5.169 36.781 1.00 11.35 ? 428 ARG A CZ 1 ATOM 2686 N NH1 . ARG A 1 347 ? 20.168 5.960 37.581 1.00 10.22 ? 428 ARG A NH1 1 ATOM 2687 N NH2 . ARG A 1 347 ? 20.834 3.855 36.959 1.00 10.73 ? 428 ARG A NH2 1 ATOM 2688 N N . GLY A 1 348 ? 22.098 4.773 31.295 1.00 11.22 ? 429 GLY A N 1 ATOM 2689 C CA . GLY A 1 348 ? 21.956 3.900 30.142 1.00 10.75 ? 429 GLY A CA 1 ATOM 2690 C C . GLY A 1 348 ? 23.283 3.501 29.526 1.00 11.98 ? 429 GLY A C 1 ATOM 2691 O O . GLY A 1 348 ? 24.267 3.286 30.235 1.00 11.86 ? 429 GLY A O 1 ATOM 2692 N N . ARG A 1 349 ? 23.310 3.393 28.202 1.00 13.56 ? 430 ARG A N 1 ATOM 2693 C CA . ARG A 1 349 ? 24.536 3.037 27.498 1.00 14.56 ? 430 ARG A CA 1 ATOM 2694 C C . ARG A 1 349 ? 25.578 4.142 27.627 1.00 14.68 ? 430 ARG A C 1 ATOM 2695 O O . ARG A 1 349 ? 25.231 5.313 27.766 1.00 15.48 ? 430 ARG A O 1 ATOM 2696 C CB . ARG A 1 349 ? 24.249 2.756 26.021 1.00 16.47 ? 430 ARG A CB 1 ATOM 2697 C CG . ARG A 1 349 ? 23.178 1.719 25.789 1.00 21.41 ? 430 ARG A CG 1 ATOM 2698 C CD . ARG A 1 349 ? 23.361 0.536 26.711 1.00 27.21 ? 430 ARG A CD 1 ATOM 2699 N NE . ARG A 1 349 ? 24.084 -0.566 26.083 1.00 38.58 ? 430 ARG A NE 1 ATOM 2700 C CZ . ARG A 1 349 ? 25.157 -1.149 26.608 1.00 40.36 ? 430 ARG A CZ 1 ATOM 2701 N NH1 . ARG A 1 349 ? 25.644 -0.728 27.765 1.00 35.70 ? 430 ARG A NH1 1 ATOM 2702 N NH2 . ARG A 1 349 ? 25.747 -2.153 25.977 1.00 52.56 ? 430 ARG A NH2 1 ATOM 2703 N N . PRO A 1 350 ? 26.866 3.771 27.568 1.00 17.56 ? 431 PRO A N 1 ATOM 2704 C CA . PRO A 1 350 ? 27.336 2.396 27.370 1.00 18.12 ? 431 PRO A CA 1 ATOM 2705 C C . PRO A 1 350 ? 27.604 1.661 28.682 1.00 19.38 ? 431 PRO A C 1 ATOM 2706 O O . PRO A 1 350 ? 28.000 0.498 28.648 1.00 22.17 ? 431 PRO A O 1 ATOM 2707 C CB . PRO A 1 350 ? 28.673 2.588 26.629 1.00 21.36 ? 431 PRO A CB 1 ATOM 2708 C CG . PRO A 1 350 ? 28.864 4.100 26.473 1.00 27.40 ? 431 PRO A CG 1 ATOM 2709 C CD . PRO A 1 350 ? 27.977 4.729 27.494 1.00 19.07 ? 431 PRO A CD 1 ATOM 2710 N N . LYS A 1 351 ? 27.397 2.326 29.814 1.00 15.52 ? 432 LYS A N 1 ATOM 2711 C CA . LYS A 1 351 ? 27.793 1.772 31.107 1.00 21.17 ? 432 LYS A CA 1 ATOM 2712 C C . LYS A 1 351 ? 26.769 0.813 31.709 1.00 21.58 ? 432 LYS A C 1 ATOM 2713 O O . LYS A 1 351 ? 27.109 -0.013 32.554 1.00 17.56 ? 432 LYS A O 1 ATOM 2714 C CB . LYS A 1 351 ? 28.084 2.900 32.103 1.00 20.59 ? 432 LYS A CB 1 ATOM 2715 C CG . LYS A 1 351 ? 29.279 3.760 31.740 1.00 23.56 ? 432 LYS A CG 1 ATOM 2716 C CD . LYS A 1 351 ? 30.573 2.970 31.827 1.00 33.26 ? 432 LYS A CD 1 ATOM 2717 C CE . LYS A 1 351 ? 31.782 3.870 31.622 1.00 38.52 ? 432 LYS A CE 1 ATOM 2718 N NZ . LYS A 1 351 ? 33.061 3.151 31.876 1.00 47.56 ? 432 LYS A NZ 1 ATOM 2719 N N . GLU A 1 352 ? 25.518 0.931 31.282 1.00 13.63 ? 433 GLU A N 1 ATOM 2720 C CA . GLU A 1 352 ? 24.444 0.127 31.858 1.00 15.27 ? 433 GLU A CA 1 ATOM 2721 C C . GLU A 1 352 ? 23.731 -0.698 30.789 1.00 14.04 ? 433 GLU A C 1 ATOM 2722 O O . GLU A 1 352 ? 23.760 -0.353 29.610 1.00 17.12 ? 433 GLU A O 1 ATOM 2723 C CB . GLU A 1 352 ? 23.459 1.021 32.614 1.00 14.20 ? 433 GLU A CB 1 ATOM 2724 C CG . GLU A 1 352 ? 24.125 1.874 33.691 1.00 16.42 ? 433 GLU A CG 1 ATOM 2725 C CD . GLU A 1 352 ? 23.155 2.793 34.408 1.00 17.06 ? 433 GLU A CD 1 ATOM 2726 O OE1 . GLU A 1 352 ? 23.045 3.974 34.011 1.00 10.12 ? 433 GLU A OE1 1 ATOM 2727 O OE2 . GLU A 1 352 ? 22.506 2.338 35.372 1.00 15.92 ? 433 GLU A OE2 1 ATOM 2728 N N . ASN A 1 353 ? 23.095 -1.788 31.208 1.00 18.97 ? 435 ASN A N 1 ATOM 2729 C CA . ASN A 1 353 ? 22.484 -2.732 30.275 1.00 23.33 ? 435 ASN A CA 1 ATOM 2730 C C . ASN A 1 353 ? 21.090 -2.323 29.811 1.00 20.54 ? 435 ASN A C 1 ATOM 2731 O O . ASN A 1 353 ? 20.094 -2.949 30.173 1.00 20.35 ? 435 ASN A O 1 ATOM 2732 C CB . ASN A 1 353 ? 22.451 -4.139 30.880 1.00 33.38 ? 435 ASN A CB 1 ATOM 2733 C CG . ASN A 1 353 ? 23.831 -4.762 30.980 1.00 41.98 ? 435 ASN A CG 1 ATOM 2734 O OD1 . ASN A 1 353 ? 24.085 -5.605 31.841 1.00 51.71 ? 435 ASN A OD1 1 ATOM 2735 N ND2 . ASN A 1 353 ? 24.733 -4.345 30.098 1.00 42.91 ? 435 ASN A ND2 1 ATOM 2736 N N . THR A 1 354 ? 21.032 -1.272 29.001 1.00 13.16 ? 436 THR A N 1 ATOM 2737 C CA . THR A 1 354 ? 19.775 -0.799 28.437 1.00 12.14 ? 436 THR A CA 1 ATOM 2738 C C . THR A 1 354 ? 19.900 -0.687 26.922 1.00 12.75 ? 436 THR A C 1 ATOM 2739 O O . THR A 1 354 ? 20.969 -0.919 26.364 1.00 12.91 ? 436 THR A O 1 ATOM 2740 C CB . THR A 1 354 ? 19.401 0.578 29.003 1.00 12.63 ? 436 THR A CB 1 ATOM 2741 O OG1 . THR A 1 354 ? 20.463 1.502 28.739 1.00 10.80 ? 436 THR A OG1 1 ATOM 2742 C CG2 . THR A 1 354 ? 19.180 0.494 30.507 1.00 11.86 ? 436 THR A CG2 1 ATOM 2743 N N . ILE A 1 355 ? 18.807 -0.337 26.254 1.00 9.90 ? 437 ILE A N 1 ATOM 2744 C CA . ILE A 1 355 ? 18.856 -0.099 24.817 1.00 11.29 ? 437 ILE A CA 1 ATOM 2745 C C . ILE A 1 355 ? 19.004 1.391 24.548 1.00 12.51 ? 437 ILE A C 1 ATOM 2746 O O . ILE A 1 355 ? 19.251 1.809 23.417 1.00 13.64 ? 437 ILE A O 1 ATOM 2747 C CB . ILE A 1 355 ? 17.585 -0.603 24.111 1.00 13.43 ? 437 ILE A CB 1 ATOM 2748 C CG1 . ILE A 1 355 ? 16.365 0.198 24.573 1.00 12.22 ? 437 ILE A CG1 1 ATOM 2749 C CG2 . ILE A 1 355 ? 17.390 -2.095 24.361 1.00 15.84 ? 437 ILE A CG2 1 ATOM 2750 C CD1 . ILE A 1 355 ? 15.094 -0.137 23.820 1.00 16.15 ? 437 ILE A CD1 1 ATOM 2751 N N . TRP A 1 356 ? 18.865 2.186 25.604 1.00 9.92 ? 438 TRP A N 1 ATOM 2752 C CA . TRP A 1 356 ? 18.782 3.637 25.474 1.00 9.61 ? 438 TRP A CA 1 ATOM 2753 C C . TRP A 1 356 ? 19.837 4.373 26.295 1.00 9.92 ? 438 TRP A C 1 ATOM 2754 O O . TRP A 1 356 ? 20.484 3.795 27.170 1.00 7.81 ? 438 TRP A O 1 ATOM 2755 C CB . TRP A 1 356 ? 17.396 4.108 25.914 1.00 8.85 ? 438 TRP A CB 1 ATOM 2756 C CG . TRP A 1 356 ? 17.026 3.619 27.285 1.00 7.98 ? 438 TRP A CG 1 ATOM 2757 C CD1 . TRP A 1 356 ? 16.434 2.428 27.596 1.00 11.65 ? 438 TRP A CD1 1 ATOM 2758 C CD2 . TRP A 1 356 ? 17.236 4.299 28.528 1.00 8.23 ? 438 TRP A CD2 1 ATOM 2759 N NE1 . TRP A 1 356 ? 16.260 2.327 28.955 1.00 10.28 ? 438 TRP A NE1 1 ATOM 2760 C CE2 . TRP A 1 356 ? 16.742 3.463 29.550 1.00 10.17 ? 438 TRP A CE2 1 ATOM 2761 C CE3 . TRP A 1 356 ? 17.789 5.536 28.877 1.00 9.07 ? 438 TRP A CE3 1 ATOM 2762 C CZ2 . TRP A 1 356 ? 16.784 3.824 30.898 1.00 10.78 ? 438 TRP A CZ2 1 ATOM 2763 C CZ3 . TRP A 1 356 ? 17.830 5.892 30.216 1.00 9.94 ? 438 TRP A CZ3 1 ATOM 2764 C CH2 . TRP A 1 356 ? 17.330 5.038 31.209 1.00 11.02 ? 438 TRP A CH2 1 ATOM 2765 N N . THR A 1 357 ? 19.994 5.658 25.998 1.00 10.02 ? 439 THR A N 1 ATOM 2766 C CA . THR A 1 357 ? 20.836 6.549 26.784 1.00 10.44 ? 439 THR A CA 1 ATOM 2767 C C . THR A 1 357 ? 20.100 7.867 26.980 1.00 8.92 ? 439 THR A C 1 ATOM 2768 O O . THR A 1 357 ? 19.580 8.440 26.026 1.00 8.52 ? 439 THR A O 1 ATOM 2769 C CB . THR A 1 357 ? 22.177 6.833 26.085 1.00 15.72 ? 439 THR A CB 1 ATOM 2770 O OG1 . THR A 1 357 ? 22.891 5.606 25.898 1.00 14.98 ? 439 THR A OG1 1 ATOM 2771 C CG2 . THR A 1 357 ? 23.023 7.786 26.921 1.00 14.28 ? 439 THR A CG2 1 ATOM 2772 N N . SER A 1 358 ? 20.048 8.343 28.219 1.00 8.54 ? 440 SER A N 1 ATOM 2773 C CA . SER A 1 358 ? 19.402 9.615 28.514 1.00 8.51 ? 440 SER A CA 1 ATOM 2774 C C . SER A 1 358 ? 19.998 10.212 29.780 1.00 14.61 ? 440 SER A C 1 ATOM 2775 O O . SER A 1 358 ? 20.725 9.541 30.509 1.00 16.17 ? 440 SER A O 1 ATOM 2776 C CB . SER A 1 358 ? 17.893 9.430 28.677 1.00 10.73 ? 440 SER A CB 1 ATOM 2777 O OG . SER A 1 358 ? 17.225 10.681 28.696 1.00 8.98 ? 440 SER A OG 1 ATOM 2778 N N . GLY A 1 359 ? 19.692 11.476 30.041 1.00 15.30 ? 441 GLY A N 1 ATOM 2779 C CA . GLY A 1 359 ? 20.214 12.131 31.223 1.00 12.99 ? 441 GLY A CA 1 ATOM 2780 C C . GLY A 1 359 ? 19.185 12.976 31.942 1.00 15.82 ? 441 GLY A C 1 ATOM 2781 O O . GLY A 1 359 ? 18.223 13.452 31.340 1.00 14.32 ? 441 GLY A O 1 ATOM 2782 N N . SER A 1 360 ? 19.380 13.141 33.245 1.00 9.91 ? 442 SER A N 1 ATOM 2783 C CA . SER A 1 360 ? 18.627 14.121 34.011 1.00 10.33 ? 442 SER A CA 1 ATOM 2784 C C . SER A 1 360 ? 19.613 15.212 34.399 1.00 10.71 ? 442 SER A C 1 ATOM 2785 O O . SER A 1 360 ? 20.779 15.166 34.000 1.00 10.92 ? 442 SER A O 1 ATOM 2786 C CB . SER A 1 360 ? 17.985 13.489 35.248 1.00 8.75 ? 442 SER A CB 1 ATOM 2787 O OG . SER A 1 360 ? 18.962 13.091 36.192 1.00 11.66 ? 442 SER A OG 1 ATOM 2788 N N . SER A 1 361 ? 19.167 16.194 35.172 1.00 9.96 ? 443 SER A N 1 ATOM 2789 C CA . SER A 1 361 ? 20.047 17.310 35.487 1.00 10.14 ? 443 SER A CA 1 ATOM 2790 C C . SER A 1 361 ? 19.887 17.847 36.902 1.00 8.32 ? 443 SER A C 1 ATOM 2791 O O . SER A 1 361 ? 18.829 17.724 37.522 1.00 9.21 ? 443 SER A O 1 ATOM 2792 C CB . SER A 1 361 ? 19.849 18.445 34.479 1.00 11.50 ? 443 SER A CB 1 ATOM 2793 O OG . SER A 1 361 ? 18.584 19.059 34.648 1.00 15.58 ? 443 SER A OG 1 ATOM 2794 N N . ILE A 1 362 ? 20.969 18.434 37.398 1.00 4.51 ? 444 ILE A N 1 ATOM 2795 C CA . ILE A 1 362 ? 20.961 19.206 38.628 1.00 6.82 ? 444 ILE A CA 1 ATOM 2796 C C . ILE A 1 362 ? 21.706 20.499 38.331 1.00 6.65 ? 444 ILE A C 1 ATOM 2797 O O . ILE A 1 362 ? 22.514 20.552 37.401 1.00 4.97 ? 444 ILE A O 1 ATOM 2798 C CB . ILE A 1 362 ? 21.673 18.461 39.776 1.00 4.98 ? 444 ILE A CB 1 ATOM 2799 C CG1 . ILE A 1 362 ? 23.072 18.018 39.338 1.00 4.67 ? 444 ILE A CG1 1 ATOM 2800 C CG2 . ILE A 1 362 ? 20.852 17.264 40.229 1.00 9.36 ? 444 ILE A CG2 1 ATOM 2801 C CD1 . ILE A 1 362 ? 23.846 17.271 40.407 1.00 4.59 ? 444 ILE A CD1 1 ATOM 2802 N N . SER A 1 363 ? 21.433 21.542 39.103 1.00 5.03 ? 445 SER A N 1 ATOM 2803 C CA . SER A 1 363 ? 22.136 22.808 38.927 1.00 7.02 ? 445 SER A CA 1 ATOM 2804 C C . SER A 1 363 ? 22.373 23.486 40.268 1.00 7.82 ? 445 SER A C 1 ATOM 2805 O O . SER A 1 363 ? 21.638 23.256 41.228 1.00 6.76 ? 445 SER A O 1 ATOM 2806 C CB . SER A 1 363 ? 21.367 23.742 37.991 1.00 8.05 ? 445 SER A CB 1 ATOM 2807 O OG . SER A 1 363 ? 20.215 24.275 38.624 1.00 7.66 ? 445 SER A OG 1 ATOM 2808 N N . PHE A 1 364 ? 23.407 24.318 40.322 1.00 4.78 ? 446 PHE A N 1 ATOM 2809 C CA . PHE A 1 364 ? 23.789 25.017 41.543 1.00 6.35 ? 446 PHE A CA 1 ATOM 2810 C C . PHE A 1 364 ? 24.158 26.457 41.209 1.00 8.28 ? 446 PHE A C 1 ATOM 2811 O O . PHE A 1 364 ? 24.563 26.751 40.084 1.00 6.05 ? 446 PHE A O 1 ATOM 2812 C CB . PHE A 1 364 ? 24.994 24.328 42.194 1.00 5.83 ? 446 PHE A CB 1 ATOM 2813 C CG . PHE A 1 364 ? 24.736 22.906 42.601 1.00 5.65 ? 446 PHE A CG 1 ATOM 2814 C CD1 . PHE A 1 364 ? 24.697 21.895 41.655 1.00 6.67 ? 446 PHE A CD1 1 ATOM 2815 C CD2 . PHE A 1 364 ? 24.547 22.578 43.933 1.00 8.94 ? 446 PHE A CD2 1 ATOM 2816 C CE1 . PHE A 1 364 ? 24.460 20.586 42.028 1.00 8.95 ? 446 PHE A CE1 1 ATOM 2817 C CE2 . PHE A 1 364 ? 24.312 21.269 44.312 1.00 8.71 ? 446 PHE A CE2 1 ATOM 2818 C CZ . PHE A 1 364 ? 24.267 20.274 43.359 1.00 7.81 ? 446 PHE A CZ 1 ATOM 2819 N N . CYS A 1 365 ? 24.025 27.351 42.183 1.00 7.02 ? 447 CYS A N 1 ATOM 2820 C CA . CYS A 1 365 ? 24.446 28.737 42.006 1.00 5.86 ? 447 CYS A CA 1 ATOM 2821 C C . CYS A 1 365 ? 25.412 29.172 43.103 1.00 6.36 ? 447 CYS A C 1 ATOM 2822 O O . CYS A 1 365 ? 25.303 28.735 44.249 1.00 7.95 ? 447 CYS A O 1 ATOM 2823 C CB . CYS A 1 365 ? 23.239 29.676 41.936 1.00 10.91 ? 447 CYS A CB 1 ATOM 2824 S SG . CYS A 1 365 ? 22.500 29.797 40.281 1.00 18.45 ? 447 CYS A SG 1 ATOM 2825 N N . GLY A 1 366 ? 26.361 30.030 42.744 1.00 7.78 ? 448 GLY A N 1 ATOM 2826 C CA . GLY A 1 366 ? 27.397 30.450 43.673 1.00 9.71 ? 448 GLY A CA 1 ATOM 2827 C C . GLY A 1 366 ? 26.896 31.462 44.682 1.00 8.60 ? 448 GLY A C 1 ATOM 2828 O O . GLY A 1 366 ? 26.223 32.425 44.319 1.00 10.66 ? 448 GLY A O 1 ATOM 2829 N N . VAL A 1 367 ? 27.224 31.241 45.952 1.00 6.23 ? 449 VAL A N 1 ATOM 2830 C CA . VAL A 1 367 ? 26.826 32.156 47.017 1.00 6.15 ? 449 VAL A CA 1 ATOM 2831 C C . VAL A 1 367 ? 27.983 32.389 47.986 1.00 8.89 ? 449 VAL A C 1 ATOM 2832 O O . VAL A 1 367 ? 28.999 31.696 47.932 1.00 8.36 ? 449 VAL A O 1 ATOM 2833 C CB . VAL A 1 367 ? 25.615 31.617 47.807 1.00 7.14 ? 449 VAL A CB 1 ATOM 2834 C CG1 . VAL A 1 367 ? 24.392 31.498 46.907 1.00 6.58 ? 449 VAL A CG1 1 ATOM 2835 C CG2 . VAL A 1 367 ? 25.950 30.278 48.446 1.00 8.24 ? 449 VAL A CG2 1 ATOM 2836 N N . ASN A 1 368 ? 27.828 33.368 48.870 1.00 11.24 ? 450 ASN A N 1 ATOM 2837 C CA . ASN A 1 368 ? 28.828 33.618 49.904 1.00 12.31 ? 450 ASN A CA 1 ATOM 2838 C C . ASN A 1 368 ? 28.309 33.299 51.299 1.00 16.87 ? 450 ASN A C 1 ATOM 2839 O O . ASN A 1 368 ? 28.993 33.528 52.297 1.00 18.98 ? 450 ASN A O 1 ATOM 2840 C CB . ASN A 1 368 ? 29.339 35.054 49.836 1.00 16.25 ? 450 ASN A CB 1 ATOM 2841 C CG . ASN A 1 368 ? 30.357 35.252 48.736 1.00 21.19 ? 450 ASN A CG 1 ATOM 2842 O OD1 . ASN A 1 368 ? 31.433 34.652 48.757 1.00 24.29 ? 450 ASN A OD1 1 ATOM 2843 N ND2 . ASN A 1 368 ? 30.025 36.093 47.765 1.00 24.02 ? 450 ASN A ND2 1 ATOM 2844 N N . SER A 1 369 ? 27.093 32.772 51.360 1.00 14.92 ? 451 SER A N 1 ATOM 2845 C CA . SER A 1 369 ? 26.530 32.299 52.617 1.00 15.62 ? 451 SER A CA 1 ATOM 2846 C C . SER A 1 369 ? 26.851 30.817 52.785 1.00 13.50 ? 451 SER A C 1 ATOM 2847 O O . SER A 1 369 ? 27.534 30.229 51.948 1.00 12.09 ? 451 SER A O 1 ATOM 2848 C CB . SER A 1 369 ? 25.020 32.542 52.653 1.00 14.22 ? 451 SER A CB 1 ATOM 2849 O OG . SER A 1 369 ? 24.406 32.102 51.454 1.00 12.98 ? 451 SER A OG 1 ATOM 2850 N N . ASP A 1 370 ? 26.355 30.214 53.860 1.00 12.71 ? 452 ASP A N 1 ATOM 2851 C CA . ASP A 1 370 ? 26.697 28.830 54.185 1.00 13.76 ? 452 ASP A CA 1 ATOM 2852 C C . ASP A 1 370 ? 26.170 27.815 53.169 1.00 10.56 ? 452 ASP A C 1 ATOM 2853 O O . ASP A 1 370 ? 25.047 27.932 52.678 1.00 11.56 ? 452 ASP A O 1 ATOM 2854 C CB . ASP A 1 370 ? 26.211 28.473 55.594 1.00 10.82 ? 452 ASP A CB 1 ATOM 2855 C CG . ASP A 1 370 ? 27.008 29.175 56.681 1.00 22.91 ? 452 ASP A CG 1 ATOM 2856 O OD1 . ASP A 1 370 ? 28.096 29.704 56.372 1.00 25.32 ? 452 ASP A OD1 1 ATOM 2857 O OD2 . ASP A 1 370 ? 26.552 29.195 57.845 1.00 19.66 ? 452 ASP A OD2 1 ATOM 2858 N N . THR A 1 371 ? 26.995 26.819 52.861 1.00 6.89 ? 453 THR A N 1 ATOM 2859 C CA . THR A 1 371 ? 26.607 25.750 51.946 1.00 6.83 ? 453 THR A CA 1 ATOM 2860 C C . THR A 1 371 ? 27.039 24.399 52.497 1.00 8.03 ? 453 THR A C 1 ATOM 2861 O O . THR A 1 371 ? 27.676 24.325 53.545 1.00 9.98 ? 453 THR A O 1 ATOM 2862 C CB . THR A 1 371 ? 27.231 25.938 50.550 1.00 10.50 ? 453 THR A CB 1 ATOM 2863 O OG1 . THR A 1 371 ? 28.658 25.989 50.666 1.00 12.52 ? 453 THR A OG1 1 ATOM 2864 C CG2 . THR A 1 371 ? 26.728 27.223 49.907 1.00 8.05 ? 453 THR A CG2 1 ATOM 2865 N N . VAL A 1 372 ? 26.695 23.331 51.786 1.00 7.22 ? 454 VAL A N 1 ATOM 2866 C CA . VAL A 1 372 ? 27.061 21.988 52.222 1.00 8.41 ? 454 VAL A CA 1 ATOM 2867 C C . VAL A 1 372 ? 27.273 21.049 51.042 1.00 9.95 ? 454 VAL A C 1 ATOM 2868 O O . VAL A 1 372 ? 26.594 21.151 50.020 1.00 9.37 ? 454 VAL A O 1 ATOM 2869 C CB . VAL A 1 372 ? 25.999 21.384 53.174 1.00 9.24 ? 454 VAL A CB 1 ATOM 2870 C CG1 . VAL A 1 372 ? 24.716 21.065 52.417 1.00 7.83 ? 454 VAL A CG1 1 ATOM 2871 C CG2 . VAL A 1 372 ? 26.539 20.134 53.855 1.00 9.63 ? 454 VAL A CG2 1 ATOM 2872 N N . GLY A 1 373 ? 28.228 20.136 51.190 1.00 8.96 ? 455 GLY A N 1 ATOM 2873 C CA . GLY A 1 373 ? 28.444 19.102 50.197 1.00 8.78 ? 455 GLY A CA 1 ATOM 2874 C C . GLY A 1 373 ? 27.516 17.931 50.450 1.00 11.17 ? 455 GLY A C 1 ATOM 2875 O O . GLY A 1 373 ? 27.139 17.666 51.591 1.00 11.63 ? 455 GLY A O 1 ATOM 2876 N N . TRP A 1 374 ? 27.136 17.237 49.384 1.00 8.34 ? 456 TRP A N 1 ATOM 2877 C CA . TRP A 1 374 ? 26.288 16.058 49.501 1.00 10.21 ? 456 TRP A CA 1 ATOM 2878 C C . TRP A 1 374 ? 26.332 15.299 48.186 1.00 10.25 ? 456 TRP A C 1 ATOM 2879 O O . TRP A 1 374 ? 27.231 15.504 47.373 1.00 10.77 ? 456 TRP A O 1 ATOM 2880 C CB . TRP A 1 374 ? 24.845 16.459 49.828 1.00 8.85 ? 456 TRP A CB 1 ATOM 2881 C CG . TRP A 1 374 ? 24.069 15.413 50.592 1.00 10.64 ? 456 TRP A CG 1 ATOM 2882 C CD1 . TRP A 1 374 ? 24.576 14.486 51.459 1.00 12.42 ? 456 TRP A CD1 1 ATOM 2883 C CD2 . TRP A 1 374 ? 22.648 15.210 50.576 1.00 8.94 ? 456 TRP A CD2 1 ATOM 2884 N NE1 . TRP A 1 374 ? 23.562 13.712 51.971 1.00 10.82 ? 456 TRP A NE1 1 ATOM 2885 C CE2 . TRP A 1 374 ? 22.369 14.137 51.448 1.00 10.49 ? 456 TRP A CE2 1 ATOM 2886 C CE3 . TRP A 1 374 ? 21.588 15.828 49.906 1.00 8.86 ? 456 TRP A CE3 1 ATOM 2887 C CZ2 . TRP A 1 374 ? 21.073 13.670 51.669 1.00 10.36 ? 456 TRP A CZ2 1 ATOM 2888 C CZ3 . TRP A 1 374 ? 20.298 15.361 50.127 1.00 10.49 ? 456 TRP A CZ3 1 ATOM 2889 C CH2 . TRP A 1 374 ? 20.054 14.293 51.000 1.00 9.71 ? 456 TRP A CH2 1 ATOM 2890 N N . SER A 1 375 ? 25.358 14.421 47.984 1.00 9.65 ? 457 SER A N 1 ATOM 2891 C CA . SER A 1 375 ? 25.208 13.735 46.712 1.00 9.87 ? 457 SER A CA 1 ATOM 2892 C C . SER A 1 375 ? 23.758 13.814 46.254 1.00 9.37 ? 457 SER A C 1 ATOM 2893 O O . SER A 1 375 ? 22.857 13.333 46.938 1.00 10.26 ? 457 SER A O 1 ATOM 2894 C CB . SER A 1 375 ? 25.647 12.275 46.828 1.00 12.95 ? 457 SER A CB 1 ATOM 2895 O OG . SER A 1 375 ? 25.549 11.622 45.574 1.00 10.07 ? 457 SER A OG 1 ATOM 2896 N N . TRP A 1 376 ? 23.539 14.437 45.101 1.00 9.59 ? 458 TRP A N 1 ATOM 2897 C CA . TRP A 1 376 ? 22.208 14.519 44.511 1.00 9.29 ? 458 TRP A CA 1 ATOM 2898 C C . TRP A 1 376 ? 22.200 13.764 43.186 1.00 8.19 ? 458 TRP A C 1 ATOM 2899 O O . TRP A 1 376 ? 22.290 14.378 42.126 1.00 10.99 ? 458 TRP A O 1 ATOM 2900 C CB . TRP A 1 376 ? 21.809 15.977 44.267 1.00 7.57 ? 458 TRP A CB 1 ATOM 2901 C CG . TRP A 1 376 ? 21.544 16.791 45.509 1.00 7.75 ? 458 TRP A CG 1 ATOM 2902 C CD1 . TRP A 1 376 ? 20.355 16.918 46.168 1.00 8.76 ? 458 TRP A CD1 1 ATOM 2903 C CD2 . TRP A 1 376 ? 22.485 17.609 46.220 1.00 9.43 ? 458 TRP A CD2 1 ATOM 2904 N NE1 . TRP A 1 376 ? 20.499 17.756 47.250 1.00 8.64 ? 458 TRP A NE1 1 ATOM 2905 C CE2 . TRP A 1 376 ? 21.796 18.193 47.303 1.00 9.85 ? 458 TRP A CE2 1 ATOM 2906 C CE3 . TRP A 1 376 ? 23.841 17.900 46.047 1.00 9.88 ? 458 TRP A CE3 1 ATOM 2907 C CZ2 . TRP A 1 376 ? 22.418 19.051 48.208 1.00 9.01 ? 458 TRP A CZ2 1 ATOM 2908 C CZ3 . TRP A 1 376 ? 24.458 18.751 46.951 1.00 9.65 ? 458 TRP A CZ3 1 ATOM 2909 C CH2 . TRP A 1 376 ? 23.746 19.317 48.015 1.00 10.29 ? 458 TRP A CH2 1 ATOM 2910 N N . PRO A 1 377 ? 22.092 12.427 43.246 1.00 8.26 ? 459 PRO A N 1 ATOM 2911 C CA . PRO A 1 377 ? 22.225 11.558 42.072 1.00 9.08 ? 459 PRO A CA 1 ATOM 2912 C C . PRO A 1 377 ? 20.938 11.466 41.258 1.00 8.57 ? 459 PRO A C 1 ATOM 2913 O O . PRO A 1 377 ? 19.896 11.958 41.688 1.00 8.72 ? 459 PRO A O 1 ATOM 2914 C CB . PRO A 1 377 ? 22.535 10.181 42.684 1.00 12.48 ? 459 PRO A CB 1 ATOM 2915 C CG . PRO A 1 377 ? 22.536 10.373 44.190 1.00 13.35 ? 459 PRO A CG 1 ATOM 2916 C CD . PRO A 1 377 ? 21.818 11.649 44.462 1.00 8.42 ? 459 PRO A CD 1 ATOM 2917 N N . ASP A 1 378 ? 21.017 10.825 40.096 1.00 10.71 ? 460 ASP A N 1 ATOM 2918 C CA . ASP A 1 378 ? 19.850 10.623 39.243 1.00 10.01 ? 460 ASP A CA 1 ATOM 2919 C C . ASP A 1 378 ? 18.751 9.846 39.965 1.00 11.20 ? 460 ASP A C 1 ATOM 2920 O O . ASP A 1 378 ? 17.599 10.277 40.003 1.00 10.30 ? 460 ASP A O 1 ATOM 2921 C CB . ASP A 1 378 ? 20.246 9.893 37.961 1.00 9.39 ? 460 ASP A CB 1 ATOM 2922 C CG . ASP A 1 378 ? 19.052 9.558 37.092 1.00 13.01 ? 460 ASP A CG 1 ATOM 2923 O OD1 . ASP A 1 378 ? 18.513 10.478 36.443 1.00 14.53 ? 460 ASP A OD1 1 ATOM 2924 O OD2 . ASP A 1 378 ? 18.650 8.376 37.063 1.00 13.11 ? 460 ASP A OD2 1 ATOM 2925 N N . GLY A 1 379 ? 19.111 8.690 40.518 1.00 8.83 ? 461 GLY A N 1 ATOM 2926 C CA . GLY A 1 379 ? 18.202 7.924 41.353 1.00 10.19 ? 461 GLY A CA 1 ATOM 2927 C C . GLY A 1 379 ? 17.247 6.981 40.640 1.00 10.88 ? 461 GLY A C 1 ATOM 2928 O O . GLY A 1 379 ? 16.394 6.367 41.279 1.00 7.31 ? 461 GLY A O 1 ATOM 2929 N N . ALA A 1 380 ? 17.378 6.857 39.323 1.00 7.74 ? 462 ALA A N 1 ATOM 2930 C CA . ALA A 1 380 ? 16.523 5.938 38.576 1.00 9.17 ? 462 ALA A CA 1 ATOM 2931 C C . ALA A 1 380 ? 16.990 4.496 38.733 1.00 11.79 ? 462 ALA A C 1 ATOM 2932 O O . ALA A 1 380 ? 18.182 4.234 38.890 1.00 10.67 ? 462 ALA A O 1 ATOM 2933 C CB . ALA A 1 380 ? 16.472 6.321 37.107 1.00 8.47 ? 462 ALA A CB 1 ATOM 2934 N N . GLU A 1 381 ? 16.043 3.564 38.696 1.00 10.09 ? 463 GLU A N 1 ATOM 2935 C CA . GLU A 1 381 ? 16.363 2.145 38.792 1.00 13.30 ? 463 GLU A CA 1 ATOM 2936 C C . GLU A 1 381 ? 16.332 1.503 37.410 1.00 13.23 ? 463 GLU A C 1 ATOM 2937 O O . GLU A 1 381 ? 15.267 1.345 36.815 1.00 13.16 ? 463 GLU A O 1 ATOM 2938 C CB . GLU A 1 381 ? 15.373 1.431 39.714 1.00 15.56 ? 463 GLU A CB 1 ATOM 2939 C CG . GLU A 1 381 ? 15.314 1.990 41.124 1.00 28.69 ? 463 GLU A CG 1 ATOM 2940 C CD . GLU A 1 381 ? 16.506 1.585 41.967 1.00 42.35 ? 463 GLU A CD 1 ATOM 2941 O OE1 . GLU A 1 381 ? 17.333 0.781 41.485 1.00 48.22 ? 463 GLU A OE1 1 ATOM 2942 O OE2 . GLU A 1 381 ? 16.614 2.066 43.115 1.00 49.50 ? 463 GLU A OE2 1 ATOM 2943 N N . LEU A 1 382 ? 17.506 1.141 36.903 1.00 12.90 ? 464 LEU A N 1 ATOM 2944 C CA . LEU A 1 382 ? 17.619 0.494 35.600 1.00 11.44 ? 464 LEU A CA 1 ATOM 2945 C C . LEU A 1 382 ? 17.822 -1.008 35.777 1.00 15.87 ? 464 LEU A C 1 ATOM 2946 O O . LEU A 1 382 ? 18.310 -1.447 36.818 1.00 16.68 ? 464 LEU A O 1 ATOM 2947 C CB . LEU A 1 382 ? 18.781 1.095 34.803 1.00 13.28 ? 464 LEU A CB 1 ATOM 2948 C CG . LEU A 1 382 ? 18.517 2.387 34.021 1.00 13.55 ? 464 LEU A CG 1 ATOM 2949 C CD1 . LEU A 1 382 ? 17.941 3.480 34.915 1.00 11.13 ? 464 LEU A CD1 1 ATOM 2950 C CD2 . LEU A 1 382 ? 19.794 2.863 33.342 1.00 10.85 ? 464 LEU A CD2 1 ATOM 2951 N N . PRO A 1 383 ? 17.454 -1.802 34.759 1.00 17.52 ? 465 PRO A N 1 ATOM 2952 C CA . PRO A 1 383 ? 16.872 -1.364 33.484 1.00 15.60 ? 465 PRO A CA 1 ATOM 2953 C C . PRO A 1 383 ? 15.389 -1.022 33.599 1.00 16.07 ? 465 PRO A C 1 ATOM 2954 O O . PRO A 1 383 ? 14.783 -1.230 34.652 1.00 16.11 ? 465 PRO A O 1 ATOM 2955 C CB . PRO A 1 383 ? 17.039 -2.595 32.578 1.00 22.64 ? 465 PRO A CB 1 ATOM 2956 C CG . PRO A 1 383 ? 17.960 -3.528 33.316 1.00 29.49 ? 465 PRO A CG 1 ATOM 2957 C CD . PRO A 1 383 ? 17.725 -3.248 34.759 1.00 23.28 ? 465 PRO A CD 1 ATOM 2958 N N . PHE A 1 384 ? 14.820 -0.505 32.514 1.00 13.42 ? 466 PHE A N 1 ATOM 2959 C CA . PHE A 1 384 ? 13.398 -0.187 32.446 1.00 14.21 ? 466 PHE A CA 1 ATOM 2960 C C . PHE A 1 384 ? 12.611 -1.310 31.773 1.00 14.87 ? 466 PHE A C 1 ATOM 2961 O O . PHE A 1 384 ? 13.186 -2.300 31.322 1.00 14.86 ? 466 PHE A O 1 ATOM 2962 C CB . PHE A 1 384 ? 13.178 1.124 31.687 1.00 12.22 ? 466 PHE A CB 1 ATOM 2963 C CG . PHE A 1 384 ? 13.371 2.356 32.527 1.00 14.34 ? 466 PHE A CG 1 ATOM 2964 C CD1 . PHE A 1 384 ? 13.903 2.267 33.803 1.00 12.72 ? 466 PHE A CD1 1 ATOM 2965 C CD2 . PHE A 1 384 ? 13.017 3.603 32.039 1.00 14.63 ? 466 PHE A CD2 1 ATOM 2966 C CE1 . PHE A 1 384 ? 14.078 3.399 34.578 1.00 12.91 ? 466 PHE A CE1 1 ATOM 2967 C CE2 . PHE A 1 384 ? 13.191 4.740 32.808 1.00 11.54 ? 466 PHE A CE2 1 ATOM 2968 C CZ . PHE A 1 384 ? 13.720 4.638 34.079 1.00 13.02 ? 466 PHE A CZ 1 ATOM 2969 N N . THR A 1 385 ? 11.294 -1.143 31.701 1.00 14.29 ? 467 THR A N 1 ATOM 2970 C CA . THR A 1 385 ? 10.414 -2.143 31.101 1.00 14.15 ? 467 THR A CA 1 ATOM 2971 C C . THR A 1 385 ? 10.771 -2.425 29.643 1.00 19.89 ? 467 THR A C 1 ATOM 2972 O O . THR A 1 385 ? 10.763 -3.576 29.204 1.00 16.96 ? 467 THR A O 1 ATOM 2973 C CB . THR A 1 385 ? 8.939 -1.707 31.177 1.00 16.85 ? 467 THR A CB 1 ATOM 2974 O OG1 . THR A 1 385 ? 8.588 -1.441 32.540 1.00 28.56 ? 467 THR A OG1 1 ATOM 2975 C CG2 . THR A 1 385 ? 8.031 -2.798 30.624 1.00 26.16 ? 467 THR A CG2 1 ATOM 2976 N N . ILE A 1 386 ? 11.077 -1.369 28.896 1.00 11.45 ? 468 ILE A N 1 ATOM 2977 C CA . ILE A 1 386 ? 11.465 -1.505 27.499 1.00 14.08 ? 468 ILE A CA 1 ATOM 2978 C C . ILE A 1 386 ? 12.840 -2.153 27.423 1.00 20.04 ? 468 ILE A C 1 ATOM 2979 O O . ILE A 1 386 ? 13.222 -2.702 26.388 1.00 20.78 ? 468 ILE A O 1 ATOM 2980 C CB . ILE A 1 386 ? 11.521 -0.129 26.797 1.00 12.45 ? 468 ILE A CB 1 ATOM 2981 C CG1 . ILE A 1 386 ? 11.433 -0.288 25.278 1.00 11.40 ? 468 ILE A CG1 1 ATOM 2982 C CG2 . ILE A 1 386 ? 12.781 0.629 27.197 1.00 13.70 ? 468 ILE A CG2 1 ATOM 2983 C CD1 . ILE A 1 386 ? 10.078 -0.756 24.791 1.00 16.31 ? 468 ILE A CD1 1 ATOM 2984 N N . ASP A 1 387 ? 13.550 -2.091 28.551 1.00 28.01 ? 469 ASP A N 1 ATOM 2985 C CA . ASP A 1 387 ? 14.957 -2.482 28.696 1.00 27.97 ? 469 ASP A CA 1 ATOM 2986 C C . ASP A 1 387 ? 15.866 -1.251 28.796 1.00 28.42 ? 469 ASP A C 1 ATOM 2987 O O . ASP A 1 387 ? 16.551 -0.861 27.849 1.00 18.92 ? 469 ASP A O 1 ATOM 2988 C CB . ASP A 1 387 ? 15.421 -3.424 27.583 1.00 33.17 ? 469 ASP A CB 1 ATOM 2989 C CG . ASP A 1 387 ? 14.901 -4.838 27.765 1.00 36.45 ? 469 ASP A CG 1 ATOM 2990 O OD1 . ASP A 1 387 ? 13.962 -5.028 28.566 1.00 38.00 ? 469 ASP A OD1 1 ATOM 2991 O OD2 . ASP A 1 387 ? 15.433 -5.758 27.109 1.00 48.49 ? 469 ASP A OD2 1 ATOM 2992 N N . SER B 1 1 ? 2.019 46.355 41.584 1.00 38.64 ? 82 SER B N 1 ATOM 2993 C CA . SER B 1 1 ? 2.300 45.447 42.690 1.00 32.05 ? 82 SER B CA 1 ATOM 2994 C C . SER B 1 1 ? 2.564 46.206 43.987 1.00 26.24 ? 82 SER B C 1 ATOM 2995 O O . SER B 1 1 ? 3.401 47.108 44.029 1.00 27.50 ? 82 SER B O 1 ATOM 2996 C CB . SER B 1 1 ? 3.488 44.542 42.356 1.00 23.11 ? 82 SER B CB 1 ATOM 2997 O OG . SER B 1 1 ? 3.155 43.625 41.330 1.00 31.67 ? 82 SER B OG 1 ATOM 2998 N N . VAL B 1 2 ? 1.842 45.834 45.040 1.00 22.47 ? 83 VAL B N 1 ATOM 2999 C CA . VAL B 1 2 ? 1.995 46.462 46.345 1.00 17.18 ? 83 VAL B CA 1 ATOM 3000 C C . VAL B 1 2 ? 2.114 45.389 47.421 1.00 19.30 ? 83 VAL B C 1 ATOM 3001 O O . VAL B 1 2 ? 1.458 44.351 47.344 1.00 16.36 ? 83 VAL B O 1 ATOM 3002 C CB . VAL B 1 2 ? 0.796 47.370 46.676 1.00 20.55 ? 83 VAL B CB 1 ATOM 3003 C CG1 . VAL B 1 2 ? 1.011 48.071 48.008 1.00 22.54 ? 83 VAL B CG1 1 ATOM 3004 C CG2 . VAL B 1 2 ? 0.576 48.387 45.566 1.00 27.64 ? 83 VAL B CG2 1 ATOM 3005 N N . LYS B 1 3 ? 2.949 45.633 48.424 1.00 18.73 ? 84 LYS B N 1 ATOM 3006 C CA . LYS B 1 3 ? 3.123 44.656 49.490 1.00 13.90 ? 84 LYS B CA 1 ATOM 3007 C C . LYS B 1 3 ? 1.872 44.535 50.358 1.00 15.73 ? 84 LYS B C 1 ATOM 3008 O O . LYS B 1 3 ? 1.117 45.493 50.525 1.00 14.46 ? 84 LYS B O 1 ATOM 3009 C CB . LYS B 1 3 ? 4.351 44.982 50.339 1.00 18.01 ? 84 LYS B CB 1 ATOM 3010 C CG . LYS B 1 3 ? 4.441 46.424 50.782 1.00 21.77 ? 84 LYS B CG 1 ATOM 3011 C CD . LYS B 1 3 ? 5.856 46.751 51.237 1.00 31.39 ? 84 LYS B CD 1 ATOM 3012 C CE . LYS B 1 3 ? 6.108 48.247 51.234 1.00 42.51 ? 84 LYS B CE 1 ATOM 3013 N NZ . LYS B 1 3 ? 7.511 48.566 51.619 1.00 41.54 ? 84 LYS B NZ 1 ATOM 3014 N N . LEU B 1 4 ? 1.652 43.339 50.891 1.00 8.50 ? 85 LEU B N 1 ATOM 3015 C CA . LEU B 1 4 ? 0.519 43.088 51.769 1.00 12.27 ? 85 LEU B CA 1 ATOM 3016 C C . LEU B 1 4 ? 0.675 43.866 53.072 1.00 10.82 ? 85 LEU B C 1 ATOM 3017 O O . LEU B 1 4 ? 1.742 43.862 53.685 1.00 14.39 ? 85 LEU B O 1 ATOM 3018 C CB . LEU B 1 4 ? 0.396 41.589 52.054 1.00 8.37 ? 85 LEU B CB 1 ATOM 3019 C CG . LEU B 1 4 ? 0.249 40.678 50.835 1.00 9.49 ? 85 LEU B CG 1 ATOM 3020 C CD1 . LEU B 1 4 ? 0.247 39.213 51.259 1.00 11.11 ? 85 LEU B CD1 1 ATOM 3021 C CD2 . LEU B 1 4 ? -1.014 41.015 50.051 1.00 10.13 ? 85 LEU B CD2 1 ATOM 3022 N N . ALA B 1 5 ? -0.391 44.542 53.488 1.00 9.16 ? 86 ALA B N 1 ATOM 3023 C CA . ALA B 1 5 ? -0.355 45.335 54.711 1.00 13.01 ? 86 ALA B CA 1 ATOM 3024 C C . ALA B 1 5 ? -0.264 44.441 55.944 1.00 11.04 ? 86 ALA B C 1 ATOM 3025 O O . ALA B 1 5 ? 0.613 44.620 56.791 1.00 11.78 ? 86 ALA B O 1 ATOM 3026 C CB . ALA B 1 5 ? -1.580 46.236 54.795 1.00 13.07 ? 86 ALA B CB 1 ATOM 3027 N N . GLY B 1 6 ? -1.177 43.479 56.037 1.00 11.32 ? 87 GLY B N 1 ATOM 3028 C CA . GLY B 1 6 ? -1.210 42.553 57.154 1.00 12.17 ? 87 GLY B CA 1 ATOM 3029 C C . GLY B 1 6 ? -1.574 43.201 58.477 1.00 10.69 ? 87 GLY B C 1 ATOM 3030 O O . GLY B 1 6 ? -1.242 42.674 59.541 1.00 10.59 ? 87 GLY B O 1 ATOM 3031 N N . ASN B 1 7 ? -2.268 44.334 58.422 1.00 9.99 ? 88 ASN B N 1 ATOM 3032 C CA . ASN B 1 7 ? -2.560 45.095 59.637 1.00 8.69 ? 88 ASN B CA 1 ATOM 3033 C C . ASN B 1 7 ? -4.000 44.982 60.150 1.00 10.23 ? 88 ASN B C 1 ATOM 3034 O O . ASN B 1 7 ? -4.326 45.509 61.216 1.00 13.40 ? 88 ASN B O 1 ATOM 3035 C CB . ASN B 1 7 ? -2.140 46.565 59.486 1.00 11.25 ? 88 ASN B CB 1 ATOM 3036 C CG . ASN B 1 7 ? -2.906 47.293 58.395 1.00 22.01 ? 88 ASN B CG 1 ATOM 3037 O OD1 . ASN B 1 7 ? -3.627 46.682 57.603 1.00 13.88 ? 88 ASN B OD1 1 ATOM 3038 N ND2 . ASN B 1 7 ? -2.743 48.613 58.345 1.00 26.41 ? 88 ASN B ND2 1 ATOM 3039 N N . SER B 1 8 ? -4.852 44.287 59.402 1.00 12.58 ? 89 SER B N 1 ATOM 3040 C CA . SER B 1 8 ? -6.232 44.071 59.833 1.00 11.53 ? 89 SER B CA 1 ATOM 3041 C C . SER B 1 8 ? -6.353 42.821 60.704 1.00 12.74 ? 89 SER B C 1 ATOM 3042 O O . SER B 1 8 ? -5.416 42.030 60.803 1.00 11.51 ? 89 SER B O 1 ATOM 3043 C CB . SER B 1 8 ? -7.174 43.976 58.629 1.00 10.06 ? 89 SER B CB 1 ATOM 3044 O OG . SER B 1 8 ? -6.873 42.847 57.830 1.00 15.86 ? 89 SER B OG 1 ATOM 3045 N N . SER B 1 9 ? -7.507 42.653 61.341 1.00 9.64 ? 90 SER B N 1 ATOM 3046 C CA . SER B 1 9 ? -7.739 41.508 62.212 1.00 10.49 ? 90 SER B CA 1 ATOM 3047 C C . SER B 1 9 ? -8.243 40.306 61.425 1.00 11.58 ? 90 SER B C 1 ATOM 3048 O O . SER B 1 9 ? -8.663 40.438 60.276 1.00 9.69 ? 90 SER B O 1 ATOM 3049 C CB . SER B 1 9 ? -8.754 41.866 63.301 1.00 17.65 ? 90 SER B CB 1 ATOM 3050 O OG . SER B 1 9 ? -8.339 43.009 64.028 1.00 27.06 ? 90 SER B OG 1 ATOM 3051 N N . LEU B 1 10 ? -8.195 39.133 62.049 1.00 12.61 ? 91 LEU B N 1 ATOM 3052 C CA . LEU B 1 10 ? -8.789 37.935 61.470 1.00 17.17 ? 91 LEU B CA 1 ATOM 3053 C C . LEU B 1 10 ? -10.297 38.097 61.381 1.00 16.41 ? 91 LEU B C 1 ATOM 3054 O O . LEU B 1 10 ? -10.930 38.593 62.314 1.00 18.04 ? 91 LEU B O 1 ATOM 3055 C CB . LEU B 1 10 ? -8.479 36.705 62.325 1.00 17.08 ? 91 LEU B CB 1 ATOM 3056 C CG . LEU B 1 10 ? -7.227 35.873 62.052 1.00 20.86 ? 91 LEU B CG 1 ATOM 3057 C CD1 . LEU B 1 10 ? -7.257 34.621 62.917 1.00 14.28 ? 91 LEU B CD1 1 ATOM 3058 C CD2 . LEU B 1 10 ? -7.124 35.500 60.583 1.00 16.00 ? 91 LEU B CD2 1 ATOM 3059 N N . CYS B 1 11 ? -10.871 37.675 60.260 1.00 13.67 ? 92 CYS B N 1 ATOM 3060 C CA . CYS B 1 11 ? -12.318 37.660 60.109 1.00 17.24 ? 92 CYS B CA 1 ATOM 3061 C C . CYS B 1 11 ? -12.921 36.641 61.067 1.00 17.43 ? 92 CYS B C 1 ATOM 3062 O O . CYS B 1 11 ? -12.543 35.470 61.052 1.00 14.91 ? 92 CYS B O 1 ATOM 3063 C CB . CYS B 1 11 ? -12.711 37.295 58.673 1.00 16.65 ? 92 CYS B CB 1 ATOM 3064 S SG . CYS B 1 11 ? -11.977 38.320 57.376 1.00 27.07 ? 92 CYS B SG 1 ATOM 3065 N N . PRO B 1 12 ? -13.856 37.082 61.916 1.00 21.45 ? 93 PRO B N 1 ATOM 3066 C CA . PRO B 1 12 ? -14.594 36.114 62.732 1.00 22.21 ? 93 PRO B CA 1 ATOM 3067 C C . PRO B 1 12 ? -15.427 35.225 61.818 1.00 19.15 ? 93 PRO B C 1 ATOM 3068 O O . PRO B 1 12 ? -16.005 35.733 60.856 1.00 18.20 ? 93 PRO B O 1 ATOM 3069 C CB . PRO B 1 12 ? -15.502 37.001 63.594 1.00 28.24 ? 93 PRO B CB 1 ATOM 3070 C CG . PRO B 1 12 ? -14.851 38.352 63.579 1.00 32.48 ? 93 PRO B CG 1 ATOM 3071 C CD . PRO B 1 12 ? -14.230 38.471 62.225 1.00 25.32 ? 93 PRO B CD 1 ATOM 3072 N N . VAL B 1 13 ? -15.472 33.925 62.097 1.00 12.65 ? 94 VAL B N 1 ATOM 3073 C CA . VAL B 1 13 ? -16.221 32.996 61.253 1.00 11.19 ? 94 VAL B CA 1 ATOM 3074 C C . VAL B 1 13 ? -17.065 32.032 62.076 1.00 11.57 ? 94 VAL B C 1 ATOM 3075 O O . VAL B 1 13 ? -16.703 31.688 63.196 1.00 11.06 ? 94 VAL B O 1 ATOM 3076 C CB . VAL B 1 13 ? -15.294 32.198 60.317 1.00 12.47 ? 94 VAL B CB 1 ATOM 3077 C CG1 . VAL B 1 13 ? -14.436 33.147 59.499 1.00 12.73 ? 94 VAL B CG1 1 ATOM 3078 C CG2 . VAL B 1 13 ? -14.424 31.257 61.120 1.00 12.23 ? 94 VAL B CG2 1 ATOM 3079 N N . SER B 1 14 ? -18.186 31.597 61.510 1.00 11.00 ? 95 SER B N 1 ATOM 3080 C CA . SER B 1 14 ? -19.101 30.704 62.211 1.00 10.41 ? 95 SER B CA 1 ATOM 3081 C C . SER B 1 14 ? -19.025 29.282 61.672 1.00 11.77 ? 95 SER B C 1 ATOM 3082 O O . SER B 1 14 ? -19.545 28.349 62.282 1.00 9.95 ? 95 SER B O 1 ATOM 3083 C CB . SER B 1 14 ? -20.535 31.230 62.105 1.00 11.77 ? 95 SER B CB 1 ATOM 3084 O OG . SER B 1 14 ? -20.960 31.286 60.755 1.00 17.95 ? 95 SER B OG 1 ATOM 3085 N N . GLY B 1 15 ? -18.371 29.120 60.527 1.00 8.34 ? 96 GLY B N 1 ATOM 3086 C CA . GLY B 1 15 ? -18.267 27.819 59.897 1.00 6.41 ? 96 GLY B CA 1 ATOM 3087 C C . GLY B 1 15 ? -17.326 27.823 58.709 1.00 8.11 ? 96 GLY B C 1 ATOM 3088 O O . GLY B 1 15 ? -16.766 28.859 58.346 1.00 7.45 ? 96 GLY B O 1 ATOM 3089 N N . TRP B 1 16 ? -17.161 26.659 58.094 1.00 7.61 ? 97 TRP B N 1 ATOM 3090 C CA . TRP B 1 16 ? -16.170 26.496 57.040 1.00 5.69 ? 97 TRP B CA 1 ATOM 3091 C C . TRP B 1 16 ? -16.788 25.928 55.769 1.00 6.78 ? 97 TRP B C 1 ATOM 3092 O O . TRP B 1 16 ? -17.473 24.902 55.801 1.00 6.67 ? 97 TRP B O 1 ATOM 3093 C CB . TRP B 1 16 ? -15.030 25.613 57.543 1.00 6.69 ? 97 TRP B CB 1 ATOM 3094 C CG . TRP B 1 16 ? -14.496 26.106 58.849 1.00 5.80 ? 97 TRP B CG 1 ATOM 3095 C CD1 . TRP B 1 16 ? -14.956 25.789 60.095 1.00 5.51 ? 97 TRP B CD1 1 ATOM 3096 C CD2 . TRP B 1 16 ? -13.424 27.034 59.041 1.00 4.92 ? 97 TRP B CD2 1 ATOM 3097 N NE1 . TRP B 1 16 ? -14.227 26.453 61.051 1.00 6.75 ? 97 TRP B NE1 1 ATOM 3098 C CE2 . TRP B 1 16 ? -13.279 27.224 60.430 1.00 7.51 ? 97 TRP B CE2 1 ATOM 3099 C CE3 . TRP B 1 16 ? -12.566 27.717 58.173 1.00 5.92 ? 97 TRP B CE3 1 ATOM 3100 C CZ2 . TRP B 1 16 ? -12.313 28.068 60.971 1.00 6.71 ? 97 TRP B CZ2 1 ATOM 3101 C CZ3 . TRP B 1 16 ? -11.608 28.556 58.713 1.00 6.31 ? 97 TRP B CZ3 1 ATOM 3102 C CH2 . TRP B 1 16 ? -11.489 28.724 60.097 1.00 7.05 ? 97 TRP B CH2 1 ATOM 3103 N N . ALA B 1 17 ? -16.553 26.614 54.656 1.00 5.57 ? 98 ALA B N 1 ATOM 3104 C CA . ALA B 1 17 ? -17.096 26.213 53.363 1.00 5.15 ? 98 ALA B CA 1 ATOM 3105 C C . ALA B 1 17 ? -16.002 25.553 52.537 1.00 6.27 ? 98 ALA B C 1 ATOM 3106 O O . ALA B 1 17 ? -14.876 26.042 52.495 1.00 5.53 ? 98 ALA B O 1 ATOM 3107 C CB . ALA B 1 17 ? -17.653 27.423 52.630 1.00 7.01 ? 98 ALA B CB 1 ATOM 3108 N N . ILE B 1 18 ? -16.327 24.442 51.883 1.00 7.55 ? 99 ILE B N 1 ATOM 3109 C CA . ILE B 1 18 ? -15.320 23.714 51.119 1.00 6.99 ? 99 ILE B CA 1 ATOM 3110 C C . ILE B 1 18 ? -14.822 24.533 49.931 1.00 7.05 ? 99 ILE B C 1 ATOM 3111 O O . ILE B 1 18 ? -15.608 25.113 49.179 1.00 6.40 ? 99 ILE B O 1 ATOM 3112 C CB . ILE B 1 18 ? -15.812 22.320 50.668 1.00 9.20 ? 99 ILE B CB 1 ATOM 3113 C CG1 . ILE B 1 18 ? -14.634 21.488 50.152 1.00 8.37 ? 99 ILE B CG1 1 ATOM 3114 C CG2 . ILE B 1 18 ? -16.918 22.441 49.629 1.00 7.36 ? 99 ILE B CG2 1 ATOM 3115 C CD1 . ILE B 1 18 ? -14.896 20.000 50.136 1.00 8.03 ? 99 ILE B CD1 1 ATOM 3116 N N . TYR B 1 19 ? -13.503 24.576 49.778 1.00 5.19 ? 100 TYR B N 1 ATOM 3117 C CA . TYR B 1 19 ? -12.865 25.460 48.815 1.00 5.07 ? 100 TYR B CA 1 ATOM 3118 C C . TYR B 1 19 ? -12.243 24.680 47.658 1.00 6.95 ? 100 TYR B C 1 ATOM 3119 O O . TYR B 1 19 ? -12.382 25.069 46.500 1.00 6.78 ? 100 TYR B O 1 ATOM 3120 C CB . TYR B 1 19 ? -11.805 26.305 49.528 1.00 7.17 ? 100 TYR B CB 1 ATOM 3121 C CG . TYR B 1 19 ? -11.205 27.418 48.700 1.00 9.50 ? 100 TYR B CG 1 ATOM 3122 C CD1 . TYR B 1 19 ? -12.012 28.337 48.043 1.00 13.20 ? 100 TYR B CD1 1 ATOM 3123 C CD2 . TYR B 1 19 ? -9.827 27.571 48.605 1.00 13.55 ? 100 TYR B CD2 1 ATOM 3124 C CE1 . TYR B 1 19 ? -11.464 29.363 47.291 1.00 13.12 ? 100 TYR B CE1 1 ATOM 3125 C CE2 . TYR B 1 19 ? -9.270 28.594 47.859 1.00 15.35 ? 100 TYR B CE2 1 ATOM 3126 C CZ . TYR B 1 19 ? -10.093 29.487 47.207 1.00 13.19 ? 100 TYR B CZ 1 ATOM 3127 O OH . TYR B 1 19 ? -9.542 30.508 46.467 1.00 21.59 ? 100 TYR B OH 1 ATOM 3128 N N . SER B 1 20 ? -11.562 23.580 47.968 1.00 6.89 ? 101 SER B N 1 ATOM 3129 C CA . SER B 1 20 ? -10.948 22.763 46.922 1.00 7.03 ? 101 SER B CA 1 ATOM 3130 C C . SER B 1 20 ? -10.834 21.285 47.293 1.00 7.28 ? 101 SER B C 1 ATOM 3131 O O . SER B 1 20 ? -10.858 20.919 48.469 1.00 7.67 ? 101 SER B O 1 ATOM 3132 C CB . SER B 1 20 ? -9.562 23.306 46.555 1.00 9.83 ? 101 SER B CB 1 ATOM 3133 O OG . SER B 1 20 ? -8.615 23.036 47.578 1.00 10.04 ? 101 SER B OG 1 ATOM 3134 N N . LYS B 1 21 ? -10.724 20.449 46.267 1.00 5.17 ? 102 LYS B N 1 ATOM 3135 C CA . LYS B 1 21 ? -10.414 19.029 46.416 1.00 7.79 ? 102 LYS B CA 1 ATOM 3136 C C . LYS B 1 21 ? -9.761 18.568 45.119 1.00 8.74 ? 102 LYS B C 1 ATOM 3137 O O . LYS B 1 21 ? -10.305 18.795 44.040 1.00 9.82 ? 102 LYS B O 1 ATOM 3138 C CB . LYS B 1 21 ? -11.680 18.214 46.681 1.00 6.25 ? 102 LYS B CB 1 ATOM 3139 C CG . LYS B 1 21 ? -11.402 16.754 47.017 1.00 8.21 ? 102 LYS B CG 1 ATOM 3140 C CD . LYS B 1 21 ? -12.685 15.967 47.224 1.00 8.24 ? 102 LYS B CD 1 ATOM 3141 C CE . LYS B 1 21 ? -12.427 14.696 48.021 1.00 8.96 ? 102 LYS B CE 1 ATOM 3142 N NZ . LYS B 1 21 ? -11.405 13.817 47.388 1.00 13.84 ? 102 LYS B NZ 1 ATOM 3143 N N . ASP B 1 22 ? -8.600 17.926 45.209 1.00 8.18 ? 103 ASP B N 1 ATOM 3144 C CA . ASP B 1 22 ? -7.852 17.586 43.997 1.00 11.84 ? 103 ASP B CA 1 ATOM 3145 C C . ASP B 1 22 ? -8.001 16.142 43.498 1.00 11.49 ? 103 ASP B C 1 ATOM 3146 O O . ASP B 1 22 ? -7.708 15.860 42.335 1.00 10.38 ? 103 ASP B O 1 ATOM 3147 C CB . ASP B 1 22 ? -6.370 17.973 44.133 1.00 8.72 ? 103 ASP B CB 1 ATOM 3148 C CG . ASP B 1 22 ? -5.724 17.402 45.382 1.00 14.34 ? 103 ASP B CG 1 ATOM 3149 O OD1 . ASP B 1 22 ? -6.250 16.413 45.934 1.00 15.07 ? 103 ASP B OD1 1 ATOM 3150 O OD2 . ASP B 1 22 ? -4.682 17.947 45.809 1.00 14.69 ? 103 ASP B OD2 1 ATOM 3151 N N . ASN B 1 23 ? -8.457 15.238 44.362 1.00 6.41 ? 104 ASN B N 1 ATOM 3152 C CA . ASN B 1 23 ? -8.631 13.836 43.981 1.00 9.44 ? 104 ASN B CA 1 ATOM 3153 C C . ASN B 1 23 ? -7.355 13.222 43.404 1.00 8.12 ? 104 ASN B C 1 ATOM 3154 O O . ASN B 1 23 ? -7.410 12.364 42.522 1.00 6.67 ? 104 ASN B O 1 ATOM 3155 C CB . ASN B 1 23 ? -9.774 13.690 42.969 1.00 8.57 ? 104 ASN B CB 1 ATOM 3156 C CG . ASN B 1 23 ? -11.137 13.936 43.586 1.00 9.49 ? 104 ASN B CG 1 ATOM 3157 O OD1 . ASN B 1 23 ? -11.447 13.424 44.659 1.00 10.02 ? 104 ASN B OD1 1 ATOM 3158 N ND2 . ASN B 1 23 ? -11.963 14.718 42.902 1.00 12.73 ? 104 ASN B ND2 1 ATOM 3159 N N . SER B 1 24 ? -6.210 13.656 43.918 1.00 4.92 ? 105 SER B N 1 ATOM 3160 C CA . SER B 1 24 ? -4.913 13.301 43.339 1.00 7.47 ? 105 SER B CA 1 ATOM 3161 C C . SER B 1 24 ? -4.652 11.798 43.224 1.00 7.32 ? 105 SER B C 1 ATOM 3162 O O . SER B 1 24 ? -4.209 11.314 42.181 1.00 7.60 ? 105 SER B O 1 ATOM 3163 C CB . SER B 1 24 ? -3.785 13.961 44.133 1.00 8.83 ? 105 SER B CB 1 ATOM 3164 O OG . SER B 1 24 ? -3.904 15.373 44.096 1.00 15.65 ? 105 SER B OG 1 ATOM 3165 N N . VAL B 1 25 ? -4.912 11.064 44.299 1.00 6.50 ? 106 VAL B N 1 ATOM 3166 C CA . VAL B 1 25 ? -4.602 9.640 44.320 1.00 7.05 ? 106 VAL B CA 1 ATOM 3167 C C . VAL B 1 25 ? -5.526 8.857 43.386 1.00 6.46 ? 106 VAL B C 1 ATOM 3168 O O . VAL B 1 25 ? -5.083 7.949 42.683 1.00 8.51 ? 106 VAL B O 1 ATOM 3169 C CB . VAL B 1 25 ? -4.650 9.062 45.744 1.00 7.31 ? 106 VAL B CB 1 ATOM 3170 C CG1 . VAL B 1 25 ? -4.278 7.588 45.728 1.00 7.55 ? 106 VAL B CG1 1 ATOM 3171 C CG2 . VAL B 1 25 ? -3.711 9.836 46.655 1.00 12.12 ? 106 VAL B CG2 1 ATOM 3172 N N . ARG B 1 26 ? -6.807 9.218 43.368 1.00 6.15 ? 107 ARG B N 1 ATOM 3173 C CA . ARG B 1 26 ? -7.756 8.588 42.454 1.00 5.23 ? 107 ARG B CA 1 ATOM 3174 C C . ARG B 1 26 ? -7.323 8.772 41.000 1.00 8.14 ? 107 ARG B C 1 ATOM 3175 O O . ARG B 1 26 ? -7.305 7.822 40.219 1.00 9.09 ? 107 ARG B O 1 ATOM 3176 C CB . ARG B 1 26 ? -9.163 9.157 42.658 1.00 6.34 ? 107 ARG B CB 1 ATOM 3177 C CG . ARG B 1 26 ? -9.838 8.699 43.941 1.00 8.27 ? 107 ARG B CG 1 ATOM 3178 C CD . ARG B 1 26 ? -11.097 9.502 44.232 1.00 6.52 ? 107 ARG B CD 1 ATOM 3179 N NE . ARG B 1 26 ? -12.055 9.451 43.131 1.00 9.30 ? 107 ARG B NE 1 ATOM 3180 C CZ . ARG B 1 26 ? -13.014 8.537 43.018 1.00 12.71 ? 107 ARG B CZ 1 ATOM 3181 N NH1 . ARG B 1 26 ? -13.142 7.591 43.939 1.00 12.65 ? 107 ARG B NH1 1 ATOM 3182 N NH2 . ARG B 1 26 ? -13.845 8.568 41.985 1.00 10.60 ? 107 ARG B NH2 1 ATOM 3183 N N . ILE B 1 27 ? -6.965 10.000 40.645 1.00 6.68 ? 108 ILE B N 1 ATOM 3184 C CA . ILE B 1 27 ? -6.554 10.312 39.281 1.00 6.07 ? 108 ILE B CA 1 ATOM 3185 C C . ILE B 1 27 ? -5.198 9.686 38.946 1.00 7.36 ? 108 ILE B C 1 ATOM 3186 O O . ILE B 1 27 ? -4.977 9.230 37.825 1.00 8.97 ? 108 ILE B O 1 ATOM 3187 C CB . ILE B 1 27 ? -6.536 11.836 39.044 1.00 6.84 ? 108 ILE B CB 1 ATOM 3188 C CG1 . ILE B 1 27 ? -7.965 12.382 39.129 1.00 9.72 ? 108 ILE B CG1 1 ATOM 3189 C CG2 . ILE B 1 27 ? -5.907 12.168 37.697 1.00 7.07 ? 108 ILE B CG2 1 ATOM 3190 C CD1 . ILE B 1 27 ? -8.051 13.883 39.262 1.00 14.68 ? 108 ILE B CD1 1 ATOM 3191 N N . GLY B 1 28 ? -4.306 9.648 39.930 1.00 6.83 ? 109 GLY B N 1 ATOM 3192 C CA . GLY B 1 28 ? -2.976 9.092 39.745 1.00 8.22 ? 109 GLY B CA 1 ATOM 3193 C C . GLY B 1 28 ? -2.968 7.603 39.447 1.00 9.56 ? 109 GLY B C 1 ATOM 3194 O O . GLY B 1 28 ? -1.942 7.048 39.056 1.00 9.30 ? 109 GLY B O 1 ATOM 3195 N N . SER B 1 29 ? -4.111 6.952 39.637 1.00 9.83 ? 110 SER B N 1 ATOM 3196 C CA . SER B 1 29 ? -4.247 5.535 39.314 1.00 10.60 ? 110 SER B CA 1 ATOM 3197 C C . SER B 1 29 ? -3.921 5.292 37.839 1.00 13.45 ? 110 SER B C 1 ATOM 3198 O O . SER B 1 29 ? -3.332 4.270 37.481 1.00 15.33 ? 110 SER B O 1 ATOM 3199 C CB . SER B 1 29 ? -5.662 5.048 39.642 1.00 14.27 ? 110 SER B CB 1 ATOM 3200 O OG . SER B 1 29 ? -5.811 3.661 39.385 1.00 15.64 ? 110 SER B OG 1 ATOM 3201 N N . LYS B 1 30 ? -4.305 6.238 36.988 1.00 12.63 ? 111 LYS B N 1 ATOM 3202 C CA . LYS B 1 30 ? -4.006 6.148 35.562 1.00 13.33 ? 111 LYS B CA 1 ATOM 3203 C C . LYS B 1 30 ? -3.152 7.314 35.086 1.00 13.69 ? 111 LYS B C 1 ATOM 3204 O O . LYS B 1 30 ? -2.212 7.127 34.317 1.00 14.89 ? 111 LYS B O 1 ATOM 3205 C CB . LYS B 1 30 ? -5.285 6.089 34.723 1.00 14.54 ? 111 LYS B CB 1 ATOM 3206 C CG . LYS B 1 30 ? -5.002 6.175 33.225 1.00 14.78 ? 111 LYS B CG 1 ATOM 3207 C CD . LYS B 1 30 ? -6.261 6.180 32.382 1.00 17.19 ? 111 LYS B CD 1 ATOM 3208 C CE . LYS B 1 30 ? -5.915 6.365 30.908 1.00 17.50 ? 111 LYS B CE 1 ATOM 3209 N NZ . LYS B 1 30 ? -7.111 6.315 30.024 1.00 26.36 ? 111 LYS B NZ 1 ATOM 3210 N N . GLY B 1 31 ? -3.493 8.517 35.544 1.00 12.09 ? 112 GLY B N 1 ATOM 3211 C CA . GLY B 1 31 ? -2.806 9.727 35.127 1.00 11.39 ? 112 GLY B CA 1 ATOM 3212 C C . GLY B 1 31 ? -1.380 9.821 35.637 1.00 11.44 ? 112 GLY B C 1 ATOM 3213 O O . GLY B 1 31 ? -0.966 9.041 36.489 1.00 13.71 ? 112 GLY B O 1 ATOM 3214 N N . ASP B 1 32 ? -0.626 10.778 35.107 1.00 10.31 ? 113 ASP B N 1 ATOM 3215 C CA . ASP B 1 32 ? 0.746 10.999 35.545 1.00 9.39 ? 113 ASP B CA 1 ATOM 3216 C C . ASP B 1 32 ? 0.760 12.000 36.689 1.00 7.30 ? 113 ASP B C 1 ATOM 3217 O O . ASP B 1 32 ? 0.814 13.210 36.473 1.00 9.19 ? 113 ASP B O 1 ATOM 3218 C CB . ASP B 1 32 ? 1.609 11.488 34.382 1.00 10.34 ? 113 ASP B CB 1 ATOM 3219 C CG . ASP B 1 32 ? 1.755 10.445 33.291 1.00 11.48 ? 113 ASP B CG 1 ATOM 3220 O OD1 . ASP B 1 32 ? 1.630 9.239 33.598 1.00 11.20 ? 113 ASP B OD1 1 ATOM 3221 O OD2 . ASP B 1 32 ? 1.992 10.830 32.129 1.00 14.78 ? 113 ASP B OD2 1 ATOM 3222 N N . VAL B 1 33 ? 0.700 11.480 37.910 1.00 6.88 ? 114 VAL B N 1 ATOM 3223 C CA . VAL B 1 33 ? 0.573 12.312 39.099 1.00 5.92 ? 114 VAL B CA 1 ATOM 3224 C C . VAL B 1 33 ? 1.720 12.038 40.065 1.00 5.86 ? 114 VAL B C 1 ATOM 3225 O O . VAL B 1 33 ? 2.056 10.883 40.326 1.00 5.44 ? 114 VAL B O 1 ATOM 3226 C CB . VAL B 1 33 ? -0.778 12.052 39.804 1.00 8.35 ? 114 VAL B CB 1 ATOM 3227 C CG1 . VAL B 1 33 ? -0.891 12.865 41.090 1.00 7.48 ? 114 VAL B CG1 1 ATOM 3228 C CG2 . VAL B 1 33 ? -1.935 12.366 38.861 1.00 8.04 ? 114 VAL B CG2 1 ATOM 3229 N N . PHE B 1 34 ? 2.330 13.101 40.583 1.00 5.70 ? 115 PHE B N 1 ATOM 3230 C CA . PHE B 1 34 ? 3.443 12.959 41.517 1.00 4.97 ? 115 PHE B CA 1 ATOM 3231 C C . PHE B 1 34 ? 3.031 12.223 42.782 1.00 6.90 ? 115 PHE B C 1 ATOM 3232 O O . PHE B 1 34 ? 1.923 12.406 43.286 1.00 4.38 ? 115 PHE B O 1 ATOM 3233 C CB . PHE B 1 34 ? 3.993 14.328 41.930 1.00 6.94 ? 115 PHE B CB 1 ATOM 3234 C CG . PHE B 1 34 ? 4.853 14.988 40.891 1.00 8.19 ? 115 PHE B CG 1 ATOM 3235 C CD1 . PHE B 1 34 ? 6.026 14.392 40.459 1.00 8.59 ? 115 PHE B CD1 1 ATOM 3236 C CD2 . PHE B 1 34 ? 4.505 16.223 40.373 1.00 6.58 ? 115 PHE B CD2 1 ATOM 3237 C CE1 . PHE B 1 34 ? 6.825 15.007 39.510 1.00 12.05 ? 115 PHE B CE1 1 ATOM 3238 C CE2 . PHE B 1 34 ? 5.301 16.844 39.423 1.00 7.44 ? 115 PHE B CE2 1 ATOM 3239 C CZ . PHE B 1 34 ? 6.461 16.235 38.993 1.00 8.72 ? 115 PHE B CZ 1 ATOM 3240 N N . VAL B 1 35 ? 3.932 11.392 43.293 1.00 8.09 ? 116 VAL B N 1 ATOM 3241 C CA . VAL B 1 35 ? 3.832 10.936 44.667 1.00 8.39 ? 116 VAL B CA 1 ATOM 3242 C C . VAL B 1 35 ? 4.229 12.129 45.521 1.00 9.15 ? 116 VAL B C 1 ATOM 3243 O O . VAL B 1 35 ? 5.327 12.663 45.369 1.00 7.44 ? 116 VAL B O 1 ATOM 3244 C CB . VAL B 1 35 ? 4.798 9.773 44.948 1.00 11.21 ? 116 VAL B CB 1 ATOM 3245 C CG1 . VAL B 1 35 ? 4.754 9.386 46.418 1.00 12.63 ? 116 VAL B CG1 1 ATOM 3246 C CG2 . VAL B 1 35 ? 4.460 8.581 44.065 1.00 13.82 ? 116 VAL B CG2 1 ATOM 3247 N N . ILE B 1 36 ? 3.334 12.570 46.398 1.00 8.25 ? 117 ILE B N 1 ATOM 3248 C CA . ILE B 1 36 ? 3.612 13.750 47.206 1.00 8.74 ? 117 ILE B CA 1 ATOM 3249 C C . ILE B 1 36 ? 3.227 13.575 48.666 1.00 12.30 ? 117 ILE B C 1 ATOM 3250 O O . ILE B 1 36 ? 2.449 12.692 49.024 1.00 11.14 ? 117 ILE B O 1 ATOM 3251 C CB . ILE B 1 36 ? 2.850 14.986 46.697 1.00 8.67 ? 117 ILE B CB 1 ATOM 3252 C CG1 . ILE B 1 36 ? 1.375 14.892 47.093 1.00 11.46 ? 117 ILE B CG1 1 ATOM 3253 C CG2 . ILE B 1 36 ? 3.009 15.145 45.189 1.00 8.05 ? 117 ILE B CG2 1 ATOM 3254 C CD1 . ILE B 1 36 ? 0.646 16.212 47.014 1.00 21.34 ? 117 ILE B CD1 1 ATOM 3255 N N . ARG B 1 37 ? 3.781 14.440 49.502 1.00 8.47 ? 118 ARG B N 1 ATOM 3256 C CA . ARG B 1 37 ? 3.324 14.585 50.872 1.00 9.04 ? 118 ARG B CA 1 ATOM 3257 C C . ARG B 1 37 ? 3.578 16.014 51.319 1.00 13.36 ? 118 ARG B C 1 ATOM 3258 O O . ARG B 1 37 ? 4.234 16.784 50.616 1.00 13.08 ? 118 ARG B O 1 ATOM 3259 C CB . ARG B 1 37 ? 4.010 13.585 51.805 1.00 11.34 ? 118 ARG B CB 1 ATOM 3260 C CG . ARG B 1 37 ? 3.268 12.261 51.931 1.00 11.42 ? 118 ARG B CG 1 ATOM 3261 C CD . ARG B 1 37 ? 3.297 11.754 53.360 1.00 15.29 ? 118 ARG B CD 1 ATOM 3262 N NE . ARG B 1 37 ? 2.739 12.731 54.289 1.00 11.43 ? 118 ARG B NE 1 ATOM 3263 C CZ . ARG B 1 37 ? 3.026 12.772 55.586 1.00 12.73 ? 118 ARG B CZ 1 ATOM 3264 N NH1 . ARG B 1 37 ? 3.873 11.895 56.107 1.00 18.38 ? 118 ARG B NH1 1 ATOM 3265 N NH2 . ARG B 1 37 ? 2.476 13.696 56.361 1.00 10.78 ? 118 ARG B NH2 1 ATOM 3266 N N . GLU B 1 38 ? 3.047 16.370 52.481 1.00 14.42 ? 119 GLU B N 1 ATOM 3267 C CA . GLU B 1 38 ? 3.207 17.718 53.005 1.00 17.39 ? 119 GLU B CA 1 ATOM 3268 C C . GLU B 1 38 ? 2.723 18.771 52.011 1.00 14.83 ? 119 GLU B C 1 ATOM 3269 O O . GLU B 1 38 ? 3.452 19.710 51.687 1.00 18.01 ? 119 GLU B O 1 ATOM 3270 C CB . GLU B 1 38 ? 4.670 17.983 53.381 1.00 14.99 ? 119 GLU B CB 1 ATOM 3271 C CG . GLU B 1 38 ? 5.195 17.128 54.531 1.00 21.08 ? 119 GLU B CG 1 ATOM 3272 C CD . GLU B 1 38 ? 5.753 15.788 54.078 1.00 24.85 ? 119 GLU B CD 1 ATOM 3273 O OE1 . GLU B 1 38 ? 5.761 14.842 54.894 1.00 22.63 ? 119 GLU B OE1 1 ATOM 3274 O OE2 . GLU B 1 38 ? 6.190 15.679 52.912 1.00 22.05 ? 119 GLU B OE2 1 ATOM 3275 N N . PRO B 1 39 ? 1.489 18.621 51.514 1.00 13.97 ? 120 PRO B N 1 ATOM 3276 C CA . PRO B 1 39 ? 0.986 19.699 50.667 1.00 12.00 ? 120 PRO B CA 1 ATOM 3277 C C . PRO B 1 39 ? 0.622 20.880 51.548 1.00 17.07 ? 120 PRO B C 1 ATOM 3278 O O . PRO B 1 39 ? 0.330 20.690 52.729 1.00 17.77 ? 120 PRO B O 1 ATOM 3279 C CB . PRO B 1 39 ? -0.276 19.094 50.060 1.00 14.89 ? 120 PRO B CB 1 ATOM 3280 C CG . PRO B 1 39 ? -0.758 18.147 51.109 1.00 13.92 ? 120 PRO B CG 1 ATOM 3281 C CD . PRO B 1 39 ? 0.484 17.562 51.721 1.00 13.60 ? 120 PRO B CD 1 ATOM 3282 N N . PHE B 1 40 ? 0.661 22.083 50.995 1.00 6.73 ? 121 PHE B N 1 ATOM 3283 C CA . PHE B 1 40 ? 0.139 23.238 51.706 1.00 5.81 ? 121 PHE B CA 1 ATOM 3284 C C . PHE B 1 40 ? -0.265 24.319 50.721 1.00 8.14 ? 121 PHE B C 1 ATOM 3285 O O . PHE B 1 40 ? 0.226 24.362 49.595 1.00 9.44 ? 121 PHE B O 1 ATOM 3286 C CB . PHE B 1 40 ? 1.122 23.762 52.767 1.00 6.92 ? 121 PHE B CB 1 ATOM 3287 C CG . PHE B 1 40 ? 2.409 24.321 52.208 1.00 5.44 ? 121 PHE B CG 1 ATOM 3288 C CD1 . PHE B 1 40 ? 2.516 25.667 51.893 1.00 5.11 ? 121 PHE B CD1 1 ATOM 3289 C CD2 . PHE B 1 40 ? 3.517 23.508 52.036 1.00 6.84 ? 121 PHE B CD2 1 ATOM 3290 C CE1 . PHE B 1 40 ? 3.696 26.189 51.399 1.00 4.81 ? 121 PHE B CE1 1 ATOM 3291 C CE2 . PHE B 1 40 ? 4.705 24.025 51.541 1.00 6.00 ? 121 PHE B CE2 1 ATOM 3292 C CZ . PHE B 1 40 ? 4.792 25.369 51.223 1.00 6.37 ? 121 PHE B CZ 1 ATOM 3293 N N . ILE B 1 41 ? -1.183 25.178 51.139 1.00 5.74 ? 122 ILE B N 1 ATOM 3294 C CA . ILE B 1 41 ? -1.685 26.221 50.260 1.00 6.31 ? 122 ILE B CA 1 ATOM 3295 C C . ILE B 1 41 ? -1.147 27.583 50.684 1.00 7.14 ? 122 ILE B C 1 ATOM 3296 O O . ILE B 1 41 ? -0.941 27.840 51.869 1.00 5.22 ? 122 ILE B O 1 ATOM 3297 C CB . ILE B 1 41 ? -3.220 26.221 50.238 1.00 6.41 ? 122 ILE B CB 1 ATOM 3298 C CG1 . ILE B 1 41 ? -3.720 24.901 49.648 1.00 8.63 ? 122 ILE B CG1 1 ATOM 3299 C CG2 . ILE B 1 41 ? -3.757 27.409 49.450 1.00 6.82 ? 122 ILE B CG2 1 ATOM 3300 C CD1 . ILE B 1 41 ? -5.205 24.718 49.754 1.00 10.53 ? 122 ILE B CD1 1 ATOM 3301 N N . SER B 1 42 ? -0.888 28.437 49.700 1.00 8.81 ? 123 SER B N 1 ATOM 3302 C CA . SER B 1 42 ? -0.463 29.805 49.956 1.00 8.21 ? 123 SER B CA 1 ATOM 3303 C C . SER B 1 42 ? -0.969 30.682 48.818 1.00 6.94 ? 123 SER B C 1 ATOM 3304 O O . SER B 1 42 ? -1.025 30.243 47.670 1.00 8.30 ? 123 SER B O 1 ATOM 3305 C CB . SER B 1 42 ? 1.060 29.895 50.072 1.00 11.34 ? 123 SER B CB 1 ATOM 3306 O OG . SER B 1 42 ? 1.453 31.142 50.628 1.00 10.68 ? 123 SER B OG 1 ATOM 3307 N N . CYS B 1 43 ? -1.334 31.919 49.138 1.00 6.72 ? 124 CYS B N 1 ATOM 3308 C CA . CYS B 1 43 ? -1.977 32.796 48.166 1.00 10.76 ? 124 CYS B CA 1 ATOM 3309 C C . CYS B 1 43 ? -1.178 34.067 47.896 1.00 12.92 ? 124 CYS B C 1 ATOM 3310 O O . CYS B 1 43 ? -0.407 34.523 48.736 1.00 8.75 ? 124 CYS B O 1 ATOM 3311 C CB . CYS B 1 43 ? -3.393 33.159 48.631 1.00 9.06 ? 124 CYS B CB 1 ATOM 3312 S SG . CYS B 1 43 ? -4.485 31.743 48.930 1.00 14.68 ? 124 CYS B SG 1 ATOM 3313 N N . SER B 1 44 ? -1.363 34.622 46.703 1.00 15.14 ? 125 SER B N 1 ATOM 3314 C CA . SER B 1 44 ? -0.801 35.916 46.353 1.00 16.51 ? 125 SER B CA 1 ATOM 3315 C C . SER B 1 44 ? -1.958 36.908 46.286 1.00 14.87 ? 125 SER B C 1 ATOM 3316 O O . SER B 1 44 ? -3.090 36.557 46.621 1.00 17.51 ? 125 SER B O 1 ATOM 3317 C CB . SER B 1 44 ? -0.080 35.833 45.007 1.00 14.19 ? 125 SER B CB 1 ATOM 3318 O OG . SER B 1 44 ? -1.001 35.647 43.945 1.00 18.34 ? 125 SER B OG 1 ATOM 3319 N N . PRO B 1 45 ? -1.686 38.155 45.870 1.00 13.82 ? 126 PRO B N 1 ATOM 3320 C CA . PRO B 1 45 ? -2.813 39.073 45.672 1.00 15.05 ? 126 PRO B CA 1 ATOM 3321 C C . PRO B 1 45 ? -3.667 38.676 44.470 1.00 17.75 ? 126 PRO B C 1 ATOM 3322 O O . PRO B 1 45 ? -4.719 39.274 44.241 1.00 20.09 ? 126 PRO B O 1 ATOM 3323 C CB . PRO B 1 45 ? -2.128 40.418 45.400 1.00 18.67 ? 126 PRO B CB 1 ATOM 3324 C CG . PRO B 1 45 ? -0.759 40.280 45.980 1.00 15.17 ? 126 PRO B CG 1 ATOM 3325 C CD . PRO B 1 45 ? -0.388 38.845 45.774 1.00 12.73 ? 126 PRO B CD 1 ATOM 3326 N N . LEU B 1 46 ? -3.221 37.677 43.714 1.00 17.77 ? 127 LEU B N 1 ATOM 3327 C CA . LEU B 1 46 ? -3.902 37.299 42.479 1.00 20.38 ? 127 LEU B CA 1 ATOM 3328 C C . LEU B 1 46 ? -4.459 35.875 42.479 1.00 22.49 ? 127 LEU B C 1 ATOM 3329 O O . LEU B 1 46 ? -5.532 35.628 41.930 1.00 23.02 ? 127 LEU B O 1 ATOM 3330 C CB . LEU B 1 46 ? -2.972 37.491 41.278 1.00 20.96 ? 127 LEU B CB 1 ATOM 3331 C CG . LEU B 1 46 ? -2.571 38.935 40.973 1.00 25.65 ? 127 LEU B CG 1 ATOM 3332 C CD1 . LEU B 1 46 ? -1.572 38.986 39.828 1.00 28.16 ? 127 LEU B CD1 1 ATOM 3333 C CD2 . LEU B 1 46 ? -3.805 39.770 40.656 1.00 25.72 ? 127 LEU B CD2 1 ATOM 3334 N N . GLU B 1 47 ? -3.732 34.941 43.085 1.00 16.34 ? 128 GLU B N 1 ATOM 3335 C CA . GLU B 1 47 ? -4.125 33.535 43.019 1.00 16.28 ? 128 GLU B CA 1 ATOM 3336 C C . GLU B 1 47 ? -3.676 32.724 44.229 1.00 16.34 ? 128 GLU B C 1 ATOM 3337 O O . GLU B 1 47 ? -2.846 33.165 45.020 1.00 16.27 ? 128 GLU B O 1 ATOM 3338 C CB . GLU B 1 47 ? -3.568 32.886 41.751 1.00 18.74 ? 128 GLU B CB 1 ATOM 3339 C CG . GLU B 1 47 ? -2.056 32.722 41.759 1.00 22.62 ? 128 GLU B CG 1 ATOM 3340 C CD . GLU B 1 47 ? -1.552 31.883 40.600 1.00 30.91 ? 128 GLU B CD 1 ATOM 3341 O OE1 . GLU B 1 47 ? -2.379 31.459 39.767 1.00 35.33 ? 128 GLU B OE1 1 ATOM 3342 O OE2 . GLU B 1 47 ? -0.327 31.648 40.524 1.00 27.12 ? 128 GLU B OE2 1 ATOM 3343 N N . CYS B 1 48 ? -4.235 31.528 44.355 1.00 11.03 ? 129 CYS B N 1 ATOM 3344 C CA . CYS B 1 48 ? -3.850 30.604 45.408 1.00 10.26 ? 129 CYS B CA 1 ATOM 3345 C C . CYS B 1 48 ? -3.222 29.369 44.786 1.00 11.23 ? 129 CYS B C 1 ATOM 3346 O O . CYS B 1 48 ? -3.715 28.847 43.785 1.00 10.21 ? 129 CYS B O 1 ATOM 3347 C CB . CYS B 1 48 ? -5.064 30.220 46.257 1.00 18.57 ? 129 CYS B CB 1 ATOM 3348 S SG . CYS B 1 48 ? -5.697 31.564 47.293 1.00 20.61 ? 129 CYS B SG 1 ATOM 3349 N N . ARG B 1 49 ? -2.128 28.905 45.377 1.00 8.17 ? 130 ARG B N 1 ATOM 3350 C CA . ARG B 1 49 ? -1.408 27.762 44.837 1.00 5.99 ? 130 ARG B CA 1 ATOM 3351 C C . ARG B 1 49 ? -1.227 26.667 45.876 1.00 8.40 ? 130 ARG B C 1 ATOM 3352 O O . ARG B 1 49 ? -1.125 26.940 47.071 1.00 8.31 ? 130 ARG B O 1 ATOM 3353 C CB . ARG B 1 49 ? -0.040 28.201 44.307 1.00 9.26 ? 130 ARG B CB 1 ATOM 3354 C CG . ARG B 1 49 ? -0.105 29.274 43.232 1.00 12.86 ? 130 ARG B CG 1 ATOM 3355 C CD . ARG B 1 49 ? 1.276 29.590 42.670 1.00 13.16 ? 130 ARG B CD 1 ATOM 3356 N NE . ARG B 1 49 ? 1.896 28.425 42.043 1.00 12.81 ? 130 ARG B NE 1 ATOM 3357 C CZ . ARG B 1 49 ? 1.647 28.023 40.801 1.00 14.53 ? 130 ARG B CZ 1 ATOM 3358 N NH1 . ARG B 1 49 ? 0.780 28.687 40.048 1.00 16.61 ? 130 ARG B NH1 1 ATOM 3359 N NH2 . ARG B 1 49 ? 2.258 26.953 40.311 1.00 10.61 ? 130 ARG B NH2 1 ATOM 3360 N N . THR B 1 50 ? -1.184 25.425 45.409 1.00 9.40 ? 131 THR B N 1 ATOM 3361 C CA . THR B 1 50 ? -0.856 24.295 46.263 1.00 10.18 ? 131 THR B CA 1 ATOM 3362 C C . THR B 1 50 ? 0.625 23.977 46.125 1.00 9.44 ? 131 THR B C 1 ATOM 3363 O O . THR B 1 50 ? 1.105 23.688 45.031 1.00 9.64 ? 131 THR B O 1 ATOM 3364 C CB . THR B 1 50 ? -1.667 23.042 45.883 1.00 12.99 ? 131 THR B CB 1 ATOM 3365 O OG1 . THR B 1 50 ? -3.061 23.292 46.092 1.00 19.10 ? 131 THR B OG1 1 ATOM 3366 C CG2 . THR B 1 50 ? -1.239 21.852 46.731 1.00 14.40 ? 131 THR B CG2 1 ATOM 3367 N N . PHE B 1 51 ? 1.351 24.053 47.233 1.00 4.60 ? 132 PHE B N 1 ATOM 3368 C CA . PHE B 1 51 ? 2.745 23.637 47.260 1.00 5.11 ? 132 PHE B CA 1 ATOM 3369 C C . PHE B 1 51 ? 2.816 22.208 47.785 1.00 5.97 ? 132 PHE B C 1 ATOM 3370 O O . PHE B 1 51 ? 1.930 21.767 48.509 1.00 6.78 ? 132 PHE B O 1 ATOM 3371 C CB . PHE B 1 51 ? 3.568 24.578 48.142 1.00 4.78 ? 132 PHE B CB 1 ATOM 3372 C CG . PHE B 1 51 ? 3.752 25.951 47.556 1.00 4.86 ? 132 PHE B CG 1 ATOM 3373 C CD1 . PHE B 1 51 ? 2.744 26.897 47.643 1.00 6.72 ? 132 PHE B CD1 1 ATOM 3374 C CD2 . PHE B 1 51 ? 4.935 26.295 46.918 1.00 4.76 ? 132 PHE B CD2 1 ATOM 3375 C CE1 . PHE B 1 51 ? 2.910 28.162 47.101 1.00 9.92 ? 132 PHE B CE1 1 ATOM 3376 C CE2 . PHE B 1 51 ? 5.107 27.555 46.375 1.00 6.88 ? 132 PHE B CE2 1 ATOM 3377 C CZ . PHE B 1 51 ? 4.094 28.491 46.468 1.00 7.18 ? 132 PHE B CZ 1 ATOM 3378 N N . PHE B 1 52 ? 3.866 21.484 47.418 1.00 5.04 ? 133 PHE B N 1 ATOM 3379 C CA . PHE B 1 52 ? 4.005 20.100 47.852 1.00 7.39 ? 133 PHE B CA 1 ATOM 3380 C C . PHE B 1 52 ? 5.429 19.587 47.698 1.00 8.51 ? 133 PHE B C 1 ATOM 3381 O O . PHE B 1 52 ? 6.204 20.096 46.887 1.00 5.83 ? 133 PHE B O 1 ATOM 3382 C CB . PHE B 1 52 ? 3.037 19.197 47.081 1.00 5.70 ? 133 PHE B CB 1 ATOM 3383 C CG . PHE B 1 52 ? 3.101 19.372 45.589 1.00 8.65 ? 133 PHE B CG 1 ATOM 3384 C CD1 . PHE B 1 52 ? 2.254 20.259 44.946 1.00 8.88 ? 133 PHE B CD1 1 ATOM 3385 C CD2 . PHE B 1 52 ? 4.009 18.653 44.832 1.00 8.71 ? 133 PHE B CD2 1 ATOM 3386 C CE1 . PHE B 1 52 ? 2.311 20.425 43.572 1.00 7.34 ? 133 PHE B CE1 1 ATOM 3387 C CE2 . PHE B 1 52 ? 4.070 18.814 43.458 1.00 10.33 ? 133 PHE B CE2 1 ATOM 3388 C CZ . PHE B 1 52 ? 3.220 19.702 42.830 1.00 10.51 ? 133 PHE B CZ 1 ATOM 3389 N N . LEU B 1 53 ? 5.765 18.573 48.488 1.00 5.03 ? 134 LEU B N 1 ATOM 3390 C CA . LEU B 1 53 ? 7.057 17.916 48.375 1.00 5.44 ? 134 LEU B CA 1 ATOM 3391 C C . LEU B 1 53 ? 6.896 16.618 47.600 1.00 8.08 ? 134 LEU B C 1 ATOM 3392 O O . LEU B 1 53 ? 6.205 15.700 48.044 1.00 7.03 ? 134 LEU B O 1 ATOM 3393 C CB . LEU B 1 53 ? 7.644 17.635 49.761 1.00 7.62 ? 134 LEU B CB 1 ATOM 3394 C CG . LEU B 1 53 ? 7.985 18.851 50.619 1.00 7.51 ? 134 LEU B CG 1 ATOM 3395 C CD1 . LEU B 1 53 ? 8.626 18.413 51.933 1.00 11.13 ? 134 LEU B CD1 1 ATOM 3396 C CD2 . LEU B 1 53 ? 8.902 19.801 49.865 1.00 8.08 ? 134 LEU B CD2 1 ATOM 3397 N N . THR B 1 54 ? 7.522 16.551 46.431 1.00 9.55 ? 135 THR B N 1 ATOM 3398 C CA . THR B 1 54 ? 7.482 15.347 45.617 1.00 10.94 ? 135 THR B CA 1 ATOM 3399 C C . THR B 1 54 ? 8.513 14.350 46.120 1.00 11.80 ? 135 THR B C 1 ATOM 3400 O O . THR B 1 54 ? 9.388 14.691 46.913 1.00 13.08 ? 135 THR B O 1 ATOM 3401 C CB . THR B 1 54 ? 7.797 15.646 44.139 1.00 11.59 ? 135 THR B CB 1 ATOM 3402 O OG1 . THR B 1 54 ? 9.197 15.916 43.993 1.00 13.38 ? 135 THR B OG1 1 ATOM 3403 C CG2 . THR B 1 54 ? 6.996 16.838 43.643 1.00 10.65 ? 135 THR B CG2 1 ATOM 3404 N N . GLN B 1 55 ? 8.403 13.114 45.651 1.00 12.23 ? 136 GLN B N 1 ATOM 3405 C CA . GLN B 1 55 ? 9.414 12.101 45.908 1.00 11.45 ? 136 GLN B CA 1 ATOM 3406 C C . GLN B 1 55 ? 10.196 11.859 44.621 1.00 11.24 ? 136 GLN B C 1 ATOM 3407 O O . GLN B 1 55 ? 10.955 10.897 44.510 1.00 13.59 ? 136 GLN B O 1 ATOM 3408 C CB . GLN B 1 55 ? 8.758 10.802 46.383 1.00 11.99 ? 136 GLN B CB 1 ATOM 3409 C CG . GLN B 1 55 ? 8.060 10.908 47.733 1.00 16.24 ? 136 GLN B CG 1 ATOM 3410 C CD . GLN B 1 55 ? 9.033 10.896 48.898 1.00 21.22 ? 136 GLN B CD 1 ATOM 3411 O OE1 . GLN B 1 55 ? 10.249 10.943 48.709 1.00 19.48 ? 136 GLN B OE1 1 ATOM 3412 N NE2 . GLN B 1 55 ? 8.500 10.827 50.114 1.00 20.29 ? 136 GLN B NE2 1 ATOM 3413 N N . GLY B 1 56 ? 10.002 12.744 43.647 1.00 10.65 ? 137 GLY B N 1 ATOM 3414 C CA . GLY B 1 56 ? 10.641 12.607 42.353 1.00 9.84 ? 137 GLY B CA 1 ATOM 3415 C C . GLY B 1 56 ? 10.179 11.350 41.647 1.00 12.52 ? 137 GLY B C 1 ATOM 3416 O O . GLY B 1 56 ? 10.949 10.703 40.935 1.00 11.34 ? 137 GLY B O 1 ATOM 3417 N N . ALA B 1 57 ? 8.911 11.003 41.850 1.00 6.52 ? 138 ALA B N 1 ATOM 3418 C CA . ALA B 1 57 ? 8.340 9.792 41.271 1.00 10.41 ? 138 ALA B CA 1 ATOM 3419 C C . ALA B 1 57 ? 6.839 9.943 41.051 1.00 6.81 ? 138 ALA B C 1 ATOM 3420 O O . ALA B 1 57 ? 6.193 10.789 41.668 1.00 6.55 ? 138 ALA B O 1 ATOM 3421 C CB . ALA B 1 57 ? 8.623 8.595 42.160 1.00 10.27 ? 138 ALA B CB 1 ATOM 3422 N N . LEU B 1 58 ? 6.290 9.113 40.170 1.00 5.18 ? 139 LEU B N 1 ATOM 3423 C CA . LEU B 1 58 ? 4.864 9.147 39.874 1.00 7.08 ? 139 LEU B CA 1 ATOM 3424 C C . LEU B 1 58 ? 4.135 7.969 40.510 1.00 8.76 ? 139 LEU B C 1 ATOM 3425 O O . LEU B 1 58 ? 4.722 6.911 40.739 1.00 8.48 ? 139 LEU B O 1 ATOM 3426 C CB . LEU B 1 58 ? 4.630 9.138 38.361 1.00 5.97 ? 139 LEU B CB 1 ATOM 3427 C CG . LEU B 1 58 ? 5.238 10.285 37.553 1.00 6.34 ? 139 LEU B CG 1 ATOM 3428 C CD1 . LEU B 1 58 ? 4.879 10.138 36.080 1.00 8.78 ? 139 LEU B CD1 1 ATOM 3429 C CD2 . LEU B 1 58 ? 4.768 11.630 38.090 1.00 6.09 ? 139 LEU B CD2 1 ATOM 3430 N N . LEU B 1 59 ? 2.850 8.161 40.789 1.00 8.78 ? 140 LEU B N 1 ATOM 3431 C CA . LEU B 1 59 ? 2.012 7.097 41.324 1.00 9.56 ? 140 LEU B CA 1 ATOM 3432 C C . LEU B 1 59 ? 1.906 5.939 40.342 1.00 11.33 ? 140 LEU B C 1 ATOM 3433 O O . LEU B 1 59 ? 1.909 6.139 39.127 1.00 10.14 ? 140 LEU B O 1 ATOM 3434 C CB . LEU B 1 59 ? 0.616 7.629 41.649 1.00 8.12 ? 140 LEU B CB 1 ATOM 3435 C CG . LEU B 1 59 ? 0.483 8.491 42.904 1.00 9.95 ? 140 LEU B CG 1 ATOM 3436 C CD1 . LEU B 1 59 ? -0.824 9.274 42.885 1.00 11.54 ? 140 LEU B CD1 1 ATOM 3437 C CD2 . LEU B 1 59 ? 0.583 7.629 44.155 1.00 11.03 ? 140 LEU B CD2 1 ATOM 3438 N N . ASN B 1 60 ? 1.812 4.729 40.883 1.00 9.92 ? 141 ASN B N 1 ATOM 3439 C CA . ASN B 1 60 ? 1.684 3.519 40.081 1.00 9.67 ? 141 ASN B CA 1 ATOM 3440 C C . ASN B 1 60 ? 2.915 3.226 39.223 1.00 13.12 ? 141 ASN B C 1 ATOM 3441 O O . ASN B 1 60 ? 2.829 2.527 38.214 1.00 14.66 ? 141 ASN B O 1 ATOM 3442 C CB . ASN B 1 60 ? 0.414 3.562 39.221 1.00 11.56 ? 141 ASN B CB 1 ATOM 3443 C CG . ASN B 1 60 ? -0.451 2.328 39.400 1.00 15.10 ? 141 ASN B CG 1 ATOM 3444 O OD1 . ASN B 1 60 ? -0.060 1.378 40.078 1.00 13.70 ? 141 ASN B OD1 1 ATOM 3445 N ND2 . ASN B 1 60 ? -1.634 2.337 38.795 1.00 13.02 ? 141 ASN B ND2 1 ATOM 3446 N N . ASP B 1 61 ? 4.060 3.765 39.632 1.00 10.73 ? 142 ASP B N 1 ATOM 3447 C CA . ASP B 1 61 ? 5.331 3.441 38.996 1.00 11.53 ? 142 ASP B CA 1 ATOM 3448 C C . ASP B 1 61 ? 6.294 2.876 40.033 1.00 10.52 ? 142 ASP B C 1 ATOM 3449 O O . ASP B 1 61 ? 6.168 3.164 41.222 1.00 11.29 ? 142 ASP B O 1 ATOM 3450 C CB . ASP B 1 61 ? 5.941 4.673 38.327 1.00 10.54 ? 142 ASP B CB 1 ATOM 3451 C CG . ASP B 1 61 ? 7.321 4.400 37.759 1.00 12.70 ? 142 ASP B CG 1 ATOM 3452 O OD1 . ASP B 1 61 ? 7.409 3.754 36.693 1.00 12.48 ? 142 ASP B OD1 1 ATOM 3453 O OD2 . ASP B 1 61 ? 8.315 4.826 38.380 1.00 11.91 ? 142 ASP B OD2 1 ATOM 3454 N N . LYS B 1 62 ? 7.260 2.080 39.584 1.00 8.08 ? 143 LYS B N 1 ATOM 3455 C CA . LYS B 1 62 ? 8.167 1.397 40.507 1.00 10.66 ? 143 LYS B CA 1 ATOM 3456 C C . LYS B 1 62 ? 8.989 2.346 41.381 1.00 10.73 ? 143 LYS B C 1 ATOM 3457 O O . LYS B 1 62 ? 9.403 1.979 42.480 1.00 12.62 ? 143 LYS B O 1 ATOM 3458 C CB . LYS B 1 62 ? 9.089 0.431 39.758 1.00 11.50 ? 143 LYS B CB 1 ATOM 3459 C CG . LYS B 1 62 ? 10.157 1.096 38.900 1.00 12.08 ? 143 LYS B CG 1 ATOM 3460 C CD . LYS B 1 62 ? 11.059 0.045 38.268 1.00 17.07 ? 143 LYS B CD 1 ATOM 3461 C CE . LYS B 1 62 ? 12.183 0.669 37.463 1.00 16.88 ? 143 LYS B CE 1 ATOM 3462 N NZ . LYS B 1 62 ? 13.093 -0.372 36.904 1.00 18.71 ? 143 LYS B NZ 1 ATOM 3463 N N . HIS B 1 63 ? 9.225 3.563 40.903 1.00 10.82 ? 144 HIS B N 1 ATOM 3464 C CA . HIS B 1 63 ? 10.030 4.516 41.662 1.00 10.05 ? 144 HIS B CA 1 ATOM 3465 C C . HIS B 1 63 ? 9.292 5.094 42.871 1.00 11.29 ? 144 HIS B C 1 ATOM 3466 O O . HIS B 1 63 ? 9.883 5.802 43.684 1.00 8.93 ? 144 HIS B O 1 ATOM 3467 C CB . HIS B 1 63 ? 10.563 5.631 40.757 1.00 9.65 ? 144 HIS B CB 1 ATOM 3468 C CG . HIS B 1 63 ? 11.549 5.157 39.737 1.00 8.79 ? 144 HIS B CG 1 ATOM 3469 N ND1 . HIS B 1 63 ? 11.186 4.794 38.460 1.00 9.37 ? 144 HIS B ND1 1 ATOM 3470 C CD2 . HIS B 1 63 ? 12.892 4.970 39.811 1.00 8.88 ? 144 HIS B CD2 1 ATOM 3471 C CE1 . HIS B 1 63 ? 12.258 4.412 37.786 1.00 11.89 ? 144 HIS B CE1 1 ATOM 3472 N NE2 . HIS B 1 63 ? 13.305 4.512 38.587 1.00 11.73 ? 144 HIS B NE2 1 ATOM 3473 N N . SER B 1 64 ? 8.005 4.785 42.993 1.00 9.58 ? 145 SER B N 1 ATOM 3474 C CA . SER B 1 64 ? 7.230 5.213 44.155 1.00 9.76 ? 145 SER B CA 1 ATOM 3475 C C . SER B 1 64 ? 7.541 4.327 45.358 1.00 10.40 ? 145 SER B C 1 ATOM 3476 O O . SER B 1 64 ? 7.066 4.571 46.467 1.00 9.41 ? 145 SER B O 1 ATOM 3477 C CB . SER B 1 64 ? 5.732 5.184 43.847 1.00 8.74 ? 145 SER B CB 1 ATOM 3478 O OG . SER B 1 64 ? 5.282 3.861 43.612 1.00 9.86 ? 145 SER B OG 1 ATOM 3479 N N . ASN B 1 65 ? 8.347 3.299 45.125 1.00 8.06 ? 146 ASN B N 1 ATOM 3480 C CA . ASN B 1 65 ? 8.730 2.354 46.167 1.00 11.55 ? 146 ASN B CA 1 ATOM 3481 C C . ASN B 1 65 ? 9.463 3.029 47.325 1.00 19.72 ? 146 ASN B C 1 ATOM 3482 O O . ASN B 1 65 ? 10.373 3.831 47.112 1.00 18.41 ? 146 ASN B O 1 ATOM 3483 C CB . ASN B 1 65 ? 9.604 1.253 45.565 1.00 17.32 ? 146 ASN B CB 1 ATOM 3484 C CG . ASN B 1 65 ? 9.784 0.074 46.496 1.00 26.33 ? 146 ASN B CG 1 ATOM 3485 O OD1 . ASN B 1 65 ? 9.191 0.019 47.572 1.00 21.59 ? 146 ASN B OD1 1 ATOM 3486 N ND2 . ASN B 1 65 ? 10.604 -0.882 46.082 1.00 42.31 ? 146 ASN B ND2 1 ATOM 3487 N N . GLY B 1 66 ? 9.056 2.704 48.548 1.00 22.04 ? 147 GLY B N 1 ATOM 3488 C CA . GLY B 1 66 ? 9.724 3.197 49.741 1.00 21.77 ? 147 GLY B CA 1 ATOM 3489 C C . GLY B 1 66 ? 9.558 4.686 49.979 1.00 27.69 ? 147 GLY B C 1 ATOM 3490 O O . GLY B 1 66 ? 10.394 5.311 50.631 1.00 24.90 ? 147 GLY B O 1 ATOM 3491 N N . THR B 1 67 ? 8.476 5.257 49.458 1.00 18.21 ? 148 THR B N 1 ATOM 3492 C CA . THR B 1 67 ? 8.231 6.690 49.610 1.00 20.14 ? 148 THR B CA 1 ATOM 3493 C C . THR B 1 67 ? 7.670 7.055 50.983 1.00 17.01 ? 148 THR B C 1 ATOM 3494 O O . THR B 1 67 ? 7.293 8.201 51.223 1.00 18.56 ? 148 THR B O 1 ATOM 3495 C CB . THR B 1 67 ? 7.309 7.245 48.504 1.00 16.44 ? 148 THR B CB 1 ATOM 3496 O OG1 . THR B 1 67 ? 6.198 6.360 48.311 1.00 13.59 ? 148 THR B OG1 1 ATOM 3497 C CG2 . THR B 1 67 ? 8.076 7.390 47.193 1.00 17.48 ? 148 THR B CG2 1 ATOM 3498 N N . ILE B 1 68 ? 7.619 6.082 51.884 1.00 21.75 ? 149 ILE B N 1 ATOM 3499 C CA . ILE B 1 68 ? 7.291 6.372 53.273 1.00 19.88 ? 149 ILE B CA 1 ATOM 3500 C C . ILE B 1 68 ? 8.432 7.175 53.891 1.00 24.85 ? 149 ILE B C 1 ATOM 3501 O O . ILE B 1 68 ? 8.265 7.815 54.931 1.00 28.97 ? 149 ILE B O 1 ATOM 3502 C CB . ILE B 1 68 ? 7.056 5.085 54.093 1.00 23.86 ? 149 ILE B CB 1 ATOM 3503 C CG1 . ILE B 1 68 ? 6.459 5.424 55.461 1.00 25.37 ? 149 ILE B CG1 1 ATOM 3504 C CG2 . ILE B 1 68 ? 8.352 4.302 54.248 1.00 20.30 ? 149 ILE B CG2 1 ATOM 3505 C CD1 . ILE B 1 68 ? 6.145 4.213 56.311 1.00 24.90 ? 149 ILE B CD1 1 ATOM 3506 N N . LYS B 1 69 ? 9.591 7.142 53.236 1.00 21.47 ? 150 LYS B N 1 ATOM 3507 C CA . LYS B 1 69 ? 10.771 7.858 53.717 1.00 22.38 ? 150 LYS B CA 1 ATOM 3508 C C . LYS B 1 69 ? 10.597 9.365 53.584 1.00 26.59 ? 150 LYS B C 1 ATOM 3509 O O . LYS B 1 69 ? 10.116 9.856 52.562 1.00 18.68 ? 150 LYS B O 1 ATOM 3510 C CB . LYS B 1 69 ? 12.028 7.403 52.967 1.00 26.19 ? 150 LYS B CB 1 ATOM 3511 C CG . LYS B 1 69 ? 13.313 8.073 53.446 1.00 30.46 ? 150 LYS B CG 1 ATOM 3512 C CD . LYS B 1 69 ? 14.533 7.228 53.115 1.00 29.72 ? 150 LYS B CD 1 ATOM 3513 C CE . LYS B 1 69 ? 15.680 7.498 54.081 1.00 35.33 ? 150 LYS B CE 1 ATOM 3514 N NZ . LYS B 1 69 ? 16.472 8.700 53.714 1.00 36.28 ? 150 LYS B NZ 1 ATOM 3515 N N . ASP B 1 70 ? 11.001 10.095 54.620 1.00 24.32 ? 151 ASP B N 1 ATOM 3516 C CA . ASP B 1 70 ? 10.793 11.538 54.667 1.00 20.32 ? 151 ASP B CA 1 ATOM 3517 C C . ASP B 1 70 ? 11.843 12.342 53.904 1.00 20.03 ? 151 ASP B C 1 ATOM 3518 O O . ASP B 1 70 ? 11.513 13.333 53.258 1.00 21.87 ? 151 ASP B O 1 ATOM 3519 C CB . ASP B 1 70 ? 10.721 12.024 56.118 1.00 24.75 ? 151 ASP B CB 1 ATOM 3520 C CG . ASP B 1 70 ? 9.487 11.518 56.840 1.00 31.17 ? 151 ASP B CG 1 ATOM 3521 O OD1 . ASP B 1 70 ? 8.442 11.341 56.179 1.00 30.54 ? 151 ASP B OD1 1 ATOM 3522 O OD2 . ASP B 1 70 ? 9.561 11.304 58.067 1.00 38.03 ? 151 ASP B OD2 1 ATOM 3523 N N . ARG B 1 71 ? 13.102 11.924 53.981 1.00 12.74 ? 152 ARG B N 1 ATOM 3524 C CA . ARG B 1 71 ? 14.190 12.716 53.419 1.00 13.95 ? 152 ARG B CA 1 ATOM 3525 C C . ARG B 1 71 ? 15.003 11.951 52.379 1.00 17.51 ? 152 ARG B C 1 ATOM 3526 O O . ARG B 1 71 ? 15.292 10.767 52.549 1.00 20.29 ? 152 ARG B O 1 ATOM 3527 C CB . ARG B 1 71 ? 15.101 13.238 54.538 1.00 14.21 ? 152 ARG B CB 1 ATOM 3528 C CG . ARG B 1 71 ? 14.351 14.008 55.624 1.00 12.99 ? 152 ARG B CG 1 ATOM 3529 C CD . ARG B 1 71 ? 15.281 14.542 56.709 1.00 10.35 ? 152 ARG B CD 1 ATOM 3530 N NE . ARG B 1 71 ? 16.003 13.478 57.403 1.00 11.06 ? 152 ARG B NE 1 ATOM 3531 C CZ . ARG B 1 71 ? 15.490 12.736 58.382 1.00 19.11 ? 152 ARG B CZ 1 ATOM 3532 N NH1 . ARG B 1 71 ? 14.243 12.930 58.784 1.00 16.01 ? 152 ARG B NH1 1 ATOM 3533 N NH2 . ARG B 1 71 ? 16.223 11.793 58.957 1.00 19.30 ? 152 ARG B NH2 1 ATOM 3534 N N . SER B 1 72 ? 15.365 12.645 51.303 1.00 10.38 ? 153 SER B N 1 ATOM 3535 C CA . SER B 1 72 ? 16.187 12.079 50.238 1.00 11.09 ? 153 SER B CA 1 ATOM 3536 C C . SER B 1 72 ? 16.629 13.200 49.303 1.00 8.18 ? 153 SER B C 1 ATOM 3537 O O . SER B 1 72 ? 16.040 14.281 49.309 1.00 9.01 ? 153 SER B O 1 ATOM 3538 C CB . SER B 1 72 ? 15.405 11.025 49.453 1.00 12.41 ? 153 SER B CB 1 ATOM 3539 O OG . SER B 1 72 ? 14.558 11.630 48.492 1.00 11.15 ? 153 SER B OG 1 ATOM 3540 N N . PRO B 1 73 ? 17.671 12.950 48.495 1.00 9.78 ? 154 PRO B N 1 ATOM 3541 C CA . PRO B 1 73 ? 18.131 13.966 47.542 1.00 9.40 ? 154 PRO B CA 1 ATOM 3542 C C . PRO B 1 73 ? 17.185 14.134 46.353 1.00 9.60 ? 154 PRO B C 1 ATOM 3543 O O . PRO B 1 73 ? 17.426 14.993 45.503 1.00 9.21 ? 154 PRO B O 1 ATOM 3544 C CB . PRO B 1 73 ? 19.480 13.416 47.069 1.00 10.62 ? 154 PRO B CB 1 ATOM 3545 C CG . PRO B 1 73 ? 19.385 11.943 47.282 1.00 10.84 ? 154 PRO B CG 1 ATOM 3546 C CD . PRO B 1 73 ? 18.542 11.760 48.507 1.00 13.80 ? 154 PRO B CD 1 ATOM 3547 N N . TYR B 1 74 ? 16.122 13.337 46.296 1.00 5.64 ? 155 TYR B N 1 ATOM 3548 C CA . TYR B 1 74 ? 15.208 13.382 45.157 1.00 7.63 ? 155 TYR B CA 1 ATOM 3549 C C . TYR B 1 74 ? 13.994 14.270 45.403 1.00 9.56 ? 155 TYR B C 1 ATOM 3550 O O . TYR B 1 74 ? 13.323 14.685 44.459 1.00 9.35 ? 155 TYR B O 1 ATOM 3551 C CB . TYR B 1 74 ? 14.746 11.972 44.778 1.00 7.63 ? 155 TYR B CB 1 ATOM 3552 C CG . TYR B 1 74 ? 15.871 10.970 44.732 1.00 10.26 ? 155 TYR B CG 1 ATOM 3553 C CD1 . TYR B 1 74 ? 16.909 11.108 43.819 1.00 8.67 ? 155 TYR B CD1 1 ATOM 3554 C CD2 . TYR B 1 74 ? 15.901 9.889 45.604 1.00 12.61 ? 155 TYR B CD2 1 ATOM 3555 C CE1 . TYR B 1 74 ? 17.948 10.197 43.775 1.00 11.63 ? 155 TYR B CE1 1 ATOM 3556 C CE2 . TYR B 1 74 ? 16.935 8.970 45.565 1.00 12.16 ? 155 TYR B CE2 1 ATOM 3557 C CZ . TYR B 1 74 ? 17.955 9.130 44.649 1.00 12.91 ? 155 TYR B CZ 1 ATOM 3558 O OH . TYR B 1 74 ? 18.988 8.220 44.604 1.00 15.85 ? 155 TYR B OH 1 ATOM 3559 N N . ARG B 1 75 ? 13.710 14.558 46.668 1.00 7.44 ? 156 ARG B N 1 ATOM 3560 C CA . ARG B 1 75 ? 12.533 15.352 47.001 1.00 9.53 ? 156 ARG B CA 1 ATOM 3561 C C . ARG B 1 75 ? 12.689 16.805 46.566 1.00 6.36 ? 156 ARG B C 1 ATOM 3562 O O . ARG B 1 75 ? 13.739 17.418 46.764 1.00 8.19 ? 156 ARG B O 1 ATOM 3563 C CB . ARG B 1 75 ? 12.213 15.264 48.496 1.00 8.97 ? 156 ARG B CB 1 ATOM 3564 C CG . ARG B 1 75 ? 11.962 13.845 48.979 1.00 12.69 ? 156 ARG B CG 1 ATOM 3565 C CD . ARG B 1 75 ? 11.107 13.821 50.233 1.00 12.93 ? 156 ARG B CD 1 ATOM 3566 N NE . ARG B 1 75 ? 9.709 14.112 49.937 1.00 11.80 ? 156 ARG B NE 1 ATOM 3567 C CZ . ARG B 1 75 ? 8.740 14.132 50.846 1.00 15.02 ? 156 ARG B CZ 1 ATOM 3568 N NH1 . ARG B 1 75 ? 9.015 13.877 52.117 1.00 14.43 ? 156 ARG B NH1 1 ATOM 3569 N NH2 . ARG B 1 75 ? 7.495 14.407 50.483 1.00 16.07 ? 156 ARG B NH2 1 ATOM 3570 N N . THR B 1 76 ? 11.637 17.342 45.959 1.00 8.33 ? 157 THR B N 1 ATOM 3571 C CA . THR B 1 76 ? 11.638 18.727 45.518 1.00 6.72 ? 157 THR B CA 1 ATOM 3572 C C . THR B 1 76 ? 10.338 19.423 45.895 1.00 7.44 ? 157 THR B C 1 ATOM 3573 O O . THR B 1 76 ? 9.276 18.802 45.962 1.00 8.53 ? 157 THR B O 1 ATOM 3574 C CB . THR B 1 76 ? 11.843 18.841 43.992 1.00 10.52 ? 157 THR B CB 1 ATOM 3575 O OG1 . THR B 1 76 ? 10.764 18.188 43.309 1.00 14.81 ? 157 THR B OG1 1 ATOM 3576 C CG2 . THR B 1 76 ? 13.161 18.205 43.577 1.00 8.70 ? 157 THR B CG2 1 ATOM 3577 N N . LEU B 1 77 ? 10.436 20.721 46.148 1.00 4.36 ? 158 LEU B N 1 ATOM 3578 C CA . LEU B 1 77 ? 9.263 21.548 46.364 1.00 3.45 ? 158 LEU B CA 1 ATOM 3579 C C . LEU B 1 77 ? 8.750 22.017 45.011 1.00 5.23 ? 158 LEU B C 1 ATOM 3580 O O . LEU B 1 77 ? 9.499 22.580 44.217 1.00 5.93 ? 158 LEU B O 1 ATOM 3581 C CB . LEU B 1 77 ? 9.619 22.753 47.232 1.00 4.15 ? 158 LEU B CB 1 ATOM 3582 C CG . LEU B 1 77 ? 8.491 23.751 47.506 1.00 4.26 ? 158 LEU B CG 1 ATOM 3583 C CD1 . LEU B 1 77 ? 7.459 23.134 48.442 1.00 4.64 ? 158 LEU B CD1 1 ATOM 3584 C CD2 . LEU B 1 77 ? 9.054 25.038 48.089 1.00 5.94 ? 158 LEU B CD2 1 ATOM 3585 N N . MET B 1 78 ? 7.475 21.765 44.745 1.00 5.73 ? 159 MET B N 1 ATOM 3586 C CA . MET B 1 78 ? 6.845 22.237 43.521 1.00 7.53 ? 159 MET B CA 1 ATOM 3587 C C . MET B 1 78 ? 5.486 22.826 43.871 1.00 6.38 ? 159 MET B C 1 ATOM 3588 O O . MET B 1 78 ? 5.047 22.735 45.015 1.00 6.79 ? 159 MET B O 1 ATOM 3589 C CB . MET B 1 78 ? 6.709 21.097 42.507 1.00 6.10 ? 159 MET B CB 1 ATOM 3590 C CG . MET B 1 78 ? 8.040 20.437 42.156 1.00 10.84 ? 159 MET B CG 1 ATOM 3591 S SD . MET B 1 78 ? 7.939 19.273 40.784 1.00 18.31 ? 159 MET B SD 1 ATOM 3592 C CE . MET B 1 78 ? 7.760 20.400 39.402 1.00 16.99 ? 159 MET B CE 1 ATOM 3593 N N . SER B 1 79 ? 4.830 23.448 42.899 1.00 4.87 ? 160 SER B N 1 ATOM 3594 C CA . SER B 1 79 ? 3.516 24.026 43.147 1.00 4.33 ? 160 SER B CA 1 ATOM 3595 C C . SER B 1 79 ? 2.634 23.956 41.911 1.00 7.93 ? 160 SER B C 1 ATOM 3596 O O . SER B 1 79 ? 3.126 23.896 40.786 1.00 5.89 ? 160 SER B O 1 ATOM 3597 C CB . SER B 1 79 ? 3.634 25.476 43.625 1.00 7.59 ? 160 SER B CB 1 ATOM 3598 O OG . SER B 1 79 ? 4.070 26.332 42.583 1.00 9.07 ? 160 SER B OG 1 ATOM 3599 N N . CYS B 1 80 ? 1.326 23.958 42.132 1.00 6.93 ? 161 CYS B N 1 ATOM 3600 C CA . CYS B 1 80 ? 0.367 23.990 41.038 1.00 8.70 ? 161 CYS B CA 1 ATOM 3601 C C . CYS B 1 80 ? -0.860 24.780 41.478 1.00 9.53 ? 161 CYS B C 1 ATOM 3602 O O . CYS B 1 80 ? -1.017 25.071 42.664 1.00 7.18 ? 161 CYS B O 1 ATOM 3603 C CB . CYS B 1 80 ? -0.017 22.569 40.611 1.00 7.95 ? 161 CYS B CB 1 ATOM 3604 S SG . CYS B 1 80 ? -0.865 21.592 41.873 1.00 14.23 ? 161 CYS B SG 1 ATOM 3605 N N . PRO B 1 81 ? -1.723 25.153 40.523 1.00 10.43 ? 162 PRO B N 1 ATOM 3606 C CA . PRO B 1 81 ? -2.950 25.861 40.897 1.00 7.61 ? 162 PRO B CA 1 ATOM 3607 C C . PRO B 1 81 ? -3.777 25.025 41.866 1.00 6.50 ? 162 PRO B C 1 ATOM 3608 O O . PRO B 1 81 ? -3.788 23.801 41.764 1.00 7.03 ? 162 PRO B O 1 ATOM 3609 C CB . PRO B 1 81 ? -3.684 26.014 39.561 1.00 8.82 ? 162 PRO B CB 1 ATOM 3610 C CG . PRO B 1 81 ? -2.591 26.004 38.539 1.00 14.97 ? 162 PRO B CG 1 ATOM 3611 C CD . PRO B 1 81 ? -1.568 25.043 39.062 1.00 9.96 ? 162 PRO B CD 1 ATOM 3612 N N . ILE B 1 82 ? -4.453 25.678 42.803 1.00 9.44 ? 163 ILE B N 1 ATOM 3613 C CA . ILE B 1 82 ? -5.240 24.961 43.796 1.00 10.42 ? 163 ILE B CA 1 ATOM 3614 C C . ILE B 1 82 ? -6.331 24.114 43.135 1.00 12.55 ? 163 ILE B C 1 ATOM 3615 O O . ILE B 1 82 ? -6.975 24.544 42.174 1.00 8.33 ? 163 ILE B O 1 ATOM 3616 C CB . ILE B 1 82 ? -5.859 25.928 44.831 1.00 13.71 ? 163 ILE B CB 1 ATOM 3617 C CG1 . ILE B 1 82 ? -6.331 25.165 46.070 1.00 15.85 ? 163 ILE B CG1 1 ATOM 3618 C CG2 . ILE B 1 82 ? -6.991 26.731 44.213 1.00 14.97 ? 163 ILE B CG2 1 ATOM 3619 C CD1 . ILE B 1 82 ? -6.914 26.060 47.142 1.00 13.67 ? 163 ILE B CD1 1 ATOM 3620 N N . GLY B 1 83 ? -6.514 22.896 43.635 1.00 6.24 ? 164 GLY B N 1 ATOM 3621 C CA . GLY B 1 83 ? -7.561 22.022 43.136 1.00 7.50 ? 164 GLY B CA 1 ATOM 3622 C C . GLY B 1 83 ? -7.150 21.133 41.975 1.00 9.18 ? 164 GLY B C 1 ATOM 3623 O O . GLY B 1 83 ? -7.883 20.216 41.607 1.00 10.76 ? 164 GLY B O 1 ATOM 3624 N N . GLU B 1 84 ? -5.989 21.407 41.386 1.00 7.86 ? 165 GLU B N 1 ATOM 3625 C CA . GLU B 1 84 ? -5.481 20.587 40.290 1.00 8.61 ? 165 GLU B CA 1 ATOM 3626 C C . GLU B 1 84 ? -4.562 19.501 40.832 1.00 10.26 ? 165 GLU B C 1 ATOM 3627 O O . GLU B 1 84 ? -3.941 19.674 41.879 1.00 8.76 ? 165 GLU B O 1 ATOM 3628 C CB . GLU B 1 84 ? -4.727 21.444 39.268 1.00 11.54 ? 165 GLU B CB 1 ATOM 3629 C CG . GLU B 1 84 ? -5.578 22.503 38.583 1.00 11.36 ? 165 GLU B CG 1 ATOM 3630 C CD . GLU B 1 84 ? -4.821 23.258 37.502 1.00 16.98 ? 165 GLU B CD 1 ATOM 3631 O OE1 . GLU B 1 84 ? -3.781 22.749 37.031 1.00 18.35 ? 165 GLU B OE1 1 ATOM 3632 O OE2 . GLU B 1 84 ? -5.266 24.360 37.122 1.00 15.73 ? 165 GLU B OE2 1 ATOM 3633 N N . VAL B 1 85 ? -4.478 18.378 40.127 1.00 10.00 ? 166 VAL B N 1 ATOM 3634 C CA . VAL B 1 85 ? -3.577 17.310 40.542 1.00 8.25 ? 166 VAL B CA 1 ATOM 3635 C C . VAL B 1 85 ? -2.133 17.728 40.300 1.00 9.18 ? 166 VAL B C 1 ATOM 3636 O O . VAL B 1 85 ? -1.831 18.388 39.306 1.00 11.40 ? 166 VAL B O 1 ATOM 3637 C CB . VAL B 1 85 ? -3.857 15.983 39.806 1.00 9.35 ? 166 VAL B CB 1 ATOM 3638 C CG1 . VAL B 1 85 ? -5.275 15.514 40.081 1.00 10.72 ? 166 VAL B CG1 1 ATOM 3639 C CG2 . VAL B 1 85 ? -3.611 16.131 38.310 1.00 11.92 ? 166 VAL B CG2 1 ATOM 3640 N N . PRO B 1 86 ? -1.237 17.358 41.224 1.00 10.15 ? 167 PRO B N 1 ATOM 3641 C CA . PRO B 1 86 ? 0.188 17.663 41.074 1.00 10.87 ? 167 PRO B CA 1 ATOM 3642 C C . PRO B 1 86 ? 0.819 16.774 40.010 1.00 9.68 ? 167 PRO B C 1 ATOM 3643 O O . PRO B 1 86 ? 1.176 15.633 40.288 1.00 10.85 ? 167 PRO B O 1 ATOM 3644 C CB . PRO B 1 86 ? 0.762 17.333 42.454 1.00 12.50 ? 167 PRO B CB 1 ATOM 3645 C CG . PRO B 1 86 ? -0.167 16.310 43.012 1.00 12.98 ? 167 PRO B CG 1 ATOM 3646 C CD . PRO B 1 86 ? -1.530 16.675 42.496 1.00 11.58 ? 167 PRO B CD 1 ATOM 3647 N N . SER B 1 87 ? 0.941 17.297 38.796 1.00 9.94 ? 168 SER B N 1 ATOM 3648 C CA . SER B 1 87 ? 1.508 16.541 37.689 1.00 9.53 ? 168 SER B CA 1 ATOM 3649 C C . SER B 1 87 ? 2.757 17.228 37.157 1.00 6.79 ? 168 SER B C 1 ATOM 3650 O O . SER B 1 87 ? 2.913 18.439 37.303 1.00 7.81 ? 168 SER B O 1 ATOM 3651 C CB . SER B 1 87 ? 0.475 16.397 36.569 1.00 10.16 ? 168 SER B CB 1 ATOM 3652 O OG . SER B 1 87 ? 1.056 15.840 35.405 1.00 14.90 ? 168 SER B OG 1 ATOM 3653 N N . PRO B 1 88 ? 3.661 16.455 36.543 1.00 10.40 ? 169 PRO B N 1 ATOM 3654 C CA . PRO B 1 88 ? 4.833 17.068 35.911 1.00 11.99 ? 169 PRO B CA 1 ATOM 3655 C C . PRO B 1 88 ? 4.435 17.996 34.765 1.00 12.99 ? 169 PRO B C 1 ATOM 3656 O O . PRO B 1 88 ? 5.262 18.784 34.308 1.00 15.61 ? 169 PRO B O 1 ATOM 3657 C CB . PRO B 1 88 ? 5.616 15.862 35.369 1.00 11.38 ? 169 PRO B CB 1 ATOM 3658 C CG . PRO B 1 88 ? 4.639 14.726 35.359 1.00 13.02 ? 169 PRO B CG 1 ATOM 3659 C CD . PRO B 1 88 ? 3.716 14.985 36.503 1.00 10.72 ? 169 PRO B CD 1 ATOM 3660 N N . TYR B 1 89 A 3.185 17.913 34.316 1.00 8.83 ? 169 TYR B N 1 ATOM 3661 C CA . TYR B 1 89 A 2.741 18.703 33.168 1.00 9.16 ? 169 TYR B CA 1 ATOM 3662 C C . TYR B 1 89 A 2.059 20.019 33.553 1.00 12.78 ? 169 TYR B C 1 ATOM 3663 O O . TYR B 1 89 A 1.803 20.863 32.693 1.00 13.56 ? 169 TYR B O 1 ATOM 3664 C CB . TYR B 1 89 A 1.815 17.882 32.264 1.00 10.16 ? 169 TYR B CB 1 ATOM 3665 C CG . TYR B 1 89 A 2.304 16.478 31.986 1.00 9.02 ? 169 TYR B CG 1 ATOM 3666 C CD1 . TYR B 1 89 A 3.631 16.233 31.652 1.00 12.04 ? 169 TYR B CD1 1 ATOM 3667 C CD2 . TYR B 1 89 A 1.435 15.398 32.050 1.00 9.39 ? 169 TYR B CD2 1 ATOM 3668 C CE1 . TYR B 1 89 A 4.078 14.944 31.400 1.00 9.73 ? 169 TYR B CE1 1 ATOM 3669 C CE2 . TYR B 1 89 A 1.869 14.113 31.797 1.00 11.37 ? 169 TYR B CE2 1 ATOM 3670 C CZ . TYR B 1 89 A 3.189 13.890 31.474 1.00 11.27 ? 169 TYR B CZ 1 ATOM 3671 O OH . TYR B 1 89 A 3.615 12.607 31.226 1.00 11.86 ? 169 TYR B OH 1 ATOM 3672 N N . ASN B 1 90 ? 1.759 20.198 34.836 1.00 11.34 ? 170 ASN B N 1 ATOM 3673 C CA . ASN B 1 90 ? 1.114 21.431 35.279 1.00 11.40 ? 170 ASN B CA 1 ATOM 3674 C C . ASN B 1 90 ? 1.760 22.040 36.516 1.00 13.46 ? 170 ASN B C 1 ATOM 3675 O O . ASN B 1 90 ? 1.240 23.004 37.081 1.00 14.52 ? 170 ASN B O 1 ATOM 3676 C CB . ASN B 1 90 ? -0.369 21.193 35.556 1.00 17.03 ? 170 ASN B CB 1 ATOM 3677 C CG . ASN B 1 90 ? -0.602 20.495 36.878 1.00 15.76 ? 170 ASN B CG 1 ATOM 3678 O OD1 . ASN B 1 90 ? 0.235 19.718 37.334 1.00 15.26 ? 170 ASN B OD1 1 ATOM 3679 N ND2 . ASN B 1 90 ? -1.739 20.774 37.505 1.00 18.04 ? 170 ASN B ND2 1 ATOM 3680 N N . SER B 1 91 ? 2.888 21.480 36.940 1.00 9.00 ? 171 SER B N 1 ATOM 3681 C CA . SER B 1 91 ? 3.533 21.927 38.173 1.00 10.10 ? 171 SER B CA 1 ATOM 3682 C C . SER B 1 91 ? 4.778 22.772 37.928 1.00 10.57 ? 171 SER B C 1 ATOM 3683 O O . SER B 1 91 ? 5.587 22.475 37.048 1.00 13.17 ? 171 SER B O 1 ATOM 3684 C CB . SER B 1 91 ? 3.879 20.734 39.065 1.00 10.95 ? 171 SER B CB 1 ATOM 3685 O OG . SER B 1 91 ? 2.705 20.045 39.458 1.00 10.43 ? 171 SER B OG 1 ATOM 3686 N N . ARG B 1 92 ? 4.920 23.826 38.725 1.00 9.58 ? 172 ARG B N 1 ATOM 3687 C CA . ARG B 1 92 ? 6.062 24.727 38.638 1.00 12.35 ? 172 ARG B CA 1 ATOM 3688 C C . ARG B 1 92 ? 7.134 24.272 39.624 1.00 11.66 ? 172 ARG B C 1 ATOM 3689 O O . ARG B 1 92 ? 6.830 23.982 40.781 1.00 10.26 ? 172 ARG B O 1 ATOM 3690 C CB . ARG B 1 92 ? 5.610 26.152 38.969 1.00 14.06 ? 172 ARG B CB 1 ATOM 3691 C CG . ARG B 1 92 ? 6.674 27.220 38.799 1.00 24.55 ? 172 ARG B CG 1 ATOM 3692 C CD . ARG B 1 92 ? 6.096 28.610 39.075 1.00 24.65 ? 172 ARG B CD 1 ATOM 3693 N NE . ARG B 1 92 ? 5.876 28.841 40.501 1.00 27.64 ? 172 ARG B NE 1 ATOM 3694 C CZ . ARG B 1 92 ? 5.069 29.776 40.995 1.00 29.93 ? 172 ARG B CZ 1 ATOM 3695 N NH1 . ARG B 1 92 ? 4.387 30.567 40.174 1.00 26.20 ? 172 ARG B NH1 1 ATOM 3696 N NH2 . ARG B 1 92 ? 4.937 29.914 42.310 1.00 25.07 ? 172 ARG B NH2 1 ATOM 3697 N N . PHE B 1 93 ? 8.383 24.190 39.176 1.00 5.75 ? 173 PHE B N 1 ATOM 3698 C CA . PHE B 1 93 ? 9.471 23.828 40.085 1.00 10.24 ? 173 PHE B CA 1 ATOM 3699 C C . PHE B 1 93 ? 9.819 25.000 40.999 1.00 7.81 ? 173 PHE B C 1 ATOM 3700 O O . PHE B 1 93 ? 9.938 26.136 40.543 1.00 9.44 ? 173 PHE B O 1 ATOM 3701 C CB . PHE B 1 93 ? 10.718 23.374 39.321 1.00 6.81 ? 173 PHE B CB 1 ATOM 3702 C CG . PHE B 1 93 ? 11.894 23.097 40.212 1.00 6.11 ? 173 PHE B CG 1 ATOM 3703 C CD1 . PHE B 1 93 ? 12.037 21.866 40.829 1.00 7.80 ? 173 PHE B CD1 1 ATOM 3704 C CD2 . PHE B 1 93 ? 12.847 24.073 40.447 1.00 7.95 ? 173 PHE B CD2 1 ATOM 3705 C CE1 . PHE B 1 93 ? 13.112 21.612 41.659 1.00 7.86 ? 173 PHE B CE1 1 ATOM 3706 C CE2 . PHE B 1 93 ? 13.924 23.823 41.275 1.00 7.21 ? 173 PHE B CE2 1 ATOM 3707 C CZ . PHE B 1 93 ? 14.054 22.592 41.881 1.00 6.24 ? 173 PHE B CZ 1 ATOM 3708 N N . GLU B 1 94 ? 9.992 24.721 42.288 1.00 10.75 ? 174 GLU B N 1 ATOM 3709 C CA . GLU B 1 94 ? 10.323 25.768 43.251 1.00 8.42 ? 174 GLU B CA 1 ATOM 3710 C C . GLU B 1 94 ? 11.736 25.614 43.810 1.00 9.37 ? 174 GLU B C 1 ATOM 3711 O O . GLU B 1 94 ? 12.543 26.540 43.740 1.00 8.99 ? 174 GLU B O 1 ATOM 3712 C CB . GLU B 1 94 ? 9.308 25.793 44.400 1.00 8.61 ? 174 GLU B CB 1 ATOM 3713 C CG . GLU B 1 94 ? 7.856 25.974 43.960 1.00 8.48 ? 174 GLU B CG 1 ATOM 3714 C CD . GLU B 1 94 ? 7.574 27.345 43.369 1.00 12.90 ? 174 GLU B CD 1 ATOM 3715 O OE1 . GLU B 1 94 ? 8.489 28.197 43.353 1.00 11.90 ? 174 GLU B OE1 1 ATOM 3716 O OE2 . GLU B 1 94 ? 6.430 27.573 42.921 1.00 13.10 ? 174 GLU B OE2 1 ATOM 3717 N N . SER B 1 95 ? 12.033 24.442 44.362 1.00 5.27 ? 175 SER B N 1 ATOM 3718 C CA . SER B 1 95 ? 13.309 24.236 45.039 1.00 5.73 ? 175 SER B CA 1 ATOM 3719 C C . SER B 1 95 ? 13.567 22.758 45.306 1.00 6.64 ? 175 SER B C 1 ATOM 3720 O O . SER B 1 95 ? 12.637 21.957 45.331 1.00 7.88 ? 175 SER B O 1 ATOM 3721 C CB . SER B 1 95 ? 13.310 25.007 46.362 1.00 9.20 ? 175 SER B CB 1 ATOM 3722 O OG . SER B 1 95 ? 14.596 25.031 46.953 1.00 19.90 ? 175 SER B OG 1 ATOM 3723 N N . VAL B 1 96 ? 14.832 22.395 45.497 1.00 6.80 ? 176 VAL B N 1 ATOM 3724 C CA . VAL B 1 96 ? 15.166 21.047 45.944 1.00 6.67 ? 176 VAL B CA 1 ATOM 3725 C C . VAL B 1 96 ? 15.025 21.033 47.461 1.00 7.76 ? 176 VAL B C 1 ATOM 3726 O O . VAL B 1 96 ? 15.661 21.832 48.147 1.00 10.56 ? 176 VAL B O 1 ATOM 3727 C CB . VAL B 1 96 ? 16.603 20.653 45.555 1.00 8.41 ? 176 VAL B CB 1 ATOM 3728 C CG1 . VAL B 1 96 ? 16.917 19.246 46.038 1.00 6.84 ? 176 VAL B CG1 1 ATOM 3729 C CG2 . VAL B 1 96 ? 16.799 20.763 44.042 1.00 5.80 ? 176 VAL B CG2 1 ATOM 3730 N N . ALA B 1 97 ? 14.190 20.144 47.991 1.00 5.64 ? 177 ALA B N 1 ATOM 3731 C CA . ALA B 1 97 ? 13.867 20.214 49.415 1.00 5.79 ? 177 ALA B CA 1 ATOM 3732 C C . ALA B 1 97 ? 13.170 18.976 49.974 1.00 6.50 ? 177 ALA B C 1 ATOM 3733 O O . ALA B 1 97 ? 12.325 18.375 49.312 1.00 6.77 ? 177 ALA B O 1 ATOM 3734 C CB . ALA B 1 97 ? 13.016 21.452 49.692 1.00 6.75 ? 177 ALA B CB 1 ATOM 3735 N N . TRP B 1 98 ? 13.529 18.610 51.203 1.00 5.25 ? 178 TRP B N 1 ATOM 3736 C CA . TRP B 1 98 ? 12.766 17.617 51.955 1.00 6.37 ? 178 TRP B CA 1 ATOM 3737 C C . TRP B 1 98 ? 12.056 18.239 53.161 1.00 6.99 ? 178 TRP B C 1 ATOM 3738 O O . TRP B 1 98 ? 11.391 17.547 53.930 1.00 5.43 ? 178 TRP B O 1 ATOM 3739 C CB . TRP B 1 98 ? 13.618 16.402 52.360 1.00 7.63 ? 178 TRP B CB 1 ATOM 3740 C CG . TRP B 1 98 ? 14.999 16.691 52.886 1.00 7.83 ? 178 TRP B CG 1 ATOM 3741 C CD1 . TRP B 1 98 ? 16.183 16.437 52.253 1.00 7.80 ? 178 TRP B CD1 1 ATOM 3742 C CD2 . TRP B 1 98 ? 15.342 17.252 54.162 1.00 6.41 ? 178 TRP B CD2 1 ATOM 3743 N NE1 . TRP B 1 98 ? 17.237 16.813 53.048 1.00 9.49 ? 178 TRP B NE1 1 ATOM 3744 C CE2 . TRP B 1 98 ? 16.749 17.319 54.224 1.00 8.03 ? 178 TRP B CE2 1 ATOM 3745 C CE3 . TRP B 1 98 ? 14.596 17.713 55.251 1.00 7.76 ? 178 TRP B CE3 1 ATOM 3746 C CZ2 . TRP B 1 98 ? 17.426 17.825 55.333 1.00 7.40 ? 178 TRP B CZ2 1 ATOM 3747 C CZ3 . TRP B 1 98 ? 15.271 18.215 56.352 1.00 9.64 ? 178 TRP B CZ3 1 ATOM 3748 C CH2 . TRP B 1 98 ? 16.671 18.268 56.384 1.00 8.59 ? 178 TRP B CH2 1 ATOM 3749 N N . SER B 1 99 ? 12.206 19.553 53.307 1.00 5.34 ? 179 SER B N 1 ATOM 3750 C CA . SER B 1 99 ? 11.424 20.345 54.252 1.00 6.82 ? 179 SER B CA 1 ATOM 3751 C C . SER B 1 99 ? 11.293 21.744 53.661 1.00 5.66 ? 179 SER B C 1 ATOM 3752 O O . SER B 1 99 ? 12.251 22.262 53.091 1.00 6.41 ? 179 SER B O 1 ATOM 3753 C CB . SER B 1 99 ? 12.109 20.403 55.618 1.00 7.67 ? 179 SER B CB 1 ATOM 3754 O OG . SER B 1 99 ? 11.323 21.127 56.553 1.00 9.63 ? 179 SER B OG 1 ATOM 3755 N N . ALA B 1 100 ? 10.121 22.360 53.780 1.00 6.43 ? 180 ALA B N 1 ATOM 3756 C CA . ALA B 1 100 ? 9.893 23.605 53.051 1.00 6.22 ? 180 ALA B CA 1 ATOM 3757 C C . ALA B 1 100 ? 8.843 24.549 53.632 1.00 9.76 ? 180 ALA B C 1 ATOM 3758 O O . ALA B 1 100 ? 8.054 24.182 54.505 1.00 6.88 ? 180 ALA B O 1 ATOM 3759 C CB . ALA B 1 100 ? 9.566 23.296 51.589 1.00 5.90 ? 180 ALA B CB 1 ATOM 3760 N N . SER B 1 101 ? 8.857 25.775 53.118 1.00 7.70 ? 181 SER B N 1 ATOM 3761 C CA . SER B 1 101 ? 7.842 26.775 53.409 1.00 8.91 ? 181 SER B CA 1 ATOM 3762 C C . SER B 1 101 ? 7.795 27.747 52.236 1.00 8.48 ? 181 SER B C 1 ATOM 3763 O O . SER B 1 101 ? 8.722 27.797 51.430 1.00 8.69 ? 181 SER B O 1 ATOM 3764 C CB . SER B 1 101 ? 8.176 27.525 54.700 1.00 10.06 ? 181 SER B CB 1 ATOM 3765 O OG . SER B 1 101 ? 7.225 28.545 54.947 1.00 10.04 ? 181 SER B OG 1 ATOM 3766 N N . ALA B 1 102 ? 6.717 28.517 52.138 1.00 2.71 ? 182 ALA B N 1 ATOM 3767 C CA . ALA B 1 102 ? 6.580 29.491 51.062 1.00 2.19 ? 182 ALA B CA 1 ATOM 3768 C C . ALA B 1 102 ? 5.484 30.499 51.383 1.00 5.96 ? 182 ALA B C 1 ATOM 3769 O O . ALA B 1 102 ? 4.536 30.186 52.101 1.00 7.33 ? 182 ALA B O 1 ATOM 3770 C CB . ALA B 1 102 ? 6.284 28.786 49.736 1.00 3.90 ? 182 ALA B CB 1 ATOM 3771 N N . CYS B 1 103 ? 5.622 31.709 50.848 1.00 5.23 ? 183 CYS B N 1 ATOM 3772 C CA . CYS B 1 103 ? 4.623 32.758 51.038 1.00 7.25 ? 183 CYS B CA 1 ATOM 3773 C C . CYS B 1 103 ? 4.881 33.935 50.101 1.00 10.85 ? 183 CYS B C 1 ATOM 3774 O O . CYS B 1 103 ? 5.992 34.106 49.600 1.00 10.38 ? 183 CYS B O 1 ATOM 3775 C CB . CYS B 1 103 ? 4.591 33.227 52.496 1.00 8.60 ? 183 CYS B CB 1 ATOM 3776 S SG . CYS B 1 103 ? 6.189 33.754 53.160 1.00 12.58 ? 183 CYS B SG 1 ATOM 3777 N N . HIS B 1 104 ? 3.847 34.737 49.867 1.00 4.80 ? 184 HIS B N 1 ATOM 3778 C CA . HIS B 1 104 ? 3.928 35.857 48.936 1.00 6.60 ? 184 HIS B CA 1 ATOM 3779 C C . HIS B 1 104 ? 3.808 37.165 49.714 1.00 6.92 ? 184 HIS B C 1 ATOM 3780 O O . HIS B 1 104 ? 2.889 37.330 50.517 1.00 10.73 ? 184 HIS B O 1 ATOM 3781 C CB . HIS B 1 104 ? 2.800 35.752 47.905 1.00 4.23 ? 184 HIS B CB 1 ATOM 3782 C CG . HIS B 1 104 ? 3.062 36.498 46.634 1.00 6.62 ? 184 HIS B CG 1 ATOM 3783 N ND1 . HIS B 1 104 ? 2.883 37.858 46.516 1.00 5.60 ? 184 HIS B ND1 1 ATOM 3784 C CD2 . HIS B 1 104 ? 3.473 36.067 45.414 1.00 5.68 ? 184 HIS B CD2 1 ATOM 3785 C CE1 . HIS B 1 104 ? 3.183 38.238 45.286 1.00 6.91 ? 184 HIS B CE1 1 ATOM 3786 N NE2 . HIS B 1 104 ? 3.544 37.168 44.599 1.00 5.06 ? 184 HIS B NE2 1 ATOM 3787 N N . ASP B 1 105 ? 4.730 38.095 49.484 1.00 6.30 ? 185 ASP B N 1 ATOM 3788 C CA . ASP B 1 105 ? 4.726 39.350 50.237 1.00 8.88 ? 185 ASP B CA 1 ATOM 3789 C C . ASP B 1 105 ? 3.893 40.442 49.569 1.00 9.71 ? 185 ASP B C 1 ATOM 3790 O O . ASP B 1 105 ? 3.847 41.576 50.045 1.00 10.62 ? 185 ASP B O 1 ATOM 3791 C CB . ASP B 1 105 ? 6.154 39.847 50.491 1.00 9.96 ? 185 ASP B CB 1 ATOM 3792 C CG . ASP B 1 105 ? 6.860 40.284 49.218 1.00 9.81 ? 185 ASP B CG 1 ATOM 3793 O OD1 . ASP B 1 105 ? 6.286 40.118 48.123 1.00 10.93 ? 185 ASP B OD1 1 ATOM 3794 O OD2 . ASP B 1 105 ? 7.995 40.798 49.315 1.00 10.70 ? 185 ASP B OD2 1 ATOM 3795 N N . GLY B 1 106 ? 3.230 40.092 48.472 1.00 8.88 ? 186 GLY B N 1 ATOM 3796 C CA . GLY B 1 106 ? 2.454 41.054 47.712 1.00 12.02 ? 186 GLY B CA 1 ATOM 3797 C C . GLY B 1 106 ? 3.144 41.422 46.412 1.00 13.26 ? 186 GLY B C 1 ATOM 3798 O O . GLY B 1 106 ? 2.503 41.876 45.465 1.00 14.61 ? 186 GLY B O 1 ATOM 3799 N N . ILE B 1 107 ? 4.458 41.223 46.371 1.00 9.38 ? 187 ILE B N 1 ATOM 3800 C CA . ILE B 1 107 ? 5.248 41.522 45.181 1.00 11.13 ? 187 ILE B CA 1 ATOM 3801 C C . ILE B 1 107 ? 5.753 40.246 44.515 1.00 10.75 ? 187 ILE B C 1 ATOM 3802 O O . ILE B 1 107 ? 5.518 40.021 43.328 1.00 9.77 ? 187 ILE B O 1 ATOM 3803 C CB . ILE B 1 107 ? 6.458 42.414 45.511 1.00 11.65 ? 187 ILE B CB 1 ATOM 3804 C CG1 . ILE B 1 107 ? 6.027 43.616 46.350 1.00 17.27 ? 187 ILE B CG1 1 ATOM 3805 C CG2 . ILE B 1 107 ? 7.149 42.863 44.232 1.00 10.42 ? 187 ILE B CG2 1 ATOM 3806 C CD1 . ILE B 1 107 ? 5.004 44.490 45.674 1.00 18.15 ? 187 ILE B CD1 1 ATOM 3807 N N . ASN B 1 108 ? 6.454 39.417 45.282 1.00 6.38 ? 188 ASN B N 1 ATOM 3808 C CA . ASN B 1 108 ? 6.992 38.166 44.755 1.00 4.87 ? 188 ASN B CA 1 ATOM 3809 C C . ASN B 1 108 ? 6.840 36.994 45.714 1.00 6.19 ? 188 ASN B C 1 ATOM 3810 O O . ASN B 1 108 ? 6.514 37.171 46.891 1.00 5.28 ? 188 ASN B O 1 ATOM 3811 C CB . ASN B 1 108 ? 8.468 38.321 44.381 1.00 5.09 ? 188 ASN B CB 1 ATOM 3812 C CG . ASN B 1 108 ? 8.676 39.193 43.160 1.00 10.38 ? 188 ASN B CG 1 ATOM 3813 O OD1 . ASN B 1 108 ? 9.373 40.207 43.220 1.00 19.87 ? 188 ASN B OD1 1 ATOM 3814 N ND2 . ASN B 1 108 ? 8.076 38.801 42.043 1.00 8.30 ? 188 ASN B ND2 1 ATOM 3815 N N . TRP B 1 109 ? 7.084 35.794 45.195 1.00 8.17 ? 189 TRP B N 1 ATOM 3816 C CA . TRP B 1 109 ? 7.070 34.582 45.999 1.00 7.96 ? 189 TRP B CA 1 ATOM 3817 C C . TRP B 1 109 ? 8.381 34.397 46.747 1.00 7.45 ? 189 TRP B C 1 ATOM 3818 O O . TRP B 1 109 ? 9.463 34.589 46.191 1.00 6.81 ? 189 TRP B O 1 ATOM 3819 C CB . TRP B 1 109 ? 6.821 33.349 45.122 1.00 5.52 ? 189 TRP B CB 1 ATOM 3820 C CG . TRP B 1 109 ? 5.388 33.156 44.732 1.00 6.87 ? 189 TRP B CG 1 ATOM 3821 C CD1 . TRP B 1 109 ? 4.831 33.385 43.505 1.00 8.99 ? 189 TRP B CD1 1 ATOM 3822 C CD2 . TRP B 1 109 ? 4.325 32.691 45.575 1.00 7.20 ? 189 TRP B CD2 1 ATOM 3823 N NE1 . TRP B 1 109 ? 3.488 33.091 43.534 1.00 8.26 ? 189 TRP B NE1 1 ATOM 3824 C CE2 . TRP B 1 109 ? 3.153 32.664 44.793 1.00 6.58 ? 189 TRP B CE2 1 ATOM 3825 C CE3 . TRP B 1 109 ? 4.252 32.295 46.915 1.00 5.35 ? 189 TRP B CE3 1 ATOM 3826 C CZ2 . TRP B 1 109 ? 1.923 32.257 45.307 1.00 14.05 ? 189 TRP B CZ2 1 ATOM 3827 C CZ3 . TRP B 1 109 ? 3.030 31.893 47.422 1.00 5.31 ? 189 TRP B CZ3 1 ATOM 3828 C CH2 . TRP B 1 109 ? 1.882 31.877 46.620 1.00 7.88 ? 189 TRP B CH2 1 ATOM 3829 N N . LEU B 1 110 ? 8.271 34.025 48.016 1.00 7.90 ? 190 LEU B N 1 ATOM 3830 C CA . LEU B 1 110 ? 9.414 33.564 48.786 1.00 7.44 ? 190 LEU B CA 1 ATOM 3831 C C . LEU B 1 110 ? 9.264 32.063 48.968 1.00 6.09 ? 190 LEU B C 1 ATOM 3832 O O . LEU B 1 110 ? 8.207 31.587 49.375 1.00 6.16 ? 190 LEU B O 1 ATOM 3833 C CB . LEU B 1 110 ? 9.454 34.246 50.154 1.00 8.36 ? 190 LEU B CB 1 ATOM 3834 C CG . LEU B 1 110 ? 10.394 33.609 51.181 1.00 7.67 ? 190 LEU B CG 1 ATOM 3835 C CD1 . LEU B 1 110 ? 11.844 33.751 50.739 1.00 6.79 ? 190 LEU B CD1 1 ATOM 3836 C CD2 . LEU B 1 110 ? 10.184 34.222 52.561 1.00 8.82 ? 190 LEU B CD2 1 ATOM 3837 N N . THR B 1 111 ? 10.309 31.312 48.646 1.00 6.63 ? 191 THR B N 1 ATOM 3838 C CA . THR B 1 111 ? 10.303 29.886 48.930 1.00 4.82 ? 191 THR B CA 1 ATOM 3839 C C . THR B 1 111 ? 11.518 29.530 49.776 1.00 7.31 ? 191 THR B C 1 ATOM 3840 O O . THR B 1 111 ? 12.600 30.089 49.596 1.00 5.29 ? 191 THR B O 1 ATOM 3841 C CB . THR B 1 111 ? 10.260 29.027 47.645 1.00 8.71 ? 191 THR B CB 1 ATOM 3842 O OG1 . THR B 1 111 ? 11.429 29.275 46.854 1.00 8.54 ? 191 THR B OG1 1 ATOM 3843 C CG2 . THR B 1 111 ? 9.016 29.355 46.823 1.00 6.19 ? 191 THR B CG2 1 ATOM 3844 N N . ILE B 1 112 ? 11.320 28.621 50.722 1.00 5.29 ? 192 ILE B N 1 ATOM 3845 C CA . ILE B 1 112 ? 12.402 28.125 51.558 1.00 6.29 ? 192 ILE B CA 1 ATOM 3846 C C . ILE B 1 112 ? 12.463 26.613 51.414 1.00 5.65 ? 192 ILE B C 1 ATOM 3847 O O . ILE B 1 112 ? 11.505 25.915 51.739 1.00 8.66 ? 192 ILE B O 1 ATOM 3848 C CB . ILE B 1 112 ? 12.185 28.495 53.036 1.00 7.58 ? 192 ILE B CB 1 ATOM 3849 C CG1 . ILE B 1 112 ? 12.092 30.015 53.192 1.00 9.92 ? 192 ILE B CG1 1 ATOM 3850 C CG2 . ILE B 1 112 ? 13.305 27.937 53.894 1.00 7.92 ? 192 ILE B CG2 1 ATOM 3851 C CD1 . ILE B 1 112 ? 11.673 30.465 54.571 1.00 11.47 ? 192 ILE B CD1 1 ATOM 3852 N N . GLY B 1 113 ? 13.585 26.115 50.906 1.00 6.24 ? 193 GLY B N 1 ATOM 3853 C CA . GLY B 1 113 ? 13.749 24.693 50.665 1.00 4.53 ? 193 GLY B CA 1 ATOM 3854 C C . GLY B 1 113 ? 14.999 24.148 51.324 1.00 7.01 ? 193 GLY B C 1 ATOM 3855 O O . GLY B 1 113 ? 16.109 24.602 51.041 1.00 5.79 ? 193 GLY B O 1 ATOM 3856 N N . ILE B 1 114 ? 14.815 23.173 52.209 1.00 3.46 ? 194 ILE B N 1 ATOM 3857 C CA . ILE B 1 114 ? 15.924 22.579 52.945 1.00 4.81 ? 194 ILE B CA 1 ATOM 3858 C C . ILE B 1 114 ? 16.315 21.234 52.346 1.00 5.65 ? 194 ILE B C 1 ATOM 3859 O O . ILE B 1 114 ? 15.473 20.359 52.159 1.00 5.34 ? 194 ILE B O 1 ATOM 3860 C CB . ILE B 1 114 ? 15.566 22.376 54.432 1.00 5.53 ? 194 ILE B CB 1 ATOM 3861 C CG1 . ILE B 1 114 ? 15.156 23.708 55.071 1.00 4.85 ? 194 ILE B CG1 1 ATOM 3862 C CG2 . ILE B 1 114 ? 16.731 21.742 55.179 1.00 8.05 ? 194 ILE B CG2 1 ATOM 3863 C CD1 . ILE B 1 114 ? 14.597 23.577 56.482 1.00 5.71 ? 194 ILE B CD1 1 ATOM 3864 N N . SER B 1 115 ? 17.598 21.077 52.044 1.00 5.03 ? 195 SER B N 1 ATOM 3865 C CA . SER B 1 115 ? 18.119 19.808 51.551 1.00 7.72 ? 195 SER B CA 1 ATOM 3866 C C . SER B 1 115 ? 19.499 19.568 52.154 1.00 6.41 ? 195 SER B C 1 ATOM 3867 O O . SER B 1 115 ? 19.964 20.352 52.981 1.00 9.33 ? 195 SER B O 1 ATOM 3868 C CB . SER B 1 115 ? 18.184 19.806 50.021 1.00 8.29 ? 195 SER B CB 1 ATOM 3869 O OG . SER B 1 115 ? 18.455 18.508 49.523 1.00 8.09 ? 195 SER B OG 1 ATOM 3870 N N . GLY B 1 116 ? 20.150 18.484 51.749 1.00 7.40 ? 196 GLY B N 1 ATOM 3871 C CA . GLY B 1 116 ? 21.447 18.137 52.302 1.00 9.78 ? 196 GLY B CA 1 ATOM 3872 C C . GLY B 1 116 ? 21.362 17.063 53.373 1.00 12.03 ? 196 GLY B C 1 ATOM 3873 O O . GLY B 1 116 ? 20.282 16.535 53.647 1.00 9.47 ? 196 GLY B O 1 ATOM 3874 N N . PRO B 1 117 ? 22.507 16.740 53.995 1.00 10.00 ? 197 PRO B N 1 ATOM 3875 C CA . PRO B 1 117 ? 22.609 15.661 54.984 1.00 10.00 ? 197 PRO B CA 1 ATOM 3876 C C . PRO B 1 117 ? 21.983 16.034 56.325 1.00 10.24 ? 197 PRO B C 1 ATOM 3877 O O . PRO B 1 117 ? 21.855 17.216 56.638 1.00 7.91 ? 197 PRO B O 1 ATOM 3878 C CB . PRO B 1 117 ? 24.121 15.491 55.143 1.00 8.70 ? 197 PRO B CB 1 ATOM 3879 C CG . PRO B 1 117 ? 24.660 16.856 54.897 1.00 12.16 ? 197 PRO B CG 1 ATOM 3880 C CD . PRO B 1 117 ? 23.788 17.448 53.819 1.00 6.38 ? 197 PRO B CD 1 ATOM 3881 N N . ASP B 1 118 ? 21.605 15.026 57.106 1.00 12.75 ? 198 ASP B N 1 ATOM 3882 C CA . ASP B 1 118 ? 20.980 15.247 58.408 1.00 18.31 ? 198 ASP B CA 1 ATOM 3883 C C . ASP B 1 118 ? 21.850 16.066 59.357 1.00 14.21 ? 198 ASP B C 1 ATOM 3884 O O . ASP B 1 118 ? 21.333 16.777 60.220 1.00 16.07 ? 198 ASP B O 1 ATOM 3885 C CB . ASP B 1 118 ? 20.622 13.911 59.068 1.00 14.92 ? 198 ASP B CB 1 ATOM 3886 C CG . ASP B 1 118 ? 19.432 13.235 58.413 1.00 17.55 ? 198 ASP B CG 1 ATOM 3887 O OD1 . ASP B 1 118 ? 18.832 13.833 57.496 1.00 18.54 ? 198 ASP B OD1 1 ATOM 3888 O OD2 . ASP B 1 118 ? 19.093 12.105 58.819 1.00 22.40 ? 198 ASP B OD2 1 ATOM 3889 N N . ASN B 1 119 ? 23.167 15.967 59.200 1.00 9.88 ? 199 ASN B N 1 ATOM 3890 C CA . ASN B 1 119 ? 24.085 16.622 60.130 1.00 14.54 ? 199 ASN B CA 1 ATOM 3891 C C . ASN B 1 119 ? 24.589 17.989 59.667 1.00 16.98 ? 199 ASN B C 1 ATOM 3892 O O . ASN B 1 119 ? 25.468 18.578 60.299 1.00 14.58 ? 199 ASN B O 1 ATOM 3893 C CB . ASN B 1 119 ? 25.267 15.705 60.464 1.00 16.00 ? 199 ASN B CB 1 ATOM 3894 C CG . ASN B 1 119 ? 26.208 15.506 59.289 1.00 27.69 ? 199 ASN B CG 1 ATOM 3895 O OD1 . ASN B 1 119 ? 25.952 15.979 58.182 1.00 14.39 ? 199 ASN B OD1 1 ATOM 3896 N ND2 . ASN B 1 119 ? 27.309 14.804 59.530 1.00 25.58 ? 199 ASN B ND2 1 ATOM 3897 N N . GLY B 1 120 ? 24.029 18.497 58.573 1.00 11.82 ? 200 GLY B N 1 ATOM 3898 C CA . GLY B 1 120 ? 24.446 19.784 58.044 1.00 14.19 ? 200 GLY B CA 1 ATOM 3899 C C . GLY B 1 120 ? 23.544 20.304 56.940 1.00 8.64 ? 200 GLY B C 1 ATOM 3900 O O . GLY B 1 120 ? 24.022 20.807 55.923 1.00 7.87 ? 200 GLY B O 1 ATOM 3901 N N . ALA B 1 121 ? 22.236 20.192 57.148 1.00 7.18 ? 201 ALA B N 1 ATOM 3902 C CA . ALA B 1 121 ? 21.257 20.609 56.150 1.00 7.34 ? 201 ALA B CA 1 ATOM 3903 C C . ALA B 1 121 ? 21.312 22.113 55.912 1.00 7.67 ? 201 ALA B C 1 ATOM 3904 O O . ALA B 1 121 ? 21.658 22.882 56.808 1.00 6.67 ? 201 ALA B O 1 ATOM 3905 C CB . ALA B 1 121 ? 19.855 20.186 56.576 1.00 5.82 ? 201 ALA B CB 1 ATOM 3906 N N . VAL B 1 122 ? 20.965 22.528 54.698 1.00 6.23 ? 202 VAL B N 1 ATOM 3907 C CA . VAL B 1 122 ? 20.996 23.939 54.338 1.00 4.39 ? 202 VAL B CA 1 ATOM 3908 C C . VAL B 1 122 ? 19.668 24.392 53.749 1.00 5.11 ? 202 VAL B C 1 ATOM 3909 O O . VAL B 1 122 ? 19.164 23.801 52.795 1.00 6.24 ? 202 VAL B O 1 ATOM 3910 C CB . VAL B 1 122 ? 22.121 24.241 53.326 1.00 7.02 ? 202 VAL B CB 1 ATOM 3911 C CG1 . VAL B 1 122 ? 21.997 25.665 52.804 1.00 6.10 ? 202 VAL B CG1 1 ATOM 3912 C CG2 . VAL B 1 122 ? 23.485 24.018 53.967 1.00 5.34 ? 202 VAL B CG2 1 ATOM 3913 N N . ALA B 1 123 ? 19.100 25.441 54.330 1.00 8.59 ? 203 ALA B N 1 ATOM 3914 C CA . ALA B 1 123 ? 17.887 26.039 53.795 1.00 5.56 ? 203 ALA B CA 1 ATOM 3915 C C . ALA B 1 123 ? 18.260 27.044 52.715 1.00 6.53 ? 203 ALA B C 1 ATOM 3916 O O . ALA B 1 123 ? 19.027 27.973 52.959 1.00 6.52 ? 203 ALA B O 1 ATOM 3917 C CB . ALA B 1 123 ? 17.098 26.712 54.899 1.00 5.55 ? 203 ALA B CB 1 ATOM 3918 N N . VAL B 1 124 ? 17.730 26.842 51.515 1.00 4.41 ? 204 VAL B N 1 ATOM 3919 C CA . VAL B 1 124 ? 17.968 27.762 50.414 1.00 5.49 ? 204 VAL B CA 1 ATOM 3920 C C . VAL B 1 124 ? 16.756 28.667 50.234 1.00 4.36 ? 204 VAL B C 1 ATOM 3921 O O . VAL B 1 124 ? 15.650 28.190 49.992 1.00 4.02 ? 204 VAL B O 1 ATOM 3922 C CB . VAL B 1 124 ? 18.253 27.010 49.103 1.00 3.98 ? 204 VAL B CB 1 ATOM 3923 C CG1 . VAL B 1 124 ? 18.319 27.979 47.934 1.00 7.55 ? 204 VAL B CG1 1 ATOM 3924 C CG2 . VAL B 1 124 ? 19.547 26.203 49.220 1.00 2.81 ? 204 VAL B CG2 1 ATOM 3925 N N . LEU B 1 125 ? 16.966 29.971 50.372 1.00 4.02 ? 205 LEU B N 1 ATOM 3926 C CA . LEU B 1 125 ? 15.890 30.939 50.204 1.00 4.81 ? 205 LEU B CA 1 ATOM 3927 C C . LEU B 1 125 ? 15.877 31.502 48.789 1.00 5.18 ? 205 LEU B C 1 ATOM 3928 O O . LEU B 1 125 ? 16.916 31.893 48.255 1.00 5.98 ? 205 LEU B O 1 ATOM 3929 C CB . LEU B 1 125 ? 16.015 32.079 51.219 1.00 5.18 ? 205 LEU B CB 1 ATOM 3930 C CG . LEU B 1 125 ? 15.638 31.769 52.673 1.00 8.44 ? 205 LEU B CG 1 ATOM 3931 C CD1 . LEU B 1 125 ? 16.627 30.796 53.300 1.00 9.16 ? 205 LEU B CD1 1 ATOM 3932 C CD2 . LEU B 1 125 ? 15.558 33.051 53.489 1.00 5.68 ? 205 LEU B CD2 1 ATOM 3933 N N . LYS B 1 126 ? 14.693 31.539 48.189 1.00 4.05 ? 206 LYS B N 1 ATOM 3934 C CA . LYS B 1 126 ? 14.523 32.110 46.859 1.00 6.76 ? 206 LYS B CA 1 ATOM 3935 C C . LYS B 1 126 ? 13.456 33.196 46.879 1.00 5.34 ? 206 LYS B C 1 ATOM 3936 O O . LYS B 1 126 ? 12.420 33.053 47.526 1.00 6.04 ? 206 LYS B O 1 ATOM 3937 C CB . LYS B 1 126 ? 14.139 31.033 45.840 1.00 6.13 ? 206 LYS B CB 1 ATOM 3938 C CG . LYS B 1 126 ? 15.243 30.040 45.511 1.00 6.73 ? 206 LYS B CG 1 ATOM 3939 C CD . LYS B 1 126 ? 14.741 29.004 44.510 1.00 11.41 ? 206 LYS B CD 1 ATOM 3940 C CE . LYS B 1 126 ? 15.817 27.993 44.156 1.00 11.75 ? 206 LYS B CE 1 ATOM 3941 N NZ . LYS B 1 126 ? 15.346 27.024 43.127 1.00 9.19 ? 206 LYS B NZ 1 ATOM 3942 N N . TYR B 1 127 ? 13.725 34.285 46.170 1.00 4.46 ? 207 TYR B N 1 ATOM 3943 C CA . TYR B 1 127 ? 12.759 35.359 46.014 1.00 3.81 ? 207 TYR B CA 1 ATOM 3944 C C . TYR B 1 127 ? 12.560 35.554 44.521 1.00 4.57 ? 207 TYR B C 1 ATOM 3945 O O . TYR B 1 127 ? 13.505 35.879 43.804 1.00 5.96 ? 207 TYR B O 1 ATOM 3946 C CB . TYR B 1 127 ? 13.285 36.638 46.663 1.00 4.86 ? 207 TYR B CB 1 ATOM 3947 C CG . TYR B 1 127 ? 12.277 37.761 46.773 1.00 7.82 ? 207 TYR B CG 1 ATOM 3948 C CD1 . TYR B 1 127 ? 11.173 37.653 47.611 1.00 8.95 ? 207 TYR B CD1 1 ATOM 3949 C CD2 . TYR B 1 127 ? 12.446 38.943 46.063 1.00 8.93 ? 207 TYR B CD2 1 ATOM 3950 C CE1 . TYR B 1 127 ? 10.253 38.685 47.721 1.00 7.24 ? 207 TYR B CE1 1 ATOM 3951 C CE2 . TYR B 1 127 ? 11.535 39.979 46.170 1.00 11.15 ? 207 TYR B CE2 1 ATOM 3952 C CZ . TYR B 1 127 ? 10.442 39.845 47.000 1.00 9.77 ? 207 TYR B CZ 1 ATOM 3953 O OH . TYR B 1 127 ? 9.537 40.877 47.106 1.00 8.02 ? 207 TYR B OH 1 ATOM 3954 N N . ASN B 1 128 ? 11.334 35.338 44.055 1.00 4.64 ? 208 ASN B N 1 ATOM 3955 C CA . ASN B 1 128 ? 11.041 35.360 42.626 1.00 8.63 ? 208 ASN B CA 1 ATOM 3956 C C . ASN B 1 128 ? 11.915 34.362 41.869 1.00 8.10 ? 208 ASN B C 1 ATOM 3957 O O . ASN B 1 128 ? 12.377 34.635 40.760 1.00 10.16 ? 208 ASN B O 1 ATOM 3958 C CB . ASN B 1 128 ? 11.217 36.768 42.050 1.00 9.29 ? 208 ASN B CB 1 ATOM 3959 C CG . ASN B 1 128 ? 10.584 36.921 40.678 1.00 18.24 ? 208 ASN B CG 1 ATOM 3960 O OD1 . ASN B 1 128 ? 9.626 36.223 40.339 1.00 13.60 ? 208 ASN B OD1 1 ATOM 3961 N ND2 . ASN B 1 128 ? 11.115 37.841 39.882 1.00 18.73 ? 208 ASN B ND2 1 ATOM 3962 N N . GLY B 1 129 ? 12.151 33.209 42.487 1.00 9.11 ? 209 GLY B N 1 ATOM 3963 C CA . GLY B 1 129 ? 12.872 32.125 41.844 1.00 11.06 ? 209 GLY B CA 1 ATOM 3964 C C . GLY B 1 129 ? 14.384 32.258 41.861 1.00 11.59 ? 209 GLY B C 1 ATOM 3965 O O . GLY B 1 129 ? 15.093 31.381 41.367 1.00 13.52 ? 209 GLY B O 1 ATOM 3966 N N . ILE B 1 130 ? 14.880 33.353 42.424 1.00 4.50 ? 210 ILE B N 1 ATOM 3967 C CA . ILE B 1 130 ? 16.319 33.604 42.479 1.00 5.68 ? 210 ILE B CA 1 ATOM 3968 C C . ILE B 1 130 ? 16.849 33.379 43.893 1.00 6.88 ? 210 ILE B C 1 ATOM 3969 O O . ILE B 1 130 ? 16.284 33.894 44.856 1.00 6.60 ? 210 ILE B O 1 ATOM 3970 C CB . ILE B 1 130 ? 16.642 35.050 42.051 1.00 11.05 ? 210 ILE B CB 1 ATOM 3971 C CG1 . ILE B 1 130 ? 16.093 35.332 40.647 1.00 10.74 ? 210 ILE B CG1 1 ATOM 3972 C CG2 . ILE B 1 130 ? 18.142 35.314 42.118 1.00 8.15 ? 210 ILE B CG2 1 ATOM 3973 C CD1 . ILE B 1 130 ? 16.726 34.491 39.553 1.00 9.75 ? 210 ILE B CD1 1 ATOM 3974 N N . ILE B 1 131 ? 17.929 32.613 44.026 1.00 6.95 ? 211 ILE B N 1 ATOM 3975 C CA . ILE B 1 131 ? 18.507 32.374 45.348 1.00 7.82 ? 211 ILE B CA 1 ATOM 3976 C C . ILE B 1 131 ? 18.967 33.683 45.973 1.00 6.75 ? 211 ILE B C 1 ATOM 3977 O O . ILE B 1 131 ? 19.719 34.445 45.366 1.00 11.44 ? 211 ILE B O 1 ATOM 3978 C CB . ILE B 1 131 ? 19.687 31.388 45.307 1.00 9.05 ? 211 ILE B CB 1 ATOM 3979 C CG1 . ILE B 1 131 ? 19.206 30.001 44.880 1.00 5.21 ? 211 ILE B CG1 1 ATOM 3980 C CG2 . ILE B 1 131 ? 20.363 31.315 46.672 1.00 5.99 ? 211 ILE B CG2 1 ATOM 3981 C CD1 . ILE B 1 131 ? 20.310 28.962 44.820 1.00 9.74 ? 211 ILE B CD1 1 ATOM 3982 N N . THR B 1 132 ? 18.514 33.938 47.194 1.00 8.00 ? 212 THR B N 1 ATOM 3983 C CA . THR B 1 132 ? 18.787 35.208 47.848 1.00 9.51 ? 212 THR B CA 1 ATOM 3984 C C . THR B 1 132 ? 19.512 35.040 49.177 1.00 10.50 ? 212 THR B C 1 ATOM 3985 O O . THR B 1 132 ? 20.072 35.993 49.708 1.00 10.22 ? 212 THR B O 1 ATOM 3986 C CB . THR B 1 132 ? 17.489 36.002 48.076 1.00 7.56 ? 212 THR B CB 1 ATOM 3987 O OG1 . THR B 1 132 ? 16.484 35.129 48.603 1.00 6.32 ? 212 THR B OG1 1 ATOM 3988 C CG2 . THR B 1 132 ? 16.990 36.599 46.765 1.00 9.59 ? 212 THR B CG2 1 ATOM 3989 N N . ASP B 1 133 ? 19.505 33.828 49.718 1.00 8.24 ? 213 ASP B N 1 ATOM 3990 C CA . ASP B 1 133 ? 20.134 33.598 51.012 1.00 10.00 ? 213 ASP B CA 1 ATOM 3991 C C . ASP B 1 133 ? 20.144 32.117 51.339 1.00 8.69 ? 213 ASP B C 1 ATOM 3992 O O . ASP B 1 133 ? 19.428 31.328 50.725 1.00 7.46 ? 213 ASP B O 1 ATOM 3993 C CB . ASP B 1 133 ? 19.386 34.368 52.106 1.00 9.37 ? 213 ASP B CB 1 ATOM 3994 C CG . ASP B 1 133 ? 20.294 34.811 53.244 1.00 14.11 ? 213 ASP B CG 1 ATOM 3995 O OD1 . ASP B 1 133 ? 21.446 34.332 53.326 1.00 13.19 ? 213 ASP B OD1 1 ATOM 3996 O OD2 . ASP B 1 133 ? 19.851 35.647 54.059 1.00 14.09 ? 213 ASP B OD2 1 ATOM 3997 N N . THR B 1 134 ? 20.974 31.743 52.305 1.00 6.68 ? 214 THR B N 1 ATOM 3998 C CA . THR B 1 134 ? 20.962 30.390 52.836 1.00 8.29 ? 214 THR B CA 1 ATOM 3999 C C . THR B 1 134 ? 21.147 30.452 54.343 1.00 11.99 ? 214 THR B C 1 ATOM 4000 O O . THR B 1 134 ? 21.686 31.422 54.875 1.00 12.51 ? 214 THR B O 1 ATOM 4001 C CB . THR B 1 134 ? 22.084 29.516 52.238 1.00 9.19 ? 214 THR B CB 1 ATOM 4002 O OG1 . THR B 1 134 ? 23.361 30.024 52.645 1.00 12.12 ? 214 THR B OG1 1 ATOM 4003 C CG2 . THR B 1 134 ? 22.007 29.490 50.718 1.00 8.59 ? 214 THR B CG2 1 ATOM 4004 N N . ILE B 1 135 ? 20.693 29.414 55.029 1.00 8.52 ? 215 ILE B N 1 ATOM 4005 C CA . ILE B 1 135 ? 20.936 29.286 56.454 1.00 12.83 ? 215 ILE B CA 1 ATOM 4006 C C . ILE B 1 135 ? 21.213 27.820 56.751 1.00 12.74 ? 215 ILE B C 1 ATOM 4007 O O . ILE B 1 135 ? 20.464 26.938 56.330 1.00 11.72 ? 215 ILE B O 1 ATOM 4008 C CB . ILE B 1 135 ? 19.758 29.838 57.291 1.00 17.53 ? 215 ILE B CB 1 ATOM 4009 C CG1 . ILE B 1 135 ? 20.062 29.752 58.790 1.00 18.88 ? 215 ILE B CG1 1 ATOM 4010 C CG2 . ILE B 1 135 ? 18.470 29.110 56.958 1.00 17.53 ? 215 ILE B CG2 1 ATOM 4011 C CD1 . ILE B 1 135 ? 19.673 28.433 59.423 1.00 19.56 ? 215 ILE B CD1 1 ATOM 4012 N N . LYS B 1 136 ? 22.309 27.561 57.454 1.00 9.42 ? 216 LYS B N 1 ATOM 4013 C CA . LYS B 1 136 ? 22.747 26.194 57.684 1.00 9.72 ? 216 LYS B CA 1 ATOM 4014 C C . LYS B 1 136 ? 22.425 25.716 59.095 1.00 10.07 ? 216 LYS B C 1 ATOM 4015 O O . LYS B 1 136 ? 22.383 26.509 60.037 1.00 9.81 ? 216 LYS B O 1 ATOM 4016 C CB . LYS B 1 136 ? 24.246 26.059 57.406 1.00 10.72 ? 216 LYS B CB 1 ATOM 4017 C CG . LYS B 1 136 ? 24.767 24.633 57.483 1.00 11.96 ? 216 LYS B CG 1 ATOM 4018 C CD . LYS B 1 136 ? 26.150 24.526 56.870 1.00 15.58 ? 216 LYS B CD 1 ATOM 4019 C CE . LYS B 1 136 ? 26.621 23.084 56.819 1.00 16.85 ? 216 LYS B CE 1 ATOM 4020 N NZ . LYS B 1 136 ? 27.963 22.983 56.185 1.00 20.12 ? 216 LYS B NZ 1 ATOM 4021 N N . SER B 1 137 ? 22.189 24.414 59.217 1.00 8.37 ? 217 SER B N 1 ATOM 4022 C CA . SER B 1 137 ? 21.940 23.765 60.498 1.00 8.38 ? 217 SER B CA 1 ATOM 4023 C C . SER B 1 137 ? 22.908 24.272 61.562 1.00 11.16 ? 217 SER B C 1 ATOM 4024 O O . SER B 1 137 ? 24.113 24.339 61.324 1.00 8.51 ? 217 SER B O 1 ATOM 4025 C CB . SER B 1 137 ? 22.086 22.250 60.333 1.00 7.72 ? 217 SER B CB 1 ATOM 4026 O OG . SER B 1 137 ? 21.849 21.560 61.546 1.00 8.75 ? 217 SER B OG 1 ATOM 4027 N N . TRP B 1 138 ? 22.381 24.634 62.730 1.00 9.50 ? 218 TRP B N 1 ATOM 4028 C CA . TRP B 1 138 ? 23.220 25.137 63.819 1.00 8.98 ? 218 TRP B CA 1 ATOM 4029 C C . TRP B 1 138 ? 23.359 24.137 64.968 1.00 9.56 ? 218 TRP B C 1 ATOM 4030 O O . TRP B 1 138 ? 24.168 24.333 65.875 1.00 12.74 ? 218 TRP B O 1 ATOM 4031 C CB . TRP B 1 138 ? 22.709 26.488 64.334 1.00 9.64 ? 218 TRP B CB 1 ATOM 4032 C CG . TRP B 1 138 ? 21.344 26.435 64.955 1.00 9.29 ? 218 TRP B CG 1 ATOM 4033 C CD1 . TRP B 1 138 ? 21.051 26.237 66.272 1.00 13.30 ? 218 TRP B CD1 1 ATOM 4034 C CD2 . TRP B 1 138 ? 20.088 26.592 64.283 1.00 10.82 ? 218 TRP B CD2 1 ATOM 4035 N NE1 . TRP B 1 138 ? 19.690 26.258 66.463 1.00 12.12 ? 218 TRP B NE1 1 ATOM 4036 C CE2 . TRP B 1 138 ? 19.076 26.472 65.257 1.00 11.51 ? 218 TRP B CE2 1 ATOM 4037 C CE3 . TRP B 1 138 ? 19.721 26.819 62.953 1.00 11.52 ? 218 TRP B CE3 1 ATOM 4038 C CZ2 . TRP B 1 138 ? 17.723 26.571 64.943 1.00 12.20 ? 218 TRP B CZ2 1 ATOM 4039 C CZ3 . TRP B 1 138 ? 18.375 26.920 62.644 1.00 9.54 ? 218 TRP B CZ3 1 ATOM 4040 C CH2 . TRP B 1 138 ? 17.393 26.795 63.634 1.00 8.11 ? 218 TRP B CH2 1 ATOM 4041 N N . ARG B 1 139 ? 22.573 23.067 64.920 1.00 8.70 ? 219 ARG B N 1 ATOM 4042 C CA . ARG B 1 139 ? 22.676 21.991 65.903 1.00 12.86 ? 219 ARG B CA 1 ATOM 4043 C C . ARG B 1 139 ? 23.070 20.678 65.234 1.00 12.72 ? 219 ARG B C 1 ATOM 4044 O O . ARG B 1 139 ? 23.240 19.658 65.903 1.00 12.98 ? 219 ARG B O 1 ATOM 4045 C CB . ARG B 1 139 ? 21.358 21.810 66.659 1.00 12.71 ? 219 ARG B CB 1 ATOM 4046 C CG . ARG B 1 139 ? 21.000 22.957 67.589 1.00 12.43 ? 219 ARG B CG 1 ATOM 4047 C CD . ARG B 1 139 ? 21.916 23.010 68.808 1.00 22.23 ? 219 ARG B CD 1 ATOM 4048 N NE . ARG B 1 139 ? 21.545 24.096 69.712 1.00 26.43 ? 219 ARG B NE 1 ATOM 4049 C CZ . ARG B 1 139 ? 20.799 23.944 70.803 1.00 28.64 ? 219 ARG B CZ 1 ATOM 4050 N NH1 . ARG B 1 139 ? 20.343 22.744 71.134 1.00 27.90 ? 219 ARG B NH1 1 ATOM 4051 N NH2 . ARG B 1 139 ? 20.512 24.992 71.563 1.00 31.40 ? 219 ARG B NH2 1 ATOM 4052 N N . ASN B 1 140 ? 23.206 20.709 63.911 1.00 13.68 ? 220 ASN B N 1 ATOM 4053 C CA . ASN B 1 140 ? 23.621 19.530 63.154 1.00 13.38 ? 220 ASN B CA 1 ATOM 4054 C C . ASN B 1 140 ? 22.701 18.334 63.373 1.00 12.00 ? 220 ASN B C 1 ATOM 4055 O O . ASN B 1 140 ? 23.158 17.192 63.435 1.00 12.41 ? 220 ASN B O 1 ATOM 4056 C CB . ASN B 1 140 ? 25.061 19.146 63.507 1.00 15.37 ? 220 ASN B CB 1 ATOM 4057 C CG . ASN B 1 140 ? 26.040 20.281 63.274 1.00 22.74 ? 220 ASN B CG 1 ATOM 4058 O OD1 . ASN B 1 140 ? 25.796 21.170 62.459 1.00 23.16 ? 220 ASN B OD1 1 ATOM 4059 N ND2 . ASN B 1 140 ? 27.157 20.254 63.990 1.00 31.61 ? 220 ASN B ND2 1 ATOM 4060 N N . ASN B 1 141 ? 21.404 18.595 63.485 1.00 12.56 ? 221 ASN B N 1 ATOM 4061 C CA . ASN B 1 141 ? 20.444 17.526 63.727 1.00 8.23 ? 221 ASN B CA 1 ATOM 4062 C C . ASN B 1 141 ? 19.106 17.771 63.031 1.00 10.75 ? 221 ASN B C 1 ATOM 4063 O O . ASN B 1 141 ? 18.100 18.067 63.676 1.00 8.64 ? 221 ASN B O 1 ATOM 4064 C CB . ASN B 1 141 ? 20.242 17.323 65.230 1.00 11.27 ? 221 ASN B CB 1 ATOM 4065 C CG . ASN B 1 141 ? 19.540 16.018 65.553 1.00 15.69 ? 221 ASN B CG 1 ATOM 4066 O OD1 . ASN B 1 141 ? 19.079 15.308 64.658 1.00 13.97 ? 221 ASN B OD1 1 ATOM 4067 N ND2 . ASN B 1 141 ? 19.457 15.694 66.838 1.00 14.04 ? 221 ASN B ND2 1 ATOM 4068 N N . ILE B 1 142 ? 19.117 17.648 61.707 1.00 9.07 ? 222 ILE B N 1 ATOM 4069 C CA . ILE B 1 142 ? 17.917 17.773 60.881 1.00 7.42 ? 222 ILE B CA 1 ATOM 4070 C C . ILE B 1 142 ? 17.237 19.138 60.989 1.00 8.82 ? 222 ILE B C 1 ATOM 4071 O O . ILE B 1 142 ? 16.162 19.265 61.574 1.00 9.48 ? 222 ILE B O 1 ATOM 4072 C CB . ILE B 1 142 ? 16.897 16.649 61.170 1.00 7.63 ? 222 ILE B CB 1 ATOM 4073 C CG1 . ILE B 1 142 ? 17.592 15.286 61.179 1.00 10.10 ? 222 ILE B CG1 1 ATOM 4074 C CG2 . ILE B 1 142 ? 15.785 16.661 60.132 1.00 11.53 ? 222 ILE B CG2 1 ATOM 4075 C CD1 . ILE B 1 142 ? 16.668 14.126 61.489 1.00 12.93 ? 222 ILE B CD1 1 ATOM 4076 N N . LEU B 1 143 ? 17.871 20.158 60.420 1.00 9.08 ? 223 LEU B N 1 ATOM 4077 C CA . LEU B 1 143 ? 17.241 21.465 60.288 1.00 7.74 ? 223 LEU B CA 1 ATOM 4078 C C . LEU B 1 143 ? 15.922 21.285 59.548 1.00 6.47 ? 223 LEU B C 1 ATOM 4079 O O . LEU B 1 143 ? 15.877 20.626 58.511 1.00 6.04 ? 223 LEU B O 1 ATOM 4080 C CB . LEU B 1 143 ? 18.152 22.414 59.513 1.00 8.47 ? 223 LEU B CB 1 ATOM 4081 C CG . LEU B 1 143 ? 17.608 23.815 59.225 1.00 7.58 ? 223 LEU B CG 1 ATOM 4082 C CD1 . LEU B 1 143 ? 17.357 24.570 60.524 1.00 4.62 ? 223 LEU B CD1 1 ATOM 4083 C CD2 . LEU B 1 143 ? 18.574 24.583 58.334 1.00 8.16 ? 223 LEU B CD2 1 ATOM 4084 N N . ARG B 1 144 ? 14.849 21.862 60.080 1.00 4.64 ? 224 ARG B N 1 ATOM 4085 C CA . ARG B 1 144 ? 13.521 21.647 59.513 1.00 7.05 ? 224 ARG B CA 1 ATOM 4086 C C . ARG B 1 144 ? 12.586 22.834 59.740 1.00 5.82 ? 224 ARG B C 1 ATOM 4087 O O . ARG B 1 144 ? 12.770 23.609 60.678 1.00 6.36 ? 224 ARG B O 1 ATOM 4088 C CB . ARG B 1 144 ? 12.911 20.351 60.061 1.00 8.46 ? 224 ARG B CB 1 ATOM 4089 C CG . ARG B 1 144 ? 12.936 20.222 61.586 1.00 7.78 ? 224 ARG B CG 1 ATOM 4090 C CD . ARG B 1 144 ? 12.766 18.764 62.004 1.00 8.89 ? 224 ARG B CD 1 ATOM 4091 N NE . ARG B 1 144 ? 12.570 18.598 63.442 1.00 7.90 ? 224 ARG B NE 1 ATOM 4092 C CZ . ARG B 1 144 ? 13.556 18.489 64.328 1.00 10.04 ? 224 ARG B CZ 1 ATOM 4093 N NH1 . ARG B 1 144 ? 14.821 18.536 63.930 1.00 7.39 ? 224 ARG B NH1 1 ATOM 4094 N NH2 . ARG B 1 144 ? 13.278 18.336 65.615 1.00 9.52 ? 224 ARG B NH2 1 ATOM 4095 N N . THR B 1 145 ? 11.584 22.975 58.876 1.00 7.48 ? 225 THR B N 1 ATOM 4096 C CA . THR B 1 145 ? 10.696 24.134 58.939 1.00 5.61 ? 225 THR B CA 1 ATOM 4097 C C . THR B 1 145 ? 9.201 23.774 58.902 1.00 7.18 ? 225 THR B C 1 ATOM 4098 O O . THR B 1 145 ? 8.816 22.649 59.224 1.00 7.50 ? 225 THR B O 1 ATOM 4099 C CB . THR B 1 145 ? 11.066 25.194 57.863 1.00 5.34 ? 225 THR B CB 1 ATOM 4100 O OG1 . THR B 1 145 ? 10.339 26.408 58.096 1.00 10.93 ? 225 THR B OG1 1 ATOM 4101 C CG2 . THR B 1 145 ? 10.788 24.679 56.455 1.00 7.60 ? 225 THR B CG2 1 ATOM 4102 N N . GLN B 1 146 ? 8.372 24.735 58.507 1.00 6.10 ? 226 GLN B N 1 ATOM 4103 C CA . GLN B 1 146 ? 6.923 24.668 58.710 1.00 5.67 ? 226 GLN B CA 1 ATOM 4104 C C . GLN B 1 146 ? 6.171 23.544 57.992 1.00 7.49 ? 226 GLN B C 1 ATOM 4105 O O . GLN B 1 146 ? 5.280 22.924 58.569 1.00 6.83 ? 226 GLN B O 1 ATOM 4106 C CB . GLN B 1 146 ? 6.282 25.995 58.307 1.00 5.55 ? 226 GLN B CB 1 ATOM 4107 C CG . GLN B 1 146 ? 6.731 27.197 59.115 1.00 7.00 ? 226 GLN B CG 1 ATOM 4108 C CD . GLN B 1 146 ? 6.011 28.460 58.687 1.00 8.96 ? 226 GLN B CD 1 ATOM 4109 O OE1 . GLN B 1 146 ? 6.623 29.396 58.171 1.00 13.32 ? 226 GLN B OE1 1 ATOM 4110 N NE2 . GLN B 1 146 ? 4.697 28.483 58.880 1.00 7.80 ? 226 GLN B NE2 1 ATOM 4111 N N . GLU B 1 147 ? 6.508 23.310 56.728 1.00 4.54 ? 227 GLU B N 1 ATOM 4112 C CA . GLU B 1 147 ? 5.678 22.481 55.853 1.00 6.14 ? 227 GLU B CA 1 ATOM 4113 C C . GLU B 1 147 ? 4.304 23.136 55.656 1.00 8.08 ? 227 GLU B C 1 ATOM 4114 O O . GLU B 1 147 ? 3.306 22.461 55.403 1.00 8.79 ? 227 GLU B O 1 ATOM 4115 C CB . GLU B 1 147 ? 5.522 21.054 56.395 1.00 11.49 ? 227 GLU B CB 1 ATOM 4116 C CG . GLU B 1 147 ? 6.726 20.505 57.160 1.00 11.80 ? 227 GLU B CG 1 ATOM 4117 C CD . GLU B 1 147 ? 7.987 20.392 56.319 1.00 15.15 ? 227 GLU B CD 1 ATOM 4118 O OE1 . GLU B 1 147 ? 7.956 20.741 55.120 1.00 10.57 ? 227 GLU B OE1 1 ATOM 4119 O OE2 . GLU B 1 147 ? 9.019 19.946 56.868 1.00 15.40 ? 227 GLU B OE2 1 ATOM 4120 N N . SER B 1 148 ? 4.264 24.457 55.803 1.00 6.03 ? 228 SER B N 1 ATOM 4121 C CA . SER B 1 148 ? 3.096 25.254 55.434 1.00 6.27 ? 228 SER B CA 1 ATOM 4122 C C . SER B 1 148 ? 3.556 26.681 55.148 1.00 8.00 ? 228 SER B C 1 ATOM 4123 O O . SER B 1 148 ? 4.752 26.970 55.205 1.00 8.55 ? 228 SER B O 1 ATOM 4124 C CB . SER B 1 148 ? 2.005 25.215 56.513 1.00 11.18 ? 228 SER B CB 1 ATOM 4125 O OG . SER B 1 148 ? 2.456 25.749 57.745 1.00 10.97 ? 228 SER B OG 1 ATOM 4126 N N . GLU B 1 149 ? 2.621 27.572 54.843 1.00 6.02 ? 229 GLU B N 1 ATOM 4127 C CA . GLU B 1 149 ? 2.991 28.913 54.393 1.00 8.02 ? 229 GLU B CA 1 ATOM 4128 C C . GLU B 1 149 ? 3.599 29.772 55.496 1.00 6.81 ? 229 GLU B C 1 ATOM 4129 O O . GLU B 1 149 ? 3.169 29.713 56.648 1.00 7.49 ? 229 GLU B O 1 ATOM 4130 C CB . GLU B 1 149 ? 1.788 29.636 53.785 1.00 6.41 ? 229 GLU B CB 1 ATOM 4131 C CG . GLU B 1 149 ? 0.807 30.191 54.806 1.00 7.83 ? 229 GLU B CG 1 ATOM 4132 C CD . GLU B 1 149 ? -0.220 31.114 54.180 1.00 14.20 ? 229 GLU B CD 1 ATOM 4133 O OE1 . GLU B 1 149 ? -0.143 31.346 52.954 1.00 12.68 ? 229 GLU B OE1 1 ATOM 4134 O OE2 . GLU B 1 149 ? -1.102 31.611 54.912 1.00 10.28 ? 229 GLU B OE2 1 ATOM 4135 N N . CYS B 1 150 ? 4.607 30.565 55.137 1.00 7.60 ? 230 CYS B N 1 ATOM 4136 C CA . CYS B 1 150 ? 5.114 31.586 56.043 1.00 9.10 ? 230 CYS B CA 1 ATOM 4137 C C . CYS B 1 150 ? 4.114 32.740 56.099 1.00 10.08 ? 230 CYS B C 1 ATOM 4138 O O . CYS B 1 150 ? 3.138 32.759 55.349 1.00 8.43 ? 230 CYS B O 1 ATOM 4139 C CB . CYS B 1 150 ? 6.522 32.066 55.644 1.00 7.90 ? 230 CYS B CB 1 ATOM 4140 S SG . CYS B 1 150 ? 6.953 32.005 53.876 1.00 10.57 ? 230 CYS B SG 1 ATOM 4141 N N . ALA B 1 151 ? 4.342 33.689 56.997 1.00 6.50 ? 231 ALA B N 1 ATOM 4142 C CA . ALA B 1 151 ? 3.395 34.783 57.190 1.00 7.98 ? 231 ALA B CA 1 ATOM 4143 C C . ALA B 1 151 ? 4.045 36.124 56.885 1.00 10.71 ? 231 ALA B C 1 ATOM 4144 O O . ALA B 1 151 ? 5.167 36.381 57.311 1.00 5.68 ? 231 ALA B O 1 ATOM 4145 C CB . ALA B 1 151 ? 2.845 34.762 58.608 1.00 8.00 ? 231 ALA B CB 1 ATOM 4146 N N . CYS B 1 152 ? 3.336 36.974 56.147 1.00 9.41 ? 232 CYS B N 1 ATOM 4147 C CA . CYS B 1 152 ? 3.900 38.243 55.695 1.00 9.87 ? 232 CYS B CA 1 ATOM 4148 C C . CYS B 1 152 ? 3.160 39.455 56.249 1.00 10.80 ? 232 CYS B C 1 ATOM 4149 O O . CYS B 1 152 ? 1.928 39.488 56.288 1.00 14.04 ? 232 CYS B O 1 ATOM 4150 C CB . CYS B 1 152 ? 3.938 38.305 54.165 1.00 13.11 ? 232 CYS B CB 1 ATOM 4151 S SG . CYS B 1 152 ? 5.036 37.090 53.387 1.00 17.90 ? 232 CYS B SG 1 ATOM 4152 N N . VAL B 1 153 ? 3.930 40.446 56.683 1.00 7.70 ? 233 VAL B N 1 ATOM 4153 C CA . VAL B 1 153 ? 3.384 41.706 57.162 1.00 8.49 ? 233 VAL B CA 1 ATOM 4154 C C . VAL B 1 153 ? 4.250 42.861 56.671 1.00 12.86 ? 233 VAL B C 1 ATOM 4155 O O . VAL B 1 153 ? 5.446 42.911 56.952 1.00 7.95 ? 233 VAL B O 1 ATOM 4156 C CB . VAL B 1 153 ? 3.330 41.764 58.701 1.00 10.56 ? 233 VAL B CB 1 ATOM 4157 C CG1 . VAL B 1 153 ? 2.926 43.159 59.160 1.00 10.84 ? 233 VAL B CG1 1 ATOM 4158 C CG2 . VAL B 1 153 ? 2.368 40.716 59.251 1.00 9.87 ? 233 VAL B CG2 1 ATOM 4159 N N . ASN B 1 154 ? 3.636 43.775 55.927 1.00 10.61 ? 234 ASN B N 1 ATOM 4160 C CA . ASN B 1 154 ? 4.300 44.988 55.452 1.00 13.80 ? 234 ASN B CA 1 ATOM 4161 C C . ASN B 1 154 ? 5.692 44.786 54.851 1.00 10.25 ? 234 ASN B C 1 ATOM 4162 O O . ASN B 1 154 ? 6.637 45.489 55.205 1.00 11.40 ? 234 ASN B O 1 ATOM 4163 C CB . ASN B 1 154 ? 4.370 46.028 56.572 1.00 14.76 ? 234 ASN B CB 1 ATOM 4164 C CG . ASN B 1 154 ? 4.797 47.391 56.070 1.00 15.33 ? 234 ASN B CG 1 ATOM 4165 O OD1 . ASN B 1 154 ? 4.411 47.809 54.979 1.00 23.49 ? 234 ASN B OD1 1 ATOM 4166 N ND2 . ASN B 1 154 ? 5.599 48.089 56.860 1.00 20.70 ? 234 ASN B ND2 1 ATOM 4167 N N . GLY B 1 155 ? 5.817 43.832 53.936 1.00 12.87 ? 235 GLY B N 1 ATOM 4168 C CA . GLY B 1 155 ? 7.071 43.632 53.230 1.00 12.94 ? 235 GLY B CA 1 ATOM 4169 C C . GLY B 1 155 ? 8.041 42.685 53.910 1.00 15.62 ? 235 GLY B C 1 ATOM 4170 O O . GLY B 1 155 ? 9.088 42.354 53.353 1.00 13.05 ? 235 GLY B O 1 ATOM 4171 N N . SER B 1 156 ? 7.708 42.249 55.119 1.00 8.10 ? 236 SER B N 1 ATOM 4172 C CA . SER B 1 156 ? 8.541 41.277 55.812 1.00 8.05 ? 236 SER B CA 1 ATOM 4173 C C . SER B 1 156 ? 7.788 39.969 55.969 1.00 10.06 ? 236 SER B C 1 ATOM 4174 O O . SER B 1 156 ? 6.595 39.967 56.271 1.00 8.47 ? 236 SER B O 1 ATOM 4175 C CB . SER B 1 156 ? 8.976 41.800 57.182 1.00 11.08 ? 236 SER B CB 1 ATOM 4176 O OG . SER B 1 156 ? 9.747 42.982 57.060 1.00 17.00 ? 236 SER B OG 1 ATOM 4177 N N . CYS B 1 157 ? 8.487 38.861 55.756 1.00 6.58 ? 237 CYS B N 1 ATOM 4178 C CA . CYS B 1 157 ? 7.899 37.540 55.923 1.00 7.02 ? 237 CYS B CA 1 ATOM 4179 C C . CYS B 1 157 ? 8.589 36.804 57.068 1.00 8.96 ? 237 CYS B C 1 ATOM 4180 O O . CYS B 1 157 ? 9.780 36.987 57.307 1.00 7.13 ? 237 CYS B O 1 ATOM 4181 C CB . CYS B 1 157 ? 7.997 36.733 54.628 1.00 7.45 ? 237 CYS B CB 1 ATOM 4182 S SG . CYS B 1 157 ? 7.038 37.429 53.254 1.00 17.43 ? 237 CYS B SG 1 ATOM 4183 N N . PHE B 1 158 ? 7.834 35.970 57.770 1.00 6.21 ? 238 PHE B N 1 ATOM 4184 C CA . PHE B 1 158 ? 8.331 35.342 58.986 1.00 6.23 ? 238 PHE B CA 1 ATOM 4185 C C . PHE B 1 158 ? 8.114 33.836 58.974 1.00 5.70 ? 238 PHE B C 1 ATOM 4186 O O . PHE B 1 158 ? 7.082 33.348 58.513 1.00 8.36 ? 238 PHE B O 1 ATOM 4187 C CB . PHE B 1 158 ? 7.639 35.951 60.206 1.00 6.30 ? 238 PHE B CB 1 ATOM 4188 C CG . PHE B 1 158 ? 7.765 37.446 60.292 1.00 6.34 ? 238 PHE B CG 1 ATOM 4189 C CD1 . PHE B 1 158 ? 6.904 38.271 59.584 1.00 6.00 ? 238 PHE B CD1 1 ATOM 4190 C CD2 . PHE B 1 158 ? 8.741 38.027 61.087 1.00 5.75 ? 238 PHE B CD2 1 ATOM 4191 C CE1 . PHE B 1 158 ? 7.016 39.647 59.662 1.00 6.42 ? 238 PHE B CE1 1 ATOM 4192 C CE2 . PHE B 1 158 ? 8.857 39.406 61.173 1.00 7.94 ? 238 PHE B CE2 1 ATOM 4193 C CZ . PHE B 1 158 ? 7.995 40.216 60.459 1.00 6.05 ? 238 PHE B CZ 1 ATOM 4194 N N . THR B 1 159 ? 9.094 33.101 59.489 1.00 7.51 ? 239 THR B N 1 ATOM 4195 C CA . THR B 1 159 ? 8.976 31.655 59.607 1.00 7.13 ? 239 THR B CA 1 ATOM 4196 C C . THR B 1 159 ? 9.684 31.158 60.865 1.00 10.46 ? 239 THR B C 1 ATOM 4197 O O . THR B 1 159 ? 10.422 31.902 61.509 1.00 10.83 ? 239 THR B O 1 ATOM 4198 C CB . THR B 1 159 ? 9.545 30.934 58.369 1.00 12.18 ? 239 THR B CB 1 ATOM 4199 O OG1 . THR B 1 159 ? 9.216 29.540 58.433 1.00 12.29 ? 239 THR B OG1 1 ATOM 4200 C CG2 . THR B 1 159 ? 11.060 31.095 58.295 1.00 10.74 ? 239 THR B CG2 1 ATOM 4201 N N . VAL B 1 160 ? 9.437 29.902 61.217 1.00 9.49 ? 240 VAL B N 1 ATOM 4202 C CA . VAL B 1 160 ? 10.086 29.273 62.357 1.00 7.29 ? 240 VAL B CA 1 ATOM 4203 C C . VAL B 1 160 ? 10.812 28.020 61.888 1.00 6.90 ? 240 VAL B C 1 ATOM 4204 O O . VAL B 1 160 ? 10.290 27.270 61.062 1.00 6.75 ? 240 VAL B O 1 ATOM 4205 C CB . VAL B 1 160 ? 9.059 28.881 63.437 1.00 8.80 ? 240 VAL B CB 1 ATOM 4206 C CG1 . VAL B 1 160 ? 9.731 28.105 64.564 1.00 8.39 ? 240 VAL B CG1 1 ATOM 4207 C CG2 . VAL B 1 160 ? 8.352 30.120 63.974 1.00 8.18 ? 240 VAL B CG2 1 ATOM 4208 N N . MET B 1 161 ? 12.018 27.804 62.402 1.00 6.14 ? 241 MET B N 1 ATOM 4209 C CA . MET B 1 161 ? 12.773 26.594 62.097 1.00 6.82 ? 241 MET B CA 1 ATOM 4210 C C . MET B 1 161 ? 13.242 25.898 63.368 1.00 6.34 ? 241 MET B C 1 ATOM 4211 O O . MET B 1 161 ? 13.453 26.538 64.397 1.00 6.36 ? 241 MET B O 1 ATOM 4212 C CB . MET B 1 161 ? 13.982 26.907 61.213 1.00 6.43 ? 241 MET B CB 1 ATOM 4213 C CG . MET B 1 161 ? 13.636 27.508 59.869 1.00 6.04 ? 241 MET B CG 1 ATOM 4214 S SD . MET B 1 161 ? 15.048 27.504 58.748 1.00 14.26 ? 241 MET B SD 1 ATOM 4215 C CE . MET B 1 161 ? 14.403 28.495 57.403 1.00 24.33 ? 241 MET B CE 1 ATOM 4216 N N . THR B 1 162 ? 13.414 24.583 63.280 1.00 5.08 ? 242 THR B N 1 ATOM 4217 C CA . THR B 1 162 ? 13.847 23.778 64.414 1.00 7.38 ? 242 THR B CA 1 ATOM 4218 C C . THR B 1 162 ? 15.086 22.966 64.051 1.00 7.72 ? 242 THR B C 1 ATOM 4219 O O . THR B 1 162 ? 15.227 22.503 62.920 1.00 5.80 ? 242 THR B O 1 ATOM 4220 C CB . THR B 1 162 ? 12.735 22.807 64.856 1.00 5.60 ? 242 THR B CB 1 ATOM 4221 O OG1 . THR B 1 162 ? 11.553 23.549 65.177 1.00 8.02 ? 242 THR B OG1 1 ATOM 4222 C CG2 . THR B 1 162 ? 13.174 21.998 66.072 1.00 6.60 ? 242 THR B CG2 1 ATOM 4223 N N . ASP B 1 163 ? 15.981 22.801 65.019 1.00 5.31 ? 243 ASP B N 1 ATOM 4224 C CA . ASP B 1 163 ? 17.172 21.981 64.841 1.00 6.82 ? 243 ASP B CA 1 ATOM 4225 C C . ASP B 1 163 ? 17.418 21.249 66.157 1.00 6.51 ? 243 ASP B C 1 ATOM 4226 O O . ASP B 1 163 ? 17.385 21.860 67.220 1.00 6.00 ? 243 ASP B O 1 ATOM 4227 C CB . ASP B 1 163 ? 18.367 22.863 64.479 1.00 7.55 ? 243 ASP B CB 1 ATOM 4228 C CG . ASP B 1 163 ? 19.474 22.098 63.776 1.00 9.45 ? 243 ASP B CG 1 ATOM 4229 O OD1 . ASP B 1 163 ? 19.499 20.852 63.859 1.00 9.75 ? 243 ASP B OD1 1 ATOM 4230 O OD2 . ASP B 1 163 ? 20.325 22.755 63.140 1.00 10.13 ? 243 ASP B OD2 1 ATOM 4231 N N . GLY B 1 164 ? 17.642 19.942 66.087 1.00 8.58 ? 244 GLY B N 1 ATOM 4232 C CA . GLY B 1 164 ? 17.802 19.142 67.290 1.00 9.41 ? 244 GLY B CA 1 ATOM 4233 C C . GLY B 1 164 ? 16.848 17.964 67.336 1.00 9.13 ? 244 GLY B C 1 ATOM 4234 O O . GLY B 1 164 ? 16.150 17.692 66.361 1.00 11.11 ? 244 GLY B O 1 ATOM 4235 N N . PRO B 1 165 ? 16.810 17.256 68.477 1.00 9.22 ? 245 PRO B N 1 ATOM 4236 C CA . PRO B 1 165 ? 16.024 16.028 68.649 1.00 11.13 ? 245 PRO B CA 1 ATOM 4237 C C . PRO B 1 165 ? 14.528 16.218 68.410 1.00 9.56 ? 245 PRO B C 1 ATOM 4238 O O . PRO B 1 165 ? 13.985 17.290 68.676 1.00 8.52 ? 245 PRO B O 1 ATOM 4239 C CB . PRO B 1 165 ? 16.267 15.661 70.118 1.00 11.89 ? 245 PRO B CB 1 ATOM 4240 C CG . PRO B 1 165 ? 17.567 16.297 70.457 1.00 15.35 ? 245 PRO B CG 1 ATOM 4241 C CD . PRO B 1 165 ? 17.593 17.581 69.682 1.00 13.32 ? 245 PRO B CD 1 ATOM 4242 N N . SER B 1 166 ? 13.873 15.175 67.912 1.00 11.27 ? 246 SER B N 1 ATOM 4243 C CA . SER B 1 166 ? 12.424 15.189 67.752 1.00 13.21 ? 246 SER B CA 1 ATOM 4244 C C . SER B 1 166 ? 11.760 14.469 68.923 1.00 15.18 ? 246 SER B C 1 ATOM 4245 O O . SER B 1 166 ? 10.534 14.347 68.980 1.00 13.41 ? 246 SER B O 1 ATOM 4246 C CB . SER B 1 166 ? 12.020 14.542 66.425 1.00 15.43 ? 246 SER B CB 1 ATOM 4247 O OG . SER B 1 166 ? 12.504 13.212 66.336 1.00 18.12 ? 246 SER B OG 1 ATOM 4248 N N . ASN B 1 167 ? 12.583 13.998 69.858 1.00 11.96 ? 247 ASN B N 1 ATOM 4249 C CA . ASN B 1 167 ? 12.098 13.276 71.029 1.00 14.31 ? 247 ASN B CA 1 ATOM 4250 C C . ASN B 1 167 ? 12.658 13.848 72.328 1.00 17.71 ? 247 ASN B C 1 ATOM 4251 O O . ASN B 1 167 ? 12.780 13.142 73.329 1.00 18.04 ? 247 ASN B O 1 ATOM 4252 C CB . ASN B 1 167 ? 12.449 11.791 70.926 1.00 16.79 ? 247 ASN B CB 1 ATOM 4253 C CG . ASN B 1 167 ? 13.945 11.542 70.976 1.00 18.93 ? 247 ASN B CG 1 ATOM 4254 O OD1 . ASN B 1 167 ? 14.745 12.462 70.808 1.00 14.83 ? 247 ASN B OD1 1 ATOM 4255 N ND2 . ASN B 1 167 ? 14.330 10.293 71.208 1.00 25.15 ? 247 ASN B ND2 1 ATOM 4256 N N . GLY B 1 168 ? 13.005 15.129 72.301 1.00 12.84 ? 248 GLY B N 1 ATOM 4257 C CA . GLY B 1 168 ? 13.549 15.797 73.467 1.00 14.11 ? 248 GLY B CA 1 ATOM 4258 C C . GLY B 1 168 ? 13.719 17.279 73.209 1.00 12.15 ? 248 GLY B C 1 ATOM 4259 O O . GLY B 1 168 ? 13.298 17.786 72.169 1.00 10.50 ? 248 GLY B O 1 ATOM 4260 N N . GLN B 1 169 ? 14.336 17.978 74.155 1.00 10.07 ? 249 GLN B N 1 ATOM 4261 C CA . GLN B 1 169 ? 14.573 19.408 74.008 1.00 11.33 ? 249 GLN B CA 1 ATOM 4262 C C . GLN B 1 169 ? 15.345 19.706 72.726 1.00 12.29 ? 249 GLN B C 1 ATOM 4263 O O . GLN B 1 169 ? 16.380 19.099 72.462 1.00 7.97 ? 249 GLN B O 1 ATOM 4264 C CB . GLN B 1 169 ? 15.348 19.947 75.209 1.00 11.04 ? 249 GLN B CB 1 ATOM 4265 C CG . GLN B 1 169 ? 15.571 21.446 75.166 1.00 10.94 ? 249 GLN B CG 1 ATOM 4266 C CD . GLN B 1 169 ? 14.303 22.225 75.447 1.00 11.49 ? 249 GLN B CD 1 ATOM 4267 O OE1 . GLN B 1 169 ? 13.711 22.100 76.519 1.00 8.91 ? 249 GLN B OE1 1 ATOM 4268 N NE2 . GLN B 1 169 ? 13.878 23.036 74.485 1.00 8.76 ? 249 GLN B NE2 1 ATOM 4269 N N . ALA B 1 170 ? 14.838 20.645 71.934 1.00 9.37 ? 250 ALA B N 1 ATOM 4270 C CA . ALA B 1 170 ? 15.521 21.064 70.717 1.00 7.38 ? 250 ALA B CA 1 ATOM 4271 C C . ALA B 1 170 ? 15.726 22.575 70.713 1.00 9.05 ? 250 ALA B C 1 ATOM 4272 O O . ALA B 1 170 ? 15.535 23.237 71.733 1.00 6.62 ? 250 ALA B O 1 ATOM 4273 C CB . ALA B 1 170 ? 14.742 20.619 69.484 1.00 8.77 ? 250 ALA B CB 1 ATOM 4274 N N . SER B 1 171 ? 16.125 23.112 69.565 1.00 5.08 ? 251 SER B N 1 ATOM 4275 C CA . SER B 1 171 ? 16.359 24.544 69.426 1.00 7.38 ? 251 SER B CA 1 ATOM 4276 C C . SER B 1 171 ? 15.421 25.136 68.379 1.00 6.90 ? 251 SER B C 1 ATOM 4277 O O . SER B 1 171 ? 15.269 24.587 67.289 1.00 5.28 ? 251 SER B O 1 ATOM 4278 C CB . SER B 1 171 ? 17.818 24.815 69.048 1.00 8.97 ? 251 SER B CB 1 ATOM 4279 O OG . SER B 1 171 ? 18.050 26.201 68.868 1.00 14.21 ? 251 SER B OG 1 ATOM 4280 N N . TYR B 1 172 ? 14.794 26.258 68.716 1.00 7.16 ? 252 TYR B N 1 ATOM 4281 C CA . TYR B 1 172 ? 13.784 26.858 67.852 1.00 7.79 ? 252 TYR B CA 1 ATOM 4282 C C . TYR B 1 172 ? 14.129 28.316 67.573 1.00 8.09 ? 252 TYR B C 1 ATOM 4283 O O . TYR B 1 172 ? 14.415 29.079 68.495 1.00 7.41 ? 252 TYR B O 1 ATOM 4284 C CB . TYR B 1 172 ? 12.403 26.736 68.506 1.00 6.84 ? 252 TYR B CB 1 ATOM 4285 C CG . TYR B 1 172 ? 12.295 25.518 69.395 1.00 7.56 ? 252 TYR B CG 1 ATOM 4286 C CD1 . TYR B 1 172 ? 12.193 24.246 68.849 1.00 5.00 ? 252 TYR B CD1 1 ATOM 4287 C CD2 . TYR B 1 172 ? 12.321 25.637 70.779 1.00 10.88 ? 252 TYR B CD2 1 ATOM 4288 C CE1 . TYR B 1 172 ? 12.112 23.128 69.653 1.00 6.18 ? 252 TYR B CE1 1 ATOM 4289 C CE2 . TYR B 1 172 ? 12.237 24.521 71.593 1.00 6.04 ? 252 TYR B CE2 1 ATOM 4290 C CZ . TYR B 1 172 ? 12.134 23.269 71.023 1.00 7.48 ? 252 TYR B CZ 1 ATOM 4291 O OH . TYR B 1 172 ? 12.058 22.151 71.823 1.00 7.25 ? 252 TYR B OH 1 ATOM 4292 N N . LYS B 1 173 ? 14.115 28.696 66.297 1.00 4.60 ? 253 LYS B N 1 ATOM 4293 C CA . LYS B 1 173 ? 14.454 30.060 65.903 1.00 4.36 ? 253 LYS B CA 1 ATOM 4294 C C . LYS B 1 173 ? 13.381 30.705 65.032 1.00 6.33 ? 253 LYS B C 1 ATOM 4295 O O . LYS B 1 173 ? 12.793 30.054 64.169 1.00 4.04 ? 253 LYS B O 1 ATOM 4296 C CB . LYS B 1 173 ? 15.793 30.094 65.162 1.00 6.06 ? 253 LYS B CB 1 ATOM 4297 C CG . LYS B 1 173 ? 17.011 29.877 66.046 1.00 9.83 ? 253 LYS B CG 1 ATOM 4298 C CD . LYS B 1 173 ? 18.291 30.066 65.248 1.00 8.51 ? 253 LYS B CD 1 ATOM 4299 C CE . LYS B 1 173 ? 19.523 29.905 66.124 1.00 14.73 ? 253 LYS B CE 1 ATOM 4300 N NZ . LYS B 1 173 ? 20.768 30.174 65.353 1.00 18.65 ? 253 LYS B NZ 1 ATOM 4301 N N . ILE B 1 174 ? 13.141 31.991 65.264 1.00 6.70 ? 254 ILE B N 1 ATOM 4302 C CA . ILE B 1 174 ? 12.222 32.764 64.442 1.00 7.76 ? 254 ILE B CA 1 ATOM 4303 C C . ILE B 1 174 ? 13.033 33.620 63.482 1.00 8.88 ? 254 ILE B C 1 ATOM 4304 O O . ILE B 1 174 ? 14.073 34.164 63.854 1.00 6.42 ? 254 ILE B O 1 ATOM 4305 C CB . ILE B 1 174 ? 11.344 33.690 65.296 1.00 8.07 ? 254 ILE B CB 1 ATOM 4306 C CG1 . ILE B 1 174 ? 10.715 32.917 66.455 1.00 8.95 ? 254 ILE B CG1 1 ATOM 4307 C CG2 . ILE B 1 174 ? 10.271 34.341 64.439 1.00 7.36 ? 254 ILE B CG2 1 ATOM 4308 C CD1 . ILE B 1 174 ? 10.028 33.811 67.474 1.00 13.53 ? 254 ILE B CD1 1 ATOM 4309 N N . PHE B 1 175 ? 12.561 33.737 62.246 1.00 8.32 ? 255 PHE B N 1 ATOM 4310 C CA . PHE B 1 175 ? 13.278 34.507 61.238 1.00 7.92 ? 255 PHE B CA 1 ATOM 4311 C C . PHE B 1 175 ? 12.421 35.613 60.639 1.00 11.30 ? 255 PHE B C 1 ATOM 4312 O O . PHE B 1 175 ? 11.233 35.419 60.376 1.00 11.38 ? 255 PHE B O 1 ATOM 4313 C CB . PHE B 1 175 ? 13.773 33.588 60.121 1.00 10.92 ? 255 PHE B CB 1 ATOM 4314 C CG . PHE B 1 175 ? 14.780 32.572 60.570 1.00 9.82 ? 255 PHE B CG 1 ATOM 4315 C CD1 . PHE B 1 175 ? 16.135 32.838 60.482 1.00 10.37 ? 255 PHE B CD1 1 ATOM 4316 C CD2 . PHE B 1 175 ? 14.372 31.347 61.074 1.00 10.92 ? 255 PHE B CD2 1 ATOM 4317 C CE1 . PHE B 1 175 ? 17.067 31.902 60.887 1.00 15.59 ? 255 PHE B CE1 1 ATOM 4318 C CE2 . PHE B 1 175 ? 15.298 30.408 61.483 1.00 9.32 ? 255 PHE B CE2 1 ATOM 4319 C CZ . PHE B 1 175 ? 16.648 30.684 61.389 1.00 12.97 ? 255 PHE B CZ 1 ATOM 4320 N N . ARG B 1 176 ? 13.030 36.777 60.433 1.00 8.74 ? 256 ARG B N 1 ATOM 4321 C CA . ARG B 1 176 ? 12.403 37.843 59.664 1.00 5.85 ? 256 ARG B CA 1 ATOM 4322 C C . ARG B 1 176 ? 13.126 37.972 58.330 1.00 9.59 ? 256 ARG B C 1 ATOM 4323 O O . ARG B 1 176 ? 14.348 38.133 58.280 1.00 5.61 ? 256 ARG B O 1 ATOM 4324 C CB . ARG B 1 176 ? 12.448 39.167 60.423 1.00 9.28 ? 256 ARG B CB 1 ATOM 4325 C CG . ARG B 1 176 ? 11.899 40.345 59.638 1.00 10.22 ? 256 ARG B CG 1 ATOM 4326 C CD . ARG B 1 176 ? 11.914 41.611 60.480 1.00 13.88 ? 256 ARG B CD 1 ATOM 4327 N NE . ARG B 1 176 ? 11.683 42.792 59.656 1.00 18.51 ? 256 ARG B NE 1 ATOM 4328 C CZ . ARG B 1 176 ? 11.401 43.999 60.137 1.00 20.65 ? 256 ARG B CZ 1 ATOM 4329 N NH1 . ARG B 1 176 ? 11.302 44.197 61.448 1.00 21.72 ? 256 ARG B NH1 1 ATOM 4330 N NH2 . ARG B 1 176 ? 11.212 45.013 59.304 1.00 20.37 ? 256 ARG B NH2 1 ATOM 4331 N N . ILE B 1 177 ? 12.360 37.898 57.250 1.00 8.25 ? 257 ILE B N 1 ATOM 4332 C CA . ILE B 1 177 ? 12.932 37.866 55.913 1.00 5.86 ? 257 ILE B CA 1 ATOM 4333 C C . ILE B 1 177 ? 12.346 38.972 55.045 1.00 8.92 ? 257 ILE B C 1 ATOM 4334 O O . ILE B 1 177 ? 11.129 39.147 54.989 1.00 8.92 ? 257 ILE B O 1 ATOM 4335 C CB . ILE B 1 177 ? 12.681 36.497 55.258 1.00 5.77 ? 257 ILE B CB 1 ATOM 4336 C CG1 . ILE B 1 177 ? 13.284 35.386 56.125 1.00 9.81 ? 257 ILE B CG1 1 ATOM 4337 C CG2 . ILE B 1 177 ? 13.260 36.462 53.848 1.00 6.25 ? 257 ILE B CG2 1 ATOM 4338 C CD1 . ILE B 1 177 ? 12.731 34.009 55.841 1.00 6.51 ? 257 ILE B CD1 1 ATOM 4339 N N . GLU B 1 178 ? 13.217 39.721 54.376 1.00 6.92 ? 258 GLU B N 1 ATOM 4340 C CA . GLU B 1 178 ? 12.782 40.783 53.478 1.00 7.09 ? 258 GLU B CA 1 ATOM 4341 C C . GLU B 1 178 ? 13.397 40.596 52.096 1.00 7.15 ? 258 GLU B C 1 ATOM 4342 O O . GLU B 1 178 ? 14.619 40.572 51.948 1.00 6.56 ? 258 GLU B O 1 ATOM 4343 C CB . GLU B 1 178 ? 13.146 42.157 54.048 1.00 10.14 ? 258 GLU B CB 1 ATOM 4344 C CG . GLU B 1 178 ? 12.548 42.425 55.424 1.00 17.03 ? 258 GLU B CG 1 ATOM 4345 C CD . GLU B 1 178 ? 12.950 43.773 55.993 1.00 24.64 ? 258 GLU B CD 1 ATOM 4346 O OE1 . GLU B 1 178 ? 13.443 44.625 55.225 1.00 30.05 ? 258 GLU B OE1 1 ATOM 4347 O OE2 . GLU B 1 178 ? 12.768 43.981 57.211 1.00 23.32 ? 258 GLU B OE2 1 ATOM 4348 N N . LYS B 1 179 ? 12.540 40.454 51.091 1.00 9.05 ? 259 LYS B N 1 ATOM 4349 C CA . LYS B 1 179 ? 12.983 40.176 49.727 1.00 8.34 ? 259 LYS B CA 1 ATOM 4350 C C . LYS B 1 179 ? 13.955 38.998 49.677 1.00 8.22 ? 259 LYS B C 1 ATOM 4351 O O . LYS B 1 179 ? 14.953 39.022 48.953 1.00 7.37 ? 259 LYS B O 1 ATOM 4352 C CB . LYS B 1 179 ? 13.597 41.423 49.088 1.00 12.54 ? 259 LYS B CB 1 ATOM 4353 C CG . LYS B 1 179 ? 12.603 42.571 48.937 1.00 15.49 ? 259 LYS B CG 1 ATOM 4354 C CD . LYS B 1 179 ? 13.225 43.769 48.245 1.00 25.25 ? 259 LYS B CD 1 ATOM 4355 C CE . LYS B 1 179 ? 12.213 44.900 48.082 1.00 34.09 ? 259 LYS B CE 1 ATOM 4356 N NZ . LYS B 1 179 ? 11.095 44.580 47.137 1.00 41.98 ? 259 LYS B NZ 1 ATOM 4357 N N . GLY B 1 180 ? 13.653 37.965 50.456 1.00 6.58 ? 260 GLY B N 1 ATOM 4358 C CA . GLY B 1 180 ? 14.428 36.739 50.429 1.00 7.20 ? 260 GLY B CA 1 ATOM 4359 C C . GLY B 1 180 ? 15.706 36.781 51.243 1.00 6.62 ? 260 GLY B C 1 ATOM 4360 O O . GLY B 1 180 ? 16.468 35.815 51.248 1.00 8.14 ? 260 GLY B O 1 ATOM 4361 N N . LYS B 1 181 ? 15.942 37.894 51.932 1.00 6.80 ? 261 LYS B N 1 ATOM 4362 C CA . LYS B 1 181 ? 17.142 38.056 52.751 1.00 7.74 ? 261 LYS B CA 1 ATOM 4363 C C . LYS B 1 181 ? 16.797 38.018 54.233 1.00 6.44 ? 261 LYS B C 1 ATOM 4364 O O . LYS B 1 181 ? 15.912 38.739 54.683 1.00 7.68 ? 261 LYS B O 1 ATOM 4365 C CB . LYS B 1 181 ? 17.819 39.390 52.437 1.00 11.79 ? 261 LYS B CB 1 ATOM 4366 C CG . LYS B 1 181 ? 18.278 39.541 51.000 1.00 18.70 ? 261 LYS B CG 1 ATOM 4367 C CD . LYS B 1 181 ? 19.522 38.712 50.736 1.00 20.00 ? 261 LYS B CD 1 ATOM 4368 C CE . LYS B 1 181 ? 20.064 38.974 49.343 1.00 24.73 ? 261 LYS B CE 1 ATOM 4369 N NZ . LYS B 1 181 ? 21.341 38.250 49.095 1.00 27.64 ? 261 LYS B NZ 1 ATOM 4370 N N . ILE B 1 182 ? 17.498 37.187 54.995 1.00 7.06 ? 262 ILE B N 1 ATOM 4371 C CA . ILE B 1 182 ? 17.297 37.158 56.439 1.00 7.89 ? 262 ILE B CA 1 ATOM 4372 C C . ILE B 1 182 ? 17.848 38.441 57.048 1.00 14.09 ? 262 ILE B C 1 ATOM 4373 O O . ILE B 1 182 ? 19.044 38.714 56.953 1.00 11.91 ? 262 ILE B O 1 ATOM 4374 C CB . ILE B 1 182 ? 17.986 35.943 57.078 1.00 10.05 ? 262 ILE B CB 1 ATOM 4375 C CG1 . ILE B 1 182 ? 17.423 34.648 56.486 1.00 12.39 ? 262 ILE B CG1 1 ATOM 4376 C CG2 . ILE B 1 182 ? 17.808 35.966 58.590 1.00 9.29 ? 262 ILE B CG2 1 ATOM 4377 C CD1 . ILE B 1 182 ? 18.187 33.407 56.887 1.00 17.19 ? 262 ILE B CD1 1 ATOM 4378 N N . VAL B 1 183 ? 16.976 39.239 57.659 1.00 6.62 ? 263 VAL B N 1 ATOM 4379 C CA . VAL B 1 183 ? 17.402 40.510 58.237 1.00 6.45 ? 263 VAL B CA 1 ATOM 4380 C C . VAL B 1 183 ? 17.482 40.448 59.757 1.00 14.17 ? 263 VAL B C 1 ATOM 4381 O O . VAL B 1 183 ? 18.098 41.306 60.387 1.00 9.00 ? 263 VAL B O 1 ATOM 4382 C CB . VAL B 1 183 ? 16.490 41.679 57.807 1.00 12.12 ? 263 VAL B CB 1 ATOM 4383 C CG1 . VAL B 1 183 ? 16.618 41.929 56.309 1.00 15.42 ? 263 VAL B CG1 1 ATOM 4384 C CG2 . VAL B 1 183 ? 15.044 41.400 58.188 1.00 13.41 ? 263 VAL B CG2 1 ATOM 4385 N N . LYS B 1 184 ? 16.860 39.428 60.339 1.00 8.28 ? 264 LYS B N 1 ATOM 4386 C CA . LYS B 1 184 ? 16.911 39.233 61.780 1.00 10.86 ? 264 LYS B CA 1 ATOM 4387 C C . LYS B 1 184 ? 16.424 37.843 62.161 1.00 10.14 ? 264 LYS B C 1 ATOM 4388 O O . LYS B 1 184 ? 15.550 37.274 61.505 1.00 8.31 ? 264 LYS B O 1 ATOM 4389 C CB . LYS B 1 184 ? 16.082 40.297 62.505 1.00 10.40 ? 264 LYS B CB 1 ATOM 4390 C CG . LYS B 1 184 ? 16.279 40.302 64.017 1.00 13.40 ? 264 LYS B CG 1 ATOM 4391 C CD . LYS B 1 184 ? 15.451 41.383 64.697 1.00 12.85 ? 264 LYS B CD 1 ATOM 4392 C CE . LYS B 1 184 ? 15.757 41.444 66.189 1.00 15.27 ? 264 LYS B CE 1 ATOM 4393 N NZ . LYS B 1 184 ? 14.947 42.477 66.894 1.00 18.58 ? 264 LYS B NZ 1 ATOM 4394 N N . SER B 1 185 ? 17.007 37.299 63.222 1.00 5.95 ? 265 SER B N 1 ATOM 4395 C CA . SER B 1 185 ? 16.559 36.035 63.780 1.00 10.11 ? 265 SER B CA 1 ATOM 4396 C C . SER B 1 185 ? 16.781 36.053 65.283 1.00 9.56 ? 265 SER B C 1 ATOM 4397 O O . SER B 1 185 ? 17.590 36.829 65.790 1.00 10.22 ? 265 SER B O 1 ATOM 4398 C CB . SER B 1 185 ? 17.309 34.859 63.149 1.00 9.94 ? 265 SER B CB 1 ATOM 4399 O OG . SER B 1 185 ? 18.682 34.887 63.486 1.00 12.60 ? 265 SER B OG 1 ATOM 4400 N N . VAL B 1 186 ? 16.051 35.207 65.994 1.00 7.74 ? 266 VAL B N 1 ATOM 4401 C CA . VAL B 1 186 ? 16.226 35.091 67.433 1.00 10.82 ? 266 VAL B CA 1 ATOM 4402 C C . VAL B 1 186 ? 15.883 33.676 67.866 1.00 13.15 ? 266 VAL B C 1 ATOM 4403 O O . VAL B 1 186 ? 14.921 33.087 67.373 1.00 9.88 ? 266 VAL B O 1 ATOM 4404 C CB . VAL B 1 186 ? 15.346 36.103 68.195 1.00 11.83 ? 266 VAL B CB 1 ATOM 4405 C CG1 . VAL B 1 186 ? 13.876 35.891 67.865 1.00 13.67 ? 266 VAL B CG1 1 ATOM 4406 C CG2 . VAL B 1 186 ? 15.582 35.994 69.698 1.00 13.32 ? 266 VAL B CG2 1 ATOM 4407 N N . GLU B 1 187 ? 16.680 33.118 68.769 1.00 11.01 ? 267 GLU B N 1 ATOM 4408 C CA . GLU B 1 187 ? 16.363 31.801 69.297 1.00 10.17 ? 267 GLU B CA 1 ATOM 4409 C C . GLU B 1 187 ? 15.376 31.916 70.448 1.00 11.10 ? 267 GLU B C 1 ATOM 4410 O O . GLU B 1 187 ? 15.578 32.694 71.378 1.00 11.29 ? 267 GLU B O 1 ATOM 4411 C CB . GLU B 1 187 ? 17.613 31.043 69.747 1.00 10.58 ? 267 GLU B CB 1 ATOM 4412 C CG . GLU B 1 187 ? 17.273 29.707 70.396 1.00 12.46 ? 267 GLU B CG 1 ATOM 4413 C CD . GLU B 1 187 ? 18.482 28.834 70.660 1.00 18.88 ? 267 GLU B CD 1 ATOM 4414 O OE1 . GLU B 1 187 ? 19.622 29.302 70.459 1.00 21.74 ? 267 GLU B OE1 1 ATOM 4415 O OE2 . GLU B 1 187 ? 18.285 27.670 71.069 1.00 15.22 ? 267 GLU B OE2 1 ATOM 4416 N N . MET B 1 188 ? 14.302 31.142 70.374 1.00 8.49 ? 268 MET B N 1 ATOM 4417 C CA . MET B 1 188 ? 13.305 31.131 71.431 1.00 6.48 ? 268 MET B CA 1 ATOM 4418 C C . MET B 1 188 ? 13.862 30.497 72.701 1.00 7.96 ? 268 MET B C 1 ATOM 4419 O O . MET B 1 188 ? 14.447 29.415 72.665 1.00 10.92 ? 268 MET B O 1 ATOM 4420 C CB . MET B 1 188 ? 12.053 30.391 70.963 1.00 9.24 ? 268 MET B CB 1 ATOM 4421 C CG . MET B 1 188 ? 11.284 31.141 69.890 1.00 8.18 ? 268 MET B CG 1 ATOM 4422 S SD . MET B 1 188 ? 10.305 30.068 68.829 1.00 12.54 ? 268 MET B SD 1 ATOM 4423 C CE . MET B 1 188 ? 9.270 29.238 70.031 1.00 7.56 ? 268 MET B CE 1 ATOM 4424 N N . ASN B 1 189 ? 13.693 31.193 73.819 1.00 10.01 ? 269 ASN B N 1 ATOM 4425 C CA . ASN B 1 189 ? 14.050 30.659 75.126 1.00 7.90 ? 269 ASN B CA 1 ATOM 4426 C C . ASN B 1 189 ? 12.871 29.840 75.639 1.00 8.19 ? 269 ASN B C 1 ATOM 4427 O O . ASN B 1 189 ? 11.995 30.361 76.329 1.00 8.64 ? 269 ASN B O 1 ATOM 4428 C CB . ASN B 1 189 ? 14.375 31.807 76.086 1.00 5.98 ? 269 ASN B CB 1 ATOM 4429 C CG . ASN B 1 189 ? 14.813 31.325 77.463 1.00 11.27 ? 269 ASN B CG 1 ATOM 4430 O OD1 . ASN B 1 189 ? 15.608 30.393 77.587 1.00 9.04 ? 269 ASN B OD1 1 ATOM 4431 N ND2 . ASN B 1 189 ? 14.303 31.973 78.503 1.00 8.36 ? 269 ASN B ND2 1 ATOM 4432 N N . ALA B 1 190 ? 12.839 28.560 75.281 1.00 7.48 ? 270 ALA B N 1 ATOM 4433 C CA . ALA B 1 190 ? 11.680 27.720 75.570 1.00 6.33 ? 270 ALA B CA 1 ATOM 4434 C C . ALA B 1 190 ? 12.057 26.360 76.153 1.00 8.43 ? 270 ALA B C 1 ATOM 4435 O O . ALA B 1 190 ? 11.832 25.326 75.523 1.00 6.55 ? 270 ALA B O 1 ATOM 4436 C CB . ALA B 1 190 ? 10.836 27.539 74.308 1.00 9.62 ? 270 ALA B CB 1 ATOM 4437 N N . PRO B 1 191 ? 12.641 26.357 77.362 1.00 11.22 ? 271 PRO B N 1 ATOM 4438 C CA . PRO B 1 191 ? 12.937 25.087 78.032 1.00 10.76 ? 271 PRO B CA 1 ATOM 4439 C C . PRO B 1 191 ? 11.656 24.319 78.350 1.00 9.70 ? 271 PRO B C 1 ATOM 4440 O O . PRO B 1 191 ? 10.680 24.912 78.811 1.00 10.92 ? 271 PRO B O 1 ATOM 4441 C CB . PRO B 1 191 ? 13.636 25.517 79.330 1.00 13.70 ? 271 PRO B CB 1 ATOM 4442 C CG . PRO B 1 191 ? 13.333 26.973 79.491 1.00 16.91 ? 271 PRO B CG 1 ATOM 4443 C CD . PRO B 1 191 ? 13.143 27.520 78.114 1.00 11.53 ? 271 PRO B CD 1 ATOM 4444 N N . ASN B 1 192 ? 11.675 23.014 78.097 1.00 9.99 ? 272 ASN B N 1 ATOM 4445 C CA . ASN B 1 192 ? 10.530 22.135 78.327 1.00 10.31 ? 272 ASN B CA 1 ATOM 4446 C C . ASN B 1 192 ? 9.434 22.255 77.267 1.00 11.70 ? 272 ASN B C 1 ATOM 4447 O O . ASN B 1 192 ? 8.414 21.570 77.340 1.00 15.80 ? 272 ASN B O 1 ATOM 4448 C CB . ASN B 1 192 ? 9.942 22.335 79.728 1.00 14.17 ? 272 ASN B CB 1 ATOM 4449 C CG . ASN B 1 192 ? 9.278 21.082 80.261 1.00 19.61 ? 272 ASN B CG 1 ATOM 4450 O OD1 . ASN B 1 192 ? 9.863 19.998 80.229 1.00 19.17 ? 272 ASN B OD1 1 ATOM 4451 N ND2 . ASN B 1 192 ? 8.053 21.221 80.755 1.00 24.29 ? 272 ASN B ND2 1 ATOM 4452 N N . TYR B 1 193 ? 9.648 23.135 76.293 1.00 12.52 ? 273 TYR B N 1 ATOM 4453 C CA . TYR B 1 193 ? 8.754 23.268 75.147 1.00 9.51 ? 273 TYR B CA 1 ATOM 4454 C C . TYR B 1 193 ? 9.322 22.487 73.969 1.00 10.42 ? 273 TYR B C 1 ATOM 4455 O O . TYR B 1 193 ? 10.527 22.250 73.900 1.00 8.61 ? 273 TYR B O 1 ATOM 4456 C CB . TYR B 1 193 ? 8.633 24.735 74.726 1.00 10.01 ? 273 TYR B CB 1 ATOM 4457 C CG . TYR B 1 193 ? 7.747 25.603 75.591 1.00 13.05 ? 273 TYR B CG 1 ATOM 4458 C CD1 . TYR B 1 193 ? 8.104 25.919 76.894 1.00 16.62 ? 273 TYR B CD1 1 ATOM 4459 C CD2 . TYR B 1 193 ? 6.571 26.144 75.086 1.00 13.92 ? 273 TYR B CD2 1 ATOM 4460 C CE1 . TYR B 1 193 ? 7.301 26.727 77.679 1.00 21.09 ? 273 TYR B CE1 1 ATOM 4461 C CE2 . TYR B 1 193 ? 5.764 26.952 75.862 1.00 14.12 ? 273 TYR B CE2 1 ATOM 4462 C CZ . TYR B 1 193 ? 6.133 27.240 77.157 1.00 17.48 ? 273 TYR B CZ 1 ATOM 4463 O OH . TYR B 1 193 ? 5.332 28.045 77.933 1.00 20.82 ? 273 TYR B OH 1 ATOM 4464 N N . HIS B 1 194 ? 8.456 22.103 73.035 1.00 7.07 ? 274 HIS B N 1 ATOM 4465 C CA . HIS B 1 194 ? 8.902 21.498 71.782 1.00 6.42 ? 274 HIS B CA 1 ATOM 4466 C C . HIS B 1 194 ? 8.076 22.041 70.620 1.00 6.31 ? 274 HIS B C 1 ATOM 4467 O O . HIS B 1 194 ? 6.845 21.984 70.646 1.00 5.65 ? 274 HIS B O 1 ATOM 4468 C CB . HIS B 1 194 ? 8.798 19.970 71.843 1.00 5.62 ? 274 HIS B CB 1 ATOM 4469 C CG . HIS B 1 194 ? 9.637 19.266 70.822 1.00 9.32 ? 274 HIS B CG 1 ATOM 4470 N ND1 . HIS B 1 194 ? 9.102 18.654 69.709 1.00 9.05 ? 274 HIS B ND1 1 ATOM 4471 C CD2 . HIS B 1 194 ? 10.977 19.084 70.743 1.00 8.02 ? 274 HIS B CD2 1 ATOM 4472 C CE1 . HIS B 1 194 ? 10.075 18.123 68.990 1.00 10.65 ? 274 HIS B CE1 1 ATOM 4473 N NE2 . HIS B 1 194 ? 11.223 18.370 69.596 1.00 10.06 ? 274 HIS B NE2 1 ATOM 4474 N N . TYR B 1 195 ? 8.758 22.571 69.608 1.00 6.74 ? 275 TYR B N 1 ATOM 4475 C CA . TYR B 1 195 ? 8.093 23.154 68.444 1.00 6.63 ? 275 TYR B CA 1 ATOM 4476 C C . TYR B 1 195 ? 8.520 22.475 67.151 1.00 7.11 ? 275 TYR B C 1 ATOM 4477 O O . TYR B 1 195 ? 9.710 22.420 66.837 1.00 6.19 ? 275 TYR B O 1 ATOM 4478 C CB . TYR B 1 195 ? 8.414 24.646 68.323 1.00 4.08 ? 275 TYR B CB 1 ATOM 4479 C CG . TYR B 1 195 ? 7.792 25.525 69.383 1.00 8.47 ? 275 TYR B CG 1 ATOM 4480 C CD1 . TYR B 1 195 ? 8.405 25.694 70.618 1.00 8.03 ? 275 TYR B CD1 1 ATOM 4481 C CD2 . TYR B 1 195 ? 6.604 26.199 69.143 1.00 4.59 ? 275 TYR B CD2 1 ATOM 4482 C CE1 . TYR B 1 195 ? 7.843 26.502 71.590 1.00 8.21 ? 275 TYR B CE1 1 ATOM 4483 C CE2 . TYR B 1 195 ? 6.034 27.010 70.108 1.00 5.84 ? 275 TYR B CE2 1 ATOM 4484 C CZ . TYR B 1 195 ? 6.659 27.156 71.330 1.00 10.84 ? 275 TYR B CZ 1 ATOM 4485 O OH . TYR B 1 195 ? 6.100 27.962 72.293 1.00 9.60 ? 275 TYR B OH 1 ATOM 4486 N N . GLU B 1 196 ? 7.543 21.981 66.398 1.00 7.25 ? 276 GLU B N 1 ATOM 4487 C CA . GLU B 1 196 ? 7.793 21.460 65.059 1.00 8.20 ? 276 GLU B CA 1 ATOM 4488 C C . GLU B 1 196 ? 6.648 21.830 64.122 1.00 7.85 ? 276 GLU B C 1 ATOM 4489 O O . GLU B 1 196 ? 5.510 22.007 64.559 1.00 5.67 ? 276 GLU B O 1 ATOM 4490 C CB . GLU B 1 196 ? 7.959 19.939 65.090 1.00 13.19 ? 276 GLU B CB 1 ATOM 4491 C CG . GLU B 1 196 ? 9.167 19.469 65.877 1.00 18.07 ? 276 GLU B CG 1 ATOM 4492 C CD . GLU B 1 196 ? 9.497 18.017 65.624 1.00 22.84 ? 276 GLU B CD 1 ATOM 4493 O OE1 . GLU B 1 196 ? 8.612 17.275 65.147 1.00 29.14 ? 276 GLU B OE1 1 ATOM 4494 O OE2 . GLU B 1 196 ? 10.643 17.614 65.906 1.00 16.51 ? 276 GLU B OE2 1 ATOM 4495 N N . GLU B 1 197 ? 6.959 21.950 62.835 1.00 5.70 ? 277 GLU B N 1 ATOM 4496 C CA . GLU B 1 197 ? 5.935 22.093 61.798 1.00 7.12 ? 277 GLU B CA 1 ATOM 4497 C C . GLU B 1 197 ? 4.879 23.153 62.118 1.00 6.60 ? 277 GLU B C 1 ATOM 4498 O O . GLU B 1 197 ? 3.678 22.887 62.053 1.00 8.44 ? 277 GLU B O 1 ATOM 4499 C CB . GLU B 1 197 ? 5.272 20.735 61.545 1.00 6.55 ? 277 GLU B CB 1 ATOM 4500 C CG . GLU B 1 197 ? 6.269 19.653 61.147 1.00 11.54 ? 277 GLU B CG 1 ATOM 4501 C CD . GLU B 1 197 ? 5.647 18.276 61.023 1.00 15.68 ? 277 GLU B CD 1 ATOM 4502 O OE1 . GLU B 1 197 ? 4.594 18.026 61.647 1.00 10.53 ? 277 GLU B OE1 1 ATOM 4503 O OE2 . GLU B 1 197 ? 6.223 17.437 60.301 1.00 12.32 ? 277 GLU B OE2 1 ATOM 4504 N N . CYS B 1 198 ? 5.332 24.358 62.449 1.00 6.69 ? 278 CYS B N 1 ATOM 4505 C CA . CYS B 1 198 ? 4.429 25.438 62.843 1.00 7.02 ? 278 CYS B CA 1 ATOM 4506 C C . CYS B 1 198 ? 3.508 25.909 61.725 1.00 7.59 ? 278 CYS B C 1 ATOM 4507 O O . CYS B 1 198 ? 3.930 26.060 60.577 1.00 6.96 ? 278 CYS B O 1 ATOM 4508 C CB . CYS B 1 198 ? 5.226 26.635 63.359 1.00 10.44 ? 278 CYS B CB 1 ATOM 4509 S SG . CYS B 1 198 ? 6.050 26.347 64.923 1.00 12.84 ? 278 CYS B SG 1 ATOM 4510 N N . SER B 1 199 ? 2.249 26.147 62.078 1.00 10.51 ? 279 SER B N 1 ATOM 4511 C CA . SER B 1 199 ? 1.305 26.806 61.186 1.00 8.32 ? 279 SER B CA 1 ATOM 4512 C C . SER B 1 199 ? 1.166 28.255 61.642 1.00 9.10 ? 279 SER B C 1 ATOM 4513 O O . SER B 1 199 ? 0.622 28.521 62.713 1.00 10.52 ? 279 SER B O 1 ATOM 4514 C CB . SER B 1 199 ? -0.053 26.102 61.224 1.00 10.36 ? 279 SER B CB 1 ATOM 4515 O OG . SER B 1 199 ? 0.033 24.792 60.689 1.00 11.87 ? 279 SER B OG 1 ATOM 4516 N N . CYS B 1 200 ? 1.674 29.183 60.834 1.00 7.64 ? 280 CYS B N 1 ATOM 4517 C CA . CYS B 1 200 ? 1.723 30.596 61.204 1.00 6.20 ? 280 CYS B CA 1 ATOM 4518 C C . CYS B 1 200 ? 0.830 31.455 60.315 1.00 8.42 ? 280 CYS B C 1 ATOM 4519 O O . CYS B 1 200 ? 0.711 31.211 59.114 1.00 8.71 ? 280 CYS B O 1 ATOM 4520 C CB . CYS B 1 200 ? 3.159 31.119 61.108 1.00 7.66 ? 280 CYS B CB 1 ATOM 4521 S SG . CYS B 1 200 ? 4.380 30.199 62.078 1.00 11.58 ? 280 CYS B SG 1 ATOM 4522 N N . TYR B 1 201 ? 0.218 32.473 60.910 1.00 4.31 ? 281 TYR B N 1 ATOM 4523 C CA . TYR B 1 201 ? -0.621 33.404 60.163 1.00 7.75 ? 281 TYR B CA 1 ATOM 4524 C C . TYR B 1 201 ? -0.503 34.804 60.754 1.00 7.58 ? 281 TYR B C 1 ATOM 4525 O O . TYR B 1 201 ? -0.179 34.953 61.936 1.00 5.26 ? 281 TYR B O 1 ATOM 4526 C CB . TYR B 1 201 ? -2.083 32.949 60.184 1.00 6.75 ? 281 TYR B CB 1 ATOM 4527 C CG . TYR B 1 201 ? -2.699 32.959 61.564 1.00 7.67 ? 281 TYR B CG 1 ATOM 4528 C CD1 . TYR B 1 201 ? -2.739 31.807 62.332 1.00 6.99 ? 281 TYR B CD1 1 ATOM 4529 C CD2 . TYR B 1 201 ? -3.235 34.122 62.100 1.00 4.49 ? 281 TYR B CD2 1 ATOM 4530 C CE1 . TYR B 1 201 ? -3.293 31.810 63.598 1.00 7.91 ? 281 TYR B CE1 1 ATOM 4531 C CE2 . TYR B 1 201 ? -3.791 34.136 63.364 1.00 8.02 ? 281 TYR B CE2 1 ATOM 4532 C CZ . TYR B 1 201 ? -3.820 32.974 64.107 1.00 7.76 ? 281 TYR B CZ 1 ATOM 4533 O OH . TYR B 1 201 ? -4.372 32.975 65.368 1.00 9.38 ? 281 TYR B OH 1 ATOM 4534 N N . PRO B 1 202 ? -0.765 35.834 59.932 1.00 9.30 ? 282 PRO B N 1 ATOM 4535 C CA . PRO B 1 202 ? -0.733 37.238 60.350 1.00 4.98 ? 282 PRO B CA 1 ATOM 4536 C C . PRO B 1 202 ? -2.071 37.668 60.937 1.00 8.41 ? 282 PRO B C 1 ATOM 4537 O O . PRO B 1 202 ? -3.116 37.191 60.501 1.00 8.00 ? 282 PRO B O 1 ATOM 4538 C CB . PRO B 1 202 ? -0.509 37.997 59.035 1.00 4.97 ? 282 PRO B CB 1 ATOM 4539 C CG . PRO B 1 202 ? -0.489 36.953 57.935 1.00 11.16 ? 282 PRO B CG 1 ATOM 4540 C CD . PRO B 1 202 ? -1.075 35.707 58.500 1.00 8.05 ? 282 PRO B CD 1 ATOM 4541 N N . ASP B 1 203 ? -2.031 38.576 61.902 1.00 6.03 ? 283 ASP B N 1 ATOM 4542 C CA . ASP B 1 203 ? -3.241 39.074 62.543 1.00 11.69 ? 283 ASP B CA 1 ATOM 4543 C C . ASP B 1 203 ? -2.907 40.380 63.255 1.00 10.36 ? 283 ASP B C 1 ATOM 4544 O O . ASP B 1 203 ? -2.150 40.386 64.223 1.00 12.23 ? 283 ASP B O 1 ATOM 4545 C CB . ASP B 1 203 ? -3.763 38.037 63.540 1.00 9.42 ? 283 ASP B CB 1 ATOM 4546 C CG . ASP B 1 203 ? -5.081 38.434 64.173 1.00 14.71 ? 283 ASP B CG 1 ATOM 4547 O OD1 . ASP B 1 203 ? -5.625 39.507 63.831 1.00 16.97 ? 283 ASP B OD1 1 ATOM 4548 O OD2 . ASP B 1 203 ? -5.578 37.663 65.020 1.00 16.58 ? 283 ASP B OD2 1 ATOM 4549 N N . SER B 1 204 ? -3.457 41.486 62.762 1.00 10.12 ? 284 SER B N 1 ATOM 4550 C CA . SER B 1 204 ? -3.204 42.800 63.351 1.00 10.87 ? 284 SER B CA 1 ATOM 4551 C C . SER B 1 204 ? -1.708 43.107 63.453 1.00 11.89 ? 284 SER B C 1 ATOM 4552 O O . SER B 1 204 ? -1.212 43.477 64.519 1.00 6.45 ? 284 SER B O 1 ATOM 4553 C CB . SER B 1 204 ? -3.859 42.902 64.733 1.00 16.13 ? 284 SER B CB 1 ATOM 4554 O OG . SER B 1 204 ? -5.269 42.776 64.641 1.00 17.08 ? 284 SER B OG 1 ATOM 4555 N N . SER B 1 205 ? -1.000 42.934 62.340 1.00 6.95 ? 285 SER B N 1 ATOM 4556 C CA . SER B 1 205 ? 0.421 43.279 62.244 1.00 8.55 ? 285 SER B CA 1 ATOM 4557 C C . SER B 1 205 ? 1.347 42.376 63.060 1.00 10.78 ? 285 SER B C 1 ATOM 4558 O O . SER B 1 205 ? 2.552 42.616 63.125 1.00 10.27 ? 285 SER B O 1 ATOM 4559 C CB . SER B 1 205 ? 0.653 44.746 62.626 1.00 14.15 ? 285 SER B CB 1 ATOM 4560 O OG . SER B 1 205 ? -0.063 45.615 61.770 1.00 12.12 ? 285 SER B OG 1 ATOM 4561 N N . GLU B 1 206 ? 0.791 41.342 63.680 1.00 10.57 ? 286 GLU B N 1 ATOM 4562 C CA . GLU B 1 206 ? 1.603 40.407 64.453 1.00 10.88 ? 286 GLU B CA 1 ATOM 4563 C C . GLU B 1 206 ? 1.394 38.976 63.976 1.00 11.29 ? 286 GLU B C 1 ATOM 4564 O O . GLU B 1 206 ? 0.395 38.671 63.328 1.00 11.30 ? 286 GLU B O 1 ATOM 4565 C CB . GLU B 1 206 ? 1.303 40.530 65.950 1.00 14.97 ? 286 GLU B CB 1 ATOM 4566 C CG . GLU B 1 206 ? 1.563 41.921 66.513 1.00 16.92 ? 286 GLU B CG 1 ATOM 4567 C CD . GLU B 1 206 ? 1.532 41.958 68.029 1.00 32.33 ? 286 GLU B CD 1 ATOM 4568 O OE1 . GLU B 1 206 ? 1.450 40.879 68.652 1.00 33.53 ? 286 GLU B OE1 1 ATOM 4569 O OE2 . GLU B 1 206 ? 1.594 43.069 68.597 1.00 38.67 ? 286 GLU B OE2 1 ATOM 4570 N N . ILE B 1 207 ? 2.342 38.102 64.297 1.00 8.55 ? 287 ILE B N 1 ATOM 4571 C CA . ILE B 1 207 ? 2.289 36.725 63.823 1.00 6.65 ? 287 ILE B CA 1 ATOM 4572 C C . ILE B 1 207 ? 1.955 35.750 64.944 1.00 5.87 ? 287 ILE B C 1 ATOM 4573 O O . ILE B 1 207 ? 2.491 35.844 66.047 1.00 8.28 ? 287 ILE B O 1 ATOM 4574 C CB . ILE B 1 207 ? 3.619 36.300 63.176 1.00 6.84 ? 287 ILE B CB 1 ATOM 4575 C CG1 . ILE B 1 207 ? 4.059 37.335 62.139 1.00 8.25 ? 287 ILE B CG1 1 ATOM 4576 C CG2 . ILE B 1 207 ? 3.485 34.918 62.548 1.00 5.11 ? 287 ILE B CG2 1 ATOM 4577 C CD1 . ILE B 1 207 ? 3.041 37.569 61.045 1.00 13.04 ? 287 ILE B CD1 1 ATOM 4578 N N . THR B 1 208 ? 1.059 34.815 64.651 1.00 6.28 ? 288 THR B N 1 ATOM 4579 C CA . THR B 1 208 ? 0.709 33.767 65.597 1.00 10.64 ? 288 THR B CA 1 ATOM 4580 C C . THR B 1 208 ? 0.998 32.416 64.965 1.00 9.55 ? 288 THR B C 1 ATOM 4581 O O . THR B 1 208 ? 0.608 32.165 63.825 1.00 6.85 ? 288 THR B O 1 ATOM 4582 C CB . THR B 1 208 ? -0.776 33.839 65.985 1.00 13.28 ? 288 THR B CB 1 ATOM 4583 O OG1 . THR B 1 208 ? -1.024 35.066 66.681 1.00 9.92 ? 288 THR B OG1 1 ATOM 4584 C CG2 . THR B 1 208 ? -1.155 32.668 66.878 1.00 8.75 ? 288 THR B CG2 1 ATOM 4585 N N . CYS B 1 209 ? 1.696 31.557 65.701 1.00 4.17 ? 289 CYS B N 1 ATOM 4586 C CA . CYS B 1 209 ? 2.021 30.219 65.218 1.00 5.62 ? 289 CYS B CA 1 ATOM 4587 C C . CYS B 1 209 ? 1.502 29.150 66.169 1.00 7.46 ? 289 CYS B C 1 ATOM 4588 O O . CYS B 1 209 ? 1.709 29.234 67.378 1.00 7.99 ? 289 CYS B O 1 ATOM 4589 C CB . CYS B 1 209 ? 3.536 30.045 65.062 1.00 7.08 ? 289 CYS B CB 1 ATOM 4590 S SG . CYS B 1 209 ? 4.334 31.146 63.876 1.00 12.23 ? 289 CYS B SG 1 ATOM 4591 N N . VAL B 1 210 ? 0.831 28.145 65.615 1.00 6.47 ? 290 VAL B N 1 ATOM 4592 C CA . VAL B 1 210 ? 0.424 26.974 66.381 1.00 6.52 ? 290 VAL B CA 1 ATOM 4593 C C . VAL B 1 210 ? 1.135 25.760 65.797 1.00 7.35 ? 290 VAL B C 1 ATOM 4594 O O . VAL B 1 210 ? 1.092 25.528 64.589 1.00 4.75 ? 290 VAL B O 1 ATOM 4595 C CB . VAL B 1 210 ? -1.101 26.774 66.356 1.00 5.01 ? 290 VAL B CB 1 ATOM 4596 C CG1 . VAL B 1 210 ? -1.487 25.514 67.121 1.00 5.02 ? 290 VAL B CG1 1 ATOM 4597 C CG2 . VAL B 1 210 ? -1.798 27.992 66.942 1.00 5.91 ? 290 VAL B CG2 1 ATOM 4598 N N . CYS B 1 211 ? 1.795 24.992 66.657 1.00 5.61 ? 291 CYS B N 1 ATOM 4599 C CA . CYS B 1 211 ? 2.770 24.014 66.194 1.00 5.89 ? 291 CYS B CA 1 ATOM 4600 C C . CYS B 1 211 ? 2.561 22.614 66.774 1.00 5.94 ? 291 CYS B C 1 ATOM 4601 O O . CYS B 1 211 ? 1.503 22.306 67.324 1.00 6.59 ? 291 CYS B O 1 ATOM 4602 C CB . CYS B 1 211 ? 4.181 24.518 66.510 1.00 5.69 ? 291 CYS B CB 1 ATOM 4603 S SG . CYS B 1 211 ? 4.416 26.287 66.149 1.00 9.16 ? 291 CYS B SG 1 ATOM 4604 N N . ARG B 1 212 ? 3.581 21.772 66.634 1.00 4.31 ? 292 ARG B N 1 ATOM 4605 C CA . ARG B 1 212 ? 3.518 20.372 67.045 1.00 6.70 ? 292 ARG B CA 1 ATOM 4606 C C . ARG B 1 212 ? 4.614 20.045 68.059 1.00 6.19 ? 292 ARG B C 1 ATOM 4607 O O . ARG B 1 212 ? 5.799 20.201 67.773 1.00 8.17 ? 292 ARG B O 1 ATOM 4608 C CB . ARG B 1 212 ? 3.650 19.467 65.814 1.00 5.64 ? 292 ARG B CB 1 ATOM 4609 C CG . ARG B 1 212 ? 4.041 18.018 66.091 1.00 6.73 ? 292 ARG B CG 1 ATOM 4610 C CD . ARG B 1 212 ? 4.236 17.259 64.775 1.00 10.72 ? 292 ARG B CD 1 ATOM 4611 N NE . ARG B 1 212 ? 4.731 15.895 64.962 1.00 6.99 ? 292 ARG B NE 1 ATOM 4612 C CZ . ARG B 1 212 ? 4.864 15.007 63.979 1.00 13.54 ? 292 ARG B CZ 1 ATOM 4613 N NH1 . ARG B 1 212 ? 4.533 15.331 62.735 1.00 6.64 ? 292 ARG B NH1 1 ATOM 4614 N NH2 . ARG B 1 212 ? 5.323 13.789 64.237 1.00 12.06 ? 292 ARG B NH2 1 ATOM 4615 N N . ASP B 1 213 ? 4.208 19.604 69.245 1.00 6.23 ? 293 ASP B N 1 ATOM 4616 C CA . ASP B 1 213 ? 5.143 19.157 70.275 1.00 6.27 ? 293 ASP B CA 1 ATOM 4617 C C . ASP B 1 213 ? 5.326 17.657 70.109 1.00 7.41 ? 293 ASP B C 1 ATOM 4618 O O . ASP B 1 213 ? 4.446 16.892 70.459 1.00 6.25 ? 293 ASP B O 1 ATOM 4619 C CB . ASP B 1 213 ? 4.579 19.479 71.667 1.00 5.34 ? 293 ASP B CB 1 ATOM 4620 C CG . ASP B 1 213 ? 5.421 18.906 72.806 1.00 9.26 ? 293 ASP B CG 1 ATOM 4621 O OD1 . ASP B 1 213 ? 6.191 17.952 72.581 1.00 8.57 ? 293 ASP B OD1 1 ATOM 4622 O OD2 . ASP B 1 213 ? 5.296 19.411 73.944 1.00 8.97 ? 293 ASP B OD2 1 ATOM 4623 N N . ASN B 1 214 ? 6.462 17.234 69.567 1.00 7.97 ? 294 ASN B N 1 ATOM 4624 C CA . ASN B 1 214 ? 6.683 15.817 69.299 1.00 8.18 ? 294 ASN B CA 1 ATOM 4625 C C . ASN B 1 214 ? 7.333 15.105 70.479 1.00 8.85 ? 294 ASN B C 1 ATOM 4626 O O . ASN B 1 214 ? 7.576 13.898 70.440 1.00 8.85 ? 294 ASN B O 1 ATOM 4627 C CB . ASN B 1 214 ? 7.549 15.641 68.051 1.00 7.90 ? 294 ASN B CB 1 ATOM 4628 C CG . ASN B 1 214 ? 7.271 14.339 67.332 1.00 13.34 ? 294 ASN B CG 1 ATOM 4629 O OD1 . ASN B 1 214 ? 6.153 14.097 66.878 1.00 11.06 ? 294 ASN B OD1 1 ATOM 4630 N ND2 . ASN B 1 214 ? 8.289 13.493 67.221 1.00 12.27 ? 294 ASN B ND2 1 ATOM 4631 N N . TRP B 1 215 ? 7.597 15.869 71.531 1.00 9.88 ? 295 TRP B N 1 ATOM 4632 C CA . TRP B 1 215 ? 8.368 15.399 72.674 1.00 9.57 ? 295 TRP B CA 1 ATOM 4633 C C . TRP B 1 215 ? 7.476 14.861 73.790 1.00 10.36 ? 295 TRP B C 1 ATOM 4634 O O . TRP B 1 215 ? 7.555 13.684 74.138 1.00 7.88 ? 295 TRP B O 1 ATOM 4635 C CB . TRP B 1 215 ? 9.246 16.546 73.181 1.00 7.85 ? 295 TRP B CB 1 ATOM 4636 C CG . TRP B 1 215 ? 10.027 16.277 74.431 1.00 9.14 ? 295 TRP B CG 1 ATOM 4637 C CD1 . TRP B 1 215 ? 10.248 15.069 75.030 1.00 13.59 ? 295 TRP B CD1 1 ATOM 4638 C CD2 . TRP B 1 215 ? 10.709 17.251 75.229 1.00 9.09 ? 295 TRP B CD2 1 ATOM 4639 N NE1 . TRP B 1 215 ? 11.019 15.236 76.158 1.00 11.53 ? 295 TRP B NE1 1 ATOM 4640 C CE2 . TRP B 1 215 ? 11.314 16.566 76.301 1.00 10.07 ? 295 TRP B CE2 1 ATOM 4641 C CE3 . TRP B 1 215 ? 10.861 18.639 75.142 1.00 8.73 ? 295 TRP B CE3 1 ATOM 4642 C CZ2 . TRP B 1 215 ? 12.063 17.221 77.275 1.00 12.68 ? 295 TRP B CZ2 1 ATOM 4643 C CZ3 . TRP B 1 215 ? 11.602 19.288 76.111 1.00 12.11 ? 295 TRP B CZ3 1 ATOM 4644 C CH2 . TRP B 1 215 ? 12.195 18.579 77.164 1.00 11.45 ? 295 TRP B CH2 1 ATOM 4645 N N . HIS B 1 216 ? 6.623 15.718 74.346 1.00 9.45 ? 296 HIS B N 1 ATOM 4646 C CA . HIS B 1 216 ? 5.816 15.326 75.499 1.00 11.34 ? 296 HIS B CA 1 ATOM 4647 C C . HIS B 1 216 ? 4.550 16.161 75.691 1.00 10.59 ? 296 HIS B C 1 ATOM 4648 O O . HIS B 1 216 ? 4.186 16.491 76.819 1.00 8.38 ? 296 HIS B O 1 ATOM 4649 C CB . HIS B 1 216 ? 6.664 15.383 76.774 1.00 9.20 ? 296 HIS B CB 1 ATOM 4650 C CG . HIS B 1 216 ? 7.278 16.725 77.031 1.00 13.21 ? 296 HIS B CG 1 ATOM 4651 N ND1 . HIS B 1 216 ? 8.305 16.913 77.932 1.00 10.36 ? 296 HIS B ND1 1 ATOM 4652 C CD2 . HIS B 1 216 ? 7.012 17.943 76.504 1.00 10.60 ? 296 HIS B CD2 1 ATOM 4653 C CE1 . HIS B 1 216 ? 8.643 18.190 77.950 1.00 11.41 ? 296 HIS B CE1 1 ATOM 4654 N NE2 . HIS B 1 216 ? 7.875 18.837 77.092 1.00 11.32 ? 296 HIS B NE2 1 ATOM 4655 N N . GLY B 1 217 ? 3.872 16.495 74.598 1.00 6.73 ? 297 GLY B N 1 ATOM 4656 C CA . GLY B 1 217 ? 2.666 17.298 74.697 1.00 8.47 ? 297 GLY B CA 1 ATOM 4657 C C . GLY B 1 217 ? 1.572 16.871 73.740 1.00 9.09 ? 297 GLY B C 1 ATOM 4658 O O . GLY B 1 217 ? 1.784 16.832 72.534 1.00 8.12 ? 297 GLY B O 1 ATOM 4659 N N . SER B 1 218 ? 0.398 16.558 74.277 1.00 9.78 ? 298 SER B N 1 ATOM 4660 C CA . SER B 1 218 ? -0.740 16.160 73.450 1.00 9.50 ? 298 SER B CA 1 ATOM 4661 C C . SER B 1 218 ? -1.624 17.358 73.108 1.00 10.12 ? 298 SER B C 1 ATOM 4662 O O . SER B 1 218 ? -2.543 17.256 72.290 1.00 8.45 ? 298 SER B O 1 ATOM 4663 C CB . SER B 1 218 ? -1.552 15.060 74.137 1.00 8.29 ? 298 SER B CB 1 ATOM 4664 O OG . SER B 1 218 ? -1.838 15.403 75.481 1.00 13.60 ? 298 SER B OG 1 ATOM 4665 N N . ASN B 1 219 ? -1.348 18.488 73.752 1.00 8.55 ? 299 ASN B N 1 ATOM 4666 C CA . ASN B 1 219 ? -1.879 19.772 73.311 1.00 8.17 ? 299 ASN B CA 1 ATOM 4667 C C . ASN B 1 219 ? -0.824 20.482 72.468 1.00 6.98 ? 299 ASN B C 1 ATOM 4668 O O . ASN B 1 219 ? 0.342 20.091 72.478 1.00 9.27 ? 299 ASN B O 1 ATOM 4669 C CB . ASN B 1 219 ? -2.304 20.640 74.498 1.00 6.50 ? 299 ASN B CB 1 ATOM 4670 C CG . ASN B 1 219 ? -1.201 20.812 75.531 1.00 10.88 ? 299 ASN B CG 1 ATOM 4671 O OD1 . ASN B 1 219 ? -0.262 20.018 75.600 1.00 8.10 ? 299 ASN B OD1 1 ATOM 4672 N ND2 . ASN B 1 219 ? -1.319 21.853 76.348 1.00 6.91 ? 299 ASN B ND2 1 ATOM 4673 N N . ARG B 1 220 ? -1.224 21.519 71.739 1.00 8.09 ? 300 ARG B N 1 ATOM 4674 C CA . ARG B 1 220 ? -0.301 22.202 70.833 1.00 5.47 ? 300 ARG B CA 1 ATOM 4675 C C . ARG B 1 220 ? 0.366 23.423 71.455 1.00 6.06 ? 300 ARG B C 1 ATOM 4676 O O . ARG B 1 220 ? -0.290 24.230 72.113 1.00 6.37 ? 300 ARG B O 1 ATOM 4677 C CB . ARG B 1 220 ? -1.011 22.606 69.537 1.00 5.29 ? 300 ARG B CB 1 ATOM 4678 C CG . ARG B 1 220 ? -1.554 21.429 68.746 1.00 6.57 ? 300 ARG B CG 1 ATOM 4679 C CD . ARG B 1 220 ? -1.857 21.802 67.300 1.00 5.65 ? 300 ARG B CD 1 ATOM 4680 N NE . ARG B 1 220 ? -2.290 20.631 66.546 1.00 7.08 ? 300 ARG B NE 1 ATOM 4681 C CZ . ARG B 1 220 ? -1.461 19.735 66.021 1.00 8.04 ? 300 ARG B CZ 1 ATOM 4682 N NH1 . ARG B 1 220 ? -0.149 19.885 66.156 1.00 6.55 ? 300 ARG B NH1 1 ATOM 4683 N NH2 . ARG B 1 220 ? -1.943 18.691 65.362 1.00 6.36 ? 300 ARG B NH2 1 ATOM 4684 N N . PRO B 1 221 ? 1.681 23.561 71.240 1.00 5.85 ? 301 PRO B N 1 ATOM 4685 C CA . PRO B 1 221 ? 2.418 24.757 71.654 1.00 6.53 ? 301 PRO B CA 1 ATOM 4686 C C . PRO B 1 221 ? 2.158 25.907 70.692 1.00 7.65 ? 301 PRO B C 1 ATOM 4687 O O . PRO B 1 221 ? 1.842 25.675 69.524 1.00 6.86 ? 301 PRO B O 1 ATOM 4688 C CB . PRO B 1 221 ? 3.876 24.314 71.542 1.00 6.43 ? 301 PRO B CB 1 ATOM 4689 C CG . PRO B 1 221 ? 3.861 23.304 70.442 1.00 7.26 ? 301 PRO B CG 1 ATOM 4690 C CD . PRO B 1 221 ? 2.562 22.558 70.615 1.00 6.58 ? 301 PRO B CD 1 ATOM 4691 N N . TRP B 1 222 ? 2.285 27.135 71.179 1.00 5.52 ? 302 TRP B N 1 ATOM 4692 C CA . TRP B 1 222 ? 2.152 28.296 70.316 1.00 7.30 ? 302 TRP B CA 1 ATOM 4693 C C . TRP B 1 222 ? 3.232 29.326 70.606 1.00 6.11 ? 302 TRP B C 1 ATOM 4694 O O . TRP B 1 222 ? 3.800 29.365 71.699 1.00 7.73 ? 302 TRP B O 1 ATOM 4695 C CB . TRP B 1 222 ? 0.755 28.924 70.432 1.00 5.77 ? 302 TRP B CB 1 ATOM 4696 C CG . TRP B 1 222 ? 0.395 29.407 71.807 1.00 7.42 ? 302 TRP B CG 1 ATOM 4697 C CD1 . TRP B 1 222 ? -0.357 28.745 72.738 1.00 7.81 ? 302 TRP B CD1 1 ATOM 4698 C CD2 . TRP B 1 222 ? 0.758 30.660 72.403 1.00 6.19 ? 302 TRP B CD2 1 ATOM 4699 N NE1 . TRP B 1 222 ? -0.479 29.506 73.876 1.00 7.06 ? 302 TRP B NE1 1 ATOM 4700 C CE2 . TRP B 1 222 ? 0.196 30.685 73.696 1.00 7.33 ? 302 TRP B CE2 1 ATOM 4701 C CE3 . TRP B 1 222 ? 1.506 31.760 71.970 1.00 6.71 ? 302 TRP B CE3 1 ATOM 4702 C CZ2 . TRP B 1 222 ? 0.358 31.768 74.561 1.00 10.89 ? 302 TRP B CZ2 1 ATOM 4703 C CZ3 . TRP B 1 222 ? 1.668 32.835 72.831 1.00 9.01 ? 302 TRP B CZ3 1 ATOM 4704 C CH2 . TRP B 1 222 ? 1.096 32.830 74.112 1.00 11.52 ? 302 TRP B CH2 1 ATOM 4705 N N . VAL B 1 223 ? 3.525 30.140 69.603 1.00 8.15 ? 303 VAL B N 1 ATOM 4706 C CA . VAL B 1 223 ? 4.431 31.263 69.763 1.00 5.77 ? 303 VAL B CA 1 ATOM 4707 C C . VAL B 1 223 ? 3.882 32.416 68.942 1.00 8.33 ? 303 VAL B C 1 ATOM 4708 O O . VAL B 1 223 ? 3.441 32.225 67.807 1.00 7.00 ? 303 VAL B O 1 ATOM 4709 C CB . VAL B 1 223 ? 5.869 30.916 69.311 1.00 6.74 ? 303 VAL B CB 1 ATOM 4710 C CG1 . VAL B 1 223 ? 5.874 30.386 67.883 1.00 5.91 ? 303 VAL B CG1 1 ATOM 4711 C CG2 . VAL B 1 223 ? 6.781 32.132 69.443 1.00 8.12 ? 303 VAL B CG2 1 ATOM 4712 N N . SER B 1 224 ? 3.871 33.606 69.529 1.00 6.18 ? 304 SER B N 1 ATOM 4713 C CA . SER B 1 224 ? 3.447 34.797 68.811 1.00 6.97 ? 304 SER B CA 1 ATOM 4714 C C . SER B 1 224 ? 4.521 35.867 68.944 1.00 10.19 ? 304 SER B C 1 ATOM 4715 O O . SER B 1 224 ? 5.263 35.895 69.925 1.00 9.03 ? 304 SER B O 1 ATOM 4716 C CB . SER B 1 224 ? 2.102 35.307 69.337 1.00 7.45 ? 304 SER B CB 1 ATOM 4717 O OG . SER B 1 224 ? 2.198 35.693 70.695 1.00 14.93 ? 304 SER B OG 1 ATOM 4718 N N . PHE B 1 225 ? 4.608 36.741 67.950 1.00 5.98 ? 305 PHE B N 1 ATOM 4719 C CA . PHE B 1 225 ? 5.641 37.766 67.942 1.00 9.40 ? 305 PHE B CA 1 ATOM 4720 C C . PHE B 1 225 ? 5.275 38.936 67.038 1.00 8.60 ? 305 PHE B C 1 ATOM 4721 O O . PHE B 1 225 ? 4.491 38.785 66.100 1.00 7.39 ? 305 PHE B O 1 ATOM 4722 C CB . PHE B 1 225 ? 6.988 37.164 67.522 1.00 4.40 ? 305 PHE B CB 1 ATOM 4723 C CG . PHE B 1 225 ? 6.923 36.329 66.267 1.00 6.43 ? 305 PHE B CG 1 ATOM 4724 C CD1 . PHE B 1 225 ? 7.157 36.897 65.025 1.00 8.00 ? 305 PHE B CD1 1 ATOM 4725 C CD2 . PHE B 1 225 ? 6.642 34.971 66.335 1.00 8.76 ? 305 PHE B CD2 1 ATOM 4726 C CE1 . PHE B 1 225 ? 7.103 36.130 63.870 1.00 6.26 ? 305 PHE B CE1 1 ATOM 4727 C CE2 . PHE B 1 225 ? 6.585 34.197 65.185 1.00 6.87 ? 305 PHE B CE2 1 ATOM 4728 C CZ . PHE B 1 225 ? 6.819 34.777 63.951 1.00 4.51 ? 305 PHE B CZ 1 ATOM 4729 N N . ASN B 1 226 ? 5.836 40.104 67.333 1.00 6.80 ? 306 ASN B N 1 ATOM 4730 C CA . ASN B 1 226 ? 5.664 41.262 66.467 1.00 10.81 ? 306 ASN B CA 1 ATOM 4731 C C . ASN B 1 226 ? 6.748 41.296 65.396 1.00 6.97 ? 306 ASN B C 1 ATOM 4732 O O . ASN B 1 226 ? 7.568 40.382 65.305 1.00 5.17 ? 306 ASN B O 1 ATOM 4733 C CB . ASN B 1 226 ? 5.630 42.565 67.275 1.00 10.89 ? 306 ASN B CB 1 ATOM 4734 C CG . ASN B 1 226 ? 6.879 42.777 68.113 1.00 10.53 ? 306 ASN B CG 1 ATOM 4735 O OD1 . ASN B 1 226 ? 7.976 42.360 67.740 1.00 7.96 ? 306 ASN B OD1 1 ATOM 4736 N ND2 . ASN B 1 226 ? 6.717 43.440 69.253 1.00 11.72 ? 306 ASN B ND2 1 ATOM 4737 N N . GLN B 1 227 ? 6.754 42.345 64.584 1.00 7.44 ? 308 GLN B N 1 ATOM 4738 C CA . GLN B 1 227 ? 7.712 42.436 63.486 1.00 8.43 ? 308 GLN B CA 1 ATOM 4739 C C . GLN B 1 227 ? 9.160 42.509 63.974 1.00 9.75 ? 308 GLN B C 1 ATOM 4740 O O . GLN B 1 227 ? 10.087 42.172 63.236 1.00 9.87 ? 308 GLN B O 1 ATOM 4741 C CB . GLN B 1 227 ? 7.382 43.622 62.581 1.00 9.93 ? 308 GLN B CB 1 ATOM 4742 C CG . GLN B 1 227 ? 6.031 43.497 61.891 1.00 8.04 ? 308 GLN B CG 1 ATOM 4743 C CD . GLN B 1 227 ? 5.630 44.764 61.169 1.00 14.43 ? 308 GLN B CD 1 ATOM 4744 O OE1 . GLN B 1 227 ? 6.308 45.205 60.244 1.00 17.88 ? 308 GLN B OE1 1 ATOM 4745 N NE2 . GLN B 1 227 ? 4.521 45.357 61.590 1.00 18.62 ? 308 GLN B NE2 1 ATOM 4746 N N . ASN B 1 228 ? 9.351 42.936 65.219 1.00 10.26 ? 309 ASN B N 1 ATOM 4747 C CA . ASN B 1 228 ? 10.693 43.032 65.788 1.00 9.96 ? 309 ASN B CA 1 ATOM 4748 C C . ASN B 1 228 ? 11.149 41.730 66.441 1.00 7.19 ? 309 ASN B C 1 ATOM 4749 O O . ASN B 1 228 ? 12.231 41.660 67.025 1.00 9.16 ? 309 ASN B O 1 ATOM 4750 C CB . ASN B 1 228 ? 10.781 44.197 66.777 1.00 10.83 ? 309 ASN B CB 1 ATOM 4751 C CG . ASN B 1 228 ? 10.896 45.544 66.082 1.00 24.18 ? 309 ASN B CG 1 ATOM 4752 O OD1 . ASN B 1 228 ? 11.148 45.615 64.880 1.00 26.23 ? 309 ASN B OD1 1 ATOM 4753 N ND2 . ASN B 1 228 ? 10.715 46.619 66.839 1.00 33.40 ? 309 ASN B ND2 1 ATOM 4754 N N . LEU B 1 229 ? 10.309 40.705 66.331 1.00 8.47 ? 310 LEU B N 1 ATOM 4755 C CA . LEU B 1 229 ? 10.596 39.369 66.853 1.00 6.61 ? 310 LEU B CA 1 ATOM 4756 C C . LEU B 1 229 ? 10.549 39.292 68.377 1.00 8.14 ? 310 LEU B C 1 ATOM 4757 O O . LEU B 1 229 ? 11.098 38.367 68.978 1.00 9.34 ? 310 LEU B O 1 ATOM 4758 C CB . LEU B 1 229 ? 11.932 38.837 66.324 1.00 8.43 ? 310 LEU B CB 1 ATOM 4759 C CG . LEU B 1 229 ? 12.070 38.773 64.801 1.00 9.25 ? 310 LEU B CG 1 ATOM 4760 C CD1 . LEU B 1 229 ? 13.335 38.021 64.412 1.00 8.76 ? 310 LEU B CD1 1 ATOM 4761 C CD2 . LEU B 1 229 ? 10.841 38.125 64.173 1.00 8.00 ? 310 LEU B CD2 1 ATOM 4762 N N . GLU B 1 230 ? 9.900 40.271 68.997 1.00 7.30 ? 311 GLU B N 1 ATOM 4763 C CA . GLU B 1 230 ? 9.596 40.192 70.418 1.00 8.80 ? 311 GLU B CA 1 ATOM 4764 C C . GLU B 1 230 ? 8.451 39.199 70.581 1.00 10.96 ? 311 GLU B C 1 ATOM 4765 O O . GLU B 1 230 ? 7.348 39.429 70.086 1.00 12.72 ? 311 GLU B O 1 ATOM 4766 C CB . GLU B 1 230 ? 9.223 41.571 70.963 1.00 10.67 ? 311 GLU B CB 1 ATOM 4767 C CG . GLU B 1 230 ? 10.363 42.578 70.854 1.00 15.96 ? 311 GLU B CG 1 ATOM 4768 C CD . GLU B 1 230 ? 9.956 43.992 71.229 1.00 26.77 ? 311 GLU B CD 1 ATOM 4769 O OE1 . GLU B 1 230 ? 8.773 44.350 71.040 1.00 22.65 ? 311 GLU B OE1 1 ATOM 4770 O OE2 . GLU B 1 230 ? 10.827 44.751 71.704 1.00 25.48 ? 311 GLU B OE2 1 ATOM 4771 N N . TYR B 1 231 ? 8.720 38.084 71.254 1.00 6.48 ? 312 TYR B N 1 ATOM 4772 C CA . TYR B 1 231 ? 7.790 36.959 71.236 1.00 6.82 ? 312 TYR B CA 1 ATOM 4773 C C . TYR B 1 231 ? 7.180 36.601 72.590 1.00 12.49 ? 312 TYR B C 1 ATOM 4774 O O . TYR B 1 231 ? 7.646 37.038 73.645 1.00 9.03 ? 312 TYR B O 1 ATOM 4775 C CB . TYR B 1 231 ? 8.471 35.718 70.646 1.00 8.19 ? 312 TYR B CB 1 ATOM 4776 C CG . TYR B 1 231 ? 9.616 35.193 71.487 1.00 11.01 ? 312 TYR B CG 1 ATOM 4777 C CD1 . TYR B 1 231 ? 9.384 34.320 72.544 1.00 9.84 ? 312 TYR B CD1 1 ATOM 4778 C CD2 . TYR B 1 231 ? 10.925 35.573 71.225 1.00 9.81 ? 312 TYR B CD2 1 ATOM 4779 C CE1 . TYR B 1 231 ? 10.427 33.842 73.317 1.00 10.55 ? 312 TYR B CE1 1 ATOM 4780 C CE2 . TYR B 1 231 ? 11.975 35.102 71.992 1.00 10.35 ? 312 TYR B CE2 1 ATOM 4781 C CZ . TYR B 1 231 ? 11.720 34.238 73.036 1.00 9.88 ? 312 TYR B CZ 1 ATOM 4782 O OH . TYR B 1 231 ? 12.763 33.769 73.800 1.00 9.96 ? 312 TYR B OH 1 ATOM 4783 N N . GLN B 1 232 ? 6.124 35.796 72.529 1.00 3.77 ? 313 GLN B N 1 ATOM 4784 C CA . GLN B 1 232 ? 5.528 35.168 73.698 1.00 9.16 ? 313 GLN B CA 1 ATOM 4785 C C . GLN B 1 232 ? 5.279 33.705 73.355 1.00 9.39 ? 313 GLN B C 1 ATOM 4786 O O . GLN B 1 232 ? 5.065 33.366 72.190 1.00 4.83 ? 313 GLN B O 1 ATOM 4787 C CB . GLN B 1 232 ? 4.213 35.850 74.073 1.00 10.85 ? 313 GLN B CB 1 ATOM 4788 C CG . GLN B 1 232 ? 4.369 37.283 74.552 1.00 14.68 ? 313 GLN B CG 1 ATOM 4789 C CD . GLN B 1 232 ? 3.046 37.908 74.953 1.00 33.17 ? 313 GLN B CD 1 ATOM 4790 O OE1 . GLN B 1 232 ? 2.127 38.019 74.140 1.00 39.18 ? 313 GLN B OE1 1 ATOM 4791 N NE2 . GLN B 1 232 ? 2.944 38.322 76.210 1.00 36.74 ? 313 GLN B NE2 1 ATOM 4792 N N . ILE B 1 233 ? 5.316 32.839 74.363 1.00 8.66 ? 314 ILE B N 1 ATOM 4793 C CA . ILE B 1 233 ? 5.122 31.410 74.144 1.00 5.41 ? 314 ILE B CA 1 ATOM 4794 C C . ILE B 1 233 ? 4.126 30.819 75.136 1.00 10.11 ? 314 ILE B C 1 ATOM 4795 O O . ILE B 1 233 ? 3.884 31.382 76.202 1.00 7.66 ? 314 ILE B O 1 ATOM 4796 C CB . ILE B 1 233 ? 6.446 30.632 74.250 1.00 8.74 ? 314 ILE B CB 1 ATOM 4797 C CG1 . ILE B 1 233 ? 7.092 30.862 75.619 1.00 9.85 ? 314 ILE B CG1 1 ATOM 4798 C CG2 . ILE B 1 233 ? 7.397 31.036 73.130 1.00 8.39 ? 314 ILE B CG2 1 ATOM 4799 C CD1 . ILE B 1 233 ? 8.349 30.048 75.842 1.00 8.74 ? 314 ILE B CD1 1 ATOM 4800 N N . GLY B 1 234 ? 3.553 29.676 74.775 1.00 7.89 ? 315 GLY B N 1 ATOM 4801 C CA . GLY B 1 234 ? 2.615 28.987 75.640 1.00 8.25 ? 315 GLY B CA 1 ATOM 4802 C C . GLY B 1 234 ? 2.074 27.732 74.987 1.00 7.86 ? 315 GLY B C 1 ATOM 4803 O O . GLY B 1 234 ? 2.541 27.325 73.922 1.00 7.76 ? 315 GLY B O 1 ATOM 4804 N N . TYR B 1 235 ? 1.097 27.113 75.638 1.00 6.36 ? 316 TYR B N 1 ATOM 4805 C CA . TYR B 1 235 ? 0.382 25.975 75.075 1.00 7.75 ? 316 TYR B CA 1 ATOM 4806 C C . TYR B 1 235 ? -1.110 26.270 75.092 1.00 7.19 ? 316 TYR B C 1 ATOM 4807 O O . TYR B 1 235 ? -1.599 26.970 75.977 1.00 8.77 ? 316 TYR B O 1 ATOM 4808 C CB . TYR B 1 235 ? 0.658 24.704 75.884 1.00 8.58 ? 316 TYR B CB 1 ATOM 4809 C CG . TYR B 1 235 ? 1.929 23.983 75.499 1.00 8.86 ? 316 TYR B CG 1 ATOM 4810 C CD1 . TYR B 1 235 ? 3.170 24.459 75.900 1.00 11.09 ? 316 TYR B CD1 1 ATOM 4811 C CD2 . TYR B 1 235 ? 1.887 22.817 74.745 1.00 7.39 ? 316 TYR B CD2 1 ATOM 4812 C CE1 . TYR B 1 235 ? 4.337 23.801 75.553 1.00 11.51 ? 316 TYR B CE1 1 ATOM 4813 C CE2 . TYR B 1 235 ? 3.049 22.148 74.393 1.00 8.56 ? 316 TYR B CE2 1 ATOM 4814 C CZ . TYR B 1 235 ? 4.271 22.646 74.801 1.00 9.79 ? 316 TYR B CZ 1 ATOM 4815 O OH . TYR B 1 235 ? 5.430 21.989 74.452 1.00 8.49 ? 316 TYR B OH 1 ATOM 4816 N N . ILE B 1 236 ? -1.833 25.741 74.111 1.00 4.91 ? 317 ILE B N 1 ATOM 4817 C CA . ILE B 1 236 ? -3.284 25.876 74.099 1.00 5.61 ? 317 ILE B CA 1 ATOM 4818 C C . ILE B 1 236 ? -3.867 25.136 75.300 1.00 7.10 ? 317 ILE B C 1 ATOM 4819 O O . ILE B 1 236 ? -3.618 23.945 75.486 1.00 6.67 ? 317 ILE B O 1 ATOM 4820 C CB . ILE B 1 236 ? -3.887 25.350 72.787 1.00 6.67 ? 317 ILE B CB 1 ATOM 4821 C CG1 . ILE B 1 236 ? -3.342 26.154 71.604 1.00 5.92 ? 317 ILE B CG1 1 ATOM 4822 C CG2 . ILE B 1 236 ? -5.407 25.432 72.832 1.00 5.18 ? 317 ILE B CG2 1 ATOM 4823 C CD1 . ILE B 1 236 ? -3.774 25.630 70.247 1.00 6.54 ? 317 ILE B CD1 1 ATOM 4824 N N . CYS B 1 237 ? -4.636 25.853 76.114 1.00 7.20 ? 318 CYS B N 1 ATOM 4825 C CA . CYS B 1 237 ? -5.075 25.348 77.415 1.00 8.43 ? 318 CYS B CA 1 ATOM 4826 C C . CYS B 1 237 ? -6.257 24.384 77.355 1.00 9.69 ? 318 CYS B C 1 ATOM 4827 O O . CYS B 1 237 ? -6.478 23.612 78.288 1.00 11.50 ? 318 CYS B O 1 ATOM 4828 C CB . CYS B 1 237 ? -5.413 26.518 78.347 1.00 8.35 ? 318 CYS B CB 1 ATOM 4829 S SG . CYS B 1 237 ? -4.009 27.596 78.731 1.00 13.01 ? 318 CYS B SG 1 ATOM 4830 N N . SER B 1 238 ? -7.012 24.431 76.262 1.00 8.13 ? 319 SER B N 1 ATOM 4831 C CA . SER B 1 238 ? -8.253 23.666 76.151 1.00 8.11 ? 319 SER B CA 1 ATOM 4832 C C . SER B 1 238 ? -8.082 22.177 76.436 1.00 10.90 ? 319 SER B C 1 ATOM 4833 O O . SER B 1 238 ? -7.103 21.559 76.016 1.00 8.44 ? 319 SER B O 1 ATOM 4834 C CB . SER B 1 238 ? -8.877 23.857 74.767 1.00 12.03 ? 319 SER B CB 1 ATOM 4835 O OG . SER B 1 238 ? -10.051 23.071 74.628 1.00 10.96 ? 319 SER B OG 1 ATOM 4836 N N . GLY B 1 239 ? -9.050 21.608 77.148 1.00 12.76 ? 320 GLY B N 1 ATOM 4837 C CA . GLY B 1 239 ? -9.091 20.177 77.387 1.00 11.01 ? 320 GLY B CA 1 ATOM 4838 C C . GLY B 1 239 ? -9.512 19.436 76.132 1.00 17.00 ? 320 GLY B C 1 ATOM 4839 O O . GLY B 1 239 ? -9.532 18.205 76.096 1.00 14.52 ? 320 GLY B O 1 ATOM 4840 N N . ILE B 1 240 ? -9.867 20.197 75.101 1.00 10.66 ? 321 ILE B N 1 ATOM 4841 C CA . ILE B 1 240 ? -10.090 19.638 73.775 1.00 11.63 ? 321 ILE B CA 1 ATOM 4842 C C . ILE B 1 240 ? -8.738 19.548 73.076 1.00 10.53 ? 321 ILE B C 1 ATOM 4843 O O . ILE B 1 240 ? -8.359 20.447 72.329 1.00 13.71 ? 321 ILE B O 1 ATOM 4844 C CB . ILE B 1 240 ? -11.036 20.524 72.944 1.00 10.59 ? 321 ILE B CB 1 ATOM 4845 C CG1 . ILE B 1 240 ? -12.332 20.796 73.712 1.00 15.78 ? 321 ILE B CG1 1 ATOM 4846 C CG2 . ILE B 1 240 ? -11.335 19.880 71.594 1.00 10.45 ? 321 ILE B CG2 1 ATOM 4847 C CD1 . ILE B 1 240 ? -13.128 19.551 74.024 1.00 16.64 ? 321 ILE B CD1 1 ATOM 4848 N N . PHE B 1 241 ? -8.011 18.464 73.329 1.00 10.13 ? 322 PHE B N 1 ATOM 4849 C CA . PHE B 1 241 ? -6.634 18.332 72.855 1.00 12.41 ? 322 PHE B CA 1 ATOM 4850 C C . PHE B 1 241 ? -6.537 18.280 71.330 1.00 10.05 ? 322 PHE B C 1 ATOM 4851 O O . PHE B 1 241 ? -7.331 17.613 70.671 1.00 9.86 ? 322 PHE B O 1 ATOM 4852 C CB . PHE B 1 241 ? -5.970 17.105 73.482 1.00 8.80 ? 322 PHE B CB 1 ATOM 4853 C CG . PHE B 1 241 ? -6.131 17.031 74.975 1.00 12.87 ? 322 PHE B CG 1 ATOM 4854 C CD1 . PHE B 1 241 ? -5.534 17.973 75.798 1.00 14.09 ? 322 PHE B CD1 1 ATOM 4855 C CD2 . PHE B 1 241 ? -6.877 16.019 75.555 1.00 14.88 ? 322 PHE B CD2 1 ATOM 4856 C CE1 . PHE B 1 241 ? -5.681 17.908 77.173 1.00 14.20 ? 322 PHE B CE1 1 ATOM 4857 C CE2 . PHE B 1 241 ? -7.026 15.947 76.929 1.00 17.19 ? 322 PHE B CE2 1 ATOM 4858 C CZ . PHE B 1 241 ? -6.428 16.893 77.737 1.00 14.18 ? 322 PHE B CZ 1 ATOM 4859 N N . GLY B 1 242 ? -5.546 18.976 70.781 1.00 10.07 ? 323 GLY B N 1 ATOM 4860 C CA . GLY B 1 242 ? -5.455 19.161 69.344 1.00 7.44 ? 323 GLY B CA 1 ATOM 4861 C C . GLY B 1 242 ? -4.483 18.265 68.602 1.00 8.73 ? 323 GLY B C 1 ATOM 4862 O O . GLY B 1 242 ? -4.537 18.173 67.374 1.00 9.97 ? 323 GLY B O 1 ATOM 4863 N N . ASP B 1 243 ? -3.589 17.602 69.326 1.00 6.16 ? 324 ASP B N 1 ATOM 4864 C CA . ASP B 1 243 ? -2.585 16.774 68.668 1.00 7.28 ? 324 ASP B CA 1 ATOM 4865 C C . ASP B 1 243 ? -3.099 15.359 68.425 1.00 8.69 ? 324 ASP B C 1 ATOM 4866 O O . ASP B 1 243 ? -4.195 14.996 68.854 1.00 9.36 ? 324 ASP B O 1 ATOM 4867 C CB . ASP B 1 243 ? -1.284 16.740 69.476 1.00 8.60 ? 324 ASP B CB 1 ATOM 4868 C CG . ASP B 1 243 ? -0.055 16.536 68.602 1.00 9.31 ? 324 ASP B CG 1 ATOM 4869 O OD1 . ASP B 1 243 ? -0.198 16.364 67.376 1.00 5.80 ? 324 ASP B OD1 1 ATOM 4870 O OD2 . ASP B 1 243 ? 1.066 16.559 69.142 1.00 7.79 ? 324 ASP B OD2 1 ATOM 4871 N N . ASN B 1 244 ? -2.294 14.576 67.718 1.00 9.34 ? 325 ASN B N 1 ATOM 4872 C CA . ASN B 1 244 ? -2.574 13.170 67.471 1.00 9.22 ? 325 ASN B CA 1 ATOM 4873 C C . ASN B 1 244 ? -1.251 12.416 67.473 1.00 8.80 ? 325 ASN B C 1 ATOM 4874 O O . ASN B 1 244 ? -0.375 12.709 66.664 1.00 8.47 ? 325 ASN B O 1 ATOM 4875 C CB . ASN B 1 244 ? -3.274 13.000 66.122 1.00 8.74 ? 325 ASN B CB 1 ATOM 4876 C CG . ASN B 1 244 ? -3.676 11.563 65.848 1.00 12.20 ? 325 ASN B CG 1 ATOM 4877 O OD1 . ASN B 1 244 ? -2.965 10.826 65.166 1.00 13.38 ? 325 ASN B OD1 1 ATOM 4878 N ND2 . ASN B 1 244 ? -4.824 11.160 66.378 1.00 10.54 ? 325 ASN B ND2 1 ATOM 4879 N N . PRO B 1 245 ? -1.097 11.437 68.377 1.00 8.39 ? 326 PRO B N 1 ATOM 4880 C CA . PRO B 1 245 ? -2.109 10.944 69.318 1.00 8.80 ? 326 PRO B CA 1 ATOM 4881 C C . PRO B 1 245 ? -2.381 11.888 70.487 1.00 10.45 ? 326 PRO B C 1 ATOM 4882 O O . PRO B 1 245 ? -1.702 12.903 70.657 1.00 7.72 ? 326 PRO B O 1 ATOM 4883 C CB . PRO B 1 245 ? -1.482 9.648 69.840 1.00 11.98 ? 326 PRO B CB 1 ATOM 4884 C CG . PRO B 1 245 ? -0.023 9.908 69.779 1.00 13.11 ? 326 PRO B CG 1 ATOM 4885 C CD . PRO B 1 245 ? 0.177 10.707 68.518 1.00 10.83 ? 326 PRO B CD 1 ATOM 4886 N N . ARG B 1 246 ? -3.376 11.529 71.291 1.00 8.77 ? 327 ARG B N 1 ATOM 4887 C CA . ARG B 1 246 ? -3.789 12.326 72.438 1.00 8.12 ? 327 ARG B CA 1 ATOM 4888 C C . ARG B 1 246 ? -4.674 11.474 73.343 1.00 10.63 ? 327 ARG B C 1 ATOM 4889 O O . ARG B 1 246 ? -5.104 10.390 72.949 1.00 10.31 ? 327 ARG B O 1 ATOM 4890 C CB . ARG B 1 246 ? -4.569 13.557 71.971 1.00 8.64 ? 327 ARG B CB 1 ATOM 4891 C CG . ARG B 1 246 ? -5.847 13.219 71.217 1.00 9.31 ? 327 ARG B CG 1 ATOM 4892 C CD . ARG B 1 246 ? -6.641 14.467 70.859 1.00 6.85 ? 327 ARG B CD 1 ATOM 4893 N NE . ARG B 1 246 ? -7.891 14.132 70.180 1.00 5.81 ? 327 ARG B NE 1 ATOM 4894 C CZ . ARG B 1 246 ? -8.035 14.074 68.860 1.00 6.04 ? 327 ARG B CZ 1 ATOM 4895 N NH1 . ARG B 1 246 ? -7.009 14.340 68.062 1.00 5.18 ? 327 ARG B NH1 1 ATOM 4896 N NH2 . ARG B 1 246 ? -9.211 13.755 68.336 1.00 7.80 ? 327 ARG B NH2 1 ATOM 4897 N N . PRO B 1 247 ? -4.945 11.958 74.564 1.00 10.24 ? 328 PRO B N 1 ATOM 4898 C CA . PRO B 1 247 ? -5.899 11.280 75.447 1.00 13.58 ? 328 PRO B CA 1 ATOM 4899 C C . PRO B 1 247 ? -7.321 11.693 75.097 1.00 13.62 ? 328 PRO B C 1 ATOM 4900 O O . PRO B 1 247 ? -7.508 12.637 74.329 1.00 9.95 ? 328 PRO B O 1 ATOM 4901 C CB . PRO B 1 247 ? -5.552 11.833 76.837 1.00 15.61 ? 328 PRO B CB 1 ATOM 4902 C CG . PRO B 1 247 ? -4.292 12.644 76.665 1.00 14.62 ? 328 PRO B CG 1 ATOM 4903 C CD . PRO B 1 247 ? -4.278 13.079 75.241 1.00 11.04 ? 328 PRO B CD 1 ATOM 4904 N N . ASN B 1 248 ? -8.310 10.999 75.652 1.00 15.69 ? 329 ASN B N 1 ATOM 4905 C CA . ASN B 1 248 ? -9.690 11.459 75.571 1.00 14.52 ? 329 ASN B CA 1 ATOM 4906 C C . ASN B 1 248 ? -9.786 12.847 76.193 1.00 13.72 ? 329 ASN B C 1 ATOM 4907 O O . ASN B 1 248 ? -9.012 13.181 77.091 1.00 13.38 ? 329 ASN B O 1 ATOM 4908 C CB . ASN B 1 248 ? -10.624 10.492 76.301 1.00 18.61 ? 329 ASN B CB 1 ATOM 4909 C CG . ASN B 1 248 ? -10.743 9.148 75.601 1.00 23.50 ? 329 ASN B CG 1 ATOM 4910 O OD1 . ASN B 1 248 ? -10.932 9.081 74.388 1.00 19.38 ? 329 ASN B OD1 1 ATOM 4911 N ND2 . ASN B 1 248 ? -10.651 8.071 76.370 1.00 26.21 ? 329 ASN B ND2 1 ATOM 4912 N N . ASP B 1 249 ? -10.731 13.655 75.721 1.00 12.37 ? 330 ASP B N 1 ATOM 4913 C CA . ASP B 1 249 ? -10.891 15.013 76.233 1.00 13.46 ? 330 ASP B CA 1 ATOM 4914 C C . ASP B 1 249 ? -11.152 15.024 77.736 1.00 21.05 ? 330 ASP B C 1 ATOM 4915 O O . ASP B 1 249 ? -12.027 14.315 78.231 1.00 14.91 ? 330 ASP B O 1 ATOM 4916 C CB . ASP B 1 249 ? -12.023 15.739 75.504 1.00 16.26 ? 330 ASP B CB 1 ATOM 4917 C CG . ASP B 1 249 ? -11.690 16.033 74.056 1.00 16.37 ? 330 ASP B CG 1 ATOM 4918 O OD1 . ASP B 1 249 ? -10.487 16.053 73.712 1.00 13.19 ? 330 ASP B OD1 1 ATOM 4919 O OD2 . ASP B 1 249 ? -12.632 16.248 73.262 1.00 13.64 ? 330 ASP B OD2 1 ATOM 4920 N N . LYS B 1 250 ? -10.380 15.833 78.453 1.00 16.70 ? 331 LYS B N 1 ATOM 4921 C CA . LYS B 1 250 ? -10.547 15.996 79.892 1.00 19.86 ? 331 LYS B CA 1 ATOM 4922 C C . LYS B 1 250 ? -10.036 17.385 80.249 1.00 20.25 ? 331 LYS B C 1 ATOM 4923 O O . LYS B 1 250 ? -9.961 18.260 79.390 1.00 29.01 ? 331 LYS B O 1 ATOM 4924 C CB . LYS B 1 250 ? -9.716 14.960 80.650 1.00 16.11 ? 331 LYS B CB 1 ATOM 4925 C CG . LYS B 1 250 ? -8.256 14.912 80.232 1.00 20.22 ? 331 LYS B CG 1 ATOM 4926 C CD . LYS B 1 250 ? -7.495 13.832 80.986 1.00 32.55 ? 331 LYS B CD 1 ATOM 4927 C CE . LYS B 1 250 ? -6.062 13.716 80.485 1.00 34.74 ? 331 LYS B CE 1 ATOM 4928 N NZ . LYS B 1 250 ? -5.336 12.579 81.118 1.00 39.95 ? 331 LYS B NZ 1 ATOM 4929 N N . THR B 1 251 ? -9.687 17.591 81.513 1.00 18.64 ? 332 THR B N 1 ATOM 4930 C CA . THR B 1 251 ? -9.095 18.858 81.923 1.00 14.33 ? 332 THR B CA 1 ATOM 4931 C C . THR B 1 251 ? -7.718 19.081 81.310 1.00 17.06 ? 332 THR B C 1 ATOM 4932 O O . THR B 1 251 ? -6.850 18.216 81.393 1.00 13.28 ? 332 THR B O 1 ATOM 4933 C CB . THR B 1 251 ? -9.009 18.965 83.455 1.00 20.22 ? 332 THR B CB 1 ATOM 4934 O OG1 . THR B 1 251 ? -10.327 18.895 84.013 1.00 21.29 ? 332 THR B OG1 1 ATOM 4935 C CG2 . THR B 1 251 ? -8.365 20.283 83.857 1.00 14.58 ? 332 THR B CG2 1 ATOM 4936 N N . GLY B 1 252 ? -7.527 20.240 80.688 1.00 14.87 ? 333 GLY B N 1 ATOM 4937 C CA . GLY B 1 252 ? -6.298 20.524 79.970 1.00 12.96 ? 333 GLY B CA 1 ATOM 4938 C C . GLY B 1 252 ? -5.251 21.222 80.815 1.00 15.49 ? 333 GLY B C 1 ATOM 4939 O O . GLY B 1 252 ? -5.377 21.307 82.038 1.00 13.40 ? 333 GLY B O 1 ATOM 4940 N N . SER B 1 253 ? -4.211 21.724 80.158 1.00 13.77 ? 335 SER B N 1 ATOM 4941 C CA . SER B 1 253 ? -3.135 22.420 80.848 1.00 13.37 ? 335 SER B CA 1 ATOM 4942 C C . SER B 1 253 ? -2.547 23.524 79.985 1.00 13.80 ? 335 SER B C 1 ATOM 4943 O O . SER B 1 253 ? -2.535 23.427 78.758 1.00 12.36 ? 335 SER B O 1 ATOM 4944 C CB . SER B 1 253 ? -2.036 21.438 81.254 1.00 16.38 ? 335 SER B CB 1 ATOM 4945 O OG . SER B 1 253 ? -0.934 22.124 81.827 1.00 17.05 ? 335 SER B OG 1 ATOM 4946 N N . CYS B 1 254 ? -2.055 24.575 80.631 1.00 13.35 ? 336 CYS B N 1 ATOM 4947 C CA . CYS B 1 254 ? -1.405 25.661 79.911 1.00 16.01 ? 336 CYS B CA 1 ATOM 4948 C C . CYS B 1 254 ? 0.065 25.336 79.668 1.00 15.66 ? 336 CYS B C 1 ATOM 4949 O O . CYS B 1 254 ? 0.813 26.145 79.124 1.00 14.55 ? 336 CYS B O 1 ATOM 4950 C CB . CYS B 1 254 ? -1.578 26.986 80.654 1.00 20.56 ? 336 CYS B CB 1 ATOM 4951 S SG . CYS B 1 254 ? -3.292 27.584 80.638 1.00 34.67 ? 336 CYS B SG 1 ATOM 4952 N N . GLY B 1 255 ? 0.461 24.135 80.076 1.00 12.58 ? 339 GLY B N 1 ATOM 4953 C CA . GLY B 1 255 ? 1.770 23.598 79.755 1.00 13.33 ? 339 GLY B CA 1 ATOM 4954 C C . GLY B 1 255 ? 1.599 22.316 78.962 1.00 10.71 ? 339 GLY B C 1 ATOM 4955 O O . GLY B 1 255 ? 0.472 21.911 78.676 1.00 10.50 ? 339 GLY B O 1 ATOM 4956 N N . PRO B 1 256 ? 2.714 21.667 78.598 1.00 10.81 ? 340 PRO B N 1 ATOM 4957 C CA . PRO B 1 256 ? 2.635 20.427 77.818 1.00 11.37 ? 340 PRO B CA 1 ATOM 4958 C C . PRO B 1 256 ? 1.895 19.316 78.564 1.00 11.98 ? 340 PRO B C 1 ATOM 4959 O O . PRO B 1 256 ? 2.257 18.977 79.691 1.00 11.45 ? 340 PRO B O 1 ATOM 4960 C CB . PRO B 1 256 ? 4.107 20.037 77.609 1.00 11.21 ? 340 PRO B CB 1 ATOM 4961 C CG . PRO B 1 256 ? 4.892 20.867 78.566 1.00 12.79 ? 340 PRO B CG 1 ATOM 4962 C CD . PRO B 1 256 ? 4.101 22.103 78.830 1.00 11.96 ? 340 PRO B CD 1 ATOM 4963 N N . VAL B 1 257 ? 0.862 18.766 77.935 1.00 10.02 ? 341 VAL B N 1 ATOM 4964 C CA . VAL B 1 257 ? 0.144 17.622 78.486 1.00 11.72 ? 341 VAL B CA 1 ATOM 4965 C C . VAL B 1 257 ? 0.908 16.340 78.166 1.00 12.28 ? 341 VAL B C 1 ATOM 4966 O O . VAL B 1 257 ? 0.988 15.926 77.010 1.00 9.88 ? 341 VAL B O 1 ATOM 4967 C CB . VAL B 1 257 ? -1.284 17.530 77.917 1.00 12.39 ? 341 VAL B CB 1 ATOM 4968 C CG1 . VAL B 1 257 ? -1.976 16.264 78.404 1.00 12.84 ? 341 VAL B CG1 1 ATOM 4969 C CG2 . VAL B 1 257 ? -2.085 18.764 78.297 1.00 9.04 ? 341 VAL B CG2 1 ATOM 4970 N N . SER B 1 258 ? 1.471 15.715 79.194 1.00 12.21 ? 342 SER B N 1 ATOM 4971 C CA . SER B 1 258 ? 2.365 14.576 78.997 1.00 10.13 ? 342 SER B CA 1 ATOM 4972 C C . SER B 1 258 ? 1.658 13.318 78.492 1.00 10.27 ? 342 SER B C 1 ATOM 4973 O O . SER B 1 258 ? 2.235 12.542 77.729 1.00 14.23 ? 342 SER B O 1 ATOM 4974 C CB . SER B 1 258 ? 3.138 14.271 80.284 1.00 16.61 ? 342 SER B CB 1 ATOM 4975 O OG . SER B 1 258 ? 2.254 13.953 81.344 1.00 18.90 ? 342 SER B OG 1 ATOM 4976 N N . SER B 1 259 ? 0.415 13.116 78.915 1.00 13.30 ? 343 SER B N 1 ATOM 4977 C CA . SER B 1 259 ? -0.337 11.929 78.517 1.00 13.38 ? 343 SER B CA 1 ATOM 4978 C C . SER B 1 259 ? -0.416 11.811 76.996 1.00 15.85 ? 343 SER B C 1 ATOM 4979 O O . SER B 1 259 ? -0.921 12.710 76.326 1.00 12.29 ? 343 SER B O 1 ATOM 4980 C CB . SER B 1 259 ? -1.743 11.958 79.119 1.00 19.76 ? 343 SER B CB 1 ATOM 4981 O OG . SER B 1 259 ? -2.497 10.834 78.701 1.00 26.98 ? 343 SER B OG 1 ATOM 4982 N N . ASN B 1 260 ? 0.089 10.702 76.460 1.00 9.76 ? 344 ASN B N 1 ATOM 4983 C CA . ASN B 1 260 ? 0.114 10.480 75.013 1.00 11.26 ? 344 ASN B CA 1 ATOM 4984 C C . ASN B 1 260 ? 0.827 11.608 74.272 1.00 13.46 ? 344 ASN B C 1 ATOM 4985 O O . ASN B 1 260 ? 0.528 11.890 73.108 1.00 10.64 ? 344 ASN B O 1 ATOM 4986 C CB . ASN B 1 260 ? -1.307 10.322 74.470 1.00 12.97 ? 344 ASN B CB 1 ATOM 4987 C CG . ASN B 1 260 ? -2.079 9.219 75.166 1.00 19.13 ? 344 ASN B CG 1 ATOM 4988 O OD1 . ASN B 1 260 ? -2.958 9.484 75.986 1.00 20.34 ? 344 ASN B OD1 1 ATOM 4989 N ND2 . ASN B 1 260 ? -1.753 7.972 74.844 1.00 21.91 ? 344 ASN B ND2 1 ATOM 4990 N N . GLY B 1 261 ? 1.777 12.241 74.953 1.00 13.52 ? 345 GLY B N 1 ATOM 4991 C CA . GLY B 1 261 ? 2.435 13.430 74.444 1.00 10.69 ? 345 GLY B CA 1 ATOM 4992 C C . GLY B 1 261 ? 3.508 13.193 73.398 1.00 11.41 ? 345 GLY B C 1 ATOM 4993 O O . GLY B 1 261 ? 3.781 14.071 72.587 1.00 7.73 ? 345 GLY B O 1 ATOM 4994 N N . ALA B 1 262 ? 4.134 12.021 73.419 1.00 11.97 ? 346 ALA B N 1 ATOM 4995 C CA . ALA B 1 262 ? 5.153 11.703 72.423 1.00 12.36 ? 346 ALA B CA 1 ATOM 4996 C C . ALA B 1 262 ? 4.518 11.582 71.039 1.00 10.06 ? 346 ALA B C 1 ATOM 4997 O O . ALA B 1 262 ? 3.330 11.287 70.923 1.00 8.16 ? 346 ALA B O 1 ATOM 4998 C CB . ALA B 1 262 ? 5.877 10.419 72.790 1.00 14.33 ? 346 ALA B CB 1 ATOM 4999 N N . ASN B 1 263 ? 5.318 11.804 69.999 1.00 11.03 ? 347 ASN B N 1 ATOM 5000 C CA . ASN B 1 263 ? 4.842 11.740 68.617 1.00 12.42 ? 347 ASN B CA 1 ATOM 5001 C C . ASN B 1 263 ? 3.884 12.892 68.336 1.00 9.15 ? 347 ASN B C 1 ATOM 5002 O O . ASN B 1 263 ? 3.807 13.826 69.119 1.00 7.16 ? 347 ASN B O 1 ATOM 5003 C CB . ASN B 1 263 ? 4.177 10.392 68.328 1.00 12.26 ? 347 ASN B CB 1 ATOM 5004 C CG . ASN B 1 263 ? 4.094 10.087 66.845 1.00 31.84 ? 347 ASN B CG 1 ATOM 5005 O OD1 . ASN B 1 263 ? 4.522 10.886 66.010 1.00 28.06 ? 347 ASN B OD1 1 ATOM 5006 N ND2 . ASN B 1 263 ? 3.546 8.924 66.508 1.00 34.46 ? 347 ASN B ND2 1 ATOM 5007 N N . GLY B 1 264 ? 3.166 12.844 67.220 1.00 6.38 ? 348 GLY B N 1 ATOM 5008 C CA . GLY B 1 264 ? 2.229 13.909 66.902 1.00 4.41 ? 348 GLY B CA 1 ATOM 5009 C C . GLY B 1 264 ? 1.905 14.020 65.425 1.00 5.46 ? 348 GLY B C 1 ATOM 5010 O O . GLY B 1 264 ? 2.203 13.120 64.645 1.00 4.32 ? 348 GLY B O 1 ATOM 5011 N N . VAL B 1 265 ? 1.282 15.133 65.050 1.00 5.77 ? 349 VAL B N 1 ATOM 5012 C CA . VAL B 1 265 ? 0.971 15.416 63.655 1.00 6.56 ? 349 VAL B CA 1 ATOM 5013 C C . VAL B 1 265 ? 0.944 16.927 63.448 1.00 6.93 ? 349 VAL B C 1 ATOM 5014 O O . VAL B 1 265 ? 0.579 17.673 64.356 1.00 6.44 ? 349 VAL B O 1 ATOM 5015 C CB . VAL B 1 265 ? -0.386 14.804 63.239 1.00 5.74 ? 349 VAL B CB 1 ATOM 5016 C CG1 . VAL B 1 265 ? -1.541 15.534 63.925 1.00 5.59 ? 349 VAL B CG1 1 ATOM 5017 C CG2 . VAL B 1 265 ? -0.548 14.836 61.723 1.00 5.91 ? 349 VAL B CG2 1 ATOM 5018 N N . LYS B 1 266 ? 1.350 17.387 62.270 1.00 6.64 ? 350 LYS B N 1 ATOM 5019 C CA . LYS B 1 266 ? 1.250 18.812 61.976 1.00 5.39 ? 350 LYS B CA 1 ATOM 5020 C C . LYS B 1 266 ? -0.210 19.239 62.017 1.00 6.13 ? 350 LYS B C 1 ATOM 5021 O O . LYS B 1 266 ? -1.079 18.554 61.475 1.00 5.74 ? 350 LYS B O 1 ATOM 5022 C CB . LYS B 1 266 ? 1.841 19.147 60.607 1.00 5.94 ? 350 LYS B CB 1 ATOM 5023 C CG . LYS B 1 266 ? 1.643 20.608 60.221 1.00 7.03 ? 350 LYS B CG 1 ATOM 5024 C CD . LYS B 1 266 ? 2.256 20.932 58.870 1.00 8.99 ? 350 LYS B CD 1 ATOM 5025 C CE . LYS B 1 266 ? 1.940 22.365 58.461 1.00 9.02 ? 350 LYS B CE 1 ATOM 5026 N NZ . LYS B 1 266 ? 2.468 23.361 59.436 1.00 5.99 ? 350 LYS B NZ 1 ATOM 5027 N N . GLY B 1 267 ? -0.471 20.371 62.662 1.00 5.73 ? 351 GLY B N 1 ATOM 5028 C CA . GLY B 1 267 ? -1.813 20.909 62.752 1.00 7.97 ? 351 GLY B CA 1 ATOM 5029 C C . GLY B 1 267 ? -1.823 22.420 62.878 1.00 6.88 ? 351 GLY B C 1 ATOM 5030 O O . GLY B 1 267 ? -0.795 23.079 62.700 1.00 8.86 ? 351 GLY B O 1 ATOM 5031 N N . PHE B 1 268 ? -2.991 22.972 63.192 1.00 6.43 ? 352 PHE B N 1 ATOM 5032 C CA . PHE B 1 268 ? -3.158 24.415 63.290 1.00 6.51 ? 352 PHE B CA 1 ATOM 5033 C C . PHE B 1 268 ? -4.291 24.755 64.253 1.00 5.87 ? 352 PHE B C 1 ATOM 5034 O O . PHE B 1 268 ? -5.056 23.883 64.662 1.00 7.46 ? 352 PHE B O 1 ATOM 5035 C CB . PHE B 1 268 ? -3.506 24.985 61.916 1.00 6.68 ? 352 PHE B CB 1 ATOM 5036 C CG . PHE B 1 268 ? -4.900 24.648 61.474 1.00 6.50 ? 352 PHE B CG 1 ATOM 5037 C CD1 . PHE B 1 268 ? -5.168 23.444 60.846 1.00 7.04 ? 352 PHE B CD1 1 ATOM 5038 C CD2 . PHE B 1 268 ? -5.948 25.521 61.716 1.00 5.65 ? 352 PHE B CD2 1 ATOM 5039 C CE1 . PHE B 1 268 ? -6.453 23.122 60.453 1.00 5.58 ? 352 PHE B CE1 1 ATOM 5040 C CE2 . PHE B 1 268 ? -7.238 25.201 61.325 1.00 7.90 ? 352 PHE B CE2 1 ATOM 5041 C CZ . PHE B 1 268 ? -7.488 24.003 60.694 1.00 5.29 ? 352 PHE B CZ 1 ATOM 5042 N N . SER B 1 269 ? -4.395 26.034 64.596 1.00 5.05 ? 353 SER B N 1 ATOM 5043 C CA . SER B 1 269 ? -5.541 26.567 65.323 1.00 7.41 ? 353 SER B CA 1 ATOM 5044 C C . SER B 1 269 ? -5.607 28.070 65.091 1.00 8.31 ? 353 SER B C 1 ATOM 5045 O O . SER B 1 269 ? -4.581 28.708 64.856 1.00 8.41 ? 353 SER B O 1 ATOM 5046 C CB . SER B 1 269 ? -5.432 26.269 66.821 1.00 9.65 ? 353 SER B CB 1 ATOM 5047 O OG . SER B 1 269 ? -5.617 24.888 67.081 1.00 8.59 ? 353 SER B OG 1 ATOM 5048 N N . PHE B 1 270 ? -6.810 28.633 65.149 1.00 5.66 ? 354 PHE B N 1 ATOM 5049 C CA . PHE B 1 270 ? -6.980 30.073 64.997 1.00 4.70 ? 354 PHE B CA 1 ATOM 5050 C C . PHE B 1 270 ? -7.409 30.704 66.317 1.00 8.23 ? 354 PHE B C 1 ATOM 5051 O O . PHE B 1 270 ? -8.408 30.302 66.910 1.00 8.89 ? 354 PHE B O 1 ATOM 5052 C CB . PHE B 1 270 ? -8.005 30.396 63.906 1.00 5.63 ? 354 PHE B CB 1 ATOM 5053 C CG . PHE B 1 270 ? -7.531 30.088 62.510 1.00 7.73 ? 354 PHE B CG 1 ATOM 5054 C CD1 . PHE B 1 270 ? -6.567 30.876 61.902 1.00 5.59 ? 354 PHE B CD1 1 ATOM 5055 C CD2 . PHE B 1 270 ? -8.063 29.022 61.801 1.00 6.20 ? 354 PHE B CD2 1 ATOM 5056 C CE1 . PHE B 1 270 ? -6.134 30.597 60.612 1.00 8.36 ? 354 PHE B CE1 1 ATOM 5057 C CE2 . PHE B 1 270 ? -7.636 28.740 60.515 1.00 4.75 ? 354 PHE B CE2 1 ATOM 5058 C CZ . PHE B 1 270 ? -6.672 29.527 59.921 1.00 5.08 ? 354 PHE B CZ 1 ATOM 5059 N N . LYS B 1 271 ? -6.648 31.695 66.767 1.00 5.29 ? 355 LYS B N 1 ATOM 5060 C CA . LYS B 1 271 ? -6.921 32.366 68.029 1.00 5.14 ? 355 LYS B CA 1 ATOM 5061 C C . LYS B 1 271 ? -7.855 33.556 67.833 1.00 7.85 ? 355 LYS B C 1 ATOM 5062 O O . LYS B 1 271 ? -7.661 34.372 66.931 1.00 7.64 ? 355 LYS B O 1 ATOM 5063 C CB . LYS B 1 271 ? -5.609 32.826 68.677 1.00 7.16 ? 355 LYS B CB 1 ATOM 5064 C CG . LYS B 1 271 ? -5.772 33.576 69.993 1.00 6.61 ? 355 LYS B CG 1 ATOM 5065 C CD . LYS B 1 271 ? -4.437 34.142 70.464 1.00 11.33 ? 355 LYS B CD 1 ATOM 5066 C CE . LYS B 1 271 ? -4.523 34.728 71.871 1.00 14.44 ? 355 LYS B CE 1 ATOM 5067 N NZ . LYS B 1 271 ? -5.381 35.943 71.946 1.00 8.22 ? 355 LYS B NZ 1 ATOM 5068 N N . TYR B 1 272 ? -8.875 33.638 68.681 1.00 5.75 ? 356 TYR B N 1 ATOM 5069 C CA . TYR B 1 272 ? -9.781 34.779 68.705 1.00 7.96 ? 356 TYR B CA 1 ATOM 5070 C C . TYR B 1 272 ? -9.996 35.204 70.154 1.00 8.46 ? 356 TYR B C 1 ATOM 5071 O O . TYR B 1 272 ? -10.882 34.688 70.832 1.00 8.18 ? 356 TYR B O 1 ATOM 5072 C CB . TYR B 1 272 ? -11.125 34.417 68.071 1.00 10.33 ? 356 TYR B CB 1 ATOM 5073 C CG . TYR B 1 272 ? -11.083 34.239 66.570 1.00 9.58 ? 356 TYR B CG 1 ATOM 5074 C CD1 . TYR B 1 272 ? -10.787 33.005 66.004 1.00 6.36 ? 356 TYR B CD1 1 ATOM 5075 C CD2 . TYR B 1 272 ? -11.347 35.304 65.719 1.00 10.08 ? 356 TYR B CD2 1 ATOM 5076 C CE1 . TYR B 1 272 ? -10.753 32.838 64.630 1.00 6.54 ? 356 TYR B CE1 1 ATOM 5077 C CE2 . TYR B 1 272 ? -11.315 35.147 64.345 1.00 11.56 ? 356 TYR B CE2 1 ATOM 5078 C CZ . TYR B 1 272 ? -11.017 33.913 63.807 1.00 12.69 ? 356 TYR B CZ 1 ATOM 5079 O OH . TYR B 1 272 ? -10.986 33.751 62.439 1.00 15.08 ? 356 TYR B OH 1 ATOM 5080 N N . GLY B 1 273 ? -9.182 36.140 70.627 1.00 11.91 ? 357 GLY B N 1 ATOM 5081 C CA . GLY B 1 273 ? -9.224 36.520 72.027 1.00 12.65 ? 357 GLY B CA 1 ATOM 5082 C C . GLY B 1 273 ? -8.888 35.322 72.896 1.00 8.94 ? 357 GLY B C 1 ATOM 5083 O O . GLY B 1 273 ? -7.837 34.707 72.729 1.00 11.87 ? 357 GLY B O 1 ATOM 5084 N N . ASN B 1 274 ? -9.781 34.983 73.822 1.00 7.53 ? 358 ASN B N 1 ATOM 5085 C CA . ASN B 1 274 ? -9.583 33.813 74.674 1.00 8.20 ? 358 ASN B CA 1 ATOM 5086 C C . ASN B 1 274 ? -10.088 32.531 74.016 1.00 7.45 ? 358 ASN B C 1 ATOM 5087 O O . ASN B 1 274 ? -9.892 31.435 74.540 1.00 7.03 ? 358 ASN B O 1 ATOM 5088 C CB . ASN B 1 274 ? -10.264 34.007 76.034 1.00 8.71 ? 358 ASN B CB 1 ATOM 5089 C CG . ASN B 1 274 ? -9.660 35.144 76.832 1.00 13.99 ? 358 ASN B CG 1 ATOM 5090 O OD1 . ASN B 1 274 ? -10.084 36.294 76.713 1.00 12.08 ? 358 ASN B OD1 1 ATOM 5091 N ND2 . ASN B 1 274 ? -8.665 34.828 77.656 1.00 13.49 ? 358 ASN B ND2 1 ATOM 5092 N N . GLY B 1 275 ? -10.734 32.679 72.863 1.00 8.56 ? 359 GLY B N 1 ATOM 5093 C CA . GLY B 1 275 ? -11.297 31.550 72.143 1.00 7.57 ? 359 GLY B CA 1 ATOM 5094 C C . GLY B 1 275 ? -10.377 30.996 71.070 1.00 8.42 ? 359 GLY B C 1 ATOM 5095 O O . GLY B 1 275 ? -9.349 31.593 70.743 1.00 5.44 ? 359 GLY B O 1 ATOM 5096 N N . VAL B 1 276 ? -10.750 29.847 70.519 1.00 7.46 ? 360 VAL B N 1 ATOM 5097 C CA . VAL B 1 276 ? -9.910 29.178 69.536 1.00 5.97 ? 360 VAL B CA 1 ATOM 5098 C C . VAL B 1 276 ? -10.715 28.264 68.617 1.00 7.87 ? 360 VAL B C 1 ATOM 5099 O O . VAL B 1 276 ? -11.596 27.531 69.071 1.00 6.60 ? 360 VAL B O 1 ATOM 5100 C CB . VAL B 1 276 ? -8.797 28.356 70.225 1.00 6.07 ? 360 VAL B CB 1 ATOM 5101 C CG1 . VAL B 1 276 ? -9.400 27.294 71.132 1.00 7.03 ? 360 VAL B CG1 1 ATOM 5102 C CG2 . VAL B 1 276 ? -7.875 27.723 69.190 1.00 7.63 ? 360 VAL B CG2 1 ATOM 5103 N N . TRP B 1 277 ? -10.422 28.336 67.321 1.00 6.20 ? 361 TRP B N 1 ATOM 5104 C CA . TRP B 1 277 ? -10.910 27.350 66.368 1.00 5.92 ? 361 TRP B CA 1 ATOM 5105 C C . TRP B 1 277 ? -9.868 26.248 66.259 1.00 9.01 ? 361 TRP B C 1 ATOM 5106 O O . TRP B 1 277 ? -8.746 26.487 65.814 1.00 7.23 ? 361 TRP B O 1 ATOM 5107 C CB . TRP B 1 277 ? -11.137 27.974 64.988 1.00 6.95 ? 361 TRP B CB 1 ATOM 5108 C CG . TRP B 1 277 ? -12.522 28.513 64.760 1.00 4.70 ? 361 TRP B CG 1 ATOM 5109 C CD1 . TRP B 1 277 ? -12.895 29.826 64.719 1.00 5.74 ? 361 TRP B CD1 1 ATOM 5110 C CD2 . TRP B 1 277 ? -13.715 27.750 64.530 1.00 5.48 ? 361 TRP B CD2 1 ATOM 5111 N NE1 . TRP B 1 277 ? -14.245 29.928 64.480 1.00 6.88 ? 361 TRP B NE1 1 ATOM 5112 C CE2 . TRP B 1 277 ? -14.772 28.668 64.361 1.00 6.06 ? 361 TRP B CE2 1 ATOM 5113 C CE3 . TRP B 1 277 ? -13.992 26.382 64.453 1.00 4.90 ? 361 TRP B CE3 1 ATOM 5114 C CZ2 . TRP B 1 277 ? -16.083 28.262 64.118 1.00 6.59 ? 361 TRP B CZ2 1 ATOM 5115 C CZ3 . TRP B 1 277 ? -15.294 25.980 64.213 1.00 6.02 ? 361 TRP B CZ3 1 ATOM 5116 C CH2 . TRP B 1 277 ? -16.323 26.917 64.048 1.00 7.27 ? 361 TRP B CH2 1 ATOM 5117 N N . ILE B 1 278 ? -10.238 25.043 66.673 1.00 5.71 ? 362 ILE B N 1 ATOM 5118 C CA . ILE B 1 278 ? -9.318 23.915 66.660 1.00 7.68 ? 362 ILE B CA 1 ATOM 5119 C C . ILE B 1 278 ? -9.654 22.956 65.528 1.00 6.78 ? 362 ILE B C 1 ATOM 5120 O O . ILE B 1 278 ? -10.790 22.502 65.408 1.00 8.98 ? 362 ILE B O 1 ATOM 5121 C CB . ILE B 1 278 ? -9.377 23.138 67.989 1.00 7.39 ? 362 ILE B CB 1 ATOM 5122 C CG1 . ILE B 1 278 ? -8.945 24.034 69.150 1.00 10.18 ? 362 ILE B CG1 1 ATOM 5123 C CG2 . ILE B 1 278 ? -8.512 21.888 67.920 1.00 7.94 ? 362 ILE B CG2 1 ATOM 5124 C CD1 . ILE B 1 278 ? -9.243 23.443 70.515 1.00 16.13 ? 362 ILE B CD1 1 ATOM 5125 N N . GLY B 1 279 ? -8.663 22.662 64.693 1.00 8.62 ? 363 GLY B N 1 ATOM 5126 C CA . GLY B 1 279 ? -8.787 21.603 63.710 1.00 6.86 ? 363 GLY B CA 1 ATOM 5127 C C . GLY B 1 279 ? -8.041 20.389 64.223 1.00 7.71 ? 363 GLY B C 1 ATOM 5128 O O . GLY B 1 279 ? -6.913 20.514 64.698 1.00 8.83 ? 363 GLY B O 1 ATOM 5129 N N . ARG B 1 280 ? -8.662 19.217 64.149 1.00 6.13 ? 364 ARG B N 1 ATOM 5130 C CA . ARG B 1 280 ? -8.015 18.008 64.651 1.00 6.04 ? 364 ARG B CA 1 ATOM 5131 C C . ARG B 1 280 ? -8.596 16.739 64.043 1.00 6.86 ? 364 ARG B C 1 ATOM 5132 O O . ARG B 1 280 ? -9.682 16.752 63.463 1.00 5.67 ? 364 ARG B O 1 ATOM 5133 C CB . ARG B 1 280 ? -8.110 17.939 66.180 1.00 6.66 ? 364 ARG B CB 1 ATOM 5134 C CG . ARG B 1 280 ? -9.504 17.625 66.713 1.00 6.44 ? 364 ARG B CG 1 ATOM 5135 C CD . ARG B 1 280 ? -9.493 17.464 68.233 1.00 5.20 ? 364 ARG B CD 1 ATOM 5136 N NE . ARG B 1 280 ? -10.795 17.045 68.750 1.00 8.00 ? 364 ARG B NE 1 ATOM 5137 C CZ . ARG B 1 280 ? -11.029 16.723 70.019 1.00 10.85 ? 364 ARG B CZ 1 ATOM 5138 N NH1 . ARG B 1 280 ? -10.047 16.769 70.910 1.00 6.80 ? 364 ARG B NH1 1 ATOM 5139 N NH2 . ARG B 1 280 ? -12.247 16.353 70.397 1.00 10.68 ? 364 ARG B NH2 1 ATOM 5140 N N . THR B 1 281 ? -7.858 15.642 64.176 1.00 7.95 ? 365 THR B N 1 ATOM 5141 C CA . THR B 1 281 ? -8.348 14.339 63.755 1.00 7.65 ? 365 THR B CA 1 ATOM 5142 C C . THR B 1 281 ? -9.517 13.946 64.644 1.00 8.82 ? 365 THR B C 1 ATOM 5143 O O . THR B 1 281 ? -9.692 14.500 65.730 1.00 9.28 ? 365 THR B O 1 ATOM 5144 C CB . THR B 1 281 ? -7.260 13.261 63.884 1.00 8.57 ? 365 THR B CB 1 ATOM 5145 O OG1 . THR B 1 281 ? -6.881 13.131 65.259 1.00 9.10 ? 365 THR B OG1 1 ATOM 5146 C CG2 . THR B 1 281 ? -6.035 13.627 63.060 1.00 11.27 ? 365 THR B CG2 1 ATOM 5147 N N . LYS B 1 282 ? -10.320 12.992 64.187 1.00 7.96 ? 366 LYS B N 1 ATOM 5148 C CA . LYS B 1 282 ? -11.417 12.483 65.001 1.00 9.28 ? 366 LYS B CA 1 ATOM 5149 C C . LYS B 1 282 ? -10.937 11.367 65.922 1.00 10.15 ? 366 LYS B C 1 ATOM 5150 O O . LYS B 1 282 ? -11.417 11.231 67.045 1.00 9.43 ? 366 LYS B O 1 ATOM 5151 C CB . LYS B 1 282 ? -12.575 12.003 64.124 1.00 10.11 ? 366 LYS B CB 1 ATOM 5152 C CG . LYS B 1 282 ? -13.413 13.133 63.538 1.00 10.12 ? 366 LYS B CG 1 ATOM 5153 C CD . LYS B 1 282 ? -14.569 12.596 62.711 1.00 10.99 ? 366 LYS B CD 1 ATOM 5154 C CE . LYS B 1 282 ? -15.533 13.706 62.308 1.00 11.81 ? 366 LYS B CE 1 ATOM 5155 N NZ . LYS B 1 282 ? -16.197 14.318 63.497 1.00 13.67 ? 366 LYS B NZ 1 ATOM 5156 N N . SER B 1 283 ? -9.984 10.572 65.443 1.00 9.07 ? 367 SER B N 1 ATOM 5157 C CA . SER B 1 283 ? -9.396 9.512 66.257 1.00 10.00 ? 367 SER B CA 1 ATOM 5158 C C . SER B 1 283 ? -8.347 10.086 67.201 1.00 8.94 ? 367 SER B C 1 ATOM 5159 O O . SER B 1 283 ? -7.594 10.981 66.825 1.00 7.49 ? 367 SER B O 1 ATOM 5160 C CB . SER B 1 283 ? -8.764 8.438 65.371 1.00 9.63 ? 367 SER B CB 1 ATOM 5161 O OG . SER B 1 283 ? -8.005 7.527 66.149 1.00 11.20 ? 367 SER B OG 1 ATOM 5162 N N . ILE B 1 284 ? -8.301 9.573 68.427 1.00 10.06 ? 368 ILE B N 1 ATOM 5163 C CA . ILE B 1 284 ? -7.315 10.038 69.395 1.00 10.11 ? 368 ILE B CA 1 ATOM 5164 C C . ILE B 1 284 ? -5.978 9.318 69.236 1.00 10.92 ? 368 ILE B C 1 ATOM 5165 O O . ILE B 1 284 ? -4.964 9.759 69.774 1.00 12.84 ? 368 ILE B O 1 ATOM 5166 C CB . ILE B 1 284 ? -7.798 9.857 70.850 1.00 11.77 ? 368 ILE B CB 1 ATOM 5167 C CG1 . ILE B 1 284 ? -7.816 8.374 71.229 1.00 11.21 ? 368 ILE B CG1 1 ATOM 5168 C CG2 . ILE B 1 284 ? -9.164 10.500 71.049 1.00 9.79 ? 368 ILE B CG2 1 ATOM 5169 C CD1 . ILE B 1 284 ? -8.109 8.123 72.696 1.00 16.06 ? 368 ILE B CD1 1 ATOM 5170 N N . SER B 1 285 ? -5.977 8.216 68.492 1.00 9.15 ? 369 SER B N 1 ATOM 5171 C CA . SER B 1 285 ? -4.797 7.357 68.417 1.00 10.68 ? 369 SER B CA 1 ATOM 5172 C C . SER B 1 285 ? -4.206 7.214 67.013 1.00 16.13 ? 369 SER B C 1 ATOM 5173 O O . SER B 1 285 ? -3.075 6.752 66.855 1.00 16.69 ? 369 SER B O 1 ATOM 5174 C CB . SER B 1 285 ? -5.119 5.972 68.983 1.00 15.07 ? 369 SER B CB 1 ATOM 5175 O OG . SER B 1 285 ? -6.194 5.373 68.281 1.00 16.68 ? 369 SER B OG 1 ATOM 5176 N N . SER B 1 286 ? -4.966 7.606 65.997 1.00 12.47 ? 370 SER B N 1 ATOM 5177 C CA . SER B 1 286 ? -4.528 7.423 64.616 1.00 12.37 ? 370 SER B CA 1 ATOM 5178 C C . SER B 1 286 ? -4.915 8.612 63.741 1.00 9.46 ? 370 SER B C 1 ATOM 5179 O O . SER B 1 286 ? -5.788 9.398 64.100 1.00 9.25 ? 370 SER B O 1 ATOM 5180 C CB . SER B 1 286 ? -5.121 6.133 64.045 1.00 17.20 ? 370 SER B CB 1 ATOM 5181 O OG . SER B 1 286 ? -4.611 5.862 62.753 1.00 29.84 ? 370 SER B OG 1 ATOM 5182 N N . ARG B 1 287 ? -4.264 8.737 62.588 1.00 8.18 ? 371 ARG B N 1 ATOM 5183 C CA . ARG B 1 287 ? -4.553 9.835 61.672 1.00 8.91 ? 371 ARG B CA 1 ATOM 5184 C C . ARG B 1 287 ? -5.798 9.545 60.833 1.00 8.52 ? 371 ARG B C 1 ATOM 5185 O O . ARG B 1 287 ? -5.718 9.329 59.621 1.00 8.83 ? 371 ARG B O 1 ATOM 5186 C CB . ARG B 1 287 ? -3.332 10.147 60.800 1.00 6.46 ? 371 ARG B CB 1 ATOM 5187 C CG . ARG B 1 287 ? -2.164 10.718 61.602 1.00 8.36 ? 371 ARG B CG 1 ATOM 5188 C CD . ARG B 1 287 ? -0.877 10.815 60.794 1.00 9.69 ? 371 ARG B CD 1 ATOM 5189 N NE . ARG B 1 287 ? 0.209 11.384 61.592 1.00 9.08 ? 371 ARG B NE 1 ATOM 5190 C CZ . ARG B 1 287 ? 1.420 11.665 61.124 1.00 12.57 ? 371 ARG B CZ 1 ATOM 5191 N NH1 . ARG B 1 287 ? 1.714 11.429 59.852 1.00 6.17 ? 371 ARG B NH1 1 ATOM 5192 N NH2 . ARG B 1 287 ? 2.339 12.186 61.929 1.00 8.22 ? 371 ARG B NH2 1 ATOM 5193 N N . ASN B 1 288 ? -6.947 9.544 61.504 1.00 9.66 ? 372 ASN B N 1 ATOM 5194 C CA . ASN B 1 288 ? -8.232 9.279 60.869 1.00 8.66 ? 372 ASN B CA 1 ATOM 5195 C C . ASN B 1 288 ? -9.253 10.357 61.194 1.00 10.13 ? 372 ASN B C 1 ATOM 5196 O O . ASN B 1 288 ? -9.360 10.797 62.340 1.00 7.98 ? 372 ASN B O 1 ATOM 5197 C CB . ASN B 1 288 ? -8.779 7.919 61.310 1.00 13.69 ? 372 ASN B CB 1 ATOM 5198 C CG . ASN B 1 288 ? -8.036 6.759 60.684 1.00 16.78 ? 372 ASN B CG 1 ATOM 5199 O OD1 . ASN B 1 288 ? -8.415 6.266 59.620 1.00 22.91 ? 372 ASN B OD1 1 ATOM 5200 N ND2 . ASN B 1 288 ? -6.976 6.312 61.341 1.00 15.78 ? 372 ASN B ND2 1 ATOM 5201 N N . GLY B 1 289 ? -10.004 10.776 60.182 1.00 7.92 ? 373 GLY B N 1 ATOM 5202 C CA . GLY B 1 289 ? -11.056 11.756 60.365 1.00 6.57 ? 373 GLY B CA 1 ATOM 5203 C C . GLY B 1 289 ? -10.521 13.157 60.579 1.00 5.83 ? 373 GLY B C 1 ATOM 5204 O O . GLY B 1 289 ? -9.329 13.354 60.808 1.00 5.77 ? 373 GLY B O 1 ATOM 5205 N N . PHE B 1 290 ? -11.410 14.138 60.496 1.00 6.64 ? 374 PHE B N 1 ATOM 5206 C CA . PHE B 1 290 ? -11.041 15.518 60.776 1.00 5.18 ? 374 PHE B CA 1 ATOM 5207 C C . PHE B 1 290 ? -12.275 16.330 61.124 1.00 5.54 ? 374 PHE B C 1 ATOM 5208 O O . PHE B 1 290 ? -13.358 16.095 60.589 1.00 6.67 ? 374 PHE B O 1 ATOM 5209 C CB . PHE B 1 290 ? -10.307 16.146 59.589 1.00 4.38 ? 374 PHE B CB 1 ATOM 5210 C CG . PHE B 1 290 ? -9.431 17.306 59.970 1.00 4.21 ? 374 PHE B CG 1 ATOM 5211 C CD1 . PHE B 1 290 ? -8.149 17.091 60.448 1.00 4.58 ? 374 PHE B CD1 1 ATOM 5212 C CD2 . PHE B 1 290 ? -9.892 18.608 59.863 1.00 5.29 ? 374 PHE B CD2 1 ATOM 5213 C CE1 . PHE B 1 290 ? -7.336 18.154 60.805 1.00 7.35 ? 374 PHE B CE1 1 ATOM 5214 C CE2 . PHE B 1 290 ? -9.084 19.678 60.220 1.00 5.14 ? 374 PHE B CE2 1 ATOM 5215 C CZ . PHE B 1 290 ? -7.806 19.450 60.692 1.00 5.65 ? 374 PHE B CZ 1 ATOM 5216 N N . GLU B 1 291 ? -12.105 17.285 62.030 1.00 5.78 ? 375 GLU B N 1 ATOM 5217 C CA . GLU B 1 291 ? -13.213 18.105 62.489 1.00 6.44 ? 375 GLU B CA 1 ATOM 5218 C C . GLU B 1 291 ? -12.721 19.483 62.902 1.00 7.19 ? 375 GLU B C 1 ATOM 5219 O O . GLU B 1 291 ? -11.561 19.646 63.283 1.00 7.48 ? 375 GLU B O 1 ATOM 5220 C CB . GLU B 1 291 ? -13.919 17.430 63.669 1.00 6.45 ? 375 GLU B CB 1 ATOM 5221 C CG . GLU B 1 291 ? -13.020 17.177 64.874 1.00 9.83 ? 375 GLU B CG 1 ATOM 5222 C CD . GLU B 1 291 ? -13.695 16.324 65.932 1.00 13.17 ? 375 GLU B CD 1 ATOM 5223 O OE1 . GLU B 1 291 ? -14.708 15.667 65.611 1.00 14.47 ? 375 GLU B OE1 1 ATOM 5224 O OE2 . GLU B 1 291 ? -13.208 16.305 67.082 1.00 13.45 ? 375 GLU B OE2 1 ATOM 5225 N N . MET B 1 292 ? -13.608 20.469 62.814 1.00 6.14 ? 376 MET B N 1 ATOM 5226 C CA . MET B 1 292 ? -13.326 21.813 63.306 1.00 8.13 ? 376 MET B CA 1 ATOM 5227 C C . MET B 1 292 ? -14.175 22.092 64.540 1.00 8.92 ? 376 MET B C 1 ATOM 5228 O O . MET B 1 292 ? -15.382 21.862 64.536 1.00 7.61 ? 376 MET B O 1 ATOM 5229 C CB . MET B 1 292 ? -13.610 22.860 62.228 1.00 6.97 ? 376 MET B CB 1 ATOM 5230 C CG . MET B 1 292 ? -12.659 22.812 61.040 1.00 8.52 ? 376 MET B CG 1 ATOM 5231 S SD . MET B 1 292 ? -10.947 23.149 61.508 1.00 10.91 ? 376 MET B SD 1 ATOM 5232 C CE . MET B 1 292 ? -11.065 24.849 62.065 1.00 7.94 ? 376 MET B CE 1 ATOM 5233 N N . ILE B 1 293 ? -13.537 22.587 65.594 1.00 6.47 ? 377 ILE B N 1 ATOM 5234 C CA . ILE B 1 293 ? -14.223 22.832 66.856 1.00 7.78 ? 377 ILE B CA 1 ATOM 5235 C C . ILE B 1 293 ? -14.019 24.264 67.328 1.00 7.49 ? 377 ILE B C 1 ATOM 5236 O O . ILE B 1 293 ? -12.890 24.745 67.399 1.00 6.85 ? 377 ILE B O 1 ATOM 5237 C CB . ILE B 1 293 ? -13.731 21.868 67.950 1.00 8.02 ? 377 ILE B CB 1 ATOM 5238 C CG1 . ILE B 1 293 ? -14.112 20.429 67.597 1.00 11.80 ? 377 ILE B CG1 1 ATOM 5239 C CG2 . ILE B 1 293 ? -14.307 22.258 69.304 1.00 6.72 ? 377 ILE B CG2 1 ATOM 5240 C CD1 . ILE B 1 293 ? -13.644 19.408 68.605 1.00 14.93 ? 377 ILE B CD1 1 ATOM 5241 N N . TRP B 1 294 ? -15.117 24.946 67.639 1.00 6.32 ? 378 TRP B N 1 ATOM 5242 C CA . TRP B 1 294 ? -15.037 26.289 68.198 1.00 8.13 ? 378 TRP B CA 1 ATOM 5243 C C . TRP B 1 294 ? -15.161 26.243 69.713 1.00 7.76 ? 378 TRP B C 1 ATOM 5244 O O . TRP B 1 294 ? -16.192 25.840 70.253 1.00 8.33 ? 378 TRP B O 1 ATOM 5245 C CB . TRP B 1 294 ? -16.113 27.203 67.611 1.00 7.94 ? 378 TRP B CB 1 ATOM 5246 C CG . TRP B 1 294 ? -16.275 28.500 68.365 1.00 8.66 ? 378 TRP B CG 1 ATOM 5247 C CD1 . TRP B 1 294 ? -17.388 28.922 69.036 1.00 12.48 ? 378 TRP B CD1 1 ATOM 5248 C CD2 . TRP B 1 294 ? -15.292 29.532 68.531 1.00 10.04 ? 378 TRP B CD2 1 ATOM 5249 N NE1 . TRP B 1 294 ? -17.160 30.153 69.604 1.00 11.44 ? 378 TRP B NE1 1 ATOM 5250 C CE2 . TRP B 1 294 ? -15.882 30.550 69.309 1.00 10.01 ? 378 TRP B CE2 1 ATOM 5251 C CE3 . TRP B 1 294 ? -13.971 29.697 68.096 1.00 8.66 ? 378 TRP B CE3 1 ATOM 5252 C CZ2 . TRP B 1 294 ? -15.199 31.714 69.660 1.00 11.52 ? 378 TRP B CZ2 1 ATOM 5253 C CZ3 . TRP B 1 294 ? -13.293 30.855 68.447 1.00 10.43 ? 378 TRP B CZ3 1 ATOM 5254 C CH2 . TRP B 1 294 ? -13.908 31.848 69.222 1.00 12.24 ? 378 TRP B CH2 1 ATOM 5255 N N . ASP B 1 295 ? -14.097 26.655 70.391 1.00 4.29 ? 379 ASP B N 1 ATOM 5256 C CA . ASP B 1 295 ? -14.080 26.683 71.844 1.00 6.17 ? 379 ASP B CA 1 ATOM 5257 C C . ASP B 1 295 ? -13.828 28.111 72.322 1.00 6.07 ? 379 ASP B C 1 ATOM 5258 O O . ASP B 1 295 ? -12.695 28.581 72.304 1.00 3.69 ? 379 ASP B O 1 ATOM 5259 C CB . ASP B 1 295 ? -13.001 25.741 72.370 1.00 5.56 ? 379 ASP B CB 1 ATOM 5260 C CG . ASP B 1 295 ? -12.981 25.681 73.871 1.00 7.11 ? 379 ASP B CG 1 ATOM 5261 O OD1 . ASP B 1 295 ? -13.776 26.421 74.483 1.00 6.81 ? 379 ASP B OD1 1 ATOM 5262 O OD2 . ASP B 1 295 ? -12.184 24.905 74.435 1.00 10.71 ? 379 ASP B OD2 1 ATOM 5263 N N . PRO B 1 296 ? -14.897 28.803 72.752 1.00 6.69 ? 380 PRO B N 1 ATOM 5264 C CA . PRO B 1 296 ? -14.892 30.241 73.060 1.00 8.38 ? 380 PRO B CA 1 ATOM 5265 C C . PRO B 1 296 ? -13.902 30.683 74.144 1.00 6.72 ? 380 PRO B C 1 ATOM 5266 O O . PRO B 1 296 ? -13.574 31.868 74.199 1.00 11.22 ? 380 PRO B O 1 ATOM 5267 C CB . PRO B 1 296 ? -16.334 30.510 73.517 1.00 9.96 ? 380 PRO B CB 1 ATOM 5268 C CG . PRO B 1 296 ? -16.897 29.173 73.852 1.00 9.74 ? 380 PRO B CG 1 ATOM 5269 C CD . PRO B 1 296 ? -16.234 28.214 72.923 1.00 9.22 ? 380 PRO B CD 1 ATOM 5270 N N . ASN B 1 297 ? -13.442 29.771 74.992 1.00 7.11 ? 381 ASN B N 1 ATOM 5271 C CA . ASN B 1 297 ? -12.414 30.125 75.971 1.00 8.30 ? 381 ASN B CA 1 ATOM 5272 C C . ASN B 1 297 ? -11.269 29.118 75.986 1.00 10.28 ? 381 ASN B C 1 ATOM 5273 O O . ASN B 1 297 ? -10.543 29.005 76.971 1.00 10.03 ? 381 ASN B O 1 ATOM 5274 C CB . ASN B 1 297 ? -13.011 30.268 77.373 1.00 8.27 ? 381 ASN B CB 1 ATOM 5275 C CG . ASN B 1 297 ? -13.336 28.933 78.001 1.00 17.54 ? 381 ASN B CG 1 ATOM 5276 O OD1 . ASN B 1 297 ? -13.372 27.918 77.318 1.00 8.97 ? 381 ASN B OD1 1 ATOM 5277 N ND2 . ASN B 1 297 ? -13.570 28.926 79.307 1.00 20.28 ? 381 ASN B ND2 1 ATOM 5278 N N . GLY B 1 298 ? -11.107 28.397 74.881 1.00 7.06 ? 382 GLY B N 1 ATOM 5279 C CA . GLY B 1 298 ? -10.154 27.304 74.808 1.00 6.58 ? 382 GLY B CA 1 ATOM 5280 C C . GLY B 1 298 ? -8.693 27.695 74.693 1.00 6.56 ? 382 GLY B C 1 ATOM 5281 O O . GLY B 1 298 ? -7.813 26.855 74.865 1.00 7.46 ? 382 GLY B O 1 ATOM 5282 N N . TRP B 1 299 ? -8.417 28.960 74.395 1.00 8.64 ? 383 TRP B N 1 ATOM 5283 C CA . TRP B 1 299 ? -7.027 29.394 74.300 1.00 9.10 ? 383 TRP B CA 1 ATOM 5284 C C . TRP B 1 299 ? -6.391 29.464 75.683 1.00 11.32 ? 383 TRP B C 1 ATOM 5285 O O . TRP B 1 299 ? -5.225 29.103 75.859 1.00 8.32 ? 383 TRP B O 1 ATOM 5286 C CB . TRP B 1 299 ? -6.910 30.748 73.600 1.00 10.43 ? 383 TRP B CB 1 ATOM 5287 C CG . TRP B 1 299 ? -5.494 31.086 73.215 1.00 10.37 ? 383 TRP B CG 1 ATOM 5288 C CD1 . TRP B 1 299 ? -4.612 31.861 73.915 1.00 9.60 ? 383 TRP B CD1 1 ATOM 5289 C CD2 . TRP B 1 299 ? -4.799 30.646 72.042 1.00 9.51 ? 383 TRP B CD2 1 ATOM 5290 N NE1 . TRP B 1 299 ? -3.413 31.935 73.244 1.00 12.52 ? 383 TRP B NE1 1 ATOM 5291 C CE2 . TRP B 1 299 ? -3.502 31.197 72.093 1.00 9.22 ? 383 TRP B CE2 1 ATOM 5292 C CE3 . TRP B 1 299 ? -5.148 29.840 70.953 1.00 7.74 ? 383 TRP B CE3 1 ATOM 5293 C CZ2 . TRP B 1 299 ? -2.556 30.970 71.097 1.00 9.52 ? 383 TRP B CZ2 1 ATOM 5294 C CZ3 . TRP B 1 299 ? -4.205 29.617 69.963 1.00 11.01 ? 383 TRP B CZ3 1 ATOM 5295 C CH2 . TRP B 1 299 ? -2.926 30.180 70.042 1.00 11.60 ? 383 TRP B CH2 1 ATOM 5296 N N . THR B 1 300 ? -7.168 29.919 76.662 1.00 9.01 ? 384 THR B N 1 ATOM 5297 C CA . THR B 1 300 ? -6.659 30.118 78.017 1.00 11.40 ? 384 THR B CA 1 ATOM 5298 C C . THR B 1 300 ? -7.380 29.284 79.077 1.00 11.58 ? 384 THR B C 1 ATOM 5299 O O . THR B 1 300 ? -6.899 29.164 80.203 1.00 13.06 ? 384 THR B O 1 ATOM 5300 C CB . THR B 1 300 ? -6.727 31.603 78.425 1.00 12.29 ? 384 THR B CB 1 ATOM 5301 O OG1 . THR B 1 300 ? -8.066 32.086 78.251 1.00 12.65 ? 384 THR B OG1 1 ATOM 5302 C CG2 . THR B 1 300 ? -5.780 32.434 77.576 1.00 13.92 ? 384 THR B CG2 1 ATOM 5303 N N . GLY B 1 301 ? -8.529 28.714 78.722 1.00 9.94 ? 385 GLY B N 1 ATOM 5304 C CA . GLY B 1 301 ? -9.317 27.929 79.661 1.00 13.15 ? 385 GLY B CA 1 ATOM 5305 C C . GLY B 1 301 ? -9.079 26.438 79.519 1.00 11.63 ? 385 GLY B C 1 ATOM 5306 O O . GLY B 1 301 ? -8.926 25.933 78.408 1.00 11.07 ? 385 GLY B O 1 ATOM 5307 N N . THR B 1 302 ? -9.065 25.723 80.642 1.00 9.19 ? 386 THR B N 1 ATOM 5308 C CA . THR B 1 302 ? -8.658 24.318 80.638 1.00 10.01 ? 386 THR B CA 1 ATOM 5309 C C . THR B 1 302 ? -9.804 23.303 80.597 1.00 11.12 ? 386 THR B C 1 ATOM 5310 O O . THR B 1 302 ? -9.560 22.099 80.545 1.00 11.87 ? 386 THR B O 1 ATOM 5311 C CB . THR B 1 302 ? -7.748 23.991 81.841 1.00 13.16 ? 386 THR B CB 1 ATOM 5312 O OG1 . THR B 1 302 ? -8.441 24.282 83.060 1.00 10.55 ? 386 THR B OG1 1 ATOM 5313 C CG2 . THR B 1 302 ? -6.467 24.812 81.781 1.00 11.60 ? 386 THR B CG2 1 ATOM 5314 N N . ASP B 1 303 ? -11.048 23.774 80.615 1.00 11.75 ? 387 ASP B N 1 ATOM 5315 C CA . ASP B 1 303 ? -12.183 22.855 80.581 1.00 15.77 ? 387 ASP B CA 1 ATOM 5316 C C . ASP B 1 303 ? -12.313 22.200 79.208 1.00 12.51 ? 387 ASP B C 1 ATOM 5317 O O . ASP B 1 303 ? -11.641 22.600 78.257 1.00 11.76 ? 387 ASP B O 1 ATOM 5318 C CB . ASP B 1 303 ? -13.480 23.569 80.967 1.00 16.45 ? 387 ASP B CB 1 ATOM 5319 C CG . ASP B 1 303 ? -13.939 24.553 79.915 1.00 18.28 ? 387 ASP B CG 1 ATOM 5320 O OD1 . ASP B 1 303 ? -14.472 24.103 78.883 1.00 17.58 ? 387 ASP B OD1 1 ATOM 5321 O OD2 . ASP B 1 303 ? -13.777 25.773 80.120 1.00 18.80 ? 387 ASP B OD2 1 ATOM 5322 N N . ASN B 1 304 ? -13.172 21.189 79.108 1.00 16.91 ? 388 ASN B N 1 ATOM 5323 C CA . ASN B 1 304 ? -13.357 20.471 77.848 1.00 20.62 ? 388 ASN B CA 1 ATOM 5324 C C . ASN B 1 304 ? -14.723 20.701 77.206 1.00 19.80 ? 388 ASN B C 1 ATOM 5325 O O . ASN B 1 304 ? -15.196 19.875 76.425 1.00 19.98 ? 388 ASN B O 1 ATOM 5326 C CB . ASN B 1 304 ? -13.103 18.970 78.027 1.00 19.70 ? 388 ASN B CB 1 ATOM 5327 C CG . ASN B 1 304 ? -14.114 18.308 78.944 1.00 28.62 ? 388 ASN B CG 1 ATOM 5328 O OD1 . ASN B 1 304 ? -14.855 18.981 79.660 1.00 36.00 ? 388 ASN B OD1 1 ATOM 5329 N ND2 . ASN B 1 304 ? -14.148 16.980 78.927 1.00 27.95 ? 388 ASN B ND2 1 ATOM 5330 N N . ASN B 1 305 ? -15.355 21.821 77.536 1.00 12.80 ? 389 ASN B N 1 ATOM 5331 C CA . ASN B 1 305 ? -16.618 22.186 76.909 1.00 12.93 ? 389 ASN B CA 1 ATOM 5332 C C . ASN B 1 305 ? -16.355 22.980 75.634 1.00 13.84 ? 389 ASN B C 1 ATOM 5333 O O . ASN B 1 305 ? -15.414 23.762 75.578 1.00 13.12 ? 389 ASN B O 1 ATOM 5334 C CB . ASN B 1 305 ? -17.474 23.010 77.871 1.00 18.11 ? 389 ASN B CB 1 ATOM 5335 C CG . ASN B 1 305 ? -17.743 22.289 79.182 1.00 25.67 ? 389 ASN B CG 1 ATOM 5336 O OD1 . ASN B 1 305 ? -18.134 22.906 80.173 1.00 36.97 ? 389 ASN B OD1 1 ATOM 5337 N ND2 . ASN B 1 305 ? -17.532 20.979 79.193 1.00 24.34 ? 389 ASN B ND2 1 ATOM 5338 N N . PHE B 1 306 ? -17.170 22.772 74.607 1.00 11.30 ? 390 PHE B N 1 ATOM 5339 C CA . PHE B 1 306 ? -17.034 23.534 73.367 1.00 10.86 ? 390 PHE B CA 1 ATOM 5340 C C . PHE B 1 306 ? -18.405 23.893 72.805 1.00 14.78 ? 390 PHE B C 1 ATOM 5341 O O . PHE B 1 306 ? -19.413 23.314 73.204 1.00 12.75 ? 390 PHE B O 1 ATOM 5342 C CB . PHE B 1 306 ? -16.200 22.768 72.335 1.00 13.67 ? 390 PHE B CB 1 ATOM 5343 C CG . PHE B 1 306 ? -16.782 21.439 71.949 1.00 14.37 ? 390 PHE B CG 1 ATOM 5344 C CD1 . PHE B 1 306 ? -17.711 21.348 70.925 1.00 12.18 ? 390 PHE B CD1 1 ATOM 5345 C CD2 . PHE B 1 306 ? -16.398 20.281 72.605 1.00 15.52 ? 390 PHE B CD2 1 ATOM 5346 C CE1 . PHE B 1 306 ? -18.248 20.126 70.566 1.00 17.71 ? 390 PHE B CE1 1 ATOM 5347 C CE2 . PHE B 1 306 ? -16.931 19.057 72.251 1.00 15.92 ? 390 PHE B CE2 1 ATOM 5348 C CZ . PHE B 1 306 ? -17.858 18.979 71.230 1.00 19.01 ? 390 PHE B CZ 1 ATOM 5349 N N . SER B 1 307 ? -18.440 24.845 71.878 1.00 10.90 ? 391 SER B N 1 ATOM 5350 C CA . SER B 1 307 ? -19.706 25.388 71.395 1.00 9.55 ? 391 SER B CA 1 ATOM 5351 C C . SER B 1 307 ? -20.121 24.884 70.017 1.00 14.39 ? 391 SER B C 1 ATOM 5352 O O . SER B 1 307 ? -21.307 24.668 69.766 1.00 14.81 ? 391 SER B O 1 ATOM 5353 C CB . SER B 1 307 ? -19.666 26.918 71.400 1.00 12.84 ? 391 SER B CB 1 ATOM 5354 O OG . SER B 1 307 ? -19.508 27.413 72.718 1.00 19.99 ? 391 SER B OG 1 ATOM 5355 N N . ILE B 1 308 ? -19.153 24.708 69.122 1.00 10.88 ? 392 ILE B N 1 ATOM 5356 C CA . ILE B 1 308 ? -19.454 24.280 67.759 1.00 10.13 ? 392 ILE B CA 1 ATOM 5357 C C . ILE B 1 308 ? -18.526 23.163 67.303 1.00 10.75 ? 392 ILE B C 1 ATOM 5358 O O . ILE B 1 308 ? -17.324 23.207 67.558 1.00 11.00 ? 392 ILE B O 1 ATOM 5359 C CB . ILE B 1 308 ? -19.305 25.444 66.757 1.00 13.64 ? 392 ILE B CB 1 ATOM 5360 C CG1 . ILE B 1 308 ? -20.152 26.643 67.183 1.00 15.00 ? 392 ILE B CG1 1 ATOM 5361 C CG2 . ILE B 1 308 ? -19.682 24.993 65.351 1.00 15.35 ? 392 ILE B CG2 1 ATOM 5362 C CD1 . ILE B 1 308 ? -19.979 27.853 66.284 1.00 15.30 ? 392 ILE B CD1 1 ATOM 5363 N N . LYS B 1 309 ? -19.087 22.165 66.627 1.00 8.18 ? 394 LYS B N 1 ATOM 5364 C CA . LYS B 1 309 ? -18.284 21.143 65.964 1.00 9.26 ? 394 LYS B CA 1 ATOM 5365 C C . LYS B 1 309 ? -18.768 20.938 64.533 1.00 12.43 ? 394 LYS B C 1 ATOM 5366 O O . LYS B 1 309 ? -19.967 20.793 64.294 1.00 13.23 ? 394 LYS B O 1 ATOM 5367 C CB . LYS B 1 309 ? -18.336 19.817 66.728 1.00 11.73 ? 394 LYS B CB 1 ATOM 5368 C CG . LYS B 1 309 ? -17.546 18.697 66.058 1.00 11.15 ? 394 LYS B CG 1 ATOM 5369 C CD . LYS B 1 309 ? -17.583 17.410 66.875 1.00 18.96 ? 394 LYS B CD 1 ATOM 5370 C CE . LYS B 1 309 ? -18.971 16.786 66.897 1.00 18.53 ? 394 LYS B CE 1 ATOM 5371 N NZ . LYS B 1 309 ? -19.410 16.329 65.550 1.00 25.40 ? 394 LYS B NZ 1 ATOM 5372 N N . GLN B 1 310 ? -17.836 20.934 63.584 1.00 8.56 ? 395 GLN B N 1 ATOM 5373 C CA . GLN B 1 310 ? -18.173 20.702 62.182 1.00 7.49 ? 395 GLN B CA 1 ATOM 5374 C C . GLN B 1 310 ? -17.338 19.564 61.604 1.00 8.83 ? 395 GLN B C 1 ATOM 5375 O O . GLN B 1 310 ? -16.107 19.618 61.619 1.00 6.33 ? 395 GLN B O 1 ATOM 5376 C CB . GLN B 1 310 ? -17.981 21.978 61.352 1.00 9.00 ? 395 GLN B CB 1 ATOM 5377 C CG . GLN B 1 310 ? -18.338 21.805 59.878 1.00 7.65 ? 395 GLN B CG 1 ATOM 5378 C CD . GLN B 1 310 ? -18.114 23.063 59.051 1.00 10.53 ? 395 GLN B CD 1 ATOM 5379 O OE1 . GLN B 1 310 ? -17.923 24.155 59.587 1.00 9.94 ? 395 GLN B OE1 1 ATOM 5380 N NE2 . GLN B 1 310 ? -18.147 22.912 57.733 1.00 8.70 ? 395 GLN B NE2 1 ATOM 5381 N N . ASP B 1 311 ? -18.016 18.536 61.101 1.00 9.18 ? 396 ASP B N 1 ATOM 5382 C CA . ASP B 1 311 ? -17.347 17.378 60.515 1.00 8.85 ? 396 ASP B CA 1 ATOM 5383 C C . ASP B 1 311 ? -16.711 17.716 59.167 1.00 9.05 ? 396 ASP B C 1 ATOM 5384 O O . ASP B 1 311 ? -17.314 18.397 58.337 1.00 7.20 ? 396 ASP B O 1 ATOM 5385 C CB . ASP B 1 311 ? -18.334 16.219 60.343 1.00 9.88 ? 396 ASP B CB 1 ATOM 5386 C CG . ASP B 1 311 ? -18.848 15.682 61.668 1.00 17.73 ? 396 ASP B CG 1 ATOM 5387 O OD1 . ASP B 1 311 ? -18.254 16.005 62.717 1.00 17.44 ? 396 ASP B OD1 1 ATOM 5388 O OD2 . ASP B 1 311 ? -19.848 14.934 61.663 1.00 25.12 ? 396 ASP B OD2 1 ATOM 5389 N N . ILE B 1 312 ? -15.496 17.221 58.951 1.00 7.31 ? 397 ILE B N 1 ATOM 5390 C CA . ILE B 1 312 ? -14.763 17.485 57.717 1.00 7.31 ? 397 ILE B CA 1 ATOM 5391 C C . ILE B 1 312 ? -14.407 16.185 56.998 1.00 7.29 ? 397 ILE B C 1 ATOM 5392 O O . ILE B 1 312 ? -14.578 16.064 55.782 1.00 6.04 ? 397 ILE B O 1 ATOM 5393 C CB . ILE B 1 312 ? -13.477 18.283 57.997 1.00 7.64 ? 397 ILE B CB 1 ATOM 5394 C CG1 . ILE B 1 312 ? -13.815 19.616 58.669 1.00 8.05 ? 397 ILE B CG1 1 ATOM 5395 C CG2 . ILE B 1 312 ? -12.692 18.510 56.710 1.00 6.52 ? 397 ILE B CG2 1 ATOM 5396 C CD1 . ILE B 1 312 ? -14.648 20.547 57.808 1.00 7.68 ? 397 ILE B CD1 1 ATOM 5397 N N . VAL B 1 313 ? -13.904 15.220 57.762 1.00 7.53 ? 398 VAL B N 1 ATOM 5398 C CA . VAL B 1 313 ? -13.606 13.888 57.248 1.00 6.57 ? 398 VAL B CA 1 ATOM 5399 C C . VAL B 1 313 ? -14.074 12.852 58.267 1.00 6.60 ? 398 VAL B C 1 ATOM 5400 O O . VAL B 1 313 ? -13.849 13.013 59.466 1.00 5.77 ? 398 VAL B O 1 ATOM 5401 C CB . VAL B 1 313 ? -12.095 13.709 56.985 1.00 6.04 ? 398 VAL B CB 1 ATOM 5402 C CG1 . VAL B 1 313 ? -11.781 12.267 56.615 1.00 6.24 ? 398 VAL B CG1 1 ATOM 5403 C CG2 . VAL B 1 313 ? -11.622 14.664 55.890 1.00 7.26 ? 398 VAL B CG2 1 ATOM 5404 N N . GLY B 1 314 ? -14.736 11.800 57.790 1.00 7.82 ? 399 GLY B N 1 ATOM 5405 C CA . GLY B 1 314 ? -15.278 10.770 58.663 1.00 10.97 ? 399 GLY B CA 1 ATOM 5406 C C . GLY B 1 314 ? -14.216 10.019 59.444 1.00 9.32 ? 399 GLY B C 1 ATOM 5407 O O . GLY B 1 314 ? -13.093 9.844 58.972 1.00 8.15 ? 399 GLY B O 1 ATOM 5408 N N . ILE B 1 315 ? -14.572 9.562 60.641 1.00 10.25 ? 400 ILE B N 1 ATOM 5409 C CA . ILE B 1 315 ? -13.607 8.905 61.518 1.00 12.16 ? 400 ILE B CA 1 ATOM 5410 C C . ILE B 1 315 ? -13.026 7.636 60.895 1.00 12.94 ? 400 ILE B C 1 ATOM 5411 O O . ILE B 1 315 ? -11.910 7.235 61.218 1.00 12.70 ? 400 ILE B O 1 ATOM 5412 C CB . ILE B 1 315 ? -14.209 8.578 62.902 1.00 13.81 ? 400 ILE B CB 1 ATOM 5413 C CG1 . ILE B 1 315 ? -13.102 8.175 63.880 1.00 13.05 ? 400 ILE B CG1 1 ATOM 5414 C CG2 . ILE B 1 315 ? -15.259 7.484 62.787 1.00 17.75 ? 400 ILE B CG2 1 ATOM 5415 C CD1 . ILE B 1 315 ? -13.585 7.960 65.297 1.00 19.64 ? 400 ILE B CD1 1 ATOM 5416 N N . ASN B 1 316 ? -13.778 7.013 59.993 1.00 11.85 ? 401 ASN B N 1 ATOM 5417 C CA . ASN B 1 316 ? -13.306 5.805 59.323 1.00 19.06 ? 401 ASN B CA 1 ATOM 5418 C C . ASN B 1 316 ? -12.453 6.089 58.084 1.00 20.45 ? 401 ASN B C 1 ATOM 5419 O O . ASN B 1 316 ? -12.021 5.163 57.399 1.00 21.53 ? 401 ASN B O 1 ATOM 5420 C CB . ASN B 1 316 ? -14.484 4.902 58.950 1.00 22.81 ? 401 ASN B CB 1 ATOM 5421 C CG . ASN B 1 316 ? -15.195 4.339 60.164 1.00 29.05 ? 401 ASN B CG 1 ATOM 5422 O OD1 . ASN B 1 316 ? -16.420 4.220 60.178 1.00 44.13 ? 401 ASN B OD1 1 ATOM 5423 N ND2 . ASN B 1 316 ? -14.430 3.994 61.193 1.00 28.47 ? 401 ASN B ND2 1 ATOM 5424 N N . GLU B 1 317 ? -12.214 7.368 57.805 1.00 13.82 ? 402 GLU B N 1 ATOM 5425 C CA . GLU B 1 317 ? -11.438 7.767 56.633 1.00 11.19 ? 402 GLU B CA 1 ATOM 5426 C C . GLU B 1 317 ? -10.074 8.326 57.034 1.00 11.94 ? 402 GLU B C 1 ATOM 5427 O O . GLU B 1 317 ? -9.930 8.932 58.093 1.00 8.15 ? 402 GLU B O 1 ATOM 5428 C CB . GLU B 1 317 ? -12.206 8.810 55.816 1.00 8.71 ? 402 GLU B CB 1 ATOM 5429 C CG . GLU B 1 317 ? -13.621 8.397 55.455 1.00 16.51 ? 402 GLU B CG 1 ATOM 5430 C CD . GLU B 1 317 ? -13.664 7.289 54.422 1.00 25.99 ? 402 GLU B CD 1 ATOM 5431 O OE1 . GLU B 1 317 ? -12.615 7.007 53.805 1.00 21.75 ? 402 GLU B OE1 1 ATOM 5432 O OE2 . GLU B 1 317 ? -14.752 6.706 54.223 1.00 37.92 ? 402 GLU B OE2 1 ATOM 5433 N N . TRP B 1 318 ? -9.076 8.119 56.179 1.00 11.65 ? 403 TRP B N 1 ATOM 5434 C CA . TRP B 1 318 ? -7.719 8.581 56.452 1.00 9.43 ? 403 TRP B CA 1 ATOM 5435 C C . TRP B 1 318 ? -7.601 10.099 56.356 1.00 9.33 ? 403 TRP B C 1 ATOM 5436 O O . TRP B 1 318 ? -8.142 10.716 55.440 1.00 11.07 ? 403 TRP B O 1 ATOM 5437 C CB . TRP B 1 318 ? -6.730 7.941 55.473 1.00 14.33 ? 403 TRP B CB 1 ATOM 5438 C CG . TRP B 1 318 ? -6.858 6.453 55.366 1.00 16.36 ? 403 TRP B CG 1 ATOM 5439 C CD1 . TRP B 1 318 ? -7.381 5.748 54.321 1.00 20.29 ? 403 TRP B CD1 1 ATOM 5440 C CD2 . TRP B 1 318 ? -6.461 5.486 56.344 1.00 17.75 ? 403 TRP B CD2 1 ATOM 5441 N NE1 . TRP B 1 318 ? -7.332 4.401 54.587 1.00 20.17 ? 403 TRP B NE1 1 ATOM 5442 C CE2 . TRP B 1 318 ? -6.773 4.214 55.824 1.00 20.97 ? 403 TRP B CE2 1 ATOM 5443 C CE3 . TRP B 1 318 ? -5.874 5.572 57.609 1.00 22.05 ? 403 TRP B CE3 1 ATOM 5444 C CZ2 . TRP B 1 318 ? -6.515 3.038 56.524 1.00 21.30 ? 403 TRP B CZ2 1 ATOM 5445 C CZ3 . TRP B 1 318 ? -5.620 4.403 58.303 1.00 29.44 ? 403 TRP B CZ3 1 ATOM 5446 C CH2 . TRP B 1 318 ? -5.940 3.153 57.758 1.00 25.23 ? 403 TRP B CH2 1 ATOM 5447 N N . SER B 1 319 ? -6.894 10.698 57.308 1.00 8.56 ? 404 SER B N 1 ATOM 5448 C CA . SER B 1 319 ? -6.530 12.108 57.204 1.00 6.25 ? 404 SER B CA 1 ATOM 5449 C C . SER B 1 319 ? -5.009 12.240 57.235 1.00 8.53 ? 404 SER B C 1 ATOM 5450 O O . SER B 1 319 ? -4.304 11.424 56.643 1.00 8.19 ? 404 SER B O 1 ATOM 5451 C CB . SER B 1 319 ? -7.199 12.949 58.300 1.00 9.20 ? 404 SER B CB 1 ATOM 5452 O OG . SER B 1 319 ? -6.931 12.442 59.597 1.00 9.14 ? 404 SER B OG 1 ATOM 5453 N N . GLY B 1 320 ? -4.501 13.258 57.920 1.00 8.65 ? 405 GLY B N 1 ATOM 5454 C CA . GLY B 1 320 ? -3.065 13.464 57.987 1.00 7.82 ? 405 GLY B CA 1 ATOM 5455 C C . GLY B 1 320 ? -2.707 14.856 58.464 1.00 7.80 ? 405 GLY B C 1 ATOM 5456 O O . GLY B 1 320 ? -3.349 15.395 59.363 1.00 6.94 ? 405 GLY B O 1 ATOM 5457 N N . TYR B 1 321 ? -1.674 15.437 57.863 1.00 5.99 ? 406 TYR B N 1 ATOM 5458 C CA . TYR B 1 321 ? -1.271 16.798 58.189 1.00 5.97 ? 406 TYR B CA 1 ATOM 5459 C C . TYR B 1 321 ? -2.387 17.790 57.879 1.00 6.23 ? 406 TYR B C 1 ATOM 5460 O O . TYR B 1 321 ? -3.227 17.554 57.008 1.00 4.45 ? 406 TYR B O 1 ATOM 5461 C CB . TYR B 1 321 ? -0.014 17.190 57.403 1.00 6.01 ? 406 TYR B CB 1 ATOM 5462 C CG . TYR B 1 321 ? 1.290 16.704 57.999 1.00 7.59 ? 406 TYR B CG 1 ATOM 5463 C CD1 . TYR B 1 321 ? 1.319 15.655 58.911 1.00 6.87 ? 406 TYR B CD1 1 ATOM 5464 C CD2 . TYR B 1 321 ? 2.498 17.295 57.642 1.00 6.42 ? 406 TYR B CD2 1 ATOM 5465 C CE1 . TYR B 1 321 ? 2.517 15.213 59.456 1.00 7.36 ? 406 TYR B CE1 1 ATOM 5466 C CE2 . TYR B 1 321 ? 3.698 16.859 58.179 1.00 9.96 ? 406 TYR B CE2 1 ATOM 5467 C CZ . TYR B 1 321 ? 3.701 15.818 59.086 1.00 10.94 ? 406 TYR B CZ 1 ATOM 5468 O OH . TYR B 1 321 ? 4.895 15.385 59.621 1.00 8.15 ? 406 TYR B OH 1 ATOM 5469 N N . SER B 1 322 ? -2.390 18.904 58.599 1.00 5.33 ? 407 SER B N 1 ATOM 5470 C CA . SER B 1 322 ? -3.279 20.011 58.284 1.00 5.39 ? 407 SER B CA 1 ATOM 5471 C C . SER B 1 322 ? -2.572 21.317 58.608 1.00 6.16 ? 407 SER B C 1 ATOM 5472 O O . SER B 1 322 ? -1.642 21.348 59.413 1.00 7.88 ? 407 SER B O 1 ATOM 5473 C CB . SER B 1 322 ? -4.602 19.901 59.050 1.00 5.02 ? 407 SER B CB 1 ATOM 5474 O OG . SER B 1 322 ? -4.386 19.879 60.452 1.00 6.98 ? 407 SER B OG 1 ATOM 5475 N N . GLY B 1 323 ? -3.002 22.396 57.972 1.00 4.75 ? 408 GLY B N 1 ATOM 5476 C CA . GLY B 1 323 ? -2.363 23.676 58.191 1.00 5.70 ? 408 GLY B CA 1 ATOM 5477 C C . GLY B 1 323 ? -3.259 24.843 57.852 1.00 6.78 ? 408 GLY B C 1 ATOM 5478 O O . GLY B 1 323 ? -4.238 24.709 57.115 1.00 6.46 ? 408 GLY B O 1 ATOM 5479 N N . SER B 1 324 ? -2.918 26.000 58.398 1.00 4.90 ? 409 SER B N 1 ATOM 5480 C CA . SER B 1 324 ? -3.656 27.212 58.108 1.00 4.95 ? 409 SER B CA 1 ATOM 5481 C C . SER B 1 324 ? -3.134 27.872 56.839 1.00 6.85 ? 409 SER B C 1 ATOM 5482 O O . SER B 1 324 ? -1.985 27.669 56.443 1.00 7.39 ? 409 SER B O 1 ATOM 5483 C CB . SER B 1 324 ? -3.537 28.183 59.282 1.00 8.32 ? 409 SER B CB 1 ATOM 5484 O OG . SER B 1 324 ? -2.174 28.433 59.586 1.00 12.28 ? 409 SER B OG 1 ATOM 5485 N N . PHE B 1 325 ? -4.000 28.635 56.184 1.00 5.84 ? 410 PHE B N 1 ATOM 5486 C CA . PHE B 1 325 ? -3.560 29.619 55.203 1.00 8.89 ? 410 PHE B CA 1 ATOM 5487 C C . PHE B 1 325 ? -4.571 30.751 55.183 1.00 6.49 ? 410 PHE B C 1 ATOM 5488 O O . PHE B 1 325 ? -5.731 30.556 55.534 1.00 9.59 ? 410 PHE B O 1 ATOM 5489 C CB . PHE B 1 325 ? -3.324 29.012 53.810 1.00 4.97 ? 410 PHE B CB 1 ATOM 5490 C CG . PHE B 1 325 ? -4.579 28.631 53.066 1.00 6.45 ? 410 PHE B CG 1 ATOM 5491 C CD1 . PHE B 1 325 ? -5.184 27.403 53.280 1.00 6.35 ? 410 PHE B CD1 1 ATOM 5492 C CD2 . PHE B 1 325 ? -5.124 29.484 52.116 1.00 7.45 ? 410 PHE B CD2 1 ATOM 5493 C CE1 . PHE B 1 325 ? -6.325 27.042 52.581 1.00 9.11 ? 410 PHE B CE1 1 ATOM 5494 C CE2 . PHE B 1 325 ? -6.267 29.131 51.415 1.00 8.02 ? 410 PHE B CE2 1 ATOM 5495 C CZ . PHE B 1 325 ? -6.868 27.906 51.647 1.00 8.19 ? 410 PHE B CZ 1 ATOM 5496 N N . VAL B 1 326 ? -4.129 31.943 54.809 1.00 8.34 ? 411 VAL B N 1 ATOM 5497 C CA . VAL B 1 326 ? -5.014 33.096 54.863 1.00 6.31 ? 411 VAL B CA 1 ATOM 5498 C C . VAL B 1 326 ? -5.166 33.753 53.505 1.00 10.37 ? 411 VAL B C 1 ATOM 5499 O O . VAL B 1 326 ? -4.329 33.585 52.618 1.00 7.96 ? 411 VAL B O 1 ATOM 5500 C CB . VAL B 1 326 ? -4.517 34.144 55.879 1.00 8.23 ? 411 VAL B CB 1 ATOM 5501 C CG1 . VAL B 1 326 ? -4.428 33.530 57.264 1.00 6.42 ? 411 VAL B CG1 1 ATOM 5502 C CG2 . VAL B 1 326 ? -3.168 34.704 55.449 1.00 11.62 ? 411 VAL B CG2 1 ATOM 5503 N N . GLN B 1 327 ? -6.256 34.491 53.349 1.00 5.23 ? 412 GLN B N 1 ATOM 5504 C CA . GLN B 1 327 ? -6.458 35.312 52.173 1.00 5.45 ? 412 GLN B CA 1 ATOM 5505 C C . GLN B 1 327 ? -6.518 36.756 52.636 1.00 6.80 ? 412 GLN B C 1 ATOM 5506 O O . GLN B 1 327 ? -7.365 37.120 53.456 1.00 5.03 ? 412 GLN B O 1 ATOM 5507 C CB . GLN B 1 327 ? -7.739 34.905 51.438 1.00 5.30 ? 412 GLN B CB 1 ATOM 5508 C CG . GLN B 1 327 ? -7.727 33.457 50.962 1.00 4.19 ? 412 GLN B CG 1 ATOM 5509 C CD . GLN B 1 327 ? -8.925 33.103 50.099 1.00 7.10 ? 412 GLN B CD 1 ATOM 5510 O OE1 . GLN B 1 327 ? -10.034 33.588 50.325 1.00 6.35 ? 412 GLN B OE1 1 ATOM 5511 N NE2 . GLN B 1 327 ? -8.706 32.246 49.108 1.00 10.67 ? 412 GLN B NE2 1 ATOM 5512 N N . HIS B 1 328 A -5.592 37.566 52.134 1.00 6.10 ? 412 HIS B N 1 ATOM 5513 C CA . HIS B 1 328 A -5.494 38.962 52.537 1.00 7.43 ? 412 HIS B CA 1 ATOM 5514 C C . HIS B 1 328 A -6.546 39.806 51.824 1.00 7.55 ? 412 HIS B C 1 ATOM 5515 O O . HIS B 1 328 A -7.012 39.443 50.744 1.00 8.32 ? 412 HIS B O 1 ATOM 5516 C CB . HIS B 1 328 A -4.096 39.505 52.237 1.00 7.80 ? 412 HIS B CB 1 ATOM 5517 C CG . HIS B 1 328 A -3.034 39.005 53.169 1.00 8.29 ? 412 HIS B CG 1 ATOM 5518 N ND1 . HIS B 1 328 A -2.436 39.811 54.114 1.00 9.55 ? 412 HIS B ND1 1 ATOM 5519 C CD2 . HIS B 1 328 A -2.455 37.788 53.292 1.00 6.52 ? 412 HIS B CD2 1 ATOM 5520 C CE1 . HIS B 1 328 A -1.534 39.111 54.779 1.00 9.58 ? 412 HIS B CE1 1 ATOM 5521 N NE2 . HIS B 1 328 A -1.528 37.879 54.302 1.00 9.61 ? 412 HIS B NE2 1 ATOM 5522 N N . PRO B 1 329 B -6.927 40.937 52.436 1.00 6.78 ? 412 PRO B N 1 ATOM 5523 C CA . PRO B 1 329 B -7.885 41.869 51.834 1.00 10.13 ? 412 PRO B CA 1 ATOM 5524 C C . PRO B 1 329 B -7.446 42.306 50.438 1.00 12.09 ? 412 PRO B C 1 ATOM 5525 O O . PRO B 1 329 B -8.293 42.613 49.598 1.00 12.73 ? 412 PRO B O 1 ATOM 5526 C CB . PRO B 1 329 B -7.859 43.059 52.795 1.00 14.42 ? 412 PRO B CB 1 ATOM 5527 C CG . PRO B 1 329 B -7.470 42.470 54.104 1.00 14.91 ? 412 PRO B CG 1 ATOM 5528 C CD . PRO B 1 329 B -6.512 41.362 53.784 1.00 10.44 ? 412 PRO B CD 1 ATOM 5529 N N . GLU B 1 330 C -6.138 42.330 50.198 1.00 11.01 ? 412 GLU B N 1 ATOM 5530 C CA . GLU B 1 330 C -5.609 42.679 48.882 1.00 11.35 ? 412 GLU B CA 1 ATOM 5531 C C . GLU B 1 330 C -6.097 41.703 47.815 1.00 16.16 ? 412 GLU B C 1 ATOM 5532 O O . GLU B 1 330 C -6.160 42.040 46.632 1.00 17.26 ? 412 GLU B O 1 ATOM 5533 C CB . GLU B 1 330 C -4.077 42.717 48.898 1.00 12.61 ? 412 GLU B CB 1 ATOM 5534 C CG . GLU B 1 330 C -3.472 43.941 49.584 1.00 16.07 ? 412 GLU B CG 1 ATOM 5535 C CD . GLU B 1 330 C -3.347 43.786 51.093 1.00 18.75 ? 412 GLU B CD 1 ATOM 5536 O OE1 . GLU B 1 330 C -3.835 42.774 51.639 1.00 11.20 ? 412 GLU B OE1 1 ATOM 5537 O OE2 . GLU B 1 330 C -2.753 44.681 51.733 1.00 14.85 ? 412 GLU B OE2 1 ATOM 5538 N N . LEU B 1 331 D -6.438 40.491 48.241 1.00 9.90 ? 412 LEU B N 1 ATOM 5539 C CA . LEU B 1 331 D -6.945 39.469 47.330 1.00 9.15 ? 412 LEU B CA 1 ATOM 5540 C C . LEU B 1 331 D -8.472 39.413 47.313 1.00 10.79 ? 412 LEU B C 1 ATOM 5541 O O . LEU B 1 331 D -9.081 39.250 46.258 1.00 11.06 ? 412 LEU B O 1 ATOM 5542 C CB . LEU B 1 331 D -6.385 38.092 47.706 1.00 9.96 ? 412 LEU B CB 1 ATOM 5543 C CG . LEU B 1 331 D -6.998 36.879 46.999 1.00 8.82 ? 412 LEU B CG 1 ATOM 5544 C CD1 . LEU B 1 331 D -6.541 36.794 45.546 1.00 12.30 ? 412 LEU B CD1 1 ATOM 5545 C CD2 . LEU B 1 331 D -6.657 35.597 47.737 1.00 8.01 ? 412 LEU B CD2 1 ATOM 5546 N N . THR B 1 332 ? -9.088 39.561 48.481 1.00 8.30 ? 413 THR B N 1 ATOM 5547 C CA . THR B 1 332 ? -10.523 39.318 48.621 1.00 7.70 ? 413 THR B CA 1 ATOM 5548 C C . THR B 1 332 ? -11.391 40.568 48.516 1.00 11.78 ? 413 THR B C 1 ATOM 5549 O O . THR B 1 332 ? -12.560 40.487 48.139 1.00 15.12 ? 413 THR B O 1 ATOM 5550 C CB . THR B 1 332 ? -10.836 38.656 49.963 1.00 12.51 ? 413 THR B CB 1 ATOM 5551 O OG1 . THR B 1 332 ? -10.541 39.575 51.022 1.00 9.37 ? 413 THR B OG1 1 ATOM 5552 C CG2 . THR B 1 332 ? -10.007 37.393 50.136 1.00 9.56 ? 413 THR B CG2 1 ATOM 5553 N N . GLY B 1 333 ? -10.829 41.718 48.869 1.00 10.18 ? 414 GLY B N 1 ATOM 5554 C CA . GLY B 1 333 ? -11.602 42.946 48.913 1.00 9.33 ? 414 GLY B CA 1 ATOM 5555 C C . GLY B 1 333 ? -12.315 43.128 50.242 1.00 17.15 ? 414 GLY B C 1 ATOM 5556 O O . GLY B 1 333 ? -13.069 44.083 50.425 1.00 16.85 ? 414 GLY B O 1 ATOM 5557 N N . LEU B 1 334 ? -12.081 42.207 51.172 1.00 11.44 ? 415 LEU B N 1 ATOM 5558 C CA . LEU B 1 334 ? -12.657 42.307 52.507 1.00 12.83 ? 415 LEU B CA 1 ATOM 5559 C C . LEU B 1 334 ? -11.861 43.306 53.340 1.00 16.03 ? 415 LEU B C 1 ATOM 5560 O O . LEU B 1 334 ? -10.828 43.803 52.897 1.00 18.43 ? 415 LEU B O 1 ATOM 5561 C CB . LEU B 1 334 ? -12.665 40.936 53.188 1.00 10.88 ? 415 LEU B CB 1 ATOM 5562 C CG . LEU B 1 334 ? -13.438 39.841 52.452 1.00 18.04 ? 415 LEU B CG 1 ATOM 5563 C CD1 . LEU B 1 334 ? -13.227 38.484 53.110 1.00 14.58 ? 415 LEU B CD1 1 ATOM 5564 C CD2 . LEU B 1 334 ? -14.920 40.187 52.384 1.00 19.86 ? 415 LEU B CD2 1 ATOM 5565 N N . ASP B 1 335 ? -12.343 43.604 54.542 1.00 16.07 ? 416 ASP B N 1 ATOM 5566 C CA . ASP B 1 335 ? -11.645 44.529 55.430 1.00 20.27 ? 416 ASP B CA 1 ATOM 5567 C C . ASP B 1 335 ? -10.980 43.784 56.584 1.00 18.99 ? 416 ASP B C 1 ATOM 5568 O O . ASP B 1 335 ? -10.643 44.372 57.612 1.00 20.48 ? 416 ASP B O 1 ATOM 5569 C CB . ASP B 1 335 ? -12.599 45.605 55.957 1.00 23.00 ? 416 ASP B CB 1 ATOM 5570 C CG . ASP B 1 335 ? -13.788 45.021 56.700 1.00 34.48 ? 416 ASP B CG 1 ATOM 5571 O OD1 . ASP B 1 335 ? -13.783 43.804 56.982 1.00 39.28 ? 416 ASP B OD1 1 ATOM 5572 O OD2 . ASP B 1 335 ? -14.728 45.782 57.008 1.00 45.45 ? 416 ASP B OD2 1 ATOM 5573 N N . CYS B 1 336 ? -10.803 42.480 56.402 1.00 15.48 ? 417 CYS B N 1 ATOM 5574 C CA . CYS B 1 336 ? -10.152 41.637 57.396 1.00 10.61 ? 417 CYS B CA 1 ATOM 5575 C C . CYS B 1 336 ? -9.396 40.507 56.706 1.00 11.36 ? 417 CYS B C 1 ATOM 5576 O O . CYS B 1 336 ? -9.582 40.261 55.515 1.00 9.60 ? 417 CYS B O 1 ATOM 5577 C CB . CYS B 1 336 ? -11.182 41.065 58.373 1.00 13.86 ? 417 CYS B CB 1 ATOM 5578 S SG . CYS B 1 336 ? -12.591 40.248 57.579 1.00 24.60 ? 417 CYS B SG 1 ATOM 5579 N N . ILE B 1 337 ? -8.535 39.831 57.457 1.00 10.71 ? 418 ILE B N 1 ATOM 5580 C CA . ILE B 1 337 ? -7.792 38.694 56.933 1.00 8.79 ? 418 ILE B CA 1 ATOM 5581 C C . ILE B 1 337 ? -8.619 37.430 57.132 1.00 8.16 ? 418 ILE B C 1 ATOM 5582 O O . ILE B 1 337 ? -8.995 37.101 58.256 1.00 9.34 ? 418 ILE B O 1 ATOM 5583 C CB . ILE B 1 337 ? -6.430 38.550 57.638 1.00 6.93 ? 418 ILE B CB 1 ATOM 5584 C CG1 . ILE B 1 337 ? -5.600 39.824 57.449 1.00 10.25 ? 418 ILE B CG1 1 ATOM 5585 C CG2 . ILE B 1 337 ? -5.677 37.338 57.107 1.00 7.84 ? 418 ILE B CG2 1 ATOM 5586 C CD1 . ILE B 1 337 ? -4.276 39.820 58.200 1.00 9.95 ? 418 ILE B CD1 1 ATOM 5587 N N . ARG B 1 338 ? -8.921 36.735 56.039 1.00 8.95 ? 419 ARG B N 1 ATOM 5588 C CA . ARG B 1 338 ? -9.781 35.555 56.104 1.00 11.03 ? 419 ARG B CA 1 ATOM 5589 C C . ARG B 1 338 ? -8.997 34.280 56.395 1.00 6.80 ? 419 ARG B C 1 ATOM 5590 O O . ARG B 1 338 ? -8.009 33.988 55.724 1.00 9.21 ? 419 ARG B O 1 ATOM 5591 C CB . ARG B 1 338 ? -10.581 35.386 54.809 1.00 10.89 ? 419 ARG B CB 1 ATOM 5592 C CG . ARG B 1 338 ? -11.163 33.988 54.636 1.00 12.20 ? 419 ARG B CG 1 ATOM 5593 C CD . ARG B 1 338 ? -11.861 33.824 53.297 1.00 13.35 ? 419 ARG B CD 1 ATOM 5594 N NE . ARG B 1 338 ? -13.241 34.290 53.342 1.00 18.60 ? 419 ARG B NE 1 ATOM 5595 C CZ . ARG B 1 338 ? -14.047 34.341 52.287 1.00 18.71 ? 419 ARG B CZ 1 ATOM 5596 N NH1 . ARG B 1 338 ? -13.606 33.963 51.095 1.00 13.16 ? 419 ARG B NH1 1 ATOM 5597 N NH2 . ARG B 1 338 ? -15.291 34.777 52.422 1.00 21.61 ? 419 ARG B NH2 1 ATOM 5598 N N . PRO B 1 339 ? -9.446 33.512 57.399 1.00 9.38 ? 420 PRO B N 1 ATOM 5599 C CA . PRO B 1 339 ? -8.820 32.242 57.776 1.00 7.18 ? 420 PRO B CA 1 ATOM 5600 C C . PRO B 1 339 ? -9.279 31.109 56.868 1.00 7.94 ? 420 PRO B C 1 ATOM 5601 O O . PRO B 1 339 ? -10.478 30.965 56.636 1.00 8.63 ? 420 PRO B O 1 ATOM 5602 C CB . PRO B 1 339 ? -9.362 31.983 59.191 1.00 10.05 ? 420 PRO B CB 1 ATOM 5603 C CG . PRO B 1 339 ? -10.243 33.161 59.532 1.00 14.69 ? 420 PRO B CG 1 ATOM 5604 C CD . PRO B 1 339 ? -10.602 33.824 58.252 1.00 9.07 ? 420 PRO B CD 1 ATOM 5605 N N . CYS B 1 340 ? -8.333 30.322 56.365 1.00 4.66 ? 421 CYS B N 1 ATOM 5606 C CA . CYS B 1 340 ? -8.643 29.103 55.629 1.00 6.13 ? 421 CYS B CA 1 ATOM 5607 C C . CYS B 1 340 ? -7.767 27.987 56.179 1.00 6.71 ? 421 CYS B C 1 ATOM 5608 O O . CYS B 1 340 ? -6.839 28.250 56.945 1.00 5.02 ? 421 CYS B O 1 ATOM 5609 C CB . CYS B 1 340 ? -8.379 29.274 54.130 1.00 5.42 ? 421 CYS B CB 1 ATOM 5610 S SG . CYS B 1 340 ? -9.254 30.637 53.313 1.00 8.57 ? 421 CYS B SG 1 ATOM 5611 N N . PHE B 1 341 ? -8.049 26.749 55.786 1.00 3.00 ? 422 PHE B N 1 ATOM 5612 C CA . PHE B 1 341 ? -7.188 25.630 56.158 1.00 5.30 ? 422 PHE B CA 1 ATOM 5613 C C . PHE B 1 341 ? -7.221 24.504 55.132 1.00 6.31 ? 422 PHE B C 1 ATOM 5614 O O . PHE B 1 341 ? -8.171 24.375 54.356 1.00 6.02 ? 422 PHE B O 1 ATOM 5615 C CB . PHE B 1 341 ? -7.526 25.090 57.557 1.00 4.28 ? 422 PHE B CB 1 ATOM 5616 C CG . PHE B 1 341 ? -8.810 24.307 57.620 1.00 5.47 ? 422 PHE B CG 1 ATOM 5617 C CD1 . PHE B 1 341 ? -10.011 24.938 57.903 1.00 6.69 ? 422 PHE B CD1 1 ATOM 5618 C CD2 . PHE B 1 341 ? -8.811 22.938 57.410 1.00 4.60 ? 422 PHE B CD2 1 ATOM 5619 C CE1 . PHE B 1 341 ? -11.195 24.216 57.969 1.00 6.06 ? 422 PHE B CE1 1 ATOM 5620 C CE2 . PHE B 1 341 ? -9.992 22.209 57.471 1.00 7.14 ? 422 PHE B CE2 1 ATOM 5621 C CZ . PHE B 1 341 ? -11.183 22.848 57.751 1.00 6.10 ? 422 PHE B CZ 1 ATOM 5622 N N . TRP B 1 342 ? -6.166 23.698 55.127 1.00 2.20 ? 423 TRP B N 1 ATOM 5623 C CA . TRP B 1 342 ? -6.088 22.544 54.242 1.00 4.34 ? 423 TRP B CA 1 ATOM 5624 C C . TRP B 1 342 ? -5.861 21.270 55.041 1.00 5.24 ? 423 TRP B C 1 ATOM 5625 O O . TRP B 1 342 ? -5.306 21.305 56.145 1.00 4.00 ? 423 TRP B O 1 ATOM 5626 C CB . TRP B 1 342 ? -4.958 22.723 53.222 1.00 6.39 ? 423 TRP B CB 1 ATOM 5627 C CG . TRP B 1 342 ? -3.628 23.032 53.849 1.00 5.66 ? 423 TRP B CG 1 ATOM 5628 C CD1 . TRP B 1 342 ? -3.067 24.267 54.008 1.00 5.38 ? 423 TRP B CD1 1 ATOM 5629 C CD2 . TRP B 1 342 ? -2.698 22.094 54.406 1.00 4.82 ? 423 TRP B CD2 1 ATOM 5630 N NE1 . TRP B 1 342 ? -1.844 24.156 54.623 1.00 6.63 ? 423 TRP B NE1 1 ATOM 5631 C CE2 . TRP B 1 342 ? -1.594 22.833 54.878 1.00 6.38 ? 423 TRP B CE2 1 ATOM 5632 C CE3 . TRP B 1 342 ? -2.688 20.702 54.545 1.00 6.42 ? 423 TRP B CE3 1 ATOM 5633 C CZ2 . TRP B 1 342 ? -0.494 22.228 55.484 1.00 6.04 ? 423 TRP B CZ2 1 ATOM 5634 C CZ3 . TRP B 1 342 ? -1.593 20.102 55.148 1.00 5.67 ? 423 TRP B CZ3 1 ATOM 5635 C CH2 . TRP B 1 342 ? -0.512 20.865 55.610 1.00 7.77 ? 423 TRP B CH2 1 ATOM 5636 N N . VAL B 1 343 ? -6.302 20.147 54.482 1.00 1.47 ? 424 VAL B N 1 ATOM 5637 C CA . VAL B 1 343 ? -6.070 18.845 55.092 1.00 3.91 ? 424 VAL B CA 1 ATOM 5638 C C . VAL B 1 343 ? -5.440 17.881 54.097 1.00 4.26 ? 424 VAL B C 1 ATOM 5639 O O . VAL B 1 343 ? -5.914 17.730 52.970 1.00 5.27 ? 424 VAL B O 1 ATOM 5640 C CB . VAL B 1 343 ? -7.374 18.210 55.620 1.00 3.66 ? 424 VAL B CB 1 ATOM 5641 C CG1 . VAL B 1 343 ? -7.052 16.944 56.412 1.00 4.27 ? 424 VAL B CG1 1 ATOM 5642 C CG2 . VAL B 1 343 ? -8.136 19.197 56.481 1.00 4.03 ? 424 VAL B CG2 1 ATOM 5643 N N . GLU B 1 344 ? -4.365 17.232 54.528 1.00 5.00 ? 425 GLU B N 1 ATOM 5644 C CA . GLU B 1 344 ? -3.714 16.199 53.739 1.00 7.60 ? 425 GLU B CA 1 ATOM 5645 C C . GLU B 1 344 ? -4.364 14.855 54.047 1.00 7.17 ? 425 GLU B C 1 ATOM 5646 O O . GLU B 1 344 ? -4.509 14.478 55.210 1.00 7.61 ? 425 GLU B O 1 ATOM 5647 C CB . GLU B 1 344 ? -2.223 16.151 54.073 1.00 8.75 ? 425 GLU B CB 1 ATOM 5648 C CG . GLU B 1 344 ? -1.438 15.067 53.354 1.00 10.62 ? 425 GLU B CG 1 ATOM 5649 C CD . GLU B 1 344 ? -0.079 14.834 53.985 1.00 13.83 ? 425 GLU B CD 1 ATOM 5650 O OE1 . GLU B 1 344 ? 0.006 14.857 55.233 1.00 10.25 ? 425 GLU B OE1 1 ATOM 5651 O OE2 . GLU B 1 344 ? 0.902 14.626 53.239 1.00 11.89 ? 425 GLU B OE2 1 ATOM 5652 N N . LEU B 1 345 ? -4.769 14.144 53.001 1.00 5.45 ? 426 LEU B N 1 ATOM 5653 C CA . LEU B 1 345 ? -5.367 12.826 53.160 1.00 6.87 ? 426 LEU B CA 1 ATOM 5654 C C . LEU B 1 345 ? -4.358 11.765 52.733 1.00 9.09 ? 426 LEU B C 1 ATOM 5655 O O . LEU B 1 345 ? -4.199 11.487 51.543 1.00 10.57 ? 426 LEU B O 1 ATOM 5656 C CB . LEU B 1 345 ? -6.648 12.722 52.330 1.00 5.88 ? 426 LEU B CB 1 ATOM 5657 C CG . LEU B 1 345 ? -7.623 13.894 52.494 1.00 7.65 ? 426 LEU B CG 1 ATOM 5658 C CD1 . LEU B 1 345 ? -8.802 13.761 51.540 1.00 8.94 ? 426 LEU B CD1 1 ATOM 5659 C CD2 . LEU B 1 345 ? -8.104 14.014 53.936 1.00 7.11 ? 426 LEU B CD2 1 ATOM 5660 N N . ILE B 1 346 ? -3.676 11.180 53.713 1.00 5.90 ? 427 ILE B N 1 ATOM 5661 C CA . ILE B 1 346 ? -2.571 10.263 53.448 1.00 5.61 ? 427 ILE B CA 1 ATOM 5662 C C . ILE B 1 346 ? -3.041 8.855 53.096 1.00 8.19 ? 427 ILE B C 1 ATOM 5663 O O . ILE B 1 346 ? -3.822 8.254 53.830 1.00 8.81 ? 427 ILE B O 1 ATOM 5664 C CB . ILE B 1 346 ? -1.626 10.165 54.664 1.00 7.45 ? 427 ILE B CB 1 ATOM 5665 C CG1 . ILE B 1 346 ? -1.178 11.560 55.106 1.00 9.06 ? 427 ILE B CG1 1 ATOM 5666 C CG2 . ILE B 1 346 ? -0.428 9.279 54.339 1.00 8.94 ? 427 ILE B CG2 1 ATOM 5667 C CD1 . ILE B 1 346 ? -0.371 11.568 56.390 1.00 10.49 ? 427 ILE B CD1 1 ATOM 5668 N N . ARG B 1 347 ? -2.553 8.330 51.975 1.00 7.92 ? 428 ARG B N 1 ATOM 5669 C CA . ARG B 1 347 ? -2.871 6.964 51.570 1.00 7.58 ? 428 ARG B CA 1 ATOM 5670 C C . ARG B 1 347 ? -1.605 6.115 51.455 1.00 10.32 ? 428 ARG B C 1 ATOM 5671 O O . ARG B 1 347 ? -0.534 6.626 51.119 1.00 8.44 ? 428 ARG B O 1 ATOM 5672 C CB . ARG B 1 347 ? -3.620 6.959 50.234 1.00 9.65 ? 428 ARG B CB 1 ATOM 5673 C CG . ARG B 1 347 ? -4.922 7.752 50.227 1.00 10.14 ? 428 ARG B CG 1 ATOM 5674 C CD . ARG B 1 347 ? -5.877 7.283 51.316 1.00 9.14 ? 428 ARG B CD 1 ATOM 5675 N NE . ARG B 1 347 ? -6.141 5.847 51.251 1.00 8.38 ? 428 ARG B NE 1 ATOM 5676 C CZ . ARG B 1 347 ? -7.100 5.294 50.517 1.00 9.58 ? 428 ARG B CZ 1 ATOM 5677 N NH1 . ARG B 1 347 ? -7.891 6.053 49.770 1.00 10.46 ? 428 ARG B NH1 1 ATOM 5678 N NH2 . ARG B 1 347 ? -7.268 3.979 50.527 1.00 9.54 ? 428 ARG B NH2 1 ATOM 5679 N N . GLY B 1 348 ? -1.728 4.820 51.729 1.00 8.79 ? 429 GLY B N 1 ATOM 5680 C CA . GLY B 1 348 ? -0.604 3.910 51.604 1.00 10.52 ? 429 GLY B CA 1 ATOM 5681 C C . GLY B 1 348 ? 0.027 3.555 52.935 1.00 12.91 ? 429 GLY B C 1 ATOM 5682 O O . GLY B 1 348 ? -0.655 3.382 53.945 1.00 12.39 ? 429 GLY B O 1 ATOM 5683 N N . ARG B 1 349 ? 1.347 3.447 52.935 1.00 16.09 ? 430 ARG B N 1 ATOM 5684 C CA . ARG B 1 349 ? 2.072 3.077 54.139 1.00 15.94 ? 430 ARG B CA 1 ATOM 5685 C C . ARG B 1 349 ? 2.041 4.184 55.193 1.00 18.01 ? 430 ARG B C 1 ATOM 5686 O O . ARG B 1 349 ? 1.973 5.370 54.858 1.00 19.38 ? 430 ARG B O 1 ATOM 5687 C CB . ARG B 1 349 ? 3.519 2.721 53.789 1.00 20.90 ? 430 ARG B CB 1 ATOM 5688 C CG . ARG B 1 349 ? 3.717 1.339 53.177 1.00 22.51 ? 430 ARG B CG 1 ATOM 5689 C CD . ARG B 1 349 ? 3.533 0.273 54.237 1.00 35.00 ? 430 ARG B CD 1 ATOM 5690 N NE . ARG B 1 349 ? 2.988 -0.967 53.694 1.00 37.31 ? 430 ARG B NE 1 ATOM 5691 C CZ . ARG B 1 349 ? 3.705 -1.885 53.055 1.00 40.53 ? 430 ARG B CZ 1 ATOM 5692 N NH1 . ARG B 1 349 ? 5.003 -1.701 52.853 1.00 49.99 ? 430 ARG B NH1 1 ATOM 5693 N NH2 . ARG B 1 349 ? 3.116 -2.982 52.607 1.00 35.16 ? 430 ARG B NH2 1 ATOM 5694 N N . PRO B 1 350 ? 2.112 3.796 56.478 1.00 19.91 ? 431 PRO B N 1 ATOM 5695 C CA . PRO B 1 350 ? 2.260 2.408 56.931 1.00 19.34 ? 431 PRO B CA 1 ATOM 5696 C C . PRO B 1 350 ? 0.928 1.687 57.152 1.00 22.93 ? 431 PRO B C 1 ATOM 5697 O O . PRO B 1 350 ? 0.929 0.480 57.399 1.00 24.78 ? 431 PRO B O 1 ATOM 5698 C CB . PRO B 1 350 ? 2.969 2.558 58.290 1.00 26.94 ? 431 PRO B CB 1 ATOM 5699 C CG . PRO B 1 350 ? 3.189 4.052 58.495 1.00 32.89 ? 431 PRO B CG 1 ATOM 5700 C CD . PRO B 1 350 ? 2.201 4.731 57.607 1.00 25.90 ? 431 PRO B CD 1 ATOM 5701 N N . LYS B 1 351 ? -0.185 2.411 57.076 1.00 18.51 ? 432 LYS B N 1 ATOM 5702 C CA . LYS B 1 351 ? -1.485 1.841 57.438 1.00 23.01 ? 432 LYS B CA 1 ATOM 5703 C C . LYS B 1 351 ? -2.079 0.906 56.384 1.00 24.37 ? 432 LYS B C 1 ATOM 5704 O O . LYS B 1 351 ? -2.957 0.100 56.689 1.00 20.62 ? 432 LYS B O 1 ATOM 5705 C CB . LYS B 1 351 ? -2.490 2.947 57.775 1.00 22.10 ? 432 LYS B CB 1 ATOM 5706 C CG . LYS B 1 351 ? -2.154 3.742 59.028 1.00 25.73 ? 432 LYS B CG 1 ATOM 5707 C CD . LYS B 1 351 ? -1.803 2.817 60.184 1.00 31.21 ? 432 LYS B CD 1 ATOM 5708 C CE . LYS B 1 351 ? -1.809 3.550 61.522 1.00 33.98 ? 432 LYS B CE 1 ATOM 5709 N NZ . LYS B 1 351 ? -3.126 3.451 62.209 1.00 32.86 ? 432 LYS B NZ 1 ATOM 5710 N N . GLU B 1 352 ? -1.600 1.011 55.150 1.00 15.63 ? 433 GLU B N 1 ATOM 5711 C CA . GLU B 1 352 ? -2.153 0.217 54.056 1.00 16.78 ? 433 GLU B CA 1 ATOM 5712 C C . GLU B 1 352 ? -1.069 -0.575 53.323 1.00 13.95 ? 433 GLU B C 1 ATOM 5713 O O . GLU B 1 352 ? 0.094 -0.171 53.291 1.00 15.79 ? 433 GLU B O 1 ATOM 5714 C CB . GLU B 1 352 ? -2.930 1.113 53.088 1.00 15.87 ? 433 GLU B CB 1 ATOM 5715 C CG . GLU B 1 352 ? -4.006 1.950 53.773 1.00 15.82 ? 433 GLU B CG 1 ATOM 5716 C CD . GLU B 1 352 ? -4.751 2.862 52.817 1.00 16.80 ? 433 GLU B CD 1 ATOM 5717 O OE1 . GLU B 1 352 ? -4.354 4.038 52.683 1.00 11.24 ? 433 GLU B OE1 1 ATOM 5718 O OE2 . GLU B 1 352 ? -5.736 2.402 52.202 1.00 15.07 ? 433 GLU B OE2 1 ATOM 5719 N N . ASN B 1 353 ? -1.458 -1.705 52.740 1.00 16.43 ? 435 ASN B N 1 ATOM 5720 C CA . ASN B 1 353 ? -0.498 -2.633 52.145 1.00 20.07 ? 435 ASN B CA 1 ATOM 5721 C C . ASN B 1 353 ? -0.047 -2.256 50.735 1.00 14.86 ? 435 ASN B C 1 ATOM 5722 O O . ASN B 1 353 ? -0.354 -2.949 49.765 1.00 15.66 ? 435 ASN B O 1 ATOM 5723 C CB . ASN B 1 353 ? -1.049 -4.061 52.164 1.00 24.94 ? 435 ASN B CB 1 ATOM 5724 C CG . ASN B 1 353 ? -1.047 -4.667 53.555 1.00 28.68 ? 435 ASN B CG 1 ATOM 5725 O OD1 . ASN B 1 353 ? -1.888 -5.504 53.883 1.00 36.11 ? 435 ASN B OD1 1 ATOM 5726 N ND2 . ASN B 1 353 ? -0.100 -4.243 54.383 1.00 33.35 ? 435 ASN B ND2 1 ATOM 5727 N N . THR B 1 354 ? 0.691 -1.156 50.636 1.00 12.37 ? 436 THR B N 1 ATOM 5728 C CA . THR B 1 354 ? 1.245 -0.706 49.366 1.00 11.24 ? 436 THR B CA 1 ATOM 5729 C C . THR B 1 354 ? 2.755 -0.561 49.491 1.00 13.12 ? 436 THR B C 1 ATOM 5730 O O . THR B 1 354 ? 3.309 -0.682 50.582 1.00 14.18 ? 436 THR B O 1 ATOM 5731 C CB . THR B 1 354 ? 0.663 0.653 48.959 1.00 12.18 ? 436 THR B CB 1 ATOM 5732 O OG1 . THR B 1 354 ? 0.892 1.597 50.013 1.00 12.36 ? 436 THR B OG1 1 ATOM 5733 C CG2 . THR B 1 354 ? -0.835 0.541 48.701 1.00 10.77 ? 436 THR B CG2 1 ATOM 5734 N N . ILE B 1 355 ? 3.422 -0.300 48.373 1.00 10.78 ? 437 ILE B N 1 ATOM 5735 C CA . ILE B 1 355 ? 4.857 -0.055 48.402 1.00 10.63 ? 437 ILE B CA 1 ATOM 5736 C C . ILE B 1 355 ? 5.128 1.434 48.573 1.00 9.88 ? 437 ILE B C 1 ATOM 5737 O O . ILE B 1 355 ? 6.261 1.843 48.830 1.00 10.83 ? 437 ILE B O 1 ATOM 5738 C CB . ILE B 1 355 ? 5.544 -0.544 47.113 1.00 13.24 ? 437 ILE B CB 1 ATOM 5739 C CG1 . ILE B 1 355 ? 5.094 0.293 45.912 1.00 11.06 ? 437 ILE B CG1 1 ATOM 5740 C CG2 . ILE B 1 355 ? 5.258 -2.024 46.884 1.00 15.62 ? 437 ILE B CG2 1 ATOM 5741 C CD1 . ILE B 1 355 ? 5.784 -0.083 44.618 1.00 14.91 ? 437 ILE B CD1 1 ATOM 5742 N N . TRP B 1 356 ? 4.073 2.235 48.450 1.00 8.25 ? 438 TRP B N 1 ATOM 5743 C CA . TRP B 1 356 ? 4.202 3.688 48.388 1.00 7.85 ? 438 TRP B CA 1 ATOM 5744 C C . TRP B 1 356 ? 3.386 4.413 49.456 1.00 8.69 ? 438 TRP B C 1 ATOM 5745 O O . TRP B 1 356 ? 2.537 3.819 50.123 1.00 7.90 ? 438 TRP B O 1 ATOM 5746 C CB . TRP B 1 356 ? 3.763 4.179 47.007 1.00 6.98 ? 438 TRP B CB 1 ATOM 5747 C CG . TRP B 1 356 ? 2.397 3.691 46.618 1.00 7.43 ? 438 TRP B CG 1 ATOM 5748 C CD1 . TRP B 1 356 ? 2.094 2.515 45.993 1.00 9.83 ? 438 TRP B CD1 1 ATOM 5749 C CD2 . TRP B 1 356 ? 1.148 4.360 46.839 1.00 8.29 ? 438 TRP B CD2 1 ATOM 5750 N NE1 . TRP B 1 356 ? 0.735 2.413 45.808 1.00 9.94 ? 438 TRP B NE1 1 ATOM 5751 C CE2 . TRP B 1 356 ? 0.133 3.532 46.318 1.00 9.93 ? 438 TRP B CE2 1 ATOM 5752 C CE3 . TRP B 1 356 ? 0.792 5.580 47.423 1.00 8.63 ? 438 TRP B CE3 1 ATOM 5753 C CZ2 . TRP B 1 356 ? -1.215 3.887 46.361 1.00 12.48 ? 438 TRP B CZ2 1 ATOM 5754 C CZ3 . TRP B 1 356 ? -0.548 5.928 47.467 1.00 10.33 ? 438 TRP B CZ3 1 ATOM 5755 C CH2 . TRP B 1 356 ? -1.534 5.084 46.940 1.00 10.75 ? 438 TRP B CH2 1 ATOM 5756 N N . THR B 1 357 ? 3.653 5.708 49.601 1.00 8.90 ? 439 THR B N 1 ATOM 5757 C CA . THR B 1 357 ? 2.866 6.585 50.458 1.00 11.16 ? 439 THR B CA 1 ATOM 5758 C C . THR B 1 357 ? 2.674 7.921 49.752 1.00 10.41 ? 439 THR B C 1 ATOM 5759 O O . THR B 1 357 ? 3.634 8.512 49.262 1.00 8.04 ? 439 THR B O 1 ATOM 5760 C CB . THR B 1 357 ? 3.564 6.839 51.807 1.00 16.26 ? 439 THR B CB 1 ATOM 5761 O OG1 . THR B 1 357 ? 3.678 5.609 52.532 1.00 12.20 ? 439 THR B OG1 1 ATOM 5762 C CG2 . THR B 1 357 ? 2.771 7.841 52.637 1.00 14.31 ? 439 THR B CG2 1 ATOM 5763 N N . SER B 1 358 ? 1.433 8.394 49.693 1.00 8.17 ? 440 SER B N 1 ATOM 5764 C CA . SER B 1 358 ? 1.142 9.677 49.066 1.00 9.42 ? 440 SER B CA 1 ATOM 5765 C C . SER B 1 358 ? -0.136 10.265 49.645 1.00 13.98 ? 440 SER B C 1 ATOM 5766 O O . SER B 1 358 ? -0.893 9.573 50.321 1.00 12.43 ? 440 SER B O 1 ATOM 5767 C CB . SER B 1 358 ? 1.011 9.521 47.549 1.00 10.59 ? 440 SER B CB 1 ATOM 5768 O OG . SER B 1 358 ? 0.998 10.785 46.907 1.00 10.08 ? 440 SER B OG 1 ATOM 5769 N N . GLY B 1 359 ? -0.378 11.542 49.380 1.00 15.79 ? 441 GLY B N 1 ATOM 5770 C CA . GLY B 1 359 ? -1.571 12.188 49.891 1.00 11.86 ? 441 GLY B CA 1 ATOM 5771 C C . GLY B 1 359 ? -2.287 13.029 48.854 1.00 13.70 ? 441 GLY B C 1 ATOM 5772 O O . GLY B 1 359 ? -1.669 13.529 47.916 1.00 17.67 ? 441 GLY B O 1 ATOM 5773 N N . SER B 1 360 ? -3.600 13.162 49.013 1.00 8.56 ? 442 SER B N 1 ATOM 5774 C CA . SER B 1 360 ? -4.364 14.147 48.259 1.00 10.04 ? 442 SER B CA 1 ATOM 5775 C C . SER B 1 360 ? -4.757 15.238 49.243 1.00 10.09 ? 442 SER B C 1 ATOM 5776 O O . SER B 1 360 ? -4.394 15.174 50.418 1.00 10.17 ? 442 SER B O 1 ATOM 5777 C CB . SER B 1 360 ? -5.599 13.520 47.608 1.00 9.51 ? 442 SER B CB 1 ATOM 5778 O OG . SER B 1 360 ? -6.559 13.139 48.575 1.00 11.11 ? 442 SER B OG 1 ATOM 5779 N N . SER B 1 361 ? -5.492 16.242 48.783 1.00 9.00 ? 443 SER B N 1 ATOM 5780 C CA . SER B 1 361 ? -5.806 17.357 49.666 1.00 9.65 ? 443 SER B CA 1 ATOM 5781 C C . SER B 1 361 ? -7.218 17.902 49.508 1.00 8.68 ? 443 SER B C 1 ATOM 5782 O O . SER B 1 361 ? -7.845 17.765 48.457 1.00 9.17 ? 443 SER B O 1 ATOM 5783 C CB . SER B 1 361 ? -4.788 18.488 49.484 1.00 11.05 ? 443 SER B CB 1 ATOM 5784 O OG . SER B 1 361 ? -4.992 19.167 48.257 1.00 15.56 ? 443 SER B OG 1 ATOM 5785 N N . ILE B 1 362 ? -7.706 18.506 50.585 1.00 4.01 ? 444 ILE B N 1 ATOM 5786 C CA . ILE B 1 362 ? -8.933 19.285 50.575 1.00 4.72 ? 444 ILE B CA 1 ATOM 5787 C C . ILE B 1 362 ? -8.645 20.579 51.324 1.00 6.07 ? 444 ILE B C 1 ATOM 5788 O O . ILE B 1 362 ? -7.722 20.634 52.139 1.00 5.81 ? 444 ILE B O 1 ATOM 5789 C CB . ILE B 1 362 ? -10.090 18.543 51.277 1.00 5.11 ? 444 ILE B CB 1 ATOM 5790 C CG1 . ILE B 1 362 ? -9.688 18.156 52.702 1.00 4.69 ? 444 ILE B CG1 1 ATOM 5791 C CG2 . ILE B 1 362 ? -10.505 17.312 50.482 1.00 8.26 ? 444 ILE B CG2 1 ATOM 5792 C CD1 . ILE B 1 362 ? -10.768 17.405 53.458 1.00 4.88 ? 444 ILE B CD1 1 ATOM 5793 N N . SER B 1 363 ? -9.424 21.620 51.048 1.00 5.06 ? 445 SER B N 1 ATOM 5794 C CA . SER B 1 363 ? -9.251 22.896 51.733 1.00 4.55 ? 445 SER B CA 1 ATOM 5795 C C . SER B 1 363 ? -10.594 23.582 51.948 1.00 6.82 ? 445 SER B C 1 ATOM 5796 O O . SER B 1 363 ? -11.551 23.339 51.210 1.00 6.31 ? 445 SER B O 1 ATOM 5797 C CB . SER B 1 363 ? -8.309 23.817 50.954 1.00 7.85 ? 445 SER B CB 1 ATOM 5798 O OG . SER B 1 363 ? -8.936 24.330 49.791 1.00 7.94 ? 445 SER B OG 1 ATOM 5799 N N . PHE B 1 364 ? -10.651 24.432 52.969 1.00 4.98 ? 446 PHE B N 1 ATOM 5800 C CA . PHE B 1 364 ? -11.875 25.128 53.353 1.00 7.31 ? 446 PHE B CA 1 ATOM 5801 C C . PHE B 1 364 ? -11.555 26.578 53.704 1.00 7.11 ? 446 PHE B C 1 ATOM 5802 O O . PHE B 1 364 ? -10.439 26.885 54.125 1.00 7.50 ? 446 PHE B O 1 ATOM 5803 C CB . PHE B 1 364 ? -12.511 24.448 54.574 1.00 5.58 ? 446 PHE B CB 1 ATOM 5804 C CG . PHE B 1 364 ? -12.903 23.018 54.342 1.00 5.14 ? 446 PHE B CG 1 ATOM 5805 C CD1 . PHE B 1 364 ? -11.945 22.017 54.306 1.00 7.18 ? 446 PHE B CD1 1 ATOM 5806 C CD2 . PHE B 1 364 ? -14.234 22.672 54.174 1.00 7.47 ? 446 PHE B CD2 1 ATOM 5807 C CE1 . PHE B 1 364 ? -12.304 20.700 54.093 1.00 9.07 ? 446 PHE B CE1 1 ATOM 5808 C CE2 . PHE B 1 364 ? -14.601 21.352 53.961 1.00 7.87 ? 446 PHE B CE2 1 ATOM 5809 C CZ . PHE B 1 364 ? -13.635 20.367 53.921 1.00 7.70 ? 446 PHE B CZ 1 ATOM 5810 N N . CYS B 1 365 ? -12.531 27.465 53.537 1.00 6.67 ? 447 CYS B N 1 ATOM 5811 C CA . CYS B 1 365 ? -12.368 28.849 53.963 1.00 5.76 ? 447 CYS B CA 1 ATOM 5812 C C . CYS B 1 365 ? -13.462 29.270 54.936 1.00 5.67 ? 447 CYS B C 1 ATOM 5813 O O . CYS B 1 365 ? -14.606 28.813 54.834 1.00 7.15 ? 447 CYS B O 1 ATOM 5814 C CB . CYS B 1 365 ? -12.308 29.792 52.760 1.00 11.23 ? 447 CYS B CB 1 ATOM 5815 S SG . CYS B 1 365 ? -10.670 29.894 51.998 1.00 19.58 ? 447 CYS B SG 1 ATOM 5816 N N . GLY B 1 366 ? -13.105 30.135 55.882 1.00 5.98 ? 448 GLY B N 1 ATOM 5817 C CA . GLY B 1 366 ? -14.038 30.554 56.914 1.00 7.66 ? 448 GLY B CA 1 ATOM 5818 C C . GLY B 1 366 ? -15.064 31.546 56.411 1.00 8.30 ? 448 GLY B C 1 ATOM 5819 O O . GLY B 1 366 ? -14.719 32.484 55.690 1.00 12.58 ? 448 GLY B O 1 ATOM 5820 N N . VAL B 1 367 ? -16.324 31.341 56.790 1.00 8.21 ? 449 VAL B N 1 ATOM 5821 C CA . VAL B 1 367 ? -17.398 32.246 56.400 1.00 5.33 ? 449 VAL B CA 1 ATOM 5822 C C . VAL B 1 367 ? -18.362 32.472 57.561 1.00 6.88 ? 449 VAL B C 1 ATOM 5823 O O . VAL B 1 367 ? -18.271 31.810 58.595 1.00 6.43 ? 449 VAL B O 1 ATOM 5824 C CB . VAL B 1 367 ? -18.190 31.701 55.198 1.00 7.44 ? 449 VAL B CB 1 ATOM 5825 C CG1 . VAL B 1 367 ? -17.277 31.495 53.998 1.00 7.52 ? 449 VAL B CG1 1 ATOM 5826 C CG2 . VAL B 1 367 ? -18.889 30.404 55.572 1.00 8.36 ? 449 VAL B CG2 1 ATOM 5827 N N . ASN B 1 368 ? -19.290 33.406 57.385 1.00 9.24 ? 450 ASN B N 1 ATOM 5828 C CA . ASN B 1 368 ? -20.318 33.659 58.393 1.00 11.72 ? 450 ASN B CA 1 ATOM 5829 C C . ASN B 1 368 ? -21.715 33.314 57.889 1.00 17.13 ? 450 ASN B C 1 ATOM 5830 O O . ASN B 1 368 ? -22.711 33.517 58.587 1.00 17.65 ? 450 ASN B O 1 ATOM 5831 C CB . ASN B 1 368 ? -20.264 35.107 58.875 1.00 15.88 ? 450 ASN B CB 1 ATOM 5832 C CG . ASN B 1 368 ? -19.143 35.343 59.860 1.00 18.74 ? 450 ASN B CG 1 ATOM 5833 O OD1 . ASN B 1 368 ? -19.126 34.761 60.943 1.00 20.44 ? 450 ASN B OD1 1 ATOM 5834 N ND2 . ASN B 1 368 ? -18.197 36.197 59.490 1.00 23.78 ? 450 ASN B ND2 1 ATOM 5835 N N . SER B 1 369 ? -21.778 32.796 56.669 1.00 10.61 ? 451 SER B N 1 ATOM 5836 C CA . SER B 1 369 ? -23.031 32.312 56.103 1.00 12.23 ? 451 SER B CA 1 ATOM 5837 C C . SER B 1 369 ? -23.202 30.836 56.448 1.00 10.71 ? 451 SER B C 1 ATOM 5838 O O . SER B 1 369 ? -22.367 30.259 57.141 1.00 9.84 ? 451 SER B O 1 ATOM 5839 C CB . SER B 1 369 ? -23.051 32.524 54.589 1.00 13.12 ? 451 SER B CB 1 ATOM 5840 O OG . SER B 1 369 ? -21.852 32.058 53.995 1.00 11.30 ? 451 SER B OG 1 ATOM 5841 N N . ASP B 1 370 ? -24.278 30.225 55.963 1.00 11.45 ? 452 ASP B N 1 ATOM 5842 C CA . ASP B 1 370 ? -24.592 28.844 56.320 1.00 12.60 ? 452 ASP B CA 1 ATOM 5843 C C . ASP B 1 370 ? -23.584 27.835 55.769 1.00 10.75 ? 452 ASP B C 1 ATOM 5844 O O . ASP B 1 370 ? -23.114 27.959 54.637 1.00 10.68 ? 452 ASP B O 1 ATOM 5845 C CB . ASP B 1 370 ? -26.009 28.482 55.866 1.00 12.84 ? 452 ASP B CB 1 ATOM 5846 C CG . ASP B 1 370 ? -27.079 29.235 56.638 1.00 18.66 ? 452 ASP B CG 1 ATOM 5847 O OD1 . ASP B 1 370 ? -26.776 29.745 57.737 1.00 24.45 ? 452 ASP B OD1 1 ATOM 5848 O OD2 . ASP B 1 370 ? -28.226 29.314 56.150 1.00 21.44 ? 452 ASP B OD2 1 ATOM 5849 N N . THR B 1 371 ? -23.253 26.839 56.585 1.00 8.29 ? 453 THR B N 1 ATOM 5850 C CA . THR B 1 371 ? -22.342 25.773 56.184 1.00 5.40 ? 453 THR B CA 1 ATOM 5851 C C . THR B 1 371 ? -22.879 24.421 56.638 1.00 7.61 ? 453 THR B C 1 ATOM 5852 O O . THR B 1 371 ? -23.906 24.346 57.311 1.00 7.93 ? 453 THR B O 1 ATOM 5853 C CB . THR B 1 371 ? -20.932 25.970 56.780 1.00 10.42 ? 453 THR B CB 1 ATOM 5854 O OG1 . THR B 1 371 ? -21.029 26.111 58.203 1.00 11.26 ? 453 THR B OG1 1 ATOM 5855 C CG2 . THR B 1 371 ? -20.262 27.208 56.195 1.00 7.19 ? 453 THR B CG2 1 ATOM 5856 N N . VAL B 1 372 ? -22.178 23.353 56.278 1.00 8.27 ? 454 VAL B N 1 ATOM 5857 C CA . VAL B 1 372 ? -22.606 22.013 56.660 1.00 7.46 ? 454 VAL B CA 1 ATOM 5858 C C . VAL B 1 372 ? -21.416 21.087 56.886 1.00 9.29 ? 454 VAL B C 1 ATOM 5859 O O . VAL B 1 372 ? -20.386 21.201 56.219 1.00 8.35 ? 454 VAL B O 1 ATOM 5860 C CB . VAL B 1 372 ? -23.547 21.394 55.599 1.00 7.98 ? 454 VAL B CB 1 ATOM 5861 C CG1 . VAL B 1 372 ? -22.782 21.092 54.316 1.00 8.01 ? 454 VAL B CG1 1 ATOM 5862 C CG2 . VAL B 1 372 ? -24.209 20.137 56.135 1.00 10.09 ? 454 VAL B CG2 1 ATOM 5863 N N . GLY B 1 373 ? -21.561 20.179 57.844 1.00 8.90 ? 455 GLY B N 1 ATOM 5864 C CA . GLY B 1 373 ? -20.561 19.154 58.070 1.00 8.39 ? 455 GLY B CA 1 ATOM 5865 C C . GLY B 1 373 ? -20.797 17.980 57.141 1.00 11.40 ? 455 GLY B C 1 ATOM 5866 O O . GLY B 1 373 ? -21.930 17.706 56.747 1.00 13.16 ? 455 GLY B O 1 ATOM 5867 N N . TRP B 1 374 ? -19.722 17.293 56.777 1.00 9.96 ? 456 TRP B N 1 ATOM 5868 C CA . TRP B 1 374 ? -19.823 16.100 55.948 1.00 8.78 ? 456 TRP B CA 1 ATOM 5869 C C . TRP B 1 374 ? -18.507 15.347 56.023 1.00 8.71 ? 456 TRP B C 1 ATOM 5870 O O . TRP B 1 374 ? -17.713 15.553 56.942 1.00 8.09 ? 456 TRP B O 1 ATOM 5871 C CB . TRP B 1 374 ? -20.129 16.474 54.494 1.00 7.86 ? 456 TRP B CB 1 ATOM 5872 C CG . TRP B 1 374 ? -20.892 15.417 53.730 1.00 8.55 ? 456 TRP B CG 1 ATOM 5873 C CD1 . TRP B 1 374 ? -21.753 14.492 54.248 1.00 11.32 ? 456 TRP B CD1 1 ATOM 5874 C CD2 . TRP B 1 374 ? -20.881 15.201 52.311 1.00 8.39 ? 456 TRP B CD2 1 ATOM 5875 N NE1 . TRP B 1 374 ? -22.268 13.707 53.243 1.00 11.77 ? 456 TRP B NE1 1 ATOM 5876 C CE2 . TRP B 1 374 ? -21.750 14.123 52.044 1.00 12.13 ? 456 TRP B CE2 1 ATOM 5877 C CE3 . TRP B 1 374 ? -20.217 15.812 51.242 1.00 9.40 ? 456 TRP B CE3 1 ATOM 5878 C CZ2 . TRP B 1 374 ? -21.973 13.643 50.753 1.00 12.79 ? 456 TRP B CZ2 1 ATOM 5879 C CZ3 . TRP B 1 374 ? -20.440 15.333 49.958 1.00 10.48 ? 456 TRP B CZ3 1 ATOM 5880 C CH2 . TRP B 1 374 ? -21.310 14.259 49.726 1.00 11.01 ? 456 TRP B CH2 1 ATOM 5881 N N . SER B 1 375 ? -18.283 14.471 55.053 1.00 9.14 ? 457 SER B N 1 ATOM 5882 C CA . SER B 1 375 ? -17.001 13.801 54.916 1.00 8.38 ? 457 SER B CA 1 ATOM 5883 C C . SER B 1 375 ? -16.550 13.874 53.465 1.00 7.51 ? 457 SER B C 1 ATOM 5884 O O . SER B 1 375 ? -17.237 13.384 52.570 1.00 7.62 ? 457 SER B O 1 ATOM 5885 C CB . SER B 1 375 ? -17.103 12.343 55.361 1.00 12.53 ? 457 SER B CB 1 ATOM 5886 O OG . SER B 1 375 ? -15.850 11.693 55.238 1.00 8.05 ? 457 SER B OG 1 ATOM 5887 N N . TRP B 1 376 ? -15.402 14.503 53.236 1.00 7.58 ? 458 TRP B N 1 ATOM 5888 C CA . TRP B 1 376 ? -14.819 14.584 51.900 1.00 8.49 ? 458 TRP B CA 1 ATOM 5889 C C . TRP B 1 376 ? -13.488 13.840 51.890 1.00 7.61 ? 458 TRP B C 1 ATOM 5890 O O . TRP B 1 376 ? -12.431 14.462 51.962 1.00 8.36 ? 458 TRP B O 1 ATOM 5891 C CB . TRP B 1 376 ? -14.588 16.042 51.496 1.00 6.87 ? 458 TRP B CB 1 ATOM 5892 C CG . TRP B 1 376 ? -15.834 16.835 51.204 1.00 6.49 ? 458 TRP B CG 1 ATOM 5893 C CD1 . TRP B 1 376 ? -16.486 16.928 50.006 1.00 8.09 ? 458 TRP B CD1 1 ATOM 5894 C CD2 . TRP B 1 376 ? -16.559 17.666 52.119 1.00 9.28 ? 458 TRP B CD2 1 ATOM 5895 N NE1 . TRP B 1 376 ? -17.577 17.755 50.123 1.00 8.87 ? 458 TRP B NE1 1 ATOM 5896 C CE2 . TRP B 1 376 ? -17.643 18.223 51.409 1.00 10.22 ? 458 TRP B CE2 1 ATOM 5897 C CE3 . TRP B 1 376 ? -16.401 17.989 53.470 1.00 9.59 ? 458 TRP B CE3 1 ATOM 5898 C CZ2 . TRP B 1 376 ? -18.564 19.084 52.007 1.00 7.10 ? 458 TRP B CZ2 1 ATOM 5899 C CZ3 . TRP B 1 376 ? -17.315 18.845 54.060 1.00 7.92 ? 458 TRP B CZ3 1 ATOM 5900 C CH2 . TRP B 1 376 ? -18.381 19.383 53.329 1.00 8.07 ? 458 TRP B CH2 1 ATOM 5901 N N . PRO B 1 377 ? -13.539 12.502 51.799 1.00 7.65 ? 459 PRO B N 1 ATOM 5902 C CA . PRO B 1 377 ? -12.361 11.636 51.917 1.00 8.86 ? 459 PRO B CA 1 ATOM 5903 C C . PRO B 1 377 ? -11.554 11.561 50.623 1.00 6.45 ? 459 PRO B C 1 ATOM 5904 O O . PRO B 1 377 ? -11.990 12.073 49.593 1.00 8.27 ? 459 PRO B O 1 ATOM 5905 C CB . PRO B 1 377 ? -12.965 10.255 52.218 1.00 11.62 ? 459 PRO B CB 1 ATOM 5906 C CG . PRO B 1 377 ? -14.464 10.460 52.319 1.00 17.01 ? 459 PRO B CG 1 ATOM 5907 C CD . PRO B 1 377 ? -14.763 11.719 51.584 1.00 8.41 ? 459 PRO B CD 1 ATOM 5908 N N . ASP B 1 378 ? -10.394 10.915 50.683 1.00 8.81 ? 460 ASP B N 1 ATOM 5909 C CA . ASP B 1 378 ? -9.544 10.742 49.507 1.00 9.35 ? 460 ASP B CA 1 ATOM 5910 C C . ASP B 1 378 ? -10.281 9.984 48.407 1.00 10.93 ? 460 ASP B C 1 ATOM 5911 O O . ASP B 1 378 ? -10.361 10.448 47.269 1.00 10.77 ? 460 ASP B O 1 ATOM 5912 C CB . ASP B 1 378 ? -8.259 10.001 49.879 1.00 8.11 ? 460 ASP B CB 1 ATOM 5913 C CG . ASP B 1 378 ? -7.413 9.669 48.669 1.00 14.53 ? 460 ASP B CG 1 ATOM 5914 O OD1 . ASP B 1 378 ? -6.784 10.592 48.112 1.00 11.00 ? 460 ASP B OD1 1 ATOM 5915 O OD2 . ASP B 1 378 ? -7.383 8.485 48.271 1.00 14.23 ? 460 ASP B OD2 1 ATOM 5916 N N . GLY B 1 379 ? -10.803 8.811 48.752 1.00 9.33 ? 461 GLY B N 1 ATOM 5917 C CA . GLY B 1 379 ? -11.662 8.058 47.857 1.00 12.19 ? 461 GLY B CA 1 ATOM 5918 C C . GLY B 1 379 ? -10.968 7.090 46.917 1.00 10.83 ? 461 GLY B C 1 ATOM 5919 O O . GLY B 1 379 ? -11.618 6.472 46.074 1.00 8.25 ? 461 GLY B O 1 ATOM 5920 N N . ALA B 1 380 ? -9.654 6.949 47.051 1.00 7.63 ? 462 ALA B N 1 ATOM 5921 C CA . ALA B 1 380 ? -8.920 6.023 46.197 1.00 7.54 ? 462 ALA B CA 1 ATOM 5922 C C . ALA B 1 380 ? -9.122 4.581 46.648 1.00 10.44 ? 462 ALA B C 1 ATOM 5923 O O . ALA B 1 380 ? -9.344 4.314 47.830 1.00 10.62 ? 462 ALA B O 1 ATOM 5924 C CB . ALA B 1 380 ? -7.442 6.370 46.173 1.00 6.99 ? 462 ALA B CB 1 ATOM 5925 N N . GLU B 1 381 ? -9.053 3.658 45.696 1.00 11.24 ? 463 GLU B N 1 ATOM 5926 C CA . GLU B 1 381 ? -9.181 2.238 45.992 1.00 11.64 ? 463 GLU B CA 1 ATOM 5927 C C . GLU B 1 381 ? -7.812 1.570 45.949 1.00 12.31 ? 463 GLU B C 1 ATOM 5928 O O . GLU B 1 381 ? -7.229 1.397 44.879 1.00 11.94 ? 463 GLU B O 1 ATOM 5929 C CB . GLU B 1 381 ? -10.124 1.566 44.993 1.00 15.78 ? 463 GLU B CB 1 ATOM 5930 C CG . GLU B 1 381 ? -11.537 2.124 44.996 1.00 27.36 ? 463 GLU B CG 1 ATOM 5931 C CD . GLU B 1 381 ? -12.324 1.731 46.233 1.00 43.30 ? 463 GLU B CD 1 ATOM 5932 O OE1 . GLU B 1 381 ? -11.814 0.920 47.034 1.00 50.21 ? 463 GLU B OE1 1 ATOM 5933 O OE2 . GLU B 1 381 ? -13.457 2.231 46.402 1.00 54.00 ? 463 GLU B OE2 1 ATOM 5934 N N . LEU B 1 382 ? -7.301 1.204 47.120 1.00 11.52 ? 464 LEU B N 1 ATOM 5935 C CA . LEU B 1 382 ? -5.997 0.557 47.225 1.00 11.52 ? 464 LEU B CA 1 ATOM 5936 C C . LEU B 1 382 ? -6.160 -0.945 47.434 1.00 13.73 ? 464 LEU B C 1 ATOM 5937 O O . LEU B 1 382 ? -7.202 -1.396 47.907 1.00 13.54 ? 464 LEU B O 1 ATOM 5938 C CB . LEU B 1 382 ? -5.193 1.164 48.378 1.00 14.04 ? 464 LEU B CB 1 ATOM 5939 C CG . LEU B 1 382 ? -4.432 2.464 48.101 1.00 13.05 ? 464 LEU B CG 1 ATOM 5940 C CD1 . LEU B 1 382 ? -5.361 3.558 47.584 1.00 10.10 ? 464 LEU B CD1 1 ATOM 5941 C CD2 . LEU B 1 382 ? -3.702 2.924 49.355 1.00 12.49 ? 464 LEU B CD2 1 ATOM 5942 N N . PRO B 1 383 ? -5.128 -1.727 47.084 1.00 13.92 ? 465 PRO B N 1 ATOM 5943 C CA . PRO B 1 383 ? -3.852 -1.286 46.507 1.00 11.13 ? 465 PRO B CA 1 ATOM 5944 C C . PRO B 1 383 ? -3.965 -0.950 45.022 1.00 12.98 ? 465 PRO B C 1 ATOM 5945 O O . PRO B 1 383 ? -5.016 -1.150 44.414 1.00 11.24 ? 465 PRO B O 1 ATOM 5946 C CB . PRO B 1 383 ? -2.946 -2.513 46.676 1.00 17.88 ? 465 PRO B CB 1 ATOM 5947 C CG . PRO B 1 383 ? -3.666 -3.422 47.628 1.00 23.71 ? 465 PRO B CG 1 ATOM 5948 C CD . PRO B 1 383 ? -5.111 -3.163 47.398 1.00 18.39 ? 465 PRO B CD 1 ATOM 5949 N N . PHE B 1 384 ? -2.872 -0.449 44.453 1.00 12.89 ? 466 PHE B N 1 ATOM 5950 C CA . PHE B 1 384 ? -2.801 -0.136 43.029 1.00 13.82 ? 466 PHE B CA 1 ATOM 5951 C C . PHE B 1 384 ? -2.128 -1.261 42.245 1.00 17.20 ? 466 PHE B C 1 ATOM 5952 O O . PHE B 1 384 ? -1.648 -2.234 42.824 1.00 16.37 ? 466 PHE B O 1 ATOM 5953 C CB . PHE B 1 384 ? -2.035 1.172 42.808 1.00 12.60 ? 466 PHE B CB 1 ATOM 5954 C CG . PHE B 1 384 ? -2.875 2.408 42.983 1.00 18.61 ? 466 PHE B CG 1 ATOM 5955 C CD1 . PHE B 1 384 ? -4.169 2.321 43.470 1.00 12.41 ? 466 PHE B CD1 1 ATOM 5956 C CD2 . PHE B 1 384 ? -2.368 3.657 42.658 1.00 13.33 ? 466 PHE B CD2 1 ATOM 5957 C CE1 . PHE B 1 384 ? -4.941 3.454 43.629 1.00 13.05 ? 466 PHE B CE1 1 ATOM 5958 C CE2 . PHE B 1 384 ? -3.138 4.795 42.815 1.00 14.11 ? 466 PHE B CE2 1 ATOM 5959 C CZ . PHE B 1 384 ? -4.426 4.693 43.300 1.00 12.73 ? 466 PHE B CZ 1 ATOM 5960 N N . THR B 1 385 ? -2.085 -1.114 40.924 1.00 13.94 ? 467 THR B N 1 ATOM 5961 C CA . THR B 1 385 ? -1.485 -2.116 40.045 1.00 15.61 ? 467 THR B CA 1 ATOM 5962 C C . THR B 1 385 ? -0.031 -2.412 40.403 1.00 19.47 ? 467 THR B C 1 ATOM 5963 O O . THR B 1 385 ? 0.393 -3.567 40.404 1.00 18.57 ? 467 THR B O 1 ATOM 5964 C CB . THR B 1 385 ? -1.553 -1.674 38.571 1.00 19.89 ? 467 THR B CB 1 ATOM 5965 O OG1 . THR B 1 385 ? -2.917 -1.438 38.206 1.00 30.16 ? 467 THR B OG1 1 ATOM 5966 C CG2 . THR B 1 385 ? -0.972 -2.747 37.663 1.00 31.13 ? 467 THR B CG2 1 ATOM 5967 N N . ILE B 1 386 ? 0.729 -1.361 40.696 1.00 13.76 ? 468 ILE B N 1 ATOM 5968 C CA . ILE B 1 386 ? 2.129 -1.503 41.078 1.00 14.76 ? 468 ILE B CA 1 ATOM 5969 C C . ILE B 1 386 ? 2.215 -2.152 42.451 1.00 18.77 ? 468 ILE B C 1 ATOM 5970 O O . ILE B 1 386 ? 3.248 -2.729 42.808 1.00 20.60 ? 468 ILE B O 1 ATOM 5971 C CB . ILE B 1 386 ? 2.832 -0.133 41.142 1.00 14.57 ? 468 ILE B CB 1 ATOM 5972 C CG1 . ILE B 1 386 ? 4.355 -0.303 41.115 1.00 14.63 ? 468 ILE B CG1 1 ATOM 5973 C CG2 . ILE B 1 386 ? 2.397 0.645 42.379 1.00 14.90 ? 468 ILE B CG2 1 ATOM 5974 C CD1 . ILE B 1 386 ? 4.896 -0.702 39.757 1.00 16.01 ? 468 ILE B CD1 1 ATOM 5975 N N . ASP B 1 387 ? 1.098 -2.065 43.180 1.00 20.64 ? 469 ASP B N 1 ATOM 5976 C CA . ASP B 1 387 ? 0.990 -2.385 44.608 1.00 27.21 ? 469 ASP B CA 1 ATOM 5977 C C . ASP B 1 387 ? 0.926 -1.118 45.460 1.00 22.34 ? 469 ASP B C 1 ATOM 5978 O O . ASP B 1 387 ? 1.884 -0.719 46.127 1.00 16.90 ? 469 ASP B O 1 ATOM 5979 C CB . ASP B 1 387 ? 2.117 -3.310 45.082 1.00 28.60 ? 469 ASP B CB 1 ATOM 5980 C CG . ASP B 1 387 ? 1.842 -4.761 44.768 1.00 29.60 ? 469 ASP B CG 1 ATOM 5981 O OD1 . ASP B 1 387 ? 1.064 -5.042 43.827 1.00 31.95 ? 469 ASP B OD1 1 ATOM 5982 O OD2 . ASP B 1 387 ? 2.405 -5.629 45.464 1.00 35.15 ? 469 ASP B OD2 1 HETATM 5983 C C1 . NAG C 2 . ? 16.460 -2.546 20.100 1.00 25.23 ? 501 NAG A C1 1 HETATM 5984 C C2 . NAG C 2 . ? 15.287 -3.529 20.127 1.00 24.64 ? 501 NAG A C2 1 HETATM 5985 C C3 . NAG C 2 . ? 15.756 -4.978 20.208 1.00 33.25 ? 501 NAG A C3 1 HETATM 5986 C C4 . NAG C 2 . ? 16.855 -5.261 19.192 1.00 26.79 ? 501 NAG A C4 1 HETATM 5987 C C5 . NAG C 2 . ? 17.940 -4.193 19.263 1.00 33.82 ? 501 NAG A C5 1 HETATM 5988 C C6 . NAG C 2 . ? 18.989 -4.423 18.182 1.00 32.81 ? 501 NAG A C6 1 HETATM 5989 C C7 . NAG C 2 . ? 13.217 -2.706 21.090 1.00 23.77 ? 501 NAG A C7 1 HETATM 5990 C C8 . NAG C 2 . ? 12.410 -2.471 22.332 1.00 22.71 ? 501 NAG A C8 1 HETATM 5991 N N2 . NAG C 2 . ? 14.418 -3.254 21.256 1.00 23.73 ? 501 NAG A N2 1 HETATM 5992 O O3 . NAG C 2 . ? 14.667 -5.852 19.997 1.00 33.09 ? 501 NAG A O3 1 HETATM 5993 O O4 . NAG C 2 . ? 17.409 -6.537 19.446 1.00 31.57 ? 501 NAG A O4 1 HETATM 5994 O O5 . NAG C 2 . ? 17.375 -2.910 19.089 1.00 25.39 ? 501 NAG A O5 1 HETATM 5995 O O6 . NAG C 2 . ? 18.343 -4.585 16.938 1.00 32.05 ? 501 NAG A O6 1 HETATM 5996 O O7 . NAG C 2 . ? 12.768 -2.393 19.990 1.00 27.43 ? 501 NAG A O7 1 HETATM 5997 C C1 . NAG D 2 . ? 17.343 -7.347 18.254 1.00 35.77 ? 502 NAG A C1 1 HETATM 5998 C C2 . NAG D 2 . ? 18.331 -8.503 18.360 1.00 36.15 ? 502 NAG A C2 1 HETATM 5999 C C3 . NAG D 2 . ? 18.333 -9.353 17.093 1.00 40.82 ? 502 NAG A C3 1 HETATM 6000 C C4 . NAG D 2 . ? 16.924 -9.614 16.563 1.00 37.11 ? 502 NAG A C4 1 HETATM 6001 C C5 . NAG D 2 . ? 16.012 -8.396 16.671 1.00 35.56 ? 502 NAG A C5 1 HETATM 6002 C C6 . NAG D 2 . ? 14.575 -8.771 16.328 1.00 37.11 ? 502 NAG A C6 1 HETATM 6003 C C7 . NAG D 2 . ? 20.228 -8.092 19.812 1.00 43.58 ? 502 NAG A C7 1 HETATM 6004 C C8 . NAG D 2 . ? 21.610 -7.524 19.952 1.00 40.78 ? 502 NAG A C8 1 HETATM 6005 N N2 . NAG D 2 . ? 19.663 -7.989 18.612 1.00 40.58 ? 502 NAG A N2 1 HETATM 6006 O O3 . NAG D 2 . ? 18.970 -10.582 17.365 1.00 38.32 ? 502 NAG A O3 1 HETATM 6007 O O4 . NAG D 2 . ? 17.017 -9.976 15.204 1.00 35.01 ? 502 NAG A O4 1 HETATM 6008 O O5 . NAG D 2 . ? 16.059 -7.857 17.973 1.00 36.06 ? 502 NAG A O5 1 HETATM 6009 O O6 . NAG D 2 . ? 14.148 -9.806 17.188 1.00 40.57 ? 502 NAG A O6 1 HETATM 6010 O O7 . NAG D 2 . ? 19.668 -8.618 20.773 1.00 45.09 ? 502 NAG A O7 1 HETATM 6011 C C1 . MAN E 3 . ? 17.701 -10.879 14.321 1.00 32.81 ? 503 MAN A C1 1 HETATM 6012 C C2 . MAN E 3 . ? 17.117 -11.350 12.995 1.00 30.96 ? 503 MAN A C2 1 HETATM 6013 C C3 . MAN E 3 . ? 16.431 -12.702 13.150 1.00 27.63 ? 503 MAN A C3 1 HETATM 6014 C C4 . MAN E 3 . ? 17.324 -13.684 13.900 1.00 34.28 ? 503 MAN A C4 1 HETATM 6015 C C5 . MAN E 3 . ? 17.892 -13.048 15.164 1.00 32.66 ? 503 MAN A C5 1 HETATM 6016 C C6 . MAN E 3 . ? 18.848 -14.001 15.872 1.00 33.77 ? 503 MAN A C6 1 HETATM 6017 O O2 . MAN E 3 . ? 18.147 -11.453 12.038 1.00 26.68 ? 503 MAN A O2 1 HETATM 6018 O O3 . MAN E 3 . ? 16.126 -13.224 11.876 1.00 24.57 ? 503 MAN A O3 1 HETATM 6019 O O4 . MAN E 3 . ? 16.576 -14.828 14.246 1.00 29.39 ? 503 MAN A O4 1 HETATM 6020 O O5 . MAN E 3 . ? 18.576 -11.862 14.825 1.00 24.75 ? 503 MAN A O5 1 HETATM 6021 O O6 . MAN E 3 . ? 19.513 -13.315 16.909 1.00 37.95 ? 503 MAN A O6 1 HETATM 6022 C C1 . MAN F 3 . ? 15.328 -14.361 11.500 1.00 23.64 ? 504 MAN A C1 1 HETATM 6023 C C2 . MAN F 3 . ? 15.604 -14.825 10.079 1.00 25.89 ? 504 MAN A C2 1 HETATM 6024 C C3 . MAN F 3 . ? 15.452 -13.630 9.152 1.00 25.05 ? 504 MAN A C3 1 HETATM 6025 C C4 . MAN F 3 . ? 14.032 -13.098 9.300 1.00 26.69 ? 504 MAN A C4 1 HETATM 6026 C C5 . MAN F 3 . ? 13.756 -12.760 10.764 1.00 22.64 ? 504 MAN A C5 1 HETATM 6027 C C6 . MAN F 3 . ? 12.315 -12.295 10.954 1.00 22.14 ? 504 MAN A C6 1 HETATM 6028 O O2 . MAN F 3 . ? 14.691 -15.835 9.721 1.00 22.23 ? 504 MAN A O2 1 HETATM 6029 O O3 . MAN F 3 . ? 15.716 -13.995 7.816 1.00 23.31 ? 504 MAN A O3 1 HETATM 6030 O O4 . MAN F 3 . ? 13.864 -11.947 8.502 1.00 23.39 ? 504 MAN A O4 1 HETATM 6031 O O5 . MAN F 3 . ? 13.998 -13.889 11.583 1.00 25.45 ? 504 MAN A O5 1 HETATM 6032 O O6 . MAN F 3 . ? 11.432 -13.386 10.811 1.00 19.50 ? 504 MAN A O6 1 HETATM 6033 C C1 . NAG G 2 . ? 27.939 48.978 33.271 1.00 33.42 ? 505 NAG A C1 1 HETATM 6034 C C2 . NAG G 2 . ? 28.590 50.275 33.756 1.00 41.29 ? 505 NAG A C2 1 HETATM 6035 C C3 . NAG G 2 . ? 27.587 51.394 34.027 1.00 46.65 ? 505 NAG A C3 1 HETATM 6036 C C4 . NAG G 2 . ? 26.547 51.479 32.922 1.00 48.00 ? 505 NAG A C4 1 HETATM 6037 C C5 . NAG G 2 . ? 25.946 50.104 32.678 1.00 44.92 ? 505 NAG A C5 1 HETATM 6038 C C6 . NAG G 2 . ? 24.876 50.168 31.597 1.00 43.49 ? 505 NAG A C6 1 HETATM 6039 C C7 . NAG G 2 . ? 30.598 50.446 35.107 1.00 44.36 ? 505 NAG A C7 1 HETATM 6040 C C8 . NAG G 2 . ? 31.274 50.102 36.401 1.00 41.58 ? 505 NAG A C8 1 HETATM 6041 N N2 . NAG G 2 . ? 29.352 50.009 34.960 1.00 41.50 ? 505 NAG A N2 1 HETATM 6042 O O3 . NAG G 2 . ? 28.271 52.626 34.115 1.00 56.21 ? 505 NAG A O3 1 HETATM 6043 O O4 . NAG G 2 . ? 25.530 52.391 33.278 1.00 44.62 ? 505 NAG A O4 1 HETATM 6044 O O5 . NAG G 2 . ? 26.964 49.215 32.278 1.00 39.38 ? 505 NAG A O5 1 HETATM 6045 O O6 . NAG G 2 . ? 25.441 50.704 30.421 1.00 41.76 ? 505 NAG A O6 1 HETATM 6046 O O7 . NAG G 2 . ? 31.186 51.102 34.247 1.00 45.22 ? 505 NAG A O7 1 HETATM 6047 CA CA . CA H 4 . ? 40.976 14.906 27.027 1.00 9.74 ? 601 CA A CA 1 HETATM 6048 CA CA . CA I 4 . ? 47.177 25.174 43.673 1.00 16.52 ? 602 CA A CA 1 HETATM 6049 CA CA . CA J 4 . ? 0.000 7.820 29.628 0.50 21.62 ? 603 CA A CA 1 HETATM 6050 C C . ACT K 5 . ? 32.827 15.129 20.838 1.00 41.71 ? 1 ACT A C 1 HETATM 6051 O O . ACT K 5 . ? 33.645 14.909 19.917 1.00 44.83 ? 1 ACT A O 1 HETATM 6052 O OXT . ACT K 5 . ? 31.736 14.524 20.764 1.00 40.42 ? 1 ACT A OXT 1 HETATM 6053 C CH3 . ACT K 5 . ? 33.133 16.065 21.969 1.00 34.36 ? 1 ACT A CH3 1 HETATM 6054 C C . ACT L 5 . ? 36.274 33.198 45.412 1.00 27.19 ? 471 ACT A C 1 HETATM 6055 O O . ACT L 5 . ? 36.143 32.475 46.426 1.00 36.04 ? 471 ACT A O 1 HETATM 6056 O OXT . ACT L 5 . ? 37.058 34.171 45.522 1.00 36.42 ? 471 ACT A OXT 1 HETATM 6057 C CH3 . ACT L 5 . ? 35.535 32.914 44.138 1.00 18.39 ? 471 ACT A CH3 1 HETATM 6058 C C . ACT M 5 . ? 51.605 24.340 23.199 1.00 43.39 ? 472 ACT A C 1 HETATM 6059 O O . ACT M 5 . ? 51.242 23.240 22.731 1.00 39.65 ? 472 ACT A O 1 HETATM 6060 O OXT . ACT M 5 . ? 51.098 24.664 24.295 1.00 48.54 ? 472 ACT A OXT 1 HETATM 6061 C CH3 . ACT M 5 . ? 52.591 25.218 22.487 1.00 43.71 ? 472 ACT A CH3 1 HETATM 6062 C C1 . NAG N 2 . ? 11.208 -1.482 47.239 1.00 60.27 ? 501 NAG B C1 1 HETATM 6063 C C2 . NAG N 2 . ? 11.395 -2.917 46.758 1.00 64.34 ? 501 NAG B C2 1 HETATM 6064 C C3 . NAG N 2 . ? 12.216 -3.732 47.750 1.00 69.86 ? 501 NAG B C3 1 HETATM 6065 C C4 . NAG N 2 . ? 13.467 -2.975 48.175 1.00 73.06 ? 501 NAG B C4 1 HETATM 6066 C C5 . NAG N 2 . ? 13.113 -1.558 48.605 1.00 74.37 ? 501 NAG B C5 1 HETATM 6067 C C6 . NAG N 2 . ? 14.358 -0.777 49.012 1.00 76.45 ? 501 NAG B C6 1 HETATM 6068 C C7 . NAG N 2 . ? 9.687 -3.910 45.347 1.00 67.74 ? 501 NAG B C7 1 HETATM 6069 C C8 . NAG N 2 . ? 8.342 -4.569 45.274 1.00 58.19 ? 501 NAG B C8 1 HETATM 6070 N N2 . NAG N 2 . ? 10.109 -3.558 46.558 1.00 64.93 ? 501 NAG B N2 1 HETATM 6071 O O3 . NAG N 2 . ? 12.584 -4.962 47.162 1.00 75.36 ? 501 NAG B O3 1 HETATM 6072 O O4 . NAG N 2 . ? 14.080 -3.652 49.250 1.00 74.03 ? 501 NAG B O4 1 HETATM 6073 O O5 . NAG N 2 . ? 12.447 -0.887 47.558 1.00 64.82 ? 501 NAG B O5 1 HETATM 6074 O O6 . NAG N 2 . ? 15.304 -0.795 47.965 1.00 75.65 ? 501 NAG B O6 1 HETATM 6075 O O7 . NAG N 2 . ? 10.346 -3.714 44.326 1.00 72.68 ? 501 NAG B O7 1 HETATM 6076 C C1 . NAG O 2 . ? -3.546 49.431 57.477 1.00 53.11 ? 502 NAG B C1 1 HETATM 6077 C C2 . NAG O 2 . ? -4.076 50.680 58.196 1.00 63.40 ? 502 NAG B C2 1 HETATM 6078 C C3 . NAG O 2 . ? -4.520 51.800 57.250 1.00 67.96 ? 502 NAG B C3 1 HETATM 6079 C C4 . NAG O 2 . ? -3.692 51.869 56.003 1.00 72.37 ? 502 NAG B C4 1 HETATM 6080 C C5 . NAG O 2 . ? -3.545 50.468 55.445 1.00 69.50 ? 502 NAG B C5 1 HETATM 6081 C C6 . NAG O 2 . ? -2.965 50.376 54.038 1.00 80.15 ? 502 NAG B C6 1 HETATM 6082 C C7 . NAG O 2 . ? -4.897 50.233 60.505 1.00 68.45 ? 502 NAG B C7 1 HETATM 6083 C C8 . NAG O 2 . ? -5.963 49.598 61.330 1.00 72.48 ? 502 NAG B C8 1 HETATM 6084 N N2 . NAG O 2 . ? -5.056 50.198 59.152 1.00 65.03 ? 502 NAG B N2 1 HETATM 6085 O O3 . NAG O 2 . ? -4.361 53.033 57.835 1.00 68.19 ? 502 NAG B O3 1 HETATM 6086 O O4 . NAG O 2 . ? -4.370 52.629 55.098 1.00 77.23 ? 502 NAG B O4 1 HETATM 6087 O O5 . NAG O 2 . ? -2.774 49.804 56.379 1.00 69.22 ? 502 NAG B O5 1 HETATM 6088 O O6 . NAG O 2 . ? -1.812 51.126 53.858 1.00 77.29 ? 502 NAG B O6 1 HETATM 6089 O O7 . NAG O 2 . ? -3.944 50.711 61.096 1.00 68.21 ? 502 NAG B O7 1 HETATM 6090 CA CA . CA P 4 . ? 2.576 15.274 70.674 1.00 8.17 ? 601 CA B CA 1 HETATM 6091 CA CA . CA Q 4 . ? -13.942 25.550 76.772 1.00 14.06 ? 602 CA B CA 1 HETATM 6092 C C . ACT R 5 . ? -16.038 33.242 65.942 1.00 28.38 ? 1 ACT B C 1 HETATM 6093 O O . ACT R 5 . ? -16.226 34.127 66.803 1.00 36.57 ? 1 ACT B O 1 HETATM 6094 O OXT . ACT R 5 . ? -16.996 32.455 65.767 1.00 33.70 ? 1 ACT B OXT 1 HETATM 6095 C CH3 . ACT R 5 . ? -14.749 33.135 65.176 1.00 24.21 ? 1 ACT B CH3 1 HETATM 6096 O O . HOH S 6 . ? 20.594 22.755 9.540 1.00 6.92 ? 6 HOH A O 1 HETATM 6097 O O . HOH S 6 . ? 34.214 21.818 27.998 1.00 6.36 ? 7 HOH A O 1 HETATM 6098 O O . HOH S 6 . ? 24.958 42.305 32.751 1.00 9.51 ? 8 HOH A O 1 HETATM 6099 O O . HOH S 6 . ? 33.558 27.668 31.942 1.00 6.95 ? 9 HOH A O 1 HETATM 6100 O O . HOH S 6 . ? 41.809 21.427 33.782 1.00 5.38 ? 10 HOH A O 1 HETATM 6101 O O . HOH S 6 . ? 25.406 35.987 29.023 1.00 11.25 ? 17 HOH A O 1 HETATM 6102 O O . HOH S 6 . ? 24.961 23.458 49.358 1.00 9.90 ? 23 HOH A O 1 HETATM 6103 O O . HOH S 6 . ? 22.321 23.890 48.831 1.00 6.54 ? 26 HOH A O 1 HETATM 6104 O O . HOH S 6 . ? 35.929 15.825 34.857 1.00 8.40 ? 27 HOH A O 1 HETATM 6105 O O . HOH S 6 . ? 46.377 28.187 13.073 1.00 14.92 ? 28 HOH A O 1 HETATM 6106 O O . HOH S 6 . ? 23.786 38.640 39.151 1.00 9.00 ? 31 HOH A O 1 HETATM 6107 O O . HOH S 6 . ? 35.123 43.923 25.326 1.00 7.83 ? 32 HOH A O 1 HETATM 6108 O O . HOH S 6 . ? 17.860 14.903 38.431 1.00 11.25 ? 34 HOH A O 1 HETATM 6109 O O . HOH S 6 . ? 15.252 32.164 19.030 1.00 8.44 ? 35 HOH A O 1 HETATM 6110 O O . HOH S 6 . ? 24.826 26.664 29.946 1.00 8.83 ? 38 HOH A O 1 HETATM 6111 O O . HOH S 6 . ? 33.128 23.414 19.371 1.00 8.95 ? 40 HOH A O 1 HETATM 6112 O O . HOH S 6 . ? 40.302 18.772 28.145 1.00 6.91 ? 41 HOH A O 1 HETATM 6113 O O . HOH S 6 . ? 30.133 19.314 8.771 1.00 10.53 ? 42 HOH A O 1 HETATM 6114 O O . HOH S 6 . ? 16.035 10.876 37.409 1.00 9.83 ? 43 HOH A O 1 HETATM 6115 O O . HOH S 6 . ? 33.363 20.532 34.546 1.00 7.08 ? 45 HOH A O 1 HETATM 6116 O O . HOH S 6 . ? 47.482 20.991 34.168 1.00 10.13 ? 51 HOH A O 1 HETATM 6117 O O . HOH S 6 . ? 19.403 23.321 11.978 1.00 10.06 ? 52 HOH A O 1 HETATM 6118 O O . HOH S 6 . ? 30.321 16.817 20.940 1.00 11.45 ? 53 HOH A O 1 HETATM 6119 O O . HOH S 6 . ? 39.167 22.409 34.607 1.00 7.13 ? 54 HOH A O 1 HETATM 6120 O O . HOH S 6 . ? 41.843 26.903 14.170 1.00 9.64 ? 57 HOH A O 1 HETATM 6121 O O . HOH S 6 . ? 45.296 26.048 48.070 1.00 17.60 ? 59 HOH A O 1 HETATM 6122 O O . HOH S 6 . ? 42.873 13.378 39.043 1.00 11.21 ? 62 HOH A O 1 HETATM 6123 O O . HOH S 6 . ? 34.220 17.926 34.001 1.00 9.80 ? 63 HOH A O 1 HETATM 6124 O O . HOH S 6 . ? 34.671 10.796 29.728 1.00 13.12 ? 66 HOH A O 1 HETATM 6125 O O . HOH S 6 . ? 18.971 16.975 13.614 1.00 7.32 ? 68 HOH A O 1 HETATM 6126 O O . HOH S 6 . ? 21.906 40.366 19.985 1.00 9.62 ? 69 HOH A O 1 HETATM 6127 O O . HOH S 6 . ? 22.245 32.819 31.613 1.00 13.92 ? 70 HOH A O 1 HETATM 6128 O O . HOH S 6 . ? 16.503 24.509 12.704 1.00 12.29 ? 71 HOH A O 1 HETATM 6129 O O . HOH S 6 . ? 26.619 5.298 30.423 1.00 17.56 ? 75 HOH A O 1 HETATM 6130 O O . HOH S 6 . ? 36.980 20.539 34.698 1.00 10.56 ? 76 HOH A O 1 HETATM 6131 O O . HOH S 6 . ? 31.635 17.183 33.069 1.00 8.73 ? 77 HOH A O 1 HETATM 6132 O O . HOH S 6 . ? 18.353 27.823 15.934 1.00 11.13 ? 81 HOH A O 1 HETATM 6133 O O . HOH S 6 . ? 29.888 19.275 20.315 1.00 25.45 ? 307 HOH A O 1 HETATM 6134 O O . HOH S 6 . ? 50.175 30.912 39.833 1.00 32.88 ? 337 HOH A O 1 HETATM 6135 O O . HOH S 6 . ? 27.359 8.996 22.390 1.00 34.94 ? 434 HOH A O 1 HETATM 6136 O O . HOH S 6 . ? 37.613 12.789 14.010 1.00 31.96 ? 473 HOH A O 1 HETATM 6137 O O . HOH S 6 . ? 20.023 -1.794 20.911 1.00 33.68 ? 474 HOH A O 1 HETATM 6138 O O . HOH S 6 . ? 29.405 50.453 27.107 1.00 43.35 ? 475 HOH A O 1 HETATM 6139 O O . HOH S 6 . ? 41.421 13.245 28.981 1.00 11.46 ? 476 HOH A O 1 HETATM 6140 O O . HOH S 6 . ? 21.086 45.693 36.333 1.00 34.73 ? 477 HOH A O 1 HETATM 6141 O O . HOH S 6 . ? 32.338 25.062 21.316 1.00 9.45 ? 478 HOH A O 1 HETATM 6142 O O . HOH S 6 . ? 46.527 29.210 32.197 1.00 13.86 ? 479 HOH A O 1 HETATM 6143 O O . HOH S 6 . ? 31.398 10.294 14.953 1.00 39.38 ? 480 HOH A O 1 HETATM 6144 O O . HOH S 6 . ? 24.051 29.766 58.193 1.00 14.99 ? 481 HOH A O 1 HETATM 6145 O O . HOH S 6 . ? 23.531 9.808 39.229 1.00 9.70 ? 482 HOH A O 1 HETATM 6146 O O . HOH S 6 . ? 3.173 4.608 31.176 1.00 30.64 ? 483 HOH A O 1 HETATM 6147 O O . HOH S 6 . ? 23.523 41.884 25.696 1.00 13.71 ? 484 HOH A O 1 HETATM 6148 O O . HOH S 6 . ? 25.087 14.177 10.378 1.00 13.46 ? 485 HOH A O 1 HETATM 6149 O O . HOH S 6 . ? 30.945 49.368 30.688 1.00 30.64 ? 486 HOH A O 1 HETATM 6150 O O . HOH S 6 . ? 21.778 37.699 18.804 1.00 11.80 ? 487 HOH A O 1 HETATM 6151 O O . HOH S 6 . ? 21.134 33.728 28.369 1.00 13.09 ? 488 HOH A O 1 HETATM 6152 O O . HOH S 6 . ? 20.059 37.138 21.839 1.00 17.66 ? 489 HOH A O 1 HETATM 6153 O O . HOH S 6 . ? 13.893 4.325 27.145 1.00 12.39 ? 490 HOH A O 1 HETATM 6154 O O . HOH S 6 . ? 12.800 35.651 22.361 1.00 11.74 ? 491 HOH A O 1 HETATM 6155 O O . HOH S 6 . ? 47.382 33.817 23.618 1.00 12.48 ? 492 HOH A O 1 HETATM 6156 O O . HOH S 6 . ? 47.702 24.738 41.138 1.00 32.15 ? 493 HOH A O 1 HETATM 6157 O O . HOH S 6 . ? 23.404 51.254 23.839 1.00 36.21 ? 494 HOH A O 1 HETATM 6158 O O . HOH S 6 . ? 52.395 29.773 40.736 1.00 45.34 ? 495 HOH A O 1 HETATM 6159 O O . HOH S 6 . ? 37.478 44.122 31.446 1.00 37.22 ? 496 HOH A O 1 HETATM 6160 O O . HOH S 6 . ? 12.048 41.718 24.878 1.00 35.65 ? 497 HOH A O 1 HETATM 6161 O O . HOH S 6 . ? 8.820 25.664 36.719 1.00 14.39 ? 498 HOH A O 1 HETATM 6162 O O . HOH S 6 . ? 31.830 18.330 50.584 1.00 13.35 ? 499 HOH A O 1 HETATM 6163 O O . HOH S 6 . ? 23.008 11.633 49.158 1.00 21.51 ? 500 HOH A O 1 HETATM 6164 O O . HOH S 6 . ? 26.990 51.493 26.791 1.00 35.27 ? 506 HOH A O 1 HETATM 6165 O O . HOH S 6 . ? 29.868 39.526 8.040 1.00 40.01 ? 507 HOH A O 1 HETATM 6166 O O . HOH S 6 . ? 43.894 21.326 35.568 1.00 16.37 ? 508 HOH A O 1 HETATM 6167 O O . HOH S 6 . ? 33.767 10.319 24.392 1.00 43.00 ? 509 HOH A O 1 HETATM 6168 O O . HOH S 6 . ? 44.477 35.693 42.216 1.00 12.12 ? 510 HOH A O 1 HETATM 6169 O O . HOH S 6 . ? 36.898 45.283 22.389 1.00 27.78 ? 511 HOH A O 1 HETATM 6170 O O . HOH S 6 . ? 15.433 11.886 30.290 1.00 15.49 ? 512 HOH A O 1 HETATM 6171 O O . HOH S 6 . ? 31.856 10.277 46.918 1.00 17.86 ? 513 HOH A O 1 HETATM 6172 O O . HOH S 6 . ? 46.715 16.180 14.044 1.00 16.26 ? 514 HOH A O 1 HETATM 6173 O O . HOH S 6 . ? 26.937 43.521 34.291 1.00 11.59 ? 515 HOH A O 1 HETATM 6174 O O . HOH S 6 . ? 8.508 18.072 36.264 1.00 10.28 ? 516 HOH A O 1 HETATM 6175 O O . HOH S 6 . ? 38.945 17.035 8.590 1.00 33.88 ? 517 HOH A O 1 HETATM 6176 O O . HOH S 6 . ? 23.522 34.196 49.825 1.00 15.56 ? 518 HOH A O 1 HETATM 6177 O O . HOH S 6 . ? 28.501 28.158 28.392 1.00 8.90 ? 519 HOH A O 1 HETATM 6178 O O . HOH S 6 . ? 27.342 8.571 17.687 1.00 30.17 ? 520 HOH A O 1 HETATM 6179 O O . HOH S 6 . ? 22.656 35.953 28.273 1.00 13.63 ? 521 HOH A O 1 HETATM 6180 O O . HOH S 6 . ? 35.848 4.918 38.790 1.00 36.82 ? 522 HOH A O 1 HETATM 6181 O O . HOH S 6 . ? 13.826 -5.045 31.649 1.00 38.21 ? 523 HOH A O 1 HETATM 6182 O O . HOH S 6 . ? 33.315 14.177 6.702 1.00 33.75 ? 524 HOH A O 1 HETATM 6183 O O . HOH S 6 . ? 22.923 -0.258 36.082 1.00 38.44 ? 525 HOH A O 1 HETATM 6184 O O . HOH S 6 . ? 23.199 10.114 23.543 1.00 19.32 ? 526 HOH A O 1 HETATM 6185 O O . HOH S 6 . ? 8.562 35.518 17.035 1.00 27.32 ? 527 HOH A O 1 HETATM 6186 O O . HOH S 6 . ? 15.979 18.343 30.652 1.00 38.27 ? 528 HOH A O 1 HETATM 6187 O O . HOH S 6 . ? 12.279 36.982 25.299 1.00 20.31 ? 529 HOH A O 1 HETATM 6188 O O . HOH S 6 . ? 19.724 31.929 41.730 1.00 12.19 ? 530 HOH A O 1 HETATM 6189 O O . HOH S 6 . ? 16.402 44.083 35.306 1.00 37.01 ? 531 HOH A O 1 HETATM 6190 O O . HOH S 6 . ? 29.821 28.606 51.159 1.00 20.71 ? 532 HOH A O 1 HETATM 6191 O O . HOH S 6 . ? 36.060 33.372 9.660 1.00 32.35 ? 533 HOH A O 1 HETATM 6192 O O . HOH S 6 . ? 38.733 13.720 43.405 1.00 38.42 ? 534 HOH A O 1 HETATM 6193 O O . HOH S 6 . ? 11.878 38.214 27.803 1.00 43.14 ? 535 HOH A O 1 HETATM 6194 O O . HOH S 6 . ? 15.393 37.269 9.585 1.00 19.61 ? 536 HOH A O 1 HETATM 6195 O O . HOH S 6 . ? 26.376 12.178 7.685 1.00 21.65 ? 537 HOH A O 1 HETATM 6196 O O . HOH S 6 . ? 50.414 28.967 19.927 1.00 34.81 ? 538 HOH A O 1 HETATM 6197 O O . HOH S 6 . ? 32.501 25.344 49.032 1.00 30.09 ? 539 HOH A O 1 HETATM 6198 O O . HOH S 6 . ? 26.233 31.428 5.306 1.00 14.64 ? 540 HOH A O 1 HETATM 6199 O O . HOH S 6 . ? 44.386 26.111 15.247 1.00 18.79 ? 541 HOH A O 1 HETATM 6200 O O . HOH S 6 . ? 17.281 20.602 36.799 1.00 13.29 ? 542 HOH A O 1 HETATM 6201 O O . HOH S 6 . ? 48.666 30.561 31.126 1.00 35.19 ? 543 HOH A O 1 HETATM 6202 O O . HOH S 6 . ? 7.908 25.774 27.826 1.00 16.38 ? 544 HOH A O 1 HETATM 6203 O O . HOH S 6 . ? 28.734 45.448 12.065 1.00 47.66 ? 545 HOH A O 1 HETATM 6204 O O . HOH S 6 . ? 39.641 4.805 38.416 1.00 39.08 ? 546 HOH A O 1 HETATM 6205 O O . HOH S 6 . ? 6.752 20.042 22.967 1.00 17.69 ? 547 HOH A O 1 HETATM 6206 O O . HOH S 6 . ? 41.859 34.525 30.353 1.00 38.61 ? 548 HOH A O 1 HETATM 6207 O O . HOH S 6 . ? 14.514 29.153 18.541 1.00 16.61 ? 549 HOH A O 1 HETATM 6208 O O . HOH S 6 . ? 25.121 5.346 32.933 1.00 15.89 ? 550 HOH A O 1 HETATM 6209 O O . HOH S 6 . ? 20.611 36.589 33.473 1.00 10.62 ? 551 HOH A O 1 HETATM 6210 O O . HOH S 6 . ? 19.904 7.839 16.044 1.00 32.33 ? 552 HOH A O 1 HETATM 6211 O O . HOH S 6 . ? 28.602 44.302 22.210 1.00 27.75 ? 553 HOH A O 1 HETATM 6212 O O . HOH S 6 . ? 10.655 17.586 38.073 1.00 16.85 ? 554 HOH A O 1 HETATM 6213 O O . HOH S 6 . ? 10.535 0.908 33.816 1.00 19.49 ? 555 HOH A O 1 HETATM 6214 O O . HOH S 6 . ? 43.562 23.889 11.836 1.00 31.86 ? 556 HOH A O 1 HETATM 6215 O O . HOH S 6 . ? 26.484 7.997 26.993 1.00 17.52 ? 557 HOH A O 1 HETATM 6216 O O . HOH S 6 . ? 41.858 21.586 51.653 1.00 35.49 ? 558 HOH A O 1 HETATM 6217 O O . HOH S 6 . ? 33.960 13.042 49.809 1.00 36.34 ? 559 HOH A O 1 HETATM 6218 O O . HOH S 6 . ? 16.192 4.654 43.332 1.00 44.16 ? 560 HOH A O 1 HETATM 6219 O O . HOH S 6 . ? 22.553 42.961 13.587 1.00 20.45 ? 561 HOH A O 1 HETATM 6220 O O . HOH S 6 . ? 21.810 35.428 31.290 1.00 14.92 ? 562 HOH A O 1 HETATM 6221 O O . HOH S 6 . ? 40.296 19.790 8.929 1.00 33.88 ? 563 HOH A O 1 HETATM 6222 O O . HOH S 6 . ? 20.052 1.381 38.568 1.00 18.40 ? 564 HOH A O 1 HETATM 6223 O O . HOH S 6 . ? 46.900 26.405 45.931 1.00 23.25 ? 565 HOH A O 1 HETATM 6224 O O . HOH S 6 . ? 18.196 44.339 38.649 1.00 42.14 ? 566 HOH A O 1 HETATM 6225 O O . HOH S 6 . ? 40.585 43.388 25.971 1.00 33.41 ? 567 HOH A O 1 HETATM 6226 O O . HOH S 6 . ? 43.284 43.370 23.170 1.00 37.60 ? 568 HOH A O 1 HETATM 6227 O O . HOH S 6 . ? 26.097 46.030 35.097 1.00 18.67 ? 569 HOH A O 1 HETATM 6228 O O . HOH S 6 . ? 10.552 37.312 36.341 1.00 31.38 ? 570 HOH A O 1 HETATM 6229 O O . HOH S 6 . ? 27.494 8.668 33.438 1.00 12.28 ? 571 HOH A O 1 HETATM 6230 O O . HOH S 6 . ? 48.633 28.364 29.276 1.00 20.64 ? 572 HOH A O 1 HETATM 6231 O O . HOH S 6 . ? 28.685 8.776 28.717 1.00 12.90 ? 573 HOH A O 1 HETATM 6232 O O . HOH S 6 . ? 43.299 22.845 53.465 1.00 42.27 ? 574 HOH A O 1 HETATM 6233 O O . HOH S 6 . ? 21.149 41.880 47.087 1.00 40.77 ? 575 HOH A O 1 HETATM 6234 O O . HOH S 6 . ? 34.481 38.449 9.922 1.00 17.63 ? 576 HOH A O 1 HETATM 6235 O O . HOH S 6 . ? 7.351 0.733 22.684 1.00 18.13 ? 577 HOH A O 1 HETATM 6236 O O . HOH S 6 . ? 42.683 8.697 27.163 1.00 18.77 ? 578 HOH A O 1 HETATM 6237 O O . HOH S 6 . ? 31.518 28.853 6.713 1.00 19.25 ? 579 HOH A O 1 HETATM 6238 O O . HOH S 6 . ? 39.181 7.326 40.196 1.00 18.87 ? 580 HOH A O 1 HETATM 6239 O O . HOH S 6 . ? 9.808 28.172 17.932 1.00 44.20 ? 581 HOH A O 1 HETATM 6240 O O . HOH S 6 . ? 31.648 35.080 9.230 1.00 40.65 ? 582 HOH A O 1 HETATM 6241 O O . HOH S 6 . ? 29.555 26.795 54.372 1.00 22.92 ? 583 HOH A O 1 HETATM 6242 O O . HOH S 6 . ? 11.905 33.363 28.090 1.00 40.47 ? 584 HOH A O 1 HETATM 6243 O O . HOH S 6 . ? 53.827 26.458 38.362 1.00 41.67 ? 585 HOH A O 1 HETATM 6244 O O . HOH S 6 . ? 51.522 13.675 30.636 1.00 23.18 ? 586 HOH A O 1 HETATM 6245 O O . HOH S 6 . ? 21.399 44.113 45.750 1.00 30.68 ? 587 HOH A O 1 HETATM 6246 O O . HOH S 6 . ? 28.164 53.408 28.288 1.00 39.03 ? 588 HOH A O 1 HETATM 6247 O O . HOH S 6 . ? 55.751 23.295 36.536 1.00 32.00 ? 589 HOH A O 1 HETATM 6248 O O . HOH S 6 . ? 30.467 22.265 3.911 1.00 19.83 ? 590 HOH A O 1 HETATM 6249 O O . HOH S 6 . ? 45.573 20.573 48.986 1.00 23.52 ? 591 HOH A O 1 HETATM 6250 O O . HOH S 6 . ? 11.684 15.650 19.220 1.00 31.94 ? 592 HOH A O 1 HETATM 6251 O O . HOH S 6 . ? 19.173 -16.176 11.798 1.00 41.28 ? 593 HOH A O 1 HETATM 6252 O O . HOH S 6 . ? 21.684 2.895 22.571 1.00 21.76 ? 594 HOH A O 1 HETATM 6253 O O . HOH S 6 . ? 34.403 45.056 35.546 1.00 39.18 ? 595 HOH A O 1 HETATM 6254 O O . HOH S 6 . ? 32.299 20.970 20.051 1.00 16.45 ? 596 HOH A O 1 HETATM 6255 O O . HOH S 6 . ? 36.270 44.454 13.846 1.00 38.41 ? 597 HOH A O 1 HETATM 6256 O O . HOH S 6 . ? 34.294 3.631 44.922 1.00 40.24 ? 598 HOH A O 1 HETATM 6257 O O . HOH S 6 . ? 21.867 45.305 15.095 1.00 41.44 ? 599 HOH A O 1 HETATM 6258 O O . HOH S 6 . ? 20.452 10.261 24.229 1.00 20.85 ? 600 HOH A O 1 HETATM 6259 O O . HOH S 6 . ? 29.236 -0.379 34.516 1.00 43.03 ? 604 HOH A O 1 HETATM 6260 O O . HOH S 6 . ? 26.611 37.979 6.195 1.00 37.96 ? 605 HOH A O 1 HETATM 6261 O O . HOH S 6 . ? 47.548 8.357 37.087 1.00 27.04 ? 606 HOH A O 1 HETATM 6262 O O . HOH S 6 . ? 43.116 33.543 43.827 1.00 18.37 ? 607 HOH A O 1 HETATM 6263 O O . HOH S 6 . ? 11.578 -6.098 29.346 1.00 42.10 ? 608 HOH A O 1 HETATM 6264 O O . HOH S 6 . ? 24.587 46.448 20.168 1.00 40.64 ? 609 HOH A O 1 HETATM 6265 O O . HOH S 6 . ? 52.180 19.965 43.631 1.00 46.18 ? 610 HOH A O 1 HETATM 6266 O O . HOH S 6 . ? 26.413 33.411 29.233 1.00 15.68 ? 611 HOH A O 1 HETATM 6267 O O . HOH S 6 . ? 47.347 12.249 43.221 1.00 30.78 ? 612 HOH A O 1 HETATM 6268 O O . HOH S 6 . ? 25.700 15.413 19.280 1.00 39.11 ? 613 HOH A O 1 HETATM 6269 O O . HOH S 6 . ? 32.782 40.864 9.607 1.00 41.82 ? 614 HOH A O 1 HETATM 6270 O O . HOH S 6 . ? 54.279 20.392 41.572 1.00 38.87 ? 615 HOH A O 1 HETATM 6271 O O . HOH S 6 . ? 46.363 13.106 45.499 1.00 37.60 ? 616 HOH A O 1 HETATM 6272 O O . HOH S 6 . ? 14.393 -4.195 24.097 1.00 32.50 ? 617 HOH A O 1 HETATM 6273 O O . HOH S 6 . ? 14.125 38.759 38.822 1.00 38.02 ? 618 HOH A O 1 HETATM 6274 O O . HOH S 6 . ? 41.490 31.654 48.742 1.00 27.61 ? 619 HOH A O 1 HETATM 6275 O O . HOH S 6 . ? 42.133 37.880 26.690 1.00 28.56 ? 620 HOH A O 1 HETATM 6276 O O . HOH S 6 . ? 37.795 10.907 18.733 1.00 29.92 ? 621 HOH A O 1 HETATM 6277 O O . HOH S 6 . ? 19.765 43.316 9.565 1.00 41.85 ? 622 HOH A O 1 HETATM 6278 O O . HOH S 6 . ? 25.233 19.806 27.391 1.00 15.03 ? 623 HOH A O 1 HETATM 6279 O O . HOH S 6 . ? 38.014 39.283 31.915 1.00 47.66 ? 624 HOH A O 1 HETATM 6280 O O . HOH S 6 . ? 50.696 26.346 19.843 1.00 33.61 ? 625 HOH A O 1 HETATM 6281 O O . HOH S 6 . ? 46.656 11.428 21.777 1.00 39.17 ? 626 HOH A O 1 HETATM 6282 O O . HOH S 6 . ? 24.183 44.319 46.106 1.00 47.21 ? 627 HOH A O 1 HETATM 6283 O O . HOH S 6 . ? 42.984 15.319 48.892 1.00 44.56 ? 628 HOH A O 1 HETATM 6284 O O . HOH S 6 . ? 19.351 7.350 13.493 1.00 39.81 ? 629 HOH A O 1 HETATM 6285 O O . HOH S 6 . ? 43.878 34.332 14.223 1.00 13.69 ? 630 HOH A O 1 HETATM 6286 O O . HOH S 6 . ? 28.755 7.280 45.977 1.00 23.82 ? 631 HOH A O 1 HETATM 6287 O O . HOH S 6 . ? 17.727 41.808 7.995 1.00 38.58 ? 632 HOH A O 1 HETATM 6288 O O . HOH S 6 . ? 20.950 46.703 31.041 1.00 20.90 ? 633 HOH A O 1 HETATM 6289 O O . HOH S 6 . ? 22.118 34.614 47.652 1.00 28.35 ? 634 HOH A O 1 HETATM 6290 O O . HOH S 6 . ? 22.099 9.940 10.366 1.00 43.30 ? 635 HOH A O 1 HETATM 6291 O O . HOH S 6 . ? 11.914 33.057 21.286 1.00 30.06 ? 636 HOH A O 1 HETATM 6292 O O . HOH S 6 . ? 24.838 48.679 23.239 1.00 36.98 ? 637 HOH A O 1 HETATM 6293 O O . HOH S 6 . ? 25.717 48.901 27.891 1.00 48.14 ? 638 HOH A O 1 HETATM 6294 O O . HOH S 6 . ? 23.548 38.572 20.124 1.00 44.50 ? 640 HOH A O 1 HETATM 6295 O O . HOH S 6 . ? 31.612 43.603 14.870 1.00 25.01 ? 641 HOH A O 1 HETATM 6296 O O . HOH S 6 . ? 23.624 11.685 54.039 1.00 23.13 ? 642 HOH A O 1 HETATM 6297 O O . HOH S 6 . ? 24.340 12.319 22.409 1.00 26.12 ? 643 HOH A O 1 HETATM 6298 O O . HOH S 6 . ? 34.056 34.344 48.313 1.00 22.33 ? 644 HOH A O 1 HETATM 6299 O O . HOH S 6 . ? 41.862 39.643 33.116 1.00 28.57 ? 645 HOH A O 1 HETATM 6300 O O . HOH S 6 . ? 15.332 43.479 29.311 1.00 22.35 ? 646 HOH A O 1 HETATM 6301 O O . HOH S 6 . ? 20.270 43.799 20.929 1.00 22.74 ? 647 HOH A O 1 HETATM 6302 O O . HOH S 6 . ? 13.845 38.297 14.623 1.00 24.54 ? 648 HOH A O 1 HETATM 6303 O O . HOH S 6 . ? 25.761 35.179 48.670 1.00 25.09 ? 649 HOH A O 1 HETATM 6304 O O . HOH S 6 . ? 5.479 2.335 24.146 1.00 35.14 ? 650 HOH A O 1 HETATM 6305 O O . HOH S 6 . ? 45.058 12.083 47.521 1.00 40.48 ? 651 HOH A O 1 HETATM 6306 O O . HOH S 6 . ? 30.390 15.892 51.699 1.00 33.54 ? 652 HOH A O 1 HETATM 6307 O O . HOH S 6 . ? 27.396 45.681 20.109 1.00 50.24 ? 653 HOH A O 1 HETATM 6308 O O . HOH S 6 . ? 28.661 35.476 6.644 1.00 35.66 ? 654 HOH A O 1 HETATM 6309 O O . HOH S 6 . ? 32.954 30.146 8.766 1.00 41.14 ? 655 HOH A O 1 HETATM 6310 O O . HOH S 6 . ? 17.525 10.433 17.186 1.00 21.22 ? 656 HOH A O 1 HETATM 6311 O O . HOH S 6 . ? 40.928 15.020 44.894 1.00 39.88 ? 657 HOH A O 1 HETATM 6312 O O . HOH S 6 . ? 52.271 20.236 27.936 1.00 34.33 ? 658 HOH A O 1 HETATM 6313 O O . HOH S 6 . ? 34.468 17.927 51.067 1.00 44.98 ? 659 HOH A O 1 HETATM 6314 O O . HOH S 6 . ? 42.692 17.353 50.772 1.00 44.79 ? 660 HOH A O 1 HETATM 6315 O O . HOH S 6 . ? 28.299 7.490 31.075 1.00 17.72 ? 661 HOH A O 1 HETATM 6316 O O . HOH S 6 . ? 50.605 19.882 16.918 1.00 44.72 ? 662 HOH A O 1 HETATM 6317 O O . HOH S 6 . ? 15.868 21.285 34.587 1.00 18.49 ? 663 HOH A O 1 HETATM 6318 O O . HOH S 6 . ? 39.647 37.198 36.793 1.00 28.63 ? 664 HOH A O 1 HETATM 6319 O O . HOH S 6 . ? 29.045 34.616 9.067 1.00 49.87 ? 665 HOH A O 1 HETATM 6320 O O . HOH S 6 . ? 53.103 20.163 51.078 1.00 41.59 ? 666 HOH A O 1 HETATM 6321 O O . HOH S 6 . ? 42.820 7.074 29.449 1.00 21.41 ? 667 HOH A O 1 HETATM 6322 O O . HOH S 6 . ? 22.987 -2.350 34.153 1.00 24.42 ? 668 HOH A O 1 HETATM 6323 O O . HOH S 6 . ? 38.200 36.678 32.990 1.00 40.97 ? 669 HOH A O 1 HETATM 6324 O O . HOH S 6 . ? 52.850 16.038 43.162 1.00 48.68 ? 670 HOH A O 1 HETATM 6325 O O . HOH S 6 . ? 29.314 12.260 25.175 1.00 21.63 ? 671 HOH A O 1 HETATM 6326 O O . HOH S 6 . ? 51.510 30.702 42.972 1.00 25.94 ? 672 HOH A O 1 HETATM 6327 O O . HOH S 6 . ? 27.991 30.367 30.858 1.00 19.42 ? 673 HOH A O 1 HETATM 6328 O O . HOH S 6 . ? 30.660 47.424 28.024 1.00 42.88 ? 674 HOH A O 1 HETATM 6329 O O . HOH S 6 . ? 6.189 -0.149 32.728 1.00 41.70 ? 675 HOH A O 1 HETATM 6330 O O . HOH S 6 . ? 34.464 13.558 15.359 1.00 41.12 ? 676 HOH A O 1 HETATM 6331 O O . HOH S 6 . ? 41.516 17.916 54.727 1.00 36.50 ? 677 HOH A O 1 HETATM 6332 O O . HOH S 6 . ? 37.872 12.810 11.333 1.00 24.91 ? 678 HOH A O 1 HETATM 6333 O O . HOH S 6 . ? 44.828 21.867 10.069 1.00 46.34 ? 679 HOH A O 1 HETATM 6334 O O . HOH S 6 . ? 23.876 42.871 11.229 1.00 34.58 ? 680 HOH A O 1 HETATM 6335 O O . HOH S 6 . ? 38.496 18.045 6.060 1.00 40.98 ? 681 HOH A O 1 HETATM 6336 O O . HOH S 6 . ? 18.776 47.436 32.612 1.00 30.52 ? 682 HOH A O 1 HETATM 6337 O O . HOH S 6 . ? 32.238 27.569 4.392 1.00 45.25 ? 683 HOH A O 1 HETATM 6338 O O . HOH S 6 . ? 31.673 11.170 9.933 1.00 24.29 ? 684 HOH A O 1 HETATM 6339 O O . HOH S 6 . ? 11.204 28.627 15.580 1.00 19.42 ? 685 HOH A O 1 HETATM 6340 O O . HOH S 6 . ? 11.727 28.812 34.704 1.00 25.32 ? 686 HOH A O 1 HETATM 6341 O O . HOH S 6 . ? 29.040 45.073 15.027 1.00 34.22 ? 687 HOH A O 1 HETATM 6342 O O . HOH S 6 . ? 49.705 16.499 24.633 1.00 22.58 ? 688 HOH A O 1 HETATM 6343 O O . HOH S 6 . ? 40.952 17.921 57.398 1.00 46.66 ? 689 HOH A O 1 HETATM 6344 O O . HOH S 6 . ? 5.430 25.973 34.696 1.00 43.15 ? 690 HOH A O 1 HETATM 6345 O O . HOH S 6 . ? 26.608 35.978 4.424 1.00 44.38 ? 691 HOH A O 1 HETATM 6346 O O . HOH S 6 . ? 10.796 41.365 20.278 1.00 43.95 ? 692 HOH A O 1 HETATM 6347 O O . HOH S 6 . ? 14.839 -3.271 37.102 1.00 39.25 ? 693 HOH A O 1 HETATM 6348 O O . HOH S 6 . ? 24.174 8.236 10.801 1.00 46.09 ? 694 HOH A O 1 HETATM 6349 O O . HOH S 6 . ? 7.108 -2.244 26.665 1.00 42.78 ? 695 HOH A O 1 HETATM 6350 O O . HOH S 6 . ? 52.964 19.847 24.605 1.00 47.01 ? 696 HOH A O 1 HETATM 6351 O O . HOH S 6 . ? 36.767 35.105 34.563 1.00 32.07 ? 697 HOH A O 1 HETATM 6352 O O . HOH S 6 . ? 32.634 32.607 8.814 1.00 42.84 ? 698 HOH A O 1 HETATM 6353 O O . HOH S 6 . ? 38.858 17.499 55.287 1.00 48.29 ? 699 HOH A O 1 HETATM 6354 O O . HOH S 6 . ? 15.027 -1.244 41.413 1.00 45.21 ? 700 HOH A O 1 HETATM 6355 O O . HOH S 6 . ? 36.765 36.832 37.605 1.00 14.30 ? 701 HOH A O 1 HETATM 6356 O O . HOH S 6 . ? 51.971 16.927 33.819 1.00 39.72 ? 702 HOH A O 1 HETATM 6357 O O . HOH S 6 . ? 56.615 14.859 47.947 1.00 22.36 ? 703 HOH A O 1 HETATM 6358 O O . HOH S 6 . ? 13.371 30.058 24.840 1.00 22.32 ? 704 HOH A O 1 HETATM 6359 O O . HOH S 6 . ? 52.131 15.854 29.278 1.00 29.41 ? 705 HOH A O 1 HETATM 6360 O O . HOH S 6 . ? 35.688 38.585 39.878 1.00 27.41 ? 706 HOH A O 1 HETATM 6361 O O . HOH S 6 . ? 22.752 45.587 44.089 1.00 35.35 ? 707 HOH A O 1 HETATM 6362 O O . HOH S 6 . ? 22.637 48.300 45.555 1.00 33.88 ? 708 HOH A O 1 HETATM 6363 O O . HOH S 6 . ? 30.191 20.013 53.257 1.00 25.52 ? 709 HOH A O 1 HETATM 6364 O O . HOH S 6 . ? 35.378 14.939 13.261 1.00 24.51 ? 710 HOH A O 1 HETATM 6365 O O . HOH S 6 . ? 10.926 18.060 17.887 1.00 28.87 ? 711 HOH A O 1 HETATM 6366 O O . HOH S 6 . ? 37.114 21.814 51.824 1.00 25.69 ? 712 HOH A O 1 HETATM 6367 O O . HOH S 6 . ? 20.147 4.732 41.298 1.00 26.18 ? 713 HOH A O 1 HETATM 6368 O O . HOH S 6 . ? 10.808 47.471 23.891 1.00 46.30 ? 714 HOH A O 1 HETATM 6369 O O . HOH S 6 . ? 49.017 20.328 14.696 1.00 26.88 ? 715 HOH A O 1 HETATM 6370 O O . HOH S 6 . ? 26.136 34.599 6.766 1.00 26.92 ? 716 HOH A O 1 HETATM 6371 O O . HOH S 6 . ? 44.240 16.770 11.730 1.00 25.44 ? 717 HOH A O 1 HETATM 6372 O O . HOH S 6 . ? 24.545 52.383 28.451 1.00 38.16 ? 718 HOH A O 1 HETATM 6373 O O . HOH S 6 . ? 15.703 6.456 17.896 1.00 49.19 ? 719 HOH A O 1 HETATM 6374 O O . HOH S 6 . ? 27.309 52.492 23.296 1.00 43.85 ? 720 HOH A O 1 HETATM 6375 O O . HOH S 6 . ? 37.555 46.820 31.087 1.00 37.87 ? 721 HOH A O 1 HETATM 6376 O O . HOH S 6 . ? 25.802 54.654 24.979 1.00 34.64 ? 722 HOH A O 1 HETATM 6377 O O . HOH S 6 . ? 40.495 11.243 20.597 1.00 25.61 ? 723 HOH A O 1 HETATM 6378 O O . HOH S 6 . ? 49.181 37.565 38.624 1.00 29.56 ? 724 HOH A O 1 HETATM 6379 O O . HOH S 6 . ? 15.369 43.017 39.341 1.00 46.31 ? 725 HOH A O 1 HETATM 6380 O O . HOH S 6 . ? 26.167 9.807 15.040 1.00 22.22 ? 726 HOH A O 1 HETATM 6381 O O . HOH S 6 . ? 44.394 39.645 22.262 1.00 38.28 ? 727 HOH A O 1 HETATM 6382 O O . HOH S 6 . ? 21.453 47.307 20.114 1.00 42.19 ? 728 HOH A O 1 HETATM 6383 O O . HOH S 6 . ? 41.990 12.048 12.517 1.00 38.22 ? 729 HOH A O 1 HETATM 6384 O O . HOH S 6 . ? 43.877 13.814 12.345 1.00 40.45 ? 730 HOH A O 1 HETATM 6385 O O . HOH S 6 . ? 53.838 24.507 32.526 1.00 33.11 ? 731 HOH A O 1 HETATM 6386 O O . HOH S 6 . ? 45.635 9.604 25.538 1.00 30.94 ? 732 HOH A O 1 HETATM 6387 O O . HOH S 6 . ? 47.434 11.877 24.683 1.00 29.30 ? 733 HOH A O 1 HETATM 6388 O O . HOH S 6 . ? 6.255 3.515 30.382 1.00 29.51 ? 734 HOH A O 1 HETATM 6389 O O . HOH S 6 . ? 43.813 26.653 10.285 1.00 32.05 ? 735 HOH A O 1 HETATM 6390 O O . HOH S 6 . ? 42.481 7.467 34.073 1.00 24.42 ? 736 HOH A O 1 HETATM 6391 O O . HOH S 6 . ? 51.599 14.900 45.347 1.00 39.85 ? 737 HOH A O 1 HETATM 6392 O O . HOH S 6 . ? 7.819 -0.014 28.051 1.00 26.65 ? 738 HOH A O 1 HETATM 6393 O O . HOH S 6 . ? 21.240 9.902 51.063 1.00 42.56 ? 739 HOH A O 1 HETATM 6394 O O . HOH S 6 . ? 35.985 37.505 31.013 1.00 28.46 ? 740 HOH A O 1 HETATM 6395 O O . HOH S 6 . ? 28.520 13.130 5.309 1.00 23.15 ? 741 HOH A O 1 HETATM 6396 O O . HOH S 6 . ? 32.184 46.591 19.463 1.00 43.86 ? 742 HOH A O 1 HETATM 6397 O O . HOH S 6 . ? 37.648 10.209 14.604 1.00 42.83 ? 743 HOH A O 1 HETATM 6398 O O . HOH S 6 . ? 23.145 47.985 28.115 1.00 34.88 ? 744 HOH A O 1 HETATM 6399 O O . HOH S 6 . ? 23.526 50.137 29.425 1.00 34.29 ? 745 HOH A O 1 HETATM 6400 O O . HOH S 6 . ? 31.382 42.190 43.554 1.00 41.71 ? 746 HOH A O 1 HETATM 6401 O O . HOH S 6 . ? 24.981 36.002 45.774 1.00 45.88 ? 747 HOH A O 1 HETATM 6402 O O . HOH S 6 . ? 44.044 12.262 42.233 1.00 32.62 ? 748 HOH A O 1 HETATM 6403 O O . HOH S 6 . ? 17.782 50.100 32.317 1.00 42.19 ? 749 HOH A O 1 HETATM 6404 O O . HOH S 6 . ? 25.642 42.509 44.643 1.00 30.29 ? 750 HOH A O 1 HETATM 6405 O O . HOH S 6 . ? 47.261 32.304 19.226 1.00 22.59 ? 752 HOH A O 1 HETATM 6406 O O . HOH S 6 . ? 49.263 30.571 27.669 1.00 43.75 ? 753 HOH A O 1 HETATM 6407 O O . HOH S 6 . ? 41.412 5.839 31.504 1.00 25.32 ? 754 HOH A O 1 HETATM 6408 O O . HOH S 6 . ? 25.682 9.498 24.603 1.00 26.06 ? 755 HOH A O 1 HETATM 6409 O O . HOH S 6 . ? 41.872 39.535 24.702 1.00 37.56 ? 756 HOH A O 1 HETATM 6410 O O . HOH S 6 . ? 19.937 42.758 12.199 1.00 27.46 ? 757 HOH A O 1 HETATM 6411 O O . HOH S 6 . ? 53.147 27.404 40.625 1.00 34.52 ? 758 HOH A O 1 HETATM 6412 O O . HOH S 6 . ? 5.865 0.611 29.986 1.00 42.71 ? 759 HOH A O 1 HETATM 6413 O O . HOH S 6 . ? 29.636 31.232 54.561 1.00 27.47 ? 760 HOH A O 1 HETATM 6414 O O . HOH S 6 . ? 49.838 14.408 20.476 1.00 27.96 ? 761 HOH A O 1 HETATM 6415 O O . HOH S 6 . ? 19.665 8.491 11.131 1.00 42.38 ? 762 HOH A O 1 HETATM 6416 O O . HOH S 6 . ? 40.094 26.863 8.164 1.00 27.32 ? 763 HOH A O 1 HETATM 6417 O O . HOH S 6 . ? 11.039 30.553 19.813 1.00 42.87 ? 764 HOH A O 1 HETATM 6418 O O . HOH S 6 . ? 51.969 21.980 15.862 1.00 48.66 ? 765 HOH A O 1 HETATM 6419 O O . HOH S 6 . ? 28.070 16.146 53.640 1.00 31.21 ? 766 HOH A O 1 HETATM 6420 O O . HOH S 6 . ? 26.699 35.148 43.646 1.00 27.61 ? 767 HOH A O 1 HETATM 6421 O O . HOH S 6 . ? 27.871 49.442 29.640 1.00 35.90 ? 768 HOH A O 1 HETATM 6422 O O . HOH S 6 . ? 34.235 44.429 16.080 1.00 43.70 ? 769 HOH A O 1 HETATM 6423 O O . HOH S 6 . ? 13.192 0.847 17.379 1.00 41.86 ? 770 HOH A O 1 HETATM 6424 O O . HOH S 6 . ? 23.365 55.474 24.562 1.00 40.67 ? 771 HOH A O 1 HETATM 6425 O O . HOH S 6 . ? 30.244 27.081 2.430 1.00 48.68 ? 772 HOH A O 1 HETATM 6426 O O . HOH S 6 . ? 23.288 -3.677 26.438 1.00 36.73 ? 773 HOH A O 1 HETATM 6427 O O . HOH S 6 . ? 11.309 26.862 36.688 1.00 22.92 ? 774 HOH A O 1 HETATM 6428 O O . HOH S 6 . ? 25.606 11.106 50.256 1.00 31.45 ? 775 HOH A O 1 HETATM 6429 O O . HOH S 6 . ? 46.355 17.489 46.563 1.00 39.56 ? 776 HOH A O 1 HETATM 6430 O O . HOH S 6 . ? 31.200 12.212 5.727 1.00 46.88 ? 777 HOH A O 1 HETATM 6431 O O . HOH S 6 . ? 8.754 -5.792 28.457 1.00 49.53 ? 778 HOH A O 1 HETATM 6432 O O . HOH S 6 . ? 30.318 23.947 51.286 1.00 29.42 ? 779 HOH A O 1 HETATM 6433 O O . HOH S 6 . ? -0.312 1.023 35.330 1.00 41.99 ? 780 HOH A O 1 HETATM 6434 O O . HOH S 6 . ? 53.601 15.848 26.480 1.00 53.38 ? 781 HOH A O 1 HETATM 6435 O O . HOH S 6 . ? 44.980 36.718 34.834 1.00 29.55 ? 782 HOH A O 1 HETATM 6436 O O . HOH S 6 . ? 22.778 21.077 23.680 1.00 19.24 ? 783 HOH A O 1 HETATM 6437 O O . HOH S 6 . ? 12.855 30.938 36.540 1.00 36.70 ? 784 HOH A O 1 HETATM 6438 O O . HOH S 6 . ? 24.673 9.109 46.304 1.00 22.28 ? 785 HOH A O 1 HETATM 6439 O O . HOH S 6 . ? 24.396 11.508 10.657 1.00 27.60 ? 786 HOH A O 1 HETATM 6440 O O . HOH S 6 . ? 26.924 41.879 6.000 1.00 41.78 ? 787 HOH A O 1 HETATM 6441 O O . HOH S 6 . ? 9.504 42.904 18.457 1.00 38.23 ? 788 HOH A O 1 HETATM 6442 O O . HOH S 6 . ? 13.345 2.880 43.217 1.00 40.47 ? 789 HOH A O 1 HETATM 6443 O O . HOH S 6 . ? 47.185 34.954 19.424 1.00 30.72 ? 790 HOH A O 1 HETATM 6444 O O . HOH S 6 . ? 36.621 40.624 36.460 1.00 31.90 ? 791 HOH A O 1 HETATM 6445 O O . HOH S 6 . ? 38.258 9.465 22.405 1.00 31.85 ? 792 HOH A O 1 HETATM 6446 O O . HOH S 6 . ? 50.812 18.193 47.083 1.00 40.28 ? 793 HOH A O 1 HETATM 6447 O O . HOH S 6 . ? 17.706 7.576 17.052 1.00 47.47 ? 794 HOH A O 1 HETATM 6448 O O . HOH S 6 . ? 28.616 14.733 17.422 1.00 37.39 ? 795 HOH A O 1 HETATM 6449 O O . HOH S 6 . ? 47.254 25.480 49.760 1.00 41.30 ? 796 HOH A O 1 HETATM 6450 O O . HOH S 6 . ? 46.448 40.069 24.227 1.00 35.38 ? 797 HOH A O 1 HETATM 6451 O O . HOH S 6 . ? 38.920 35.926 45.470 1.00 47.56 ? 798 HOH A O 1 HETATM 6452 O O . HOH S 6 . ? 10.529 15.791 41.289 1.00 25.59 ? 799 HOH A O 1 HETATM 6453 O O . HOH S 6 . ? 40.249 37.741 34.179 1.00 45.09 ? 800 HOH A O 1 HETATM 6454 O O . HOH S 6 . ? 54.790 21.755 34.278 1.00 28.90 ? 801 HOH A O 1 HETATM 6455 O O . HOH S 6 . ? 23.228 46.895 41.834 1.00 43.62 ? 802 HOH A O 1 HETATM 6456 O O . HOH S 6 . ? 20.708 50.803 22.188 1.00 41.23 ? 803 HOH A O 1 HETATM 6457 O O . HOH S 6 . ? 31.844 12.019 24.408 1.00 22.04 ? 804 HOH A O 1 HETATM 6458 O O . HOH S 6 . ? 40.952 35.412 43.165 1.00 31.03 ? 805 HOH A O 1 HETATM 6459 O O . HOH S 6 . ? 31.141 7.727 27.260 1.00 41.41 ? 806 HOH A O 1 HETATM 6460 O O . HOH S 6 . ? 29.734 43.540 10.311 1.00 40.34 ? 807 HOH A O 1 HETATM 6461 O O . HOH S 6 . ? 8.073 44.639 20.067 1.00 39.61 ? 808 HOH A O 1 HETATM 6462 O O . HOH S 6 . ? 17.437 43.635 30.816 1.00 24.49 ? 809 HOH A O 1 HETATM 6463 O O . HOH S 6 . ? 48.419 13.396 16.888 1.00 36.61 ? 810 HOH A O 1 HETATM 6464 O O . HOH S 6 . ? 26.268 33.520 3.714 1.00 42.85 ? 811 HOH A O 1 HETATM 6465 O O . HOH S 6 . ? 11.777 18.090 40.475 1.00 24.66 ? 812 HOH A O 1 HETATM 6466 O O . HOH S 6 . ? 40.221 12.130 10.536 1.00 48.59 ? 813 HOH A O 1 HETATM 6467 O O . HOH S 6 . ? 14.273 5.906 45.403 1.00 26.72 ? 814 HOH A O 1 HETATM 6468 O O . HOH S 6 . ? 11.690 49.432 25.490 1.00 44.80 ? 815 HOH A O 1 HETATM 6469 O O . HOH S 6 . ? 33.187 13.358 9.148 1.00 33.24 ? 816 HOH A O 1 HETATM 6470 O O . HOH S 6 . ? 51.087 18.202 22.815 1.00 46.40 ? 817 HOH A O 1 HETATM 6471 O O . HOH S 6 . ? 14.221 32.857 37.844 1.00 41.00 ? 818 HOH A O 1 HETATM 6472 O O . HOH S 6 . ? 23.772 0.986 21.612 1.00 47.25 ? 819 HOH A O 1 HETATM 6473 O O . HOH S 6 . ? 21.916 57.460 25.455 1.00 36.31 ? 820 HOH A O 1 HETATM 6474 O O . HOH S 6 . ? 19.967 40.982 44.953 1.00 37.06 ? 821 HOH A O 1 HETATM 6475 O O . HOH S 6 . ? 28.347 32.963 56.250 1.00 48.90 ? 822 HOH A O 1 HETATM 6476 O O . HOH S 6 . ? 21.797 36.478 6.785 1.00 40.75 ? 823 HOH A O 1 HETATM 6477 O O . HOH S 6 . ? 23.743 50.415 26.561 1.00 32.76 ? 824 HOH A O 1 HETATM 6478 O O . HOH S 6 . ? 37.184 45.383 26.438 1.00 40.89 ? 825 HOH A O 1 HETATM 6479 O O . HOH S 6 . ? 16.489 15.998 32.023 1.00 32.69 ? 826 HOH A O 1 HETATM 6480 O O . HOH S 6 . ? 29.070 42.013 44.893 1.00 43.87 ? 827 HOH A O 1 HETATM 6481 O O . HOH S 6 . ? 46.659 38.220 22.074 1.00 42.05 ? 828 HOH A O 1 HETATM 6482 O O . HOH S 6 . ? 31.664 37.615 8.720 1.00 43.05 ? 829 HOH A O 1 HETATM 6483 O O . HOH S 6 . ? 26.213 41.293 9.260 1.00 39.97 ? 830 HOH A O 1 HETATM 6484 O O . HOH S 6 . ? 18.043 38.493 43.968 1.00 23.87 ? 831 HOH A O 1 HETATM 6485 O O . HOH S 6 . ? 23.848 7.072 39.894 1.00 27.25 ? 832 HOH A O 1 HETATM 6486 O O . HOH S 6 . ? 12.188 35.923 29.211 1.00 31.68 ? 833 HOH A O 1 HETATM 6487 O O . HOH S 6 . ? 11.825 -6.430 20.776 1.00 41.07 ? 834 HOH A O 1 HETATM 6488 O O . HOH S 6 . ? 35.604 10.954 22.237 1.00 33.00 ? 835 HOH A O 1 HETATM 6489 O O . HOH S 6 . ? 33.050 42.480 7.259 1.00 39.53 ? 836 HOH A O 1 HETATM 6490 O O . HOH S 6 . ? 60.280 15.879 45.034 1.00 55.61 ? 837 HOH A O 1 HETATM 6491 O O . HOH S 6 . ? 20.701 9.913 17.592 1.00 26.83 ? 838 HOH A O 1 HETATM 6492 O O . HOH S 6 . ? 29.788 47.421 23.661 1.00 45.46 ? 839 HOH A O 1 HETATM 6493 O O . HOH S 6 . ? 54.737 23.176 40.597 1.00 30.25 ? 840 HOH A O 1 HETATM 6494 O O . HOH S 6 . ? 30.525 49.585 24.821 1.00 31.21 ? 841 HOH A O 1 HETATM 6495 O O . HOH S 6 . ? 38.883 5.693 30.931 1.00 36.30 ? 842 HOH A O 1 HETATM 6496 O O . HOH S 6 . ? 22.886 53.601 33.391 1.00 35.25 ? 843 HOH A O 1 HETATM 6497 O O . HOH S 6 . ? 40.677 12.584 41.086 1.00 24.14 ? 844 HOH A O 1 HETATM 6498 O O . HOH S 6 . ? 42.876 43.338 16.441 1.00 31.10 ? 845 HOH A O 1 HETATM 6499 O O . HOH S 6 . ? 31.313 7.050 31.680 1.00 29.92 ? 846 HOH A O 1 HETATM 6500 O O . HOH S 6 . ? 13.474 30.921 21.367 1.00 35.03 ? 847 HOH A O 1 HETATM 6501 O O . HOH S 6 . ? 46.063 18.438 53.285 1.00 48.95 ? 848 HOH A O 1 HETATM 6502 O O . HOH S 6 . ? 27.197 20.336 1.276 1.00 36.66 ? 849 HOH A O 1 HETATM 6503 O O . HOH S 6 . ? 28.098 12.587 50.337 1.00 34.36 ? 850 HOH A O 1 HETATM 6504 O O . HOH S 6 . ? 41.537 7.749 17.490 1.00 40.77 ? 851 HOH A O 1 HETATM 6505 O O . HOH S 6 . ? 49.510 11.078 38.010 1.00 39.24 ? 852 HOH A O 1 HETATM 6506 O O . HOH S 6 . ? 26.104 50.622 21.809 1.00 40.67 ? 853 HOH A O 1 HETATM 6507 O O . HOH S 6 . ? 52.938 25.985 42.695 1.00 45.28 ? 854 HOH A O 1 HETATM 6508 O O . HOH S 6 . ? 23.353 46.176 34.333 1.00 21.36 ? 855 HOH A O 1 HETATM 6509 O O . HOH S 6 . ? 29.655 53.737 26.116 1.00 30.45 ? 856 HOH A O 1 HETATM 6510 O O . HOH S 6 . ? 40.678 7.032 26.369 1.00 30.72 ? 857 HOH A O 1 HETATM 6511 O O . HOH S 6 . ? 22.737 44.576 19.089 1.00 37.59 ? 858 HOH A O 1 HETATM 6512 O O . HOH S 6 . ? 28.077 46.959 28.325 1.00 32.44 ? 859 HOH A O 1 HETATM 6513 O O . HOH S 6 . ? 37.447 46.254 39.718 1.00 42.28 ? 860 HOH A O 1 HETATM 6514 O O . HOH S 6 . ? 7.583 28.212 29.416 1.00 29.86 ? 861 HOH A O 1 HETATM 6515 O O . HOH S 6 . ? 47.972 33.119 27.231 1.00 31.98 ? 862 HOH A O 1 HETATM 6516 O O . HOH S 6 . ? 21.777 -0.542 22.404 1.00 44.45 ? 863 HOH A O 1 HETATM 6517 O O . HOH S 6 . ? 39.702 35.930 31.120 1.00 32.88 ? 864 HOH A O 1 HETATM 6518 O O . HOH S 6 . ? 42.681 38.736 30.363 1.00 45.38 ? 865 HOH A O 1 HETATM 6519 O O . HOH S 6 . ? 29.785 12.179 48.314 1.00 45.19 ? 866 HOH A O 1 HETATM 6520 O O . HOH S 6 . ? 44.824 16.944 44.281 1.00 42.62 ? 867 HOH A O 1 HETATM 6521 O O . HOH S 6 . ? 21.373 7.062 40.787 1.00 22.01 ? 868 HOH A O 1 HETATM 6522 O O . HOH S 6 . ? 14.773 19.730 32.777 1.00 25.64 ? 869 HOH A O 1 HETATM 6523 O O . HOH S 6 . ? 25.751 45.106 11.502 1.00 45.43 ? 870 HOH A O 1 HETATM 6524 O O . HOH S 6 . ? 22.383 45.388 10.272 1.00 35.19 ? 871 HOH A O 1 HETATM 6525 O O . HOH S 6 . ? 31.875 44.825 38.960 1.00 43.43 ? 872 HOH A O 1 HETATM 6526 O O . HOH S 6 . ? 36.247 23.618 53.677 1.00 39.95 ? 873 HOH A O 1 HETATM 6527 O O . HOH S 6 . ? 33.289 5.170 40.123 1.00 38.97 ? 874 HOH A O 1 HETATM 6528 O O . HOH S 6 . ? 49.684 26.345 26.145 1.00 31.08 ? 875 HOH A O 1 HETATM 6529 O O . HOH S 6 . ? 12.816 6.768 47.578 1.00 49.93 ? 876 HOH A O 1 HETATM 6530 O O . HOH S 6 . ? 39.125 46.112 20.758 1.00 33.06 ? 877 HOH A O 1 HETATM 6531 O O . HOH S 6 . ? 13.806 40.605 28.872 1.00 37.47 ? 878 HOH A O 1 HETATM 6532 O O . HOH S 6 . ? 33.723 46.448 32.120 1.00 27.52 ? 879 HOH A O 1 HETATM 6533 O O . HOH S 6 . ? 48.834 17.815 52.729 1.00 44.54 ? 880 HOH A O 1 HETATM 6534 O O . HOH S 6 . ? 43.662 11.359 20.329 1.00 37.13 ? 881 HOH A O 1 HETATM 6535 O O . HOH S 6 . ? 23.156 45.392 48.537 1.00 41.13 ? 882 HOH A O 1 HETATM 6536 O O . HOH S 6 . ? 19.033 -5.461 30.215 1.00 41.15 ? 883 HOH A O 1 HETATM 6537 O O . HOH S 6 . ? 15.973 5.754 11.361 1.00 36.96 ? 884 HOH A O 1 HETATM 6538 O O . HOH S 6 . ? 37.254 47.672 27.853 1.00 44.03 ? 885 HOH A O 1 HETATM 6539 O O . HOH S 6 . ? 48.855 32.519 21.635 1.00 45.48 ? 886 HOH A O 1 HETATM 6540 O O . HOH S 6 . ? 17.043 45.482 32.626 1.00 33.94 ? 887 HOH A O 1 HETATM 6541 O O . HOH S 6 . ? 30.057 12.639 22.521 1.00 47.02 ? 888 HOH A O 1 HETATM 6542 O O . HOH S 6 . ? 42.152 7.139 41.331 1.00 43.17 ? 889 HOH A O 1 HETATM 6543 O O . HOH S 6 . ? 18.013 -4.798 14.290 1.00 51.23 ? 891 HOH A O 1 HETATM 6544 O O . HOH S 6 . ? 54.663 16.591 48.078 1.00 45.13 ? 892 HOH A O 1 HETATM 6545 O O . HOH S 6 . ? 8.982 36.713 21.948 1.00 41.42 ? 893 HOH A O 1 HETATM 6546 O O . HOH S 6 . ? -0.827 3.673 35.755 1.00 31.73 ? 894 HOH A O 1 HETATM 6547 O O . HOH S 6 . ? 32.240 21.737 51.469 1.00 37.62 ? 895 HOH A O 1 HETATM 6548 O O . HOH S 6 . ? 31.572 28.231 53.389 1.00 40.42 ? 896 HOH A O 1 HETATM 6549 O O . HOH S 6 . ? 36.701 46.399 15.601 1.00 42.72 ? 897 HOH A O 1 HETATM 6550 O O . HOH S 6 . ? 9.780 -1.621 16.158 1.00 45.07 ? 898 HOH A O 1 HETATM 6551 O O . HOH S 6 . ? 17.926 0.514 44.939 1.00 47.27 ? 900 HOH A O 1 HETATM 6552 O O . HOH S 6 . ? 20.048 54.585 33.552 1.00 37.70 ? 901 HOH A O 1 HETATM 6553 O O . HOH T 6 . ? 17.611 23.407 48.966 1.00 7.67 ? 2 HOH B O 1 HETATM 6554 O O . HOH T 6 . ? 0.666 13.545 71.109 1.00 10.79 ? 3 HOH B O 1 HETATM 6555 O O . HOH T 6 . ? -3.139 42.430 54.421 1.00 11.99 ? 4 HOH B O 1 HETATM 6556 O O . HOH T 6 . ? 1.657 22.075 63.772 1.00 5.45 ? 5 HOH B O 1 HETATM 6557 O O . HOH T 6 . ? 15.905 16.983 48.567 1.00 5.50 ? 11 HOH B O 1 HETATM 6558 O O . HOH T 6 . ? -4.149 21.738 71.476 1.00 6.15 ? 12 HOH B O 1 HETATM 6559 O O . HOH T 6 . ? -4.970 22.713 68.872 1.00 5.49 ? 13 HOH B O 1 HETATM 6560 O O . HOH T 6 . ? -4.523 21.376 77.221 1.00 8.27 ? 14 HOH B O 1 HETATM 6561 O O . HOH T 6 . ? 20.072 22.706 50.190 1.00 7.87 ? 15 HOH B O 1 HETATM 6562 O O . HOH T 6 . ? -2.319 27.874 63.101 1.00 9.82 ? 16 HOH B O 1 HETATM 6563 O O . HOH T 6 . ? 16.551 28.392 75.958 1.00 11.21 ? 18 HOH B O 1 HETATM 6564 O O . HOH T 6 . ? 8.215 7.605 38.505 1.00 9.57 ? 19 HOH B O 1 HETATM 6565 O O . HOH T 6 . ? -0.290 26.801 54.406 1.00 9.77 ? 20 HOH B O 1 HETATM 6566 O O . HOH T 6 . ? 8.606 17.067 60.014 1.00 8.69 ? 21 HOH B O 1 HETATM 6567 O O . HOH T 6 . ? 1.408 19.140 69.967 1.00 5.76 ? 22 HOH B O 1 HETATM 6568 O O . HOH T 6 . ? 10.686 32.132 44.794 1.00 9.50 ? 24 HOH B O 1 HETATM 6569 O O . HOH T 6 . ? 10.251 23.610 62.754 1.00 10.42 ? 25 HOH B O 1 HETATM 6570 O O . HOH T 6 . ? -9.478 13.709 72.599 1.00 10.63 ? 29 HOH B O 1 HETATM 6571 O O . HOH T 6 . ? -19.790 23.536 54.570 1.00 10.71 ? 30 HOH B O 1 HETATM 6572 O O . HOH T 6 . ? -4.826 20.671 62.991 1.00 7.54 ? 33 HOH B O 1 HETATM 6573 O O . HOH T 6 . ? -4.381 18.084 63.761 1.00 7.92 ? 36 HOH B O 1 HETATM 6574 O O . HOH T 6 . ? 15.489 27.279 71.449 1.00 11.16 ? 37 HOH B O 1 HETATM 6575 O O . HOH T 6 . ? -8.844 7.561 37.920 1.00 11.06 ? 39 HOH B O 1 HETATM 6576 O O . HOH T 6 . ? -3.456 17.435 61.304 1.00 6.74 ? 44 HOH B O 1 HETATM 6577 O O . HOH T 6 . ? 4.359 44.140 64.593 1.00 7.50 ? 46 HOH B O 1 HETATM 6578 O O . HOH T 6 . ? 0.651 36.107 54.896 1.00 12.19 ? 47 HOH B O 1 HETATM 6579 O O . HOH T 6 . ? -7.792 10.960 45.715 1.00 10.49 ? 48 HOH B O 1 HETATM 6580 O O . HOH T 6 . ? -5.292 16.044 65.582 1.00 6.77 ? 49 HOH B O 1 HETATM 6581 O O . HOH T 6 . ? -8.769 14.827 47.530 1.00 9.51 ? 50 HOH B O 1 HETATM 6582 O O . HOH T 6 . ? -0.680 11.966 45.176 1.00 12.80 ? 55 HOH B O 1 HETATM 6583 O O . HOH T 6 . ? -11.237 25.189 77.513 1.00 28.08 ? 56 HOH B O 1 HETATM 6584 O O . HOH T 6 . ? 20.878 19.468 59.732 1.00 9.78 ? 58 HOH B O 1 HETATM 6585 O O . HOH T 6 . ? -19.172 23.787 51.961 1.00 6.13 ? 60 HOH B O 1 HETATM 6586 O O . HOH T 6 . ? 1.263 28.341 57.988 1.00 8.64 ? 61 HOH B O 1 HETATM 6587 O O . HOH T 6 . ? 1.322 35.993 52.132 1.00 12.13 ? 64 HOH B O 1 HETATM 6588 O O . HOH T 6 . ? 9.708 40.416 51.447 1.00 10.61 ? 65 HOH B O 1 HETATM 6589 O O . HOH T 6 . ? -20.877 18.559 61.473 1.00 14.46 ? 67 HOH B O 1 HETATM 6590 O O . HOH T 6 . ? 13.752 27.836 47.906 1.00 10.71 ? 72 HOH B O 1 HETATM 6591 O O . HOH T 6 . ? -9.567 38.739 53.242 1.00 9.37 ? 73 HOH B O 1 HETATM 6592 O O . HOH T 6 . ? -17.136 10.240 61.684 1.00 11.58 ? 74 HOH B O 1 HETATM 6593 O O . HOH T 6 . ? -19.210 11.505 52.674 1.00 18.44 ? 78 HOH B O 1 HETATM 6594 O O . HOH T 6 . ? 8.256 25.307 61.882 1.00 8.96 ? 79 HOH B O 1 HETATM 6595 O O . HOH T 6 . ? 1.356 33.809 50.662 1.00 12.66 ? 80 HOH B O 1 HETATM 6596 O O . HOH T 6 . ? -21.303 24.177 60.332 1.00 36.88 ? 334 HOH B O 1 HETATM 6597 O O . HOH T 6 . ? -9.273 44.937 61.241 1.00 39.63 ? 338 HOH B O 1 HETATM 6598 O O . HOH T 6 . ? 12.442 17.272 57.402 1.00 49.54 ? 393 HOH B O 1 HETATM 6599 O O . HOH T 6 . ? 12.010 8.361 71.906 1.00 42.55 ? 471 HOH B O 1 HETATM 6600 O O . HOH T 6 . ? 1.361 20.793 81.916 1.00 29.28 ? 472 HOH B O 1 HETATM 6601 O O . HOH T 6 . ? 6.059 34.094 76.975 1.00 12.41 ? 473 HOH B O 1 HETATM 6602 O O . HOH T 6 . ? 2.403 4.364 43.473 1.00 11.23 ? 474 HOH B O 1 HETATM 6603 O O . HOH T 6 . ? -18.487 26.124 75.095 1.00 12.31 ? 475 HOH B O 1 HETATM 6604 O O . HOH T 6 . ? -18.126 9.213 56.809 1.00 31.39 ? 476 HOH B O 1 HETATM 6605 O O . HOH T 6 . ? 6.640 19.957 36.365 1.00 16.34 ? 477 HOH B O 1 HETATM 6606 O O . HOH T 6 . ? -19.294 25.474 62.006 1.00 27.07 ? 478 HOH B O 1 HETATM 6607 O O . HOH T 6 . ? 8.810 46.528 68.699 1.00 28.94 ? 479 HOH B O 1 HETATM 6608 O O . HOH T 6 . ? -12.046 31.954 49.221 1.00 10.52 ? 480 HOH B O 1 HETATM 6609 O O . HOH T 6 . ? 18.080 5.531 45.452 1.00 34.97 ? 481 HOH B O 1 HETATM 6610 O O . HOH T 6 . ? 12.035 8.589 56.996 1.00 33.10 ? 482 HOH B O 1 HETATM 6611 O O . HOH T 6 . ? 16.966 24.519 46.073 1.00 10.76 ? 483 HOH B O 1 HETATM 6612 O O . HOH T 6 . ? -9.849 27.592 83.175 1.00 36.37 ? 484 HOH B O 1 HETATM 6613 O O . HOH T 6 . ? 23.426 34.142 55.409 1.00 43.45 ? 485 HOH B O 1 HETATM 6614 O O . HOH T 6 . ? -0.868 5.455 56.190 1.00 14.14 ? 486 HOH B O 1 HETATM 6615 O O . HOH T 6 . ? -5.578 46.157 55.586 1.00 15.14 ? 487 HOH B O 1 HETATM 6616 O O . HOH T 6 . ? 0.000 10.723 29.628 0.50 28.59 ? 488 HOH B O 1 HETATM 6617 O O . HOH T 6 . ? -0.056 11.071 64.453 1.00 14.68 ? 489 HOH B O 1 HETATM 6618 O O . HOH T 6 . ? 7.830 37.134 49.643 1.00 17.72 ? 490 HOH B O 1 HETATM 6619 O O . HOH T 6 . ? 20.849 38.104 55.155 1.00 39.73 ? 491 HOH B O 1 HETATM 6620 O O . HOH T 6 . ? 8.493 31.041 43.058 1.00 26.48 ? 492 HOH B O 1 HETATM 6621 O O . HOH T 6 . ? 5.275 50.719 57.133 1.00 36.19 ? 493 HOH B O 1 HETATM 6622 O O . HOH T 6 . ? 1.906 25.707 37.676 1.00 12.78 ? 494 HOH B O 1 HETATM 6623 O O . HOH T 6 . ? 10.696 37.812 51.394 1.00 9.53 ? 495 HOH B O 1 HETATM 6624 O O . HOH T 6 . ? 15.555 16.529 76.413 1.00 15.82 ? 496 HOH B O 1 HETATM 6625 O O . HOH T 6 . ? -1.890 32.911 51.699 1.00 15.19 ? 497 HOH B O 1 HETATM 6626 O O . HOH T 6 . ? 20.831 19.926 70.072 1.00 28.38 ? 498 HOH B O 1 HETATM 6627 O O . HOH T 6 . ? 12.030 4.583 44.887 1.00 35.83 ? 499 HOH B O 1 HETATM 6628 O O . HOH T 6 . ? -8.117 33.133 43.431 1.00 45.54 ? 500 HOH B O 1 HETATM 6629 O O . HOH T 6 . ? -3.735 36.663 50.114 1.00 10.19 ? 503 HOH B O 1 HETATM 6630 O O . HOH T 6 . ? 7.275 35.669 42.313 1.00 11.08 ? 504 HOH B O 1 HETATM 6631 O O . HOH T 6 . ? 9.973 31.261 40.492 1.00 41.83 ? 505 HOH B O 1 HETATM 6632 O O . HOH T 6 . ? -5.122 20.919 66.572 1.00 11.46 ? 506 HOH B O 1 HETATM 6633 O O . HOH T 6 . ? 14.385 26.298 74.003 1.00 15.29 ? 507 HOH B O 1 HETATM 6634 O O . HOH T 6 . ? 6.071 47.662 59.424 1.00 36.71 ? 508 HOH B O 1 HETATM 6635 O O . HOH T 6 . ? -20.252 34.203 53.074 1.00 15.06 ? 509 HOH B O 1 HETATM 6636 O O . HOH T 6 . ? -12.786 38.198 70.750 1.00 39.08 ? 510 HOH B O 1 HETATM 6637 O O . HOH T 6 . ? -4.289 1.034 40.088 1.00 17.87 ? 511 HOH B O 1 HETATM 6638 O O . HOH T 6 . ? 4.692 41.449 41.336 1.00 35.18 ? 512 HOH B O 1 HETATM 6639 O O . HOH T 6 . ? 12.591 14.773 59.046 1.00 40.58 ? 513 HOH B O 1 HETATM 6640 O O . HOH T 6 . ? 9.102 11.540 73.361 1.00 40.30 ? 514 HOH B O 1 HETATM 6641 O O . HOH T 6 . ? 23.809 27.351 68.981 1.00 39.25 ? 515 HOH B O 1 HETATM 6642 O O . HOH T 6 . ? -3.667 52.764 51.471 1.00 41.59 ? 516 HOH B O 1 HETATM 6643 O O . HOH T 6 . ? -12.517 35.955 73.963 1.00 13.04 ? 517 HOH B O 1 HETATM 6644 O O . HOH T 6 . ? 8.484 17.322 57.449 1.00 39.61 ? 518 HOH B O 1 HETATM 6645 O O . HOH T 6 . ? 9.931 15.096 63.839 1.00 34.54 ? 519 HOH B O 1 HETATM 6646 O O . HOH T 6 . ? 6.834 23.778 80.994 1.00 30.00 ? 520 HOH B O 1 HETATM 6647 O O . HOH T 6 . ? -11.308 29.571 82.101 1.00 43.48 ? 521 HOH B O 1 HETATM 6648 O O . HOH T 6 . ? -8.415 17.750 40.353 1.00 16.15 ? 522 HOH B O 1 HETATM 6649 O O . HOH T 6 . ? -3.165 5.431 54.722 1.00 18.72 ? 523 HOH B O 1 HETATM 6650 O O . HOH T 6 . ? -9.394 9.821 53.232 1.00 11.14 ? 524 HOH B O 1 HETATM 6651 O O . HOH T 6 . ? 3.940 42.071 52.974 1.00 14.15 ? 525 HOH B O 1 HETATM 6652 O O . HOH T 6 . ? 5.971 51.303 52.986 1.00 35.49 ? 526 HOH B O 1 HETATM 6653 O O . HOH T 6 . ? -28.587 29.815 53.660 1.00 15.29 ? 527 HOH B O 1 HETATM 6654 O O . HOH T 6 . ? -4.608 43.749 56.359 1.00 13.48 ? 528 HOH B O 1 HETATM 6655 O O . HOH T 6 . ? 3.480 26.711 79.315 1.00 30.58 ? 529 HOH B O 1 HETATM 6656 O O . HOH T 6 . ? 20.767 35.841 67.901 1.00 42.44 ? 530 HOH B O 1 HETATM 6657 O O . HOH T 6 . ? 0.419 33.492 55.995 1.00 12.40 ? 531 HOH B O 1 HETATM 6658 O O . HOH T 6 . ? -16.685 29.112 78.022 1.00 36.97 ? 532 HOH B O 1 HETATM 6659 O O . HOH T 6 . ? -6.673 18.011 38.127 1.00 11.88 ? 533 HOH B O 1 HETATM 6660 O O . HOH T 6 . ? 0.266 28.681 78.198 1.00 17.23 ? 534 HOH B O 1 HETATM 6661 O O . HOH T 6 . ? -7.203 20.780 46.862 1.00 10.30 ? 535 HOH B O 1 HETATM 6662 O O . HOH T 6 . ? 3.980 48.349 61.278 1.00 42.86 ? 536 HOH B O 1 HETATM 6663 O O . HOH T 6 . ? 4.830 21.409 33.429 1.00 31.33 ? 537 HOH B O 1 HETATM 6664 O O . HOH T 6 . ? 19.079 34.591 69.712 1.00 12.04 ? 538 HOH B O 1 HETATM 6665 O O . HOH T 6 . ? 24.386 31.363 55.670 1.00 14.45 ? 539 HOH B O 1 HETATM 6666 O O . HOH T 6 . ? 17.550 24.176 73.418 1.00 30.38 ? 540 HOH B O 1 HETATM 6667 O O . HOH T 6 . ? -21.128 18.086 64.195 1.00 35.84 ? 541 HOH B O 1 HETATM 6668 O O . HOH T 6 . ? 7.102 9.170 56.978 1.00 37.96 ? 542 HOH B O 1 HETATM 6669 O O . HOH T 6 . ? -10.578 7.683 68.929 1.00 16.86 ? 543 HOH B O 1 HETATM 6670 O O . HOH T 6 . ? -9.189 5.044 65.544 1.00 37.35 ? 544 HOH B O 1 HETATM 6671 O O . HOH T 6 . ? -14.066 33.907 72.532 1.00 17.69 ? 545 HOH B O 1 HETATM 6672 O O . HOH T 6 . ? -2.534 29.578 76.122 1.00 12.19 ? 546 HOH B O 1 HETATM 6673 O O . HOH T 6 . ? 7.543 50.868 50.143 1.00 42.87 ? 547 HOH B O 1 HETATM 6674 O O . HOH T 6 . ? -21.524 28.742 59.330 1.00 18.42 ? 548 HOH B O 1 HETATM 6675 O O . HOH T 6 . ? 13.764 -1.875 39.150 1.00 33.00 ? 549 HOH B O 1 HETATM 6676 O O . HOH T 6 . ? -4.775 7.656 76.895 1.00 30.95 ? 550 HOH B O 1 HETATM 6677 O O . HOH T 6 . ? 25.717 33.636 56.207 1.00 41.48 ? 551 HOH B O 1 HETATM 6678 O O . HOH T 6 . ? 9.111 14.819 79.478 1.00 21.69 ? 552 HOH B O 1 HETATM 6679 O O . HOH T 6 . ? 12.496 13.796 78.238 1.00 36.99 ? 553 HOH B O 1 HETATM 6680 O O . HOH T 6 . ? 5.242 10.304 63.549 1.00 40.39 ? 554 HOH B O 1 HETATM 6681 O O . HOH T 6 . ? 21.246 17.366 68.792 1.00 28.88 ? 555 HOH B O 1 HETATM 6682 O O . HOH T 6 . ? 19.279 14.318 54.749 1.00 15.11 ? 556 HOH B O 1 HETATM 6683 O O . HOH T 6 . ? 6.553 14.762 80.611 1.00 44.64 ? 557 HOH B O 1 HETATM 6684 O O . HOH T 6 . ? 6.959 0.704 37.004 1.00 15.42 ? 558 HOH B O 1 HETATM 6685 O O . HOH T 6 . ? -12.938 12.996 73.878 1.00 21.92 ? 559 HOH B O 1 HETATM 6686 O O . HOH T 6 . ? -4.428 7.648 72.079 1.00 17.56 ? 560 HOH B O 1 HETATM 6687 O O . HOH T 6 . ? -26.344 15.359 57.214 1.00 33.67 ? 561 HOH B O 1 HETATM 6688 O O . HOH T 6 . ? 14.991 45.099 58.442 1.00 33.11 ? 562 HOH B O 1 HETATM 6689 O O . HOH T 6 . ? -8.896 1.469 49.662 1.00 15.80 ? 563 HOH B O 1 HETATM 6690 O O . HOH T 6 . ? -6.794 40.890 65.925 1.00 27.08 ? 564 HOH B O 1 HETATM 6691 O O . HOH T 6 . ? -1.431 49.820 60.626 1.00 32.76 ? 565 HOH B O 1 HETATM 6692 O O . HOH T 6 . ? 9.548 21.168 61.896 1.00 11.88 ? 566 HOH B O 1 HETATM 6693 O O . HOH T 6 . ? -4.381 -2.516 52.683 1.00 24.45 ? 567 HOH B O 1 HETATM 6694 O O . HOH T 6 . ? 2.483 9.094 72.365 1.00 17.61 ? 568 HOH B O 1 HETATM 6695 O O . HOH T 6 . ? 21.062 33.185 68.029 1.00 43.44 ? 569 HOH B O 1 HETATM 6696 O O . HOH T 6 . ? 2.787 38.255 71.242 1.00 22.57 ? 570 HOH B O 1 HETATM 6697 O O . HOH T 6 . ? -6.279 48.937 46.730 1.00 31.53 ? 571 HOH B O 1 HETATM 6698 O O . HOH T 6 . ? -8.566 44.610 47.382 1.00 34.17 ? 572 HOH B O 1 HETATM 6699 O O . HOH T 6 . ? -10.149 8.461 79.121 1.00 43.29 ? 573 HOH B O 1 HETATM 6700 O O . HOH T 6 . ? -6.983 37.610 69.110 1.00 27.41 ? 574 HOH B O 1 HETATM 6701 O O . HOH T 6 . ? -16.499 26.894 76.517 1.00 22.86 ? 575 HOH B O 1 HETATM 6702 O O . HOH T 6 . ? -5.322 46.248 43.824 1.00 42.58 ? 576 HOH B O 1 HETATM 6703 O O . HOH T 6 . ? -5.175 28.845 41.356 1.00 29.76 ? 577 HOH B O 1 HETATM 6704 O O . HOH T 6 . ? -19.467 11.341 58.982 1.00 43.33 ? 578 HOH B O 1 HETATM 6705 O O . HOH T 6 . ? 4.387 48.242 48.329 1.00 29.84 ? 579 HOH B O 1 HETATM 6706 O O . HOH T 6 . ? 23.325 38.816 52.940 1.00 36.18 ? 580 HOH B O 1 HETATM 6707 O O . HOH T 6 . ? -0.999 14.206 81.302 1.00 16.16 ? 581 HOH B O 1 HETATM 6708 O O . HOH T 6 . ? -6.729 31.009 42.832 1.00 24.72 ? 582 HOH B O 1 HETATM 6709 O O . HOH T 6 . ? 13.606 44.796 63.893 1.00 42.45 ? 583 HOH B O 1 HETATM 6710 O O . HOH T 6 . ? -19.205 35.436 55.242 1.00 28.80 ? 584 HOH B O 1 HETATM 6711 O O . HOH T 6 . ? 2.700 8.074 56.197 1.00 17.27 ? 585 HOH B O 1 HETATM 6712 O O . HOH T 6 . ? -9.026 38.596 43.634 1.00 39.94 ? 586 HOH B O 1 HETATM 6713 O O . HOH T 6 . ? -7.174 25.608 38.462 1.00 14.25 ? 587 HOH B O 1 HETATM 6714 O O . HOH T 6 . ? 19.553 38.735 63.868 1.00 17.34 ? 588 HOH B O 1 HETATM 6715 O O . HOH T 6 . ? 4.352 36.798 41.755 1.00 22.90 ? 589 HOH B O 1 HETATM 6716 O O . HOH T 6 . ? -8.294 46.898 55.605 1.00 41.88 ? 590 HOH B O 1 HETATM 6717 O O . HOH T 6 . ? 27.793 19.761 59.447 1.00 37.37 ? 591 HOH B O 1 HETATM 6718 O O . HOH T 6 . ? 16.159 42.962 51.950 1.00 20.89 ? 592 HOH B O 1 HETATM 6719 O O . HOH T 6 . ? -5.848 21.783 73.556 1.00 16.39 ? 593 HOH B O 1 HETATM 6720 O O . HOH T 6 . ? -15.523 0.533 47.592 1.00 45.43 ? 594 HOH B O 1 HETATM 6721 O O . HOH T 6 . ? -1.471 46.735 50.294 1.00 19.93 ? 595 HOH B O 1 HETATM 6722 O O . HOH T 6 . ? -20.789 10.993 54.977 1.00 33.75 ? 596 HOH B O 1 HETATM 6723 O O . HOH T 6 . ? -19.050 31.734 71.129 1.00 23.27 ? 597 HOH B O 1 HETATM 6724 O O . HOH T 6 . ? 20.190 37.166 44.771 1.00 22.06 ? 598 HOH B O 1 HETATM 6725 O O . HOH T 6 . ? -1.367 7.601 57.954 1.00 17.40 ? 599 HOH B O 1 HETATM 6726 O O . HOH T 6 . ? 3.816 44.085 69.923 1.00 33.33 ? 600 HOH B O 1 HETATM 6727 O O . HOH T 6 . ? 1.042 8.912 58.337 1.00 15.14 ? 603 HOH B O 1 HETATM 6728 O O . HOH T 6 . ? -19.180 20.704 75.136 1.00 23.26 ? 604 HOH B O 1 HETATM 6729 O O . HOH T 6 . ? 22.284 12.317 56.394 1.00 24.55 ? 605 HOH B O 1 HETATM 6730 O O . HOH T 6 . ? -1.301 4.550 32.878 1.00 35.04 ? 606 HOH B O 1 HETATM 6731 O O . HOH T 6 . ? -23.588 28.161 61.169 1.00 38.68 ? 607 HOH B O 1 HETATM 6732 O O . HOH T 6 . ? 7.882 44.681 57.910 1.00 30.06 ? 608 HOH B O 1 HETATM 6733 O O . HOH T 6 . ? 0.266 43.498 44.616 1.00 22.59 ? 609 HOH B O 1 HETATM 6734 O O . HOH T 6 . ? 0.341 7.510 72.752 1.00 19.92 ? 610 HOH B O 1 HETATM 6735 O O . HOH T 6 . ? -10.501 5.356 63.124 1.00 32.60 ? 611 HOH B O 1 HETATM 6736 O O . HOH T 6 . ? -9.979 6.999 53.616 1.00 18.03 ? 612 HOH B O 1 HETATM 6737 O O . HOH T 6 . ? -2.331 18.314 36.207 1.00 27.67 ? 613 HOH B O 1 HETATM 6738 O O . HOH T 6 . ? 12.429 10.466 47.194 1.00 21.71 ? 614 HOH B O 1 HETATM 6739 O O . HOH T 6 . ? 8.673 43.843 49.764 1.00 22.63 ? 615 HOH B O 1 HETATM 6740 O O . HOH T 6 . ? -16.282 7.460 58.470 1.00 20.62 ? 616 HOH B O 1 HETATM 6741 O O . HOH T 6 . ? -4.950 21.468 45.486 1.00 21.82 ? 617 HOH B O 1 HETATM 6742 O O . HOH T 6 . ? -1.279 30.527 57.513 1.00 18.22 ? 618 HOH B O 1 HETATM 6743 O O . HOH T 6 . ? 6.418 29.911 79.703 1.00 41.82 ? 619 HOH B O 1 HETATM 6744 O O . HOH T 6 . ? -4.831 26.109 34.810 1.00 45.26 ? 620 HOH B O 1 HETATM 6745 O O . HOH T 6 . ? -15.586 5.832 44.203 1.00 34.13 ? 621 HOH B O 1 HETATM 6746 O O . HOH T 6 . ? 4.927 50.082 59.512 1.00 31.62 ? 622 HOH B O 1 HETATM 6747 O O . HOH T 6 . ? 20.399 33.062 61.938 1.00 41.36 ? 623 HOH B O 1 HETATM 6748 O O . HOH T 6 . ? -7.354 8.690 77.217 1.00 23.81 ? 624 HOH B O 1 HETATM 6749 O O . HOH T 6 . ? 8.447 -1.981 49.547 1.00 43.05 ? 625 HOH B O 1 HETATM 6750 O O . HOH T 6 . ? 4.964 16.972 79.365 1.00 24.43 ? 626 HOH B O 1 HETATM 6751 O O . HOH T 6 . ? -8.376 8.587 30.784 1.00 25.01 ? 627 HOH B O 1 HETATM 6752 O O . HOH T 6 . ? 10.789 11.393 67.582 1.00 28.33 ? 628 HOH B O 1 HETATM 6753 O O . HOH T 6 . ? -13.326 30.993 81.159 1.00 27.52 ? 629 HOH B O 1 HETATM 6754 O O . HOH T 6 . ? -22.073 21.901 66.797 1.00 20.75 ? 630 HOH B O 1 HETATM 6755 O O . HOH T 6 . ? 11.173 29.099 44.092 1.00 15.03 ? 631 HOH B O 1 HETATM 6756 O O . HOH T 6 . ? -2.796 24.885 83.426 1.00 27.51 ? 632 HOH B O 1 HETATM 6757 O O . HOH T 6 . ? -17.930 34.714 51.862 1.00 21.35 ? 633 HOH B O 1 HETATM 6758 O O . HOH T 6 . ? -11.570 4.595 49.916 1.00 30.62 ? 634 HOH B O 1 HETATM 6759 O O . HOH T 6 . ? -24.877 26.867 59.090 1.00 22.22 ? 635 HOH B O 1 HETATM 6760 O O . HOH T 6 . ? 14.963 38.268 43.482 1.00 22.71 ? 636 HOH B O 1 HETATM 6761 O O . HOH T 6 . ? 23.033 29.068 61.063 1.00 19.51 ? 637 HOH B O 1 HETATM 6762 O O . HOH T 6 . ? 8.955 11.409 70.142 1.00 25.08 ? 638 HOH B O 1 HETATM 6763 O O . HOH T 6 . ? 25.663 22.490 60.059 1.00 22.31 ? 639 HOH B O 1 HETATM 6764 O O . HOH T 6 . ? -18.552 34.724 63.468 1.00 24.72 ? 640 HOH B O 1 HETATM 6765 O O . HOH T 6 . ? -12.039 26.801 81.854 1.00 37.17 ? 641 HOH B O 1 HETATM 6766 O O . HOH T 6 . ? 6.878 18.231 80.937 1.00 33.00 ? 642 HOH B O 1 HETATM 6767 O O . HOH T 6 . ? 3.500 30.503 37.643 1.00 44.50 ? 643 HOH B O 1 HETATM 6768 O O . HOH T 6 . ? 21.805 39.808 59.313 1.00 36.03 ? 644 HOH B O 1 HETATM 6769 O O . HOH T 6 . ? -1.829 6.409 71.519 1.00 20.36 ? 645 HOH B O 1 HETATM 6770 O O . HOH T 6 . ? -12.652 10.551 73.080 1.00 36.56 ? 646 HOH B O 1 HETATM 6771 O O . HOH T 6 . ? -16.141 43.961 51.163 1.00 37.43 ? 648 HOH B O 1 HETATM 6772 O O . HOH T 6 . ? 18.597 10.316 56.768 1.00 35.38 ? 650 HOH B O 1 HETATM 6773 O O . HOH T 6 . ? 2.376 19.994 54.832 1.00 21.95 ? 651 HOH B O 1 HETATM 6774 O O . HOH T 6 . ? -1.537 35.531 51.353 1.00 15.21 ? 652 HOH B O 1 HETATM 6775 O O . HOH T 6 . ? -1.422 37.520 65.605 1.00 23.66 ? 653 HOH B O 1 HETATM 6776 O O . HOH T 6 . ? 17.740 17.293 73.890 1.00 23.04 ? 654 HOH B O 1 HETATM 6777 O O . HOH T 6 . ? 24.316 13.202 58.153 1.00 22.25 ? 655 HOH B O 1 HETATM 6778 O O . HOH T 6 . ? -1.627 35.994 69.154 1.00 39.97 ? 656 HOH B O 1 HETATM 6779 O O . HOH T 6 . ? 6.129 10.245 52.747 1.00 19.19 ? 657 HOH B O 1 HETATM 6780 O O . HOH T 6 . ? -7.044 26.898 40.955 1.00 23.74 ? 658 HOH B O 1 HETATM 6781 O O . HOH T 6 . ? -4.704 22.225 84.585 1.00 26.47 ? 659 HOH B O 1 HETATM 6782 O O . HOH T 6 . ? -10.004 38.780 65.194 1.00 21.31 ? 660 HOH B O 1 HETATM 6783 O O . HOH T 6 . ? -2.267 39.669 67.318 1.00 45.13 ? 661 HOH B O 1 HETATM 6784 O O . HOH T 6 . ? 9.253 19.489 59.615 1.00 29.45 ? 662 HOH B O 1 HETATM 6785 O O . HOH T 6 . ? -1.385 5.678 68.960 1.00 40.38 ? 663 HOH B O 1 HETATM 6786 O O . HOH T 6 . ? 2.456 33.745 77.593 1.00 37.94 ? 664 HOH B O 1 HETATM 6787 O O . HOH T 6 . ? 1.025 8.575 38.111 1.00 17.97 ? 665 HOH B O 1 HETATM 6788 O O . HOH T 6 . ? -24.246 11.487 53.224 1.00 25.72 ? 666 HOH B O 1 HETATM 6789 O O . HOH T 6 . ? 20.023 42.740 58.923 1.00 42.77 ? 667 HOH B O 1 HETATM 6790 O O . HOH T 6 . ? -0.608 35.363 71.490 1.00 35.24 ? 668 HOH B O 1 HETATM 6791 O O . HOH T 6 . ? -4.671 46.342 52.745 1.00 24.84 ? 669 HOH B O 1 HETATM 6792 O O . HOH T 6 . ? 8.280 33.139 41.517 1.00 29.44 ? 670 HOH B O 1 HETATM 6793 O O . HOH T 6 . ? 28.418 17.255 56.487 1.00 43.61 ? 671 HOH B O 1 HETATM 6794 O O . HOH T 6 . ? 7.969 32.422 78.431 1.00 37.64 ? 672 HOH B O 1 HETATM 6795 O O . HOH T 6 . ? 22.927 41.360 62.675 1.00 43.69 ? 673 HOH B O 1 HETATM 6796 O O . HOH T 6 . ? -3.726 8.791 57.477 1.00 15.79 ? 674 HOH B O 1 HETATM 6797 O O . HOH T 6 . ? -14.761 45.814 52.408 1.00 26.49 ? 675 HOH B O 1 HETATM 6798 O O . HOH T 6 . ? 4.420 12.409 58.929 1.00 18.07 ? 676 HOH B O 1 HETATM 6799 O O . HOH T 6 . ? 4.893 12.397 77.000 1.00 25.97 ? 677 HOH B O 1 HETATM 6800 O O . HOH T 6 . ? -20.982 9.979 51.324 1.00 39.58 ? 678 HOH B O 1 HETATM 6801 O O . HOH T 6 . ? -11.353 7.179 51.061 1.00 25.98 ? 679 HOH B O 1 HETATM 6802 O O . HOH T 6 . ? 14.182 28.585 40.868 1.00 20.23 ? 680 HOH B O 1 HETATM 6803 O O . HOH T 6 . ? 13.310 38.823 70.721 1.00 22.11 ? 681 HOH B O 1 HETATM 6804 O O . HOH T 6 . ? 20.432 43.025 49.846 1.00 35.64 ? 682 HOH B O 1 HETATM 6805 O O . HOH T 6 . ? -15.223 16.405 74.249 1.00 25.74 ? 683 HOH B O 1 HETATM 6806 O O . HOH T 6 . ? -6.374 45.033 63.455 1.00 38.69 ? 685 HOH B O 1 HETATM 6807 O O . HOH T 6 . ? -8.705 4.947 69.296 1.00 38.57 ? 686 HOH B O 1 HETATM 6808 O O . HOH T 6 . ? 20.801 30.447 62.291 1.00 37.12 ? 687 HOH B O 1 HETATM 6809 O O . HOH T 6 . ? 2.731 44.921 66.908 1.00 41.31 ? 688 HOH B O 1 HETATM 6810 O O . HOH T 6 . ? -7.898 37.101 66.247 1.00 18.82 ? 689 HOH B O 1 HETATM 6811 O O . HOH T 6 . ? 6.994 3.121 51.334 1.00 27.94 ? 690 HOH B O 1 HETATM 6812 O O . HOH T 6 . ? 10.420 32.593 76.977 1.00 23.34 ? 691 HOH B O 1 HETATM 6813 O O . HOH T 6 . ? -1.683 15.087 45.761 1.00 39.47 ? 692 HOH B O 1 HETATM 6814 O O . HOH T 6 . ? -16.618 34.601 72.192 1.00 22.81 ? 693 HOH B O 1 HETATM 6815 O O . HOH T 6 . ? 19.763 33.559 65.706 1.00 32.03 ? 694 HOH B O 1 HETATM 6816 O O . HOH T 6 . ? 1.641 0.085 37.394 1.00 27.09 ? 695 HOH B O 1 HETATM 6817 O O . HOH T 6 . ? 18.223 13.043 67.519 1.00 31.54 ? 696 HOH B O 1 HETATM 6818 O O . HOH T 6 . ? 12.433 -4.341 34.626 1.00 42.81 ? 697 HOH B O 1 HETATM 6819 O O . HOH T 6 . ? -4.439 30.368 80.934 1.00 32.97 ? 698 HOH B O 1 HETATM 6820 O O . HOH T 6 . ? -4.848 35.369 66.272 1.00 24.99 ? 699 HOH B O 1 HETATM 6821 O O . HOH T 6 . ? -3.084 47.370 48.215 1.00 29.09 ? 700 HOH B O 1 HETATM 6822 O O . HOH T 6 . ? 17.053 12.541 72.430 1.00 46.08 ? 701 HOH B O 1 HETATM 6823 O O . HOH T 6 . ? -16.735 9.141 54.448 1.00 22.06 ? 702 HOH B O 1 HETATM 6824 O O . HOH T 6 . ? 5.369 10.473 50.039 1.00 19.74 ? 703 HOH B O 1 HETATM 6825 O O . HOH T 6 . ? 15.534 12.795 67.287 1.00 34.00 ? 704 HOH B O 1 HETATM 6826 O O . HOH T 6 . ? -18.372 14.948 86.207 1.00 22.45 ? 705 HOH B O 1 HETATM 6827 O O . HOH T 6 . ? 8.626 14.882 61.539 1.00 26.94 ? 706 HOH B O 1 HETATM 6828 O O . HOH T 6 . ? -23.610 20.033 59.790 1.00 25.20 ? 707 HOH B O 1 HETATM 6829 O O . HOH T 6 . ? 12.145 10.138 50.466 1.00 31.52 ? 708 HOH B O 1 HETATM 6830 O O . HOH T 6 . ? 10.427 35.189 76.538 1.00 29.26 ? 709 HOH B O 1 HETATM 6831 O O . HOH T 6 . ? 10.252 44.161 51.945 1.00 28.69 ? 710 HOH B O 1 HETATM 6832 O O . HOH T 6 . ? 9.488 17.846 62.299 1.00 29.49 ? 711 HOH B O 1 HETATM 6833 O O . HOH T 6 . ? 17.275 40.278 48.213 1.00 29.42 ? 712 HOH B O 1 HETATM 6834 O O . HOH T 6 . ? 4.051 10.009 75.535 1.00 29.07 ? 713 HOH B O 1 HETATM 6835 O O . HOH T 6 . ? -2.276 -5.019 43.623 1.00 35.78 ? 714 HOH B O 1 HETATM 6836 O O . HOH T 6 . ? -25.864 23.237 68.675 1.00 39.56 ? 715 HOH B O 1 HETATM 6837 O O . HOH T 6 . ? 2.934 -4.612 48.637 1.00 35.68 ? 716 HOH B O 1 HETATM 6838 O O . HOH T 6 . ? -2.921 24.161 34.728 1.00 38.19 ? 717 HOH B O 1 HETATM 6839 O O . HOH T 6 . ? 20.858 31.537 69.985 1.00 23.64 ? 718 HOH B O 1 HETATM 6840 O O . HOH T 6 . ? -3.341 19.883 44.353 1.00 20.83 ? 719 HOH B O 1 HETATM 6841 O O . HOH T 6 . ? 0.436 36.140 41.695 1.00 35.39 ? 720 HOH B O 1 HETATM 6842 O O . HOH T 6 . ? -16.592 17.606 76.057 1.00 32.04 ? 721 HOH B O 1 HETATM 6843 O O . HOH T 6 . ? -2.963 45.606 46.259 1.00 38.39 ? 722 HOH B O 1 HETATM 6844 O O . HOH T 6 . ? 21.613 33.090 57.144 1.00 39.37 ? 723 HOH B O 1 HETATM 6845 O O . HOH T 6 . ? -18.711 18.601 77.957 1.00 40.32 ? 724 HOH B O 1 HETATM 6846 O O . HOH T 6 . ? 28.833 20.265 56.931 1.00 34.29 ? 725 HOH B O 1 HETATM 6847 O O . HOH T 6 . ? -17.797 12.003 64.596 1.00 39.75 ? 726 HOH B O 1 HETATM 6848 O O . HOH T 6 . ? 19.435 11.594 54.706 1.00 34.76 ? 727 HOH B O 1 HETATM 6849 O O . HOH T 6 . ? 1.514 47.574 60.481 1.00 31.85 ? 728 HOH B O 1 HETATM 6850 O O . HOH T 6 . ? -2.372 46.665 63.252 1.00 33.17 ? 729 HOH B O 1 HETATM 6851 O O . HOH T 6 . ? 12.541 3.730 51.478 1.00 37.18 ? 730 HOH B O 1 HETATM 6852 O O . HOH T 6 . ? 14.607 12.928 75.863 1.00 38.94 ? 731 HOH B O 1 HETATM 6853 O O . HOH T 6 . ? -9.774 45.928 51.407 1.00 35.42 ? 732 HOH B O 1 HETATM 6854 O O . HOH T 6 . ? 14.759 20.748 78.678 1.00 30.73 ? 733 HOH B O 1 HETATM 6855 O O . HOH T 6 . ? -21.262 12.807 57.559 1.00 42.06 ? 734 HOH B O 1 HETATM 6856 O O . HOH T 6 . ? 17.887 14.764 73.977 1.00 48.97 ? 735 HOH B O 1 HETATM 6857 O O . HOH T 6 . ? -3.839 43.108 42.951 1.00 36.84 ? 736 HOH B O 1 HETATM 6858 O O . HOH T 6 . ? -6.905 37.063 40.178 1.00 39.84 ? 737 HOH B O 1 HETATM 6859 O O . HOH T 6 . ? -6.882 -0.063 52.149 1.00 44.04 ? 738 HOH B O 1 HETATM 6860 O O . HOH T 6 . ? -10.857 23.640 84.408 1.00 31.89 ? 739 HOH B O 1 HETATM 6861 O O . HOH T 6 . ? 9.578 55.530 60.673 1.00 32.67 ? 741 HOH B O 1 HETATM 6862 O O . HOH T 6 . ? -1.205 43.735 46.819 1.00 21.24 ? 742 HOH B O 1 HETATM 6863 O O . HOH T 6 . ? -1.720 43.782 67.130 1.00 36.73 ? 743 HOH B O 1 HETATM 6864 O O . HOH T 6 . ? -2.016 7.169 62.001 1.00 26.84 ? 744 HOH B O 1 HETATM 6865 O O . HOH T 6 . ? 12.938 39.574 41.263 1.00 40.81 ? 745 HOH B O 1 HETATM 6866 O O . HOH T 6 . ? 0.639 16.752 82.088 1.00 34.16 ? 746 HOH B O 1 HETATM 6867 O O . HOH T 6 . ? 19.762 11.338 61.375 1.00 35.17 ? 747 HOH B O 1 HETATM 6868 O O . HOH T 6 . ? -20.421 24.867 76.526 1.00 36.88 ? 748 HOH B O 1 HETATM 6869 O O . HOH T 6 . ? 16.310 14.896 65.148 1.00 29.50 ? 749 HOH B O 1 HETATM 6870 O O . HOH T 6 . ? 10.407 46.635 62.069 1.00 47.08 ? 750 HOH B O 1 HETATM 6871 O O . HOH T 6 . ? 5.240 12.544 61.482 1.00 21.36 ? 751 HOH B O 1 HETATM 6872 O O . HOH T 6 . ? -27.594 21.985 67.001 1.00 40.07 ? 752 HOH B O 1 HETATM 6873 O O . HOH T 6 . ? 12.633 20.284 80.513 1.00 45.76 ? 753 HOH B O 1 HETATM 6874 O O . HOH T 6 . ? -2.534 46.057 65.941 1.00 38.03 ? 755 HOH B O 1 HETATM 6875 O O . HOH T 6 . ? 15.429 18.136 79.023 1.00 35.32 ? 756 HOH B O 1 HETATM 6876 O O . HOH T 6 . ? -13.817 4.896 46.009 1.00 42.96 ? 757 HOH B O 1 HETATM 6877 O O . HOH T 6 . ? -3.907 49.904 44.933 1.00 42.81 ? 758 HOH B O 1 HETATM 6878 O O . HOH T 6 . ? 20.423 13.375 62.947 1.00 33.15 ? 759 HOH B O 1 HETATM 6879 O O . HOH T 6 . ? 15.618 44.896 53.648 1.00 45.05 ? 760 HOH B O 1 HETATM 6880 O O . HOH T 6 . ? -2.496 55.919 48.926 1.00 36.84 ? 761 HOH B O 1 HETATM 6881 O O . HOH T 6 . ? 7.041 12.568 54.017 1.00 27.98 ? 762 HOH B O 1 HETATM 6882 O O . HOH T 6 . ? 15.461 47.339 64.926 1.00 43.86 ? 763 HOH B O 1 HETATM 6883 O O . HOH T 6 . ? -2.742 49.986 47.373 1.00 31.74 ? 764 HOH B O 1 HETATM 6884 O O . HOH T 6 . ? -5.520 44.529 45.823 1.00 36.50 ? 765 HOH B O 1 HETATM 6885 O O . HOH T 6 . ? -16.924 16.771 87.028 1.00 41.76 ? 766 HOH B O 1 HETATM 6886 O O . HOH T 6 . ? -11.536 39.093 42.885 1.00 42.44 ? 767 HOH B O 1 HETATM 6887 O O . HOH T 6 . ? -13.903 20.308 81.789 1.00 37.30 ? 768 HOH B O 1 HETATM 6888 O O . HOH T 6 . ? 22.887 36.332 51.580 1.00 37.45 ? 769 HOH B O 1 HETATM 6889 O O . HOH T 6 . ? 5.050 9.347 55.317 1.00 23.35 ? 770 HOH B O 1 HETATM 6890 O O . HOH T 6 . ? -10.319 18.718 87.077 1.00 43.17 ? 771 HOH B O 1 HETATM 6891 O O . HOH T 6 . ? 14.933 40.913 44.740 1.00 39.92 ? 772 HOH B O 1 HETATM 6892 O O . HOH T 6 . ? -14.199 16.624 85.082 1.00 45.27 ? 773 HOH B O 1 HETATM 6893 O O . HOH T 6 . ? -23.020 33.662 61.351 1.00 36.65 ? 774 HOH B O 1 HETATM 6894 O O . HOH T 6 . ? 6.294 36.903 78.314 1.00 44.00 ? 775 HOH B O 1 HETATM 6895 O O . HOH T 6 . ? -1.611 45.125 42.119 1.00 40.37 ? 776 HOH B O 1 HETATM 6896 O O . HOH T 6 . ? 20.666 39.004 46.498 1.00 34.48 ? 777 HOH B O 1 HETATM 6897 O O . HOH T 6 . ? 2.440 50.462 58.815 1.00 30.13 ? 778 HOH B O 1 HETATM 6898 O O . HOH T 6 . ? -15.177 42.434 58.974 1.00 45.25 ? 779 HOH B O 1 HETATM 6899 O O . HOH T 6 . ? -14.293 35.169 56.062 1.00 28.04 ? 780 HOH B O 1 HETATM 6900 O O . HOH T 6 . ? 11.567 28.189 39.334 1.00 38.65 ? 781 HOH B O 1 HETATM 6901 O O . HOH T 6 . ? 10.878 16.773 59.475 1.00 37.82 ? 782 HOH B O 1 HETATM 6902 O O . HOH T 6 . ? 18.949 37.688 67.936 1.00 20.38 ? 783 HOH B O 1 HETATM 6903 O O . HOH T 6 . ? 17.658 42.751 49.456 1.00 35.16 ? 784 HOH B O 1 HETATM 6904 O O . HOH T 6 . ? 0.000 24.274 29.628 0.50 35.35 ? 785 HOH B O 1 HETATM 6905 O O . HOH T 6 . ? 21.309 27.112 69.703 1.00 28.51 ? 786 HOH B O 1 HETATM 6906 O O . HOH T 6 . ? 17.892 45.848 57.467 1.00 38.93 ? 787 HOH B O 1 HETATM 6907 O O . HOH T 6 . ? -3.504 37.011 67.857 1.00 38.34 ? 788 HOH B O 1 HETATM 6908 O O . HOH T 6 . ? 13.139 43.445 72.646 1.00 34.32 ? 789 HOH B O 1 HETATM 6909 O O . HOH T 6 . ? -23.946 16.412 58.000 1.00 27.13 ? 790 HOH B O 1 HETATM 6910 O O . HOH T 6 . ? 7.442 45.506 66.139 1.00 22.11 ? 791 HOH B O 1 HETATM 6911 O O . HOH T 6 . ? 6.522 48.665 54.139 1.00 41.00 ? 792 HOH B O 1 HETATM 6912 O O . HOH T 6 . ? 0.769 46.387 69.869 1.00 50.66 ? 793 HOH B O 1 HETATM 6913 O O . HOH T 6 . ? 0.401 28.063 36.945 1.00 28.56 ? 794 HOH B O 1 HETATM 6914 O O . HOH T 6 . ? -13.464 35.610 70.479 1.00 34.59 ? 795 HOH B O 1 HETATM 6915 O O . HOH T 6 . ? 7.502 11.364 65.542 1.00 31.12 ? 796 HOH B O 1 HETATM 6916 O O . HOH T 6 . ? 10.063 16.049 55.695 1.00 41.41 ? 797 HOH B O 1 HETATM 6917 O O . HOH T 6 . ? 1.389 47.073 57.831 1.00 35.49 ? 798 HOH B O 1 HETATM 6918 O O . HOH T 6 . ? -5.706 47.485 64.458 1.00 41.77 ? 799 HOH B O 1 HETATM 6919 O O . HOH T 6 . ? 11.783 11.541 75.286 1.00 31.94 ? 800 HOH B O 1 HETATM 6920 O O . HOH T 6 . ? 7.454 38.674 76.430 1.00 37.43 ? 801 HOH B O 1 HETATM 6921 O O . HOH T 6 . ? 5.426 40.324 75.934 1.00 34.62 ? 802 HOH B O 1 HETATM 6922 O O . HOH T 6 . ? -14.329 38.493 47.621 1.00 24.25 ? 803 HOH B O 1 HETATM 6923 O O . HOH T 6 . ? 22.641 35.138 58.622 1.00 40.46 ? 804 HOH B O 1 HETATM 6924 O O . HOH T 6 . ? 11.195 -1.608 35.022 1.00 30.49 ? 805 HOH B O 1 HETATM 6925 O O . HOH T 6 . ? 7.518 15.095 58.732 1.00 41.22 ? 806 HOH B O 1 HETATM 6926 O O . HOH T 6 . ? -0.120 6.776 60.283 1.00 36.20 ? 807 HOH B O 1 HETATM 6927 O O . HOH T 6 . ? 1.409 33.459 41.593 1.00 29.11 ? 808 HOH B O 1 HETATM 6928 O O . HOH T 6 . ? 0.000 21.134 29.628 0.50 38.53 ? 809 HOH B O 1 HETATM 6929 O O . HOH T 6 . ? 22.366 37.034 46.823 1.00 41.72 ? 810 HOH B O 1 HETATM 6930 O O . HOH T 6 . ? -22.112 27.980 63.442 1.00 39.19 ? 811 HOH B O 1 HETATM 6931 O O . HOH T 6 . ? -6.928 23.857 85.293 1.00 36.42 ? 813 HOH B O 1 HETATM 6932 O O . HOH T 6 . ? -4.062 21.750 49.229 1.00 39.63 ? 814 HOH B O 1 HETATM 6933 O O . HOH T 6 . ? 12.915 35.568 38.192 1.00 22.57 ? 815 HOH B O 1 HETATM 6934 O O . HOH T 6 . ? 9.620 54.825 65.713 1.00 40.94 ? 816 HOH B O 1 HETATM 6935 O O . HOH T 6 . ? -19.834 15.557 81.923 1.00 38.11 ? 817 HOH B O 1 HETATM 6936 O O . HOH T 6 . ? 10.281 47.309 71.153 1.00 45.83 ? 818 HOH B O 1 HETATM 6937 O O . HOH T 6 . ? -8.423 11.426 79.270 1.00 28.96 ? 819 HOH B O 1 HETATM 6938 O O . HOH T 6 . ? -4.254 17.021 81.518 1.00 44.04 ? 820 HOH B O 1 HETATM 6939 O O . HOH T 6 . ? 15.788 44.701 65.569 1.00 41.44 ? 821 HOH B O 1 HETATM 6940 O O . HOH T 6 . ? -15.282 42.730 54.933 1.00 40.89 ? 822 HOH B O 1 HETATM 6941 O O . HOH T 6 . ? -22.009 13.747 82.322 1.00 40.95 ? 823 HOH B O 1 HETATM 6942 O O . HOH T 6 . ? 2.838 22.350 30.567 1.00 44.23 ? 824 HOH B O 1 HETATM 6943 O O . HOH T 6 . ? 22.948 14.249 63.063 1.00 32.32 ? 825 HOH B O 1 HETATM 6944 O O . HOH T 6 . ? -20.219 16.256 88.269 1.00 45.13 ? 826 HOH B O 1 HETATM 6945 O O . HOH T 6 . ? 14.742 43.782 61.184 1.00 32.48 ? 827 HOH B O 1 HETATM 6946 O O . HOH T 6 . ? -25.048 31.439 59.038 1.00 37.38 ? 828 HOH B O 1 HETATM 6947 O O . HOH T 6 . ? 24.388 12.124 60.658 1.00 46.16 ? 829 HOH B O 1 HETATM 6948 O O . HOH T 6 . ? 14.694 10.562 61.177 1.00 39.59 ? 831 HOH B O 1 HETATM 6949 O O . HOH T 6 . ? -15.606 48.387 52.064 1.00 42.31 ? 832 HOH B O 1 HETATM 6950 O O . HOH T 6 . ? 13.212 0.810 44.948 1.00 39.89 ? 833 HOH B O 1 HETATM 6951 O O . HOH T 6 . ? -10.020 22.219 86.904 1.00 42.53 ? 835 HOH B O 1 HETATM 6952 O O . HOH T 6 . ? 30.343 23.067 54.690 1.00 45.51 ? 838 HOH B O 1 HETATM 6953 O O . HOH T 6 . ? 3.005 -7.344 48.491 1.00 34.96 ? 839 HOH B O 1 HETATM 6954 O O . HOH T 6 . ? -19.738 30.147 78.108 1.00 34.39 ? 840 HOH B O 1 HETATM 6955 O O . HOH T 6 . ? -2.556 56.374 54.573 1.00 36.40 ? 842 HOH B O 1 HETATM 6956 O O . HOH T 6 . ? 2.813 -4.529 38.561 1.00 37.93 ? 847 HOH B O 1 HETATM 6957 O O . HOH T 6 . ? 3.573 53.860 59.574 1.00 33.58 ? 849 HOH B O 1 HETATM 6958 O O . HOH T 6 . ? 4.847 39.916 71.236 1.00 35.11 ? 850 HOH B O 1 HETATM 6959 O O . HOH T 6 . ? 19.299 27.242 73.429 1.00 32.43 ? 851 HOH B O 1 HETATM 6960 O O . HOH T 6 . ? 3.954 41.478 78.380 1.00 33.93 ? 854 HOH B O 1 HETATM 6961 O O . HOH T 6 . ? -9.736 43.299 44.717 1.00 37.91 ? 855 HOH B O 1 HETATM 6962 O O . HOH T 6 . ? -12.158 41.421 62.073 1.00 34.46 ? 857 HOH B O 1 HETATM 6963 O O . HOH T 6 . ? 20.964 37.854 61.111 1.00 42.86 ? 859 HOH B O 1 HETATM 6964 O O . HOH T 6 . ? 9.694 26.891 80.517 1.00 36.89 ? 861 HOH B O 1 HETATM 6965 O O . HOH T 6 . ? 3.036 55.503 57.491 1.00 37.30 ? 862 HOH B O 1 HETATM 6966 O O . HOH T 6 . ? -17.612 31.131 76.466 1.00 45.73 ? 866 HOH B O 1 HETATM 6967 O O . HOH T 6 . ? -16.837 25.941 80.829 1.00 41.44 ? 867 HOH B O 1 HETATM 6968 O O . HOH T 6 . ? 2.890 -2.285 37.060 1.00 41.63 ? 868 HOH B O 1 HETATM 6969 O O . HOH T 6 . ? 22.069 36.233 56.409 1.00 53.07 ? 869 HOH B O 1 HETATM 6970 O O . HOH T 6 . ? 35.707 20.349 61.926 1.00 43.72 ? 870 HOH B O 1 HETATM 6971 O O . HOH T 6 . ? 14.750 -6.113 48.190 1.00 49.96 ? 872 HOH B O 1 HETATM 6972 O O . HOH T 6 . ? 20.743 17.588 71.798 1.00 39.88 ? 873 HOH B O 1 HETATM 6973 O O . HOH T 6 . ? 7.401 12.627 59.801 1.00 41.74 ? 874 HOH B O 1 HETATM 6974 O O . HOH T 6 . ? -27.708 14.211 59.273 1.00 37.91 ? 875 HOH B O 1 HETATM 6975 O O . HOH T 6 . ? -15.624 18.474 83.284 1.00 44.53 ? 879 HOH B O 1 HETATM 6976 O O . HOH T 6 . ? -11.842 16.158 84.094 1.00 51.81 ? 887 HOH B O 1 HETATM 6977 O O . HOH T 6 . ? -0.892 38.065 72.627 1.00 43.33 ? 894 HOH B O 1 HETATM 6978 O O . HOH T 6 . ? 23.304 43.002 51.767 1.00 37.71 ? 895 HOH B O 1 HETATM 6979 O O . HOH T 6 . ? -3.536 56.469 51.892 1.00 46.57 ? 896 HOH B O 1 HETATM 6980 O O . HOH T 6 . ? -5.067 -6.073 44.023 1.00 43.46 ? 898 HOH B O 1 HETATM 6981 O O . HOH T 6 . ? 8.446 11.703 76.110 1.00 42.58 ? 899 HOH B O 1 HETATM 6982 O O . HOH T 6 . ? 2.331 8.422 30.743 1.00 59.74 ? 902 HOH B O 1 HETATM 6983 O O . HOH T 6 . ? -0.746 8.740 31.804 1.00 59.00 ? 903 HOH B O 1 HETATM 6984 O O . HOH T 6 . ? 0.000 5.228 29.628 0.50 33.87 ? 905 HOH B 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 . SER A 1 ? 0.6169 0.5862 0.6092 0.0062 0.0079 0.0153 82 SER A N 2 C CA . SER A 1 ? 0.4277 0.3990 0.4203 0.0051 0.0070 0.0144 82 SER A CA 3 C C . SER A 1 ? 0.3794 0.3490 0.3718 0.0039 0.0081 0.0145 82 SER A C 4 O O . SER A 1 ? 0.4157 0.3843 0.4076 0.0044 0.0091 0.0159 82 SER A O 5 C CB . SER A 1 ? 0.3817 0.3564 0.3741 0.0060 0.0061 0.0151 82 SER A CB 6 O OG . SER A 1 ? 0.4339 0.4105 0.4267 0.0067 0.0051 0.0147 82 SER A OG 7 N N . VAL A 2 ? 0.2721 0.2416 0.2649 0.0023 0.0077 0.0130 83 VAL A N 8 C CA . VAL A 2 ? 0.2338 0.2022 0.2267 0.0009 0.0086 0.0127 83 VAL A CA 9 C C . VAL A 2 ? 0.2376 0.2085 0.2310 -0.0001 0.0075 0.0116 83 VAL A C 10 O O . VAL A 2 ? 0.1943 0.1667 0.1881 -0.0004 0.0064 0.0105 83 VAL A O 11 C CB . VAL A 2 ? 0.2619 0.2271 0.2548 -0.0002 0.0096 0.0118 83 VAL A CB 12 C CG1 . VAL A 2 ? 0.2702 0.2343 0.2632 -0.0018 0.0106 0.0115 83 VAL A CG1 13 C CG2 . VAL A 2 ? 0.4108 0.3733 0.4034 0.0009 0.0108 0.0128 83 VAL A CG2 14 N N . LYS A 3 ? 0.2092 0.1807 0.2025 -0.0007 0.0080 0.0120 84 LYS A N 15 C CA . LYS A 3 ? 0.2067 0.1807 0.2005 -0.0016 0.0071 0.0110 84 LYS A CA 16 C C . LYS A 3 ? 0.2206 0.1942 0.2150 -0.0031 0.0069 0.0094 84 LYS A C 17 O O . LYS A 3 ? 0.1995 0.1707 0.1939 -0.0040 0.0079 0.0091 84 LYS A O 18 C CB . LYS A 3 ? 0.2596 0.2343 0.2532 -0.0019 0.0077 0.0118 84 LYS A CB 19 C CG . LYS A 3 ? 0.3460 0.3177 0.3392 -0.0026 0.0095 0.0125 84 LYS A CG 20 C CD . LYS A 3 ? 0.4259 0.3982 0.4186 -0.0024 0.0102 0.0138 84 LYS A CD 21 C CE . LYS A 3 ? 0.5481 0.5170 0.5403 -0.0025 0.0121 0.0151 84 LYS A CE 22 N NZ . LYS A 3 ? 0.5946 0.5640 0.5863 -0.0026 0.0129 0.0164 84 LYS A NZ 23 N N . LEU A 4 ? 0.1467 0.1229 0.1418 -0.0035 0.0057 0.0084 85 LEU A N 24 C CA . LEU A 4 ? 0.1670 0.1435 0.1627 -0.0048 0.0053 0.0069 85 LEU A CA 25 C C . LEU A 4 ? 0.1788 0.1549 0.1746 -0.0063 0.0063 0.0066 85 LEU A C 26 O O . LEU A 4 ? 0.1866 0.1636 0.1824 -0.0063 0.0066 0.0072 85 LEU A O 27 C CB . LEU A 4 ? 0.1080 0.0874 0.1044 -0.0046 0.0039 0.0062 85 LEU A CB 28 C CG . LEU A 4 ? 0.1653 0.1452 0.1615 -0.0033 0.0029 0.0064 85 LEU A CG 29 C CD1 . LEU A 4 ? 0.1393 0.1218 0.1362 -0.0031 0.0017 0.0056 85 LEU A CD1 30 C CD2 . LEU A 4 ? 0.1485 0.1268 0.1446 -0.0032 0.0030 0.0060 85 LEU A CD2 31 N N . ALA A 5 ? 0.1457 0.1205 0.1417 -0.0076 0.0068 0.0057 86 ALA A N 32 C CA . ALA A 5 ? 0.1446 0.1191 0.1409 -0.0092 0.0077 0.0052 86 ALA A CA 33 C C . ALA A 5 ? 0.1558 0.1335 0.1528 -0.0099 0.0069 0.0044 86 ALA A C 34 O O . ALA A 5 ? 0.1894 0.1681 0.1866 -0.0103 0.0073 0.0047 86 ALA A O 35 C CB . ALA A 5 ? 0.1747 0.1471 0.1709 -0.0105 0.0085 0.0041 86 ALA A CB 36 N N . GLY A 6 ? 0.1076 0.0872 0.1052 -0.0099 0.0057 0.0034 87 GLY A N 37 C CA . GLY A 6 ? 0.1402 0.1229 0.1386 -0.0104 0.0048 0.0027 87 GLY A CA 38 C C . GLY A 6 ? 0.1593 0.1427 0.1582 -0.0122 0.0055 0.0018 87 GLY A C 39 O O . GLY A 6 ? 0.1132 0.0993 0.1129 -0.0126 0.0051 0.0014 87 GLY A O 40 N N . ASN A 7 ? 0.1210 0.1022 0.1196 -0.0134 0.0065 0.0014 88 ASN A N 41 C CA . ASN A 7 ? 0.1246 0.1061 0.1235 -0.0154 0.0074 0.0004 88 ASN A CA 42 C C . ASN A 7 ? 0.1805 0.1635 0.1800 -0.0166 0.0069 -0.0011 88 ASN A C 43 O O . ASN A 7 ? 0.1731 0.1571 0.1730 -0.0184 0.0074 -0.0021 88 ASN A O 44 C CB . ASN A 7 ? 0.1740 0.1521 0.1723 -0.0162 0.0092 0.0009 88 ASN A CB 45 C CG . ASN A 7 ? 0.2609 0.2357 0.2586 -0.0160 0.0098 0.0008 88 ASN A CG 46 O OD1 . ASN A 7 ? 0.1995 0.1744 0.1970 -0.0149 0.0088 0.0008 88 ASN A OD1 47 N ND2 . ASN A 7 ? 0.3141 0.2858 0.3113 -0.0171 0.0115 0.0008 88 ASN A ND2 48 N N . SER A 8 ? 0.1779 0.1613 0.1773 -0.0157 0.0059 -0.0013 89 SER A N 49 C CA . SER A 8 ? 0.1421 0.1272 0.1418 -0.0166 0.0053 -0.0026 89 SER A CA 50 C C . SER A 8 ? 0.1673 0.1565 0.1680 -0.0163 0.0039 -0.0029 89 SER A C 51 O O . SER A 8 ? 0.1352 0.1255 0.1361 -0.0151 0.0034 -0.0021 89 SER A O 52 C CB . SER A 8 ? 0.1418 0.1252 0.1410 -0.0159 0.0049 -0.0027 89 SER A CB 53 O OG . SER A 8 ? 0.1675 0.1516 0.1666 -0.0140 0.0038 -0.0019 89 SER A OG 54 N N . SER A 9 ? 0.1161 0.1075 0.1172 -0.0173 0.0034 -0.0041 90 SER A N 55 C CA . SER A 9 ? 0.1220 0.1174 0.1240 -0.0169 0.0022 -0.0043 90 SER A CA 56 C C . SER A 9 ? 0.1727 0.1687 0.1746 -0.0152 0.0010 -0.0037 90 SER A C 57 O O . SER A 9 ? 0.1519 0.1456 0.1531 -0.0146 0.0010 -0.0035 90 SER A O 58 C CB . SER A 9 ? 0.1729 0.1710 0.1754 -0.0187 0.0022 -0.0056 90 SER A CB 59 O OG . SER A 9 ? 0.3520 0.3496 0.3546 -0.0205 0.0035 -0.0063 90 SER A OG 60 N N . LEU A 10 ? 0.1799 0.1789 0.1826 -0.0143 0.0000 -0.0035 91 LEU A N 61 C CA . LEU A 10 ? 0.2406 0.2404 0.2434 -0.0128 -0.0012 -0.0031 91 LEU A CA 62 C C . LEU A 10 ? 0.2054 0.2061 0.2080 -0.0135 -0.0015 -0.0038 91 LEU A C 63 O O . LEU A 10 ? 0.2417 0.2443 0.2446 -0.0150 -0.0013 -0.0048 91 LEU A O 64 C CB . LEU A 10 ? 0.1971 0.2002 0.2009 -0.0119 -0.0020 -0.0028 91 LEU A CB 65 C CG . LEU A 10 ? 0.2363 0.2389 0.2404 -0.0104 -0.0022 -0.0019 91 LEU A CG 66 C CD1 . LEU A 10 ? 0.1835 0.1894 0.1887 -0.0095 -0.0030 -0.0018 91 LEU A CD1 67 C CD2 . LEU A 10 ? 0.1722 0.1722 0.1755 -0.0092 -0.0024 -0.0013 91 LEU A CD2 68 N N . CYS A 11 ? 0.1606 0.1600 0.1627 -0.0125 -0.0020 -0.0035 92 CYS A N 69 C CA . CYS A 11 ? 0.2262 0.2265 0.2280 -0.0130 -0.0023 -0.0041 92 CYS A CA 70 C C . CYS A 11 ? 0.2301 0.2345 0.2327 -0.0126 -0.0033 -0.0041 92 CYS A C 71 O O . CYS A 11 ? 0.2000 0.2052 0.2031 -0.0111 -0.0041 -0.0032 92 CYS A O 72 C CB . CYS A 11 ? 0.2025 0.2006 0.2036 -0.0119 -0.0026 -0.0035 92 CYS A CB 73 S SG . CYS A 11 ? 0.3089 0.3024 0.3090 -0.0118 -0.0015 -0.0033 92 CYS A SG 74 N N . PRO A 12 ? 0.3042 0.3112 0.3070 -0.0140 -0.0034 -0.0050 93 PRO A N 75 C CA . PRO A 12 ? 0.2897 0.3008 0.2932 -0.0135 -0.0044 -0.0049 93 PRO A CA 76 C C . PRO A 12 ? 0.2636 0.2744 0.2667 -0.0122 -0.0051 -0.0043 93 PRO A C 77 O O . PRO A 12 ? 0.2722 0.2807 0.2744 -0.0126 -0.0048 -0.0046 93 PRO A O 78 C CB . PRO A 12 ? 0.3876 0.4013 0.3913 -0.0155 -0.0041 -0.0063 93 PRO A CB 79 C CG . PRO A 12 ? 0.4522 0.4634 0.4555 -0.0171 -0.0029 -0.0070 93 PRO A CG 80 C CD . PRO A 12 ? 0.3859 0.3925 0.3885 -0.0161 -0.0024 -0.0063 93 PRO A CD 81 N N . VAL A 13 ? 0.1857 0.1984 0.1895 -0.0107 -0.0060 -0.0033 94 VAL A N 82 C CA . VAL A 13 ? 0.1516 0.1638 0.1550 -0.0094 -0.0066 -0.0025 94 VAL A CA 83 C C . VAL A 13 ? 0.1411 0.1574 0.1452 -0.0087 -0.0075 -0.0021 94 VAL A C 84 O O . VAL A 13 ? 0.1420 0.1610 0.1470 -0.0085 -0.0077 -0.0020 94 VAL A O 85 C CB . VAL A 13 ? 0.1342 0.1435 0.1376 -0.0078 -0.0066 -0.0015 94 VAL A CB 86 C CG1 . VAL A 13 ? 0.2084 0.2141 0.2111 -0.0084 -0.0058 -0.0018 94 VAL A CG1 87 C CG2 . VAL A 13 ? 0.1633 0.1741 0.1677 -0.0068 -0.0069 -0.0009 94 VAL A CG2 88 N N . SER A 14 ? 0.1514 0.1680 0.1549 -0.0083 -0.0079 -0.0017 95 SER A N 89 C CA . SER A 14 ? 0.1223 0.1427 0.1262 -0.0075 -0.0088 -0.0011 95 SER A CA 90 C C . SER A 14 ? 0.1405 0.1599 0.1447 -0.0054 -0.0092 0.0004 95 SER A C 91 O O . SER A 14 ? 0.1204 0.1427 0.1253 -0.0043 -0.0098 0.0013 95 SER A O 92 C CB . SER A 14 ? 0.1578 0.1801 0.1609 -0.0085 -0.0090 -0.0017 95 SER A CB 93 O OG . SER A 14 ? 0.1828 0.2020 0.1849 -0.0083 -0.0088 -0.0015 95 SER A OG 94 N N . GLY A 15 ? 0.1343 0.1499 0.1381 -0.0048 -0.0089 0.0008 96 GLY A N 95 C CA . GLY A 15 ? 0.0895 0.1036 0.0934 -0.0031 -0.0091 0.0020 96 GLY A CA 96 C C . GLY A 15 ? 0.0941 0.1041 0.0977 -0.0028 -0.0087 0.0021 96 GLY A C 97 O O . GLY A 15 ? 0.1003 0.1085 0.1034 -0.0038 -0.0081 0.0013 96 GLY A O 98 N N . TRP A 16 ? 0.1046 0.1132 0.1084 -0.0014 -0.0088 0.0030 97 TRP A N 99 C CA . TRP A 16 ? 0.0968 0.1020 0.1004 -0.0010 -0.0084 0.0031 97 TRP A CA 100 C C . TRP A 16 ? 0.0961 0.0994 0.0991 -0.0005 -0.0085 0.0037 97 TRP A C 101 O O . TRP A 16 ? 0.0875 0.0917 0.0908 0.0005 -0.0088 0.0046 97 TRP A O 102 C CB . TRP A 16 ? 0.0810 0.0861 0.0856 0.0001 -0.0083 0.0034 97 TRP A CB 103 C CG . TRP A 16 ? 0.0824 0.0897 0.0876 -0.0004 -0.0083 0.0029 97 TRP A CG 104 C CD1 . TRP A 16 ? 0.0799 0.0906 0.0860 -0.0001 -0.0086 0.0032 97 TRP A CD1 105 C CD2 . TRP A 16 ? 0.0985 0.1050 0.1037 -0.0013 -0.0078 0.0022 97 TRP A CD2 106 N NE1 . TRP A 16 ? 0.1211 0.1331 0.1276 -0.0008 -0.0084 0.0025 97 TRP A NE1 107 C CE2 . TRP A 16 ? 0.0990 0.1083 0.1049 -0.0016 -0.0079 0.0019 97 TRP A CE2 108 C CE3 . TRP A 16 ? 0.0817 0.0855 0.0863 -0.0018 -0.0073 0.0018 97 TRP A CE3 109 C CZ2 . TRP A 16 ? 0.0673 0.0767 0.0734 -0.0025 -0.0074 0.0012 97 TRP A CZ2 110 C CZ3 . TRP A 16 ? 0.0910 0.0948 0.0957 -0.0026 -0.0069 0.0012 97 TRP A CZ3 111 C CH2 . TRP A 16 ? 0.0745 0.0810 0.0799 -0.0030 -0.0069 0.0009 97 TRP A CH2 112 N N . ALA A 17 ? 0.0876 0.0886 0.0899 -0.0011 -0.0081 0.0032 98 ALA A N 113 C CA . ALA A 17 ? 0.0761 0.0753 0.0778 -0.0007 -0.0081 0.0036 98 ALA A CA 114 C C . ALA A 17 ? 0.0817 0.0785 0.0836 0.0000 -0.0079 0.0039 98 ALA A C 115 O O . ALA A 17 ? 0.0913 0.0871 0.0933 -0.0003 -0.0076 0.0034 98 ALA A O 116 C CB . ALA A 17 ? 0.0982 0.0966 0.0989 -0.0018 -0.0079 0.0029 98 ALA A CB 117 N N . ILE A 18 ? 0.0909 0.0869 0.0929 0.0008 -0.0080 0.0046 99 ILE A N 118 C CA . ILE A 18 ? 0.0795 0.0734 0.0818 0.0013 -0.0077 0.0047 99 ILE A CA 119 C C . ILE A 18 ? 0.0992 0.0914 0.1009 0.0007 -0.0074 0.0041 99 ILE A C 120 O O . ILE A 18 ? 0.0804 0.0721 0.0813 0.0003 -0.0074 0.0041 99 ILE A O 121 C CB . ILE A 18 ? 0.0898 0.0831 0.0924 0.0022 -0.0078 0.0055 99 ILE A CB 122 C CG1 . ILE A 18 ? 0.0994 0.0910 0.1025 0.0027 -0.0074 0.0054 99 ILE A CG1 123 C CG2 . ILE A 18 ? 0.1087 0.1014 0.1105 0.0019 -0.0078 0.0058 99 ILE A CG2 124 C CD1 . ILE A 18 ? 0.1170 0.1079 0.1207 0.0037 -0.0073 0.0062 99 ILE A CD1 125 N N . TYR A 19 ? 0.0704 0.0616 0.0723 0.0008 -0.0072 0.0038 100 TYR A N 126 C CA . TYR A 19 ? 0.0647 0.0545 0.0661 0.0004 -0.0068 0.0034 100 TYR A CA 127 C C . TYR A 19 ? 0.0959 0.0844 0.0973 0.0008 -0.0067 0.0035 100 TYR A C 128 O O . TYR A 19 ? 0.0870 0.0746 0.0880 0.0006 -0.0066 0.0034 100 TYR A O 129 C CB . TYR A 19 ? 0.0900 0.0802 0.0915 0.0001 -0.0066 0.0029 100 TYR A CB 130 C CG . TYR A 19 ? 0.1252 0.1141 0.1260 -0.0004 -0.0062 0.0026 100 TYR A CG 131 C CD1 . TYR A 19 ? 0.1581 0.1464 0.1582 -0.0008 -0.0061 0.0025 100 TYR A CD1 132 C CD2 . TYR A 19 ? 0.1835 0.1721 0.1845 -0.0002 -0.0060 0.0025 100 TYR A CD2 133 C CE1 . TYR A 19 ? 0.1778 0.1649 0.1774 -0.0010 -0.0056 0.0024 100 TYR A CE1 134 C CE2 . TYR A 19 ? 0.1737 0.1612 0.1740 -0.0004 -0.0056 0.0024 100 TYR A CE2 135 C CZ . TYR A 19 ? 0.2146 0.2014 0.2143 -0.0008 -0.0054 0.0024 100 TYR A CZ 136 O OH . TYR A 19 ? 0.2899 0.2756 0.2891 -0.0009 -0.0049 0.0025 100 TYR A OH 137 N N . SER A 20 ? 0.0722 0.0607 0.0744 0.0014 -0.0067 0.0035 101 SER A N 138 C CA . SER A 20 ? 0.0922 0.0795 0.0945 0.0016 -0.0065 0.0034 101 SER A CA 139 C C . SER A 20 ? 0.0918 0.0788 0.0948 0.0023 -0.0065 0.0036 101 SER A C 140 O O . SER A 20 ? 0.0984 0.0863 0.1020 0.0027 -0.0065 0.0038 101 SER A O 141 C CB . SER A 20 ? 0.1117 0.0988 0.1139 0.0015 -0.0063 0.0029 101 SER A CB 142 O OG . SER A 20 ? 0.1476 0.1354 0.1503 0.0017 -0.0062 0.0026 101 SER A OG 143 N N . LYS A 21 ? 0.0555 0.0415 0.0587 0.0024 -0.0063 0.0036 102 LYS A N 144 C CA . LYS A 21 ? 0.1324 0.1176 0.1363 0.0029 -0.0060 0.0036 102 LYS A CA 145 C C . LYS A 21 ? 0.1315 0.1156 0.1354 0.0025 -0.0057 0.0031 102 LYS A C 146 O O . LYS A 21 ? 0.1176 0.1013 0.1211 0.0022 -0.0057 0.0032 102 LYS A O 147 C CB . LYS A 21 ? 0.0899 0.0748 0.0940 0.0033 -0.0060 0.0045 102 LYS A CB 148 C CG . LYS A 21 ? 0.0906 0.0746 0.0956 0.0040 -0.0056 0.0046 102 LYS A CG 149 C CD . LYS A 21 ? 0.1259 0.1097 0.1311 0.0046 -0.0056 0.0058 102 LYS A CD 150 C CE . LYS A 21 ? 0.1178 0.1009 0.1240 0.0056 -0.0051 0.0061 102 LYS A CE 151 N NZ . LYS A 21 ? 0.1564 0.1376 0.1630 0.0054 -0.0045 0.0053 102 LYS A NZ 152 N N . ASP A 22 ? 0.1155 0.0994 0.1199 0.0026 -0.0054 0.0024 103 ASP A N 153 C CA . ASP A 22 ? 0.1480 0.1313 0.1524 0.0022 -0.0051 0.0017 103 ASP A CA 154 C C . ASP A 22 ? 0.1244 0.1063 0.1293 0.0022 -0.0047 0.0016 103 ASP A C 155 O O . ASP A 22 ? 0.1348 0.1163 0.1396 0.0016 -0.0045 0.0010 103 ASP A O 156 C CB . ASP A 22 ? 0.1308 0.1151 0.1352 0.0020 -0.0051 0.0009 103 ASP A CB 157 C CG . ASP A 22 ? 0.1752 0.1596 0.1803 0.0025 -0.0049 0.0005 103 ASP A CG 158 O OD1 . ASP A 22 ? 0.1600 0.1435 0.1657 0.0030 -0.0046 0.0008 103 ASP A OD1 159 O OD2 . ASP A 22 ? 0.2621 0.2475 0.2670 0.0025 -0.0049 0.0001 103 ASP A OD2 160 N N . ASN A 23 ? 0.1070 0.0882 0.1126 0.0028 -0.0044 0.0020 104 ASN A N 161 C CA . ASN A 23 ? 0.1206 0.1001 0.1268 0.0029 -0.0038 0.0020 104 ASN A CA 162 C C . ASN A 23 ? 0.0989 0.0779 0.1054 0.0023 -0.0033 0.0007 104 ASN A C 163 O O . ASN A 23 ? 0.0878 0.0656 0.0945 0.0019 -0.0028 0.0003 104 ASN A O 164 C CB . ASN A 23 ? 0.1041 0.0829 0.1099 0.0025 -0.0038 0.0026 104 ASN A CB 165 C CG . ASN A 23 ? 0.1195 0.0986 0.1251 0.0031 -0.0041 0.0040 104 ASN A CG 166 O OD1 . ASN A 23 ? 0.0936 0.0725 0.0995 0.0039 -0.0040 0.0046 104 ASN A OD1 167 N ND2 . ASN A 23 ? 0.1413 0.1210 0.1461 0.0027 -0.0045 0.0043 104 ASN A ND2 168 N N . SER A 24 ? 0.0858 0.0659 0.0923 0.0024 -0.0034 -0.0001 105 SER A N 169 C CA . SER A 24 ? 0.1211 0.1014 0.1277 0.0018 -0.0031 -0.0015 105 SER A CA 170 C C . SER A 24 ? 0.1121 0.0907 0.1195 0.0017 -0.0022 -0.0022 105 SER A C 171 O O . SER A 24 ? 0.1435 0.1218 0.1509 0.0008 -0.0019 -0.0031 105 SER A O 172 C CB . SER A 24 ? 0.1285 0.1104 0.1350 0.0020 -0.0033 -0.0020 105 SER A CB 173 O OG . SER A 24 ? 0.2103 0.1937 0.2161 0.0019 -0.0039 -0.0015 105 SER A OG 174 N N . VAL A 25 ? 0.0891 0.0666 0.0972 0.0025 -0.0018 -0.0017 106 VAL A N 175 C CA . VAL A 25 ? 0.0973 0.0729 0.1062 0.0026 -0.0008 -0.0024 106 VAL A CA 176 C C . VAL A 25 ? 0.0820 0.0555 0.0910 0.0022 -0.0004 -0.0020 106 VAL A C 177 O O . VAL A 25 ? 0.1193 0.0916 0.1287 0.0015 0.0004 -0.0030 106 VAL A O 178 C CB . VAL A 25 ? 0.1036 0.0785 0.1132 0.0038 -0.0005 -0.0020 106 VAL A CB 179 C CG1 . VAL A 25 ? 0.1192 0.0919 0.1297 0.0039 0.0007 -0.0028 106 VAL A CG1 180 C CG2 . VAL A 25 ? 0.1459 0.1230 0.1554 0.0041 -0.0009 -0.0024 106 VAL A CG2 181 N N . ARG A 26 ? 0.0892 0.0627 0.0979 0.0026 -0.0008 -0.0005 107 ARG A N 182 C CA . ARG A 26 ? 0.0777 0.0496 0.0864 0.0022 -0.0004 0.0001 107 ARG A CA 183 C C . ARG A 26 ? 0.1052 0.0775 0.1136 0.0008 -0.0003 -0.0010 107 ARG A C 184 O O . ARG A 26 ? 0.1133 0.0841 0.1221 0.0001 0.0005 -0.0016 107 ARG A O 185 C CB . ARG A 26 ? 0.0662 0.0386 0.0744 0.0027 -0.0010 0.0018 107 ARG A CB 186 C CG . ARG A 26 ? 0.1057 0.0774 0.1143 0.0041 -0.0008 0.0031 107 ARG A CG 187 C CD . ARG A 26 ? 0.0826 0.0558 0.0906 0.0045 -0.0016 0.0045 107 ARG A CD 188 N NE . ARG A 26 ? 0.0902 0.0628 0.0977 0.0039 -0.0016 0.0052 107 ARG A NE 189 C CZ . ARG A 26 ? 0.1409 0.1120 0.1485 0.0043 -0.0011 0.0063 107 ARG A CZ 190 N NH1 . ARG A 26 ? 0.1202 0.0900 0.1286 0.0054 -0.0005 0.0070 107 ARG A NH1 191 N NH2 . ARG A 26 ? 0.0973 0.0681 0.1045 0.0037 -0.0010 0.0069 107 ARG A NH2 192 N N . ILE A 27 ? 0.0659 0.0404 0.0736 0.0004 -0.0012 -0.0013 108 ILE A N 193 C CA . ILE A 27 ? 0.0788 0.0543 0.0861 -0.0007 -0.0013 -0.0021 108 ILE A CA 194 C C . ILE A 27 ? 0.0966 0.0723 0.1044 -0.0015 -0.0007 -0.0039 108 ILE A C 195 O O . ILE A 27 ? 0.1103 0.0860 0.1182 -0.0025 -0.0004 -0.0048 108 ILE A O 196 C CB . ILE A 27 ? 0.0791 0.0569 0.0856 -0.0007 -0.0022 -0.0018 108 ILE A CB 197 C CG1 . ILE A 27 ? 0.1077 0.0853 0.1138 -0.0002 -0.0026 -0.0003 108 ILE A CG1 198 C CG2 . ILE A 27 ? 0.0795 0.0587 0.0857 -0.0017 -0.0023 -0.0027 108 ILE A CG2 199 C CD1 . ILE A 27 ? 0.1899 0.1693 0.1952 0.0000 -0.0034 0.0001 108 ILE A CD1 200 N N . GLY A 28 ? 0.0858 0.0618 0.0938 -0.0010 -0.0007 -0.0044 109 GLY A N 201 C CA . GLY A 28 ? 0.1321 0.1085 0.1404 -0.0016 -0.0002 -0.0062 109 GLY A CA 202 C C . GLY A 28 ? 0.1428 0.1169 0.1519 -0.0022 0.0010 -0.0071 109 GLY A C 203 O O . GLY A 28 ? 0.1572 0.1316 0.1666 -0.0030 0.0015 -0.0088 109 GLY A O 204 N N . SER A 29 ? 0.1408 0.1125 0.1502 -0.0017 0.0014 -0.0059 110 SER A N 205 C CA . SER A 29 ? 0.1450 0.1140 0.1553 -0.0022 0.0027 -0.0065 110 SER A CA 206 C C . SER A 29 ? 0.1841 0.1536 0.1943 -0.0039 0.0030 -0.0078 110 SER A C 207 O O . SER A 29 ? 0.2254 0.1936 0.2362 -0.0048 0.0040 -0.0093 110 SER A O 208 C CB . SER A 29 ? 0.1957 0.1623 0.2062 -0.0014 0.0030 -0.0047 110 SER A CB 209 O OG . SER A 29 ? 0.2452 0.2088 0.2564 -0.0018 0.0044 -0.0052 110 SER A OG 210 N N . LYS A 30 ? 0.1491 0.1206 0.1587 -0.0043 0.0021 -0.0073 111 LYS A N 211 C CA . LYS A 30 ? 0.1652 0.1378 0.1747 -0.0059 0.0023 -0.0084 111 LYS A CA 212 C C . LYS A 30 ? 0.1890 0.1651 0.1978 -0.0062 0.0013 -0.0090 111 LYS A C 213 O O . LYS A 30 ? 0.1885 0.1662 0.1975 -0.0073 0.0015 -0.0106 111 LYS A O 214 C CB . LYS A 30 ? 0.1649 0.1365 0.1743 -0.0062 0.0023 -0.0073 111 LYS A CB 215 C CG . LYS A 30 ? 0.1639 0.1373 0.1732 -0.0077 0.0023 -0.0083 111 LYS A CG 216 C CD . LYS A 30 ? 0.2193 0.1921 0.2286 -0.0081 0.0024 -0.0072 111 LYS A CD 217 C CE . LYS A 30 ? 0.2026 0.1777 0.2119 -0.0095 0.0023 -0.0083 111 LYS A CE 218 N NZ . LYS A 30 ? 0.3110 0.2858 0.3202 -0.0100 0.0024 -0.0073 111 LYS A NZ 219 N N . GLY A 31 ? 0.0972 0.0746 0.1054 -0.0052 0.0003 -0.0078 112 GLY A N 220 C CA . GLY A 31 ? 0.1279 0.1085 0.1354 -0.0052 -0.0006 -0.0080 112 GLY A CA 221 C C . GLY A 31 ? 0.1327 0.1149 0.1403 -0.0052 -0.0006 -0.0092 112 GLY A C 222 O O . GLY A 31 ? 0.1665 0.1472 0.1745 -0.0049 -0.0001 -0.0098 112 GLY A O 223 N N . ASP A 32 ? 0.1271 0.1122 0.1341 -0.0053 -0.0013 -0.0095 113 ASP A N 224 C CA . ASP A 32 ? 0.1270 0.1140 0.1338 -0.0053 -0.0014 -0.0105 113 ASP A CA 225 C C . ASP A 32 ? 0.1085 0.0958 0.1148 -0.0040 -0.0020 -0.0093 113 ASP A C 226 O O . ASP A 32 ? 0.1128 0.1019 0.1184 -0.0036 -0.0027 -0.0085 113 ASP A O 227 C CB . ASP A 32 ? 0.1419 0.1321 0.1483 -0.0061 -0.0018 -0.0113 113 ASP A CB 228 C CG . ASP A 32 ? 0.1335 0.1239 0.1405 -0.0075 -0.0011 -0.0129 113 ASP A CG 229 O OD1 . ASP A 32 ? 0.1516 0.1394 0.1592 -0.0080 -0.0002 -0.0136 113 ASP A OD1 230 O OD2 . ASP A 32 ? 0.1793 0.1723 0.1861 -0.0082 -0.0014 -0.0133 113 ASP A OD2 231 N N . VAL A 33 ? 0.0747 0.0602 0.0813 -0.0034 -0.0016 -0.0092 114 VAL A N 232 C CA . VAL A 33 ? 0.0603 0.0459 0.0666 -0.0023 -0.0021 -0.0081 114 VAL A CA 233 C C . VAL A 33 ? 0.0622 0.0483 0.0687 -0.0021 -0.0018 -0.0091 114 VAL A C 234 O O . VAL A 33 ? 0.0713 0.0561 0.0784 -0.0023 -0.0010 -0.0101 114 VAL A O 235 C CB . VAL A 33 ? 0.0736 0.0568 0.0803 -0.0016 -0.0020 -0.0068 114 VAL A CB 236 C CG1 . VAL A 33 ? 0.0706 0.0541 0.0770 -0.0006 -0.0024 -0.0058 114 VAL A CG1 237 C CG2 . VAL A 33 ? 0.0988 0.0815 0.1052 -0.0018 -0.0023 -0.0059 114 VAL A CG2 238 N N . PHE A 34 ? 0.0716 0.0597 0.0775 -0.0016 -0.0023 -0.0087 115 PHE A N 239 C CA . PHE A 34 ? 0.0747 0.0637 0.0807 -0.0014 -0.0021 -0.0095 115 PHE A CA 240 C C . PHE A 34 ? 0.1012 0.0881 0.1079 -0.0007 -0.0016 -0.0093 115 PHE A C 241 O O . PHE A 34 ? 0.0643 0.0499 0.0712 0.0000 -0.0018 -0.0080 115 PHE A O 242 C CB . PHE A 34 ? 0.0964 0.0875 0.1017 -0.0009 -0.0027 -0.0088 115 PHE A CB 243 C CG . PHE A 34 ? 0.0943 0.0880 0.0988 -0.0015 -0.0030 -0.0092 115 PHE A CG 244 C CD1 . PHE A 34 ? 0.1418 0.1371 0.1463 -0.0021 -0.0027 -0.0107 115 PHE A CD1 245 C CD2 . PHE A 34 ? 0.1082 0.1029 0.1120 -0.0012 -0.0036 -0.0080 115 PHE A CD2 246 C CE1 . PHE A 34 ? 0.1445 0.1427 0.1484 -0.0025 -0.0030 -0.0110 115 PHE A CE1 247 C CE2 . PHE A 34 ? 0.1058 0.1031 0.1090 -0.0015 -0.0039 -0.0081 115 PHE A CE2 248 C CZ . PHE A 34 ? 0.0736 0.0728 0.0769 -0.0022 -0.0036 -0.0096 115 PHE A CZ 249 N N . VAL A 35 ? 0.1117 0.0986 0.1189 -0.0008 -0.0010 -0.0107 116 VAL A N 250 C CA . VAL A 35 ? 0.0970 0.0827 0.1049 0.0002 -0.0006 -0.0105 116 VAL A CA 251 C C . VAL A 35 ? 0.1202 0.1078 0.1275 0.0007 -0.0012 -0.0097 116 VAL A C 252 O O . VAL A 35 ? 0.1163 0.1061 0.1230 0.0004 -0.0014 -0.0103 116 VAL A O 253 C CB . VAL A 35 ? 0.1231 0.1082 0.1315 -0.0001 0.0004 -0.0122 116 VAL A CB 254 C CG1 . VAL A 35 ? 0.1329 0.1171 0.1421 0.0010 0.0008 -0.0119 116 VAL A CG1 255 C CG2 . VAL A 35 ? 0.1315 0.1146 0.1405 -0.0009 0.0011 -0.0131 116 VAL A CG2 256 N N . ILE A 36 ? 0.0788 0.0657 0.0862 0.0016 -0.0015 -0.0083 117 ILE A N 257 C CA . ILE A 36 ? 0.1185 0.1071 0.1255 0.0020 -0.0020 -0.0076 117 ILE A CA 258 C C . ILE A 36 ? 0.1488 0.1370 0.1565 0.0029 -0.0018 -0.0070 117 ILE A C 259 O O . ILE A 36 ? 0.1813 0.1677 0.1898 0.0034 -0.0015 -0.0068 117 ILE A O 260 C CB . ILE A 36 ? 0.0958 0.0848 0.1020 0.0019 -0.0027 -0.0063 117 ILE A CB 261 C CG1 . ILE A 36 ? 0.1457 0.1331 0.1524 0.0024 -0.0029 -0.0051 117 ILE A CG1 262 C CG2 . ILE A 36 ? 0.1294 0.1190 0.1351 0.0011 -0.0029 -0.0066 117 ILE A CG2 263 C CD1 . ILE A 36 ? 0.2592 0.2471 0.2652 0.0024 -0.0035 -0.0039 117 ILE A CD1 264 N N . ARG A 37 ? 0.0993 0.0892 0.1067 0.0031 -0.0021 -0.0067 118 ARG A N 265 C CA . ARG A 37 ? 0.1249 0.1150 0.1328 0.0039 -0.0021 -0.0060 118 ARG A CA 266 C C . ARG A 37 ? 0.1546 0.1465 0.1618 0.0038 -0.0026 -0.0053 118 ARG A C 267 O O . ARG A 37 ? 0.1530 0.1459 0.1594 0.0032 -0.0029 -0.0054 118 ARG A O 268 C CB . ARG A 37 ? 0.1656 0.1557 0.1744 0.0045 -0.0014 -0.0069 118 ARG A CB 269 C CG . ARG A 37 ? 0.1499 0.1378 0.1597 0.0052 -0.0009 -0.0069 118 ARG A CG 270 C CD . ARG A 37 ? 0.2047 0.1929 0.2155 0.0063 -0.0005 -0.0068 118 ARG A CD 271 N NE . ARG A 37 ? 0.1647 0.1545 0.1754 0.0066 -0.0011 -0.0056 118 ARG A NE 272 C CZ . ARG A 37 ? 0.1582 0.1494 0.1695 0.0073 -0.0010 -0.0055 118 ARG A CZ 273 N NH1 . ARG A 37 ? 0.2107 0.2020 0.2226 0.0078 -0.0003 -0.0065 118 ARG A NH1 274 N NH2 . ARG A 37 ? 0.1111 0.1037 0.1223 0.0075 -0.0016 -0.0044 118 ARG A NH2 275 N N . GLU A 38 ? 0.1886 0.1810 0.1963 0.0043 -0.0028 -0.0045 119 GLU A N 276 C CA . GLU A 38 ? 0.2065 0.2004 0.2136 0.0040 -0.0031 -0.0039 119 GLU A CA 277 C C . GLU A 38 ? 0.1720 0.1656 0.1781 0.0035 -0.0036 -0.0032 119 GLU A C 278 O O . GLU A 38 ? 0.1936 0.1883 0.1990 0.0030 -0.0037 -0.0032 119 GLU A O 279 C CB . GLU A 38 ? 0.1922 0.1879 0.1991 0.0039 -0.0028 -0.0047 119 GLU A CB 280 C CG . GLU A 38 ? 0.2730 0.2693 0.2808 0.0045 -0.0023 -0.0053 119 GLU A CG 281 C CD . GLU A 38 ? 0.3274 0.3227 0.3356 0.0047 -0.0018 -0.0066 119 GLU A CD 282 O OE1 . GLU A 38 ? 0.2988 0.2936 0.3080 0.0054 -0.0013 -0.0069 119 GLU A OE1 283 O OE2 . GLU A 38 ? 0.2582 0.2533 0.2658 0.0041 -0.0017 -0.0072 119 GLU A OE2 284 N N . PRO A 39 ? 0.1678 0.1601 0.1740 0.0035 -0.0039 -0.0026 120 PRO A N 285 C CA . PRO A 39 ? 0.1800 0.1721 0.1854 0.0030 -0.0043 -0.0019 120 PRO A CA 286 C C . PRO A 39 ? 0.2240 0.2169 0.2292 0.0029 -0.0045 -0.0012 120 PRO A C 287 O O . PRO A 39 ? 0.2516 0.2451 0.2573 0.0032 -0.0044 -0.0011 120 PRO A O 288 C CB . PRO A 39 ? 0.2318 0.2224 0.2374 0.0031 -0.0044 -0.0016 120 PRO A CB 289 C CG . PRO A 39 ? 0.1989 0.1892 0.2054 0.0038 -0.0042 -0.0015 120 PRO A CG 290 C CD . PRO A 39 ? 0.1774 0.1685 0.1844 0.0041 -0.0038 -0.0023 120 PRO A CD 291 N N . PHE A 40 ? 0.0769 0.0700 0.0812 0.0024 -0.0046 -0.0008 121 PHE A N 292 C CA . PHE A 40 ? 0.0769 0.0703 0.0809 0.0021 -0.0047 -0.0002 121 PHE A CA 293 C C . PHE A 40 ? 0.1041 0.0967 0.1073 0.0017 -0.0048 0.0004 121 PHE A C 294 O O . PHE A 40 ? 0.1321 0.1244 0.1348 0.0017 -0.0048 0.0003 121 PHE A O 295 C CB . PHE A 40 ? 0.0776 0.0724 0.0817 0.0020 -0.0044 -0.0003 121 PHE A CB 296 C CG . PHE A 40 ? 0.0508 0.0461 0.0541 0.0018 -0.0042 -0.0004 121 PHE A CG 297 C CD1 . PHE A 40 ? 0.0734 0.0684 0.0759 0.0014 -0.0041 0.0002 121 PHE A CD1 298 C CD2 . PHE A 40 ? 0.0998 0.0959 0.1033 0.0020 -0.0040 -0.0011 121 PHE A CD2 299 C CE1 . PHE A 40 ? 0.0647 0.0604 0.0665 0.0013 -0.0038 0.0003 121 PHE A CE1 300 C CE2 . PHE A 40 ? 0.0795 0.0764 0.0822 0.0019 -0.0038 -0.0011 121 PHE A CE2 301 C CZ . PHE A 40 ? 0.0435 0.0404 0.0455 0.0016 -0.0037 -0.0003 121 PHE A CZ 302 N N . ILE A 41 ? 0.0645 0.0569 0.0676 0.0014 -0.0049 0.0008 122 ILE A N 303 C CA . ILE A 41 ? 0.0687 0.0601 0.0709 0.0011 -0.0049 0.0013 122 ILE A CA 304 C C . ILE A 41 ? 0.0762 0.0679 0.0779 0.0006 -0.0045 0.0016 122 ILE A C 305 O O . ILE A 41 ? 0.0658 0.0584 0.0678 0.0004 -0.0044 0.0015 122 ILE A O 306 C CB . ILE A 41 ? 0.0797 0.0705 0.0820 0.0009 -0.0052 0.0015 122 ILE A CB 307 C CG1 . ILE A 41 ? 0.0793 0.0696 0.0821 0.0014 -0.0054 0.0014 122 ILE A CG1 308 C CG2 . ILE A 41 ? 0.0655 0.0554 0.0670 0.0005 -0.0051 0.0019 122 ILE A CG2 309 C CD1 . ILE A 41 ? 0.1536 0.1436 0.1564 0.0014 -0.0057 0.0017 122 ILE A CD1 310 N N . SER A 42 ? 0.1057 0.0967 0.1067 0.0006 -0.0043 0.0019 123 SER A N 311 C CA . SER A 42 ? 0.1301 0.1208 0.1305 0.0002 -0.0039 0.0024 123 SER A CA 312 C C . SER A 42 ? 0.0973 0.0867 0.0970 0.0002 -0.0037 0.0029 123 SER A C 313 O O . SER A 42 ? 0.1086 0.0977 0.1081 0.0006 -0.0039 0.0029 123 SER A O 314 C CB . SER A 42 ? 0.1351 0.1269 0.1353 0.0004 -0.0036 0.0025 123 SER A CB 315 O OG . SER A 42 ? 0.1426 0.1343 0.1424 0.0000 -0.0030 0.0029 123 SER A OG 316 N N . CYS A 43 ? 0.0972 0.0858 0.0966 -0.0003 -0.0032 0.0032 124 CYS A N 317 C CA . CYS A 43 ? 0.1440 0.1310 0.1427 -0.0003 -0.0030 0.0036 124 CYS A CA 318 C C . CYS A 43 ? 0.1567 0.1429 0.1548 -0.0002 -0.0022 0.0043 124 CYS A C 319 O O . CYS A 43 ? 0.1294 0.1160 0.1274 -0.0005 -0.0018 0.0044 124 CYS A O 320 C CB . CYS A 43 ? 0.1488 0.1351 0.1477 -0.0009 -0.0029 0.0032 124 CYS A CB 321 S SG . CYS A 43 ? 0.1968 0.1840 0.1964 -0.0009 -0.0038 0.0027 124 CYS A SG 322 N N . SER A 44 ? 0.1977 0.1829 0.1952 0.0003 -0.0020 0.0047 125 SER A N 323 C CA . SER A 44 ? 0.2126 0.1967 0.2095 0.0005 -0.0012 0.0056 125 SER A CA 324 C C . SER A 44 ? 0.2141 0.1962 0.2108 0.0000 -0.0007 0.0055 125 SER A C 325 O O . SER A 44 ? 0.2244 0.2065 0.2214 -0.0005 -0.0010 0.0048 125 SER A O 326 C CB . SER A 44 ? 0.2275 0.2122 0.2241 0.0015 -0.0013 0.0062 125 SER A CB 327 O OG . SER A 44 ? 0.2582 0.2423 0.2548 0.0018 -0.0016 0.0061 125 SER A OG 328 N N . PRO A 45 ? 0.2107 0.1913 0.2069 0.0002 0.0002 0.0062 126 PRO A N 329 C CA . PRO A 45 ? 0.2086 0.1872 0.2046 -0.0002 0.0008 0.0060 126 PRO A CA 330 C C . PRO A 45 ? 0.2143 0.1927 0.2103 0.0004 0.0004 0.0059 126 PRO A C 331 O O . PRO A 45 ? 0.2545 0.2315 0.2503 0.0000 0.0008 0.0056 126 PRO A O 332 C CB . PRO A 45 ? 0.2817 0.2585 0.2771 0.0001 0.0020 0.0070 126 PRO A CB 333 C CG . PRO A 45 ? 0.2309 0.2090 0.2262 0.0002 0.0020 0.0075 126 PRO A CG 334 C CD . PRO A 45 ? 0.2029 0.1834 0.1987 0.0007 0.0009 0.0072 126 PRO A CD 335 N N . LEU A 46 ? 0.2853 0.2652 0.2814 0.0011 -0.0003 0.0061 127 LEU A N 336 C CA . LEU A 46 ? 0.3197 0.2997 0.3158 0.0017 -0.0007 0.0060 127 LEU A CA 337 C C . LEU A 46 ? 0.3279 0.3093 0.3246 0.0015 -0.0017 0.0053 127 LEU A C 338 O O . LEU A 46 ? 0.3094 0.2905 0.3061 0.0014 -0.0019 0.0050 127 LEU A O 339 C CB . LEU A 46 ? 0.3128 0.2934 0.3087 0.0028 -0.0006 0.0069 127 LEU A CB 340 C CG . LEU A 46 ? 0.4028 0.3817 0.3981 0.0034 0.0005 0.0079 127 LEU A CG 341 C CD1 . LEU A 46 ? 0.4283 0.4085 0.4234 0.0046 0.0005 0.0089 127 LEU A CD1 342 C CD2 . LEU A 46 ? 0.3868 0.3636 0.3819 0.0032 0.0011 0.0077 127 LEU A CD2 343 N N . GLU A 47 ? 0.2298 0.2126 0.2268 0.0014 -0.0022 0.0051 128 GLU A N 344 C CA . GLU A 47 ? 0.2414 0.2254 0.2390 0.0013 -0.0030 0.0045 128 GLU A CA 345 C C . GLU A 47 ? 0.2146 0.1995 0.2125 0.0009 -0.0033 0.0040 128 GLU A C 346 O O . GLU A 47 ? 0.2002 0.1854 0.1981 0.0007 -0.0030 0.0042 128 GLU A O 347 C CB . GLU A 47 ? 0.2750 0.2599 0.2725 0.0020 -0.0033 0.0046 128 GLU A CB 348 C CG . GLU A 47 ? 0.3136 0.2999 0.3111 0.0023 -0.0033 0.0049 128 GLU A CG 349 C CD . GLU A 47 ? 0.4315 0.4193 0.4292 0.0028 -0.0037 0.0048 128 GLU A CD 350 O OE1 . GLU A 47 ? 0.5100 0.4976 0.5079 0.0028 -0.0040 0.0046 128 GLU A OE1 351 O OE2 . GLU A 47 ? 0.3587 0.3479 0.3563 0.0031 -0.0037 0.0049 128 GLU A OE2 352 N N . CYS A 48 ? 0.1207 0.1063 0.1192 0.0008 -0.0039 0.0036 129 CYS A N 353 C CA . CYS A 48 ? 0.1453 0.1319 0.1444 0.0007 -0.0042 0.0032 129 CYS A CA 354 C C . CYS A 48 ? 0.1134 0.1009 0.1128 0.0011 -0.0046 0.0029 129 CYS A C 355 O O . CYS A 48 ? 0.1374 0.1247 0.1368 0.0012 -0.0048 0.0028 129 CYS A O 356 C CB . CYS A 48 ? 0.2153 0.2018 0.2147 0.0002 -0.0045 0.0028 129 CYS A CB 357 S SG . CYS A 48 ? 0.2617 0.2477 0.2608 -0.0006 -0.0040 0.0028 129 CYS A SG 358 N N . ARG A 49 ? 0.1030 0.0915 0.1026 0.0012 -0.0046 0.0027 130 ARG A N 359 C CA . ARG A 49 ? 0.0968 0.0861 0.0967 0.0014 -0.0048 0.0022 130 ARG A CA 360 C C . ARG A 49 ? 0.1018 0.0917 0.1025 0.0014 -0.0050 0.0017 130 ARG A C 361 O O . ARG A 49 ? 0.1168 0.1070 0.1177 0.0012 -0.0048 0.0017 130 ARG A O 362 C CB . ARG A 49 ? 0.1115 0.1019 0.1110 0.0017 -0.0046 0.0024 130 ARG A CB 363 C CG . ARG A 49 ? 0.1454 0.1354 0.1442 0.0020 -0.0044 0.0031 130 ARG A CG 364 C CD . ARG A 49 ? 0.1803 0.1717 0.1788 0.0024 -0.0042 0.0034 130 ARG A CD 365 N NE . ARG A 49 ? 0.1586 0.1515 0.1574 0.0024 -0.0046 0.0027 130 ARG A NE 366 C CZ . ARG A 49 ? 0.1537 0.1470 0.1526 0.0025 -0.0048 0.0026 130 ARG A CZ 367 N NH1 . ARG A 49 ? 0.2140 0.2063 0.2126 0.0027 -0.0047 0.0031 130 ARG A NH1 368 N NH2 . ARG A 49 ? 0.1329 0.1275 0.1320 0.0023 -0.0050 0.0018 130 ARG A NH2 369 N N . THR A 50 ? 0.0957 0.0858 0.0968 0.0015 -0.0051 0.0012 131 THR A N 370 C CA . THR A 50 ? 0.1322 0.1227 0.1340 0.0016 -0.0051 0.0006 131 THR A CA 371 C C . THR A 50 ? 0.1008 0.0924 0.1025 0.0017 -0.0050 0.0000 131 THR A C 372 O O . THR A 50 ? 0.0826 0.0747 0.0842 0.0016 -0.0050 -0.0003 131 THR A O 373 C CB . THR A 50 ? 0.1636 0.1532 0.1660 0.0017 -0.0053 0.0003 131 THR A CB 374 O OG1 . THR A 50 ? 0.2426 0.2314 0.2450 0.0016 -0.0054 0.0008 131 THR A OG1 375 C CG2 . THR A 50 ? 0.1704 0.1602 0.1735 0.0019 -0.0051 -0.0003 131 THR A CG2 376 N N . PHE A 51 ? 0.0677 0.0602 0.0696 0.0017 -0.0048 -0.0001 132 PHE A N 377 C CA . PHE A 51 ? 0.0690 0.0628 0.0709 0.0018 -0.0046 -0.0008 132 PHE A CA 378 C C . PHE A 51 ? 0.0951 0.0888 0.0978 0.0019 -0.0045 -0.0016 132 PHE A C 379 O O . PHE A 51 ? 0.1023 0.0951 0.1056 0.0021 -0.0045 -0.0015 132 PHE A O 380 C CB . PHE A 51 ? 0.0644 0.0592 0.0659 0.0017 -0.0043 -0.0004 132 PHE A CB 381 C CG . PHE A 51 ? 0.0638 0.0586 0.0644 0.0017 -0.0043 0.0005 132 PHE A CG 382 C CD1 . PHE A 51 ? 0.0862 0.0798 0.0866 0.0015 -0.0043 0.0012 132 PHE A CD1 383 C CD2 . PHE A 51 ? 0.0768 0.0729 0.0768 0.0018 -0.0041 0.0006 132 PHE A CD2 384 C CE1 . PHE A 51 ? 0.1300 0.1233 0.1297 0.0016 -0.0040 0.0020 132 PHE A CE1 385 C CE2 . PHE A 51 ? 0.1236 0.1197 0.1229 0.0019 -0.0040 0.0015 132 PHE A CE2 386 C CZ . PHE A 51 ? 0.1044 0.0989 0.1035 0.0018 -0.0039 0.0023 132 PHE A CZ 387 N N . PHE A 52 ? 0.0734 0.0679 0.0762 0.0018 -0.0043 -0.0025 133 PHE A N 388 C CA . PHE A 52 ? 0.0869 0.0810 0.0905 0.0020 -0.0040 -0.0035 133 PHE A CA 389 C C . PHE A 52 ? 0.1039 0.0995 0.1074 0.0018 -0.0037 -0.0046 133 PHE A C 390 O O . PHE A 52 ? 0.0808 0.0777 0.0836 0.0015 -0.0038 -0.0047 133 PHE A O 391 C CB . PHE A 52 ? 0.0591 0.0517 0.0632 0.0019 -0.0041 -0.0036 133 PHE A CB 392 C CG . PHE A 52 ? 0.1049 0.0977 0.1085 0.0015 -0.0042 -0.0037 133 PHE A CG 393 C CD1 . PHE A 52 ? 0.1284 0.1208 0.1314 0.0014 -0.0046 -0.0028 133 PHE A CD1 394 C CD2 . PHE A 52 ? 0.1135 0.1071 0.1171 0.0011 -0.0040 -0.0049 133 PHE A CD2 395 C CE1 . PHE A 52 ? 0.0893 0.0821 0.0920 0.0011 -0.0047 -0.0029 133 PHE A CE1 396 C CE2 . PHE A 52 ? 0.1522 0.1463 0.1554 0.0007 -0.0042 -0.0050 133 PHE A CE2 397 C CZ . PHE A 52 ? 0.1384 0.1322 0.1411 0.0008 -0.0045 -0.0039 133 PHE A CZ 398 N N . LEU A 53 ? 0.0604 0.0559 0.0647 0.0020 -0.0033 -0.0054 134 LEU A N 399 C CA . LEU A 53 ? 0.0738 0.0706 0.0781 0.0018 -0.0030 -0.0068 134 LEU A CA 400 C C . LEU A 53 ? 0.1077 0.1033 0.1125 0.0015 -0.0027 -0.0078 134 LEU A C 401 O O . LEU A 53 ? 0.0969 0.0908 0.1026 0.0018 -0.0024 -0.0080 134 LEU A O 402 C CB . LEU A 53 ? 0.0909 0.0884 0.0957 0.0022 -0.0026 -0.0072 134 LEU A CB 403 C CG . LEU A 53 ? 0.0937 0.0926 0.0980 0.0023 -0.0027 -0.0064 134 LEU A CG 404 C CD1 . LEU A 53 ? 0.1306 0.1304 0.1355 0.0026 -0.0023 -0.0070 134 LEU A CD1 405 C CD2 . LEU A 53 ? 0.0738 0.0744 0.0769 0.0019 -0.0028 -0.0062 134 LEU A CD2 406 N N . THR A 54 ? 0.1227 0.1193 0.1270 0.0009 -0.0027 -0.0085 135 THR A N 407 C CA . THR A 54 ? 0.1329 0.1286 0.1377 0.0004 -0.0024 -0.0097 135 THR A CA 408 C C . THR A 54 ? 0.1756 0.1718 0.1807 0.0002 -0.0017 -0.0113 135 THR A C 409 O O . THR A 54 ? 0.1884 0.1862 0.1933 0.0005 -0.0016 -0.0115 135 THR A O 410 C CB . THR A 54 ? 0.1341 0.1312 0.1382 -0.0003 -0.0026 -0.0100 135 THR A CB 411 O OG1 . THR A 54 ? 0.1884 0.1883 0.1919 -0.0006 -0.0026 -0.0107 135 THR A OG1 412 C CG2 . THR A 54 ? 0.1639 0.1609 0.1675 -0.0001 -0.0033 -0.0084 135 THR A CG2 413 N N . GLN A 55 ? 0.1550 0.1499 0.1608 -0.0002 -0.0011 -0.0126 136 GLN A N 414 C CA . GLN A 55 ? 0.1840 0.1793 0.1902 -0.0005 -0.0004 -0.0144 136 GLN A CA 415 C C . GLN A 55 ? 0.1857 0.1827 0.1914 -0.0017 -0.0003 -0.0158 136 GLN A C 416 O O . GLN A 55 ? 0.2160 0.2132 0.2220 -0.0023 0.0004 -0.0176 136 GLN A O 417 C CB . GLN A 55 ? 0.1799 0.1723 0.1873 -0.0002 0.0004 -0.0149 136 GLN A CB 418 C CG . GLN A 55 ? 0.1922 0.1832 0.2001 0.0010 0.0004 -0.0137 136 GLN A CG 419 C CD . GLN A 55 ? 0.2947 0.2871 0.3028 0.0014 0.0008 -0.0144 136 GLN A CD 420 O OE1 . GLN A 55 ? 0.2305 0.2249 0.2381 0.0009 0.0010 -0.0157 136 GLN A OE1 421 N NE2 . GLN A 55 ? 0.2422 0.2338 0.2510 0.0025 0.0009 -0.0135 136 GLN A NE2 422 N N . GLY A 56 ? 0.1079 0.1063 0.1129 -0.0020 -0.0010 -0.0149 137 GLY A N 423 C CA . GLY A 56 ? 0.1191 0.1195 0.1237 -0.0030 -0.0011 -0.0161 137 GLY A CA 424 C C . GLY A 56 ? 0.1470 0.1455 0.1524 -0.0038 -0.0005 -0.0173 137 GLY A C 425 O O . GLY A 56 ? 0.1160 0.1158 0.1213 -0.0049 -0.0001 -0.0190 137 GLY A O 426 N N . ALA A 57 ? 0.0466 0.0420 0.0526 -0.0034 -0.0004 -0.0164 138 ALA A N 427 C CA . ALA A 57 ? 0.1371 0.1301 0.1439 -0.0041 0.0003 -0.0173 138 ALA A CA 428 C C . ALA A 57 ? 0.0912 0.0818 0.0982 -0.0037 0.0001 -0.0156 138 ALA A C 429 O O . ALA A 57 ? 0.0761 0.0665 0.0828 -0.0027 -0.0005 -0.0139 138 ALA A O 430 C CB . ALA A 57 ? 0.1031 0.0941 0.1107 -0.0040 0.0014 -0.0186 138 ALA A CB 431 N N . LEU A 58 ? 0.0843 0.0732 0.0918 -0.0045 0.0006 -0.0162 139 LEU A N 432 C CA . LEU A 58 ? 0.0868 0.0736 0.0945 -0.0042 0.0004 -0.0147 139 LEU A CA 433 C C . LEU A 58 ? 0.1047 0.0880 0.1133 -0.0038 0.0013 -0.0146 139 LEU A C 434 O O . LEU A 58 ? 0.1059 0.0880 0.1151 -0.0042 0.0022 -0.0161 139 LEU A O 435 C CB . LEU A 58 ? 0.0761 0.0638 0.0837 -0.0053 0.0002 -0.0150 139 LEU A CB 436 C CG . LEU A 58 ? 0.0631 0.0545 0.0698 -0.0056 -0.0006 -0.0150 139 LEU A CG 437 C CD1 . LEU A 58 ? 0.1179 0.1101 0.1246 -0.0066 -0.0007 -0.0152 139 LEU A CD1 438 C CD2 . LEU A 58 ? 0.0655 0.0575 0.0715 -0.0044 -0.0015 -0.0130 139 LEU A CD2 439 N N . LEU A 59 ? 0.1120 0.0935 0.1207 -0.0030 0.0010 -0.0129 140 LEU A N 440 C CA . LEU A 59 ? 0.1230 0.1012 0.1326 -0.0025 0.0018 -0.0124 140 LEU A CA 441 C C . LEU A 59 ? 0.1352 0.1116 0.1453 -0.0037 0.0028 -0.0136 140 LEU A C 442 O O . LEU A 59 ? 0.1249 0.1024 0.1347 -0.0048 0.0026 -0.0140 140 LEU A O 443 C CB . LEU A 59 ? 0.1180 0.0952 0.1275 -0.0016 0.0013 -0.0103 140 LEU A CB 444 C CG . LEU A 59 ? 0.1474 0.1256 0.1566 -0.0003 0.0006 -0.0090 140 LEU A CG 445 C CD1 . LEU A 59 ? 0.1627 0.1405 0.1716 0.0002 -0.0001 -0.0071 140 LEU A CD1 446 C CD2 . LEU A 59 ? 0.1484 0.1250 0.1584 0.0006 0.0013 -0.0092 140 LEU A CD2 447 N N . ASN A 60 ? 0.1147 0.0883 0.1257 -0.0034 0.0040 -0.0142 141 ASN A N 448 C CA . ASN A 60 ? 0.1326 0.1039 0.1442 -0.0046 0.0051 -0.0153 141 ASN A CA 449 C C . ASN A 60 ? 0.1423 0.1152 0.1538 -0.0062 0.0055 -0.0177 141 ASN A C 450 O O . ASN A 60 ? 0.2028 0.1748 0.2147 -0.0076 0.0062 -0.0188 141 ASN A O 451 C CB . ASN A 60 ? 0.1499 0.1201 0.1614 -0.0049 0.0049 -0.0139 141 ASN A CB 452 C CG . ASN A 60 ? 0.1998 0.1659 0.2121 -0.0046 0.0062 -0.0134 141 ASN A CG 453 O OD1 . ASN A 60 ? 0.1602 0.1242 0.1732 -0.0042 0.0072 -0.0141 141 ASN A OD1 454 N ND2 . ASN A 60 ? 0.2183 0.1834 0.2305 -0.0048 0.0061 -0.0121 141 ASN A ND2 455 N N . ASP A 61 ? 0.1378 0.1135 0.1488 -0.0062 0.0050 -0.0186 142 ASP A N 456 C CA . ASP A 61 ? 0.1579 0.1356 0.1689 -0.0076 0.0054 -0.0210 142 ASP A CA 457 C C . ASP A 61 ? 0.1383 0.1156 0.1497 -0.0072 0.0062 -0.0224 142 ASP A C 458 O O . ASP A 61 ? 0.1311 0.1078 0.1426 -0.0057 0.0060 -0.0213 142 ASP A O 459 C CB . ASP A 61 ? 0.1352 0.1172 0.1452 -0.0080 0.0042 -0.0210 142 ASP A CB 460 C CG . ASP A 61 ? 0.1559 0.1406 0.1657 -0.0094 0.0045 -0.0235 142 ASP A CG 461 O OD1 . ASP A 61 ? 0.1680 0.1529 0.1780 -0.0110 0.0050 -0.0248 142 ASP A OD1 462 O OD2 . ASP A 61 ? 0.1495 0.1362 0.1589 -0.0090 0.0042 -0.0241 142 ASP A OD2 463 N N . LYS A 62 ? 0.1398 0.1174 0.1514 -0.0086 0.0071 -0.0249 143 LYS A N 464 C CA . LYS A 62 ? 0.1386 0.1155 0.1506 -0.0083 0.0080 -0.0264 143 LYS A CA 465 C C . LYS A 62 ? 0.1316 0.1116 0.1430 -0.0073 0.0072 -0.0261 143 LYS A C 466 O O . LYS A 62 ? 0.1490 0.1281 0.1608 -0.0064 0.0078 -0.0265 143 LYS A O 467 C CB . LYS A 62 ? 0.1698 0.1469 0.1821 -0.0102 0.0092 -0.0294 143 LYS A CB 468 C CG . LYS A 62 ? 0.1521 0.1340 0.1635 -0.0115 0.0084 -0.0307 143 LYS A CG 469 C CD . LYS A 62 ? 0.2057 0.1878 0.2175 -0.0135 0.0096 -0.0339 143 LYS A CD 470 C CE . LYS A 62 ? 0.2022 0.1896 0.2131 -0.0147 0.0088 -0.0352 143 LYS A CE 471 N NZ . LYS A 62 ? 0.2281 0.2161 0.2393 -0.0167 0.0100 -0.0385 143 LYS A NZ 472 N N . HIS A 63 ? 0.1064 0.0899 0.1168 -0.0075 0.0058 -0.0254 144 HIS A N 473 C CA . HIS A 63 ? 0.1243 0.1108 0.1340 -0.0067 0.0051 -0.0250 144 HIS A CA 474 C C . HIS A 63 ? 0.1020 0.0873 0.1118 -0.0049 0.0046 -0.0228 144 HIS A C 475 O O . HIS A 63 ? 0.0962 0.0836 0.1056 -0.0041 0.0041 -0.0225 144 HIS A O 476 C CB . HIS A 63 ? 0.0917 0.0823 0.1003 -0.0073 0.0039 -0.0248 144 HIS A CB 477 C CG . HIS A 63 ? 0.1085 0.1015 0.1169 -0.0090 0.0043 -0.0272 144 HIS A CG 478 N ND1 . HIS A 63 ? 0.1068 0.0997 0.1154 -0.0104 0.0045 -0.0279 144 HIS A ND1 479 C CD2 . HIS A 63 ? 0.1054 0.1012 0.1135 -0.0097 0.0045 -0.0291 144 HIS A CD2 480 C CE1 . HIS A 63 ? 0.1227 0.1183 0.1311 -0.0118 0.0048 -0.0302 144 HIS A CE1 481 N NE2 . HIS A 63 ? 0.1240 0.1214 0.1320 -0.0114 0.0048 -0.0309 144 HIS A NE2 482 N N . SER A 64 ? 0.1298 0.1121 0.1402 -0.0042 0.0048 -0.0214 145 SER A N 483 C CA . SER A 64 ? 0.1518 0.1329 0.1624 -0.0025 0.0044 -0.0194 145 SER A CA 484 C C . SER A 64 ? 0.1590 0.1382 0.1705 -0.0017 0.0055 -0.0201 145 SER A C 485 O O . SER A 64 ? 0.1423 0.1207 0.1541 -0.0003 0.0054 -0.0187 145 SER A O 486 C CB . SER A 64 ? 0.1163 0.0952 0.1272 -0.0021 0.0042 -0.0176 145 SER A CB 487 O OG . SER A 64 ? 0.1430 0.1186 0.1546 -0.0025 0.0053 -0.0181 145 SER A OG 488 N N . ASN A 65 ? 0.1038 0.0822 0.1157 -0.0026 0.0066 -0.0224 146 ASN A N 489 C CA . ASN A 65 ? 0.1688 0.1453 0.1816 -0.0018 0.0079 -0.0233 146 ASN A CA 490 C C . ASN A 65 ? 0.2220 0.2009 0.2346 -0.0008 0.0075 -0.0232 146 ASN A C 491 O O . ASN A 65 ? 0.2205 0.2026 0.2322 -0.0015 0.0069 -0.0240 146 ASN A O 492 C CB . ASN A 65 ? 0.1756 0.1513 0.1888 -0.0033 0.0092 -0.0261 146 ASN A CB 493 C CG . ASN A 65 ? 0.2337 0.2055 0.2480 -0.0026 0.0109 -0.0269 146 ASN A CG 494 O OD1 . ASN A 65 ? 0.1641 0.1346 0.1791 -0.0009 0.0110 -0.0256 146 ASN A OD1 495 N ND2 . ASN A 65 ? 0.2672 0.2372 0.2820 -0.0040 0.0122 -0.0290 146 ASN A ND2 496 N N . GLY A 66 ? 0.2535 0.2307 0.2668 0.0008 0.0079 -0.0222 147 GLY A N 497 C CA . GLY A 66 ? 0.2745 0.2538 0.2879 0.0017 0.0077 -0.0221 147 GLY A CA 498 C C . GLY A 66 ? 0.3022 0.2844 0.3148 0.0021 0.0062 -0.0204 147 GLY A C 499 O O . GLY A 66 ? 0.2418 0.2264 0.2540 0.0025 0.0059 -0.0206 147 GLY A O 500 N N . THR A 67 ? 0.1733 0.1551 0.1854 0.0021 0.0053 -0.0187 148 THR A N 501 C CA . THR A 67 ? 0.2181 0.2023 0.2294 0.0023 0.0040 -0.0171 148 THR A CA 502 C C . THR A 67 ? 0.2298 0.2141 0.2416 0.0038 0.0037 -0.0155 148 THR A C 503 O O . THR A 67 ? 0.2499 0.2356 0.2612 0.0040 0.0027 -0.0140 148 THR A O 504 C CB . THR A 67 ? 0.1831 0.1671 0.1938 0.0017 0.0032 -0.0159 148 THR A CB 505 O OG1 . THR A 67 ? 0.1504 0.1312 0.1618 0.0019 0.0037 -0.0153 148 THR A OG1 506 C CG2 . THR A 67 ? 0.2007 0.1863 0.2107 0.0002 0.0030 -0.0172 148 THR A CG2 507 N N . ILE A 68 ? 0.2320 0.2148 0.2449 0.0048 0.0047 -0.0159 149 ILE A N 508 C CA . ILE A 68 ? 0.2344 0.2179 0.2478 0.0062 0.0045 -0.0147 149 ILE A CA 509 C C . ILE A 68 ? 0.2991 0.2857 0.3120 0.0061 0.0042 -0.0152 149 ILE A C 510 O O . ILE A 68 ? 0.3485 0.3367 0.3616 0.0069 0.0037 -0.0142 149 ILE A O 511 C CB . ILE A 68 ? 0.2890 0.2702 0.3038 0.0074 0.0057 -0.0149 149 ILE A CB 512 C CG1 . ILE A 68 ? 0.3279 0.3100 0.3433 0.0090 0.0054 -0.0133 149 ILE A CG1 513 C CG2 . ILE A 68 ? 0.2847 0.2657 0.2998 0.0071 0.0068 -0.0172 149 ILE A CG2 514 C CD1 . ILE A 68 ? 0.3579 0.3379 0.3747 0.0105 0.0065 -0.0132 149 ILE A CD1 515 N N . LYS A 69 ? 0.3281 0.3160 0.3405 0.0050 0.0044 -0.0170 150 LYS A N 516 C CA . LYS A 69 ? 0.3371 0.3281 0.3489 0.0047 0.0042 -0.0176 150 LYS A CA 517 C C . LYS A 69 ? 0.3681 0.3612 0.3787 0.0044 0.0030 -0.0161 150 LYS A C 518 O O . LYS A 69 ? 0.3195 0.3124 0.3296 0.0037 0.0023 -0.0155 150 LYS A O 519 C CB . LYS A 69 ? 0.3847 0.3766 0.3960 0.0036 0.0048 -0.0198 150 LYS A CB 520 C CG . LYS A 69 ? 0.3936 0.3887 0.4042 0.0033 0.0047 -0.0207 150 LYS A CG 521 C CD . LYS A 69 ? 0.4587 0.4548 0.4688 0.0021 0.0053 -0.0229 150 LYS A CD 522 C CE . LYS A 69 ? 0.5277 0.5274 0.5370 0.0018 0.0051 -0.0236 150 LYS A CE 523 N NZ . LYS A 69 ? 0.5025 0.5044 0.5105 0.0004 0.0048 -0.0246 150 LYS A NZ 524 N N . ASP A 70 ? 0.2731 0.2684 0.2837 0.0049 0.0027 -0.0156 151 ASP A N 525 C CA . ASP A 70 ? 0.3036 0.3005 0.3133 0.0047 0.0017 -0.0140 151 ASP A CA 526 C C . ASP A 70 ? 0.2752 0.2745 0.2837 0.0037 0.0014 -0.0145 151 ASP A C 527 O O . ASP A 70 ? 0.2281 0.2278 0.2357 0.0032 0.0006 -0.0134 151 ASP A O 528 C CB . ASP A 70 ? 0.3519 0.3502 0.3621 0.0055 0.0017 -0.0132 151 ASP A CB 529 C CG . ASP A 70 ? 0.4178 0.4143 0.4291 0.0066 0.0017 -0.0122 151 ASP A CG 530 O OD1 . ASP A 70 ? 0.3301 0.3249 0.3414 0.0065 0.0013 -0.0113 151 ASP A OD1 531 O OD2 . ASP A 70 ? 0.4552 0.4524 0.4674 0.0075 0.0021 -0.0122 151 ASP A OD2 532 N N . ARG A 71 ? 0.1812 0.1820 0.1895 0.0033 0.0019 -0.0161 152 ARG A N 533 C CA . ARG A 71 ? 0.1566 0.1601 0.1636 0.0025 0.0016 -0.0164 152 ARG A CA 534 C C . ARG A 71 ? 0.2295 0.2334 0.2361 0.0016 0.0020 -0.0182 152 ARG A C 535 O O . ARG A 71 ? 0.2293 0.2322 0.2366 0.0016 0.0028 -0.0199 152 ARG A O 536 C CB . ARG A 71 ? 0.2140 0.2199 0.2208 0.0028 0.0018 -0.0163 152 ARG A CB 537 C CG . ARG A 71 ? 0.1316 0.1373 0.1388 0.0036 0.0014 -0.0147 152 ARG A CG 538 C CD . ARG A 71 ? 0.1461 0.1544 0.1532 0.0037 0.0017 -0.0147 152 ARG A CD 539 N NE . ARG A 71 ? 0.1588 0.1674 0.1666 0.0041 0.0026 -0.0164 152 ARG A NE 540 C CZ . ARG A 71 ? 0.2324 0.2397 0.2415 0.0050 0.0031 -0.0165 152 ARG A CZ 541 N NH1 . ARG A 71 ? 0.1958 0.2016 0.2056 0.0056 0.0027 -0.0151 152 ARG A NH1 542 N NH2 . ARG A 71 ? 0.1949 0.2026 0.2047 0.0054 0.0040 -0.0181 152 ARG A NH2 543 N N . SER A 72 ? 0.1346 0.1402 0.1401 0.0009 0.0014 -0.0180 153 SER A N 544 C CA . SER A 72 ? 0.1321 0.1390 0.1372 -0.0001 0.0017 -0.0197 153 SER A CA 545 C C . SER A 72 ? 0.1236 0.1331 0.1274 -0.0006 0.0009 -0.0189 153 SER A C 546 O O . SER A 72 ? 0.0985 0.1078 0.1019 -0.0002 0.0002 -0.0170 153 SER A O 547 C CB . SER A 72 ? 0.1514 0.1555 0.1572 -0.0005 0.0020 -0.0206 153 SER A CB 548 O OG . SER A 72 ? 0.1601 0.1637 0.1655 -0.0008 0.0012 -0.0193 153 SER A OG 549 N N . PRO A 73 ? 0.1170 0.1289 0.1201 -0.0015 0.0010 -0.0203 154 PRO A N 550 C CA . PRO A 73 ? 0.1031 0.1178 0.1050 -0.0018 0.0003 -0.0195 154 PRO A CA 551 C C . PRO A 73 ? 0.1053 0.1187 0.1072 -0.0021 -0.0003 -0.0187 154 PRO A C 552 O O . PRO A 73 ? 0.1146 0.1301 0.1156 -0.0022 -0.0009 -0.0178 154 PRO A O 553 C CB . PRO A 73 ? 0.1199 0.1376 0.1212 -0.0027 0.0007 -0.0216 154 PRO A CB 554 C CG . PRO A 73 ? 0.1412 0.1568 0.1436 -0.0031 0.0016 -0.0237 154 PRO A CG 555 C CD . PRO A 73 ? 0.1357 0.1481 0.1391 -0.0021 0.0019 -0.0229 154 PRO A CD 556 N N . TYR A 74 ? 0.0846 0.0947 0.0875 -0.0021 0.0000 -0.0189 155 TYR A N 557 C CA . TYR A 74 ? 0.1089 0.1179 0.1119 -0.0024 -0.0004 -0.0183 155 TYR A CA 558 C C . TYR A 74 ? 0.1252 0.1322 0.1282 -0.0016 -0.0010 -0.0161 155 TYR A C 559 O O . TYR A 74 ? 0.1169 0.1235 0.1197 -0.0018 -0.0015 -0.0152 155 TYR A O 560 C CB . TYR A 74 ? 0.1275 0.1341 0.1314 -0.0031 0.0002 -0.0200 155 TYR A CB 561 C CG . TYR A 74 ? 0.1418 0.1497 0.1459 -0.0039 0.0010 -0.0224 155 TYR A CG 562 C CD1 . TYR A 74 ? 0.1139 0.1254 0.1171 -0.0048 0.0008 -0.0235 155 TYR A CD1 563 C CD2 . TYR A 74 ? 0.1887 0.1945 0.1937 -0.0037 0.0020 -0.0237 155 TYR A CD2 564 C CE1 . TYR A 74 ? 0.1364 0.1494 0.1397 -0.0057 0.0016 -0.0260 155 TYR A CE1 565 C CE2 . TYR A 74 ? 0.1774 0.1843 0.1825 -0.0045 0.0028 -0.0261 155 TYR A CE2 566 C CZ . TYR A 74 ? 0.1901 0.2006 0.1942 -0.0055 0.0026 -0.0273 155 TYR A CZ 567 O OH . TYR A 74 ? 0.2000 0.2118 0.2042 -0.0065 0.0034 -0.0299 155 TYR A OH 568 N N . ARG A 75 ? 0.0875 0.0935 0.0909 -0.0008 -0.0009 -0.0152 156 ARG A N 569 C CA . ARG A 75 ? 0.1178 0.1220 0.1213 -0.0002 -0.0014 -0.0133 156 ARG A CA 570 C C . ARG A 75 ? 0.0758 0.0816 0.0782 -0.0001 -0.0020 -0.0118 156 ARG A C 571 O O . ARG A 75 ? 0.0850 0.0933 0.0867 -0.0001 -0.0020 -0.0117 156 ARG A O 572 C CB . ARG A 75 ? 0.1243 0.1272 0.1284 0.0006 -0.0011 -0.0129 156 ARG A CB 573 C CG . ARG A 75 ? 0.1670 0.1680 0.1723 0.0007 -0.0004 -0.0142 156 ARG A CG 574 C CD . ARG A 75 ? 0.1704 0.1698 0.1765 0.0016 -0.0003 -0.0132 156 ARG A CD 575 N NE . ARG A 75 ? 0.1619 0.1593 0.1682 0.0019 -0.0008 -0.0118 156 ARG A NE 576 C CZ . ARG A 75 ? 0.2187 0.2148 0.2257 0.0026 -0.0008 -0.0108 156 ARG A CZ 577 N NH1 . ARG A 75 ? 0.1754 0.1719 0.1830 0.0032 -0.0004 -0.0110 156 ARG A NH1 578 N NH2 . ARG A 75 ? 0.2146 0.2091 0.2216 0.0027 -0.0012 -0.0096 156 ARG A NH2 579 N N . THR A 76 ? 0.0879 0.0924 0.0903 0.0001 -0.0025 -0.0105 157 THR A N 580 C CA . THR A 76 ? 0.0763 0.0819 0.0777 0.0003 -0.0030 -0.0090 157 THR A CA 581 C C . THR A 76 ? 0.1117 0.1152 0.1134 0.0007 -0.0033 -0.0075 157 THR A C 582 O O . THR A 76 ? 0.1194 0.1207 0.1218 0.0007 -0.0032 -0.0075 157 THR A O 583 C CB . THR A 76 ? 0.1431 0.1502 0.1441 -0.0002 -0.0033 -0.0092 157 THR A CB 584 O OG1 . THR A 76 ? 0.1580 0.1630 0.1595 -0.0004 -0.0033 -0.0094 157 THR A OG1 585 C CG2 . THR A 76 ? 0.1114 0.1212 0.1120 -0.0007 -0.0030 -0.0107 157 THR A CG2 586 N N . LEU A 77 ? 0.0822 0.0862 0.0831 0.0010 -0.0034 -0.0061 158 LEU A N 587 C CA . LEU A 77 ? 0.0749 0.0771 0.0759 0.0013 -0.0037 -0.0047 158 LEU A CA 588 C C . LEU A 77 ? 0.0869 0.0889 0.0875 0.0013 -0.0040 -0.0041 158 LEU A C 589 O O . LEU A 77 ? 0.0854 0.0891 0.0852 0.0013 -0.0041 -0.0038 158 LEU A O 590 C CB . LEU A 77 ? 0.0830 0.0858 0.0835 0.0016 -0.0036 -0.0037 158 LEU A CB 591 C CG . LEU A 77 ? 0.0768 0.0779 0.0772 0.0017 -0.0037 -0.0024 158 LEU A CG 592 C CD1 . LEU A 77 ? 0.0668 0.0662 0.0682 0.0018 -0.0037 -0.0026 158 LEU A CD1 593 C CD2 . LEU A 77 ? 0.0992 0.1011 0.0990 0.0018 -0.0035 -0.0013 158 LEU A CD2 594 N N . MET A 78 ? 0.0999 0.0999 0.1010 0.0013 -0.0042 -0.0039 159 MET A N 595 C CA . MET A 78 ? 0.1065 0.1061 0.1072 0.0012 -0.0045 -0.0033 159 MET A CA 596 C C . MET A 78 ? 0.0943 0.0919 0.0952 0.0014 -0.0046 -0.0022 159 MET A C 597 O O . MET A 78 ? 0.0896 0.0861 0.0908 0.0015 -0.0045 -0.0021 159 MET A O 598 C CB . MET A 78 ? 0.1145 0.1141 0.1156 0.0008 -0.0045 -0.0043 159 MET A CB 599 C CG . MET A 78 ? 0.1587 0.1605 0.1597 0.0004 -0.0043 -0.0056 159 MET A CG 600 S SD . MET A 78 ? 0.2565 0.2586 0.2579 -0.0003 -0.0043 -0.0069 159 MET A SD 601 C CE . MET A 78 ? 0.1749 0.1784 0.1757 -0.0001 -0.0048 -0.0057 159 MET A CE 602 N N . SER A 79 ? 0.0572 0.0543 0.0577 0.0015 -0.0048 -0.0015 160 SER A N 603 C CA . SER A 79 ? 0.0642 0.0595 0.0648 0.0016 -0.0049 -0.0007 160 SER A CA 604 C C . SER A 79 ? 0.0782 0.0728 0.0788 0.0016 -0.0051 -0.0005 160 SER A C 605 O O . SER A 79 ? 0.0634 0.0592 0.0637 0.0015 -0.0051 -0.0007 160 SER A O 606 C CB . SER A 79 ? 0.0691 0.0643 0.0690 0.0019 -0.0047 0.0004 160 SER A CB 607 O OG . SER A 79 ? 0.1094 0.1055 0.1087 0.0021 -0.0047 0.0010 160 SER A OG 608 N N . CYS A 80 ? 0.1086 0.1015 0.1094 0.0015 -0.0052 -0.0002 161 CYS A N 609 C CA . CYS A 80 ? 0.1310 0.1232 0.1318 0.0015 -0.0053 0.0001 161 CYS A CA 610 C C . CYS A 80 ? 0.1365 0.1273 0.1371 0.0015 -0.0053 0.0008 161 CYS A C 611 O O . CYS A 80 ? 0.1094 0.0997 0.1101 0.0016 -0.0053 0.0010 161 CYS A O 612 C CB . CYS A 80 ? 0.1296 0.1214 0.1311 0.0011 -0.0053 -0.0007 161 CYS A CB 613 S SG . CYS A 80 ? 0.1806 0.1708 0.1828 0.0011 -0.0052 -0.0009 161 CYS A SG 614 N N . PRO A 81 ? 0.1387 0.1290 0.1391 0.0016 -0.0054 0.0012 162 PRO A N 615 C CA . PRO A 81 ? 0.1093 0.0982 0.1095 0.0016 -0.0054 0.0018 162 PRO A CA 616 C C . PRO A 81 ? 0.1030 0.0912 0.1038 0.0014 -0.0055 0.0016 162 PRO A C 617 O O . PRO A 81 ? 0.0907 0.0788 0.0919 0.0013 -0.0056 0.0011 162 PRO A O 618 C CB . PRO A 81 ? 0.1569 0.1456 0.1570 0.0016 -0.0054 0.0020 162 PRO A CB 619 C CG . PRO A 81 ? 0.1879 0.1781 0.1878 0.0018 -0.0054 0.0019 162 PRO A CG 620 C CD . PRO A 81 ? 0.1252 0.1162 0.1255 0.0016 -0.0054 0.0012 162 PRO A CD 621 N N . ILE A 82 ? 0.1452 0.1328 0.1458 0.0013 -0.0055 0.0019 163 ILE A N 622 C CA . ILE A 82 ? 0.1422 0.1294 0.1433 0.0013 -0.0056 0.0019 163 ILE A CA 623 C C . ILE A 82 ? 0.1512 0.1378 0.1525 0.0012 -0.0058 0.0019 163 ILE A C 624 O O . ILE A 82 ? 0.1237 0.1100 0.1247 0.0011 -0.0058 0.0022 163 ILE A O 625 C CB . ILE A 82 ? 0.1658 0.1529 0.1667 0.0011 -0.0056 0.0022 163 ILE A CB 626 C CG1 . ILE A 82 ? 0.1930 0.1805 0.1945 0.0012 -0.0058 0.0021 163 ILE A CG1 627 C CG2 . ILE A 82 ? 0.1573 0.1438 0.1577 0.0009 -0.0056 0.0025 163 ILE A CG2 628 C CD1 . ILE A 82 ? 0.2203 0.2081 0.2217 0.0008 -0.0058 0.0023 163 ILE A CD1 629 N N . GLY A 83 ? 0.0893 0.0757 0.0912 0.0014 -0.0058 0.0018 164 GLY A N 630 C CA . GLY A 83 ? 0.1224 0.1081 0.1245 0.0014 -0.0059 0.0020 164 GLY A CA 631 C C . GLY A 83 ? 0.1279 0.1132 0.1303 0.0012 -0.0057 0.0016 164 GLY A C 632 O O . GLY A 83 ? 0.1719 0.1565 0.1746 0.0012 -0.0056 0.0017 164 GLY A O 633 N N . GLU A 84 ? 0.1310 0.1171 0.1333 0.0011 -0.0056 0.0011 165 GLU A N 634 C CA . GLU A 84 ? 0.1386 0.1248 0.1410 0.0008 -0.0055 0.0005 165 GLU A CA 635 C C . GLU A 84 ? 0.1533 0.1395 0.1564 0.0008 -0.0052 -0.0002 165 GLU A C 636 O O . GLU A 84 ? 0.1344 0.1211 0.1376 0.0011 -0.0052 -0.0004 165 GLU A O 637 C CB . GLU A 84 ? 0.1420 0.1294 0.1440 0.0007 -0.0055 0.0004 165 GLU A CB 638 C CG . GLU A 84 ? 0.1713 0.1586 0.1728 0.0008 -0.0056 0.0011 165 GLU A CG 639 C CD . GLU A 84 ? 0.2107 0.1992 0.2118 0.0009 -0.0056 0.0010 165 GLU A CD 640 O OE1 . GLU A 84 ? 0.2652 0.2549 0.2665 0.0007 -0.0056 0.0004 165 GLU A OE1 641 O OE2 . GLU A 84 ? 0.2094 0.1979 0.2100 0.0011 -0.0056 0.0016 165 GLU A OE2 642 N N . VAL A 85 ? 0.1201 0.1058 0.1236 0.0004 -0.0049 -0.0008 166 VAL A N 643 C CA . VAL A 85 ? 0.1187 0.1043 0.1228 0.0004 -0.0046 -0.0017 166 VAL A CA 644 C C . VAL A 85 ? 0.1101 0.0974 0.1139 0.0002 -0.0046 -0.0025 166 VAL A C 645 O O . VAL A 85 ? 0.1242 0.1127 0.1276 -0.0001 -0.0048 -0.0025 166 VAL A O 646 C CB . VAL A 85 ? 0.1055 0.0900 0.1102 -0.0001 -0.0041 -0.0022 166 VAL A CB 647 C CG1 . VAL A 85 ? 0.1247 0.1074 0.1296 0.0002 -0.0040 -0.0013 166 VAL A CG1 648 C CG2 . VAL A 85 ? 0.1590 0.1444 0.1634 -0.0008 -0.0042 -0.0027 166 VAL A CG2 649 N N . PRO A 86 ? 0.1110 0.0987 0.1151 0.0003 -0.0044 -0.0030 167 PRO A N 650 C CA . PRO A 86 ? 0.1151 0.1045 0.1189 0.0002 -0.0044 -0.0038 167 PRO A CA 651 C C . PRO A 86 ? 0.1106 0.1007 0.1147 -0.0006 -0.0041 -0.0050 167 PRO A C 652 O O . PRO A 86 ? 0.1350 0.1243 0.1397 -0.0008 -0.0036 -0.0060 167 PRO A O 653 C CB . PRO A 86 ? 0.1268 0.1162 0.1310 0.0005 -0.0042 -0.0041 167 PRO A CB 654 C CG . PRO A 86 ? 0.1391 0.1264 0.1440 0.0008 -0.0039 -0.0040 167 PRO A CG 655 C CD . PRO A 86 ? 0.1139 0.1004 0.1186 0.0008 -0.0042 -0.0029 167 PRO A CD 656 N N . SER A 87 ? 0.1135 0.1049 0.1171 -0.0009 -0.0043 -0.0050 168 SER A N 657 C CA . SER A 87 ? 0.1155 0.1080 0.1194 -0.0017 -0.0041 -0.0061 168 SER A CA 658 C C . SER A 87 ? 0.1092 0.1046 0.1125 -0.0018 -0.0044 -0.0065 168 SER A C 659 O O . SER A 87 ? 0.1071 0.1034 0.1098 -0.0012 -0.0047 -0.0055 168 SER A O 660 C CB . SER A 87 ? 0.1409 0.1326 0.1449 -0.0021 -0.0042 -0.0058 168 SER A CB 661 O OG . SER A 87 ? 0.1766 0.1697 0.1808 -0.0030 -0.0040 -0.0069 168 SER A OG 662 N N . PRO A 88 ? 0.1271 0.1239 0.1306 -0.0026 -0.0041 -0.0079 169 PRO A N 663 C CA . PRO A 88 ? 0.1351 0.1352 0.1380 -0.0027 -0.0044 -0.0082 169 PRO A CA 664 C C . PRO A 88 ? 0.1771 0.1785 0.1797 -0.0024 -0.0048 -0.0072 169 PRO A C 665 O O . PRO A 88 ? 0.1590 0.1631 0.1611 -0.0021 -0.0051 -0.0069 169 PRO A O 666 C CB . PRO A 88 ? 0.1238 0.1250 0.1272 -0.0038 -0.0040 -0.0101 169 PRO A CB 667 C CG . PRO A 88 ? 0.1331 0.1313 0.1373 -0.0043 -0.0035 -0.0106 169 PRO A CG 668 C CD . PRO A 88 ? 0.1112 0.1068 0.1155 -0.0033 -0.0035 -0.0093 169 PRO A CD 669 N N . TYR A 89 A 0.1241 0.1237 0.1269 -0.0025 -0.0048 -0.0067 169 TYR A N 670 C CA . TYR A 89 A 0.1225 0.1234 0.1251 -0.0023 -0.0051 -0.0059 169 TYR A CA 671 C C . TYR A 89 A 0.1756 0.1755 0.1777 -0.0013 -0.0054 -0.0042 169 TYR A C 672 O O . TYR A 89 A 0.1516 0.1526 0.1534 -0.0009 -0.0056 -0.0035 169 TYR A O 673 C CB . TYR A 89 A 0.1506 0.1506 0.1538 -0.0031 -0.0049 -0.0063 169 TYR A CB 674 C CG . TYR A 89 A 0.1049 0.1050 0.1087 -0.0042 -0.0045 -0.0080 169 TYR A CG 675 C CD1 . TYR A 89 A 0.1461 0.1490 0.1499 -0.0048 -0.0044 -0.0092 169 TYR A CD1 676 C CD2 . TYR A 89 A 0.1537 0.1513 0.1582 -0.0049 -0.0040 -0.0084 169 TYR A CD2 677 C CE1 . TYR A 89 A 0.1304 0.1333 0.1348 -0.0060 -0.0039 -0.0110 169 TYR A CE1 678 C CE2 . TYR A 89 A 0.1551 0.1524 0.1602 -0.0060 -0.0034 -0.0100 169 TYR A CE2 679 C CZ . TYR A 89 A 0.1340 0.1340 0.1391 -0.0066 -0.0034 -0.0114 169 TYR A CZ 680 O OH . TYR A 89 A 0.1531 0.1527 0.1587 -0.0078 -0.0027 -0.0132 169 TYR A OH 681 N N . ASN A 90 ? 0.1321 0.1301 0.1341 -0.0009 -0.0053 -0.0038 170 ASN A N 682 C CA . ASN A 90 ? 0.1525 0.1494 0.1540 -0.0001 -0.0055 -0.0024 170 ASN A CA 683 C C . ASN A 90 ? 0.1443 0.1411 0.1454 0.0004 -0.0055 -0.0020 170 ASN A C 684 O O . ASN A 90 ? 0.1961 0.1920 0.1969 0.0009 -0.0055 -0.0010 170 ASN A O 685 C CB . ASN A 90 ? 0.1928 0.1872 0.1946 -0.0001 -0.0054 -0.0019 170 ASN A CB 686 C CG . ASN A 90 ? 0.2032 0.1959 0.2053 -0.0002 -0.0053 -0.0022 170 ASN A CG 687 O OD1 . ASN A 90 ? 0.1993 0.1924 0.2018 -0.0004 -0.0051 -0.0031 170 ASN A OD1 688 N ND2 . ASN A 90 ? 0.2368 0.2277 0.2389 0.0001 -0.0053 -0.0014 170 ASN A ND2 689 N N . SER A 91 ? 0.1324 0.1304 0.1336 0.0002 -0.0054 -0.0029 171 SER A N 690 C CA . SER A 91 ? 0.1338 0.1318 0.1347 0.0005 -0.0053 -0.0026 171 SER A CA 691 C C . SER A 91 ? 0.1475 0.1480 0.1478 0.0009 -0.0053 -0.0023 171 SER A C 692 O O . SER A 91 ? 0.1603 0.1630 0.1605 0.0007 -0.0054 -0.0029 171 SER A O 693 C CB . SER A 91 ? 0.1595 0.1569 0.1610 0.0002 -0.0050 -0.0038 171 SER A CB 694 O OG . SER A 91 ? 0.1664 0.1615 0.1685 0.0001 -0.0049 -0.0037 171 SER A OG 695 N N . ARG A 92 ? 0.1009 0.1010 0.1007 0.0014 -0.0053 -0.0013 172 ARG A N 696 C CA . ARG A 92 ? 0.1420 0.1441 0.1411 0.0019 -0.0052 -0.0007 172 ARG A CA 697 C C . ARG A 92 ? 0.1206 0.1238 0.1197 0.0017 -0.0051 -0.0014 172 ARG A C 698 O O . ARG A 92 ? 0.1175 0.1191 0.1170 0.0016 -0.0049 -0.0017 172 ARG A O 699 C CB . ARG A 92 ? 0.1602 0.1612 0.1588 0.0025 -0.0051 0.0008 172 ARG A CB 700 C CG . ARG A 92 ? 0.3209 0.3236 0.3187 0.0031 -0.0049 0.0017 172 ARG A CG 701 C CD . ARG A 92 ? 0.4661 0.4679 0.4634 0.0038 -0.0047 0.0031 172 ARG A CD 702 N NE . ARG A 92 ? 0.4115 0.4109 0.4088 0.0038 -0.0044 0.0038 172 ARG A NE 703 C CZ . ARG A 92 ? 0.4797 0.4770 0.4769 0.0040 -0.0042 0.0045 172 ARG A CZ 704 N NH1 . ARG A 92 ? 0.4724 0.4699 0.4696 0.0043 -0.0044 0.0047 172 ARG A NH1 705 N NH2 . ARG A 92 ? 0.3598 0.3552 0.3569 0.0038 -0.0039 0.0048 172 ARG A NH2 706 N N . PHE A 93 ? 0.0930 0.0989 0.0917 0.0017 -0.0051 -0.0018 173 PHE A N 707 C CA . PHE A 93 ? 0.1104 0.1175 0.1090 0.0015 -0.0049 -0.0025 173 PHE A CA 708 C C . PHE A 93 ? 0.0894 0.0963 0.0874 0.0021 -0.0047 -0.0012 173 PHE A C 709 O O . PHE A 93 ? 0.1068 0.1142 0.1041 0.0027 -0.0047 0.0001 173 PHE A O 710 C CB . PHE A 93 ? 0.1087 0.1192 0.1070 0.0013 -0.0050 -0.0034 173 PHE A CB 711 C CG . PHE A 93 ? 0.0743 0.0862 0.0723 0.0011 -0.0047 -0.0041 173 PHE A CG 712 C CD1 . PHE A 93 ? 0.1090 0.1204 0.1076 0.0005 -0.0045 -0.0057 173 PHE A CD1 713 C CD2 . PHE A 93 ? 0.0746 0.0885 0.0717 0.0017 -0.0046 -0.0030 173 PHE A CD2 714 C CE1 . PHE A 93 ? 0.1078 0.1207 0.1062 0.0004 -0.0042 -0.0064 173 PHE A CE1 715 C CE2 . PHE A 93 ? 0.0795 0.0950 0.0764 0.0015 -0.0044 -0.0037 173 PHE A CE2 716 C CZ . PHE A 93 ? 0.0731 0.0881 0.0707 0.0009 -0.0042 -0.0054 173 PHE A CZ 717 N N . GLU A 94 ? 0.0965 0.1027 0.0948 0.0019 -0.0044 -0.0016 174 GLU A N 718 C CA . GLU A 94 ? 0.0907 0.0966 0.0885 0.0023 -0.0042 -0.0005 174 GLU A CA 719 C C . GLU A 94 ? 0.0953 0.1036 0.0927 0.0022 -0.0039 -0.0010 174 GLU A C 720 O O . GLU A 94 ? 0.1233 0.1331 0.1198 0.0026 -0.0038 0.0000 174 GLU A O 721 C CB . GLU A 94 ? 0.1164 0.1198 0.1148 0.0022 -0.0040 -0.0004 174 GLU A CB 722 C CG . GLU A 94 ? 0.0890 0.0901 0.0876 0.0022 -0.0042 0.0000 174 GLU A CG 723 C CD . GLU A 94 ? 0.1606 0.1613 0.1586 0.0026 -0.0042 0.0015 174 GLU A CD 724 O OE1 . GLU A 94 ? 0.1593 0.1611 0.1566 0.0029 -0.0039 0.0023 174 GLU A OE1 725 O OE2 . GLU A 94 ? 0.1701 0.1691 0.1683 0.0026 -0.0043 0.0018 174 GLU A OE2 726 N N . SER A 95 ? 0.0690 0.0776 0.0670 0.0018 -0.0038 -0.0025 175 SER A N 727 C CA . SER A 95 ? 0.1011 0.1119 0.0988 0.0017 -0.0036 -0.0031 175 SER A CA 728 C C . SER A 95 ? 0.0945 0.1055 0.0929 0.0012 -0.0034 -0.0051 175 SER A C 729 O O . SER A 95 ? 0.0797 0.0886 0.0789 0.0011 -0.0035 -0.0057 175 SER A O 730 C CB . SER A 95 ? 0.1494 0.1595 0.1470 0.0019 -0.0032 -0.0022 175 SER A CB 731 O OG . SER A 95 ? 0.2531 0.2653 0.2503 0.0018 -0.0029 -0.0028 175 SER A OG 732 N N . VAL A 96 ? 0.0787 0.0922 0.0767 0.0010 -0.0032 -0.0060 176 VAL A N 733 C CA . VAL A 96 ? 0.0673 0.0809 0.0660 0.0006 -0.0029 -0.0079 176 VAL A CA 734 C C . VAL A 96 ? 0.0739 0.0863 0.0732 0.0009 -0.0025 -0.0078 176 VAL A C 735 O O . VAL A 96 ? 0.1070 0.1205 0.1056 0.0011 -0.0024 -0.0070 176 VAL A O 736 C CB . VAL A 96 ? 0.0822 0.0992 0.0803 0.0002 -0.0027 -0.0091 176 VAL A CB 737 C CG1 . VAL A 96 ? 0.0732 0.0900 0.0721 -0.0002 -0.0023 -0.0112 176 VAL A CG1 738 C CG2 . VAL A 96 ? 0.0766 0.0954 0.0741 0.0000 -0.0031 -0.0091 176 VAL A CG2 739 N N . ALA A 97 ? 0.0893 0.0994 0.0896 0.0009 -0.0024 -0.0085 177 ALA A N 740 C CA . ALA A 97 ? 0.1038 0.1129 0.1047 0.0012 -0.0021 -0.0082 177 ALA A CA 741 C C . ALA A 97 ? 0.0862 0.0933 0.0884 0.0013 -0.0019 -0.0092 177 ALA A C 742 O O . ALA A 97 ? 0.0916 0.0968 0.0941 0.0012 -0.0020 -0.0094 177 ALA A O 743 C CB . ALA A 97 ? 0.0922 0.1000 0.0929 0.0015 -0.0024 -0.0064 177 ALA A CB 744 N N . TRP A 98 ? 0.0463 0.0537 0.0489 0.0016 -0.0014 -0.0097 178 TRP A N 745 C CA . TRP A 98 ? 0.0694 0.0749 0.0733 0.0020 -0.0012 -0.0103 178 TRP A CA 746 C C . TRP A 98 ? 0.0730 0.0779 0.0773 0.0025 -0.0012 -0.0091 178 TRP A C 747 O O . TRP A 98 ? 0.0803 0.0840 0.0857 0.0029 -0.0010 -0.0093 178 TRP A O 748 C CB . TRP A 98 ? 0.1004 0.1065 0.1049 0.0020 -0.0005 -0.0121 178 TRP A CB 749 C CG . TRP A 98 ? 0.0895 0.0983 0.0934 0.0019 -0.0001 -0.0127 178 TRP A CG 750 C CD1 . TRP A 98 ? 0.0817 0.0926 0.0849 0.0013 0.0001 -0.0139 178 TRP A CD1 751 C CD2 . TRP A 98 ? 0.0556 0.0656 0.0596 0.0022 0.0001 -0.0121 178 TRP A CD2 752 N NE1 . TRP A 98 ? 0.1033 0.1166 0.1061 0.0014 0.0004 -0.0141 178 TRP A NE1 753 C CE2 . TRP A 98 ? 0.1049 0.1175 0.1082 0.0019 0.0004 -0.0130 178 TRP A CE2 754 C CE3 . TRP A 98 ? 0.0823 0.0916 0.0869 0.0027 0.0000 -0.0111 178 TRP A CE3 755 C CZ2 . TRP A 98 ? 0.0800 0.0944 0.0832 0.0021 0.0007 -0.0127 178 TRP A CZ2 756 C CZ3 . TRP A 98 ? 0.0987 0.1098 0.1033 0.0029 0.0003 -0.0109 178 TRP A CZ3 757 C CH2 . TRP A 98 ? 0.0734 0.0869 0.0772 0.0026 0.0007 -0.0117 178 TRP A CH2 758 N N . SER A 99 ? 0.0730 0.0788 0.0766 0.0023 -0.0015 -0.0078 179 SER A N 759 C CA . SER A 99 ? 0.0947 0.1000 0.0985 0.0025 -0.0017 -0.0066 179 SER A CA 760 C C . SER A 99 ? 0.0948 0.1002 0.0976 0.0022 -0.0020 -0.0053 179 SER A C 761 O O . SER A 99 ? 0.1209 0.1277 0.1228 0.0020 -0.0019 -0.0052 179 SER A O 762 C CB . SER A 99 ? 0.0958 0.1027 0.1001 0.0027 -0.0012 -0.0069 179 SER A CB 763 O OG . SER A 99 ? 0.0974 0.1040 0.1020 0.0028 -0.0013 -0.0059 179 SER A OG 764 N N . ALA A 100 ? 0.0954 0.0993 0.0984 0.0022 -0.0023 -0.0043 180 ALA A N 765 C CA . ALA A 100 ? 0.0766 0.0802 0.0787 0.0019 -0.0025 -0.0031 180 ALA A CA 766 C C . ALA A 100 ? 0.1241 0.1266 0.1263 0.0018 -0.0026 -0.0021 180 ALA A C 767 O O . ALA A 100 ? 0.0965 0.0986 0.0996 0.0019 -0.0026 -0.0022 180 ALA A O 768 C CB . ALA A 100 ? 0.1068 0.1095 0.1085 0.0019 -0.0028 -0.0032 180 ALA A CB 769 N N . SER A 101 ? 0.0983 0.1004 0.0996 0.0015 -0.0026 -0.0011 181 SER A N 770 C CA . SER A 101 ? 0.0949 0.0958 0.0962 0.0012 -0.0026 -0.0002 181 SER A CA 771 C C . SER A 101 ? 0.0746 0.0747 0.0749 0.0012 -0.0026 0.0007 181 SER A C 772 O O . SER A 101 ? 0.1015 0.1025 0.1012 0.0014 -0.0026 0.0008 181 SER A O 773 C CB . SER A 101 ? 0.1309 0.1327 0.1324 0.0009 -0.0022 0.0002 181 SER A CB 774 O OG . SER A 101 ? 0.1564 0.1569 0.1577 0.0004 -0.0022 0.0009 181 SER A OG 775 N N . ALA A 102 ? 0.0316 0.0301 0.0318 0.0010 -0.0027 0.0014 182 ALA A N 776 C CA . ALA A 102 ? 0.0376 0.0351 0.0370 0.0010 -0.0026 0.0023 182 ALA A CA 777 C C . ALA A 102 ? 0.0818 0.0776 0.0811 0.0006 -0.0024 0.0028 182 ALA A C 778 O O . ALA A 102 ? 0.0787 0.0742 0.0787 0.0003 -0.0026 0.0024 182 ALA A O 779 C CB . ALA A 102 ? 0.0757 0.0728 0.0750 0.0014 -0.0030 0.0020 182 ALA A CB 780 N N . CYS A 103 ? 0.0810 0.0760 0.0796 0.0006 -0.0020 0.0038 183 CYS A N 781 C CA . CYS A 103 ? 0.1151 0.1084 0.1136 0.0001 -0.0017 0.0042 183 CYS A CA 782 C C . CYS A 103 ? 0.1154 0.1075 0.1130 0.0004 -0.0012 0.0053 183 CYS A C 783 O O . CYS A 103 ? 0.1317 0.1247 0.1287 0.0009 -0.0010 0.0058 183 CYS A O 784 C CB . CYS A 103 ? 0.1054 0.0989 0.1042 -0.0006 -0.0013 0.0041 183 CYS A CB 785 S SG . CYS A 103 ? 0.1699 0.1648 0.1683 -0.0007 -0.0006 0.0046 183 CYS A SG 786 N N . HIS A 104 ? 0.0608 0.0510 0.0582 0.0001 -0.0009 0.0055 184 HIS A N 787 C CA . HIS A 104 ? 0.0658 0.0546 0.0625 0.0005 -0.0004 0.0065 184 HIS A CA 788 C C . HIS A 104 ? 0.0894 0.0767 0.0859 -0.0002 0.0006 0.0070 184 HIS A C 789 O O . HIS A 104 ? 0.1241 0.1107 0.1210 -0.0011 0.0006 0.0064 184 HIS A O 790 C CB . HIS A 104 ? 0.0647 0.0522 0.0614 0.0007 -0.0007 0.0064 184 HIS A CB 791 C CG . HIS A 104 ? 0.0606 0.0474 0.0566 0.0015 -0.0003 0.0074 184 HIS A CG 792 N ND1 . HIS A 104 ? 0.0777 0.0625 0.0732 0.0015 0.0006 0.0082 184 HIS A ND1 793 C CD2 . HIS A 104 ? 0.0740 0.0617 0.0698 0.0024 -0.0007 0.0076 184 HIS A CD2 794 C CE1 . HIS A 104 ? 0.0761 0.0608 0.0712 0.0025 0.0007 0.0090 184 HIS A CE1 795 N NE2 . HIS A 104 ? 0.0728 0.0594 0.0681 0.0030 -0.0001 0.0087 184 HIS A NE2 796 N N . ASP A 105 ? 0.0689 0.0557 0.0647 0.0001 0.0014 0.0081 185 ASP A N 797 C CA . ASP A 105 ? 0.1214 0.1066 0.1169 -0.0007 0.0024 0.0086 185 ASP A CA 798 C C . ASP A 105 ? 0.1219 0.1044 0.1170 -0.0006 0.0031 0.0091 185 ASP A C 799 O O . ASP A 105 ? 0.1331 0.1137 0.1279 -0.0012 0.0042 0.0096 185 ASP A O 800 C CB . ASP A 105 ? 0.1164 0.1024 0.1113 -0.0004 0.0031 0.0097 185 ASP A CB 801 C CG . ASP A 105 ? 0.1117 0.0975 0.1058 0.0009 0.0034 0.0110 185 ASP A CG 802 O OD1 . ASP A 105 ? 0.1244 0.1097 0.1185 0.0015 0.0030 0.0110 185 ASP A OD1 803 O OD2 . ASP A 105 ? 0.1380 0.1243 0.1315 0.0012 0.0040 0.0121 185 ASP A OD2 804 N N . GLY A 106 ? 0.0819 0.0640 0.0771 0.0000 0.0026 0.0089 186 GLY A N 805 C CA . GLY A 106 ? 0.1111 0.0907 0.1059 0.0002 0.0033 0.0093 186 GLY A CA 806 C C . GLY A 106 ? 0.1508 0.1303 0.1450 0.0016 0.0035 0.0106 186 GLY A C 807 O O . GLY A 106 ? 0.1831 0.1613 0.1771 0.0022 0.0037 0.0108 186 GLY A O 808 N N . ILE A 107 ? 0.1419 0.1231 0.1357 0.0022 0.0035 0.0114 187 ILE A N 809 C CA . ILE A 107 ? 0.1419 0.1237 0.1352 0.0037 0.0037 0.0128 187 ILE A CA 810 C C . ILE A 107 ? 0.1560 0.1408 0.1494 0.0043 0.0025 0.0123 187 ILE A C 811 O O . ILE A 107 ? 0.1663 0.1516 0.1598 0.0051 0.0021 0.0125 187 ILE A O 812 C CB . ILE A 107 ? 0.1901 0.1719 0.1827 0.0040 0.0046 0.0142 187 ILE A CB 813 C CG1 . ILE A 107 ? 0.2459 0.2247 0.2384 0.0032 0.0059 0.0145 187 ILE A CG1 814 C CG2 . ILE A 107 ? 0.1902 0.1728 0.1823 0.0056 0.0048 0.0158 187 ILE A CG2 815 C CD1 . ILE A 107 ? 0.2705 0.2464 0.2629 0.0034 0.0066 0.0147 187 ILE A CD1 816 N N . ASN A 108 ? 0.0978 0.0847 0.0915 0.0038 0.0019 0.0117 188 ASN A N 817 C CA . ASN A 108 ? 0.0898 0.0795 0.0837 0.0042 0.0010 0.0111 188 ASN A CA 818 C C . ASN A 108 ? 0.0872 0.0780 0.0817 0.0034 0.0003 0.0097 188 ASN A C 819 O O . ASN A 108 ? 0.0771 0.0670 0.0719 0.0025 0.0006 0.0093 188 ASN A O 820 C CB . ASN A 108 ? 0.1128 0.1046 0.1060 0.0051 0.0011 0.0122 188 ASN A CB 821 C CG . ASN A 108 ? 0.1477 0.1393 0.1403 0.0063 0.0016 0.0137 188 ASN A CG 822 O OD1 . ASN A 108 ? 0.2466 0.2377 0.2386 0.0069 0.0024 0.0151 188 ASN A OD1 823 N ND2 . ASN A 108 ? 0.1372 0.1291 0.1301 0.0068 0.0010 0.0133 188 ASN A ND2 824 N N . TRP A 109 ? 0.0959 0.0887 0.0907 0.0036 -0.0006 0.0089 189 TRP A N 825 C CA . TRP A 109 ? 0.0995 0.0934 0.0950 0.0030 -0.0011 0.0076 189 TRP A CA 826 C C . TRP A 109 ? 0.1041 0.0999 0.0993 0.0029 -0.0010 0.0076 189 TRP A C 827 O O . TRP A 109 ? 0.1011 0.0986 0.0958 0.0035 -0.0008 0.0083 189 TRP A O 828 C CB . TRP A 109 ? 0.0840 0.0790 0.0799 0.0032 -0.0019 0.0067 189 TRP A CB 829 C CG . TRP A 109 ? 0.1140 0.1073 0.1104 0.0030 -0.0022 0.0063 189 TRP A CG 830 C CD1 . TRP A 109 ? 0.1173 0.1100 0.1135 0.0035 -0.0023 0.0066 189 TRP A CD1 831 C CD2 . TRP A 109 ? 0.0825 0.0747 0.0796 0.0023 -0.0025 0.0054 189 TRP A CD2 832 N NE1 . TRP A 109 ? 0.1341 0.1254 0.1308 0.0031 -0.0026 0.0060 189 TRP A NE1 833 C CE2 . TRP A 109 ? 0.1034 0.0944 0.1005 0.0024 -0.0027 0.0054 189 TRP A CE2 834 C CE3 . TRP A 109 ? 0.0717 0.0640 0.0692 0.0018 -0.0025 0.0048 189 TRP A CE3 835 C CZ2 . TRP A 109 ? 0.1698 0.1597 0.1675 0.0019 -0.0030 0.0047 189 TRP A CZ2 836 C CZ3 . TRP A 109 ? 0.1027 0.0941 0.1008 0.0013 -0.0028 0.0042 189 TRP A CZ3 837 C CH2 . TRP A 109 ? 0.1089 0.0991 0.1071 0.0014 -0.0030 0.0042 189 TRP A CH2 838 N N . LEU A 110 ? 0.1077 0.1036 0.1035 0.0022 -0.0009 0.0069 190 LEU A N 839 C CA . LEU A 110 ? 0.0949 0.0928 0.0907 0.0021 -0.0009 0.0066 190 LEU A CA 840 C C . LEU A 110 ? 0.0736 0.0727 0.0702 0.0020 -0.0016 0.0051 190 LEU A C 841 O O . LEU A 110 ? 0.0736 0.0715 0.0709 0.0016 -0.0018 0.0044 190 LEU A O 842 C CB . LEU A 110 ? 0.0922 0.0895 0.0880 0.0015 -0.0002 0.0068 190 LEU A CB 843 C CG . LEU A 110 ? 0.1137 0.1132 0.1098 0.0012 -0.0002 0.0062 190 LEU A CG 844 C CD1 . LEU A 110 ? 0.0897 0.0912 0.0849 0.0018 0.0000 0.0069 190 LEU A CD1 845 C CD2 . LEU A 110 ? 0.1207 0.1196 0.1171 0.0004 0.0004 0.0063 190 LEU A CD2 846 N N . THR A 111 ? 0.0856 0.0868 0.0820 0.0022 -0.0018 0.0046 191 THR A N 847 C CA . THR A 111 ? 0.0733 0.0754 0.0705 0.0021 -0.0022 0.0031 191 THR A CA 848 C C . THR A 111 ? 0.1013 0.1055 0.0984 0.0020 -0.0020 0.0026 191 THR A C 849 O O . THR A 111 ? 0.0993 0.1050 0.0956 0.0022 -0.0016 0.0033 191 THR A O 850 C CB . THR A 111 ? 0.1256 0.1283 0.1228 0.0023 -0.0027 0.0025 191 THR A CB 851 O OG1 . THR A 111 ? 0.1152 0.1200 0.1116 0.0027 -0.0027 0.0029 191 THR A OG1 852 C CG2 . THR A 111 ? 0.0853 0.0861 0.0826 0.0024 -0.0030 0.0029 191 THR A CG2 853 N N . ILE A 112 ? 0.0783 0.0827 0.0763 0.0017 -0.0021 0.0015 192 ILE A N 854 C CA . ILE A 112 ? 0.0791 0.0854 0.0772 0.0016 -0.0018 0.0009 192 ILE A CA 855 C C . ILE A 112 ? 0.0817 0.0886 0.0805 0.0017 -0.0021 -0.0007 192 ILE A C 856 O O . ILE A 112 ? 0.1161 0.1217 0.1158 0.0017 -0.0023 -0.0013 192 ILE A O 857 C CB . ILE A 112 ? 0.0855 0.0914 0.0841 0.0013 -0.0014 0.0010 192 ILE A CB 858 C CG1 . ILE A 112 ? 0.1061 0.1110 0.1040 0.0010 -0.0010 0.0025 192 ILE A CG1 859 C CG2 . ILE A 112 ? 0.1072 0.1153 0.1059 0.0012 -0.0011 0.0003 192 ILE A CG2 860 C CD1 . ILE A 112 ? 0.1449 0.1495 0.1434 0.0005 -0.0006 0.0025 192 ILE A CD1 861 N N . GLY A 113 ? 0.0611 0.0700 0.0594 0.0018 -0.0021 -0.0014 193 GLY A N 862 C CA . GLY A 113 ? 0.0524 0.0618 0.0513 0.0017 -0.0022 -0.0030 193 GLY A CA 863 C C . GLY A 113 ? 0.0629 0.0745 0.0618 0.0017 -0.0018 -0.0040 193 GLY A C 864 O O . GLY A 113 ? 0.0523 0.0661 0.0503 0.0017 -0.0017 -0.0037 193 GLY A O 865 N N . ILE A 114 ? 0.0465 0.0577 0.0464 0.0017 -0.0016 -0.0051 194 ILE A N 866 C CA . ILE A 114 ? 0.0477 0.0610 0.0477 0.0016 -0.0012 -0.0062 194 ILE A CA 867 C C . ILE A 114 ? 0.0727 0.0864 0.0730 0.0015 -0.0011 -0.0080 194 ILE A C 868 O O . ILE A 114 ? 0.0664 0.0782 0.0675 0.0016 -0.0012 -0.0087 194 ILE A O 869 C CB . ILE A 114 ? 0.0737 0.0864 0.0747 0.0018 -0.0009 -0.0064 194 ILE A CB 870 C CG1 . ILE A 114 ? 0.0618 0.0741 0.0625 0.0017 -0.0008 -0.0048 194 ILE A CG1 871 C CG2 . ILE A 114 ? 0.1116 0.1264 0.1127 0.0018 -0.0003 -0.0076 194 ILE A CG2 872 C CD1 . ILE A 114 ? 0.0694 0.0812 0.0712 0.0018 -0.0006 -0.0049 194 ILE A CD1 873 N N . SER A 115 ? 0.0796 0.0959 0.0792 0.0013 -0.0009 -0.0087 195 SER A N 874 C CA . SER A 115 ? 0.0910 0.1081 0.0908 0.0010 -0.0007 -0.0107 195 SER A CA 875 C C . SER A 115 ? 0.0997 0.1196 0.0990 0.0009 -0.0002 -0.0117 195 SER A C 876 O O . SER A 115 ? 0.1131 0.1342 0.1120 0.0010 0.0000 -0.0108 195 SER A O 877 C CB . SER A 115 ? 0.0880 0.1057 0.0872 0.0007 -0.0011 -0.0108 195 SER A CB 878 O OG . SER A 115 ? 0.0964 0.1141 0.0960 0.0002 -0.0009 -0.0128 195 SER A OG 879 N N . GLY A 116 ? 0.0977 0.1185 0.0972 0.0005 0.0001 -0.0137 196 GLY A N 880 C CA . GLY A 116 ? 0.1274 0.1510 0.1266 0.0003 0.0006 -0.0150 196 GLY A CA 881 C C . GLY A 116 ? 0.1253 0.1477 0.1257 0.0005 0.0013 -0.0165 196 GLY A C 882 O O . GLY A 116 ? 0.1097 0.1292 0.1112 0.0008 0.0013 -0.0165 196 GLY A O 883 N N . PRO A 117 ? 0.1123 0.1370 0.1124 0.0004 0.0019 -0.0177 197 PRO A N 884 C CA . PRO A 117 ? 0.1057 0.1297 0.1070 0.0007 0.0027 -0.0193 197 PRO A CA 885 C C . PRO A 117 ? 0.1360 0.1588 0.1382 0.0014 0.0028 -0.0181 197 PRO A C 886 O O . PRO A 117 ? 0.1011 0.1246 0.1028 0.0016 0.0024 -0.0163 197 PRO A O 887 C CB . PRO A 117 ? 0.0985 0.1260 0.0990 0.0003 0.0032 -0.0207 197 PRO A CB 888 C CG . PRO A 117 ? 0.1557 0.1858 0.1547 0.0002 0.0027 -0.0189 197 PRO A CG 889 C CD . PRO A 117 ? 0.0790 0.1075 0.0777 0.0001 0.0019 -0.0175 197 PRO A CD 890 N N . ASP A 118 ? 0.1378 0.1589 0.1413 0.0019 0.0034 -0.0192 198 ASP A N 891 C CA . ASP A 118 ? 0.1798 0.2000 0.1843 0.0027 0.0035 -0.0182 198 ASP A CA 892 C C . ASP A 118 ? 0.1759 0.1991 0.1799 0.0027 0.0037 -0.0177 198 ASP A C 893 O O . ASP A 118 ? 0.1668 0.1899 0.1712 0.0031 0.0036 -0.0163 198 ASP A O 894 C CB . ASP A 118 ? 0.1625 0.1810 0.1685 0.0034 0.0042 -0.0196 198 ASP A CB 895 C CG . ASP A 118 ? 0.2524 0.2675 0.2592 0.0036 0.0040 -0.0195 198 ASP A CG 896 O OD1 . ASP A 118 ? 0.2274 0.2416 0.2336 0.0032 0.0033 -0.0184 198 ASP A OD1 897 O OD2 . ASP A 118 ? 0.2779 0.2912 0.2859 0.0042 0.0046 -0.0205 198 ASP A OD2 898 N N . ASN A 119 ? 0.1209 0.1467 0.1240 0.0023 0.0041 -0.0188 199 ASN A N 899 C CA . ASN A 119 ? 0.1323 0.1610 0.1349 0.0023 0.0045 -0.0185 199 ASN A CA 900 C C . ASN A 119 ? 0.1736 0.2043 0.1746 0.0018 0.0040 -0.0168 199 ASN A C 901 O O . ASN A 119 ? 0.1540 0.1872 0.1544 0.0017 0.0043 -0.0164 199 ASN A O 902 C CB . ASN A 119 ? 0.1855 0.2164 0.1881 0.0022 0.0053 -0.0207 199 ASN A CB 903 C CG . ASN A 119 ? 0.2972 0.3299 0.2984 0.0014 0.0053 -0.0218 199 ASN A CG 904 O OD1 . ASN A 119 ? 0.1938 0.2262 0.1943 0.0010 0.0046 -0.0210 199 ASN A OD1 905 N ND2 . ASN A 119 ? 0.3191 0.3541 0.3202 0.0012 0.0060 -0.0238 199 ASN A ND2 906 N N . GLY A 120 ? 0.1064 0.1358 0.1068 0.0015 0.0033 -0.0157 200 GLY A N 907 C CA . GLY A 120 ? 0.1188 0.1497 0.1178 0.0012 0.0029 -0.0139 200 GLY A CA 908 C C . GLY A 120 ? 0.0993 0.1283 0.0980 0.0012 0.0022 -0.0127 200 GLY A C 909 O O . GLY A 120 ? 0.0929 0.1232 0.0904 0.0009 0.0019 -0.0121 200 GLY A O 910 N N . ALA A 121 ? 0.0869 0.1128 0.0866 0.0015 0.0019 -0.0122 201 ALA A N 911 C CA . ALA A 121 ? 0.0791 0.1029 0.0787 0.0014 0.0012 -0.0111 201 ALA A CA 912 C C . ALA A 121 ? 0.0866 0.1109 0.0851 0.0013 0.0010 -0.0090 201 ALA A C 913 O O . ALA A 121 ? 0.0776 0.1029 0.0759 0.0013 0.0013 -0.0081 201 ALA A O 914 C CB . ALA A 121 ? 0.0916 0.1123 0.0925 0.0018 0.0011 -0.0110 201 ALA A CB 915 N N . VAL A 122 ? 0.0584 0.0820 0.0563 0.0013 0.0005 -0.0082 202 VAL A N 916 C CA . VAL A 122 ? 0.0678 0.0916 0.0647 0.0013 0.0003 -0.0061 202 VAL A CA 917 C C . VAL A 122 ? 0.0824 0.1033 0.0796 0.0014 -0.0002 -0.0051 202 VAL A C 918 O O . VAL A 122 ? 0.0811 0.1010 0.0785 0.0014 -0.0006 -0.0057 202 VAL A O 919 C CB . VAL A 122 ? 0.0980 0.1245 0.0934 0.0013 0.0002 -0.0059 202 VAL A CB 920 C CG1 . VAL A 122 ? 0.0758 0.1020 0.0703 0.0015 0.0001 -0.0036 202 VAL A CG1 921 C CG2 . VAL A 122 ? 0.0593 0.0890 0.0542 0.0011 0.0008 -0.0066 202 VAL A CG2 922 N N . ALA A 123 ? 0.1045 0.1241 0.1017 0.0014 -0.0001 -0.0036 203 ALA A N 923 C CA . ALA A 123 ? 0.0938 0.1108 0.0911 0.0015 -0.0004 -0.0025 203 ALA A CA 924 C C . ALA A 123 ? 0.0740 0.0915 0.0700 0.0017 -0.0005 -0.0011 203 ALA A C 925 O O . ALA A 123 ? 0.0867 0.1055 0.0819 0.0017 -0.0001 0.0001 203 ALA A O 926 C CB . ALA A 123 ? 0.0805 0.0958 0.0783 0.0014 -0.0002 -0.0017 203 ALA A CB 927 N N . VAL A 124 ? 0.0592 0.0759 0.0552 0.0018 -0.0010 -0.0011 204 VAL A N 928 C CA . VAL A 124 ? 0.0643 0.0815 0.0593 0.0022 -0.0011 0.0003 204 VAL A CA 929 C C . VAL A 124 ? 0.0673 0.0816 0.0624 0.0023 -0.0012 0.0016 204 VAL A C 930 O O . VAL A 124 ? 0.0614 0.0737 0.0573 0.0022 -0.0016 0.0010 204 VAL A O 931 C CB . VAL A 124 ? 0.0416 0.0602 0.0363 0.0022 -0.0016 -0.0006 204 VAL A CB 932 C CG1 . VAL A 124 ? 0.0943 0.1134 0.0881 0.0027 -0.0018 0.0009 204 VAL A CG1 933 C CG2 . VAL A 124 ? 0.0572 0.0789 0.0516 0.0020 -0.0015 -0.0020 204 VAL A CG2 934 N N . LEU A 125 ? 0.0531 0.0670 0.0475 0.0024 -0.0008 0.0033 205 LEU A N 935 C CA . LEU A 125 ? 0.0680 0.0791 0.0624 0.0025 -0.0007 0.0045 205 LEU A CA 936 C C . LEU A 125 ? 0.0860 0.0971 0.0797 0.0031 -0.0008 0.0055 205 LEU A C 937 O O . LEU A 125 ? 0.0798 0.0930 0.0726 0.0036 -0.0006 0.0064 205 LEU A O 938 C CB . LEU A 125 ? 0.0772 0.0875 0.0714 0.0022 0.0001 0.0056 205 LEU A CB 939 C CG . LEU A 125 ? 0.0906 0.1004 0.0857 0.0016 0.0003 0.0048 205 LEU A CG 940 C CD1 . LEU A 125 ? 0.1367 0.1492 0.1319 0.0015 0.0003 0.0036 205 LEU A CD1 941 C CD2 . LEU A 125 ? 0.1151 0.1238 0.1100 0.0012 0.0010 0.0060 205 LEU A CD2 942 N N . LYS A 126 ? 0.0686 0.0776 0.0627 0.0032 -0.0012 0.0055 206 LYS A N 943 C CA . LYS A 126 ? 0.0643 0.0731 0.0579 0.0038 -0.0013 0.0066 206 LYS A CA 944 C C . LYS A 126 ? 0.0659 0.0716 0.0595 0.0039 -0.0009 0.0077 206 LYS A C 945 O O . LYS A 126 ? 0.0686 0.0723 0.0630 0.0033 -0.0010 0.0071 206 LYS A O 946 C CB . LYS A 126 ? 0.0703 0.0797 0.0643 0.0038 -0.0020 0.0054 206 LYS A CB 947 C CG . LYS A 126 ? 0.1004 0.1131 0.0943 0.0038 -0.0023 0.0042 206 LYS A CG 948 C CD . LYS A 126 ? 0.1291 0.1420 0.1235 0.0036 -0.0029 0.0030 206 LYS A CD 949 C CE . LYS A 126 ? 0.1131 0.1291 0.1074 0.0033 -0.0031 0.0016 206 LYS A CE 950 N NZ . LYS A 126 ? 0.1215 0.1377 0.1164 0.0031 -0.0036 0.0004 206 LYS A NZ 951 N N . TYR A 127 ? 0.0681 0.0736 0.0609 0.0046 -0.0005 0.0093 207 TYR A N 952 C CA . TYR A 127 ? 0.0466 0.0492 0.0394 0.0047 -0.0001 0.0103 207 TYR A CA 953 C C . TYR A 127 ? 0.0784 0.0812 0.0710 0.0056 -0.0003 0.0110 207 TYR A C 954 O O . TYR A 127 ? 0.0794 0.0843 0.0712 0.0064 -0.0002 0.0120 207 TYR A O 955 C CB . TYR A 127 ? 0.0674 0.0691 0.0596 0.0047 0.0009 0.0119 207 TYR A CB 956 C CG . TYR A 127 ? 0.1075 0.1057 0.0998 0.0046 0.0016 0.0126 207 TYR A CG 957 C CD1 . TYR A 127 ? 0.1281 0.1243 0.1211 0.0036 0.0016 0.0116 207 TYR A CD1 958 C CD2 . TYR A 127 ? 0.1315 0.1285 0.1231 0.0054 0.0023 0.0144 207 TYR A CD2 959 C CE1 . TYR A 127 ? 0.0994 0.0926 0.0924 0.0033 0.0022 0.0121 207 TYR A CE1 960 C CE2 . TYR A 127 ? 0.1224 0.1161 0.1140 0.0052 0.0031 0.0149 207 TYR A CE2 961 C CZ . TYR A 127 ? 0.1104 0.1022 0.1027 0.0041 0.0030 0.0137 207 TYR A CZ 962 O OH . TYR A 127 ? 0.1264 0.1151 0.1188 0.0037 0.0038 0.0141 207 TYR A OH 963 N N . ASN A 128 ? 0.0711 0.0721 0.0643 0.0054 -0.0007 0.0104 208 ASN A N 964 C CA . ASN A 128 ? 0.1145 0.1159 0.1075 0.0062 -0.0010 0.0108 208 ASN A CA 965 C C . ASN A 128 ? 0.0803 0.0852 0.0733 0.0064 -0.0017 0.0101 208 ASN A C 966 O O . ASN A 128 ? 0.1047 0.1113 0.0973 0.0072 -0.0018 0.0108 208 ASN A O 967 C CB . ASN A 128 ? 0.1421 0.1426 0.1344 0.0072 -0.0002 0.0127 208 ASN A CB 968 C CG . ASN A 128 ? 0.2087 0.2091 0.2012 0.0079 -0.0005 0.0130 208 ASN A CG 969 O OD1 . ASN A 128 ? 0.1679 0.1678 0.1610 0.0075 -0.0011 0.0119 208 ASN A OD1 970 N ND2 . ASN A 128 ? 0.2664 0.2672 0.2582 0.0091 0.0000 0.0147 208 ASN A ND2 971 N N . GLY A 129 ? 0.1198 0.1258 0.1133 0.0056 -0.0021 0.0085 209 GLY A N 972 C CA . GLY A 129 ? 0.1563 0.1654 0.1498 0.0056 -0.0027 0.0075 209 GLY A CA 973 C C . GLY A 129 ? 0.1523 0.1646 0.1449 0.0060 -0.0025 0.0080 209 GLY A C 974 O O . GLY A 129 ? 0.1579 0.1731 0.1505 0.0059 -0.0030 0.0071 209 GLY A O 975 N N . ILE A 130 ? 0.0517 0.0636 0.0437 0.0063 -0.0019 0.0094 210 ILE A N 976 C CA . ILE A 130 ? 0.0736 0.0886 0.0647 0.0068 -0.0016 0.0102 210 ILE A CA 977 C C . ILE A 130 ? 0.0796 0.0947 0.0708 0.0061 -0.0013 0.0096 210 ILE A C 978 O O . ILE A 130 ? 0.0784 0.0908 0.0698 0.0057 -0.0008 0.0099 210 ILE A O 979 C CB . ILE A 130 ? 0.1320 0.1466 0.1222 0.0079 -0.0010 0.0126 210 ILE A CB 980 C CG1 . ILE A 130 ? 0.1320 0.1467 0.1223 0.0087 -0.0012 0.0132 210 ILE A CG1 981 C CG2 . ILE A 130 ? 0.0987 0.1167 0.0879 0.0084 -0.0007 0.0135 210 ILE A CG2 982 C CD1 . ILE A 130 ? 0.1294 0.1481 0.1196 0.0090 -0.0020 0.0125 210 ILE A CD1 983 N N . ILE A 131 ? 0.0736 0.0919 0.0644 0.0059 -0.0015 0.0087 211 ILE A N 984 C CA . ILE A 131 ? 0.0933 0.1119 0.0841 0.0053 -0.0011 0.0081 211 ILE A CA 985 C C . ILE A 131 ? 0.0868 0.1048 0.0769 0.0056 -0.0003 0.0101 211 ILE A C 986 O O . ILE A 131 ? 0.1257 0.1453 0.1148 0.0064 0.0000 0.0117 211 ILE A O 987 C CB . ILE A 131 ? 0.0952 0.1177 0.0858 0.0050 -0.0014 0.0068 211 ILE A CB 988 C CG1 . ILE A 131 ? 0.0343 0.0569 0.0257 0.0044 -0.0021 0.0046 211 ILE A CG1 989 C CG2 . ILE A 131 ? 0.0772 0.1002 0.0677 0.0045 -0.0009 0.0064 211 ILE A CG2 990 C CD1 . ILE A 131 ? 0.1105 0.1367 0.1018 0.0040 -0.0022 0.0030 211 ILE A CD1 991 N N . THR A 132 ? 0.0754 0.0911 0.0659 0.0050 0.0001 0.0100 212 THR A N 992 C CA . THR A 132 ? 0.1006 0.1151 0.0906 0.0051 0.0011 0.0117 212 THR A CA 993 C C . THR A 132 ? 0.1341 0.1496 0.1240 0.0045 0.0015 0.0113 212 THR A C 994 O O . THR A 132 ? 0.1363 0.1519 0.1256 0.0045 0.0023 0.0127 212 THR A O 995 C CB . THR A 132 ? 0.0890 0.0994 0.0794 0.0049 0.0014 0.0123 212 THR A CB 996 O OG1 . THR A 132 ? 0.0858 0.0949 0.0774 0.0041 0.0009 0.0106 212 THR A OG1 997 C CG2 . THR A 132 ? 0.1214 0.1308 0.1115 0.0058 0.0014 0.0134 212 THR A CG2 998 N N . ASP A 133 ? 0.1099 0.1265 0.1006 0.0038 0.0010 0.0093 213 ASP A N 999 C CA . ASP A 133 ? 0.0955 0.1132 0.0864 0.0033 0.0014 0.0087 213 ASP A CA 1000 C C . ASP A 133 ? 0.1068 0.1258 0.0985 0.0028 0.0009 0.0064 213 ASP A C 1001 O O . ASP A 133 ? 0.0808 0.0990 0.0731 0.0029 0.0002 0.0053 213 ASP A O 1002 C CB . ASP A 133 ? 0.1252 0.1401 0.1165 0.0027 0.0020 0.0092 213 ASP A CB 1003 C CG . ASP A 133 ? 0.1650 0.1811 0.1559 0.0023 0.0029 0.0098 213 ASP A CG 1004 O OD1 . ASP A 133 ? 0.1590 0.1782 0.1493 0.0025 0.0029 0.0095 213 ASP A OD1 1005 O OD2 . ASP A 133 ? 0.1871 0.2012 0.1782 0.0018 0.0035 0.0106 213 ASP A OD2 1006 N N . THR A 134 ? 0.0798 0.1006 0.0715 0.0025 0.0012 0.0057 214 THR A N 1007 C CA . THR A 134 ? 0.1037 0.1254 0.0964 0.0021 0.0009 0.0036 214 THR A CA 1008 C C . THR A 134 ? 0.1184 0.1402 0.1116 0.0016 0.0014 0.0033 214 THR A C 1009 O O . THR A 134 ? 0.1513 0.1733 0.1438 0.0015 0.0021 0.0046 214 THR A O 1010 C CB . THR A 134 ? 0.1260 0.1511 0.1181 0.0023 0.0007 0.0024 214 THR A CB 1011 O OG1 . THR A 134 ? 0.1221 0.1498 0.1131 0.0023 0.0012 0.0033 214 THR A OG1 1012 C CG2 . THR A 134 ? 0.1028 0.1284 0.0943 0.0027 0.0001 0.0027 214 THR A CG2 1013 N N . ILE A 135 ? 0.0918 0.1133 0.0861 0.0014 0.0012 0.0016 215 ILE A N 1014 C CA . ILE A 135 ? 0.1320 0.1542 0.1268 0.0010 0.0017 0.0011 215 ILE A CA 1015 C C . ILE A 135 ? 0.1287 0.1522 0.1243 0.0010 0.0016 -0.0010 215 ILE A C 1016 O O . ILE A 135 ? 0.1372 0.1595 0.1337 0.0011 0.0011 -0.0021 215 ILE A O 1017 C CB . ILE A 135 ? 0.1876 0.2073 0.1834 0.0006 0.0019 0.0016 215 ILE A CB 1018 C CG1 . ILE A 135 ? 0.2028 0.2237 0.1993 0.0002 0.0024 0.0011 215 ILE A CG1 1019 C CG2 . ILE A 135 ? 0.1754 0.1929 0.1722 0.0007 0.0012 0.0008 215 ILE A CG2 1020 C CD1 . ILE A 135 ? 0.2029 0.2239 0.2007 0.0003 0.0021 -0.0007 215 ILE A CD1 1021 N N . LYS A 136 ? 0.1058 0.1320 0.1012 0.0009 0.0020 -0.0016 216 LYS A N 1022 C CA . LYS A 136 ? 0.1152 0.1428 0.1112 0.0010 0.0020 -0.0037 216 LYS A CA 1023 C C . LYS A 136 ? 0.0895 0.1168 0.0868 0.0009 0.0024 -0.0045 216 LYS A C 1024 O O . LYS A 136 ? 0.1131 0.1403 0.1105 0.0007 0.0028 -0.0035 216 LYS A O 1025 C CB . LYS A 136 ? 0.1520 0.1830 0.1468 0.0010 0.0023 -0.0041 216 LYS A CB 1026 C CG . LYS A 136 ? 0.1098 0.1423 0.1052 0.0010 0.0024 -0.0064 216 LYS A CG 1027 C CD . LYS A 136 ? 0.1557 0.1918 0.1498 0.0009 0.0026 -0.0069 216 LYS A CD 1028 C CE . LYS A 136 ? 0.1896 0.2269 0.1842 0.0008 0.0027 -0.0095 216 LYS A CE 1029 N NZ . LYS A 136 ? 0.3024 0.3435 0.2956 0.0006 0.0028 -0.0101 216 LYS A NZ 1030 N N . SER A 137 ? 0.1080 0.1350 0.1063 0.0011 0.0023 -0.0063 217 SER A N 1031 C CA . SER A 137 ? 0.0837 0.1108 0.0835 0.0013 0.0026 -0.0072 217 SER A CA 1032 C C . SER A 137 ? 0.1437 0.1732 0.1431 0.0011 0.0033 -0.0070 217 SER A C 1033 O O . SER A 137 ? 0.0959 0.1279 0.0943 0.0009 0.0036 -0.0072 217 SER A O 1034 C CB . SER A 137 ? 0.0837 0.1109 0.0842 0.0016 0.0027 -0.0093 217 SER A CB 1035 O OG . SER A 137 ? 0.0958 0.1229 0.0976 0.0020 0.0031 -0.0102 217 SER A OG 1036 N N . TRP A 138 ? 0.0866 0.1158 0.0869 0.0010 0.0035 -0.0065 218 TRP A N 1037 C CA . TRP A 138 ? 0.1057 0.1373 0.1059 0.0007 0.0042 -0.0062 218 TRP A CA 1038 C C . TRP A 138 ? 0.1171 0.1500 0.1187 0.0010 0.0046 -0.0077 218 TRP A C 1039 O O . TRP A 138 ? 0.1476 0.1828 0.1492 0.0009 0.0053 -0.0079 218 TRP A O 1040 C CB . TRP A 138 ? 0.1057 0.1365 0.1059 0.0001 0.0044 -0.0044 218 TRP A CB 1041 C CG . TRP A 138 ? 0.1230 0.1519 0.1246 0.0001 0.0041 -0.0044 218 TRP A CG 1042 C CD1 . TRP A 138 ? 0.1015 0.1314 0.1044 0.0001 0.0044 -0.0048 218 TRP A CD1 1043 C CD2 . TRP A 138 ? 0.1182 0.1443 0.1200 0.0002 0.0034 -0.0039 218 TRP A CD2 1044 N NE1 . TRP A 138 ? 0.1309 0.1589 0.1348 0.0001 0.0039 -0.0046 218 TRP A NE1 1045 C CE2 . TRP A 138 ? 0.1192 0.1448 0.1224 0.0001 0.0034 -0.0040 218 TRP A CE2 1046 C CE3 . TRP A 138 ? 0.1342 0.1584 0.1352 0.0002 0.0029 -0.0033 218 TRP A CE3 1047 C CZ2 . TRP A 138 ? 0.1346 0.1578 0.1384 0.0002 0.0028 -0.0037 218 TRP A CZ2 1048 C CZ3 . TRP A 138 ? 0.1315 0.1532 0.1331 0.0002 0.0024 -0.0030 218 TRP A CZ3 1049 C CH2 . TRP A 138 ? 0.0912 0.1124 0.0940 0.0002 0.0023 -0.0031 218 TRP A CH2 1050 N N . ARG A 139 ? 0.1153 0.1466 0.1181 0.0016 0.0043 -0.0088 219 ARG A N 1051 C CA . ARG A 139 ? 0.1423 0.1745 0.1464 0.0022 0.0047 -0.0103 219 ARG A CA 1052 C C . ARG A 139 ? 0.1283 0.1603 0.1326 0.0027 0.0048 -0.0122 219 ARG A C 1053 O O . ARG A 139 ? 0.1419 0.1743 0.1472 0.0033 0.0053 -0.0136 219 ARG A O 1054 C CB . ARG A 139 ? 0.1055 0.1361 0.1112 0.0026 0.0045 -0.0100 219 ARG A CB 1055 C CG . ARG A 139 ? 0.1453 0.1768 0.1513 0.0020 0.0046 -0.0087 219 ARG A CG 1056 C CD . ARG A 139 ? 0.2792 0.3138 0.2854 0.0019 0.0054 -0.0091 219 ARG A CD 1057 N NE . ARG A 139 ? 0.2697 0.3051 0.2762 0.0013 0.0055 -0.0079 219 ARG A NE 1058 C CZ . ARG A 139 ? 0.3499 0.3859 0.3580 0.0015 0.0056 -0.0081 219 ARG A CZ 1059 N NH1 . ARG A 139 ? 0.3710 0.4068 0.3805 0.0026 0.0055 -0.0092 219 ARG A NH1 1060 N NH2 . ARG A 139 ? 0.3455 0.3825 0.3539 0.0007 0.0058 -0.0071 219 ARG A NH2 1061 N N . ASN A 140 ? 0.1263 0.1575 0.1294 0.0024 0.0044 -0.0122 220 ASN A N 1062 C CA . ASN A 140 ? 0.1601 0.1912 0.1632 0.0026 0.0045 -0.0140 220 ASN A CA 1063 C C . ASN A 140 ? 0.1446 0.1732 0.1492 0.0033 0.0046 -0.0150 220 ASN A C 1064 O O . ASN A 140 ? 0.1272 0.1561 0.1324 0.0036 0.0051 -0.0169 220 ASN A O 1065 C CB . ASN A 140 ? 0.1513 0.1854 0.1539 0.0025 0.0053 -0.0153 220 ASN A CB 1066 C CG . ASN A 140 ? 0.2324 0.2690 0.2333 0.0019 0.0053 -0.0142 220 ASN A CG 1067 O OD1 . ASN A 140 ? 0.2416 0.2774 0.2416 0.0016 0.0048 -0.0126 220 ASN A OD1 1068 N ND2 . ASN A 140 ? 0.3623 0.4020 0.3627 0.0018 0.0060 -0.0151 220 ASN A ND2 1069 N N . ASN A 141 ? 0.1258 0.1522 0.1312 0.0035 0.0041 -0.0139 221 ASN A N 1070 C CA . ASN A 141 ? 0.0973 0.1216 0.1042 0.0043 0.0041 -0.0145 221 ASN A CA 1071 C C . ASN A 141 ? 0.1207 0.1422 0.1277 0.0043 0.0033 -0.0134 221 ASN A C 1072 O O . ASN A 141 ? 0.1024 0.1232 0.1102 0.0046 0.0031 -0.0123 221 ASN A O 1073 C CB . ASN A 141 ? 0.1406 0.1657 0.1488 0.0050 0.0046 -0.0146 221 ASN A CB 1074 C CG . ASN A 141 ? 0.2161 0.2394 0.2259 0.0060 0.0048 -0.0155 221 ASN A CG 1075 O OD1 . ASN A 141 ? 0.1721 0.1932 0.1820 0.0061 0.0047 -0.0161 221 ASN A OD1 1076 N ND2 . ASN A 141 ? 0.1989 0.2232 0.2101 0.0068 0.0052 -0.0155 221 ASN A ND2 1077 N N . ILE A 142 ? 0.1214 0.1418 0.1275 0.0039 0.0030 -0.0136 222 ILE A N 1078 C CA . ILE A 142 ? 0.0933 0.1111 0.0995 0.0038 0.0023 -0.0127 222 ILE A CA 1079 C C . ILE A 142 ? 0.1016 0.1192 0.1074 0.0035 0.0018 -0.0108 222 ILE A C 1080 O O . ILE A 142 ? 0.1152 0.1316 0.1218 0.0038 0.0016 -0.0100 222 ILE A O 1081 C CB . ILE A 142 ? 0.0931 0.1086 0.1007 0.0046 0.0024 -0.0132 222 ILE A CB 1082 C CG1 . ILE A 142 ? 0.1621 0.1776 0.1703 0.0050 0.0032 -0.0152 222 ILE A CG1 1083 C CG2 . ILE A 142 ? 0.1179 0.1309 0.1255 0.0045 0.0018 -0.0125 222 ILE A CG2 1084 C CD1 . ILE A 142 ? 0.1707 0.1838 0.1804 0.0059 0.0035 -0.0156 222 ILE A CD1 1085 N N . LEU A 143 ? 0.0764 0.0951 0.0809 0.0029 0.0016 -0.0100 223 LEU A N 1086 C CA . LEU A 143 ? 0.0949 0.1128 0.0988 0.0025 0.0012 -0.0083 223 LEU A CA 1087 C C . LEU A 143 ? 0.0812 0.0965 0.0854 0.0026 0.0006 -0.0078 223 LEU A C 1088 O O . LEU A 143 ? 0.0724 0.0867 0.0764 0.0027 0.0004 -0.0085 223 LEU A O 1089 C CB . LEU A 143 ? 0.0886 0.1078 0.0909 0.0020 0.0012 -0.0075 223 LEU A CB 1090 C CG . LEU A 143 ? 0.1100 0.1282 0.1116 0.0016 0.0009 -0.0057 223 LEU A CG 1091 C CD1 . LEU A 143 ? 0.0606 0.0792 0.0627 0.0014 0.0012 -0.0049 223 LEU A CD1 1092 C CD2 . LEU A 143 ? 0.1078 0.1271 0.1079 0.0014 0.0009 -0.0050 223 LEU A CD2 1093 N N . ARG A 144 ? 0.0545 0.0687 0.0593 0.0026 0.0004 -0.0068 224 ARG A N 1094 C CA . ARG A 144 ? 0.1016 0.1134 0.1067 0.0028 -0.0002 -0.0064 224 ARG A CA 1095 C C . ARG A 144 ? 0.0820 0.0931 0.0870 0.0024 -0.0005 -0.0050 224 ARG A C 1096 O O . ARG A 144 ? 0.0839 0.0962 0.0890 0.0021 -0.0002 -0.0045 224 ARG A O 1097 C CB . ARG A 144 ? 0.1163 0.1274 0.1228 0.0035 -0.0001 -0.0073 224 ARG A CB 1098 C CG . ARG A 144 ? 0.0830 0.0955 0.0905 0.0039 0.0003 -0.0074 224 ARG A CG 1099 C CD . ARG A 144 ? 0.0963 0.1083 0.1051 0.0049 0.0006 -0.0085 224 ARG A CD 1100 N NE . ARG A 144 ? 0.0871 0.1005 0.0971 0.0054 0.0009 -0.0084 224 ARG A NE 1101 C CZ . ARG A 144 ? 0.1415 0.1571 0.1519 0.0056 0.0015 -0.0091 224 ARG A CZ 1102 N NH1 . ARG A 144 ? 0.0957 0.1123 0.1051 0.0052 0.0018 -0.0099 224 ARG A NH1 1103 N NH2 . ARG A 144 ? 0.1197 0.1366 0.1312 0.0061 0.0017 -0.0090 224 ARG A NH2 1104 N N . THR A 145 ? 0.0963 0.1054 0.1011 0.0024 -0.0009 -0.0045 225 THR A N 1105 C CA . THR A 145 ? 0.0610 0.0693 0.0656 0.0019 -0.0012 -0.0033 225 THR A CA 1106 C C . THR A 145 ? 0.0782 0.0848 0.0835 0.0021 -0.0016 -0.0031 225 THR A C 1107 O O . THR A 145 ? 0.0767 0.0831 0.0829 0.0028 -0.0017 -0.0037 225 THR A O 1108 C CB . THR A 145 ? 0.0646 0.0724 0.0678 0.0015 -0.0012 -0.0025 225 THR A CB 1109 O OG1 . THR A 145 ? 0.1030 0.1100 0.1060 0.0009 -0.0012 -0.0014 225 THR A OG1 1110 C CG2 . THR A 145 ? 0.0750 0.0815 0.0778 0.0017 -0.0016 -0.0027 225 THR A CG2 1111 N N . GLN A 146 ? 0.0851 0.0906 0.0899 0.0017 -0.0019 -0.0022 226 GLN A N 1112 C CA . GLN A 146 ? 0.0877 0.0921 0.0931 0.0017 -0.0023 -0.0019 226 GLN A CA 1113 C C . GLN A 146 ? 0.0893 0.0923 0.0951 0.0023 -0.0027 -0.0022 226 GLN A C 1114 O O . GLN A 146 ? 0.0851 0.0880 0.0918 0.0027 -0.0028 -0.0022 226 GLN A O 1115 C CB . GLN A 146 ? 0.0833 0.0867 0.0879 0.0010 -0.0024 -0.0010 226 GLN A CB 1116 C CG . GLN A 146 ? 0.0745 0.0789 0.0789 0.0003 -0.0020 -0.0005 226 GLN A CG 1117 C CD . GLN A 146 ? 0.1201 0.1230 0.1238 -0.0004 -0.0019 0.0003 226 GLN A CD 1118 O OE1 . GLN A 146 ? 0.1835 0.1859 0.1862 -0.0007 -0.0016 0.0008 226 GLN A OE1 1119 N NE2 . GLN A 146 ? 0.0946 0.0969 0.0987 -0.0006 -0.0023 0.0003 226 GLN A NE2 1120 N N . GLU A 147 ? 0.0819 0.0839 0.0870 0.0023 -0.0027 -0.0024 227 GLU A N 1121 C CA . GLU A 147 ? 0.0746 0.0750 0.0799 0.0027 -0.0030 -0.0025 227 GLU A CA 1122 C C . GLU A 147 ? 0.1116 0.1108 0.1168 0.0024 -0.0034 -0.0017 227 GLU A C 1123 O O . GLU A 147 ? 0.1238 0.1219 0.1294 0.0027 -0.0037 -0.0016 227 GLU A O 1124 C CB . GLU A 147 ? 0.1521 0.1524 0.1585 0.0034 -0.0029 -0.0032 227 GLU A CB 1125 C CG . GLU A 147 ? 0.1455 0.1473 0.1524 0.0037 -0.0024 -0.0041 227 GLU A CG 1126 C CD . GLU A 147 ? 0.1929 0.1951 0.1990 0.0034 -0.0022 -0.0048 227 GLU A CD 1127 O OE1 . GLU A 147 ? 0.1656 0.1672 0.1709 0.0030 -0.0024 -0.0046 227 GLU A OE1 1128 O OE2 . GLU A 147 ? 0.2029 0.2065 0.2092 0.0035 -0.0017 -0.0056 227 GLU A OE2 1129 N N . SER A 148 ? 0.0891 0.0886 0.0938 0.0018 -0.0034 -0.0010 228 SER A N 1130 C CA . SER A 148 ? 0.1051 0.1035 0.1094 0.0015 -0.0037 -0.0004 228 SER A CA 1131 C C . SER A 148 ? 0.1051 0.1034 0.1084 0.0008 -0.0034 0.0002 228 SER A C 1132 O O . SER A 148 ? 0.1323 0.1314 0.1352 0.0008 -0.0030 0.0001 228 SER A O 1133 C CB . SER A 148 ? 0.1309 0.1296 0.1359 0.0014 -0.0039 -0.0002 228 SER A CB 1134 O OG . SER A 148 ? 0.1260 0.1264 0.1314 0.0011 -0.0036 -0.0003 228 SER A OG 1135 N N . GLU A 149 ? 0.0785 0.0757 0.0814 0.0004 -0.0035 0.0007 229 GLU A N 1136 C CA . GLU A 149 ? 0.0846 0.0810 0.0865 0.0000 -0.0031 0.0013 229 GLU A CA 1137 C C . GLU A 149 ? 0.0879 0.0853 0.0898 -0.0006 -0.0026 0.0015 229 GLU A C 1138 O O . GLU A 149 ? 0.1070 0.1054 0.1096 -0.0009 -0.0026 0.0013 229 GLU A O 1139 C CB . GLU A 149 ? 0.0754 0.0703 0.0770 -0.0004 -0.0032 0.0017 229 GLU A CB 1140 C CG . GLU A 149 ? 0.1082 0.1032 0.1102 -0.0010 -0.0031 0.0017 229 GLU A CG 1141 C CD . GLU A 149 ? 0.1780 0.1714 0.1795 -0.0015 -0.0031 0.0020 229 GLU A CD 1142 O OE1 . GLU A 149 ? 0.1393 0.1315 0.1401 -0.0012 -0.0030 0.0023 229 GLU A OE1 1143 O OE2 . GLU A 149 ? 0.1295 0.1230 0.1311 -0.0021 -0.0030 0.0018 229 GLU A OE2 1144 N N . CYS A 150 ? 0.0934 0.0908 0.0945 -0.0007 -0.0021 0.0020 230 CYS A N 1145 C CA . CYS A 150 ? 0.1321 0.1300 0.1330 -0.0014 -0.0014 0.0024 230 CYS A CA 1146 C C . CYS A 150 ? 0.1555 0.1518 0.1562 -0.0021 -0.0012 0.0028 230 CYS A C 1147 O O . CYS A 150 ? 0.1303 0.1253 0.1309 -0.0020 -0.0015 0.0028 230 CYS A O 1148 C CB . CYS A 150 ? 0.1289 0.1273 0.1291 -0.0012 -0.0010 0.0029 230 CYS A CB 1149 S SG . CYS A 150 ? 0.1701 0.1677 0.1694 -0.0004 -0.0012 0.0034 230 CYS A SG 1150 N N . ALA A 151 ? 0.1030 0.0996 0.1037 -0.0029 -0.0005 0.0030 231 ALA A N 1151 C CA . ALA A 151 ? 0.1087 0.1038 0.1092 -0.0038 -0.0001 0.0031 231 ALA A CA 1152 C C . ALA A 151 ? 0.1220 0.1157 0.1216 -0.0042 0.0008 0.0040 231 ALA A C 1153 O O . ALA A 151 ? 0.0717 0.0662 0.0711 -0.0043 0.0013 0.0044 231 ALA A O 1154 C CB . ALA A 151 ? 0.1440 0.1406 0.1454 -0.0047 -0.0001 0.0025 231 ALA A CB 1155 N N . CYS A 152 ? 0.1235 0.1150 0.1226 -0.0045 0.0011 0.0043 232 CYS A N 1156 C CA . CYS A 152 ? 0.1107 0.1003 0.1089 -0.0046 0.0021 0.0053 232 CYS A CA 1157 C C . CYS A 152 ? 0.1325 0.1205 0.1307 -0.0059 0.0030 0.0052 232 CYS A C 1158 O O . CYS A 152 ? 0.1596 0.1471 0.1581 -0.0064 0.0027 0.0045 232 CYS A O 1159 C CB . CYS A 152 ? 0.1554 0.1436 0.1529 -0.0035 0.0020 0.0060 232 CYS A CB 1160 S SG . CYS A 152 ? 0.2452 0.2354 0.2426 -0.0022 0.0012 0.0061 232 CYS A SG 1161 N N . VAL A 153 ? 0.0937 0.0810 0.0915 -0.0064 0.0041 0.0059 233 VAL A N 1162 C CA . VAL A 153 ? 0.1427 0.1281 0.1404 -0.0077 0.0052 0.0058 233 VAL A CA 1163 C C . VAL A 153 ? 0.1793 0.1625 0.1760 -0.0075 0.0064 0.0071 233 VAL A C 1164 O O . VAL A 153 ? 0.1013 0.0856 0.0979 -0.0073 0.0068 0.0079 233 VAL A O 1165 C CB . VAL A 153 ? 0.1777 0.1649 0.1762 -0.0091 0.0054 0.0050 233 VAL A CB 1166 C CG1 . VAL A 153 ? 0.1465 0.1316 0.1447 -0.0106 0.0067 0.0049 233 VAL A CG1 1167 C CG2 . VAL A 153 ? 0.1222 0.1115 0.1216 -0.0093 0.0043 0.0038 233 VAL A CG2 1168 N N . ASN A 154 ? 0.1113 0.0917 0.1076 -0.0075 0.0071 0.0075 234 ASN A N 1169 C CA . ASN A 154 ? 0.1684 0.1464 0.1639 -0.0072 0.0085 0.0089 234 ASN A CA 1170 C C . ASN A 154 ? 0.1327 0.1116 0.1275 -0.0058 0.0084 0.0103 234 ASN A C 1171 O O . ASN A 154 ? 0.1217 0.1003 0.1161 -0.0060 0.0094 0.0113 234 ASN A O 1172 C CB . ASN A 154 ? 0.1728 0.1495 0.1683 -0.0089 0.0098 0.0088 234 ASN A CB 1173 C CG . ASN A 154 ? 0.1725 0.1457 0.1672 -0.0087 0.0115 0.0101 234 ASN A CG 1174 O OD1 . ASN A 154 ? 0.3407 0.3119 0.3350 -0.0078 0.0116 0.0105 234 ASN A OD1 1175 N ND2 . ASN A 154 ? 0.2250 0.1976 0.2195 -0.0096 0.0127 0.0107 234 ASN A ND2 1176 N N . GLY A 155 ? 0.1297 0.1100 0.1244 -0.0045 0.0073 0.0104 235 GLY A N 1177 C CA . GLY A 155 ? 0.1766 0.1581 0.1707 -0.0031 0.0072 0.0117 235 GLY A CA 1178 C C . GLY A 155 ? 0.1781 0.1627 0.1724 -0.0031 0.0066 0.0114 235 GLY A C 1179 O O . GLY A 155 ? 0.1806 0.1668 0.1744 -0.0020 0.0064 0.0122 235 GLY A O 1180 N N . SER A 156 ? 0.0964 0.0823 0.0916 -0.0042 0.0063 0.0102 236 SER A N 1181 C CA . SER A 156 ? 0.1280 0.1170 0.1236 -0.0041 0.0057 0.0097 236 SER A CA 1182 C C . SER A 156 ? 0.1604 0.1508 0.1568 -0.0041 0.0044 0.0083 236 SER A C 1183 O O . SER A 156 ? 0.1172 0.1068 0.1141 -0.0048 0.0042 0.0074 236 SER A O 1184 C CB . SER A 156 ? 0.1628 0.1523 0.1586 -0.0054 0.0066 0.0097 236 SER A CB 1185 O OG . SER A 156 ? 0.2133 0.2013 0.2083 -0.0055 0.0079 0.0111 236 SER A OG 1186 N N . CYS A 157 ? 0.1078 0.1004 0.1043 -0.0033 0.0036 0.0080 237 CYS A N 1187 C CA . CYS A 157 ? 0.1211 0.1152 0.1185 -0.0031 0.0026 0.0067 237 CYS A CA 1188 C C . CYS A 157 ? 0.0922 0.0888 0.0902 -0.0033 0.0024 0.0061 237 CYS A C 1189 O O . CYS A 157 ? 0.1226 0.1204 0.1202 -0.0032 0.0029 0.0066 237 CYS A O 1190 C CB . CYS A 157 ? 0.1403 0.1345 0.1374 -0.0020 0.0018 0.0067 237 CYS A CB 1191 S SG . CYS A 157 ? 0.2491 0.2407 0.2457 -0.0016 0.0018 0.0073 237 CYS A SG 1192 N N . PHE A 158 ? 0.0785 0.0761 0.0775 -0.0036 0.0018 0.0050 238 PHE A N 1193 C CA . PHE A 158 ? 0.0989 0.0988 0.0986 -0.0039 0.0018 0.0043 238 PHE A CA 1194 C C . PHE A 158 ? 0.0986 0.0999 0.0991 -0.0031 0.0009 0.0034 238 PHE A C 1195 O O . PHE A 158 ? 0.1122 0.1126 0.1130 -0.0028 0.0002 0.0030 238 PHE A O 1196 C CB . PHE A 158 ? 0.0917 0.0918 0.0921 -0.0051 0.0022 0.0040 238 PHE A CB 1197 C CG . PHE A 158 ? 0.0817 0.0801 0.0814 -0.0060 0.0032 0.0048 238 PHE A CG 1198 C CD1 . PHE A 158 ? 0.0885 0.0843 0.0878 -0.0063 0.0035 0.0051 238 PHE A CD1 1199 C CD2 . PHE A 158 ? 0.0754 0.0747 0.0749 -0.0066 0.0041 0.0053 238 PHE A CD2 1200 C CE1 . PHE A 158 ? 0.0835 0.0774 0.0822 -0.0072 0.0046 0.0059 238 PHE A CE1 1201 C CE2 . PHE A 158 ? 0.1102 0.1076 0.1091 -0.0075 0.0052 0.0061 238 PHE A CE2 1202 C CZ . PHE A 158 ? 0.0954 0.0901 0.0939 -0.0077 0.0055 0.0064 238 PHE A CZ 1203 N N . THR A 159 ? 0.0923 0.0957 0.0931 -0.0028 0.0009 0.0029 239 THR A N 1204 C CA . THR A 159 ? 0.0859 0.0905 0.0875 -0.0021 0.0002 0.0020 239 THR A CA 1205 C C . THR A 159 ? 0.1152 0.1222 0.1175 -0.0021 0.0004 0.0014 239 THR A C 1206 O O . THR A 159 ? 0.1185 0.1264 0.1205 -0.0027 0.0011 0.0018 239 THR A O 1207 C CB . THR A 159 ? 0.1570 0.1613 0.1580 -0.0012 -0.0002 0.0019 239 THR A CB 1208 O OG1 . THR A 159 ? 0.1533 0.1582 0.1552 -0.0006 -0.0008 0.0009 239 THR A OG1 1209 C CG2 . THR A 159 ? 0.1365 0.1424 0.1368 -0.0010 0.0003 0.0022 239 THR A CG2 1210 N N . VAL A 160 ? 0.1356 0.1435 0.1388 -0.0015 -0.0001 0.0005 240 VAL A N 1211 C CA . VAL A 160 ? 0.1089 0.1192 0.1129 -0.0013 0.0002 -0.0002 240 VAL A CA 1212 C C . VAL A 160 ? 0.1086 0.1195 0.1128 -0.0004 0.0000 -0.0009 240 VAL A C 1213 O O . VAL A 160 ? 0.0908 0.1005 0.0951 0.0002 -0.0005 -0.0012 240 VAL A O 1214 C CB . VAL A 160 ? 0.1555 0.1666 0.1608 -0.0014 -0.0001 -0.0006 240 VAL A CB 1215 C CG1 . VAL A 160 ? 0.1298 0.1406 0.1351 -0.0026 0.0002 0.0000 240 VAL A CG1 1216 C CG2 . VAL A 160 ? 0.2307 0.2407 0.2366 -0.0007 -0.0008 -0.0009 240 VAL A CG2 1217 N N . MET A 161 ? 0.0844 0.0972 0.0885 -0.0003 0.0004 -0.0013 241 MET A N 1218 C CA . MET A 161 ? 0.0698 0.0834 0.0740 0.0005 0.0003 -0.0023 241 MET A CA 1219 C C . MET A 161 ? 0.0685 0.0842 0.0738 0.0008 0.0007 -0.0031 241 MET A C 1220 O O . MET A 161 ? 0.0766 0.0938 0.0822 0.0003 0.0011 -0.0028 241 MET A O 1221 C CB . MET A 161 ? 0.0685 0.0826 0.0715 0.0005 0.0006 -0.0021 241 MET A CB 1222 C CG . MET A 161 ? 0.0858 0.0980 0.0877 0.0003 0.0003 -0.0012 241 MET A CG 1223 S SD . MET A 161 ? 0.1788 0.1922 0.1794 0.0006 0.0004 -0.0012 241 MET A SD 1224 C CE . MET A 161 ? 0.2905 0.3017 0.2901 0.0005 0.0002 0.0001 241 MET A CE 1225 N N . THR A 162 ? 0.0805 0.0964 0.0864 0.0016 0.0006 -0.0042 242 THR A N 1226 C CA . THR A 162 ? 0.0785 0.0963 0.0856 0.0021 0.0010 -0.0051 242 THR A CA 1227 C C . THR A 162 ? 0.0863 0.1050 0.0929 0.0025 0.0013 -0.0061 242 THR A C 1228 O O . THR A 162 ? 0.0780 0.0955 0.0839 0.0026 0.0011 -0.0065 242 THR A O 1229 C CB . THR A 162 ? 0.0738 0.0909 0.0823 0.0029 0.0007 -0.0055 242 THR A CB 1230 O OG1 . THR A 162 ? 0.0936 0.1102 0.1024 0.0025 0.0003 -0.0045 242 THR A OG1 1231 C CG2 . THR A 162 ? 0.0662 0.0853 0.0759 0.0036 0.0011 -0.0063 242 THR A CG2 1232 N N . ASP A 163 ? 0.0775 0.0985 0.0845 0.0026 0.0019 -0.0067 243 ASP A N 1233 C CA . ASP A 163 ? 0.0754 0.0976 0.0821 0.0029 0.0024 -0.0080 243 ASP A CA 1234 C C . ASP A 163 ? 0.0802 0.1042 0.0882 0.0035 0.0029 -0.0088 243 ASP A C 1235 O O . ASP A 163 ? 0.0766 0.1023 0.0851 0.0032 0.0031 -0.0083 243 ASP A O 1236 C CB . ASP A 163 ? 0.0755 0.0992 0.0807 0.0022 0.0026 -0.0075 243 ASP A CB 1237 C CG . ASP A 163 ? 0.1181 0.1428 0.1227 0.0024 0.0029 -0.0087 243 ASP A CG 1238 O OD1 . ASP A 163 ? 0.1111 0.1355 0.1165 0.0030 0.0031 -0.0102 243 ASP A OD1 1239 O OD2 . ASP A 163 ? 0.1045 0.1302 0.1077 0.0019 0.0030 -0.0083 243 ASP A OD2 1240 N N . GLY A 164 ? 0.0929 0.1166 0.1017 0.0043 0.0031 -0.0102 244 GLY A N 1241 C CA . GLY A 164 ? 0.0875 0.1126 0.0976 0.0051 0.0037 -0.0111 244 GLY A CA 1242 C C . GLY A 164 ? 0.1082 0.1315 0.1197 0.0062 0.0036 -0.0116 244 GLY A C 1243 O O . GLY A 164 ? 0.1265 0.1473 0.1377 0.0062 0.0032 -0.0114 244 GLY A O 1244 N N . PRO A 165 ? 0.1290 0.1534 0.1419 0.0071 0.0041 -0.0121 245 PRO A N 1245 C CA . PRO A 165 ? 0.1183 0.1411 0.1326 0.0084 0.0043 -0.0126 245 PRO A CA 1246 C C . PRO A 165 ? 0.1236 0.1447 0.1383 0.0085 0.0035 -0.0113 245 PRO A C 1247 O O . PRO A 165 ? 0.0868 0.1087 0.1012 0.0079 0.0030 -0.0101 245 PRO A O 1248 C CB . PRO A 165 ? 0.1122 0.1374 0.1279 0.0093 0.0049 -0.0129 245 PRO A CB 1249 C CG . PRO A 165 ? 0.1935 0.2213 0.2084 0.0085 0.0053 -0.0134 245 PRO A CG 1250 C CD . PRO A 165 ? 0.1234 0.1509 0.1366 0.0071 0.0047 -0.0124 245 PRO A CD 1251 N N . SER A 166 ? 0.1355 0.1541 0.1507 0.0094 0.0035 -0.0116 246 SER A N 1252 C CA . SER A 166 ? 0.1420 0.1589 0.1576 0.0097 0.0028 -0.0104 246 SER A CA 1253 C C . SER A 166 ? 0.1790 0.1968 0.1964 0.0111 0.0031 -0.0101 246 SER A C 1254 O O . SER A 166 ? 0.1740 0.1909 0.1920 0.0117 0.0026 -0.0091 246 SER A O 1255 C CB . SER A 166 ? 0.1902 0.2039 0.2053 0.0097 0.0027 -0.0106 246 SER A CB 1256 O OG . SER A 166 ? 0.2278 0.2404 0.2436 0.0105 0.0035 -0.0119 246 SER A OG 1257 N N . ASN A 167 ? 0.1300 0.1496 0.1483 0.0119 0.0039 -0.0110 247 ASN A N 1258 C CA . ASN A 167 ? 0.1613 0.1821 0.1813 0.0134 0.0042 -0.0108 247 ASN A CA 1259 C C . ASN A 167 ? 0.2031 0.2276 0.2237 0.0134 0.0045 -0.0108 247 ASN A C 1260 O O . ASN A 167 ? 0.1666 0.1926 0.1887 0.0147 0.0051 -0.0112 247 ASN A O 1261 C CB . ASN A 167 ? 0.2032 0.2220 0.2240 0.0147 0.0051 -0.0119 247 ASN A CB 1262 C CG . ASN A 167 ? 0.2580 0.2778 0.2785 0.0145 0.0060 -0.0136 247 ASN A CG 1263 O OD1 . ASN A 167 ? 0.1422 0.1635 0.1615 0.0132 0.0058 -0.0139 247 ASN A OD1 1264 N ND2 . ASN A 167 ? 0.2394 0.2582 0.2609 0.0158 0.0070 -0.0147 247 ASN A ND2 1265 N N . GLY A 168 ? 0.1079 0.1339 0.1275 0.0119 0.0041 -0.0104 248 GLY A N 1266 C CA . GLY A 168 ? 0.1366 0.1663 0.1567 0.0115 0.0043 -0.0104 248 GLY A CA 1267 C C . GLY A 168 ? 0.1124 0.1429 0.1311 0.0097 0.0038 -0.0097 248 GLY A C 1268 O O . GLY A 168 ? 0.1012 0.1295 0.1188 0.0089 0.0033 -0.0092 248 GLY A O 1269 N N . GLN A 169 ? 0.1279 0.1613 0.1467 0.0091 0.0042 -0.0098 249 GLN A N 1270 C CA . GLN A 169 ? 0.1365 0.1707 0.1541 0.0074 0.0039 -0.0091 249 GLN A CA 1271 C C . GLN A 169 ? 0.1281 0.1602 0.1439 0.0066 0.0039 -0.0093 249 GLN A C 1272 O O . GLN A 169 ? 0.1240 0.1562 0.1394 0.0069 0.0045 -0.0103 249 GLN A O 1273 C CB . GLN A 169 ? 0.1294 0.1672 0.1475 0.0069 0.0045 -0.0092 249 GLN A CB 1274 C CG . GLN A 169 ? 0.1153 0.1538 0.1323 0.0051 0.0044 -0.0084 249 GLN A CG 1275 C CD . GLN A 169 ? 0.1559 0.1945 0.1733 0.0044 0.0038 -0.0074 249 GLN A CD 1276 O OE1 . GLN A 169 ? 0.1082 0.1491 0.1271 0.0049 0.0038 -0.0073 249 GLN A OE1 1277 N NE2 . GLN A 169 ? 0.1112 0.1476 0.1273 0.0034 0.0034 -0.0067 249 GLN A NE2 1278 N N . ALA A 170 ? 0.0970 0.1276 0.1118 0.0055 0.0034 -0.0083 250 ALA A N 1279 C CA . ALA A 170 ? 0.0850 0.1140 0.0980 0.0047 0.0033 -0.0083 250 ALA A CA 1280 C C . ALA A 170 ? 0.1294 0.1590 0.1414 0.0033 0.0033 -0.0073 250 ALA A C 1281 O O . ALA A 170 ? 0.1179 0.1493 0.1305 0.0028 0.0034 -0.0068 250 ALA A O 1282 C CB . ALA A 170 ? 0.0832 0.1090 0.0958 0.0050 0.0027 -0.0082 250 ALA A CB 1283 N N . SER A 171 ? 0.0585 0.0866 0.0689 0.0027 0.0032 -0.0069 251 SER A N 1284 C CA . SER A 171 ? 0.0758 0.1040 0.0850 0.0014 0.0033 -0.0059 251 SER A CA 1285 C C . SER A 171 ? 0.0892 0.1146 0.0976 0.0010 0.0026 -0.0050 251 SER A C 1286 O O . SER A 171 ? 0.0789 0.1024 0.0869 0.0015 0.0023 -0.0052 251 SER A O 1287 C CB . SER A 171 ? 0.1122 0.1414 0.1202 0.0011 0.0038 -0.0060 251 SER A CB 1288 O OG . SER A 171 ? 0.1377 0.1668 0.1445 0.0000 0.0040 -0.0048 251 SER A OG 1289 N N . TYR A 172 ? 0.0787 0.1039 0.0871 0.0001 0.0026 -0.0040 252 TYR A N 1290 C CA . TYR A 172 ? 0.0809 0.1035 0.0887 -0.0003 0.0021 -0.0033 252 TYR A CA 1291 C C . TYR A 172 ? 0.0903 0.1123 0.0969 -0.0015 0.0025 -0.0022 252 TYR A C 1292 O O . TYR A 172 ? 0.0978 0.1213 0.1046 -0.0023 0.0030 -0.0019 252 TYR A O 1293 C CB . TYR A 172 ? 0.0668 0.0895 0.0759 -0.0003 0.0017 -0.0032 252 TYR A CB 1294 C CG . TYR A 172 ? 0.0975 0.1219 0.1080 0.0008 0.0016 -0.0041 252 TYR A CG 1295 C CD1 . TYR A 172 ? 0.0560 0.0793 0.0669 0.0020 0.0014 -0.0047 252 TYR A CD1 1296 C CD2 . TYR A 172 ? 0.1004 0.1276 0.1121 0.0006 0.0019 -0.0043 252 TYR A CD2 1297 C CE1 . TYR A 172 ? 0.0659 0.0906 0.0782 0.0031 0.0015 -0.0055 252 TYR A CE1 1298 C CE2 . TYR A 172 ? 0.0727 0.1016 0.0858 0.0018 0.0020 -0.0050 252 TYR A CE2 1299 C CZ . TYR A 172 ? 0.0854 0.1129 0.0988 0.0031 0.0018 -0.0055 252 TYR A CZ 1300 O OH . TYR A 172 ? 0.0924 0.1213 0.1073 0.0043 0.0019 -0.0062 252 TYR A OH 1301 N N . LYS A 173 ? 0.0547 0.0745 0.0601 -0.0015 0.0023 -0.0016 253 LYS A N 1302 C CA . LYS A 173 ? 0.0463 0.0652 0.0505 -0.0024 0.0027 -0.0005 253 LYS A CA 1303 C C . LYS A 173 ? 0.1059 0.1221 0.1097 -0.0027 0.0023 0.0002 253 LYS A C 1304 O O . LYS A 173 ? 0.0598 0.0746 0.0636 -0.0021 0.0017 -0.0001 253 LYS A O 1305 C CB . LYS A 173 ? 0.0574 0.0768 0.0603 -0.0021 0.0030 -0.0002 253 LYS A CB 1306 C CG . LYS A 173 ? 0.0827 0.1049 0.0857 -0.0022 0.0036 -0.0006 253 LYS A CG 1307 C CD . LYS A 173 ? 0.1304 0.1532 0.1319 -0.0020 0.0039 -0.0002 253 LYS A CD 1308 C CE . LYS A 173 ? 0.2082 0.2340 0.2097 -0.0020 0.0046 -0.0006 253 LYS A CE 1309 N NZ . LYS A 173 ? 0.2312 0.2579 0.2312 -0.0019 0.0049 -0.0001 253 LYS A NZ 1310 N N . ILE A 174 ? 0.0986 0.1140 0.1019 -0.0037 0.0028 0.0011 254 ILE A N 1311 C CA . ILE A 174 ? 0.0944 0.1071 0.0972 -0.0041 0.0027 0.0017 254 ILE A CA 1312 C C . ILE A 174 ? 0.1166 0.1280 0.1179 -0.0041 0.0032 0.0029 254 ILE A C 1313 O O . ILE A 174 ? 0.1024 0.1148 0.1031 -0.0045 0.0039 0.0034 254 ILE A O 1314 C CB . ILE A 174 ? 0.1147 0.1271 0.1180 -0.0053 0.0030 0.0019 254 ILE A CB 1315 C CG1 . ILE A 174 ? 0.0950 0.1095 0.0998 -0.0053 0.0026 0.0009 254 ILE A CG1 1316 C CG2 . ILE A 174 ? 0.1223 0.1319 0.1251 -0.0056 0.0028 0.0023 254 ILE A CG2 1317 C CD1 . ILE A 174 ? 0.1452 0.1603 0.1507 -0.0067 0.0030 0.0009 254 ILE A CD1 1318 N N . PHE A 175 ? 0.0926 0.1019 0.0933 -0.0037 0.0028 0.0033 255 PHE A N 1319 C CA . PHE A 175 ? 0.1108 0.1190 0.1101 -0.0035 0.0032 0.0044 255 PHE A CA 1320 C C . PHE A 175 ? 0.1248 0.1302 0.1236 -0.0039 0.0034 0.0053 255 PHE A C 1321 O O . PHE A 175 ? 0.1165 0.1205 0.1158 -0.0040 0.0029 0.0048 255 PHE A O 1322 C CB . PHE A 175 ? 0.0977 0.1064 0.0966 -0.0024 0.0025 0.0041 255 PHE A CB 1323 C CG . PHE A 175 ? 0.1164 0.1277 0.1154 -0.0020 0.0025 0.0033 255 PHE A CG 1324 C CD1 . PHE A 175 ? 0.0934 0.1063 0.0915 -0.0018 0.0030 0.0038 255 PHE A CD1 1325 C CD2 . PHE A 175 ? 0.1125 0.1248 0.1128 -0.0017 0.0020 0.0019 255 PHE A CD2 1326 C CE1 . PHE A 175 ? 0.1701 0.1856 0.1685 -0.0015 0.0029 0.0029 255 PHE A CE1 1327 C CE2 . PHE A 175 ? 0.0984 0.1130 0.0990 -0.0013 0.0020 0.0010 255 PHE A CE2 1328 C CZ . PHE A 175 ? 0.1398 0.1559 0.1393 -0.0012 0.0025 0.0014 255 PHE A CZ 1329 N N . ARG A 176 ? 0.0998 0.1043 0.0976 -0.0042 0.0043 0.0065 256 ARG A N 1330 C CA . ARG A 176 ? 0.0716 0.0732 0.0688 -0.0044 0.0047 0.0075 256 ARG A CA 1331 C C . ARG A 176 ? 0.0928 0.0940 0.0889 -0.0033 0.0047 0.0085 256 ARG A C 1332 O O . ARG A 176 ? 0.0991 0.1017 0.0945 -0.0029 0.0051 0.0093 256 ARG A O 1333 C CB . ARG A 176 ? 0.1099 0.1104 0.1069 -0.0055 0.0059 0.0083 256 ARG A CB 1334 C CG . ARG A 176 ? 0.1053 0.1026 0.1016 -0.0057 0.0066 0.0093 256 ARG A CG 1335 C CD . ARG A 176 ? 0.1586 0.1545 0.1548 -0.0070 0.0079 0.0099 256 ARG A CD 1336 N NE . ARG A 176 ? 0.2123 0.2049 0.2077 -0.0070 0.0088 0.0110 256 ARG A NE 1337 C CZ . ARG A 176 ? 0.3015 0.2920 0.2968 -0.0082 0.0100 0.0114 256 ARG A CZ 1338 N NH1 . ARG A 176 ? 0.2340 0.2255 0.2300 -0.0097 0.0105 0.0108 256 ARG A NH1 1339 N NH2 . ARG A 176 ? 0.2943 0.2816 0.2889 -0.0080 0.0109 0.0125 256 ARG A NH2 1340 N N . ILE A 177 ? 0.1007 0.1003 0.0967 -0.0027 0.0042 0.0085 257 ILE A N 1341 C CA . ILE A 177 ? 0.0903 0.0900 0.0854 -0.0016 0.0040 0.0094 257 ILE A CA 1342 C C . ILE A 177 ? 0.1225 0.1193 0.1169 -0.0014 0.0045 0.0105 257 ILE A C 1343 O O . ILE A 177 ? 0.1111 0.1059 0.1060 -0.0019 0.0043 0.0100 257 ILE A O 1344 C CB . ILE A 177 ? 0.0769 0.0776 0.0723 -0.0009 0.0028 0.0082 257 ILE A CB 1345 C CG1 . ILE A 177 ? 0.1047 0.1080 0.1008 -0.0010 0.0024 0.0070 257 ILE A CG1 1346 C CG2 . ILE A 177 ? 0.0949 0.0961 0.0895 0.0001 0.0026 0.0090 257 ILE A CG2 1347 C CD1 . ILE A 177 ? 0.0972 0.1010 0.0941 -0.0007 0.0015 0.0056 257 ILE A CD1 1348 N N . GLU A 178 ? 0.0878 0.0844 0.0812 -0.0007 0.0051 0.0120 258 GLU A N 1349 C CA . GLU A 178 ? 0.0774 0.0714 0.0702 -0.0003 0.0057 0.0132 258 GLU A CA 1350 C C . GLU A 178 ? 0.0936 0.0885 0.0856 0.0011 0.0053 0.0141 258 GLU A C 1351 O O . GLU A 178 ? 0.1256 0.1226 0.1169 0.0017 0.0054 0.0150 258 GLU A O 1352 C CB . GLU A 178 ? 0.1287 0.1209 0.1210 -0.0009 0.0071 0.0146 258 GLU A CB 1353 C CG . GLU A 178 ? 0.1956 0.1868 0.1887 -0.0025 0.0076 0.0137 258 GLU A CG 1354 C CD . GLU A 178 ? 0.3073 0.2969 0.2999 -0.0032 0.0091 0.0149 258 GLU A CD 1355 O OE1 . GLU A 178 ? 0.3435 0.3318 0.3352 -0.0023 0.0099 0.0166 258 GLU A OE1 1356 O OE2 . GLU A 178 ? 0.3022 0.2916 0.2953 -0.0046 0.0096 0.0142 258 GLU A OE2 1357 N N . LYS A 179 ? 0.1141 0.1078 0.1063 0.0016 0.0048 0.0139 259 LYS A N 1358 C CA . LYS A 179 ? 0.1272 0.1222 0.1188 0.0029 0.0043 0.0146 259 LYS A CA 1359 C C . LYS A 179 ? 0.1152 0.1137 0.1068 0.0032 0.0035 0.0138 259 LYS A C 1360 O O . LYS A 179 ? 0.0967 0.0973 0.0876 0.0041 0.0034 0.0147 259 LYS A O 1361 C CB . LYS A 179 ? 0.1508 0.1449 0.1415 0.0038 0.0053 0.0167 259 LYS A CB 1362 C CG . LYS A 179 ? 0.2164 0.2067 0.2071 0.0037 0.0062 0.0174 259 LYS A CG 1363 C CD . LYS A 179 ? 0.3228 0.3120 0.3125 0.0047 0.0073 0.0196 259 LYS A CD 1364 C CE . LYS A 179 ? 0.3991 0.3842 0.3888 0.0046 0.0083 0.0202 259 LYS A CE 1365 N NZ . LYS A 179 ? 0.5359 0.5203 0.5261 0.0049 0.0075 0.0192 259 LYS A NZ 1366 N N . GLY A 180 ? 0.0849 0.0843 0.0773 0.0025 0.0028 0.0121 260 GLY A N 1367 C CA . GLY A 180 ? 0.0646 0.0671 0.0572 0.0027 0.0021 0.0111 260 GLY A CA 1368 C C . GLY A 180 ? 0.1207 0.1254 0.1128 0.0025 0.0026 0.0114 260 GLY A C 1369 O O . GLY A 180 ? 0.1200 0.1274 0.1122 0.0026 0.0021 0.0105 260 GLY A O 1370 N N . LYS A 181 ? 0.0813 0.0849 0.0731 0.0022 0.0036 0.0126 261 LYS A N 1371 C CA . LYS A 181 ? 0.0976 0.1032 0.0888 0.0019 0.0041 0.0130 261 LYS A CA 1372 C C . LYS A 181 ? 0.0834 0.0884 0.0754 0.0008 0.0045 0.0122 261 LYS A C 1373 O O . LYS A 181 ? 0.0900 0.0925 0.0825 0.0001 0.0050 0.0124 261 LYS A O 1374 C CB . LYS A 181 ? 0.1885 0.1936 0.1787 0.0025 0.0052 0.0152 261 LYS A CB 1375 C CG . LYS A 181 ? 0.2232 0.2289 0.2124 0.0038 0.0049 0.0164 261 LYS A CG 1376 C CD . LYS A 181 ? 0.3026 0.3124 0.2912 0.0043 0.0044 0.0161 261 LYS A CD 1377 C CE . LYS A 181 ? 0.2865 0.2976 0.2744 0.0057 0.0042 0.0174 261 LYS A CE 1378 N NZ . LYS A 181 ? 0.3129 0.3283 0.3001 0.0061 0.0037 0.0171 261 LYS A NZ 1379 N N . ILE A 182 ? 0.0872 0.0948 0.0795 0.0005 0.0043 0.0111 262 ILE A N 1380 C CA . ILE A 182 ? 0.0942 0.1019 0.0874 -0.0005 0.0046 0.0104 262 ILE A CA 1381 C C . ILE A 182 ? 0.1769 0.1839 0.1694 -0.0010 0.0059 0.0120 262 ILE A C 1382 O O . ILE A 182 ? 0.1461 0.1548 0.1376 -0.0006 0.0063 0.0130 262 ILE A O 1383 C CB . ILE A 182 ? 0.1317 0.1423 0.1253 -0.0006 0.0042 0.0090 262 ILE A CB 1384 C CG1 . ILE A 182 ? 0.1514 0.1622 0.1457 -0.0001 0.0031 0.0075 262 ILE A CG1 1385 C CG2 . ILE A 182 ? 0.1221 0.1330 0.1166 -0.0016 0.0046 0.0084 262 ILE A CG2 1386 C CD1 . ILE A 182 ? 0.2132 0.2268 0.2080 0.0000 0.0028 0.0060 262 ILE A CD1 1387 N N . VAL A 183 ? 0.0812 0.0858 0.0742 -0.0019 0.0065 0.0121 263 VAL A N 1388 C CA . VAL A 183 ? 0.1058 0.1093 0.0983 -0.0026 0.0078 0.0135 263 VAL A CA 1389 C C . VAL A 183 ? 0.1703 0.1750 0.1635 -0.0038 0.0082 0.0127 263 VAL A C 1390 O O . VAL A 183 ? 0.1220 0.1267 0.1148 -0.0044 0.0093 0.0137 263 VAL A O 1391 C CB . VAL A 183 ? 0.1440 0.1438 0.1363 -0.0029 0.0085 0.0144 263 VAL A CB 1392 C CG1 . VAL A 183 ? 0.1959 0.1946 0.1873 -0.0015 0.0083 0.0156 263 VAL A CG1 1393 C CG2 . VAL A 183 ? 0.1514 0.1497 0.1448 -0.0037 0.0079 0.0129 263 VAL A CG2 1394 N N . LYS A 184 ? 0.1136 0.1193 0.1080 -0.0041 0.0073 0.0110 264 LYS A N 1395 C CA . LYS A 184 ? 0.1504 0.1577 0.1457 -0.0051 0.0076 0.0101 264 LYS A CA 1396 C C . LYS A 184 ? 0.1237 0.1328 0.1202 -0.0049 0.0065 0.0083 264 LYS A C 1397 O O . LYS A 184 ? 0.1051 0.1131 0.1019 -0.0044 0.0057 0.0076 264 LYS A O 1398 C CB . LYS A 184 ? 0.1574 0.1626 0.1531 -0.0065 0.0085 0.0103 264 LYS A CB 1399 C CG . LYS A 184 ? 0.1615 0.1686 0.1581 -0.0077 0.0090 0.0097 264 LYS A CG 1400 C CD . LYS A 184 ? 0.2130 0.2181 0.2101 -0.0092 0.0098 0.0097 264 LYS A CD 1401 C CE . LYS A 184 ? 0.2197 0.2271 0.2176 -0.0105 0.0105 0.0092 264 LYS A CE 1402 N NZ . LYS A 184 ? 0.2412 0.2470 0.2396 -0.0122 0.0112 0.0089 264 LYS A NZ 1403 N N . SER A 185 ? 0.0598 0.0715 0.0568 -0.0052 0.0066 0.0075 265 SER A N 1404 C CA . SER A 185 ? 0.1032 0.1166 0.1015 -0.0050 0.0058 0.0059 265 SER A CA 1405 C C . SER A 185 ? 0.1247 0.1402 0.1240 -0.0058 0.0063 0.0053 265 SER A C 1406 O O . SER A 185 ? 0.1396 0.1558 0.1383 -0.0065 0.0073 0.0061 265 SER A O 1407 C CB . SER A 185 ? 0.1000 0.1151 0.0981 -0.0038 0.0051 0.0052 265 SER A CB 1408 O OG . SER A 185 ? 0.1184 0.1358 0.1158 -0.0037 0.0057 0.0055 265 SER A OG 1409 N N . VAL A 186 ? 0.1039 0.1204 0.1045 -0.0058 0.0057 0.0040 266 VAL A N 1410 C CA . VAL A 186 ? 0.1445 0.1633 0.1461 -0.0065 0.0061 0.0034 266 VAL A CA 1411 C C . VAL A 186 ? 0.1333 0.1540 0.1362 -0.0057 0.0053 0.0020 266 VAL A C 1412 O O . VAL A 186 ? 0.1235 0.1429 0.1269 -0.0051 0.0045 0.0015 266 VAL A O 1413 C CB . VAL A 186 ? 0.1371 0.1551 0.1394 -0.0079 0.0066 0.0036 266 VAL A CB 1414 C CG1 . VAL A 186 ? 0.1835 0.1998 0.1864 -0.0078 0.0058 0.0030 266 VAL A CG1 1415 C CG2 . VAL A 186 ? 0.1897 0.2105 0.1931 -0.0087 0.0070 0.0030 266 VAL A CG2 1416 N N . GLU A 187 ? 0.1273 0.1508 0.1308 -0.0056 0.0056 0.0013 267 GLU A N 1417 C CA . GLU A 187 ? 0.1341 0.1593 0.1390 -0.0048 0.0050 0.0000 267 GLU A CA 1418 C C . GLU A 187 ? 0.1574 0.1835 0.1636 -0.0054 0.0050 -0.0004 267 GLU A C 1419 O O . GLU A 187 ? 0.1256 0.1530 0.1321 -0.0065 0.0057 -0.0001 267 GLU A O 1420 C CB . GLU A 187 ? 0.1279 0.1557 0.1328 -0.0042 0.0054 -0.0006 267 GLU A CB 1421 C CG . GLU A 187 ? 0.1505 0.1800 0.1569 -0.0033 0.0049 -0.0020 267 GLU A CG 1422 C CD . GLU A 187 ? 0.2243 0.2560 0.2308 -0.0025 0.0053 -0.0028 267 GLU A CD 1423 O OE1 . GLU A 187 ? 0.2473 0.2798 0.2526 -0.0028 0.0058 -0.0024 267 GLU A OE1 1424 O OE2 . GLU A 187 ? 0.1603 0.1929 0.1679 -0.0016 0.0050 -0.0039 267 GLU A OE2 1425 N N . MET A 188 ? 0.1071 0.1328 0.1144 -0.0047 0.0042 -0.0010 268 MET A N 1426 C CA . MET A 188 ? 0.0942 0.1212 0.1028 -0.0052 0.0040 -0.0014 268 MET A CA 1427 C C . MET A 188 ? 0.1046 0.1351 0.1144 -0.0048 0.0043 -0.0021 268 MET A C 1428 O O . MET A 188 ? 0.1043 0.1357 0.1145 -0.0036 0.0041 -0.0028 268 MET A O 1429 C CB . MET A 188 ? 0.0882 0.1139 0.0974 -0.0044 0.0030 -0.0017 268 MET A CB 1430 C CG . MET A 188 ? 0.0686 0.0911 0.0768 -0.0048 0.0028 -0.0010 268 MET A CG 1431 S SD . MET A 188 ? 0.1365 0.1571 0.1449 -0.0036 0.0017 -0.0013 268 MET A SD 1432 C CE . MET A 188 ? 0.1084 0.1314 0.1186 -0.0032 0.0013 -0.0020 268 MET A CE 1433 N N . ASN A 189 ? 0.1120 0.1445 0.1226 -0.0060 0.0048 -0.0021 269 ASN A N 1434 C CA . ASN A 189 ? 0.0908 0.1269 0.1028 -0.0058 0.0050 -0.0028 269 ASN A CA 1435 C C . ASN A 189 ? 0.1064 0.1437 0.1199 -0.0050 0.0043 -0.0033 269 ASN A C 1436 O O . ASN A 189 ? 0.0848 0.1233 0.0991 -0.0059 0.0042 -0.0033 269 ASN A O 1437 C CB . ASN A 189 ? 0.0805 0.1184 0.0926 -0.0075 0.0059 -0.0024 269 ASN A CB 1438 C CG . ASN A 189 ? 0.1354 0.1773 0.1489 -0.0073 0.0063 -0.0031 269 ASN A CG 1439 O OD1 . ASN A 189 ? 0.0858 0.1292 0.0997 -0.0060 0.0063 -0.0037 269 ASN A OD1 1440 N ND2 . ASN A 189 ? 0.0818 0.1258 0.0962 -0.0087 0.0066 -0.0032 269 ASN A ND2 1441 N N . ALA A 190 ? 0.0946 0.1315 0.1085 -0.0033 0.0038 -0.0038 270 ALA A N 1442 C CA . ALA A 190 ? 0.0641 0.1017 0.0794 -0.0023 0.0031 -0.0041 270 ALA A CA 1443 C C . ALA A 190 ? 0.0971 0.1366 0.1136 -0.0006 0.0031 -0.0048 270 ALA A C 1444 O O . ALA A 190 ? 0.0361 0.0739 0.0526 0.0007 0.0027 -0.0050 270 ALA A O 1445 C CB . ALA A 190 ? 0.0816 0.1157 0.0961 -0.0020 0.0023 -0.0037 270 ALA A CB 1446 N N . PRO A 191 ? 0.1490 0.1919 0.1665 -0.0007 0.0036 -0.0052 271 PRO A N 1447 C CA . PRO A 191 ? 0.1362 0.1811 0.1550 0.0010 0.0038 -0.0059 271 PRO A CA 1448 C C . PRO A 191 ? 0.1221 0.1675 0.1423 0.0022 0.0031 -0.0058 271 PRO A C 1449 O O . PRO A 191 ? 0.1091 0.1556 0.1298 0.0014 0.0027 -0.0054 271 PRO A O 1450 C CB . PRO A 191 ? 0.1481 0.1968 0.1677 0.0004 0.0045 -0.0062 271 PRO A CB 1451 C CG . PRO A 191 ? 0.1955 0.2444 0.2145 -0.0017 0.0046 -0.0056 271 PRO A CG 1452 C CD . PRO A 191 ? 0.1408 0.1857 0.1581 -0.0024 0.0043 -0.0050 271 PRO A CD 1453 N N . ASN A 192 ? 0.1095 0.1541 0.1302 0.0040 0.0030 -0.0062 272 ASN A N 1454 C CA . ASN A 192 ? 0.0981 0.1429 0.1201 0.0055 0.0025 -0.0060 272 ASN A CA 1455 C C . ASN A 192 ? 0.1231 0.1648 0.1443 0.0053 0.0017 -0.0054 272 ASN A C 1456 O O . ASN A 192 ? 0.1377 0.1795 0.1599 0.0064 0.0012 -0.0050 272 ASN A O 1457 C CB . ASN A 192 ? 0.1440 0.1931 0.1678 0.0055 0.0024 -0.0059 272 ASN A CB 1458 C CG . ASN A 192 ? 0.2215 0.2718 0.2468 0.0076 0.0022 -0.0058 272 ASN A CG 1459 O OD1 . ASN A 192 ? 0.2485 0.2981 0.2743 0.0092 0.0026 -0.0063 272 ASN A OD1 1460 N ND2 . ASN A 192 ? 0.2351 0.2875 0.2614 0.0077 0.0016 -0.0052 272 ASN A ND2 1461 N N . TYR A 193 ? 0.1389 0.1781 0.1585 0.0039 0.0016 -0.0052 273 TYR A N 1462 C CA . TYR A 193 ? 0.1322 0.1682 0.1509 0.0037 0.0010 -0.0047 273 TYR A CA 1463 C C . TYR A 193 ? 0.1118 0.1446 0.1296 0.0046 0.0010 -0.0050 273 TYR A C 1464 O O . TYR A 193 ? 0.0753 0.1083 0.0928 0.0048 0.0016 -0.0056 273 TYR A O 1465 C CB . TYR A 193 ? 0.1012 0.1362 0.1185 0.0018 0.0009 -0.0042 273 TYR A CB 1466 C CG . TYR A 193 ? 0.1436 0.1808 0.1616 0.0006 0.0007 -0.0039 273 TYR A CG 1467 C CD1 . TYR A 193 ? 0.1908 0.2316 0.2097 0.0001 0.0011 -0.0042 273 TYR A CD1 1468 C CD2 . TYR A 193 ? 0.1626 0.1983 0.1801 0.0000 0.0001 -0.0035 273 TYR A CD2 1469 C CE1 . TYR A 193 ? 0.2380 0.2810 0.2575 -0.0012 0.0010 -0.0041 273 TYR A CE1 1470 C CE2 . TYR A 193 ? 0.1287 0.1665 0.1467 -0.0012 0.0000 -0.0034 273 TYR A CE2 1471 C CZ . TYR A 193 ? 0.2031 0.2446 0.2221 -0.0019 0.0004 -0.0037 273 TYR A CZ 1472 O OH . TYR A 193 ? 0.2635 0.3073 0.2831 -0.0032 0.0003 -0.0037 273 TYR A OH 1473 N N . HIS A 194 ? 0.0924 0.1226 0.1097 0.0050 0.0005 -0.0046 274 HIS A N 1474 C CA . HIS A 194 ? 0.0856 0.1127 0.1020 0.0055 0.0005 -0.0049 274 HIS A CA 1475 C C . HIS A 194 ? 0.1009 0.1252 0.1162 0.0047 -0.0001 -0.0043 274 HIS A C 1476 O O . HIS A 194 ? 0.0785 0.1026 0.0942 0.0049 -0.0006 -0.0038 274 HIS A O 1477 C CB . HIS A 194 ? 0.1053 0.1319 0.1228 0.0073 0.0006 -0.0054 274 HIS A CB 1478 C CG . HIS A 194 ? 0.1076 0.1318 0.1243 0.0076 0.0010 -0.0061 274 HIS A CG 1479 N ND1 . HIS A 194 ? 0.1259 0.1471 0.1422 0.0081 0.0007 -0.0061 274 HIS A ND1 1480 C CD2 . HIS A 194 ? 0.0823 0.1069 0.0985 0.0075 0.0016 -0.0070 274 HIS A CD2 1481 C CE1 . HIS A 194 ? 0.1311 0.1510 0.1468 0.0082 0.0011 -0.0069 274 HIS A CE1 1482 N NE2 . HIS A 194 ? 0.1474 0.1694 0.1630 0.0078 0.0017 -0.0075 274 HIS A NE2 1483 N N . TYR A 195 ? 0.0663 0.0889 0.0802 0.0040 0.0000 -0.0043 275 TYR A N 1484 C CA . TYR A 195 ? 0.0764 0.0964 0.0892 0.0033 -0.0005 -0.0038 275 TYR A CA 1485 C C . TYR A 195 ? 0.0876 0.1051 0.0995 0.0038 -0.0005 -0.0041 275 TYR A C 1486 O O . TYR A 195 ? 0.0719 0.0895 0.0832 0.0037 -0.0001 -0.0046 275 TYR A O 1487 C CB . TYR A 195 ? 0.0500 0.0701 0.0617 0.0018 -0.0003 -0.0033 275 TYR A CB 1488 C CG . TYR A 195 ? 0.0914 0.1134 0.1037 0.0009 -0.0003 -0.0030 275 TYR A CG 1489 C CD1 . TYR A 195 ? 0.1103 0.1351 0.1233 0.0006 0.0002 -0.0032 275 TYR A CD1 1490 C CD2 . TYR A 195 ? 0.0920 0.1132 0.1041 0.0002 -0.0007 -0.0025 275 TYR A CD2 1491 C CE1 . TYR A 195 ? 0.0916 0.1185 0.1052 -0.0003 0.0003 -0.0030 275 TYR A CE1 1492 C CE2 . TYR A 195 ? 0.0709 0.0940 0.0835 -0.0008 -0.0007 -0.0023 275 TYR A CE2 1493 C CZ . TYR A 195 ? 0.1045 0.1305 0.1179 -0.0011 -0.0002 -0.0026 275 TYR A CZ 1494 O OH . TYR A 195 ? 0.1072 0.1354 0.1213 -0.0022 -0.0001 -0.0026 275 TYR A OH 1495 N N . GLU A 196 ? 0.0889 0.1044 0.1009 0.0042 -0.0010 -0.0039 276 GLU A N 1496 C CA . GLU A 196 ? 0.1169 0.1300 0.1280 0.0045 -0.0010 -0.0041 276 GLU A CA 1497 C C . GLU A 196 ? 0.0944 0.1055 0.1050 0.0041 -0.0016 -0.0034 276 GLU A C 1498 O O . GLU A 196 ? 0.0995 0.1108 0.1106 0.0041 -0.0020 -0.0029 276 GLU A O 1499 C CB . GLU A 196 ? 0.1587 0.1714 0.1708 0.0057 -0.0008 -0.0049 276 GLU A CB 1500 C CG . GLU A 196 ? 0.2614 0.2758 0.2738 0.0061 -0.0001 -0.0058 276 GLU A CG 1501 C CD . GLU A 196 ? 0.2767 0.2901 0.2899 0.0072 0.0003 -0.0067 276 GLU A CD 1502 O OE1 . GLU A 196 ? 0.3535 0.3653 0.3673 0.0079 0.0001 -0.0064 276 GLU A OE1 1503 O OE2 . GLU A 196 ? 0.2186 0.2328 0.2318 0.0074 0.0009 -0.0078 276 GLU A OE2 1504 N N . GLU A 197 ? 0.0913 0.1006 0.1008 0.0038 -0.0017 -0.0035 277 GLU A N 1505 C CA . GLU A 197 ? 0.0940 0.1012 0.1030 0.0036 -0.0022 -0.0029 277 GLU A CA 1506 C C . GLU A 197 ? 0.0973 0.1047 0.1062 0.0029 -0.0025 -0.0021 277 GLU A C 1507 O O . GLU A 197 ? 0.1105 0.1173 0.1198 0.0032 -0.0029 -0.0018 277 GLU A O 1508 C CB . GLU A 197 ? 0.1024 0.1084 0.1121 0.0046 -0.0023 -0.0032 277 GLU A CB 1509 C CG . GLU A 197 ? 0.1400 0.1455 0.1498 0.0051 -0.0019 -0.0042 277 GLU A CG 1510 C CD . GLU A 197 ? 0.1803 0.1845 0.1910 0.0061 -0.0018 -0.0044 277 GLU A CD 1511 O OE1 . GLU A 197 ? 0.1345 0.1389 0.1460 0.0067 -0.0020 -0.0038 277 GLU A OE1 1512 O OE2 . GLU A 197 ? 0.1761 0.1791 0.1867 0.0063 -0.0015 -0.0052 277 GLU A OE2 1513 N N . CYS A 198 ? 0.0820 0.0902 0.0903 0.0020 -0.0023 -0.0019 278 CYS A N 1514 C CA . CYS A 198 ? 0.0831 0.0916 0.0914 0.0012 -0.0025 -0.0013 278 CYS A CA 1515 C C . CYS A 198 ? 0.0806 0.0869 0.0880 0.0008 -0.0028 -0.0008 278 CYS A C 1516 O O . CYS A 198 ? 0.0829 0.0876 0.0894 0.0008 -0.0028 -0.0007 278 CYS A O 1517 C CB . CYS A 198 ? 0.1300 0.1396 0.1378 0.0002 -0.0020 -0.0012 278 CYS A CB 1518 S SG . CYS A 198 ? 0.1720 0.1846 0.1808 0.0004 -0.0015 -0.0017 278 CYS A SG 1519 N N . SER A 199 ? 0.1157 0.1222 0.1235 0.0006 -0.0032 -0.0006 279 SER A N 1520 C CA . SER A 199 ? 0.1018 0.1066 0.1089 0.0001 -0.0034 -0.0002 279 SER A CA 1521 C C . SER A 199 ? 0.1020 0.1070 0.1086 -0.0012 -0.0031 0.0000 279 SER A C 1522 O O . SER A 199 ? 0.1264 0.1332 0.1337 -0.0017 -0.0031 -0.0001 279 SER A O 1523 C CB . SER A 199 ? 0.1057 0.1104 0.1133 0.0006 -0.0040 0.0000 279 SER A CB 1524 O OG . SER A 199 ? 0.1675 0.1715 0.1754 0.0017 -0.0042 -0.0002 279 SER A OG 1525 N N . CYS A 200 ? 0.0957 0.0992 0.1013 -0.0017 -0.0028 0.0003 280 CYS A N 1526 C CA . CYS A 200 ? 0.0952 0.0986 0.1003 -0.0029 -0.0022 0.0005 280 CYS A CA 1527 C C . CYS A 200 ? 0.1319 0.1332 0.1362 -0.0035 -0.0022 0.0008 280 CYS A C 1528 O O . CYS A 200 ? 0.1423 0.1419 0.1460 -0.0030 -0.0024 0.0010 280 CYS A O 1529 C CB . CYS A 200 ? 0.1348 0.1382 0.1393 -0.0031 -0.0016 0.0007 280 CYS A CB 1530 S SG . CYS A 200 ? 0.1525 0.1584 0.1578 -0.0025 -0.0015 0.0003 280 CYS A SG 1531 N N . TYR A 201 ? 0.0708 0.0722 0.0751 -0.0046 -0.0019 0.0007 281 TYR A N 1532 C CA . TYR A 201 ? 0.0915 0.0908 0.0950 -0.0053 -0.0017 0.0008 281 TYR A CA 1533 C C . TYR A 201 ? 0.0955 0.0945 0.0987 -0.0067 -0.0009 0.0008 281 TYR A C 1534 O O . TYR A 201 ? 0.0910 0.0919 0.0948 -0.0073 -0.0006 0.0005 281 TYR A O 1535 C CB . TYR A 201 ? 0.0964 0.0962 0.1003 -0.0053 -0.0024 0.0005 281 TYR A CB 1536 C CG . TYR A 201 ? 0.0974 0.0998 0.1023 -0.0060 -0.0025 0.0000 281 TYR A CG 1537 C CD1 . TYR A 201 ? 0.0946 0.0993 0.1005 -0.0052 -0.0031 -0.0001 281 TYR A CD1 1538 C CD2 . TYR A 201 ? 0.0749 0.0774 0.0796 -0.0075 -0.0020 -0.0004 281 TYR A CD2 1539 C CE1 . TYR A 201 ? 0.1211 0.1285 0.1278 -0.0057 -0.0032 -0.0005 281 TYR A CE1 1540 C CE2 . TYR A 201 ? 0.1138 0.1192 0.1194 -0.0082 -0.0022 -0.0009 281 TYR A CE2 1541 C CZ . TYR A 201 ? 0.1149 0.1229 0.1215 -0.0072 -0.0028 -0.0009 281 TYR A CZ 1542 O OH . TYR A 201 ? 0.1183 0.1294 0.1258 -0.0078 -0.0030 -0.0014 281 TYR A OH 1543 N N . PRO A 202 ? 0.1132 0.1099 0.1156 -0.0072 -0.0003 0.0011 282 PRO A N 1544 C CA . PRO A 202 ? 0.0578 0.0535 0.0599 -0.0086 0.0007 0.0010 282 PRO A CA 1545 C C . PRO A 202 ? 0.0961 0.0922 0.0984 -0.0098 0.0006 0.0002 282 PRO A C 1546 O O . PRO A 202 ? 0.0982 0.0942 0.1006 -0.0094 0.0000 0.0000 282 PRO A O 1547 C CB . PRO A 202 ? 0.0646 0.0573 0.0656 -0.0083 0.0012 0.0018 282 PRO A CB 1548 C CG . PRO A 202 ? 0.1121 0.1042 0.1129 -0.0071 0.0004 0.0018 282 PRO A CG 1549 C CD . PRO A 202 ? 0.1124 0.1068 0.1140 -0.0064 -0.0006 0.0015 282 PRO A CD 1550 N N . ASP A 203 ? 0.0629 0.0597 0.0655 -0.0112 0.0014 -0.0002 283 ASP A N 1551 C CA . ASP A 203 ? 0.1125 0.1101 0.1154 -0.0126 0.0014 -0.0011 283 ASP A CA 1552 C C . ASP A 203 ? 0.1337 0.1306 0.1365 -0.0144 0.0027 -0.0014 283 ASP A C 1553 O O . ASP A 203 ? 0.1303 0.1290 0.1337 -0.0148 0.0030 -0.0014 283 ASP A O 1554 C CB . ASP A 203 ? 0.0924 0.0937 0.0964 -0.0125 0.0005 -0.0017 283 ASP A CB 1555 C CG . ASP A 203 ? 0.2012 0.2039 0.2055 -0.0139 0.0004 -0.0027 283 ASP A CG 1556 O OD1 . ASP A 203 ? 0.1976 0.1983 0.2013 -0.0151 0.0012 -0.0031 283 ASP A OD1 1557 O OD2 . ASP A 203 ? 0.2245 0.2305 0.2297 -0.0138 -0.0003 -0.0031 283 ASP A OD2 1558 N N . SER A 204 ? 0.1184 0.1126 0.1205 -0.0153 0.0035 -0.0017 284 SER A N 1559 C CA . SER A 204 ? 0.1393 0.1325 0.1413 -0.0171 0.0049 -0.0020 284 SER A CA 1560 C C . SER A 204 ? 0.1245 0.1168 0.1263 -0.0168 0.0057 -0.0010 284 SER A C 1561 O O . SER A 204 ? 0.0447 0.0383 0.0469 -0.0180 0.0064 -0.0012 284 SER A O 1562 C CB . SER A 204 ? 0.1537 0.1500 0.1567 -0.0188 0.0049 -0.0032 284 SER A CB 1563 O OG . SER A 204 ? 0.2093 0.2065 0.2123 -0.0192 0.0042 -0.0042 284 SER A OG 1564 N N . SER A 205 ? 0.1074 0.0977 0.1084 -0.0153 0.0057 0.0002 285 SER A N 1565 C CA . SER A 205 ? 0.1548 0.1442 0.1553 -0.0148 0.0064 0.0013 285 SER A CA 1566 C C . SER A 205 ? 0.1507 0.1432 0.1519 -0.0143 0.0059 0.0015 285 SER A C 1567 O O . SER A 205 ? 0.1716 0.1639 0.1725 -0.0139 0.0064 0.0023 285 SER A O 1568 C CB . SER A 205 ? 0.1912 0.1786 0.1915 -0.0165 0.0081 0.0014 285 SER A CB 1569 O OG . SER A 205 ? 0.1715 0.1554 0.1710 -0.0167 0.0088 0.0014 285 SER A OG 1570 N N . GLU A 206 ? 0.1030 0.0985 0.1052 -0.0142 0.0048 0.0006 286 GLU A N 1571 C CA . GLU A 206 ? 0.1497 0.1482 0.1526 -0.0135 0.0043 0.0007 286 GLU A CA 1572 C C . GLU A 206 ? 0.1287 0.1285 0.1319 -0.0118 0.0029 0.0007 286 GLU A C 1573 O O . GLU A 206 ? 0.1105 0.1094 0.1136 -0.0114 0.0023 0.0004 286 GLU A O 1574 C CB . GLU A 206 ? 0.1746 0.1761 0.1785 -0.0149 0.0044 -0.0002 286 GLU A CB 1575 C CG . GLU A 206 ? 0.1907 0.1911 0.1944 -0.0167 0.0059 -0.0002 286 GLU A CG 1576 C CD . GLU A 206 ? 0.4231 0.4268 0.4279 -0.0182 0.0060 -0.0012 286 GLU A CD 1577 O OE1 . GLU A 206 ? 0.4470 0.4541 0.4528 -0.0175 0.0050 -0.0015 286 GLU A OE1 1578 O OE2 . GLU A 206 ? 0.5217 0.5247 0.5264 -0.0200 0.0072 -0.0015 286 GLU A OE2 1579 N N . ILE A 207 ? 0.0824 0.0841 0.0860 -0.0109 0.0026 0.0009 287 ILE A N 1580 C CA . ILE A 207 ? 0.0734 0.0759 0.0773 -0.0093 0.0015 0.0008 287 ILE A CA 1581 C C . ILE A 207 ? 0.0732 0.0790 0.0784 -0.0091 0.0009 0.0002 287 ILE A C 1582 O O . ILE A 207 ? 0.1190 0.1270 0.1248 -0.0097 0.0012 -0.0001 287 ILE A O 1583 C CB . ILE A 207 ? 0.0789 0.0810 0.0822 -0.0081 0.0016 0.0015 287 ILE A CB 1584 C CG1 . ILE A 207 ? 0.0844 0.0837 0.0865 -0.0082 0.0023 0.0024 287 ILE A CG1 1585 C CG2 . ILE A 207 ? 0.0658 0.0684 0.0694 -0.0067 0.0006 0.0014 287 ILE A CG2 1586 C CD1 . ILE A 207 ? 0.1358 0.1327 0.1374 -0.0079 0.0020 0.0025 287 ILE A CD1 1587 N N . THR A 208 ? 0.0904 0.0966 0.0959 -0.0083 -0.0001 -0.0001 288 THR A N 1588 C CA . THR A 208 ? 0.1174 0.1266 0.1242 -0.0077 -0.0007 -0.0006 288 THR A CA 1589 C C . THR A 208 ? 0.0964 0.1054 0.1033 -0.0060 -0.0014 -0.0004 288 THR A C 1590 O O . THR A 208 ? 0.0877 0.0946 0.0940 -0.0054 -0.0017 -0.0001 288 THR A O 1591 C CB . THR A 208 ? 0.1575 0.1679 0.1648 -0.0083 -0.0012 -0.0010 288 THR A CB 1592 O OG1 . THR A 208 ? 0.1432 0.1539 0.1504 -0.0101 -0.0005 -0.0014 288 THR A OG1 1593 C CG2 . THR A 208 ? 0.1395 0.1532 0.1481 -0.0075 -0.0018 -0.0013 288 THR A CG2 1594 N N . CYS A 209 ? 0.0765 0.0876 0.0842 -0.0052 -0.0015 -0.0005 289 CYS A N 1595 C CA . CYS A 209 ? 0.0854 0.0963 0.0933 -0.0037 -0.0019 -0.0005 289 CYS A CA 1596 C C . CYS A 209 ? 0.1156 0.1290 0.1249 -0.0028 -0.0024 -0.0008 289 CYS A C 1597 O O . CYS A 209 ? 0.1023 0.1183 0.1124 -0.0031 -0.0022 -0.0011 289 CYS A O 1598 C CB . CYS A 209 ? 0.1161 0.1270 0.1237 -0.0033 -0.0014 -0.0005 289 CYS A CB 1599 S SG . CYS A 209 ? 0.1513 0.1595 0.1573 -0.0038 -0.0009 0.0001 289 CYS A SG 1600 N N . VAL A 210 ? 0.0785 0.0912 0.0880 -0.0018 -0.0030 -0.0007 290 VAL A N 1601 C CA . VAL A 210 ? 0.0570 0.0716 0.0677 -0.0006 -0.0033 -0.0008 290 VAL A CA 1602 C C . VAL A 210 ? 0.0935 0.1070 0.1043 0.0008 -0.0033 -0.0009 290 VAL A C 1603 O O . VAL A 210 ? 0.0506 0.0616 0.0606 0.0010 -0.0035 -0.0007 290 VAL A O 1604 C CB . VAL A 210 ? 0.0582 0.0731 0.0692 -0.0004 -0.0040 -0.0005 290 VAL A CB 1605 C CG1 . VAL A 210 ? 0.0652 0.0822 0.0775 0.0010 -0.0043 -0.0004 290 VAL A CG1 1606 C CG2 . VAL A 210 ? 0.0728 0.0891 0.0837 -0.0020 -0.0040 -0.0007 290 VAL A CG2 1607 N N . CYS A 211 ? 0.0853 0.1006 0.0971 0.0016 -0.0031 -0.0012 291 CYS A N 1608 C CA . CYS A 211 ? 0.0722 0.0866 0.0840 0.0026 -0.0028 -0.0015 291 CYS A CA 1609 C C . CYS A 211 ? 0.0687 0.0840 0.0818 0.0041 -0.0029 -0.0016 291 CYS A C 1610 O O . CYS A 211 ? 0.0831 0.0995 0.0970 0.0046 -0.0033 -0.0012 291 CYS A O 1611 C CB . CYS A 211 ? 0.0805 0.0957 0.0920 0.0020 -0.0022 -0.0019 291 CYS A CB 1612 S SG . CYS A 211 ? 0.1460 0.1603 0.1561 0.0003 -0.0020 -0.0015 291 CYS A SG 1613 N N . ARG A 212 ? 0.0559 0.0707 0.0692 0.0049 -0.0025 -0.0022 292 ARG A N 1614 C CA . ARG A 212 ? 0.0556 0.0706 0.0700 0.0064 -0.0023 -0.0024 292 ARG A CA 1615 C C . ARG A 212 ? 0.0682 0.0854 0.0835 0.0069 -0.0017 -0.0030 292 ARG A C 1616 O O . ARG A 212 ? 0.0813 0.0983 0.0959 0.0064 -0.0013 -0.0036 292 ARG A O 1617 C CB . ARG A 212 ? 0.0515 0.0636 0.0654 0.0070 -0.0022 -0.0026 292 ARG A CB 1618 C CG . ARG A 212 ? 0.0776 0.0893 0.0925 0.0084 -0.0017 -0.0031 292 ARG A CG 1619 C CD . ARG A 212 ? 0.1116 0.1203 0.1259 0.0086 -0.0016 -0.0036 292 ARG A CD 1620 N NE . ARG A 212 ? 0.0982 0.1062 0.1134 0.0098 -0.0009 -0.0042 292 ARG A NE 1621 C CZ . ARG A 212 ? 0.1599 0.1654 0.1749 0.0101 -0.0006 -0.0047 292 ARG A CZ 1622 N NH1 . ARG A 212 ? 0.0849 0.0886 0.0988 0.0092 -0.0010 -0.0046 292 ARG A NH1 1623 N NH2 . ARG A 212 ? 0.1468 0.1515 0.1627 0.0112 0.0001 -0.0054 292 ARG A NH2 1624 N N . ASP A 213 ? 0.0832 0.1027 0.0998 0.0078 -0.0017 -0.0028 293 ASP A N 1625 C CA . ASP A 213 ? 0.0798 0.1014 0.0973 0.0084 -0.0011 -0.0034 293 ASP A CA 1626 C C . ASP A 213 ? 0.0906 0.1108 0.1089 0.0101 -0.0007 -0.0038 293 ASP A C 1627 O O . ASP A 213 ? 0.0933 0.1137 0.1126 0.0113 -0.0008 -0.0033 293 ASP A O 1628 C CB . ASP A 213 ? 0.0657 0.0909 0.0844 0.0085 -0.0012 -0.0031 293 ASP A CB 1629 C CG . ASP A 213 ? 0.1000 0.1277 0.1200 0.0095 -0.0006 -0.0036 293 ASP A CG 1630 O OD1 . ASP A 213 ? 0.0998 0.1263 0.1200 0.0105 -0.0001 -0.0043 293 ASP A OD1 1631 O OD2 . ASP A 213 ? 0.1040 0.1351 0.1248 0.0092 -0.0006 -0.0035 293 ASP A OD2 1632 N N . ASN A 214 ? 0.0797 0.0986 0.0975 0.0101 -0.0001 -0.0047 294 ASN A N 1633 C CA . ASN A 214 ? 0.0909 0.1081 0.1094 0.0115 0.0004 -0.0053 294 ASN A CA 1634 C C . ASN A 214 ? 0.1262 0.1455 0.1461 0.0127 0.0011 -0.0059 294 ASN A C 1635 O O . ASN A 214 ? 0.1299 0.1478 0.1504 0.0140 0.0017 -0.0064 294 ASN A O 1636 C CB . ASN A 214 ? 0.1008 0.1156 0.1181 0.0108 0.0007 -0.0062 294 ASN A CB 1637 C CG . ASN A 214 ? 0.1542 0.1661 0.1718 0.0118 0.0010 -0.0065 294 ASN A CG 1638 O OD1 . ASN A 214 ? 0.1485 0.1588 0.1662 0.0122 0.0006 -0.0057 294 ASN A OD1 1639 N ND2 . ASN A 214 ? 0.1500 0.1612 0.1677 0.0122 0.0018 -0.0078 294 ASN A ND2 1640 N N . TRP A 215 ? 0.0854 0.1079 0.1056 0.0122 0.0011 -0.0058 295 TRP A N 1641 C CA . TRP A 215 ? 0.0900 0.1149 0.1114 0.0131 0.0018 -0.0064 295 TRP A CA 1642 C C . TRP A 215 ? 0.1143 0.1414 0.1374 0.0146 0.0017 -0.0057 295 TRP A C 1643 O O . TRP A 215 ? 0.0854 0.1120 0.1096 0.0163 0.0023 -0.0060 295 TRP A O 1644 C CB . TRP A 215 ? 0.1140 0.1416 0.1349 0.0117 0.0019 -0.0068 295 TRP A CB 1645 C CG . TRP A 215 ? 0.1019 0.1325 0.1239 0.0124 0.0026 -0.0074 295 TRP A CG 1646 C CD1 . TRP A 215 ? 0.1439 0.1749 0.1673 0.0142 0.0032 -0.0079 295 TRP A CD1 1647 C CD2 . TRP A 215 ? 0.0929 0.1266 0.1148 0.0114 0.0028 -0.0075 295 TRP A CD2 1648 N NE1 . TRP A 215 ? 0.1259 0.1603 0.1501 0.0143 0.0038 -0.0084 295 TRP A NE1 1649 C CE2 . TRP A 215 ? 0.0858 0.1219 0.1091 0.0126 0.0035 -0.0082 295 TRP A CE2 1650 C CE3 . TRP A 215 ? 0.0660 0.1005 0.0869 0.0095 0.0025 -0.0072 295 TRP A CE3 1651 C CZ2 . TRP A 215 ? 0.1219 0.1615 0.1456 0.0119 0.0039 -0.0085 295 TRP A CZ2 1652 C CZ3 . TRP A 215 ? 0.1021 0.1399 0.1233 0.0088 0.0029 -0.0074 295 TRP A CZ3 1653 C CH2 . TRP A 215 ? 0.1033 0.1436 0.1259 0.0100 0.0036 -0.0081 295 TRP A CH2 1654 N N . HIS A 216 ? 0.1055 0.1349 0.1288 0.0140 0.0011 -0.0048 296 HIS A N 1655 C CA . HIS A 216 ? 0.1068 0.1391 0.1318 0.0153 0.0009 -0.0041 296 HIS A CA 1656 C C . HIS A 216 ? 0.1078 0.1416 0.1327 0.0146 0.0000 -0.0030 296 HIS A C 1657 O O . HIS A 216 ? 0.0893 0.1270 0.1153 0.0147 -0.0002 -0.0027 296 HIS A O 1658 C CB . HIS A 216 ? 0.0930 0.1288 0.1190 0.0157 0.0015 -0.0047 296 HIS A CB 1659 C CG . HIS A 216 ? 0.1324 0.1703 0.1577 0.0136 0.0014 -0.0050 296 HIS A CG 1660 N ND1 . HIS A 216 ? 0.1125 0.1534 0.1384 0.0135 0.0020 -0.0057 296 HIS A ND1 1661 C CD2 . HIS A 216 ? 0.0911 0.1284 0.1151 0.0117 0.0009 -0.0047 296 HIS A CD2 1662 C CE1 . HIS A 216 ? 0.0933 0.1352 0.1183 0.0115 0.0019 -0.0057 296 HIS A CE1 1663 N NE2 . HIS A 216 ? 0.1455 0.1851 0.1693 0.0104 0.0012 -0.0052 296 HIS A NE2 1664 N N . GLY A 217 ? 0.1040 0.1351 0.1276 0.0138 -0.0006 -0.0026 297 GLY A N 1665 C CA . GLY A 217 ? 0.0933 0.1257 0.1167 0.0129 -0.0014 -0.0017 297 GLY A CA 1666 C C . GLY A 217 ? 0.1423 0.1720 0.1653 0.0134 -0.0019 -0.0009 297 GLY A C 1667 O O . GLY A 217 ? 0.0914 0.1175 0.1131 0.0129 -0.0018 -0.0012 297 GLY A O 1668 N N . SER A 218 ? 0.1172 0.1487 0.1410 0.0144 -0.0023 0.0000 298 SER A N 1669 C CA . SER A 218 ? 0.1230 0.1523 0.1463 0.0148 -0.0028 0.0009 298 SER A CA 1670 C C . SER A 218 ? 0.1057 0.1356 0.1280 0.0131 -0.0036 0.0013 298 SER A C 1671 O O . SER A 218 ? 0.1131 0.1411 0.1347 0.0131 -0.0040 0.0019 298 SER A O 1672 C CB . SER A 218 ? 0.1301 0.1606 0.1548 0.0171 -0.0028 0.0020 298 SER A CB 1673 O OG . SER A 218 ? 0.1864 0.2218 0.2123 0.0173 -0.0031 0.0023 298 SER A OG 1674 N N . ASN A 219 ? 0.0908 0.1233 0.1130 0.0116 -0.0037 0.0008 299 ASN A N 1675 C CA . ASN A 219 ? 0.1184 0.1507 0.1394 0.0096 -0.0042 0.0007 299 ASN A CA 1676 C C . ASN A 219 ? 0.0979 0.1274 0.1176 0.0082 -0.0039 -0.0001 299 ASN A C 1677 O O . ASN A 219 ? 0.1079 0.1365 0.1277 0.0086 -0.0033 -0.0006 299 ASN A O 1678 C CB . ASN A 219 ? 0.0952 0.1320 0.1169 0.0086 -0.0045 0.0007 299 ASN A CB 1679 C CG . ASN A 219 ? 0.0979 0.1372 0.1204 0.0085 -0.0039 0.0000 299 ASN A CG 1680 O OD1 . ASN A 219 ? 0.0725 0.1109 0.0955 0.0096 -0.0034 -0.0003 299 ASN A OD1 1681 N ND2 . ASN A 219 ? 0.1009 0.1433 0.1236 0.0069 -0.0040 -0.0004 299 ASN A ND2 1682 N N . ARG A 220 ? 0.1064 0.1346 0.1249 0.0066 -0.0042 -0.0001 300 ARG A N 1683 C CA . ARG A 220 ? 0.0948 0.1202 0.1119 0.0054 -0.0038 -0.0006 300 ARG A CA 1684 C C . ARG A 220 ? 0.0619 0.0891 0.0788 0.0038 -0.0035 -0.0011 300 ARG A C 1685 O O . ARG A 220 ? 0.0756 0.1051 0.0928 0.0028 -0.0037 -0.0011 300 ARG A O 1686 C CB . ARG A 220 ? 0.0869 0.1093 0.1027 0.0047 -0.0042 -0.0003 300 ARG A CB 1687 C CG . ARG A 220 ? 0.0744 0.0947 0.0903 0.0061 -0.0044 0.0002 300 ARG A CG 1688 C CD . ARG A 220 ? 0.0825 0.0995 0.0970 0.0054 -0.0046 0.0003 300 ARG A CD 1689 N NE . ARG A 220 ? 0.0656 0.0804 0.0801 0.0067 -0.0047 0.0007 300 ARG A NE 1690 C CZ . ARG A 220 ? 0.0720 0.0849 0.0866 0.0075 -0.0043 0.0003 300 ARG A CZ 1691 N NH1 . ARG A 220 ? 0.0652 0.0782 0.0797 0.0071 -0.0038 -0.0004 300 ARG A NH1 1692 N NH2 . ARG A 220 ? 0.0731 0.0840 0.0878 0.0085 -0.0043 0.0007 300 ARG A NH2 1693 N N . PRO A 221 ? 0.0713 0.0975 0.0878 0.0035 -0.0029 -0.0016 301 PRO A N 1694 C CA . PRO A 221 ? 0.0882 0.1155 0.1043 0.0019 -0.0025 -0.0019 301 PRO A CA 1695 C C . PRO A 221 ? 0.0831 0.1079 0.0978 0.0004 -0.0025 -0.0017 301 PRO A C 1696 O O . PRO A 221 ? 0.0747 0.0966 0.0885 0.0008 -0.0028 -0.0015 301 PRO A O 1697 C CB . PRO A 221 ? 0.0590 0.0858 0.0750 0.0024 -0.0018 -0.0024 301 PRO A CB 1698 C CG . PRO A 221 ? 0.0756 0.0994 0.0911 0.0036 -0.0020 -0.0023 301 PRO A CG 1699 C CD . PRO A 221 ? 0.0639 0.0879 0.0802 0.0046 -0.0026 -0.0018 301 PRO A CD 1700 N N . TRP A 222 ? 0.0603 0.0860 0.0746 -0.0012 -0.0022 -0.0019 302 TRP A N 1701 C CA . TRP A 222 ? 0.0851 0.1084 0.0981 -0.0026 -0.0020 -0.0017 302 TRP A CA 1702 C C . TRP A 222 ? 0.0963 0.1196 0.1087 -0.0038 -0.0012 -0.0018 302 TRP A C 1703 O O . TRP A 222 ? 0.0807 0.1067 0.0939 -0.0040 -0.0008 -0.0021 302 TRP A O 1704 C CB . TRP A 222 ? 0.0659 0.0896 0.0788 -0.0035 -0.0024 -0.0017 302 TRP A CB 1705 C CG . TRP A 222 ? 0.0709 0.0982 0.0848 -0.0045 -0.0023 -0.0020 302 TRP A CG 1706 C CD1 . TRP A 222 ? 0.0800 0.1105 0.0952 -0.0038 -0.0028 -0.0021 302 TRP A CD1 1707 C CD2 . TRP A 222 ? 0.0752 0.1034 0.0890 -0.0064 -0.0016 -0.0024 302 TRP A CD2 1708 N NE1 . TRP A 222 ? 0.0746 0.1083 0.0905 -0.0052 -0.0026 -0.0025 302 TRP A NE1 1709 C CE2 . TRP A 222 ? 0.0745 0.1067 0.0896 -0.0068 -0.0018 -0.0027 302 TRP A CE2 1710 C CE3 . TRP A 222 ? 0.0695 0.0955 0.0822 -0.0076 -0.0009 -0.0023 302 TRP A CE3 1711 C CZ2 . TRP A 222 ? 0.0892 0.1233 0.1045 -0.0087 -0.0012 -0.0032 302 TRP A CZ2 1712 C CZ3 . TRP A 222 ? 0.1024 0.1300 0.1153 -0.0094 -0.0002 -0.0027 302 TRP A CZ3 1713 C CH2 . TRP A 222 ? 0.1244 0.1560 0.1387 -0.0100 -0.0004 -0.0032 302 TRP A CH2 1714 N N . VAL A 223 ? 0.1014 0.1219 0.1125 -0.0046 -0.0009 -0.0016 303 VAL A N 1715 C CA . VAL A 223 ? 0.0810 0.1012 0.0914 -0.0058 -0.0001 -0.0014 303 VAL A CA 1716 C C . VAL A 223 ? 0.0779 0.0954 0.0872 -0.0070 0.0001 -0.0011 303 VAL A C 1717 O O . VAL A 223 ? 0.0799 0.0949 0.0884 -0.0064 -0.0003 -0.0008 303 VAL A O 1718 C CB . VAL A 223 ? 0.0654 0.0848 0.0752 -0.0051 0.0003 -0.0013 303 VAL A CB 1719 C CG1 . VAL A 223 ? 0.0704 0.0871 0.0793 -0.0041 -0.0001 -0.0010 303 VAL A CG1 1720 C CG2 . VAL A 223 ? 0.0612 0.0802 0.0702 -0.0064 0.0012 -0.0009 303 VAL A CG2 1721 N N . SER A 224 ? 0.0767 0.0946 0.0859 -0.0086 0.0008 -0.0012 304 SER A N 1722 C CA . SER A 224 ? 0.0849 0.1000 0.0930 -0.0098 0.0012 -0.0009 304 SER A CA 1723 C C . SER A 224 ? 0.1162 0.1305 0.1237 -0.0108 0.0023 -0.0005 304 SER A C 1724 O O . SER A 224 ? 0.1001 0.1166 0.1082 -0.0112 0.0028 -0.0007 304 SER A O 1725 C CB . SER A 224 ? 0.1345 0.1505 0.1431 -0.0109 0.0010 -0.0015 304 SER A CB 1726 O OG . SER A 224 ? 0.2215 0.2405 0.2311 -0.0121 0.0015 -0.0020 304 SER A OG 1727 N N . PHE A 225 ? 0.0612 0.0723 0.0675 -0.0111 0.0028 0.0001 305 PHE A N 1728 C CA . PHE A 225 ? 0.1096 0.1194 0.1151 -0.0120 0.0040 0.0007 305 PHE A CA 1729 C C . PHE A 225 ? 0.1050 0.1112 0.1093 -0.0127 0.0046 0.0012 305 PHE A C 1730 O O . PHE A 225 ? 0.0931 0.0975 0.0971 -0.0121 0.0041 0.0012 305 PHE A O 1731 C CB . PHE A 225 ? 0.0557 0.0658 0.0607 -0.0107 0.0040 0.0013 305 PHE A CB 1732 C CG . PHE A 225 ? 0.0580 0.0666 0.0624 -0.0091 0.0032 0.0015 305 PHE A CG 1733 C CD1 . PHE A 225 ? 0.0858 0.0915 0.0890 -0.0088 0.0035 0.0023 305 PHE A CD1 1734 C CD2 . PHE A 225 ? 0.0729 0.0830 0.0781 -0.0079 0.0022 0.0009 305 PHE A CD2 1735 C CE1 . PHE A 225 ? 0.0660 0.0707 0.0687 -0.0075 0.0028 0.0025 305 PHE A CE1 1736 C CE2 . PHE A 225 ? 0.0737 0.0824 0.0784 -0.0067 0.0016 0.0011 305 PHE A CE2 1737 C CZ . PHE A 225 ? 0.0608 0.0670 0.0644 -0.0065 0.0018 0.0018 305 PHE A CZ 1738 N N . ASN A 226 ? 0.0909 0.0961 0.0948 -0.0139 0.0058 0.0017 306 ASN A N 1739 C CA . ASN A 226 ? 0.1382 0.1397 0.1409 -0.0144 0.0067 0.0023 306 ASN A CA 1740 C C . ASN A 226 ? 0.0869 0.0867 0.0886 -0.0131 0.0069 0.0036 306 ASN A C 1741 O O . ASN A 226 ? 0.0849 0.0864 0.0866 -0.0119 0.0064 0.0038 306 ASN A O 1742 C CB . ASN A 226 ? 0.1104 0.1113 0.1133 -0.0164 0.0081 0.0022 306 ASN A CB 1743 C CG . ASN A 226 ? 0.1809 0.1833 0.1838 -0.0169 0.0089 0.0027 306 ASN A CG 1744 O OD1 . ASN A 226 ? 0.1000 0.1030 0.1025 -0.0156 0.0088 0.0035 306 ASN A OD1 1745 N ND2 . ASN A 226 ? 0.1364 0.1398 0.1399 -0.0188 0.0098 0.0021 306 ASN A ND2 1746 N N . GLN A 227 ? 0.1020 0.0985 0.1027 -0.0133 0.0078 0.0044 308 GLN A N 1747 C CA . GLN A 227 ? 0.1249 0.1198 0.1244 -0.0120 0.0080 0.0058 308 GLN A CA 1748 C C . GLN A 227 ? 0.1564 0.1528 0.1556 -0.0118 0.0086 0.0066 308 GLN A C 1749 O O . GLN A 227 ? 0.1456 0.1421 0.1440 -0.0105 0.0085 0.0075 308 GLN A O 1750 C CB . GLN A 227 ? 0.1413 0.1325 0.1399 -0.0121 0.0089 0.0066 308 GLN A CB 1751 C CG . GLN A 227 ? 0.1185 0.1082 0.1172 -0.0120 0.0082 0.0059 308 GLN A CG 1752 C CD . GLN A 227 ? 0.1457 0.1317 0.1438 -0.0125 0.0094 0.0064 308 GLN A CD 1753 O OE1 . GLN A 227 ? 0.2141 0.1981 0.2112 -0.0115 0.0099 0.0077 308 GLN A OE1 1754 N NE2 . GLN A 227 ? 0.2317 0.2168 0.2301 -0.0140 0.0097 0.0054 308 GLN A NE2 1755 N N . ASN A 228 ? 0.0946 0.0923 0.0943 -0.0133 0.0094 0.0063 309 ASN A N 1756 C CA . ASN A 228 ? 0.1060 0.1053 0.1055 -0.0133 0.0101 0.0070 309 ASN A CA 1757 C C . ASN A 228 ? 0.1051 0.1083 0.1055 -0.0126 0.0091 0.0061 309 ASN A C 1758 O O . ASN A 228 ? 0.1422 0.1473 0.1425 -0.0127 0.0095 0.0065 309 ASN A O 1759 C CB . ASN A 228 ? 0.1435 0.1423 0.1432 -0.0152 0.0115 0.0071 309 ASN A CB 1760 C CG . ASN A 228 ? 0.3184 0.3133 0.3169 -0.0155 0.0129 0.0084 309 ASN A CG 1761 O OD1 . ASN A 228 ? 0.3585 0.3514 0.3562 -0.0142 0.0127 0.0094 309 ASN A OD1 1762 N ND2 . ASN A 228 ? 0.4344 0.4282 0.4330 -0.0173 0.0143 0.0085 309 ASN A ND2 1763 N N . LEU A 229 ? 0.0877 0.0919 0.0888 -0.0120 0.0078 0.0051 310 LEU A N 1764 C CA . LEU A 229 ? 0.1154 0.1228 0.1174 -0.0111 0.0069 0.0043 310 LEU A CA 1765 C C . LEU A 229 ? 0.1003 0.1106 0.1035 -0.0122 0.0071 0.0035 310 LEU A C 1766 O O . LEU A 229 ? 0.1210 0.1341 0.1249 -0.0116 0.0068 0.0030 310 LEU A O 1767 C CB . LEU A 229 ? 0.1068 0.1150 0.1080 -0.0099 0.0068 0.0049 310 LEU A CB 1768 C CG . LEU A 229 ? 0.1090 0.1151 0.1092 -0.0086 0.0065 0.0057 310 LEU A CG 1769 C CD1 . LEU A 229 ? 0.1212 0.1291 0.1208 -0.0074 0.0062 0.0059 310 LEU A CD1 1770 C CD2 . LEU A 229 ? 0.1000 0.1050 0.1005 -0.0081 0.0054 0.0050 310 LEU A CD2 1771 N N . GLU A 230 ? 0.0811 0.0908 0.0847 -0.0139 0.0078 0.0032 311 GLU A N 1772 C CA . GLU A 230 ? 0.1168 0.1295 0.1217 -0.0150 0.0079 0.0023 311 GLU A CA 1773 C C . GLU A 230 ? 0.1003 0.1145 0.1062 -0.0145 0.0067 0.0012 311 GLU A C 1774 O O . GLU A 230 ? 0.1380 0.1505 0.1438 -0.0147 0.0063 0.0009 311 GLU A O 1775 C CB . GLU A 230 ? 0.1082 0.1196 0.1130 -0.0172 0.0091 0.0023 311 GLU A CB 1776 C CG . GLU A 230 ? 0.1806 0.1904 0.1843 -0.0177 0.0106 0.0035 311 GLU A CG 1777 C CD . GLU A 230 ? 0.2810 0.2885 0.2845 -0.0198 0.0119 0.0036 311 GLU A CD 1778 O OE1 . GLU A 230 ? 0.2530 0.2591 0.2567 -0.0205 0.0118 0.0029 311 GLU A OE1 1779 O OE2 . GLU A 230 ? 0.2852 0.2922 0.2882 -0.0206 0.0132 0.0044 311 GLU A OE2 1780 N N . TYR A 231 ? 0.0658 0.0832 0.0727 -0.0136 0.0060 0.0006 312 TYR A N 1781 C CA . TYR A 231 ? 0.0892 0.1078 0.0970 -0.0125 0.0048 -0.0001 312 TYR A CA 1782 C C . TYR A 231 ? 0.1290 0.1514 0.1384 -0.0131 0.0045 -0.0010 312 TYR A C 1783 O O . TYR A 231 ? 0.0870 0.1116 0.0969 -0.0141 0.0052 -0.0012 312 TYR A O 1784 C CB . TYR A 231 ? 0.0631 0.0820 0.0708 -0.0106 0.0041 0.0000 312 TYR A CB 1785 C CG . TYR A 231 ? 0.0845 0.1062 0.0927 -0.0102 0.0045 -0.0001 312 TYR A CG 1786 C CD1 . TYR A 231 ? 0.0732 0.0982 0.0828 -0.0098 0.0041 -0.0009 312 TYR A CD1 1787 C CD2 . TYR A 231 ? 0.0619 0.0831 0.0691 -0.0101 0.0052 0.0005 312 TYR A CD2 1788 C CE1 . TYR A 231 ? 0.0762 0.1039 0.0863 -0.0095 0.0044 -0.0011 312 TYR A CE1 1789 C CE2 . TYR A 231 ? 0.1011 0.1251 0.1087 -0.0098 0.0055 0.0003 312 TYR A CE2 1790 C CZ . TYR A 231 ? 0.0701 0.0972 0.0793 -0.0095 0.0052 -0.0006 312 TYR A CZ 1791 O OH . TYR A 231 ? 0.0983 0.1281 0.1079 -0.0092 0.0056 -0.0009 312 TYR A OH 1792 N N . GLN A 232 ? 0.0569 0.0800 0.0670 -0.0123 0.0035 -0.0015 313 GLN A N 1793 C CA . GLN A 232 ? 0.1042 0.1311 0.1158 -0.0122 0.0030 -0.0022 313 GLN A CA 1794 C C . GLN A 232 ? 0.0834 0.1108 0.0955 -0.0102 0.0020 -0.0022 313 GLN A C 1795 O O . GLN A 232 ? 0.0658 0.0904 0.0771 -0.0092 0.0015 -0.0019 313 GLN A O 1796 C CB . GLN A 232 ? 0.1339 0.1615 0.1460 -0.0137 0.0029 -0.0027 313 GLN A CB 1797 C CG . GLN A 232 ? 0.2271 0.2541 0.2388 -0.0160 0.0040 -0.0029 313 GLN A CG 1798 C CD . GLN A 232 ? 0.3816 0.4095 0.3937 -0.0175 0.0039 -0.0036 313 GLN A CD 1799 O OE1 . GLN A 232 ? 0.4337 0.4595 0.4452 -0.0174 0.0035 -0.0037 313 GLN A OE1 1800 N NE2 . GLN A 232 ? 0.4533 0.4845 0.4665 -0.0190 0.0043 -0.0043 313 GLN A NE2 1801 N N . ILE A 233 ? 0.0748 0.1057 0.0883 -0.0094 0.0017 -0.0027 314 ILE A N 1802 C CA . ILE A 233 ? 0.0468 0.0781 0.0609 -0.0073 0.0009 -0.0027 314 ILE A CA 1803 C C . ILE A 233 ? 0.1086 0.1434 0.1242 -0.0069 0.0003 -0.0030 314 ILE A C 1804 O O . ILE A 233 ? 0.0657 0.1035 0.0822 -0.0081 0.0005 -0.0034 314 ILE A O 1805 C CB . ILE A 233 ? 0.0776 0.1095 0.0918 -0.0061 0.0012 -0.0027 314 ILE A CB 1806 C CG1 . ILE A 233 ? 0.1057 0.1411 0.1209 -0.0068 0.0018 -0.0031 314 ILE A CG1 1807 C CG2 . ILE A 233 ? 0.1122 0.1408 0.1248 -0.0061 0.0016 -0.0023 314 ILE A CG2 1808 C CD1 . ILE A 233 ? 0.1571 0.1935 0.1724 -0.0056 0.0022 -0.0032 314 ILE A CD1 1809 N N . GLY A 234 ? 0.1028 0.1372 0.1188 -0.0052 -0.0005 -0.0029 315 GLY A N 1810 C CA . GLY A 234 ? 0.1239 0.1616 0.1414 -0.0044 -0.0011 -0.0030 315 GLY A CA 1811 C C . GLY A 234 ? 0.1061 0.1425 0.1238 -0.0024 -0.0018 -0.0026 315 GLY A C 1812 O O . GLY A 234 ? 0.1234 0.1565 0.1401 -0.0017 -0.0017 -0.0025 315 GLY A O 1813 N N . TYR A 235 ? 0.0702 0.1092 0.0890 -0.0016 -0.0024 -0.0025 316 TYR A N 1814 C CA . TYR A 235 ? 0.0899 0.1276 0.1088 0.0002 -0.0030 -0.0020 316 TYR A CA 1815 C C . TYR A 235 ? 0.0817 0.1206 0.1007 -0.0003 -0.0037 -0.0018 316 TYR A C 1816 O O . TYR A 235 ? 0.0999 0.1419 0.1194 -0.0015 -0.0037 -0.0021 316 TYR A O 1817 C CB . TYR A 235 ? 0.0985 0.1387 0.1189 0.0022 -0.0030 -0.0019 316 TYR A CB 1818 C CG . TYR A 235 ? 0.0979 0.1362 0.1182 0.0033 -0.0024 -0.0021 316 TYR A CG 1819 C CD1 . TYR A 235 ? 0.1113 0.1503 0.1315 0.0025 -0.0017 -0.0027 316 TYR A CD1 1820 C CD2 . TYR A 235 ? 0.1031 0.1388 0.1233 0.0050 -0.0025 -0.0019 316 TYR A CD2 1821 C CE1 . TYR A 235 ? 0.1130 0.1505 0.1330 0.0034 -0.0012 -0.0030 316 TYR A CE1 1822 C CE2 . TYR A 235 ? 0.0708 0.1049 0.0909 0.0058 -0.0020 -0.0023 316 TYR A CE2 1823 C CZ . TYR A 235 ? 0.1075 0.1426 0.1274 0.0050 -0.0013 -0.0029 316 TYR A CZ 1824 O OH . TYR A 235 ? 0.0882 0.1219 0.1079 0.0058 -0.0008 -0.0034 316 TYR A OH 1825 N N . ILE A 236 ? 0.0468 0.0831 0.0652 0.0006 -0.0041 -0.0013 317 ILE A N 1826 C CA . ILE A 236 ? 0.0555 0.0930 0.0738 0.0004 -0.0048 -0.0010 317 ILE A CA 1827 C C . ILE A 236 ? 0.0555 0.0975 0.0755 0.0016 -0.0052 -0.0006 317 ILE A C 1828 O O . ILE A 236 ? 0.0579 0.1002 0.0788 0.0036 -0.0052 -0.0002 317 ILE A O 1829 C CB . ILE A 236 ? 0.0682 0.1021 0.0856 0.0012 -0.0052 -0.0004 317 ILE A CB 1830 C CG1 . ILE A 236 ? 0.0766 0.1065 0.0925 0.0000 -0.0048 -0.0007 317 ILE A CG1 1831 C CG2 . ILE A 236 ? 0.0705 0.1060 0.0879 0.0010 -0.0059 -0.0001 317 ILE A CG2 1832 C CD1 . ILE A 236 ? 0.0439 0.0703 0.0589 0.0007 -0.0052 -0.0002 317 ILE A CD1 1833 N N . CYS A 237 ? 0.0778 0.1233 0.0982 0.0003 -0.0055 -0.0009 318 CYS A N 1834 C CA . CYS A 237 ? 0.0915 0.1421 0.1135 0.0012 -0.0058 -0.0007 318 CYS A CA 1835 C C . CYS A 237 ? 0.1239 0.1757 0.1463 0.0029 -0.0065 0.0003 318 CYS A C 1836 O O . CYS A 237 ? 0.1216 0.1770 0.1455 0.0045 -0.0068 0.0008 318 CYS A O 1837 C CB . CYS A 237 ? 0.1122 0.1666 0.1346 -0.0010 -0.0058 -0.0015 318 CYS A CB 1838 S SG . CYS A 237 ? 0.1728 0.2267 0.1950 -0.0030 -0.0048 -0.0025 318 CYS A SG 1839 N N . SER A 238 ? 0.0887 0.1375 0.1100 0.0028 -0.0069 0.0006 319 SER A N 1840 C CA . SER A 238 ? 0.0992 0.1491 0.1207 0.0042 -0.0076 0.0016 319 SER A CA 1841 C C . SER A 238 ? 0.1283 0.1786 0.1509 0.0070 -0.0076 0.0026 319 SER A C 1842 O O . SER A 238 ? 0.0904 0.1377 0.1131 0.0079 -0.0070 0.0026 319 SER A O 1843 C CB . SER A 238 ? 0.1378 0.1836 0.1577 0.0037 -0.0078 0.0018 319 SER A CB 1844 O OG . SER A 238 ? 0.1213 0.1681 0.1413 0.0051 -0.0084 0.0028 319 SER A OG 1845 N N . GLY A 239 ? 0.1299 0.1839 0.1534 0.0082 -0.0081 0.0035 320 GLY A N 1846 C CA . GLY A 239 ? 0.1213 0.1756 0.1459 0.0110 -0.0081 0.0047 320 GLY A CA 1847 C C . GLY A 239 ? 0.1865 0.2363 0.2102 0.0121 -0.0081 0.0055 320 GLY A C 1848 O O . GLY A 239 ? 0.1462 0.1949 0.1706 0.0143 -0.0079 0.0065 320 GLY A O 1849 N N . ILE A 240 ? 0.1008 0.1477 0.1229 0.0104 -0.0083 0.0051 321 ILE A N 1850 C CA . ILE A 240 ? 0.1320 0.1742 0.1531 0.0110 -0.0082 0.0056 321 ILE A CA 1851 C C . ILE A 240 ? 0.1128 0.1508 0.1334 0.0109 -0.0075 0.0049 321 ILE A C 1852 O O . ILE A 240 ? 0.1413 0.1769 0.1609 0.0091 -0.0074 0.0040 321 ILE A O 1853 C CB . ILE A 240 ? 0.1218 0.1628 0.1413 0.0093 -0.0087 0.0054 321 ILE A CB 1854 C CG1 . ILE A 240 ? 0.1745 0.2203 0.1944 0.0089 -0.0094 0.0057 321 ILE A CG1 1855 C CG2 . ILE A 240 ? 0.1066 0.1431 0.1252 0.0100 -0.0086 0.0060 321 ILE A CG2 1856 C CD1 . ILE A 240 ? 0.2089 0.2560 0.2293 0.0111 -0.0098 0.0073 321 ILE A CD1 1857 N N . PHE A 241 ? 0.1056 0.1430 0.1273 0.0127 -0.0070 0.0052 322 PHE A N 1858 C CA . PHE A 241 ? 0.1368 0.1710 0.1583 0.0126 -0.0063 0.0043 322 PHE A CA 1859 C C . PHE A 241 ? 0.1214 0.1507 0.1415 0.0121 -0.0061 0.0042 322 PHE A C 1860 O O . PHE A 241 ? 0.1227 0.1503 0.1425 0.0129 -0.0063 0.0051 322 PHE A O 1861 C CB . PHE A 241 ? 0.1255 0.1600 0.1484 0.0147 -0.0057 0.0046 322 PHE A CB 1862 C CG . PHE A 241 ? 0.1418 0.1814 0.1662 0.0155 -0.0058 0.0049 322 PHE A CG 1863 C CD1 . PHE A 241 ? 0.1240 0.1666 0.1486 0.0140 -0.0058 0.0040 322 PHE A CD1 1864 C CD2 . PHE A 241 ? 0.1412 0.1826 0.1668 0.0178 -0.0058 0.0061 322 PHE A CD2 1865 C CE1 . PHE A 241 ? 0.1168 0.1644 0.1430 0.0147 -0.0058 0.0042 322 PHE A CE1 1866 C CE2 . PHE A 241 ? 0.1819 0.2284 0.2090 0.0186 -0.0059 0.0064 322 PHE A CE2 1867 C CZ . PHE A 241 ? 0.1574 0.2070 0.1848 0.0171 -0.0059 0.0054 322 PHE A CZ 1868 N N . GLY A 242 ? 0.1016 0.1288 0.1208 0.0107 -0.0058 0.0032 323 GLY A N 1869 C CA . GLY A 242 ? 0.1013 0.1244 0.1192 0.0099 -0.0058 0.0030 323 GLY A CA 1870 C C . GLY A 242 ? 0.0936 0.1133 0.1113 0.0107 -0.0052 0.0027 323 GLY A C 1871 O O . GLY A 242 ? 0.1155 0.1319 0.1322 0.0105 -0.0052 0.0027 323 GLY A O 1872 N N . ASP A 243 ? 0.0640 0.0845 0.0827 0.0116 -0.0046 0.0023 324 ASP A N 1873 C CA . ASP A 243 ? 0.0856 0.1031 0.1042 0.0122 -0.0040 0.0017 324 ASP A CA 1874 C C . ASP A 243 ? 0.1191 0.1348 0.1383 0.0140 -0.0037 0.0024 324 ASP A C 1875 O O . ASP A 243 ? 0.1072 0.1243 0.1270 0.0150 -0.0040 0.0035 324 ASP A O 1876 C CB . ASP A 243 ? 0.1062 0.1252 0.1255 0.0123 -0.0034 0.0009 324 ASP A CB 1877 C CG . ASP A 243 ? 0.1558 0.1719 0.1743 0.0120 -0.0028 -0.0001 324 ASP A CG 1878 O OD1 . ASP A 243 ? 0.0738 0.0869 0.0915 0.0117 -0.0029 -0.0001 324 ASP A OD1 1879 O OD2 . ASP A 243 ? 0.0956 0.1128 0.1144 0.0120 -0.0023 -0.0009 324 ASP A OD2 1880 N N . ASN A 244 ? 0.1227 0.1354 0.1418 0.0144 -0.0031 0.0018 325 ASN A N 1881 C CA . ASN A 244 ? 0.1258 0.1364 0.1456 0.0161 -0.0025 0.0023 325 ASN A CA 1882 C C . ASN A 244 ? 0.1415 0.1506 0.1617 0.0166 -0.0016 0.0011 325 ASN A C 1883 O O . ASN A 244 ? 0.1334 0.1409 0.1527 0.0154 -0.0014 0.0001 325 ASN A O 1884 C CB . ASN A 244 ? 0.1196 0.1271 0.1384 0.0157 -0.0028 0.0027 325 ASN A CB 1885 C CG . ASN A 244 ? 0.1726 0.1775 0.1920 0.0173 -0.0021 0.0033 325 ASN A CG 1886 O OD1 . ASN A 244 ? 0.1987 0.2009 0.2181 0.0174 -0.0014 0.0024 325 ASN A OD1 1887 N ND2 . ASN A 244 ? 0.1576 0.1634 0.1776 0.0185 -0.0023 0.0047 325 ASN A ND2 1888 N N . PRO A 245 ? 0.1463 0.1562 0.1679 0.0183 -0.0010 0.0013 326 PRO A N 1889 C CA . PRO A 245 ? 0.1520 0.1639 0.1747 0.0200 -0.0011 0.0027 326 PRO A CA 1890 C C . PRO A 245 ? 0.1577 0.1742 0.1809 0.0196 -0.0018 0.0030 326 PRO A C 1891 O O . PRO A 245 ? 0.1119 0.1298 0.1345 0.0181 -0.0020 0.0022 326 PRO A O 1892 C CB . PRO A 245 ? 0.1665 0.1775 0.1906 0.0219 0.0000 0.0024 326 PRO A CB 1893 C CG . PRO A 245 ? 0.1997 0.2105 0.2235 0.0209 0.0005 0.0007 326 PRO A CG 1894 C CD . PRO A 245 ? 0.1725 0.1814 0.1946 0.0189 0.0000 0.0001 326 PRO A CD 1895 N N . ARG A 246 ? 0.0823 0.1012 0.1065 0.0211 -0.0020 0.0043 327 ARG A N 1896 C CA . ARG A 246 ? 0.0898 0.1135 0.1146 0.0208 -0.0027 0.0047 327 ARG A CA 1897 C C . ARG A 246 ? 0.1206 0.1466 0.1468 0.0231 -0.0026 0.0061 327 ARG A C 1898 O O . ARG A 246 ? 0.1243 0.1478 0.1507 0.0246 -0.0022 0.0070 327 ARG A O 1899 C CB . ARG A 246 ? 0.1021 0.1265 0.1256 0.0189 -0.0036 0.0048 327 ARG A CB 1900 C CG . ARG A 246 ? 0.0957 0.1186 0.1187 0.0193 -0.0040 0.0061 327 ARG A CG 1901 C CD . ARG A 246 ? 0.0778 0.1018 0.0996 0.0175 -0.0050 0.0061 327 ARG A CD 1902 N NE . ARG A 246 ? 0.0672 0.0901 0.0885 0.0180 -0.0054 0.0073 327 ARG A NE 1903 C CZ . ARG A 246 ? 0.0868 0.1060 0.1069 0.0173 -0.0053 0.0073 327 ARG A CZ 1904 N NH1 . ARG A 246 ? 0.0758 0.0921 0.0951 0.0161 -0.0050 0.0061 327 ARG A NH1 1905 N NH2 . ARG A 246 ? 0.0617 0.0803 0.0814 0.0178 -0.0057 0.0084 327 ARG A NH2 1906 N N . PRO A 247 ? 0.1151 0.1459 0.1422 0.0233 -0.0031 0.0064 328 PRO A N 1907 C CA . PRO A 247 ? 0.1360 0.1698 0.1644 0.0254 -0.0032 0.0080 328 PRO A CA 1908 C C . PRO A 247 ? 0.1470 0.1816 0.1746 0.0249 -0.0042 0.0092 328 PRO A C 1909 O O . PRO A 247 ? 0.1118 0.1451 0.1380 0.0228 -0.0047 0.0086 328 PRO A O 1910 C CB . PRO A 247 ? 0.1362 0.1753 0.1657 0.0252 -0.0034 0.0076 328 PRO A CB 1911 C CG . PRO A 247 ? 0.1762 0.2145 0.2051 0.0234 -0.0031 0.0059 328 PRO A CG 1912 C CD . PRO A 247 ? 0.1413 0.1753 0.1685 0.0217 -0.0033 0.0053 328 PRO A CD 1913 N N . ASN A 248 ? 0.1353 0.1721 0.1638 0.0268 -0.0043 0.0108 329 ASN A N 1914 C CA . ASN A 248 ? 0.1679 0.2068 0.1957 0.0264 -0.0053 0.0119 329 ASN A CA 1915 C C . ASN A 248 ? 0.1507 0.1943 0.1784 0.0244 -0.0061 0.0111 329 ASN A C 1916 O O . ASN A 248 ? 0.1769 0.2234 0.2056 0.0242 -0.0060 0.0103 329 ASN A O 1917 C CB . ASN A 248 ? 0.1796 0.2208 0.2086 0.0290 -0.0053 0.0139 329 ASN A CB 1918 C CG . ASN A 248 ? 0.2731 0.3093 0.3019 0.0307 -0.0045 0.0150 329 ASN A CG 1919 O OD1 . ASN A 248 ? 0.2240 0.2568 0.2515 0.0297 -0.0047 0.0150 329 ASN A OD1 1920 N ND2 . ASN A 248 ? 0.2638 0.2997 0.2941 0.0333 -0.0036 0.0158 329 ASN A ND2 1921 N N . ASP A 249 ? 0.1492 0.1934 0.1757 0.0228 -0.0070 0.0112 330 ASP A N 1922 C CA . ASP A 249 ? 0.1315 0.1796 0.1577 0.0207 -0.0076 0.0102 330 ASP A CA 1923 C C . ASP A 249 ? 0.2325 0.2868 0.2603 0.0216 -0.0079 0.0107 330 ASP A C 1924 O O . ASP A 249 ? 0.1805 0.2372 0.2091 0.0236 -0.0081 0.0122 330 ASP A O 1925 C CB . ASP A 249 ? 0.1540 0.2020 0.1788 0.0192 -0.0084 0.0105 330 ASP A CB 1926 C CG . ASP A 249 ? 0.1810 0.2234 0.2042 0.0178 -0.0082 0.0098 330 ASP A CG 1927 O OD1 . ASP A 249 ? 0.1531 0.1924 0.1761 0.0174 -0.0076 0.0088 330 ASP A OD1 1928 O OD2 . ASP A 249 ? 0.1740 0.2154 0.1960 0.0172 -0.0087 0.0102 330 ASP A OD2 1929 N N . LYS A 250 ? 0.2068 0.2637 0.2349 0.0200 -0.0079 0.0094 331 LYS A N 1930 C CA . LYS A 250 ? 0.2267 0.2899 0.2563 0.0205 -0.0082 0.0095 331 LYS A CA 1931 C C . LYS A 250 ? 0.2403 0.3060 0.2696 0.0177 -0.0084 0.0079 331 LYS A C 1932 O O . LYS A 250 ? 0.2842 0.3486 0.3121 0.0155 -0.0088 0.0072 331 LYS A O 1933 C CB . LYS A 250 ? 0.2131 0.2768 0.2444 0.0229 -0.0074 0.0099 331 LYS A CB 1934 C CG . LYS A 250 ? 0.2674 0.3269 0.2984 0.0224 -0.0065 0.0086 331 LYS A CG 1935 C CD . LYS A 250 ? 0.3973 0.4575 0.4300 0.0248 -0.0057 0.0089 331 LYS A CD 1936 C CE . LYS A 250 ? 0.4799 0.5358 0.5123 0.0244 -0.0048 0.0076 331 LYS A CE 1937 N NZ . LYS A 250 ? 0.5061 0.5622 0.5400 0.0268 -0.0039 0.0078 331 LYS A NZ 1938 N N . THR A 251 ? 0.1990 0.2683 0.2296 0.0179 -0.0081 0.0074 332 THR A N 1939 C CA . THR A 251 ? 0.1534 0.2248 0.1839 0.0152 -0.0081 0.0058 332 THR A CA 1940 C C . THR A 251 ? 0.1602 0.2269 0.1900 0.0142 -0.0073 0.0047 332 THR A C 1941 O O . THR A 251 ? 0.1841 0.2492 0.2146 0.0158 -0.0066 0.0048 332 THR A O 1942 C CB . THR A 251 ? 0.2368 0.3147 0.2692 0.0156 -0.0082 0.0057 332 THR A CB 1943 O OG1 . THR A 251 ? 0.2637 0.3466 0.2966 0.0162 -0.0090 0.0067 332 THR A OG1 1944 C CG2 . THR A 251 ? 0.1755 0.2550 0.2077 0.0127 -0.0080 0.0041 332 THR A CG2 1945 N N . GLY A 252 ? 0.1672 0.2317 0.1955 0.0116 -0.0074 0.0037 333 GLY A N 1946 C CA . GLY A 252 ? 0.1535 0.2136 0.1809 0.0106 -0.0067 0.0028 333 GLY A CA 1947 C C . GLY A 252 ? 0.1748 0.2373 0.2029 0.0094 -0.0061 0.0017 333 GLY A C 1948 O O . GLY A 252 ? 0.1586 0.2262 0.1880 0.0096 -0.0062 0.0017 333 GLY A O 1949 N N . SER A 253 ? 0.1517 0.2105 0.1787 0.0081 -0.0056 0.0009 335 SER A N 1950 C CA . SER A 253 ? 0.1642 0.2246 0.1916 0.0069 -0.0049 -0.0001 335 SER A CA 1951 C C . SER A 253 ? 0.1580 0.2148 0.1837 0.0046 -0.0046 -0.0008 335 SER A C 1952 O O . SER A 253 ? 0.1576 0.2098 0.1821 0.0047 -0.0046 -0.0007 335 SER A O 1953 C CB . SER A 253 ? 0.1728 0.2331 0.2012 0.0088 -0.0043 -0.0001 335 SER A CB 1954 O OG . SER A 253 ? 0.2310 0.2924 0.2596 0.0075 -0.0036 -0.0010 335 SER A OG 1955 N N . CYS A 254 ? 0.1614 0.2203 0.1873 0.0026 -0.0042 -0.0016 336 CYS A N 1956 C CA . CYS A 254 ? 0.2178 0.2734 0.2422 0.0006 -0.0037 -0.0022 336 CYS A CA 1957 C C . CYS A 254 ? 0.1590 0.2123 0.1831 0.0012 -0.0030 -0.0025 336 CYS A C 1958 O O . CYS A 254 ? 0.1896 0.2404 0.2126 -0.0002 -0.0025 -0.0028 336 CYS A O 1959 C CB . CYS A 254 ? 0.2063 0.2647 0.2308 -0.0019 -0.0035 -0.0030 336 CYS A CB 1960 S SG . CYS A 254 ? 0.4484 0.5086 0.4726 -0.0031 -0.0043 -0.0030 336 CYS A SG 1961 N N . GLY A 255 ? 0.1674 0.2219 0.1927 0.0033 -0.0029 -0.0022 339 GLY A N 1962 C CA . GLY A 255 ? 0.1793 0.2316 0.2044 0.0042 -0.0022 -0.0025 339 GLY A CA 1963 C C . GLY A 255 ? 0.1581 0.2074 0.1831 0.0063 -0.0024 -0.0020 339 GLY A C 1964 O O . GLY A 255 ? 0.1460 0.1948 0.1710 0.0070 -0.0030 -0.0014 339 GLY A O 1965 N N . PRO A 256 ? 0.1311 0.1783 0.1559 0.0073 -0.0018 -0.0024 340 PRO A N 1966 C CA . PRO A 256 ? 0.1284 0.1725 0.1531 0.0091 -0.0018 -0.0020 340 PRO A CA 1967 C C . PRO A 256 ? 0.1222 0.1685 0.1486 0.0113 -0.0020 -0.0014 340 PRO A C 1968 O O . PRO A 256 ? 0.1155 0.1652 0.1433 0.0122 -0.0016 -0.0016 340 PRO A O 1969 C CB . PRO A 256 ? 0.1135 0.1561 0.1380 0.0095 -0.0010 -0.0028 340 PRO A CB 1970 C CG . PRO A 256 ? 0.1392 0.1851 0.1641 0.0084 -0.0005 -0.0033 340 PRO A CG 1971 C CD . PRO A 256 ? 0.1063 0.1538 0.1309 0.0065 -0.0010 -0.0031 340 PRO A CD 1972 N N . VAL A 257 ? 0.1456 0.1901 0.1718 0.0123 -0.0025 -0.0006 341 VAL A N 1973 C CA . VAL A 257 ? 0.1255 0.1715 0.1531 0.0145 -0.0026 0.0002 341 VAL A CA 1974 C C . VAL A 257 ? 0.1774 0.2207 0.2054 0.0164 -0.0018 0.0000 341 VAL A C 1975 O O . VAL A 257 ? 0.1487 0.1877 0.1757 0.0166 -0.0017 0.0000 341 VAL A O 1976 C CB . VAL A 257 ? 0.1721 0.2173 0.1992 0.0148 -0.0034 0.0013 341 VAL A CB 1977 C CG1 . VAL A 257 ? 0.1741 0.2206 0.2026 0.0174 -0.0034 0.0023 341 VAL A CG1 1978 C CG2 . VAL A 257 ? 0.0939 0.1421 0.1207 0.0129 -0.0041 0.0013 341 VAL A CG2 1979 N N . SER A 258 ? 0.1283 0.1741 0.1578 0.0178 -0.0012 -0.0002 342 SER A N 1980 C CA . SER A 258 ? 0.1447 0.1880 0.1745 0.0194 -0.0003 -0.0007 342 SER A CA 1981 C C . SER A 258 ? 0.1416 0.1822 0.1719 0.0215 -0.0002 0.0002 342 SER A C 1982 O O . SER A 258 ? 0.1425 0.1793 0.1724 0.0221 0.0005 -0.0003 342 SER A O 1983 C CB . SER A 258 ? 0.2172 0.2641 0.2486 0.0204 0.0004 -0.0012 342 SER A CB 1984 O OG . SER A 258 ? 0.2272 0.2783 0.2603 0.0218 0.0001 -0.0002 342 SER A OG 1985 N N . SER A 259 ? 0.1446 0.1872 0.1756 0.0225 -0.0008 0.0015 343 SER A N 1986 C CA . SER A 259 ? 0.1407 0.1809 0.1721 0.0246 -0.0006 0.0026 343 SER A CA 1987 C C . SER A 259 ? 0.1732 0.2082 0.2030 0.0237 -0.0006 0.0024 343 SER A C 1988 O O . SER A 259 ? 0.1393 0.1737 0.1678 0.0220 -0.0014 0.0026 343 SER A O 1989 C CB . SER A 259 ? 0.2362 0.2798 0.2683 0.0254 -0.0014 0.0041 343 SER A CB 1990 O OG . SER A 259 ? 0.2665 0.3078 0.2990 0.0274 -0.0012 0.0054 343 SER A OG 1991 N N . ASN A 260 ? 0.1318 0.1630 0.1617 0.0249 0.0003 0.0021 344 ASN A N 1992 C CA . ASN A 260 ? 0.1610 0.1873 0.1895 0.0242 0.0003 0.0018 344 ASN A CA 1993 C C . ASN A 260 ? 0.1508 0.1762 0.1777 0.0216 0.0000 0.0006 344 ASN A C 1994 O O . ASN A 260 ? 0.1286 0.1511 0.1542 0.0205 -0.0003 0.0007 344 ASN A O 1995 C CB . ASN A 260 ? 0.1521 0.1774 0.1803 0.0245 -0.0003 0.0033 344 ASN A CB 1996 C CG . ASN A 260 ? 0.2131 0.2390 0.2427 0.0271 0.0001 0.0047 344 ASN A CG 1997 O OD1 . ASN A 260 ? 0.2486 0.2784 0.2790 0.0279 -0.0005 0.0058 344 ASN A OD1 1998 N ND2 . ASN A 260 ? 0.2394 0.2614 0.2693 0.0285 0.0010 0.0047 344 ASN A ND2 1999 N N . GLY A 261 ? 0.1529 0.1808 0.1800 0.0208 0.0002 -0.0003 345 GLY A N 2000 C CA . GLY A 261 ? 0.1572 0.1848 0.1829 0.0185 -0.0001 -0.0012 345 GLY A CA 2001 C C . GLY A 261 ? 0.1728 0.1969 0.1975 0.0179 0.0005 -0.0023 345 GLY A C 2002 O O . GLY A 261 ? 0.1133 0.1363 0.1366 0.0161 0.0002 -0.0027 345 GLY A O 2003 N N . ALA A 262 ? 0.1229 0.1453 0.1483 0.0193 0.0014 -0.0029 346 ALA A N 2004 C CA . ALA A 262 ? 0.1526 0.1720 0.1771 0.0187 0.0020 -0.0042 346 ALA A CA 2005 C C . ALA A 262 ? 0.1204 0.1361 0.1437 0.0181 0.0016 -0.0038 346 ALA A C 2006 O O . ALA A 262 ? 0.1047 0.1198 0.1283 0.0188 0.0012 -0.0026 346 ALA A O 2007 C CB . ALA A 262 ? 0.1765 0.1950 0.2022 0.0204 0.0032 -0.0050 346 ALA A CB 2008 N N . ASN A 263 ? 0.1344 0.1480 0.1565 0.0169 0.0018 -0.0048 347 ASN A N 2009 C CA . ASN A 263 ? 0.1551 0.1655 0.1761 0.0162 0.0015 -0.0047 347 ASN A CA 2010 C C . ASN A 263 ? 0.1594 0.1705 0.1795 0.0150 0.0004 -0.0036 347 ASN A C 2011 O O . ASN A 263 ? 0.1052 0.1193 0.1254 0.0145 0.0000 -0.0033 347 ASN A O 2012 C CB . ASN A 263 ? 0.1736 0.1813 0.1954 0.0177 0.0019 -0.0042 347 ASN A CB 2013 C CG . ASN A 263 ? 0.3386 0.3427 0.3593 0.0169 0.0020 -0.0047 347 ASN A CG 2014 O OD1 . ASN A 263 ? 0.2981 0.3018 0.3175 0.0153 0.0016 -0.0051 347 ASN A OD1 2015 N ND2 . ASN A 263 ? 0.4175 0.4188 0.4388 0.0180 0.0027 -0.0045 347 ASN A ND2 2016 N N . GLY A 264 ? 0.0835 0.0921 0.1028 0.0145 0.0000 -0.0031 348 GLY A N 2017 C CA . GLY A 264 ? 0.0865 0.0957 0.1049 0.0135 -0.0009 -0.0022 348 GLY A CA 2018 C C . GLY A 264 ? 0.0679 0.0742 0.0851 0.0126 -0.0012 -0.0022 348 GLY A C 2019 O O . GLY A 264 ? 0.0760 0.0798 0.0932 0.0129 -0.0007 -0.0027 348 GLY A O 2020 N N . VAL A 265 ? 0.0939 0.1007 0.1103 0.0115 -0.0020 -0.0016 349 VAL A N 2021 C CA . VAL A 265 ? 0.0813 0.0857 0.0964 0.0105 -0.0023 -0.0015 349 VAL A CA 2022 C C . VAL A 265 ? 0.0875 0.0929 0.1016 0.0090 -0.0028 -0.0014 349 VAL A C 2023 O O . VAL A 265 ? 0.0755 0.0833 0.0899 0.0088 -0.0031 -0.0010 349 VAL A O 2024 C CB . VAL A 265 ? 0.0866 0.0895 0.1019 0.0112 -0.0025 -0.0005 349 VAL A CB 2025 C CG1 . VAL A 265 ? 0.0773 0.0824 0.0928 0.0112 -0.0032 0.0005 349 VAL A CG1 2026 C CG2 . VAL A 265 ? 0.0855 0.0857 0.0997 0.0104 -0.0027 -0.0006 349 VAL A CG2 2027 N N . LYS A 266 ? 0.0923 0.0960 0.1052 0.0081 -0.0029 -0.0017 350 LYS A N 2028 C CA . LYS A 266 ? 0.0703 0.0746 0.0822 0.0068 -0.0033 -0.0015 350 LYS A CA 2029 C C . LYS A 266 ? 0.0797 0.0841 0.0915 0.0066 -0.0039 -0.0006 350 LYS A C 2030 O O . LYS A 266 ? 0.0680 0.0710 0.0799 0.0072 -0.0041 -0.0001 350 LYS A O 2031 C CB . LYS A 266 ? 0.0895 0.0919 0.1002 0.0060 -0.0033 -0.0018 350 LYS A CB 2032 C CG . LYS A 266 ? 0.0701 0.0726 0.0797 0.0048 -0.0036 -0.0014 350 LYS A CG 2033 C CD . LYS A 266 ? 0.0996 0.1006 0.1082 0.0042 -0.0036 -0.0017 350 LYS A CD 2034 C CE . LYS A 266 ? 0.0919 0.0927 0.0995 0.0032 -0.0038 -0.0011 350 LYS A CE 2035 N NZ . LYS A 266 ? 0.0542 0.0566 0.0617 0.0026 -0.0036 -0.0011 350 LYS A NZ 2036 N N . GLY A 267 ? 0.0631 0.0693 0.0748 0.0058 -0.0041 -0.0003 351 GLY A N 2037 C CA . GLY A 267 ? 0.0981 0.1049 0.1096 0.0055 -0.0047 0.0004 351 GLY A CA 2038 C C . GLY A 267 ? 0.0776 0.0851 0.0884 0.0040 -0.0047 0.0003 351 GLY A C 2039 O O . GLY A 267 ? 0.1027 0.1098 0.1129 0.0033 -0.0044 -0.0001 351 GLY A O 2040 N N . PHE A 268 ? 0.0777 0.0863 0.0885 0.0035 -0.0051 0.0007 352 PHE A N 2041 C CA . PHE A 268 ? 0.0674 0.0764 0.0775 0.0021 -0.0051 0.0006 352 PHE A CA 2042 C C . PHE A 268 ? 0.0842 0.0957 0.0948 0.0017 -0.0055 0.0008 352 PHE A C 2043 O O . PHE A 268 ? 0.1087 0.1214 0.1201 0.0027 -0.0058 0.0012 352 PHE A O 2044 C CB . PHE A 268 ? 0.0738 0.0802 0.0827 0.0015 -0.0052 0.0007 352 PHE A CB 2045 C CG . PHE A 268 ? 0.0863 0.0922 0.0951 0.0017 -0.0057 0.0011 352 PHE A CG 2046 C CD1 . PHE A 268 ? 0.0748 0.0794 0.0838 0.0029 -0.0059 0.0015 352 PHE A CD1 2047 C CD2 . PHE A 268 ? 0.0955 0.1023 0.1039 0.0008 -0.0059 0.0012 352 PHE A CD2 2048 C CE1 . PHE A 268 ? 0.0805 0.0848 0.0893 0.0031 -0.0063 0.0020 352 PHE A CE1 2049 C CE2 . PHE A 268 ? 0.1022 0.1089 0.1105 0.0011 -0.0064 0.0016 352 PHE A CE2 2050 C CZ . PHE A 268 ? 0.0760 0.0814 0.0844 0.0023 -0.0066 0.0021 352 PHE A CZ 2051 N N . SER A 269 ? 0.0551 0.0674 0.0653 0.0003 -0.0054 0.0005 353 SER A N 2052 C CA . SER A 269 ? 0.1012 0.1158 0.1117 -0.0004 -0.0057 0.0005 353 SER A CA 2053 C C . SER A 269 ? 0.0925 0.1062 0.1020 -0.0022 -0.0054 0.0000 353 SER A C 2054 O O . SER A 269 ? 0.0757 0.0882 0.0848 -0.0028 -0.0048 -0.0002 353 SER A O 2055 C CB . SER A 269 ? 0.0754 0.0936 0.0871 -0.0001 -0.0057 0.0004 353 SER A CB 2056 O OG . SER A 269 ? 0.1046 0.1235 0.1172 0.0017 -0.0060 0.0009 353 SER A OG 2057 N N . PHE A 270 ? 0.0708 0.0853 0.0801 -0.0030 -0.0056 -0.0001 354 PHE A N 2058 C CA . PHE A 270 ? 0.0728 0.0865 0.0813 -0.0048 -0.0052 -0.0006 354 PHE A CA 2059 C C . PHE A 270 ? 0.0985 0.1156 0.1077 -0.0060 -0.0052 -0.0012 354 PHE A C 2060 O O . PHE A 270 ? 0.0792 0.0989 0.0889 -0.0059 -0.0057 -0.0012 354 PHE A O 2061 C CB . PHE A 270 ? 0.0853 0.0970 0.0928 -0.0051 -0.0054 -0.0006 354 PHE A CB 2062 C CG . PHE A 270 ? 0.0842 0.0925 0.0910 -0.0043 -0.0053 -0.0001 354 PHE A CG 2063 C CD1 . PHE A 270 ? 0.0913 0.0974 0.0974 -0.0048 -0.0047 -0.0002 354 PHE A CD1 2064 C CD2 . PHE A 270 ? 0.0789 0.0863 0.0856 -0.0031 -0.0058 0.0004 354 PHE A CD2 2065 C CE1 . PHE A 270 ? 0.1036 0.1069 0.1090 -0.0041 -0.0046 0.0002 354 PHE A CE1 2066 C CE2 . PHE A 270 ? 0.0707 0.0754 0.0768 -0.0025 -0.0057 0.0007 354 PHE A CE2 2067 C CZ . PHE A 270 ? 0.0847 0.0874 0.0901 -0.0030 -0.0052 0.0005 354 PHE A CZ 2068 N N . LYS A 271 ? 0.0590 0.0760 0.0681 -0.0073 -0.0044 -0.0017 355 LYS A N 2069 C CA . LYS A 271 ? 0.0521 0.0723 0.0619 -0.0087 -0.0042 -0.0024 355 LYS A CA 2070 C C . LYS A 271 ? 0.0918 0.1113 0.1008 -0.0105 -0.0040 -0.0031 355 LYS A C 2071 O O . LYS A 271 ? 0.1095 0.1257 0.1175 -0.0112 -0.0034 -0.0031 355 LYS A O 2072 C CB . LYS A 271 ? 0.0899 0.1104 0.1000 -0.0093 -0.0035 -0.0025 355 LYS A CB 2073 C CG . LYS A 271 ? 0.0872 0.1108 0.0980 -0.0110 -0.0031 -0.0033 355 LYS A CG 2074 C CD . LYS A 271 ? 0.1280 0.1516 0.1390 -0.0116 -0.0023 -0.0034 355 LYS A CD 2075 C CE . LYS A 271 ? 0.1592 0.1863 0.1710 -0.0132 -0.0019 -0.0042 355 LYS A CE 2076 N NZ . LYS A 271 ? 0.1137 0.1403 0.1251 -0.0153 -0.0014 -0.0050 355 LYS A NZ 2077 N N . TYR A 272 ? 0.0600 0.0829 0.0696 -0.0112 -0.0044 -0.0036 356 TYR A N 2078 C CA . TYR A 272 ? 0.1115 0.1346 0.1206 -0.0132 -0.0040 -0.0045 356 TYR A CA 2079 C C . TYR A 272 ? 0.0962 0.1236 0.1063 -0.0145 -0.0039 -0.0053 356 TYR A C 2080 O O . TYR A 272 ? 0.0631 0.0944 0.0739 -0.0142 -0.0047 -0.0054 356 TYR A O 2081 C CB . TYR A 272 ? 0.1238 0.1469 0.1323 -0.0128 -0.0047 -0.0044 356 TYR A CB 2082 C CG . TYR A 272 ? 0.1202 0.1391 0.1277 -0.0119 -0.0047 -0.0038 356 TYR A CG 2083 C CD1 . TYR A 272 ? 0.0758 0.0938 0.0834 -0.0098 -0.0053 -0.0028 356 TYR A CD1 2084 C CD2 . TYR A 272 ? 0.1193 0.1350 0.1257 -0.0130 -0.0041 -0.0043 356 TYR A CD2 2085 C CE1 . TYR A 272 ? 0.0744 0.0888 0.0811 -0.0091 -0.0052 -0.0023 356 TYR A CE1 2086 C CE2 . TYR A 272 ? 0.1509 0.1631 0.1564 -0.0121 -0.0041 -0.0037 356 TYR A CE2 2087 C CZ . TYR A 272 ? 0.1359 0.1476 0.1415 -0.0102 -0.0047 -0.0027 356 TYR A CZ 2088 O OH . TYR A 272 ? 0.1568 0.1652 0.1616 -0.0093 -0.0047 -0.0022 356 TYR A OH 2089 N N . GLY A 273 ? 0.1573 0.1843 0.1674 -0.0161 -0.0030 -0.0059 357 GLY A N 2090 C CA . GLY A 273 ? 0.1667 0.1979 0.1779 -0.0174 -0.0028 -0.0067 357 GLY A CA 2091 C C . GLY A 273 ? 0.0978 0.1326 0.1103 -0.0158 -0.0035 -0.0061 357 GLY A C 2092 O O . GLY A 273 ? 0.1216 0.1550 0.1343 -0.0144 -0.0034 -0.0053 357 GLY A O 2093 N N . ASN A 274 ? 0.0601 0.0996 0.0735 -0.0159 -0.0042 -0.0064 358 ASN A N 2094 C CA . ASN A 274 ? 0.0694 0.1127 0.0842 -0.0141 -0.0049 -0.0057 358 ASN A CA 2095 C C . ASN A 274 ? 0.0805 0.1231 0.0952 -0.0117 -0.0058 -0.0046 358 ASN A C 2096 O O . ASN A 274 ? 0.0961 0.1410 0.1118 -0.0098 -0.0063 -0.0038 358 ASN A O 2097 C CB . ASN A 274 ? 0.0994 0.1486 0.1154 -0.0151 -0.0051 -0.0064 358 ASN A CB 2098 C CG . ASN A 274 ? 0.1484 0.1986 0.1647 -0.0174 -0.0042 -0.0075 358 ASN A CG 2099 O OD1 . ASN A 274 ? 0.1571 0.2062 0.1728 -0.0197 -0.0036 -0.0086 358 ASN A OD1 2100 N ND2 . ASN A 274 ? 0.1538 0.2060 0.1712 -0.0170 -0.0039 -0.0073 358 ASN A ND2 2101 N N . GLY A 275 ? 0.0783 0.1178 0.0918 -0.0117 -0.0059 -0.0045 359 GLY A N 2102 C CA . GLY A 275 ? 0.0690 0.1076 0.0823 -0.0097 -0.0067 -0.0034 359 GLY A CA 2103 C C . GLY A 275 ? 0.1057 0.1397 0.1184 -0.0082 -0.0065 -0.0026 359 GLY A C 2104 O O . GLY A 275 ? 0.0572 0.0885 0.0694 -0.0089 -0.0057 -0.0029 359 GLY A O 2105 N N . VAL A 276 ? 0.0829 0.1163 0.0956 -0.0063 -0.0070 -0.0017 360 VAL A N 2106 C CA . VAL A 276 ? 0.0384 0.0679 0.0507 -0.0049 -0.0069 -0.0010 360 VAL A CA 2107 C C . VAL A 276 ? 0.0987 0.1266 0.1105 -0.0035 -0.0074 -0.0002 360 VAL A C 2108 O O . VAL A 276 ? 0.0895 0.1201 0.1019 -0.0026 -0.0080 0.0004 360 VAL A O 2109 C CB . VAL A 276 ? 0.0660 0.0966 0.0794 -0.0036 -0.0067 -0.0007 360 VAL A CB 2110 C CG1 . VAL A 276 ? 0.0682 0.1025 0.0829 -0.0021 -0.0073 -0.0001 360 VAL A CG1 2111 C CG2 . VAL A 276 ? 0.0863 0.1129 0.0992 -0.0025 -0.0064 -0.0003 360 VAL A CG2 2112 N N . TRP A 277 ? 0.1111 0.1349 0.1219 -0.0034 -0.0072 0.0000 361 TRP A N 2113 C CA . TRP A 277 ? 0.1061 0.1280 0.1166 -0.0020 -0.0076 0.0008 361 TRP A CA 2114 C C . TRP A 277 ? 0.0963 0.1169 0.1074 -0.0004 -0.0074 0.0013 361 TRP A C 2115 O O . TRP A 277 ? 0.0975 0.1157 0.1082 -0.0006 -0.0069 0.0010 361 TRP A O 2116 C CB . TRP A 277 ? 0.0996 0.1179 0.1087 -0.0027 -0.0074 0.0006 361 TRP A CB 2117 C CG . TRP A 277 ? 0.0887 0.1078 0.0972 -0.0036 -0.0077 0.0004 361 TRP A CG 2118 C CD1 . TRP A 277 ? 0.0846 0.1035 0.0924 -0.0054 -0.0074 -0.0005 361 TRP A CD1 2119 C CD2 . TRP A 277 ? 0.0712 0.0912 0.0795 -0.0027 -0.0083 0.0011 361 TRP A CD2 2120 N NE1 . TRP A 277 ? 0.1064 0.1263 0.1136 -0.0057 -0.0078 -0.0005 361 TRP A NE1 2121 C CE2 . TRP A 277 ? 0.0780 0.0987 0.0856 -0.0041 -0.0084 0.0005 361 TRP A CE2 2122 C CE3 . TRP A 277 ? 0.0802 0.1006 0.0891 -0.0008 -0.0087 0.0022 361 TRP A CE3 2123 C CZ2 . TRP A 277 ? 0.0875 0.1094 0.0947 -0.0037 -0.0090 0.0010 361 TRP A CZ2 2124 C CZ3 . TRP A 277 ? 0.0960 0.1174 0.1046 -0.0004 -0.0092 0.0028 361 TRP A CZ3 2125 C CH2 . TRP A 277 ? 0.1309 0.1533 0.1387 -0.0018 -0.0094 0.0022 361 TRP A CH2 2126 N N . ILE A 278 ? 0.0886 0.1108 0.1005 0.0012 -0.0078 0.0021 362 ILE A N 2127 C CA . ILE A 278 ? 0.1018 0.1230 0.1145 0.0028 -0.0075 0.0025 362 ILE A CA 2128 C C . ILE A 278 ? 0.1126 0.1308 0.1248 0.0040 -0.0076 0.0032 362 ILE A C 2129 O O . ILE A 278 ? 0.1136 0.1326 0.1258 0.0046 -0.0081 0.0039 362 ILE A O 2130 C CB . ILE A 278 ? 0.1081 0.1329 0.1222 0.0040 -0.0077 0.0029 362 ILE A CB 2131 C CG1 . ILE A 278 ? 0.1332 0.1609 0.1478 0.0029 -0.0075 0.0021 362 ILE A CG1 2132 C CG2 . ILE A 278 ? 0.1153 0.1387 0.1301 0.0059 -0.0074 0.0033 362 ILE A CG2 2133 C CD1 . ILE A 278 ? 0.1930 0.2251 0.2091 0.0039 -0.0077 0.0025 362 ILE A CD1 2134 N N . GLY A 279 ? 0.0933 0.1084 0.1051 0.0042 -0.0072 0.0029 363 GLY A N 2135 C CA . GLY A 279 ? 0.0869 0.0994 0.0986 0.0054 -0.0072 0.0035 363 GLY A CA 2136 C C . GLY A 279 ? 0.0949 0.1073 0.1076 0.0069 -0.0068 0.0037 363 GLY A C 2137 O O . GLY A 279 ? 0.1177 0.1305 0.1308 0.0067 -0.0064 0.0030 363 GLY A O 2138 N N . ARG A 280 ? 0.0587 0.0709 0.0720 0.0083 -0.0069 0.0045 364 ARG A N 2139 C CA . ARG A 280 ? 0.0812 0.0932 0.0956 0.0099 -0.0064 0.0047 364 ARG A CA 2140 C C . ARG A 280 ? 0.0939 0.1037 0.1084 0.0113 -0.0063 0.0056 364 ARG A C 2141 O O . ARG A 280 ? 0.0664 0.0758 0.0803 0.0112 -0.0066 0.0063 364 ARG A O 2142 C CB . ARG A 280 ? 0.0684 0.0842 0.0840 0.0106 -0.0065 0.0049 364 ARG A CB 2143 C CG . ARG A 280 ? 0.1017 0.1199 0.1177 0.0115 -0.0070 0.0061 364 ARG A CG 2144 C CD . ARG A 280 ? 0.0860 0.1083 0.1035 0.0125 -0.0071 0.0064 364 ARG A CD 2145 N NE . ARG A 280 ? 0.0754 0.1002 0.0932 0.0135 -0.0076 0.0076 364 ARG A NE 2146 C CZ . ARG A 280 ? 0.1094 0.1381 0.1285 0.0146 -0.0077 0.0082 364 ARG A CZ 2147 N NH1 . ARG A 280 ? 0.0941 0.1245 0.1141 0.0147 -0.0074 0.0075 364 ARG A NH1 2148 N NH2 . ARG A 280 ? 0.1229 0.1541 0.1423 0.0156 -0.0082 0.0095 364 ARG A NH2 2149 N N . THR A 281 ? 0.1236 0.1322 0.1390 0.0125 -0.0056 0.0055 365 THR A N 2150 C CA . THR A 281 ? 0.1258 0.1323 0.1415 0.0139 -0.0053 0.0064 365 THR A CA 2151 C C . THR A 281 ? 0.1216 0.1307 0.1380 0.0152 -0.0056 0.0078 365 THR A C 2152 O O . THR A 281 ? 0.1297 0.1425 0.1467 0.0152 -0.0060 0.0078 365 THR A O 2153 C CB . THR A 281 ? 0.1479 0.1525 0.1644 0.0150 -0.0044 0.0059 365 THR A CB 2154 O OG1 . THR A 281 ? 0.1406 0.1480 0.1584 0.0159 -0.0042 0.0059 365 THR A OG1 2155 C CG2 . THR A 281 ? 0.1210 0.1237 0.1369 0.0137 -0.0041 0.0045 365 THR A CG2 2156 N N . LYS A 282 ? 0.1265 0.1341 0.1430 0.0163 -0.0054 0.0089 366 LYS A N 2157 C CA . LYS A 282 ? 0.1406 0.1506 0.1579 0.0178 -0.0057 0.0104 366 LYS A CA 2158 C C . LYS A 282 ? 0.1433 0.1535 0.1620 0.0198 -0.0050 0.0109 366 LYS A C 2159 O O . LYS A 282 ? 0.1700 0.1836 0.1896 0.0210 -0.0052 0.0118 366 LYS A O 2160 C CB . LYS A 282 ? 0.1260 0.1343 0.1425 0.0181 -0.0058 0.0117 366 LYS A CB 2161 C CG . LYS A 282 ? 0.1353 0.1445 0.1505 0.0165 -0.0066 0.0115 366 LYS A CG 2162 C CD . LYS A 282 ? 0.1245 0.1325 0.1391 0.0169 -0.0067 0.0128 366 LYS A CD 2163 C CE . LYS A 282 ? 0.1317 0.1413 0.1451 0.0154 -0.0075 0.0127 366 LYS A CE 2164 N NZ . LYS A 282 ? 0.1549 0.1693 0.1686 0.0154 -0.0082 0.0130 366 LYS A NZ 2165 N N . SER A 283 ? 0.0973 0.1042 0.1163 0.0202 -0.0041 0.0102 367 SER A N 2166 C CA . SER A 283 ? 0.1500 0.1566 0.1704 0.0220 -0.0032 0.0104 367 SER A CA 2167 C C . SER A 283 ? 0.1346 0.1437 0.1556 0.0217 -0.0032 0.0092 367 SER A C 2168 O O . SER A 283 ? 0.1086 0.1176 0.1289 0.0199 -0.0034 0.0078 367 SER A O 2169 C CB . SER A 283 ? 0.1559 0.1579 0.1764 0.0224 -0.0022 0.0099 367 SER A CB 2170 O OG . SER A 283 ? 0.1874 0.1890 0.2092 0.0239 -0.0012 0.0096 367 SER A OG 2171 N N . ILE A 284 ? 0.1596 0.1710 0.1821 0.0234 -0.0029 0.0097 368 ILE A N 2172 C CA . ILE A 284 ? 0.1727 0.1866 0.1959 0.0232 -0.0028 0.0086 368 ILE A CA 2173 C C . ILE A 284 ? 0.1382 0.1493 0.1619 0.0237 -0.0017 0.0074 368 ILE A C 2174 O O . ILE A 284 ? 0.1617 0.1744 0.1858 0.0233 -0.0015 0.0063 368 ILE A O 2175 C CB . ILE A 284 ? 0.1805 0.1989 0.2051 0.0248 -0.0030 0.0097 368 ILE A CB 2176 C CG1 . ILE A 284 ? 0.1778 0.1948 0.2036 0.0275 -0.0021 0.0108 368 ILE A CG1 2177 C CG2 . ILE A 284 ? 0.1698 0.1915 0.1939 0.0243 -0.0041 0.0108 368 ILE A CG2 2178 C CD1 . ILE A 284 ? 0.2454 0.2670 0.2728 0.0293 -0.0021 0.0118 368 ILE A CD1 2179 N N . SER A 285 ? 0.1303 0.1374 0.1539 0.0244 -0.0009 0.0076 369 SER A N 2180 C CA . SER A 285 ? 0.1440 0.1484 0.1682 0.0250 0.0003 0.0065 369 SER A CA 2181 C C . SER A 285 ? 0.2210 0.2214 0.2441 0.0235 0.0006 0.0052 369 SER A C 2182 O O . SER A 285 ? 0.1801 0.1790 0.2032 0.0231 0.0013 0.0037 369 SER A O 2183 C CB . SER A 285 ? 0.2143 0.2174 0.2398 0.0275 0.0013 0.0076 369 SER A CB 2184 O OG . SER A 285 ? 0.2549 0.2554 0.2800 0.0279 0.0013 0.0089 369 SER A OG 2185 N N . SER A 286 ? 0.1748 0.1736 0.1968 0.0226 0.0001 0.0059 370 SER A N 2186 C CA . SER A 286 ? 0.1686 0.1639 0.1895 0.0212 0.0004 0.0048 370 SER A CA 2187 C C . SER A 286 ? 0.1365 0.1324 0.1560 0.0193 -0.0007 0.0048 370 SER A C 2188 O O . SER A 286 ? 0.1346 0.1332 0.1539 0.0191 -0.0016 0.0057 370 SER A O 2189 C CB . SER A 286 ? 0.2323 0.2240 0.2535 0.0222 0.0012 0.0056 370 SER A CB 2190 O OG . SER A 286 ? 0.4135 0.4019 0.4339 0.0209 0.0016 0.0044 370 SER A OG 2191 N N . ARG A 287 ? 0.1331 0.1267 0.1517 0.0179 -0.0005 0.0036 371 ARG A N 2192 C CA . ARG A 287 ? 0.1435 0.1374 0.1608 0.0162 -0.0014 0.0035 371 ARG A CA 2193 C C . ARG A 287 ? 0.1299 0.1221 0.1466 0.0162 -0.0016 0.0046 371 ARG A C 2194 O O . ARG A 287 ? 0.1247 0.1144 0.1407 0.0153 -0.0014 0.0042 371 ARG A O 2195 C CB . ARG A 287 ? 0.1086 0.1012 0.1251 0.0147 -0.0012 0.0018 371 ARG A CB 2196 C CG . ARG A 287 ? 0.0861 0.0808 0.1029 0.0145 -0.0011 0.0008 371 ARG A CG 2197 C CD . ARG A 287 ? 0.1346 0.1281 0.1507 0.0133 -0.0008 -0.0008 371 ARG A CD 2198 N NE . ARG A 287 ? 0.1015 0.0973 0.1177 0.0131 -0.0007 -0.0017 371 ARG A NE 2199 C CZ . ARG A 287 ? 0.1361 0.1318 0.1517 0.0121 -0.0005 -0.0029 371 ARG A CZ 2200 N NH1 . ARG A 287 ? 0.1096 0.1032 0.1244 0.0112 -0.0004 -0.0036 371 ARG A NH1 2201 N NH2 . ARG A 287 ? 0.0961 0.0939 0.1118 0.0120 -0.0004 -0.0036 371 ARG A NH2 2202 N N . ASN A 288 ? 0.1559 0.1499 0.1730 0.0172 -0.0020 0.0061 372 ASN A N 2203 C CA . ASN A 288 ? 0.1304 0.1233 0.1470 0.0173 -0.0023 0.0075 372 ASN A CA 2204 C C . ASN A 288 ? 0.1242 0.1202 0.1402 0.0169 -0.0034 0.0083 372 ASN A C 2205 O O . ASN A 288 ? 0.0999 0.0991 0.1164 0.0173 -0.0038 0.0085 372 ASN A O 2206 C CB . ASN A 288 ? 0.1800 0.1716 0.1976 0.0193 -0.0015 0.0087 372 ASN A CB 2207 C CG . ASN A 288 ? 0.2531 0.2409 0.2711 0.0196 -0.0003 0.0079 372 ASN A CG 2208 O OD1 . ASN A 288 ? 0.2912 0.2762 0.3087 0.0190 0.0000 0.0080 372 ASN A OD1 2209 N ND2 . ASN A 288 ? 0.2378 0.2256 0.2567 0.0203 0.0004 0.0070 372 ASN A ND2 2210 N N . GLY A 289 ? 0.0931 0.0882 0.1081 0.0159 -0.0038 0.0087 373 GLY A N 2211 C CA . GLY A 289 ? 0.0859 0.0836 0.1002 0.0154 -0.0047 0.0094 373 GLY A CA 2212 C C . GLY A 289 ? 0.0934 0.0930 0.1072 0.0139 -0.0053 0.0082 373 GLY A C 2213 O O . GLY A 289 ? 0.0904 0.0899 0.1044 0.0135 -0.0050 0.0071 373 GLY A O 2214 N N . PHE A 290 ? 0.0877 0.0891 0.1007 0.0130 -0.0060 0.0085 374 PHE A N 2215 C CA . PHE A 290 ? 0.0746 0.0778 0.0871 0.0115 -0.0065 0.0075 374 PHE A CA 2216 C C . PHE A 290 ? 0.0732 0.0791 0.0852 0.0110 -0.0072 0.0081 374 PHE A C 2217 O O . PHE A 290 ? 0.0680 0.0735 0.0795 0.0111 -0.0074 0.0089 374 PHE A O 2218 C CB . PHE A 290 ? 0.0602 0.0610 0.0717 0.0101 -0.0063 0.0065 374 PHE A CB 2219 C CG . PHE A 290 ? 0.0723 0.0743 0.0836 0.0090 -0.0065 0.0054 374 PHE A CG 2220 C CD1 . PHE A 290 ? 0.0709 0.0729 0.0828 0.0092 -0.0060 0.0047 374 PHE A CD1 2221 C CD2 . PHE A 290 ? 0.0668 0.0700 0.0773 0.0077 -0.0069 0.0052 374 PHE A CD2 2222 C CE1 . PHE A 290 ? 0.0869 0.0901 0.0985 0.0082 -0.0061 0.0038 374 PHE A CE1 2223 C CE2 . PHE A 290 ? 0.0758 0.0798 0.0860 0.0066 -0.0069 0.0043 374 PHE A CE2 2224 C CZ . PHE A 290 ? 0.0763 0.0804 0.0871 0.0069 -0.0065 0.0037 374 PHE A CZ 2225 N N . GLU A 291 ? 0.0702 0.0789 0.0824 0.0102 -0.0075 0.0075 375 GLU A N 2226 C CA . GLU A 291 ? 0.0893 0.1010 0.1011 0.0096 -0.0082 0.0078 375 GLU A CA 2227 C C . GLU A 291 ? 0.0790 0.0922 0.0905 0.0080 -0.0083 0.0066 375 GLU A C 2228 O O . GLU A 291 ? 0.0849 0.0979 0.0968 0.0078 -0.0080 0.0059 375 GLU A O 2229 C CB . GLU A 291 ? 0.0858 0.1008 0.0986 0.0110 -0.0084 0.0089 375 GLU A CB 2230 C CG . GLU A 291 ? 0.1290 0.1460 0.1431 0.0117 -0.0082 0.0086 375 GLU A CG 2231 C CD . GLU A 291 ? 0.1913 0.2112 0.2065 0.0135 -0.0083 0.0099 375 GLU A CD 2232 O OE1 . GLU A 291 ? 0.1594 0.1796 0.1745 0.0144 -0.0085 0.0111 375 GLU A OE1 2233 O OE2 . GLU A 291 ? 0.1586 0.1807 0.1750 0.0142 -0.0081 0.0097 375 GLU A OE2 2234 N N . MET A 292 ? 0.0682 0.0826 0.0788 0.0067 -0.0087 0.0064 376 MET A N 2235 C CA . MET A 292 ? 0.0746 0.0905 0.0850 0.0051 -0.0088 0.0054 376 MET A CA 2236 C C . MET A 292 ? 0.1323 0.1527 0.1433 0.0050 -0.0092 0.0055 376 MET A C 2237 O O . MET A 292 ? 0.1025 0.1243 0.1132 0.0053 -0.0097 0.0062 376 MET A O 2238 C CB . MET A 292 ? 0.0948 0.1087 0.1039 0.0036 -0.0087 0.0048 376 MET A CB 2239 C CG . MET A 292 ? 0.1003 0.1103 0.1089 0.0035 -0.0083 0.0044 376 MET A CG 2240 S SD . MET A 292 ? 0.1350 0.1445 0.1440 0.0032 -0.0078 0.0036 376 MET A SD 2241 C CE . MET A 292 ? 0.0894 0.1004 0.0979 0.0013 -0.0077 0.0027 376 MET A CE 2242 N N . ILE A 293 ? 0.0782 0.1008 0.0898 0.0045 -0.0091 0.0049 377 ILE A N 2243 C CA . ILE A 293 ? 0.0927 0.1200 0.1051 0.0043 -0.0095 0.0050 377 ILE A CA 2244 C C . ILE A 293 ? 0.1144 0.1432 0.1265 0.0022 -0.0094 0.0037 377 ILE A C 2245 O O . ILE A 293 ? 0.0794 0.1069 0.0916 0.0016 -0.0089 0.0029 377 ILE A O 2246 C CB . ILE A 293 ? 0.0996 0.1293 0.1135 0.0060 -0.0095 0.0055 377 ILE A CB 2247 C CG1 . ILE A 293 ? 0.1276 0.1559 0.1418 0.0081 -0.0095 0.0069 377 ILE A CG1 2248 C CG2 . ILE A 293 ? 0.0983 0.1332 0.1129 0.0056 -0.0099 0.0055 377 ILE A CG2 2249 C CD1 . ILE A 293 ? 0.1982 0.2281 0.2139 0.0099 -0.0093 0.0075 377 ILE A CD1 2250 N N . TRP A 294 ? 0.0686 0.0999 0.0803 0.0011 -0.0098 0.0033 378 TRP A N 2251 C CA . TRP A 294 ? 0.0937 0.1267 0.1052 -0.0010 -0.0096 0.0021 378 TRP A CA 2252 C C . TRP A 294 ? 0.0970 0.1351 0.1098 -0.0009 -0.0099 0.0020 378 TRP A C 2253 O O . TRP A 294 ? 0.1215 0.1632 0.1346 -0.0003 -0.0105 0.0026 378 TRP A O 2254 C CB . TRP A 294 ? 0.0997 0.1325 0.1100 -0.0025 -0.0098 0.0014 378 TRP A CB 2255 C CG . TRP A 294 ? 0.1122 0.1474 0.1225 -0.0047 -0.0096 0.0001 378 TRP A CG 2256 C CD1 . TRP A 294 ? 0.1531 0.1922 0.1633 -0.0058 -0.0100 -0.0004 378 TRP A CD1 2257 C CD2 . TRP A 294 ? 0.1162 0.1500 0.1265 -0.0062 -0.0088 -0.0010 378 TRP A CD2 2258 N NE1 . TRP A 294 ? 0.1344 0.1745 0.1447 -0.0079 -0.0095 -0.0019 378 TRP A NE1 2259 C CE2 . TRP A 294 ? 0.1547 0.1915 0.1650 -0.0082 -0.0088 -0.0021 378 TRP A CE2 2260 C CE3 . TRP A 294 ? 0.1013 0.1316 0.1115 -0.0061 -0.0082 -0.0010 378 TRP A CE3 2261 C CZ2 . TRP A 294 ? 0.1551 0.1912 0.1653 -0.0101 -0.0080 -0.0033 378 TRP A CZ2 2262 C CZ3 . TRP A 294 ? 0.1054 0.1353 0.1155 -0.0079 -0.0075 -0.0021 378 TRP A CZ3 2263 C CH2 . TRP A 294 ? 0.1281 0.1608 0.1383 -0.0098 -0.0074 -0.0032 378 TRP A CH2 2264 N N . ASP A 295 ? 0.0940 0.1326 0.1074 -0.0016 -0.0094 0.0013 379 ASP A N 2265 C CA . ASP A 295 ? 0.0928 0.1363 0.1075 -0.0016 -0.0096 0.0011 379 ASP A CA 2266 C C . ASP A 295 ? 0.0852 0.1298 0.0997 -0.0041 -0.0092 -0.0004 379 ASP A C 2267 O O . ASP A 295 ? 0.0543 0.0971 0.0689 -0.0048 -0.0085 -0.0009 379 ASP A O 2268 C CB . ASP A 295 ? 0.0792 0.1227 0.0951 0.0001 -0.0093 0.0017 379 ASP A CB 2269 C CG . ASP A 295 ? 0.1382 0.1870 0.1556 0.0003 -0.0095 0.0016 379 ASP A CG 2270 O OD1 . ASP A 295 ? 0.1206 0.1730 0.1380 -0.0012 -0.0098 0.0009 379 ASP A OD1 2271 O OD2 . ASP A 295 ? 0.1794 0.2287 0.1978 0.0019 -0.0093 0.0021 379 ASP A OD2 2272 N N . PRO A 296 ? 0.0995 0.1473 0.1139 -0.0056 -0.0095 -0.0010 380 PRO A N 2273 C CA . PRO A 296 ? 0.1137 0.1621 0.1276 -0.0083 -0.0090 -0.0026 380 PRO A CA 2274 C C . PRO A 296 ? 0.0750 0.1256 0.0901 -0.0092 -0.0085 -0.0033 380 PRO A C 2275 O O . PRO A 296 ? 0.1135 0.1633 0.1282 -0.0113 -0.0078 -0.0045 380 PRO A O 2276 C CB . PRO A 296 ? 0.1299 0.1825 0.1437 -0.0091 -0.0096 -0.0030 380 PRO A CB 2277 C CG . PRO A 296 ? 0.1663 0.2218 0.1809 -0.0068 -0.0104 -0.0015 380 PRO A CG 2278 C CD . PRO A 296 ? 0.1282 0.1792 0.1426 -0.0047 -0.0103 -0.0003 380 PRO A CD 2279 N N . ASN A 297 ? 0.0597 0.1129 0.0761 -0.0075 -0.0087 -0.0025 381 ASN A N 2280 C CA . ASN A 297 ? 0.0897 0.1447 0.1070 -0.0082 -0.0082 -0.0031 381 ASN A CA 2281 C C . ASN A 297 ? 0.1131 0.1667 0.1312 -0.0061 -0.0080 -0.0022 381 ASN A C 2282 O O . ASN A 297 ? 0.1308 0.1871 0.1501 -0.0059 -0.0078 -0.0024 381 ASN A O 2283 C CB . ASN A 297 ? 0.1053 0.1669 0.1239 -0.0089 -0.0085 -0.0036 381 ASN A CB 2284 C CG . ASN A 297 ? 0.1555 0.2208 0.1753 -0.0064 -0.0093 -0.0023 381 ASN A CG 2285 O OD1 . ASN A 297 ? 0.0999 0.1628 0.1194 -0.0043 -0.0096 -0.0011 381 ASN A OD1 2286 N ND2 . ASN A 297 ? 0.2564 0.3276 0.2777 -0.0065 -0.0095 -0.0026 381 ASN A ND2 2287 N N . GLY A 298 ? 0.0672 0.1166 0.0846 -0.0046 -0.0080 -0.0014 382 GLY A N 2288 C CA . GLY A 298 ? 0.0834 0.1312 0.1014 -0.0025 -0.0079 -0.0006 382 GLY A CA 2289 C C . GLY A 298 ? 0.0808 0.1261 0.0987 -0.0031 -0.0070 -0.0011 382 GLY A C 2290 O O . GLY A 298 ? 0.0772 0.1222 0.0957 -0.0016 -0.0068 -0.0007 382 GLY A O 2291 N N . TRP A 299 ? 0.0813 0.1248 0.0982 -0.0052 -0.0065 -0.0020 383 TRP A N 2292 C CA . TRP A 299 ? 0.0780 0.1192 0.0947 -0.0058 -0.0057 -0.0023 383 TRP A CA 2293 C C . TRP A 299 ? 0.1379 0.1832 0.1559 -0.0061 -0.0054 -0.0027 383 TRP A C 2294 O O . TRP A 299 ? 0.1104 0.1550 0.1288 -0.0053 -0.0050 -0.0026 383 TRP A O 2295 C CB . TRP A 299 ? 0.1022 0.1404 0.1176 -0.0079 -0.0051 -0.0030 383 TRP A CB 2296 C CG . TRP A 299 ? 0.1078 0.1431 0.1227 -0.0081 -0.0043 -0.0030 383 TRP A CG 2297 C CD1 . TRP A 299 ? 0.0897 0.1259 0.1049 -0.0095 -0.0035 -0.0035 383 TRP A CD1 2298 C CD2 . TRP A 299 ? 0.0946 0.1257 0.1086 -0.0070 -0.0041 -0.0025 383 TRP A CD2 2299 N NE1 . TRP A 299 ? 0.1405 0.1734 0.1550 -0.0092 -0.0029 -0.0033 383 TRP A NE1 2300 C CE2 . TRP A 299 ? 0.1267 0.1566 0.1405 -0.0077 -0.0033 -0.0026 383 TRP A CE2 2301 C CE3 . TRP A 299 ? 0.0843 0.1128 0.0977 -0.0056 -0.0046 -0.0018 383 TRP A CE3 2302 C CZ2 . TRP A 299 ? 0.0951 0.1215 0.1081 -0.0069 -0.0030 -0.0022 383 TRP A CZ2 2303 C CZ3 . TRP A 299 ? 0.1571 0.1821 0.1698 -0.0049 -0.0043 -0.0015 383 TRP A CZ3 2304 C CH2 . TRP A 299 ? 0.1196 0.1437 0.1320 -0.0056 -0.0035 -0.0018 383 TRP A CH2 2305 N N . THR A 300 ? 0.0969 0.1465 0.1157 -0.0072 -0.0056 -0.0032 384 THR A N 2306 C CA . THR A 300 ? 0.1153 0.1692 0.1355 -0.0077 -0.0053 -0.0037 384 THR A CA 2307 C C . THR A 300 ? 0.1762 0.2355 0.1978 -0.0065 -0.0061 -0.0033 384 THR A C 2308 O O . THR A 300 ? 0.1660 0.2292 0.1889 -0.0064 -0.0059 -0.0035 384 THR A O 2309 C CB . THR A 300 ? 0.1780 0.2327 0.1978 -0.0107 -0.0047 -0.0048 384 THR A CB 2310 O OG1 . THR A 300 ? 0.1534 0.2093 0.1728 -0.0118 -0.0052 -0.0053 384 THR A OG1 2311 C CG2 . THR A 300 ? 0.1405 0.1902 0.1590 -0.0118 -0.0038 -0.0051 384 THR A CG2 2312 N N . GLY A 301 ? 0.0888 0.1486 0.1102 -0.0054 -0.0069 -0.0026 385 GLY A N 2313 C CA . GLY A 301 ? 0.1289 0.1939 0.1517 -0.0040 -0.0076 -0.0021 385 GLY A CA 2314 C C . GLY A 301 ? 0.1456 0.2097 0.1690 -0.0009 -0.0078 -0.0008 385 GLY A C 2315 O O . GLY A 301 ? 0.1140 0.1734 0.1365 0.0001 -0.0078 -0.0002 385 GLY A O 2316 N N . THR A 302 ? 0.1070 0.1758 0.1321 0.0006 -0.0081 -0.0003 386 THR A N 2317 C CA . THR A 302 ? 0.1402 0.2082 0.1661 0.0035 -0.0080 0.0008 386 THR A CA 2318 C C . THR A 302 ? 0.1947 0.2643 0.2210 0.0056 -0.0088 0.0022 386 THR A C 2319 O O . THR A 302 ? 0.1679 0.2365 0.1949 0.0081 -0.0086 0.0032 386 THR A O 2320 C CB . THR A 302 ? 0.1570 0.2285 0.1846 0.0043 -0.0076 0.0007 386 THR A CB 2321 O OG1 . THR A 302 ? 0.1228 0.2008 0.1516 0.0037 -0.0080 0.0005 386 THR A OG1 2322 C CG2 . THR A 302 ? 0.1666 0.2359 0.1937 0.0025 -0.0068 -0.0004 386 THR A CG2 2323 N N . ASP A 303 ? 0.1841 0.2560 0.2099 0.0047 -0.0094 0.0022 387 ASP A N 2324 C CA . ASP A 303 ? 0.2136 0.2873 0.2397 0.0066 -0.0101 0.0036 387 ASP A CA 2325 C C . ASP A 303 ? 0.1725 0.2402 0.1973 0.0077 -0.0101 0.0044 387 ASP A C 2326 O O . ASP A 303 ? 0.1532 0.2160 0.1769 0.0066 -0.0096 0.0037 387 ASP A O 2327 C CB . ASP A 303 ? 0.1778 0.2560 0.2036 0.0052 -0.0109 0.0033 387 ASP A CB 2328 C CG . ASP A 303 ? 0.2054 0.2803 0.2295 0.0029 -0.0109 0.0024 387 ASP A CG 2329 O OD1 . ASP A 303 ? 0.2293 0.3010 0.2523 0.0037 -0.0112 0.0032 387 ASP A OD1 2330 O OD2 . ASP A 303 ? 0.1816 0.2570 0.2053 0.0003 -0.0106 0.0010 387 ASP A OD2 2331 N N . ASN A 304 ? 0.1786 0.2470 0.2037 0.0098 -0.0105 0.0059 388 ASN A N 2332 C CA . ASN A 304 ? 0.1952 0.2583 0.2192 0.0109 -0.0104 0.0068 388 ASN A CA 2333 C C . ASN A 304 ? 0.2093 0.2727 0.2321 0.0103 -0.0111 0.0072 388 ASN A C 2334 O O . ASN A 304 ? 0.2024 0.2629 0.2246 0.0116 -0.0111 0.0083 388 ASN A O 2335 C CB . ASN A 304 ? 0.1913 0.2535 0.2163 0.0140 -0.0101 0.0082 388 ASN A CB 2336 C CG . ASN A 304 ? 0.3318 0.3995 0.3580 0.0158 -0.0107 0.0096 388 ASN A CG 2337 O OD1 . ASN A 304 ? 0.4004 0.4731 0.4268 0.0147 -0.0113 0.0094 388 ASN A OD1 2338 N ND2 . ASN A 304 ? 0.3037 0.3705 0.3309 0.0186 -0.0103 0.0111 388 ASN A ND2 2339 N N . ASN A 305 ? 0.1338 0.2005 0.1562 0.0081 -0.0115 0.0063 389 ASN A N 2340 C CA . ASN A 305 ? 0.1373 0.2043 0.1585 0.0072 -0.0121 0.0064 389 ASN A CA 2341 C C . ASN A 305 ? 0.1729 0.2345 0.1925 0.0054 -0.0117 0.0054 389 ASN A C 2342 O O . ASN A 305 ? 0.1532 0.2126 0.1726 0.0040 -0.0112 0.0042 389 ASN A O 2343 C CB . ASN A 305 ? 0.1851 0.2583 0.2066 0.0056 -0.0126 0.0056 389 ASN A CB 2344 C CG . ASN A 305 ? 0.2576 0.3369 0.2808 0.0074 -0.0131 0.0066 389 ASN A CG 2345 O OD1 . ASN A 305 ? 0.4313 0.5162 0.4552 0.0062 -0.0134 0.0059 389 ASN A OD1 2346 N ND2 . ASN A 305 ? 0.3095 0.3879 0.3335 0.0104 -0.0130 0.0083 389 ASN A ND2 2347 N N . PHE A 306 ? 0.1275 0.1868 0.1458 0.0055 -0.0120 0.0059 390 PHE A N 2348 C CA . PHE A 306 ? 0.1183 0.1727 0.1351 0.0039 -0.0117 0.0050 390 PHE A CA 2349 C C . PHE A 306 ? 0.1683 0.2236 0.1839 0.0031 -0.0122 0.0051 390 PHE A C 2350 O O . PHE A 306 ? 0.1474 0.2063 0.1633 0.0042 -0.0128 0.0062 390 PHE A O 2351 C CB . PHE A 306 ? 0.1649 0.2137 0.1814 0.0052 -0.0112 0.0056 390 PHE A CB 2352 C CG . PHE A 306 ? 0.1367 0.1848 0.1534 0.0076 -0.0114 0.0074 390 PHE A CG 2353 C CD1 . PHE A 306 ? 0.1553 0.2012 0.1708 0.0076 -0.0116 0.0079 390 PHE A CD1 2354 C CD2 . PHE A 306 ? 0.2008 0.2501 0.2188 0.0098 -0.0113 0.0085 390 PHE A CD2 2355 C CE1 . PHE A 306 ? 0.2064 0.2515 0.2220 0.0097 -0.0117 0.0096 390 PHE A CE1 2356 C CE2 . PHE A 306 ? 0.2346 0.2830 0.2528 0.0120 -0.0113 0.0102 390 PHE A CE2 2357 C CZ . PHE A 306 ? 0.2218 0.2680 0.2388 0.0119 -0.0115 0.0108 390 PHE A CZ 2358 N N . SER A 307 ? 0.1187 0.1706 0.1329 0.0012 -0.0119 0.0040 391 SER A N 2359 C CA . SER A 307 ? 0.0919 0.1446 0.1050 0.0001 -0.0123 0.0038 391 SER A CA 2360 C C . SER A 307 ? 0.1696 0.2180 0.1815 0.0009 -0.0123 0.0046 391 SER A C 2361 O O . SER A 307 ? 0.1869 0.2369 0.1982 0.0012 -0.0128 0.0052 391 SER A O 2362 C CB . SER A 307 ? 0.1271 0.1797 0.1395 -0.0028 -0.0120 0.0018 391 SER A CB 2363 O OG . SER A 307 ? 0.2038 0.2608 0.2172 -0.0038 -0.0120 0.0010 391 SER A OG 2364 N N . ILE A 308 ? 0.1346 0.1779 0.1463 0.0013 -0.0118 0.0046 392 ILE A N 2365 C CA . ILE A 308 ? 0.1432 0.1824 0.1539 0.0019 -0.0117 0.0053 392 ILE A CA 2366 C C . ILE A 308 ? 0.1617 0.1974 0.1729 0.0038 -0.0113 0.0062 392 ILE A C 2367 O O . ILE A 308 ? 0.1398 0.1742 0.1516 0.0038 -0.0109 0.0057 392 ILE A O 2368 C CB . ILE A 308 ? 0.1861 0.2218 0.1955 0.0000 -0.0113 0.0040 392 ILE A CB 2369 C CG1 . ILE A 308 ? 0.2389 0.2777 0.2478 -0.0021 -0.0114 0.0027 392 ILE A CG1 2370 C CG2 . ILE A 308 ? 0.2120 0.2439 0.2204 0.0006 -0.0112 0.0047 392 ILE A CG2 2371 C CD1 . ILE A 308 ? 0.2082 0.2435 0.2159 -0.0040 -0.0109 0.0014 392 ILE A CD1 2372 N N . LYS A 309 ? 0.0967 0.1308 0.1076 0.0052 -0.0114 0.0076 394 LYS A N 2373 C CA . LYS A 309 ? 0.1094 0.1396 0.1206 0.0067 -0.0110 0.0083 394 LYS A CA 2374 C C . LYS A 309 ? 0.1485 0.1751 0.1585 0.0066 -0.0109 0.0087 394 LYS A C 2375 O O . LYS A 309 ? 0.1449 0.1728 0.1544 0.0068 -0.0112 0.0094 394 LYS A O 2376 C CB . LYS A 309 ? 0.1522 0.1841 0.1646 0.0090 -0.0110 0.0097 394 LYS A CB 2377 C CG . LYS A 309 ? 0.1768 0.2043 0.1894 0.0104 -0.0104 0.0104 394 LYS A CG 2378 C CD . LYS A 309 ? 0.2627 0.2916 0.2766 0.0128 -0.0103 0.0119 394 LYS A CD 2379 C CE . LYS A 309 ? 0.2765 0.3073 0.2917 0.0134 -0.0101 0.0115 394 LYS A CE 2380 N NZ . LYS A 309 ? 0.4130 0.4434 0.4294 0.0158 -0.0097 0.0128 394 LYS A NZ 2381 N N . GLN A 310 ? 0.1196 0.1419 0.1293 0.0064 -0.0104 0.0081 395 GLN A N 2382 C CA . GLN A 310 ? 0.1036 0.1225 0.1123 0.0064 -0.0102 0.0085 395 GLN A CA 2383 C C . GLN A 310 ? 0.1240 0.1395 0.1331 0.0077 -0.0097 0.0090 395 GLN A C 2384 O O . GLN A 310 ? 0.0940 0.1080 0.1036 0.0076 -0.0093 0.0083 395 GLN A O 2385 C CB . GLN A 310 ? 0.1312 0.1481 0.1388 0.0045 -0.0100 0.0072 395 GLN A CB 2386 C CG . GLN A 310 ? 0.0814 0.0951 0.0880 0.0044 -0.0099 0.0074 395 GLN A CG 2387 C CD . GLN A 310 ? 0.1394 0.1510 0.1450 0.0028 -0.0097 0.0062 395 GLN A CD 2388 O OE1 . GLN A 310 ? 0.1181 0.1309 0.1236 0.0015 -0.0096 0.0052 395 GLN A OE1 2389 N NE2 . GLN A 310 ? 0.1297 0.1382 0.1347 0.0028 -0.0094 0.0063 395 GLN A NE2 2390 N N . ASP A 311 ? 0.1059 0.1204 0.1150 0.0089 -0.0097 0.0103 396 ASP A N 2391 C CA . ASP A 311 ? 0.1100 0.1211 0.1195 0.0101 -0.0091 0.0108 396 ASP A CA 2392 C C . ASP A 311 ? 0.1006 0.1079 0.1093 0.0090 -0.0087 0.0099 396 ASP A C 2393 O O . ASP A 311 ? 0.0934 0.1002 0.1011 0.0079 -0.0089 0.0096 396 ASP A O 2394 C CB . ASP A 311 ? 0.1407 0.1515 0.1503 0.0115 -0.0090 0.0124 396 ASP A CB 2395 C CG . ASP A 311 ? 0.2113 0.2256 0.2219 0.0130 -0.0092 0.0136 396 ASP A CG 2396 O OD1 . ASP A 311 ? 0.2024 0.2189 0.2138 0.0131 -0.0093 0.0131 396 ASP A OD1 2397 O OD2 . ASP A 311 ? 0.3419 0.3569 0.3525 0.0142 -0.0093 0.0152 396 ASP A OD2 2398 N N . ILE A 312 ? 0.0806 0.0856 0.0898 0.0093 -0.0082 0.0094 397 ILE A N 2399 C CA . ILE A 312 ? 0.0826 0.0844 0.0912 0.0085 -0.0079 0.0085 397 ILE A CA 2400 C C . ILE A 312 ? 0.0969 0.0958 0.1059 0.0094 -0.0073 0.0090 397 ILE A C 2401 O O . ILE A 312 ? 0.0811 0.0777 0.0894 0.0090 -0.0071 0.0089 397 ILE A O 2402 C CB . ILE A 312 ? 0.0802 0.0821 0.0889 0.0076 -0.0077 0.0073 397 ILE A CB 2403 C CG1 . ILE A 312 ? 0.0745 0.0790 0.0829 0.0065 -0.0081 0.0067 397 ILE A CG1 2404 C CG2 . ILE A 312 ? 0.0823 0.0811 0.0903 0.0069 -0.0074 0.0065 397 ILE A CG2 2405 C CD1 . ILE A 312 ? 0.0996 0.1035 0.1068 0.0053 -0.0084 0.0065 397 ILE A CD1 2406 N N . VAL A 313 ? 0.0764 0.0753 0.0864 0.0107 -0.0069 0.0093 398 VAL A N 2407 C CA . VAL A 313 ? 0.0794 0.0756 0.0899 0.0117 -0.0062 0.0097 398 VAL A CA 2408 C C . VAL A 313 ? 0.0883 0.0857 0.0999 0.0135 -0.0060 0.0110 398 VAL A C 2409 O O . VAL A 313 ? 0.0843 0.0841 0.0966 0.0140 -0.0062 0.0110 398 VAL A O 2410 C CB . VAL A 313 ? 0.0654 0.0598 0.0763 0.0114 -0.0057 0.0084 398 VAL A CB 2411 C CG1 . VAL A 313 ? 0.1001 0.0917 0.1117 0.0124 -0.0048 0.0087 398 VAL A CG1 2412 C CG2 . VAL A 313 ? 0.0927 0.0859 0.1026 0.0098 -0.0058 0.0073 398 VAL A CG2 2413 N N . GLY A 314 ? 0.0771 0.0728 0.0887 0.0143 -0.0056 0.0122 399 GLY A N 2414 C CA . GLY A 314 ? 0.1113 0.1078 0.1238 0.0162 -0.0053 0.0137 399 GLY A CA 2415 C C . GLY A 314 ? 0.1179 0.1139 0.1317 0.0174 -0.0047 0.0133 399 GLY A C 2416 O O . GLY A 314 ? 0.1017 0.0955 0.1156 0.0168 -0.0042 0.0120 399 GLY A O 2417 N N . ILE A 315 ? 0.1331 0.1313 0.1478 0.0190 -0.0046 0.0145 400 ILE A N 2418 C CA . ILE A 315 ? 0.1505 0.1487 0.1665 0.0202 -0.0040 0.0142 400 ILE A CA 2419 C C . ILE A 315 ? 0.1859 0.1799 0.2025 0.0209 -0.0028 0.0140 400 ILE A C 2420 O O . ILE A 315 ? 0.2266 0.2197 0.2439 0.0213 -0.0022 0.0130 400 ILE A O 2421 C CB . ILE A 315 ? 0.1965 0.1982 0.2135 0.0221 -0.0042 0.0156 400 ILE A CB 2422 C CG1 . ILE A 315 ? 0.2548 0.2571 0.2731 0.0231 -0.0037 0.0150 400 ILE A CG1 2423 C CG2 . ILE A 315 ? 0.2221 0.2227 0.2393 0.0237 -0.0038 0.0177 400 ILE A CG2 2424 C CD1 . ILE A 315 ? 0.3522 0.3585 0.3717 0.0249 -0.0039 0.0164 400 ILE A CD1 2425 N N . ASN A 316 ? 0.1611 0.1524 0.1772 0.0211 -0.0024 0.0149 401 ASN A N 2426 C CA . ASN A 316 ? 0.2584 0.2455 0.2750 0.0216 -0.0012 0.0147 401 ASN A CA 2427 C C . ASN A 316 ? 0.2463 0.2307 0.2621 0.0197 -0.0010 0.0130 401 ASN A C 2428 O O . ASN A 316 ? 0.2792 0.2601 0.2953 0.0196 0.0000 0.0126 401 ASN A O 2429 C CB . ASN A 316 ? 0.3335 0.3189 0.3500 0.0227 -0.0007 0.0167 401 ASN A CB 2430 C CG . ASN A 316 ? 0.4018 0.3895 0.4192 0.0250 -0.0006 0.0187 401 ASN A CG 2431 O OD1 . ASN A 316 ? 0.4986 0.4871 0.5157 0.0258 -0.0008 0.0205 401 ASN A OD1 2432 N ND2 . ASN A 316 ? 0.3654 0.3543 0.3841 0.0261 -0.0003 0.0182 401 ASN A ND2 2433 N N . GLU A 317 ? 0.1595 0.1456 0.1744 0.0181 -0.0019 0.0119 402 GLU A N 2434 C CA . GLU A 317 ? 0.1243 0.1085 0.1385 0.0163 -0.0018 0.0103 402 GLU A CA 2435 C C . GLU A 317 ? 0.1497 0.1349 0.1641 0.0156 -0.0019 0.0086 402 GLU A C 2436 O O . GLU A 317 ? 0.1268 0.1148 0.1415 0.0160 -0.0024 0.0086 402 GLU A O 2437 C CB . GLU A 317 ? 0.1371 0.1223 0.1500 0.0150 -0.0027 0.0105 402 GLU A CB 2438 C CG . GLU A 317 ? 0.2508 0.2357 0.2634 0.0155 -0.0028 0.0122 402 GLU A CG 2439 C CD . GLU A 317 ? 0.3346 0.3158 0.3472 0.0156 -0.0018 0.0125 402 GLU A CD 2440 O OE1 . GLU A 317 ? 0.3343 0.3132 0.3470 0.0147 -0.0013 0.0111 402 GLU A OE1 2441 O OE2 . GLU A 317 ? 0.5545 0.5351 0.5670 0.0164 -0.0016 0.0141 402 GLU A OE2 2442 N N . TRP A 318 ? 0.1236 0.1065 0.1377 0.0146 -0.0014 0.0072 403 TRP A N 2443 C CA . TRP A 318 ? 0.1089 0.0925 0.1231 0.0140 -0.0014 0.0056 403 TRP A CA 2444 C C . TRP A 318 ? 0.1144 0.1004 0.1277 0.0127 -0.0024 0.0051 403 TRP A C 2445 O O . TRP A 318 ? 0.1315 0.1172 0.1438 0.0117 -0.0029 0.0053 403 TRP A O 2446 C CB . TRP A 318 ? 0.1703 0.1511 0.1845 0.0132 -0.0006 0.0042 403 TRP A CB 2447 C CG . TRP A 318 ? 0.2053 0.1833 0.2204 0.0143 0.0006 0.0045 403 TRP A CG 2448 C CD1 . TRP A 318 ? 0.2461 0.2214 0.2610 0.0140 0.0011 0.0049 403 TRP A CD1 2449 C CD2 . TRP A 318 ? 0.2396 0.2170 0.2558 0.0157 0.0015 0.0045 403 TRP A CD2 2450 N NE1 . TRP A 318 ? 0.2722 0.2450 0.2880 0.0152 0.0023 0.0052 403 TRP A NE1 2451 C CE2 . TRP A 318 ? 0.2602 0.2343 0.2769 0.0163 0.0026 0.0049 403 TRP A CE2 2452 C CE3 . TRP A 318 ? 0.2614 0.2409 0.2784 0.0166 0.0015 0.0041 403 TRP A CE3 2453 C CZ2 . TRP A 318 ? 0.2983 0.2709 0.3162 0.0179 0.0037 0.0050 403 TRP A CZ2 2454 C CZ3 . TRP A 318 ? 0.3955 0.3737 0.4137 0.0181 0.0026 0.0042 403 TRP A CZ3 2455 C CH2 . TRP A 318 ? 0.3032 0.2779 0.3219 0.0188 0.0037 0.0047 403 TRP A CH2 2456 N N . SER A 319 ? 0.1028 0.0909 0.1164 0.0128 -0.0026 0.0045 404 SER A N 2457 C CA . SER A 319 ? 0.0930 0.0830 0.1058 0.0115 -0.0033 0.0039 404 SER A CA 2458 C C . SER A 319 ? 0.1261 0.1161 0.1390 0.0110 -0.0029 0.0024 404 SER A C 2459 O O . SER A 319 ? 0.1060 0.0939 0.1190 0.0109 -0.0023 0.0016 404 SER A O 2460 C CB . SER A 319 ? 0.1137 0.1068 0.1266 0.0117 -0.0040 0.0046 404 SER A CB 2461 O OG . SER A 319 ? 0.1354 0.1300 0.1494 0.0130 -0.0037 0.0048 404 SER A OG 2462 N N . GLY A 320 ? 0.0671 0.0594 0.0798 0.0106 -0.0033 0.0021 405 GLY A N 2463 C CA . GLY A 320 ? 0.0838 0.0764 0.0965 0.0101 -0.0030 0.0008 405 GLY A CA 2464 C C . GLY A 320 ? 0.0836 0.0785 0.0958 0.0092 -0.0035 0.0006 405 GLY A C 2465 O O . GLY A 320 ? 0.0673 0.0642 0.0797 0.0093 -0.0039 0.0012 405 GLY A O 2466 N N . TYR A 321 ? 0.0829 0.0776 0.0944 0.0082 -0.0034 -0.0003 406 TYR A N 2467 C CA . TYR A 321 ? 0.0906 0.0870 0.1014 0.0073 -0.0037 -0.0005 406 TYR A CA 2468 C C . TYR A 321 ? 0.0901 0.0868 0.1003 0.0067 -0.0044 0.0003 406 TYR A C 2469 O O . TYR A 321 ? 0.0848 0.0800 0.0946 0.0066 -0.0046 0.0008 406 TYR A O 2470 C CB . TYR A 321 ? 0.0982 0.0941 0.1083 0.0065 -0.0035 -0.0014 406 TYR A CB 2471 C CG . TYR A 321 ? 0.1018 0.0985 0.1123 0.0068 -0.0030 -0.0023 406 TYR A CG 2472 C CD1 . TYR A 321 ? 0.0932 0.0902 0.1049 0.0079 -0.0025 -0.0025 406 TYR A CD1 2473 C CD2 . TYR A 321 ? 0.0823 0.0797 0.0921 0.0061 -0.0028 -0.0030 406 TYR A CD2 2474 C CE1 . TYR A 321 ? 0.1120 0.1098 0.1242 0.0082 -0.0020 -0.0034 406 TYR A CE1 2475 C CE2 . TYR A 321 ? 0.1211 0.1194 0.1313 0.0063 -0.0023 -0.0039 406 TYR A CE2 2476 C CZ . TYR A 321 ? 0.1293 0.1279 0.1407 0.0074 -0.0019 -0.0042 406 TYR A CZ 2477 O OH . TYR A 321 ? 0.1281 0.1276 0.1398 0.0076 -0.0013 -0.0052 406 TYR A OH 2478 N N . SER A 322 ? 0.0656 0.0642 0.0756 0.0061 -0.0046 0.0005 407 SER A N 2479 C CA . SER A 322 ? 0.0745 0.0732 0.0837 0.0053 -0.0051 0.0009 407 SER A CA 2480 C C . SER A 322 ? 0.0709 0.0706 0.0796 0.0043 -0.0050 0.0006 407 SER A C 2481 O O . SER A 322 ? 0.0992 0.1002 0.1083 0.0044 -0.0047 0.0002 407 SER A O 2482 C CB . SER A 322 ? 0.0581 0.0581 0.0678 0.0057 -0.0055 0.0017 407 SER A CB 2483 O OG . SER A 322 ? 0.0785 0.0809 0.0891 0.0060 -0.0054 0.0017 407 SER A OG 2484 N N . GLY A 323 ? 0.0585 0.0577 0.0663 0.0034 -0.0052 0.0008 408 GLY A N 2485 C CA . GLY A 323 ? 0.0762 0.0759 0.0833 0.0024 -0.0050 0.0006 408 GLY A CA 2486 C C . GLY A 323 ? 0.0891 0.0884 0.0955 0.0015 -0.0052 0.0009 408 GLY A C 2487 O O . GLY A 323 ? 0.0925 0.0907 0.0986 0.0016 -0.0055 0.0012 408 GLY A O 2488 N N . SER A 324 ? 0.0743 0.0744 0.0804 0.0006 -0.0050 0.0008 409 SER A N 2489 C CA . SER A 324 ? 0.0734 0.0729 0.0789 -0.0003 -0.0049 0.0009 409 SER A CA 2490 C C . SER A 324 ? 0.0869 0.0844 0.0914 -0.0006 -0.0047 0.0010 409 SER A C 2491 O O . SER A 324 ? 0.0915 0.0886 0.0958 -0.0003 -0.0044 0.0010 409 SER A O 2492 C CB . SER A 324 ? 0.1148 0.1160 0.1205 -0.0013 -0.0047 0.0007 409 SER A CB 2493 O OG . SER A 324 ? 0.1474 0.1486 0.1529 -0.0014 -0.0042 0.0006 409 SER A OG 2494 N N . PHE A 325 ? 0.0983 0.0946 0.1021 -0.0012 -0.0047 0.0012 410 PHE A N 2495 C CA . PHE A 325 ? 0.1052 0.0998 0.1081 -0.0015 -0.0043 0.0014 410 PHE A CA 2496 C C . PHE A 325 ? 0.0961 0.0902 0.0986 -0.0024 -0.0041 0.0014 410 PHE A C 2497 O O . PHE A 325 ? 0.1569 0.1517 0.1596 -0.0026 -0.0045 0.0012 410 PHE A O 2498 C CB . PHE A 325 ? 0.0877 0.0810 0.0902 -0.0008 -0.0045 0.0016 410 PHE A CB 2499 C CG . PHE A 325 ? 0.1103 0.1028 0.1127 -0.0006 -0.0049 0.0017 410 PHE A CG 2500 C CD1 . PHE A 325 ? 0.0973 0.0904 0.1003 -0.0001 -0.0053 0.0016 410 PHE A CD1 2501 C CD2 . PHE A 325 ? 0.0856 0.0767 0.0872 -0.0010 -0.0047 0.0018 410 PHE A CD2 2502 C CE1 . PHE A 325 ? 0.0978 0.0903 0.1007 0.0001 -0.0056 0.0018 410 PHE A CE1 2503 C CE2 . PHE A 325 ? 0.1239 0.1145 0.1255 -0.0008 -0.0051 0.0019 410 PHE A CE2 2504 C CZ . PHE A 325 ? 0.0915 0.0827 0.0936 -0.0003 -0.0055 0.0020 410 PHE A CZ 2505 N N . VAL A 326 ? 0.1047 0.0975 0.1064 -0.0030 -0.0035 0.0015 411 VAL A N 2506 C CA . VAL A 326 ? 0.0904 0.0824 0.0917 -0.0039 -0.0032 0.0013 411 VAL A CA 2507 C C . VAL A 326 ? 0.1557 0.1454 0.1561 -0.0038 -0.0029 0.0016 411 VAL A C 2508 O O . VAL A 326 ? 0.1093 0.0983 0.1094 -0.0031 -0.0028 0.0021 411 VAL A O 2509 C CB . VAL A 326 ? 0.1262 0.1185 0.1275 -0.0049 -0.0025 0.0012 411 VAL A CB 2510 C CG1 . VAL A 326 ? 0.0879 0.0828 0.0901 -0.0052 -0.0028 0.0008 411 VAL A CG1 2511 C CG2 . VAL A 326 ? 0.1099 0.1013 0.1107 -0.0047 -0.0019 0.0017 411 VAL A CG2 2512 N N . GLN A 327 ? 0.0815 0.0704 0.0816 -0.0045 -0.0027 0.0014 412 GLN A N 2513 C CA . GLN A 327 ? 0.0599 0.0467 0.0592 -0.0044 -0.0022 0.0016 412 GLN A CA 2514 C C . GLN A 327 ? 0.1011 0.0867 0.1000 -0.0055 -0.0013 0.0014 412 GLN A C 2515 O O . GLN A 327 ? 0.0642 0.0505 0.0633 -0.0066 -0.0012 0.0007 412 GLN A O 2516 C CB . GLN A 327 ? 0.0729 0.0594 0.0721 -0.0042 -0.0027 0.0014 412 GLN A CB 2517 C CG . GLN A 327 ? 0.0749 0.0621 0.0744 -0.0032 -0.0035 0.0017 412 GLN A CG 2518 C CD . GLN A 327 ? 0.0970 0.0838 0.0962 -0.0030 -0.0038 0.0017 412 GLN A CD 2519 O OE1 . GLN A 327 ? 0.0891 0.0760 0.0882 -0.0037 -0.0038 0.0013 412 GLN A OE1 2520 N NE2 . GLN A 327 ? 0.1398 0.1262 0.1390 -0.0022 -0.0041 0.0020 412 GLN A NE2 2521 N N . HIS A 328 A 0.1089 0.0929 0.1073 -0.0053 -0.0005 0.0019 412 HIS A N 2522 C CA . HIS A 328 A 0.1094 0.0919 0.1075 -0.0063 0.0006 0.0019 412 HIS A CA 2523 C C . HIS A 328 A 0.0942 0.0747 0.0917 -0.0067 0.0011 0.0015 412 HIS A C 2524 O O . HIS A 328 A 0.1073 0.0873 0.1047 -0.0059 0.0007 0.0017 412 HIS A O 2525 C CB . HIS A 328 A 0.1085 0.0900 0.1062 -0.0058 0.0013 0.0028 412 HIS A CB 2526 C CG . HIS A 328 A 0.1354 0.1188 0.1336 -0.0058 0.0011 0.0030 412 HIS A CG 2527 N ND1 . HIS A 328 A 0.1310 0.1143 0.1292 -0.0067 0.0019 0.0030 412 HIS A ND1 2528 C CD2 . HIS A 328 A 0.1037 0.0889 0.1023 -0.0050 0.0003 0.0030 412 HIS A CD2 2529 C CE1 . HIS A 328 A 0.1594 0.1447 0.1581 -0.0064 0.0016 0.0031 412 HIS A CE1 2530 N NE2 . HIS A 328 A 0.1274 0.1138 0.1263 -0.0054 0.0006 0.0031 412 HIS A NE2 2531 N N . PRO A 329 B 0.0644 0.0439 0.0618 -0.0080 0.0020 0.0010 412 PRO A N 2532 C CA . PRO A 329 B 0.0947 0.0722 0.0917 -0.0085 0.0027 0.0005 412 PRO A CA 2533 C C . PRO A 329 B 0.1461 0.1212 0.1424 -0.0073 0.0032 0.0014 412 PRO A C 2534 O O . PRO A 329 B 0.1641 0.1380 0.1601 -0.0071 0.0034 0.0012 412 PRO A O 2535 C CB . PRO A 329 B 0.1368 0.1132 0.1336 -0.0100 0.0039 -0.0001 412 PRO A CB 2536 C CG . PRO A 329 B 0.1502 0.1294 0.1478 -0.0106 0.0033 -0.0004 412 PRO A CG 2537 C CD . PRO A 329 B 0.0939 0.0744 0.0917 -0.0092 0.0024 0.0006 412 PRO A CD 2538 N N . GLU A 330 C 0.1514 0.1262 0.1476 -0.0064 0.0035 0.0025 412 GLU A N 2539 C CA . GLU A 330 C 0.1623 0.1354 0.1581 -0.0051 0.0039 0.0035 412 GLU A CA 2540 C C . GLU A 330 C 0.2368 0.2109 0.2326 -0.0041 0.0028 0.0036 412 GLU A C 2541 O O . GLU A 330 C 0.2552 0.2279 0.2506 -0.0032 0.0031 0.0040 412 GLU A O 2542 C CB . GLU A 330 C 0.2093 0.1827 0.2049 -0.0043 0.0041 0.0047 412 GLU A CB 2543 C CG . GLU A 330 C 0.2648 0.2365 0.2601 -0.0050 0.0054 0.0051 412 GLU A CG 2544 C CD . GLU A 330 C 0.1979 0.1710 0.1937 -0.0064 0.0054 0.0044 412 GLU A CD 2545 O OE1 . GLU A 330 C 0.1729 0.1484 0.1693 -0.0067 0.0043 0.0036 412 GLU A OE1 2546 O OE2 . GLU A 330 C 0.1651 0.1372 0.1608 -0.0071 0.0065 0.0047 412 GLU A OE2 2547 N N . LEU A 331 D 0.1433 0.1196 0.1396 -0.0042 0.0017 0.0031 412 LEU A N 2548 C CA . LEU A 331 D 0.1373 0.1145 0.1337 -0.0034 0.0008 0.0031 412 LEU A CA 2549 C C . LEU A 331 D 0.1645 0.1417 0.1608 -0.0040 0.0005 0.0022 412 LEU A C 2550 O O . LEU A 331 D 0.1476 0.1243 0.1437 -0.0034 0.0004 0.0022 412 LEU A O 2551 C CB . LEU A 331 D 0.1479 0.1274 0.1448 -0.0029 -0.0003 0.0031 412 LEU A CB 2552 C CG . LEU A 331 D 0.1176 0.0981 0.1147 -0.0024 -0.0012 0.0030 412 LEU A CG 2553 C CD1 . LEU A 331 D 0.1847 0.1647 0.1816 -0.0013 -0.0012 0.0036 412 LEU A CD1 2554 C CD2 . LEU A 331 D 0.1726 0.1551 0.1703 -0.0022 -0.0020 0.0029 412 LEU A CD2 2555 N N . THR A 332 ? 0.1035 0.0815 0.1001 -0.0052 0.0005 0.0014 413 THR A N 2556 C CA . THR A 332 ? 0.1204 0.0991 0.1170 -0.0058 0.0002 0.0005 413 THR A CA 2557 C C . THR A 332 ? 0.1812 0.1581 0.1772 -0.0067 0.0011 -0.0002 413 THR A C 2558 O O . THR A 332 ? 0.2155 0.1926 0.2114 -0.0070 0.0010 -0.0008 413 THR A O 2559 C CB . THR A 332 ? 0.1571 0.1382 0.1543 -0.0066 -0.0005 -0.0001 413 THR A CB 2560 O OG1 . THR A 332 ? 0.1345 0.1153 0.1317 -0.0078 0.0003 -0.0005 413 THR A OG1 2561 C CG2 . THR A 332 ? 0.1399 0.1226 0.1376 -0.0058 -0.0013 0.0005 413 THR A CG2 2562 N N . GLY A 333 ? 0.1619 0.1371 0.1578 -0.0073 0.0022 -0.0002 414 GLY A N 2563 C CA . GLY A 333 ? 0.1860 0.1593 0.1815 -0.0084 0.0034 -0.0011 414 GLY A CA 2564 C C . GLY A 333 ? 0.2405 0.2153 0.2362 -0.0101 0.0034 -0.0023 414 GLY A C 2565 O O . GLY A 333 ? 0.2140 0.1876 0.2094 -0.0113 0.0042 -0.0034 414 GLY A O 2566 N N . LEU A 334 ? 0.1711 0.1486 0.1674 -0.0102 0.0024 -0.0023 415 LEU A N 2567 C CA . LEU A 334 ? 0.1801 0.1596 0.1767 -0.0118 0.0023 -0.0034 415 LEU A CA 2568 C C . LEU A 334 ? 0.2055 0.1839 0.2022 -0.0128 0.0034 -0.0035 415 LEU A C 2569 O O . LEU A 334 ? 0.2038 0.1800 0.2004 -0.0122 0.0042 -0.0027 415 LEU A O 2570 C CB . LEU A 334 ? 0.1300 0.1128 0.1273 -0.0113 0.0009 -0.0031 415 LEU A CB 2571 C CG . LEU A 334 ? 0.2594 0.2435 0.2567 -0.0104 -0.0001 -0.0029 415 LEU A CG 2572 C CD1 . LEU A 334 ? 0.2099 0.1967 0.2079 -0.0097 -0.0013 -0.0024 415 LEU A CD1 2573 C CD2 . LEU A 334 ? 0.2840 0.2688 0.2809 -0.0114 -0.0001 -0.0040 415 LEU A CD2 2574 N N . ASP A 335 ? 0.1726 0.1527 0.1697 -0.0144 0.0035 -0.0046 416 ASP A N 2575 C CA . ASP A 335 ? 0.3105 0.2898 0.3077 -0.0157 0.0046 -0.0049 416 ASP A CA 2576 C C . ASP A 335 ? 0.2408 0.2231 0.2388 -0.0158 0.0039 -0.0046 416 ASP A C 2577 O O . ASP A 335 ? 0.2644 0.2473 0.2628 -0.0171 0.0046 -0.0052 416 ASP A O 2578 C CB . ASP A 335 ? 0.3022 0.2811 0.2993 -0.0177 0.0056 -0.0065 416 ASP A CB 2579 C CG . ASP A 335 ? 0.4604 0.4429 0.4578 -0.0187 0.0046 -0.0077 416 ASP A CG 2580 O OD1 . ASP A 335 ? 0.5107 0.4962 0.5087 -0.0178 0.0033 -0.0071 416 ASP A OD1 2581 O OD2 . ASP A 335 ? 0.5877 0.5703 0.5849 -0.0203 0.0052 -0.0091 416 ASP A OD2 2582 N N . CYS A 336 ? 0.2136 0.1978 0.2120 -0.0143 0.0026 -0.0039 417 CYS A N 2583 C CA . CYS A 336 ? 0.1537 0.1408 0.1529 -0.0141 0.0019 -0.0036 417 CYS A CA 2584 C C . CYS A 336 ? 0.1514 0.1387 0.1507 -0.0122 0.0010 -0.0024 417 CYS A C 2585 O O . CYS A 336 ? 0.1419 0.1277 0.1407 -0.0111 0.0008 -0.0019 417 CYS A O 2586 C CB . CYS A 336 ? 0.1537 0.1442 0.1534 -0.0149 0.0011 -0.0045 417 CYS A CB 2587 S SG . CYS A 336 ? 0.2972 0.2887 0.2967 -0.0141 0.0000 -0.0046 417 CYS A SG 2588 N N . ILE A 337 ? 0.1240 0.1132 0.1239 -0.0118 0.0006 -0.0020 418 ILE A N 2589 C CA . ILE A 337 ? 0.1081 0.0977 0.1082 -0.0102 -0.0002 -0.0011 418 ILE A CA 2590 C C . ILE A 337 ? 0.1134 0.1054 0.1141 -0.0095 -0.0014 -0.0012 418 ILE A C 2591 O O . ILE A 337 ? 0.1186 0.1132 0.1199 -0.0101 -0.0017 -0.0017 418 ILE A O 2592 C CB . ILE A 337 ? 0.1139 0.1043 0.1144 -0.0100 0.0000 -0.0007 418 ILE A CB 2593 C CG1 . ILE A 337 ? 0.1101 0.0981 0.1101 -0.0105 0.0013 -0.0003 418 ILE A CG1 2594 C CG2 . ILE A 337 ? 0.1236 0.1147 0.1244 -0.0084 -0.0007 0.0001 418 ILE A CG2 2595 C CD1 . ILE A 337 ? 0.1368 0.1256 0.1370 -0.0105 0.0016 0.0002 418 ILE A CD1 2596 N N . ARG A 338 ? 0.0972 0.0883 0.0976 -0.0084 -0.0019 -0.0008 419 ARG A N 2597 C CA . ARG A 338 ? 0.1504 0.1433 0.1511 -0.0077 -0.0029 -0.0008 419 ARG A CA 2598 C C . ARG A 338 ? 0.0918 0.0860 0.0932 -0.0066 -0.0035 -0.0002 419 ARG A C 2599 O O . ARG A 338 ? 0.1051 0.0981 0.1064 -0.0057 -0.0034 0.0003 419 ARG A O 2600 C CB . ARG A 338 ? 0.1268 0.1182 0.1269 -0.0072 -0.0031 -0.0006 419 ARG A CB 2601 C CG . ARG A 338 ? 0.1365 0.1293 0.1370 -0.0062 -0.0041 -0.0002 419 ARG A CG 2602 C CD . ARG A 338 ? 0.1639 0.1552 0.1638 -0.0057 -0.0042 0.0000 419 ARG A CD 2603 N NE . ARG A 338 ? 0.2410 0.2329 0.2406 -0.0065 -0.0042 -0.0006 419 ARG A NE 2604 C CZ . ARG A 338 ? 0.2332 0.2238 0.2321 -0.0063 -0.0042 -0.0005 419 ARG A CZ 2605 N NH1 . ARG A 338 ? 0.1776 0.1665 0.1763 -0.0054 -0.0042 0.0000 419 ARG A NH1 2606 N NH2 . ARG A 338 ? 0.2588 0.2502 0.2573 -0.0071 -0.0042 -0.0011 419 ARG A NH2 2607 N N . PRO A 339 ? 0.1315 0.1284 0.1337 -0.0065 -0.0041 -0.0004 420 PRO A N 2608 C CA . PRO A 339 ? 0.1104 0.1086 0.1133 -0.0053 -0.0046 0.0001 420 PRO A CA 2609 C C . PRO A 339 ? 0.0955 0.0931 0.0984 -0.0042 -0.0052 0.0006 420 PRO A C 2610 O O . PRO A 339 ? 0.1258 0.1237 0.1285 -0.0043 -0.0055 0.0005 420 PRO A O 2611 C CB . PRO A 339 ? 0.1295 0.1308 0.1333 -0.0057 -0.0049 -0.0003 420 PRO A CB 2612 C CG . PRO A 339 ? 0.2152 0.2170 0.2186 -0.0072 -0.0046 -0.0010 420 PRO A CG 2613 C CD . PRO A 339 ? 0.1155 0.1145 0.1179 -0.0074 -0.0043 -0.0010 420 PRO A CD 2614 N N . CYS A 340 ? 0.0572 0.0540 0.0602 -0.0031 -0.0052 0.0009 421 CYS A N 2615 C CA . CYS A 340 ? 0.0730 0.0693 0.0762 -0.0021 -0.0057 0.0014 421 CYS A CA 2616 C C . CYS A 340 ? 0.0943 0.0915 0.0983 -0.0012 -0.0058 0.0015 421 CYS A C 2617 O O . CYS A 340 ? 0.0720 0.0701 0.0764 -0.0014 -0.0056 0.0013 421 CYS A O 2618 C CB . CYS A 340 ? 0.0633 0.0572 0.0657 -0.0019 -0.0055 0.0015 421 CYS A CB 2619 S SG . CYS A 340 ? 0.1106 0.1031 0.1121 -0.0028 -0.0052 0.0014 421 CYS A SG 2620 N N . PHE A 341 ? 0.0469 0.0438 0.0512 -0.0002 -0.0062 0.0018 422 PHE A N 2621 C CA . PHE A 341 ? 0.0752 0.0725 0.0803 0.0007 -0.0062 0.0019 422 PHE A CA 2622 C C . PHE A 341 ? 0.0749 0.0707 0.0800 0.0015 -0.0062 0.0021 422 PHE A C 2623 O O . PHE A 341 ? 0.0794 0.0744 0.0841 0.0015 -0.0064 0.0024 422 PHE A O 2624 C CB . PHE A 341 ? 0.0493 0.0491 0.0554 0.0011 -0.0064 0.0020 422 PHE A CB 2625 C CG . PHE A 341 ? 0.0784 0.0787 0.0848 0.0017 -0.0068 0.0025 422 PHE A CG 2626 C CD1 . PHE A 341 ? 0.0789 0.0805 0.0850 0.0011 -0.0071 0.0026 422 PHE A CD1 2627 C CD2 . PHE A 341 ? 0.1057 0.1054 0.1126 0.0029 -0.0068 0.0029 422 PHE A CD2 2628 C CE1 . PHE A 341 ? 0.0818 0.0842 0.0881 0.0018 -0.0075 0.0032 422 PHE A CE1 2629 C CE2 . PHE A 341 ? 0.0936 0.0939 0.1008 0.0036 -0.0072 0.0036 422 PHE A CE2 2630 C CZ . PHE A 341 ? 0.0812 0.0830 0.0881 0.0030 -0.0075 0.0038 422 PHE A CZ 2631 N N . TRP A 342 ? 0.0315 0.0270 0.0370 0.0021 -0.0060 0.0019 423 TRP A N 2632 C CA . TRP A 342 ? 0.0667 0.0608 0.0723 0.0028 -0.0060 0.0020 423 TRP A CA 2633 C C . TRP A 342 ? 0.0591 0.0538 0.0658 0.0037 -0.0059 0.0020 423 TRP A C 2634 O O . TRP A 342 ? 0.0364 0.0326 0.0437 0.0039 -0.0058 0.0018 423 TRP A O 2635 C CB . TRP A 342 ? 0.0733 0.0662 0.0785 0.0025 -0.0057 0.0015 423 TRP A CB 2636 C CG . TRP A 342 ? 0.0723 0.0662 0.0777 0.0024 -0.0054 0.0011 423 TRP A CG 2637 C CD1 . TRP A 342 ? 0.0764 0.0707 0.0812 0.0018 -0.0053 0.0010 423 TRP A CD1 2638 C CD2 . TRP A 342 ? 0.0941 0.0885 0.1002 0.0030 -0.0052 0.0006 423 TRP A CD2 2639 N NE1 . TRP A 342 ? 0.0787 0.0740 0.0838 0.0019 -0.0050 0.0006 423 TRP A NE1 2640 C CE2 . TRP A 342 ? 0.0870 0.0825 0.0929 0.0027 -0.0049 0.0003 423 TRP A CE2 2641 C CE3 . TRP A 342 ? 0.0773 0.0713 0.0841 0.0038 -0.0051 0.0005 423 TRP A CE3 2642 C CZ2 . TRP A 342 ? 0.0948 0.0910 0.1011 0.0031 -0.0046 -0.0002 423 TRP A CZ2 2643 C CZ3 . TRP A 342 ? 0.0652 0.0599 0.0726 0.0042 -0.0047 -0.0001 423 TRP A CZ3 2644 C CH2 . TRP A 342 ? 0.1063 0.1021 0.1134 0.0039 -0.0045 -0.0005 423 TRP A CH2 2645 N N . VAL A 343 ? 0.0272 0.0207 0.0342 0.0044 -0.0059 0.0022 424 VAL A N 2646 C CA . VAL A 343 ? 0.0533 0.0469 0.0613 0.0054 -0.0056 0.0023 424 VAL A CA 2647 C C . VAL A 343 ? 0.0871 0.0787 0.0951 0.0056 -0.0052 0.0018 424 VAL A C 2648 O O . VAL A 343 ? 0.0817 0.0718 0.0892 0.0053 -0.0052 0.0020 424 VAL A O 2649 C CB . VAL A 343 ? 0.0599 0.0540 0.0684 0.0062 -0.0058 0.0032 424 VAL A CB 2650 C CG1 . VAL A 343 ? 0.0960 0.0901 0.1055 0.0074 -0.0054 0.0033 424 VAL A CG1 2651 C CG2 . VAL A 343 ? 0.0698 0.0663 0.0782 0.0058 -0.0063 0.0035 424 VAL A CG2 2652 N N . GLU A 344 ? 0.0830 0.0747 0.0917 0.0060 -0.0048 0.0012 425 GLU A N 2653 C CA . GLU A 344 ? 0.1056 0.0955 0.1144 0.0062 -0.0043 0.0005 425 GLU A CA 2654 C C . GLU A 344 ? 0.0902 0.0790 0.0999 0.0072 -0.0039 0.0010 425 GLU A C 2655 O O . GLU A 344 ? 0.1049 0.0948 0.1154 0.0081 -0.0038 0.0013 425 GLU A O 2656 C CB . GLU A 344 ? 0.0902 0.0807 0.0991 0.0061 -0.0039 -0.0005 425 GLU A CB 2657 C CG . GLU A 344 ? 0.1100 0.0991 0.1192 0.0061 -0.0033 -0.0014 425 GLU A CG 2658 C CD . GLU A 344 ? 0.1459 0.1359 0.1555 0.0063 -0.0028 -0.0025 425 GLU A CD 2659 O OE1 . GLU A 344 ? 0.1382 0.1295 0.1484 0.0069 -0.0028 -0.0023 425 GLU A OE1 2660 O OE2 . GLU A 344 ? 0.1277 0.1174 0.1369 0.0057 -0.0025 -0.0035 425 GLU A OE2 2661 N N . LEU A 345 ? 0.0777 0.0646 0.0873 0.0071 -0.0037 0.0011 426 LEU A N 2662 C CA . LEU A 345 ? 0.0764 0.0618 0.0867 0.0081 -0.0032 0.0016 426 LEU A CA 2663 C C . LEU A 345 ? 0.1058 0.0895 0.1167 0.0081 -0.0023 0.0005 426 LEU A C 2664 O O . LEU A 345 ? 0.1018 0.0840 0.1123 0.0074 -0.0021 0.0000 426 LEU A O 2665 C CB . LEU A 345 ? 0.0789 0.0632 0.0888 0.0080 -0.0034 0.0026 426 LEU A CB 2666 C CG . LEU A 345 ? 0.1010 0.0870 0.1103 0.0076 -0.0042 0.0034 426 LEU A CG 2667 C CD1 . LEU A 345 ? 0.1200 0.1049 0.1288 0.0075 -0.0043 0.0042 426 LEU A CD1 2668 C CD2 . LEU A 345 ? 0.1067 0.0947 0.1165 0.0084 -0.0045 0.0041 426 LEU A CD2 2669 N N . ILE A 346 ? 0.0769 0.0610 0.0886 0.0089 -0.0019 0.0001 427 ILE A N 2670 C CA . ILE A 346 ? 0.1049 0.0876 0.1170 0.0088 -0.0010 -0.0013 427 ILE A CA 2671 C C . ILE A 346 ? 0.1226 0.1026 0.1354 0.0094 -0.0001 -0.0011 427 ILE A C 2672 O O . ILE A 346 ? 0.0983 0.0779 0.1118 0.0107 0.0001 0.0000 427 ILE A O 2673 C CB . ILE A 346 ? 0.0978 0.0820 0.1106 0.0095 -0.0007 -0.0019 427 ILE A CB 2674 C CG1 . ILE A 346 ? 0.1026 0.0894 0.1147 0.0088 -0.0014 -0.0021 427 ILE A CG1 2675 C CG2 . ILE A 346 ? 0.1098 0.0927 0.1230 0.0093 0.0003 -0.0035 427 ILE A CG2 2676 C CD1 . ILE A 346 ? 0.1323 0.1210 0.1451 0.0094 -0.0012 -0.0025 427 ILE A CD1 2677 N N . ARG A 347 ? 0.1247 0.1030 0.1373 0.0086 0.0004 -0.0021 428 ARG A N 2678 C CA . ARG A 347 ? 0.1257 0.1010 0.1389 0.0089 0.0014 -0.0022 428 ARG A CA 2679 C C . ARG A 347 ? 0.1462 0.1205 0.1599 0.0085 0.0024 -0.0040 428 ARG A C 2680 O O . ARG A 347 ? 0.1286 0.1042 0.1417 0.0075 0.0021 -0.0054 428 ARG A O 2681 C CB . ARG A 347 ? 0.1383 0.1122 0.1509 0.0080 0.0013 -0.0018 428 ARG A CB 2682 C CG . ARG A 347 ? 0.1280 0.1029 0.1400 0.0082 0.0004 -0.0001 428 ARG A CG 2683 C CD . ARG A 347 ? 0.1397 0.1145 0.1525 0.0098 0.0005 0.0015 428 ARG A CD 2684 N NE . ARG A 347 ? 0.1195 0.0913 0.1330 0.0105 0.0017 0.0018 428 ARG A NE 2685 C CZ . ARG A 347 ? 0.1493 0.1193 0.1627 0.0104 0.0020 0.0027 428 ARG A CZ 2686 N NH1 . ARG A 347 ? 0.1350 0.1059 0.1475 0.0097 0.0011 0.0034 428 ARG A NH1 2687 N NH2 . ARG A 347 ? 0.1421 0.1092 0.1563 0.0110 0.0031 0.0030 428 ARG A NH2 2688 N N . GLY A 348 ? 0.1466 0.1185 0.1613 0.0094 0.0035 -0.0041 429 GLY A N 2689 C CA . GLY A 348 ? 0.1409 0.1114 0.1560 0.0090 0.0046 -0.0060 429 GLY A CA 2690 C C . GLY A 348 ? 0.1561 0.1272 0.1721 0.0103 0.0052 -0.0064 429 GLY A C 2691 O O . GLY A 348 ? 0.1542 0.1254 0.1710 0.0118 0.0052 -0.0050 429 GLY A O 2692 N N . ARG A 349 ? 0.1759 0.1476 0.1919 0.0097 0.0056 -0.0083 430 ARG A N 2693 C CA . ARG A 349 ? 0.1880 0.1604 0.2049 0.0108 0.0062 -0.0089 430 ARG A CA 2694 C C . ARG A 349 ? 0.1885 0.1642 0.2052 0.0115 0.0051 -0.0078 430 ARG A C 2695 O O . ARG A 349 ? 0.1982 0.1759 0.2140 0.0107 0.0040 -0.0073 430 ARG A O 2696 C CB . ARG A 349 ? 0.2121 0.1848 0.2288 0.0098 0.0069 -0.0113 430 ARG A CB 2697 C CG . ARG A 349 ? 0.2755 0.2454 0.2924 0.0088 0.0080 -0.0127 430 ARG A CG 2698 C CD . ARG A 349 ? 0.3499 0.3161 0.3678 0.0099 0.0091 -0.0118 430 ARG A CD 2699 N NE . ARG A 349 ? 0.4941 0.4586 0.5131 0.0108 0.0106 -0.0129 430 ARG A NE 2700 C CZ . ARG A 349 ? 0.5167 0.4801 0.5368 0.0128 0.0112 -0.0117 430 ARG A CZ 2701 N NH1 . ARG A 349 ? 0.4574 0.4215 0.4775 0.0140 0.0104 -0.0093 430 ARG A NH1 2702 N NH2 . ARG A 349 ? 0.6713 0.6330 0.6925 0.0137 0.0127 -0.0129 430 ARG A NH2 2703 N N . PRO A 350 ? 0.2244 0.2007 0.2421 0.0130 0.0056 -0.0074 431 PRO A N 2704 C CA . PRO A 350 ? 0.2319 0.2058 0.2509 0.0142 0.0070 -0.0079 431 PRO A CA 2705 C C . PRO A 350 ? 0.2482 0.2200 0.2680 0.0157 0.0074 -0.0060 431 PRO A C 2706 O O . PRO A 350 ? 0.2840 0.2534 0.3048 0.0169 0.0087 -0.0061 431 PRO A O 2707 C CB . PRO A 350 ? 0.2719 0.2482 0.2915 0.0152 0.0071 -0.0083 431 PRO A CB 2708 C CG . PRO A 350 ? 0.3475 0.3275 0.3662 0.0144 0.0057 -0.0079 431 PRO A CG 2709 C CD . PRO A 350 ? 0.2424 0.2220 0.2601 0.0136 0.0047 -0.0067 431 PRO A CD 2710 N N . LYS A 351 ? 0.1993 0.1719 0.2184 0.0157 0.0064 -0.0042 432 LYS A N 2711 C CA . LYS A 351 ? 0.2711 0.2425 0.2909 0.0172 0.0066 -0.0021 432 LYS A CA 2712 C C . LYS A 351 ? 0.2775 0.2451 0.2973 0.0169 0.0074 -0.0019 432 LYS A C 2713 O O . LYS A 351 ? 0.2270 0.1927 0.2475 0.0184 0.0081 -0.0004 432 LYS A O 2714 C CB . LYS A 351 ? 0.2629 0.2372 0.2821 0.0173 0.0051 -0.0004 432 LYS A CB 2715 C CG . LYS A 351 ? 0.2993 0.2773 0.3186 0.0178 0.0043 -0.0003 432 LYS A CG 2716 C CD . LYS A 351 ? 0.4216 0.3999 0.4424 0.0199 0.0050 0.0004 432 LYS A CD 2717 C CE . LYS A 351 ? 0.4867 0.4692 0.5078 0.0204 0.0042 0.0007 432 LYS A CE 2718 N NZ . LYS A 351 ? 0.6004 0.5837 0.6229 0.0226 0.0048 0.0016 432 LYS A NZ 2719 N N . GLU A 352 ? 0.1774 0.1439 0.1964 0.0151 0.0074 -0.0032 433 GLU A N 2720 C CA . GLU A 352 ? 0.1993 0.1624 0.2183 0.0145 0.0082 -0.0030 433 GLU A CA 2721 C C . GLU A 352 ? 0.1846 0.1453 0.2038 0.0134 0.0095 -0.0054 433 GLU A C 2722 O O . GLU A 352 ? 0.2231 0.1853 0.2420 0.0125 0.0094 -0.0072 433 GLU A O 2723 C CB . GLU A 352 ? 0.1859 0.1499 0.2036 0.0132 0.0070 -0.0022 433 GLU A CB 2724 C CG . GLU A 352 ? 0.2132 0.1798 0.2307 0.0142 0.0058 -0.0001 433 GLU A CG 2725 C CD . GLU A 352 ? 0.2214 0.1889 0.2377 0.0129 0.0047 0.0005 433 GLU A CD 2726 O OE1 . GLU A 352 ? 0.1330 0.1031 0.1485 0.0120 0.0036 -0.0001 433 GLU A OE1 2727 O OE2 . GLU A 352 ? 0.2078 0.1733 0.2239 0.0129 0.0049 0.0016 433 GLU A OE2 2728 N N . ASN A 353 ? 0.2480 0.2050 0.2676 0.0133 0.0107 -0.0053 435 ASN A N 2729 C CA . ASN A 353 ? 0.3041 0.2584 0.3240 0.0122 0.0122 -0.0076 435 ASN A CA 2730 C C . ASN A 353 ? 0.2689 0.2237 0.2878 0.0098 0.0118 -0.0092 435 ASN A C 2731 O O . ASN A 353 ? 0.2674 0.2196 0.2863 0.0088 0.0125 -0.0094 435 ASN A O 2732 C CB . ASN A 353 ? 0.4325 0.3823 0.4534 0.0131 0.0140 -0.0069 435 ASN A CB 2733 C CG . ASN A 353 ? 0.5413 0.4904 0.5634 0.0155 0.0148 -0.0059 435 ASN A CG 2734 O OD1 . ASN A 353 ? 0.6652 0.6116 0.6881 0.0170 0.0157 -0.0042 435 ASN A OD1 2735 N ND2 . ASN A 353 ? 0.5521 0.5038 0.5745 0.0161 0.0144 -0.0068 435 ASN A ND2 2736 N N . THR A 354 ? 0.1745 0.1327 0.1927 0.0089 0.0106 -0.0102 436 THR A N 2737 C CA . THR A 354 ? 0.1616 0.1210 0.1788 0.0067 0.0102 -0.0117 436 THR A CA 2738 C C . THR A 354 ? 0.1687 0.1299 0.1859 0.0059 0.0104 -0.0141 436 THR A C 2739 O O . THR A 354 ? 0.1704 0.1319 0.1881 0.0070 0.0108 -0.0145 436 THR A O 2740 C CB . THR A 354 ? 0.1671 0.1294 0.1833 0.0063 0.0084 -0.0104 436 THR A CB 2741 O OG1 . THR A 354 ? 0.1431 0.1083 0.1591 0.0073 0.0074 -0.0098 436 THR A OG1 2742 C CG2 . THR A 354 ? 0.1579 0.1187 0.1741 0.0069 0.0082 -0.0082 436 THR A CG2 2743 N N . ILE A 355 ? 0.1324 0.0950 0.1488 0.0041 0.0100 -0.0157 437 ILE A N 2744 C CA . ILE A 355 ? 0.1493 0.1142 0.1654 0.0032 0.0100 -0.0178 437 ILE A CA 2745 C C . ILE A 355 ? 0.1638 0.1327 0.1789 0.0032 0.0084 -0.0171 437 ILE A C 2746 O O . ILE A 355 ? 0.1774 0.1488 0.1921 0.0028 0.0082 -0.0184 437 ILE A O 2747 C CB . ILE A 355 ? 0.1767 0.1411 0.1925 0.0012 0.0107 -0.0201 437 ILE A CB 2748 C CG1 . ILE A 355 ? 0.1612 0.1271 0.1761 -0.0001 0.0096 -0.0195 437 ILE A CG1 2749 C CG2 . ILE A 355 ? 0.2083 0.1684 0.2251 0.0010 0.0125 -0.0209 437 ILE A CG2 2750 C CD1 . ILE A 355 ? 0.2109 0.1774 0.2255 -0.0022 0.0100 -0.0217 437 ILE A CD1 2751 N N . TRP A 356 ? 0.1310 0.1005 0.1456 0.0035 0.0073 -0.0150 438 TRP A N 2752 C CA . TRP A 356 ? 0.1262 0.0991 0.1398 0.0033 0.0058 -0.0143 438 TRP A CA 2753 C C . TRP A 356 ? 0.1299 0.1036 0.1435 0.0047 0.0049 -0.0122 438 TRP A C 2754 O O . TRP A 356 ? 0.1035 0.0754 0.1179 0.0059 0.0054 -0.0110 438 TRP A O 2755 C CB . TRP A 356 ? 0.1167 0.0899 0.1295 0.0020 0.0051 -0.0141 438 TRP A CB 2756 C CG . TRP A 356 ? 0.1064 0.0770 0.1196 0.0023 0.0054 -0.0127 438 TRP A CG 2757 C CD1 . TRP A 356 ? 0.1538 0.1213 0.1675 0.0018 0.0065 -0.0132 438 TRP A CD1 2758 C CD2 . TRP A 356 ? 0.1097 0.0804 0.1226 0.0031 0.0045 -0.0104 438 TRP A CD2 2759 N NE1 . TRP A 356 ? 0.1370 0.1028 0.1508 0.0023 0.0064 -0.0114 438 TRP A NE1 2760 C CE2 . TRP A 356 ? 0.1351 0.1030 0.1484 0.0031 0.0051 -0.0097 438 TRP A CE2 2761 C CE3 . TRP A 356 ? 0.1198 0.0928 0.1321 0.0037 0.0033 -0.0091 438 TRP A CE3 2762 C CZ2 . TRP A 356 ? 0.1429 0.1104 0.1561 0.0038 0.0045 -0.0076 438 TRP A CZ2 2763 C CZ3 . TRP A 356 ? 0.1310 0.1035 0.1431 0.0043 0.0027 -0.0072 438 TRP A CZ3 2764 C CH2 . TRP A 356 ? 0.1455 0.1154 0.1580 0.0043 0.0033 -0.0064 438 TRP A CH2 2765 N N . THR A 357 ? 0.1303 0.1070 0.1432 0.0045 0.0038 -0.0118 439 THR A N 2766 C CA . THR A 357 ? 0.1354 0.1133 0.1481 0.0055 0.0029 -0.0099 439 THR A CA 2767 C C . THR A 357 ? 0.1159 0.0957 0.1275 0.0047 0.0018 -0.0093 439 THR A C 2768 O O . THR A 357 ? 0.1104 0.0920 0.1212 0.0038 0.0015 -0.0102 439 THR A O 2769 C CB . THR A 357 ? 0.2016 0.1813 0.2146 0.0064 0.0029 -0.0101 439 THR A CB 2770 O OG1 . THR A 357 ? 0.1924 0.1704 0.2065 0.0074 0.0041 -0.0107 439 THR A OG1 2771 C CG2 . THR A 357 ? 0.1828 0.1640 0.1957 0.0072 0.0020 -0.0082 439 THR A CG2 2772 N N . SER A 358 ? 0.1112 0.0906 0.1225 0.0051 0.0011 -0.0076 440 SER A N 2773 C CA . SER A 358 ? 0.1106 0.0916 0.1210 0.0044 0.0001 -0.0069 440 SER A CA 2774 C C . SER A 358 ? 0.1879 0.1691 0.1982 0.0051 -0.0005 -0.0051 440 SER A C 2775 O O . SER A 358 ? 0.2077 0.1878 0.2188 0.0061 -0.0002 -0.0043 440 SER A O 2776 C CB . SER A 358 ? 0.1392 0.1194 0.1492 0.0033 0.0002 -0.0073 440 SER A CB 2777 O OG . SER A 358 ? 0.1168 0.0987 0.1258 0.0027 -0.0007 -0.0069 440 SER A OG 2778 N N . GLY A 359 ? 0.1964 0.1791 0.2059 0.0047 -0.0014 -0.0044 441 GLY A N 2779 C CA . GLY A 359 ? 0.1671 0.1502 0.1764 0.0052 -0.0020 -0.0029 441 GLY A CA 2780 C C . GLY A 359 ? 0.2031 0.1863 0.2116 0.0045 -0.0026 -0.0023 441 GLY A C 2781 O O . GLY A 359 ? 0.1842 0.1679 0.1921 0.0037 -0.0027 -0.0029 441 GLY A O 2782 N N . SER A 360 ? 0.1284 0.1112 0.1368 0.0049 -0.0029 -0.0010 442 SER A N 2783 C CA . SER A 360 ? 0.1338 0.1170 0.1415 0.0044 -0.0035 -0.0004 442 SER A CA 2784 C C . SER A 360 ? 0.1383 0.1231 0.1456 0.0046 -0.0041 0.0003 442 SER A C 2785 O O . SER A 360 ? 0.1404 0.1262 0.1483 0.0051 -0.0040 0.0003 442 SER A O 2786 C CB . SER A 360 ? 0.1144 0.0960 0.1220 0.0044 -0.0034 0.0004 442 SER A CB 2787 O OG . SER A 360 ? 0.1511 0.1327 0.1593 0.0054 -0.0034 0.0014 442 SER A OG 2788 N N . SER A 361 ? 0.1288 0.1140 0.1355 0.0042 -0.0046 0.0009 443 SER A N 2789 C CA . SER A 361 ? 0.1307 0.1174 0.1370 0.0042 -0.0050 0.0014 443 SER A CA 2790 C C . SER A 361 ? 0.1078 0.0947 0.1138 0.0041 -0.0054 0.0023 443 SER A C 2791 O O . SER A 361 ? 0.1195 0.1054 0.1251 0.0038 -0.0054 0.0025 443 SER A O 2792 C CB . SER A 361 ? 0.1478 0.1355 0.1535 0.0036 -0.0051 0.0009 443 SER A CB 2793 O OG . SER A 361 ? 0.2000 0.1871 0.2050 0.0030 -0.0053 0.0009 443 SER A OG 2794 N N . ILE A 362 ? 0.0590 0.0473 0.0650 0.0043 -0.0057 0.0027 444 ILE A N 2795 C CA . ILE A 362 ? 0.0883 0.0771 0.0938 0.0040 -0.0061 0.0034 444 ILE A CA 2796 C C . ILE A 362 ? 0.0858 0.0761 0.0910 0.0035 -0.0063 0.0031 444 ILE A C 2797 O O . ILE A 362 ? 0.0640 0.0551 0.0696 0.0036 -0.0062 0.0027 444 ILE A O 2798 C CB . ILE A 362 ? 0.0647 0.0540 0.0706 0.0047 -0.0063 0.0042 444 ILE A CB 2799 C CG1 . ILE A 362 ? 0.0600 0.0506 0.0668 0.0054 -0.0062 0.0043 444 ILE A CG1 2800 C CG2 . ILE A 362 ? 0.1206 0.1082 0.1267 0.0051 -0.0060 0.0047 444 ILE A CG2 2801 C CD1 . ILE A 362 ? 0.0586 0.0501 0.0659 0.0064 -0.0063 0.0053 444 ILE A CD1 2802 N N . SER A 363 ? 0.0654 0.0559 0.0698 0.0029 -0.0065 0.0033 445 SER A N 2803 C CA . SER A 363 ? 0.0903 0.0820 0.0944 0.0022 -0.0066 0.0030 445 SER A CA 2804 C C . SER A 363 ? 0.1003 0.0928 0.1041 0.0018 -0.0069 0.0033 445 SER A C 2805 O O . SER A 363 ? 0.0871 0.0790 0.0905 0.0018 -0.0070 0.0037 445 SER A O 2806 C CB . SER A 363 ? 0.1038 0.0946 0.1073 0.0017 -0.0064 0.0026 445 SER A CB 2807 O OG . SER A 363 ? 0.0995 0.0893 0.1023 0.0013 -0.0064 0.0027 445 SER A OG 2808 N N . PHE A 364 ? 0.0613 0.0553 0.0651 0.0013 -0.0069 0.0031 446 PHE A N 2809 C CA . PHE A 364 ? 0.0808 0.0760 0.0843 0.0007 -0.0072 0.0032 446 PHE A CA 2810 C C . PHE A 364 ? 0.1053 0.1008 0.1083 -0.0003 -0.0069 0.0026 446 PHE A C 2811 O O . PHE A 364 ? 0.0771 0.0725 0.0803 -0.0004 -0.0066 0.0023 446 PHE A O 2812 C CB . PHE A 364 ? 0.0733 0.0707 0.0775 0.0013 -0.0075 0.0036 446 PHE A CB 2813 C CG . PHE A 364 ? 0.0711 0.0681 0.0757 0.0024 -0.0076 0.0043 446 PHE A CG 2814 C CD1 . PHE A 364 ? 0.0841 0.0802 0.0893 0.0032 -0.0074 0.0044 446 PHE A CD1 2815 C CD2 . PHE A 364 ? 0.1126 0.1102 0.1170 0.0026 -0.0079 0.0050 446 PHE A CD2 2816 C CE1 . PHE A 364 ? 0.1129 0.1083 0.1186 0.0042 -0.0074 0.0051 446 PHE A CE1 2817 C CE2 . PHE A 364 ? 0.1098 0.1068 0.1145 0.0036 -0.0079 0.0058 446 PHE A CE2 2818 C CZ . PHE A 364 ? 0.0985 0.0943 0.1039 0.0044 -0.0076 0.0058 446 PHE A CZ 2819 N N . CYS A 365 ? 0.0896 0.0852 0.0920 -0.0011 -0.0069 0.0024 447 CYS A N 2820 C CA . CYS A 365 ? 0.0749 0.0707 0.0769 -0.0022 -0.0065 0.0017 447 CYS A CA 2821 C C . CYS A 365 ? 0.0805 0.0785 0.0826 -0.0030 -0.0067 0.0014 447 CYS A C 2822 O O . CYS A 365 ? 0.1004 0.0994 0.1024 -0.0028 -0.0071 0.0017 447 CYS A O 2823 C CB . CYS A 365 ? 0.1400 0.1335 0.1411 -0.0027 -0.0061 0.0015 447 CYS A CB 2824 S SG . CYS A 365 ? 0.2360 0.2277 0.2371 -0.0022 -0.0057 0.0017 447 CYS A SG 2825 N N . GLY A 366 ? 0.0981 0.0971 0.1004 -0.0039 -0.0064 0.0008 448 GLY A N 2826 C CA . GLY A 366 ? 0.1217 0.1232 0.1241 -0.0047 -0.0066 0.0004 448 GLY A CA 2827 C C . GLY A 366 ? 0.1081 0.1090 0.1096 -0.0058 -0.0064 -0.0002 448 GLY A C 2828 O O . GLY A 366 ? 0.1351 0.1338 0.1360 -0.0064 -0.0057 -0.0006 448 GLY A O 2829 N N . VAL A 367 ? 0.0774 0.0805 0.0789 -0.0060 -0.0068 -0.0003 449 VAL A N 2830 C CA . VAL A 367 ? 0.0767 0.0796 0.0773 -0.0071 -0.0066 -0.0010 449 VAL A CA 2831 C C . VAL A 367 ? 0.1102 0.1167 0.1110 -0.0081 -0.0069 -0.0016 449 VAL A C 2832 O O . VAL A 367 ? 0.1022 0.1114 0.1039 -0.0076 -0.0074 -0.0013 449 VAL A O 2833 C CB . VAL A 367 ? 0.0898 0.0916 0.0898 -0.0064 -0.0069 -0.0005 449 VAL A CB 2834 C CG1 . VAL A 367 ? 0.0839 0.0824 0.0837 -0.0056 -0.0065 0.0000 449 VAL A CG1 2835 C CG2 . VAL A 367 ? 0.1028 0.1069 0.1033 -0.0053 -0.0076 0.0004 449 VAL A CG2 2836 N N . ASN A 368 ? 0.1402 0.1468 0.1403 -0.0094 -0.0066 -0.0026 450 ASN A N 2837 C CA . ASN A 368 ? 0.1524 0.1627 0.1526 -0.0104 -0.0069 -0.0033 450 ASN A CA 2838 C C . ASN A 368 ? 0.2100 0.2216 0.2095 -0.0103 -0.0073 -0.0032 450 ASN A C 2839 O O . ASN A 368 ? 0.2357 0.2505 0.2351 -0.0111 -0.0076 -0.0039 450 ASN A O 2840 C CB . ASN A 368 ? 0.2024 0.2126 0.2024 -0.0124 -0.0061 -0.0048 450 ASN A CB 2841 C CG . ASN A 368 ? 0.2645 0.2752 0.2653 -0.0127 -0.0058 -0.0050 450 ASN A CG 2842 O OD1 . ASN A 368 ? 0.3024 0.3165 0.3040 -0.0125 -0.0064 -0.0047 450 ASN A OD1 2843 N ND2 . ASN A 368 ? 0.3015 0.3091 0.3022 -0.0133 -0.0049 -0.0053 450 ASN A ND2 2844 N N . SER A 369 ? 0.1863 0.1955 0.1853 -0.0092 -0.0074 -0.0024 451 SER A N 2845 C CA . SER A 369 ? 0.1950 0.2052 0.1934 -0.0088 -0.0078 -0.0020 451 SER A CA 2846 C C . SER A 369 ? 0.1673 0.1795 0.1663 -0.0072 -0.0087 -0.0005 451 SER A C 2847 O O . SER A 369 ? 0.1489 0.1616 0.1488 -0.0065 -0.0088 0.0000 451 SER A O 2848 C CB . SER A 369 ? 0.1787 0.1854 0.1763 -0.0086 -0.0074 -0.0020 451 SER A CB 2849 O OG . SER A 369 ? 0.1638 0.1677 0.1618 -0.0075 -0.0072 -0.0012 451 SER A OG 2850 N N . ASP A 370 ? 0.1571 0.1702 0.1555 -0.0067 -0.0091 0.0001 452 ASP A N 2851 C CA . ASP A 370 ? 0.1696 0.1847 0.1686 -0.0051 -0.0097 0.0017 452 ASP A CA 2852 C C . ASP A 370 ? 0.1298 0.1422 0.1294 -0.0037 -0.0097 0.0028 452 ASP A C 2853 O O . ASP A 370 ? 0.1437 0.1527 0.1429 -0.0036 -0.0093 0.0027 452 ASP A O 2854 C CB . ASP A 370 ? 0.1321 0.1487 0.1302 -0.0049 -0.0101 0.0022 452 ASP A CB 2855 C CG . ASP A 370 ? 0.2841 0.3047 0.2818 -0.0062 -0.0103 0.0012 452 ASP A CG 2856 O OD1 . ASP A 370 ? 0.3138 0.3364 0.3120 -0.0070 -0.0103 0.0004 452 ASP A OD1 2857 O OD2 . ASP A 370 ? 0.2428 0.2647 0.2397 -0.0064 -0.0105 0.0013 452 ASP A OD2 2858 N N . THR A 371 ? 0.0824 0.0964 0.0829 -0.0025 -0.0101 0.0038 453 THR A N 2859 C CA . THR A 371 ? 0.0823 0.0939 0.0835 -0.0011 -0.0100 0.0048 453 THR A CA 2860 C C . THR A 371 ? 0.0967 0.1101 0.0984 0.0004 -0.0104 0.0063 453 THR A C 2861 O O . THR A 371 ? 0.1202 0.1370 0.1218 0.0005 -0.0108 0.0066 453 THR A O 2862 C CB . THR A 371 ? 0.1287 0.1396 0.1307 -0.0011 -0.0097 0.0043 453 THR A CB 2863 O OG1 . THR A 371 ? 0.1528 0.1673 0.1555 -0.0012 -0.0100 0.0042 453 THR A OG1 2864 C CG2 . THR A 371 ? 0.0986 0.1072 0.1001 -0.0025 -0.0091 0.0030 453 THR A CG2 2865 N N . VAL A 372 ? 0.0869 0.0983 0.0892 0.0017 -0.0102 0.0072 454 VAL A N 2866 C CA . VAL A 372 ? 0.1013 0.1138 0.1042 0.0033 -0.0105 0.0087 454 VAL A CA 2867 C C . VAL A 372 ? 0.1211 0.1318 0.1250 0.0045 -0.0102 0.0092 454 VAL A C 2868 O O . VAL A 372 ? 0.1148 0.1225 0.1188 0.0042 -0.0097 0.0086 454 VAL A O 2869 C CB . VAL A 372 ? 0.1126 0.1239 0.1147 0.0038 -0.0104 0.0097 454 VAL A CB 2870 C CG1 . VAL A 372 ? 0.0961 0.1033 0.0981 0.0038 -0.0099 0.0096 454 VAL A CG1 2871 C CG2 . VAL A 372 ? 0.1167 0.1298 0.1193 0.0054 -0.0107 0.0114 454 VAL A CG2 2872 N N . GLY A 373 ? 0.1077 0.1204 0.1125 0.0058 -0.0103 0.0102 455 GLY A N 2873 C CA . GLY A 373 ? 0.1056 0.1167 0.1115 0.0071 -0.0100 0.0108 455 GLY A CA 2874 C C . GLY A 373 ? 0.1367 0.1451 0.1425 0.0082 -0.0096 0.0119 455 GLY A C 2875 O O . GLY A 373 ? 0.1425 0.1516 0.1477 0.0084 -0.0098 0.0128 455 GLY A O 2876 N N . TRP A 374 ? 0.1017 0.1072 0.1081 0.0087 -0.0091 0.0118 456 TRP A N 2877 C CA . TRP A 374 ? 0.1263 0.1290 0.1327 0.0096 -0.0086 0.0128 456 TRP A CA 2878 C C . TRP A 374 ? 0.1273 0.1276 0.1346 0.0103 -0.0080 0.0124 456 TRP A C 2879 O O . TRP A 374 ? 0.1332 0.1347 0.1413 0.0104 -0.0080 0.0118 456 TRP A O 2880 C CB . TRP A 374 ? 0.1102 0.1107 0.1155 0.0086 -0.0085 0.0124 456 TRP A CB 2881 C CG . TRP A 374 ? 0.1333 0.1323 0.1385 0.0093 -0.0082 0.0137 456 TRP A CG 2882 C CD1 . TRP A 374 ? 0.1554 0.1555 0.1608 0.0106 -0.0081 0.0153 456 TRP A CD1 2883 C CD2 . TRP A 374 ? 0.1130 0.1090 0.1176 0.0087 -0.0078 0.0135 456 TRP A CD2 2884 N NE1 . TRP A 374 ? 0.1361 0.1339 0.1411 0.0109 -0.0077 0.0162 456 TRP A NE1 2885 C CE2 . TRP A 374 ? 0.1329 0.1283 0.1375 0.0097 -0.0075 0.0151 456 TRP A CE2 2886 C CE3 . TRP A 374 ? 0.1129 0.1068 0.1170 0.0076 -0.0076 0.0123 456 TRP A CE3 2887 C CZ2 . TRP A 374 ? 0.1323 0.1251 0.1364 0.0094 -0.0070 0.0153 456 TRP A CZ2 2888 C CZ3 . TRP A 374 ? 0.1343 0.1260 0.1381 0.0073 -0.0072 0.0125 456 TRP A CZ3 2889 C CH2 . TRP A 374 ? 0.1248 0.1158 0.1285 0.0081 -0.0069 0.0140 456 TRP A CH2 2890 N N . SER A 375 ? 0.1207 0.1179 0.1281 0.0106 -0.0074 0.0127 457 SER A N 2891 C CA . SER A 375 ? 0.1241 0.1188 0.1322 0.0110 -0.0068 0.0121 457 SER A CA 2892 C C . SER A 375 ? 0.1189 0.1107 0.1264 0.0099 -0.0064 0.0113 457 SER A C 2893 O O . SER A 375 ? 0.1308 0.1210 0.1379 0.0099 -0.0062 0.0120 457 SER A O 2894 C CB . SER A 375 ? 0.1630 0.1568 0.1721 0.0127 -0.0062 0.0134 457 SER A CB 2895 O OG . SER A 375 ? 0.1271 0.1186 0.1369 0.0129 -0.0055 0.0126 457 SER A OG 2896 N N . TRP A 376 ? 0.1220 0.1131 0.1295 0.0091 -0.0064 0.0099 458 TRP A N 2897 C CA . TRP A 376 ? 0.1190 0.1078 0.1261 0.0082 -0.0061 0.0091 458 TRP A CA 2898 C C . TRP A 376 ? 0.1055 0.0925 0.1133 0.0085 -0.0054 0.0083 458 TRP A C 2899 O O . TRP A 376 ? 0.1408 0.1281 0.1486 0.0079 -0.0055 0.0072 458 TRP A O 2900 C CB . TRP A 376 ? 0.0973 0.0868 0.1035 0.0069 -0.0065 0.0081 458 TRP A CB 2901 C CG . TRP A 376 ? 0.0995 0.0902 0.1048 0.0063 -0.0070 0.0085 458 TRP A CG 2902 C CD1 . TRP A 376 ? 0.1129 0.1025 0.1174 0.0058 -0.0070 0.0087 458 TRP A CD1 2903 C CD2 . TRP A 376 ? 0.1199 0.1133 0.1250 0.0061 -0.0075 0.0087 458 TRP A CD2 2904 N NE1 . TRP A 376 ? 0.1110 0.1024 0.1149 0.0053 -0.0074 0.0089 458 TRP A NE1 2905 C CE2 . TRP A 376 ? 0.1254 0.1192 0.1295 0.0055 -0.0078 0.0089 458 TRP A CE2 2906 C CE3 . TRP A 376 ? 0.1247 0.1204 0.1303 0.0064 -0.0078 0.0086 458 TRP A CE3 2907 C CZ2 . TRP A 376 ? 0.1141 0.1104 0.1178 0.0051 -0.0082 0.0089 458 TRP A CZ2 2908 C CZ3 . TRP A 376 ? 0.1211 0.1194 0.1263 0.0060 -0.0083 0.0087 458 TRP A CZ3 2909 C CH2 . TRP A 376 ? 0.1294 0.1280 0.1336 0.0053 -0.0085 0.0088 458 TRP A CH2 2910 N N . PRO A 377 ? 0.1068 0.0920 0.1152 0.0093 -0.0048 0.0089 459 PRO A N 2911 C CA . PRO A 377 ? 0.1174 0.1010 0.1267 0.0097 -0.0041 0.0081 459 PRO A CA 2912 C C . PRO A 377 ? 0.1117 0.0932 0.1206 0.0087 -0.0037 0.0070 459 PRO A C 2913 O O . PRO A 377 ? 0.1140 0.0952 0.1222 0.0078 -0.0039 0.0069 459 PRO A O 2914 C CB . PRO A 377 ? 0.1607 0.1430 0.1707 0.0111 -0.0034 0.0094 459 PRO A CB 2915 C CG . PRO A 377 ? 0.1714 0.1549 0.1809 0.0114 -0.0039 0.0109 459 PRO A CG 2916 C CD . PRO A 377 ? 0.1090 0.0935 0.1174 0.0100 -0.0046 0.0103 459 PRO A CD 2917 N N . ASP A 378 ? 0.1390 0.1194 0.1487 0.0088 -0.0031 0.0060 460 ASP A N 2918 C CA . ASP A 378 ? 0.1307 0.1094 0.1401 0.0078 -0.0027 0.0047 460 ASP A CA 2919 C C . ASP A 378 ? 0.1466 0.1232 0.1559 0.0075 -0.0022 0.0052 460 ASP A C 2920 O O . ASP A 378 ? 0.1354 0.1117 0.1440 0.0064 -0.0024 0.0048 460 ASP A O 2921 C CB . ASP A 378 ? 0.1229 0.1008 0.1331 0.0081 -0.0020 0.0036 460 ASP A CB 2922 C CG . ASP A 378 ? 0.1692 0.1457 0.1793 0.0070 -0.0015 0.0023 460 ASP A CG 2923 O OD1 . ASP A 378 ? 0.1884 0.1660 0.1978 0.0060 -0.0019 0.0014 460 ASP A OD1 2924 O OD2 . ASP A 378 ? 0.1711 0.1453 0.1816 0.0071 -0.0006 0.0021 460 ASP A OD2 2925 N N . GLY A 379 ? 0.1168 0.0919 0.1267 0.0085 -0.0015 0.0062 461 GLY A N 2926 C CA . GLY A 379 ? 0.1348 0.1079 0.1446 0.0083 -0.0010 0.0069 461 GLY A CA 2927 C C . GLY A 379 ? 0.1442 0.1147 0.1544 0.0076 0.0000 0.0058 461 GLY A C 2928 O O . GLY A 379 ? 0.0997 0.0684 0.1098 0.0072 0.0005 0.0063 461 GLY A O 2929 N N . ALA A 380 ? 0.1044 0.0747 0.1150 0.0073 0.0003 0.0043 462 ALA A N 2930 C CA . ALA A 380 ? 0.1231 0.0912 0.1341 0.0065 0.0013 0.0030 462 ALA A CA 2931 C C . ALA A 380 ? 0.1569 0.1222 0.1689 0.0074 0.0025 0.0035 462 ALA A C 2932 O O . ALA A 380 ? 0.1424 0.1080 0.1549 0.0089 0.0026 0.0043 462 ALA A O 2933 C CB . ALA A 380 ? 0.1139 0.0830 0.1249 0.0057 0.0012 0.0011 462 ALA A CB 2934 N N . GLU A 381 ? 0.1361 0.0989 0.1484 0.0067 0.0035 0.0029 463 GLU A N 2935 C CA . GLU A 381 ? 0.1775 0.1372 0.1907 0.0075 0.0049 0.0033 463 GLU A CA 2936 C C . GLU A 381 ? 0.1768 0.1352 0.1906 0.0069 0.0059 0.0012 463 GLU A C 2937 O O . GLU A 381 ? 0.1762 0.1340 0.1899 0.0053 0.0062 -0.0004 463 GLU A O 2938 C CB . GLU A 381 ? 0.2070 0.1642 0.2200 0.0069 0.0057 0.0041 463 GLU A CB 2939 C CG . GLU A 381 ? 0.3731 0.3316 0.3855 0.0074 0.0049 0.0062 463 GLU A CG 2940 C CD . GLU A 381 ? 0.5460 0.5043 0.5587 0.0094 0.0050 0.0082 463 GLU A CD 2941 O OE1 . GLU A 381 ? 0.6205 0.5775 0.6342 0.0105 0.0058 0.0081 463 GLU A OE1 2942 O OE2 . GLU A 381 ? 0.6362 0.5960 0.6484 0.0099 0.0043 0.0099 463 GLU A OE2 2943 N N . LEU A 382 ? 0.1724 0.1307 0.1870 0.0082 0.0063 0.0010 464 LEU A N 2944 C CA . LEU A 382 ? 0.1541 0.1113 0.1693 0.0078 0.0072 -0.0010 464 LEU A CA 2945 C C . LEU A 382 ? 0.2111 0.1644 0.2273 0.0086 0.0090 -0.0007 464 LEU A C 2946 O O . LEU A 382 ? 0.2217 0.1738 0.2383 0.0100 0.0093 0.0013 464 LEU A O 2947 C CB . LEU A 382 ? 0.1765 0.1362 0.1919 0.0087 0.0066 -0.0015 464 LEU A CB 2948 C CG . LEU A 382 ? 0.1791 0.1420 0.1936 0.0075 0.0054 -0.0026 464 LEU A CG 2949 C CD1 . LEU A 382 ? 0.1482 0.1129 0.1617 0.0070 0.0041 -0.0014 464 LEU A CD1 2950 C CD2 . LEU A 382 ? 0.1441 0.1092 0.1589 0.0085 0.0050 -0.0028 464 LEU A CD2 2951 N N . PRO A 383 ? 0.2326 0.1839 0.2493 0.0077 0.0102 -0.0028 465 PRO A N 2952 C CA . PRO A 383 ? 0.2078 0.1608 0.2242 0.0060 0.0099 -0.0053 465 PRO A CA 2953 C C . PRO A 383 ? 0.2138 0.1673 0.2295 0.0040 0.0095 -0.0060 465 PRO A C 2954 O O . PRO A 383 ? 0.2149 0.1670 0.2304 0.0039 0.0096 -0.0046 465 PRO A O 2955 C CB . PRO A 383 ? 0.2975 0.2477 0.3149 0.0059 0.0116 -0.0071 465 PRO A CB 2956 C CG . PRO A 383 ? 0.3849 0.3323 0.4032 0.0079 0.0127 -0.0054 465 PRO A CG 2957 C CD . PRO A 383 ? 0.3064 0.2538 0.3243 0.0084 0.0121 -0.0029 465 PRO A CD 2958 N N . PHE A 384 ? 0.1797 0.1352 0.1949 0.0026 0.0091 -0.0079 466 PHE A N 2959 C CA . PHE A 384 ? 0.1897 0.1460 0.2042 0.0007 0.0087 -0.0088 466 PHE A CA 2960 C C . PHE A 384 ? 0.1985 0.1527 0.2137 -0.0008 0.0102 -0.0109 466 PHE A C 2961 O O . PHE A 384 ? 0.1990 0.1507 0.2149 -0.0003 0.0116 -0.0118 466 PHE A O 2962 C CB . PHE A 384 ? 0.1634 0.1238 0.1771 0.0001 0.0073 -0.0096 466 PHE A CB 2963 C CG . PHE A 384 ? 0.1897 0.1523 0.2027 0.0008 0.0058 -0.0077 466 PHE A CG 2964 C CD1 . PHE A 384 ? 0.1696 0.1310 0.1827 0.0021 0.0057 -0.0055 466 PHE A CD1 2965 C CD2 . PHE A 384 ? 0.1926 0.1584 0.2047 0.0002 0.0046 -0.0081 466 PHE A CD2 2966 C CE1 . PHE A 384 ? 0.1716 0.1350 0.1839 0.0026 0.0045 -0.0040 466 PHE A CE1 2967 C CE2 . PHE A 384 ? 0.1531 0.1207 0.1645 0.0008 0.0034 -0.0065 466 PHE A CE2 2968 C CZ . PHE A 384 ? 0.1722 0.1387 0.1838 0.0019 0.0033 -0.0045 466 PHE A CZ 2969 N N . THR A 385 ? 0.1911 0.1460 0.2058 -0.0026 0.0101 -0.0119 467 THR A N 2970 C CA . THR A 385 ? 0.1897 0.1429 0.2049 -0.0043 0.0114 -0.0140 467 THR A CA 2971 C C . THR A 385 ? 0.2620 0.2160 0.2776 -0.0048 0.0119 -0.0164 467 THR A C 2972 O O . THR A 385 ? 0.2256 0.1768 0.2419 -0.0054 0.0136 -0.0180 467 THR A O 2973 C CB . THR A 385 ? 0.2235 0.1785 0.2381 -0.0062 0.0109 -0.0146 467 THR A CB 2974 O OG1 . THR A 385 ? 0.3721 0.3265 0.3865 -0.0058 0.0104 -0.0124 467 THR A OG1 2975 C CG2 . THR A 385 ? 0.3418 0.2951 0.3570 -0.0082 0.0124 -0.0169 467 THR A CG2 2976 N N . ILE A 386 ? 0.1542 0.1119 0.1690 -0.0046 0.0107 -0.0168 468 ILE A N 2977 C CA . ILE A 386 ? 0.1870 0.1461 0.2020 -0.0050 0.0110 -0.0190 468 ILE A CA 2978 C C . ILE A 386 ? 0.2630 0.2198 0.2788 -0.0033 0.0119 -0.0187 468 ILE A C 2979 O O . ILE A 386 ? 0.2724 0.2289 0.2885 -0.0035 0.0128 -0.0206 468 ILE A O 2980 C CB . ILE A 386 ? 0.1651 0.1287 0.1791 -0.0050 0.0094 -0.0191 468 ILE A CB 2981 C CG1 . ILE A 386 ? 0.1512 0.1168 0.1651 -0.0060 0.0097 -0.0217 468 ILE A CG1 2982 C CG2 . ILE A 386 ? 0.1807 0.1451 0.1946 -0.0030 0.0085 -0.0171 468 ILE A CG2 2983 C CD1 . ILE A 386 ? 0.2133 0.1794 0.2272 -0.0082 0.0103 -0.0238 468 ILE A CD1 2984 N N . ASP A 387 ? 0.3643 0.3196 0.3803 -0.0016 0.0117 -0.0162 469 ASP A N 2985 C CA . ASP A 387 ? 0.3642 0.3180 0.3808 0.0005 0.0122 -0.0153 469 ASP A CA 2986 C C . ASP A 387 ? 0.3689 0.3259 0.3850 0.0018 0.0106 -0.0138 469 ASP A C 2987 O O . ASP A 387 ? 0.2479 0.2071 0.2640 0.0021 0.0103 -0.0147 469 ASP A O 2988 C CB . ASP A 387 ? 0.4302 0.3826 0.4476 0.0003 0.0136 -0.0175 469 ASP A CB 2989 C CG . ASP A 387 ? 0.4729 0.4209 0.4912 -0.0004 0.0156 -0.0184 469 ASP A CG 2990 O OD1 . ASP A 387 ? 0.4930 0.4396 0.5111 -0.0013 0.0157 -0.0177 469 ASP A OD1 2991 O OD2 . ASP A 387 ? 0.6258 0.5716 0.6448 -0.0001 0.0171 -0.0198 469 ASP A OD2 2992 N N . SER B 1 ? 0.5033 0.4675 0.4973 0.0088 0.0080 0.0069 82 SER B N 2993 C CA . SER B 1 ? 0.4194 0.3849 0.4134 0.0074 0.0070 0.0055 82 SER B CA 2994 C C . SER B 1 ? 0.3467 0.3101 0.3404 0.0065 0.0080 0.0042 82 SER B C 2995 O O . SER B 1 ? 0.3636 0.3244 0.3569 0.0058 0.0090 0.0038 82 SER B O 2996 C CB . SER B 1 ? 0.3058 0.2725 0.2999 0.0061 0.0059 0.0052 82 SER B CB 2997 O OG . SER B 1 ? 0.4133 0.3824 0.4077 0.0068 0.0049 0.0061 82 SER B OG 2998 N N . VAL B 2 ? 0.2986 0.2629 0.2922 0.0065 0.0077 0.0035 83 VAL B N 2999 C CA . VAL B 2 ? 0.2323 0.1950 0.2256 0.0056 0.0086 0.0021 83 VAL B CA 3000 C C . VAL B 2 ? 0.2584 0.2233 0.2516 0.0045 0.0074 0.0011 83 VAL B C 3001 O O . VAL B 2 ? 0.2203 0.1877 0.2138 0.0049 0.0064 0.0016 83 VAL B O 3002 C CB . VAL B 2 ? 0.2754 0.2368 0.2687 0.0070 0.0098 0.0023 83 VAL B CB 3003 C CG1 . VAL B 2 ? 0.3013 0.2609 0.2941 0.0060 0.0108 0.0007 83 VAL B CG1 3004 C CG2 . VAL B 2 ? 0.3658 0.3252 0.3593 0.0084 0.0110 0.0036 83 VAL B CG2 3005 N N . LYS B 3 ? 0.2515 0.2157 0.2442 0.0030 0.0077 -0.0003 84 LYS B N 3006 C CA . LYS B 3 ? 0.1897 0.1561 0.1822 0.0020 0.0067 -0.0011 84 LYS B CA 3007 C C . LYS B 3 ? 0.2126 0.1799 0.2052 0.0026 0.0068 -0.0013 84 LYS B C 3008 O O . LYS B 3 ? 0.1971 0.1628 0.1896 0.0034 0.0080 -0.0014 84 LYS B O 3009 C CB . LYS B 3 ? 0.2421 0.2080 0.2342 0.0002 0.0069 -0.0025 84 LYS B CB 3010 C CG . LYS B 3 ? 0.2909 0.2539 0.2826 -0.0001 0.0086 -0.0035 84 LYS B CG 3011 C CD . LYS B 3 ? 0.4130 0.3755 0.4043 -0.0020 0.0087 -0.0048 84 LYS B CD 3012 C CE . LYS B 3 ? 0.5550 0.5142 0.5461 -0.0024 0.0105 -0.0056 84 LYS B CE 3013 N NZ . LYS B 3 ? 0.5429 0.5019 0.5336 -0.0044 0.0107 -0.0070 84 LYS B NZ 3014 N N . LEU B 4 ? 0.1203 0.0900 0.1129 0.0023 0.0056 -0.0013 85 LEU B N 3015 C CA . LEU B 4 ? 0.1676 0.1385 0.1602 0.0027 0.0057 -0.0015 85 LEU B CA 3016 C C . LEU B 4 ? 0.1498 0.1197 0.1417 0.0019 0.0066 -0.0030 85 LEU B C 3017 O O . LEU B 4 ? 0.1951 0.1651 0.1865 0.0005 0.0064 -0.0039 85 LEU B O 3018 C CB . LEU B 4 ? 0.1172 0.0909 0.1100 0.0023 0.0043 -0.0011 85 LEU B CB 3019 C CG . LEU B 4 ? 0.1308 0.1056 0.1242 0.0030 0.0033 0.0001 85 LEU B CG 3020 C CD1 . LEU B 4 ? 0.1505 0.1277 0.1440 0.0024 0.0021 0.0002 85 LEU B CD1 3021 C CD2 . LEU B 4 ? 0.1386 0.1136 0.1325 0.0045 0.0038 0.0009 85 LEU B CD2 3022 N N . ALA B 5 ? 0.1290 0.0982 0.1209 0.0027 0.0076 -0.0032 86 ALA B N 3023 C CA . ALA B 5 ? 0.1783 0.1465 0.1696 0.0020 0.0086 -0.0047 86 ALA B CA 3024 C C . ALA B 5 ? 0.1527 0.1234 0.1435 0.0009 0.0077 -0.0054 86 ALA B C 3025 O O . ALA B 5 ? 0.1622 0.1329 0.1523 -0.0005 0.0078 -0.0066 86 ALA B O 3026 C CB . ALA B 5 ? 0.1795 0.1464 0.1709 0.0034 0.0099 -0.0047 86 ALA B CB 3027 N N . GLY B 6 ? 0.1554 0.1283 0.1465 0.0016 0.0069 -0.0046 87 GLY B N 3028 C CA . GLY B 6 ? 0.1655 0.1407 0.1562 0.0007 0.0062 -0.0050 87 GLY B CA 3029 C C . GLY B 6 ? 0.1470 0.1222 0.1370 0.0003 0.0071 -0.0063 87 GLY B C 3030 O O . GLY B 6 ? 0.1453 0.1223 0.1347 -0.0008 0.0066 -0.0070 87 GLY B O 3031 N N . ASN B 7 ? 0.1387 0.1120 0.1288 0.0012 0.0085 -0.0068 88 ASN B N 3032 C CA . ASN B 7 ? 0.1226 0.0955 0.1121 0.0007 0.0096 -0.0083 88 ASN B CA 3033 C C . ASN B 7 ? 0.1417 0.1158 0.1313 0.0018 0.0099 -0.0081 88 ASN B C 3034 O O . ASN B 7 ? 0.1820 0.1561 0.1711 0.0014 0.0108 -0.0094 88 ASN B O 3035 C CB . ASN B 7 ? 0.1562 0.1258 0.1455 0.0006 0.0111 -0.0094 88 ASN B CB 3036 C CG . ASN B 7 ? 0.2930 0.2604 0.2830 0.0024 0.0120 -0.0084 88 ASN B CG 3037 O OD1 . ASN B 7 ? 0.1894 0.1580 0.1801 0.0037 0.0113 -0.0069 88 ASN B OD1 3038 N ND2 . ASN B 7 ? 0.3498 0.3141 0.3397 0.0026 0.0136 -0.0092 88 ASN B ND2 3039 N N . SER B 8 ? 0.1708 0.1461 0.1612 0.0029 0.0093 -0.0066 89 SER B N 3040 C CA . SER B 8 ? 0.1568 0.1337 0.1475 0.0039 0.0095 -0.0064 89 SER B CA 3041 C C . SER B 8 ? 0.1713 0.1511 0.1617 0.0030 0.0084 -0.0063 89 SER B C 3042 O O . SER B 8 ? 0.1556 0.1363 0.1456 0.0019 0.0074 -0.0061 89 SER B O 3043 C CB . SER B 8 ? 0.1377 0.1148 0.1295 0.0056 0.0094 -0.0049 89 SER B CB 3044 O OG . SER B 8 ? 0.2106 0.1891 0.2028 0.0053 0.0080 -0.0038 89 SER B OG 3045 N N . SER B 9 ? 0.1314 0.1129 0.1219 0.0035 0.0087 -0.0063 90 SER B N 3046 C CA . SER B 9 ? 0.1414 0.1257 0.1316 0.0027 0.0079 -0.0061 90 SER B CA 3047 C C . SER B 9 ? 0.1544 0.1403 0.1454 0.0031 0.0068 -0.0046 90 SER B C 3048 O O . SER B 9 ? 0.1304 0.1157 0.1222 0.0042 0.0068 -0.0038 90 SER B O 3049 C CB . SER B 9 ? 0.2318 0.2171 0.2216 0.0029 0.0088 -0.0069 90 SER B CB 3050 O OG . SER B 9 ? 0.3519 0.3356 0.3409 0.0025 0.0100 -0.0085 90 SER B OG 3051 N N . LEU B 10 ? 0.1668 0.1547 0.1575 0.0022 0.0060 -0.0042 91 LEU B N 3052 C CA . LEU B 10 ? 0.2237 0.2133 0.2152 0.0024 0.0051 -0.0029 91 LEU B CA 3053 C C . LEU B 10 ? 0.2135 0.2043 0.2057 0.0035 0.0057 -0.0027 91 LEU B C 3054 O O . LEU B 10 ? 0.2341 0.2255 0.2260 0.0036 0.0065 -0.0034 91 LEU B O 3055 C CB . LEU B 10 ? 0.2222 0.2136 0.2132 0.0013 0.0043 -0.0026 91 LEU B CB 3056 C CG . LEU B 10 ? 0.2703 0.2614 0.2610 0.0004 0.0033 -0.0021 91 LEU B CG 3057 C CD1 . LEU B 10 ? 0.1863 0.1794 0.1767 -0.0004 0.0027 -0.0015 91 LEU B CD1 3058 C CD2 . LEU B 10 ? 0.2087 0.1990 0.2004 0.0010 0.0027 -0.0012 91 LEU B CD2 3059 N N . CYS B 11 ? 0.1783 0.1696 0.1715 0.0042 0.0053 -0.0017 92 CYS B N 3060 C CA . CYS B 11 ? 0.2226 0.2157 0.2167 0.0052 0.0057 -0.0014 92 CYS B CA 3061 C C . CYS B 11 ? 0.2243 0.2198 0.2182 0.0044 0.0054 -0.0013 92 CYS B C 3062 O O . CYS B 11 ? 0.1922 0.1883 0.1861 0.0034 0.0045 -0.0007 92 CYS B O 3063 C CB . CYS B 11 ? 0.2146 0.2083 0.2098 0.0060 0.0051 -0.0004 92 CYS B CB 3064 S SG . CYS B 11 ? 0.3474 0.3385 0.3428 0.0069 0.0053 -0.0002 92 CYS B SG 3065 N N . PRO B 12 ? 0.2748 0.2714 0.2686 0.0047 0.0062 -0.0018 93 PRO B N 3066 C CA . PRO B 12 ? 0.2837 0.2827 0.2775 0.0040 0.0061 -0.0016 93 PRO B CA 3067 C C . PRO B 12 ? 0.2439 0.2447 0.2390 0.0042 0.0055 -0.0006 93 PRO B C 3068 O O . PRO B 12 ? 0.2315 0.2325 0.2275 0.0054 0.0057 -0.0004 93 PRO B O 3069 C CB . PRO B 12 ? 0.3598 0.3596 0.3535 0.0047 0.0072 -0.0024 93 PRO B CB 3070 C CG . PRO B 12 ? 0.4145 0.4118 0.4077 0.0053 0.0080 -0.0033 93 PRO B CG 3071 C CD . PRO B 12 ? 0.3243 0.3199 0.3180 0.0057 0.0074 -0.0027 93 PRO B CD 3072 N N . VAL B 13 ? 0.1611 0.1632 0.1562 0.0031 0.0049 0.0000 94 VAL B N 3073 C CA . VAL B 13 ? 0.1417 0.1455 0.1379 0.0031 0.0044 0.0007 94 VAL B CA 3074 C C . VAL B 13 ? 0.1458 0.1519 0.1421 0.0022 0.0045 0.0010 94 VAL B C 3075 O O . VAL B 13 ? 0.1396 0.1457 0.1350 0.0013 0.0046 0.0009 94 VAL B O 3076 C CB . VAL B 13 ? 0.1583 0.1609 0.1547 0.0025 0.0035 0.0013 94 VAL B CB 3077 C CG1 . VAL B 13 ? 0.1624 0.1628 0.1586 0.0033 0.0034 0.0011 94 VAL B CG1 3078 C CG2 . VAL B 13 ? 0.1557 0.1577 0.1512 0.0012 0.0030 0.0015 94 VAL B CG2 3079 N N . SER B 14 ? 0.1374 0.1457 0.1349 0.0024 0.0045 0.0013 95 SER B N 3080 C CA . SER B 14 ? 0.1291 0.1396 0.1268 0.0015 0.0047 0.0015 95 SER B CA 3081 C C . SER B 14 ? 0.1460 0.1569 0.1443 0.0003 0.0041 0.0022 95 SER B C 3082 O O . SER B 14 ? 0.1224 0.1347 0.1208 -0.0007 0.0042 0.0025 95 SER B O 3083 C CB . SER B 14 ? 0.1451 0.1582 0.1438 0.0024 0.0054 0.0013 95 SER B CB 3084 O OG . SER B 14 ? 0.2228 0.2367 0.2227 0.0031 0.0051 0.0015 95 SER B OG 3085 N N . GLY B 15 ? 0.1028 0.1124 0.1015 0.0004 0.0034 0.0024 96 GLY B N 3086 C CA . GLY B 15 ? 0.0782 0.0879 0.0774 -0.0006 0.0029 0.0029 96 GLY B CA 3087 C C . GLY B 15 ? 0.1003 0.1083 0.0997 -0.0004 0.0022 0.0030 96 GLY B C 3088 O O . GLY B 15 ? 0.0924 0.0990 0.0915 0.0007 0.0022 0.0027 96 GLY B O 3089 N N . TRP B 16 ? 0.0938 0.1016 0.0936 -0.0013 0.0018 0.0033 97 TRP B N 3090 C CA . TRP B 16 ? 0.0701 0.0762 0.0700 -0.0012 0.0011 0.0034 97 TRP B CA 3091 C C . TRP B 16 ? 0.0830 0.0906 0.0842 -0.0014 0.0009 0.0033 97 TRP B C 3092 O O . TRP B 16 ? 0.0809 0.0898 0.0827 -0.0025 0.0010 0.0033 97 TRP B O 3093 C CB . TRP B 16 ? 0.0837 0.0877 0.0828 -0.0022 0.0008 0.0038 97 TRP B CB 3094 C CG . TRP B 16 ? 0.0730 0.0762 0.0711 -0.0021 0.0011 0.0038 97 TRP B CG 3095 C CD1 . TRP B 16 ? 0.0693 0.0733 0.0668 -0.0026 0.0015 0.0040 97 TRP B CD1 3096 C CD2 . TRP B 16 ? 0.0628 0.0643 0.0600 -0.0014 0.0010 0.0036 97 TRP B CD2 3097 N NE1 . TRP B 16 ? 0.0856 0.0888 0.0820 -0.0024 0.0016 0.0039 97 TRP B NE1 3098 C CE2 . TRP B 16 ? 0.0959 0.0975 0.0920 -0.0017 0.0013 0.0036 97 TRP B CE2 3099 C CE3 . TRP B 16 ? 0.0760 0.0759 0.0730 -0.0008 0.0006 0.0034 97 TRP B CE3 3100 C CZ2 . TRP B 16 ? 0.0866 0.0869 0.0817 -0.0014 0.0013 0.0033 97 TRP B CZ2 3101 C CZ3 . TRP B 16 ? 0.0817 0.0802 0.0778 -0.0005 0.0006 0.0031 97 TRP B CZ3 3102 C CH2 . TRP B 16 ? 0.0913 0.0901 0.0865 -0.0008 0.0010 0.0030 97 TRP B CH2 3103 N N . ALA B 17 ? 0.0676 0.0750 0.0690 -0.0005 0.0006 0.0031 98 ALA B N 3104 C CA . ALA B 17 ? 0.0614 0.0705 0.0639 -0.0005 0.0003 0.0030 98 ALA B CA 3105 C C . ALA B 17 ? 0.0762 0.0834 0.0786 -0.0011 -0.0003 0.0030 98 ALA B C 3106 O O . ALA B 17 ? 0.0678 0.0728 0.0695 -0.0006 -0.0005 0.0032 98 ALA B O 3107 C CB . ALA B 17 ? 0.0842 0.0949 0.0871 0.0010 0.0003 0.0029 98 ALA B CB 3108 N N . ILE B 18 ? 0.0918 0.1000 0.0949 -0.0021 -0.0005 0.0028 99 ILE B N 3109 C CA . ILE B 18 ? 0.0853 0.0918 0.0884 -0.0027 -0.0009 0.0028 99 ILE B CA 3110 C C . ILE B 18 ? 0.0861 0.0924 0.0892 -0.0016 -0.0013 0.0027 99 ILE B C 3111 O O . ILE B 18 ? 0.0769 0.0855 0.0806 -0.0008 -0.0014 0.0026 99 ILE B O 3112 C CB . ILE B 18 ? 0.1127 0.1202 0.1167 -0.0042 -0.0009 0.0024 99 ILE B CB 3113 C CG1 . ILE B 18 ? 0.1031 0.1081 0.1069 -0.0048 -0.0012 0.0024 99 ILE B CG1 3114 C CG2 . ILE B 18 ? 0.0880 0.0987 0.0929 -0.0041 -0.0010 0.0019 99 ILE B CG2 3115 C CD1 . ILE B 18 ? 0.0986 0.1034 0.1030 -0.0064 -0.0009 0.0021 99 ILE B CD1 3116 N N . TYR B 19 ? 0.0636 0.0674 0.0661 -0.0014 -0.0016 0.0029 100 TYR B N 3117 C CA . TYR B 19 ? 0.0623 0.0655 0.0646 -0.0004 -0.0020 0.0029 100 TYR B CA 3118 C C . TYR B 19 ? 0.0863 0.0891 0.0889 -0.0009 -0.0024 0.0027 100 TYR B C 3119 O O . TYR B 19 ? 0.0836 0.0876 0.0865 -0.0003 -0.0026 0.0026 100 TYR B O 3120 C CB . TYR B 19 ? 0.0901 0.0909 0.0914 0.0002 -0.0019 0.0032 100 TYR B CB 3121 C CG . TYR B 19 ? 0.1200 0.1200 0.1210 0.0014 -0.0020 0.0033 100 TYR B CG 3122 C CD1 . TYR B 19 ? 0.1661 0.1678 0.1675 0.0025 -0.0019 0.0034 100 TYR B CD1 3123 C CD2 . TYR B 19 ? 0.1723 0.1700 0.1727 0.0014 -0.0023 0.0034 100 TYR B CD2 3124 C CE1 . TYR B 19 ? 0.1656 0.1664 0.1667 0.0036 -0.0019 0.0037 100 TYR B CE1 3125 C CE2 . TYR B 19 ? 0.1954 0.1923 0.1955 0.0023 -0.0023 0.0036 100 TYR B CE2 3126 C CZ . TYR B 19 ? 0.1674 0.1657 0.1679 0.0034 -0.0021 0.0037 100 TYR B CZ 3127 O OH . TYR B 19 ? 0.2743 0.2717 0.2745 0.0044 -0.0020 0.0040 100 TYR B OH 3128 N N . SER B 20 ? 0.0860 0.0871 0.0885 -0.0020 -0.0025 0.0026 101 SER B N 3129 C CA . SER B 20 ? 0.0879 0.0884 0.0907 -0.0025 -0.0028 0.0023 101 SER B CA 3130 C C . SER B 20 ? 0.0913 0.0909 0.0944 -0.0039 -0.0026 0.0021 101 SER B C 3131 O O . SER B 20 ? 0.0967 0.0953 0.0995 -0.0043 -0.0023 0.0025 101 SER B O 3132 C CB . SER B 20 ? 0.1242 0.1227 0.1264 -0.0018 -0.0031 0.0025 101 SER B CB 3133 O OG . SER B 20 ? 0.1279 0.1241 0.1295 -0.0021 -0.0030 0.0029 101 SER B OG 3134 N N . LYS B 21 ? 0.0643 0.0641 0.0680 -0.0046 -0.0027 0.0016 102 LYS B N 3135 C CA . LYS B 21 ? 0.0979 0.0961 0.1019 -0.0058 -0.0024 0.0014 102 LYS B CA 3136 C C . LYS B 21 ? 0.1099 0.1078 0.1142 -0.0060 -0.0026 0.0008 102 LYS B C 3137 O O . LYS B 21 ? 0.1228 0.1228 0.1275 -0.0059 -0.0028 0.0001 102 LYS B O 3138 C CB . LYS B 21 ? 0.0776 0.0775 0.0823 -0.0070 -0.0019 0.0010 102 LYS B CB 3139 C CG . LYS B 21 ? 0.1030 0.1008 0.1080 -0.0083 -0.0014 0.0009 102 LYS B CG 3140 C CD . LYS B 21 ? 0.1027 0.1021 0.1084 -0.0096 -0.0008 0.0004 102 LYS B CD 3141 C CE . LYS B 21 ? 0.1125 0.1095 0.1183 -0.0107 -0.0001 0.0008 102 LYS B CE 3142 N NZ . LYS B 21 ? 0.1751 0.1696 0.1811 -0.0110 0.0000 0.0005 102 LYS B NZ 3143 N N . ASP B 22 ? 0.1039 0.0991 0.1079 -0.0061 -0.0026 0.0010 103 ASP B N 3144 C CA . ASP B 22 ? 0.1503 0.1450 0.1546 -0.0061 -0.0028 0.0004 103 ASP B CA 3145 C C . ASP B 22 ? 0.1458 0.1400 0.1508 -0.0074 -0.0024 -0.0004 103 ASP B C 3146 O O . ASP B 22 ? 0.1315 0.1260 0.1368 -0.0076 -0.0025 -0.0012 103 ASP B O 3147 C CB . ASP B 22 ? 0.1118 0.1043 0.1154 -0.0052 -0.0031 0.0010 103 ASP B CB 3148 C CG . ASP B 22 ? 0.1838 0.1741 0.1871 -0.0053 -0.0029 0.0018 103 ASP B CG 3149 O OD1 . ASP B 22 ? 0.1930 0.1828 0.1967 -0.0062 -0.0023 0.0018 103 ASP B OD1 3150 O OD2 . ASP B 22 ? 0.1888 0.1779 0.1915 -0.0046 -0.0031 0.0024 103 ASP B OD2 3151 N N . ASN B 23 ? 0.0816 0.0749 0.0869 -0.0084 -0.0018 -0.0003 104 ASN B N 3152 C CA . ASN B 23 ? 0.1201 0.1125 0.1261 -0.0097 -0.0011 -0.0010 104 ASN B CA 3153 C C . ASN B 23 ? 0.1042 0.0942 0.1102 -0.0095 -0.0011 -0.0012 104 ASN B C 3154 O O . ASN B 23 ? 0.0857 0.0755 0.0923 -0.0104 -0.0007 -0.0023 104 ASN B O 3155 C CB . ASN B 23 ? 0.1078 0.1031 0.1146 -0.0107 -0.0011 -0.0024 104 ASN B CB 3156 C CG . ASN B 23 ? 0.1186 0.1162 0.1256 -0.0111 -0.0009 -0.0023 104 ASN B CG 3157 O OD1 . ASN B 23 ? 0.1257 0.1222 0.1328 -0.0117 -0.0004 -0.0018 104 ASN B OD1 3158 N ND2 . ASN B 23 ? 0.1584 0.1595 0.1657 -0.0109 -0.0013 -0.0028 104 ASN B ND2 3159 N N . SER B 24 ? 0.0644 0.0527 0.0698 -0.0084 -0.0014 -0.0002 105 SER B N 3160 C CA . SER B 24 ? 0.0973 0.0838 0.1027 -0.0080 -0.0015 -0.0003 105 SER B CA 3161 C C . SER B 24 ? 0.0960 0.0802 0.1019 -0.0089 -0.0007 -0.0007 105 SER B C 3162 O O . SER B 24 ? 0.0996 0.0833 0.1059 -0.0091 -0.0006 -0.0016 105 SER B O 3163 C CB . SER B 24 ? 0.1153 0.1004 0.1198 -0.0067 -0.0019 0.0009 105 SER B CB 3164 O OG . SER B 24 ? 0.2012 0.1881 0.2052 -0.0059 -0.0025 0.0011 105 SER B OG 3165 N N . VAL B 25 ? 0.0861 0.0687 0.0921 -0.0093 -0.0001 0.0000 106 VAL B N 3166 C CA . VAL B 25 ? 0.0937 0.0737 0.1003 -0.0100 0.0009 -0.0001 106 VAL B CA 3167 C C . VAL B 25 ? 0.0857 0.0665 0.0932 -0.0116 0.0015 -0.0017 106 VAL B C 3168 O O . VAL B 25 ? 0.1121 0.0912 0.1200 -0.0121 0.0020 -0.0025 106 VAL B O 3169 C CB . VAL B 25 ? 0.0977 0.0759 0.1040 -0.0101 0.0015 0.0013 106 VAL B CB 3170 C CG1 . VAL B 25 ? 0.1015 0.0767 0.1085 -0.0107 0.0025 0.0013 106 VAL B CG1 3171 C CG2 . VAL B 25 ? 0.1591 0.1369 0.1645 -0.0087 0.0008 0.0028 106 VAL B CG2 3172 N N . ARG B 26 ? 0.0809 0.0643 0.0885 -0.0124 0.0014 -0.0023 107 ARG B N 3173 C CA . ARG B 26 ? 0.0686 0.0533 0.0770 -0.0140 0.0019 -0.0039 107 ARG B CA 3174 C C . ARG B 26 ? 0.1050 0.0909 0.1136 -0.0138 0.0015 -0.0052 107 ARG B C 3175 O O . ARG B 26 ? 0.1170 0.1021 0.1262 -0.0149 0.0021 -0.0065 107 ARG B O 3176 C CB . ARG B 26 ? 0.0815 0.0695 0.0900 -0.0146 0.0017 -0.0042 107 ARG B CB 3177 C CG . ARG B 26 ? 0.1062 0.0933 0.1148 -0.0153 0.0023 -0.0034 107 ARG B CG 3178 C CD . ARG B 26 ? 0.0828 0.0734 0.0914 -0.0155 0.0020 -0.0034 107 ARG B CD 3179 N NE . ARG B 26 ? 0.1167 0.1105 0.1261 -0.0166 0.0019 -0.0051 107 ARG B NE 3180 C CZ . ARG B 26 ? 0.1594 0.1539 0.1696 -0.0184 0.0028 -0.0061 107 ARG B CZ 3181 N NH1 . ARG B 26 ? 0.1594 0.1514 0.1698 -0.0193 0.0038 -0.0056 107 ARG B NH1 3182 N NH2 . ARG B 26 ? 0.1313 0.1292 0.1422 -0.0193 0.0026 -0.0077 107 ARG B NH2 3183 N N . ILE B 27 ? 0.0861 0.0737 0.0941 -0.0125 0.0005 -0.0048 108 ILE B N 3184 C CA . ILE B 27 ? 0.0778 0.0669 0.0858 -0.0123 0.0000 -0.0059 108 ILE B CA 3185 C C . ILE B 27 ? 0.0952 0.0814 0.1032 -0.0118 0.0003 -0.0059 108 ILE B C 3186 O O . ILE B 27 ? 0.1153 0.1017 0.1236 -0.0123 0.0005 -0.0072 108 ILE B O 3187 C CB . ILE B 27 ? 0.0870 0.0785 0.0943 -0.0109 -0.0010 -0.0053 108 ILE B CB 3188 C CG1 . ILE B 27 ? 0.1223 0.1172 0.1299 -0.0114 -0.0012 -0.0055 108 ILE B CG1 3189 C CG2 . ILE B 27 ? 0.0896 0.0822 0.0969 -0.0105 -0.0015 -0.0060 108 ILE B CG2 3190 C CD1 . ILE B 27 ? 0.1847 0.1814 0.1916 -0.0100 -0.0020 -0.0045 108 ILE B CD1 3191 N N . GLY B 28 ? 0.0895 0.0730 0.0971 -0.0109 0.0003 -0.0045 109 GLY B N 3192 C CA . GLY B 28 ? 0.1079 0.0889 0.1156 -0.0103 0.0006 -0.0043 109 GLY B CA 3193 C C . GLY B 28 ? 0.1254 0.1041 0.1339 -0.0114 0.0017 -0.0052 109 GLY B C 3194 O O . GLY B 28 ? 0.1227 0.0993 0.1313 -0.0109 0.0021 -0.0054 109 GLY B O 3195 N N . SER B 29 ? 0.1285 0.1074 0.1375 -0.0128 0.0024 -0.0059 110 SER B N 3196 C CA . SER B 29 ? 0.1387 0.1154 0.1485 -0.0142 0.0037 -0.0070 110 SER B CA 3197 C C . SER B 29 ? 0.1745 0.1520 0.1846 -0.0146 0.0037 -0.0088 110 SER B C 3198 O O . SER B 29 ? 0.1990 0.1739 0.2096 -0.0149 0.0046 -0.0095 110 SER B O 3199 C CB . SER B 29 ? 0.1847 0.1623 0.1950 -0.0159 0.0043 -0.0077 110 SER B CB 3200 O OG . SER B 29 ? 0.2027 0.1779 0.2138 -0.0173 0.0057 -0.0088 110 SER B OG 3201 N N . LYS B 30 ? 0.1629 0.1440 0.1728 -0.0145 0.0028 -0.0096 111 LYS B N 3202 C CA . LYS B 30 ? 0.1713 0.1537 0.1813 -0.0148 0.0027 -0.0112 111 LYS B CA 3203 C C . LYS B 30 ? 0.1756 0.1595 0.1849 -0.0132 0.0016 -0.0106 111 LYS B C 3204 O O . LYS B 30 ? 0.1911 0.1743 0.2004 -0.0127 0.0017 -0.0111 111 LYS B O 3205 C CB . LYS B 30 ? 0.1854 0.1713 0.1958 -0.0164 0.0028 -0.0130 111 LYS B CB 3206 C CG . LYS B 30 ? 0.1878 0.1758 0.1981 -0.0166 0.0025 -0.0146 111 LYS B CG 3207 C CD . LYS B 30 ? 0.2168 0.2089 0.2276 -0.0181 0.0024 -0.0164 111 LYS B CD 3208 C CE . LYS B 30 ? 0.2200 0.2145 0.2306 -0.0181 0.0021 -0.0178 111 LYS B CE 3209 N NZ . LYS B 30 ? 0.3306 0.3294 0.3414 -0.0196 0.0020 -0.0196 111 LYS B NZ 3210 N N . GLY B 31 ? 0.1549 0.1408 0.1636 -0.0123 0.0007 -0.0094 112 GLY B N 3211 C CA . GLY B 31 ? 0.1458 0.1331 0.1538 -0.0109 -0.0003 -0.0087 112 GLY B CA 3212 C C . GLY B 31 ? 0.1474 0.1321 0.1551 -0.0096 -0.0004 -0.0075 112 GLY B C 3213 O O . GLY B 31 ? 0.1770 0.1588 0.1850 -0.0095 0.0002 -0.0069 112 GLY B O 3214 N N . ASP B 32 ? 0.1329 0.1187 0.1401 -0.0085 -0.0011 -0.0071 113 ASP B N 3215 C CA . ASP B 32 ? 0.1221 0.1059 0.1290 -0.0072 -0.0013 -0.0060 113 ASP B CA 3216 C C . ASP B 32 ? 0.0957 0.0796 0.1020 -0.0064 -0.0019 -0.0044 113 ASP B C 3217 O O . ASP B 32 ? 0.1194 0.1049 0.1251 -0.0057 -0.0026 -0.0040 113 ASP B O 3218 C CB . ASP B 32 ? 0.1339 0.1187 0.1405 -0.0066 -0.0017 -0.0065 113 ASP B CB 3219 C CG . ASP B 32 ? 0.1481 0.1327 0.1553 -0.0074 -0.0011 -0.0082 113 ASP B CG 3220 O OD1 . ASP B 32 ? 0.1450 0.1275 0.1529 -0.0082 -0.0002 -0.0087 113 ASP B OD1 3221 O OD2 . ASP B 32 ? 0.1893 0.1758 0.1963 -0.0073 -0.0014 -0.0089 113 ASP B OD2 3222 N N . VAL B 33 ? 0.0910 0.0729 0.0973 -0.0064 -0.0015 -0.0035 114 VAL B N 3223 C CA . VAL B 33 ? 0.0790 0.0611 0.0848 -0.0058 -0.0019 -0.0022 114 VAL B CA 3224 C C . VAL B 33 ? 0.0791 0.0589 0.0847 -0.0050 -0.0018 -0.0009 114 VAL B C 3225 O O . VAL B 33 ? 0.0743 0.0520 0.0804 -0.0052 -0.0011 -0.0009 114 VAL B O 3226 C CB . VAL B 33 ? 0.1095 0.0921 0.1155 -0.0067 -0.0016 -0.0021 114 VAL B CB 3227 C CG1 . VAL B 33 ? 0.0987 0.0814 0.1040 -0.0061 -0.0020 -0.0008 114 VAL B CG1 3228 C CG2 . VAL B 33 ? 0.1046 0.0900 0.1108 -0.0075 -0.0018 -0.0033 114 VAL B CG2 3229 N N . PHE B 34 ? 0.0770 0.0573 0.0820 -0.0040 -0.0025 0.0000 115 PHE B N 3230 C CA . PHE B 34 ? 0.0684 0.0472 0.0732 -0.0032 -0.0025 0.0012 115 PHE B CA 3231 C C . PHE B 34 ? 0.0933 0.0707 0.0981 -0.0035 -0.0020 0.0021 115 PHE B C 3232 O O . PHE B 34 ? 0.0612 0.0394 0.0659 -0.0041 -0.0020 0.0021 115 PHE B O 3233 C CB . PHE B 34 ? 0.0932 0.0731 0.0973 -0.0024 -0.0032 0.0019 115 PHE B CB 3234 C CG . PHE B 34 ? 0.1089 0.0895 0.1128 -0.0019 -0.0036 0.0014 115 PHE B CG 3235 C CD1 . PHE B 34 ? 0.1141 0.0938 0.1185 -0.0015 -0.0035 0.0014 115 PHE B CD1 3236 C CD2 . PHE B 34 ? 0.0880 0.0704 0.0916 -0.0018 -0.0041 0.0012 115 PHE B CD2 3237 C CE1 . PHE B 34 ? 0.1577 0.1382 0.1620 -0.0011 -0.0038 0.0010 115 PHE B CE1 3238 C CE2 . PHE B 34 ? 0.0987 0.0817 0.1021 -0.0014 -0.0044 0.0009 115 PHE B CE2 3239 C CZ . PHE B 34 ? 0.1152 0.0973 0.1189 -0.0011 -0.0043 0.0008 115 PHE B CZ 3240 N N . VAL B 35 ? 0.1089 0.0845 0.1140 -0.0030 -0.0016 0.0028 116 VAL B N 3241 C CA . VAL B 35 ? 0.1132 0.0877 0.1180 -0.0028 -0.0013 0.0041 116 VAL B CA 3242 C C . VAL B 35 ? 0.1226 0.0985 0.1266 -0.0022 -0.0021 0.0050 116 VAL B C 3243 O O . VAL B 35 ? 0.1008 0.0772 0.1047 -0.0014 -0.0026 0.0052 116 VAL B O 3244 C CB . VAL B 35 ? 0.1495 0.1218 0.1548 -0.0022 -0.0007 0.0049 116 VAL B CB 3245 C CG1 . VAL B 35 ? 0.1677 0.1392 0.1727 -0.0020 -0.0005 0.0065 116 VAL B CG1 3246 C CG2 . VAL B 35 ? 0.1827 0.1534 0.1889 -0.0030 0.0002 0.0038 116 VAL B CG2 3247 N N . ILE B 36 ? 0.1111 0.0878 0.1146 -0.0025 -0.0022 0.0054 117 ILE B N 3248 C CA . ILE B 36 ? 0.1171 0.0952 0.1198 -0.0020 -0.0028 0.0060 117 ILE B CA 3249 C C . ILE B 36 ? 0.1624 0.1403 0.1646 -0.0021 -0.0027 0.0071 117 ILE B C 3250 O O . ILE B 36 ? 0.1478 0.1249 0.1503 -0.0026 -0.0020 0.0074 117 ILE B O 3251 C CB . ILE B 36 ? 0.1158 0.0956 0.1182 -0.0023 -0.0033 0.0052 117 ILE B CB 3252 C CG1 . ILE B 36 ? 0.1509 0.1312 0.1533 -0.0031 -0.0030 0.0050 117 ILE B CG1 3253 C CG2 . ILE B 36 ? 0.1077 0.0878 0.1105 -0.0023 -0.0034 0.0041 117 ILE B CG2 3254 C CD1 . ILE B 36 ? 0.2755 0.2576 0.2775 -0.0030 -0.0034 0.0046 117 ILE B CD1 3255 N N . ARG B 37 ? 0.1138 0.0928 0.1153 -0.0015 -0.0032 0.0078 118 ARG B N 3256 C CA . ARG B 37 ? 0.1211 0.1006 0.1219 -0.0016 -0.0031 0.0086 118 ARG B CA 3257 C C . ARG B 37 ? 0.1755 0.1566 0.1755 -0.0013 -0.0037 0.0085 118 ARG B C 3258 O O . ARG B 37 ? 0.1718 0.1534 0.1718 -0.0010 -0.0041 0.0079 118 ARG B O 3259 C CB . ARG B 37 ? 0.1506 0.1291 0.1513 -0.0012 -0.0028 0.0100 118 ARG B CB 3260 C CG . ARG B 37 ? 0.1519 0.1288 0.1532 -0.0017 -0.0019 0.0104 118 ARG B CG 3261 C CD . ARG B 37 ? 0.2011 0.1779 0.2018 -0.0014 -0.0016 0.0120 118 ARG B CD 3262 N NE . ARG B 37 ? 0.1520 0.1306 0.1518 -0.0017 -0.0020 0.0121 118 ARG B NE 3263 C CZ . ARG B 37 ? 0.1684 0.1478 0.1675 -0.0013 -0.0021 0.0133 118 ARG B CZ 3264 N NH1 . ARG B 37 ? 0.2402 0.2189 0.2393 -0.0006 -0.0018 0.0147 118 ARG B NH1 3265 N NH2 . ARG B 37 ? 0.1433 0.1245 0.1416 -0.0016 -0.0023 0.0132 118 ARG B NH2 3266 N N . GLU B 38 ? 0.1889 0.1709 0.1883 -0.0015 -0.0037 0.0090 119 GLU B N 3267 C CA . GLU B 38 ? 0.2262 0.2096 0.2248 -0.0014 -0.0041 0.0087 119 GLU B CA 3268 C C . GLU B 38 ? 0.1937 0.1775 0.1923 -0.0015 -0.0043 0.0076 119 GLU B C 3269 O O . GLU B 38 ? 0.2339 0.2182 0.2324 -0.0012 -0.0047 0.0072 119 GLU B O 3270 C CB . GLU B 38 ? 0.1958 0.1796 0.1940 -0.0008 -0.0046 0.0092 119 GLU B CB 3271 C CG . GLU B 38 ? 0.2730 0.2569 0.2709 -0.0005 -0.0045 0.0105 119 GLU B CG 3272 C CD . GLU B 38 ? 0.3210 0.3035 0.3197 -0.0001 -0.0042 0.0112 119 GLU B CD 3273 O OE1 . GLU B 38 ? 0.2931 0.2751 0.2917 0.0001 -0.0038 0.0124 119 GLU B OE1 3274 O OE2 . GLU B 38 ? 0.2856 0.2673 0.2849 0.0001 -0.0042 0.0106 119 GLU B OE2 3275 N N . PRO B 39 ? 0.1826 0.1664 0.1816 -0.0019 -0.0040 0.0071 120 PRO B N 3276 C CA . PRO B 39 ? 0.1574 0.1420 0.1565 -0.0019 -0.0042 0.0062 120 PRO B CA 3277 C C . PRO B 39 ? 0.2216 0.2072 0.2200 -0.0018 -0.0042 0.0061 120 PRO B C 3278 O O . PRO B 39 ? 0.2305 0.2164 0.2284 -0.0020 -0.0040 0.0066 120 PRO B O 3279 C CB . PRO B 39 ? 0.1937 0.1785 0.1935 -0.0024 -0.0038 0.0058 120 PRO B CB 3280 C CG . PRO B 39 ? 0.1816 0.1660 0.1813 -0.0029 -0.0034 0.0064 120 PRO B CG 3281 C CD . PRO B 39 ? 0.1779 0.1614 0.1774 -0.0025 -0.0035 0.0073 120 PRO B CD 3282 N N . PHE B 40 ? 0.0906 0.0765 0.0888 -0.0015 -0.0044 0.0055 121 PHE B N 3283 C CA . PHE B 40 ? 0.0789 0.0656 0.0764 -0.0014 -0.0042 0.0053 121 PHE B CA 3284 C C . PHE B 40 ? 0.1083 0.0952 0.1060 -0.0010 -0.0042 0.0047 121 PHE B C 3285 O O . PHE B 40 ? 0.1247 0.1112 0.1227 -0.0008 -0.0044 0.0045 121 PHE B O 3286 C CB . PHE B 40 ? 0.0932 0.0799 0.0899 -0.0013 -0.0044 0.0055 121 PHE B CB 3287 C CG . PHE B 40 ? 0.0746 0.0609 0.0713 -0.0011 -0.0047 0.0053 121 PHE B CG 3288 C CD1 . PHE B 40 ? 0.0705 0.0567 0.0668 -0.0009 -0.0046 0.0047 121 PHE B CD1 3289 C CD2 . PHE B 40 ? 0.0924 0.0783 0.0893 -0.0010 -0.0050 0.0057 121 PHE B CD2 3290 C CE1 . PHE B 40 ? 0.0668 0.0527 0.0632 -0.0008 -0.0048 0.0045 121 PHE B CE1 3291 C CE2 . PHE B 40 ? 0.0818 0.0676 0.0787 -0.0008 -0.0052 0.0055 121 PHE B CE2 3292 C CZ . PHE B 40 ? 0.0865 0.0723 0.0831 -0.0008 -0.0052 0.0048 121 PHE B CZ 3293 N N . ILE B 41 ? 0.0777 0.0652 0.0751 -0.0009 -0.0039 0.0045 122 ILE B N 3294 C CA . ILE B 41 ? 0.0848 0.0726 0.0824 -0.0004 -0.0038 0.0041 122 ILE B CA 3295 C C . ILE B 41 ? 0.0957 0.0830 0.0926 0.0000 -0.0036 0.0038 122 ILE B C 3296 O O . ILE B 41 ? 0.0716 0.0588 0.0678 -0.0003 -0.0035 0.0038 122 ILE B O 3297 C CB . ILE B 41 ? 0.0856 0.0746 0.0835 -0.0003 -0.0035 0.0040 122 ILE B CB 3298 C CG1 . ILE B 41 ? 0.1132 0.1027 0.1119 -0.0008 -0.0036 0.0040 122 ILE B CG1 3299 C CG2 . ILE B 41 ? 0.0905 0.0799 0.0885 0.0004 -0.0033 0.0037 122 ILE B CG2 3300 C CD1 . ILE B 41 ? 0.1367 0.1277 0.1358 -0.0010 -0.0033 0.0039 122 ILE B CD1 3301 N N . SER B 42 ? 0.1170 0.1038 0.1139 0.0004 -0.0035 0.0036 123 SER B N 3302 C CA . SER B 42 ? 0.1098 0.0959 0.1062 0.0007 -0.0032 0.0033 123 SER B CA 3303 C C . SER B 42 ? 0.0936 0.0796 0.0903 0.0015 -0.0029 0.0033 123 SER B C 3304 O O . SER B 42 ? 0.1106 0.0970 0.1078 0.0017 -0.0032 0.0035 123 SER B O 3305 C CB . SER B 42 ? 0.1498 0.1351 0.1459 0.0004 -0.0034 0.0032 123 SER B CB 3306 O OG . SER B 42 ? 0.1419 0.1265 0.1374 0.0004 -0.0030 0.0027 123 SER B OG 3307 N N . CYS B 43 ? 0.0912 0.0766 0.0874 0.0019 -0.0023 0.0031 124 CYS B N 3308 C CA . CYS B 43 ? 0.1422 0.1277 0.1388 0.0029 -0.0019 0.0033 124 CYS B CA 3309 C C . CYS B 43 ? 0.1703 0.1541 0.1664 0.0031 -0.0014 0.0031 124 CYS B C 3310 O O . CYS B 43 ? 0.1181 0.1008 0.1136 0.0026 -0.0012 0.0027 124 CYS B O 3311 C CB . CYS B 43 ? 0.1204 0.1068 0.1171 0.0034 -0.0015 0.0033 124 CYS B CB 3312 S SG . CYS B 43 ? 0.1906 0.1791 0.1879 0.0030 -0.0019 0.0034 124 CYS B SG 3313 N N . SER B 44 ? 0.1984 0.1821 0.1948 0.0039 -0.0013 0.0035 125 SER B N 3314 C CA . SER B 44 ? 0.2165 0.1984 0.2125 0.0043 -0.0006 0.0035 125 SER B CA 3315 C C . SER B 44 ? 0.1957 0.1775 0.1918 0.0055 0.0002 0.0038 125 SER B C 3316 O O . SER B 44 ? 0.2286 0.2118 0.2249 0.0058 0.0002 0.0039 125 SER B O 3317 C CB . SER B 44 ? 0.1871 0.1689 0.1833 0.0045 -0.0009 0.0040 125 SER B CB 3318 O OG . SER B 44 ? 0.2389 0.2222 0.2356 0.0053 -0.0010 0.0046 125 SER B OG 3319 N N . PRO B 45 ? 0.1830 0.1632 0.1788 0.0061 0.0010 0.0040 126 PRO B N 3320 C CA . PRO B 45 ? 0.1985 0.1786 0.1945 0.0074 0.0018 0.0045 126 PRO B CA 3321 C C . PRO B 45 ? 0.2319 0.2141 0.2285 0.0084 0.0014 0.0054 126 PRO B C 3322 O O . PRO B 45 ? 0.2612 0.2440 0.2581 0.0096 0.0019 0.0059 126 PRO B O 3323 C CB . PRO B 45 ? 0.2455 0.2229 0.2410 0.0077 0.0028 0.0046 126 PRO B CB 3324 C CG . PRO B 45 ? 0.2017 0.1779 0.1968 0.0063 0.0026 0.0037 126 PRO B CG 3325 C CD . PRO B 45 ? 0.1701 0.1482 0.1655 0.0055 0.0013 0.0037 126 PRO B CD 3326 N N . LEU B 46 ? 0.2317 0.2151 0.2285 0.0078 0.0005 0.0055 127 LEU B N 3327 C CA . LEU B 46 ? 0.2638 0.2493 0.2611 0.0086 0.0001 0.0062 127 LEU B CA 3328 C C . LEU B 46 ? 0.2896 0.2776 0.2874 0.0080 -0.0008 0.0059 127 LEU B C 3329 O O . LEU B 46 ? 0.2953 0.2856 0.2937 0.0086 -0.0009 0.0063 127 LEU B O 3330 C CB . LEU B 46 ? 0.2715 0.2564 0.2686 0.0087 0.0000 0.0067 127 LEU B CB 3331 C CG . LEU B 46 ? 0.3316 0.3144 0.3284 0.0095 0.0010 0.0072 127 LEU B CG 3332 C CD1 . LEU B 46 ? 0.3636 0.3460 0.3602 0.0094 0.0008 0.0076 127 LEU B CD1 3333 C CD2 . LEU B 46 ? 0.3323 0.3158 0.3293 0.0111 0.0017 0.0081 127 LEU B CD2 3334 N N . GLU B 47 ? 0.2119 0.1994 0.2096 0.0067 -0.0013 0.0053 128 GLU B N 3335 C CA . GLU B 47 ? 0.2103 0.1997 0.2085 0.0060 -0.0020 0.0050 128 GLU B CA 3336 C C . GLU B 47 ? 0.2114 0.2001 0.2095 0.0049 -0.0023 0.0044 128 GLU B C 3337 O O . GLU B 47 ? 0.2112 0.1982 0.2087 0.0045 -0.0020 0.0042 128 GLU B O 3338 C CB . GLU B 47 ? 0.2411 0.2312 0.2396 0.0058 -0.0026 0.0051 128 GLU B CB 3339 C CG . GLU B 47 ? 0.2910 0.2794 0.2891 0.0051 -0.0027 0.0049 128 GLU B CG 3340 C CD . GLU B 47 ? 0.3956 0.3848 0.3940 0.0047 -0.0033 0.0048 128 GLU B CD 3341 O OE1 . GLU B 47 ? 0.4508 0.4421 0.4496 0.0050 -0.0035 0.0049 128 GLU B OE1 3342 O OE2 . GLU B 47 ? 0.3480 0.3361 0.3462 0.0042 -0.0035 0.0046 128 GLU B OE2 3343 N N . CYS B 48 ? 0.1435 0.1336 0.1420 0.0043 -0.0027 0.0043 129 CYS B N 3344 C CA . CYS B 48 ? 0.1339 0.1236 0.1323 0.0033 -0.0029 0.0039 129 CYS B CA 3345 C C . CYS B 48 ? 0.1461 0.1360 0.1448 0.0026 -0.0035 0.0038 129 CYS B C 3346 O O . CYS B 48 ? 0.1325 0.1237 0.1317 0.0026 -0.0037 0.0038 129 CYS B O 3347 C CB . CYS B 48 ? 0.2387 0.2296 0.2373 0.0031 -0.0028 0.0038 129 CYS B CB 3348 S SG . CYS B 48 ? 0.2648 0.2554 0.2630 0.0038 -0.0020 0.0038 129 CYS B SG 3349 N N . ARG B 49 ? 0.1078 0.0964 0.1063 0.0019 -0.0037 0.0037 130 ARG B N 3350 C CA . ARG B 49 ? 0.0801 0.0685 0.0789 0.0014 -0.0041 0.0036 130 ARG B CA 3351 C C . ARG B 49 ? 0.1108 0.0989 0.1096 0.0006 -0.0042 0.0036 130 ARG B C 3352 O O . ARG B 49 ? 0.1099 0.0976 0.1083 0.0005 -0.0041 0.0037 130 ARG B O 3353 C CB . ARG B 49 ? 0.1220 0.1093 0.1205 0.0015 -0.0042 0.0036 130 ARG B CB 3354 C CG . ARG B 49 ? 0.1676 0.1551 0.1660 0.0022 -0.0040 0.0038 130 ARG B CG 3355 C CD . ARG B 49 ? 0.1718 0.1583 0.1700 0.0022 -0.0041 0.0038 130 ARG B CD 3356 N NE . ARG B 49 ? 0.1672 0.1539 0.1658 0.0018 -0.0046 0.0036 130 ARG B NE 3357 C CZ . ARG B 49 ? 0.1885 0.1763 0.1875 0.0019 -0.0047 0.0035 130 ARG B CZ 3358 N NH1 . ARG B 49 ? 0.2144 0.2033 0.2135 0.0025 -0.0046 0.0037 130 ARG B NH1 3359 N NH2 . ARG B 49 ? 0.1386 0.1265 0.1380 0.0015 -0.0050 0.0032 130 ARG B NH2 3360 N N . THR B 50 ? 0.1232 0.1115 0.1225 0.0002 -0.0044 0.0035 131 THR B N 3361 C CA . THR B 50 ? 0.1332 0.1209 0.1327 -0.0004 -0.0045 0.0036 131 THR B CA 3362 C C . THR B 50 ? 0.1242 0.1108 0.1236 -0.0004 -0.0047 0.0038 131 THR B C 3363 O O . THR B 50 ? 0.1268 0.1133 0.1264 -0.0004 -0.0049 0.0035 131 THR B O 3364 C CB . THR B 50 ? 0.1684 0.1568 0.1685 -0.0010 -0.0044 0.0034 131 THR B CB 3365 O OG1 . THR B 50 ? 0.2452 0.2349 0.2455 -0.0011 -0.0042 0.0033 131 THR B OG1 3366 C CG2 . THR B 50 ? 0.1865 0.1738 0.1867 -0.0016 -0.0043 0.0038 131 THR B CG2 3367 N N . PHE B 51 ? 0.0633 0.0492 0.0621 -0.0005 -0.0048 0.0041 132 PHE B N 3368 C CA . PHE B 51 ? 0.0701 0.0553 0.0689 -0.0005 -0.0050 0.0043 132 PHE B CA 3369 C C . PHE B 51 ? 0.0810 0.0658 0.0802 -0.0008 -0.0050 0.0047 132 PHE B C 3370 O O . PHE B 51 ? 0.0912 0.0762 0.0903 -0.0011 -0.0047 0.0049 132 PHE B O 3371 C CB . PHE B 51 ? 0.0661 0.0512 0.0642 -0.0004 -0.0051 0.0044 132 PHE B CB 3372 C CG . PHE B 51 ? 0.0672 0.0523 0.0651 -0.0001 -0.0050 0.0040 132 PHE B CG 3373 C CD1 . PHE B 51 ? 0.0908 0.0761 0.0884 0.0001 -0.0047 0.0038 132 PHE B CD1 3374 C CD2 . PHE B 51 ? 0.0661 0.0507 0.0639 0.0000 -0.0052 0.0039 132 PHE B CD2 3375 C CE1 . PHE B 51 ? 0.1316 0.1165 0.1289 0.0004 -0.0045 0.0036 132 PHE B CE1 3376 C CE2 . PHE B 51 ? 0.0932 0.0776 0.0908 0.0002 -0.0050 0.0036 132 PHE B CE2 3377 C CZ . PHE B 51 ? 0.0970 0.0814 0.0944 0.0005 -0.0046 0.0035 132 PHE B CZ 3378 N N . PHE B 52 ? 0.0693 0.0535 0.0688 -0.0007 -0.0051 0.0048 133 PHE B N 3379 C CA . PHE B 52 ? 0.0991 0.0827 0.0990 -0.0009 -0.0050 0.0053 133 PHE B CA 3380 C C . PHE B 52 ? 0.1134 0.0964 0.1135 -0.0005 -0.0051 0.0056 133 PHE B C 3381 O O . PHE B 52 ? 0.0794 0.0625 0.0796 -0.0003 -0.0054 0.0053 133 PHE B O 3382 C CB . PHE B 52 ? 0.0776 0.0609 0.0781 -0.0013 -0.0046 0.0049 133 PHE B CB 3383 C CG . PHE B 52 ? 0.1148 0.0983 0.1157 -0.0013 -0.0047 0.0042 133 PHE B CG 3384 C CD1 . PHE B 52 ? 0.1174 0.1020 0.1182 -0.0013 -0.0048 0.0037 133 PHE B CD1 3385 C CD2 . PHE B 52 ? 0.1155 0.0983 0.1169 -0.0011 -0.0047 0.0040 133 PHE B CD2 3386 C CE1 . PHE B 52 ? 0.0975 0.0826 0.0987 -0.0012 -0.0049 0.0030 133 PHE B CE1 3387 C CE2 . PHE B 52 ? 0.1358 0.1190 0.1375 -0.0011 -0.0048 0.0033 133 PHE B CE2 3388 C CZ . PHE B 52 ? 0.1378 0.1222 0.1393 -0.0012 -0.0049 0.0028 133 PHE B CZ 3389 N N . LEU B 53 ? 0.0695 0.0519 0.0697 -0.0004 -0.0050 0.0064 134 LEU B N 3390 C CA . LEU B 53 ? 0.0748 0.0567 0.0753 0.0000 -0.0051 0.0068 134 LEU B CA 3391 C C . LEU B 53 ? 0.1083 0.0889 0.1096 0.0000 -0.0046 0.0067 134 LEU B C 3392 O O . LEU B 53 ? 0.0953 0.0751 0.0968 -0.0003 -0.0042 0.0071 134 LEU B O 3393 C CB . LEU B 53 ? 0.1024 0.0847 0.1025 0.0004 -0.0051 0.0079 134 LEU B CB 3394 C CG . LEU B 53 ? 0.1009 0.0845 0.1001 0.0003 -0.0055 0.0079 134 LEU B CG 3395 C CD1 . LEU B 53 ? 0.1465 0.1308 0.1454 0.0007 -0.0056 0.0090 134 LEU B CD1 3396 C CD2 . LEU B 53 ? 0.1078 0.0920 0.1071 0.0005 -0.0059 0.0073 134 LEU B CD2 3397 N N . THR B 54 ? 0.1269 0.1073 0.1287 0.0002 -0.0047 0.0061 135 THR B N 3398 C CA . THR B 54 ? 0.1446 0.1238 0.1472 0.0001 -0.0042 0.0057 135 THR B CA 3399 C C . THR B 54 ? 0.1558 0.1340 0.1587 0.0007 -0.0040 0.0066 135 THR B C 3400 O O . THR B 54 ? 0.1719 0.1508 0.1745 0.0013 -0.0043 0.0074 135 THR B O 3401 C CB . THR B 54 ? 0.1526 0.1321 0.1556 0.0001 -0.0043 0.0047 135 THR B CB 3402 O OG1 . THR B 54 ? 0.1752 0.1551 0.1782 0.0008 -0.0046 0.0049 135 THR B OG1 3403 C CG2 . THR B 54 ? 0.1405 0.1212 0.1430 -0.0003 -0.0046 0.0041 135 THR B CG2 3404 N N . GLN B 55 ? 0.1615 0.1381 0.1651 0.0007 -0.0034 0.0065 136 GLN B N 3405 C CA . GLN B 55 ? 0.1517 0.1273 0.1559 0.0015 -0.0030 0.0073 136 GLN B CA 3406 C C . GLN B 55 ? 0.1490 0.1243 0.1538 0.0018 -0.0029 0.0064 136 GLN B C 3407 O O . GLN B 55 ? 0.1790 0.1531 0.1844 0.0024 -0.0024 0.0068 136 GLN B O 3408 C CB . GLN B 55 ? 0.1591 0.1327 0.1637 0.0012 -0.0021 0.0078 136 GLN B CB 3409 C CG . GLN B 55 ? 0.2130 0.1869 0.2170 0.0010 -0.0021 0.0089 136 GLN B CG 3410 C CD . GLN B 55 ? 0.2761 0.2506 0.2796 0.0020 -0.0024 0.0104 136 GLN B CD 3411 O OE1 . GLN B 55 ? 0.2538 0.2287 0.2575 0.0029 -0.0027 0.0107 136 GLN B OE1 3412 N NE2 . GLN B 55 ? 0.2645 0.2391 0.2674 0.0019 -0.0023 0.0114 136 GLN B NE2 3413 N N . GLY B 56 ? 0.1412 0.1176 0.1459 0.0014 -0.0033 0.0053 137 GLY B N 3414 C CA . GLY B 56 ? 0.1308 0.1071 0.1360 0.0015 -0.0032 0.0044 137 GLY B CA 3415 C C . GLY B 56 ? 0.1650 0.1397 0.1709 0.0011 -0.0024 0.0036 137 GLY B C 3416 O O . GLY B 56 ? 0.1501 0.1240 0.1566 0.0016 -0.0020 0.0032 137 GLY B O 3417 N N . ALA B 57 ? 0.0892 0.0633 0.0951 0.0003 -0.0020 0.0034 138 ALA B N 3418 C CA . ALA B 57 ? 0.1388 0.1113 0.1454 -0.0004 -0.0011 0.0025 138 ALA B CA 3419 C C . ALA B 57 ? 0.0930 0.0661 0.0994 -0.0016 -0.0011 0.0017 138 ALA B C 3420 O O . ALA B 57 ? 0.0896 0.0640 0.0954 -0.0018 -0.0016 0.0021 138 ALA B O 3421 C CB . ALA B 57 ? 0.1377 0.1079 0.1447 0.0001 -0.0004 0.0036 138 ALA B CB 3422 N N . LEU B 58 ? 0.0725 0.0449 0.0795 -0.0024 -0.0004 0.0004 139 LEU B N 3423 C CA . LEU B 58 ? 0.0962 0.0695 0.1032 -0.0037 -0.0002 -0.0005 139 LEU B CA 3424 C C . LEU B 58 ? 0.1180 0.0893 0.1255 -0.0045 0.0007 -0.0004 139 LEU B C 3425 O O . LEU B 58 ? 0.1151 0.0840 0.1230 -0.0042 0.0015 0.0000 139 LEU B O 3426 C CB . LEU B 58 ? 0.0816 0.0561 0.0889 -0.0043 -0.0002 -0.0023 139 LEU B CB 3427 C CG . LEU B 58 ? 0.0859 0.0624 0.0927 -0.0037 -0.0011 -0.0025 139 LEU B CG 3428 C CD1 . LEU B 58 ? 0.1162 0.0940 0.1233 -0.0044 -0.0009 -0.0042 139 LEU B CD1 3429 C CD2 . LEU B 58 ? 0.0824 0.0607 0.0884 -0.0035 -0.0019 -0.0017 139 LEU B CD2 3430 N N . LEU B 59 ? 0.1180 0.0903 0.1253 -0.0055 0.0007 -0.0006 140 LEU B N 3431 C CA . LEU B 59 ? 0.1283 0.0990 0.1360 -0.0065 0.0017 -0.0007 140 LEU B CA 3432 C C . LEU B 59 ? 0.1509 0.1202 0.1595 -0.0074 0.0027 -0.0022 140 LEU B C 3433 O O . LEU B 59 ? 0.1353 0.1059 0.1441 -0.0077 0.0025 -0.0036 140 LEU B O 3434 C CB . LEU B 59 ? 0.1094 0.0821 0.1169 -0.0074 0.0014 -0.0009 140 LEU B CB 3435 C CG . LEU B 59 ? 0.1327 0.1062 0.1394 -0.0068 0.0008 0.0006 140 LEU B CG 3436 C CD1 . LEU B 59 ? 0.1520 0.1280 0.1585 -0.0075 0.0004 0.0001 140 LEU B CD1 3437 C CD2 . LEU B 59 ? 0.1470 0.1182 0.1538 -0.0067 0.0016 0.0020 140 LEU B CD2 3438 N N . ASN B 60 ? 0.1338 0.1002 0.1429 -0.0078 0.0038 -0.0018 141 ASN B N 3439 C CA . ASN B 60 ? 0.1309 0.0954 0.1409 -0.0088 0.0050 -0.0033 141 ASN B CA 3440 C C . ASN B 60 ? 0.1750 0.1385 0.1852 -0.0079 0.0052 -0.0038 141 ASN B C 3441 O O . ASN B 60 ? 0.1945 0.1573 0.2053 -0.0087 0.0059 -0.0056 141 ASN B O 3442 C CB . ASN B 60 ? 0.1542 0.1208 0.1644 -0.0105 0.0051 -0.0052 141 ASN B CB 3443 C CG . ASN B 60 ? 0.1994 0.1639 0.2103 -0.0121 0.0065 -0.0060 141 ASN B CG 3444 O OD1 . ASN B 60 ? 0.1827 0.1439 0.1939 -0.0118 0.0076 -0.0050 141 ASN B OD1 3445 N ND2 . ASN B 60 ? 0.1724 0.1390 0.1835 -0.0138 0.0066 -0.0076 141 ASN B ND2 3446 N N . ASP B 61 ? 0.1447 0.1083 0.1546 -0.0062 0.0045 -0.0024 142 ASP B N 3447 C CA . ASP B 61 ? 0.1552 0.1177 0.1654 -0.0052 0.0047 -0.0027 142 ASP B CA 3448 C C . ASP B 61 ? 0.1431 0.1032 0.1535 -0.0037 0.0052 -0.0007 142 ASP B C 3449 O O . ASP B 61 ? 0.1529 0.1131 0.1628 -0.0033 0.0048 0.0009 142 ASP B O 3450 C CB . ASP B 61 ? 0.1418 0.1072 0.1516 -0.0044 0.0035 -0.0029 142 ASP B CB 3451 C CG . ASP B 61 ? 0.1693 0.1338 0.1794 -0.0033 0.0036 -0.0030 142 ASP B CG 3452 O OD1 . ASP B 61 ? 0.1666 0.1305 0.1772 -0.0038 0.0043 -0.0046 142 ASP B OD1 3453 O OD2 . ASP B 61 ? 0.1594 0.1240 0.1692 -0.0019 0.0031 -0.0015 142 ASP B OD2 3454 N N . LYS B 62 ? 0.1126 0.0707 0.1236 -0.0030 0.0059 -0.0009 143 LYS B N 3455 C CA . LYS B 62 ? 0.1460 0.1018 0.1573 -0.0015 0.0065 0.0009 143 LYS B CA 3456 C C . LYS B 62 ? 0.1465 0.1041 0.1571 0.0000 0.0053 0.0028 143 LYS B C 3457 O O . LYS B 62 ? 0.1708 0.1273 0.1814 0.0010 0.0056 0.0047 143 LYS B O 3458 C CB . LYS B 62 ? 0.1571 0.1106 0.1693 -0.0008 0.0075 0.0003 143 LYS B CB 3459 C CG . LYS B 62 ? 0.1638 0.1193 0.1760 0.0001 0.0067 -0.0003 143 LYS B CG 3460 C CD . LYS B 62 ? 0.2274 0.1805 0.2405 0.0009 0.0079 -0.0009 143 LYS B CD 3461 C CE . LYS B 62 ? 0.2244 0.1795 0.2375 0.0019 0.0072 -0.0014 143 LYS B CE 3462 N NZ . LYS B 62 ? 0.2480 0.2008 0.2621 0.0028 0.0084 -0.0018 143 LYS B NZ 3463 N N . HIS B 63 ? 0.1468 0.1074 0.1569 0.0000 0.0040 0.0023 144 HIS B N 3464 C CA . HIS B 63 ? 0.1366 0.0990 0.1461 0.0012 0.0029 0.0038 144 HIS B CA 3465 C C . HIS B 63 ? 0.1523 0.1157 0.1610 0.0009 0.0024 0.0050 144 HIS B C 3466 O O . HIS B 63 ? 0.1221 0.0869 0.1303 0.0018 0.0016 0.0062 144 HIS B O 3467 C CB . HIS B 63 ? 0.1308 0.0959 0.1401 0.0014 0.0019 0.0028 144 HIS B CB 3468 C CG . HIS B 63 ? 0.1199 0.0844 0.1298 0.0020 0.0023 0.0020 144 HIS B CG 3469 N ND1 . HIS B 63 ? 0.1271 0.0913 0.1374 0.0011 0.0028 0.0001 144 HIS B ND1 3470 C CD2 . HIS B 63 ? 0.1210 0.0853 0.1313 0.0035 0.0024 0.0028 144 HIS B CD2 3471 C CE1 . HIS B 63 ? 0.1591 0.1228 0.1700 0.0020 0.0032 -0.0003 144 HIS B CE1 3472 N NE2 . HIS B 63 ? 0.1570 0.1208 0.1679 0.0035 0.0029 0.0014 144 HIS B NE2 3473 N N . SER B 64 ? 0.1308 0.0936 0.1395 -0.0004 0.0029 0.0044 145 SER B N 3474 C CA . SER B 64 ? 0.1331 0.0966 0.1411 -0.0007 0.0026 0.0055 145 SER B CA 3475 C C . SER B 64 ? 0.1419 0.1034 0.1500 0.0000 0.0033 0.0074 145 SER B C 3476 O O . SER B 64 ? 0.1293 0.0914 0.1368 0.0000 0.0031 0.0086 145 SER B O 3477 C CB . SER B 64 ? 0.1201 0.0839 0.1282 -0.0024 0.0028 0.0043 145 SER B CB 3478 O OG . SER B 64 ? 0.1349 0.0961 0.1437 -0.0032 0.0042 0.0038 145 SER B OG 3479 N N . ASN B 65 ? 0.1127 0.0720 0.1216 0.0009 0.0042 0.0077 146 ASN B N 3480 C CA . ASN B 65 ? 0.1576 0.1147 0.1666 0.0018 0.0050 0.0096 146 ASN B CA 3481 C C . ASN B 65 ? 0.2606 0.2197 0.2689 0.0031 0.0041 0.0116 146 ASN B C 3482 O O . ASN B 65 ? 0.2434 0.2046 0.2515 0.0039 0.0031 0.0115 146 ASN B O 3483 C CB . ASN B 65 ? 0.2311 0.1857 0.2411 0.0027 0.0061 0.0096 146 ASN B CB 3484 C CG . ASN B 65 ? 0.3461 0.2978 0.3564 0.0035 0.0073 0.0114 146 ASN B CG 3485 O OD1 . ASN B 65 ? 0.2863 0.2379 0.2961 0.0033 0.0074 0.0128 146 ASN B OD1 3486 N ND2 . ASN B 65 ? 0.5490 0.4983 0.5602 0.0046 0.0083 0.0116 146 ASN B ND2 3487 N N . GLY B 66 ? 0.2904 0.2489 0.2982 0.0032 0.0044 0.0132 147 GLY B N 3488 C CA . GLY B 66 ? 0.2865 0.2469 0.2936 0.0044 0.0036 0.0151 147 GLY B CA 3489 C C . GLY B 66 ? 0.3607 0.3244 0.3669 0.0040 0.0022 0.0146 147 GLY B C 3490 O O . GLY B 66 ? 0.3248 0.2906 0.3305 0.0049 0.0014 0.0156 147 GLY B O 3491 N N . THR B 67 ? 0.2405 0.2048 0.2465 0.0025 0.0020 0.0131 148 THR B N 3492 C CA . THR B 67 ? 0.2643 0.2315 0.2695 0.0021 0.0008 0.0126 148 THR B CA 3493 C C . THR B 67 ? 0.2246 0.1929 0.2289 0.0020 0.0006 0.0138 148 THR B C 3494 O O . THR B 67 ? 0.2437 0.2142 0.2473 0.0015 -0.0003 0.0133 148 THR B O 3495 C CB . THR B 67 ? 0.2171 0.1849 0.2224 0.0008 0.0006 0.0106 148 THR B CB 3496 O OG1 . THR B 67 ? 0.1815 0.1475 0.1873 -0.0003 0.0016 0.0100 148 THR B OG1 3497 C CG2 . THR B 67 ? 0.2301 0.1980 0.2360 0.0011 0.0004 0.0093 148 THR B CG2 3498 N N . ILE B 68 ? 0.2851 0.2520 0.2894 0.0023 0.0013 0.0154 149 ILE B N 3499 C CA . ILE B 68 ? 0.2613 0.2295 0.2647 0.0024 0.0011 0.0168 149 ILE B CA 3500 C C . ILE B 68 ? 0.3236 0.2942 0.3263 0.0035 0.0001 0.0176 149 ILE B C 3501 O O . ILE B 68 ? 0.3754 0.3480 0.3772 0.0035 -0.0004 0.0183 149 ILE B O 3502 C CB . ILE B 68 ? 0.3123 0.2783 0.3158 0.0027 0.0023 0.0185 149 ILE B CB 3503 C CG1 . ILE B 68 ? 0.3313 0.2988 0.3338 0.0024 0.0021 0.0197 149 ILE B CG1 3504 C CG2 . ILE B 68 ? 0.2675 0.2325 0.2715 0.0043 0.0026 0.0199 149 ILE B CG2 3505 C CD1 . ILE B 68 ? 0.3261 0.2915 0.3286 0.0026 0.0033 0.0215 149 ILE B CD1 3506 N N . LYS B 69 ? 0.2805 0.2513 0.2838 0.0045 -0.0002 0.0174 150 LYS B N 3507 C CA . LYS B 69 ? 0.2914 0.2647 0.2942 0.0055 -0.0011 0.0181 150 LYS B CA 3508 C C . LYS B 69 ? 0.3441 0.3198 0.3463 0.0047 -0.0021 0.0168 150 LYS B C 3509 O O . LYS B 69 ? 0.2440 0.2193 0.2464 0.0039 -0.0022 0.0151 150 LYS B O 3510 C CB . LYS B 69 ? 0.3396 0.3124 0.3433 0.0066 -0.0010 0.0181 150 LYS B CB 3511 C CG . LYS B 69 ? 0.3928 0.3685 0.3962 0.0076 -0.0019 0.0188 150 LYS B CG 3512 C CD . LYS B 69 ? 0.3833 0.3583 0.3876 0.0091 -0.0016 0.0196 150 LYS B CD 3513 C CE . LYS B 69 ? 0.4535 0.4315 0.4575 0.0103 -0.0023 0.0211 150 LYS B CE 3514 N NZ . LYS B 69 ? 0.4646 0.4454 0.4685 0.0102 -0.0033 0.0200 150 LYS B NZ 3515 N N . ASP B 70 ? 0.3149 0.2930 0.3162 0.0050 -0.0028 0.0175 151 ASP B N 3516 C CA . ASP B 70 ? 0.2638 0.2440 0.2644 0.0043 -0.0036 0.0163 151 ASP B CA 3517 C C . ASP B 70 ? 0.2595 0.2411 0.2604 0.0045 -0.0043 0.0154 151 ASP B C 3518 O O . ASP B 70 ? 0.2827 0.2647 0.2834 0.0038 -0.0046 0.0140 151 ASP B O 3519 C CB . ASP B 70 ? 0.3195 0.3019 0.3190 0.0043 -0.0040 0.0173 151 ASP B CB 3520 C CG . ASP B 70 ? 0.4013 0.3827 0.4004 0.0037 -0.0034 0.0179 151 ASP B CG 3521 O OD1 . ASP B 70 ? 0.3938 0.3735 0.3932 0.0029 -0.0029 0.0170 151 ASP B OD1 3522 O OD2 . ASP B 70 ? 0.4880 0.4706 0.4864 0.0041 -0.0033 0.0193 151 ASP B OD2 3523 N N . ARG B 71 ? 0.1669 0.1491 0.1681 0.0056 -0.0044 0.0163 152 ARG B N 3524 C CA . ARG B 71 ? 0.1815 0.1654 0.1830 0.0059 -0.0051 0.0155 152 ARG B CA 3525 C C . ARG B 71 ? 0.2266 0.2093 0.2292 0.0067 -0.0047 0.0154 152 ARG B C 3526 O O . ARG B 71 ? 0.2622 0.2436 0.2653 0.0076 -0.0042 0.0166 152 ARG B O 3527 C CB . ARG B 71 ? 0.1841 0.1710 0.1849 0.0064 -0.0057 0.0164 152 ARG B CB 3528 C CG . ARG B 71 ? 0.1686 0.1568 0.1683 0.0056 -0.0060 0.0164 152 ARG B CG 3529 C CD . ARG B 71 ? 0.1343 0.1258 0.1333 0.0059 -0.0066 0.0170 152 ARG B CD 3530 N NE . ARG B 71 ? 0.1430 0.1352 0.1422 0.0072 -0.0065 0.0189 152 ARG B NE 3531 C CZ . ARG B 71 ? 0.2452 0.2371 0.2439 0.0075 -0.0061 0.0204 152 ARG B CZ 3532 N NH1 . ARG B 71 ? 0.2064 0.1975 0.2045 0.0066 -0.0058 0.0201 152 ARG B NH1 3533 N NH2 . ARG B 71 ? 0.2473 0.2399 0.2463 0.0089 -0.0059 0.0222 152 ARG B NH2 3534 N N . SER B 72 ? 0.1362 0.1192 0.1391 0.0063 -0.0051 0.0140 153 SER B N 3535 C CA . SER B 72 ? 0.1451 0.1273 0.1490 0.0070 -0.0048 0.0137 153 SER B CA 3536 C C . SER B 72 ? 0.1079 0.0913 0.1117 0.0065 -0.0053 0.0123 153 SER B C 3537 O O . SER B 72 ? 0.1183 0.1024 0.1215 0.0056 -0.0057 0.0115 153 SER B O 3538 C CB . SER B 72 ? 0.1626 0.1418 0.1671 0.0069 -0.0039 0.0133 153 SER B CB 3539 O OG . SER B 72 ? 0.1469 0.1255 0.1513 0.0057 -0.0040 0.0118 153 SER B OG 3540 N N . PRO B 73 ? 0.1277 0.1114 0.1324 0.0072 -0.0053 0.0121 154 PRO B N 3541 C CA . PRO B 73 ? 0.1225 0.1073 0.1272 0.0067 -0.0057 0.0108 154 PRO B CA 3542 C C . PRO B 73 ? 0.1257 0.1088 0.1304 0.0058 -0.0054 0.0094 154 PRO B C 3543 O O . PRO B 73 ? 0.1205 0.1044 0.1252 0.0054 -0.0057 0.0084 154 PRO B O 3544 C CB . PRO B 73 ? 0.1375 0.1229 0.1431 0.0078 -0.0056 0.0111 154 PRO B CB 3545 C CG . PRO B 73 ? 0.1407 0.1243 0.1470 0.0087 -0.0049 0.0121 154 PRO B CG 3546 C CD . PRO B 73 ? 0.1786 0.1618 0.1841 0.0085 -0.0049 0.0131 154 PRO B CD 3547 N N . TYR B 74 ? 0.0761 0.0573 0.0810 0.0056 -0.0049 0.0094 155 TYR B N 3548 C CA . TYR B 74 ? 0.1017 0.0815 0.1066 0.0048 -0.0046 0.0082 155 TYR B CA 3549 C C . TYR B 74 ? 0.1263 0.1064 0.1304 0.0038 -0.0048 0.0077 155 TYR B C 3550 O O . TYR B 74 ? 0.1237 0.1037 0.1278 0.0031 -0.0048 0.0066 155 TYR B O 3551 C CB . TYR B 74 ? 0.1023 0.0798 0.1079 0.0049 -0.0037 0.0081 155 TYR B CB 3552 C CG . TYR B 74 ? 0.1355 0.1124 0.1419 0.0061 -0.0033 0.0088 155 TYR B CG 3553 C CD1 . TYR B 74 ? 0.1148 0.0926 0.1218 0.0066 -0.0034 0.0082 155 TYR B CD1 3554 C CD2 . TYR B 74 ? 0.1655 0.1412 0.1723 0.0068 -0.0028 0.0101 155 TYR B CD2 3555 C CE1 . TYR B 74 ? 0.1523 0.1296 0.1601 0.0078 -0.0030 0.0089 155 TYR B CE1 3556 C CE2 . TYR B 74 ? 0.1598 0.1349 0.1674 0.0081 -0.0023 0.0109 155 TYR B CE2 3557 C CZ . TYR B 74 ? 0.1689 0.1448 0.1770 0.0086 -0.0024 0.0102 155 TYR B CZ 3558 O OH . TYR B 74 ? 0.2059 0.1814 0.2149 0.0100 -0.0019 0.0109 155 TYR B OH 3559 N N . ARG B 75 ? 0.0995 0.0803 0.1030 0.0037 -0.0050 0.0085 156 ARG B N 3560 C CA . ARG B 75 ? 0.1261 0.1071 0.1289 0.0029 -0.0052 0.0082 156 ARG B CA 3561 C C . ARG B 75 ? 0.0857 0.0680 0.0880 0.0025 -0.0057 0.0073 156 ARG B C 3562 O O . ARG B 75 ? 0.1085 0.0921 0.1107 0.0027 -0.0061 0.0075 156 ARG B O 3563 C CB . ARG B 75 ? 0.1191 0.1005 0.1212 0.0029 -0.0052 0.0092 156 ARG B CB 3564 C CG . ARG B 75 ? 0.1666 0.1465 0.1692 0.0033 -0.0046 0.0102 156 ARG B CG 3565 C CD . ARG B 75 ? 0.1698 0.1499 0.1717 0.0030 -0.0045 0.0110 156 ARG B CD 3566 N NE . ARG B 75 ? 0.1557 0.1352 0.1574 0.0020 -0.0043 0.0102 156 ARG B NE 3567 C CZ . ARG B 75 ? 0.1967 0.1763 0.1979 0.0015 -0.0042 0.0106 156 ARG B CZ 3568 N NH1 . ARG B 75 ? 0.1891 0.1693 0.1898 0.0019 -0.0042 0.0119 156 ARG B NH1 3569 N NH2 . ARG B 75 ? 0.2100 0.1894 0.2111 0.0007 -0.0040 0.0098 156 ARG B NH2 3570 N N . THR B 76 ? 0.1108 0.0929 0.1129 0.0018 -0.0056 0.0065 157 THR B N 3571 C CA . THR B 76 ? 0.0903 0.0732 0.0919 0.0015 -0.0059 0.0059 157 THR B CA 3572 C C . THR B 76 ? 0.0995 0.0826 0.1006 0.0010 -0.0059 0.0057 157 THR B C 3573 O O . THR B 76 ? 0.1135 0.0959 0.1147 0.0007 -0.0056 0.0057 157 THR B O 3574 C CB . THR B 76 ? 0.1382 0.1211 0.1403 0.0015 -0.0059 0.0050 157 THR B CB 3575 O OG1 . THR B 76 ? 0.1927 0.1749 0.1951 0.0012 -0.0055 0.0045 157 THR B OG1 3576 C CG2 . THR B 76 ? 0.1150 0.0979 0.1177 0.0021 -0.0059 0.0052 157 THR B CG2 3577 N N . LEU B 77 ? 0.0605 0.0443 0.0609 0.0008 -0.0061 0.0054 158 LEU B N 3578 C CA . LEU B 77 ? 0.0491 0.0330 0.0489 0.0004 -0.0060 0.0051 158 LEU B CA 3579 C C . LEU B 77 ? 0.0717 0.0555 0.0717 0.0003 -0.0059 0.0045 158 LEU B C 3580 O O . LEU B 77 ? 0.0804 0.0645 0.0805 0.0005 -0.0060 0.0041 158 LEU B O 3581 C CB . LEU B 77 ? 0.0579 0.0426 0.0571 0.0003 -0.0062 0.0051 158 LEU B CB 3582 C CG . LEU B 77 ? 0.0596 0.0442 0.0582 0.0000 -0.0060 0.0048 158 LEU B CG 3583 C CD1 . LEU B 77 ? 0.0643 0.0490 0.0628 -0.0002 -0.0058 0.0052 158 LEU B CD1 3584 C CD2 . LEU B 77 ? 0.0809 0.0660 0.0789 -0.0002 -0.0060 0.0045 158 LEU B CD2 3585 N N . MET B 78 ? 0.0780 0.0617 0.0781 0.0001 -0.0057 0.0043 159 MET B N 3586 C CA . MET B 78 ? 0.1005 0.0846 0.1008 0.0001 -0.0056 0.0037 159 MET B CA 3587 C C . MET B 78 ? 0.0860 0.0705 0.0860 0.0000 -0.0055 0.0036 159 MET B C 3588 O O . MET B 78 ? 0.0913 0.0757 0.0910 -0.0002 -0.0054 0.0040 159 MET B O 3589 C CB . MET B 78 ? 0.0824 0.0662 0.0833 0.0000 -0.0055 0.0033 159 MET B CB 3590 C CG . MET B 78 ? 0.1424 0.1257 0.1438 0.0003 -0.0056 0.0033 159 MET B CG 3591 S SD . MET B 78 ? 0.2368 0.2200 0.2390 0.0001 -0.0053 0.0026 159 MET B SD 3592 C CE . MET B 78 ? 0.2198 0.2041 0.2217 0.0002 -0.0055 0.0020 159 MET B CE 3593 N N . SER B 79 ? 0.0667 0.0518 0.0667 0.0001 -0.0054 0.0033 160 SER B N 3594 C CA . SER B 79 ? 0.0597 0.0454 0.0595 0.0001 -0.0053 0.0033 160 SER B CA 3595 C C . SER B 79 ? 0.1048 0.0915 0.1049 0.0001 -0.0052 0.0029 160 SER B C 3596 O O . SER B 79 ? 0.0789 0.0659 0.0792 0.0003 -0.0053 0.0026 160 SER B O 3597 C CB . SER B 79 ? 0.1013 0.0868 0.1004 0.0004 -0.0052 0.0034 160 SER B CB 3598 O OG . SER B 79 ? 0.1200 0.1056 0.1190 0.0008 -0.0052 0.0034 160 SER B OG 3599 N N . CYS B 80 ? 0.0918 0.0794 0.0920 0.0000 -0.0051 0.0028 161 CYS B N 3600 C CA . CYS B 80 ? 0.1136 0.1028 0.1142 0.0001 -0.0051 0.0025 161 CYS B CA 3601 C C . CYS B 80 ? 0.1239 0.1141 0.1243 0.0004 -0.0049 0.0027 161 CYS B C 3602 O O . CYS B 80 ? 0.0944 0.0839 0.0945 0.0004 -0.0048 0.0030 161 CYS B O 3603 C CB . CYS B 80 ? 0.1038 0.0934 0.1051 -0.0006 -0.0051 0.0019 161 CYS B CB 3604 S SG . CYS B 80 ? 0.1833 0.1725 0.1848 -0.0013 -0.0048 0.0020 161 CYS B SG 3605 N N . PRO B 81 ? 0.1346 0.1265 0.1353 0.0007 -0.0049 0.0026 162 PRO B N 3606 C CA . PRO B 81 ? 0.0985 0.0916 0.0991 0.0012 -0.0047 0.0028 162 PRO B CA 3607 C C . PRO B 81 ? 0.0842 0.0776 0.0851 0.0005 -0.0046 0.0026 162 PRO B C 3608 O O . PRO B 81 ? 0.0907 0.0842 0.0921 -0.0004 -0.0046 0.0022 162 PRO B O 3609 C CB . PRO B 81 ? 0.1130 0.1084 0.1139 0.0015 -0.0048 0.0027 162 PRO B CB 3610 C CG . PRO B 81 ? 0.1910 0.1859 0.1918 0.0016 -0.0050 0.0026 162 PRO B CG 3611 C CD . PRO B 81 ? 0.1282 0.1212 0.1291 0.0009 -0.0051 0.0023 162 PRO B CD 3612 N N . ILE B 82 ? 0.1215 0.1151 0.1222 0.0008 -0.0043 0.0029 163 ILE B N 3613 C CA . ILE B 82 ? 0.1336 0.1276 0.1346 0.0001 -0.0041 0.0028 163 ILE B CA 3614 C C . ILE B 82 ? 0.1597 0.1558 0.1615 -0.0005 -0.0042 0.0023 163 ILE B C 3615 O O . ILE B 82 ? 0.1055 0.1035 0.1075 0.0000 -0.0042 0.0022 163 ILE B O 3616 C CB . ILE B 82 ? 0.1754 0.1695 0.1760 0.0006 -0.0038 0.0031 163 ILE B CB 3617 C CG1 . ILE B 82 ? 0.2025 0.1965 0.2031 -0.0001 -0.0036 0.0032 163 ILE B CG1 3618 C CG2 . ILE B 82 ? 0.1906 0.1867 0.1914 0.0014 -0.0037 0.0032 163 ILE B CG2 3619 C CD1 . ILE B 82 ? 0.1750 0.1692 0.1752 0.0003 -0.0033 0.0034 163 ILE B CD1 3620 N N . GLY B 83 ? 0.0798 0.0754 0.0818 -0.0015 -0.0040 0.0021 164 GLY B N 3621 C CA . GLY B 83 ? 0.0948 0.0924 0.0977 -0.0023 -0.0039 0.0015 164 GLY B CA 3622 C C . GLY B 83 ? 0.1159 0.1136 0.1192 -0.0029 -0.0041 0.0008 164 GLY B C 3623 O O . GLY B 83 ? 0.1354 0.1343 0.1393 -0.0038 -0.0039 0.0001 164 GLY B O 3624 N N . GLU B 84 ? 0.0998 0.0962 0.1027 -0.0024 -0.0043 0.0009 165 GLU B N 3625 C CA . GLU B 84 ? 0.1092 0.1055 0.1124 -0.0029 -0.0044 0.0002 165 GLU B CA 3626 C C . GLU B 84 ? 0.1309 0.1247 0.1342 -0.0035 -0.0042 0.0002 165 GLU B C 3627 O O . GLU B 84 ? 0.1126 0.1047 0.1155 -0.0032 -0.0042 0.0009 165 GLU B O 3628 C CB . GLU B 84 ? 0.1464 0.1430 0.1493 -0.0020 -0.0047 0.0004 165 GLU B CB 3629 C CG . GLU B 84 ? 0.1432 0.1423 0.1460 -0.0013 -0.0049 0.0005 165 GLU B CG 3630 C CD . GLU B 84 ? 0.2144 0.2138 0.2169 -0.0004 -0.0051 0.0007 165 GLU B CD 3631 O OE1 . GLU B 84 ? 0.2322 0.2304 0.2346 -0.0007 -0.0052 0.0004 165 GLU B OE1 3632 O OE2 . GLU B 84 ? 0.1982 0.1990 0.2004 0.0005 -0.0052 0.0013 165 GLU B OE2 3633 N N . VAL B 85 ? 0.1275 0.1211 0.1313 -0.0043 -0.0040 -0.0006 166 VAL B N 3634 C CA . VAL B 85 ? 0.1061 0.0972 0.1101 -0.0048 -0.0037 -0.0006 166 VAL B CA 3635 C C . VAL B 85 ? 0.1185 0.1082 0.1221 -0.0039 -0.0040 -0.0002 166 VAL B C 3636 O O . VAL B 85 ? 0.1463 0.1371 0.1497 -0.0034 -0.0043 -0.0004 166 VAL B O 3637 C CB . VAL B 85 ? 0.1198 0.1109 0.1245 -0.0059 -0.0033 -0.0017 166 VAL B CB 3638 C CG1 . VAL B 85 ? 0.1365 0.1290 0.1417 -0.0069 -0.0029 -0.0021 166 VAL B CG1 3639 C CG2 . VAL B 85 ? 0.1518 0.1443 0.1567 -0.0058 -0.0035 -0.0025 166 VAL B CG2 3640 N N . PRO B 86 ? 0.1315 0.1192 0.1349 -0.0037 -0.0039 0.0005 167 PRO B N 3641 C CA . PRO B 86 ? 0.1412 0.1276 0.1442 -0.0030 -0.0041 0.0008 167 PRO B CA 3642 C C . PRO B 86 ? 0.1261 0.1120 0.1297 -0.0033 -0.0040 0.0001 167 PRO B C 3643 O O . PRO B 86 ? 0.1413 0.1256 0.1452 -0.0036 -0.0036 0.0001 167 PRO B O 3644 C CB . PRO B 86 ? 0.1625 0.1473 0.1653 -0.0029 -0.0040 0.0018 167 PRO B CB 3645 C CG . PRO B 86 ? 0.1685 0.1529 0.1717 -0.0037 -0.0035 0.0017 167 PRO B CG 3646 C CD . PRO B 86 ? 0.1500 0.1364 0.1534 -0.0042 -0.0035 0.0010 167 PRO B CD 3647 N N . SER B 87 ? 0.1289 0.1161 0.1324 -0.0031 -0.0042 -0.0005 168 SER B N 3648 C CA . SER B 87 ? 0.1237 0.1107 0.1277 -0.0033 -0.0041 -0.0013 168 SER B CA 3649 C C . SER B 87 ? 0.0891 0.0760 0.0927 -0.0025 -0.0044 -0.0011 168 SER B C 3650 O O . SER B 87 ? 0.1020 0.0896 0.1051 -0.0019 -0.0048 -0.0004 168 SER B O 3651 C CB . SER B 87 ? 0.1309 0.1201 0.1352 -0.0040 -0.0040 -0.0024 168 SER B CB 3652 O OG . SER B 87 ? 0.1907 0.1801 0.1953 -0.0042 -0.0039 -0.0033 168 SER B OG 3653 N N . PRO B 88 ? 0.1351 0.1211 0.1391 -0.0025 -0.0042 -0.0016 169 PRO B N 3654 C CA . PRO B 88 ? 0.1552 0.1414 0.1589 -0.0018 -0.0045 -0.0014 169 PRO B CA 3655 C C . PRO B 88 ? 0.1673 0.1557 0.1707 -0.0017 -0.0048 -0.0018 169 PRO B C 3656 O O . PRO B 88 ? 0.2005 0.1891 0.2035 -0.0012 -0.0050 -0.0015 169 PRO B O 3657 C CB . PRO B 88 ? 0.1477 0.1328 0.1520 -0.0020 -0.0041 -0.0021 169 PRO B CB 3658 C CG . PRO B 88 ? 0.1683 0.1530 0.1732 -0.0029 -0.0035 -0.0029 169 PRO B CG 3659 C CD . PRO B 88 ? 0.1393 0.1239 0.1439 -0.0031 -0.0036 -0.0022 169 PRO B CD 3660 N N . TYR B 89 A 0.1141 0.1041 0.1176 -0.0023 -0.0047 -0.0024 169 TYR B N 3661 C CA . TYR B 89 A 0.1175 0.1098 0.1206 -0.0021 -0.0050 -0.0026 169 TYR B CA 3662 C C . TYR B 89 A 0.1632 0.1566 0.1658 -0.0015 -0.0053 -0.0017 169 TYR B C 3663 O O . TYR B 89 A 0.1726 0.1678 0.1748 -0.0010 -0.0055 -0.0016 169 TYR B O 3664 C CB . TYR B 89 A 0.1294 0.1236 0.1330 -0.0029 -0.0048 -0.0039 169 TYR B CB 3665 C CG . TYR B 89 A 0.1152 0.1080 0.1194 -0.0037 -0.0043 -0.0049 169 TYR B CG 3666 C CD1 . TYR B 89 A 0.1539 0.1454 0.1582 -0.0033 -0.0042 -0.0050 169 TYR B CD1 3667 C CD2 . TYR B 89 A 0.1197 0.1126 0.1245 -0.0047 -0.0039 -0.0059 169 TYR B CD2 3668 C CE1 . TYR B 89 A 0.1249 0.1150 0.1297 -0.0038 -0.0037 -0.0060 169 TYR B CE1 3669 C CE2 . TYR B 89 A 0.1452 0.1364 0.1505 -0.0054 -0.0033 -0.0069 169 TYR B CE2 3670 C CZ . TYR B 89 A 0.1443 0.1342 0.1497 -0.0048 -0.0032 -0.0069 169 TYR B CZ 3671 O OH . TYR B 89 A 0.1521 0.1404 0.1582 -0.0054 -0.0025 -0.0079 169 TYR B OH 3672 N N . ASN B 90 ? 0.1454 0.1377 0.1479 -0.0014 -0.0052 -0.0011 170 ASN B N 3673 C CA . ASN B 90 ? 0.1460 0.1390 0.1481 -0.0008 -0.0054 -0.0003 170 ASN B CA 3674 C C . ASN B 90 ? 0.1728 0.1640 0.1745 -0.0004 -0.0054 0.0006 170 ASN B C 3675 O O . ASN B 90 ? 0.1863 0.1777 0.1876 0.0000 -0.0054 0.0012 170 ASN B O 3676 C CB . ASN B 90 ? 0.2168 0.2113 0.2192 -0.0013 -0.0053 -0.0005 170 ASN B CB 3677 C CG . ASN B 90 ? 0.2011 0.1940 0.2037 -0.0018 -0.0051 -0.0004 170 ASN B CG 3678 O OD1 . ASN B 90 ? 0.1953 0.1864 0.1981 -0.0020 -0.0049 -0.0004 170 ASN B OD1 3679 N ND2 . ASN B 90 ? 0.2296 0.2235 0.2323 -0.0019 -0.0050 -0.0002 170 ASN B ND2 3680 N N . SER B 91 ? 0.1169 0.1063 0.1187 -0.0005 -0.0054 0.0006 171 SER B N 3681 C CA . SER B 91 ? 0.1314 0.1194 0.1328 -0.0003 -0.0054 0.0013 171 SER B CA 3682 C C . SER B 91 ? 0.1377 0.1252 0.1388 0.0002 -0.0055 0.0017 171 SER B C 3683 O O . SER B 91 ? 0.1705 0.1581 0.1718 0.0003 -0.0056 0.0014 171 SER B O 3684 C CB . SER B 91 ? 0.1425 0.1291 0.1443 -0.0006 -0.0052 0.0014 171 SER B CB 3685 O OG . SER B 91 ? 0.1358 0.1227 0.1379 -0.0012 -0.0050 0.0012 171 SER B OG 3686 N N . ARG B 92 ? 0.1254 0.1125 0.1260 0.0005 -0.0055 0.0022 172 ARG B N 3687 C CA . ARG B 92 ? 0.1608 0.1474 0.1610 0.0008 -0.0056 0.0025 172 ARG B CA 3688 C C . ARG B 92 ? 0.1523 0.1379 0.1526 0.0007 -0.0057 0.0027 172 ARG B C 3689 O O . ARG B 92 ? 0.1348 0.1200 0.1350 0.0005 -0.0056 0.0029 172 ARG B O 3690 C CB . ARG B 92 ? 0.1827 0.1692 0.1823 0.0012 -0.0054 0.0029 172 ARG B CB 3691 C CG . ARG B 92 ? 0.3158 0.3018 0.3150 0.0014 -0.0053 0.0031 172 ARG B CG 3692 C CD . ARG B 92 ? 0.3174 0.3031 0.3161 0.0017 -0.0049 0.0034 172 ARG B CD 3693 N NE . ARG B 92 ? 0.3555 0.3405 0.3540 0.0015 -0.0048 0.0035 172 ARG B NE 3694 C CZ . ARG B 92 ? 0.3848 0.3695 0.3828 0.0018 -0.0045 0.0037 172 ARG B CZ 3695 N NH1 . ARG B 92 ? 0.3374 0.3225 0.3354 0.0024 -0.0042 0.0039 172 ARG B NH1 3696 N NH2 . ARG B 92 ? 0.3235 0.3077 0.3213 0.0015 -0.0044 0.0036 172 ARG B NH2 3697 N N . PHE B 93 ? 0.0776 0.0630 0.0780 0.0008 -0.0057 0.0026 173 PHE B N 3698 C CA . PHE B 93 ? 0.1346 0.1195 0.1351 0.0007 -0.0058 0.0029 173 PHE B CA 3699 C C . PHE B 93 ? 0.1040 0.0888 0.1039 0.0007 -0.0058 0.0031 173 PHE B C 3700 O O . PHE B 93 ? 0.1248 0.1096 0.1243 0.0007 -0.0057 0.0031 173 PHE B O 3701 C CB . PHE B 93 ? 0.0910 0.0760 0.0919 0.0009 -0.0059 0.0027 173 PHE B CB 3702 C CG . PHE B 93 ? 0.0821 0.0669 0.0831 0.0010 -0.0061 0.0030 173 PHE B CG 3703 C CD1 . PHE B 93 ? 0.1035 0.0880 0.1050 0.0011 -0.0061 0.0032 173 PHE B CD1 3704 C CD2 . PHE B 93 ? 0.1054 0.0906 0.1061 0.0009 -0.0061 0.0031 173 PHE B CD2 3705 C CE1 . PHE B 93 ? 0.1042 0.0888 0.1058 0.0013 -0.0062 0.0037 173 PHE B CE1 3706 C CE2 . PHE B 93 ? 0.0958 0.0813 0.0967 0.0009 -0.0063 0.0034 173 PHE B CE2 3707 C CZ . PHE B 93 ? 0.0835 0.0688 0.0848 0.0012 -0.0064 0.0037 173 PHE B CZ 3708 N N . GLU B 94 ? 0.1413 0.1259 0.1411 0.0005 -0.0059 0.0034 174 GLU B N 3709 C CA . GLU B 94 ? 0.1120 0.0965 0.1112 0.0004 -0.0059 0.0035 174 GLU B CA 3710 C C . GLU B 94 ? 0.1239 0.1088 0.1232 0.0003 -0.0061 0.0036 174 GLU B C 3711 O O . GLU B 94 ? 0.1192 0.1043 0.1182 0.0001 -0.0061 0.0034 174 GLU B O 3712 C CB . GLU B 94 ? 0.1146 0.0990 0.1134 0.0002 -0.0058 0.0037 174 GLU B CB 3713 C CG . GLU B 94 ? 0.1130 0.0973 0.1118 0.0003 -0.0056 0.0036 174 GLU B CG 3714 C CD . GLU B 94 ? 0.1691 0.1533 0.1676 0.0005 -0.0053 0.0034 174 GLU B CD 3715 O OE1 . GLU B 94 ? 0.1567 0.1406 0.1549 0.0004 -0.0053 0.0033 174 GLU B OE1 3716 O OE2 . GLU B 94 ? 0.1716 0.1560 0.1701 0.0007 -0.0052 0.0034 174 GLU B OE2 3717 N N . SER B 95 ? 0.0719 0.0570 0.0715 0.0004 -0.0063 0.0040 175 SER B N 3718 C CA . SER B 95 ? 0.0774 0.0633 0.0771 0.0005 -0.0066 0.0043 175 SER B CA 3719 C C . SER B 95 ? 0.0888 0.0746 0.0891 0.0009 -0.0067 0.0048 175 SER B C 3720 O O . SER B 95 ? 0.1046 0.0897 0.1051 0.0010 -0.0065 0.0050 175 SER B O 3721 C CB . SER B 95 ? 0.1214 0.1078 0.1205 0.0001 -0.0066 0.0043 175 SER B CB 3722 O OG . SER B 95 ? 0.2565 0.2441 0.2556 0.0000 -0.0069 0.0045 175 SER B OG 3723 N N . VAL B 96 ? 0.0903 0.0770 0.0910 0.0012 -0.0069 0.0051 176 VAL B N 3724 C CA . VAL B 96 ? 0.0886 0.0752 0.0897 0.0018 -0.0069 0.0058 176 VAL B CA 3725 C C . VAL B 96 ? 0.1023 0.0896 0.1029 0.0017 -0.0070 0.0065 176 VAL B C 3726 O O . VAL B 96 ? 0.1375 0.1262 0.1377 0.0015 -0.0073 0.0064 176 VAL B O 3727 C CB . VAL B 96 ? 0.1100 0.0975 0.1119 0.0023 -0.0070 0.0060 176 VAL B CB 3728 C CG1 . VAL B 96 ? 0.0901 0.0774 0.0925 0.0031 -0.0069 0.0068 176 VAL B CG1 3729 C CG2 . VAL B 96 ? 0.0770 0.0641 0.0793 0.0023 -0.0068 0.0052 176 VAL B CG2 3730 N N . ALA B 97 ? 0.0757 0.0621 0.0763 0.0019 -0.0068 0.0070 177 ALA B N 3731 C CA . ALA B 97 ? 0.0776 0.0648 0.0776 0.0018 -0.0069 0.0076 177 ALA B CA 3732 C C . ALA B 97 ? 0.0869 0.0732 0.0871 0.0021 -0.0066 0.0085 177 ALA B C 3733 O O . ALA B 97 ? 0.0906 0.0754 0.0911 0.0020 -0.0063 0.0083 177 ALA B O 3734 C CB . ALA B 97 ? 0.0900 0.0773 0.0892 0.0011 -0.0069 0.0070 177 ALA B CB 3735 N N . TRP B 98 ? 0.0708 0.0580 0.0706 0.0024 -0.0068 0.0095 178 TRP B N 3736 C CA . TRP B 98 ? 0.0853 0.0717 0.0850 0.0026 -0.0064 0.0104 178 TRP B CA 3737 C C . TRP B 98 ? 0.0931 0.0805 0.0919 0.0020 -0.0065 0.0106 178 TRP B C 3738 O O . TRP B 98 ? 0.0736 0.0606 0.0721 0.0021 -0.0062 0.0114 178 TRP B O 3739 C CB . TRP B 98 ? 0.1010 0.0875 0.1012 0.0035 -0.0063 0.0117 178 TRP B CB 3740 C CG . TRP B 98 ? 0.1029 0.0917 0.1031 0.0041 -0.0068 0.0122 178 TRP B CG 3741 C CD1 . TRP B 98 ? 0.1021 0.0913 0.1030 0.0047 -0.0070 0.0122 178 TRP B CD1 3742 C CD2 . TRP B 98 ? 0.0843 0.0754 0.0837 0.0039 -0.0072 0.0127 178 TRP B CD2 3743 N NE1 . TRP B 98 ? 0.1227 0.1145 0.1233 0.0050 -0.0074 0.0127 178 TRP B NE1 3744 C CE2 . TRP B 98 ? 0.1041 0.0971 0.1037 0.0045 -0.0076 0.0130 178 TRP B CE2 3745 C CE3 . TRP B 98 ? 0.1015 0.0934 0.0999 0.0034 -0.0073 0.0128 178 TRP B CE3 3746 C CZ2 . TRP B 98 ? 0.0954 0.0913 0.0944 0.0045 -0.0081 0.0133 178 TRP B CZ2 3747 C CZ3 . TRP B 98 ? 0.1247 0.1192 0.1223 0.0034 -0.0077 0.0131 178 TRP B CZ3 3748 C CH2 . TRP B 98 ? 0.1106 0.1072 0.1086 0.0039 -0.0081 0.0134 178 TRP B CH2 3749 N N . SER B 99 ? 0.0721 0.0606 0.0702 0.0015 -0.0068 0.0097 179 SER B N 3750 C CA . SER B 99 ? 0.0908 0.0801 0.0881 0.0009 -0.0068 0.0095 179 SER B CA 3751 C C . SER B 99 ? 0.0763 0.0656 0.0733 0.0004 -0.0068 0.0082 179 SER B C 3752 O O . SER B 99 ? 0.0856 0.0753 0.0828 0.0004 -0.0071 0.0077 179 SER B O 3753 C CB . SER B 99 ? 0.1012 0.0926 0.0978 0.0010 -0.0071 0.0102 179 SER B CB 3754 O OG . SER B 99 ? 0.1260 0.1181 0.1217 0.0004 -0.0070 0.0098 179 SER B OG 3755 N N . ALA B 100 ? 0.0863 0.0751 0.0829 -0.0001 -0.0066 0.0076 180 ALA B N 3756 C CA . ALA B 100 ? 0.0839 0.0722 0.0803 -0.0005 -0.0065 0.0065 180 ALA B CA 3757 C C . ALA B 100 ? 0.1289 0.1173 0.1247 -0.0009 -0.0062 0.0060 180 ALA B C 3758 O O . ALA B 100 ? 0.0925 0.0810 0.0879 -0.0010 -0.0060 0.0064 180 ALA B O 3759 C CB . ALA B 100 ? 0.0800 0.0669 0.0772 -0.0003 -0.0063 0.0063 180 ALA B CB 3760 N N . SER B 101 ? 0.1030 0.0910 0.0986 -0.0012 -0.0060 0.0051 181 SER B N 3761 C CA . SER B 101 ? 0.1186 0.1063 0.1138 -0.0014 -0.0056 0.0045 181 SER B CA 3762 C C . SER B 101 ? 0.1135 0.1001 0.1088 -0.0014 -0.0054 0.0038 181 SER B C 3763 O O . SER B 101 ? 0.1160 0.1025 0.1117 -0.0013 -0.0056 0.0037 181 SER B O 3764 C CB . SER B 101 ? 0.1331 0.1218 0.1273 -0.0019 -0.0056 0.0041 181 SER B CB 3765 O OG . SER B 101 ? 0.1331 0.1213 0.1269 -0.0021 -0.0051 0.0034 181 SER B OG 3766 N N . ALA B 102 ? 0.0407 0.0267 0.0358 -0.0013 -0.0049 0.0034 182 ALA B N 3767 C CA . ALA B 102 ? 0.0343 0.0194 0.0296 -0.0011 -0.0046 0.0030 182 ALA B CA 3768 C C . ALA B 102 ? 0.0823 0.0669 0.0772 -0.0010 -0.0040 0.0026 182 ALA B C 3769 O O . ALA B 102 ? 0.0995 0.0846 0.0943 -0.0010 -0.0039 0.0027 182 ALA B O 3770 C CB . ALA B 102 ? 0.0558 0.0405 0.0519 -0.0007 -0.0048 0.0033 182 ALA B CB 3771 N N . CYS B 103 ? 0.0734 0.0571 0.0682 -0.0009 -0.0036 0.0021 183 CYS B N 3772 C CA . CYS B 103 ? 0.0993 0.0823 0.0938 -0.0007 -0.0029 0.0017 183 CYS B CA 3773 C C . CYS B 103 ? 0.1454 0.1270 0.1399 -0.0004 -0.0024 0.0015 183 CYS B C 3774 O O . CYS B 103 ? 0.1395 0.1208 0.1341 -0.0007 -0.0025 0.0014 183 CYS B O 3775 C CB . CYS B 103 ? 0.1166 0.1000 0.1104 -0.0012 -0.0026 0.0012 183 CYS B CB 3776 S SG . CYS B 103 ? 0.1671 0.1507 0.1603 -0.0021 -0.0026 0.0005 183 CYS B SG 3777 N N . HIS B 104 ? 0.0690 0.0499 0.0634 0.0002 -0.0017 0.0015 184 HIS B N 3778 C CA . HIS B 104 ? 0.0922 0.0718 0.0867 0.0006 -0.0011 0.0015 184 HIS B CA 3779 C C . HIS B 104 ? 0.0969 0.0752 0.0908 0.0005 -0.0002 0.0008 184 HIS B C 3780 O O . HIS B 104 ? 0.1451 0.1236 0.1388 0.0007 0.0002 0.0006 184 HIS B O 3781 C CB . HIS B 104 ? 0.0620 0.0418 0.0570 0.0017 -0.0011 0.0022 184 HIS B CB 3782 C CG . HIS B 104 ? 0.0925 0.0714 0.0876 0.0022 -0.0007 0.0025 184 HIS B CG 3783 N ND1 . HIS B 104 ? 0.0802 0.0575 0.0750 0.0027 0.0003 0.0025 184 HIS B ND1 3784 C CD2 . HIS B 104 ? 0.0803 0.0596 0.0758 0.0024 -0.0011 0.0030 184 HIS B CD2 3785 C CE1 . HIS B 104 ? 0.0970 0.0737 0.0920 0.0031 0.0004 0.0030 184 HIS B CE1 3786 N NE2 . HIS B 104 ? 0.0729 0.0510 0.0683 0.0030 -0.0004 0.0033 184 HIS B NE2 3787 N N . ASP B 105 ? 0.0895 0.0665 0.0832 0.0001 0.0003 0.0004 185 ASP B N 3788 C CA . ASP B 105 ? 0.1229 0.0984 0.1161 -0.0003 0.0014 -0.0005 185 ASP B CA 3789 C C . ASP B 105 ? 0.1340 0.1077 0.1272 0.0008 0.0024 -0.0002 185 ASP B C 3790 O O . ASP B 105 ? 0.1462 0.1182 0.1390 0.0006 0.0035 -0.0009 185 ASP B O 3791 C CB . ASP B 105 ? 0.1369 0.1118 0.1297 -0.0014 0.0016 -0.0013 185 ASP B CB 3792 C CG . ASP B 105 ? 0.1352 0.1090 0.1284 -0.0013 0.0018 -0.0009 185 ASP B CG 3793 O OD1 . ASP B 105 ? 0.1494 0.1229 0.1429 -0.0003 0.0017 0.0001 185 ASP B OD1 3794 O OD2 . ASP B 105 ? 0.1468 0.1200 0.1398 -0.0023 0.0021 -0.0015 185 ASP B OD2 3795 N N . GLY B 106 ? 0.1231 0.0973 0.1169 0.0018 0.0021 0.0008 186 GLY B N 3796 C CA . GLY B 106 ? 0.1633 0.1361 0.1572 0.0030 0.0030 0.0014 186 GLY B CA 3797 C C . GLY B 106 ? 0.1793 0.1512 0.1733 0.0033 0.0032 0.0021 186 GLY B C 3798 O O . GLY B 106 ? 0.1964 0.1679 0.1907 0.0045 0.0036 0.0030 186 GLY B O 3799 N N . ILE B 107 ? 0.1302 0.1020 0.1241 0.0022 0.0028 0.0017 187 ILE B N 3800 C CA . ILE B 107 ? 0.1526 0.1237 0.1466 0.0022 0.0030 0.0022 187 ILE B CA 3801 C C . ILE B 107 ? 0.1470 0.1200 0.1414 0.0020 0.0017 0.0026 187 ILE B C 3802 O O . ILE B 107 ? 0.1343 0.1078 0.1290 0.0028 0.0015 0.0034 187 ILE B O 3803 C CB . ILE B 107 ? 0.1599 0.1292 0.1536 0.0011 0.0037 0.0014 187 ILE B CB 3804 C CG1 . ILE B 107 ? 0.2320 0.1992 0.2252 0.0010 0.0050 0.0007 187 ILE B CG1 3805 C CG2 . ILE B 107 ? 0.1446 0.1130 0.1384 0.0012 0.0040 0.0020 187 ILE B CG2 3806 C CD1 . ILE B 107 ? 0.2435 0.2092 0.2368 0.0025 0.0060 0.0016 187 ILE B CD1 3807 N N . ASN B 108 ? 0.0913 0.0655 0.0857 0.0010 0.0010 0.0019 188 ASN B N 3808 C CA . ASN B 108 ? 0.0715 0.0473 0.0663 0.0008 -0.0001 0.0022 188 ASN B CA 3809 C C . ASN B 108 ? 0.0877 0.0651 0.0826 0.0004 -0.0009 0.0020 188 ASN B C 3810 O O . ASN B 108 ? 0.0762 0.0535 0.0707 0.0001 -0.0007 0.0015 188 ASN B O 3811 C CB . ASN B 108 ? 0.0744 0.0499 0.0692 0.0000 -0.0001 0.0020 188 ASN B CB 3812 C CG . ASN B 108 ? 0.1418 0.1161 0.1366 0.0004 0.0006 0.0025 188 ASN B CG 3813 O OD1 . ASN B 108 ? 0.2626 0.2354 0.2571 -0.0001 0.0014 0.0022 188 ASN B OD1 3814 N ND2 . ASN B 108 ? 0.1151 0.0900 0.1102 0.0014 0.0003 0.0034 188 ASN B ND2 3815 N N . TRP B 109 ? 0.1122 0.0909 0.1075 0.0005 -0.0017 0.0023 189 TRP B N 3816 C CA . TRP B 109 ? 0.1090 0.0890 0.1045 0.0002 -0.0024 0.0022 189 TRP B CA 3817 C C . TRP B 109 ? 0.1024 0.0828 0.0978 -0.0007 -0.0027 0.0018 189 TRP B C 3818 O O . TRP B 109 ? 0.0944 0.0746 0.0898 -0.0011 -0.0028 0.0017 189 TRP B O 3819 C CB . TRP B 109 ? 0.0775 0.0586 0.0736 0.0005 -0.0031 0.0027 189 TRP B CB 3820 C CG . TRP B 109 ? 0.0944 0.0759 0.0907 0.0012 -0.0030 0.0031 189 TRP B CG 3821 C CD1 . TRP B 109 ? 0.1212 0.1028 0.1177 0.0019 -0.0029 0.0035 189 TRP B CD1 3822 C CD2 . TRP B 109 ? 0.0984 0.0805 0.0947 0.0013 -0.0031 0.0031 189 TRP B CD2 3823 N NE1 . TRP B 109 ? 0.1116 0.0940 0.1083 0.0024 -0.0029 0.0037 189 TRP B NE1 3824 C CE2 . TRP B 109 ? 0.0902 0.0729 0.0868 0.0020 -0.0030 0.0034 189 TRP B CE2 3825 C CE3 . TRP B 109 ? 0.0749 0.0573 0.0710 0.0008 -0.0032 0.0029 189 TRP B CE3 3826 C CZ2 . TRP B 109 ? 0.1845 0.1681 0.1813 0.0022 -0.0030 0.0035 189 TRP B CZ2 3827 C CZ3 . TRP B 109 ? 0.0742 0.0572 0.0703 0.0010 -0.0032 0.0030 189 TRP B CZ3 3828 C CH2 . TRP B 109 ? 0.1065 0.0901 0.1030 0.0017 -0.0031 0.0033 189 TRP B CH2 3829 N N . LEU B 110 ? 0.1080 0.0891 0.1030 -0.0011 -0.0029 0.0015 190 LEU B N 3830 C CA . LEU B 110 ? 0.1019 0.0840 0.0968 -0.0018 -0.0034 0.0012 190 LEU B CA 3831 C C . LEU B 110 ? 0.0842 0.0675 0.0795 -0.0016 -0.0041 0.0018 190 LEU B C 3832 O O . LEU B 110 ? 0.0850 0.0685 0.0803 -0.0013 -0.0041 0.0021 190 LEU B O 3833 C CB . LEU B 110 ? 0.1137 0.0960 0.1080 -0.0025 -0.0030 0.0005 190 LEU B CB 3834 C CG . LEU B 110 ? 0.1044 0.0884 0.0986 -0.0031 -0.0036 0.0004 190 LEU B CG 3835 C CD1 . LEU B 110 ? 0.0931 0.0776 0.0875 -0.0036 -0.0038 0.0002 190 LEU B CD1 3836 C CD2 . LEU B 110 ? 0.1191 0.1035 0.1125 -0.0037 -0.0033 -0.0003 190 LEU B CD2 3837 N N . THR B 111 ? 0.0906 0.0747 0.0864 -0.0017 -0.0046 0.0021 191 THR B N 3838 C CA . THR B 111 ? 0.0673 0.0523 0.0634 -0.0014 -0.0052 0.0026 191 THR B CA 3839 C C . THR B 111 ? 0.0985 0.0848 0.0945 -0.0018 -0.0055 0.0027 191 THR B C 3840 O O . THR B 111 ? 0.0727 0.0594 0.0688 -0.0022 -0.0055 0.0023 191 THR B O 3841 C CB . THR B 111 ? 0.1164 0.1011 0.1132 -0.0009 -0.0054 0.0030 191 THR B CB 3842 O OG1 . THR B 111 ? 0.1143 0.0990 0.1113 -0.0010 -0.0055 0.0029 191 THR B OG1 3843 C CG2 . THR B 111 ? 0.0848 0.0687 0.0817 -0.0005 -0.0051 0.0031 191 THR B CG2 3844 N N . ILE B 112 ? 0.0727 0.0598 0.0686 -0.0017 -0.0058 0.0031 192 ILE B N 3845 C CA . ILE B 112 ? 0.0848 0.0735 0.0807 -0.0019 -0.0063 0.0034 192 ILE B CA 3846 C C . ILE B 112 ? 0.0765 0.0654 0.0729 -0.0012 -0.0066 0.0043 192 ILE B C 3847 O O . ILE B 112 ? 0.1147 0.1032 0.1111 -0.0010 -0.0066 0.0048 192 ILE B O 3848 C CB . ILE B 112 ? 0.1010 0.0908 0.0961 -0.0023 -0.0062 0.0032 192 ILE B CB 3849 C CG1 . ILE B 112 ? 0.1310 0.1203 0.1255 -0.0030 -0.0057 0.0021 192 ILE B CG1 3850 C CG2 . ILE B 112 ? 0.1047 0.0965 0.0997 -0.0024 -0.0067 0.0036 192 ILE B CG2 3851 C CD1 . ILE B 112 ? 0.1506 0.1408 0.1443 -0.0035 -0.0055 0.0017 192 ILE B CD1 3852 N N . GLY B 113 ? 0.0835 0.0730 0.0806 -0.0010 -0.0069 0.0046 193 GLY B N 3853 C CA . GLY B 113 ? 0.0617 0.0511 0.0594 -0.0003 -0.0071 0.0054 193 GLY B CA 3854 C C . GLY B 113 ? 0.0924 0.0836 0.0903 0.0000 -0.0075 0.0060 193 GLY B C 3855 O O . GLY B 113 ? 0.0765 0.0687 0.0746 -0.0002 -0.0077 0.0056 193 GLY B O 3856 N N . ILE B 114 ? 0.0473 0.0390 0.0451 0.0004 -0.0076 0.0069 194 ILE B N 3857 C CA . ILE B 114 ? 0.0638 0.0573 0.0617 0.0008 -0.0079 0.0077 194 ILE B CA 3858 C C . ILE B 114 ? 0.0743 0.0671 0.0731 0.0018 -0.0079 0.0086 194 ILE B C 3859 O O . ILE B 114 ? 0.0708 0.0620 0.0699 0.0021 -0.0076 0.0091 194 ILE B O 3860 C CB . ILE B 114 ? 0.0727 0.0675 0.0699 0.0008 -0.0080 0.0084 194 ILE B CB 3861 C CG1 . ILE B 114 ? 0.0642 0.0596 0.0604 -0.0002 -0.0080 0.0074 194 ILE B CG1 3862 C CG2 . ILE B 114 ? 0.1039 0.1010 0.1012 0.0014 -0.0084 0.0094 194 ILE B CG2 3863 C CD1 . ILE B 114 ? 0.0750 0.0716 0.0704 -0.0004 -0.0080 0.0079 194 ILE B CD1 3864 N N . SER B 115 ? 0.0658 0.0600 0.0652 0.0022 -0.0082 0.0087 195 SER B N 3865 C CA . SER B 115 ? 0.0998 0.0935 0.1001 0.0032 -0.0081 0.0096 195 SER B CA 3866 C C . SER B 115 ? 0.0822 0.0785 0.0829 0.0038 -0.0085 0.0103 195 SER B C 3867 O O . SER B 115 ? 0.1187 0.1172 0.1187 0.0033 -0.0088 0.0101 195 SER B O 3868 C CB . SER B 115 ? 0.1072 0.0994 0.1083 0.0032 -0.0078 0.0088 195 SER B CB 3869 O OG . SER B 115 ? 0.1047 0.0959 0.1066 0.0042 -0.0076 0.0095 195 SER B OG 3870 N N . GLY B 116 ? 0.0945 0.0906 0.0960 0.0049 -0.0084 0.0111 196 GLY B N 3871 C CA . GLY B 116 ? 0.1236 0.1224 0.1255 0.0057 -0.0087 0.0119 196 GLY B CA 3872 C C . GLY B 116 ? 0.1520 0.1512 0.1538 0.0067 -0.0086 0.0136 196 GLY B C 3873 O O . GLY B 116 ? 0.1204 0.1175 0.1218 0.0067 -0.0083 0.0141 196 GLY B O 3874 N N . PRO B 117 ? 0.1253 0.1273 0.1274 0.0076 -0.0090 0.0146 197 PRO B N 3875 C CA . PRO B 117 ? 0.1250 0.1277 0.1271 0.0088 -0.0089 0.0164 197 PRO B CA 3876 C C . PRO B 117 ? 0.1281 0.1321 0.1290 0.0082 -0.0091 0.0169 197 PRO B C 3877 O O . PRO B 117 ? 0.0984 0.1038 0.0985 0.0070 -0.0095 0.0157 197 PRO B O 3878 C CB . PRO B 117 ? 0.1073 0.1133 0.1101 0.0098 -0.0093 0.0171 197 PRO B CB 3879 C CG . PRO B 117 ? 0.1504 0.1585 0.1530 0.0085 -0.0098 0.0155 197 PRO B CG 3880 C CD . PRO B 117 ? 0.0784 0.0833 0.0808 0.0074 -0.0095 0.0140 197 PRO B CD 3881 N N . ASP B 118 ? 0.1601 0.1636 0.1608 0.0091 -0.0088 0.0185 198 ASP B N 3882 C CA . ASP B 118 ? 0.2305 0.2353 0.2300 0.0087 -0.0090 0.0191 198 ASP B CA 3883 C C . ASP B 118 ? 0.1772 0.1865 0.1761 0.0084 -0.0097 0.0190 198 ASP B C 3884 O O . ASP B 118 ? 0.2008 0.2113 0.1986 0.0074 -0.0099 0.0186 198 ASP B O 3885 C CB . ASP B 118 ? 0.1879 0.1916 0.1875 0.0099 -0.0085 0.0212 198 ASP B CB 3886 C CG . ASP B 118 ? 0.2225 0.2218 0.2224 0.0097 -0.0077 0.0211 198 ASP B CG 3887 O OD1 . ASP B 118 ? 0.2358 0.2332 0.2357 0.0087 -0.0076 0.0195 198 ASP B OD1 3888 O OD2 . ASP B 118 ? 0.2844 0.2822 0.2843 0.0106 -0.0071 0.0228 198 ASP B OD2 3889 N N . ASN B 119 ? 0.1213 0.1331 0.1209 0.0091 -0.0101 0.0193 199 ASN B N 3890 C CA . ASN B 119 ? 0.1789 0.1955 0.1780 0.0089 -0.0108 0.0193 199 ASN B CA 3891 C C . ASN B 119 ? 0.2094 0.2275 0.2085 0.0074 -0.0112 0.0172 199 ASN B C 3892 O O . ASN B 119 ? 0.1777 0.1998 0.1766 0.0070 -0.0118 0.0169 199 ASN B O 3893 C CB . ASN B 119 ? 0.1963 0.2156 0.1961 0.0107 -0.0111 0.0211 199 ASN B CB 3894 C CG . ASN B 119 ? 0.3440 0.3630 0.3453 0.0113 -0.0110 0.0207 199 ASN B CG 3895 O OD1 . ASN B 119 ? 0.1762 0.1927 0.1779 0.0105 -0.0108 0.0192 199 ASN B OD1 3896 N ND2 . ASN B 119 ? 0.3160 0.3378 0.3181 0.0129 -0.0112 0.0222 199 ASN B ND2 3897 N N . GLY B 120 ? 0.1450 0.1598 0.1443 0.0065 -0.0109 0.0157 200 GLY B N 3898 C CA . GLY B 120 ? 0.1747 0.1903 0.1740 0.0051 -0.0111 0.0138 200 GLY B CA 3899 C C . GLY B 120 ? 0.1057 0.1175 0.1050 0.0043 -0.0106 0.0125 200 GLY B C 3900 O O . GLY B 120 ? 0.0960 0.1072 0.0959 0.0039 -0.0105 0.0114 200 GLY B O 3901 N N . ALA B 121 ? 0.0882 0.0975 0.0870 0.0040 -0.0102 0.0125 201 ALA B N 3902 C CA . ALA B 121 ? 0.0915 0.0972 0.0902 0.0033 -0.0098 0.0115 201 ALA B CA 3903 C C . ALA B 121 ? 0.0956 0.1018 0.0939 0.0019 -0.0098 0.0097 201 ALA B C 3904 O O . ALA B 121 ? 0.0824 0.0911 0.0800 0.0011 -0.0101 0.0092 201 ALA B O 3905 C CB . ALA B 121 ? 0.0731 0.0766 0.0712 0.0033 -0.0094 0.0120 201 ALA B CB 3906 N N . VAL B 122 ? 0.0781 0.0818 0.0768 0.0015 -0.0095 0.0088 202 VAL B N 3907 C CA . VAL B 122 ? 0.0550 0.0586 0.0533 0.0003 -0.0094 0.0072 202 VAL B CA 3908 C C . VAL B 122 ? 0.0653 0.0658 0.0633 -0.0002 -0.0089 0.0066 202 VAL B C 3909 O O . VAL B 122 ? 0.0801 0.0784 0.0786 0.0004 -0.0087 0.0068 202 VAL B O 3910 C CB . VAL B 122 ? 0.0878 0.0920 0.0869 0.0002 -0.0094 0.0067 202 VAL B CB 3911 C CG1 . VAL B 122 ? 0.0766 0.0799 0.0753 -0.0011 -0.0091 0.0052 202 VAL B CG1 3912 C CG2 . VAL B 122 ? 0.0652 0.0731 0.0647 0.0004 -0.0099 0.0071 202 VAL B CG2 3913 N N . ALA B 123 ? 0.1097 0.1101 0.1068 -0.0011 -0.0087 0.0057 203 ALA B N 3914 C CA . ALA B 123 ? 0.0722 0.0700 0.0689 -0.0015 -0.0082 0.0051 203 ALA B CA 3915 C C . ALA B 123 ? 0.0847 0.0816 0.0817 -0.0021 -0.0080 0.0040 203 ALA B C 3916 O O . ALA B 123 ? 0.0842 0.0824 0.0810 -0.0029 -0.0079 0.0032 203 ALA B O 3917 C CB . ALA B 123 ? 0.0724 0.0705 0.0682 -0.0022 -0.0080 0.0046 203 ALA B CB 3918 N N . VAL B 124 ? 0.0584 0.0532 0.0559 -0.0017 -0.0077 0.0041 204 VAL B N 3919 C CA . VAL B 124 ? 0.0725 0.0662 0.0701 -0.0021 -0.0074 0.0033 204 VAL B CA 3920 C C . VAL B 124 ? 0.0590 0.0507 0.0561 -0.0025 -0.0069 0.0027 204 VAL B C 3921 O O . VAL B 124 ? 0.0551 0.0455 0.0521 -0.0020 -0.0068 0.0031 204 VAL B O 3922 C CB . VAL B 124 ? 0.0532 0.0461 0.0517 -0.0014 -0.0074 0.0037 204 VAL B CB 3923 C CG1 . VAL B 124 ? 0.0988 0.0906 0.0974 -0.0018 -0.0070 0.0030 204 VAL B CG1 3924 C CG2 . VAL B 124 ? 0.0376 0.0325 0.0367 -0.0010 -0.0079 0.0042 204 VAL B CG2 3925 N N . LEU B 125 ? 0.0548 0.0464 0.0514 -0.0034 -0.0065 0.0018 205 LEU B N 3926 C CA . LEU B 125 ? 0.0656 0.0553 0.0617 -0.0036 -0.0059 0.0013 205 LEU B CA 3927 C C . LEU B 125 ? 0.0708 0.0589 0.0672 -0.0035 -0.0055 0.0012 205 LEU B C 3928 O O . LEU B 125 ? 0.0806 0.0692 0.0773 -0.0039 -0.0054 0.0009 205 LEU B O 3929 C CB . LEU B 125 ? 0.0704 0.0605 0.0658 -0.0046 -0.0055 0.0004 205 LEU B CB 3930 C CG . LEU B 125 ? 0.1114 0.1029 0.1062 -0.0047 -0.0057 0.0004 205 LEU B CG 3931 C CD1 . LEU B 125 ? 0.1196 0.1136 0.1147 -0.0046 -0.0064 0.0010 205 LEU B CD1 3932 C CD2 . LEU B 125 ? 0.0767 0.0681 0.0708 -0.0058 -0.0051 -0.0008 205 LEU B CD2 3933 N N . LYS B 126 ? 0.0570 0.0436 0.0534 -0.0030 -0.0052 0.0014 206 LYS B N 3934 C CA . LYS B 126 ? 0.0917 0.0769 0.0883 -0.0027 -0.0048 0.0014 206 LYS B CA 3935 C C . LYS B 126 ? 0.0744 0.0580 0.0705 -0.0027 -0.0041 0.0011 206 LYS B C 3936 O O . LYS B 126 ? 0.0835 0.0668 0.0792 -0.0025 -0.0041 0.0012 206 LYS B O 3937 C CB . LYS B 126 ? 0.0836 0.0687 0.0808 -0.0019 -0.0051 0.0020 206 LYS B CB 3938 C CG . LYS B 126 ? 0.0906 0.0769 0.0884 -0.0018 -0.0056 0.0023 206 LYS B CG 3939 C CD . LYS B 126 ? 0.1498 0.1357 0.1481 -0.0010 -0.0058 0.0027 206 LYS B CD 3940 C CE . LYS B 126 ? 0.1535 0.1405 0.1526 -0.0008 -0.0062 0.0030 206 LYS B CE 3941 N NZ . LYS B 126 ? 0.1210 0.1075 0.1206 -0.0002 -0.0062 0.0032 206 LYS B NZ 3942 N N . TYR B 127 ? 0.0637 0.0462 0.0596 -0.0030 -0.0035 0.0009 207 TYR B N 3943 C CA . TYR B 127 ? 0.0562 0.0370 0.0517 -0.0028 -0.0027 0.0008 207 TYR B CA 3944 C C . TYR B 127 ? 0.0659 0.0459 0.0617 -0.0022 -0.0025 0.0013 207 TYR B C 3945 O O . TYR B 127 ? 0.0835 0.0634 0.0795 -0.0025 -0.0023 0.0013 207 TYR B O 3946 C CB . TYR B 127 ? 0.0698 0.0498 0.0649 -0.0037 -0.0020 -0.0001 207 TYR B CB 3947 C CG . TYR B 127 ? 0.1082 0.0862 0.1028 -0.0035 -0.0010 -0.0003 207 TYR B CG 3948 C CD1 . TYR B 127 ? 0.1226 0.1006 0.1169 -0.0031 -0.0010 -0.0003 207 TYR B CD1 3949 C CD2 . TYR B 127 ? 0.1229 0.0991 0.1174 -0.0036 -0.0001 -0.0004 207 TYR B CD2 3950 C CE1 . TYR B 127 ? 0.1016 0.0779 0.0955 -0.0028 -0.0001 -0.0005 207 TYR B CE1 3951 C CE2 . TYR B 127 ? 0.1518 0.1261 0.1459 -0.0033 0.0009 -0.0005 207 TYR B CE2 3952 C CZ . TYR B 127 ? 0.1343 0.1087 0.1282 -0.0028 0.0009 -0.0005 207 TYR B CZ 3953 O OH . TYR B 127 ? 0.1129 0.0854 0.1065 -0.0023 0.0019 -0.0006 207 TYR B OH 3954 N N . ASN B 128 ? 0.0669 0.0465 0.0628 -0.0013 -0.0025 0.0018 208 ASN B N 3955 C CA . ASN B 128 ? 0.1175 0.0968 0.1136 -0.0006 -0.0024 0.0024 208 ASN B CA 3956 C C . ASN B 128 ? 0.1103 0.0908 0.1069 -0.0007 -0.0030 0.0026 208 ASN B C 3957 O O . ASN B 128 ? 0.1363 0.1167 0.1331 -0.0005 -0.0028 0.0028 208 ASN B O 3958 C CB . ASN B 128 ? 0.1264 0.1042 0.1222 -0.0006 -0.0014 0.0025 208 ASN B CB 3959 C CG . ASN B 128 ? 0.2399 0.2175 0.2358 0.0003 -0.0012 0.0033 208 ASN B CG 3960 O OD1 . ASN B 128 ? 0.1808 0.1593 0.1769 0.0010 -0.0016 0.0037 208 ASN B OD1 3961 N ND2 . ASN B 128 ? 0.2465 0.2231 0.2422 0.0003 -0.0006 0.0036 208 ASN B ND2 3962 N N . GLY B 129 ? 0.1226 0.1042 0.1195 -0.0008 -0.0037 0.0025 209 GLY B N 3963 C CA . GLY B 129 ? 0.1467 0.1294 0.1442 -0.0007 -0.0042 0.0026 209 GLY B CA 3964 C C . GLY B 129 ? 0.1531 0.1364 0.1508 -0.0013 -0.0043 0.0023 209 GLY B C 3965 O O . GLY B 129 ? 0.1771 0.1613 0.1753 -0.0011 -0.0047 0.0024 209 GLY B O 3966 N N . ILE B 130 ? 0.0636 0.0464 0.0609 -0.0019 -0.0038 0.0019 210 ILE B N 3967 C CA . ILE B 130 ? 0.0783 0.0618 0.0758 -0.0027 -0.0038 0.0015 210 ILE B CA 3968 C C . ILE B 130 ? 0.0931 0.0778 0.0905 -0.0032 -0.0042 0.0011 210 ILE B C 3969 O O . ILE B 130 ? 0.0899 0.0741 0.0868 -0.0035 -0.0039 0.0008 210 ILE B O 3970 C CB . ILE B 130 ? 0.1469 0.1292 0.1440 -0.0032 -0.0030 0.0013 210 ILE B CB 3971 C CG1 . ILE B 130 ? 0.1432 0.1245 0.1402 -0.0025 -0.0026 0.0019 210 ILE B CG1 3972 C CG2 . ILE B 130 ? 0.1096 0.0930 0.1070 -0.0041 -0.0029 0.0008 210 ILE B CG2 3973 C CD1 . ILE B 130 ? 0.1301 0.1127 0.1278 -0.0022 -0.0030 0.0022 210 ILE B CD1 3974 N N . ILE B 131 ? 0.0933 0.0797 0.0912 -0.0034 -0.0047 0.0011 211 ILE B N 3975 C CA . ILE B 131 ? 0.1038 0.0918 0.1016 -0.0038 -0.0050 0.0009 211 ILE B CA 3976 C C . ILE B 131 ? 0.0905 0.0783 0.0878 -0.0050 -0.0045 0.0000 211 ILE B C 3977 O O . ILE B 131 ? 0.1499 0.1375 0.1474 -0.0056 -0.0041 -0.0004 211 ILE B O 3978 C CB . ILE B 131 ? 0.1185 0.1084 0.1170 -0.0036 -0.0056 0.0011 211 ILE B CB 3979 C CG1 . ILE B 131 ? 0.0697 0.0596 0.0687 -0.0026 -0.0061 0.0018 211 ILE B CG1 3980 C CG2 . ILE B 131 ? 0.0790 0.0710 0.0774 -0.0042 -0.0060 0.0008 211 ILE B CG2 3981 C CD1 . ILE B 131 ? 0.1263 0.1179 0.1260 -0.0021 -0.0066 0.0022 211 ILE B CD1 3982 N N . THR B 132 ? 0.1064 0.0944 0.1032 -0.0054 -0.0045 -0.0004 212 THR B N 3983 C CA . THR B 132 ? 0.1258 0.1135 0.1220 -0.0065 -0.0038 -0.0014 212 THR B CA 3984 C C . THR B 132 ? 0.1376 0.1277 0.1336 -0.0073 -0.0042 -0.0019 212 THR B C 3985 O O . THR B 132 ? 0.1340 0.1245 0.1298 -0.0085 -0.0038 -0.0029 212 THR B O 3986 C CB . THR B 132 ? 0.1021 0.0876 0.0977 -0.0064 -0.0031 -0.0016 212 THR B CB 3987 O OG1 . THR B 132 ? 0.0863 0.0720 0.0818 -0.0056 -0.0036 -0.0010 212 THR B OG1 3988 C CG2 . THR B 132 ? 0.1285 0.1117 0.1242 -0.0059 -0.0025 -0.0012 212 THR B CG2 3989 N N . ASP B 133 ? 0.1084 0.1002 0.1047 -0.0066 -0.0050 -0.0012 213 ASP B N 3990 C CA . ASP B 133 ? 0.1298 0.1242 0.1259 -0.0071 -0.0055 -0.0015 213 ASP B CA 3991 C C . ASP B 133 ? 0.1126 0.1086 0.1090 -0.0060 -0.0063 -0.0004 213 ASP B C 3992 O O . ASP B 133 ? 0.0974 0.0920 0.0941 -0.0050 -0.0065 0.0005 213 ASP B O 3993 C CB . ASP B 133 ? 0.1223 0.1162 0.1175 -0.0078 -0.0051 -0.0023 213 ASP B CB 3994 C CG . ASP B 133 ? 0.1816 0.1781 0.1764 -0.0090 -0.0052 -0.0032 213 ASP B CG 3995 O OD1 . ASP B 133 ? 0.1689 0.1681 0.1642 -0.0091 -0.0057 -0.0031 213 ASP B OD1 3996 O OD2 . ASP B 133 ? 0.1818 0.1779 0.1758 -0.0098 -0.0046 -0.0042 213 ASP B OD2 3997 N N . THR B 134 ? 0.0862 0.0850 0.0826 -0.0063 -0.0068 -0.0004 214 THR B N 3998 C CA . THR B 134 ? 0.1060 0.1064 0.1027 -0.0053 -0.0075 0.0008 214 THR B CA 3999 C C . THR B 134 ? 0.1522 0.1551 0.1482 -0.0058 -0.0078 0.0006 214 THR B C 4000 O O . THR B 134 ? 0.1585 0.1627 0.1541 -0.0070 -0.0076 -0.0005 214 THR B O 4001 C CB . THR B 134 ? 0.1165 0.1184 0.1142 -0.0046 -0.0080 0.0015 214 THR B CB 4002 O OG1 . THR B 134 ? 0.1526 0.1574 0.1504 -0.0054 -0.0082 0.0008 214 THR B OG1 4003 C CG2 . THR B 134 ? 0.1094 0.1092 0.1077 -0.0042 -0.0077 0.0016 214 THR B CG2 4004 N N . ILE B 135 ? 0.1081 0.1117 0.1040 -0.0049 -0.0082 0.0017 215 ILE B N 4005 C CA . ILE B 135 ? 0.1620 0.1684 0.1572 -0.0052 -0.0086 0.0018 215 ILE B CA 4006 C C . ILE B 135 ? 0.1603 0.1681 0.1559 -0.0038 -0.0092 0.0034 215 ILE B C 4007 O O . ILE B 135 ? 0.1478 0.1537 0.1438 -0.0028 -0.0091 0.0044 215 ILE B O 4008 C CB . ILE B 135 ? 0.2222 0.2276 0.2164 -0.0057 -0.0082 0.0013 215 ILE B CB 4009 C CG1 . ILE B 135 ? 0.2384 0.2471 0.2318 -0.0061 -0.0085 0.0013 215 ILE B CG1 4010 C CG2 . ILE B 135 ? 0.2230 0.2258 0.2172 -0.0047 -0.0080 0.0022 215 ILE B CG2 4011 C CD1 . ILE B 135 ? 0.2468 0.2564 0.2402 -0.0049 -0.0090 0.0029 215 ILE B CD1 4012 N N . LYS B 136 ? 0.1170 0.1284 0.1127 -0.0038 -0.0097 0.0037 216 LYS B N 4013 C CA . LYS B 136 ? 0.1200 0.1330 0.1163 -0.0024 -0.0102 0.0054 216 LYS B CA 4014 C C . LYS B 136 ? 0.1240 0.1390 0.1195 -0.0021 -0.0105 0.0063 216 LYS B C 4015 O O . LYS B 136 ? 0.1205 0.1373 0.1150 -0.0032 -0.0105 0.0054 216 LYS B O 4016 C CB . LYS B 136 ? 0.1315 0.1473 0.1286 -0.0023 -0.0106 0.0055 216 LYS B CB 4017 C CG . LYS B 136 ? 0.1464 0.1636 0.1443 -0.0006 -0.0110 0.0073 216 LYS B CG 4018 C CD . LYS B 136 ? 0.1913 0.2106 0.1902 -0.0003 -0.0113 0.0073 216 LYS B CD 4019 C CE . LYS B 136 ? 0.2067 0.2268 0.2065 0.0016 -0.0115 0.0091 216 LYS B CE 4020 N NZ . LYS B 136 ? 0.2471 0.2694 0.2480 0.0020 -0.0117 0.0091 216 LYS B NZ 4021 N N . SER B 137 ? 0.1025 0.1172 0.0983 -0.0007 -0.0106 0.0080 217 SER B N 4022 C CA . SER B 137 ? 0.1022 0.1188 0.0973 -0.0002 -0.0109 0.0092 217 SER B CA 4023 C C . SER B 137 ? 0.1360 0.1572 0.1306 -0.0008 -0.0113 0.0089 217 SER B C 4024 O O . SER B 137 ? 0.1015 0.1252 0.0968 -0.0008 -0.0117 0.0087 217 SER B O 4025 C CB . SER B 137 ? 0.0938 0.1099 0.0896 0.0016 -0.0109 0.0113 217 SER B CB 4026 O OG . SER B 137 ? 0.1065 0.1243 0.1016 0.0022 -0.0111 0.0127 217 SER B OG 4027 N N . TRP B 138 ? 0.1150 0.1377 0.1084 -0.0015 -0.0114 0.0086 218 TRP B N 4028 C CA . TRP B 138 ? 0.1070 0.1344 0.0998 -0.0022 -0.0118 0.0081 218 TRP B CA 4029 C C . TRP B 138 ? 0.1135 0.1439 0.1058 -0.0011 -0.0123 0.0100 218 TRP B C 4030 O O . TRP B 138 ? 0.1524 0.1875 0.1443 -0.0014 -0.0128 0.0100 218 TRP B O 4031 C CB . TRP B 138 ? 0.1157 0.1431 0.1074 -0.0040 -0.0115 0.0060 218 TRP B CB 4032 C CG . TRP B 138 ? 0.1123 0.1378 0.1030 -0.0041 -0.0111 0.0062 218 TRP B CG 4033 C CD1 . TRP B 138 ? 0.1626 0.1907 0.1522 -0.0041 -0.0112 0.0068 218 TRP B CD1 4034 C CD2 . TRP B 138 ? 0.1332 0.1542 0.1239 -0.0041 -0.0104 0.0059 218 TRP B CD2 4035 N NE1 . TRP B 138 ? 0.1487 0.1740 0.1377 -0.0042 -0.0107 0.0068 218 TRP B NE1 4036 C CE2 . TRP B 138 ? 0.1422 0.1632 0.1318 -0.0042 -0.0102 0.0062 218 TRP B CE2 4037 C CE3 . TRP B 138 ? 0.1430 0.1601 0.1345 -0.0040 -0.0100 0.0054 218 TRP B CE3 4038 C CZ2 . TRP B 138 ? 0.1522 0.1696 0.1417 -0.0042 -0.0096 0.0061 218 TRP B CZ2 4039 C CZ3 . TRP B 138 ? 0.1192 0.1329 0.1105 -0.0040 -0.0095 0.0053 218 TRP B CZ3 4040 C CH2 . TRP B 138 ? 0.1013 0.1152 0.0916 -0.0041 -0.0093 0.0056 218 TRP B CH2 4041 N N . ARG B 139 ? 0.1034 0.1314 0.0957 0.0002 -0.0120 0.0117 219 ARG B N 4042 C CA . ARG B 139 ? 0.1554 0.1857 0.1474 0.0015 -0.0123 0.0139 219 ARG B CA 4043 C C . ARG B 139 ? 0.1537 0.1827 0.1469 0.0033 -0.0123 0.0159 219 ARG B C 4044 O O . ARG B 139 ? 0.1565 0.1871 0.1496 0.0047 -0.0124 0.0179 219 ARG B O 4045 C CB . ARG B 139 ? 0.1544 0.1833 0.1453 0.0013 -0.0119 0.0144 219 ARG B CB 4046 C CG . ARG B 139 ? 0.1506 0.1814 0.1402 -0.0003 -0.0119 0.0127 219 ARG B CG 4047 C CD . ARG B 139 ? 0.2731 0.3096 0.2619 -0.0004 -0.0126 0.0131 219 ARG B CD 4048 N NE . ARG B 139 ? 0.3261 0.3646 0.3137 -0.0020 -0.0125 0.0113 219 ARG B NE 4049 C CZ . ARG B 139 ? 0.3542 0.3937 0.3405 -0.0021 -0.0123 0.0119 219 ARG B CZ 4050 N NH1 . ARG B 139 ? 0.3450 0.3839 0.3312 -0.0006 -0.0123 0.0143 219 ARG B NH1 4051 N NH2 . ARG B 139 ? 0.3889 0.4301 0.3740 -0.0036 -0.0122 0.0100 219 ARG B NH2 4052 N N . ASN B 140 ? 0.1664 0.1925 0.1607 0.0034 -0.0121 0.0152 220 ASN B N 4053 C CA . ASN B 140 ? 0.1628 0.1874 0.1583 0.0051 -0.0119 0.0167 220 ASN B CA 4054 C C . ASN B 140 ? 0.1462 0.1682 0.1416 0.0063 -0.0115 0.0186 220 ASN B C 4055 O O . ASN B 140 ? 0.1510 0.1733 0.1471 0.0079 -0.0114 0.0205 220 ASN B O 4056 C CB . ASN B 140 ? 0.1862 0.2153 0.1823 0.0061 -0.0125 0.0178 220 ASN B CB 4057 C CG . ASN B 140 ? 0.2787 0.3106 0.2749 0.0048 -0.0130 0.0159 220 ASN B CG 4058 O OD1 . ASN B 140 ? 0.2847 0.3143 0.2811 0.0036 -0.0127 0.0141 220 ASN B OD1 4059 N ND2 . ASN B 140 ? 0.3893 0.4262 0.3856 0.0052 -0.0136 0.0165 220 ASN B ND2 4060 N N . ASN B 141 ? 0.1544 0.1737 0.1491 0.0054 -0.0110 0.0180 221 ASN B N 4061 C CA . ASN B 141 ? 0.1005 0.1172 0.0951 0.0063 -0.0105 0.0196 221 ASN B CA 4062 C C . ASN B 141 ? 0.1338 0.1463 0.1283 0.0054 -0.0099 0.0185 221 ASN B C 4063 O O . ASN B 141 ? 0.1076 0.1197 0.1012 0.0047 -0.0097 0.0183 221 ASN B O 4064 C CB . ASN B 141 ? 0.1384 0.1579 0.1317 0.0064 -0.0107 0.0209 221 ASN B CB 4065 C CG . ASN B 141 ? 0.1951 0.2126 0.1885 0.0076 -0.0101 0.0230 221 ASN B CG 4066 O OD1 . ASN B 141 ? 0.1743 0.1879 0.1685 0.0081 -0.0095 0.0233 221 ASN B OD1 4067 N ND2 . ASN B 141 ? 0.1736 0.1937 0.1660 0.0080 -0.0102 0.0245 221 ASN B ND2 4068 N N . ILE B 142 ? 0.1132 0.1229 0.1087 0.0055 -0.0097 0.0179 222 ILE B N 4069 C CA . ILE B 142 ? 0.0935 0.0993 0.0892 0.0049 -0.0091 0.0169 222 ILE B CA 4070 C C . ILE B 142 ? 0.1115 0.1174 0.1064 0.0034 -0.0092 0.0151 222 ILE B C 4071 O O . ILE B 142 ? 0.1203 0.1255 0.1144 0.0029 -0.0089 0.0151 222 ILE B O 4072 C CB . ILE B 142 ? 0.0969 0.1004 0.0925 0.0054 -0.0085 0.0183 222 ILE B CB 4073 C CG1 . ILE B 142 ? 0.1281 0.1314 0.1244 0.0070 -0.0083 0.0203 222 ILE B CG1 4074 C CG2 . ILE B 142 ? 0.1474 0.1472 0.1435 0.0048 -0.0080 0.0173 222 ILE B CG2 4075 C CD1 . ILE B 142 ? 0.1647 0.1657 0.1611 0.0076 -0.0076 0.0218 222 ILE B CD1 4076 N N . LEU B 143 ? 0.1144 0.1210 0.1095 0.0027 -0.0094 0.0136 223 LEU B N 4077 C CA . LEU B 143 ? 0.0980 0.1039 0.0924 0.0013 -0.0093 0.0118 223 LEU B CA 4078 C C . LEU B 143 ? 0.0830 0.0853 0.0776 0.0012 -0.0087 0.0116 223 LEU B C 4079 O O . LEU B 143 ? 0.0778 0.0781 0.0734 0.0018 -0.0085 0.0119 223 LEU B O 4080 C CB . LEU B 143 ? 0.1068 0.1133 0.1017 0.0007 -0.0095 0.0104 223 LEU B CB 4081 C CG . LEU B 143 ? 0.0961 0.1015 0.0905 -0.0005 -0.0092 0.0086 223 LEU B CG 4082 C CD1 . LEU B 143 ? 0.0583 0.0658 0.0515 -0.0014 -0.0092 0.0080 223 LEU B CD1 4083 C CD2 . LEU B 143 ? 0.1031 0.1089 0.0981 -0.0010 -0.0093 0.0075 223 LEU B CD2 4084 N N . ARG B 144 ? 0.0602 0.0620 0.0540 0.0005 -0.0085 0.0110 224 ARG B N 4085 C CA . ARG B 144 ? 0.0917 0.0906 0.0857 0.0004 -0.0080 0.0108 224 ARG B CA 4086 C C . ARG B 144 ? 0.0764 0.0750 0.0697 -0.0005 -0.0077 0.0095 224 ARG B C 4087 O O . ARG B 144 ? 0.0829 0.0834 0.0753 -0.0011 -0.0078 0.0089 224 ARG B O 4088 C CB . ARG B 144 ? 0.1097 0.1080 0.1037 0.0011 -0.0077 0.0124 224 ARG B CB 4089 C CG . ARG B 144 ? 0.1007 0.1015 0.0937 0.0011 -0.0078 0.0133 224 ARG B CG 4090 C CD . ARG B 144 ? 0.1147 0.1150 0.1079 0.0020 -0.0076 0.0153 224 ARG B CD 4091 N NE . ARG B 144 ? 0.1019 0.1044 0.0940 0.0020 -0.0076 0.0162 224 ARG B NE 4092 C CZ . ARG B 144 ? 0.1281 0.1337 0.1198 0.0025 -0.0081 0.0171 224 ARG B CZ 4093 N NH1 . ARG B 144 ? 0.0939 0.1008 0.0862 0.0029 -0.0085 0.0171 224 ARG B NH1 4094 N NH2 . ARG B 144 ? 0.1212 0.1288 0.1118 0.0024 -0.0081 0.0180 224 ARG B NH2 4095 N N . THR B 145 ? 0.0982 0.0943 0.0918 -0.0007 -0.0073 0.0090 225 THR B N 4096 C CA . THR B 145 ? 0.0748 0.0703 0.0679 -0.0014 -0.0070 0.0077 225 THR B CA 4097 C C . THR B 145 ? 0.0952 0.0893 0.0883 -0.0014 -0.0065 0.0080 225 THR B C 4098 O O . THR B 145 ? 0.0993 0.0931 0.0925 -0.0010 -0.0064 0.0091 225 THR B O 4099 C CB . THR B 145 ? 0.0716 0.0662 0.0650 -0.0017 -0.0069 0.0065 225 THR B CB 4100 O OG1 . THR B 145 ? 0.1428 0.1370 0.1356 -0.0024 -0.0065 0.0053 225 THR B OG1 4101 C CG2 . THR B 145 ? 0.1006 0.0931 0.0950 -0.0013 -0.0068 0.0066 225 THR B CG2 4102 N N . GLN B 146 ? 0.0819 0.0749 0.0748 -0.0018 -0.0062 0.0069 226 GLN B N 4103 C CA . GLN B 146 ? 0.0768 0.0691 0.0696 -0.0019 -0.0057 0.0069 226 GLN B CA 4104 C C . GLN B 146 ? 0.1000 0.0909 0.0936 -0.0015 -0.0056 0.0076 226 GLN B C 4105 O O . GLN B 146 ? 0.0916 0.0826 0.0851 -0.0016 -0.0053 0.0082 226 GLN B O 4106 C CB . GLN B 146 ? 0.0756 0.0671 0.0683 -0.0022 -0.0054 0.0056 226 GLN B CB 4107 C CG . GLN B 146 ? 0.0938 0.0864 0.0856 -0.0027 -0.0053 0.0046 226 GLN B CG 4108 C CD . GLN B 146 ? 0.1191 0.1106 0.1109 -0.0029 -0.0047 0.0035 226 GLN B CD 4109 O OE1 . GLN B 146 ? 0.1744 0.1654 0.1662 -0.0031 -0.0046 0.0027 226 GLN B OE1 4110 N NE2 . GLN B 146 ? 0.1045 0.0957 0.0962 -0.0028 -0.0043 0.0035 226 GLN B NE2 4111 N N . GLU B 147 ? 0.0628 0.0525 0.0573 -0.0012 -0.0057 0.0075 227 GLU B N 4112 C CA . GLU B 147 ? 0.0832 0.0716 0.0785 -0.0011 -0.0054 0.0077 227 GLU B CA 4113 C C . GLU B 147 ? 0.1080 0.0960 0.1032 -0.0014 -0.0051 0.0070 227 GLU B C 4114 O O . GLU B 147 ? 0.1169 0.1044 0.1125 -0.0014 -0.0048 0.0073 227 GLU B O 4115 C CB . GLU B 147 ? 0.1510 0.1392 0.1464 -0.0009 -0.0053 0.0089 227 GLU B CB 4116 C CG . GLU B 147 ? 0.1546 0.1438 0.1498 -0.0006 -0.0056 0.0099 227 GLU B CG 4117 C CD . GLU B 147 ? 0.1970 0.1859 0.1928 -0.0001 -0.0060 0.0098 227 GLU B CD 4118 O OE1 . GLU B 147 ? 0.1392 0.1271 0.1355 -0.0002 -0.0060 0.0090 227 GLU B OE1 4119 O OE2 . GLU B 147 ? 0.1999 0.1898 0.1955 0.0003 -0.0062 0.0106 227 GLU B OE2 4120 N N . SER B 148 ? 0.0820 0.0704 0.0767 -0.0015 -0.0050 0.0062 228 SER B N 4121 C CA . SER B 148 ? 0.0851 0.0732 0.0798 -0.0015 -0.0046 0.0055 228 SER B CA 4122 C C . SER B 148 ? 0.1072 0.0950 0.1016 -0.0015 -0.0045 0.0046 228 SER B C 4123 O O . SER B 148 ? 0.1142 0.1022 0.1084 -0.0016 -0.0048 0.0045 228 SER B O 4124 C CB . SER B 148 ? 0.1473 0.1361 0.1415 -0.0018 -0.0043 0.0056 228 SER B CB 4125 O OG . SER B 148 ? 0.1446 0.1344 0.1379 -0.0020 -0.0043 0.0055 228 SER B OG 4126 N N . GLU B 149 ? 0.0823 0.0698 0.0767 -0.0014 -0.0041 0.0040 229 GLU B N 4127 C CA . GLU B 149 ? 0.1079 0.0948 0.1021 -0.0013 -0.0039 0.0033 229 GLU B CA 4128 C C . GLU B 149 ? 0.0927 0.0800 0.0860 -0.0018 -0.0037 0.0027 229 GLU B C 4129 O O . GLU B 149 ? 0.1012 0.0893 0.0939 -0.0020 -0.0036 0.0027 229 GLU B O 4130 C CB . GLU B 149 ? 0.0876 0.0740 0.0820 -0.0009 -0.0034 0.0030 229 GLU B CB 4131 C CG . GLU B 149 ? 0.1056 0.0924 0.0995 -0.0009 -0.0029 0.0026 229 GLU B CG 4132 C CD . GLU B 149 ? 0.1863 0.1727 0.1805 -0.0003 -0.0024 0.0023 229 GLU B CD 4133 O OE1 . GLU B 149 ? 0.1671 0.1528 0.1618 0.0001 -0.0024 0.0024 229 GLU B OE1 4134 O OE2 . GLU B 149 ? 0.1367 0.1234 0.1306 -0.0002 -0.0019 0.0020 229 GLU B OE2 4135 N N . CYS B 150 ? 0.1029 0.0897 0.0961 -0.0019 -0.0037 0.0022 230 CYS B N 4136 C CA . CYS B 150 ? 0.1220 0.1091 0.1145 -0.0025 -0.0034 0.0013 230 CYS B CA 4137 C C . CYS B 150 ? 0.1349 0.1210 0.1271 -0.0023 -0.0026 0.0006 230 CYS B C 4138 O O . CYS B 150 ? 0.1141 0.0995 0.1068 -0.0017 -0.0024 0.0009 230 CYS B O 4139 C CB . CYS B 150 ? 0.1069 0.0939 0.0994 -0.0029 -0.0035 0.0009 230 CYS B CB 4140 S SG . CYS B 150 ? 0.1409 0.1265 0.1342 -0.0024 -0.0037 0.0012 230 CYS B SG 4141 N N . ALA B 151 ? 0.0898 0.0760 0.0812 -0.0029 -0.0021 -0.0003 231 ALA B N 4142 C CA . ALA B 151 ? 0.1089 0.0942 0.1002 -0.0026 -0.0012 -0.0010 231 ALA B CA 4143 C C . ALA B 151 ? 0.1441 0.1279 0.1351 -0.0030 -0.0005 -0.0020 231 ALA B C 4144 O O . ALA B 151 ? 0.0804 0.0646 0.0710 -0.0038 -0.0007 -0.0026 231 ALA B O 4145 C CB . ALA B 151 ? 0.1090 0.0955 0.0994 -0.0030 -0.0010 -0.0014 231 ALA B CB 4146 N N . CYS B 152 ? 0.1280 0.1101 0.1193 -0.0023 0.0002 -0.0021 232 CYS B N 4147 C CA . CYS B 152 ? 0.1346 0.1148 0.1257 -0.0025 0.0010 -0.0029 232 CYS B CA 4148 C C . CYS B 152 ? 0.1469 0.1258 0.1376 -0.0023 0.0021 -0.0038 232 CYS B C 4149 O O . CYS B 152 ? 0.1878 0.1667 0.1788 -0.0015 0.0025 -0.0035 232 CYS B O 4150 C CB . CYS B 152 ? 0.1757 0.1547 0.1676 -0.0017 0.0009 -0.0021 232 CYS B CB 4151 S SG . CYS B 152 ? 0.2359 0.2160 0.2283 -0.0020 -0.0003 -0.0013 232 CYS B SG 4152 N N . VAL B 153 ? 0.1080 0.0860 0.0983 -0.0032 0.0028 -0.0050 233 VAL B N 4153 C CA . VAL B 153 ? 0.1188 0.0951 0.1086 -0.0032 0.0042 -0.0060 233 VAL B CA 4154 C C . VAL B 153 ? 0.1750 0.1490 0.1648 -0.0037 0.0051 -0.0068 233 VAL B C 4155 O O . VAL B 153 ? 0.1126 0.0872 0.1022 -0.0050 0.0048 -0.0075 233 VAL B O 4156 C CB . VAL B 153 ? 0.1448 0.1225 0.1338 -0.0041 0.0044 -0.0072 233 VAL B CB 4157 C CG1 . VAL B 153 ? 0.1492 0.1249 0.1378 -0.0042 0.0059 -0.0085 233 VAL B CG1 4158 C CG2 . VAL B 153 ? 0.1354 0.1152 0.1245 -0.0036 0.0037 -0.0064 233 VAL B CG2 4159 N N . ASN B 154 ? 0.1471 0.1187 0.1372 -0.0028 0.0061 -0.0066 234 ASN B N 4160 C CA . ASN B 154 ? 0.1885 0.1575 0.1785 -0.0032 0.0072 -0.0072 234 ASN B CA 4161 C C . ASN B 154 ? 0.1433 0.1125 0.1336 -0.0041 0.0067 -0.0071 234 ASN B C 4162 O O . ASN B 154 ? 0.1583 0.1268 0.1482 -0.0055 0.0073 -0.0084 234 ASN B O 4163 C CB . ASN B 154 ? 0.2011 0.1690 0.1905 -0.0041 0.0085 -0.0090 234 ASN B CB 4164 C CG . ASN B 154 ? 0.2095 0.1741 0.1989 -0.0044 0.0100 -0.0097 234 ASN B CG 4165 O OD1 . ASN B 154 ? 0.3134 0.2759 0.3032 -0.0032 0.0105 -0.0086 234 ASN B OD1 4166 N ND2 . ASN B 154 ? 0.2779 0.2419 0.2667 -0.0060 0.0107 -0.0114 234 ASN B ND2 4167 N N . GLY B 155 ? 0.1759 0.1463 0.1667 -0.0035 0.0056 -0.0058 235 GLY B N 4168 C CA . GLY B 155 ? 0.1767 0.1472 0.1676 -0.0042 0.0051 -0.0056 235 GLY B CA 4169 C C . GLY B 155 ? 0.2098 0.1830 0.2006 -0.0053 0.0039 -0.0059 235 GLY B C 4170 O O . GLY B 155 ? 0.1770 0.1508 0.1681 -0.0058 0.0033 -0.0057 235 GLY B O 4171 N N . SER B 156 ? 0.1142 0.0891 0.1046 -0.0057 0.0036 -0.0064 236 SER B N 4172 C CA . SER B 156 ? 0.1126 0.0903 0.1029 -0.0065 0.0024 -0.0065 236 SER B CA 4173 C C . SER B 156 ? 0.1374 0.1168 0.1278 -0.0056 0.0014 -0.0054 236 SER B C 4174 O O . SER B 156 ? 0.1174 0.0966 0.1077 -0.0049 0.0017 -0.0052 236 SER B O 4175 C CB . SER B 156 ? 0.1509 0.1296 0.1403 -0.0078 0.0028 -0.0081 236 SER B CB 4176 O OG . SER B 156 ? 0.2264 0.2036 0.2157 -0.0089 0.0038 -0.0093 236 SER B OG 4177 N N . CYS B 157 ? 0.0927 0.0739 0.0835 -0.0057 0.0003 -0.0046 237 CYS B N 4178 C CA . CYS B 157 ? 0.0977 0.0804 0.0886 -0.0050 -0.0006 -0.0035 237 CYS B CA 4179 C C . CYS B 157 ? 0.1216 0.1069 0.1121 -0.0057 -0.0013 -0.0036 237 CYS B C 4180 O O . CYS B 157 ? 0.0981 0.0844 0.0885 -0.0066 -0.0015 -0.0042 237 CYS B O 4181 C CB . CYS B 157 ? 0.1029 0.0854 0.0947 -0.0042 -0.0012 -0.0023 237 CYS B CB 4182 S SG . CYS B 157 ? 0.2300 0.2101 0.2223 -0.0032 -0.0005 -0.0019 237 CYS B SG 4183 N N . PHE B 158 ? 0.0864 0.0729 0.0767 -0.0053 -0.0017 -0.0031 238 PHE B N 4184 C CA . PHE B 158 ? 0.0859 0.0750 0.0757 -0.0059 -0.0022 -0.0031 238 PHE B CA 4185 C C . PHE B 158 ? 0.0787 0.0690 0.0689 -0.0053 -0.0031 -0.0016 238 PHE B C 4186 O O . PHE B 158 ? 0.1125 0.1019 0.1031 -0.0045 -0.0030 -0.0009 238 PHE B O 4187 C CB . PHE B 158 ? 0.0870 0.0766 0.0760 -0.0064 -0.0016 -0.0040 238 PHE B CB 4188 C CG . PHE B 158 ? 0.0881 0.0762 0.0767 -0.0070 -0.0006 -0.0056 238 PHE B CG 4189 C CD1 . PHE B 158 ? 0.0845 0.0700 0.0734 -0.0064 0.0003 -0.0058 238 PHE B CD1 4190 C CD2 . PHE B 158 ? 0.0803 0.0697 0.0683 -0.0083 -0.0004 -0.0068 238 PHE B CD2 4191 C CE1 . PHE B 158 ? 0.0905 0.0743 0.0790 -0.0070 0.0014 -0.0072 238 PHE B CE1 4192 C CE2 . PHE B 158 ? 0.1088 0.0966 0.0964 -0.0090 0.0007 -0.0084 238 PHE B CE2 4193 C CZ . PHE B 158 ? 0.0857 0.0705 0.0736 -0.0084 0.0016 -0.0085 238 PHE B CZ 4194 N N . THR B 159 ? 0.1009 0.0932 0.0910 -0.0055 -0.0038 -0.0012 239 THR B N 4195 C CA . THR B 159 ? 0.0957 0.0890 0.0861 -0.0049 -0.0044 0.0002 239 THR B CA 4196 C C . THR B 159 ? 0.1372 0.1332 0.1269 -0.0053 -0.0049 0.0005 239 THR B C 4197 O O . THR B 159 ? 0.1417 0.1391 0.1308 -0.0062 -0.0048 -0.0005 239 THR B O 4198 C CB . THR B 159 ? 0.1597 0.1522 0.1510 -0.0043 -0.0049 0.0011 239 THR B CB 4199 O OG1 . THR B 159 ? 0.1607 0.1537 0.1524 -0.0037 -0.0053 0.0024 239 THR B OG1 4200 C CG2 . THR B 159 ? 0.1410 0.1348 0.1324 -0.0048 -0.0053 0.0008 239 THR B CG2 4201 N N . VAL B 160 ? 0.1246 0.1216 0.1144 -0.0048 -0.0054 0.0019 240 VAL B N 4202 C CA . VAL B 160 ? 0.0961 0.0958 0.0853 -0.0049 -0.0058 0.0025 240 VAL B CA 4203 C C . VAL B 160 ? 0.0907 0.0908 0.0807 -0.0041 -0.0065 0.0039 240 VAL B C 4204 O O . VAL B 160 ? 0.0891 0.0875 0.0798 -0.0035 -0.0064 0.0047 240 VAL B O 4205 C CB . VAL B 160 ? 0.1151 0.1156 0.1036 -0.0048 -0.0056 0.0030 240 VAL B CB 4206 C CG1 . VAL B 160 ? 0.1091 0.1126 0.0970 -0.0048 -0.0062 0.0039 240 VAL B CG1 4207 C CG2 . VAL B 160 ? 0.1075 0.1078 0.0953 -0.0055 -0.0049 0.0015 240 VAL B CG2 4208 N N . MET B 161 ? 0.0803 0.0829 0.0702 -0.0043 -0.0070 0.0042 241 MET B N 4209 C CA . MET B 161 ? 0.0885 0.0916 0.0790 -0.0034 -0.0075 0.0057 241 MET B CA 4210 C C . MET B 161 ? 0.0816 0.0878 0.0715 -0.0032 -0.0079 0.0067 241 MET B C 4211 O O . MET B 161 ? 0.0814 0.0899 0.0703 -0.0039 -0.0080 0.0060 241 MET B O 4212 C CB . MET B 161 ? 0.0833 0.0866 0.0745 -0.0035 -0.0078 0.0052 241 MET B CB 4213 C CG . MET B 161 ? 0.0791 0.0796 0.0709 -0.0036 -0.0074 0.0043 241 MET B CG 4214 S SD . MET B 161 ? 0.1828 0.1834 0.1756 -0.0034 -0.0077 0.0042 241 MET B SD 4215 C CE . MET B 161 ? 0.3112 0.3087 0.3044 -0.0037 -0.0071 0.0031 241 MET B CE 4216 N N . THR B 162 ? 0.0655 0.0716 0.0558 -0.0022 -0.0082 0.0085 242 THR B N 4217 C CA . THR B 162 ? 0.0938 0.1027 0.0837 -0.0017 -0.0085 0.0099 242 THR B CA 4218 C C . THR B 162 ? 0.0976 0.1076 0.0882 -0.0008 -0.0090 0.0110 242 THR B C 4219 O O . THR B 162 ? 0.0736 0.0814 0.0653 -0.0002 -0.0089 0.0113 242 THR B O 4220 C CB . THR B 162 ? 0.0718 0.0796 0.0614 -0.0012 -0.0082 0.0112 242 THR B CB 4221 O OG1 . THR B 162 ? 0.1030 0.1099 0.0919 -0.0019 -0.0077 0.0102 242 THR B OG1 4222 C CG2 . THR B 162 ? 0.0837 0.0944 0.0727 -0.0006 -0.0085 0.0129 242 THR B CG2 4223 N N . ASP B 163 ? 0.0660 0.0797 0.0562 -0.0006 -0.0095 0.0116 243 ASP B N 4224 C CA . ASP B 163 ? 0.0843 0.0995 0.0752 0.0004 -0.0099 0.0129 243 ASP B CA 4225 C C . ASP B 163 ? 0.0796 0.0980 0.0698 0.0011 -0.0102 0.0146 243 ASP B C 4226 O O . ASP B 163 ? 0.0726 0.0938 0.0617 0.0003 -0.0103 0.0141 243 ASP B O 4227 C CB . ASP B 163 ? 0.0928 0.1100 0.0841 -0.0002 -0.0103 0.0116 243 ASP B CB 4228 C CG . ASP B 163 ? 0.1164 0.1340 0.1088 0.0009 -0.0106 0.0126 243 ASP B CG 4229 O OD1 . ASP B 163 ? 0.1201 0.1374 0.1129 0.0022 -0.0106 0.0145 243 ASP B OD1 4230 O OD2 . ASP B 163 ? 0.1245 0.1429 0.1175 0.0004 -0.0108 0.0114 243 ASP B OD2 4231 N N . GLY B 164 ? 0.1058 0.1237 0.0965 0.0025 -0.0102 0.0167 244 GLY B N 4232 C CA . GLY B 164 ? 0.1156 0.1361 0.1057 0.0034 -0.0103 0.0186 244 GLY B CA 4233 C C . GLY B 164 ? 0.1130 0.1307 0.1032 0.0042 -0.0097 0.0204 244 GLY B C 4234 O O . GLY B 164 ? 0.1391 0.1529 0.1301 0.0042 -0.0092 0.0201 244 GLY B O 4235 N N . PRO B 165 ? 0.1136 0.1334 0.1031 0.0050 -0.0097 0.0223 245 PRO B N 4236 C CA . PRO B 165 ? 0.1387 0.1561 0.1282 0.0058 -0.0090 0.0243 245 PRO B CA 4237 C C . PRO B 165 ? 0.1199 0.1339 0.1092 0.0049 -0.0084 0.0234 245 PRO B C 4238 O O . PRO B 165 ? 0.1068 0.1215 0.0953 0.0036 -0.0085 0.0217 245 PRO B O 4239 C CB . PRO B 165 ? 0.1474 0.1686 0.1358 0.0064 -0.0092 0.0261 245 PRO B CB 4240 C CG . PRO B 165 ? 0.1897 0.2154 0.1779 0.0064 -0.0101 0.0255 245 PRO B CG 4241 C CD . PRO B 165 ? 0.1642 0.1891 0.1527 0.0049 -0.0103 0.0227 245 PRO B CD 4242 N N . SER B 166 ? 0.1426 0.1531 0.1326 0.0055 -0.0077 0.0245 246 SER B N 4243 C CA . SER B 166 ? 0.1682 0.1759 0.1580 0.0046 -0.0070 0.0239 246 SER B CA 4244 C C . SER B 166 ? 0.1931 0.2015 0.1820 0.0049 -0.0066 0.0257 246 SER B C 4245 O O . SER B 166 ? 0.1714 0.1779 0.1601 0.0042 -0.0060 0.0256 246 SER B O 4246 C CB . SER B 166 ? 0.1973 0.2008 0.1884 0.0048 -0.0065 0.0237 246 SER B CB 4247 O OG . SER B 166 ? 0.2314 0.2338 0.2233 0.0061 -0.0061 0.0258 246 SER B OG 4248 N N . ASN B 167 ? 0.1515 0.1629 0.1399 0.0058 -0.0069 0.0275 247 ASN B N 4249 C CA . ASN B 167 ? 0.1813 0.1937 0.1687 0.0062 -0.0064 0.0296 247 ASN B CA 4250 C C . ASN B 167 ? 0.2232 0.2406 0.2092 0.0062 -0.0071 0.0299 247 ASN B C 4251 O O . ASN B 167 ? 0.2269 0.2463 0.2122 0.0070 -0.0069 0.0321 247 ASN B O 4252 C CB . ASN B 167 ? 0.2131 0.2237 0.2013 0.0078 -0.0059 0.0322 247 ASN B CB 4253 C CG . ASN B 167 ? 0.2391 0.2523 0.2276 0.0092 -0.0065 0.0333 247 ASN B CG 4254 O OD1 . ASN B 167 ? 0.1864 0.2022 0.1749 0.0088 -0.0073 0.0318 247 ASN B OD1 4255 N ND2 . ASN B 167 ? 0.3181 0.3307 0.3070 0.0108 -0.0060 0.0359 247 ASN B ND2 4256 N N . GLY B 168 ? 0.1608 0.1804 0.1465 0.0052 -0.0077 0.0277 248 GLY B N 4257 C CA . GLY B 168 ? 0.1757 0.2003 0.1600 0.0048 -0.0084 0.0275 248 GLY B CA 4258 C C . GLY B 168 ? 0.1506 0.1763 0.1347 0.0034 -0.0088 0.0245 248 GLY B C 4259 O O . GLY B 168 ? 0.1305 0.1530 0.1154 0.0027 -0.0086 0.0228 248 GLY B O 4260 N N . GLN B 169 ? 0.1231 0.1534 0.1061 0.0029 -0.0094 0.0239 249 GLN B N 4261 C CA . GLN B 169 ? 0.1387 0.1703 0.1215 0.0015 -0.0097 0.0211 249 GLN B CA 4262 C C . GLN B 169 ? 0.1510 0.1809 0.1352 0.0015 -0.0100 0.0200 249 GLN B C 4263 O O . GLN B 169 ? 0.0956 0.1266 0.0805 0.0026 -0.0104 0.0213 249 GLN B O 4264 C CB . GLN B 169 ? 0.1335 0.1707 0.1151 0.0010 -0.0103 0.0208 249 GLN B CB 4265 C CG . GLN B 169 ? 0.1320 0.1705 0.1131 -0.0006 -0.0105 0.0178 249 GLN B CG 4266 C CD . GLN B 169 ? 0.1399 0.1767 0.1202 -0.0019 -0.0099 0.0161 249 GLN B CD 4267 O OE1 . GLN B 169 ? 0.1069 0.1455 0.0860 -0.0020 -0.0097 0.0167 249 GLN B OE1 4268 N NE2 . GLN B 169 ? 0.1061 0.1395 0.0871 -0.0027 -0.0095 0.0141 249 GLN B NE2 4269 N N . ALA B 170 ? 0.1147 0.1419 0.0992 0.0004 -0.0097 0.0178 250 ALA B N 4270 C CA . ALA B 170 ? 0.0896 0.1152 0.0753 0.0003 -0.0100 0.0166 250 ALA B CA 4271 C C . ALA B 170 ? 0.1106 0.1373 0.0959 -0.0012 -0.0101 0.0140 250 ALA B C 4272 O O . ALA B 170 ? 0.0794 0.1087 0.0635 -0.0021 -0.0101 0.0131 250 ALA B O 4273 C CB . ALA B 170 ? 0.1086 0.1293 0.0954 0.0007 -0.0094 0.0167 250 ALA B CB 4274 N N . SER B 171 ? 0.0606 0.0854 0.0469 -0.0016 -0.0101 0.0127 251 SER B N 4275 C CA . SER B 171 ? 0.0898 0.1151 0.0758 -0.0030 -0.0100 0.0102 251 SER B CA 4276 C C . SER B 171 ? 0.0850 0.1058 0.0715 -0.0035 -0.0094 0.0089 251 SER B C 4277 O O . SER B 171 ? 0.0651 0.0830 0.0527 -0.0028 -0.0093 0.0095 251 SER B O 4278 C CB . SER B 171 ? 0.1089 0.1364 0.0955 -0.0031 -0.0106 0.0097 251 SER B CB 4279 O OG . SER B 171 ? 0.1752 0.2030 0.1617 -0.0046 -0.0104 0.0072 251 SER B OG 4280 N N . TYR B 172 ? 0.0886 0.1091 0.0743 -0.0047 -0.0090 0.0070 252 TYR B N 4281 C CA . TYR B 172 ? 0.0977 0.1143 0.0839 -0.0050 -0.0083 0.0059 252 TYR B CA 4282 C C . TYR B 172 ? 0.1016 0.1179 0.0877 -0.0063 -0.0080 0.0036 252 TYR B C 4283 O O . TYR B 172 ? 0.0926 0.1114 0.0777 -0.0073 -0.0080 0.0024 252 TYR B O 4284 C CB . TYR B 172 ? 0.0862 0.1019 0.0716 -0.0050 -0.0078 0.0062 252 TYR B CB 4285 C CG . TYR B 172 ? 0.0949 0.1124 0.0798 -0.0042 -0.0081 0.0083 252 TYR B CG 4286 C CD1 . TYR B 172 ? 0.0628 0.0787 0.0486 -0.0030 -0.0082 0.0102 252 TYR B CD1 4287 C CD2 . TYR B 172 ? 0.1363 0.1573 0.1199 -0.0046 -0.0082 0.0083 252 TYR B CD2 4288 C CE1 . TYR B 172 ? 0.0774 0.0947 0.0627 -0.0022 -0.0083 0.0122 252 TYR B CE1 4289 C CE2 . TYR B 172 ? 0.0745 0.0972 0.0577 -0.0038 -0.0083 0.0104 252 TYR B CE2 4290 C CZ . TYR B 172 ? 0.0932 0.1139 0.0772 -0.0026 -0.0084 0.0124 252 TYR B CZ 4291 O OH . TYR B 172 ? 0.0899 0.1122 0.0735 -0.0017 -0.0084 0.0146 252 TYR B OH 4292 N N . LYS B 173 ? 0.0582 0.0715 0.0452 -0.0062 -0.0078 0.0030 253 LYS B N 4293 C CA . LYS B 173 ? 0.0553 0.0679 0.0423 -0.0074 -0.0074 0.0010 253 LYS B CA 4294 C C . LYS B 173 ? 0.0815 0.0902 0.0688 -0.0074 -0.0066 0.0002 253 LYS B C 4295 O O . LYS B 173 ? 0.0531 0.0594 0.0411 -0.0065 -0.0066 0.0012 253 LYS B O 4296 C CB . LYS B 173 ? 0.0764 0.0898 0.0642 -0.0074 -0.0078 0.0009 253 LYS B CB 4297 C CG . LYS B 173 ? 0.1228 0.1405 0.1102 -0.0077 -0.0085 0.0010 253 LYS B CG 4298 C CD . LYS B 173 ? 0.1055 0.1240 0.0939 -0.0079 -0.0088 0.0007 253 LYS B CD 4299 C CE . LYS B 173 ? 0.1827 0.2061 0.1708 -0.0083 -0.0095 0.0008 253 LYS B CE 4300 N NZ . LYS B 173 ? 0.2318 0.2560 0.2208 -0.0086 -0.0097 0.0002 253 LYS B NZ 4301 N N . ILE B 174 ? 0.0866 0.0946 0.0734 -0.0084 -0.0060 -0.0016 254 ILE B N 4302 C CA . ILE B 174 ? 0.1011 0.1055 0.0881 -0.0084 -0.0052 -0.0024 254 ILE B CA 4303 C C . ILE B 174 ? 0.1156 0.1187 0.1032 -0.0089 -0.0049 -0.0034 254 ILE B C 4304 O O . ILE B 174 ? 0.0838 0.0889 0.0712 -0.0099 -0.0050 -0.0045 254 ILE B O 4305 C CB . ILE B 174 ? 0.1054 0.1096 0.0915 -0.0091 -0.0044 -0.0038 254 ILE B CB 4306 C CG1 . ILE B 174 ? 0.1161 0.1224 0.1015 -0.0088 -0.0046 -0.0029 254 ILE B CG1 4307 C CG2 . ILE B 174 ? 0.0975 0.0981 0.0840 -0.0087 -0.0036 -0.0042 254 ILE B CG2 4308 C CD1 . ILE B 174 ? 0.1743 0.1811 0.1586 -0.0096 -0.0039 -0.0043 254 ILE B CD1 4309 N N . PHE B 175 ? 0.1093 0.1093 0.0977 -0.0083 -0.0046 -0.0032 255 PHE B N 4310 C CA . PHE B 175 ? 0.1044 0.1030 0.0934 -0.0088 -0.0043 -0.0039 255 PHE B CA 4311 C C . PHE B 175 ? 0.1483 0.1437 0.1373 -0.0088 -0.0033 -0.0049 255 PHE B C 4312 O O . PHE B 175 ? 0.1498 0.1436 0.1389 -0.0080 -0.0031 -0.0043 255 PHE B O 4313 C CB . PHE B 175 ? 0.1422 0.1404 0.1322 -0.0079 -0.0050 -0.0026 255 PHE B CB 4314 C CG . PHE B 175 ? 0.1273 0.1285 0.1174 -0.0077 -0.0059 -0.0017 255 PHE B CG 4315 C CD1 . PHE B 175 ? 0.1335 0.1365 0.1239 -0.0083 -0.0061 -0.0022 255 PHE B CD1 4316 C CD2 . PHE B 175 ? 0.1409 0.1431 0.1310 -0.0068 -0.0064 -0.0003 255 PHE B CD2 4317 C CE1 . PHE B 175 ? 0.1986 0.2045 0.1892 -0.0080 -0.0070 -0.0013 255 PHE B CE1 4318 C CE2 . PHE B 175 ? 0.1197 0.1245 0.1099 -0.0064 -0.0071 0.0008 255 PHE B CE2 4319 C CZ . PHE B 175 ? 0.1651 0.1719 0.1556 -0.0070 -0.0074 0.0003 255 PHE B CZ 4320 N N . ARG B 176 ? 0.1161 0.1108 0.1050 -0.0098 -0.0027 -0.0062 256 ARG B N 4321 C CA . ARG B 176 ? 0.0806 0.0719 0.0696 -0.0097 -0.0016 -0.0069 256 ARG B CA 4322 C C . ARG B 176 ? 0.1282 0.1182 0.1181 -0.0096 -0.0017 -0.0066 256 ARG B C 4323 O O . ARG B 176 ? 0.0772 0.0685 0.0673 -0.0105 -0.0019 -0.0071 256 ARG B O 4324 C CB . ARG B 176 ? 0.1244 0.1153 0.1128 -0.0110 -0.0006 -0.0088 256 ARG B CB 4325 C CG . ARG B 176 ? 0.1376 0.1248 0.1261 -0.0109 0.0006 -0.0094 256 ARG B CG 4326 C CD . ARG B 176 ? 0.1844 0.1710 0.1721 -0.0121 0.0018 -0.0114 256 ARG B CD 4327 N NE . ARG B 176 ? 0.2441 0.2272 0.2322 -0.0121 0.0030 -0.0120 256 ARG B NE 4328 C CZ . ARG B 176 ? 0.2719 0.2532 0.2594 -0.0129 0.0044 -0.0136 256 ARG B CZ 4329 N NH1 . ARG B 176 ? 0.2852 0.2682 0.2719 -0.0138 0.0046 -0.0149 256 ARG B NH1 4330 N NH2 . ARG B 176 ? 0.2695 0.2473 0.2573 -0.0127 0.0056 -0.0138 256 ARG B NH2 4331 N N . ILE B 177 ? 0.1118 0.0994 0.1022 -0.0086 -0.0015 -0.0057 257 ILE B N 4332 C CA . ILE B 177 ? 0.0817 0.0682 0.0728 -0.0082 -0.0016 -0.0052 257 ILE B CA 4333 C C . ILE B 177 ? 0.1215 0.1048 0.1127 -0.0080 -0.0005 -0.0055 257 ILE B C 4334 O O . ILE B 177 ? 0.1219 0.1039 0.1131 -0.0072 -0.0001 -0.0052 257 ILE B O 4335 C CB . ILE B 177 ? 0.0801 0.0671 0.0719 -0.0071 -0.0025 -0.0036 257 ILE B CB 4336 C CG1 . ILE B 177 ? 0.1304 0.1204 0.1221 -0.0072 -0.0034 -0.0031 257 ILE B CG1 4337 C CG2 . ILE B 177 ? 0.0864 0.0724 0.0789 -0.0067 -0.0026 -0.0031 257 ILE B CG2 4338 C CD1 . ILE B 177 ? 0.0883 0.0786 0.0805 -0.0060 -0.0041 -0.0017 257 ILE B CD1 4339 N N . GLU B 178 ? 0.0964 0.0788 0.0879 -0.0086 0.0000 -0.0060 258 GLU B N 4340 C CA . GLU B 178 ? 0.0995 0.0788 0.0911 -0.0084 0.0011 -0.0061 258 GLU B CA 4341 C C . GLU B 178 ? 0.1002 0.0789 0.0924 -0.0080 0.0009 -0.0053 258 GLU B C 4342 O O . GLU B 178 ? 0.0923 0.0722 0.0848 -0.0088 0.0006 -0.0056 258 GLU B O 4343 C CB . GLU B 178 ? 0.1387 0.1168 0.1298 -0.0097 0.0023 -0.0077 258 GLU B CB 4344 C CG . GLU B 178 ? 0.2260 0.2047 0.2164 -0.0101 0.0026 -0.0087 258 GLU B CG 4345 C CD . GLU B 178 ? 0.3230 0.3003 0.3128 -0.0115 0.0039 -0.0105 258 GLU B CD 4346 O OE1 . GLU B 178 ? 0.3921 0.3674 0.3822 -0.0120 0.0048 -0.0108 258 GLU B OE1 4347 O OE2 . GLU B 178 ? 0.3061 0.2846 0.2953 -0.0122 0.0041 -0.0117 258 GLU B OE2 4348 N N . LYS B 179 ? 0.1247 0.1020 0.1172 -0.0067 0.0009 -0.0042 259 LYS B N 4349 C CA . LYS B 179 ? 0.1155 0.0925 0.1087 -0.0062 0.0007 -0.0033 259 LYS B CA 4350 C C . LYS B 179 ? 0.1132 0.0926 0.1068 -0.0064 -0.0005 -0.0030 259 LYS B C 4351 O O . LYS B 179 ? 0.1021 0.0818 0.0960 -0.0068 -0.0006 -0.0029 259 LYS B O 4352 C CB . LYS B 179 ? 0.1695 0.1445 0.1626 -0.0069 0.0018 -0.0038 259 LYS B CB 4353 C CG . LYS B 179 ? 0.2079 0.1800 0.2007 -0.0064 0.0030 -0.0039 259 LYS B CG 4354 C CD . LYS B 179 ? 0.3322 0.3022 0.3250 -0.0070 0.0042 -0.0042 259 LYS B CD 4355 C CE . LYS B 179 ? 0.4453 0.4123 0.4378 -0.0062 0.0056 -0.0041 259 LYS B CE 4356 N NZ . LYS B 179 ? 0.5453 0.5117 0.5380 -0.0044 0.0054 -0.0025 259 LYS B NZ 4357 N N . GLY B 180 ? 0.0918 0.0730 0.0853 -0.0061 -0.0013 -0.0027 260 GLY B N 4358 C CA . GLY B 180 ? 0.0987 0.0821 0.0927 -0.0060 -0.0023 -0.0021 260 GLY B CA 4359 C C . GLY B 180 ? 0.0907 0.0762 0.0846 -0.0072 -0.0026 -0.0029 260 GLY B C 4360 O O . GLY B 180 ? 0.1092 0.0966 0.1035 -0.0070 -0.0034 -0.0024 260 GLY B O 4361 N N . LYS B 181 ? 0.0933 0.0785 0.0867 -0.0083 -0.0019 -0.0041 261 LYS B N 4362 C CA . LYS B 181 ? 0.1045 0.0919 0.0978 -0.0095 -0.0021 -0.0050 261 LYS B CA 4363 C C . LYS B 181 ? 0.0878 0.0766 0.0803 -0.0100 -0.0022 -0.0056 261 LYS B C 4364 O O . LYS B 181 ? 0.1041 0.0914 0.0961 -0.0101 -0.0015 -0.0062 261 LYS B O 4365 C CB . LYS B 181 ? 0.1562 0.1424 0.1494 -0.0108 -0.0011 -0.0062 261 LYS B CB 4366 C CG . LYS B 181 ? 0.2439 0.2288 0.2377 -0.0105 -0.0009 -0.0056 261 LYS B CG 4367 C CD . LYS B 181 ? 0.2594 0.2469 0.2538 -0.0106 -0.0018 -0.0053 261 LYS B CD 4368 C CE . LYS B 181 ? 0.3194 0.3058 0.3144 -0.0105 -0.0015 -0.0049 261 LYS B CE 4369 N NZ . LYS B 181 ? 0.3551 0.3442 0.3508 -0.0107 -0.0022 -0.0047 261 LYS B NZ 4370 N N . ILE B 182 ? 0.0946 0.0866 0.0872 -0.0102 -0.0031 -0.0054 262 ILE B N 4371 C CA . ILE B 182 ? 0.1047 0.0985 0.0965 -0.0107 -0.0033 -0.0060 262 ILE B CA 4372 C C . ILE B 182 ? 0.1833 0.1775 0.1746 -0.0123 -0.0025 -0.0078 262 ILE B C 4373 O O . ILE B 182 ? 0.1551 0.1508 0.1467 -0.0133 -0.0025 -0.0085 262 ILE B O 4374 C CB . ILE B 182 ? 0.1309 0.1282 0.1228 -0.0104 -0.0044 -0.0052 262 ILE B CB 4375 C CG1 . ILE B 182 ? 0.1604 0.1572 0.1529 -0.0088 -0.0050 -0.0035 262 ILE B CG1 4376 C CG2 . ILE B 182 ? 0.1207 0.1203 0.1118 -0.0109 -0.0045 -0.0058 262 ILE B CG2 4377 C CD1 . ILE B 182 ? 0.2203 0.2200 0.2131 -0.0083 -0.0060 -0.0024 262 ILE B CD1 4378 N N . VAL B 183 ? 0.0894 0.0820 0.0800 -0.0127 -0.0016 -0.0088 263 VAL B N 4379 C CA . VAL B 183 ? 0.0875 0.0800 0.0776 -0.0144 -0.0007 -0.0107 263 VAL B CA 4380 C C . VAL B 183 ? 0.1845 0.1800 0.1738 -0.0152 -0.0009 -0.0116 263 VAL B C 4381 O O . VAL B 183 ? 0.1188 0.1153 0.1077 -0.0168 -0.0004 -0.0133 263 VAL B O 4382 C CB . VAL B 183 ? 0.1607 0.1491 0.1505 -0.0143 0.0007 -0.0113 263 VAL B CB 4383 C CG1 . VAL B 183 ? 0.2031 0.1890 0.1937 -0.0138 0.0011 -0.0106 263 VAL B CG1 4384 C CG2 . VAL B 183 ? 0.1775 0.1649 0.1670 -0.0132 0.0008 -0.0107 263 VAL B CG2 4385 N N . LYS B 184 ? 0.1096 0.1065 0.0986 -0.0142 -0.0017 -0.0105 264 LYS B N 4386 C CA . LYS B 184 ? 0.1415 0.1416 0.1296 -0.0148 -0.0021 -0.0111 264 LYS B CA 4387 C C . LYS B 184 ? 0.1318 0.1336 0.1199 -0.0135 -0.0031 -0.0093 264 LYS B C 4388 O O . LYS B 184 ? 0.1092 0.1089 0.0977 -0.0121 -0.0032 -0.0080 264 LYS B O 4389 C CB . LYS B 184 ? 0.1364 0.1349 0.1237 -0.0156 -0.0009 -0.0127 264 LYS B CB 4390 C CG . LYS B 184 ? 0.1736 0.1757 0.1599 -0.0166 -0.0011 -0.0137 264 LYS B CG 4391 C CD . LYS B 184 ? 0.1674 0.1678 0.1529 -0.0173 0.0001 -0.0154 264 LYS B CD 4392 C CE . LYS B 184 ? 0.1972 0.2015 0.1816 -0.0185 0.0000 -0.0167 264 LYS B CE 4393 N NZ . LYS B 184 ? 0.2398 0.2425 0.2234 -0.0193 0.0013 -0.0185 264 LYS B NZ 4394 N N . SER B 185 ? 0.0776 0.0833 0.0652 -0.0139 -0.0038 -0.0092 265 SER B N 4395 C CA . SER B 185 ? 0.1297 0.1372 0.1172 -0.0127 -0.0047 -0.0076 265 SER B CA 4396 C C . SER B 185 ? 0.1219 0.1330 0.1083 -0.0135 -0.0049 -0.0083 265 SER B C 4397 O O . SER B 185 ? 0.1297 0.1428 0.1157 -0.0150 -0.0047 -0.0099 265 SER B O 4398 C CB . SER B 185 ? 0.1269 0.1356 0.1153 -0.0117 -0.0056 -0.0059 265 SER B CB 4399 O OG . SER B 185 ? 0.1595 0.1715 0.1479 -0.0125 -0.0061 -0.0063 265 SER B OG 4400 N N . VAL B 186 ? 0.0986 0.1109 0.0845 -0.0127 -0.0053 -0.0071 266 VAL B N 4401 C CA . VAL B 186 ? 0.1367 0.1529 0.1216 -0.0133 -0.0056 -0.0074 266 VAL B CA 4402 C C . VAL B 186 ? 0.1658 0.1835 0.1506 -0.0119 -0.0064 -0.0052 266 VAL B C 4403 O O . VAL B 186 ? 0.1251 0.1401 0.1102 -0.0108 -0.0063 -0.0040 266 VAL B O 4404 C CB . VAL B 186 ? 0.1501 0.1654 0.1340 -0.0142 -0.0046 -0.0092 266 VAL B CB 4405 C CG1 . VAL B 186 ? 0.1745 0.1864 0.1584 -0.0131 -0.0041 -0.0084 266 VAL B CG1 4406 C CG2 . VAL B 186 ? 0.1680 0.1876 0.1507 -0.0149 -0.0049 -0.0097 266 VAL B CG2 4407 N N . GLU B 187 ? 0.1373 0.1593 0.1216 -0.0120 -0.0071 -0.0046 267 GLU B N 4408 C CA . GLU B 187 ? 0.1263 0.1498 0.1104 -0.0107 -0.0077 -0.0024 267 GLU B CA 4409 C C . GLU B 187 ? 0.1381 0.1625 0.1210 -0.0110 -0.0074 -0.0027 267 GLU B C 4410 O O . GLU B 187 ? 0.1400 0.1669 0.1219 -0.0122 -0.0071 -0.0043 267 GLU B O 4411 C CB . GLU B 187 ? 0.1299 0.1578 0.1141 -0.0104 -0.0087 -0.0013 267 GLU B CB 4412 C CG . GLU B 187 ? 0.1534 0.1828 0.1373 -0.0090 -0.0092 0.0011 267 GLU B CG 4413 C CD . GLU B 187 ? 0.2332 0.2665 0.2175 -0.0082 -0.0101 0.0026 267 GLU B CD 4414 O OE1 . GLU B 187 ? 0.2687 0.3040 0.2533 -0.0089 -0.0104 0.0017 267 GLU B OE1 4415 O OE2 . GLU B 187 ? 0.1867 0.2208 0.1708 -0.0069 -0.0105 0.0048 267 GLU B OE2 4416 N N . MET B 188 ? 0.1057 0.1282 0.0886 -0.0099 -0.0073 -0.0012 268 MET B N 4417 C CA . MET B 188 ? 0.0804 0.1037 0.0622 -0.0100 -0.0069 -0.0012 268 MET B CA 4418 C C . MET B 188 ? 0.0978 0.1259 0.0786 -0.0100 -0.0075 -0.0003 268 MET B C 4419 O O . MET B 188 ? 0.1347 0.1643 0.1160 -0.0089 -0.0083 0.0017 268 MET B O 4420 C CB . MET B 188 ? 0.1163 0.1364 0.0985 -0.0089 -0.0066 0.0002 268 MET B CB 4421 C CG . MET B 188 ? 0.1040 0.1198 0.0869 -0.0089 -0.0059 -0.0009 268 MET B CG 4422 S SD . MET B 188 ? 0.1600 0.1723 0.1440 -0.0075 -0.0059 0.0010 268 MET B SD 4423 C CE . MET B 188 ? 0.0968 0.1106 0.0799 -0.0071 -0.0058 0.0023 268 MET B CE 4424 N N . ASN B 189 ? 0.1234 0.1539 0.1029 -0.0111 -0.0072 -0.0017 269 ASN B N 4425 C CA . ASN B 189 ? 0.0954 0.1308 0.0739 -0.0111 -0.0078 -0.0008 269 ASN B CA 4426 C C . ASN B 189 ? 0.0995 0.1342 0.0775 -0.0102 -0.0076 0.0008 269 ASN B C 4427 O O . ASN B 189 ? 0.1055 0.1403 0.0825 -0.0108 -0.0069 -0.0002 269 ASN B O 4428 C CB . ASN B 189 ? 0.0705 0.1089 0.0478 -0.0128 -0.0075 -0.0033 269 ASN B CB 4429 C CG . ASN B 189 ? 0.1360 0.1801 0.1120 -0.0129 -0.0081 -0.0026 269 ASN B CG 4430 O OD1 . ASN B 189 ? 0.1069 0.1537 0.0831 -0.0120 -0.0089 -0.0006 269 ASN B OD1 4431 N ND2 . ASN B 189 ? 0.0990 0.1449 0.0737 -0.0140 -0.0075 -0.0041 269 ASN B ND2 4432 N N . ALA B 190 ? 0.0905 0.1245 0.0691 -0.0087 -0.0080 0.0034 270 ALA B N 4433 C CA . ALA B 190 ? 0.0765 0.1091 0.0548 -0.0079 -0.0077 0.0050 270 ALA B CA 4434 C C . ALA B 190 ? 0.1024 0.1375 0.0805 -0.0067 -0.0083 0.0078 270 ALA B C 4435 O O . ALA B 190 ? 0.0790 0.1117 0.0580 -0.0055 -0.0083 0.0097 270 ALA B O 4436 C CB . ALA B 190 ? 0.1195 0.1470 0.0991 -0.0073 -0.0072 0.0053 270 ALA B CB 4437 N N . PRO B 191 ? 0.1365 0.1765 0.1134 -0.0070 -0.0087 0.0080 271 PRO B N 4438 C CA . PRO B 191 ? 0.1299 0.1725 0.1064 -0.0058 -0.0091 0.0108 271 PRO B CA 4439 C C . PRO B 191 ? 0.1172 0.1579 0.0934 -0.0051 -0.0085 0.0124 271 PRO B C 4440 O O . PRO B 191 ? 0.1331 0.1733 0.1085 -0.0060 -0.0079 0.0111 271 PRO B O 4441 C CB . PRO B 191 ? 0.1656 0.2141 0.1407 -0.0065 -0.0096 0.0102 271 PRO B CB 4442 C CG . PRO B 191 ? 0.2065 0.2548 0.1810 -0.0083 -0.0091 0.0069 271 PRO B CG 4443 C CD . PRO B 191 ? 0.1397 0.1831 0.1155 -0.0085 -0.0087 0.0056 271 PRO B CD 4444 N N . ASN B 192 ? 0.1210 0.1606 0.0978 -0.0037 -0.0087 0.0151 272 ASN B N 4445 C CA . ASN B 192 ? 0.1258 0.1634 0.1025 -0.0031 -0.0081 0.0168 272 ASN B CA 4446 C C . ASN B 192 ? 0.1449 0.1772 0.1225 -0.0033 -0.0074 0.0160 272 ASN B C 4447 O O . ASN B 192 ? 0.1973 0.2278 0.1750 -0.0030 -0.0068 0.0172 272 ASN B O 4448 C CB . ASN B 192 ? 0.1742 0.2150 0.1491 -0.0037 -0.0078 0.0168 272 ASN B CB 4449 C CG . ASN B 192 ? 0.2434 0.2839 0.2179 -0.0027 -0.0074 0.0196 272 ASN B CG 4450 O OD1 . ASN B 192 ? 0.2376 0.2784 0.2125 -0.0015 -0.0077 0.0220 272 ASN B OD1 4451 N ND2 . ASN B 192 ? 0.3030 0.3428 0.2769 -0.0033 -0.0067 0.0192 272 ASN B ND2 4452 N N . TYR B 193 ? 0.1556 0.1859 0.1341 -0.0039 -0.0074 0.0140 273 TYR B N 4453 C CA . TYR B 193 ? 0.1187 0.1444 0.0983 -0.0039 -0.0069 0.0133 273 TYR B CA 4454 C C . TYR B 193 ? 0.1306 0.1538 0.1117 -0.0029 -0.0072 0.0144 273 TYR B C 4455 O O . TYR B 193 ? 0.1069 0.1319 0.0883 -0.0025 -0.0078 0.0150 273 TYR B O 4456 C CB . TYR B 193 ? 0.1253 0.1500 0.1049 -0.0050 -0.0067 0.0104 273 TYR B CB 4457 C CG . TYR B 193 ? 0.1639 0.1897 0.1424 -0.0060 -0.0061 0.0089 273 TYR B CG 4458 C CD1 . TYR B 193 ? 0.2082 0.2381 0.1853 -0.0066 -0.0063 0.0085 273 TYR B CD1 4459 C CD2 . TYR B 193 ? 0.1757 0.1985 0.1547 -0.0063 -0.0054 0.0077 273 TYR B CD2 4460 C CE1 . TYR B 193 ? 0.2647 0.2956 0.2408 -0.0074 -0.0057 0.0070 273 TYR B CE1 4461 C CE2 . TYR B 193 ? 0.1783 0.2020 0.1563 -0.0071 -0.0048 0.0063 273 TYR B CE2 4462 C CZ . TYR B 193 ? 0.2200 0.2476 0.1965 -0.0077 -0.0049 0.0059 273 TYR B CZ 4463 O OH . TYR B 193 ? 0.2623 0.2909 0.2378 -0.0084 -0.0042 0.0044 273 TYR B OH 4464 N N . HIS B 194 ? 0.0891 0.1084 0.0711 -0.0027 -0.0067 0.0146 274 HIS B N 4465 C CA . HIS B 194 ? 0.0813 0.0979 0.0648 -0.0019 -0.0069 0.0152 274 HIS B CA 4466 C C . HIS B 194 ? 0.0808 0.0939 0.0652 -0.0024 -0.0065 0.0138 274 HIS B C 4467 O O . HIS B 194 ? 0.0730 0.0845 0.0573 -0.0026 -0.0059 0.0137 274 HIS B O 4468 C CB . HIS B 194 ? 0.0713 0.0871 0.0552 -0.0009 -0.0067 0.0178 274 HIS B CB 4469 C CG . HIS B 194 ? 0.1183 0.1324 0.1035 0.0001 -0.0070 0.0186 274 HIS B CG 4470 N ND1 . HIS B 194 ? 0.1157 0.1261 0.1021 0.0004 -0.0066 0.0189 274 HIS B ND1 4471 C CD2 . HIS B 194 ? 0.1012 0.1171 0.0866 0.0007 -0.0076 0.0192 274 HIS B CD2 4472 C CE1 . HIS B 194 ? 0.1359 0.1456 0.1232 0.0012 -0.0069 0.0196 274 HIS B CE1 4473 N NE2 . HIS B 194 ? 0.1275 0.1405 0.1143 0.0014 -0.0075 0.0198 274 HIS B NE2 4474 N N . TYR B 195 ? 0.0863 0.0983 0.0715 -0.0024 -0.0068 0.0127 275 TYR B N 4475 C CA . TYR B 195 ? 0.0857 0.0945 0.0718 -0.0027 -0.0064 0.0113 275 TYR B CA 4476 C C . TYR B 195 ? 0.0921 0.0985 0.0794 -0.0020 -0.0066 0.0120 275 TYR B C 4477 O O . TYR B 195 ? 0.0800 0.0874 0.0678 -0.0017 -0.0071 0.0121 275 TYR B O 4478 C CB . TYR B 195 ? 0.0533 0.0626 0.0391 -0.0036 -0.0064 0.0091 275 TYR B CB 4479 C CG . TYR B 195 ? 0.1087 0.1196 0.0933 -0.0044 -0.0061 0.0080 275 TYR B CG 4480 C CD1 . TYR B 195 ? 0.1024 0.1168 0.0858 -0.0048 -0.0063 0.0080 275 TYR B CD1 4481 C CD2 . TYR B 195 ? 0.0602 0.0693 0.0448 -0.0048 -0.0054 0.0069 275 TYR B CD2 4482 C CE1 . TYR B 195 ? 0.1045 0.1205 0.0868 -0.0056 -0.0059 0.0068 275 TYR B CE1 4483 C CE2 . TYR B 195 ? 0.0760 0.0863 0.0595 -0.0054 -0.0050 0.0057 275 TYR B CE2 4484 C CZ . TYR B 195 ? 0.1386 0.1524 0.1210 -0.0059 -0.0052 0.0056 275 TYR B CZ 4485 O OH . TYR B 195 ? 0.1228 0.1380 0.1041 -0.0066 -0.0047 0.0044 275 TYR B OH 4486 N N . GLU B 196 ? 0.0945 0.0983 0.0826 -0.0018 -0.0062 0.0122 276 GLU B N 4487 C CA . GLU B 196 ? 0.1070 0.1083 0.0964 -0.0013 -0.0062 0.0124 276 GLU B CA 4488 C C . GLU B 196 ? 0.1032 0.1020 0.0931 -0.0017 -0.0058 0.0114 276 GLU B C 4489 O O . GLU B 196 ? 0.0757 0.0744 0.0652 -0.0020 -0.0053 0.0112 276 GLU B O 4490 C CB . GLU B 196 ? 0.1702 0.1709 0.1600 -0.0005 -0.0061 0.0144 276 GLU B CB 4491 C CG . GLU B 196 ? 0.2313 0.2345 0.2207 0.0001 -0.0066 0.0157 276 GLU B CG 4492 C CD . GLU B 196 ? 0.2918 0.2938 0.2820 0.0011 -0.0064 0.0176 276 GLU B CD 4493 O OE1 . GLU B 196 ? 0.3724 0.3718 0.3631 0.0012 -0.0059 0.0180 276 GLU B OE1 4494 O OE2 . GLU B 196 ? 0.2111 0.2148 0.2013 0.0019 -0.0068 0.0186 276 GLU B OE2 4495 N N . GLU B 197 ? 0.0762 0.0733 0.0671 -0.0015 -0.0059 0.0109 277 GLU B N 4496 C CA . GLU B 197 ? 0.0946 0.0896 0.0862 -0.0016 -0.0055 0.0102 277 GLU B CA 4497 C C . GLU B 197 ? 0.0882 0.0833 0.0792 -0.0022 -0.0051 0.0090 277 GLU B C 4498 O O . GLU B 197 ? 0.1118 0.1061 0.1030 -0.0023 -0.0047 0.0091 277 GLU B O 4499 C CB . GLU B 197 ? 0.0878 0.0813 0.0800 -0.0013 -0.0052 0.0113 277 GLU B CB 4500 C CG . GLU B 197 ? 0.1508 0.1438 0.1437 -0.0007 -0.0054 0.0125 277 GLU B CG 4501 C CD . GLU B 197 ? 0.2036 0.1951 0.1971 -0.0005 -0.0049 0.0136 277 GLU B CD 4502 O OE1 . GLU B 197 ? 0.1386 0.1300 0.1316 -0.0008 -0.0045 0.0140 277 GLU B OE1 4503 O OE2 . GLU B 197 ? 0.1613 0.1515 0.1555 0.0000 -0.0049 0.0142 277 GLU B OE2 4504 N N . CYS B 198 ? 0.0892 0.0853 0.0797 -0.0026 -0.0052 0.0079 278 CYS B N 4505 C CA . CYS B 198 ? 0.0935 0.0898 0.0834 -0.0030 -0.0048 0.0067 278 CYS B CA 4506 C C . CYS B 198 ? 0.1011 0.0954 0.0917 -0.0029 -0.0044 0.0060 278 CYS B C 4507 O O . CYS B 198 ? 0.0933 0.0864 0.0847 -0.0027 -0.0046 0.0057 278 CYS B O 4508 C CB . CYS B 198 ? 0.1367 0.1342 0.1259 -0.0035 -0.0048 0.0056 278 CYS B CB 4509 S SG . CYS B 198 ? 0.1664 0.1670 0.1544 -0.0038 -0.0052 0.0061 278 CYS B SG 4510 N N . SER B 199 ? 0.1381 0.1325 0.1286 -0.0030 -0.0039 0.0058 279 SER B N 4511 C CA . SER B 199 ? 0.1107 0.1038 0.1017 -0.0028 -0.0035 0.0050 279 SER B CA 4512 C C . SER B 199 ? 0.1208 0.1141 0.1111 -0.0031 -0.0031 0.0037 279 SER B C 4513 O O . SER B 199 ? 0.1385 0.1330 0.1281 -0.0033 -0.0027 0.0034 279 SER B O 4514 C CB . SER B 199 ? 0.1364 0.1294 0.1278 -0.0028 -0.0032 0.0055 279 SER B CB 4515 O OG . SER B 199 ? 0.1555 0.1479 0.1476 -0.0027 -0.0034 0.0066 279 SER B OG 4516 N N . CYS B 200 ? 0.1025 0.0947 0.0930 -0.0030 -0.0030 0.0029 280 CYS B N 4517 C CA . CYS B 200 ? 0.0845 0.0766 0.0745 -0.0032 -0.0025 0.0016 280 CYS B CA 4518 C C . CYS B 200 ? 0.1129 0.1034 0.1034 -0.0027 -0.0020 0.0010 280 CYS B C 4519 O O . CYS B 200 ? 0.1167 0.1062 0.1080 -0.0023 -0.0021 0.0014 280 CYS B O 4520 C CB . CYS B 200 ? 0.1031 0.0952 0.0928 -0.0036 -0.0028 0.0010 280 CYS B CB 4521 S SG . CYS B 200 ? 0.1522 0.1465 0.1414 -0.0041 -0.0035 0.0017 280 CYS B SG 4522 N N . TYR B 201 ? 0.0610 0.0515 0.0510 -0.0028 -0.0012 0.0001 281 TYR B N 4523 C CA . TYR B 201 ? 0.1049 0.0940 0.0954 -0.0022 -0.0006 -0.0004 281 TYR B CA 4524 C C . TYR B 201 ? 0.1032 0.0917 0.0930 -0.0024 0.0002 -0.0017 281 TYR B C 4525 O O . TYR B 201 ? 0.0738 0.0634 0.0627 -0.0031 0.0004 -0.0023 281 TYR B O 4526 C CB . TYR B 201 ? 0.0919 0.0817 0.0828 -0.0017 -0.0004 0.0001 281 TYR B CB 4527 C CG . TYR B 201 ? 0.1034 0.0945 0.0935 -0.0020 0.0000 -0.0002 281 TYR B CG 4528 C CD1 . TYR B 201 ? 0.0944 0.0870 0.0842 -0.0024 -0.0004 0.0006 281 TYR B CD1 4529 C CD2 . TYR B 201 ? 0.0633 0.0542 0.0530 -0.0019 0.0009 -0.0013 281 TYR B CD2 4530 C CE1 . TYR B 201 ? 0.1058 0.0999 0.0949 -0.0028 0.0000 0.0004 281 TYR B CE1 4531 C CE2 . TYR B 201 ? 0.1078 0.1001 0.0968 -0.0022 0.0013 -0.0016 281 TYR B CE2 4532 C CZ . TYR B 201 ? 0.1040 0.0980 0.0926 -0.0027 0.0008 -0.0008 281 TYR B CZ 4533 O OH . TYR B 201 ? 0.1243 0.1199 0.1122 -0.0030 0.0012 -0.0011 281 TYR B OH 4534 N N . PRO B 202 ? 0.1255 0.1122 0.1156 -0.0019 0.0009 -0.0022 282 PRO B N 4535 C CA . PRO B 202 ? 0.0714 0.0570 0.0610 -0.0020 0.0019 -0.0035 282 PRO B CA 4536 C C . PRO B 202 ? 0.1147 0.1005 0.1042 -0.0015 0.0027 -0.0038 282 PRO B C 4537 O O . PRO B 202 ? 0.1092 0.0955 0.0993 -0.0007 0.0026 -0.0030 282 PRO B O 4538 C CB . PRO B 202 ? 0.0718 0.0552 0.0620 -0.0014 0.0022 -0.0034 282 PRO B CB 4539 C CG . PRO B 202 ? 0.1497 0.1334 0.1407 -0.0009 0.0013 -0.0021 282 PRO B CG 4540 C CD . PRO B 202 ? 0.1097 0.0953 0.1007 -0.0010 0.0007 -0.0014 282 PRO B CD 4541 N N . ASP B 203 ? 0.0849 0.0705 0.0736 -0.0019 0.0035 -0.0051 283 ASP B N 4542 C CA . ASP B 203 ? 0.1565 0.1424 0.1451 -0.0015 0.0044 -0.0056 283 ASP B CA 4543 C C . ASP B 203 ? 0.1404 0.1251 0.1282 -0.0020 0.0055 -0.0073 283 ASP B C 4544 O O . ASP B 203 ? 0.1640 0.1498 0.1509 -0.0031 0.0054 -0.0082 283 ASP B O 4545 C CB . ASP B 203 ? 0.1271 0.1155 0.1153 -0.0018 0.0039 -0.0052 283 ASP B CB 4546 C CG . ASP B 203 ? 0.1939 0.1829 0.1821 -0.0013 0.0048 -0.0056 283 ASP B CG 4547 O OD1 . ASP B 203 ? 0.2230 0.2104 0.2114 -0.0005 0.0058 -0.0062 283 ASP B OD1 4548 O OD2 . ASP B 203 ? 0.2170 0.2081 0.2048 -0.0016 0.0045 -0.0053 283 ASP B OD2 4549 N N . SER B 204 ? 0.1378 0.1205 0.1260 -0.0011 0.0066 -0.0078 284 SER B N 4550 C CA . SER B 204 ? 0.1482 0.1292 0.1357 -0.0016 0.0079 -0.0095 284 SER B CA 4551 C C . SER B 204 ? 0.1614 0.1418 0.1485 -0.0029 0.0077 -0.0104 284 SER B C 4552 O O . SER B 204 ? 0.0926 0.0738 0.0788 -0.0041 0.0081 -0.0118 284 SER B O 4553 C CB . SER B 204 ? 0.2145 0.1971 0.2013 -0.0019 0.0084 -0.0105 284 SER B CB 4554 O OG . SER B 204 ? 0.2261 0.2092 0.2135 -0.0006 0.0088 -0.0098 284 SER B OG 4555 N N . SER B 205 ? 0.0991 0.0784 0.0867 -0.0028 0.0072 -0.0095 285 SER B N 4556 C CA . SER B 205 ? 0.1196 0.0983 0.1069 -0.0040 0.0071 -0.0103 285 SER B CA 4557 C C . SER B 205 ? 0.1472 0.1287 0.1339 -0.0053 0.0059 -0.0104 285 SER B C 4558 O O . SER B 205 ? 0.1408 0.1224 0.1272 -0.0064 0.0058 -0.0111 285 SER B O 4559 C CB . SER B 205 ? 0.1915 0.1680 0.1783 -0.0046 0.0086 -0.0121 285 SER B CB 4560 O OG . SER B 205 ? 0.1665 0.1401 0.1539 -0.0033 0.0097 -0.0118 285 SER B OG 4561 N N . GLU B 206 ? 0.1437 0.1276 0.1302 -0.0051 0.0052 -0.0096 286 GLU B N 4562 C CA . GLU B 206 ? 0.1469 0.1335 0.1328 -0.0061 0.0041 -0.0094 286 GLU B CA 4563 C C . GLU B 206 ? 0.1515 0.1394 0.1380 -0.0054 0.0029 -0.0075 286 GLU B C 4564 O O . GLU B 206 ? 0.1517 0.1389 0.1389 -0.0043 0.0029 -0.0066 286 GLU B O 4565 C CB . GLU B 206 ? 0.1984 0.1870 0.1833 -0.0068 0.0045 -0.0105 286 GLU B CB 4566 C CG . GLU B 206 ? 0.2237 0.2111 0.2079 -0.0076 0.0057 -0.0126 286 GLU B CG 4567 C CD . GLU B 206 ? 0.4184 0.4084 0.4015 -0.0086 0.0059 -0.0138 286 GLU B CD 4568 O OE1 . GLU B 206 ? 0.4328 0.4256 0.4155 -0.0086 0.0050 -0.0128 286 GLU B OE1 4569 O OE2 . GLU B 206 ? 0.4992 0.4883 0.4817 -0.0093 0.0071 -0.0157 286 GLU B OE2 4570 N N . ILE B 207 ? 0.1162 0.1061 0.1025 -0.0060 0.0019 -0.0070 287 ILE B N 4571 C CA . ILE B 207 ? 0.0917 0.0825 0.0786 -0.0055 0.0008 -0.0053 287 ILE B CA 4572 C C . ILE B 207 ? 0.0811 0.0744 0.0674 -0.0057 0.0004 -0.0046 287 ILE B C 4573 O O . ILE B 207 ? 0.1113 0.1065 0.0967 -0.0065 0.0003 -0.0053 287 ILE B O 4574 C CB . ILE B 207 ? 0.0940 0.0849 0.0812 -0.0058 0.0000 -0.0048 287 ILE B CB 4575 C CG1 . ILE B 207 ? 0.1124 0.1009 0.1001 -0.0057 0.0006 -0.0055 287 ILE B CG1 4576 C CG2 . ILE B 207 ? 0.0717 0.0630 0.0596 -0.0051 -0.0008 -0.0031 287 ILE B CG2 4577 C CD1 . ILE B 207 ? 0.1736 0.1599 0.1620 -0.0046 0.0010 -0.0049 287 ILE B CD1 4578 N N . THR B 208 ? 0.0861 0.0795 0.0729 -0.0049 0.0001 -0.0034 288 THR B N 4579 C CA . THR B 208 ? 0.1408 0.1363 0.1271 -0.0050 -0.0003 -0.0025 288 THR B CA 4580 C C . THR B 208 ? 0.1266 0.1224 0.1137 -0.0047 -0.0012 -0.0008 288 THR B C 4581 O O . THR B 208 ? 0.0927 0.0869 0.0807 -0.0041 -0.0013 -0.0003 288 THR B O 4582 C CB . THR B 208 ? 0.1742 0.1699 0.1605 -0.0046 0.0003 -0.0025 288 THR B CB 4583 O OG1 . THR B 208 ? 0.1318 0.1275 0.1175 -0.0050 0.0012 -0.0041 288 THR B OG1 4584 C CG2 . THR B 208 ? 0.1163 0.1141 0.1022 -0.0048 0.0000 -0.0014 288 THR B CG2 4585 N N . CYS B 209 ? 0.0581 0.0557 0.0446 -0.0050 -0.0018 -0.0001 289 CYS B N 4586 C CA . CYS B 209 ? 0.0763 0.0740 0.0635 -0.0046 -0.0025 0.0015 289 CYS B CA 4587 C C . CYS B 209 ? 0.0992 0.0985 0.0859 -0.0046 -0.0026 0.0027 289 CYS B C 4588 O O . CYS B 209 ? 0.1055 0.1068 0.0912 -0.0051 -0.0026 0.0025 289 CYS B O 4589 C CB . CYS B 209 ? 0.0946 0.0929 0.0817 -0.0049 -0.0032 0.0017 289 CYS B CB 4590 S SG . CYS B 209 ? 0.1602 0.1566 0.1479 -0.0049 -0.0031 0.0005 289 CYS B SG 4591 N N . VAL B 210 ? 0.0866 0.0850 0.0741 -0.0042 -0.0027 0.0038 290 VAL B N 4592 C CA . VAL B 210 ? 0.0870 0.0866 0.0742 -0.0042 -0.0028 0.0052 290 VAL B CA 4593 C C . VAL B 210 ? 0.0974 0.0964 0.0853 -0.0038 -0.0033 0.0066 290 VAL B C 4594 O O . VAL B 210 ? 0.0648 0.0621 0.0537 -0.0035 -0.0034 0.0067 290 VAL B O 4595 C CB . VAL B 210 ? 0.0679 0.0671 0.0554 -0.0041 -0.0022 0.0053 290 VAL B CB 4596 C CG1 . VAL B 210 ? 0.0677 0.0680 0.0550 -0.0042 -0.0022 0.0068 290 VAL B CG1 4597 C CG2 . VAL B 210 ? 0.0792 0.0791 0.0662 -0.0043 -0.0016 0.0039 290 VAL B CG2 4598 N N . CYS B 211 ? 0.0751 0.0757 0.0624 -0.0038 -0.0036 0.0077 291 CYS B N 4599 C CA . CYS B 211 ? 0.0786 0.0788 0.0664 -0.0034 -0.0041 0.0089 291 CYS B CA 4600 C C . CYS B 211 ? 0.0791 0.0797 0.0669 -0.0031 -0.0041 0.0107 291 CYS B C 4601 O O . CYS B 211 ? 0.0874 0.0882 0.0749 -0.0034 -0.0036 0.0111 291 CYS B O 4602 C CB . CYS B 211 ? 0.0757 0.0774 0.0630 -0.0035 -0.0047 0.0085 291 CYS B CB 4603 S SG . CYS B 211 ? 0.1199 0.1213 0.1070 -0.0040 -0.0045 0.0062 291 CYS B SG 4604 N N . ARG B 212 ? 0.0584 0.0590 0.0464 -0.0027 -0.0045 0.0119 292 ARG B N 4605 C CA . ARG B 212 ? 0.0886 0.0892 0.0767 -0.0023 -0.0043 0.0138 292 ARG B CA 4606 C C . ARG B 212 ? 0.0816 0.0846 0.0689 -0.0019 -0.0048 0.0150 292 ARG B C 4607 O O . ARG B 212 ? 0.1065 0.1101 0.0939 -0.0016 -0.0053 0.0149 292 ARG B O 4608 C CB . ARG B 212 ? 0.0756 0.0737 0.0650 -0.0018 -0.0043 0.0144 292 ARG B CB 4609 C CG . ARG B 212 ? 0.0895 0.0871 0.0791 -0.0012 -0.0042 0.0164 292 ARG B CG 4610 C CD . ARG B 212 ? 0.1404 0.1354 0.1313 -0.0008 -0.0041 0.0166 292 ARG B CD 4611 N NE . ARG B 212 ? 0.0934 0.0877 0.0846 -0.0001 -0.0039 0.0185 292 ARG B NE 4612 C CZ . ARG B 212 ? 0.1768 0.1687 0.1691 0.0002 -0.0036 0.0189 292 ARG B CZ 4613 N NH1 . ARG B 212 ? 0.0896 0.0799 0.0828 -0.0001 -0.0036 0.0175 292 ARG B NH1 4614 N NH2 . ARG B 212 ? 0.1582 0.1493 0.1508 0.0009 -0.0033 0.0206 292 ARG B NH2 4615 N N . ASP B 213 ? 0.0820 0.0865 0.0683 -0.0019 -0.0045 0.0161 293 ASP B N 4616 C CA . ASP B 213 ? 0.0819 0.0890 0.0674 -0.0015 -0.0049 0.0175 293 ASP B CA 4617 C C . ASP B 213 ? 0.0965 0.1023 0.0826 -0.0006 -0.0046 0.0197 293 ASP B C 4618 O O . ASP B 213 ? 0.0822 0.0871 0.0683 -0.0007 -0.0040 0.0208 293 ASP B O 4619 C CB . ASP B 213 ? 0.0697 0.0794 0.0538 -0.0020 -0.0046 0.0176 293 ASP B CB 4620 C CG . ASP B 213 ? 0.1187 0.1315 0.1018 -0.0015 -0.0049 0.0193 293 ASP B CG 4621 O OD1 . ASP B 213 ? 0.1099 0.1223 0.0935 -0.0005 -0.0051 0.0209 293 ASP B OD1 4622 O OD2 . ASP B 213 ? 0.1144 0.1301 0.0962 -0.0019 -0.0049 0.0190 293 ASP B OD2 4623 N N . ASN B 214 ? 0.1035 0.1090 0.0903 0.0001 -0.0051 0.0203 294 ASN B N 4624 C CA . ASN B 214 ? 0.1065 0.1102 0.0940 0.0010 -0.0047 0.0223 294 ASN B CA 4625 C C . ASN B 214 ? 0.1145 0.1207 0.1012 0.0018 -0.0048 0.0245 294 ASN B C 4626 O O . ASN B 214 ? 0.1147 0.1196 0.1018 0.0027 -0.0045 0.0264 294 ASN B O 4627 C CB . ASN B 214 ? 0.1031 0.1052 0.0919 0.0016 -0.0050 0.0219 294 ASN B CB 4628 C CG . ASN B 214 ? 0.1728 0.1716 0.1626 0.0021 -0.0044 0.0231 294 ASN B CG 4629 O OD1 . ASN B 214 ? 0.1444 0.1410 0.1347 0.0015 -0.0038 0.0227 294 ASN B OD1 4630 N ND2 . ASN B 214 ? 0.1591 0.1578 0.1494 0.0032 -0.0045 0.0246 294 ASN B ND2 4631 N N . TRP B 215 ? 0.1267 0.1365 0.1121 0.0015 -0.0052 0.0241 295 TRP B N 4632 C CA . TRP B 215 ? 0.1220 0.1350 0.1065 0.0023 -0.0055 0.0260 295 TRP B CA 4633 C C . TRP B 215 ? 0.1322 0.1460 0.1156 0.0022 -0.0049 0.0274 295 TRP B C 4634 O O . TRP B 215 ? 0.1008 0.1141 0.0843 0.0031 -0.0045 0.0298 295 TRP B O 4635 C CB . TRP B 215 ? 0.0993 0.1161 0.0829 0.0019 -0.0063 0.0246 295 TRP B CB 4636 C CG . TRP B 215 ? 0.1145 0.1356 0.0971 0.0025 -0.0067 0.0262 295 TRP B CG 4637 C CD1 . TRP B 215 ? 0.1707 0.1924 0.1531 0.0037 -0.0065 0.0289 295 TRP B CD1 4638 C CD2 . TRP B 215 ? 0.1129 0.1383 0.0944 0.0019 -0.0074 0.0251 295 TRP B CD2 4639 N NE1 . TRP B 215 ? 0.1435 0.1700 0.1247 0.0040 -0.0071 0.0297 295 TRP B NE1 4640 C CE2 . TRP B 215 ? 0.1243 0.1533 0.1050 0.0029 -0.0076 0.0273 295 TRP B CE2 4641 C CE3 . TRP B 215 ? 0.1080 0.1347 0.0892 0.0007 -0.0078 0.0224 295 TRP B CE3 4642 C CZ2 . TRP B 215 ? 0.1562 0.1901 0.1356 0.0025 -0.0083 0.0268 295 TRP B CZ2 4643 C CZ3 . TRP B 215 ? 0.1496 0.1809 0.1296 0.0003 -0.0083 0.0218 295 TRP B CZ3 4644 C CH2 . TRP B 215 ? 0.1403 0.1754 0.1194 0.0012 -0.0086 0.0240 295 TRP B CH2 4645 N N . HIS B 216 ? 0.1205 0.1354 0.1030 0.0011 -0.0048 0.0260 296 HIS B N 4646 C CA . HIS B 216 ? 0.1443 0.1606 0.1257 0.0009 -0.0042 0.0273 296 HIS B CA 4647 C C . HIS B 216 ? 0.1351 0.1512 0.1161 -0.0004 -0.0038 0.0255 296 HIS B C 4648 O O . HIS B 216 ? 0.1066 0.1255 0.0862 -0.0008 -0.0037 0.0255 296 HIS B O 4649 C CB . HIS B 216 ? 0.1162 0.1370 0.0962 0.0013 -0.0047 0.0284 296 HIS B CB 4650 C CG . HIS B 216 ? 0.1661 0.1901 0.1455 0.0006 -0.0055 0.0262 296 HIS B CG 4651 N ND1 . HIS B 216 ? 0.1290 0.1574 0.1073 0.0009 -0.0061 0.0268 296 HIS B ND1 4652 C CD2 . HIS B 216 ? 0.1332 0.1566 0.1128 -0.0004 -0.0056 0.0235 296 HIS B CD2 4653 C CE1 . HIS B 216 ? 0.1417 0.1720 0.1197 0.0000 -0.0066 0.0243 296 HIS B CE1 4654 N NE2 . HIS B 216 ? 0.1415 0.1685 0.1202 -0.0008 -0.0063 0.0223 296 HIS B NE2 4655 N N . GLY B 217 ? 0.0869 0.0999 0.0689 -0.0009 -0.0036 0.0240 297 GLY B N 4656 C CA . GLY B 217 ? 0.1091 0.1219 0.0909 -0.0019 -0.0031 0.0223 297 GLY B CA 4657 C C . GLY B 217 ? 0.1178 0.1270 0.1007 -0.0022 -0.0025 0.0220 297 GLY B C 4658 O O . GLY B 217 ? 0.1058 0.1126 0.0900 -0.0020 -0.0026 0.0214 297 GLY B O 4659 N N . SER B 218 ? 0.1266 0.1358 0.1092 -0.0027 -0.0018 0.0225 298 SER B N 4660 C CA . SER B 218 ? 0.1236 0.1299 0.1074 -0.0031 -0.0011 0.0222 298 SER B CA 4661 C C . SER B 218 ? 0.1314 0.1378 0.1153 -0.0039 -0.0010 0.0198 298 SER B C 4662 O O . SER B 218 ? 0.1106 0.1149 0.0955 -0.0042 -0.0006 0.0192 298 SER B O 4663 C CB . SER B 218 ? 0.1084 0.1145 0.0920 -0.0033 -0.0002 0.0240 298 SER B CB 4664 O OG . SER B 218 ? 0.1752 0.1843 0.1572 -0.0036 -0.0001 0.0244 298 SER B OG 4665 N N . ASN B 219 ? 0.1110 0.1198 0.0939 -0.0041 -0.0014 0.0186 299 ASN B N 4666 C CA . ASN B 219 ? 0.1062 0.1148 0.0893 -0.0045 -0.0014 0.0163 299 ASN B CA 4667 C C . ASN B 219 ? 0.0912 0.0991 0.0748 -0.0043 -0.0021 0.0151 299 ASN B C 4668 O O . ASN B 219 ? 0.1201 0.1285 0.1036 -0.0038 -0.0026 0.0160 299 ASN B O 4669 C CB . ASN B 219 ? 0.0846 0.0959 0.0663 -0.0050 -0.0011 0.0154 299 ASN B CB 4670 C CG . ASN B 219 ? 0.1396 0.1539 0.1200 -0.0049 -0.0016 0.0158 299 ASN B CG 4671 O OD1 . ASN B 219 ? 0.1042 0.1188 0.0846 -0.0043 -0.0020 0.0174 299 ASN B OD1 4672 N ND2 . ASN B 219 ? 0.0889 0.1055 0.0682 -0.0054 -0.0015 0.0144 299 ASN B ND2 4673 N N . ARG B 220 ? 0.1054 0.1124 0.0895 -0.0045 -0.0020 0.0132 300 ARG B N 4674 C CA . ARG B 220 ? 0.0724 0.0784 0.0571 -0.0043 -0.0026 0.0121 300 ARG B CA 4675 C C . ARG B 220 ? 0.0796 0.0875 0.0632 -0.0046 -0.0028 0.0107 300 ARG B C 4676 O O . ARG B 220 ? 0.0834 0.0925 0.0663 -0.0051 -0.0024 0.0096 300 ARG B O 4677 C CB . ARG B 220 ? 0.0706 0.0742 0.0564 -0.0043 -0.0023 0.0110 300 ARG B CB 4678 C CG . ARG B 220 ? 0.0870 0.0886 0.0739 -0.0041 -0.0021 0.0121 300 ARG B CG 4679 C CD . ARG B 220 ? 0.0757 0.0752 0.0638 -0.0040 -0.0022 0.0111 300 ARG B CD 4680 N NE . ARG B 220 ? 0.0940 0.0918 0.0832 -0.0040 -0.0020 0.0120 300 ARG B NE 4681 C CZ . ARG B 220 ? 0.1064 0.1030 0.0961 -0.0036 -0.0022 0.0130 300 ARG B CZ 4682 N NH1 . ARG B 220 ? 0.0874 0.0845 0.0768 -0.0032 -0.0028 0.0132 300 ARG B NH1 4683 N NH2 . ARG B 220 ? 0.0853 0.0803 0.0760 -0.0037 -0.0019 0.0136 300 ARG B NH2 4684 N N . PRO B 221 ? 0.0767 0.0851 0.0603 -0.0044 -0.0034 0.0107 301 PRO B N 4685 C CA . PRO B 221 ? 0.0850 0.0951 0.0679 -0.0049 -0.0037 0.0091 301 PRO B CA 4686 C C . PRO B 221 ? 0.0997 0.1078 0.0832 -0.0051 -0.0034 0.0072 301 PRO B C 4687 O O . PRO B 221 ? 0.0902 0.0958 0.0748 -0.0047 -0.0034 0.0073 301 PRO B O 4688 C CB . PRO B 221 ? 0.0835 0.0945 0.0664 -0.0045 -0.0044 0.0099 301 PRO B CB 4689 C CG . PRO B 221 ? 0.0944 0.1029 0.0786 -0.0038 -0.0045 0.0111 301 PRO B CG 4690 C CD . PRO B 221 ? 0.0861 0.0936 0.0704 -0.0038 -0.0039 0.0121 301 PRO B CD 4691 N N . TRP B 222 ? 0.0726 0.0817 0.0553 -0.0057 -0.0032 0.0055 302 TRP B N 4692 C CA . TRP B 222 ? 0.0956 0.1028 0.0789 -0.0058 -0.0029 0.0037 302 TRP B CA 4693 C C . TRP B 222 ? 0.0804 0.0887 0.0631 -0.0064 -0.0030 0.0022 302 TRP B C 4694 O O . TRP B 222 ? 0.1003 0.1114 0.0820 -0.0069 -0.0032 0.0021 302 TRP B O 4695 C CB . TRP B 222 ? 0.0765 0.0828 0.0598 -0.0059 -0.0021 0.0028 302 TRP B CB 4696 C CG . TRP B 222 ? 0.0971 0.1058 0.0791 -0.0065 -0.0016 0.0021 302 TRP B CG 4697 C CD1 . TRP B 222 ? 0.1016 0.1119 0.0830 -0.0065 -0.0014 0.0030 302 TRP B CD1 4698 C CD2 . TRP B 222 ? 0.0815 0.0911 0.0626 -0.0071 -0.0013 0.0001 302 TRP B CD2 4699 N NE1 . TRP B 222 ? 0.0920 0.1043 0.0721 -0.0071 -0.0010 0.0018 302 TRP B NE1 4700 C CE2 . TRP B 222 ? 0.0955 0.1075 0.0755 -0.0075 -0.0009 -0.0001 302 TRP B CE2 4701 C CE3 . TRP B 222 ? 0.0883 0.0970 0.0695 -0.0075 -0.0011 -0.0015 302 TRP B CE3 4702 C CZ2 . TRP B 222 ? 0.1405 0.1539 0.1194 -0.0083 -0.0004 -0.0019 302 TRP B CZ2 4703 C CZ3 . TRP B 222 ? 0.1174 0.1274 0.0976 -0.0084 -0.0006 -0.0033 302 TRP B CZ3 4704 C CH2 . TRP B 222 ? 0.1488 0.1611 0.1278 -0.0087 -0.0002 -0.0036 302 TRP B CH2 4705 N N . VAL B 223 ? 0.1067 0.1130 0.0901 -0.0065 -0.0029 0.0011 303 VAL B N 4706 C CA . VAL B 223 ? 0.0765 0.0833 0.0594 -0.0072 -0.0028 -0.0005 303 VAL B CA 4707 C C . VAL B 223 ? 0.1096 0.1137 0.0931 -0.0072 -0.0021 -0.0020 303 VAL B C 4708 O O . VAL B 223 ? 0.0932 0.0949 0.0777 -0.0066 -0.0020 -0.0014 303 VAL B O 4709 C CB . VAL B 223 ? 0.0884 0.0959 0.0718 -0.0072 -0.0036 -0.0001 303 VAL B CB 4710 C CG1 . VAL B 223 ? 0.0784 0.0832 0.0630 -0.0065 -0.0039 0.0009 303 VAL B CG1 4711 C CG2 . VAL B 223 ? 0.1058 0.1139 0.0887 -0.0082 -0.0034 -0.0019 303 VAL B CG2 4712 N N . SER B 224 ? 0.0826 0.0869 0.0653 -0.0080 -0.0014 -0.0038 304 SER B N 4713 C CA . SER B 224 ? 0.0933 0.0950 0.0765 -0.0079 -0.0006 -0.0052 304 SER B CA 4714 C C . SER B 224 ? 0.1342 0.1360 0.1170 -0.0090 -0.0003 -0.0069 304 SER B C 4715 O O . SER B 224 ? 0.1190 0.1234 0.1009 -0.0098 -0.0006 -0.0075 304 SER B O 4716 C CB . SER B 224 ? 0.0997 0.1009 0.0825 -0.0078 0.0004 -0.0059 304 SER B CB 4717 O OG . SER B 224 ? 0.1940 0.1976 0.1756 -0.0086 0.0007 -0.0070 304 SER B OG 4718 N N . PHE B 225 ? 0.0816 0.0806 0.0651 -0.0089 0.0002 -0.0077 305 PHE B N 4719 C CA . PHE B 225 ? 0.1251 0.1238 0.1083 -0.0099 0.0006 -0.0093 305 PHE B CA 4720 C C . PHE B 225 ? 0.1160 0.1112 0.0997 -0.0097 0.0016 -0.0103 305 PHE B C 4721 O O . PHE B 225 ? 0.1010 0.0941 0.0856 -0.0086 0.0018 -0.0094 305 PHE B O 4722 C CB . PHE B 225 ? 0.0612 0.0612 0.0448 -0.0102 -0.0004 -0.0086 305 PHE B CB 4723 C CG . PHE B 225 ? 0.0871 0.0855 0.0718 -0.0091 -0.0010 -0.0069 305 PHE B CG 4724 C CD1 . PHE B 225 ? 0.1075 0.1033 0.0931 -0.0088 -0.0007 -0.0071 305 PHE B CD1 4725 C CD2 . PHE B 225 ? 0.1161 0.1156 0.1010 -0.0083 -0.0018 -0.0050 305 PHE B CD2 4726 C CE1 . PHE B 225 ? 0.0856 0.0801 0.0721 -0.0079 -0.0013 -0.0056 305 PHE B CE1 4727 C CE2 . PHE B 225 ? 0.0924 0.0905 0.0783 -0.0074 -0.0023 -0.0037 305 PHE B CE2 4728 C CZ . PHE B 225 ? 0.0630 0.0587 0.0497 -0.0072 -0.0020 -0.0040 305 PHE B CZ 4729 N N . ASN B 226 ? 0.0935 0.0881 0.0768 -0.0108 0.0024 -0.0122 306 ASN B N 4730 C CA . ASN B 226 ? 0.1452 0.1364 0.1290 -0.0106 0.0036 -0.0131 306 ASN B CA 4731 C C . ASN B 226 ? 0.0967 0.0868 0.0813 -0.0108 0.0031 -0.0127 306 ASN B C 4732 O O . ASN B 226 ? 0.0732 0.0654 0.0579 -0.0110 0.0020 -0.0118 306 ASN B O 4733 C CB . ASN B 226 ? 0.1467 0.1372 0.1297 -0.0117 0.0049 -0.0154 306 ASN B CB 4734 C CG . ASN B 226 ? 0.1416 0.1347 0.1239 -0.0134 0.0046 -0.0168 306 ASN B CG 4735 O OD1 . ASN B 226 ? 0.1086 0.1028 0.0911 -0.0139 0.0038 -0.0163 306 ASN B OD1 4736 N ND2 . ASN B 226 ? 0.1566 0.1507 0.1379 -0.0144 0.0054 -0.0186 306 ASN B ND2 4737 N N . GLN B 227 ? 0.1036 0.0905 0.0885 -0.0108 0.0042 -0.0134 308 GLN B N 4738 C CA . GLN B 227 ? 0.1163 0.1021 0.1019 -0.0110 0.0039 -0.0131 308 GLN B CA 4739 C C . GLN B 227 ? 0.1324 0.1204 0.1177 -0.0125 0.0035 -0.0141 308 GLN B C 4740 O O . GLN B 227 ? 0.1337 0.1219 0.1195 -0.0127 0.0028 -0.0134 308 GLN B O 4741 C CB . GLN B 227 ? 0.1364 0.1183 0.1225 -0.0106 0.0052 -0.0136 308 GLN B CB 4742 C CG . GLN B 227 ? 0.1129 0.0930 0.0996 -0.0089 0.0055 -0.0123 308 GLN B CG 4743 C CD . GLN B 227 ? 0.1951 0.1714 0.1820 -0.0084 0.0070 -0.0128 308 GLN B CD 4744 O OE1 . GLN B 227 ? 0.2391 0.2137 0.2264 -0.0086 0.0072 -0.0127 308 GLN B OE1 4745 N NE2 . GLN B 227 ? 0.2485 0.2237 0.2352 -0.0078 0.0080 -0.0133 308 GLN B NE2 4746 N N . ASN B 228 ? 0.1386 0.1284 0.1229 -0.0138 0.0038 -0.0157 309 ASN B N 4747 C CA . ASN B 228 ? 0.1340 0.1264 0.1179 -0.0154 0.0035 -0.0168 309 ASN B CA 4748 C C . ASN B 228 ? 0.0977 0.0943 0.0814 -0.0153 0.0019 -0.0156 309 ASN B C 4749 O O . ASN B 228 ? 0.1217 0.1214 0.1050 -0.0164 0.0015 -0.0163 309 ASN B O 4750 C CB . ASN B 228 ? 0.1453 0.1378 0.1283 -0.0169 0.0047 -0.0193 309 ASN B CB 4751 C CG . ASN B 228 ? 0.3156 0.3042 0.2990 -0.0175 0.0062 -0.0206 309 ASN B CG 4752 O OD1 . ASN B 228 ? 0.3420 0.3284 0.3262 -0.0169 0.0062 -0.0197 309 ASN B OD1 4753 N ND2 . ASN B 228 ? 0.4328 0.4206 0.4155 -0.0186 0.0075 -0.0228 309 ASN B ND2 4754 N N . LEU B 229 ? 0.1137 0.1106 0.0976 -0.0138 0.0013 -0.0138 310 LEU B N 4755 C CA . LEU B 229 ? 0.0890 0.0893 0.0728 -0.0134 0.0000 -0.0123 310 LEU B CA 4756 C C . LEU B 229 ? 0.1077 0.1114 0.0903 -0.0142 -0.0001 -0.0131 310 LEU B C 4757 O O . LEU B 229 ? 0.1218 0.1289 0.1041 -0.0142 -0.0012 -0.0121 310 LEU B O 4758 C CB . LEU B 229 ? 0.1114 0.1132 0.0957 -0.0136 -0.0010 -0.0116 310 LEU B CB 4759 C CG . LEU B 229 ? 0.1223 0.1212 0.1078 -0.0128 -0.0010 -0.0107 310 LEU B CG 4760 C CD1 . LEU B 229 ? 0.1152 0.1162 0.1013 -0.0129 -0.0021 -0.0098 310 LEU B CD1 4761 C CD2 . LEU B 229 ? 0.1071 0.1039 0.0930 -0.0113 -0.0011 -0.0091 310 LEU B CD2 4762 N N . GLU B 230 ? 0.0976 0.1004 0.0795 -0.0148 0.0010 -0.0148 311 GLU B N 4763 C CA . GLU B 230 ? 0.1160 0.1218 0.0967 -0.0154 0.0010 -0.0155 311 GLU B CA 4764 C C . GLU B 230 ? 0.1433 0.1492 0.1240 -0.0140 0.0006 -0.0136 311 GLU B C 4765 O O . GLU B 230 ? 0.1664 0.1693 0.1475 -0.0131 0.0013 -0.0134 311 GLU B O 4766 C CB . GLU B 230 ? 0.1404 0.1448 0.1204 -0.0165 0.0025 -0.0180 311 GLU B CB 4767 C CG . GLU B 230 ? 0.2074 0.2116 0.1874 -0.0181 0.0030 -0.0199 311 GLU B CG 4768 C CD . GLU B 230 ? 0.3452 0.3473 0.3247 -0.0191 0.0047 -0.0225 311 GLU B CD 4769 O OE1 . GLU B 230 ? 0.2939 0.2931 0.2735 -0.0182 0.0056 -0.0224 311 GLU B OE1 4770 O OE2 . GLU B 230 ? 0.3287 0.3319 0.3077 -0.0209 0.0052 -0.0245 311 GLU B OE2 4771 N N . TYR B 231 ? 0.0855 0.0948 0.0658 -0.0138 -0.0004 -0.0123 312 TYR B N 4772 C CA . TYR B 231 ? 0.0898 0.0990 0.0702 -0.0125 -0.0009 -0.0102 312 TYR B CA 4773 C C . TYR B 231 ? 0.1610 0.1731 0.1403 -0.0126 -0.0008 -0.0101 312 TYR B C 4774 O O . TYR B 231 ? 0.1166 0.1315 0.0949 -0.0137 -0.0007 -0.0114 312 TYR B O 4775 C CB . TYR B 231 ? 0.1067 0.1168 0.0879 -0.0117 -0.0021 -0.0081 312 TYR B CB 4776 C CG . TYR B 231 ? 0.1412 0.1554 0.1217 -0.0122 -0.0029 -0.0078 312 TYR B CG 4777 C CD1 . TYR B 231 ? 0.1257 0.1429 0.1054 -0.0120 -0.0034 -0.0066 312 TYR B CD1 4778 C CD2 . TYR B 231 ? 0.1256 0.1409 0.1064 -0.0130 -0.0033 -0.0085 312 TYR B CD2 4779 C CE1 . TYR B 231 ? 0.1335 0.1548 0.1127 -0.0123 -0.0042 -0.0061 312 TYR B CE1 4780 C CE2 . TYR B 231 ? 0.1312 0.1507 0.1114 -0.0135 -0.0041 -0.0082 312 TYR B CE2 4781 C CZ . TYR B 231 ? 0.1244 0.1470 0.1039 -0.0131 -0.0046 -0.0070 312 TYR B CZ 4782 O OH . TYR B 231 ? 0.1242 0.1512 0.1031 -0.0134 -0.0054 -0.0065 312 TYR B OH 4783 N N . GLN B 232 ? 0.0508 0.0621 0.0303 -0.0115 -0.0009 -0.0085 313 GLN B N 4784 C CA . GLN B 232 ? 0.1185 0.1325 0.0971 -0.0114 -0.0010 -0.0078 313 GLN B CA 4785 C C . GLN B 232 ? 0.1212 0.1352 0.1003 -0.0103 -0.0018 -0.0052 313 GLN B C 4786 O O . GLN B 232 ? 0.0640 0.0753 0.0443 -0.0095 -0.0020 -0.0043 313 GLN B O 4787 C CB . GLN B 232 ? 0.1404 0.1532 0.1186 -0.0114 0.0001 -0.0089 313 GLN B CB 4788 C CG . GLN B 232 ? 0.1892 0.2018 0.1668 -0.0126 0.0011 -0.0116 313 GLN B CG 4789 C CD . GLN B 232 ? 0.4239 0.4353 0.4011 -0.0124 0.0022 -0.0126 313 GLN B CD 4790 O OE1 . GLN B 232 ? 0.5008 0.5092 0.4789 -0.0114 0.0027 -0.0122 313 GLN B OE1 4791 N NE2 . GLN B 232 ? 0.4687 0.4826 0.4446 -0.0133 0.0027 -0.0140 313 GLN B NE2 4792 N N . ILE B 233 ? 0.1112 0.1284 0.0895 -0.0102 -0.0023 -0.0040 314 ILE B N 4793 C CA . ILE B 233 ? 0.0699 0.0871 0.0487 -0.0092 -0.0029 -0.0015 314 ILE B CA 4794 C C . ILE B 233 ? 0.1291 0.1479 0.1071 -0.0090 -0.0027 -0.0006 314 ILE B C 4795 O O . ILE B 233 ? 0.0978 0.1187 0.0746 -0.0097 -0.0022 -0.0017 314 ILE B O 4796 C CB . ILE B 233 ? 0.1113 0.1309 0.0901 -0.0091 -0.0039 -0.0002 314 ILE B CB 4797 C CG1 . ILE B 233 ? 0.1243 0.1482 0.1017 -0.0099 -0.0041 -0.0009 314 ILE B CG1 4798 C CG2 . ILE B 233 ? 0.1071 0.1250 0.0869 -0.0091 -0.0042 -0.0009 314 ILE B CG2 4799 C CD1 . ILE B 233 ? 0.1093 0.1361 0.0866 -0.0096 -0.0051 0.0006 314 ILE B CD1 4800 N N . GLY B 234 ? 0.1012 0.1189 0.0798 -0.0081 -0.0029 0.0014 315 GLY B N 4801 C CA . GLY B 234 ? 0.1055 0.1246 0.0835 -0.0080 -0.0026 0.0026 315 GLY B CA 4802 C C . GLY B 234 ? 0.1008 0.1180 0.0798 -0.0071 -0.0027 0.0047 315 GLY B C 4803 O O . GLY B 234 ? 0.0998 0.1150 0.0799 -0.0066 -0.0031 0.0054 315 GLY B O 4804 N N . TYR B 235 ? 0.0817 0.0996 0.0603 -0.0070 -0.0023 0.0057 316 TYR B N 4805 C CA . TYR B 235 ? 0.0996 0.1157 0.0791 -0.0063 -0.0022 0.0075 316 TYR B CA 4806 C C . TYR B 235 ? 0.0928 0.1079 0.0724 -0.0065 -0.0014 0.0069 316 TYR B C 4807 O O . TYR B 235 ? 0.1126 0.1293 0.0913 -0.0069 -0.0009 0.0058 316 TYR B O 4808 C CB . TYR B 235 ? 0.1098 0.1277 0.0886 -0.0060 -0.0025 0.0098 316 TYR B CB 4809 C CG . TYR B 235 ? 0.1132 0.1312 0.0924 -0.0055 -0.0033 0.0111 316 TYR B CG 4810 C CD1 . TYR B 235 ? 0.1409 0.1612 0.1194 -0.0057 -0.0039 0.0106 316 TYR B CD1 4811 C CD2 . TYR B 235 ? 0.0949 0.1108 0.0752 -0.0048 -0.0034 0.0129 316 TYR B CD2 4812 C CE1 . TYR B 235 ? 0.1458 0.1665 0.1249 -0.0051 -0.0046 0.0118 316 TYR B CE1 4813 C CE2 . TYR B 235 ? 0.1095 0.1254 0.0903 -0.0041 -0.0040 0.0141 316 TYR B CE2 4814 C CZ . TYR B 235 ? 0.1246 0.1429 0.1047 -0.0042 -0.0046 0.0136 316 TYR B CZ 4815 O OH . TYR B 235 ? 0.1078 0.1264 0.0884 -0.0035 -0.0052 0.0148 316 TYR B OH 4816 N N . ILE B 236 ? 0.0644 0.0769 0.0453 -0.0061 -0.0012 0.0075 317 ILE B N 4817 C CA . ILE B 236 ? 0.0734 0.0853 0.0546 -0.0061 -0.0005 0.0071 317 ILE B CA 4818 C C . ILE B 236 ? 0.0918 0.1059 0.0721 -0.0064 -0.0001 0.0084 317 ILE B C 4819 O O . ILE B 236 ? 0.0863 0.1006 0.0665 -0.0062 -0.0004 0.0103 317 ILE B O 4820 C CB . ILE B 236 ? 0.0872 0.0964 0.0700 -0.0057 -0.0004 0.0076 317 ILE B CB 4821 C CG1 . ILE B 236 ? 0.0780 0.0853 0.0616 -0.0055 -0.0007 0.0064 317 ILE B CG1 4822 C CG2 . ILE B 236 ? 0.0682 0.0773 0.0514 -0.0058 0.0003 0.0073 317 ILE B CG2 4823 C CD1 . ILE B 236 ? 0.0861 0.0910 0.0712 -0.0051 -0.0008 0.0069 317 ILE B CD1 4824 N N . CYS B 237 ? 0.0929 0.1085 0.0724 -0.0068 0.0005 0.0073 318 CYS B N 4825 C CA . CYS B 237 ? 0.1079 0.1261 0.0862 -0.0071 0.0008 0.0082 318 CYS B CA 4826 C C . CYS B 237 ? 0.1239 0.1416 0.1029 -0.0070 0.0013 0.0096 318 CYS B C 4827 O O . CYS B 237 ? 0.1465 0.1658 0.1246 -0.0072 0.0016 0.0110 318 CYS B O 4828 C CB . CYS B 237 ? 0.1067 0.1269 0.0839 -0.0076 0.0014 0.0063 318 CYS B CB 4829 S SG . CYS B 237 ? 0.1655 0.1872 0.1417 -0.0079 0.0009 0.0047 318 CYS B SG 4830 N N . SER B 238 ? 0.1044 0.1197 0.0847 -0.0068 0.0016 0.0092 319 SER B N 4831 C CA . SER B 238 ? 0.1041 0.1190 0.0851 -0.0070 0.0022 0.0100 319 SER B CA 4832 C C . SER B 238 ? 0.1394 0.1543 0.1204 -0.0071 0.0021 0.0124 319 SER B C 4833 O O . SER B 238 ? 0.1086 0.1223 0.0898 -0.0067 0.0015 0.0134 319 SER B O 4834 C CB . SER B 238 ? 0.1540 0.1665 0.1367 -0.0067 0.0022 0.0093 319 SER B CB 4835 O OG . SER B 238 ? 0.1401 0.1525 0.1236 -0.0070 0.0028 0.0101 319 SER B OG 4836 N N . GLY B 239 ? 0.1627 0.1787 0.1433 -0.0075 0.0028 0.0133 320 GLY B N 4837 C CA . GLY B 239 ? 0.1406 0.1563 0.1213 -0.0076 0.0030 0.0155 320 GLY B CA 4838 C C . GLY B 239 ? 0.2169 0.2297 0.1993 -0.0076 0.0031 0.0159 320 GLY B C 4839 O O . GLY B 239 ? 0.1858 0.1976 0.1685 -0.0077 0.0034 0.0177 320 GLY B O 4840 N N . ILE B 240 ? 0.1366 0.1483 0.1201 -0.0075 0.0030 0.0143 321 ILE B N 4841 C CA . ILE B 240 ? 0.1492 0.1583 0.1343 -0.0075 0.0029 0.0144 321 ILE B CA 4842 C C . ILE B 240 ? 0.1357 0.1433 0.1210 -0.0069 0.0021 0.0146 321 ILE B C 4843 O O . ILE B 240 ? 0.1762 0.1830 0.1619 -0.0065 0.0016 0.0132 321 ILE B O 4844 C CB . ILE B 240 ? 0.1358 0.1447 0.1220 -0.0074 0.0031 0.0126 321 ILE B CB 4845 C CG1 . ILE B 240 ? 0.2009 0.2119 0.1868 -0.0079 0.0039 0.0122 321 ILE B CG1 4846 C CG2 . ILE B 240 ? 0.1341 0.1409 0.1219 -0.0075 0.0030 0.0127 321 ILE B CG2 4847 C CD1 . ILE B 240 ? 0.2117 0.2228 0.1979 -0.0086 0.0045 0.0137 321 ILE B CD1 4848 N N . PHE B 241 ? 0.1309 0.1379 0.1160 -0.0068 0.0020 0.0163 322 PHE B N 4849 C CA . PHE B 241 ? 0.1602 0.1660 0.1453 -0.0062 0.0012 0.0167 322 PHE B CA 4850 C C . PHE B 241 ? 0.1306 0.1339 0.1172 -0.0060 0.0010 0.0160 322 PHE B C 4851 O O . PHE B 241 ? 0.1284 0.1303 0.1161 -0.0064 0.0014 0.0162 322 PHE B O 4852 C CB . PHE B 241 ? 0.1147 0.1205 0.0993 -0.0059 0.0013 0.0190 322 PHE B CB 4853 C CG . PHE B 241 ? 0.1658 0.1743 0.1490 -0.0061 0.0016 0.0199 322 PHE B CG 4854 C CD1 . PHE B 241 ? 0.1808 0.1918 0.1626 -0.0060 0.0012 0.0192 322 PHE B CD1 4855 C CD2 . PHE B 241 ? 0.1913 0.1998 0.1743 -0.0065 0.0024 0.0215 322 PHE B CD2 4856 C CE1 . PHE B 241 ? 0.1819 0.1956 0.1622 -0.0062 0.0015 0.0201 322 PHE B CE1 4857 C CE2 . PHE B 241 ? 0.2201 0.2312 0.2017 -0.0066 0.0028 0.0225 322 PHE B CE2 4858 C CZ . PHE B 241 ? 0.1816 0.1953 0.1618 -0.0064 0.0022 0.0218 322 PHE B CZ 4859 N N . GLY B 242 ? 0.1310 0.1339 0.1177 -0.0055 0.0003 0.0151 323 GLY B N 4860 C CA . GLY B 242 ? 0.0980 0.0989 0.0859 -0.0053 0.0000 0.0142 323 GLY B CA 4861 C C . GLY B 242 ? 0.1147 0.1138 0.1033 -0.0049 -0.0004 0.0151 323 GLY B C 4862 O O . GLY B 242 ? 0.1306 0.1279 0.1203 -0.0049 -0.0005 0.0145 323 GLY B O 4863 N N . ASP B 243 ? 0.0823 0.0818 0.0702 -0.0046 -0.0005 0.0166 324 ASP B N 4864 C CA . ASP B 243 ? 0.0968 0.0946 0.0853 -0.0041 -0.0008 0.0175 324 ASP B CA 4865 C C . ASP B 243 ? 0.1150 0.1109 0.1043 -0.0043 -0.0001 0.0189 324 ASP B C 4866 O O . ASP B 243 ? 0.1234 0.1195 0.1127 -0.0049 0.0006 0.0192 324 ASP B O 4867 C CB . ASP B 243 ? 0.1132 0.1126 0.1008 -0.0034 -0.0013 0.0185 324 ASP B CB 4868 C CG . ASP B 243 ? 0.1224 0.1205 0.1106 -0.0028 -0.0019 0.0186 324 ASP B CG 4869 O OD1 . ASP B 243 ? 0.0783 0.0743 0.0677 -0.0028 -0.0019 0.0180 324 ASP B OD1 4870 O OD2 . ASP B 243 ? 0.1030 0.1026 0.0906 -0.0022 -0.0024 0.0193 324 ASP B OD2 4871 N N . ASN B 244 ? 0.1236 0.1177 0.1136 -0.0038 -0.0002 0.0196 325 ASN B N 4872 C CA . ASN B 244 ? 0.1225 0.1144 0.1133 -0.0039 0.0005 0.0209 325 ASN B CA 4873 C C . ASN B 244 ? 0.1175 0.1085 0.1083 -0.0029 0.0003 0.0223 325 ASN B C 4874 O O . ASN B 244 ? 0.1133 0.1038 0.1046 -0.0024 -0.0003 0.0217 325 ASN B O 4875 C CB . ASN B 244 ? 0.1167 0.1066 0.1089 -0.0045 0.0008 0.0196 325 ASN B CB 4876 C CG . ASN B 244 ? 0.1610 0.1485 0.1539 -0.0049 0.0017 0.0207 325 ASN B CG 4877 O OD1 . ASN B 244 ? 0.1764 0.1619 0.1700 -0.0044 0.0017 0.0212 325 ASN B OD1 4878 N ND2 . ASN B 244 ? 0.1399 0.1276 0.1328 -0.0057 0.0025 0.0211 325 ASN B ND2 4879 N N . PRO B 245 ? 0.1125 0.1035 0.1028 -0.0026 0.0008 0.0244 326 PRO B N 4880 C CA . PRO B 245 ? 0.1177 0.1091 0.1074 -0.0032 0.0017 0.0255 326 PRO B CA 4881 C C . PRO B 245 ? 0.1380 0.1327 0.1263 -0.0034 0.0013 0.0252 326 PRO B C 4882 O O . PRO B 245 ? 0.1030 0.0997 0.0907 -0.0031 0.0005 0.0243 326 PRO B O 4883 C CB . PRO B 245 ? 0.1585 0.1487 0.1481 -0.0025 0.0022 0.0280 326 PRO B CB 4884 C CG . PRO B 245 ? 0.1725 0.1637 0.1619 -0.0013 0.0013 0.0283 326 PRO B CG 4885 C CD . PRO B 245 ? 0.1435 0.1340 0.1338 -0.0015 0.0007 0.0261 326 PRO B CD 4886 N N . ARG B 246 ? 0.1167 0.1121 0.1046 -0.0041 0.0021 0.0260 327 ARG B N 4887 C CA . ARG B 246 ? 0.1078 0.1062 0.0944 -0.0044 0.0020 0.0257 327 ARG B CA 4888 C C . ARG B 246 ? 0.1397 0.1383 0.1258 -0.0049 0.0030 0.0273 327 ARG B C 4889 O O . ARG B 246 ? 0.1362 0.1323 0.1231 -0.0052 0.0039 0.0283 327 ARG B O 4890 C CB . ARG B 246 ? 0.1141 0.1133 0.1009 -0.0050 0.0017 0.0233 327 ARG B CB 4891 C CG . ARG B 246 ? 0.1227 0.1202 0.1107 -0.0059 0.0024 0.0226 327 ARG B CG 4892 C CD . ARG B 246 ? 0.0911 0.0898 0.0793 -0.0063 0.0022 0.0204 327 ARG B CD 4893 N NE . ARG B 246 ? 0.0780 0.0756 0.0673 -0.0072 0.0029 0.0197 327 ARG B NE 4894 C CZ . ARG B 246 ? 0.0810 0.0769 0.0716 -0.0073 0.0027 0.0187 327 ARG B CZ 4895 N NH1 . ARG B 246 ? 0.0704 0.0652 0.0613 -0.0066 0.0020 0.0182 327 ARG B NH1 4896 N NH2 . ARG B 246 ? 0.1031 0.0985 0.0946 -0.0082 0.0033 0.0181 327 ARG B NH2 4897 N N . PRO B 247 ? 0.1343 0.1358 0.1190 -0.0050 0.0031 0.0276 328 PRO B N 4898 C CA . PRO B 247 ? 0.1766 0.1786 0.1608 -0.0057 0.0041 0.0290 328 PRO B CA 4899 C C . PRO B 247 ? 0.1770 0.1789 0.1618 -0.0068 0.0046 0.0273 328 PRO B C 4900 O O . PRO B 247 ? 0.1302 0.1321 0.1156 -0.0070 0.0040 0.0252 328 PRO B O 4901 C CB . PRO B 247 ? 0.2017 0.2074 0.1841 -0.0053 0.0037 0.0296 328 PRO B CB 4902 C CG . PRO B 247 ? 0.1888 0.1957 0.1708 -0.0045 0.0026 0.0287 328 PRO B CG 4903 C CD . PRO B 247 ? 0.1438 0.1484 0.1273 -0.0047 0.0022 0.0268 328 PRO B CD 4904 N N . ASN B 248 ? 0.2032 0.2051 0.1879 -0.0076 0.0056 0.0284 329 ASN B N 4905 C CA . ASN B 248 ? 0.1879 0.1907 0.1731 -0.0086 0.0061 0.0269 329 ASN B CA 4906 C C . ASN B 248 ? 0.1770 0.1830 0.1611 -0.0085 0.0055 0.0254 329 ASN B C 4907 O O . ASN B 248 ? 0.1726 0.1806 0.1554 -0.0079 0.0050 0.0261 329 ASN B O 4908 C CB . ASN B 248 ? 0.2398 0.2425 0.2248 -0.0095 0.0073 0.0285 329 ASN B CB 4909 C CG . ASN B 248 ? 0.3025 0.3018 0.2887 -0.0099 0.0081 0.0296 329 ASN B CG 4910 O OD1 . ASN B 248 ? 0.2505 0.2478 0.2381 -0.0102 0.0080 0.0283 329 ASN B OD1 4911 N ND2 . ASN B 248 ? 0.3373 0.3358 0.3229 -0.0099 0.0090 0.0320 329 ASN B ND2 4912 N N . ASP B 249 ? 0.1596 0.1661 0.1443 -0.0090 0.0055 0.0235 330 ASP B N 4913 C CA . ASP B 249 ? 0.1727 0.1819 0.1567 -0.0089 0.0051 0.0219 330 ASP B CA 4914 C C . ASP B 249 ? 0.2685 0.2805 0.2508 -0.0091 0.0056 0.0228 330 ASP B C 4915 O O . ASP B 249 ? 0.1907 0.2030 0.1730 -0.0098 0.0065 0.0239 330 ASP B O 4916 C CB . ASP B 249 ? 0.2078 0.2171 0.1928 -0.0094 0.0053 0.0199 330 ASP B CB 4917 C CG . ASP B 249 ? 0.2095 0.2166 0.1958 -0.0090 0.0047 0.0186 330 ASP B CG 4918 O OD1 . ASP B 249 ? 0.1696 0.1757 0.1558 -0.0084 0.0040 0.0189 330 ASP B OD1 4919 O OD2 . ASP B 249 ? 0.1746 0.1814 0.1622 -0.0094 0.0050 0.0175 330 ASP B OD2 4920 N N . LYS B 250 ? 0.2131 0.2272 0.1941 -0.0086 0.0050 0.0224 331 LYS B N 4921 C CA . LYS B 250 ? 0.2527 0.2699 0.2321 -0.0088 0.0053 0.0230 331 LYS B CA 4922 C C . LYS B 250 ? 0.2572 0.2766 0.2356 -0.0085 0.0047 0.0211 331 LYS B C 4923 O O . LYS B 250 ? 0.3681 0.3868 0.3473 -0.0084 0.0044 0.0191 331 LYS B O 4924 C CB . LYS B 250 ? 0.2053 0.2229 0.1837 -0.0084 0.0053 0.0256 331 LYS B CB 4925 C CG . LYS B 250 ? 0.2577 0.2744 0.2360 -0.0074 0.0044 0.0261 331 LYS B CG 4926 C CD . LYS B 250 ? 0.4140 0.4312 0.3915 -0.0069 0.0045 0.0288 331 LYS B CD 4927 C CE . LYS B 250 ? 0.4421 0.4583 0.4197 -0.0059 0.0036 0.0293 331 LYS B CE 4928 N NZ . LYS B 250 ? 0.5081 0.5246 0.4851 -0.0051 0.0038 0.0322 331 LYS B NZ 4929 N N . THR B 251 ? 0.2365 0.2587 0.2131 -0.0084 0.0046 0.0218 332 THR B N 4930 C CA . THR B 251 ? 0.1815 0.2060 0.1572 -0.0083 0.0041 0.0199 332 THR B CA 4931 C C . THR B 251 ? 0.2163 0.2397 0.1922 -0.0077 0.0031 0.0196 332 THR B C 4932 O O . THR B 251 ? 0.1686 0.1918 0.1443 -0.0072 0.0027 0.0215 332 THR B O 4933 C CB . THR B 251 ? 0.2554 0.2836 0.2291 -0.0085 0.0043 0.0205 332 THR B CB 4934 O OG1 . THR B 251 ? 0.2687 0.2981 0.2422 -0.0091 0.0052 0.0205 332 THR B OG1 4935 C CG2 . THR B 251 ? 0.1836 0.2140 0.1563 -0.0085 0.0037 0.0184 332 THR B CG2 4936 N N . GLY B 252 ? 0.1886 0.2115 0.1650 -0.0076 0.0027 0.0173 333 GLY B N 4937 C CA . GLY B 252 ? 0.1647 0.1864 0.1414 -0.0071 0.0018 0.0169 333 GLY B CA 4938 C C . GLY B 252 ? 0.1963 0.2209 0.1716 -0.0071 0.0012 0.0162 333 GLY B C 4939 O O . GLY B 252 ? 0.1692 0.1968 0.1430 -0.0074 0.0015 0.0165 333 GLY B O 4940 N N . SER B 253 ? 0.1746 0.1984 0.1503 -0.0068 0.0005 0.0153 335 SER B N 4941 C CA . SER B 253 ? 0.1690 0.1955 0.1434 -0.0069 0.0000 0.0145 335 SER B CA 4942 C C . SER B 253 ? 0.1746 0.1998 0.1498 -0.0070 -0.0005 0.0123 335 SER B C 4943 O O . SER B 253 ? 0.1570 0.1791 0.1336 -0.0067 -0.0006 0.0122 335 SER B O 4944 C CB . SER B 253 ? 0.2068 0.2347 0.1808 -0.0064 -0.0006 0.0168 335 SER B CB 4945 O OG . SER B 253 ? 0.2148 0.2456 0.1876 -0.0065 -0.0013 0.0159 335 SER B OG 4946 N N . CYS B 254 ? 0.1686 0.1960 0.1426 -0.0075 -0.0006 0.0106 336 CYS B N 4947 C CA . CYS B 254 ? 0.2025 0.2288 0.1771 -0.0077 -0.0009 0.0085 336 CYS B CA 4948 C C . CYS B 254 ? 0.1978 0.2248 0.1725 -0.0074 -0.0018 0.0093 336 CYS B C 4949 O O . CYS B 254 ? 0.1838 0.2102 0.1588 -0.0076 -0.0021 0.0078 336 CYS B O 4950 C CB . CYS B 254 ? 0.2598 0.2880 0.2333 -0.0085 -0.0004 0.0061 336 CYS B CB 4951 S SG . CYS B 254 ? 0.4389 0.4657 0.4127 -0.0086 0.0007 0.0048 336 CYS B SG 4952 N N . GLY B 255 ? 0.1585 0.1867 0.1328 -0.0068 -0.0022 0.0117 339 GLY B N 4953 C CA . GLY B 255 ? 0.1678 0.1964 0.1424 -0.0063 -0.0030 0.0129 339 GLY B CA 4954 C C . GLY B 255 ? 0.1351 0.1608 0.1109 -0.0054 -0.0030 0.0151 339 GLY B C 4955 O O . GLY B 255 ? 0.1329 0.1566 0.1093 -0.0054 -0.0024 0.0155 339 GLY B O 4956 N N . PRO B 256 ? 0.1362 0.1619 0.1125 -0.0047 -0.0036 0.0164 340 PRO B N 4957 C CA . PRO B 256 ? 0.1439 0.1668 0.1214 -0.0039 -0.0035 0.0184 340 PRO B CA 4958 C C . PRO B 256 ? 0.1516 0.1748 0.1286 -0.0036 -0.0030 0.0206 340 PRO B C 4959 O O . PRO B 256 ? 0.1443 0.1707 0.1201 -0.0034 -0.0031 0.0220 340 PRO B O 4960 C CB . PRO B 256 ? 0.1414 0.1652 0.1191 -0.0031 -0.0043 0.0194 340 PRO B CB 4961 C CG . PRO B 256 ? 0.1606 0.1886 0.1370 -0.0036 -0.0048 0.0184 340 PRO B CG 4962 C CD . PRO B 256 ? 0.1501 0.1784 0.1259 -0.0047 -0.0044 0.0159 340 PRO B CD 4963 N N . VAL B 257 ? 0.1275 0.1476 0.1055 -0.0037 -0.0023 0.0210 341 VAL B N 4964 C CA . VAL B 257 ? 0.1493 0.1691 0.1270 -0.0035 -0.0016 0.0232 341 VAL B CA 4965 C C . VAL B 257 ? 0.1565 0.1750 0.1349 -0.0025 -0.0017 0.0256 341 VAL B C 4966 O O . VAL B 257 ? 0.1268 0.1420 0.1066 -0.0022 -0.0017 0.0256 341 VAL B O 4967 C CB . VAL B 257 ? 0.1583 0.1755 0.1370 -0.0041 -0.0008 0.0226 341 VAL B CB 4968 C CG1 . VAL B 257 ? 0.1642 0.1808 0.1428 -0.0040 0.0000 0.0249 341 VAL B CG1 4969 C CG2 . VAL B 257 ? 0.1156 0.1342 0.0937 -0.0049 -0.0006 0.0204 341 VAL B CG2 4970 N N . SER B 258 ? 0.1552 0.1762 0.1325 -0.0019 -0.0018 0.0277 342 SER B N 4971 C CA . SER B 258 ? 0.1290 0.1491 0.1067 -0.0007 -0.0019 0.0301 342 SER B CA 4972 C C . SER B 258 ? 0.1317 0.1480 0.1104 -0.0005 -0.0010 0.0317 342 SER B C 4973 O O . SER B 258 ? 0.1823 0.1962 0.1622 0.0003 -0.0010 0.0328 342 SER B O 4974 C CB . SER B 258 ? 0.2102 0.2344 0.1864 -0.0001 -0.0023 0.0320 342 SER B CB 4975 O OG . SER B 258 ? 0.2391 0.2647 0.2142 -0.0004 -0.0016 0.0331 342 SER B OG 4976 N N . SER B 259 ? 0.1703 0.1862 0.1488 -0.0013 -0.0002 0.0319 343 SER B N 4977 C CA . SER B 259 ? 0.1722 0.1847 0.1516 -0.0013 0.0008 0.0334 343 SER B CA 4978 C C . SER B 259 ? 0.2042 0.2128 0.1854 -0.0014 0.0008 0.0322 343 SER B C 4979 O O . SER B 259 ? 0.1590 0.1671 0.1408 -0.0021 0.0006 0.0299 343 SER B O 4980 C CB . SER B 259 ? 0.2531 0.2659 0.2319 -0.0023 0.0017 0.0333 343 SER B CB 4981 O OG . SER B 259 ? 0.3453 0.3548 0.3251 -0.0026 0.0027 0.0345 343 SER B OG 4982 N N . ASN B 260 ? 0.1276 0.1336 0.1097 -0.0006 0.0012 0.0339 344 ASN B N 4983 C CA . ASN B 260 ? 0.1472 0.1496 0.1309 -0.0007 0.0012 0.0328 344 ASN B CA 4984 C C . ASN B 260 ? 0.1747 0.1778 0.1588 -0.0006 0.0001 0.0306 344 ASN B C 4985 O O . ASN B 260 ? 0.1394 0.1403 0.1246 -0.0010 0.0001 0.0289 344 ASN B O 4986 C CB . ASN B 260 ? 0.1694 0.1695 0.1540 -0.0019 0.0020 0.0318 344 ASN B CB 4987 C CG . ASN B 260 ? 0.2478 0.2470 0.2321 -0.0021 0.0032 0.0339 344 ASN B CG 4988 O OD1 . ASN B 260 ? 0.2628 0.2637 0.2463 -0.0029 0.0036 0.0338 344 ASN B OD1 4989 N ND2 . ASN B 260 ? 0.2837 0.2801 0.2687 -0.0016 0.0039 0.0357 344 ASN B ND2 4990 N N . GLY B 261 ? 0.1747 0.1811 0.1578 -0.0001 -0.0007 0.0306 345 GLY B N 4991 C CA . GLY B 261 ? 0.1385 0.1460 0.1217 -0.0002 -0.0016 0.0285 345 GLY B CA 4992 C C . GLY B 261 ? 0.1477 0.1536 0.1321 0.0006 -0.0021 0.0284 345 GLY B C 4993 O O . GLY B 261 ? 0.1010 0.1066 0.0859 0.0003 -0.0027 0.0264 345 GLY B O 4994 N N . ALA B 262 ? 0.1551 0.1600 0.1398 0.0017 -0.0019 0.0306 346 ALA B N 4995 C CA . ALA B 262 ? 0.1601 0.1634 0.1459 0.0025 -0.0022 0.0307 346 ALA B CA 4996 C C . ALA B 262 ? 0.1318 0.1313 0.1191 0.0019 -0.0018 0.0293 346 ALA B C 4997 O O . ALA B 262 ? 0.1083 0.1060 0.0958 0.0011 -0.0011 0.0291 346 ALA B O 4998 C CB . ALA B 262 ? 0.1852 0.1881 0.1711 0.0039 -0.0019 0.0335 346 ALA B CB 4999 N N . ASN B 263 ? 0.1441 0.1426 0.1323 0.0023 -0.0023 0.0283 347 ASN B N 5000 C CA . ASN B 263 ? 0.1624 0.1577 0.1519 0.0018 -0.0021 0.0269 347 ASN B CA 5001 C C . ASN B 263 ? 0.1209 0.1166 0.1103 0.0006 -0.0022 0.0247 347 ASN B C 5002 O O . ASN B 263 ? 0.0952 0.0935 0.0836 0.0003 -0.0026 0.0240 347 ASN B O 5003 C CB . ASN B 263 ? 0.1612 0.1533 0.1515 0.0019 -0.0010 0.0282 347 ASN B CB 5004 C CG . ASN B 263 ? 0.4097 0.3987 0.4015 0.0017 -0.0008 0.0270 347 ASN B CG 5005 O OD1 . ASN B 263 ? 0.3616 0.3508 0.3538 0.0016 -0.0014 0.0254 347 ASN B OD1 5006 N ND2 . ASN B 263 ? 0.4436 0.4296 0.4361 0.0015 0.0002 0.0279 347 ASN B ND2 5007 N N . GLY B 264 ? 0.0863 0.0795 0.0768 0.0001 -0.0019 0.0235 348 GLY B N 5008 C CA . GLY B 264 ? 0.0612 0.0547 0.0516 -0.0009 -0.0020 0.0215 348 GLY B CA 5009 C C . GLY B 264 ? 0.0749 0.0661 0.0665 -0.0012 -0.0020 0.0200 348 GLY B C 5010 O O . GLY B 264 ? 0.0608 0.0499 0.0534 -0.0009 -0.0017 0.0205 348 GLY B O 5011 N N . VAL B 265 ? 0.0787 0.0704 0.0703 -0.0018 -0.0022 0.0183 349 VAL B N 5012 C CA . VAL B 265 ? 0.0888 0.0789 0.0814 -0.0021 -0.0022 0.0168 349 VAL B CA 5013 C C . VAL B 265 ? 0.0931 0.0845 0.0855 -0.0023 -0.0027 0.0152 349 VAL B C 5014 O O . VAL B 265 ? 0.0867 0.0799 0.0781 -0.0025 -0.0028 0.0148 349 VAL B O 5015 C CB . VAL B 265 ? 0.0786 0.0673 0.0720 -0.0028 -0.0015 0.0167 349 VAL B CB 5016 C CG1 . VAL B 265 ? 0.0764 0.0667 0.0692 -0.0035 -0.0013 0.0160 349 VAL B CG1 5017 C CG2 . VAL B 265 ? 0.0810 0.0681 0.0755 -0.0030 -0.0015 0.0154 349 VAL B CG2 5018 N N . LYS B 266 ? 0.0895 0.0800 0.0826 -0.0021 -0.0031 0.0141 350 LYS B N 5019 C CA . LYS B 266 ? 0.0736 0.0649 0.0664 -0.0023 -0.0034 0.0125 350 LYS B CA 5020 C C . LYS B 266 ? 0.0828 0.0743 0.0756 -0.0029 -0.0030 0.0118 350 LYS B C 5021 O O . LYS B 266 ? 0.0780 0.0684 0.0715 -0.0032 -0.0026 0.0119 350 LYS B O 5022 C CB . LYS B 266 ? 0.0806 0.0708 0.0742 -0.0020 -0.0038 0.0117 350 LYS B CB 5023 C CG . LYS B 266 ? 0.0944 0.0850 0.0878 -0.0022 -0.0039 0.0102 350 LYS B CG 5024 C CD . LYS B 266 ? 0.1193 0.1088 0.1134 -0.0019 -0.0042 0.0095 350 LYS B CD 5025 C CE . LYS B 266 ? 0.1197 0.1094 0.1136 -0.0020 -0.0043 0.0081 350 LYS B CE 5026 N NZ . LYS B 266 ? 0.0812 0.0723 0.0742 -0.0022 -0.0044 0.0077 350 LYS B NZ 5027 N N . GLY B 267 ? 0.0776 0.0705 0.0696 -0.0030 -0.0030 0.0110 351 GLY B N 5028 C CA . GLY B 267 ? 0.1058 0.0992 0.0979 -0.0034 -0.0026 0.0103 351 GLY B CA 5029 C C . GLY B 267 ? 0.0919 0.0861 0.0834 -0.0033 -0.0026 0.0089 351 GLY B C 5030 O O . GLY B 267 ? 0.1170 0.1112 0.1083 -0.0031 -0.0030 0.0085 351 GLY B O 5031 N N . PHE B 268 ? 0.0860 0.0808 0.0774 -0.0035 -0.0022 0.0083 352 PHE B N 5032 C CA . PHE B 268 ? 0.0870 0.0823 0.0779 -0.0034 -0.0021 0.0070 352 PHE B CA 5033 C C . PHE B 268 ? 0.0787 0.0754 0.0691 -0.0037 -0.0015 0.0068 352 PHE B C 5034 O O . PHE B 268 ? 0.0985 0.0957 0.0891 -0.0040 -0.0012 0.0076 352 PHE B O 5035 C CB . PHE B 268 ? 0.0892 0.0834 0.0811 -0.0031 -0.0021 0.0062 352 PHE B CB 5036 C CG . PHE B 268 ? 0.0867 0.0809 0.0793 -0.0032 -0.0017 0.0063 352 PHE B CG 5037 C CD1 . PHE B 268 ? 0.0934 0.0871 0.0869 -0.0034 -0.0017 0.0070 352 PHE B CD1 5038 C CD2 . PHE B 268 ? 0.0756 0.0707 0.0682 -0.0030 -0.0012 0.0055 352 PHE B CD2 5039 C CE1 . PHE B 268 ? 0.0745 0.0686 0.0687 -0.0036 -0.0013 0.0069 352 PHE B CE1 5040 C CE2 . PHE B 268 ? 0.1037 0.0994 0.0971 -0.0031 -0.0008 0.0055 352 PHE B CE2 5041 C CZ . PHE B 268 ? 0.0705 0.0658 0.0647 -0.0034 -0.0009 0.0062 352 PHE B CZ 5042 N N . SER B 269 ? 0.0683 0.0655 0.0582 -0.0036 -0.0012 0.0056 353 SER B N 5043 C CA . SER B 269 ? 0.0978 0.0962 0.0874 -0.0037 -0.0006 0.0051 353 SER B CA 5044 C C . SER B 269 ? 0.1095 0.1074 0.0989 -0.0034 -0.0003 0.0037 353 SER B C 5045 O O . SER B 269 ? 0.1111 0.1083 0.1003 -0.0033 -0.0005 0.0031 353 SER B O 5046 C CB . SER B 269 ? 0.1260 0.1261 0.1144 -0.0042 -0.0005 0.0056 353 SER B CB 5047 O OG . SER B 269 ? 0.1125 0.1129 0.1011 -0.0044 -0.0005 0.0070 353 SER B OG 5048 N N . PHE B 270 ? 0.0756 0.0740 0.0653 -0.0031 0.0003 0.0031 354 PHE B N 5049 C CA . PHE B 270 ? 0.0637 0.0615 0.0533 -0.0027 0.0008 0.0018 354 PHE B CA 5050 C C . PHE B 270 ? 0.1083 0.1075 0.0969 -0.0029 0.0015 0.0010 354 PHE B C 5051 O O . PHE B 270 ? 0.1162 0.1168 0.1048 -0.0030 0.0018 0.0013 354 PHE B O 5052 C CB . PHE B 270 ? 0.0753 0.0726 0.0660 -0.0020 0.0011 0.0017 354 PHE B CB 5053 C CG . PHE B 270 ? 0.1021 0.0979 0.0937 -0.0017 0.0006 0.0021 354 PHE B CG 5054 C CD1 . PHE B 270 ? 0.0755 0.0699 0.0670 -0.0014 0.0004 0.0016 354 PHE B CD1 5055 C CD2 . PHE B 270 ? 0.0823 0.0785 0.0748 -0.0017 0.0003 0.0029 354 PHE B CD2 5056 C CE1 . PHE B 270 ? 0.1106 0.1039 0.1029 -0.0011 0.0000 0.0019 354 PHE B CE1 5057 C CE2 . PHE B 270 ? 0.0640 0.0591 0.0573 -0.0015 -0.0002 0.0031 354 PHE B CE2 5058 C CZ . PHE B 270 ? 0.0687 0.0624 0.0618 -0.0012 -0.0004 0.0027 354 PHE B CZ 5059 N N . LYS B 271 ? 0.0714 0.0703 0.0592 -0.0031 0.0017 0.0000 355 LYS B N 5060 C CA . LYS B 271 ? 0.0695 0.0696 0.0562 -0.0034 0.0023 -0.0010 355 LYS B CA 5061 C C . LYS B 271 ? 0.1039 0.1034 0.0910 -0.0027 0.0033 -0.0021 355 LYS B C 5062 O O . LYS B 271 ? 0.1017 0.0993 0.0893 -0.0022 0.0035 -0.0027 355 LYS B O 5063 C CB . LYS B 271 ? 0.0954 0.0957 0.0811 -0.0041 0.0021 -0.0017 355 LYS B CB 5064 C CG . LYS B 271 ? 0.0883 0.0901 0.0728 -0.0045 0.0028 -0.0030 355 LYS B CG 5065 C CD . LYS B 271 ? 0.1483 0.1503 0.1319 -0.0053 0.0026 -0.0039 355 LYS B CD 5066 C CE . LYS B 271 ? 0.1876 0.1915 0.1698 -0.0059 0.0032 -0.0052 355 LYS B CE 5067 N NZ . LYS B 271 ? 0.1091 0.1120 0.0914 -0.0056 0.0044 -0.0067 355 LYS B NZ 5068 N N . TYR B 272 ? 0.0769 0.0778 0.0636 -0.0027 0.0039 -0.0024 356 TYR B N 5069 C CA . TYR B 272 ? 0.1049 0.1055 0.0919 -0.0020 0.0049 -0.0035 356 TYR B CA 5070 C C . TYR B 272 ? 0.1111 0.1132 0.0969 -0.0026 0.0056 -0.0045 356 TYR B C 5071 O O . TYR B 272 ? 0.1071 0.1111 0.0928 -0.0027 0.0059 -0.0041 356 TYR B O 5072 C CB . TYR B 272 ? 0.1344 0.1354 0.1226 -0.0013 0.0051 -0.0028 356 TYR B CB 5073 C CG . TYR B 272 ? 0.1250 0.1246 0.1144 -0.0006 0.0047 -0.0021 356 TYR B CG 5074 C CD1 . TYR B 272 ? 0.0840 0.0838 0.0739 -0.0010 0.0038 -0.0009 356 TYR B CD1 5075 C CD2 . TYR B 272 ? 0.1316 0.1298 0.1217 0.0004 0.0052 -0.0027 356 TYR B CD2 5076 C CE1 . TYR B 272 ? 0.0862 0.0849 0.0772 -0.0005 0.0033 -0.0004 356 TYR B CE1 5077 C CE2 . TYR B 272 ? 0.1504 0.1474 0.1415 0.0010 0.0047 -0.0020 356 TYR B CE2 5078 C CZ . TYR B 272 ? 0.1644 0.1618 0.1559 0.0005 0.0038 -0.0009 356 TYR B CZ 5079 O OH . TYR B 272 ? 0.1947 0.1913 0.1871 0.0010 0.0034 -0.0004 356 TYR B OH 5080 N N . GLY B 273 ? 0.1553 0.1568 0.1403 -0.0030 0.0060 -0.0059 357 GLY B N 5081 C CA . GLY B 273 ? 0.1646 0.1678 0.1482 -0.0036 0.0066 -0.0070 357 GLY B CA 5082 C C . GLY B 273 ? 0.1171 0.1227 0.0999 -0.0045 0.0058 -0.0059 357 GLY B C 5083 O O . GLY B 273 ? 0.1542 0.1599 0.1369 -0.0049 0.0049 -0.0051 357 GLY B O 5084 N N . ASN B 274 ? 0.0986 0.1064 0.0810 -0.0046 0.0062 -0.0057 358 ASN B N 5085 C CA . ASN B 274 ? 0.1066 0.1168 0.0882 -0.0053 0.0056 -0.0045 358 ASN B CA 5086 C C . ASN B 274 ? 0.0969 0.1069 0.0795 -0.0051 0.0051 -0.0025 358 ASN B C 5087 O O . ASN B 274 ? 0.0912 0.1027 0.0733 -0.0055 0.0046 -0.0012 358 ASN B O 5088 C CB . ASN B 274 ? 0.1126 0.1252 0.0931 -0.0057 0.0064 -0.0052 358 ASN B CB 5089 C CG . ASN B 274 ? 0.1797 0.1927 0.1590 -0.0063 0.0069 -0.0071 358 ASN B CG 5090 O OD1 . ASN B 274 ? 0.1558 0.1676 0.1354 -0.0059 0.0079 -0.0088 358 ASN B OD1 5091 N ND2 . ASN B 274 ? 0.1732 0.1880 0.1512 -0.0072 0.0064 -0.0071 358 ASN B ND2 5092 N N . GLY B 275 ? 0.1110 0.1194 0.0950 -0.0043 0.0052 -0.0024 359 GLY B N 5093 C CA . GLY B 275 ? 0.0981 0.1065 0.0832 -0.0041 0.0048 -0.0009 359 GLY B CA 5094 C C . GLY B 275 ? 0.1093 0.1158 0.0950 -0.0040 0.0038 0.0000 359 GLY B C 5095 O O . GLY B 275 ? 0.0719 0.0772 0.0574 -0.0040 0.0036 -0.0006 359 GLY B O 5096 N N . VAL B 276 ? 0.0968 0.1033 0.0833 -0.0041 0.0035 0.0013 360 VAL B N 5097 C CA . VAL B 276 ? 0.0782 0.0832 0.0654 -0.0041 0.0026 0.0022 360 VAL B CA 5098 C C . VAL B 276 ? 0.1020 0.1066 0.0905 -0.0039 0.0025 0.0031 360 VAL B C 5099 O O . VAL B 276 ? 0.0854 0.0913 0.0740 -0.0043 0.0028 0.0038 360 VAL B O 5100 C CB . VAL B 276 ? 0.0796 0.0851 0.0659 -0.0046 0.0021 0.0031 360 VAL B CB 5101 C CG1 . VAL B 276 ? 0.0913 0.0985 0.0771 -0.0051 0.0022 0.0043 360 VAL B CG1 5102 C CG2 . VAL B 276 ? 0.0997 0.1036 0.0866 -0.0045 0.0013 0.0039 360 VAL B CG2 5103 N N . TRP B 277 ? 0.0810 0.0840 0.0704 -0.0035 0.0021 0.0031 361 TRP B N 5104 C CA . TRP B 277 ? 0.0773 0.0798 0.0679 -0.0035 0.0019 0.0040 361 TRP B CA 5105 C C . TRP B 277 ? 0.1167 0.1185 0.1072 -0.0040 0.0012 0.0050 361 TRP B C 5106 O O . TRP B 277 ? 0.0946 0.0951 0.0849 -0.0038 0.0007 0.0049 361 TRP B O 5107 C CB . TRP B 277 ? 0.0903 0.0918 0.0820 -0.0028 0.0018 0.0034 361 TRP B CB 5108 C CG . TRP B 277 ? 0.0612 0.0637 0.0536 -0.0023 0.0024 0.0029 361 TRP B CG 5109 C CD1 . TRP B 277 ? 0.0743 0.0769 0.0667 -0.0015 0.0029 0.0019 361 TRP B CD1 5110 C CD2 . TRP B 277 ? 0.0703 0.0743 0.0637 -0.0026 0.0026 0.0033 361 TRP B CD2 5111 N NE1 . TRP B 277 ? 0.0880 0.0920 0.0813 -0.0011 0.0034 0.0018 361 TRP B NE1 5112 C CE2 . TRP B 277 ? 0.0771 0.0822 0.0710 -0.0018 0.0032 0.0026 361 TRP B CE2 5113 C CE3 . TRP B 277 ? 0.0626 0.0671 0.0565 -0.0034 0.0024 0.0042 361 TRP B CE3 5114 C CZ2 . TRP B 277 ? 0.0829 0.0898 0.0778 -0.0018 0.0035 0.0028 361 TRP B CZ2 5115 C CZ3 . TRP B 277 ? 0.0760 0.0821 0.0708 -0.0036 0.0028 0.0043 361 TRP B CZ3 5116 C CH2 . TRP B 277 ? 0.0911 0.0986 0.0864 -0.0028 0.0033 0.0036 361 TRP B CH2 5117 N N . ILE B 278 ? 0.0747 0.0771 0.0653 -0.0046 0.0013 0.0061 362 ILE B N 5118 C CA . ILE B 278 ? 0.1000 0.1015 0.0904 -0.0049 0.0009 0.0073 362 ILE B CA 5119 C C . ILE B 278 ? 0.0885 0.0888 0.0802 -0.0050 0.0008 0.0078 362 ILE B C 5120 O O . ILE B 278 ? 0.1159 0.1169 0.1083 -0.0054 0.0012 0.0079 362 ILE B O 5121 C CB . ILE B 278 ? 0.0962 0.0989 0.0857 -0.0054 0.0011 0.0084 362 ILE B CB 5122 C CG1 . ILE B 278 ? 0.1315 0.1356 0.1196 -0.0054 0.0012 0.0078 362 ILE B CG1 5123 C CG2 . ILE B 278 ? 0.1035 0.1052 0.0931 -0.0056 0.0008 0.0098 362 ILE B CG2 5124 C CD1 . ILE B 278 ? 0.2066 0.2125 0.1937 -0.0059 0.0016 0.0087 362 ILE B CD1 5125 N N . GLY B 279 ? 0.1122 0.1109 0.1042 -0.0048 0.0002 0.0080 363 GLY B N 5126 C CA . GLY B 279 ? 0.0899 0.0875 0.0831 -0.0051 0.0001 0.0085 363 GLY B CA 5127 C C . GLY B 279 ? 0.1011 0.0979 0.0939 -0.0054 0.0001 0.0099 363 GLY B C 5128 O O . GLY B 279 ? 0.1156 0.1123 0.1076 -0.0051 -0.0003 0.0102 363 GLY B O 5129 N N . ARG B 280 ? 0.0810 0.0774 0.0744 -0.0060 0.0005 0.0106 364 ARG B N 5130 C CA . ARG B 280 ? 0.0803 0.0758 0.0734 -0.0062 0.0006 0.0121 364 ARG B CA 5131 C C . ARG B 280 ? 0.0907 0.0850 0.0849 -0.0069 0.0011 0.0126 364 ARG B C 5132 O O . ARG B 280 ? 0.0753 0.0700 0.0703 -0.0074 0.0014 0.0118 364 ARG B O 5133 C CB . ARG B 280 ? 0.0881 0.0850 0.0800 -0.0063 0.0009 0.0130 364 ARG B CB 5134 C CG . ARG B 280 ? 0.0849 0.0830 0.0769 -0.0071 0.0017 0.0131 364 ARG B CG 5135 C CD . ARG B 280 ? 0.0691 0.0687 0.0599 -0.0072 0.0020 0.0142 364 ARG B CD 5136 N NE . ARG B 280 ? 0.1042 0.1048 0.0951 -0.0080 0.0028 0.0144 364 ARG B NE 5137 C CZ . ARG B 280 ? 0.1401 0.1421 0.1300 -0.0083 0.0033 0.0155 364 ARG B CZ 5138 N NH1 . ARG B 280 ? 0.0891 0.0916 0.0778 -0.0078 0.0030 0.0163 364 ARG B NH1 5139 N NH2 . ARG B 280 ? 0.1375 0.1405 0.1277 -0.0091 0.0041 0.0156 364 ARG B NH2 5140 N N . THR B 281 ? 0.1051 0.0978 0.0992 -0.0069 0.0012 0.0138 365 THR B N 5141 C CA . THR B 281 ? 0.1015 0.0927 0.0965 -0.0076 0.0019 0.0144 365 THR B CA 5142 C C . THR B 281 ? 0.1160 0.1083 0.1108 -0.0084 0.0027 0.0149 365 THR B C 5143 O O . THR B 281 ? 0.1216 0.1157 0.1155 -0.0083 0.0027 0.0152 365 THR B O 5144 C CB . THR B 281 ? 0.1138 0.1031 0.1087 -0.0073 0.0020 0.0158 365 THR B CB 5145 O OG1 . THR B 281 ? 0.1207 0.1108 0.1144 -0.0069 0.0021 0.0172 365 THR B OG1 5146 C CG2 . THR B 281 ? 0.1483 0.1366 0.1434 -0.0064 0.0012 0.0154 365 THR B CG2 5147 N N . LYS B 282 ? 0.1051 0.0965 0.1009 -0.0094 0.0034 0.0149 366 LYS B N 5148 C CA . LYS B 282 ? 0.1215 0.1138 0.1172 -0.0103 0.0043 0.0155 366 LYS B CA 5149 C C . LYS B 282 ? 0.1332 0.1242 0.1284 -0.0104 0.0049 0.0175 366 LYS B C 5150 O O . LYS B 282 ? 0.1239 0.1161 0.1183 -0.0107 0.0054 0.0184 366 LYS B O 5151 C CB . LYS B 282 ? 0.1316 0.1238 0.1287 -0.0115 0.0049 0.0145 366 LYS B CB 5152 C CG . LYS B 282 ? 0.1308 0.1253 0.1284 -0.0114 0.0044 0.0129 366 LYS B CG 5153 C CD . LYS B 282 ? 0.1412 0.1362 0.1402 -0.0126 0.0050 0.0120 366 LYS B CD 5154 C CE . LYS B 282 ? 0.1505 0.1482 0.1499 -0.0125 0.0047 0.0106 366 LYS B CE 5155 N NZ . LYS B 282 ? 0.1736 0.1735 0.1722 -0.0124 0.0049 0.0108 366 LYS B NZ 5156 N N . SER B 283 ? 0.1202 0.1087 0.1157 -0.0101 0.0049 0.0182 367 SER B N 5157 C CA . SER B 283 ? 0.1327 0.1197 0.1276 -0.0098 0.0055 0.0202 367 SER B CA 5158 C C . SER B 283 ? 0.1193 0.1076 0.1128 -0.0086 0.0048 0.0212 367 SER B C 5159 O O . SER B 283 ? 0.1008 0.0897 0.0941 -0.0079 0.0039 0.0203 367 SER B O 5160 C CB . SER B 283 ? 0.1288 0.1127 0.1246 -0.0098 0.0059 0.0206 367 SER B CB 5161 O OG . SER B 283 ? 0.1493 0.1317 0.1445 -0.0092 0.0064 0.0227 367 SER B OG 5162 N N . ILE B 284 ? 0.1336 0.1224 0.1262 -0.0086 0.0053 0.0230 368 ILE B N 5163 C CA . ILE B 284 ? 0.1341 0.1245 0.1253 -0.0075 0.0047 0.0240 368 ILE B CA 5164 C C . ILE B 284 ? 0.1451 0.1337 0.1363 -0.0065 0.0045 0.0254 368 ILE B C 5165 O O . ILE B 284 ? 0.1692 0.1591 0.1595 -0.0055 0.0038 0.0259 368 ILE B O 5166 C CB . ILE B 284 ? 0.1550 0.1472 0.1449 -0.0078 0.0053 0.0254 368 ILE B CB 5167 C CG1 . ILE B 284 ? 0.1486 0.1387 0.1387 -0.0079 0.0064 0.0276 368 ILE B CG1 5168 C CG2 . ILE B 284 ? 0.1293 0.1233 0.1193 -0.0088 0.0056 0.0241 368 ILE B CG2 5169 C CD1 . ILE B 284 ? 0.2099 0.2018 0.1986 -0.0080 0.0069 0.0294 368 ILE B CD1 5170 N N . SER B 285 ? 0.1232 0.1088 0.1155 -0.0067 0.0052 0.0258 369 SER B N 5171 C CA . SER B 285 ? 0.1433 0.1269 0.1357 -0.0057 0.0053 0.0274 369 SER B CA 5172 C C . SER B 285 ? 0.2126 0.1940 0.2062 -0.0054 0.0050 0.0262 369 SER B C 5173 O O . SER B 285 ? 0.2201 0.2003 0.2138 -0.0043 0.0049 0.0272 369 SER B O 5174 C CB . SER B 285 ? 0.1995 0.1811 0.1919 -0.0060 0.0067 0.0295 369 SER B CB 5175 O OG . SER B 285 ? 0.2202 0.1998 0.2138 -0.0073 0.0076 0.0286 369 SER B OG 5176 N N . SER B 286 ? 0.1660 0.1471 0.1605 -0.0063 0.0049 0.0242 370 SER B N 5177 C CA . SER B 286 ? 0.1650 0.1442 0.1607 -0.0062 0.0047 0.0230 370 SER B CA 5178 C C . SER B 286 ? 0.1276 0.1083 0.1237 -0.0066 0.0039 0.0208 370 SER B C 5179 O O . SER B 286 ? 0.1244 0.1071 0.1200 -0.0071 0.0037 0.0200 370 SER B O 5180 C CB . SER B 286 ? 0.2268 0.2030 0.2236 -0.0071 0.0060 0.0232 370 SER B CB 5181 O OG . SER B 286 ? 0.3872 0.3616 0.3851 -0.0070 0.0059 0.0221 370 SER B OG 5182 N N . ARG B 287 ? 0.1115 0.0911 0.1083 -0.0062 0.0034 0.0198 371 ARG B N 5183 C CA . ARG B 287 ? 0.1202 0.1011 0.1173 -0.0064 0.0027 0.0178 371 ARG B CA 5184 C C . ARG B 287 ? 0.1151 0.0955 0.1133 -0.0076 0.0032 0.0165 371 ARG B C 5185 O O . ARG B 287 ? 0.1190 0.0983 0.1181 -0.0079 0.0032 0.0154 371 ARG B O 5186 C CB . ARG B 287 ? 0.0892 0.0695 0.0866 -0.0055 0.0019 0.0172 371 ARG B CB 5187 C CG . ARG B 287 ? 0.1132 0.0948 0.1096 -0.0043 0.0012 0.0182 371 ARG B CG 5188 C CD . ARG B 287 ? 0.1302 0.1110 0.1270 -0.0034 0.0006 0.0179 371 ARG B CD 5189 N NE . ARG B 287 ? 0.1223 0.1047 0.1181 -0.0025 -0.0001 0.0187 371 ARG B NE 5190 C CZ . ARG B 287 ? 0.1664 0.1489 0.1623 -0.0016 -0.0007 0.0185 371 ARG B CZ 5191 N NH1 . ARG B 287 ? 0.0855 0.0664 0.0825 -0.0016 -0.0008 0.0176 371 ARG B NH1 5192 N NH2 . ARG B 287 ? 0.1110 0.0953 0.1061 -0.0009 -0.0014 0.0192 371 ARG B NH2 5193 N N . ASN B 288 ? 0.1292 0.1108 0.1272 -0.0085 0.0037 0.0166 372 ASN B N 5194 C CA . ASN B 288 ? 0.1161 0.0979 0.1151 -0.0098 0.0043 0.0154 372 ASN B CA 5195 C C . ASN B 288 ? 0.1338 0.1185 0.1325 -0.0101 0.0040 0.0145 372 ASN B C 5196 O O . ASN B 288 ? 0.1065 0.0926 0.1042 -0.0099 0.0040 0.0153 372 ASN B O 5197 C CB . ASN B 288 ? 0.1802 0.1603 0.1795 -0.0108 0.0056 0.0165 372 ASN B CB 5198 C CG . ASN B 288 ? 0.2202 0.1971 0.2202 -0.0107 0.0062 0.0169 372 ASN B CG 5199 O OD1 . ASN B 288 ? 0.2979 0.2737 0.2990 -0.0116 0.0066 0.0157 372 ASN B OD1 5200 N ND2 . ASN B 288 ? 0.2082 0.1837 0.2076 -0.0097 0.0062 0.0186 372 ASN B ND2 5201 N N . GLY B 289 ? 0.1053 0.0909 0.1047 -0.0107 0.0038 0.0129 373 GLY B N 5202 C CA . GLY B 289 ? 0.0873 0.0757 0.0867 -0.0109 0.0036 0.0120 373 GLY B CA 5203 C C . GLY B 289 ? 0.0776 0.0675 0.0762 -0.0097 0.0027 0.0117 373 GLY B C 5204 O O . GLY B 289 ? 0.0774 0.0664 0.0753 -0.0088 0.0022 0.0123 373 GLY B O 5205 N N . PHE B 290 ? 0.0872 0.0792 0.0858 -0.0097 0.0025 0.0107 374 PHE B N 5206 C CA . PHE B 290 ? 0.0685 0.0619 0.0664 -0.0087 0.0019 0.0103 374 PHE B CA 5207 C C . PHE B 290 ? 0.0723 0.0680 0.0702 -0.0088 0.0021 0.0096 374 PHE B C 5208 O O . PHE B 290 ? 0.0859 0.0827 0.0848 -0.0095 0.0024 0.0090 374 PHE B O 5209 C CB . PHE B 290 ? 0.0585 0.0511 0.0567 -0.0079 0.0011 0.0095 374 PHE B CB 5210 C CG . PHE B 290 ? 0.0566 0.0496 0.0539 -0.0069 0.0005 0.0094 374 PHE B CG 5211 C CD1 . PHE B 290 ? 0.0619 0.0537 0.0585 -0.0064 0.0002 0.0102 374 PHE B CD1 5212 C CD2 . PHE B 290 ? 0.0698 0.0643 0.0669 -0.0064 0.0003 0.0085 374 PHE B CD2 5213 C CE1 . PHE B 290 ? 0.0971 0.0894 0.0928 -0.0057 -0.0003 0.0100 374 PHE B CE1 5214 C CE2 . PHE B 290 ? 0.0681 0.0627 0.0644 -0.0056 -0.0002 0.0083 374 PHE B CE2 5215 C CZ . PHE B 290 ? 0.0752 0.0687 0.0707 -0.0053 -0.0005 0.0090 374 PHE B CZ 5216 N N . GLU B 291 ? 0.0753 0.0721 0.0722 -0.0082 0.0019 0.0097 375 GLU B N 5217 C CA . GLU B 291 ? 0.0829 0.0820 0.0797 -0.0082 0.0022 0.0091 375 GLU B CA 5218 C C . GLU B 291 ? 0.0925 0.0923 0.0885 -0.0072 0.0017 0.0086 375 GLU B C 5219 O O . GLU B 291 ? 0.0968 0.0955 0.0919 -0.0067 0.0014 0.0090 375 GLU B O 5220 C CB . GLU B 291 ? 0.0828 0.0829 0.0793 -0.0090 0.0029 0.0100 375 GLU B CB 5221 C CG . GLU B 291 ? 0.1263 0.1257 0.1215 -0.0088 0.0029 0.0112 375 GLU B CG 5222 C CD . GLU B 291 ? 0.1685 0.1686 0.1634 -0.0096 0.0037 0.0122 375 GLU B CD 5223 O OE1 . GLU B 291 ? 0.1845 0.1850 0.1803 -0.0106 0.0043 0.0121 375 GLU B OE1 5224 O OE2 . GLU B 291 ? 0.1723 0.1728 0.1660 -0.0094 0.0038 0.0132 375 GLU B OE2 5225 N N . MET B 292 ? 0.0786 0.0801 0.0748 -0.0068 0.0019 0.0077 376 MET B N 5226 C CA . MET B 292 ? 0.1039 0.1059 0.0992 -0.0059 0.0017 0.0072 376 MET B CA 5227 C C . MET B 292 ? 0.1134 0.1173 0.1082 -0.0061 0.0024 0.0072 376 MET B C 5228 O O . MET B 292 ? 0.0961 0.1015 0.0915 -0.0066 0.0028 0.0070 376 MET B O 5229 C CB . MET B 292 ? 0.0889 0.0911 0.0849 -0.0051 0.0015 0.0061 376 MET B CB 5230 C CG . MET B 292 ? 0.1090 0.1095 0.1054 -0.0048 0.0009 0.0060 376 MET B CG 5231 S SD . MET B 292 ? 0.1402 0.1390 0.1354 -0.0044 0.0004 0.0063 376 MET B SD 5232 C CE . MET B 292 ? 0.1025 0.1020 0.0970 -0.0036 0.0006 0.0054 376 MET B CE 5233 N N . ILE B 293 ? 0.0828 0.0868 0.0763 -0.0059 0.0023 0.0073 377 ILE B N 5234 C CA . ILE B 293 ? 0.0990 0.1049 0.0918 -0.0061 0.0029 0.0073 377 ILE B CA 5235 C C . ILE B 293 ? 0.0954 0.1018 0.0873 -0.0054 0.0030 0.0063 377 ILE B C 5236 O O . ILE B 293 ? 0.0879 0.0932 0.0791 -0.0051 0.0026 0.0061 377 ILE B O 5237 C CB . ILE B 293 ? 0.1024 0.1082 0.0942 -0.0068 0.0031 0.0086 377 ILE B CB 5238 C CG1 . ILE B 293 ? 0.1502 0.1554 0.1428 -0.0076 0.0033 0.0096 377 ILE B CG1 5239 C CG2 . ILE B 293 ? 0.0856 0.0935 0.0763 -0.0070 0.0036 0.0085 377 ILE B CG2 5240 C CD1 . ILE B 293 ? 0.1903 0.1952 0.1820 -0.0081 0.0035 0.0111 377 ILE B CD1 5241 N N . TRP B 294 ? 0.0800 0.0881 0.0722 -0.0052 0.0036 0.0056 378 TRP B N 5242 C CA . TRP B 294 ? 0.1030 0.1115 0.0943 -0.0045 0.0039 0.0045 378 TRP B CA 5243 C C . TRP B 294 ? 0.0982 0.1083 0.0883 -0.0050 0.0043 0.0046 378 TRP B C 5244 O O . TRP B 294 ? 0.1048 0.1166 0.0951 -0.0054 0.0049 0.0049 378 TRP B O 5245 C CB . TRP B 294 ? 0.1000 0.1093 0.0923 -0.0037 0.0043 0.0035 378 TRP B CB 5246 C CG . TRP B 294 ? 0.1092 0.1191 0.1008 -0.0031 0.0049 0.0025 378 TRP B CG 5247 C CD1 . TRP B 294 ? 0.1569 0.1688 0.1485 -0.0029 0.0057 0.0020 378 TRP B CD1 5248 C CD2 . TRP B 294 ? 0.1274 0.1359 0.1181 -0.0027 0.0048 0.0016 378 TRP B CD2 5249 N NE1 . TRP B 294 ? 0.1441 0.1558 0.1349 -0.0023 0.0062 0.0008 378 TRP B NE1 5250 C CE2 . TRP B 294 ? 0.1268 0.1364 0.1170 -0.0022 0.0057 0.0006 378 TRP B CE2 5251 C CE3 . TRP B 294 ? 0.1107 0.1173 0.1010 -0.0026 0.0042 0.0016 378 TRP B CE3 5252 C CZ2 . TRP B 294 ? 0.1466 0.1551 0.1359 -0.0019 0.0059 -0.0005 378 TRP B CZ2 5253 C CZ3 . TRP B 294 ? 0.1337 0.1394 0.1232 -0.0023 0.0044 0.0005 378 TRP B CZ3 5254 C CH2 . TRP B 294 ? 0.1565 0.1632 0.1455 -0.0020 0.0053 -0.0006 378 TRP B CH2 5255 N N . ASP B 295 ? 0.0548 0.0645 0.0437 -0.0050 0.0041 0.0044 379 ASP B N 5256 C CA . ASP B 295 ? 0.0785 0.0898 0.0660 -0.0054 0.0045 0.0045 379 ASP B CA 5257 C C . ASP B 295 ? 0.0774 0.0890 0.0641 -0.0050 0.0048 0.0030 379 ASP B C 5258 O O . ASP B 295 ? 0.0479 0.0585 0.0339 -0.0049 0.0044 0.0025 379 ASP B O 5259 C CB . ASP B 295 ? 0.0711 0.0823 0.0577 -0.0060 0.0040 0.0058 379 ASP B CB 5260 C CG . ASP B 295 ? 0.0906 0.1038 0.0757 -0.0064 0.0043 0.0060 379 ASP B CG 5261 O OD1 . ASP B 295 ? 0.0864 0.1011 0.0712 -0.0064 0.0050 0.0051 379 ASP B OD1 5262 O OD2 . ASP B 295 ? 0.1363 0.1499 0.1206 -0.0068 0.0040 0.0072 379 ASP B OD2 5263 N N . PRO B 296 ? 0.0848 0.0978 0.0716 -0.0047 0.0056 0.0021 380 PRO B N 5264 C CA . PRO B 296 ? 0.1065 0.1194 0.0927 -0.0042 0.0062 0.0004 380 PRO B CA 5265 C C . PRO B 296 ? 0.0858 0.0992 0.0704 -0.0046 0.0062 -0.0002 380 PRO B C 5266 O O . PRO B 296 ? 0.1432 0.1558 0.1274 -0.0043 0.0065 -0.0017 380 PRO B O 5267 C CB . PRO B 296 ? 0.1256 0.1405 0.1123 -0.0039 0.0071 0.0000 380 PRO B CB 5268 C CG . PRO B 296 ? 0.1223 0.1387 0.1091 -0.0047 0.0070 0.0014 380 PRO B CG 5269 C CD . PRO B 296 ? 0.1161 0.1308 0.1036 -0.0049 0.0062 0.0026 380 PRO B CD 5270 N N . ASN B 297 ? 0.0906 0.1053 0.0742 -0.0054 0.0058 0.0008 381 ASN B N 5271 C CA . ASN B 297 ? 0.1059 0.1215 0.0879 -0.0059 0.0057 0.0003 381 ASN B CA 5272 C C . ASN B 297 ? 0.1311 0.1466 0.1128 -0.0063 0.0047 0.0018 381 ASN B C 5273 O O . ASN B 297 ? 0.1280 0.1450 0.1082 -0.0068 0.0045 0.0019 381 ASN B O 5274 C CB . ASN B 297 ? 0.1050 0.1233 0.0859 -0.0063 0.0064 -0.0001 381 ASN B CB 5275 C CG . ASN B 297 ? 0.2219 0.2419 0.2024 -0.0069 0.0063 0.0017 381 ASN B CG 5276 O OD1 . ASN B 297 ? 0.1135 0.1325 0.0948 -0.0069 0.0058 0.0032 381 ASN B OD1 5277 N ND2 . ASN B 297 ? 0.2563 0.2789 0.2355 -0.0074 0.0067 0.0017 381 ASN B ND2 5278 N N . GLY B 298 ? 0.0907 0.1043 0.0734 -0.0061 0.0042 0.0028 382 GLY B N 5279 C CA . GLY B 298 ? 0.0847 0.0980 0.0673 -0.0063 0.0034 0.0044 382 GLY B CA 5280 C C . GLY B 298 ? 0.0848 0.0974 0.0668 -0.0063 0.0027 0.0040 382 GLY B C 5281 O O . GLY B 298 ? 0.0963 0.1092 0.0780 -0.0064 0.0021 0.0053 382 GLY B O 5282 N N . TRP B 299 ? 0.1115 0.1233 0.0935 -0.0061 0.0029 0.0023 383 TRP B N 5283 C CA . TRP B 299 ? 0.1176 0.1289 0.0991 -0.0062 0.0023 0.0017 383 TRP B CA 5284 C C . TRP B 299 ? 0.1455 0.1595 0.1254 -0.0069 0.0023 0.0016 383 TRP B C 5285 O O . TRP B 299 ? 0.1074 0.1221 0.0868 -0.0071 0.0016 0.0021 383 TRP B O 5286 C CB . TRP B 299 ? 0.1349 0.1444 0.1168 -0.0059 0.0026 -0.0001 383 TRP B CB 5287 C CG . TRP B 299 ? 0.1345 0.1432 0.1163 -0.0061 0.0020 -0.0005 383 TRP B CG 5288 C CD1 . TRP B 299 ? 0.1247 0.1345 0.1054 -0.0067 0.0020 -0.0017 383 TRP B CD1 5289 C CD2 . TRP B 299 ? 0.1239 0.1308 0.1067 -0.0058 0.0013 0.0003 383 TRP B CD2 5290 N NE1 . TRP B 299 ? 0.1620 0.1707 0.1430 -0.0067 0.0014 -0.0018 383 TRP B NE1 5291 C CE2 . TRP B 299 ? 0.1203 0.1272 0.1026 -0.0061 0.0009 -0.0005 383 TRP B CE2 5292 C CE3 . TRP B 299 ? 0.1016 0.1070 0.0856 -0.0053 0.0010 0.0015 383 TRP B CE3 5293 C CZ2 . TRP B 299 ? 0.1245 0.1299 0.1075 -0.0059 0.0003 0.0000 383 TRP B CZ2 5294 C CZ3 . TRP B 299 ? 0.1433 0.1471 0.1280 -0.0051 0.0003 0.0018 383 TRP B CZ3 5295 C CH2 . TRP B 299 ? 0.1509 0.1548 0.1351 -0.0054 0.0000 0.0011 383 TRP B CH2 5296 N N . THR B 300 ? 0.1159 0.1316 0.0950 -0.0071 0.0030 0.0007 384 THR B N 5297 C CA . THR B 300 ? 0.1457 0.1642 0.1231 -0.0078 0.0030 0.0003 384 THR B CA 5298 C C . THR B 300 ? 0.1474 0.1685 0.1241 -0.0080 0.0033 0.0015 384 THR B C 5299 O O . THR B 300 ? 0.1658 0.1896 0.1410 -0.0085 0.0032 0.0017 384 THR B O 5300 C CB . THR B 300 ? 0.1571 0.1760 0.1339 -0.0081 0.0038 -0.0022 384 THR B CB 5301 O OG1 . THR B 300 ? 0.1618 0.1798 0.1392 -0.0077 0.0047 -0.0029 384 THR B OG1 5302 C CG2 . THR B 300 ? 0.1783 0.1950 0.1556 -0.0080 0.0035 -0.0034 384 THR B CG2 5303 N N . GLY B 301 ? 0.1266 0.1469 0.1041 -0.0077 0.0037 0.0024 385 GLY B N 5304 C CA . GLY B 301 ? 0.1668 0.1892 0.1437 -0.0080 0.0041 0.0036 385 GLY B CA 5305 C C . GLY B 301 ? 0.1475 0.1698 0.1247 -0.0080 0.0036 0.0061 385 GLY B C 5306 O O . GLY B 301 ? 0.1407 0.1606 0.1192 -0.0076 0.0032 0.0069 385 GLY B O 5307 N N . THR B 302 ? 0.1162 0.1409 0.0922 -0.0083 0.0037 0.0075 386 THR B N 5308 C CA . THR B 302 ? 0.1266 0.1511 0.1027 -0.0082 0.0033 0.0099 386 THR B CA 5309 C C . THR B 302 ? 0.1405 0.1645 0.1173 -0.0084 0.0039 0.0114 386 THR B C 5310 O O . THR B 302 ? 0.1502 0.1736 0.1271 -0.0083 0.0037 0.0135 386 THR B O 5311 C CB . THR B 302 ? 0.1661 0.1935 0.1405 -0.0084 0.0029 0.0110 386 THR B CB 5312 O OG1 . THR B 302 ? 0.1325 0.1627 0.1055 -0.0089 0.0036 0.0106 386 THR B OG1 5313 C CG2 . THR B 302 ? 0.1464 0.1742 0.1202 -0.0084 0.0022 0.0097 386 THR B CG2 5314 N N . ASP B 303 ? 0.1483 0.1726 0.1255 -0.0085 0.0047 0.0104 387 ASP B N 5315 C CA . ASP B 303 ? 0.1990 0.2231 0.1769 -0.0088 0.0053 0.0116 387 ASP B CA 5316 C C . ASP B 303 ? 0.1582 0.1793 0.1378 -0.0086 0.0051 0.0122 387 ASP B C 5317 O O . ASP B 303 ? 0.1491 0.1683 0.1294 -0.0082 0.0044 0.0115 387 ASP B O 5318 C CB . ASP B 303 ? 0.2072 0.2328 0.1851 -0.0091 0.0062 0.0103 387 ASP B CB 5319 C CG . ASP B 303 ? 0.2305 0.2545 0.2098 -0.0086 0.0062 0.0084 387 ASP B CG 5320 O OD1 . ASP B 303 ? 0.2217 0.2439 0.2025 -0.0085 0.0062 0.0087 387 ASP B OD1 5321 O OD2 . ASP B 303 ? 0.2370 0.2615 0.2158 -0.0084 0.0063 0.0065 387 ASP B OD2 5322 N N . ASN B 304 ? 0.2138 0.2346 0.1942 -0.0090 0.0056 0.0135 388 ASN B N 5323 C CA . ASN B 304 ? 0.2611 0.2791 0.2431 -0.0090 0.0055 0.0140 388 ASN B CA 5324 C C . ASN B 304 ? 0.2503 0.2683 0.2337 -0.0093 0.0060 0.0130 388 ASN B C 5325 O O . ASN B 304 ? 0.2527 0.2692 0.2373 -0.0096 0.0062 0.0137 388 ASN B O 5326 C CB . ASN B 304 ? 0.2498 0.2670 0.2318 -0.0093 0.0056 0.0164 388 ASN B CB 5327 C CG . ASN B 304 ? 0.3624 0.3812 0.3439 -0.0100 0.0065 0.0175 388 ASN B CG 5328 O OD1 . ASN B 304 ? 0.4552 0.4763 0.4362 -0.0103 0.0070 0.0166 388 ASN B OD1 5329 N ND2 . ASN B 304 ? 0.3542 0.3718 0.3361 -0.0104 0.0069 0.0194 388 ASN B ND2 5330 N N . ASN B 305 ? 0.1612 0.1807 0.1443 -0.0091 0.0064 0.0114 389 ASN B N 5331 C CA . ASN B 305 ? 0.1623 0.1821 0.1468 -0.0091 0.0069 0.0104 389 ASN B CA 5332 C C . ASN B 305 ? 0.1741 0.1920 0.1596 -0.0084 0.0063 0.0091 389 ASN B C 5333 O O . ASN B 305 ? 0.1654 0.1827 0.1503 -0.0079 0.0058 0.0083 389 ASN B O 5334 C CB . ASN B 305 ? 0.2273 0.2497 0.2110 -0.0091 0.0076 0.0093 389 ASN B CB 5335 C CG . ASN B 305 ? 0.3228 0.3473 0.3053 -0.0098 0.0082 0.0106 389 ASN B CG 5336 O OD1 . ASN B 305 ? 0.4654 0.4922 0.4469 -0.0099 0.0087 0.0099 389 ASN B OD1 5337 N ND2 . ASN B 305 ? 0.3061 0.3298 0.2888 -0.0104 0.0081 0.0126 389 ASN B ND2 5338 N N . PHE B 306 ? 0.1416 0.1589 0.1288 -0.0084 0.0065 0.0088 390 PHE B N 5339 C CA . PHE B 306 ? 0.1362 0.1520 0.1244 -0.0076 0.0060 0.0077 390 PHE B CA 5340 C C . PHE B 306 ? 0.1851 0.2020 0.1746 -0.0075 0.0066 0.0069 390 PHE B C 5341 O O . PHE B 306 ? 0.1587 0.1772 0.1485 -0.0081 0.0072 0.0073 390 PHE B O 5342 C CB . PHE B 306 ? 0.1724 0.1858 0.1613 -0.0077 0.0053 0.0084 390 PHE B CB 5343 C CG . PHE B 306 ? 0.1810 0.1941 0.1708 -0.0085 0.0056 0.0096 390 PHE B CG 5344 C CD1 . PHE B 306 ? 0.1527 0.1658 0.1441 -0.0086 0.0057 0.0090 390 PHE B CD1 5345 C CD2 . PHE B 306 ? 0.1960 0.2087 0.1852 -0.0092 0.0057 0.0112 390 PHE B CD2 5346 C CE1 . PHE B 306 ? 0.2226 0.2354 0.2149 -0.0095 0.0060 0.0099 390 PHE B CE1 5347 C CE2 . PHE B 306 ? 0.2009 0.2130 0.1910 -0.0100 0.0061 0.0121 390 PHE B CE2 5348 C CZ . PHE B 306 ? 0.2395 0.2516 0.2312 -0.0103 0.0063 0.0114 390 PHE B CZ 5349 N N . SER B 307 ? 0.1359 0.1521 0.1262 -0.0066 0.0063 0.0057 391 SER B N 5350 C CA . SER B 307 ? 0.1179 0.1356 0.1094 -0.0062 0.0068 0.0049 391 SER B CA 5351 C C . SER B 307 ? 0.1789 0.1959 0.1720 -0.0062 0.0065 0.0050 391 SER B C 5352 O O . SER B 307 ? 0.1833 0.2021 0.1775 -0.0064 0.0069 0.0049 391 SER B O 5353 C CB . SER B 307 ? 0.1597 0.1773 0.1509 -0.0050 0.0070 0.0035 391 SER B CB 5354 O OG . SER B 307 ? 0.2504 0.2690 0.2402 -0.0051 0.0075 0.0030 391 SER B OG 5355 N N . ILE B 308 ? 0.1351 0.1499 0.1284 -0.0060 0.0058 0.0052 392 ILE B N 5356 C CA . ILE B 308 ? 0.1252 0.1395 0.1200 -0.0060 0.0054 0.0053 392 ILE B CA 5357 C C . ILE B 308 ? 0.1339 0.1461 0.1286 -0.0067 0.0049 0.0062 392 ILE B C 5358 O O . ILE B 308 ? 0.1379 0.1484 0.1317 -0.0065 0.0044 0.0065 392 ILE B O 5359 C CB . ILE B 308 ? 0.1698 0.1834 0.1651 -0.0048 0.0051 0.0043 392 ILE B CB 5360 C CG1 . ILE B 308 ? 0.1864 0.2017 0.1817 -0.0039 0.0058 0.0034 392 ILE B CG1 5361 C CG2 . ILE B 308 ? 0.1910 0.2046 0.1878 -0.0048 0.0048 0.0043 392 ILE B CG2 5362 C CD1 . ILE B 308 ? 0.1903 0.2048 0.1861 -0.0025 0.0056 0.0026 392 ILE B CD1 5363 N N . LYS B 309 ? 0.1008 0.1132 0.0967 -0.0075 0.0049 0.0066 394 LYS B N 5364 C CA . LYS B 309 ? 0.1152 0.1254 0.1113 -0.0080 0.0045 0.0072 394 LYS B CA 5365 C C . LYS B 309 ? 0.1548 0.1651 0.1524 -0.0081 0.0043 0.0067 394 LYS B C 5366 O O . LYS B 309 ? 0.1639 0.1763 0.1626 -0.0085 0.0047 0.0063 394 LYS B O 5367 C CB . LYS B 309 ? 0.1466 0.1566 0.1425 -0.0092 0.0050 0.0084 394 LYS B CB 5368 C CG . LYS B 309 ? 0.1400 0.1475 0.1362 -0.0098 0.0047 0.0092 394 LYS B CG 5369 C CD . LYS B 309 ? 0.2392 0.2462 0.2350 -0.0108 0.0053 0.0105 394 LYS B CD 5370 C CE . LYS B 309 ? 0.2328 0.2414 0.2296 -0.0120 0.0061 0.0104 394 LYS B CE 5371 N NZ . LYS B 309 ? 0.3195 0.3278 0.3179 -0.0125 0.0060 0.0097 394 LYS B NZ 5372 N N . GLN B 310 ? 0.1064 0.1148 0.1042 -0.0077 0.0036 0.0066 395 GLN B N 5373 C CA . GLN B 310 ? 0.0923 0.1008 0.0914 -0.0078 0.0033 0.0061 395 GLN B CA 5374 C C . GLN B 310 ? 0.1101 0.1163 0.1094 -0.0085 0.0031 0.0066 395 GLN B C 5375 O O . GLN B 310 ? 0.0793 0.0834 0.0778 -0.0081 0.0026 0.0070 395 GLN B O 5376 C CB . GLN B 310 ? 0.1114 0.1200 0.1106 -0.0065 0.0029 0.0053 395 GLN B CB 5377 C CG . GLN B 310 ? 0.0937 0.1029 0.0943 -0.0065 0.0026 0.0048 395 GLN B CG 5378 C CD . GLN B 310 ? 0.1301 0.1393 0.1307 -0.0051 0.0022 0.0042 395 GLN B CD 5379 O OE1 . GLN B 310 ? 0.1228 0.1319 0.1228 -0.0041 0.0022 0.0040 395 GLN B OE1 5380 N NE2 . GLN B 310 ? 0.1065 0.1159 0.1080 -0.0050 0.0018 0.0039 395 GLN B NE2 5381 N N . ASP B 311 ? 0.1140 0.1206 0.1143 -0.0096 0.0034 0.0066 396 ASP B N 5382 C CA . ASP B 311 ? 0.1103 0.1148 0.1110 -0.0104 0.0033 0.0069 396 ASP B CA 5383 C C . ASP B 311 ? 0.1131 0.1166 0.1142 -0.0097 0.0026 0.0063 396 ASP B C 5384 O O . ASP B 311 ? 0.0888 0.0940 0.0906 -0.0093 0.0024 0.0054 396 ASP B O 5385 C CB . ASP B 311 ? 0.1228 0.1280 0.1245 -0.0119 0.0040 0.0069 396 ASP B CB 5386 C CG . ASP B 311 ? 0.2222 0.2279 0.2234 -0.0127 0.0048 0.0077 396 ASP B CG 5387 O OD1 . ASP B 311 ? 0.2193 0.2243 0.2192 -0.0121 0.0048 0.0085 396 ASP B OD1 5388 O OD2 . ASP B 311 ? 0.3153 0.3221 0.3173 -0.0140 0.0055 0.0076 396 ASP B OD2 5389 N N . ILE B 312 ? 0.0920 0.0930 0.0928 -0.0096 0.0023 0.0067 397 ILE B N 5390 C CA . ILE B 312 ? 0.0923 0.0922 0.0933 -0.0091 0.0017 0.0062 397 ILE B CA 5391 C C . ILE B 312 ? 0.0924 0.0906 0.0941 -0.0100 0.0018 0.0062 397 ILE B C 5392 O O . ILE B 312 ? 0.0761 0.0747 0.0787 -0.0102 0.0016 0.0054 397 ILE B O 5393 C CB . ILE B 312 ? 0.0973 0.0958 0.0973 -0.0079 0.0011 0.0065 397 ILE B CB 5394 C CG1 . ILE B 312 ? 0.1022 0.1022 0.1015 -0.0070 0.0011 0.0063 397 ILE B CG1 5395 C CG2 . ILE B 312 ? 0.0832 0.0807 0.0836 -0.0074 0.0005 0.0060 397 ILE B CG2 5396 C CD1 . ILE B 312 ? 0.0966 0.0986 0.0967 -0.0065 0.0010 0.0054 397 ILE B CD1 5397 N N . VAL B 313 ? 0.0962 0.0925 0.0975 -0.0105 0.0023 0.0072 398 VAL B N 5398 C CA . VAL B 313 ? 0.0845 0.0788 0.0864 -0.0114 0.0027 0.0074 398 VAL B CA 5399 C C . VAL B 313 ? 0.0851 0.0788 0.0869 -0.0125 0.0036 0.0083 398 VAL B C 5400 O O . VAL B 313 ? 0.0749 0.0686 0.0757 -0.0121 0.0037 0.0094 398 VAL B O 5401 C CB . VAL B 313 ? 0.0787 0.0705 0.0801 -0.0106 0.0022 0.0079 398 VAL B CB 5402 C CG1 . VAL B 313 ? 0.0819 0.0713 0.0839 -0.0115 0.0028 0.0081 398 VAL B CG1 5403 C CG2 . VAL B 313 ? 0.0940 0.0863 0.0956 -0.0097 0.0014 0.0069 398 VAL B CG2 5404 N N . GLY B 314 ? 0.1004 0.0937 0.1032 -0.0138 0.0043 0.0079 399 GLY B N 5405 C CA . GLY B 314 ? 0.1404 0.1330 0.1432 -0.0150 0.0053 0.0088 399 GLY B CA 5406 C C . GLY B 314 ? 0.1207 0.1105 0.1228 -0.0147 0.0057 0.0104 399 GLY B C 5407 O O . GLY B 314 ? 0.1066 0.0944 0.1086 -0.0139 0.0053 0.0106 399 GLY B O 5408 N N . ILE B 315 ? 0.1328 0.1225 0.1343 -0.0151 0.0064 0.0116 400 ILE B N 5409 C CA . ILE B 315 ? 0.1580 0.1454 0.1586 -0.0146 0.0067 0.0134 400 ILE B CA 5410 C C . ILE B 315 ? 0.1687 0.1528 0.1700 -0.0151 0.0074 0.0137 400 ILE B C 5411 O O . ILE B 315 ? 0.1665 0.1485 0.1673 -0.0142 0.0073 0.0149 400 ILE B O 5412 C CB . ILE B 315 ? 0.1789 0.1670 0.1788 -0.0151 0.0075 0.0147 400 ILE B CB 5413 C CG1 . ILE B 315 ? 0.1702 0.1566 0.1690 -0.0142 0.0076 0.0166 400 ILE B CG1 5414 C CG2 . ILE B 315 ? 0.2287 0.2162 0.2296 -0.0169 0.0088 0.0146 400 ILE B CG2 5415 C CD1 . ILE B 315 ? 0.2537 0.2411 0.2516 -0.0145 0.0083 0.0181 400 ILE B CD1 5416 N N . ASN B 316 ? 0.1546 0.1384 0.1572 -0.0164 0.0079 0.0125 401 ASN B N 5417 C CA . ASN B 316 ? 0.2468 0.2273 0.2500 -0.0170 0.0087 0.0125 401 ASN B CA 5418 C C . ASN B 316 ? 0.2646 0.2444 0.2682 -0.0162 0.0079 0.0114 401 ASN B C 5419 O O . ASN B 316 ? 0.2788 0.2560 0.2832 -0.0166 0.0084 0.0112 401 ASN B O 5420 C CB . ASN B 316 ? 0.2940 0.2744 0.2984 -0.0190 0.0099 0.0116 401 ASN B CB 5421 C CG . ASN B 316 ? 0.3731 0.3535 0.3772 -0.0199 0.0109 0.0129 401 ASN B CG 5422 O OD1 . ASN B 316 ? 0.5633 0.5454 0.5680 -0.0214 0.0115 0.0121 401 ASN B OD1 5423 N ND2 . ASN B 316 ? 0.3667 0.3453 0.3698 -0.0190 0.0112 0.0150 401 ASN B ND2 5424 N N . GLU B 317 ? 0.1800 0.1620 0.1833 -0.0152 0.0066 0.0108 402 GLU B N 5425 C CA . GLU B 317 ? 0.1467 0.1283 0.1503 -0.0144 0.0058 0.0097 402 GLU B CA 5426 C C . GLU B 317 ? 0.1567 0.1375 0.1593 -0.0127 0.0050 0.0108 402 GLU B C 5427 O O . GLU B 317 ? 0.1087 0.0906 0.1103 -0.0120 0.0047 0.0117 402 GLU B O 5428 C CB . GLU B 317 ? 0.1140 0.0987 0.1180 -0.0145 0.0051 0.0081 402 GLU B CB 5429 C CG . GLU B 317 ? 0.2121 0.1983 0.2171 -0.0162 0.0058 0.0070 402 GLU B CG 5430 C CD . GLU B 317 ? 0.3323 0.3169 0.3383 -0.0174 0.0064 0.0060 402 GLU B CD 5431 O OE1 . GLU B 317 ? 0.2793 0.2617 0.2854 -0.0168 0.0062 0.0060 402 GLU B OE1 5432 O OE2 . GLU B 317 ? 0.4828 0.4682 0.4897 -0.0190 0.0072 0.0052 402 GLU B OE2 5433 N N . TRP B 318 ? 0.1536 0.1327 0.1564 -0.0121 0.0047 0.0104 403 TRP B N 5434 C CA . TRP B 318 ? 0.1259 0.1045 0.1280 -0.0106 0.0040 0.0113 403 TRP B CA 5435 C C . TRP B 318 ? 0.1240 0.1050 0.1255 -0.0097 0.0028 0.0107 403 TRP B C 5436 O O . TRP B 318 ? 0.1454 0.1279 0.1474 -0.0100 0.0025 0.0093 403 TRP B O 5437 C CB . TRP B 318 ? 0.1885 0.1648 0.1912 -0.0102 0.0040 0.0110 403 TRP B CB 5438 C CG . TRP B 318 ? 0.2149 0.1884 0.2183 -0.0111 0.0053 0.0114 403 TRP B CG 5439 C CD1 . TRP B 318 ? 0.2646 0.2371 0.2690 -0.0123 0.0059 0.0100 403 TRP B CD1 5440 C CD2 . TRP B 318 ? 0.2333 0.2046 0.2364 -0.0109 0.0061 0.0132 403 TRP B CD2 5441 N NE1 . TRP B 318 ? 0.2639 0.2336 0.2688 -0.0129 0.0072 0.0108 403 TRP B NE1 5442 C CE2 . TRP B 318 ? 0.2746 0.2434 0.2786 -0.0120 0.0074 0.0128 403 TRP B CE2 5443 C CE3 . TRP B 318 ? 0.2882 0.2595 0.2902 -0.0098 0.0060 0.0151 403 TRP B CE3 5444 C CZ2 . TRP B 318 ? 0.2798 0.2457 0.2838 -0.0120 0.0086 0.0145 403 TRP B CZ2 5445 C CZ3 . TRP B 318 ? 0.3826 0.3515 0.3846 -0.0098 0.0071 0.0168 403 TRP B CZ3 5446 C CH2 . TRP B 318 ? 0.3299 0.2959 0.3329 -0.0108 0.0084 0.0165 403 TRP B CH2 5447 N N . SER B 319 ? 0.1144 0.0959 0.1149 -0.0087 0.0024 0.0117 404 SER B N 5448 C CA . SER B 319 ? 0.0848 0.0680 0.0847 -0.0078 0.0014 0.0111 404 SER B CA 5449 C C . SER B 319 ? 0.1141 0.0964 0.1135 -0.0067 0.0008 0.0118 404 SER B C 5450 O O . SER B 319 ? 0.1102 0.0906 0.1102 -0.0065 0.0010 0.0119 404 SER B O 5451 C CB . SER B 319 ? 0.1217 0.1070 0.1208 -0.0078 0.0013 0.0114 404 SER B CB 5452 O OG . SER B 319 ? 0.1214 0.1064 0.1197 -0.0077 0.0017 0.0129 404 SER B OG 5453 N N . GLY B 320 ? 0.1155 0.0991 0.1140 -0.0059 0.0002 0.0120 405 GLY B N 5454 C CA . GLY B 320 ? 0.1053 0.0884 0.1033 -0.0049 -0.0004 0.0125 405 GLY B CA 5455 C C . GLY B 320 ? 0.1048 0.0897 0.1020 -0.0044 -0.0011 0.0122 405 GLY B C 5456 O O . GLY B 320 ? 0.0936 0.0800 0.0902 -0.0046 -0.0010 0.0123 405 GLY B O 5457 N N . TYR B 321 ? 0.0819 0.0667 0.0791 -0.0037 -0.0017 0.0117 406 TYR B N 5458 C CA . TYR B 321 ? 0.0814 0.0676 0.0778 -0.0033 -0.0023 0.0112 406 TYR B CA 5459 C C . TYR B 321 ? 0.0843 0.0717 0.0808 -0.0037 -0.0023 0.0101 406 TYR B C 5460 O O . TYR B 321 ? 0.0616 0.0486 0.0589 -0.0041 -0.0020 0.0094 406 TYR B O 5461 C CB . TYR B 321 ? 0.0820 0.0679 0.0786 -0.0027 -0.0029 0.0108 406 TYR B CB 5462 C CG . TYR B 321 ? 0.1021 0.0878 0.0983 -0.0021 -0.0031 0.0119 406 TYR B CG 5463 C CD1 . TYR B 321 ? 0.0932 0.0786 0.0892 -0.0021 -0.0027 0.0133 406 TYR B CD1 5464 C CD2 . TYR B 321 ? 0.0873 0.0733 0.0834 -0.0016 -0.0037 0.0116 406 TYR B CD2 5465 C CE1 . TYR B 321 ? 0.0995 0.0851 0.0952 -0.0014 -0.0029 0.0145 406 TYR B CE1 5466 C CE2 . TYR B 321 ? 0.1321 0.1184 0.1280 -0.0010 -0.0039 0.0126 406 TYR B CE2 5467 C CZ . TYR B 321 ? 0.1446 0.1307 0.1403 -0.0008 -0.0035 0.0141 406 TYR B CZ 5468 O OH . TYR B 321 ? 0.1092 0.0959 0.1046 -0.0001 -0.0038 0.0152 406 TYR B OH 5469 N N . SER B 322 ? 0.0727 0.0613 0.0683 -0.0035 -0.0025 0.0097 407 SER B N 5470 C CA . SER B 322 ? 0.0732 0.0627 0.0688 -0.0035 -0.0024 0.0087 407 SER B CA 5471 C C . SER B 322 ? 0.0830 0.0732 0.0780 -0.0031 -0.0028 0.0081 407 SER B C 5472 O O . SER B 322 ? 0.1049 0.0954 0.0991 -0.0029 -0.0030 0.0086 407 SER B O 5473 C CB . SER B 322 ? 0.0681 0.0588 0.0637 -0.0040 -0.0019 0.0088 407 SER B CB 5474 O OG . SER B 322 ? 0.0930 0.0845 0.0876 -0.0041 -0.0018 0.0095 407 SER B OG 5475 N N . GLY B 323 ? 0.0650 0.0553 0.0600 -0.0029 -0.0028 0.0072 408 GLY B N 5476 C CA . GLY B 323 ? 0.0771 0.0678 0.0716 -0.0025 -0.0030 0.0065 408 GLY B CA 5477 C C . GLY B 323 ? 0.0907 0.0817 0.0852 -0.0023 -0.0027 0.0056 408 GLY B C 5478 O O . GLY B 323 ? 0.0863 0.0775 0.0816 -0.0022 -0.0025 0.0054 408 GLY B O 5479 N N . SER B 324 ? 0.0670 0.0583 0.0608 -0.0021 -0.0026 0.0050 409 SER B N 5480 C CA . SER B 324 ? 0.0676 0.0589 0.0614 -0.0017 -0.0022 0.0042 409 SER B CA 5481 C C . SER B 324 ? 0.0919 0.0821 0.0862 -0.0013 -0.0023 0.0038 409 SER B C 5482 O O . SER B 324 ? 0.0990 0.0885 0.0933 -0.0013 -0.0028 0.0040 409 SER B O 5483 C CB . SER B 324 ? 0.1105 0.1024 0.1034 -0.0018 -0.0018 0.0036 409 SER B CB 5484 O OG . SER B 324 ? 0.1609 0.1524 0.1532 -0.0021 -0.0021 0.0035 409 SER B OG 5485 N N . PHE B 325 ? 0.0790 0.0692 0.0737 -0.0008 -0.0020 0.0034 410 PHE B N 5486 C CA . PHE B 325 ? 0.1179 0.1071 0.1127 -0.0002 -0.0020 0.0030 410 PHE B CA 5487 C C . PHE B 325 ? 0.0875 0.0769 0.0823 0.0004 -0.0013 0.0026 410 PHE B C 5488 O O . PHE B 325 ? 0.1263 0.1168 0.1214 0.0005 -0.0010 0.0026 410 PHE B O 5489 C CB . PHE B 325 ? 0.0682 0.0570 0.0638 -0.0001 -0.0024 0.0033 410 PHE B CB 5490 C CG . PHE B 325 ? 0.0863 0.0762 0.0827 0.0002 -0.0023 0.0035 410 PHE B CG 5491 C CD1 . PHE B 325 ? 0.0846 0.0753 0.0814 -0.0003 -0.0024 0.0038 410 PHE B CD1 5492 C CD2 . PHE B 325 ? 0.0987 0.0887 0.0955 0.0010 -0.0021 0.0033 410 PHE B CD2 5493 C CE1 . PHE B 325 ? 0.1189 0.1108 0.1165 -0.0002 -0.0023 0.0038 410 PHE B CE1 5494 C CE2 . PHE B 325 ? 0.1053 0.0966 0.1028 0.0012 -0.0021 0.0034 410 PHE B CE2 5495 C CZ . PHE B 325 ? 0.1069 0.0993 0.1049 0.0005 -0.0022 0.0036 410 PHE B CZ 5496 N N . VAL B 326 ? 0.1113 0.0995 0.1059 0.0009 -0.0010 0.0021 411 VAL B N 5497 C CA . VAL B 326 ? 0.0856 0.0738 0.0803 0.0016 -0.0002 0.0017 411 VAL B CA 5498 C C . VAL B 326 ? 0.1371 0.1245 0.1323 0.0025 -0.0001 0.0019 411 VAL B C 5499 O O . VAL B 326 ? 0.1068 0.0935 0.1021 0.0024 -0.0005 0.0022 411 VAL B O 5500 C CB . VAL B 326 ? 0.1106 0.0978 0.1043 0.0014 0.0004 0.0009 411 VAL B CB 5501 C CG1 . VAL B 326 ? 0.0875 0.0758 0.0806 0.0006 0.0002 0.0008 411 VAL B CG1 5502 C CG2 . VAL B 326 ? 0.1542 0.1398 0.1476 0.0012 0.0003 0.0007 411 VAL B CG2 5503 N N . GLN B 327 ? 0.0719 0.0597 0.0673 0.0034 0.0005 0.0019 412 GLN B N 5504 C CA . GLN B 327 ? 0.0747 0.0619 0.0705 0.0045 0.0008 0.0022 412 GLN B CA 5505 C C . GLN B 327 ? 0.0924 0.0781 0.0878 0.0051 0.0019 0.0017 412 GLN B C 5506 O O . GLN B 327 ? 0.0699 0.0562 0.0652 0.0054 0.0025 0.0014 412 GLN B O 5507 C CB . GLN B 327 ? 0.0718 0.0611 0.0686 0.0052 0.0007 0.0027 412 GLN B CB 5508 C CG . GLN B 327 ? 0.0572 0.0478 0.0544 0.0044 -0.0001 0.0031 412 GLN B CG 5509 C CD . GLN B 327 ? 0.0929 0.0857 0.0910 0.0050 -0.0003 0.0034 412 GLN B CD 5510 O OE1 . GLN B 327 ? 0.0830 0.0770 0.0814 0.0057 0.0002 0.0035 412 GLN B OE1 5511 N NE2 . GLN B 327 ? 0.1378 0.1313 0.1363 0.0047 -0.0009 0.0037 412 GLN B NE2 5512 N N . HIS B 328 A 0.0843 0.0681 0.0794 0.0052 0.0021 0.0016 412 HIS B N 5513 C CA . HIS B 328 A 0.1020 0.0838 0.0967 0.0056 0.0032 0.0010 412 HIS B CA 5514 C C . HIS B 328 A 0.1033 0.0851 0.0985 0.0072 0.0040 0.0016 412 HIS B C 5515 O O . HIS B 328 A 0.1125 0.0955 0.1083 0.0079 0.0036 0.0025 412 HIS B O 5516 C CB . HIS B 328 A 0.1074 0.0872 0.1017 0.0050 0.0034 0.0007 412 HIS B CB 5517 C CG . HIS B 328 A 0.1138 0.0936 0.1074 0.0036 0.0029 0.0000 412 HIS B CG 5518 N ND1 . HIS B 328 A 0.1304 0.1090 0.1233 0.0029 0.0035 -0.0010 412 HIS B ND1 5519 C CD2 . HIS B 328 A 0.0910 0.0721 0.0846 0.0027 0.0018 0.0002 412 HIS B CD2 5520 C CE1 . HIS B 328 A 0.1308 0.1101 0.1232 0.0017 0.0028 -0.0014 412 HIS B CE1 5521 N NE2 . HIS B 328 A 0.1304 0.1112 0.1233 0.0017 0.0018 -0.0006 412 HIS B NE2 5522 N N . PRO B 329 B 0.0941 0.0745 0.0890 0.0078 0.0052 0.0011 412 PRO B N 5523 C CA . PRO B 329 B 0.1364 0.1165 0.1318 0.0095 0.0061 0.0017 412 PRO B CA 5524 C C . PRO B 329 B 0.1616 0.1406 0.1573 0.0103 0.0061 0.0026 412 PRO B C 5525 O O . PRO B 329 B 0.1692 0.1491 0.1655 0.0118 0.0064 0.0035 412 PRO B O 5526 C CB . PRO B 329 B 0.1916 0.1696 0.1865 0.0096 0.0074 0.0007 412 PRO B CB 5527 C CG . PRO B 329 B 0.1979 0.1765 0.1921 0.0081 0.0070 -0.0004 412 PRO B CG 5528 C CD . PRO B 329 B 0.1410 0.1204 0.1352 0.0069 0.0057 -0.0001 412 PRO B CD 5529 N N . GLU B 330 C 0.1486 0.1260 0.1439 0.0093 0.0059 0.0023 412 GLU B N 5530 C CA . GLU B 330 C 0.1531 0.1296 0.1485 0.0099 0.0059 0.0032 412 GLU B CA 5531 C C . GLU B 330 C 0.2129 0.1920 0.2090 0.0103 0.0048 0.0042 412 GLU B C 5532 O O . GLU B 330 C 0.2267 0.2058 0.2231 0.0113 0.0049 0.0051 412 GLU B O 5533 C CB . GLU B 330 C 0.1699 0.1446 0.1648 0.0085 0.0057 0.0026 412 GLU B CB 5534 C CG . GLU B 330 C 0.2148 0.1865 0.2091 0.0081 0.0069 0.0017 412 GLU B CG 5535 C CD . GLU B 330 C 0.2490 0.2209 0.2427 0.0069 0.0070 0.0004 412 GLU B CD 5536 O OE1 . GLU B 330 C 0.1524 0.1267 0.1463 0.0066 0.0061 0.0003 412 GLU B OE1 5537 O OE2 . GLU B 330 C 0.2004 0.1702 0.1936 0.0063 0.0079 -0.0007 412 GLU B OE2 5538 N N . LEU B 331 D 0.1328 0.1141 0.1291 0.0096 0.0039 0.0039 412 LEU B N 5539 C CA . LEU B 331 D 0.1223 0.1062 0.1192 0.0097 0.0029 0.0046 412 LEU B CA 5540 C C . LEU B 331 D 0.1421 0.1283 0.1396 0.0108 0.0031 0.0050 412 LEU B C 5541 O O . LEU B 331 D 0.1446 0.1327 0.1427 0.0117 0.0028 0.0058 412 LEU B O 5542 C CB . LEU B 331 D 0.1322 0.1171 0.1291 0.0082 0.0019 0.0041 412 LEU B CB 5543 C CG . LEU B 331 D 0.1167 0.1043 0.1143 0.0081 0.0010 0.0045 412 LEU B CG 5544 C CD1 . LEU B 331 D 0.1606 0.1484 0.1583 0.0085 0.0006 0.0051 412 LEU B CD1 5545 C CD2 . LEU B 331 D 0.1063 0.0945 0.1037 0.0067 0.0002 0.0040 412 LEU B CD2 5546 N N . THR B 332 ? 0.1104 0.0969 0.1079 0.0108 0.0035 0.0044 413 THR B N 5547 C CA . THR B 332 ? 0.1018 0.0909 0.0999 0.0115 0.0036 0.0047 413 THR B CA 5548 C C . THR B 332 ? 0.1535 0.1423 0.1519 0.0133 0.0047 0.0051 413 THR B C 5549 O O . THR B 332 ? 0.1947 0.1860 0.1938 0.0144 0.0047 0.0057 413 THR B O 5550 C CB . THR B 332 ? 0.1625 0.1524 0.1604 0.0105 0.0035 0.0039 413 THR B CB 5551 O OG1 . THR B 332 ? 0.1236 0.1113 0.1209 0.0104 0.0044 0.0032 413 THR B OG1 5552 C CG2 . THR B 332 ? 0.1252 0.1153 0.1229 0.0088 0.0024 0.0036 413 THR B CG2 5553 N N . GLY B 333 ? 0.1344 0.1201 0.1322 0.0137 0.0057 0.0048 414 GLY B N 5554 C CA . GLY B 333 ? 0.1238 0.1088 0.1219 0.0154 0.0070 0.0052 414 GLY B CA 5555 C C . GLY B 333 ? 0.2227 0.2080 0.2207 0.0154 0.0077 0.0043 414 GLY B C 5556 O O . GLY B 333 ? 0.2190 0.2038 0.2173 0.0168 0.0088 0.0045 414 GLY B O 5557 N N . LEU B 334 ? 0.1503 0.1364 0.1480 0.0138 0.0070 0.0035 415 LEU B N 5558 C CA . LEU B 334 ? 0.1678 0.1543 0.1653 0.0135 0.0076 0.0026 415 LEU B CA 5559 C C . LEU B 334 ? 0.2097 0.1929 0.2063 0.0131 0.0086 0.0015 415 LEU B C 5560 O O . LEU B 334 ? 0.2411 0.2218 0.2373 0.0128 0.0088 0.0015 415 LEU B O 5561 C CB . LEU B 334 ? 0.1425 0.1311 0.1399 0.0119 0.0065 0.0021 415 LEU B CB 5562 C CG . LEU B 334 ? 0.2318 0.2236 0.2300 0.0120 0.0055 0.0029 415 LEU B CG 5563 C CD1 . LEU B 334 ? 0.1876 0.1807 0.1856 0.0102 0.0046 0.0025 415 LEU B CD1 5564 C CD2 . LEU B 334 ? 0.2538 0.2479 0.2529 0.0134 0.0061 0.0033 415 LEU B CD2 5565 N N . ASP B 335 ? 0.2103 0.1935 0.2066 0.0130 0.0093 0.0006 416 ASP B N 5566 C CA . ASP B 335 ? 0.2648 0.2451 0.2602 0.0124 0.0104 -0.0006 416 ASP B CA 5567 C C . ASP B 335 ? 0.2487 0.2296 0.2433 0.0104 0.0097 -0.0017 416 ASP B C 5568 O O . ASP B 335 ? 0.2682 0.2478 0.2620 0.0098 0.0105 -0.0030 416 ASP B O 5569 C CB . ASP B 335 ? 0.2996 0.2793 0.2952 0.0138 0.0119 -0.0011 416 ASP B CB 5570 C CG . ASP B 335 ? 0.4438 0.4265 0.4398 0.0140 0.0118 -0.0012 416 ASP B CG 5571 O OD1 . ASP B 335 ? 0.5037 0.4889 0.4997 0.0128 0.0106 -0.0011 416 ASP B OD1 5572 O OD2 . ASP B 335 ? 0.5826 0.5654 0.5790 0.0153 0.0129 -0.0013 416 ASP B OD2 5573 N N . CYS B 336 ? 0.2034 0.1864 0.1982 0.0095 0.0083 -0.0012 417 CYS B N 5574 C CA . CYS B 336 ? 0.1418 0.1256 0.1358 0.0078 0.0076 -0.0019 417 CYS B CA 5575 C C . CYS B 336 ? 0.1510 0.1355 0.1451 0.0069 0.0063 -0.0011 417 CYS B C 5576 O O . CYS B 336 ? 0.1283 0.1132 0.1232 0.0076 0.0058 -0.0002 417 CYS B O 5577 C CB . CYS B 336 ? 0.1821 0.1684 0.1762 0.0076 0.0076 -0.0021 417 CYS B CB 5578 S SG . CYS B 336 ? 0.3167 0.3060 0.3120 0.0086 0.0071 -0.0008 417 CYS B SG 5579 N N . ILE B 337 ? 0.1429 0.1277 0.1364 0.0055 0.0056 -0.0016 418 ILE B N 5580 C CA . ILE B 337 ? 0.1183 0.1037 0.1119 0.0046 0.0044 -0.0010 418 ILE B CA 5581 C C . ILE B 337 ? 0.1093 0.0973 0.1033 0.0044 0.0037 -0.0004 418 ILE B C 5582 O O . ILE B 337 ? 0.1241 0.1132 0.1177 0.0039 0.0039 -0.0007 418 ILE B O 5583 C CB . ILE B 337 ? 0.0953 0.0799 0.0880 0.0033 0.0041 -0.0016 418 ILE B CB 5584 C CG1 . ILE B 337 ? 0.1384 0.1205 0.1307 0.0033 0.0049 -0.0023 418 ILE B CG1 5585 C CG2 . ILE B 337 ? 0.1065 0.0918 0.0994 0.0026 0.0029 -0.0009 418 ILE B CG2 5586 C CD1 . ILE B 337 ? 0.1350 0.1166 0.1264 0.0019 0.0046 -0.0032 418 ILE B CD1 5587 N N . ARG B 338 ? 0.1188 0.1077 0.1137 0.0048 0.0031 0.0005 419 ARG B N 5588 C CA . ARG B 338 ? 0.1442 0.1354 0.1396 0.0045 0.0026 0.0010 419 ARG B CA 5589 C C . ARG B 338 ? 0.0906 0.0821 0.0857 0.0032 0.0017 0.0012 419 ARG B C 5590 O O . ARG B 338 ? 0.1214 0.1119 0.1165 0.0029 0.0011 0.0015 419 ARG B O 5591 C CB . ARG B 338 ? 0.1416 0.1339 0.1380 0.0054 0.0024 0.0017 419 ARG B CB 5592 C CG . ARG B 338 ? 0.1573 0.1518 0.1544 0.0047 0.0017 0.0021 419 ARG B CG 5593 C CD . ARG B 338 ? 0.1711 0.1670 0.1692 0.0055 0.0014 0.0027 419 ARG B CD 5594 N NE . ARG B 338 ? 0.2368 0.2346 0.2354 0.0064 0.0020 0.0027 419 ARG B NE 5595 C CZ . ARG B 338 ? 0.2373 0.2368 0.2368 0.0073 0.0019 0.0032 419 ARG B CZ 5596 N NH1 . ARG B 338 ? 0.1669 0.1665 0.1667 0.0073 0.0013 0.0036 419 ARG B NH1 5597 N NH2 . ARG B 338 ? 0.2732 0.2747 0.2733 0.0082 0.0024 0.0033 419 ARG B NH2 5598 N N . PRO B 339 ? 0.1229 0.1158 0.1178 0.0025 0.0016 0.0012 420 PRO B N 5599 C CA . PRO B 339 ? 0.0950 0.0882 0.0896 0.0014 0.0009 0.0016 420 PRO B CA 5600 C C . PRO B 339 ? 0.1040 0.0982 0.0996 0.0013 0.0004 0.0023 420 PRO B C 5601 O O . PRO B 339 ? 0.1119 0.1076 0.1082 0.0016 0.0006 0.0024 420 PRO B O 5602 C CB . PRO B 339 ? 0.1311 0.1256 0.1252 0.0009 0.0013 0.0015 420 PRO B CB 5603 C CG . PRO B 339 ? 0.1897 0.1845 0.1838 0.0017 0.0022 0.0008 420 PRO B CG 5604 C CD . PRO B 339 ? 0.1185 0.1127 0.1133 0.0028 0.0023 0.0009 420 PRO B CD 5605 N N . CYS B 340 ? 0.0627 0.0561 0.0584 0.0007 -0.0003 0.0027 421 CYS B N 5606 C CA . CYS B 340 ? 0.0808 0.0749 0.0772 0.0004 -0.0007 0.0032 421 CYS B CA 5607 C C . CYS B 340 ? 0.0884 0.0820 0.0844 -0.0005 -0.0011 0.0036 421 CYS B C 5608 O O . CYS B 340 ? 0.0676 0.0604 0.0628 -0.0007 -0.0012 0.0035 421 CYS B O 5609 C CB . CYS B 340 ? 0.0718 0.0654 0.0688 0.0009 -0.0010 0.0032 421 CYS B CB 5610 S SG . CYS B 340 ? 0.1114 0.1055 0.1088 0.0022 -0.0006 0.0030 421 CYS B SG 5611 N N . PHE B 341 ? 0.0411 0.0351 0.0377 -0.0011 -0.0014 0.0040 422 PHE B N 5612 C CA . PHE B 341 ? 0.0706 0.0638 0.0671 -0.0018 -0.0017 0.0045 422 PHE B CA 5613 C C . PHE B 341 ? 0.0832 0.0762 0.0805 -0.0021 -0.0020 0.0048 422 PHE B C 5614 O O . PHE B 341 ? 0.0789 0.0728 0.0770 -0.0021 -0.0019 0.0045 422 PHE B O 5615 C CB . PHE B 341 ? 0.0576 0.0516 0.0535 -0.0023 -0.0014 0.0049 422 PHE B CB 5616 C CG . PHE B 341 ? 0.0721 0.0672 0.0686 -0.0028 -0.0011 0.0051 422 PHE B CG 5617 C CD1 . PHE B 341 ? 0.0870 0.0837 0.0837 -0.0026 -0.0006 0.0047 422 PHE B CD1 5618 C CD2 . PHE B 341 ? 0.0610 0.0558 0.0580 -0.0035 -0.0011 0.0057 422 PHE B CD2 5619 C CE1 . PHE B 341 ? 0.0782 0.0763 0.0756 -0.0031 -0.0003 0.0049 422 PHE B CE1 5620 C CE2 . PHE B 341 ? 0.0925 0.0885 0.0902 -0.0041 -0.0007 0.0058 422 PHE B CE2 5621 C CZ . PHE B 341 ? 0.0787 0.0764 0.0765 -0.0040 -0.0003 0.0054 422 PHE B CZ 5622 N N . TRP B 342 ? 0.0315 0.0233 0.0287 -0.0024 -0.0023 0.0052 423 TRP B N 5623 C CA . TRP B 342 ? 0.0585 0.0499 0.0565 -0.0028 -0.0024 0.0054 423 TRP B CA 5624 C C . TRP B 342 ? 0.0701 0.0608 0.0680 -0.0035 -0.0023 0.0061 423 TRP B C 5625 O O . TRP B 342 ? 0.0548 0.0453 0.0518 -0.0035 -0.0023 0.0066 423 TRP B O 5626 C CB . TRP B 342 ? 0.0848 0.0750 0.0829 -0.0025 -0.0029 0.0052 423 TRP B CB 5627 C CG . TRP B 342 ? 0.0762 0.0655 0.0735 -0.0022 -0.0031 0.0055 423 TRP B CG 5628 C CD1 . TRP B 342 ? 0.0728 0.0620 0.0696 -0.0017 -0.0032 0.0051 423 TRP B CD1 5629 C CD2 . TRP B 342 ? 0.0659 0.0544 0.0630 -0.0024 -0.0033 0.0062 423 TRP B CD2 5630 N NE1 . TRP B 342 ? 0.0890 0.0777 0.0852 -0.0018 -0.0035 0.0055 423 TRP B NE1 5631 C CE2 . TRP B 342 ? 0.0859 0.0742 0.0823 -0.0021 -0.0035 0.0062 423 TRP B CE2 5632 C CE3 . TRP B 342 ? 0.0862 0.0741 0.0837 -0.0029 -0.0031 0.0068 423 TRP B CE3 5633 C CZ2 . TRP B 342 ? 0.0819 0.0698 0.0779 -0.0021 -0.0037 0.0068 423 TRP B CZ2 5634 C CZ3 . TRP B 342 ? 0.0770 0.0642 0.0741 -0.0028 -0.0033 0.0076 423 TRP B CZ3 5635 C CH2 . TRP B 342 ? 0.1038 0.0912 0.1003 -0.0024 -0.0036 0.0076 423 TRP B CH2 5636 N N . VAL B 343 ? 0.0223 0.0127 0.0209 -0.0041 -0.0021 0.0062 424 VAL B N 5637 C CA . VAL B 343 ? 0.0534 0.0429 0.0521 -0.0047 -0.0018 0.0070 424 VAL B CA 5638 C C . VAL B 343 ? 0.0582 0.0462 0.0576 -0.0048 -0.0018 0.0069 424 VAL B C 5639 O O . VAL B 343 ? 0.0707 0.0590 0.0708 -0.0051 -0.0018 0.0062 424 VAL B O 5640 C CB . VAL B 343 ? 0.0499 0.0403 0.0489 -0.0055 -0.0012 0.0071 424 VAL B CB 5641 C CG1 . VAL B 343 ? 0.0580 0.0472 0.0569 -0.0060 -0.0008 0.0082 424 VAL B CG1 5642 C CG2 . VAL B 343 ? 0.0542 0.0463 0.0527 -0.0053 -0.0010 0.0070 424 VAL B CG2 5643 N N . GLU B 344 ? 0.0680 0.0547 0.0671 -0.0047 -0.0019 0.0077 425 GLU B N 5644 C CA . GLU B 344 ? 0.1014 0.0864 0.1011 -0.0048 -0.0018 0.0078 425 GLU B CA 5645 C C . GLU B 344 ? 0.0960 0.0802 0.0962 -0.0056 -0.0011 0.0083 425 GLU B C 5646 O O . GLU B 344 ? 0.1018 0.0859 0.1015 -0.0058 -0.0007 0.0093 425 GLU B O 5647 C CB . GLU B 344 ? 0.1164 0.1005 0.1157 -0.0040 -0.0022 0.0085 425 GLU B CB 5648 C CG . GLU B 344 ? 0.1405 0.1228 0.1404 -0.0040 -0.0020 0.0087 425 GLU B CG 5649 C CD . GLU B 344 ? 0.1815 0.1631 0.1809 -0.0032 -0.0022 0.0098 425 GLU B CD 5650 O OE1 . GLU B 344 ? 0.1362 0.1184 0.1349 -0.0031 -0.0022 0.0107 425 GLU B OE1 5651 O OE2 . GLU B 344 ? 0.1570 0.1378 0.1568 -0.0028 -0.0024 0.0096 425 GLU B OE2 5652 N N . LEU B 345 ? 0.0742 0.0578 0.0753 -0.0062 -0.0008 0.0076 426 LEU B N 5653 C CA . LEU B 345 ? 0.0922 0.0748 0.0939 -0.0072 0.0001 0.0078 426 LEU B CA 5654 C C . LEU B 345 ? 0.1211 0.1012 0.1232 -0.0070 0.0004 0.0082 426 LEU B C 5655 O O . LEU B 345 ? 0.1398 0.1194 0.1425 -0.0072 0.0004 0.0072 426 LEU B O 5656 C CB . LEU B 345 ? 0.0790 0.0628 0.0815 -0.0082 0.0004 0.0066 426 LEU B CB 5657 C CG . LEU B 345 ? 0.1007 0.0870 0.1029 -0.0081 0.0000 0.0061 426 LEU B CG 5658 C CD1 . LEU B 345 ? 0.1162 0.1041 0.1194 -0.0090 0.0002 0.0049 426 LEU B CD1 5659 C CD2 . LEU B 345 ? 0.0938 0.0807 0.0954 -0.0082 0.0003 0.0070 426 LEU B CD2 5660 N N . ILE B 346 ? 0.0812 0.0600 0.0829 -0.0066 0.0006 0.0096 427 ILE B N 5661 C CA . ILE B 346 ? 0.0782 0.0548 0.0801 -0.0061 0.0009 0.0101 427 ILE B CA 5662 C C . ILE B 346 ? 0.1112 0.0857 0.1141 -0.0071 0.0020 0.0100 427 ILE B C 5663 O O . ILE B 346 ? 0.1193 0.0934 0.1221 -0.0078 0.0027 0.0106 427 ILE B O 5664 C CB . ILE B 346 ? 0.1020 0.0781 0.1031 -0.0052 0.0008 0.0119 427 ILE B CB 5665 C CG1 . ILE B 346 ? 0.1219 0.1001 0.1221 -0.0044 -0.0002 0.0118 427 ILE B CG1 5666 C CG2 . ILE B 346 ? 0.1213 0.0954 0.1229 -0.0044 0.0010 0.0125 427 ILE B CG2 5667 C CD1 . ILE B 346 ? 0.1402 0.1189 0.1396 -0.0036 -0.0003 0.0134 427 ILE B CD1 5668 N N . ARG B 347 ? 0.1081 0.0812 0.1116 -0.0071 0.0022 0.0092 428 ARG B N 5669 C CA . ARG B 347 ? 0.1042 0.0750 0.1086 -0.0080 0.0033 0.0089 428 ARG B CA 5670 C C . ARG B 347 ? 0.1398 0.1080 0.1444 -0.0071 0.0037 0.0097 428 ARG B C 5671 O O . ARG B 347 ? 0.1159 0.0845 0.1204 -0.0060 0.0030 0.0098 428 ARG B O 5672 C CB . ARG B 347 ? 0.1300 0.1016 0.1352 -0.0091 0.0034 0.0069 428 ARG B CB 5673 C CG . ARG B 347 ? 0.1352 0.1096 0.1404 -0.0100 0.0030 0.0061 428 ARG B CG 5674 C CD . ARG B 347 ? 0.1227 0.0970 0.1277 -0.0108 0.0038 0.0069 428 ARG B CD 5675 N NE . ARG B 347 ? 0.1136 0.0853 0.1194 -0.0119 0.0051 0.0069 428 ARG B NE 5676 C CZ . ARG B 347 ? 0.1284 0.1004 0.1351 -0.0134 0.0057 0.0055 428 ARG B CZ 5677 N NH1 . ARG B 347 ? 0.1385 0.1134 0.1454 -0.0140 0.0051 0.0040 428 ARG B NH1 5678 N NH2 . ARG B 347 ? 0.1286 0.0979 0.1359 -0.0144 0.0070 0.0055 428 ARG B NH2 5679 N N . GLY B 348 ? 0.1211 0.0867 0.1262 -0.0076 0.0049 0.0104 429 GLY B N 5680 C CA . GLY B 348 ? 0.1437 0.1067 0.1492 -0.0066 0.0055 0.0112 429 GLY B CA 5681 C C . GLY B 348 ? 0.1745 0.1366 0.1794 -0.0055 0.0057 0.0135 429 GLY B C 5682 O O . GLY B 348 ? 0.1680 0.1302 0.1724 -0.0060 0.0062 0.0146 429 GLY B O 5683 N N . ARG B 349 ? 0.2150 0.1764 0.2199 -0.0040 0.0055 0.0144 430 ARG B N 5684 C CA . ARG B 349 ? 0.2134 0.1743 0.2177 -0.0028 0.0057 0.0167 430 ARG B CA 5685 C C . ARG B 349 ? 0.2390 0.2029 0.2422 -0.0023 0.0046 0.0175 430 ARG B C 5686 O O . ARG B 349 ? 0.2557 0.2221 0.2585 -0.0025 0.0035 0.0164 430 ARG B O 5687 C CB . ARG B 349 ? 0.2765 0.2363 0.2812 -0.0012 0.0056 0.0173 430 ARG B CB 5688 C CG . ARG B 349 ? 0.2978 0.2539 0.3035 -0.0012 0.0070 0.0173 430 ARG B CG 5689 C CD . ARG B 349 ? 0.4568 0.4107 0.4625 -0.0010 0.0083 0.0193 430 ARG B CD 5690 N NE . ARG B 349 ? 0.4869 0.4372 0.4935 -0.0020 0.0099 0.0188 430 ARG B NE 5691 C CZ . ARG B 349 ? 0.5284 0.4758 0.5359 -0.0013 0.0109 0.0187 430 ARG B CZ 5692 N NH1 . ARG B 349 ? 0.6479 0.5958 0.6555 0.0004 0.0103 0.0192 430 ARG B NH1 5693 N NH2 . ARG B 349 ? 0.4611 0.4052 0.4695 -0.0024 0.0125 0.0180 430 ARG B NH2 5694 N N . PRO B 350 ? 0.2634 0.2272 0.2659 -0.0018 0.0050 0.0196 431 PRO B N 5695 C CA . PRO B 350 ? 0.2570 0.2179 0.2599 -0.0015 0.0063 0.0212 431 PRO B CA 5696 C C . PRO B 350 ? 0.3029 0.2622 0.3060 -0.0030 0.0076 0.0212 431 PRO B C 5697 O O . PRO B 350 ? 0.3272 0.2835 0.3307 -0.0030 0.0089 0.0223 431 PRO B O 5698 C CB . PRO B 350 ? 0.3531 0.3154 0.3550 -0.0001 0.0059 0.0236 431 PRO B CB 5699 C CG . PRO B 350 ? 0.4275 0.3936 0.4285 0.0001 0.0044 0.0228 431 PRO B CG 5700 C CD . PRO B 350 ? 0.3387 0.3053 0.3400 -0.0013 0.0041 0.0205 431 PRO B CD 5701 N N . LYS B 351 ? 0.2464 0.2076 0.2493 -0.0044 0.0072 0.0198 432 LYS B N 5702 C CA . LYS B 351 ? 0.3037 0.2640 0.3067 -0.0059 0.0082 0.0198 432 LYS B CA 5703 C C . LYS B 351 ? 0.3213 0.2789 0.3256 -0.0073 0.0094 0.0184 432 LYS B C 5704 O O . LYS B 351 ? 0.2742 0.2303 0.2788 -0.0085 0.0106 0.0186 432 LYS B O 5705 C CB . LYS B 351 ? 0.2912 0.2548 0.2937 -0.0068 0.0074 0.0190 432 LYS B CB 5706 C CG . LYS B 351 ? 0.3368 0.3029 0.3380 -0.0058 0.0066 0.0204 432 LYS B CG 5707 C CD . LYS B 351 ? 0.4068 0.3714 0.4075 -0.0051 0.0075 0.0229 432 LYS B CD 5708 C CE . LYS B 351 ? 0.4415 0.4089 0.4408 -0.0046 0.0068 0.0242 432 LYS B CE 5709 N NZ . LYS B 351 ? 0.4272 0.3952 0.4262 -0.0059 0.0075 0.0244 432 LYS B NZ 5710 N N . GLU B 352 ? 0.2105 0.1678 0.2155 -0.0071 0.0090 0.0168 433 GLU B N 5711 C CA . GLU B 352 ? 0.2254 0.1806 0.2315 -0.0085 0.0101 0.0150 433 GLU B CA 5712 C C . GLU B 352 ? 0.1903 0.1426 0.1971 -0.0076 0.0106 0.0150 433 GLU B C 5713 O O . GLU B 352 ? 0.2135 0.1664 0.2200 -0.0060 0.0098 0.0156 433 GLU B O 5714 C CB . GLU B 352 ? 0.2129 0.1708 0.2193 -0.0097 0.0092 0.0127 433 GLU B CB 5715 C CG . GLU B 352 ? 0.2115 0.1723 0.2172 -0.0104 0.0086 0.0126 433 GLU B CG 5716 C CD . GLU B 352 ? 0.2229 0.1865 0.2289 -0.0113 0.0078 0.0105 433 GLU B CD 5717 O OE1 . GLU B 352 ? 0.1519 0.1178 0.1573 -0.0104 0.0065 0.0102 433 GLU B OE1 5718 O OE2 . GLU B 352 ? 0.2007 0.1642 0.2075 -0.0130 0.0085 0.0091 433 GLU B OE2 5719 N N . ASN B 353 ? 0.2224 0.1717 0.2302 -0.0088 0.0121 0.0141 435 ASN B N 5720 C CA . ASN B 353 ? 0.2693 0.2154 0.2779 -0.0079 0.0130 0.0142 435 ASN B CA 5721 C C . ASN B 353 ? 0.2029 0.1497 0.2119 -0.0079 0.0124 0.0120 435 ASN B C 5722 O O . ASN B 353 ? 0.2134 0.1584 0.2233 -0.0091 0.0133 0.0103 435 ASN B O 5723 C CB . ASN B 353 ? 0.3320 0.2741 0.3413 -0.0091 0.0151 0.0143 435 ASN B CB 5724 C CG . ASN B 353 ? 0.3802 0.3206 0.3890 -0.0085 0.0160 0.0170 435 ASN B CG 5725 O OD1 . ASN B 353 ? 0.4749 0.4131 0.4840 -0.0099 0.0175 0.0173 435 ASN B OD1 5726 N ND2 . ASN B 353 ? 0.4391 0.3807 0.4472 -0.0065 0.0152 0.0192 435 ASN B ND2 5727 N N . THR B 354 ? 0.1707 0.1203 0.1792 -0.0067 0.0108 0.0121 436 THR B N 5728 C CA . THR B 354 ? 0.1559 0.1065 0.1648 -0.0064 0.0100 0.0103 436 THR B CA 5729 C C . THR B 354 ? 0.1798 0.1301 0.1885 -0.0043 0.0095 0.0116 436 THR B C 5730 O O . THR B 354 ? 0.1936 0.1436 0.2018 -0.0030 0.0095 0.0138 436 THR B O 5731 C CB . THR B 354 ? 0.1667 0.1211 0.1751 -0.0071 0.0086 0.0090 436 THR B CB 5732 O OG1 . THR B 354 ? 0.1685 0.1252 0.1758 -0.0061 0.0075 0.0105 436 THR B OG1 5733 C CG2 . THR B 354 ? 0.1485 0.1036 0.1572 -0.0092 0.0090 0.0075 436 THR B CG2 5734 N N . ILE B 355 ? 0.1498 0.1007 0.1589 -0.0039 0.0090 0.0102 437 ILE B N 5735 C CA . ILE B 355 ? 0.1479 0.0991 0.1569 -0.0020 0.0084 0.0112 437 ILE B CA 5736 C C . ILE B 355 ? 0.1375 0.0925 0.1456 -0.0015 0.0066 0.0112 437 ILE B C 5737 O O . ILE B 355 ? 0.1493 0.1053 0.1571 0.0000 0.0059 0.0122 437 ILE B O 5738 C CB . ILE B 355 ? 0.1811 0.1309 0.1910 -0.0017 0.0089 0.0097 437 ILE B CB 5739 C CG1 . ILE B 355 ? 0.1528 0.1049 0.1627 -0.0029 0.0080 0.0073 437 ILE B CG1 5740 C CG2 . ILE B 355 ? 0.2123 0.1580 0.2231 -0.0024 0.0108 0.0094 437 ILE B CG2 5741 C CD1 . ILE B 355 ? 0.2015 0.1527 0.2122 -0.0027 0.0084 0.0058 437 ILE B CD1 5742 N N . TRP B 356 ? 0.1162 0.0733 0.1239 -0.0028 0.0060 0.0101 438 TRP B N 5743 C CA . TRP B 356 ? 0.1102 0.0707 0.1172 -0.0025 0.0045 0.0097 438 TRP B CA 5744 C C . TRP B 356 ? 0.1205 0.0829 0.1266 -0.0029 0.0040 0.0105 438 TRP B C 5745 O O . TRP B 356 ? 0.1109 0.0722 0.1170 -0.0037 0.0047 0.0111 438 TRP B O 5746 C CB . TRP B 356 ? 0.0987 0.0604 0.1060 -0.0035 0.0041 0.0075 438 TRP B CB 5747 C CG . TRP B 356 ? 0.1044 0.0656 0.1122 -0.0052 0.0049 0.0062 438 TRP B CG 5748 C CD1 . TRP B 356 ? 0.1354 0.0942 0.1440 -0.0061 0.0061 0.0052 438 TRP B CD1 5749 C CD2 . TRP B 356 ? 0.1148 0.0781 0.1222 -0.0063 0.0045 0.0057 438 TRP B CD2 5750 N NE1 . TRP B 356 ? 0.1364 0.0959 0.1452 -0.0078 0.0065 0.0041 438 TRP B NE1 5751 C CE2 . TRP B 356 ? 0.1357 0.0980 0.1437 -0.0079 0.0055 0.0044 438 TRP B CE2 5752 C CE3 . TRP B 356 ? 0.1184 0.0844 0.1249 -0.0061 0.0034 0.0061 438 TRP B CE3 5753 C CZ2 . TRP B 356 ? 0.1673 0.1315 0.1753 -0.0093 0.0054 0.0036 438 TRP B CZ2 5754 C CZ3 . TRP B 356 ? 0.1395 0.1071 0.1460 -0.0074 0.0034 0.0054 438 TRP B CZ3 5755 C CH2 . TRP B 356 ? 0.1448 0.1116 0.1520 -0.0089 0.0043 0.0042 438 TRP B CH2 5756 N N . THR B 357 ? 0.1226 0.0876 0.1280 -0.0024 0.0027 0.0105 439 THR B N 5757 C CA . THR B 357 ? 0.1507 0.1179 0.1553 -0.0029 0.0021 0.0108 439 THR B CA 5758 C C . THR B 357 ? 0.1405 0.1101 0.1448 -0.0031 0.0011 0.0095 439 THR B C 5759 O O . THR B 357 ? 0.1103 0.0806 0.1145 -0.0023 0.0004 0.0092 439 THR B O 5760 C CB . THR B 357 ? 0.2154 0.1832 0.2192 -0.0017 0.0018 0.0127 439 THR B CB 5761 O OG1 . THR B 357 ? 0.1647 0.1303 0.1687 -0.0014 0.0028 0.0143 439 THR B OG1 5762 C CG2 . THR B 357 ? 0.1903 0.1604 0.1931 -0.0022 0.0012 0.0129 439 THR B CG2 5763 N N . SER B 358 ? 0.1118 0.0827 0.1160 -0.0041 0.0010 0.0087 440 SER B N 5764 C CA . SER B 358 ? 0.1270 0.1002 0.1309 -0.0042 0.0001 0.0076 440 SER B CA 5765 C C . SER B 358 ? 0.1843 0.1591 0.1878 -0.0050 0.0000 0.0074 440 SER B C 5766 O O . SER B 358 ? 0.1648 0.1390 0.1684 -0.0056 0.0007 0.0079 440 SER B O 5767 C CB . SER B 358 ? 0.1415 0.1147 0.1461 -0.0047 0.0002 0.0059 440 SER B CB 5768 O OG . SER B 358 ? 0.1345 0.1097 0.1388 -0.0045 -0.0007 0.0051 440 SER B OG 5769 N N . GLY B 359 ? 0.2067 0.1835 0.2097 -0.0048 -0.0007 0.0068 441 GLY B N 5770 C CA . GLY B 359 ? 0.1565 0.1350 0.1592 -0.0054 -0.0008 0.0067 441 GLY B CA 5771 C C . GLY B 359 ? 0.1791 0.1595 0.1820 -0.0057 -0.0012 0.0053 441 GLY B C 5772 O O . GLY B 359 ? 0.2292 0.2099 0.2323 -0.0052 -0.0017 0.0047 441 GLY B O 5773 N N . SER B 360 ? 0.1135 0.0952 0.1166 -0.0064 -0.0010 0.0050 442 SER B N 5774 C CA . SER B 360 ? 0.1314 0.1153 0.1346 -0.0065 -0.0014 0.0040 442 SER B CA 5775 C C . SER B 360 ? 0.1318 0.1171 0.1343 -0.0060 -0.0017 0.0045 442 SER B C 5776 O O . SER B 360 ? 0.1333 0.1179 0.1352 -0.0058 -0.0016 0.0055 442 SER B O 5777 C CB . SER B 360 ? 0.1242 0.1091 0.1282 -0.0077 -0.0009 0.0030 442 SER B CB 5778 O OG . SER B 360 ? 0.1443 0.1295 0.1483 -0.0084 -0.0004 0.0034 442 SER B OG 5779 N N . SER B 361 ? 0.1175 0.1047 0.1199 -0.0058 -0.0020 0.0039 443 SER B N 5780 C CA . SER B 361 ? 0.1256 0.1139 0.1273 -0.0053 -0.0022 0.0043 443 SER B CA 5781 C C . SER B 361 ? 0.1124 0.1030 0.1144 -0.0055 -0.0021 0.0038 443 SER B C 5782 O O . SER B 361 ? 0.1179 0.1097 0.1206 -0.0059 -0.0021 0.0030 443 SER B O 5783 C CB . SER B 361 ? 0.1435 0.1316 0.1446 -0.0043 -0.0028 0.0044 443 SER B CB 5784 O OG . SER B 361 ? 0.2001 0.1894 0.2016 -0.0039 -0.0031 0.0037 443 SER B OG 5785 N N . ILE B 362 ? 0.0532 0.0445 0.0547 -0.0053 -0.0020 0.0042 444 ILE B N 5786 C CA . ILE B 362 ? 0.0614 0.0550 0.0631 -0.0052 -0.0019 0.0039 444 ILE B CA 5787 C C . ILE B 362 ? 0.0787 0.0724 0.0796 -0.0042 -0.0021 0.0042 444 ILE B C 5788 O O . ILE B 362 ? 0.0761 0.0685 0.0763 -0.0040 -0.0022 0.0047 444 ILE B O 5789 C CB . ILE B 362 ? 0.0659 0.0604 0.0680 -0.0062 -0.0013 0.0039 444 ILE B CB 5790 C CG1 . ILE B 362 ? 0.0611 0.0544 0.0625 -0.0063 -0.0011 0.0048 444 ILE B CG1 5791 C CG2 . ILE B 362 ? 0.1054 0.0999 0.1084 -0.0073 -0.0010 0.0034 444 ILE B CG2 5792 C CD1 . ILE B 362 ? 0.0633 0.0574 0.0650 -0.0073 -0.0004 0.0051 444 ILE B CD1 5793 N N . SER B 363 ? 0.0653 0.0607 0.0663 -0.0037 -0.0021 0.0038 445 SER B N 5794 C CA . SER B 363 ? 0.0591 0.0545 0.0593 -0.0028 -0.0021 0.0040 445 SER B CA 5795 C C . SER B 363 ? 0.0870 0.0845 0.0875 -0.0025 -0.0018 0.0038 445 SER B C 5796 O O . SER B 363 ? 0.0798 0.0790 0.0811 -0.0027 -0.0017 0.0034 445 SER B O 5797 C CB . SER B 363 ? 0.1012 0.0957 0.1012 -0.0019 -0.0025 0.0039 445 SER B CB 5798 O OG . SER B 363 ? 0.1018 0.0977 0.1023 -0.0014 -0.0026 0.0035 445 SER B OG 5799 N N . PHE B 364 ? 0.0640 0.0615 0.0638 -0.0020 -0.0015 0.0039 446 PHE B N 5800 C CA . PHE B 364 ? 0.0928 0.0921 0.0927 -0.0016 -0.0011 0.0037 446 PHE B CA 5801 C C . PHE B 364 ? 0.0907 0.0894 0.0900 -0.0005 -0.0009 0.0036 446 PHE B C 5802 O O . PHE B 364 ? 0.0965 0.0934 0.0950 -0.0004 -0.0011 0.0037 446 PHE B O 5803 C CB . PHE B 364 ? 0.0708 0.0708 0.0706 -0.0024 -0.0007 0.0039 446 PHE B CB 5804 C CG . PHE B 364 ? 0.0647 0.0652 0.0652 -0.0036 -0.0007 0.0040 446 PHE B CG 5805 C CD1 . PHE B 364 ? 0.0913 0.0898 0.0916 -0.0042 -0.0008 0.0044 446 PHE B CD1 5806 C CD2 . PHE B 364 ? 0.0932 0.0959 0.0946 -0.0040 -0.0003 0.0038 446 PHE B CD2 5807 C CE1 . PHE B 364 ? 0.1150 0.1136 0.1160 -0.0053 -0.0006 0.0044 446 PHE B CE1 5808 C CE2 . PHE B 364 ? 0.0981 0.1010 0.1001 -0.0053 -0.0002 0.0037 446 PHE B CE2 5809 C CZ . PHE B 364 ? 0.0966 0.0973 0.0985 -0.0059 -0.0003 0.0041 446 PHE B CZ 5810 N N . CYS B 365 ? 0.0846 0.0848 0.0842 0.0003 -0.0006 0.0034 447 CYS B N 5811 C CA . CYS B 365 ? 0.0735 0.0730 0.0725 0.0013 -0.0002 0.0032 447 CYS B CA 5812 C C . CYS B 365 ? 0.0719 0.0728 0.0708 0.0016 0.0004 0.0030 447 CYS B C 5813 O O . CYS B 365 ? 0.0896 0.0928 0.0894 0.0014 0.0006 0.0031 447 CYS B O 5814 C CB . CYS B 365 ? 0.1427 0.1420 0.1420 0.0025 -0.0003 0.0032 447 CYS B CB 5815 S SG . CYS B 365 ? 0.2494 0.2463 0.2483 0.0024 -0.0008 0.0033 447 CYS B SG 5816 N N . GLY B 366 ? 0.0764 0.0763 0.0746 0.0019 0.0008 0.0028 448 GLY B N 5817 C CA . GLY B 366 ? 0.0973 0.0985 0.0953 0.0021 0.0015 0.0025 448 GLY B CA 5818 C C . GLY B 366 ? 0.1048 0.1073 0.1034 0.0034 0.0020 0.0024 448 GLY B C 5819 O O . GLY B 366 ? 0.1594 0.1607 0.1580 0.0044 0.0021 0.0024 448 GLY B O 5820 N N . VAL B 367 ? 0.1026 0.1075 0.1018 0.0035 0.0024 0.0023 449 VAL B N 5821 C CA . VAL B 367 ? 0.0654 0.0718 0.0653 0.0048 0.0029 0.0023 449 VAL B CA 5822 C C . VAL B 367 ? 0.0845 0.0926 0.0844 0.0049 0.0037 0.0020 449 VAL B C 5823 O O . VAL B 367 ? 0.0790 0.0871 0.0783 0.0038 0.0037 0.0019 449 VAL B O 5824 C CB . VAL B 367 ? 0.0909 0.0997 0.0920 0.0050 0.0025 0.0026 449 VAL B CB 5825 C CG1 . VAL B 367 ? 0.0923 0.0998 0.0935 0.0050 0.0018 0.0029 449 VAL B CG1 5826 C CG2 . VAL B 367 ? 0.1017 0.1127 0.1034 0.0036 0.0023 0.0027 449 VAL B CG2 5827 N N . ASN B 368 ? 0.1137 0.1231 0.1142 0.0063 0.0043 0.0019 450 ASN B N 5828 C CA . ASN B 368 ? 0.1445 0.1557 0.1451 0.0066 0.0051 0.0016 450 ASN B CA 5829 C C . ASN B 368 ? 0.2113 0.2262 0.2133 0.0069 0.0051 0.0018 450 ASN B C 5830 O O . ASN B 368 ? 0.2172 0.2341 0.2195 0.0073 0.0057 0.0016 450 ASN B O 5831 C CB . ASN B 368 ? 0.1979 0.2076 0.1979 0.0079 0.0060 0.0011 450 ASN B CB 5832 C CG . ASN B 368 ? 0.2354 0.2424 0.2341 0.0071 0.0061 0.0005 450 ASN B CG 5833 O OD1 . ASN B 368 ? 0.2569 0.2645 0.2550 0.0060 0.0062 0.0003 450 ASN B OD1 5834 N ND2 . ASN B 368 ? 0.3004 0.3047 0.2985 0.0077 0.0062 0.0003 450 ASN B ND2 5835 N N . SER B 369 ? 0.1282 0.1441 0.1310 0.0069 0.0044 0.0022 451 SER B N 5836 C CA . SER B 369 ? 0.1470 0.1666 0.1510 0.0069 0.0043 0.0024 451 SER B CA 5837 C C . SER B 369 ? 0.1273 0.1481 0.1315 0.0049 0.0039 0.0023 451 SER B C 5838 O O . SER B 369 ? 0.1174 0.1360 0.1207 0.0037 0.0038 0.0023 451 SER B O 5839 C CB . SER B 369 ? 0.1577 0.1782 0.1625 0.0079 0.0038 0.0028 451 SER B CB 5840 O OG . SER B 369 ? 0.1357 0.1537 0.1400 0.0071 0.0031 0.0030 451 SER B OG 5841 N N . ASP B 370 ? 0.1352 0.1594 0.1406 0.0045 0.0038 0.0024 452 ASP B N 5842 C CA . ASP B 370 ? 0.1492 0.1747 0.1550 0.0026 0.0037 0.0022 452 ASP B CA 5843 C C . ASP B 370 ? 0.1266 0.1500 0.1320 0.0012 0.0030 0.0023 452 ASP B C 5844 O O . ASP B 370 ? 0.1258 0.1486 0.1314 0.0017 0.0024 0.0024 452 ASP B O 5845 C CB . ASP B 370 ? 0.1503 0.1802 0.1575 0.0024 0.0038 0.0021 452 ASP B CB 5846 C CG . ASP B 370 ? 0.2230 0.2554 0.2306 0.0034 0.0046 0.0020 452 ASP B CG 5847 O OD1 . ASP B 370 ? 0.2973 0.3278 0.3039 0.0037 0.0051 0.0019 452 ASP B OD1 5848 O OD2 . ASP B 370 ? 0.2565 0.2927 0.2653 0.0039 0.0047 0.0019 452 ASP B OD2 5849 N N . THR B 371 ? 0.0960 0.1181 0.1009 -0.0004 0.0030 0.0024 453 THR B N 5850 C CA . THR B 371 ? 0.0601 0.0802 0.0647 -0.0017 0.0025 0.0025 453 THR B CA 5851 C C . THR B 371 ? 0.0877 0.1088 0.0927 -0.0035 0.0028 0.0025 453 THR B C 5852 O O . THR B 371 ? 0.0907 0.1142 0.0962 -0.0039 0.0033 0.0024 453 THR B O 5853 C CB . THR B 371 ? 0.1254 0.1417 0.1287 -0.0016 0.0023 0.0028 453 THR B CB 5854 O OG1 . THR B 371 ? 0.1365 0.1525 0.1390 -0.0018 0.0029 0.0028 453 THR B OG1 5855 C CG2 . THR B 371 ? 0.0852 0.1000 0.0880 0.0000 0.0021 0.0027 453 THR B CG2 5856 N N . VAL B 372 ? 0.0967 0.1159 0.1016 -0.0048 0.0024 0.0026 454 VAL B N 5857 C CA . VAL B 372 ? 0.0862 0.1059 0.0915 -0.0066 0.0028 0.0026 454 VAL B CA 5858 C C . VAL B 372 ? 0.1108 0.1270 0.1154 -0.0075 0.0026 0.0031 454 VAL B C 5859 O O . VAL B 372 ? 0.0996 0.1137 0.1038 -0.0071 0.0021 0.0031 454 VAL B O 5860 C CB . VAL B 372 ? 0.0913 0.1138 0.0981 -0.0075 0.0027 0.0020 454 VAL B CB 5861 C CG1 . VAL B 372 ? 0.0920 0.1132 0.0990 -0.0075 0.0021 0.0017 454 VAL B CG1 5862 C CG2 . VAL B 372 ? 0.1175 0.1409 0.1249 -0.0094 0.0033 0.0020 454 VAL B CG2 5863 N N . GLY B 373 ? 0.1060 0.1218 0.1104 -0.0088 0.0032 0.0035 455 GLY B N 5864 C CA . GLY B 373 ? 0.1007 0.1134 0.1045 -0.0097 0.0031 0.0040 455 GLY B CA 5865 C C . GLY B 373 ? 0.1385 0.1512 0.1434 -0.0111 0.0032 0.0036 455 GLY B C 5866 O O . GLY B 373 ? 0.1595 0.1749 0.1655 -0.0118 0.0035 0.0030 455 GLY B O 5867 N N . TRP B 374 ? 0.1213 0.1311 0.1259 -0.0114 0.0030 0.0039 456 TRP B N 5868 C CA . TRP B 374 ? 0.1063 0.1155 0.1117 -0.0128 0.0032 0.0035 456 TRP B CA 5869 C C . TRP B 374 ? 0.1068 0.1123 0.1116 -0.0129 0.0032 0.0041 456 TRP B C 5870 O O . TRP B 374 ? 0.1000 0.1037 0.1037 -0.0123 0.0031 0.0050 456 TRP B O 5871 C CB . TRP B 374 ? 0.0937 0.1048 0.1000 -0.0125 0.0027 0.0024 456 TRP B CB 5872 C CG . TRP B 374 ? 0.1017 0.1141 0.1093 -0.0142 0.0031 0.0015 456 TRP B CG 5873 C CD1 . TRP B 374 ? 0.1363 0.1495 0.1444 -0.0158 0.0039 0.0015 456 TRP B CD1 5874 C CD2 . TRP B 374 ? 0.0990 0.1122 0.1074 -0.0145 0.0027 0.0006 456 TRP B CD2 5875 N NE1 . TRP B 374 ? 0.1411 0.1555 0.1504 -0.0172 0.0041 0.0004 456 TRP B NE1 5876 C CE2 . TRP B 374 ? 0.1457 0.1602 0.1551 -0.0164 0.0033 -0.0002 456 TRP B CE2 5877 C CE3 . TRP B 374 ? 0.1119 0.1250 0.1202 -0.0134 0.0019 0.0002 456 TRP B CE3 5878 C CZ2 . TRP B 374 ? 0.1533 0.1691 0.1636 -0.0173 0.0032 -0.0014 456 TRP B CZ2 5879 C CZ3 . TRP B 374 ? 0.1249 0.1393 0.1340 -0.0142 0.0018 -0.0009 456 TRP B CZ3 5880 C CH2 . TRP B 374 ? 0.1308 0.1466 0.1409 -0.0161 0.0024 -0.0017 456 TRP B CH2 5881 N N . SER B 375 ? 0.1124 0.1168 0.1179 -0.0138 0.0032 0.0036 457 SER B N 5882 C CA . SER B 375 ? 0.1042 0.1051 0.1092 -0.0137 0.0031 0.0041 457 SER B CA 5883 C C . SER B 375 ? 0.0930 0.0938 0.0986 -0.0135 0.0026 0.0031 457 SER B C 5884 O O . SER B 375 ? 0.0935 0.0957 0.1001 -0.0145 0.0028 0.0021 457 SER B O 5885 C CB . SER B 375 ? 0.1572 0.1563 0.1626 -0.0153 0.0041 0.0045 457 SER B CB 5886 O OG . SER B 375 ? 0.1017 0.0974 0.1067 -0.0150 0.0041 0.0051 457 SER B OG 5887 N N . TRP B 376 ? 0.0946 0.0939 0.0995 -0.0122 0.0019 0.0035 458 TRP B N 5888 C CA . TRP B 376 ? 0.1061 0.1050 0.1114 -0.0119 0.0014 0.0027 458 TRP B CA 5889 C C . TRP B 376 ? 0.0962 0.0917 0.1011 -0.0118 0.0014 0.0032 458 TRP B C 5890 O O . TRP B 376 ? 0.1064 0.1007 0.1106 -0.0106 0.0009 0.0037 458 TRP B O 5891 C CB . TRP B 376 ? 0.0854 0.0856 0.0902 -0.0103 0.0006 0.0026 458 TRP B CB 5892 C CG . TRP B 376 ? 0.0792 0.0829 0.0845 -0.0101 0.0005 0.0020 458 TRP B CG 5893 C CD1 . TRP B 376 ? 0.0983 0.1044 0.1045 -0.0103 0.0003 0.0010 458 TRP B CD1 5894 C CD2 . TRP B 376 ? 0.1141 0.1195 0.1192 -0.0095 0.0006 0.0024 458 TRP B CD2 5895 N NE1 . TRP B 376 ? 0.1070 0.1163 0.1136 -0.0098 0.0003 0.0009 458 TRP B NE1 5896 C CE2 . TRP B 376 ? 0.1246 0.1334 0.1304 -0.0093 0.0005 0.0017 458 TRP B CE2 5897 C CE3 . TRP B 376 ? 0.1186 0.1232 0.1228 -0.0091 0.0009 0.0032 458 TRP B CE3 5898 C CZ2 . TRP B 376 ? 0.0842 0.0953 0.0901 -0.0086 0.0007 0.0018 458 TRP B CZ2 5899 C CZ3 . TRP B 376 ? 0.0966 0.1034 0.1007 -0.0086 0.0010 0.0032 458 TRP B CZ3 5900 C CH2 . TRP B 376 ? 0.0972 0.1072 0.1023 -0.0083 0.0010 0.0025 458 TRP B CH2 5901 N N . PRO B 377 ? 0.0971 0.0910 0.1025 -0.0131 0.0021 0.0031 459 PRO B N 5902 C CA . PRO B 377 ? 0.1137 0.1042 0.1188 -0.0130 0.0024 0.0038 459 PRO B CA 5903 C C . PRO B 377 ? 0.0833 0.0729 0.0887 -0.0127 0.0019 0.0030 459 PRO B C 5904 O O . PRO B 377 ? 0.1055 0.0972 0.1114 -0.0127 0.0015 0.0019 459 PRO B O 5905 C CB . PRO B 377 ? 0.1487 0.1381 0.1545 -0.0146 0.0035 0.0038 459 PRO B CB 5906 C CG . PRO B 377 ? 0.2158 0.2082 0.2222 -0.0156 0.0038 0.0031 459 PRO B CG 5907 C CD . PRO B 377 ? 0.1059 0.1012 0.1123 -0.0147 0.0028 0.0023 459 PRO B CD 5908 N N . ASP B 378 ? 0.1142 0.1010 0.1195 -0.0124 0.0021 0.0036 460 ASP B N 5909 C CA . ASP B 378 ? 0.1213 0.1070 0.1268 -0.0120 0.0018 0.0029 460 ASP B CA 5910 C C . ASP B 378 ? 0.1408 0.1271 0.1474 -0.0135 0.0023 0.0014 460 ASP B C 5911 O O . ASP B 378 ? 0.1380 0.1261 0.1449 -0.0133 0.0018 0.0003 460 ASP B O 5912 C CB . ASP B 378 ? 0.1068 0.0892 0.1120 -0.0115 0.0021 0.0039 460 ASP B CB 5913 C CG . ASP B 378 ? 0.1884 0.1696 0.1940 -0.0113 0.0019 0.0030 460 ASP B CG 5914 O OD1 . ASP B 378 ? 0.1435 0.1256 0.1488 -0.0103 0.0011 0.0028 460 ASP B OD1 5915 O OD2 . ASP B 378 ? 0.1850 0.1644 0.1913 -0.0122 0.0028 0.0026 460 ASP B OD2 5916 N N . GLY B 379 ? 0.1207 0.1058 0.1279 -0.0148 0.0033 0.0013 461 GLY B N 5917 C CA . GLY B 379 ? 0.1564 0.1423 0.1645 -0.0165 0.0039 -0.0002 461 GLY B CA 5918 C C . GLY B 379 ? 0.1397 0.1233 0.1484 -0.0170 0.0044 -0.0011 461 GLY B C 5919 O O . GLY B 379 ? 0.1065 0.0909 0.1160 -0.0184 0.0049 -0.0026 461 GLY B O 5920 N N . ALA B 380 ? 0.1002 0.0812 0.1085 -0.0158 0.0043 -0.0002 462 ALA B N 5921 C CA . ALA B 380 ? 0.0997 0.0782 0.1084 -0.0161 0.0048 -0.0010 462 ALA B CA 5922 C C . ALA B 380 ? 0.1373 0.1128 0.1466 -0.0174 0.0063 -0.0008 462 ALA B C 5923 O O . ALA B 380 ? 0.1400 0.1145 0.1490 -0.0174 0.0068 0.0005 462 ALA B O 5924 C CB . ALA B 380 ? 0.0936 0.0704 0.1017 -0.0144 0.0042 -0.0001 462 ALA B CB 5925 N N . GLU B 381 ? 0.1477 0.1218 0.1577 -0.0185 0.0070 -0.0022 463 GLU B N 5926 C CA . GLU B 381 ? 0.1536 0.1244 0.1643 -0.0197 0.0086 -0.0022 463 GLU B CA 5927 C C . GLU B 381 ? 0.1634 0.1304 0.1741 -0.0186 0.0091 -0.0015 463 GLU B C 5928 O O . GLU B 381 ? 0.1588 0.1253 0.1697 -0.0185 0.0090 -0.0027 463 GLU B O 5929 C CB . GLU B 381 ? 0.2054 0.1771 0.2171 -0.0219 0.0094 -0.0045 463 GLU B CB 5930 C CG . GLU B 381 ? 0.3506 0.3264 0.3625 -0.0230 0.0090 -0.0053 463 GLU B CG 5931 C CD . GLU B 381 ? 0.5527 0.5280 0.5647 -0.0239 0.0099 -0.0042 463 GLU B CD 5932 O OE1 . GLU B 381 ? 0.6415 0.6129 0.6533 -0.0237 0.0108 -0.0029 463 GLU B OE1 5933 O OE2 . GLU B 381 ? 0.6870 0.6656 0.6991 -0.0247 0.0096 -0.0046 463 GLU B OE2 5934 N N . LEU B 382 ? 0.1543 0.1188 0.1645 -0.0177 0.0096 0.0006 464 LEU B N 5935 C CA . LEU B 382 ? 0.1555 0.1164 0.1656 -0.0165 0.0101 0.0016 464 LEU B CA 5936 C C . LEU B 382 ? 0.1845 0.1416 0.1954 -0.0176 0.0119 0.0017 464 LEU B C 5937 O O . LEU B 382 ? 0.1822 0.1391 0.1933 -0.0191 0.0128 0.0016 464 LEU B O 5938 C CB . LEU B 382 ? 0.1878 0.1487 0.1969 -0.0146 0.0093 0.0039 464 LEU B CB 5939 C CG . LEU B 382 ? 0.1747 0.1381 0.1832 -0.0130 0.0077 0.0040 464 LEU B CG 5940 C CD1 . LEU B 382 ? 0.1361 0.1033 0.1445 -0.0136 0.0067 0.0027 464 LEU B CD1 5941 C CD2 . LEU B 382 ? 0.1679 0.1311 0.1754 -0.0114 0.0071 0.0063 464 LEU B CD2 5942 N N . PRO B 383 ? 0.1880 0.1418 0.1992 -0.0168 0.0127 0.0019 465 PRO B N 5943 C CA . PRO B 383 ? 0.1527 0.1065 0.1637 -0.0151 0.0118 0.0019 465 PRO B CA 5944 C C . PRO B 383 ? 0.1754 0.1311 0.1868 -0.0158 0.0113 -0.0006 465 PRO B C 5945 O O . PRO B 383 ? 0.1527 0.1097 0.1646 -0.0177 0.0116 -0.0024 465 PRO B O 5946 C CB . PRO B 383 ? 0.2396 0.1889 0.2510 -0.0144 0.0132 0.0028 465 PRO B CB 5947 C CG . PRO B 383 ? 0.3141 0.2610 0.3257 -0.0154 0.0146 0.0039 465 PRO B CG 5948 C CD . PRO B 383 ? 0.2459 0.1953 0.2577 -0.0175 0.0146 0.0023 465 PRO B CD 5949 N N . PHE B 384 ? 0.1741 0.1303 0.1853 -0.0143 0.0104 -0.0006 466 PHE B N 5950 C CA . PHE B 384 ? 0.1852 0.1432 0.1967 -0.0148 0.0099 -0.0028 466 PHE B CA 5951 C C . PHE B 384 ? 0.2289 0.1837 0.2412 -0.0149 0.0111 -0.0038 466 PHE B C 5952 O O . PHE B 384 ? 0.2195 0.1706 0.2321 -0.0145 0.0123 -0.0027 466 PHE B O 5953 C CB . PHE B 384 ? 0.1691 0.1297 0.1799 -0.0131 0.0082 -0.0023 466 PHE B CB 5954 C CG . PHE B 384 ? 0.2442 0.2086 0.2544 -0.0133 0.0070 -0.0023 466 PHE B CG 5955 C CD1 . PHE B 384 ? 0.1653 0.1307 0.1755 -0.0147 0.0073 -0.0025 466 PHE B CD1 5956 C CD2 . PHE B 384 ? 0.1766 0.1436 0.1862 -0.0121 0.0056 -0.0022 466 PHE B CD2 5957 C CE1 . PHE B 384 ? 0.1723 0.1413 0.1821 -0.0148 0.0063 -0.0025 466 PHE B CE1 5958 C CE2 . PHE B 384 ? 0.1856 0.1558 0.1946 -0.0122 0.0046 -0.0021 466 PHE B CE2 5959 C CZ . PHE B 384 ? 0.1677 0.1390 0.1769 -0.0135 0.0049 -0.0023 466 PHE B CZ 5960 N N . THR B 385 ? 0.1869 0.1432 0.1995 -0.0155 0.0109 -0.0059 467 THR B N 5961 C CA . THR B 385 ? 0.2087 0.1623 0.2220 -0.0157 0.0120 -0.0073 467 THR B CA 5962 C C . THR B 385 ? 0.2585 0.2093 0.2718 -0.0136 0.0122 -0.0057 467 THR B C 5963 O O . THR B 385 ? 0.2482 0.1952 0.2622 -0.0136 0.0137 -0.0057 467 THR B O 5964 C CB . THR B 385 ? 0.2620 0.2184 0.2754 -0.0164 0.0114 -0.0096 467 THR B CB 5965 O OG1 . THR B 385 ? 0.3911 0.3505 0.4046 -0.0183 0.0112 -0.0112 467 THR B OG1 5966 C CG2 . THR B 385 ? 0.4050 0.3587 0.4192 -0.0168 0.0127 -0.0113 467 THR B CG2 5967 N N . ILE B 386 ? 0.1858 0.1385 0.1983 -0.0119 0.0108 -0.0043 468 ILE B N 5968 C CA . ILE B 386 ? 0.1992 0.1500 0.2117 -0.0098 0.0108 -0.0027 468 ILE B CA 5969 C C . ILE B 386 ? 0.2508 0.1989 0.2633 -0.0092 0.0116 -0.0004 468 ILE B C 5970 O O . ILE B 386 ? 0.2749 0.2204 0.2876 -0.0077 0.0122 0.0009 468 ILE B O 5971 C CB . ILE B 386 ? 0.1960 0.1500 0.2077 -0.0083 0.0090 -0.0018 468 ILE B CB 5972 C CG1 . ILE B 386 ? 0.1971 0.1497 0.2089 -0.0064 0.0090 -0.0008 468 ILE B CG1 5973 C CG2 . ILE B 386 ? 0.2000 0.1555 0.2108 -0.0080 0.0081 0.0000 468 ILE B CG2 5974 C CD1 . ILE B 386 ? 0.2147 0.1667 0.2271 -0.0065 0.0094 -0.0027 468 ILE B CD1 5975 N N . ASP B 387 ? 0.2744 0.2231 0.2866 -0.0103 0.0117 0.0000 469 ASP B N 5976 C CA . ASP B 387 ? 0.3583 0.3054 0.3701 -0.0098 0.0121 0.0023 469 ASP B CA 5977 C C . ASP B 387 ? 0.2959 0.2463 0.3067 -0.0090 0.0105 0.0037 469 ASP B C 5978 O O . ASP B 387 ? 0.2271 0.1777 0.2374 -0.0072 0.0099 0.0055 469 ASP B O 5979 C CB . ASP B 387 ? 0.3770 0.3205 0.3892 -0.0082 0.0132 0.0040 469 ASP B CB 5980 C CG . ASP B 387 ? 0.3908 0.3302 0.4039 -0.0092 0.0152 0.0032 469 ASP B CG 5981 O OD1 . ASP B 387 ? 0.4203 0.3598 0.4340 -0.0111 0.0158 0.0008 469 ASP B OD1 5982 O OD2 . ASP B 387 ? 0.4620 0.3981 0.4754 -0.0082 0.0164 0.0050 469 ASP B OD2 5983 C C1 . NAG C . ? 0.3256 0.2914 0.3416 -0.0032 0.0138 -0.0294 501 NAG A C1 5984 C C2 . NAG C . ? 0.3188 0.2822 0.3351 -0.0050 0.0150 -0.0311 501 NAG A C2 5985 C C3 . NAG C . ? 0.4289 0.3877 0.4465 -0.0046 0.0171 -0.0321 501 NAG A C3 5986 C C4 . NAG C . ? 0.3468 0.3062 0.3648 -0.0037 0.0179 -0.0336 501 NAG A C4 5987 C C5 . NAG C . ? 0.4352 0.3973 0.4527 -0.0019 0.0164 -0.0316 501 NAG A C5 5988 C C6 . NAG C . ? 0.4218 0.3850 0.4397 -0.0012 0.0171 -0.0331 501 NAG A C6 5989 C C7 . NAG C . ? 0.3076 0.2728 0.3229 -0.0071 0.0135 -0.0300 501 NAG A C7 5990 C C8 . NAG C . ? 0.2945 0.2586 0.3097 -0.0073 0.0129 -0.0281 501 NAG A C8 5991 N N2 . NAG C . ? 0.3076 0.2702 0.3237 -0.0054 0.0144 -0.0294 501 NAG A N2 5992 O O3 . NAG C . ? 0.4275 0.3845 0.4453 -0.0066 0.0183 -0.0343 501 NAG A O3 5993 O O4 . NAG C . ? 0.4085 0.3632 0.4277 -0.0029 0.0198 -0.0340 501 NAG A O4 5994 O O5 . NAG C . ? 0.3274 0.2937 0.3438 -0.0026 0.0146 -0.0309 501 NAG A O5 5995 O O6 . NAG C . ? 0.4117 0.3769 0.4290 -0.0031 0.0175 -0.0360 501 NAG A O6 5996 O O7 . NAG C . ? 0.3530 0.3215 0.3677 -0.0083 0.0132 -0.0318 501 NAG A O7 5997 C C1 . NAG D . ? 0.4617 0.4161 0.4812 -0.0041 0.0213 -0.0373 502 NAG A C1 5998 C C2 . NAG D . ? 0.4676 0.4176 0.4884 -0.0025 0.0233 -0.0376 502 NAG A C2 5999 C C3 . NAG D . ? 0.5268 0.4763 0.5480 -0.0037 0.0250 -0.0412 502 NAG A C3 6000 C C4 . NAG D . ? 0.4798 0.4300 0.5004 -0.0067 0.0253 -0.0438 502 NAG A C4 6001 C C5 . NAG D . ? 0.4591 0.4138 0.4784 -0.0079 0.0231 -0.0428 502 NAG A C5 6002 C C6 . NAG D . ? 0.4786 0.4337 0.4976 -0.0107 0.0236 -0.0452 502 NAG A C6 6003 C C7 . NAG D . ? 0.5618 0.5104 0.5835 0.0019 0.0225 -0.0326 502 NAG A C7 6004 C C8 . NAG D . ? 0.5257 0.4761 0.5477 0.0043 0.0217 -0.0308 502 NAG A C8 6005 N N2 . NAG D . ? 0.5233 0.4743 0.5443 0.0000 0.0226 -0.0355 502 NAG A N2 6006 O O3 . NAG D . ? 0.4964 0.4408 0.5189 -0.0025 0.0271 -0.0414 502 NAG A O3 6007 O O4 . NAG D . ? 0.4526 0.4045 0.4731 -0.0079 0.0262 -0.0471 502 NAG A O4 6008 O O5 . NAG D . ? 0.4656 0.4194 0.4849 -0.0065 0.0220 -0.0395 502 NAG A O5 6009 O O6 . NAG D . ? 0.5238 0.4738 0.5438 -0.0111 0.0251 -0.0450 502 NAG A O6 6010 O O7 . NAG D . ? 0.5820 0.5273 0.6041 0.0018 0.0231 -0.0316 502 NAG A O7 6011 C C1 . MAN E . ? 0.4260 0.3731 0.4476 -0.0085 0.0287 -0.0493 503 MAN A C1 6012 C C2 . MAN E . ? 0.4018 0.3514 0.4230 -0.0108 0.0295 -0.0533 503 MAN A C2 6013 C C3 . MAN E . ? 0.3610 0.3057 0.3832 -0.0116 0.0323 -0.0561 503 MAN A C3 6014 C C4 . MAN E . ? 0.4462 0.3865 0.4697 -0.0088 0.0337 -0.0548 503 MAN A C4 6015 C C5 . MAN E . ? 0.4262 0.3648 0.4500 -0.0066 0.0326 -0.0505 503 MAN A C5 6016 C C6 . MAN E . ? 0.4410 0.3758 0.4661 -0.0037 0.0339 -0.0490 503 MAN A C6 6017 O O2 . MAN E . ? 0.3465 0.3003 0.3670 -0.0099 0.0286 -0.0537 503 MAN A O2 6018 O O3 . MAN E . ? 0.3213 0.2692 0.3431 -0.0132 0.0327 -0.0597 503 MAN A O3 6019 O O4 . MAN E . ? 0.3857 0.3206 0.4104 -0.0096 0.0364 -0.0569 503 MAN A O4 6020 O O5 . MAN E . ? 0.3247 0.2685 0.3474 -0.0061 0.0300 -0.0485 503 MAN A O5 6021 O O6 . MAN E . ? 0.4946 0.4273 0.5200 -0.0020 0.0333 -0.0453 503 MAN A O6 6022 C C1 . MAN F . ? 0.3102 0.2558 0.3323 -0.0159 0.0346 -0.0629 504 MAN A C1 6023 C C2 . MAN F . ? 0.3381 0.2854 0.3601 -0.0170 0.0358 -0.0668 504 MAN A C2 6024 C C3 . MAN F . ? 0.3255 0.2802 0.3460 -0.0177 0.0336 -0.0672 504 MAN A C3 6025 C C4 . MAN F . ? 0.3455 0.3034 0.3651 -0.0200 0.0322 -0.0673 504 MAN A C4 6026 C C5 . MAN F . ? 0.2949 0.2503 0.3148 -0.0189 0.0313 -0.0636 504 MAN A C5 6027 C C6 . MAN F . ? 0.2879 0.2462 0.3070 -0.0211 0.0301 -0.0637 504 MAN A C6 6028 O O2 . MAN F . ? 0.2924 0.2375 0.3147 -0.0197 0.0377 -0.0702 504 MAN A O2 6029 O O3 . MAN F . ? 0.3029 0.2597 0.3231 -0.0187 0.0346 -0.0708 504 MAN A O3 6030 O O4 . MAN F . ? 0.3019 0.2667 0.3201 -0.0204 0.0302 -0.0673 504 MAN A O4 6031 O O5 . MAN F . ? 0.3324 0.2809 0.3536 -0.0182 0.0334 -0.0632 504 MAN A O5 6032 O O6 . MAN F . ? 0.2551 0.2108 0.2749 -0.0237 0.0320 -0.0666 504 MAN A O6 6033 C C1 . NAG G . ? 0.4349 0.4036 0.4315 -0.0166 0.0120 0.0008 505 NAG A C1 6034 C C2 . NAG G . ? 0.5349 0.5021 0.5317 -0.0190 0.0135 -0.0004 505 NAG A C2 6035 C C3 . NAG G . ? 0.6045 0.5673 0.6007 -0.0192 0.0151 -0.0004 505 NAG A C3 6036 C C4 . NAG G . ? 0.6227 0.5829 0.6182 -0.0172 0.0157 0.0016 505 NAG A C4 6037 C C5 . NAG G . ? 0.5830 0.5454 0.5784 -0.0150 0.0139 0.0025 505 NAG A C5 6038 C C6 . NAG G . ? 0.5658 0.5261 0.5606 -0.0130 0.0144 0.0044 505 NAG A C6 6039 C C7 . NAG G . ? 0.5718 0.5437 0.5699 -0.0223 0.0130 -0.0032 505 NAG A C7 6040 C C8 . NAG G . ? 0.5353 0.5106 0.5340 -0.0236 0.0120 -0.0050 505 NAG A C8 6041 N N2 . NAG G . ? 0.5364 0.5065 0.5338 -0.0204 0.0126 -0.0022 505 NAG A N2 6042 O O3 . NAG G . ? 0.7262 0.6873 0.7224 -0.0213 0.0168 -0.0012 505 NAG A O3 6043 O O4 . NAG G . ? 0.5814 0.5375 0.5763 -0.0171 0.0171 0.0016 505 NAG A O4 6044 O O5 . NAG G . ? 0.5114 0.4775 0.5074 -0.0151 0.0127 0.0025 505 NAG A O5 6045 O O6 . NAG G . ? 0.5441 0.5038 0.5387 -0.0131 0.0154 0.0056 505 NAG A O6 6046 O O7 . NAG G . ? 0.5830 0.5541 0.5811 -0.0231 0.0141 -0.0027 505 NAG A O7 6047 CA CA . CA H . ? 0.1099 0.1294 0.1308 0.0139 -0.0011 -0.0019 601 CA A CA 6048 CA CA . CA I . ? 0.1818 0.2439 0.2020 0.0005 -0.0104 0.0016 602 CA A CA 6049 CA CA . CA J . ? 0.2748 0.2633 0.2835 0.0000 0.0008 0.0000 603 CA A CA 6050 C C . ACT K . ? 0.5220 0.5280 0.5347 0.0081 0.0005 -0.0080 1 ACT A C 6051 O O . ACT K . ? 0.5608 0.5686 0.5740 0.0084 0.0010 -0.0087 1 ACT A O 6052 O OXT . ACT K . ? 0.5065 0.5106 0.5189 0.0079 0.0006 -0.0085 1 ACT A OXT 6053 C CH3 . ACT K . ? 0.4288 0.4353 0.4416 0.0078 -0.0003 -0.0066 1 ACT A CH3 6054 C C . ACT L . ? 0.3343 0.3581 0.3407 -0.0116 -0.0068 -0.0040 471 ACT A C 6055 O O . ACT L . ? 0.4458 0.4714 0.4522 -0.0107 -0.0076 -0.0035 471 ACT A O 6056 O OXT . ACT L . ? 0.4505 0.4760 0.4571 -0.0134 -0.0064 -0.0051 471 ACT A OXT 6057 C CH3 . ACT L . ? 0.2242 0.2442 0.2305 -0.0105 -0.0065 -0.0033 471 ACT A CH3 6058 C C . ACT M . ? 0.5229 0.5779 0.5479 0.0020 0.0007 -0.0045 472 ACT A C 6059 O O . ACT M . ? 0.4760 0.5295 0.5012 0.0038 0.0008 -0.0046 472 ACT A O 6060 O OXT . ACT M . ? 0.5887 0.6424 0.6133 0.0015 0.0000 -0.0041 472 ACT A OXT 6061 C CH3 . ACT M . ? 0.5258 0.5839 0.5512 0.0004 0.0014 -0.0050 472 ACT A CH3 6062 C C1 . NAG N . ? 0.7768 0.7251 0.7880 0.0061 0.0088 0.0141 501 NAG B C1 6063 C C2 . NAG N . ? 0.8295 0.7736 0.8418 0.0065 0.0106 0.0139 501 NAG B C2 6064 C C3 . NAG N . ? 0.8998 0.8423 0.9124 0.0085 0.0114 0.0166 501 NAG B C3 6065 C C4 . NAG N . ? 0.9393 0.8851 0.9515 0.0103 0.0101 0.0180 501 NAG B C4 6066 C C5 . NAG N . ? 0.9550 0.9047 0.9660 0.0096 0.0083 0.0178 501 NAG B C5 6067 C C6 . NAG N . ? 0.9802 0.9334 0.9910 0.0112 0.0070 0.0189 501 NAG B C6 6068 C C7 . NAG N . ? 0.8735 0.8138 0.8866 0.0033 0.0125 0.0104 501 NAG B C7 6069 C C8 . NAG N . ? 0.7531 0.6912 0.7665 0.0012 0.0137 0.0094 501 NAG B C8 6070 N N2 . NAG N . ? 0.8376 0.7792 0.8501 0.0046 0.0118 0.0128 501 NAG B N2 6071 O O3 . NAG N . ? 0.9704 0.9090 0.9840 0.0091 0.0131 0.0163 501 NAG B O3 6072 O O4 . NAG N . ? 0.9519 0.8967 0.9642 0.0122 0.0107 0.0207 501 NAG B O4 6073 O O5 . NAG N . ? 0.8337 0.7844 0.8447 0.0078 0.0078 0.0153 501 NAG B O5 6074 O O6 . NAG N . ? 0.9698 0.9231 0.9813 0.0119 0.0069 0.0178 501 NAG B O6 6075 O O7 . NAG N . ? 0.9357 0.8767 0.9493 0.0036 0.0122 0.0090 501 NAG B O7 6076 C C1 . NAG O . ? 0.6883 0.6509 0.6788 0.0045 0.0145 -0.0080 502 NAG B C1 6077 C C2 . NAG O . ? 0.8197 0.7789 0.8105 0.0052 0.0157 -0.0076 502 NAG B C2 6078 C C3 . NAG O . ? 0.8786 0.8345 0.8692 0.0056 0.0178 -0.0088 502 NAG B C3 6079 C C4 . NAG O . ? 0.9340 0.8910 0.9247 0.0067 0.0184 -0.0091 502 NAG B C4 6080 C C5 . NAG O . ? 0.8965 0.8572 0.8868 0.0057 0.0170 -0.0096 502 NAG B C5 6081 C C6 . NAG O . ? 1.0309 0.9930 1.0215 0.0068 0.0175 -0.0098 502 NAG B C6 6082 C C7 . NAG O . ? 0.8843 0.8412 0.8752 0.0042 0.0152 -0.0067 502 NAG B C7 6083 C C8 . NAG O . ? 0.9354 0.8922 0.9261 0.0025 0.0146 -0.0072 502 NAG B C8 6084 N N2 . NAG O . ? 0.8406 0.7992 0.8311 0.0037 0.0151 -0.0078 502 NAG B N2 6085 O O3 . NAG O . ? 0.8824 0.8352 0.8734 0.0068 0.0190 -0.0078 502 NAG B O3 6086 O O4 . NAG O . ? 0.9966 0.9507 0.9870 0.0066 0.0204 -0.0107 502 NAG B O4 6087 O O5 . NAG O . ? 0.8921 0.8553 0.8828 0.0057 0.0151 -0.0081 502 NAG B O5 6088 O O6 . NAG O . ? 0.9943 0.9567 0.9858 0.0090 0.0176 -0.0080 502 NAG B O6 6089 O O7 . NAG O . ? 0.8815 0.8372 0.8730 0.0060 0.0159 -0.0054 502 NAG B O7 6090 CA CA . CA P . ? 0.1074 0.1094 0.0938 -0.0010 -0.0026 0.0227 601 CA B CA 6091 CA CA . CA Q . ? 0.1777 0.1962 0.1604 -0.0074 0.0055 0.0064 602 CA B CA 6092 C C . ACT R . ? 0.3601 0.3656 0.3528 0.0010 0.0059 -0.0008 1 ACT B C 6093 O O . ACT R . ? 0.4639 0.4696 0.4560 0.0013 0.0067 -0.0018 1 ACT B O 6094 O OXT . ACT R . ? 0.4265 0.4338 0.4201 0.0009 0.0058 -0.0002 1 ACT B OXT 6095 C CH3 . ACT R . ? 0.3080 0.3113 0.3006 0.0009 0.0051 -0.0006 1 ACT B CH3 6096 O O . HOH S . ? 0.0812 0.1040 0.0775 0.0011 -0.0011 -0.0073 6 HOH A O 6097 O O . HOH S . ? 0.0737 0.0829 0.0851 0.0043 -0.0035 -0.0012 7 HOH A O 6098 O O . HOH S . ? 0.1283 0.1074 0.1257 -0.0087 0.0042 0.0027 8 HOH A O 6099 O O . HOH S . ? 0.0826 0.0907 0.0908 -0.0014 -0.0043 0.0000 9 HOH A O 6100 O O . HOH S . ? 0.0523 0.0816 0.0704 0.0064 -0.0055 0.0012 10 HOH A O 6101 O O . HOH S . ? 0.1460 0.1359 0.1455 -0.0041 -0.0002 0.0034 17 HOH A O 6102 O O . HOH S . ? 0.1232 0.1274 0.1256 0.0016 -0.0092 0.0062 23 HOH A O 6103 O O . HOH S . ? 0.0829 0.0816 0.0841 0.0010 -0.0086 0.0057 26 HOH A O 6104 O O . HOH S . ? 0.0974 0.1080 0.1138 0.0122 -0.0048 0.0035 27 HOH A O 6105 O O . HOH S . ? 0.1711 0.2120 0.1839 -0.0033 0.0058 -0.0044 28 HOH A O 6106 O O . HOH S . ? 0.1197 0.1042 0.1181 -0.0083 -0.0004 -0.0006 31 HOH A O 6107 O O . HOH S . ? 0.1015 0.0937 0.1022 -0.0160 0.0089 0.0032 32 HOH A O 6108 O O . HOH S . ? 0.1461 0.1286 0.1526 0.0045 -0.0046 0.0030 34 HOH A O 6109 O O . HOH S . ? 0.1078 0.1102 0.1028 0.0039 -0.0022 0.0064 35 HOH A O 6110 O O . HOH S . ? 0.1122 0.1076 0.1157 0.0006 -0.0043 0.0009 38 HOH A O 6111 O O . HOH S . ? 0.1068 0.1189 0.1142 0.0024 -0.0006 -0.0038 40 HOH A O 6112 O O . HOH S . ? 0.0745 0.0957 0.0925 0.0090 -0.0027 -0.0012 41 HOH A O 6113 O O . HOH S . ? 0.1247 0.1481 0.1274 0.0024 0.0025 -0.0125 42 HOH A O 6114 O O . HOH S . ? 0.1296 0.1061 0.1378 0.0044 -0.0022 0.0016 43 HOH A O 6115 O O . HOH S . ? 0.0831 0.0911 0.0949 0.0059 -0.0057 0.0019 45 HOH A O 6116 O O . HOH S . ? 0.1043 0.1523 0.1282 0.0082 -0.0057 0.0014 51 HOH A O 6117 O O . HOH S . ? 0.1225 0.1403 0.1195 0.0014 -0.0019 -0.0056 52 HOH A O 6118 O O . HOH S . ? 0.1402 0.1445 0.1502 0.0060 -0.0006 -0.0072 53 HOH A O 6119 O O . HOH S . ? 0.0776 0.1003 0.0929 0.0047 -0.0059 0.0013 54 HOH A O 6120 O O . HOH S . ? 0.1086 0.1392 0.1185 -0.0011 0.0037 -0.0040 57 HOH A O 6121 O O . HOH S . ? 0.1962 0.2597 0.2127 -0.0015 -0.0122 0.0019 59 HOH A O 6122 O O . HOH S . ? 0.1236 0.1553 0.1471 0.0204 -0.0061 0.0094 62 HOH A O 6123 O O . HOH S . ? 0.1167 0.1248 0.1307 0.0089 -0.0051 0.0022 63 HOH A O 6124 O O . HOH S . ? 0.1599 0.1603 0.1784 0.0156 -0.0005 -0.0007 66 HOH A O 6125 O O . HOH S . ? 0.0882 0.1001 0.0897 0.0001 -0.0011 -0.0135 68 HOH A O 6126 O O . HOH S . ? 0.1275 0.1170 0.1211 0.0003 0.0043 0.0119 69 HOH A O 6127 O O . HOH S . ? 0.1799 0.1691 0.1798 -0.0018 -0.0027 0.0027 70 HOH A O 6128 O O . HOH S . ? 0.1511 0.1690 0.1470 0.0017 -0.0028 -0.0036 71 HOH A O 6129 O O . HOH S . ? 0.2243 0.2021 0.2410 0.0133 0.0033 -0.0032 75 HOH A O 6130 O O . HOH S . ? 0.1234 0.1398 0.1379 0.0067 -0.0058 0.0020 76 HOH A O 6131 O O . HOH S . ? 0.1057 0.1077 0.1182 0.0085 -0.0045 0.0014 77 HOH A O 6132 O O . HOH S . ? 0.1391 0.1484 0.1355 0.0024 -0.0024 0.0010 81 HOH A O 6133 O O . HOH S . ? 0.3176 0.3237 0.3257 0.0044 -0.0011 -0.0061 307 HOH A O 6134 O O . HOH S . ? 0.3876 0.4531 0.4086 -0.0112 -0.0068 -0.0052 337 HOH A O 6135 O O . HOH S . ? 0.4411 0.4317 0.4547 0.0086 0.0027 -0.0113 434 HOH A O 6136 O O . HOH S . ? 0.3939 0.4111 0.4093 0.0102 0.0051 -0.0148 473 HOH A O 6137 O O . HOH S . ? 0.4322 0.3981 0.4492 0.0023 0.0131 -0.0250 474 HOH A O 6138 O O . HOH S . ? 0.5613 0.5288 0.5569 -0.0155 0.0156 0.0070 475 HOH A O 6139 O O . HOH S . ? 0.1312 0.1505 0.1538 0.0169 -0.0012 -0.0001 476 HOH A O 6140 O O . HOH S . ? 0.4519 0.4203 0.4472 -0.0086 0.0070 0.0019 477 HOH A O 6141 O O . HOH S . ? 0.1143 0.1237 0.1209 0.0013 -0.0013 -0.0022 478 HOH A O 6142 O O . HOH S . ? 0.1553 0.1978 0.1736 -0.0060 -0.0034 -0.0030 479 HOH A O 6143 O O . HOH S . ? 0.4927 0.4980 0.5056 0.0080 0.0048 -0.0173 480 HOH A O 6144 O O . HOH S . ? 0.1860 0.2022 0.1813 -0.0067 -0.0096 0.0008 481 HOH A O 6145 O O . HOH S . ? 0.1252 0.1069 0.1367 0.0111 -0.0025 0.0062 482 HOH A O 6146 O O . HOH S . ? 0.3928 0.3683 0.4032 -0.0104 0.0037 -0.0140 483 HOH A O 6147 O O . HOH S . ? 0.1812 0.1628 0.1769 -0.0039 0.0050 0.0084 484 HOH A O 6148 O O . HOH S . ? 0.1641 0.1792 0.1682 0.0016 0.0024 -0.0187 485 HOH A O 6149 O O . HOH S . ? 0.3981 0.3703 0.3957 -0.0190 0.0133 0.0016 486 HOH A O 6150 O O . HOH S . ? 0.1530 0.1483 0.1472 0.0010 0.0024 0.0102 487 HOH A O 6151 O O . HOH S . ? 0.1698 0.1591 0.1684 -0.0008 -0.0018 0.0041 488 HOH A O 6152 O O . HOH S . ? 0.2280 0.2197 0.2231 0.0012 0.0012 0.0089 489 HOH A O 6153 O O . HOH S . ? 0.1622 0.1347 0.1739 -0.0011 0.0045 -0.0140 490 HOH A O 6154 O O . HOH S . ? 0.1524 0.1470 0.1467 0.0053 -0.0011 0.0098 491 HOH A O 6155 O O . HOH S . ? 0.1408 0.1777 0.1558 -0.0123 0.0031 -0.0034 492 HOH A O 6156 O O . HOH S . ? 0.3801 0.4395 0.4017 0.0017 -0.0091 0.0013 493 HOH A O 6157 O O . HOH S . ? 0.4742 0.4358 0.4660 -0.0055 0.0164 0.0157 494 HOH A O 6158 O O . HOH S . ? 0.5406 0.6178 0.5645 -0.0095 -0.0079 -0.0047 495 HOH A O 6159 O O . HOH S . ? 0.4710 0.4686 0.4746 -0.0216 0.0072 -0.0031 496 HOH A O 6160 O O . HOH S . ? 0.4598 0.4422 0.4527 0.0068 0.0032 0.0142 497 HOH A O 6161 O O . HOH S . ? 0.1867 0.1733 0.1867 0.0012 -0.0056 0.0024 498 HOH A O 6162 O O . HOH S . ? 0.1597 0.1796 0.1679 0.0093 -0.0107 0.0122 499 HOH A O 6163 O O . HOH S . ? 0.2732 0.2637 0.2803 0.0119 -0.0059 0.0153 500 HOH A O 6164 O O . HOH S . ? 0.4614 0.4232 0.4555 -0.0126 0.0168 0.0095 506 HOH A O 6165 O O . HOH S . ? 0.5055 0.5187 0.4961 -0.0019 0.0085 0.0144 507 HOH A O 6166 O O . HOH S . ? 0.1881 0.2255 0.2082 0.0071 -0.0064 0.0020 508 HOH A O 6167 O O . HOH S . ? 0.5390 0.5383 0.5565 0.0134 0.0018 -0.0066 509 HOH A O 6168 O O . HOH S . ? 0.1348 0.1782 0.1476 -0.0187 -0.0048 -0.0082 510 HOH A O 6169 O O . HOH S . ? 0.3538 0.3474 0.3542 -0.0177 0.0117 0.0050 511 HOH A O 6170 O O . HOH S . ? 0.1996 0.1816 0.2075 0.0018 -0.0018 -0.0053 512 HOH A O 6171 O O . HOH S . ? 0.2199 0.2249 0.2338 0.0195 -0.0062 0.0169 513 HOH A O 6172 O O . HOH S . ? 0.1859 0.2245 0.2075 0.0113 0.0058 -0.0114 514 HOH A O 6173 O O . HOH S . ? 0.1542 0.1337 0.1523 -0.0121 0.0052 0.0006 515 HOH A O 6174 O O . HOH S . ? 0.1342 0.1187 0.1375 -0.0001 -0.0049 0.0000 516 HOH A O 6175 O O . HOH S . ? 0.4153 0.4459 0.4259 0.0060 0.0059 -0.0150 517 HOH A O 6176 O O . HOH S . ? 0.1985 0.1968 0.1960 -0.0087 -0.0056 -0.0025 518 HOH A O 6177 O O . HOH S . ? 0.1113 0.1111 0.1158 -0.0006 -0.0033 0.0006 519 HOH A O 6178 O O . HOH S . ? 0.3794 0.3750 0.3920 0.0067 0.0044 -0.0170 520 HOH A O 6179 O O . HOH S . ? 0.1772 0.1652 0.1754 -0.0022 -0.0003 0.0046 521 HOH A O 6180 O O . HOH S . ? 0.4599 0.4566 0.4826 0.0270 0.0003 0.0122 522 HOH A O 6181 O O . HOH S . ? 0.4969 0.4401 0.5149 0.0007 0.0153 -0.0120 523 HOH A O 6182 O O . HOH S . ? 0.4165 0.4422 0.4235 0.0045 0.0060 -0.0205 524 HOH A O 6183 O O . HOH S . ? 0.4944 0.4539 0.5124 0.0152 0.0076 0.0029 525 HOH A O 6184 O O . HOH S . ? 0.2449 0.2332 0.2559 0.0054 0.0011 -0.0107 526 HOH A O 6185 O O . HOH S . ? 0.3456 0.3551 0.3375 0.0093 -0.0019 0.0129 527 HOH A O 6186 O O . HOH S . ? 0.4871 0.4752 0.4917 0.0019 -0.0045 -0.0020 528 HOH A O 6187 O O . HOH S . ? 0.2627 0.2516 0.2574 0.0051 -0.0005 0.0099 529 HOH A O 6188 O O . HOH S . ? 0.1588 0.1465 0.1579 -0.0030 -0.0048 0.0014 530 HOH A O 6189 O O . HOH S . ? 0.4810 0.4497 0.4756 -0.0026 0.0053 0.0052 531 HOH A O 6190 O O . HOH S . ? 0.2557 0.2734 0.2578 -0.0047 -0.0097 0.0014 532 HOH A O 6191 O O . HOH S . ? 0.4024 0.4254 0.4012 -0.0040 0.0061 0.0036 533 HOH A O 6192 O O . HOH S . ? 0.4722 0.4968 0.4907 0.0184 -0.0078 0.0123 534 HOH A O 6193 O O . HOH S . ? 0.5533 0.5376 0.5482 0.0047 0.0002 0.0097 535 HOH A O 6194 O O . HOH S . ? 0.2467 0.2641 0.2343 0.0082 0.0015 0.0165 536 HOH A O 6195 O O . HOH S . ? 0.2664 0.2852 0.2710 0.0014 0.0046 -0.0236 537 HOH A O 6196 O O . HOH S . ? 0.4178 0.4671 0.4376 -0.0055 0.0034 -0.0046 538 HOH A O 6197 O O . HOH S . ? 0.3718 0.3936 0.3778 -0.0002 -0.0104 0.0042 539 HOH A O 6198 O O . HOH S . ? 0.1790 0.2074 0.1699 0.0015 0.0031 0.0048 540 HOH A O 6199 O O . HOH S . ? 0.2217 0.2571 0.2350 -0.0006 0.0037 -0.0048 541 HOH A O 6200 O O . HOH S . ? 0.1716 0.1582 0.1753 0.0023 -0.0058 0.0020 542 HOH A O 6201 O O . HOH S . ? 0.4230 0.4712 0.4427 -0.0087 -0.0023 -0.0042 543 HOH A O 6202 O O . HOH S . ? 0.2089 0.2052 0.2084 0.0022 -0.0054 0.0011 544 HOH A O 6203 O O . HOH S . ? 0.6089 0.6029 0.5991 -0.0038 0.0128 0.0195 545 HOH A O 6204 O O . HOH S . ? 0.4840 0.4907 0.5102 0.0310 0.0002 0.0133 546 HOH A O 6205 O O . HOH S . ? 0.2221 0.2268 0.2231 -0.0009 -0.0051 -0.0060 547 HOH A O 6206 O O . HOH S . ? 0.4777 0.5006 0.4887 -0.0121 -0.0002 -0.0030 548 HOH A O 6207 O O . HOH S . ? 0.2098 0.2155 0.2058 0.0034 -0.0033 0.0032 549 HOH A O 6208 O O . HOH S . ? 0.2042 0.1797 0.2200 0.0129 0.0025 -0.0005 550 HOH A O 6209 O O . HOH S . ? 0.1406 0.1242 0.1386 -0.0030 -0.0009 0.0034 551 HOH A O 6210 O O . HOH S . ? 0.4080 0.4035 0.4167 -0.0001 0.0040 -0.0223 552 HOH A O 6211 O O . HOH S . ? 0.3583 0.3421 0.3541 -0.0081 0.0090 0.0097 553 HOH A O 6212 O O . HOH S . ? 0.2179 0.2006 0.2215 0.0008 -0.0050 0.0014 554 HOH A O 6213 O O . HOH S . ? 0.2564 0.2148 0.2695 -0.0021 0.0074 -0.0080 555 HOH A O 6214 O O . HOH S . ? 0.3872 0.4239 0.3993 0.0016 0.0049 -0.0071 556 HOH A O 6215 O O . HOH S . ? 0.2222 0.2067 0.2369 0.0102 0.0020 -0.0068 557 HOH A O 6216 O O . HOH S . ? 0.4257 0.4830 0.4397 0.0069 -0.0137 0.0093 558 HOH A O 6217 O O . HOH S . ? 0.4495 0.4688 0.4623 0.0179 -0.0092 0.0177 559 HOH A O 6218 O O . HOH S . ? 0.5674 0.5328 0.5779 0.0085 0.0017 0.0093 560 HOH A O 6219 O O . HOH S . ? 0.2641 0.2593 0.2537 0.0023 0.0080 0.0189 561 HOH A O 6220 O O . HOH S . ? 0.1940 0.1805 0.1926 -0.0025 -0.0012 0.0036 562 HOH A O 6221 O O . HOH S . ? 0.4146 0.4481 0.4247 0.0045 0.0055 -0.0119 563 HOH A O 6222 O O . HOH S . ? 0.2411 0.2017 0.2562 0.0121 0.0054 0.0051 564 HOH A O 6223 O O . HOH S . ? 0.2662 0.3323 0.2847 -0.0023 -0.0114 0.0008 565 HOH A O 6224 O O . HOH S . ? 0.5458 0.5146 0.5407 -0.0063 0.0052 0.0014 566 HOH A O 6225 O O . HOH S . ? 0.4199 0.4248 0.4249 -0.0211 0.0089 -0.0007 567 HOH A O 6226 O O . HOH S . ? 0.4703 0.4818 0.4767 -0.0225 0.0104 -0.0002 568 HOH A O 6227 O O . HOH S . ? 0.2463 0.2196 0.2433 -0.0135 0.0078 0.0002 569 HOH A O 6228 O O . HOH S . ? 0.4059 0.3845 0.4019 0.0021 -0.0008 0.0054 570 HOH A O 6229 O O . HOH S . ? 0.1557 0.1403 0.1707 0.0131 -0.0003 0.0012 571 HOH A O 6230 O O . HOH S . ? 0.2387 0.2862 0.2593 -0.0047 -0.0021 -0.0034 572 HOH A O 6231 O O . HOH S . ? 0.1624 0.1499 0.1780 0.0123 0.0010 -0.0038 573 HOH A O 6232 O O . HOH S . ? 0.5080 0.5759 0.5219 0.0046 -0.0148 0.0082 574 HOH A O 6233 O O . HOH S . ? 0.5243 0.5055 0.5195 -0.0124 0.0013 -0.0058 575 HOH A O 6234 O O . HOH S . ? 0.2200 0.2346 0.2152 -0.0057 0.0088 0.0098 576 HOH A O 6235 O O . HOH S . ? 0.2335 0.2100 0.2456 -0.0122 0.0084 -0.0274 577 HOH A O 6236 O O . HOH S . ? 0.2236 0.2393 0.2503 0.0232 0.0024 -0.0013 578 HOH A O 6237 O O . HOH S . ? 0.2357 0.2638 0.2320 -0.0001 0.0038 -0.0004 579 HOH A O 6238 O O . HOH S . ? 0.2271 0.2392 0.2508 0.0275 -0.0027 0.0139 580 HOH A O 6239 O O . HOH S . ? 0.5573 0.5690 0.5529 0.0040 -0.0045 0.0026 581 HOH A O 6240 O O . HOH S . ? 0.5107 0.5287 0.5053 -0.0023 0.0057 0.0073 582 HOH A O 6241 O O . HOH S . ? 0.2821 0.3054 0.2833 -0.0029 -0.0111 0.0038 583 HOH A O 6242 O O . HOH S . ? 0.5171 0.5066 0.5138 0.0035 -0.0028 0.0062 584 HOH A O 6243 O O . HOH S . ? 0.4918 0.5719 0.5195 -0.0022 -0.0077 -0.0020 585 HOH A O 6244 O O . HOH S . ? 0.2647 0.3182 0.2978 0.0226 -0.0020 0.0028 586 HOH A O 6245 O O . HOH S . ? 0.3982 0.3745 0.3932 -0.0135 0.0038 -0.0061 587 HOH A O 6246 O O . HOH S . ? 0.5104 0.4675 0.5049 -0.0165 0.0195 0.0073 588 HOH A O 6247 O O . HOH S . ? 0.3661 0.4516 0.3982 0.0049 -0.0072 0.0001 589 HOH A O 6248 O O . HOH S . ? 0.2403 0.2753 0.2379 0.0011 0.0037 -0.0106 590 HOH A O 6249 O O . HOH S . ? 0.2697 0.3352 0.2889 0.0097 -0.0131 0.0094 591 HOH A O 6250 O O . HOH S . ? 0.4023 0.4062 0.4050 -0.0021 -0.0028 -0.0125 592 HOH A O 6251 O O . HOH S . ? 0.5361 0.4708 0.5615 -0.0087 0.0390 -0.0615 593 HOH A O 6252 O O . HOH S . ? 0.2789 0.2543 0.2937 0.0050 0.0074 -0.0176 594 HOH A O 6253 O O . HOH S . ? 0.4987 0.4895 0.5004 -0.0217 0.0068 -0.0050 595 HOH A O 6254 O O . HOH S . ? 0.2022 0.2120 0.2108 0.0039 -0.0009 -0.0051 596 HOH A O 6255 O O . HOH S . ? 0.4876 0.4882 0.4837 -0.0123 0.0135 0.0122 597 HOH A O 6256 O O . HOH S . ? 0.5041 0.5003 0.5246 0.0299 -0.0008 0.0210 598 HOH A O 6257 O O . HOH S . ? 0.5326 0.5202 0.5219 0.0023 0.0099 0.0208 599 HOH A O 6258 O O . HOH S . ? 0.2652 0.2520 0.2750 0.0036 0.0006 -0.0107 600 HOH A O 6259 O O . HOH S . ? 0.5483 0.5163 0.5703 0.0226 0.0078 0.0041 604 HOH A O 6260 O O . HOH S . ? 0.4783 0.4972 0.4667 0.0013 0.0066 0.0147 605 HOH A O 6261 O O . HOH S . ? 0.3191 0.3574 0.3510 0.0320 -0.0026 0.0120 606 HOH A O 6262 O O . HOH S . ? 0.2141 0.2575 0.2263 -0.0146 -0.0068 -0.0061 607 HOH A O 6263 O O . HOH S . ? 0.5461 0.4891 0.5643 -0.0046 0.0172 -0.0187 608 HOH A O 6264 O O . HOH S . ? 0.5245 0.5027 0.5168 -0.0035 0.0110 0.0155 609 HOH A O 6265 O O . HOH S . ? 0.5481 0.6299 0.5766 0.0123 -0.0112 0.0072 610 HOH A O 6266 O O . HOH S . ? 0.2003 0.1939 0.2014 -0.0033 -0.0017 0.0023 611 HOH A O 6267 O O . HOH S . ? 0.3629 0.4160 0.3907 0.0264 -0.0082 0.0152 612 HOH A O 6268 O O . HOH S . ? 0.4924 0.4936 0.5001 0.0042 -0.0003 -0.0101 613 HOH A O 6269 O O . HOH S . ? 0.5288 0.5385 0.5215 -0.0053 0.0103 0.0137 614 HOH A O 6270 O O . HOH S . ? 0.4528 0.5402 0.4841 0.0117 -0.0103 0.0055 615 HOH A O 6271 O O . HOH S . ? 0.4495 0.5041 0.4750 0.0247 -0.0097 0.0162 616 HOH A O 6272 O O . HOH S . ? 0.4209 0.3760 0.4381 -0.0037 0.0152 -0.0251 617 HOH A O 6273 O O . HOH S . ? 0.4908 0.4670 0.4867 -0.0014 0.0001 0.0032 618 HOH A O 6274 O O . HOH S . ? 0.3301 0.3784 0.3403 -0.0118 -0.0098 -0.0043 619 HOH A O 6275 O O . HOH S . ? 0.3527 0.3708 0.3617 -0.0158 0.0037 -0.0021 620 HOH A O 6276 O O . HOH S . ? 0.3691 0.3797 0.3879 0.0136 0.0042 -0.0114 621 HOH A O 6277 O O . HOH S . ? 0.5335 0.5372 0.5194 0.0068 0.0080 0.0240 622 HOH A O 6278 O O . HOH S . ? 0.1893 0.1854 0.1963 0.0039 -0.0037 -0.0022 623 HOH A O 6279 O O . HOH S . ? 0.5991 0.6067 0.6051 -0.0164 0.0024 -0.0029 624 HOH A O 6280 O O . HOH S . ? 0.4014 0.4525 0.4230 -0.0014 0.0028 -0.0051 625 HOH A O 6281 O O . HOH S . ? 0.4767 0.5072 0.5045 0.0202 0.0038 -0.0062 626 HOH A O 6282 O O . HOH S . ? 0.6058 0.5865 0.6016 -0.0166 0.0037 -0.0080 627 HOH A O 6283 O O . HOH S . ? 0.5408 0.5917 0.5604 0.0191 -0.0116 0.0160 628 HOH A O 6284 O O . HOH S . ? 0.5016 0.5017 0.5094 -0.0018 0.0048 -0.0261 629 HOH A O 6285 O O . HOH S . ? 0.1610 0.1907 0.1684 -0.0095 0.0072 0.0004 630 HOH A O 6286 O O . HOH S . ? 0.3000 0.2913 0.3140 0.0201 -0.0033 0.0171 631 HOH A O 6287 O O . HOH S . ? 0.4897 0.5017 0.4746 0.0089 0.0061 0.0239 632 HOH A O 6288 O O . HOH S . ? 0.2776 0.2445 0.2720 -0.0057 0.0090 0.0072 633 HOH A O 6289 O O . HOH S . ? 0.3622 0.3551 0.3597 -0.0076 -0.0047 -0.0018 634 HOH A O 6290 O O . HOH S . ? 0.5432 0.5534 0.5488 -0.0005 0.0041 -0.0252 635 HOH A O 6291 O O . HOH S . ? 0.3825 0.3823 0.3774 0.0052 -0.0026 0.0077 636 HOH A O 6292 O O . HOH S . ? 0.4808 0.4506 0.4737 -0.0062 0.0133 0.0138 637 HOH A O 6293 O O . HOH S . ? 0.6225 0.5894 0.6172 -0.0103 0.0128 0.0082 638 HOH A O 6294 O O . HOH S . ? 0.5677 0.5603 0.5627 -0.0008 0.0032 0.0096 640 HOH A O 6295 O O . HOH S . ? 0.3202 0.3159 0.3143 -0.0075 0.0110 0.0134 641 HOH A O 6296 O O . HOH S . ? 0.2918 0.2901 0.2968 0.0134 -0.0072 0.0202 642 HOH A O 6297 O O . HOH S . ? 0.3298 0.3230 0.3397 0.0052 0.0002 -0.0100 643 HOH A O 6298 O O . HOH S . ? 0.2746 0.2956 0.2782 -0.0132 -0.0069 -0.0051 644 HOH A O 6299 O O . HOH S . ? 0.3528 0.3710 0.3619 -0.0203 0.0024 -0.0055 645 HOH A O 6300 O O . HOH S . ? 0.2940 0.2671 0.2879 0.0018 0.0051 0.0105 646 HOH A O 6301 O O . HOH S . ? 0.2967 0.2785 0.2889 0.0011 0.0071 0.0151 647 HOH A O 6302 O O . HOH S . ? 0.3124 0.3177 0.3024 0.0082 0.0014 0.0161 648 HOH A O 6303 O O . HOH S . ? 0.3182 0.3185 0.3168 -0.0103 -0.0051 -0.0035 649 HOH A O 6304 O O . HOH S . ? 0.4481 0.4278 0.4593 -0.0126 0.0063 -0.0246 650 HOH A O 6305 O O . HOH S . ? 0.4872 0.5394 0.5113 0.0264 -0.0100 0.0192 651 HOH A O 6306 O O . HOH S . ? 0.4169 0.4327 0.4249 0.0121 -0.0101 0.0154 652 HOH A O 6307 O O . HOH S . ? 0.6445 0.6262 0.6383 -0.0064 0.0108 0.0132 653 HOH A O 6308 O O . HOH S . ? 0.4476 0.4690 0.4385 -0.0001 0.0056 0.0099 654 HOH A O 6309 O O . HOH S . ? 0.5136 0.5379 0.5115 -0.0011 0.0041 0.0009 655 HOH A O 6310 O O . HOH S . ? 0.2672 0.2654 0.2738 -0.0011 0.0014 -0.0188 656 HOH A O 6311 O O . HOH S . ? 0.4869 0.5224 0.5061 0.0178 -0.0093 0.0127 657 HOH A O 6312 O O . HOH S . ? 0.4052 0.4645 0.4346 0.0099 -0.0020 -0.0018 658 HOH A O 6313 O O . HOH S . ? 0.5570 0.5852 0.5670 0.0110 -0.0114 0.0132 659 HOH A O 6314 O O . HOH S . ? 0.5429 0.5987 0.5603 0.0153 -0.0130 0.0147 660 HOH A O 6315 O O . HOH S . ? 0.2243 0.2084 0.2406 0.0138 0.0012 -0.0013 661 HOH A O 6316 O O . HOH S . ? 0.5414 0.5917 0.5660 0.0082 0.0042 -0.0078 662 HOH A O 6317 O O . HOH S . ? 0.2374 0.2245 0.2406 0.0018 -0.0056 0.0010 663 HOH A O 6318 O O . HOH S . ? 0.3536 0.3721 0.3621 -0.0165 -0.0011 -0.0053 664 HOH A O 6319 O O . HOH S . ? 0.6280 0.6455 0.6213 -0.0007 0.0046 0.0078 665 HOH A O 6320 O O . HOH S . ? 0.4828 0.5877 0.5097 0.0127 -0.0159 0.0111 666 HOH A O 6321 O O . HOH S . ? 0.2571 0.2711 0.2853 0.0266 0.0024 0.0017 667 HOH A O 6322 O O . HOH S . ? 0.3179 0.2722 0.3376 0.0152 0.0107 -0.0003 668 HOH A O 6323 O O . HOH S . ? 0.5123 0.5245 0.5197 -0.0136 -0.0001 -0.0029 669 HOH A O 6324 O O . HOH S . ? 0.5789 0.6599 0.6107 0.0215 -0.0104 0.0116 670 HOH A O 6325 O O . HOH S . ? 0.2711 0.2663 0.2844 0.0092 0.0000 -0.0062 671 HOH A O 6326 O O . HOH S . ? 0.2954 0.3728 0.3176 -0.0117 -0.0087 -0.0055 672 HOH A O 6327 O O . HOH S . ? 0.2457 0.2432 0.2492 -0.0023 -0.0033 0.0011 673 HOH A O 6328 O O . HOH S . ? 0.5517 0.5283 0.5492 -0.0155 0.0115 0.0043 674 HOH A O 6329 O O . HOH S . ? 0.5373 0.4966 0.5506 -0.0084 0.0089 -0.0130 675 HOH A O 6330 O O . HOH S . ? 0.5124 0.5246 0.5254 0.0083 0.0035 -0.0134 676 HOH A O 6331 O O . HOH S . ? 0.4373 0.4985 0.4513 0.0141 -0.0146 0.0164 677 HOH A O 6332 O O . HOH S . ? 0.3037 0.3248 0.3180 0.0093 0.0063 -0.0172 678 HOH A O 6333 O O . HOH S . ? 0.5687 0.6096 0.5823 0.0035 0.0062 -0.0097 679 HOH A O 6334 O O . HOH S . ? 0.4418 0.4416 0.4304 0.0020 0.0087 0.0198 680 HOH A O 6335 O O . HOH S . ? 0.5047 0.5396 0.5126 0.0045 0.0066 -0.0156 681 HOH A O 6336 O O . HOH S . ? 0.4008 0.3641 0.3947 -0.0043 0.0095 0.0071 682 HOH A O 6337 O O . HOH S . ? 0.5632 0.5971 0.5590 0.0000 0.0045 -0.0026 683 HOH A O 6338 O O . HOH S . ? 0.2994 0.3142 0.3093 0.0058 0.0061 -0.0216 684 HOH A O 6339 O O . HOH S . ? 0.2428 0.2580 0.2372 0.0042 -0.0040 0.0030 685 HOH A O 6340 O O . HOH S . ? 0.3254 0.3119 0.3245 0.0015 -0.0049 0.0031 686 HOH A O 6341 O O . HOH S . ? 0.4392 0.4296 0.4314 -0.0054 0.0117 0.0163 687 HOH A O 6342 O O . HOH S . ? 0.2613 0.3071 0.2896 0.0150 0.0004 -0.0031 688 HOH A O 6343 O O . HOH S . ? 0.5650 0.6311 0.5770 0.0141 -0.0157 0.0181 689 HOH A O 6344 O O . HOH S . ? 0.5499 0.5399 0.5498 0.0017 -0.0055 0.0022 690 HOH A O 6345 O O . HOH S . ? 0.5575 0.5834 0.5455 0.0017 0.0057 0.0123 691 HOH A O 6346 O O . HOH S . ? 0.5624 0.5540 0.5537 0.0098 0.0028 0.0177 692 HOH A O 6347 O O . HOH S . ? 0.5100 0.4551 0.5264 0.0057 0.0119 -0.0007 693 HOH A O 6348 O O . HOH S . ? 0.5790 0.5853 0.5870 0.0011 0.0058 -0.0264 694 HOH A O 6349 O O . HOH S . ? 0.5498 0.5114 0.5644 -0.0117 0.0119 -0.0240 695 HOH A O 6350 O O . HOH S . ? 0.5657 0.6251 0.5956 0.0102 0.0001 -0.0036 696 HOH A O 6351 O O . HOH S . ? 0.4000 0.4114 0.4071 -0.0113 -0.0018 -0.0025 697 HOH A O 6352 O O . HOH S . ? 0.5364 0.5584 0.5328 -0.0019 0.0049 0.0040 698 HOH A O 6353 O O . HOH S . ? 0.5904 0.6424 0.6020 0.0139 -0.0141 0.0171 699 HOH A O 6354 O O . HOH S . ? 0.5846 0.5346 0.5988 0.0081 0.0086 0.0069 700 HOH A O 6355 O O . HOH S . ? 0.1750 0.1868 0.1814 -0.0145 -0.0017 -0.0043 701 HOH A O 6356 O O . HOH S . ? 0.4719 0.5339 0.5034 0.0173 -0.0049 0.0036 702 HOH A O 6357 O O . HOH S . ? 0.2347 0.3445 0.2704 0.0273 -0.0136 0.0175 703 HOH A O 6358 O O . HOH S . ? 0.2850 0.2805 0.2825 0.0030 -0.0038 0.0040 704 HOH A O 6359 O O . HOH S . ? 0.3428 0.3996 0.3751 0.0184 -0.0019 0.0007 705 HOH A O 6360 O O . HOH S . ? 0.3426 0.3516 0.3474 -0.0169 -0.0011 -0.0058 706 HOH A O 6361 O O . HOH S . ? 0.4580 0.4319 0.4534 -0.0150 0.0056 -0.0061 707 HOH A O 6362 O O . HOH S . ? 0.4413 0.4102 0.4357 -0.0179 0.0088 -0.0090 708 HOH A O 6363 O O . HOH S . ? 0.3145 0.3358 0.3195 0.0066 -0.0114 0.0116 709 HOH A O 6364 O O . HOH S . ? 0.3006 0.3180 0.3124 0.0073 0.0038 -0.0139 710 HOH A O 6365 O O . HOH S . ? 0.3622 0.3716 0.3630 -0.0015 -0.0037 -0.0105 711 HOH A O 6366 O O . HOH S . ? 0.3086 0.3491 0.3184 0.0055 -0.0127 0.0091 712 HOH A O 6367 O O . HOH S . ? 0.3378 0.3066 0.3503 0.0118 0.0015 0.0085 713 HOH A O 6368 O O . HOH S . ? 0.5986 0.5713 0.5893 0.0105 0.0091 0.0210 714 HOH A O 6369 O O . HOH S . ? 0.3176 0.3644 0.3391 0.0068 0.0050 -0.0088 715 HOH A O 6370 O O . HOH S . ? 0.3369 0.3589 0.3272 0.0014 0.0042 0.0095 716 HOH A O 6371 O O . HOH S . ? 0.3046 0.3401 0.3221 0.0090 0.0061 -0.0128 717 HOH A O 6372 O O . HOH S . ? 0.5001 0.4563 0.4935 -0.0108 0.0174 0.0096 718 HOH A O 6373 O O . HOH S . ? 0.6231 0.6142 0.6319 -0.0032 0.0041 -0.0233 719 HOH A O 6374 O O . HOH S . ? 0.5707 0.5321 0.5634 -0.0111 0.0190 0.0142 720 HOH A O 6375 O O . HOH S . ? 0.4815 0.4733 0.4841 -0.0247 0.0105 -0.0033 721 HOH A O 6376 O O . HOH S . ? 0.4572 0.4096 0.4493 -0.0110 0.0217 0.0143 722 HOH A O 6377 O O . HOH S . ? 0.3121 0.3273 0.3337 0.0159 0.0036 -0.0087 723 HOH A O 6378 O O . HOH S . ? 0.3511 0.4042 0.3680 -0.0239 -0.0019 -0.0105 724 HOH A O 6379 O O . HOH S . ? 0.5984 0.5681 0.5932 -0.0036 0.0038 0.0023 725 HOH A O 6380 O O . HOH S . ? 0.2778 0.2788 0.2878 0.0044 0.0040 -0.0192 726 HOH A O 6381 O O . HOH S . ? 0.4749 0.4959 0.4837 -0.0183 0.0075 -0.0009 727 HOH A O 6382 O O . HOH S . ? 0.5456 0.5208 0.5365 0.0001 0.0114 0.0182 728 HOH A O 6383 O O . HOH S . ? 0.4692 0.4947 0.4884 0.0129 0.0072 -0.0161 729 HOH A O 6384 O O . HOH S . ? 0.4952 0.5267 0.5148 0.0122 0.0069 -0.0146 730 HOH A O 6385 O O . HOH S . ? 0.3860 0.4572 0.4150 0.0021 -0.0046 -0.0020 731 HOH A O 6386 O O . HOH S . ? 0.3739 0.3991 0.4028 0.0236 0.0028 -0.0025 732 HOH A O 6387 O O . HOH S . ? 0.3502 0.3838 0.3792 0.0212 0.0020 -0.0031 733 HOH A O 6388 O O . HOH S . ? 0.3797 0.3507 0.3908 -0.0080 0.0049 -0.0142 734 HOH A O 6389 O O . HOH S . ? 0.3899 0.4284 0.3996 -0.0012 0.0060 -0.0053 735 HOH A O 6390 O O . HOH S . ? 0.2946 0.3111 0.3222 0.0278 -0.0001 0.0073 736 HOH A O 6391 O O . HOH S . ? 0.4683 0.5472 0.4987 0.0239 -0.0111 0.0147 737 HOH A O 6392 O O . HOH S . ? 0.3448 0.3095 0.3582 -0.0089 0.0090 -0.0193 738 HOH A O 6393 O O . HOH S . ? 0.5413 0.5282 0.5477 0.0126 -0.0049 0.0180 739 HOH A O 6394 O O . HOH S . ? 0.3571 0.3621 0.3623 -0.0126 0.0012 -0.0013 740 HOH A O 6395 O O . HOH S . ? 0.2834 0.3091 0.2870 0.0017 0.0054 -0.0240 741 HOH A O 6396 O O . HOH S . ? 0.5620 0.5470 0.5576 -0.0119 0.0131 0.0114 742 HOH A O 6397 O O . HOH S . ? 0.5322 0.5455 0.5498 0.0124 0.0064 -0.0162 743 HOH A O 6398 O O . HOH S . ? 0.4548 0.4217 0.4489 -0.0069 0.0112 0.0093 744 HOH A O 6399 O O . HOH S . ? 0.4492 0.4103 0.4431 -0.0091 0.0139 0.0084 745 HOH A O 6400 O O . HOH S . ? 0.5293 0.5259 0.5297 -0.0197 0.0014 -0.0083 746 HOH A O 6401 O O . HOH S . ? 0.5833 0.5778 0.5820 -0.0096 -0.0038 -0.0029 747 HOH A O 6402 O O . HOH S . ? 0.3920 0.4308 0.4166 0.0239 -0.0073 0.0135 748 HOH A O 6403 O O . HOH S . ? 0.5512 0.5077 0.5442 -0.0035 0.0129 0.0088 749 HOH A O 6404 O O . HOH S . ? 0.3896 0.3747 0.3868 -0.0155 0.0019 -0.0064 750 HOH A O 6405 O O . HOH S . ? 0.2688 0.3066 0.2830 -0.0094 0.0045 -0.0028 752 HOH A O 6406 O O . HOH S . ? 0.5317 0.5792 0.5515 -0.0085 -0.0004 -0.0042 753 HOH A O 6407 O O . HOH S . ? 0.3086 0.3172 0.3364 0.0280 0.0024 0.0041 754 HOH A O 6408 O O . HOH S . ? 0.3298 0.3177 0.3426 0.0079 0.0015 -0.0091 755 HOH A O 6409 O O . HOH S . ? 0.4683 0.4830 0.4758 -0.0170 0.0059 -0.0009 756 HOH A O 6410 O O . HOH S . ? 0.3522 0.3511 0.3401 0.0054 0.0072 0.0211 757 HOH A O 6411 O O . HOH S . ? 0.4014 0.4826 0.4275 -0.0043 -0.0088 -0.0024 758 HOH A O 6412 O O . HOH S . ? 0.5483 0.5134 0.5612 -0.0100 0.0081 -0.0171 759 HOH A O 6413 O O . HOH S . ? 0.3406 0.3630 0.3401 -0.0090 -0.0096 -0.0017 760 HOH A O 6414 O O . HOH S . ? 0.3299 0.3735 0.3588 0.0172 0.0035 -0.0066 761 HOH A O 6415 O O . HOH S . ? 0.5323 0.5395 0.5383 -0.0023 0.0044 -0.0272 762 HOH A O 6416 O O . HOH S . ? 0.3328 0.3676 0.3376 -0.0009 0.0058 -0.0046 763 HOH A O 6417 O O . HOH S . ? 0.5428 0.5480 0.5381 0.0047 -0.0037 0.0053 764 HOH A O 6418 O O . HOH S . ? 0.5897 0.6452 0.6140 0.0051 0.0049 -0.0078 765 HOH A O 6419 O O . HOH S . ? 0.3890 0.4024 0.3944 0.0109 -0.0102 0.0161 766 HOH A O 6420 O O . HOH S . ? 0.3507 0.3472 0.3510 -0.0090 -0.0041 -0.0021 767 HOH A O 6421 O O . HOH S . ? 0.4669 0.4344 0.4627 -0.0145 0.0134 0.0049 768 HOH A O 6422 O O . HOH S . ? 0.5563 0.5518 0.5523 -0.0112 0.0122 0.0116 769 HOH A O 6423 O O . HOH S . ? 0.5322 0.5142 0.5440 -0.0081 0.0095 -0.0320 770 HOH A O 6424 O O . HOH S . ? 0.5354 0.4837 0.5263 -0.0071 0.0227 0.0173 771 HOH A O 6425 O O . HOH S . ? 0.6061 0.6442 0.5994 0.0005 0.0043 -0.0032 772 HOH A O 6426 O O . HOH S . ? 0.4731 0.4282 0.4941 0.0111 0.0145 -0.0143 773 HOH A O 6427 O O . HOH S . ? 0.2950 0.2810 0.2948 0.0012 -0.0055 0.0027 774 HOH A O 6428 O O . HOH S . ? 0.3969 0.3930 0.4052 0.0146 -0.0064 0.0176 775 HOH A O 6429 O O . HOH S . ? 0.4730 0.5343 0.4956 0.0160 -0.0116 0.0119 776 HOH A O 6430 O O . HOH S . ? 0.5836 0.6080 0.5899 0.0036 0.0067 -0.0245 777 HOH A O 6431 O O . HOH S . ? 0.6392 0.5860 0.6566 -0.0096 0.0168 -0.0224 778 HOH A O 6432 O O . HOH S . ? 0.3646 0.3842 0.3689 0.0014 -0.0108 0.0064 779 HOH A O 6433 O O . HOH S . ? 0.5391 0.5049 0.5514 -0.0147 0.0078 -0.0126 780 HOH A O 6434 O O . HOH S . ? 0.6448 0.7049 0.6785 0.0183 -0.0001 -0.0014 781 HOH A O 6435 O O . HOH S . ? 0.3587 0.3923 0.3719 -0.0184 -0.0006 -0.0065 782 HOH A O 6436 O O . HOH S . ? 0.2429 0.2409 0.2472 0.0026 -0.0033 -0.0035 783 HOH A O 6437 O O . HOH S . ? 0.4706 0.4550 0.4690 0.0008 -0.0043 0.0034 784 HOH A O 6438 O O . HOH S . ? 0.2832 0.2698 0.2937 0.0147 -0.0040 0.0147 785 HOH A O 6439 O O . HOH S . ? 0.3438 0.3552 0.3496 0.0013 0.0036 -0.0221 786 HOH A O 6440 O O . HOH S . ? 0.5293 0.5421 0.5158 0.0011 0.0100 0.0206 787 HOH A O 6441 O O . HOH S . ? 0.4897 0.4834 0.4796 0.0127 0.0040 0.0216 788 HOH A O 6442 O O . HOH S . ? 0.5225 0.4821 0.5332 0.0058 0.0039 0.0080 789 HOH A O 6443 O O . HOH S . ? 0.3732 0.4082 0.3859 -0.0130 0.0059 -0.0021 790 HOH A O 6444 O O . HOH S . ? 0.4008 0.4058 0.4056 -0.0188 0.0019 -0.0053 791 HOH A O 6445 O O . HOH S . ? 0.3940 0.4011 0.4152 0.0168 0.0036 -0.0079 792 HOH A O 6446 O O . HOH S . ? 0.4737 0.5561 0.5006 0.0163 -0.0128 0.0116 793 HOH A O 6447 O O . HOH S . ? 0.6004 0.5942 0.6089 -0.0015 0.0036 -0.0222 794 HOH A O 6448 O O . HOH S . ? 0.4689 0.4738 0.4780 0.0053 0.0010 -0.0116 795 HOH A O 6449 O O . HOH S . ? 0.4918 0.5675 0.5100 -0.0005 -0.0135 0.0028 796 HOH A O 6450 O O . HOH S . ? 0.4356 0.4619 0.4468 -0.0212 0.0073 -0.0030 797 HOH A O 6451 O O . HOH S . ? 0.5901 0.6196 0.5974 -0.0171 -0.0054 -0.0074 798 HOH A O 6452 O O . HOH S . ? 0.3295 0.3096 0.3334 0.0011 -0.0046 0.0034 799 HOH A O 6453 O O . HOH S . ? 0.5625 0.5797 0.5712 -0.0168 0.0003 -0.0046 800 HOH A O 6454 O O . HOH S . ? 0.3297 0.4069 0.3616 0.0081 -0.0058 0.0005 801 HOH A O 6455 O O . HOH S . ? 0.5639 0.5340 0.5594 -0.0150 0.0076 -0.0048 802 HOH A O 6456 O O . HOH S . ? 0.5375 0.5011 0.5280 -0.0006 0.0154 0.0194 803 HOH A O 6457 O O . HOH S . ? 0.2746 0.2733 0.2896 0.0108 0.0006 -0.0065 804 HOH A O 6458 O O . HOH S . ? 0.3788 0.4117 0.3884 -0.0166 -0.0051 -0.0069 805 HOH A O 6459 O O . HOH S . ? 0.5219 0.5117 0.5397 0.0145 0.0024 -0.0049 806 HOH A O 6460 O O . HOH S . ? 0.5136 0.5151 0.5039 -0.0036 0.0115 0.0181 807 HOH A O 6461 O O . HOH S . ? 0.5087 0.4973 0.4988 0.0144 0.0054 0.0231 808 HOH A O 6462 O O . HOH S . ? 0.3213 0.2932 0.3158 -0.0011 0.0053 0.0083 809 HOH A O 6463 O O . HOH S . ? 0.4418 0.4807 0.4685 0.0167 0.0057 -0.0102 810 HOH A O 6464 O O . HOH S . ? 0.5364 0.5669 0.5249 0.0018 0.0044 0.0085 811 HOH A O 6465 O O . HOH S . ? 0.3172 0.2996 0.3204 0.0014 -0.0054 0.0031 812 HOH A O 6466 O O . HOH S . ? 0.6017 0.6266 0.6181 0.0109 0.0076 -0.0183 813 HOH A O 6467 O O . HOH S . ? 0.3465 0.3137 0.3550 0.0068 0.0006 0.0106 814 HOH A O 6468 O O . HOH S . ? 0.5822 0.5471 0.5730 0.0091 0.0117 0.0204 815 HOH A O 6469 O O . HOH S . ? 0.4113 0.4313 0.4203 0.0056 0.0055 -0.0194 816 HOH A O 6470 O O . HOH S . ? 0.5612 0.6123 0.5895 0.0122 0.0012 -0.0045 817 HOH A O 6471 O O . HOH S . ? 0.5257 0.5086 0.5236 -0.0002 -0.0036 0.0032 818 HOH A O 6472 O O . HOH S . ? 0.6018 0.5748 0.6188 0.0072 0.0100 -0.0194 819 HOH A O 6473 O O . HOH S . ? 0.4830 0.4234 0.4734 -0.0060 0.0256 0.0184 820 HOH A O 6474 O O . HOH S . ? 0.4777 0.4570 0.4733 -0.0097 0.0009 -0.0033 821 HOH A O 6475 O O . HOH S . ? 0.6131 0.6343 0.6104 -0.0114 -0.0088 -0.0039 822 HOH A O 6476 O O . HOH S . ? 0.5133 0.5340 0.5008 0.0043 0.0037 0.0140 823 HOH A O 6477 O O . HOH S . ? 0.4299 0.3919 0.4230 -0.0075 0.0148 0.0117 824 HOH A O 6478 O O . HOH S . ? 0.5195 0.5127 0.5214 -0.0201 0.0104 0.0013 825 HOH A O 6479 O O . HOH S . ? 0.4169 0.4022 0.4228 0.0025 -0.0040 -0.0019 826 HOH A O 6480 O O . HOH S . ? 0.5582 0.5514 0.5571 -0.0182 0.0010 -0.0080 827 HOH A O 6481 O O . HOH S . ? 0.5189 0.5482 0.5305 -0.0180 0.0068 -0.0022 828 HOH A O 6482 O O . HOH S . ? 0.5423 0.5580 0.5353 -0.0030 0.0075 0.0107 829 HOH A O 6483 O O . HOH S . ? 0.5077 0.5144 0.4965 0.0006 0.0084 0.0179 830 HOH A O 6484 O O . HOH S . ? 0.3102 0.2904 0.3062 -0.0064 -0.0009 -0.0010 831 HOH A O 6485 O O . HOH S . ? 0.3482 0.3258 0.3614 0.0135 -0.0007 0.0077 832 HOH A O 6486 O O . HOH S . ? 0.4074 0.3929 0.4034 0.0036 -0.0014 0.0075 833 HOH A O 6487 O O . HOH S . ? 0.5291 0.4847 0.5467 -0.0107 0.0188 -0.0355 834 HOH A O 6488 O O . HOH S . ? 0.4105 0.4149 0.4285 0.0134 0.0024 -0.0082 835 HOH A O 6489 O O . HOH S . ? 0.5002 0.5113 0.4906 -0.0053 0.0126 0.0171 836 HOH A O 6490 O O . HOH S . ? 0.6497 0.7722 0.6908 0.0258 -0.0126 0.0138 837 HOH A O 6491 O O . HOH S . ? 0.3384 0.3343 0.3467 0.0013 0.0022 -0.0180 838 HOH A O 6492 O O . HOH S . ? 0.5848 0.5620 0.5805 -0.0119 0.0125 0.0093 839 HOH A O 6493 O O . HOH S . ? 0.3436 0.4320 0.3740 0.0053 -0.0097 0.0019 840 HOH A O 6494 O O . HOH S . ? 0.4059 0.3781 0.4017 -0.0149 0.0151 0.0085 841 HOH A O 6495 O O . HOH S . ? 0.4508 0.4522 0.4763 0.0254 0.0028 0.0025 842 HOH A O 6496 O O . HOH S . ? 0.4653 0.4152 0.4589 -0.0126 0.0183 0.0045 843 HOH A O 6497 O O . HOH S . ? 0.2899 0.3160 0.3114 0.0208 -0.0065 0.0115 844 HOH A O 6498 O O . HOH S . ? 0.3887 0.4011 0.3918 -0.0192 0.0132 0.0052 845 HOH A O 6499 O O . HOH S . ? 0.3767 0.3647 0.3953 0.0171 0.0014 0.0005 846 HOH A O 6500 O O . HOH S . ? 0.4449 0.4452 0.4410 0.0038 -0.0032 0.0051 847 HOH A O 6501 O O . HOH S . ? 0.5880 0.6649 0.6069 0.0146 -0.0152 0.0150 848 HOH A O 6502 O O . HOH S . ? 0.4522 0.4935 0.4471 0.0003 0.0034 -0.0149 849 HOH A O 6503 O O . HOH S . ? 0.4309 0.4348 0.4397 0.0147 -0.0078 0.0171 850 HOH A O 6504 O O . HOH S . ? 0.5037 0.5175 0.5277 0.0190 0.0076 -0.0135 851 HOH A O 6505 O O . HOH S . ? 0.4692 0.5206 0.5013 0.0287 -0.0049 0.0114 852 HOH A O 6506 O O . HOH S . ? 0.5287 0.4956 0.5209 -0.0076 0.0164 0.0158 853 HOH A O 6507 O O . HOH S . ? 0.5365 0.6212 0.5628 -0.0013 -0.0103 -0.0004 854 HOH A O 6508 O O . HOH S . ? 0.2821 0.2516 0.2779 -0.0101 0.0080 0.0025 855 HOH A O 6509 O O . HOH S . ? 0.4012 0.3600 0.3957 -0.0173 0.0207 0.0091 856 HOH A O 6510 O O . HOH S . ? 0.3779 0.3855 0.4038 0.0233 0.0039 -0.0029 857 HOH A O 6511 O O . HOH S . ? 0.4844 0.4675 0.4763 -0.0006 0.0087 0.0160 858 HOH A O 6512 O O . HOH S . ? 0.4207 0.3948 0.4171 -0.0123 0.0105 0.0056 859 HOH A O 6513 O O . HOH S . ? 0.5345 0.5342 0.5377 -0.0288 0.0068 -0.0111 860 HOH A O 6514 O O . HOH S . ? 0.3807 0.3745 0.3794 0.0030 -0.0050 0.0031 861 HOH A O 6515 O O . HOH S . ? 0.3858 0.4267 0.4028 -0.0122 0.0010 -0.0043 862 HOH A O 6516 O O . HOH S . ? 0.5680 0.5354 0.5853 0.0055 0.0114 -0.0204 863 HOH A O 6517 O O . HOH S . ? 0.4082 0.4241 0.4169 -0.0130 0.0002 -0.0027 864 HOH A O 6518 O O . HOH S . ? 0.5648 0.5848 0.5747 -0.0185 0.0029 -0.0042 865 HOH A O 6519 O O . HOH S . ? 0.5672 0.5718 0.5782 0.0159 -0.0074 0.0160 866 HOH A O 6520 O O . HOH S . ? 0.5156 0.5660 0.5377 0.0161 -0.0101 0.0108 867 HOH A O 6521 O O . HOH S . ? 0.2833 0.2580 0.2951 0.0115 -0.0006 0.0078 868 HOH A O 6522 O O . HOH S . ? 0.3278 0.3150 0.3315 0.0017 -0.0051 -0.0004 869 HOH A O 6523 O O . HOH S . ? 0.5810 0.5757 0.5695 -0.0002 0.0116 0.0214 870 HOH A O 6524 O O . HOH S . ? 0.4514 0.4481 0.4377 0.0042 0.0110 0.0250 871 HOH A O 6525 O O . HOH S . ? 0.5540 0.5421 0.5542 -0.0207 0.0055 -0.0064 872 HOH A O 6526 O O . HOH S . ? 0.4894 0.5316 0.4968 0.0022 -0.0131 0.0074 873 HOH A O 6527 O O . HOH S . ? 0.4895 0.4814 0.5097 0.0246 -0.0002 0.0128 874 HOH A O 6528 O O . HOH S . ? 0.3696 0.4193 0.3920 -0.0013 -0.0009 -0.0036 875 HOH A O 6529 O O . HOH S . ? 0.6405 0.6092 0.6473 0.0059 -0.0001 0.0123 876 HOH A O 6530 O O . HOH S . ? 0.4195 0.4161 0.4205 -0.0201 0.0137 0.0053 877 HOH A O 6531 O O . HOH S . ? 0.4835 0.4623 0.4780 0.0032 0.0023 0.0099 878 HOH A O 6532 O O . HOH S . ? 0.3535 0.3381 0.3539 -0.0205 0.0094 -0.0017 879 HOH A O 6533 O O . HOH S . ? 0.5275 0.6149 0.5500 0.0171 -0.0155 0.0158 880 HOH A O 6534 O O . HOH S . ? 0.4546 0.4773 0.4790 0.0178 0.0041 -0.0083 881 HOH A O 6535 O O . HOH S . ? 0.5296 0.5090 0.5242 -0.0180 0.0046 -0.0103 882 HOH A O 6536 O O . HOH S . ? 0.5331 0.4772 0.5533 0.0078 0.0160 -0.0110 883 HOH A O 6537 O O . HOH S . ? 0.4645 0.4688 0.4711 -0.0064 0.0058 -0.0324 884 HOH A O 6538 O O . HOH S . ? 0.5611 0.5494 0.5626 -0.0235 0.0127 0.0001 885 HOH A O 6539 O O . HOH S . ? 0.5564 0.5986 0.5730 -0.0107 0.0037 -0.0037 886 HOH A O 6540 O O . HOH S . ? 0.4428 0.4098 0.4369 -0.0020 0.0071 0.0076 887 HOH A O 6541 O O . HOH S . ? 0.5917 0.5901 0.6047 0.0086 0.0007 -0.0084 888 HOH A O 6542 O O . HOH S . ? 0.5304 0.5531 0.5567 0.0310 -0.0034 0.0165 889 HOH A O 6543 O O . HOH S . ? 0.6533 0.6236 0.6698 -0.0056 0.0183 -0.0415 891 HOH A O 6544 O O . HOH S . ? 0.5269 0.6288 0.5590 0.0219 -0.0138 0.0148 892 HOH A O 6545 O O . HOH S . ? 0.5276 0.5249 0.5211 0.0082 -0.0011 0.0122 893 HOH A O 6546 O O . HOH S . ? 0.4076 0.3797 0.4184 -0.0133 0.0050 -0.0107 894 HOH A O 6547 O O . HOH S . ? 0.4661 0.4907 0.4726 0.0047 -0.0114 0.0089 895 HOH A O 6548 O O . HOH S . ? 0.5022 0.5289 0.5045 -0.0049 -0.0109 0.0017 896 HOH A O 6549 O O . HOH S . ? 0.5439 0.5390 0.5404 -0.0150 0.0153 0.0119 897 HOH A O 6550 O O . HOH S . ? 0.5726 0.5547 0.5850 -0.0145 0.0121 -0.0394 898 HOH A O 6551 O O . HOH S . ? 0.6084 0.5662 0.6214 0.0132 0.0054 0.0140 900 HOH A O 6552 O O . HOH S . ? 0.4985 0.4430 0.4910 -0.0089 0.0196 0.0067 901 HOH A O 6553 O O . HOH T . ? 0.1000 0.0919 0.0997 0.0009 -0.0078 0.0059 2 HOH B O 6554 O O . HOH T . ? 0.1412 0.1407 0.1280 -0.0016 -0.0009 0.0248 3 HOH B O 6555 O O . HOH T . ? 0.1627 0.1377 0.1553 0.0041 0.0061 -0.0021 4 HOH B O 6556 O O . HOH T . ? 0.0737 0.0692 0.0641 -0.0028 -0.0039 0.0102 5 HOH B O 6557 O O . HOH T . ? 0.0735 0.0597 0.0757 0.0040 -0.0066 0.0093 11 HOH B O 6558 O O . HOH T . ? 0.0810 0.0868 0.0659 -0.0052 -0.0006 0.0122 12 HOH B O 6559 O O . HOH T . ? 0.0730 0.0751 0.0603 -0.0049 -0.0006 0.0099 13 HOH B O 6560 O O . HOH T . ? 0.1061 0.1228 0.0853 -0.0063 0.0003 0.0148 14 HOH B O 6561 O O . HOH T . ? 0.1007 0.0971 0.1011 0.0016 -0.0085 0.0069 15 HOH B O 6562 O O . HOH T . ? 0.1293 0.1243 0.1194 -0.0031 -0.0018 0.0040 16 HOH B O 6563 O O . HOH T . ? 0.1343 0.1787 0.1129 -0.0091 -0.0100 0.0036 18 HOH B O 6564 O O . HOH T . ? 0.1284 0.0984 0.1367 -0.0016 0.0007 -0.0009 19 HOH B O 6565 O O . HOH T . ? 0.1294 0.1173 0.1246 -0.0012 -0.0036 0.0043 20 HOH B O 6566 O O . HOH T . ? 0.1148 0.1060 0.1095 0.0012 -0.0056 0.0150 21 HOH B O 6567 O O . HOH T . ? 0.0764 0.0799 0.0624 -0.0028 -0.0031 0.0164 22 HOH B O 6568 O O . HOH T . ? 0.1274 0.1097 0.1240 -0.0008 -0.0041 0.0024 24 HOH B O 6569 O O . HOH T . ? 0.1349 0.1357 0.1255 -0.0018 -0.0071 0.0093 25 HOH B O 6570 O O . HOH T . ? 0.1385 0.1396 0.1260 -0.0082 0.0042 0.0215 29 HOH B O 6571 O O . HOH T . ? 0.1295 0.1439 0.1337 -0.0039 0.0012 0.0027 30 HOH B O 6572 O O . HOH T . ? 0.0999 0.0941 0.0925 -0.0043 -0.0014 0.0099 33 HOH B O 6573 O O . HOH T . ? 0.1051 0.0981 0.0977 -0.0046 -0.0010 0.0126 36 HOH B O 6574 O O . HOH T . ? 0.1374 0.1663 0.1205 -0.0064 -0.0093 0.0056 37 HOH B O 6575 O O . HOH T . ? 0.1398 0.1305 0.1500 -0.0172 0.0021 -0.0101 39 HOH B O 6576 O O . HOH T . ? 0.0906 0.0804 0.0851 -0.0042 -0.0014 0.0120 44 HOH B O 6577 O O . HOH T . ? 0.1061 0.0880 0.0910 -0.0094 0.0069 -0.0147 46 HOH B O 6578 O O . HOH T . ? 0.1628 0.1451 0.1553 -0.0002 0.0001 -0.0005 47 HOH B O 6579 O O . HOH T . ? 0.1355 0.1212 0.1419 -0.0113 0.0007 0.0001 48 HOH B O 6580 O O . HOH T . ? 0.0906 0.0839 0.0827 -0.0054 0.0002 0.0154 49 HOH B O 6581 O O . HOH T . ? 0.1219 0.1129 0.1264 -0.0086 -0.0010 0.0018 50 HOH B O 6582 O O . HOH T . ? 0.1677 0.1465 0.1723 -0.0056 -0.0012 0.0028 55 HOH B O 6583 O O . HOH T . ? 0.3560 0.3744 0.3366 -0.0075 0.0042 0.0075 56 HOH B O 6584 O O . HOH T . ? 0.1213 0.1321 0.1181 0.0043 -0.0102 0.0146 58 HOH B O 6585 O O . HOH T . ? 0.0711 0.0858 0.0762 -0.0031 0.0002 0.0022 60 HOH B O 6586 O O . HOH T . ? 0.1154 0.1050 0.1080 -0.0021 -0.0034 0.0036 61 HOH B O 6587 O O . HOH T . ? 0.1621 0.1431 0.1558 0.0007 -0.0003 0.0006 64 HOH B O 6588 O O . HOH T . ? 0.1451 0.1208 0.1373 -0.0047 0.0014 -0.0034 65 HOH B O 6589 O O . HOH T . ? 0.1784 0.1907 0.1802 -0.0107 0.0045 0.0058 67 HOH B O 6590 O O . HOH T . ? 0.1407 0.1279 0.1383 -0.0012 -0.0063 0.0033 72 HOH B O 6591 O O . HOH T . ? 0.1242 0.1113 0.1203 0.0079 0.0041 0.0016 73 HOH B O 6592 O O . HOH T . ? 0.1476 0.1428 0.1495 -0.0165 0.0072 0.0109 74 HOH B O 6593 O O . HOH T . ? 0.2294 0.2335 0.2378 -0.0180 0.0044 0.0011 78 HOH B O 6594 O O . HOH T . ? 0.1174 0.1150 0.1080 -0.0026 -0.0061 0.0070 79 HOH B O 6595 O O . HOH T . ? 0.1679 0.1506 0.1626 0.0009 -0.0018 0.0019 80 HOH B O 6596 O O . HOH T . ? 0.4612 0.4773 0.4629 -0.0045 0.0036 0.0035 334 HOH B O 6597 O O . HOH T . ? 0.5120 0.4907 0.5032 0.0061 0.0116 -0.0071 338 HOH B O 6598 O O . HOH T . ? 0.6313 0.6230 0.6281 0.0028 -0.0067 0.0141 393 HOH B O 6599 O O . HOH T . ? 0.5406 0.5471 0.5290 0.0107 -0.0037 0.0390 471 HOH B O 6600 O O . HOH T . ? 0.3690 0.4018 0.3417 -0.0052 -0.0026 0.0192 472 HOH B O 6601 O O . HOH T . ? 0.1573 0.1814 0.1327 -0.0126 -0.0019 -0.0071 473 HOH B O 6602 O O . HOH T . ? 0.1515 0.1152 0.1600 -0.0063 0.0042 0.0019 474 HOH B O 6603 O O . HOH T . ? 0.1536 0.1737 0.1405 -0.0068 0.0075 0.0047 475 HOH B O 6604 O O . HOH T . ? 0.3969 0.3927 0.4031 -0.0191 0.0069 0.0058 476 HOH B O 6605 O O . HOH T . ? 0.2107 0.1972 0.2131 -0.0003 -0.0053 0.0003 477 HOH B O 6606 O O . HOH T . ? 0.3392 0.3513 0.3381 -0.0035 0.0036 0.0037 478 HOH B O 6607 O O . HOH T . ? 0.3763 0.3658 0.3576 -0.0179 0.0082 -0.0236 479 HOH B O 6608 O O . HOH T . ? 0.1334 0.1327 0.1336 0.0055 -0.0004 0.0038 480 HOH B O 6609 O O . HOH T . ? 0.4497 0.4195 0.4596 0.0109 0.0002 0.0127 481 HOH B O 6610 O O . HOH T . ? 0.4260 0.4051 0.4267 0.0072 -0.0023 0.0218 482 HOH B O 6611 O O . HOH T . ? 0.1398 0.1290 0.1399 0.0005 -0.0072 0.0045 483 HOH B O 6612 O O . HOH T . ? 0.4594 0.4900 0.4324 -0.0093 0.0051 0.0042 484 HOH B O 6613 O O . HOH T . ? 0.5497 0.5564 0.5448 -0.0106 -0.0067 -0.0040 485 HOH B O 6614 O O . HOH T . ? 0.1891 0.1569 0.1913 -0.0050 0.0044 0.0164 486 HOH B O 6615 O O . HOH T . ? 0.2043 0.1743 0.1967 0.0071 0.0108 -0.0037 487 HOH B O 6616 O O . HOH T . ? 0.3620 0.3551 0.3691 0.0000 -0.0014 0.0000 488 HOH B O 6617 O O . HOH T . ? 0.1929 0.1781 0.1866 -0.0022 0.0003 0.0216 489 HOH B O 6618 O O . HOH T . ? 0.2337 0.2122 0.2274 -0.0019 -0.0009 -0.0002 490 HOH B O 6619 O O . HOH T . ? 0.5066 0.5034 0.4998 -0.0131 -0.0032 -0.0075 491 HOH B O 6620 O O . HOH T . ? 0.3421 0.3247 0.3394 0.0005 -0.0043 0.0031 492 HOH B O 6621 O O . HOH T . ? 0.4763 0.4340 0.4648 -0.0063 0.0144 -0.0136 493 HOH B O 6622 O O . HOH T . ? 0.1650 0.1553 0.1652 0.0014 -0.0053 0.0025 494 HOH B O 6623 O O . HOH T . ? 0.1297 0.1096 0.1227 -0.0046 -0.0009 -0.0022 495 HOH B O 6624 O O . HOH T . ? 0.1938 0.2322 0.1752 0.0051 -0.0100 0.0287 496 HOH B O 6625 O O . HOH T . ? 0.1988 0.1841 0.1940 0.0016 -0.0015 0.0023 497 HOH B O 6626 O O . HOH T . ? 0.3514 0.3872 0.3398 0.0033 -0.0123 0.0192 498 HOH B O 6627 O O . HOH T . ? 0.4632 0.4262 0.4721 0.0047 0.0023 0.0092 499 HOH B O 6628 O O . HOH T . ? 0.5783 0.5739 0.5780 0.0072 -0.0017 0.0053 500 HOH B O 6629 O O . HOH T . ? 0.1363 0.1193 0.1317 0.0046 0.0008 0.0024 503 HOH B O 6630 O O . HOH T . ? 0.1487 0.1277 0.1446 0.0015 -0.0019 0.0034 504 HOH B O 6631 O O . HOH T . ? 0.5362 0.5191 0.5339 0.0007 -0.0043 0.0033 505 HOH B O 6632 O O . HOH T . ? 0.1492 0.1474 0.1390 -0.0047 -0.0008 0.0111 506 HOH B O 6633 O O . HOH T . ? 0.1888 0.2225 0.1696 -0.0060 -0.0093 0.0077 507 HOH B O 6634 O O . HOH T . ? 0.4798 0.4479 0.4673 -0.0084 0.0102 -0.0141 508 HOH B O 6635 O O . HOH T . ? 0.1853 0.1982 0.1885 0.0096 0.0034 0.0034 509 HOH B O 6636 O O . HOH T . ? 0.4989 0.5006 0.4853 -0.0004 0.0091 -0.0077 510 HOH B O 6637 O O . HOH T . ? 0.2337 0.1995 0.2457 -0.0173 0.0085 -0.0080 511 HOH B O 6638 O O . HOH T . ? 0.4566 0.4288 0.4513 0.0048 0.0027 0.0052 512 HOH B O 6639 O O . HOH T . ? 0.5178 0.5094 0.5146 0.0044 -0.0061 0.0178 513 HOH B O 6640 O O . HOH T . ? 0.5117 0.5223 0.4969 0.0057 -0.0042 0.0335 514 HOH B O 6641 O O . HOH T . ? 0.4868 0.5296 0.4749 -0.0063 -0.0127 0.0050 515 HOH B O 6642 O O . HOH T . ? 0.5455 0.4966 0.5382 0.0108 0.0184 -0.0019 516 HOH B O 6643 O O . HOH T . ? 0.1679 0.1763 0.1514 -0.0032 0.0082 -0.0068 517 HOH B O 6644 O O . HOH T . ? 0.5068 0.4950 0.5031 0.0010 -0.0055 0.0131 518 HOH B O 6645 O O . HOH T . ? 0.4411 0.4375 0.4339 0.0031 -0.0057 0.0203 519 HOH B O 6646 O O . HOH T . ? 0.3759 0.4154 0.3487 -0.0059 -0.0059 0.0136 520 HOH B O 6647 O O . HOH T . ? 0.5499 0.5775 0.5246 -0.0087 0.0063 0.0006 521 HOH B O 6648 O O . HOH T . ? 0.2028 0.2026 0.2081 -0.0063 -0.0034 -0.0018 522 HOH B O 6649 O O . HOH T . ? 0.2465 0.2148 0.2499 -0.0079 0.0050 0.0132 523 HOH B O 6650 O O . HOH T . ? 0.1456 0.1283 0.1496 -0.0119 0.0030 0.0067 524 HOH B O 6651 O O . HOH T . ? 0.1911 0.1637 0.1828 -0.0011 0.0041 -0.0033 525 HOH B O 6652 O O . HOH T . ? 0.4686 0.4212 0.4586 -0.0039 0.0148 -0.0092 526 HOH B O 6653 O O . HOH T . ? 0.1770 0.2166 0.1874 0.0057 0.0038 0.0023 527 HOH B O 6654 O O . HOH T . ? 0.1820 0.1563 0.1739 0.0046 0.0081 -0.0037 528 HOH B O 6655 O O . HOH T . ? 0.3859 0.4158 0.3602 -0.0079 -0.0035 0.0069 529 HOH B O 6656 O O . HOH T . ? 0.5334 0.5603 0.5190 -0.0165 -0.0069 -0.0099 530 HOH B O 6657 O O . HOH T . ? 0.1644 0.1499 0.1570 -0.0009 -0.0012 0.0006 531 HOH B O 6658 O O . HOH T . ? 0.4667 0.4890 0.4490 -0.0064 0.0082 0.0012 532 HOH B O 6659 O O . HOH T . ? 0.1490 0.1484 0.1539 -0.0055 -0.0040 -0.0025 533 HOH B O 6660 O O . HOH T . ? 0.2186 0.2418 0.1942 -0.0085 -0.0012 0.0030 534 HOH B O 6661 O O . HOH T . ? 0.1319 0.1256 0.1340 -0.0034 -0.0032 0.0027 535 HOH B O 6662 O O . HOH T . ? 0.5579 0.5259 0.5446 -0.0076 0.0118 -0.0157 536 HOH B O 6663 O O . HOH T . ? 0.3991 0.3904 0.4009 -0.0002 -0.0055 -0.0005 537 HOH B O 6664 O O . HOH T . ? 0.1483 0.1771 0.1321 -0.0150 -0.0074 -0.0079 538 HOH B O 6665 O O . HOH T . ? 0.1805 0.1918 0.1768 -0.0080 -0.0085 -0.0010 539 HOH B O 6666 O O . HOH T . ? 0.3775 0.4165 0.3602 -0.0032 -0.0112 0.0119 540 HOH B O 6667 O O . HOH T . ? 0.4497 0.4624 0.4498 -0.0116 0.0057 0.0073 541 HOH B O 6668 O O . HOH T . ? 0.4887 0.4650 0.4886 0.0026 -0.0011 0.0190 542 HOH B O 6669 O O . HOH T . ? 0.2200 0.2072 0.2135 -0.0111 0.0079 0.0242 543 HOH B O 6670 O O . HOH T . ? 0.4816 0.4591 0.4786 -0.0114 0.0089 0.0235 544 HOH B O 6671 O O . HOH T . ? 0.2256 0.2350 0.2115 -0.0025 0.0073 -0.0036 545 HOH B O 6672 O O . HOH T . ? 0.1562 0.1723 0.1345 -0.0076 0.0004 0.0015 546 HOH B O 6673 O O . HOH T . ? 0.5619 0.5142 0.5527 -0.0036 0.0138 -0.0063 547 HOH B O 6674 O O . HOH T . ? 0.2272 0.2437 0.2289 0.0009 0.0039 0.0023 548 HOH B O 6675 O O . HOH T . ? 0.4304 0.3784 0.4452 0.0052 0.0099 0.0022 549 HOH B O 6676 O O . HOH T . ? 0.3980 0.3967 0.3814 -0.0041 0.0060 0.0368 550 HOH B O 6677 O O . HOH T . ? 0.5221 0.5359 0.5180 -0.0113 -0.0077 -0.0041 551 HOH B O 6678 O O . HOH T . ? 0.2716 0.3037 0.2488 0.0033 -0.0060 0.0325 552 HOH B O 6679 O O . HOH T . ? 0.4640 0.4979 0.4436 0.0064 -0.0075 0.0349 553 HOH B O 6680 O O . HOH T . ? 0.5184 0.5033 0.5129 0.0020 -0.0014 0.0239 554 HOH B O 6681 O O . HOH T . ? 0.3585 0.3897 0.3492 0.0069 -0.0118 0.0233 555 HOH B O 6682 O O . HOH T . ? 0.1926 0.1872 0.1941 0.0082 -0.0074 0.0168 556 HOH B O 6683 O O . HOH T . ? 0.5632 0.5940 0.5389 0.0017 -0.0045 0.0325 557 HOH B O 6684 O O . HOH T . ? 0.2057 0.1623 0.2180 -0.0049 0.0076 -0.0054 558 HOH B O 6685 O O . HOH T . ? 0.2804 0.2843 0.2683 -0.0107 0.0066 0.0218 559 HOH B O 6686 O O . HOH T . ? 0.2297 0.2194 0.2183 -0.0046 0.0053 0.0315 560 HOH B O 6687 O O . HOH T . ? 0.4150 0.4398 0.4246 -0.0171 0.0059 0.0016 561 HOH B O 6688 O O . HOH T . ? 0.4295 0.4105 0.4181 -0.0159 0.0047 -0.0149 562 HOH B O 6689 O O . HOH T . ? 0.2083 0.1743 0.2176 -0.0184 0.0100 0.0032 563 HOH B O 6690 O O . HOH T . ? 0.3512 0.3395 0.3384 -0.0006 0.0078 -0.0086 564 HOH B O 6691 O O . HOH T . ? 0.4313 0.3942 0.4194 -0.0007 0.0152 -0.0134 565 HOH B O 6692 O O . HOH T . ? 0.1538 0.1516 0.1458 -0.0004 -0.0067 0.0118 566 HOH B O 6693 O O . HOH T . ? 0.3238 0.2729 0.3324 -0.0133 0.0140 0.0120 567 HOH B O 6694 O O . HOH T . ? 0.2286 0.2249 0.2155 0.0016 0.0007 0.0335 568 HOH B O 6695 O O . HOH T . ? 0.5447 0.5749 0.5308 -0.0133 -0.0088 -0.0053 569 HOH B O 6696 O O . HOH T . ? 0.2915 0.2939 0.2722 -0.0102 0.0024 -0.0111 570 HOH B O 6697 O O . HOH T . ? 0.4126 0.3774 0.4080 0.0161 0.0126 0.0058 571 HOH B O 6698 O O . HOH T . ? 0.4414 0.4188 0.4382 0.0149 0.0079 0.0057 572 HOH B O 6699 O O . HOH T . ? 0.5528 0.5571 0.5349 -0.0090 0.0089 0.0348 573 HOH B O 6700 O O . HOH T . ? 0.3531 0.3500 0.3383 -0.0031 0.0058 -0.0071 574 HOH B O 6701 O O . HOH T . ? 0.2882 0.3082 0.2723 -0.0068 0.0071 0.0042 575 HOH B O 6702 O O . HOH T . ? 0.5502 0.5215 0.5461 0.0152 0.0086 0.0081 576 HOH B O 6703 O O . HOH T . ? 0.3784 0.3736 0.3786 0.0034 -0.0039 0.0039 577 HOH B O 6704 O O . HOH T . ? 0.5468 0.5482 0.5515 -0.0176 0.0065 0.0067 578 HOH B O 6705 O O . HOH T . ? 0.3946 0.3526 0.3867 0.0018 0.0106 -0.0015 579 HOH B O 6706 O O . HOH T . ? 0.4609 0.4580 0.4557 -0.0144 -0.0028 -0.0079 580 HOH B O 6707 O O . HOH T . ? 0.2054 0.2276 0.1808 -0.0027 0.0004 0.0312 581 HOH B O 6708 O O . HOH T . ? 0.3147 0.3099 0.3145 0.0051 -0.0029 0.0046 582 HOH B O 6709 O O . HOH T . ? 0.5460 0.5356 0.5312 -0.0181 0.0044 -0.0188 583 HOH B O 6710 O O . HOH T . ? 0.3617 0.3697 0.3629 0.0095 0.0046 0.0025 584 HOH B O 6711 O O . HOH T . ? 0.2277 0.2001 0.2284 -0.0013 0.0011 0.0168 585 HOH B O 6712 O O . HOH T . ? 0.5093 0.5002 0.5081 0.0124 0.0017 0.0072 586 HOH B O 6713 O O . HOH T . ? 0.1789 0.1814 0.1812 0.0015 -0.0048 0.0021 587 HOH B O 6714 O O . HOH T . ? 0.2203 0.2308 0.2078 -0.0172 -0.0036 -0.0124 588 HOH B O 6715 O O . HOH T . ? 0.2985 0.2773 0.2944 0.0036 -0.0009 0.0045 589 HOH B O 6716 O O . HOH T . ? 0.5422 0.5133 0.5357 0.0103 0.0123 -0.0028 590 HOH B O 6717 O O . HOH T . ? 0.4641 0.4914 0.4642 0.0062 -0.0125 0.0150 591 HOH B O 6718 O O . HOH T . ? 0.2747 0.2523 0.2669 -0.0115 0.0026 -0.0080 592 HOH B O 6719 O O . HOH T . ? 0.2101 0.2194 0.1934 -0.0060 0.0005 0.0125 593 HOH B O 6720 O O . HOH T . ? 0.5784 0.5561 0.5917 -0.0286 0.0122 -0.0049 594 HOH B O 6721 O O . HOH T . ? 0.2666 0.2310 0.2596 0.0067 0.0098 -0.0003 595 HOH B O 6722 O O . HOH T . ? 0.4228 0.4284 0.4311 -0.0195 0.0059 0.0024 596 HOH B O 6723 O O . HOH T . ? 0.2929 0.3079 0.2834 -0.0014 0.0081 -0.0010 597 HOH B O 6724 O O . HOH T . ? 0.2855 0.2704 0.2823 -0.0073 -0.0022 -0.0015 598 HOH B O 6725 O O . HOH T . ? 0.2293 0.2025 0.2294 -0.0047 0.0028 0.0170 599 HOH B O 6726 O O . HOH T . ? 0.4313 0.4228 0.4122 -0.0126 0.0074 -0.0190 600 HOH B O 6727 O O . HOH T . ? 0.2003 0.1757 0.1993 -0.0023 0.0010 0.0177 603 HOH B O 6728 O O . HOH T . ? 0.2921 0.3114 0.2803 -0.0102 0.0078 0.0108 604 HOH B O 6729 O O . HOH T . ? 0.3100 0.3102 0.3127 0.0122 -0.0077 0.0213 605 HOH B O 6730 O O . HOH T . ? 0.4473 0.4262 0.4580 -0.0144 0.0039 -0.0143 606 HOH B O 6731 O O . HOH T . ? 0.4822 0.5034 0.4843 -0.0001 0.0051 0.0021 607 HOH B O 6732 O O . HOH T . ? 0.3933 0.3669 0.3819 -0.0083 0.0061 -0.0108 608 HOH B O 6733 O O . HOH T . ? 0.2979 0.2681 0.2924 0.0075 0.0053 0.0045 609 HOH B O 6734 O O . HOH T . ? 0.2591 0.2516 0.2463 0.0002 0.0030 0.0352 610 HOH B O 6735 O O . HOH T . ? 0.4205 0.3981 0.4200 -0.0133 0.0088 0.0193 611 HOH B O 6736 O O . HOH T . ? 0.2338 0.2122 0.2390 -0.0143 0.0055 0.0073 612 HOH B O 6737 O O . HOH T . ? 0.3509 0.3458 0.3548 -0.0038 -0.0046 -0.0023 613 HOH B O 6738 O O . HOH T . ? 0.2817 0.2565 0.2867 0.0043 -0.0027 0.0102 614 HOH B O 6739 O O . HOH T . ? 0.2998 0.2681 0.2919 -0.0036 0.0049 -0.0034 615 HOH B O 6740 O O . HOH T . ? 0.2634 0.2521 0.2680 -0.0188 0.0081 0.0090 616 HOH B O 6741 O O . HOH T . ? 0.2785 0.2702 0.2801 -0.0024 -0.0038 0.0027 617 HOH B O 6742 O O . HOH T . ? 0.2368 0.2257 0.2296 -0.0013 -0.0020 0.0022 618 HOH B O 6743 O O . HOH T . ? 0.5270 0.5618 0.5002 -0.0106 -0.0042 0.0006 619 HOH B O 6744 O O . HOH T . ? 0.5717 0.5748 0.5732 0.0024 -0.0054 0.0021 620 HOH B O 6745 O O . HOH T . ? 0.4302 0.4242 0.4424 -0.0237 0.0058 -0.0075 621 HOH B O 6746 O O . HOH T . ? 0.4173 0.3793 0.4047 -0.0077 0.0137 -0.0158 622 HOH B O 6747 O O . HOH T . ? 0.5224 0.5362 0.5129 -0.0106 -0.0076 -0.0036 623 HOH B O 6748 O O . HOH T . ? 0.3069 0.3077 0.2902 -0.0066 0.0068 0.0340 624 HOH B O 6749 O O . HOH T . ? 0.5597 0.5062 0.5696 0.0036 0.0099 0.0163 625 HOH B O 6750 O O . HOH T . ? 0.3082 0.3354 0.2847 -0.0009 -0.0042 0.0265 626 HOH B O 6751 O O . HOH T . ? 0.3120 0.3162 0.3221 -0.0178 0.0001 -0.0169 627 HOH B O 6752 O O . HOH T . ? 0.3618 0.3616 0.3530 0.0064 -0.0046 0.0289 628 HOH B O 6753 O O . HOH T . ? 0.3477 0.3733 0.3244 -0.0078 0.0078 -0.0018 629 HOH B O 6754 O O . HOH T . ? 0.2575 0.2754 0.2554 -0.0084 0.0063 0.0060 630 HOH B O 6755 O O . HOH T . ? 0.1964 0.1804 0.1943 -0.0003 -0.0053 0.0030 631 HOH B O 6756 O O . HOH T . ? 0.3466 0.3811 0.3174 -0.0085 0.0002 0.0104 632 HOH B O 6757 O O . HOH T . ? 0.2672 0.2748 0.2692 0.0097 0.0028 0.0037 633 HOH B O 6758 O O . HOH T . ? 0.3924 0.3699 0.4011 -0.0189 0.0074 0.0019 634 HOH B O 6759 O O . HOH T . ? 0.2715 0.2967 0.2762 -0.0010 0.0045 0.0022 635 HOH B O 6760 O O . HOH T . ? 0.2966 0.2743 0.2921 -0.0040 -0.0007 0.0004 636 HOH B O 6761 O O . HOH T . ? 0.2426 0.2627 0.2359 -0.0065 -0.0102 0.0018 637 HOH B O 6762 O O . HOH T . ? 0.3207 0.3233 0.3092 0.0053 -0.0039 0.0306 638 HOH B O 6763 O O . HOH T . ? 0.2752 0.2995 0.2728 0.0019 -0.0121 0.0111 639 HOH B O 6764 O O . HOH T . ? 0.3121 0.3192 0.3081 0.0044 0.0068 -0.0008 640 HOH B O 6765 O O . HOH T . ? 0.4696 0.4972 0.4453 -0.0088 0.0059 0.0053 641 HOH B O 6766 O O . HOH T . ? 0.4145 0.4506 0.3889 -0.0011 -0.0057 0.0255 642 HOH B O 6767 O O . HOH T . ? 0.5684 0.5558 0.5667 0.0033 -0.0043 0.0043 643 HOH B O 6768 O O . HOH T . ? 0.4581 0.4621 0.4489 -0.0175 -0.0027 -0.0121 644 HOH B O 6769 O O . HOH T . ? 0.2659 0.2528 0.2550 -0.0020 0.0049 0.0340 645 HOH B O 6770 O O . HOH T . ? 0.4670 0.4658 0.4562 -0.0114 0.0077 0.0242 646 HOH B O 6771 O O . HOH T . ? 0.4771 0.4679 0.4770 0.0192 0.0094 0.0049 648 HOH B O 6772 O O . HOH T . ? 0.4505 0.4414 0.4525 0.0115 -0.0055 0.0226 650 HOH B O 6773 O O . HOH T . ? 0.2837 0.2697 0.2805 -0.0016 -0.0043 0.0083 651 HOH B O 6774 O O . HOH T . ? 0.2002 0.1829 0.1949 0.0024 -0.0001 0.0017 652 HOH B O 6775 O O . HOH T . ? 0.3072 0.2986 0.2933 -0.0044 0.0029 -0.0063 653 HOH B O 6776 O O . HOH T . ? 0.2847 0.3215 0.2691 0.0053 -0.0110 0.0260 654 HOH B O 6777 O O . HOH T . ? 0.2781 0.2873 0.2802 0.0129 -0.0092 0.0224 655 HOH B O 6778 O O . HOH T . ? 0.5122 0.5107 0.4958 -0.0060 0.0024 -0.0061 656 HOH B O 6779 O O . HOH T . ? 0.2510 0.2255 0.2528 0.0007 -0.0014 0.0134 657 HOH B O 6780 O O . HOH T . ? 0.3004 0.2996 0.3019 0.0022 -0.0042 0.0030 658 HOH B O 6781 O O . HOH T . ? 0.3334 0.3688 0.3037 -0.0081 0.0014 0.0158 659 HOH B O 6782 O O . HOH T . ? 0.2760 0.2685 0.2654 0.0014 0.0070 -0.0055 660 HOH B O 6783 O O . HOH T . ? 0.5797 0.5708 0.5644 -0.0049 0.0052 -0.0094 661 HOH B O 6784 O O . HOH T . ? 0.3772 0.3704 0.3714 0.0004 -0.0063 0.0125 662 HOH B O 6785 O O . HOH T . ? 0.5204 0.5017 0.5123 -0.0020 0.0051 0.0321 663 HOH B O 6786 O O . HOH T . ? 0.4816 0.5030 0.4567 -0.0113 -0.0002 -0.0062 664 HOH B O 6787 O O . HOH T . ? 0.2328 0.2096 0.2405 -0.0077 0.0005 -0.0044 665 HOH B O 6788 O O . HOH T . ? 0.3162 0.3332 0.3277 -0.0217 0.0059 -0.0010 666 HOH B O 6789 O O . HOH T . ? 0.5468 0.5416 0.5366 -0.0189 0.0007 -0.0149 667 HOH B O 6790 O O . HOH T . ? 0.4512 0.4550 0.4327 -0.0076 0.0018 -0.0064 668 HOH B O 6791 O O . HOH T . ? 0.3275 0.2956 0.3207 0.0083 0.0103 -0.0013 669 HOH B O 6792 O O . HOH T . ? 0.3801 0.3616 0.3770 0.0011 -0.0034 0.0034 670 HOH B O 6793 O O . HOH T . ? 0.5443 0.5651 0.5478 0.0098 -0.0114 0.0168 671 HOH B O 6794 O O . HOH T . ? 0.4745 0.5070 0.4486 -0.0126 -0.0038 -0.0044 672 HOH B O 6795 O O . HOH T . ? 0.5532 0.5649 0.5420 -0.0221 -0.0022 -0.0169 673 HOH B O 6796 O O . HOH T . ? 0.2078 0.1839 0.2081 -0.0067 0.0027 0.0145 674 HOH B O 6797 O O . HOH T . ? 0.3414 0.3251 0.3398 0.0188 0.0115 0.0033 675 HOH B O 6798 O O . HOH T . ? 0.2359 0.2179 0.2329 0.0001 -0.0023 0.0171 676 HOH B O 6799 O O . HOH T . ? 0.3303 0.3454 0.3110 0.0023 -0.0025 0.0335 677 HOH B O 6800 O O . HOH T . ? 0.4952 0.5026 0.5059 -0.0215 0.0055 -0.0014 678 HOH B O 6801 O O . HOH T . ? 0.3329 0.3146 0.3398 -0.0161 0.0052 0.0035 679 HOH B O 6802 O O . HOH T . ? 0.2615 0.2466 0.2606 -0.0001 -0.0055 0.0029 680 HOH B O 6803 O O . HOH T . ? 0.2816 0.2961 0.2625 -0.0170 -0.0018 -0.0145 681 HOH B O 6804 O O . HOH T . ? 0.4597 0.4407 0.4536 -0.0142 0.0022 -0.0083 682 HOH B O 6805 O O . HOH T . ? 0.3266 0.3370 0.3144 -0.0108 0.0065 0.0169 683 HOH B O 6806 O O . HOH T . ? 0.5011 0.4793 0.4896 0.0017 0.0113 -0.0104 685 HOH B O 6807 O O . HOH T . ? 0.4971 0.4780 0.4905 -0.0099 0.0094 0.0287 686 HOH B O 6808 O O . HOH T . ? 0.4674 0.4844 0.4586 -0.0080 -0.0091 0.0000 687 HOH B O 6809 O O . HOH T . ? 0.5343 0.5176 0.5177 -0.0097 0.0085 -0.0170 688 HOH B O 6810 O O . HOH T . ? 0.2444 0.2386 0.2322 -0.0010 0.0052 -0.0050 689 HOH B O 6811 O O . HOH T . ? 0.3652 0.3251 0.3712 0.0019 0.0043 0.0158 690 HOH B O 6812 O O . HOH T . ? 0.2929 0.3254 0.2686 -0.0128 -0.0050 -0.0047 691 HOH B O 6813 O O . HOH T . ? 0.5044 0.4876 0.5075 -0.0048 -0.0026 0.0030 692 HOH B O 6814 O O . HOH T . ? 0.2894 0.3003 0.2770 -0.0010 0.0088 -0.0042 693 HOH B O 6815 O O . HOH T . ? 0.4029 0.4237 0.3904 -0.0124 -0.0077 -0.0051 694 HOH B O 6816 O O . HOH T . ? 0.3527 0.3114 0.3651 -0.0117 0.0088 -0.0085 695 HOH B O 6817 O O . HOH T . ? 0.3968 0.4124 0.3892 0.0103 -0.0087 0.0291 696 HOH B O 6818 O O . HOH T . ? 0.5555 0.4985 0.5724 0.0006 0.0139 -0.0072 697 HOH B O 6819 O O . HOH T . ? 0.4177 0.4438 0.3910 -0.0095 0.0024 -0.0004 698 HOH B O 6820 O O . HOH T . ? 0.3226 0.3174 0.3095 -0.0030 0.0029 -0.0037 699 HOH B O 6821 O O . HOH T . ? 0.3823 0.3466 0.3763 0.0103 0.0105 0.0025 700 HOH B O 6822 O O . HOH T . ? 0.5794 0.6046 0.5669 0.0106 -0.0087 0.0340 701 HOH B O 6823 O O . HOH T . ? 0.2792 0.2730 0.2860 -0.0184 0.0059 0.0041 702 HOH B O 6824 O O . HOH T . ? 0.2578 0.2314 0.2608 -0.0005 -0.0014 0.0102 703 HOH B O 6825 O O . HOH T . ? 0.4303 0.4395 0.4222 0.0087 -0.0074 0.0283 704 HOH B O 6826 O O . HOH T . ? 0.2818 0.3142 0.2572 -0.0140 0.0123 0.0257 705 HOH B O 6827 O O . HOH T . ? 0.3460 0.3371 0.3404 0.0023 -0.0049 0.0184 706 HOH B O 6828 O O . HOH T . ? 0.3109 0.3309 0.3155 -0.0098 0.0046 0.0037 707 HOH B O 6829 O O . HOH T . ? 0.4060 0.3818 0.4097 0.0050 -0.0027 0.0136 708 HOH B O 6830 O O . HOH T . ? 0.3689 0.3981 0.3446 -0.0151 -0.0035 -0.0097 709 HOH B O 6831 O O . HOH T . ? 0.3762 0.3462 0.3676 -0.0065 0.0050 -0.0062 710 HOH B O 6832 O O . HOH T . ? 0.3772 0.3733 0.3701 0.0013 -0.0062 0.0158 711 HOH B O 6833 O O . HOH T . ? 0.3812 0.3609 0.3755 -0.0088 0.0002 -0.0040 712 HOH B O 6834 O O . HOH T . ? 0.3716 0.3782 0.3548 0.0029 -0.0007 0.0361 713 HOH B O 6835 O O . HOH T . ? 0.4675 0.4104 0.4815 -0.0165 0.0164 -0.0023 714 HOH B O 6836 O O . HOH T . ? 0.4923 0.5194 0.4912 -0.0081 0.0085 0.0046 715 HOH B O 6837 O O . HOH T . ? 0.4686 0.4071 0.4799 -0.0051 0.0148 0.0113 716 HOH B O 6838 O O . HOH T . ? 0.4830 0.4831 0.4848 0.0007 -0.0055 0.0008 717 HOH B O 6839 O O . HOH T . ? 0.2923 0.3286 0.2772 -0.0119 -0.0099 -0.0026 718 HOH B O 6840 O O . HOH T . ? 0.2666 0.2562 0.2686 -0.0029 -0.0040 0.0022 719 HOH B O 6841 O O . HOH T . ? 0.4552 0.4377 0.4519 0.0057 -0.0011 0.0053 720 HOH B O 6842 O O . HOH T . ? 0.4052 0.4205 0.3915 -0.0111 0.0073 0.0159 721 HOH B O 6843 O O . HOH T . ? 0.4984 0.4670 0.4931 0.0106 0.0081 0.0045 722 HOH B O 6844 O O . HOH T . ? 0.4984 0.5052 0.4922 -0.0094 -0.0071 -0.0028 723 HOH B O 6845 O O . HOH T . ? 0.5086 0.5297 0.4938 -0.0117 0.0088 0.0149 724 HOH B O 6846 O O . HOH T . ? 0.4253 0.4503 0.4274 0.0058 -0.0122 0.0131 725 HOH B O 6847 O O . HOH T . ? 0.5037 0.5035 0.5031 -0.0153 0.0071 0.0123 726 HOH B O 6848 O O . HOH T . ? 0.4422 0.4334 0.4451 0.0106 -0.0061 0.0195 727 HOH B O 6849 O O . HOH T . ? 0.4182 0.3863 0.4058 -0.0041 0.0114 -0.0129 728 HOH B O 6850 O O . HOH T . ? 0.4334 0.4067 0.4204 -0.0020 0.0119 -0.0132 729 HOH B O 6851 O O . HOH T . ? 0.4806 0.4450 0.4871 0.0081 0.0022 0.0189 730 HOH B O 6852 O O . HOH T . ? 0.4888 0.5189 0.4718 0.0087 -0.0081 0.0354 731 HOH B O 6853 O O . HOH T . ? 0.4582 0.4334 0.4542 0.0144 0.0105 0.0023 732 HOH B O 6854 O O . HOH T . ? 0.3810 0.4282 0.3583 -0.0005 -0.0105 0.0207 733 HOH B O 6855 O O . HOH T . ? 0.5279 0.5359 0.5343 -0.0174 0.0058 0.0043 734 HOH B O 6856 O O . HOH T . ? 0.6135 0.6483 0.5989 0.0085 -0.0103 0.0312 735 HOH B O 6857 O O . HOH T . ? 0.4758 0.4520 0.4719 0.0121 0.0050 0.0075 736 HOH B O 6858 O O . HOH T . ? 0.5075 0.5001 0.5062 0.0113 -0.0002 0.0080 737 HOH B O 6859 O O . HOH T . ? 0.5689 0.5274 0.5771 -0.0158 0.0116 0.0086 738 HOH B O 6860 O O . HOH T . ? 0.4020 0.4350 0.3744 -0.0096 0.0054 0.0116 739 HOH B O 6861 O O . HOH T . ? 0.4346 0.3863 0.4205 -0.0172 0.0209 -0.0257 741 HOH B O 6862 O O . HOH T . ? 0.2807 0.2512 0.2751 0.0076 0.0060 0.0032 742 HOH B O 6863 O O . HOH T . ? 0.4756 0.4599 0.4600 -0.0055 0.0089 -0.0142 743 HOH B O 6864 O O . HOH T . ? 0.3489 0.3245 0.3464 -0.0044 0.0037 0.0216 744 HOH B O 6865 O O . HOH T . ? 0.5269 0.5014 0.5221 -0.0018 0.0006 0.0021 745 HOH B O 6866 O O . HOH T . ? 0.4317 0.4608 0.4053 -0.0031 -0.0015 0.0273 746 HOH B O 6867 O O . HOH T . ? 0.4449 0.4477 0.4437 0.0123 -0.0074 0.0265 747 HOH B O 6868 O O . HOH T . ? 0.4634 0.4877 0.4503 -0.0081 0.0089 0.0060 748 HOH B O 6869 O O . HOH T . ? 0.3731 0.3817 0.3662 0.0070 -0.0083 0.0235 749 HOH B O 6870 O O . HOH T . ? 0.6083 0.5864 0.5942 -0.0147 0.0077 -0.0179 750 HOH B O 6871 O O . HOH T . ? 0.2769 0.2625 0.2722 0.0010 -0.0026 0.0196 751 HOH B O 6872 O O . HOH T . ? 0.4967 0.5272 0.4987 -0.0096 0.0087 0.0044 752 HOH B O 6873 O O . HOH T . ? 0.5719 0.6199 0.5468 -0.0009 -0.0094 0.0221 753 HOH B O 6874 O O . HOH T . ? 0.4938 0.4719 0.4791 -0.0039 0.0116 -0.0153 755 HOH B O 6875 O O . HOH T . ? 0.4387 0.4868 0.4166 0.0029 -0.0106 0.0268 756 HOH B O 6876 O O . HOH T . ? 0.5451 0.5309 0.5563 -0.0223 0.0068 -0.0046 757 HOH B O 6877 O O . HOH T . ? 0.5572 0.5173 0.5519 0.0151 0.0133 0.0068 758 HOH B O 6878 O O . HOH T . ? 0.4174 0.4278 0.4143 0.0109 -0.0089 0.0252 759 HOH B O 6879 O O . HOH T . ? 0.5819 0.5572 0.5729 -0.0132 0.0047 -0.0107 760 HOH B O 6880 O O . HOH T . ? 0.4888 0.4294 0.4816 0.0128 0.0228 0.0006 761 HOH B O 6881 O O . HOH T . ? 0.3614 0.3403 0.3615 0.0012 -0.0031 0.0136 762 HOH B O 6882 O O . HOH T . ? 0.5642 0.5539 0.5486 -0.0229 0.0068 -0.0243 763 HOH B O 6883 O O . HOH T . ? 0.4181 0.3759 0.4118 0.0118 0.0137 0.0032 764 HOH B O 6884 O O . HOH T . ? 0.4724 0.4464 0.4683 0.0129 0.0071 0.0059 765 HOH B O 6885 O O . HOH T . ? 0.5260 0.5617 0.4991 -0.0128 0.0109 0.0236 766 HOH B O 6886 O O . HOH T . ? 0.5389 0.5348 0.5389 0.0151 0.0021 0.0085 767 HOH B O 6887 O O . HOH T . ? 0.4713 0.4971 0.4489 -0.0100 0.0068 0.0158 768 HOH B O 6888 O O . HOH T . ? 0.4766 0.4739 0.4725 -0.0111 -0.0044 -0.0047 769 HOH B O 6889 O O . HOH T . ? 0.3040 0.2784 0.3047 0.0004 -0.0006 0.0161 770 HOH B O 6890 O O . HOH T . ? 0.5445 0.5816 0.5140 -0.0096 0.0059 0.0224 771 HOH B O 6891 O O . HOH T . ? 0.5160 0.4903 0.5106 -0.0055 0.0014 -0.0011 772 HOH B O 6892 O O . HOH T . ? 0.5719 0.6019 0.5462 -0.0112 0.0086 0.0238 773 HOH B O 6893 O O . HOH T . ? 0.4582 0.4752 0.4590 0.0063 0.0070 0.0006 774 HOH B O 6894 O O . HOH T . ? 0.5575 0.5831 0.5311 -0.0155 -0.0001 -0.0131 775 HOH B O 6895 O O . HOH T . ? 0.5230 0.4930 0.5181 0.0117 0.0069 0.0078 776 HOH B O 6896 O O . HOH T . ? 0.4432 0.4276 0.4392 -0.0096 -0.0011 -0.0035 777 HOH B O 6897 O O . HOH T . ? 0.3991 0.3586 0.3872 -0.0041 0.0149 -0.0138 778 HOH B O 6898 O O . HOH T . ? 0.5778 0.5679 0.5736 0.0115 0.0102 -0.0020 779 HOH B O 6899 O O . HOH T . ? 0.3564 0.3547 0.3542 0.0064 0.0035 0.0017 780 HOH B O 6900 O O . HOH T . ? 0.4949 0.4796 0.4940 0.0007 -0.0054 0.0030 781 HOH B O 6901 O O . HOH T . ? 0.4831 0.4755 0.4785 0.0024 -0.0063 0.0155 782 HOH B O 6902 O O . HOH T . ? 0.2564 0.2769 0.2409 -0.0178 -0.0048 -0.0127 783 HOH B O 6903 O O . HOH T . ? 0.4551 0.4323 0.4484 -0.0113 0.0024 -0.0065 784 HOH B O 6904 O O . HOH T . ? 0.4464 0.4496 0.4473 0.0000 -0.0060 0.0000 785 HOH B O 6905 O O . HOH T . ? 0.3530 0.3910 0.3395 -0.0060 -0.0118 0.0056 786 HOH B O 6906 O O . HOH T . ? 0.5025 0.4849 0.4920 -0.0188 0.0049 -0.0163 787 HOH B O 6907 O O . HOH T . ? 0.4921 0.4873 0.4772 -0.0044 0.0037 -0.0064 788 HOH B O 6908 O O . HOH T . ? 0.4377 0.4500 0.4162 -0.0225 0.0027 -0.0240 789 HOH B O 6909 O O . HOH T . ? 0.3351 0.3538 0.3420 -0.0144 0.0051 0.0031 790 HOH B O 6910 O O . HOH T . ? 0.2907 0.2753 0.2741 -0.0140 0.0074 -0.0191 791 HOH B O 6911 O O . HOH T . ? 0.5358 0.4962 0.5257 -0.0051 0.0111 -0.0093 792 HOH B O 6912 O O . HOH T . ? 0.6529 0.6377 0.6343 -0.0104 0.0113 -0.0210 793 HOH B O 6913 O O . HOH T . ? 0.3645 0.3567 0.3641 0.0029 -0.0049 0.0035 794 HOH B O 6914 O O . HOH T . ? 0.4408 0.4455 0.4280 -0.0010 0.0075 -0.0047 795 HOH B O 6915 O O . HOH T . ? 0.3993 0.3911 0.3919 0.0036 -0.0030 0.0256 796 HOH B O 6916 O O . HOH T . ? 0.5297 0.5160 0.5277 0.0022 -0.0055 0.0134 797 HOH B O 6917 O O . HOH T . ? 0.4642 0.4307 0.4534 -0.0019 0.0106 -0.0096 798 HOH B O 6918 O O . HOH T . ? 0.5420 0.5158 0.5294 0.0008 0.0142 -0.0138 799 HOH B O 6919 O O . HOH T . ? 0.4032 0.4236 0.3867 0.0080 -0.0058 0.0365 800 HOH B O 6920 O O . HOH T . ? 0.4756 0.4957 0.4509 -0.0164 0.0007 -0.0158 801 HOH B O 6921 O O . HOH T . ? 0.4420 0.4556 0.4177 -0.0159 0.0032 -0.0181 802 HOH B O 6922 O O . HOH T . ? 0.3076 0.3058 0.3082 0.0139 0.0033 0.0060 803 HOH B O 6923 O O . HOH T . ? 0.5114 0.5215 0.5042 -0.0126 -0.0065 -0.0060 804 HOH B O 6924 O O . HOH T . ? 0.3977 0.3484 0.4124 -0.0008 0.0103 -0.0065 805 HOH B O 6925 O O . HOH T . ? 0.5277 0.5145 0.5240 0.0014 -0.0045 0.0157 806 HOH B O 6926 O O . HOH T . ? 0.4678 0.4409 0.4665 -0.0030 0.0032 0.0210 807 HOH B O 6927 O O . HOH T . ? 0.3748 0.3592 0.3720 0.0041 -0.0027 0.0046 808 HOH B O 6928 O O . HOH T . ? 0.4864 0.4890 0.4886 0.0000 -0.0057 0.0000 809 HOH B O 6929 O O . HOH T . ? 0.5327 0.5226 0.5298 -0.0094 -0.0029 -0.0031 810 HOH B O 6930 O O . HOH T . ? 0.4906 0.5084 0.4901 -0.0012 0.0054 0.0023 811 HOH B O 6931 O O . HOH T . ? 0.4592 0.4957 0.4289 -0.0092 0.0030 0.0122 813 HOH B O 6932 O O . HOH T . ? 0.5055 0.4948 0.5055 -0.0023 -0.0035 0.0042 814 HOH B O 6933 O O . HOH T . ? 0.2937 0.2736 0.2904 0.0000 -0.0021 0.0036 815 HOH B O 6934 O O . HOH T . ? 0.5365 0.4996 0.5194 -0.0217 0.0198 -0.0323 816 HOH B O 6935 O O . HOH T . ? 0.4802 0.5060 0.4619 -0.0143 0.0117 0.0211 817 HOH B O 6936 O O . HOH T . ? 0.5888 0.5846 0.5681 -0.0220 0.0085 -0.0281 818 HOH B O 6937 O O . HOH T . ? 0.3701 0.3798 0.3506 -0.0074 0.0060 0.0310 819 HOH B O 6938 O O . HOH T . ? 0.5583 0.5818 0.5334 -0.0057 0.0014 0.0247 820 HOH B O 6939 O O . HOH T . ? 0.5310 0.5282 0.5154 -0.0212 0.0035 -0.0212 821 HOH B O 6940 O O . HOH T . ? 0.5220 0.5119 0.5199 0.0146 0.0092 0.0013 822 HOH B O 6941 O O . HOH T . ? 0.5155 0.5421 0.4985 -0.0167 0.0139 0.0230 823 HOH B O 6942 O O . HOH T . ? 0.5605 0.5580 0.5620 0.0001 -0.0057 -0.0012 824 HOH B O 6943 O O . HOH T . ? 0.4043 0.4220 0.4018 0.0114 -0.0103 0.0248 825 HOH B O 6944 O O . HOH T . ? 0.5671 0.6070 0.5406 -0.0149 0.0137 0.0239 826 HOH B O 6945 O O . HOH T . ? 0.4196 0.4076 0.4069 -0.0165 0.0031 -0.0157 827 HOH B O 6946 O O . HOH T . ? 0.4640 0.4882 0.4681 0.0052 0.0057 0.0017 828 HOH B O 6947 O O . HOH T . ? 0.5800 0.5931 0.5809 0.0147 -0.0093 0.0263 829 HOH B O 6948 O O . HOH T . ? 0.5049 0.4970 0.5024 0.0091 -0.0050 0.0253 831 HOH B O 6949 O O . HOH T . ? 0.5430 0.5228 0.5419 0.0226 0.0146 0.0041 832 HOH B O 6950 O O . HOH T . ? 0.5165 0.4713 0.5278 0.0070 0.0059 0.0110 833 HOH B O 6951 O O . HOH T . ? 0.5360 0.5751 0.5050 -0.0099 0.0053 0.0153 835 HOH B O 6952 O O . HOH T . ? 0.5668 0.5926 0.5699 0.0023 -0.0120 0.0085 838 HOH B O 6953 O O . HOH T . ? 0.4619 0.3915 0.4750 -0.0056 0.0188 0.0117 839 HOH B O 6954 O O . HOH T . ? 0.4324 0.4576 0.4165 -0.0054 0.0102 -0.0005 840 HOH B O 6955 O O . HOH T . ? 0.4838 0.4242 0.4749 0.0076 0.0245 -0.0083 842 HOH B O 6956 O O . HOH T . ? 0.4942 0.4377 0.5092 -0.0115 0.0148 -0.0074 847 HOH B O 6957 O O . HOH T . ? 0.4457 0.3971 0.4330 -0.0067 0.0197 -0.0183 849 HOH B O 6958 O O . HOH T . ? 0.4506 0.4527 0.4308 -0.0124 0.0029 -0.0142 850 HOH B O 6959 O O . HOH T . ? 0.4020 0.4458 0.3843 -0.0071 -0.0114 0.0058 851 HOH B O 6960 O O . HOH T . ? 0.4332 0.4497 0.4064 -0.0172 0.0052 -0.0215 854 HOH B O 6961 O O . HOH T . ? 0.4862 0.4699 0.4842 0.0167 0.0061 0.0082 855 HOH B O 6962 O O . HOH T . ? 0.4428 0.4314 0.4352 0.0063 0.0092 -0.0048 857 HOH B O 6963 O O . HOH T . ? 0.5434 0.5519 0.5333 -0.0158 -0.0044 -0.0102 859 HOH B O 6964 O O . HOH T . ? 0.4617 0.5055 0.4346 -0.0085 -0.0070 0.0071 861 HOH B O 6965 O O . HOH T . ? 0.4950 0.4390 0.4832 -0.0041 0.0223 -0.0162 862 HOH B O 6966 O O . HOH T . ? 0.5777 0.5977 0.5621 -0.0046 0.0089 -0.0013 866 HOH B O 6967 O O . HOH T . ? 0.5225 0.5501 0.5021 -0.0087 0.0084 0.0058 867 HOH B O 6968 O O . HOH T . ? 0.5388 0.4902 0.5527 -0.0114 0.0117 -0.0092 868 HOH B O 6969 O O . HOH T . ? 0.6732 0.6767 0.6667 -0.0125 -0.0051 -0.0063 869 HOH B O 6970 O O . HOH T . ? 0.5325 0.5926 0.5359 0.0076 -0.0161 0.0160 870 HOH B O 6971 O O . HOH T . ? 0.6489 0.5859 0.6634 0.0136 0.0141 0.0205 872 HOH B O 6972 O O . HOH T . ? 0.4963 0.5350 0.4838 0.0063 -0.0122 0.0247 873 HOH B O 6973 O O . HOH T . ? 0.5348 0.5197 0.5313 0.0023 -0.0034 0.0188 874 HOH B O 6974 O O . HOH T . ? 0.4683 0.4944 0.4779 -0.0196 0.0078 0.0024 875 HOH B O 6975 O O . HOH T . ? 0.5623 0.5906 0.5393 -0.0113 0.0085 0.0190 879 HOH B O 6976 O O . HOH T . ? 0.6557 0.6825 0.6303 -0.0098 0.0069 0.0250 887 HOH B O 6977 O O . HOH T . ? 0.5545 0.5575 0.5346 -0.0087 0.0040 -0.0108 894 HOH B O 6978 O O . HOH T . ? 0.4833 0.4720 0.4775 -0.0179 0.0014 -0.0111 895 HOH B O 6979 O O . HOH T . ? 0.6124 0.5523 0.6047 0.0118 0.0244 -0.0034 896 HOH B O 6980 O O . HOH T . ? 0.5646 0.5072 0.5794 -0.0213 0.0185 -0.0042 898 HOH B O 6981 O O . HOH T . ? 0.5395 0.5565 0.5216 0.0054 -0.0041 0.0356 899 HOH B O 6982 O O . HOH T . ? 0.7591 0.7434 0.7674 -0.0090 0.0004 -0.0121 902 HOH B O 6983 O O . HOH T . ? 0.7486 0.7361 0.7569 -0.0110 0.0001 -0.0120 903 HOH B O 6984 O O . HOH T . ? 0.4311 0.4146 0.4412 0.0000 0.0031 0.0000 905 HOH B O # 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 82 82 SER SER A . n A 1 2 VAL 2 83 83 VAL VAL A . n A 1 3 LYS 3 84 84 LYS LYS A . n A 1 4 LEU 4 85 85 LEU LEU A . n A 1 5 ALA 5 86 86 ALA ALA A . n A 1 6 GLY 6 87 87 GLY GLY A . n A 1 7 ASN 7 88 88 ASN ASN A . n A 1 8 SER 8 89 89 SER SER A . n A 1 9 SER 9 90 90 SER SER A . n A 1 10 LEU 10 91 91 LEU LEU A . n A 1 11 CYS 11 92 92 CYS CYS A . n A 1 12 PRO 12 93 93 PRO PRO A . n A 1 13 VAL 13 94 94 VAL VAL A . n A 1 14 SER 14 95 95 SER SER A . n A 1 15 GLY 15 96 96 GLY GLY A . n A 1 16 TRP 16 97 97 TRP TRP A . n A 1 17 ALA 17 98 98 ALA ALA A . n A 1 18 ILE 18 99 99 ILE ILE A . n A 1 19 TYR 19 100 100 TYR TYR A . n A 1 20 SER 20 101 101 SER SER A . n A 1 21 LYS 21 102 102 LYS LYS A . n A 1 22 ASP 22 103 103 ASP ASP A . n A 1 23 ASN 23 104 104 ASN ASN A . n A 1 24 SER 24 105 105 SER SER A . n A 1 25 VAL 25 106 106 VAL VAL A . n A 1 26 ARG 26 107 107 ARG ARG A . n A 1 27 ILE 27 108 108 ILE ILE A . n A 1 28 GLY 28 109 109 GLY GLY A . n A 1 29 SER 29 110 110 SER SER A . n A 1 30 LYS 30 111 111 LYS LYS A . n A 1 31 GLY 31 112 112 GLY GLY A . n A 1 32 ASP 32 113 113 ASP ASP A . n A 1 33 VAL 33 114 114 VAL VAL A . n A 1 34 PHE 34 115 115 PHE PHE A . n A 1 35 VAL 35 116 116 VAL VAL A . n A 1 36 ILE 36 117 117 ILE ILE A . n A 1 37 ARG 37 118 118 ARG ARG A . n A 1 38 GLU 38 119 119 GLU GLU A . n A 1 39 PRO 39 120 120 PRO PRO A . n A 1 40 PHE 40 121 121 PHE PHE A . n A 1 41 ILE 41 122 122 ILE ILE A . n A 1 42 SER 42 123 123 SER SER A . n A 1 43 CYS 43 124 124 CYS CYS A . n A 1 44 SER 44 125 125 SER SER A . n A 1 45 PRO 45 126 126 PRO PRO A . n A 1 46 LEU 46 127 127 LEU LEU A . n A 1 47 GLU 47 128 128 GLU GLU A . n A 1 48 CYS 48 129 129 CYS CYS A . n A 1 49 ARG 49 130 130 ARG ARG A . n A 1 50 THR 50 131 131 THR THR A . n A 1 51 PHE 51 132 132 PHE PHE A . n A 1 52 PHE 52 133 133 PHE PHE A . n A 1 53 LEU 53 134 134 LEU LEU A . n A 1 54 THR 54 135 135 THR THR A . n A 1 55 GLN 55 136 136 GLN GLN A . n A 1 56 GLY 56 137 137 GLY GLY A . n A 1 57 ALA 57 138 138 ALA ALA A . n A 1 58 LEU 58 139 139 LEU LEU A . n A 1 59 LEU 59 140 140 LEU LEU A . n A 1 60 ASN 60 141 141 ASN ASN A . n A 1 61 ASP 61 142 142 ASP ASP A . n A 1 62 LYS 62 143 143 LYS LYS A . n A 1 63 HIS 63 144 144 HIS HIS A . n A 1 64 SER 64 145 145 SER SER A . n A 1 65 ASN 65 146 146 ASN ASN A . n A 1 66 GLY 66 147 147 GLY GLY A . n A 1 67 THR 67 148 148 THR THR A . n A 1 68 ILE 68 149 149 ILE ILE A . n A 1 69 LYS 69 150 150 LYS LYS A . n A 1 70 ASP 70 151 151 ASP ASP A . n A 1 71 ARG 71 152 152 ARG ARG A . n A 1 72 SER 72 153 153 SER SER A . n A 1 73 PRO 73 154 154 PRO PRO A . n A 1 74 TYR 74 155 155 TYR TYR A . n A 1 75 ARG 75 156 156 ARG ARG A . n A 1 76 THR 76 157 157 THR THR A . n A 1 77 LEU 77 158 158 LEU LEU A . n A 1 78 MET 78 159 159 MET MET A . n A 1 79 SER 79 160 160 SER SER A . n A 1 80 CYS 80 161 161 CYS CYS A . n A 1 81 PRO 81 162 162 PRO PRO A . n A 1 82 ILE 82 163 163 ILE ILE A . n A 1 83 GLY 83 164 164 GLY GLY A . n A 1 84 GLU 84 165 165 GLU GLU A . n A 1 85 VAL 85 166 166 VAL VAL A . n A 1 86 PRO 86 167 167 PRO PRO A . n A 1 87 SER 87 168 168 SER SER A . n A 1 88 PRO 88 169 169 PRO PRO A . n A 1 89 TYR 89 169 169 TYR TYR A A n A 1 90 ASN 90 170 170 ASN ASN A . n A 1 91 SER 91 171 171 SER SER A . n A 1 92 ARG 92 172 172 ARG ARG A . n A 1 93 PHE 93 173 173 PHE PHE A . n A 1 94 GLU 94 174 174 GLU GLU A . n A 1 95 SER 95 175 175 SER SER A . n A 1 96 VAL 96 176 176 VAL VAL A . n A 1 97 ALA 97 177 177 ALA ALA A . n A 1 98 TRP 98 178 178 TRP TRP A . n A 1 99 SER 99 179 179 SER SER A . n A 1 100 ALA 100 180 180 ALA ALA A . n A 1 101 SER 101 181 181 SER SER A . n A 1 102 ALA 102 182 182 ALA ALA A . n A 1 103 CYS 103 183 183 CYS CYS A . n A 1 104 HIS 104 184 184 HIS HIS A . n A 1 105 ASP 105 185 185 ASP ASP A . n A 1 106 GLY 106 186 186 GLY GLY A . n A 1 107 ILE 107 187 187 ILE ILE A . n A 1 108 ASN 108 188 188 ASN ASN A . n A 1 109 TRP 109 189 189 TRP TRP A . n A 1 110 LEU 110 190 190 LEU LEU A . n A 1 111 THR 111 191 191 THR THR A . n A 1 112 ILE 112 192 192 ILE ILE A . n A 1 113 GLY 113 193 193 GLY GLY A . n A 1 114 ILE 114 194 194 ILE ILE A . n A 1 115 SER 115 195 195 SER SER A . n A 1 116 GLY 116 196 196 GLY GLY A . n A 1 117 PRO 117 197 197 PRO PRO A . n A 1 118 ASP 118 198 198 ASP ASP A . n A 1 119 ASN 119 199 199 ASN ASN A . n A 1 120 GLY 120 200 200 GLY GLY A . n A 1 121 ALA 121 201 201 ALA ALA A . n A 1 122 VAL 122 202 202 VAL VAL A . n A 1 123 ALA 123 203 203 ALA ALA A . n A 1 124 VAL 124 204 204 VAL VAL A . n A 1 125 LEU 125 205 205 LEU LEU A . n A 1 126 LYS 126 206 206 LYS LYS A . n A 1 127 TYR 127 207 207 TYR TYR A . n A 1 128 ASN 128 208 208 ASN ASN A . n A 1 129 GLY 129 209 209 GLY GLY A . n A 1 130 ILE 130 210 210 ILE ILE A . n A 1 131 ILE 131 211 211 ILE ILE A . n A 1 132 THR 132 212 212 THR THR A . n A 1 133 ASP 133 213 213 ASP ASP A . n A 1 134 THR 134 214 214 THR THR A . n A 1 135 ILE 135 215 215 ILE ILE A . n A 1 136 LYS 136 216 216 LYS LYS A . n A 1 137 SER 137 217 217 SER SER A . n A 1 138 TRP 138 218 218 TRP TRP A . n A 1 139 ARG 139 219 219 ARG ARG A . n A 1 140 ASN 140 220 220 ASN ASN A . n A 1 141 ASN 141 221 221 ASN ASN A . n A 1 142 ILE 142 222 222 ILE ILE A . n A 1 143 LEU 143 223 223 LEU LEU A . n A 1 144 ARG 144 224 224 ARG ARG A . n A 1 145 THR 145 225 225 THR THR A . n A 1 146 GLN 146 226 226 GLN GLN A . n A 1 147 GLU 147 227 227 GLU GLU A . n A 1 148 SER 148 228 228 SER SER A . n A 1 149 GLU 149 229 229 GLU GLU A . n A 1 150 CYS 150 230 230 CYS CYS A . n A 1 151 ALA 151 231 231 ALA ALA A . n A 1 152 CYS 152 232 232 CYS CYS A . n A 1 153 VAL 153 233 233 VAL VAL A . n A 1 154 ASN 154 234 234 ASN ASN A . n A 1 155 GLY 155 235 235 GLY GLY A . n A 1 156 SER 156 236 236 SER SER A . n A 1 157 CYS 157 237 237 CYS CYS A . n A 1 158 PHE 158 238 238 PHE PHE A . n A 1 159 THR 159 239 239 THR THR A . n A 1 160 VAL 160 240 240 VAL VAL A . n A 1 161 MET 161 241 241 MET MET A . n A 1 162 THR 162 242 242 THR THR A . n A 1 163 ASP 163 243 243 ASP ASP A . n A 1 164 GLY 164 244 244 GLY GLY A . n A 1 165 PRO 165 245 245 PRO PRO A . n A 1 166 SER 166 246 246 SER SER A . n A 1 167 ASN 167 247 247 ASN ASN A . n A 1 168 GLY 168 248 248 GLY GLY A . n A 1 169 GLN 169 249 249 GLN GLN A . n A 1 170 ALA 170 250 250 ALA ALA A . n A 1 171 SER 171 251 251 SER SER A . n A 1 172 TYR 172 252 252 TYR TYR A . n A 1 173 LYS 173 253 253 LYS LYS A . n A 1 174 ILE 174 254 254 ILE ILE A . n A 1 175 PHE 175 255 255 PHE PHE A . n A 1 176 ARG 176 256 256 ARG ARG A . n A 1 177 ILE 177 257 257 ILE ILE A . n A 1 178 GLU 178 258 258 GLU GLU A . n A 1 179 LYS 179 259 259 LYS LYS A . n A 1 180 GLY 180 260 260 GLY GLY A . n A 1 181 LYS 181 261 261 LYS LYS A . n A 1 182 ILE 182 262 262 ILE ILE A . n A 1 183 VAL 183 263 263 VAL VAL A . n A 1 184 LYS 184 264 264 LYS LYS A . n A 1 185 SER 185 265 265 SER SER A . n A 1 186 VAL 186 266 266 VAL VAL A . n A 1 187 GLU 187 267 267 GLU GLU A . n A 1 188 MET 188 268 268 MET MET A . n A 1 189 ASN 189 269 269 ASN ASN A . n A 1 190 ALA 190 270 270 ALA ALA A . n A 1 191 PRO 191 271 271 PRO PRO A . n A 1 192 ASN 192 272 272 ASN ASN A . n A 1 193 TYR 193 273 273 TYR TYR A . n A 1 194 HIS 194 274 274 HIS HIS A . n A 1 195 TYR 195 275 275 TYR TYR A . n A 1 196 GLU 196 276 276 GLU GLU A . n A 1 197 GLU 197 277 277 GLU GLU A . n A 1 198 CYS 198 278 278 CYS CYS A . n A 1 199 SER 199 279 279 SER SER A . n A 1 200 CYS 200 280 280 CYS CYS A . n A 1 201 TYR 201 281 281 TYR TYR A . n A 1 202 PRO 202 282 282 PRO PRO A . n A 1 203 ASP 203 283 283 ASP ASP A . n A 1 204 SER 204 284 284 SER SER A . n A 1 205 SER 205 285 285 SER SER A . n A 1 206 GLU 206 286 286 GLU GLU A . n A 1 207 ILE 207 287 287 ILE ILE A . n A 1 208 THR 208 288 288 THR THR A . n A 1 209 CYS 209 289 289 CYS CYS A . n A 1 210 VAL 210 290 290 VAL VAL A . n A 1 211 CYS 211 291 291 CYS CYS A . n A 1 212 ARG 212 292 292 ARG ARG A . n A 1 213 ASP 213 293 293 ASP ASP A . n A 1 214 ASN 214 294 294 ASN ASN A . n A 1 215 TRP 215 295 295 TRP TRP A . n A 1 216 HIS 216 296 296 HIS HIS A . n A 1 217 GLY 217 297 297 GLY GLY A . n A 1 218 SER 218 298 298 SER SER A . n A 1 219 ASN 219 299 299 ASN ASN A . n A 1 220 ARG 220 300 300 ARG ARG A . n A 1 221 PRO 221 301 301 PRO PRO A . n A 1 222 TRP 222 302 302 TRP TRP A . n A 1 223 VAL 223 303 303 VAL VAL A . n A 1 224 SER 224 304 304 SER SER A . n A 1 225 PHE 225 305 305 PHE PHE A . n A 1 226 ASN 226 306 306 ASN ASN A . n A 1 227 GLN 227 308 308 GLN GLN A . n A 1 228 ASN 228 309 309 ASN ASN A . n A 1 229 LEU 229 310 310 LEU LEU A . n A 1 230 GLU 230 311 311 GLU GLU A . n A 1 231 TYR 231 312 312 TYR TYR A . n A 1 232 GLN 232 313 313 GLN GLN A . n A 1 233 ILE 233 314 314 ILE ILE A . n A 1 234 GLY 234 315 315 GLY GLY A . n A 1 235 TYR 235 316 316 TYR TYR A . n A 1 236 ILE 236 317 317 ILE ILE A . n A 1 237 CYS 237 318 318 CYS CYS A . n A 1 238 SER 238 319 319 SER SER A . n A 1 239 GLY 239 320 320 GLY GLY A . n A 1 240 ILE 240 321 321 ILE ILE A . n A 1 241 PHE 241 322 322 PHE PHE A . n A 1 242 GLY 242 323 323 GLY GLY A . n A 1 243 ASP 243 324 324 ASP ASP A . n A 1 244 ASN 244 325 325 ASN ASN A . n A 1 245 PRO 245 326 326 PRO PRO A . n A 1 246 ARG 246 327 327 ARG ARG A . n A 1 247 PRO 247 328 328 PRO PRO A . n A 1 248 ASN 248 329 329 ASN ASN A . n A 1 249 ASP 249 330 330 ASP ASP A . n A 1 250 LYS 250 331 331 LYS LYS A . n A 1 251 THR 251 332 332 THR THR A . n A 1 252 GLY 252 333 333 GLY GLY A . n A 1 253 SER 253 335 335 SER SER A . n A 1 254 CYS 254 336 336 CYS CYS A . n A 1 255 GLY 255 339 339 GLY GLY A . n A 1 256 PRO 256 340 340 PRO PRO A . n A 1 257 VAL 257 341 341 VAL VAL A . n A 1 258 SER 258 342 342 SER SER A . n A 1 259 SER 259 343 343 SER SER A . n A 1 260 ASN 260 344 344 ASN ASN A . n A 1 261 GLY 261 345 345 GLY GLY A . n A 1 262 ALA 262 346 346 ALA ALA A . n A 1 263 ASN 263 347 347 ASN ASN A . n A 1 264 GLY 264 348 348 GLY GLY A . n A 1 265 VAL 265 349 349 VAL VAL A . n A 1 266 LYS 266 350 350 LYS LYS A . n A 1 267 GLY 267 351 351 GLY GLY A . n A 1 268 PHE 268 352 352 PHE PHE A . n A 1 269 SER 269 353 353 SER SER A . n A 1 270 PHE 270 354 354 PHE PHE A . n A 1 271 LYS 271 355 355 LYS LYS A . n A 1 272 TYR 272 356 356 TYR TYR A . n A 1 273 GLY 273 357 357 GLY GLY A . n A 1 274 ASN 274 358 358 ASN ASN A . n A 1 275 GLY 275 359 359 GLY GLY A . n A 1 276 VAL 276 360 360 VAL VAL A . n A 1 277 TRP 277 361 361 TRP TRP A . n A 1 278 ILE 278 362 362 ILE ILE A . n A 1 279 GLY 279 363 363 GLY GLY A . n A 1 280 ARG 280 364 364 ARG ARG A . n A 1 281 THR 281 365 365 THR THR A . n A 1 282 LYS 282 366 366 LYS LYS A . n A 1 283 SER 283 367 367 SER SER A . n A 1 284 ILE 284 368 368 ILE ILE A . n A 1 285 SER 285 369 369 SER SER A . n A 1 286 SER 286 370 370 SER SER A . n A 1 287 ARG 287 371 371 ARG ARG A . n A 1 288 ASN 288 372 372 ASN ASN A . n A 1 289 GLY 289 373 373 GLY GLY A . n A 1 290 PHE 290 374 374 PHE PHE A . n A 1 291 GLU 291 375 375 GLU GLU A . n A 1 292 MET 292 376 376 MET MET A . n A 1 293 ILE 293 377 377 ILE ILE A . n A 1 294 TRP 294 378 378 TRP TRP A . n A 1 295 ASP 295 379 379 ASP ASP A . n A 1 296 PRO 296 380 380 PRO PRO A . n A 1 297 ASN 297 381 381 ASN ASN A . n A 1 298 GLY 298 382 382 GLY GLY A . n A 1 299 TRP 299 383 383 TRP TRP A . n A 1 300 THR 300 384 384 THR THR A . n A 1 301 GLY 301 385 385 GLY GLY A . n A 1 302 THR 302 386 386 THR THR A . n A 1 303 ASP 303 387 387 ASP ASP A . n A 1 304 ASN 304 388 388 ASN ASN A . n A 1 305 ASN 305 389 389 ASN ASN A . n A 1 306 PHE 306 390 390 PHE PHE A . n A 1 307 SER 307 391 391 SER SER A . n A 1 308 ILE 308 392 392 ILE ILE A . n A 1 309 LYS 309 394 394 LYS LYS A . n A 1 310 GLN 310 395 395 GLN GLN A . n A 1 311 ASP 311 396 396 ASP ASP A . n A 1 312 ILE 312 397 397 ILE ILE A . n A 1 313 VAL 313 398 398 VAL VAL A . n A 1 314 GLY 314 399 399 GLY GLY A . n A 1 315 ILE 315 400 400 ILE ILE A . n A 1 316 ASN 316 401 401 ASN ASN A . n A 1 317 GLU 317 402 402 GLU GLU A . n A 1 318 TRP 318 403 403 TRP TRP A . n A 1 319 SER 319 404 404 SER SER A . n A 1 320 GLY 320 405 405 GLY GLY A . n A 1 321 TYR 321 406 406 TYR TYR A . n A 1 322 SER 322 407 407 SER SER A . n A 1 323 GLY 323 408 408 GLY GLY A . n A 1 324 SER 324 409 409 SER SER A . n A 1 325 PHE 325 410 410 PHE PHE A . n A 1 326 VAL 326 411 411 VAL VAL A . n A 1 327 GLN 327 412 412 GLN GLN A . n A 1 328 HIS 328 412 412 HIS HIS A A n A 1 329 PRO 329 412 412 PRO PRO A B n A 1 330 GLU 330 412 412 GLU GLU A C n A 1 331 LEU 331 412 412 LEU LEU A D n A 1 332 THR 332 413 413 THR THR A . n A 1 333 GLY 333 414 414 GLY GLY A . n A 1 334 LEU 334 415 415 LEU LEU A . n A 1 335 ASP 335 416 416 ASP ASP A . n A 1 336 CYS 336 417 417 CYS CYS A . n A 1 337 ILE 337 418 418 ILE ILE A . n A 1 338 ARG 338 419 419 ARG ARG A . n A 1 339 PRO 339 420 420 PRO PRO A . n A 1 340 CYS 340 421 421 CYS CYS A . n A 1 341 PHE 341 422 422 PHE PHE A . n A 1 342 TRP 342 423 423 TRP TRP A . n A 1 343 VAL 343 424 424 VAL VAL A . n A 1 344 GLU 344 425 425 GLU GLU A . n A 1 345 LEU 345 426 426 LEU LEU A . n A 1 346 ILE 346 427 427 ILE ILE A . n A 1 347 ARG 347 428 428 ARG ARG A . n A 1 348 GLY 348 429 429 GLY GLY A . n A 1 349 ARG 349 430 430 ARG ARG A . n A 1 350 PRO 350 431 431 PRO PRO A . n A 1 351 LYS 351 432 432 LYS LYS A . n A 1 352 GLU 352 433 433 GLU GLU A . n A 1 353 ASN 353 435 435 ASN ASN A . n A 1 354 THR 354 436 436 THR THR A . n A 1 355 ILE 355 437 437 ILE ILE A . n A 1 356 TRP 356 438 438 TRP TRP A . n A 1 357 THR 357 439 439 THR THR A . n A 1 358 SER 358 440 440 SER SER A . n A 1 359 GLY 359 441 441 GLY GLY A . n A 1 360 SER 360 442 442 SER SER A . n A 1 361 SER 361 443 443 SER SER A . n A 1 362 ILE 362 444 444 ILE ILE A . n A 1 363 SER 363 445 445 SER SER A . n A 1 364 PHE 364 446 446 PHE PHE A . n A 1 365 CYS 365 447 447 CYS CYS A . n A 1 366 GLY 366 448 448 GLY GLY A . n A 1 367 VAL 367 449 449 VAL VAL A . n A 1 368 ASN 368 450 450 ASN ASN A . n A 1 369 SER 369 451 451 SER SER A . n A 1 370 ASP 370 452 452 ASP ASP A . n A 1 371 THR 371 453 453 THR THR A . n A 1 372 VAL 372 454 454 VAL VAL A . n A 1 373 GLY 373 455 455 GLY GLY A . n A 1 374 TRP 374 456 456 TRP TRP A . n A 1 375 SER 375 457 457 SER SER A . n A 1 376 TRP 376 458 458 TRP TRP A . n A 1 377 PRO 377 459 459 PRO PRO A . n A 1 378 ASP 378 460 460 ASP ASP A . n A 1 379 GLY 379 461 461 GLY GLY A . n A 1 380 ALA 380 462 462 ALA ALA A . n A 1 381 GLU 381 463 463 GLU GLU A . n A 1 382 LEU 382 464 464 LEU LEU A . n A 1 383 PRO 383 465 465 PRO PRO A . n A 1 384 PHE 384 466 466 PHE PHE A . n A 1 385 THR 385 467 467 THR THR A . n A 1 386 ILE 386 468 468 ILE ILE A . n A 1 387 ASP 387 469 469 ASP ASP A . n A 1 388 LYS 388 470 ? ? ? A . n B 1 1 SER 1 82 82 SER SER B . n B 1 2 VAL 2 83 83 VAL VAL B . n B 1 3 LYS 3 84 84 LYS LYS B . n B 1 4 LEU 4 85 85 LEU LEU B . n B 1 5 ALA 5 86 86 ALA ALA B . n B 1 6 GLY 6 87 87 GLY GLY B . n B 1 7 ASN 7 88 88 ASN ASN B . n B 1 8 SER 8 89 89 SER SER B . n B 1 9 SER 9 90 90 SER SER B . n B 1 10 LEU 10 91 91 LEU LEU B . n B 1 11 CYS 11 92 92 CYS CYS B . n B 1 12 PRO 12 93 93 PRO PRO B . n B 1 13 VAL 13 94 94 VAL VAL B . n B 1 14 SER 14 95 95 SER SER B . n B 1 15 GLY 15 96 96 GLY GLY B . n B 1 16 TRP 16 97 97 TRP TRP B . n B 1 17 ALA 17 98 98 ALA ALA B . n B 1 18 ILE 18 99 99 ILE ILE B . n B 1 19 TYR 19 100 100 TYR TYR B . n B 1 20 SER 20 101 101 SER SER B . n B 1 21 LYS 21 102 102 LYS LYS B . n B 1 22 ASP 22 103 103 ASP ASP B . n B 1 23 ASN 23 104 104 ASN ASN B . n B 1 24 SER 24 105 105 SER SER B . n B 1 25 VAL 25 106 106 VAL VAL B . n B 1 26 ARG 26 107 107 ARG ARG B . n B 1 27 ILE 27 108 108 ILE ILE B . n B 1 28 GLY 28 109 109 GLY GLY B . n B 1 29 SER 29 110 110 SER SER B . n B 1 30 LYS 30 111 111 LYS LYS B . n B 1 31 GLY 31 112 112 GLY GLY B . n B 1 32 ASP 32 113 113 ASP ASP B . n B 1 33 VAL 33 114 114 VAL VAL B . n B 1 34 PHE 34 115 115 PHE PHE B . n B 1 35 VAL 35 116 116 VAL VAL B . n B 1 36 ILE 36 117 117 ILE ILE B . n B 1 37 ARG 37 118 118 ARG ARG B . n B 1 38 GLU 38 119 119 GLU GLU B . n B 1 39 PRO 39 120 120 PRO PRO B . n B 1 40 PHE 40 121 121 PHE PHE B . n B 1 41 ILE 41 122 122 ILE ILE B . n B 1 42 SER 42 123 123 SER SER B . n B 1 43 CYS 43 124 124 CYS CYS B . n B 1 44 SER 44 125 125 SER SER B . n B 1 45 PRO 45 126 126 PRO PRO B . n B 1 46 LEU 46 127 127 LEU LEU B . n B 1 47 GLU 47 128 128 GLU GLU B . n B 1 48 CYS 48 129 129 CYS CYS B . n B 1 49 ARG 49 130 130 ARG ARG B . n B 1 50 THR 50 131 131 THR THR B . n B 1 51 PHE 51 132 132 PHE PHE B . n B 1 52 PHE 52 133 133 PHE PHE B . n B 1 53 LEU 53 134 134 LEU LEU B . n B 1 54 THR 54 135 135 THR THR B . n B 1 55 GLN 55 136 136 GLN GLN B . n B 1 56 GLY 56 137 137 GLY GLY B . n B 1 57 ALA 57 138 138 ALA ALA B . n B 1 58 LEU 58 139 139 LEU LEU B . n B 1 59 LEU 59 140 140 LEU LEU B . n B 1 60 ASN 60 141 141 ASN ASN B . n B 1 61 ASP 61 142 142 ASP ASP B . n B 1 62 LYS 62 143 143 LYS LYS B . n B 1 63 HIS 63 144 144 HIS HIS B . n B 1 64 SER 64 145 145 SER SER B . n B 1 65 ASN 65 146 146 ASN ASN B . n B 1 66 GLY 66 147 147 GLY GLY B . n B 1 67 THR 67 148 148 THR THR B . n B 1 68 ILE 68 149 149 ILE ILE B . n B 1 69 LYS 69 150 150 LYS LYS B . n B 1 70 ASP 70 151 151 ASP ASP B . n B 1 71 ARG 71 152 152 ARG ARG B . n B 1 72 SER 72 153 153 SER SER B . n B 1 73 PRO 73 154 154 PRO PRO B . n B 1 74 TYR 74 155 155 TYR TYR B . n B 1 75 ARG 75 156 156 ARG ARG B . n B 1 76 THR 76 157 157 THR THR B . n B 1 77 LEU 77 158 158 LEU LEU B . n B 1 78 MET 78 159 159 MET MET B . n B 1 79 SER 79 160 160 SER SER B . n B 1 80 CYS 80 161 161 CYS CYS B . n B 1 81 PRO 81 162 162 PRO PRO B . n B 1 82 ILE 82 163 163 ILE ILE B . n B 1 83 GLY 83 164 164 GLY GLY B . n B 1 84 GLU 84 165 165 GLU GLU B . n B 1 85 VAL 85 166 166 VAL VAL B . n B 1 86 PRO 86 167 167 PRO PRO B . n B 1 87 SER 87 168 168 SER SER B . n B 1 88 PRO 88 169 169 PRO PRO B . n B 1 89 TYR 89 169 169 TYR TYR B A n B 1 90 ASN 90 170 170 ASN ASN B . n B 1 91 SER 91 171 171 SER SER B . n B 1 92 ARG 92 172 172 ARG ARG B . n B 1 93 PHE 93 173 173 PHE PHE B . n B 1 94 GLU 94 174 174 GLU GLU B . n B 1 95 SER 95 175 175 SER SER B . n B 1 96 VAL 96 176 176 VAL VAL B . n B 1 97 ALA 97 177 177 ALA ALA B . n B 1 98 TRP 98 178 178 TRP TRP B . n B 1 99 SER 99 179 179 SER SER B . n B 1 100 ALA 100 180 180 ALA ALA B . n B 1 101 SER 101 181 181 SER SER B . n B 1 102 ALA 102 182 182 ALA ALA B . n B 1 103 CYS 103 183 183 CYS CYS B . n B 1 104 HIS 104 184 184 HIS HIS B . n B 1 105 ASP 105 185 185 ASP ASP B . n B 1 106 GLY 106 186 186 GLY GLY B . n B 1 107 ILE 107 187 187 ILE ILE B . n B 1 108 ASN 108 188 188 ASN ASN B . n B 1 109 TRP 109 189 189 TRP TRP B . n B 1 110 LEU 110 190 190 LEU LEU B . n B 1 111 THR 111 191 191 THR THR B . n B 1 112 ILE 112 192 192 ILE ILE B . n B 1 113 GLY 113 193 193 GLY GLY B . n B 1 114 ILE 114 194 194 ILE ILE B . n B 1 115 SER 115 195 195 SER SER B . n B 1 116 GLY 116 196 196 GLY GLY B . n B 1 117 PRO 117 197 197 PRO PRO B . n B 1 118 ASP 118 198 198 ASP ASP B . n B 1 119 ASN 119 199 199 ASN ASN B . n B 1 120 GLY 120 200 200 GLY GLY B . n B 1 121 ALA 121 201 201 ALA ALA B . n B 1 122 VAL 122 202 202 VAL VAL B . n B 1 123 ALA 123 203 203 ALA ALA B . n B 1 124 VAL 124 204 204 VAL VAL B . n B 1 125 LEU 125 205 205 LEU LEU B . n B 1 126 LYS 126 206 206 LYS LYS B . n B 1 127 TYR 127 207 207 TYR TYR B . n B 1 128 ASN 128 208 208 ASN ASN B . n B 1 129 GLY 129 209 209 GLY GLY B . n B 1 130 ILE 130 210 210 ILE ILE B . n B 1 131 ILE 131 211 211 ILE ILE B . n B 1 132 THR 132 212 212 THR THR B . n B 1 133 ASP 133 213 213 ASP ASP B . n B 1 134 THR 134 214 214 THR THR B . n B 1 135 ILE 135 215 215 ILE ILE B . n B 1 136 LYS 136 216 216 LYS LYS B . n B 1 137 SER 137 217 217 SER SER B . n B 1 138 TRP 138 218 218 TRP TRP B . n B 1 139 ARG 139 219 219 ARG ARG B . n B 1 140 ASN 140 220 220 ASN ASN B . n B 1 141 ASN 141 221 221 ASN ASN B . n B 1 142 ILE 142 222 222 ILE ILE B . n B 1 143 LEU 143 223 223 LEU LEU B . n B 1 144 ARG 144 224 224 ARG ARG B . n B 1 145 THR 145 225 225 THR THR B . n B 1 146 GLN 146 226 226 GLN GLN B . n B 1 147 GLU 147 227 227 GLU GLU B . n B 1 148 SER 148 228 228 SER SER B . n B 1 149 GLU 149 229 229 GLU GLU B . n B 1 150 CYS 150 230 230 CYS CYS B . n B 1 151 ALA 151 231 231 ALA ALA B . n B 1 152 CYS 152 232 232 CYS CYS B . n B 1 153 VAL 153 233 233 VAL VAL B . n B 1 154 ASN 154 234 234 ASN ASN B . n B 1 155 GLY 155 235 235 GLY GLY B . n B 1 156 SER 156 236 236 SER SER B . n B 1 157 CYS 157 237 237 CYS CYS B . n B 1 158 PHE 158 238 238 PHE PHE B . n B 1 159 THR 159 239 239 THR THR B . n B 1 160 VAL 160 240 240 VAL VAL B . n B 1 161 MET 161 241 241 MET MET B . n B 1 162 THR 162 242 242 THR THR B . n B 1 163 ASP 163 243 243 ASP ASP B . n B 1 164 GLY 164 244 244 GLY GLY B . n B 1 165 PRO 165 245 245 PRO PRO B . n B 1 166 SER 166 246 246 SER SER B . n B 1 167 ASN 167 247 247 ASN ASN B . n B 1 168 GLY 168 248 248 GLY GLY B . n B 1 169 GLN 169 249 249 GLN GLN B . n B 1 170 ALA 170 250 250 ALA ALA B . n B 1 171 SER 171 251 251 SER SER B . n B 1 172 TYR 172 252 252 TYR TYR B . n B 1 173 LYS 173 253 253 LYS LYS B . n B 1 174 ILE 174 254 254 ILE ILE B . n B 1 175 PHE 175 255 255 PHE PHE B . n B 1 176 ARG 176 256 256 ARG ARG B . n B 1 177 ILE 177 257 257 ILE ILE B . n B 1 178 GLU 178 258 258 GLU GLU B . n B 1 179 LYS 179 259 259 LYS LYS B . n B 1 180 GLY 180 260 260 GLY GLY B . n B 1 181 LYS 181 261 261 LYS LYS B . n B 1 182 ILE 182 262 262 ILE ILE B . n B 1 183 VAL 183 263 263 VAL VAL B . n B 1 184 LYS 184 264 264 LYS LYS B . n B 1 185 SER 185 265 265 SER SER B . n B 1 186 VAL 186 266 266 VAL VAL B . n B 1 187 GLU 187 267 267 GLU GLU B . n B 1 188 MET 188 268 268 MET MET B . n B 1 189 ASN 189 269 269 ASN ASN B . n B 1 190 ALA 190 270 270 ALA ALA B . n B 1 191 PRO 191 271 271 PRO PRO B . n B 1 192 ASN 192 272 272 ASN ASN B . n B 1 193 TYR 193 273 273 TYR TYR B . n B 1 194 HIS 194 274 274 HIS HIS B . n B 1 195 TYR 195 275 275 TYR TYR B . n B 1 196 GLU 196 276 276 GLU GLU B . n B 1 197 GLU 197 277 277 GLU GLU B . n B 1 198 CYS 198 278 278 CYS CYS B . n B 1 199 SER 199 279 279 SER SER B . n B 1 200 CYS 200 280 280 CYS CYS B . n B 1 201 TYR 201 281 281 TYR TYR B . n B 1 202 PRO 202 282 282 PRO PRO B . n B 1 203 ASP 203 283 283 ASP ASP B . n B 1 204 SER 204 284 284 SER SER B . n B 1 205 SER 205 285 285 SER SER B . n B 1 206 GLU 206 286 286 GLU GLU B . n B 1 207 ILE 207 287 287 ILE ILE B . n B 1 208 THR 208 288 288 THR THR B . n B 1 209 CYS 209 289 289 CYS CYS B . n B 1 210 VAL 210 290 290 VAL VAL B . n B 1 211 CYS 211 291 291 CYS CYS B . n B 1 212 ARG 212 292 292 ARG ARG B . n B 1 213 ASP 213 293 293 ASP ASP B . n B 1 214 ASN 214 294 294 ASN ASN B . n B 1 215 TRP 215 295 295 TRP TRP B . n B 1 216 HIS 216 296 296 HIS HIS B . n B 1 217 GLY 217 297 297 GLY GLY B . n B 1 218 SER 218 298 298 SER SER B . n B 1 219 ASN 219 299 299 ASN ASN B . n B 1 220 ARG 220 300 300 ARG ARG B . n B 1 221 PRO 221 301 301 PRO PRO B . n B 1 222 TRP 222 302 302 TRP TRP B . n B 1 223 VAL 223 303 303 VAL VAL B . n B 1 224 SER 224 304 304 SER SER B . n B 1 225 PHE 225 305 305 PHE PHE B . n B 1 226 ASN 226 306 306 ASN ASN B . n B 1 227 GLN 227 308 308 GLN GLN B . n B 1 228 ASN 228 309 309 ASN ASN B . n B 1 229 LEU 229 310 310 LEU LEU B . n B 1 230 GLU 230 311 311 GLU GLU B . n B 1 231 TYR 231 312 312 TYR TYR B . n B 1 232 GLN 232 313 313 GLN GLN B . n B 1 233 ILE 233 314 314 ILE ILE B . n B 1 234 GLY 234 315 315 GLY GLY B . n B 1 235 TYR 235 316 316 TYR TYR B . n B 1 236 ILE 236 317 317 ILE ILE B . n B 1 237 CYS 237 318 318 CYS CYS B . n B 1 238 SER 238 319 319 SER SER B . n B 1 239 GLY 239 320 320 GLY GLY B . n B 1 240 ILE 240 321 321 ILE ILE B . n B 1 241 PHE 241 322 322 PHE PHE B . n B 1 242 GLY 242 323 323 GLY GLY B . n B 1 243 ASP 243 324 324 ASP ASP B . n B 1 244 ASN 244 325 325 ASN ASN B . n B 1 245 PRO 245 326 326 PRO PRO B . n B 1 246 ARG 246 327 327 ARG ARG B . n B 1 247 PRO 247 328 328 PRO PRO B . n B 1 248 ASN 248 329 329 ASN ASN B . n B 1 249 ASP 249 330 330 ASP ASP B . n B 1 250 LYS 250 331 331 LYS LYS B . n B 1 251 THR 251 332 332 THR THR B . n B 1 252 GLY 252 333 333 GLY GLY B . n B 1 253 SER 253 335 335 SER SER B . n B 1 254 CYS 254 336 336 CYS CYS B . n B 1 255 GLY 255 339 339 GLY GLY B . n B 1 256 PRO 256 340 340 PRO PRO B . n B 1 257 VAL 257 341 341 VAL VAL B . n B 1 258 SER 258 342 342 SER SER B . n B 1 259 SER 259 343 343 SER SER B . n B 1 260 ASN 260 344 344 ASN ASN B . n B 1 261 GLY 261 345 345 GLY GLY B . n B 1 262 ALA 262 346 346 ALA ALA B . n B 1 263 ASN 263 347 347 ASN ASN B . n B 1 264 GLY 264 348 348 GLY GLY B . n B 1 265 VAL 265 349 349 VAL VAL B . n B 1 266 LYS 266 350 350 LYS LYS B . n B 1 267 GLY 267 351 351 GLY GLY B . n B 1 268 PHE 268 352 352 PHE PHE B . n B 1 269 SER 269 353 353 SER SER B . n B 1 270 PHE 270 354 354 PHE PHE B . n B 1 271 LYS 271 355 355 LYS LYS B . n B 1 272 TYR 272 356 356 TYR TYR B . n B 1 273 GLY 273 357 357 GLY GLY B . n B 1 274 ASN 274 358 358 ASN ASN B . n B 1 275 GLY 275 359 359 GLY GLY B . n B 1 276 VAL 276 360 360 VAL VAL B . n B 1 277 TRP 277 361 361 TRP TRP B . n B 1 278 ILE 278 362 362 ILE ILE B . n B 1 279 GLY 279 363 363 GLY GLY B . n B 1 280 ARG 280 364 364 ARG ARG B . n B 1 281 THR 281 365 365 THR THR B . n B 1 282 LYS 282 366 366 LYS LYS B . n B 1 283 SER 283 367 367 SER SER B . n B 1 284 ILE 284 368 368 ILE ILE B . n B 1 285 SER 285 369 369 SER SER B . n B 1 286 SER 286 370 370 SER SER B . n B 1 287 ARG 287 371 371 ARG ARG B . n B 1 288 ASN 288 372 372 ASN ASN B . n B 1 289 GLY 289 373 373 GLY GLY B . n B 1 290 PHE 290 374 374 PHE PHE B . n B 1 291 GLU 291 375 375 GLU GLU B . n B 1 292 MET 292 376 376 MET MET B . n B 1 293 ILE 293 377 377 ILE ILE B . n B 1 294 TRP 294 378 378 TRP TRP B . n B 1 295 ASP 295 379 379 ASP ASP B . n B 1 296 PRO 296 380 380 PRO PRO B . n B 1 297 ASN 297 381 381 ASN ASN B . n B 1 298 GLY 298 382 382 GLY GLY B . n B 1 299 TRP 299 383 383 TRP TRP B . n B 1 300 THR 300 384 384 THR THR B . n B 1 301 GLY 301 385 385 GLY GLY B . n B 1 302 THR 302 386 386 THR THR B . n B 1 303 ASP 303 387 387 ASP ASP B . n B 1 304 ASN 304 388 388 ASN ASN B . n B 1 305 ASN 305 389 389 ASN ASN B . n B 1 306 PHE 306 390 390 PHE PHE B . n B 1 307 SER 307 391 391 SER SER B . n B 1 308 ILE 308 392 392 ILE ILE B . n B 1 309 LYS 309 394 394 LYS LYS B . n B 1 310 GLN 310 395 395 GLN GLN B . n B 1 311 ASP 311 396 396 ASP ASP B . n B 1 312 ILE 312 397 397 ILE ILE B . n B 1 313 VAL 313 398 398 VAL VAL B . n B 1 314 GLY 314 399 399 GLY GLY B . n B 1 315 ILE 315 400 400 ILE ILE B . n B 1 316 ASN 316 401 401 ASN ASN B . n B 1 317 GLU 317 402 402 GLU GLU B . n B 1 318 TRP 318 403 403 TRP TRP B . n B 1 319 SER 319 404 404 SER SER B . n B 1 320 GLY 320 405 405 GLY GLY B . n B 1 321 TYR 321 406 406 TYR TYR B . n B 1 322 SER 322 407 407 SER SER B . n B 1 323 GLY 323 408 408 GLY GLY B . n B 1 324 SER 324 409 409 SER SER B . n B 1 325 PHE 325 410 410 PHE PHE B . n B 1 326 VAL 326 411 411 VAL VAL B . n B 1 327 GLN 327 412 412 GLN GLN B . n B 1 328 HIS 328 412 412 HIS HIS B A n B 1 329 PRO 329 412 412 PRO PRO B B n B 1 330 GLU 330 412 412 GLU GLU B C n B 1 331 LEU 331 412 412 LEU LEU B D n B 1 332 THR 332 413 413 THR THR B . n B 1 333 GLY 333 414 414 GLY GLY B . n B 1 334 LEU 334 415 415 LEU LEU B . n B 1 335 ASP 335 416 416 ASP ASP B . n B 1 336 CYS 336 417 417 CYS CYS B . n B 1 337 ILE 337 418 418 ILE ILE B . n B 1 338 ARG 338 419 419 ARG ARG B . n B 1 339 PRO 339 420 420 PRO PRO B . n B 1 340 CYS 340 421 421 CYS CYS B . n B 1 341 PHE 341 422 422 PHE PHE B . n B 1 342 TRP 342 423 423 TRP TRP B . n B 1 343 VAL 343 424 424 VAL VAL B . n B 1 344 GLU 344 425 425 GLU GLU B . n B 1 345 LEU 345 426 426 LEU LEU B . n B 1 346 ILE 346 427 427 ILE ILE B . n B 1 347 ARG 347 428 428 ARG ARG B . n B 1 348 GLY 348 429 429 GLY GLY B . n B 1 349 ARG 349 430 430 ARG ARG B . n B 1 350 PRO 350 431 431 PRO PRO B . n B 1 351 LYS 351 432 432 LYS LYS B . n B 1 352 GLU 352 433 433 GLU GLU B . n B 1 353 ASN 353 435 435 ASN ASN B . n B 1 354 THR 354 436 436 THR THR B . n B 1 355 ILE 355 437 437 ILE ILE B . n B 1 356 TRP 356 438 438 TRP TRP B . n B 1 357 THR 357 439 439 THR THR B . n B 1 358 SER 358 440 440 SER SER B . n B 1 359 GLY 359 441 441 GLY GLY B . n B 1 360 SER 360 442 442 SER SER B . n B 1 361 SER 361 443 443 SER SER B . n B 1 362 ILE 362 444 444 ILE ILE B . n B 1 363 SER 363 445 445 SER SER B . n B 1 364 PHE 364 446 446 PHE PHE B . n B 1 365 CYS 365 447 447 CYS CYS B . n B 1 366 GLY 366 448 448 GLY GLY B . n B 1 367 VAL 367 449 449 VAL VAL B . n B 1 368 ASN 368 450 450 ASN ASN B . n B 1 369 SER 369 451 451 SER SER B . n B 1 370 ASP 370 452 452 ASP ASP B . n B 1 371 THR 371 453 453 THR THR B . n B 1 372 VAL 372 454 454 VAL VAL B . n B 1 373 GLY 373 455 455 GLY GLY B . n B 1 374 TRP 374 456 456 TRP TRP B . n B 1 375 SER 375 457 457 SER SER B . n B 1 376 TRP 376 458 458 TRP TRP B . n B 1 377 PRO 377 459 459 PRO PRO B . n B 1 378 ASP 378 460 460 ASP ASP B . n B 1 379 GLY 379 461 461 GLY GLY B . n B 1 380 ALA 380 462 462 ALA ALA B . n B 1 381 GLU 381 463 463 GLU GLU B . n B 1 382 LEU 382 464 464 LEU LEU B . n B 1 383 PRO 383 465 465 PRO PRO B . n B 1 384 PHE 384 466 466 PHE PHE B . n B 1 385 THR 385 467 467 THR THR B . n B 1 386 ILE 386 468 468 ILE ILE B . n B 1 387 ASP 387 469 469 ASP ASP B . n B 1 388 LYS 388 470 ? ? ? B . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 B ASN 65 B ASN 146 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 7 B ASN 88 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 7 A ASN 88 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 65 A ASN 146 ? ASN 'GLYCOSYLATION SITE' # _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 tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _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,G,H,I,J,K,L,M,N,O,P,Q,R,S,T # 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)' 12350 ? 1 MORE -67 ? 1 'SSA (A^2)' 44200 ? # 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' 3_555 -x,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 59.2560000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A CA 603 ? J CA . 2 1 B HOH 488 ? T HOH . 3 1 B HOH 785 ? T HOH . 4 1 B HOH 809 ? T HOH . 5 1 B HOH 905 ? T HOH . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 81.5 ? 2 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? B ASN 305 ? B ASN 389 ? 1_555 81.6 ? 3 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? B ASN 305 ? B ASN 389 ? 1_555 151.7 ? 4 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 164.4 ? 5 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 113.3 ? 6 O ? B ASN 305 ? B ASN 389 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 82.9 ? 7 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 46.3 ? 8 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 103.9 ? 9 O ? B ASN 305 ? B ASN 389 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 80.0 ? 10 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 129.1 ? 11 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 56 ? 1_555 103.0 ? 12 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 56 ? 1_555 81.1 ? 13 O ? B ASN 305 ? B ASN 389 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 56 ? 1_555 125.0 ? 14 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 56 ? 1_555 84.9 ? 15 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 56 ? 1_555 67.4 ? 16 OD1 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 79.2 ? 17 OD1 ? B ASN 297 ? B ASN 381 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 77.3 ? 18 O ? B ASN 305 ? B ASN 389 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 77.3 ? 19 OD1 ? B ASP 303 ? B ASP 387 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 98.6 ? 20 OD2 ? B ASP 295 ? B ASP 379 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 123.3 ? 21 O ? T HOH . ? B HOH 56 ? 1_555 CA ? Q CA . ? B CA 602 ? 1_555 O ? T HOH . ? B HOH 575 ? 1_555 157.8 ? 22 O ? B ASN 263 ? B ASN 347 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B ASP 213 ? B ASP 293 ? 1_555 87.2 ? 23 O ? B ASN 263 ? B ASN 347 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 OD2 ? B ASP 243 ? B ASP 324 ? 1_555 102.6 ? 24 O ? B ASP 213 ? B ASP 293 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 OD2 ? B ASP 243 ? B ASP 324 ? 1_555 93.8 ? 25 O ? B ASN 263 ? B ASN 347 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 217 ? B GLY 297 ? 1_555 167.7 ? 26 O ? B ASP 213 ? B ASP 293 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 217 ? B GLY 297 ? 1_555 84.2 ? 27 OD2 ? B ASP 243 ? B ASP 324 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 217 ? B GLY 297 ? 1_555 86.9 ? 28 O ? B ASN 263 ? B ASN 347 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 261 ? B GLY 345 ? 1_555 87.7 ? 29 O ? B ASP 213 ? B ASP 293 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 261 ? B GLY 345 ? 1_555 90.9 ? 30 OD2 ? B ASP 243 ? B ASP 324 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 261 ? B GLY 345 ? 1_555 168.9 ? 31 O ? B GLY 217 ? B GLY 297 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? B GLY 261 ? B GLY 345 ? 1_555 83.6 ? 32 O ? B ASN 263 ? B ASN 347 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? T HOH . ? B HOH 3 ? 1_555 94.7 ? 33 O ? B ASP 213 ? B ASP 293 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? T HOH . ? B HOH 3 ? 1_555 175.2 ? 34 OD2 ? B ASP 243 ? B ASP 324 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? T HOH . ? B HOH 3 ? 1_555 90.0 ? 35 O ? B GLY 217 ? B GLY 297 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? T HOH . ? B HOH 3 ? 1_555 93.2 ? 36 O ? B GLY 261 ? B GLY 345 ? 1_555 CA ? P CA . ? B CA 601 ? 1_555 O ? T HOH . ? B HOH 3 ? 1_555 84.8 ? 37 O ? A ASN 263 ? A ASN 347 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A ASP 213 ? A ASP 293 ? 1_555 88.8 ? 38 O ? A ASN 263 ? A ASN 347 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 OD2 ? A ASP 243 ? A ASP 324 ? 1_555 102.4 ? 39 O ? A ASP 213 ? A ASP 293 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 OD2 ? A ASP 243 ? A ASP 324 ? 1_555 92.9 ? 40 O ? A ASN 263 ? A ASN 347 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 261 ? A GLY 345 ? 1_555 87.6 ? 41 O ? A ASP 213 ? A ASP 293 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 261 ? A GLY 345 ? 1_555 91.2 ? 42 OD2 ? A ASP 243 ? A ASP 324 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 261 ? A GLY 345 ? 1_555 169.3 ? 43 O ? A ASN 263 ? A ASN 347 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 217 ? A GLY 297 ? 1_555 167.4 ? 44 O ? A ASP 213 ? A ASP 293 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 217 ? A GLY 297 ? 1_555 82.4 ? 45 OD2 ? A ASP 243 ? A ASP 324 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 217 ? A GLY 297 ? 1_555 87.1 ? 46 O ? A GLY 261 ? A GLY 345 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? A GLY 217 ? A GLY 297 ? 1_555 83.7 ? 47 O ? A ASN 263 ? A ASN 347 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? S HOH . ? A HOH 476 ? 1_555 95.6 ? 48 O ? A ASP 213 ? A ASP 293 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? S HOH . ? A HOH 476 ? 1_555 174.7 ? 49 OD2 ? A ASP 243 ? A ASP 324 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? S HOH . ? A HOH 476 ? 1_555 89.0 ? 50 O ? A GLY 261 ? A GLY 345 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? S HOH . ? A HOH 476 ? 1_555 86.0 ? 51 O ? A GLY 217 ? A GLY 297 ? 1_555 CA ? H CA . ? A CA 601 ? 1_555 O ? S HOH . ? A HOH 476 ? 1_555 92.8 ? 52 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 79.7 ? 53 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? A ASN 305 ? A ASN 389 ? 1_555 150.3 ? 54 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? A ASN 305 ? A ASN 389 ? 1_555 82.2 ? 55 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 114.4 ? 56 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 165.7 ? 57 O ? A ASN 305 ? A ASN 389 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 84.3 ? 58 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 105.1 ? 59 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 44.0 ? 60 O ? A ASN 305 ? A ASN 389 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 76.8 ? 61 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 127.8 ? 62 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 565 ? 1_555 75.2 ? 63 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 565 ? 1_555 81.7 ? 64 O ? A ASN 305 ? A ASN 389 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 565 ? 1_555 79.0 ? 65 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 565 ? 1_555 100.1 ? 66 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 565 ? 1_555 122.5 ? 67 OD1 ? A ASN 297 ? A ASN 381 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 85.4 ? 68 OD1 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 96.0 ? 69 O ? A ASN 305 ? A ASN 389 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 119.9 ? 70 OD1 ? A ASP 303 ? A ASP 387 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 86.9 ? 71 OD2 ? A ASP 295 ? A ASP 379 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 63.2 ? 72 O ? S HOH . ? A HOH 565 ? 1_555 CA ? I CA . ? A CA 602 ? 1_555 O ? S HOH . ? A HOH 493 ? 1_555 160.6 ? 73 O ? T HOH . ? B HOH 903 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 905 ? 1_555 111.8 ? 74 O ? T HOH . ? B HOH 903 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 902 ? 1_555 79.1 ? 75 O ? T HOH . ? B HOH 905 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 902 ? 1_555 103.1 ? 76 O ? T HOH . ? B HOH 903 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 488 ? 1_555 68.2 ? 77 O ? T HOH . ? B HOH 905 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 488 ? 1_555 180.0 ? 78 O ? T HOH . ? B HOH 902 ? 1_555 CA ? J CA . ? A CA 603 ? 1_555 O ? T HOH . ? B HOH 488 ? 1_555 76.9 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2010-09-22 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2014-02-26 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 14.7588 _pdbx_refine_tls.origin_y 23.2347 _pdbx_refine_tls.origin_z 43.1779 _pdbx_refine_tls.T[1][1] 0.0167 _pdbx_refine_tls.T[2][2] 0.0028 _pdbx_refine_tls.T[3][3] 0.0176 _pdbx_refine_tls.T[1][2] 0.0010 _pdbx_refine_tls.T[1][3] -0.0066 _pdbx_refine_tls.T[2][3] 0.0041 _pdbx_refine_tls.L[1][1] 0.1834 _pdbx_refine_tls.L[2][2] 0.0417 _pdbx_refine_tls.L[3][3] 0.1700 _pdbx_refine_tls.L[1][2] 0.0062 _pdbx_refine_tls.L[1][3] -0.0834 _pdbx_refine_tls.L[2][3] 0.0067 _pdbx_refine_tls.S[1][1] 0.0014 _pdbx_refine_tls.S[1][2] -0.0131 _pdbx_refine_tls.S[1][3] -0.0179 _pdbx_refine_tls.S[2][1] 0.0067 _pdbx_refine_tls.S[2][2] -0.0022 _pdbx_refine_tls.S[2][3] -0.0062 _pdbx_refine_tls.S[3][1] 0.0060 _pdbx_refine_tls.S[3][2] 0.0180 _pdbx_refine_tls.S[3][3] -0.0000 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details all # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal MAR345dtb 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.5_2)' ? 3 HKL-2000 'data reduction' . ? 4 SCALEPACK 'data scaling' . ? 5 # 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 ILE A 222 ? ? 59.40 70.99 2 1 THR A 225 ? ? -133.49 -157.61 3 1 ASP A 283 ? ? -160.55 114.54 4 1 CYS A 291 ? ? -129.09 -167.39 5 1 TRP A 295 ? ? -92.68 -62.22 6 1 HIS A 296 ? ? -153.31 24.55 7 1 LYS A 331 ? ? -161.27 -159.86 8 1 ASN A 347 ? ? 67.98 -168.02 9 1 SER A 404 ? ? -127.43 -156.13 10 1 TRP A 456 ? ? -165.49 -162.23 11 1 TRP A 458 ? ? -115.81 79.73 12 1 ILE B 222 ? ? 60.57 71.41 13 1 THR B 225 ? ? -131.03 -158.04 14 1 ALA B 250 ? ? -125.83 -168.70 15 1 ASN B 272 ? ? 76.54 -0.57 16 1 ASP B 283 ? ? -162.11 112.37 17 1 CYS B 291 ? ? -129.52 -165.17 18 1 TRP B 295 ? ? -94.10 -61.77 19 1 HIS B 296 ? ? -157.72 39.97 20 1 LYS B 331 ? ? -153.00 -158.69 21 1 ASN B 347 ? ? 68.33 -167.48 22 1 SER B 404 ? ? -120.73 -140.52 23 1 TRP B 456 ? ? -164.77 -161.14 24 1 TRP B 458 ? ? -115.96 79.25 # 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 LYS 470 ? A LYS 388 2 1 Y 1 B LYS 470 ? B LYS 388 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'CALCIUM ION' CA 5 'ACETATE ION' ACT 6 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 501 501 NAG NAG A . D 2 NAG 2 502 502 NAG NAG A . E 3 MAN 3 503 503 MAN MAN A . F 3 MAN 4 504 504 MAN MAN A . G 2 NAG 1 505 505 NAG NAG A . H 4 CA 1 601 601 CA CA A . I 4 CA 1 602 602 CA CA A . J 4 CA 1 603 603 CA CA A . K 5 ACT 1 1 1 ACT ACT A . L 5 ACT 1 471 471 ACT ACT A . M 5 ACT 1 472 472 ACT ACT A . N 2 NAG 1 501 501 NAG NAG B . O 2 NAG 1 502 502 NAG NAG B . P 4 CA 1 601 601 CA CA B . Q 4 CA 1 602 602 CA CA B . R 5 ACT 1 1 1 ACT ACT B . S 6 HOH 1 6 6 HOH HOH A . S 6 HOH 2 7 7 HOH HOH A . S 6 HOH 3 8 8 HOH HOH A . S 6 HOH 4 9 9 HOH HOH A . S 6 HOH 5 10 10 HOH HOH A . S 6 HOH 6 17 17 HOH HOH A . S 6 HOH 7 23 23 HOH HOH A . S 6 HOH 8 26 26 HOH HOH A . S 6 HOH 9 27 27 HOH HOH A . S 6 HOH 10 28 28 HOH HOH A . S 6 HOH 11 31 31 HOH HOH A . S 6 HOH 12 32 32 HOH HOH A . S 6 HOH 13 34 34 HOH HOH A . S 6 HOH 14 35 35 HOH HOH A . S 6 HOH 15 38 38 HOH HOH A . S 6 HOH 16 40 40 HOH HOH A . S 6 HOH 17 41 41 HOH HOH A . S 6 HOH 18 42 42 HOH HOH A . S 6 HOH 19 43 43 HOH HOH A . S 6 HOH 20 45 45 HOH HOH A . S 6 HOH 21 51 51 HOH HOH A . S 6 HOH 22 52 52 HOH HOH A . S 6 HOH 23 53 53 HOH HOH A . S 6 HOH 24 54 54 HOH HOH A . S 6 HOH 25 57 57 HOH HOH A . S 6 HOH 26 59 59 HOH HOH A . S 6 HOH 27 62 62 HOH HOH A . S 6 HOH 28 63 63 HOH HOH A . S 6 HOH 29 66 66 HOH HOH A . S 6 HOH 30 68 68 HOH HOH A . S 6 HOH 31 69 69 HOH HOH A . S 6 HOH 32 70 70 HOH HOH A . S 6 HOH 33 71 71 HOH HOH A . S 6 HOH 34 75 75 HOH HOH A . S 6 HOH 35 76 76 HOH HOH A . S 6 HOH 36 77 77 HOH HOH A . S 6 HOH 37 81 81 HOH HOH A . S 6 HOH 38 307 307 HOH HOH A . S 6 HOH 39 337 337 HOH HOH A . S 6 HOH 40 434 434 HOH HOH A . S 6 HOH 41 473 473 HOH HOH A . S 6 HOH 42 474 474 HOH HOH A . S 6 HOH 43 475 475 HOH HOH A . S 6 HOH 44 476 476 HOH HOH A . S 6 HOH 45 477 477 HOH HOH A . S 6 HOH 46 478 478 HOH HOH A . S 6 HOH 47 479 479 HOH HOH A . S 6 HOH 48 480 480 HOH HOH A . S 6 HOH 49 481 481 HOH HOH A . S 6 HOH 50 482 482 HOH HOH A . S 6 HOH 51 483 483 HOH HOH A . S 6 HOH 52 484 484 HOH HOH A . S 6 HOH 53 485 485 HOH HOH A . S 6 HOH 54 486 486 HOH HOH A . S 6 HOH 55 487 487 HOH HOH A . S 6 HOH 56 488 488 HOH HOH A . S 6 HOH 57 489 489 HOH HOH A . S 6 HOH 58 490 490 HOH HOH A . S 6 HOH 59 491 491 HOH HOH A . S 6 HOH 60 492 492 HOH HOH A . S 6 HOH 61 493 493 HOH HOH A . S 6 HOH 62 494 494 HOH HOH A . S 6 HOH 63 495 495 HOH HOH A . S 6 HOH 64 496 496 HOH HOH A . S 6 HOH 65 497 497 HOH HOH A . S 6 HOH 66 498 498 HOH HOH A . S 6 HOH 67 499 499 HOH HOH A . S 6 HOH 68 500 500 HOH HOH A . S 6 HOH 69 506 506 HOH HOH A . S 6 HOH 70 507 507 HOH HOH A . S 6 HOH 71 508 508 HOH HOH A . S 6 HOH 72 509 509 HOH HOH A . S 6 HOH 73 510 510 HOH HOH A . S 6 HOH 74 511 511 HOH HOH A . S 6 HOH 75 512 512 HOH HOH A . S 6 HOH 76 513 513 HOH HOH A . S 6 HOH 77 514 514 HOH HOH A . S 6 HOH 78 515 515 HOH HOH A . S 6 HOH 79 516 516 HOH HOH A . S 6 HOH 80 517 517 HOH HOH A . S 6 HOH 81 518 518 HOH HOH A . S 6 HOH 82 519 519 HOH HOH A . S 6 HOH 83 520 520 HOH HOH A . S 6 HOH 84 521 521 HOH HOH A . S 6 HOH 85 522 522 HOH HOH A . S 6 HOH 86 523 523 HOH HOH A . S 6 HOH 87 524 524 HOH HOH A . S 6 HOH 88 525 525 HOH HOH A . S 6 HOH 89 526 526 HOH HOH A . S 6 HOH 90 527 527 HOH HOH A . S 6 HOH 91 528 528 HOH HOH A . S 6 HOH 92 529 529 HOH HOH A . S 6 HOH 93 530 530 HOH HOH A . S 6 HOH 94 531 531 HOH HOH A . S 6 HOH 95 532 532 HOH HOH A . S 6 HOH 96 533 533 HOH HOH A . S 6 HOH 97 534 534 HOH HOH A . S 6 HOH 98 535 535 HOH HOH A . S 6 HOH 99 536 536 HOH HOH A . S 6 HOH 100 537 537 HOH HOH A . S 6 HOH 101 538 538 HOH HOH A . S 6 HOH 102 539 539 HOH HOH A . S 6 HOH 103 540 540 HOH HOH A . S 6 HOH 104 541 541 HOH HOH A . S 6 HOH 105 542 542 HOH HOH A . S 6 HOH 106 543 543 HOH HOH A . S 6 HOH 107 544 544 HOH HOH A . S 6 HOH 108 545 545 HOH HOH A . S 6 HOH 109 546 546 HOH HOH A . S 6 HOH 110 547 547 HOH HOH A . S 6 HOH 111 548 548 HOH HOH A . S 6 HOH 112 549 549 HOH HOH A . S 6 HOH 113 550 550 HOH HOH A . S 6 HOH 114 551 551 HOH HOH A . S 6 HOH 115 552 552 HOH HOH A . S 6 HOH 116 553 553 HOH HOH A . S 6 HOH 117 554 554 HOH HOH A . S 6 HOH 118 555 555 HOH HOH A . S 6 HOH 119 556 556 HOH HOH A . S 6 HOH 120 557 557 HOH HOH A . S 6 HOH 121 558 558 HOH HOH A . S 6 HOH 122 559 559 HOH HOH A . S 6 HOH 123 560 560 HOH HOH A . S 6 HOH 124 561 561 HOH HOH A . S 6 HOH 125 562 562 HOH HOH A . S 6 HOH 126 563 563 HOH HOH A . S 6 HOH 127 564 564 HOH HOH A . S 6 HOH 128 565 565 HOH HOH A . S 6 HOH 129 566 566 HOH HOH A . S 6 HOH 130 567 567 HOH HOH A . S 6 HOH 131 568 568 HOH HOH A . S 6 HOH 132 569 569 HOH HOH A . S 6 HOH 133 570 570 HOH HOH A . S 6 HOH 134 571 571 HOH HOH A . S 6 HOH 135 572 572 HOH HOH A . S 6 HOH 136 573 573 HOH HOH A . S 6 HOH 137 574 574 HOH HOH A . S 6 HOH 138 575 575 HOH HOH A . S 6 HOH 139 576 576 HOH HOH A . S 6 HOH 140 577 577 HOH HOH A . S 6 HOH 141 578 578 HOH HOH A . S 6 HOH 142 579 579 HOH HOH A . S 6 HOH 143 580 580 HOH HOH A . S 6 HOH 144 581 581 HOH HOH A . S 6 HOH 145 582 582 HOH HOH A . S 6 HOH 146 583 583 HOH HOH A . S 6 HOH 147 584 584 HOH HOH A . S 6 HOH 148 585 585 HOH HOH A . S 6 HOH 149 586 586 HOH HOH A . S 6 HOH 150 587 587 HOH HOH A . S 6 HOH 151 588 588 HOH HOH A . S 6 HOH 152 589 589 HOH HOH A . S 6 HOH 153 590 590 HOH HOH A . S 6 HOH 154 591 591 HOH HOH A . S 6 HOH 155 592 592 HOH HOH A . S 6 HOH 156 593 593 HOH HOH A . S 6 HOH 157 594 594 HOH HOH A . S 6 HOH 158 595 595 HOH HOH A . S 6 HOH 159 596 596 HOH HOH A . S 6 HOH 160 597 597 HOH HOH A . S 6 HOH 161 598 598 HOH HOH A . S 6 HOH 162 599 599 HOH HOH A . S 6 HOH 163 600 600 HOH HOH A . S 6 HOH 164 604 604 HOH HOH A . S 6 HOH 165 605 605 HOH HOH A . S 6 HOH 166 606 606 HOH HOH A . S 6 HOH 167 607 607 HOH HOH A . S 6 HOH 168 608 608 HOH HOH A . S 6 HOH 169 609 609 HOH HOH A . S 6 HOH 170 610 610 HOH HOH A . S 6 HOH 171 611 611 HOH HOH A . S 6 HOH 172 612 612 HOH HOH A . S 6 HOH 173 613 613 HOH HOH A . S 6 HOH 174 614 614 HOH HOH A . S 6 HOH 175 615 615 HOH HOH A . S 6 HOH 176 616 616 HOH HOH A . S 6 HOH 177 617 617 HOH HOH A . S 6 HOH 178 618 618 HOH HOH A . S 6 HOH 179 619 619 HOH HOH A . S 6 HOH 180 620 620 HOH HOH A . S 6 HOH 181 621 621 HOH HOH A . S 6 HOH 182 622 622 HOH HOH A . S 6 HOH 183 623 623 HOH HOH A . S 6 HOH 184 624 624 HOH HOH A . S 6 HOH 185 625 625 HOH HOH A . S 6 HOH 186 626 626 HOH HOH A . S 6 HOH 187 627 627 HOH HOH A . S 6 HOH 188 628 628 HOH HOH A . S 6 HOH 189 629 629 HOH HOH A . S 6 HOH 190 630 630 HOH HOH A . S 6 HOH 191 631 631 HOH HOH A . S 6 HOH 192 632 632 HOH HOH A . S 6 HOH 193 633 633 HOH HOH A . S 6 HOH 194 634 634 HOH HOH A . S 6 HOH 195 635 635 HOH HOH A . S 6 HOH 196 636 636 HOH HOH A . S 6 HOH 197 637 637 HOH HOH A . S 6 HOH 198 638 638 HOH HOH A . S 6 HOH 199 640 640 HOH HOH A . S 6 HOH 200 641 641 HOH HOH A . S 6 HOH 201 642 642 HOH HOH A . S 6 HOH 202 643 643 HOH HOH A . S 6 HOH 203 644 644 HOH HOH A . S 6 HOH 204 645 645 HOH HOH A . S 6 HOH 205 646 646 HOH HOH A . S 6 HOH 206 647 647 HOH HOH A . S 6 HOH 207 648 648 HOH HOH A . S 6 HOH 208 649 649 HOH HOH A . S 6 HOH 209 650 650 HOH HOH A . S 6 HOH 210 651 651 HOH HOH A . S 6 HOH 211 652 652 HOH HOH A . S 6 HOH 212 653 653 HOH HOH A . S 6 HOH 213 654 654 HOH HOH A . S 6 HOH 214 655 655 HOH HOH A . S 6 HOH 215 656 656 HOH HOH A . S 6 HOH 216 657 657 HOH HOH A . S 6 HOH 217 658 658 HOH HOH A . S 6 HOH 218 659 659 HOH HOH A . S 6 HOH 219 660 660 HOH HOH A . S 6 HOH 220 661 661 HOH HOH A . S 6 HOH 221 662 662 HOH HOH A . S 6 HOH 222 663 663 HOH HOH A . S 6 HOH 223 664 664 HOH HOH A . S 6 HOH 224 665 665 HOH HOH A . S 6 HOH 225 666 666 HOH HOH A . S 6 HOH 226 667 667 HOH HOH A . S 6 HOH 227 668 668 HOH HOH A . S 6 HOH 228 669 669 HOH HOH A . S 6 HOH 229 670 670 HOH HOH A . S 6 HOH 230 671 671 HOH HOH A . S 6 HOH 231 672 672 HOH HOH A . S 6 HOH 232 673 673 HOH HOH A . S 6 HOH 233 674 674 HOH HOH A . S 6 HOH 234 675 675 HOH HOH A . S 6 HOH 235 676 676 HOH HOH A . S 6 HOH 236 677 677 HOH HOH A . S 6 HOH 237 678 678 HOH HOH A . S 6 HOH 238 679 679 HOH HOH A . S 6 HOH 239 680 680 HOH HOH A . S 6 HOH 240 681 681 HOH HOH A . S 6 HOH 241 682 682 HOH HOH A . S 6 HOH 242 683 683 HOH HOH A . S 6 HOH 243 684 684 HOH HOH A . S 6 HOH 244 685 685 HOH HOH A . S 6 HOH 245 686 686 HOH HOH A . S 6 HOH 246 687 687 HOH HOH A . S 6 HOH 247 688 688 HOH HOH A . S 6 HOH 248 689 689 HOH HOH A . S 6 HOH 249 690 690 HOH HOH A . S 6 HOH 250 691 691 HOH HOH A . S 6 HOH 251 692 692 HOH HOH A . S 6 HOH 252 693 693 HOH HOH A . S 6 HOH 253 694 694 HOH HOH A . S 6 HOH 254 695 695 HOH HOH A . S 6 HOH 255 696 696 HOH HOH A . S 6 HOH 256 697 697 HOH HOH A . S 6 HOH 257 698 698 HOH HOH A . S 6 HOH 258 699 699 HOH HOH A . S 6 HOH 259 700 700 HOH HOH A . S 6 HOH 260 701 701 HOH HOH A . S 6 HOH 261 702 702 HOH HOH A . S 6 HOH 262 703 703 HOH HOH A . S 6 HOH 263 704 704 HOH HOH A . S 6 HOH 264 705 705 HOH HOH A . S 6 HOH 265 706 706 HOH HOH A . S 6 HOH 266 707 707 HOH HOH A . S 6 HOH 267 708 708 HOH HOH A . S 6 HOH 268 709 709 HOH HOH A . S 6 HOH 269 710 710 HOH HOH A . S 6 HOH 270 711 711 HOH HOH A . S 6 HOH 271 712 712 HOH HOH A . S 6 HOH 272 713 713 HOH HOH A . S 6 HOH 273 714 714 HOH HOH A . S 6 HOH 274 715 715 HOH HOH A . S 6 HOH 275 716 716 HOH HOH A . S 6 HOH 276 717 717 HOH HOH A . S 6 HOH 277 718 718 HOH HOH A . S 6 HOH 278 719 719 HOH HOH A . S 6 HOH 279 720 720 HOH HOH A . S 6 HOH 280 721 721 HOH HOH A . S 6 HOH 281 722 722 HOH HOH A . S 6 HOH 282 723 723 HOH HOH A . S 6 HOH 283 724 724 HOH HOH A . S 6 HOH 284 725 725 HOH HOH A . S 6 HOH 285 726 726 HOH HOH A . S 6 HOH 286 727 727 HOH HOH A . S 6 HOH 287 728 728 HOH HOH A . S 6 HOH 288 729 729 HOH HOH A . S 6 HOH 289 730 730 HOH HOH A . S 6 HOH 290 731 731 HOH HOH A . S 6 HOH 291 732 732 HOH HOH A . S 6 HOH 292 733 733 HOH HOH A . S 6 HOH 293 734 734 HOH HOH A . S 6 HOH 294 735 735 HOH HOH A . S 6 HOH 295 736 736 HOH HOH A . S 6 HOH 296 737 737 HOH HOH A . S 6 HOH 297 738 738 HOH HOH A . S 6 HOH 298 739 739 HOH HOH A . S 6 HOH 299 740 740 HOH HOH A . S 6 HOH 300 741 741 HOH HOH A . S 6 HOH 301 742 742 HOH HOH A . S 6 HOH 302 743 743 HOH HOH A . S 6 HOH 303 744 744 HOH HOH A . S 6 HOH 304 745 745 HOH HOH A . S 6 HOH 305 746 746 HOH HOH A . S 6 HOH 306 747 747 HOH HOH A . S 6 HOH 307 748 748 HOH HOH A . S 6 HOH 308 749 749 HOH HOH A . S 6 HOH 309 750 750 HOH HOH A . S 6 HOH 310 752 752 HOH HOH A . S 6 HOH 311 753 753 HOH HOH A . S 6 HOH 312 754 754 HOH HOH A . S 6 HOH 313 755 755 HOH HOH A . S 6 HOH 314 756 756 HOH HOH A . S 6 HOH 315 757 757 HOH HOH A . S 6 HOH 316 758 758 HOH HOH A . S 6 HOH 317 759 759 HOH HOH A . S 6 HOH 318 760 760 HOH HOH A . S 6 HOH 319 761 761 HOH HOH A . S 6 HOH 320 762 762 HOH HOH A . S 6 HOH 321 763 763 HOH HOH A . S 6 HOH 322 764 764 HOH HOH A . S 6 HOH 323 765 765 HOH HOH A . S 6 HOH 324 766 766 HOH HOH A . S 6 HOH 325 767 767 HOH HOH A . S 6 HOH 326 768 768 HOH HOH A . S 6 HOH 327 769 769 HOH HOH A . S 6 HOH 328 770 770 HOH HOH A . S 6 HOH 329 771 771 HOH HOH A . S 6 HOH 330 772 772 HOH HOH A . S 6 HOH 331 773 773 HOH HOH A . S 6 HOH 332 774 774 HOH HOH A . S 6 HOH 333 775 775 HOH HOH A . S 6 HOH 334 776 776 HOH HOH A . S 6 HOH 335 777 777 HOH HOH A . S 6 HOH 336 778 778 HOH HOH A . S 6 HOH 337 779 779 HOH HOH A . S 6 HOH 338 780 780 HOH HOH A . S 6 HOH 339 781 781 HOH HOH A . S 6 HOH 340 782 782 HOH HOH A . S 6 HOH 341 783 783 HOH HOH A . S 6 HOH 342 784 784 HOH HOH A . S 6 HOH 343 785 785 HOH HOH A . S 6 HOH 344 786 786 HOH HOH A . S 6 HOH 345 787 787 HOH HOH A . S 6 HOH 346 788 788 HOH HOH A . S 6 HOH 347 789 789 HOH HOH A . S 6 HOH 348 790 790 HOH HOH A . S 6 HOH 349 791 791 HOH HOH A . S 6 HOH 350 792 792 HOH HOH A . S 6 HOH 351 793 793 HOH HOH A . S 6 HOH 352 794 794 HOH HOH A . S 6 HOH 353 795 795 HOH HOH A . S 6 HOH 354 796 796 HOH HOH A . S 6 HOH 355 797 797 HOH HOH A . S 6 HOH 356 798 798 HOH HOH A . S 6 HOH 357 799 799 HOH HOH A . S 6 HOH 358 800 800 HOH HOH A . S 6 HOH 359 801 801 HOH HOH A . S 6 HOH 360 802 802 HOH HOH A . S 6 HOH 361 803 803 HOH HOH A . S 6 HOH 362 804 804 HOH HOH A . S 6 HOH 363 805 805 HOH HOH A . S 6 HOH 364 806 806 HOH HOH A . S 6 HOH 365 807 807 HOH HOH A . S 6 HOH 366 808 808 HOH HOH A . S 6 HOH 367 809 809 HOH HOH A . S 6 HOH 368 810 810 HOH HOH A . S 6 HOH 369 811 811 HOH HOH A . S 6 HOH 370 812 812 HOH HOH A . S 6 HOH 371 813 813 HOH HOH A . S 6 HOH 372 814 814 HOH HOH A . S 6 HOH 373 815 815 HOH HOH A . S 6 HOH 374 816 816 HOH HOH A . S 6 HOH 375 817 817 HOH HOH A . S 6 HOH 376 818 818 HOH HOH A . S 6 HOH 377 819 819 HOH HOH A . S 6 HOH 378 820 820 HOH HOH A . S 6 HOH 379 821 821 HOH HOH A . S 6 HOH 380 822 822 HOH HOH A . S 6 HOH 381 823 823 HOH HOH A . S 6 HOH 382 824 824 HOH HOH A . S 6 HOH 383 825 825 HOH HOH A . S 6 HOH 384 826 826 HOH HOH A . S 6 HOH 385 827 827 HOH HOH A . S 6 HOH 386 828 828 HOH HOH A . S 6 HOH 387 829 829 HOH HOH A . S 6 HOH 388 830 830 HOH HOH A . S 6 HOH 389 831 831 HOH HOH A . S 6 HOH 390 832 832 HOH HOH A . S 6 HOH 391 833 833 HOH HOH A . S 6 HOH 392 834 834 HOH HOH A . S 6 HOH 393 835 835 HOH HOH A . S 6 HOH 394 836 836 HOH HOH A . S 6 HOH 395 837 837 HOH HOH A . S 6 HOH 396 838 838 HOH HOH A . S 6 HOH 397 839 839 HOH HOH A . S 6 HOH 398 840 840 HOH HOH A . S 6 HOH 399 841 841 HOH HOH A . S 6 HOH 400 842 842 HOH HOH A . S 6 HOH 401 843 843 HOH HOH A . S 6 HOH 402 844 844 HOH HOH A . S 6 HOH 403 845 845 HOH HOH A . S 6 HOH 404 846 846 HOH HOH A . S 6 HOH 405 847 847 HOH HOH A . S 6 HOH 406 848 848 HOH HOH A . S 6 HOH 407 849 849 HOH HOH A . S 6 HOH 408 850 850 HOH HOH A . S 6 HOH 409 851 851 HOH HOH A . S 6 HOH 410 852 852 HOH HOH A . S 6 HOH 411 853 853 HOH HOH A . S 6 HOH 412 854 854 HOH HOH A . S 6 HOH 413 855 855 HOH HOH A . S 6 HOH 414 856 856 HOH HOH A . S 6 HOH 415 857 857 HOH HOH A . S 6 HOH 416 858 858 HOH HOH A . S 6 HOH 417 859 859 HOH HOH A . S 6 HOH 418 860 860 HOH HOH A . S 6 HOH 419 861 861 HOH HOH A . S 6 HOH 420 862 862 HOH HOH A . S 6 HOH 421 863 863 HOH HOH A . S 6 HOH 422 864 864 HOH HOH A . S 6 HOH 423 865 865 HOH HOH A . S 6 HOH 424 866 866 HOH HOH A . S 6 HOH 425 867 867 HOH HOH A . S 6 HOH 426 868 868 HOH HOH A . S 6 HOH 427 869 869 HOH HOH A . S 6 HOH 428 870 870 HOH HOH A . S 6 HOH 429 871 871 HOH HOH A . S 6 HOH 430 872 872 HOH HOH A . S 6 HOH 431 873 873 HOH HOH A . S 6 HOH 432 874 874 HOH HOH A . S 6 HOH 433 875 875 HOH HOH A . S 6 HOH 434 876 876 HOH HOH A . S 6 HOH 435 877 877 HOH HOH A . S 6 HOH 436 878 878 HOH HOH A . S 6 HOH 437 879 879 HOH HOH A . S 6 HOH 438 880 880 HOH HOH A . S 6 HOH 439 881 881 HOH HOH A . S 6 HOH 440 882 882 HOH HOH A . S 6 HOH 441 883 883 HOH HOH A . S 6 HOH 442 884 884 HOH HOH A . S 6 HOH 443 885 885 HOH HOH A . S 6 HOH 444 886 886 HOH HOH A . S 6 HOH 445 887 887 HOH HOH A . S 6 HOH 446 888 888 HOH HOH A . S 6 HOH 447 889 889 HOH HOH A . S 6 HOH 448 891 891 HOH HOH A . S 6 HOH 449 892 892 HOH HOH A . S 6 HOH 450 893 893 HOH HOH A . S 6 HOH 451 894 894 HOH HOH A . S 6 HOH 452 895 895 HOH HOH A . S 6 HOH 453 896 896 HOH HOH A . S 6 HOH 454 897 897 HOH HOH A . S 6 HOH 455 898 898 HOH HOH A . S 6 HOH 456 900 900 HOH HOH A . S 6 HOH 457 901 901 HOH HOH A . T 6 HOH 1 2 2 HOH HOH B . T 6 HOH 2 3 3 HOH HOH B . T 6 HOH 3 4 4 HOH HOH B . T 6 HOH 4 5 5 HOH HOH B . T 6 HOH 5 11 11 HOH HOH B . T 6 HOH 6 12 12 HOH HOH B . T 6 HOH 7 13 13 HOH HOH B . T 6 HOH 8 14 14 HOH HOH B . T 6 HOH 9 15 15 HOH HOH B . T 6 HOH 10 16 16 HOH HOH B . T 6 HOH 11 18 18 HOH HOH B . T 6 HOH 12 19 19 HOH HOH B . T 6 HOH 13 20 20 HOH HOH B . T 6 HOH 14 21 21 HOH HOH B . T 6 HOH 15 22 22 HOH HOH B . T 6 HOH 16 24 24 HOH HOH B . T 6 HOH 17 25 25 HOH HOH B . T 6 HOH 18 29 29 HOH HOH B . T 6 HOH 19 30 30 HOH HOH B . T 6 HOH 20 33 33 HOH HOH B . T 6 HOH 21 36 36 HOH HOH B . T 6 HOH 22 37 37 HOH HOH B . T 6 HOH 23 39 39 HOH HOH B . T 6 HOH 24 44 44 HOH HOH B . T 6 HOH 25 46 46 HOH HOH B . T 6 HOH 26 47 47 HOH HOH B . T 6 HOH 27 48 48 HOH HOH B . T 6 HOH 28 49 49 HOH HOH B . T 6 HOH 29 50 50 HOH HOH B . T 6 HOH 30 55 55 HOH HOH B . T 6 HOH 31 56 56 HOH HOH B . T 6 HOH 32 58 58 HOH HOH B . T 6 HOH 33 60 60 HOH HOH B . T 6 HOH 34 61 61 HOH HOH B . T 6 HOH 35 64 64 HOH HOH B . T 6 HOH 36 65 65 HOH HOH B . T 6 HOH 37 67 67 HOH HOH B . T 6 HOH 38 72 72 HOH HOH B . T 6 HOH 39 73 73 HOH HOH B . T 6 HOH 40 74 74 HOH HOH B . T 6 HOH 41 78 78 HOH HOH B . T 6 HOH 42 79 79 HOH HOH B . T 6 HOH 43 80 80 HOH HOH B . T 6 HOH 44 334 334 HOH HOH B . T 6 HOH 45 338 338 HOH HOH B . T 6 HOH 46 393 393 HOH HOH B . T 6 HOH 47 471 471 HOH HOH B . T 6 HOH 48 472 472 HOH HOH B . T 6 HOH 49 473 473 HOH HOH B . T 6 HOH 50 474 474 HOH HOH B . T 6 HOH 51 475 475 HOH HOH B . T 6 HOH 52 476 476 HOH HOH B . T 6 HOH 53 477 477 HOH HOH B . T 6 HOH 54 478 478 HOH HOH B . T 6 HOH 55 479 479 HOH HOH B . T 6 HOH 56 480 480 HOH HOH B . T 6 HOH 57 481 481 HOH HOH B . T 6 HOH 58 482 482 HOH HOH B . T 6 HOH 59 483 483 HOH HOH B . T 6 HOH 60 484 484 HOH HOH B . T 6 HOH 61 485 485 HOH HOH B . T 6 HOH 62 486 486 HOH HOH B . T 6 HOH 63 487 487 HOH HOH B . T 6 HOH 64 488 488 HOH HOH B . T 6 HOH 65 489 489 HOH HOH B . T 6 HOH 66 490 490 HOH HOH B . T 6 HOH 67 491 491 HOH HOH B . T 6 HOH 68 492 492 HOH HOH B . T 6 HOH 69 493 493 HOH HOH B . T 6 HOH 70 494 494 HOH HOH B . T 6 HOH 71 495 495 HOH HOH B . T 6 HOH 72 496 496 HOH HOH B . T 6 HOH 73 497 497 HOH HOH B . T 6 HOH 74 498 498 HOH HOH B . T 6 HOH 75 499 499 HOH HOH B . T 6 HOH 76 500 500 HOH HOH B . T 6 HOH 77 503 503 HOH HOH B . T 6 HOH 78 504 504 HOH HOH B . T 6 HOH 79 505 505 HOH HOH B . T 6 HOH 80 506 506 HOH HOH B . T 6 HOH 81 507 507 HOH HOH B . T 6 HOH 82 508 508 HOH HOH B . T 6 HOH 83 509 509 HOH HOH B . T 6 HOH 84 510 510 HOH HOH B . T 6 HOH 85 511 511 HOH HOH B . T 6 HOH 86 512 512 HOH HOH B . T 6 HOH 87 513 513 HOH HOH B . T 6 HOH 88 514 514 HOH HOH B . T 6 HOH 89 515 515 HOH HOH B . T 6 HOH 90 516 516 HOH HOH B . T 6 HOH 91 517 517 HOH HOH B . T 6 HOH 92 518 518 HOH HOH B . T 6 HOH 93 519 519 HOH HOH B . T 6 HOH 94 520 520 HOH HOH B . T 6 HOH 95 521 521 HOH HOH B . T 6 HOH 96 522 522 HOH HOH B . T 6 HOH 97 523 523 HOH HOH B . T 6 HOH 98 524 524 HOH HOH B . T 6 HOH 99 525 525 HOH HOH B . T 6 HOH 100 526 526 HOH HOH B . T 6 HOH 101 527 527 HOH HOH B . T 6 HOH 102 528 528 HOH HOH B . T 6 HOH 103 529 529 HOH HOH B . T 6 HOH 104 530 530 HOH HOH B . T 6 HOH 105 531 531 HOH HOH B . T 6 HOH 106 532 532 HOH HOH B . T 6 HOH 107 533 533 HOH HOH B . T 6 HOH 108 534 534 HOH HOH B . T 6 HOH 109 535 535 HOH HOH B . T 6 HOH 110 536 536 HOH HOH B . T 6 HOH 111 537 537 HOH HOH B . T 6 HOH 112 538 538 HOH HOH B . T 6 HOH 113 539 539 HOH HOH B . T 6 HOH 114 540 540 HOH HOH B . T 6 HOH 115 541 541 HOH HOH B . T 6 HOH 116 542 542 HOH HOH B . T 6 HOH 117 543 543 HOH HOH B . T 6 HOH 118 544 544 HOH HOH B . T 6 HOH 119 545 545 HOH HOH B . T 6 HOH 120 546 546 HOH HOH B . T 6 HOH 121 547 547 HOH HOH B . T 6 HOH 122 548 548 HOH HOH B . T 6 HOH 123 549 549 HOH HOH B . T 6 HOH 124 550 550 HOH HOH B . T 6 HOH 125 551 551 HOH HOH B . T 6 HOH 126 552 552 HOH HOH B . T 6 HOH 127 553 553 HOH HOH B . T 6 HOH 128 554 554 HOH HOH B . T 6 HOH 129 555 555 HOH HOH B . T 6 HOH 130 556 556 HOH HOH B . T 6 HOH 131 557 557 HOH HOH B . T 6 HOH 132 558 558 HOH HOH B . T 6 HOH 133 559 559 HOH HOH B . T 6 HOH 134 560 560 HOH HOH B . T 6 HOH 135 561 561 HOH HOH B . T 6 HOH 136 562 562 HOH HOH B . T 6 HOH 137 563 563 HOH HOH B . T 6 HOH 138 564 564 HOH HOH B . T 6 HOH 139 565 565 HOH HOH B . T 6 HOH 140 566 566 HOH HOH B . T 6 HOH 141 567 567 HOH HOH B . T 6 HOH 142 568 568 HOH HOH B . T 6 HOH 143 569 569 HOH HOH B . T 6 HOH 144 570 570 HOH HOH B . T 6 HOH 145 571 571 HOH HOH B . T 6 HOH 146 572 572 HOH HOH B . T 6 HOH 147 573 573 HOH HOH B . T 6 HOH 148 574 574 HOH HOH B . T 6 HOH 149 575 575 HOH HOH B . T 6 HOH 150 576 576 HOH HOH B . T 6 HOH 151 577 577 HOH HOH B . T 6 HOH 152 578 578 HOH HOH B . T 6 HOH 153 579 579 HOH HOH B . T 6 HOH 154 580 580 HOH HOH B . T 6 HOH 155 581 581 HOH HOH B . T 6 HOH 156 582 582 HOH HOH B . T 6 HOH 157 583 583 HOH HOH B . T 6 HOH 158 584 584 HOH HOH B . T 6 HOH 159 585 585 HOH HOH B . T 6 HOH 160 586 586 HOH HOH B . T 6 HOH 161 587 587 HOH HOH B . T 6 HOH 162 588 588 HOH HOH B . T 6 HOH 163 589 589 HOH HOH B . T 6 HOH 164 590 590 HOH HOH B . T 6 HOH 165 591 591 HOH HOH B . T 6 HOH 166 592 592 HOH HOH B . T 6 HOH 167 593 593 HOH HOH B . T 6 HOH 168 594 594 HOH HOH B . T 6 HOH 169 595 595 HOH HOH B . T 6 HOH 170 596 596 HOH HOH B . T 6 HOH 171 597 597 HOH HOH B . T 6 HOH 172 598 598 HOH HOH B . T 6 HOH 173 599 599 HOH HOH B . T 6 HOH 174 600 600 HOH HOH B . T 6 HOH 175 603 603 HOH HOH B . T 6 HOH 176 604 604 HOH HOH B . T 6 HOH 177 605 605 HOH HOH B . T 6 HOH 178 606 606 HOH HOH B . T 6 HOH 179 607 607 HOH HOH B . T 6 HOH 180 608 608 HOH HOH B . T 6 HOH 181 609 609 HOH HOH B . T 6 HOH 182 610 610 HOH HOH B . T 6 HOH 183 611 611 HOH HOH B . T 6 HOH 184 612 612 HOH HOH B . T 6 HOH 185 613 613 HOH HOH B . T 6 HOH 186 614 614 HOH HOH B . T 6 HOH 187 615 615 HOH HOH B . T 6 HOH 188 616 616 HOH HOH B . T 6 HOH 189 617 617 HOH HOH B . T 6 HOH 190 618 618 HOH HOH B . T 6 HOH 191 619 619 HOH HOH B . T 6 HOH 192 620 620 HOH HOH B . T 6 HOH 193 621 621 HOH HOH B . T 6 HOH 194 622 622 HOH HOH B . T 6 HOH 195 623 623 HOH HOH B . T 6 HOH 196 624 624 HOH HOH B . T 6 HOH 197 625 625 HOH HOH B . T 6 HOH 198 626 626 HOH HOH B . T 6 HOH 199 627 627 HOH HOH B . T 6 HOH 200 628 628 HOH HOH B . T 6 HOH 201 629 629 HOH HOH B . T 6 HOH 202 630 630 HOH HOH B . T 6 HOH 203 631 631 HOH HOH B . T 6 HOH 204 632 632 HOH HOH B . T 6 HOH 205 633 633 HOH HOH B . T 6 HOH 206 634 634 HOH HOH B . T 6 HOH 207 635 635 HOH HOH B . T 6 HOH 208 636 636 HOH HOH B . T 6 HOH 209 637 637 HOH HOH B . T 6 HOH 210 638 638 HOH HOH B . T 6 HOH 211 639 639 HOH HOH B . T 6 HOH 212 640 640 HOH HOH B . T 6 HOH 213 641 641 HOH HOH B . T 6 HOH 214 642 642 HOH HOH B . T 6 HOH 215 643 643 HOH HOH B . T 6 HOH 216 644 644 HOH HOH B . T 6 HOH 217 645 645 HOH HOH B . T 6 HOH 218 646 646 HOH HOH B . T 6 HOH 219 648 648 HOH HOH B . T 6 HOH 220 650 650 HOH HOH B . T 6 HOH 221 651 651 HOH HOH B . T 6 HOH 222 652 652 HOH HOH B . T 6 HOH 223 653 653 HOH HOH B . T 6 HOH 224 654 654 HOH HOH B . T 6 HOH 225 655 655 HOH HOH B . T 6 HOH 226 656 656 HOH HOH B . T 6 HOH 227 657 657 HOH HOH B . T 6 HOH 228 658 658 HOH HOH B . T 6 HOH 229 659 659 HOH HOH B . T 6 HOH 230 660 660 HOH HOH B . T 6 HOH 231 661 661 HOH HOH B . T 6 HOH 232 662 662 HOH HOH B . T 6 HOH 233 663 663 HOH HOH B . T 6 HOH 234 664 664 HOH HOH B . T 6 HOH 235 665 665 HOH HOH B . T 6 HOH 236 666 666 HOH HOH B . T 6 HOH 237 667 667 HOH HOH B . T 6 HOH 238 668 668 HOH HOH B . T 6 HOH 239 669 669 HOH HOH B . T 6 HOH 240 670 670 HOH HOH B . T 6 HOH 241 671 671 HOH HOH B . T 6 HOH 242 672 672 HOH HOH B . T 6 HOH 243 673 673 HOH HOH B . T 6 HOH 244 674 674 HOH HOH B . T 6 HOH 245 675 675 HOH HOH B . T 6 HOH 246 676 676 HOH HOH B . T 6 HOH 247 677 677 HOH HOH B . T 6 HOH 248 678 678 HOH HOH B . T 6 HOH 249 679 679 HOH HOH B . T 6 HOH 250 680 680 HOH HOH B . T 6 HOH 251 681 681 HOH HOH B . T 6 HOH 252 682 682 HOH HOH B . T 6 HOH 253 683 683 HOH HOH B . T 6 HOH 254 685 685 HOH HOH B . T 6 HOH 255 686 686 HOH HOH B . T 6 HOH 256 687 687 HOH HOH B . T 6 HOH 257 688 688 HOH HOH B . T 6 HOH 258 689 689 HOH HOH B . T 6 HOH 259 690 690 HOH HOH B . T 6 HOH 260 691 691 HOH HOH B . T 6 HOH 261 692 692 HOH HOH B . T 6 HOH 262 693 693 HOH HOH B . T 6 HOH 263 694 694 HOH HOH B . T 6 HOH 264 695 695 HOH HOH B . T 6 HOH 265 696 696 HOH HOH B . T 6 HOH 266 697 697 HOH HOH B . T 6 HOH 267 698 698 HOH HOH B . T 6 HOH 268 699 699 HOH HOH B . T 6 HOH 269 700 700 HOH HOH B . T 6 HOH 270 701 701 HOH HOH B . T 6 HOH 271 702 702 HOH HOH B . T 6 HOH 272 703 703 HOH HOH B . T 6 HOH 273 704 704 HOH HOH B . T 6 HOH 274 705 705 HOH HOH B . T 6 HOH 275 706 706 HOH HOH B . T 6 HOH 276 707 707 HOH HOH B . T 6 HOH 277 708 708 HOH HOH B . T 6 HOH 278 709 709 HOH HOH B . T 6 HOH 279 710 710 HOH HOH B . T 6 HOH 280 711 711 HOH HOH B . T 6 HOH 281 712 712 HOH HOH B . T 6 HOH 282 713 713 HOH HOH B . T 6 HOH 283 714 714 HOH HOH B . T 6 HOH 284 715 715 HOH HOH B . T 6 HOH 285 716 716 HOH HOH B . T 6 HOH 286 717 717 HOH HOH B . T 6 HOH 287 718 718 HOH HOH B . T 6 HOH 288 719 719 HOH HOH B . T 6 HOH 289 720 720 HOH HOH B . T 6 HOH 290 721 721 HOH HOH B . T 6 HOH 291 722 722 HOH HOH B . T 6 HOH 292 723 723 HOH HOH B . T 6 HOH 293 724 724 HOH HOH B . T 6 HOH 294 725 725 HOH HOH B . T 6 HOH 295 726 726 HOH HOH B . T 6 HOH 296 727 727 HOH HOH B . T 6 HOH 297 728 728 HOH HOH B . T 6 HOH 298 729 729 HOH HOH B . T 6 HOH 299 730 730 HOH HOH B . T 6 HOH 300 731 731 HOH HOH B . T 6 HOH 301 732 732 HOH HOH B . T 6 HOH 302 733 733 HOH HOH B . T 6 HOH 303 734 734 HOH HOH B . T 6 HOH 304 735 735 HOH HOH B . T 6 HOH 305 736 736 HOH HOH B . T 6 HOH 306 737 737 HOH HOH B . T 6 HOH 307 738 738 HOH HOH B . T 6 HOH 308 739 739 HOH HOH B . T 6 HOH 309 741 741 HOH HOH B . T 6 HOH 310 742 742 HOH HOH B . T 6 HOH 311 743 743 HOH HOH B . T 6 HOH 312 744 744 HOH HOH B . T 6 HOH 313 745 745 HOH HOH B . T 6 HOH 314 746 746 HOH HOH B . T 6 HOH 315 747 747 HOH HOH B . T 6 HOH 316 748 748 HOH HOH B . T 6 HOH 317 749 749 HOH HOH B . T 6 HOH 318 750 750 HOH HOH B . T 6 HOH 319 751 751 HOH HOH B . T 6 HOH 320 752 752 HOH HOH B . T 6 HOH 321 753 753 HOH HOH B . T 6 HOH 322 755 755 HOH HOH B . T 6 HOH 323 756 756 HOH HOH B . T 6 HOH 324 757 757 HOH HOH B . T 6 HOH 325 758 758 HOH HOH B . T 6 HOH 326 759 759 HOH HOH B . T 6 HOH 327 760 760 HOH HOH B . T 6 HOH 328 761 761 HOH HOH B . T 6 HOH 329 762 762 HOH HOH B . T 6 HOH 330 763 763 HOH HOH B . T 6 HOH 331 764 764 HOH HOH B . T 6 HOH 332 765 765 HOH HOH B . T 6 HOH 333 766 766 HOH HOH B . T 6 HOH 334 767 767 HOH HOH B . T 6 HOH 335 768 768 HOH HOH B . T 6 HOH 336 769 769 HOH HOH B . T 6 HOH 337 770 770 HOH HOH B . T 6 HOH 338 771 771 HOH HOH B . T 6 HOH 339 772 772 HOH HOH B . T 6 HOH 340 773 773 HOH HOH B . T 6 HOH 341 774 774 HOH HOH B . T 6 HOH 342 775 775 HOH HOH B . T 6 HOH 343 776 776 HOH HOH B . T 6 HOH 344 777 777 HOH HOH B . T 6 HOH 345 778 778 HOH HOH B . T 6 HOH 346 779 779 HOH HOH B . T 6 HOH 347 780 780 HOH HOH B . T 6 HOH 348 781 781 HOH HOH B . T 6 HOH 349 782 782 HOH HOH B . T 6 HOH 350 783 783 HOH HOH B . T 6 HOH 351 784 784 HOH HOH B . T 6 HOH 352 785 785 HOH HOH B . T 6 HOH 353 786 786 HOH HOH B . T 6 HOH 354 787 787 HOH HOH B . T 6 HOH 355 788 788 HOH HOH B . T 6 HOH 356 789 789 HOH HOH B . T 6 HOH 357 790 790 HOH HOH B . T 6 HOH 358 791 791 HOH HOH B . T 6 HOH 359 792 792 HOH HOH B . T 6 HOH 360 793 793 HOH HOH B . T 6 HOH 361 794 794 HOH HOH B . T 6 HOH 362 795 795 HOH HOH B . T 6 HOH 363 796 796 HOH HOH B . T 6 HOH 364 797 797 HOH HOH B . T 6 HOH 365 798 798 HOH HOH B . T 6 HOH 366 799 799 HOH HOH B . T 6 HOH 367 800 800 HOH HOH B . T 6 HOH 368 801 801 HOH HOH B . T 6 HOH 369 802 802 HOH HOH B . T 6 HOH 370 803 803 HOH HOH B . T 6 HOH 371 804 804 HOH HOH B . T 6 HOH 372 805 805 HOH HOH B . T 6 HOH 373 806 806 HOH HOH B . T 6 HOH 374 807 807 HOH HOH B . T 6 HOH 375 808 808 HOH HOH B . T 6 HOH 376 809 809 HOH HOH B . T 6 HOH 377 810 810 HOH HOH B . T 6 HOH 378 811 811 HOH HOH B . T 6 HOH 379 813 813 HOH HOH B . T 6 HOH 380 814 814 HOH HOH B . T 6 HOH 381 815 815 HOH HOH B . T 6 HOH 382 816 816 HOH HOH B . T 6 HOH 383 817 817 HOH HOH B . T 6 HOH 384 818 818 HOH HOH B . T 6 HOH 385 819 819 HOH HOH B . T 6 HOH 386 820 820 HOH HOH B . T 6 HOH 387 821 821 HOH HOH B . T 6 HOH 388 822 822 HOH HOH B . T 6 HOH 389 823 823 HOH HOH B . T 6 HOH 390 824 824 HOH HOH B . T 6 HOH 391 825 825 HOH HOH B . T 6 HOH 392 826 826 HOH HOH B . T 6 HOH 393 827 827 HOH HOH B . T 6 HOH 394 828 828 HOH HOH B . T 6 HOH 395 829 829 HOH HOH B . T 6 HOH 396 831 831 HOH HOH B . T 6 HOH 397 832 832 HOH HOH B . T 6 HOH 398 833 833 HOH HOH B . T 6 HOH 399 835 835 HOH HOH B . T 6 HOH 400 838 838 HOH HOH B . T 6 HOH 401 839 839 HOH HOH B . T 6 HOH 402 840 840 HOH HOH B . T 6 HOH 403 842 842 HOH HOH B . T 6 HOH 404 847 847 HOH HOH B . T 6 HOH 405 849 849 HOH HOH B . T 6 HOH 406 850 850 HOH HOH B . T 6 HOH 407 851 851 HOH HOH B . T 6 HOH 408 854 854 HOH HOH B . T 6 HOH 409 855 855 HOH HOH B . T 6 HOH 410 857 857 HOH HOH B . T 6 HOH 411 859 859 HOH HOH B . T 6 HOH 412 861 861 HOH HOH B . T 6 HOH 413 862 862 HOH HOH B . T 6 HOH 414 866 866 HOH HOH B . T 6 HOH 415 867 867 HOH HOH B . T 6 HOH 416 868 868 HOH HOH B . T 6 HOH 417 869 869 HOH HOH B . T 6 HOH 418 870 870 HOH HOH B . T 6 HOH 419 872 872 HOH HOH B . T 6 HOH 420 873 873 HOH HOH B . T 6 HOH 421 874 874 HOH HOH B . T 6 HOH 422 875 875 HOH HOH B . T 6 HOH 423 879 879 HOH HOH B . T 6 HOH 424 887 887 HOH HOH B . T 6 HOH 425 894 894 HOH HOH B . T 6 HOH 426 895 895 HOH HOH B . T 6 HOH 427 896 896 HOH HOH B . T 6 HOH 428 898 898 HOH HOH B . T 6 HOH 429 899 899 HOH HOH B . T 6 HOH 430 902 902 HOH HOH B . T 6 HOH 431 903 903 HOH HOH B . T 6 HOH 432 905 905 HOH HOH B . #