data_3G70 # _entry.id 3G70 # _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 3G70 RCSB RCSB051502 WWPDB D_1000051502 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3G6Z 'Same inhibitor class' unspecified PDB 3g72 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3G70 _pdbx_database_status.recvd_initial_deposition_date 2009-02-09 _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.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Bezencon, O.' 1 'Bur, D.' 2 'Prade, L.' 3 'Weller, T.' 4 'Boss, C.' 5 'Fischli, W.' 6 # _citation.id primary _citation.title 'Design and Preparation of Potent, Nonpeptidic, Bioavailable Renin Inhibitors' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 52 _citation.page_first 3689 _citation.page_last 3702 _citation.year 2009 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19358611 _citation.pdbx_database_id_DOI 10.1021/jm900022f # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Bezencon, O.' 1 primary 'Bur, D.' 2 primary 'Weller, T.' 3 primary 'Richard-Bildstein, S.' 4 primary 'Remen, L.' 5 primary 'Sifferlen, T.' 6 primary 'Corminboeuf, O.' 7 primary 'Grisostomi, C.' 8 primary 'Boss, C.' 9 primary 'Prade, L.' 10 primary 'Delahaye, S.' 11 primary 'Treiber, A.' 12 primary 'Strickner, P.' 13 primary 'Binkert, C.' 14 primary 'Hess, P.' 15 primary 'Steiner, B.' 16 primary 'Fischli, W.' 17 # _cell.entry_id 3G70 _cell.length_a 65.730 _cell.length_b 89.460 _cell.length_c 118.370 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _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 3G70 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _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 Renin 37405.152 2 3.4.23.15 ? ? ? 2 non-polymer syn ;(1R,5S)-7-{4-[3-(2-chloro-3,6-difluorophenoxy)propyl]phenyl}-N-cyclopropyl-N-(2,3-dichlorobenzyl)-3,9-diazabicyclo[3.3.1]non-6-ene-6-carboxamide ; 646.982 2 ? ? ? ? 3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133 2 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 5 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 1 ? ? ? ? 6 water nat water 18.015 374 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name Angiotensinogenase # _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 ;LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELT LRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSF YYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIE KLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFI RKFYTEFDRRNNRIGFALARH ; _entity_poly.pdbx_seq_one_letter_code_can ;LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELT LRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSF YYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIE KLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFI RKFYTEFDRRNNRIGFALARH ; _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 LEU n 1 2 THR n 1 3 LEU n 1 4 GLY n 1 5 ASN n 1 6 THR n 1 7 THR n 1 8 SER n 1 9 SER n 1 10 VAL n 1 11 ILE n 1 12 LEU n 1 13 THR n 1 14 ASN n 1 15 TYR n 1 16 MET n 1 17 ASP n 1 18 THR n 1 19 GLN n 1 20 TYR n 1 21 TYR n 1 22 GLY n 1 23 GLU n 1 24 ILE n 1 25 GLY n 1 26 ILE n 1 27 GLY n 1 28 THR n 1 29 PRO n 1 30 PRO n 1 31 GLN n 1 32 THR n 1 33 PHE n 1 34 LYS n 1 35 VAL n 1 36 VAL n 1 37 PHE n 1 38 ASP n 1 39 THR n 1 40 GLY n 1 41 SER n 1 42 SER n 1 43 ASN n 1 44 VAL n 1 45 TRP n 1 46 VAL n 1 47 PRO n 1 48 SER n 1 49 SER n 1 50 LYS n 1 51 CYS n 1 52 SER n 1 53 ARG n 1 54 LEU n 1 55 TYR n 1 56 THR n 1 57 ALA n 1 58 CYS n 1 59 VAL n 1 60 TYR n 1 61 HIS n 1 62 LYS n 1 63 LEU n 1 64 PHE n 1 65 ASP n 1 66 ALA n 1 67 SER n 1 68 ASP n 1 69 SER n 1 70 SER n 1 71 SER n 1 72 TYR n 1 73 LYS n 1 74 HIS n 1 75 ASN n 1 76 GLY n 1 77 THR n 1 78 GLU n 1 79 LEU n 1 80 THR n 1 81 LEU n 1 82 ARG n 1 83 TYR n 1 84 SER n 1 85 THR n 1 86 GLY n 1 87 THR n 1 88 VAL n 1 89 SER n 1 90 GLY n 1 91 PHE n 1 92 LEU n 1 93 SER n 1 94 GLN n 1 95 ASP n 1 96 ILE n 1 97 ILE n 1 98 THR n 1 99 VAL n 1 100 GLY n 1 101 GLY n 1 102 ILE n 1 103 THR n 1 104 VAL n 1 105 THR n 1 106 GLN n 1 107 MET n 1 108 PHE n 1 109 GLY n 1 110 GLU n 1 111 VAL n 1 112 THR n 1 113 GLU n 1 114 MET n 1 115 PRO n 1 116 ALA n 1 117 LEU n 1 118 PRO n 1 119 PHE n 1 120 MET n 1 121 LEU n 1 122 ALA n 1 123 GLU n 1 124 PHE n 1 125 ASP n 1 126 GLY n 1 127 VAL n 1 128 VAL n 1 129 GLY n 1 130 MET n 1 131 GLY n 1 132 PHE n 1 133 ILE n 1 134 GLU n 1 135 GLN n 1 136 ALA n 1 137 ILE n 1 138 GLY n 1 139 ARG n 1 140 VAL n 1 141 THR n 1 142 PRO n 1 143 ILE n 1 144 PHE n 1 145 ASP n 1 146 ASN n 1 147 ILE n 1 148 ILE n 1 149 SER n 1 150 GLN n 1 151 GLY n 1 152 VAL n 1 153 LEU n 1 154 LYS n 1 155 GLU n 1 156 ASP n 1 157 VAL n 1 158 PHE n 1 159 SER n 1 160 PHE n 1 161 TYR n 1 162 TYR n 1 163 ASN n 1 164 ARG n 1 165 ASP n 1 166 SER n 1 167 GLU n 1 168 ASN n 1 169 SER n 1 170 GLN n 1 171 SER n 1 172 LEU n 1 173 GLY n 1 174 GLY n 1 175 GLN n 1 176 ILE n 1 177 VAL n 1 178 LEU n 1 179 GLY n 1 180 GLY n 1 181 SER n 1 182 ASP n 1 183 PRO n 1 184 GLN n 1 185 HIS n 1 186 TYR n 1 187 GLU n 1 188 GLY n 1 189 ASN n 1 190 PHE n 1 191 HIS n 1 192 TYR n 1 193 ILE n 1 194 ASN n 1 195 LEU n 1 196 ILE n 1 197 LYS n 1 198 THR n 1 199 GLY n 1 200 VAL n 1 201 TRP n 1 202 GLN n 1 203 ILE n 1 204 GLN n 1 205 MET n 1 206 LYS n 1 207 GLY n 1 208 VAL n 1 209 SER n 1 210 VAL n 1 211 GLY n 1 212 SER n 1 213 SER n 1 214 THR n 1 215 LEU n 1 216 LEU n 1 217 CYS n 1 218 GLU n 1 219 ASP n 1 220 GLY n 1 221 CYS n 1 222 LEU n 1 223 ALA n 1 224 LEU n 1 225 VAL n 1 226 ASP n 1 227 THR n 1 228 GLY n 1 229 ALA n 1 230 SER n 1 231 TYR n 1 232 ILE n 1 233 SER n 1 234 GLY n 1 235 SER n 1 236 THR n 1 237 SER n 1 238 SER n 1 239 ILE n 1 240 GLU n 1 241 LYS n 1 242 LEU n 1 243 MET n 1 244 GLU n 1 245 ALA n 1 246 LEU n 1 247 GLY n 1 248 ALA n 1 249 LYS n 1 250 LYS n 1 251 ARG n 1 252 LEU n 1 253 PHE n 1 254 ASP n 1 255 TYR n 1 256 VAL n 1 257 VAL n 1 258 LYS n 1 259 CYS n 1 260 ASN n 1 261 GLU n 1 262 GLY n 1 263 PRO n 1 264 THR n 1 265 LEU n 1 266 PRO n 1 267 ASP n 1 268 ILE n 1 269 SER n 1 270 PHE n 1 271 HIS n 1 272 LEU n 1 273 GLY n 1 274 GLY n 1 275 LYS n 1 276 GLU n 1 277 TYR n 1 278 THR n 1 279 LEU n 1 280 THR n 1 281 SER n 1 282 ALA n 1 283 ASP n 1 284 TYR n 1 285 VAL n 1 286 PHE n 1 287 GLN n 1 288 GLU n 1 289 SER n 1 290 TYR n 1 291 SER n 1 292 SER n 1 293 LYS n 1 294 LYS n 1 295 LEU n 1 296 CYS n 1 297 THR n 1 298 LEU n 1 299 ALA n 1 300 ILE n 1 301 HIS n 1 302 ALA n 1 303 MET n 1 304 ASP n 1 305 ILE n 1 306 PRO n 1 307 PRO n 1 308 PRO n 1 309 THR n 1 310 GLY n 1 311 PRO n 1 312 THR n 1 313 TRP n 1 314 ALA n 1 315 LEU n 1 316 GLY n 1 317 ALA n 1 318 THR n 1 319 PHE n 1 320 ILE n 1 321 ARG n 1 322 LYS n 1 323 PHE n 1 324 TYR n 1 325 THR n 1 326 GLU n 1 327 PHE n 1 328 ASP n 1 329 ARG n 1 330 ARG n 1 331 ASN n 1 332 ASN n 1 333 ARG n 1 334 ILE n 1 335 GLY n 1 336 PHE n 1 337 ALA n 1 338 LEU n 1 339 ALA n 1 340 ARG n 1 341 HIS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name human _entity_src_gen.pdbx_host_org_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _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 'human embryonic kidney cell' _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code RENI_HUMAN _struct_ref.pdbx_db_accession P00797 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELT LRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSF YYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIE KLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFI RKFYTEFDRRNNRIGFALAR ; _struct_ref.pdbx_align_begin 67 _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 3G70 A 1 ? 340 ? P00797 67 ? 406 ? 1 340 2 1 3G70 B 1 ? 340 ? P00797 67 ? 406 ? 1 340 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3G70 HIS A 341 ? UNP P00797 ? ? 'EXPRESSION TAG' 341 1 2 3G70 HIS B 341 ? UNP P00797 ? ? 'EXPRESSION TAG' 341 2 # 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 A5T non-polymer . ;(1R,5S)-7-{4-[3-(2-chloro-3,6-difluorophenoxy)propyl]phenyl}-N-cyclopropyl-N-(2,3-dichlorobenzyl)-3,9-diazabicyclo[3.3.1]non-6-ene-6-carboxamide ; ? 'C33 H32 Cl3 F2 N3 O2' 646.982 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 DMS non-polymer . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S' 78.133 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? '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 3G70 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.33 _exptl_crystal.density_percent_sol 47.12 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.5 _exptl_crystal_grow.pdbx_details '25-30% PEG 4000, 0.6M NaCl, 0.1M Citrate(pH 4-5), VAPOR DIFFUSION, SITTING DROP, temperature 293K' _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 'IMAGE PLATE' _diffrn_detector.type 'MAR scanner 345 mm plate' _diffrn_detector.pdbx_collection_date 2004-11-15 _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 ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X06SA' _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X06SA _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0 # _reflns.entry_id 3G70 _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 70 _reflns.d_resolution_high 2.0 _reflns.number_obs 40473 _reflns.number_all ? _reflns.percent_possible_obs 85 _reflns.pdbx_Rmerge_I_obs 0.075 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.6 _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 3G70 _refine.ls_number_reflns_obs 38393 _refine.ls_number_reflns_all 40473 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 36.98 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 84.41 _refine.ls_R_factor_obs 0.19947 _refine.ls_R_factor_all 0.22 _refine.ls_R_factor_R_work 0.19606 _refine.ls_R_factor_R_free 0.26291 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 2042 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.952 _refine.correlation_coeff_Fo_to_Fc_free 0.913 _refine.B_iso_mean 36.102 _refine.aniso_B[1][1] 0.26 _refine.aniso_B[2][2] 1.44 _refine.aniso_B[3][3] -1.70 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.256 _refine.pdbx_overall_ESU_R_Free 0.218 _refine.overall_SU_ML 0.147 _refine.overall_SU_B 5.257 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _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_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 5175 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 122 _refine_hist.number_atoms_solvent 374 _refine_hist.number_atoms_total 5671 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 36.98 # 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 r_bond_refined_d 0.013 0.022 ? 5473 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.488 1.967 ? 7441 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.911 5.000 ? 675 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.464 23.964 ? 222 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.968 15.000 ? 862 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.542 15.000 ? 20 'X-RAY DIFFRACTION' ? r_chiral_restr 0.096 0.200 ? 828 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 4124 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.209 0.200 ? 2299 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.308 0.200 ? 3697 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.165 0.200 ? 333 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.216 0.200 ? 89 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.284 0.200 ? 35 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 1.923 3.000 ? 3426 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 2.809 5.000 ? 5411 'X-RAY DIFFRACTION' ? r_scbond_it 2.209 3.000 ? 2364 'X-RAY DIFFRACTION' ? r_scangle_it 3.273 6.000 ? 2024 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.000 _refine_ls_shell.d_res_low 2.052 _refine_ls_shell.number_reflns_R_work 2164 _refine_ls_shell.R_factor_R_work 0.245 _refine_ls_shell.percent_reflns_obs 65.37 _refine_ls_shell.R_factor_R_free 0.357 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 122 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3G70 _struct.title 'Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors' _struct.pdbx_descriptor 'Renin (E.C.3.4.23.15)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3G70 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;human renin, Aspartyl protease, Cleavage on pair of basic residues, Disease mutation, Glycoprotein, Hydrolase, Membrane, Protease, Secreted, Zymogen ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 2 ? G N N 3 ? H N N 5 ? I N N 6 ? J 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 TYR A 55 ? TYR A 60 ? TYR A 55 TYR A 60 1 ? 6 HELX_P HELX_P2 2 ASP A 65 ? SER A 69 ? ASP A 65 SER A 69 5 ? 5 HELX_P HELX_P3 3 PRO A 118 ? ALA A 122 ? PRO A 118 ALA A 122 5 ? 5 HELX_P HELX_P4 4 PHE A 132 ? VAL A 140 ? PHE A 132 VAL A 140 5 ? 9 HELX_P HELX_P5 5 PRO A 142 ? SER A 149 ? PRO A 142 SER A 149 1 ? 8 HELX_P HELX_P6 6 ASP A 182 ? GLN A 184 ? ASP A 182 GLN A 184 5 ? 3 HELX_P HELX_P7 7 SER A 235 ? GLY A 247 ? SER A 235 GLY A 247 1 ? 13 HELX_P HELX_P8 8 ASN A 260 ? LEU A 265 ? ASN A 260 LEU A 265 5 ? 6 HELX_P HELX_P9 9 THR A 280 ? VAL A 285 ? THR A 280 VAL A 285 1 ? 6 HELX_P HELX_P10 10 GLY A 316 ? LYS A 322 ? GLY A 316 LYS A 322 1 ? 7 HELX_P HELX_P11 11 TYR B 55 ? TYR B 60 ? TYR B 55 TYR B 60 1 ? 6 HELX_P HELX_P12 12 ASP B 65 ? SER B 69 ? ASP B 65 SER B 69 5 ? 5 HELX_P HELX_P13 13 PRO B 118 ? ALA B 122 ? PRO B 118 ALA B 122 5 ? 5 HELX_P HELX_P14 14 PHE B 132 ? VAL B 140 ? PHE B 132 VAL B 140 5 ? 9 HELX_P HELX_P15 15 PRO B 142 ? GLN B 150 ? PRO B 142 GLN B 150 1 ? 9 HELX_P HELX_P16 16 SER B 235 ? GLY B 247 ? SER B 235 GLY B 247 1 ? 13 HELX_P HELX_P17 17 ASN B 260 ? LEU B 265 ? ASN B 260 LEU B 265 5 ? 6 HELX_P HELX_P18 18 THR B 280 ? VAL B 285 ? THR B 280 VAL B 285 1 ? 6 HELX_P HELX_P19 19 GLY B 316 ? LYS B 322 ? GLY B 316 LYS B 322 1 ? 7 # _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 51 SG ? ? ? 1_555 A CYS 58 SG ? ? A CYS 51 A CYS 58 1_555 ? ? ? ? ? ? ? 2.008 ? disulf2 disulf ? ? A CYS 217 SG ? ? ? 1_555 A CYS 221 SG ? ? A CYS 217 A CYS 221 1_555 ? ? ? ? ? ? ? 2.036 ? disulf3 disulf ? ? A CYS 259 SG ? ? ? 1_555 A CYS 296 SG ? ? A CYS 259 A CYS 296 1_555 ? ? ? ? ? ? ? 2.049 ? disulf4 disulf ? ? B CYS 51 SG ? ? ? 1_555 B CYS 58 SG ? ? B CYS 51 B CYS 58 1_555 ? ? ? ? ? ? ? 2.031 ? disulf5 disulf ? ? B CYS 217 SG ? ? ? 1_555 B CYS 221 SG ? ? B CYS 217 B CYS 221 1_555 ? ? ? ? ? ? ? 2.039 ? disulf6 disulf ? ? B CYS 259 SG ? ? ? 1_555 B CYS 296 SG ? ? B CYS 259 B CYS 296 1_555 ? ? ? ? ? ? ? 2.567 ? covale1 covale ? ? A ASN 75 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 75 A NAG 344 1_555 ? ? ? ? ? ? ? 1.455 ? covale2 covale ? ? B ASN 75 ND2 ? ? ? 1_555 H NDG . C1 ? ? B ASN 75 B NDG 344 1_555 ? ? ? ? ? ? ? 1.644 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # 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 THR 28 A . ? THR 28 A PRO 29 A ? PRO 29 A 1 -2.83 2 LEU 117 A . ? LEU 117 A PRO 118 A ? PRO 118 A 1 0.62 3 PRO 307 A . ? PRO 307 A PRO 308 A ? PRO 308 A 1 3.55 4 GLY 310 A . ? GLY 310 A PRO 311 A ? PRO 311 A 1 -5.60 5 THR 28 B . ? THR 28 B PRO 29 B ? PRO 29 B 1 -3.01 6 LEU 117 B . ? LEU 117 B PRO 118 B ? PRO 118 B 1 3.60 7 PRO 307 B . ? PRO 307 B PRO 308 B ? PRO 308 B 1 0.30 8 GLY 310 B . ? GLY 310 B PRO 311 B ? PRO 311 B 1 -1.28 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 9 ? B ? 13 ? C ? 4 ? D ? 6 ? E ? 3 ? F ? 9 ? G ? 13 ? H ? 5 ? I ? 4 ? J ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel A 8 9 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? parallel B 4 5 ? anti-parallel B 5 6 ? parallel B 6 7 ? anti-parallel B 7 8 ? anti-parallel B 8 9 ? anti-parallel B 9 10 ? anti-parallel B 10 11 ? anti-parallel B 11 12 ? anti-parallel B 12 13 ? 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 ? parallel D 4 5 ? anti-parallel D 5 6 ? parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel F 4 5 ? anti-parallel F 5 6 ? anti-parallel F 6 7 ? anti-parallel F 7 8 ? anti-parallel F 8 9 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? parallel G 4 5 ? anti-parallel G 5 6 ? parallel G 6 7 ? anti-parallel G 7 8 ? anti-parallel G 8 9 ? anti-parallel G 9 10 ? anti-parallel G 10 11 ? anti-parallel G 11 12 ? anti-parallel G 12 13 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? parallel H 3 4 ? anti-parallel H 4 5 ? 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 # 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 LYS A 73 ? TYR A 83 ? LYS A 73 TYR A 83 A 2 GLY A 86 ? VAL A 99 ? GLY A 86 VAL A 99 A 3 GLN A 19 ? ILE A 26 ? GLN A 19 ILE A 26 A 4 SER A 8 ? TYR A 15 ? SER A 8 TYR A 15 A 5 GLY A 174 ? LEU A 178 ? GLY A 174 LEU A 178 A 6 VAL A 157 ? TYR A 162 ? VAL A 157 TYR A 162 A 7 PHE A 323 ? ASP A 328 ? PHE A 323 ASP A 328 A 8 ARG A 333 ? ALA A 339 ? ARG A 333 ALA A 339 A 9 TYR A 186 ? ASN A 194 ? TYR A 186 ASN A 194 B 1 LYS A 73 ? TYR A 83 ? LYS A 73 TYR A 83 B 2 GLY A 86 ? VAL A 99 ? GLY A 86 VAL A 99 B 3 ILE A 102 ? GLU A 113 ? ILE A 102 GLU A 113 B 4 VAL A 44 ? PRO A 47 ? VAL A 44 PRO A 47 B 5 GLY A 126 ? GLY A 129 ? GLY A 126 GLY A 129 B 6 GLN A 31 ? ASP A 38 ? GLN A 31 ASP A 38 B 7 GLN A 19 ? ILE A 26 ? GLN A 19 ILE A 26 B 8 SER A 8 ? TYR A 15 ? SER A 8 TYR A 15 B 9 GLY A 174 ? LEU A 178 ? GLY A 174 LEU A 178 B 10 VAL A 157 ? TYR A 162 ? VAL A 157 TYR A 162 B 11 PHE A 323 ? ASP A 328 ? PHE A 323 ASP A 328 B 12 ARG A 333 ? ALA A 339 ? ARG A 333 ALA A 339 B 13 TYR A 186 ? ASN A 194 ? TYR A 186 ASN A 194 C 1 SER A 213 ? LEU A 216 ? SER A 213 LEU A 216 C 2 GLN A 202 ? VAL A 210 ? GLN A 202 VAL A 210 C 3 ILE A 268 ? LEU A 272 ? ILE A 268 LEU A 272 C 4 LYS A 275 ? LEU A 279 ? LYS A 275 LEU A 279 D 1 SER A 213 ? LEU A 216 ? SER A 213 LEU A 216 D 2 GLN A 202 ? VAL A 210 ? GLN A 202 VAL A 210 D 3 CYS A 221 ? VAL A 225 ? CYS A 221 VAL A 225 D 4 TRP A 313 ? LEU A 315 ? TRP A 313 LEU A 315 D 5 ILE A 232 ? GLY A 234 ? ILE A 232 GLY A 234 D 6 ILE A 300 ? ALA A 302 ? ILE A 300 ALA A 302 E 1 LYS A 249 ? LYS A 250 ? LYS A 249 LYS A 250 E 2 TYR A 255 ? LYS A 258 ? TYR A 255 LYS A 258 E 3 LEU A 295 ? THR A 297 ? LEU A 295 THR A 297 F 1 LYS B 73 ? TYR B 83 ? LYS B 73 TYR B 83 F 2 GLY B 86 ? VAL B 99 ? GLY B 86 VAL B 99 F 3 GLN B 19 ? ILE B 26 ? GLN B 19 ILE B 26 F 4 SER B 8 ? TYR B 15 ? SER B 8 TYR B 15 F 5 GLY B 174 ? LEU B 178 ? GLY B 174 LEU B 178 F 6 VAL B 157 ? TYR B 162 ? VAL B 157 TYR B 162 F 7 PHE B 323 ? ASP B 328 ? PHE B 323 ASP B 328 F 8 ARG B 333 ? ALA B 339 ? ARG B 333 ALA B 339 F 9 TYR B 186 ? ASN B 194 ? TYR B 186 ASN B 194 G 1 LYS B 73 ? TYR B 83 ? LYS B 73 TYR B 83 G 2 GLY B 86 ? VAL B 99 ? GLY B 86 VAL B 99 G 3 ILE B 102 ? GLU B 113 ? ILE B 102 GLU B 113 G 4 VAL B 44 ? PRO B 47 ? VAL B 44 PRO B 47 G 5 GLY B 126 ? GLY B 129 ? GLY B 126 GLY B 129 G 6 GLN B 31 ? ASP B 38 ? GLN B 31 ASP B 38 G 7 GLN B 19 ? ILE B 26 ? GLN B 19 ILE B 26 G 8 SER B 8 ? TYR B 15 ? SER B 8 TYR B 15 G 9 GLY B 174 ? LEU B 178 ? GLY B 174 LEU B 178 G 10 VAL B 157 ? TYR B 162 ? VAL B 157 TYR B 162 G 11 PHE B 323 ? ASP B 328 ? PHE B 323 ASP B 328 G 12 ARG B 333 ? ALA B 339 ? ARG B 333 ALA B 339 G 13 TYR B 186 ? ASN B 194 ? TYR B 186 ASN B 194 H 1 GLN B 202 ? MET B 205 ? GLN B 202 MET B 205 H 2 CYS B 221 ? VAL B 225 ? CYS B 221 VAL B 225 H 3 TRP B 313 ? LEU B 315 ? TRP B 313 LEU B 315 H 4 ILE B 232 ? GLY B 234 ? ILE B 232 GLY B 234 H 5 ILE B 300 ? ALA B 302 ? ILE B 300 ALA B 302 I 1 SER B 213 ? LEU B 216 ? SER B 213 LEU B 216 I 2 VAL B 208 ? VAL B 210 ? VAL B 208 VAL B 210 I 3 ILE B 268 ? LEU B 272 ? ILE B 268 LEU B 272 I 4 LYS B 275 ? LEU B 279 ? LYS B 275 LEU B 279 J 1 LYS B 249 ? LYS B 250 ? LYS B 249 LYS B 250 J 2 TYR B 255 ? LYS B 258 ? TYR B 255 LYS B 258 J 3 LEU B 295 ? THR B 297 ? LEU B 295 THR B 297 # 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 LEU A 81 ? N LEU A 81 O VAL A 88 ? O VAL A 88 A 2 3 O THR A 98 ? O THR A 98 N GLY A 25 ? N GLY A 25 A 3 4 O GLN A 19 ? O GLN A 19 N TYR A 15 ? N TYR A 15 A 4 5 N SER A 8 ? N SER A 8 O LEU A 178 ? O LEU A 178 A 5 6 O GLN A 175 ? O GLN A 175 N TYR A 161 ? N TYR A 161 A 6 7 N PHE A 158 ? N PHE A 158 O PHE A 327 ? O PHE A 327 A 7 8 N GLU A 326 ? N GLU A 326 O GLY A 335 ? O GLY A 335 A 8 9 O PHE A 336 ? O PHE A 336 N HIS A 191 ? N HIS A 191 B 1 2 N LEU A 81 ? N LEU A 81 O VAL A 88 ? O VAL A 88 B 2 3 N ILE A 97 ? N ILE A 97 O VAL A 104 ? O VAL A 104 B 3 4 O GLY A 109 ? O GLY A 109 N VAL A 44 ? N VAL A 44 B 4 5 N TRP A 45 ? N TRP A 45 O VAL A 127 ? O VAL A 127 B 5 6 O VAL A 128 ? O VAL A 128 N VAL A 36 ? N VAL A 36 B 6 7 O VAL A 35 ? O VAL A 35 N GLY A 22 ? N GLY A 22 B 7 8 O GLN A 19 ? O GLN A 19 N TYR A 15 ? N TYR A 15 B 8 9 N SER A 8 ? N SER A 8 O LEU A 178 ? O LEU A 178 B 9 10 O GLN A 175 ? O GLN A 175 N TYR A 161 ? N TYR A 161 B 10 11 N PHE A 158 ? N PHE A 158 O PHE A 327 ? O PHE A 327 B 11 12 N GLU A 326 ? N GLU A 326 O GLY A 335 ? O GLY A 335 B 12 13 O PHE A 336 ? O PHE A 336 N HIS A 191 ? N HIS A 191 C 1 2 O LEU A 216 ? O LEU A 216 N VAL A 208 ? N VAL A 208 C 2 3 N GLY A 207 ? N GLY A 207 O HIS A 271 ? O HIS A 271 C 3 4 N PHE A 270 ? N PHE A 270 O TYR A 277 ? O TYR A 277 D 1 2 O LEU A 216 ? O LEU A 216 N VAL A 208 ? N VAL A 208 D 2 3 N ILE A 203 ? N ILE A 203 O ALA A 223 ? O ALA A 223 D 3 4 N LEU A 224 ? N LEU A 224 O LEU A 315 ? O LEU A 315 D 4 5 O ALA A 314 ? O ALA A 314 N SER A 233 ? N SER A 233 D 5 6 N ILE A 232 ? N ILE A 232 O HIS A 301 ? O HIS A 301 E 1 2 N LYS A 249 ? N LYS A 249 O VAL A 256 ? O VAL A 256 E 2 3 N VAL A 257 ? N VAL A 257 O CYS A 296 ? O CYS A 296 F 1 2 N GLY B 76 ? N GLY B 76 O LEU B 92 ? O LEU B 92 F 2 3 O THR B 98 ? O THR B 98 N GLY B 25 ? N GLY B 25 F 3 4 O TYR B 21 ? O TYR B 21 N THR B 13 ? N THR B 13 F 4 5 N SER B 8 ? N SER B 8 O LEU B 178 ? O LEU B 178 F 5 6 O GLN B 175 ? O GLN B 175 N TYR B 161 ? N TYR B 161 F 6 7 N PHE B 158 ? N PHE B 158 O PHE B 327 ? O PHE B 327 F 7 8 N GLU B 326 ? N GLU B 326 O GLY B 335 ? O GLY B 335 F 8 9 O LEU B 338 ? O LEU B 338 N GLU B 187 ? N GLU B 187 G 1 2 N GLY B 76 ? N GLY B 76 O LEU B 92 ? O LEU B 92 G 2 3 N PHE B 91 ? N PHE B 91 O GLU B 110 ? O GLU B 110 G 3 4 O GLY B 109 ? O GLY B 109 N VAL B 44 ? N VAL B 44 G 4 5 N TRP B 45 ? N TRP B 45 O VAL B 127 ? O VAL B 127 G 5 6 O VAL B 128 ? O VAL B 128 N VAL B 36 ? N VAL B 36 G 6 7 O VAL B 35 ? O VAL B 35 N GLY B 22 ? N GLY B 22 G 7 8 O TYR B 21 ? O TYR B 21 N THR B 13 ? N THR B 13 G 8 9 N SER B 8 ? N SER B 8 O LEU B 178 ? O LEU B 178 G 9 10 O GLN B 175 ? O GLN B 175 N TYR B 161 ? N TYR B 161 G 10 11 N PHE B 158 ? N PHE B 158 O PHE B 327 ? O PHE B 327 G 11 12 N GLU B 326 ? N GLU B 326 O GLY B 335 ? O GLY B 335 G 12 13 O LEU B 338 ? O LEU B 338 N GLU B 187 ? N GLU B 187 H 1 2 N MET B 205 ? N MET B 205 O CYS B 221 ? O CYS B 221 H 2 3 N LEU B 224 ? N LEU B 224 O LEU B 315 ? O LEU B 315 H 3 4 O ALA B 314 ? O ALA B 314 N SER B 233 ? N SER B 233 H 4 5 N ILE B 232 ? N ILE B 232 O HIS B 301 ? O HIS B 301 I 1 2 O LEU B 216 ? O LEU B 216 N VAL B 208 ? N VAL B 208 I 2 3 N SER B 209 ? N SER B 209 O SER B 269 ? O SER B 269 I 3 4 N ILE B 268 ? N ILE B 268 O LEU B 279 ? O LEU B 279 J 1 2 N LYS B 249 ? N LYS B 249 O VAL B 256 ? O VAL B 256 J 2 3 N VAL B 257 ? N VAL B 257 O CYS B 296 ? O CYS B 296 # 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 ? ? ? ? 17 'BINDING SITE FOR RESIDUE A5T A 342' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE DMS A 343' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 344' AC4 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE A5T B 342' AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE DMS B 343' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NDG B 344' # 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 17 GLN A 19 ? GLN A 19 . ? 1_555 ? 2 AC1 17 ASP A 38 ? ASP A 38 . ? 1_555 ? 3 AC1 17 GLY A 40 ? GLY A 40 . ? 1_555 ? 4 AC1 17 PRO A 47 ? PRO A 47 . ? 1_555 ? 5 AC1 17 HIS A 61 ? HIS A 61 . ? 1_555 ? 6 AC1 17 LEU A 81 ? LEU A 81 . ? 1_555 ? 7 AC1 17 TYR A 83 ? TYR A 83 . ? 1_555 ? 8 AC1 17 VAL A 111 ? VAL A 111 . ? 1_555 ? 9 AC1 17 MET A 114 ? MET A 114 . ? 1_555 ? 10 AC1 17 PHE A 119 ? PHE A 119 . ? 1_555 ? 11 AC1 17 ALA A 122 ? ALA A 122 . ? 1_555 ? 12 AC1 17 PHE A 124 ? PHE A 124 . ? 1_555 ? 13 AC1 17 ASP A 125 ? ASP A 125 . ? 1_555 ? 14 AC1 17 VAL A 127 ? VAL A 127 . ? 1_555 ? 15 AC1 17 ASP A 226 ? ASP A 226 . ? 1_555 ? 16 AC1 17 GLY A 228 ? GLY A 228 . ? 1_555 ? 17 AC1 17 SER A 230 ? SER A 230 . ? 1_555 ? 18 AC2 9 THR A 18 ? THR A 18 . ? 1_555 ? 19 AC2 9 GLN A 19 ? GLN A 19 . ? 1_555 ? 20 AC2 9 TYR A 20 ? TYR A 20 . ? 1_555 ? 21 AC2 9 VAL A 36 ? VAL A 36 . ? 1_555 ? 22 AC2 9 PHE A 124 ? PHE A 124 . ? 1_555 ? 23 AC2 9 THR A 227 ? THR A 227 . ? 1_555 ? 24 AC2 9 GLY A 228 ? GLY A 228 . ? 1_555 ? 25 AC2 9 ALA A 229 ? ALA A 229 . ? 1_555 ? 26 AC2 9 SER A 230 ? SER A 230 . ? 1_555 ? 27 AC3 3 ASN A 75 ? ASN A 75 . ? 1_555 ? 28 AC3 3 THR A 77 ? THR A 77 . ? 1_555 ? 29 AC3 3 MET A 107 ? MET A 107 . ? 1_555 ? 30 AC4 16 ASP B 38 ? ASP B 38 . ? 1_555 ? 31 AC4 16 GLY B 40 ? GLY B 40 . ? 1_555 ? 32 AC4 16 HIS B 61 ? HIS B 61 . ? 1_555 ? 33 AC4 16 TYR B 83 ? TYR B 83 . ? 1_555 ? 34 AC4 16 VAL B 111 ? VAL B 111 . ? 1_555 ? 35 AC4 16 MET B 114 ? MET B 114 . ? 1_555 ? 36 AC4 16 PHE B 119 ? PHE B 119 . ? 1_555 ? 37 AC4 16 ALA B 122 ? ALA B 122 . ? 1_555 ? 38 AC4 16 PHE B 124 ? PHE B 124 . ? 1_555 ? 39 AC4 16 ASP B 125 ? ASP B 125 . ? 1_555 ? 40 AC4 16 VAL B 127 ? VAL B 127 . ? 1_555 ? 41 AC4 16 ASP B 226 ? ASP B 226 . ? 1_555 ? 42 AC4 16 GLY B 228 ? GLY B 228 . ? 1_555 ? 43 AC4 16 DMS G . ? DMS B 343 . ? 1_555 ? 44 AC4 16 HOH J . ? HOH B 392 . ? 1_555 ? 45 AC4 16 HOH J . ? HOH B 515 . ? 1_555 ? 46 AC5 8 THR B 18 ? THR B 18 . ? 1_555 ? 47 AC5 8 GLN B 19 ? GLN B 19 . ? 1_555 ? 48 AC5 8 TYR B 20 ? TYR B 20 . ? 1_555 ? 49 AC5 8 VAL B 36 ? VAL B 36 . ? 1_555 ? 50 AC5 8 THR B 227 ? THR B 227 . ? 1_555 ? 51 AC5 8 GLY B 228 ? GLY B 228 . ? 1_555 ? 52 AC5 8 ALA B 229 ? ALA B 229 . ? 1_555 ? 53 AC5 8 A5T F . ? A5T B 342 . ? 1_555 ? 54 AC6 5 ASN B 75 ? ASN B 75 . ? 1_555 ? 55 AC6 5 THR B 77 ? THR B 77 . ? 1_555 ? 56 AC6 5 MET B 107 ? MET B 107 . ? 1_555 ? 57 AC6 5 HOH J . ? HOH B 459 . ? 1_555 ? 58 AC6 5 HOH J . ? HOH B 528 . ? 1_555 ? # _database_PDB_matrix.entry_id 3G70 _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 3G70 _atom_sites.fract_transf_matrix[1][1] 0.015214 _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] 0.011178 _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] 0.008448 _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 CL F 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 . GLY A 1 4 ? 21.344 32.894 4.448 1.00 59.78 ? 4 GLY A N 1 ATOM 2 C CA . GLY A 1 4 ? 20.179 33.818 4.406 1.00 59.42 ? 4 GLY A CA 1 ATOM 3 C C . GLY A 1 4 ? 19.485 33.935 5.749 1.00 60.66 ? 4 GLY A C 1 ATOM 4 O O . GLY A 1 4 ? 19.900 33.313 6.735 1.00 60.04 ? 4 GLY A O 1 ATOM 5 N N . ASN A 1 5 ? 18.435 34.754 5.787 1.00 61.64 ? 5 ASN A N 1 ATOM 6 C CA . ASN A 1 5 ? 17.628 34.921 6.992 1.00 62.14 ? 5 ASN A CA 1 ATOM 7 C C . ASN A 1 5 ? 16.149 34.679 6.677 1.00 62.06 ? 5 ASN A C 1 ATOM 8 O O . ASN A 1 5 ? 15.297 35.571 6.837 1.00 62.98 ? 5 ASN A O 1 ATOM 9 C CB . ASN A 1 5 ? 17.859 36.305 7.632 1.00 62.14 ? 5 ASN A CB 1 ATOM 10 C CG . ASN A 1 5 ? 17.821 36.264 9.159 1.00 60.98 ? 5 ASN A CG 1 ATOM 11 O OD1 . ASN A 1 5 ? 18.549 35.497 9.786 1.00 60.50 ? 5 ASN A OD1 1 ATOM 12 N ND2 . ASN A 1 5 ? 16.983 37.100 9.758 1.00 60.96 ? 5 ASN A ND2 1 ATOM 13 N N . THR A 1 6 ? 15.863 33.471 6.198 1.00 60.16 ? 6 THR A N 1 ATOM 14 C CA . THR A 1 6 ? 14.490 33.052 5.960 1.00 59.68 ? 6 THR A CA 1 ATOM 15 C C . THR A 1 6 ? 14.140 31.709 6.594 1.00 57.80 ? 6 THR A C 1 ATOM 16 O O . THR A 1 6 ? 14.957 30.784 6.672 1.00 55.38 ? 6 THR A O 1 ATOM 17 C CB . THR A 1 6 ? 14.132 33.037 4.448 1.00 61.50 ? 6 THR A CB 1 ATOM 18 O OG1 . THR A 1 6 ? 15.234 32.531 3.687 1.00 62.91 ? 6 THR A OG1 1 ATOM 19 C CG2 . THR A 1 6 ? 13.930 34.463 3.908 1.00 61.74 ? 6 THR A CG2 1 ATOM 20 N N . THR A 1 7 ? 12.909 31.643 7.078 1.00 56.82 ? 7 THR A N 1 ATOM 21 C CA . THR A 1 7 ? 12.274 30.386 7.403 1.00 55.78 ? 7 THR A CA 1 ATOM 22 C C . THR A 1 7 ? 10.965 30.304 6.649 1.00 54.20 ? 7 THR A C 1 ATOM 23 O O . THR A 1 7 ? 10.384 31.315 6.235 1.00 53.98 ? 7 THR A O 1 ATOM 24 C CB . THR A 1 7 ? 12.024 30.231 8.907 1.00 57.47 ? 7 THR A CB 1 ATOM 25 O OG1 . THR A 1 7 ? 11.381 31.410 9.415 1.00 58.64 ? 7 THR A OG1 1 ATOM 26 C CG2 . THR A 1 7 ? 13.345 30.140 9.673 1.00 57.91 ? 7 THR A CG2 1 ATOM 27 N N . SER A 1 8 ? 10.508 29.079 6.475 1.00 51.37 ? 8 SER A N 1 ATOM 28 C CA . SER A 1 8 ? 9.319 28.803 5.705 1.00 48.93 ? 8 SER A CA 1 ATOM 29 C C . SER A 1 8 ? 8.569 27.707 6.448 1.00 45.26 ? 8 SER A C 1 ATOM 30 O O . SER A 1 8 ? 9.103 26.627 6.700 1.00 43.67 ? 8 SER A O 1 ATOM 31 C CB . SER A 1 8 ? 9.725 28.343 4.301 1.00 49.89 ? 8 SER A CB 1 ATOM 32 O OG . SER A 1 8 ? 8.628 27.865 3.538 1.00 50.92 ? 8 SER A OG 1 ATOM 33 N N . SER A 1 9 ? 7.333 27.998 6.813 1.00 41.20 ? 9 SER A N 1 ATOM 34 C CA . SER A 1 9 ? 6.491 27.001 7.456 1.00 38.87 ? 9 SER A CA 1 ATOM 35 C C . SER A 1 9 ? 5.341 26.580 6.552 1.00 37.56 ? 9 SER A C 1 ATOM 36 O O . SER A 1 9 ? 4.886 27.360 5.700 1.00 37.06 ? 9 SER A O 1 ATOM 37 C CB . SER A 1 9 ? 5.959 27.551 8.761 1.00 39.10 ? 9 SER A CB 1 ATOM 38 O OG . SER A 1 9 ? 5.058 28.582 8.486 1.00 40.40 ? 9 SER A OG 1 ATOM 39 N N . VAL A 1 10 ? 4.895 25.333 6.729 1.00 33.56 ? 10 VAL A N 1 ATOM 40 C CA . VAL A 1 10 ? 3.759 24.754 5.983 1.00 31.71 ? 10 VAL A CA 1 ATOM 41 C C . VAL A 1 10 ? 2.772 24.149 6.996 1.00 29.56 ? 10 VAL A C 1 ATOM 42 O O . VAL A 1 10 ? 3.183 23.401 7.879 1.00 27.32 ? 10 VAL A O 1 ATOM 43 C CB . VAL A 1 10 ? 4.229 23.622 5.001 1.00 32.45 ? 10 VAL A CB 1 ATOM 44 C CG1 . VAL A 1 10 ? 3.121 23.227 4.003 1.00 30.54 ? 10 VAL A CG1 1 ATOM 45 C CG2 . VAL A 1 10 ? 5.503 24.016 4.238 1.00 35.12 ? 10 VAL A CG2 1 ATOM 46 N N . ILE A 1 11 ? 1.488 24.500 6.878 1.00 27.65 ? 11 ILE A N 1 ATOM 47 C CA . ILE A 1 11 ? 0.407 23.981 7.735 1.00 28.09 ? 11 ILE A CA 1 ATOM 48 C C . ILE A 1 11 ? 0.110 22.527 7.380 1.00 27.08 ? 11 ILE A C 1 ATOM 49 O O . ILE A 1 11 ? -0.076 22.196 6.195 1.00 27.29 ? 11 ILE A O 1 ATOM 50 C CB . ILE A 1 11 ? -0.916 24.808 7.507 1.00 30.63 ? 11 ILE A CB 1 ATOM 51 C CG1 . ILE A 1 11 ? -0.782 26.290 7.890 1.00 30.27 ? 11 ILE A CG1 1 ATOM 52 C CG2 . ILE A 1 11 ? -2.129 24.175 8.195 1.00 33.95 ? 11 ILE A CG2 1 ATOM 53 C CD1 . ILE A 1 11 ? 0.022 26.571 9.110 1.00 28.42 ? 11 ILE A CD1 1 ATOM 54 N N . LEU A 1 12 ? -0.005 21.681 8.398 1.00 25.30 ? 12 LEU A N 1 ATOM 55 C CA . LEU A 1 12 ? -0.402 20.296 8.160 1.00 24.70 ? 12 LEU A CA 1 ATOM 56 C C . LEU A 1 12 ? -1.804 20.015 8.643 1.00 24.18 ? 12 LEU A C 1 ATOM 57 O O . LEU A 1 12 ? -2.275 20.640 9.589 1.00 21.65 ? 12 LEU A O 1 ATOM 58 C CB . LEU A 1 12 ? 0.568 19.295 8.828 1.00 22.88 ? 12 LEU A CB 1 ATOM 59 C CG . LEU A 1 12 ? 2.068 19.398 8.508 1.00 23.98 ? 12 LEU A CG 1 ATOM 60 C CD1 . LEU A 1 12 ? 2.899 18.265 9.151 1.00 21.33 ? 12 LEU A CD1 1 ATOM 61 C CD2 . LEU A 1 12 ? 2.375 19.468 7.018 1.00 23.78 ? 12 LEU A CD2 1 ATOM 62 N N . THR A 1 13 ? -2.434 19.049 7.975 1.00 23.31 ? 13 THR A N 1 ATOM 63 C CA . THR A 1 13 ? -3.705 18.452 8.343 1.00 24.10 ? 13 THR A CA 1 ATOM 64 C C . THR A 1 13 ? -3.436 17.071 8.990 1.00 24.72 ? 13 THR A C 1 ATOM 65 O O . THR A 1 13 ? -2.645 16.277 8.474 1.00 24.37 ? 13 THR A O 1 ATOM 66 C CB . THR A 1 13 ? -4.586 18.295 7.061 1.00 25.59 ? 13 THR A CB 1 ATOM 67 O OG1 . THR A 1 13 ? -4.987 19.591 6.589 1.00 27.51 ? 13 THR A OG1 1 ATOM 68 C CG2 . THR A 1 13 ? -5.926 17.604 7.349 1.00 23.99 ? 13 THR A CG2 1 ATOM 69 N N . ASN A 1 14 ? -4.101 16.822 10.115 1.00 22.09 ? 14 ASN A N 1 ATOM 70 C CA . ASN A 1 14 ? -4.031 15.553 10.859 1.00 25.27 ? 14 ASN A CA 1 ATOM 71 C C . ASN A 1 14 ? -5.271 14.738 10.495 1.00 24.70 ? 14 ASN A C 1 ATOM 72 O O . ASN A 1 14 ? -6.401 15.129 10.819 1.00 24.09 ? 14 ASN A O 1 ATOM 73 C CB . ASN A 1 14 ? -3.986 15.854 12.365 1.00 23.87 ? 14 ASN A CB 1 ATOM 74 C CG . ASN A 1 14 ? -4.047 14.602 13.246 1.00 24.18 ? 14 ASN A CG 1 ATOM 75 O OD1 . ASN A 1 14 ? -4.047 14.714 14.477 1.00 23.55 ? 14 ASN A OD1 1 ATOM 76 N ND2 . ASN A 1 14 ? -4.112 13.428 12.639 1.00 16.89 ? 14 ASN A ND2 1 ATOM 77 N N . TYR A 1 15 ? -5.077 13.661 9.739 1.00 24.16 ? 15 TYR A N 1 ATOM 78 C CA . TYR A 1 15 ? -6.158 12.723 9.529 1.00 25.61 ? 15 TYR A CA 1 ATOM 79 C C . TYR A 1 15 ? -6.038 11.562 10.523 1.00 26.49 ? 15 TYR A C 1 ATOM 80 O O . TYR A 1 15 ? -5.141 10.715 10.401 1.00 21.30 ? 15 TYR A O 1 ATOM 81 C CB . TYR A 1 15 ? -6.171 12.227 8.092 1.00 29.31 ? 15 TYR A CB 1 ATOM 82 C CG . TYR A 1 15 ? -7.179 11.146 7.817 1.00 30.22 ? 15 TYR A CG 1 ATOM 83 C CD1 . TYR A 1 15 ? -8.532 11.454 7.657 1.00 30.24 ? 15 TYR A CD1 1 ATOM 84 C CD2 . TYR A 1 15 ? -6.782 9.815 7.686 1.00 32.05 ? 15 TYR A CD2 1 ATOM 85 C CE1 . TYR A 1 15 ? -9.462 10.465 7.381 1.00 32.45 ? 15 TYR A CE1 1 ATOM 86 C CE2 . TYR A 1 15 ? -7.707 8.807 7.401 1.00 33.01 ? 15 TYR A CE2 1 ATOM 87 C CZ . TYR A 1 15 ? -9.049 9.146 7.251 1.00 33.67 ? 15 TYR A CZ 1 ATOM 88 O OH . TYR A 1 15 ? -9.975 8.166 6.957 1.00 33.65 ? 15 TYR A OH 1 ATOM 89 N N . MET A 1 16 ? -6.936 11.557 11.518 1.00 29.19 ? 16 MET A N 1 ATOM 90 C CA . MET A 1 16 ? -7.107 10.429 12.454 1.00 33.03 ? 16 MET A CA 1 ATOM 91 C C . MET A 1 16 ? -5.812 9.930 13.118 1.00 29.92 ? 16 MET A C 1 ATOM 92 O O . MET A 1 16 ? -5.662 8.727 13.447 1.00 23.41 ? 16 MET A O 1 ATOM 93 C CB . MET A 1 16 ? -7.864 9.299 11.744 1.00 37.31 ? 16 MET A CB 1 ATOM 94 C CG . MET A 1 16 ? -9.195 9.814 11.173 1.00 40.47 ? 16 MET A CG 1 ATOM 95 S SD . MET A 1 16 ? -10.413 8.526 10.883 1.00 46.95 ? 16 MET A SD 1 ATOM 96 C CE . MET A 1 16 ? -11.828 9.485 10.325 1.00 41.78 ? 16 MET A CE 1 ATOM 97 N N . ASP A 1 17 ? -4.886 10.873 13.333 1.00 25.98 ? 17 ASP A N 1 ATOM 98 C CA . ASP A 1 17 ? -3.622 10.590 14.013 1.00 25.13 ? 17 ASP A CA 1 ATOM 99 C C . ASP A 1 17 ? -2.633 9.720 13.198 1.00 25.36 ? 17 ASP A C 1 ATOM 100 O O . ASP A 1 17 ? -1.593 9.339 13.711 1.00 25.59 ? 17 ASP A O 1 ATOM 101 C CB . ASP A 1 17 ? -3.905 9.899 15.359 1.00 24.61 ? 17 ASP A CB 1 ATOM 102 C CG . ASP A 1 17 ? -4.196 10.874 16.517 1.00 26.40 ? 17 ASP A CG 1 ATOM 103 O OD1 . ASP A 1 17 ? -4.199 12.139 16.358 1.00 25.96 ? 17 ASP A OD1 1 ATOM 104 O OD2 . ASP A 1 17 ? -4.448 10.412 17.652 1.00 26.96 ? 17 ASP A OD2 1 ATOM 105 N N . THR A 1 18 ? -2.967 9.355 11.963 1.00 24.03 ? 18 THR A N 1 ATOM 106 C CA . THR A 1 18 ? -2.091 8.458 11.199 1.00 24.04 ? 18 THR A CA 1 ATOM 107 C C . THR A 1 18 ? -1.476 9.101 9.974 1.00 22.34 ? 18 THR A C 1 ATOM 108 O O . THR A 1 18 ? -0.539 8.546 9.398 1.00 23.09 ? 18 THR A O 1 ATOM 109 C CB . THR A 1 18 ? -2.820 7.173 10.766 1.00 22.61 ? 18 THR A CB 1 ATOM 110 O OG1 . THR A 1 18 ? -4.066 7.513 10.152 1.00 21.49 ? 18 THR A OG1 1 ATOM 111 C CG2 . THR A 1 18 ? -3.198 6.322 11.964 1.00 23.39 ? 18 THR A CG2 1 ATOM 112 N N . GLN A 1 19 ? -2.038 10.234 9.552 1.00 24.40 ? 19 GLN A N 1 ATOM 113 C CA . GLN A 1 19 ? -1.598 10.921 8.325 1.00 22.43 ? 19 GLN A CA 1 ATOM 114 C C . GLN A 1 19 ? -1.531 12.424 8.518 1.00 22.52 ? 19 GLN A C 1 ATOM 115 O O . GLN A 1 19 ? -2.525 13.083 8.834 1.00 21.70 ? 19 GLN A O 1 ATOM 116 C CB . GLN A 1 19 ? -2.561 10.628 7.166 1.00 24.46 ? 19 GLN A CB 1 ATOM 117 C CG . GLN A 1 19 ? -2.692 9.162 6.795 1.00 21.36 ? 19 GLN A CG 1 ATOM 118 C CD . GLN A 1 19 ? -3.735 8.936 5.730 1.00 22.98 ? 19 GLN A CD 1 ATOM 119 O OE1 . GLN A 1 19 ? -3.903 9.763 4.843 1.00 22.52 ? 19 GLN A OE1 1 ATOM 120 N NE2 . GLN A 1 19 ? -4.429 7.803 5.800 1.00 22.49 ? 19 GLN A NE2 1 ATOM 121 N N . TYR A 1 20 ? -0.355 12.966 8.289 1.00 21.01 ? 20 TYR A N 1 ATOM 122 C CA . TYR A 1 20 ? -0.091 14.384 8.527 1.00 21.78 ? 20 TYR A CA 1 ATOM 123 C C . TYR A 1 20 ? 0.439 14.893 7.213 1.00 20.57 ? 20 TYR A C 1 ATOM 124 O O . TYR A 1 20 ? 1.499 14.469 6.776 1.00 22.68 ? 20 TYR A O 1 ATOM 125 C CB . TYR A 1 20 ? 0.946 14.562 9.656 1.00 22.12 ? 20 TYR A CB 1 ATOM 126 C CG . TYR A 1 20 ? 0.410 14.209 11.039 1.00 21.34 ? 20 TYR A CG 1 ATOM 127 C CD1 . TYR A 1 20 ? -0.077 15.203 11.901 1.00 23.29 ? 20 TYR A CD1 1 ATOM 128 C CD2 . TYR A 1 20 ? 0.380 12.883 11.479 1.00 19.76 ? 20 TYR A CD2 1 ATOM 129 C CE1 . TYR A 1 20 ? -0.587 14.874 13.171 1.00 21.33 ? 20 TYR A CE1 1 ATOM 130 C CE2 . TYR A 1 20 ? -0.122 12.545 12.706 1.00 20.34 ? 20 TYR A CE2 1 ATOM 131 C CZ . TYR A 1 20 ? -0.586 13.550 13.566 1.00 21.99 ? 20 TYR A CZ 1 ATOM 132 O OH . TYR A 1 20 ? -1.092 13.219 14.800 1.00 21.91 ? 20 TYR A OH 1 ATOM 133 N N . TYR A 1 21 ? -0.329 15.739 6.543 1.00 21.35 ? 21 TYR A N 1 ATOM 134 C CA . TYR A 1 21 ? 0.041 16.195 5.209 1.00 22.80 ? 21 TYR A CA 1 ATOM 135 C C . TYR A 1 21 ? -0.154 17.685 4.958 1.00 22.47 ? 21 TYR A C 1 ATOM 136 O O . TYR A 1 21 ? -0.984 18.333 5.599 1.00 24.36 ? 21 TYR A O 1 ATOM 137 C CB . TYR A 1 21 ? -0.737 15.415 4.156 1.00 23.73 ? 21 TYR A CB 1 ATOM 138 C CG . TYR A 1 21 ? -2.252 15.411 4.372 1.00 23.11 ? 21 TYR A CG 1 ATOM 139 C CD1 . TYR A 1 21 ? -2.877 14.389 5.103 1.00 24.92 ? 21 TYR A CD1 1 ATOM 140 C CD2 . TYR A 1 21 ? -3.047 16.394 3.814 1.00 22.16 ? 21 TYR A CD2 1 ATOM 141 C CE1 . TYR A 1 21 ? -4.259 14.368 5.284 1.00 23.46 ? 21 TYR A CE1 1 ATOM 142 C CE2 . TYR A 1 21 ? -4.442 16.389 3.986 1.00 25.12 ? 21 TYR A CE2 1 ATOM 143 C CZ . TYR A 1 21 ? -5.026 15.366 4.720 1.00 25.99 ? 21 TYR A CZ 1 ATOM 144 O OH . TYR A 1 21 ? -6.386 15.363 4.898 1.00 27.70 ? 21 TYR A OH 1 ATOM 145 N N . GLY A 1 22 ? 0.562 18.203 3.954 1.00 25.17 ? 22 GLY A N 1 ATOM 146 C CA . GLY A 1 22 ? 0.550 19.631 3.633 1.00 23.78 ? 22 GLY A CA 1 ATOM 147 C C . GLY A 1 22 ? 0.635 19.860 2.142 1.00 30.07 ? 22 GLY A C 1 ATOM 148 O O . GLY A 1 22 ? 0.805 18.923 1.368 1.00 29.53 ? 22 GLY A O 1 ATOM 149 N N . GLU A 1 23 ? 0.527 21.108 1.728 1.00 28.78 ? 23 GLU A N 1 ATOM 150 C CA . GLU A 1 23 ? 0.454 21.386 0.323 1.00 33.55 ? 23 GLU A CA 1 ATOM 151 C C . GLU A 1 23 ? 1.827 21.700 -0.252 1.00 31.77 ? 23 GLU A C 1 ATOM 152 O O . GLU A 1 23 ? 2.697 22.296 0.437 1.00 33.54 ? 23 GLU A O 1 ATOM 153 C CB . GLU A 1 23 ? -0.532 22.544 0.065 1.00 36.37 ? 23 GLU A CB 1 ATOM 154 C CG . GLU A 1 23 ? -0.748 22.881 -1.404 1.00 38.09 ? 23 GLU A CG 1 ATOM 155 C CD . GLU A 1 23 ? -1.670 24.070 -1.579 1.00 41.46 ? 23 GLU A CD 1 ATOM 156 O OE1 . GLU A 1 23 ? -2.857 23.953 -1.180 1.00 43.98 ? 23 GLU A OE1 1 ATOM 157 O OE2 . GLU A 1 23 ? -1.206 25.122 -2.100 1.00 44.34 ? 23 GLU A OE2 1 ATOM 158 N N . ILE A 1 24 ? 2.022 21.249 -1.491 1.00 26.34 ? 24 ILE A N 1 ATOM 159 C CA . ILE A 1 24 ? 3.062 21.757 -2.389 1.00 26.95 ? 24 ILE A CA 1 ATOM 160 C C . ILE A 1 24 ? 2.405 22.115 -3.749 1.00 26.65 ? 24 ILE A C 1 ATOM 161 O O . ILE A 1 24 ? 1.279 21.693 -4.065 1.00 24.81 ? 24 ILE A O 1 ATOM 162 C CB . ILE A 1 24 ? 4.190 20.728 -2.606 1.00 26.95 ? 24 ILE A CB 1 ATOM 163 C CG1 . ILE A 1 24 ? 3.649 19.496 -3.329 1.00 23.67 ? 24 ILE A CG1 1 ATOM 164 C CG2 . ILE A 1 24 ? 4.909 20.389 -1.283 1.00 25.13 ? 24 ILE A CG2 1 ATOM 165 C CD1 . ILE A 1 24 ? 4.743 18.605 -3.903 1.00 27.43 ? 24 ILE A CD1 1 ATOM 166 N N . GLY A 1 25 ? 3.115 22.897 -4.548 1.00 26.63 ? 25 GLY A N 1 ATOM 167 C CA . GLY A 1 25 ? 2.651 23.259 -5.888 1.00 23.33 ? 25 GLY A CA 1 ATOM 168 C C . GLY A 1 25 ? 3.762 22.870 -6.844 1.00 25.47 ? 25 GLY A C 1 ATOM 169 O O . GLY A 1 25 ? 4.930 23.121 -6.564 1.00 26.72 ? 25 GLY A O 1 ATOM 170 N N . ILE A 1 26 ? 3.406 22.230 -7.951 1.00 24.00 ? 26 ILE A N 1 ATOM 171 C CA . ILE A 1 26 ? 4.385 21.816 -8.957 1.00 24.49 ? 26 ILE A CA 1 ATOM 172 C C . ILE A 1 26 ? 3.989 22.358 -10.315 1.00 26.19 ? 26 ILE A C 1 ATOM 173 O O . ILE A 1 26 ? 2.853 22.146 -10.755 1.00 24.61 ? 26 ILE A O 1 ATOM 174 C CB . ILE A 1 26 ? 4.496 20.266 -9.064 1.00 22.50 ? 26 ILE A CB 1 ATOM 175 C CG1 . ILE A 1 26 ? 4.617 19.629 -7.685 1.00 24.70 ? 26 ILE A CG1 1 ATOM 176 C CG2 . ILE A 1 26 ? 5.694 19.853 -9.994 1.00 24.23 ? 26 ILE A CG2 1 ATOM 177 C CD1 . ILE A 1 26 ? 4.765 18.116 -7.726 1.00 23.91 ? 26 ILE A CD1 1 ATOM 178 N N . GLY A 1 27 ? 4.927 23.041 -10.979 1.00 25.68 ? 27 GLY A N 1 ATOM 179 C CA . GLY A 1 27 ? 4.729 23.440 -12.372 1.00 22.97 ? 27 GLY A CA 1 ATOM 180 C C . GLY A 1 27 ? 4.274 24.877 -12.527 1.00 28.75 ? 27 GLY A C 1 ATOM 181 O O . GLY A 1 27 ? 4.141 25.595 -11.536 1.00 29.18 ? 27 GLY A O 1 ATOM 182 N N . THR A 1 28 ? 4.049 25.269 -13.789 1.00 30.56 ? 28 THR A N 1 ATOM 183 C CA . THR A 1 28 ? 3.580 26.591 -14.213 1.00 29.17 ? 28 THR A CA 1 ATOM 184 C C . THR A 1 28 ? 2.385 26.420 -15.154 1.00 27.24 ? 28 THR A C 1 ATOM 185 O O . THR A 1 28 ? 2.532 25.834 -16.209 1.00 30.36 ? 28 THR A O 1 ATOM 186 C CB . THR A 1 28 ? 4.703 27.296 -14.979 1.00 28.58 ? 28 THR A CB 1 ATOM 187 O OG1 . THR A 1 28 ? 5.840 27.411 -14.121 1.00 27.59 ? 28 THR A OG1 1 ATOM 188 C CG2 . THR A 1 28 ? 4.323 28.719 -15.321 1.00 27.26 ? 28 THR A CG2 1 ATOM 189 N N . PRO A 1 29 ? 1.189 26.853 -14.765 1.00 25.80 ? 29 PRO A N 1 ATOM 190 C CA . PRO A 1 29 ? 0.927 27.434 -13.462 1.00 28.00 ? 29 PRO A CA 1 ATOM 191 C C . PRO A 1 29 ? 0.942 26.278 -12.459 1.00 28.20 ? 29 PRO A C 1 ATOM 192 O O . PRO A 1 29 ? 0.968 25.135 -12.918 1.00 26.87 ? 29 PRO A O 1 ATOM 193 C CB . PRO A 1 29 ? -0.486 27.992 -13.621 1.00 24.97 ? 29 PRO A CB 1 ATOM 194 C CG . PRO A 1 29 ? -1.118 27.053 -14.604 1.00 26.89 ? 29 PRO A CG 1 ATOM 195 C CD . PRO A 1 29 ? -0.030 26.738 -15.585 1.00 24.40 ? 29 PRO A CD 1 ATOM 196 N N . PRO A 1 30 ? 0.944 26.576 -11.146 1.00 29.64 ? 30 PRO A N 1 ATOM 197 C CA . PRO A 1 30 ? 1.079 25.566 -10.069 1.00 30.91 ? 30 PRO A CA 1 ATOM 198 C C . PRO A 1 30 ? -0.050 24.538 -10.011 1.00 30.62 ? 30 PRO A C 1 ATOM 199 O O . PRO A 1 30 ? -1.217 24.917 -10.100 1.00 30.24 ? 30 PRO A O 1 ATOM 200 C CB . PRO A 1 30 ? 1.055 26.411 -8.794 1.00 33.41 ? 30 PRO A CB 1 ATOM 201 C CG . PRO A 1 30 ? 1.486 27.822 -9.264 1.00 34.06 ? 30 PRO A CG 1 ATOM 202 C CD . PRO A 1 30 ? 0.836 27.941 -10.590 1.00 30.85 ? 30 PRO A CD 1 ATOM 203 N N . GLN A 1 31 ? 0.320 23.252 -9.942 1.00 28.98 ? 31 GLN A N 1 ATOM 204 C CA . GLN A 1 31 ? -0.616 22.134 -9.732 1.00 28.21 ? 31 GLN A CA 1 ATOM 205 C C . GLN A 1 31 ? -0.395 21.655 -8.292 1.00 28.30 ? 31 GLN A C 1 ATOM 206 O O . GLN A 1 31 ? 0.732 21.210 -7.959 1.00 24.68 ? 31 GLN A O 1 ATOM 207 C CB . GLN A 1 31 ? -0.342 20.979 -10.724 1.00 30.39 ? 31 GLN A CB 1 ATOM 208 C CG . GLN A 1 31 ? -0.812 21.188 -12.159 1.00 27.93 ? 31 GLN A CG 1 ATOM 209 C CD . GLN A 1 31 ? -0.309 20.120 -13.141 1.00 26.60 ? 31 GLN A CD 1 ATOM 210 O OE1 . GLN A 1 31 ? -0.598 18.933 -12.980 1.00 24.52 ? 31 GLN A OE1 1 ATOM 211 N NE2 . GLN A 1 31 ? 0.406 20.554 -14.186 1.00 21.93 ? 31 GLN A NE2 1 ATOM 212 N N . THR A 1 32 ? -1.446 21.745 -7.450 1.00 24.24 ? 32 THR A N 1 ATOM 213 C CA . THR A 1 32 ? -1.314 21.485 -6.013 1.00 23.17 ? 32 THR A CA 1 ATOM 214 C C . THR A 1 32 ? -1.617 20.050 -5.627 1.00 22.59 ? 32 THR A C 1 ATOM 215 O O . THR A 1 32 ? -2.548 19.406 -6.157 1.00 23.40 ? 32 THR A O 1 ATOM 216 C CB . THR A 1 32 ? -2.189 22.399 -5.132 1.00 24.24 ? 32 THR A CB 1 ATOM 217 O OG1 . THR A 1 32 ? -3.574 22.197 -5.467 1.00 29.74 ? 32 THR A OG1 1 ATOM 218 C CG2 . THR A 1 32 ? -1.942 23.868 -5.412 1.00 24.96 ? 32 THR A CG2 1 ATOM 219 N N . PHE A 1 33 ? -0.825 19.583 -4.675 1.00 22.02 ? 33 PHE A N 1 ATOM 220 C CA . PHE A 1 33 ? -0.864 18.229 -4.199 1.00 23.44 ? 33 PHE A CA 1 ATOM 221 C C . PHE A 1 33 ? -0.715 18.245 -2.690 1.00 24.39 ? 33 PHE A C 1 ATOM 222 O O . PHE A 1 33 ? 0.055 19.043 -2.140 1.00 25.86 ? 33 PHE A O 1 ATOM 223 C CB . PHE A 1 33 ? 0.299 17.444 -4.822 1.00 23.42 ? 33 PHE A CB 1 ATOM 224 C CG . PHE A 1 33 ? 0.177 17.266 -6.300 1.00 24.95 ? 33 PHE A CG 1 ATOM 225 C CD1 . PHE A 1 33 ? -0.521 16.178 -6.815 1.00 18.67 ? 33 PHE A CD1 1 ATOM 226 C CD2 . PHE A 1 33 ? 0.745 18.198 -7.181 1.00 22.15 ? 33 PHE A CD2 1 ATOM 227 C CE1 . PHE A 1 33 ? -0.651 16.021 -8.174 1.00 22.50 ? 33 PHE A CE1 1 ATOM 228 C CE2 . PHE A 1 33 ? 0.625 18.050 -8.546 1.00 21.63 ? 33 PHE A CE2 1 ATOM 229 C CZ . PHE A 1 33 ? -0.085 16.946 -9.051 1.00 20.43 ? 33 PHE A CZ 1 ATOM 230 N N . LYS A 1 34 ? -1.448 17.363 -2.019 1.00 24.22 ? 34 LYS A N 1 ATOM 231 C CA . LYS A 1 34 ? -1.225 17.110 -0.607 1.00 23.07 ? 34 LYS A CA 1 ATOM 232 C C . LYS A 1 34 ? -0.160 16.035 -0.474 1.00 22.36 ? 34 LYS A C 1 ATOM 233 O O . LYS A 1 34 ? -0.211 14.971 -1.123 1.00 24.70 ? 34 LYS A O 1 ATOM 234 C CB . LYS A 1 34 ? -2.502 16.643 0.091 1.00 26.57 ? 34 LYS A CB 1 ATOM 235 C CG . LYS A 1 34 ? -3.741 17.496 -0.214 1.00 29.36 ? 34 LYS A CG 1 ATOM 236 C CD . LYS A 1 34 ? -4.833 17.142 0.766 1.00 36.62 ? 34 LYS A CD 1 ATOM 237 C CE . LYS A 1 34 ? -6.198 17.071 0.175 1.00 37.94 ? 34 LYS A CE 1 ATOM 238 N NZ . LYS A 1 34 ? -6.425 15.661 -0.176 1.00 39.32 ? 34 LYS A NZ 1 ATOM 239 N N . VAL A 1 35 ? 0.811 16.313 0.368 1.00 21.72 ? 35 VAL A N 1 ATOM 240 C CA . VAL A 1 35 ? 1.930 15.404 0.544 1.00 21.24 ? 35 VAL A CA 1 ATOM 241 C C . VAL A 1 35 ? 2.274 15.188 2.012 1.00 20.31 ? 35 VAL A C 1 ATOM 242 O O . VAL A 1 35 ? 2.099 16.089 2.848 1.00 21.32 ? 35 VAL A O 1 ATOM 243 C CB . VAL A 1 35 ? 3.177 15.886 -0.266 1.00 20.55 ? 35 VAL A CB 1 ATOM 244 C CG1 . VAL A 1 35 ? 2.868 15.966 -1.752 1.00 23.35 ? 35 VAL A CG1 1 ATOM 245 C CG2 . VAL A 1 35 ? 3.696 17.218 0.292 1.00 19.21 ? 35 VAL A CG2 1 ATOM 246 N N . VAL A 1 36 ? 2.730 13.969 2.327 1.00 22.12 ? 36 VAL A N 1 ATOM 247 C CA . VAL A 1 36 ? 3.490 13.690 3.550 1.00 19.62 ? 36 VAL A CA 1 ATOM 248 C C . VAL A 1 36 ? 4.969 14.132 3.365 1.00 19.11 ? 36 VAL A C 1 ATOM 249 O O . VAL A 1 36 ? 5.583 13.829 2.372 1.00 19.53 ? 36 VAL A O 1 ATOM 250 C CB . VAL A 1 36 ? 3.462 12.136 3.918 1.00 20.86 ? 36 VAL A CB 1 ATOM 251 C CG1 . VAL A 1 36 ? 4.398 11.842 5.070 1.00 19.45 ? 36 VAL A CG1 1 ATOM 252 C CG2 . VAL A 1 36 ? 2.079 11.693 4.338 1.00 22.31 ? 36 VAL A CG2 1 ATOM 253 N N . PHE A 1 37 ? 5.505 14.864 4.336 1.00 19.79 ? 37 PHE A N 1 ATOM 254 C CA . PHE A 1 37 ? 6.932 15.154 4.467 1.00 20.46 ? 37 PHE A CA 1 ATOM 255 C C . PHE A 1 37 ? 7.576 14.060 5.313 1.00 21.35 ? 37 PHE A C 1 ATOM 256 O O . PHE A 1 37 ? 7.312 13.935 6.502 1.00 23.04 ? 37 PHE A O 1 ATOM 257 C CB . PHE A 1 37 ? 7.115 16.559 5.074 1.00 20.01 ? 37 PHE A CB 1 ATOM 258 C CG . PHE A 1 37 ? 6.471 17.641 4.247 1.00 22.01 ? 37 PHE A CG 1 ATOM 259 C CD1 . PHE A 1 37 ? 5.145 18.023 4.465 1.00 22.65 ? 37 PHE A CD1 1 ATOM 260 C CD2 . PHE A 1 37 ? 7.165 18.239 3.230 1.00 24.17 ? 37 PHE A CD2 1 ATOM 261 C CE1 . PHE A 1 37 ? 4.565 18.988 3.699 1.00 23.30 ? 37 PHE A CE1 1 ATOM 262 C CE2 . PHE A 1 37 ? 6.574 19.204 2.437 1.00 26.00 ? 37 PHE A CE2 1 ATOM 263 C CZ . PHE A 1 37 ? 5.282 19.579 2.666 1.00 21.69 ? 37 PHE A CZ 1 ATOM 264 N N . ASP A 1 38 ? 8.406 13.255 4.653 1.00 23.61 ? 38 ASP A N 1 ATOM 265 C CA . ASP A 1 38 ? 8.811 11.933 5.122 1.00 25.36 ? 38 ASP A CA 1 ATOM 266 C C . ASP A 1 38 ? 10.320 11.857 5.325 1.00 22.44 ? 38 ASP A C 1 ATOM 267 O O . ASP A 1 38 ? 11.045 11.924 4.357 1.00 22.62 ? 38 ASP A O 1 ATOM 268 C CB . ASP A 1 38 ? 8.429 10.919 4.036 1.00 23.28 ? 38 ASP A CB 1 ATOM 269 C CG . ASP A 1 38 ? 8.478 9.482 4.527 1.00 30.06 ? 38 ASP A CG 1 ATOM 270 O OD1 . ASP A 1 38 ? 9.500 9.030 5.023 1.00 33.36 ? 38 ASP A OD1 1 ATOM 271 O OD2 . ASP A 1 38 ? 7.515 8.725 4.474 1.00 33.18 ? 38 ASP A OD2 1 ATOM 272 N N . THR A 1 39 ? 10.780 11.734 6.570 1.00 26.41 ? 39 THR A N 1 ATOM 273 C CA . THR A 1 39 ? 12.228 11.576 6.863 1.00 24.08 ? 39 THR A CA 1 ATOM 274 C C . THR A 1 39 ? 12.814 10.170 6.562 1.00 27.93 ? 39 THR A C 1 ATOM 275 O O . THR A 1 39 ? 14.025 10.005 6.511 1.00 29.13 ? 39 THR A O 1 ATOM 276 C CB . THR A 1 39 ? 12.563 12.057 8.296 1.00 23.72 ? 39 THR A CB 1 ATOM 277 O OG1 . THR A 1 39 ? 11.684 11.447 9.245 1.00 28.08 ? 39 THR A OG1 1 ATOM 278 C CG2 . THR A 1 39 ? 12.216 13.554 8.473 1.00 23.50 ? 39 THR A CG2 1 ATOM 279 N N . GLY A 1 40 ? 11.959 9.184 6.287 1.00 28.19 ? 40 GLY A N 1 ATOM 280 C CA . GLY A 1 40 ? 12.408 7.827 5.956 1.00 27.98 ? 40 GLY A CA 1 ATOM 281 C C . GLY A 1 40 ? 12.565 7.506 4.490 1.00 29.56 ? 40 GLY A C 1 ATOM 282 O O . GLY A 1 40 ? 12.717 6.340 4.101 1.00 30.91 ? 40 GLY A O 1 ATOM 283 N N . SER A 1 41 ? 12.515 8.540 3.653 1.00 27.21 ? 41 SER A N 1 ATOM 284 C CA . SER A 1 41 ? 12.715 8.380 2.247 1.00 24.19 ? 41 SER A CA 1 ATOM 285 C C . SER A 1 41 ? 13.333 9.667 1.682 1.00 25.67 ? 41 SER A C 1 ATOM 286 O O . SER A 1 41 ? 13.308 10.713 2.358 1.00 24.97 ? 41 SER A O 1 ATOM 287 C CB . SER A 1 41 ? 11.413 7.974 1.551 1.00 27.31 ? 41 SER A CB 1 ATOM 288 O OG . SER A 1 41 ? 10.452 9.014 1.519 1.00 26.49 ? 41 SER A OG 1 ATOM 289 N N . SER A 1 42 ? 13.904 9.559 0.479 1.00 26.92 ? 42 SER A N 1 ATOM 290 C CA . SER A 1 42 ? 14.650 10.664 -0.168 1.00 28.16 ? 42 SER A CA 1 ATOM 291 C C . SER A 1 42 ? 14.167 11.105 -1.564 1.00 26.33 ? 42 SER A C 1 ATOM 292 O O . SER A 1 42 ? 14.850 11.885 -2.234 1.00 29.64 ? 42 SER A O 1 ATOM 293 C CB . SER A 1 42 ? 16.135 10.323 -0.232 1.00 27.21 ? 42 SER A CB 1 ATOM 294 O OG . SER A 1 42 ? 16.626 9.915 1.043 1.00 29.13 ? 42 SER A OG 1 ATOM 295 N N . ASN A 1 43 ? 13.015 10.616 -2.018 1.00 26.41 ? 43 ASN A N 1 ATOM 296 C CA . ASN A 1 43 ? 12.493 10.960 -3.353 1.00 21.63 ? 43 ASN A CA 1 ATOM 297 C C . ASN A 1 43 ? 11.188 11.723 -3.231 1.00 23.50 ? 43 ASN A C 1 ATOM 298 O O . ASN A 1 43 ? 10.420 11.456 -2.305 1.00 24.03 ? 43 ASN A O 1 ATOM 299 C CB . ASN A 1 43 ? 12.202 9.680 -4.169 1.00 23.31 ? 43 ASN A CB 1 ATOM 300 C CG . ASN A 1 43 ? 13.469 8.945 -4.616 1.00 26.28 ? 43 ASN A CG 1 ATOM 301 O OD1 . ASN A 1 43 ? 14.036 8.161 -3.867 1.00 28.43 ? 43 ASN A OD1 1 ATOM 302 N ND2 . ASN A 1 43 ? 13.904 9.191 -5.841 1.00 24.68 ? 43 ASN A ND2 1 ATOM 303 N N . VAL A 1 44 ? 10.916 12.650 -4.155 1.00 23.26 ? 44 VAL A N 1 ATOM 304 C CA . VAL A 1 44 ? 9.558 13.245 -4.264 1.00 23.13 ? 44 VAL A CA 1 ATOM 305 C C . VAL A 1 44 ? 8.714 12.352 -5.190 1.00 20.96 ? 44 VAL A C 1 ATOM 306 O O . VAL A 1 44 ? 9.208 11.924 -6.223 1.00 20.90 ? 44 VAL A O 1 ATOM 307 C CB . VAL A 1 44 ? 9.618 14.725 -4.767 1.00 22.31 ? 44 VAL A CB 1 ATOM 308 C CG1 . VAL A 1 44 ? 8.241 15.305 -4.973 1.00 21.43 ? 44 VAL A CG1 1 ATOM 309 C CG2 . VAL A 1 44 ? 10.409 15.607 -3.774 1.00 19.64 ? 44 VAL A CG2 1 ATOM 310 N N . TRP A 1 45 ? 7.480 12.032 -4.815 1.00 20.17 ? 45 TRP A N 1 ATOM 311 C CA . TRP A 1 45 ? 6.603 11.230 -5.672 1.00 21.05 ? 45 TRP A CA 1 ATOM 312 C C . TRP A 1 45 ? 5.220 11.874 -5.781 1.00 21.58 ? 45 TRP A C 1 ATOM 313 O O . TRP A 1 45 ? 4.647 12.211 -4.765 1.00 23.59 ? 45 TRP A O 1 ATOM 314 C CB . TRP A 1 45 ? 6.353 9.838 -5.059 1.00 25.37 ? 45 TRP A CB 1 ATOM 315 C CG . TRP A 1 45 ? 7.503 8.862 -4.989 1.00 25.29 ? 45 TRP A CG 1 ATOM 316 C CD1 . TRP A 1 45 ? 8.301 8.646 -3.925 1.00 25.39 ? 45 TRP A CD1 1 ATOM 317 C CD2 . TRP A 1 45 ? 7.908 7.912 -5.991 1.00 25.07 ? 45 TRP A CD2 1 ATOM 318 N NE1 . TRP A 1 45 ? 9.197 7.640 -4.195 1.00 26.31 ? 45 TRP A NE1 1 ATOM 319 C CE2 . TRP A 1 45 ? 8.974 7.169 -5.457 1.00 25.02 ? 45 TRP A CE2 1 ATOM 320 C CE3 . TRP A 1 45 ? 7.480 7.617 -7.292 1.00 28.99 ? 45 TRP A CE3 1 ATOM 321 C CZ2 . TRP A 1 45 ? 9.634 6.164 -6.173 1.00 25.15 ? 45 TRP A CZ2 1 ATOM 322 C CZ3 . TRP A 1 45 ? 8.136 6.611 -8.014 1.00 26.68 ? 45 TRP A CZ3 1 ATOM 323 C CH2 . TRP A 1 45 ? 9.197 5.889 -7.436 1.00 26.14 ? 45 TRP A CH2 1 ATOM 324 N N . VAL A 1 46 ? 4.681 12.046 -6.984 1.00 22.79 ? 46 VAL A N 1 ATOM 325 C CA . VAL A 1 46 ? 3.254 12.388 -7.129 1.00 21.99 ? 46 VAL A CA 1 ATOM 326 C C . VAL A 1 46 ? 2.685 11.447 -8.147 1.00 20.09 ? 46 VAL A C 1 ATOM 327 O O . VAL A 1 46 ? 3.461 10.929 -8.956 1.00 21.06 ? 46 VAL A O 1 ATOM 328 C CB . VAL A 1 46 ? 2.981 13.875 -7.563 1.00 22.15 ? 46 VAL A CB 1 ATOM 329 C CG1 . VAL A 1 46 ? 3.327 14.858 -6.399 1.00 24.59 ? 46 VAL A CG1 1 ATOM 330 C CG2 . VAL A 1 46 ? 3.736 14.220 -8.838 1.00 21.94 ? 46 VAL A CG2 1 ATOM 331 N N . PRO A 1 47 ? 1.353 11.233 -8.154 1.00 20.86 ? 47 PRO A N 1 ATOM 332 C CA . PRO A 1 47 ? 0.717 10.383 -9.209 1.00 21.57 ? 47 PRO A CA 1 ATOM 333 C C . PRO A 1 47 ? 0.769 11.045 -10.581 1.00 22.46 ? 47 PRO A C 1 ATOM 334 O O . PRO A 1 47 ? 0.632 12.279 -10.676 1.00 25.94 ? 47 PRO A O 1 ATOM 335 C CB . PRO A 1 47 ? -0.743 10.254 -8.755 1.00 20.23 ? 47 PRO A CB 1 ATOM 336 C CG . PRO A 1 47 ? -0.837 10.878 -7.345 1.00 22.11 ? 47 PRO A CG 1 ATOM 337 C CD . PRO A 1 47 ? 0.360 11.796 -7.221 1.00 19.89 ? 47 PRO A CD 1 ATOM 338 N N . SER A 1 48 ? 0.949 10.250 -11.636 1.00 22.98 ? 48 SER A N 1 ATOM 339 C CA . SER A 1 48 ? 1.019 10.773 -12.982 1.00 24.03 ? 48 SER A CA 1 ATOM 340 C C . SER A 1 48 ? -0.338 10.751 -13.681 1.00 26.15 ? 48 SER A C 1 ATOM 341 O O . SER A 1 48 ? -1.165 9.848 -13.456 1.00 24.44 ? 48 SER A O 1 ATOM 342 C CB . SER A 1 48 ? 2.053 10.001 -13.811 1.00 28.63 ? 48 SER A CB 1 ATOM 343 O OG . SER A 1 48 ? 2.043 10.385 -15.187 1.00 27.88 ? 48 SER A OG 1 ATOM 344 N N . SER A 1 49 ? -0.549 11.733 -14.556 1.00 22.21 ? 49 SER A N 1 ATOM 345 C CA . SER A 1 49 ? -1.696 11.721 -15.429 1.00 24.34 ? 49 SER A CA 1 ATOM 346 C C . SER A 1 49 ? -1.575 10.520 -16.366 1.00 25.61 ? 49 SER A C 1 ATOM 347 O O . SER A 1 49 ? -2.559 10.106 -16.976 1.00 26.31 ? 49 SER A O 1 ATOM 348 C CB . SER A 1 49 ? -1.832 13.025 -16.216 1.00 25.25 ? 49 SER A CB 1 ATOM 349 O OG . SER A 1 49 ? -0.724 13.199 -17.093 1.00 32.81 ? 49 SER A OG 1 ATOM 350 N N . LYS A 1 50 ? -0.379 9.948 -16.463 1.00 24.24 ? 50 LYS A N 1 ATOM 351 C CA . LYS A 1 50 ? -0.200 8.691 -17.235 1.00 28.24 ? 50 LYS A CA 1 ATOM 352 C C . LYS A 1 50 ? -0.632 7.411 -16.478 1.00 30.20 ? 50 LYS A C 1 ATOM 353 O O . LYS A 1 50 ? -0.615 6.309 -17.048 1.00 33.71 ? 50 LYS A O 1 ATOM 354 C CB . LYS A 1 50 ? 1.220 8.557 -17.781 1.00 27.75 ? 50 LYS A CB 1 ATOM 355 C CG . LYS A 1 50 ? 1.515 9.453 -18.973 1.00 32.91 ? 50 LYS A CG 1 ATOM 356 C CD . LYS A 1 50 ? 2.043 10.824 -18.549 1.00 35.22 ? 50 LYS A CD 1 ATOM 357 C CE . LYS A 1 50 ? 2.583 11.636 -19.743 1.00 39.89 ? 50 LYS A CE 1 ATOM 358 N NZ . LYS A 1 50 ? 2.905 13.063 -19.394 1.00 38.56 ? 50 LYS A NZ 1 ATOM 359 N N . CYS A 1 51 ? -1.067 7.563 -15.228 1.00 26.79 ? 51 CYS A N 1 ATOM 360 C CA . CYS A 1 51 ? -1.594 6.437 -14.461 1.00 28.59 ? 51 CYS A CA 1 ATOM 361 C C . CYS A 1 51 ? -2.954 5.992 -14.974 1.00 31.00 ? 51 CYS A C 1 ATOM 362 O O . CYS A 1 51 ? -3.881 6.809 -15.019 1.00 30.85 ? 51 CYS A O 1 ATOM 363 C CB . CYS A 1 51 ? -1.714 6.817 -13.000 1.00 29.68 ? 51 CYS A CB 1 ATOM 364 S SG . CYS A 1 51 ? -1.889 5.404 -11.870 1.00 32.01 ? 51 CYS A SG 1 ATOM 365 N N . SER A 1 52 ? -3.064 4.720 -15.377 1.00 28.21 ? 52 SER A N 1 ATOM 366 C CA . SER A 1 52 ? -4.364 4.126 -15.822 1.00 30.73 ? 52 SER A CA 1 ATOM 367 C C . SER A 1 52 ? -5.508 4.338 -14.816 1.00 31.16 ? 52 SER A C 1 ATOM 368 O O . SER A 1 52 ? -5.312 4.187 -13.604 1.00 29.41 ? 52 SER A O 1 ATOM 369 C CB . SER A 1 52 ? -4.219 2.609 -16.092 1.00 32.84 ? 52 SER A CB 1 ATOM 370 O OG . SER A 1 52 ? -5.487 1.952 -16.134 1.00 35.67 ? 52 SER A OG 1 ATOM 371 N N . ARG A 1 53 ? -6.713 4.658 -15.303 1.00 32.03 ? 53 ARG A N 1 ATOM 372 C CA . ARG A 1 53 ? -7.846 4.810 -14.375 1.00 31.75 ? 53 ARG A CA 1 ATOM 373 C C . ARG A 1 53 ? -8.319 3.475 -13.800 1.00 30.00 ? 53 ARG A C 1 ATOM 374 O O . ARG A 1 53 ? -9.237 3.431 -12.977 1.00 28.17 ? 53 ARG A O 1 ATOM 375 C CB . ARG A 1 53 ? -9.006 5.575 -15.011 1.00 35.43 ? 53 ARG A CB 1 ATOM 376 C CG . ARG A 1 53 ? -9.564 4.945 -16.274 1.00 37.96 ? 53 ARG A CG 1 ATOM 377 C CD . ARG A 1 53 ? -10.948 5.453 -16.642 1.00 41.46 ? 53 ARG A CD 1 ATOM 378 N NE . ARG A 1 53 ? -11.593 4.569 -17.611 1.00 45.23 ? 53 ARG A NE 1 ATOM 379 C CZ . ARG A 1 53 ? -12.449 3.593 -17.304 1.00 46.20 ? 53 ARG A CZ 1 ATOM 380 N NH1 . ARG A 1 53 ? -12.786 3.354 -16.034 1.00 46.53 ? 53 ARG A NH1 1 ATOM 381 N NH2 . ARG A 1 53 ? -12.979 2.854 -18.281 1.00 44.79 ? 53 ARG A NH2 1 ATOM 382 N N . LEU A 1 54 ? -7.675 2.387 -14.209 1.00 27.82 ? 54 LEU A N 1 ATOM 383 C CA . LEU A 1 54 ? -7.888 1.115 -13.550 1.00 28.93 ? 54 LEU A CA 1 ATOM 384 C C . LEU A 1 54 ? -6.936 0.902 -12.377 1.00 29.82 ? 54 LEU A C 1 ATOM 385 O O . LEU A 1 54 ? -6.766 -0.242 -11.915 1.00 32.85 ? 54 LEU A O 1 ATOM 386 C CB . LEU A 1 54 ? -7.812 -0.049 -14.545 1.00 29.74 ? 54 LEU A CB 1 ATOM 387 C CG . LEU A 1 54 ? -9.135 -0.529 -15.155 1.00 32.16 ? 54 LEU A CG 1 ATOM 388 C CD1 . LEU A 1 54 ? -9.956 0.606 -15.738 1.00 31.88 ? 54 LEU A CD1 1 ATOM 389 C CD2 . LEU A 1 54 ? -8.922 -1.676 -16.173 1.00 30.86 ? 54 LEU A CD2 1 ATOM 390 N N . TYR A 1 55 ? -6.300 1.981 -11.904 1.00 27.01 ? 55 TYR A N 1 ATOM 391 C CA . TYR A 1 55 ? -5.686 1.976 -10.558 1.00 27.66 ? 55 TYR A CA 1 ATOM 392 C C . TYR A 1 55 ? -6.551 2.811 -9.601 1.00 27.84 ? 55 TYR A C 1 ATOM 393 O O . TYR A 1 55 ? -6.740 3.998 -9.819 1.00 25.19 ? 55 TYR A O 1 ATOM 394 C CB . TYR A 1 55 ? -4.231 2.474 -10.569 1.00 27.65 ? 55 TYR A CB 1 ATOM 395 C CG . TYR A 1 55 ? -3.286 1.538 -11.287 1.00 27.01 ? 55 TYR A CG 1 ATOM 396 C CD1 . TYR A 1 55 ? -2.752 0.423 -10.640 1.00 25.69 ? 55 TYR A CD1 1 ATOM 397 C CD2 . TYR A 1 55 ? -2.949 1.742 -12.609 1.00 25.31 ? 55 TYR A CD2 1 ATOM 398 C CE1 . TYR A 1 55 ? -1.909 -0.458 -11.310 1.00 25.14 ? 55 TYR A CE1 1 ATOM 399 C CE2 . TYR A 1 55 ? -2.096 0.852 -13.284 1.00 26.78 ? 55 TYR A CE2 1 ATOM 400 C CZ . TYR A 1 55 ? -1.595 -0.242 -12.626 1.00 24.00 ? 55 TYR A CZ 1 ATOM 401 O OH . TYR A 1 55 ? -0.743 -1.120 -13.280 1.00 26.75 ? 55 TYR A OH 1 ATOM 402 N N . THR A 1 56 ? -7.091 2.166 -8.563 1.00 27.32 ? 56 THR A N 1 ATOM 403 C CA . THR A 1 56 ? -7.931 2.841 -7.587 1.00 31.78 ? 56 THR A CA 1 ATOM 404 C C . THR A 1 56 ? -7.137 3.954 -6.876 1.00 30.39 ? 56 THR A C 1 ATOM 405 O O . THR A 1 56 ? -7.659 5.042 -6.685 1.00 30.17 ? 56 THR A O 1 ATOM 406 C CB . THR A 1 56 ? -8.507 1.828 -6.558 1.00 33.25 ? 56 THR A CB 1 ATOM 407 O OG1 . THR A 1 56 ? -9.278 0.828 -7.233 1.00 36.89 ? 56 THR A OG1 1 ATOM 408 C CG2 . THR A 1 56 ? -9.531 2.490 -5.702 1.00 31.72 ? 56 THR A CG2 1 ATOM 409 N N . ALA A 1 57 ? -5.875 3.678 -6.533 1.00 31.16 ? 57 ALA A N 1 ATOM 410 C CA . ALA A 1 57 ? -4.994 4.689 -5.941 1.00 33.17 ? 57 ALA A CA 1 ATOM 411 C C . ALA A 1 57 ? -4.830 5.912 -6.845 1.00 34.45 ? 57 ALA A C 1 ATOM 412 O O . ALA A 1 57 ? -4.555 7.011 -6.375 1.00 38.54 ? 57 ALA A O 1 ATOM 413 C CB . ALA A 1 57 ? -3.630 4.093 -5.601 1.00 31.54 ? 57 ALA A CB 1 ATOM 414 N N . CYS A 1 58 ? -4.996 5.745 -8.142 1.00 31.99 ? 58 CYS A N 1 ATOM 415 C CA . CYS A 1 58 ? -4.872 6.912 -8.994 1.00 33.38 ? 58 CYS A CA 1 ATOM 416 C C . CYS A 1 58 ? -6.169 7.669 -9.112 1.00 32.26 ? 58 CYS A C 1 ATOM 417 O O . CYS A 1 58 ? -6.156 8.882 -8.969 1.00 33.46 ? 58 CYS A O 1 ATOM 418 C CB . CYS A 1 58 ? -4.271 6.574 -10.346 1.00 34.12 ? 58 CYS A CB 1 ATOM 419 S SG . CYS A 1 58 ? -2.501 6.279 -10.169 1.00 34.62 ? 58 CYS A SG 1 ATOM 420 N N . VAL A 1 59 ? -7.271 6.948 -9.329 1.00 31.44 ? 59 VAL A N 1 ATOM 421 C CA . VAL A 1 59 ? -8.630 7.540 -9.443 1.00 35.06 ? 59 VAL A CA 1 ATOM 422 C C . VAL A 1 59 ? -8.983 8.513 -8.319 1.00 34.07 ? 59 VAL A C 1 ATOM 423 O O . VAL A 1 59 ? -9.569 9.556 -8.572 1.00 36.22 ? 59 VAL A O 1 ATOM 424 C CB . VAL A 1 59 ? -9.760 6.437 -9.469 1.00 36.12 ? 59 VAL A CB 1 ATOM 425 C CG1 . VAL A 1 59 ? -11.151 7.077 -9.542 1.00 37.02 ? 59 VAL A CG1 1 ATOM 426 C CG2 . VAL A 1 59 ? -9.565 5.497 -10.623 1.00 37.15 ? 59 VAL A CG2 1 ATOM 427 N N . TYR A 1 60 ? -8.655 8.142 -7.081 1.00 34.01 ? 60 TYR A N 1 ATOM 428 C CA . TYR A 1 60 ? -9.024 8.921 -5.883 1.00 33.96 ? 60 TYR A CA 1 ATOM 429 C C . TYR A 1 60 ? -8.082 10.111 -5.591 1.00 30.02 ? 60 TYR A C 1 ATOM 430 O O . TYR A 1 60 ? -8.269 10.794 -4.588 1.00 29.12 ? 60 TYR A O 1 ATOM 431 C CB . TYR A 1 60 ? -8.992 8.038 -4.619 1.00 41.19 ? 60 TYR A CB 1 ATOM 432 C CG . TYR A 1 60 ? -9.938 6.853 -4.537 1.00 42.28 ? 60 TYR A CG 1 ATOM 433 C CD1 . TYR A 1 60 ? -9.720 5.866 -3.571 1.00 44.33 ? 60 TYR A CD1 1 ATOM 434 C CD2 . TYR A 1 60 ? -11.042 6.716 -5.402 1.00 42.17 ? 60 TYR A CD2 1 ATOM 435 C CE1 . TYR A 1 60 ? -10.568 4.757 -3.462 1.00 45.72 ? 60 TYR A CE1 1 ATOM 436 C CE2 . TYR A 1 60 ? -11.905 5.606 -5.306 1.00 43.19 ? 60 TYR A CE2 1 ATOM 437 C CZ . TYR A 1 60 ? -11.651 4.630 -4.333 1.00 44.57 ? 60 TYR A CZ 1 ATOM 438 O OH . TYR A 1 60 ? -12.467 3.522 -4.190 1.00 45.45 ? 60 TYR A OH 1 ATOM 439 N N . HIS A 1 61 ? -7.072 10.338 -6.432 1.00 25.01 ? 61 HIS A N 1 ATOM 440 C CA . HIS A 1 61 ? -6.012 11.314 -6.107 1.00 25.64 ? 61 HIS A CA 1 ATOM 441 C C . HIS A 1 61 ? -5.789 12.325 -7.227 1.00 23.54 ? 61 HIS A C 1 ATOM 442 O O . HIS A 1 61 ? -6.215 12.090 -8.338 1.00 19.94 ? 61 HIS A O 1 ATOM 443 C CB . HIS A 1 61 ? -4.709 10.578 -5.731 1.00 23.19 ? 61 HIS A CB 1 ATOM 444 C CG . HIS A 1 61 ? -4.812 9.843 -4.432 1.00 26.18 ? 61 HIS A CG 1 ATOM 445 N ND1 . HIS A 1 61 ? -4.765 8.470 -4.344 1.00 28.18 ? 61 HIS A ND1 1 ATOM 446 C CD2 . HIS A 1 61 ? -5.016 10.293 -3.171 1.00 27.15 ? 61 HIS A CD2 1 ATOM 447 C CE1 . HIS A 1 61 ? -4.911 8.107 -3.083 1.00 29.32 ? 61 HIS A CE1 1 ATOM 448 N NE2 . HIS A 1 61 ? -5.087 9.194 -2.353 1.00 27.64 ? 61 HIS A NE2 1 ATOM 449 N N . LYS A 1 62 ? -5.162 13.462 -6.927 1.00 23.92 ? 62 LYS A N 1 ATOM 450 C CA . LYS A 1 62 ? -4.843 14.407 -7.990 1.00 25.65 ? 62 LYS A CA 1 ATOM 451 C C . LYS A 1 62 ? -3.660 13.863 -8.786 1.00 27.21 ? 62 LYS A C 1 ATOM 452 O O . LYS A 1 62 ? -2.747 13.296 -8.209 1.00 24.32 ? 62 LYS A O 1 ATOM 453 C CB . LYS A 1 62 ? -4.512 15.777 -7.439 1.00 27.66 ? 62 LYS A CB 1 ATOM 454 C CG . LYS A 1 62 ? -5.587 16.409 -6.557 1.00 27.56 ? 62 LYS A CG 1 ATOM 455 C CD . LYS A 1 62 ? -6.919 16.642 -7.225 1.00 30.85 ? 62 LYS A CD 1 ATOM 456 C CE . LYS A 1 62 ? -7.922 17.198 -6.199 1.00 36.81 ? 62 LYS A CE 1 ATOM 457 N NZ . LYS A 1 62 ? -7.595 16.831 -4.720 1.00 37.25 ? 62 LYS A NZ 1 ATOM 458 N N . LEU A 1 63 ? -3.677 14.065 -10.103 1.00 27.23 ? 63 LEU A N 1 ATOM 459 C CA . LEU A 1 63 ? -2.634 13.570 -11.003 1.00 23.65 ? 63 LEU A CA 1 ATOM 460 C C . LEU A 1 63 ? -1.813 14.720 -11.601 1.00 25.77 ? 63 LEU A C 1 ATOM 461 O O . LEU A 1 63 ? -2.367 15.718 -12.076 1.00 26.97 ? 63 LEU A O 1 ATOM 462 C CB . LEU A 1 63 ? -3.258 12.696 -12.126 1.00 21.53 ? 63 LEU A CB 1 ATOM 463 C CG . LEU A 1 63 ? -4.277 11.601 -11.730 1.00 23.09 ? 63 LEU A CG 1 ATOM 464 C CD1 . LEU A 1 63 ? -4.874 10.871 -12.932 1.00 22.43 ? 63 LEU A CD1 1 ATOM 465 C CD2 . LEU A 1 63 ? -3.628 10.595 -10.817 1.00 21.82 ? 63 LEU A CD2 1 ATOM 466 N N . PHE A 1 64 ? -0.490 14.596 -11.573 1.00 24.94 ? 64 PHE A N 1 ATOM 467 C CA . PHE A 1 64 ? 0.362 15.585 -12.278 1.00 25.26 ? 64 PHE A CA 1 ATOM 468 C C . PHE A 1 64 ? 0.364 15.443 -13.805 1.00 26.10 ? 64 PHE A C 1 ATOM 469 O O . PHE A 1 64 ? 0.668 14.375 -14.342 1.00 24.66 ? 64 PHE A O 1 ATOM 470 C CB . PHE A 1 64 ? 1.795 15.592 -11.761 1.00 21.18 ? 64 PHE A CB 1 ATOM 471 C CG . PHE A 1 64 ? 2.651 16.654 -12.419 1.00 23.00 ? 64 PHE A CG 1 ATOM 472 C CD1 . PHE A 1 64 ? 2.531 17.986 -12.055 1.00 21.25 ? 64 PHE A CD1 1 ATOM 473 C CD2 . PHE A 1 64 ? 3.546 16.316 -13.422 1.00 22.44 ? 64 PHE A CD2 1 ATOM 474 C CE1 . PHE A 1 64 ? 3.324 18.992 -12.694 1.00 21.43 ? 64 PHE A CE1 1 ATOM 475 C CE2 . PHE A 1 64 ? 4.345 17.294 -14.045 1.00 22.90 ? 64 PHE A CE2 1 ATOM 476 C CZ . PHE A 1 64 ? 4.242 18.625 -13.667 1.00 19.42 ? 64 PHE A CZ 1 ATOM 477 N N . ASP A 1 65 ? 0.002 16.523 -14.494 1.00 26.71 ? 65 ASP A N 1 ATOM 478 C CA . ASP A 1 65 ? -0.014 16.540 -15.945 1.00 27.84 ? 65 ASP A CA 1 ATOM 479 C C . ASP A 1 65 ? 1.074 17.467 -16.475 1.00 26.11 ? 65 ASP A C 1 ATOM 480 O O . ASP A 1 65 ? 0.989 18.705 -16.345 1.00 23.95 ? 65 ASP A O 1 ATOM 481 C CB . ASP A 1 65 ? -1.392 16.953 -16.488 1.00 29.51 ? 65 ASP A CB 1 ATOM 482 C CG . ASP A 1 65 ? -1.643 16.453 -17.901 1.00 34.50 ? 65 ASP A CG 1 ATOM 483 O OD1 . ASP A 1 65 ? -0.700 16.353 -18.707 1.00 37.70 ? 65 ASP A OD1 1 ATOM 484 O OD2 . ASP A 1 65 ? -2.778 16.140 -18.314 1.00 38.37 ? 65 ASP A OD2 1 ATOM 485 N N . ALA A 1 66 ? 2.081 16.855 -17.095 1.00 20.95 ? 66 ALA A N 1 ATOM 486 C CA . ALA A 1 66 ? 3.223 17.582 -17.628 1.00 21.89 ? 66 ALA A CA 1 ATOM 487 C C . ALA A 1 66 ? 2.765 18.456 -18.803 1.00 26.40 ? 66 ALA A C 1 ATOM 488 O O . ALA A 1 66 ? 3.283 19.550 -19.003 1.00 26.23 ? 66 ALA A O 1 ATOM 489 C CB . ALA A 1 66 ? 4.269 16.609 -18.090 1.00 18.16 ? 66 ALA A CB 1 ATOM 490 N N . SER A 1 67 ? 1.769 17.965 -19.549 1.00 26.84 ? 67 SER A N 1 ATOM 491 C CA . SER A 1 67 ? 1.249 18.661 -20.730 1.00 25.51 ? 67 SER A CA 1 ATOM 492 C C . SER A 1 67 ? 0.476 19.965 -20.416 1.00 25.22 ? 67 SER A C 1 ATOM 493 O O . SER A 1 67 ? 0.058 20.706 -21.325 1.00 28.88 ? 67 SER A O 1 ATOM 494 C CB . SER A 1 67 ? 0.459 17.688 -21.608 1.00 27.87 ? 67 SER A CB 1 ATOM 495 O OG . SER A 1 67 ? -0.837 17.458 -21.070 1.00 35.96 ? 67 SER A OG 1 ATOM 496 N N . ASP A 1 68 ? 0.332 20.273 -19.138 1.00 23.75 ? 68 ASP A N 1 ATOM 497 C CA . ASP A 1 68 ? -0.165 21.574 -18.684 1.00 25.34 ? 68 ASP A CA 1 ATOM 498 C C . ASP A 1 68 ? 0.865 22.510 -18.080 1.00 25.46 ? 68 ASP A C 1 ATOM 499 O O . ASP A 1 68 ? 0.523 23.651 -17.765 1.00 26.24 ? 68 ASP A O 1 ATOM 500 C CB . ASP A 1 68 ? -1.305 21.417 -17.707 1.00 25.15 ? 68 ASP A CB 1 ATOM 501 C CG . ASP A 1 68 ? -2.500 20.751 -18.337 1.00 29.73 ? 68 ASP A CG 1 ATOM 502 O OD1 . ASP A 1 68 ? -2.660 20.886 -19.571 1.00 31.70 ? 68 ASP A OD1 1 ATOM 503 O OD2 . ASP A 1 68 ? -3.316 20.074 -17.684 1.00 30.18 ? 68 ASP A OD2 1 ATOM 504 N N . SER A 1 69 ? 2.106 22.047 -17.935 1.00 27.03 ? 69 SER A N 1 ATOM 505 C CA . SER A 1 69 ? 3.150 22.854 -17.305 1.00 24.78 ? 69 SER A CA 1 ATOM 506 C C . SER A 1 69 ? 4.110 23.362 -18.341 1.00 24.32 ? 69 SER A C 1 ATOM 507 O O . SER A 1 69 ? 4.647 22.585 -19.120 1.00 22.96 ? 69 SER A O 1 ATOM 508 C CB . SER A 1 69 ? 3.943 22.051 -16.291 1.00 26.23 ? 69 SER A CB 1 ATOM 509 O OG . SER A 1 69 ? 4.938 22.876 -15.681 1.00 21.59 ? 69 SER A OG 1 ATOM 510 N N . SER A 1 70 ? 4.354 24.666 -18.323 1.00 25.86 ? 70 SER A N 1 ATOM 511 C CA . SER A 1 70 ? 5.272 25.276 -19.296 1.00 26.52 ? 70 SER A CA 1 ATOM 512 C C . SER A 1 70 ? 6.725 25.157 -18.845 1.00 27.20 ? 70 SER A C 1 ATOM 513 O O . SER A 1 70 ? 7.648 25.291 -19.651 1.00 30.00 ? 70 SER A O 1 ATOM 514 C CB . SER A 1 70 ? 4.901 26.747 -19.544 1.00 25.77 ? 70 SER A CB 1 ATOM 515 O OG . SER A 1 70 ? 5.247 27.549 -18.449 1.00 24.31 ? 70 SER A OG 1 ATOM 516 N N . SER A 1 71 ? 6.939 24.856 -17.573 1.00 25.58 ? 71 SER A N 1 ATOM 517 C CA . SER A 1 71 ? 8.300 24.817 -17.060 1.00 23.62 ? 71 SER A CA 1 ATOM 518 C C . SER A 1 71 ? 8.872 23.419 -16.919 1.00 25.34 ? 71 SER A C 1 ATOM 519 O O . SER A 1 71 ? 9.993 23.267 -16.442 1.00 24.20 ? 71 SER A O 1 ATOM 520 C CB . SER A 1 71 ? 8.428 25.627 -15.749 1.00 25.52 ? 71 SER A CB 1 ATOM 521 O OG . SER A 1 71 ? 7.361 25.343 -14.857 1.00 26.59 ? 71 SER A OG 1 ATOM 522 N N . TYR A 1 72 ? 8.101 22.422 -17.368 1.00 25.61 ? 72 TYR A N 1 ATOM 523 C CA . TYR A 1 72 ? 8.416 21.001 -17.267 1.00 29.88 ? 72 TYR A CA 1 ATOM 524 C C . TYR A 1 72 ? 9.586 20.614 -18.144 1.00 30.81 ? 72 TYR A C 1 ATOM 525 O O . TYR A 1 72 ? 9.725 21.127 -19.242 1.00 34.06 ? 72 TYR A O 1 ATOM 526 C CB . TYR A 1 72 ? 7.183 20.187 -17.689 1.00 29.73 ? 72 TYR A CB 1 ATOM 527 C CG . TYR A 1 72 ? 7.436 18.756 -18.141 1.00 29.56 ? 72 TYR A CG 1 ATOM 528 C CD1 . TYR A 1 72 ? 7.475 18.420 -19.496 1.00 32.07 ? 72 TYR A CD1 1 ATOM 529 C CD2 . TYR A 1 72 ? 7.583 17.722 -17.205 1.00 30.67 ? 72 TYR A CD2 1 ATOM 530 C CE1 . TYR A 1 72 ? 7.699 17.077 -19.925 1.00 32.18 ? 72 TYR A CE1 1 ATOM 531 C CE2 . TYR A 1 72 ? 7.784 16.394 -17.614 1.00 30.20 ? 72 TYR A CE2 1 ATOM 532 C CZ . TYR A 1 72 ? 7.848 16.080 -18.974 1.00 31.13 ? 72 TYR A CZ 1 ATOM 533 O OH . TYR A 1 72 ? 8.032 14.760 -19.376 1.00 30.80 ? 72 TYR A OH 1 ATOM 534 N N . LYS A 1 73 ? 10.426 19.704 -17.671 1.00 29.93 ? 73 LYS A N 1 ATOM 535 C CA . LYS A 1 73 ? 11.550 19.231 -18.487 1.00 29.20 ? 73 LYS A CA 1 ATOM 536 C C . LYS A 1 73 ? 11.586 17.705 -18.428 1.00 29.41 ? 73 LYS A C 1 ATOM 537 O O . LYS A 1 73 ? 11.746 17.111 -17.342 1.00 28.48 ? 73 LYS A O 1 ATOM 538 C CB . LYS A 1 73 ? 12.885 19.847 -18.038 1.00 31.90 ? 73 LYS A CB 1 ATOM 539 C CG . LYS A 1 73 ? 12.942 21.407 -18.004 1.00 36.17 ? 73 LYS A CG 1 ATOM 540 C CD . LYS A 1 73 ? 13.768 22.022 -19.146 1.00 37.01 ? 73 LYS A CD 1 ATOM 541 C CE . LYS A 1 73 ? 15.256 22.196 -18.759 1.00 38.82 ? 73 LYS A CE 1 ATOM 542 N NZ . LYS A 1 73 ? 16.281 22.252 -19.898 1.00 38.63 ? 73 LYS A NZ 1 ATOM 543 N N A HIS A 1 74 ? 11.408 17.080 -19.593 0.50 27.97 ? 74 HIS A N 1 ATOM 544 N N B HIS A 1 74 ? 11.419 17.080 -19.588 0.50 29.17 ? 74 HIS A N 1 ATOM 545 C CA A HIS A 1 74 ? 11.386 15.626 -19.747 0.50 27.97 ? 74 HIS A CA 1 ATOM 546 C CA B HIS A 1 74 ? 11.371 15.635 -19.678 0.50 30.06 ? 74 HIS A CA 1 ATOM 547 C C A HIS A 1 74 ? 12.686 15.013 -19.226 0.50 29.80 ? 74 HIS A C 1 ATOM 548 C C B HIS A 1 74 ? 12.678 15.038 -19.163 0.50 30.95 ? 74 HIS A C 1 ATOM 549 O O A HIS A 1 74 ? 13.759 15.605 -19.375 0.50 27.29 ? 74 HIS A O 1 ATOM 550 O O B HIS A 1 74 ? 13.737 15.666 -19.246 0.50 28.82 ? 74 HIS A O 1 ATOM 551 C CB A HIS A 1 74 ? 11.200 15.262 -21.236 0.50 27.56 ? 74 HIS A CB 1 ATOM 552 C CB B HIS A 1 74 ? 11.086 15.187 -21.124 0.50 31.67 ? 74 HIS A CB 1 ATOM 553 C CG A HIS A 1 74 ? 11.118 13.786 -21.505 0.50 25.82 ? 74 HIS A CG 1 ATOM 554 C CG B HIS A 1 74 ? 12.314 14.943 -21.953 0.50 32.09 ? 74 HIS A CG 1 ATOM 555 N ND1 A HIS A 1 74 ? 12.153 13.066 -22.068 0.50 24.99 ? 74 HIS A ND1 1 ATOM 556 N ND1 B HIS A 1 74 ? 13.007 15.955 -22.584 0.50 32.80 ? 74 HIS A ND1 1 ATOM 557 C CD2 A HIS A 1 74 ? 10.121 12.896 -21.292 0.50 24.80 ? 74 HIS A CD2 1 ATOM 558 C CD2 B HIS A 1 74 ? 12.955 13.793 -22.279 0.50 32.50 ? 74 HIS A CD2 1 ATOM 559 C CE1 A HIS A 1 74 ? 11.802 11.799 -22.179 0.50 22.41 ? 74 HIS A CE1 1 ATOM 560 C CE1 B HIS A 1 74 ? 14.026 15.441 -23.250 0.50 31.50 ? 74 HIS A CE1 1 ATOM 561 N NE2 A HIS A 1 74 ? 10.576 11.666 -21.711 0.50 23.13 ? 74 HIS A NE2 1 ATOM 562 N NE2 B HIS A 1 74 ? 14.020 14.133 -23.077 0.50 30.88 ? 74 HIS A NE2 1 ATOM 563 N N . ASN A 1 75 ? 12.581 13.833 -18.616 1.00 29.69 ? 75 ASN A N 1 ATOM 564 C CA . ASN A 1 75 ? 13.743 13.008 -18.371 1.00 29.51 ? 75 ASN A CA 1 ATOM 565 C C . ASN A 1 75 ? 13.372 11.594 -18.816 1.00 30.61 ? 75 ASN A C 1 ATOM 566 O O . ASN A 1 75 ? 13.882 11.130 -19.840 1.00 30.89 ? 75 ASN A O 1 ATOM 567 C CB . ASN A 1 75 ? 14.182 13.074 -16.928 1.00 33.49 ? 75 ASN A CB 1 ATOM 568 C CG . ASN A 1 75 ? 15.297 12.118 -16.630 1.00 36.61 ? 75 ASN A CG 1 ATOM 569 O OD1 . ASN A 1 75 ? 15.056 10.928 -16.402 1.00 32.09 ? 75 ASN A OD1 1 ATOM 570 N ND2 . ASN A 1 75 ? 16.540 12.630 -16.655 1.00 42.79 ? 75 ASN A ND2 1 ATOM 571 N N . GLY A 1 76 ? 12.461 10.930 -18.088 1.00 28.36 ? 76 GLY A N 1 ATOM 572 C CA . GLY A 1 76 ? 11.862 9.663 -18.553 1.00 28.17 ? 76 GLY A CA 1 ATOM 573 C C . GLY A 1 76 ? 12.469 8.376 -18.007 1.00 31.15 ? 76 GLY A C 1 ATOM 574 O O . GLY A 1 76 ? 12.006 7.276 -18.325 1.00 29.81 ? 76 GLY A O 1 ATOM 575 N N . THR A 1 77 ? 13.503 8.517 -17.182 1.00 28.49 ? 77 THR A N 1 ATOM 576 C CA . THR A 1 77 ? 14.153 7.390 -16.534 1.00 31.77 ? 77 THR A CA 1 ATOM 577 C C . THR A 1 77 ? 13.183 6.701 -15.581 1.00 33.21 ? 77 THR A C 1 ATOM 578 O O . THR A 1 77 ? 12.538 7.370 -14.750 1.00 31.81 ? 77 THR A O 1 ATOM 579 C CB . THR A 1 77 ? 15.381 7.871 -15.792 1.00 29.87 ? 77 THR A CB 1 ATOM 580 O OG1 . THR A 1 77 ? 16.359 8.268 -16.755 1.00 34.09 ? 77 THR A OG1 1 ATOM 581 C CG2 . THR A 1 77 ? 16.063 6.720 -15.041 1.00 31.67 ? 77 THR A CG2 1 ATOM 582 N N . GLU A 1 78 ? 13.077 5.383 -15.720 1.00 33.18 ? 78 GLU A N 1 ATOM 583 C CA . GLU A 1 78 ? 12.182 4.578 -14.886 1.00 37.62 ? 78 GLU A CA 1 ATOM 584 C C . GLU A 1 78 ? 12.658 4.445 -13.438 1.00 35.81 ? 78 GLU A C 1 ATOM 585 O O . GLU A 1 78 ? 13.855 4.259 -13.180 1.00 33.44 ? 78 GLU A O 1 ATOM 586 C CB . GLU A 1 78 ? 11.993 3.188 -15.489 1.00 40.10 ? 78 GLU A CB 1 ATOM 587 C CG . GLU A 1 78 ? 11.104 3.169 -16.723 1.00 45.24 ? 78 GLU A CG 1 ATOM 588 C CD . GLU A 1 78 ? 11.070 1.815 -17.430 1.00 46.17 ? 78 GLU A CD 1 ATOM 589 O OE1 . GLU A 1 78 ? 11.591 0.798 -16.876 1.00 48.66 ? 78 GLU A OE1 1 ATOM 590 O OE2 . GLU A 1 78 ? 10.512 1.773 -18.557 1.00 50.21 ? 78 GLU A OE2 1 ATOM 591 N N . LEU A 1 79 ? 11.699 4.511 -12.510 1.00 32.29 ? 79 LEU A N 1 ATOM 592 C CA . LEU A 1 79 ? 11.956 4.483 -11.063 1.00 33.07 ? 79 LEU A CA 1 ATOM 593 C C . LEU A 1 79 ? 11.058 3.443 -10.434 1.00 32.47 ? 79 LEU A C 1 ATOM 594 O O . LEU A 1 79 ? 9.850 3.423 -10.710 1.00 30.83 ? 79 LEU A O 1 ATOM 595 C CB . LEU A 1 79 ? 11.554 5.817 -10.432 1.00 33.35 ? 79 LEU A CB 1 ATOM 596 C CG . LEU A 1 79 ? 12.269 7.066 -10.895 1.00 37.39 ? 79 LEU A CG 1 ATOM 597 C CD1 . LEU A 1 79 ? 11.224 8.167 -10.960 1.00 37.93 ? 79 LEU A CD1 1 ATOM 598 C CD2 . LEU A 1 79 ? 13.359 7.389 -9.900 1.00 36.87 ? 79 LEU A CD2 1 ATOM 599 N N . THR A 1 80 ? 11.626 2.631 -9.557 1.00 31.93 ? 80 THR A N 1 ATOM 600 C CA . THR A 1 80 ? 10.863 1.597 -8.873 1.00 32.52 ? 80 THR A CA 1 ATOM 601 C C . THR A 1 80 ? 11.094 1.589 -7.375 1.00 31.13 ? 80 THR A C 1 ATOM 602 O O . THR A 1 80 ? 12.232 1.696 -6.911 1.00 27.81 ? 80 THR A O 1 ATOM 603 C CB . THR A 1 80 ? 11.195 0.214 -9.480 1.00 35.77 ? 80 THR A CB 1 ATOM 604 O OG1 . THR A 1 80 ? 10.528 0.091 -10.737 1.00 36.13 ? 80 THR A OG1 1 ATOM 605 C CG2 . THR A 1 80 ? 10.586 -0.926 -8.659 1.00 34.91 ? 80 THR A CG2 1 ATOM 606 N N . LEU A 1 81 ? 9.997 1.468 -6.628 1.00 33.20 ? 81 LEU A N 1 ATOM 607 C CA . LEU A 1 81 ? 10.037 1.205 -5.193 1.00 34.18 ? 81 LEU A CA 1 ATOM 608 C C . LEU A 1 81 ? 9.332 -0.135 -4.897 1.00 35.40 ? 81 LEU A C 1 ATOM 609 O O . LEU A 1 81 ? 8.168 -0.327 -5.231 1.00 34.57 ? 81 LEU A O 1 ATOM 610 C CB . LEU A 1 81 ? 9.342 2.336 -4.437 1.00 36.54 ? 81 LEU A CB 1 ATOM 611 C CG . LEU A 1 81 ? 9.661 2.760 -2.998 1.00 37.46 ? 81 LEU A CG 1 ATOM 612 C CD1 . LEU A 1 81 ? 8.349 2.903 -2.273 1.00 36.93 ? 81 LEU A CD1 1 ATOM 613 C CD2 . LEU A 1 81 ? 10.598 1.822 -2.228 1.00 37.13 ? 81 LEU A CD2 1 ATOM 614 N N . ARG A 1 82 ? 10.027 -1.061 -4.254 1.00 37.74 ? 82 ARG A N 1 ATOM 615 C CA . ARG A 1 82 ? 9.402 -2.334 -3.901 1.00 40.03 ? 82 ARG A CA 1 ATOM 616 C C . ARG A 1 82 ? 8.782 -2.261 -2.496 1.00 40.79 ? 82 ARG A C 1 ATOM 617 O O . ARG A 1 82 ? 9.413 -2.613 -1.496 1.00 41.31 ? 82 ARG A O 1 ATOM 618 C CB . ARG A 1 82 ? 10.406 -3.473 -4.020 1.00 43.82 ? 82 ARG A CB 1 ATOM 619 C CG . ARG A 1 82 ? 11.161 -3.494 -5.346 1.00 49.36 ? 82 ARG A CG 1 ATOM 620 C CD . ARG A 1 82 ? 12.675 -3.687 -5.193 1.00 56.55 ? 82 ARG A CD 1 ATOM 621 N NE . ARG A 1 82 ? 13.331 -4.077 -6.448 1.00 63.23 ? 82 ARG A NE 1 ATOM 622 C CZ . ARG A 1 82 ? 13.421 -5.337 -6.907 1.00 66.36 ? 82 ARG A CZ 1 ATOM 623 N NH1 . ARG A 1 82 ? 12.887 -6.348 -6.221 1.00 67.81 ? 82 ARG A NH1 1 ATOM 624 N NH2 . ARG A 1 82 ? 14.042 -5.587 -8.060 1.00 65.87 ? 82 ARG A NH2 1 ATOM 625 N N . TYR A 1 83 ? 7.543 -1.788 -2.434 1.00 38.25 ? 83 TYR A N 1 ATOM 626 C CA . TYR A 1 83 ? 6.815 -1.641 -1.176 1.00 39.43 ? 83 TYR A CA 1 ATOM 627 C C . TYR A 1 83 ? 6.281 -3.031 -0.711 1.00 39.32 ? 83 TYR A C 1 ATOM 628 O O . TYR A 1 83 ? 6.463 -4.017 -1.430 1.00 40.53 ? 83 TYR A O 1 ATOM 629 C CB . TYR A 1 83 ? 5.704 -0.588 -1.385 1.00 38.07 ? 83 TYR A CB 1 ATOM 630 C CG . TYR A 1 83 ? 4.921 -0.242 -0.142 1.00 36.26 ? 83 TYR A CG 1 ATOM 631 C CD1 . TYR A 1 83 ? 3.690 -0.846 0.117 1.00 34.08 ? 83 TYR A CD1 1 ATOM 632 C CD2 . TYR A 1 83 ? 5.402 0.691 0.764 1.00 36.42 ? 83 TYR A CD2 1 ATOM 633 C CE1 . TYR A 1 83 ? 2.973 -0.551 1.255 1.00 36.71 ? 83 TYR A CE1 1 ATOM 634 C CE2 . TYR A 1 83 ? 4.681 1.011 1.919 1.00 36.60 ? 83 TYR A CE2 1 ATOM 635 C CZ . TYR A 1 83 ? 3.466 0.390 2.150 1.00 38.61 ? 83 TYR A CZ 1 ATOM 636 O OH . TYR A 1 83 ? 2.755 0.705 3.284 1.00 40.48 ? 83 TYR A OH 1 ATOM 637 N N . SER A 1 84 ? 5.645 -3.111 0.467 1.00 39.71 ? 84 SER A N 1 ATOM 638 C CA . SER A 1 84 ? 5.150 -4.383 1.060 1.00 40.40 ? 84 SER A CA 1 ATOM 639 C C . SER A 1 84 ? 4.101 -5.137 0.237 1.00 40.09 ? 84 SER A C 1 ATOM 640 O O . SER A 1 84 ? 4.214 -6.354 0.011 1.00 38.17 ? 84 SER A O 1 ATOM 641 C CB . SER A 1 84 ? 4.529 -4.126 2.432 1.00 41.37 ? 84 SER A CB 1 ATOM 642 O OG . SER A 1 84 ? 5.215 -3.112 3.121 1.00 43.36 ? 84 SER A OG 1 ATOM 643 N N . THR A 1 85 ? 3.066 -4.393 -0.164 1.00 38.42 ? 85 THR A N 1 ATOM 644 C CA . THR A 1 85 ? 1.951 -4.884 -0.961 1.00 35.86 ? 85 THR A CA 1 ATOM 645 C C . THR A 1 85 ? 2.205 -4.942 -2.476 1.00 36.06 ? 85 THR A C 1 ATOM 646 O O . THR A 1 85 ? 1.325 -5.374 -3.240 1.00 40.11 ? 85 THR A O 1 ATOM 647 C CB . THR A 1 85 ? 0.726 -3.995 -0.697 1.00 35.47 ? 85 THR A CB 1 ATOM 648 O OG1 . THR A 1 85 ? 1.096 -2.613 -0.849 1.00 31.28 ? 85 THR A OG1 1 ATOM 649 C CG2 . THR A 1 85 ? 0.306 -4.099 0.761 1.00 35.74 ? 85 THR A CG2 1 ATOM 650 N N . GLY A 1 86 ? 3.374 -4.497 -2.927 1.00 32.58 ? 86 GLY A N 1 ATOM 651 C CA . GLY A 1 86 ? 3.680 -4.513 -4.348 1.00 33.83 ? 86 GLY A CA 1 ATOM 652 C C . GLY A 1 86 ? 4.545 -3.333 -4.750 1.00 35.41 ? 86 GLY A C 1 ATOM 653 O O . GLY A 1 86 ? 4.962 -2.549 -3.904 1.00 32.27 ? 86 GLY A O 1 ATOM 654 N N . THR A 1 87 ? 4.781 -3.213 -6.055 1.00 34.72 ? 87 THR A N 1 ATOM 655 C CA . THR A 1 87 ? 5.731 -2.260 -6.637 1.00 33.80 ? 87 THR A CA 1 ATOM 656 C C . THR A 1 87 ? 5.047 -0.942 -6.948 1.00 31.11 ? 87 THR A C 1 ATOM 657 O O . THR A 1 87 ? 3.920 -0.921 -7.472 1.00 29.01 ? 87 THR A O 1 ATOM 658 C CB . THR A 1 87 ? 6.324 -2.861 -7.927 1.00 35.56 ? 87 THR A CB 1 ATOM 659 O OG1 . THR A 1 87 ? 7.024 -4.071 -7.592 1.00 40.15 ? 87 THR A OG1 1 ATOM 660 C CG2 . THR A 1 87 ? 7.420 -1.982 -8.499 1.00 37.90 ? 87 THR A CG2 1 ATOM 661 N N . VAL A 1 88 ? 5.719 0.149 -6.592 1.00 30.21 ? 88 VAL A N 1 ATOM 662 C CA . VAL A 1 88 ? 5.303 1.485 -7.024 1.00 28.02 ? 88 VAL A CA 1 ATOM 663 C C . VAL A 1 88 ? 6.326 1.870 -8.061 1.00 29.10 ? 88 VAL A C 1 ATOM 664 O O . VAL A 1 88 ? 7.528 1.870 -7.779 1.00 29.30 ? 88 VAL A O 1 ATOM 665 C CB . VAL A 1 88 ? 5.292 2.529 -5.876 1.00 27.05 ? 88 VAL A CB 1 ATOM 666 C CG1 . VAL A 1 88 ? 4.810 3.920 -6.387 1.00 27.16 ? 88 VAL A CG1 1 ATOM 667 C CG2 . VAL A 1 88 ? 4.440 2.057 -4.679 1.00 28.14 ? 88 VAL A CG2 1 ATOM 668 N N . SER A 1 89 ? 5.891 2.175 -9.277 1.00 26.31 ? 89 SER A N 1 ATOM 669 C CA . SER A 1 89 ? 6.883 2.580 -10.258 1.00 28.04 ? 89 SER A CA 1 ATOM 670 C C . SER A 1 89 ? 6.380 3.724 -11.077 1.00 25.02 ? 89 SER A C 1 ATOM 671 O O . SER A 1 89 ? 5.187 3.952 -11.165 1.00 26.37 ? 89 SER A O 1 ATOM 672 C CB . SER A 1 89 ? 7.339 1.402 -11.144 1.00 29.97 ? 89 SER A CB 1 ATOM 673 O OG . SER A 1 89 ? 6.249 0.831 -11.816 1.00 35.65 ? 89 SER A OG 1 ATOM 674 N N . GLY A 1 90 ? 7.308 4.471 -11.650 1.00 25.49 ? 90 GLY A N 1 ATOM 675 C CA . GLY A 1 90 ? 6.960 5.554 -12.533 1.00 27.15 ? 90 GLY A CA 1 ATOM 676 C C . GLY A 1 90 ? 8.190 6.015 -13.297 1.00 28.50 ? 90 GLY A C 1 ATOM 677 O O . GLY A 1 90 ? 9.044 5.195 -13.677 1.00 28.43 ? 90 GLY A O 1 ATOM 678 N N . PHE A 1 91 ? 8.279 7.318 -13.534 1.00 27.12 ? 91 PHE A N 1 ATOM 679 C CA . PHE A 1 91 ? 9.406 7.884 -14.303 1.00 24.54 ? 91 PHE A CA 1 ATOM 680 C C . PHE A 1 91 ? 9.814 9.295 -13.834 1.00 27.81 ? 91 PHE A C 1 ATOM 681 O O . PHE A 1 91 ? 9.040 10.001 -13.170 1.00 25.25 ? 91 PHE A O 1 ATOM 682 C CB . PHE A 1 91 ? 9.083 7.870 -15.800 1.00 27.20 ? 91 PHE A CB 1 ATOM 683 C CG . PHE A 1 91 ? 7.864 8.680 -16.163 1.00 28.18 ? 91 PHE A CG 1 ATOM 684 C CD1 . PHE A 1 91 ? 7.984 10.045 -16.454 1.00 28.35 ? 91 PHE A CD1 1 ATOM 685 C CD2 . PHE A 1 91 ? 6.595 8.078 -16.202 1.00 28.66 ? 91 PHE A CD2 1 ATOM 686 C CE1 . PHE A 1 91 ? 6.867 10.805 -16.764 1.00 26.78 ? 91 PHE A CE1 1 ATOM 687 C CE2 . PHE A 1 91 ? 5.449 8.833 -16.520 1.00 29.36 ? 91 PHE A CE2 1 ATOM 688 C CZ . PHE A 1 91 ? 5.593 10.202 -16.805 1.00 28.17 ? 91 PHE A CZ 1 ATOM 689 N N . LEU A 1 92 ? 11.026 9.713 -14.183 1.00 24.28 ? 92 LEU A N 1 ATOM 690 C CA . LEU A 1 92 ? 11.548 10.957 -13.631 1.00 26.24 ? 92 LEU A CA 1 ATOM 691 C C . LEU A 1 92 ? 11.097 12.108 -14.498 1.00 25.36 ? 92 LEU A C 1 ATOM 692 O O . LEU A 1 92 ? 10.998 11.973 -15.706 1.00 28.15 ? 92 LEU A O 1 ATOM 693 C CB . LEU A 1 92 ? 13.071 10.943 -13.543 1.00 28.28 ? 92 LEU A CB 1 ATOM 694 C CG . LEU A 1 92 ? 13.763 10.268 -12.346 1.00 31.24 ? 92 LEU A CG 1 ATOM 695 C CD1 . LEU A 1 92 ? 15.280 10.359 -12.492 1.00 31.63 ? 92 LEU A CD1 1 ATOM 696 C CD2 . LEU A 1 92 ? 13.311 10.879 -11.014 1.00 26.79 ? 92 LEU A CD2 1 ATOM 697 N N . SER A 1 93 ? 10.802 13.226 -13.855 1.00 27.76 ? 93 SER A N 1 ATOM 698 C CA . SER A 1 93 ? 10.462 14.475 -14.528 1.00 27.47 ? 93 SER A CA 1 ATOM 699 C C . SER A 1 93 ? 11.089 15.595 -13.706 1.00 25.40 ? 93 SER A C 1 ATOM 700 O O . SER A 1 93 ? 11.385 15.401 -12.540 1.00 27.28 ? 93 SER A O 1 ATOM 701 C CB . SER A 1 93 ? 8.958 14.639 -14.552 1.00 24.91 ? 93 SER A CB 1 ATOM 702 O OG . SER A 1 93 ? 8.393 13.638 -15.358 1.00 27.12 ? 93 SER A OG 1 ATOM 703 N N . GLN A 1 94 ? 11.333 16.746 -14.318 1.00 24.97 ? 94 GLN A N 1 ATOM 704 C CA . GLN A 1 94 ? 11.826 17.908 -13.575 1.00 23.69 ? 94 GLN A CA 1 ATOM 705 C C . GLN A 1 94 ? 10.811 19.034 -13.695 1.00 24.18 ? 94 GLN A C 1 ATOM 706 O O . GLN A 1 94 ? 10.280 19.250 -14.753 1.00 25.45 ? 94 GLN A O 1 ATOM 707 C CB . GLN A 1 94 ? 13.170 18.368 -14.127 1.00 24.13 ? 94 GLN A CB 1 ATOM 708 C CG . GLN A 1 94 ? 13.731 19.601 -13.413 1.00 28.94 ? 94 GLN A CG 1 ATOM 709 C CD . GLN A 1 94 ? 14.927 20.182 -14.134 1.00 35.14 ? 94 GLN A CD 1 ATOM 710 O OE1 . GLN A 1 94 ? 16.059 19.717 -13.956 1.00 35.54 ? 94 GLN A OE1 1 ATOM 711 N NE2 . GLN A 1 94 ? 14.681 21.185 -14.975 1.00 36.51 ? 94 GLN A NE2 1 ATOM 712 N N . ASP A 1 95 ? 10.521 19.747 -12.611 1.00 25.71 ? 95 ASP A N 1 ATOM 713 C CA . ASP A 1 95 ? 9.693 20.949 -12.748 1.00 24.72 ? 95 ASP A CA 1 ATOM 714 C C . ASP A 1 95 ? 9.967 21.793 -11.553 1.00 25.44 ? 95 ASP A C 1 ATOM 715 O O . ASP A 1 95 ? 10.701 21.377 -10.666 1.00 26.80 ? 95 ASP A O 1 ATOM 716 C CB . ASP A 1 95 ? 8.209 20.612 -12.831 1.00 23.93 ? 95 ASP A CB 1 ATOM 717 C CG . ASP A 1 95 ? 7.428 21.604 -13.687 1.00 24.49 ? 95 ASP A CG 1 ATOM 718 O OD1 . ASP A 1 95 ? 7.701 22.831 -13.629 1.00 23.04 ? 95 ASP A OD1 1 ATOM 719 O OD2 . ASP A 1 95 ? 6.503 21.247 -14.433 1.00 22.86 ? 95 ASP A OD2 1 ATOM 720 N N . ILE A 1 96 ? 9.355 22.964 -11.521 1.00 25.62 ? 96 ILE A N 1 ATOM 721 C CA . ILE A 1 96 ? 9.475 23.882 -10.399 1.00 28.45 ? 96 ILE A CA 1 ATOM 722 C C . ILE A 1 96 ? 8.464 23.541 -9.298 1.00 27.65 ? 96 ILE A C 1 ATOM 723 O O . ILE A 1 96 ? 7.247 23.486 -9.548 1.00 28.51 ? 96 ILE A O 1 ATOM 724 C CB . ILE A 1 96 ? 9.256 25.335 -10.882 1.00 31.92 ? 96 ILE A CB 1 ATOM 725 C CG1 . ILE A 1 96 ? 10.306 25.710 -11.926 1.00 33.07 ? 96 ILE A CG1 1 ATOM 726 C CG2 . ILE A 1 96 ? 9.365 26.308 -9.724 1.00 33.40 ? 96 ILE A CG2 1 ATOM 727 C CD1 . ILE A 1 96 ? 10.196 27.143 -12.389 1.00 37.07 ? 96 ILE A CD1 1 ATOM 728 N N . ILE A 1 97 ? 8.978 23.344 -8.089 1.00 25.07 ? 97 ILE A N 1 ATOM 729 C CA . ILE A 1 97 ? 8.154 23.000 -6.920 1.00 27.98 ? 97 ILE A CA 1 ATOM 730 C C . ILE A 1 97 ? 8.207 24.075 -5.826 1.00 27.58 ? 97 ILE A C 1 ATOM 731 O O . ILE A 1 97 ? 9.293 24.520 -5.425 1.00 26.75 ? 97 ILE A O 1 ATOM 732 C CB . ILE A 1 97 ? 8.509 21.575 -6.351 1.00 27.00 ? 97 ILE A CB 1 ATOM 733 C CG1 . ILE A 1 97 ? 8.556 20.527 -7.473 1.00 26.32 ? 97 ILE A CG1 1 ATOM 734 C CG2 . ILE A 1 97 ? 7.492 21.177 -5.251 1.00 27.63 ? 97 ILE A CG2 1 ATOM 735 C CD1 . ILE A 1 97 ? 8.855 19.110 -7.035 1.00 27.66 ? 97 ILE A CD1 1 ATOM 736 N N . THR A 1 98 ? 7.022 24.498 -5.375 1.00 27.69 ? 98 THR A N 1 ATOM 737 C CA . THR A 1 98 ? 6.886 25.478 -4.294 1.00 30.73 ? 98 THR A CA 1 ATOM 738 C C . THR A 1 98 ? 6.488 24.808 -2.988 1.00 29.92 ? 98 THR A C 1 ATOM 739 O O . THR A 1 98 ? 5.562 23.995 -2.968 1.00 28.02 ? 98 THR A O 1 ATOM 740 C CB . THR A 1 98 ? 5.822 26.556 -4.642 1.00 32.03 ? 98 THR A CB 1 ATOM 741 O OG1 . THR A 1 98 ? 4.685 25.922 -5.255 1.00 35.59 ? 98 THR A OG1 1 ATOM 742 C CG2 . THR A 1 98 ? 6.343 27.476 -5.723 1.00 31.46 ? 98 THR A CG2 1 ATOM 743 N N . VAL A 1 99 ? 7.168 25.192 -1.904 1.00 28.99 ? 99 VAL A N 1 ATOM 744 C CA . VAL A 1 99 ? 6.929 24.663 -0.551 1.00 30.16 ? 99 VAL A CA 1 ATOM 745 C C . VAL A 1 99 ? 6.993 25.868 0.390 1.00 33.29 ? 99 VAL A C 1 ATOM 746 O O . VAL A 1 99 ? 8.069 26.438 0.588 1.00 33.38 ? 99 VAL A O 1 ATOM 747 C CB . VAL A 1 99 ? 8.045 23.667 -0.113 1.00 28.30 ? 99 VAL A CB 1 ATOM 748 C CG1 . VAL A 1 99 ? 7.670 22.933 1.201 1.00 29.05 ? 99 VAL A CG1 1 ATOM 749 C CG2 . VAL A 1 99 ? 8.360 22.661 -1.202 1.00 26.55 ? 99 VAL A CG2 1 ATOM 750 N N . GLY A 1 100 ? 5.846 26.262 0.942 1.00 33.86 ? 100 GLY A N 1 ATOM 751 C CA . GLY A 1 100 ? 5.753 27.457 1.788 1.00 36.70 ? 100 GLY A CA 1 ATOM 752 C C . GLY A 1 100 ? 6.604 28.645 1.348 1.00 38.89 ? 100 GLY A C 1 ATOM 753 O O . GLY A 1 100 ? 7.409 29.165 2.123 1.00 41.57 ? 100 GLY A O 1 ATOM 754 N N . GLY A 1 101 ? 6.464 29.100 0.113 1.00 39.89 ? 101 GLY A N 1 ATOM 755 C CA . GLY A 1 101 ? 7.206 30.329 -0.244 1.00 37.92 ? 101 GLY A CA 1 ATOM 756 C C . GLY A 1 101 ? 8.672 30.155 -0.632 1.00 38.56 ? 101 GLY A C 1 ATOM 757 O O . GLY A 1 101 ? 9.366 31.132 -0.922 1.00 39.37 ? 101 GLY A O 1 ATOM 758 N N . ILE A 1 102 ? 9.157 28.918 -0.642 1.00 37.03 ? 102 ILE A N 1 ATOM 759 C CA . ILE A 1 102 ? 10.426 28.610 -1.278 1.00 37.86 ? 102 ILE A CA 1 ATOM 760 C C . ILE A 1 102 ? 10.112 27.949 -2.617 1.00 37.57 ? 102 ILE A C 1 ATOM 761 O O . ILE A 1 102 ? 9.202 27.133 -2.701 1.00 35.66 ? 102 ILE A O 1 ATOM 762 C CB . ILE A 1 102 ? 11.305 27.681 -0.367 1.00 39.14 ? 102 ILE A CB 1 ATOM 763 C CG1 . ILE A 1 102 ? 11.660 28.394 0.938 1.00 40.14 ? 102 ILE A CG1 1 ATOM 764 C CG2 . ILE A 1 102 ? 12.587 27.212 -1.095 1.00 39.87 ? 102 ILE A CG2 1 ATOM 765 C CD1 . ILE A 1 102 ? 12.392 27.529 1.937 1.00 38.39 ? 102 ILE A CD1 1 ATOM 766 N N . THR A 1 103 ? 10.868 28.301 -3.657 1.00 37.00 ? 103 THR A N 1 ATOM 767 C CA . THR A 1 103 ? 10.689 27.734 -4.994 1.00 37.92 ? 103 THR A CA 1 ATOM 768 C C . THR A 1 103 ? 11.979 27.077 -5.452 1.00 38.23 ? 103 THR A C 1 ATOM 769 O O . THR A 1 103 ? 13.051 27.685 -5.358 1.00 38.59 ? 103 THR A O 1 ATOM 770 C CB . THR A 1 103 ? 10.277 28.827 -5.994 1.00 39.22 ? 103 THR A CB 1 ATOM 771 O OG1 . THR A 1 103 ? 9.039 29.412 -5.573 1.00 40.97 ? 103 THR A OG1 1 ATOM 772 C CG2 . THR A 1 103 ? 9.918 28.224 -7.321 1.00 38.01 ? 103 THR A CG2 1 ATOM 773 N N . VAL A 1 104 ? 11.865 25.842 -5.952 1.00 36.54 ? 104 VAL A N 1 ATOM 774 C CA . VAL A 1 104 ? 13.023 25.021 -6.313 1.00 35.65 ? 104 VAL A CA 1 ATOM 775 C C . VAL A 1 104 ? 12.761 24.120 -7.529 1.00 34.45 ? 104 VAL A C 1 ATOM 776 O O . VAL A 1 104 ? 11.717 23.480 -7.623 1.00 35.00 ? 104 VAL A O 1 ATOM 777 C CB . VAL A 1 104 ? 13.575 24.241 -5.063 1.00 38.39 ? 104 VAL A CB 1 ATOM 778 C CG1 . VAL A 1 104 ? 12.625 23.162 -4.596 1.00 38.95 ? 104 VAL A CG1 1 ATOM 779 C CG2 . VAL A 1 104 ? 14.942 23.640 -5.332 1.00 41.31 ? 104 VAL A CG2 1 ATOM 780 N N . THR A 1 105 ? 13.707 24.114 -8.469 1.00 33.79 ? 105 THR A N 1 ATOM 781 C CA . THR A 1 105 ? 13.708 23.216 -9.615 1.00 32.36 ? 105 THR A CA 1 ATOM 782 C C . THR A 1 105 ? 14.091 21.814 -9.151 1.00 32.45 ? 105 THR A C 1 ATOM 783 O O . THR A 1 105 ? 15.228 21.576 -8.712 1.00 32.62 ? 105 THR A O 1 ATOM 784 C CB . THR A 1 105 ? 14.697 23.699 -10.682 1.00 33.77 ? 105 THR A CB 1 ATOM 785 O OG1 . THR A 1 105 ? 14.334 25.011 -11.111 1.00 32.80 ? 105 THR A OG1 1 ATOM 786 C CG2 . THR A 1 105 ? 14.536 22.894 -11.947 1.00 33.64 ? 105 THR A CG2 1 ATOM 787 N N . GLN A 1 106 ? 13.144 20.880 -9.259 1.00 28.62 ? 106 GLN A N 1 ATOM 788 C CA . GLN A 1 106 ? 13.296 19.607 -8.575 1.00 27.81 ? 106 GLN A CA 1 ATOM 789 C C . GLN A 1 106 ? 13.002 18.428 -9.518 1.00 27.93 ? 106 GLN A C 1 ATOM 790 O O . GLN A 1 106 ? 12.058 18.487 -10.281 1.00 27.06 ? 106 GLN A O 1 ATOM 791 C CB . GLN A 1 106 ? 12.397 19.602 -7.317 1.00 27.51 ? 106 GLN A CB 1 ATOM 792 C CG . GLN A 1 106 ? 12.417 18.316 -6.498 1.00 27.05 ? 106 GLN A CG 1 ATOM 793 C CD . GLN A 1 106 ? 13.770 18.000 -5.914 1.00 28.08 ? 106 GLN A CD 1 ATOM 794 O OE1 . GLN A 1 106 ? 14.450 18.904 -5.425 1.00 26.55 ? 106 GLN A OE1 1 ATOM 795 N NE2 . GLN A 1 106 ? 14.176 16.712 -5.963 1.00 27.85 ? 106 GLN A NE2 1 ATOM 796 N N . MET A 1 107 ? 13.837 17.390 -9.483 1.00 26.45 ? 107 MET A N 1 ATOM 797 C CA . MET A 1 107 ? 13.496 16.102 -10.098 1.00 29.98 ? 107 MET A CA 1 ATOM 798 C C . MET A 1 107 ? 12.595 15.263 -9.173 1.00 27.21 ? 107 MET A C 1 ATOM 799 O O . MET A 1 107 ? 12.917 15.049 -8.007 1.00 28.53 ? 107 MET A O 1 ATOM 800 C CB . MET A 1 107 ? 14.750 15.307 -10.413 1.00 31.49 ? 107 MET A CB 1 ATOM 801 C CG . MET A 1 107 ? 15.413 15.679 -11.695 1.00 38.04 ? 107 MET A CG 1 ATOM 802 S SD . MET A 1 107 ? 14.723 14.718 -13.062 1.00 43.07 ? 107 MET A SD 1 ATOM 803 C CE . MET A 1 107 ? 16.115 14.841 -14.183 1.00 38.36 ? 107 MET A CE 1 ATOM 804 N N . PHE A 1 108 ? 11.483 14.777 -9.709 1.00 23.91 ? 108 PHE A N 1 ATOM 805 C CA . PHE A 1 108 ? 10.517 14.056 -8.904 1.00 21.84 ? 108 PHE A CA 1 ATOM 806 C C . PHE A 1 108 ? 10.019 12.867 -9.723 1.00 21.91 ? 108 PHE A C 1 ATOM 807 O O . PHE A 1 108 ? 10.137 12.893 -10.936 1.00 22.81 ? 108 PHE A O 1 ATOM 808 C CB . PHE A 1 108 ? 9.390 14.997 -8.437 1.00 20.55 ? 108 PHE A CB 1 ATOM 809 C CG . PHE A 1 108 ? 8.572 15.601 -9.564 1.00 21.59 ? 108 PHE A CG 1 ATOM 810 C CD1 . PHE A 1 108 ? 8.971 16.774 -10.182 1.00 24.03 ? 108 PHE A CD1 1 ATOM 811 C CD2 . PHE A 1 108 ? 7.398 14.997 -9.989 1.00 22.85 ? 108 PHE A CD2 1 ATOM 812 C CE1 . PHE A 1 108 ? 8.221 17.325 -11.237 1.00 23.35 ? 108 PHE A CE1 1 ATOM 813 C CE2 . PHE A 1 108 ? 6.658 15.527 -11.041 1.00 22.57 ? 108 PHE A CE2 1 ATOM 814 C CZ . PHE A 1 108 ? 7.074 16.710 -11.659 1.00 20.88 ? 108 PHE A CZ 1 ATOM 815 N N . GLY A 1 109 ? 9.478 11.832 -9.063 1.00 24.11 ? 109 GLY A N 1 ATOM 816 C CA . GLY A 1 109 ? 8.874 10.677 -9.757 1.00 20.04 ? 109 GLY A CA 1 ATOM 817 C C . GLY A 1 109 ? 7.373 10.817 -9.990 1.00 24.64 ? 109 GLY A C 1 ATOM 818 O O . GLY A 1 109 ? 6.626 11.232 -9.109 1.00 19.96 ? 109 GLY A O 1 ATOM 819 N N . GLU A 1 110 ? 6.940 10.487 -11.203 1.00 23.53 ? 110 GLU A N 1 ATOM 820 C CA . GLU A 1 110 ? 5.560 10.489 -11.565 1.00 24.12 ? 110 GLU A CA 1 ATOM 821 C C . GLU A 1 110 ? 5.122 9.035 -11.514 1.00 22.11 ? 110 GLU A C 1 ATOM 822 O O . GLU A 1 110 ? 5.579 8.234 -12.328 1.00 25.92 ? 110 GLU A O 1 ATOM 823 C CB . GLU A 1 110 ? 5.408 11.016 -13.001 1.00 25.06 ? 110 GLU A CB 1 ATOM 824 C CG . GLU A 1 110 ? 5.265 12.513 -13.166 1.00 26.99 ? 110 GLU A CG 1 ATOM 825 C CD . GLU A 1 110 ? 4.861 12.892 -14.597 1.00 27.28 ? 110 GLU A CD 1 ATOM 826 O OE1 . GLU A 1 110 ? 3.697 12.592 -14.999 1.00 26.10 ? 110 GLU A OE1 1 ATOM 827 O OE2 . GLU A 1 110 ? 5.696 13.498 -15.318 1.00 25.89 ? 110 GLU A OE2 1 ATOM 828 N N . VAL A 1 111 ? 4.248 8.685 -10.569 1.00 22.50 ? 111 VAL A N 1 ATOM 829 C CA . VAL A 1 111 ? 3.759 7.295 -10.436 1.00 21.63 ? 111 VAL A CA 1 ATOM 830 C C . VAL A 1 111 ? 2.702 6.873 -11.499 1.00 23.38 ? 111 VAL A C 1 ATOM 831 O O . VAL A 1 111 ? 1.630 7.486 -11.610 1.00 26.08 ? 111 VAL A O 1 ATOM 832 C CB . VAL A 1 111 ? 3.165 7.046 -9.035 1.00 21.20 ? 111 VAL A CB 1 ATOM 833 C CG1 . VAL A 1 111 ? 2.672 5.628 -8.909 1.00 24.26 ? 111 VAL A CG1 1 ATOM 834 C CG2 . VAL A 1 111 ? 4.160 7.359 -7.918 1.00 23.50 ? 111 VAL A CG2 1 ATOM 835 N N . THR A 1 112 ? 3.003 5.796 -12.232 1.00 23.94 ? 112 THR A N 1 ATOM 836 C CA . THR A 1 112 ? 2.102 5.166 -13.201 1.00 24.68 ? 112 THR A CA 1 ATOM 837 C C . THR A 1 112 ? 1.453 3.862 -12.764 1.00 26.98 ? 112 THR A C 1 ATOM 838 O O . THR A 1 112 ? 0.493 3.432 -13.406 1.00 29.60 ? 112 THR A O 1 ATOM 839 C CB . THR A 1 112 ? 2.854 4.837 -14.491 1.00 26.42 ? 112 THR A CB 1 ATOM 840 O OG1 . THR A 1 112 ? 3.980 3.990 -14.170 1.00 24.79 ? 112 THR A OG1 1 ATOM 841 C CG2 . THR A 1 112 ? 3.439 6.114 -15.132 1.00 22.57 ? 112 THR A CG2 1 ATOM 842 N N . GLU A 1 113 ? 2.009 3.202 -11.742 1.00 25.50 ? 113 GLU A N 1 ATOM 843 C CA . GLU A 1 113 ? 1.372 2.061 -11.118 1.00 28.41 ? 113 GLU A CA 1 ATOM 844 C C . GLU A 1 113 ? 1.761 1.905 -9.636 1.00 28.54 ? 113 GLU A C 1 ATOM 845 O O . GLU A 1 113 ? 2.873 2.240 -9.222 1.00 27.26 ? 113 GLU A O 1 ATOM 846 C CB . GLU A 1 113 ? 1.683 0.771 -11.894 1.00 29.94 ? 113 GLU A CB 1 ATOM 847 C CG . GLU A 1 113 ? 3.078 0.219 -11.663 1.00 29.36 ? 113 GLU A CG 1 ATOM 848 C CD . GLU A 1 113 ? 3.536 -0.738 -12.759 1.00 32.67 ? 113 GLU A CD 1 ATOM 849 O OE1 . GLU A 1 113 ? 4.761 -0.824 -12.996 1.00 37.10 ? 113 GLU A OE1 1 ATOM 850 O OE2 . GLU A 1 113 ? 2.696 -1.393 -13.389 1.00 27.74 ? 113 GLU A OE2 1 ATOM 851 N N . MET A 1 114 ? 0.817 1.376 -8.860 1.00 28.07 ? 114 MET A N 1 ATOM 852 C CA . MET A 1 114 ? 0.976 1.077 -7.448 1.00 28.10 ? 114 MET A CA 1 ATOM 853 C C . MET A 1 114 ? -0.192 0.228 -6.986 1.00 28.42 ? 114 MET A C 1 ATOM 854 O O . MET A 1 114 ? -1.270 0.282 -7.599 1.00 26.99 ? 114 MET A O 1 ATOM 855 C CB . MET A 1 114 ? 0.988 2.359 -6.596 1.00 28.76 ? 114 MET A CB 1 ATOM 856 C CG . MET A 1 114 ? -0.144 3.331 -6.870 1.00 29.63 ? 114 MET A CG 1 ATOM 857 S SD . MET A 1 114 ? 0.088 4.843 -5.892 1.00 32.30 ? 114 MET A SD 1 ATOM 858 C CE . MET A 1 114 ? -0.525 6.051 -7.076 1.00 29.49 ? 114 MET A CE 1 ATOM 859 N N . PRO A 1 115 ? -0.001 -0.488 -5.870 1.00 27.86 ? 115 PRO A N 1 ATOM 860 C CA . PRO A 1 115 ? -1.074 -1.310 -5.261 1.00 26.90 ? 115 PRO A CA 1 ATOM 861 C C . PRO A 1 115 ? -2.220 -0.460 -4.737 1.00 28.95 ? 115 PRO A C 1 ATOM 862 O O . PRO A 1 115 ? -2.022 0.714 -4.398 1.00 28.77 ? 115 PRO A O 1 ATOM 863 C CB . PRO A 1 115 ? -0.382 -2.006 -4.082 1.00 25.93 ? 115 PRO A CB 1 ATOM 864 C CG . PRO A 1 115 ? 1.058 -1.669 -4.157 1.00 25.90 ? 115 PRO A CG 1 ATOM 865 C CD . PRO A 1 115 ? 1.249 -0.506 -5.080 1.00 24.82 ? 115 PRO A CD 1 ATOM 866 N N . ALA A 1 116 ? -3.415 -1.046 -4.669 1.00 31.36 ? 116 ALA A N 1 ATOM 867 C CA . ALA A 1 116 ? -4.589 -0.350 -4.141 1.00 33.03 ? 116 ALA A CA 1 ATOM 868 C C . ALA A 1 116 ? -4.462 -0.145 -2.647 1.00 32.38 ? 116 ALA A C 1 ATOM 869 O O . ALA A 1 116 ? -4.946 0.841 -2.122 1.00 33.64 ? 116 ALA A O 1 ATOM 870 C CB . ALA A 1 116 ? -5.894 -1.102 -4.469 1.00 31.67 ? 116 ALA A CB 1 ATOM 871 N N . LEU A 1 117 ? -3.804 -1.074 -1.962 1.00 32.52 ? 117 LEU A N 1 ATOM 872 C CA . LEU A 1 117 ? -3.572 -0.923 -0.534 1.00 30.36 ? 117 LEU A CA 1 ATOM 873 C C . LEU A 1 117 ? -2.083 -0.746 -0.262 1.00 30.24 ? 117 LEU A C 1 ATOM 874 O O . LEU A 1 117 ? -1.258 -1.502 -0.773 1.00 28.25 ? 117 LEU A O 1 ATOM 875 C CB . LEU A 1 117 ? -4.113 -2.128 0.244 1.00 33.64 ? 117 LEU A CB 1 ATOM 876 C CG . LEU A 1 117 ? -5.639 -2.303 0.211 1.00 35.73 ? 117 LEU A CG 1 ATOM 877 C CD1 . LEU A 1 117 ? -6.048 -3.782 0.463 1.00 37.24 ? 117 LEU A CD1 1 ATOM 878 C CD2 . LEU A 1 117 ? -6.330 -1.337 1.184 1.00 37.18 ? 117 LEU A CD2 1 ATOM 879 N N . PRO A 1 118 ? -1.727 0.187 0.611 1.00 29.30 ? 118 PRO A N 1 ATOM 880 C CA . PRO A 1 118 ? -2.652 1.052 1.344 1.00 26.90 ? 118 PRO A CA 1 ATOM 881 C C . PRO A 1 118 ? -3.052 2.337 0.622 1.00 28.37 ? 118 PRO A C 1 ATOM 882 O O . PRO A 1 118 ? -3.830 3.127 1.168 1.00 29.58 ? 118 PRO A O 1 ATOM 883 C CB . PRO A 1 118 ? -1.824 1.444 2.566 1.00 26.78 ? 118 PRO A CB 1 ATOM 884 C CG . PRO A 1 118 ? -0.425 1.405 2.075 1.00 26.77 ? 118 PRO A CG 1 ATOM 885 C CD . PRO A 1 118 ? -0.323 0.399 1.015 1.00 28.55 ? 118 PRO A CD 1 ATOM 886 N N . PHE A 1 119 ? -2.495 2.544 -0.569 1.00 26.24 ? 119 PHE A N 1 ATOM 887 C CA . PHE A 1 119 ? -2.528 3.839 -1.252 1.00 27.46 ? 119 PHE A CA 1 ATOM 888 C C . PHE A 1 119 ? -3.891 4.461 -1.549 1.00 28.20 ? 119 PHE A C 1 ATOM 889 O O . PHE A 1 119 ? -4.036 5.694 -1.533 1.00 29.75 ? 119 PHE A O 1 ATOM 890 C CB . PHE A 1 119 ? -1.609 3.793 -2.469 1.00 26.18 ? 119 PHE A CB 1 ATOM 891 C CG . PHE A 1 119 ? -0.207 3.426 -2.102 1.00 26.53 ? 119 PHE A CG 1 ATOM 892 C CD1 . PHE A 1 119 ? 0.562 4.287 -1.314 1.00 26.15 ? 119 PHE A CD1 1 ATOM 893 C CD2 . PHE A 1 119 ? 0.331 2.194 -2.475 1.00 23.13 ? 119 PHE A CD2 1 ATOM 894 C CE1 . PHE A 1 119 ? 1.856 3.948 -0.937 1.00 27.86 ? 119 PHE A CE1 1 ATOM 895 C CE2 . PHE A 1 119 ? 1.616 1.850 -2.097 1.00 27.24 ? 119 PHE A CE2 1 ATOM 896 C CZ . PHE A 1 119 ? 2.386 2.729 -1.334 1.00 27.47 ? 119 PHE A CZ 1 ATOM 897 N N . MET A 1 120 ? -4.903 3.639 -1.789 1.00 27.79 ? 120 MET A N 1 ATOM 898 C CA . MET A 1 120 ? -6.249 4.199 -1.999 1.00 31.17 ? 120 MET A CA 1 ATOM 899 C C . MET A 1 120 ? -6.856 4.788 -0.713 1.00 30.63 ? 120 MET A C 1 ATOM 900 O O . MET A 1 120 ? -7.771 5.598 -0.793 1.00 31.30 ? 120 MET A O 1 ATOM 901 C CB . MET A 1 120 ? -7.206 3.158 -2.596 1.00 30.97 ? 120 MET A CB 1 ATOM 902 C CG . MET A 1 120 ? -7.689 2.115 -1.605 1.00 33.10 ? 120 MET A CG 1 ATOM 903 S SD . MET A 1 120 ? -8.876 0.960 -2.358 1.00 38.05 ? 120 MET A SD 1 ATOM 904 C CE . MET A 1 120 ? -8.707 -0.393 -1.259 1.00 32.83 ? 120 MET A CE 1 ATOM 905 N N . LEU A 1 121 ? -6.345 4.366 0.453 1.00 31.47 ? 121 LEU A N 1 ATOM 906 C CA . LEU A 1 121 ? -6.758 4.874 1.773 1.00 30.83 ? 121 LEU A CA 1 ATOM 907 C C . LEU A 1 121 ? -6.067 6.169 2.220 1.00 28.93 ? 121 LEU A C 1 ATOM 908 O O . LEU A 1 121 ? -6.509 6.817 3.179 1.00 27.19 ? 121 LEU A O 1 ATOM 909 C CB . LEU A 1 121 ? -6.536 3.796 2.836 1.00 33.85 ? 121 LEU A CB 1 ATOM 910 C CG . LEU A 1 121 ? -7.199 2.432 2.578 1.00 34.69 ? 121 LEU A CG 1 ATOM 911 C CD1 . LEU A 1 121 ? -6.730 1.419 3.598 1.00 35.74 ? 121 LEU A CD1 1 ATOM 912 C CD2 . LEU A 1 121 ? -8.724 2.553 2.591 1.00 34.82 ? 121 LEU A CD2 1 ATOM 913 N N . ALA A 1 122 ? -4.996 6.538 1.519 1.00 25.59 ? 122 ALA A N 1 ATOM 914 C CA . ALA A 1 122 ? -4.259 7.781 1.756 1.00 21.09 ? 122 ALA A CA 1 ATOM 915 C C . ALA A 1 122 ? -5.142 8.995 1.482 1.00 22.33 ? 122 ALA A C 1 ATOM 916 O O . ALA A 1 122 ? -5.715 9.109 0.399 1.00 25.66 ? 122 ALA A O 1 ATOM 917 C CB . ALA A 1 122 ? -3.015 7.819 0.857 1.00 20.44 ? 122 ALA A CB 1 ATOM 918 N N . GLU A 1 123 ? -5.269 9.910 2.441 1.00 24.20 ? 123 GLU A N 1 ATOM 919 C CA . GLU A 1 123 ? -6.029 11.159 2.192 1.00 23.20 ? 123 GLU A CA 1 ATOM 920 C C . GLU A 1 123 ? -5.200 12.189 1.387 1.00 25.78 ? 123 GLU A C 1 ATOM 921 O O . GLU A 1 123 ? -5.744 13.148 0.830 1.00 29.85 ? 123 GLU A O 1 ATOM 922 C CB . GLU A 1 123 ? -6.516 11.793 3.511 1.00 27.75 ? 123 GLU A CB 1 ATOM 923 C CG . GLU A 1 123 ? -7.426 10.935 4.373 1.00 29.33 ? 123 GLU A CG 1 ATOM 924 C CD . GLU A 1 123 ? -8.677 10.490 3.653 1.00 38.38 ? 123 GLU A CD 1 ATOM 925 O OE1 . GLU A 1 123 ? -9.556 11.342 3.444 1.00 38.51 ? 123 GLU A OE1 1 ATOM 926 O OE2 . GLU A 1 123 ? -8.775 9.289 3.286 1.00 43.34 ? 123 GLU A OE2 1 ATOM 927 N N . PHE A 1 124 ? -3.897 11.958 1.304 1.00 25.45 ? 124 PHE A N 1 ATOM 928 C CA . PHE A 1 124 ? -2.946 12.793 0.565 1.00 22.70 ? 124 PHE A CA 1 ATOM 929 C C . PHE A 1 124 ? -2.578 12.148 -0.807 1.00 26.44 ? 124 PHE A C 1 ATOM 930 O O . PHE A 1 124 ? -2.811 10.951 -1.034 1.00 25.47 ? 124 PHE A O 1 ATOM 931 C CB . PHE A 1 124 ? -1.694 12.993 1.433 1.00 23.30 ? 124 PHE A CB 1 ATOM 932 C CG . PHE A 1 124 ? -1.063 11.696 1.873 1.00 23.43 ? 124 PHE A CG 1 ATOM 933 C CD1 . PHE A 1 124 ? -1.524 11.027 3.004 1.00 23.41 ? 124 PHE A CD1 1 ATOM 934 C CD2 . PHE A 1 124 ? -0.048 11.114 1.117 1.00 24.95 ? 124 PHE A CD2 1 ATOM 935 C CE1 . PHE A 1 124 ? -0.965 9.810 3.390 1.00 23.39 ? 124 PHE A CE1 1 ATOM 936 C CE2 . PHE A 1 124 ? 0.512 9.885 1.487 1.00 25.40 ? 124 PHE A CE2 1 ATOM 937 C CZ . PHE A 1 124 ? 0.060 9.240 2.625 1.00 22.60 ? 124 PHE A CZ 1 ATOM 938 N N . ASP A 1 125 ? -2.002 12.948 -1.711 1.00 25.16 ? 125 ASP A N 1 ATOM 939 C CA . ASP A 1 125 ? -1.665 12.529 -3.064 1.00 23.33 ? 125 ASP A CA 1 ATOM 940 C C . ASP A 1 125 ? -0.251 12.022 -3.210 1.00 24.60 ? 125 ASP A C 1 ATOM 941 O O . ASP A 1 125 ? -0.008 11.136 -4.000 1.00 22.95 ? 125 ASP A O 1 ATOM 942 C CB . ASP A 1 125 ? -1.816 13.713 -4.041 1.00 25.31 ? 125 ASP A CB 1 ATOM 943 C CG . ASP A 1 125 ? -3.142 14.425 -3.886 1.00 28.84 ? 125 ASP A CG 1 ATOM 944 O OD1 . ASP A 1 125 ? -4.193 13.793 -4.180 1.00 28.96 ? 125 ASP A OD1 1 ATOM 945 O OD2 . ASP A 1 125 ? -3.218 15.606 -3.470 1.00 27.33 ? 125 ASP A OD2 1 ATOM 946 N N . GLY A 1 126 ? 0.699 12.618 -2.494 1.00 24.92 ? 126 GLY A N 1 ATOM 947 C CA . GLY A 1 126 ? 2.075 12.269 -2.728 1.00 22.36 ? 126 GLY A CA 1 ATOM 948 C C . GLY A 1 126 ? 2.959 12.295 -1.511 1.00 22.05 ? 126 GLY A C 1 ATOM 949 O O . GLY A 1 126 ? 2.484 12.349 -0.376 1.00 22.08 ? 126 GLY A O 1 ATOM 950 N N A VAL A 1 127 ? 4.262 12.281 -1.783 0.50 19.40 ? 127 VAL A N 1 ATOM 951 N N B VAL A 1 127 ? 4.270 12.256 -1.738 0.50 20.76 ? 127 VAL A N 1 ATOM 952 C CA A VAL A 1 127 ? 5.295 12.201 -0.770 0.50 18.32 ? 127 VAL A CA 1 ATOM 953 C CA B VAL A 1 127 ? 5.238 12.234 -0.644 0.50 20.61 ? 127 VAL A CA 1 ATOM 954 C C A VAL A 1 127 ? 6.414 13.171 -1.134 0.50 17.97 ? 127 VAL A C 1 ATOM 955 C C B VAL A 1 127 ? 6.505 12.988 -1.022 0.50 19.55 ? 127 VAL A C 1 ATOM 956 O O A VAL A 1 127 ? 6.754 13.302 -2.304 0.50 18.71 ? 127 VAL A O 1 ATOM 957 O O B VAL A 1 127 ? 7.056 12.764 -2.086 0.50 20.49 ? 127 VAL A O 1 ATOM 958 C CB A VAL A 1 127 ? 5.823 10.735 -0.674 0.50 16.80 ? 127 VAL A CB 1 ATOM 959 C CB B VAL A 1 127 ? 5.571 10.762 -0.213 0.50 21.01 ? 127 VAL A CB 1 ATOM 960 C CG1 A VAL A 1 127 ? 7.097 10.643 0.153 0.50 17.09 ? 127 VAL A CG1 1 ATOM 961 C CG1 B VAL A 1 127 ? 6.044 9.947 -1.392 0.50 19.57 ? 127 VAL A CG1 1 ATOM 962 C CG2 A VAL A 1 127 ? 4.726 9.803 -0.096 0.50 14.17 ? 127 VAL A CG2 1 ATOM 963 C CG2 B VAL A 1 127 ? 6.593 10.717 0.929 0.50 20.22 ? 127 VAL A CG2 1 ATOM 964 N N . VAL A 1 128 ? 6.952 13.883 -0.142 1.00 20.67 ? 128 VAL A N 1 ATOM 965 C CA . VAL A 1 128 ? 8.191 14.638 -0.327 1.00 20.44 ? 128 VAL A CA 1 ATOM 966 C C . VAL A 1 128 ? 9.212 14.000 0.647 1.00 21.45 ? 128 VAL A C 1 ATOM 967 O O . VAL A 1 128 ? 9.100 14.168 1.828 1.00 25.17 ? 128 VAL A O 1 ATOM 968 C CB . VAL A 1 128 ? 7.987 16.164 -0.018 1.00 22.06 ? 128 VAL A CB 1 ATOM 969 C CG1 . VAL A 1 128 ? 9.321 16.889 0.189 1.00 20.11 ? 128 VAL A CG1 1 ATOM 970 C CG2 . VAL A 1 128 ? 7.201 16.843 -1.143 1.00 21.81 ? 128 VAL A CG2 1 ATOM 971 N N . GLY A 1 129 ? 10.177 13.238 0.140 1.00 23.78 ? 129 GLY A N 1 ATOM 972 C CA . GLY A 1 129 ? 11.184 12.610 1.002 1.00 23.65 ? 129 GLY A CA 1 ATOM 973 C C . GLY A 1 129 ? 12.174 13.627 1.521 1.00 22.80 ? 129 GLY A C 1 ATOM 974 O O . GLY A 1 129 ? 12.751 14.400 0.738 1.00 25.81 ? 129 GLY A O 1 ATOM 975 N N . MET A 1 130 ? 12.333 13.673 2.840 1.00 23.51 ? 130 MET A N 1 ATOM 976 C CA . MET A 1 130 ? 13.241 14.648 3.465 1.00 23.38 ? 130 MET A CA 1 ATOM 977 C C . MET A 1 130 ? 14.570 13.987 3.881 1.00 25.12 ? 130 MET A C 1 ATOM 978 O O . MET A 1 130 ? 15.301 14.510 4.735 1.00 27.47 ? 130 MET A O 1 ATOM 979 C CB . MET A 1 130 ? 12.563 15.343 4.642 1.00 20.64 ? 130 MET A CB 1 ATOM 980 C CG . MET A 1 130 ? 11.273 16.032 4.283 1.00 21.55 ? 130 MET A CG 1 ATOM 981 S SD . MET A 1 130 ? 11.534 17.497 3.259 1.00 28.12 ? 130 MET A SD 1 ATOM 982 C CE . MET A 1 130 ? 12.360 18.522 4.466 1.00 20.92 ? 130 MET A CE 1 ATOM 983 N N . GLY A 1 131 ? 14.854 12.822 3.286 1.00 26.65 ? 131 GLY A N 1 ATOM 984 C CA . GLY A 1 131 ? 16.065 12.047 3.588 1.00 25.27 ? 131 GLY A CA 1 ATOM 985 C C . GLY A 1 131 ? 17.244 12.473 2.727 1.00 26.54 ? 131 GLY A C 1 ATOM 986 O O . GLY A 1 131 ? 17.138 13.431 1.955 1.00 28.16 ? 131 GLY A O 1 ATOM 987 N N . PHE A 1 132 ? 18.360 11.740 2.832 1.00 28.49 ? 132 PHE A N 1 ATOM 988 C CA . PHE A 1 132 ? 19.627 12.109 2.163 1.00 28.86 ? 132 PHE A CA 1 ATOM 989 C C . PHE A 1 132 ? 19.833 11.462 0.791 1.00 31.49 ? 132 PHE A C 1 ATOM 990 O O . PHE A 1 132 ? 19.255 10.399 0.513 1.00 30.24 ? 132 PHE A O 1 ATOM 991 C CB . PHE A 1 132 ? 20.803 11.659 3.014 1.00 27.93 ? 132 PHE A CB 1 ATOM 992 C CG . PHE A 1 132 ? 20.855 12.252 4.397 1.00 28.86 ? 132 PHE A CG 1 ATOM 993 C CD1 . PHE A 1 132 ? 20.037 11.766 5.427 1.00 29.85 ? 132 PHE A CD1 1 ATOM 994 C CD2 . PHE A 1 132 ? 21.796 13.229 4.705 1.00 28.28 ? 132 PHE A CD2 1 ATOM 995 C CE1 . PHE A 1 132 ? 20.129 12.293 6.718 1.00 28.53 ? 132 PHE A CE1 1 ATOM 996 C CE2 . PHE A 1 132 ? 21.883 13.737 6.000 1.00 28.67 ? 132 PHE A CE2 1 ATOM 997 C CZ . PHE A 1 132 ? 21.060 13.268 6.999 1.00 26.11 ? 132 PHE A CZ 1 ATOM 998 N N . ILE A 1 133 ? 20.703 12.053 -0.040 1.00 27.26 ? 133 ILE A N 1 ATOM 999 C CA . ILE A 1 133 ? 21.017 11.478 -1.364 1.00 31.45 ? 133 ILE A CA 1 ATOM 1000 C C . ILE A 1 133 ? 21.452 9.990 -1.304 1.00 31.87 ? 133 ILE A C 1 ATOM 1001 O O . ILE A 1 133 ? 21.166 9.215 -2.226 1.00 34.13 ? 133 ILE A O 1 ATOM 1002 C CB . ILE A 1 133 ? 22.080 12.362 -2.149 1.00 32.72 ? 133 ILE A CB 1 ATOM 1003 C CG1 . ILE A 1 133 ? 22.003 12.136 -3.672 1.00 32.11 ? 133 ILE A CG1 1 ATOM 1004 C CG2 . ILE A 1 133 ? 23.517 12.141 -1.621 1.00 32.59 ? 133 ILE A CG2 1 ATOM 1005 C CD1 . ILE A 1 133 ? 22.821 13.184 -4.515 1.00 30.82 ? 133 ILE A CD1 1 ATOM 1006 N N . GLU A 1 134 ? 22.123 9.599 -0.224 1.00 31.96 ? 134 GLU A N 1 ATOM 1007 C CA . GLU A 1 134 ? 22.553 8.208 -0.033 1.00 34.40 ? 134 GLU A CA 1 ATOM 1008 C C . GLU A 1 134 ? 21.433 7.170 -0.218 1.00 36.15 ? 134 GLU A C 1 ATOM 1009 O O . GLU A 1 134 ? 21.675 6.086 -0.770 1.00 36.96 ? 134 GLU A O 1 ATOM 1010 C CB . GLU A 1 134 ? 23.229 8.038 1.325 1.00 35.64 ? 134 GLU A CB 1 ATOM 1011 C CG . GLU A 1 134 ? 24.645 8.593 1.398 1.00 41.14 ? 134 GLU A CG 1 ATOM 1012 C CD . GLU A 1 134 ? 24.716 10.100 1.622 1.00 44.00 ? 134 GLU A CD 1 ATOM 1013 O OE1 . GLU A 1 134 ? 23.675 10.791 1.576 1.00 43.76 ? 134 GLU A OE1 1 ATOM 1014 O OE2 . GLU A 1 134 ? 25.832 10.606 1.849 1.00 45.65 ? 134 GLU A OE2 1 ATOM 1015 N N . GLN A 1 135 ? 20.208 7.488 0.203 1.00 33.58 ? 135 GLN A N 1 ATOM 1016 C CA . GLN A 1 135 ? 19.105 6.532 0.028 1.00 35.38 ? 135 GLN A CA 1 ATOM 1017 C C . GLN A 1 135 ? 18.128 6.890 -1.098 1.00 33.92 ? 135 GLN A C 1 ATOM 1018 O O . GLN A 1 135 ? 17.028 6.334 -1.177 1.00 32.69 ? 135 GLN A O 1 ATOM 1019 C CB . GLN A 1 135 ? 18.371 6.273 1.356 1.00 37.77 ? 135 GLN A CB 1 ATOM 1020 C CG . GLN A 1 135 ? 19.257 5.553 2.394 1.00 44.74 ? 135 GLN A CG 1 ATOM 1021 C CD . GLN A 1 135 ? 18.651 4.244 2.941 1.00 50.09 ? 135 GLN A CD 1 ATOM 1022 O OE1 . GLN A 1 135 ? 18.856 3.909 4.117 1.00 52.78 ? 135 GLN A OE1 1 ATOM 1023 N NE2 . GLN A 1 135 ? 17.936 3.497 2.088 1.00 51.99 ? 135 GLN A NE2 1 ATOM 1024 N N . ALA A 1 136 ? 18.538 7.800 -1.979 1.00 34.74 ? 136 ALA A N 1 ATOM 1025 C CA . ALA A 1 136 ? 17.674 8.261 -3.078 1.00 33.58 ? 136 ALA A CA 1 ATOM 1026 C C . ALA A 1 136 ? 17.685 7.249 -4.200 1.00 34.14 ? 136 ALA A C 1 ATOM 1027 O O . ALA A 1 136 ? 18.760 6.914 -4.714 1.00 34.74 ? 136 ALA A O 1 ATOM 1028 C CB . ALA A 1 136 ? 18.128 9.604 -3.594 1.00 32.67 ? 136 ALA A CB 1 ATOM 1029 N N . ILE A 1 137 ? 16.493 6.768 -4.570 1.00 33.27 ? 137 ILE A N 1 ATOM 1030 C CA . ILE A 1 137 ? 16.321 5.866 -5.727 1.00 31.97 ? 137 ILE A CA 1 ATOM 1031 C C . ILE A 1 137 ? 16.809 6.616 -6.969 1.00 34.48 ? 137 ILE A C 1 ATOM 1032 O O . ILE A 1 137 ? 16.385 7.749 -7.244 1.00 33.96 ? 137 ILE A O 1 ATOM 1033 C CB . ILE A 1 137 ? 14.828 5.390 -5.839 1.00 30.13 ? 137 ILE A CB 1 ATOM 1034 C CG1 . ILE A 1 137 ? 14.440 4.619 -4.580 1.00 30.18 ? 137 ILE A CG1 1 ATOM 1035 C CG2 . ILE A 1 137 ? 14.591 4.519 -7.099 1.00 31.35 ? 137 ILE A CG2 1 ATOM 1036 C CD1 . ILE A 1 137 ? 12.966 4.498 -4.340 1.00 27.32 ? 137 ILE A CD1 1 ATOM 1037 N N . GLY A 1 138 ? 17.761 6.002 -7.673 1.00 35.19 ? 138 GLY A N 1 ATOM 1038 C CA . GLY A 1 138 ? 18.379 6.597 -8.845 1.00 34.04 ? 138 GLY A CA 1 ATOM 1039 C C . GLY A 1 138 ? 19.367 7.703 -8.551 1.00 33.55 ? 138 GLY A C 1 ATOM 1040 O O . GLY A 1 138 ? 19.784 8.415 -9.463 1.00 35.65 ? 138 GLY A O 1 ATOM 1041 N N . ARG A 1 139 ? 19.721 7.857 -7.283 1.00 34.55 ? 139 ARG A N 1 ATOM 1042 C CA . ARG A 1 139 ? 20.575 8.963 -6.795 1.00 38.28 ? 139 ARG A CA 1 ATOM 1043 C C . ARG A 1 139 ? 20.071 10.361 -7.203 1.00 37.01 ? 139 ARG A C 1 ATOM 1044 O O . ARG A 1 139 ? 20.862 11.276 -7.482 1.00 36.83 ? 139 ARG A O 1 ATOM 1045 C CB . ARG A 1 139 ? 22.047 8.773 -7.226 1.00 44.12 ? 139 ARG A CB 1 ATOM 1046 C CG . ARG A 1 139 ? 22.847 7.705 -6.476 1.00 48.69 ? 139 ARG A CG 1 ATOM 1047 C CD . ARG A 1 139 ? 22.931 6.346 -7.211 1.00 54.43 ? 139 ARG A CD 1 ATOM 1048 N NE . ARG A 1 139 ? 24.312 5.861 -7.361 1.00 58.30 ? 139 ARG A NE 1 ATOM 1049 C CZ . ARG A 1 139 ? 25.053 5.962 -8.482 1.00 60.25 ? 139 ARG A CZ 1 ATOM 1050 N NH1 . ARG A 1 139 ? 24.555 6.530 -9.582 1.00 59.88 ? 139 ARG A NH1 1 ATOM 1051 N NH2 . ARG A 1 139 ? 26.300 5.491 -8.503 1.00 59.86 ? 139 ARG A NH2 1 ATOM 1052 N N . VAL A 1 140 ? 18.756 10.540 -7.232 1.00 34.78 ? 140 VAL A N 1 ATOM 1053 C CA . VAL A 1 140 ? 18.186 11.843 -7.561 1.00 32.15 ? 140 VAL A CA 1 ATOM 1054 C C . VAL A 1 140 ? 18.448 12.780 -6.372 1.00 30.21 ? 140 VAL A C 1 ATOM 1055 O O . VAL A 1 140 ? 18.157 12.425 -5.224 1.00 28.95 ? 140 VAL A O 1 ATOM 1056 C CB . VAL A 1 140 ? 16.666 11.733 -7.862 1.00 30.35 ? 140 VAL A CB 1 ATOM 1057 C CG1 . VAL A 1 140 ? 16.107 13.061 -8.270 1.00 30.00 ? 140 VAL A CG1 1 ATOM 1058 C CG2 . VAL A 1 140 ? 16.410 10.714 -8.961 1.00 27.84 ? 140 VAL A CG2 1 ATOM 1059 N N . THR A 1 141 ? 19.015 13.957 -6.647 1.00 27.80 ? 141 THR A N 1 ATOM 1060 C CA . THR A 1 141 ? 19.259 14.972 -5.612 1.00 27.77 ? 141 THR A CA 1 ATOM 1061 C C . THR A 1 141 ? 17.943 15.281 -4.898 1.00 29.45 ? 141 THR A C 1 ATOM 1062 O O . THR A 1 141 ? 17.004 15.695 -5.555 1.00 27.22 ? 141 THR A O 1 ATOM 1063 C CB . THR A 1 141 ? 19.824 16.268 -6.247 1.00 28.16 ? 141 THR A CB 1 ATOM 1064 O OG1 . THR A 1 141 ? 20.962 15.955 -7.060 1.00 25.78 ? 141 THR A OG1 1 ATOM 1065 C CG2 . THR A 1 141 ? 20.344 17.235 -5.177 1.00 27.25 ? 141 THR A CG2 1 ATOM 1066 N N . PRO A 1 142 ? 17.865 15.062 -3.575 1.00 30.81 ? 142 PRO A N 1 ATOM 1067 C CA . PRO A 1 142 ? 16.619 15.278 -2.819 1.00 30.10 ? 142 PRO A CA 1 ATOM 1068 C C . PRO A 1 142 ? 16.308 16.762 -2.623 1.00 29.43 ? 142 PRO A C 1 ATOM 1069 O O . PRO A 1 142 ? 17.206 17.598 -2.746 1.00 30.29 ? 142 PRO A O 1 ATOM 1070 C CB . PRO A 1 142 ? 16.902 14.622 -1.453 1.00 28.97 ? 142 PRO A CB 1 ATOM 1071 C CG . PRO A 1 142 ? 18.163 13.837 -1.648 1.00 29.00 ? 142 PRO A CG 1 ATOM 1072 C CD . PRO A 1 142 ? 18.955 14.620 -2.689 1.00 30.28 ? 142 PRO A CD 1 ATOM 1073 N N . ILE A 1 143 ? 15.037 17.069 -2.351 1.00 24.63 ? 143 ILE A N 1 ATOM 1074 C CA . ILE A 1 143 ? 14.550 18.436 -2.284 1.00 25.66 ? 143 ILE A CA 1 ATOM 1075 C C . ILE A 1 143 ? 15.234 19.327 -1.272 1.00 28.86 ? 143 ILE A C 1 ATOM 1076 O O . ILE A 1 143 ? 15.503 20.487 -1.573 1.00 31.01 ? 143 ILE A O 1 ATOM 1077 C CB . ILE A 1 143 ? 12.970 18.498 -2.125 1.00 26.88 ? 143 ILE A CB 1 ATOM 1078 C CG1 . ILE A 1 143 ? 12.466 19.934 -2.373 1.00 27.45 ? 143 ILE A CG1 1 ATOM 1079 C CG2 . ILE A 1 143 ? 12.499 17.868 -0.815 1.00 27.01 ? 143 ILE A CG2 1 ATOM 1080 C CD1 . ILE A 1 143 ? 11.117 20.047 -3.004 1.00 27.63 ? 143 ILE A CD1 1 ATOM 1081 N N . PHE A 1 144 ? 15.518 18.812 -0.078 1.00 29.06 ? 144 PHE A N 1 ATOM 1082 C CA . PHE A 1 144 ? 16.127 19.661 0.938 1.00 30.15 ? 144 PHE A CA 1 ATOM 1083 C C . PHE A 1 144 ? 17.595 19.990 0.624 1.00 30.90 ? 144 PHE A C 1 ATOM 1084 O O . PHE A 1 144 ? 18.049 21.060 0.996 1.00 32.60 ? 144 PHE A O 1 ATOM 1085 C CB . PHE A 1 144 ? 15.935 19.126 2.359 1.00 31.05 ? 144 PHE A CB 1 ATOM 1086 C CG . PHE A 1 144 ? 16.167 20.170 3.430 1.00 32.60 ? 144 PHE A CG 1 ATOM 1087 C CD1 . PHE A 1 144 ? 15.258 21.229 3.603 1.00 31.26 ? 144 PHE A CD1 1 ATOM 1088 C CD2 . PHE A 1 144 ? 17.308 20.123 4.237 1.00 30.72 ? 144 PHE A CD2 1 ATOM 1089 C CE1 . PHE A 1 144 ? 15.476 22.190 4.577 1.00 30.43 ? 144 PHE A CE1 1 ATOM 1090 C CE2 . PHE A 1 144 ? 17.523 21.078 5.222 1.00 30.58 ? 144 PHE A CE2 1 ATOM 1091 C CZ . PHE A 1 144 ? 16.607 22.110 5.397 1.00 29.49 ? 144 PHE A CZ 1 ATOM 1092 N N . ASP A 1 145 ? 18.306 19.080 -0.064 1.00 30.15 ? 145 ASP A N 1 ATOM 1093 C CA . ASP A 1 145 ? 19.599 19.360 -0.700 1.00 29.89 ? 145 ASP A CA 1 ATOM 1094 C C . ASP A 1 145 ? 19.572 20.551 -1.673 1.00 31.42 ? 145 ASP A C 1 ATOM 1095 O O . ASP A 1 145 ? 20.453 21.407 -1.654 1.00 32.99 ? 145 ASP A O 1 ATOM 1096 C CB . ASP A 1 145 ? 20.095 18.129 -1.455 1.00 31.16 ? 145 ASP A CB 1 ATOM 1097 C CG . ASP A 1 145 ? 20.782 17.137 -0.550 1.00 34.81 ? 145 ASP A CG 1 ATOM 1098 O OD1 . ASP A 1 145 ? 20.400 17.061 0.625 1.00 38.82 ? 145 ASP A OD1 1 ATOM 1099 O OD2 . ASP A 1 145 ? 21.713 16.399 -0.915 1.00 35.55 ? 145 ASP A OD2 1 ATOM 1100 N N . ASN A 1 146 ? 18.558 20.593 -2.528 1.00 30.12 ? 146 ASN A N 1 ATOM 1101 C CA . ASN A 1 146 ? 18.408 21.680 -3.476 1.00 32.16 ? 146 ASN A CA 1 ATOM 1102 C C . ASN A 1 146 ? 17.993 23.022 -2.807 1.00 32.24 ? 146 ASN A C 1 ATOM 1103 O O . ASN A 1 146 ? 18.272 24.094 -3.341 1.00 32.25 ? 146 ASN A O 1 ATOM 1104 C CB . ASN A 1 146 ? 17.455 21.260 -4.606 1.00 32.87 ? 146 ASN A CB 1 ATOM 1105 C CG . ASN A 1 146 ? 18.142 20.423 -5.678 1.00 33.82 ? 146 ASN A CG 1 ATOM 1106 O OD1 . ASN A 1 146 ? 19.365 20.481 -5.854 1.00 34.55 ? 146 ASN A OD1 1 ATOM 1107 N ND2 . ASN A 1 146 ? 17.355 19.654 -6.410 1.00 32.90 ? 146 ASN A ND2 1 ATOM 1108 N N . ILE A 1 147 ? 17.361 22.942 -1.637 1.00 30.43 ? 147 ILE A N 1 ATOM 1109 C CA . ILE A 1 147 ? 17.047 24.127 -0.814 1.00 30.12 ? 147 ILE A CA 1 ATOM 1110 C C . ILE A 1 147 ? 18.298 24.674 -0.063 1.00 33.64 ? 147 ILE A C 1 ATOM 1111 O O . ILE A 1 147 ? 18.517 25.895 -0.012 1.00 35.17 ? 147 ILE A O 1 ATOM 1112 C CB . ILE A 1 147 ? 15.839 23.848 0.142 1.00 28.40 ? 147 ILE A CB 1 ATOM 1113 C CG1 . ILE A 1 147 ? 14.556 23.555 -0.671 1.00 26.74 ? 147 ILE A CG1 1 ATOM 1114 C CG2 . ILE A 1 147 ? 15.570 25.031 1.032 1.00 29.79 ? 147 ILE A CG2 1 ATOM 1115 C CD1 . ILE A 1 147 ? 13.323 23.207 0.183 1.00 29.37 ? 147 ILE A CD1 1 ATOM 1116 N N . ILE A 1 148 ? 19.098 23.773 0.509 1.00 31.98 ? 148 ILE A N 1 ATOM 1117 C CA . ILE A 1 148 ? 20.381 24.122 1.111 1.00 34.20 ? 148 ILE A CA 1 ATOM 1118 C C . ILE A 1 148 ? 21.299 24.832 0.098 1.00 35.34 ? 148 ILE A C 1 ATOM 1119 O O . ILE A 1 148 ? 21.909 25.862 0.425 1.00 38.38 ? 148 ILE A O 1 ATOM 1120 C CB . ILE A 1 148 ? 21.055 22.868 1.712 1.00 33.62 ? 148 ILE A CB 1 ATOM 1121 C CG1 . ILE A 1 148 ? 20.241 22.346 2.907 1.00 32.90 ? 148 ILE A CG1 1 ATOM 1122 C CG2 . ILE A 1 148 ? 22.560 23.147 2.075 1.00 34.72 ? 148 ILE A CG2 1 ATOM 1123 C CD1 . ILE A 1 148 ? 20.739 21.029 3.464 1.00 32.43 ? 148 ILE A CD1 1 ATOM 1124 N N . SER A 1 149 ? 21.343 24.328 -1.133 1.00 36.44 ? 149 SER A N 1 ATOM 1125 C CA . SER A 1 149 ? 22.166 24.919 -2.199 1.00 40.28 ? 149 SER A CA 1 ATOM 1126 C C . SER A 1 149 ? 21.750 26.332 -2.665 1.00 42.58 ? 149 SER A C 1 ATOM 1127 O O . SER A 1 149 ? 22.514 27.006 -3.377 1.00 41.64 ? 149 SER A O 1 ATOM 1128 C CB . SER A 1 149 ? 22.243 23.980 -3.407 1.00 40.89 ? 149 SER A CB 1 ATOM 1129 O OG . SER A 1 149 ? 23.041 22.846 -3.096 1.00 44.49 ? 149 SER A OG 1 ATOM 1130 N N . GLN A 1 150 ? 20.549 26.768 -2.286 1.00 43.22 ? 150 GLN A N 1 ATOM 1131 C CA . GLN A 1 150 ? 20.064 28.095 -2.662 1.00 42.87 ? 150 GLN A CA 1 ATOM 1132 C C . GLN A 1 150 ? 20.579 29.190 -1.748 1.00 41.58 ? 150 GLN A C 1 ATOM 1133 O O . GLN A 1 150 ? 20.458 30.375 -2.069 1.00 40.70 ? 150 GLN A O 1 ATOM 1134 C CB . GLN A 1 150 ? 18.543 28.144 -2.659 1.00 43.96 ? 150 GLN A CB 1 ATOM 1135 C CG . GLN A 1 150 ? 17.886 27.657 -3.911 1.00 45.02 ? 150 GLN A CG 1 ATOM 1136 C CD . GLN A 1 150 ? 16.383 27.753 -3.803 1.00 50.63 ? 150 GLN A CD 1 ATOM 1137 O OE1 . GLN A 1 150 ? 15.660 27.179 -4.622 1.00 53.89 ? 150 GLN A OE1 1 ATOM 1138 N NE2 . GLN A 1 150 ? 15.899 28.476 -2.784 1.00 49.40 ? 150 GLN A NE2 1 ATOM 1139 N N . GLY A 1 151 ? 21.118 28.787 -0.602 1.00 44.09 ? 151 GLY A N 1 ATOM 1140 C CA . GLY A 1 151 ? 21.671 29.705 0.394 1.00 45.86 ? 151 GLY A CA 1 ATOM 1141 C C . GLY A 1 151 ? 20.707 30.399 1.356 1.00 48.00 ? 151 GLY A C 1 ATOM 1142 O O . GLY A 1 151 ? 21.156 31.037 2.315 1.00 50.66 ? 151 GLY A O 1 ATOM 1143 N N . VAL A 1 152 ? 19.400 30.243 1.137 1.00 46.98 ? 152 VAL A N 1 ATOM 1144 C CA . VAL A 1 152 ? 18.376 31.127 1.726 1.00 45.59 ? 152 VAL A CA 1 ATOM 1145 C C . VAL A 1 152 ? 17.923 30.862 3.175 1.00 44.86 ? 152 VAL A C 1 ATOM 1146 O O . VAL A 1 152 ? 17.452 31.773 3.844 1.00 45.05 ? 152 VAL A O 1 ATOM 1147 C CB . VAL A 1 152 ? 17.129 31.258 0.807 1.00 47.46 ? 152 VAL A CB 1 ATOM 1148 C CG1 . VAL A 1 152 ? 17.522 31.852 -0.537 1.00 47.51 ? 152 VAL A CG1 1 ATOM 1149 C CG2 . VAL A 1 152 ? 16.392 29.905 0.619 1.00 47.51 ? 152 VAL A CG2 1 ATOM 1150 N N . LEU A 1 153 ? 18.062 29.633 3.662 1.00 42.60 ? 153 LEU A N 1 ATOM 1151 C CA . LEU A 1 153 ? 17.581 29.300 5.007 1.00 40.77 ? 153 LEU A CA 1 ATOM 1152 C C . LEU A 1 153 ? 18.466 29.902 6.097 1.00 40.07 ? 153 LEU A C 1 ATOM 1153 O O . LEU A 1 153 ? 19.695 29.996 5.930 1.00 38.80 ? 153 LEU A O 1 ATOM 1154 C CB . LEU A 1 153 ? 17.509 27.785 5.197 1.00 39.61 ? 153 LEU A CB 1 ATOM 1155 C CG . LEU A 1 153 ? 16.689 26.919 4.237 1.00 36.87 ? 153 LEU A CG 1 ATOM 1156 C CD1 . LEU A 1 153 ? 16.806 25.476 4.690 1.00 36.06 ? 153 LEU A CD1 1 ATOM 1157 C CD2 . LEU A 1 153 ? 15.246 27.378 4.225 1.00 36.73 ? 153 LEU A CD2 1 ATOM 1158 N N . LYS A 1 154 ? 17.834 30.286 7.205 1.00 38.48 ? 154 LYS A N 1 ATOM 1159 C CA . LYS A 1 154 ? 18.521 30.768 8.408 1.00 40.22 ? 154 LYS A CA 1 ATOM 1160 C C . LYS A 1 154 ? 19.419 29.692 9.058 1.00 41.76 ? 154 LYS A C 1 ATOM 1161 O O . LYS A 1 154 ? 20.506 29.986 9.580 1.00 39.92 ? 154 LYS A O 1 ATOM 1162 C CB . LYS A 1 154 ? 17.495 31.297 9.416 1.00 40.53 ? 154 LYS A CB 1 ATOM 1163 C CG . LYS A 1 154 ? 18.064 32.281 10.444 1.00 43.04 ? 154 LYS A CG 1 ATOM 1164 C CD . LYS A 1 154 ? 17.194 32.427 11.706 1.00 44.64 ? 154 LYS A CD 1 ATOM 1165 C CE . LYS A 1 154 ? 15.738 32.877 11.415 1.00 47.99 ? 154 LYS A CE 1 ATOM 1166 N NZ . LYS A 1 154 ? 15.573 34.018 10.428 1.00 49.40 ? 154 LYS A NZ 1 ATOM 1167 N N . GLU A 1 155 ? 18.961 28.443 9.034 1.00 40.52 ? 155 GLU A N 1 ATOM 1168 C CA . GLU A 1 155 ? 19.747 27.322 9.536 1.00 39.31 ? 155 GLU A CA 1 ATOM 1169 C C . GLU A 1 155 ? 19.454 26.131 8.631 1.00 36.20 ? 155 GLU A C 1 ATOM 1170 O O . GLU A 1 155 ? 18.350 26.001 8.113 1.00 33.19 ? 155 GLU A O 1 ATOM 1171 C CB . GLU A 1 155 ? 19.351 26.971 10.963 1.00 43.46 ? 155 GLU A CB 1 ATOM 1172 C CG . GLU A 1 155 ? 19.717 27.991 12.041 1.00 47.38 ? 155 GLU A CG 1 ATOM 1173 C CD . GLU A 1 155 ? 19.028 27.710 13.375 1.00 48.02 ? 155 GLU A CD 1 ATOM 1174 O OE1 . GLU A 1 155 ? 18.083 26.880 13.403 1.00 50.87 ? 155 GLU A OE1 1 ATOM 1175 O OE2 . GLU A 1 155 ? 19.427 28.319 14.408 1.00 51.98 ? 155 GLU A OE2 1 ATOM 1176 N N . ASP A 1 156 ? 20.432 25.260 8.415 1.00 33.27 ? 156 ASP A N 1 ATOM 1177 C CA . ASP A 1 156 ? 20.162 24.100 7.569 1.00 34.33 ? 156 ASP A CA 1 ATOM 1178 C C . ASP A 1 156 ? 19.475 22.999 8.397 1.00 32.18 ? 156 ASP A C 1 ATOM 1179 O O . ASP A 1 156 ? 20.008 21.907 8.575 1.00 32.85 ? 156 ASP A O 1 ATOM 1180 C CB . ASP A 1 156 ? 21.421 23.627 6.870 1.00 34.87 ? 156 ASP A CB 1 ATOM 1181 C CG . ASP A 1 156 ? 21.963 24.657 5.889 1.00 37.96 ? 156 ASP A CG 1 ATOM 1182 O OD1 . ASP A 1 156 ? 21.179 25.492 5.357 1.00 36.45 ? 156 ASP A OD1 1 ATOM 1183 O OD2 . ASP A 1 156 ? 23.176 24.681 5.567 1.00 41.00 ? 156 ASP A OD2 1 ATOM 1184 N N . VAL A 1 157 ? 18.310 23.352 8.939 1.00 30.89 ? 157 VAL A N 1 ATOM 1185 C CA . VAL A 1 157 ? 17.473 22.444 9.742 1.00 29.41 ? 157 VAL A CA 1 ATOM 1186 C C . VAL A 1 157 ? 16.018 22.507 9.255 1.00 30.09 ? 157 VAL A C 1 ATOM 1187 O O . VAL A 1 157 ? 15.610 23.463 8.579 1.00 30.48 ? 157 VAL A O 1 ATOM 1188 C CB . VAL A 1 157 ? 17.547 22.778 11.279 1.00 29.24 ? 157 VAL A CB 1 ATOM 1189 C CG1 . VAL A 1 157 ? 18.994 22.894 11.743 1.00 27.11 ? 157 VAL A CG1 1 ATOM 1190 C CG2 . VAL A 1 157 ? 16.815 24.079 11.605 1.00 29.03 ? 157 VAL A CG2 1 ATOM 1191 N N . PHE A 1 158 ? 15.239 21.480 9.584 1.00 30.14 ? 158 PHE A N 1 ATOM 1192 C CA . PHE A 1 158 ? 13.785 21.555 9.407 1.00 28.48 ? 158 PHE A CA 1 ATOM 1193 C C . PHE A 1 158 ? 13.144 20.859 10.598 1.00 27.47 ? 158 PHE A C 1 ATOM 1194 O O . PHE A 1 158 ? 13.774 20.013 11.214 1.00 25.00 ? 158 PHE A O 1 ATOM 1195 C CB . PHE A 1 158 ? 13.349 20.974 8.052 1.00 25.08 ? 158 PHE A CB 1 ATOM 1196 C CG . PHE A 1 158 ? 13.783 19.564 7.824 1.00 24.56 ? 158 PHE A CG 1 ATOM 1197 C CD1 . PHE A 1 158 ? 12.974 18.489 8.240 1.00 24.52 ? 158 PHE A CD1 1 ATOM 1198 C CD2 . PHE A 1 158 ? 14.988 19.284 7.196 1.00 25.01 ? 158 PHE A CD2 1 ATOM 1199 C CE1 . PHE A 1 158 ? 13.377 17.166 8.020 1.00 22.36 ? 158 PHE A CE1 1 ATOM 1200 C CE2 . PHE A 1 158 ? 15.395 17.960 6.997 1.00 22.64 ? 158 PHE A CE2 1 ATOM 1201 C CZ . PHE A 1 158 ? 14.607 16.908 7.419 1.00 21.59 ? 158 PHE A CZ 1 ATOM 1202 N N . SER A 1 159 ? 11.928 21.236 10.980 1.00 27.08 ? 159 SER A N 1 ATOM 1203 C CA . SER A 1 159 ? 11.368 20.614 12.169 1.00 29.24 ? 159 SER A CA 1 ATOM 1204 C C . SER A 1 159 ? 9.877 20.284 12.069 1.00 31.07 ? 159 SER A C 1 ATOM 1205 O O . SER A 1 159 ? 9.137 20.915 11.316 1.00 31.52 ? 159 SER A O 1 ATOM 1206 C CB . SER A 1 159 ? 11.648 21.499 13.382 1.00 33.57 ? 159 SER A CB 1 ATOM 1207 O OG . SER A 1 159 ? 10.870 22.655 13.301 1.00 35.37 ? 159 SER A OG 1 ATOM 1208 N N . PHE A 1 160 ? 9.445 19.282 12.828 1.00 30.13 ? 160 PHE A N 1 ATOM 1209 C CA . PHE A 1 160 ? 8.041 18.852 12.782 1.00 30.32 ? 160 PHE A CA 1 ATOM 1210 C C . PHE A 1 160 ? 7.274 19.048 14.074 1.00 28.36 ? 160 PHE A C 1 ATOM 1211 O O . PHE A 1 160 ? 7.756 18.740 15.172 1.00 26.62 ? 160 PHE A O 1 ATOM 1212 C CB . PHE A 1 160 ? 7.943 17.373 12.403 1.00 28.48 ? 160 PHE A CB 1 ATOM 1213 C CG . PHE A 1 160 ? 8.283 17.079 10.981 1.00 27.62 ? 160 PHE A CG 1 ATOM 1214 C CD1 . PHE A 1 160 ? 9.596 17.171 10.526 1.00 27.43 ? 160 PHE A CD1 1 ATOM 1215 C CD2 . PHE A 1 160 ? 7.290 16.655 10.088 1.00 27.75 ? 160 PHE A CD2 1 ATOM 1216 C CE1 . PHE A 1 160 ? 9.904 16.877 9.201 1.00 26.23 ? 160 PHE A CE1 1 ATOM 1217 C CE2 . PHE A 1 160 ? 7.594 16.359 8.773 1.00 26.58 ? 160 PHE A CE2 1 ATOM 1218 C CZ . PHE A 1 160 ? 8.903 16.459 8.327 1.00 28.01 ? 160 PHE A CZ 1 ATOM 1219 N N . TYR A 1 161 ? 6.046 19.514 13.914 1.00 29.23 ? 161 TYR A N 1 ATOM 1220 C CA . TYR A 1 161 ? 5.069 19.525 14.989 1.00 28.76 ? 161 TYR A CA 1 ATOM 1221 C C . TYR A 1 161 ? 3.835 18.732 14.537 1.00 27.62 ? 161 TYR A C 1 ATOM 1222 O O . TYR A 1 161 ? 3.244 19.086 13.533 1.00 27.44 ? 161 TYR A O 1 ATOM 1223 C CB . TYR A 1 161 ? 4.667 20.961 15.341 1.00 27.79 ? 161 TYR A CB 1 ATOM 1224 C CG . TYR A 1 161 ? 3.412 21.032 16.182 1.00 28.83 ? 161 TYR A CG 1 ATOM 1225 C CD1 . TYR A 1 161 ? 3.417 20.573 17.488 1.00 26.73 ? 161 TYR A CD1 1 ATOM 1226 C CD2 . TYR A 1 161 ? 2.208 21.527 15.652 1.00 26.95 ? 161 TYR A CD2 1 ATOM 1227 C CE1 . TYR A 1 161 ? 2.269 20.590 18.267 1.00 28.31 ? 161 TYR A CE1 1 ATOM 1228 C CE2 . TYR A 1 161 ? 1.052 21.556 16.427 1.00 29.64 ? 161 TYR A CE2 1 ATOM 1229 C CZ . TYR A 1 161 ? 1.103 21.097 17.742 1.00 29.11 ? 161 TYR A CZ 1 ATOM 1230 O OH . TYR A 1 161 ? -0.007 21.116 18.533 1.00 30.97 ? 161 TYR A OH 1 ATOM 1231 N N . TYR A 1 162 ? 3.464 17.675 15.278 1.00 28.11 ? 162 TYR A N 1 ATOM 1232 C CA . TYR A 1 162 ? 2.245 16.886 14.994 1.00 24.55 ? 162 TYR A CA 1 ATOM 1233 C C . TYR A 1 162 ? 1.308 17.035 16.189 1.00 25.87 ? 162 TYR A C 1 ATOM 1234 O O . TYR A 1 162 ? 1.693 16.711 17.309 1.00 27.13 ? 162 TYR A O 1 ATOM 1235 C CB . TYR A 1 162 ? 2.563 15.385 14.754 1.00 22.66 ? 162 TYR A CB 1 ATOM 1236 C CG . TYR A 1 162 ? 3.200 14.990 13.426 1.00 24.09 ? 162 TYR A CG 1 ATOM 1237 C CD1 . TYR A 1 162 ? 3.306 15.887 12.342 1.00 23.03 ? 162 TYR A CD1 1 ATOM 1238 C CD2 . TYR A 1 162 ? 3.674 13.691 13.243 1.00 25.43 ? 162 TYR A CD2 1 ATOM 1239 C CE1 . TYR A 1 162 ? 3.873 15.478 11.123 1.00 24.19 ? 162 TYR A CE1 1 ATOM 1240 C CE2 . TYR A 1 162 ? 4.247 13.280 12.040 1.00 24.12 ? 162 TYR A CE2 1 ATOM 1241 C CZ . TYR A 1 162 ? 4.350 14.175 10.987 1.00 23.64 ? 162 TYR A CZ 1 ATOM 1242 O OH . TYR A 1 162 ? 4.936 13.740 9.815 1.00 25.17 ? 162 TYR A OH 1 ATOM 1243 N N . ASN A 1 163 ? 0.100 17.564 15.980 1.00 28.55 ? 163 ASN A N 1 ATOM 1244 C CA . ASN A 1 163 ? -0.908 17.683 17.077 1.00 31.16 ? 163 ASN A CA 1 ATOM 1245 C C . ASN A 1 163 ? -1.681 16.378 17.328 1.00 33.27 ? 163 ASN A C 1 ATOM 1246 O O . ASN A 1 163 ? -1.697 15.458 16.483 1.00 31.07 ? 163 ASN A O 1 ATOM 1247 C CB . ASN A 1 163 ? -1.918 18.815 16.770 1.00 31.85 ? 163 ASN A CB 1 ATOM 1248 C CG . ASN A 1 163 ? -2.683 19.332 18.030 1.00 34.69 ? 163 ASN A CG 1 ATOM 1249 O OD1 . ASN A 1 163 ? -2.545 18.810 19.139 1.00 34.83 ? 163 ASN A OD1 1 ATOM 1250 N ND2 . ASN A 1 163 ? -3.501 20.365 17.832 1.00 32.58 ? 163 ASN A ND2 1 ATOM 1251 N N . ARG A 1 164 ? -2.338 16.326 18.478 1.00 38.46 ? 164 ARG A N 1 ATOM 1252 C CA . ARG A 1 164 ? -3.297 15.283 18.813 1.00 46.89 ? 164 ARG A CA 1 ATOM 1253 C C . ARG A 1 164 ? -4.621 15.597 18.126 1.00 49.01 ? 164 ARG A C 1 ATOM 1254 O O . ARG A 1 164 ? -4.916 16.756 17.841 1.00 49.59 ? 164 ARG A O 1 ATOM 1255 C CB . ARG A 1 164 ? -3.523 15.261 20.321 1.00 48.86 ? 164 ARG A CB 1 ATOM 1256 C CG . ARG A 1 164 ? -2.317 14.804 21.148 1.00 52.01 ? 164 ARG A CG 1 ATOM 1257 C CD . ARG A 1 164 ? -2.437 15.086 22.653 1.00 52.61 ? 164 ARG A CD 1 ATOM 1258 N NE . ARG A 1 164 ? -3.511 14.319 23.295 1.00 57.61 ? 164 ARG A NE 1 ATOM 1259 C CZ . ARG A 1 164 ? -3.372 13.093 23.798 1.00 59.67 ? 164 ARG A CZ 1 ATOM 1260 N NH1 . ARG A 1 164 ? -2.195 12.473 23.728 1.00 62.11 ? 164 ARG A NH1 1 ATOM 1261 N NH2 . ARG A 1 164 ? -4.411 12.479 24.368 1.00 57.91 ? 164 ARG A NH2 1 ATOM 1262 N N . ASP A 1 165 ? -5.429 14.576 17.875 1.00 51.82 ? 165 ASP A N 1 ATOM 1263 C CA . ASP A 1 165 ? -6.667 14.781 17.132 1.00 56.02 ? 165 ASP A CA 1 ATOM 1264 C C . ASP A 1 165 ? -7.700 15.587 17.936 1.00 58.48 ? 165 ASP A C 1 ATOM 1265 O O . ASP A 1 165 ? -7.665 15.596 19.172 1.00 59.31 ? 165 ASP A O 1 ATOM 1266 C CB . ASP A 1 165 ? -7.239 13.443 16.655 1.00 57.37 ? 165 ASP A CB 1 ATOM 1267 C CG . ASP A 1 165 ? -7.865 13.538 15.275 1.00 58.63 ? 165 ASP A CG 1 ATOM 1268 O OD1 . ASP A 1 165 ? -8.453 12.527 14.843 1.00 59.51 ? 165 ASP A OD1 1 ATOM 1269 O OD2 . ASP A 1 165 ? -7.821 14.567 14.549 1.00 57.51 ? 165 ASP A OD2 1 ATOM 1270 N N . SER A 1 166 ? -8.608 16.261 17.225 1.00 61.13 ? 166 SER A N 1 ATOM 1271 C CA . SER A 1 166 ? -9.611 17.146 17.843 1.00 62.49 ? 166 SER A CA 1 ATOM 1272 C C . SER A 1 166 ? -11.037 16.571 17.823 1.00 63.44 ? 166 SER A C 1 ATOM 1273 O O . SER A 1 166 ? -11.389 15.756 16.962 1.00 64.39 ? 166 SER A O 1 ATOM 1274 C CB . SER A 1 166 ? -9.594 18.527 17.174 1.00 62.34 ? 166 SER A CB 1 ATOM 1275 O OG . SER A 1 166 ? -8.296 19.090 17.210 1.00 62.35 ? 166 SER A OG 1 ATOM 1276 N N . SER A 1 171 ? -8.433 24.132 14.858 1.00 50.46 ? 171 SER A N 1 ATOM 1277 C CA . SER A 1 171 ? -7.275 23.417 15.408 1.00 49.66 ? 171 SER A CA 1 ATOM 1278 C C . SER A 1 171 ? -6.216 23.147 14.337 1.00 46.70 ? 171 SER A C 1 ATOM 1279 O O . SER A 1 171 ? -6.538 22.666 13.252 1.00 46.11 ? 171 SER A O 1 ATOM 1280 C CB . SER A 1 171 ? -7.721 22.094 16.039 1.00 52.39 ? 171 SER A CB 1 ATOM 1281 O OG . SER A 1 171 ? -6.639 21.428 16.695 1.00 55.53 ? 171 SER A OG 1 ATOM 1282 N N . LEU A 1 172 ? -4.955 23.452 14.658 1.00 44.47 ? 172 LEU A N 1 ATOM 1283 C CA . LEU A 1 172 ? -3.816 23.186 13.781 1.00 40.47 ? 172 LEU A CA 1 ATOM 1284 C C . LEU A 1 172 ? -3.417 21.703 13.867 1.00 38.11 ? 172 LEU A C 1 ATOM 1285 O O . LEU A 1 172 ? -3.044 21.235 14.941 1.00 42.46 ? 172 LEU A O 1 ATOM 1286 C CB . LEU A 1 172 ? -2.636 24.100 14.187 1.00 39.98 ? 172 LEU A CB 1 ATOM 1287 C CG . LEU A 1 172 ? -1.305 23.987 13.433 1.00 41.11 ? 172 LEU A CG 1 ATOM 1288 C CD1 . LEU A 1 172 ? -1.416 24.524 12.004 1.00 40.98 ? 172 LEU A CD1 1 ATOM 1289 C CD2 . LEU A 1 172 ? -0.177 24.717 14.165 1.00 40.67 ? 172 LEU A CD2 1 ATOM 1290 N N . GLY A 1 173 ? -3.488 20.971 12.757 1.00 33.52 ? 173 GLY A N 1 ATOM 1291 C CA . GLY A 1 173 ? -3.081 19.543 12.724 1.00 29.84 ? 173 GLY A CA 1 ATOM 1292 C C . GLY A 1 173 ? -1.589 19.291 12.894 1.00 26.97 ? 173 GLY A C 1 ATOM 1293 O O . GLY A 1 173 ? -1.165 18.258 13.413 1.00 26.14 ? 173 GLY A O 1 ATOM 1294 N N . GLY A 1 174 ? -0.770 20.240 12.444 1.00 28.60 ? 174 GLY A N 1 ATOM 1295 C CA . GLY A 1 174 ? 0.668 20.096 12.535 1.00 26.08 ? 174 GLY A CA 1 ATOM 1296 C C . GLY A 1 174 ? 1.331 21.229 11.802 1.00 27.63 ? 174 GLY A C 1 ATOM 1297 O O . GLY A 1 174 ? 0.659 22.070 11.209 1.00 27.41 ? 174 GLY A O 1 ATOM 1298 N N . GLN A 1 175 ? 2.651 21.266 11.852 1.00 25.06 ? 175 GLN A N 1 ATOM 1299 C CA . GLN A 1 175 ? 3.387 22.273 11.111 1.00 27.75 ? 175 GLN A CA 1 ATOM 1300 C C . GLN A 1 175 ? 4.782 21.754 10.817 1.00 26.50 ? 175 GLN A C 1 ATOM 1301 O O . GLN A 1 175 ? 5.406 21.146 11.695 1.00 27.77 ? 175 GLN A O 1 ATOM 1302 C CB . GLN A 1 175 ? 3.490 23.568 11.927 1.00 29.02 ? 175 GLN A CB 1 ATOM 1303 C CG . GLN A 1 175 ? 4.245 24.686 11.224 1.00 29.11 ? 175 GLN A CG 1 ATOM 1304 C CD . GLN A 1 175 ? 4.483 25.880 12.121 1.00 30.58 ? 175 GLN A CD 1 ATOM 1305 O OE1 . GLN A 1 175 ? 5.114 25.756 13.178 1.00 31.53 ? 175 GLN A OE1 1 ATOM 1306 N NE2 . GLN A 1 175 ? 4.016 27.043 11.692 1.00 31.45 ? 175 GLN A NE2 1 ATOM 1307 N N . ILE A 1 176 ? 5.264 21.981 9.595 1.00 24.96 ? 176 ILE A N 1 ATOM 1308 C CA . ILE A 1 176 ? 6.680 21.760 9.290 1.00 26.65 ? 176 ILE A CA 1 ATOM 1309 C C . ILE A 1 176 ? 7.331 23.128 9.088 1.00 27.62 ? 176 ILE A C 1 ATOM 1310 O O . ILE A 1 176 ? 6.764 23.997 8.423 1.00 27.92 ? 176 ILE A O 1 ATOM 1311 C CB . ILE A 1 176 ? 6.911 20.787 8.068 1.00 25.47 ? 176 ILE A CB 1 ATOM 1312 C CG1 . ILE A 1 176 ? 8.413 20.666 7.741 1.00 25.98 ? 176 ILE A CG1 1 ATOM 1313 C CG2 . ILE A 1 176 ? 6.163 21.230 6.827 1.00 28.70 ? 176 ILE A CG2 1 ATOM 1314 C CD1 . ILE A 1 176 ? 8.785 19.492 6.771 1.00 28.17 ? 176 ILE A CD1 1 ATOM 1315 N N . VAL A 1 177 ? 8.487 23.340 9.707 1.00 29.88 ? 177 VAL A N 1 ATOM 1316 C CA . VAL A 1 177 ? 9.216 24.580 9.486 1.00 29.50 ? 177 VAL A CA 1 ATOM 1317 C C . VAL A 1 177 ? 10.523 24.265 8.782 1.00 30.01 ? 177 VAL A C 1 ATOM 1318 O O . VAL A 1 177 ? 11.250 23.396 9.234 1.00 31.45 ? 177 VAL A O 1 ATOM 1319 C CB . VAL A 1 177 ? 9.441 25.336 10.821 1.00 30.30 ? 177 VAL A CB 1 ATOM 1320 C CG1 . VAL A 1 177 ? 10.451 26.498 10.663 1.00 30.85 ? 177 VAL A CG1 1 ATOM 1321 C CG2 . VAL A 1 177 ? 8.109 25.821 11.377 1.00 29.78 ? 177 VAL A CG2 1 ATOM 1322 N N . LEU A 1 178 ? 10.796 24.946 7.664 1.00 30.41 ? 178 LEU A N 1 ATOM 1323 C CA . LEU A 1 178 ? 12.093 24.878 6.977 1.00 31.37 ? 178 LEU A CA 1 ATOM 1324 C C . LEU A 1 178 ? 12.972 26.037 7.442 1.00 32.29 ? 178 LEU A C 1 ATOM 1325 O O . LEU A 1 178 ? 12.557 27.198 7.396 1.00 30.32 ? 178 LEU A O 1 ATOM 1326 C CB . LEU A 1 178 ? 11.929 24.973 5.461 1.00 30.45 ? 178 LEU A CB 1 ATOM 1327 C CG . LEU A 1 178 ? 11.006 23.951 4.778 1.00 32.65 ? 178 LEU A CG 1 ATOM 1328 C CD1 . LEU A 1 178 ? 11.023 24.165 3.271 1.00 30.77 ? 178 LEU A CD1 1 ATOM 1329 C CD2 . LEU A 1 178 ? 11.399 22.493 5.161 1.00 29.38 ? 178 LEU A CD2 1 ATOM 1330 N N . GLY A 1 179 ? 14.171 25.716 7.901 1.00 31.13 ? 179 GLY A N 1 ATOM 1331 C CA . GLY A 1 179 ? 15.114 26.749 8.322 1.00 34.85 ? 179 GLY A CA 1 ATOM 1332 C C . GLY A 1 179 ? 15.156 27.072 9.800 1.00 35.62 ? 179 GLY A C 1 ATOM 1333 O O . GLY A 1 179 ? 15.848 28.012 10.225 1.00 35.34 ? 179 GLY A O 1 ATOM 1334 N N . GLY A 1 180 ? 14.433 26.299 10.604 1.00 34.17 ? 180 GLY A N 1 ATOM 1335 C CA . GLY A 1 180 ? 14.373 26.580 12.026 1.00 35.30 ? 180 GLY A CA 1 ATOM 1336 C C . GLY A 1 180 ? 13.316 25.760 12.720 1.00 36.97 ? 180 GLY A C 1 ATOM 1337 O O . GLY A 1 180 ? 12.897 24.714 12.210 1.00 34.92 ? 180 GLY A O 1 ATOM 1338 N N . SER A 1 181 ? 12.905 26.244 13.887 1.00 37.05 ? 181 SER A N 1 ATOM 1339 C CA . SER A 1 181 ? 11.843 25.654 14.698 1.00 38.36 ? 181 SER A CA 1 ATOM 1340 C C . SER A 1 181 ? 10.911 26.760 15.096 1.00 37.93 ? 181 SER A C 1 ATOM 1341 O O . SER A 1 181 ? 11.247 27.933 14.928 1.00 40.95 ? 181 SER A O 1 ATOM 1342 C CB . SER A 1 181 ? 12.429 25.037 15.953 1.00 39.93 ? 181 SER A CB 1 ATOM 1343 O OG . SER A 1 181 ? 13.311 24.005 15.580 1.00 42.66 ? 181 SER A OG 1 ATOM 1344 N N . ASP A 1 182 ? 9.741 26.393 15.615 1.00 38.55 ? 182 ASP A N 1 ATOM 1345 C CA . ASP A 1 182 ? 8.736 27.358 16.098 1.00 38.99 ? 182 ASP A CA 1 ATOM 1346 C C . ASP A 1 182 ? 8.557 27.191 17.613 1.00 39.34 ? 182 ASP A C 1 ATOM 1347 O O . ASP A 1 182 ? 7.913 26.233 18.027 1.00 39.80 ? 182 ASP A O 1 ATOM 1348 C CB . ASP A 1 182 ? 7.401 27.125 15.363 1.00 40.16 ? 182 ASP A CB 1 ATOM 1349 C CG . ASP A 1 182 ? 6.370 28.230 15.623 1.00 42.23 ? 182 ASP A CG 1 ATOM 1350 O OD1 . ASP A 1 182 ? 6.479 28.928 16.655 1.00 40.84 ? 182 ASP A OD1 1 ATOM 1351 O OD2 . ASP A 1 182 ? 5.409 28.468 14.852 1.00 41.87 ? 182 ASP A OD2 1 ATOM 1352 N N . PRO A 1 183 ? 9.103 28.105 18.439 1.00 40.67 ? 183 PRO A N 1 ATOM 1353 C CA . PRO A 1 183 ? 9.072 27.940 19.904 1.00 41.23 ? 183 PRO A CA 1 ATOM 1354 C C . PRO A 1 183 ? 7.669 27.819 20.482 1.00 41.97 ? 183 PRO A C 1 ATOM 1355 O O . PRO A 1 183 ? 7.503 27.228 21.540 1.00 43.79 ? 183 PRO A O 1 ATOM 1356 C CB . PRO A 1 183 ? 9.753 29.217 20.437 1.00 40.54 ? 183 PRO A CB 1 ATOM 1357 C CG . PRO A 1 183 ? 9.706 30.191 19.331 1.00 40.83 ? 183 PRO A CG 1 ATOM 1358 C CD . PRO A 1 183 ? 9.779 29.365 18.062 1.00 41.18 ? 183 PRO A CD 1 ATOM 1359 N N . GLN A 1 184 ? 6.673 28.367 19.788 1.00 42.27 ? 184 GLN A N 1 ATOM 1360 C CA . GLN A 1 184 ? 5.282 28.331 20.245 1.00 42.53 ? 184 GLN A CA 1 ATOM 1361 C C . GLN A 1 184 ? 4.729 26.901 20.359 1.00 42.89 ? 184 GLN A C 1 ATOM 1362 O O . GLN A 1 184 ? 3.659 26.683 20.933 1.00 41.28 ? 184 GLN A O 1 ATOM 1363 C CB . GLN A 1 184 ? 4.412 29.179 19.304 1.00 44.29 ? 184 GLN A CB 1 ATOM 1364 C CG . GLN A 1 184 ? 4.387 30.695 19.622 1.00 49.70 ? 184 GLN A CG 1 ATOM 1365 C CD . GLN A 1 184 ? 5.783 31.357 19.715 1.00 54.05 ? 184 GLN A CD 1 ATOM 1366 O OE1 . GLN A 1 184 ? 6.388 31.720 18.688 1.00 55.61 ? 184 GLN A OE1 1 ATOM 1367 N NE2 . GLN A 1 184 ? 6.274 31.543 20.948 1.00 54.18 ? 184 GLN A NE2 1 ATOM 1368 N N . HIS A 1 185 ? 5.471 25.930 19.828 1.00 42.39 ? 185 HIS A N 1 ATOM 1369 C CA . HIS A 1 185 ? 4.971 24.557 19.742 1.00 41.06 ? 185 HIS A CA 1 ATOM 1370 C C . HIS A 1 185 ? 5.747 23.532 20.535 1.00 40.63 ? 185 HIS A C 1 ATOM 1371 O O . HIS A 1 185 ? 5.451 22.343 20.452 1.00 43.26 ? 185 HIS A O 1 ATOM 1372 C CB . HIS A 1 185 ? 4.874 24.103 18.289 1.00 38.81 ? 185 HIS A CB 1 ATOM 1373 C CG . HIS A 1 185 ? 3.737 24.719 17.546 1.00 37.90 ? 185 HIS A CG 1 ATOM 1374 N ND1 . HIS A 1 185 ? 3.916 25.465 16.400 1.00 37.86 ? 185 HIS A ND1 1 ATOM 1375 C CD2 . HIS A 1 185 ? 2.407 24.705 17.785 1.00 37.91 ? 185 HIS A CD2 1 ATOM 1376 C CE1 . HIS A 1 185 ? 2.742 25.888 15.969 1.00 36.90 ? 185 HIS A CE1 1 ATOM 1377 N NE2 . HIS A 1 185 ? 1.812 25.440 16.790 1.00 37.88 ? 185 HIS A NE2 1 ATOM 1378 N N . TYR A 1 186 ? 6.750 23.981 21.272 1.00 38.44 ? 186 TYR A N 1 ATOM 1379 C CA . TYR A 1 186 ? 7.435 23.122 22.229 1.00 39.55 ? 186 TYR A CA 1 ATOM 1380 C C . TYR A 1 186 ? 7.794 23.937 23.465 1.00 41.14 ? 186 TYR A C 1 ATOM 1381 O O . TYR A 1 186 ? 7.656 25.154 23.465 1.00 38.99 ? 186 TYR A O 1 ATOM 1382 C CB . TYR A 1 186 ? 8.682 22.473 21.627 1.00 39.99 ? 186 TYR A CB 1 ATOM 1383 C CG . TYR A 1 186 ? 9.753 23.441 21.161 1.00 40.53 ? 186 TYR A CG 1 ATOM 1384 C CD1 . TYR A 1 186 ? 9.837 23.816 19.821 1.00 42.22 ? 186 TYR A CD1 1 ATOM 1385 C CD2 . TYR A 1 186 ? 10.691 23.965 22.051 1.00 41.42 ? 186 TYR A CD2 1 ATOM 1386 C CE1 . TYR A 1 186 ? 10.816 24.693 19.376 1.00 41.34 ? 186 TYR A CE1 1 ATOM 1387 C CE2 . TYR A 1 186 ? 11.677 24.852 21.615 1.00 42.50 ? 186 TYR A CE2 1 ATOM 1388 C CZ . TYR A 1 186 ? 11.733 25.208 20.274 1.00 41.28 ? 186 TYR A CZ 1 ATOM 1389 O OH . TYR A 1 186 ? 12.705 26.070 19.817 1.00 40.74 ? 186 TYR A OH 1 ATOM 1390 N N . GLU A 1 187 ? 8.230 23.259 24.515 1.00 42.30 ? 187 GLU A N 1 ATOM 1391 C CA . GLU A 1 187 ? 8.610 23.942 25.729 1.00 47.46 ? 187 GLU A CA 1 ATOM 1392 C C . GLU A 1 187 ? 9.981 23.466 26.176 1.00 46.45 ? 187 GLU A C 1 ATOM 1393 O O . GLU A 1 187 ? 10.403 22.357 25.840 1.00 47.02 ? 187 GLU A O 1 ATOM 1394 C CB . GLU A 1 187 ? 7.553 23.752 26.820 1.00 47.98 ? 187 GLU A CB 1 ATOM 1395 C CG . GLU A 1 187 ? 7.457 22.338 27.381 1.00 50.49 ? 187 GLU A CG 1 ATOM 1396 C CD . GLU A 1 187 ? 6.517 22.258 28.572 1.00 52.58 ? 187 GLU A CD 1 ATOM 1397 O OE1 . GLU A 1 187 ? 5.313 22.592 28.398 1.00 54.37 ? 187 GLU A OE1 1 ATOM 1398 O OE2 . GLU A 1 187 ? 6.981 21.857 29.676 1.00 54.38 ? 187 GLU A OE2 1 ATOM 1399 N N . GLY A 1 188 ? 10.687 24.311 26.918 1.00 45.86 ? 188 GLY A N 1 ATOM 1400 C CA . GLY A 1 188 ? 12.045 23.976 27.318 1.00 45.87 ? 188 GLY A CA 1 ATOM 1401 C C . GLY A 1 188 ? 12.993 23.961 26.135 1.00 44.81 ? 188 GLY A C 1 ATOM 1402 O O . GLY A 1 188 ? 12.791 24.669 25.145 1.00 45.27 ? 188 GLY A O 1 ATOM 1403 N N . ASN A 1 189 ? 14.036 23.149 26.223 1.00 45.55 ? 189 ASN A N 1 ATOM 1404 C CA . ASN A 1 189 ? 15.074 23.200 25.201 1.00 47.53 ? 189 ASN A CA 1 ATOM 1405 C C . ASN A 1 189 ? 15.263 21.839 24.533 1.00 46.91 ? 189 ASN A C 1 ATOM 1406 O O . ASN A 1 189 ? 14.832 20.812 25.076 1.00 45.47 ? 189 ASN A O 1 ATOM 1407 C CB . ASN A 1 189 ? 16.395 23.720 25.797 1.00 50.84 ? 189 ASN A CB 1 ATOM 1408 C CG . ASN A 1 189 ? 16.209 24.973 26.651 1.00 53.16 ? 189 ASN A CG 1 ATOM 1409 O OD1 . ASN A 1 189 ? 16.160 26.098 26.139 1.00 55.45 ? 189 ASN A OD1 1 ATOM 1410 N ND2 . ASN A 1 189 ? 16.103 24.778 27.960 1.00 53.04 ? 189 ASN A ND2 1 ATOM 1411 N N . PHE A 1 190 ? 15.890 21.839 23.360 1.00 45.15 ? 190 PHE A N 1 ATOM 1412 C CA . PHE A 1 190 ? 16.134 20.603 22.627 1.00 45.13 ? 190 PHE A CA 1 ATOM 1413 C C . PHE A 1 190 ? 17.229 19.805 23.288 1.00 45.18 ? 190 PHE A C 1 ATOM 1414 O O . PHE A 1 190 ? 18.115 20.370 23.938 1.00 44.55 ? 190 PHE A O 1 ATOM 1415 C CB . PHE A 1 190 ? 16.513 20.888 21.172 1.00 44.52 ? 190 PHE A CB 1 ATOM 1416 C CG . PHE A 1 190 ? 15.345 21.224 20.306 1.00 44.96 ? 190 PHE A CG 1 ATOM 1417 C CD1 . PHE A 1 190 ? 14.562 20.218 19.763 1.00 43.94 ? 190 PHE A CD1 1 ATOM 1418 C CD2 . PHE A 1 190 ? 15.009 22.546 20.050 1.00 46.14 ? 190 PHE A CD2 1 ATOM 1419 C CE1 . PHE A 1 190 ? 13.463 20.516 18.986 1.00 43.27 ? 190 PHE A CE1 1 ATOM 1420 C CE2 . PHE A 1 190 ? 13.908 22.849 19.259 1.00 46.02 ? 190 PHE A CE2 1 ATOM 1421 C CZ . PHE A 1 190 ? 13.138 21.827 18.729 1.00 44.81 ? 190 PHE A CZ 1 ATOM 1422 N N . HIS A 1 191 ? 17.142 18.489 23.130 1.00 43.61 ? 191 HIS A N 1 ATOM 1423 C CA . HIS A 1 191 ? 18.214 17.575 23.480 1.00 43.60 ? 191 HIS A CA 1 ATOM 1424 C C . HIS A 1 191 ? 18.555 16.850 22.201 1.00 43.53 ? 191 HIS A C 1 ATOM 1425 O O . HIS A 1 191 ? 17.654 16.361 21.507 1.00 42.01 ? 191 HIS A O 1 ATOM 1426 C CB . HIS A 1 191 ? 17.740 16.586 24.551 1.00 46.87 ? 191 HIS A CB 1 ATOM 1427 C CG . HIS A 1 191 ? 17.336 17.244 25.835 1.00 51.63 ? 191 HIS A CG 1 ATOM 1428 N ND1 . HIS A 1 191 ? 16.018 17.444 26.189 1.00 52.23 ? 191 HIS A ND1 1 ATOM 1429 C CD2 . HIS A 1 191 ? 18.079 17.778 26.836 1.00 52.63 ? 191 HIS A CD2 1 ATOM 1430 C CE1 . HIS A 1 191 ? 15.965 18.063 27.355 1.00 53.03 ? 191 HIS A CE1 1 ATOM 1431 N NE2 . HIS A 1 191 ? 17.201 18.275 27.771 1.00 54.68 ? 191 HIS A NE2 1 ATOM 1432 N N . TYR A 1 192 ? 19.842 16.777 21.877 1.00 42.07 ? 192 TYR A N 1 ATOM 1433 C CA . TYR A 1 192 ? 20.288 16.291 20.570 1.00 40.45 ? 192 TYR A CA 1 ATOM 1434 C C . TYR A 1 192 ? 20.875 14.893 20.603 1.00 40.20 ? 192 TYR A C 1 ATOM 1435 O O . TYR A 1 192 ? 21.359 14.455 21.640 1.00 44.70 ? 192 TYR A O 1 ATOM 1436 C CB . TYR A 1 192 ? 21.292 17.275 19.991 1.00 39.27 ? 192 TYR A CB 1 ATOM 1437 C CG . TYR A 1 192 ? 20.664 18.603 19.730 1.00 38.22 ? 192 TYR A CG 1 ATOM 1438 C CD1 . TYR A 1 192 ? 19.939 18.823 18.562 1.00 39.02 ? 192 TYR A CD1 1 ATOM 1439 C CD2 . TYR A 1 192 ? 20.765 19.634 20.650 1.00 37.43 ? 192 TYR A CD2 1 ATOM 1440 C CE1 . TYR A 1 192 ? 19.342 20.050 18.305 1.00 39.03 ? 192 TYR A CE1 1 ATOM 1441 C CE2 . TYR A 1 192 ? 20.181 20.869 20.404 1.00 37.22 ? 192 TYR A CE2 1 ATOM 1442 C CZ . TYR A 1 192 ? 19.467 21.069 19.234 1.00 38.68 ? 192 TYR A CZ 1 ATOM 1443 O OH . TYR A 1 192 ? 18.874 22.278 18.976 1.00 36.68 ? 192 TYR A OH 1 ATOM 1444 N N . ILE A 1 193 ? 20.792 14.177 19.484 1.00 38.60 ? 193 ILE A N 1 ATOM 1445 C CA . ILE A 1 193 ? 21.523 12.920 19.313 1.00 38.68 ? 193 ILE A CA 1 ATOM 1446 C C . ILE A 1 193 ? 22.147 12.886 17.928 1.00 39.39 ? 193 ILE A C 1 ATOM 1447 O O . ILE A 1 193 ? 21.472 13.176 16.931 1.00 40.12 ? 193 ILE A O 1 ATOM 1448 C CB . ILE A 1 193 ? 20.635 11.645 19.494 1.00 37.97 ? 193 ILE A CB 1 ATOM 1449 C CG1 . ILE A 1 193 ? 19.769 11.714 20.754 1.00 38.23 ? 193 ILE A CG1 1 ATOM 1450 C CG2 . ILE A 1 193 ? 21.520 10.399 19.540 1.00 37.02 ? 193 ILE A CG2 1 ATOM 1451 C CD1 . ILE A 1 193 ? 18.356 12.252 20.521 1.00 39.20 ? 193 ILE A CD1 1 ATOM 1452 N N . ASN A 1 194 ? 23.427 12.522 17.871 1.00 38.08 ? 194 ASN A N 1 ATOM 1453 C CA . ASN A 1 194 ? 24.139 12.353 16.620 1.00 38.80 ? 194 ASN A CA 1 ATOM 1454 C C . ASN A 1 194 ? 23.598 11.164 15.830 1.00 37.99 ? 194 ASN A C 1 ATOM 1455 O O . ASN A 1 194 ? 23.276 10.117 16.406 1.00 39.61 ? 194 ASN A O 1 ATOM 1456 C CB . ASN A 1 194 ? 25.641 12.148 16.880 1.00 39.03 ? 194 ASN A CB 1 ATOM 1457 C CG . ASN A 1 194 ? 26.411 13.465 17.009 1.00 41.95 ? 194 ASN A CG 1 ATOM 1458 O OD1 . ASN A 1 194 ? 27.644 13.474 16.976 1.00 43.44 ? 194 ASN A OD1 1 ATOM 1459 N ND2 . ASN A 1 194 ? 25.694 14.574 17.137 1.00 40.53 ? 194 ASN A ND2 1 ATOM 1460 N N . LEU A 1 195 ? 23.487 11.347 14.520 1.00 33.52 ? 195 LEU A N 1 ATOM 1461 C CA . LEU A 1 195 ? 23.212 10.259 13.588 1.00 33.57 ? 195 LEU A CA 1 ATOM 1462 C C . LEU A 1 195 ? 24.312 9.222 13.719 1.00 35.83 ? 195 LEU A C 1 ATOM 1463 O O . LEU A 1 195 ? 25.434 9.590 14.014 1.00 37.05 ? 195 LEU A O 1 ATOM 1464 C CB . LEU A 1 195 ? 23.232 10.799 12.165 1.00 29.49 ? 195 LEU A CB 1 ATOM 1465 C CG . LEU A 1 195 ? 22.189 11.873 11.880 1.00 26.96 ? 195 LEU A CG 1 ATOM 1466 C CD1 . LEU A 1 195 ? 22.210 12.165 10.396 1.00 29.35 ? 195 LEU A CD1 1 ATOM 1467 C CD2 . LEU A 1 195 ? 20.795 11.394 12.323 1.00 25.77 ? 195 LEU A CD2 1 ATOM 1468 N N . ILE A 1 196 ? 23.997 7.946 13.499 1.00 36.89 ? 196 ILE A N 1 ATOM 1469 C CA . ILE A 1 196 ? 25.022 6.898 13.493 1.00 39.91 ? 196 ILE A CA 1 ATOM 1470 C C . ILE A 1 196 ? 25.997 7.175 12.365 1.00 40.33 ? 196 ILE A C 1 ATOM 1471 O O . ILE A 1 196 ? 27.200 6.967 12.508 1.00 40.36 ? 196 ILE A O 1 ATOM 1472 C CB . ILE A 1 196 ? 24.416 5.496 13.275 1.00 40.15 ? 196 ILE A CB 1 ATOM 1473 C CG1 . ILE A 1 196 ? 23.366 5.167 14.326 1.00 39.94 ? 196 ILE A CG1 1 ATOM 1474 C CG2 . ILE A 1 196 ? 25.532 4.432 13.237 1.00 41.20 ? 196 ILE A CG2 1 ATOM 1475 C CD1 . ILE A 1 196 ? 23.776 5.525 15.724 1.00 44.67 ? 196 ILE A CD1 1 ATOM 1476 N N . LYS A 1 197 ? 25.442 7.608 11.236 1.00 40.97 ? 197 LYS A N 1 ATOM 1477 C CA . LYS A 1 197 ? 26.194 8.057 10.068 1.00 42.09 ? 197 LYS A CA 1 ATOM 1478 C C . LYS A 1 197 ? 25.251 8.873 9.194 1.00 41.56 ? 197 LYS A C 1 ATOM 1479 O O . LYS A 1 197 ? 24.038 8.602 9.161 1.00 39.93 ? 197 LYS A O 1 ATOM 1480 C CB . LYS A 1 197 ? 26.727 6.858 9.271 1.00 44.71 ? 197 LYS A CB 1 ATOM 1481 C CG . LYS A 1 197 ? 25.639 5.994 8.644 1.00 46.45 ? 197 LYS A CG 1 ATOM 1482 C CD . LYS A 1 197 ? 26.126 4.587 8.350 1.00 48.62 ? 197 LYS A CD 1 ATOM 1483 C CE . LYS A 1 197 ? 24.945 3.660 8.153 1.00 48.38 ? 197 LYS A CE 1 ATOM 1484 N NZ . LYS A 1 197 ? 24.235 4.000 6.911 1.00 49.39 ? 197 LYS A NZ 1 ATOM 1485 N N . THR A 1 198 ? 25.802 9.863 8.489 1.00 40.53 ? 198 THR A N 1 ATOM 1486 C CA . THR A 1 198 ? 25.038 10.606 7.480 1.00 42.12 ? 198 THR A CA 1 ATOM 1487 C C . THR A 1 198 ? 24.552 9.649 6.395 1.00 42.42 ? 198 THR A C 1 ATOM 1488 O O . THR A 1 198 ? 25.167 8.608 6.137 1.00 42.67 ? 198 THR A O 1 ATOM 1489 C CB . THR A 1 198 ? 25.869 11.760 6.858 1.00 43.52 ? 198 THR A CB 1 ATOM 1490 O OG1 . THR A 1 198 ? 27.028 11.230 6.197 1.00 44.20 ? 198 THR A OG1 1 ATOM 1491 C CG2 . THR A 1 198 ? 26.476 12.597 7.936 1.00 45.65 ? 198 THR A CG2 1 ATOM 1492 N N . GLY A 1 199 ? 23.444 10.004 5.762 1.00 42.13 ? 199 GLY A N 1 ATOM 1493 C CA . GLY A 1 199 ? 22.842 9.128 4.769 1.00 38.76 ? 199 GLY A CA 1 ATOM 1494 C C . GLY A 1 199 ? 21.420 8.809 5.161 1.00 36.05 ? 199 GLY A C 1 ATOM 1495 O O . GLY A 1 199 ? 20.561 8.688 4.308 1.00 36.84 ? 199 GLY A O 1 ATOM 1496 N N . VAL A 1 200 ? 21.173 8.725 6.466 1.00 36.59 ? 200 VAL A N 1 ATOM 1497 C CA . VAL A 1 200 ? 19.874 8.295 7.006 1.00 35.67 ? 200 VAL A CA 1 ATOM 1498 C C . VAL A 1 200 ? 19.566 8.987 8.356 1.00 35.04 ? 200 VAL A C 1 ATOM 1499 O O . VAL A 1 200 ? 20.477 9.281 9.142 1.00 35.86 ? 200 VAL A O 1 ATOM 1500 C CB . VAL A 1 200 ? 19.795 6.706 7.020 1.00 36.32 ? 200 VAL A CB 1 ATOM 1501 C CG1 . VAL A 1 200 ? 21.047 6.102 7.605 1.00 35.29 ? 200 VAL A CG1 1 ATOM 1502 C CG2 . VAL A 1 200 ? 18.515 6.157 7.690 1.00 34.95 ? 200 VAL A CG2 1 ATOM 1503 N N . TRP A 1 201 ? 18.294 9.286 8.610 1.00 32.63 ? 201 TRP A N 1 ATOM 1504 C CA . TRP A 1 201 ? 17.894 9.882 9.886 1.00 31.53 ? 201 TRP A CA 1 ATOM 1505 C C . TRP A 1 201 ? 17.650 8.800 10.946 1.00 33.60 ? 201 TRP A C 1 ATOM 1506 O O . TRP A 1 201 ? 16.511 8.564 11.373 1.00 35.62 ? 201 TRP A O 1 ATOM 1507 C CB . TRP A 1 201 ? 16.649 10.767 9.721 1.00 28.15 ? 201 TRP A CB 1 ATOM 1508 C CG . TRP A 1 201 ? 16.842 11.958 8.830 1.00 27.65 ? 201 TRP A CG 1 ATOM 1509 C CD1 . TRP A 1 201 ? 16.350 12.125 7.565 1.00 27.07 ? 201 TRP A CD1 1 ATOM 1510 C CD2 . TRP A 1 201 ? 17.539 13.173 9.150 1.00 26.46 ? 201 TRP A CD2 1 ATOM 1511 N NE1 . TRP A 1 201 ? 16.711 13.361 7.073 1.00 25.67 ? 201 TRP A NE1 1 ATOM 1512 C CE2 . TRP A 1 201 ? 17.442 14.026 8.022 1.00 27.21 ? 201 TRP A CE2 1 ATOM 1513 C CE3 . TRP A 1 201 ? 18.245 13.629 10.271 1.00 24.45 ? 201 TRP A CE3 1 ATOM 1514 C CZ2 . TRP A 1 201 ? 18.022 15.312 7.991 1.00 27.86 ? 201 TRP A CZ2 1 ATOM 1515 C CZ3 . TRP A 1 201 ? 18.832 14.908 10.238 1.00 25.54 ? 201 TRP A CZ3 1 ATOM 1516 C CH2 . TRP A 1 201 ? 18.712 15.734 9.112 1.00 27.05 ? 201 TRP A CH2 1 ATOM 1517 N N . GLN A 1 202 ? 18.744 8.162 11.372 1.00 34.47 ? 202 GLN A N 1 ATOM 1518 C CA . GLN A 1 202 ? 18.731 7.000 12.253 1.00 33.31 ? 202 GLN A CA 1 ATOM 1519 C C . GLN A 1 202 ? 19.735 7.253 13.368 1.00 36.24 ? 202 GLN A C 1 ATOM 1520 O O . GLN A 1 202 ? 20.868 7.682 13.103 1.00 34.29 ? 202 GLN A O 1 ATOM 1521 C CB . GLN A 1 202 ? 19.103 5.759 11.437 1.00 33.49 ? 202 GLN A CB 1 ATOM 1522 C CG . GLN A 1 202 ? 19.156 4.419 12.174 1.00 34.50 ? 202 GLN A CG 1 ATOM 1523 C CD . GLN A 1 202 ? 19.017 3.249 11.215 1.00 35.02 ? 202 GLN A CD 1 ATOM 1524 O OE1 . GLN A 1 202 ? 18.026 2.516 11.262 1.00 36.31 ? 202 GLN A OE1 1 ATOM 1525 N NE2 . GLN A 1 202 ? 19.994 3.080 10.335 1.00 34.49 ? 202 GLN A NE2 1 ATOM 1526 N N . ILE A 1 203 ? 19.306 6.993 14.608 1.00 37.37 ? 203 ILE A N 1 ATOM 1527 C CA . ILE A 1 203 ? 20.122 7.202 15.827 1.00 37.61 ? 203 ILE A CA 1 ATOM 1528 C C . ILE A 1 203 ? 20.255 5.889 16.641 1.00 39.18 ? 203 ILE A C 1 ATOM 1529 O O . ILE A 1 203 ? 19.547 4.903 16.379 1.00 35.28 ? 203 ILE A O 1 ATOM 1530 C CB . ILE A 1 203 ? 19.538 8.359 16.723 1.00 36.84 ? 203 ILE A CB 1 ATOM 1531 C CG1 . ILE A 1 203 ? 18.055 8.131 17.049 1.00 36.27 ? 203 ILE A CG1 1 ATOM 1532 C CG2 . ILE A 1 203 ? 19.737 9.728 16.077 1.00 35.57 ? 203 ILE A CG2 1 ATOM 1533 C CD1 . ILE A 1 203 ? 17.497 9.095 18.129 1.00 35.65 ? 203 ILE A CD1 1 ATOM 1534 N N . GLN A 1 204 ? 21.167 5.874 17.612 1.00 39.86 ? 204 GLN A N 1 ATOM 1535 C CA . GLN A 1 204 ? 21.268 4.743 18.534 1.00 40.78 ? 204 GLN A CA 1 ATOM 1536 C C . GLN A 1 204 ? 20.228 4.867 19.660 1.00 40.48 ? 204 GLN A C 1 ATOM 1537 O O . GLN A 1 204 ? 20.005 5.952 20.214 1.00 41.79 ? 204 GLN A O 1 ATOM 1538 C CB . GLN A 1 204 ? 22.700 4.605 19.103 1.00 42.60 ? 204 GLN A CB 1 ATOM 1539 C CG . GLN A 1 204 ? 22.977 3.305 19.883 1.00 44.85 ? 204 GLN A CG 1 ATOM 1540 C CD . GLN A 1 204 ? 23.161 2.081 18.998 1.00 49.56 ? 204 GLN A CD 1 ATOM 1541 O OE1 . GLN A 1 204 ? 23.571 2.190 17.841 1.00 53.35 ? 204 GLN A OE1 1 ATOM 1542 N NE2 . GLN A 1 204 ? 22.875 0.907 19.546 1.00 51.31 ? 204 GLN A NE2 1 ATOM 1543 N N . MET A 1 205 ? 19.579 3.750 19.971 1.00 38.86 ? 205 MET A N 1 ATOM 1544 C CA . MET A 1 205 ? 18.691 3.669 21.118 1.00 39.69 ? 205 MET A CA 1 ATOM 1545 C C . MET A 1 205 ? 19.283 2.657 22.096 1.00 39.40 ? 205 MET A C 1 ATOM 1546 O O . MET A 1 205 ? 19.708 1.564 21.701 1.00 37.85 ? 205 MET A O 1 ATOM 1547 C CB . MET A 1 205 ? 17.282 3.247 20.687 1.00 39.23 ? 205 MET A CB 1 ATOM 1548 C CG . MET A 1 205 ? 16.254 3.326 21.814 1.00 39.71 ? 205 MET A CG 1 ATOM 1549 S SD . MET A 1 205 ? 14.562 3.270 21.225 1.00 39.82 ? 205 MET A SD 1 ATOM 1550 C CE . MET A 1 205 ? 14.509 1.683 20.407 1.00 39.50 ? 205 MET A CE 1 ATOM 1551 N N . LYS A 1 206 ? 19.312 3.030 23.364 1.00 40.28 ? 206 LYS A N 1 ATOM 1552 C CA . LYS A 1 206 ? 20.036 2.243 24.369 1.00 44.46 ? 206 LYS A CA 1 ATOM 1553 C C . LYS A 1 206 ? 19.127 1.389 25.253 1.00 45.39 ? 206 LYS A C 1 ATOM 1554 O O . LYS A 1 206 ? 19.610 0.625 26.104 1.00 45.71 ? 206 LYS A O 1 ATOM 1555 C CB . LYS A 1 206 ? 20.885 3.159 25.245 1.00 44.05 ? 206 LYS A CB 1 ATOM 1556 C CG . LYS A 1 206 ? 21.811 4.044 24.466 1.00 46.97 ? 206 LYS A CG 1 ATOM 1557 C CD . LYS A 1 206 ? 22.302 5.136 25.365 1.00 49.36 ? 206 LYS A CD 1 ATOM 1558 C CE . LYS A 1 206 ? 22.995 6.198 24.582 1.00 49.93 ? 206 LYS A CE 1 ATOM 1559 N NZ . LYS A 1 206 ? 22.880 7.439 25.374 1.00 50.54 ? 206 LYS A NZ 1 ATOM 1560 N N . GLY A 1 207 ? 17.815 1.517 25.053 1.00 43.37 ? 207 GLY A N 1 ATOM 1561 C CA . GLY A 1 207 ? 16.876 0.742 25.832 1.00 40.41 ? 207 GLY A CA 1 ATOM 1562 C C . GLY A 1 207 ? 15.443 1.178 25.671 1.00 40.88 ? 207 GLY A C 1 ATOM 1563 O O . GLY A 1 207 ? 15.152 2.381 25.539 1.00 39.11 ? 207 GLY A O 1 ATOM 1564 N N . VAL A 1 208 ? 14.560 0.178 25.671 1.00 41.02 ? 208 VAL A N 1 ATOM 1565 C CA . VAL A 1 208 ? 13.119 0.388 25.803 1.00 42.97 ? 208 VAL A CA 1 ATOM 1566 C C . VAL A 1 208 ? 12.623 -0.237 27.120 1.00 43.45 ? 208 VAL A C 1 ATOM 1567 O O . VAL A 1 208 ? 12.864 -1.415 27.388 1.00 38.11 ? 208 VAL A O 1 ATOM 1568 C CB . VAL A 1 208 ? 12.317 -0.160 24.588 1.00 43.12 ? 208 VAL A CB 1 ATOM 1569 C CG1 . VAL A 1 208 ? 10.802 0.078 24.776 1.00 43.09 ? 208 VAL A CG1 1 ATOM 1570 C CG2 . VAL A 1 208 ? 12.797 0.488 23.294 1.00 42.46 ? 208 VAL A CG2 1 ATOM 1571 N N . SER A 1 209 ? 11.934 0.577 27.921 1.00 43.17 ? 209 SER A N 1 ATOM 1572 C CA . SER A 1 209 ? 11.390 0.143 29.200 1.00 47.32 ? 209 SER A CA 1 ATOM 1573 C C . SER A 1 209 ? 9.855 0.079 29.219 1.00 49.35 ? 209 SER A C 1 ATOM 1574 O O . SER A 1 209 ? 9.171 0.979 28.716 1.00 47.13 ? 209 SER A O 1 ATOM 1575 C CB . SER A 1 209 ? 11.859 1.085 30.311 1.00 47.23 ? 209 SER A CB 1 ATOM 1576 O OG . SER A 1 209 ? 13.273 1.103 30.405 1.00 49.26 ? 209 SER A OG 1 ATOM 1577 N N . VAL A 1 210 ? 9.332 -0.997 29.804 1.00 51.65 ? 210 VAL A N 1 ATOM 1578 C CA . VAL A 1 210 ? 7.939 -1.053 30.247 1.00 53.80 ? 210 VAL A CA 1 ATOM 1579 C C . VAL A 1 210 ? 7.953 -0.789 31.758 1.00 56.32 ? 210 VAL A C 1 ATOM 1580 O O . VAL A 1 210 ? 8.618 -1.502 32.515 1.00 56.35 ? 210 VAL A O 1 ATOM 1581 C CB . VAL A 1 210 ? 7.288 -2.419 29.911 1.00 53.69 ? 210 VAL A CB 1 ATOM 1582 C CG1 . VAL A 1 210 ? 6.131 -2.741 30.864 1.00 54.90 ? 210 VAL A CG1 1 ATOM 1583 C CG2 . VAL A 1 210 ? 6.823 -2.456 28.468 1.00 51.51 ? 210 VAL A CG2 1 ATOM 1584 N N . GLY A 1 211 ? 7.253 0.254 32.190 1.00 58.70 ? 211 GLY A N 1 ATOM 1585 C CA . GLY A 1 211 ? 7.304 0.676 33.594 1.00 62.00 ? 211 GLY A CA 1 ATOM 1586 C C . GLY A 1 211 ? 8.648 1.302 33.948 1.00 64.86 ? 211 GLY A C 1 ATOM 1587 O O . GLY A 1 211 ? 9.122 2.204 33.255 1.00 64.19 ? 211 GLY A O 1 ATOM 1588 N N . SER A 1 212 ? 9.270 0.822 35.023 1.00 67.16 ? 212 SER A N 1 ATOM 1589 C CA . SER A 1 212 ? 10.557 1.372 35.472 1.00 68.18 ? 212 SER A CA 1 ATOM 1590 C C . SER A 1 212 ? 11.786 0.481 35.202 1.00 67.94 ? 212 SER A C 1 ATOM 1591 O O . SER A 1 212 ? 12.918 0.922 35.398 1.00 67.21 ? 212 SER A O 1 ATOM 1592 C CB . SER A 1 212 ? 10.488 1.797 36.947 1.00 69.46 ? 212 SER A CB 1 ATOM 1593 O OG . SER A 1 212 ? 10.047 0.740 37.787 1.00 70.19 ? 212 SER A OG 1 ATOM 1594 N N . SER A 1 213 ? 11.567 -0.752 34.742 1.00 68.20 ? 213 SER A N 1 ATOM 1595 C CA . SER A 1 213 ? 12.680 -1.657 34.408 1.00 69.65 ? 213 SER A CA 1 ATOM 1596 C C . SER A 1 213 ? 12.882 -1.827 32.888 1.00 69.20 ? 213 SER A C 1 ATOM 1597 O O . SER A 1 213 ? 11.905 -1.923 32.132 1.00 69.64 ? 213 SER A O 1 ATOM 1598 C CB . SER A 1 213 ? 12.522 -3.017 35.113 1.00 70.64 ? 213 SER A CB 1 ATOM 1599 O OG . SER A 1 213 ? 11.431 -3.766 34.593 1.00 72.16 ? 213 SER A OG 1 ATOM 1600 N N . THR A 1 214 ? 14.146 -1.856 32.451 1.00 67.27 ? 214 THR A N 1 ATOM 1601 C CA . THR A 1 214 ? 14.477 -1.962 31.020 1.00 65.64 ? 214 THR A CA 1 ATOM 1602 C C . THR A 1 214 ? 14.132 -3.333 30.446 1.00 63.87 ? 214 THR A C 1 ATOM 1603 O O . THR A 1 214 ? 14.796 -4.329 30.710 1.00 64.79 ? 214 THR A O 1 ATOM 1604 C CB . THR A 1 214 ? 15.956 -1.585 30.744 1.00 66.18 ? 214 THR A CB 1 ATOM 1605 O OG1 . THR A 1 214 ? 16.253 -0.333 31.367 1.00 66.71 ? 214 THR A OG1 1 ATOM 1606 C CG2 . THR A 1 214 ? 16.174 -1.282 29.261 1.00 66.33 ? 214 THR A CG2 1 ATOM 1607 N N . LEU A 1 215 ? 13.073 -3.360 29.652 1.00 62.35 ? 215 LEU A N 1 ATOM 1608 C CA . LEU A 1 215 ? 12.534 -4.592 29.117 1.00 60.59 ? 215 LEU A CA 1 ATOM 1609 C C . LEU A 1 215 ? 13.371 -5.082 27.931 1.00 58.85 ? 215 LEU A C 1 ATOM 1610 O O . LEU A 1 215 ? 13.821 -6.231 27.915 1.00 59.04 ? 215 LEU A O 1 ATOM 1611 C CB . LEU A 1 215 ? 11.064 -4.359 28.713 1.00 60.79 ? 215 LEU A CB 1 ATOM 1612 C CG . LEU A 1 215 ? 9.982 -5.449 28.683 1.00 60.17 ? 215 LEU A CG 1 ATOM 1613 C CD1 . LEU A 1 215 ? 9.945 -6.163 27.339 1.00 60.21 ? 215 LEU A CD1 1 ATOM 1614 C CD2 . LEU A 1 215 ? 10.083 -6.442 29.852 1.00 60.20 ? 215 LEU A CD2 1 ATOM 1615 N N . LEU A 1 216 ? 13.597 -4.188 26.965 1.00 56.43 ? 216 LEU A N 1 ATOM 1616 C CA . LEU A 1 216 ? 14.162 -4.533 25.661 1.00 54.66 ? 216 LEU A CA 1 ATOM 1617 C C . LEU A 1 216 ? 15.317 -3.637 25.245 1.00 53.39 ? 216 LEU A C 1 ATOM 1618 O O . LEU A 1 216 ? 15.571 -2.591 25.863 1.00 50.78 ? 216 LEU A O 1 ATOM 1619 C CB . LEU A 1 216 ? 13.078 -4.424 24.577 1.00 55.76 ? 216 LEU A CB 1 ATOM 1620 C CG . LEU A 1 216 ? 12.034 -5.529 24.425 1.00 55.09 ? 216 LEU A CG 1 ATOM 1621 C CD1 . LEU A 1 216 ? 10.758 -4.941 23.832 1.00 56.78 ? 216 LEU A CD1 1 ATOM 1622 C CD2 . LEU A 1 216 ? 12.561 -6.688 23.583 1.00 54.15 ? 216 LEU A CD2 1 ATOM 1623 N N . CYS A 1 217 ? 15.983 -4.063 24.166 1.00 55.01 ? 217 CYS A N 1 ATOM 1624 C CA . CYS A 1 217 ? 17.062 -3.320 23.502 1.00 55.74 ? 217 CYS A CA 1 ATOM 1625 C C . CYS A 1 217 ? 18.203 -3.126 24.501 1.00 56.84 ? 217 CYS A C 1 ATOM 1626 O O . CYS A 1 217 ? 18.792 -2.046 24.624 1.00 57.20 ? 217 CYS A O 1 ATOM 1627 C CB . CYS A 1 217 ? 16.506 -2.010 22.902 1.00 55.91 ? 217 CYS A CB 1 ATOM 1628 S SG . CYS A 1 217 ? 17.642 -0.956 21.973 1.00 55.60 ? 217 CYS A SG 1 ATOM 1629 N N . GLU A 1 218 ? 18.494 -4.215 25.216 1.00 59.30 ? 218 GLU A N 1 ATOM 1630 C CA . GLU A 1 218 ? 19.480 -4.251 26.302 1.00 61.20 ? 218 GLU A CA 1 ATOM 1631 C C . GLU A 1 218 ? 20.885 -3.829 25.862 1.00 60.67 ? 218 GLU A C 1 ATOM 1632 O O . GLU A 1 218 ? 21.446 -2.868 26.392 1.00 60.14 ? 218 GLU A O 1 ATOM 1633 C CB . GLU A 1 218 ? 19.511 -5.645 26.943 1.00 63.77 ? 218 GLU A CB 1 ATOM 1634 C CG . GLU A 1 218 ? 18.316 -5.946 27.840 1.00 66.27 ? 218 GLU A CG 1 ATOM 1635 C CD . GLU A 1 218 ? 18.335 -5.135 29.126 1.00 68.22 ? 218 GLU A CD 1 ATOM 1636 O OE1 . GLU A 1 218 ? 17.445 -4.273 29.297 1.00 68.61 ? 218 GLU A OE1 1 ATOM 1637 O OE2 . GLU A 1 218 ? 19.246 -5.345 29.960 1.00 69.35 ? 218 GLU A OE2 1 ATOM 1638 N N . ASP A 1 219 ? 21.433 -4.531 24.875 1.00 60.48 ? 219 ASP A N 1 ATOM 1639 C CA . ASP A 1 219 ? 22.727 -4.166 24.306 1.00 61.07 ? 219 ASP A CA 1 ATOM 1640 C C . ASP A 1 219 ? 22.618 -3.231 23.081 1.00 58.87 ? 219 ASP A C 1 ATOM 1641 O O . ASP A 1 219 ? 23.389 -3.350 22.126 1.00 58.73 ? 219 ASP A O 1 ATOM 1642 C CB . ASP A 1 219 ? 23.557 -5.425 23.998 1.00 63.58 ? 219 ASP A CB 1 ATOM 1643 C CG . ASP A 1 219 ? 22.733 -6.533 23.378 1.00 65.45 ? 219 ASP A CG 1 ATOM 1644 O OD1 . ASP A 1 219 ? 22.414 -7.510 24.103 1.00 65.83 ? 219 ASP A OD1 1 ATOM 1645 O OD2 . ASP A 1 219 ? 22.355 -6.504 22.181 1.00 66.84 ? 219 ASP A OD2 1 ATOM 1646 N N . GLY A 1 220 ? 21.662 -2.305 23.120 1.00 56.54 ? 220 GLY A N 1 ATOM 1647 C CA . GLY A 1 220 ? 21.528 -1.285 22.076 1.00 53.40 ? 220 GLY A CA 1 ATOM 1648 C C . GLY A 1 220 ? 20.873 -1.759 20.791 1.00 52.41 ? 220 GLY A C 1 ATOM 1649 O O . GLY A 1 220 ? 20.824 -2.964 20.489 1.00 49.88 ? 220 GLY A O 1 ATOM 1650 N N . CYS A 1 221 ? 20.356 -0.789 20.038 1.00 50.27 ? 221 CYS A N 1 ATOM 1651 C CA . CYS A 1 221 ? 19.692 -1.032 18.761 1.00 48.42 ? 221 CYS A CA 1 ATOM 1652 C C . CYS A 1 221 ? 19.575 0.271 17.947 1.00 44.87 ? 221 CYS A C 1 ATOM 1653 O O . CYS A 1 221 ? 20.228 1.278 18.247 1.00 44.63 ? 221 CYS A O 1 ATOM 1654 C CB . CYS A 1 221 ? 18.312 -1.684 18.972 1.00 50.86 ? 221 CYS A CB 1 ATOM 1655 S SG . CYS A 1 221 ? 17.152 -0.744 20.008 1.00 53.38 ? 221 CYS A SG 1 ATOM 1656 N N . LEU A 1 222 ? 18.743 0.257 16.918 1.00 42.57 ? 222 LEU A N 1 ATOM 1657 C CA . LEU A 1 222 ? 18.656 1.416 16.049 1.00 38.91 ? 222 LEU A CA 1 ATOM 1658 C C . LEU A 1 222 ? 17.246 2.002 16.071 1.00 39.63 ? 222 LEU A C 1 ATOM 1659 O O . LEU A 1 222 ? 16.260 1.258 16.254 1.00 40.91 ? 222 LEU A O 1 ATOM 1660 C CB . LEU A 1 222 ? 19.121 1.051 14.641 1.00 36.29 ? 222 LEU A CB 1 ATOM 1661 C CG . LEU A 1 222 ? 20.504 0.378 14.478 1.00 38.43 ? 222 LEU A CG 1 ATOM 1662 C CD1 . LEU A 1 222 ? 20.737 -0.004 13.026 1.00 37.91 ? 222 LEU A CD1 1 ATOM 1663 C CD2 . LEU A 1 222 ? 21.665 1.236 14.986 1.00 38.80 ? 222 LEU A CD2 1 ATOM 1664 N N . ALA A 1 223 ? 17.167 3.330 15.926 1.00 35.20 ? 223 ALA A N 1 ATOM 1665 C CA . ALA A 1 223 ? 15.894 4.055 15.848 1.00 33.71 ? 223 ALA A CA 1 ATOM 1666 C C . ALA A 1 223 ? 15.880 4.974 14.632 1.00 33.52 ? 223 ALA A C 1 ATOM 1667 O O . ALA A 1 223 ? 16.617 5.963 14.577 1.00 35.25 ? 223 ALA A O 1 ATOM 1668 C CB . ALA A 1 223 ? 15.605 4.837 17.146 1.00 30.31 ? 223 ALA A CB 1 ATOM 1669 N N . LEU A 1 224 ? 15.084 4.605 13.634 1.00 28.08 ? 224 LEU A N 1 ATOM 1670 C CA . LEU A 1 224 ? 14.818 5.467 12.512 1.00 28.79 ? 224 LEU A CA 1 ATOM 1671 C C . LEU A 1 224 ? 13.754 6.479 12.949 1.00 28.85 ? 224 LEU A C 1 ATOM 1672 O O . LEU A 1 224 ? 12.752 6.099 13.541 1.00 29.68 ? 224 LEU A O 1 ATOM 1673 C CB . LEU A 1 224 ? 14.339 4.623 11.316 1.00 27.77 ? 224 LEU A CB 1 ATOM 1674 C CG . LEU A 1 224 ? 13.956 5.319 10.013 1.00 29.01 ? 224 LEU A CG 1 ATOM 1675 C CD1 . LEU A 1 224 ? 15.175 5.828 9.257 1.00 28.18 ? 224 LEU A CD1 1 ATOM 1676 C CD2 . LEU A 1 224 ? 13.143 4.358 9.125 1.00 29.82 ? 224 LEU A CD2 1 ATOM 1677 N N . VAL A 1 225 ? 13.983 7.762 12.678 1.00 27.44 ? 225 VAL A N 1 ATOM 1678 C CA . VAL A 1 225 ? 13.016 8.796 13.047 1.00 28.11 ? 225 VAL A CA 1 ATOM 1679 C C . VAL A 1 225 ? 12.286 9.177 11.755 1.00 28.02 ? 225 VAL A C 1 ATOM 1680 O O . VAL A 1 225 ? 12.811 9.920 10.928 1.00 26.73 ? 225 VAL A O 1 ATOM 1681 C CB . VAL A 1 225 ? 13.718 9.977 13.748 1.00 28.48 ? 225 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 225 ? 12.715 10.963 14.307 1.00 27.36 ? 225 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 225 ? 14.590 9.455 14.867 1.00 26.96 ? 225 VAL A CG2 1 ATOM 1684 N N . ASP A 1 226 ? 11.099 8.587 11.571 1.00 26.56 ? 226 ASP A N 1 ATOM 1685 C CA . ASP A 1 226 ? 10.392 8.568 10.294 1.00 25.72 ? 226 ASP A CA 1 ATOM 1686 C C . ASP A 1 226 ? 9.077 9.303 10.423 1.00 25.35 ? 226 ASP A C 1 ATOM 1687 O O . ASP A 1 226 ? 8.112 8.750 10.928 1.00 24.74 ? 226 ASP A O 1 ATOM 1688 C CB . ASP A 1 226 ? 10.145 7.107 9.868 1.00 29.51 ? 226 ASP A CB 1 ATOM 1689 C CG . ASP A 1 226 ? 9.504 6.971 8.486 1.00 30.17 ? 226 ASP A CG 1 ATOM 1690 O OD1 . ASP A 1 226 ? 9.224 7.987 7.794 1.00 29.03 ? 226 ASP A OD1 1 ATOM 1691 O OD2 . ASP A 1 226 ? 9.251 5.845 7.989 1.00 30.36 ? 226 ASP A OD2 1 ATOM 1692 N N . THR A 1 227 ? 9.033 10.540 9.932 1.00 24.66 ? 227 THR A N 1 ATOM 1693 C CA . THR A 1 227 ? 7.823 11.391 10.042 1.00 23.35 ? 227 THR A CA 1 ATOM 1694 C C . THR A 1 227 ? 6.702 10.844 9.167 1.00 22.12 ? 227 THR A C 1 ATOM 1695 O O . THR A 1 227 ? 5.541 11.232 9.295 1.00 22.71 ? 227 THR A O 1 ATOM 1696 C CB . THR A 1 227 ? 8.134 12.843 9.631 1.00 23.89 ? 227 THR A CB 1 ATOM 1697 O OG1 . THR A 1 227 ? 8.889 12.831 8.420 1.00 26.61 ? 227 THR A OG1 1 ATOM 1698 C CG2 . THR A 1 227 ? 9.121 13.518 10.622 1.00 22.45 ? 227 THR A CG2 1 ATOM 1699 N N . GLY A 1 228 ? 7.069 9.939 8.271 1.00 21.49 ? 228 GLY A N 1 ATOM 1700 C CA . GLY A 1 228 ? 6.127 9.382 7.326 1.00 26.16 ? 228 GLY A CA 1 ATOM 1701 C C . GLY A 1 228 ? 5.530 8.074 7.794 1.00 28.27 ? 228 GLY A C 1 ATOM 1702 O O . GLY A 1 228 ? 4.697 7.504 7.090 1.00 29.61 ? 228 GLY A O 1 ATOM 1703 N N . ALA A 1 229 ? 5.980 7.587 8.959 1.00 28.88 ? 229 ALA A N 1 ATOM 1704 C CA . ALA A 1 229 ? 5.392 6.405 9.592 1.00 26.35 ? 229 ALA A CA 1 ATOM 1705 C C . ALA A 1 229 ? 4.299 6.886 10.521 1.00 24.37 ? 229 ALA A C 1 ATOM 1706 O O . ALA A 1 229 ? 4.455 7.898 11.209 1.00 25.81 ? 229 ALA A O 1 ATOM 1707 C CB . ALA A 1 229 ? 6.435 5.626 10.371 1.00 23.92 ? 229 ALA A CB 1 ATOM 1708 N N . SER A 1 230 ? 3.175 6.171 10.519 1.00 24.50 ? 230 SER A N 1 ATOM 1709 C CA . SER A 1 230 ? 2.033 6.446 11.421 1.00 22.97 ? 230 SER A CA 1 ATOM 1710 C C . SER A 1 230 ? 2.308 6.097 12.895 1.00 24.99 ? 230 SER A C 1 ATOM 1711 O O . SER A 1 230 ? 1.885 6.814 13.812 1.00 23.28 ? 230 SER A O 1 ATOM 1712 C CB . SER A 1 230 ? 0.817 5.625 10.948 1.00 25.73 ? 230 SER A CB 1 ATOM 1713 O OG . SER A 1 230 ? 0.342 6.012 9.666 1.00 25.62 ? 230 SER A OG 1 ATOM 1714 N N . TYR A 1 231 ? 3.017 4.983 13.106 1.00 23.41 ? 231 TYR A N 1 ATOM 1715 C CA . TYR A 1 231 ? 3.193 4.373 14.421 1.00 26.83 ? 231 TYR A CA 1 ATOM 1716 C C . TYR A 1 231 ? 4.655 4.305 14.866 1.00 28.72 ? 231 TYR A C 1 ATOM 1717 O O . TYR A 1 231 ? 5.571 4.562 14.080 1.00 27.61 ? 231 TYR A O 1 ATOM 1718 C CB . TYR A 1 231 ? 2.606 2.942 14.372 1.00 28.01 ? 231 TYR A CB 1 ATOM 1719 C CG . TYR A 1 231 ? 1.191 2.927 13.825 1.00 28.75 ? 231 TYR A CG 1 ATOM 1720 C CD1 . TYR A 1 231 ? 0.184 3.642 14.467 1.00 25.18 ? 231 TYR A CD1 1 ATOM 1721 C CD2 . TYR A 1 231 ? 0.868 2.242 12.638 1.00 31.75 ? 231 TYR A CD2 1 ATOM 1722 C CE1 . TYR A 1 231 ? -1.143 3.660 13.982 1.00 27.16 ? 231 TYR A CE1 1 ATOM 1723 C CE2 . TYR A 1 231 ? -0.465 2.251 12.133 1.00 33.37 ? 231 TYR A CE2 1 ATOM 1724 C CZ . TYR A 1 231 ? -1.461 2.964 12.834 1.00 30.56 ? 231 TYR A CZ 1 ATOM 1725 O OH . TYR A 1 231 ? -2.775 3.016 12.373 1.00 32.66 ? 231 TYR A OH 1 ATOM 1726 N N . ILE A 1 232 ? 4.860 3.926 16.121 1.00 29.23 ? 232 ILE A N 1 ATOM 1727 C CA . ILE A 1 232 ? 6.129 3.334 16.543 1.00 31.26 ? 232 ILE A CA 1 ATOM 1728 C C . ILE A 1 232 ? 6.156 1.878 16.076 1.00 31.19 ? 232 ILE A C 1 ATOM 1729 O O . ILE A 1 232 ? 5.217 1.124 16.328 1.00 31.85 ? 232 ILE A O 1 ATOM 1730 C CB . ILE A 1 232 ? 6.298 3.423 18.066 1.00 31.62 ? 232 ILE A CB 1 ATOM 1731 C CG1 . ILE A 1 232 ? 6.344 4.888 18.512 1.00 30.87 ? 232 ILE A CG1 1 ATOM 1732 C CG2 . ILE A 1 232 ? 7.620 2.784 18.508 1.00 34.01 ? 232 ILE A CG2 1 ATOM 1733 C CD1 . ILE A 1 232 ? 6.183 5.060 20.008 1.00 29.30 ? 232 ILE A CD1 1 ATOM 1734 N N . SER A 1 233 ? 7.220 1.493 15.379 1.00 31.56 ? 233 SER A N 1 ATOM 1735 C CA . SER A 1 233 ? 7.437 0.097 14.989 1.00 32.11 ? 233 SER A CA 1 ATOM 1736 C C . SER A 1 233 ? 8.758 -0.485 15.492 1.00 33.30 ? 233 SER A C 1 ATOM 1737 O O . SER A 1 233 ? 9.764 0.227 15.643 1.00 30.40 ? 233 SER A O 1 ATOM 1738 C CB . SER A 1 233 ? 7.312 -0.100 13.466 1.00 33.22 ? 233 SER A CB 1 ATOM 1739 O OG . SER A 1 233 ? 8.397 0.476 12.753 1.00 33.09 ? 233 SER A OG 1 ATOM 1740 N N . GLY A 1 234 ? 8.718 -1.789 15.755 1.00 32.52 ? 234 GLY A N 1 ATOM 1741 C CA . GLY A 1 234 ? 9.890 -2.581 16.067 1.00 29.33 ? 234 GLY A CA 1 ATOM 1742 C C . GLY A 1 234 ? 9.796 -3.878 15.294 1.00 30.69 ? 234 GLY A C 1 ATOM 1743 O O . GLY A 1 234 ? 8.781 -4.148 14.640 1.00 28.59 ? 234 GLY A O 1 ATOM 1744 N N . SER A 1 235 ? 10.851 -4.691 15.378 1.00 30.35 ? 235 SER A N 1 ATOM 1745 C CA . SER A 1 235 ? 10.893 -5.976 14.700 1.00 32.71 ? 235 SER A CA 1 ATOM 1746 C C . SER A 1 235 ? 9.776 -6.843 15.250 1.00 32.06 ? 235 SER A C 1 ATOM 1747 O O . SER A 1 235 ? 9.371 -6.670 16.381 1.00 30.30 ? 235 SER A O 1 ATOM 1748 C CB . SER A 1 235 ? 12.227 -6.660 14.987 1.00 35.46 ? 235 SER A CB 1 ATOM 1749 O OG . SER A 1 235 ? 12.320 -6.981 16.378 1.00 37.20 ? 235 SER A OG 1 ATOM 1750 N N . THR A 1 236 ? 9.282 -7.772 14.439 1.00 36.02 ? 236 THR A N 1 ATOM 1751 C CA . THR A 1 236 ? 8.275 -8.736 14.880 1.00 37.13 ? 236 THR A CA 1 ATOM 1752 C C . THR A 1 236 ? 8.588 -9.372 16.247 1.00 37.69 ? 236 THR A C 1 ATOM 1753 O O . THR A 1 236 ? 7.680 -9.527 17.076 1.00 37.48 ? 236 THR A O 1 ATOM 1754 C CB . THR A 1 236 ? 8.055 -9.784 13.778 1.00 37.21 ? 236 THR A CB 1 ATOM 1755 O OG1 . THR A 1 236 ? 7.373 -9.149 12.691 1.00 40.36 ? 236 THR A OG1 1 ATOM 1756 C CG2 . THR A 1 236 ? 7.062 -10.865 14.199 1.00 37.42 ? 236 THR A CG2 1 ATOM 1757 N N . SER A 1 237 ? 9.856 -9.700 16.504 1.00 38.61 ? 237 SER A N 1 ATOM 1758 C CA . SER A 1 237 ? 10.217 -10.359 17.766 1.00 39.92 ? 237 SER A CA 1 ATOM 1759 C C . SER A 1 237 ? 10.301 -9.441 18.986 1.00 41.72 ? 237 SER A C 1 ATOM 1760 O O . SER A 1 237 ? 9.966 -9.869 20.092 1.00 44.15 ? 237 SER A O 1 ATOM 1761 C CB . SER A 1 237 ? 11.473 -11.232 17.627 1.00 41.01 ? 237 SER A CB 1 ATOM 1762 O OG . SER A 1 237 ? 12.653 -10.457 17.608 1.00 41.19 ? 237 SER A OG 1 ATOM 1763 N N . SER A 1 238 ? 10.735 -8.189 18.797 1.00 40.73 ? 238 SER A N 1 ATOM 1764 C CA . SER A 1 238 ? 10.679 -7.154 19.868 1.00 38.37 ? 238 SER A CA 1 ATOM 1765 C C . SER A 1 238 ? 9.258 -6.699 20.204 1.00 37.82 ? 238 SER A C 1 ATOM 1766 O O . SER A 1 238 ? 8.936 -6.414 21.365 1.00 38.33 ? 238 SER A O 1 ATOM 1767 C CB . SER A 1 238 ? 11.448 -5.905 19.461 1.00 38.50 ? 238 SER A CB 1 ATOM 1768 O OG . SER A 1 238 ? 12.715 -6.233 18.947 1.00 45.18 ? 238 SER A OG 1 ATOM 1769 N N . ILE A 1 239 ? 8.424 -6.586 19.177 1.00 37.68 ? 239 ILE A N 1 ATOM 1770 C CA . ILE A 1 239 ? 7.042 -6.202 19.385 1.00 39.21 ? 239 ILE A CA 1 ATOM 1771 C C . ILE A 1 239 ? 6.262 -7.296 20.120 1.00 41.39 ? 239 ILE A C 1 ATOM 1772 O O . ILE A 1 239 ? 5.455 -6.967 20.989 1.00 39.50 ? 239 ILE A O 1 ATOM 1773 C CB . ILE A 1 239 ? 6.364 -5.742 18.064 1.00 36.32 ? 239 ILE A CB 1 ATOM 1774 C CG1 . ILE A 1 239 ? 6.952 -4.401 17.605 1.00 33.65 ? 239 ILE A CG1 1 ATOM 1775 C CG2 . ILE A 1 239 ? 4.854 -5.637 18.231 1.00 37.17 ? 239 ILE A CG2 1 ATOM 1776 C CD1 . ILE A 1 239 ? 7.113 -3.332 18.708 1.00 30.41 ? 239 ILE A CD1 1 ATOM 1777 N N . GLU A 1 240 ? 6.529 -8.572 19.801 1.00 44.08 ? 240 GLU A N 1 ATOM 1778 C CA . GLU A 1 240 ? 5.933 -9.701 20.539 1.00 47.53 ? 240 GLU A CA 1 ATOM 1779 C C . GLU A 1 240 ? 6.170 -9.561 22.043 1.00 47.16 ? 240 GLU A C 1 ATOM 1780 O O . GLU A 1 240 ? 5.237 -9.696 22.839 1.00 45.70 ? 240 GLU A O 1 ATOM 1781 C CB . GLU A 1 240 ? 6.507 -11.046 20.074 1.00 48.97 ? 240 GLU A CB 1 ATOM 1782 C CG . GLU A 1 240 ? 5.899 -11.639 18.807 1.00 52.02 ? 240 GLU A CG 1 ATOM 1783 C CD . GLU A 1 240 ? 6.503 -13.006 18.441 1.00 53.29 ? 240 GLU A CD 1 ATOM 1784 O OE1 . GLU A 1 240 ? 7.693 -13.076 18.033 1.00 54.86 ? 240 GLU A OE1 1 ATOM 1785 O OE2 . GLU A 1 240 ? 5.781 -14.026 18.554 1.00 55.83 ? 240 GLU A OE2 1 ATOM 1786 N N . LYS A 1 241 ? 7.423 -9.285 22.414 1.00 47.24 ? 241 LYS A N 1 ATOM 1787 C CA . LYS A 1 241 ? 7.832 -9.146 23.812 1.00 46.80 ? 241 LYS A CA 1 ATOM 1788 C C . LYS A 1 241 ? 7.241 -7.912 24.477 1.00 45.01 ? 241 LYS A C 1 ATOM 1789 O O . LYS A 1 241 ? 6.836 -7.986 25.635 1.00 45.18 ? 241 LYS A O 1 ATOM 1790 C CB . LYS A 1 241 ? 9.364 -9.135 23.960 1.00 47.33 ? 241 LYS A CB 1 ATOM 1791 C CG . LYS A 1 241 ? 10.043 -10.471 23.619 1.00 49.74 ? 241 LYS A CG 1 ATOM 1792 C CD . LYS A 1 241 ? 11.577 -10.364 23.557 1.00 49.84 ? 241 LYS A CD 1 ATOM 1793 C CE . LYS A 1 241 ? 12.218 -10.361 24.947 1.00 52.82 ? 241 LYS A CE 1 ATOM 1794 N NZ . LYS A 1 241 ? 13.596 -9.769 24.938 1.00 53.69 ? 241 LYS A NZ 1 ATOM 1795 N N . LEU A 1 242 ? 7.205 -6.781 23.769 1.00 42.59 ? 242 LEU A N 1 ATOM 1796 C CA . LEU A 1 242 ? 6.545 -5.564 24.288 1.00 41.79 ? 242 LEU A CA 1 ATOM 1797 C C . LEU A 1 242 ? 5.055 -5.808 24.595 1.00 42.37 ? 242 LEU A C 1 ATOM 1798 O O . LEU A 1 242 ? 4.549 -5.378 25.625 1.00 43.70 ? 242 LEU A O 1 ATOM 1799 C CB . LEU A 1 242 ? 6.697 -4.406 23.296 1.00 41.14 ? 242 LEU A CB 1 ATOM 1800 C CG . LEU A 1 242 ? 6.073 -3.042 23.609 1.00 41.75 ? 242 LEU A CG 1 ATOM 1801 C CD1 . LEU A 1 242 ? 6.660 -2.441 24.872 1.00 41.55 ? 242 LEU A CD1 1 ATOM 1802 C CD2 . LEU A 1 242 ? 6.291 -2.079 22.451 1.00 39.92 ? 242 LEU A CD2 1 ATOM 1803 N N . MET A 1 243 ? 4.380 -6.522 23.695 1.00 44.06 ? 243 MET A N 1 ATOM 1804 C CA . MET A 1 243 ? 2.948 -6.775 23.770 1.00 44.30 ? 243 MET A CA 1 ATOM 1805 C C . MET A 1 243 ? 2.575 -7.882 24.756 1.00 48.02 ? 243 MET A C 1 ATOM 1806 O O . MET A 1 243 ? 1.464 -7.884 25.287 1.00 48.84 ? 243 MET A O 1 ATOM 1807 C CB . MET A 1 243 ? 2.406 -7.119 22.387 1.00 42.83 ? 243 MET A CB 1 ATOM 1808 C CG . MET A 1 243 ? 2.567 -5.999 21.359 1.00 42.87 ? 243 MET A CG 1 ATOM 1809 S SD . MET A 1 243 ? 1.579 -4.560 21.762 1.00 43.50 ? 243 MET A SD 1 ATOM 1810 C CE . MET A 1 243 ? 2.001 -3.481 20.392 1.00 40.65 ? 243 MET A CE 1 ATOM 1811 N N . GLU A 1 244 ? 3.481 -8.838 24.962 1.00 48.44 ? 244 GLU A N 1 ATOM 1812 C CA . GLU A 1 244 ? 3.381 -9.784 26.078 1.00 49.24 ? 244 GLU A CA 1 ATOM 1813 C C . GLU A 1 244 ? 3.389 -8.977 27.396 1.00 49.01 ? 244 GLU A C 1 ATOM 1814 O O . GLU A 1 244 ? 2.495 -9.135 28.241 1.00 49.24 ? 244 GLU A O 1 ATOM 1815 C CB . GLU A 1 244 ? 4.552 -10.780 26.033 1.00 50.94 ? 244 GLU A CB 1 ATOM 1816 C CG . GLU A 1 244 ? 4.336 -12.100 26.776 1.00 54.43 ? 244 GLU A CG 1 ATOM 1817 C CD . GLU A 1 244 ? 4.124 -11.920 28.276 1.00 57.85 ? 244 GLU A CD 1 ATOM 1818 O OE1 . GLU A 1 244 ? 3.073 -12.402 28.803 1.00 58.42 ? 244 GLU A OE1 1 ATOM 1819 O OE2 . GLU A 1 244 ? 4.997 -11.280 28.926 1.00 57.25 ? 244 GLU A OE2 1 ATOM 1820 N N . ALA A 1 245 ? 4.386 -8.098 27.533 1.00 47.30 ? 245 ALA A N 1 ATOM 1821 C CA . ALA A 1 245 ? 4.564 -7.234 28.701 1.00 46.54 ? 245 ALA A CA 1 ATOM 1822 C C . ALA A 1 245 ? 3.411 -6.257 28.957 1.00 47.46 ? 245 ALA A C 1 ATOM 1823 O O . ALA A 1 245 ? 3.144 -5.906 30.111 1.00 45.90 ? 245 ALA A O 1 ATOM 1824 C CB . ALA A 1 245 ? 5.879 -6.481 28.594 1.00 46.27 ? 245 ALA A CB 1 ATOM 1825 N N . LEU A 1 246 ? 2.750 -5.811 27.887 1.00 48.51 ? 246 LEU A N 1 ATOM 1826 C CA . LEU A 1 246 ? 1.577 -4.920 27.993 1.00 49.31 ? 246 LEU A CA 1 ATOM 1827 C C . LEU A 1 246 ? 0.264 -5.686 28.151 1.00 50.74 ? 246 LEU A C 1 ATOM 1828 O O . LEU A 1 246 ? -0.780 -5.088 28.454 1.00 52.44 ? 246 LEU A O 1 ATOM 1829 C CB . LEU A 1 246 ? 1.487 -3.977 26.781 1.00 46.07 ? 246 LEU A CB 1 ATOM 1830 C CG . LEU A 1 246 ? 2.641 -2.978 26.638 1.00 43.17 ? 246 LEU A CG 1 ATOM 1831 C CD1 . LEU A 1 246 ? 2.435 -2.111 25.401 1.00 43.36 ? 246 LEU A CD1 1 ATOM 1832 C CD2 . LEU A 1 246 ? 2.785 -2.129 27.893 1.00 38.85 ? 246 LEU A CD2 1 ATOM 1833 N N . GLY A 1 247 ? 0.326 -7.001 27.943 1.00 50.33 ? 247 GLY A N 1 ATOM 1834 C CA . GLY A 1 247 ? -0.860 -7.851 27.940 1.00 50.47 ? 247 GLY A CA 1 ATOM 1835 C C . GLY A 1 247 ? -1.813 -7.646 26.765 1.00 50.53 ? 247 GLY A C 1 ATOM 1836 O O . GLY A 1 247 ? -3.024 -7.837 26.908 1.00 50.05 ? 247 GLY A O 1 ATOM 1837 N N . ALA A 1 248 ? -1.268 -7.289 25.600 1.00 49.12 ? 248 ALA A N 1 ATOM 1838 C CA . ALA A 1 248 ? -2.068 -7.004 24.405 1.00 48.62 ? 248 ALA A CA 1 ATOM 1839 C C . ALA A 1 248 ? -2.180 -8.223 23.487 1.00 50.17 ? 248 ALA A C 1 ATOM 1840 O O . ALA A 1 248 ? -1.278 -9.069 23.460 1.00 50.38 ? 248 ALA A O 1 ATOM 1841 C CB . ALA A 1 248 ? -1.482 -5.819 23.647 1.00 46.48 ? 248 ALA A CB 1 ATOM 1842 N N . LYS A 1 249 ? -3.283 -8.299 22.738 1.00 50.62 ? 249 LYS A N 1 ATOM 1843 C CA . LYS A 1 249 ? -3.582 -9.440 21.875 1.00 53.11 ? 249 LYS A CA 1 ATOM 1844 C C . LYS A 1 249 ? -3.321 -9.125 20.409 1.00 53.84 ? 249 LYS A C 1 ATOM 1845 O O . LYS A 1 249 ? -3.728 -8.076 19.901 1.00 51.81 ? 249 LYS A O 1 ATOM 1846 C CB . LYS A 1 249 ? -5.045 -9.881 22.027 1.00 55.43 ? 249 LYS A CB 1 ATOM 1847 C CG . LYS A 1 249 ? -5.381 -10.693 23.271 1.00 57.07 ? 249 LYS A CG 1 ATOM 1848 C CD . LYS A 1 249 ? -6.730 -11.389 23.061 1.00 58.02 ? 249 LYS A CD 1 ATOM 1849 C CE . LYS A 1 249 ? -7.152 -12.300 24.222 1.00 57.64 ? 249 LYS A CE 1 ATOM 1850 N NZ . LYS A 1 249 ? -8.578 -12.767 24.033 1.00 56.42 ? 249 LYS A NZ 1 ATOM 1851 N N . LYS A 1 250 ? -2.652 -10.061 19.741 1.00 54.80 ? 250 LYS A N 1 ATOM 1852 C CA . LYS A 1 250 ? -2.338 -9.974 18.320 1.00 55.37 ? 250 LYS A CA 1 ATOM 1853 C C . LYS A 1 250 ? -3.570 -10.181 17.449 1.00 55.49 ? 250 LYS A C 1 ATOM 1854 O O . LYS A 1 250 ? -4.155 -11.270 17.422 1.00 56.70 ? 250 LYS A O 1 ATOM 1855 C CB . LYS A 1 250 ? -1.259 -11.018 17.963 1.00 56.96 ? 250 LYS A CB 1 ATOM 1856 C CG . LYS A 1 250 ? -0.963 -11.197 16.471 1.00 58.52 ? 250 LYS A CG 1 ATOM 1857 C CD . LYS A 1 250 ? 0.073 -10.201 15.974 1.00 61.09 ? 250 LYS A CD 1 ATOM 1858 C CE . LYS A 1 250 ? 0.263 -10.263 14.462 1.00 62.65 ? 250 LYS A CE 1 ATOM 1859 N NZ . LYS A 1 250 ? 0.617 -11.626 13.977 1.00 62.19 ? 250 LYS A NZ 1 ATOM 1860 N N . ARG A 1 251 ? -3.960 -9.133 16.741 1.00 55.00 ? 251 ARG A N 1 ATOM 1861 C CA . ARG A 1 251 ? -4.902 -9.285 15.642 1.00 57.88 ? 251 ARG A CA 1 ATOM 1862 C C . ARG A 1 251 ? -4.102 -9.437 14.329 1.00 59.38 ? 251 ARG A C 1 ATOM 1863 O O . ARG A 1 251 ? -2.872 -9.578 14.369 1.00 60.03 ? 251 ARG A O 1 ATOM 1864 C CB . ARG A 1 251 ? -5.917 -8.132 15.607 1.00 56.86 ? 251 ARG A CB 1 ATOM 1865 C CG . ARG A 1 251 ? -6.981 -8.191 16.716 1.00 55.55 ? 251 ARG A CG 1 ATOM 1866 C CD . ARG A 1 251 ? -8.415 -8.176 16.180 1.00 56.20 ? 251 ARG A CD 1 ATOM 1867 N NE . ARG A 1 251 ? -9.201 -6.956 16.426 1.00 56.06 ? 251 ARG A NE 1 ATOM 1868 C CZ . ARG A 1 251 ? -8.983 -5.758 15.873 1.00 55.94 ? 251 ARG A CZ 1 ATOM 1869 N NH1 . ARG A 1 251 ? -7.962 -5.561 15.054 1.00 55.05 ? 251 ARG A NH1 1 ATOM 1870 N NH2 . ARG A 1 251 ? -9.781 -4.740 16.164 1.00 54.94 ? 251 ARG A NH2 1 ATOM 1871 N N . LEU A 1 252 ? -4.777 -9.426 13.178 1.00 60.48 ? 252 LEU A N 1 ATOM 1872 C CA . LEU A 1 252 ? -4.095 -9.722 11.908 1.00 62.14 ? 252 LEU A CA 1 ATOM 1873 C C . LEU A 1 252 ? -3.200 -8.578 11.408 1.00 61.32 ? 252 LEU A C 1 ATOM 1874 O O . LEU A 1 252 ? -2.147 -8.827 10.813 1.00 61.40 ? 252 LEU A O 1 ATOM 1875 C CB . LEU A 1 252 ? -5.092 -10.174 10.822 1.00 63.10 ? 252 LEU A CB 1 ATOM 1876 C CG . LEU A 1 252 ? -4.559 -11.100 9.708 1.00 63.57 ? 252 LEU A CG 1 ATOM 1877 C CD1 . LEU A 1 252 ? -4.288 -12.534 10.208 1.00 63.71 ? 252 LEU A CD1 1 ATOM 1878 C CD2 . LEU A 1 252 ? -5.509 -11.127 8.524 1.00 63.48 ? 252 LEU A CD2 1 ATOM 1879 N N . PHE A 1 253 ? -3.617 -7.336 11.661 1.00 60.23 ? 253 PHE A N 1 ATOM 1880 C CA . PHE A 1 253 ? -2.865 -6.161 11.208 1.00 59.20 ? 253 PHE A CA 1 ATOM 1881 C C . PHE A 1 253 ? -2.604 -5.138 12.325 1.00 57.23 ? 253 PHE A C 1 ATOM 1882 O O . PHE A 1 253 ? -2.201 -4.000 12.045 1.00 56.55 ? 253 PHE A O 1 ATOM 1883 C CB . PHE A 1 253 ? -3.554 -5.503 9.993 1.00 60.39 ? 253 PHE A CB 1 ATOM 1884 C CG . PHE A 1 253 ? -3.751 -6.441 8.819 1.00 61.42 ? 253 PHE A CG 1 ATOM 1885 C CD1 . PHE A 1 253 ? -2.650 -7.018 8.172 1.00 61.57 ? 253 PHE A CD1 1 ATOM 1886 C CD2 . PHE A 1 253 ? -5.040 -6.753 8.365 1.00 61.70 ? 253 PHE A CD2 1 ATOM 1887 C CE1 . PHE A 1 253 ? -2.829 -7.900 7.100 1.00 61.16 ? 253 PHE A CE1 1 ATOM 1888 C CE2 . PHE A 1 253 ? -5.230 -7.634 7.295 1.00 60.20 ? 253 PHE A CE2 1 ATOM 1889 C CZ . PHE A 1 253 ? -4.123 -8.205 6.662 1.00 60.49 ? 253 PHE A CZ 1 ATOM 1890 N N . ASP A 1 254 ? -2.825 -5.551 13.577 1.00 55.53 ? 254 ASP A N 1 ATOM 1891 C CA . ASP A 1 254 ? -2.624 -4.687 14.758 1.00 54.61 ? 254 ASP A CA 1 ATOM 1892 C C . ASP A 1 254 ? -2.602 -5.456 16.085 1.00 52.37 ? 254 ASP A C 1 ATOM 1893 O O . ASP A 1 254 ? -2.772 -6.682 16.105 1.00 51.93 ? 254 ASP A O 1 ATOM 1894 C CB . ASP A 1 254 ? -3.690 -3.577 14.813 1.00 56.96 ? 254 ASP A CB 1 ATOM 1895 C CG . ASP A 1 254 ? -5.076 -4.107 15.112 1.00 58.31 ? 254 ASP A CG 1 ATOM 1896 O OD1 . ASP A 1 254 ? -5.238 -5.334 15.273 1.00 59.20 ? 254 ASP A OD1 1 ATOM 1897 O OD2 . ASP A 1 254 ? -6.075 -3.370 15.210 1.00 60.23 ? 254 ASP A OD2 1 ATOM 1898 N N . TYR A 1 255 ? -2.385 -4.728 17.183 1.00 48.33 ? 255 TYR A N 1 ATOM 1899 C CA . TYR A 1 255 ? -2.506 -5.277 18.534 1.00 45.92 ? 255 TYR A CA 1 ATOM 1900 C C . TYR A 1 255 ? -3.601 -4.560 19.302 1.00 43.02 ? 255 TYR A C 1 ATOM 1901 O O . TYR A 1 255 ? -3.788 -3.361 19.131 1.00 42.92 ? 255 TYR A O 1 ATOM 1902 C CB . TYR A 1 255 ? -1.189 -5.142 19.296 1.00 48.41 ? 255 TYR A CB 1 ATOM 1903 C CG . TYR A 1 255 ? -0.189 -6.221 18.961 1.00 49.12 ? 255 TYR A CG 1 ATOM 1904 C CD1 . TYR A 1 255 ? -0.181 -7.427 19.655 1.00 50.11 ? 255 TYR A CD1 1 ATOM 1905 C CD2 . TYR A 1 255 ? 0.743 -6.037 17.943 1.00 48.24 ? 255 TYR A CD2 1 ATOM 1906 C CE1 . TYR A 1 255 ? 0.741 -8.428 19.344 1.00 50.24 ? 255 TYR A CE1 1 ATOM 1907 C CE2 . TYR A 1 255 ? 1.659 -7.024 17.626 1.00 49.09 ? 255 TYR A CE2 1 ATOM 1908 C CZ . TYR A 1 255 ? 1.654 -8.214 18.331 1.00 49.50 ? 255 TYR A CZ 1 ATOM 1909 O OH . TYR A 1 255 ? 2.564 -9.197 18.015 1.00 50.42 ? 255 TYR A OH 1 ATOM 1910 N N . VAL A 1 256 ? -4.315 -5.295 20.152 1.00 41.36 ? 256 VAL A N 1 ATOM 1911 C CA . VAL A 1 256 ? -5.462 -4.743 20.894 1.00 39.25 ? 256 VAL A CA 1 ATOM 1912 C C . VAL A 1 256 ? -5.463 -5.101 22.374 1.00 40.70 ? 256 VAL A C 1 ATOM 1913 O O . VAL A 1 256 ? -4.943 -6.141 22.774 1.00 41.38 ? 256 VAL A O 1 ATOM 1914 C CB . VAL A 1 256 ? -6.828 -5.213 20.293 1.00 39.71 ? 256 VAL A CB 1 ATOM 1915 C CG1 . VAL A 1 256 ? -7.039 -4.656 18.895 1.00 38.45 ? 256 VAL A CG1 1 ATOM 1916 C CG2 . VAL A 1 256 ? -6.939 -6.741 20.282 1.00 39.47 ? 256 VAL A CG2 1 ATOM 1917 N N . VAL A 1 257 ? -6.079 -4.237 23.181 1.00 39.37 ? 257 VAL A N 1 ATOM 1918 C CA . VAL A 1 257 ? -6.371 -4.511 24.593 1.00 38.83 ? 257 VAL A CA 1 ATOM 1919 C C . VAL A 1 257 ? -7.868 -4.267 24.847 1.00 39.23 ? 257 VAL A C 1 ATOM 1920 O O . VAL A 1 257 ? -8.504 -3.533 24.085 1.00 38.07 ? 257 VAL A O 1 ATOM 1921 C CB . VAL A 1 257 ? -5.525 -3.626 25.544 1.00 37.50 ? 257 VAL A CB 1 ATOM 1922 C CG1 . VAL A 1 257 ? -4.035 -3.910 25.367 1.00 38.75 ? 257 VAL A CG1 1 ATOM 1923 C CG2 . VAL A 1 257 ? -5.818 -2.137 25.333 1.00 35.94 ? 257 VAL A CG2 1 ATOM 1924 N N . LYS A 1 258 ? -8.440 -4.887 25.882 1.00 40.44 ? 258 LYS A N 1 ATOM 1925 C CA . LYS A 1 258 ? -9.823 -4.569 26.279 1.00 41.94 ? 258 LYS A CA 1 ATOM 1926 C C . LYS A 1 258 ? -9.808 -3.093 26.649 1.00 39.65 ? 258 LYS A C 1 ATOM 1927 O O . LYS A 1 258 ? -8.883 -2.633 27.309 1.00 39.02 ? 258 LYS A O 1 ATOM 1928 C CB . LYS A 1 258 ? -10.302 -5.418 27.470 1.00 44.32 ? 258 LYS A CB 1 ATOM 1929 C CG . LYS A 1 258 ? -10.543 -6.899 27.176 1.00 46.78 ? 258 LYS A CG 1 ATOM 1930 C CD . LYS A 1 258 ? -11.051 -7.645 28.440 1.00 47.17 ? 258 LYS A CD 1 ATOM 1931 C CE . LYS A 1 258 ? -11.430 -9.129 28.166 1.00 49.31 ? 258 LYS A CE 1 ATOM 1932 N NZ . LYS A 1 258 ? -10.488 -10.138 28.790 1.00 48.97 ? 258 LYS A NZ 1 ATOM 1933 N N . CYS A 1 259 ? -10.805 -2.342 26.199 1.00 39.65 ? 259 CYS A N 1 ATOM 1934 C CA . CYS A 1 259 ? -10.757 -0.876 26.307 1.00 38.39 ? 259 CYS A CA 1 ATOM 1935 C C . CYS A 1 259 ? -10.609 -0.301 27.714 1.00 38.93 ? 259 CYS A C 1 ATOM 1936 O O . CYS A 1 259 ? -10.016 0.785 27.894 1.00 37.22 ? 259 CYS A O 1 ATOM 1937 C CB . CYS A 1 259 ? -11.937 -0.249 25.591 1.00 36.18 ? 259 CYS A CB 1 ATOM 1938 S SG . CYS A 1 259 ? -11.690 -0.346 23.819 1.00 38.81 ? 259 CYS A SG 1 ATOM 1939 N N . ASN A 1 260 ? -11.134 -1.033 28.695 1.00 36.68 ? 260 ASN A N 1 ATOM 1940 C CA . ASN A 1 260 ? -11.127 -0.599 30.092 1.00 38.66 ? 260 ASN A CA 1 ATOM 1941 C C . ASN A 1 260 ? -9.762 -0.805 30.770 1.00 39.25 ? 260 ASN A C 1 ATOM 1942 O O . ASN A 1 260 ? -9.471 -0.207 31.821 1.00 38.43 ? 260 ASN A O 1 ATOM 1943 C CB . ASN A 1 260 ? -12.247 -1.314 30.873 1.00 39.88 ? 260 ASN A CB 1 ATOM 1944 C CG . ASN A 1 260 ? -11.909 -2.754 31.190 1.00 40.14 ? 260 ASN A CG 1 ATOM 1945 O OD1 . ASN A 1 260 ? -11.488 -3.517 30.325 1.00 41.90 ? 260 ASN A OD1 1 ATOM 1946 N ND2 . ASN A 1 260 ? -12.089 -3.132 32.446 1.00 43.01 ? 260 ASN A ND2 1 ATOM 1947 N N . GLU A 1 261 ? -8.929 -1.649 30.155 1.00 39.26 ? 261 GLU A N 1 ATOM 1948 C CA . GLU A 1 261 ? -7.533 -1.828 30.574 1.00 39.26 ? 261 GLU A CA 1 ATOM 1949 C C . GLU A 1 261 ? -6.633 -0.717 30.034 1.00 36.14 ? 261 GLU A C 1 ATOM 1950 O O . GLU A 1 261 ? -5.530 -0.511 30.519 1.00 34.08 ? 261 GLU A O 1 ATOM 1951 C CB . GLU A 1 261 ? -7.012 -3.178 30.107 1.00 41.48 ? 261 GLU A CB 1 ATOM 1952 C CG . GLU A 1 261 ? -7.584 -4.342 30.902 1.00 47.25 ? 261 GLU A CG 1 ATOM 1953 C CD . GLU A 1 261 ? -7.444 -5.681 30.184 1.00 52.62 ? 261 GLU A CD 1 ATOM 1954 O OE1 . GLU A 1 261 ? -6.665 -5.778 29.191 1.00 53.13 ? 261 GLU A OE1 1 ATOM 1955 O OE2 . GLU A 1 261 ? -8.124 -6.645 30.620 1.00 54.64 ? 261 GLU A OE2 1 ATOM 1956 N N . GLY A 1 262 ? -7.133 0.004 29.044 1.00 31.44 ? 262 GLY A N 1 ATOM 1957 C CA . GLY A 1 262 ? -6.385 1.072 28.403 1.00 33.44 ? 262 GLY A CA 1 ATOM 1958 C C . GLY A 1 262 ? -5.699 2.058 29.314 1.00 31.19 ? 262 GLY A C 1 ATOM 1959 O O . GLY A 1 262 ? -4.478 2.162 29.275 1.00 33.39 ? 262 GLY A O 1 ATOM 1960 N N . PRO A 1 263 ? -6.460 2.805 30.118 1.00 31.71 ? 263 PRO A N 1 ATOM 1961 C CA . PRO A 1 263 ? -5.879 3.819 31.005 1.00 32.52 ? 263 PRO A CA 1 ATOM 1962 C C . PRO A 1 263 ? -4.881 3.327 32.039 1.00 34.04 ? 263 PRO A C 1 ATOM 1963 O O . PRO A 1 263 ? -4.039 4.109 32.482 1.00 36.53 ? 263 PRO A O 1 ATOM 1964 C CB . PRO A 1 263 ? -7.101 4.396 31.707 1.00 32.14 ? 263 PRO A CB 1 ATOM 1965 C CG . PRO A 1 263 ? -8.157 4.197 30.731 1.00 30.91 ? 263 PRO A CG 1 ATOM 1966 C CD . PRO A 1 263 ? -7.926 2.807 30.212 1.00 32.05 ? 263 PRO A CD 1 ATOM 1967 N N . THR A 1 264 ? -4.947 2.050 32.403 1.00 35.00 ? 264 THR A N 1 ATOM 1968 C CA . THR A 1 264 ? -4.033 1.516 33.408 1.00 38.95 ? 264 THR A CA 1 ATOM 1969 C C . THR A 1 264 ? -2.753 0.850 32.870 1.00 40.43 ? 264 THR A C 1 ATOM 1970 O O . THR A 1 264 ? -1.971 0.334 33.660 1.00 43.57 ? 264 THR A O 1 ATOM 1971 C CB . THR A 1 264 ? -4.776 0.554 34.377 1.00 39.87 ? 264 THR A CB 1 ATOM 1972 O OG1 . THR A 1 264 ? -5.280 -0.576 33.652 1.00 39.90 ? 264 THR A OG1 1 ATOM 1973 C CG2 . THR A 1 264 ? -6.034 1.218 34.942 1.00 41.85 ? 264 THR A CG2 1 ATOM 1974 N N . LEU A 1 265 ? -2.531 0.857 31.556 1.00 39.52 ? 265 LEU A N 1 ATOM 1975 C CA . LEU A 1 265 ? -1.297 0.271 30.984 1.00 37.65 ? 265 LEU A CA 1 ATOM 1976 C C . LEU A 1 265 ? -0.027 1.043 31.374 1.00 36.53 ? 265 LEU A C 1 ATOM 1977 O O . LEU A 1 265 ? -0.085 2.254 31.624 1.00 38.13 ? 265 LEU A O 1 ATOM 1978 C CB . LEU A 1 265 ? -1.394 0.132 29.467 1.00 37.92 ? 265 LEU A CB 1 ATOM 1979 C CG . LEU A 1 265 ? -2.395 -0.859 28.860 1.00 38.49 ? 265 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 265 ? -2.342 -0.778 27.334 1.00 36.68 ? 265 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 265 ? -2.138 -2.270 29.340 1.00 36.60 ? 265 LEU A CD2 1 ATOM 1982 N N . PRO A 1 266 ? 1.107 0.342 31.456 1.00 35.79 ? 266 PRO A N 1 ATOM 1983 C CA . PRO A 1 266 ? 2.379 0.969 31.834 1.00 35.84 ? 266 PRO A CA 1 ATOM 1984 C C . PRO A 1 266 ? 2.850 2.074 30.899 1.00 33.77 ? 266 PRO A C 1 ATOM 1985 O O . PRO A 1 266 ? 2.561 2.037 29.711 1.00 34.89 ? 266 PRO A O 1 ATOM 1986 C CB . PRO A 1 266 ? 3.386 -0.186 31.752 1.00 35.79 ? 266 PRO A CB 1 ATOM 1987 C CG . PRO A 1 266 ? 2.595 -1.407 31.819 1.00 35.14 ? 266 PRO A CG 1 ATOM 1988 C CD . PRO A 1 266 ? 1.266 -1.106 31.204 1.00 34.93 ? 266 PRO A CD 1 ATOM 1989 N N . ASP A 1 267 ? 3.576 3.041 31.456 1.00 33.93 ? 267 ASP A N 1 ATOM 1990 C CA . ASP A 1 267 ? 4.439 3.937 30.691 1.00 34.43 ? 267 ASP A CA 1 ATOM 1991 C C . ASP A 1 267 ? 5.444 3.137 29.856 1.00 34.52 ? 267 ASP A C 1 ATOM 1992 O O . ASP A 1 267 ? 5.949 2.102 30.314 1.00 34.21 ? 267 ASP A O 1 ATOM 1993 C CB . ASP A 1 267 ? 5.222 4.852 31.649 1.00 37.26 ? 267 ASP A CB 1 ATOM 1994 C CG . ASP A 1 267 ? 4.369 5.991 32.224 1.00 38.13 ? 267 ASP A CG 1 ATOM 1995 O OD1 . ASP A 1 267 ? 3.143 6.008 32.008 1.00 38.43 ? 267 ASP A OD1 1 ATOM 1996 O OD2 . ASP A 1 267 ? 4.841 6.914 32.922 1.00 38.60 ? 267 ASP A OD2 1 ATOM 1997 N N . ILE A 1 268 ? 5.717 3.596 28.634 1.00 31.64 ? 268 ILE A N 1 ATOM 1998 C CA . ILE A 1 268 ? 6.830 3.065 27.829 1.00 31.90 ? 268 ILE A CA 1 ATOM 1999 C C . ILE A 1 268 ? 7.865 4.149 27.579 1.00 34.45 ? 268 ILE A C 1 ATOM 2000 O O . ILE A 1 268 ? 7.530 5.283 27.197 1.00 37.10 ? 268 ILE A O 1 ATOM 2001 C CB . ILE A 1 268 ? 6.352 2.490 26.489 1.00 32.50 ? 268 ILE A CB 1 ATOM 2002 C CG1 . ILE A 1 268 ? 5.188 1.517 26.700 1.00 31.05 ? 268 ILE A CG1 1 ATOM 2003 C CG2 . ILE A 1 268 ? 7.530 1.851 25.714 1.00 32.84 ? 268 ILE A CG2 1 ATOM 2004 C CD1 . ILE A 1 268 ? 4.634 0.964 25.412 1.00 32.26 ? 268 ILE A CD1 1 ATOM 2005 N N . SER A 1 269 ? 9.123 3.780 27.768 1.00 34.92 ? 269 SER A N 1 ATOM 2006 C CA . SER A 1 269 ? 10.227 4.722 27.697 1.00 36.59 ? 269 SER A CA 1 ATOM 2007 C C . SER A 1 269 ? 11.297 4.349 26.673 1.00 34.64 ? 269 SER A C 1 ATOM 2008 O O . SER A 1 269 ? 11.745 3.203 26.601 1.00 38.17 ? 269 SER A O 1 ATOM 2009 C CB . SER A 1 269 ? 10.854 4.863 29.084 1.00 38.32 ? 269 SER A CB 1 ATOM 2010 O OG . SER A 1 269 ? 10.114 5.774 29.869 1.00 42.76 ? 269 SER A OG 1 ATOM 2011 N N . PHE A 1 270 ? 11.707 5.342 25.892 1.00 33.52 ? 270 PHE A N 1 ATOM 2012 C CA . PHE A 1 270 ? 12.773 5.190 24.919 1.00 33.96 ? 270 PHE A CA 1 ATOM 2013 C C . PHE A 1 270 ? 14.005 5.975 25.392 1.00 33.81 ? 270 PHE A C 1 ATOM 2014 O O . PHE A 1 270 ? 13.915 7.159 25.727 1.00 33.52 ? 270 PHE A O 1 ATOM 2015 C CB . PHE A 1 270 ? 12.299 5.609 23.521 1.00 31.95 ? 270 PHE A CB 1 ATOM 2016 C CG . PHE A 1 270 ? 11.069 4.887 23.080 1.00 30.53 ? 270 PHE A CG 1 ATOM 2017 C CD1 . PHE A 1 270 ? 11.162 3.705 22.352 1.00 30.37 ? 270 PHE A CD1 1 ATOM 2018 C CD2 . PHE A 1 270 ? 9.814 5.357 23.442 1.00 30.73 ? 270 PHE A CD2 1 ATOM 2019 C CE1 . PHE A 1 270 ? 10.042 3.024 21.975 1.00 31.67 ? 270 PHE A CE1 1 ATOM 2020 C CE2 . PHE A 1 270 ? 8.675 4.674 23.072 1.00 32.18 ? 270 PHE A CE2 1 ATOM 2021 C CZ . PHE A 1 270 ? 8.792 3.506 22.331 1.00 32.00 ? 270 PHE A CZ 1 ATOM 2022 N N . HIS A 1 271 ? 15.134 5.270 25.459 1.00 34.76 ? 271 HIS A N 1 ATOM 2023 C CA . HIS A 1 271 ? 16.401 5.834 25.933 1.00 33.98 ? 271 HIS A CA 1 ATOM 2024 C C . HIS A 1 271 ? 17.228 6.269 24.744 1.00 32.11 ? 271 HIS A C 1 ATOM 2025 O O . HIS A 1 271 ? 17.755 5.444 24.015 1.00 32.15 ? 271 HIS A O 1 ATOM 2026 C CB . HIS A 1 271 ? 17.168 4.800 26.770 1.00 37.11 ? 271 HIS A CB 1 ATOM 2027 C CG . HIS A 1 271 ? 18.349 5.361 27.508 1.00 40.59 ? 271 HIS A CG 1 ATOM 2028 N ND1 . HIS A 1 271 ? 19.463 4.606 27.815 1.00 41.73 ? 271 HIS A ND1 1 ATOM 2029 C CD2 . HIS A 1 271 ? 18.591 6.602 27.995 1.00 41.47 ? 271 HIS A CD2 1 ATOM 2030 C CE1 . HIS A 1 271 ? 20.334 5.357 28.468 1.00 42.40 ? 271 HIS A CE1 1 ATOM 2031 N NE2 . HIS A 1 271 ? 19.833 6.574 28.580 1.00 43.75 ? 271 HIS A NE2 1 ATOM 2032 N N . LEU A 1 272 ? 17.340 7.580 24.558 1.00 34.33 ? 272 LEU A N 1 ATOM 2033 C CA . LEU A 1 272 ? 17.955 8.154 23.362 1.00 31.44 ? 272 LEU A CA 1 ATOM 2034 C C . LEU A 1 272 ? 18.839 9.319 23.780 1.00 33.68 ? 272 LEU A C 1 ATOM 2035 O O . LEU A 1 272 ? 18.364 10.302 24.386 1.00 31.94 ? 272 LEU A O 1 ATOM 2036 C CB . LEU A 1 272 ? 16.874 8.647 22.374 1.00 29.27 ? 272 LEU A CB 1 ATOM 2037 C CG . LEU A 1 272 ? 15.817 7.637 21.916 1.00 30.17 ? 272 LEU A CG 1 ATOM 2038 C CD1 . LEU A 1 272 ? 14.490 8.288 21.487 1.00 28.50 ? 272 LEU A CD1 1 ATOM 2039 C CD2 . LEU A 1 272 ? 16.341 6.728 20.819 1.00 28.80 ? 272 LEU A CD2 1 ATOM 2040 N N . GLY A 1 273 ? 20.124 9.220 23.446 1.00 35.28 ? 273 GLY A N 1 ATOM 2041 C CA . GLY A 1 273 ? 21.111 10.201 23.932 1.00 34.26 ? 273 GLY A CA 1 ATOM 2042 C C . GLY A 1 273 ? 21.108 10.192 25.447 1.00 34.77 ? 273 GLY A C 1 ATOM 2043 O O . GLY A 1 273 ? 21.242 9.124 26.069 1.00 35.92 ? 273 GLY A O 1 ATOM 2044 N N . GLY A 1 274 ? 20.912 11.353 26.059 1.00 32.09 ? 274 GLY A N 1 ATOM 2045 C CA . GLY A 1 274 ? 20.920 11.415 27.515 1.00 35.62 ? 274 GLY A CA 1 ATOM 2046 C C . GLY A 1 274 ? 19.587 11.592 28.241 1.00 38.67 ? 274 GLY A C 1 ATOM 2047 O O . GLY A 1 274 ? 19.551 12.211 29.303 1.00 40.53 ? 274 GLY A O 1 ATOM 2048 N N . LYS A 1 275 ? 18.503 11.036 27.685 1.00 37.06 ? 275 LYS A N 1 ATOM 2049 C CA . LYS A 1 275 ? 17.150 11.193 28.222 1.00 35.66 ? 275 LYS A CA 1 ATOM 2050 C C . LYS A 1 275 ? 16.307 9.948 27.948 1.00 35.79 ? 275 LYS A C 1 ATOM 2051 O O . LYS A 1 275 ? 16.564 9.208 26.988 1.00 38.10 ? 275 LYS A O 1 ATOM 2052 C CB . LYS A 1 275 ? 16.485 12.447 27.619 1.00 37.55 ? 275 LYS A CB 1 ATOM 2053 C CG . LYS A 1 275 ? 15.024 12.643 28.002 1.00 39.94 ? 275 LYS A CG 1 ATOM 2054 C CD . LYS A 1 275 ? 14.595 14.109 27.939 1.00 43.33 ? 275 LYS A CD 1 ATOM 2055 C CE . LYS A 1 275 ? 13.075 14.276 28.066 1.00 44.41 ? 275 LYS A CE 1 ATOM 2056 N NZ . LYS A 1 275 ? 12.438 13.349 29.055 1.00 47.27 ? 275 LYS A NZ 1 ATOM 2057 N N . GLU A 1 276 ? 15.337 9.699 28.823 1.00 37.04 ? 276 GLU A N 1 ATOM 2058 C CA . GLU A 1 276 ? 14.314 8.682 28.603 1.00 38.18 ? 276 GLU A CA 1 ATOM 2059 C C . GLU A 1 276 ? 13.113 9.463 28.137 1.00 36.78 ? 276 GLU A C 1 ATOM 2060 O O . GLU A 1 276 ? 12.684 10.403 28.799 1.00 35.37 ? 276 GLU A O 1 ATOM 2061 C CB . GLU A 1 276 ? 13.938 7.944 29.891 1.00 40.54 ? 276 GLU A CB 1 ATOM 2062 C CG . GLU A 1 276 ? 15.055 7.151 30.538 1.00 41.24 ? 276 GLU A CG 1 ATOM 2063 C CD . GLU A 1 276 ? 15.286 5.813 29.880 1.00 42.89 ? 276 GLU A CD 1 ATOM 2064 O OE1 . GLU A 1 276 ? 14.540 5.447 28.947 1.00 42.88 ? 276 GLU A OE1 1 ATOM 2065 O OE2 . GLU A 1 276 ? 16.219 5.117 30.308 1.00 45.43 ? 276 GLU A OE2 1 ATOM 2066 N N . TYR A 1 277 ? 12.610 9.098 26.968 1.00 34.75 ? 277 TYR A N 1 ATOM 2067 C CA . TYR A 1 277 ? 11.460 9.751 26.400 1.00 30.23 ? 277 TYR A CA 1 ATOM 2068 C C . TYR A 1 277 ? 10.323 8.806 26.709 1.00 31.28 ? 277 TYR A C 1 ATOM 2069 O O . TYR A 1 277 ? 10.357 7.646 26.316 1.00 30.77 ? 277 TYR A O 1 ATOM 2070 C CB . TYR A 1 277 ? 11.674 9.969 24.905 1.00 31.02 ? 277 TYR A CB 1 ATOM 2071 C CG . TYR A 1 277 ? 12.735 11.021 24.629 1.00 29.91 ? 277 TYR A CG 1 ATOM 2072 C CD1 . TYR A 1 277 ? 12.380 12.354 24.468 1.00 31.65 ? 277 TYR A CD1 1 ATOM 2073 C CD2 . TYR A 1 277 ? 14.077 10.699 24.590 1.00 28.99 ? 277 TYR A CD2 1 ATOM 2074 C CE1 . TYR A 1 277 ? 13.323 13.328 24.233 1.00 30.62 ? 277 TYR A CE1 1 ATOM 2075 C CE2 . TYR A 1 277 ? 15.043 11.676 24.342 1.00 31.09 ? 277 TYR A CE2 1 ATOM 2076 C CZ . TYR A 1 277 ? 14.652 12.995 24.173 1.00 32.53 ? 277 TYR A CZ 1 ATOM 2077 O OH . TYR A 1 277 ? 15.579 14.008 23.947 1.00 32.89 ? 277 TYR A OH 1 ATOM 2078 N N . THR A 1 278 ? 9.346 9.314 27.451 1.00 31.70 ? 278 THR A N 1 ATOM 2079 C CA . THR A 1 278 ? 8.275 8.515 28.039 1.00 35.19 ? 278 THR A CA 1 ATOM 2080 C C . THR A 1 278 ? 6.948 8.741 27.326 1.00 33.85 ? 278 THR A C 1 ATOM 2081 O O . THR A 1 278 ? 6.552 9.882 27.092 1.00 33.42 ? 278 THR A O 1 ATOM 2082 C CB . THR A 1 278 ? 8.115 8.901 29.542 1.00 37.77 ? 278 THR A CB 1 ATOM 2083 O OG1 . THR A 1 278 ? 9.328 8.608 30.247 1.00 40.39 ? 278 THR A OG1 1 ATOM 2084 C CG2 . THR A 1 278 ? 7.056 8.025 30.255 1.00 38.85 ? 278 THR A CG2 1 ATOM 2085 N N . LEU A 1 279 ? 6.280 7.640 26.976 1.00 34.03 ? 279 LEU A N 1 ATOM 2086 C CA . LEU A 1 279 ? 4.888 7.663 26.511 1.00 33.48 ? 279 LEU A CA 1 ATOM 2087 C C . LEU A 1 279 ? 3.990 6.951 27.515 1.00 31.39 ? 279 LEU A C 1 ATOM 2088 O O . LEU A 1 279 ? 4.279 5.836 27.922 1.00 28.11 ? 279 LEU A O 1 ATOM 2089 C CB . LEU A 1 279 ? 4.742 6.996 25.120 1.00 35.17 ? 279 LEU A CB 1 ATOM 2090 C CG . LEU A 1 279 ? 5.629 7.369 23.923 1.00 34.97 ? 279 LEU A CG 1 ATOM 2091 C CD1 . LEU A 1 279 ? 4.985 6.955 22.602 1.00 29.35 ? 279 LEU A CD1 1 ATOM 2092 C CD2 . LEU A 1 279 ? 5.997 8.844 23.899 1.00 34.62 ? 279 LEU A CD2 1 ATOM 2093 N N . THR A 1 280 ? 2.930 7.627 27.944 1.00 31.86 ? 280 THR A N 1 ATOM 2094 C CA . THR A 1 280 ? 1.947 7.029 28.833 1.00 34.76 ? 280 THR A CA 1 ATOM 2095 C C . THR A 1 280 ? 0.898 6.347 27.946 1.00 35.18 ? 280 THR A C 1 ATOM 2096 O O . THR A 1 280 ? 0.890 6.573 26.740 1.00 36.08 ? 280 THR A O 1 ATOM 2097 C CB . THR A 1 280 ? 1.324 8.111 29.737 1.00 37.65 ? 280 THR A CB 1 ATOM 2098 O OG1 . THR A 1 280 ? 0.679 9.110 28.931 1.00 38.18 ? 280 THR A OG1 1 ATOM 2099 C CG2 . THR A 1 280 ? 2.419 8.916 30.444 1.00 38.12 ? 280 THR A CG2 1 ATOM 2100 N N . SER A 1 281 ? 0.029 5.511 28.520 1.00 32.69 ? 281 SER A N 1 ATOM 2101 C CA . SER A 1 281 ? -1.010 4.856 27.732 1.00 32.45 ? 281 SER A CA 1 ATOM 2102 C C . SER A 1 281 ? -1.833 5.863 26.917 1.00 30.29 ? 281 SER A C 1 ATOM 2103 O O . SER A 1 281 ? -2.303 5.533 25.840 1.00 31.20 ? 281 SER A O 1 ATOM 2104 C CB . SER A 1 281 ? -1.913 3.958 28.608 1.00 31.40 ? 281 SER A CB 1 ATOM 2105 O OG . SER A 1 281 ? -2.753 4.727 29.450 1.00 31.23 ? 281 SER A OG 1 ATOM 2106 N N . ALA A 1 282 ? -1.972 7.086 27.424 1.00 29.94 ? 282 ALA A N 1 ATOM 2107 C CA . ALA A 1 282 ? -2.667 8.181 26.708 1.00 31.99 ? 282 ALA A CA 1 ATOM 2108 C C . ALA A 1 282 ? -1.981 8.579 25.390 1.00 31.80 ? 282 ALA A C 1 ATOM 2109 O O . ALA A 1 282 ? -2.607 9.159 24.520 1.00 34.44 ? 282 ALA A O 1 ATOM 2110 C CB . ALA A 1 282 ? -2.817 9.392 27.598 1.00 31.60 ? 282 ALA A CB 1 ATOM 2111 N N . ASP A 1 283 ? -0.705 8.235 25.253 1.00 29.31 ? 283 ASP A N 1 ATOM 2112 C CA . ASP A 1 283 ? 0.081 8.509 24.058 1.00 28.01 ? 283 ASP A CA 1 ATOM 2113 C C . ASP A 1 283 ? 0.109 7.342 23.070 1.00 26.56 ? 283 ASP A C 1 ATOM 2114 O O . ASP A 1 283 ? 0.377 7.522 21.882 1.00 27.24 ? 283 ASP A O 1 ATOM 2115 C CB . ASP A 1 283 ? 1.507 8.852 24.469 1.00 28.31 ? 283 ASP A CB 1 ATOM 2116 C CG . ASP A 1 283 ? 1.576 10.098 25.317 1.00 31.38 ? 283 ASP A CG 1 ATOM 2117 O OD1 . ASP A 1 283 ? 0.966 11.108 24.911 1.00 31.12 ? 283 ASP A OD1 1 ATOM 2118 O OD2 . ASP A 1 283 ? 2.215 10.165 26.401 1.00 32.91 ? 283 ASP A OD2 1 ATOM 2119 N N . TYR A 1 284 ? -0.184 6.142 23.532 1.00 23.33 ? 284 TYR A N 1 ATOM 2120 C CA . TYR A 1 284 ? -0.090 5.028 22.597 1.00 26.30 ? 284 TYR A CA 1 ATOM 2121 C C . TYR A 1 284 ? -1.351 4.136 22.498 1.00 25.64 ? 284 TYR A C 1 ATOM 2122 O O . TYR A 1 284 ? -1.359 3.141 21.776 1.00 26.98 ? 284 TYR A O 1 ATOM 2123 C CB . TYR A 1 284 ? 1.202 4.242 22.863 1.00 24.87 ? 284 TYR A CB 1 ATOM 2124 C CG . TYR A 1 284 ? 1.205 3.446 24.169 1.00 24.54 ? 284 TYR A CG 1 ATOM 2125 C CD1 . TYR A 1 284 ? 0.577 2.195 24.234 1.00 23.26 ? 284 TYR A CD1 1 ATOM 2126 C CD2 . TYR A 1 284 ? 1.850 3.926 25.325 1.00 20.00 ? 284 TYR A CD2 1 ATOM 2127 C CE1 . TYR A 1 284 ? 0.560 1.440 25.406 1.00 22.59 ? 284 TYR A CE1 1 ATOM 2128 C CE2 . TYR A 1 284 ? 1.843 3.157 26.531 1.00 25.53 ? 284 TYR A CE2 1 ATOM 2129 C CZ . TYR A 1 284 ? 1.203 1.903 26.539 1.00 26.18 ? 284 TYR A CZ 1 ATOM 2130 O OH . TYR A 1 284 ? 1.151 1.102 27.667 1.00 26.64 ? 284 TYR A OH 1 ATOM 2131 N N . VAL A 1 285 ? -2.409 4.472 23.220 1.00 27.78 ? 285 VAL A N 1 ATOM 2132 C CA . VAL A 1 285 ? -3.640 3.681 23.098 1.00 27.54 ? 285 VAL A CA 1 ATOM 2133 C C . VAL A 1 285 ? -4.693 4.508 22.407 1.00 26.68 ? 285 VAL A C 1 ATOM 2134 O O . VAL A 1 285 ? -4.897 5.670 22.771 1.00 27.74 ? 285 VAL A O 1 ATOM 2135 C CB . VAL A 1 285 ? -4.187 3.208 24.472 1.00 29.13 ? 285 VAL A CB 1 ATOM 2136 C CG1 . VAL A 1 285 ? -5.582 2.494 24.327 1.00 29.15 ? 285 VAL A CG1 1 ATOM 2137 C CG2 . VAL A 1 285 ? -3.178 2.315 25.175 1.00 30.59 ? 285 VAL A CG2 1 ATOM 2138 N N . PHE A 1 286 ? -5.385 3.898 21.445 1.00 26.60 ? 286 PHE A N 1 ATOM 2139 C CA . PHE A 1 286 ? -6.543 4.525 20.791 1.00 26.88 ? 286 PHE A CA 1 ATOM 2140 C C . PHE A 1 286 ? -7.788 4.211 21.591 1.00 28.48 ? 286 PHE A C 1 ATOM 2141 O O . PHE A 1 286 ? -8.420 3.152 21.386 1.00 30.01 ? 286 PHE A O 1 ATOM 2142 C CB . PHE A 1 286 ? -6.711 4.047 19.331 1.00 29.11 ? 286 PHE A CB 1 ATOM 2143 C CG . PHE A 1 286 ? -5.696 4.639 18.359 1.00 28.26 ? 286 PHE A CG 1 ATOM 2144 C CD1 . PHE A 1 286 ? -5.776 5.978 17.970 1.00 29.82 ? 286 PHE A CD1 1 ATOM 2145 C CD2 . PHE A 1 286 ? -4.686 3.855 17.841 1.00 28.12 ? 286 PHE A CD2 1 ATOM 2146 C CE1 . PHE A 1 286 ? -4.844 6.531 17.091 1.00 31.68 ? 286 PHE A CE1 1 ATOM 2147 C CE2 . PHE A 1 286 ? -3.744 4.382 16.959 1.00 32.12 ? 286 PHE A CE2 1 ATOM 2148 C CZ . PHE A 1 286 ? -3.823 5.728 16.568 1.00 32.86 ? 286 PHE A CZ 1 ATOM 2149 N N . GLN A 1 287 ? -8.131 5.125 22.491 1.00 23.60 ? 287 GLN A N 1 ATOM 2150 C CA . GLN A 1 287 ? -9.190 4.936 23.480 1.00 26.14 ? 287 GLN A CA 1 ATOM 2151 C C . GLN A 1 287 ? -10.516 5.349 22.894 1.00 30.06 ? 287 GLN A C 1 ATOM 2152 O O . GLN A 1 287 ? -11.014 6.462 23.142 1.00 31.37 ? 287 GLN A O 1 ATOM 2153 C CB . GLN A 1 287 ? -8.890 5.780 24.728 1.00 28.71 ? 287 GLN A CB 1 ATOM 2154 C CG . GLN A 1 287 ? -9.485 5.286 26.005 1.00 29.61 ? 287 GLN A CG 1 ATOM 2155 C CD . GLN A 1 287 ? -8.914 3.943 26.505 1.00 27.75 ? 287 GLN A CD 1 ATOM 2156 O OE1 . GLN A 1 287 ? -7.721 3.806 26.736 1.00 27.22 ? 287 GLN A OE1 1 ATOM 2157 N NE2 . GLN A 1 287 ? -9.796 2.996 26.739 1.00 27.21 ? 287 GLN A NE2 1 ATOM 2158 N N . GLU A 1 288 ? -11.088 4.450 22.101 1.00 30.03 ? 288 GLU A N 1 ATOM 2159 C CA . GLU A 1 288 ? -12.308 4.761 21.365 1.00 32.95 ? 288 GLU A CA 1 ATOM 2160 C C . GLU A 1 288 ? -13.530 4.463 22.221 1.00 30.92 ? 288 GLU A C 1 ATOM 2161 O O . GLU A 1 288 ? -14.652 4.783 21.869 1.00 32.59 ? 288 GLU A O 1 ATOM 2162 C CB . GLU A 1 288 ? -12.333 3.996 20.048 1.00 33.83 ? 288 GLU A CB 1 ATOM 2163 C CG . GLU A 1 288 ? -11.251 4.483 19.084 1.00 39.73 ? 288 GLU A CG 1 ATOM 2164 C CD . GLU A 1 288 ? -11.434 3.971 17.675 1.00 46.15 ? 288 GLU A CD 1 ATOM 2165 O OE1 . GLU A 1 288 ? -10.424 3.514 17.086 1.00 50.21 ? 288 GLU A OE1 1 ATOM 2166 O OE2 . GLU A 1 288 ? -12.579 4.017 17.154 1.00 45.65 ? 288 GLU A OE2 1 ATOM 2167 N N . SER A 1 289 ? -13.282 3.874 23.373 1.00 33.17 ? 289 SER A N 1 ATOM 2168 C CA . SER A 1 289 ? -14.336 3.473 24.289 1.00 34.50 ? 289 SER A CA 1 ATOM 2169 C C . SER A 1 289 ? -13.631 3.211 25.627 1.00 36.22 ? 289 SER A C 1 ATOM 2170 O O . SER A 1 289 ? -12.383 3.134 25.665 1.00 34.11 ? 289 SER A O 1 ATOM 2171 C CB . SER A 1 289 ? -15.031 2.213 23.714 1.00 33.90 ? 289 SER A CB 1 ATOM 2172 O OG . SER A 1 289 ? -15.904 1.655 24.659 1.00 37.93 ? 289 SER A OG 1 ATOM 2173 N N . TYR A 1 290 ? -14.392 3.118 26.721 1.00 35.58 ? 290 TYR A N 1 ATOM 2174 C CA . TYR A 1 290 ? -13.822 2.681 28.009 1.00 36.39 ? 290 TYR A CA 1 ATOM 2175 C C . TYR A 1 290 ? -14.436 1.353 28.478 1.00 36.50 ? 290 TYR A C 1 ATOM 2176 O O . TYR A 1 290 ? -14.214 0.914 29.595 1.00 37.78 ? 290 TYR A O 1 ATOM 2177 C CB . TYR A 1 290 ? -13.930 3.778 29.087 1.00 35.45 ? 290 TYR A CB 1 ATOM 2178 C CG . TYR A 1 290 ? -13.057 4.970 28.782 1.00 33.87 ? 290 TYR A CG 1 ATOM 2179 C CD1 . TYR A 1 290 ? -11.763 5.040 29.275 1.00 34.24 ? 290 TYR A CD1 1 ATOM 2180 C CD2 . TYR A 1 290 ? -13.513 6.006 27.953 1.00 33.41 ? 290 TYR A CD2 1 ATOM 2181 C CE1 . TYR A 1 290 ? -10.937 6.123 28.977 1.00 34.67 ? 290 TYR A CE1 1 ATOM 2182 C CE2 . TYR A 1 290 ? -12.694 7.091 27.641 1.00 34.54 ? 290 TYR A CE2 1 ATOM 2183 C CZ . TYR A 1 290 ? -11.408 7.137 28.154 1.00 35.21 ? 290 TYR A CZ 1 ATOM 2184 O OH . TYR A 1 290 ? -10.587 8.194 27.860 1.00 35.45 ? 290 TYR A OH 1 ATOM 2185 N N . SER A 1 291 ? -15.191 0.722 27.589 1.00 38.35 ? 291 SER A N 1 ATOM 2186 C CA . SER A 1 291 ? -15.955 -0.466 27.897 1.00 38.19 ? 291 SER A CA 1 ATOM 2187 C C . SER A 1 291 ? -15.073 -1.716 27.895 1.00 40.22 ? 291 SER A C 1 ATOM 2188 O O . SER A 1 291 ? -14.086 -1.798 27.142 1.00 37.85 ? 291 SER A O 1 ATOM 2189 C CB . SER A 1 291 ? -17.100 -0.602 26.891 1.00 38.39 ? 291 SER A CB 1 ATOM 2190 O OG . SER A 1 291 ? -17.797 -1.832 27.043 1.00 40.18 ? 291 SER A OG 1 ATOM 2191 N N . SER A 1 292 ? -15.437 -2.675 28.751 1.00 39.53 ? 292 SER A N 1 ATOM 2192 C CA . SER A 1 292 ? -14.814 -3.994 28.777 1.00 41.49 ? 292 SER A CA 1 ATOM 2193 C C . SER A 1 292 ? -15.306 -4.897 27.656 1.00 42.87 ? 292 SER A C 1 ATOM 2194 O O . SER A 1 292 ? -14.656 -5.901 27.345 1.00 44.49 ? 292 SER A O 1 ATOM 2195 C CB . SER A 1 292 ? -15.055 -4.674 30.126 1.00 43.26 ? 292 SER A CB 1 ATOM 2196 O OG . SER A 1 292 ? -16.438 -4.716 30.444 1.00 42.97 ? 292 SER A OG 1 ATOM 2197 N N . LYS A 1 293 ? -16.445 -4.554 27.049 1.00 43.89 ? 293 LYS A N 1 ATOM 2198 C CA . LYS A 1 293 ? -16.969 -5.338 25.917 1.00 46.29 ? 293 LYS A CA 1 ATOM 2199 C C . LYS A 1 293 ? -16.398 -4.915 24.548 1.00 45.50 ? 293 LYS A C 1 ATOM 2200 O O . LYS A 1 293 ? -16.892 -5.355 23.510 1.00 46.27 ? 293 LYS A O 1 ATOM 2201 C CB . LYS A 1 293 ? -18.520 -5.328 25.863 1.00 46.76 ? 293 LYS A CB 1 ATOM 2202 C CG . LYS A 1 293 ? -19.249 -5.510 27.192 1.00 50.80 ? 293 LYS A CG 1 ATOM 2203 C CD . LYS A 1 293 ? -19.899 -4.192 27.620 1.00 54.78 ? 293 LYS A CD 1 ATOM 2204 C CE . LYS A 1 293 ? -19.898 -3.995 29.141 1.00 56.72 ? 293 LYS A CE 1 ATOM 2205 N NZ . LYS A 1 293 ? -21.058 -4.658 29.834 1.00 56.56 ? 293 LYS A NZ 1 ATOM 2206 N N . LYS A 1 294 ? -15.379 -4.052 24.539 1.00 45.13 ? 294 LYS A N 1 ATOM 2207 C CA . LYS A 1 294 ? -14.805 -3.547 23.278 1.00 43.55 ? 294 LYS A CA 1 ATOM 2208 C C . LYS A 1 294 ? -13.280 -3.605 23.300 1.00 41.83 ? 294 LYS A C 1 ATOM 2209 O O . LYS A 1 294 ? -12.669 -3.648 24.378 1.00 41.50 ? 294 LYS A O 1 ATOM 2210 C CB . LYS A 1 294 ? -15.289 -2.121 22.959 1.00 44.95 ? 294 LYS A CB 1 ATOM 2211 C CG . LYS A 1 294 ? -16.804 -1.960 22.920 1.00 47.67 ? 294 LYS A CG 1 ATOM 2212 C CD . LYS A 1 294 ? -17.261 -0.876 21.954 1.00 49.69 ? 294 LYS A CD 1 ATOM 2213 C CE . LYS A 1 294 ? -18.722 -1.097 21.532 1.00 50.39 ? 294 LYS A CE 1 ATOM 2214 N NZ . LYS A 1 294 ? -18.941 -2.450 20.893 1.00 50.89 ? 294 LYS A NZ 1 ATOM 2215 N N . LEU A 1 295 ? -12.673 -3.623 22.115 1.00 39.90 ? 295 LEU A N 1 ATOM 2216 C CA . LEU A 1 295 ? -11.216 -3.762 21.997 1.00 38.03 ? 295 LEU A CA 1 ATOM 2217 C C . LEU A 1 295 ? -10.590 -2.500 21.404 1.00 37.95 ? 295 LEU A C 1 ATOM 2218 O O . LEU A 1 295 ? -11.119 -1.914 20.452 1.00 36.35 ? 295 LEU A O 1 ATOM 2219 C CB . LEU A 1 295 ? -10.833 -5.006 21.183 1.00 38.84 ? 295 LEU A CB 1 ATOM 2220 C CG . LEU A 1 295 ? -11.249 -6.402 21.685 1.00 37.17 ? 295 LEU A CG 1 ATOM 2221 C CD1 . LEU A 1 295 ? -10.985 -7.413 20.607 1.00 39.54 ? 295 LEU A CD1 1 ATOM 2222 C CD2 . LEU A 1 295 ? -10.514 -6.785 22.938 1.00 35.34 ? 295 LEU A CD2 1 ATOM 2223 N N . CYS A 1 296 ? -9.472 -2.089 21.999 1.00 35.84 ? 296 CYS A N 1 ATOM 2224 C CA . CYS A 1 296 ? -8.794 -0.857 21.648 1.00 34.78 ? 296 CYS A CA 1 ATOM 2225 C C . CYS A 1 296 ? -7.440 -1.123 21.001 1.00 34.26 ? 296 CYS A C 1 ATOM 2226 O O . CYS A 1 296 ? -6.624 -1.873 21.532 1.00 32.68 ? 296 CYS A O 1 ATOM 2227 C CB . CYS A 1 296 ? -8.633 0.024 22.889 1.00 34.50 ? 296 CYS A CB 1 ATOM 2228 S SG . CYS A 1 296 ? -10.163 0.909 23.279 1.00 37.99 ? 296 CYS A SG 1 ATOM 2229 N N . THR A 1 297 ? -7.218 -0.490 19.855 1.00 32.65 ? 297 THR A N 1 ATOM 2230 C CA . THR A 1 297 ? -5.971 -0.649 19.093 1.00 32.96 ? 297 THR A CA 1 ATOM 2231 C C . THR A 1 297 ? -4.849 0.182 19.700 1.00 29.62 ? 297 THR A C 1 ATOM 2232 O O . THR A 1 297 ? -5.089 1.265 20.239 1.00 28.17 ? 297 THR A O 1 ATOM 2233 C CB . THR A 1 297 ? -6.197 -0.228 17.635 1.00 34.90 ? 297 THR A CB 1 ATOM 2234 O OG1 . THR A 1 297 ? -7.204 -1.061 17.061 1.00 36.48 ? 297 THR A OG1 1 ATOM 2235 C CG2 . THR A 1 297 ? -4.957 -0.498 16.767 1.00 37.44 ? 297 THR A CG2 1 ATOM 2236 N N . LEU A 1 298 ? -3.629 -0.342 19.599 1.00 30.78 ? 298 LEU A N 1 ATOM 2237 C CA . LEU A 1 298 ? -2.438 0.359 20.053 1.00 31.46 ? 298 LEU A CA 1 ATOM 2238 C C . LEU A 1 298 ? -1.674 0.996 18.883 1.00 31.82 ? 298 LEU A C 1 ATOM 2239 O O . LEU A 1 298 ? -1.545 0.399 17.808 1.00 28.07 ? 298 LEU A O 1 ATOM 2240 C CB . LEU A 1 298 ? -1.515 -0.586 20.847 1.00 33.55 ? 298 LEU A CB 1 ATOM 2241 C CG . LEU A 1 298 ? -2.007 -1.338 22.099 1.00 34.49 ? 298 LEU A CG 1 ATOM 2242 C CD1 . LEU A 1 298 ? -0.835 -1.962 22.874 1.00 34.00 ? 298 LEU A CD1 1 ATOM 2243 C CD2 . LEU A 1 298 ? -2.811 -0.467 23.026 1.00 33.25 ? 298 LEU A CD2 1 ATOM 2244 N N . ALA A 1 299 ? -1.133 2.190 19.134 1.00 29.56 ? 299 ALA A N 1 ATOM 2245 C CA . ALA A 1 299 ? -0.368 2.955 18.163 1.00 27.72 ? 299 ALA A CA 1 ATOM 2246 C C . ALA A 1 299 ? 1.077 2.461 18.071 1.00 28.76 ? 299 ALA A C 1 ATOM 2247 O O . ALA A 1 299 ? 2.011 3.257 17.856 1.00 24.56 ? 299 ALA A O 1 ATOM 2248 C CB . ALA A 1 299 ? -0.408 4.445 18.539 1.00 28.30 ? 299 ALA A CB 1 ATOM 2249 N N . ILE A 1 300 ? 1.243 1.149 18.270 1.00 28.92 ? 300 ILE A N 1 ATOM 2250 C CA . ILE A 1 300 ? 2.515 0.433 18.121 1.00 32.66 ? 300 ILE A CA 1 ATOM 2251 C C . ILE A 1 300 ? 2.297 -0.853 17.298 1.00 36.45 ? 300 ILE A C 1 ATOM 2252 O O . ILE A 1 300 ? 1.405 -1.655 17.598 1.00 34.98 ? 300 ILE A O 1 ATOM 2253 C CB . ILE A 1 300 ? 3.091 0.049 19.496 1.00 33.63 ? 300 ILE A CB 1 ATOM 2254 C CG1 . ILE A 1 300 ? 3.211 1.279 20.400 1.00 34.60 ? 300 ILE A CG1 1 ATOM 2255 C CG2 . ILE A 1 300 ? 4.442 -0.676 19.339 1.00 30.86 ? 300 ILE A CG2 1 ATOM 2256 C CD1 . ILE A 1 300 ? 3.141 0.952 21.844 1.00 34.57 ? 300 ILE A CD1 1 ATOM 2257 N N . HIS A 1 301 ? 3.124 -1.046 16.271 1.00 37.81 ? 301 HIS A N 1 ATOM 2258 C CA . HIS A 1 301 ? 2.943 -2.143 15.313 1.00 39.28 ? 301 HIS A CA 1 ATOM 2259 C C . HIS A 1 301 ? 4.288 -2.776 14.954 1.00 38.94 ? 301 HIS A C 1 ATOM 2260 O O . HIS A 1 301 ? 5.322 -2.111 14.984 1.00 37.01 ? 301 HIS A O 1 ATOM 2261 C CB . HIS A 1 301 ? 2.288 -1.616 14.025 1.00 42.01 ? 301 HIS A CB 1 ATOM 2262 C CG . HIS A 1 301 ? 0.853 -1.208 14.177 1.00 46.77 ? 301 HIS A CG 1 ATOM 2263 N ND1 . HIS A 1 301 ? -0.188 -1.923 13.619 1.00 48.19 ? 301 HIS A ND1 1 ATOM 2264 C CD2 . HIS A 1 301 ? 0.285 -0.145 14.799 1.00 48.86 ? 301 HIS A CD2 1 ATOM 2265 C CE1 . HIS A 1 301 ? -1.333 -1.322 13.897 1.00 49.63 ? 301 HIS A CE1 1 ATOM 2266 N NE2 . HIS A 1 301 ? -1.074 -0.241 14.612 1.00 49.33 ? 301 HIS A NE2 1 ATOM 2267 N N . ALA A 1 302 ? 4.270 -4.058 14.600 1.00 39.13 ? 302 ALA A N 1 ATOM 2268 C CA . ALA A 1 302 ? 5.479 -4.746 14.131 1.00 39.88 ? 302 ALA A CA 1 ATOM 2269 C C . ALA A 1 302 ? 5.739 -4.452 12.649 1.00 40.47 ? 302 ALA A C 1 ATOM 2270 O O . ALA A 1 302 ? 4.814 -4.499 11.817 1.00 40.49 ? 302 ALA A O 1 ATOM 2271 C CB . ALA A 1 302 ? 5.361 -6.259 14.370 1.00 38.04 ? 302 ALA A CB 1 ATOM 2272 N N . MET A 1 303 ? 6.991 -4.120 12.334 1.00 41.86 ? 303 MET A N 1 ATOM 2273 C CA . MET A 1 303 ? 7.459 -3.985 10.954 1.00 44.98 ? 303 MET A CA 1 ATOM 2274 C C . MET A 1 303 ? 8.911 -4.449 10.836 1.00 42.52 ? 303 MET A C 1 ATOM 2275 O O . MET A 1 303 ? 9.816 -3.899 11.490 1.00 41.61 ? 303 MET A O 1 ATOM 2276 C CB . MET A 1 303 ? 7.332 -2.544 10.455 1.00 46.23 ? 303 MET A CB 1 ATOM 2277 C CG . MET A 1 303 ? 7.357 -2.441 8.941 1.00 50.85 ? 303 MET A CG 1 ATOM 2278 S SD . MET A 1 303 ? 6.537 -0.986 8.231 1.00 56.40 ? 303 MET A SD 1 ATOM 2279 C CE . MET A 1 303 ? 7.953 -0.008 7.695 1.00 54.33 ? 303 MET A CE 1 ATOM 2280 N N . ASP A 1 304 ? 9.130 -5.467 10.009 1.00 41.14 ? 304 ASP A N 1 ATOM 2281 C CA . ASP A 1 304 ? 10.495 -5.921 9.718 1.00 41.11 ? 304 ASP A CA 1 ATOM 2282 C C . ASP A 1 304 ? 11.073 -5.055 8.592 1.00 41.05 ? 304 ASP A C 1 ATOM 2283 O O . ASP A 1 304 ? 10.733 -5.227 7.416 1.00 42.59 ? 304 ASP A O 1 ATOM 2284 C CB . ASP A 1 304 ? 10.529 -7.412 9.356 1.00 38.68 ? 304 ASP A CB 1 ATOM 2285 C CG . ASP A 1 304 ? 10.062 -8.304 10.492 1.00 38.85 ? 304 ASP A CG 1 ATOM 2286 O OD1 . ASP A 1 304 ? 10.414 -8.028 11.664 1.00 33.20 ? 304 ASP A OD1 1 ATOM 2287 O OD2 . ASP A 1 304 ? 9.347 -9.323 10.300 1.00 41.89 ? 304 ASP A OD2 1 ATOM 2288 N N . ILE A 1 305 ? 11.924 -4.106 8.956 1.00 39.58 ? 305 ILE A N 1 ATOM 2289 C CA . ILE A 1 305 ? 12.456 -3.196 7.963 1.00 41.44 ? 305 ILE A CA 1 ATOM 2290 C C . ILE A 1 305 ? 13.724 -3.823 7.378 1.00 44.17 ? 305 ILE A C 1 ATOM 2291 O O . ILE A 1 305 ? 14.646 -4.166 8.129 1.00 42.95 ? 305 ILE A O 1 ATOM 2292 C CB . ILE A 1 305 ? 12.683 -1.796 8.564 1.00 40.79 ? 305 ILE A CB 1 ATOM 2293 C CG1 . ILE A 1 305 ? 11.328 -1.137 8.875 1.00 38.31 ? 305 ILE A CG1 1 ATOM 2294 C CG2 . ILE A 1 305 ? 13.499 -0.912 7.607 1.00 41.99 ? 305 ILE A CG2 1 ATOM 2295 C CD1 . ILE A 1 305 ? 11.462 0.037 9.800 1.00 38.13 ? 305 ILE A CD1 1 ATOM 2296 N N . PRO A 1 306 ? 13.747 -3.983 6.048 1.00 47.67 ? 306 PRO A N 1 ATOM 2297 C CA . PRO A 1 306 ? 14.814 -4.714 5.355 1.00 50.12 ? 306 PRO A CA 1 ATOM 2298 C C . PRO A 1 306 ? 16.083 -3.888 5.227 1.00 51.76 ? 306 PRO A C 1 ATOM 2299 O O . PRO A 1 306 ? 15.996 -2.653 5.150 1.00 51.08 ? 306 PRO A O 1 ATOM 2300 C CB . PRO A 1 306 ? 14.230 -4.960 3.952 1.00 49.49 ? 306 PRO A CB 1 ATOM 2301 C CG . PRO A 1 306 ? 12.812 -4.474 4.007 1.00 50.45 ? 306 PRO A CG 1 ATOM 2302 C CD . PRO A 1 306 ? 12.754 -3.455 5.093 1.00 49.00 ? 306 PRO A CD 1 ATOM 2303 N N . PRO A 1 307 ? 17.242 -4.563 5.197 1.00 53.06 ? 307 PRO A N 1 ATOM 2304 C CA . PRO A 1 307 ? 18.531 -3.904 4.919 1.00 53.20 ? 307 PRO A CA 1 ATOM 2305 C C . PRO A 1 307 ? 18.476 -3.045 3.645 1.00 52.63 ? 307 PRO A C 1 ATOM 2306 O O . PRO A 1 307 ? 17.622 -3.292 2.785 1.00 51.94 ? 307 PRO A O 1 ATOM 2307 C CB . PRO A 1 307 ? 19.498 -5.084 4.738 1.00 53.80 ? 307 PRO A CB 1 ATOM 2308 C CG . PRO A 1 307 ? 18.901 -6.196 5.538 1.00 53.68 ? 307 PRO A CG 1 ATOM 2309 C CD . PRO A 1 307 ? 17.405 -6.013 5.443 1.00 52.88 ? 307 PRO A CD 1 ATOM 2310 N N . PRO A 1 308 ? 19.366 -2.053 3.509 1.00 52.46 ? 308 PRO A N 1 ATOM 2311 C CA . PRO A 1 308 ? 20.443 -1.786 4.477 1.00 52.51 ? 308 PRO A CA 1 ATOM 2312 C C . PRO A 1 308 ? 20.039 -1.021 5.755 1.00 52.50 ? 308 PRO A C 1 ATOM 2313 O O . PRO A 1 308 ? 20.701 -1.179 6.786 1.00 54.79 ? 308 PRO A O 1 ATOM 2314 C CB . PRO A 1 308 ? 21.442 -0.976 3.655 1.00 52.36 ? 308 PRO A CB 1 ATOM 2315 C CG . PRO A 1 308 ? 20.602 -0.256 2.636 1.00 51.40 ? 308 PRO A CG 1 ATOM 2316 C CD . PRO A 1 308 ? 19.411 -1.126 2.359 1.00 51.34 ? 308 PRO A CD 1 ATOM 2317 N N . THR A 1 309 ? 18.974 -0.221 5.699 1.00 51.29 ? 309 THR A N 1 ATOM 2318 C CA . THR A 1 309 ? 18.560 0.594 6.862 1.00 50.18 ? 309 THR A CA 1 ATOM 2319 C C . THR A 1 309 ? 18.064 -0.190 8.096 1.00 47.47 ? 309 THR A C 1 ATOM 2320 O O . THR A 1 309 ? 18.303 0.225 9.241 1.00 45.16 ? 309 THR A O 1 ATOM 2321 C CB . THR A 1 309 ? 17.579 1.745 6.454 1.00 51.00 ? 309 THR A CB 1 ATOM 2322 O OG1 . THR A 1 309 ? 16.524 1.868 7.423 1.00 52.46 ? 309 THR A OG1 1 ATOM 2323 C CG2 . THR A 1 309 ? 16.835 1.409 5.170 1.00 52.55 ? 309 THR A CG2 1 ATOM 2324 N N . GLY A 1 310 ? 17.400 -1.325 7.861 1.00 44.45 ? 310 GLY A N 1 ATOM 2325 C CA . GLY A 1 310 ? 16.954 -2.192 8.950 1.00 43.02 ? 310 GLY A CA 1 ATOM 2326 C C . GLY A 1 310 ? 17.815 -3.444 9.005 1.00 43.39 ? 310 GLY A C 1 ATOM 2327 O O . GLY A 1 310 ? 18.710 -3.590 8.177 1.00 42.20 ? 310 GLY A O 1 ATOM 2328 N N . PRO A 1 311 ? 17.567 -4.365 9.944 1.00 43.88 ? 311 PRO A N 1 ATOM 2329 C CA . PRO A 1 311 ? 16.580 -4.234 11.042 1.00 41.18 ? 311 PRO A CA 1 ATOM 2330 C C . PRO A 1 311 ? 16.694 -3.032 12.001 1.00 39.64 ? 311 PRO A C 1 ATOM 2331 O O . PRO A 1 311 ? 17.780 -2.660 12.433 1.00 38.40 ? 311 PRO A O 1 ATOM 2332 C CB . PRO A 1 311 ? 16.745 -5.555 11.831 1.00 42.54 ? 311 PRO A CB 1 ATOM 2333 C CG . PRO A 1 311 ? 17.970 -6.237 11.294 1.00 41.00 ? 311 PRO A CG 1 ATOM 2334 C CD . PRO A 1 311 ? 18.189 -5.705 9.916 1.00 42.39 ? 311 PRO A CD 1 ATOM 2335 N N . THR A 1 312 ? 15.545 -2.460 12.357 1.00 36.06 ? 312 THR A N 1 ATOM 2336 C CA . THR A 1 312 ? 15.516 -1.217 13.112 1.00 34.55 ? 312 THR A CA 1 ATOM 2337 C C . THR A 1 312 ? 14.119 -0.932 13.689 1.00 34.26 ? 312 THR A C 1 ATOM 2338 O O . THR A 1 312 ? 13.103 -1.410 13.167 1.00 36.69 ? 312 THR A O 1 ATOM 2339 C CB . THR A 1 312 ? 16.016 -0.011 12.225 1.00 30.67 ? 312 THR A CB 1 ATOM 2340 O OG1 . THR A 1 312 ? 16.069 1.190 13.012 1.00 30.63 ? 312 THR A OG1 1 ATOM 2341 C CG2 . THR A 1 312 ? 15.022 0.327 11.138 1.00 31.25 ? 312 THR A CG2 1 ATOM 2342 N N . TRP A 1 313 ? 14.084 -0.182 14.780 1.00 31.18 ? 313 TRP A N 1 ATOM 2343 C CA . TRP A 1 313 ? 12.840 0.419 15.247 1.00 32.14 ? 313 TRP A CA 1 ATOM 2344 C C . TRP A 1 313 ? 12.550 1.622 14.351 1.00 30.78 ? 313 TRP A C 1 ATOM 2345 O O . TRP A 1 313 ? 13.444 2.092 13.640 1.00 27.58 ? 313 TRP A O 1 ATOM 2346 C CB . TRP A 1 313 ? 13.007 0.876 16.684 1.00 33.64 ? 313 TRP A CB 1 ATOM 2347 C CG . TRP A 1 313 ? 13.028 -0.276 17.664 1.00 34.76 ? 313 TRP A CG 1 ATOM 2348 C CD1 . TRP A 1 313 ? 14.034 -1.204 17.845 1.00 33.90 ? 313 TRP A CD1 1 ATOM 2349 C CD2 . TRP A 1 313 ? 11.979 -0.641 18.575 1.00 34.63 ? 313 TRP A CD2 1 ATOM 2350 N NE1 . TRP A 1 313 ? 13.672 -2.103 18.820 1.00 32.72 ? 313 TRP A NE1 1 ATOM 2351 C CE2 . TRP A 1 313 ? 12.423 -1.775 19.294 1.00 34.08 ? 313 TRP A CE2 1 ATOM 2352 C CE3 . TRP A 1 313 ? 10.721 -0.098 18.883 1.00 33.67 ? 313 TRP A CE3 1 ATOM 2353 C CZ2 . TRP A 1 313 ? 11.650 -2.384 20.281 1.00 35.52 ? 313 TRP A CZ2 1 ATOM 2354 C CZ3 . TRP A 1 313 ? 9.945 -0.711 19.870 1.00 33.79 ? 313 TRP A CZ3 1 ATOM 2355 C CH2 . TRP A 1 313 ? 10.420 -1.839 20.560 1.00 33.77 ? 313 TRP A CH2 1 ATOM 2356 N N . ALA A 1 314 ? 11.293 2.066 14.331 1.00 30.65 ? 314 ALA A N 1 ATOM 2357 C CA . ALA A 1 314 ? 10.939 3.329 13.706 1.00 28.76 ? 314 ALA A CA 1 ATOM 2358 C C . ALA A 1 314 ? 10.104 4.163 14.665 1.00 28.59 ? 314 ALA A C 1 ATOM 2359 O O . ALA A 1 314 ? 9.109 3.684 15.215 1.00 27.07 ? 314 ALA A O 1 ATOM 2360 C CB . ALA A 1 314 ? 10.204 3.117 12.404 1.00 27.77 ? 314 ALA A CB 1 ATOM 2361 N N . LEU A 1 315 ? 10.515 5.403 14.876 1.00 24.44 ? 315 LEU A N 1 ATOM 2362 C CA . LEU A 1 315 ? 9.737 6.316 15.711 1.00 25.36 ? 315 LEU A CA 1 ATOM 2363 C C . LEU A 1 315 ? 8.879 7.200 14.806 1.00 26.26 ? 315 LEU A C 1 ATOM 2364 O O . LEU A 1 315 ? 9.378 8.142 14.227 1.00 25.29 ? 315 LEU A O 1 ATOM 2365 C CB . LEU A 1 315 ? 10.672 7.177 16.582 1.00 25.67 ? 315 LEU A CB 1 ATOM 2366 C CG . LEU A 1 315 ? 11.777 6.443 17.375 1.00 27.86 ? 315 LEU A CG 1 ATOM 2367 C CD1 . LEU A 1 315 ? 12.642 7.469 18.144 1.00 24.64 ? 315 LEU A CD1 1 ATOM 2368 C CD2 . LEU A 1 315 ? 11.175 5.366 18.340 1.00 28.54 ? 315 LEU A CD2 1 ATOM 2369 N N . GLY A 1 316 ? 7.595 6.879 14.677 1.00 25.87 ? 316 GLY A N 1 ATOM 2370 C CA . GLY A 1 316 ? 6.717 7.573 13.748 1.00 24.28 ? 316 GLY A CA 1 ATOM 2371 C C . GLY A 1 316 ? 5.971 8.693 14.440 1.00 24.34 ? 316 GLY A C 1 ATOM 2372 O O . GLY A 1 316 ? 6.522 9.351 15.291 1.00 27.22 ? 316 GLY A O 1 ATOM 2373 N N . ALA A 1 317 ? 4.710 8.891 14.073 1.00 21.83 ? 317 ALA A N 1 ATOM 2374 C CA . ALA A 1 317 ? 3.922 10.009 14.552 1.00 25.89 ? 317 ALA A CA 1 ATOM 2375 C C . ALA A 1 317 ? 3.489 9.797 16.003 1.00 24.59 ? 317 ALA A C 1 ATOM 2376 O O . ALA A 1 317 ? 3.393 10.751 16.769 1.00 29.28 ? 317 ALA A O 1 ATOM 2377 C CB . ALA A 1 317 ? 2.693 10.298 13.575 1.00 21.49 ? 317 ALA A CB 1 ATOM 2378 N N . THR A 1 318 ? 3.259 8.544 16.397 1.00 24.76 ? 318 THR A N 1 ATOM 2379 C CA . THR A 1 318 ? 3.043 8.227 17.803 1.00 24.05 ? 318 THR A CA 1 ATOM 2380 C C . THR A 1 318 ? 4.086 8.939 18.703 1.00 25.24 ? 318 THR A C 1 ATOM 2381 O O . THR A 1 318 ? 3.753 9.520 19.752 1.00 22.24 ? 318 THR A O 1 ATOM 2382 C CB . THR A 1 318 ? 3.078 6.701 18.005 1.00 26.86 ? 318 THR A CB 1 ATOM 2383 O OG1 . THR A 1 318 ? 2.002 6.082 17.254 1.00 27.98 ? 318 THR A OG1 1 ATOM 2384 C CG2 . THR A 1 318 ? 2.762 6.356 19.453 1.00 25.65 ? 318 THR A CG2 1 ATOM 2385 N N . PHE A 1 319 ? 5.348 8.876 18.294 1.00 24.22 ? 319 PHE A N 1 ATOM 2386 C CA . PHE A 1 319 ? 6.436 9.439 19.074 1.00 24.35 ? 319 PHE A CA 1 ATOM 2387 C C . PHE A 1 319 ? 6.526 10.953 18.858 1.00 27.32 ? 319 PHE A C 1 ATOM 2388 O O . PHE A 1 319 ? 6.619 11.742 19.822 1.00 25.36 ? 319 PHE A O 1 ATOM 2389 C CB . PHE A 1 319 ? 7.747 8.753 18.698 1.00 25.04 ? 319 PHE A CB 1 ATOM 2390 C CG . PHE A 1 319 ? 8.936 9.188 19.543 1.00 28.30 ? 319 PHE A CG 1 ATOM 2391 C CD1 . PHE A 1 319 ? 9.702 10.295 19.176 1.00 27.85 ? 319 PHE A CD1 1 ATOM 2392 C CD2 . PHE A 1 319 ? 9.301 8.466 20.691 1.00 30.62 ? 319 PHE A CD2 1 ATOM 2393 C CE1 . PHE A 1 319 ? 10.797 10.711 19.962 1.00 26.57 ? 319 PHE A CE1 1 ATOM 2394 C CE2 . PHE A 1 319 ? 10.399 8.881 21.489 1.00 30.59 ? 319 PHE A CE2 1 ATOM 2395 C CZ . PHE A 1 319 ? 11.147 10.000 21.108 1.00 26.74 ? 319 PHE A CZ 1 ATOM 2396 N N . ILE A 1 320 ? 6.475 11.350 17.585 1.00 28.42 ? 320 ILE A N 1 ATOM 2397 C CA . ILE A 1 320 ? 6.572 12.760 17.181 1.00 30.05 ? 320 ILE A CA 1 ATOM 2398 C C . ILE A 1 320 ? 5.476 13.687 17.725 1.00 28.82 ? 320 ILE A C 1 ATOM 2399 O O . ILE A 1 320 ? 5.755 14.875 18.036 1.00 27.40 ? 320 ILE A O 1 ATOM 2400 C CB . ILE A 1 320 ? 6.723 12.859 15.646 1.00 30.25 ? 320 ILE A CB 1 ATOM 2401 C CG1 . ILE A 1 320 ? 8.070 12.249 15.250 1.00 29.23 ? 320 ILE A CG1 1 ATOM 2402 C CG2 . ILE A 1 320 ? 6.615 14.315 15.197 1.00 33.28 ? 320 ILE A CG2 1 ATOM 2403 C CD1 . ILE A 1 320 ? 8.199 11.933 13.808 1.00 29.67 ? 320 ILE A CD1 1 ATOM 2404 N N . ARG A 1 321 ? 4.248 13.164 17.856 1.00 28.90 ? 321 ARG A N 1 ATOM 2405 C CA . ARG A 1 321 ? 3.181 13.899 18.571 1.00 25.79 ? 321 ARG A CA 1 ATOM 2406 C C . ARG A 1 321 ? 3.634 14.412 19.942 1.00 26.76 ? 321 ARG A C 1 ATOM 2407 O O . ARG A 1 321 ? 3.436 15.592 20.251 1.00 29.15 ? 321 ARG A O 1 ATOM 2408 C CB . ARG A 1 321 ? 1.922 13.056 18.769 1.00 25.86 ? 321 ARG A CB 1 ATOM 2409 C CG . ARG A 1 321 ? 0.829 13.234 17.755 1.00 24.75 ? 321 ARG A CG 1 ATOM 2410 C CD . ARG A 1 321 ? -0.535 12.622 18.194 1.00 24.45 ? 321 ARG A CD 1 ATOM 2411 N NE . ARG A 1 321 ? -0.453 11.151 18.301 1.00 23.67 ? 321 ARG A NE 1 ATOM 2412 C CZ . ARG A 1 321 ? -0.406 10.343 17.260 1.00 21.46 ? 321 ARG A CZ 1 ATOM 2413 N NH1 . ARG A 1 321 ? -0.470 10.854 16.044 1.00 22.71 ? 321 ARG A NH1 1 ATOM 2414 N NH2 . ARG A 1 321 ? -0.356 9.025 17.422 1.00 24.35 ? 321 ARG A NH2 1 ATOM 2415 N N . LYS A 1 322 ? 4.223 13.560 20.783 1.00 24.80 ? 322 LYS A N 1 ATOM 2416 C CA . LYS A 1 322 ? 4.640 14.025 22.112 1.00 24.46 ? 322 LYS A CA 1 ATOM 2417 C C . LYS A 1 322 ? 5.902 14.916 22.101 1.00 27.60 ? 322 LYS A C 1 ATOM 2418 O O . LYS A 1 322 ? 5.993 15.861 22.891 1.00 29.93 ? 322 LYS A O 1 ATOM 2419 C CB . LYS A 1 322 ? 4.848 12.869 23.102 1.00 25.97 ? 322 LYS A CB 1 ATOM 2420 C CG . LYS A 1 322 ? 4.670 13.336 24.544 1.00 30.77 ? 322 LYS A CG 1 ATOM 2421 C CD . LYS A 1 322 ? 5.098 12.317 25.575 1.00 33.92 ? 322 LYS A CD 1 ATOM 2422 C CE . LYS A 1 322 ? 4.484 12.640 26.910 1.00 33.80 ? 322 LYS A CE 1 ATOM 2423 N NZ . LYS A 1 322 ? 4.505 11.470 27.813 1.00 34.62 ? 322 LYS A NZ 1 ATOM 2424 N N . PHE A 1 323 ? 6.854 14.578 21.226 1.00 25.18 ? 323 PHE A N 1 ATOM 2425 C CA . PHE A 1 323 ? 8.166 15.232 21.130 1.00 25.33 ? 323 PHE A CA 1 ATOM 2426 C C . PHE A 1 323 ? 8.403 15.919 19.801 1.00 24.57 ? 323 PHE A C 1 ATOM 2427 O O . PHE A 1 323 ? 8.592 15.284 18.760 1.00 26.35 ? 323 PHE A O 1 ATOM 2428 C CB . PHE A 1 323 ? 9.292 14.255 21.440 1.00 27.40 ? 323 PHE A CB 1 ATOM 2429 C CG . PHE A 1 323 ? 9.107 13.552 22.751 1.00 30.02 ? 323 PHE A CG 1 ATOM 2430 C CD1 . PHE A 1 323 ? 9.277 14.239 23.950 1.00 28.53 ? 323 PHE A CD1 1 ATOM 2431 C CD2 . PHE A 1 323 ? 8.698 12.215 22.788 1.00 28.50 ? 323 PHE A CD2 1 ATOM 2432 C CE1 . PHE A 1 323 ? 9.076 13.606 25.154 1.00 28.54 ? 323 PHE A CE1 1 ATOM 2433 C CE2 . PHE A 1 323 ? 8.485 11.576 23.996 1.00 28.51 ? 323 PHE A CE2 1 ATOM 2434 C CZ . PHE A 1 323 ? 8.674 12.269 25.181 1.00 27.72 ? 323 PHE A CZ 1 ATOM 2435 N N . TYR A 1 324 ? 8.374 17.241 19.865 1.00 27.05 ? 324 TYR A N 1 ATOM 2436 C CA . TYR A 1 324 ? 8.677 18.127 18.748 1.00 26.67 ? 324 TYR A CA 1 ATOM 2437 C C . TYR A 1 324 ? 10.085 17.786 18.236 1.00 29.41 ? 324 TYR A C 1 ATOM 2438 O O . TYR A 1 324 ? 11.013 17.614 19.037 1.00 29.91 ? 324 TYR A O 1 ATOM 2439 C CB . TYR A 1 324 ? 8.579 19.577 19.247 1.00 27.79 ? 324 TYR A CB 1 ATOM 2440 C CG . TYR A 1 324 ? 8.668 20.629 18.163 1.00 27.57 ? 324 TYR A CG 1 ATOM 2441 C CD1 . TYR A 1 324 ? 9.885 20.946 17.592 1.00 28.41 ? 324 TYR A CD1 1 ATOM 2442 C CD2 . TYR A 1 324 ? 7.532 21.298 17.708 1.00 26.31 ? 324 TYR A CD2 1 ATOM 2443 C CE1 . TYR A 1 324 ? 9.990 21.902 16.601 1.00 27.95 ? 324 TYR A CE1 1 ATOM 2444 C CE2 . TYR A 1 324 ? 7.629 22.279 16.710 1.00 29.04 ? 324 TYR A CE2 1 ATOM 2445 C CZ . TYR A 1 324 ? 8.868 22.576 16.171 1.00 27.46 ? 324 TYR A CZ 1 ATOM 2446 O OH . TYR A 1 324 ? 9.009 23.512 15.168 1.00 29.17 ? 324 TYR A OH 1 ATOM 2447 N N . THR A 1 325 ? 10.250 17.645 16.917 1.00 27.43 ? 325 THR A N 1 ATOM 2448 C CA . THR A 1 325 ? 11.504 17.075 16.382 1.00 27.47 ? 325 THR A CA 1 ATOM 2449 C C . THR A 1 325 ? 12.179 18.029 15.409 1.00 29.52 ? 325 THR A C 1 ATOM 2450 O O . THR A 1 325 ? 11.525 18.534 14.497 1.00 30.25 ? 325 THR A O 1 ATOM 2451 C CB . THR A 1 325 ? 11.228 15.722 15.640 1.00 24.23 ? 325 THR A CB 1 ATOM 2452 O OG1 . THR A 1 325 ? 10.637 14.792 16.537 1.00 24.92 ? 325 THR A OG1 1 ATOM 2453 C CG2 . THR A 1 325 ? 12.574 15.034 15.249 1.00 22.86 ? 325 THR A CG2 1 ATOM 2454 N N . GLU A 1 326 ? 13.479 18.260 15.588 1.00 29.96 ? 326 GLU A N 1 ATOM 2455 C CA . GLU A 1 326 ? 14.253 19.066 14.630 1.00 28.10 ? 326 GLU A CA 1 ATOM 2456 C C . GLU A 1 326 ? 15.330 18.224 13.973 1.00 26.13 ? 326 GLU A C 1 ATOM 2457 O O . GLU A 1 326 ? 16.058 17.499 14.649 1.00 27.08 ? 326 GLU A O 1 ATOM 2458 C CB . GLU A 1 326 ? 14.848 20.310 15.295 1.00 30.62 ? 326 GLU A CB 1 ATOM 2459 C CG . GLU A 1 326 ? 15.749 21.127 14.398 1.00 34.25 ? 326 GLU A CG 1 ATOM 2460 C CD . GLU A 1 326 ? 16.542 22.141 15.193 1.00 38.49 ? 326 GLU A CD 1 ATOM 2461 O OE1 . GLU A 1 326 ? 17.695 21.815 15.581 1.00 39.37 ? 326 GLU A OE1 1 ATOM 2462 O OE2 . GLU A 1 326 ? 15.993 23.238 15.462 1.00 37.03 ? 326 GLU A OE2 1 ATOM 2463 N N . PHE A 1 327 ? 15.389 18.318 12.640 1.00 25.16 ? 327 PHE A N 1 ATOM 2464 C CA . PHE A 1 327 ? 16.300 17.550 11.822 1.00 26.63 ? 327 PHE A CA 1 ATOM 2465 C C . PHE A 1 327 ? 17.366 18.497 11.327 1.00 27.10 ? 327 PHE A C 1 ATOM 2466 O O . PHE A 1 327 ? 17.078 19.458 10.618 1.00 26.28 ? 327 PHE A O 1 ATOM 2467 C CB . PHE A 1 327 ? 15.542 16.891 10.668 1.00 26.48 ? 327 PHE A CB 1 ATOM 2468 C CG . PHE A 1 327 ? 14.558 15.843 11.123 1.00 27.17 ? 327 PHE A CG 1 ATOM 2469 C CD1 . PHE A 1 327 ? 14.981 14.534 11.378 1.00 26.23 ? 327 PHE A CD1 1 ATOM 2470 C CD2 . PHE A 1 327 ? 13.221 16.169 11.321 1.00 25.80 ? 327 PHE A CD2 1 ATOM 2471 C CE1 . PHE A 1 327 ? 14.079 13.578 11.830 1.00 27.94 ? 327 PHE A CE1 1 ATOM 2472 C CE2 . PHE A 1 327 ? 12.314 15.211 11.753 1.00 25.95 ? 327 PHE A CE2 1 ATOM 2473 C CZ . PHE A 1 327 ? 12.753 13.913 12.016 1.00 28.04 ? 327 PHE A CZ 1 ATOM 2474 N N . ASP A 1 328 ? 18.595 18.216 11.729 1.00 27.77 ? 328 ASP A N 1 ATOM 2475 C CA . ASP A 1 328 ? 19.694 19.166 11.570 1.00 29.42 ? 328 ASP A CA 1 ATOM 2476 C C . ASP A 1 328 ? 20.739 18.607 10.599 1.00 29.92 ? 328 ASP A C 1 ATOM 2477 O O . ASP A 1 328 ? 21.506 17.704 10.951 1.00 33.00 ? 328 ASP A O 1 ATOM 2478 C CB . ASP A 1 328 ? 20.248 19.500 12.953 1.00 31.40 ? 328 ASP A CB 1 ATOM 2479 C CG . ASP A 1 328 ? 21.383 20.528 12.935 1.00 33.35 ? 328 ASP A CG 1 ATOM 2480 O OD1 . ASP A 1 328 ? 22.009 20.762 11.889 1.00 32.85 ? 328 ASP A OD1 1 ATOM 2481 O OD2 . ASP A 1 328 ? 21.730 21.132 13.969 1.00 33.95 ? 328 ASP A OD2 1 ATOM 2482 N N . ARG A 1 329 ? 20.751 19.147 9.377 1.00 29.71 ? 329 ARG A N 1 ATOM 2483 C CA . ARG A 1 329 ? 21.680 18.704 8.324 1.00 32.74 ? 329 ARG A CA 1 ATOM 2484 C C . ARG A 1 329 ? 23.079 19.254 8.503 1.00 33.29 ? 329 ARG A C 1 ATOM 2485 O O . ARG A 1 329 ? 24.049 18.585 8.170 1.00 34.03 ? 329 ARG A O 1 ATOM 2486 C CB . ARG A 1 329 ? 21.172 19.121 6.936 1.00 33.77 ? 329 ARG A CB 1 ATOM 2487 C CG . ARG A 1 329 ? 20.101 18.223 6.363 1.00 34.19 ? 329 ARG A CG 1 ATOM 2488 C CD . ARG A 1 329 ? 20.565 16.806 6.082 1.00 34.83 ? 329 ARG A CD 1 ATOM 2489 N NE . ARG A 1 329 ? 21.641 16.779 5.088 1.00 36.26 ? 329 ARG A NE 1 ATOM 2490 C CZ . ARG A 1 329 ? 21.472 16.850 3.768 1.00 37.79 ? 329 ARG A CZ 1 ATOM 2491 N NH1 . ARG A 1 329 ? 20.260 16.966 3.227 1.00 33.90 ? 329 ARG A NH1 1 ATOM 2492 N NH2 . ARG A 1 329 ? 22.540 16.826 2.979 1.00 39.68 ? 329 ARG A NH2 1 ATOM 2493 N N . ARG A 1 330 ? 23.158 20.486 9.000 1.00 35.00 ? 330 ARG A N 1 ATOM 2494 C CA . ARG A 1 330 ? 24.421 21.179 9.302 1.00 35.47 ? 330 ARG A CA 1 ATOM 2495 C C . ARG A 1 330 ? 25.336 20.359 10.231 1.00 36.72 ? 330 ARG A C 1 ATOM 2496 O O . ARG A 1 330 ? 26.540 20.220 9.984 1.00 38.44 ? 330 ARG A O 1 ATOM 2497 C CB . ARG A 1 330 ? 24.089 22.510 9.984 1.00 34.26 ? 330 ARG A CB 1 ATOM 2498 C CG . ARG A 1 330 ? 25.300 23.347 10.392 1.00 34.12 ? 330 ARG A CG 1 ATOM 2499 C CD . ARG A 1 330 ? 25.976 24.017 9.235 1.00 30.72 ? 330 ARG A CD 1 ATOM 2500 N NE . ARG A 1 330 ? 27.178 24.789 9.587 1.00 27.26 ? 330 ARG A NE 1 ATOM 2501 C CZ . ARG A 1 330 ? 28.092 25.097 8.684 1.00 25.50 ? 330 ARG A CZ 1 ATOM 2502 N NH1 . ARG A 1 330 ? 27.909 24.679 7.451 1.00 27.70 ? 330 ARG A NH1 1 ATOM 2503 N NH2 . ARG A 1 330 ? 29.181 25.792 8.994 1.00 25.75 ? 330 ARG A NH2 1 ATOM 2504 N N . ASN A 1 331 ? 24.741 19.837 11.301 1.00 35.59 ? 331 ASN A N 1 ATOM 2505 C CA . ASN A 1 331 ? 25.452 19.149 12.359 1.00 36.14 ? 331 ASN A CA 1 ATOM 2506 C C . ASN A 1 331 ? 25.186 17.631 12.421 1.00 37.63 ? 331 ASN A C 1 ATOM 2507 O O . ASN A 1 331 ? 25.704 16.950 13.311 1.00 39.70 ? 331 ASN A O 1 ATOM 2508 C CB . ASN A 1 331 ? 25.156 19.839 13.708 1.00 34.70 ? 331 ASN A CB 1 ATOM 2509 C CG . ASN A 1 331 ? 25.692 21.274 13.763 1.00 35.59 ? 331 ASN A CG 1 ATOM 2510 O OD1 . ASN A 1 331 ? 24.957 22.234 14.030 1.00 37.81 ? 331 ASN A OD1 1 ATOM 2511 N ND2 . ASN A 1 331 ? 26.971 21.423 13.488 1.00 33.95 ? 331 ASN A ND2 1 ATOM 2512 N N . ASN A 1 332 ? 24.413 17.108 11.462 1.00 38.54 ? 332 ASN A N 1 ATOM 2513 C CA . ASN A 1 332 ? 24.008 15.685 11.427 1.00 37.11 ? 332 ASN A CA 1 ATOM 2514 C C . ASN A 1 332 ? 23.507 15.146 12.763 1.00 36.50 ? 332 ASN A C 1 ATOM 2515 O O . ASN A 1 332 ? 24.064 14.188 13.325 1.00 35.14 ? 332 ASN A O 1 ATOM 2516 C CB . ASN A 1 332 ? 25.114 14.800 10.860 1.00 39.27 ? 332 ASN A CB 1 ATOM 2517 C CG . ASN A 1 332 ? 25.272 14.960 9.363 1.00 41.39 ? 332 ASN A CG 1 ATOM 2518 O OD1 . ASN A 1 332 ? 24.337 14.714 8.585 1.00 39.98 ? 332 ASN A OD1 1 ATOM 2519 N ND2 . ASN A 1 332 ? 26.474 15.362 8.941 1.00 41.64 ? 332 ASN A ND2 1 ATOM 2520 N N . ARG A 1 333 ? 22.443 15.772 13.266 1.00 33.20 ? 333 ARG A N 1 ATOM 2521 C CA . ARG A 1 333 ? 21.815 15.341 14.507 1.00 33.59 ? 333 ARG A CA 1 ATOM 2522 C C . ARG A 1 333 ? 20.318 15.557 14.472 1.00 34.19 ? 333 ARG A C 1 ATOM 2523 O O . ARG A 1 333 ? 19.809 16.210 13.577 1.00 34.09 ? 333 ARG A O 1 ATOM 2524 C CB . ARG A 1 333 ? 22.405 16.048 15.734 1.00 33.03 ? 333 ARG A CB 1 ATOM 2525 C CG . ARG A 1 333 ? 23.092 17.342 15.453 1.00 37.40 ? 333 ARG A CG 1 ATOM 2526 C CD . ARG A 1 333 ? 22.355 18.590 15.850 1.00 40.07 ? 333 ARG A CD 1 ATOM 2527 N NE . ARG A 1 333 ? 23.004 19.186 17.001 1.00 39.72 ? 333 ARG A NE 1 ATOM 2528 C CZ . ARG A 1 333 ? 22.879 20.445 17.407 1.00 41.16 ? 333 ARG A CZ 1 ATOM 2529 N NH1 . ARG A 1 333 ? 22.113 21.315 16.767 1.00 42.34 ? 333 ARG A NH1 1 ATOM 2530 N NH2 . ARG A 1 333 ? 23.528 20.831 18.489 1.00 39.88 ? 333 ARG A NH2 1 ATOM 2531 N N . ILE A 1 334 ? 19.634 14.983 15.459 1.00 34.69 ? 334 ILE A N 1 ATOM 2532 C CA . ILE A 1 334 ? 18.198 15.158 15.672 1.00 33.85 ? 334 ILE A CA 1 ATOM 2533 C C . ILE A 1 334 ? 17.972 15.716 17.082 1.00 32.55 ? 334 ILE A C 1 ATOM 2534 O O . ILE A 1 334 ? 18.501 15.187 18.060 1.00 34.62 ? 334 ILE A O 1 ATOM 2535 C CB . ILE A 1 334 ? 17.431 13.800 15.464 1.00 32.76 ? 334 ILE A CB 1 ATOM 2536 C CG1 . ILE A 1 334 ? 17.556 13.337 14.005 1.00 33.46 ? 334 ILE A CG1 1 ATOM 2537 C CG2 . ILE A 1 334 ? 15.976 13.946 15.881 1.00 31.30 ? 334 ILE A CG2 1 ATOM 2538 C CD1 . ILE A 1 334 ? 17.220 11.868 13.743 1.00 34.19 ? 334 ILE A CD1 1 ATOM 2539 N N . GLY A 1 335 ? 17.194 16.785 17.181 1.00 29.30 ? 335 GLY A N 1 ATOM 2540 C CA . GLY A 1 335 ? 16.832 17.347 18.457 1.00 27.08 ? 335 GLY A CA 1 ATOM 2541 C C . GLY A 1 335 ? 15.386 17.050 18.809 1.00 30.99 ? 335 GLY A C 1 ATOM 2542 O O . GLY A 1 335 ? 14.496 17.089 17.929 1.00 28.53 ? 335 GLY A O 1 ATOM 2543 N N . PHE A 1 336 ? 15.156 16.724 20.081 1.00 29.61 ? 336 PHE A N 1 ATOM 2544 C CA . PHE A 1 336 ? 13.795 16.525 20.594 1.00 31.11 ? 336 PHE A CA 1 ATOM 2545 C C . PHE A 1 336 ? 13.448 17.547 21.659 1.00 29.42 ? 336 PHE A C 1 ATOM 2546 O O . PHE A 1 336 ? 14.255 17.816 22.549 1.00 31.45 ? 336 PHE A O 1 ATOM 2547 C CB . PHE A 1 336 ? 13.629 15.110 21.165 1.00 27.80 ? 336 PHE A CB 1 ATOM 2548 C CG . PHE A 1 336 ? 13.637 14.035 20.122 1.00 29.55 ? 336 PHE A CG 1 ATOM 2549 C CD1 . PHE A 1 336 ? 12.652 13.993 19.157 1.00 27.43 ? 336 PHE A CD1 1 ATOM 2550 C CD2 . PHE A 1 336 ? 14.633 13.055 20.115 1.00 27.72 ? 336 PHE A CD2 1 ATOM 2551 C CE1 . PHE A 1 336 ? 12.634 13.011 18.202 1.00 28.94 ? 336 PHE A CE1 1 ATOM 2552 C CE2 . PHE A 1 336 ? 14.628 12.059 19.163 1.00 27.03 ? 336 PHE A CE2 1 ATOM 2553 C CZ . PHE A 1 336 ? 13.622 12.044 18.188 1.00 28.33 ? 336 PHE A CZ 1 ATOM 2554 N N . ALA A 1 337 ? 12.233 18.085 21.594 1.00 30.01 ? 337 ALA A N 1 ATOM 2555 C CA . ALA A 1 337 ? 11.685 18.905 22.691 1.00 29.47 ? 337 ALA A CA 1 ATOM 2556 C C . ALA A 1 337 ? 10.227 18.526 22.976 1.00 31.44 ? 337 ALA A C 1 ATOM 2557 O O . ALA A 1 337 ? 9.532 18.053 22.098 1.00 32.07 ? 337 ALA A O 1 ATOM 2558 C CB . ALA A 1 337 ? 11.808 20.393 22.370 1.00 29.98 ? 337 ALA A CB 1 ATOM 2559 N N . LEU A 1 338 ? 9.756 18.736 24.198 1.00 34.15 ? 338 LEU A N 1 ATOM 2560 C CA . LEU A 1 338 ? 8.394 18.351 24.540 1.00 35.38 ? 338 LEU A CA 1 ATOM 2561 C C . LEU A 1 338 ? 7.420 19.302 23.845 1.00 37.76 ? 338 LEU A C 1 ATOM 2562 O O . LEU A 1 338 ? 7.512 20.523 24.018 1.00 38.11 ? 338 LEU A O 1 ATOM 2563 C CB . LEU A 1 338 ? 8.193 18.348 26.057 1.00 37.05 ? 338 LEU A CB 1 ATOM 2564 C CG . LEU A 1 338 ? 6.840 17.903 26.637 1.00 36.18 ? 338 LEU A CG 1 ATOM 2565 C CD1 . LEU A 1 338 ? 6.750 16.373 26.697 1.00 33.23 ? 338 LEU A CD1 1 ATOM 2566 C CD2 . LEU A 1 338 ? 6.595 18.538 28.012 1.00 36.95 ? 338 LEU A CD2 1 ATOM 2567 N N . ALA A 1 339 ? 6.499 18.731 23.059 1.00 34.29 ? 339 ALA A N 1 ATOM 2568 C CA . ALA A 1 339 ? 5.537 19.511 22.299 1.00 36.33 ? 339 ALA A CA 1 ATOM 2569 C C . ALA A 1 339 ? 4.525 20.177 23.211 1.00 36.70 ? 339 ALA A C 1 ATOM 2570 O O . ALA A 1 339 ? 4.055 19.583 24.175 1.00 36.65 ? 339 ALA A O 1 ATOM 2571 C CB . ALA A 1 339 ? 4.820 18.636 21.272 1.00 32.23 ? 339 ALA A CB 1 ATOM 2572 N N . ARG A 1 340 ? 4.210 21.424 22.897 1.00 40.63 ? 340 ARG A N 1 ATOM 2573 C CA . ARG A 1 340 ? 3.111 22.134 23.523 1.00 43.04 ? 340 ARG A CA 1 ATOM 2574 C C . ARG A 1 340 ? 1.879 21.885 22.682 1.00 44.64 ? 340 ARG A C 1 ATOM 2575 O O . ARG A 1 340 ? 1.890 22.092 21.467 1.00 42.66 ? 340 ARG A O 1 ATOM 2576 C CB . ARG A 1 340 ? 3.384 23.632 23.562 1.00 44.78 ? 340 ARG A CB 1 ATOM 2577 C CG . ARG A 1 340 ? 3.577 24.198 24.931 1.00 47.77 ? 340 ARG A CG 1 ATOM 2578 C CD . ARG A 1 340 ? 3.448 25.716 24.976 1.00 49.27 ? 340 ARG A CD 1 ATOM 2579 N NE . ARG A 1 340 ? 4.598 26.374 24.366 1.00 50.52 ? 340 ARG A NE 1 ATOM 2580 C CZ . ARG A 1 340 ? 5.603 26.931 25.043 1.00 52.91 ? 340 ARG A CZ 1 ATOM 2581 N NH1 . ARG A 1 340 ? 5.617 26.921 26.375 1.00 53.81 ? 340 ARG A NH1 1 ATOM 2582 N NH2 . ARG A 1 340 ? 6.608 27.500 24.384 1.00 52.54 ? 340 ARG A NH2 1 ATOM 2583 N N . HIS A 1 341 ? 0.830 21.409 23.338 1.00 47.22 ? 341 HIS A N 1 ATOM 2584 C CA . HIS A 1 341 ? -0.472 21.264 22.721 1.00 49.34 ? 341 HIS A CA 1 ATOM 2585 C C . HIS A 1 341 ? -1.411 22.186 23.490 1.00 51.95 ? 341 HIS A C 1 ATOM 2586 O O . HIS A 1 341 ? -2.139 22.997 22.899 1.00 52.34 ? 341 HIS A O 1 ATOM 2587 C CB . HIS A 1 341 ? -0.948 19.796 22.746 1.00 47.26 ? 341 HIS A CB 1 ATOM 2588 C CG . HIS A 1 341 ? -0.097 18.862 21.928 1.00 46.81 ? 341 HIS A CG 1 ATOM 2589 N ND1 . HIS A 1 341 ? 0.502 17.737 22.456 1.00 46.33 ? 341 HIS A ND1 1 ATOM 2590 C CD2 . HIS A 1 341 ? 0.253 18.889 20.618 1.00 45.73 ? 341 HIS A CD2 1 ATOM 2591 C CE1 . HIS A 1 341 ? 1.184 17.115 21.509 1.00 45.22 ? 341 HIS A CE1 1 ATOM 2592 N NE2 . HIS A 1 341 ? 1.049 17.792 20.383 1.00 43.08 ? 341 HIS A NE2 1 ATOM 2593 O OXT . HIS A 1 341 ? -1.421 22.162 24.729 1.00 54.25 ? 341 HIS A OXT 1 ATOM 2594 N N . LEU B 1 1 ? 27.828 36.363 95.039 1.00 26.08 ? 1 LEU B N 1 ATOM 2595 C CA . LEU B 1 1 ? 27.538 35.773 96.363 1.00 28.51 ? 1 LEU B CA 1 ATOM 2596 C C . LEU B 1 1 ? 26.090 36.008 96.664 1.00 30.46 ? 1 LEU B C 1 ATOM 2597 O O . LEU B 1 1 ? 25.530 37.043 96.295 1.00 29.43 ? 1 LEU B O 1 ATOM 2598 C CB . LEU B 1 1 ? 28.378 36.429 97.464 1.00 27.34 ? 1 LEU B CB 1 ATOM 2599 C CG . LEU B 1 1 ? 29.898 36.385 97.313 1.00 28.55 ? 1 LEU B CG 1 ATOM 2600 C CD1 . LEU B 1 1 ? 30.520 37.254 98.409 1.00 31.44 ? 1 LEU B CD1 1 ATOM 2601 C CD2 . LEU B 1 1 ? 30.409 34.972 97.355 1.00 27.72 ? 1 LEU B CD2 1 ATOM 2602 N N . THR B 1 2 ? 25.504 35.062 97.380 1.00 30.27 ? 2 THR B N 1 ATOM 2603 C CA . THR B 1 2 ? 24.081 35.053 97.648 1.00 35.52 ? 2 THR B CA 1 ATOM 2604 C C . THR B 1 2 ? 23.827 34.645 99.105 1.00 37.75 ? 2 THR B C 1 ATOM 2605 O O . THR B 1 2 ? 24.640 33.913 99.690 1.00 35.40 ? 2 THR B O 1 ATOM 2606 C CB . THR B 1 2 ? 23.420 34.062 96.651 1.00 39.15 ? 2 THR B CB 1 ATOM 2607 O OG1 . THR B 1 2 ? 22.736 34.798 95.618 1.00 42.96 ? 2 THR B OG1 1 ATOM 2608 C CG2 . THR B 1 2 ? 22.341 33.256 97.316 1.00 37.46 ? 2 THR B CG2 1 ATOM 2609 N N . LEU B 1 3 ? 22.723 35.134 99.690 1.00 35.73 ? 3 LEU B N 1 ATOM 2610 C CA . LEU B 1 3 ? 22.344 34.777 101.062 1.00 35.88 ? 3 LEU B CA 1 ATOM 2611 C C . LEU B 1 3 ? 21.099 33.889 101.179 1.00 36.43 ? 3 LEU B C 1 ATOM 2612 O O . LEU B 1 3 ? 20.534 33.786 102.247 1.00 38.97 ? 3 LEU B O 1 ATOM 2613 C CB . LEU B 1 3 ? 22.164 36.027 101.921 1.00 35.70 ? 3 LEU B CB 1 ATOM 2614 C CG . LEU B 1 3 ? 23.305 37.050 101.959 1.00 37.52 ? 3 LEU B CG 1 ATOM 2615 C CD1 . LEU B 1 3 ? 22.896 38.284 102.711 1.00 37.85 ? 3 LEU B CD1 1 ATOM 2616 C CD2 . LEU B 1 3 ? 24.547 36.447 102.599 1.00 35.98 ? 3 LEU B CD2 1 ATOM 2617 N N . GLY B 1 4 ? 20.687 33.236 100.096 1.00 36.29 ? 4 GLY B N 1 ATOM 2618 C CA . GLY B 1 4 ? 19.565 32.295 100.138 1.00 34.60 ? 4 GLY B CA 1 ATOM 2619 C C . GLY B 1 4 ? 18.194 32.897 99.909 1.00 38.14 ? 4 GLY B C 1 ATOM 2620 O O . GLY B 1 4 ? 17.166 32.218 100.106 1.00 41.17 ? 4 GLY B O 1 ATOM 2621 N N . ASN B 1 5 ? 18.152 34.160 99.491 1.00 36.29 ? 5 ASN B N 1 ATOM 2622 C CA . ASN B 1 5 ? 16.872 34.865 99.323 1.00 33.54 ? 5 ASN B CA 1 ATOM 2623 C C . ASN B 1 5 ? 16.748 35.593 97.975 1.00 30.51 ? 5 ASN B C 1 ATOM 2624 O O . ASN B 1 5 ? 15.816 36.360 97.747 1.00 28.79 ? 5 ASN B O 1 ATOM 2625 C CB . ASN B 1 5 ? 16.643 35.832 100.501 1.00 33.93 ? 5 ASN B CB 1 ATOM 2626 C CG . ASN B 1 5 ? 15.160 36.091 100.775 1.00 35.11 ? 5 ASN B CG 1 ATOM 2627 O OD1 . ASN B 1 5 ? 14.310 35.224 100.531 1.00 36.01 ? 5 ASN B OD1 1 ATOM 2628 N ND2 . ASN B 1 5 ? 14.842 37.296 101.263 1.00 32.85 ? 5 ASN B ND2 1 ATOM 2629 N N . THR B 1 6 ? 17.666 35.344 97.053 1.00 28.90 ? 6 THR B N 1 ATOM 2630 C CA . THR B 1 6 ? 17.581 36.068 95.768 1.00 28.31 ? 6 THR B CA 1 ATOM 2631 C C . THR B 1 6 ? 16.800 35.432 94.594 1.00 28.07 ? 6 THR B C 1 ATOM 2632 O O . THR B 1 6 ? 16.876 34.218 94.332 1.00 28.39 ? 6 THR B O 1 ATOM 2633 C CB . THR B 1 6 ? 18.933 36.763 95.373 1.00 28.36 ? 6 THR B CB 1 ATOM 2634 O OG1 . THR B 1 6 ? 19.241 36.532 93.994 1.00 32.22 ? 6 THR B OG1 1 ATOM 2635 C CG2 . THR B 1 6 ? 20.063 36.163 96.057 1.00 26.65 ? 6 THR B CG2 1 ATOM 2636 N N . THR B 1 7 ? 15.969 36.268 93.965 1.00 28.81 ? 7 THR B N 1 ATOM 2637 C CA . THR B 1 7 ? 15.240 35.924 92.768 1.00 28.93 ? 7 THR B CA 1 ATOM 2638 C C . THR B 1 7 ? 15.416 37.046 91.748 1.00 29.65 ? 7 THR B C 1 ATOM 2639 O O . THR B 1 7 ? 15.880 38.148 92.085 1.00 27.78 ? 7 THR B O 1 ATOM 2640 C CB . THR B 1 7 ? 13.708 35.722 93.032 1.00 30.85 ? 7 THR B CB 1 ATOM 2641 O OG1 . THR B 1 7 ? 13.099 36.971 93.400 1.00 27.48 ? 7 THR B OG1 1 ATOM 2642 C CG2 . THR B 1 7 ? 13.449 34.789 94.224 1.00 28.94 ? 7 THR B CG2 1 ATOM 2643 N N . SER B 1 8 ? 15.070 36.733 90.501 1.00 31.14 ? 8 SER B N 1 ATOM 2644 C CA . SER B 1 8 ? 14.956 37.744 89.443 1.00 33.18 ? 8 SER B CA 1 ATOM 2645 C C . SER B 1 8 ? 13.644 37.571 88.657 1.00 30.37 ? 8 SER B C 1 ATOM 2646 O O . SER B 1 8 ? 13.012 36.485 88.675 1.00 32.01 ? 8 SER B O 1 ATOM 2647 C CB . SER B 1 8 ? 16.186 37.731 88.528 1.00 35.24 ? 8 SER B CB 1 ATOM 2648 O OG . SER B 1 8 ? 15.999 36.933 87.373 1.00 40.11 ? 8 SER B OG 1 ATOM 2649 N N . SER B 1 9 ? 13.224 38.649 88.001 1.00 28.87 ? 9 SER B N 1 ATOM 2650 C CA . SER B 1 9 ? 11.930 38.708 87.322 1.00 28.29 ? 9 SER B CA 1 ATOM 2651 C C . SER B 1 9 ? 12.158 39.291 85.961 1.00 29.44 ? 9 SER B C 1 ATOM 2652 O O . SER B 1 9 ? 13.054 40.165 85.805 1.00 25.39 ? 9 SER B O 1 ATOM 2653 C CB . SER B 1 9 ? 10.966 39.641 88.039 1.00 27.76 ? 9 SER B CB 1 ATOM 2654 O OG . SER B 1 9 ? 10.880 39.317 89.399 1.00 36.97 ? 9 SER B OG 1 ATOM 2655 N N . VAL B 1 10 ? 11.355 38.810 85.003 1.00 22.58 ? 10 VAL B N 1 ATOM 2656 C CA . VAL B 1 10 ? 11.253 39.390 83.674 1.00 25.56 ? 10 VAL B CA 1 ATOM 2657 C C . VAL B 1 10 ? 9.810 39.829 83.406 1.00 24.86 ? 10 VAL B C 1 ATOM 2658 O O . VAL B 1 10 ? 8.868 39.057 83.627 1.00 22.73 ? 10 VAL B O 1 ATOM 2659 C CB . VAL B 1 10 ? 11.750 38.407 82.555 1.00 27.04 ? 10 VAL B CB 1 ATOM 2660 C CG1 . VAL B 1 10 ? 11.818 39.110 81.210 1.00 28.15 ? 10 VAL B CG1 1 ATOM 2661 C CG2 . VAL B 1 10 ? 13.175 37.863 82.873 1.00 25.25 ? 10 VAL B CG2 1 ATOM 2662 N N . ILE B 1 11 ? 9.646 41.064 82.930 1.00 25.37 ? 11 ILE B N 1 ATOM 2663 C CA . ILE B 1 11 ? 8.333 41.632 82.545 1.00 24.50 ? 11 ILE B CA 1 ATOM 2664 C C . ILE B 1 11 ? 7.894 41.241 81.118 1.00 20.76 ? 11 ILE B C 1 ATOM 2665 O O . ILE B 1 11 ? 8.651 41.428 80.161 1.00 23.54 ? 11 ILE B O 1 ATOM 2666 C CB . ILE B 1 11 ? 8.391 43.179 82.628 1.00 28.96 ? 11 ILE B CB 1 ATOM 2667 C CG1 . ILE B 1 11 ? 8.989 43.655 83.956 1.00 30.24 ? 11 ILE B CG1 1 ATOM 2668 C CG2 . ILE B 1 11 ? 7.026 43.788 82.360 1.00 28.78 ? 11 ILE B CG2 1 ATOM 2669 C CD1 . ILE B 1 11 ? 8.103 43.453 85.146 1.00 31.31 ? 11 ILE B CD1 1 ATOM 2670 N N . LEU B 1 12 ? 6.664 40.756 80.961 1.00 16.65 ? 12 LEU B N 1 ATOM 2671 C CA . LEU B 1 12 ? 6.183 40.272 79.666 1.00 16.51 ? 12 LEU B CA 1 ATOM 2672 C C . LEU B 1 12 ? 5.196 41.263 79.060 1.00 19.15 ? 12 LEU B C 1 ATOM 2673 O O . LEU B 1 12 ? 4.482 41.962 79.799 1.00 19.96 ? 12 LEU B O 1 ATOM 2674 C CB . LEU B 1 12 ? 5.535 38.878 79.813 1.00 17.10 ? 12 LEU B CB 1 ATOM 2675 C CG . LEU B 1 12 ? 6.372 37.779 80.552 1.00 19.96 ? 12 LEU B CG 1 ATOM 2676 C CD1 . LEU B 1 12 ? 5.734 36.397 80.493 1.00 24.57 ? 12 LEU B CD1 1 ATOM 2677 C CD2 . LEU B 1 12 ? 7.755 37.669 79.909 1.00 19.03 ? 12 LEU B CD2 1 ATOM 2678 N N . THR B 1 13 ? 5.164 41.308 77.733 1.00 19.59 ? 13 THR B N 1 ATOM 2679 C CA . THR B 1 13 ? 4.119 41.955 76.966 1.00 22.68 ? 13 THR B CA 1 ATOM 2680 C C . THR B 1 13 ? 3.129 40.911 76.472 1.00 22.09 ? 13 THR B C 1 ATOM 2681 O O . THR B 1 13 ? 3.540 39.880 75.983 1.00 21.50 ? 13 THR B O 1 ATOM 2682 C CB . THR B 1 13 ? 4.716 42.714 75.767 1.00 21.94 ? 13 THR B CB 1 ATOM 2683 O OG1 . THR B 1 13 ? 5.421 43.857 76.253 1.00 23.45 ? 13 THR B OG1 1 ATOM 2684 C CG2 . THR B 1 13 ? 3.609 43.288 74.870 1.00 16.55 ? 13 THR B CG2 1 ATOM 2685 N N . ASN B 1 14 ? 1.841 41.225 76.600 1.00 23.10 ? 14 ASN B N 1 ATOM 2686 C CA . ASN B 1 14 ? 0.730 40.384 76.133 1.00 25.18 ? 14 ASN B CA 1 ATOM 2687 C C . ASN B 1 14 ? 0.125 40.950 74.842 1.00 24.84 ? 14 ASN B C 1 ATOM 2688 O O . ASN B 1 14 ? -0.607 41.920 74.895 1.00 26.29 ? 14 ASN B O 1 ATOM 2689 C CB . ASN B 1 14 ? -0.352 40.269 77.251 1.00 24.56 ? 14 ASN B CB 1 ATOM 2690 C CG . ASN B 1 14 ? -1.645 39.513 76.808 1.00 24.52 ? 14 ASN B CG 1 ATOM 2691 O OD1 . ASN B 1 14 ? -2.562 39.249 77.623 1.00 25.39 ? 14 ASN B OD1 1 ATOM 2692 N ND2 . ASN B 1 14 ? -1.736 39.208 75.549 1.00 19.19 ? 14 ASN B ND2 1 ATOM 2693 N N . TYR B 1 15 ? 0.412 40.333 73.691 1.00 24.69 ? 15 TYR B N 1 ATOM 2694 C CA . TYR B 1 15 ? -0.293 40.667 72.440 1.00 25.76 ? 15 TYR B CA 1 ATOM 2695 C C . TYR B 1 15 ? -1.504 39.759 72.260 1.00 26.56 ? 15 TYR B C 1 ATOM 2696 O O . TYR B 1 15 ? -1.343 38.563 72.139 1.00 26.25 ? 15 TYR B O 1 ATOM 2697 C CB . TYR B 1 15 ? 0.645 40.597 71.220 1.00 24.12 ? 15 TYR B CB 1 ATOM 2698 C CG . TYR B 1 15 ? -0.002 40.790 69.864 1.00 25.84 ? 15 TYR B CG 1 ATOM 2699 C CD1 . TYR B 1 15 ? -0.800 41.924 69.579 1.00 24.08 ? 15 TYR B CD1 1 ATOM 2700 C CD2 . TYR B 1 15 ? 0.214 39.868 68.841 1.00 26.42 ? 15 TYR B CD2 1 ATOM 2701 C CE1 . TYR B 1 15 ? -1.385 42.092 68.337 1.00 22.15 ? 15 TYR B CE1 1 ATOM 2702 C CE2 . TYR B 1 15 ? -0.344 40.042 67.584 1.00 26.99 ? 15 TYR B CE2 1 ATOM 2703 C CZ . TYR B 1 15 ? -1.162 41.156 67.356 1.00 26.59 ? 15 TYR B CZ 1 ATOM 2704 O OH . TYR B 1 15 ? -1.714 41.313 66.120 1.00 28.48 ? 15 TYR B OH 1 ATOM 2705 N N . MET B 1 16 ? -2.701 40.362 72.293 1.00 28.98 ? 16 MET B N 1 ATOM 2706 C CA . MET B 1 16 ? -4.010 39.715 72.034 1.00 29.92 ? 16 MET B CA 1 ATOM 2707 C C . MET B 1 16 ? -4.290 38.344 72.701 1.00 27.76 ? 16 MET B C 1 ATOM 2708 O O . MET B 1 16 ? -5.086 37.545 72.174 1.00 28.50 ? 16 MET B O 1 ATOM 2709 C CB . MET B 1 16 ? -4.347 39.691 70.524 1.00 31.10 ? 16 MET B CB 1 ATOM 2710 C CG . MET B 1 16 ? -3.472 38.799 69.627 1.00 34.36 ? 16 MET B CG 1 ATOM 2711 S SD . MET B 1 16 ? -4.009 38.562 67.891 1.00 34.34 ? 16 MET B SD 1 ATOM 2712 C CE . MET B 1 16 ? -5.692 37.996 68.128 1.00 38.13 ? 16 MET B CE 1 ATOM 2713 N N . ASP B 1 17 ? -3.638 38.076 73.831 1.00 25.69 ? 17 ASP B N 1 ATOM 2714 C CA . ASP B 1 17 ? -3.921 36.868 74.652 1.00 26.83 ? 17 ASP B CA 1 ATOM 2715 C C . ASP B 1 17 ? -3.380 35.584 74.007 1.00 24.59 ? 17 ASP B C 1 ATOM 2716 O O . ASP B 1 17 ? -3.712 34.472 74.431 1.00 27.82 ? 17 ASP B O 1 ATOM 2717 C CB . ASP B 1 17 ? -5.439 36.732 74.927 1.00 26.35 ? 17 ASP B CB 1 ATOM 2718 C CG . ASP B 1 17 ? -5.925 37.563 76.116 1.00 28.20 ? 17 ASP B CG 1 ATOM 2719 O OD1 . ASP B 1 17 ? -5.131 38.167 76.845 1.00 26.64 ? 17 ASP B OD1 1 ATOM 2720 O OD2 . ASP B 1 17 ? -7.137 37.674 76.400 1.00 32.83 ? 17 ASP B OD2 1 ATOM 2721 N N . THR B 1 18 ? -2.523 35.739 72.999 1.00 24.79 ? 18 THR B N 1 ATOM 2722 C CA . THR B 1 18 ? -1.909 34.600 72.279 1.00 23.73 ? 18 THR B CA 1 ATOM 2723 C C . THR B 1 18 ? -0.378 34.610 72.314 1.00 25.14 ? 18 THR B C 1 ATOM 2724 O O . THR B 1 18 ? 0.250 33.558 72.103 1.00 25.26 ? 18 THR B O 1 ATOM 2725 C CB . THR B 1 18 ? -2.352 34.574 70.815 1.00 24.58 ? 18 THR B CB 1 ATOM 2726 O OG1 . THR B 1 18 ? -1.956 35.795 70.158 1.00 24.63 ? 18 THR B OG1 1 ATOM 2727 C CG2 . THR B 1 18 ? -3.888 34.581 70.679 1.00 24.32 ? 18 THR B CG2 1 ATOM 2728 N N . GLN B 1 19 ? 0.220 35.793 72.529 1.00 21.76 ? 19 GLN B N 1 ATOM 2729 C CA . GLN B 1 19 ? 1.694 35.927 72.501 1.00 24.35 ? 19 GLN B CA 1 ATOM 2730 C C . GLN B 1 19 ? 2.144 36.699 73.712 1.00 22.18 ? 19 GLN B C 1 ATOM 2731 O O . GLN B 1 19 ? 1.724 37.854 73.920 1.00 27.75 ? 19 GLN B O 1 ATOM 2732 C CB . GLN B 1 19 ? 2.220 36.622 71.215 1.00 24.29 ? 19 GLN B CB 1 ATOM 2733 C CG . GLN B 1 19 ? 1.873 35.940 69.873 1.00 25.13 ? 19 GLN B CG 1 ATOM 2734 C CD . GLN B 1 19 ? 2.259 36.764 68.624 1.00 25.09 ? 19 GLN B CD 1 ATOM 2735 O OE1 . GLN B 1 19 ? 3.255 37.480 68.629 1.00 27.15 ? 19 GLN B OE1 1 ATOM 2736 N NE2 . GLN B 1 19 ? 1.497 36.610 67.548 1.00 28.71 ? 19 GLN B NE2 1 ATOM 2737 N N . TYR B 1 20 ? 2.978 36.058 74.527 1.00 23.98 ? 20 TYR B N 1 ATOM 2738 C CA . TYR B 1 20 ? 3.510 36.626 75.779 1.00 23.31 ? 20 TYR B CA 1 ATOM 2739 C C . TYR B 1 20 ? 5.034 36.573 75.704 1.00 25.03 ? 20 TYR B C 1 ATOM 2740 O O . TYR B 1 20 ? 5.639 35.489 75.582 1.00 21.78 ? 20 TYR B O 1 ATOM 2741 C CB . TYR B 1 20 ? 3.024 35.822 76.986 1.00 22.85 ? 20 TYR B CB 1 ATOM 2742 C CG . TYR B 1 20 ? 1.536 35.957 77.278 1.00 23.35 ? 20 TYR B CG 1 ATOM 2743 C CD1 . TYR B 1 20 ? 1.094 36.839 78.247 1.00 21.05 ? 20 TYR B CD1 1 ATOM 2744 C CD2 . TYR B 1 20 ? 0.568 35.207 76.567 1.00 23.66 ? 20 TYR B CD2 1 ATOM 2745 C CE1 . TYR B 1 20 ? -0.258 36.984 78.527 1.00 20.22 ? 20 TYR B CE1 1 ATOM 2746 C CE2 . TYR B 1 20 ? -0.812 35.345 76.859 1.00 22.70 ? 20 TYR B CE2 1 ATOM 2747 C CZ . TYR B 1 20 ? -1.204 36.236 77.828 1.00 22.46 ? 20 TYR B CZ 1 ATOM 2748 O OH . TYR B 1 20 ? -2.532 36.399 78.168 1.00 23.51 ? 20 TYR B OH 1 ATOM 2749 N N . TYR B 1 21 ? 5.666 37.742 75.747 1.00 23.34 ? 21 TYR B N 1 ATOM 2750 C CA . TYR B 1 21 ? 7.094 37.794 75.426 1.00 21.83 ? 21 TYR B CA 1 ATOM 2751 C C . TYR B 1 21 ? 7.738 38.925 76.197 1.00 24.48 ? 21 TYR B C 1 ATOM 2752 O O . TYR B 1 21 ? 7.070 39.904 76.523 1.00 23.15 ? 21 TYR B O 1 ATOM 2753 C CB . TYR B 1 21 ? 7.325 37.924 73.914 1.00 21.98 ? 21 TYR B CB 1 ATOM 2754 C CG . TYR B 1 21 ? 6.656 39.117 73.245 1.00 20.45 ? 21 TYR B CG 1 ATOM 2755 C CD1 . TYR B 1 21 ? 5.346 39.029 72.729 1.00 21.50 ? 21 TYR B CD1 1 ATOM 2756 C CD2 . TYR B 1 21 ? 7.329 40.333 73.133 1.00 19.47 ? 21 TYR B CD2 1 ATOM 2757 C CE1 . TYR B 1 21 ? 4.731 40.164 72.130 1.00 22.44 ? 21 TYR B CE1 1 ATOM 2758 C CE2 . TYR B 1 21 ? 6.734 41.435 72.537 1.00 19.51 ? 21 TYR B CE2 1 ATOM 2759 C CZ . TYR B 1 21 ? 5.442 41.335 72.027 1.00 23.20 ? 21 TYR B CZ 1 ATOM 2760 O OH . TYR B 1 21 ? 4.868 42.442 71.439 1.00 26.84 ? 21 TYR B OH 1 ATOM 2761 N N . GLY B 1 22 ? 9.021 38.776 76.497 1.00 24.19 ? 22 GLY B N 1 ATOM 2762 C CA . GLY B 1 22 ? 9.790 39.807 77.199 1.00 26.41 ? 22 GLY B CA 1 ATOM 2763 C C . GLY B 1 22 ? 11.174 39.831 76.593 1.00 27.17 ? 22 GLY B C 1 ATOM 2764 O O . GLY B 1 22 ? 11.382 39.203 75.569 1.00 26.75 ? 22 GLY B O 1 ATOM 2765 N N . GLU B 1 23 ? 12.115 40.536 77.222 1.00 28.23 ? 23 GLU B N 1 ATOM 2766 C CA . GLU B 1 23 ? 13.459 40.763 76.634 1.00 28.94 ? 23 GLU B CA 1 ATOM 2767 C C . GLU B 1 23 ? 14.599 40.012 77.305 1.00 28.26 ? 23 GLU B C 1 ATOM 2768 O O . GLU B 1 23 ? 14.607 39.870 78.527 1.00 29.63 ? 23 GLU B O 1 ATOM 2769 C CB . GLU B 1 23 ? 13.802 42.260 76.655 1.00 28.95 ? 23 GLU B CB 1 ATOM 2770 C CG . GLU B 1 23 ? 12.973 43.080 75.682 1.00 30.15 ? 23 GLU B CG 1 ATOM 2771 C CD . GLU B 1 23 ? 13.503 44.496 75.500 1.00 32.80 ? 23 GLU B CD 1 ATOM 2772 O OE1 . GLU B 1 23 ? 13.823 45.154 76.512 1.00 33.52 ? 23 GLU B OE1 1 ATOM 2773 O OE2 . GLU B 1 23 ? 13.601 44.947 74.334 1.00 34.74 ? 23 GLU B OE2 1 ATOM 2774 N N . ILE B 1 24 ? 15.543 39.523 76.483 1.00 26.63 ? 24 ILE B N 1 ATOM 2775 C CA . ILE B 1 24 ? 16.861 39.050 76.929 1.00 22.91 ? 24 ILE B CA 1 ATOM 2776 C C . ILE B 1 24 ? 17.916 39.821 76.128 1.00 24.69 ? 24 ILE B C 1 ATOM 2777 O O . ILE B 1 24 ? 17.587 40.418 75.115 1.00 22.55 ? 24 ILE B O 1 ATOM 2778 C CB . ILE B 1 24 ? 17.033 37.502 76.746 1.00 24.24 ? 24 ILE B CB 1 ATOM 2779 C CG1 . ILE B 1 24 ? 17.102 37.103 75.265 1.00 21.92 ? 24 ILE B CG1 1 ATOM 2780 C CG2 . ILE B 1 24 ? 15.929 36.767 77.501 1.00 22.42 ? 24 ILE B CG2 1 ATOM 2781 C CD1 . ILE B 1 24 ? 17.345 35.617 74.936 1.00 25.42 ? 24 ILE B CD1 1 ATOM 2782 N N . GLY B 1 25 ? 19.170 39.813 76.599 1.00 26.27 ? 25 GLY B N 1 ATOM 2783 C CA . GLY B 1 25 ? 20.298 40.335 75.839 1.00 23.95 ? 25 GLY B CA 1 ATOM 2784 C C . GLY B 1 25 ? 21.269 39.207 75.554 1.00 27.30 ? 25 GLY B C 1 ATOM 2785 O O . GLY B 1 25 ? 21.397 38.288 76.375 1.00 28.38 ? 25 GLY B O 1 ATOM 2786 N N . ILE B 1 26 ? 21.889 39.246 74.367 1.00 26.38 ? 26 ILE B N 1 ATOM 2787 C CA . ILE B 1 26 ? 22.926 38.299 73.971 1.00 29.00 ? 26 ILE B CA 1 ATOM 2788 C C . ILE B 1 26 ? 24.167 39.018 73.451 1.00 29.98 ? 26 ILE B C 1 ATOM 2789 O O . ILE B 1 26 ? 24.082 39.829 72.527 1.00 31.04 ? 26 ILE B O 1 ATOM 2790 C CB . ILE B 1 26 ? 22.424 37.294 72.915 1.00 27.53 ? 26 ILE B CB 1 ATOM 2791 C CG1 . ILE B 1 26 ? 21.283 36.450 73.495 1.00 32.48 ? 26 ILE B CG1 1 ATOM 2792 C CG2 . ILE B 1 26 ? 23.579 36.363 72.502 1.00 29.00 ? 26 ILE B CG2 1 ATOM 2793 C CD1 . ILE B 1 26 ? 20.495 35.650 72.483 1.00 29.95 ? 26 ILE B CD1 1 ATOM 2794 N N . GLY B 1 27 ? 25.308 38.718 74.079 1.00 31.30 ? 27 GLY B N 1 ATOM 2795 C CA . GLY B 1 27 ? 26.614 39.225 73.675 1.00 32.30 ? 27 GLY B CA 1 ATOM 2796 C C . GLY B 1 27 ? 27.161 40.412 74.449 1.00 33.80 ? 27 GLY B C 1 ATOM 2797 O O . GLY B 1 27 ? 26.526 40.927 75.375 1.00 33.83 ? 27 GLY B O 1 ATOM 2798 N N . THR B 1 28 ? 28.341 40.870 74.028 1.00 36.25 ? 28 THR B N 1 ATOM 2799 C CA . THR B 1 28 ? 29.000 42.035 74.621 1.00 36.89 ? 28 THR B CA 1 ATOM 2800 C C . THR B 1 28 ? 29.370 43.059 73.532 1.00 37.70 ? 28 THR B C 1 ATOM 2801 O O . THR B 1 28 ? 30.250 42.796 72.714 1.00 36.36 ? 28 THR B O 1 ATOM 2802 C CB . THR B 1 28 ? 30.256 41.609 75.426 1.00 38.55 ? 28 THR B CB 1 ATOM 2803 O OG1 . THR B 1 28 ? 29.871 40.743 76.511 1.00 38.61 ? 28 THR B OG1 1 ATOM 2804 C CG2 . THR B 1 28 ? 30.861 42.829 76.140 1.00 38.98 ? 28 THR B CG2 1 ATOM 2805 N N . PRO B 1 29 ? 28.691 44.208 73.496 1.00 37.84 ? 29 PRO B N 1 ATOM 2806 C CA . PRO B 1 29 ? 27.576 44.522 74.390 1.00 37.57 ? 29 PRO B CA 1 ATOM 2807 C C . PRO B 1 29 ? 26.298 43.710 74.051 1.00 37.09 ? 29 PRO B C 1 ATOM 2808 O O . PRO B 1 29 ? 26.213 43.126 72.962 1.00 36.96 ? 29 PRO B O 1 ATOM 2809 C CB . PRO B 1 29 ? 27.346 46.008 74.118 1.00 38.73 ? 29 PRO B CB 1 ATOM 2810 C CG . PRO B 1 29 ? 27.757 46.185 72.710 1.00 38.35 ? 29 PRO B CG 1 ATOM 2811 C CD . PRO B 1 29 ? 28.976 45.314 72.565 1.00 39.15 ? 29 PRO B CD 1 ATOM 2812 N N . PRO B 1 30 ? 25.337 43.653 74.979 1.00 36.71 ? 30 PRO B N 1 ATOM 2813 C CA . PRO B 1 30 ? 24.078 42.925 74.735 1.00 35.32 ? 30 PRO B CA 1 ATOM 2814 C C . PRO B 1 30 ? 23.374 43.355 73.465 1.00 33.55 ? 30 PRO B C 1 ATOM 2815 O O . PRO B 1 30 ? 23.172 44.541 73.235 1.00 35.54 ? 30 PRO B O 1 ATOM 2816 C CB . PRO B 1 30 ? 23.212 43.246 75.964 1.00 36.11 ? 30 PRO B CB 1 ATOM 2817 C CG . PRO B 1 30 ? 23.981 44.279 76.774 1.00 37.91 ? 30 PRO B CG 1 ATOM 2818 C CD . PRO B 1 30 ? 25.400 44.238 76.332 1.00 35.46 ? 30 PRO B CD 1 ATOM 2819 N N . GLN B 1 31 ? 23.042 42.386 72.623 1.00 32.13 ? 31 GLN B N 1 ATOM 2820 C CA . GLN B 1 31 ? 22.092 42.606 71.558 1.00 31.41 ? 31 GLN B CA 1 ATOM 2821 C C . GLN B 1 31 ? 20.730 42.148 72.083 1.00 32.87 ? 31 GLN B C 1 ATOM 2822 O O . GLN B 1 31 ? 20.605 41.041 72.613 1.00 31.40 ? 31 GLN B O 1 ATOM 2823 C CB . GLN B 1 31 ? 22.503 41.833 70.299 1.00 30.88 ? 31 GLN B CB 1 ATOM 2824 C CG . GLN B 1 31 ? 23.733 42.452 69.564 1.00 32.19 ? 31 GLN B CG 1 ATOM 2825 C CD . GLN B 1 31 ? 24.334 41.500 68.559 1.00 31.59 ? 31 GLN B CD 1 ATOM 2826 O OE1 . GLN B 1 31 ? 23.635 41.030 67.652 1.00 32.80 ? 31 GLN B OE1 1 ATOM 2827 N NE2 . GLN B 1 31 ? 25.624 41.203 68.709 1.00 32.24 ? 31 GLN B NE2 1 ATOM 2828 N N . THR B 1 32 ? 19.730 43.015 71.957 1.00 31.69 ? 32 THR B N 1 ATOM 2829 C CA . THR B 1 32 ? 18.423 42.814 72.590 1.00 31.22 ? 32 THR B CA 1 ATOM 2830 C C . THR B 1 32 ? 17.413 42.030 71.718 1.00 28.60 ? 32 THR B C 1 ATOM 2831 O O . THR B 1 32 ? 17.219 42.340 70.539 1.00 25.86 ? 32 THR B O 1 ATOM 2832 C CB . THR B 1 32 ? 17.870 44.195 73.024 1.00 32.86 ? 32 THR B CB 1 ATOM 2833 O OG1 . THR B 1 32 ? 18.775 44.774 73.975 1.00 35.48 ? 32 THR B OG1 1 ATOM 2834 C CG2 . THR B 1 32 ? 16.612 44.058 73.852 1.00 33.83 ? 32 THR B CG2 1 ATOM 2835 N N . PHE B 1 33 ? 16.784 41.004 72.304 1.00 28.51 ? 33 PHE B N 1 ATOM 2836 C CA . PHE B 1 33 ? 15.806 40.171 71.601 1.00 24.00 ? 33 PHE B CA 1 ATOM 2837 C C . PHE B 1 33 ? 14.532 39.978 72.431 1.00 25.09 ? 33 PHE B C 1 ATOM 2838 O O . PHE B 1 33 ? 14.614 39.786 73.645 1.00 25.01 ? 33 PHE B O 1 ATOM 2839 C CB . PHE B 1 33 ? 16.394 38.789 71.265 1.00 26.48 ? 33 PHE B CB 1 ATOM 2840 C CG . PHE B 1 33 ? 17.587 38.840 70.348 1.00 28.22 ? 33 PHE B CG 1 ATOM 2841 C CD1 . PHE B 1 33 ? 17.421 38.826 68.963 1.00 27.60 ? 33 PHE B CD1 1 ATOM 2842 C CD2 . PHE B 1 33 ? 18.879 38.914 70.874 1.00 26.61 ? 33 PHE B CD2 1 ATOM 2843 C CE1 . PHE B 1 33 ? 18.533 38.885 68.106 1.00 27.99 ? 33 PHE B CE1 1 ATOM 2844 C CE2 . PHE B 1 33 ? 20.000 38.958 70.022 1.00 25.35 ? 33 PHE B CE2 1 ATOM 2845 C CZ . PHE B 1 33 ? 19.816 38.955 68.640 1.00 26.54 ? 33 PHE B CZ 1 ATOM 2846 N N . LYS B 1 34 ? 13.376 40.010 71.761 1.00 22.64 ? 34 LYS B N 1 ATOM 2847 C CA . LYS B 1 34 ? 12.063 39.707 72.342 1.00 23.64 ? 34 LYS B CA 1 ATOM 2848 C C . LYS B 1 34 ? 11.864 38.215 72.193 1.00 25.01 ? 34 LYS B C 1 ATOM 2849 O O . LYS B 1 34 ? 12.035 37.670 71.089 1.00 23.58 ? 34 LYS B O 1 ATOM 2850 C CB . LYS B 1 34 ? 10.945 40.418 71.575 1.00 23.74 ? 34 LYS B CB 1 ATOM 2851 C CG . LYS B 1 34 ? 11.084 41.962 71.529 1.00 24.40 ? 34 LYS B CG 1 ATOM 2852 C CD . LYS B 1 34 ? 10.028 42.522 70.541 1.00 27.89 ? 34 LYS B CD 1 ATOM 2853 C CE . LYS B 1 34 ? 10.548 43.646 69.670 1.00 34.59 ? 34 LYS B CE 1 ATOM 2854 N NZ . LYS B 1 34 ? 11.709 43.189 68.820 1.00 40.78 ? 34 LYS B NZ 1 ATOM 2855 N N . VAL B 1 35 ? 11.540 37.538 73.298 1.00 23.47 ? 35 VAL B N 1 ATOM 2856 C CA . VAL B 1 35 ? 11.481 36.081 73.274 1.00 24.29 ? 35 VAL B CA 1 ATOM 2857 C C . VAL B 1 35 ? 10.282 35.555 74.067 1.00 22.03 ? 35 VAL B C 1 ATOM 2858 O O . VAL B 1 35 ? 9.830 36.193 75.024 1.00 20.27 ? 35 VAL B O 1 ATOM 2859 C CB . VAL B 1 35 ? 12.807 35.442 73.841 1.00 21.71 ? 35 VAL B CB 1 ATOM 2860 C CG1 . VAL B 1 35 ? 14.031 35.839 73.002 1.00 22.61 ? 35 VAL B CG1 1 ATOM 2861 C CG2 . VAL B 1 35 ? 13.002 35.806 75.290 1.00 16.33 ? 35 VAL B CG2 1 ATOM 2862 N N . VAL B 1 36 ? 9.776 34.400 73.644 1.00 21.39 ? 36 VAL B N 1 ATOM 2863 C CA . VAL B 1 36 ? 8.851 33.577 74.430 1.00 19.36 ? 36 VAL B CA 1 ATOM 2864 C C . VAL B 1 36 ? 9.640 32.636 75.374 1.00 22.34 ? 36 VAL B C 1 ATOM 2865 O O . VAL B 1 36 ? 10.644 32.046 74.998 1.00 20.39 ? 36 VAL B O 1 ATOM 2866 C CB . VAL B 1 36 ? 7.905 32.796 73.486 1.00 21.74 ? 36 VAL B CB 1 ATOM 2867 C CG1 . VAL B 1 36 ? 7.169 31.635 74.183 1.00 21.83 ? 36 VAL B CG1 1 ATOM 2868 C CG2 . VAL B 1 36 ? 6.887 33.751 72.918 1.00 22.21 ? 36 VAL B CG2 1 ATOM 2869 N N . PHE B 1 37 ? 9.189 32.525 76.614 1.00 25.08 ? 37 PHE B N 1 ATOM 2870 C CA . PHE B 1 37 ? 9.755 31.569 77.549 1.00 24.06 ? 37 PHE B CA 1 ATOM 2871 C C . PHE B 1 37 ? 8.819 30.396 77.512 1.00 25.23 ? 37 PHE B C 1 ATOM 2872 O O . PHE B 1 37 ? 7.629 30.523 77.852 1.00 21.35 ? 37 PHE B O 1 ATOM 2873 C CB . PHE B 1 37 ? 9.885 32.206 78.930 1.00 24.71 ? 37 PHE B CB 1 ATOM 2874 C CG . PHE B 1 37 ? 10.794 33.403 78.924 1.00 24.52 ? 37 PHE B CG 1 ATOM 2875 C CD1 . PHE B 1 37 ? 10.303 34.685 78.642 1.00 22.65 ? 37 PHE B CD1 1 ATOM 2876 C CD2 . PHE B 1 37 ? 12.159 33.244 79.142 1.00 24.26 ? 37 PHE B CD2 1 ATOM 2877 C CE1 . PHE B 1 37 ? 11.176 35.789 78.584 1.00 20.12 ? 37 PHE B CE1 1 ATOM 2878 C CE2 . PHE B 1 37 ? 13.010 34.321 79.125 1.00 22.73 ? 37 PHE B CE2 1 ATOM 2879 C CZ . PHE B 1 37 ? 12.522 35.598 78.833 1.00 23.05 ? 37 PHE B CZ 1 ATOM 2880 N N . ASP B 1 38 ? 9.359 29.288 77.005 1.00 23.65 ? 38 ASP B N 1 ATOM 2881 C CA . ASP B 1 38 ? 8.589 28.141 76.569 1.00 24.35 ? 38 ASP B CA 1 ATOM 2882 C C . ASP B 1 38 ? 8.925 26.886 77.390 1.00 24.11 ? 38 ASP B C 1 ATOM 2883 O O . ASP B 1 38 ? 10.053 26.372 77.295 1.00 24.06 ? 38 ASP B O 1 ATOM 2884 C CB . ASP B 1 38 ? 8.974 27.894 75.111 1.00 29.08 ? 38 ASP B CB 1 ATOM 2885 C CG . ASP B 1 38 ? 8.155 26.811 74.460 1.00 33.20 ? 38 ASP B CG 1 ATOM 2886 O OD1 . ASP B 1 38 ? 7.366 27.156 73.573 1.00 34.97 ? 38 ASP B OD1 1 ATOM 2887 O OD2 . ASP B 1 38 ? 8.235 25.592 74.759 1.00 34.73 ? 38 ASP B OD2 1 ATOM 2888 N N . THR B 1 39 ? 7.950 26.350 78.138 1.00 23.57 ? 39 THR B N 1 ATOM 2889 C CA . THR B 1 39 ? 8.194 25.141 78.948 1.00 23.79 ? 39 THR B CA 1 ATOM 2890 C C . THR B 1 39 ? 7.967 23.844 78.164 1.00 24.94 ? 39 THR B C 1 ATOM 2891 O O . THR B 1 39 ? 8.262 22.757 78.673 1.00 28.46 ? 39 THR B O 1 ATOM 2892 C CB . THR B 1 39 ? 7.343 25.109 80.241 1.00 21.66 ? 39 THR B CB 1 ATOM 2893 O OG1 . THR B 1 39 ? 5.962 25.267 79.898 1.00 27.24 ? 39 THR B OG1 1 ATOM 2894 C CG2 . THR B 1 39 ? 7.650 26.327 81.193 1.00 18.48 ? 39 THR B CG2 1 ATOM 2895 N N . GLY B 1 40 ? 7.407 23.953 76.966 1.00 24.61 ? 40 GLY B N 1 ATOM 2896 C CA . GLY B 1 40 ? 7.261 22.810 76.059 1.00 26.03 ? 40 GLY B CA 1 ATOM 2897 C C . GLY B 1 40 ? 8.463 22.549 75.147 1.00 25.90 ? 40 GLY B C 1 ATOM 2898 O O . GLY B 1 40 ? 8.361 21.799 74.191 1.00 29.09 ? 40 GLY B O 1 ATOM 2899 N N . SER B 1 41 ? 9.605 23.159 75.449 1.00 25.84 ? 41 SER B N 1 ATOM 2900 C CA . SER B 1 41 ? 10.826 23.025 74.640 1.00 25.90 ? 41 SER B CA 1 ATOM 2901 C C . SER B 1 41 ? 12.039 23.371 75.486 1.00 26.22 ? 41 SER B C 1 ATOM 2902 O O . SER B 1 41 ? 11.886 23.938 76.565 1.00 25.01 ? 41 SER B O 1 ATOM 2903 C CB . SER B 1 41 ? 10.788 23.925 73.387 1.00 30.54 ? 41 SER B CB 1 ATOM 2904 O OG . SER B 1 41 ? 10.916 25.307 73.724 1.00 29.64 ? 41 SER B OG 1 ATOM 2905 N N . SER B 1 42 ? 13.243 23.038 75.003 1.00 27.43 ? 42 SER B N 1 ATOM 2906 C CA . SER B 1 42 ? 14.450 23.131 75.829 1.00 25.52 ? 42 SER B CA 1 ATOM 2907 C C . SER B 1 42 ? 15.680 23.786 75.181 1.00 25.54 ? 42 SER B C 1 ATOM 2908 O O . SER B 1 42 ? 16.759 23.696 75.746 1.00 25.80 ? 42 SER B O 1 ATOM 2909 C CB . SER B 1 42 ? 14.841 21.740 76.333 1.00 28.83 ? 42 SER B CB 1 ATOM 2910 O OG . SER B 1 42 ? 13.690 20.992 76.684 1.00 29.63 ? 42 SER B OG 1 ATOM 2911 N N . ASN B 1 43 ? 15.536 24.434 74.022 1.00 25.00 ? 43 ASN B N 1 ATOM 2912 C CA . ASN B 1 43 ? 16.646 25.190 73.415 1.00 26.86 ? 43 ASN B CA 1 ATOM 2913 C C . ASN B 1 43 ? 16.379 26.696 73.387 1.00 28.90 ? 43 ASN B C 1 ATOM 2914 O O . ASN B 1 43 ? 15.224 27.141 73.503 1.00 30.98 ? 43 ASN B O 1 ATOM 2915 C CB . ASN B 1 43 ? 16.937 24.729 71.969 1.00 27.91 ? 43 ASN B CB 1 ATOM 2916 C CG . ASN B 1 43 ? 17.368 23.278 71.890 1.00 31.61 ? 43 ASN B CG 1 ATOM 2917 O OD1 . ASN B 1 43 ? 16.559 22.373 72.097 1.00 32.54 ? 43 ASN B OD1 1 ATOM 2918 N ND2 . ASN B 1 43 ? 18.646 23.051 71.567 1.00 29.46 ? 43 ASN B ND2 1 ATOM 2919 N N . VAL B 1 44 ? 17.454 27.462 73.221 1.00 27.11 ? 44 VAL B N 1 ATOM 2920 C CA . VAL B 1 44 ? 17.400 28.894 72.932 1.00 27.00 ? 44 VAL B CA 1 ATOM 2921 C C . VAL B 1 44 ? 17.636 29.126 71.444 1.00 26.53 ? 44 VAL B C 1 ATOM 2922 O O . VAL B 1 44 ? 18.628 28.672 70.890 1.00 27.62 ? 44 VAL B O 1 ATOM 2923 C CB . VAL B 1 44 ? 18.443 29.678 73.774 1.00 26.80 ? 44 VAL B CB 1 ATOM 2924 C CG1 . VAL B 1 44 ? 18.377 31.186 73.485 1.00 26.50 ? 44 VAL B CG1 1 ATOM 2925 C CG2 . VAL B 1 44 ? 18.241 29.409 75.272 1.00 26.29 ? 44 VAL B CG2 1 ATOM 2926 N N . TRP B 1 45 ? 16.709 29.821 70.791 1.00 26.85 ? 45 TRP B N 1 ATOM 2927 C CA . TRP B 1 45 ? 16.843 30.158 69.383 1.00 28.43 ? 45 TRP B CA 1 ATOM 2928 C C . TRP B 1 45 ? 16.636 31.644 69.169 1.00 26.39 ? 45 TRP B C 1 ATOM 2929 O O . TRP B 1 45 ? 15.659 32.194 69.666 1.00 23.70 ? 45 TRP B O 1 ATOM 2930 C CB . TRP B 1 45 ? 15.753 29.473 68.575 1.00 30.82 ? 45 TRP B CB 1 ATOM 2931 C CG . TRP B 1 45 ? 15.707 27.970 68.565 1.00 30.82 ? 45 TRP B CG 1 ATOM 2932 C CD1 . TRP B 1 45 ? 14.982 27.159 69.403 1.00 29.59 ? 45 TRP B CD1 1 ATOM 2933 C CD2 . TRP B 1 45 ? 16.330 27.100 67.607 1.00 30.74 ? 45 TRP B CD2 1 ATOM 2934 N NE1 . TRP B 1 45 ? 15.127 25.843 69.027 1.00 29.55 ? 45 TRP B NE1 1 ATOM 2935 C CE2 . TRP B 1 45 ? 15.950 25.776 67.932 1.00 31.77 ? 45 TRP B CE2 1 ATOM 2936 C CE3 . TRP B 1 45 ? 17.189 27.304 66.516 1.00 32.27 ? 45 TRP B CE3 1 ATOM 2937 C CZ2 . TRP B 1 45 ? 16.403 24.662 67.206 1.00 33.91 ? 45 TRP B CZ2 1 ATOM 2938 C CZ3 . TRP B 1 45 ? 17.638 26.188 65.781 1.00 31.92 ? 45 TRP B CZ3 1 ATOM 2939 C CH2 . TRP B 1 45 ? 17.234 24.891 66.131 1.00 32.08 ? 45 TRP B CH2 1 ATOM 2940 N N . VAL B 1 46 ? 17.541 32.282 68.422 1.00 25.75 ? 46 VAL B N 1 ATOM 2941 C CA . VAL B 1 46 ? 17.296 33.613 67.848 1.00 29.12 ? 46 VAL B CA 1 ATOM 2942 C C . VAL B 1 46 ? 17.649 33.602 66.356 1.00 30.42 ? 46 VAL B C 1 ATOM 2943 O O . VAL B 1 46 ? 18.384 32.709 65.910 1.00 29.46 ? 46 VAL B O 1 ATOM 2944 C CB . VAL B 1 46 ? 18.063 34.740 68.573 1.00 28.55 ? 46 VAL B CB 1 ATOM 2945 C CG1 . VAL B 1 46 ? 17.435 34.990 69.953 1.00 30.78 ? 46 VAL B CG1 1 ATOM 2946 C CG2 . VAL B 1 46 ? 19.571 34.448 68.630 1.00 26.10 ? 46 VAL B CG2 1 ATOM 2947 N N . PRO B 1 47 ? 17.119 34.553 65.572 1.00 29.12 ? 47 PRO B N 1 ATOM 2948 C CA . PRO B 1 47 ? 17.466 34.605 64.151 1.00 30.61 ? 47 PRO B CA 1 ATOM 2949 C C . PRO B 1 47 ? 18.924 35.074 63.975 1.00 30.85 ? 47 PRO B C 1 ATOM 2950 O O . PRO B 1 47 ? 19.425 35.881 64.766 1.00 30.02 ? 47 PRO B O 1 ATOM 2951 C CB . PRO B 1 47 ? 16.445 35.603 63.545 1.00 30.96 ? 47 PRO B CB 1 ATOM 2952 C CG . PRO B 1 47 ? 15.586 36.101 64.679 1.00 29.48 ? 47 PRO B CG 1 ATOM 2953 C CD . PRO B 1 47 ? 16.225 35.660 65.975 1.00 31.15 ? 47 PRO B CD 1 ATOM 2954 N N . SER B 1 48 ? 19.599 34.522 62.973 1.00 31.78 ? 48 SER B N 1 ATOM 2955 C CA . SER B 1 48 ? 20.990 34.859 62.677 1.00 32.17 ? 48 SER B CA 1 ATOM 2956 C C . SER B 1 48 ? 21.102 35.966 61.620 1.00 33.14 ? 48 SER B C 1 ATOM 2957 O O . SER B 1 48 ? 20.251 36.062 60.746 1.00 32.71 ? 48 SER B O 1 ATOM 2958 C CB . SER B 1 48 ? 21.699 33.625 62.137 1.00 32.81 ? 48 SER B CB 1 ATOM 2959 O OG . SER B 1 48 ? 23.035 33.932 61.787 1.00 32.99 ? 48 SER B OG 1 ATOM 2960 N N . SER B 1 49 ? 22.150 36.782 61.702 1.00 32.93 ? 49 SER B N 1 ATOM 2961 C CA . SER B 1 49 ? 22.500 37.724 60.613 1.00 35.54 ? 49 SER B CA 1 ATOM 2962 C C . SER B 1 49 ? 22.851 37.019 59.296 1.00 37.10 ? 49 SER B C 1 ATOM 2963 O O . SER B 1 49 ? 22.774 37.614 58.221 1.00 40.92 ? 49 SER B O 1 ATOM 2964 C CB . SER B 1 49 ? 23.640 38.660 61.021 1.00 33.20 ? 49 SER B CB 1 ATOM 2965 O OG . SER B 1 49 ? 24.776 37.950 61.499 1.00 30.78 ? 49 SER B OG 1 ATOM 2966 N N . LYS B 1 50 ? 23.220 35.748 59.375 1.00 40.50 ? 50 LYS B N 1 ATOM 2967 C CA . LYS B 1 50 ? 23.503 34.964 58.176 1.00 39.57 ? 50 LYS B CA 1 ATOM 2968 C C . LYS B 1 50 ? 22.255 34.323 57.581 1.00 41.09 ? 50 LYS B C 1 ATOM 2969 O O . LYS B 1 50 ? 22.348 33.562 56.618 1.00 41.77 ? 50 LYS B O 1 ATOM 2970 C CB . LYS B 1 50 ? 24.607 33.948 58.445 1.00 42.35 ? 50 LYS B CB 1 ATOM 2971 C CG . LYS B 1 50 ? 25.917 34.621 58.843 1.00 45.74 ? 50 LYS B CG 1 ATOM 2972 C CD . LYS B 1 50 ? 26.957 33.605 59.162 1.00 48.70 ? 50 LYS B CD 1 ATOM 2973 C CE . LYS B 1 50 ? 27.683 33.957 60.436 1.00 51.04 ? 50 LYS B CE 1 ATOM 2974 N NZ . LYS B 1 50 ? 28.590 32.829 60.826 1.00 52.89 ? 50 LYS B NZ 1 ATOM 2975 N N . CYS B 1 51 ? 21.087 34.641 58.140 1.00 41.42 ? 51 CYS B N 1 ATOM 2976 C CA . CYS B 1 51 ? 19.810 34.238 57.539 1.00 43.28 ? 51 CYS B CA 1 ATOM 2977 C C . CYS B 1 51 ? 19.644 34.942 56.211 1.00 43.96 ? 51 CYS B C 1 ATOM 2978 O O . CYS B 1 51 ? 19.918 36.136 56.115 1.00 46.06 ? 51 CYS B O 1 ATOM 2979 C CB . CYS B 1 51 ? 18.625 34.575 58.444 1.00 41.96 ? 51 CYS B CB 1 ATOM 2980 S SG . CYS B 1 51 ? 17.108 33.679 58.023 1.00 41.56 ? 51 CYS B SG 1 ATOM 2981 N N . SER B 1 52 ? 19.211 34.197 55.193 1.00 45.09 ? 52 SER B N 1 ATOM 2982 C CA . SER B 1 52 ? 19.039 34.735 53.841 1.00 47.56 ? 52 SER B CA 1 ATOM 2983 C C . SER B 1 52 ? 17.776 35.584 53.727 1.00 48.61 ? 52 SER B C 1 ATOM 2984 O O . SER B 1 52 ? 16.755 35.260 54.338 1.00 45.66 ? 52 SER B O 1 ATOM 2985 C CB . SER B 1 52 ? 18.976 33.595 52.823 1.00 48.99 ? 52 SER B CB 1 ATOM 2986 O OG . SER B 1 52 ? 18.542 34.054 51.551 1.00 50.94 ? 52 SER B OG 1 ATOM 2987 N N . ARG B 1 53 ? 17.849 36.651 52.923 1.00 49.70 ? 53 ARG B N 1 ATOM 2988 C CA . ARG B 1 53 ? 16.713 37.555 52.726 1.00 51.54 ? 53 ARG B CA 1 ATOM 2989 C C . ARG B 1 53 ? 15.517 36.826 52.078 1.00 49.93 ? 53 ARG B C 1 ATOM 2990 O O . ARG B 1 53 ? 14.402 37.349 52.057 1.00 50.32 ? 53 ARG B O 1 ATOM 2991 C CB . ARG B 1 53 ? 17.111 38.804 51.908 1.00 55.28 ? 53 ARG B CB 1 ATOM 2992 C CG . ARG B 1 53 ? 18.396 39.548 52.346 1.00 59.57 ? 53 ARG B CG 1 ATOM 2993 C CD . ARG B 1 53 ? 18.240 40.525 53.537 1.00 63.34 ? 53 ARG B CD 1 ATOM 2994 N NE . ARG B 1 53 ? 18.569 39.894 54.825 1.00 66.46 ? 53 ARG B NE 1 ATOM 2995 C CZ . ARG B 1 53 ? 19.567 40.268 55.635 1.00 67.09 ? 53 ARG B CZ 1 ATOM 2996 N NH1 . ARG B 1 53 ? 20.353 41.293 55.320 1.00 66.66 ? 53 ARG B NH1 1 ATOM 2997 N NH2 . ARG B 1 53 ? 19.777 39.612 56.771 1.00 67.22 ? 53 ARG B NH2 1 ATOM 2998 N N . LEU B 1 54 ? 15.765 35.620 51.563 1.00 48.26 ? 54 LEU B N 1 ATOM 2999 C CA . LEU B 1 54 ? 14.714 34.732 51.045 1.00 48.31 ? 54 LEU B CA 1 ATOM 3000 C C . LEU B 1 54 ? 13.727 34.302 52.129 1.00 46.47 ? 54 LEU B C 1 ATOM 3001 O O . LEU B 1 54 ? 12.572 33.976 51.837 1.00 45.84 ? 54 LEU B O 1 ATOM 3002 C CB . LEU B 1 54 ? 15.346 33.500 50.374 1.00 50.08 ? 54 LEU B CB 1 ATOM 3003 C CG . LEU B 1 54 ? 14.611 32.155 50.238 1.00 50.78 ? 54 LEU B CG 1 ATOM 3004 C CD1 . LEU B 1 54 ? 13.549 32.146 49.117 1.00 51.65 ? 54 LEU B CD1 1 ATOM 3005 C CD2 . LEU B 1 54 ? 15.640 31.064 50.012 1.00 50.45 ? 54 LEU B CD2 1 ATOM 3006 N N . TYR B 1 55 ? 14.188 34.300 53.380 1.00 45.26 ? 55 TYR B N 1 ATOM 3007 C CA . TYR B 1 55 ? 13.339 33.945 54.511 1.00 43.33 ? 55 TYR B CA 1 ATOM 3008 C C . TYR B 1 55 ? 12.649 35.176 55.101 1.00 43.37 ? 55 TYR B C 1 ATOM 3009 O O . TYR B 1 55 ? 13.278 36.006 55.764 1.00 41.69 ? 55 TYR B O 1 ATOM 3010 C CB . TYR B 1 55 ? 14.143 33.134 55.537 1.00 40.57 ? 55 TYR B CB 1 ATOM 3011 C CG . TYR B 1 55 ? 14.572 31.820 54.939 1.00 39.25 ? 55 TYR B CG 1 ATOM 3012 C CD1 . TYR B 1 55 ? 13.650 30.795 54.766 1.00 40.54 ? 55 TYR B CD1 1 ATOM 3013 C CD2 . TYR B 1 55 ? 15.874 31.623 54.479 1.00 40.26 ? 55 TYR B CD2 1 ATOM 3014 C CE1 . TYR B 1 55 ? 14.016 29.576 54.183 1.00 39.99 ? 55 TYR B CE1 1 ATOM 3015 C CE2 . TYR B 1 55 ? 16.264 30.395 53.892 1.00 39.55 ? 55 TYR B CE2 1 ATOM 3016 C CZ . TYR B 1 55 ? 15.317 29.381 53.742 1.00 39.36 ? 55 TYR B CZ 1 ATOM 3017 O OH . TYR B 1 55 ? 15.637 28.158 53.174 1.00 38.58 ? 55 TYR B OH 1 ATOM 3018 N N . THR B 1 56 ? 11.356 35.300 54.809 1.00 44.54 ? 56 THR B N 1 ATOM 3019 C CA . THR B 1 56 ? 10.562 36.474 55.205 1.00 45.89 ? 56 THR B CA 1 ATOM 3020 C C . THR B 1 56 ? 10.535 36.664 56.724 1.00 46.04 ? 56 THR B C 1 ATOM 3021 O O . THR B 1 56 ? 10.631 37.794 57.225 1.00 45.63 ? 56 THR B O 1 ATOM 3022 C CB . THR B 1 56 ? 9.141 36.378 54.602 1.00 47.16 ? 56 THR B CB 1 ATOM 3023 O OG1 . THR B 1 56 ? 9.242 36.396 53.171 1.00 47.73 ? 56 THR B OG1 1 ATOM 3024 C CG2 . THR B 1 56 ? 8.321 37.621 54.893 1.00 46.80 ? 56 THR B CG2 1 ATOM 3025 N N . ALA B 1 57 ? 10.456 35.552 57.454 1.00 46.06 ? 57 ALA B N 1 ATOM 3026 C CA . ALA B 1 57 ? 10.476 35.583 58.914 1.00 45.49 ? 57 ALA B CA 1 ATOM 3027 C C . ALA B 1 57 ? 11.781 36.145 59.493 1.00 45.82 ? 57 ALA B C 1 ATOM 3028 O O . ALA B 1 57 ? 11.827 36.516 60.666 1.00 48.79 ? 57 ALA B O 1 ATOM 3029 C CB . ALA B 1 57 ? 10.162 34.191 59.491 1.00 45.32 ? 57 ALA B CB 1 ATOM 3030 N N . CYS B 1 58 ? 12.826 36.218 58.671 1.00 44.18 ? 58 CYS B N 1 ATOM 3031 C CA . CYS B 1 58 ? 14.111 36.829 59.053 1.00 43.50 ? 58 CYS B CA 1 ATOM 3032 C C . CYS B 1 58 ? 14.247 38.318 58.695 1.00 44.12 ? 58 CYS B C 1 ATOM 3033 O O . CYS B 1 58 ? 14.772 39.095 59.483 1.00 45.96 ? 58 CYS B O 1 ATOM 3034 C CB . CYS B 1 58 ? 15.273 36.066 58.414 1.00 43.54 ? 58 CYS B CB 1 ATOM 3035 S SG . CYS B 1 58 ? 15.644 34.476 59.184 1.00 43.85 ? 58 CYS B SG 1 ATOM 3036 N N . VAL B 1 59 ? 13.800 38.724 57.511 1.00 43.70 ? 59 VAL B N 1 ATOM 3037 C CA . VAL B 1 59 ? 13.901 40.139 57.124 1.00 43.29 ? 59 VAL B CA 1 ATOM 3038 C C . VAL B 1 59 ? 13.268 41.073 58.173 1.00 40.75 ? 59 VAL B C 1 ATOM 3039 O O . VAL B 1 59 ? 13.773 42.164 58.433 1.00 39.08 ? 59 VAL B O 1 ATOM 3040 C CB . VAL B 1 59 ? 13.367 40.422 55.658 1.00 44.46 ? 59 VAL B CB 1 ATOM 3041 C CG1 . VAL B 1 59 ? 12.121 39.633 55.349 1.00 43.10 ? 59 VAL B CG1 1 ATOM 3042 C CG2 . VAL B 1 59 ? 13.132 41.933 55.406 1.00 44.19 ? 59 VAL B CG2 1 ATOM 3043 N N . TYR B 1 60 ? 12.196 40.615 58.808 1.00 40.64 ? 60 TYR B N 1 ATOM 3044 C CA . TYR B 1 60 ? 11.423 41.480 59.692 1.00 40.46 ? 60 TYR B CA 1 ATOM 3045 C C . TYR B 1 60 ? 11.648 41.309 61.217 1.00 39.89 ? 60 TYR B C 1 ATOM 3046 O O . TYR B 1 60 ? 10.958 41.937 62.026 1.00 41.06 ? 60 TYR B O 1 ATOM 3047 C CB . TYR B 1 60 ? 9.949 41.373 59.309 1.00 43.40 ? 60 TYR B CB 1 ATOM 3048 C CG . TYR B 1 60 ? 9.676 41.782 57.868 1.00 43.77 ? 60 TYR B CG 1 ATOM 3049 C CD1 . TYR B 1 60 ? 9.113 40.882 56.967 1.00 42.26 ? 60 TYR B CD1 1 ATOM 3050 C CD2 . TYR B 1 60 ? 10.004 43.070 57.404 1.00 44.33 ? 60 TYR B CD2 1 ATOM 3051 C CE1 . TYR B 1 60 ? 8.854 41.247 55.644 1.00 43.38 ? 60 TYR B CE1 1 ATOM 3052 C CE2 . TYR B 1 60 ? 9.754 43.447 56.077 1.00 42.64 ? 60 TYR B CE2 1 ATOM 3053 C CZ . TYR B 1 60 ? 9.176 42.528 55.208 1.00 44.02 ? 60 TYR B CZ 1 ATOM 3054 O OH . TYR B 1 60 ? 8.910 42.882 53.903 1.00 44.54 ? 60 TYR B OH 1 ATOM 3055 N N . HIS B 1 61 ? 12.604 40.466 61.604 1.00 35.58 ? 61 HIS B N 1 ATOM 3056 C CA . HIS B 1 61 ? 12.946 40.291 63.008 1.00 31.87 ? 61 HIS B CA 1 ATOM 3057 C C . HIS B 1 61 ? 14.387 40.750 63.255 1.00 32.42 ? 61 HIS B C 1 ATOM 3058 O O . HIS B 1 61 ? 15.151 40.916 62.312 1.00 33.56 ? 61 HIS B O 1 ATOM 3059 C CB . HIS B 1 61 ? 12.689 38.840 63.484 1.00 31.71 ? 61 HIS B CB 1 ATOM 3060 C CG . HIS B 1 61 ? 11.231 38.490 63.626 1.00 30.68 ? 61 HIS B CG 1 ATOM 3061 N ND1 . HIS B 1 61 ? 10.572 37.660 62.744 1.00 31.73 ? 61 HIS B ND1 1 ATOM 3062 C CD2 . HIS B 1 61 ? 10.302 38.872 64.540 1.00 30.56 ? 61 HIS B CD2 1 ATOM 3063 C CE1 . HIS B 1 61 ? 9.298 37.555 63.096 1.00 30.09 ? 61 HIS B CE1 1 ATOM 3064 N NE2 . HIS B 1 61 ? 9.109 38.278 64.183 1.00 29.83 ? 61 HIS B NE2 1 ATOM 3065 N N . LYS B 1 62 ? 14.719 40.997 64.522 1.00 33.75 ? 62 LYS B N 1 ATOM 3066 C CA . LYS B 1 62 ? 16.065 41.347 64.981 1.00 36.88 ? 62 LYS B CA 1 ATOM 3067 C C . LYS B 1 62 ? 17.011 40.154 64.809 1.00 35.12 ? 62 LYS B C 1 ATOM 3068 O O . LYS B 1 62 ? 16.639 39.021 65.108 1.00 31.17 ? 62 LYS B O 1 ATOM 3069 C CB . LYS B 1 62 ? 15.999 41.738 66.451 1.00 39.36 ? 62 LYS B CB 1 ATOM 3070 C CG . LYS B 1 62 ? 16.738 43.023 66.791 1.00 46.39 ? 62 LYS B CG 1 ATOM 3071 C CD . LYS B 1 62 ? 18.123 42.776 67.380 1.00 49.41 ? 62 LYS B CD 1 ATOM 3072 C CE . LYS B 1 62 ? 18.656 44.061 68.029 1.00 51.83 ? 62 LYS B CE 1 ATOM 3073 N NZ . LYS B 1 62 ? 17.607 44.794 68.823 1.00 50.69 ? 62 LYS B NZ 1 ATOM 3074 N N . LEU B 1 63 ? 18.234 40.409 64.341 1.00 36.13 ? 63 LEU B N 1 ATOM 3075 C CA . LEU B 1 63 ? 19.161 39.323 63.963 1.00 35.34 ? 63 LEU B CA 1 ATOM 3076 C C . LEU B 1 63 ? 20.436 39.348 64.776 1.00 34.78 ? 63 LEU B C 1 ATOM 3077 O O . LEU B 1 63 ? 21.015 40.400 64.960 1.00 33.65 ? 63 LEU B O 1 ATOM 3078 C CB . LEU B 1 63 ? 19.523 39.426 62.474 1.00 35.11 ? 63 LEU B CB 1 ATOM 3079 C CG . LEU B 1 63 ? 18.398 39.628 61.462 1.00 36.22 ? 63 LEU B CG 1 ATOM 3080 C CD1 . LEU B 1 63 ? 18.984 40.114 60.141 1.00 38.19 ? 63 LEU B CD1 1 ATOM 3081 C CD2 . LEU B 1 63 ? 17.526 38.376 61.266 1.00 34.92 ? 63 LEU B CD2 1 ATOM 3082 N N . PHE B 1 64 ? 20.893 38.193 65.258 1.00 33.56 ? 64 PHE B N 1 ATOM 3083 C CA . PHE B 1 64 ? 22.127 38.178 66.053 1.00 33.09 ? 64 PHE B CA 1 ATOM 3084 C C . PHE B 1 64 ? 23.371 38.370 65.162 1.00 33.21 ? 64 PHE B C 1 ATOM 3085 O O . PHE B 1 64 ? 23.555 37.627 64.211 1.00 30.44 ? 64 PHE B O 1 ATOM 3086 C CB . PHE B 1 64 ? 22.238 36.886 66.877 1.00 33.04 ? 64 PHE B CB 1 ATOM 3087 C CG . PHE B 1 64 ? 23.558 36.726 67.583 1.00 31.79 ? 64 PHE B CG 1 ATOM 3088 C CD1 . PHE B 1 64 ? 23.894 37.543 68.647 1.00 31.99 ? 64 PHE B CD1 1 ATOM 3089 C CD2 . PHE B 1 64 ? 24.451 35.742 67.189 1.00 33.41 ? 64 PHE B CD2 1 ATOM 3090 C CE1 . PHE B 1 64 ? 25.100 37.404 69.309 1.00 30.57 ? 64 PHE B CE1 1 ATOM 3091 C CE2 . PHE B 1 64 ? 25.680 35.592 67.844 1.00 33.60 ? 64 PHE B CE2 1 ATOM 3092 C CZ . PHE B 1 64 ? 25.993 36.425 68.911 1.00 33.59 ? 64 PHE B CZ 1 ATOM 3093 N N . ASP B 1 65 ? 24.191 39.381 65.453 1.00 32.07 ? 65 ASP B N 1 ATOM 3094 C CA . ASP B 1 65 ? 25.418 39.610 64.664 1.00 33.48 ? 65 ASP B CA 1 ATOM 3095 C C . ASP B 1 65 ? 26.647 39.168 65.428 1.00 32.47 ? 65 ASP B C 1 ATOM 3096 O O . ASP B 1 65 ? 27.161 39.915 66.266 1.00 32.86 ? 65 ASP B O 1 ATOM 3097 C CB . ASP B 1 65 ? 25.559 41.074 64.240 1.00 36.87 ? 65 ASP B CB 1 ATOM 3098 C CG . ASP B 1 65 ? 26.550 41.251 63.087 1.00 41.18 ? 65 ASP B CG 1 ATOM 3099 O OD1 . ASP B 1 65 ? 27.495 40.432 62.976 1.00 39.83 ? 65 ASP B OD1 1 ATOM 3100 O OD2 . ASP B 1 65 ? 26.460 42.165 62.234 1.00 43.11 ? 65 ASP B OD2 1 ATOM 3101 N N . ALA B 1 66 ? 27.117 37.947 65.151 1.00 33.84 ? 66 ALA B N 1 ATOM 3102 C CA . ALA B 1 66 ? 28.237 37.362 65.926 1.00 35.64 ? 66 ALA B CA 1 ATOM 3103 C C . ALA B 1 66 ? 29.506 38.222 65.863 1.00 37.05 ? 66 ALA B C 1 ATOM 3104 O O . ALA B 1 66 ? 30.203 38.383 66.856 1.00 37.56 ? 66 ALA B O 1 ATOM 3105 C CB . ALA B 1 66 ? 28.532 35.916 65.473 1.00 35.54 ? 66 ALA B CB 1 ATOM 3106 N N . SER B 1 67 ? 29.774 38.795 64.694 1.00 38.22 ? 67 SER B N 1 ATOM 3107 C CA . SER B 1 67 ? 30.917 39.670 64.495 1.00 39.41 ? 67 SER B CA 1 ATOM 3108 C C . SER B 1 67 ? 30.903 40.883 65.430 1.00 40.40 ? 67 SER B C 1 ATOM 3109 O O . SER B 1 67 ? 31.966 41.434 65.710 1.00 42.24 ? 67 SER B O 1 ATOM 3110 C CB . SER B 1 67 ? 30.993 40.130 63.031 1.00 39.65 ? 67 SER B CB 1 ATOM 3111 O OG . SER B 1 67 ? 29.950 41.044 62.693 1.00 39.06 ? 67 SER B OG 1 ATOM 3112 N N . ASP B 1 68 ? 29.713 41.292 65.892 1.00 38.88 ? 68 ASP B N 1 ATOM 3113 C CA . ASP B 1 68 ? 29.566 42.411 66.836 1.00 39.71 ? 68 ASP B CA 1 ATOM 3114 C C . ASP B 1 68 ? 29.769 42.050 68.314 1.00 39.15 ? 68 ASP B C 1 ATOM 3115 O O . ASP B 1 68 ? 29.750 42.935 69.160 1.00 39.52 ? 68 ASP B O 1 ATOM 3116 C CB . ASP B 1 68 ? 28.180 43.082 66.713 1.00 42.02 ? 68 ASP B CB 1 ATOM 3117 C CG . ASP B 1 68 ? 27.981 43.836 65.403 1.00 45.06 ? 68 ASP B CG 1 ATOM 3118 O OD1 . ASP B 1 68 ? 28.971 44.379 64.845 1.00 47.83 ? 68 ASP B OD1 1 ATOM 3119 O OD2 . ASP B 1 68 ? 26.849 43.945 64.869 1.00 44.93 ? 68 ASP B OD2 1 ATOM 3120 N N . SER B 1 69 ? 29.953 40.775 68.645 1.00 39.37 ? 69 SER B N 1 ATOM 3121 C CA . SER B 1 69 ? 30.064 40.390 70.068 1.00 39.77 ? 69 SER B CA 1 ATOM 3122 C C . SER B 1 69 ? 31.483 39.953 70.431 1.00 40.36 ? 69 SER B C 1 ATOM 3123 O O . SER B 1 69 ? 31.982 38.977 69.868 1.00 39.85 ? 69 SER B O 1 ATOM 3124 C CB . SER B 1 69 ? 29.046 39.286 70.433 1.00 39.85 ? 69 SER B CB 1 ATOM 3125 O OG . SER B 1 69 ? 29.181 38.885 71.792 1.00 38.84 ? 69 SER B OG 1 ATOM 3126 N N . SER B 1 70 ? 32.111 40.678 71.364 1.00 40.88 ? 70 SER B N 1 ATOM 3127 C CA . SER B 1 70 ? 33.454 40.355 71.873 1.00 41.50 ? 70 SER B CA 1 ATOM 3128 C C . SER B 1 70 ? 33.537 39.080 72.708 1.00 43.55 ? 70 SER B C 1 ATOM 3129 O O . SER B 1 70 ? 34.629 38.524 72.883 1.00 45.62 ? 70 SER B O 1 ATOM 3130 C CB . SER B 1 70 ? 33.994 41.510 72.706 1.00 41.54 ? 70 SER B CB 1 ATOM 3131 O OG . SER B 1 70 ? 33.326 41.597 73.952 1.00 39.92 ? 70 SER B OG 1 ATOM 3132 N N . SER B 1 71 ? 32.395 38.626 73.232 1.00 41.92 ? 71 SER B N 1 ATOM 3133 C CA . SER B 1 71 ? 32.327 37.380 73.999 1.00 39.72 ? 71 SER B CA 1 ATOM 3134 C C . SER B 1 71 ? 31.828 36.161 73.214 1.00 38.38 ? 71 SER B C 1 ATOM 3135 O O . SER B 1 71 ? 31.695 35.071 73.783 1.00 38.78 ? 71 SER B O 1 ATOM 3136 C CB . SER B 1 71 ? 31.483 37.579 75.269 1.00 40.23 ? 71 SER B CB 1 ATOM 3137 O OG . SER B 1 71 ? 30.344 38.384 75.033 1.00 39.02 ? 71 SER B OG 1 ATOM 3138 N N . TYR B 1 72 ? 31.564 36.329 71.921 1.00 38.53 ? 72 TYR B N 1 ATOM 3139 C CA . TYR B 1 72 ? 31.042 35.228 71.079 1.00 39.48 ? 72 TYR B CA 1 ATOM 3140 C C . TYR B 1 72 ? 32.066 34.095 70.915 1.00 42.46 ? 72 TYR B C 1 ATOM 3141 O O . TYR B 1 72 ? 33.276 34.351 70.869 1.00 43.92 ? 72 TYR B O 1 ATOM 3142 C CB . TYR B 1 72 ? 30.587 35.782 69.720 1.00 37.05 ? 72 TYR B CB 1 ATOM 3143 C CG . TYR B 1 72 ? 30.446 34.768 68.601 1.00 37.02 ? 72 TYR B CG 1 ATOM 3144 C CD1 . TYR B 1 72 ? 31.477 34.581 67.673 1.00 36.29 ? 72 TYR B CD1 1 ATOM 3145 C CD2 . TYR B 1 72 ? 29.279 33.993 68.460 1.00 37.03 ? 72 TYR B CD2 1 ATOM 3146 C CE1 . TYR B 1 72 ? 31.354 33.642 66.634 1.00 37.16 ? 72 TYR B CE1 1 ATOM 3147 C CE2 . TYR B 1 72 ? 29.149 33.058 67.430 1.00 36.78 ? 72 TYR B CE2 1 ATOM 3148 C CZ . TYR B 1 72 ? 30.195 32.893 66.523 1.00 36.74 ? 72 TYR B CZ 1 ATOM 3149 O OH . TYR B 1 72 ? 30.080 31.989 65.505 1.00 39.08 ? 72 TYR B OH 1 ATOM 3150 N N . LYS B 1 73 ? 31.588 32.854 70.841 1.00 42.17 ? 73 LYS B N 1 ATOM 3151 C CA . LYS B 1 73 ? 32.457 31.723 70.561 1.00 44.73 ? 73 LYS B CA 1 ATOM 3152 C C . LYS B 1 73 ? 31.850 30.824 69.502 1.00 44.88 ? 73 LYS B C 1 ATOM 3153 O O . LYS B 1 73 ? 30.740 30.304 69.653 1.00 43.63 ? 73 LYS B O 1 ATOM 3154 C CB . LYS B 1 73 ? 32.768 30.919 71.821 1.00 46.30 ? 73 LYS B CB 1 ATOM 3155 C CG . LYS B 1 73 ? 34.067 30.117 71.757 1.00 48.40 ? 73 LYS B CG 1 ATOM 3156 C CD . LYS B 1 73 ? 34.276 29.269 73.024 1.00 49.07 ? 73 LYS B CD 1 ATOM 3157 C CE . LYS B 1 73 ? 34.940 30.051 74.165 1.00 50.98 ? 73 LYS B CE 1 ATOM 3158 N NZ . LYS B 1 73 ? 36.411 29.811 74.230 1.00 51.28 ? 73 LYS B NZ 1 ATOM 3159 N N . HIS B 1 74 ? 32.586 30.657 68.408 1.00 46.57 ? 74 HIS B N 1 ATOM 3160 C CA . HIS B 1 74 ? 32.184 29.748 67.357 1.00 46.93 ? 74 HIS B CA 1 ATOM 3161 C C . HIS B 1 74 ? 31.995 28.350 67.925 1.00 45.39 ? 74 HIS B C 1 ATOM 3162 O O . HIS B 1 74 ? 32.721 27.915 68.820 1.00 46.60 ? 74 HIS B O 1 ATOM 3163 C CB . HIS B 1 74 ? 33.215 29.729 66.214 1.00 49.13 ? 74 HIS B CB 1 ATOM 3164 C CG . HIS B 1 74 ? 32.822 28.852 65.066 1.00 51.24 ? 74 HIS B CG 1 ATOM 3165 N ND1 . HIS B 1 74 ? 33.535 27.726 64.712 1.00 53.21 ? 74 HIS B ND1 1 ATOM 3166 C CD2 . HIS B 1 74 ? 31.767 28.912 64.216 1.00 53.22 ? 74 HIS B CD2 1 ATOM 3167 C CE1 . HIS B 1 74 ? 32.949 27.142 63.680 1.00 53.36 ? 74 HIS B CE1 1 ATOM 3168 N NE2 . HIS B 1 74 ? 31.869 27.836 63.364 1.00 53.33 ? 74 HIS B NE2 1 ATOM 3169 N N . ASN B 1 75 ? 30.973 27.683 67.423 1.00 45.10 ? 75 ASN B N 1 ATOM 3170 C CA . ASN B 1 75 ? 30.799 26.263 67.608 1.00 46.06 ? 75 ASN B CA 1 ATOM 3171 C C . ASN B 1 75 ? 30.472 25.704 66.214 1.00 45.42 ? 75 ASN B C 1 ATOM 3172 O O . ASN B 1 75 ? 31.320 25.070 65.568 1.00 41.70 ? 75 ASN B O 1 ATOM 3173 C CB . ASN B 1 75 ? 29.693 25.987 68.637 1.00 46.93 ? 75 ASN B CB 1 ATOM 3174 C CG . ASN B 1 75 ? 29.637 24.538 69.054 1.00 50.54 ? 75 ASN B CG 1 ATOM 3175 O OD1 . ASN B 1 75 ? 28.964 23.731 68.415 1.00 49.78 ? 75 ASN B OD1 1 ATOM 3176 N ND2 . ASN B 1 75 ? 30.337 24.201 70.144 1.00 56.12 ? 75 ASN B ND2 1 ATOM 3177 N N . GLY B 1 76 ? 29.254 25.981 65.743 1.00 43.59 ? 76 GLY B N 1 ATOM 3178 C CA . GLY B 1 76 ? 28.886 25.702 64.370 1.00 42.47 ? 76 GLY B CA 1 ATOM 3179 C C . GLY B 1 76 ? 28.184 24.395 64.082 1.00 43.19 ? 76 GLY B C 1 ATOM 3180 O O . GLY B 1 76 ? 27.837 24.145 62.936 1.00 45.07 ? 76 GLY B O 1 ATOM 3181 N N . THR B 1 77 ? 27.958 23.557 65.094 1.00 43.98 ? 77 THR B N 1 ATOM 3182 C CA . THR B 1 77 ? 27.172 22.333 64.892 1.00 47.11 ? 77 THR B CA 1 ATOM 3183 C C . THR B 1 77 ? 25.755 22.693 64.404 1.00 47.47 ? 77 THR B C 1 ATOM 3184 O O . THR B 1 77 ? 25.085 23.517 65.011 1.00 46.55 ? 77 THR B O 1 ATOM 3185 C CB . THR B 1 77 ? 27.094 21.481 66.185 1.00 48.87 ? 77 THR B CB 1 ATOM 3186 O OG1 . THR B 1 77 ? 28.407 21.072 66.591 1.00 50.44 ? 77 THR B OG1 1 ATOM 3187 C CG2 . THR B 1 77 ? 26.393 20.148 65.910 1.00 49.46 ? 77 THR B CG2 1 ATOM 3188 N N . GLU B 1 78 ? 25.322 22.085 63.306 1.00 47.78 ? 78 GLU B N 1 ATOM 3189 C CA . GLU B 1 78 ? 24.020 22.362 62.715 1.00 51.15 ? 78 GLU B CA 1 ATOM 3190 C C . GLU B 1 78 ? 22.903 21.782 63.597 1.00 48.82 ? 78 GLU B C 1 ATOM 3191 O O . GLU B 1 78 ? 23.080 20.730 64.226 1.00 46.19 ? 78 GLU B O 1 ATOM 3192 C CB . GLU B 1 78 ? 23.954 21.796 61.277 1.00 53.70 ? 78 GLU B CB 1 ATOM 3193 C CG . GLU B 1 78 ? 24.956 22.405 60.282 1.00 56.74 ? 78 GLU B CG 1 ATOM 3194 C CD . GLU B 1 78 ? 24.617 22.162 58.792 1.00 59.20 ? 78 GLU B CD 1 ATOM 3195 O OE1 . GLU B 1 78 ? 24.182 21.038 58.433 1.00 61.43 ? 78 GLU B OE1 1 ATOM 3196 O OE2 . GLU B 1 78 ? 24.798 23.099 57.959 1.00 60.43 ? 78 GLU B OE2 1 ATOM 3197 N N . LEU B 1 79 ? 21.764 22.476 63.656 1.00 48.44 ? 79 LEU B N 1 ATOM 3198 C CA . LEU B 1 79 ? 20.586 22.006 64.409 1.00 46.53 ? 79 LEU B CA 1 ATOM 3199 C C . LEU B 1 79 ? 19.339 22.119 63.557 1.00 45.37 ? 79 LEU B C 1 ATOM 3200 O O . LEU B 1 79 ? 19.174 23.104 62.827 1.00 42.68 ? 79 LEU B O 1 ATOM 3201 C CB . LEU B 1 79 ? 20.360 22.837 65.676 1.00 48.71 ? 79 LEU B CB 1 ATOM 3202 C CG . LEU B 1 79 ? 21.524 23.322 66.536 1.00 50.14 ? 79 LEU B CG 1 ATOM 3203 C CD1 . LEU B 1 79 ? 21.092 24.512 67.362 1.00 51.23 ? 79 LEU B CD1 1 ATOM 3204 C CD2 . LEU B 1 79 ? 22.030 22.188 67.424 1.00 52.78 ? 79 LEU B CD2 1 ATOM 3205 N N . THR B 1 80 ? 18.454 21.129 63.684 1.00 43.45 ? 80 THR B N 1 ATOM 3206 C CA . THR B 1 80 ? 17.175 21.094 62.962 1.00 43.15 ? 80 THR B CA 1 ATOM 3207 C C . THR B 1 80 ? 16.014 20.785 63.897 1.00 41.15 ? 80 THR B C 1 ATOM 3208 O O . THR B 1 80 ? 16.180 20.075 64.874 1.00 39.94 ? 80 THR B O 1 ATOM 3209 C CB . THR B 1 80 ? 17.235 20.068 61.787 1.00 44.24 ? 80 THR B CB 1 ATOM 3210 O OG1 . THR B 1 80 ? 17.675 20.735 60.597 1.00 47.99 ? 80 THR B OG1 1 ATOM 3211 C CG2 . THR B 1 80 ? 15.844 19.568 61.391 1.00 43.98 ? 80 THR B CG2 1 ATOM 3212 N N . LEU B 1 81 ? 14.841 21.333 63.591 1.00 42.30 ? 81 LEU B N 1 ATOM 3213 C CA . LEU B 1 81 ? 13.604 20.989 64.298 1.00 41.52 ? 81 LEU B CA 1 ATOM 3214 C C . LEU B 1 81 ? 12.509 20.826 63.255 1.00 41.52 ? 81 LEU B C 1 ATOM 3215 O O . LEU B 1 81 ? 12.236 21.756 62.481 1.00 38.52 ? 81 LEU B O 1 ATOM 3216 C CB . LEU B 1 81 ? 13.216 22.106 65.280 1.00 42.11 ? 81 LEU B CB 1 ATOM 3217 C CG . LEU B 1 81 ? 12.230 21.989 66.458 1.00 44.55 ? 81 LEU B CG 1 ATOM 3218 C CD1 . LEU B 1 81 ? 11.641 23.401 66.753 1.00 44.37 ? 81 LEU B CD1 1 ATOM 3219 C CD2 . LEU B 1 81 ? 11.102 20.961 66.297 1.00 44.24 ? 81 LEU B CD2 1 ATOM 3220 N N . ARG B 1 82 ? 11.879 19.657 63.232 1.00 42.74 ? 82 ARG B N 1 ATOM 3221 C CA . ARG B 1 82 ? 10.792 19.406 62.294 1.00 46.96 ? 82 ARG B CA 1 ATOM 3222 C C . ARG B 1 82 ? 9.487 20.023 62.810 1.00 47.26 ? 82 ARG B C 1 ATOM 3223 O O . ARG B 1 82 ? 8.657 19.365 63.441 1.00 48.80 ? 82 ARG B O 1 ATOM 3224 C CB . ARG B 1 82 ? 10.664 17.911 61.980 1.00 49.77 ? 82 ARG B CB 1 ATOM 3225 C CG . ARG B 1 82 ? 11.940 17.329 61.367 1.00 53.28 ? 82 ARG B CG 1 ATOM 3226 C CD . ARG B 1 82 ? 11.721 16.509 60.092 1.00 59.34 ? 82 ARG B CD 1 ATOM 3227 N NE . ARG B 1 82 ? 11.498 15.083 60.353 1.00 61.65 ? 82 ARG B NE 1 ATOM 3228 C CZ . ARG B 1 82 ? 10.381 14.425 60.050 1.00 63.80 ? 82 ARG B CZ 1 ATOM 3229 N NH1 . ARG B 1 82 ? 10.281 13.126 60.326 1.00 63.07 ? 82 ARG B NH1 1 ATOM 3230 N NH2 . ARG B 1 82 ? 9.363 15.055 59.461 1.00 64.22 ? 82 ARG B NH2 1 ATOM 3231 N N . TYR B 1 83 ? 9.341 21.317 62.560 1.00 47.41 ? 83 TYR B N 1 ATOM 3232 C CA . TYR B 1 83 ? 8.164 22.048 62.987 1.00 45.64 ? 83 TYR B CA 1 ATOM 3233 C C . TYR B 1 83 ? 6.992 21.724 62.053 1.00 45.29 ? 83 TYR B C 1 ATOM 3234 O O . TYR B 1 83 ? 7.200 21.358 60.898 1.00 46.25 ? 83 TYR B O 1 ATOM 3235 C CB . TYR B 1 83 ? 8.461 23.553 63.043 1.00 43.20 ? 83 TYR B CB 1 ATOM 3236 C CG . TYR B 1 83 ? 7.291 24.358 63.550 1.00 42.30 ? 83 TYR B CG 1 ATOM 3237 C CD1 . TYR B 1 83 ? 6.513 25.113 62.674 1.00 41.15 ? 83 TYR B CD1 1 ATOM 3238 C CD2 . TYR B 1 83 ? 6.934 24.328 64.899 1.00 40.24 ? 83 TYR B CD2 1 ATOM 3239 C CE1 . TYR B 1 83 ? 5.408 25.834 63.135 1.00 41.31 ? 83 TYR B CE1 1 ATOM 3240 C CE2 . TYR B 1 83 ? 5.835 25.054 65.372 1.00 40.04 ? 83 TYR B CE2 1 ATOM 3241 C CZ . TYR B 1 83 ? 5.078 25.801 64.483 1.00 41.86 ? 83 TYR B CZ 1 ATOM 3242 O OH . TYR B 1 83 ? 3.991 26.525 64.931 1.00 41.43 ? 83 TYR B OH 1 ATOM 3243 N N . SER B 1 84 ? 5.767 21.858 62.553 1.00 46.97 ? 84 SER B N 1 ATOM 3244 C CA . SER B 1 84 ? 4.572 21.424 61.811 1.00 47.97 ? 84 SER B CA 1 ATOM 3245 C C . SER B 1 84 ? 4.398 22.003 60.403 1.00 47.68 ? 84 SER B C 1 ATOM 3246 O O . SER B 1 84 ? 3.950 21.288 59.508 1.00 46.53 ? 84 SER B O 1 ATOM 3247 C CB . SER B 1 84 ? 3.300 21.643 62.636 1.00 49.75 ? 84 SER B CB 1 ATOM 3248 O OG . SER B 1 84 ? 2.963 23.015 62.709 1.00 51.68 ? 84 SER B OG 1 ATOM 3249 N N . THR B 1 85 ? 4.743 23.284 60.205 1.00 47.67 ? 85 THR B N 1 ATOM 3250 C CA . THR B 1 85 ? 4.592 23.929 58.882 1.00 45.58 ? 85 THR B CA 1 ATOM 3251 C C . THR B 1 85 ? 5.840 23.860 57.990 1.00 46.02 ? 85 THR B C 1 ATOM 3252 O O . THR B 1 85 ? 5.852 24.408 56.873 1.00 45.43 ? 85 THR B O 1 ATOM 3253 C CB . THR B 1 85 ? 4.115 25.403 59.005 1.00 46.07 ? 85 THR B CB 1 ATOM 3254 O OG1 . THR B 1 85 ? 5.176 26.216 59.529 1.00 45.64 ? 85 THR B OG1 1 ATOM 3255 C CG2 . THR B 1 85 ? 2.996 25.531 60.019 1.00 45.34 ? 85 THR B CG2 1 ATOM 3256 N N . GLY B 1 86 ? 6.886 23.192 58.473 1.00 46.15 ? 86 GLY B N 1 ATOM 3257 C CA . GLY B 1 86 ? 8.133 23.059 57.711 1.00 46.98 ? 86 GLY B CA 1 ATOM 3258 C C . GLY B 1 86 ? 9.351 23.079 58.609 1.00 47.38 ? 86 GLY B C 1 ATOM 3259 O O . GLY B 1 86 ? 9.230 23.236 59.825 1.00 47.92 ? 86 GLY B O 1 ATOM 3260 N N . THR B 1 87 ? 10.533 22.953 58.010 1.00 46.25 ? 87 THR B N 1 ATOM 3261 C CA . THR B 1 87 ? 11.768 22.788 58.780 1.00 44.38 ? 87 THR B CA 1 ATOM 3262 C C . THR B 1 87 ? 12.375 24.099 59.335 1.00 42.29 ? 87 THR B C 1 ATOM 3263 O O . THR B 1 87 ? 12.454 25.110 58.626 1.00 41.17 ? 87 THR B O 1 ATOM 3264 C CB . THR B 1 87 ? 12.801 21.984 57.944 1.00 45.55 ? 87 THR B CB 1 ATOM 3265 O OG1 . THR B 1 87 ? 13.399 20.958 58.757 1.00 47.79 ? 87 THR B OG1 1 ATOM 3266 C CG2 . THR B 1 87 ? 13.968 22.860 57.514 1.00 45.26 ? 87 THR B CG2 1 ATOM 3267 N N . VAL B 1 88 ? 12.796 24.076 60.603 1.00 38.70 ? 88 VAL B N 1 ATOM 3268 C CA . VAL B 1 88 ? 13.637 25.173 61.143 1.00 37.79 ? 88 VAL B CA 1 ATOM 3269 C C . VAL B 1 88 ? 15.055 24.673 61.402 1.00 35.92 ? 88 VAL B C 1 ATOM 3270 O O . VAL B 1 88 ? 15.256 23.601 61.997 1.00 36.41 ? 88 VAL B O 1 ATOM 3271 C CB . VAL B 1 88 ? 12.941 26.008 62.323 1.00 37.31 ? 88 VAL B CB 1 ATOM 3272 C CG1 . VAL B 1 88 ? 11.914 25.194 63.074 1.00 40.14 ? 88 VAL B CG1 1 ATOM 3273 C CG2 . VAL B 1 88 ? 13.937 26.715 63.259 1.00 35.39 ? 88 VAL B CG2 1 ATOM 3274 N N . SER B 1 89 ? 16.038 25.403 60.881 1.00 33.74 ? 89 SER B N 1 ATOM 3275 C CA . SER B 1 89 ? 17.415 25.007 61.083 1.00 33.75 ? 89 SER B CA 1 ATOM 3276 C C . SER B 1 89 ? 18.337 26.150 61.432 1.00 32.89 ? 89 SER B C 1 ATOM 3277 O O . SER B 1 89 ? 18.055 27.317 61.163 1.00 32.53 ? 89 SER B O 1 ATOM 3278 C CB . SER B 1 89 ? 17.958 24.193 59.890 1.00 36.15 ? 89 SER B CB 1 ATOM 3279 O OG . SER B 1 89 ? 17.500 24.697 58.646 1.00 39.02 ? 89 SER B OG 1 ATOM 3280 N N . GLY B 1 90 ? 19.460 25.800 62.031 1.00 31.07 ? 90 GLY B N 1 ATOM 3281 C CA . GLY B 1 90 ? 20.455 26.787 62.373 1.00 31.58 ? 90 GLY B CA 1 ATOM 3282 C C . GLY B 1 90 ? 21.731 26.113 62.808 1.00 31.68 ? 90 GLY B C 1 ATOM 3283 O O . GLY B 1 90 ? 21.943 24.929 62.563 1.00 33.12 ? 90 GLY B O 1 ATOM 3284 N N . PHE B 1 91 ? 22.581 26.870 63.468 1.00 31.36 ? 91 PHE B N 1 ATOM 3285 C CA . PHE B 1 91 ? 23.831 26.333 63.970 1.00 31.36 ? 91 PHE B CA 1 ATOM 3286 C C . PHE B 1 91 ? 23.999 26.769 65.425 1.00 31.91 ? 91 PHE B C 1 ATOM 3287 O O . PHE B 1 91 ? 23.332 27.723 65.873 1.00 32.77 ? 91 PHE B O 1 ATOM 3288 C CB . PHE B 1 91 ? 25.017 26.755 63.054 1.00 32.90 ? 91 PHE B CB 1 ATOM 3289 C CG . PHE B 1 91 ? 25.174 28.246 62.885 1.00 32.13 ? 91 PHE B CG 1 ATOM 3290 C CD1 . PHE B 1 91 ? 26.005 28.966 63.737 1.00 32.71 ? 91 PHE B CD1 1 ATOM 3291 C CD2 . PHE B 1 91 ? 24.513 28.921 61.873 1.00 34.61 ? 91 PHE B CD2 1 ATOM 3292 C CE1 . PHE B 1 91 ? 26.164 30.332 63.616 1.00 31.32 ? 91 PHE B CE1 1 ATOM 3293 C CE2 . PHE B 1 91 ? 24.670 30.313 61.718 1.00 32.64 ? 91 PHE B CE2 1 ATOM 3294 C CZ . PHE B 1 91 ? 25.488 31.017 62.594 1.00 33.70 ? 91 PHE B CZ 1 ATOM 3295 N N . LEU B 1 92 ? 24.846 26.046 66.168 1.00 31.75 ? 92 LEU B N 1 ATOM 3296 C CA . LEU B 1 92 ? 25.142 26.341 67.549 1.00 33.69 ? 92 LEU B CA 1 ATOM 3297 C C . LEU B 1 92 ? 26.183 27.440 67.639 1.00 36.24 ? 92 LEU B C 1 ATOM 3298 O O . LEU B 1 92 ? 27.216 27.416 66.929 1.00 36.89 ? 92 LEU B O 1 ATOM 3299 C CB . LEU B 1 92 ? 25.697 25.101 68.275 1.00 36.09 ? 92 LEU B CB 1 ATOM 3300 C CG . LEU B 1 92 ? 24.815 23.983 68.852 1.00 38.93 ? 92 LEU B CG 1 ATOM 3301 C CD1 . LEU B 1 92 ? 25.680 22.924 69.531 1.00 38.52 ? 92 LEU B CD1 1 ATOM 3302 C CD2 . LEU B 1 92 ? 23.776 24.524 69.857 1.00 38.89 ? 92 LEU B CD2 1 ATOM 3303 N N . SER B 1 93 ? 25.937 28.377 68.545 1.00 35.89 ? 93 SER B N 1 ATOM 3304 C CA . SER B 1 93 ? 26.953 29.343 68.959 1.00 34.36 ? 93 SER B CA 1 ATOM 3305 C C . SER B 1 93 ? 26.974 29.450 70.471 1.00 35.95 ? 93 SER B C 1 ATOM 3306 O O . SER B 1 93 ? 26.035 29.044 71.154 1.00 35.89 ? 93 SER B O 1 ATOM 3307 C CB . SER B 1 93 ? 26.685 30.712 68.335 1.00 33.73 ? 93 SER B CB 1 ATOM 3308 O OG . SER B 1 93 ? 26.450 30.570 66.958 1.00 33.62 ? 93 SER B OG 1 ATOM 3309 N N . GLN B 1 94 ? 28.047 30.006 71.006 1.00 34.51 ? 94 GLN B N 1 ATOM 3310 C CA . GLN B 1 94 ? 28.080 30.253 72.419 1.00 34.66 ? 94 GLN B CA 1 ATOM 3311 C C . GLN B 1 94 ? 28.243 31.733 72.673 1.00 33.24 ? 94 GLN B C 1 ATOM 3312 O O . GLN B 1 94 ? 29.023 32.396 71.987 1.00 30.37 ? 94 GLN B O 1 ATOM 3313 C CB . GLN B 1 94 ? 29.198 29.467 73.082 1.00 37.56 ? 94 GLN B CB 1 ATOM 3314 C CG . GLN B 1 94 ? 29.382 29.790 74.541 1.00 38.40 ? 94 GLN B CG 1 ATOM 3315 C CD . GLN B 1 94 ? 30.633 29.178 75.073 1.00 41.82 ? 94 GLN B CD 1 ATOM 3316 O OE1 . GLN B 1 94 ? 30.691 27.970 75.260 1.00 42.30 ? 94 GLN B OE1 1 ATOM 3317 N NE2 . GLN B 1 94 ? 31.654 30.001 75.302 1.00 42.76 ? 94 GLN B NE2 1 ATOM 3318 N N . ASP B 1 95 ? 27.482 32.239 73.648 1.00 31.31 ? 95 ASP B N 1 ATOM 3319 C CA . ASP B 1 95 ? 27.617 33.621 74.083 1.00 33.44 ? 95 ASP B CA 1 ATOM 3320 C C . ASP B 1 95 ? 27.008 33.851 75.462 1.00 32.88 ? 95 ASP B C 1 ATOM 3321 O O . ASP B 1 95 ? 26.330 32.975 76.012 1.00 33.36 ? 95 ASP B O 1 ATOM 3322 C CB . ASP B 1 95 ? 27.003 34.573 73.042 1.00 33.98 ? 95 ASP B CB 1 ATOM 3323 C CG . ASP B 1 95 ? 27.815 35.851 72.850 1.00 35.55 ? 95 ASP B CG 1 ATOM 3324 O OD1 . ASP B 1 95 ? 28.412 36.373 73.831 1.00 36.74 ? 95 ASP B OD1 1 ATOM 3325 O OD2 . ASP B 1 95 ? 27.891 36.413 71.732 1.00 34.64 ? 95 ASP B OD2 1 ATOM 3326 N N . ILE B 1 96 ? 27.305 35.019 76.030 1.00 32.93 ? 96 ILE B N 1 ATOM 3327 C CA . ILE B 1 96 ? 26.721 35.459 77.289 1.00 31.98 ? 96 ILE B CA 1 ATOM 3328 C C . ILE B 1 96 ? 25.293 35.936 77.046 1.00 34.32 ? 96 ILE B C 1 ATOM 3329 O O . ILE B 1 96 ? 25.056 36.853 76.251 1.00 36.06 ? 96 ILE B O 1 ATOM 3330 C CB . ILE B 1 96 ? 27.571 36.587 77.948 1.00 33.32 ? 96 ILE B CB 1 ATOM 3331 C CG1 . ILE B 1 96 ? 28.950 36.081 78.364 1.00 34.87 ? 96 ILE B CG1 1 ATOM 3332 C CG2 . ILE B 1 96 ? 26.876 37.146 79.208 1.00 33.57 ? 96 ILE B CG2 1 ATOM 3333 C CD1 . ILE B 1 96 ? 29.833 35.666 77.241 1.00 38.33 ? 96 ILE B CD1 1 ATOM 3334 N N . ILE B 1 97 ? 24.349 35.299 77.733 1.00 32.97 ? 97 ILE B N 1 ATOM 3335 C CA . ILE B 1 97 ? 22.953 35.723 77.703 1.00 31.85 ? 97 ILE B CA 1 ATOM 3336 C C . ILE B 1 97 ? 22.559 36.309 79.052 1.00 32.25 ? 97 ILE B C 1 ATOM 3337 O O . ILE B 1 97 ? 22.818 35.693 80.100 1.00 30.71 ? 97 ILE B O 1 ATOM 3338 C CB . ILE B 1 97 ? 22.001 34.534 77.292 1.00 30.62 ? 97 ILE B CB 1 ATOM 3339 C CG1 . ILE B 1 97 ? 22.388 33.991 75.920 1.00 27.91 ? 97 ILE B CG1 1 ATOM 3340 C CG2 . ILE B 1 97 ? 20.508 34.971 77.369 1.00 29.39 ? 97 ILE B CG2 1 ATOM 3341 C CD1 . ILE B 1 97 ? 21.382 32.957 75.309 1.00 29.58 ? 97 ILE B CD1 1 ATOM 3342 N N . THR B 1 98 ? 21.938 37.494 78.995 1.00 32.58 ? 98 THR B N 1 ATOM 3343 C CA . THR B 1 98 ? 21.372 38.218 80.146 1.00 34.84 ? 98 THR B CA 1 ATOM 3344 C C . THR B 1 98 ? 19.855 38.052 80.317 1.00 33.69 ? 98 THR B C 1 ATOM 3345 O O . THR B 1 98 ? 19.085 38.501 79.482 1.00 35.99 ? 98 THR B O 1 ATOM 3346 C CB . THR B 1 98 ? 21.701 39.715 80.023 1.00 36.51 ? 98 THR B CB 1 ATOM 3347 O OG1 . THR B 1 98 ? 23.123 39.865 80.017 1.00 39.26 ? 98 THR B OG1 1 ATOM 3348 C CG2 . THR B 1 98 ? 21.295 40.466 81.281 1.00 36.17 ? 98 THR B CG2 1 ATOM 3349 N N . VAL B 1 99 ? 19.429 37.426 81.407 1.00 32.90 ? 99 VAL B N 1 ATOM 3350 C CA . VAL B 1 99 ? 18.001 37.225 81.659 1.00 34.32 ? 99 VAL B CA 1 ATOM 3351 C C . VAL B 1 99 ? 17.643 37.809 83.030 1.00 35.55 ? 99 VAL B C 1 ATOM 3352 O O . VAL B 1 99 ? 18.122 37.332 84.061 1.00 36.45 ? 99 VAL B O 1 ATOM 3353 C CB . VAL B 1 99 ? 17.587 35.731 81.614 1.00 34.28 ? 99 VAL B CB 1 ATOM 3354 C CG1 . VAL B 1 99 ? 16.061 35.609 81.569 1.00 32.96 ? 99 VAL B CG1 1 ATOM 3355 C CG2 . VAL B 1 99 ? 18.201 35.010 80.423 1.00 33.68 ? 99 VAL B CG2 1 ATOM 3356 N N . GLY B 1 100 ? 16.805 38.843 83.039 1.00 35.40 ? 100 GLY B N 1 ATOM 3357 C CA . GLY B 1 100 ? 16.486 39.568 84.276 1.00 32.11 ? 100 GLY B CA 1 ATOM 3358 C C . GLY B 1 100 ? 17.725 39.890 85.116 1.00 33.13 ? 100 GLY B C 1 ATOM 3359 O O . GLY B 1 100 ? 17.694 39.768 86.343 1.00 32.77 ? 100 GLY B O 1 ATOM 3360 N N . GLY B 1 101 ? 18.819 40.278 84.455 1.00 30.74 ? 101 GLY B N 1 ATOM 3361 C CA . GLY B 1 101 ? 20.028 40.680 85.150 1.00 30.68 ? 101 GLY B CA 1 ATOM 3362 C C . GLY B 1 101 ? 21.029 39.565 85.379 1.00 32.51 ? 101 GLY B C 1 ATOM 3363 O O . GLY B 1 101 ? 22.199 39.831 85.634 1.00 32.56 ? 101 GLY B O 1 ATOM 3364 N N . ILE B 1 102 ? 20.562 38.315 85.305 1.00 34.95 ? 102 ILE B N 1 ATOM 3365 C CA . ILE B 1 102 ? 21.395 37.129 85.495 1.00 34.34 ? 102 ILE B CA 1 ATOM 3366 C C . ILE B 1 102 ? 22.152 36.864 84.210 1.00 33.80 ? 102 ILE B C 1 ATOM 3367 O O . ILE B 1 102 ? 21.537 36.791 83.152 1.00 34.97 ? 102 ILE B O 1 ATOM 3368 C CB . ILE B 1 102 ? 20.510 35.888 85.893 1.00 35.39 ? 102 ILE B CB 1 ATOM 3369 C CG1 . ILE B 1 102 ? 19.781 36.141 87.218 1.00 33.44 ? 102 ILE B CG1 1 ATOM 3370 C CG2 . ILE B 1 102 ? 21.349 34.592 85.954 1.00 36.01 ? 102 ILE B CG2 1 ATOM 3371 C CD1 . ILE B 1 102 ? 18.908 35.008 87.697 1.00 34.63 ? 102 ILE B CD1 1 ATOM 3372 N N . THR B 1 103 ? 23.477 36.712 84.287 1.00 35.35 ? 103 THR B N 1 ATOM 3373 C CA . THR B 1 103 ? 24.303 36.430 83.087 1.00 36.54 ? 103 THR B CA 1 ATOM 3374 C C . THR B 1 103 ? 24.795 34.991 83.057 1.00 36.45 ? 103 THR B C 1 ATOM 3375 O O . THR B 1 103 ? 25.295 34.473 84.053 1.00 38.60 ? 103 THR B O 1 ATOM 3376 C CB . THR B 1 103 ? 25.486 37.410 82.940 1.00 40.11 ? 103 THR B CB 1 ATOM 3377 O OG1 . THR B 1 103 ? 26.250 37.426 84.151 1.00 44.31 ? 103 THR B OG1 1 ATOM 3378 C CG2 . THR B 1 103 ? 24.994 38.858 82.802 1.00 39.74 ? 103 THR B CG2 1 ATOM 3379 N N . VAL B 1 104 ? 24.625 34.351 81.905 1.00 35.21 ? 104 VAL B N 1 ATOM 3380 C CA . VAL B 1 104 ? 24.906 32.930 81.725 1.00 34.20 ? 104 VAL B CA 1 ATOM 3381 C C . VAL B 1 104 ? 25.680 32.749 80.437 1.00 34.26 ? 104 VAL B C 1 ATOM 3382 O O . VAL B 1 104 ? 25.238 33.203 79.384 1.00 35.16 ? 104 VAL B O 1 ATOM 3383 C CB . VAL B 1 104 ? 23.616 32.059 81.522 1.00 33.81 ? 104 VAL B CB 1 ATOM 3384 C CG1 . VAL B 1 104 ? 23.703 30.795 82.337 1.00 34.36 ? 104 VAL B CG1 1 ATOM 3385 C CG2 . VAL B 1 104 ? 22.343 32.805 81.851 1.00 34.97 ? 104 VAL B CG2 1 ATOM 3386 N N . THR B 1 105 ? 26.825 32.084 80.502 1.00 32.50 ? 105 THR B N 1 ATOM 3387 C CA . THR B 1 105 ? 27.467 31.593 79.296 1.00 31.36 ? 105 THR B CA 1 ATOM 3388 C C . THR B 1 105 ? 26.602 30.420 78.827 1.00 32.49 ? 105 THR B C 1 ATOM 3389 O O . THR B 1 105 ? 26.383 29.463 79.580 1.00 32.86 ? 105 THR B O 1 ATOM 3390 C CB . THR B 1 105 ? 28.923 31.172 79.582 1.00 32.47 ? 105 THR B CB 1 ATOM 3391 O OG1 . THR B 1 105 ? 29.630 32.273 80.159 1.00 36.86 ? 105 THR B OG1 1 ATOM 3392 C CG2 . THR B 1 105 ? 29.689 30.967 78.303 1.00 28.97 ? 105 THR B CG2 1 ATOM 3393 N N . GLN B 1 106 ? 26.084 30.527 77.599 1.00 31.85 ? 106 GLN B N 1 ATOM 3394 C CA . GLN B 1 106 ? 24.977 29.700 77.119 1.00 27.80 ? 106 GLN B CA 1 ATOM 3395 C C . GLN B 1 106 ? 25.150 29.315 75.674 1.00 30.80 ? 106 GLN B C 1 ATOM 3396 O O . GLN B 1 106 ? 25.530 30.138 74.851 1.00 33.42 ? 106 GLN B O 1 ATOM 3397 C CB . GLN B 1 106 ? 23.638 30.454 77.288 1.00 25.63 ? 106 GLN B CB 1 ATOM 3398 C CG . GLN B 1 106 ? 22.374 29.708 76.852 1.00 26.22 ? 106 GLN B CG 1 ATOM 3399 C CD . GLN B 1 106 ? 22.134 28.437 77.646 1.00 25.53 ? 106 GLN B CD 1 ATOM 3400 O OE1 . GLN B 1 106 ? 22.425 28.388 78.835 1.00 32.83 ? 106 GLN B OE1 1 ATOM 3401 N NE2 . GLN B 1 106 ? 21.656 27.402 76.984 1.00 18.07 ? 106 GLN B NE2 1 ATOM 3402 N N . MET B 1 107 ? 24.832 28.065 75.366 1.00 31.32 ? 107 MET B N 1 ATOM 3403 C CA . MET B 1 107 ? 24.747 27.598 73.991 1.00 32.60 ? 107 MET B CA 1 ATOM 3404 C C . MET B 1 107 ? 23.362 27.848 73.416 1.00 32.88 ? 107 MET B C 1 ATOM 3405 O O . MET B 1 107 ? 22.340 27.495 74.022 1.00 34.11 ? 107 MET B O 1 ATOM 3406 C CB . MET B 1 107 ? 25.054 26.102 73.910 1.00 35.48 ? 107 MET B CB 1 ATOM 3407 C CG . MET B 1 107 ? 26.394 25.700 74.526 1.00 40.47 ? 107 MET B CG 1 ATOM 3408 S SD . MET B 1 107 ? 27.804 26.152 73.506 1.00 46.68 ? 107 MET B SD 1 ATOM 3409 C CE . MET B 1 107 ? 27.641 24.989 72.148 1.00 44.23 ? 107 MET B CE 1 ATOM 3410 N N . PHE B 1 108 ? 23.312 28.455 72.242 1.00 31.60 ? 108 PHE B N 1 ATOM 3411 C CA . PHE B 1 108 ? 22.027 28.696 71.596 1.00 31.12 ? 108 PHE B CA 1 ATOM 3412 C C . PHE B 1 108 ? 22.120 28.431 70.118 1.00 31.39 ? 108 PHE B C 1 ATOM 3413 O O . PHE B 1 108 ? 23.215 28.397 69.569 1.00 31.05 ? 108 PHE B O 1 ATOM 3414 C CB . PHE B 1 108 ? 21.533 30.139 71.858 1.00 31.69 ? 108 PHE B CB 1 ATOM 3415 C CG . PHE B 1 108 ? 22.467 31.206 71.364 1.00 29.01 ? 108 PHE B CG 1 ATOM 3416 C CD1 . PHE B 1 108 ? 23.652 31.484 72.047 1.00 28.30 ? 108 PHE B CD1 1 ATOM 3417 C CD2 . PHE B 1 108 ? 22.159 31.936 70.222 1.00 27.24 ? 108 PHE B CD2 1 ATOM 3418 C CE1 . PHE B 1 108 ? 24.524 32.481 71.584 1.00 30.10 ? 108 PHE B CE1 1 ATOM 3419 C CE2 . PHE B 1 108 ? 23.025 32.934 69.750 1.00 29.47 ? 108 PHE B CE2 1 ATOM 3420 C CZ . PHE B 1 108 ? 24.200 33.211 70.439 1.00 29.27 ? 108 PHE B CZ 1 ATOM 3421 N N . GLY B 1 109 ? 20.966 28.277 69.469 1.00 30.10 ? 109 GLY B N 1 ATOM 3422 C CA . GLY B 1 109 ? 20.895 28.199 68.013 1.00 33.11 ? 109 GLY B CA 1 ATOM 3423 C C . GLY B 1 109 ? 20.660 29.512 67.284 1.00 32.93 ? 109 GLY B C 1 ATOM 3424 O O . GLY B 1 109 ? 19.727 30.259 67.614 1.00 31.52 ? 109 GLY B O 1 ATOM 3425 N N . GLU B 1 110 ? 21.511 29.797 66.289 1.00 31.10 ? 110 GLU B N 1 ATOM 3426 C CA . GLU B 1 110 ? 21.301 30.907 65.356 1.00 33.10 ? 110 GLU B CA 1 ATOM 3427 C C . GLU B 1 110 ? 20.499 30.395 64.145 1.00 32.87 ? 110 GLU B C 1 ATOM 3428 O O . GLU B 1 110 ? 20.994 29.565 63.392 1.00 35.49 ? 110 GLU B O 1 ATOM 3429 C CB . GLU B 1 110 ? 22.638 31.474 64.892 1.00 33.25 ? 110 GLU B CB 1 ATOM 3430 C CG . GLU B 1 110 ? 23.285 32.515 65.798 1.00 35.54 ? 110 GLU B CG 1 ATOM 3431 C CD . GLU B 1 110 ? 24.506 33.165 65.135 1.00 37.16 ? 110 GLU B CD 1 ATOM 3432 O OE1 . GLU B 1 110 ? 24.326 33.904 64.117 1.00 37.22 ? 110 GLU B OE1 1 ATOM 3433 O OE2 . GLU B 1 110 ? 25.643 32.947 65.633 1.00 35.79 ? 110 GLU B OE2 1 ATOM 3434 N N . VAL B 1 111 ? 19.260 30.871 63.983 1.00 32.11 ? 111 VAL B N 1 ATOM 3435 C CA . VAL B 1 111 ? 18.314 30.366 62.956 1.00 32.49 ? 111 VAL B CA 1 ATOM 3436 C C . VAL B 1 111 ? 18.651 30.958 61.577 1.00 31.92 ? 111 VAL B C 1 ATOM 3437 O O . VAL B 1 111 ? 18.831 32.172 61.456 1.00 31.77 ? 111 VAL B O 1 ATOM 3438 C CB . VAL B 1 111 ? 16.828 30.671 63.325 1.00 32.43 ? 111 VAL B CB 1 ATOM 3439 C CG1 . VAL B 1 111 ? 15.874 30.129 62.272 1.00 29.25 ? 111 VAL B CG1 1 ATOM 3440 C CG2 . VAL B 1 111 ? 16.477 30.097 64.690 1.00 32.17 ? 111 VAL B CG2 1 ATOM 3441 N N . THR B 1 112 ? 18.784 30.085 60.573 1.00 30.00 ? 112 THR B N 1 ATOM 3442 C CA . THR B 1 112 ? 19.166 30.484 59.219 1.00 31.56 ? 112 THR B CA 1 ATOM 3443 C C . THR B 1 112 ? 18.029 30.235 58.231 1.00 32.08 ? 112 THR B C 1 ATOM 3444 O O . THR B 1 112 ? 18.021 30.805 57.138 1.00 31.91 ? 112 THR B O 1 ATOM 3445 C CB . THR B 1 112 ? 20.436 29.718 58.733 1.00 30.96 ? 112 THR B CB 1 ATOM 3446 O OG1 . THR B 1 112 ? 20.205 28.306 58.825 1.00 29.46 ? 112 THR B OG1 1 ATOM 3447 C CG2 . THR B 1 112 ? 21.664 29.962 59.637 1.00 23.62 ? 112 THR B CG2 1 ATOM 3448 N N . GLU B 1 113 ? 17.093 29.361 58.601 1.00 35.26 ? 113 GLU B N 1 ATOM 3449 C CA . GLU B 1 113 ? 15.923 29.044 57.760 1.00 39.95 ? 113 GLU B CA 1 ATOM 3450 C C . GLU B 1 113 ? 14.703 28.685 58.595 1.00 36.70 ? 113 GLU B C 1 ATOM 3451 O O . GLU B 1 113 ? 14.817 27.961 59.580 1.00 35.65 ? 113 GLU B O 1 ATOM 3452 C CB . GLU B 1 113 ? 16.219 27.868 56.829 1.00 42.53 ? 113 GLU B CB 1 ATOM 3453 C CG . GLU B 1 113 ? 17.687 27.738 56.422 1.00 47.76 ? 113 GLU B CG 1 ATOM 3454 C CD . GLU B 1 113 ? 17.931 26.603 55.447 1.00 49.25 ? 113 GLU B CD 1 ATOM 3455 O OE1 . GLU B 1 113 ? 17.093 25.661 55.410 1.00 52.85 ? 113 GLU B OE1 1 ATOM 3456 O OE2 . GLU B 1 113 ? 18.961 26.659 54.721 1.00 51.95 ? 113 GLU B OE2 1 ATOM 3457 N N . MET B 1 114 ? 13.535 29.181 58.181 1.00 36.74 ? 114 MET B N 1 ATOM 3458 C CA . MET B 1 114 ? 12.256 28.826 58.799 1.00 38.55 ? 114 MET B CA 1 ATOM 3459 C C . MET B 1 114 ? 11.093 29.206 57.884 1.00 37.50 ? 114 MET B C 1 ATOM 3460 O O . MET B 1 114 ? 11.190 30.180 57.136 1.00 38.38 ? 114 MET B O 1 ATOM 3461 C CB . MET B 1 114 ? 12.084 29.488 60.185 1.00 38.99 ? 114 MET B CB 1 ATOM 3462 C CG . MET B 1 114 ? 11.987 31.012 60.167 1.00 40.76 ? 114 MET B CG 1 ATOM 3463 S SD . MET B 1 114 ? 12.017 31.746 61.823 1.00 41.53 ? 114 MET B SD 1 ATOM 3464 C CE . MET B 1 114 ? 13.414 32.842 61.581 1.00 40.84 ? 114 MET B CE 1 ATOM 3465 N N . PRO B 1 115 ? 9.996 28.447 57.960 1.00 37.33 ? 115 PRO B N 1 ATOM 3466 C CA . PRO B 1 115 ? 8.770 28.749 57.201 1.00 36.11 ? 115 PRO B CA 1 ATOM 3467 C C . PRO B 1 115 ? 8.260 30.163 57.441 1.00 34.82 ? 115 PRO B C 1 ATOM 3468 O O . PRO B 1 115 ? 8.454 30.720 58.517 1.00 35.74 ? 115 PRO B O 1 ATOM 3469 C CB . PRO B 1 115 ? 7.740 27.748 57.758 1.00 35.36 ? 115 PRO B CB 1 ATOM 3470 C CG . PRO B 1 115 ? 8.499 26.683 58.417 1.00 34.75 ? 115 PRO B CG 1 ATOM 3471 C CD . PRO B 1 115 ? 9.852 27.232 58.790 1.00 37.80 ? 115 PRO B CD 1 ATOM 3472 N N . ALA B 1 116 ? 7.586 30.737 56.455 1.00 35.32 ? 116 ALA B N 1 ATOM 3473 C CA . ALA B 1 116 ? 6.993 32.063 56.641 1.00 34.54 ? 116 ALA B CA 1 ATOM 3474 C C . ALA B 1 116 ? 5.928 32.063 57.747 1.00 34.37 ? 116 ALA B C 1 ATOM 3475 O O . ALA B 1 116 ? 5.876 32.984 58.556 1.00 33.27 ? 116 ALA B O 1 ATOM 3476 C CB . ALA B 1 116 ? 6.432 32.615 55.317 1.00 33.64 ? 116 ALA B CB 1 ATOM 3477 N N . LEU B 1 117 ? 5.104 31.021 57.784 1.00 34.99 ? 117 LEU B N 1 ATOM 3478 C CA . LEU B 1 117 ? 4.035 30.920 58.763 1.00 35.81 ? 117 LEU B CA 1 ATOM 3479 C C . LEU B 1 117 ? 4.330 29.837 59.815 1.00 34.98 ? 117 LEU B C 1 ATOM 3480 O O . LEU B 1 117 ? 4.685 28.704 59.447 1.00 33.68 ? 117 LEU B O 1 ATOM 3481 C CB . LEU B 1 117 ? 2.694 30.659 58.053 1.00 38.67 ? 117 LEU B CB 1 ATOM 3482 C CG . LEU B 1 117 ? 2.143 31.771 57.149 1.00 39.30 ? 117 LEU B CG 1 ATOM 3483 C CD1 . LEU B 1 117 ? 1.176 31.183 56.167 1.00 40.67 ? 117 LEU B CD1 1 ATOM 3484 C CD2 . LEU B 1 117 ? 1.465 32.847 57.952 1.00 41.89 ? 117 LEU B CD2 1 ATOM 3485 N N . PRO B 1 118 ? 4.146 30.152 61.105 1.00 34.10 ? 118 PRO B N 1 ATOM 3486 C CA . PRO B 1 118 ? 3.608 31.442 61.569 1.00 33.10 ? 118 PRO B CA 1 ATOM 3487 C C . PRO B 1 118 ? 4.677 32.464 61.954 1.00 32.29 ? 118 PRO B C 1 ATOM 3488 O O . PRO B 1 118 ? 4.356 33.538 62.462 1.00 31.89 ? 118 PRO B O 1 ATOM 3489 C CB . PRO B 1 118 ? 2.839 31.035 62.818 1.00 34.42 ? 118 PRO B CB 1 ATOM 3490 C CG . PRO B 1 118 ? 3.671 29.856 63.393 1.00 35.71 ? 118 PRO B CG 1 ATOM 3491 C CD . PRO B 1 118 ? 4.373 29.219 62.229 1.00 33.99 ? 118 PRO B CD 1 ATOM 3492 N N . PHE B 1 119 ? 5.931 32.151 61.671 1.00 30.16 ? 119 PHE B N 1 ATOM 3493 C CA . PHE B 1 119 ? 7.026 32.871 62.286 1.00 30.45 ? 119 PHE B CA 1 ATOM 3494 C C . PHE B 1 119 ? 7.119 34.325 61.863 1.00 32.45 ? 119 PHE B C 1 ATOM 3495 O O . PHE B 1 119 ? 7.583 35.152 62.640 1.00 33.99 ? 119 PHE B O 1 ATOM 3496 C CB . PHE B 1 119 ? 8.329 32.107 62.071 1.00 30.93 ? 119 PHE B CB 1 ATOM 3497 C CG . PHE B 1 119 ? 8.271 30.687 62.593 1.00 30.53 ? 119 PHE B CG 1 ATOM 3498 C CD1 . PHE B 1 119 ? 8.417 30.432 63.947 1.00 31.71 ? 119 PHE B CD1 1 ATOM 3499 C CD2 . PHE B 1 119 ? 8.054 29.622 61.734 1.00 30.45 ? 119 PHE B CD2 1 ATOM 3500 C CE1 . PHE B 1 119 ? 8.352 29.123 64.450 1.00 32.45 ? 119 PHE B CE1 1 ATOM 3501 C CE2 . PHE B 1 119 ? 7.984 28.308 62.220 1.00 29.08 ? 119 PHE B CE2 1 ATOM 3502 C CZ . PHE B 1 119 ? 8.131 28.066 63.577 1.00 29.85 ? 119 PHE B CZ 1 ATOM 3503 N N . MET B 1 120 ? 6.659 34.647 60.653 1.00 35.12 ? 120 MET B N 1 ATOM 3504 C CA . MET B 1 120 ? 6.730 36.032 60.181 1.00 39.05 ? 120 MET B CA 1 ATOM 3505 C C . MET B 1 120 ? 5.750 36.939 60.926 1.00 37.94 ? 120 MET B C 1 ATOM 3506 O O . MET B 1 120 ? 5.975 38.144 61.010 1.00 39.69 ? 120 MET B O 1 ATOM 3507 C CB . MET B 1 120 ? 6.572 36.145 58.660 1.00 40.60 ? 120 MET B CB 1 ATOM 3508 C CG . MET B 1 120 ? 5.123 36.136 58.138 1.00 43.83 ? 120 MET B CG 1 ATOM 3509 S SD . MET B 1 120 ? 5.060 36.546 56.373 1.00 45.35 ? 120 MET B SD 1 ATOM 3510 C CE . MET B 1 120 ? 4.940 38.336 56.427 1.00 46.53 ? 120 MET B CE 1 ATOM 3511 N N . LEU B 1 121 ? 4.716 36.331 61.508 1.00 36.25 ? 121 LEU B N 1 ATOM 3512 C CA . LEU B 1 121 ? 3.662 37.042 62.225 1.00 36.28 ? 121 LEU B CA 1 ATOM 3513 C C . LEU B 1 121 ? 3.822 37.082 63.755 1.00 35.85 ? 121 LEU B C 1 ATOM 3514 O O . LEU B 1 121 ? 2.908 37.537 64.460 1.00 35.79 ? 121 LEU B O 1 ATOM 3515 C CB . LEU B 1 121 ? 2.290 36.445 61.871 1.00 35.18 ? 121 LEU B CB 1 ATOM 3516 C CG . LEU B 1 121 ? 1.848 36.411 60.412 1.00 36.02 ? 121 LEU B CG 1 ATOM 3517 C CD1 . LEU B 1 121 ? 0.443 35.877 60.373 1.00 35.05 ? 121 LEU B CD1 1 ATOM 3518 C CD2 . LEU B 1 121 ? 1.945 37.796 59.728 1.00 36.06 ? 121 LEU B CD2 1 ATOM 3519 N N . ALA B 1 122 ? 4.958 36.583 64.248 1.00 30.98 ? 122 ALA B N 1 ATOM 3520 C CA . ALA B 1 122 ? 5.316 36.638 65.647 1.00 30.09 ? 122 ALA B CA 1 ATOM 3521 C C . ALA B 1 122 ? 5.856 38.044 65.994 1.00 30.54 ? 122 ALA B C 1 ATOM 3522 O O . ALA B 1 122 ? 6.621 38.612 65.213 1.00 28.73 ? 122 ALA B O 1 ATOM 3523 C CB . ALA B 1 122 ? 6.350 35.581 65.930 1.00 27.83 ? 122 ALA B CB 1 ATOM 3524 N N . GLU B 1 123 ? 5.424 38.611 67.129 1.00 28.85 ? 123 GLU B N 1 ATOM 3525 C CA . GLU B 1 123 ? 5.936 39.898 67.614 1.00 31.19 ? 123 GLU B CA 1 ATOM 3526 C C . GLU B 1 123 ? 7.339 39.752 68.182 1.00 32.32 ? 123 GLU B C 1 ATOM 3527 O O . GLU B 1 123 ? 8.115 40.711 68.191 1.00 30.80 ? 123 GLU B O 1 ATOM 3528 C CB . GLU B 1 123 ? 5.087 40.477 68.745 1.00 31.04 ? 123 GLU B CB 1 ATOM 3529 C CG . GLU B 1 123 ? 3.685 40.926 68.396 1.00 31.26 ? 123 GLU B CG 1 ATOM 3530 C CD . GLU B 1 123 ? 3.676 42.013 67.338 1.00 35.76 ? 123 GLU B CD 1 ATOM 3531 O OE1 . GLU B 1 123 ? 4.494 42.983 67.409 1.00 31.45 ? 123 GLU B OE1 1 ATOM 3532 O OE2 . GLU B 1 123 ? 2.849 41.867 66.419 1.00 39.54 ? 123 GLU B OE2 1 ATOM 3533 N N . PHE B 1 124 ? 7.633 38.559 68.685 1.00 27.67 ? 124 PHE B N 1 ATOM 3534 C CA . PHE B 1 124 ? 8.922 38.279 69.302 1.00 26.82 ? 124 PHE B CA 1 ATOM 3535 C C . PHE B 1 124 ? 9.868 37.716 68.232 1.00 26.41 ? 124 PHE B C 1 ATOM 3536 O O . PHE B 1 124 ? 9.423 37.245 67.182 1.00 26.29 ? 124 PHE B O 1 ATOM 3537 C CB . PHE B 1 124 ? 8.725 37.295 70.454 1.00 23.90 ? 124 PHE B CB 1 ATOM 3538 C CG . PHE B 1 124 ? 7.948 36.074 70.047 1.00 21.58 ? 124 PHE B CG 1 ATOM 3539 C CD1 . PHE B 1 124 ? 6.549 36.080 70.089 1.00 21.96 ? 124 PHE B CD1 1 ATOM 3540 C CD2 . PHE B 1 124 ? 8.613 34.941 69.573 1.00 21.89 ? 124 PHE B CD2 1 ATOM 3541 C CE1 . PHE B 1 124 ? 5.810 34.970 69.680 1.00 22.98 ? 124 PHE B CE1 1 ATOM 3542 C CE2 . PHE B 1 124 ? 7.884 33.816 69.155 1.00 22.88 ? 124 PHE B CE2 1 ATOM 3543 C CZ . PHE B 1 124 ? 6.480 33.832 69.213 1.00 23.08 ? 124 PHE B CZ 1 ATOM 3544 N N . ASP B 1 125 ? 11.168 37.801 68.513 1.00 27.38 ? 125 ASP B N 1 ATOM 3545 C CA . ASP B 1 125 ? 12.231 37.345 67.635 1.00 28.43 ? 125 ASP B CA 1 ATOM 3546 C C . ASP B 1 125 ? 12.685 35.916 67.886 1.00 28.08 ? 125 ASP B C 1 ATOM 3547 O O . ASP B 1 125 ? 13.303 35.315 66.999 1.00 31.10 ? 125 ASP B O 1 ATOM 3548 C CB . ASP B 1 125 ? 13.470 38.222 67.833 1.00 28.79 ? 125 ASP B CB 1 ATOM 3549 C CG . ASP B 1 125 ? 13.142 39.670 67.807 1.00 29.22 ? 125 ASP B CG 1 ATOM 3550 O OD1 . ASP B 1 125 ? 12.619 40.117 66.768 1.00 27.09 ? 125 ASP B OD1 1 ATOM 3551 O OD2 . ASP B 1 125 ? 13.351 40.433 68.778 1.00 29.87 ? 125 ASP B OD2 1 ATOM 3552 N N . GLY B 1 126 ? 12.420 35.381 69.080 1.00 26.57 ? 126 GLY B N 1 ATOM 3553 C CA . GLY B 1 126 ? 13.044 34.121 69.479 1.00 24.24 ? 126 GLY B CA 1 ATOM 3554 C C . GLY B 1 126 ? 12.364 33.374 70.610 1.00 24.35 ? 126 GLY B C 1 ATOM 3555 O O . GLY B 1 126 ? 11.295 33.766 71.067 1.00 22.63 ? 126 GLY B O 1 ATOM 3556 N N . VAL B 1 127 ? 12.996 32.287 71.055 1.00 21.52 ? 127 VAL B N 1 ATOM 3557 C CA . VAL B 1 127 ? 12.425 31.395 72.099 1.00 24.00 ? 127 VAL B CA 1 ATOM 3558 C C . VAL B 1 127 ? 13.510 31.007 73.112 1.00 24.67 ? 127 VAL B C 1 ATOM 3559 O O . VAL B 1 127 ? 14.668 30.692 72.723 1.00 24.15 ? 127 VAL B O 1 ATOM 3560 C CB . VAL B 1 127 ? 11.821 30.087 71.485 1.00 24.67 ? 127 VAL B CB 1 ATOM 3561 C CG1 . VAL B 1 127 ? 11.073 29.215 72.560 1.00 25.42 ? 127 VAL B CG1 1 ATOM 3562 C CG2 . VAL B 1 127 ? 10.901 30.391 70.373 1.00 26.22 ? 127 VAL B CG2 1 ATOM 3563 N N . VAL B 1 128 ? 13.152 31.086 74.399 1.00 23.03 ? 128 VAL B N 1 ATOM 3564 C CA . VAL B 1 128 ? 13.937 30.537 75.494 1.00 21.39 ? 128 VAL B CA 1 ATOM 3565 C C . VAL B 1 128 ? 13.255 29.264 75.996 1.00 24.25 ? 128 VAL B C 1 ATOM 3566 O O . VAL B 1 128 ? 12.183 29.317 76.601 1.00 23.62 ? 128 VAL B O 1 ATOM 3567 C CB . VAL B 1 128 ? 14.176 31.586 76.622 1.00 21.35 ? 128 VAL B CB 1 ATOM 3568 C CG1 . VAL B 1 128 ? 14.927 30.998 77.833 1.00 23.11 ? 128 VAL B CG1 1 ATOM 3569 C CG2 . VAL B 1 128 ? 14.991 32.747 76.054 1.00 20.92 ? 128 VAL B CG2 1 ATOM 3570 N N . GLY B 1 129 ? 13.877 28.116 75.731 1.00 22.62 ? 129 GLY B N 1 ATOM 3571 C CA . GLY B 1 129 ? 13.285 26.831 76.119 1.00 22.60 ? 129 GLY B CA 1 ATOM 3572 C C . GLY B 1 129 ? 13.525 26.611 77.584 1.00 22.05 ? 129 GLY B C 1 ATOM 3573 O O . GLY B 1 129 ? 14.670 26.675 78.039 1.00 25.58 ? 129 GLY B O 1 ATOM 3574 N N . MET B 1 130 ? 12.442 26.382 78.327 1.00 19.94 ? 130 MET B N 1 ATOM 3575 C CA . MET B 1 130 ? 12.488 26.213 79.768 1.00 22.45 ? 130 MET B CA 1 ATOM 3576 C C . MET B 1 130 ? 12.246 24.760 80.200 1.00 23.37 ? 130 MET B C 1 ATOM 3577 O O . MET B 1 130 ? 12.059 24.492 81.374 1.00 25.32 ? 130 MET B O 1 ATOM 3578 C CB . MET B 1 130 ? 11.484 27.170 80.468 1.00 24.37 ? 130 MET B CB 1 ATOM 3579 C CG . MET B 1 130 ? 11.760 28.694 80.232 1.00 23.86 ? 130 MET B CG 1 ATOM 3580 S SD . MET B 1 130 ? 13.275 29.346 80.999 1.00 33.12 ? 130 MET B SD 1 ATOM 3581 C CE . MET B 1 130 ? 12.796 29.485 82.727 1.00 30.90 ? 130 MET B CE 1 ATOM 3582 N N . GLY B 1 131 ? 12.248 23.826 79.255 1.00 26.05 ? 131 GLY B N 1 ATOM 3583 C CA . GLY B 1 131 ? 12.131 22.394 79.578 1.00 26.81 ? 131 GLY B CA 1 ATOM 3584 C C . GLY B 1 131 ? 13.396 21.717 80.106 1.00 27.02 ? 131 GLY B C 1 ATOM 3585 O O . GLY B 1 131 ? 14.328 22.378 80.558 1.00 26.78 ? 131 GLY B O 1 ATOM 3586 N N . PHE B 1 132 ? 13.418 20.381 80.067 1.00 30.74 ? 132 PHE B N 1 ATOM 3587 C CA . PHE B 1 132 ? 14.559 19.587 80.572 1.00 29.67 ? 132 PHE B CA 1 ATOM 3588 C C . PHE B 1 132 ? 15.560 19.237 79.473 1.00 31.49 ? 132 PHE B C 1 ATOM 3589 O O . PHE B 1 132 ? 15.243 19.341 78.280 1.00 30.70 ? 132 PHE B O 1 ATOM 3590 C CB . PHE B 1 132 ? 14.052 18.279 81.176 1.00 30.41 ? 132 PHE B CB 1 ATOM 3591 C CG . PHE B 1 132 ? 13.154 18.454 82.368 1.00 31.34 ? 132 PHE B CG 1 ATOM 3592 C CD1 . PHE B 1 132 ? 11.811 18.830 82.207 1.00 28.65 ? 132 PHE B CD1 1 ATOM 3593 C CD2 . PHE B 1 132 ? 13.637 18.200 83.657 1.00 31.95 ? 132 PHE B CD2 1 ATOM 3594 C CE1 . PHE B 1 132 ? 10.970 18.979 83.320 1.00 28.69 ? 132 PHE B CE1 1 ATOM 3595 C CE2 . PHE B 1 132 ? 12.804 18.342 84.776 1.00 30.99 ? 132 PHE B CE2 1 ATOM 3596 C CZ . PHE B 1 132 ? 11.468 18.736 84.605 1.00 29.94 ? 132 PHE B CZ 1 ATOM 3597 N N . ILE B 1 133 ? 16.748 18.772 79.867 1.00 33.43 ? 133 ILE B N 1 ATOM 3598 C CA . ILE B 1 133 ? 17.793 18.376 78.897 1.00 35.95 ? 133 ILE B CA 1 ATOM 3599 C C . ILE B 1 133 ? 17.352 17.188 78.020 1.00 37.93 ? 133 ILE B C 1 ATOM 3600 O O . ILE B 1 133 ? 17.731 17.098 76.852 1.00 38.03 ? 133 ILE B O 1 ATOM 3601 C CB . ILE B 1 133 ? 19.179 18.151 79.594 1.00 37.74 ? 133 ILE B CB 1 ATOM 3602 C CG1 . ILE B 1 133 ? 20.332 18.284 78.593 1.00 38.86 ? 133 ILE B CG1 1 ATOM 3603 C CG2 . ILE B 1 133 ? 19.268 16.786 80.282 1.00 38.80 ? 133 ILE B CG2 1 ATOM 3604 C CD1 . ILE B 1 133 ? 21.657 18.635 79.240 1.00 39.79 ? 133 ILE B CD1 1 ATOM 3605 N N . GLU B 1 134 ? 16.510 16.316 78.569 1.00 38.75 ? 134 GLU B N 1 ATOM 3606 C CA . GLU B 1 134 ? 15.956 15.158 77.840 1.00 41.13 ? 134 GLU B CA 1 ATOM 3607 C C . GLU B 1 134 ? 15.339 15.499 76.477 1.00 42.98 ? 134 GLU B C 1 ATOM 3608 O O . GLU B 1 134 ? 15.279 14.650 75.585 1.00 44.33 ? 134 GLU B O 1 ATOM 3609 C CB . GLU B 1 134 ? 14.916 14.422 78.707 1.00 42.68 ? 134 GLU B CB 1 ATOM 3610 C CG . GLU B 1 134 ? 15.492 13.507 79.787 1.00 46.66 ? 134 GLU B CG 1 ATOM 3611 C CD . GLU B 1 134 ? 15.743 14.184 81.137 1.00 48.27 ? 134 GLU B CD 1 ATOM 3612 O OE1 . GLU B 1 134 ? 15.633 15.418 81.266 1.00 49.38 ? 134 GLU B OE1 1 ATOM 3613 O OE2 . GLU B 1 134 ? 16.057 13.468 82.102 1.00 50.72 ? 134 GLU B OE2 1 ATOM 3614 N N . GLN B 1 135 ? 14.891 16.741 76.316 1.00 42.97 ? 135 GLN B N 1 ATOM 3615 C CA . GLN B 1 135 ? 14.235 17.179 75.091 1.00 43.51 ? 135 GLN B CA 1 ATOM 3616 C C . GLN B 1 135 ? 15.035 18.209 74.267 1.00 41.29 ? 135 GLN B C 1 ATOM 3617 O O . GLN B 1 135 ? 14.623 18.563 73.163 1.00 42.91 ? 135 GLN B O 1 ATOM 3618 C CB . GLN B 1 135 ? 12.844 17.725 75.415 1.00 44.79 ? 135 GLN B CB 1 ATOM 3619 C CG . GLN B 1 135 ? 11.800 16.651 75.652 1.00 47.30 ? 135 GLN B CG 1 ATOM 3620 C CD . GLN B 1 135 ? 10.368 17.176 75.572 1.00 49.92 ? 135 GLN B CD 1 ATOM 3621 O OE1 . GLN B 1 135 ? 9.448 16.430 75.205 1.00 52.08 ? 135 GLN B OE1 1 ATOM 3622 N NE2 . GLN B 1 135 ? 10.170 18.453 75.924 1.00 53.21 ? 135 GLN B NE2 1 ATOM 3623 N N . ALA B 1 136 ? 16.163 18.684 74.797 1.00 37.58 ? 136 ALA B N 1 ATOM 3624 C CA . ALA B 1 136 ? 17.006 19.647 74.087 1.00 37.03 ? 136 ALA B CA 1 ATOM 3625 C C . ALA B 1 136 ? 17.614 19.021 72.850 1.00 39.29 ? 136 ALA B C 1 ATOM 3626 O O . ALA B 1 136 ? 18.315 18.009 72.944 1.00 40.15 ? 136 ALA B O 1 ATOM 3627 C CB . ALA B 1 136 ? 18.119 20.174 74.993 1.00 33.41 ? 136 ALA B CB 1 ATOM 3628 N N . ILE B 1 137 ? 17.340 19.626 71.696 1.00 39.22 ? 137 ILE B N 1 ATOM 3629 C CA . ILE B 1 137 ? 17.965 19.232 70.441 1.00 38.04 ? 137 ILE B CA 1 ATOM 3630 C C . ILE B 1 137 ? 19.449 19.475 70.592 1.00 38.59 ? 137 ILE B C 1 ATOM 3631 O O . ILE B 1 137 ? 19.864 20.503 71.146 1.00 40.32 ? 137 ILE B O 1 ATOM 3632 C CB . ILE B 1 137 ? 17.400 20.070 69.277 1.00 36.81 ? 137 ILE B CB 1 ATOM 3633 C CG1 . ILE B 1 137 ? 15.909 19.808 69.126 1.00 36.37 ? 137 ILE B CG1 1 ATOM 3634 C CG2 . ILE B 1 137 ? 18.166 19.794 67.955 1.00 38.34 ? 137 ILE B CG2 1 ATOM 3635 C CD1 . ILE B 1 137 ? 15.163 20.923 68.462 1.00 37.76 ? 137 ILE B CD1 1 ATOM 3636 N N . GLY B 1 138 ? 20.250 18.515 70.137 1.00 39.82 ? 138 GLY B N 1 ATOM 3637 C CA . GLY B 1 138 ? 21.705 18.629 70.216 1.00 41.88 ? 138 GLY B CA 1 ATOM 3638 C C . GLY B 1 138 ? 22.254 18.334 71.600 1.00 43.29 ? 138 GLY B C 1 ATOM 3639 O O . GLY B 1 138 ? 23.457 18.471 71.838 1.00 42.43 ? 138 GLY B O 1 ATOM 3640 N N . ARG B 1 139 ? 21.372 17.956 72.525 1.00 45.29 ? 139 ARG B N 1 ATOM 3641 C CA . ARG B 1 139 ? 21.779 17.613 73.889 1.00 46.22 ? 139 ARG B CA 1 ATOM 3642 C C . ARG B 1 139 ? 22.455 18.777 74.620 1.00 44.49 ? 139 ARG B C 1 ATOM 3643 O O . ARG B 1 139 ? 23.258 18.574 75.528 1.00 43.89 ? 139 ARG B O 1 ATOM 3644 C CB . ARG B 1 139 ? 22.693 16.378 73.871 1.00 49.05 ? 139 ARG B CB 1 ATOM 3645 C CG . ARG B 1 139 ? 21.940 15.056 73.816 1.00 53.37 ? 139 ARG B CG 1 ATOM 3646 C CD . ARG B 1 139 ? 21.503 14.591 72.413 1.00 57.12 ? 139 ARG B CD 1 ATOM 3647 N NE . ARG B 1 139 ? 22.530 13.892 71.612 1.00 58.98 ? 139 ARG B NE 1 ATOM 3648 C CZ . ARG B 1 139 ? 23.741 13.494 72.024 1.00 59.35 ? 139 ARG B CZ 1 ATOM 3649 N NH1 . ARG B 1 139 ? 24.162 13.697 73.275 1.00 57.30 ? 139 ARG B NH1 1 ATOM 3650 N NH2 . ARG B 1 139 ? 24.540 12.883 71.158 1.00 58.89 ? 139 ARG B NH2 1 ATOM 3651 N N . VAL B 1 140 ? 22.133 19.997 74.212 1.00 41.93 ? 140 VAL B N 1 ATOM 3652 C CA . VAL B 1 140 ? 22.718 21.183 74.842 1.00 42.50 ? 140 VAL B CA 1 ATOM 3653 C C . VAL B 1 140 ? 22.046 21.561 76.164 1.00 40.27 ? 140 VAL B C 1 ATOM 3654 O O . VAL B 1 140 ? 20.815 21.512 76.294 1.00 38.57 ? 140 VAL B O 1 ATOM 3655 C CB . VAL B 1 140 ? 22.755 22.402 73.887 1.00 42.86 ? 140 VAL B CB 1 ATOM 3656 C CG1 . VAL B 1 140 ? 24.116 22.479 73.199 1.00 42.25 ? 140 VAL B CG1 1 ATOM 3657 C CG2 . VAL B 1 140 ? 21.668 22.294 72.866 1.00 42.46 ? 140 VAL B CG2 1 ATOM 3658 N N . THR B 1 141 ? 22.879 21.937 77.129 1.00 39.43 ? 141 THR B N 1 ATOM 3659 C CA . THR B 1 141 ? 22.443 22.316 78.459 1.00 39.26 ? 141 THR B CA 1 ATOM 3660 C C . THR B 1 141 ? 21.469 23.485 78.342 1.00 37.27 ? 141 THR B C 1 ATOM 3661 O O . THR B 1 141 ? 21.839 24.542 77.809 1.00 39.26 ? 141 THR B O 1 ATOM 3662 C CB . THR B 1 141 ? 23.670 22.737 79.325 1.00 41.23 ? 141 THR B CB 1 ATOM 3663 O OG1 . THR B 1 141 ? 24.643 21.687 79.338 1.00 41.25 ? 141 THR B OG1 1 ATOM 3664 C CG2 . THR B 1 141 ? 23.282 22.905 80.815 1.00 40.41 ? 141 THR B CG2 1 ATOM 3665 N N . PRO B 1 142 ? 20.241 23.309 78.836 1.00 32.55 ? 142 PRO B N 1 ATOM 3666 C CA . PRO B 1 142 ? 19.246 24.401 78.837 1.00 30.01 ? 142 PRO B CA 1 ATOM 3667 C C . PRO B 1 142 ? 19.623 25.564 79.756 1.00 30.20 ? 142 PRO B C 1 ATOM 3668 O O . PRO B 1 142 ? 20.363 25.390 80.740 1.00 28.30 ? 142 PRO B O 1 ATOM 3669 C CB . PRO B 1 142 ? 17.960 23.708 79.302 1.00 30.56 ? 142 PRO B CB 1 ATOM 3670 C CG . PRO B 1 142 ? 18.223 22.232 79.082 1.00 30.88 ? 142 PRO B CG 1 ATOM 3671 C CD . PRO B 1 142 ? 19.685 22.057 79.384 1.00 31.55 ? 142 PRO B CD 1 ATOM 3672 N N . ILE B 1 143 ? 19.144 26.756 79.428 1.00 28.48 ? 143 ILE B N 1 ATOM 3673 C CA . ILE B 1 143 ? 19.451 27.928 80.237 1.00 29.34 ? 143 ILE B CA 1 ATOM 3674 C C . ILE B 1 143 ? 19.161 27.811 81.748 1.00 31.01 ? 143 ILE B C 1 ATOM 3675 O O . ILE B 1 143 ? 19.971 28.264 82.559 1.00 31.89 ? 143 ILE B O 1 ATOM 3676 C CB . ILE B 1 143 ? 18.796 29.201 79.622 1.00 30.64 ? 143 ILE B CB 1 ATOM 3677 C CG1 . ILE B 1 143 ? 19.481 30.466 80.170 1.00 31.07 ? 143 ILE B CG1 1 ATOM 3678 C CG2 . ILE B 1 143 ? 17.265 29.202 79.859 1.00 29.70 ? 143 ILE B CG2 1 ATOM 3679 C CD1 . ILE B 1 143 ? 19.468 31.648 79.219 1.00 31.10 ? 143 ILE B CD1 1 ATOM 3680 N N . PHE B 1 144 ? 18.029 27.209 82.137 1.00 30.16 ? 144 PHE B N 1 ATOM 3681 C CA . PHE B 1 144 ? 17.695 27.135 83.552 1.00 30.27 ? 144 PHE B CA 1 ATOM 3682 C C . PHE B 1 144 ? 18.562 26.121 84.264 1.00 31.16 ? 144 PHE B C 1 ATOM 3683 O O . PHE B 1 144 ? 18.865 26.281 85.430 1.00 30.82 ? 144 PHE B O 1 ATOM 3684 C CB . PHE B 1 144 ? 16.217 26.837 83.828 1.00 26.71 ? 144 PHE B CB 1 ATOM 3685 C CG . PHE B 1 144 ? 15.811 27.151 85.241 1.00 28.50 ? 144 PHE B CG 1 ATOM 3686 C CD1 . PHE B 1 144 ? 15.833 28.468 85.712 1.00 25.75 ? 144 PHE B CD1 1 ATOM 3687 C CD2 . PHE B 1 144 ? 15.417 26.128 86.113 1.00 26.54 ? 144 PHE B CD2 1 ATOM 3688 C CE1 . PHE B 1 144 ? 15.468 28.756 87.042 1.00 25.40 ? 144 PHE B CE1 1 ATOM 3689 C CE2 . PHE B 1 144 ? 15.049 26.405 87.435 1.00 25.79 ? 144 PHE B CE2 1 ATOM 3690 C CZ . PHE B 1 144 ? 15.079 27.707 87.905 1.00 23.99 ? 144 PHE B CZ 1 ATOM 3691 N N . ASP B 1 145 ? 18.956 25.071 83.561 1.00 34.37 ? 145 ASP B N 1 ATOM 3692 C CA . ASP B 1 145 ? 19.990 24.187 84.081 1.00 37.31 ? 145 ASP B CA 1 ATOM 3693 C C . ASP B 1 145 ? 21.323 24.899 84.396 1.00 36.21 ? 145 ASP B C 1 ATOM 3694 O O . ASP B 1 145 ? 21.950 24.607 85.421 1.00 36.29 ? 145 ASP B O 1 ATOM 3695 C CB . ASP B 1 145 ? 20.219 23.026 83.120 1.00 40.47 ? 145 ASP B CB 1 ATOM 3696 C CG . ASP B 1 145 ? 19.296 21.869 83.389 1.00 44.96 ? 145 ASP B CG 1 ATOM 3697 O OD1 . ASP B 1 145 ? 18.061 22.045 83.270 1.00 46.82 ? 145 ASP B OD1 1 ATOM 3698 O OD2 . ASP B 1 145 ? 19.720 20.739 83.716 1.00 47.76 ? 145 ASP B OD2 1 ATOM 3699 N N . ASN B 1 146 ? 21.759 25.812 83.522 1.00 34.94 ? 146 ASN B N 1 ATOM 3700 C CA . ASN B 1 146 ? 23.000 26.586 83.742 1.00 32.28 ? 146 ASN B CA 1 ATOM 3701 C C . ASN B 1 146 ? 22.844 27.640 84.819 1.00 33.51 ? 146 ASN B C 1 ATOM 3702 O O . ASN B 1 146 ? 23.815 27.981 85.479 1.00 33.93 ? 146 ASN B O 1 ATOM 3703 C CB . ASN B 1 146 ? 23.496 27.283 82.454 1.00 35.23 ? 146 ASN B CB 1 ATOM 3704 C CG . ASN B 1 146 ? 24.156 26.322 81.452 1.00 34.09 ? 146 ASN B CG 1 ATOM 3705 O OD1 . ASN B 1 146 ? 24.985 25.492 81.817 1.00 35.70 ? 146 ASN B OD1 1 ATOM 3706 N ND2 . ASN B 1 146 ? 23.797 26.455 80.182 1.00 27.81 ? 146 ASN B ND2 1 ATOM 3707 N N . ILE B 1 147 ? 21.630 28.171 84.991 1.00 33.20 ? 147 ILE B N 1 ATOM 3708 C CA . ILE B 1 147 ? 21.346 29.158 86.063 1.00 31.54 ? 147 ILE B CA 1 ATOM 3709 C C . ILE B 1 147 ? 21.345 28.502 87.439 1.00 31.93 ? 147 ILE B C 1 ATOM 3710 O O . ILE B 1 147 ? 21.940 29.044 88.366 1.00 34.54 ? 147 ILE B O 1 ATOM 3711 C CB . ILE B 1 147 ? 20.033 29.957 85.803 1.00 29.89 ? 147 ILE B CB 1 ATOM 3712 C CG1 . ILE B 1 147 ? 20.227 30.946 84.648 1.00 29.84 ? 147 ILE B CG1 1 ATOM 3713 C CG2 . ILE B 1 147 ? 19.612 30.757 87.046 1.00 28.41 ? 147 ILE B CG2 1 ATOM 3714 C CD1 . ILE B 1 147 ? 18.916 31.503 84.075 1.00 31.27 ? 147 ILE B CD1 1 ATOM 3715 N N . ILE B 1 148 ? 20.703 27.335 87.548 1.00 32.10 ? 148 ILE B N 1 ATOM 3716 C CA . ILE B 1 148 ? 20.811 26.444 88.722 1.00 34.95 ? 148 ILE B CA 1 ATOM 3717 C C . ILE B 1 148 ? 22.256 26.180 89.197 1.00 36.37 ? 148 ILE B C 1 ATOM 3718 O O . ILE B 1 148 ? 22.536 26.267 90.400 1.00 35.98 ? 148 ILE B O 1 ATOM 3719 C CB . ILE B 1 148 ? 20.079 25.090 88.475 1.00 35.90 ? 148 ILE B CB 1 ATOM 3720 C CG1 . ILE B 1 148 ? 18.564 25.240 88.665 1.00 36.65 ? 148 ILE B CG1 1 ATOM 3721 C CG2 . ILE B 1 148 ? 20.601 24.014 89.436 1.00 38.05 ? 148 ILE B CG2 1 ATOM 3722 C CD1 . ILE B 1 148 ? 17.740 24.115 87.980 1.00 34.79 ? 148 ILE B CD1 1 ATOM 3723 N N . SER B 1 149 ? 23.164 25.873 88.263 1.00 38.08 ? 149 SER B N 1 ATOM 3724 C CA . SER B 1 149 ? 24.577 25.624 88.582 1.00 38.13 ? 149 SER B CA 1 ATOM 3725 C C . SER B 1 149 ? 25.288 26.814 89.226 1.00 38.97 ? 149 SER B C 1 ATOM 3726 O O . SER B 1 149 ? 26.193 26.625 90.032 1.00 39.88 ? 149 SER B O 1 ATOM 3727 C CB . SER B 1 149 ? 25.332 25.188 87.335 1.00 38.70 ? 149 SER B CB 1 ATOM 3728 O OG . SER B 1 149 ? 24.788 23.977 86.863 1.00 38.96 ? 149 SER B OG 1 ATOM 3729 N N . GLN B 1 150 ? 24.883 28.034 88.872 1.00 38.86 ? 150 GLN B N 1 ATOM 3730 C CA . GLN B 1 150 ? 25.452 29.233 89.488 1.00 38.24 ? 150 GLN B CA 1 ATOM 3731 C C . GLN B 1 150 ? 25.109 29.329 90.962 1.00 37.00 ? 150 GLN B C 1 ATOM 3732 O O . GLN B 1 150 ? 25.802 30.021 91.715 1.00 35.85 ? 150 GLN B O 1 ATOM 3733 C CB . GLN B 1 150 ? 24.938 30.489 88.802 1.00 40.61 ? 150 GLN B CB 1 ATOM 3734 C CG . GLN B 1 150 ? 25.779 30.969 87.658 1.00 41.71 ? 150 GLN B CG 1 ATOM 3735 C CD . GLN B 1 150 ? 25.120 32.103 86.915 1.00 41.12 ? 150 GLN B CD 1 ATOM 3736 O OE1 . GLN B 1 150 ? 24.872 31.992 85.722 1.00 44.34 ? 150 GLN B OE1 1 ATOM 3737 N NE2 . GLN B 1 150 ? 24.832 33.195 87.614 1.00 41.83 ? 150 GLN B NE2 1 ATOM 3738 N N . GLY B 1 151 ? 24.009 28.676 91.353 1.00 34.39 ? 151 GLY B N 1 ATOM 3739 C CA . GLY B 1 151 ? 23.591 28.599 92.746 1.00 35.44 ? 151 GLY B CA 1 ATOM 3740 C C . GLY B 1 151 ? 23.269 29.960 93.314 1.00 36.93 ? 151 GLY B C 1 ATOM 3741 O O . GLY B 1 151 ? 23.607 30.258 94.463 1.00 40.32 ? 151 GLY B O 1 ATOM 3742 N N . VAL B 1 152 ? 22.628 30.793 92.498 1.00 35.81 ? 152 VAL B N 1 ATOM 3743 C CA . VAL B 1 152 ? 22.260 32.145 92.893 1.00 34.39 ? 152 VAL B CA 1 ATOM 3744 C C . VAL B 1 152 ? 20.829 32.219 93.437 1.00 33.63 ? 152 VAL B C 1 ATOM 3745 O O . VAL B 1 152 ? 20.531 33.062 94.267 1.00 33.25 ? 152 VAL B O 1 ATOM 3746 C CB . VAL B 1 152 ? 22.392 33.149 91.723 1.00 35.52 ? 152 VAL B CB 1 ATOM 3747 C CG1 . VAL B 1 152 ? 23.819 33.704 91.634 1.00 36.37 ? 152 VAL B CG1 1 ATOM 3748 C CG2 . VAL B 1 152 ? 21.926 32.531 90.363 1.00 37.22 ? 152 VAL B CG2 1 ATOM 3749 N N . LEU B 1 153 ? 19.966 31.316 92.984 1.00 33.25 ? 153 LEU B N 1 ATOM 3750 C CA . LEU B 1 153 ? 18.520 31.459 93.183 1.00 35.32 ? 153 LEU B CA 1 ATOM 3751 C C . LEU B 1 153 ? 18.027 30.845 94.488 1.00 34.92 ? 153 LEU B C 1 ATOM 3752 O O . LEU B 1 153 ? 18.557 29.840 94.917 1.00 35.02 ? 153 LEU B O 1 ATOM 3753 C CB . LEU B 1 153 ? 17.760 30.869 91.985 1.00 34.97 ? 153 LEU B CB 1 ATOM 3754 C CG . LEU B 1 153 ? 18.023 31.480 90.608 1.00 34.96 ? 153 LEU B CG 1 ATOM 3755 C CD1 . LEU B 1 153 ? 17.132 30.825 89.573 1.00 33.34 ? 153 LEU B CD1 1 ATOM 3756 C CD2 . LEU B 1 153 ? 17.874 33.033 90.619 1.00 33.09 ? 153 LEU B CD2 1 ATOM 3757 N N . LYS B 1 154 ? 17.011 31.468 95.098 1.00 34.27 ? 154 LYS B N 1 ATOM 3758 C CA . LYS B 1 154 ? 16.454 31.045 96.379 1.00 33.46 ? 154 LYS B CA 1 ATOM 3759 C C . LYS B 1 154 ? 16.058 29.563 96.399 1.00 34.00 ? 154 LYS B C 1 ATOM 3760 O O . LYS B 1 154 ? 16.317 28.866 97.368 1.00 31.48 ? 154 LYS B O 1 ATOM 3761 C CB . LYS B 1 154 ? 15.252 31.921 96.743 1.00 35.13 ? 154 LYS B CB 1 ATOM 3762 C CG . LYS B 1 154 ? 14.538 31.544 98.047 1.00 35.45 ? 154 LYS B CG 1 ATOM 3763 C CD . LYS B 1 154 ? 13.320 32.445 98.372 1.00 36.80 ? 154 LYS B CD 1 ATOM 3764 C CE . LYS B 1 154 ? 12.262 32.512 97.258 1.00 40.22 ? 154 LYS B CE 1 ATOM 3765 N NZ . LYS B 1 154 ? 11.668 31.198 96.807 1.00 42.69 ? 154 LYS B NZ 1 ATOM 3766 N N . GLU B 1 155 ? 15.407 29.108 95.334 1.00 34.60 ? 155 GLU B N 1 ATOM 3767 C CA . GLU B 1 155 ? 15.088 27.695 95.140 1.00 37.36 ? 155 GLU B CA 1 ATOM 3768 C C . GLU B 1 155 ? 15.060 27.359 93.661 1.00 32.96 ? 155 GLU B C 1 ATOM 3769 O O . GLU B 1 155 ? 14.939 28.248 92.825 1.00 32.63 ? 155 GLU B O 1 ATOM 3770 C CB . GLU B 1 155 ? 13.774 27.297 95.839 1.00 37.89 ? 155 GLU B CB 1 ATOM 3771 C CG . GLU B 1 155 ? 12.701 28.361 95.815 1.00 41.39 ? 155 GLU B CG 1 ATOM 3772 C CD . GLU B 1 155 ? 11.354 27.862 96.305 1.00 45.27 ? 155 GLU B CD 1 ATOM 3773 O OE1 . GLU B 1 155 ? 11.251 26.653 96.654 1.00 49.18 ? 155 GLU B OE1 1 ATOM 3774 O OE2 . GLU B 1 155 ? 10.382 28.675 96.308 1.00 47.68 ? 155 GLU B OE2 1 ATOM 3775 N N . ASP B 1 156 ? 15.188 26.070 93.347 1.00 33.41 ? 156 ASP B N 1 ATOM 3776 C CA . ASP B 1 156 ? 15.206 25.571 91.967 1.00 30.56 ? 156 ASP B CA 1 ATOM 3777 C C . ASP B 1 156 ? 13.792 25.479 91.350 1.00 27.98 ? 156 ASP B C 1 ATOM 3778 O O . ASP B 1 156 ? 13.311 24.384 91.020 1.00 26.11 ? 156 ASP B O 1 ATOM 3779 C CB . ASP B 1 156 ? 15.895 24.207 91.914 1.00 33.40 ? 156 ASP B CB 1 ATOM 3780 C CG . ASP B 1 156 ? 17.387 24.280 92.225 1.00 39.71 ? 156 ASP B CG 1 ATOM 3781 O OD1 . ASP B 1 156 ? 17.981 25.392 92.133 1.00 39.31 ? 156 ASP B OD1 1 ATOM 3782 O OD2 . ASP B 1 156 ? 18.046 23.254 92.554 1.00 40.99 ? 156 ASP B OD2 1 ATOM 3783 N N . VAL B 1 157 ? 13.159 26.645 91.199 1.00 24.84 ? 157 VAL B N 1 ATOM 3784 C CA . VAL B 1 157 ? 11.820 26.819 90.615 1.00 23.35 ? 157 VAL B CA 1 ATOM 3785 C C . VAL B 1 157 ? 11.755 28.145 89.827 1.00 24.42 ? 157 VAL B C 1 ATOM 3786 O O . VAL B 1 157 ? 12.593 29.053 90.035 1.00 22.28 ? 157 VAL B O 1 ATOM 3787 C CB . VAL B 1 157 ? 10.674 26.830 91.676 1.00 24.61 ? 157 VAL B CB 1 ATOM 3788 C CG1 . VAL B 1 157 ? 10.877 25.765 92.785 1.00 20.24 ? 157 VAL B CG1 1 ATOM 3789 C CG2 . VAL B 1 157 ? 10.503 28.202 92.314 1.00 26.40 ? 157 VAL B CG2 1 ATOM 3790 N N . PHE B 1 158 ? 10.765 28.239 88.936 1.00 22.00 ? 158 PHE B N 1 ATOM 3791 C CA . PHE B 1 158 ? 10.428 29.471 88.226 1.00 20.70 ? 158 PHE B CA 1 ATOM 3792 C C . PHE B 1 158 ? 8.909 29.520 88.016 1.00 24.15 ? 158 PHE B C 1 ATOM 3793 O O . PHE B 1 158 ? 8.256 28.479 87.924 1.00 25.20 ? 158 PHE B O 1 ATOM 3794 C CB . PHE B 1 158 ? 11.202 29.620 86.892 1.00 20.16 ? 158 PHE B CB 1 ATOM 3795 C CG . PHE B 1 158 ? 10.993 28.480 85.911 1.00 20.25 ? 158 PHE B CG 1 ATOM 3796 C CD1 . PHE B 1 158 ? 9.863 28.423 85.103 1.00 20.56 ? 158 PHE B CD1 1 ATOM 3797 C CD2 . PHE B 1 158 ? 11.917 27.446 85.818 1.00 20.34 ? 158 PHE B CD2 1 ATOM 3798 C CE1 . PHE B 1 158 ? 9.669 27.361 84.226 1.00 18.69 ? 158 PHE B CE1 1 ATOM 3799 C CE2 . PHE B 1 158 ? 11.723 26.386 84.936 1.00 17.06 ? 158 PHE B CE2 1 ATOM 3800 C CZ . PHE B 1 158 ? 10.608 26.361 84.133 1.00 19.84 ? 158 PHE B CZ 1 ATOM 3801 N N . SER B 1 159 ? 8.332 30.717 87.963 1.00 22.92 ? 159 SER B N 1 ATOM 3802 C CA . SER B 1 159 ? 6.880 30.808 87.838 1.00 24.53 ? 159 SER B CA 1 ATOM 3803 C C . SER B 1 159 ? 6.432 31.773 86.771 1.00 24.93 ? 159 SER B C 1 ATOM 3804 O O . SER B 1 159 ? 7.187 32.661 86.381 1.00 21.80 ? 159 SER B O 1 ATOM 3805 C CB . SER B 1 159 ? 6.234 31.174 89.170 1.00 26.86 ? 159 SER B CB 1 ATOM 3806 O OG . SER B 1 159 ? 6.939 32.218 89.773 1.00 31.59 ? 159 SER B OG 1 ATOM 3807 N N . PHE B 1 160 ? 5.178 31.614 86.340 1.00 24.77 ? 160 PHE B N 1 ATOM 3808 C CA . PHE B 1 160 ? 4.618 32.399 85.247 1.00 23.88 ? 160 PHE B CA 1 ATOM 3809 C C . PHE B 1 160 ? 3.327 33.051 85.672 1.00 26.78 ? 160 PHE B C 1 ATOM 3810 O O . PHE B 1 160 ? 2.386 32.370 86.176 1.00 24.83 ? 160 PHE B O 1 ATOM 3811 C CB . PHE B 1 160 ? 4.331 31.516 84.023 1.00 20.61 ? 160 PHE B CB 1 ATOM 3812 C CG . PHE B 1 160 ? 5.564 31.216 83.166 1.00 21.93 ? 160 PHE B CG 1 ATOM 3813 C CD1 . PHE B 1 160 ? 6.554 30.336 83.622 1.00 20.93 ? 160 PHE B CD1 1 ATOM 3814 C CD2 . PHE B 1 160 ? 5.724 31.795 81.911 1.00 22.14 ? 160 PHE B CD2 1 ATOM 3815 C CE1 . PHE B 1 160 ? 7.702 30.031 82.834 1.00 21.54 ? 160 PHE B CE1 1 ATOM 3816 C CE2 . PHE B 1 160 ? 6.859 31.485 81.110 1.00 22.20 ? 160 PHE B CE2 1 ATOM 3817 C CZ . PHE B 1 160 ? 7.856 30.591 81.598 1.00 21.15 ? 160 PHE B CZ 1 ATOM 3818 N N . TYR B 1 161 ? 3.296 34.366 85.488 1.00 23.89 ? 161 TYR B N 1 ATOM 3819 C CA . TYR B 1 161 ? 2.073 35.142 85.602 1.00 23.90 ? 161 TYR B CA 1 ATOM 3820 C C . TYR B 1 161 ? 1.748 35.657 84.194 1.00 23.98 ? 161 TYR B C 1 ATOM 3821 O O . TYR B 1 161 ? 2.604 36.304 83.566 1.00 21.00 ? 161 TYR B O 1 ATOM 3822 C CB . TYR B 1 161 ? 2.244 36.329 86.586 1.00 23.97 ? 161 TYR B CB 1 ATOM 3823 C CG . TYR B 1 161 ? 1.114 37.336 86.448 1.00 25.54 ? 161 TYR B CG 1 ATOM 3824 C CD1 . TYR B 1 161 ? -0.207 36.971 86.775 1.00 24.50 ? 161 TYR B CD1 1 ATOM 3825 C CD2 . TYR B 1 161 ? 1.350 38.635 85.975 1.00 23.81 ? 161 TYR B CD2 1 ATOM 3826 C CE1 . TYR B 1 161 ? -1.229 37.852 86.657 1.00 24.13 ? 161 TYR B CE1 1 ATOM 3827 C CE2 . TYR B 1 161 ? 0.321 39.539 85.853 1.00 24.97 ? 161 TYR B CE2 1 ATOM 3828 C CZ . TYR B 1 161 ? -0.959 39.140 86.197 1.00 26.33 ? 161 TYR B CZ 1 ATOM 3829 O OH . TYR B 1 161 ? -2.007 39.989 86.071 1.00 27.78 ? 161 TYR B OH 1 ATOM 3830 N N . TYR B 1 162 ? 0.564 35.309 83.680 1.00 20.96 ? 162 TYR B N 1 ATOM 3831 C CA . TYR B 1 162 ? 0.041 35.859 82.432 1.00 24.63 ? 162 TYR B CA 1 ATOM 3832 C C . TYR B 1 162 ? -1.262 36.659 82.712 1.00 27.12 ? 162 TYR B C 1 ATOM 3833 O O . TYR B 1 162 ? -2.212 36.106 83.267 1.00 27.32 ? 162 TYR B O 1 ATOM 3834 C CB . TYR B 1 162 ? -0.287 34.740 81.415 1.00 21.30 ? 162 TYR B CB 1 ATOM 3835 C CG . TYR B 1 162 ? 0.847 34.095 80.638 1.00 21.29 ? 162 TYR B CG 1 ATOM 3836 C CD1 . TYR B 1 162 ? 2.170 34.550 80.722 1.00 22.97 ? 162 TYR B CD1 1 ATOM 3837 C CD2 . TYR B 1 162 ? 0.584 33.027 79.776 1.00 21.65 ? 162 TYR B CD2 1 ATOM 3838 C CE1 . TYR B 1 162 ? 3.191 33.919 79.986 1.00 22.82 ? 162 TYR B CE1 1 ATOM 3839 C CE2 . TYR B 1 162 ? 1.599 32.407 79.035 1.00 21.72 ? 162 TYR B CE2 1 ATOM 3840 C CZ . TYR B 1 162 ? 2.891 32.850 79.147 1.00 20.52 ? 162 TYR B CZ 1 ATOM 3841 O OH . TYR B 1 162 ? 3.879 32.222 78.417 1.00 20.51 ? 162 TYR B OH 1 ATOM 3842 N N . ASN B 1 163 ? -1.297 37.932 82.308 1.00 26.08 ? 163 ASN B N 1 ATOM 3843 C CA . ASN B 1 163 ? -2.481 38.819 82.479 1.00 26.50 ? 163 ASN B CA 1 ATOM 3844 C C . ASN B 1 163 ? -3.515 38.634 81.342 1.00 27.34 ? 163 ASN B C 1 ATOM 3845 O O . ASN B 1 163 ? -3.182 38.198 80.231 1.00 26.21 ? 163 ASN B O 1 ATOM 3846 C CB . ASN B 1 163 ? -2.002 40.285 82.543 1.00 24.86 ? 163 ASN B CB 1 ATOM 3847 C CG . ASN B 1 163 ? -2.970 41.265 83.305 1.00 28.16 ? 163 ASN B CG 1 ATOM 3848 O OD1 . ASN B 1 163 ? -2.604 42.429 83.522 1.00 31.47 ? 163 ASN B OD1 1 ATOM 3849 N ND2 . ASN B 1 163 ? -4.155 40.819 83.686 1.00 22.83 ? 163 ASN B ND2 1 ATOM 3850 N N . ARG B 1 164 ? -4.780 38.945 81.625 1.00 28.17 ? 164 ARG B N 1 ATOM 3851 C CA . ARG B 1 164 ? -5.756 39.158 80.565 1.00 32.81 ? 164 ARG B CA 1 ATOM 3852 C C . ARG B 1 164 ? -5.341 40.420 79.765 1.00 34.42 ? 164 ARG B C 1 ATOM 3853 O O . ARG B 1 164 ? -4.629 41.290 80.271 1.00 35.84 ? 164 ARG B O 1 ATOM 3854 C CB . ARG B 1 164 ? -7.190 39.274 81.150 1.00 32.45 ? 164 ARG B CB 1 ATOM 3855 C CG . ARG B 1 164 ? -7.566 38.119 82.096 1.00 33.89 ? 164 ARG B CG 1 ATOM 3856 C CD . ARG B 1 164 ? -8.909 38.264 82.835 1.00 37.51 ? 164 ARG B CD 1 ATOM 3857 N NE . ARG B 1 164 ? -9.988 38.604 81.894 1.00 46.68 ? 164 ARG B NE 1 ATOM 3858 C CZ . ARG B 1 164 ? -11.044 37.839 81.607 1.00 48.27 ? 164 ARG B CZ 1 ATOM 3859 N NH1 . ARG B 1 164 ? -11.225 36.666 82.206 1.00 49.02 ? 164 ARG B NH1 1 ATOM 3860 N NH2 . ARG B 1 164 ? -11.946 38.276 80.730 1.00 49.61 ? 164 ARG B NH2 1 ATOM 3861 N N . ASP B 1 165 ? -5.747 40.485 78.505 1.00 35.62 ? 165 ASP B N 1 ATOM 3862 C CA . ASP B 1 165 ? -5.410 41.598 77.639 1.00 38.17 ? 165 ASP B CA 1 ATOM 3863 C C . ASP B 1 165 ? -6.293 42.797 78.011 1.00 43.60 ? 165 ASP B C 1 ATOM 3864 O O . ASP B 1 165 ? -7.521 42.727 77.899 1.00 46.12 ? 165 ASP B O 1 ATOM 3865 C CB . ASP B 1 165 ? -5.622 41.180 76.181 1.00 35.34 ? 165 ASP B CB 1 ATOM 3866 C CG . ASP B 1 165 ? -5.009 42.147 75.182 1.00 34.79 ? 165 ASP B CG 1 ATOM 3867 O OD1 . ASP B 1 165 ? -4.129 42.982 75.557 1.00 32.87 ? 165 ASP B OD1 1 ATOM 3868 O OD2 . ASP B 1 165 ? -5.374 42.134 73.987 1.00 33.60 ? 165 ASP B OD2 1 ATOM 3869 N N . SER B 1 166 ? -5.665 43.869 78.500 1.00 46.49 ? 166 SER B N 1 ATOM 3870 C CA . SER B 1 166 ? -6.369 45.116 78.822 1.00 51.82 ? 166 SER B CA 1 ATOM 3871 C C . SER B 1 166 ? -5.544 46.342 78.420 1.00 52.34 ? 166 SER B C 1 ATOM 3872 O O . SER B 1 166 ? -4.507 46.628 79.025 1.00 52.74 ? 166 SER B O 1 ATOM 3873 C CB . SER B 1 166 ? -6.749 45.177 80.319 1.00 54.45 ? 166 SER B CB 1 ATOM 3874 O OG . SER B 1 166 ? -8.085 44.707 80.555 1.00 55.61 ? 166 SER B OG 1 ATOM 3875 N N . SER B 1 171 ? -1.070 48.396 82.274 1.00 44.43 ? 171 SER B N 1 ATOM 3876 C CA . SER B 1 171 ? -0.271 47.617 83.227 1.00 46.07 ? 171 SER B CA 1 ATOM 3877 C C . SER B 1 171 ? 0.325 46.307 82.647 1.00 42.75 ? 171 SER B C 1 ATOM 3878 O O . SER B 1 171 ? 0.231 46.036 81.447 1.00 42.61 ? 171 SER B O 1 ATOM 3879 C CB . SER B 1 171 ? -1.090 47.326 84.497 1.00 46.76 ? 171 SER B CB 1 ATOM 3880 O OG . SER B 1 171 ? -2.132 46.399 84.212 1.00 49.97 ? 171 SER B OG 1 ATOM 3881 N N . LEU B 1 172 ? 0.902 45.499 83.538 1.00 40.49 ? 172 LEU B N 1 ATOM 3882 C CA . LEU B 1 172 ? 1.775 44.373 83.197 1.00 37.28 ? 172 LEU B CA 1 ATOM 3883 C C . LEU B 1 172 ? 1.089 43.322 82.334 1.00 30.91 ? 172 LEU B C 1 ATOM 3884 O O . LEU B 1 172 ? 0.033 42.835 82.686 1.00 32.22 ? 172 LEU B O 1 ATOM 3885 C CB . LEU B 1 172 ? 2.266 43.730 84.502 1.00 38.49 ? 172 LEU B CB 1 ATOM 3886 C CG . LEU B 1 172 ? 3.760 43.521 84.708 1.00 40.69 ? 172 LEU B CG 1 ATOM 3887 C CD1 . LEU B 1 172 ? 4.475 44.886 84.821 1.00 42.22 ? 172 LEU B CD1 1 ATOM 3888 C CD2 . LEU B 1 172 ? 4.006 42.671 85.943 1.00 38.73 ? 172 LEU B CD2 1 ATOM 3889 N N . GLY B 1 173 ? 1.687 42.960 81.210 1.00 30.18 ? 173 GLY B N 1 ATOM 3890 C CA . GLY B 1 173 ? 1.143 41.859 80.402 1.00 25.57 ? 173 GLY B CA 1 ATOM 3891 C C . GLY B 1 173 ? 1.404 40.495 81.027 1.00 23.97 ? 173 GLY B C 1 ATOM 3892 O O . GLY B 1 173 ? 0.719 39.517 80.730 1.00 25.53 ? 173 GLY B O 1 ATOM 3893 N N . GLY B 1 174 ? 2.447 40.398 81.840 1.00 22.45 ? 174 GLY B N 1 ATOM 3894 C CA . GLY B 1 174 ? 2.754 39.129 82.485 1.00 20.20 ? 174 GLY B CA 1 ATOM 3895 C C . GLY B 1 174 ? 4.091 39.248 83.157 1.00 23.59 ? 174 GLY B C 1 ATOM 3896 O O . GLY B 1 174 ? 4.757 40.285 83.050 1.00 23.68 ? 174 GLY B O 1 ATOM 3897 N N . GLN B 1 175 ? 4.535 38.162 83.788 1.00 22.05 ? 175 GLN B N 1 ATOM 3898 C CA . GLN B 1 175 ? 5.810 38.181 84.467 1.00 22.24 ? 175 GLN B CA 1 ATOM 3899 C C . GLN B 1 175 ? 6.309 36.800 84.764 1.00 22.44 ? 175 GLN B C 1 ATOM 3900 O O . GLN B 1 175 ? 5.544 35.950 85.259 1.00 23.00 ? 175 GLN B O 1 ATOM 3901 C CB . GLN B 1 175 ? 5.692 38.952 85.785 1.00 24.00 ? 175 GLN B CB 1 ATOM 3902 C CG . GLN B 1 175 ? 7.009 39.249 86.518 1.00 24.87 ? 175 GLN B CG 1 ATOM 3903 C CD . GLN B 1 175 ? 6.759 39.578 87.987 1.00 26.49 ? 175 GLN B CD 1 ATOM 3904 O OE1 . GLN B 1 175 ? 6.171 38.765 88.734 1.00 26.07 ? 175 GLN B OE1 1 ATOM 3905 N NE2 . GLN B 1 175 ? 7.186 40.751 88.403 1.00 27.22 ? 175 GLN B NE2 1 ATOM 3906 N N A ILE B 1 176 ? 7.589 36.586 84.465 0.50 20.11 ? 176 ILE B N 1 ATOM 3907 N N B ILE B 1 176 ? 7.577 36.537 84.437 0.50 21.39 ? 176 ILE B N 1 ATOM 3908 C CA A ILE B 1 176 ? 8.313 35.411 84.962 0.50 21.40 ? 176 ILE B CA 1 ATOM 3909 C CA B ILE B 1 176 ? 8.252 35.304 84.916 0.50 23.12 ? 176 ILE B CA 1 ATOM 3910 C C A ILE B 1 176 ? 9.125 35.776 86.182 0.50 21.44 ? 176 ILE B C 1 ATOM 3911 C C B ILE B 1 176 ? 9.238 35.627 86.047 0.50 22.86 ? 176 ILE B C 1 ATOM 3912 O O A ILE B 1 176 ? 9.671 36.881 86.271 0.50 21.59 ? 176 ILE B O 1 ATOM 3913 O O B ILE B 1 176 ? 9.994 36.589 85.948 0.50 24.33 ? 176 ILE B O 1 ATOM 3914 C CB A ILE B 1 176 ? 9.233 34.839 83.883 0.50 17.59 ? 176 ILE B CB 1 ATOM 3915 C CB B ILE B 1 176 ? 8.920 34.487 83.745 0.50 21.37 ? 176 ILE B CB 1 ATOM 3916 C CG1 A ILE B 1 176 ? 8.377 34.174 82.823 0.50 18.13 ? 176 ILE B CG1 1 ATOM 3917 C CG1 B ILE B 1 176 ? 9.803 33.337 84.265 0.50 21.97 ? 176 ILE B CG1 1 ATOM 3918 C CG2 A ILE B 1 176 ? 10.217 33.829 84.467 0.50 16.32 ? 176 ILE B CG2 1 ATOM 3919 C CG2 B ILE B 1 176 ? 9.718 35.382 82.807 0.50 22.44 ? 176 ILE B CG2 1 ATOM 3920 C CD1 A ILE B 1 176 ? 8.905 34.377 81.460 0.50 16.24 ? 176 ILE B CD1 1 ATOM 3921 C CD1 B ILE B 1 176 ? 10.426 32.472 83.138 0.50 21.18 ? 176 ILE B CD1 1 ATOM 3922 N N . VAL B 1 177 ? 9.182 34.843 87.127 1.00 22.34 ? 177 VAL B N 1 ATOM 3923 C CA . VAL B 1 177 ? 10.092 34.971 88.283 1.00 22.73 ? 177 VAL B CA 1 ATOM 3924 C C . VAL B 1 177 ? 11.006 33.740 88.285 1.00 22.76 ? 177 VAL B C 1 ATOM 3925 O O . VAL B 1 177 ? 10.534 32.611 88.140 1.00 21.73 ? 177 VAL B O 1 ATOM 3926 C CB . VAL B 1 177 ? 9.323 35.095 89.617 1.00 21.68 ? 177 VAL B CB 1 ATOM 3927 C CG1 . VAL B 1 177 ? 10.267 35.062 90.836 1.00 20.65 ? 177 VAL B CG1 1 ATOM 3928 C CG2 . VAL B 1 177 ? 8.464 36.380 89.636 1.00 24.88 ? 177 VAL B CG2 1 ATOM 3929 N N . LEU B 1 178 ? 12.304 33.971 88.412 1.00 23.99 ? 178 LEU B N 1 ATOM 3930 C CA . LEU B 1 178 ? 13.281 32.878 88.484 1.00 23.65 ? 178 LEU B CA 1 ATOM 3931 C C . LEU B 1 178 ? 13.684 32.789 89.931 1.00 22.89 ? 178 LEU B C 1 ATOM 3932 O O . LEU B 1 178 ? 14.021 33.801 90.562 1.00 21.71 ? 178 LEU B O 1 ATOM 3933 C CB . LEU B 1 178 ? 14.513 33.181 87.613 1.00 24.32 ? 178 LEU B CB 1 ATOM 3934 C CG . LEU B 1 178 ? 14.305 33.672 86.185 1.00 28.36 ? 178 LEU B CG 1 ATOM 3935 C CD1 . LEU B 1 178 ? 15.653 34.123 85.587 1.00 29.91 ? 178 LEU B CD1 1 ATOM 3936 C CD2 . LEU B 1 178 ? 13.599 32.607 85.300 1.00 28.12 ? 178 LEU B CD2 1 ATOM 3937 N N . GLY B 1 179 ? 13.596 31.591 90.494 1.00 22.92 ? 179 GLY B N 1 ATOM 3938 C CA . GLY B 1 179 ? 13.895 31.425 91.886 1.00 22.02 ? 179 GLY B CA 1 ATOM 3939 C C . GLY B 1 179 ? 12.714 31.428 92.846 1.00 25.29 ? 179 GLY B C 1 ATOM 3940 O O . GLY B 1 179 ? 12.923 31.266 94.021 1.00 24.40 ? 179 GLY B O 1 ATOM 3941 N N . GLY B 1 180 ? 11.478 31.576 92.364 1.00 24.62 ? 180 GLY B N 1 ATOM 3942 C CA . GLY B 1 180 ? 10.345 31.700 93.282 1.00 24.30 ? 180 GLY B CA 1 ATOM 3943 C C . GLY B 1 180 ? 9.031 32.075 92.617 1.00 26.12 ? 180 GLY B C 1 ATOM 3944 O O . GLY B 1 180 ? 8.838 31.826 91.432 1.00 25.57 ? 180 GLY B O 1 ATOM 3945 N N . SER B 1 181 ? 8.124 32.642 93.414 1.00 27.11 ? 181 SER B N 1 ATOM 3946 C CA . SER B 1 181 ? 6.837 33.167 92.978 1.00 27.67 ? 181 SER B CA 1 ATOM 3947 C C . SER B 1 181 ? 6.581 34.550 93.575 1.00 27.92 ? 181 SER B C 1 ATOM 3948 O O . SER B 1 181 ? 7.044 34.846 94.657 1.00 28.55 ? 181 SER B O 1 ATOM 3949 C CB . SER B 1 181 ? 5.728 32.220 93.421 1.00 30.78 ? 181 SER B CB 1 ATOM 3950 O OG . SER B 1 181 ? 5.734 31.055 92.592 1.00 34.64 ? 181 SER B OG 1 ATOM 3951 N N . ASP B 1 182 ? 5.824 35.384 92.876 1.00 28.39 ? 182 ASP B N 1 ATOM 3952 C CA . ASP B 1 182 ? 5.501 36.733 93.352 1.00 28.17 ? 182 ASP B CA 1 ATOM 3953 C C . ASP B 1 182 ? 4.061 36.790 93.881 1.00 25.74 ? 182 ASP B C 1 ATOM 3954 O O . ASP B 1 182 ? 3.115 36.723 93.076 1.00 25.36 ? 182 ASP B O 1 ATOM 3955 C CB . ASP B 1 182 ? 5.654 37.682 92.181 1.00 29.60 ? 182 ASP B CB 1 ATOM 3956 C CG . ASP B 1 182 ? 5.408 39.133 92.540 1.00 30.44 ? 182 ASP B CG 1 ATOM 3957 O OD1 . ASP B 1 182 ? 5.106 39.476 93.694 1.00 31.79 ? 182 ASP B OD1 1 ATOM 3958 O OD2 . ASP B 1 182 ? 5.472 40.016 91.675 1.00 33.12 ? 182 ASP B OD2 1 ATOM 3959 N N . PRO B 1 183 ? 3.869 36.909 95.205 1.00 27.76 ? 183 PRO B N 1 ATOM 3960 C CA . PRO B 1 183 ? 2.501 36.899 95.760 1.00 28.68 ? 183 PRO B CA 1 ATOM 3961 C C . PRO B 1 183 ? 1.633 38.105 95.389 1.00 30.45 ? 183 PRO B C 1 ATOM 3962 O O . PRO B 1 183 ? 0.442 38.101 95.677 1.00 32.35 ? 183 PRO B O 1 ATOM 3963 C CB . PRO B 1 183 ? 2.711 36.758 97.269 1.00 28.73 ? 183 PRO B CB 1 ATOM 3964 C CG . PRO B 1 183 ? 4.099 37.296 97.525 1.00 28.10 ? 183 PRO B CG 1 ATOM 3965 C CD . PRO B 1 183 ? 4.894 37.009 96.271 1.00 28.07 ? 183 PRO B CD 1 ATOM 3966 N N . GLN B 1 184 ? 2.201 39.100 94.705 1.00 30.87 ? 184 GLN B N 1 ATOM 3967 C CA . GLN B 1 184 ? 1.389 40.202 94.135 1.00 31.00 ? 184 GLN B CA 1 ATOM 3968 C C . GLN B 1 184 ? 0.452 39.700 93.058 1.00 27.92 ? 184 GLN B C 1 ATOM 3969 O O . GLN B 1 184 ? -0.590 40.295 92.802 1.00 29.06 ? 184 GLN B O 1 ATOM 3970 C CB . GLN B 1 184 ? 2.281 41.291 93.548 1.00 34.63 ? 184 GLN B CB 1 ATOM 3971 C CG . GLN B 1 184 ? 2.946 42.151 94.592 1.00 40.80 ? 184 GLN B CG 1 ATOM 3972 C CD . GLN B 1 184 ? 1.925 42.941 95.391 1.00 45.54 ? 184 GLN B CD 1 ATOM 3973 O OE1 . GLN B 1 184 ? 1.050 43.610 94.820 1.00 46.92 ? 184 GLN B OE1 1 ATOM 3974 N NE2 . GLN B 1 184 ? 2.021 42.856 96.717 1.00 47.89 ? 184 GLN B NE2 1 ATOM 3975 N N . HIS B 1 185 ? 0.801 38.567 92.447 1.00 26.30 ? 185 HIS B N 1 ATOM 3976 C CA . HIS B 1 185 ? 0.128 38.127 91.245 1.00 25.39 ? 185 HIS B CA 1 ATOM 3977 C C . HIS B 1 185 ? -0.664 36.836 91.398 1.00 28.19 ? 185 HIS B C 1 ATOM 3978 O O . HIS B 1 185 ? -1.287 36.350 90.435 1.00 24.74 ? 185 HIS B O 1 ATOM 3979 C CB . HIS B 1 185 ? 1.116 38.113 90.076 1.00 25.79 ? 185 HIS B CB 1 ATOM 3980 C CG . HIS B 1 185 ? 1.601 39.490 89.714 1.00 28.07 ? 185 HIS B CG 1 ATOM 3981 N ND1 . HIS B 1 185 ? 2.937 39.826 89.644 1.00 31.63 ? 185 HIS B ND1 1 ATOM 3982 C CD2 . HIS B 1 185 ? 0.914 40.625 89.441 1.00 28.94 ? 185 HIS B CD2 1 ATOM 3983 C CE1 . HIS B 1 185 ? 3.054 41.107 89.336 1.00 30.32 ? 185 HIS B CE1 1 ATOM 3984 N NE2 . HIS B 1 185 ? 1.841 41.616 89.209 1.00 32.57 ? 185 HIS B NE2 1 ATOM 3985 N N . TYR B 1 186 ? -0.673 36.295 92.614 1.00 25.62 ? 186 TYR B N 1 ATOM 3986 C CA . TYR B 1 186 ? -1.604 35.216 92.911 1.00 28.69 ? 186 TYR B CA 1 ATOM 3987 C C . TYR B 1 186 ? -2.349 35.431 94.261 1.00 27.38 ? 186 TYR B C 1 ATOM 3988 O O . TYR B 1 186 ? -2.009 36.295 95.063 1.00 28.73 ? 186 TYR B O 1 ATOM 3989 C CB . TYR B 1 186 ? -0.931 33.819 92.761 1.00 27.80 ? 186 TYR B CB 1 ATOM 3990 C CG . TYR B 1 186 ? 0.111 33.561 93.817 1.00 28.34 ? 186 TYR B CG 1 ATOM 3991 C CD1 . TYR B 1 186 ? 1.454 33.937 93.636 1.00 27.24 ? 186 TYR B CD1 1 ATOM 3992 C CD2 . TYR B 1 186 ? -0.249 32.946 95.018 1.00 27.36 ? 186 TYR B CD2 1 ATOM 3993 C CE1 . TYR B 1 186 ? 2.406 33.688 94.659 1.00 29.71 ? 186 TYR B CE1 1 ATOM 3994 C CE2 . TYR B 1 186 ? 0.670 32.707 96.019 1.00 25.87 ? 186 TYR B CE2 1 ATOM 3995 C CZ . TYR B 1 186 ? 1.984 33.083 95.853 1.00 28.51 ? 186 TYR B CZ 1 ATOM 3996 O OH . TYR B 1 186 ? 2.851 32.831 96.903 1.00 27.19 ? 186 TYR B OH 1 ATOM 3997 N N . GLU B 1 187 ? -3.385 34.648 94.481 1.00 27.62 ? 187 GLU B N 1 ATOM 3998 C CA . GLU B 1 187 ? -4.107 34.692 95.729 1.00 30.19 ? 187 GLU B CA 1 ATOM 3999 C C . GLU B 1 187 ? -4.269 33.261 96.262 1.00 30.39 ? 187 GLU B C 1 ATOM 4000 O O . GLU B 1 187 ? -4.159 32.279 95.505 1.00 30.17 ? 187 GLU B O 1 ATOM 4001 C CB . GLU B 1 187 ? -5.444 35.392 95.525 1.00 30.66 ? 187 GLU B CB 1 ATOM 4002 C CG . GLU B 1 187 ? -6.482 34.558 94.792 1.00 33.98 ? 187 GLU B CG 1 ATOM 4003 C CD . GLU B 1 187 ? -7.837 35.236 94.796 1.00 41.93 ? 187 GLU B CD 1 ATOM 4004 O OE1 . GLU B 1 187 ? -8.730 34.790 95.571 1.00 44.53 ? 187 GLU B OE1 1 ATOM 4005 O OE2 . GLU B 1 187 ? -7.986 36.240 94.062 1.00 42.84 ? 187 GLU B OE2 1 ATOM 4006 N N . GLY B 1 188 ? -4.494 33.140 97.565 1.00 31.04 ? 188 GLY B N 1 ATOM 4007 C CA . GLY B 1 188 ? -4.564 31.818 98.208 1.00 31.44 ? 188 GLY B CA 1 ATOM 4008 C C . GLY B 1 188 ? -3.211 31.112 98.186 1.00 30.98 ? 188 GLY B C 1 ATOM 4009 O O . GLY B 1 188 ? -2.165 31.769 98.197 1.00 29.71 ? 188 GLY B O 1 ATOM 4010 N N . ASN B 1 189 ? -3.242 29.777 98.127 1.00 28.89 ? 189 ASN B N 1 ATOM 4011 C CA . ASN B 1 189 ? -2.043 28.949 98.264 1.00 28.73 ? 189 ASN B CA 1 ATOM 4012 C C . ASN B 1 189 ? -1.848 28.002 97.084 1.00 26.49 ? 189 ASN B C 1 ATOM 4013 O O . ASN B 1 189 ? -2.802 27.609 96.445 1.00 26.27 ? 189 ASN B O 1 ATOM 4014 C CB . ASN B 1 189 ? -2.142 28.116 99.558 1.00 29.27 ? 189 ASN B CB 1 ATOM 4015 C CG . ASN B 1 189 ? -2.424 28.971 100.791 1.00 33.49 ? 189 ASN B CG 1 ATOM 4016 O OD1 . ASN B 1 189 ? -1.580 29.754 101.222 1.00 27.27 ? 189 ASN B OD1 1 ATOM 4017 N ND2 . ASN B 1 189 ? -3.624 28.810 101.370 1.00 33.81 ? 189 ASN B ND2 1 ATOM 4018 N N . PHE B 1 190 ? -0.605 27.632 96.793 1.00 27.30 ? 190 PHE B N 1 ATOM 4019 C CA . PHE B 1 190 ? -0.347 26.627 95.763 1.00 24.62 ? 190 PHE B CA 1 ATOM 4020 C C . PHE B 1 190 ? -0.785 25.235 96.125 1.00 25.91 ? 190 PHE B C 1 ATOM 4021 O O . PHE B 1 190 ? -0.646 24.825 97.275 1.00 24.64 ? 190 PHE B O 1 ATOM 4022 C CB . PHE B 1 190 ? 1.127 26.541 95.435 1.00 25.47 ? 190 PHE B CB 1 ATOM 4023 C CG . PHE B 1 190 ? 1.642 27.738 94.702 1.00 26.39 ? 190 PHE B CG 1 ATOM 4024 C CD1 . PHE B 1 190 ? 1.376 27.898 93.357 1.00 23.65 ? 190 PHE B CD1 1 ATOM 4025 C CD2 . PHE B 1 190 ? 2.392 28.694 95.358 1.00 26.51 ? 190 PHE B CD2 1 ATOM 4026 C CE1 . PHE B 1 190 ? 1.839 29.011 92.665 1.00 25.44 ? 190 PHE B CE1 1 ATOM 4027 C CE2 . PHE B 1 190 ? 2.849 29.809 94.667 1.00 27.88 ? 190 PHE B CE2 1 ATOM 4028 C CZ . PHE B 1 190 ? 2.566 29.955 93.324 1.00 24.98 ? 190 PHE B CZ 1 ATOM 4029 N N A HIS B 1 191 ? -1.355 24.535 95.142 0.50 26.62 ? 191 HIS B N 1 ATOM 4030 N N B HIS B 1 191 ? -1.278 24.519 95.116 0.50 26.97 ? 191 HIS B N 1 ATOM 4031 C CA A HIS B 1 191 ? -1.480 23.072 95.156 0.50 25.04 ? 191 HIS B CA 1 ATOM 4032 C CA B HIS B 1 191 ? -1.486 23.074 95.168 0.50 25.54 ? 191 HIS B CA 1 ATOM 4033 C C A HIS B 1 191 ? -0.572 22.528 94.072 0.50 25.07 ? 191 HIS B C 1 ATOM 4034 C C B HIS B 1 191 ? -0.682 22.445 94.035 0.50 25.45 ? 191 HIS B C 1 ATOM 4035 O O A HIS B 1 191 ? -0.488 23.113 92.985 0.50 26.00 ? 191 HIS B O 1 ATOM 4036 O O B HIS B 1 191 ? -0.752 22.910 92.889 0.50 27.00 ? 191 HIS B O 1 ATOM 4037 C CB A HIS B 1 191 ? -2.928 22.623 94.900 0.50 26.03 ? 191 HIS B CB 1 ATOM 4038 C CB B HIS B 1 191 ? -2.985 22.751 95.071 0.50 26.81 ? 191 HIS B CB 1 ATOM 4039 C CG A HIS B 1 191 ? -3.081 21.136 94.744 0.50 25.10 ? 191 HIS B CG 1 ATOM 4040 C CG B HIS B 1 191 ? -3.788 23.338 96.190 0.50 25.76 ? 191 HIS B CG 1 ATOM 4041 N ND1 A HIS B 1 191 ? -2.888 20.254 95.782 0.50 24.68 ? 191 HIS B ND1 1 ATOM 4042 N ND1 B HIS B 1 191 ? -4.391 24.575 96.106 0.50 26.27 ? 191 HIS B ND1 1 ATOM 4043 C CD2 A HIS B 1 191 ? -3.410 20.382 93.666 0.50 24.12 ? 191 HIS B CD2 1 ATOM 4044 C CD2 B HIS B 1 191 ? -4.055 22.877 97.434 0.50 26.88 ? 191 HIS B CD2 1 ATOM 4045 C CE1 A HIS B 1 191 ? -3.094 19.021 95.352 0.50 23.73 ? 191 HIS B CE1 1 ATOM 4046 C CE1 B HIS B 1 191 ? -5.003 24.846 97.245 0.50 24.43 ? 191 HIS B CE1 1 ATOM 4047 N NE2 A HIS B 1 191 ? -3.406 19.073 94.073 0.50 19.39 ? 191 HIS B NE2 1 ATOM 4048 N NE2 B HIS B 1 191 ? -4.820 23.829 98.066 0.50 24.46 ? 191 HIS B NE2 1 ATOM 4049 N N . TYR B 1 192 ? 0.101 21.414 94.370 1.00 22.82 ? 192 TYR B N 1 ATOM 4050 C CA . TYR B 1 192 ? 1.100 20.836 93.488 1.00 25.67 ? 192 TYR B CA 1 ATOM 4051 C C . TYR B 1 192 ? 0.675 19.486 92.924 1.00 25.82 ? 192 TYR B C 1 ATOM 4052 O O . TYR B 1 192 ? -0.028 18.727 93.590 1.00 25.48 ? 192 TYR B O 1 ATOM 4053 C CB . TYR B 1 192 ? 2.470 20.720 94.198 1.00 25.11 ? 192 TYR B CB 1 ATOM 4054 C CG . TYR B 1 192 ? 3.055 22.059 94.612 1.00 24.12 ? 192 TYR B CG 1 ATOM 4055 C CD1 . TYR B 1 192 ? 3.893 22.778 93.747 1.00 26.18 ? 192 TYR B CD1 1 ATOM 4056 C CD2 . TYR B 1 192 ? 2.745 22.620 95.847 1.00 25.64 ? 192 TYR B CD2 1 ATOM 4057 C CE1 . TYR B 1 192 ? 4.417 24.025 94.118 1.00 22.75 ? 192 TYR B CE1 1 ATOM 4058 C CE2 . TYR B 1 192 ? 3.283 23.841 96.248 1.00 24.37 ? 192 TYR B CE2 1 ATOM 4059 C CZ . TYR B 1 192 ? 4.100 24.543 95.367 1.00 24.56 ? 192 TYR B CZ 1 ATOM 4060 O OH . TYR B 1 192 ? 4.601 25.751 95.749 1.00 26.17 ? 192 TYR B OH 1 ATOM 4061 N N . ILE B 1 193 ? 1.087 19.218 91.685 1.00 26.22 ? 193 ILE B N 1 ATOM 4062 C CA . ILE B 1 193 ? 0.872 17.895 91.045 1.00 25.86 ? 193 ILE B CA 1 ATOM 4063 C C . ILE B 1 193 ? 2.244 17.379 90.609 1.00 26.63 ? 193 ILE B C 1 ATOM 4064 O O . ILE B 1 193 ? 3.011 18.104 89.973 1.00 27.12 ? 193 ILE B O 1 ATOM 4065 C CB . ILE B 1 193 ? -0.135 17.998 89.827 1.00 27.64 ? 193 ILE B CB 1 ATOM 4066 C CG1 . ILE B 1 193 ? -1.432 18.741 90.221 1.00 27.83 ? 193 ILE B CG1 1 ATOM 4067 C CG2 . ILE B 1 193 ? -0.456 16.607 89.218 1.00 27.28 ? 193 ILE B CG2 1 ATOM 4068 C CD1 . ILE B 1 193 ? -1.413 20.251 89.932 1.00 29.38 ? 193 ILE B CD1 1 ATOM 4069 N N . ASN B 1 194 ? 2.554 16.129 90.955 1.00 25.48 ? 194 ASN B N 1 ATOM 4070 C CA . ASN B 1 194 ? 3.810 15.516 90.542 1.00 27.94 ? 194 ASN B CA 1 ATOM 4071 C C . ASN B 1 194 ? 3.875 15.248 89.048 1.00 28.67 ? 194 ASN B C 1 ATOM 4072 O O . ASN B 1 194 ? 2.859 14.931 88.419 1.00 31.28 ? 194 ASN B O 1 ATOM 4073 C CB . ASN B 1 194 ? 4.074 14.215 91.321 1.00 28.66 ? 194 ASN B CB 1 ATOM 4074 C CG . ASN B 1 194 ? 4.375 14.449 92.785 1.00 30.47 ? 194 ASN B CG 1 ATOM 4075 O OD1 . ASN B 1 194 ? 4.056 13.601 93.616 1.00 33.78 ? 194 ASN B OD1 1 ATOM 4076 N ND2 . ASN B 1 194 ? 5.025 15.570 93.116 1.00 32.65 ? 194 ASN B ND2 1 ATOM 4077 N N . LEU B 1 195 ? 5.072 15.380 88.474 1.00 30.75 ? 195 LEU B N 1 ATOM 4078 C CA . LEU B 1 195 ? 5.271 15.047 87.069 1.00 30.43 ? 195 LEU B CA 1 ATOM 4079 C C . LEU B 1 195 ? 5.101 13.540 86.928 1.00 31.89 ? 195 LEU B C 1 ATOM 4080 O O . LEU B 1 195 ? 5.402 12.799 87.871 1.00 30.22 ? 195 LEU B O 1 ATOM 4081 C CB . LEU B 1 195 ? 6.669 15.469 86.584 1.00 28.82 ? 195 LEU B CB 1 ATOM 4082 C CG . LEU B 1 195 ? 6.992 16.972 86.498 1.00 28.24 ? 195 LEU B CG 1 ATOM 4083 C CD1 . LEU B 1 195 ? 8.449 17.256 86.067 1.00 27.33 ? 195 LEU B CD1 1 ATOM 4084 C CD2 . LEU B 1 195 ? 6.018 17.688 85.612 1.00 28.00 ? 195 LEU B CD2 1 ATOM 4085 N N . ILE B 1 196 ? 4.605 13.095 85.778 1.00 33.96 ? 196 ILE B N 1 ATOM 4086 C CA . ILE B 1 196 ? 4.549 11.654 85.462 1.00 39.48 ? 196 ILE B CA 1 ATOM 4087 C C . ILE B 1 196 ? 5.974 11.113 85.520 1.00 42.99 ? 196 ILE B C 1 ATOM 4088 O O . ILE B 1 196 ? 6.285 10.186 86.300 1.00 44.95 ? 196 ILE B O 1 ATOM 4089 C CB . ILE B 1 196 ? 3.981 11.415 84.043 1.00 41.09 ? 196 ILE B CB 1 ATOM 4090 C CG1 . ILE B 1 196 ? 2.538 11.915 83.918 1.00 39.66 ? 196 ILE B CG1 1 ATOM 4091 C CG2 . ILE B 1 196 ? 4.135 9.934 83.637 1.00 42.32 ? 196 ILE B CG2 1 ATOM 4092 C CD1 . ILE B 1 196 ? 1.632 11.343 84.951 1.00 41.46 ? 196 ILE B CD1 1 ATOM 4093 N N . LYS B 1 197 ? 6.837 11.724 84.706 1.00 43.05 ? 197 LYS B N 1 ATOM 4094 C CA . LYS B 1 197 ? 8.267 11.434 84.697 1.00 46.05 ? 197 LYS B CA 1 ATOM 4095 C C . LYS B 1 197 ? 9.076 12.715 84.478 1.00 45.92 ? 197 LYS B C 1 ATOM 4096 O O . LYS B 1 197 ? 8.578 13.680 83.885 1.00 45.83 ? 197 LYS B O 1 ATOM 4097 C CB . LYS B 1 197 ? 8.578 10.405 83.607 1.00 46.03 ? 197 LYS B CB 1 ATOM 4098 C CG . LYS B 1 197 ? 8.170 10.848 82.218 1.00 47.93 ? 197 LYS B CG 1 ATOM 4099 C CD . LYS B 1 197 ? 7.687 9.671 81.377 1.00 50.88 ? 197 LYS B CD 1 ATOM 4100 C CE . LYS B 1 197 ? 7.797 9.957 79.876 1.00 51.54 ? 197 LYS B CE 1 ATOM 4101 N NZ . LYS B 1 197 ? 9.217 9.871 79.410 1.00 53.50 ? 197 LYS B NZ 1 ATOM 4102 N N . THR B 1 198 ? 10.321 12.727 84.949 1.00 46.64 ? 198 THR B N 1 ATOM 4103 C CA . THR B 1 198 ? 11.210 13.867 84.689 1.00 45.37 ? 198 THR B CA 1 ATOM 4104 C C . THR B 1 198 ? 11.509 13.938 83.188 1.00 41.45 ? 198 THR B C 1 ATOM 4105 O O . THR B 1 198 ? 11.252 12.983 82.435 1.00 41.07 ? 198 THR B O 1 ATOM 4106 C CB . THR B 1 198 ? 12.541 13.820 85.524 1.00 48.40 ? 198 THR B CB 1 ATOM 4107 O OG1 . THR B 1 198 ? 13.498 12.956 84.886 1.00 50.42 ? 198 THR B OG1 1 ATOM 4108 C CG2 . THR B 1 198 ? 12.329 13.194 86.884 1.00 46.83 ? 198 THR B CG2 1 ATOM 4109 N N . GLY B 1 199 ? 12.019 15.079 82.747 1.00 37.97 ? 199 GLY B N 1 ATOM 4110 C CA . GLY B 1 199 ? 12.322 15.253 81.330 1.00 35.90 ? 199 GLY B CA 1 ATOM 4111 C C . GLY B 1 199 ? 11.255 15.972 80.531 1.00 34.24 ? 199 GLY B C 1 ATOM 4112 O O . GLY B 1 199 ? 11.521 16.427 79.434 1.00 32.60 ? 199 GLY B O 1 ATOM 4113 N N . VAL B 1 200 ? 10.060 16.101 81.101 1.00 33.74 ? 200 VAL B N 1 ATOM 4114 C CA . VAL B 1 200 ? 8.938 16.775 80.444 1.00 32.14 ? 200 VAL B CA 1 ATOM 4115 C C . VAL B 1 200 ? 8.005 17.399 81.497 1.00 29.75 ? 200 VAL B C 1 ATOM 4116 O O . VAL B 1 200 ? 7.745 16.778 82.544 1.00 28.88 ? 200 VAL B O 1 ATOM 4117 C CB . VAL B 1 200 ? 8.161 15.820 79.451 1.00 32.91 ? 200 VAL B CB 1 ATOM 4118 C CG1 . VAL B 1 200 ? 7.507 14.653 80.162 1.00 35.13 ? 200 VAL B CG1 1 ATOM 4119 C CG2 . VAL B 1 200 ? 7.125 16.593 78.600 1.00 31.98 ? 200 VAL B CG2 1 ATOM 4120 N N . TRP B 1 201 ? 7.531 18.622 81.224 1.00 27.64 ? 201 TRP B N 1 ATOM 4121 C CA . TRP B 1 201 ? 6.577 19.337 82.113 1.00 23.87 ? 201 TRP B CA 1 ATOM 4122 C C . TRP B 1 201 ? 5.144 18.851 81.875 1.00 27.11 ? 201 TRP B C 1 ATOM 4123 O O . TRP B 1 201 ? 4.260 19.621 81.468 1.00 27.38 ? 201 TRP B O 1 ATOM 4124 C CB . TRP B 1 201 ? 6.697 20.868 81.958 1.00 24.54 ? 201 TRP B CB 1 ATOM 4125 C CG . TRP B 1 201 ? 7.996 21.493 82.534 1.00 21.86 ? 201 TRP B CG 1 ATOM 4126 C CD1 . TRP B 1 201 ? 8.987 22.148 81.825 1.00 23.72 ? 201 TRP B CD1 1 ATOM 4127 C CD2 . TRP B 1 201 ? 8.407 21.528 83.901 1.00 21.31 ? 201 TRP B CD2 1 ATOM 4128 N NE1 . TRP B 1 201 ? 9.988 22.574 82.670 1.00 22.47 ? 201 TRP B NE1 1 ATOM 4129 C CE2 . TRP B 1 201 ? 9.664 22.195 83.951 1.00 22.51 ? 201 TRP B CE2 1 ATOM 4130 C CE3 . TRP B 1 201 ? 7.855 21.041 85.104 1.00 21.95 ? 201 TRP B CE3 1 ATOM 4131 C CZ2 . TRP B 1 201 ? 10.352 22.419 85.152 1.00 22.29 ? 201 TRP B CZ2 1 ATOM 4132 C CZ3 . TRP B 1 201 ? 8.540 21.265 86.294 1.00 22.81 ? 201 TRP B CZ3 1 ATOM 4133 C CH2 . TRP B 1 201 ? 9.780 21.956 86.306 1.00 23.74 ? 201 TRP B CH2 1 ATOM 4134 N N . GLN B 1 202 ? 4.917 17.560 82.155 1.00 26.10 ? 202 GLN B N 1 ATOM 4135 C CA . GLN B 1 202 ? 3.645 16.900 81.822 1.00 27.39 ? 202 GLN B CA 1 ATOM 4136 C C . GLN B 1 202 ? 3.135 16.119 83.025 1.00 26.30 ? 202 GLN B C 1 ATOM 4137 O O . GLN B 1 202 ? 3.921 15.489 83.704 1.00 22.85 ? 202 GLN B O 1 ATOM 4138 C CB . GLN B 1 202 ? 3.857 15.965 80.640 1.00 28.69 ? 202 GLN B CB 1 ATOM 4139 C CG . GLN B 1 202 ? 2.608 15.364 80.092 1.00 33.14 ? 202 GLN B CG 1 ATOM 4140 C CD . GLN B 1 202 ? 2.873 14.571 78.825 1.00 35.51 ? 202 GLN B CD 1 ATOM 4141 O OE1 . GLN B 1 202 ? 2.084 14.629 77.879 1.00 36.07 ? 202 GLN B OE1 1 ATOM 4142 N NE2 . GLN B 1 202 ? 3.978 13.843 78.803 1.00 33.31 ? 202 GLN B NE2 1 ATOM 4143 N N . ILE B 1 203 ? 1.826 16.202 83.292 1.00 26.30 ? 203 ILE B N 1 ATOM 4144 C CA . ILE B 1 203 ? 1.208 15.667 84.510 1.00 28.73 ? 203 ILE B CA 1 ATOM 4145 C C . ILE B 1 203 ? -0.027 14.844 84.148 1.00 29.54 ? 203 ILE B C 1 ATOM 4146 O O . ILE B 1 203 ? -0.545 15.005 83.058 1.00 29.73 ? 203 ILE B O 1 ATOM 4147 C CB . ILE B 1 203 ? 0.779 16.794 85.500 1.00 28.47 ? 203 ILE B CB 1 ATOM 4148 C CG1 . ILE B 1 203 ? -0.371 17.645 84.914 1.00 26.39 ? 203 ILE B CG1 1 ATOM 4149 C CG2 . ILE B 1 203 ? 1.987 17.575 86.043 1.00 30.25 ? 203 ILE B CG2 1 ATOM 4150 C CD1 . ILE B 1 203 ? -0.851 18.717 85.815 1.00 27.06 ? 203 ILE B CD1 1 ATOM 4151 N N . GLN B 1 204 ? -0.489 13.990 85.062 1.00 32.29 ? 204 GLN B N 1 ATOM 4152 C CA . GLN B 1 204 ? -1.749 13.236 84.907 1.00 34.50 ? 204 GLN B CA 1 ATOM 4153 C C . GLN B 1 204 ? -2.961 14.142 85.016 1.00 33.43 ? 204 GLN B C 1 ATOM 4154 O O . GLN B 1 204 ? -2.996 15.050 85.835 1.00 35.27 ? 204 GLN B O 1 ATOM 4155 C CB . GLN B 1 204 ? -1.895 12.162 85.999 1.00 35.40 ? 204 GLN B CB 1 ATOM 4156 C CG . GLN B 1 204 ? -1.506 10.719 85.639 1.00 38.04 ? 204 GLN B CG 1 ATOM 4157 C CD . GLN B 1 204 ? -2.292 10.117 84.476 1.00 43.24 ? 204 GLN B CD 1 ATOM 4158 O OE1 . GLN B 1 204 ? -1.709 9.775 83.451 1.00 45.66 ? 204 GLN B OE1 1 ATOM 4159 N NE2 . GLN B 1 204 ? -3.602 9.985 84.631 1.00 45.87 ? 204 GLN B NE2 1 ATOM 4160 N N . MET B 1 205 ? -3.958 13.882 84.188 1.00 34.98 ? 205 MET B N 1 ATOM 4161 C CA . MET B 1 205 ? -5.269 14.519 84.312 1.00 35.80 ? 205 MET B CA 1 ATOM 4162 C C . MET B 1 205 ? -6.264 13.357 84.522 1.00 36.67 ? 205 MET B C 1 ATOM 4163 O O . MET B 1 205 ? -6.132 12.323 83.872 1.00 39.03 ? 205 MET B O 1 ATOM 4164 C CB . MET B 1 205 ? -5.576 15.375 83.064 1.00 32.32 ? 205 MET B CB 1 ATOM 4165 C CG . MET B 1 205 ? -6.870 16.208 83.134 1.00 32.48 ? 205 MET B CG 1 ATOM 4166 S SD . MET B 1 205 ? -6.896 17.814 82.226 1.00 35.95 ? 205 MET B SD 1 ATOM 4167 C CE . MET B 1 205 ? -6.885 17.247 80.531 1.00 34.39 ? 205 MET B CE 1 ATOM 4168 N N . LYS B 1 206 ? -7.204 13.481 85.452 1.00 37.48 ? 206 LYS B N 1 ATOM 4169 C CA . LYS B 1 206 ? -8.142 12.357 85.696 1.00 41.56 ? 206 LYS B CA 1 ATOM 4170 C C . LYS B 1 206 ? -9.590 12.715 85.355 1.00 42.04 ? 206 LYS B C 1 ATOM 4171 O O . LYS B 1 206 ? -10.531 12.096 85.867 1.00 45.91 ? 206 LYS B O 1 ATOM 4172 C CB . LYS B 1 206 ? -8.061 11.775 87.123 1.00 43.55 ? 206 LYS B CB 1 ATOM 4173 C CG . LYS B 1 206 ? -6.781 12.012 87.934 1.00 48.14 ? 206 LYS B CG 1 ATOM 4174 C CD . LYS B 1 206 ? -6.889 13.320 88.764 1.00 50.43 ? 206 LYS B CD 1 ATOM 4175 C CE . LYS B 1 206 ? -6.232 13.203 90.129 1.00 50.36 ? 206 LYS B CE 1 ATOM 4176 N NZ . LYS B 1 206 ? -7.159 12.675 91.174 1.00 52.34 ? 206 LYS B NZ 1 ATOM 4177 N N . GLY B 1 207 ? -9.766 13.706 84.486 1.00 39.14 ? 207 GLY B N 1 ATOM 4178 C CA . GLY B 1 207 ? -11.080 14.031 83.974 1.00 37.50 ? 207 GLY B CA 1 ATOM 4179 C C . GLY B 1 207 ? -11.223 15.468 83.529 1.00 37.35 ? 207 GLY B C 1 ATOM 4180 O O . GLY B 1 207 ? -10.646 16.371 84.143 1.00 37.46 ? 207 GLY B O 1 ATOM 4181 N N . VAL B 1 208 ? -11.977 15.669 82.449 1.00 35.09 ? 208 VAL B N 1 ATOM 4182 C CA . VAL B 1 208 ? -12.441 17.001 82.044 1.00 34.66 ? 208 VAL B CA 1 ATOM 4183 C C . VAL B 1 208 ? -13.983 17.023 82.174 1.00 34.46 ? 208 VAL B C 1 ATOM 4184 O O . VAL B 1 208 ? -14.671 16.163 81.627 1.00 32.37 ? 208 VAL B O 1 ATOM 4185 C CB . VAL B 1 208 ? -11.992 17.374 80.593 1.00 34.18 ? 208 VAL B CB 1 ATOM 4186 C CG1 . VAL B 1 208 ? -12.530 18.763 80.172 1.00 34.80 ? 208 VAL B CG1 1 ATOM 4187 C CG2 . VAL B 1 208 ? -10.459 17.306 80.450 1.00 31.97 ? 208 VAL B CG2 1 ATOM 4188 N N . SER B 1 209 ? -14.496 17.998 82.913 1.00 36.05 ? 209 SER B N 1 ATOM 4189 C CA . SER B 1 209 ? -15.916 18.118 83.187 1.00 37.69 ? 209 SER B CA 1 ATOM 4190 C C . SER B 1 209 ? -16.486 19.332 82.501 1.00 40.73 ? 209 SER B C 1 ATOM 4191 O O . SER B 1 209 ? -15.861 20.395 82.473 1.00 40.65 ? 209 SER B O 1 ATOM 4192 C CB . SER B 1 209 ? -16.159 18.253 84.683 1.00 37.89 ? 209 SER B CB 1 ATOM 4193 O OG . SER B 1 209 ? -15.813 17.062 85.348 1.00 38.69 ? 209 SER B OG 1 ATOM 4194 N N . VAL B 1 210 ? -17.681 19.168 81.941 1.00 43.90 ? 210 VAL B N 1 ATOM 4195 C CA . VAL B 1 210 ? -18.455 20.300 81.455 1.00 43.71 ? 210 VAL B CA 1 ATOM 4196 C C . VAL B 1 210 ? -19.624 20.451 82.409 1.00 45.68 ? 210 VAL B C 1 ATOM 4197 O O . VAL B 1 210 ? -20.414 19.517 82.580 1.00 46.53 ? 210 VAL B O 1 ATOM 4198 C CB . VAL B 1 210 ? -18.944 20.110 80.001 1.00 43.31 ? 210 VAL B CB 1 ATOM 4199 C CG1 . VAL B 1 210 ? -19.865 21.270 79.592 1.00 43.70 ? 210 VAL B CG1 1 ATOM 4200 C CG2 . VAL B 1 210 ? -17.781 20.027 79.057 1.00 40.97 ? 210 VAL B CG2 1 ATOM 4201 N N . GLY B 1 211 ? -19.721 21.621 83.039 1.00 45.29 ? 211 GLY B N 1 ATOM 4202 C CA . GLY B 1 211 ? -20.683 21.847 84.102 1.00 47.01 ? 211 GLY B CA 1 ATOM 4203 C C . GLY B 1 211 ? -20.430 20.887 85.253 1.00 48.75 ? 211 GLY B C 1 ATOM 4204 O O . GLY B 1 211 ? -19.322 20.849 85.803 1.00 45.95 ? 211 GLY B O 1 ATOM 4205 N N . SER B 1 212 ? -21.449 20.100 85.609 1.00 50.23 ? 212 SER B N 1 ATOM 4206 C CA . SER B 1 212 ? -21.372 19.218 86.785 1.00 51.76 ? 212 SER B CA 1 ATOM 4207 C C . SER B 1 212 ? -20.821 17.848 86.424 1.00 52.30 ? 212 SER B C 1 ATOM 4208 O O . SER B 1 212 ? -20.263 17.150 87.266 1.00 52.57 ? 212 SER B O 1 ATOM 4209 C CB . SER B 1 212 ? -22.742 19.069 87.459 1.00 53.83 ? 212 SER B CB 1 ATOM 4210 O OG . SER B 1 212 ? -23.169 20.291 88.050 1.00 56.21 ? 212 SER B OG 1 ATOM 4211 N N . SER B 1 213 ? -20.968 17.478 85.160 1.00 51.72 ? 213 SER B N 1 ATOM 4212 C CA . SER B 1 213 ? -20.659 16.126 84.721 1.00 52.29 ? 213 SER B CA 1 ATOM 4213 C C . SER B 1 213 ? -19.299 16.030 84.039 1.00 51.63 ? 213 SER B C 1 ATOM 4214 O O . SER B 1 213 ? -18.918 16.910 83.250 1.00 49.23 ? 213 SER B O 1 ATOM 4215 C CB . SER B 1 213 ? -21.755 15.629 83.777 1.00 52.95 ? 213 SER B CB 1 ATOM 4216 O OG . SER B 1 213 ? -23.038 15.938 84.307 1.00 54.82 ? 213 SER B OG 1 ATOM 4217 N N . THR B 1 214 ? -18.579 14.955 84.353 1.00 50.43 ? 214 THR B N 1 ATOM 4218 C CA . THR B 1 214 ? -17.365 14.599 83.638 1.00 49.45 ? 214 THR B CA 1 ATOM 4219 C C . THR B 1 214 ? -17.748 14.051 82.279 1.00 49.15 ? 214 THR B C 1 ATOM 4220 O O . THR B 1 214 ? -18.514 13.092 82.174 1.00 50.47 ? 214 THR B O 1 ATOM 4221 C CB . THR B 1 214 ? -16.559 13.553 84.420 1.00 50.26 ? 214 THR B CB 1 ATOM 4222 O OG1 . THR B 1 214 ? -16.456 13.965 85.788 1.00 49.97 ? 214 THR B OG1 1 ATOM 4223 C CG2 . THR B 1 214 ? -15.116 13.521 83.943 1.00 49.86 ? 214 THR B CG2 1 ATOM 4224 N N . LEU B 1 215 ? -17.206 14.678 81.243 1.00 47.89 ? 215 LEU B N 1 ATOM 4225 C CA . LEU B 1 215 ? -17.442 14.286 79.870 1.00 46.62 ? 215 LEU B CA 1 ATOM 4226 C C . LEU B 1 215 ? -16.275 13.479 79.306 1.00 45.88 ? 215 LEU B C 1 ATOM 4227 O O . LEU B 1 215 ? -16.460 12.601 78.463 1.00 45.45 ? 215 LEU B O 1 ATOM 4228 C CB . LEU B 1 215 ? -17.619 15.551 79.045 1.00 46.48 ? 215 LEU B CB 1 ATOM 4229 C CG . LEU B 1 215 ? -18.012 15.566 77.578 1.00 44.75 ? 215 LEU B CG 1 ATOM 4230 C CD1 . LEU B 1 215 ? -19.526 15.498 77.476 1.00 46.40 ? 215 LEU B CD1 1 ATOM 4231 C CD2 . LEU B 1 215 ? -17.526 16.889 76.997 1.00 44.11 ? 215 LEU B CD2 1 ATOM 4232 N N . LEU B 1 216 ? -15.073 13.781 79.774 1.00 45.40 ? 216 LEU B N 1 ATOM 4233 C CA . LEU B 1 216 ? -13.872 13.377 79.054 1.00 45.82 ? 216 LEU B CA 1 ATOM 4234 C C . LEU B 1 216 ? -12.781 12.862 79.965 1.00 45.52 ? 216 LEU B C 1 ATOM 4235 O O . LEU B 1 216 ? -12.724 13.214 81.141 1.00 44.73 ? 216 LEU B O 1 ATOM 4236 C CB . LEU B 1 216 ? -13.321 14.560 78.246 1.00 47.03 ? 216 LEU B CB 1 ATOM 4237 C CG . LEU B 1 216 ? -14.088 15.152 77.060 1.00 47.69 ? 216 LEU B CG 1 ATOM 4238 C CD1 . LEU B 1 216 ? -13.420 16.439 76.630 1.00 47.73 ? 216 LEU B CD1 1 ATOM 4239 C CD2 . LEU B 1 216 ? -14.188 14.161 75.879 1.00 47.36 ? 216 LEU B CD2 1 ATOM 4240 N N . CYS B 1 217 ? -11.923 12.010 79.413 1.00 47.50 ? 217 CYS B N 1 ATOM 4241 C CA . CYS B 1 217 ? -10.677 11.669 80.066 1.00 49.28 ? 217 CYS B CA 1 ATOM 4242 C C . CYS B 1 217 ? -10.901 10.891 81.380 1.00 51.35 ? 217 CYS B C 1 ATOM 4243 O O . CYS B 1 217 ? -10.056 10.914 82.281 1.00 50.60 ? 217 CYS B O 1 ATOM 4244 C CB . CYS B 1 217 ? -9.834 12.958 80.244 1.00 49.63 ? 217 CYS B CB 1 ATOM 4245 S SG . CYS B 1 217 ? -8.290 12.835 81.167 1.00 52.58 ? 217 CYS B SG 1 ATOM 4246 N N . GLU B 1 218 ? -12.037 10.195 81.491 1.00 53.26 ? 218 GLU B N 1 ATOM 4247 C CA . GLU B 1 218 ? -12.139 9.124 82.494 1.00 55.40 ? 218 GLU B CA 1 ATOM 4248 C C . GLU B 1 218 ? -11.134 8.089 82.017 1.00 54.84 ? 218 GLU B C 1 ATOM 4249 O O . GLU B 1 218 ? -10.907 7.951 80.806 1.00 53.96 ? 218 GLU B O 1 ATOM 4250 C CB . GLU B 1 218 ? -13.525 8.478 82.566 1.00 57.22 ? 218 GLU B CB 1 ATOM 4251 C CG . GLU B 1 218 ? -14.702 9.391 82.904 1.00 59.12 ? 218 GLU B CG 1 ATOM 4252 C CD . GLU B 1 218 ? -15.576 9.664 81.687 1.00 60.14 ? 218 GLU B CD 1 ATOM 4253 O OE1 . GLU B 1 218 ? -16.824 9.732 81.855 1.00 59.03 ? 218 GLU B OE1 1 ATOM 4254 O OE2 . GLU B 1 218 ? -15.012 9.789 80.560 1.00 59.66 ? 218 GLU B OE2 1 ATOM 4255 N N . ASP B 1 219 ? -10.511 7.382 82.949 1.00 54.79 ? 219 ASP B N 1 ATOM 4256 C CA . ASP B 1 219 ? -9.474 6.409 82.591 1.00 55.81 ? 219 ASP B CA 1 ATOM 4257 C C . ASP B 1 219 ? -8.130 7.085 82.310 1.00 53.39 ? 219 ASP B C 1 ATOM 4258 O O . ASP B 1 219 ? -7.166 6.423 81.899 1.00 53.97 ? 219 ASP B O 1 ATOM 4259 C CB . ASP B 1 219 ? -9.922 5.516 81.412 1.00 58.32 ? 219 ASP B CB 1 ATOM 4260 C CG . ASP B 1 219 ? -11.153 4.671 81.755 1.00 62.21 ? 219 ASP B CG 1 ATOM 4261 O OD1 . ASP B 1 219 ? -11.014 3.730 82.580 1.00 64.14 ? 219 ASP B OD1 1 ATOM 4262 O OD2 . ASP B 1 219 ? -12.297 4.877 81.263 1.00 62.81 ? 219 ASP B OD2 1 ATOM 4263 N N . GLY B 1 220 ? -8.079 8.401 82.536 1.00 50.42 ? 220 GLY B N 1 ATOM 4264 C CA . GLY B 1 220 ? -6.840 9.165 82.513 1.00 44.96 ? 220 GLY B CA 1 ATOM 4265 C C . GLY B 1 220 ? -6.361 9.654 81.161 1.00 44.82 ? 220 GLY B C 1 ATOM 4266 O O . GLY B 1 220 ? -6.670 9.068 80.115 1.00 44.03 ? 220 GLY B O 1 ATOM 4267 N N . CYS B 1 221 ? -5.604 10.750 81.206 1.00 42.88 ? 221 CYS B N 1 ATOM 4268 C CA . CYS B 1 221 ? -4.930 11.351 80.059 1.00 43.07 ? 221 CYS B CA 1 ATOM 4269 C C . CYS B 1 221 ? -3.780 12.245 80.564 1.00 41.33 ? 221 CYS B C 1 ATOM 4270 O O . CYS B 1 221 ? -3.681 12.510 81.758 1.00 42.47 ? 221 CYS B O 1 ATOM 4271 C CB . CYS B 1 221 ? -5.914 12.144 79.202 1.00 44.18 ? 221 CYS B CB 1 ATOM 4272 S SG . CYS B 1 221 ? -6.709 13.504 80.066 1.00 48.72 ? 221 CYS B SG 1 ATOM 4273 N N . LEU B 1 222 ? -2.909 12.683 79.660 1.00 39.95 ? 222 LEU B N 1 ATOM 4274 C CA . LEU B 1 222 ? -1.743 13.485 80.021 1.00 35.41 ? 222 LEU B CA 1 ATOM 4275 C C . LEU B 1 222 ? -1.999 14.959 79.736 1.00 33.77 ? 222 LEU B C 1 ATOM 4276 O O . LEU B 1 222 ? -2.773 15.291 78.841 1.00 36.58 ? 222 LEU B O 1 ATOM 4277 C CB . LEU B 1 222 ? -0.528 13.012 79.238 1.00 35.49 ? 222 LEU B CB 1 ATOM 4278 C CG . LEU B 1 222 ? -0.145 11.524 79.259 1.00 34.83 ? 222 LEU B CG 1 ATOM 4279 C CD1 . LEU B 1 222 ? 0.988 11.291 78.264 1.00 32.26 ? 222 LEU B CD1 1 ATOM 4280 C CD2 . LEU B 1 222 ? 0.234 11.027 80.660 1.00 33.03 ? 222 LEU B CD2 1 ATOM 4281 N N . ALA B 1 223 ? -1.369 15.843 80.507 1.00 30.49 ? 223 ALA B N 1 ATOM 4282 C CA . ALA B 1 223 ? -1.561 17.284 80.314 1.00 27.55 ? 223 ALA B CA 1 ATOM 4283 C C . ALA B 1 223 ? -0.201 17.979 80.327 1.00 28.21 ? 223 ALA B C 1 ATOM 4284 O O . ALA B 1 223 ? 0.479 17.976 81.338 1.00 26.09 ? 223 ALA B O 1 ATOM 4285 C CB . ALA B 1 223 ? -2.484 17.849 81.390 1.00 26.38 ? 223 ALA B CB 1 ATOM 4286 N N . LEU B 1 224 ? 0.213 18.504 79.178 1.00 28.12 ? 224 LEU B N 1 ATOM 4287 C CA . LEU B 1 224 ? 1.463 19.244 79.068 1.00 26.82 ? 224 LEU B CA 1 ATOM 4288 C C . LEU B 1 224 ? 1.182 20.681 79.504 1.00 24.71 ? 224 LEU B C 1 ATOM 4289 O O . LEU B 1 224 ? 0.254 21.309 79.014 1.00 29.28 ? 224 LEU B O 1 ATOM 4290 C CB . LEU B 1 224 ? 2.000 19.190 77.620 1.00 27.34 ? 224 LEU B CB 1 ATOM 4291 C CG . LEU B 1 224 ? 3.329 19.913 77.298 1.00 28.50 ? 224 LEU B CG 1 ATOM 4292 C CD1 . LEU B 1 224 ? 4.512 19.196 77.906 1.00 28.76 ? 224 LEU B CD1 1 ATOM 4293 C CD2 . LEU B 1 224 ? 3.566 20.128 75.800 1.00 26.76 ? 224 LEU B CD2 1 ATOM 4294 N N . VAL B 1 225 ? 1.956 21.194 80.452 1.00 26.01 ? 225 VAL B N 1 ATOM 4295 C CA . VAL B 1 225 ? 1.831 22.612 80.834 1.00 24.94 ? 225 VAL B CA 1 ATOM 4296 C C . VAL B 1 225 ? 2.895 23.409 80.024 1.00 25.44 ? 225 VAL B C 1 ATOM 4297 O O . VAL B 1 225 ? 4.089 23.529 80.425 1.00 22.74 ? 225 VAL B O 1 ATOM 4298 C CB . VAL B 1 225 ? 1.901 22.823 82.375 1.00 26.36 ? 225 VAL B CB 1 ATOM 4299 C CG1 . VAL B 1 225 ? 1.464 24.256 82.788 1.00 24.72 ? 225 VAL B CG1 1 ATOM 4300 C CG2 . VAL B 1 225 ? 1.002 21.779 83.124 1.00 26.49 ? 225 VAL B CG2 1 ATOM 4301 N N . ASP B 1 226 ? 2.425 23.926 78.881 1.00 23.32 ? 226 ASP B N 1 ATOM 4302 C CA . ASP B 1 226 ? 3.229 24.627 77.885 1.00 23.98 ? 226 ASP B CA 1 ATOM 4303 C C . ASP B 1 226 ? 3.000 26.156 77.828 1.00 23.26 ? 226 ASP B C 1 ATOM 4304 O O . ASP B 1 226 ? 2.036 26.629 77.251 1.00 21.12 ? 226 ASP B O 1 ATOM 4305 C CB . ASP B 1 226 ? 2.972 24.025 76.504 1.00 25.20 ? 226 ASP B CB 1 ATOM 4306 C CG . ASP B 1 226 ? 3.950 24.562 75.452 1.00 26.77 ? 226 ASP B CG 1 ATOM 4307 O OD1 . ASP B 1 226 ? 4.821 25.360 75.840 1.00 24.99 ? 226 ASP B OD1 1 ATOM 4308 O OD2 . ASP B 1 226 ? 3.927 24.241 74.253 1.00 25.73 ? 226 ASP B OD2 1 ATOM 4309 N N . THR B 1 227 ? 3.913 26.923 78.411 1.00 24.69 ? 227 THR B N 1 ATOM 4310 C CA . THR B 1 227 ? 3.777 28.375 78.457 1.00 23.80 ? 227 THR B CA 1 ATOM 4311 C C . THR B 1 227 ? 3.899 28.998 77.073 1.00 24.26 ? 227 THR B C 1 ATOM 4312 O O . THR B 1 227 ? 3.589 30.163 76.899 1.00 26.07 ? 227 THR B O 1 ATOM 4313 C CB . THR B 1 227 ? 4.845 28.978 79.380 1.00 23.51 ? 227 THR B CB 1 ATOM 4314 O OG1 . THR B 1 227 ? 6.148 28.492 78.994 1.00 21.58 ? 227 THR B OG1 1 ATOM 4315 C CG2 . THR B 1 227 ? 4.654 28.477 80.777 1.00 24.16 ? 227 THR B CG2 1 ATOM 4316 N N . GLY B 1 228 ? 4.361 28.221 76.096 1.00 23.36 ? 228 GLY B N 1 ATOM 4317 C CA . GLY B 1 228 ? 4.558 28.736 74.742 1.00 24.73 ? 228 GLY B CA 1 ATOM 4318 C C . GLY B 1 228 ? 3.437 28.393 73.774 1.00 25.81 ? 228 GLY B C 1 ATOM 4319 O O . GLY B 1 228 ? 3.546 28.685 72.591 1.00 25.56 ? 228 GLY B O 1 ATOM 4320 N N . ALA B 1 229 ? 2.369 27.754 74.272 1.00 25.41 ? 229 ALA B N 1 ATOM 4321 C CA . ALA B 1 229 ? 1.170 27.477 73.478 1.00 22.73 ? 229 ALA B CA 1 ATOM 4322 C C . ALA B 1 229 ? 0.099 28.543 73.792 1.00 24.27 ? 229 ALA B C 1 ATOM 4323 O O . ALA B 1 229 ? -0.088 28.892 74.942 1.00 22.58 ? 229 ALA B O 1 ATOM 4324 C CB . ALA B 1 229 ? 0.633 26.109 73.825 1.00 22.39 ? 229 ALA B CB 1 ATOM 4325 N N . SER B 1 230 ? -0.619 29.051 72.796 1.00 25.92 ? 230 SER B N 1 ATOM 4326 C CA . SER B 1 230 ? -1.538 30.149 73.085 1.00 26.15 ? 230 SER B CA 1 ATOM 4327 C C . SER B 1 230 ? -2.796 29.714 73.825 1.00 25.80 ? 230 SER B C 1 ATOM 4328 O O . SER B 1 230 ? -3.415 30.522 74.517 1.00 26.81 ? 230 SER B O 1 ATOM 4329 C CB . SER B 1 230 ? -1.927 30.896 71.801 1.00 25.65 ? 230 SER B CB 1 ATOM 4330 O OG . SER B 1 230 ? -0.777 31.413 71.163 1.00 25.77 ? 230 SER B OG 1 ATOM 4331 N N . TYR B 1 231 ? -3.175 28.443 73.675 1.00 27.32 ? 231 TYR B N 1 ATOM 4332 C CA . TYR B 1 231 ? -4.512 27.971 74.049 1.00 26.46 ? 231 TYR B CA 1 ATOM 4333 C C . TYR B 1 231 ? -4.487 26.723 74.912 1.00 26.76 ? 231 TYR B C 1 ATOM 4334 O O . TYR B 1 231 ? -3.447 26.068 75.063 1.00 26.21 ? 231 TYR B O 1 ATOM 4335 C CB . TYR B 1 231 ? -5.314 27.628 72.789 1.00 27.99 ? 231 TYR B CB 1 ATOM 4336 C CG . TYR B 1 231 ? -5.399 28.724 71.765 1.00 29.92 ? 231 TYR B CG 1 ATOM 4337 C CD1 . TYR B 1 231 ? -6.135 29.883 72.019 1.00 30.62 ? 231 TYR B CD1 1 ATOM 4338 C CD2 . TYR B 1 231 ? -4.762 28.598 70.531 1.00 28.51 ? 231 TYR B CD2 1 ATOM 4339 C CE1 . TYR B 1 231 ? -6.208 30.908 71.078 1.00 29.82 ? 231 TYR B CE1 1 ATOM 4340 C CE2 . TYR B 1 231 ? -4.835 29.621 69.577 1.00 30.54 ? 231 TYR B CE2 1 ATOM 4341 C CZ . TYR B 1 231 ? -5.563 30.773 69.858 1.00 30.94 ? 231 TYR B CZ 1 ATOM 4342 O OH . TYR B 1 231 ? -5.673 31.805 68.906 1.00 30.07 ? 231 TYR B OH 1 ATOM 4343 N N . ILE B 1 232 ? -5.656 26.364 75.439 1.00 29.88 ? 232 ILE B N 1 ATOM 4344 C CA . ILE B 1 232 ? -5.878 24.992 75.892 1.00 28.06 ? 232 ILE B CA 1 ATOM 4345 C C . ILE B 1 232 ? -6.131 24.182 74.604 1.00 30.18 ? 232 ILE B C 1 ATOM 4346 O O . ILE B 1 232 ? -6.911 24.594 73.713 1.00 28.82 ? 232 ILE B O 1 ATOM 4347 C CB . ILE B 1 232 ? -7.046 24.901 76.938 1.00 29.95 ? 232 ILE B CB 1 ATOM 4348 C CG1 . ILE B 1 232 ? -6.602 25.479 78.298 1.00 29.35 ? 232 ILE B CG1 1 ATOM 4349 C CG2 . ILE B 1 232 ? -7.502 23.452 77.154 1.00 29.74 ? 232 ILE B CG2 1 ATOM 4350 C CD1 . ILE B 1 232 ? -7.730 25.857 79.230 1.00 28.12 ? 232 ILE B CD1 1 ATOM 4351 N N . SER B 1 233 ? -5.414 23.074 74.466 1.00 27.33 ? 233 SER B N 1 ATOM 4352 C CA . SER B 1 233 ? -5.619 22.187 73.341 1.00 26.35 ? 233 SER B CA 1 ATOM 4353 C C . SER B 1 233 ? -5.776 20.731 73.748 1.00 28.54 ? 233 SER B C 1 ATOM 4354 O O . SER B 1 233 ? -5.195 20.277 74.736 1.00 28.34 ? 233 SER B O 1 ATOM 4355 C CB . SER B 1 233 ? -4.493 22.328 72.314 1.00 26.75 ? 233 SER B CB 1 ATOM 4356 O OG . SER B 1 233 ? -3.261 21.778 72.768 1.00 26.08 ? 233 SER B OG 1 ATOM 4357 N N . GLY B 1 234 ? -6.557 20.007 72.953 1.00 28.92 ? 234 GLY B N 1 ATOM 4358 C CA . GLY B 1 234 ? -6.732 18.570 73.124 1.00 27.66 ? 234 GLY B CA 1 ATOM 4359 C C . GLY B 1 234 ? -6.646 17.948 71.751 1.00 30.75 ? 234 GLY B C 1 ATOM 4360 O O . GLY B 1 234 ? -6.631 18.660 70.728 1.00 29.18 ? 234 GLY B O 1 ATOM 4361 N N . SER B 1 235 ? -6.557 16.624 71.718 1.00 32.95 ? 235 SER B N 1 ATOM 4362 C CA . SER B 1 235 ? -6.663 15.890 70.463 1.00 35.30 ? 235 SER B CA 1 ATOM 4363 C C . SER B 1 235 ? -7.924 16.357 69.733 1.00 33.91 ? 235 SER B C 1 ATOM 4364 O O . SER B 1 235 ? -8.912 16.774 70.361 1.00 36.09 ? 235 SER B O 1 ATOM 4365 C CB . SER B 1 235 ? -6.750 14.391 70.729 1.00 34.54 ? 235 SER B CB 1 ATOM 4366 O OG . SER B 1 235 ? -8.034 14.070 71.251 1.00 36.04 ? 235 SER B OG 1 ATOM 4367 N N . THR B 1 236 ? -7.880 16.290 68.411 1.00 35.97 ? 236 THR B N 1 ATOM 4368 C CA . THR B 1 236 ? -9.028 16.610 67.558 1.00 38.50 ? 236 THR B CA 1 ATOM 4369 C C . THR B 1 236 ? -10.288 15.872 68.024 1.00 38.57 ? 236 THR B C 1 ATOM 4370 O O . THR B 1 236 ? -11.337 16.488 68.150 1.00 40.19 ? 236 THR B O 1 ATOM 4371 C CB . THR B 1 236 ? -8.707 16.284 66.088 1.00 38.32 ? 236 THR B CB 1 ATOM 4372 O OG1 . THR B 1 236 ? -7.792 17.256 65.569 1.00 39.01 ? 236 THR B OG1 1 ATOM 4373 C CG2 . THR B 1 236 ? -9.928 16.465 65.200 1.00 39.11 ? 236 THR B CG2 1 ATOM 4374 N N . SER B 1 237 ? -10.182 14.570 68.304 1.00 37.32 ? 237 SER B N 1 ATOM 4375 C CA . SER B 1 237 ? -11.344 13.818 68.802 1.00 38.76 ? 237 SER B CA 1 ATOM 4376 C C . SER B 1 237 ? -11.891 14.314 70.157 1.00 38.35 ? 237 SER B C 1 ATOM 4377 O O . SER B 1 237 ? -13.111 14.402 70.327 1.00 38.02 ? 237 SER B O 1 ATOM 4378 C CB . SER B 1 237 ? -11.063 12.317 68.854 1.00 39.86 ? 237 SER B CB 1 ATOM 4379 O OG . SER B 1 237 ? -10.161 12.008 69.898 1.00 43.68 ? 237 SER B OG 1 ATOM 4380 N N . SER B 1 238 ? -11.003 14.651 71.102 1.00 34.22 ? 238 SER B N 1 ATOM 4381 C CA . SER B 1 238 ? -11.428 15.188 72.409 1.00 31.79 ? 238 SER B CA 1 ATOM 4382 C C . SER B 1 238 ? -12.120 16.540 72.293 1.00 32.06 ? 238 SER B C 1 ATOM 4383 O O . SER B 1 238 ? -13.137 16.792 72.946 1.00 30.88 ? 238 SER B O 1 ATOM 4384 C CB . SER B 1 238 ? -10.229 15.370 73.342 1.00 35.71 ? 238 SER B CB 1 ATOM 4385 O OG . SER B 1 238 ? -9.801 14.143 73.891 1.00 39.11 ? 238 SER B OG 1 ATOM 4386 N N . ILE B 1 239 ? -11.549 17.419 71.484 1.00 29.46 ? 239 ILE B N 1 ATOM 4387 C CA . ILE B 1 239 ? -12.086 18.777 71.334 1.00 32.74 ? 239 ILE B CA 1 ATOM 4388 C C . ILE B 1 239 ? -13.409 18.778 70.577 1.00 32.69 ? 239 ILE B C 1 ATOM 4389 O O . ILE B 1 239 ? -14.280 19.586 70.864 1.00 31.95 ? 239 ILE B O 1 ATOM 4390 C CB . ILE B 1 239 ? -11.011 19.735 70.685 1.00 32.42 ? 239 ILE B CB 1 ATOM 4391 C CG1 . ILE B 1 239 ? -9.822 19.874 71.635 1.00 32.42 ? 239 ILE B CG1 1 ATOM 4392 C CG2 . ILE B 1 239 ? -11.602 21.122 70.324 1.00 34.16 ? 239 ILE B CG2 1 ATOM 4393 C CD1 . ILE B 1 239 ? -10.203 20.443 73.000 1.00 32.56 ? 239 ILE B CD1 1 ATOM 4394 N N . GLU B 1 240 ? -13.552 17.862 69.624 1.00 33.04 ? 240 GLU B N 1 ATOM 4395 C CA . GLU B 1 240 ? -14.844 17.640 68.965 1.00 36.25 ? 240 GLU B CA 1 ATOM 4396 C C . GLU B 1 240 ? -15.945 17.350 69.987 1.00 36.18 ? 240 GLU B C 1 ATOM 4397 O O . GLU B 1 240 ? -17.018 17.968 69.953 1.00 35.46 ? 240 GLU B O 1 ATOM 4398 C CB . GLU B 1 240 ? -14.741 16.461 68.003 1.00 38.79 ? 240 GLU B CB 1 ATOM 4399 C CG . GLU B 1 240 ? -14.082 16.749 66.666 1.00 43.11 ? 240 GLU B CG 1 ATOM 4400 C CD . GLU B 1 240 ? -13.742 15.465 65.928 1.00 48.24 ? 240 GLU B CD 1 ATOM 4401 O OE1 . GLU B 1 240 ? -13.980 14.365 66.499 1.00 48.51 ? 240 GLU B OE1 1 ATOM 4402 O OE2 . GLU B 1 240 ? -13.237 15.551 64.787 1.00 50.23 ? 240 GLU B OE2 1 ATOM 4403 N N . LYS B 1 241 ? -15.665 16.419 70.905 1.00 36.09 ? 241 LYS B N 1 ATOM 4404 C CA . LYS B 1 241 ? -16.593 16.075 71.988 1.00 36.50 ? 241 LYS B CA 1 ATOM 4405 C C . LYS B 1 241 ? -16.826 17.246 72.926 1.00 35.29 ? 241 LYS B C 1 ATOM 4406 O O . LYS B 1 241 ? -17.966 17.540 73.307 1.00 34.69 ? 241 LYS B O 1 ATOM 4407 C CB . LYS B 1 241 ? -16.065 14.897 72.806 1.00 38.99 ? 241 LYS B CB 1 ATOM 4408 C CG . LYS B 1 241 ? -16.200 13.552 72.141 1.00 40.68 ? 241 LYS B CG 1 ATOM 4409 C CD . LYS B 1 241 ? -16.371 12.462 73.187 1.00 44.89 ? 241 LYS B CD 1 ATOM 4410 C CE . LYS B 1 241 ? -17.756 12.535 73.862 1.00 47.50 ? 241 LYS B CE 1 ATOM 4411 N NZ . LYS B 1 241 ? -17.976 11.405 74.809 1.00 46.55 ? 241 LYS B NZ 1 ATOM 4412 N N . LEU B 1 242 ? -15.745 17.918 73.305 1.00 32.19 ? 242 LEU B N 1 ATOM 4413 C CA . LEU B 1 242 ? -15.887 19.094 74.151 1.00 31.45 ? 242 LEU B CA 1 ATOM 4414 C C . LEU B 1 242 ? -16.797 20.136 73.517 1.00 31.58 ? 242 LEU B C 1 ATOM 4415 O O . LEU B 1 242 ? -17.658 20.684 74.180 1.00 32.67 ? 242 LEU B O 1 ATOM 4416 C CB . LEU B 1 242 ? -14.531 19.727 74.485 1.00 29.77 ? 242 LEU B CB 1 ATOM 4417 C CG . LEU B 1 242 ? -14.582 20.850 75.535 1.00 28.94 ? 242 LEU B CG 1 ATOM 4418 C CD1 . LEU B 1 242 ? -14.839 20.252 76.892 1.00 29.68 ? 242 LEU B CD1 1 ATOM 4419 C CD2 . LEU B 1 242 ? -13.259 21.640 75.568 1.00 29.42 ? 242 LEU B CD2 1 ATOM 4420 N N . MET B 1 243 ? -16.584 20.416 72.236 1.00 34.02 ? 243 MET B N 1 ATOM 4421 C CA . MET B 1 243 ? -17.291 21.514 71.563 1.00 34.26 ? 243 MET B CA 1 ATOM 4422 C C . MET B 1 243 ? -18.752 21.182 71.264 1.00 38.01 ? 243 MET B C 1 ATOM 4423 O O . MET B 1 243 ? -19.621 22.064 71.233 1.00 40.53 ? 243 MET B O 1 ATOM 4424 C CB . MET B 1 243 ? -16.539 21.915 70.304 1.00 29.79 ? 243 MET B CB 1 ATOM 4425 C CG . MET B 1 243 ? -15.186 22.554 70.605 1.00 30.14 ? 243 MET B CG 1 ATOM 4426 S SD . MET B 1 243 ? -15.415 24.070 71.570 1.00 33.52 ? 243 MET B SD 1 ATOM 4427 C CE . MET B 1 243 ? -13.690 24.549 71.698 1.00 29.74 ? 243 MET B CE 1 ATOM 4428 N N . GLU B 1 244 ? -19.022 19.903 71.059 1.00 41.37 ? 244 GLU B N 1 ATOM 4429 C CA . GLU B 1 244 ? -20.385 19.423 70.923 1.00 44.55 ? 244 GLU B CA 1 ATOM 4430 C C . GLU B 1 244 ? -21.138 19.750 72.211 1.00 45.51 ? 244 GLU B C 1 ATOM 4431 O O . GLU B 1 244 ? -22.211 20.338 72.176 1.00 47.31 ? 244 GLU B O 1 ATOM 4432 C CB . GLU B 1 244 ? -20.362 17.920 70.664 1.00 45.59 ? 244 GLU B CB 1 ATOM 4433 C CG . GLU B 1 244 ? -21.531 17.391 69.862 1.00 50.60 ? 244 GLU B CG 1 ATOM 4434 C CD . GLU B 1 244 ? -21.916 15.970 70.253 1.00 54.44 ? 244 GLU B CD 1 ATOM 4435 O OE1 . GLU B 1 244 ? -22.454 15.239 69.387 1.00 56.77 ? 244 GLU B OE1 1 ATOM 4436 O OE2 . GLU B 1 244 ? -21.700 15.585 71.427 1.00 54.50 ? 244 GLU B OE2 1 ATOM 4437 N N . ALA B 1 245 ? -20.542 19.405 73.352 1.00 45.64 ? 245 ALA B N 1 ATOM 4438 C CA . ALA B 1 245 ? -21.136 19.667 74.661 1.00 44.50 ? 245 ALA B CA 1 ATOM 4439 C C . ALA B 1 245 ? -21.300 21.147 75.002 1.00 44.52 ? 245 ALA B C 1 ATOM 4440 O O . ALA B 1 245 ? -22.153 21.502 75.818 1.00 45.73 ? 245 ALA B O 1 ATOM 4441 C CB . ALA B 1 245 ? -20.328 18.966 75.752 1.00 44.60 ? 245 ALA B CB 1 ATOM 4442 N N . LEU B 1 246 ? -20.479 22.015 74.418 1.00 44.74 ? 246 LEU B N 1 ATOM 4443 C CA . LEU B 1 246 ? -20.590 23.448 74.715 1.00 45.00 ? 246 LEU B CA 1 ATOM 4444 C C . LEU B 1 246 ? -21.622 24.144 73.833 1.00 46.75 ? 246 LEU B C 1 ATOM 4445 O O . LEU B 1 246 ? -22.118 25.219 74.176 1.00 49.73 ? 246 LEU B O 1 ATOM 4446 C CB . LEU B 1 246 ? -19.222 24.157 74.637 1.00 44.43 ? 246 LEU B CB 1 ATOM 4447 C CG . LEU B 1 246 ? -18.114 23.681 75.599 1.00 43.69 ? 246 LEU B CG 1 ATOM 4448 C CD1 . LEU B 1 246 ? -16.745 24.297 75.270 1.00 40.63 ? 246 LEU B CD1 1 ATOM 4449 C CD2 . LEU B 1 246 ? -18.492 23.919 77.067 1.00 46.45 ? 246 LEU B CD2 1 ATOM 4450 N N . GLY B 1 247 ? -21.952 23.521 72.703 1.00 47.41 ? 247 GLY B N 1 ATOM 4451 C CA . GLY B 1 247 ? -22.786 24.154 71.682 1.00 46.51 ? 247 GLY B CA 1 ATOM 4452 C C . GLY B 1 247 ? -22.005 25.057 70.742 1.00 46.31 ? 247 GLY B C 1 ATOM 4453 O O . GLY B 1 247 ? -22.590 25.855 70.016 1.00 46.99 ? 247 GLY B O 1 ATOM 4454 N N . ALA B 1 248 ? -20.678 24.931 70.759 1.00 45.48 ? 248 ALA B N 1 ATOM 4455 C CA . ALA B 1 248 ? -19.812 25.703 69.885 1.00 44.00 ? 248 ALA B CA 1 ATOM 4456 C C . ALA B 1 248 ? -19.812 25.080 68.487 1.00 44.94 ? 248 ALA B C 1 ATOM 4457 O O . ALA B 1 248 ? -19.934 23.853 68.355 1.00 44.39 ? 248 ALA B O 1 ATOM 4458 C CB . ALA B 1 248 ? -18.416 25.748 70.453 1.00 42.65 ? 248 ALA B CB 1 ATOM 4459 N N . LYS B 1 249 ? -19.696 25.923 67.455 1.00 44.78 ? 249 LYS B N 1 ATOM 4460 C CA . LYS B 1 249 ? -19.722 25.466 66.061 1.00 45.37 ? 249 LYS B CA 1 ATOM 4461 C C . LYS B 1 249 ? -18.344 25.559 65.421 1.00 46.04 ? 249 LYS B C 1 ATOM 4462 O O . LYS B 1 249 ? -17.638 26.560 65.583 1.00 46.95 ? 249 LYS B O 1 ATOM 4463 C CB . LYS B 1 249 ? -20.764 26.240 65.239 1.00 45.23 ? 249 LYS B CB 1 ATOM 4464 C CG . LYS B 1 249 ? -21.105 25.583 63.877 1.00 48.89 ? 249 LYS B CG 1 ATOM 4465 C CD . LYS B 1 249 ? -22.084 26.412 63.006 1.00 48.29 ? 249 LYS B CD 1 ATOM 4466 C CE . LYS B 1 249 ? -23.544 26.018 63.254 1.00 51.43 ? 249 LYS B CE 1 ATOM 4467 N NZ . LYS B 1 249 ? -24.553 26.908 62.576 1.00 51.40 ? 249 LYS B NZ 1 ATOM 4468 N N . LYS B 1 250 ? -17.962 24.506 64.702 1.00 46.62 ? 250 LYS B N 1 ATOM 4469 C CA . LYS B 1 250 ? -16.672 24.443 64.009 1.00 47.55 ? 250 LYS B CA 1 ATOM 4470 C C . LYS B 1 250 ? -16.574 25.392 62.803 1.00 49.56 ? 250 LYS B C 1 ATOM 4471 O O . LYS B 1 250 ? -17.443 25.398 61.932 1.00 49.12 ? 250 LYS B O 1 ATOM 4472 C CB . LYS B 1 250 ? -16.363 22.997 63.600 1.00 46.61 ? 250 LYS B CB 1 ATOM 4473 C CG . LYS B 1 250 ? -15.220 22.817 62.617 1.00 46.27 ? 250 LYS B CG 1 ATOM 4474 C CD . LYS B 1 250 ? -13.909 22.564 63.310 1.00 45.47 ? 250 LYS B CD 1 ATOM 4475 C CE . LYS B 1 250 ? -12.880 22.032 62.335 1.00 46.62 ? 250 LYS B CE 1 ATOM 4476 N NZ . LYS B 1 250 ? -11.584 21.836 63.024 1.00 47.96 ? 250 LYS B NZ 1 ATOM 4477 N N . ARG B 1 251 ? -15.506 26.189 62.786 1.00 50.94 ? 251 ARG B N 1 ATOM 4478 C CA . ARG B 1 251 ? -15.118 27.014 61.649 1.00 52.31 ? 251 ARG B CA 1 ATOM 4479 C C . ARG B 1 251 ? -13.822 26.449 61.083 1.00 53.88 ? 251 ARG B C 1 ATOM 4480 O O . ARG B 1 251 ? -13.303 25.441 61.580 1.00 53.80 ? 251 ARG B O 1 ATOM 4481 C CB . ARG B 1 251 ? -14.829 28.432 62.103 1.00 53.81 ? 251 ARG B CB 1 ATOM 4482 C CG . ARG B 1 251 ? -15.853 29.493 61.819 1.00 54.38 ? 251 ARG B CG 1 ATOM 4483 C CD . ARG B 1 251 ? -15.152 30.833 61.676 1.00 55.79 ? 251 ARG B CD 1 ATOM 4484 N NE . ARG B 1 251 ? -15.842 31.970 62.277 1.00 56.27 ? 251 ARG B NE 1 ATOM 4485 C CZ . ARG B 1 251 ? -15.220 32.948 62.931 1.00 56.72 ? 251 ARG B CZ 1 ATOM 4486 N NH1 . ARG B 1 251 ? -13.904 32.914 63.107 1.00 54.70 ? 251 ARG B NH1 1 ATOM 4487 N NH2 . ARG B 1 251 ? -15.916 33.953 63.439 1.00 58.76 ? 251 ARG B NH2 1 ATOM 4488 N N . LEU B 1 252 ? -13.285 27.117 60.065 1.00 55.04 ? 252 LEU B N 1 ATOM 4489 C CA . LEU B 1 252 ? -12.053 26.680 59.416 1.00 56.79 ? 252 LEU B CA 1 ATOM 4490 C C . LEU B 1 252 ? -10.893 26.562 60.399 1.00 57.69 ? 252 LEU B C 1 ATOM 4491 O O . LEU B 1 252 ? -10.182 25.564 60.399 1.00 58.67 ? 252 LEU B O 1 ATOM 4492 C CB . LEU B 1 252 ? -11.669 27.629 58.272 1.00 57.61 ? 252 LEU B CB 1 ATOM 4493 C CG . LEU B 1 252 ? -11.766 27.191 56.807 1.00 58.40 ? 252 LEU B CG 1 ATOM 4494 C CD1 . LEU B 1 252 ? -11.346 28.345 55.897 1.00 58.55 ? 252 LEU B CD1 1 ATOM 4495 C CD2 . LEU B 1 252 ? -10.899 25.966 56.532 1.00 58.43 ? 252 LEU B CD2 1 ATOM 4496 N N . PHE B 1 253 ? -10.715 27.579 61.241 1.00 58.61 ? 253 PHE B N 1 ATOM 4497 C CA . PHE B 1 253 ? -9.534 27.665 62.100 1.00 58.86 ? 253 PHE B CA 1 ATOM 4498 C C . PHE B 1 253 ? -9.838 27.799 63.610 1.00 57.54 ? 253 PHE B C 1 ATOM 4499 O O . PHE B 1 253 ? -8.922 28.028 64.404 1.00 58.48 ? 253 PHE B O 1 ATOM 4500 C CB . PHE B 1 253 ? -8.629 28.826 61.634 1.00 61.64 ? 253 PHE B CB 1 ATOM 4501 C CG . PHE B 1 253 ? -8.291 28.804 60.154 1.00 62.33 ? 253 PHE B CG 1 ATOM 4502 C CD1 . PHE B 1 253 ? -7.492 27.785 59.611 1.00 63.20 ? 253 PHE B CD1 1 ATOM 4503 C CD2 . PHE B 1 253 ? -8.743 29.824 59.312 1.00 62.41 ? 253 PHE B CD2 1 ATOM 4504 C CE1 . PHE B 1 253 ? -7.173 27.775 58.242 1.00 62.87 ? 253 PHE B CE1 1 ATOM 4505 C CE2 . PHE B 1 253 ? -8.433 29.829 57.945 1.00 61.51 ? 253 PHE B CE2 1 ATOM 4506 C CZ . PHE B 1 253 ? -7.648 28.806 57.410 1.00 62.54 ? 253 PHE B CZ 1 ATOM 4507 N N . ASP B 1 254 ? -11.107 27.647 63.998 1.00 53.49 ? 254 ASP B N 1 ATOM 4508 C CA . ASP B 1 254 ? -11.533 27.806 65.390 1.00 51.19 ? 254 ASP B CA 1 ATOM 4509 C C . ASP B 1 254 ? -12.985 27.357 65.595 1.00 48.01 ? 254 ASP B C 1 ATOM 4510 O O . ASP B 1 254 ? -13.594 26.809 64.676 1.00 47.21 ? 254 ASP B O 1 ATOM 4511 C CB . ASP B 1 254 ? -11.359 29.268 65.838 1.00 51.89 ? 254 ASP B CB 1 ATOM 4512 C CG . ASP B 1 254 ? -12.199 30.221 65.034 1.00 52.81 ? 254 ASP B CG 1 ATOM 4513 O OD1 . ASP B 1 254 ? -12.523 29.893 63.878 1.00 54.67 ? 254 ASP B OD1 1 ATOM 4514 O OD2 . ASP B 1 254 ? -12.590 31.320 65.465 1.00 54.05 ? 254 ASP B OD2 1 ATOM 4515 N N . TYR B 1 255 ? -13.519 27.596 66.802 1.00 44.44 ? 255 TYR B N 1 ATOM 4516 C CA . TYR B 1 255 ? -14.909 27.312 67.159 1.00 39.93 ? 255 TYR B CA 1 ATOM 4517 C C . TYR B 1 255 ? -15.561 28.584 67.661 1.00 40.74 ? 255 TYR B C 1 ATOM 4518 O O . TYR B 1 255 ? -14.913 29.391 68.330 1.00 43.70 ? 255 TYR B O 1 ATOM 4519 C CB . TYR B 1 255 ? -14.990 26.239 68.249 1.00 39.74 ? 255 TYR B CB 1 ATOM 4520 C CG . TYR B 1 255 ? -14.650 24.843 67.781 1.00 38.54 ? 255 TYR B CG 1 ATOM 4521 C CD1 . TYR B 1 255 ? -15.653 23.928 67.467 1.00 40.13 ? 255 TYR B CD1 1 ATOM 4522 C CD2 . TYR B 1 255 ? -13.325 24.437 67.646 1.00 37.32 ? 255 TYR B CD2 1 ATOM 4523 C CE1 . TYR B 1 255 ? -15.339 22.626 67.034 1.00 39.25 ? 255 TYR B CE1 1 ATOM 4524 C CE2 . TYR B 1 255 ? -12.999 23.166 67.215 1.00 37.54 ? 255 TYR B CE2 1 ATOM 4525 C CZ . TYR B 1 255 ? -14.007 22.263 66.916 1.00 39.50 ? 255 TYR B CZ 1 ATOM 4526 O OH . TYR B 1 255 ? -13.678 21.003 66.481 1.00 41.71 ? 255 TYR B OH 1 ATOM 4527 N N . VAL B 1 256 ? -16.837 28.773 67.349 1.00 40.11 ? 256 VAL B N 1 ATOM 4528 C CA . VAL B 1 256 ? -17.535 30.009 67.720 1.00 42.01 ? 256 VAL B CA 1 ATOM 4529 C C . VAL B 1 256 ? -18.890 29.771 68.372 1.00 42.06 ? 256 VAL B C 1 ATOM 4530 O O . VAL B 1 256 ? -19.451 28.678 68.269 1.00 42.40 ? 256 VAL B O 1 ATOM 4531 C CB . VAL B 1 256 ? -17.696 31.001 66.509 1.00 42.68 ? 256 VAL B CB 1 ATOM 4532 C CG1 . VAL B 1 256 ? -16.371 31.638 66.140 1.00 43.21 ? 256 VAL B CG1 1 ATOM 4533 C CG2 . VAL B 1 256 ? -18.321 30.314 65.286 1.00 43.62 ? 256 VAL B CG2 1 ATOM 4534 N N . VAL B 1 257 ? -19.388 30.795 69.066 1.00 43.43 ? 257 VAL B N 1 ATOM 4535 C CA . VAL B 1 257 ? -20.795 30.886 69.476 1.00 45.98 ? 257 VAL B CA 1 ATOM 4536 C C . VAL B 1 257 ? -21.288 32.317 69.273 1.00 48.43 ? 257 VAL B C 1 ATOM 4537 O O . VAL B 1 257 ? -20.489 33.209 68.977 1.00 47.55 ? 257 VAL B O 1 ATOM 4538 C CB . VAL B 1 257 ? -21.038 30.486 70.947 1.00 47.03 ? 257 VAL B CB 1 ATOM 4539 C CG1 . VAL B 1 257 ? -20.862 28.983 71.153 1.00 48.17 ? 257 VAL B CG1 1 ATOM 4540 C CG2 . VAL B 1 257 ? -20.134 31.250 71.862 1.00 47.45 ? 257 VAL B CG2 1 ATOM 4541 N N . LYS B 1 258 ? -22.598 32.533 69.414 1.00 48.69 ? 258 LYS B N 1 ATOM 4542 C CA . LYS B 1 258 ? -23.164 33.875 69.309 1.00 49.93 ? 258 LYS B CA 1 ATOM 4543 C C . LYS B 1 258 ? -22.806 34.622 70.576 1.00 49.38 ? 258 LYS B C 1 ATOM 4544 O O . LYS B 1 258 ? -22.883 34.059 71.668 1.00 50.69 ? 258 LYS B O 1 ATOM 4545 C CB . LYS B 1 258 ? -24.683 33.836 69.106 1.00 51.41 ? 258 LYS B CB 1 ATOM 4546 C CG . LYS B 1 258 ? -25.093 33.354 67.721 1.00 54.42 ? 258 LYS B CG 1 ATOM 4547 C CD . LYS B 1 258 ? -26.555 32.908 67.654 1.00 56.49 ? 258 LYS B CD 1 ATOM 4548 C CE . LYS B 1 258 ? -26.724 31.812 66.585 1.00 58.48 ? 258 LYS B CE 1 ATOM 4549 N NZ . LYS B 1 258 ? -28.149 31.596 66.151 1.00 59.92 ? 258 LYS B NZ 1 ATOM 4550 N N . CYS B 1 259 ? -22.420 35.886 70.425 1.00 48.76 ? 259 CYS B N 1 ATOM 4551 C CA . CYS B 1 259 ? -21.813 36.648 71.509 1.00 50.29 ? 259 CYS B CA 1 ATOM 4552 C C . CYS B 1 259 ? -22.675 36.795 72.738 1.00 51.69 ? 259 CYS B C 1 ATOM 4553 O O . CYS B 1 259 ? -22.164 36.734 73.858 1.00 52.32 ? 259 CYS B O 1 ATOM 4554 C CB . CYS B 1 259 ? -21.397 38.020 71.020 1.00 50.63 ? 259 CYS B CB 1 ATOM 4555 S SG . CYS B 1 259 ? -20.141 37.866 69.766 1.00 52.18 ? 259 CYS B SG 1 ATOM 4556 N N . ASN B 1 260 ? -23.971 36.997 72.529 1.00 51.38 ? 260 ASN B N 1 ATOM 4557 C CA . ASN B 1 260 ? -24.926 37.074 73.634 1.00 53.30 ? 260 ASN B CA 1 ATOM 4558 C C . ASN B 1 260 ? -25.081 35.759 74.433 1.00 52.25 ? 260 ASN B C 1 ATOM 4559 O O . ASN B 1 260 ? -25.496 35.775 75.598 1.00 51.58 ? 260 ASN B O 1 ATOM 4560 C CB . ASN B 1 260 ? -26.297 37.552 73.117 1.00 53.51 ? 260 ASN B CB 1 ATOM 4561 C CG . ASN B 1 260 ? -27.029 36.483 72.318 1.00 53.65 ? 260 ASN B CG 1 ATOM 4562 O OD1 . ASN B 1 260 ? -26.496 35.942 71.348 1.00 52.82 ? 260 ASN B OD1 1 ATOM 4563 N ND2 . ASN B 1 260 ? -28.267 36.183 72.721 1.00 54.28 ? 260 ASN B ND2 1 ATOM 4564 N N . GLU B 1 261 ? -24.752 34.635 73.800 1.00 50.99 ? 261 GLU B N 1 ATOM 4565 C CA . GLU B 1 261 ? -24.911 33.323 74.425 1.00 51.82 ? 261 GLU B CA 1 ATOM 4566 C C . GLU B 1 261 ? -23.630 32.855 75.141 1.00 51.40 ? 261 GLU B C 1 ATOM 4567 O O . GLU B 1 261 ? -23.656 31.890 75.915 1.00 50.99 ? 261 GLU B O 1 ATOM 4568 C CB . GLU B 1 261 ? -25.402 32.285 73.399 1.00 52.85 ? 261 GLU B CB 1 ATOM 4569 C CG . GLU B 1 261 ? -26.620 32.753 72.607 1.00 54.43 ? 261 GLU B CG 1 ATOM 4570 C CD . GLU B 1 261 ? -27.510 31.632 72.083 1.00 56.72 ? 261 GLU B CD 1 ATOM 4571 O OE1 . GLU B 1 261 ? -28.618 31.956 71.591 1.00 56.50 ? 261 GLU B OE1 1 ATOM 4572 O OE2 . GLU B 1 261 ? -27.127 30.440 72.159 1.00 56.28 ? 261 GLU B OE2 1 ATOM 4573 N N . GLY B 1 262 ? -22.530 33.563 74.888 1.00 50.91 ? 262 GLY B N 1 ATOM 4574 C CA . GLY B 1 262 ? -21.250 33.330 75.552 1.00 50.98 ? 262 GLY B CA 1 ATOM 4575 C C . GLY B 1 262 ? -21.352 33.198 77.064 1.00 51.89 ? 262 GLY B C 1 ATOM 4576 O O . GLY B 1 262 ? -20.993 32.143 77.612 1.00 51.03 ? 262 GLY B O 1 ATOM 4577 N N . PRO B 1 263 ? -21.841 34.254 77.735 1.00 51.75 ? 263 PRO B N 1 ATOM 4578 C CA . PRO B 1 263 ? -21.956 34.287 79.196 1.00 51.45 ? 263 PRO B CA 1 ATOM 4579 C C . PRO B 1 263 ? -22.774 33.157 79.828 1.00 51.85 ? 263 PRO B C 1 ATOM 4580 O O . PRO B 1 263 ? -22.654 32.923 81.030 1.00 53.93 ? 263 PRO B O 1 ATOM 4581 C CB . PRO B 1 263 ? -22.641 35.637 79.456 1.00 50.65 ? 263 PRO B CB 1 ATOM 4582 C CG . PRO B 1 263 ? -22.253 36.465 78.319 1.00 51.28 ? 263 PRO B CG 1 ATOM 4583 C CD . PRO B 1 263 ? -22.289 35.530 77.143 1.00 51.80 ? 263 PRO B CD 1 ATOM 4584 N N . THR B 1 264 ? -23.586 32.459 79.041 1.00 51.04 ? 264 THR B N 1 ATOM 4585 C CA . THR B 1 264 ? -24.438 31.408 79.596 1.00 50.09 ? 264 THR B CA 1 ATOM 4586 C C . THR B 1 264 ? -23.832 30.018 79.430 1.00 47.53 ? 264 THR B C 1 ATOM 4587 O O . THR B 1 264 ? -24.343 29.055 79.983 1.00 48.08 ? 264 THR B O 1 ATOM 4588 C CB . THR B 1 264 ? -25.881 31.460 79.003 1.00 50.18 ? 264 THR B CB 1 ATOM 4589 O OG1 . THR B 1 264 ? -25.882 30.955 77.660 1.00 52.07 ? 264 THR B OG1 1 ATOM 4590 C CG2 . THR B 1 264 ? -26.378 32.898 78.862 1.00 50.58 ? 264 THR B CG2 1 ATOM 4591 N N . LEU B 1 265 ? -22.748 29.918 78.664 1.00 47.04 ? 265 LEU B N 1 ATOM 4592 C CA . LEU B 1 265 ? -22.058 28.635 78.451 1.00 44.65 ? 265 LEU B CA 1 ATOM 4593 C C . LEU B 1 265 ? -21.543 28.052 79.769 1.00 42.65 ? 265 LEU B C 1 ATOM 4594 O O . LEU B 1 265 ? -21.256 28.798 80.703 1.00 43.31 ? 265 LEU B O 1 ATOM 4595 C CB . LEU B 1 265 ? -20.934 28.776 77.404 1.00 44.72 ? 265 LEU B CB 1 ATOM 4596 C CG . LEU B 1 265 ? -21.153 28.130 76.017 1.00 44.38 ? 265 LEU B CG 1 ATOM 4597 C CD1 . LEU B 1 265 ? -22.303 28.723 75.224 1.00 43.21 ? 265 LEU B CD1 1 ATOM 4598 C CD2 . LEU B 1 265 ? -19.873 28.107 75.178 1.00 45.19 ? 265 LEU B CD2 1 ATOM 4599 N N . PRO B 1 266 ? -21.456 26.729 79.865 1.00 42.52 ? 266 PRO B N 1 ATOM 4600 C CA . PRO B 1 266 ? -21.029 26.079 81.102 1.00 43.39 ? 266 PRO B CA 1 ATOM 4601 C C . PRO B 1 266 ? -19.548 26.256 81.443 1.00 43.14 ? 266 PRO B C 1 ATOM 4602 O O . PRO B 1 266 ? -18.740 26.528 80.552 1.00 44.71 ? 266 PRO B O 1 ATOM 4603 C CB . PRO B 1 266 ? -21.325 24.598 80.838 1.00 43.91 ? 266 PRO B CB 1 ATOM 4604 C CG . PRO B 1 266 ? -21.319 24.461 79.403 1.00 43.14 ? 266 PRO B CG 1 ATOM 4605 C CD . PRO B 1 266 ? -21.790 25.748 78.819 1.00 42.69 ? 266 PRO B CD 1 ATOM 4606 N N . ASP B 1 267 ? -19.228 26.114 82.732 1.00 42.12 ? 267 ASP B N 1 ATOM 4607 C CA . ASP B 1 267 ? -17.855 26.015 83.234 1.00 42.71 ? 267 ASP B CA 1 ATOM 4608 C C . ASP B 1 267 ? -17.176 24.719 82.755 1.00 41.91 ? 267 ASP B C 1 ATOM 4609 O O . ASP B 1 267 ? -17.811 23.664 82.697 1.00 40.92 ? 267 ASP B O 1 ATOM 4610 C CB . ASP B 1 267 ? -17.852 26.045 84.774 1.00 43.44 ? 267 ASP B CB 1 ATOM 4611 C CG . ASP B 1 267 ? -18.369 27.369 85.364 1.00 46.54 ? 267 ASP B CG 1 ATOM 4612 O OD1 . ASP B 1 267 ? -18.604 28.355 84.638 1.00 48.22 ? 267 ASP B OD1 1 ATOM 4613 O OD2 . ASP B 1 267 ? -18.580 27.518 86.585 1.00 49.39 ? 267 ASP B OD2 1 ATOM 4614 N N . ILE B 1 268 ? -15.895 24.799 82.390 1.00 40.62 ? 268 ILE B N 1 ATOM 4615 C CA . ILE B 1 268 ? -15.117 23.595 82.099 1.00 39.13 ? 268 ILE B CA 1 ATOM 4616 C C . ILE B 1 268 ? -14.150 23.341 83.267 1.00 38.21 ? 268 ILE B C 1 ATOM 4617 O O . ILE B 1 268 ? -13.502 24.285 83.748 1.00 37.41 ? 268 ILE B O 1 ATOM 4618 C CB . ILE B 1 268 ? -14.345 23.703 80.745 1.00 39.20 ? 268 ILE B CB 1 ATOM 4619 C CG1 . ILE B 1 268 ? -15.251 24.221 79.627 1.00 41.40 ? 268 ILE B CG1 1 ATOM 4620 C CG2 . ILE B 1 268 ? -13.819 22.333 80.339 1.00 39.69 ? 268 ILE B CG2 1 ATOM 4621 C CD1 . ILE B 1 268 ? -14.539 24.431 78.288 1.00 40.54 ? 268 ILE B CD1 1 ATOM 4622 N N . SER B 1 269 ? -14.060 22.086 83.728 1.00 36.55 ? 269 SER B N 1 ATOM 4623 C CA . SER B 1 269 ? -13.197 21.747 84.884 1.00 33.99 ? 269 SER B CA 1 ATOM 4624 C C . SER B 1 269 ? -12.111 20.774 84.511 1.00 32.00 ? 269 SER B C 1 ATOM 4625 O O . SER B 1 269 ? -12.371 19.811 83.800 1.00 32.02 ? 269 SER B O 1 ATOM 4626 C CB . SER B 1 269 ? -14.026 21.132 86.025 1.00 35.35 ? 269 SER B CB 1 ATOM 4627 O OG . SER B 1 269 ? -14.602 22.114 86.855 1.00 39.28 ? 269 SER B OG 1 ATOM 4628 N N . PHE B 1 270 ? -10.897 20.996 85.022 1.00 32.98 ? 270 PHE B N 1 ATOM 4629 C CA . PHE B 1 270 ? -9.782 20.081 84.776 1.00 31.13 ? 270 PHE B CA 1 ATOM 4630 C C . PHE B 1 270 ? -9.363 19.411 86.089 1.00 32.35 ? 270 PHE B C 1 ATOM 4631 O O . PHE B 1 270 ? -8.980 20.081 87.042 1.00 32.58 ? 270 PHE B O 1 ATOM 4632 C CB . PHE B 1 270 ? -8.615 20.819 84.080 1.00 33.21 ? 270 PHE B CB 1 ATOM 4633 C CG . PHE B 1 270 ? -8.994 21.404 82.736 1.00 34.66 ? 270 PHE B CG 1 ATOM 4634 C CD1 . PHE B 1 270 ? -8.870 20.652 81.566 1.00 34.04 ? 270 PHE B CD1 1 ATOM 4635 C CD2 . PHE B 1 270 ? -9.523 22.691 82.650 1.00 34.87 ? 270 PHE B CD2 1 ATOM 4636 C CE1 . PHE B 1 270 ? -9.251 21.188 80.329 1.00 35.63 ? 270 PHE B CE1 1 ATOM 4637 C CE2 . PHE B 1 270 ? -9.909 23.228 81.433 1.00 33.44 ? 270 PHE B CE2 1 ATOM 4638 C CZ . PHE B 1 270 ? -9.773 22.472 80.263 1.00 33.99 ? 270 PHE B CZ 1 ATOM 4639 N N . HIS B 1 271 ? -9.465 18.089 86.158 1.00 32.71 ? 271 HIS B N 1 ATOM 4640 C CA . HIS B 1 271 ? -9.166 17.401 87.416 1.00 32.96 ? 271 HIS B CA 1 ATOM 4641 C C . HIS B 1 271 ? -7.687 17.057 87.475 1.00 31.12 ? 271 HIS B C 1 ATOM 4642 O O . HIS B 1 271 ? -7.235 16.078 86.881 1.00 30.75 ? 271 HIS B O 1 ATOM 4643 C CB . HIS B 1 271 ? -10.038 16.140 87.595 1.00 36.56 ? 271 HIS B CB 1 ATOM 4644 C CG . HIS B 1 271 ? -10.051 15.598 88.997 1.00 41.46 ? 271 HIS B CG 1 ATOM 4645 N ND1 . HIS B 1 271 ? -10.166 14.253 89.278 1.00 45.61 ? 271 HIS B ND1 1 ATOM 4646 C CD2 . HIS B 1 271 ? -9.965 16.223 90.198 1.00 43.97 ? 271 HIS B CD2 1 ATOM 4647 C CE1 . HIS B 1 271 ? -10.158 14.073 90.588 1.00 46.51 ? 271 HIS B CE1 1 ATOM 4648 N NE2 . HIS B 1 271 ? -10.030 15.253 91.169 1.00 45.65 ? 271 HIS B NE2 1 ATOM 4649 N N . LEU B 1 272 ? -6.938 17.879 88.195 1.00 31.75 ? 272 LEU B N 1 ATOM 4650 C CA . LEU B 1 272 ? -5.487 17.725 88.309 1.00 31.32 ? 272 LEU B CA 1 ATOM 4651 C C . LEU B 1 272 ? -5.090 17.564 89.767 1.00 31.46 ? 272 LEU B C 1 ATOM 4652 O O . LEU B 1 272 ? -5.406 18.419 90.609 1.00 30.53 ? 272 LEU B O 1 ATOM 4653 C CB . LEU B 1 272 ? -4.742 18.927 87.664 1.00 32.92 ? 272 LEU B CB 1 ATOM 4654 C CG . LEU B 1 272 ? -5.123 19.351 86.233 1.00 32.26 ? 272 LEU B CG 1 ATOM 4655 C CD1 . LEU B 1 272 ? -4.651 20.771 85.958 1.00 33.00 ? 272 LEU B CD1 1 ATOM 4656 C CD2 . LEU B 1 272 ? -4.564 18.391 85.178 1.00 34.42 ? 272 LEU B CD2 1 ATOM 4657 N N . GLY B 1 273 ? -4.397 16.465 90.059 1.00 30.25 ? 273 GLY B N 1 ATOM 4658 C CA . GLY B 1 273 ? -3.954 16.157 91.422 1.00 36.39 ? 273 GLY B CA 1 ATOM 4659 C C . GLY B 1 273 ? -5.047 16.238 92.488 1.00 38.94 ? 273 GLY B C 1 ATOM 4660 O O . GLY B 1 273 ? -4.869 16.877 93.528 1.00 36.47 ? 273 GLY B O 1 ATOM 4661 N N . GLY B 1 274 ? -6.193 15.611 92.221 1.00 41.16 ? 274 GLY B N 1 ATOM 4662 C CA . GLY B 1 274 ? -7.265 15.554 93.214 1.00 43.53 ? 274 GLY B CA 1 ATOM 4663 C C . GLY B 1 274 ? -8.059 16.838 93.420 1.00 46.04 ? 274 GLY B C 1 ATOM 4664 O O . GLY B 1 274 ? -9.143 16.791 94.027 1.00 47.68 ? 274 GLY B O 1 ATOM 4665 N N . LYS B 1 275 ? -7.525 17.971 92.926 1.00 45.15 ? 275 LYS B N 1 ATOM 4666 C CA . LYS B 1 275 ? -8.216 19.274 92.927 1.00 42.70 ? 275 LYS B CA 1 ATOM 4667 C C . LYS B 1 275 ? -8.893 19.506 91.571 1.00 41.44 ? 275 LYS B C 1 ATOM 4668 O O . LYS B 1 275 ? -8.458 18.939 90.579 1.00 41.85 ? 275 LYS B O 1 ATOM 4669 C CB . LYS B 1 275 ? -7.221 20.398 93.202 1.00 42.59 ? 275 LYS B CB 1 ATOM 4670 C CG . LYS B 1 275 ? -7.846 21.671 93.760 1.00 45.56 ? 275 LYS B CG 1 ATOM 4671 C CD . LYS B 1 275 ? -7.225 22.972 93.212 1.00 44.57 ? 275 LYS B CD 1 ATOM 4672 C CE . LYS B 1 275 ? -8.252 24.106 93.281 1.00 46.94 ? 275 LYS B CE 1 ATOM 4673 N NZ . LYS B 1 275 ? -8.111 25.284 92.322 1.00 45.70 ? 275 LYS B NZ 1 ATOM 4674 N N . GLU B 1 276 ? -9.943 20.334 91.521 1.00 38.24 ? 276 GLU B N 1 ATOM 4675 C CA . GLU B 1 276 ? -10.607 20.674 90.252 1.00 34.64 ? 276 GLU B CA 1 ATOM 4676 C C . GLU B 1 276 ? -10.288 22.127 89.843 1.00 34.30 ? 276 GLU B C 1 ATOM 4677 O O . GLU B 1 276 ? -10.479 23.078 90.632 1.00 35.15 ? 276 GLU B O 1 ATOM 4678 C CB . GLU B 1 276 ? -12.121 20.480 90.337 1.00 38.84 ? 276 GLU B CB 1 ATOM 4679 C CG . GLU B 1 276 ? -12.615 19.035 90.431 1.00 40.69 ? 276 GLU B CG 1 ATOM 4680 C CD . GLU B 1 276 ? -12.967 18.414 89.095 1.00 44.21 ? 276 GLU B CD 1 ATOM 4681 O OE1 . GLU B 1 276 ? -12.654 18.998 88.034 1.00 45.70 ? 276 GLU B OE1 1 ATOM 4682 O OE2 . GLU B 1 276 ? -13.551 17.310 89.093 1.00 46.27 ? 276 GLU B OE2 1 ATOM 4683 N N . TYR B 1 277 ? -9.800 22.301 88.614 1.00 30.82 ? 277 TYR B N 1 ATOM 4684 C CA . TYR B 1 277 ? -9.435 23.636 88.095 1.00 28.87 ? 277 TYR B CA 1 ATOM 4685 C C . TYR B 1 277 ? -10.460 24.061 87.054 1.00 27.90 ? 277 TYR B C 1 ATOM 4686 O O . TYR B 1 277 ? -10.542 23.481 85.991 1.00 26.44 ? 277 TYR B O 1 ATOM 4687 C CB . TYR B 1 277 ? -8.007 23.622 87.519 1.00 29.67 ? 277 TYR B CB 1 ATOM 4688 C CG . TYR B 1 277 ? -6.987 23.319 88.592 1.00 26.92 ? 277 TYR B CG 1 ATOM 4689 C CD1 . TYR B 1 277 ? -6.388 24.350 89.285 1.00 28.77 ? 277 TYR B CD1 1 ATOM 4690 C CD2 . TYR B 1 277 ? -6.681 22.008 88.958 1.00 26.58 ? 277 TYR B CD2 1 ATOM 4691 C CE1 . TYR B 1 277 ? -5.491 24.101 90.288 1.00 28.25 ? 277 TYR B CE1 1 ATOM 4692 C CE2 . TYR B 1 277 ? -5.765 21.737 89.970 1.00 24.77 ? 277 TYR B CE2 1 ATOM 4693 C CZ . TYR B 1 277 ? -5.184 22.795 90.630 1.00 28.00 ? 277 TYR B CZ 1 ATOM 4694 O OH . TYR B 1 277 ? -4.261 22.605 91.633 1.00 30.97 ? 277 TYR B OH 1 ATOM 4695 N N . THR B 1 278 ? -11.256 25.060 87.420 1.00 29.49 ? 278 THR B N 1 ATOM 4696 C CA . THR B 1 278 ? -12.442 25.471 86.685 1.00 30.19 ? 278 THR B CA 1 ATOM 4697 C C . THR B 1 278 ? -12.217 26.763 85.913 1.00 32.12 ? 278 THR B C 1 ATOM 4698 O O . THR B 1 278 ? -11.752 27.767 86.471 1.00 31.99 ? 278 THR B O 1 ATOM 4699 C CB . THR B 1 278 ? -13.601 25.645 87.695 1.00 28.24 ? 278 THR B CB 1 ATOM 4700 O OG1 . THR B 1 278 ? -13.874 24.372 88.278 1.00 30.78 ? 278 THR B OG1 1 ATOM 4701 C CG2 . THR B 1 278 ? -14.950 26.028 86.981 1.00 29.01 ? 278 THR B CG2 1 ATOM 4702 N N . LEU B 1 279 ? -12.547 26.726 84.625 1.00 34.19 ? 279 LEU B N 1 ATOM 4703 C CA . LEU B 1 279 ? -12.607 27.946 83.821 1.00 33.72 ? 279 LEU B CA 1 ATOM 4704 C C . LEU B 1 279 ? -14.071 28.214 83.506 1.00 35.02 ? 279 LEU B C 1 ATOM 4705 O O . LEU B 1 279 ? -14.768 27.349 82.988 1.00 32.77 ? 279 LEU B O 1 ATOM 4706 C CB . LEU B 1 279 ? -11.788 27.838 82.521 1.00 32.05 ? 279 LEU B CB 1 ATOM 4707 C CG . LEU B 1 279 ? -10.325 27.371 82.392 1.00 34.51 ? 279 LEU B CG 1 ATOM 4708 C CD1 . LEU B 1 279 ? -9.685 28.185 81.269 1.00 31.49 ? 279 LEU B CD1 1 ATOM 4709 C CD2 . LEU B 1 279 ? -9.467 27.459 83.643 1.00 29.50 ? 279 LEU B CD2 1 ATOM 4710 N N . THR B 1 280 ? -14.537 29.404 83.868 1.00 36.89 ? 280 THR B N 1 ATOM 4711 C CA . THR B 1 280 ? -15.885 29.809 83.532 1.00 39.00 ? 280 THR B CA 1 ATOM 4712 C C . THR B 1 280 ? -15.861 30.329 82.122 1.00 39.17 ? 280 THR B C 1 ATOM 4713 O O . THR B 1 280 ? -14.790 30.592 81.553 1.00 38.43 ? 280 THR B O 1 ATOM 4714 C CB . THR B 1 280 ? -16.401 30.937 84.461 1.00 39.76 ? 280 THR B CB 1 ATOM 4715 O OG1 . THR B 1 280 ? -15.569 32.092 84.310 1.00 40.98 ? 280 THR B OG1 1 ATOM 4716 C CG2 . THR B 1 280 ? -16.278 30.555 85.932 1.00 41.19 ? 280 THR B CG2 1 ATOM 4717 N N . SER B 1 281 ? -17.057 30.500 81.571 1.00 36.77 ? 281 SER B N 1 ATOM 4718 C CA . SER B 1 281 ? -17.248 31.104 80.273 1.00 36.12 ? 281 SER B CA 1 ATOM 4719 C C . SER B 1 281 ? -16.376 32.343 79.999 1.00 35.64 ? 281 SER B C 1 ATOM 4720 O O . SER B 1 281 ? -15.785 32.447 78.932 1.00 35.61 ? 281 SER B O 1 ATOM 4721 C CB . SER B 1 281 ? -18.714 31.467 80.101 1.00 36.92 ? 281 SER B CB 1 ATOM 4722 O OG . SER B 1 281 ? -18.952 31.635 78.732 1.00 42.28 ? 281 SER B OG 1 ATOM 4723 N N . ALA B 1 282 ? -16.310 33.290 80.939 1.00 35.30 ? 282 ALA B N 1 ATOM 4724 C CA . ALA B 1 282 ? -15.508 34.506 80.734 1.00 36.15 ? 282 ALA B CA 1 ATOM 4725 C C . ALA B 1 282 ? -14.010 34.206 80.610 1.00 34.08 ? 282 ALA B C 1 ATOM 4726 O O . ALA B 1 282 ? -13.249 35.035 80.114 1.00 34.93 ? 282 ALA B O 1 ATOM 4727 C CB . ALA B 1 282 ? -15.750 35.507 81.852 1.00 36.76 ? 282 ALA B CB 1 ATOM 4728 N N . ASP B 1 283 ? -13.596 33.022 81.045 1.00 31.24 ? 283 ASP B N 1 ATOM 4729 C CA . ASP B 1 283 ? -12.181 32.643 80.994 1.00 31.62 ? 283 ASP B CA 1 ATOM 4730 C C . ASP B 1 283 ? -11.725 32.036 79.647 1.00 32.35 ? 283 ASP B C 1 ATOM 4731 O O . ASP B 1 283 ? -10.545 32.164 79.272 1.00 30.05 ? 283 ASP B O 1 ATOM 4732 C CB . ASP B 1 283 ? -11.814 31.746 82.200 1.00 31.68 ? 283 ASP B CB 1 ATOM 4733 C CG . ASP B 1 283 ? -12.137 32.409 83.558 1.00 32.56 ? 283 ASP B CG 1 ATOM 4734 O OD1 . ASP B 1 283 ? -11.672 33.547 83.818 1.00 35.46 ? 283 ASP B OD1 1 ATOM 4735 O OD2 . ASP B 1 283 ? -12.827 31.868 84.442 1.00 31.86 ? 283 ASP B OD2 1 ATOM 4736 N N . TYR B 1 284 ? -12.657 31.410 78.910 1.00 30.94 ? 284 TYR B N 1 ATOM 4737 C CA . TYR B 1 284 ? -12.324 30.727 77.655 1.00 32.38 ? 284 TYR B CA 1 ATOM 4738 C C . TYR B 1 284 ? -13.108 31.220 76.434 1.00 33.78 ? 284 TYR B C 1 ATOM 4739 O O . TYR B 1 284 ? -12.938 30.692 75.338 1.00 32.69 ? 284 TYR B O 1 ATOM 4740 C CB . TYR B 1 284 ? -12.461 29.203 77.794 1.00 35.79 ? 284 TYR B CB 1 ATOM 4741 C CG . TYR B 1 284 ? -13.883 28.689 77.948 1.00 37.86 ? 284 TYR B CG 1 ATOM 4742 C CD1 . TYR B 1 284 ? -14.706 28.479 76.833 1.00 38.45 ? 284 TYR B CD1 1 ATOM 4743 C CD2 . TYR B 1 284 ? -14.393 28.382 79.204 1.00 38.30 ? 284 TYR B CD2 1 ATOM 4744 C CE1 . TYR B 1 284 ? -16.014 27.999 76.981 1.00 37.17 ? 284 TYR B CE1 1 ATOM 4745 C CE2 . TYR B 1 284 ? -15.697 27.903 79.360 1.00 38.40 ? 284 TYR B CE2 1 ATOM 4746 C CZ . TYR B 1 284 ? -16.493 27.713 78.248 1.00 37.10 ? 284 TYR B CZ 1 ATOM 4747 O OH . TYR B 1 284 ? -17.777 27.242 78.412 1.00 38.35 ? 284 TYR B OH 1 ATOM 4748 N N . VAL B 1 285 ? -13.972 32.212 76.627 1.00 35.25 ? 285 VAL B N 1 ATOM 4749 C CA . VAL B 1 285 ? -14.622 32.884 75.484 1.00 36.64 ? 285 VAL B CA 1 ATOM 4750 C C . VAL B 1 285 ? -14.010 34.276 75.275 1.00 37.50 ? 285 VAL B C 1 ATOM 4751 O O . VAL B 1 285 ? -13.922 35.059 76.220 1.00 35.97 ? 285 VAL B O 1 ATOM 4752 C CB . VAL B 1 285 ? -16.136 33.029 75.689 1.00 36.54 ? 285 VAL B CB 1 ATOM 4753 C CG1 . VAL B 1 285 ? -16.746 33.784 74.534 1.00 39.36 ? 285 VAL B CG1 1 ATOM 4754 C CG2 . VAL B 1 285 ? -16.812 31.655 75.856 1.00 35.38 ? 285 VAL B CG2 1 ATOM 4755 N N . PHE B 1 286 ? -13.565 34.559 74.052 1.00 37.76 ? 286 PHE B N 1 ATOM 4756 C CA . PHE B 1 286 ? -13.206 35.917 73.652 1.00 38.78 ? 286 PHE B CA 1 ATOM 4757 C C . PHE B 1 286 ? -14.476 36.756 73.460 1.00 41.06 ? 286 PHE B C 1 ATOM 4758 O O . PHE B 1 286 ? -15.084 36.750 72.382 1.00 41.94 ? 286 PHE B O 1 ATOM 4759 C CB . PHE B 1 286 ? -12.383 35.895 72.364 1.00 37.11 ? 286 PHE B CB 1 ATOM 4760 C CG . PHE B 1 286 ? -11.009 35.295 72.521 1.00 37.64 ? 286 PHE B CG 1 ATOM 4761 C CD1 . PHE B 1 286 ? -10.020 35.949 73.261 1.00 37.91 ? 286 PHE B CD1 1 ATOM 4762 C CD2 . PHE B 1 286 ? -10.686 34.095 71.887 1.00 39.21 ? 286 PHE B CD2 1 ATOM 4763 C CE1 . PHE B 1 286 ? -8.727 35.389 73.386 1.00 36.29 ? 286 PHE B CE1 1 ATOM 4764 C CE2 . PHE B 1 286 ? -9.402 33.544 71.991 1.00 38.68 ? 286 PHE B CE2 1 ATOM 4765 C CZ . PHE B 1 286 ? -8.427 34.193 72.751 1.00 36.99 ? 286 PHE B CZ 1 ATOM 4766 N N . GLN B 1 287 ? -14.864 37.460 74.521 1.00 43.86 ? 287 GLN B N 1 ATOM 4767 C CA . GLN B 1 287 ? -16.141 38.147 74.616 1.00 48.54 ? 287 GLN B CA 1 ATOM 4768 C C . GLN B 1 287 ? -16.027 39.587 74.093 1.00 53.44 ? 287 GLN B C 1 ATOM 4769 O O . GLN B 1 287 ? -16.347 40.554 74.788 1.00 55.33 ? 287 GLN B O 1 ATOM 4770 C CB . GLN B 1 287 ? -16.614 38.111 76.070 1.00 49.28 ? 287 GLN B CB 1 ATOM 4771 C CG . GLN B 1 287 ? -18.117 38.199 76.271 1.00 51.42 ? 287 GLN B CG 1 ATOM 4772 C CD . GLN B 1 287 ? -18.867 37.008 75.691 1.00 50.93 ? 287 GLN B CD 1 ATOM 4773 O OE1 . GLN B 1 287 ? -19.405 37.099 74.593 1.00 51.17 ? 287 GLN B OE1 1 ATOM 4774 N NE2 . GLN B 1 287 ? -18.892 35.894 76.420 1.00 50.06 ? 287 GLN B NE2 1 ATOM 4775 N N . GLU B 1 288 ? -15.571 39.711 72.851 1.00 57.67 ? 288 GLU B N 1 ATOM 4776 C CA . GLU B 1 288 ? -15.303 41.005 72.231 1.00 62.09 ? 288 GLU B CA 1 ATOM 4777 C C . GLU B 1 288 ? -16.581 41.778 71.882 1.00 64.59 ? 288 GLU B C 1 ATOM 4778 O O . GLU B 1 288 ? -16.535 42.980 71.594 1.00 66.03 ? 288 GLU B O 1 ATOM 4779 C CB . GLU B 1 288 ? -14.394 40.823 71.009 1.00 63.27 ? 288 GLU B CB 1 ATOM 4780 C CG . GLU B 1 288 ? -12.959 41.341 71.188 1.00 66.18 ? 288 GLU B CG 1 ATOM 4781 C CD . GLU B 1 288 ? -12.225 40.821 72.428 1.00 67.34 ? 288 GLU B CD 1 ATOM 4782 O OE1 . GLU B 1 288 ? -11.674 41.667 73.174 1.00 67.40 ? 288 GLU B OE1 1 ATOM 4783 O OE2 . GLU B 1 288 ? -12.173 39.583 72.655 1.00 67.64 ? 288 GLU B OE2 1 ATOM 4784 N N . SER B 1 289 ? -17.715 41.080 71.925 1.00 65.88 ? 289 SER B N 1 ATOM 4785 C CA . SER B 1 289 ? -19.031 41.696 71.777 1.00 66.56 ? 289 SER B CA 1 ATOM 4786 C C . SER B 1 289 ? -20.066 40.985 72.660 1.00 67.27 ? 289 SER B C 1 ATOM 4787 O O . SER B 1 289 ? -19.802 39.918 73.222 1.00 66.16 ? 289 SER B O 1 ATOM 4788 C CB . SER B 1 289 ? -19.459 41.677 70.308 1.00 66.20 ? 289 SER B CB 1 ATOM 4789 O OG . SER B 1 289 ? -20.826 42.015 70.180 1.00 67.18 ? 289 SER B OG 1 ATOM 4790 N N . TYR B 1 290 ? -21.236 41.593 72.795 1.00 68.28 ? 290 TYR B N 1 ATOM 4791 C CA . TYR B 1 290 ? -22.348 40.949 73.479 1.00 70.14 ? 290 TYR B CA 1 ATOM 4792 C C . TYR B 1 290 ? -23.556 40.859 72.560 1.00 70.39 ? 290 TYR B C 1 ATOM 4793 O O . TYR B 1 290 ? -24.600 40.325 72.939 1.00 71.49 ? 290 TYR B O 1 ATOM 4794 C CB . TYR B 1 290 ? -22.701 41.708 74.757 1.00 71.63 ? 290 TYR B CB 1 ATOM 4795 C CG . TYR B 1 290 ? -21.786 41.382 75.908 1.00 72.67 ? 290 TYR B CG 1 ATOM 4796 C CD1 . TYR B 1 290 ? -22.109 40.360 76.810 1.00 72.39 ? 290 TYR B CD1 1 ATOM 4797 C CD2 . TYR B 1 290 ? -20.591 42.081 76.094 1.00 72.39 ? 290 TYR B CD2 1 ATOM 4798 C CE1 . TYR B 1 290 ? -21.266 40.044 77.868 1.00 72.26 ? 290 TYR B CE1 1 ATOM 4799 C CE2 . TYR B 1 290 ? -19.742 41.776 77.152 1.00 73.26 ? 290 TYR B CE2 1 ATOM 4800 C CZ . TYR B 1 290 ? -20.086 40.756 78.035 1.00 72.69 ? 290 TYR B CZ 1 ATOM 4801 O OH . TYR B 1 290 ? -19.250 40.451 79.083 1.00 72.29 ? 290 TYR B OH 1 ATOM 4802 N N . SER B 1 291 ? -23.395 41.385 71.351 1.00 69.99 ? 291 SER B N 1 ATOM 4803 C CA . SER B 1 291 ? -24.473 41.471 70.379 1.00 70.37 ? 291 SER B CA 1 ATOM 4804 C C . SER B 1 291 ? -24.911 40.097 69.879 1.00 70.44 ? 291 SER B C 1 ATOM 4805 O O . SER B 1 291 ? -24.080 39.275 69.475 1.00 71.06 ? 291 SER B O 1 ATOM 4806 C CB . SER B 1 291 ? -24.052 42.360 69.206 1.00 70.16 ? 291 SER B CB 1 ATOM 4807 O OG . SER B 1 291 ? -24.880 42.158 68.074 1.00 70.87 ? 291 SER B OG 1 ATOM 4808 N N . SER B 1 292 ? -26.225 39.868 69.898 1.00 69.05 ? 292 SER B N 1 ATOM 4809 C CA . SER B 1 292 ? -26.818 38.639 69.358 1.00 67.49 ? 292 SER B CA 1 ATOM 4810 C C . SER B 1 292 ? -26.536 38.445 67.864 1.00 65.66 ? 292 SER B C 1 ATOM 4811 O O . SER B 1 292 ? -26.657 37.336 67.340 1.00 64.40 ? 292 SER B O 1 ATOM 4812 C CB . SER B 1 292 ? -28.329 38.566 69.662 1.00 68.10 ? 292 SER B CB 1 ATOM 4813 O OG . SER B 1 292 ? -28.949 39.848 69.661 1.00 67.75 ? 292 SER B OG 1 ATOM 4814 N N . LYS B 1 293 ? -26.124 39.524 67.199 1.00 65.72 ? 293 LYS B N 1 ATOM 4815 C CA . LYS B 1 293 ? -25.865 39.516 65.756 1.00 65.25 ? 293 LYS B CA 1 ATOM 4816 C C . LYS B 1 293 ? -24.467 39.008 65.386 1.00 63.24 ? 293 LYS B C 1 ATOM 4817 O O . LYS B 1 293 ? -24.189 38.768 64.211 1.00 63.28 ? 293 LYS B O 1 ATOM 4818 C CB . LYS B 1 293 ? -26.108 40.920 65.163 1.00 67.19 ? 293 LYS B CB 1 ATOM 4819 C CG . LYS B 1 293 ? -26.414 40.956 63.653 1.00 67.61 ? 293 LYS B CG 1 ATOM 4820 C CD . LYS B 1 293 ? -27.839 40.508 63.335 1.00 68.32 ? 293 LYS B CD 1 ATOM 4821 C CE . LYS B 1 293 ? -28.085 40.428 61.833 1.00 68.47 ? 293 LYS B CE 1 ATOM 4822 N NZ . LYS B 1 293 ? -29.505 40.096 61.514 1.00 68.76 ? 293 LYS B NZ 1 ATOM 4823 N N . LYS B 1 294 ? -23.597 38.824 66.381 1.00 62.24 ? 294 LYS B N 1 ATOM 4824 C CA . LYS B 1 294 ? -22.180 38.497 66.120 1.00 59.86 ? 294 LYS B CA 1 ATOM 4825 C C . LYS B 1 294 ? -21.704 37.128 66.634 1.00 57.40 ? 294 LYS B C 1 ATOM 4826 O O . LYS B 1 294 ? -22.275 36.562 67.578 1.00 55.80 ? 294 LYS B O 1 ATOM 4827 C CB . LYS B 1 294 ? -21.274 39.605 66.663 1.00 60.84 ? 294 LYS B CB 1 ATOM 4828 C CG . LYS B 1 294 ? -21.261 40.850 65.816 1.00 61.64 ? 294 LYS B CG 1 ATOM 4829 C CD . LYS B 1 294 ? -20.898 42.066 66.636 1.00 63.28 ? 294 LYS B CD 1 ATOM 4830 C CE . LYS B 1 294 ? -21.236 43.350 65.887 1.00 65.05 ? 294 LYS B CE 1 ATOM 4831 N NZ . LYS B 1 294 ? -20.478 43.503 64.597 1.00 65.35 ? 294 LYS B NZ 1 ATOM 4832 N N . LEU B 1 295 ? -20.656 36.611 65.989 1.00 55.71 ? 295 LEU B N 1 ATOM 4833 C CA . LEU B 1 295 ? -19.981 35.376 66.406 1.00 54.03 ? 295 LEU B CA 1 ATOM 4834 C C . LEU B 1 295 ? -18.782 35.644 67.332 1.00 53.35 ? 295 LEU B C 1 ATOM 4835 O O . LEU B 1 295 ? -18.027 36.599 67.122 1.00 52.62 ? 295 LEU B O 1 ATOM 4836 C CB . LEU B 1 295 ? -19.520 34.577 65.185 1.00 53.98 ? 295 LEU B CB 1 ATOM 4837 C CG . LEU B 1 295 ? -20.537 33.969 64.210 1.00 54.43 ? 295 LEU B CG 1 ATOM 4838 C CD1 . LEU B 1 295 ? -19.826 33.365 63.007 1.00 54.53 ? 295 LEU B CD1 1 ATOM 4839 C CD2 . LEU B 1 295 ? -21.392 32.914 64.899 1.00 55.11 ? 295 LEU B CD2 1 ATOM 4840 N N . CYS B 1 296 ? -18.613 34.788 68.343 1.00 51.87 ? 296 CYS B N 1 ATOM 4841 C CA . CYS B 1 296 ? -17.511 34.898 69.306 1.00 49.92 ? 296 CYS B CA 1 ATOM 4842 C C . CYS B 1 296 ? -16.721 33.611 69.380 1.00 47.18 ? 296 CYS B C 1 ATOM 4843 O O . CYS B 1 296 ? -17.293 32.532 69.514 1.00 44.87 ? 296 CYS B O 1 ATOM 4844 C CB . CYS B 1 296 ? -18.016 35.257 70.699 1.00 50.96 ? 296 CYS B CB 1 ATOM 4845 S SG . CYS B 1 296 ? -18.048 37.029 70.994 1.00 52.47 ? 296 CYS B SG 1 ATOM 4846 N N . THR B 1 297 ? -15.403 33.752 69.311 1.00 44.49 ? 297 THR B N 1 ATOM 4847 C CA . THR B 1 297 ? -14.496 32.621 69.212 1.00 42.98 ? 297 THR B CA 1 ATOM 4848 C C . THR B 1 297 ? -14.001 32.160 70.586 1.00 41.47 ? 297 THR B C 1 ATOM 4849 O O . THR B 1 297 ? -14.022 32.928 71.553 1.00 42.46 ? 297 THR B O 1 ATOM 4850 C CB . THR B 1 297 ? -13.333 32.983 68.282 1.00 42.60 ? 297 THR B CB 1 ATOM 4851 O OG1 . THR B 1 297 ? -12.531 31.820 68.055 1.00 47.54 ? 297 THR B OG1 1 ATOM 4852 C CG2 . THR B 1 297 ? -12.364 33.941 68.953 1.00 41.96 ? 297 THR B CG2 1 ATOM 4853 N N . LEU B 1 298 ? -13.558 30.907 70.671 1.00 39.01 ? 298 LEU B N 1 ATOM 4854 C CA . LEU B 1 298 ? -13.129 30.330 71.943 1.00 36.62 ? 298 LEU B CA 1 ATOM 4855 C C . LEU B 1 298 ? -11.607 30.166 72.006 1.00 37.29 ? 298 LEU B C 1 ATOM 4856 O O . LEU B 1 298 ? -10.960 29.858 71.002 1.00 38.03 ? 298 LEU B O 1 ATOM 4857 C CB . LEU B 1 298 ? -13.801 28.970 72.219 1.00 36.04 ? 298 LEU B CB 1 ATOM 4858 C CG . LEU B 1 298 ? -15.317 28.690 72.200 1.00 38.27 ? 298 LEU B CG 1 ATOM 4859 C CD1 . LEU B 1 298 ? -15.605 27.290 72.755 1.00 37.72 ? 298 LEU B CD1 1 ATOM 4860 C CD2 . LEU B 1 298 ? -16.102 29.687 72.968 1.00 37.28 ? 298 LEU B CD2 1 ATOM 4861 N N . ALA B 1 299 ? -11.060 30.350 73.206 1.00 36.18 ? 299 ALA B N 1 ATOM 4862 C CA . ALA B 1 299 ? -9.641 30.150 73.487 1.00 31.05 ? 299 ALA B CA 1 ATOM 4863 C C . ALA B 1 299 ? -9.238 28.682 73.670 1.00 32.13 ? 299 ALA B C 1 ATOM 4864 O O . ALA B 1 299 ? -8.319 28.381 74.456 1.00 30.54 ? 299 ALA B O 1 ATOM 4865 C CB . ALA B 1 299 ? -9.260 30.946 74.711 1.00 31.18 ? 299 ALA B CB 1 ATOM 4866 N N . ILE B 1 300 ? -9.891 27.793 72.914 1.00 31.06 ? 300 ILE B N 1 ATOM 4867 C CA . ILE B 1 300 ? -9.654 26.340 72.944 1.00 31.46 ? 300 ILE B CA 1 ATOM 4868 C C . ILE B 1 300 ? -9.647 25.793 71.517 1.00 31.55 ? 300 ILE B C 1 ATOM 4869 O O . ILE B 1 300 ? -10.577 26.037 70.722 1.00 32.31 ? 300 ILE B O 1 ATOM 4870 C CB . ILE B 1 300 ? -10.730 25.601 73.778 1.00 30.20 ? 300 ILE B CB 1 ATOM 4871 C CG1 . ILE B 1 300 ? -10.964 26.278 75.127 1.00 29.31 ? 300 ILE B CG1 1 ATOM 4872 C CG2 . ILE B 1 300 ? -10.363 24.111 73.970 1.00 31.66 ? 300 ILE B CG2 1 ATOM 4873 C CD1 . ILE B 1 300 ? -12.228 25.808 75.799 1.00 32.12 ? 300 ILE B CD1 1 ATOM 4874 N N . HIS B 1 301 ? -8.602 25.042 71.208 1.00 31.64 ? 301 HIS B N 1 ATOM 4875 C CA . HIS B 1 301 ? -8.302 24.606 69.839 1.00 33.73 ? 301 HIS B CA 1 ATOM 4876 C C . HIS B 1 301 ? -7.896 23.141 69.827 1.00 32.77 ? 301 HIS B C 1 ATOM 4877 O O . HIS B 1 301 ? -7.324 22.672 70.779 1.00 36.30 ? 301 HIS B O 1 ATOM 4878 C CB . HIS B 1 301 ? -7.125 25.422 69.295 1.00 34.64 ? 301 HIS B CB 1 ATOM 4879 C CG . HIS B 1 301 ? -7.528 26.691 68.622 1.00 39.01 ? 301 HIS B CG 1 ATOM 4880 N ND1 . HIS B 1 301 ? -8.130 27.731 69.294 1.00 40.54 ? 301 HIS B ND1 1 ATOM 4881 C CD2 . HIS B 1 301 ? -7.431 27.085 67.331 1.00 41.79 ? 301 HIS B CD2 1 ATOM 4882 C CE1 . HIS B 1 301 ? -8.399 28.706 68.445 1.00 40.39 ? 301 HIS B CE1 1 ATOM 4883 N NE2 . HIS B 1 301 ? -7.978 28.343 67.248 1.00 41.29 ? 301 HIS B NE2 1 ATOM 4884 N N . ALA B 1 302 ? -8.161 22.428 68.740 1.00 34.86 ? 302 ALA B N 1 ATOM 4885 C CA . ALA B 1 302 ? -7.607 21.099 68.563 1.00 34.74 ? 302 ALA B CA 1 ATOM 4886 C C . ALA B 1 302 ? -6.113 21.177 68.158 1.00 37.89 ? 302 ALA B C 1 ATOM 4887 O O . ALA B 1 302 ? -5.686 22.061 67.389 1.00 34.92 ? 302 ALA B O 1 ATOM 4888 C CB . ALA B 1 302 ? -8.419 20.325 67.522 1.00 35.97 ? 302 ALA B CB 1 ATOM 4889 N N . MET B 1 303 ? -5.320 20.261 68.707 1.00 38.32 ? 303 MET B N 1 ATOM 4890 C CA . MET B 1 303 ? -3.907 20.155 68.384 1.00 40.56 ? 303 MET B CA 1 ATOM 4891 C C . MET B 1 303 ? -3.511 18.695 68.598 1.00 38.77 ? 303 MET B C 1 ATOM 4892 O O . MET B 1 303 ? -3.562 18.186 69.728 1.00 37.67 ? 303 MET B O 1 ATOM 4893 C CB . MET B 1 303 ? -3.091 21.089 69.283 1.00 45.21 ? 303 MET B CB 1 ATOM 4894 C CG . MET B 1 303 ? -1.634 21.229 68.936 1.00 50.34 ? 303 MET B CG 1 ATOM 4895 S SD . MET B 1 303 ? -1.321 22.675 67.892 1.00 57.19 ? 303 MET B SD 1 ATOM 4896 C CE . MET B 1 303 ? 0.474 22.787 68.023 1.00 52.86 ? 303 MET B CE 1 ATOM 4897 N N . ASP B 1 304 ? -3.160 18.009 67.514 1.00 38.66 ? 304 ASP B N 1 ATOM 4898 C CA . ASP B 1 304 ? -2.672 16.630 67.617 1.00 40.05 ? 304 ASP B CA 1 ATOM 4899 C C . ASP B 1 304 ? -1.154 16.614 67.731 1.00 40.38 ? 304 ASP B C 1 ATOM 4900 O O . ASP B 1 304 ? -0.453 16.808 66.742 1.00 41.03 ? 304 ASP B O 1 ATOM 4901 C CB . ASP B 1 304 ? -3.169 15.766 66.451 1.00 39.96 ? 304 ASP B CB 1 ATOM 4902 C CG . ASP B 1 304 ? -4.682 15.540 66.499 1.00 40.01 ? 304 ASP B CG 1 ATOM 4903 O OD1 . ASP B 1 304 ? -5.219 15.160 67.562 1.00 42.47 ? 304 ASP B OD1 1 ATOM 4904 O OD2 . ASP B 1 304 ? -5.427 15.735 65.535 1.00 37.73 ? 304 ASP B OD2 1 ATOM 4905 N N . ILE B 1 305 ? -0.666 16.403 68.955 1.00 41.23 ? 305 ILE B N 1 ATOM 4906 C CA . ILE B 1 305 ? 0.772 16.438 69.267 1.00 39.75 ? 305 ILE B CA 1 ATOM 4907 C C . ILE B 1 305 ? 1.387 15.029 69.101 1.00 42.02 ? 305 ILE B C 1 ATOM 4908 O O . ILE B 1 305 ? 0.900 14.062 69.682 1.00 41.21 ? 305 ILE B O 1 ATOM 4909 C CB . ILE B 1 305 ? 1.016 17.054 70.691 1.00 38.17 ? 305 ILE B CB 1 ATOM 4910 C CG1 . ILE B 1 305 ? 0.519 18.509 70.735 1.00 36.93 ? 305 ILE B CG1 1 ATOM 4911 C CG2 . ILE B 1 305 ? 2.486 17.022 71.086 1.00 35.27 ? 305 ILE B CG2 1 ATOM 4912 C CD1 . ILE B 1 305 ? 0.331 19.085 72.145 1.00 37.11 ? 305 ILE B CD1 1 ATOM 4913 N N . PRO B 1 306 ? 2.435 14.933 68.276 1.00 43.67 ? 306 PRO B N 1 ATOM 4914 C CA . PRO B 1 306 ? 3.085 13.661 67.967 1.00 45.21 ? 306 PRO B CA 1 ATOM 4915 C C . PRO B 1 306 ? 3.821 13.023 69.147 1.00 47.59 ? 306 PRO B C 1 ATOM 4916 O O . PRO B 1 306 ? 4.306 13.744 70.026 1.00 46.92 ? 306 PRO B O 1 ATOM 4917 C CB . PRO B 1 306 ? 4.111 14.059 66.893 1.00 44.80 ? 306 PRO B CB 1 ATOM 4918 C CG . PRO B 1 306 ? 4.405 15.496 67.159 1.00 45.61 ? 306 PRO B CG 1 ATOM 4919 C CD . PRO B 1 306 ? 3.054 16.055 67.538 1.00 43.92 ? 306 PRO B CD 1 ATOM 4920 N N . PRO B 1 307 ? 3.926 11.688 69.156 1.00 49.45 ? 307 PRO B N 1 ATOM 4921 C CA . PRO B 1 307 ? 4.821 10.989 70.078 1.00 50.03 ? 307 PRO B CA 1 ATOM 4922 C C . PRO B 1 307 ? 6.238 11.554 69.952 1.00 51.44 ? 307 PRO B C 1 ATOM 4923 O O . PRO B 1 307 ? 6.550 12.117 68.893 1.00 51.11 ? 307 PRO B O 1 ATOM 4924 C CB . PRO B 1 307 ? 4.782 9.551 69.567 1.00 50.84 ? 307 PRO B CB 1 ATOM 4925 C CG . PRO B 1 307 ? 3.429 9.412 68.947 1.00 50.14 ? 307 PRO B CG 1 ATOM 4926 C CD . PRO B 1 307 ? 3.173 10.746 68.296 1.00 50.44 ? 307 PRO B CD 1 ATOM 4927 N N . PRO B 1 308 ? 7.084 11.448 70.991 1.00 51.13 ? 308 PRO B N 1 ATOM 4928 C CA . PRO B 1 308 ? 6.763 10.806 72.293 1.00 49.58 ? 308 PRO B CA 1 ATOM 4929 C C . PRO B 1 308 ? 6.017 11.695 73.319 1.00 47.72 ? 308 PRO B C 1 ATOM 4930 O O . PRO B 1 308 ? 5.470 11.184 74.294 1.00 46.85 ? 308 PRO B O 1 ATOM 4931 C CB . PRO B 1 308 ? 8.147 10.445 72.839 1.00 50.98 ? 308 PRO B CB 1 ATOM 4932 C CG . PRO B 1 308 ? 9.072 11.541 72.270 1.00 51.36 ? 308 PRO B CG 1 ATOM 4933 C CD . PRO B 1 308 ? 8.467 11.970 70.955 1.00 51.68 ? 308 PRO B CD 1 ATOM 4934 N N . THR B 1 309 ? 5.992 13.004 73.095 1.00 46.12 ? 309 THR B N 1 ATOM 4935 C CA . THR B 1 309 ? 5.270 13.942 73.973 1.00 46.08 ? 309 THR B CA 1 ATOM 4936 C C . THR B 1 309 ? 3.734 13.734 74.018 1.00 44.17 ? 309 THR B C 1 ATOM 4937 O O . THR B 1 309 ? 3.131 13.785 75.099 1.00 43.44 ? 309 THR B O 1 ATOM 4938 C CB . THR B 1 309 ? 5.637 15.398 73.606 1.00 46.93 ? 309 THR B CB 1 ATOM 4939 O OG1 . THR B 1 309 ? 7.022 15.624 73.909 1.00 47.48 ? 309 THR B OG1 1 ATOM 4940 C CG2 . THR B 1 309 ? 4.891 16.397 74.502 1.00 46.81 ? 309 THR B CG2 1 ATOM 4941 N N . GLY B 1 310 ? 3.116 13.506 72.860 1.00 41.54 ? 310 GLY B N 1 ATOM 4942 C CA . GLY B 1 310 ? 1.683 13.240 72.776 1.00 42.49 ? 310 GLY B CA 1 ATOM 4943 C C . GLY B 1 310 ? 1.341 11.810 72.340 1.00 42.76 ? 310 GLY B C 1 ATOM 4944 O O . GLY B 1 310 ? 2.241 10.999 72.171 1.00 42.48 ? 310 GLY B O 1 ATOM 4945 N N . PRO B 1 311 ? 0.054 11.486 72.151 1.00 42.61 ? 311 PRO B N 1 ATOM 4946 C CA . PRO B 1 311 ? -1.060 12.418 72.364 1.00 41.49 ? 311 PRO B CA 1 ATOM 4947 C C . PRO B 1 311 ? -1.162 12.947 73.785 1.00 40.40 ? 311 PRO B C 1 ATOM 4948 O O . PRO B 1 311 ? -0.849 12.248 74.758 1.00 40.26 ? 311 PRO B O 1 ATOM 4949 C CB . PRO B 1 311 ? -2.305 11.583 72.008 1.00 41.22 ? 311 PRO B CB 1 ATOM 4950 C CG . PRO B 1 311 ? -1.788 10.528 71.086 1.00 41.06 ? 311 PRO B CG 1 ATOM 4951 C CD . PRO B 1 311 ? -0.423 10.174 71.667 1.00 42.58 ? 311 PRO B CD 1 ATOM 4952 N N . THR B 1 312 ? -1.609 14.192 73.880 1.00 38.28 ? 312 THR B N 1 ATOM 4953 C CA . THR B 1 312 ? -1.673 14.899 75.143 1.00 35.00 ? 312 THR B CA 1 ATOM 4954 C C . THR B 1 312 ? -2.518 16.159 74.989 1.00 33.16 ? 312 THR B C 1 ATOM 4955 O O . THR B 1 312 ? -2.596 16.724 73.900 1.00 32.55 ? 312 THR B O 1 ATOM 4956 C CB . THR B 1 312 ? -0.231 15.254 75.652 1.00 34.80 ? 312 THR B CB 1 ATOM 4957 O OG1 . THR B 1 312 ? -0.313 15.920 76.920 1.00 33.47 ? 312 THR B OG1 1 ATOM 4958 C CG2 . THR B 1 312 ? 0.479 16.284 74.724 1.00 32.73 ? 312 THR B CG2 1 ATOM 4959 N N . TRP B 1 313 ? -3.175 16.566 76.072 1.00 33.78 ? 313 TRP B N 1 ATOM 4960 C CA . TRP B 1 313 ? -3.720 17.919 76.169 1.00 30.36 ? 313 TRP B CA 1 ATOM 4961 C C . TRP B 1 313 ? -2.552 18.854 76.408 1.00 29.48 ? 313 TRP B C 1 ATOM 4962 O O . TRP B 1 313 ? -1.504 18.422 76.885 1.00 25.29 ? 313 TRP B O 1 ATOM 4963 C CB . TRP B 1 313 ? -4.668 18.027 77.342 1.00 29.96 ? 313 TRP B CB 1 ATOM 4964 C CG . TRP B 1 313 ? -5.988 17.325 77.154 1.00 30.04 ? 313 TRP B CG 1 ATOM 4965 C CD1 . TRP B 1 313 ? -6.231 15.981 77.241 1.00 32.61 ? 313 TRP B CD1 1 ATOM 4966 C CD2 . TRP B 1 313 ? -7.242 17.939 76.881 1.00 30.06 ? 313 TRP B CD2 1 ATOM 4967 N NE1 . TRP B 1 313 ? -7.566 15.721 77.040 1.00 32.34 ? 313 TRP B NE1 1 ATOM 4968 C CE2 . TRP B 1 313 ? -8.215 16.905 76.817 1.00 31.07 ? 313 TRP B CE2 1 ATOM 4969 C CE3 . TRP B 1 313 ? -7.654 19.263 76.684 1.00 28.73 ? 313 TRP B CE3 1 ATOM 4970 C CZ2 . TRP B 1 313 ? -9.560 17.154 76.556 1.00 29.94 ? 313 TRP B CZ2 1 ATOM 4971 C CZ3 . TRP B 1 313 ? -9.004 19.513 76.436 1.00 32.26 ? 313 TRP B CZ3 1 ATOM 4972 C CH2 . TRP B 1 313 ? -9.941 18.460 76.365 1.00 29.46 ? 313 TRP B CH2 1 ATOM 4973 N N . ALA B 1 314 ? -2.720 20.124 76.048 1.00 27.36 ? 314 ALA B N 1 ATOM 4974 C CA . ALA B 1 314 ? -1.751 21.149 76.417 1.00 27.77 ? 314 ALA B CA 1 ATOM 4975 C C . ALA B 1 314 ? -2.506 22.289 77.081 1.00 27.81 ? 314 ALA B C 1 ATOM 4976 O O . ALA B 1 314 ? -3.500 22.774 76.560 1.00 29.24 ? 314 ALA B O 1 ATOM 4977 C CB . ALA B 1 314 ? -0.965 21.638 75.228 1.00 26.65 ? 314 ALA B CB 1 ATOM 4978 N N . LEU B 1 315 ? -2.028 22.666 78.255 1.00 25.48 ? 315 LEU B N 1 ATOM 4979 C CA . LEU B 1 315 ? -2.611 23.747 79.051 1.00 26.03 ? 315 LEU B CA 1 ATOM 4980 C C . LEU B 1 315 ? -1.680 24.926 78.810 1.00 23.95 ? 315 LEU B C 1 ATOM 4981 O O . LEU B 1 315 ? -0.583 24.991 79.344 1.00 26.54 ? 315 LEU B O 1 ATOM 4982 C CB . LEU B 1 315 ? -2.695 23.343 80.525 1.00 25.05 ? 315 LEU B CB 1 ATOM 4983 C CG . LEU B 1 315 ? -3.452 22.039 80.884 1.00 23.99 ? 315 LEU B CG 1 ATOM 4984 C CD1 . LEU B 1 315 ? -3.366 21.774 82.407 1.00 22.90 ? 315 LEU B CD1 1 ATOM 4985 C CD2 . LEU B 1 315 ? -4.909 22.044 80.412 1.00 21.74 ? 315 LEU B CD2 1 ATOM 4986 N N . GLY B 1 316 ? -2.082 25.814 77.914 1.00 23.29 ? 316 GLY B N 1 ATOM 4987 C CA . GLY B 1 316 ? -1.220 26.928 77.544 1.00 21.05 ? 316 GLY B CA 1 ATOM 4988 C C . GLY B 1 316 ? -1.817 28.184 78.142 1.00 23.96 ? 316 GLY B C 1 ATOM 4989 O O . GLY B 1 316 ? -2.519 28.088 79.138 1.00 22.67 ? 316 GLY B O 1 ATOM 4990 N N . ALA B 1 317 ? -1.576 29.336 77.499 1.00 24.06 ? 317 ALA B N 1 ATOM 4991 C CA . ALA B 1 317 ? -1.935 30.664 78.062 1.00 23.26 ? 317 ALA B CA 1 ATOM 4992 C C . ALA B 1 317 ? -3.367 30.755 78.573 1.00 20.51 ? 317 ALA B C 1 ATOM 4993 O O . ALA B 1 317 ? -3.651 31.464 79.535 1.00 24.53 ? 317 ALA B O 1 ATOM 4994 C CB . ALA B 1 317 ? -1.656 31.800 77.025 1.00 21.68 ? 317 ALA B CB 1 ATOM 4995 N N . THR B 1 318 ? -4.293 30.061 77.922 1.00 20.66 ? 318 THR B N 1 ATOM 4996 C CA . THR B 1 318 ? -5.688 30.131 78.344 1.00 24.17 ? 318 THR B CA 1 ATOM 4997 C C . THR B 1 318 ? -5.845 29.679 79.813 1.00 21.93 ? 318 THR B C 1 ATOM 4998 O O . THR B 1 318 ? -6.525 30.319 80.659 1.00 18.65 ? 318 THR B O 1 ATOM 4999 C CB . THR B 1 318 ? -6.564 29.271 77.398 1.00 25.37 ? 318 THR B CB 1 ATOM 5000 O OG1 . THR B 1 318 ? -6.565 29.874 76.091 1.00 30.80 ? 318 THR B OG1 1 ATOM 5001 C CG2 . THR B 1 318 ? -8.022 29.300 77.866 1.00 22.75 ? 318 THR B CG2 1 ATOM 5002 N N . PHE B 1 319 ? -5.200 28.560 80.115 1.00 21.63 ? 319 PHE B N 1 ATOM 5003 C CA . PHE B 1 319 ? -5.212 28.006 81.473 1.00 20.07 ? 319 PHE B CA 1 ATOM 5004 C C . PHE B 1 319 ? -4.383 28.857 82.437 1.00 21.01 ? 319 PHE B C 1 ATOM 5005 O O . PHE B 1 319 ? -4.817 29.167 83.553 1.00 20.87 ? 319 PHE B O 1 ATOM 5006 C CB . PHE B 1 319 ? -4.651 26.563 81.461 1.00 16.58 ? 319 PHE B CB 1 ATOM 5007 C CG . PHE B 1 319 ? -4.867 25.824 82.763 1.00 19.34 ? 319 PHE B CG 1 ATOM 5008 C CD1 . PHE B 1 319 ? -3.903 25.832 83.752 1.00 20.44 ? 319 PHE B CD1 1 ATOM 5009 C CD2 . PHE B 1 319 ? -6.073 25.167 83.000 1.00 21.73 ? 319 PHE B CD2 1 ATOM 5010 C CE1 . PHE B 1 319 ? -4.084 25.149 84.938 1.00 20.80 ? 319 PHE B CE1 1 ATOM 5011 C CE2 . PHE B 1 319 ? -6.280 24.485 84.191 1.00 24.23 ? 319 PHE B CE2 1 ATOM 5012 C CZ . PHE B 1 319 ? -5.282 24.480 85.169 1.00 20.58 ? 319 PHE B CZ 1 ATOM 5013 N N . ILE B 1 320 ? -3.162 29.184 82.016 1.00 22.85 ? 320 ILE B N 1 ATOM 5014 C CA . ILE B 1 320 ? -2.233 29.991 82.825 1.00 22.37 ? 320 ILE B CA 1 ATOM 5015 C C . ILE B 1 320 ? -2.726 31.384 83.211 1.00 24.06 ? 320 ILE B C 1 ATOM 5016 O O . ILE B 1 320 ? -2.339 31.895 84.263 1.00 26.77 ? 320 ILE B O 1 ATOM 5017 C CB . ILE B 1 320 ? -0.841 30.070 82.129 1.00 24.35 ? 320 ILE B CB 1 ATOM 5018 C CG1 . ILE B 1 320 ? -0.273 28.644 81.994 1.00 24.06 ? 320 ILE B CG1 1 ATOM 5019 C CG2 . ILE B 1 320 ? 0.119 31.020 82.866 1.00 22.30 ? 320 ILE B CG2 1 ATOM 5020 C CD1 . ILE B 1 320 ? 0.999 28.581 81.183 1.00 26.37 ? 320 ILE B CD1 1 ATOM 5021 N N . ARG B 1 321 ? -3.524 32.023 82.366 1.00 23.90 ? 321 ARG B N 1 ATOM 5022 C CA . ARG B 1 321 ? -4.078 33.331 82.708 1.00 25.28 ? 321 ARG B CA 1 ATOM 5023 C C . ARG B 1 321 ? -4.947 33.188 83.944 1.00 25.96 ? 321 ARG B C 1 ATOM 5024 O O . ARG B 1 321 ? -5.069 34.113 84.744 1.00 26.91 ? 321 ARG B O 1 ATOM 5025 C CB . ARG B 1 321 ? -4.988 33.842 81.594 1.00 25.20 ? 321 ARG B CB 1 ATOM 5026 C CG . ARG B 1 321 ? -4.329 34.575 80.498 1.00 21.68 ? 321 ARG B CG 1 ATOM 5027 C CD . ARG B 1 321 ? -5.347 35.371 79.677 1.00 20.49 ? 321 ARG B CD 1 ATOM 5028 N NE . ARG B 1 321 ? -6.154 34.525 78.811 1.00 19.10 ? 321 ARG B NE 1 ATOM 5029 C CZ . ARG B 1 321 ? -5.771 34.073 77.626 1.00 20.60 ? 321 ARG B CZ 1 ATOM 5030 N NH1 . ARG B 1 321 ? -4.569 34.374 77.139 1.00 20.54 ? 321 ARG B NH1 1 ATOM 5031 N NH2 . ARG B 1 321 ? -6.602 33.349 76.901 1.00 24.14 ? 321 ARG B NH2 1 ATOM 5032 N N . LYS B 1 322 ? -5.589 32.030 84.078 1.00 25.36 ? 322 LYS B N 1 ATOM 5033 C CA . LYS B 1 322 ? -6.484 31.810 85.204 1.00 25.97 ? 322 LYS B CA 1 ATOM 5034 C C . LYS B 1 322 ? -5.673 31.371 86.446 1.00 27.51 ? 322 LYS B C 1 ATOM 5035 O O . LYS B 1 322 ? -5.908 31.864 87.566 1.00 26.65 ? 322 LYS B O 1 ATOM 5036 C CB . LYS B 1 322 ? -7.584 30.813 84.793 1.00 27.97 ? 322 LYS B CB 1 ATOM 5037 C CG . LYS B 1 322 ? -8.538 30.402 85.900 1.00 29.66 ? 322 LYS B CG 1 ATOM 5038 C CD . LYS B 1 322 ? -9.604 31.403 86.140 1.00 31.49 ? 322 LYS B CD 1 ATOM 5039 C CE . LYS B 1 322 ? -10.456 30.940 87.311 1.00 33.09 ? 322 LYS B CE 1 ATOM 5040 N NZ . LYS B 1 322 ? -11.616 31.832 87.357 1.00 35.65 ? 322 LYS B NZ 1 ATOM 5041 N N . PHE B 1 323 ? -4.690 30.485 86.230 1.00 20.28 ? 323 PHE B N 1 ATOM 5042 C CA . PHE B 1 323 ? -3.893 29.941 87.321 1.00 22.57 ? 323 PHE B CA 1 ATOM 5043 C C . PHE B 1 323 ? -2.404 30.283 87.200 1.00 24.23 ? 323 PHE B C 1 ATOM 5044 O O . PHE B 1 323 ? -1.704 29.730 86.336 1.00 22.49 ? 323 PHE B O 1 ATOM 5045 C CB . PHE B 1 323 ? -4.117 28.433 87.410 1.00 22.42 ? 323 PHE B CB 1 ATOM 5046 C CG . PHE B 1 323 ? -5.570 28.064 87.636 1.00 22.73 ? 323 PHE B CG 1 ATOM 5047 C CD1 . PHE B 1 323 ? -6.164 28.248 88.876 1.00 26.87 ? 323 PHE B CD1 1 ATOM 5048 C CD2 . PHE B 1 323 ? -6.344 27.551 86.595 1.00 26.92 ? 323 PHE B CD2 1 ATOM 5049 C CE1 . PHE B 1 323 ? -7.529 27.944 89.078 1.00 27.49 ? 323 PHE B CE1 1 ATOM 5050 C CE2 . PHE B 1 323 ? -7.696 27.227 86.789 1.00 27.24 ? 323 PHE B CE2 1 ATOM 5051 C CZ . PHE B 1 323 ? -8.286 27.442 88.032 1.00 25.45 ? 323 PHE B CZ 1 ATOM 5052 N N . TYR B 1 324 ? -1.943 31.205 88.054 1.00 22.87 ? 324 TYR B N 1 ATOM 5053 C CA . TYR B 1 324 ? -0.506 31.504 88.242 1.00 25.33 ? 324 TYR B CA 1 ATOM 5054 C C . TYR B 1 324 ? 0.214 30.159 88.385 1.00 26.03 ? 324 TYR B C 1 ATOM 5055 O O . TYR B 1 324 ? -0.199 29.323 89.200 1.00 22.04 ? 324 TYR B O 1 ATOM 5056 C CB . TYR B 1 324 ? -0.296 32.391 89.495 1.00 22.93 ? 324 TYR B CB 1 ATOM 5057 C CG . TYR B 1 324 ? 1.124 32.912 89.720 1.00 24.14 ? 324 TYR B CG 1 ATOM 5058 C CD1 . TYR B 1 324 ? 2.119 32.094 90.260 1.00 23.36 ? 324 TYR B CD1 1 ATOM 5059 C CD2 . TYR B 1 324 ? 1.471 34.240 89.403 1.00 23.28 ? 324 TYR B CD2 1 ATOM 5060 C CE1 . TYR B 1 324 ? 3.423 32.572 90.473 1.00 22.26 ? 324 TYR B CE1 1 ATOM 5061 C CE2 . TYR B 1 324 ? 2.765 34.708 89.590 1.00 22.62 ? 324 TYR B CE2 1 ATOM 5062 C CZ . TYR B 1 324 ? 3.735 33.881 90.121 1.00 25.37 ? 324 TYR B CZ 1 ATOM 5063 O OH . TYR B 1 324 ? 5.022 34.362 90.289 1.00 21.19 ? 324 TYR B OH 1 ATOM 5064 N N . THR B 1 325 ? 1.277 29.948 87.598 1.00 23.06 ? 325 THR B N 1 ATOM 5065 C CA . THR B 1 325 ? 1.948 28.623 87.568 1.00 24.22 ? 325 THR B CA 1 ATOM 5066 C C . THR B 1 325 ? 3.393 28.602 88.086 1.00 24.72 ? 325 THR B C 1 ATOM 5067 O O . THR B 1 325 ? 4.208 29.362 87.615 1.00 23.78 ? 325 THR B O 1 ATOM 5068 C CB . THR B 1 325 ? 1.864 28.033 86.144 1.00 24.47 ? 325 THR B CB 1 ATOM 5069 O OG1 . THR B 1 325 ? 0.487 27.854 85.795 1.00 22.90 ? 325 THR B OG1 1 ATOM 5070 C CG2 . THR B 1 325 ? 2.416 26.621 86.113 1.00 23.47 ? 325 THR B CG2 1 ATOM 5071 N N . GLU B 1 326 ? 3.698 27.716 89.040 1.00 25.65 ? 326 GLU B N 1 ATOM 5072 C CA . GLU B 1 326 ? 5.066 27.518 89.512 1.00 27.24 ? 326 GLU B CA 1 ATOM 5073 C C . GLU B 1 326 ? 5.599 26.164 89.047 1.00 27.14 ? 326 GLU B C 1 ATOM 5074 O O . GLU B 1 326 ? 5.007 25.135 89.327 1.00 28.61 ? 326 GLU B O 1 ATOM 5075 C CB . GLU B 1 326 ? 5.141 27.614 91.035 1.00 29.44 ? 326 GLU B CB 1 ATOM 5076 C CG . GLU B 1 326 ? 6.507 27.275 91.668 1.00 30.73 ? 326 GLU B CG 1 ATOM 5077 C CD . GLU B 1 326 ? 6.591 27.708 93.123 1.00 32.80 ? 326 GLU B CD 1 ATOM 5078 O OE1 . GLU B 1 326 ? 6.353 26.872 94.015 1.00 32.02 ? 326 GLU B OE1 1 ATOM 5079 O OE2 . GLU B 1 326 ? 6.863 28.909 93.384 1.00 38.77 ? 326 GLU B OE2 1 ATOM 5080 N N . PHE B 1 327 ? 6.757 26.201 88.396 1.00 25.17 ? 327 PHE B N 1 ATOM 5081 C CA . PHE B 1 327 ? 7.433 25.030 87.852 1.00 25.09 ? 327 PHE B CA 1 ATOM 5082 C C . PHE B 1 327 ? 8.590 24.686 88.798 1.00 25.48 ? 327 PHE B C 1 ATOM 5083 O O . PHE B 1 327 ? 9.528 25.467 88.953 1.00 24.32 ? 327 PHE B O 1 ATOM 5084 C CB . PHE B 1 327 ? 7.925 25.330 86.429 1.00 23.08 ? 327 PHE B CB 1 ATOM 5085 C CG . PHE B 1 327 ? 6.822 25.532 85.421 1.00 19.95 ? 327 PHE B CG 1 ATOM 5086 C CD1 . PHE B 1 327 ? 6.268 24.433 84.745 1.00 20.16 ? 327 PHE B CD1 1 ATOM 5087 C CD2 . PHE B 1 327 ? 6.341 26.802 85.129 1.00 22.59 ? 327 PHE B CD2 1 ATOM 5088 C CE1 . PHE B 1 327 ? 5.257 24.597 83.827 1.00 20.05 ? 327 PHE B CE1 1 ATOM 5089 C CE2 . PHE B 1 327 ? 5.320 26.985 84.183 1.00 16.22 ? 327 PHE B CE2 1 ATOM 5090 C CZ . PHE B 1 327 ? 4.772 25.887 83.548 1.00 21.50 ? 327 PHE B CZ 1 ATOM 5091 N N . ASP B 1 328 ? 8.485 23.527 89.453 1.00 25.88 ? 328 ASP B N 1 ATOM 5092 C CA . ASP B 1 328 ? 9.326 23.153 90.602 1.00 25.85 ? 328 ASP B CA 1 ATOM 5093 C C . ASP B 1 328 ? 10.286 22.050 90.173 1.00 27.14 ? 328 ASP B C 1 ATOM 5094 O O . ASP B 1 328 ? 9.870 20.892 90.038 1.00 25.70 ? 328 ASP B O 1 ATOM 5095 C CB . ASP B 1 328 ? 8.394 22.735 91.785 1.00 27.53 ? 328 ASP B CB 1 ATOM 5096 C CG . ASP B 1 328 ? 9.136 22.391 93.101 1.00 28.82 ? 328 ASP B CG 1 ATOM 5097 O OD1 . ASP B 1 328 ? 10.398 22.352 93.181 1.00 25.39 ? 328 ASP B OD1 1 ATOM 5098 O OD2 . ASP B 1 328 ? 8.487 22.124 94.141 1.00 27.32 ? 328 ASP B OD2 1 ATOM 5099 N N . ARG B 1 329 ? 11.556 22.425 89.938 1.00 24.09 ? 329 ARG B N 1 ATOM 5100 C CA . ARG B 1 329 ? 12.600 21.502 89.476 1.00 27.19 ? 329 ARG B CA 1 ATOM 5101 C C . ARG B 1 329 ? 13.184 20.674 90.615 1.00 28.76 ? 329 ARG B C 1 ATOM 5102 O O . ARG B 1 329 ? 13.643 19.552 90.393 1.00 27.29 ? 329 ARG B O 1 ATOM 5103 C CB . ARG B 1 329 ? 13.762 22.238 88.774 1.00 29.05 ? 329 ARG B CB 1 ATOM 5104 C CG . ARG B 1 329 ? 13.485 22.747 87.337 1.00 31.93 ? 329 ARG B CG 1 ATOM 5105 C CD . ARG B 1 329 ? 13.389 21.620 86.300 1.00 37.41 ? 329 ARG B CD 1 ATOM 5106 N NE . ARG B 1 329 ? 14.510 20.688 86.376 1.00 41.29 ? 329 ARG B NE 1 ATOM 5107 C CZ . ARG B 1 329 ? 15.659 20.851 85.728 1.00 44.10 ? 329 ARG B CZ 1 ATOM 5108 N NH1 . ARG B 1 329 ? 15.837 21.914 84.943 1.00 42.95 ? 329 ARG B NH1 1 ATOM 5109 N NH2 . ARG B 1 329 ? 16.626 19.944 85.861 1.00 41.87 ? 329 ARG B NH2 1 ATOM 5110 N N . ARG B 1 330 ? 13.182 21.224 91.823 1.00 27.75 ? 330 ARG B N 1 ATOM 5111 C CA . ARG B 1 330 ? 13.752 20.517 92.971 1.00 30.99 ? 330 ARG B CA 1 ATOM 5112 C C . ARG B 1 330 ? 12.924 19.271 93.312 1.00 31.48 ? 330 ARG B C 1 ATOM 5113 O O . ARG B 1 330 ? 13.486 18.228 93.691 1.00 31.86 ? 330 ARG B O 1 ATOM 5114 C CB . ARG B 1 330 ? 13.896 21.462 94.170 1.00 31.50 ? 330 ARG B CB 1 ATOM 5115 C CG . ARG B 1 330 ? 14.193 20.837 95.537 1.00 36.18 ? 330 ARG B CG 1 ATOM 5116 C CD . ARG B 1 330 ? 15.525 20.061 95.660 1.00 39.12 ? 330 ARG B CD 1 ATOM 5117 N NE . ARG B 1 330 ? 15.280 18.783 96.345 1.00 42.87 ? 330 ARG B NE 1 ATOM 5118 C CZ . ARG B 1 330 ? 15.574 18.531 97.609 1.00 43.08 ? 330 ARG B CZ 1 ATOM 5119 N NH1 . ARG B 1 330 ? 16.181 19.443 98.354 1.00 46.59 ? 330 ARG B NH1 1 ATOM 5120 N NH2 . ARG B 1 330 ? 15.286 17.358 98.129 1.00 40.99 ? 330 ARG B NH2 1 ATOM 5121 N N . ASN B 1 331 ? 11.603 19.400 93.174 1.00 28.27 ? 331 ASN B N 1 ATOM 5122 C CA . ASN B 1 331 ? 10.654 18.361 93.569 1.00 29.30 ? 331 ASN B CA 1 ATOM 5123 C C . ASN B 1 331 ? 9.959 17.660 92.408 1.00 28.68 ? 331 ASN B C 1 ATOM 5124 O O . ASN B 1 331 ? 9.259 16.693 92.644 1.00 29.95 ? 331 ASN B O 1 ATOM 5125 C CB . ASN B 1 331 ? 9.584 18.918 94.513 1.00 29.13 ? 331 ASN B CB 1 ATOM 5126 C CG . ASN B 1 331 ? 10.154 19.474 95.804 1.00 30.12 ? 331 ASN B CG 1 ATOM 5127 O OD1 . ASN B 1 331 ? 9.777 20.571 96.230 1.00 28.91 ? 331 ASN B OD1 1 ATOM 5128 N ND2 . ASN B 1 331 ? 11.071 18.735 96.430 1.00 29.23 ? 331 ASN B ND2 1 ATOM 5129 N N . ASN B 1 332 ? 10.155 18.148 91.177 1.00 26.56 ? 332 ASN B N 1 ATOM 5130 C CA . ASN B 1 332 ? 9.536 17.600 89.954 1.00 29.73 ? 332 ASN B CA 1 ATOM 5131 C C . ASN B 1 332 ? 8.016 17.653 90.063 1.00 28.66 ? 332 ASN B C 1 ATOM 5132 O O . ASN B 1 332 ? 7.325 16.630 90.094 1.00 29.73 ? 332 ASN B O 1 ATOM 5133 C CB . ASN B 1 332 ? 10.039 16.181 89.598 1.00 30.50 ? 332 ASN B CB 1 ATOM 5134 C CG . ASN B 1 332 ? 11.459 16.179 89.025 1.00 32.44 ? 332 ASN B CG 1 ATOM 5135 O OD1 . ASN B 1 332 ? 11.762 16.930 88.090 1.00 31.22 ? 332 ASN B OD1 1 ATOM 5136 N ND2 . ASN B 1 332 ? 12.341 15.332 89.593 1.00 30.73 ? 332 ASN B ND2 1 ATOM 5137 N N . ARG B 1 333 ? 7.518 18.876 90.165 1.00 26.24 ? 333 ARG B N 1 ATOM 5138 C CA . ARG B 1 333 ? 6.109 19.126 90.327 1.00 21.69 ? 333 ARG B CA 1 ATOM 5139 C C . ARG B 1 333 ? 5.773 20.525 89.826 1.00 23.19 ? 333 ARG B C 1 ATOM 5140 O O . ARG B 1 333 ? 6.658 21.387 89.698 1.00 23.01 ? 333 ARG B O 1 ATOM 5141 C CB . ARG B 1 333 ? 5.670 18.932 91.789 1.00 22.16 ? 333 ARG B CB 1 ATOM 5142 C CG . ARG B 1 333 ? 6.212 19.986 92.800 1.00 21.81 ? 333 ARG B CG 1 ATOM 5143 C CD . ARG B 1 333 ? 6.074 19.623 94.244 1.00 22.71 ? 333 ARG B CD 1 ATOM 5144 N NE . ARG B 1 333 ? 6.341 20.791 95.078 1.00 24.76 ? 333 ARG B NE 1 ATOM 5145 C CZ . ARG B 1 333 ? 5.902 20.989 96.308 1.00 26.90 ? 333 ARG B CZ 1 ATOM 5146 N NH1 . ARG B 1 333 ? 6.225 22.140 96.936 1.00 23.82 ? 333 ARG B NH1 1 ATOM 5147 N NH2 . ARG B 1 333 ? 5.164 20.056 96.921 1.00 23.21 ? 333 ARG B NH2 1 ATOM 5148 N N . ILE B 1 334 ? 4.489 20.724 89.544 1.00 22.16 ? 334 ILE B N 1 ATOM 5149 C CA . ILE B 1 334 ? 3.980 21.984 89.016 1.00 25.21 ? 334 ILE B CA 1 ATOM 5150 C C . ILE B 1 334 ? 2.902 22.468 90.000 1.00 24.98 ? 334 ILE B C 1 ATOM 5151 O O . ILE B 1 334 ? 2.011 21.693 90.392 1.00 23.23 ? 334 ILE B O 1 ATOM 5152 C CB . ILE B 1 334 ? 3.398 21.792 87.578 1.00 24.22 ? 334 ILE B CB 1 ATOM 5153 C CG1 . ILE B 1 334 ? 4.495 21.400 86.580 1.00 22.71 ? 334 ILE B CG1 1 ATOM 5154 C CG2 . ILE B 1 334 ? 2.713 23.087 87.039 1.00 26.25 ? 334 ILE B CG2 1 ATOM 5155 C CD1 . ILE B 1 334 ? 3.916 20.985 85.255 1.00 17.67 ? 334 ILE B CD1 1 ATOM 5156 N N . GLY B 1 335 ? 3.004 23.722 90.430 1.00 23.21 ? 335 GLY B N 1 ATOM 5157 C CA . GLY B 1 335 ? 1.988 24.255 91.339 1.00 21.41 ? 335 GLY B CA 1 ATOM 5158 C C . GLY B 1 335 ? 1.121 25.304 90.690 1.00 25.87 ? 335 GLY B C 1 ATOM 5159 O O . GLY B 1 335 ? 1.622 26.093 89.850 1.00 22.93 ? 335 GLY B O 1 ATOM 5160 N N . PHE B 1 336 ? -0.161 25.333 91.097 1.00 23.73 ? 336 PHE B N 1 ATOM 5161 C CA . PHE B 1 336 ? -1.147 26.301 90.586 1.00 23.35 ? 336 PHE B CA 1 ATOM 5162 C C . PHE B 1 336 ? -1.749 27.055 91.742 1.00 23.91 ? 336 PHE B C 1 ATOM 5163 O O . PHE B 1 336 ? -2.058 26.489 92.817 1.00 22.33 ? 336 PHE B O 1 ATOM 5164 C CB . PHE B 1 336 ? -2.287 25.641 89.786 1.00 23.20 ? 336 PHE B CB 1 ATOM 5165 C CG . PHE B 1 336 ? -1.823 24.903 88.550 1.00 25.90 ? 336 PHE B CG 1 ATOM 5166 C CD1 . PHE B 1 336 ? -1.255 25.587 87.468 1.00 23.99 ? 336 PHE B CD1 1 ATOM 5167 C CD2 . PHE B 1 336 ? -1.944 23.524 88.475 1.00 26.85 ? 336 PHE B CD2 1 ATOM 5168 C CE1 . PHE B 1 336 ? -0.814 24.896 86.334 1.00 24.98 ? 336 PHE B CE1 1 ATOM 5169 C CE2 . PHE B 1 336 ? -1.530 22.833 87.353 1.00 24.85 ? 336 PHE B CE2 1 ATOM 5170 C CZ . PHE B 1 336 ? -0.953 23.521 86.284 1.00 25.76 ? 336 PHE B CZ 1 ATOM 5171 N N . ALA B 1 337 ? -1.861 28.354 91.539 1.00 21.75 ? 337 ALA B N 1 ATOM 5172 C CA . ALA B 1 337 ? -2.611 29.190 92.463 1.00 21.76 ? 337 ALA B CA 1 ATOM 5173 C C . ALA B 1 337 ? -3.407 30.117 91.591 1.00 22.95 ? 337 ALA B C 1 ATOM 5174 O O . ALA B 1 337 ? -2.981 30.419 90.500 1.00 25.95 ? 337 ALA B O 1 ATOM 5175 C CB . ALA B 1 337 ? -1.667 29.972 93.337 1.00 22.07 ? 337 ALA B CB 1 ATOM 5176 N N . LEU B 1 338 ? -4.539 30.612 92.074 1.00 25.60 ? 338 LEU B N 1 ATOM 5177 C CA . LEU B 1 338 ? -5.407 31.503 91.299 1.00 24.51 ? 338 LEU B CA 1 ATOM 5178 C C . LEU B 1 338 ? -4.695 32.829 91.065 1.00 23.57 ? 338 LEU B C 1 ATOM 5179 O O . LEU B 1 338 ? -4.182 33.427 91.994 1.00 24.57 ? 338 LEU B O 1 ATOM 5180 C CB . LEU B 1 338 ? -6.685 31.731 92.109 1.00 27.44 ? 338 LEU B CB 1 ATOM 5181 C CG . LEU B 1 338 ? -7.825 32.632 91.695 1.00 31.68 ? 338 LEU B CG 1 ATOM 5182 C CD1 . LEU B 1 338 ? -8.474 32.108 90.411 1.00 33.42 ? 338 LEU B CD1 1 ATOM 5183 C CD2 . LEU B 1 338 ? -8.850 32.630 92.854 1.00 31.60 ? 338 LEU B CD2 1 ATOM 5184 N N . ALA B 1 339 ? -4.630 33.266 89.820 1.00 24.04 ? 339 ALA B N 1 ATOM 5185 C CA . ALA B 1 339 ? -3.948 34.507 89.485 1.00 24.80 ? 339 ALA B CA 1 ATOM 5186 C C . ALA B 1 339 ? -4.802 35.666 89.940 1.00 28.06 ? 339 ALA B C 1 ATOM 5187 O O . ALA B 1 339 ? -6.030 35.613 89.871 1.00 28.15 ? 339 ALA B O 1 ATOM 5188 C CB . ALA B 1 339 ? -3.727 34.600 87.982 1.00 23.15 ? 339 ALA B CB 1 ATOM 5189 N N . ARG B 1 340 ? -4.174 36.715 90.427 1.00 31.91 ? 340 ARG B N 1 ATOM 5190 C CA . ARG B 1 340 ? -4.961 37.897 90.643 1.00 37.11 ? 340 ARG B CA 1 ATOM 5191 C C . ARG B 1 340 ? -4.486 39.000 89.740 1.00 38.65 ? 340 ARG B C 1 ATOM 5192 O O . ARG B 1 340 ? -3.281 39.120 89.454 1.00 38.16 ? 340 ARG B O 1 ATOM 5193 C CB . ARG B 1 340 ? -5.039 38.302 92.109 1.00 39.73 ? 340 ARG B CB 1 ATOM 5194 C CG . ARG B 1 340 ? -3.760 38.548 92.800 1.00 44.00 ? 340 ARG B CG 1 ATOM 5195 C CD . ARG B 1 340 ? -3.973 38.680 94.290 1.00 49.57 ? 340 ARG B CD 1 ATOM 5196 N NE . ARG B 1 340 ? -2.807 39.215 94.979 1.00 54.97 ? 340 ARG B NE 1 ATOM 5197 C CZ . ARG B 1 340 ? -2.880 40.000 96.047 1.00 57.92 ? 340 ARG B CZ 1 ATOM 5198 N NH1 . ARG B 1 340 ? -4.072 40.349 96.537 1.00 57.94 ? 340 ARG B NH1 1 ATOM 5199 N NH2 . ARG B 1 340 ? -1.765 40.442 96.621 1.00 57.97 ? 340 ARG B NH2 1 ATOM 5200 N N . HIS B 1 341 ? -5.445 39.795 89.282 1.00 41.43 ? 341 HIS B N 1 ATOM 5201 C CA . HIS B 1 341 ? -5.181 40.725 88.204 1.00 44.92 ? 341 HIS B CA 1 ATOM 5202 C C . HIS B 1 341 ? -5.159 42.170 88.668 1.00 47.31 ? 341 HIS B C 1 ATOM 5203 O O . HIS B 1 341 ? -4.170 42.872 88.445 1.00 47.84 ? 341 HIS B O 1 ATOM 5204 C CB . HIS B 1 341 ? -6.116 40.453 87.022 1.00 44.47 ? 341 HIS B CB 1 ATOM 5205 C CG . HIS B 1 341 ? -5.910 39.093 86.416 1.00 45.60 ? 341 HIS B CG 1 ATOM 5206 N ND1 . HIS B 1 341 ? -6.768 38.037 86.639 1.00 47.03 ? 341 HIS B ND1 1 ATOM 5207 C CD2 . HIS B 1 341 ? -4.913 38.604 85.640 1.00 45.74 ? 341 HIS B CD2 1 ATOM 5208 C CE1 . HIS B 1 341 ? -6.317 36.963 86.015 1.00 45.70 ? 341 HIS B CE1 1 ATOM 5209 N NE2 . HIS B 1 341 ? -5.191 37.280 85.403 1.00 46.37 ? 341 HIS B NE2 1 ATOM 5210 O OXT . HIS B 1 341 ? -6.085 42.656 89.314 1.00 49.71 ? 341 HIS B OXT 1 HETATM 5211 CL CLA . A5T C 2 . ? -2.389 5.606 3.948 1.00 43.34 ? 342 A5T A CLA 1 HETATM 5212 C C36 . A5T C 2 . ? -0.684 5.620 4.497 1.00 39.28 ? 342 A5T A C36 1 HETATM 5213 C C33 . A5T C 2 . ? 0.319 5.444 3.560 1.00 38.98 ? 342 A5T A C33 1 HETATM 5214 CL CLR3 . A5T C 2 . ? -0.115 5.191 1.844 1.00 40.13 ? 342 A5T A CLR3 1 HETATM 5215 C C38 . A5T C 2 . ? -0.354 5.828 5.840 1.00 38.76 ? 342 A5T A C38 1 HETATM 5216 C C37 . A5T C 2 . ? 0.981 5.831 6.245 1.00 39.53 ? 342 A5T A C37 1 HETATM 5217 C C34 . A5T C 2 . ? 1.983 5.633 5.291 1.00 40.13 ? 342 A5T A C34 1 HETATM 5218 C C32 . A5T C 2 . ? 1.655 5.445 3.953 1.00 38.44 ? 342 A5T A C32 1 HETATM 5219 C C29 . A5T C 2 . ? 2.691 5.233 2.878 1.00 36.89 ? 342 A5T A C29 1 HETATM 5220 N N26 . A5T C 2 . ? 4.051 5.696 3.127 1.00 31.04 ? 342 A5T A N26 1 HETATM 5221 C C28 . A5T C 2 . ? 4.269 7.063 2.597 1.00 30.02 ? 342 A5T A C28 1 HETATM 5222 C C31 . A5T C 2 . ? 3.404 8.069 3.363 1.00 25.83 ? 342 A5T A C31 1 HETATM 5223 C C30 . A5T C 2 . ? 4.881 7.954 3.674 1.00 26.08 ? 342 A5T A C30 1 HETATM 5224 C C22 . A5T C 2 . ? 4.968 4.877 3.699 1.00 33.05 ? 342 A5T A C22 1 HETATM 5225 O O25 . A5T C 2 . ? 4.641 3.732 4.083 1.00 30.98 ? 342 A5T A O25 1 HETATM 5226 C C20 . A5T C 2 . ? 6.389 5.264 3.907 1.00 32.30 ? 342 A5T A C20 1 HETATM 5227 C C23 . A5T C 2 . ? 6.896 5.282 5.331 1.00 32.79 ? 342 A5T A C23 1 HETATM 5228 N N27 . A5T C 2 . ? 8.053 6.167 5.480 1.00 31.13 ? 342 A5T A N27 1 HETATM 5229 C C24 . A5T C 2 . ? 9.141 5.747 4.625 1.00 29.75 ? 342 A5T A C24 1 HETATM 5230 C C21 . A5T C 2 . ? 8.722 5.890 3.152 1.00 32.87 ? 342 A5T A C21 1 HETATM 5231 C C . A5T C 2 . ? 7.275 3.868 5.781 1.00 31.92 ? 342 A5T A C 1 HETATM 5232 N NB . A5T C 2 . ? 8.387 3.388 4.960 1.00 32.17 ? 342 A5T A NB 1 HETATM 5233 C CA . A5T C 2 . ? 9.538 4.301 4.980 1.00 31.99 ? 342 A5T A CA 1 HETATM 5234 C C19 . A5T C 2 . ? 7.250 5.537 2.878 1.00 32.60 ? 342 A5T A C19 1 HETATM 5235 C C18 . A5T C 2 . ? 6.872 5.541 1.405 1.00 30.93 ? 342 A5T A C18 1 HETATM 5236 C C16 . A5T C 2 . ? 6.047 4.567 0.831 1.00 30.34 ? 342 A5T A C16 1 HETATM 5237 C C14 . A5T C 2 . ? 5.735 4.615 -0.528 1.00 29.43 ? 342 A5T A C14 1 HETATM 5238 C C17 . A5T C 2 . ? 7.392 6.544 0.578 1.00 28.90 ? 342 A5T A C17 1 HETATM 5239 C C15 . A5T C 2 . ? 7.107 6.590 -0.781 1.00 27.81 ? 342 A5T A C15 1 HETATM 5240 C C13 . A5T C 2 . ? 6.278 5.618 -1.338 1.00 31.16 ? 342 A5T A C13 1 HETATM 5241 C C12 . A5T C 2 . ? 5.951 5.669 -2.784 1.00 31.54 ? 342 A5T A C12 1 HETATM 5242 C C10 . A5T C 2 . ? 4.738 6.067 -3.199 1.00 36.99 ? 342 A5T A C10 1 HETATM 5243 C C8 . A5T C 2 . ? 3.859 6.963 -2.365 1.00 36.53 ? 342 A5T A C8 1 HETATM 5244 O O5 . A5T C 2 . ? 3.218 8.001 -3.132 1.00 38.91 ? 342 A5T A O5 1 HETATM 5245 C C3 . A5T C 2 . ? 1.861 8.041 -2.818 1.00 39.20 ? 342 A5T A C3 1 HETATM 5246 C C6 . A5T C 2 . ? 1.330 7.887 -1.534 1.00 39.99 ? 342 A5T A C6 1 HETATM 5247 F F1 . A5T C 2 . ? 2.124 7.674 -0.484 1.00 40.20 ? 342 A5T A F1 1 HETATM 5248 C C2 . A5T C 2 . ? 0.977 8.253 -3.847 1.00 39.00 ? 342 A5T A C2 1 HETATM 5249 CL CL11 . A5T C 2 . ? 1.712 8.462 -5.475 1.00 42.60 ? 342 A5T A CL11 1 HETATM 5250 C C4 . A5T C 2 . ? -0.399 8.300 -3.614 1.00 38.46 ? 342 A5T A C4 1 HETATM 5251 F F2 . A5T C 2 . ? -1.269 8.513 -4.611 1.00 38.54 ? 342 A5T A F2 1 HETATM 5252 C C7 . A5T C 2 . ? -0.917 8.146 -2.341 1.00 39.44 ? 342 A5T A C7 1 HETATM 5253 C C9 . A5T C 2 . ? -0.042 7.925 -1.296 1.00 39.82 ? 342 A5T A C9 1 HETATM 5254 S S . DMS D 3 . ? 2.374 9.934 7.496 1.00 42.30 ? 343 DMS A S 1 HETATM 5255 O O . DMS D 3 . ? 2.216 11.525 8.294 1.00 40.03 ? 343 DMS A O 1 HETATM 5256 C C1 . DMS D 3 . ? 2.074 8.624 8.690 1.00 44.50 ? 343 DMS A C1 1 HETATM 5257 C C2 . DMS D 3 . ? 0.931 9.597 6.458 1.00 46.14 ? 343 DMS A C2 1 HETATM 5258 C C1 . NAG E 4 . ? 17.576 11.777 -16.093 1.00 51.34 ? 344 NAG A C1 1 HETATM 5259 C C2 . NAG E 4 . ? 18.513 11.702 -17.304 1.00 55.71 ? 344 NAG A C2 1 HETATM 5260 C C3 . NAG E 4 . ? 19.803 10.937 -16.963 1.00 57.16 ? 344 NAG A C3 1 HETATM 5261 C C4 . NAG E 4 . ? 20.480 11.509 -15.707 1.00 57.36 ? 344 NAG A C4 1 HETATM 5262 C C5 . NAG E 4 . ? 19.443 11.631 -14.579 1.00 57.34 ? 344 NAG A C5 1 HETATM 5263 C C6 . NAG E 4 . ? 20.063 12.219 -13.303 1.00 57.01 ? 344 NAG A C6 1 HETATM 5264 C C7 . NAG E 4 . ? 17.903 11.609 -19.657 1.00 57.34 ? 344 NAG A C7 1 HETATM 5265 C C8 . NAG E 4 . ? 18.518 10.720 -20.698 1.00 59.41 ? 344 NAG A C8 1 HETATM 5266 N N2 . NAG E 4 . ? 17.828 11.098 -18.432 1.00 56.60 ? 344 NAG A N2 1 HETATM 5267 O O3 . NAG E 4 . ? 20.682 10.960 -18.074 1.00 59.00 ? 344 NAG A O3 1 HETATM 5268 O O4 . NAG E 4 . ? 21.560 10.702 -15.279 1.00 56.95 ? 344 NAG A O4 1 HETATM 5269 O O5 . NAG E 4 . ? 18.308 12.383 -15.028 1.00 54.29 ? 344 NAG A O5 1 HETATM 5270 O O6 . NAG E 4 . ? 19.999 11.276 -12.245 1.00 56.91 ? 344 NAG A O6 1 HETATM 5271 O O7 . NAG E 4 . ? 17.499 12.733 -19.952 1.00 56.63 ? 344 NAG A O7 1 HETATM 5272 CL CLA . A5T F 2 . ? 3.348 33.556 66.279 1.00 43.33 ? 342 A5T B CLA 1 HETATM 5273 C C36 . A5T F 2 . ? 3.346 32.103 67.330 1.00 41.48 ? 342 A5T B C36 1 HETATM 5274 C C33 . A5T F 2 . ? 4.447 31.260 67.249 1.00 40.63 ? 342 A5T B C33 1 HETATM 5275 CL CLR3 . A5T F 2 . ? 5.780 31.687 66.127 1.00 41.82 ? 342 A5T B CLR3 1 HETATM 5276 C C38 . A5T F 2 . ? 2.287 31.813 68.181 1.00 37.99 ? 342 A5T B C38 1 HETATM 5277 C C37 . A5T F 2 . ? 2.359 30.663 68.957 1.00 40.11 ? 342 A5T B C37 1 HETATM 5278 C C34 . A5T F 2 . ? 3.461 29.804 68.877 1.00 39.79 ? 342 A5T B C34 1 HETATM 5279 C C32 . A5T F 2 . ? 4.523 30.112 68.024 1.00 40.11 ? 342 A5T B C32 1 HETATM 5280 C C29 . A5T F 2 . ? 5.764 29.250 67.868 1.00 35.24 ? 342 A5T B C29 1 HETATM 5281 N N26 . A5T F 2 . ? 6.169 28.413 69.001 1.00 30.70 ? 342 A5T B N26 1 HETATM 5282 C C28 . A5T F 2 . ? 7.228 29.032 69.816 1.00 28.40 ? 342 A5T B C28 1 HETATM 5283 C C31 . A5T F 2 . ? 6.735 30.389 70.315 1.00 26.19 ? 342 A5T B C31 1 HETATM 5284 C C30 . A5T F 2 . ? 6.738 29.200 71.255 1.00 25.14 ? 342 A5T B C30 1 HETATM 5285 C C22 . A5T F 2 . ? 5.651 27.181 69.182 1.00 31.94 ? 342 A5T B C22 1 HETATM 5286 O O25 . A5T F 2 . ? 4.796 26.780 68.403 1.00 30.51 ? 342 A5T B O25 1 HETATM 5287 C C20 . A5T F 2 . ? 6.063 26.233 70.227 1.00 32.00 ? 342 A5T B C20 1 HETATM 5288 C C23 . A5T F 2 . ? 5.030 25.661 71.179 1.00 32.79 ? 342 A5T B C23 1 HETATM 5289 N N27 . A5T F 2 . ? 5.675 25.155 72.374 1.00 32.14 ? 342 A5T B N27 1 HETATM 5290 C C24 . A5T F 2 . ? 6.642 24.116 72.075 1.00 30.85 ? 342 A5T B C24 1 HETATM 5291 C C21 . A5T F 2 . ? 7.781 24.730 71.268 1.00 32.55 ? 342 A5T B C21 1 HETATM 5292 C C . A5T F 2 . ? 4.310 24.467 70.517 1.00 32.77 ? 342 A5T B C 1 HETATM 5293 N NB . A5T F 2 . ? 5.234 23.371 70.191 1.00 31.60 ? 342 A5T B NB 1 HETATM 5294 C CA . A5T F 2 . ? 6.020 22.937 71.332 1.00 29.79 ? 342 A5T B CA 1 HETATM 5295 C C19 . A5T F 2 . ? 7.332 25.758 70.254 1.00 32.26 ? 342 A5T B C19 1 HETATM 5296 C C18 . A5T F 2 . ? 8.442 26.195 69.326 1.00 32.41 ? 342 A5T B C18 1 HETATM 5297 C C16 . A5T F 2 . ? 8.276 26.263 67.944 1.00 29.83 ? 342 A5T B C16 1 HETATM 5298 C C14 . A5T F 2 . ? 9.340 26.662 67.125 1.00 31.67 ? 342 A5T B C14 1 HETATM 5299 C C17 . A5T F 2 . ? 9.695 26.489 69.875 1.00 31.47 ? 342 A5T B C17 1 HETATM 5300 C C15 . A5T F 2 . ? 10.751 26.885 69.060 1.00 33.47 ? 342 A5T B C15 1 HETATM 5301 C C13 . A5T F 2 . ? 10.583 26.974 67.677 1.00 33.19 ? 342 A5T B C13 1 HETATM 5302 C C12 . A5T F 2 . ? 11.724 27.396 66.813 1.00 33.72 ? 342 A5T B C12 1 HETATM 5303 C C10 . A5T F 2 . ? 12.280 28.605 66.955 1.00 34.32 ? 342 A5T B C10 1 HETATM 5304 C C8 . A5T F 2 . ? 11.619 29.804 66.322 1.00 37.81 ? 342 A5T B C8 1 HETATM 5305 O O5 . A5T F 2 . ? 12.031 31.005 66.975 1.00 41.49 ? 342 A5T B O5 1 HETATM 5306 C C3 . A5T F 2 . ? 11.429 32.098 66.376 1.00 42.13 ? 342 A5T B C3 1 HETATM 5307 C C6 . A5T F 2 . ? 10.109 32.416 66.659 1.00 42.47 ? 342 A5T B C6 1 HETATM 5308 F F1 . A5T F 2 . ? 9.408 31.646 67.497 1.00 40.89 ? 342 A5T B F1 1 HETATM 5309 C C2 . A5T F 2 . ? 12.150 32.906 65.503 1.00 42.26 ? 342 A5T B C2 1 HETATM 5310 CL CL11 . A5T F 2 . ? 13.881 32.502 65.192 1.00 44.20 ? 342 A5T B CL11 1 HETATM 5311 C C4 . A5T F 2 . ? 11.524 34.010 64.912 1.00 42.60 ? 342 A5T B C4 1 HETATM 5312 F F2 . A5T F 2 . ? 12.170 34.817 64.042 1.00 42.20 ? 342 A5T B F2 1 HETATM 5313 C C7 . A5T F 2 . ? 10.196 34.305 65.197 1.00 41.88 ? 342 A5T B C7 1 HETATM 5314 C C9 . A5T F 2 . ? 9.484 33.504 66.061 1.00 42.44 ? 342 A5T B C9 1 HETATM 5315 S S . DMS G 3 . ? 3.369 31.962 73.781 1.00 37.41 ? 343 DMS B S 1 HETATM 5316 O O . DMS G 3 . ? 1.776 31.775 74.651 1.00 38.36 ? 343 DMS B O 1 HETATM 5317 C C1 . DMS G 3 . ? 3.150 31.817 72.000 1.00 37.91 ? 343 DMS B C1 1 HETATM 5318 C C2 . DMS G 3 . ? 3.883 33.669 73.899 1.00 34.39 ? 343 DMS B C2 1 HETATM 5319 C C1 . NDG H 5 . ? 31.042 22.959 70.958 1.00 64.52 ? 344 NDG B C1 1 HETATM 5320 C C2 . NDG H 5 . ? 31.988 21.952 70.341 1.00 68.85 ? 344 NDG B C2 1 HETATM 5321 C C3 . NDG H 5 . ? 31.856 20.584 70.999 1.00 69.80 ? 344 NDG B C3 1 HETATM 5322 C C4 . NDG H 5 . ? 31.070 20.666 72.299 1.00 69.92 ? 344 NDG B C4 1 HETATM 5323 C C5 . NDG H 5 . ? 29.741 21.333 72.125 1.00 69.39 ? 344 NDG B C5 1 HETATM 5324 C C6 . NDG H 5 . ? 29.267 21.780 73.485 1.00 70.22 ? 344 NDG B C6 1 HETATM 5325 C C7 . NDG H 5 . ? 31.686 20.964 68.045 1.00 72.61 ? 344 NDG B C7 1 HETATM 5326 C C8 . NDG H 5 . ? 31.688 19.557 68.562 1.00 72.85 ? 344 NDG B C8 1 HETATM 5327 O O . NDG H 5 . ? 29.799 22.383 71.192 1.00 67.57 ? 344 NDG B O 1 HETATM 5328 O O3 . NDG H 5 . ? 33.163 20.245 71.341 1.00 70.70 ? 344 NDG B O3 1 HETATM 5329 O O4 . NDG H 5 . ? 30.775 19.408 72.838 1.00 69.88 ? 344 NDG B O4 1 HETATM 5330 O O6 . NDG H 5 . ? 27.939 21.350 73.659 1.00 71.56 ? 344 NDG B O6 1 HETATM 5331 O O7 . NDG H 5 . ? 31.553 21.157 66.848 1.00 72.63 ? 344 NDG B O7 1 HETATM 5332 N N2 . NDG H 5 . ? 31.837 21.974 68.902 1.00 70.48 ? 344 NDG B N2 1 HETATM 5333 O O . HOH I 6 . ? 4.749 17.526 17.960 1.00 22.75 ? 345 HOH A O 1 HETATM 5334 O O . HOH I 6 . ? 16.633 17.163 -8.178 1.00 23.77 ? 346 HOH A O 1 HETATM 5335 O O . HOH I 6 . ? 19.877 -1.658 27.797 1.00 70.56 ? 347 HOH A O 1 HETATM 5336 O O . HOH I 6 . ? 13.480 14.542 -2.100 1.00 26.86 ? 348 HOH A O 1 HETATM 5337 O O . HOH I 6 . ? 18.155 25.505 17.926 1.00 56.91 ? 349 HOH A O 1 HETATM 5338 O O . HOH I 6 . ? -1.328 9.588 -21.237 1.00 47.77 ? 350 HOH A O 1 HETATM 5339 O O . HOH I 6 . ? 9.678 13.000 -18.076 1.00 22.98 ? 351 HOH A O 1 HETATM 5340 O O . HOH I 6 . ? 21.358 26.850 3.458 1.00 42.20 ? 352 HOH A O 1 HETATM 5341 O O . HOH I 6 . ? 15.162 16.103 0.968 1.00 24.75 ? 353 HOH A O 1 HETATM 5342 O O . HOH I 6 . ? -5.621 12.063 20.022 1.00 19.69 ? 354 HOH A O 1 HETATM 5343 O O . HOH I 6 . ? 10.130 9.205 -0.773 1.00 34.86 ? 355 HOH A O 1 HETATM 5344 O O . HOH I 6 . ? -4.209 1.049 -7.325 1.00 35.37 ? 356 HOH A O 1 HETATM 5345 O O . HOH I 6 . ? 20.707 16.076 26.202 1.00 66.86 ? 357 HOH A O 1 HETATM 5346 O O . HOH I 6 . ? 0.538 23.342 -14.470 1.00 25.87 ? 358 HOH A O 1 HETATM 5347 O O . HOH I 6 . ? 4.029 14.997 7.125 1.00 23.32 ? 359 HOH A O 1 HETATM 5348 O O . HOH I 6 . ? 23.419 7.856 17.545 1.00 26.67 ? 360 HOH A O 1 HETATM 5349 O O . HOH I 6 . ? -6.238 15.331 -11.314 1.00 27.28 ? 361 HOH A O 1 HETATM 5350 O O . HOH I 6 . ? -5.861 19.051 10.964 1.00 20.07 ? 362 HOH A O 1 HETATM 5351 O O . HOH I 6 . ? 8.735 2.576 1.858 1.00 35.68 ? 363 HOH A O 1 HETATM 5352 O O . HOH I 6 . ? -2.634 -4.340 -5.427 1.00 51.15 ? 364 HOH A O 1 HETATM 5353 O O . HOH I 6 . ? 18.181 13.064 24.282 1.00 22.33 ? 365 HOH A O 1 HETATM 5354 O O . HOH I 6 . ? 9.185 12.572 32.398 1.00 49.62 ? 366 HOH A O 1 HETATM 5355 O O . HOH I 6 . ? 25.869 13.560 3.927 1.00 43.57 ? 367 HOH A O 1 HETATM 5356 O O . HOH I 6 . ? -9.084 13.487 -8.132 1.00 45.03 ? 368 HOH A O 1 HETATM 5357 O O . HOH I 6 . ? 21.789 14.440 0.786 1.00 29.63 ? 369 HOH A O 1 HETATM 5358 O O . HOH I 6 . ? -19.703 2.717 23.928 1.00 53.65 ? 370 HOH A O 1 HETATM 5359 O O . HOH I 6 . ? 2.142 13.897 -16.972 1.00 34.61 ? 371 HOH A O 1 HETATM 5360 O O . HOH I 6 . ? -5.552 25.102 -6.999 1.00 67.41 ? 372 HOH A O 1 HETATM 5361 O O . HOH I 6 . ? 10.786 33.984 8.681 1.00 41.92 ? 373 HOH A O 1 HETATM 5362 O O . HOH I 6 . ? -6.403 -6.813 12.012 1.00 63.68 ? 374 HOH A O 1 HETATM 5363 O O . HOH I 6 . ? 16.396 8.559 6.470 1.00 31.45 ? 375 HOH A O 1 HETATM 5364 O O . HOH I 6 . ? -12.651 8.495 19.279 1.00 31.98 ? 376 HOH A O 1 HETATM 5365 O O . HOH I 6 . ? 1.355 25.768 -19.151 1.00 23.50 ? 377 HOH A O 1 HETATM 5366 O O . HOH I 6 . ? 17.803 16.015 4.259 1.00 28.80 ? 378 HOH A O 1 HETATM 5367 O O . HOH I 6 . ? 21.190 -3.045 13.873 1.00 44.35 ? 379 HOH A O 1 HETATM 5368 O O . HOH I 6 . ? -1.549 4.470 8.556 1.00 40.91 ? 380 HOH A O 1 HETATM 5369 O O . HOH I 6 . ? 12.549 -3.310 -9.007 1.00 64.99 ? 381 HOH A O 1 HETATM 5370 O O . HOH I 6 . ? 10.159 23.826 -20.367 1.00 24.18 ? 382 HOH A O 1 HETATM 5371 O O . HOH I 6 . ? -2.737 -14.619 22.118 1.00 42.84 ? 383 HOH A O 1 HETATM 5372 O O . HOH I 6 . ? 0.887 25.703 -3.192 1.00 37.83 ? 384 HOH A O 1 HETATM 5373 O O . HOH I 6 . ? 20.435 35.281 2.024 1.00 53.57 ? 385 HOH A O 1 HETATM 5374 O O . HOH I 6 . ? 13.769 0.710 -12.573 1.00 43.39 ? 386 HOH A O 1 HETATM 5375 O O . HOH I 6 . ? 12.065 22.642 -14.759 1.00 33.25 ? 387 HOH A O 1 HETATM 5376 O O . HOH I 6 . ? -2.747 18.017 -11.434 1.00 32.21 ? 388 HOH A O 1 HETATM 5377 O O . HOH I 6 . ? 15.308 12.724 -4.763 1.00 23.82 ? 389 HOH A O 1 HETATM 5378 O O . HOH I 6 . ? 6.935 23.146 13.493 1.00 33.89 ? 390 HOH A O 1 HETATM 5379 O O . HOH I 6 . ? 0.801 4.982 31.382 1.00 25.37 ? 391 HOH A O 1 HETATM 5380 O O . HOH I 6 . ? 10.488 -1.346 12.763 1.00 30.49 ? 392 HOH A O 1 HETATM 5381 O O . HOH I 6 . ? 3.085 3.890 8.855 1.00 28.29 ? 393 HOH A O 1 HETATM 5382 O O . HOH I 6 . ? 3.799 16.855 24.264 1.00 37.10 ? 394 HOH A O 1 HETATM 5383 O O . HOH I 6 . ? 21.370 7.343 21.823 1.00 35.38 ? 395 HOH A O 1 HETATM 5384 O O . HOH I 6 . ? 11.852 20.239 26.167 1.00 33.16 ? 396 HOH A O 1 HETATM 5385 O O . HOH I 6 . ? 4.309 2.605 34.241 1.00 30.00 ? 397 HOH A O 1 HETATM 5386 O O . HOH I 6 . ? 5.228 28.523 -11.266 1.00 45.25 ? 398 HOH A O 1 HETATM 5387 O O . HOH I 6 . ? 13.069 13.110 -6.232 1.00 17.77 ? 399 HOH A O 1 HETATM 5388 O O . HOH I 6 . ? 3.874 28.274 -1.822 1.00 38.99 ? 400 HOH A O 1 HETATM 5389 O O . HOH I 6 . ? -3.772 5.787 8.042 1.00 31.07 ? 401 HOH A O 1 HETATM 5390 O O . HOH I 6 . ? -0.821 2.947 -15.727 1.00 28.55 ? 402 HOH A O 1 HETATM 5391 O O . HOH I 6 . ? -0.754 7.418 15.190 1.00 31.48 ? 403 HOH A O 1 HETATM 5392 O O . HOH I 6 . ? 9.734 3.449 8.998 1.00 30.48 ? 404 HOH A O 1 HETATM 5393 O O . HOH I 6 . ? 4.588 2.448 11.141 1.00 24.90 ? 405 HOH A O 1 HETATM 5394 O O . HOH I 6 . ? 17.890 9.231 4.244 1.00 30.18 ? 406 HOH A O 1 HETATM 5395 O O . HOH I 6 . ? -9.204 1.418 19.119 1.00 30.15 ? 407 HOH A O 1 HETATM 5396 O O . HOH I 6 . ? -2.172 23.446 -14.711 1.00 27.82 ? 408 HOH A O 1 HETATM 5397 O O . HOH I 6 . ? 3.346 24.829 0.304 1.00 34.04 ? 409 HOH A O 1 HETATM 5398 O O . HOH I 6 . ? 18.557 3.307 -7.194 1.00 39.03 ? 410 HOH A O 1 HETATM 5399 O O . HOH I 6 . ? 2.939 25.818 -2.195 1.00 31.58 ? 411 HOH A O 1 HETATM 5400 O O . HOH I 6 . ? 7.542 2.171 10.470 1.00 56.17 ? 412 HOH A O 1 HETATM 5401 O O . HOH I 6 . ? 1.279 9.721 20.708 1.00 22.29 ? 413 HOH A O 1 HETATM 5402 O O . HOH I 6 . ? 16.405 25.997 -7.695 1.00 33.27 ? 414 HOH A O 1 HETATM 5403 O O . HOH I 6 . ? 3.825 14.570 -21.514 1.00 35.58 ? 415 HOH A O 1 HETATM 5404 O O . HOH I 6 . ? 1.230 27.496 14.020 1.00 45.79 ? 416 HOH A O 1 HETATM 5405 O O . HOH I 6 . ? 3.500 -0.438 11.315 1.00 39.35 ? 417 HOH A O 1 HETATM 5406 O O . HOH I 6 . ? 1.297 -5.053 14.198 1.00 30.30 ? 418 HOH A O 1 HETATM 5407 O O . HOH I 6 . ? 13.094 -0.510 -3.440 1.00 33.66 ? 419 HOH A O 1 HETATM 5408 O O . HOH I 6 . ? 23.071 1.063 -7.760 1.00 54.46 ? 420 HOH A O 1 HETATM 5409 O O . HOH I 6 . ? -17.373 -1.656 30.873 1.00 44.24 ? 421 HOH A O 1 HETATM 5410 O O . HOH I 6 . ? 5.084 25.612 -9.013 1.00 35.01 ? 422 HOH A O 1 HETATM 5411 O O . HOH I 6 . ? -14.118 7.597 15.506 1.00 46.25 ? 423 HOH A O 1 HETATM 5412 O O . HOH I 6 . ? 14.808 3.646 -17.788 1.00 31.71 ? 424 HOH A O 1 HETATM 5413 O O . HOH I 6 . ? 9.611 11.785 28.774 1.00 45.28 ? 425 HOH A O 1 HETATM 5414 O O . HOH I 6 . ? -3.795 22.987 -8.838 1.00 32.83 ? 426 HOH A O 1 HETATM 5415 O O . HOH I 6 . ? 13.053 29.891 -2.915 1.00 39.39 ? 427 HOH A O 1 HETATM 5416 O O . HOH I 6 . ? 17.209 15.336 -17.369 1.00 42.56 ? 428 HOH A O 1 HETATM 5417 O O . HOH I 6 . ? 21.893 -0.298 25.371 1.00 56.15 ? 429 HOH A O 1 HETATM 5418 O O . HOH I 6 . ? 19.147 27.589 1.936 1.00 36.79 ? 430 HOH A O 1 HETATM 5419 O O . HOH I 6 . ? 14.195 2.985 28.647 1.00 35.17 ? 431 HOH A O 1 HETATM 5420 O O . HOH I 6 . ? 13.268 -3.975 17.006 1.00 40.36 ? 432 HOH A O 1 HETATM 5421 O O . HOH I 6 . ? 14.631 2.052 -9.776 1.00 36.62 ? 433 HOH A O 1 HETATM 5422 O O . HOH I 6 . ? 26.441 22.550 17.505 1.00 50.37 ? 434 HOH A O 1 HETATM 5423 O O . HOH I 6 . ? -17.147 5.641 22.861 1.00 34.84 ? 435 HOH A O 1 HETATM 5424 O O . HOH I 6 . ? -10.173 13.613 17.666 1.00 71.25 ? 436 HOH A O 1 HETATM 5425 O O . HOH I 6 . ? 14.014 -6.765 8.797 1.00 40.65 ? 437 HOH A O 1 HETATM 5426 O O . HOH I 6 . ? 22.576 4.605 10.516 1.00 44.64 ? 438 HOH A O 1 HETATM 5427 O O . HOH I 6 . ? -1.162 -2.271 17.041 1.00 37.99 ? 439 HOH A O 1 HETATM 5428 O O . HOH I 6 . ? 7.761 28.421 -18.085 1.00 37.58 ? 440 HOH A O 1 HETATM 5429 O O . HOH I 6 . ? 8.727 3.414 31.221 1.00 41.26 ? 441 HOH A O 1 HETATM 5430 O O . HOH I 6 . ? -9.484 13.009 11.480 1.00 32.76 ? 442 HOH A O 1 HETATM 5431 O O . HOH I 6 . ? -1.471 12.007 -19.939 1.00 41.41 ? 443 HOH A O 1 HETATM 5432 O O . HOH I 6 . ? 0.984 27.075 5.272 1.00 42.62 ? 444 HOH A O 1 HETATM 5433 O O . HOH I 6 . ? 17.242 15.649 29.084 1.00 67.90 ? 445 HOH A O 1 HETATM 5434 O O . HOH I 6 . ? 17.418 -2.472 16.010 1.00 28.45 ? 446 HOH A O 1 HETATM 5435 O O . HOH I 6 . ? -4.527 22.233 10.196 1.00 37.13 ? 447 HOH A O 1 HETATM 5436 O O . HOH I 6 . ? 22.576 -9.261 27.377 1.00 45.59 ? 448 HOH A O 1 HETATM 5437 O O . HOH I 6 . ? -0.461 23.266 3.580 1.00 31.61 ? 449 HOH A O 1 HETATM 5438 O O . HOH I 6 . ? 1.120 26.161 1.670 1.00 41.36 ? 450 HOH A O 1 HETATM 5439 O O . HOH I 6 . ? 0.652 11.880 22.401 1.00 38.70 ? 451 HOH A O 1 HETATM 5440 O O . HOH I 6 . ? 10.412 1.685 7.178 1.00 68.17 ? 452 HOH A O 1 HETATM 5441 O O . HOH I 6 . ? 14.216 6.998 -0.596 1.00 37.67 ? 453 HOH A O 1 HETATM 5442 O O . HOH I 6 . ? 24.344 15.686 19.090 1.00 36.03 ? 454 HOH A O 1 HETATM 5443 O O . HOH I 6 . ? 20.311 14.044 24.466 1.00 27.30 ? 455 HOH A O 1 HETATM 5444 O O . HOH I 6 . ? 16.636 24.532 22.385 1.00 33.98 ? 456 HOH A O 1 HETATM 5445 O O . HOH I 6 . ? 0.945 13.180 26.487 1.00 49.92 ? 457 HOH A O 1 HETATM 5446 O O . HOH I 6 . ? 4.698 -9.081 11.611 1.00 38.09 ? 458 HOH A O 1 HETATM 5447 O O . HOH I 6 . ? -12.247 9.336 6.553 1.00 42.65 ? 459 HOH A O 1 HETATM 5448 O O . HOH I 6 . ? -3.153 20.776 5.087 1.00 46.42 ? 460 HOH A O 1 HETATM 5449 O O . HOH I 6 . ? 5.936 13.616 -17.859 1.00 38.44 ? 461 HOH A O 1 HETATM 5450 O O . HOH I 6 . ? 0.402 -11.035 28.315 1.00 43.98 ? 462 HOH A O 1 HETATM 5451 O O . HOH I 6 . ? 13.279 4.521 5.707 1.00 39.99 ? 463 HOH A O 1 HETATM 5452 O O . HOH I 6 . ? 28.574 17.447 13.085 1.00 35.37 ? 464 HOH A O 1 HETATM 5453 O O . HOH I 6 . ? 25.484 23.304 5.713 1.00 43.77 ? 465 HOH A O 1 HETATM 5454 O O . HOH I 6 . ? 24.436 18.600 22.376 1.00 45.10 ? 466 HOH A O 1 HETATM 5455 O O . HOH I 6 . ? 22.416 7.272 10.509 1.00 28.08 ? 467 HOH A O 1 HETATM 5456 O O . HOH I 6 . ? 17.228 22.442 -16.352 1.00 59.01 ? 468 HOH A O 1 HETATM 5457 O O . HOH I 6 . ? -2.680 -1.574 10.159 1.00 55.05 ? 469 HOH A O 1 HETATM 5458 O O . HOH I 6 . ? 24.560 20.959 5.137 1.00 39.06 ? 470 HOH A O 1 HETATM 5459 O O . HOH I 6 . ? -3.415 -3.789 -3.128 1.00 38.70 ? 471 HOH A O 1 HETATM 5460 O O . HOH I 6 . ? 8.433 11.387 -19.881 1.00 47.44 ? 472 HOH A O 1 HETATM 5461 O O . HOH I 6 . ? 21.522 17.730 24.158 1.00 34.38 ? 473 HOH A O 1 HETATM 5462 O O . HOH I 6 . ? -4.516 23.429 22.708 1.00 45.10 ? 474 HOH A O 1 HETATM 5463 O O . HOH I 6 . ? 24.513 16.580 6.594 1.00 28.98 ? 475 HOH A O 1 HETATM 5464 O O . HOH I 6 . ? 2.157 -12.205 19.021 1.00 39.40 ? 476 HOH A O 1 HETATM 5465 O O . HOH I 6 . ? -5.022 18.017 -3.670 1.00 31.90 ? 477 HOH A O 1 HETATM 5466 O O . HOH I 6 . ? 24.782 25.410 13.730 1.00 39.81 ? 478 HOH A O 1 HETATM 5467 O O . HOH I 6 . ? 11.066 6.839 -1.818 1.00 37.11 ? 479 HOH A O 1 HETATM 5468 O O . HOH I 6 . ? -8.835 8.435 0.141 1.00 41.60 ? 480 HOH A O 1 HETATM 5469 O O . HOH I 6 . ? 2.534 30.346 -12.636 1.00 48.97 ? 481 HOH A O 1 HETATM 5470 O O . HOH I 6 . ? 9.292 27.219 23.989 1.00 42.86 ? 482 HOH A O 1 HETATM 5471 O O . HOH I 6 . ? 12.996 -4.229 11.804 1.00 40.31 ? 483 HOH A O 1 HETATM 5472 O O . HOH I 6 . ? 23.835 -0.199 6.014 1.00 60.86 ? 484 HOH A O 1 HETATM 5473 O O . HOH I 6 . ? 3.020 1.420 -15.658 1.00 30.67 ? 485 HOH A O 1 HETATM 5474 O O . HOH I 6 . ? 12.642 10.784 -7.473 1.00 40.86 ? 486 HOH A O 1 HETATM 5475 O O . HOH I 6 . ? 27.487 11.432 12.928 1.00 35.86 ? 487 HOH A O 1 HETATM 5476 O O . HOH I 6 . ? -3.073 24.573 -12.676 1.00 39.53 ? 488 HOH A O 1 HETATM 5477 O O . HOH I 6 . ? -5.367 11.592 -16.221 1.00 52.59 ? 489 HOH A O 1 HETATM 5478 O O . HOH I 6 . ? -10.065 2.090 -10.537 1.00 49.33 ? 490 HOH A O 1 HETATM 5479 O O . HOH I 6 . ? -2.784 -12.987 13.896 1.00 50.75 ? 491 HOH A O 1 HETATM 5480 O O . HOH I 6 . ? 24.767 18.068 19.386 1.00 38.86 ? 492 HOH A O 1 HETATM 5481 O O . HOH I 6 . ? -5.182 5.102 27.783 1.00 42.49 ? 493 HOH A O 1 HETATM 5482 O O . HOH I 6 . ? -1.724 8.703 30.930 1.00 49.63 ? 494 HOH A O 1 HETATM 5483 O O . HOH I 6 . ? 4.198 9.384 33.944 1.00 48.03 ? 495 HOH A O 1 HETATM 5484 O O . HOH I 6 . ? 9.879 14.363 28.739 1.00 45.37 ? 496 HOH A O 1 HETATM 5485 O O . HOH I 6 . ? -8.455 6.570 4.557 1.00 33.31 ? 497 HOH A O 1 HETATM 5486 O O . HOH I 6 . ? -5.313 14.519 -15.952 1.00 47.12 ? 498 HOH A O 1 HETATM 5487 O O . HOH I 6 . ? 21.686 20.375 24.498 1.00 44.77 ? 499 HOH A O 1 HETATM 5488 O O . HOH I 6 . ? -6.742 -8.664 31.906 1.00 50.12 ? 500 HOH A O 1 HETATM 5489 O O . HOH I 6 . ? -6.549 14.022 -3.342 1.00 37.98 ? 501 HOH A O 1 HETATM 5490 O O . HOH I 6 . ? -13.303 -7.159 25.281 1.00 67.63 ? 502 HOH A O 1 HETATM 5491 O O . HOH I 6 . ? 25.986 7.031 17.406 1.00 34.93 ? 503 HOH A O 1 HETATM 5492 O O . HOH I 6 . ? 3.371 29.629 15.599 1.00 50.63 ? 504 HOH A O 1 HETATM 5493 O O . HOH I 6 . ? 0.431 14.526 22.818 1.00 47.38 ? 506 HOH A O 1 HETATM 5494 O O . HOH I 6 . ? -3.621 1.150 6.604 1.00 52.32 ? 508 HOH A O 1 HETATM 5495 O O . HOH I 6 . ? -7.536 10.920 -10.858 1.00 38.29 ? 509 HOH A O 1 HETATM 5496 O O . HOH I 6 . ? 24.332 13.580 1.665 1.00 37.65 ? 510 HOH A O 1 HETATM 5497 O O . HOH I 6 . ? 17.424 22.471 28.442 1.00 62.28 ? 511 HOH A O 1 HETATM 5498 O O . HOH I 6 . ? 18.150 40.075 8.672 1.00 45.78 ? 512 HOH A O 1 HETATM 5499 O O . HOH I 6 . ? 17.049 -6.542 24.849 1.00 61.40 ? 513 HOH A O 1 HETATM 5500 O O . HOH I 6 . ? 22.636 25.702 10.137 1.00 40.24 ? 514 HOH A O 1 HETATM 5501 O O . HOH I 6 . ? -5.019 6.601 29.666 1.00 44.51 ? 515 HOH A O 1 HETATM 5502 O O . HOH I 6 . ? -5.881 18.746 14.876 1.00 46.93 ? 516 HOH A O 1 HETATM 5503 O O . HOH I 6 . ? 26.988 13.857 13.820 1.00 36.84 ? 517 HOH A O 1 HETATM 5504 O O . HOH I 6 . ? 1.569 7.040 33.590 1.00 48.43 ? 518 HOH A O 1 HETATM 5505 O O . HOH I 6 . ? 23.092 21.293 -1.349 1.00 37.44 ? 519 HOH A O 1 HETATM 5506 O O . HOH I 6 . ? -6.638 5.679 12.920 1.00 42.42 ? 520 HOH A O 1 HETATM 5507 O O . HOH I 6 . ? -13.884 6.476 17.981 1.00 40.52 ? 521 HOH A O 1 HETATM 5508 O O . HOH J 6 . ? 32.481 43.543 70.625 1.00 48.70 ? 345 HOH B O 1 HETATM 5509 O O . HOH J 6 . ? 29.388 37.322 61.922 1.00 67.47 ? 346 HOH B O 1 HETATM 5510 O O . HOH J 6 . ? -0.823 34.398 67.557 1.00 19.91 ? 347 HOH B O 1 HETATM 5511 O O . HOH J 6 . ? -8.590 34.114 82.647 1.00 45.98 ? 348 HOH B O 1 HETATM 5512 O O . HOH J 6 . ? 1.086 44.116 77.687 1.00 14.30 ? 349 HOH B O 1 HETATM 5513 O O . HOH J 6 . ? 6.637 33.637 77.412 1.00 25.50 ? 350 HOH B O 1 HETATM 5514 O O . HOH J 6 . ? 22.020 43.110 85.696 1.00 44.02 ? 351 HOH B O 1 HETATM 5515 O O . HOH J 6 . ? 19.978 45.638 70.553 1.00 31.43 ? 352 HOH B O 1 HETATM 5516 O O . HOH J 6 . ? 11.251 40.654 51.955 1.00 51.92 ? 353 HOH B O 1 HETATM 5517 O O . HOH J 6 . ? 15.785 26.357 80.873 1.00 42.87 ? 354 HOH B O 1 HETATM 5518 O O . HOH J 6 . ? -1.879 43.795 74.864 1.00 18.01 ? 355 HOH B O 1 HETATM 5519 O O . HOH J 6 . ? -1.413 34.156 85.325 1.00 22.31 ? 356 HOH B O 1 HETATM 5520 O O . HOH J 6 . ? -5.192 32.343 74.311 1.00 27.18 ? 357 HOH B O 1 HETATM 5521 O O . HOH J 6 . ? -12.224 29.463 89.831 1.00 60.26 ? 358 HOH B O 1 HETATM 5522 O O . HOH J 6 . ? 21.868 24.476 58.990 1.00 49.15 ? 359 HOH B O 1 HETATM 5523 O O . HOH J 6 . ? 20.449 22.092 59.137 1.00 72.86 ? 360 HOH B O 1 HETATM 5524 O O . HOH J 6 . ? -3.111 15.659 71.139 1.00 41.45 ? 361 HOH B O 1 HETATM 5525 O O . HOH J 6 . ? 0.248 14.206 92.217 1.00 29.53 ? 362 HOH B O 1 HETATM 5526 O O . HOH J 6 . ? 0.533 39.326 64.320 1.00 53.62 ? 363 HOH B O 1 HETATM 5527 O O . HOH J 6 . ? 31.468 32.610 75.337 1.00 33.49 ? 364 HOH B O 1 HETATM 5528 O O . HOH J 6 . ? -10.501 35.406 77.263 1.00 44.97 ? 365 HOH B O 1 HETATM 5529 O O . HOH J 6 . ? 11.829 42.852 82.669 1.00 35.98 ? 366 HOH B O 1 HETATM 5530 O O . HOH J 6 . ? 19.591 32.949 96.851 1.00 36.95 ? 367 HOH B O 1 HETATM 5531 O O . HOH J 6 . ? 23.443 42.175 84.455 1.00 33.65 ? 368 HOH B O 1 HETATM 5532 O O . HOH J 6 . ? -19.242 32.486 73.141 1.00 54.03 ? 369 HOH B O 1 HETATM 5533 O O . HOH J 6 . ? 11.756 23.631 95.309 1.00 36.32 ? 370 HOH B O 1 HETATM 5534 O O . HOH J 6 . ? 14.857 41.262 93.629 1.00 75.47 ? 371 HOH B O 1 HETATM 5535 O O . HOH J 6 . ? -0.197 27.828 70.117 1.00 26.96 ? 372 HOH B O 1 HETATM 5536 O O . HOH J 6 . ? 29.105 29.352 65.920 1.00 30.29 ? 373 HOH B O 1 HETATM 5537 O O . HOH J 6 . ? 17.168 26.814 77.312 1.00 24.77 ? 374 HOH B O 1 HETATM 5538 O O . HOH J 6 . ? -1.237 31.714 68.396 1.00 36.66 ? 375 HOH B O 1 HETATM 5539 O O . HOH J 6 . ? -6.895 20.044 97.262 1.00 48.95 ? 376 HOH B O 1 HETATM 5540 O O . HOH J 6 . ? 19.645 24.087 75.349 1.00 29.31 ? 377 HOH B O 1 HETATM 5541 O O . HOH J 6 . ? 19.437 18.424 64.996 1.00 36.52 ? 378 HOH B O 1 HETATM 5542 O O . HOH J 6 . ? 17.416 19.380 82.467 1.00 35.25 ? 379 HOH B O 1 HETATM 5543 O O . HOH J 6 . ? 27.305 30.281 83.557 1.00 31.67 ? 380 HOH B O 1 HETATM 5544 O O . HOH J 6 . ? -8.400 18.200 98.546 1.00 44.29 ? 381 HOH B O 1 HETATM 5545 O O . HOH J 6 . ? -7.755 17.245 97.195 1.00 43.24 ? 382 HOH B O 1 HETATM 5546 O O . HOH J 6 . ? 0.976 13.676 87.556 1.00 33.26 ? 383 HOH B O 1 HETATM 5547 O O . HOH J 6 . ? -21.844 25.229 84.797 1.00 32.61 ? 384 HOH B O 1 HETATM 5548 O O . HOH J 6 . ? 19.186 14.749 75.115 1.00 43.83 ? 385 HOH B O 1 HETATM 5549 O O . HOH J 6 . ? -12.170 1.158 83.760 1.00 40.22 ? 386 HOH B O 1 HETATM 5550 O O . HOH J 6 . ? 23.573 24.342 92.867 1.00 39.20 ? 387 HOH B O 1 HETATM 5551 O O . HOH J 6 . ? -10.912 26.232 90.283 1.00 27.36 ? 388 HOH B O 1 HETATM 5552 O O . HOH J 6 . ? 1.536 27.060 63.421 1.00 32.04 ? 389 HOH B O 1 HETATM 5553 O O . HOH J 6 . ? 11.470 42.654 66.066 1.00 37.57 ? 390 HOH B O 1 HETATM 5554 O O . HOH J 6 . ? -9.445 23.895 66.310 1.00 32.36 ? 391 HOH B O 1 HETATM 5555 O O . HOH J 6 . ? 7.320 22.719 68.152 1.00 35.18 ? 392 HOH B O 1 HETATM 5556 O O . HOH J 6 . ? 6.103 14.140 83.118 1.00 37.50 ? 393 HOH B O 1 HETATM 5557 O O . HOH J 6 . ? 10.883 19.426 78.663 1.00 28.53 ? 394 HOH B O 1 HETATM 5558 O O . HOH J 6 . ? 20.265 26.119 73.801 1.00 30.93 ? 395 HOH B O 1 HETATM 5559 O O . HOH J 6 . ? 10.588 32.807 56.398 1.00 45.01 ? 396 HOH B O 1 HETATM 5560 O O . HOH J 6 . ? -19.401 29.350 82.669 1.00 33.09 ? 397 HOH B O 1 HETATM 5561 O O . HOH J 6 . ? 15.814 40.713 91.446 1.00 30.32 ? 398 HOH B O 1 HETATM 5562 O O . HOH J 6 . ? 27.290 42.605 70.360 1.00 31.71 ? 399 HOH B O 1 HETATM 5563 O O . HOH J 6 . ? 7.501 43.922 78.561 1.00 30.51 ? 400 HOH B O 1 HETATM 5564 O O . HOH J 6 . ? -2.454 25.983 71.601 1.00 22.04 ? 401 HOH B O 1 HETATM 5565 O O . HOH J 6 . ? -4.196 12.475 76.839 1.00 40.93 ? 402 HOH B O 1 HETATM 5566 O O . HOH J 6 . ? 5.340 36.135 88.088 1.00 28.96 ? 403 HOH B O 1 HETATM 5567 O O . HOH J 6 . ? -14.274 36.935 69.812 1.00 34.80 ? 404 HOH B O 1 HETATM 5568 O O . HOH J 6 . ? 18.785 43.247 63.176 1.00 42.18 ? 405 HOH B O 1 HETATM 5569 O O . HOH J 6 . ? -11.609 20.661 94.188 1.00 37.27 ? 406 HOH B O 1 HETATM 5570 O O . HOH J 6 . ? 6.860 44.058 67.121 1.00 41.20 ? 407 HOH B O 1 HETATM 5571 O O . HOH J 6 . ? -12.196 30.416 60.568 1.00 64.90 ? 408 HOH B O 1 HETATM 5572 O O . HOH J 6 . ? 4.117 44.498 80.611 1.00 24.70 ? 409 HOH B O 1 HETATM 5573 O O . HOH J 6 . ? 7.504 14.192 91.422 1.00 34.66 ? 410 HOH B O 1 HETATM 5574 O O . HOH J 6 . ? 7.652 24.413 95.371 1.00 30.15 ? 411 HOH B O 1 HETATM 5575 O O . HOH J 6 . ? 15.454 40.072 80.775 1.00 36.62 ? 412 HOH B O 1 HETATM 5576 O O . HOH J 6 . ? 21.279 11.219 72.731 1.00 52.73 ? 413 HOH B O 1 HETATM 5577 O O . HOH J 6 . ? -3.972 25.137 69.047 1.00 54.26 ? 414 HOH B O 1 HETATM 5578 O O . HOH J 6 . ? 14.903 24.193 95.435 1.00 43.63 ? 415 HOH B O 1 HETATM 5579 O O . HOH J 6 . ? -7.842 33.001 98.008 1.00 31.29 ? 416 HOH B O 1 HETATM 5580 O O . HOH J 6 . ? -14.315 37.214 78.948 1.00 45.69 ? 417 HOH B O 1 HETATM 5581 O O . HOH J 6 . ? 12.802 26.272 72.347 1.00 32.88 ? 418 HOH B O 1 HETATM 5582 O O . HOH J 6 . ? -7.720 12.514 67.563 1.00 40.30 ? 419 HOH B O 1 HETATM 5583 O O . HOH J 6 . ? 12.242 43.990 63.832 1.00 51.73 ? 420 HOH B O 1 HETATM 5584 O O . HOH J 6 . ? -9.677 46.786 80.215 1.00 68.67 ? 421 HOH B O 1 HETATM 5585 O O . HOH J 6 . ? -5.105 29.684 95.033 1.00 33.29 ? 422 HOH B O 1 HETATM 5586 O O . HOH J 6 . ? 14.091 36.502 103.991 1.00 41.00 ? 423 HOH B O 1 HETATM 5587 O O . HOH J 6 . ? 8.372 41.804 63.231 1.00 36.13 ? 424 HOH B O 1 HETATM 5588 O O . HOH J 6 . ? -6.595 27.323 92.835 1.00 60.58 ? 425 HOH B O 1 HETATM 5589 O O . HOH J 6 . ? 8.781 42.535 65.864 1.00 45.29 ? 426 HOH B O 1 HETATM 5590 O O . HOH J 6 . ? -3.327 19.205 72.108 1.00 40.79 ? 427 HOH B O 1 HETATM 5591 O O . HOH J 6 . ? 5.472 12.203 80.896 1.00 50.32 ? 428 HOH B O 1 HETATM 5592 O O . HOH J 6 . ? -1.534 23.792 72.229 1.00 48.54 ? 429 HOH B O 1 HETATM 5593 O O . HOH J 6 . ? 25.577 35.868 63.089 1.00 38.08 ? 430 HOH B O 1 HETATM 5594 O O . HOH J 6 . ? -1.570 13.142 68.228 1.00 38.43 ? 431 HOH B O 1 HETATM 5595 O O . HOH J 6 . ? 25.697 22.104 76.165 1.00 35.43 ? 432 HOH B O 1 HETATM 5596 O O . HOH J 6 . ? -3.794 13.803 69.392 1.00 32.39 ? 433 HOH B O 1 HETATM 5597 O O . HOH J 6 . ? -1.237 13.123 90.073 1.00 38.42 ? 434 HOH B O 1 HETATM 5598 O O . HOH J 6 . ? 13.701 37.962 96.728 1.00 37.65 ? 435 HOH B O 1 HETATM 5599 O O . HOH J 6 . ? -2.480 42.767 79.461 1.00 35.63 ? 436 HOH B O 1 HETATM 5600 O O . HOH J 6 . ? 10.209 34.625 96.283 1.00 49.41 ? 437 HOH B O 1 HETATM 5601 O O . HOH J 6 . ? 9.266 15.219 63.000 1.00 48.78 ? 438 HOH B O 1 HETATM 5602 O O . HOH J 6 . ? 19.644 31.241 55.203 1.00 45.71 ? 439 HOH B O 1 HETATM 5603 O O . HOH J 6 . ? -17.877 34.959 78.653 1.00 57.47 ? 440 HOH B O 1 HETATM 5604 O O . HOH J 6 . ? 5.391 43.303 88.967 1.00 48.79 ? 441 HOH B O 1 HETATM 5605 O O . HOH J 6 . ? -0.923 36.458 98.041 1.00 34.78 ? 442 HOH B O 1 HETATM 5606 O O . HOH J 6 . ? -23.169 28.503 68.547 1.00 57.33 ? 443 HOH B O 1 HETATM 5607 O O . HOH J 6 . ? -11.685 27.945 69.228 1.00 38.51 ? 444 HOH B O 1 HETATM 5608 O O . HOH J 6 . ? 20.684 23.350 92.947 1.00 40.91 ? 445 HOH B O 1 HETATM 5609 O O . HOH J 6 . ? 5.964 15.582 70.305 1.00 52.95 ? 446 HOH B O 1 HETATM 5610 O O . HOH J 6 . ? -7.921 32.610 80.430 1.00 28.80 ? 447 HOH B O 1 HETATM 5611 O O . HOH J 6 . ? -2.811 19.579 65.025 1.00 39.28 ? 448 HOH B O 1 HETATM 5612 O O . HOH J 6 . ? 18.909 15.997 68.967 1.00 44.78 ? 449 HOH B O 1 HETATM 5613 O O . HOH J 6 . ? 1.137 28.555 98.958 1.00 31.44 ? 450 HOH B O 1 HETATM 5614 O O . HOH J 6 . ? 8.896 45.257 53.196 1.00 33.78 ? 451 HOH B O 1 HETATM 5615 O O . HOH J 6 . ? -20.175 15.786 74.210 1.00 38.42 ? 452 HOH B O 1 HETATM 5616 O O . HOH J 6 . ? 20.453 28.865 91.252 1.00 36.49 ? 453 HOH B O 1 HETATM 5617 O O . HOH J 6 . ? 6.593 19.951 74.019 1.00 43.88 ? 454 HOH B O 1 HETATM 5618 O O . HOH J 6 . ? 7.193 16.236 94.911 1.00 39.52 ? 455 HOH B O 1 HETATM 5619 O O . HOH J 6 . ? -0.867 34.094 98.929 1.00 31.22 ? 456 HOH B O 1 HETATM 5620 O O . HOH J 6 . ? 4.342 17.532 96.193 1.00 40.73 ? 457 HOH B O 1 HETATM 5621 O O . HOH J 6 . ? 0.779 28.406 61.210 1.00 40.02 ? 458 HOH B O 1 HETATM 5622 O O . HOH J 6 . ? 32.264 19.358 75.292 1.00 47.84 ? 459 HOH B O 1 HETATM 5623 O O . HOH J 6 . ? -18.783 25.245 87.888 1.00 40.15 ? 460 HOH B O 1 HETATM 5624 O O . HOH J 6 . ? 21.792 22.190 86.802 1.00 40.59 ? 461 HOH B O 1 HETATM 5625 O O . HOH J 6 . ? 8.242 20.017 78.832 1.00 29.03 ? 462 HOH B O 1 HETATM 5626 O O . HOH J 6 . ? -4.833 11.433 69.793 1.00 39.80 ? 463 HOH B O 1 HETATM 5627 O O . HOH J 6 . ? 3.908 20.055 72.388 1.00 47.30 ? 464 HOH B O 1 HETATM 5628 O O . HOH J 6 . ? -7.592 33.925 87.943 1.00 33.81 ? 465 HOH B O 1 HETATM 5629 O O . HOH J 6 . ? -23.908 47.623 69.015 1.00 43.01 ? 466 HOH B O 1 HETATM 5630 O O . HOH J 6 . ? -3.847 14.238 88.511 1.00 39.94 ? 467 HOH B O 1 HETATM 5631 O O . HOH J 6 . ? -1.861 41.374 89.128 1.00 34.02 ? 468 HOH B O 1 HETATM 5632 O O . HOH J 6 . ? -1.001 16.116 93.902 1.00 35.38 ? 469 HOH B O 1 HETATM 5633 O O . HOH J 6 . ? -4.549 26.000 93.740 1.00 32.21 ? 470 HOH B O 1 HETATM 5634 O O . HOH J 6 . ? -1.420 28.857 67.945 1.00 36.25 ? 471 HOH B O 1 HETATM 5635 O O . HOH J 6 . ? 18.011 15.345 72.911 1.00 44.08 ? 472 HOH B O 1 HETATM 5636 O O . HOH J 6 . ? 16.165 15.347 71.086 1.00 49.99 ? 473 HOH B O 1 HETATM 5637 O O . HOH J 6 . ? -3.762 29.457 104.402 1.00 40.34 ? 474 HOH B O 1 HETATM 5638 O O . HOH J 6 . ? 26.111 44.803 69.290 1.00 32.90 ? 475 HOH B O 1 HETATM 5639 O O . HOH J 6 . ? -6.887 48.431 75.548 1.00 44.02 ? 476 HOH B O 1 HETATM 5640 O O . HOH J 6 . ? 11.087 42.248 79.286 1.00 36.33 ? 477 HOH B O 1 HETATM 5641 O O . HOH J 6 . ? 22.854 22.367 91.959 1.00 36.29 ? 478 HOH B O 1 HETATM 5642 O O . HOH J 6 . ? -2.750 41.894 98.926 1.00 55.03 ? 479 HOH B O 1 HETATM 5643 O O . HOH J 6 . ? 16.036 23.806 81.951 1.00 36.29 ? 480 HOH B O 1 HETATM 5644 O O . HOH J 6 . ? 14.595 36.149 47.512 1.00 58.63 ? 481 HOH B O 1 HETATM 5645 O O . HOH J 6 . ? -22.138 44.523 73.054 1.00 46.41 ? 482 HOH B O 1 HETATM 5646 O O . HOH J 6 . ? 25.274 21.275 92.741 1.00 46.80 ? 483 HOH B O 1 HETATM 5647 O O . HOH J 6 . ? -9.227 33.445 76.988 1.00 36.76 ? 484 HOH B O 1 HETATM 5648 O O . HOH J 6 . ? 18.466 41.675 81.465 1.00 46.84 ? 485 HOH B O 1 HETATM 5649 O O . HOH J 6 . ? 20.035 26.743 92.763 1.00 34.95 ? 486 HOH B O 1 HETATM 5650 O O . HOH J 6 . ? -10.072 34.675 87.660 1.00 39.17 ? 487 HOH B O 1 HETATM 5651 O O . HOH J 6 . ? 8.461 36.738 97.834 1.00 45.94 ? 488 HOH B O 1 HETATM 5652 O O . HOH J 6 . ? -2.336 24.325 99.207 1.00 47.58 ? 489 HOH B O 1 HETATM 5653 O O . HOH J 6 . ? 24.403 25.667 77.318 1.00 40.92 ? 490 HOH B O 1 HETATM 5654 O O . HOH J 6 . ? -7.879 35.604 84.444 1.00 45.65 ? 491 HOH B O 1 HETATM 5655 O O . HOH J 6 . ? 1.947 10.918 88.307 1.00 36.32 ? 492 HOH B O 1 HETATM 5656 O O . HOH J 6 . ? 4.304 28.542 55.683 1.00 41.73 ? 493 HOH B O 1 HETATM 5657 O O . HOH J 6 . ? -11.095 11.020 72.643 1.00 48.39 ? 494 HOH B O 1 HETATM 5658 O O . HOH J 6 . ? -0.460 20.712 64.546 1.00 44.72 ? 495 HOH B O 1 HETATM 5659 O O . HOH J 6 . ? 12.085 38.987 91.797 1.00 35.50 ? 496 HOH B O 1 HETATM 5660 O O . HOH J 6 . ? 27.132 46.462 63.713 1.00 44.19 ? 497 HOH B O 1 HETATM 5661 O O . HOH J 6 . ? -27.663 37.172 62.715 1.00 67.63 ? 498 HOH B O 1 HETATM 5662 O O . HOH J 6 . ? -8.471 39.358 90.239 1.00 40.58 ? 499 HOH B O 1 HETATM 5663 O O . HOH J 6 . ? 0.631 27.477 66.460 1.00 51.21 ? 500 HOH B O 1 HETATM 5664 O O . HOH J 6 . ? 1.036 25.373 70.159 1.00 45.80 ? 501 HOH B O 1 HETATM 5665 O O . HOH J 6 . ? 6.067 29.642 96.172 1.00 48.65 ? 502 HOH B O 1 HETATM 5666 O O . HOH J 6 . ? 12.739 36.221 97.982 1.00 40.91 ? 503 HOH B O 1 HETATM 5667 O O . HOH J 6 . ? 8.427 34.063 51.851 1.00 50.18 ? 504 HOH B O 1 HETATM 5668 O O . HOH J 6 . ? 13.390 41.806 90.468 1.00 48.47 ? 505 HOH B O 1 HETATM 5669 O O . HOH J 6 . ? 10.544 19.449 72.491 1.00 53.02 ? 506 HOH B O 1 HETATM 5670 O O . HOH J 6 . ? -6.884 45.915 87.871 1.00 49.83 ? 507 HOH B O 1 HETATM 5671 O O . HOH J 6 . ? 5.387 42.340 92.398 1.00 44.92 ? 508 HOH B O 1 HETATM 5672 O O . HOH J 6 . ? -25.043 44.793 65.569 1.00 71.63 ? 509 HOH B O 1 HETATM 5673 O O . HOH J 6 . ? -3.902 8.242 80.226 1.00 56.29 ? 510 HOH B O 1 HETATM 5674 O O . HOH J 6 . ? 15.366 40.533 88.043 1.00 33.85 ? 511 HOH B O 1 HETATM 5675 O O . HOH J 6 . ? 2.238 22.423 73.215 1.00 28.06 ? 512 HOH B O 1 HETATM 5676 O O . HOH J 6 . ? 1.790 33.303 99.313 1.00 38.67 ? 513 HOH B O 1 HETATM 5677 O O . HOH J 6 . ? -11.630 8.917 85.841 1.00 57.78 ? 514 HOH B O 1 HETATM 5678 O O . HOH J 6 . ? 2.660 25.768 67.395 1.00 42.36 ? 515 HOH B O 1 HETATM 5679 O O . HOH J 6 . ? -21.523 14.017 66.411 1.00 44.13 ? 516 HOH B O 1 HETATM 5680 O O . HOH J 6 . ? 13.787 21.613 72.610 1.00 32.48 ? 517 HOH B O 1 HETATM 5681 O O . HOH J 6 . ? 9.647 32.258 53.068 1.00 49.37 ? 518 HOH B O 1 HETATM 5682 O O . HOH J 6 . ? -13.227 16.788 86.093 1.00 44.85 ? 519 HOH B O 1 HETATM 5683 O O . HOH J 6 . ? -0.746 13.172 65.372 1.00 47.73 ? 520 HOH B O 1 HETATM 5684 O O . HOH J 6 . ? 27.383 31.918 91.289 1.00 41.74 ? 521 HOH B O 1 HETATM 5685 O O . HOH J 6 . ? 5.994 18.151 69.716 1.00 56.03 ? 522 HOH B O 1 HETATM 5686 O O . HOH J 6 . ? -16.734 38.095 79.827 1.00 46.95 ? 523 HOH B O 1 HETATM 5687 O O . HOH J 6 . ? -5.853 28.122 98.734 1.00 62.01 ? 524 HOH B O 1 HETATM 5688 O O . HOH J 6 . ? -23.964 20.546 70.393 1.00 44.06 ? 525 HOH B O 1 HETATM 5689 O O . HOH J 6 . ? 15.791 16.471 59.864 1.00 67.48 ? 526 HOH B O 1 HETATM 5690 O O . HOH J 6 . ? -4.571 44.920 89.289 1.00 42.66 ? 527 HOH B O 1 HETATM 5691 O O . HOH J 6 . ? 33.432 24.101 68.024 1.00 53.66 ? 528 HOH B O 1 HETATM 5692 O O . HOH J 6 . ? 12.833 38.714 103.762 1.00 45.19 ? 529 HOH B O 1 HETATM 5693 O O . HOH J 6 . ? 11.074 14.293 92.769 1.00 46.47 ? 530 HOH B O 1 HETATM 5694 O O . HOH J 6 . ? 15.579 15.621 85.436 1.00 45.32 ? 531 HOH B O 1 HETATM 5695 O O . HOH J 6 . ? 27.824 26.972 78.207 1.00 50.69 ? 532 HOH B O 1 HETATM 5696 O O . HOH J 6 . ? -18.740 27.664 88.890 1.00 59.59 ? 533 HOH B O 1 HETATM 5697 O O . HOH J 6 . ? 0.333 19.393 67.510 1.00 53.56 ? 534 HOH B O 1 HETATM 5698 O O . HOH J 6 . ? -9.083 31.792 69.078 1.00 53.50 ? 535 HOH B O 1 HETATM 5699 O O . HOH J 6 . ? -23.224 41.715 63.281 1.00 63.25 ? 536 HOH B O 1 HETATM 5700 O O . HOH J 6 . ? 24.814 39.865 77.136 1.00 44.84 ? 537 HOH B O 1 HETATM 5701 O O . HOH J 6 . ? 19.188 13.095 79.616 1.00 53.59 ? 538 HOH B O 1 HETATM 5702 O O . HOH J 6 . ? 3.579 9.674 76.489 1.00 44.52 ? 539 HOH B O 1 HETATM 5703 O O . HOH J 6 . ? -8.029 25.479 64.694 1.00 62.20 ? 540 HOH B O 1 HETATM 5704 O O . HOH J 6 . ? 19.025 35.208 104.206 1.00 51.47 ? 541 HOH B O 1 HETATM 5705 O O . HOH J 6 . ? 8.969 38.768 95.775 1.00 55.84 ? 542 HOH B O 1 HETATM 5706 O O . HOH J 6 . ? 5.839 39.960 62.753 1.00 44.41 ? 543 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 LEU 1 1 ? ? ? A . n A 1 2 THR 2 2 ? ? ? A . n A 1 3 LEU 3 3 ? ? ? A . n A 1 4 GLY 4 4 4 GLY GLY A . n A 1 5 ASN 5 5 5 ASN ASN A . n A 1 6 THR 6 6 6 THR THR A . n A 1 7 THR 7 7 7 THR THR A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 VAL 10 10 10 VAL VAL A . n A 1 11 ILE 11 11 11 ILE ILE A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 ASN 14 14 14 ASN ASN A . n A 1 15 TYR 15 15 15 TYR TYR A . n A 1 16 MET 16 16 16 MET MET A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 GLN 19 19 19 GLN GLN A . n A 1 20 TYR 20 20 20 TYR TYR A . n A 1 21 TYR 21 21 21 TYR TYR A . n A 1 22 GLY 22 22 22 GLY GLY A . n A 1 23 GLU 23 23 23 GLU GLU A . n A 1 24 ILE 24 24 24 ILE ILE A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 ILE 26 26 26 ILE ILE A . n A 1 27 GLY 27 27 27 GLY GLY A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 PRO 29 29 29 PRO PRO A . n A 1 30 PRO 30 30 30 PRO PRO A . n A 1 31 GLN 31 31 31 GLN GLN A . n A 1 32 THR 32 32 32 THR THR A . n A 1 33 PHE 33 33 33 PHE PHE A . n A 1 34 LYS 34 34 34 LYS LYS A . n A 1 35 VAL 35 35 35 VAL VAL A . n A 1 36 VAL 36 36 36 VAL VAL A . n A 1 37 PHE 37 37 37 PHE PHE A . n A 1 38 ASP 38 38 38 ASP ASP A . n A 1 39 THR 39 39 39 THR THR A . n A 1 40 GLY 40 40 40 GLY GLY A . n A 1 41 SER 41 41 41 SER SER A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 ASN 43 43 43 ASN ASN A . n A 1 44 VAL 44 44 44 VAL VAL A . n A 1 45 TRP 45 45 45 TRP TRP A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 PRO 47 47 47 PRO PRO A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 SER 49 49 49 SER SER A . n A 1 50 LYS 50 50 50 LYS LYS A . n A 1 51 CYS 51 51 51 CYS CYS A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 LEU 54 54 54 LEU LEU A . n A 1 55 TYR 55 55 55 TYR TYR A . n A 1 56 THR 56 56 56 THR THR A . n A 1 57 ALA 57 57 57 ALA ALA A . n A 1 58 CYS 58 58 58 CYS CYS A . n A 1 59 VAL 59 59 59 VAL VAL A . n A 1 60 TYR 60 60 60 TYR TYR A . n A 1 61 HIS 61 61 61 HIS HIS A . n A 1 62 LYS 62 62 62 LYS LYS A . n A 1 63 LEU 63 63 63 LEU LEU A . n A 1 64 PHE 64 64 64 PHE PHE A . n A 1 65 ASP 65 65 65 ASP ASP A . n A 1 66 ALA 66 66 66 ALA ALA A . n A 1 67 SER 67 67 67 SER SER A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 SER 69 69 69 SER SER A . n A 1 70 SER 70 70 70 SER SER A . n A 1 71 SER 71 71 71 SER SER A . n A 1 72 TYR 72 72 72 TYR TYR A . n A 1 73 LYS 73 73 73 LYS LYS A . n A 1 74 HIS 74 74 74 HIS HIS A . n A 1 75 ASN 75 75 75 ASN ASN A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 THR 77 77 77 THR THR A . n A 1 78 GLU 78 78 78 GLU GLU A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 LEU 81 81 81 LEU LEU A . n A 1 82 ARG 82 82 82 ARG ARG A . n A 1 83 TYR 83 83 83 TYR TYR A . n A 1 84 SER 84 84 84 SER SER A . n A 1 85 THR 85 85 85 THR THR A . n A 1 86 GLY 86 86 86 GLY GLY A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 VAL 88 88 88 VAL VAL A . n A 1 89 SER 89 89 89 SER SER A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 PHE 91 91 91 PHE PHE A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 SER 93 93 93 SER SER A . n A 1 94 GLN 94 94 94 GLN GLN A . n A 1 95 ASP 95 95 95 ASP ASP A . n A 1 96 ILE 96 96 96 ILE ILE A . n A 1 97 ILE 97 97 97 ILE ILE A . n A 1 98 THR 98 98 98 THR THR A . n A 1 99 VAL 99 99 99 VAL VAL A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 GLY 101 101 101 GLY GLY A . n A 1 102 ILE 102 102 102 ILE ILE A . n A 1 103 THR 103 103 103 THR THR A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 THR 105 105 105 THR THR A . n A 1 106 GLN 106 106 106 GLN GLN A . n A 1 107 MET 107 107 107 MET MET A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 GLY 109 109 109 GLY GLY A . n A 1 110 GLU 110 110 110 GLU GLU A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 MET 114 114 114 MET MET A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 ALA 116 116 116 ALA ALA A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 PHE 119 119 119 PHE PHE A . n A 1 120 MET 120 120 120 MET MET A . n A 1 121 LEU 121 121 121 LEU LEU A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 PHE 124 124 124 PHE PHE A . n A 1 125 ASP 125 125 125 ASP ASP A . n A 1 126 GLY 126 126 126 GLY GLY A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 MET 130 130 130 MET MET A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 PHE 132 132 132 PHE PHE A . n A 1 133 ILE 133 133 133 ILE ILE A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 GLN 135 135 135 GLN GLN A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 ILE 137 137 137 ILE ILE A . n A 1 138 GLY 138 138 138 GLY GLY A . n A 1 139 ARG 139 139 139 ARG ARG A . n A 1 140 VAL 140 140 140 VAL VAL A . n A 1 141 THR 141 141 141 THR THR A . n A 1 142 PRO 142 142 142 PRO PRO A . n A 1 143 ILE 143 143 143 ILE ILE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ASP 145 145 145 ASP ASP A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 ILE 147 147 147 ILE ILE A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 GLN 150 150 150 GLN GLN A . n A 1 151 GLY 151 151 151 GLY GLY A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 LEU 153 153 153 LEU LEU A . n A 1 154 LYS 154 154 154 LYS LYS A . n A 1 155 GLU 155 155 155 GLU GLU A . n A 1 156 ASP 156 156 156 ASP ASP A . n A 1 157 VAL 157 157 157 VAL VAL A . n A 1 158 PHE 158 158 158 PHE PHE A . n A 1 159 SER 159 159 159 SER SER A . n A 1 160 PHE 160 160 160 PHE PHE A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 TYR 162 162 162 TYR TYR A . n A 1 163 ASN 163 163 163 ASN ASN A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 SER 166 166 166 SER SER A . n A 1 167 GLU 167 167 ? ? ? A . n A 1 168 ASN 168 168 ? ? ? A . n A 1 169 SER 169 169 ? ? ? A . n A 1 170 GLN 170 170 ? ? ? A . n A 1 171 SER 171 171 171 SER SER A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 GLY 173 173 173 GLY GLY A . n A 1 174 GLY 174 174 174 GLY GLY A . n A 1 175 GLN 175 175 175 GLN GLN A . n A 1 176 ILE 176 176 176 ILE ILE A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 LEU 178 178 178 LEU LEU A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 GLY 180 180 180 GLY GLY A . n A 1 181 SER 181 181 181 SER SER A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 PRO 183 183 183 PRO PRO A . n A 1 184 GLN 184 184 184 GLN GLN A . n A 1 185 HIS 185 185 185 HIS HIS A . n A 1 186 TYR 186 186 186 TYR TYR A . n A 1 187 GLU 187 187 187 GLU GLU A . n A 1 188 GLY 188 188 188 GLY GLY A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 PHE 190 190 190 PHE PHE A . n A 1 191 HIS 191 191 191 HIS HIS A . n A 1 192 TYR 192 192 192 TYR TYR A . n A 1 193 ILE 193 193 193 ILE ILE A . n A 1 194 ASN 194 194 194 ASN ASN A . n A 1 195 LEU 195 195 195 LEU LEU A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 LYS 197 197 197 LYS LYS A . n A 1 198 THR 198 198 198 THR THR A . n A 1 199 GLY 199 199 199 GLY GLY A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 TRP 201 201 201 TRP TRP A . n A 1 202 GLN 202 202 202 GLN GLN A . n A 1 203 ILE 203 203 203 ILE ILE A . n A 1 204 GLN 204 204 204 GLN GLN A . n A 1 205 MET 205 205 205 MET MET A . n A 1 206 LYS 206 206 206 LYS LYS A . n A 1 207 GLY 207 207 207 GLY GLY A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 SER 209 209 209 SER SER A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 GLY 211 211 211 GLY GLY A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 THR 214 214 214 THR THR A . n A 1 215 LEU 215 215 215 LEU LEU A . n A 1 216 LEU 216 216 216 LEU LEU A . n A 1 217 CYS 217 217 217 CYS CYS A . n A 1 218 GLU 218 218 218 GLU GLU A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 CYS 221 221 221 CYS CYS A . n A 1 222 LEU 222 222 222 LEU LEU A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 THR 227 227 227 THR THR A . n A 1 228 GLY 228 228 228 GLY GLY A . n A 1 229 ALA 229 229 229 ALA ALA A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 TYR 231 231 231 TYR TYR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 GLY 234 234 234 GLY GLY A . n A 1 235 SER 235 235 235 SER SER A . n A 1 236 THR 236 236 236 THR THR A . n A 1 237 SER 237 237 237 SER SER A . n A 1 238 SER 238 238 238 SER SER A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 GLU 240 240 240 GLU GLU A . n A 1 241 LYS 241 241 241 LYS LYS A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 MET 243 243 243 MET MET A . n A 1 244 GLU 244 244 244 GLU GLU A . n A 1 245 ALA 245 245 245 ALA ALA A . n A 1 246 LEU 246 246 246 LEU LEU A . n A 1 247 GLY 247 247 247 GLY GLY A . n A 1 248 ALA 248 248 248 ALA ALA A . n A 1 249 LYS 249 249 249 LYS LYS A . n A 1 250 LYS 250 250 250 LYS LYS A . n A 1 251 ARG 251 251 251 ARG ARG A . n A 1 252 LEU 252 252 252 LEU LEU A . n A 1 253 PHE 253 253 253 PHE PHE A . n A 1 254 ASP 254 254 254 ASP ASP A . n A 1 255 TYR 255 255 255 TYR TYR A . n A 1 256 VAL 256 256 256 VAL VAL A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 CYS 259 259 259 CYS CYS A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 GLU 261 261 261 GLU GLU A . n A 1 262 GLY 262 262 262 GLY GLY A . n A 1 263 PRO 263 263 263 PRO PRO A . n A 1 264 THR 264 264 264 THR THR A . n A 1 265 LEU 265 265 265 LEU LEU A . n A 1 266 PRO 266 266 266 PRO PRO A . n A 1 267 ASP 267 267 267 ASP ASP A . n A 1 268 ILE 268 268 268 ILE ILE A . n A 1 269 SER 269 269 269 SER SER A . n A 1 270 PHE 270 270 270 PHE PHE A . n A 1 271 HIS 271 271 271 HIS HIS A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 GLY 273 273 273 GLY GLY A . n A 1 274 GLY 274 274 274 GLY GLY A . n A 1 275 LYS 275 275 275 LYS LYS A . n A 1 276 GLU 276 276 276 GLU GLU A . n A 1 277 TYR 277 277 277 TYR TYR A . n A 1 278 THR 278 278 278 THR THR A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 SER 281 281 281 SER SER A . n A 1 282 ALA 282 282 282 ALA ALA A . n A 1 283 ASP 283 283 283 ASP ASP A . n A 1 284 TYR 284 284 284 TYR TYR A . n A 1 285 VAL 285 285 285 VAL VAL A . n A 1 286 PHE 286 286 286 PHE PHE A . n A 1 287 GLN 287 287 287 GLN GLN A . n A 1 288 GLU 288 288 288 GLU GLU A . n A 1 289 SER 289 289 289 SER SER A . n A 1 290 TYR 290 290 290 TYR TYR A . n A 1 291 SER 291 291 291 SER SER A . n A 1 292 SER 292 292 292 SER SER A . n A 1 293 LYS 293 293 293 LYS LYS A . n A 1 294 LYS 294 294 294 LYS LYS A . n A 1 295 LEU 295 295 295 LEU LEU A . n A 1 296 CYS 296 296 296 CYS CYS A . n A 1 297 THR 297 297 297 THR THR A . n A 1 298 LEU 298 298 298 LEU LEU A . n A 1 299 ALA 299 299 299 ALA ALA A . n A 1 300 ILE 300 300 300 ILE ILE A . n A 1 301 HIS 301 301 301 HIS HIS A . n A 1 302 ALA 302 302 302 ALA ALA A . n A 1 303 MET 303 303 303 MET MET A . n A 1 304 ASP 304 304 304 ASP ASP A . n A 1 305 ILE 305 305 305 ILE ILE A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 PRO 307 307 307 PRO PRO A . n A 1 308 PRO 308 308 308 PRO PRO A . n A 1 309 THR 309 309 309 THR THR A . n A 1 310 GLY 310 310 310 GLY GLY A . n A 1 311 PRO 311 311 311 PRO PRO A . n A 1 312 THR 312 312 312 THR THR A . n A 1 313 TRP 313 313 313 TRP TRP A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 LEU 315 315 315 LEU LEU A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 PHE 319 319 319 PHE PHE A . n A 1 320 ILE 320 320 320 ILE ILE A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 LYS 322 322 322 LYS LYS A . n A 1 323 PHE 323 323 323 PHE PHE A . n A 1 324 TYR 324 324 324 TYR TYR A . n A 1 325 THR 325 325 325 THR THR A . n A 1 326 GLU 326 326 326 GLU GLU A . n A 1 327 PHE 327 327 327 PHE PHE A . n A 1 328 ASP 328 328 328 ASP ASP A . n A 1 329 ARG 329 329 329 ARG ARG A . n A 1 330 ARG 330 330 330 ARG ARG A . n A 1 331 ASN 331 331 331 ASN ASN A . n A 1 332 ASN 332 332 332 ASN ASN A . n A 1 333 ARG 333 333 333 ARG ARG A . n A 1 334 ILE 334 334 334 ILE ILE A . n A 1 335 GLY 335 335 335 GLY GLY A . n A 1 336 PHE 336 336 336 PHE PHE A . n A 1 337 ALA 337 337 337 ALA ALA A . n A 1 338 LEU 338 338 338 LEU LEU A . n A 1 339 ALA 339 339 339 ALA ALA A . n A 1 340 ARG 340 340 340 ARG ARG A . n A 1 341 HIS 341 341 341 HIS HIS A . n B 1 1 LEU 1 1 1 LEU LEU B . n B 1 2 THR 2 2 2 THR THR B . n B 1 3 LEU 3 3 3 LEU LEU B . n B 1 4 GLY 4 4 4 GLY GLY B . n B 1 5 ASN 5 5 5 ASN ASN B . n B 1 6 THR 6 6 6 THR THR B . n B 1 7 THR 7 7 7 THR THR B . n B 1 8 SER 8 8 8 SER SER B . n B 1 9 SER 9 9 9 SER SER B . n B 1 10 VAL 10 10 10 VAL VAL B . n B 1 11 ILE 11 11 11 ILE ILE B . n B 1 12 LEU 12 12 12 LEU LEU B . n B 1 13 THR 13 13 13 THR THR B . n B 1 14 ASN 14 14 14 ASN ASN B . n B 1 15 TYR 15 15 15 TYR TYR B . n B 1 16 MET 16 16 16 MET MET B . n B 1 17 ASP 17 17 17 ASP ASP B . n B 1 18 THR 18 18 18 THR THR B . n B 1 19 GLN 19 19 19 GLN GLN B . n B 1 20 TYR 20 20 20 TYR TYR B . n B 1 21 TYR 21 21 21 TYR TYR B . n B 1 22 GLY 22 22 22 GLY GLY B . n B 1 23 GLU 23 23 23 GLU GLU B . n B 1 24 ILE 24 24 24 ILE ILE B . n B 1 25 GLY 25 25 25 GLY GLY B . n B 1 26 ILE 26 26 26 ILE ILE B . n B 1 27 GLY 27 27 27 GLY GLY B . n B 1 28 THR 28 28 28 THR THR B . n B 1 29 PRO 29 29 29 PRO PRO B . n B 1 30 PRO 30 30 30 PRO PRO B . n B 1 31 GLN 31 31 31 GLN GLN B . n B 1 32 THR 32 32 32 THR THR B . n B 1 33 PHE 33 33 33 PHE PHE B . n B 1 34 LYS 34 34 34 LYS LYS B . n B 1 35 VAL 35 35 35 VAL VAL B . n B 1 36 VAL 36 36 36 VAL VAL B . n B 1 37 PHE 37 37 37 PHE PHE B . n B 1 38 ASP 38 38 38 ASP ASP B . n B 1 39 THR 39 39 39 THR THR B . n B 1 40 GLY 40 40 40 GLY GLY B . n B 1 41 SER 41 41 41 SER SER B . n B 1 42 SER 42 42 42 SER SER B . n B 1 43 ASN 43 43 43 ASN ASN B . n B 1 44 VAL 44 44 44 VAL VAL B . n B 1 45 TRP 45 45 45 TRP TRP B . n B 1 46 VAL 46 46 46 VAL VAL B . n B 1 47 PRO 47 47 47 PRO PRO B . n B 1 48 SER 48 48 48 SER SER B . n B 1 49 SER 49 49 49 SER SER B . n B 1 50 LYS 50 50 50 LYS LYS B . n B 1 51 CYS 51 51 51 CYS CYS B . n B 1 52 SER 52 52 52 SER SER B . n B 1 53 ARG 53 53 53 ARG ARG B . n B 1 54 LEU 54 54 54 LEU LEU B . n B 1 55 TYR 55 55 55 TYR TYR B . n B 1 56 THR 56 56 56 THR THR B . n B 1 57 ALA 57 57 57 ALA ALA B . n B 1 58 CYS 58 58 58 CYS CYS B . n B 1 59 VAL 59 59 59 VAL VAL B . n B 1 60 TYR 60 60 60 TYR TYR B . n B 1 61 HIS 61 61 61 HIS HIS B . n B 1 62 LYS 62 62 62 LYS LYS B . n B 1 63 LEU 63 63 63 LEU LEU B . n B 1 64 PHE 64 64 64 PHE PHE B . n B 1 65 ASP 65 65 65 ASP ASP B . n B 1 66 ALA 66 66 66 ALA ALA B . n B 1 67 SER 67 67 67 SER SER B . n B 1 68 ASP 68 68 68 ASP ASP B . n B 1 69 SER 69 69 69 SER SER B . n B 1 70 SER 70 70 70 SER SER B . n B 1 71 SER 71 71 71 SER SER B . n B 1 72 TYR 72 72 72 TYR TYR B . n B 1 73 LYS 73 73 73 LYS LYS B . n B 1 74 HIS 74 74 74 HIS HIS B . n B 1 75 ASN 75 75 75 ASN ASN B . n B 1 76 GLY 76 76 76 GLY GLY B . n B 1 77 THR 77 77 77 THR THR B . n B 1 78 GLU 78 78 78 GLU GLU B . n B 1 79 LEU 79 79 79 LEU LEU B . n B 1 80 THR 80 80 80 THR THR B . n B 1 81 LEU 81 81 81 LEU LEU B . n B 1 82 ARG 82 82 82 ARG ARG B . n B 1 83 TYR 83 83 83 TYR TYR B . n B 1 84 SER 84 84 84 SER SER B . n B 1 85 THR 85 85 85 THR THR B . n B 1 86 GLY 86 86 86 GLY GLY B . n B 1 87 THR 87 87 87 THR THR B . n B 1 88 VAL 88 88 88 VAL VAL B . n B 1 89 SER 89 89 89 SER SER B . n B 1 90 GLY 90 90 90 GLY GLY B . n B 1 91 PHE 91 91 91 PHE PHE B . n B 1 92 LEU 92 92 92 LEU LEU B . n B 1 93 SER 93 93 93 SER SER B . n B 1 94 GLN 94 94 94 GLN GLN B . n B 1 95 ASP 95 95 95 ASP ASP B . n B 1 96 ILE 96 96 96 ILE ILE B . n B 1 97 ILE 97 97 97 ILE ILE B . n B 1 98 THR 98 98 98 THR THR B . n B 1 99 VAL 99 99 99 VAL VAL B . n B 1 100 GLY 100 100 100 GLY GLY B . n B 1 101 GLY 101 101 101 GLY GLY B . n B 1 102 ILE 102 102 102 ILE ILE B . n B 1 103 THR 103 103 103 THR THR B . n B 1 104 VAL 104 104 104 VAL VAL B . n B 1 105 THR 105 105 105 THR THR B . n B 1 106 GLN 106 106 106 GLN GLN B . n B 1 107 MET 107 107 107 MET MET B . n B 1 108 PHE 108 108 108 PHE PHE B . n B 1 109 GLY 109 109 109 GLY GLY B . n B 1 110 GLU 110 110 110 GLU GLU B . n B 1 111 VAL 111 111 111 VAL VAL B . n B 1 112 THR 112 112 112 THR THR B . n B 1 113 GLU 113 113 113 GLU GLU B . n B 1 114 MET 114 114 114 MET MET B . n B 1 115 PRO 115 115 115 PRO PRO B . n B 1 116 ALA 116 116 116 ALA ALA B . n B 1 117 LEU 117 117 117 LEU LEU B . n B 1 118 PRO 118 118 118 PRO PRO B . n B 1 119 PHE 119 119 119 PHE PHE B . n B 1 120 MET 120 120 120 MET MET B . n B 1 121 LEU 121 121 121 LEU LEU B . n B 1 122 ALA 122 122 122 ALA ALA B . n B 1 123 GLU 123 123 123 GLU GLU B . n B 1 124 PHE 124 124 124 PHE PHE B . n B 1 125 ASP 125 125 125 ASP ASP B . n B 1 126 GLY 126 126 126 GLY GLY B . n B 1 127 VAL 127 127 127 VAL VAL B . n B 1 128 VAL 128 128 128 VAL VAL B . n B 1 129 GLY 129 129 129 GLY GLY B . n B 1 130 MET 130 130 130 MET MET B . n B 1 131 GLY 131 131 131 GLY GLY B . n B 1 132 PHE 132 132 132 PHE PHE B . n B 1 133 ILE 133 133 133 ILE ILE B . n B 1 134 GLU 134 134 134 GLU GLU B . n B 1 135 GLN 135 135 135 GLN GLN B . n B 1 136 ALA 136 136 136 ALA ALA B . n B 1 137 ILE 137 137 137 ILE ILE B . n B 1 138 GLY 138 138 138 GLY GLY B . n B 1 139 ARG 139 139 139 ARG ARG B . n B 1 140 VAL 140 140 140 VAL VAL B . n B 1 141 THR 141 141 141 THR THR B . n B 1 142 PRO 142 142 142 PRO PRO B . n B 1 143 ILE 143 143 143 ILE ILE B . n B 1 144 PHE 144 144 144 PHE PHE B . n B 1 145 ASP 145 145 145 ASP ASP B . n B 1 146 ASN 146 146 146 ASN ASN B . n B 1 147 ILE 147 147 147 ILE ILE B . n B 1 148 ILE 148 148 148 ILE ILE B . n B 1 149 SER 149 149 149 SER SER B . n B 1 150 GLN 150 150 150 GLN GLN B . n B 1 151 GLY 151 151 151 GLY GLY B . n B 1 152 VAL 152 152 152 VAL VAL B . n B 1 153 LEU 153 153 153 LEU LEU B . n B 1 154 LYS 154 154 154 LYS LYS B . n B 1 155 GLU 155 155 155 GLU GLU B . n B 1 156 ASP 156 156 156 ASP ASP B . n B 1 157 VAL 157 157 157 VAL VAL B . n B 1 158 PHE 158 158 158 PHE PHE B . n B 1 159 SER 159 159 159 SER SER B . n B 1 160 PHE 160 160 160 PHE PHE B . n B 1 161 TYR 161 161 161 TYR TYR B . n B 1 162 TYR 162 162 162 TYR TYR B . n B 1 163 ASN 163 163 163 ASN ASN B . n B 1 164 ARG 164 164 164 ARG ARG B . n B 1 165 ASP 165 165 165 ASP ASP B . n B 1 166 SER 166 166 166 SER SER B . n B 1 167 GLU 167 167 ? ? ? B . n B 1 168 ASN 168 168 ? ? ? B . n B 1 169 SER 169 169 ? ? ? B . n B 1 170 GLN 170 170 ? ? ? B . n B 1 171 SER 171 171 171 SER SER B . n B 1 172 LEU 172 172 172 LEU LEU B . n B 1 173 GLY 173 173 173 GLY GLY B . n B 1 174 GLY 174 174 174 GLY GLY B . n B 1 175 GLN 175 175 175 GLN GLN B . n B 1 176 ILE 176 176 176 ILE ILE B . n B 1 177 VAL 177 177 177 VAL VAL B . n B 1 178 LEU 178 178 178 LEU LEU B . n B 1 179 GLY 179 179 179 GLY GLY B . n B 1 180 GLY 180 180 180 GLY GLY B . n B 1 181 SER 181 181 181 SER SER B . n B 1 182 ASP 182 182 182 ASP ASP B . n B 1 183 PRO 183 183 183 PRO PRO B . n B 1 184 GLN 184 184 184 GLN GLN B . n B 1 185 HIS 185 185 185 HIS HIS B . n B 1 186 TYR 186 186 186 TYR TYR B . n B 1 187 GLU 187 187 187 GLU GLU B . n B 1 188 GLY 188 188 188 GLY GLY B . n B 1 189 ASN 189 189 189 ASN ASN B . n B 1 190 PHE 190 190 190 PHE PHE B . n B 1 191 HIS 191 191 191 HIS HIS B . n B 1 192 TYR 192 192 192 TYR TYR B . n B 1 193 ILE 193 193 193 ILE ILE B . n B 1 194 ASN 194 194 194 ASN ASN B . n B 1 195 LEU 195 195 195 LEU LEU B . n B 1 196 ILE 196 196 196 ILE ILE B . n B 1 197 LYS 197 197 197 LYS LYS B . n B 1 198 THR 198 198 198 THR THR B . n B 1 199 GLY 199 199 199 GLY GLY B . n B 1 200 VAL 200 200 200 VAL VAL B . n B 1 201 TRP 201 201 201 TRP TRP B . n B 1 202 GLN 202 202 202 GLN GLN B . n B 1 203 ILE 203 203 203 ILE ILE B . n B 1 204 GLN 204 204 204 GLN GLN B . n B 1 205 MET 205 205 205 MET MET B . n B 1 206 LYS 206 206 206 LYS LYS B . n B 1 207 GLY 207 207 207 GLY GLY B . n B 1 208 VAL 208 208 208 VAL VAL B . n B 1 209 SER 209 209 209 SER SER B . n B 1 210 VAL 210 210 210 VAL VAL B . n B 1 211 GLY 211 211 211 GLY GLY B . n B 1 212 SER 212 212 212 SER SER B . n B 1 213 SER 213 213 213 SER SER B . n B 1 214 THR 214 214 214 THR THR B . n B 1 215 LEU 215 215 215 LEU LEU B . n B 1 216 LEU 216 216 216 LEU LEU B . n B 1 217 CYS 217 217 217 CYS CYS B . n B 1 218 GLU 218 218 218 GLU GLU B . n B 1 219 ASP 219 219 219 ASP ASP B . n B 1 220 GLY 220 220 220 GLY GLY B . n B 1 221 CYS 221 221 221 CYS CYS B . n B 1 222 LEU 222 222 222 LEU LEU B . n B 1 223 ALA 223 223 223 ALA ALA B . n B 1 224 LEU 224 224 224 LEU LEU B . n B 1 225 VAL 225 225 225 VAL VAL B . n B 1 226 ASP 226 226 226 ASP ASP B . n B 1 227 THR 227 227 227 THR THR B . n B 1 228 GLY 228 228 228 GLY GLY B . n B 1 229 ALA 229 229 229 ALA ALA B . n B 1 230 SER 230 230 230 SER SER B . n B 1 231 TYR 231 231 231 TYR TYR B . n B 1 232 ILE 232 232 232 ILE ILE B . n B 1 233 SER 233 233 233 SER SER B . n B 1 234 GLY 234 234 234 GLY GLY B . n B 1 235 SER 235 235 235 SER SER B . n B 1 236 THR 236 236 236 THR THR B . n B 1 237 SER 237 237 237 SER SER B . n B 1 238 SER 238 238 238 SER SER B . n B 1 239 ILE 239 239 239 ILE ILE B . n B 1 240 GLU 240 240 240 GLU GLU B . n B 1 241 LYS 241 241 241 LYS LYS B . n B 1 242 LEU 242 242 242 LEU LEU B . n B 1 243 MET 243 243 243 MET MET B . n B 1 244 GLU 244 244 244 GLU GLU B . n B 1 245 ALA 245 245 245 ALA ALA B . n B 1 246 LEU 246 246 246 LEU LEU B . n B 1 247 GLY 247 247 247 GLY GLY B . n B 1 248 ALA 248 248 248 ALA ALA B . n B 1 249 LYS 249 249 249 LYS LYS B . n B 1 250 LYS 250 250 250 LYS LYS B . n B 1 251 ARG 251 251 251 ARG ARG B . n B 1 252 LEU 252 252 252 LEU LEU B . n B 1 253 PHE 253 253 253 PHE PHE B . n B 1 254 ASP 254 254 254 ASP ASP B . n B 1 255 TYR 255 255 255 TYR TYR B . n B 1 256 VAL 256 256 256 VAL VAL B . n B 1 257 VAL 257 257 257 VAL VAL B . n B 1 258 LYS 258 258 258 LYS LYS B . n B 1 259 CYS 259 259 259 CYS CYS B . n B 1 260 ASN 260 260 260 ASN ASN B . n B 1 261 GLU 261 261 261 GLU GLU B . n B 1 262 GLY 262 262 262 GLY GLY B . n B 1 263 PRO 263 263 263 PRO PRO B . n B 1 264 THR 264 264 264 THR THR B . n B 1 265 LEU 265 265 265 LEU LEU B . n B 1 266 PRO 266 266 266 PRO PRO B . n B 1 267 ASP 267 267 267 ASP ASP B . n B 1 268 ILE 268 268 268 ILE ILE B . n B 1 269 SER 269 269 269 SER SER B . n B 1 270 PHE 270 270 270 PHE PHE B . n B 1 271 HIS 271 271 271 HIS HIS B . n B 1 272 LEU 272 272 272 LEU LEU B . n B 1 273 GLY 273 273 273 GLY GLY B . n B 1 274 GLY 274 274 274 GLY GLY B . n B 1 275 LYS 275 275 275 LYS LYS B . n B 1 276 GLU 276 276 276 GLU GLU B . n B 1 277 TYR 277 277 277 TYR TYR B . n B 1 278 THR 278 278 278 THR THR B . n B 1 279 LEU 279 279 279 LEU LEU B . n B 1 280 THR 280 280 280 THR THR B . n B 1 281 SER 281 281 281 SER SER B . n B 1 282 ALA 282 282 282 ALA ALA B . n B 1 283 ASP 283 283 283 ASP ASP B . n B 1 284 TYR 284 284 284 TYR TYR B . n B 1 285 VAL 285 285 285 VAL VAL B . n B 1 286 PHE 286 286 286 PHE PHE B . n B 1 287 GLN 287 287 287 GLN GLN B . n B 1 288 GLU 288 288 288 GLU GLU B . n B 1 289 SER 289 289 289 SER SER B . n B 1 290 TYR 290 290 290 TYR TYR B . n B 1 291 SER 291 291 291 SER SER B . n B 1 292 SER 292 292 292 SER SER B . n B 1 293 LYS 293 293 293 LYS LYS B . n B 1 294 LYS 294 294 294 LYS LYS B . n B 1 295 LEU 295 295 295 LEU LEU B . n B 1 296 CYS 296 296 296 CYS CYS B . n B 1 297 THR 297 297 297 THR THR B . n B 1 298 LEU 298 298 298 LEU LEU B . n B 1 299 ALA 299 299 299 ALA ALA B . n B 1 300 ILE 300 300 300 ILE ILE B . n B 1 301 HIS 301 301 301 HIS HIS B . n B 1 302 ALA 302 302 302 ALA ALA B . n B 1 303 MET 303 303 303 MET MET B . n B 1 304 ASP 304 304 304 ASP ASP B . n B 1 305 ILE 305 305 305 ILE ILE B . n B 1 306 PRO 306 306 306 PRO PRO B . n B 1 307 PRO 307 307 307 PRO PRO B . n B 1 308 PRO 308 308 308 PRO PRO B . n B 1 309 THR 309 309 309 THR THR B . n B 1 310 GLY 310 310 310 GLY GLY B . n B 1 311 PRO 311 311 311 PRO PRO B . n B 1 312 THR 312 312 312 THR THR B . n B 1 313 TRP 313 313 313 TRP TRP B . n B 1 314 ALA 314 314 314 ALA ALA B . n B 1 315 LEU 315 315 315 LEU LEU B . n B 1 316 GLY 316 316 316 GLY GLY B . n B 1 317 ALA 317 317 317 ALA ALA B . n B 1 318 THR 318 318 318 THR THR B . n B 1 319 PHE 319 319 319 PHE PHE B . n B 1 320 ILE 320 320 320 ILE ILE B . n B 1 321 ARG 321 321 321 ARG ARG B . n B 1 322 LYS 322 322 322 LYS LYS B . n B 1 323 PHE 323 323 323 PHE PHE B . n B 1 324 TYR 324 324 324 TYR TYR B . n B 1 325 THR 325 325 325 THR THR B . n B 1 326 GLU 326 326 326 GLU GLU B . n B 1 327 PHE 327 327 327 PHE PHE B . n B 1 328 ASP 328 328 328 ASP ASP B . n B 1 329 ARG 329 329 329 ARG ARG B . n B 1 330 ARG 330 330 330 ARG ARG B . n B 1 331 ASN 331 331 331 ASN ASN B . n B 1 332 ASN 332 332 332 ASN ASN B . n B 1 333 ARG 333 333 333 ARG ARG B . n B 1 334 ILE 334 334 334 ILE ILE B . n B 1 335 GLY 335 335 335 GLY GLY B . n B 1 336 PHE 336 336 336 PHE PHE B . n B 1 337 ALA 337 337 337 ALA ALA B . n B 1 338 LEU 338 338 338 LEU LEU B . n B 1 339 ALA 339 339 339 ALA ALA B . n B 1 340 ARG 340 340 340 ARG ARG B . n B 1 341 HIS 341 341 341 HIS HIS 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 A ASN 75 A ASN 75 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 75 B ASN 75 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 3 software_defined_assembly PISA dimeric 2 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,I 2 1 B,F,G,H,J 3 1 A,C,D,E,I 3 2 B,F,G,H,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 3 'ABSA (A^2)' 2510 ? 3 MORE 5 ? 3 'SSA (A^2)' 28490 ? # 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_545 -x,y-1/2,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 -44.7300000000 0.0000000000 0.0000000000 -1.0000000000 59.1850000000 # 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 2009-06-30 2 'Structure model' 1 1 2011-07-13 # _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' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal MAR345dtb 'data collection' . ? 1 MOLREP phasing . ? 2 REFMAC refinement 5.2.0003 ? 3 MOSFLM 'data reduction' . ? 4 SCALA 'data scaling' . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O B HOH 381 ? ? O B HOH 382 ? ? 1.78 2 1 CG2 B VAL 257 ? ? O B HOH 369 ? ? 1.99 3 1 O B HOH 351 ? ? O B HOH 368 ? ? 2.11 4 1 ND2 B ASN 75 ? ? O B NDG 344 ? ? 2.17 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 370 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 B _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 371 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 4_456 _pdbx_validate_symm_contact.dist 2.02 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 145 ? ? CG A ASP 145 ? ? OD2 A ASP 145 ? ? 123.75 118.30 5.45 0.90 N 2 1 CB A ASP 165 ? ? CG A ASP 165 ? ? OD2 A ASP 165 ? ? 124.08 118.30 5.78 0.90 N 3 1 CB B ASP 38 ? ? CG B ASP 38 ? ? OD2 B ASP 38 ? ? 124.04 118.30 5.74 0.90 N 4 1 CB B ASP 226 ? ? CG B ASP 226 ? ? OD2 B ASP 226 ? ? 124.07 118.30 5.77 0.90 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 75 ? ? -132.92 -69.09 2 1 ASN A 75 ? ? -136.27 -69.09 3 1 ASP A 219 ? ? -92.35 37.31 4 1 CYS A 221 ? ? -163.38 -165.46 5 1 ALA A 299 ? ? -80.87 32.95 6 1 MET B 16 ? ? 45.32 26.05 7 1 ASN B 75 ? ? -132.66 -72.76 8 1 ASP B 254 ? ? -170.75 -173.03 9 1 GLN B 287 ? ? -90.31 55.98 10 1 ALA B 299 ? ? -79.11 34.78 # 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 LEU 1 ? A LEU 1 2 1 Y 1 A THR 2 ? A THR 2 3 1 Y 1 A LEU 3 ? A LEU 3 4 1 Y 1 A GLU 167 ? A GLU 167 5 1 Y 1 A ASN 168 ? A ASN 168 6 1 Y 1 A SER 169 ? A SER 169 7 1 Y 1 A GLN 170 ? A GLN 170 8 1 Y 1 B GLU 167 ? B GLU 167 9 1 Y 1 B ASN 168 ? B ASN 168 10 1 Y 1 B SER 169 ? B SER 169 11 1 Y 1 B GLN 170 ? B GLN 170 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ;(1R,5S)-7-{4-[3-(2-chloro-3,6-difluorophenoxy)propyl]phenyl}-N-cyclopropyl-N-(2,3-dichlorobenzyl)-3,9-diazabicyclo[3.3.1]non-6-ene-6-carboxamide ; A5T 3 'DIMETHYL SULFOXIDE' DMS 4 N-ACETYL-D-GLUCOSAMINE NAG 5 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 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 A5T 1 342 342 A5T A5T A . D 3 DMS 1 343 343 DMS DMS A . E 4 NAG 1 344 344 NAG NAG A . F 2 A5T 1 342 342 A5T A5T B . G 3 DMS 1 343 343 DMS DMS B . H 5 NDG 1 344 344 NDG NDG B . I 6 HOH 1 345 345 HOH HOH A . I 6 HOH 2 346 346 HOH HOH A . I 6 HOH 3 347 347 HOH HOH A . I 6 HOH 4 348 348 HOH HOH A . I 6 HOH 5 349 349 HOH HOH A . I 6 HOH 6 350 350 HOH HOH A . I 6 HOH 7 351 351 HOH HOH A . I 6 HOH 8 352 352 HOH HOH A . I 6 HOH 9 353 353 HOH HOH A . I 6 HOH 10 354 354 HOH HOH A . I 6 HOH 11 355 355 HOH HOH A . I 6 HOH 12 356 356 HOH HOH A . I 6 HOH 13 357 357 HOH HOH A . I 6 HOH 14 358 358 HOH HOH A . I 6 HOH 15 359 359 HOH HOH A . I 6 HOH 16 360 360 HOH HOH A . I 6 HOH 17 361 361 HOH HOH A . I 6 HOH 18 362 362 HOH HOH A . I 6 HOH 19 363 363 HOH HOH A . I 6 HOH 20 364 364 HOH HOH A . I 6 HOH 21 365 365 HOH HOH A . I 6 HOH 22 366 366 HOH HOH A . I 6 HOH 23 367 367 HOH HOH A . I 6 HOH 24 368 368 HOH HOH A . I 6 HOH 25 369 369 HOH HOH A . I 6 HOH 26 370 370 HOH HOH A . I 6 HOH 27 371 371 HOH HOH A . I 6 HOH 28 372 372 HOH HOH A . I 6 HOH 29 373 373 HOH HOH A . I 6 HOH 30 374 374 HOH HOH A . I 6 HOH 31 375 375 HOH HOH A . I 6 HOH 32 376 376 HOH HOH A . I 6 HOH 33 377 377 HOH HOH A . I 6 HOH 34 378 378 HOH HOH A . I 6 HOH 35 379 379 HOH HOH A . I 6 HOH 36 380 380 HOH HOH A . I 6 HOH 37 381 381 HOH HOH A . I 6 HOH 38 382 382 HOH HOH A . I 6 HOH 39 383 383 HOH HOH A . I 6 HOH 40 384 384 HOH HOH A . I 6 HOH 41 385 385 HOH HOH A . I 6 HOH 42 386 386 HOH HOH A . I 6 HOH 43 387 387 HOH HOH A . I 6 HOH 44 388 388 HOH HOH A . I 6 HOH 45 389 389 HOH HOH A . I 6 HOH 46 390 390 HOH HOH A . I 6 HOH 47 391 391 HOH HOH A . I 6 HOH 48 392 392 HOH HOH A . I 6 HOH 49 393 393 HOH HOH A . I 6 HOH 50 394 394 HOH HOH A . I 6 HOH 51 395 395 HOH HOH A . I 6 HOH 52 396 396 HOH HOH A . I 6 HOH 53 397 397 HOH HOH A . I 6 HOH 54 398 398 HOH HOH A . I 6 HOH 55 399 399 HOH HOH A . I 6 HOH 56 400 400 HOH HOH A . I 6 HOH 57 401 401 HOH HOH A . I 6 HOH 58 402 402 HOH HOH A . I 6 HOH 59 403 403 HOH HOH A . I 6 HOH 60 404 404 HOH HOH A . I 6 HOH 61 405 405 HOH HOH A . I 6 HOH 62 406 406 HOH HOH A . I 6 HOH 63 407 407 HOH HOH A . I 6 HOH 64 408 408 HOH HOH A . I 6 HOH 65 409 409 HOH HOH A . I 6 HOH 66 410 410 HOH HOH A . I 6 HOH 67 411 411 HOH HOH A . I 6 HOH 68 412 412 HOH HOH A . I 6 HOH 69 413 413 HOH HOH A . I 6 HOH 70 414 414 HOH HOH A . I 6 HOH 71 415 415 HOH HOH A . I 6 HOH 72 416 416 HOH HOH A . I 6 HOH 73 417 417 HOH HOH A . I 6 HOH 74 418 418 HOH HOH A . I 6 HOH 75 419 419 HOH HOH A . I 6 HOH 76 420 420 HOH HOH A . I 6 HOH 77 421 421 HOH HOH A . I 6 HOH 78 422 422 HOH HOH A . I 6 HOH 79 423 423 HOH HOH A . I 6 HOH 80 424 424 HOH HOH A . I 6 HOH 81 425 425 HOH HOH A . I 6 HOH 82 426 426 HOH HOH A . I 6 HOH 83 427 427 HOH HOH A . I 6 HOH 84 428 428 HOH HOH A . I 6 HOH 85 429 429 HOH HOH A . I 6 HOH 86 430 430 HOH HOH A . I 6 HOH 87 431 431 HOH HOH A . I 6 HOH 88 432 432 HOH HOH A . I 6 HOH 89 433 433 HOH HOH A . I 6 HOH 90 434 434 HOH HOH A . I 6 HOH 91 435 435 HOH HOH A . I 6 HOH 92 436 436 HOH HOH A . I 6 HOH 93 437 437 HOH HOH A . I 6 HOH 94 438 438 HOH HOH A . I 6 HOH 95 439 439 HOH HOH A . I 6 HOH 96 440 440 HOH HOH A . I 6 HOH 97 441 441 HOH HOH A . I 6 HOH 98 442 442 HOH HOH A . I 6 HOH 99 443 443 HOH HOH A . I 6 HOH 100 444 444 HOH HOH A . I 6 HOH 101 445 445 HOH HOH A . I 6 HOH 102 446 446 HOH HOH A . I 6 HOH 103 447 447 HOH HOH A . I 6 HOH 104 448 448 HOH HOH A . I 6 HOH 105 449 449 HOH HOH A . I 6 HOH 106 450 450 HOH HOH A . I 6 HOH 107 451 451 HOH HOH A . I 6 HOH 108 452 452 HOH HOH A . I 6 HOH 109 453 453 HOH HOH A . I 6 HOH 110 454 454 HOH HOH A . I 6 HOH 111 455 455 HOH HOH A . I 6 HOH 112 456 456 HOH HOH A . I 6 HOH 113 457 457 HOH HOH A . I 6 HOH 114 458 458 HOH HOH A . I 6 HOH 115 459 459 HOH HOH A . I 6 HOH 116 460 460 HOH HOH A . I 6 HOH 117 461 461 HOH HOH A . I 6 HOH 118 462 462 HOH HOH A . I 6 HOH 119 463 463 HOH HOH A . I 6 HOH 120 464 464 HOH HOH A . I 6 HOH 121 465 465 HOH HOH A . I 6 HOH 122 466 466 HOH HOH A . I 6 HOH 123 467 467 HOH HOH A . I 6 HOH 124 468 468 HOH HOH A . I 6 HOH 125 469 469 HOH HOH A . I 6 HOH 126 470 470 HOH HOH A . I 6 HOH 127 471 471 HOH HOH A . I 6 HOH 128 472 472 HOH HOH A . I 6 HOH 129 473 473 HOH HOH A . I 6 HOH 130 474 474 HOH HOH A . I 6 HOH 131 475 475 HOH HOH A . I 6 HOH 132 476 476 HOH HOH A . I 6 HOH 133 477 477 HOH HOH A . I 6 HOH 134 478 478 HOH HOH A . I 6 HOH 135 479 479 HOH HOH A . I 6 HOH 136 480 480 HOH HOH A . I 6 HOH 137 481 481 HOH HOH A . I 6 HOH 138 482 482 HOH HOH A . I 6 HOH 139 483 483 HOH HOH A . I 6 HOH 140 484 484 HOH HOH A . I 6 HOH 141 485 485 HOH HOH A . I 6 HOH 142 486 486 HOH HOH A . I 6 HOH 143 487 487 HOH HOH A . I 6 HOH 144 488 488 HOH HOH A . I 6 HOH 145 489 489 HOH HOH A . I 6 HOH 146 490 490 HOH HOH A . I 6 HOH 147 491 491 HOH HOH A . I 6 HOH 148 492 492 HOH HOH A . I 6 HOH 149 493 493 HOH HOH A . I 6 HOH 150 494 494 HOH HOH A . I 6 HOH 151 495 495 HOH HOH A . I 6 HOH 152 496 496 HOH HOH A . I 6 HOH 153 497 497 HOH HOH A . I 6 HOH 154 498 498 HOH HOH A . I 6 HOH 155 499 499 HOH HOH A . I 6 HOH 156 500 500 HOH HOH A . I 6 HOH 157 501 501 HOH HOH A . I 6 HOH 158 502 502 HOH HOH A . I 6 HOH 159 503 503 HOH HOH A . I 6 HOH 160 504 504 HOH HOH A . I 6 HOH 161 506 506 HOH HOH A . I 6 HOH 162 508 508 HOH HOH A . I 6 HOH 163 509 509 HOH HOH A . I 6 HOH 164 510 510 HOH HOH A . I 6 HOH 165 511 511 HOH HOH A . I 6 HOH 166 512 512 HOH HOH A . I 6 HOH 167 513 513 HOH HOH A . I 6 HOH 168 514 514 HOH HOH A . I 6 HOH 169 515 515 HOH HOH A . I 6 HOH 170 516 516 HOH HOH A . I 6 HOH 171 517 517 HOH HOH A . I 6 HOH 172 518 518 HOH HOH A . I 6 HOH 173 519 519 HOH HOH A . I 6 HOH 174 520 520 HOH HOH A . I 6 HOH 175 521 521 HOH HOH A . J 6 HOH 1 345 345 HOH HOH B . J 6 HOH 2 346 346 HOH HOH B . J 6 HOH 3 347 347 HOH HOH B . J 6 HOH 4 348 348 HOH HOH B . J 6 HOH 5 349 349 HOH HOH B . J 6 HOH 6 350 350 HOH HOH B . J 6 HOH 7 351 351 HOH HOH B . J 6 HOH 8 352 352 HOH HOH B . J 6 HOH 9 353 353 HOH HOH B . J 6 HOH 10 354 354 HOH HOH B . J 6 HOH 11 355 355 HOH HOH B . J 6 HOH 12 356 356 HOH HOH B . J 6 HOH 13 357 357 HOH HOH B . J 6 HOH 14 358 358 HOH HOH B . J 6 HOH 15 359 359 HOH HOH B . J 6 HOH 16 360 360 HOH HOH B . J 6 HOH 17 361 361 HOH HOH B . J 6 HOH 18 362 362 HOH HOH B . J 6 HOH 19 363 363 HOH HOH B . J 6 HOH 20 364 364 HOH HOH B . J 6 HOH 21 365 365 HOH HOH B . J 6 HOH 22 366 366 HOH HOH B . J 6 HOH 23 367 367 HOH HOH B . J 6 HOH 24 368 368 HOH HOH B . J 6 HOH 25 369 369 HOH HOH B . J 6 HOH 26 370 370 HOH HOH B . J 6 HOH 27 371 371 HOH HOH B . J 6 HOH 28 372 372 HOH HOH B . J 6 HOH 29 373 373 HOH HOH B . J 6 HOH 30 374 374 HOH HOH B . J 6 HOH 31 375 375 HOH HOH B . J 6 HOH 32 376 376 HOH HOH B . J 6 HOH 33 377 377 HOH HOH B . J 6 HOH 34 378 378 HOH HOH B . J 6 HOH 35 379 379 HOH HOH B . J 6 HOH 36 380 380 HOH HOH B . J 6 HOH 37 381 381 HOH HOH B . J 6 HOH 38 382 382 HOH HOH B . J 6 HOH 39 383 383 HOH HOH B . J 6 HOH 40 384 384 HOH HOH B . J 6 HOH 41 385 385 HOH HOH B . J 6 HOH 42 386 386 HOH HOH B . J 6 HOH 43 387 387 HOH HOH B . J 6 HOH 44 388 388 HOH HOH B . J 6 HOH 45 389 389 HOH HOH B . J 6 HOH 46 390 390 HOH HOH B . J 6 HOH 47 391 391 HOH HOH B . J 6 HOH 48 392 392 HOH HOH B . J 6 HOH 49 393 393 HOH HOH B . J 6 HOH 50 394 394 HOH HOH B . J 6 HOH 51 395 395 HOH HOH B . J 6 HOH 52 396 396 HOH HOH B . J 6 HOH 53 397 397 HOH HOH B . J 6 HOH 54 398 398 HOH HOH B . J 6 HOH 55 399 399 HOH HOH B . J 6 HOH 56 400 400 HOH HOH B . J 6 HOH 57 401 401 HOH HOH B . J 6 HOH 58 402 402 HOH HOH B . J 6 HOH 59 403 403 HOH HOH B . J 6 HOH 60 404 404 HOH HOH B . J 6 HOH 61 405 405 HOH HOH B . J 6 HOH 62 406 406 HOH HOH B . J 6 HOH 63 407 407 HOH HOH B . J 6 HOH 64 408 408 HOH HOH B . J 6 HOH 65 409 409 HOH HOH B . J 6 HOH 66 410 410 HOH HOH B . J 6 HOH 67 411 411 HOH HOH B . J 6 HOH 68 412 412 HOH HOH B . J 6 HOH 69 413 413 HOH HOH B . J 6 HOH 70 414 414 HOH HOH B . J 6 HOH 71 415 415 HOH HOH B . J 6 HOH 72 416 416 HOH HOH B . J 6 HOH 73 417 417 HOH HOH B . J 6 HOH 74 418 418 HOH HOH B . J 6 HOH 75 419 419 HOH HOH B . J 6 HOH 76 420 420 HOH HOH B . J 6 HOH 77 421 421 HOH HOH B . J 6 HOH 78 422 422 HOH HOH B . J 6 HOH 79 423 423 HOH HOH B . J 6 HOH 80 424 424 HOH HOH B . J 6 HOH 81 425 425 HOH HOH B . J 6 HOH 82 426 426 HOH HOH B . J 6 HOH 83 427 427 HOH HOH B . J 6 HOH 84 428 428 HOH HOH B . J 6 HOH 85 429 429 HOH HOH B . J 6 HOH 86 430 430 HOH HOH B . J 6 HOH 87 431 431 HOH HOH B . J 6 HOH 88 432 432 HOH HOH B . J 6 HOH 89 433 433 HOH HOH B . J 6 HOH 90 434 434 HOH HOH B . J 6 HOH 91 435 435 HOH HOH B . J 6 HOH 92 436 436 HOH HOH B . J 6 HOH 93 437 437 HOH HOH B . J 6 HOH 94 438 438 HOH HOH B . J 6 HOH 95 439 439 HOH HOH B . J 6 HOH 96 440 440 HOH HOH B . J 6 HOH 97 441 441 HOH HOH B . J 6 HOH 98 442 442 HOH HOH B . J 6 HOH 99 443 443 HOH HOH B . J 6 HOH 100 444 444 HOH HOH B . J 6 HOH 101 445 445 HOH HOH B . J 6 HOH 102 446 446 HOH HOH B . J 6 HOH 103 447 447 HOH HOH B . J 6 HOH 104 448 448 HOH HOH B . J 6 HOH 105 449 449 HOH HOH B . J 6 HOH 106 450 450 HOH HOH B . J 6 HOH 107 451 451 HOH HOH B . J 6 HOH 108 452 452 HOH HOH B . J 6 HOH 109 453 453 HOH HOH B . J 6 HOH 110 454 454 HOH HOH B . J 6 HOH 111 455 455 HOH HOH B . J 6 HOH 112 456 456 HOH HOH B . J 6 HOH 113 457 457 HOH HOH B . J 6 HOH 114 458 458 HOH HOH B . J 6 HOH 115 459 459 HOH HOH B . J 6 HOH 116 460 460 HOH HOH B . J 6 HOH 117 461 461 HOH HOH B . J 6 HOH 118 462 462 HOH HOH B . J 6 HOH 119 463 463 HOH HOH B . J 6 HOH 120 464 464 HOH HOH B . J 6 HOH 121 465 465 HOH HOH B . J 6 HOH 122 466 466 HOH HOH B . J 6 HOH 123 467 467 HOH HOH B . J 6 HOH 124 468 468 HOH HOH B . J 6 HOH 125 469 469 HOH HOH B . J 6 HOH 126 470 470 HOH HOH B . J 6 HOH 127 471 471 HOH HOH B . J 6 HOH 128 472 472 HOH HOH B . J 6 HOH 129 473 473 HOH HOH B . J 6 HOH 130 474 474 HOH HOH B . J 6 HOH 131 475 475 HOH HOH B . J 6 HOH 132 476 476 HOH HOH B . J 6 HOH 133 477 477 HOH HOH B . J 6 HOH 134 478 478 HOH HOH B . J 6 HOH 135 479 479 HOH HOH B . J 6 HOH 136 480 480 HOH HOH B . J 6 HOH 137 481 481 HOH HOH B . J 6 HOH 138 482 482 HOH HOH B . J 6 HOH 139 483 483 HOH HOH B . J 6 HOH 140 484 484 HOH HOH B . J 6 HOH 141 485 485 HOH HOH B . J 6 HOH 142 486 486 HOH HOH B . J 6 HOH 143 487 487 HOH HOH B . J 6 HOH 144 488 488 HOH HOH B . J 6 HOH 145 489 489 HOH HOH B . J 6 HOH 146 490 490 HOH HOH B . J 6 HOH 147 491 491 HOH HOH B . J 6 HOH 148 492 492 HOH HOH B . J 6 HOH 149 493 493 HOH HOH B . J 6 HOH 150 494 494 HOH HOH B . J 6 HOH 151 495 495 HOH HOH B . J 6 HOH 152 496 496 HOH HOH B . J 6 HOH 153 497 497 HOH HOH B . J 6 HOH 154 498 498 HOH HOH B . J 6 HOH 155 499 499 HOH HOH B . J 6 HOH 156 500 500 HOH HOH B . J 6 HOH 157 501 501 HOH HOH B . J 6 HOH 158 502 502 HOH HOH B . J 6 HOH 159 503 503 HOH HOH B . J 6 HOH 160 504 504 HOH HOH B . J 6 HOH 161 505 505 HOH HOH B . J 6 HOH 162 506 506 HOH HOH B . J 6 HOH 163 507 507 HOH HOH B . J 6 HOH 164 508 508 HOH HOH B . J 6 HOH 165 509 509 HOH HOH B . J 6 HOH 166 510 510 HOH HOH B . J 6 HOH 167 511 511 HOH HOH B . J 6 HOH 168 512 512 HOH HOH B . J 6 HOH 169 513 513 HOH HOH B . J 6 HOH 170 514 514 HOH HOH B . J 6 HOH 171 515 515 HOH HOH B . J 6 HOH 172 516 516 HOH HOH B . J 6 HOH 173 517 517 HOH HOH B . J 6 HOH 174 518 518 HOH HOH B . J 6 HOH 175 519 519 HOH HOH B . J 6 HOH 176 520 520 HOH HOH B . J 6 HOH 177 521 521 HOH HOH B . J 6 HOH 178 522 522 HOH HOH B . J 6 HOH 179 523 523 HOH HOH B . J 6 HOH 180 524 524 HOH HOH B . J 6 HOH 181 525 525 HOH HOH B . J 6 HOH 182 526 526 HOH HOH B . J 6 HOH 183 527 527 HOH HOH B . J 6 HOH 184 528 528 HOH HOH B . J 6 HOH 185 529 529 HOH HOH B . J 6 HOH 186 530 530 HOH HOH B . J 6 HOH 187 531 531 HOH HOH B . J 6 HOH 188 532 532 HOH HOH B . J 6 HOH 189 533 533 HOH HOH B . J 6 HOH 190 534 534 HOH HOH B . J 6 HOH 191 535 535 HOH HOH B . J 6 HOH 192 536 536 HOH HOH B . J 6 HOH 193 537 537 HOH HOH B . J 6 HOH 194 538 538 HOH HOH B . J 6 HOH 195 539 539 HOH HOH B . J 6 HOH 196 540 540 HOH HOH B . J 6 HOH 197 541 541 HOH HOH B . J 6 HOH 198 542 542 HOH HOH B . J 6 HOH 199 543 543 HOH HOH B . #