data_3RTJ # _entry.id 3RTJ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3RTJ NDB NA1103 RCSB RCSB065358 WWPDB D_1000065358 # _pdbx_database_PDB_obs_spr.id SPRSDE _pdbx_database_PDB_obs_spr.date 2011-08-31 _pdbx_database_PDB_obs_spr.pdb_id 3RTJ _pdbx_database_PDB_obs_spr.replace_pdb_id 1APG _pdbx_database_PDB_obs_spr.details ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 2AAI 'native structure of ricin' unspecified PDB 3RTI 'ricin bound with formycin monophosphate' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3RTJ _pdbx_database_status.recvd_initial_deposition_date 2011-05-03 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Monzingo, A.F.' 1 'Robertus, J.D.' 2 # _citation.id primary _citation.title 'X-ray analysis of substrate analogs in the ricin A-chain active site.' _citation.journal_abbrev J.Mol.Biol. _citation.journal_volume 227 _citation.page_first 1136 _citation.page_last 1145 _citation.year 1992 _citation.journal_id_ASTM JMOBAK _citation.country UK _citation.journal_id_ISSN 0022-2836 _citation.journal_id_CSD 0070 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 1433290 _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Monzingo, A.F.' 1 primary 'Robertus, J.D.' 2 # _cell.entry_id 3RTJ _cell.length_a 72.740 _cell.length_b 78.490 _cell.length_c 114.340 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _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 3RTJ _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 syn ;RNA (5'-R(*AP*G)-3') ; 629.454 1 ? ? ? ? 2 polymer nat 'Ricin A chain' 29936.758 1 3.2.2.22 ? ? ? 3 polymer nat 'Ricin B chain' 28989.580 1 3.2.2.22 ? ? ? 4 non-polymer man BETA-D-GALACTOSE 180.156 2 ? ? ? ? 5 non-polymer man BETA-D-GLUCOSE 180.156 2 ? ? ? ? 6 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 2 'Ricin A chain, rRNA N-glycosidase, Linker peptide, Ricin B chain' 3 'Ricin A chain, rRNA N-glycosidase, Linker peptide, Ricin B chain' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 polyribonucleotide no no AG AG D ? 2 'polypeptide(L)' no no ;IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAY VVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQ LPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKF SVYDVSILIPIIALMVYRCAPPPSSQF ; ;IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAY VVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQ LPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKF SVYDVSILIPIIALMVYRCAPPPSSQF ; A ? 3 'polypeptide(L)' no no ;ADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDC NTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVW IEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDP SLKQIILYPLHGDPNQIWLPLF ; ;ADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDC NTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVW IEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDP SLKQIILYPLHGDPNQIWLPLF ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 A n 1 2 G n 2 1 ILE n 2 2 PHE n 2 3 PRO n 2 4 LYS n 2 5 GLN n 2 6 TYR n 2 7 PRO n 2 8 ILE n 2 9 ILE n 2 10 ASN n 2 11 PHE n 2 12 THR n 2 13 THR n 2 14 ALA n 2 15 GLY n 2 16 ALA n 2 17 THR n 2 18 VAL n 2 19 GLN n 2 20 SER n 2 21 TYR n 2 22 THR n 2 23 ASN n 2 24 PHE n 2 25 ILE n 2 26 ARG n 2 27 ALA n 2 28 VAL n 2 29 ARG n 2 30 GLY n 2 31 ARG n 2 32 LEU n 2 33 THR n 2 34 THR n 2 35 GLY n 2 36 ALA n 2 37 ASP n 2 38 VAL n 2 39 ARG n 2 40 HIS n 2 41 GLU n 2 42 ILE n 2 43 PRO n 2 44 VAL n 2 45 LEU n 2 46 PRO n 2 47 ASN n 2 48 ARG n 2 49 VAL n 2 50 GLY n 2 51 LEU n 2 52 PRO n 2 53 ILE n 2 54 ASN n 2 55 GLN n 2 56 ARG n 2 57 PHE n 2 58 ILE n 2 59 LEU n 2 60 VAL n 2 61 GLU n 2 62 LEU n 2 63 SER n 2 64 ASN n 2 65 HIS n 2 66 ALA n 2 67 GLU n 2 68 LEU n 2 69 SER n 2 70 VAL n 2 71 THR n 2 72 LEU n 2 73 ALA n 2 74 LEU n 2 75 ASP n 2 76 VAL n 2 77 THR n 2 78 ASN n 2 79 ALA n 2 80 TYR n 2 81 VAL n 2 82 VAL n 2 83 GLY n 2 84 TYR n 2 85 ARG n 2 86 ALA n 2 87 GLY n 2 88 ASN n 2 89 SER n 2 90 ALA n 2 91 TYR n 2 92 PHE n 2 93 PHE n 2 94 HIS n 2 95 PRO n 2 96 ASP n 2 97 ASN n 2 98 GLN n 2 99 GLU n 2 100 ASP n 2 101 ALA n 2 102 GLU n 2 103 ALA n 2 104 ILE n 2 105 THR n 2 106 HIS n 2 107 LEU n 2 108 PHE n 2 109 THR n 2 110 ASP n 2 111 VAL n 2 112 GLN n 2 113 ASN n 2 114 ARG n 2 115 TYR n 2 116 THR n 2 117 PHE n 2 118 ALA n 2 119 PHE n 2 120 GLY n 2 121 GLY n 2 122 ASN n 2 123 TYR n 2 124 ASP n 2 125 ARG n 2 126 LEU n 2 127 GLU n 2 128 GLN n 2 129 LEU n 2 130 ALA n 2 131 GLY n 2 132 ASN n 2 133 LEU n 2 134 ARG n 2 135 GLU n 2 136 ASN n 2 137 ILE n 2 138 GLU n 2 139 LEU n 2 140 GLY n 2 141 ASN n 2 142 GLY n 2 143 PRO n 2 144 LEU n 2 145 GLU n 2 146 GLU n 2 147 ALA n 2 148 ILE n 2 149 SER n 2 150 ALA n 2 151 LEU n 2 152 TYR n 2 153 TYR n 2 154 TYR n 2 155 SER n 2 156 THR n 2 157 GLY n 2 158 GLY n 2 159 THR n 2 160 GLN n 2 161 LEU n 2 162 PRO n 2 163 THR n 2 164 LEU n 2 165 ALA n 2 166 ARG n 2 167 SER n 2 168 PHE n 2 169 ILE n 2 170 ILE n 2 171 CYS n 2 172 ILE n 2 173 GLN n 2 174 MET n 2 175 ILE n 2 176 SER n 2 177 GLU n 2 178 ALA n 2 179 ALA n 2 180 ARG n 2 181 PHE n 2 182 GLN n 2 183 TYR n 2 184 ILE n 2 185 GLU n 2 186 GLY n 2 187 GLU n 2 188 MET n 2 189 ARG n 2 190 THR n 2 191 ARG n 2 192 ILE n 2 193 ARG n 2 194 TYR n 2 195 ASN n 2 196 ARG n 2 197 ARG n 2 198 SER n 2 199 ALA n 2 200 PRO n 2 201 ASP n 2 202 PRO n 2 203 SER n 2 204 VAL n 2 205 ILE n 2 206 THR n 2 207 LEU n 2 208 GLU n 2 209 ASN n 2 210 SER n 2 211 TRP n 2 212 GLY n 2 213 ARG n 2 214 LEU n 2 215 SER n 2 216 THR n 2 217 ALA n 2 218 ILE n 2 219 GLN n 2 220 GLU n 2 221 SER n 2 222 ASN n 2 223 GLN n 2 224 GLY n 2 225 ALA n 2 226 PHE n 2 227 ALA n 2 228 SER n 2 229 PRO n 2 230 ILE n 2 231 GLN n 2 232 LEU n 2 233 GLN n 2 234 ARG n 2 235 ARG n 2 236 ASN n 2 237 GLY n 2 238 SER n 2 239 LYS n 2 240 PHE n 2 241 SER n 2 242 VAL n 2 243 TYR n 2 244 ASP n 2 245 VAL n 2 246 SER n 2 247 ILE n 2 248 LEU n 2 249 ILE n 2 250 PRO n 2 251 ILE n 2 252 ILE n 2 253 ALA n 2 254 LEU n 2 255 MET n 2 256 VAL n 2 257 TYR n 2 258 ARG n 2 259 CYS n 2 260 ALA n 2 261 PRO n 2 262 PRO n 2 263 PRO n 2 264 SER n 2 265 SER n 2 266 GLN n 2 267 PHE n 3 1 ALA n 3 2 ASP n 3 3 VAL n 3 4 CYS n 3 5 MET n 3 6 ASP n 3 7 PRO n 3 8 GLU n 3 9 PRO n 3 10 ILE n 3 11 VAL n 3 12 ARG n 3 13 ILE n 3 14 VAL n 3 15 GLY n 3 16 ARG n 3 17 ASN n 3 18 GLY n 3 19 LEU n 3 20 CYS n 3 21 VAL n 3 22 ASP n 3 23 VAL n 3 24 ARG n 3 25 ASP n 3 26 GLY n 3 27 ARG n 3 28 PHE n 3 29 HIS n 3 30 ASN n 3 31 GLY n 3 32 ASN n 3 33 ALA n 3 34 ILE n 3 35 GLN n 3 36 LEU n 3 37 TRP n 3 38 PRO n 3 39 CYS n 3 40 LYS n 3 41 SER n 3 42 ASN n 3 43 THR n 3 44 ASP n 3 45 ALA n 3 46 ASN n 3 47 GLN n 3 48 LEU n 3 49 TRP n 3 50 THR n 3 51 LEU n 3 52 LYS n 3 53 ARG n 3 54 ASP n 3 55 ASN n 3 56 THR n 3 57 ILE n 3 58 ARG n 3 59 SER n 3 60 ASN n 3 61 GLY n 3 62 LYS n 3 63 CYS n 3 64 LEU n 3 65 THR n 3 66 THR n 3 67 TYR n 3 68 GLY n 3 69 TYR n 3 70 SER n 3 71 PRO n 3 72 GLY n 3 73 VAL n 3 74 TYR n 3 75 VAL n 3 76 MET n 3 77 ILE n 3 78 TYR n 3 79 ASP n 3 80 CYS n 3 81 ASN n 3 82 THR n 3 83 ALA n 3 84 ALA n 3 85 THR n 3 86 ASP n 3 87 ALA n 3 88 THR n 3 89 ARG n 3 90 TRP n 3 91 GLN n 3 92 ILE n 3 93 TRP n 3 94 ASP n 3 95 ASN n 3 96 GLY n 3 97 THR n 3 98 ILE n 3 99 ILE n 3 100 ASN n 3 101 PRO n 3 102 ARG n 3 103 SER n 3 104 SER n 3 105 LEU n 3 106 VAL n 3 107 LEU n 3 108 ALA n 3 109 ALA n 3 110 THR n 3 111 SER n 3 112 GLY n 3 113 ASN n 3 114 SER n 3 115 GLY n 3 116 THR n 3 117 THR n 3 118 LEU n 3 119 THR n 3 120 VAL n 3 121 GLN n 3 122 THR n 3 123 ASN n 3 124 ILE n 3 125 TYR n 3 126 ALA n 3 127 VAL n 3 128 SER n 3 129 GLN n 3 130 GLY n 3 131 TRP n 3 132 LEU n 3 133 PRO n 3 134 THR n 3 135 ASN n 3 136 ASN n 3 137 THR n 3 138 GLN n 3 139 PRO n 3 140 PHE n 3 141 VAL n 3 142 THR n 3 143 THR n 3 144 ILE n 3 145 VAL n 3 146 GLY n 3 147 LEU n 3 148 TYR n 3 149 GLY n 3 150 LEU n 3 151 CYS n 3 152 LEU n 3 153 GLN n 3 154 ALA n 3 155 ASN n 3 156 SER n 3 157 GLY n 3 158 GLN n 3 159 VAL n 3 160 TRP n 3 161 ILE n 3 162 GLU n 3 163 ASP n 3 164 CYS n 3 165 SER n 3 166 SER n 3 167 GLU n 3 168 LYS n 3 169 ALA n 3 170 GLU n 3 171 GLN n 3 172 GLN n 3 173 TRP n 3 174 ALA n 3 175 LEU n 3 176 TYR n 3 177 ALA n 3 178 ASP n 3 179 GLY n 3 180 SER n 3 181 ILE n 3 182 ARG n 3 183 PRO n 3 184 GLN n 3 185 GLN n 3 186 ASN n 3 187 ARG n 3 188 ASP n 3 189 ASN n 3 190 CYS n 3 191 LEU n 3 192 THR n 3 193 SER n 3 194 ASP n 3 195 SER n 3 196 ASN n 3 197 ILE n 3 198 ARG n 3 199 GLU n 3 200 THR n 3 201 VAL n 3 202 VAL n 3 203 LYS n 3 204 ILE n 3 205 LEU n 3 206 SER n 3 207 CYS n 3 208 GLY n 3 209 PRO n 3 210 ALA n 3 211 SER n 3 212 SER n 3 213 GLY n 3 214 GLN n 3 215 ARG n 3 216 TRP n 3 217 MET n 3 218 PHE n 3 219 LYS n 3 220 ASN n 3 221 ASP n 3 222 GLY n 3 223 THR n 3 224 ILE n 3 225 LEU n 3 226 ASN n 3 227 LEU n 3 228 TYR n 3 229 SER n 3 230 GLY n 3 231 LEU n 3 232 VAL n 3 233 LEU n 3 234 ASP n 3 235 VAL n 3 236 ARG n 3 237 ALA n 3 238 SER n 3 239 ASP n 3 240 PRO n 3 241 SER n 3 242 LEU n 3 243 LYS n 3 244 GLN n 3 245 ILE n 3 246 ILE n 3 247 LEU n 3 248 TYR n 3 249 PRO n 3 250 LEU n 3 251 HIS n 3 252 GLY n 3 253 ASP n 3 254 PRO n 3 255 ASN n 3 256 GLN n 3 257 ILE n 3 258 TRP n 3 259 LEU n 3 260 PRO n 3 261 LEU n 3 262 PHE n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 2 1 sample ? ? 'Castor bean' 'Ricinus communis' 3988 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? seed 3 1 sample ? ? 'Castor bean' 'Ricinus communis' 3988 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? seed # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP RICI_RICCO P02879 2 ;IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAY VVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQ LPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKF SVYDVSILIPIIALMVYRCAPPPSSQF ; 36 ? 2 UNP RICI_RICCO P02879 3 ;ADVCMDPEPIVRIVGRNGLCVDVRDGRFHNGNAIQLWPCKSNTDANQLWTLKRDNTIRSNGKCLTTYGYSPGVYVMIYDC NTAATDATRWQIWDNGTIINPRSSLVLAATSGNSGTTLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGLCLQANSGQVW IEDCSSEKAEQQWALYADGSIRPQQNRDNCLTSDSNIRETVVKILSCGPASSGQRWMFKNDGTILNLYSGLVLDVRASDP SLKQIILYPLHGDPNQIWLPLF ; 315 ? 3 PDB 3RTJ 3RTJ 1 AG ? ? # 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 3RTJ A 1 ? 267 ? P02879 36 ? 302 ? 1 267 2 2 3RTJ B 1 ? 262 ? P02879 315 ? 576 ? 1 262 3 3 3RTJ D 1 ? 2 ? 3RTJ 701 ? 702 ? 701 702 # 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 A 'RNA linking' y "ADENOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O7 P' 347.221 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 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 G 'RNA linking' y "GUANOSINE-5'-MONOPHOSPHATE" ? 'C10 H14 N5 O8 P' 363.221 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 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 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 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 3RTJ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.74 _exptl_crystal.density_percent_sol 55.11 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method batch _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.75 _exptl_crystal_grow.pdbx_details '11.5% PEG 8000, 0.05 M sodium acetate, 2 mM lactose, pH 4.75, batch, temperature 298K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 298 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'AREA DETECTOR' _diffrn_detector.type 'San Diego Multiwire Systems' _diffrn_detector.pdbx_collection_date 1991-06-11 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator graphite _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'ELLIOTT GX-20' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 3RTJ _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low ? _reflns.d_resolution_high 3.0 _reflns.number_obs 8250 _reflns.number_all 8250 _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _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 3RTJ _refine.ls_number_reflns_obs 8250 _refine.ls_number_reflns_all 8250 _refine.pdbx_ls_sigma_I ? _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 19.91 _refine.ls_d_res_high 3.0 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.198 _refine.ls_R_factor_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _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 4045 _refine_hist.pdbx_number_atoms_nucleic_acid 42 _refine_hist.pdbx_number_atoms_ligand 102 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 4189 _refine_hist.d_res_high 3.0 _refine_hist.d_res_low 19.91 # 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_restraint_function _refine_ls_restr.pdbx_refine_id x_bond_d 0.014 ? ? ? ? 'X-RAY DIFFRACTION' x_angle_deg 4.0 ? ? ? ? 'X-RAY DIFFRACTION' # _struct.entry_id 3RTJ _struct.title 'Crystal structure of ricin bound with dinucleotide ApG' _struct.pdbx_descriptor 'Ricin/RNA Complex' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3RTJ _struct_keywords.pdbx_keywords HYDROLASE/RNA _struct_keywords.text ;enzyme-substrate complex, glycosidase ribosome-inactivating protein lectin glycoprotein, lactose binding, glycosylation, HYDROLASE, HYDROLASE-RNA complex ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 4 ? G N N 5 ? H N N 6 ? I N N 6 ? J N N 6 ? K 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 THR B 17 ? THR B 33 ? THR A 17 THR A 33 1 ? 17 HELX_P HELX_P2 2 ASN B 97 ? ILE B 104 ? ASN A 97 ILE A 104 1 ? 8 HELX_P HELX_P3 3 THR B 105 ? LEU B 107 ? THR A 105 LEU A 107 5 ? 3 HELX_P HELX_P4 4 ASN B 122 ? GLY B 131 ? ASN A 122 GLY A 131 1 ? 10 HELX_P HELX_P5 5 GLY B 140 ? TYR B 154 ? GLY A 140 TYR A 154 1 ? 15 HELX_P HELX_P6 6 GLN B 160 ? PHE B 181 ? GLN A 160 PHE A 181 1 ? 22 HELX_P HELX_P7 7 PHE B 181 ? TYR B 194 ? PHE A 181 TYR A 194 1 ? 14 HELX_P HELX_P8 8 ASP B 201 ? SER B 210 ? ASP A 201 SER A 210 1 ? 10 HELX_P HELX_P9 9 SER B 210 ? GLU B 220 ? SER A 210 GLU A 220 1 ? 11 HELX_P HELX_P10 10 GLY C 15 ? LEU C 19 ? GLY B 15 LEU B 19 5 ? 5 HELX_P HELX_P11 11 ASP C 25 ? ARG C 27 ? ASP B 25 ARG B 27 5 ? 3 HELX_P HELX_P12 12 ALA C 84 ? THR C 88 ? ALA B 84 THR B 88 5 ? 5 HELX_P HELX_P13 13 ALA C 126 ? GLY C 130 ? ALA B 126 GLY B 130 5 ? 5 HELX_P HELX_P14 14 GLY C 146 ? LEU C 150 ? GLY B 146 LEU B 150 5 ? 5 HELX_P HELX_P15 15 ALA C 237 ? LYS C 243 ? ALA B 237 LYS B 243 5 ? 7 HELX_P HELX_P16 16 ASP C 253 ? ILE C 257 ? ASP B 253 ILE B 257 5 ? 5 # _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 ? ? B CYS 259 SG ? ? ? 1_555 C CYS 4 SG ? ? A CYS 259 B CYS 4 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? C CYS 20 SG ? ? ? 1_555 C CYS 39 SG ? ? B CYS 20 B CYS 39 1_555 ? ? ? ? ? ? ? 2.032 ? disulf3 disulf ? ? C CYS 63 SG ? ? ? 1_555 C CYS 80 SG ? ? B CYS 63 B CYS 80 1_555 ? ? ? ? ? ? ? 2.029 ? disulf4 disulf ? ? C CYS 151 SG ? ? ? 1_555 C CYS 164 SG ? ? B CYS 151 B CYS 164 1_555 ? ? ? ? ? ? ? 2.024 ? disulf5 disulf ? ? C CYS 190 SG ? ? ? 1_555 C CYS 207 SG ? ? B CYS 190 B CYS 207 1_555 ? ? ? ? ? ? ? 2.027 ? covale1 covale ? ? F GAL . C1 ? ? ? 1_555 G BGC . O4 ? ? B GAL 267 B BGC 268 1_555 ? ? ? ? ? ? ? 1.387 ? covale2 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? B NAG 280 B NAG 281 1_555 ? ? ? ? ? ? ? 1.388 ? covale3 covale ? ? D GAL . C1 ? ? ? 1_555 E BGC . O4 ? ? B GAL 264 B BGC 265 1_555 ? ? ? ? ? ? ? 1.388 ? covale4 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? B NAG 270 B NAG 271 1_555 ? ? ? ? ? ? ? 1.397 ? covale5 covale ? ? C ASN 95 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 95 B NAG 270 1_555 ? ? ? ? ? ? ? 1.447 ? covale6 covale ? ? C ASN 135 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 135 B NAG 280 1_555 ? ? ? ? ? ? ? 1.449 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 6 ? B ? 2 ? C ? 2 ? D ? 5 ? E ? 2 ? F ? 2 ? G ? 2 ? H ? 2 ? I ? 4 ? J ? 2 ? K ? 2 ? L ? 2 ? M ? 2 ? # 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 ? parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel E 1 2 ? anti-parallel F 1 2 ? anti-parallel G 1 2 ? anti-parallel H 1 2 ? anti-parallel I 1 2 ? anti-parallel I 2 3 ? anti-parallel I 3 4 ? anti-parallel J 1 2 ? anti-parallel K 1 2 ? anti-parallel L 1 2 ? anti-parallel M 1 2 ? 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 ILE B 8 ? THR B 12 ? ILE A 8 THR A 12 A 2 PHE B 57 ? SER B 63 ? PHE A 57 SER A 63 A 3 SER B 69 ? ASP B 75 ? SER A 69 ASP A 75 A 4 VAL B 81 ? ALA B 86 ? VAL A 81 ALA A 86 A 5 SER B 89 ? PHE B 92 ? SER A 89 PHE A 92 A 6 ASN B 113 ? THR B 116 ? ASN A 113 THR A 116 B 1 VAL B 38 ? ARG B 39 ? VAL A 38 ARG A 39 B 2 ILE B 42 ? PRO B 43 ? ILE A 42 PRO A 43 C 1 ALA B 225 ? GLN B 233 ? ALA A 225 GLN A 233 C 2 LYS B 239 ? ASP B 244 ? LYS A 239 ASP A 244 D 1 ILE C 10 ? VAL C 11 ? ILE B 10 VAL B 11 D 2 TRP C 49 ? LEU C 51 ? TRP B 49 LEU B 51 D 3 ILE C 57 ? SER C 59 ? ILE B 57 SER B 59 D 4 LYS C 62 ? THR C 66 ? LYS B 62 THR B 66 D 5 VAL C 75 ? TYR C 78 ? VAL B 75 TYR B 78 E 1 ILE C 13 ? VAL C 14 ? ILE B 13 VAL B 14 E 2 LEU C 132 ? PRO C 133 ? LEU B 132 PRO B 133 F 1 CYS C 20 ? VAL C 23 ? CYS B 20 VAL B 23 F 2 ILE C 34 ? TRP C 37 ? ILE B 34 TRP B 37 G 1 GLN C 91 ? ILE C 92 ? GLN B 91 ILE B 92 G 2 ILE C 98 ? ILE C 99 ? ILE B 98 ILE B 99 H 1 LEU C 105 ? ALA C 108 ? LEU B 105 ALA B 108 H 2 THR C 119 ? THR C 122 ? THR B 119 THR B 122 I 1 ILE C 181 ? PRO C 183 ? ILE B 181 PRO B 183 I 2 GLN C 172 ? LEU C 175 ? GLN B 172 LEU B 175 I 3 PHE C 140 ? VAL C 145 ? PHE B 140 VAL B 145 I 4 LEU C 259 ? LEU C 261 ? LEU B 259 LEU B 261 J 1 CYS C 151 ? ASN C 155 ? CYS B 151 ASN B 155 J 2 GLN C 158 ? GLU C 162 ? GLN B 158 GLU B 162 K 1 ASN C 189 ? THR C 192 ? ASN B 189 THR B 192 K 2 LYS C 203 ? SER C 206 ? LYS B 203 SER B 206 L 1 MET C 217 ? PHE C 218 ? MET B 217 PHE B 218 L 2 ILE C 224 ? LEU C 225 ? ILE B 224 LEU B 225 M 1 VAL C 232 ? VAL C 235 ? VAL B 232 VAL B 235 M 2 ILE C 245 ? TYR C 248 ? ILE B 245 TYR B 248 # 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 ILE B 9 ? N ILE A 9 O GLU B 61 ? O GLU A 61 A 2 3 N VAL B 60 ? N VAL A 60 O LEU B 72 ? O LEU A 72 A 3 4 N THR B 71 ? N THR A 71 O ARG B 85 ? O ARG A 85 A 4 5 N TYR B 84 ? N TYR A 84 O TYR B 91 ? O TYR A 91 A 5 6 N ALA B 90 ? N ALA A 90 O TYR B 115 ? O TYR A 115 B 1 2 N ARG B 39 ? N ARG A 39 O ILE B 42 ? O ILE A 42 C 1 2 N PHE B 226 ? N PHE A 226 O TYR B 243 ? O TYR A 243 D 1 2 N VAL C 11 ? N VAL B 11 O TRP C 49 ? O TRP B 49 D 2 3 N THR C 50 ? N THR B 50 O ARG C 58 ? O ARG B 58 D 3 4 N ILE C 57 ? N ILE B 57 O LEU C 64 ? O LEU B 64 D 4 5 N THR C 65 ? N THR B 65 O MET C 76 ? O MET B 76 E 1 2 N VAL C 14 ? N VAL B 14 O LEU C 132 ? O LEU B 132 F 1 2 N ASP C 22 ? N ASP B 22 O GLN C 35 ? O GLN B 35 G 1 2 N GLN C 91 ? N GLN B 91 O ILE C 99 ? O ILE B 99 H 1 2 N ALA C 108 ? N ALA B 108 O THR C 119 ? O THR B 119 I 1 2 O ARG C 182 ? O ARG B 182 N ALA C 174 ? N ALA B 174 I 2 3 O TRP C 173 ? O TRP B 173 N THR C 142 ? N THR B 142 I 3 4 N THR C 143 ? N THR B 143 O LEU C 261 ? O LEU B 261 J 1 2 N GLN C 153 ? N GLN B 153 O TRP C 160 ? O TRP B 160 K 1 2 N THR C 192 ? N THR B 192 O LYS C 203 ? O LYS B 203 L 1 2 N MET C 217 ? N MET B 217 O LEU C 225 ? O LEU B 225 M 1 2 N ASP C 234 ? N ASP B 234 O ILE C 246 ? O ILE B 246 # 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 ? ? ? ? 7 'BINDING SITE FOR RESIDUE GAL B 264' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BGC B 265' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GAL B 267' AC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BGC B 268' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 270' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 271' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 280' AC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 281' # 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 7 ASP C 22 ? ASP B 22 . ? 1_555 ? 2 AC1 7 ASP C 25 ? ASP B 25 . ? 1_555 ? 3 AC1 7 GLN C 35 ? GLN B 35 . ? 1_555 ? 4 AC1 7 TRP C 37 ? TRP B 37 . ? 1_555 ? 5 AC1 7 LYS C 40 ? LYS B 40 . ? 1_555 ? 6 AC1 7 ASN C 46 ? ASN B 46 . ? 1_555 ? 7 AC1 7 BGC E . ? BGC B 265 . ? 1_555 ? 8 AC2 2 ASP C 25 ? ASP B 25 . ? 1_555 ? 9 AC2 2 GAL D . ? GAL B 264 . ? 1_555 ? 10 AC3 8 GLU C 199 ? GLU B 199 . ? 1_555 ? 11 AC3 8 ASP C 234 ? ASP B 234 . ? 1_555 ? 12 AC3 8 ARG C 236 ? ARG B 236 . ? 1_555 ? 13 AC3 8 ALA C 237 ? ALA B 237 . ? 1_555 ? 14 AC3 8 TYR C 248 ? TYR B 248 . ? 1_555 ? 15 AC3 8 HIS C 251 ? HIS B 251 . ? 1_555 ? 16 AC3 8 ASN C 255 ? ASN B 255 . ? 1_555 ? 17 AC3 8 BGC G . ? BGC B 268 . ? 1_555 ? 18 AC4 2 ALA C 237 ? ALA B 237 . ? 1_555 ? 19 AC4 2 GAL F . ? GAL B 267 . ? 1_555 ? 20 AC5 4 ASN C 95 ? ASN B 95 . ? 1_555 ? 21 AC5 4 TYR C 125 ? TYR B 125 . ? 1_555 ? 22 AC5 4 LEU C 227 ? LEU B 227 . ? 1_555 ? 23 AC5 4 NAG I . ? NAG B 271 . ? 1_555 ? 24 AC6 3 GLN C 91 ? GLN B 91 . ? 1_555 ? 25 AC6 3 TRP C 93 ? TRP B 93 . ? 1_555 ? 26 AC6 3 NAG H . ? NAG B 270 . ? 1_555 ? 27 AC7 6 ALA B 227 ? ALA A 227 . ? 1_555 ? 28 AC7 6 PRO B 229 ? PRO A 229 . ? 1_555 ? 29 AC7 6 TYR B 243 ? TYR A 243 . ? 1_555 ? 30 AC7 6 ILE C 10 ? ILE B 10 . ? 1_555 ? 31 AC7 6 ASN C 135 ? ASN B 135 . ? 1_555 ? 32 AC7 6 NAG K . ? NAG B 281 . ? 1_555 ? 33 AC8 3 THR C 43 ? THR B 43 . ? 1_555 ? 34 AC8 3 LEU C 48 ? LEU B 48 . ? 1_555 ? 35 AC8 3 NAG J . ? NAG B 280 . ? 1_555 ? # _database_PDB_matrix.entry_id 3RTJ _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 3RTJ _atom_sites.fract_transf_matrix[1][1] 0.013748 _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] 0.012740 _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] 0.008746 _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 N O P S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 O "O5'" . A A 1 1 ? 23.773 67.116 51.806 1.00 75.12 ? 701 A D "O5'" 1 ATOM 2 C "C5'" . A A 1 1 ? 23.980 65.743 51.432 1.00 77.48 ? 701 A D "C5'" 1 ATOM 3 C "C4'" . A A 1 1 ? 25.016 65.059 52.305 1.00 79.60 ? 701 A D "C4'" 1 ATOM 4 O "O4'" . A A 1 1 ? 24.997 65.565 53.655 1.00 77.88 ? 701 A D "O4'" 1 ATOM 5 C "C3'" . A A 1 1 ? 24.949 63.534 52.409 1.00 81.33 ? 701 A D "C3'" 1 ATOM 6 O "O3'" . A A 1 1 ? 25.874 62.987 51.446 1.00 88.03 ? 701 A D "O3'" 1 ATOM 7 C "C2'" . A A 1 1 ? 25.312 63.187 53.869 1.00 78.87 ? 701 A D "C2'" 1 ATOM 8 O "O2'" . A A 1 1 ? 26.465 62.388 54.027 1.00 79.19 ? 701 A D "O2'" 1 ATOM 9 C "C1'" . A A 1 1 ? 25.520 64.569 54.506 1.00 74.49 ? 701 A D "C1'" 1 ATOM 10 N N9 . A A 1 1 ? 25.167 64.881 55.891 1.00 67.57 ? 701 A D N9 1 ATOM 11 C C8 . A A 1 1 ? 26.065 65.344 56.819 1.00 64.72 ? 701 A D C8 1 ATOM 12 N N7 . A A 1 1 ? 25.520 65.707 57.945 1.00 62.69 ? 701 A D N7 1 ATOM 13 C C5 . A A 1 1 ? 24.175 65.434 57.763 1.00 62.68 ? 701 A D C5 1 ATOM 14 C C6 . A A 1 1 ? 23.075 65.634 58.581 1.00 62.03 ? 701 A D C6 1 ATOM 15 N N6 . A A 1 1 ? 23.153 66.213 59.780 1.00 63.47 ? 701 A D N6 1 ATOM 16 N N1 . A A 1 1 ? 21.869 65.235 58.122 1.00 62.78 ? 701 A D N1 1 ATOM 17 C C2 . A A 1 1 ? 21.797 64.690 56.907 1.00 62.54 ? 701 A D C2 1 ATOM 18 N N3 . A A 1 1 ? 22.766 64.471 56.028 1.00 63.23 ? 701 A D N3 1 ATOM 19 C C4 . A A 1 1 ? 23.948 64.877 56.521 1.00 64.00 ? 701 A D C4 1 ATOM 20 P P . G A 1 2 ? 27.473 63.362 51.520 1.00 90.12 ? 702 G D P 1 ATOM 21 O OP1 . G A 1 2 ? 28.092 62.880 50.248 1.00 92.54 ? 702 G D OP1 1 ATOM 22 O OP2 . G A 1 2 ? 28.072 62.934 52.826 1.00 90.23 ? 702 G D OP2 1 ATOM 23 O "O5'" . G A 1 2 ? 27.528 64.966 51.498 1.00 91.43 ? 702 G D "O5'" 1 ATOM 24 C "C5'" . G A 1 2 ? 28.641 65.690 50.926 1.00 89.96 ? 702 G D "C5'" 1 ATOM 25 C "C4'" . G A 1 2 ? 29.747 65.879 51.958 1.00 88.66 ? 702 G D "C4'" 1 ATOM 26 O "O4'" . G A 1 2 ? 30.694 66.897 51.506 1.00 87.79 ? 702 G D "O4'" 1 ATOM 27 C "C3'" . G A 1 2 ? 29.315 66.398 53.327 1.00 87.26 ? 702 G D "C3'" 1 ATOM 28 O "O3'" . G A 1 2 ? 28.693 65.415 54.188 1.00 85.64 ? 702 G D "O3'" 1 ATOM 29 C "C2'" . G A 1 2 ? 30.623 66.938 53.892 1.00 86.21 ? 702 G D "C2'" 1 ATOM 30 O "O2'" . G A 1 2 ? 31.448 65.925 54.437 1.00 82.74 ? 702 G D "O2'" 1 ATOM 31 C "C1'" . G A 1 2 ? 31.246 67.566 52.642 1.00 86.43 ? 702 G D "C1'" 1 ATOM 32 N N9 . G A 1 2 ? 30.976 69.002 52.543 1.00 86.16 ? 702 G D N9 1 ATOM 33 C C8 . G A 1 2 ? 31.677 70.014 53.170 1.00 85.76 ? 702 G D C8 1 ATOM 34 N N7 . G A 1 2 ? 31.182 71.203 52.944 1.00 85.76 ? 702 G D N7 1 ATOM 35 C C5 . G A 1 2 ? 30.092 70.972 52.105 1.00 85.65 ? 702 G D C5 1 ATOM 36 C C6 . G A 1 2 ? 29.155 71.893 51.515 1.00 85.72 ? 702 G D C6 1 ATOM 37 O O6 . G A 1 2 ? 29.098 73.134 51.636 1.00 84.42 ? 702 G D O6 1 ATOM 38 N N1 . G A 1 2 ? 28.216 71.229 50.721 1.00 85.05 ? 702 G D N1 1 ATOM 39 C C2 . G A 1 2 ? 28.170 69.861 50.518 1.00 84.72 ? 702 G D C2 1 ATOM 40 N N2 . G A 1 2 ? 27.186 69.407 49.713 1.00 83.70 ? 702 G D N2 1 ATOM 41 N N3 . G A 1 2 ? 29.028 69.000 51.064 1.00 84.69 ? 702 G D N3 1 ATOM 42 C C4 . G A 1 2 ? 29.955 69.620 51.839 1.00 85.69 ? 702 G D C4 1 ATOM 43 N N . GLN B 2 5 ? 2.983 74.676 63.863 1.00 52.48 ? 5 GLN A N 1 ATOM 44 C CA . GLN B 2 5 ? 3.568 73.434 64.464 1.00 52.49 ? 5 GLN A CA 1 ATOM 45 C C . GLN B 2 5 ? 4.128 72.475 63.396 1.00 50.39 ? 5 GLN A C 1 ATOM 46 O O . GLN B 2 5 ? 3.535 72.295 62.324 1.00 52.50 ? 5 GLN A O 1 ATOM 47 C CB . GLN B 2 5 ? 2.504 72.700 65.292 1.00 54.19 ? 5 GLN A CB 1 ATOM 48 C CG . GLN B 2 5 ? 1.991 73.477 66.518 1.00 57.01 ? 5 GLN A CG 1 ATOM 49 C CD . GLN B 2 5 ? 3.037 73.628 67.616 1.00 58.30 ? 5 GLN A CD 1 ATOM 50 O OE1 . GLN B 2 5 ? 3.990 74.399 67.481 1.00 60.12 ? 5 GLN A OE1 1 ATOM 51 N NE2 . GLN B 2 5 ? 2.866 72.880 68.705 1.00 56.04 ? 5 GLN A NE2 1 ATOM 52 N N . TYR B 2 6 ? 5.279 71.867 63.685 1.00 46.07 ? 6 TYR A N 1 ATOM 53 C CA . TYR B 2 6 ? 5.894 70.918 62.755 1.00 39.57 ? 6 TYR A CA 1 ATOM 54 C C . TYR B 2 6 ? 5.536 69.499 63.164 1.00 35.90 ? 6 TYR A C 1 ATOM 55 O O . TYR B 2 6 ? 5.401 69.201 64.353 1.00 36.27 ? 6 TYR A O 1 ATOM 56 C CB . TYR B 2 6 ? 7.416 71.056 62.746 1.00 37.30 ? 6 TYR A CB 1 ATOM 57 C CG . TYR B 2 6 ? 7.919 72.368 62.210 1.00 35.08 ? 6 TYR A CG 1 ATOM 58 C CD1 . TYR B 2 6 ? 7.732 72.720 60.875 1.00 33.81 ? 6 TYR A CD1 1 ATOM 59 C CD2 . TYR B 2 6 ? 8.612 73.249 63.033 1.00 33.88 ? 6 TYR A CD2 1 ATOM 60 C CE1 . TYR B 2 6 ? 8.230 73.919 60.374 1.00 32.29 ? 6 TYR A CE1 1 ATOM 61 C CE2 . TYR B 2 6 ? 9.112 74.446 62.544 1.00 32.39 ? 6 TYR A CE2 1 ATOM 62 C CZ . TYR B 2 6 ? 8.918 74.773 61.217 1.00 31.29 ? 6 TYR A CZ 1 ATOM 63 O OH . TYR B 2 6 ? 9.420 75.958 60.748 1.00 32.39 ? 6 TYR A OH 1 ATOM 64 N N . PRO B 2 7 ? 5.374 68.607 62.177 1.00 31.59 ? 7 PRO A N 1 ATOM 65 C CA . PRO B 2 7 ? 5.033 67.202 62.393 1.00 29.48 ? 7 PRO A CA 1 ATOM 66 C C . PRO B 2 7 ? 6.043 66.546 63.326 1.00 28.06 ? 7 PRO A C 1 ATOM 67 O O . PRO B 2 7 ? 7.221 66.901 63.313 1.00 27.50 ? 7 PRO A O 1 ATOM 68 C CB . PRO B 2 7 ? 5.099 66.622 60.990 1.00 28.83 ? 7 PRO A CB 1 ATOM 69 C CG . PRO B 2 7 ? 4.722 67.772 60.133 1.00 29.68 ? 7 PRO A CG 1 ATOM 70 C CD . PRO B 2 7 ? 5.492 68.898 60.741 1.00 30.86 ? 7 PRO A CD 1 ATOM 71 N N . ILE B 2 8 ? 5.588 65.592 64.132 1.00 26.72 ? 8 ILE A N 1 ATOM 72 C CA . ILE B 2 8 ? 6.478 64.915 65.064 1.00 27.03 ? 8 ILE A CA 1 ATOM 73 C C . ILE B 2 8 ? 6.383 63.399 65.058 1.00 27.25 ? 8 ILE A C 1 ATOM 74 O O . ILE B 2 8 ? 5.405 62.823 65.524 1.00 28.22 ? 8 ILE A O 1 ATOM 75 C CB . ILE B 2 8 ? 6.244 65.379 66.520 1.00 25.79 ? 8 ILE A CB 1 ATOM 76 C CG1 . ILE B 2 8 ? 6.461 66.881 66.626 1.00 26.91 ? 8 ILE A CG1 1 ATOM 77 C CG2 . ILE B 2 8 ? 7.227 64.692 67.464 1.00 24.65 ? 8 ILE A CG2 1 ATOM 78 C CD1 . ILE B 2 8 ? 6.259 67.408 68.021 1.00 30.08 ? 8 ILE A CD1 1 ATOM 79 N N . ILE B 2 9 ? 7.417 62.760 64.529 1.00 28.23 ? 9 ILE A N 1 ATOM 80 C CA . ILE B 2 9 ? 7.491 61.312 64.508 1.00 30.17 ? 9 ILE A CA 1 ATOM 81 C C . ILE B 2 9 ? 8.333 60.946 65.726 1.00 31.88 ? 9 ILE A C 1 ATOM 82 O O . ILE B 2 9 ? 9.268 61.666 66.065 1.00 32.52 ? 9 ILE A O 1 ATOM 83 C CB . ILE B 2 9 ? 8.238 60.789 63.266 1.00 29.41 ? 9 ILE A CB 1 ATOM 84 C CG1 . ILE B 2 9 ? 7.475 61.128 61.987 1.00 30.29 ? 9 ILE A CG1 1 ATOM 85 C CG2 . ILE B 2 9 ? 8.428 59.298 63.383 1.00 30.28 ? 9 ILE A CG2 1 ATOM 86 C CD1 . ILE B 2 9 ? 7.805 62.480 61.415 1.00 31.75 ? 9 ILE A CD1 1 ATOM 87 N N . ASN B 2 10 ? 8.005 59.848 66.396 1.00 34.18 ? 10 ASN A N 1 ATOM 88 C CA . ASN B 2 10 ? 8.810 59.423 67.535 1.00 36.18 ? 10 ASN A CA 1 ATOM 89 C C . ASN B 2 10 ? 9.202 57.944 67.462 1.00 36.90 ? 10 ASN A C 1 ATOM 90 O O . ASN B 2 10 ? 8.478 57.108 66.922 1.00 38.32 ? 10 ASN A O 1 ATOM 91 C CB . ASN B 2 10 ? 8.118 59.731 68.881 1.00 38.30 ? 10 ASN A CB 1 ATOM 92 C CG . ASN B 2 10 ? 6.700 59.175 68.976 1.00 41.56 ? 10 ASN A CG 1 ATOM 93 O OD1 . ASN B 2 10 ? 6.345 58.201 68.305 1.00 43.16 ? 10 ASN A OD1 1 ATOM 94 N ND2 . ASN B 2 10 ? 5.886 59.787 69.837 1.00 43.02 ? 10 ASN A ND2 1 ATOM 95 N N . PHE B 2 11 ? 10.378 57.642 67.991 1.00 36.82 ? 11 PHE A N 1 ATOM 96 C CA . PHE B 2 11 ? 10.903 56.288 68.011 1.00 37.44 ? 11 PHE A CA 1 ATOM 97 C C . PHE B 2 11 ? 11.637 56.168 69.330 1.00 38.19 ? 11 PHE A C 1 ATOM 98 O O . PHE B 2 11 ? 12.244 57.131 69.806 1.00 38.13 ? 11 PHE A O 1 ATOM 99 C CB . PHE B 2 11 ? 11.882 56.081 66.852 1.00 38.06 ? 11 PHE A CB 1 ATOM 100 C CG . PHE B 2 11 ? 12.579 54.740 66.860 1.00 37.73 ? 11 PHE A CG 1 ATOM 101 C CD1 . PHE B 2 11 ? 11.890 53.578 66.545 1.00 38.31 ? 11 PHE A CD1 1 ATOM 102 C CD2 . PHE B 2 11 ? 13.932 54.645 67.162 1.00 37.20 ? 11 PHE A CD2 1 ATOM 103 C CE1 . PHE B 2 11 ? 12.540 52.343 66.527 1.00 37.83 ? 11 PHE A CE1 1 ATOM 104 C CE2 . PHE B 2 11 ? 14.585 53.412 67.146 1.00 36.92 ? 11 PHE A CE2 1 ATOM 105 C CZ . PHE B 2 11 ? 13.887 52.263 66.828 1.00 36.17 ? 11 PHE A CZ 1 ATOM 106 N N . THR B 2 12 ? 11.572 54.989 69.928 1.00 38.98 ? 12 THR A N 1 ATOM 107 C CA . THR B 2 12 ? 12.238 54.754 71.197 1.00 38.55 ? 12 THR A CA 1 ATOM 108 C C . THR B 2 12 ? 13.085 53.491 71.060 1.00 39.82 ? 12 THR A C 1 ATOM 109 O O . THR B 2 12 ? 12.655 52.510 70.451 1.00 41.82 ? 12 THR A O 1 ATOM 110 C CB . THR B 2 12 ? 11.197 54.611 72.342 1.00 36.86 ? 12 THR A CB 1 ATOM 111 O OG1 . THR B 2 12 ? 11.874 54.379 73.582 1.00 36.79 ? 12 THR A OG1 1 ATOM 112 C CG2 . THR B 2 12 ? 10.240 53.470 72.063 1.00 34.75 ? 12 THR A CG2 1 ATOM 113 N N . THR B 2 13 ? 14.299 53.528 71.597 1.00 38.86 ? 13 THR A N 1 ATOM 114 C CA . THR B 2 13 ? 15.194 52.383 71.521 1.00 38.34 ? 13 THR A CA 1 ATOM 115 C C . THR B 2 13 ? 14.896 51.413 72.649 1.00 40.36 ? 13 THR A C 1 ATOM 116 O O . THR B 2 13 ? 15.604 50.427 72.828 1.00 41.67 ? 13 THR A O 1 ATOM 117 C CB . THR B 2 13 ? 16.651 52.814 71.651 1.00 36.66 ? 13 THR A CB 1 ATOM 118 O OG1 . THR B 2 13 ? 16.835 53.448 72.922 1.00 35.03 ? 13 THR A OG1 1 ATOM 119 C CG2 . THR B 2 13 ? 17.024 53.780 70.534 1.00 35.45 ? 13 THR A CG2 1 ATOM 120 N N . ALA B 2 14 ? 13.850 51.704 73.417 1.00 41.08 ? 14 ALA A N 1 ATOM 121 C CA . ALA B 2 14 ? 13.461 50.864 74.542 1.00 41.01 ? 14 ALA A CA 1 ATOM 122 C C . ALA B 2 14 ? 13.120 49.465 74.065 1.00 41.11 ? 14 ALA A C 1 ATOM 123 O O . ALA B 2 14 ? 13.915 48.546 74.211 1.00 43.07 ? 14 ALA A O 1 ATOM 124 C CB . ALA B 2 14 ? 12.280 51.470 75.249 1.00 41.13 ? 14 ALA A CB 1 ATOM 125 N N . GLY B 2 15 ? 11.934 49.300 73.498 1.00 40.33 ? 15 GLY A N 1 ATOM 126 C CA . GLY B 2 15 ? 11.545 47.993 73.002 1.00 40.45 ? 15 GLY A CA 1 ATOM 127 C C . GLY B 2 15 ? 11.751 47.917 71.503 1.00 40.48 ? 15 GLY A C 1 ATOM 128 O O . GLY B 2 15 ? 11.016 47.214 70.806 1.00 41.32 ? 15 GLY A O 1 ATOM 129 N N . ALA B 2 16 ? 12.754 48.649 71.012 1.00 40.15 ? 16 ALA A N 1 ATOM 130 C CA . ALA B 2 16 ? 13.072 48.691 69.587 1.00 39.18 ? 16 ALA A CA 1 ATOM 131 C C . ALA B 2 16 ? 13.069 47.289 68.995 1.00 38.92 ? 16 ALA A C 1 ATOM 132 O O . ALA B 2 16 ? 13.641 46.357 69.558 1.00 40.22 ? 16 ALA A O 1 ATOM 133 C CB . ALA B 2 16 ? 14.429 49.359 69.369 1.00 38.51 ? 16 ALA A CB 1 ATOM 134 N N . THR B 2 17 ? 12.429 47.154 67.845 1.00 38.99 ? 17 THR A N 1 ATOM 135 C CA . THR B 2 17 ? 12.318 45.870 67.179 1.00 38.85 ? 17 THR A CA 1 ATOM 136 C C . THR B 2 17 ? 12.459 46.103 65.654 1.00 38.14 ? 17 THR A C 1 ATOM 137 O O . THR B 2 17 ? 12.475 47.257 65.213 1.00 39.14 ? 17 THR A O 1 ATOM 138 C CB . THR B 2 17 ? 10.955 45.236 67.574 1.00 38.00 ? 17 THR A CB 1 ATOM 139 O OG1 . THR B 2 17 ? 10.925 43.864 67.174 1.00 41.69 ? 17 THR A OG1 1 ATOM 140 C CG2 . THR B 2 17 ? 9.792 46.000 66.943 1.00 35.86 ? 17 THR A CG2 1 ATOM 141 N N . VAL B 2 18 ? 12.580 45.050 64.842 1.00 36.97 ? 18 VAL A N 1 ATOM 142 C CA . VAL B 2 18 ? 12.734 45.279 63.399 1.00 36.72 ? 18 VAL A CA 1 ATOM 143 C C . VAL B 2 18 ? 11.502 45.932 62.780 1.00 36.08 ? 18 VAL A C 1 ATOM 144 O O . VAL B 2 18 ? 11.618 46.648 61.785 1.00 36.09 ? 18 VAL A O 1 ATOM 145 C CB . VAL B 2 18 ? 13.050 43.979 62.597 1.00 35.92 ? 18 VAL A CB 1 ATOM 146 C CG1 . VAL B 2 18 ? 14.303 43.315 63.134 1.00 34.32 ? 18 VAL A CG1 1 ATOM 147 C CG2 . VAL B 2 18 ? 11.879 43.037 62.643 1.00 37.00 ? 18 VAL A CG2 1 ATOM 148 N N . GLN B 2 19 ? 10.331 45.690 63.373 1.00 36.11 ? 19 GLN A N 1 ATOM 149 C CA . GLN B 2 19 ? 9.079 46.266 62.875 1.00 35.92 ? 19 GLN A CA 1 ATOM 150 C C . GLN B 2 19 ? 8.946 47.741 63.241 1.00 33.88 ? 19 GLN A C 1 ATOM 151 O O . GLN B 2 19 ? 8.634 48.572 62.388 1.00 32.09 ? 19 GLN A O 1 ATOM 152 C CB . GLN B 2 19 ? 7.857 45.514 63.430 1.00 38.56 ? 19 GLN A CB 1 ATOM 153 C CG . GLN B 2 19 ? 7.721 44.058 62.997 1.00 43.39 ? 19 GLN A CG 1 ATOM 154 C CD . GLN B 2 19 ? 8.323 43.081 64.005 1.00 47.44 ? 19 GLN A CD 1 ATOM 155 O OE1 . GLN B 2 19 ? 8.712 43.476 65.106 1.00 49.31 ? 19 GLN A OE1 1 ATOM 156 N NE2 . GLN B 2 19 ? 8.388 41.799 63.636 1.00 47.94 ? 19 GLN A NE2 1 ATOM 157 N N . SER B 2 20 ? 9.182 48.059 64.513 1.00 32.60 ? 20 SER A N 1 ATOM 158 C CA . SER B 2 20 ? 9.077 49.434 64.989 1.00 32.54 ? 20 SER A CA 1 ATOM 159 C C . SER B 2 20 ? 10.079 50.340 64.285 1.00 33.52 ? 20 SER A C 1 ATOM 160 O O . SER B 2 20 ? 9.877 51.553 64.189 1.00 33.28 ? 20 SER A O 1 ATOM 161 C CB . SER B 2 20 ? 9.296 49.494 66.502 1.00 32.08 ? 20 SER A CB 1 ATOM 162 O OG . SER B 2 20 ? 10.626 49.168 66.842 1.00 32.34 ? 20 SER A OG 1 ATOM 163 N N . TYR B 2 21 ? 11.167 49.747 63.799 1.00 34.04 ? 21 TYR A N 1 ATOM 164 C CA . TYR B 2 21 ? 12.187 50.505 63.087 1.00 33.32 ? 21 TYR A CA 1 ATOM 165 C C . TYR B 2 21 ? 11.736 50.745 61.647 1.00 33.03 ? 21 TYR A C 1 ATOM 166 O O . TYR B 2 21 ? 11.920 51.831 61.102 1.00 33.71 ? 21 TYR A O 1 ATOM 167 C CB . TYR B 2 21 ? 13.513 49.755 63.084 1.00 31.48 ? 21 TYR A CB 1 ATOM 168 C CG . TYR B 2 21 ? 14.591 50.548 62.410 1.00 29.82 ? 21 TYR A CG 1 ATOM 169 C CD1 . TYR B 2 21 ? 15.051 51.734 62.972 1.00 30.24 ? 21 TYR A CD1 1 ATOM 170 C CD2 . TYR B 2 21 ? 15.112 50.152 61.178 1.00 29.47 ? 21 TYR A CD2 1 ATOM 171 C CE1 . TYR B 2 21 ? 16.005 52.514 62.327 1.00 31.26 ? 21 TYR A CE1 1 ATOM 172 C CE2 . TYR B 2 21 ? 16.067 50.924 60.521 1.00 30.04 ? 21 TYR A CE2 1 ATOM 173 C CZ . TYR B 2 21 ? 16.512 52.107 61.105 1.00 31.64 ? 21 TYR A CZ 1 ATOM 174 O OH . TYR B 2 21 ? 17.478 52.878 60.493 1.00 30.67 ? 21 TYR A OH 1 ATOM 175 N N . THR B 2 22 ? 11.147 49.721 61.037 1.00 32.79 ? 22 THR A N 1 ATOM 176 C CA . THR B 2 22 ? 10.657 49.814 59.666 1.00 33.18 ? 22 THR A CA 1 ATOM 177 C C . THR B 2 22 ? 9.474 50.793 59.558 1.00 34.14 ? 22 THR A C 1 ATOM 178 O O . THR B 2 22 ? 9.281 51.427 58.512 1.00 34.95 ? 22 THR A O 1 ATOM 179 C CB . THR B 2 22 ? 10.234 48.419 59.146 1.00 32.56 ? 22 THR A CB 1 ATOM 180 O OG1 . THR B 2 22 ? 11.391 47.581 59.044 1.00 32.38 ? 22 THR A OG1 1 ATOM 181 C CG2 . THR B 2 22 ? 9.584 48.526 57.780 1.00 32.49 ? 22 THR A CG2 1 ATOM 182 N N . ASN B 2 23 ? 8.686 50.913 60.630 1.00 33.81 ? 23 ASN A N 1 ATOM 183 C CA . ASN B 2 23 ? 7.544 51.830 60.645 1.00 32.50 ? 23 ASN A CA 1 ATOM 184 C C . ASN B 2 23 ? 8.046 53.249 60.878 1.00 31.41 ? 23 ASN A C 1 ATOM 185 O O . ASN B 2 23 ? 7.523 54.212 60.326 1.00 31.95 ? 23 ASN A O 1 ATOM 186 C CB . ASN B 2 23 ? 6.549 51.467 61.758 1.00 34.33 ? 23 ASN A CB 1 ATOM 187 C CG . ASN B 2 23 ? 5.888 50.115 61.544 1.00 35.27 ? 23 ASN A CG 1 ATOM 188 O OD1 . ASN B 2 23 ? 5.513 49.768 60.426 1.00 36.21 ? 23 ASN A OD1 1 ATOM 189 N ND2 . ASN B 2 23 ? 5.727 49.354 62.621 1.00 34.76 ? 23 ASN A ND2 1 ATOM 190 N N . PHE B 2 24 ? 9.064 53.370 61.712 1.00 29.76 ? 24 PHE A N 1 ATOM 191 C CA . PHE B 2 24 ? 9.644 54.665 62.012 1.00 29.49 ? 24 PHE A CA 1 ATOM 192 C C . PHE B 2 24 ? 10.137 55.310 60.716 1.00 30.20 ? 24 PHE A C 1 ATOM 193 O O . PHE B 2 24 ? 9.712 56.403 60.356 1.00 30.63 ? 24 PHE A O 1 ATOM 194 C CB . PHE B 2 24 ? 10.795 54.474 63.008 1.00 28.23 ? 24 PHE A CB 1 ATOM 195 C CG . PHE B 2 24 ? 11.666 55.679 63.177 1.00 26.53 ? 24 PHE A CG 1 ATOM 196 C CD1 . PHE B 2 24 ? 11.138 56.877 63.611 1.00 25.72 ? 24 PHE A CD1 1 ATOM 197 C CD2 . PHE B 2 24 ? 13.028 55.606 62.909 1.00 26.69 ? 24 PHE A CD2 1 ATOM 198 C CE1 . PHE B 2 24 ? 11.952 57.984 63.775 1.00 26.74 ? 24 PHE A CE1 1 ATOM 199 C CE2 . PHE B 2 24 ? 13.848 56.706 63.071 1.00 26.01 ? 24 PHE A CE2 1 ATOM 200 C CZ . PHE B 2 24 ? 13.309 57.898 63.506 1.00 27.06 ? 24 PHE A CZ 1 ATOM 201 N N . ILE B 2 25 ? 11.021 54.613 60.012 1.00 29.72 ? 25 ILE A N 1 ATOM 202 C CA . ILE B 2 25 ? 11.577 55.106 58.760 1.00 29.46 ? 25 ILE A CA 1 ATOM 203 C C . ILE B 2 25 ? 10.478 55.313 57.714 1.00 30.54 ? 25 ILE A C 1 ATOM 204 O O . ILE B 2 25 ? 10.536 56.239 56.906 1.00 30.75 ? 25 ILE A O 1 ATOM 205 C CB . ILE B 2 25 ? 12.653 54.128 58.246 1.00 28.47 ? 25 ILE A CB 1 ATOM 206 C CG1 . ILE B 2 25 ? 13.793 54.060 59.260 1.00 27.30 ? 25 ILE A CG1 1 ATOM 207 C CG2 . ILE B 2 25 ? 13.193 54.577 56.899 1.00 29.20 ? 25 ILE A CG2 1 ATOM 208 C CD1 . ILE B 2 25 ? 14.518 55.381 59.451 1.00 27.79 ? 25 ILE A CD1 1 ATOM 209 N N . ARG B 2 26 ? 9.468 54.452 57.740 1.00 31.71 ? 26 ARG A N 1 ATOM 210 C CA . ARG B 2 26 ? 8.348 54.554 56.812 1.00 33.14 ? 26 ARG A CA 1 ATOM 211 C C . ARG B 2 26 ? 7.588 55.850 57.089 1.00 33.46 ? 26 ARG A C 1 ATOM 212 O O . ARG B 2 26 ? 7.056 56.483 56.167 1.00 34.45 ? 26 ARG A O 1 ATOM 213 C CB . ARG B 2 26 ? 7.426 53.351 56.991 1.00 35.59 ? 26 ARG A CB 1 ATOM 214 C CG . ARG B 2 26 ? 6.187 53.334 56.112 1.00 39.66 ? 26 ARG A CG 1 ATOM 215 C CD . ARG B 2 26 ? 5.697 51.908 55.971 1.00 43.11 ? 26 ARG A CD 1 ATOM 216 N NE . ARG B 2 26 ? 6.745 51.088 55.361 1.00 48.16 ? 26 ARG A NE 1 ATOM 217 C CZ . ARG B 2 26 ? 6.757 49.759 55.352 1.00 50.11 ? 26 ARG A CZ 1 ATOM 218 N NH1 . ARG B 2 26 ? 5.767 49.081 55.928 1.00 52.10 ? 26 ARG A NH1 1 ATOM 219 N NH2 . ARG B 2 26 ? 7.758 49.108 54.765 1.00 49.40 ? 26 ARG A NH2 1 ATOM 220 N N . ALA B 2 27 ? 7.556 56.236 58.367 1.00 32.64 ? 27 ALA A N 1 ATOM 221 C CA . ALA B 2 27 ? 6.888 57.457 58.828 1.00 31.03 ? 27 ALA A CA 1 ATOM 222 C C . ALA B 2 27 ? 7.700 58.710 58.484 1.00 30.54 ? 27 ALA A C 1 ATOM 223 O O . ALA B 2 27 ? 7.136 59.740 58.110 1.00 30.08 ? 27 ALA A O 1 ATOM 224 C CB . ALA B 2 27 ? 6.661 57.384 60.330 1.00 30.23 ? 27 ALA A CB 1 ATOM 225 N N . VAL B 2 28 ? 9.023 58.607 58.621 1.00 29.63 ? 28 VAL A N 1 ATOM 226 C CA . VAL B 2 28 ? 9.952 59.695 58.320 1.00 28.46 ? 28 VAL A CA 1 ATOM 227 C C . VAL B 2 28 ? 9.937 60.011 56.819 1.00 29.40 ? 28 VAL A C 1 ATOM 228 O O . VAL B 2 28 ? 9.941 61.182 56.415 1.00 29.92 ? 28 VAL A O 1 ATOM 229 C CB . VAL B 2 28 ? 11.389 59.314 58.763 1.00 27.54 ? 28 VAL A CB 1 ATOM 230 C CG1 . VAL B 2 28 ? 12.383 60.394 58.369 1.00 26.03 ? 28 VAL A CG1 1 ATOM 231 C CG2 . VAL B 2 28 ? 11.412 59.111 60.262 1.00 26.98 ? 28 VAL A CG2 1 ATOM 232 N N . ARG B 2 29 ? 9.919 58.971 55.990 1.00 28.32 ? 29 ARG A N 1 ATOM 233 C CA . ARG B 2 29 ? 9.872 59.169 54.548 1.00 27.58 ? 29 ARG A CA 1 ATOM 234 C C . ARG B 2 29 ? 8.510 59.726 54.193 1.00 29.37 ? 29 ARG A C 1 ATOM 235 O O . ARG B 2 29 ? 8.384 60.587 53.325 1.00 28.85 ? 29 ARG A O 1 ATOM 236 C CB . ARG B 2 29 ? 10.055 57.853 53.813 1.00 25.21 ? 29 ARG A CB 1 ATOM 237 C CG . ARG B 2 29 ? 11.453 57.319 53.815 1.00 22.99 ? 29 ARG A CG 1 ATOM 238 C CD . ARG B 2 29 ? 11.479 56.064 53.004 1.00 20.37 ? 29 ARG A CD 1 ATOM 239 N NE . ARG B 2 29 ? 12.717 55.339 53.200 1.00 20.24 ? 29 ARG A NE 1 ATOM 240 C CZ . ARG B 2 29 ? 12.772 54.029 53.390 1.00 22.64 ? 29 ARG A CZ 1 ATOM 241 N NH1 . ARG B 2 29 ? 11.651 53.327 53.404 1.00 25.00 ? 29 ARG A NH1 1 ATOM 242 N NH2 . ARG B 2 29 ? 13.937 53.426 53.571 1.00 24.66 ? 29 ARG A NH2 1 ATOM 243 N N . GLY B 2 30 ? 7.488 59.219 54.875 1.00 30.68 ? 30 GLY A N 1 ATOM 244 C CA . GLY B 2 30 ? 6.136 59.665 54.612 1.00 32.29 ? 30 GLY A CA 1 ATOM 245 C C . GLY B 2 30 ? 5.923 61.149 54.831 1.00 33.67 ? 30 GLY A C 1 ATOM 246 O O . GLY B 2 30 ? 5.069 61.762 54.183 1.00 33.68 ? 30 GLY A O 1 ATOM 247 N N . ARG B 2 31 ? 6.713 61.730 55.732 1.00 34.72 ? 31 ARG A N 1 ATOM 248 C CA . ARG B 2 31 ? 6.601 63.147 56.074 1.00 36.05 ? 31 ARG A CA 1 ATOM 249 C C . ARG B 2 31 ? 7.525 64.079 55.278 1.00 35.96 ? 31 ARG A C 1 ATOM 250 O O . ARG B 2 31 ? 7.299 65.291 55.218 1.00 34.43 ? 31 ARG A O 1 ATOM 251 C CB . ARG B 2 31 ? 6.866 63.322 57.566 1.00 37.72 ? 31 ARG A CB 1 ATOM 252 C CG . ARG B 2 31 ? 5.939 64.301 58.252 1.00 43.83 ? 31 ARG A CG 1 ATOM 253 C CD . ARG B 2 31 ? 4.509 63.775 58.353 1.00 44.89 ? 31 ARG A CD 1 ATOM 254 N NE . ARG B 2 31 ? 4.483 62.379 58.793 1.00 47.85 ? 31 ARG A NE 1 ATOM 255 C CZ . ARG B 2 31 ? 3.503 61.842 59.515 1.00 48.57 ? 31 ARG A CZ 1 ATOM 256 N NH1 . ARG B 2 31 ? 2.472 62.596 59.886 1.00 47.31 ? 31 ARG A NH1 1 ATOM 257 N NH2 . ARG B 2 31 ? 3.544 60.551 59.845 1.00 46.56 ? 31 ARG A NH2 1 ATOM 258 N N . LEU B 2 32 ? 8.561 63.518 54.665 1.00 36.11 ? 32 LEU A N 1 ATOM 259 C CA . LEU B 2 32 ? 9.490 64.326 53.888 1.00 36.88 ? 32 LEU A CA 1 ATOM 260 C C . LEU B 2 32 ? 8.939 64.684 52.514 1.00 37.81 ? 32 LEU A C 1 ATOM 261 O O . LEU B 2 32 ? 8.910 65.855 52.144 1.00 38.25 ? 32 LEU A O 1 ATOM 262 C CB . LEU B 2 32 ? 10.825 63.596 53.743 1.00 36.27 ? 32 LEU A CB 1 ATOM 263 C CG . LEU B 2 32 ? 11.619 63.488 55.044 1.00 35.37 ? 32 LEU A CG 1 ATOM 264 C CD1 . LEU B 2 32 ? 12.798 62.536 54.874 1.00 35.30 ? 32 LEU A CD1 1 ATOM 265 C CD2 . LEU B 2 32 ? 12.083 64.879 55.442 1.00 35.81 ? 32 LEU A CD2 1 ATOM 266 N N . THR B 2 33 ? 8.505 63.673 51.761 1.00 37.78 ? 33 THR A N 1 ATOM 267 C CA . THR B 2 33 ? 7.950 63.883 50.422 1.00 37.40 ? 33 THR A CA 1 ATOM 268 C C . THR B 2 33 ? 6.448 64.070 50.475 1.00 37.25 ? 33 THR A C 1 ATOM 269 O O . THR B 2 33 ? 5.788 63.597 51.400 1.00 36.61 ? 33 THR A O 1 ATOM 270 C CB . THR B 2 33 ? 8.199 62.681 49.491 1.00 37.83 ? 33 THR A CB 1 ATOM 271 O OG1 . THR B 2 33 ? 7.921 61.468 50.201 1.00 37.89 ? 33 THR A OG1 1 ATOM 272 C CG2 . THR B 2 33 ? 9.620 62.673 48.975 1.00 38.73 ? 33 THR A CG2 1 ATOM 273 N N . THR B 2 34 ? 5.915 64.755 49.468 1.00 37.76 ? 34 THR A N 1 ATOM 274 C CA . THR B 2 34 ? 4.481 64.988 49.370 1.00 37.76 ? 34 THR A CA 1 ATOM 275 C C . THR B 2 34 ? 3.895 63.991 48.375 1.00 37.85 ? 34 THR A C 1 ATOM 276 O O . THR B 2 34 ? 2.686 63.943 48.171 1.00 39.07 ? 34 THR A O 1 ATOM 277 C CB . THR B 2 34 ? 4.181 66.422 48.894 1.00 37.18 ? 34 THR A CB 1 ATOM 278 O OG1 . THR B 2 34 ? 4.686 66.612 47.564 1.00 36.50 ? 34 THR A OG1 1 ATOM 279 C CG2 . THR B 2 34 ? 4.842 67.430 49.824 1.00 37.03 ? 34 THR A CG2 1 ATOM 280 N N . GLY B 2 35 ? 4.765 63.199 47.755 1.00 37.52 ? 35 GLY A N 1 ATOM 281 C CA . GLY B 2 35 ? 4.318 62.211 46.789 1.00 38.48 ? 35 GLY A CA 1 ATOM 282 C C . GLY B 2 35 ? 3.817 62.805 45.482 1.00 38.40 ? 35 GLY A C 1 ATOM 283 O O . GLY B 2 35 ? 3.273 62.092 44.637 1.00 39.07 ? 35 GLY A O 1 ATOM 284 N N . ALA B 2 36 ? 4.006 64.111 45.313 1.00 36.53 ? 36 ALA A N 1 ATOM 285 C CA . ALA B 2 36 ? 3.570 64.801 44.106 1.00 34.95 ? 36 ALA A CA 1 ATOM 286 C C . ALA B 2 36 ? 4.614 64.669 43.014 1.00 34.20 ? 36 ALA A C 1 ATOM 287 O O . ALA B 2 36 ? 4.287 64.569 41.840 1.00 35.32 ? 36 ALA A O 1 ATOM 288 C CB . ALA B 2 36 ? 3.321 66.271 44.406 1.00 33.21 ? 36 ALA A CB 1 ATOM 289 N N . ASP B 2 37 ? 5.876 64.664 43.413 1.00 33.48 ? 37 ASP A N 1 ATOM 290 C CA . ASP B 2 37 ? 6.982 64.575 42.472 1.00 32.56 ? 37 ASP A CA 1 ATOM 291 C C . ASP B 2 37 ? 7.715 63.239 42.601 1.00 32.73 ? 37 ASP A C 1 ATOM 292 O O . ASP B 2 37 ? 8.352 62.968 43.624 1.00 35.33 ? 37 ASP A O 1 ATOM 293 C CB . ASP B 2 37 ? 7.937 65.751 42.721 1.00 30.20 ? 37 ASP A CB 1 ATOM 294 C CG . ASP B 2 37 ? 9.093 65.782 41.760 1.00 28.21 ? 37 ASP A CG 1 ATOM 295 O OD1 . ASP B 2 37 ? 9.036 65.068 40.745 1.00 26.78 ? 37 ASP A OD1 1 ATOM 296 O OD2 . ASP B 2 37 ? 10.059 66.533 42.014 1.00 27.54 ? 37 ASP A OD2 1 ATOM 297 N N . VAL B 2 38 ? 7.605 62.408 41.561 1.00 30.85 ? 38 VAL A N 1 ATOM 298 C CA . VAL B 2 38 ? 8.244 61.092 41.514 1.00 27.59 ? 38 VAL A CA 1 ATOM 299 C C . VAL B 2 38 ? 8.856 60.863 40.135 1.00 27.70 ? 38 VAL A C 1 ATOM 300 O O . VAL B 2 38 ? 8.190 61.043 39.120 1.00 27.92 ? 38 VAL A O 1 ATOM 301 C CB . VAL B 2 38 ? 7.227 59.964 41.789 1.00 24.74 ? 38 VAL A CB 1 ATOM 302 C CG1 . VAL B 2 38 ? 7.875 58.623 41.572 1.00 23.02 ? 38 VAL A CG1 1 ATOM 303 C CG2 . VAL B 2 38 ? 6.702 60.066 43.207 1.00 23.53 ? 38 VAL A CG2 1 ATOM 304 N N . ARG B 2 39 ? 10.123 60.472 40.093 1.00 28.51 ? 39 ARG A N 1 ATOM 305 C CA . ARG B 2 39 ? 10.776 60.236 38.813 1.00 31.88 ? 39 ARG A CA 1 ATOM 306 C C . ARG B 2 39 ? 11.448 58.881 38.773 1.00 34.72 ? 39 ARG A C 1 ATOM 307 O O . ARG B 2 39 ? 12.230 58.537 39.663 1.00 36.35 ? 39 ARG A O 1 ATOM 308 C CB . ARG B 2 39 ? 11.789 61.334 38.538 1.00 30.30 ? 39 ARG A CB 1 ATOM 309 C CG . ARG B 2 39 ? 11.141 62.678 38.577 1.00 31.07 ? 39 ARG A CG 1 ATOM 310 C CD . ARG B 2 39 ? 12.119 63.790 38.417 1.00 31.87 ? 39 ARG A CD 1 ATOM 311 N NE . ARG B 2 39 ? 11.597 64.979 39.065 1.00 35.39 ? 39 ARG A NE 1 ATOM 312 C CZ . ARG B 2 39 ? 12.226 66.145 39.106 1.00 38.18 ? 39 ARG A CZ 1 ATOM 313 N NH1 . ARG B 2 39 ? 13.410 66.278 38.525 1.00 39.66 ? 39 ARG A NH1 1 ATOM 314 N NH2 . ARG B 2 39 ? 11.679 67.171 39.746 1.00 40.54 ? 39 ARG A NH2 1 ATOM 315 N N . HIS B 2 40 ? 11.132 58.116 37.728 1.00 36.03 ? 40 HIS A N 1 ATOM 316 C CA . HIS B 2 40 ? 11.669 56.776 37.551 1.00 35.50 ? 40 HIS A CA 1 ATOM 317 C C . HIS B 2 40 ? 11.313 55.907 38.766 1.00 35.42 ? 40 HIS A C 1 ATOM 318 O O . HIS B 2 40 ? 12.076 55.028 39.169 1.00 35.99 ? 40 HIS A O 1 ATOM 319 C CB . HIS B 2 40 ? 13.179 56.857 37.329 1.00 36.14 ? 40 HIS A CB 1 ATOM 320 C CG . HIS B 2 40 ? 13.561 57.632 36.105 1.00 37.64 ? 40 HIS A CG 1 ATOM 321 N ND1 . HIS B 2 40 ? 13.248 57.210 34.830 1.00 38.84 ? 40 HIS A ND1 1 ATOM 322 C CD2 . HIS B 2 40 ? 14.205 58.815 35.959 1.00 38.53 ? 40 HIS A CD2 1 ATOM 323 C CE1 . HIS B 2 40 ? 13.682 58.099 33.954 1.00 38.73 ? 40 HIS A CE1 1 ATOM 324 N NE2 . HIS B 2 40 ? 14.266 59.083 34.612 1.00 38.69 ? 40 HIS A NE2 1 ATOM 325 N N . GLU B 2 41 ? 10.135 56.184 39.332 1.00 34.60 ? 41 GLU A N 1 ATOM 326 C CA . GLU B 2 41 ? 9.572 55.476 40.485 1.00 35.01 ? 41 GLU A CA 1 ATOM 327 C C . GLU B 2 41 ? 10.185 55.833 41.833 1.00 35.22 ? 41 GLU A C 1 ATOM 328 O O . GLU B 2 41 ? 9.910 55.170 42.840 1.00 35.84 ? 41 GLU A O 1 ATOM 329 C CB . GLU B 2 41 ? 9.660 53.961 40.281 1.00 35.70 ? 41 GLU A CB 1 ATOM 330 C CG . GLU B 2 41 ? 9.126 53.492 38.941 1.00 38.60 ? 41 GLU A CG 1 ATOM 331 C CD . GLU B 2 41 ? 8.925 51.990 38.872 1.00 39.98 ? 41 GLU A CD 1 ATOM 332 O OE1 . GLU B 2 41 ? 9.073 51.316 39.921 1.00 37.95 ? 41 GLU A OE1 1 ATOM 333 O OE2 . GLU B 2 41 ? 8.608 51.496 37.763 1.00 41.37 ? 41 GLU A OE2 1 ATOM 334 N N . ILE B 2 42 ? 11.005 56.880 41.853 1.00 34.36 ? 42 ILE A N 1 ATOM 335 C CA . ILE B 2 42 ? 11.661 57.323 43.084 1.00 31.76 ? 42 ILE A CA 1 ATOM 336 C C . ILE B 2 42 ? 11.142 58.707 43.471 1.00 31.11 ? 42 ILE A C 1 ATOM 337 O O . ILE B 2 42 ? 11.195 59.649 42.678 1.00 31.91 ? 42 ILE A O 1 ATOM 338 C CB . ILE B 2 42 ? 13.199 57.363 42.890 1.00 31.27 ? 42 ILE A CB 1 ATOM 339 C CG1 . ILE B 2 42 ? 13.661 56.034 42.281 1.00 30.92 ? 42 ILE A CG1 1 ATOM 340 C CG2 . ILE B 2 42 ? 13.896 57.598 44.219 1.00 28.31 ? 42 ILE A CG2 1 ATOM 341 C CD1 . ILE B 2 42 ? 15.102 56.010 41.838 1.00 31.15 ? 42 ILE A CD1 1 ATOM 342 N N . PRO B 2 43 ? 10.618 58.848 44.695 1.00 29.53 ? 43 PRO A N 1 ATOM 343 C CA . PRO B 2 43 ? 10.096 60.144 45.137 1.00 29.05 ? 43 PRO A CA 1 ATOM 344 C C . PRO B 2 43 ? 11.160 61.233 45.267 1.00 29.98 ? 43 PRO A C 1 ATOM 345 O O . PRO B 2 43 ? 12.257 60.985 45.764 1.00 31.69 ? 43 PRO A O 1 ATOM 346 C CB . PRO B 2 43 ? 9.472 59.824 46.495 1.00 26.88 ? 43 PRO A CB 1 ATOM 347 C CG . PRO B 2 43 ? 9.174 58.383 46.417 1.00 26.80 ? 43 PRO A CG 1 ATOM 348 C CD . PRO B 2 43 ? 10.372 57.819 45.714 1.00 28.06 ? 43 PRO A CD 1 ATOM 349 N N . VAL B 2 44 ? 10.837 62.441 44.824 1.00 30.40 ? 44 VAL A N 1 ATOM 350 C CA . VAL B 2 44 ? 11.768 63.553 44.960 1.00 30.73 ? 44 VAL A CA 1 ATOM 351 C C . VAL B 2 44 ? 11.322 64.412 46.149 1.00 31.93 ? 44 VAL A C 1 ATOM 352 O O . VAL B 2 44 ? 10.136 64.437 46.505 1.00 33.11 ? 44 VAL A O 1 ATOM 353 C CB . VAL B 2 44 ? 11.808 64.419 43.696 1.00 30.08 ? 44 VAL A CB 1 ATOM 354 C CG1 . VAL B 2 44 ? 12.799 65.557 43.881 1.00 27.88 ? 44 VAL A CG1 1 ATOM 355 C CG2 . VAL B 2 44 ? 12.189 63.565 42.506 1.00 30.28 ? 44 VAL A CG2 1 ATOM 356 N N . LEU B 2 45 ? 12.279 65.096 46.768 1.00 32.10 ? 45 LEU A N 1 ATOM 357 C CA . LEU B 2 45 ? 12.008 65.950 47.919 1.00 32.15 ? 45 LEU A CA 1 ATOM 358 C C . LEU B 2 45 ? 11.617 67.357 47.447 1.00 33.85 ? 45 LEU A C 1 ATOM 359 O O . LEU B 2 45 ? 11.976 67.767 46.343 1.00 35.54 ? 45 LEU A O 1 ATOM 360 C CB . LEU B 2 45 ? 13.248 66.004 48.824 1.00 29.80 ? 45 LEU A CB 1 ATOM 361 C CG . LEU B 2 45 ? 13.661 64.704 49.525 1.00 25.61 ? 45 LEU A CG 1 ATOM 362 C CD1 . LEU B 2 45 ? 14.990 64.888 50.227 1.00 24.20 ? 45 LEU A CD1 1 ATOM 363 C CD2 . LEU B 2 45 ? 12.597 64.306 50.525 1.00 25.64 ? 45 LEU A CD2 1 ATOM 364 N N . PRO B 2 46 ? 10.870 68.108 48.277 1.00 34.24 ? 46 PRO A N 1 ATOM 365 C CA . PRO B 2 46 ? 10.433 69.462 47.932 1.00 35.37 ? 46 PRO A CA 1 ATOM 366 C C . PRO B 2 46 ? 11.557 70.363 47.435 1.00 38.57 ? 46 PRO A C 1 ATOM 367 O O . PRO B 2 46 ? 12.719 70.179 47.805 1.00 40.32 ? 46 PRO A O 1 ATOM 368 C CB . PRO B 2 46 ? 9.834 69.967 49.238 1.00 33.39 ? 46 PRO A CB 1 ATOM 369 C CG . PRO B 2 46 ? 9.276 68.733 49.842 1.00 33.07 ? 46 PRO A CG 1 ATOM 370 C CD . PRO B 2 46 ? 10.405 67.748 49.629 1.00 34.17 ? 46 PRO A CD 1 ATOM 371 N N . ASN B 2 47 ? 11.206 71.327 46.585 1.00 41.00 ? 47 ASN A N 1 ATOM 372 C CA . ASN B 2 47 ? 12.172 72.285 46.060 1.00 43.35 ? 47 ASN A CA 1 ATOM 373 C C . ASN B 2 47 ? 12.322 73.325 47.163 1.00 44.73 ? 47 ASN A C 1 ATOM 374 O O . ASN B 2 47 ? 11.328 73.773 47.736 1.00 45.14 ? 47 ASN A O 1 ATOM 375 C CB . ASN B 2 47 ? 11.642 72.960 44.789 1.00 45.37 ? 47 ASN A CB 1 ATOM 376 C CG . ASN B 2 47 ? 12.722 73.754 44.044 1.00 48.60 ? 47 ASN A CG 1 ATOM 377 O OD1 . ASN B 2 47 ? 13.805 74.024 44.578 1.00 49.66 ? 47 ASN A OD1 1 ATOM 378 N ND2 . ASN B 2 47 ? 12.423 74.135 42.804 1.00 48.95 ? 47 ASN A ND2 1 ATOM 379 N N . ARG B 2 48 ? 13.555 73.707 47.468 1.00 46.02 ? 48 ARG A N 1 ATOM 380 C CA . ARG B 2 48 ? 13.784 74.682 48.522 1.00 47.52 ? 48 ARG A CA 1 ATOM 381 C C . ARG B 2 48 ? 13.152 76.021 48.179 1.00 47.04 ? 48 ARG A C 1 ATOM 382 O O . ARG B 2 48 ? 12.378 76.571 48.967 1.00 47.92 ? 48 ARG A O 1 ATOM 383 C CB . ARG B 2 48 ? 15.280 74.866 48.757 1.00 49.92 ? 48 ARG A CB 1 ATOM 384 C CG . ARG B 2 48 ? 15.617 75.361 50.154 1.00 54.54 ? 48 ARG A CG 1 ATOM 385 C CD . ARG B 2 48 ? 17.087 75.124 50.471 1.00 57.31 ? 48 ARG A CD 1 ATOM 386 N NE . ARG B 2 48 ? 17.940 75.901 49.585 1.00 60.56 ? 48 ARG A NE 1 ATOM 387 C CZ . ARG B 2 48 ? 18.109 77.216 49.677 1.00 62.05 ? 48 ARG A CZ 1 ATOM 388 N NH1 . ARG B 2 48 ? 17.484 77.912 50.628 1.00 60.27 ? 48 ARG A NH1 1 ATOM 389 N NH2 . ARG B 2 48 ? 18.902 77.836 48.809 1.00 62.88 ? 48 ARG A NH2 1 ATOM 390 N N . VAL B 2 49 ? 13.473 76.541 46.998 1.00 46.11 ? 49 VAL A N 1 ATOM 391 C CA . VAL B 2 49 ? 12.942 77.831 46.568 1.00 44.19 ? 49 VAL A CA 1 ATOM 392 C C . VAL B 2 49 ? 11.406 77.838 46.533 1.00 44.89 ? 49 VAL A C 1 ATOM 393 O O . VAL B 2 49 ? 10.776 77.084 45.787 1.00 44.89 ? 49 VAL A O 1 ATOM 394 C CB . VAL B 2 49 ? 13.522 78.239 45.169 1.00 42.07 ? 49 VAL A CB 1 ATOM 395 C CG1 . VAL B 2 49 ? 14.910 77.631 44.978 1.00 42.00 ? 49 VAL A CG1 1 ATOM 396 C CG2 . VAL B 2 49 ? 12.602 77.816 44.053 1.00 41.40 ? 49 VAL A CG2 1 ATOM 397 N N . GLY B 2 50 ? 10.803 78.678 47.370 1.00 44.36 ? 50 GLY A N 1 ATOM 398 C CA . GLY B 2 50 ? 9.355 78.769 47.390 1.00 44.34 ? 50 GLY A CA 1 ATOM 399 C C . GLY B 2 50 ? 8.657 77.854 48.375 1.00 45.03 ? 50 GLY A C 1 ATOM 400 O O . GLY B 2 50 ? 7.452 77.608 48.251 1.00 44.76 ? 50 GLY A O 1 ATOM 401 N N . LEU B 2 51 ? 9.400 77.347 49.356 1.00 43.97 ? 51 LEU A N 1 ATOM 402 C CA . LEU B 2 51 ? 8.812 76.462 50.354 1.00 43.66 ? 51 LEU A CA 1 ATOM 403 C C . LEU B 2 51 ? 8.590 77.192 51.682 1.00 43.73 ? 51 LEU A C 1 ATOM 404 O O . LEU B 2 51 ? 9.544 77.545 52.377 1.00 43.83 ? 51 LEU A O 1 ATOM 405 C CB . LEU B 2 51 ? 9.703 75.233 50.573 1.00 42.19 ? 51 LEU A CB 1 ATOM 406 C CG . LEU B 2 51 ? 9.074 74.118 51.416 1.00 41.96 ? 51 LEU A CG 1 ATOM 407 C CD1 . LEU B 2 51 ? 7.965 73.434 50.610 1.00 39.87 ? 51 LEU A CD1 1 ATOM 408 C CD2 . LEU B 2 51 ? 10.148 73.118 51.842 1.00 40.74 ? 51 LEU A CD2 1 ATOM 409 N N . PRO B 2 52 ? 7.317 77.438 52.038 1.00 44.23 ? 52 PRO A N 1 ATOM 410 C CA . PRO B 2 52 ? 6.868 78.118 53.264 1.00 44.08 ? 52 PRO A CA 1 ATOM 411 C C . PRO B 2 52 ? 7.466 77.491 54.524 1.00 43.45 ? 52 PRO A C 1 ATOM 412 O O . PRO B 2 52 ? 7.254 76.306 54.778 1.00 45.06 ? 52 PRO A O 1 ATOM 413 C CB . PRO B 2 52 ? 5.348 77.934 53.220 1.00 44.95 ? 52 PRO A CB 1 ATOM 414 C CG . PRO B 2 52 ? 5.059 77.925 51.752 1.00 45.69 ? 52 PRO A CG 1 ATOM 415 C CD . PRO B 2 52 ? 6.163 77.057 51.199 1.00 43.98 ? 52 PRO A CD 1 ATOM 416 N N . ILE B 2 53 ? 8.189 78.278 55.318 1.00 43.00 ? 53 ILE A N 1 ATOM 417 C CA . ILE B 2 53 ? 8.817 77.766 56.541 1.00 42.56 ? 53 ILE A CA 1 ATOM 418 C C . ILE B 2 53 ? 7.961 76.885 57.458 1.00 43.20 ? 53 ILE A C 1 ATOM 419 O O . ILE B 2 53 ? 8.478 76.344 58.434 1.00 42.78 ? 53 ILE A O 1 ATOM 420 C CB . ILE B 2 53 ? 9.401 78.909 57.410 1.00 41.59 ? 53 ILE A CB 1 ATOM 421 C CG1 . ILE B 2 53 ? 8.567 80.185 57.249 1.00 42.62 ? 53 ILE A CG1 1 ATOM 422 C CG2 . ILE B 2 53 ? 10.852 79.154 57.032 1.00 40.09 ? 53 ILE A CG2 1 ATOM 423 C CD1 . ILE B 2 53 ? 7.082 80.035 57.577 1.00 43.41 ? 53 ILE A CD1 1 ATOM 424 N N . ASN B 2 54 ? 6.670 76.737 57.158 1.00 44.08 ? 54 ASN A N 1 ATOM 425 C CA . ASN B 2 54 ? 5.788 75.901 57.980 1.00 45.47 ? 54 ASN A CA 1 ATOM 426 C C . ASN B 2 54 ? 5.741 74.436 57.533 1.00 44.77 ? 54 ASN A C 1 ATOM 427 O O . ASN B 2 54 ? 5.133 73.594 58.199 1.00 44.29 ? 54 ASN A O 1 ATOM 428 C CB . ASN B 2 54 ? 4.361 76.478 58.010 1.00 48.15 ? 54 ASN A CB 1 ATOM 429 C CG . ASN B 2 54 ? 4.024 77.288 56.767 1.00 51.76 ? 54 ASN A CG 1 ATOM 430 O OD1 . ASN B 2 54 ? 4.578 78.373 56.550 1.00 53.36 ? 54 ASN A OD1 1 ATOM 431 N ND2 . ASN B 2 54 ? 3.116 76.763 55.938 1.00 52.75 ? 54 ASN A ND2 1 ATOM 432 N N . GLN B 2 55 ? 6.393 74.144 56.411 1.00 44.72 ? 55 GLN A N 1 ATOM 433 C CA . GLN B 2 55 ? 6.450 72.795 55.854 1.00 44.31 ? 55 GLN A CA 1 ATOM 434 C C . GLN B 2 55 ? 7.902 72.528 55.488 1.00 42.75 ? 55 GLN A C 1 ATOM 435 O O . GLN B 2 55 ? 8.201 71.674 54.649 1.00 44.14 ? 55 GLN A O 1 ATOM 436 C CB . GLN B 2 55 ? 5.607 72.725 54.586 1.00 46.97 ? 55 GLN A CB 1 ATOM 437 C CG . GLN B 2 55 ? 4.282 73.454 54.695 1.00 50.71 ? 55 GLN A CG 1 ATOM 438 C CD . GLN B 2 55 ? 3.725 73.843 53.340 1.00 53.17 ? 55 GLN A CD 1 ATOM 439 O OE1 . GLN B 2 55 ? 4.376 74.561 52.575 1.00 54.72 ? 55 GLN A OE1 1 ATOM 440 N NE2 . GLN B 2 55 ? 2.517 73.374 53.033 1.00 52.96 ? 55 GLN A NE2 1 ATOM 441 N N . ARG B 2 56 ? 8.796 73.275 56.129 1.00 39.86 ? 56 ARG A N 1 ATOM 442 C CA . ARG B 2 56 ? 10.225 73.195 55.876 1.00 36.20 ? 56 ARG A CA 1 ATOM 443 C C . ARG B 2 56 ? 10.987 72.223 56.781 1.00 34.58 ? 56 ARG A C 1 ATOM 444 O O . ARG B 2 56 ? 12.116 71.843 56.476 1.00 35.74 ? 56 ARG A O 1 ATOM 445 C CB . ARG B 2 56 ? 10.820 74.603 56.003 1.00 34.38 ? 56 ARG A CB 1 ATOM 446 C CG . ARG B 2 56 ? 12.298 74.698 55.729 1.00 32.89 ? 56 ARG A CG 1 ATOM 447 C CD . ARG B 2 56 ? 12.614 74.297 54.310 1.00 32.93 ? 56 ARG A CD 1 ATOM 448 N NE . ARG B 2 56 ? 14.053 74.276 54.082 1.00 34.47 ? 56 ARG A NE 1 ATOM 449 C CZ . ARG B 2 56 ? 14.821 75.358 54.065 1.00 35.41 ? 56 ARG A CZ 1 ATOM 450 N NH1 . ARG B 2 56 ? 14.283 76.553 54.259 1.00 37.71 ? 56 ARG A NH1 1 ATOM 451 N NH2 . ARG B 2 56 ? 16.127 75.247 53.862 1.00 35.58 ? 56 ARG A NH2 1 ATOM 452 N N . PHE B 2 57 ? 10.382 71.812 57.887 1.00 32.30 ? 57 PHE A N 1 ATOM 453 C CA . PHE B 2 57 ? 11.051 70.905 58.813 1.00 30.29 ? 57 PHE A CA 1 ATOM 454 C C . PHE B 2 57 ? 10.069 69.899 59.381 1.00 29.65 ? 57 PHE A C 1 ATOM 455 O O . PHE B 2 57 ? 8.858 70.116 59.375 1.00 30.66 ? 57 PHE A O 1 ATOM 456 C CB . PHE B 2 57 ? 11.639 71.673 60.013 1.00 31.36 ? 57 PHE A CB 1 ATOM 457 C CG . PHE B 2 57 ? 12.670 72.721 59.658 1.00 34.20 ? 57 PHE A CG 1 ATOM 458 C CD1 . PHE B 2 57 ? 13.952 72.358 59.246 1.00 36.43 ? 57 PHE A CD1 1 ATOM 459 C CD2 . PHE B 2 57 ? 12.370 74.077 59.776 1.00 34.90 ? 57 PHE A CD2 1 ATOM 460 C CE1 . PHE B 2 57 ? 14.920 73.337 58.960 1.00 35.85 ? 57 PHE A CE1 1 ATOM 461 C CE2 . PHE B 2 57 ? 13.328 75.057 59.491 1.00 35.53 ? 57 PHE A CE2 1 ATOM 462 C CZ . PHE B 2 57 ? 14.604 74.685 59.084 1.00 34.88 ? 57 PHE A CZ 1 ATOM 463 N N . ILE B 2 58 ? 10.607 68.791 59.868 1.00 28.77 ? 58 ILE A N 1 ATOM 464 C CA . ILE B 2 58 ? 9.808 67.775 60.528 1.00 28.65 ? 58 ILE A CA 1 ATOM 465 C C . ILE B 2 58 ? 10.619 67.521 61.783 1.00 29.69 ? 58 ILE A C 1 ATOM 466 O O . ILE B 2 58 ? 11.814 67.790 61.818 1.00 29.60 ? 58 ILE A O 1 ATOM 467 C CB . ILE B 2 58 ? 9.657 66.461 59.708 1.00 28.54 ? 58 ILE A CB 1 ATOM 468 C CG1 . ILE B 2 58 ? 11.010 65.775 59.518 1.00 29.28 ? 58 ILE A CG1 1 ATOM 469 C CG2 . ILE B 2 58 ? 9.015 66.762 58.373 1.00 28.95 ? 58 ILE A CG2 1 ATOM 470 C CD1 . ILE B 2 58 ? 10.901 64.371 58.938 1.00 29.00 ? 58 ILE A CD1 1 ATOM 471 N N . LEU B 2 59 ? 9.982 67.026 62.826 1.00 31.98 ? 59 LEU A N 1 ATOM 472 C CA . LEU B 2 59 ? 10.705 66.788 64.059 1.00 33.47 ? 59 LEU A CA 1 ATOM 473 C C . LEU B 2 59 ? 10.688 65.324 64.464 1.00 34.42 ? 59 LEU A C 1 ATOM 474 O O . LEU B 2 59 ? 9.624 64.727 64.610 1.00 36.09 ? 59 LEU A O 1 ATOM 475 C CB . LEU B 2 59 ? 10.110 67.656 65.184 1.00 33.24 ? 59 LEU A CB 1 ATOM 476 C CG . LEU B 2 59 ? 10.705 69.047 65.459 1.00 31.70 ? 59 LEU A CG 1 ATOM 477 C CD1 . LEU B 2 59 ? 11.010 69.794 64.177 1.00 30.28 ? 59 LEU A CD1 1 ATOM 478 C CD2 . LEU B 2 59 ? 9.729 69.822 66.300 1.00 30.24 ? 59 LEU A CD2 1 ATOM 479 N N . VAL B 2 60 ? 11.871 64.746 64.633 1.00 35.03 ? 60 VAL A N 1 ATOM 480 C CA . VAL B 2 60 ? 11.982 63.355 65.059 1.00 34.71 ? 60 VAL A CA 1 ATOM 481 C C . VAL B 2 60 ? 12.362 63.326 66.544 1.00 35.63 ? 60 VAL A C 1 ATOM 482 O O . VAL B 2 60 ? 13.353 63.931 66.950 1.00 36.43 ? 60 VAL A O 1 ATOM 483 C CB . VAL B 2 60 ? 13.049 62.606 64.238 1.00 33.11 ? 60 VAL A CB 1 ATOM 484 C CG1 . VAL B 2 60 ? 13.245 61.211 64.787 1.00 31.73 ? 60 VAL A CG1 1 ATOM 485 C CG2 . VAL B 2 60 ? 12.626 62.539 62.788 1.00 31.43 ? 60 VAL A CG2 1 ATOM 486 N N . GLU B 2 61 ? 11.557 62.649 67.356 1.00 36.22 ? 61 GLU A N 1 ATOM 487 C CA . GLU B 2 61 ? 11.838 62.551 68.782 1.00 37.43 ? 61 GLU A CA 1 ATOM 488 C C . GLU B 2 61 ? 12.306 61.150 69.147 1.00 36.35 ? 61 GLU A C 1 ATOM 489 O O . GLU B 2 61 ? 11.614 60.165 68.898 1.00 36.67 ? 61 GLU A O 1 ATOM 490 C CB . GLU B 2 61 ? 10.605 62.905 69.610 1.00 40.46 ? 61 GLU A CB 1 ATOM 491 C CG . GLU B 2 61 ? 10.694 62.409 71.049 1.00 47.15 ? 61 GLU A CG 1 ATOM 492 C CD . GLU B 2 61 ? 9.528 62.854 71.913 1.00 51.67 ? 61 GLU A CD 1 ATOM 493 O OE1 . GLU B 2 61 ? 8.360 62.645 71.508 1.00 55.13 ? 61 GLU A OE1 1 ATOM 494 O OE2 . GLU B 2 61 ? 9.780 63.405 73.008 1.00 53.05 ? 61 GLU A OE2 1 ATOM 495 N N . LEU B 2 62 ? 13.484 61.074 69.752 1.00 34.70 ? 62 LEU A N 1 ATOM 496 C CA . LEU B 2 62 ? 14.063 59.804 70.143 1.00 33.18 ? 62 LEU A CA 1 ATOM 497 C C . LEU B 2 62 ? 14.143 59.708 71.660 1.00 32.57 ? 62 LEU A C 1 ATOM 498 O O . LEU B 2 62 ? 14.437 60.689 72.328 1.00 30.60 ? 62 LEU A O 1 ATOM 499 C CB . LEU B 2 62 ? 15.463 59.691 69.546 1.00 34.13 ? 62 LEU A CB 1 ATOM 500 C CG . LEU B 2 62 ? 15.584 60.093 68.074 1.00 33.65 ? 62 LEU A CG 1 ATOM 501 C CD1 . LEU B 2 62 ? 17.053 60.152 67.699 1.00 34.96 ? 62 LEU A CD1 1 ATOM 502 C CD2 . LEU B 2 62 ? 14.827 59.106 67.185 1.00 34.28 ? 62 LEU A CD2 1 ATOM 503 N N . SER B 2 63 ? 13.884 58.520 72.193 1.00 33.94 ? 63 SER A N 1 ATOM 504 C CA . SER B 2 63 ? 13.934 58.286 73.633 1.00 36.36 ? 63 SER A CA 1 ATOM 505 C C . SER B 2 63 ? 14.440 56.874 73.891 1.00 38.16 ? 63 SER A C 1 ATOM 506 O O . SER B 2 63 ? 14.067 55.942 73.185 1.00 37.76 ? 63 SER A O 1 ATOM 507 C CB . SER B 2 63 ? 12.546 58.461 74.244 1.00 35.08 ? 63 SER A CB 1 ATOM 508 O OG . SER B 2 63 ? 11.575 57.768 73.478 1.00 37.78 ? 63 SER A OG 1 ATOM 509 N N . ASN B 2 64 ? 15.287 56.709 74.898 1.00 41.03 ? 64 ASN A N 1 ATOM 510 C CA . ASN B 2 64 ? 15.829 55.391 75.185 1.00 45.24 ? 64 ASN A CA 1 ATOM 511 C C . ASN B 2 64 ? 15.353 54.806 76.501 1.00 48.57 ? 64 ASN A C 1 ATOM 512 O O . ASN B 2 64 ? 14.442 55.338 77.140 1.00 48.09 ? 64 ASN A O 1 ATOM 513 C CB . ASN B 2 64 ? 17.359 55.440 75.170 1.00 46.06 ? 64 ASN A CB 1 ATOM 514 C CG . ASN B 2 64 ? 17.918 56.469 76.131 1.00 47.08 ? 64 ASN A CG 1 ATOM 515 O OD1 . ASN B 2 64 ? 17.714 56.381 77.341 1.00 47.88 ? 64 ASN A OD1 1 ATOM 516 N ND2 . ASN B 2 64 ? 18.629 57.455 75.596 1.00 47.28 ? 64 ASN A ND2 1 ATOM 517 N N . HIS B 2 65 ? 15.995 53.702 76.885 1.00 53.04 ? 65 HIS A N 1 ATOM 518 C CA . HIS B 2 65 ? 15.697 52.965 78.113 1.00 56.65 ? 65 HIS A CA 1 ATOM 519 C C . HIS B 2 65 ? 15.790 53.839 79.357 1.00 56.97 ? 65 HIS A C 1 ATOM 520 O O . HIS B 2 65 ? 14.957 53.726 80.260 1.00 57.35 ? 65 HIS A O 1 ATOM 521 C CB . HIS B 2 65 ? 16.663 51.781 78.255 1.00 60.14 ? 65 HIS A CB 1 ATOM 522 C CG . HIS B 2 65 ? 16.266 50.790 79.308 1.00 64.08 ? 65 HIS A CG 1 ATOM 523 N ND1 . HIS B 2 65 ? 15.000 50.243 79.378 1.00 65.65 ? 65 HIS A ND1 1 ATOM 524 C CD2 . HIS B 2 65 ? 16.981 50.205 80.300 1.00 65.81 ? 65 HIS A CD2 1 ATOM 525 C CE1 . HIS B 2 65 ? 14.953 49.365 80.364 1.00 66.21 ? 65 HIS A CE1 1 ATOM 526 N NE2 . HIS B 2 65 ? 16.143 49.322 80.940 1.00 67.55 ? 65 HIS A NE2 1 ATOM 527 N N . ALA B 2 66 ? 16.804 54.705 79.397 1.00 57.34 ? 66 ALA A N 1 ATOM 528 C CA . ALA B 2 66 ? 17.034 55.602 80.534 1.00 56.62 ? 66 ALA A CA 1 ATOM 529 C C . ALA B 2 66 ? 15.994 56.718 80.685 1.00 56.16 ? 66 ALA A C 1 ATOM 530 O O . ALA B 2 66 ? 16.147 57.596 81.538 1.00 56.11 ? 66 ALA A O 1 ATOM 531 C CB . ALA B 2 66 ? 18.438 56.211 80.436 1.00 55.85 ? 66 ALA A CB 1 ATOM 532 N N . GLU B 2 67 ? 14.946 56.686 79.862 1.00 55.98 ? 67 GLU A N 1 ATOM 533 C CA . GLU B 2 67 ? 13.891 57.697 79.917 1.00 55.22 ? 67 GLU A CA 1 ATOM 534 C C . GLU B 2 67 ? 14.306 59.072 79.400 1.00 53.34 ? 67 GLU A C 1 ATOM 535 O O . GLU B 2 67 ? 13.509 60.020 79.421 1.00 52.84 ? 67 GLU A O 1 ATOM 536 C CB . GLU B 2 67 ? 13.360 57.824 81.346 1.00 58.27 ? 67 GLU A CB 1 ATOM 537 C CG . GLU B 2 67 ? 12.592 56.604 81.773 1.00 62.04 ? 67 GLU A CG 1 ATOM 538 C CD . GLU B 2 67 ? 11.587 56.202 80.711 1.00 65.32 ? 67 GLU A CD 1 ATOM 539 O OE1 . GLU B 2 67 ? 10.690 57.023 80.415 1.00 66.65 ? 67 GLU A OE1 1 ATOM 540 O OE2 . GLU B 2 67 ? 11.703 55.081 80.165 1.00 66.16 ? 67 GLU A OE2 1 ATOM 541 N N . LEU B 2 68 ? 15.552 59.171 78.943 1.00 50.20 ? 68 LEU A N 1 ATOM 542 C CA . LEU B 2 68 ? 16.086 60.414 78.408 1.00 46.76 ? 68 LEU A CA 1 ATOM 543 C C . LEU B 2 68 ? 15.462 60.624 77.036 1.00 44.85 ? 68 LEU A C 1 ATOM 544 O O . LEU B 2 68 ? 15.224 59.661 76.307 1.00 45.38 ? 68 LEU A O 1 ATOM 545 C CB . LEU B 2 68 ? 17.606 60.318 78.280 1.00 46.52 ? 68 LEU A CB 1 ATOM 546 C CG . LEU B 2 68 ? 18.355 59.993 79.570 1.00 46.55 ? 68 LEU A CG 1 ATOM 547 C CD1 . LEU B 2 68 ? 19.807 59.700 79.261 1.00 46.37 ? 68 LEU A CD1 1 ATOM 548 C CD2 . LEU B 2 68 ? 18.228 61.148 80.546 1.00 46.02 ? 68 LEU A CD2 1 ATOM 549 N N . SER B 2 69 ? 15.199 61.878 76.687 1.00 41.51 ? 69 SER A N 1 ATOM 550 C CA . SER B 2 69 ? 14.598 62.189 75.401 1.00 38.49 ? 69 SER A CA 1 ATOM 551 C C . SER B 2 69 ? 15.320 63.342 74.696 1.00 36.17 ? 69 SER A C 1 ATOM 552 O O . SER B 2 69 ? 15.871 64.226 75.340 1.00 35.92 ? 69 SER A O 1 ATOM 553 C CB . SER B 2 69 ? 13.118 62.525 75.594 1.00 38.60 ? 69 SER A CB 1 ATOM 554 O OG . SER B 2 69 ? 12.494 62.831 74.363 1.00 40.96 ? 69 SER A OG 1 ATOM 555 N N . VAL B 2 70 ? 15.313 63.312 73.366 1.00 33.42 ? 70 VAL A N 1 ATOM 556 C CA . VAL B 2 70 ? 15.959 64.323 72.530 1.00 30.35 ? 70 VAL A CA 1 ATOM 557 C C . VAL B 2 70 ? 15.132 64.512 71.253 1.00 30.22 ? 70 VAL A C 1 ATOM 558 O O . VAL B 2 70 ? 14.554 63.554 70.747 1.00 30.68 ? 70 VAL A O 1 ATOM 559 C CB . VAL B 2 70 ? 17.376 63.863 72.143 1.00 28.92 ? 70 VAL A CB 1 ATOM 560 C CG1 . VAL B 2 70 ? 17.930 64.746 71.062 1.00 28.71 ? 70 VAL A CG1 1 ATOM 561 C CG2 . VAL B 2 70 ? 18.277 63.898 73.352 1.00 28.33 ? 70 VAL A CG2 1 ATOM 562 N N . THR B 2 71 ? 15.060 65.730 70.724 1.00 29.75 ? 71 THR A N 1 ATOM 563 C CA . THR B 2 71 ? 14.281 65.947 69.499 1.00 28.63 ? 71 THR A CA 1 ATOM 564 C C . THR B 2 71 ? 15.100 66.515 68.338 1.00 29.65 ? 71 THR A C 1 ATOM 565 O O . THR B 2 71 ? 15.569 67.648 68.396 1.00 30.97 ? 71 THR A O 1 ATOM 566 C CB . THR B 2 71 ? 13.061 66.878 69.752 1.00 26.86 ? 71 THR A CB 1 ATOM 567 O OG1 . THR B 2 71 ? 12.106 66.200 70.580 1.00 25.38 ? 71 THR A OG1 1 ATOM 568 C CG2 . THR B 2 71 ? 12.385 67.251 68.430 1.00 23.60 ? 71 THR A CG2 1 ATOM 569 N N . LEU B 2 72 ? 15.257 65.725 67.280 1.00 29.46 ? 72 LEU A N 1 ATOM 570 C CA . LEU B 2 72 ? 16.013 66.158 66.110 1.00 29.54 ? 72 LEU A CA 1 ATOM 571 C C . LEU B 2 72 ? 15.115 66.889 65.124 1.00 29.72 ? 72 LEU A C 1 ATOM 572 O O . LEU B 2 72 ? 13.951 66.533 64.954 1.00 30.36 ? 72 LEU A O 1 ATOM 573 C CB . LEU B 2 72 ? 16.639 64.956 65.407 1.00 29.74 ? 72 LEU A CB 1 ATOM 574 C CG . LEU B 2 72 ? 17.526 64.056 66.263 1.00 30.01 ? 72 LEU A CG 1 ATOM 575 C CD1 . LEU B 2 72 ? 17.915 62.843 65.446 1.00 30.26 ? 72 LEU A CD1 1 ATOM 576 C CD2 . LEU B 2 72 ? 18.756 64.817 66.738 1.00 29.41 ? 72 LEU A CD2 1 ATOM 577 N N . ALA B 2 73 ? 15.666 67.911 64.475 1.00 28.55 ? 73 ALA A N 1 ATOM 578 C CA . ALA B 2 73 ? 14.938 68.699 63.487 1.00 26.50 ? 73 ALA A CA 1 ATOM 579 C C . ALA B 2 73 ? 15.573 68.436 62.130 1.00 26.17 ? 73 ALA A C 1 ATOM 580 O O . ALA B 2 73 ? 16.727 68.794 61.916 1.00 26.30 ? 73 ALA A O 1 ATOM 581 C CB . ALA B 2 73 ? 15.034 70.184 63.831 1.00 25.10 ? 73 ALA A CB 1 ATOM 582 N N . LEU B 2 74 ? 14.832 67.796 61.226 1.00 25.85 ? 74 LEU A N 1 ATOM 583 C CA . LEU B 2 74 ? 15.344 67.491 59.883 1.00 25.96 ? 74 LEU A CA 1 ATOM 584 C C . LEU B 2 74 ? 14.780 68.447 58.840 1.00 26.33 ? 74 LEU A C 1 ATOM 585 O O . LEU B 2 74 ? 13.603 68.774 58.869 1.00 27.36 ? 74 LEU A O 1 ATOM 586 C CB . LEU B 2 74 ? 15.000 66.047 59.472 1.00 25.39 ? 74 LEU A CB 1 ATOM 587 C CG . LEU B 2 74 ? 15.668 64.855 60.182 1.00 24.59 ? 74 LEU A CG 1 ATOM 588 C CD1 . LEU B 2 74 ? 14.995 64.622 61.509 1.00 24.31 ? 74 LEU A CD1 1 ATOM 589 C CD2 . LEU B 2 74 ? 15.542 63.600 59.338 1.00 22.17 ? 74 LEU A CD2 1 ATOM 590 N N . ASP B 2 75 ? 15.630 68.899 57.925 1.00 26.69 ? 75 ASP A N 1 ATOM 591 C CA . ASP B 2 75 ? 15.215 69.806 56.859 1.00 27.54 ? 75 ASP A CA 1 ATOM 592 C C . ASP B 2 75 ? 14.570 68.944 55.777 1.00 28.60 ? 75 ASP A C 1 ATOM 593 O O . ASP B 2 75 ? 15.183 68.004 55.265 1.00 29.77 ? 75 ASP A O 1 ATOM 594 C CB . ASP B 2 75 ? 16.434 70.540 56.287 1.00 28.27 ? 75 ASP A CB 1 ATOM 595 C CG . ASP B 2 75 ? 16.064 71.543 55.207 1.00 29.64 ? 75 ASP A CG 1 ATOM 596 O OD1 . ASP B 2 75 ? 15.305 71.179 54.290 1.00 30.55 ? 75 ASP A OD1 1 ATOM 597 O OD2 . ASP B 2 75 ? 16.541 72.695 55.260 1.00 29.92 ? 75 ASP A OD2 1 ATOM 598 N N . VAL B 2 76 ? 13.335 69.273 55.428 1.00 28.22 ? 76 VAL A N 1 ATOM 599 C CA . VAL B 2 76 ? 12.584 68.519 54.435 1.00 27.70 ? 76 VAL A CA 1 ATOM 600 C C . VAL B 2 76 ? 13.148 68.532 53.005 1.00 29.41 ? 76 VAL A C 1 ATOM 601 O O . VAL B 2 76 ? 12.869 67.618 52.227 1.00 29.71 ? 76 VAL A O 1 ATOM 602 C CB . VAL B 2 76 ? 11.106 68.991 54.447 1.00 26.81 ? 76 VAL A CB 1 ATOM 603 C CG1 . VAL B 2 76 ? 10.364 68.481 53.251 1.00 28.52 ? 76 VAL A CG1 1 ATOM 604 C CG2 . VAL B 2 76 ? 10.433 68.491 55.711 1.00 25.73 ? 76 VAL A CG2 1 ATOM 605 N N . THR B 2 77 ? 13.953 69.537 52.655 1.00 29.62 ? 77 THR A N 1 ATOM 606 C CA . THR B 2 77 ? 14.516 69.607 51.300 1.00 30.27 ? 77 THR A CA 1 ATOM 607 C C . THR B 2 77 ? 15.704 68.677 51.023 1.00 31.12 ? 77 THR A C 1 ATOM 608 O O . THR B 2 77 ? 16.036 68.433 49.863 1.00 31.70 ? 77 THR A O 1 ATOM 609 C CB . THR B 2 77 ? 14.955 71.050 50.909 1.00 29.64 ? 77 THR A CB 1 ATOM 610 O OG1 . THR B 2 77 ? 15.954 71.518 51.822 1.00 28.43 ? 77 THR A OG1 1 ATOM 611 C CG2 . THR B 2 77 ? 13.764 71.999 50.899 1.00 27.75 ? 77 THR A CG2 1 ATOM 612 N N . ASN B 2 78 ? 16.346 68.165 52.070 1.00 31.39 ? 78 ASN A N 1 ATOM 613 C CA . ASN B 2 78 ? 17.488 67.263 51.897 1.00 30.90 ? 78 ASN A CA 1 ATOM 614 C C . ASN B 2 78 ? 17.625 66.186 52.972 1.00 31.12 ? 78 ASN A C 1 ATOM 615 O O . ASN B 2 78 ? 18.605 65.439 52.968 1.00 32.82 ? 78 ASN A O 1 ATOM 616 C CB . ASN B 2 78 ? 18.796 68.058 51.824 1.00 28.63 ? 78 ASN A CB 1 ATOM 617 C CG . ASN B 2 78 ? 18.918 69.099 52.926 1.00 27.76 ? 78 ASN A CG 1 ATOM 618 O OD1 . ASN B 2 78 ? 18.322 68.965 53.997 1.00 26.85 ? 78 ASN A OD1 1 ATOM 619 N ND2 . ASN B 2 78 ? 19.707 70.139 52.670 1.00 26.48 ? 78 ASN A ND2 1 ATOM 620 N N . ALA B 2 79 ? 16.647 66.111 53.879 1.00 30.61 ? 79 ALA A N 1 ATOM 621 C CA . ALA B 2 79 ? 16.632 65.131 54.973 1.00 30.34 ? 79 ALA A CA 1 ATOM 622 C C . ALA B 2 79 ? 17.853 65.310 55.864 1.00 30.98 ? 79 ALA A C 1 ATOM 623 O O . ALA B 2 79 ? 18.314 64.374 56.514 1.00 30.21 ? 79 ALA A O 1 ATOM 624 C CB . ALA B 2 79 ? 16.588 63.710 54.412 1.00 29.51 ? 79 ALA A CB 1 ATOM 625 N N . TYR B 2 80 ? 18.353 66.540 55.878 1.00 32.43 ? 80 TYR A N 1 ATOM 626 C CA . TYR B 2 80 ? 19.522 66.955 56.649 1.00 34.26 ? 80 TYR A CA 1 ATOM 627 C C . TYR B 2 80 ? 19.148 67.225 58.111 1.00 31.73 ? 80 TYR A C 1 ATOM 628 O O . TYR B 2 80 ? 18.188 67.942 58.380 1.00 31.68 ? 80 TYR A O 1 ATOM 629 C CB . TYR B 2 80 ? 20.056 68.260 56.045 1.00 40.78 ? 80 TYR A CB 1 ATOM 630 C CG . TYR B 2 80 ? 21.560 68.403 55.923 1.00 46.98 ? 80 TYR A CG 1 ATOM 631 C CD1 . TYR B 2 80 ? 22.242 67.909 54.802 1.00 48.41 ? 80 TYR A CD1 1 ATOM 632 C CD2 . TYR B 2 80 ? 22.294 69.087 56.900 1.00 50.12 ? 80 TYR A CD2 1 ATOM 633 C CE1 . TYR B 2 80 ? 23.614 68.097 54.651 1.00 51.01 ? 80 TYR A CE1 1 ATOM 634 C CE2 . TYR B 2 80 ? 23.674 69.281 56.763 1.00 52.94 ? 80 TYR A CE2 1 ATOM 635 C CZ . TYR B 2 80 ? 24.328 68.783 55.635 1.00 53.57 ? 80 TYR A CZ 1 ATOM 636 O OH . TYR B 2 80 ? 25.694 68.961 55.494 1.00 55.40 ? 80 TYR A OH 1 ATOM 637 N N . VAL B 2 81 ? 19.894 66.660 59.055 1.00 28.63 ? 81 VAL A N 1 ATOM 638 C CA . VAL B 2 81 ? 19.628 66.927 60.470 1.00 25.76 ? 81 VAL A CA 1 ATOM 639 C C . VAL B 2 81 ? 20.276 68.298 60.718 1.00 27.49 ? 81 VAL A C 1 ATOM 640 O O . VAL B 2 81 ? 21.503 68.425 60.655 1.00 28.62 ? 81 VAL A O 1 ATOM 641 C CB . VAL B 2 81 ? 20.293 65.879 61.401 1.00 21.60 ? 81 VAL A CB 1 ATOM 642 C CG1 . VAL B 2 81 ? 20.155 66.311 62.838 1.00 20.49 ? 81 VAL A CG1 1 ATOM 643 C CG2 . VAL B 2 81 ? 19.662 64.520 61.206 1.00 16.73 ? 81 VAL A CG2 1 ATOM 644 N N . VAL B 2 82 ? 19.466 69.322 60.986 1.00 27.34 ? 82 VAL A N 1 ATOM 645 C CA . VAL B 2 82 ? 19.996 70.671 61.187 1.00 26.41 ? 82 VAL A CA 1 ATOM 646 C C . VAL B 2 82 ? 20.209 71.108 62.624 1.00 25.75 ? 82 VAL A C 1 ATOM 647 O O . VAL B 2 82 ? 20.892 72.099 62.877 1.00 26.62 ? 82 VAL A O 1 ATOM 648 C CB . VAL B 2 82 ? 19.101 71.717 60.515 1.00 27.49 ? 82 VAL A CB 1 ATOM 649 C CG1 . VAL B 2 82 ? 18.898 71.345 59.061 1.00 29.89 ? 82 VAL A CG1 1 ATOM 650 C CG2 . VAL B 2 82 ? 17.760 71.817 61.241 1.00 28.27 ? 82 VAL A CG2 1 ATOM 651 N N . GLY B 2 83 ? 19.623 70.382 63.564 1.00 24.60 ? 83 GLY A N 1 ATOM 652 C CA . GLY B 2 83 ? 19.785 70.743 64.954 1.00 24.42 ? 83 GLY A CA 1 ATOM 653 C C . GLY B 2 83 ? 19.009 69.815 65.852 1.00 25.83 ? 83 GLY A C 1 ATOM 654 O O . GLY B 2 83 ? 18.545 68.763 65.424 1.00 25.61 ? 83 GLY A O 1 ATOM 655 N N . TYR B 2 84 ? 18.885 70.194 67.114 1.00 27.49 ? 84 TYR A N 1 ATOM 656 C CA . TYR B 2 84 ? 18.131 69.383 68.045 1.00 30.50 ? 84 TYR A CA 1 ATOM 657 C C . TYR B 2 84 ? 17.846 70.115 69.347 1.00 32.51 ? 84 TYR A C 1 ATOM 658 O O . TYR B 2 84 ? 18.462 71.125 69.669 1.00 32.34 ? 84 TYR A O 1 ATOM 659 C CB . TYR B 2 84 ? 18.859 68.061 68.328 1.00 30.82 ? 84 TYR A CB 1 ATOM 660 C CG . TYR B 2 84 ? 19.935 68.117 69.390 1.00 31.95 ? 84 TYR A CG 1 ATOM 661 C CD1 . TYR B 2 84 ? 21.142 68.770 69.158 1.00 32.69 ? 84 TYR A CD1 1 ATOM 662 C CD2 . TYR B 2 84 ? 19.748 67.502 70.626 1.00 31.90 ? 84 TYR A CD2 1 ATOM 663 C CE1 . TYR B 2 84 ? 22.137 68.806 70.134 1.00 33.68 ? 84 TYR A CE1 1 ATOM 664 C CE2 . TYR B 2 84 ? 20.733 67.532 71.605 1.00 32.80 ? 84 TYR A CE2 1 ATOM 665 C CZ . TYR B 2 84 ? 21.921 68.183 71.354 1.00 33.77 ? 84 TYR A CZ 1 ATOM 666 O OH . TYR B 2 84 ? 22.890 68.210 72.328 1.00 36.14 ? 84 TYR A OH 1 ATOM 667 N N . ARG B 2 85 ? 16.880 69.592 70.082 1.00 35.59 ? 85 ARG A N 1 ATOM 668 C CA . ARG B 2 85 ? 16.493 70.155 71.356 1.00 38.37 ? 85 ARG A CA 1 ATOM 669 C C . ARG B 2 85 ? 16.686 69.077 72.416 1.00 39.11 ? 85 ARG A C 1 ATOM 670 O O . ARG B 2 85 ? 16.473 67.887 72.157 1.00 38.95 ? 85 ARG A O 1 ATOM 671 C CB . ARG B 2 85 ? 15.027 70.597 71.306 1.00 41.00 ? 85 ARG A CB 1 ATOM 672 C CG . ARG B 2 85 ? 14.436 70.951 72.654 1.00 44.75 ? 85 ARG A CG 1 ATOM 673 C CD . ARG B 2 85 ? 13.035 71.526 72.519 1.00 49.47 ? 85 ARG A CD 1 ATOM 674 N NE . ARG B 2 85 ? 12.521 72.001 73.803 1.00 54.84 ? 85 ARG A NE 1 ATOM 675 C CZ . ARG B 2 85 ? 11.486 72.830 73.944 1.00 57.47 ? 85 ARG A CZ 1 ATOM 676 N NH1 . ARG B 2 85 ? 10.841 73.287 72.871 1.00 58.23 ? 85 ARG A NH1 1 ATOM 677 N NH2 . ARG B 2 85 ? 11.099 73.212 75.161 1.00 57.47 ? 85 ARG A NH2 1 ATOM 678 N N . ALA B 2 86 ? 17.117 69.496 73.597 1.00 38.99 ? 86 ALA A N 1 ATOM 679 C CA . ALA B 2 86 ? 17.319 68.583 74.706 1.00 40.91 ? 86 ALA A CA 1 ATOM 680 C C . ALA B 2 86 ? 16.918 69.378 75.927 1.00 42.41 ? 86 ALA A C 1 ATOM 681 O O . ALA B 2 86 ? 17.633 70.296 76.324 1.00 45.10 ? 86 ALA A O 1 ATOM 682 C CB . ALA B 2 86 ? 18.780 68.168 74.801 1.00 40.19 ? 86 ALA A CB 1 ATOM 683 N N . GLY B 2 87 ? 15.767 69.044 76.508 1.00 43.16 ? 87 GLY A N 1 ATOM 684 C CA . GLY B 2 87 ? 15.301 69.762 77.680 1.00 43.99 ? 87 GLY A CA 1 ATOM 685 C C . GLY B 2 87 ? 14.819 71.166 77.352 1.00 45.32 ? 87 GLY A C 1 ATOM 686 O O . GLY B 2 87 ? 13.868 71.340 76.596 1.00 46.53 ? 87 GLY A O 1 ATOM 687 N N . ASN B 2 88 ? 15.485 72.171 77.911 1.00 46.88 ? 88 ASN A N 1 ATOM 688 C CA . ASN B 2 88 ? 15.121 73.571 77.700 1.00 48.85 ? 88 ASN A CA 1 ATOM 689 C C . ASN B 2 88 ? 16.068 74.263 76.711 1.00 48.10 ? 88 ASN A C 1 ATOM 690 O O . ASN B 2 88 ? 15.951 75.471 76.475 1.00 48.93 ? 88 ASN A O 1 ATOM 691 C CB . ASN B 2 88 ? 15.195 74.315 79.028 1.00 52.54 ? 88 ASN A CB 1 ATOM 692 C CG . ASN B 2 88 ? 16.637 74.483 79.509 1.00 57.58 ? 88 ASN A CG 1 ATOM 693 O OD1 . ASN B 2 88 ? 17.437 73.537 79.449 1.00 59.50 ? 88 ASN A OD1 1 ATOM 694 N ND2 . ASN B 2 88 ? 16.978 75.684 79.984 1.00 59.76 ? 88 ASN A ND2 1 ATOM 695 N N . SER B 2 89 ? 17.009 73.505 76.149 1.00 46.57 ? 89 SER A N 1 ATOM 696 C CA . SER B 2 89 ? 17.983 74.056 75.209 1.00 44.18 ? 89 SER A CA 1 ATOM 697 C C . SER B 2 89 ? 17.879 73.479 73.807 1.00 43.10 ? 89 SER A C 1 ATOM 698 O O . SER B 2 89 ? 17.336 72.391 73.606 1.00 43.95 ? 89 SER A O 1 ATOM 699 C CB . SER B 2 89 ? 19.395 73.811 75.724 1.00 44.23 ? 89 SER A CB 1 ATOM 700 O OG . SER B 2 89 ? 19.516 74.257 77.056 1.00 45.86 ? 89 SER A OG 1 ATOM 701 N N . ALA B 2 90 ? 18.424 74.215 72.844 1.00 40.60 ? 90 ALA A N 1 ATOM 702 C CA . ALA B 2 90 ? 18.430 73.803 71.447 1.00 38.17 ? 90 ALA A CA 1 ATOM 703 C C . ALA B 2 90 ? 19.804 74.112 70.862 1.00 36.88 ? 90 ALA A C 1 ATOM 704 O O . ALA B 2 90 ? 20.371 75.160 71.137 1.00 37.27 ? 90 ALA A O 1 ATOM 705 C CB . ALA B 2 90 ? 17.346 74.551 70.676 1.00 37.55 ? 90 ALA A CB 1 ATOM 706 N N . TYR B 2 91 ? 20.342 73.196 70.066 1.00 35.29 ? 91 TYR A N 1 ATOM 707 C CA . TYR B 2 91 ? 21.647 73.393 69.445 1.00 33.43 ? 91 TYR A CA 1 ATOM 708 C C . TYR B 2 91 ? 21.523 73.216 67.933 1.00 32.86 ? 91 TYR A C 1 ATOM 709 O O . TYR B 2 91 ? 20.885 72.274 67.472 1.00 33.52 ? 91 TYR A O 1 ATOM 710 C CB . TYR B 2 91 ? 22.655 72.395 70.014 1.00 31.61 ? 91 TYR A CB 1 ATOM 711 C CG . TYR B 2 91 ? 22.804 72.481 71.511 1.00 31.33 ? 91 TYR A CG 1 ATOM 712 C CD1 . TYR B 2 91 ? 21.860 71.914 72.357 1.00 31.90 ? 91 TYR A CD1 1 ATOM 713 C CD2 . TYR B 2 91 ? 23.870 73.174 72.079 1.00 31.47 ? 91 TYR A CD2 1 ATOM 714 C CE1 . TYR B 2 91 ? 21.969 72.038 73.742 1.00 34.90 ? 91 TYR A CE1 1 ATOM 715 C CE2 . TYR B 2 91 ? 23.995 73.308 73.457 1.00 32.92 ? 91 TYR A CE2 1 ATOM 716 C CZ . TYR B 2 91 ? 23.042 72.742 74.288 1.00 35.12 ? 91 TYR A CZ 1 ATOM 717 O OH . TYR B 2 91 ? 23.148 72.904 75.660 1.00 35.22 ? 91 TYR A OH 1 ATOM 718 N N . PHE B 2 92 ? 22.124 74.123 67.166 1.00 33.09 ? 92 PHE A N 1 ATOM 719 C CA . PHE B 2 92 ? 22.059 74.076 65.699 1.00 33.66 ? 92 PHE A CA 1 ATOM 720 C C . PHE B 2 92 ? 23.438 73.995 65.045 1.00 34.25 ? 92 PHE A C 1 ATOM 721 O O . PHE B 2 92 ? 24.380 74.649 65.478 1.00 35.07 ? 92 PHE A O 1 ATOM 722 C CB . PHE B 2 92 ? 21.366 75.334 65.148 1.00 33.77 ? 92 PHE A CB 1 ATOM 723 C CG . PHE B 2 92 ? 19.959 75.546 65.651 1.00 35.36 ? 92 PHE A CG 1 ATOM 724 C CD1 . PHE B 2 92 ? 18.873 74.951 65.010 1.00 35.89 ? 92 PHE A CD1 1 ATOM 725 C CD2 . PHE B 2 92 ? 19.718 76.362 66.756 1.00 35.68 ? 92 PHE A CD2 1 ATOM 726 C CE1 . PHE B 2 92 ? 17.567 75.170 65.462 1.00 35.83 ? 92 PHE A CE1 1 ATOM 727 C CE2 . PHE B 2 92 ? 18.420 76.585 67.214 1.00 36.16 ? 92 PHE A CE2 1 ATOM 728 C CZ . PHE B 2 92 ? 17.344 75.989 66.567 1.00 35.87 ? 92 PHE A CZ 1 ATOM 729 N N . PHE B 2 93 ? 23.567 73.191 63.999 1.00 34.96 ? 93 PHE A N 1 ATOM 730 C CA . PHE B 2 93 ? 24.839 73.127 63.293 1.00 35.77 ? 93 PHE A CA 1 ATOM 731 C C . PHE B 2 93 ? 24.983 74.506 62.654 1.00 37.49 ? 93 PHE A C 1 ATOM 732 O O . PHE B 2 93 ? 23.980 75.136 62.317 1.00 38.87 ? 93 PHE A O 1 ATOM 733 C CB . PHE B 2 93 ? 24.803 72.060 62.198 1.00 32.62 ? 93 PHE A CB 1 ATOM 734 C CG . PHE B 2 93 ? 24.910 70.660 62.711 1.00 29.47 ? 93 PHE A CG 1 ATOM 735 C CD1 . PHE B 2 93 ? 26.026 70.258 63.429 1.00 28.10 ? 93 PHE A CD1 1 ATOM 736 C CD2 . PHE B 2 93 ? 23.906 69.737 62.463 1.00 27.35 ? 93 PHE A CD2 1 ATOM 737 C CE1 . PHE B 2 93 ? 26.141 68.959 63.883 1.00 27.42 ? 93 PHE A CE1 1 ATOM 738 C CE2 . PHE B 2 93 ? 24.015 68.436 62.915 1.00 26.16 ? 93 PHE A CE2 1 ATOM 739 C CZ . PHE B 2 93 ? 25.135 68.046 63.629 1.00 26.46 ? 93 PHE A CZ 1 ATOM 740 N N . HIS B 2 94 ? 26.216 74.973 62.496 1.00 39.01 ? 94 HIS A N 1 ATOM 741 C CA . HIS B 2 94 ? 26.478 76.283 61.896 1.00 40.63 ? 94 HIS A CA 1 ATOM 742 C C . HIS B 2 94 ? 25.913 76.319 60.482 1.00 41.29 ? 94 HIS A C 1 ATOM 743 O O . HIS B 2 94 ? 26.333 75.541 59.629 1.00 42.78 ? 94 HIS A O 1 ATOM 744 C CB . HIS B 2 94 ? 27.996 76.552 61.869 1.00 41.17 ? 94 HIS A CB 1 ATOM 745 C CG . HIS B 2 94 ? 28.371 77.917 61.376 1.00 41.49 ? 94 HIS A CG 1 ATOM 746 N ND1 . HIS B 2 94 ? 28.452 78.233 60.034 1.00 41.57 ? 94 HIS A ND1 1 ATOM 747 C CD2 . HIS B 2 94 ? 28.679 79.054 62.045 1.00 41.68 ? 94 HIS A CD2 1 ATOM 748 C CE1 . HIS B 2 94 ? 28.793 79.500 59.900 1.00 40.69 ? 94 HIS A CE1 1 ATOM 749 N NE2 . HIS B 2 94 ? 28.936 80.023 61.106 1.00 41.93 ? 94 HIS A NE2 1 ATOM 750 N N . PRO B 2 95 ? 24.945 77.218 60.216 1.00 41.70 ? 95 PRO A N 1 ATOM 751 C CA . PRO B 2 95 ? 24.339 77.329 58.881 1.00 42.32 ? 95 PRO A CA 1 ATOM 752 C C . PRO B 2 95 ? 25.365 77.756 57.834 1.00 43.59 ? 95 PRO A C 1 ATOM 753 O O . PRO B 2 95 ? 26.212 78.605 58.107 1.00 44.73 ? 95 PRO A O 1 ATOM 754 C CB . PRO B 2 95 ? 23.239 78.368 59.090 1.00 41.31 ? 95 PRO A CB 1 ATOM 755 C CG . PRO B 2 95 ? 23.806 79.241 60.157 1.00 41.15 ? 95 PRO A CG 1 ATOM 756 C CD . PRO B 2 95 ? 24.397 78.240 61.124 1.00 41.83 ? 95 PRO A CD 1 ATOM 757 N N . ASP B 2 96 ? 25.296 77.179 56.638 1.00 45.59 ? 96 ASP A N 1 ATOM 758 C CA . ASP B 2 96 ? 26.266 77.522 55.605 1.00 47.05 ? 96 ASP A CA 1 ATOM 759 C C . ASP B 2 96 ? 25.772 78.548 54.580 1.00 47.43 ? 96 ASP A C 1 ATOM 760 O O . ASP B 2 96 ? 26.299 78.626 53.469 1.00 49.54 ? 96 ASP A O 1 ATOM 761 C CB . ASP B 2 96 ? 26.753 76.248 54.902 1.00 48.22 ? 96 ASP A CB 1 ATOM 762 C CG . ASP B 2 96 ? 25.707 75.653 53.985 1.00 51.09 ? 96 ASP A CG 1 ATOM 763 O OD1 . ASP B 2 96 ? 24.514 75.646 54.379 1.00 51.56 ? 96 ASP A OD1 1 ATOM 764 O OD2 . ASP B 2 96 ? 26.080 75.192 52.878 1.00 51.26 ? 96 ASP A OD2 1 ATOM 765 N N . ASN B 2 97 ? 24.762 79.330 54.953 1.00 46.78 ? 97 ASN A N 1 ATOM 766 C CA . ASN B 2 97 ? 24.228 80.383 54.088 1.00 46.31 ? 97 ASN A CA 1 ATOM 767 C C . ASN B 2 97 ? 23.141 81.180 54.809 1.00 46.32 ? 97 ASN A C 1 ATOM 768 O O . ASN B 2 97 ? 22.489 80.674 55.720 1.00 45.80 ? 97 ASN A O 1 ATOM 769 C CB . ASN B 2 97 ? 23.713 79.802 52.761 1.00 46.63 ? 97 ASN A CB 1 ATOM 770 C CG . ASN B 2 97 ? 22.613 78.784 52.945 1.00 48.79 ? 97 ASN A CG 1 ATOM 771 O OD1 . ASN B 2 97 ? 21.458 79.131 53.201 1.00 50.53 ? 97 ASN A OD1 1 ATOM 772 N ND2 . ASN B 2 97 ? 22.964 77.513 52.810 1.00 49.09 ? 97 ASN A ND2 1 ATOM 773 N N . GLN B 2 98 ? 22.967 82.437 54.407 1.00 47.29 ? 98 GLN A N 1 ATOM 774 C CA . GLN B 2 98 ? 21.989 83.326 55.033 1.00 48.24 ? 98 GLN A CA 1 ATOM 775 C C . GLN B 2 98 ? 20.558 82.778 55.109 1.00 48.55 ? 98 GLN A C 1 ATOM 776 O O . GLN B 2 98 ? 19.928 82.825 56.174 1.00 48.40 ? 98 GLN A O 1 ATOM 777 C CB . GLN B 2 98 ? 21.991 84.684 54.322 1.00 48.34 ? 98 GLN A CB 1 ATOM 778 N N . GLU B 2 99 ? 20.042 82.271 53.988 1.00 48.25 ? 99 GLU A N 1 ATOM 779 C CA . GLU B 2 99 ? 18.683 81.730 53.951 1.00 47.31 ? 99 GLU A CA 1 ATOM 780 C C . GLU B 2 99 ? 18.447 80.694 55.063 1.00 46.80 ? 99 GLU A C 1 ATOM 781 O O . GLU B 2 99 ? 17.475 80.796 55.821 1.00 45.70 ? 99 GLU A O 1 ATOM 782 C CB . GLU B 2 99 ? 18.404 81.118 52.572 1.00 46.36 ? 99 GLU A CB 1 ATOM 783 N N . ASP B 2 100 ? 19.342 79.708 55.158 1.00 45.86 ? 100 ASP A N 1 ATOM 784 C CA . ASP B 2 100 ? 19.253 78.657 56.173 1.00 44.96 ? 100 ASP A CA 1 ATOM 785 C C . ASP B 2 100 ? 19.278 79.203 57.590 1.00 44.50 ? 100 ASP A C 1 ATOM 786 O O . ASP B 2 100 ? 18.526 78.750 58.451 1.00 43.42 ? 100 ASP A O 1 ATOM 787 C CB . ASP B 2 100 ? 20.407 77.671 56.027 1.00 46.37 ? 100 ASP A CB 1 ATOM 788 C CG . ASP B 2 100 ? 20.154 76.636 54.965 1.00 48.61 ? 100 ASP A CG 1 ATOM 789 O OD1 . ASP B 2 100 ? 19.035 76.625 54.408 1.00 49.91 ? 100 ASP A OD1 1 ATOM 790 O OD2 . ASP B 2 100 ? 21.074 75.833 54.696 1.00 50.61 ? 100 ASP A OD2 1 ATOM 791 N N . ALA B 2 101 ? 20.170 80.158 57.835 1.00 44.11 ? 101 ALA A N 1 ATOM 792 C CA . ALA B 2 101 ? 20.285 80.763 59.154 1.00 44.02 ? 101 ALA A CA 1 ATOM 793 C C . ALA B 2 101 ? 18.943 81.394 59.536 1.00 44.07 ? 101 ALA A C 1 ATOM 794 O O . ALA B 2 101 ? 18.493 81.272 60.675 1.00 44.56 ? 101 ALA A O 1 ATOM 795 C CB . ALA B 2 101 ? 21.391 81.813 59.152 1.00 41.81 ? 101 ALA A CB 1 ATOM 796 N N . GLU B 2 102 ? 18.299 82.050 58.573 1.00 44.73 ? 102 GLU A N 1 ATOM 797 C CA . GLU B 2 102 ? 17.012 82.698 58.817 1.00 44.83 ? 102 GLU A CA 1 ATOM 798 C C . GLU B 2 102 ? 15.896 81.693 59.100 1.00 44.73 ? 102 GLU A C 1 ATOM 799 O O . GLU B 2 102 ? 14.944 82.005 59.822 1.00 45.37 ? 102 GLU A O 1 ATOM 800 C CB . GLU B 2 102 ? 16.630 83.574 57.624 1.00 44.32 ? 102 GLU A CB 1 ATOM 801 N N . ALA B 2 103 ? 16.020 80.491 58.533 1.00 43.27 ? 103 ALA A N 1 ATOM 802 C CA . ALA B 2 103 ? 15.018 79.439 58.700 1.00 40.72 ? 103 ALA A CA 1 ATOM 803 C C . ALA B 2 103 ? 15.082 78.723 60.046 1.00 39.41 ? 103 ALA A C 1 ATOM 804 O O . ALA B 2 103 ? 14.043 78.436 60.639 1.00 38.29 ? 103 ALA A O 1 ATOM 805 C CB . ALA B 2 103 ? 15.135 78.428 57.567 1.00 38.65 ? 103 ALA A CB 1 ATOM 806 N N . ILE B 2 104 ? 16.285 78.433 60.537 1.00 39.26 ? 104 ILE A N 1 ATOM 807 C CA . ILE B 2 104 ? 16.401 77.733 61.818 1.00 40.19 ? 104 ILE A CA 1 ATOM 808 C C . ILE B 2 104 ? 15.891 78.583 62.986 1.00 41.75 ? 104 ILE A C 1 ATOM 809 O O . ILE B 2 104 ? 15.817 78.115 64.130 1.00 42.23 ? 104 ILE A O 1 ATOM 810 C CB . ILE B 2 104 ? 17.873 77.265 62.120 1.00 37.98 ? 104 ILE A CB 1 ATOM 811 C CG1 . ILE B 2 104 ? 18.842 78.447 62.076 1.00 35.90 ? 104 ILE A CG1 1 ATOM 812 C CG2 . ILE B 2 104 ? 18.294 76.183 61.135 1.00 36.05 ? 104 ILE A CG2 1 ATOM 813 C CD1 . ILE B 2 104 ? 20.234 78.115 62.598 1.00 30.76 ? 104 ILE A CD1 1 ATOM 814 N N . THR B 2 105 ? 15.526 79.827 62.688 1.00 42.58 ? 105 THR A N 1 ATOM 815 C CA . THR B 2 105 ? 15.012 80.745 63.698 1.00 43.31 ? 105 THR A CA 1 ATOM 816 C C . THR B 2 105 ? 13.651 80.274 64.185 1.00 44.14 ? 105 THR A C 1 ATOM 817 O O . THR B 2 105 ? 13.300 80.471 65.348 1.00 45.25 ? 105 THR A O 1 ATOM 818 C CB . THR B 2 105 ? 14.851 82.165 63.121 1.00 43.18 ? 105 THR A CB 1 ATOM 819 O OG1 . THR B 2 105 ? 16.119 82.627 62.644 1.00 43.49 ? 105 THR A OG1 1 ATOM 820 C CG2 . THR B 2 105 ? 14.323 83.127 64.183 1.00 43.18 ? 105 THR A CG2 1 ATOM 821 N N . HIS B 2 106 ? 12.895 79.643 63.289 1.00 44.22 ? 106 HIS A N 1 ATOM 822 C CA . HIS B 2 106 ? 11.557 79.155 63.606 1.00 44.71 ? 106 HIS A CA 1 ATOM 823 C C . HIS B 2 106 ? 11.519 77.791 64.289 1.00 43.70 ? 106 HIS A C 1 ATOM 824 O O . HIS B 2 106 ? 10.443 77.270 64.583 1.00 42.77 ? 106 HIS A O 1 ATOM 825 C CB . HIS B 2 106 ? 10.709 79.093 62.336 1.00 47.67 ? 106 HIS A CB 1 ATOM 826 C CG . HIS B 2 106 ? 10.752 80.346 61.521 1.00 50.76 ? 106 HIS A CG 1 ATOM 827 N ND1 . HIS B 2 106 ? 10.491 81.593 62.054 1.00 52.05 ? 106 HIS A ND1 1 ATOM 828 C CD2 . HIS B 2 106 ? 11.035 80.552 60.213 1.00 52.35 ? 106 HIS A CD2 1 ATOM 829 C CE1 . HIS B 2 106 ? 10.614 82.507 61.110 1.00 52.99 ? 106 HIS A CE1 1 ATOM 830 N NE2 . HIS B 2 106 ? 10.944 81.902 59.981 1.00 52.35 ? 106 HIS A NE2 1 ATOM 831 N N . LEU B 2 107 ? 12.683 77.203 64.528 1.00 43.97 ? 107 LEU A N 1 ATOM 832 C CA . LEU B 2 107 ? 12.732 75.907 65.188 1.00 44.74 ? 107 LEU A CA 1 ATOM 833 C C . LEU B 2 107 ? 12.898 76.095 66.688 1.00 45.74 ? 107 LEU A C 1 ATOM 834 O O . LEU B 2 107 ? 13.603 77.006 67.137 1.00 46.80 ? 107 LEU A O 1 ATOM 835 C CB . LEU B 2 107 ? 13.881 75.055 64.637 1.00 44.43 ? 107 LEU A CB 1 ATOM 836 C CG . LEU B 2 107 ? 13.671 74.332 63.300 1.00 44.26 ? 107 LEU A CG 1 ATOM 837 C CD1 . LEU B 2 107 ? 14.975 73.686 62.866 1.00 44.60 ? 107 LEU A CD1 1 ATOM 838 C CD2 . LEU B 2 107 ? 12.581 73.278 63.440 1.00 42.16 ? 107 LEU A CD2 1 ATOM 839 N N . PHE B 2 108 ? 12.235 75.231 67.454 1.00 47.51 ? 108 PHE A N 1 ATOM 840 C CA . PHE B 2 108 ? 12.288 75.272 68.916 1.00 48.63 ? 108 PHE A CA 1 ATOM 841 C C . PHE B 2 108 ? 12.229 76.708 69.432 1.00 50.73 ? 108 PHE A C 1 ATOM 842 O O . PHE B 2 108 ? 13.182 77.201 70.045 1.00 51.39 ? 108 PHE A O 1 ATOM 843 C CB . PHE B 2 108 ? 13.577 74.608 69.418 1.00 47.14 ? 108 PHE A CB 1 ATOM 844 C CG . PHE B 2 108 ? 13.909 73.320 68.725 1.00 44.08 ? 108 PHE A CG 1 ATOM 845 C CD1 . PHE B 2 108 ? 13.052 72.231 68.807 1.00 41.95 ? 108 PHE A CD1 1 ATOM 846 C CD2 . PHE B 2 108 ? 15.071 73.208 67.966 1.00 42.53 ? 108 PHE A CD2 1 ATOM 847 C CE1 . PHE B 2 108 ? 13.351 71.046 68.150 1.00 41.63 ? 108 PHE A CE1 1 ATOM 848 C CE2 . PHE B 2 108 ? 15.379 72.026 67.304 1.00 41.71 ? 108 PHE A CE2 1 ATOM 849 C CZ . PHE B 2 108 ? 14.517 70.944 67.392 1.00 41.93 ? 108 PHE A CZ 1 ATOM 850 N N . THR B 2 109 ? 11.112 77.378 69.177 1.00 52.27 ? 109 THR A N 1 ATOM 851 C CA . THR B 2 109 ? 10.942 78.749 69.631 1.00 52.40 ? 109 THR A CA 1 ATOM 852 C C . THR B 2 109 ? 10.717 78.791 71.144 1.00 52.50 ? 109 THR A C 1 ATOM 853 O O . THR B 2 109 ? 11.001 79.793 71.795 1.00 51.24 ? 109 THR A O 1 ATOM 854 C CB . THR B 2 109 ? 9.767 79.413 68.900 1.00 53.05 ? 109 THR A CB 1 ATOM 855 O OG1 . THR B 2 109 ? 10.110 79.574 67.517 1.00 53.76 ? 109 THR A OG1 1 ATOM 856 C CG2 . THR B 2 109 ? 9.449 80.771 69.509 1.00 53.95 ? 109 THR A CG2 1 ATOM 857 N N . ASP B 2 110 ? 10.224 77.686 71.697 1.00 53.91 ? 110 ASP A N 1 ATOM 858 C CA . ASP B 2 110 ? 9.966 77.573 73.133 1.00 56.23 ? 110 ASP A CA 1 ATOM 859 C C . ASP B 2 110 ? 11.229 77.818 73.949 1.00 56.85 ? 110 ASP A C 1 ATOM 860 O O . ASP B 2 110 ? 11.334 78.801 74.679 1.00 57.73 ? 110 ASP A O 1 ATOM 861 C CB . ASP B 2 110 ? 9.469 76.170 73.485 1.00 58.20 ? 110 ASP A CB 1 ATOM 862 C CG . ASP B 2 110 ? 8.298 75.732 72.641 1.00 61.33 ? 110 ASP A CG 1 ATOM 863 O OD1 . ASP B 2 110 ? 7.188 76.284 72.831 1.00 63.13 ? 110 ASP A OD1 1 ATOM 864 O OD2 . ASP B 2 110 ? 8.495 74.834 71.788 1.00 62.36 ? 110 ASP A OD2 1 ATOM 865 N N . VAL B 2 111 ? 12.171 76.884 73.816 1.00 56.97 ? 111 VAL A N 1 ATOM 866 C CA . VAL B 2 111 ? 13.453 76.885 74.521 1.00 55.86 ? 111 VAL A CA 1 ATOM 867 C C . VAL B 2 111 ? 14.009 78.230 74.971 1.00 56.75 ? 111 VAL A C 1 ATOM 868 O O . VAL B 2 111 ? 13.945 79.228 74.248 1.00 57.41 ? 111 VAL A O 1 ATOM 869 C CB . VAL B 2 111 ? 14.537 76.194 73.677 1.00 54.85 ? 111 VAL A CB 1 ATOM 870 C CG1 . VAL B 2 111 ? 14.119 74.771 73.382 1.00 53.33 ? 111 VAL A CG1 1 ATOM 871 C CG2 . VAL B 2 111 ? 14.773 76.974 72.392 1.00 52.67 ? 111 VAL A CG2 1 ATOM 872 N N . GLN B 2 112 ? 14.581 78.234 76.171 1.00 56.17 ? 112 GLN A N 1 ATOM 873 C CA . GLN B 2 112 ? 15.175 79.437 76.736 1.00 55.97 ? 112 GLN A CA 1 ATOM 874 C C . GLN B 2 112 ? 16.597 79.687 76.195 1.00 55.81 ? 112 GLN A C 1 ATOM 875 O O . GLN B 2 112 ? 17.019 80.840 76.055 1.00 55.62 ? 112 GLN A O 1 ATOM 876 C CB . GLN B 2 112 ? 15.202 79.324 78.261 1.00 55.47 ? 112 GLN A CB 1 ATOM 877 N N . ASN B 2 113 ? 17.321 78.612 75.875 1.00 55.21 ? 113 ASN A N 1 ATOM 878 C CA . ASN B 2 113 ? 18.703 78.721 75.388 1.00 54.38 ? 113 ASN A CA 1 ATOM 879 C C . ASN B 2 113 ? 18.941 78.142 73.991 1.00 53.50 ? 113 ASN A C 1 ATOM 880 O O . ASN B 2 113 ? 18.826 76.930 73.797 1.00 54.81 ? 113 ASN A O 1 ATOM 881 C CB . ASN B 2 113 ? 19.632 78.008 76.371 1.00 54.32 ? 113 ASN A CB 1 ATOM 882 C CG . ASN B 2 113 ? 19.263 78.280 77.812 1.00 54.85 ? 113 ASN A CG 1 ATOM 883 O OD1 . ASN B 2 113 ? 19.619 79.317 78.374 1.00 55.54 ? 113 ASN A OD1 1 ATOM 884 N ND2 . ASN B 2 113 ? 18.522 77.356 78.415 1.00 54.90 ? 113 ASN A ND2 1 ATOM 885 N N . ARG B 2 114 ? 19.275 79.000 73.027 1.00 50.74 ? 114 ARG A N 1 ATOM 886 C CA . ARG B 2 114 ? 19.548 78.549 71.662 1.00 47.67 ? 114 ARG A CA 1 ATOM 887 C C . ARG B 2 114 ? 21.031 78.766 71.392 1.00 46.19 ? 114 ARG A C 1 ATOM 888 O O . ARG B 2 114 ? 21.524 79.894 71.444 1.00 46.84 ? 114 ARG A O 1 ATOM 889 C CB . ARG B 2 114 ? 18.723 79.334 70.619 1.00 46.46 ? 114 ARG A CB 1 ATOM 890 C CG . ARG B 2 114 ? 17.212 79.333 70.846 1.00 47.57 ? 114 ARG A CG 1 ATOM 891 C CD . ARG B 2 114 ? 16.392 78.906 69.612 1.00 49.48 ? 114 ARG A CD 1 ATOM 892 N NE . ARG B 2 114 ? 16.196 79.958 68.614 1.00 51.98 ? 114 ARG A NE 1 ATOM 893 C CZ . ARG B 2 114 ? 17.037 80.239 67.620 1.00 55.13 ? 114 ARG A CZ 1 ATOM 894 N NH1 . ARG B 2 114 ? 18.159 79.547 67.468 1.00 56.97 ? 114 ARG A NH1 1 ATOM 895 N NH2 . ARG B 2 114 ? 16.750 81.214 66.766 1.00 55.82 ? 114 ARG A NH2 1 ATOM 896 N N . TYR B 2 115 ? 21.747 77.684 71.118 1.00 44.88 ? 115 TYR A N 1 ATOM 897 C CA . TYR B 2 115 ? 23.172 77.768 70.830 1.00 44.08 ? 115 TYR A CA 1 ATOM 898 C C . TYR B 2 115 ? 23.399 77.331 69.398 1.00 41.22 ? 115 TYR A C 1 ATOM 899 O O . TYR B 2 115 ? 22.693 76.464 68.894 1.00 41.72 ? 115 TYR A O 1 ATOM 900 C CB . TYR B 2 115 ? 23.955 76.843 71.751 1.00 47.89 ? 115 TYR A CB 1 ATOM 901 C CG . TYR B 2 115 ? 23.731 77.102 73.220 1.00 53.23 ? 115 TYR A CG 1 ATOM 902 C CD1 . TYR B 2 115 ? 24.439 78.100 73.891 1.00 55.79 ? 115 TYR A CD1 1 ATOM 903 C CD2 . TYR B 2 115 ? 22.815 76.339 73.946 1.00 55.76 ? 115 TYR A CD2 1 ATOM 904 C CE1 . TYR B 2 115 ? 24.242 78.331 75.259 1.00 58.08 ? 115 TYR A CE1 1 ATOM 905 C CE2 . TYR B 2 115 ? 22.607 76.559 75.310 1.00 58.45 ? 115 TYR A CE2 1 ATOM 906 C CZ . TYR B 2 115 ? 23.325 77.555 75.963 1.00 59.62 ? 115 TYR A CZ 1 ATOM 907 O OH . TYR B 2 115 ? 23.133 77.769 77.315 1.00 61.97 ? 115 TYR A OH 1 ATOM 908 N N . THR B 2 116 ? 24.379 77.935 68.740 1.00 38.01 ? 116 THR A N 1 ATOM 909 C CA . THR B 2 116 ? 24.702 77.576 67.368 1.00 34.39 ? 116 THR A CA 1 ATOM 910 C C . THR B 2 116 ? 26.145 77.110 67.317 1.00 34.13 ? 116 THR A C 1 ATOM 911 O O . THR B 2 116 ? 27.060 77.902 67.523 1.00 36.09 ? 116 THR A O 1 ATOM 912 C CB . THR B 2 116 ? 24.546 78.766 66.411 1.00 32.85 ? 116 THR A CB 1 ATOM 913 O OG1 . THR B 2 116 ? 23.172 79.161 66.358 1.00 31.91 ? 116 THR A OG1 1 ATOM 914 C CG2 . THR B 2 116 ? 25.012 78.388 65.011 1.00 31.08 ? 116 THR A CG2 1 ATOM 915 N N . PHE B 2 117 ? 26.342 75.824 67.051 1.00 32.63 ? 117 PHE A N 1 ATOM 916 C CA . PHE B 2 117 ? 27.679 75.253 66.959 1.00 31.30 ? 117 PHE A CA 1 ATOM 917 C C . PHE B 2 117 ? 28.582 76.060 66.020 1.00 31.84 ? 117 PHE A C 1 ATOM 918 O O . PHE B 2 117 ? 28.107 76.731 65.101 1.00 30.70 ? 117 PHE A O 1 ATOM 919 C CB . PHE B 2 117 ? 27.593 73.813 66.466 1.00 29.84 ? 117 PHE A CB 1 ATOM 920 C CG . PHE B 2 117 ? 26.899 72.884 67.419 1.00 26.98 ? 117 PHE A CG 1 ATOM 921 C CD1 . PHE B 2 117 ? 27.415 72.662 68.687 1.00 24.01 ? 117 PHE A CD1 1 ATOM 922 C CD2 . PHE B 2 117 ? 25.737 72.214 67.034 1.00 26.22 ? 117 PHE A CD2 1 ATOM 923 C CE1 . PHE B 2 117 ? 26.797 71.783 69.558 1.00 23.29 ? 117 PHE A CE1 1 ATOM 924 C CE2 . PHE B 2 117 ? 25.107 71.328 67.900 1.00 25.19 ? 117 PHE A CE2 1 ATOM 925 C CZ . PHE B 2 117 ? 25.638 71.113 69.169 1.00 23.94 ? 117 PHE A CZ 1 ATOM 926 N N . ALA B 2 118 ? 29.888 75.991 66.267 1.00 32.55 ? 118 ALA A N 1 ATOM 927 C CA . ALA B 2 118 ? 30.868 76.711 65.464 1.00 33.14 ? 118 ALA A CA 1 ATOM 928 C C . ALA B 2 118 ? 31.143 75.961 64.174 1.00 34.76 ? 118 ALA A C 1 ATOM 929 O O . ALA B 2 118 ? 31.703 76.515 63.230 1.00 35.48 ? 118 ALA A O 1 ATOM 930 C CB . ALA B 2 118 ? 32.158 76.867 66.248 1.00 31.68 ? 118 ALA A CB 1 ATOM 931 N N . PHE B 2 119 ? 30.731 74.697 64.142 1.00 36.05 ? 119 PHE A N 1 ATOM 932 C CA . PHE B 2 119 ? 30.949 73.824 62.993 1.00 36.94 ? 119 PHE A CA 1 ATOM 933 C C . PHE B 2 119 ? 29.665 73.401 62.285 1.00 37.48 ? 119 PHE A C 1 ATOM 934 O O . PHE B 2 119 ? 28.565 73.584 62.798 1.00 37.43 ? 119 PHE A O 1 ATOM 935 C CB . PHE B 2 119 ? 31.717 72.583 63.454 1.00 37.13 ? 119 PHE A CB 1 ATOM 936 C CG . PHE B 2 119 ? 31.153 71.958 64.703 1.00 37.64 ? 119 PHE A CG 1 ATOM 937 C CD1 . PHE B 2 119 ? 29.931 71.291 64.677 1.00 37.67 ? 119 PHE A CD1 1 ATOM 938 C CD2 . PHE B 2 119 ? 31.828 72.071 65.916 1.00 38.13 ? 119 PHE A CD2 1 ATOM 939 C CE1 . PHE B 2 119 ? 29.385 70.750 65.838 1.00 37.61 ? 119 PHE A CE1 1 ATOM 940 C CE2 . PHE B 2 119 ? 31.292 71.534 67.087 1.00 38.60 ? 119 PHE A CE2 1 ATOM 941 C CZ . PHE B 2 119 ? 30.066 70.872 67.045 1.00 38.25 ? 119 PHE A CZ 1 ATOM 942 N N . GLY B 2 120 ? 29.822 72.821 61.101 1.00 38.31 ? 120 GLY A N 1 ATOM 943 C CA . GLY B 2 120 ? 28.676 72.371 60.334 1.00 39.20 ? 120 GLY A CA 1 ATOM 944 C C . GLY B 2 120 ? 28.343 70.915 60.603 1.00 40.22 ? 120 GLY A C 1 ATOM 945 O O . GLY B 2 120 ? 29.034 70.236 61.366 1.00 39.95 ? 120 GLY A O 1 ATOM 946 N N . GLY B 2 121 ? 27.278 70.433 59.968 1.00 40.86 ? 121 GLY A N 1 ATOM 947 C CA . GLY B 2 121 ? 26.859 69.059 60.159 1.00 39.27 ? 121 GLY A CA 1 ATOM 948 C C . GLY B 2 121 ? 27.513 68.076 59.212 1.00 38.37 ? 121 GLY A C 1 ATOM 949 O O . GLY B 2 121 ? 27.489 66.878 59.463 1.00 39.37 ? 121 GLY A O 1 ATOM 950 N N . ASN B 2 122 ? 28.096 68.569 58.125 1.00 36.53 ? 122 ASN A N 1 ATOM 951 C CA . ASN B 2 122 ? 28.754 67.699 57.157 1.00 36.70 ? 122 ASN A CA 1 ATOM 952 C C . ASN B 2 122 ? 29.596 66.607 57.830 1.00 34.94 ? 122 ASN A C 1 ATOM 953 O O . ASN B 2 122 ? 30.088 66.788 58.943 1.00 34.36 ? 122 ASN A O 1 ATOM 954 C CB . ASN B 2 122 ? 29.622 68.539 56.216 1.00 39.61 ? 122 ASN A CB 1 ATOM 955 C CG . ASN B 2 122 ? 30.672 69.357 56.949 1.00 42.92 ? 122 ASN A CG 1 ATOM 956 O OD1 . ASN B 2 122 ? 30.342 70.237 57.746 1.00 45.30 ? 122 ASN A OD1 1 ATOM 957 N ND2 . ASN B 2 122 ? 31.947 69.074 56.678 1.00 41.98 ? 122 ASN A ND2 1 ATOM 958 N N . TYR B 2 123 ? 29.757 65.471 57.158 1.00 33.41 ? 123 TYR A N 1 ATOM 959 C CA . TYR B 2 123 ? 30.517 64.366 57.727 1.00 33.29 ? 123 TYR A CA 1 ATOM 960 C C . TYR B 2 123 ? 31.988 64.653 58.014 1.00 34.91 ? 123 TYR A C 1 ATOM 961 O O . TYR B 2 123 ? 32.490 64.293 59.079 1.00 34.75 ? 123 TYR A O 1 ATOM 962 C CB . TYR B 2 123 ? 30.429 63.133 56.831 1.00 31.82 ? 123 TYR A CB 1 ATOM 963 C CG . TYR B 2 123 ? 29.168 62.319 56.974 1.00 29.86 ? 123 TYR A CG 1 ATOM 964 C CD1 . TYR B 2 123 ? 28.521 62.191 58.204 1.00 30.31 ? 123 TYR A CD1 1 ATOM 965 C CD2 . TYR B 2 123 ? 28.648 61.626 55.885 1.00 29.09 ? 123 TYR A CD2 1 ATOM 966 C CE1 . TYR B 2 123 ? 27.375 61.386 58.341 1.00 29.37 ? 123 TYR A CE1 1 ATOM 967 C CE2 . TYR B 2 123 ? 27.516 60.820 56.010 1.00 29.15 ? 123 TYR A CE2 1 ATOM 968 C CZ . TYR B 2 123 ? 26.882 60.706 57.231 1.00 28.67 ? 123 TYR A CZ 1 ATOM 969 O OH . TYR B 2 123 ? 25.742 59.937 57.315 1.00 27.90 ? 123 TYR A OH 1 ATOM 970 N N . ASP B 2 124 ? 32.685 65.274 57.066 1.00 36.31 ? 124 ASP A N 1 ATOM 971 C CA . ASP B 2 124 ? 34.097 65.576 57.263 1.00 37.73 ? 124 ASP A CA 1 ATOM 972 C C . ASP B 2 124 ? 34.292 66.266 58.599 1.00 37.58 ? 124 ASP A C 1 ATOM 973 O O . ASP B 2 124 ? 34.960 65.746 59.494 1.00 39.55 ? 124 ASP A O 1 ATOM 974 C CB . ASP B 2 124 ? 34.621 66.493 56.164 1.00 41.71 ? 124 ASP A CB 1 ATOM 975 C CG . ASP B 2 124 ? 34.333 65.966 54.783 1.00 46.92 ? 124 ASP A CG 1 ATOM 976 O OD1 . ASP B 2 124 ? 34.402 64.730 54.592 1.00 51.52 ? 124 ASP A OD1 1 ATOM 977 O OD2 . ASP B 2 124 ? 34.047 66.792 53.886 1.00 49.11 ? 124 ASP A OD2 1 ATOM 978 N N . ARG B 2 125 ? 33.700 67.445 58.730 1.00 36.56 ? 125 ARG A N 1 ATOM 979 C CA . ARG B 2 125 ? 33.821 68.207 59.956 1.00 35.19 ? 125 ARG A CA 1 ATOM 980 C C . ARG B 2 125 ? 33.460 67.349 61.168 1.00 34.34 ? 125 ARG A C 1 ATOM 981 O O . ARG B 2 125 ? 34.158 67.372 62.169 1.00 34.46 ? 125 ARG A O 1 ATOM 982 C CB . ARG B 2 125 ? 32.942 69.456 59.865 1.00 35.14 ? 125 ARG A CB 1 ATOM 983 C CG . ARG B 2 125 ? 33.060 70.419 61.029 1.00 36.77 ? 125 ARG A CG 1 ATOM 984 C CD . ARG B 2 125 ? 34.480 70.514 61.586 1.00 39.92 ? 125 ARG A CD 1 ATOM 985 N NE . ARG B 2 125 ? 35.493 70.969 60.632 1.00 41.96 ? 125 ARG A NE 1 ATOM 986 C CZ . ARG B 2 125 ? 35.435 72.106 59.943 1.00 43.37 ? 125 ARG A CZ 1 ATOM 987 N NH1 . ARG B 2 125 ? 34.395 72.926 60.080 1.00 43.40 ? 125 ARG A NH1 1 ATOM 988 N NH2 . ARG B 2 125 ? 36.438 72.440 59.138 1.00 41.91 ? 125 ARG A NH2 1 ATOM 989 N N . LEU B 2 126 ? 32.390 66.569 61.073 1.00 34.36 ? 126 LEU A N 1 ATOM 990 C CA . LEU B 2 126 ? 31.975 65.714 62.187 1.00 34.53 ? 126 LEU A CA 1 ATOM 991 C C . LEU B 2 126 ? 32.926 64.542 62.471 1.00 35.20 ? 126 LEU A C 1 ATOM 992 O O . LEU B 2 126 ? 33.120 64.165 63.633 1.00 34.56 ? 126 LEU A O 1 ATOM 993 C CB . LEU B 2 126 ? 30.554 65.191 61.945 1.00 32.80 ? 126 LEU A CB 1 ATOM 994 C CG . LEU B 2 126 ? 29.457 65.875 62.761 1.00 31.09 ? 126 LEU A CG 1 ATOM 995 C CD1 . LEU B 2 126 ? 29.594 67.382 62.698 1.00 29.34 ? 126 LEU A CD1 1 ATOM 996 C CD2 . LEU B 2 126 ? 28.117 65.428 62.232 1.00 31.96 ? 126 LEU A CD2 1 ATOM 997 N N . GLU B 2 127 ? 33.510 63.966 61.419 1.00 35.84 ? 127 GLU A N 1 ATOM 998 C CA . GLU B 2 127 ? 34.452 62.856 61.579 1.00 35.69 ? 127 GLU A CA 1 ATOM 999 C C . GLU B 2 127 ? 35.757 63.363 62.181 1.00 34.17 ? 127 GLU A C 1 ATOM 1000 O O . GLU B 2 127 ? 36.407 62.675 62.958 1.00 33.65 ? 127 GLU A O 1 ATOM 1001 C CB . GLU B 2 127 ? 34.754 62.201 60.231 1.00 36.30 ? 127 GLU A CB 1 ATOM 1002 C CG . GLU B 2 127 ? 33.633 61.366 59.685 1.00 38.94 ? 127 GLU A CG 1 ATOM 1003 C CD . GLU B 2 127 ? 34.029 60.639 58.425 1.00 42.02 ? 127 GLU A CD 1 ATOM 1004 O OE1 . GLU B 2 127 ? 34.476 61.307 57.469 1.00 43.09 ? 127 GLU A OE1 1 ATOM 1005 O OE2 . GLU B 2 127 ? 33.891 59.399 58.385 1.00 42.79 ? 127 GLU A OE2 1 ATOM 1006 N N . GLN B 2 128 ? 36.136 64.574 61.805 1.00 33.00 ? 128 GLN A N 1 ATOM 1007 C CA . GLN B 2 128 ? 37.355 65.186 62.299 1.00 34.09 ? 128 GLN A CA 1 ATOM 1008 C C . GLN B 2 128 ? 37.267 65.430 63.806 1.00 33.07 ? 128 GLN A C 1 ATOM 1009 O O . GLN B 2 128 ? 38.148 65.027 64.560 1.00 32.45 ? 128 GLN A O 1 ATOM 1010 C CB . GLN B 2 128 ? 37.582 66.495 61.544 1.00 36.24 ? 128 GLN A CB 1 ATOM 1011 C CG . GLN B 2 128 ? 38.672 67.392 62.085 1.00 41.58 ? 128 GLN A CG 1 ATOM 1012 C CD . GLN B 2 128 ? 38.952 68.571 61.161 1.00 45.36 ? 128 GLN A CD 1 ATOM 1013 O OE1 . GLN B 2 128 ? 38.052 69.068 60.476 1.00 48.63 ? 128 GLN A OE1 1 ATOM 1014 N NE2 . GLN B 2 128 ? 40.196 69.033 61.148 1.00 46.03 ? 128 GLN A NE2 1 ATOM 1015 N N . LEU B 2 129 ? 36.189 66.082 64.228 1.00 31.88 ? 129 LEU A N 1 ATOM 1016 C CA . LEU B 2 129 ? 35.948 66.402 65.631 1.00 29.90 ? 129 LEU A CA 1 ATOM 1017 C C . LEU B 2 129 ? 35.771 65.140 66.464 1.00 30.36 ? 129 LEU A C 1 ATOM 1018 O O . LEU B 2 129 ? 36.189 65.083 67.621 1.00 30.95 ? 129 LEU A O 1 ATOM 1019 C CB . LEU B 2 129 ? 34.686 67.266 65.770 1.00 28.70 ? 129 LEU A CB 1 ATOM 1020 C CG . LEU B 2 129 ? 34.575 68.570 64.973 1.00 26.89 ? 129 LEU A CG 1 ATOM 1021 C CD1 . LEU B 2 129 ? 33.205 69.156 65.177 1.00 26.99 ? 129 LEU A CD1 1 ATOM 1022 C CD2 . LEU B 2 129 ? 35.627 69.552 65.409 1.00 27.88 ? 129 LEU A CD2 1 ATOM 1023 N N . ALA B 2 130 ? 35.142 64.130 65.877 1.00 30.72 ? 130 ALA A N 1 ATOM 1024 C CA . ALA B 2 130 ? 34.896 62.879 66.587 1.00 31.27 ? 130 ALA A CA 1 ATOM 1025 C C . ALA B 2 130 ? 36.179 62.088 66.827 1.00 31.33 ? 130 ALA A C 1 ATOM 1026 O O . ALA B 2 130 ? 36.283 61.323 67.787 1.00 31.46 ? 130 ALA A O 1 ATOM 1027 C CB . ALA B 2 130 ? 33.890 62.027 65.811 1.00 29.05 ? 130 ALA A CB 1 ATOM 1028 N N . GLY B 2 131 ? 37.160 62.286 65.955 1.00 32.65 ? 131 GLY A N 1 ATOM 1029 C CA . GLY B 2 131 ? 38.408 61.561 66.079 1.00 35.14 ? 131 GLY A CA 1 ATOM 1030 C C . GLY B 2 131 ? 38.236 60.155 65.530 1.00 36.89 ? 131 GLY A C 1 ATOM 1031 O O . GLY B 2 131 ? 38.963 59.239 65.902 1.00 39.42 ? 131 GLY A O 1 ATOM 1032 N N . ASN B 2 132 ? 37.257 59.981 64.650 1.00 36.82 ? 132 ASN A N 1 ATOM 1033 C CA . ASN B 2 132 ? 36.987 58.687 64.046 1.00 36.18 ? 132 ASN A CA 1 ATOM 1034 C C . ASN B 2 132 ? 36.319 58.839 62.694 1.00 34.89 ? 132 ASN A C 1 ATOM 1035 O O . ASN B 2 132 ? 35.641 59.833 62.414 1.00 33.26 ? 132 ASN A O 1 ATOM 1036 C CB . ASN B 2 132 ? 36.081 57.834 64.939 1.00 39.09 ? 132 ASN A CB 1 ATOM 1037 C CG . ASN B 2 132 ? 36.858 56.974 65.915 1.00 41.77 ? 132 ASN A CG 1 ATOM 1038 O OD1 . ASN B 2 132 ? 37.751 56.221 65.525 1.00 42.38 ? 132 ASN A OD1 1 ATOM 1039 N ND2 . ASN B 2 132 ? 36.510 57.070 67.193 1.00 44.48 ? 132 ASN A ND2 1 ATOM 1040 N N . LEU B 2 133 ? 36.525 57.835 61.853 1.00 32.76 ? 133 LEU A N 1 ATOM 1041 C CA . LEU B 2 133 ? 35.932 57.816 60.532 1.00 30.59 ? 133 LEU A CA 1 ATOM 1042 C C . LEU B 2 133 ? 34.618 57.056 60.656 1.00 30.72 ? 133 LEU A C 1 ATOM 1043 O O . LEU B 2 133 ? 34.429 56.252 61.574 1.00 29.50 ? 133 LEU A O 1 ATOM 1044 C CB . LEU B 2 133 ? 36.866 57.110 59.540 1.00 28.94 ? 133 LEU A CB 1 ATOM 1045 C CG . LEU B 2 133 ? 37.787 57.972 58.665 1.00 25.61 ? 133 LEU A CG 1 ATOM 1046 C CD1 . LEU B 2 133 ? 38.609 58.897 59.512 1.00 26.45 ? 133 LEU A CD1 1 ATOM 1047 C CD2 . LEU B 2 133 ? 38.690 57.078 57.854 1.00 24.49 ? 133 LEU A CD2 1 ATOM 1048 N N . ARG B 2 134 ? 33.702 57.326 59.739 1.00 30.50 ? 134 ARG A N 1 ATOM 1049 C CA . ARG B 2 134 ? 32.417 56.655 59.744 1.00 30.60 ? 134 ARG A CA 1 ATOM 1050 C C . ARG B 2 134 ? 32.610 55.145 59.825 1.00 32.02 ? 134 ARG A C 1 ATOM 1051 O O . ARG B 2 134 ? 31.745 54.422 60.343 1.00 32.41 ? 134 ARG A O 1 ATOM 1052 C CB . ARG B 2 134 ? 31.670 57.003 58.470 1.00 27.34 ? 134 ARG A CB 1 ATOM 1053 C CG . ARG B 2 134 ? 30.622 58.052 58.647 1.00 23.42 ? 134 ARG A CG 1 ATOM 1054 C CD . ARG B 2 134 ? 30.069 58.358 57.309 1.00 21.87 ? 134 ARG A CD 1 ATOM 1055 N NE . ARG B 2 134 ? 31.003 59.183 56.568 1.00 22.89 ? 134 ARG A NE 1 ATOM 1056 C CZ . ARG B 2 134 ? 30.911 59.426 55.269 1.00 24.00 ? 134 ARG A CZ 1 ATOM 1057 N NH1 . ARG B 2 134 ? 29.923 58.893 54.559 1.00 22.60 ? 134 ARG A NH1 1 ATOM 1058 N NH2 . ARG B 2 134 ? 31.798 60.223 54.690 1.00 25.53 ? 134 ARG A NH2 1 ATOM 1059 N N . GLU B 2 135 ? 33.758 54.693 59.313 1.00 33.39 ? 135 GLU A N 1 ATOM 1060 C CA . GLU B 2 135 ? 34.124 53.278 59.266 1.00 34.26 ? 135 GLU A CA 1 ATOM 1061 C C . GLU B 2 135 ? 34.485 52.637 60.592 1.00 34.25 ? 135 GLU A C 1 ATOM 1062 O O . GLU B 2 135 ? 34.536 51.417 60.690 1.00 34.96 ? 135 GLU A O 1 ATOM 1063 C CB . GLU B 2 135 ? 35.283 53.059 58.291 1.00 33.20 ? 135 GLU A CB 1 ATOM 1064 C CG . GLU B 2 135 ? 34.902 53.241 56.842 1.00 34.45 ? 135 GLU A CG 1 ATOM 1065 C CD . GLU B 2 135 ? 35.131 54.650 56.337 1.00 35.80 ? 135 GLU A CD 1 ATOM 1066 O OE1 . GLU B 2 135 ? 35.208 55.591 57.155 1.00 35.90 ? 135 GLU A OE1 1 ATOM 1067 O OE2 . GLU B 2 135 ? 35.224 54.820 55.104 1.00 37.10 ? 135 GLU A OE2 1 ATOM 1068 N N . ASN B 2 136 ? 34.734 53.445 61.614 1.00 34.32 ? 136 ASN A N 1 ATOM 1069 C CA . ASN B 2 136 ? 35.110 52.903 62.912 1.00 34.31 ? 136 ASN A CA 1 ATOM 1070 C C . ASN B 2 136 ? 34.032 53.088 63.959 1.00 33.68 ? 136 ASN A C 1 ATOM 1071 O O . ASN B 2 136 ? 34.081 52.480 65.023 1.00 34.21 ? 136 ASN A O 1 ATOM 1072 C CB . ASN B 2 136 ? 36.413 53.547 63.363 1.00 36.33 ? 136 ASN A CB 1 ATOM 1073 C CG . ASN B 2 136 ? 37.542 53.288 62.390 1.00 38.55 ? 136 ASN A CG 1 ATOM 1074 O OD1 . ASN B 2 136 ? 38.562 53.979 62.402 1.00 40.52 ? 136 ASN A OD1 1 ATOM 1075 N ND2 . ASN B 2 136 ? 37.367 52.280 61.539 1.00 37.29 ? 136 ASN A ND2 1 ATOM 1076 N N . ILE B 2 137 ? 33.055 53.929 63.645 1.00 32.80 ? 137 ILE A N 1 ATOM 1077 C CA . ILE B 2 137 ? 31.936 54.191 64.542 1.00 31.21 ? 137 ILE A CA 1 ATOM 1078 C C . ILE B 2 137 ? 30.908 53.087 64.286 1.00 32.18 ? 137 ILE A C 1 ATOM 1079 O O . ILE B 2 137 ? 30.381 52.979 63.178 1.00 32.47 ? 137 ILE A O 1 ATOM 1080 C CB . ILE B 2 137 ? 31.304 55.566 64.230 1.00 29.34 ? 137 ILE A CB 1 ATOM 1081 C CG1 . ILE B 2 137 ? 32.360 56.667 64.382 1.00 27.57 ? 137 ILE A CG1 1 ATOM 1082 C CG2 . ILE B 2 137 ? 30.115 55.813 65.132 1.00 28.12 ? 137 ILE A CG2 1 ATOM 1083 C CD1 . ILE B 2 137 ? 31.916 58.018 63.877 1.00 27.12 ? 137 ILE A CD1 1 ATOM 1084 N N . GLU B 2 138 ? 30.638 52.260 65.295 1.00 32.26 ? 138 GLU A N 1 ATOM 1085 C CA . GLU B 2 138 ? 29.682 51.167 65.139 1.00 32.98 ? 138 GLU A CA 1 ATOM 1086 C C . GLU B 2 138 ? 28.253 51.670 65.169 1.00 32.22 ? 138 GLU A C 1 ATOM 1087 O O . GLU B 2 138 ? 27.951 52.689 65.784 1.00 33.02 ? 138 GLU A O 1 ATOM 1088 C CB . GLU B 2 138 ? 29.854 50.132 66.244 1.00 35.17 ? 138 GLU A CB 1 ATOM 1089 C CG . GLU B 2 138 ? 31.266 49.628 66.428 1.00 39.95 ? 138 GLU A CG 1 ATOM 1090 C CD . GLU B 2 138 ? 31.383 48.709 67.625 1.00 42.22 ? 138 GLU A CD 1 ATOM 1091 O OE1 . GLU B 2 138 ? 30.866 49.077 68.704 1.00 44.70 ? 138 GLU A OE1 1 ATOM 1092 O OE2 . GLU B 2 138 ? 31.990 47.627 67.491 1.00 42.39 ? 138 GLU A OE2 1 ATOM 1093 N N . LEU B 2 139 ? 27.369 50.929 64.515 1.00 30.85 ? 139 LEU A N 1 ATOM 1094 C CA . LEU B 2 139 ? 25.969 51.296 64.448 1.00 28.56 ? 139 LEU A CA 1 ATOM 1095 C C . LEU B 2 139 ? 25.095 50.150 64.942 1.00 28.88 ? 139 LEU A C 1 ATOM 1096 O O . LEU B 2 139 ? 25.502 48.993 64.914 1.00 30.33 ? 139 LEU A O 1 ATOM 1097 C CB . LEU B 2 139 ? 25.618 51.672 63.009 1.00 27.46 ? 139 LEU A CB 1 ATOM 1098 C CG . LEU B 2 139 ? 26.379 52.897 62.474 1.00 27.11 ? 139 LEU A CG 1 ATOM 1099 C CD1 . LEU B 2 139 ? 26.026 53.124 61.019 1.00 25.88 ? 139 LEU A CD1 1 ATOM 1100 C CD2 . LEU B 2 139 ? 26.034 54.136 63.296 1.00 25.92 ? 139 LEU A CD2 1 ATOM 1101 N N . GLY B 2 140 ? 23.899 50.483 65.410 1.00 28.71 ? 140 GLY A N 1 ATOM 1102 C CA . GLY B 2 140 ? 22.983 49.476 65.911 1.00 29.83 ? 140 GLY A CA 1 ATOM 1103 C C . GLY B 2 140 ? 22.060 50.127 66.913 1.00 31.55 ? 140 GLY A C 1 ATOM 1104 O O . GLY B 2 140 ? 22.029 51.353 67.008 1.00 32.20 ? 140 GLY A O 1 ATOM 1105 N N . ASN B 2 141 ? 21.302 49.332 67.662 1.00 33.21 ? 141 ASN A N 1 ATOM 1106 C CA . ASN B 2 141 ? 20.407 49.914 68.650 1.00 33.91 ? 141 ASN A CA 1 ATOM 1107 C C . ASN B 2 141 ? 21.209 50.299 69.880 1.00 33.72 ? 141 ASN A C 1 ATOM 1108 O O . ASN B 2 141 ? 20.880 51.259 70.570 1.00 34.65 ? 141 ASN A O 1 ATOM 1109 C CB . ASN B 2 141 ? 19.302 48.941 69.038 1.00 36.10 ? 141 ASN A CB 1 ATOM 1110 C CG . ASN B 2 141 ? 18.163 49.633 69.761 1.00 38.09 ? 141 ASN A CG 1 ATOM 1111 O OD1 . ASN B 2 141 ? 17.542 50.554 69.222 1.00 40.66 ? 141 ASN A OD1 1 ATOM 1112 N ND2 . ASN B 2 141 ? 17.889 49.208 70.988 1.00 38.27 ? 141 ASN A ND2 1 ATOM 1113 N N . GLY B 2 142 ? 22.260 49.537 70.159 1.00 33.46 ? 142 GLY A N 1 ATOM 1114 C CA . GLY B 2 142 ? 23.099 49.853 71.297 1.00 33.29 ? 142 GLY A CA 1 ATOM 1115 C C . GLY B 2 142 ? 23.660 51.252 71.108 1.00 32.85 ? 142 GLY A C 1 ATOM 1116 O O . GLY B 2 142 ? 23.497 52.110 71.976 1.00 33.86 ? 142 GLY A O 1 ATOM 1117 N N . PRO B 2 143 ? 24.333 51.512 69.976 1.00 31.20 ? 143 PRO A N 1 ATOM 1118 C CA . PRO B 2 143 ? 24.914 52.822 69.677 1.00 30.32 ? 143 PRO A CA 1 ATOM 1119 C C . PRO B 2 143 ? 23.915 53.980 69.651 1.00 30.03 ? 143 PRO A C 1 ATOM 1120 O O . PRO B 2 143 ? 24.297 55.118 69.900 1.00 30.54 ? 143 PRO A O 1 ATOM 1121 C CB . PRO B 2 143 ? 25.574 52.597 68.322 1.00 29.49 ? 143 PRO A CB 1 ATOM 1122 C CG . PRO B 2 143 ? 26.045 51.202 68.441 1.00 31.04 ? 143 PRO A CG 1 ATOM 1123 C CD . PRO B 2 143 ? 24.844 50.500 69.036 1.00 30.71 ? 143 PRO A CD 1 ATOM 1124 N N . LEU B 2 144 ? 22.648 53.700 69.347 1.00 29.10 ? 144 LEU A N 1 ATOM 1125 C CA . LEU B 2 144 ? 21.629 54.751 69.307 1.00 28.51 ? 144 LEU A CA 1 ATOM 1126 C C . LEU B 2 144 ? 21.188 55.141 70.725 1.00 29.62 ? 144 LEU A C 1 ATOM 1127 O O . LEU B 2 144 ? 20.886 56.306 70.987 1.00 29.54 ? 144 LEU A O 1 ATOM 1128 C CB . LEU B 2 144 ? 20.423 54.297 68.473 1.00 27.20 ? 144 LEU A CB 1 ATOM 1129 C CG . LEU B 2 144 ? 19.349 55.327 68.091 1.00 25.13 ? 144 LEU A CG 1 ATOM 1130 C CD1 . LEU B 2 144 ? 19.970 56.550 67.429 1.00 24.27 ? 144 LEU A CD1 1 ATOM 1131 C CD2 . LEU B 2 144 ? 18.351 54.680 67.152 1.00 21.38 ? 144 LEU A CD2 1 ATOM 1132 N N . GLU B 2 145 ? 21.155 54.172 71.637 1.00 30.66 ? 145 GLU A N 1 ATOM 1133 C CA . GLU B 2 145 ? 20.783 54.456 73.018 1.00 33.18 ? 145 GLU A CA 1 ATOM 1134 C C . GLU B 2 145 ? 21.855 55.357 73.604 1.00 34.78 ? 145 GLU A C 1 ATOM 1135 O O . GLU B 2 145 ? 21.563 56.361 74.257 1.00 35.81 ? 145 GLU A O 1 ATOM 1136 C CB . GLU B 2 145 ? 20.710 53.177 73.853 1.00 32.69 ? 145 GLU A CB 1 ATOM 1137 C CG . GLU B 2 145 ? 19.507 52.314 73.567 1.00 38.60 ? 145 GLU A CG 1 ATOM 1138 C CD . GLU B 2 145 ? 19.114 51.435 74.750 1.00 41.54 ? 145 GLU A CD 1 ATOM 1139 O OE1 . GLU B 2 145 ? 19.854 50.462 75.056 1.00 41.72 ? 145 GLU A OE1 1 ATOM 1140 O OE2 . GLU B 2 145 ? 18.060 51.733 75.373 1.00 42.29 ? 145 GLU A OE2 1 ATOM 1141 N N . GLU B 2 146 ? 23.106 54.990 73.355 1.00 34.91 ? 146 GLU A N 1 ATOM 1142 C CA . GLU B 2 146 ? 24.244 55.741 73.857 1.00 35.83 ? 146 GLU A CA 1 ATOM 1143 C C . GLU B 2 146 ? 24.308 57.142 73.270 1.00 35.45 ? 146 GLU A C 1 ATOM 1144 O O . GLU B 2 146 ? 24.682 58.095 73.958 1.00 36.36 ? 146 GLU A O 1 ATOM 1145 C CB . GLU B 2 146 ? 25.539 54.999 73.533 1.00 37.83 ? 146 GLU A CB 1 ATOM 1146 C CG . GLU B 2 146 ? 25.491 53.518 73.841 1.00 40.75 ? 146 GLU A CG 1 ATOM 1147 C CD . GLU B 2 146 ? 26.827 52.835 73.621 1.00 43.70 ? 146 GLU A CD 1 ATOM 1148 O OE1 . GLU B 2 146 ? 27.445 53.037 72.549 1.00 44.85 ? 146 GLU A OE1 1 ATOM 1149 O OE2 . GLU B 2 146 ? 27.258 52.089 74.523 1.00 44.61 ? 146 GLU A OE2 1 ATOM 1150 N N . ALA B 2 147 ? 23.947 57.261 71.997 1.00 34.18 ? 147 ALA A N 1 ATOM 1151 C CA . ALA B 2 147 ? 23.983 58.544 71.314 1.00 33.62 ? 147 ALA A CA 1 ATOM 1152 C C . ALA B 2 147 ? 22.921 59.487 71.853 1.00 34.31 ? 147 ALA A C 1 ATOM 1153 O O . ALA B 2 147 ? 23.157 60.692 71.962 1.00 36.31 ? 147 ALA A O 1 ATOM 1154 C CB . ALA B 2 147 ? 23.802 58.346 69.821 1.00 31.49 ? 147 ALA A CB 1 ATOM 1155 N N . ILE B 2 148 ? 21.753 58.947 72.194 1.00 33.88 ? 148 ILE A N 1 ATOM 1156 C CA . ILE B 2 148 ? 20.686 59.788 72.722 1.00 32.64 ? 148 ILE A CA 1 ATOM 1157 C C . ILE B 2 148 ? 21.097 60.366 74.071 1.00 33.08 ? 148 ILE A C 1 ATOM 1158 O O . ILE B 2 148 ? 20.950 61.563 74.309 1.00 33.00 ? 148 ILE A O 1 ATOM 1159 C CB . ILE B 2 148 ? 19.366 59.011 72.883 1.00 31.10 ? 148 ILE A CB 1 ATOM 1160 C CG1 . ILE B 2 148 ? 18.939 58.424 71.537 1.00 28.63 ? 148 ILE A CG1 1 ATOM 1161 C CG2 . ILE B 2 148 ? 18.278 59.947 73.402 1.00 32.66 ? 148 ILE A CG2 1 ATOM 1162 C CD1 . ILE B 2 148 ? 17.686 57.591 71.598 1.00 25.28 ? 148 ILE A CD1 1 ATOM 1163 N N . SER B 2 149 ? 21.623 59.515 74.948 1.00 32.68 ? 149 SER A N 1 ATOM 1164 C CA . SER B 2 149 ? 22.069 59.955 76.265 1.00 32.81 ? 149 SER A CA 1 ATOM 1165 C C . SER B 2 149 ? 23.195 60.959 76.117 1.00 33.60 ? 149 SER A C 1 ATOM 1166 O O . SER B 2 149 ? 23.228 61.982 76.796 1.00 33.74 ? 149 SER A O 1 ATOM 1167 C CB . SER B 2 149 ? 22.562 58.770 77.081 1.00 31.96 ? 149 SER A CB 1 ATOM 1168 O OG . SER B 2 149 ? 21.553 57.791 77.182 1.00 33.95 ? 149 SER A OG 1 ATOM 1169 N N . ALA B 2 150 ? 24.124 60.658 75.220 1.00 35.33 ? 150 ALA A N 1 ATOM 1170 C CA . ALA B 2 150 ? 25.259 61.536 74.982 1.00 36.83 ? 150 ALA A CA 1 ATOM 1171 C C . ALA B 2 150 ? 24.771 62.910 74.537 1.00 37.71 ? 150 ALA A C 1 ATOM 1172 O O . ALA B 2 150 ? 25.272 63.935 75.000 1.00 38.43 ? 150 ALA A O 1 ATOM 1173 C CB . ALA B 2 150 ? 26.175 60.929 73.916 1.00 36.66 ? 150 ALA A CB 1 ATOM 1174 N N . LEU B 2 151 ? 23.790 62.911 73.638 1.00 38.49 ? 151 LEU A N 1 ATOM 1175 C CA . LEU B 2 151 ? 23.210 64.135 73.093 1.00 38.49 ? 151 LEU A CA 1 ATOM 1176 C C . LEU B 2 151 ? 22.442 64.896 74.155 1.00 39.73 ? 151 LEU A C 1 ATOM 1177 O O . LEU B 2 151 ? 22.492 66.127 74.219 1.00 39.47 ? 151 LEU A O 1 ATOM 1178 C CB . LEU B 2 151 ? 22.260 63.792 71.944 1.00 36.62 ? 151 LEU A CB 1 ATOM 1179 C CG . LEU B 2 151 ? 22.689 64.139 70.520 1.00 34.50 ? 151 LEU A CG 1 ATOM 1180 C CD1 . LEU B 2 151 ? 24.098 63.715 70.256 1.00 33.85 ? 151 LEU A CD1 1 ATOM 1181 C CD2 . LEU B 2 151 ? 21.768 63.444 69.571 1.00 36.02 ? 151 LEU A CD2 1 ATOM 1182 N N . TYR B 2 152 ? 21.731 64.144 74.987 1.00 41.18 ? 152 TYR A N 1 ATOM 1183 C CA . TYR B 2 152 ? 20.923 64.718 76.049 1.00 42.26 ? 152 TYR A CA 1 ATOM 1184 C C . TYR B 2 152 ? 21.756 65.446 77.092 1.00 41.97 ? 152 TYR A C 1 ATOM 1185 O O . TYR B 2 152 ? 21.476 66.597 77.428 1.00 42.53 ? 152 TYR A O 1 ATOM 1186 C CB . TYR B 2 152 ? 20.103 63.634 76.745 1.00 43.09 ? 152 TYR A CB 1 ATOM 1187 C CG . TYR B 2 152 ? 19.236 64.204 77.828 1.00 45.66 ? 152 TYR A CG 1 ATOM 1188 C CD1 . TYR B 2 152 ? 18.085 64.924 77.517 1.00 47.01 ? 152 TYR A CD1 1 ATOM 1189 C CD2 . TYR B 2 152 ? 19.612 64.115 79.163 1.00 46.69 ? 152 TYR A CD2 1 ATOM 1190 C CE1 . TYR B 2 152 ? 17.333 65.549 78.512 1.00 47.60 ? 152 TYR A CE1 1 ATOM 1191 C CE2 . TYR B 2 152 ? 18.870 64.737 80.164 1.00 47.90 ? 152 TYR A CE2 1 ATOM 1192 C CZ . TYR B 2 152 ? 17.734 65.452 79.831 1.00 47.64 ? 152 TYR A CZ 1 ATOM 1193 O OH . TYR B 2 152 ? 17.007 66.070 80.822 1.00 48.71 ? 152 TYR A OH 1 ATOM 1194 N N . TYR B 2 153 ? 22.779 64.769 77.604 1.00 42.14 ? 153 TYR A N 1 ATOM 1195 C CA . TYR B 2 153 ? 23.644 65.343 78.626 1.00 41.62 ? 153 TYR A CA 1 ATOM 1196 C C . TYR B 2 153 ? 24.528 66.489 78.168 1.00 41.29 ? 153 TYR A C 1 ATOM 1197 O O . TYR B 2 153 ? 25.139 67.165 78.990 1.00 40.94 ? 153 TYR A O 1 ATOM 1198 C CB . TYR B 2 153 ? 24.509 64.254 79.250 1.00 41.49 ? 153 TYR A CB 1 ATOM 1199 C CG . TYR B 2 153 ? 23.714 63.297 80.099 1.00 41.79 ? 153 TYR A CG 1 ATOM 1200 C CD1 . TYR B 2 153 ? 22.870 63.770 81.102 1.00 42.70 ? 153 TYR A CD1 1 ATOM 1201 C CD2 . TYR B 2 153 ? 23.807 61.923 79.909 1.00 42.20 ? 153 TYR A CD2 1 ATOM 1202 C CE1 . TYR B 2 153 ? 22.137 62.898 81.896 1.00 43.57 ? 153 TYR A CE1 1 ATOM 1203 C CE2 . TYR B 2 153 ? 23.081 61.041 80.698 1.00 43.92 ? 153 TYR A CE2 1 ATOM 1204 C CZ . TYR B 2 153 ? 22.248 61.535 81.690 1.00 44.36 ? 153 TYR A CZ 1 ATOM 1205 O OH . TYR B 2 153 ? 21.538 60.661 82.480 1.00 45.87 ? 153 TYR A OH 1 ATOM 1206 N N . TYR B 2 154 ? 24.608 66.722 76.866 1.00 40.94 ? 154 TYR A N 1 ATOM 1207 C CA . TYR B 2 154 ? 25.433 67.818 76.399 1.00 41.20 ? 154 TYR A CA 1 ATOM 1208 C C . TYR B 2 154 ? 24.855 69.141 76.885 1.00 43.70 ? 154 TYR A C 1 ATOM 1209 O O . TYR B 2 154 ? 25.588 70.121 77.035 1.00 46.27 ? 154 TYR A O 1 ATOM 1210 C CB . TYR B 2 154 ? 25.520 67.847 74.880 1.00 36.78 ? 154 TYR A CB 1 ATOM 1211 C CG . TYR B 2 154 ? 26.474 68.905 74.395 1.00 33.05 ? 154 TYR A CG 1 ATOM 1212 C CD1 . TYR B 2 154 ? 27.838 68.807 74.656 1.00 32.15 ? 154 TYR A CD1 1 ATOM 1213 C CD2 . TYR B 2 154 ? 26.017 70.020 73.710 1.00 31.32 ? 154 TYR A CD2 1 ATOM 1214 C CE1 . TYR B 2 154 ? 28.723 69.796 74.247 1.00 29.69 ? 154 TYR A CE1 1 ATOM 1215 C CE2 . TYR B 2 154 ? 26.898 71.015 73.295 1.00 30.55 ? 154 TYR A CE2 1 ATOM 1216 C CZ . TYR B 2 154 ? 28.246 70.894 73.569 1.00 29.17 ? 154 TYR A CZ 1 ATOM 1217 O OH . TYR B 2 154 ? 29.118 71.877 73.168 1.00 29.36 ? 154 TYR A OH 1 ATOM 1218 N N . SER B 2 155 ? 23.544 69.172 77.130 1.00 45.87 ? 155 SER A N 1 ATOM 1219 C CA . SER B 2 155 ? 22.887 70.390 77.606 1.00 46.76 ? 155 SER A CA 1 ATOM 1220 C C . SER B 2 155 ? 23.252 70.688 79.067 1.00 47.45 ? 155 SER A C 1 ATOM 1221 O O . SER B 2 155 ? 23.300 71.848 79.479 1.00 47.81 ? 155 SER A O 1 ATOM 1222 C CB . SER B 2 155 ? 21.360 70.278 77.455 1.00 47.27 ? 155 SER A CB 1 ATOM 1223 O OG . SER B 2 155 ? 20.816 69.261 78.284 1.00 46.54 ? 155 SER A OG 1 ATOM 1224 N N . THR B 2 156 ? 23.518 69.638 79.843 1.00 47.51 ? 156 THR A N 1 ATOM 1225 C CA . THR B 2 156 ? 23.885 69.806 81.248 1.00 47.01 ? 156 THR A CA 1 ATOM 1226 C C . THR B 2 156 ? 25.408 69.891 81.390 1.00 47.36 ? 156 THR A C 1 ATOM 1227 O O . THR B 2 156 ? 25.932 70.050 82.489 1.00 47.48 ? 156 THR A O 1 ATOM 1228 C CB . THR B 2 156 ? 23.371 68.636 82.124 1.00 46.31 ? 156 THR A CB 1 ATOM 1229 O OG1 . THR B 2 156 ? 24.366 67.606 82.191 1.00 46.00 ? 156 THR A OG1 1 ATOM 1230 C CG2 . THR B 2 156 ? 22.089 68.058 81.541 1.00 45.90 ? 156 THR A CG2 1 ATOM 1231 N N . GLY B 2 157 ? 26.115 69.766 80.272 1.00 47.00 ? 157 GLY A N 1 ATOM 1232 C CA . GLY B 2 157 ? 27.564 69.855 80.301 1.00 47.59 ? 157 GLY A CA 1 ATOM 1233 C C . GLY B 2 157 ? 28.363 68.587 80.558 1.00 47.66 ? 157 GLY A C 1 ATOM 1234 O O . GLY B 2 157 ? 29.571 68.666 80.755 1.00 48.87 ? 157 GLY A O 1 ATOM 1235 N N . GLY B 2 158 ? 27.723 67.423 80.549 1.00 47.52 ? 158 GLY A N 1 ATOM 1236 C CA . GLY B 2 158 ? 28.458 66.192 80.793 1.00 46.73 ? 158 GLY A CA 1 ATOM 1237 C C . GLY B 2 158 ? 28.695 65.317 79.572 1.00 47.23 ? 158 GLY A C 1 ATOM 1238 O O . GLY B 2 158 ? 28.530 64.097 79.643 1.00 49.10 ? 158 GLY A O 1 ATOM 1239 N N . THR B 2 159 ? 29.075 65.928 78.451 1.00 46.57 ? 159 THR A N 1 ATOM 1240 C CA . THR B 2 159 ? 29.343 65.199 77.206 1.00 44.92 ? 159 THR A CA 1 ATOM 1241 C C . THR B 2 159 ? 30.455 65.951 76.492 1.00 45.12 ? 159 THR A C 1 ATOM 1242 O O . THR B 2 159 ? 30.261 67.097 76.095 1.00 46.07 ? 159 THR A O 1 ATOM 1243 C CB . THR B 2 159 ? 28.114 65.178 76.258 1.00 43.92 ? 159 THR A CB 1 ATOM 1244 O OG1 . THR B 2 159 ? 26.991 64.596 76.925 1.00 43.96 ? 159 THR A OG1 1 ATOM 1245 C CG2 . THR B 2 159 ? 28.421 64.364 75.007 1.00 43.29 ? 159 THR A CG2 1 ATOM 1246 N N . GLN B 2 160 ? 31.613 65.317 76.329 1.00 45.00 ? 160 GLN A N 1 ATOM 1247 C CA . GLN B 2 160 ? 32.737 65.968 75.657 1.00 44.50 ? 160 GLN A CA 1 ATOM 1248 C C . GLN B 2 160 ? 32.436 66.147 74.164 1.00 42.37 ? 160 GLN A C 1 ATOM 1249 O O . GLN B 2 160 ? 31.692 65.364 73.575 1.00 42.74 ? 160 GLN A O 1 ATOM 1250 C CB . GLN B 2 160 ? 34.016 65.143 75.843 1.00 47.27 ? 160 GLN A CB 1 ATOM 1251 C CG . GLN B 2 160 ? 34.347 64.799 77.302 1.00 51.32 ? 160 GLN A CG 1 ATOM 1252 C CD . GLN B 2 160 ? 34.526 66.030 78.185 1.00 54.31 ? 160 GLN A CD 1 ATOM 1253 O OE1 . GLN B 2 160 ? 35.362 66.896 77.904 1.00 55.57 ? 160 GLN A OE1 1 ATOM 1254 N NE2 . GLN B 2 160 ? 33.742 66.110 79.262 1.00 54.58 ? 160 GLN A NE2 1 ATOM 1255 N N . LEU B 2 161 ? 33.015 67.173 73.553 1.00 39.77 ? 161 LEU A N 1 ATOM 1256 C CA . LEU B 2 161 ? 32.784 67.441 72.138 1.00 37.35 ? 161 LEU A CA 1 ATOM 1257 C C . LEU B 2 161 ? 33.089 66.259 71.205 1.00 36.51 ? 161 LEU A C 1 ATOM 1258 O O . LEU B 2 161 ? 32.376 66.040 70.221 1.00 37.02 ? 161 LEU A O 1 ATOM 1259 C CB . LEU B 2 161 ? 33.588 68.665 71.707 1.00 35.44 ? 161 LEU A CB 1 ATOM 1260 C CG . LEU B 2 161 ? 33.197 69.245 70.352 1.00 34.09 ? 161 LEU A CG 1 ATOM 1261 C CD1 . LEU B 2 161 ? 31.687 69.427 70.302 1.00 34.22 ? 161 LEU A CD1 1 ATOM 1262 C CD2 . LEU B 2 161 ? 33.909 70.572 70.141 1.00 33.54 ? 161 LEU A CD2 1 ATOM 1263 N N . PRO B 2 162 ? 34.162 65.495 71.482 1.00 35.09 ? 162 PRO A N 1 ATOM 1264 C CA . PRO B 2 162 ? 34.446 64.365 70.594 1.00 34.41 ? 162 PRO A CA 1 ATOM 1265 C C . PRO B 2 162 ? 33.279 63.368 70.540 1.00 33.51 ? 162 PRO A C 1 ATOM 1266 O O . PRO B 2 162 ? 32.987 62.801 69.483 1.00 32.85 ? 162 PRO A O 1 ATOM 1267 C CB . PRO B 2 162 ? 35.702 63.752 71.212 1.00 32.94 ? 162 PRO A CB 1 ATOM 1268 C CG . PRO B 2 162 ? 36.402 64.928 71.757 1.00 32.59 ? 162 PRO A CG 1 ATOM 1269 C CD . PRO B 2 162 ? 35.281 65.707 72.416 1.00 34.53 ? 162 PRO A CD 1 ATOM 1270 N N . THR B 2 163 ? 32.616 63.168 71.682 1.00 31.83 ? 163 THR A N 1 ATOM 1271 C CA . THR B 2 163 ? 31.490 62.231 71.794 1.00 30.33 ? 163 THR A CA 1 ATOM 1272 C C . THR B 2 163 ? 30.181 62.772 71.229 1.00 30.67 ? 163 THR A C 1 ATOM 1273 O O . THR B 2 163 ? 29.325 62.007 70.785 1.00 29.84 ? 163 THR A O 1 ATOM 1274 C CB . THR B 2 163 ? 31.263 61.816 73.260 1.00 29.82 ? 163 THR A CB 1 ATOM 1275 O OG1 . THR B 2 163 ? 32.397 61.066 73.717 1.00 28.39 ? 163 THR A OG1 1 ATOM 1276 C CG2 . THR B 2 163 ? 30.001 60.962 73.394 1.00 29.08 ? 163 THR A CG2 1 ATOM 1277 N N . LEU B 2 164 ? 30.010 64.088 71.260 1.00 31.47 ? 164 LEU A N 1 ATOM 1278 C CA . LEU B 2 164 ? 28.804 64.676 70.704 1.00 30.69 ? 164 LEU A CA 1 ATOM 1279 C C . LEU B 2 164 ? 28.867 64.379 69.209 1.00 31.29 ? 164 LEU A C 1 ATOM 1280 O O . LEU B 2 164 ? 27.916 63.847 68.640 1.00 33.24 ? 164 LEU A O 1 ATOM 1281 C CB . LEU B 2 164 ? 28.769 66.188 70.937 1.00 28.63 ? 164 LEU A CB 1 ATOM 1282 C CG . LEU B 2 164 ? 27.493 66.896 70.474 1.00 27.23 ? 164 LEU A CG 1 ATOM 1283 C CD1 . LEU B 2 164 ? 26.329 66.539 71.395 1.00 26.09 ? 164 LEU A CD1 1 ATOM 1284 C CD2 . LEU B 2 164 ? 27.719 68.387 70.476 1.00 26.84 ? 164 LEU A CD2 1 ATOM 1285 N N . ALA B 2 165 ? 30.006 64.693 68.589 1.00 30.67 ? 165 ALA A N 1 ATOM 1286 C CA . ALA B 2 165 ? 30.212 64.467 67.161 1.00 30.17 ? 165 ALA A CA 1 ATOM 1287 C C . ALA B 2 165 ? 30.098 62.996 66.757 1.00 30.88 ? 165 ALA A C 1 ATOM 1288 O O . ALA B 2 165 ? 29.692 62.688 65.642 1.00 30.99 ? 165 ALA A O 1 ATOM 1289 C CB . ALA B 2 165 ? 31.567 65.017 66.746 1.00 30.59 ? 165 ALA A CB 1 ATOM 1290 N N . ARG B 2 166 ? 30.465 62.086 67.649 1.00 33.17 ? 166 ARG A N 1 ATOM 1291 C CA . ARG B 2 166 ? 30.364 60.658 67.358 1.00 35.72 ? 166 ARG A CA 1 ATOM 1292 C C . ARG B 2 166 ? 28.889 60.245 67.435 1.00 38.02 ? 166 ARG A C 1 ATOM 1293 O O . ARG B 2 166 ? 28.475 59.262 66.820 1.00 39.89 ? 166 ARG A O 1 ATOM 1294 C CB . ARG B 2 166 ? 31.181 59.857 68.378 1.00 36.83 ? 166 ARG A CB 1 ATOM 1295 C CG . ARG B 2 166 ? 31.154 58.345 68.212 1.00 37.05 ? 166 ARG A CG 1 ATOM 1296 C CD . ARG B 2 166 ? 31.761 57.674 69.442 1.00 40.59 ? 166 ARG A CD 1 ATOM 1297 N NE . ARG B 2 166 ? 31.737 56.210 69.380 1.00 45.88 ? 166 ARG A NE 1 ATOM 1298 C CZ . ARG B 2 166 ? 32.557 55.468 68.634 1.00 49.89 ? 166 ARG A CZ 1 ATOM 1299 N NH1 . ARG B 2 166 ? 33.483 56.048 67.875 1.00 52.44 ? 166 ARG A NH1 1 ATOM 1300 N NH2 . ARG B 2 166 ? 32.454 54.140 68.646 1.00 50.86 ? 166 ARG A NH2 1 ATOM 1301 N N . SER B 2 167 ? 28.097 61.004 68.192 1.00 38.51 ? 167 SER A N 1 ATOM 1302 C CA . SER B 2 167 ? 26.668 60.720 68.349 1.00 37.83 ? 167 SER A CA 1 ATOM 1303 C C . SER B 2 167 ? 25.862 61.288 67.183 1.00 37.24 ? 167 SER A C 1 ATOM 1304 O O . SER B 2 167 ? 24.825 60.743 66.810 1.00 37.91 ? 167 SER A O 1 ATOM 1305 C CB . SER B 2 167 ? 26.156 61.296 69.675 1.00 37.32 ? 167 SER A CB 1 ATOM 1306 O OG . SER B 2 167 ? 26.801 60.693 70.784 1.00 35.96 ? 167 SER A OG 1 ATOM 1307 N N . PHE B 2 168 ? 26.336 62.390 66.618 1.00 36.51 ? 168 PHE A N 1 ATOM 1308 C CA . PHE B 2 168 ? 25.669 62.991 65.476 1.00 36.21 ? 168 PHE A CA 1 ATOM 1309 C C . PHE B 2 168 ? 25.876 62.097 64.258 1.00 35.05 ? 168 PHE A C 1 ATOM 1310 O O . PHE B 2 168 ? 24.977 61.935 63.443 1.00 36.40 ? 168 PHE A O 1 ATOM 1311 C CB . PHE B 2 168 ? 26.222 64.390 65.197 1.00 36.74 ? 168 PHE A CB 1 ATOM 1312 C CG . PHE B 2 168 ? 25.446 65.486 65.859 1.00 38.85 ? 168 PHE A CG 1 ATOM 1313 C CD1 . PHE B 2 168 ? 24.076 65.608 65.643 1.00 40.25 ? 168 PHE A CD1 1 ATOM 1314 C CD2 . PHE B 2 168 ? 26.080 66.412 66.674 1.00 40.27 ? 168 PHE A CD2 1 ATOM 1315 C CE1 . PHE B 2 168 ? 23.342 66.641 66.227 1.00 41.57 ? 168 PHE A CE1 1 ATOM 1316 C CE2 . PHE B 2 168 ? 25.361 67.451 67.265 1.00 42.38 ? 168 PHE A CE2 1 ATOM 1317 C CZ . PHE B 2 168 ? 23.985 67.567 67.040 1.00 41.88 ? 168 PHE A CZ 1 ATOM 1318 N N . ILE B 2 169 ? 27.058 61.507 64.142 1.00 32.81 ? 169 ILE A N 1 ATOM 1319 C CA . ILE B 2 169 ? 27.354 60.619 63.026 1.00 31.41 ? 169 ILE A CA 1 ATOM 1320 C C . ILE B 2 169 ? 26.477 59.360 63.093 1.00 31.33 ? 169 ILE A C 1 ATOM 1321 O O . ILE B 2 169 ? 26.108 58.792 62.066 1.00 31.41 ? 169 ILE A O 1 ATOM 1322 C CB . ILE B 2 169 ? 28.858 60.212 63.024 1.00 30.11 ? 169 ILE A CB 1 ATOM 1323 C CG1 . ILE B 2 169 ? 29.716 61.437 62.702 1.00 27.55 ? 169 ILE A CG1 1 ATOM 1324 C CG2 . ILE B 2 169 ? 29.109 59.089 62.014 1.00 30.36 ? 169 ILE A CG2 1 ATOM 1325 C CD1 . ILE B 2 169 ? 31.176 61.156 62.684 1.00 26.39 ? 169 ILE A CD1 1 ATOM 1326 N N . ILE B 2 170 ? 26.142 58.929 64.307 1.00 30.62 ? 170 ILE A N 1 ATOM 1327 C CA . ILE B 2 170 ? 25.317 57.743 64.488 1.00 29.27 ? 170 ILE A CA 1 ATOM 1328 C C . ILE B 2 170 ? 23.863 58.033 64.142 1.00 30.22 ? 170 ILE A C 1 ATOM 1329 O O . ILE B 2 170 ? 23.237 57.287 63.389 1.00 32.60 ? 170 ILE A O 1 ATOM 1330 C CB . ILE B 2 170 ? 25.387 57.209 65.938 1.00 26.16 ? 170 ILE A CB 1 ATOM 1331 C CG1 . ILE B 2 170 ? 26.825 56.795 66.268 1.00 24.23 ? 170 ILE A CG1 1 ATOM 1332 C CG2 . ILE B 2 170 ? 24.426 56.030 66.105 1.00 26.21 ? 170 ILE A CG2 1 ATOM 1333 C CD1 . ILE B 2 170 ? 26.999 56.133 67.612 1.00 19.20 ? 170 ILE A CD1 1 ATOM 1334 N N . CYS B 2 171 ? 23.323 59.122 64.674 1.00 27.84 ? 171 CYS A N 1 ATOM 1335 C CA . CYS B 2 171 ? 21.937 59.457 64.397 1.00 24.85 ? 171 CYS A CA 1 ATOM 1336 C C . CYS B 2 171 ? 21.705 59.775 62.931 1.00 23.37 ? 171 CYS A C 1 ATOM 1337 O O . CYS B 2 171 ? 20.725 59.321 62.342 1.00 23.53 ? 171 CYS A O 1 ATOM 1338 C CB . CYS B 2 171 ? 21.497 60.638 65.254 1.00 24.58 ? 171 CYS A CB 1 ATOM 1339 S SG . CYS B 2 171 ? 21.454 60.287 67.006 1.00 26.41 ? 171 CYS A SG 1 ATOM 1340 N N . ILE B 2 172 ? 22.603 60.552 62.339 1.00 20.75 ? 172 ILE A N 1 ATOM 1341 C CA . ILE B 2 172 ? 22.450 60.926 60.942 1.00 20.47 ? 172 ILE A CA 1 ATOM 1342 C C . ILE B 2 172 ? 22.356 59.699 60.053 1.00 22.18 ? 172 ILE A C 1 ATOM 1343 O O . ILE B 2 172 ? 21.498 59.625 59.184 1.00 24.58 ? 172 ILE A O 1 ATOM 1344 C CB . ILE B 2 172 ? 23.610 61.816 60.463 1.00 17.76 ? 172 ILE A CB 1 ATOM 1345 C CG1 . ILE B 2 172 ? 23.590 63.144 61.233 1.00 17.63 ? 172 ILE A CG1 1 ATOM 1346 C CG2 . ILE B 2 172 ? 23.488 62.071 58.974 1.00 16.86 ? 172 ILE A CG2 1 ATOM 1347 C CD1 . ILE B 2 172 ? 24.808 64.027 60.997 1.00 17.31 ? 172 ILE A CD1 1 ATOM 1348 N N . GLN B 2 173 ? 23.220 58.721 60.283 1.00 22.31 ? 173 GLN A N 1 ATOM 1349 C CA . GLN B 2 173 ? 23.217 57.505 59.479 1.00 22.18 ? 173 GLN A CA 1 ATOM 1350 C C . GLN B 2 173 ? 22.006 56.592 59.690 1.00 21.65 ? 173 GLN A C 1 ATOM 1351 O O . GLN B 2 173 ? 21.482 56.009 58.742 1.00 21.06 ? 173 GLN A O 1 ATOM 1352 C CB . GLN B 2 173 ? 24.509 56.723 59.733 1.00 22.30 ? 173 GLN A CB 1 ATOM 1353 C CG . GLN B 2 173 ? 25.733 57.392 59.144 1.00 23.41 ? 173 GLN A CG 1 ATOM 1354 C CD . GLN B 2 173 ? 26.993 56.562 59.283 1.00 23.49 ? 173 GLN A CD 1 ATOM 1355 O OE1 . GLN B 2 173 ? 27.614 56.498 60.354 1.00 24.22 ? 173 GLN A OE1 1 ATOM 1356 N NE2 . GLN B 2 173 ? 27.375 55.913 58.196 1.00 21.70 ? 173 GLN A NE2 1 ATOM 1357 N N . MET B 2 174 ? 21.555 56.468 60.929 1.00 21.54 ? 174 MET A N 1 ATOM 1358 C CA . MET B 2 174 ? 20.419 55.604 61.230 1.00 21.37 ? 174 MET A CA 1 ATOM 1359 C C . MET B 2 174 ? 19.037 56.205 60.961 1.00 21.51 ? 174 MET A C 1 ATOM 1360 O O . MET B 2 174 ? 18.035 55.492 60.939 1.00 20.73 ? 174 MET A O 1 ATOM 1361 C CB . MET B 2 174 ? 20.489 55.149 62.687 1.00 20.32 ? 174 MET A CB 1 ATOM 1362 C CG . MET B 2 174 ? 21.700 54.309 63.020 1.00 17.64 ? 174 MET A CG 1 ATOM 1363 S SD . MET B 2 174 ? 21.489 53.544 64.617 1.00 16.95 ? 174 MET A SD 1 ATOM 1364 C CE . MET B 2 174 ? 20.649 51.992 64.195 1.00 14.42 ? 174 MET A CE 1 ATOM 1365 N N . ILE B 2 175 ? 18.981 57.509 60.740 1.00 20.47 ? 175 ILE A N 1 ATOM 1366 C CA . ILE B 2 175 ? 17.707 58.156 60.497 1.00 19.38 ? 175 ILE A CA 1 ATOM 1367 C C . ILE B 2 175 ? 17.647 58.785 59.117 1.00 20.12 ? 175 ILE A C 1 ATOM 1368 O O . ILE B 2 175 ? 16.811 58.412 58.307 1.00 19.94 ? 175 ILE A O 1 ATOM 1369 C CB . ILE B 2 175 ? 17.449 59.216 61.584 1.00 18.00 ? 175 ILE A CB 1 ATOM 1370 C CG1 . ILE B 2 175 ? 17.484 58.528 62.949 1.00 17.91 ? 175 ILE A CG1 1 ATOM 1371 C CG2 . ILE B 2 175 ? 16.116 59.903 61.358 1.00 15.81 ? 175 ILE A CG2 1 ATOM 1372 C CD1 . ILE B 2 175 ? 17.232 59.432 64.098 1.00 21.02 ? 175 ILE A CD1 1 ATOM 1373 N N . SER B 2 176 ? 18.546 59.726 58.850 1.00 20.51 ? 176 SER A N 1 ATOM 1374 C CA . SER B 2 176 ? 18.584 60.412 57.566 1.00 22.23 ? 176 SER A CA 1 ATOM 1375 C C . SER B 2 176 ? 19.100 59.584 56.414 1.00 23.62 ? 176 SER A C 1 ATOM 1376 O O . SER B 2 176 ? 18.579 59.692 55.311 1.00 27.29 ? 176 SER A O 1 ATOM 1377 C CB . SER B 2 176 ? 19.420 61.683 57.659 1.00 23.18 ? 176 SER A CB 1 ATOM 1378 O OG . SER B 2 176 ? 18.715 62.683 58.362 1.00 25.90 ? 176 SER A OG 1 ATOM 1379 N N . GLU B 2 177 ? 20.128 58.773 56.644 1.00 22.66 ? 177 GLU A N 1 ATOM 1380 C CA . GLU B 2 177 ? 20.665 57.946 55.572 1.00 21.72 ? 177 GLU A CA 1 ATOM 1381 C C . GLU B 2 177 ? 19.794 56.719 55.372 1.00 20.74 ? 177 GLU A C 1 ATOM 1382 O O . GLU B 2 177 ? 19.749 56.160 54.282 1.00 21.90 ? 177 GLU A O 1 ATOM 1383 C CB . GLU B 2 177 ? 22.104 57.529 55.877 1.00 21.79 ? 177 GLU A CB 1 ATOM 1384 C CG . GLU B 2 177 ? 23.083 58.699 55.924 1.00 26.30 ? 177 GLU A CG 1 ATOM 1385 C CD . GLU B 2 177 ? 23.324 59.342 54.561 1.00 28.39 ? 177 GLU A CD 1 ATOM 1386 O OE1 . GLU B 2 177 ? 22.352 59.614 53.815 1.00 28.96 ? 177 GLU A OE1 1 ATOM 1387 O OE2 . GLU B 2 177 ? 24.500 59.591 54.234 1.00 28.95 ? 177 GLU A OE2 1 ATOM 1388 N N . ALA B 2 178 ? 19.094 56.314 56.428 1.00 20.25 ? 178 ALA A N 1 ATOM 1389 C CA . ALA B 2 178 ? 18.212 55.149 56.383 1.00 20.58 ? 178 ALA A CA 1 ATOM 1390 C C . ALA B 2 178 ? 16.918 55.482 55.646 1.00 21.28 ? 178 ALA A C 1 ATOM 1391 O O . ALA B 2 178 ? 16.295 54.616 55.030 1.00 22.38 ? 178 ALA A O 1 ATOM 1392 C CB . ALA B 2 178 ? 17.897 54.671 57.806 1.00 18.10 ? 178 ALA A CB 1 ATOM 1393 N N . ALA B 2 179 ? 16.512 56.742 55.717 1.00 21.70 ? 179 ALA A N 1 ATOM 1394 C CA . ALA B 2 179 ? 15.298 57.182 55.055 1.00 22.41 ? 179 ALA A CA 1 ATOM 1395 C C . ALA B 2 179 ? 15.590 57.378 53.572 1.00 23.36 ? 179 ALA A C 1 ATOM 1396 O O . ALA B 2 179 ? 14.700 57.269 52.734 1.00 25.58 ? 179 ALA A O 1 ATOM 1397 C CB . ALA B 2 179 ? 14.804 58.488 55.680 1.00 22.25 ? 179 ALA A CB 1 ATOM 1398 N N . ARG B 2 180 ? 16.845 57.658 53.251 1.00 22.54 ? 180 ARG A N 1 ATOM 1399 C CA . ARG B 2 180 ? 17.240 57.881 51.865 1.00 22.64 ? 180 ARG A CA 1 ATOM 1400 C C . ARG B 2 180 ? 17.476 56.610 51.051 1.00 22.95 ? 180 ARG A C 1 ATOM 1401 O O . ARG B 2 180 ? 17.277 56.605 49.835 1.00 23.89 ? 180 ARG A O 1 ATOM 1402 C CB . ARG B 2 180 ? 18.506 58.731 51.812 1.00 21.34 ? 180 ARG A CB 1 ATOM 1403 C CG . ARG B 2 180 ? 18.340 60.146 52.280 1.00 20.43 ? 180 ARG A CG 1 ATOM 1404 C CD . ARG B 2 180 ? 19.696 60.789 52.300 1.00 21.84 ? 180 ARG A CD 1 ATOM 1405 N NE . ARG B 2 180 ? 19.699 62.105 52.920 1.00 22.38 ? 180 ARG A NE 1 ATOM 1406 C CZ . ARG B 2 180 ? 20.807 62.721 53.314 1.00 23.33 ? 180 ARG A CZ 1 ATOM 1407 N NH1 . ARG B 2 180 ? 21.990 62.131 53.150 1.00 24.93 ? 180 ARG A NH1 1 ATOM 1408 N NH2 . ARG B 2 180 ? 20.739 63.921 53.871 1.00 22.16 ? 180 ARG A NH2 1 ATOM 1409 N N . PHE B 2 181 ? 17.905 55.535 51.706 1.00 21.59 ? 181 PHE A N 1 ATOM 1410 C CA . PHE B 2 181 ? 18.173 54.295 50.985 1.00 19.23 ? 181 PHE A CA 1 ATOM 1411 C C . PHE B 2 181 ? 17.559 53.075 51.648 1.00 19.14 ? 181 PHE A C 1 ATOM 1412 O O . PHE B 2 181 ? 17.732 52.866 52.843 1.00 18.59 ? 181 PHE A O 1 ATOM 1413 C CB . PHE B 2 181 ? 19.679 54.060 50.864 1.00 17.45 ? 181 PHE A CB 1 ATOM 1414 C CG . PHE B 2 181 ? 20.432 55.163 50.167 1.00 14.51 ? 181 PHE A CG 1 ATOM 1415 C CD1 . PHE B 2 181 ? 20.942 56.236 50.883 1.00 11.61 ? 181 PHE A CD1 1 ATOM 1416 C CD2 . PHE B 2 181 ? 20.696 55.084 48.803 1.00 13.19 ? 181 PHE A CD2 1 ATOM 1417 C CE1 . PHE B 2 181 ? 21.715 57.211 50.256 1.00 12.71 ? 181 PHE A CE1 1 ATOM 1418 C CE2 . PHE B 2 181 ? 21.464 56.051 48.169 1.00 14.00 ? 181 PHE A CE2 1 ATOM 1419 C CZ . PHE B 2 181 ? 21.979 57.121 48.900 1.00 13.50 ? 181 PHE A CZ 1 ATOM 1420 N N . GLN B 2 182 ? 16.850 52.262 50.870 1.00 19.58 ? 182 GLN A N 1 ATOM 1421 C CA . GLN B 2 182 ? 16.248 51.050 51.410 1.00 20.41 ? 182 GLN A CA 1 ATOM 1422 C C . GLN B 2 182 ? 17.389 50.114 51.726 1.00 21.15 ? 182 GLN A C 1 ATOM 1423 O O . GLN B 2 182 ? 17.278 49.238 52.576 1.00 21.88 ? 182 GLN A O 1 ATOM 1424 C CB . GLN B 2 182 ? 15.324 50.374 50.397 1.00 20.45 ? 182 GLN A CB 1 ATOM 1425 C CG . GLN B 2 182 ? 14.130 51.188 49.994 1.00 23.45 ? 182 GLN A CG 1 ATOM 1426 C CD . GLN B 2 182 ? 14.382 51.945 48.730 1.00 25.45 ? 182 GLN A CD 1 ATOM 1427 O OE1 . GLN B 2 182 ? 15.285 52.769 48.662 1.00 28.39 ? 182 GLN A OE1 1 ATOM 1428 N NE2 . GLN B 2 182 ? 13.592 51.664 47.706 1.00 27.25 ? 182 GLN A NE2 1 ATOM 1429 N N . TYR B 2 183 ? 18.496 50.302 51.026 1.00 21.73 ? 183 TYR A N 1 ATOM 1430 C CA . TYR B 2 183 ? 19.658 49.466 51.248 1.00 22.56 ? 183 TYR A CA 1 ATOM 1431 C C . TYR B 2 183 ? 20.206 49.734 52.646 1.00 22.00 ? 183 TYR A C 1 ATOM 1432 O O . TYR B 2 183 ? 20.499 48.795 53.387 1.00 24.02 ? 183 TYR A O 1 ATOM 1433 C CB . TYR B 2 183 ? 20.734 49.752 50.193 1.00 22.84 ? 183 TYR A CB 1 ATOM 1434 C CG . TYR B 2 183 ? 21.978 48.917 50.364 1.00 22.48 ? 183 TYR A CG 1 ATOM 1435 C CD1 . TYR B 2 183 ? 22.038 47.614 49.896 1.00 23.21 ? 183 TYR A CD1 1 ATOM 1436 C CD2 . TYR B 2 183 ? 23.079 49.422 51.040 1.00 24.23 ? 183 TYR A CD2 1 ATOM 1437 C CE1 . TYR B 2 183 ? 23.171 46.834 50.099 1.00 25.00 ? 183 TYR A CE1 1 ATOM 1438 C CE2 . TYR B 2 183 ? 24.210 48.656 51.252 1.00 24.93 ? 183 TYR A CE2 1 ATOM 1439 C CZ . TYR B 2 183 ? 24.253 47.367 50.781 1.00 24.63 ? 183 TYR A CZ 1 ATOM 1440 O OH . TYR B 2 183 ? 25.380 46.622 51.001 1.00 24.97 ? 183 TYR A OH 1 ATOM 1441 N N . ILE B 2 184 ? 20.330 51.010 53.012 1.00 20.31 ? 184 ILE A N 1 ATOM 1442 C CA . ILE B 2 184 ? 20.851 51.377 54.328 1.00 17.35 ? 184 ILE A CA 1 ATOM 1443 C C . ILE B 2 184 ? 19.838 51.109 55.440 1.00 19.37 ? 184 ILE A C 1 ATOM 1444 O O . ILE B 2 184 ? 20.219 50.871 56.586 1.00 19.61 ? 184 ILE A O 1 ATOM 1445 C CB . ILE B 2 184 ? 21.305 52.842 54.347 1.00 13.85 ? 184 ILE A CB 1 ATOM 1446 C CG1 . ILE B 2 184 ? 22.326 53.050 53.215 1.00 11.53 ? 184 ILE A CG1 1 ATOM 1447 C CG2 . ILE B 2 184 ? 21.907 53.182 55.699 1.00 10.30 ? 184 ILE A CG2 1 ATOM 1448 C CD1 . ILE B 2 184 ? 22.851 54.464 53.041 1.00 10.90 ? 184 ILE A CD1 1 ATOM 1449 N N . GLU B 2 185 ? 18.548 51.131 55.103 1.00 21.30 ? 185 GLU A N 1 ATOM 1450 C CA . GLU B 2 185 ? 17.505 50.835 56.087 1.00 23.05 ? 185 GLU A CA 1 ATOM 1451 C C . GLU B 2 185 ? 17.692 49.360 56.438 1.00 24.21 ? 185 GLU A C 1 ATOM 1452 O O . GLU B 2 185 ? 17.838 49.002 57.602 1.00 24.34 ? 185 GLU A O 1 ATOM 1453 C CB . GLU B 2 185 ? 16.105 51.030 55.499 1.00 23.39 ? 185 GLU A CB 1 ATOM 1454 C CG . GLU B 2 185 ? 14.997 50.881 56.533 1.00 25.22 ? 185 GLU A CG 1 ATOM 1455 C CD . GLU B 2 185 ? 13.634 50.633 55.915 1.00 27.20 ? 185 GLU A CD 1 ATOM 1456 O OE1 . GLU B 2 185 ? 13.421 51.048 54.755 1.00 26.80 ? 185 GLU A OE1 1 ATOM 1457 O OE2 . GLU B 2 185 ? 12.776 50.033 56.602 1.00 27.58 ? 185 GLU A OE2 1 ATOM 1458 N N . GLY B 2 186 ? 17.688 48.512 55.409 1.00 25.41 ? 186 GLY A N 1 ATOM 1459 C CA . GLY B 2 186 ? 17.887 47.087 55.603 1.00 25.82 ? 186 GLY A CA 1 ATOM 1460 C C . GLY B 2 186 ? 19.167 46.783 56.366 1.00 26.89 ? 186 GLY A C 1 ATOM 1461 O O . GLY B 2 186 ? 19.220 45.838 57.149 1.00 25.53 ? 186 GLY A O 1 ATOM 1462 N N . GLU B 2 187 ? 20.210 47.573 56.132 1.00 27.64 ? 187 GLU A N 1 ATOM 1463 C CA . GLU B 2 187 ? 21.467 47.379 56.835 1.00 30.10 ? 187 GLU A CA 1 ATOM 1464 C C . GLU B 2 187 ? 21.250 47.591 58.327 1.00 31.50 ? 187 GLU A C 1 ATOM 1465 O O . GLU B 2 187 ? 21.690 46.782 59.138 1.00 33.90 ? 187 GLU A O 1 ATOM 1466 C CB . GLU B 2 187 ? 22.522 48.362 56.339 1.00 33.08 ? 187 GLU A CB 1 ATOM 1467 C CG . GLU B 2 187 ? 23.227 47.927 55.084 1.00 38.44 ? 187 GLU A CG 1 ATOM 1468 C CD . GLU B 2 187 ? 24.114 46.729 55.325 1.00 42.06 ? 187 GLU A CD 1 ATOM 1469 O OE1 . GLU B 2 187 ? 25.031 46.838 56.174 1.00 41.15 ? 187 GLU A OE1 1 ATOM 1470 O OE2 . GLU B 2 187 ? 23.889 45.685 54.666 1.00 44.87 ? 187 GLU A OE2 1 ATOM 1471 N N . MET B 2 188 ? 20.569 48.679 58.691 1.00 29.88 ? 188 MET A N 1 ATOM 1472 C CA . MET B 2 188 ? 20.304 48.984 60.097 1.00 28.45 ? 188 MET A CA 1 ATOM 1473 C C . MET B 2 188 ? 19.355 47.950 60.694 1.00 29.56 ? 188 MET A C 1 ATOM 1474 O O . MET B 2 188 ? 19.453 47.594 61.868 1.00 30.01 ? 188 MET A O 1 ATOM 1475 C CB . MET B 2 188 ? 19.676 50.372 60.235 1.00 26.92 ? 188 MET A CB 1 ATOM 1476 C CG . MET B 2 188 ? 20.472 51.492 59.618 1.00 25.86 ? 188 MET A CG 1 ATOM 1477 S SD . MET B 2 188 ? 22.098 51.629 60.352 1.00 27.79 ? 188 MET A SD 1 ATOM 1478 C CE . MET B 2 188 ? 23.102 50.943 59.055 1.00 28.16 ? 188 MET A CE 1 ATOM 1479 N N . ARG B 2 189 ? 18.431 47.475 59.869 1.00 30.32 ? 189 ARG A N 1 ATOM 1480 C CA . ARG B 2 189 ? 17.440 46.498 60.289 1.00 30.94 ? 189 ARG A CA 1 ATOM 1481 C C . ARG B 2 189 ? 18.078 45.162 60.625 1.00 31.10 ? 189 ARG A C 1 ATOM 1482 O O . ARG B 2 189 ? 17.575 44.430 61.473 1.00 30.86 ? 189 ARG A O 1 ATOM 1483 C CB . ARG B 2 189 ? 16.400 46.324 59.188 1.00 32.67 ? 189 ARG A CB 1 ATOM 1484 C CG . ARG B 2 189 ? 15.189 45.515 59.581 1.00 35.05 ? 189 ARG A CG 1 ATOM 1485 C CD . ARG B 2 189 ? 14.098 45.724 58.563 1.00 36.28 ? 189 ARG A CD 1 ATOM 1486 N NE . ARG B 2 189 ? 14.522 45.315 57.232 1.00 38.76 ? 189 ARG A NE 1 ATOM 1487 C CZ . ARG B 2 189 ? 14.242 45.996 56.126 1.00 40.42 ? 189 ARG A CZ 1 ATOM 1488 N NH1 . ARG B 2 189 ? 13.540 47.121 56.211 1.00 40.53 ? 189 ARG A NH1 1 ATOM 1489 N NH2 . ARG B 2 189 ? 14.659 45.552 54.941 1.00 38.76 ? 189 ARG A NH2 1 ATOM 1490 N N . THR B 2 190 ? 19.182 44.841 59.959 1.00 31.13 ? 190 THR A N 1 ATOM 1491 C CA . THR B 2 190 ? 19.884 43.587 60.220 1.00 31.47 ? 190 THR A CA 1 ATOM 1492 C C . THR B 2 190 ? 20.632 43.671 61.538 1.00 31.59 ? 190 THR A C 1 ATOM 1493 O O . THR B 2 190 ? 20.729 42.686 62.269 1.00 33.29 ? 190 THR A O 1 ATOM 1494 C CB . THR B 2 190 ? 20.891 43.257 59.119 1.00 30.46 ? 190 THR A CB 1 ATOM 1495 O OG1 . THR B 2 190 ? 20.190 42.830 57.945 1.00 32.37 ? 190 THR A OG1 1 ATOM 1496 C CG2 . THR B 2 190 ? 21.828 42.160 59.574 1.00 29.93 ? 190 THR A CG2 1 ATOM 1497 N N . ARG B 2 191 ? 21.161 44.851 61.838 1.00 31.19 ? 191 ARG A N 1 ATOM 1498 C CA . ARG B 2 191 ? 21.890 45.057 63.080 1.00 30.16 ? 191 ARG A CA 1 ATOM 1499 C C . ARG B 2 191 ? 20.974 44.960 64.286 1.00 30.36 ? 191 ARG A C 1 ATOM 1500 O O . ARG B 2 191 ? 21.428 44.649 65.382 1.00 30.88 ? 191 ARG A O 1 ATOM 1501 C CB . ARG B 2 191 ? 22.579 46.417 63.070 1.00 28.53 ? 191 ARG A CB 1 ATOM 1502 C CG . ARG B 2 191 ? 23.661 46.519 62.027 1.00 25.64 ? 191 ARG A CG 1 ATOM 1503 C CD . ARG B 2 191 ? 24.347 47.860 62.096 1.00 25.68 ? 191 ARG A CD 1 ATOM 1504 N NE . ARG B 2 191 ? 25.629 47.847 61.396 1.00 25.71 ? 191 ARG A NE 1 ATOM 1505 C CZ . ARG B 2 191 ? 25.778 47.539 60.114 1.00 24.98 ? 191 ARG A CZ 1 ATOM 1506 N NH1 . ARG B 2 191 ? 24.720 47.218 59.382 1.00 25.57 ? 191 ARG A NH1 1 ATOM 1507 N NH2 . ARG B 2 191 ? 26.984 47.546 59.564 1.00 23.88 ? 191 ARG A NH2 1 ATOM 1508 N N . ILE B 2 192 ? 19.688 45.229 64.084 1.00 29.37 ? 192 ILE A N 1 ATOM 1509 C CA . ILE B 2 192 ? 18.730 45.157 65.178 1.00 29.58 ? 192 ILE A CA 1 ATOM 1510 C C . ILE B 2 192 ? 18.243 43.725 65.340 1.00 31.06 ? 192 ILE A C 1 ATOM 1511 O O . ILE B 2 192 ? 18.116 43.229 66.456 1.00 32.87 ? 192 ILE A O 1 ATOM 1512 C CB . ILE B 2 192 ? 17.509 46.070 64.936 1.00 27.24 ? 192 ILE A CB 1 ATOM 1513 C CG1 . ILE B 2 192 ? 17.959 47.533 64.858 1.00 27.56 ? 192 ILE A CG1 1 ATOM 1514 C CG2 . ILE B 2 192 ? 16.499 45.888 66.057 1.00 25.13 ? 192 ILE A CG2 1 ATOM 1515 C CD1 . ILE B 2 192 ? 16.844 48.512 64.508 1.00 25.86 ? 192 ILE A CD1 1 ATOM 1516 N N . ARG B 2 193 ? 17.986 43.057 64.221 1.00 31.52 ? 193 ARG A N 1 ATOM 1517 C CA . ARG B 2 193 ? 17.495 41.684 64.248 1.00 31.24 ? 193 ARG A CA 1 ATOM 1518 C C . ARG B 2 193 ? 18.387 40.740 65.062 1.00 32.55 ? 193 ARG A C 1 ATOM 1519 O O . ARG B 2 193 ? 17.886 39.897 65.817 1.00 31.51 ? 193 ARG A O 1 ATOM 1520 C CB . ARG B 2 193 ? 17.356 41.149 62.821 1.00 29.53 ? 193 ARG A CB 1 ATOM 1521 C CG . ARG B 2 193 ? 16.598 39.841 62.726 1.00 28.23 ? 193 ARG A CG 1 ATOM 1522 C CD . ARG B 2 193 ? 16.667 39.255 61.331 1.00 27.83 ? 193 ARG A CD 1 ATOM 1523 N NE . ARG B 2 193 ? 16.092 40.116 60.296 1.00 27.43 ? 193 ARG A NE 1 ATOM 1524 C CZ . ARG B 2 193 ? 14.801 40.415 60.179 1.00 28.51 ? 193 ARG A CZ 1 ATOM 1525 N NH1 . ARG B 2 193 ? 13.910 39.930 61.040 1.00 26.85 ? 193 ARG A NH1 1 ATOM 1526 N NH2 . ARG B 2 193 ? 14.403 41.200 59.183 1.00 27.61 ? 193 ARG A NH2 1 ATOM 1527 N N . TYR B 2 194 ? 19.704 40.890 64.915 1.00 33.20 ? 194 TYR A N 1 ATOM 1528 C CA . TYR B 2 194 ? 20.655 40.030 65.613 1.00 33.52 ? 194 TYR A CA 1 ATOM 1529 C C . TYR B 2 194 ? 21.422 40.716 66.734 1.00 34.80 ? 194 TYR A C 1 ATOM 1530 O O . TYR B 2 194 ? 22.424 40.188 67.217 1.00 35.34 ? 194 TYR A O 1 ATOM 1531 C CB . TYR B 2 194 ? 21.652 39.444 64.617 1.00 32.01 ? 194 TYR A CB 1 ATOM 1532 C CG . TYR B 2 194 ? 21.015 38.884 63.368 1.00 32.11 ? 194 TYR A CG 1 ATOM 1533 C CD1 . TYR B 2 194 ? 19.950 37.986 63.441 1.00 31.48 ? 194 TYR A CD1 1 ATOM 1534 C CD2 . TYR B 2 194 ? 21.481 39.249 62.107 1.00 32.65 ? 194 TYR A CD2 1 ATOM 1535 C CE1 . TYR B 2 194 ? 19.365 37.466 62.285 1.00 31.32 ? 194 TYR A CE1 1 ATOM 1536 C CE2 . TYR B 2 194 ? 20.906 38.735 60.947 1.00 31.67 ? 194 TYR A CE2 1 ATOM 1537 C CZ . TYR B 2 194 ? 19.849 37.846 61.041 1.00 32.25 ? 194 TYR A CZ 1 ATOM 1538 O OH . TYR B 2 194 ? 19.280 37.353 59.889 1.00 32.30 ? 194 TYR A OH 1 ATOM 1539 N N . ASN B 2 195 ? 20.950 41.884 67.151 1.00 35.36 ? 195 ASN A N 1 ATOM 1540 C CA . ASN B 2 195 ? 21.596 42.640 68.218 1.00 36.86 ? 195 ASN A CA 1 ATOM 1541 C C . ASN B 2 195 ? 23.103 42.840 67.986 1.00 38.35 ? 195 ASN A C 1 ATOM 1542 O O . ASN B 2 195 ? 23.920 42.570 68.869 1.00 38.58 ? 195 ASN A O 1 ATOM 1543 C CB . ASN B 2 195 ? 21.348 41.957 69.566 1.00 33.61 ? 195 ASN A CB 1 ATOM 1544 C CG . ASN B 2 195 ? 21.925 42.736 70.735 1.00 32.77 ? 195 ASN A CG 1 ATOM 1545 O OD1 . ASN B 2 195 ? 21.947 43.966 70.734 1.00 31.43 ? 195 ASN A OD1 1 ATOM 1546 N ND2 . ASN B 2 195 ? 22.381 42.014 71.749 1.00 32.93 ? 195 ASN A ND2 1 ATOM 1547 N N . ARG B 2 196 ? 23.456 43.326 66.794 1.00 39.72 ? 196 ARG A N 1 ATOM 1548 C CA . ARG B 2 196 ? 24.847 43.588 66.433 1.00 39.97 ? 196 ARG A CA 1 ATOM 1549 C C . ARG B 2 196 ? 25.220 45.068 66.524 1.00 40.04 ? 196 ARG A C 1 ATOM 1550 O O . ARG B 2 196 ? 24.369 45.952 66.388 1.00 40.37 ? 196 ARG A O 1 ATOM 1551 C CB . ARG B 2 196 ? 25.143 43.144 65.001 1.00 40.64 ? 196 ARG A CB 1 ATOM 1552 C CG . ARG B 2 196 ? 25.073 41.671 64.740 1.00 43.49 ? 196 ARG A CG 1 ATOM 1553 C CD . ARG B 2 196 ? 26.086 41.314 63.670 1.00 45.46 ? 196 ARG A CD 1 ATOM 1554 N NE . ARG B 2 196 ? 25.791 40.040 63.024 1.00 50.42 ? 196 ARG A NE 1 ATOM 1555 C CZ . ARG B 2 196 ? 24.978 39.904 61.979 1.00 52.49 ? 196 ARG A CZ 1 ATOM 1556 N NH1 . ARG B 2 196 ? 24.381 40.972 61.461 1.00 53.08 ? 196 ARG A NH1 1 ATOM 1557 N NH2 . ARG B 2 196 ? 24.767 38.702 61.446 1.00 53.42 ? 196 ARG A NH2 1 ATOM 1558 N N . ARG B 2 197 ? 26.506 45.317 66.750 1.00 38.11 ? 197 ARG A N 1 ATOM 1559 C CA . ARG B 2 197 ? 27.057 46.661 66.811 1.00 36.16 ? 197 ARG A CA 1 ATOM 1560 C C . ARG B 2 197 ? 28.236 46.579 65.853 1.00 35.32 ? 197 ARG A C 1 ATOM 1561 O O . ARG B 2 197 ? 29.236 45.937 66.164 1.00 35.69 ? 197 ARG A O 1 ATOM 1562 C CB . ARG B 2 197 ? 27.583 46.988 68.210 1.00 36.14 ? 197 ARG A CB 1 ATOM 1563 C CG . ARG B 2 197 ? 26.538 47.056 69.310 1.00 37.40 ? 197 ARG A CG 1 ATOM 1564 C CD . ARG B 2 197 ? 27.199 47.391 70.653 1.00 37.16 ? 197 ARG A CD 1 ATOM 1565 N NE . ARG B 2 197 ? 28.091 48.542 70.538 1.00 37.01 ? 197 ARG A NE 1 ATOM 1566 C CZ . ARG B 2 197 ? 28.005 49.643 71.283 1.00 36.98 ? 197 ARG A CZ 1 ATOM 1567 N NH1 . ARG B 2 197 ? 27.061 49.757 72.211 1.00 35.40 ? 197 ARG A NH1 1 ATOM 1568 N NH2 . ARG B 2 197 ? 28.867 50.635 71.097 1.00 36.35 ? 197 ARG A NH2 1 ATOM 1569 N N . SER B 2 198 ? 28.134 47.197 64.684 1.00 32.57 ? 198 SER A N 1 ATOM 1570 C CA . SER B 2 198 ? 29.244 47.135 63.747 1.00 31.32 ? 198 SER A CA 1 ATOM 1571 C C . SER B 2 198 ? 29.251 48.301 62.774 1.00 31.33 ? 198 SER A C 1 ATOM 1572 O O . SER B 2 198 ? 28.204 48.722 62.298 1.00 33.49 ? 198 SER A O 1 ATOM 1573 C CB . SER B 2 198 ? 29.206 45.810 62.989 1.00 29.69 ? 198 SER A CB 1 ATOM 1574 O OG . SER B 2 198 ? 28.022 45.681 62.235 1.00 29.45 ? 198 SER A OG 1 ATOM 1575 N N . ALA B 2 199 ? 30.439 48.819 62.475 1.00 31.04 ? 199 ALA A N 1 ATOM 1576 C CA . ALA B 2 199 ? 30.579 49.950 61.566 1.00 30.70 ? 199 ALA A CA 1 ATOM 1577 C C . ALA B 2 199 ? 30.054 49.645 60.166 1.00 31.03 ? 199 ALA A C 1 ATOM 1578 O O . ALA B 2 199 ? 30.038 48.491 59.737 1.00 31.14 ? 199 ALA A O 1 ATOM 1579 C CB . ALA B 2 199 ? 32.033 50.373 61.493 1.00 30.51 ? 199 ALA A CB 1 ATOM 1580 N N . PRO B 2 200 ? 29.629 50.689 59.429 1.00 30.34 ? 200 PRO A N 1 ATOM 1581 C CA . PRO B 2 200 ? 29.097 50.563 58.071 1.00 32.22 ? 200 PRO A CA 1 ATOM 1582 C C . PRO B 2 200 ? 30.114 50.069 57.041 1.00 33.41 ? 200 PRO A C 1 ATOM 1583 O O . PRO B 2 200 ? 31.273 50.490 57.048 1.00 33.55 ? 200 PRO A O 1 ATOM 1584 C CB . PRO B 2 200 ? 28.617 51.973 57.769 1.00 30.57 ? 200 PRO A CB 1 ATOM 1585 C CG . PRO B 2 200 ? 29.607 52.809 58.513 1.00 29.88 ? 200 PRO A CG 1 ATOM 1586 C CD . PRO B 2 200 ? 29.671 52.106 59.835 1.00 30.13 ? 200 PRO A CD 1 ATOM 1587 N N . ASP B 2 201 ? 29.655 49.179 56.159 1.00 34.06 ? 201 ASP A N 1 ATOM 1588 C CA . ASP B 2 201 ? 30.458 48.594 55.086 1.00 35.85 ? 201 ASP A CA 1 ATOM 1589 C C . ASP B 2 201 ? 30.865 49.633 54.076 1.00 35.58 ? 201 ASP A C 1 ATOM 1590 O O . ASP B 2 201 ? 30.356 50.750 54.078 1.00 36.05 ? 201 ASP A O 1 ATOM 1591 C CB . ASP B 2 201 ? 29.652 47.550 54.326 1.00 38.41 ? 201 ASP A CB 1 ATOM 1592 C CG . ASP B 2 201 ? 29.371 46.332 55.143 1.00 43.29 ? 201 ASP A CG 1 ATOM 1593 O OD1 . ASP B 2 201 ? 30.343 45.609 55.449 1.00 46.15 ? 201 ASP A OD1 1 ATOM 1594 O OD2 . ASP B 2 201 ? 28.187 46.100 55.483 1.00 45.28 ? 201 ASP A OD2 1 ATOM 1595 N N . PRO B 2 202 ? 31.795 49.275 53.186 1.00 34.77 ? 202 PRO A N 1 ATOM 1596 C CA . PRO B 2 202 ? 32.236 50.220 52.159 1.00 35.99 ? 202 PRO A CA 1 ATOM 1597 C C . PRO B 2 202 ? 31.035 50.569 51.260 1.00 35.43 ? 202 PRO A C 1 ATOM 1598 O O . PRO B 2 202 ? 30.970 51.655 50.681 1.00 36.38 ? 202 PRO A O 1 ATOM 1599 C CB . PRO B 2 202 ? 33.313 49.435 51.419 1.00 35.53 ? 202 PRO A CB 1 ATOM 1600 C CG . PRO B 2 202 ? 33.897 48.584 52.508 1.00 35.47 ? 202 PRO A CG 1 ATOM 1601 C CD . PRO B 2 202 ? 32.669 48.091 53.225 1.00 35.20 ? 202 PRO A CD 1 ATOM 1602 N N . SER B 2 203 ? 30.082 49.641 51.168 1.00 33.76 ? 203 SER A N 1 ATOM 1603 C CA . SER B 2 203 ? 28.886 49.827 50.350 1.00 32.65 ? 203 SER A CA 1 ATOM 1604 C C . SER B 2 203 ? 28.020 50.953 50.886 1.00 31.46 ? 203 SER A C 1 ATOM 1605 O O . SER B 2 203 ? 27.522 51.784 50.123 1.00 32.42 ? 203 SER A O 1 ATOM 1606 C CB . SER B 2 203 ? 28.062 48.541 50.317 1.00 33.46 ? 203 SER A CB 1 ATOM 1607 O OG . SER B 2 203 ? 27.634 48.186 51.621 1.00 35.85 ? 203 SER A OG 1 ATOM 1608 N N . VAL B 2 204 ? 27.836 50.964 52.205 1.00 28.85 ? 204 VAL A N 1 ATOM 1609 C CA . VAL B 2 204 ? 27.034 51.975 52.880 1.00 25.62 ? 204 VAL A CA 1 ATOM 1610 C C . VAL B 2 204 ? 27.715 53.342 52.818 1.00 25.81 ? 204 VAL A C 1 ATOM 1611 O O . VAL B 2 204 ? 27.089 54.330 52.434 1.00 26.96 ? 204 VAL A O 1 ATOM 1612 C CB . VAL B 2 204 ? 26.783 51.565 54.338 1.00 24.25 ? 204 VAL A CB 1 ATOM 1613 C CG1 . VAL B 2 204 ? 26.027 52.648 55.063 1.00 23.39 ? 204 VAL A CG1 1 ATOM 1614 C CG2 . VAL B 2 204 ? 25.996 50.267 54.365 1.00 22.79 ? 204 VAL A CG2 1 ATOM 1615 N N . ILE B 2 205 ? 28.996 53.397 53.183 1.00 24.61 ? 205 ILE A N 1 ATOM 1616 C CA . ILE B 2 205 ? 29.762 54.644 53.136 1.00 23.52 ? 205 ILE A CA 1 ATOM 1617 C C . ILE B 2 205 ? 29.696 55.286 51.738 1.00 23.10 ? 205 ILE A C 1 ATOM 1618 O O . ILE B 2 205 ? 29.508 56.492 51.616 1.00 23.81 ? 205 ILE A O 1 ATOM 1619 C CB . ILE B 2 205 ? 31.259 54.407 53.492 1.00 22.41 ? 205 ILE A CB 1 ATOM 1620 C CG1 . ILE B 2 205 ? 31.396 53.910 54.931 1.00 21.24 ? 205 ILE A CG1 1 ATOM 1621 C CG2 . ILE B 2 205 ? 32.049 55.699 53.326 1.00 21.66 ? 205 ILE A CG2 1 ATOM 1622 C CD1 . ILE B 2 205 ? 31.014 54.932 55.963 1.00 22.49 ? 205 ILE A CD1 1 ATOM 1623 N N . THR B 2 206 ? 29.850 54.480 50.688 1.00 22.88 ? 206 THR A N 1 ATOM 1624 C CA . THR B 2 206 ? 29.815 54.987 49.313 1.00 23.40 ? 206 THR A CA 1 ATOM 1625 C C . THR B 2 206 ? 28.446 55.493 48.875 1.00 23.80 ? 206 THR A C 1 ATOM 1626 O O . THR B 2 206 ? 28.349 56.508 48.179 1.00 23.84 ? 206 THR A O 1 ATOM 1627 C CB . THR B 2 206 ? 30.273 53.914 48.301 1.00 22.70 ? 206 THR A CB 1 ATOM 1628 O OG1 . THR B 2 206 ? 31.689 53.752 48.386 1.00 22.16 ? 206 THR A OG1 1 ATOM 1629 C CG2 . THR B 2 206 ? 29.921 54.325 46.885 1.00 23.46 ? 206 THR A CG2 1 ATOM 1630 N N . LEU B 2 207 ? 27.392 54.776 49.258 1.00 23.97 ? 207 LEU A N 1 ATOM 1631 C CA . LEU B 2 207 ? 26.037 55.178 48.890 1.00 24.24 ? 207 LEU A CA 1 ATOM 1632 C C . LEU B 2 207 ? 25.713 56.504 49.554 1.00 24.53 ? 207 LEU A C 1 ATOM 1633 O O . LEU B 2 207 ? 25.009 57.334 48.986 1.00 26.14 ? 207 LEU A O 1 ATOM 1634 C CB . LEU B 2 207 ? 25.011 54.133 49.334 1.00 24.23 ? 207 LEU A CB 1 ATOM 1635 C CG . LEU B 2 207 ? 24.743 52.902 48.468 1.00 22.70 ? 207 LEU A CG 1 ATOM 1636 C CD1 . LEU B 2 207 ? 23.662 52.052 49.113 1.00 19.22 ? 207 LEU A CD1 1 ATOM 1637 C CD2 . LEU B 2 207 ? 24.306 53.350 47.092 1.00 23.57 ? 207 LEU A CD2 1 ATOM 1638 N N . GLU B 2 208 ? 26.225 56.695 50.767 1.00 24.09 ? 208 GLU A N 1 ATOM 1639 C CA . GLU B 2 208 ? 25.991 57.927 51.506 1.00 22.61 ? 208 GLU A CA 1 ATOM 1640 C C . GLU B 2 208 ? 26.627 59.094 50.792 1.00 21.69 ? 208 GLU A C 1 ATOM 1641 O O . GLU B 2 208 ? 26.049 60.166 50.707 1.00 21.05 ? 208 GLU A O 1 ATOM 1642 C CB . GLU B 2 208 ? 26.582 57.841 52.906 1.00 22.35 ? 208 GLU A CB 1 ATOM 1643 C CG . GLU B 2 208 ? 25.836 56.950 53.866 1.00 23.78 ? 208 GLU A CG 1 ATOM 1644 C CD . GLU B 2 208 ? 26.589 56.800 55.166 1.00 24.19 ? 208 GLU A CD 1 ATOM 1645 O OE1 . GLU B 2 208 ? 27.568 57.551 55.357 1.00 26.57 ? 208 GLU A OE1 1 ATOM 1646 O OE2 . GLU B 2 208 ? 26.217 55.946 55.998 1.00 23.12 ? 208 GLU A OE2 1 ATOM 1647 N N . ASN B 2 209 ? 27.828 58.868 50.283 1.00 22.25 ? 209 ASN A N 1 ATOM 1648 C CA . ASN B 2 209 ? 28.589 59.892 49.581 1.00 25.96 ? 209 ASN A CA 1 ATOM 1649 C C . ASN B 2 209 ? 28.064 60.233 48.190 1.00 29.37 ? 209 ASN A C 1 ATOM 1650 O O . ASN B 2 209 ? 28.204 61.366 47.731 1.00 31.63 ? 209 ASN A O 1 ATOM 1651 C CB . ASN B 2 209 ? 30.047 59.450 49.463 1.00 23.06 ? 209 ASN A CB 1 ATOM 1652 C CG . ASN B 2 209 ? 30.726 59.320 50.810 1.00 22.65 ? 209 ASN A CG 1 ATOM 1653 O OD1 . ASN B 2 209 ? 31.743 58.647 50.943 1.00 21.38 ? 209 ASN A OD1 1 ATOM 1654 N ND2 . ASN B 2 209 ? 30.170 59.982 51.819 1.00 23.05 ? 209 ASN A ND2 1 ATOM 1655 N N . SER B 2 210 ? 27.451 59.258 47.526 1.00 31.25 ? 210 SER A N 1 ATOM 1656 C CA . SER B 2 210 ? 26.949 59.457 46.173 1.00 32.95 ? 210 SER A CA 1 ATOM 1657 C C . SER B 2 210 ? 25.498 59.919 46.064 1.00 34.76 ? 210 SER A C 1 ATOM 1658 O O . SER B 2 210 ? 24.965 60.041 44.957 1.00 35.45 ? 210 SER A O 1 ATOM 1659 C CB . SER B 2 210 ? 27.125 58.161 45.387 1.00 33.05 ? 210 SER A CB 1 ATOM 1660 O OG . SER B 2 210 ? 28.440 57.665 45.547 1.00 32.31 ? 210 SER A OG 1 ATOM 1661 N N . TRP B 2 211 ? 24.859 60.184 47.200 1.00 35.91 ? 211 TRP A N 1 ATOM 1662 C CA . TRP B 2 211 ? 23.463 60.611 47.189 1.00 35.96 ? 211 TRP A CA 1 ATOM 1663 C C . TRP B 2 211 ? 23.245 61.828 46.298 1.00 36.65 ? 211 TRP A C 1 ATOM 1664 O O . TRP B 2 211 ? 22.312 61.858 45.502 1.00 37.05 ? 211 TRP A O 1 ATOM 1665 C CB . TRP B 2 211 ? 22.976 60.916 48.608 1.00 35.77 ? 211 TRP A CB 1 ATOM 1666 C CG . TRP B 2 211 ? 21.488 61.083 48.688 1.00 35.19 ? 211 TRP A CG 1 ATOM 1667 C CD1 . TRP B 2 211 ? 20.541 60.200 48.254 1.00 34.76 ? 211 TRP A CD1 1 ATOM 1668 C CD2 . TRP B 2 211 ? 20.775 62.198 49.233 1.00 34.92 ? 211 TRP A CD2 1 ATOM 1669 N NE1 . TRP B 2 211 ? 19.284 60.696 48.493 1.00 35.02 ? 211 TRP A NE1 1 ATOM 1670 C CE2 . TRP B 2 211 ? 19.398 61.923 49.093 1.00 35.06 ? 211 TRP A CE2 1 ATOM 1671 C CE3 . TRP B 2 211 ? 21.166 63.406 49.827 1.00 35.39 ? 211 TRP A CE3 1 ATOM 1672 C CZ2 . TRP B 2 211 ? 18.407 62.810 49.524 1.00 35.98 ? 211 TRP A CZ2 1 ATOM 1673 C CZ3 . TRP B 2 211 ? 20.181 64.289 50.257 1.00 36.51 ? 211 TRP A CZ3 1 ATOM 1674 C CH2 . TRP B 2 211 ? 18.817 63.984 50.102 1.00 37.00 ? 211 TRP A CH2 1 ATOM 1675 N N . GLY B 2 212 ? 24.103 62.832 46.428 1.00 37.16 ? 212 GLY A N 1 ATOM 1676 C CA . GLY B 2 212 ? 23.953 64.015 45.607 1.00 36.60 ? 212 GLY A CA 1 ATOM 1677 C C . GLY B 2 212 ? 24.137 63.694 44.137 1.00 37.24 ? 212 GLY A C 1 ATOM 1678 O O . GLY B 2 212 ? 23.321 64.094 43.305 1.00 37.08 ? 212 GLY A O 1 ATOM 1679 N N . ARG B 2 213 ? 25.206 62.965 43.814 1.00 37.80 ? 213 ARG A N 1 ATOM 1680 C CA . ARG B 2 213 ? 25.494 62.609 42.427 1.00 38.41 ? 213 ARG A CA 1 ATOM 1681 C C . ARG B 2 213 ? 24.387 61.777 41.791 1.00 37.59 ? 213 ARG A C 1 ATOM 1682 O O . ARG B 2 213 ? 23.999 62.026 40.652 1.00 37.83 ? 213 ARG A O 1 ATOM 1683 C CB . ARG B 2 213 ? 26.838 61.870 42.316 1.00 40.90 ? 213 ARG A CB 1 ATOM 1684 C CG . ARG B 2 213 ? 28.064 62.794 42.316 1.00 45.25 ? 213 ARG A CG 1 ATOM 1685 C CD . ARG B 2 213 ? 29.342 62.074 41.879 1.00 48.07 ? 213 ARG A CD 1 ATOM 1686 N NE . ARG B 2 213 ? 29.721 61.015 42.812 1.00 53.74 ? 213 ARG A NE 1 ATOM 1687 C CZ . ARG B 2 213 ? 30.078 61.219 44.082 1.00 56.78 ? 213 ARG A CZ 1 ATOM 1688 N NH1 . ARG B 2 213 ? 30.113 62.450 44.581 1.00 59.11 ? 213 ARG A NH1 1 ATOM 1689 N NH2 . ARG B 2 213 ? 30.392 60.190 44.863 1.00 57.12 ? 213 ARG A NH2 1 ATOM 1690 N N . LEU B 2 214 ? 23.877 60.794 42.524 1.00 35.50 ? 214 LEU A N 1 ATOM 1691 C CA . LEU B 2 214 ? 22.811 59.943 42.009 1.00 33.35 ? 214 LEU A CA 1 ATOM 1692 C C . LEU B 2 214 ? 21.532 60.747 41.774 1.00 32.58 ? 214 LEU A C 1 ATOM 1693 O O . LEU B 2 214 ? 20.859 60.562 40.760 1.00 34.36 ? 214 LEU A O 1 ATOM 1694 C CB . LEU B 2 214 ? 22.539 58.798 42.983 1.00 32.04 ? 214 LEU A CB 1 ATOM 1695 C CG . LEU B 2 214 ? 23.709 57.841 43.196 1.00 30.88 ? 214 LEU A CG 1 ATOM 1696 C CD1 . LEU B 2 214 ? 23.467 56.979 44.420 1.00 31.23 ? 214 LEU A CD1 1 ATOM 1697 C CD2 . LEU B 2 214 ? 23.878 56.992 41.958 1.00 30.13 ? 214 LEU A CD2 1 ATOM 1698 N N . SER B 2 215 ? 21.194 61.636 42.706 1.00 30.86 ? 215 SER A N 1 ATOM 1699 C CA . SER B 2 215 ? 19.996 62.456 42.562 1.00 29.61 ? 215 SER A CA 1 ATOM 1700 C C . SER B 2 215 ? 20.047 63.200 41.239 1.00 30.09 ? 215 SER A C 1 ATOM 1701 O O . SER B 2 215 ? 19.055 63.302 40.518 1.00 29.65 ? 215 SER A O 1 ATOM 1702 C CB . SER B 2 215 ? 19.888 63.460 43.707 1.00 28.55 ? 215 SER A CB 1 ATOM 1703 O OG . SER B 2 215 ? 19.415 62.835 44.880 1.00 27.48 ? 215 SER A OG 1 ATOM 1704 N N . THR B 2 216 ? 21.221 63.721 40.921 1.00 30.18 ? 216 THR A N 1 ATOM 1705 C CA . THR B 2 216 ? 21.407 64.445 39.677 1.00 30.60 ? 216 THR A CA 1 ATOM 1706 C C . THR B 2 216 ? 21.343 63.539 38.444 1.00 30.27 ? 216 THR A C 1 ATOM 1707 O O . THR B 2 216 ? 20.532 63.771 37.551 1.00 30.93 ? 216 THR A O 1 ATOM 1708 C CB . THR B 2 216 ? 22.746 65.184 39.687 1.00 30.41 ? 216 THR A CB 1 ATOM 1709 O OG1 . THR B 2 216 ? 22.709 66.204 40.696 1.00 30.41 ? 216 THR A OG1 1 ATOM 1710 C CG2 . THR B 2 216 ? 23.016 65.808 38.333 1.00 29.09 ? 216 THR A CG2 1 ATOM 1711 N N . ALA B 2 217 ? 22.186 62.507 38.404 1.00 28.55 ? 217 ALA A N 1 ATOM 1712 C CA . ALA B 2 217 ? 22.235 61.583 37.273 1.00 27.08 ? 217 ALA A CA 1 ATOM 1713 C C . ALA B 2 217 ? 20.873 61.075 36.830 1.00 28.01 ? 217 ALA A C 1 ATOM 1714 O O . ALA B 2 217 ? 20.541 61.129 35.647 1.00 29.51 ? 217 ALA A O 1 ATOM 1715 C CB . ALA B 2 217 ? 23.127 60.415 37.605 1.00 25.10 ? 217 ALA A CB 1 ATOM 1716 N N . ILE B 2 218 ? 20.084 60.584 37.780 1.00 29.25 ? 218 ILE A N 1 ATOM 1717 C CA . ILE B 2 218 ? 18.758 60.047 37.483 1.00 30.47 ? 218 ILE A CA 1 ATOM 1718 C C . ILE B 2 218 ? 17.786 61.104 36.951 1.00 31.34 ? 218 ILE A C 1 ATOM 1719 O O . ILE B 2 218 ? 17.130 60.899 35.930 1.00 32.18 ? 218 ILE A O 1 ATOM 1720 C CB . ILE B 2 218 ? 18.114 59.405 38.735 1.00 29.63 ? 218 ILE A CB 1 ATOM 1721 C CG1 . ILE B 2 218 ? 19.072 58.393 39.370 1.00 28.35 ? 218 ILE A CG1 1 ATOM 1722 C CG2 . ILE B 2 218 ? 16.822 58.710 38.349 1.00 29.54 ? 218 ILE A CG2 1 ATOM 1723 C CD1 . ILE B 2 218 ? 18.527 57.728 40.629 1.00 26.84 ? 218 ILE A CD1 1 ATOM 1724 N N . GLN B 2 219 ? 17.693 62.228 37.652 1.00 32.90 ? 219 GLN A N 1 ATOM 1725 C CA . GLN B 2 219 ? 16.789 63.303 37.269 1.00 33.78 ? 219 GLN A CA 1 ATOM 1726 C C . GLN B 2 219 ? 17.097 63.928 35.919 1.00 34.94 ? 219 GLN A C 1 ATOM 1727 O O . GLN B 2 219 ? 16.193 64.434 35.259 1.00 35.44 ? 219 GLN A O 1 ATOM 1728 C CB . GLN B 2 219 ? 16.770 64.382 38.355 1.00 33.34 ? 219 GLN A CB 1 ATOM 1729 C CG . GLN B 2 219 ? 15.958 63.989 39.583 1.00 33.63 ? 219 GLN A CG 1 ATOM 1730 C CD . GLN B 2 219 ? 16.120 64.957 40.737 1.00 33.82 ? 219 GLN A CD 1 ATOM 1731 O OE1 . GLN B 2 219 ? 15.902 66.158 40.596 1.00 33.14 ? 219 GLN A OE1 1 ATOM 1732 N NE2 . GLN B 2 219 ? 16.498 64.431 41.894 1.00 33.30 ? 219 GLN A NE2 1 ATOM 1733 N N . GLU B 2 220 ? 18.358 63.910 35.500 1.00 37.24 ? 220 GLU A N 1 ATOM 1734 C CA . GLU B 2 220 ? 18.688 64.479 34.204 1.00 40.34 ? 220 GLU A CA 1 ATOM 1735 C C . GLU B 2 220 ? 19.310 63.440 33.296 1.00 41.55 ? 220 GLU A C 1 ATOM 1736 O O . GLU B 2 220 ? 20.316 63.670 32.622 1.00 42.65 ? 220 GLU A O 1 ATOM 1737 C CB . GLU B 2 220 ? 19.601 65.692 34.345 1.00 41.55 ? 220 GLU A CB 1 ATOM 1738 C CG . GLU B 2 220 ? 20.918 65.446 34.999 1.00 46.32 ? 220 GLU A CG 1 ATOM 1739 C CD . GLU B 2 220 ? 21.695 66.735 35.123 1.00 51.30 ? 220 GLU A CD 1 ATOM 1740 O OE1 . GLU B 2 220 ? 21.098 67.735 35.600 1.00 53.25 ? 220 GLU A OE1 1 ATOM 1741 O OE2 . GLU B 2 220 ? 22.890 66.754 34.743 1.00 54.68 ? 220 GLU A OE2 1 ATOM 1742 N N . SER B 2 221 ? 18.678 62.277 33.298 1.00 41.72 ? 221 SER A N 1 ATOM 1743 C CA . SER B 2 221 ? 19.098 61.168 32.478 1.00 40.69 ? 221 SER A CA 1 ATOM 1744 C C . SER B 2 221 ? 18.186 61.228 31.276 1.00 41.27 ? 221 SER A C 1 ATOM 1745 O O . SER B 2 221 ? 17.153 61.898 31.305 1.00 40.47 ? 221 SER A O 1 ATOM 1746 C CB . SER B 2 221 ? 18.853 59.853 33.206 1.00 40.48 ? 221 SER A CB 1 ATOM 1747 O OG . SER B 2 221 ? 17.460 59.613 33.325 1.00 37.94 ? 221 SER A OG 1 ATOM 1748 N N . ASN B 2 222 ? 18.574 60.534 30.215 1.00 42.18 ? 222 ASN A N 1 ATOM 1749 C CA . ASN B 2 222 ? 17.752 60.478 29.023 1.00 42.16 ? 222 ASN A CA 1 ATOM 1750 C C . ASN B 2 222 ? 17.089 59.118 29.069 1.00 42.46 ? 222 ASN A C 1 ATOM 1751 O O . ASN B 2 222 ? 17.687 58.117 28.680 1.00 40.89 ? 222 ASN A O 1 ATOM 1752 C CB . ASN B 2 222 ? 18.589 60.574 27.752 1.00 41.93 ? 222 ASN A CB 1 ATOM 1753 C CG . ASN B 2 222 ? 17.730 60.689 26.507 1.00 41.55 ? 222 ASN A CG 1 ATOM 1754 O OD1 . ASN B 2 222 ? 16.581 60.247 26.486 1.00 39.88 ? 222 ASN A OD1 1 ATOM 1755 N ND2 . ASN B 2 222 ? 18.287 61.274 25.457 1.00 42.44 ? 222 ASN A ND2 1 ATOM 1756 N N . GLN B 2 223 ? 15.863 59.082 29.573 1.00 43.70 ? 223 GLN A N 1 ATOM 1757 C CA . GLN B 2 223 ? 15.119 57.835 29.655 1.00 45.50 ? 223 GLN A CA 1 ATOM 1758 C C . GLN B 2 223 ? 15.873 56.781 30.472 1.00 45.64 ? 223 GLN A C 1 ATOM 1759 O O . GLN B 2 223 ? 16.230 55.712 29.970 1.00 46.66 ? 223 GLN A O 1 ATOM 1760 C CB . GLN B 2 223 ? 14.830 57.315 28.237 1.00 46.36 ? 223 GLN A CB 1 ATOM 1761 C CG . GLN B 2 223 ? 14.223 58.369 27.309 1.00 44.91 ? 223 GLN A CG 1 ATOM 1762 C CD . GLN B 2 223 ? 13.760 57.804 25.984 1.00 44.94 ? 223 GLN A CD 1 ATOM 1763 O OE1 . GLN B 2 223 ? 14.550 57.264 25.202 1.00 43.74 ? 223 GLN A OE1 1 ATOM 1764 N NE2 . GLN B 2 223 ? 12.466 57.929 25.722 1.00 45.49 ? 223 GLN A NE2 1 ATOM 1765 N N . GLY B 2 224 ? 16.122 57.096 31.737 1.00 44.99 ? 224 GLY A N 1 ATOM 1766 C CA . GLY B 2 224 ? 16.805 56.156 32.599 1.00 42.92 ? 224 GLY A CA 1 ATOM 1767 C C . GLY B 2 224 ? 18.271 55.922 32.304 1.00 42.18 ? 224 GLY A C 1 ATOM 1768 O O . GLY B 2 224 ? 18.949 55.287 33.108 1.00 43.75 ? 224 GLY A O 1 ATOM 1769 N N . ALA B 2 225 ? 18.773 56.412 31.174 1.00 40.94 ? 225 ALA A N 1 ATOM 1770 C CA . ALA B 2 225 ? 20.187 56.215 30.853 1.00 40.57 ? 225 ALA A CA 1 ATOM 1771 C C . ALA B 2 225 ? 21.006 57.381 31.389 1.00 40.38 ? 225 ALA A C 1 ATOM 1772 O O . ALA B 2 225 ? 20.654 58.538 31.168 1.00 41.63 ? 225 ALA A O 1 ATOM 1773 C CB . ALA B 2 225 ? 20.383 56.093 29.343 1.00 39.60 ? 225 ALA A CB 1 ATOM 1774 N N . PHE B 2 226 ? 22.086 57.083 32.103 1.00 39.86 ? 226 PHE A N 1 ATOM 1775 C CA . PHE B 2 226 ? 22.933 58.140 32.642 1.00 39.08 ? 226 PHE A CA 1 ATOM 1776 C C . PHE B 2 226 ? 23.875 58.593 31.534 1.00 39.15 ? 226 PHE A C 1 ATOM 1777 O O . PHE B 2 226 ? 24.145 57.833 30.599 1.00 40.09 ? 226 PHE A O 1 ATOM 1778 C CB . PHE B 2 226 ? 23.775 57.631 33.817 1.00 38.38 ? 226 PHE A CB 1 ATOM 1779 C CG . PHE B 2 226 ? 22.983 57.278 35.045 1.00 36.63 ? 226 PHE A CG 1 ATOM 1780 C CD1 . PHE B 2 226 ? 21.602 57.419 35.080 1.00 36.11 ? 226 PHE A CD1 1 ATOM 1781 C CD2 . PHE B 2 226 ? 23.635 56.782 36.171 1.00 35.62 ? 226 PHE A CD2 1 ATOM 1782 C CE1 . PHE B 2 226 ? 20.883 57.062 36.225 1.00 36.44 ? 226 PHE A CE1 1 ATOM 1783 C CE2 . PHE B 2 226 ? 22.931 56.425 37.312 1.00 34.27 ? 226 PHE A CE2 1 ATOM 1784 C CZ . PHE B 2 226 ? 21.556 56.564 37.342 1.00 34.96 ? 226 PHE A CZ 1 ATOM 1785 N N . ALA B 2 227 ? 24.376 59.822 31.642 1.00 38.44 ? 227 ALA A N 1 ATOM 1786 C CA . ALA B 2 227 ? 25.307 60.353 30.650 1.00 37.01 ? 227 ALA A CA 1 ATOM 1787 C C . ALA B 2 227 ? 26.730 59.904 31.013 1.00 36.81 ? 227 ALA A C 1 ATOM 1788 O O . ALA B 2 227 ? 27.570 59.663 30.148 1.00 35.50 ? 227 ALA A O 1 ATOM 1789 C CB . ALA B 2 227 ? 25.213 61.874 30.620 1.00 35.69 ? 227 ALA A CB 1 ATOM 1790 N N . SER B 2 228 ? 26.979 59.786 32.311 1.00 37.70 ? 228 SER A N 1 ATOM 1791 C CA . SER B 2 228 ? 28.276 59.362 32.826 1.00 37.32 ? 228 SER A CA 1 ATOM 1792 C C . SER B 2 228 ? 28.011 58.345 33.923 1.00 36.78 ? 228 SER A C 1 ATOM 1793 O O . SER B 2 228 ? 27.067 58.490 34.705 1.00 36.41 ? 228 SER A O 1 ATOM 1794 C CB . SER B 2 228 ? 29.024 60.542 33.438 1.00 38.78 ? 228 SER A CB 1 ATOM 1795 O OG . SER B 2 228 ? 28.736 61.745 32.750 1.00 42.22 ? 228 SER A OG 1 ATOM 1796 N N . PRO B 2 229 ? 28.846 57.309 34.011 1.00 35.00 ? 229 PRO A N 1 ATOM 1797 C CA . PRO B 2 229 ? 28.618 56.313 35.057 1.00 36.00 ? 229 PRO A CA 1 ATOM 1798 C C . PRO B 2 229 ? 28.849 56.832 36.473 1.00 37.51 ? 229 PRO A C 1 ATOM 1799 O O . PRO B 2 229 ? 29.702 57.689 36.706 1.00 38.77 ? 229 PRO A O 1 ATOM 1800 C CB . PRO B 2 229 ? 29.598 55.204 34.688 1.00 35.44 ? 229 PRO A CB 1 ATOM 1801 C CG . PRO B 2 229 ? 30.719 55.956 34.071 1.00 34.44 ? 229 PRO A CG 1 ATOM 1802 C CD . PRO B 2 229 ? 30.003 56.945 33.183 1.00 33.82 ? 229 PRO A CD 1 ATOM 1803 N N . ILE B 2 230 ? 28.057 56.330 37.413 1.00 37.62 ? 230 ILE A N 1 ATOM 1804 C CA . ILE B 2 230 ? 28.224 56.691 38.816 1.00 37.45 ? 230 ILE A CA 1 ATOM 1805 C C . ILE B 2 230 ? 28.894 55.444 39.371 1.00 38.27 ? 230 ILE A C 1 ATOM 1806 O O . ILE B 2 230 ? 28.423 54.333 39.133 1.00 39.69 ? 230 ILE A O 1 ATOM 1807 C CB . ILE B 2 230 ? 26.878 56.882 39.555 1.00 36.35 ? 230 ILE A CB 1 ATOM 1808 C CG1 . ILE B 2 230 ? 26.113 58.081 38.982 1.00 35.27 ? 230 ILE A CG1 1 ATOM 1809 C CG2 . ILE B 2 230 ? 27.144 57.050 41.049 1.00 35.41 ? 230 ILE A CG2 1 ATOM 1810 C CD1 . ILE B 2 230 ? 26.791 59.419 39.183 1.00 34.83 ? 230 ILE A CD1 1 ATOM 1811 N N . GLN B 2 231 ? 29.991 55.601 40.093 1.00 38.41 ? 231 GLN A N 1 ATOM 1812 C CA . GLN B 2 231 ? 30.647 54.421 40.613 1.00 38.34 ? 231 GLN A CA 1 ATOM 1813 C C . GLN B 2 231 ? 30.311 54.135 42.068 1.00 37.52 ? 231 GLN A C 1 ATOM 1814 O O . GLN B 2 231 ? 30.356 55.024 42.921 1.00 37.90 ? 231 GLN A O 1 ATOM 1815 C CB . GLN B 2 231 ? 32.145 54.541 40.433 1.00 39.82 ? 231 GLN A CB 1 ATOM 1816 C CG . GLN B 2 231 ? 32.825 53.222 40.582 1.00 45.79 ? 231 GLN A CG 1 ATOM 1817 C CD . GLN B 2 231 ? 34.290 53.313 40.286 1.00 49.04 ? 231 GLN A CD 1 ATOM 1818 O OE1 . GLN B 2 231 ? 34.684 53.754 39.202 1.00 49.25 ? 231 GLN A OE1 1 ATOM 1819 N NE2 . GLN B 2 231 ? 35.118 52.896 41.247 1.00 50.53 ? 231 GLN A NE2 1 ATOM 1820 N N . LEU B 2 232 ? 29.969 52.882 42.342 1.00 36.48 ? 232 LEU A N 1 ATOM 1821 C CA . LEU B 2 232 ? 29.598 52.463 43.685 1.00 35.27 ? 232 LEU A CA 1 ATOM 1822 C C . LEU B 2 232 ? 30.465 51.288 44.131 1.00 36.64 ? 232 LEU A C 1 ATOM 1823 O O . LEU B 2 232 ? 31.283 50.784 43.358 1.00 36.61 ? 232 LEU A O 1 ATOM 1824 C CB . LEU B 2 232 ? 28.121 52.062 43.705 1.00 33.18 ? 232 LEU A CB 1 ATOM 1825 C CG . LEU B 2 232 ? 27.115 53.063 43.117 1.00 30.83 ? 232 LEU A CG 1 ATOM 1826 C CD1 . LEU B 2 232 ? 25.780 52.365 42.918 1.00 28.16 ? 232 LEU A CD1 1 ATOM 1827 C CD2 . LEU B 2 232 ? 26.968 54.277 44.021 1.00 27.50 ? 232 LEU A CD2 1 ATOM 1828 N N . GLN B 2 233 ? 30.281 50.856 45.376 1.00 37.08 ? 233 GLN A N 1 ATOM 1829 C CA . GLN B 2 233 ? 31.045 49.745 45.929 1.00 37.00 ? 233 GLN A CA 1 ATOM 1830 C C . GLN B 2 233 ? 30.152 48.641 46.442 1.00 36.26 ? 233 GLN A C 1 ATOM 1831 O O . GLN B 2 233 ? 28.971 48.852 46.688 1.00 35.93 ? 233 GLN A O 1 ATOM 1832 C CB . GLN B 2 233 ? 31.915 50.211 47.086 1.00 37.87 ? 233 GLN A CB 1 ATOM 1833 C CG . GLN B 2 233 ? 33.213 50.834 46.680 1.00 41.40 ? 233 GLN A CG 1 ATOM 1834 C CD . GLN B 2 233 ? 34.058 51.181 47.883 1.00 43.29 ? 233 GLN A CD 1 ATOM 1835 O OE1 . GLN B 2 233 ? 33.720 52.072 48.658 1.00 43.76 ? 233 GLN A OE1 1 ATOM 1836 N NE2 . GLN B 2 233 ? 35.160 50.466 48.055 1.00 45.44 ? 233 GLN A NE2 1 ATOM 1837 N N . ARG B 2 234 ? 30.738 47.464 46.615 1.00 36.40 ? 234 ARG A N 1 ATOM 1838 C CA . ARG B 2 234 ? 30.017 46.315 47.121 1.00 37.41 ? 234 ARG A CA 1 ATOM 1839 C C . ARG B 2 234 ? 30.364 46.155 48.587 1.00 39.43 ? 234 ARG A C 1 ATOM 1840 O O . ARG B 2 234 ? 31.149 46.928 49.129 1.00 40.01 ? 234 ARG A O 1 ATOM 1841 C CB . ARG B 2 234 ? 30.424 45.067 46.351 1.00 36.02 ? 234 ARG A CB 1 ATOM 1842 C CG . ARG B 2 234 ? 29.884 45.031 44.951 1.00 37.22 ? 234 ARG A CG 1 ATOM 1843 C CD . ARG B 2 234 ? 30.424 43.849 44.182 1.00 41.10 ? 234 ARG A CD 1 ATOM 1844 N NE . ARG B 2 234 ? 29.506 43.468 43.117 1.00 45.46 ? 234 ARG A NE 1 ATOM 1845 C CZ . ARG B 2 234 ? 28.337 42.869 43.326 1.00 47.88 ? 234 ARG A CZ 1 ATOM 1846 N NH1 . ARG B 2 234 ? 27.946 42.572 44.564 1.00 46.41 ? 234 ARG A NH1 1 ATOM 1847 N NH2 . ARG B 2 234 ? 27.550 42.584 42.293 1.00 49.35 ? 234 ARG A NH2 1 ATOM 1848 N N . ARG B 2 235 ? 29.779 45.157 49.233 1.00 42.37 ? 235 ARG A N 1 ATOM 1849 C CA . ARG B 2 235 ? 30.069 44.921 50.639 1.00 45.99 ? 235 ARG A CA 1 ATOM 1850 C C . ARG B 2 235 ? 31.548 44.557 50.814 1.00 46.35 ? 235 ARG A C 1 ATOM 1851 O O . ARG B 2 235 ? 32.186 44.989 51.778 1.00 48.10 ? 235 ARG A O 1 ATOM 1852 C CB . ARG B 2 235 ? 29.189 43.792 51.182 1.00 48.81 ? 235 ARG A CB 1 ATOM 1853 C CG . ARG B 2 235 ? 27.701 44.049 51.038 1.00 53.57 ? 235 ARG A CG 1 ATOM 1854 C CD . ARG B 2 235 ? 26.877 42.818 51.398 1.00 58.86 ? 235 ARG A CD 1 ATOM 1855 N NE . ARG B 2 235 ? 27.099 42.421 52.782 1.00 65.05 ? 235 ARG A NE 1 ATOM 1856 C CZ . ARG B 2 235 ? 26.819 43.194 53.828 1.00 68.29 ? 235 ARG A CZ 1 ATOM 1857 N NH1 . ARG B 2 235 ? 26.305 44.403 53.640 1.00 70.10 ? 235 ARG A NH1 1 ATOM 1858 N NH2 . ARG B 2 235 ? 27.061 42.765 55.063 1.00 70.55 ? 235 ARG A NH2 1 ATOM 1859 N N . ASN B 2 236 ? 32.097 43.773 49.882 1.00 45.67 ? 236 ASN A N 1 ATOM 1860 C CA . ASN B 2 236 ? 33.502 43.372 49.980 1.00 44.32 ? 236 ASN A CA 1 ATOM 1861 C C . ASN B 2 236 ? 34.489 44.477 49.578 1.00 44.25 ? 236 ASN A C 1 ATOM 1862 O O . ASN B 2 236 ? 35.701 44.301 49.716 1.00 45.72 ? 236 ASN A O 1 ATOM 1863 C CB . ASN B 2 236 ? 33.781 42.097 49.157 1.00 41.42 ? 236 ASN A CB 1 ATOM 1864 C CG . ASN B 2 236 ? 33.721 42.331 47.648 1.00 40.28 ? 236 ASN A CG 1 ATOM 1865 O OD1 . ASN B 2 236 ? 34.269 43.306 47.136 1.00 39.01 ? 236 ASN A OD1 1 ATOM 1866 N ND2 . ASN B 2 236 ? 33.072 41.418 46.929 1.00 39.47 ? 236 ASN A ND2 1 ATOM 1867 N N . GLY B 2 237 ? 33.980 45.606 49.082 1.00 42.34 ? 237 GLY A N 1 ATOM 1868 C CA . GLY B 2 237 ? 34.859 46.696 48.695 1.00 39.97 ? 237 GLY A CA 1 ATOM 1869 C C . GLY B 2 237 ? 35.105 46.871 47.208 1.00 39.24 ? 237 GLY A C 1 ATOM 1870 O O . GLY B 2 237 ? 35.484 47.955 46.772 1.00 38.23 ? 237 GLY A O 1 ATOM 1871 N N . SER B 2 238 ? 34.909 45.816 46.426 1.00 39.61 ? 238 SER A N 1 ATOM 1872 C CA . SER B 2 238 ? 35.106 45.889 44.977 1.00 40.44 ? 238 SER A CA 1 ATOM 1873 C C . SER B 2 238 ? 34.133 46.898 44.358 1.00 41.71 ? 238 SER A C 1 ATOM 1874 O O . SER B 2 238 ? 32.965 46.956 44.746 1.00 42.93 ? 238 SER A O 1 ATOM 1875 C CB . SER B 2 238 ? 34.892 44.510 44.351 1.00 39.56 ? 238 SER A CB 1 ATOM 1876 O OG . SER B 2 238 ? 33.594 44.014 44.626 1.00 38.25 ? 238 SER A OG 1 ATOM 1877 N N . LYS B 2 239 ? 34.607 47.687 43.395 1.00 41.91 ? 239 LYS A N 1 ATOM 1878 C CA . LYS B 2 239 ? 33.757 48.695 42.764 1.00 42.16 ? 239 LYS A CA 1 ATOM 1879 C C . LYS B 2 239 ? 33.059 48.168 41.524 1.00 40.63 ? 239 LYS A C 1 ATOM 1880 O O . LYS B 2 239 ? 33.448 47.139 40.970 1.00 40.64 ? 239 LYS A O 1 ATOM 1881 C CB . LYS B 2 239 ? 34.573 49.937 42.369 1.00 43.81 ? 239 LYS A CB 1 ATOM 1882 C CG . LYS B 2 239 ? 35.978 49.979 42.941 1.00 47.50 ? 239 LYS A CG 1 ATOM 1883 C CD . LYS B 2 239 ? 36.180 51.116 43.942 1.00 49.41 ? 239 LYS A CD 1 ATOM 1884 C CE . LYS B 2 239 ? 37.630 51.128 44.459 1.00 51.07 ? 239 LYS A CE 1 ATOM 1885 N NZ . LYS B 2 239 ? 37.977 52.300 45.325 1.00 51.45 ? 239 LYS A NZ 1 ATOM 1886 N N . PHE B 2 240 ? 32.011 48.887 41.123 1.00 39.22 ? 240 PHE A N 1 ATOM 1887 C CA . PHE B 2 240 ? 31.221 48.595 39.931 1.00 37.89 ? 240 PHE A CA 1 ATOM 1888 C C . PHE B 2 240 ? 30.541 49.896 39.490 1.00 38.03 ? 240 PHE A C 1 ATOM 1889 O O . PHE B 2 240 ? 30.223 50.759 40.313 1.00 39.41 ? 240 PHE A O 1 ATOM 1890 C CB . PHE B 2 240 ? 30.183 47.490 40.184 1.00 35.66 ? 240 PHE A CB 1 ATOM 1891 C CG . PHE B 2 240 ? 29.090 47.872 41.121 1.00 35.88 ? 240 PHE A CG 1 ATOM 1892 C CD1 . PHE B 2 240 ? 29.305 47.890 42.491 1.00 36.44 ? 240 PHE A CD1 1 ATOM 1893 C CD2 . PHE B 2 240 ? 27.827 48.190 40.634 1.00 36.49 ? 240 PHE A CD2 1 ATOM 1894 C CE1 . PHE B 2 240 ? 28.267 48.217 43.375 1.00 39.17 ? 240 PHE A CE1 1 ATOM 1895 C CE2 . PHE B 2 240 ? 26.779 48.519 41.502 1.00 38.37 ? 240 PHE A CE2 1 ATOM 1896 C CZ . PHE B 2 240 ? 26.998 48.533 42.875 1.00 38.25 ? 240 PHE A CZ 1 ATOM 1897 N N . SER B 2 241 ? 30.341 50.044 38.186 1.00 36.86 ? 241 SER A N 1 ATOM 1898 C CA . SER B 2 241 ? 29.741 51.253 37.651 1.00 34.30 ? 241 SER A CA 1 ATOM 1899 C C . SER B 2 241 ? 28.298 51.069 37.240 1.00 32.92 ? 241 SER A C 1 ATOM 1900 O O . SER B 2 241 ? 27.928 50.050 36.663 1.00 32.71 ? 241 SER A O 1 ATOM 1901 C CB . SER B 2 241 ? 30.542 51.743 36.449 1.00 35.04 ? 241 SER A CB 1 ATOM 1902 O OG . SER B 2 241 ? 31.883 52.002 36.820 1.00 35.95 ? 241 SER A OG 1 ATOM 1903 N N . VAL B 2 242 ? 27.493 52.080 37.536 1.00 31.36 ? 242 VAL A N 1 ATOM 1904 C CA . VAL B 2 242 ? 26.082 52.072 37.208 1.00 30.00 ? 242 VAL A CA 1 ATOM 1905 C C . VAL B 2 242 ? 25.843 53.049 36.064 1.00 29.47 ? 242 VAL A C 1 ATOM 1906 O O . VAL B 2 242 ? 26.240 54.209 36.145 1.00 29.01 ? 242 VAL A O 1 ATOM 1907 C CB . VAL B 2 242 ? 25.255 52.487 38.421 1.00 29.45 ? 242 VAL A CB 1 ATOM 1908 C CG1 . VAL B 2 242 ? 23.786 52.449 38.081 1.00 31.53 ? 242 VAL A CG1 1 ATOM 1909 C CG2 . VAL B 2 242 ? 25.554 51.557 39.582 1.00 30.14 ? 242 VAL A CG2 1 ATOM 1910 N N . TYR B 2 243 ? 25.197 52.565 35.003 1.00 29.17 ? 243 TYR A N 1 ATOM 1911 C CA . TYR B 2 243 ? 24.915 53.365 33.815 1.00 29.35 ? 243 TYR A CA 1 ATOM 1912 C C . TYR B 2 243 ? 23.439 53.638 33.661 1.00 29.42 ? 243 TYR A C 1 ATOM 1913 O O . TYR B 2 243 ? 23.051 54.579 32.974 1.00 30.91 ? 243 TYR A O 1 ATOM 1914 C CB . TYR B 2 243 ? 25.414 52.637 32.561 1.00 30.04 ? 243 TYR A CB 1 ATOM 1915 C CG . TYR B 2 243 ? 26.912 52.449 32.527 1.00 31.34 ? 243 TYR A CG 1 ATOM 1916 C CD1 . TYR B 2 243 ? 27.747 53.448 32.042 1.00 30.83 ? 243 TYR A CD1 1 ATOM 1917 C CD2 . TYR B 2 243 ? 27.500 51.299 33.060 1.00 32.24 ? 243 TYR A CD2 1 ATOM 1918 C CE1 . TYR B 2 243 ? 29.129 53.316 32.095 1.00 31.86 ? 243 TYR A CE1 1 ATOM 1919 C CE2 . TYR B 2 243 ? 28.881 51.157 33.120 1.00 32.08 ? 243 TYR A CE2 1 ATOM 1920 C CZ . TYR B 2 243 ? 29.685 52.171 32.640 1.00 32.55 ? 243 TYR A CZ 1 ATOM 1921 O OH . TYR B 2 243 ? 31.048 52.050 32.733 1.00 34.16 ? 243 TYR A OH 1 ATOM 1922 N N . ASP B 2 244 ? 22.615 52.815 34.299 1.00 29.82 ? 244 ASP A N 1 ATOM 1923 C CA . ASP B 2 244 ? 21.174 52.968 34.193 1.00 29.97 ? 244 ASP A CA 1 ATOM 1924 C C . ASP B 2 244 ? 20.458 53.180 35.519 1.00 29.19 ? 244 ASP A C 1 ATOM 1925 O O . ASP B 2 244 ? 20.971 52.822 36.568 1.00 28.35 ? 244 ASP A O 1 ATOM 1926 C CB . ASP B 2 244 ? 20.582 51.750 33.509 1.00 33.59 ? 244 ASP A CB 1 ATOM 1927 C CG . ASP B 2 244 ? 19.401 52.103 32.659 1.00 39.05 ? 244 ASP A CG 1 ATOM 1928 O OD1 . ASP B 2 244 ? 19.639 52.633 31.551 1.00 43.39 ? 244 ASP A OD1 1 ATOM 1929 O OD2 . ASP B 2 244 ? 18.242 51.876 33.094 1.00 41.63 ? 244 ASP A OD2 1 ATOM 1930 N N . VAL B 2 245 ? 19.253 53.740 35.454 1.00 28.99 ? 245 VAL A N 1 ATOM 1931 C CA . VAL B 2 245 ? 18.446 54.018 36.643 1.00 30.43 ? 245 VAL A CA 1 ATOM 1932 C C . VAL B 2 245 ? 17.805 52.776 37.265 1.00 31.67 ? 245 VAL A C 1 ATOM 1933 O O . VAL B 2 245 ? 17.738 52.642 38.487 1.00 31.40 ? 245 VAL A O 1 ATOM 1934 C CB . VAL B 2 245 ? 17.314 55.034 36.327 1.00 29.88 ? 245 VAL A CB 1 ATOM 1935 C CG1 . VAL B 2 245 ? 16.329 54.427 35.365 1.00 30.43 ? 245 VAL A CG1 1 ATOM 1936 C CG2 . VAL B 2 245 ? 16.598 55.435 37.596 1.00 30.31 ? 245 VAL A CG2 1 ATOM 1937 N N . SER B 2 246 ? 17.339 51.871 36.409 1.00 33.87 ? 246 SER A N 1 ATOM 1938 C CA . SER B 2 246 ? 16.673 50.634 36.828 1.00 35.77 ? 246 SER A CA 1 ATOM 1939 C C . SER B 2 246 ? 17.309 49.854 37.982 1.00 36.12 ? 246 SER A C 1 ATOM 1940 O O . SER B 2 246 ? 16.601 49.343 38.850 1.00 37.72 ? 246 SER A O 1 ATOM 1941 C CB . SER B 2 246 ? 16.520 49.697 35.624 1.00 35.11 ? 246 SER A CB 1 ATOM 1942 O OG . SER B 2 246 ? 17.783 49.284 35.141 1.00 34.36 ? 246 SER A OG 1 ATOM 1943 N N . ILE B 2 247 ? 18.634 49.746 37.991 1.00 35.88 ? 247 ILE A N 1 ATOM 1944 C CA . ILE B 2 247 ? 19.312 49.003 39.052 1.00 34.82 ? 247 ILE A CA 1 ATOM 1945 C C . ILE B 2 247 ? 19.257 49.710 40.401 1.00 33.15 ? 247 ILE A C 1 ATOM 1946 O O . ILE B 2 247 ? 19.523 49.101 41.432 1.00 32.22 ? 247 ILE A O 1 ATOM 1947 C CB . ILE B 2 247 ? 20.793 48.738 38.691 1.00 35.35 ? 247 ILE A CB 1 ATOM 1948 C CG1 . ILE B 2 247 ? 21.506 48.081 39.873 1.00 36.53 ? 247 ILE A CG1 1 ATOM 1949 C CG2 . ILE B 2 247 ? 21.476 50.033 38.296 1.00 33.38 ? 247 ILE A CG2 1 ATOM 1950 C CD1 . ILE B 2 247 ? 22.986 47.841 39.648 1.00 39.82 ? 247 ILE A CD1 1 ATOM 1951 N N . LEU B 2 248 ? 18.900 50.993 40.386 1.00 30.87 ? 248 LEU A N 1 ATOM 1952 C CA . LEU B 2 248 ? 18.832 51.796 41.603 1.00 28.82 ? 248 LEU A CA 1 ATOM 1953 C C . LEU B 2 248 ? 17.425 51.933 42.175 1.00 28.13 ? 248 LEU A C 1 ATOM 1954 O O . LEU B 2 248 ? 17.256 52.318 43.331 1.00 29.37 ? 248 LEU A O 1 ATOM 1955 C CB . LEU B 2 248 ? 19.389 53.199 41.342 1.00 26.75 ? 248 LEU A CB 1 ATOM 1956 C CG . LEU B 2 248 ? 20.866 53.352 41.000 1.00 26.17 ? 248 LEU A CG 1 ATOM 1957 C CD1 . LEU B 2 248 ? 21.139 54.800 40.648 1.00 25.58 ? 248 LEU A CD1 1 ATOM 1958 C CD2 . LEU B 2 248 ? 21.726 52.899 42.171 1.00 25.86 ? 248 LEU A CD2 1 ATOM 1959 N N . ILE B 2 249 ? 16.413 51.627 41.375 1.00 26.26 ? 249 ILE A N 1 ATOM 1960 C CA . ILE B 2 249 ? 15.047 51.752 41.840 1.00 25.12 ? 249 ILE A CA 1 ATOM 1961 C C . ILE B 2 249 ? 14.766 51.072 43.184 1.00 26.16 ? 249 ILE A C 1 ATOM 1962 O O . ILE B 2 249 ? 14.038 51.618 44.011 1.00 28.55 ? 249 ILE A O 1 ATOM 1963 C CB . ILE B 2 249 ? 14.065 51.244 40.778 1.00 23.24 ? 249 ILE A CB 1 ATOM 1964 C CG1 . ILE B 2 249 ? 14.190 52.119 39.526 1.00 24.65 ? 249 ILE A CG1 1 ATOM 1965 C CG2 . ILE B 2 249 ? 12.663 51.283 41.321 1.00 22.09 ? 249 ILE A CG2 1 ATOM 1966 C CD1 . ILE B 2 249 ? 13.217 51.797 38.416 1.00 23.60 ? 249 ILE A CD1 1 ATOM 1967 N N . PRO B 2 250 ? 15.335 49.878 43.433 1.00 26.16 ? 250 PRO A N 1 ATOM 1968 C CA . PRO B 2 250 ? 15.035 49.273 44.734 1.00 25.94 ? 250 PRO A CA 1 ATOM 1969 C C . PRO B 2 250 ? 16.025 49.653 45.831 1.00 26.58 ? 250 PRO A C 1 ATOM 1970 O O . PRO B 2 250 ? 15.958 49.113 46.933 1.00 27.22 ? 250 PRO A O 1 ATOM 1971 C CB . PRO B 2 250 ? 15.072 47.788 44.426 1.00 25.61 ? 250 PRO A CB 1 ATOM 1972 C CG . PRO B 2 250 ? 16.175 47.705 43.439 1.00 23.69 ? 250 PRO A CG 1 ATOM 1973 C CD . PRO B 2 250 ? 15.894 48.870 42.512 1.00 25.02 ? 250 PRO A CD 1 ATOM 1974 N N . ILE B 2 251 ? 16.926 50.590 45.531 1.00 26.01 ? 251 ILE A N 1 ATOM 1975 C CA . ILE B 2 251 ? 17.953 51.038 46.478 1.00 25.33 ? 251 ILE A CA 1 ATOM 1976 C C . ILE B 2 251 ? 17.790 52.459 47.025 1.00 24.81 ? 251 ILE A C 1 ATOM 1977 O O . ILE B 2 251 ? 18.065 52.706 48.202 1.00 24.70 ? 251 ILE A O 1 ATOM 1978 C CB . ILE B 2 251 ? 19.334 50.914 45.849 1.00 24.36 ? 251 ILE A CB 1 ATOM 1979 C CG1 . ILE B 2 251 ? 19.611 49.450 45.552 1.00 25.91 ? 251 ILE A CG1 1 ATOM 1980 C CG2 . ILE B 2 251 ? 20.387 51.438 46.776 1.00 23.47 ? 251 ILE A CG2 1 ATOM 1981 C CD1 . ILE B 2 251 ? 20.800 49.257 44.663 1.00 31.10 ? 251 ILE A CD1 1 ATOM 1982 N N . ILE B 2 252 ? 17.363 53.397 46.180 1.00 24.34 ? 252 ILE A N 1 ATOM 1983 C CA . ILE B 2 252 ? 17.149 54.775 46.630 1.00 23.24 ? 252 ILE A CA 1 ATOM 1984 C C . ILE B 2 252 ? 15.674 54.948 46.990 1.00 21.61 ? 252 ILE A C 1 ATOM 1985 O O . ILE B 2 252 ? 14.789 54.404 46.324 1.00 21.35 ? 252 ILE A O 1 ATOM 1986 C CB . ILE B 2 252 ? 17.512 55.817 45.537 1.00 23.31 ? 252 ILE A CB 1 ATOM 1987 C CG1 . ILE B 2 252 ? 18.923 55.563 45.023 1.00 24.18 ? 252 ILE A CG1 1 ATOM 1988 C CG2 . ILE B 2 252 ? 17.451 57.232 46.113 1.00 22.59 ? 252 ILE A CG2 1 ATOM 1989 C CD1 . ILE B 2 252 ? 19.465 56.680 44.157 1.00 25.75 ? 252 ILE A CD1 1 ATOM 1990 N N . ALA B 2 253 ? 15.407 55.700 48.048 1.00 20.36 ? 253 ALA A N 1 ATOM 1991 C CA . ALA B 2 253 ? 14.035 55.918 48.472 1.00 20.91 ? 253 ALA A CA 1 ATOM 1992 C C . ALA B 2 253 ? 13.624 57.371 48.334 1.00 21.53 ? 253 ALA A C 1 ATOM 1993 O O . ALA B 2 253 ? 12.437 57.671 48.227 1.00 23.36 ? 253 ALA A O 1 ATOM 1994 C CB . ALA B 2 253 ? 13.858 55.466 49.906 1.00 20.21 ? 253 ALA A CB 1 ATOM 1995 N N . LEU B 2 254 ? 14.607 58.267 48.326 1.00 21.56 ? 254 LEU A N 1 ATOM 1996 C CA . LEU B 2 254 ? 14.359 59.705 48.217 1.00 21.61 ? 254 LEU A CA 1 ATOM 1997 C C . LEU B 2 254 ? 15.444 60.395 47.391 1.00 22.58 ? 254 LEU A C 1 ATOM 1998 O O . LEU B 2 254 ? 16.602 59.981 47.397 1.00 23.41 ? 254 LEU A O 1 ATOM 1999 C CB . LEU B 2 254 ? 14.331 60.340 49.615 1.00 21.03 ? 254 LEU A CB 1 ATOM 2000 C CG . LEU B 2 254 ? 13.262 59.928 50.634 1.00 22.55 ? 254 LEU A CG 1 ATOM 2001 C CD1 . LEU B 2 254 ? 13.686 60.390 52.025 1.00 23.10 ? 254 LEU A CD1 1 ATOM 2002 C CD2 . LEU B 2 254 ? 11.916 60.518 50.253 1.00 19.16 ? 254 LEU A CD2 1 ATOM 2003 N N . MET B 2 255 ? 15.065 61.448 46.681 1.00 24.02 ? 255 MET A N 1 ATOM 2004 C CA . MET B 2 255 ? 16.013 62.203 45.877 1.00 26.17 ? 255 MET A CA 1 ATOM 2005 C C . MET B 2 255 ? 15.910 63.690 46.191 1.00 28.24 ? 255 MET A C 1 ATOM 2006 O O . MET B 2 255 ? 14.811 64.221 46.342 1.00 28.66 ? 255 MET A O 1 ATOM 2007 C CB . MET B 2 255 ? 15.741 62.014 44.384 1.00 26.86 ? 255 MET A CB 1 ATOM 2008 C CG . MET B 2 255 ? 16.447 60.851 43.729 1.00 28.18 ? 255 MET A CG 1 ATOM 2009 S SD . MET B 2 255 ? 16.171 60.877 41.951 1.00 30.42 ? 255 MET A SD 1 ATOM 2010 C CE . MET B 2 255 ? 14.444 60.422 41.868 1.00 28.21 ? 255 MET A CE 1 ATOM 2011 N N . VAL B 2 256 ? 17.052 64.362 46.296 1.00 28.93 ? 256 VAL A N 1 ATOM 2012 C CA . VAL B 2 256 ? 17.054 65.795 46.544 1.00 28.79 ? 256 VAL A CA 1 ATOM 2013 C C . VAL B 2 256 ? 16.724 66.441 45.190 1.00 30.55 ? 256 VAL A C 1 ATOM 2014 O O . VAL B 2 256 ? 17.322 66.102 44.174 1.00 30.11 ? 256 VAL A O 1 ATOM 2015 C CB . VAL B 2 256 ? 18.445 66.265 47.065 1.00 26.51 ? 256 VAL A CB 1 ATOM 2016 C CG1 . VAL B 2 256 ? 19.542 65.855 46.100 1.00 23.74 ? 256 VAL A CG1 1 ATOM 2017 C CG2 . VAL B 2 256 ? 18.442 67.764 47.273 1.00 23.24 ? 256 VAL A CG2 1 ATOM 2018 N N . TYR B 2 257 ? 15.747 67.340 45.170 1.00 32.33 ? 257 TYR A N 1 ATOM 2019 C CA . TYR B 2 257 ? 15.331 68.007 43.932 1.00 34.29 ? 257 TYR A CA 1 ATOM 2020 C C . TYR B 2 257 ? 16.493 68.728 43.253 1.00 36.04 ? 257 TYR A C 1 ATOM 2021 O O . TYR B 2 257 ? 17.185 69.522 43.886 1.00 37.21 ? 257 TYR A O 1 ATOM 2022 C CB . TYR B 2 257 ? 14.211 69.001 44.249 1.00 33.96 ? 257 TYR A CB 1 ATOM 2023 C CG . TYR B 2 257 ? 13.663 69.767 43.062 1.00 34.28 ? 257 TYR A CG 1 ATOM 2024 C CD1 . TYR B 2 257 ? 14.476 70.625 42.322 1.00 34.08 ? 257 TYR A CD1 1 ATOM 2025 C CD2 . TYR B 2 257 ? 12.310 69.669 42.705 1.00 33.98 ? 257 TYR A CD2 1 ATOM 2026 C CE1 . TYR B 2 257 ? 13.962 71.372 41.260 1.00 34.76 ? 257 TYR A CE1 1 ATOM 2027 C CE2 . TYR B 2 257 ? 11.784 70.415 41.643 1.00 33.42 ? 257 TYR A CE2 1 ATOM 2028 C CZ . TYR B 2 257 ? 12.620 71.264 40.929 1.00 34.09 ? 257 TYR A CZ 1 ATOM 2029 O OH . TYR B 2 257 ? 12.132 72.021 39.890 1.00 33.90 ? 257 TYR A OH 1 ATOM 2030 N N . ARG B 2 258 ? 16.689 68.466 41.961 1.00 37.16 ? 258 ARG A N 1 ATOM 2031 C CA . ARG B 2 258 ? 17.775 69.087 41.199 1.00 38.25 ? 258 ARG A CA 1 ATOM 2032 C C . ARG B 2 258 ? 17.326 70.024 40.088 1.00 39.14 ? 258 ARG A C 1 ATOM 2033 O O . ARG B 2 258 ? 17.900 71.094 39.898 1.00 39.63 ? 258 ARG A O 1 ATOM 2034 C CB . ARG B 2 258 ? 18.669 68.020 40.577 1.00 38.78 ? 258 ARG A CB 1 ATOM 2035 C CG . ARG B 2 258 ? 19.542 67.296 41.558 1.00 42.67 ? 258 ARG A CG 1 ATOM 2036 C CD . ARG B 2 258 ? 20.396 68.264 42.355 1.00 45.26 ? 258 ARG A CD 1 ATOM 2037 N NE . ARG B 2 258 ? 21.423 67.549 43.102 1.00 50.67 ? 258 ARG A NE 1 ATOM 2038 C CZ . ARG B 2 258 ? 22.230 68.113 43.993 1.00 52.56 ? 258 ARG A CZ 1 ATOM 2039 N NH1 . ARG B 2 258 ? 22.128 69.409 44.256 1.00 55.02 ? 258 ARG A NH1 1 ATOM 2040 N NH2 . ARG B 2 258 ? 23.148 67.382 44.616 1.00 53.63 ? 258 ARG A NH2 1 ATOM 2041 N N . CYS B 2 259 ? 16.312 69.608 39.341 1.00 41.11 ? 259 CYS A N 1 ATOM 2042 C CA . CYS B 2 259 ? 15.809 70.397 38.229 1.00 43.44 ? 259 CYS A CA 1 ATOM 2043 C C . CYS B 2 259 ? 14.368 69.994 37.926 1.00 43.97 ? 259 CYS A C 1 ATOM 2044 O O . CYS B 2 259 ? 13.948 68.895 38.272 1.00 43.90 ? 259 CYS A O 1 ATOM 2045 C CB . CYS B 2 259 ? 16.704 70.174 37.004 1.00 46.13 ? 259 CYS A CB 1 ATOM 2046 S SG . CYS B 2 259 ? 17.047 68.414 36.667 1.00 50.91 ? 259 CYS A SG 1 ATOM 2047 N N . ALA B 2 260 ? 13.618 70.886 37.280 1.00 45.30 ? 260 ALA A N 1 ATOM 2048 C CA . ALA B 2 260 ? 12.222 70.632 36.950 1.00 46.94 ? 260 ALA A CA 1 ATOM 2049 C C . ALA B 2 260 ? 12.058 69.699 35.763 1.00 50.56 ? 260 ALA A C 1 ATOM 2050 O O . ALA B 2 260 ? 12.900 69.664 34.868 1.00 50.45 ? 260 ALA A O 1 ATOM 2051 C CB . ALA B 2 260 ? 11.515 71.939 36.669 1.00 45.51 ? 260 ALA A CB 1 ATOM 2052 N N . PRO B 2 261 ? 10.958 68.926 35.742 1.00 53.66 ? 261 PRO A N 1 ATOM 2053 C CA . PRO B 2 261 ? 10.673 67.984 34.653 1.00 57.36 ? 261 PRO A CA 1 ATOM 2054 C C . PRO B 2 261 ? 10.313 68.773 33.395 1.00 60.79 ? 261 PRO A C 1 ATOM 2055 O O . PRO B 2 261 ? 9.792 69.890 33.489 1.00 61.18 ? 261 PRO A O 1 ATOM 2056 C CB . PRO B 2 261 ? 9.463 67.197 35.169 1.00 56.34 ? 261 PRO A CB 1 ATOM 2057 C CG . PRO B 2 261 ? 9.495 67.397 36.659 1.00 55.93 ? 261 PRO A CG 1 ATOM 2058 C CD . PRO B 2 261 ? 9.940 68.823 36.801 1.00 54.74 ? 261 PRO A CD 1 ATOM 2059 N N . PRO B 2 262 ? 10.603 68.218 32.204 1.00 62.26 ? 262 PRO A N 1 ATOM 2060 C CA . PRO B 2 262 ? 10.258 68.951 30.977 1.00 63.89 ? 262 PRO A CA 1 ATOM 2061 C C . PRO B 2 262 ? 8.743 68.957 30.711 1.00 64.49 ? 262 PRO A C 1 ATOM 2062 O O . PRO B 2 262 ? 8.048 68.030 31.195 1.00 64.31 ? 262 PRO A O 1 ATOM 2063 C CB . PRO B 2 262 ? 11.037 68.199 29.896 1.00 63.34 ? 262 PRO A CB 1 ATOM 2064 C CG . PRO B 2 262 ? 12.260 67.715 30.642 1.00 63.71 ? 262 PRO A CG 1 ATOM 2065 C CD . PRO B 2 262 ? 11.634 67.200 31.932 1.00 64.00 ? 262 PRO A CD 1 ATOM 2066 N N . ALA C 3 1 ? 17.506 74.488 39.737 1.00 66.85 ? 1 ALA B N 1 ATOM 2067 C CA . ALA C 3 1 ? 18.166 75.343 38.705 1.00 67.52 ? 1 ALA B CA 1 ATOM 2068 C C . ALA C 3 1 ? 17.718 74.933 37.303 1.00 67.34 ? 1 ALA B C 1 ATOM 2069 O O . ALA C 3 1 ? 18.083 73.858 36.812 1.00 68.45 ? 1 ALA B O 1 ATOM 2070 C CB . ALA C 3 1 ? 19.700 75.236 38.824 1.00 66.56 ? 1 ALA B CB 1 ATOM 2071 N N . ASP C 3 2 ? 16.927 75.793 36.667 1.00 67.27 ? 2 ASP B N 1 ATOM 2072 C CA . ASP C 3 2 ? 16.425 75.536 35.317 1.00 66.24 ? 2 ASP B CA 1 ATOM 2073 C C . ASP C 3 2 ? 15.498 74.331 35.300 1.00 64.71 ? 2 ASP B C 1 ATOM 2074 O O . ASP C 3 2 ? 15.004 73.879 36.337 1.00 64.16 ? 2 ASP B O 1 ATOM 2075 C CB . ASP C 3 2 ? 17.583 75.249 34.339 1.00 67.84 ? 2 ASP B CB 1 ATOM 2076 C CG . ASP C 3 2 ? 18.562 76.407 34.217 1.00 69.15 ? 2 ASP B CG 1 ATOM 2077 O OD1 . ASP C 3 2 ? 18.130 77.515 33.821 1.00 69.72 ? 2 ASP B OD1 1 ATOM 2078 O OD2 . ASP C 3 2 ? 19.763 76.195 34.513 1.00 69.72 ? 2 ASP B OD2 1 ATOM 2079 N N . VAL C 3 3 ? 15.268 73.832 34.089 1.00 64.04 ? 3 VAL B N 1 ATOM 2080 C CA . VAL C 3 3 ? 14.454 72.649 33.869 1.00 63.05 ? 3 VAL B CA 1 ATOM 2081 C C . VAL C 3 3 ? 15.504 71.586 33.563 1.00 61.68 ? 3 VAL B C 1 ATOM 2082 O O . VAL C 3 3 ? 16.600 71.913 33.103 1.00 61.85 ? 3 VAL B O 1 ATOM 2083 C CB . VAL C 3 3 ? 13.518 72.811 32.646 1.00 64.18 ? 3 VAL B CB 1 ATOM 2084 C CG1 . VAL C 3 3 ? 12.599 71.590 32.524 1.00 64.20 ? 3 VAL B CG1 1 ATOM 2085 C CG2 . VAL C 3 3 ? 12.696 74.089 32.783 1.00 64.40 ? 3 VAL B CG2 1 ATOM 2086 N N . CYS C 3 4 ? 15.186 70.323 33.826 1.00 59.65 ? 4 CYS B N 1 ATOM 2087 C CA . CYS C 3 4 ? 16.141 69.254 33.574 1.00 58.24 ? 4 CYS B CA 1 ATOM 2088 C C . CYS C 3 4 ? 16.538 69.157 32.107 1.00 57.62 ? 4 CYS B C 1 ATOM 2089 O O . CYS C 3 4 ? 15.688 69.184 31.209 1.00 59.22 ? 4 CYS B O 1 ATOM 2090 C CB . CYS C 3 4 ? 15.575 67.916 34.035 1.00 56.63 ? 4 CYS B CB 1 ATOM 2091 S SG . CYS C 3 4 ? 15.310 67.770 35.835 1.00 56.92 ? 4 CYS B SG 1 ATOM 2092 N N . MET C 3 5 ? 17.842 69.045 31.883 1.00 56.87 ? 5 MET B N 1 ATOM 2093 C CA . MET C 3 5 ? 18.404 68.933 30.544 1.00 56.11 ? 5 MET B CA 1 ATOM 2094 C C . MET C 3 5 ? 18.823 67.479 30.317 1.00 54.22 ? 5 MET B C 1 ATOM 2095 O O . MET C 3 5 ? 19.858 67.044 30.818 1.00 54.42 ? 5 MET B O 1 ATOM 2096 C CB . MET C 3 5 ? 19.627 69.850 30.427 1.00 59.89 ? 5 MET B CB 1 ATOM 2097 C CG . MET C 3 5 ? 20.742 69.481 31.408 1.00 64.96 ? 5 MET B CG 1 ATOM 2098 S SD . MET C 3 5 ? 22.113 70.651 31.542 1.00 70.80 ? 5 MET B SD 1 ATOM 2099 C CE . MET C 3 5 ? 22.021 71.119 33.350 1.00 67.42 ? 5 MET B CE 1 ATOM 2100 N N . ASP C 3 6 ? 18.026 66.711 29.584 1.00 52.43 ? 6 ASP B N 1 ATOM 2101 C CA . ASP C 3 6 ? 18.420 65.329 29.345 1.00 51.53 ? 6 ASP B CA 1 ATOM 2102 C C . ASP C 3 6 ? 19.547 65.299 28.302 1.00 50.79 ? 6 ASP B C 1 ATOM 2103 O O . ASP C 3 6 ? 19.485 65.979 27.272 1.00 51.23 ? 6 ASP B O 1 ATOM 2104 C CB . ASP C 3 6 ? 17.222 64.474 28.887 1.00 51.40 ? 6 ASP B CB 1 ATOM 2105 C CG . ASP C 3 6 ? 16.827 64.724 27.446 1.00 50.98 ? 6 ASP B CG 1 ATOM 2106 O OD1 . ASP C 3 6 ? 17.655 64.482 26.548 1.00 51.90 ? 6 ASP B OD1 1 ATOM 2107 O OD2 . ASP C 3 6 ? 15.680 65.152 27.203 1.00 50.09 ? 6 ASP B OD2 1 ATOM 2108 N N . PRO C 3 7 ? 20.610 64.533 28.576 1.00 49.26 ? 7 PRO B N 1 ATOM 2109 C CA . PRO C 3 7 ? 21.731 64.449 27.636 1.00 48.21 ? 7 PRO B CA 1 ATOM 2110 C C . PRO C 3 7 ? 21.517 63.374 26.567 1.00 47.69 ? 7 PRO B C 1 ATOM 2111 O O . PRO C 3 7 ? 20.447 62.765 26.486 1.00 48.05 ? 7 PRO B O 1 ATOM 2112 C CB . PRO C 3 7 ? 22.905 64.130 28.549 1.00 49.11 ? 7 PRO B CB 1 ATOM 2113 C CG . PRO C 3 7 ? 22.262 63.199 29.560 1.00 49.01 ? 7 PRO B CG 1 ATOM 2114 C CD . PRO C 3 7 ? 20.933 63.872 29.856 1.00 47.77 ? 7 PRO B CD 1 ATOM 2115 N N . GLU C 3 8 ? 22.542 63.147 25.751 1.00 45.33 ? 8 GLU B N 1 ATOM 2116 C CA . GLU C 3 8 ? 22.484 62.138 24.700 1.00 42.89 ? 8 GLU B CA 1 ATOM 2117 C C . GLU C 3 8 ? 23.662 61.184 24.898 1.00 41.46 ? 8 GLU B C 1 ATOM 2118 O O . GLU C 3 8 ? 24.714 61.342 24.273 1.00 41.47 ? 8 GLU B O 1 ATOM 2119 C CB . GLU C 3 8 ? 22.579 62.792 23.319 1.00 43.44 ? 8 GLU B CB 1 ATOM 2120 C CG . GLU C 3 8 ? 21.592 63.919 23.073 1.00 42.17 ? 8 GLU B CG 1 ATOM 2121 C CD . GLU C 3 8 ? 21.685 64.451 21.653 1.00 43.89 ? 8 GLU B CD 1 ATOM 2122 O OE1 . GLU C 3 8 ? 22.811 64.488 21.107 1.00 43.64 ? 8 GLU B OE1 1 ATOM 2123 O OE2 . GLU C 3 8 ? 20.641 64.840 21.085 1.00 42.70 ? 8 GLU B OE2 1 ATOM 2124 N N . PRO C 3 9 ? 23.494 60.179 25.776 1.00 39.83 ? 9 PRO B N 1 ATOM 2125 C CA . PRO C 3 9 ? 24.521 59.179 26.092 1.00 38.43 ? 9 PRO B CA 1 ATOM 2126 C C . PRO C 3 9 ? 24.801 58.119 25.023 1.00 37.99 ? 9 PRO B C 1 ATOM 2127 O O . PRO C 3 9 ? 23.893 57.662 24.325 1.00 38.37 ? 9 PRO B O 1 ATOM 2128 C CB . PRO C 3 9 ? 23.995 58.557 27.380 1.00 37.76 ? 9 PRO B CB 1 ATOM 2129 C CG . PRO C 3 9 ? 22.519 58.560 27.154 1.00 37.72 ? 9 PRO B CG 1 ATOM 2130 C CD . PRO C 3 9 ? 22.279 59.945 26.581 1.00 38.85 ? 9 PRO B CD 1 ATOM 2131 N N . ILE C 3 10 ? 26.072 57.743 24.908 1.00 36.61 ? 10 ILE B N 1 ATOM 2132 C CA . ILE C 3 10 ? 26.508 56.708 23.975 1.00 34.84 ? 10 ILE B CA 1 ATOM 2133 C C . ILE C 3 10 ? 26.659 55.478 24.854 1.00 34.60 ? 10 ILE B C 1 ATOM 2134 O O . ILE C 3 10 ? 27.495 55.451 25.753 1.00 34.95 ? 10 ILE B O 1 ATOM 2135 C CB . ILE C 3 10 ? 27.874 57.040 23.364 1.00 34.00 ? 10 ILE B CB 1 ATOM 2136 C CG1 . ILE C 3 10 ? 27.762 58.286 22.498 1.00 31.78 ? 10 ILE B CG1 1 ATOM 2137 C CG2 . ILE C 3 10 ? 28.383 55.866 22.546 1.00 34.28 ? 10 ILE B CG2 1 ATOM 2138 C CD1 . ILE C 3 10 ? 29.090 58.756 22.028 1.00 32.64 ? 10 ILE B CD1 1 ATOM 2139 N N . VAL C 3 11 ? 25.859 54.455 24.593 1.00 34.38 ? 11 VAL B N 1 ATOM 2140 C CA . VAL C 3 11 ? 25.898 53.260 25.416 1.00 34.10 ? 11 VAL B CA 1 ATOM 2141 C C . VAL C 3 11 ? 25.613 51.993 24.595 1.00 34.16 ? 11 VAL B C 1 ATOM 2142 O O . VAL C 3 11 ? 25.190 52.070 23.442 1.00 34.95 ? 11 VAL B O 1 ATOM 2143 C CB . VAL C 3 11 ? 24.864 53.420 26.567 1.00 33.20 ? 11 VAL B CB 1 ATOM 2144 C CG1 . VAL C 3 11 ? 23.450 53.428 26.012 1.00 32.06 ? 11 VAL B CG1 1 ATOM 2145 C CG2 . VAL C 3 11 ? 25.038 52.343 27.581 1.00 35.42 ? 11 VAL B CG2 1 ATOM 2146 N N . ARG C 3 12 ? 25.883 50.826 25.164 1.00 33.71 ? 12 ARG B N 1 ATOM 2147 C CA . ARG C 3 12 ? 25.592 49.591 24.456 1.00 33.78 ? 12 ARG B CA 1 ATOM 2148 C C . ARG C 3 12 ? 24.175 49.242 24.868 1.00 33.14 ? 12 ARG B C 1 ATOM 2149 O O . ARG C 3 12 ? 23.658 49.789 25.842 1.00 33.61 ? 12 ARG B O 1 ATOM 2150 C CB . ARG C 3 12 ? 26.522 48.454 24.897 1.00 34.57 ? 12 ARG B CB 1 ATOM 2151 C CG . ARG C 3 12 ? 27.991 48.676 24.620 1.00 37.42 ? 12 ARG B CG 1 ATOM 2152 C CD . ARG C 3 12 ? 28.819 47.479 25.076 1.00 38.43 ? 12 ARG B CD 1 ATOM 2153 N NE . ARG C 3 12 ? 30.256 47.748 25.008 1.00 38.81 ? 12 ARG B NE 1 ATOM 2154 C CZ . ARG C 3 12 ? 30.937 47.892 23.877 1.00 38.83 ? 12 ARG B CZ 1 ATOM 2155 N NH1 . ARG C 3 12 ? 30.314 47.789 22.714 1.00 39.96 ? 12 ARG B NH1 1 ATOM 2156 N NH2 . ARG C 3 12 ? 32.239 48.140 23.905 1.00 38.62 ? 12 ARG B NH2 1 ATOM 2157 N N . ILE C 3 13 ? 23.539 48.342 24.133 1.00 31.93 ? 13 ILE B N 1 ATOM 2158 C CA . ILE C 3 13 ? 22.199 47.926 24.497 1.00 29.60 ? 13 ILE B CA 1 ATOM 2159 C C . ILE C 3 13 ? 22.226 46.419 24.685 1.00 30.10 ? 13 ILE B C 1 ATOM 2160 O O . ILE C 3 13 ? 22.197 45.677 23.712 1.00 31.80 ? 13 ILE B O 1 ATOM 2161 C CB . ILE C 3 13 ? 21.173 48.301 23.416 1.00 27.68 ? 13 ILE B CB 1 ATOM 2162 C CG1 . ILE C 3 13 ? 21.151 49.825 23.251 1.00 26.84 ? 13 ILE B CG1 1 ATOM 2163 C CG2 . ILE C 3 13 ? 19.803 47.756 23.785 1.00 26.51 ? 13 ILE B CG2 1 ATOM 2164 C CD1 . ILE C 3 13 ? 19.908 50.368 22.597 1.00 24.91 ? 13 ILE B CD1 1 ATOM 2165 N N . VAL C 3 14 ? 22.317 45.978 25.941 1.00 29.50 ? 14 VAL B N 1 ATOM 2166 C CA . VAL C 3 14 ? 22.352 44.549 26.281 1.00 27.70 ? 14 VAL B CA 1 ATOM 2167 C C . VAL C 3 14 ? 20.931 44.013 26.403 1.00 27.96 ? 14 VAL B C 1 ATOM 2168 O O . VAL C 3 14 ? 20.072 44.660 26.996 1.00 29.73 ? 14 VAL B O 1 ATOM 2169 C CB . VAL C 3 14 ? 23.074 44.296 27.620 1.00 24.44 ? 14 VAL B CB 1 ATOM 2170 C CG1 . VAL C 3 14 ? 23.182 42.816 27.877 1.00 22.45 ? 14 VAL B CG1 1 ATOM 2171 C CG2 . VAL C 3 14 ? 24.442 44.910 27.593 1.00 23.91 ? 14 VAL B CG2 1 ATOM 2172 N N . GLY C 3 15 ? 20.687 42.831 25.848 1.00 26.80 ? 15 GLY B N 1 ATOM 2173 C CA . GLY C 3 15 ? 19.354 42.256 25.903 1.00 27.18 ? 15 GLY B CA 1 ATOM 2174 C C . GLY C 3 15 ? 19.337 40.776 26.205 1.00 26.73 ? 15 GLY B C 1 ATOM 2175 O O . GLY C 3 15 ? 20.151 40.303 26.989 1.00 27.44 ? 15 GLY B O 1 ATOM 2176 N N . ARG C 3 16 ? 18.415 40.049 25.576 1.00 26.49 ? 16 ARG B N 1 ATOM 2177 C CA . ARG C 3 16 ? 18.280 38.605 25.789 1.00 26.37 ? 16 ARG B CA 1 ATOM 2178 C C . ARG C 3 16 ? 19.595 37.846 25.965 1.00 26.30 ? 16 ARG B C 1 ATOM 2179 O O . ARG C 3 16 ? 20.511 37.988 25.162 1.00 26.97 ? 16 ARG B O 1 ATOM 2180 C CB . ARG C 3 16 ? 17.496 37.980 24.641 1.00 25.49 ? 16 ARG B CB 1 ATOM 2181 C CG . ARG C 3 16 ? 17.289 36.506 24.827 1.00 25.30 ? 16 ARG B CG 1 ATOM 2182 C CD . ARG C 3 16 ? 16.214 35.967 23.913 1.00 27.50 ? 16 ARG B CD 1 ATOM 2183 N NE . ARG C 3 16 ? 15.934 34.574 24.239 1.00 30.33 ? 16 ARG B NE 1 ATOM 2184 C CZ . ARG C 3 16 ? 15.049 33.814 23.609 1.00 32.46 ? 16 ARG B CZ 1 ATOM 2185 N NH1 . ARG C 3 16 ? 14.339 34.304 22.603 1.00 34.60 ? 16 ARG B NH1 1 ATOM 2186 N NH2 . ARG C 3 16 ? 14.879 32.556 23.984 1.00 35.43 ? 16 ARG B NH2 1 ATOM 2187 N N . ASN C 3 17 ? 19.666 37.029 27.013 1.00 26.30 ? 17 ASN B N 1 ATOM 2188 C CA . ASN C 3 17 ? 20.850 36.225 27.347 1.00 27.66 ? 17 ASN B CA 1 ATOM 2189 C C . ASN C 3 17 ? 22.140 37.023 27.538 1.00 27.46 ? 17 ASN B C 1 ATOM 2190 O O . ASN C 3 17 ? 23.231 36.460 27.471 1.00 28.50 ? 17 ASN B O 1 ATOM 2191 C CB . ASN C 3 17 ? 21.119 35.136 26.289 1.00 28.76 ? 17 ASN B CB 1 ATOM 2192 C CG . ASN C 3 17 ? 20.102 34.006 26.322 1.00 29.50 ? 17 ASN B CG 1 ATOM 2193 O OD1 . ASN C 3 17 ? 19.567 33.661 27.372 1.00 30.56 ? 17 ASN B OD1 1 ATOM 2194 N ND2 . ASN C 3 17 ? 19.852 33.406 25.164 1.00 30.45 ? 17 ASN B ND2 1 ATOM 2195 N N . GLY C 3 18 ? 22.031 38.325 27.769 1.00 26.61 ? 18 GLY B N 1 ATOM 2196 C CA . GLY C 3 18 ? 23.227 39.122 27.961 1.00 26.11 ? 18 GLY B CA 1 ATOM 2197 C C . GLY C 3 18 ? 23.951 39.503 26.683 1.00 27.01 ? 18 GLY B C 1 ATOM 2198 O O . GLY C 3 18 ? 25.082 39.982 26.751 1.00 27.18 ? 18 GLY B O 1 ATOM 2199 N N . LEU C 3 19 ? 23.311 39.291 25.530 1.00 27.48 ? 19 LEU B N 1 ATOM 2200 C CA . LEU C 3 19 ? 23.891 39.637 24.225 1.00 28.58 ? 19 LEU B CA 1 ATOM 2201 C C . LEU C 3 19 ? 23.677 41.115 23.915 1.00 29.99 ? 19 LEU B C 1 ATOM 2202 O O . LEU C 3 19 ? 22.802 41.746 24.491 1.00 32.52 ? 19 LEU B O 1 ATOM 2203 C CB . LEU C 3 19 ? 23.249 38.812 23.115 1.00 28.34 ? 19 LEU B CB 1 ATOM 2204 C CG . LEU C 3 19 ? 23.562 37.321 23.028 1.00 29.10 ? 19 LEU B CG 1 ATOM 2205 C CD1 . LEU C 3 19 ? 22.686 36.699 21.941 1.00 29.18 ? 19 LEU B CD1 1 ATOM 2206 C CD2 . LEU C 3 19 ? 25.029 37.123 22.717 1.00 27.15 ? 19 LEU B CD2 1 ATOM 2207 N N . CYS C 3 20 ? 24.457 41.661 22.988 1.00 30.05 ? 20 CYS B N 1 ATOM 2208 C CA . CYS C 3 20 ? 24.349 43.075 22.632 1.00 31.63 ? 20 CYS B CA 1 ATOM 2209 C C . CYS C 3 20 ? 23.656 43.380 21.309 1.00 31.63 ? 20 CYS B C 1 ATOM 2210 O O . CYS C 3 20 ? 23.631 42.545 20.412 1.00 31.77 ? 20 CYS B O 1 ATOM 2211 C CB . CYS C 3 20 ? 25.744 43.703 22.633 1.00 33.08 ? 20 CYS B CB 1 ATOM 2212 S SG . CYS C 3 20 ? 26.292 44.151 24.308 1.00 38.63 ? 20 CYS B SG 1 ATOM 2213 N N . VAL C 3 21 ? 23.078 44.578 21.203 1.00 31.86 ? 21 VAL B N 1 ATOM 2214 C CA . VAL C 3 21 ? 22.419 44.997 19.969 1.00 32.01 ? 21 VAL B CA 1 ATOM 2215 C C . VAL C 3 21 ? 23.572 45.388 19.063 1.00 33.89 ? 21 VAL B C 1 ATOM 2216 O O . VAL C 3 21 ? 24.254 46.391 19.287 1.00 35.46 ? 21 VAL B O 1 ATOM 2217 C CB . VAL C 3 21 ? 21.484 46.193 20.177 1.00 30.49 ? 21 VAL B CB 1 ATOM 2218 C CG1 . VAL C 3 21 ? 20.890 46.617 18.842 1.00 30.78 ? 21 VAL B CG1 1 ATOM 2219 C CG2 . VAL C 3 21 ? 20.370 45.813 21.130 1.00 28.98 ? 21 VAL B CG2 1 ATOM 2220 N N . ASP C 3 22 ? 23.756 44.570 18.035 1.00 34.39 ? 22 ASP B N 1 ATOM 2221 C CA . ASP C 3 22 ? 24.849 44.647 17.073 1.00 35.25 ? 22 ASP B CA 1 ATOM 2222 C C . ASP C 3 22 ? 24.389 44.940 15.621 1.00 36.19 ? 22 ASP B C 1 ATOM 2223 O O . ASP C 3 22 ? 23.351 44.443 15.181 1.00 36.80 ? 22 ASP B O 1 ATOM 2224 C CB . ASP C 3 22 ? 25.542 43.277 17.185 1.00 36.32 ? 22 ASP B CB 1 ATOM 2225 C CG . ASP C 3 22 ? 26.801 43.163 16.387 1.00 37.66 ? 22 ASP B CG 1 ATOM 2226 O OD1 . ASP C 3 22 ? 26.741 43.239 15.145 1.00 40.12 ? 22 ASP B OD1 1 ATOM 2227 O OD2 . ASP C 3 22 ? 27.860 42.965 17.013 1.00 40.30 ? 22 ASP B OD2 1 ATOM 2228 N N . VAL C 3 23 ? 25.140 45.756 14.881 1.00 36.20 ? 23 VAL B N 1 ATOM 2229 C CA . VAL C 3 23 ? 24.794 46.031 13.479 1.00 36.13 ? 23 VAL B CA 1 ATOM 2230 C C . VAL C 3 23 ? 25.613 45.026 12.670 1.00 35.40 ? 23 VAL B C 1 ATOM 2231 O O . VAL C 3 23 ? 26.836 45.146 12.586 1.00 35.14 ? 23 VAL B O 1 ATOM 2232 C CB . VAL C 3 23 ? 25.196 47.453 13.044 1.00 36.54 ? 23 VAL B CB 1 ATOM 2233 C CG1 . VAL C 3 23 ? 24.629 47.757 11.654 1.00 36.94 ? 23 VAL B CG1 1 ATOM 2234 C CG2 . VAL C 3 23 ? 24.700 48.460 14.051 1.00 36.51 ? 23 VAL B CG2 1 ATOM 2235 N N . ARG C 3 24 ? 24.931 44.046 12.081 1.00 35.56 ? 24 ARG B N 1 ATOM 2236 C CA . ARG C 3 24 ? 25.567 42.965 11.322 1.00 36.17 ? 24 ARG B CA 1 ATOM 2237 C C . ARG C 3 24 ? 26.759 43.293 10.427 1.00 37.24 ? 24 ARG B C 1 ATOM 2238 O O . ARG C 3 24 ? 26.706 44.204 9.597 1.00 38.28 ? 24 ARG B O 1 ATOM 2239 C CB . ARG C 3 24 ? 24.517 42.217 10.500 1.00 34.94 ? 24 ARG B CB 1 ATOM 2240 C CG . ARG C 3 24 ? 25.052 40.968 9.804 1.00 33.49 ? 24 ARG B CG 1 ATOM 2241 C CD . ARG C 3 24 ? 23.918 40.125 9.256 1.00 31.12 ? 24 ARG B CD 1 ATOM 2242 N NE . ARG C 3 24 ? 23.205 39.424 10.320 1.00 29.23 ? 24 ARG B NE 1 ATOM 2243 C CZ . ARG C 3 24 ? 21.909 39.125 10.286 1.00 27.85 ? 24 ARG B CZ 1 ATOM 2244 N NH1 . ARG C 3 24 ? 21.171 39.469 9.239 1.00 27.82 ? 24 ARG B NH1 1 ATOM 2245 N NH2 . ARG C 3 24 ? 21.349 38.485 11.301 1.00 25.88 ? 24 ARG B NH2 1 ATOM 2246 N N . ASP C 3 25 ? 27.824 42.510 10.616 1.00 37.61 ? 25 ASP B N 1 ATOM 2247 C CA . ASP C 3 25 ? 29.086 42.613 9.883 1.00 38.18 ? 25 ASP B CA 1 ATOM 2248 C C . ASP C 3 25 ? 29.710 44.006 9.785 1.00 38.98 ? 25 ASP B C 1 ATOM 2249 O O . ASP C 3 25 ? 30.476 44.282 8.869 1.00 40.27 ? 25 ASP B O 1 ATOM 2250 C CB . ASP C 3 25 ? 28.929 42.021 8.479 1.00 38.54 ? 25 ASP B CB 1 ATOM 2251 C CG . ASP C 3 25 ? 28.547 40.553 8.509 1.00 39.98 ? 25 ASP B CG 1 ATOM 2252 O OD1 . ASP C 3 25 ? 29.173 39.799 9.287 1.00 39.01 ? 25 ASP B OD1 1 ATOM 2253 O OD2 . ASP C 3 25 ? 27.632 40.154 7.750 1.00 40.38 ? 25 ASP B OD2 1 ATOM 2254 N N . GLY C 3 26 ? 29.391 44.880 10.732 1.00 38.87 ? 26 GLY B N 1 ATOM 2255 C CA . GLY C 3 26 ? 29.956 46.216 10.718 1.00 38.99 ? 26 GLY B CA 1 ATOM 2256 C C . GLY C 3 26 ? 29.624 47.109 9.532 1.00 40.14 ? 26 GLY B C 1 ATOM 2257 O O . GLY C 3 26 ? 30.221 48.174 9.384 1.00 40.07 ? 26 GLY B O 1 ATOM 2258 N N . ARG C 3 27 ? 28.673 46.705 8.695 1.00 41.77 ? 27 ARG B N 1 ATOM 2259 C CA . ARG C 3 27 ? 28.306 47.511 7.527 1.00 43.16 ? 27 ARG B CA 1 ATOM 2260 C C . ARG C 3 27 ? 27.085 48.396 7.772 1.00 42.51 ? 27 ARG B C 1 ATOM 2261 O O . ARG C 3 27 ? 26.162 48.013 8.502 1.00 43.79 ? 27 ARG B O 1 ATOM 2262 C CB . ARG C 3 27 ? 28.031 46.610 6.335 1.00 45.53 ? 27 ARG B CB 1 ATOM 2263 C CG . ARG C 3 27 ? 28.964 45.442 6.235 1.00 48.93 ? 27 ARG B CG 1 ATOM 2264 C CD . ARG C 3 27 ? 28.957 44.939 4.822 1.00 51.49 ? 27 ARG B CD 1 ATOM 2265 N NE . ARG C 3 27 ? 29.895 45.680 3.993 1.00 51.56 ? 27 ARG B NE 1 ATOM 2266 C CZ . ARG C 3 27 ? 31.207 45.483 4.017 1.00 51.31 ? 27 ARG B CZ 1 ATOM 2267 N NH1 . ARG C 3 27 ? 31.728 44.568 4.827 1.00 49.35 ? 27 ARG B NH1 1 ATOM 2268 N NH2 . ARG C 3 27 ? 31.999 46.199 3.231 1.00 52.53 ? 27 ARG B NH2 1 ATOM 2269 N N . PHE C 3 28 ? 27.058 49.560 7.124 1.00 40.48 ? 28 PHE B N 1 ATOM 2270 C CA . PHE C 3 28 ? 25.959 50.491 7.331 1.00 39.96 ? 28 PHE B CA 1 ATOM 2271 C C . PHE C 3 28 ? 25.094 50.872 6.140 1.00 39.40 ? 28 PHE B C 1 ATOM 2272 O O . PHE C 3 28 ? 24.523 51.964 6.105 1.00 40.12 ? 28 PHE B O 1 ATOM 2273 C CB . PHE C 3 28 ? 26.504 51.747 8.012 1.00 38.72 ? 28 PHE B CB 1 ATOM 2274 C CG . PHE C 3 28 ? 27.006 51.492 9.403 1.00 38.14 ? 28 PHE B CG 1 ATOM 2275 C CD1 . PHE C 3 28 ? 26.135 51.535 10.486 1.00 37.06 ? 28 PHE B CD1 1 ATOM 2276 C CD2 . PHE C 3 28 ? 28.332 51.127 9.622 1.00 37.08 ? 28 PHE B CD2 1 ATOM 2277 C CE1 . PHE C 3 28 ? 26.580 51.222 11.763 1.00 36.70 ? 28 PHE B CE1 1 ATOM 2278 C CE2 . PHE C 3 28 ? 28.780 50.813 10.894 1.00 35.42 ? 28 PHE B CE2 1 ATOM 2279 C CZ . PHE C 3 28 ? 27.901 50.857 11.964 1.00 35.63 ? 28 PHE B CZ 1 ATOM 2280 N N . HIS C 3 29 ? 24.978 49.977 5.169 1.00 39.09 ? 29 HIS B N 1 ATOM 2281 C CA . HIS C 3 29 ? 24.136 50.268 4.020 1.00 38.86 ? 29 HIS B CA 1 ATOM 2282 C C . HIS C 3 29 ? 22.675 50.188 4.477 1.00 38.84 ? 29 HIS B C 1 ATOM 2283 O O . HIS C 3 29 ? 22.314 49.347 5.305 1.00 39.30 ? 29 HIS B O 1 ATOM 2284 C CB . HIS C 3 29 ? 24.431 49.288 2.866 1.00 38.93 ? 29 HIS B CB 1 ATOM 2285 C CG . HIS C 3 29 ? 24.427 47.847 3.267 1.00 39.00 ? 29 HIS B CG 1 ATOM 2286 N ND1 . HIS C 3 29 ? 23.274 47.094 3.332 1.00 40.15 ? 29 HIS B ND1 1 ATOM 2287 C CD2 . HIS C 3 29 ? 25.435 47.029 3.651 1.00 39.23 ? 29 HIS B CD2 1 ATOM 2288 C CE1 . HIS C 3 29 ? 23.571 45.872 3.740 1.00 40.95 ? 29 HIS B CE1 1 ATOM 2289 N NE2 . HIS C 3 29 ? 24.875 45.807 3.941 1.00 40.90 ? 29 HIS B NE2 1 ATOM 2290 N N . ASN C 3 30 ? 21.845 51.085 3.962 1.00 38.02 ? 30 ASN B N 1 ATOM 2291 C CA . ASN C 3 30 ? 20.437 51.117 4.337 1.00 38.68 ? 30 ASN B CA 1 ATOM 2292 C C . ASN C 3 30 ? 19.729 49.775 4.180 1.00 37.79 ? 30 ASN B C 1 ATOM 2293 O O . ASN C 3 30 ? 19.485 49.315 3.067 1.00 38.20 ? 30 ASN B O 1 ATOM 2294 C CB . ASN C 3 30 ? 19.709 52.182 3.520 1.00 40.43 ? 30 ASN B CB 1 ATOM 2295 C CG . ASN C 3 30 ? 20.163 53.589 3.858 1.00 43.21 ? 30 ASN B CG 1 ATOM 2296 O OD1 . ASN C 3 30 ? 21.101 53.788 4.644 1.00 43.50 ? 30 ASN B OD1 1 ATOM 2297 N ND2 . ASN C 3 30 ? 19.501 54.580 3.261 1.00 43.83 ? 30 ASN B ND2 1 ATOM 2298 N N . GLY C 3 31 ? 19.399 49.148 5.303 1.00 37.37 ? 31 GLY B N 1 ATOM 2299 C CA . GLY C 3 31 ? 18.712 47.876 5.247 1.00 37.28 ? 31 GLY B CA 1 ATOM 2300 C C . GLY C 3 31 ? 19.432 46.758 5.968 1.00 37.60 ? 31 GLY B C 1 ATOM 2301 O O . GLY C 3 31 ? 18.788 45.792 6.385 1.00 39.43 ? 31 GLY B O 1 ATOM 2302 N N . ASN C 3 32 ? 20.754 46.868 6.111 1.00 36.26 ? 32 ASN B N 1 ATOM 2303 C CA . ASN C 3 32 ? 21.524 45.829 6.800 1.00 35.51 ? 32 ASN B CA 1 ATOM 2304 C C . ASN C 3 32 ? 20.826 45.580 8.138 1.00 35.12 ? 32 ASN B C 1 ATOM 2305 O O . ASN C 3 32 ? 20.443 46.523 8.830 1.00 36.11 ? 32 ASN B O 1 ATOM 2306 C CB . ASN C 3 32 ? 22.975 46.283 7.011 1.00 34.06 ? 32 ASN B CB 1 ATOM 2307 C CG . ASN C 3 32 ? 23.867 45.171 7.540 1.00 32.86 ? 32 ASN B CG 1 ATOM 2308 O OD1 . ASN C 3 32 ? 23.853 44.050 7.030 1.00 32.12 ? 32 ASN B OD1 1 ATOM 2309 N ND2 . ASN C 3 32 ? 24.659 45.483 8.558 1.00 31.74 ? 32 ASN B ND2 1 ATOM 2310 N N . ALA C 3 33 ? 20.654 44.311 8.492 1.00 34.75 ? 33 ALA B N 1 ATOM 2311 C CA . ALA C 3 33 ? 19.952 43.945 9.719 1.00 33.34 ? 33 ALA B CA 1 ATOM 2312 C C . ALA C 3 33 ? 20.650 44.285 11.025 1.00 32.23 ? 33 ALA B C 1 ATOM 2313 O O . ALA C 3 33 ? 21.844 44.566 11.057 1.00 31.46 ? 33 ALA B O 1 ATOM 2314 C CB . ALA C 3 33 ? 19.614 42.448 9.699 1.00 33.53 ? 33 ALA B CB 1 ATOM 2315 N N . ILE C 3 34 ? 19.862 44.269 12.095 1.00 31.17 ? 34 ILE B N 1 ATOM 2316 C CA . ILE C 3 34 ? 20.328 44.513 13.453 1.00 31.69 ? 34 ILE B CA 1 ATOM 2317 C C . ILE C 3 34 ? 20.217 43.119 14.086 1.00 31.89 ? 34 ILE B C 1 ATOM 2318 O O . ILE C 3 34 ? 19.234 42.415 13.865 1.00 32.36 ? 34 ILE B O 1 ATOM 2319 C CB . ILE C 3 34 ? 19.406 45.520 14.178 1.00 32.30 ? 34 ILE B CB 1 ATOM 2320 C CG1 . ILE C 3 34 ? 19.434 46.872 13.455 1.00 33.12 ? 34 ILE B CG1 1 ATOM 2321 C CG2 . ILE C 3 34 ? 19.851 45.703 15.620 1.00 31.71 ? 34 ILE B CG2 1 ATOM 2322 C CD1 . ILE C 3 34 ? 20.756 47.614 13.564 1.00 33.27 ? 34 ILE B CD1 1 ATOM 2323 N N . GLN C 3 35 ? 21.216 42.707 14.857 1.00 31.36 ? 35 GLN B N 1 ATOM 2324 C CA . GLN C 3 35 ? 21.191 41.369 15.436 1.00 31.77 ? 35 GLN B CA 1 ATOM 2325 C C . GLN C 3 35 ? 21.727 41.274 16.856 1.00 32.95 ? 35 GLN B C 1 ATOM 2326 O O . GLN C 3 35 ? 22.320 42.217 17.373 1.00 33.31 ? 35 GLN B O 1 ATOM 2327 C CB . GLN C 3 35 ? 22.015 40.438 14.550 1.00 30.59 ? 35 GLN B CB 1 ATOM 2328 C CG . GLN C 3 35 ? 23.304 41.086 14.053 1.00 30.28 ? 35 GLN B CG 1 ATOM 2329 C CD . GLN C 3 35 ? 24.352 40.087 13.589 1.00 31.47 ? 35 GLN B CD 1 ATOM 2330 O OE1 . GLN C 3 35 ? 24.048 39.108 12.916 1.00 31.76 ? 35 GLN B OE1 1 ATOM 2331 N NE2 . GLN C 3 35 ? 25.602 40.349 13.937 1.00 31.34 ? 35 GLN B NE2 1 ATOM 2332 N N . LEU C 3 36 ? 21.500 40.124 17.488 1.00 33.83 ? 36 LEU B N 1 ATOM 2333 C CA . LEU C 3 36 ? 22.017 39.875 18.828 1.00 33.80 ? 36 LEU B CA 1 ATOM 2334 C C . LEU C 3 36 ? 23.430 39.373 18.590 1.00 34.23 ? 36 LEU B C 1 ATOM 2335 O O . LEU C 3 36 ? 23.669 38.584 17.681 1.00 34.00 ? 36 LEU B O 1 ATOM 2336 C CB . LEU C 3 36 ? 21.218 38.791 19.552 1.00 33.92 ? 36 LEU B CB 1 ATOM 2337 C CG . LEU C 3 36 ? 19.995 39.189 20.372 1.00 33.55 ? 36 LEU B CG 1 ATOM 2338 C CD1 . LEU C 3 36 ? 19.475 37.956 21.078 1.00 33.57 ? 36 LEU B CD1 1 ATOM 2339 C CD2 . LEU C 3 36 ? 20.365 40.255 21.385 1.00 33.70 ? 36 LEU B CD2 1 ATOM 2340 N N . TRP C 3 37 ? 24.375 39.822 19.398 1.00 35.12 ? 37 TRP B N 1 ATOM 2341 C CA . TRP C 3 37 ? 25.741 39.395 19.197 1.00 35.97 ? 37 TRP B CA 1 ATOM 2342 C C . TRP C 3 37 ? 26.562 39.593 20.452 1.00 35.96 ? 37 TRP B C 1 ATOM 2343 O O . TRP C 3 37 ? 26.407 40.593 21.141 1.00 36.53 ? 37 TRP B O 1 ATOM 2344 C CB . TRP C 3 37 ? 26.351 40.202 18.050 1.00 36.62 ? 37 TRP B CB 1 ATOM 2345 C CG . TRP C 3 37 ? 27.599 39.613 17.525 1.00 38.30 ? 37 TRP B CG 1 ATOM 2346 C CD1 . TRP C 3 37 ? 28.875 40.035 17.759 1.00 37.85 ? 37 TRP B CD1 1 ATOM 2347 C CD2 . TRP C 3 37 ? 27.701 38.453 16.695 1.00 39.79 ? 37 TRP B CD2 1 ATOM 2348 N NE1 . TRP C 3 37 ? 29.772 39.208 17.122 1.00 39.32 ? 37 TRP B NE1 1 ATOM 2349 C CE2 . TRP C 3 37 ? 29.079 38.230 16.461 1.00 39.95 ? 37 TRP B CE2 1 ATOM 2350 C CE3 . TRP C 3 37 ? 26.759 37.582 16.119 1.00 40.57 ? 37 TRP B CE3 1 ATOM 2351 C CZ2 . TRP C 3 37 ? 29.541 37.162 15.679 1.00 40.49 ? 37 TRP B CZ2 1 ATOM 2352 C CZ3 . TRP C 3 37 ? 27.216 36.524 15.342 1.00 40.59 ? 37 TRP B CZ3 1 ATOM 2353 C CH2 . TRP C 3 37 ? 28.598 36.324 15.127 1.00 40.69 ? 37 TRP B CH2 1 ATOM 2354 N N . PRO C 3 38 ? 27.443 38.630 20.769 1.00 35.81 ? 38 PRO B N 1 ATOM 2355 C CA . PRO C 3 38 ? 28.295 38.724 21.955 1.00 35.62 ? 38 PRO B CA 1 ATOM 2356 C C . PRO C 3 38 ? 28.873 40.134 22.059 1.00 35.45 ? 38 PRO B C 1 ATOM 2357 O O . PRO C 3 38 ? 29.361 40.693 21.073 1.00 35.14 ? 38 PRO B O 1 ATOM 2358 C CB . PRO C 3 38 ? 29.356 37.667 21.683 1.00 35.22 ? 38 PRO B CB 1 ATOM 2359 C CG . PRO C 3 38 ? 28.549 36.591 21.019 1.00 36.43 ? 38 PRO B CG 1 ATOM 2360 C CD . PRO C 3 38 ? 27.687 37.368 20.047 1.00 36.21 ? 38 PRO B CD 1 ATOM 2361 N N . CYS C 3 39 ? 28.802 40.710 23.252 1.00 35.39 ? 39 CYS B N 1 ATOM 2362 C CA . CYS C 3 39 ? 29.286 42.063 23.467 1.00 36.13 ? 39 CYS B CA 1 ATOM 2363 C C . CYS C 3 39 ? 30.793 42.204 23.331 1.00 37.41 ? 39 CYS B C 1 ATOM 2364 O O . CYS C 3 39 ? 31.565 41.349 23.768 1.00 36.50 ? 39 CYS B O 1 ATOM 2365 C CB . CYS C 3 39 ? 28.832 42.563 24.832 1.00 35.04 ? 39 CYS B CB 1 ATOM 2366 S SG . CYS C 3 39 ? 27.042 42.440 25.107 1.00 34.90 ? 39 CYS B SG 1 ATOM 2367 N N . LYS C 3 40 ? 31.198 43.315 22.731 1.00 39.46 ? 40 LYS B N 1 ATOM 2368 C CA . LYS C 3 40 ? 32.600 43.581 22.495 1.00 42.56 ? 40 LYS B CA 1 ATOM 2369 C C . LYS C 3 40 ? 33.236 44.541 23.479 1.00 44.72 ? 40 LYS B C 1 ATOM 2370 O O . LYS C 3 40 ? 32.585 45.453 23.990 1.00 45.30 ? 40 LYS B O 1 ATOM 2371 C CB . LYS C 3 40 ? 32.778 44.108 21.074 1.00 41.91 ? 40 LYS B CB 1 ATOM 2372 C CG . LYS C 3 40 ? 32.297 43.125 20.033 1.00 43.41 ? 40 LYS B CG 1 ATOM 2373 C CD . LYS C 3 40 ? 32.735 43.502 18.636 1.00 43.47 ? 40 LYS B CD 1 ATOM 2374 C CE . LYS C 3 40 ? 32.020 44.728 18.125 1.00 43.24 ? 40 LYS B CE 1 ATOM 2375 N NZ . LYS C 3 40 ? 32.229 44.829 16.654 1.00 43.69 ? 40 LYS B NZ 1 ATOM 2376 N N . SER C 3 41 ? 34.520 44.315 23.740 1.00 47.20 ? 41 SER B N 1 ATOM 2377 C CA . SER C 3 41 ? 35.299 45.159 24.636 1.00 48.88 ? 41 SER B CA 1 ATOM 2378 C C . SER C 3 41 ? 36.182 46.015 23.735 1.00 50.11 ? 41 SER B C 1 ATOM 2379 O O . SER C 3 41 ? 37.348 45.683 23.512 1.00 51.79 ? 41 SER B O 1 ATOM 2380 C CB . SER C 3 41 ? 36.190 44.307 25.547 1.00 47.99 ? 41 SER B CB 1 ATOM 2381 O OG . SER C 3 41 ? 35.438 43.326 26.235 1.00 46.69 ? 41 SER B OG 1 ATOM 2382 N N . ASN C 3 42 ? 35.617 47.097 23.203 1.00 50.29 ? 42 ASN B N 1 ATOM 2383 C CA . ASN C 3 42 ? 36.348 48.001 22.317 1.00 50.30 ? 42 ASN B CA 1 ATOM 2384 C C . ASN C 3 42 ? 35.473 49.175 21.895 1.00 51.31 ? 42 ASN B C 1 ATOM 2385 O O . ASN C 3 42 ? 34.512 49.521 22.584 1.00 51.63 ? 42 ASN B O 1 ATOM 2386 C CB . ASN C 3 42 ? 36.835 47.256 21.075 1.00 49.05 ? 42 ASN B CB 1 ATOM 2387 C CG . ASN C 3 42 ? 35.739 46.455 20.422 1.00 48.58 ? 42 ASN B CG 1 ATOM 2388 O OD1 . ASN C 3 42 ? 34.753 47.009 19.937 1.00 49.08 ? 42 ASN B OD1 1 ATOM 2389 N ND2 . ASN C 3 42 ? 35.895 45.137 20.416 1.00 47.76 ? 42 ASN B ND2 1 ATOM 2390 N N . THR C 3 43 ? 35.791 49.772 20.751 1.00 52.46 ? 43 THR B N 1 ATOM 2391 C CA . THR C 3 43 ? 35.037 50.926 20.281 1.00 53.02 ? 43 THR B CA 1 ATOM 2392 C C . THR C 3 43 ? 34.303 50.742 18.954 1.00 52.38 ? 43 THR B C 1 ATOM 2393 O O . THR C 3 43 ? 33.871 51.727 18.349 1.00 53.12 ? 43 THR B O 1 ATOM 2394 C CB . THR C 3 43 ? 35.958 52.151 20.134 1.00 54.16 ? 43 THR B CB 1 ATOM 2395 O OG1 . THR C 3 43 ? 36.868 52.199 21.238 1.00 55.02 ? 43 THR B OG1 1 ATOM 2396 C CG2 . THR C 3 43 ? 35.133 53.440 20.113 1.00 55.55 ? 43 THR B CG2 1 ATOM 2397 N N . ASP C 3 44 ? 34.153 49.502 18.495 1.00 51.46 ? 44 ASP B N 1 ATOM 2398 C CA . ASP C 3 44 ? 33.467 49.272 17.226 1.00 50.52 ? 44 ASP B CA 1 ATOM 2399 C C . ASP C 3 44 ? 32.071 49.893 17.263 1.00 49.87 ? 44 ASP B C 1 ATOM 2400 O O . ASP C 3 44 ? 31.164 49.375 17.918 1.00 50.32 ? 44 ASP B O 1 ATOM 2401 C CB . ASP C 3 44 ? 33.391 47.773 16.923 1.00 50.05 ? 44 ASP B CB 1 ATOM 2402 C CG . ASP C 3 44 ? 34.769 47.135 16.820 1.00 49.74 ? 44 ASP B CG 1 ATOM 2403 O OD1 . ASP C 3 44 ? 35.705 47.829 16.361 1.00 48.67 ? 44 ASP B OD1 1 ATOM 2404 O OD2 . ASP C 3 44 ? 34.920 45.945 17.186 1.00 49.56 ? 44 ASP B OD2 1 ATOM 2405 N N . ALA C 3 45 ? 31.918 51.010 16.549 1.00 47.64 ? 45 ALA B N 1 ATOM 2406 C CA . ALA C 3 45 ? 30.665 51.759 16.497 1.00 45.50 ? 45 ALA B CA 1 ATOM 2407 C C . ALA C 3 45 ? 29.437 50.951 16.115 1.00 43.90 ? 45 ALA B C 1 ATOM 2408 O O . ALA C 3 45 ? 28.318 51.455 16.206 1.00 43.99 ? 45 ALA B O 1 ATOM 2409 C CB . ALA C 3 45 ? 30.807 52.946 15.550 1.00 44.19 ? 45 ALA B CB 1 ATOM 2410 N N . ASN C 3 46 ? 29.630 49.706 15.689 1.00 41.61 ? 46 ASN B N 1 ATOM 2411 C CA . ASN C 3 46 ? 28.495 48.881 15.298 1.00 39.04 ? 46 ASN B CA 1 ATOM 2412 C C . ASN C 3 46 ? 27.824 48.246 16.510 1.00 37.79 ? 46 ASN B C 1 ATOM 2413 O O . ASN C 3 46 ? 26.866 47.483 16.370 1.00 37.75 ? 46 ASN B O 1 ATOM 2414 C CB . ASN C 3 46 ? 28.933 47.799 14.300 1.00 38.31 ? 46 ASN B CB 1 ATOM 2415 C CG . ASN C 3 46 ? 29.424 46.538 14.975 1.00 37.41 ? 46 ASN B CG 1 ATOM 2416 O OD1 . ASN C 3 46 ? 30.254 46.589 15.876 1.00 38.99 ? 46 ASN B OD1 1 ATOM 2417 N ND2 . ASN C 3 46 ? 28.918 45.394 14.531 1.00 35.70 ? 46 ASN B ND2 1 ATOM 2418 N N . GLN C 3 47 ? 28.320 48.569 17.702 1.00 35.87 ? 47 GLN B N 1 ATOM 2419 C CA . GLN C 3 47 ? 27.741 48.017 18.917 1.00 35.20 ? 47 GLN B CA 1 ATOM 2420 C C . GLN C 3 47 ? 27.436 49.076 19.977 1.00 35.01 ? 47 GLN B C 1 ATOM 2421 O O . GLN C 3 47 ? 26.892 48.759 21.042 1.00 35.80 ? 47 GLN B O 1 ATOM 2422 C CB . GLN C 3 47 ? 28.654 46.932 19.484 1.00 33.05 ? 47 GLN B CB 1 ATOM 2423 C CG . GLN C 3 47 ? 27.908 45.644 19.771 1.00 32.85 ? 47 GLN B CG 1 ATOM 2424 C CD . GLN C 3 47 ? 28.823 44.510 20.143 1.00 32.45 ? 47 GLN B CD 1 ATOM 2425 O OE1 . GLN C 3 47 ? 29.584 44.602 21.105 1.00 35.12 ? 47 GLN B OE1 1 ATOM 2426 N NE2 . GLN C 3 47 ? 28.754 43.426 19.385 1.00 31.19 ? 47 GLN B NE2 1 ATOM 2427 N N . LEU C 3 48 ? 27.774 50.329 19.660 1.00 34.81 ? 48 LEU B N 1 ATOM 2428 C CA . LEU C 3 48 ? 27.543 51.481 20.540 1.00 34.34 ? 48 LEU B CA 1 ATOM 2429 C C . LEU C 3 48 ? 26.409 52.320 19.975 1.00 33.50 ? 48 LEU B C 1 ATOM 2430 O O . LEU C 3 48 ? 26.411 52.650 18.787 1.00 35.01 ? 48 LEU B O 1 ATOM 2431 C CB . LEU C 3 48 ? 28.789 52.362 20.624 1.00 33.04 ? 48 LEU B CB 1 ATOM 2432 C CG . LEU C 3 48 ? 30.018 51.785 21.308 1.00 32.43 ? 48 LEU B CG 1 ATOM 2433 C CD1 . LEU C 3 48 ? 31.161 52.736 21.111 1.00 34.72 ? 48 LEU B CD1 1 ATOM 2434 C CD2 . LEU C 3 48 ? 29.751 51.572 22.779 1.00 32.66 ? 48 LEU B CD2 1 ATOM 2435 N N . TRP C 3 49 ? 25.451 52.686 20.816 1.00 32.58 ? 49 TRP B N 1 ATOM 2436 C CA . TRP C 3 49 ? 24.334 53.480 20.330 1.00 32.41 ? 49 TRP B CA 1 ATOM 2437 C C . TRP C 3 49 ? 24.157 54.815 21.041 1.00 33.01 ? 49 TRP B C 1 ATOM 2438 O O . TRP C 3 49 ? 24.263 54.901 22.263 1.00 33.53 ? 49 TRP B O 1 ATOM 2439 C CB . TRP C 3 49 ? 23.037 52.664 20.418 1.00 31.18 ? 49 TRP B CB 1 ATOM 2440 C CG . TRP C 3 49 ? 23.105 51.392 19.642 1.00 29.85 ? 49 TRP B CG 1 ATOM 2441 C CD1 . TRP C 3 49 ? 23.683 50.225 20.034 1.00 30.92 ? 49 TRP B CD1 1 ATOM 2442 C CD2 . TRP C 3 49 ? 22.629 51.176 18.313 1.00 29.67 ? 49 TRP B CD2 1 ATOM 2443 N NE1 . TRP C 3 49 ? 23.601 49.290 19.032 1.00 29.44 ? 49 TRP B NE1 1 ATOM 2444 C CE2 . TRP C 3 49 ? 22.958 49.848 17.965 1.00 29.06 ? 49 TRP B CE2 1 ATOM 2445 C CE3 . TRP C 3 49 ? 21.957 51.976 17.380 1.00 30.75 ? 49 TRP B CE3 1 ATOM 2446 C CZ2 . TRP C 3 49 ? 22.635 49.300 16.726 1.00 29.39 ? 49 TRP B CZ2 1 ATOM 2447 C CZ3 . TRP C 3 49 ? 21.636 51.429 16.146 1.00 31.51 ? 49 TRP B CZ3 1 ATOM 2448 C CH2 . TRP C 3 49 ? 21.976 50.102 15.832 1.00 31.35 ? 49 TRP B CH2 1 ATOM 2449 N N . THR C 3 50 ? 23.899 55.863 20.264 1.00 33.19 ? 50 THR B N 1 ATOM 2450 C CA . THR C 3 50 ? 23.680 57.186 20.828 1.00 33.07 ? 50 THR B CA 1 ATOM 2451 C C . THR C 3 50 ? 22.185 57.398 20.938 1.00 34.74 ? 50 THR B C 1 ATOM 2452 O O . THR C 3 50 ? 21.480 57.387 19.931 1.00 34.92 ? 50 THR B O 1 ATOM 2453 C CB . THR C 3 50 ? 24.264 58.301 19.941 1.00 31.67 ? 50 THR B CB 1 ATOM 2454 O OG1 . THR C 3 50 ? 25.682 58.370 20.132 1.00 30.72 ? 50 THR B OG1 1 ATOM 2455 C CG2 . THR C 3 50 ? 23.633 59.646 20.285 1.00 29.41 ? 50 THR B CG2 1 ATOM 2456 N N . LEU C 3 51 ? 21.711 57.567 22.170 1.00 36.72 ? 51 LEU B N 1 ATOM 2457 C CA . LEU C 3 51 ? 20.297 57.808 22.452 1.00 38.36 ? 51 LEU B CA 1 ATOM 2458 C C . LEU C 3 51 ? 20.036 59.312 22.261 1.00 40.53 ? 51 LEU B C 1 ATOM 2459 O O . LEU C 3 51 ? 20.244 60.105 23.176 1.00 42.08 ? 51 LEU B O 1 ATOM 2460 C CB . LEU C 3 51 ? 19.973 57.391 23.898 1.00 36.29 ? 51 LEU B CB 1 ATOM 2461 C CG . LEU C 3 51 ? 19.664 55.929 24.257 1.00 34.23 ? 51 LEU B CG 1 ATOM 2462 C CD1 . LEU C 3 51 ? 20.631 54.992 23.575 1.00 35.83 ? 51 LEU B CD1 1 ATOM 2463 C CD2 . LEU C 3 51 ? 19.730 55.760 25.765 1.00 31.50 ? 51 LEU B CD2 1 ATOM 2464 N N . LYS C 3 52 ? 19.584 59.691 21.067 1.00 41.60 ? 52 LYS B N 1 ATOM 2465 C CA . LYS C 3 52 ? 19.323 61.087 20.728 1.00 42.05 ? 52 LYS B CA 1 ATOM 2466 C C . LYS C 3 52 ? 18.145 61.727 21.451 1.00 42.78 ? 52 LYS B C 1 ATOM 2467 O O . LYS C 3 52 ? 17.274 61.035 21.962 1.00 42.74 ? 52 LYS B O 1 ATOM 2468 C CB . LYS C 3 52 ? 19.123 61.212 19.216 1.00 42.01 ? 52 LYS B CB 1 ATOM 2469 C CG . LYS C 3 52 ? 20.419 61.173 18.426 1.00 42.18 ? 52 LYS B CG 1 ATOM 2470 C CD . LYS C 3 52 ? 21.296 62.318 18.877 1.00 43.04 ? 52 LYS B CD 1 ATOM 2471 C CE . LYS C 3 52 ? 22.424 62.601 17.923 1.00 44.32 ? 52 LYS B CE 1 ATOM 2472 N NZ . LYS C 3 52 ? 23.120 63.835 18.376 1.00 45.08 ? 52 LYS B NZ 1 ATOM 2473 N N . ARG C 3 53 ? 18.128 63.058 21.485 1.00 44.38 ? 53 ARG B N 1 ATOM 2474 C CA . ARG C 3 53 ? 17.062 63.810 22.146 1.00 45.21 ? 53 ARG B CA 1 ATOM 2475 C C . ARG C 3 53 ? 15.720 63.674 21.442 1.00 44.79 ? 53 ARG B C 1 ATOM 2476 O O . ARG C 3 53 ? 14.674 63.756 22.087 1.00 43.59 ? 53 ARG B O 1 ATOM 2477 C CB . ARG C 3 53 ? 17.397 65.301 22.220 1.00 47.35 ? 53 ARG B CB 1 ATOM 2478 C CG . ARG C 3 53 ? 18.465 65.688 23.219 1.00 49.56 ? 53 ARG B CG 1 ATOM 2479 C CD . ARG C 3 53 ? 18.492 67.207 23.374 1.00 53.12 ? 53 ARG B CD 1 ATOM 2480 N NE . ARG C 3 53 ? 19.508 67.655 24.325 1.00 57.74 ? 53 ARG B NE 1 ATOM 2481 C CZ . ARG C 3 53 ? 20.821 67.622 24.102 1.00 60.67 ? 53 ARG B CZ 1 ATOM 2482 N NH1 . ARG C 3 53 ? 21.294 67.163 22.948 1.00 62.11 ? 53 ARG B NH1 1 ATOM 2483 N NH2 . ARG C 3 53 ? 21.667 68.048 25.036 1.00 61.18 ? 53 ARG B NH2 1 ATOM 2484 N N . ASP C 3 54 ? 15.757 63.486 20.123 1.00 44.78 ? 54 ASP B N 1 ATOM 2485 C CA . ASP C 3 54 ? 14.542 63.359 19.311 1.00 44.90 ? 54 ASP B CA 1 ATOM 2486 C C . ASP C 3 54 ? 13.870 61.999 19.427 1.00 45.23 ? 54 ASP B C 1 ATOM 2487 O O . ASP C 3 54 ? 12.815 61.771 18.821 1.00 46.92 ? 54 ASP B O 1 ATOM 2488 C CB . ASP C 3 54 ? 14.846 63.617 17.834 1.00 44.55 ? 54 ASP B CB 1 ATOM 2489 C CG . ASP C 3 54 ? 15.956 62.734 17.309 1.00 44.07 ? 54 ASP B CG 1 ATOM 2490 O OD1 . ASP C 3 54 ? 16.270 61.718 17.967 1.00 44.20 ? 54 ASP B OD1 1 ATOM 2491 O OD2 . ASP C 3 54 ? 16.508 63.055 16.236 1.00 44.58 ? 54 ASP B OD2 1 ATOM 2492 N N . ASN C 3 55 ? 14.488 61.104 20.196 1.00 43.62 ? 55 ASN B N 1 ATOM 2493 C CA . ASN C 3 55 ? 13.976 59.757 20.413 1.00 41.02 ? 55 ASN B CA 1 ATOM 2494 C C . ASN C 3 55 ? 14.401 58.748 19.354 1.00 38.74 ? 55 ASN B C 1 ATOM 2495 O O . ASN C 3 55 ? 13.688 57.783 19.095 1.00 38.02 ? 55 ASN B O 1 ATOM 2496 C CB . ASN C 3 55 ? 12.450 59.772 20.518 1.00 42.31 ? 55 ASN B CB 1 ATOM 2497 C CG . ASN C 3 55 ? 11.961 60.039 21.929 1.00 43.52 ? 55 ASN B CG 1 ATOM 2498 O OD1 . ASN C 3 55 ? 10.766 60.207 22.153 1.00 45.58 ? 55 ASN B OD1 1 ATOM 2499 N ND2 . ASN C 3 55 ? 12.877 60.064 22.886 1.00 43.58 ? 55 ASN B ND2 1 ATOM 2500 N N . THR C 3 56 ? 15.552 58.975 18.732 1.00 37.34 ? 56 THR B N 1 ATOM 2501 C CA . THR C 3 56 ? 16.060 58.037 17.739 1.00 37.49 ? 56 THR B CA 1 ATOM 2502 C C . THR C 3 56 ? 17.322 57.414 18.333 1.00 37.41 ? 56 THR B C 1 ATOM 2503 O O . THR C 3 56 ? 18.044 58.065 19.092 1.00 37.49 ? 56 THR B O 1 ATOM 2504 C CB . THR C 3 56 ? 16.404 58.729 16.389 1.00 38.95 ? 56 THR B CB 1 ATOM 2505 O OG1 . THR C 3 56 ? 17.436 59.706 16.585 1.00 40.56 ? 56 THR B OG1 1 ATOM 2506 C CG2 . THR C 3 56 ? 15.169 59.406 15.809 1.00 40.82 ? 56 THR B CG2 1 ATOM 2507 N N . ILE C 3 57 ? 17.574 56.147 18.013 1.00 36.48 ? 57 ILE B N 1 ATOM 2508 C CA . ILE C 3 57 ? 18.755 55.456 18.524 1.00 34.36 ? 57 ILE B CA 1 ATOM 2509 C C . ILE C 3 57 ? 19.714 55.311 17.341 1.00 35.41 ? 57 ILE B C 1 ATOM 2510 O O . ILE C 3 57 ? 19.415 54.629 16.364 1.00 36.07 ? 57 ILE B O 1 ATOM 2511 C CB . ILE C 3 57 ? 18.365 54.083 19.119 1.00 31.16 ? 57 ILE B CB 1 ATOM 2512 C CG1 . ILE C 3 57 ? 17.105 54.241 19.975 1.00 27.91 ? 57 ILE B CG1 1 ATOM 2513 C CG2 . ILE C 3 57 ? 19.480 53.563 20.003 1.00 29.89 ? 57 ILE B CG2 1 ATOM 2514 C CD1 . ILE C 3 57 ? 16.526 52.948 20.470 1.00 27.19 ? 57 ILE B CD1 1 ATOM 2515 N N . ARG C 3 58 ? 20.866 55.968 17.429 1.00 36.10 ? 58 ARG B N 1 ATOM 2516 C CA . ARG C 3 58 ? 21.818 55.950 16.327 1.00 36.97 ? 58 ARG B CA 1 ATOM 2517 C C . ARG C 3 58 ? 23.162 55.309 16.563 1.00 37.54 ? 58 ARG B C 1 ATOM 2518 O O . ARG C 3 58 ? 23.816 55.540 17.576 1.00 39.29 ? 58 ARG B O 1 ATOM 2519 C CB . ARG C 3 58 ? 22.063 57.375 15.844 1.00 35.25 ? 58 ARG B CB 1 ATOM 2520 C CG . ARG C 3 58 ? 20.794 58.141 15.706 1.00 35.46 ? 58 ARG B CG 1 ATOM 2521 C CD . ARG C 3 58 ? 21.031 59.561 15.313 1.00 34.94 ? 58 ARG B CD 1 ATOM 2522 N NE . ARG C 3 58 ? 19.745 60.209 15.101 1.00 37.14 ? 58 ARG B NE 1 ATOM 2523 C CZ . ARG C 3 58 ? 19.570 61.271 14.330 1.00 38.38 ? 58 ARG B CZ 1 ATOM 2524 N NH1 . ARG C 3 58 ? 20.611 61.805 13.703 1.00 38.46 ? 58 ARG B NH1 1 ATOM 2525 N NH2 . ARG C 3 58 ? 18.354 61.778 14.165 1.00 38.09 ? 58 ARG B NH2 1 ATOM 2526 N N . SER C 3 59 ? 23.574 54.511 15.592 1.00 37.69 ? 59 SER B N 1 ATOM 2527 C CA . SER C 3 59 ? 24.866 53.866 15.640 1.00 37.49 ? 59 SER B CA 1 ATOM 2528 C C . SER C 3 59 ? 25.656 54.387 14.457 1.00 38.15 ? 59 SER B C 1 ATOM 2529 O O . SER C 3 59 ? 25.185 54.352 13.321 1.00 37.78 ? 59 SER B O 1 ATOM 2530 C CB . SER C 3 59 ? 24.738 52.355 15.520 1.00 37.95 ? 59 SER B CB 1 ATOM 2531 O OG . SER C 3 59 ? 26.005 51.787 15.228 1.00 36.90 ? 59 SER B OG 1 ATOM 2532 N N . ASN C 3 60 ? 26.846 54.900 14.736 1.00 38.75 ? 60 ASN B N 1 ATOM 2533 C CA . ASN C 3 60 ? 27.725 55.407 13.699 1.00 39.42 ? 60 ASN B CA 1 ATOM 2534 C C . ASN C 3 60 ? 27.071 56.384 12.719 1.00 39.11 ? 60 ASN B C 1 ATOM 2535 O O . ASN C 3 60 ? 27.522 56.534 11.584 1.00 38.60 ? 60 ASN B O 1 ATOM 2536 C CB . ASN C 3 60 ? 28.328 54.219 12.943 1.00 41.21 ? 60 ASN B CB 1 ATOM 2537 C CG . ASN C 3 60 ? 29.338 54.641 11.910 1.00 41.53 ? 60 ASN B CG 1 ATOM 2538 O OD1 . ASN C 3 60 ? 30.145 55.540 12.152 1.00 43.48 ? 60 ASN B OD1 1 ATOM 2539 N ND2 . ASN C 3 60 ? 29.309 53.994 10.753 1.00 41.56 ? 60 ASN B ND2 1 ATOM 2540 N N . GLY C 3 61 ? 26.007 57.051 13.153 1.00 39.18 ? 61 GLY B N 1 ATOM 2541 C CA . GLY C 3 61 ? 25.357 58.016 12.284 1.00 39.07 ? 61 GLY B CA 1 ATOM 2542 C C . GLY C 3 61 ? 24.001 57.624 11.737 1.00 39.58 ? 61 GLY B C 1 ATOM 2543 O O . GLY C 3 61 ? 23.203 58.491 11.388 1.00 40.93 ? 61 GLY B O 1 ATOM 2544 N N . LYS C 3 62 ? 23.727 56.327 11.663 1.00 39.16 ? 62 LYS B N 1 ATOM 2545 C CA . LYS C 3 62 ? 22.453 55.859 11.135 1.00 39.49 ? 62 LYS B CA 1 ATOM 2546 C C . LYS C 3 62 ? 21.407 55.565 12.221 1.00 38.92 ? 62 LYS B C 1 ATOM 2547 O O . LYS C 3 62 ? 21.738 55.363 13.388 1.00 38.66 ? 62 LYS B O 1 ATOM 2548 C CB . LYS C 3 62 ? 22.695 54.622 10.281 1.00 41.36 ? 62 LYS B CB 1 ATOM 2549 C CG . LYS C 3 62 ? 23.739 54.832 9.192 1.00 43.88 ? 62 LYS B CG 1 ATOM 2550 C CD . LYS C 3 62 ? 23.122 54.668 7.804 1.00 46.76 ? 62 LYS B CD 1 ATOM 2551 C CE . LYS C 3 62 ? 24.166 54.773 6.698 1.00 47.05 ? 62 LYS B CE 1 ATOM 2552 N NZ . LYS C 3 62 ? 23.567 54.504 5.358 1.00 45.54 ? 62 LYS B NZ 1 ATOM 2553 N N . CYS C 3 63 ? 20.142 55.532 11.819 1.00 38.59 ? 63 CYS B N 1 ATOM 2554 C CA . CYS C 3 63 ? 19.034 55.291 12.739 1.00 38.30 ? 63 CYS B CA 1 ATOM 2555 C C . CYS C 3 63 ? 18.546 53.849 12.836 1.00 36.82 ? 63 CYS B C 1 ATOM 2556 O O . CYS C 3 63 ? 18.424 53.146 11.830 1.00 37.67 ? 63 CYS B O 1 ATOM 2557 C CB . CYS C 3 63 ? 17.839 56.185 12.358 1.00 39.88 ? 63 CYS B CB 1 ATOM 2558 S SG . CYS C 3 63 ? 18.014 57.891 12.966 1.00 42.17 ? 63 CYS B SG 1 ATOM 2559 N N . LEU C 3 64 ? 18.262 53.414 14.059 1.00 34.34 ? 64 LEU B N 1 ATOM 2560 C CA . LEU C 3 64 ? 17.727 52.077 14.276 1.00 31.95 ? 64 LEU B CA 1 ATOM 2561 C C . LEU C 3 64 ? 16.300 52.181 13.756 1.00 32.89 ? 64 LEU B C 1 ATOM 2562 O O . LEU C 3 64 ? 15.442 52.769 14.413 1.00 33.86 ? 64 LEU B O 1 ATOM 2563 C CB . LEU C 3 64 ? 17.690 51.736 15.763 1.00 28.73 ? 64 LEU B CB 1 ATOM 2564 C CG . LEU C 3 64 ? 16.972 50.425 16.093 1.00 26.05 ? 64 LEU B CG 1 ATOM 2565 C CD1 . LEU C 3 64 ? 17.975 49.299 16.150 1.00 26.83 ? 64 LEU B CD1 1 ATOM 2566 C CD2 . LEU C 3 64 ? 16.260 50.549 17.415 1.00 24.07 ? 64 LEU B CD2 1 ATOM 2567 N N . THR C 3 65 ? 16.044 51.608 12.586 1.00 32.79 ? 65 THR B N 1 ATOM 2568 C CA . THR C 3 65 ? 14.724 51.685 11.981 1.00 33.53 ? 65 THR B CA 1 ATOM 2569 C C . THR C 3 65 ? 13.972 50.359 11.870 1.00 34.81 ? 65 THR B C 1 ATOM 2570 O O . THR C 3 65 ? 14.571 49.320 11.606 1.00 35.88 ? 65 THR B O 1 ATOM 2571 C CB . THR C 3 65 ? 14.846 52.294 10.580 1.00 32.65 ? 65 THR B CB 1 ATOM 2572 O OG1 . THR C 3 65 ? 15.647 53.477 10.656 1.00 33.72 ? 65 THR B OG1 1 ATOM 2573 C CG2 . THR C 3 65 ? 13.486 52.650 10.026 1.00 32.59 ? 65 THR B CG2 1 ATOM 2574 N N . THR C 3 66 ? 12.659 50.394 12.081 1.00 35.48 ? 66 THR B N 1 ATOM 2575 C CA . THR C 3 66 ? 11.844 49.191 11.950 1.00 36.78 ? 66 THR B CA 1 ATOM 2576 C C . THR C 3 66 ? 11.359 49.094 10.489 1.00 37.75 ? 66 THR B C 1 ATOM 2577 O O . THR C 3 66 ? 11.100 50.116 9.850 1.00 39.04 ? 66 THR B O 1 ATOM 2578 C CB . THR C 3 66 ? 10.639 49.215 12.918 1.00 35.85 ? 66 THR B CB 1 ATOM 2579 O OG1 . THR C 3 66 ? 9.729 48.164 12.571 1.00 37.93 ? 66 THR B OG1 1 ATOM 2580 C CG2 . THR C 3 66 ? 9.926 50.549 12.864 1.00 35.80 ? 66 THR B CG2 1 ATOM 2581 N N . TYR C 3 67 ? 11.248 47.876 9.961 1.00 38.21 ? 67 TYR B N 1 ATOM 2582 C CA . TYR C 3 67 ? 10.828 47.671 8.571 1.00 39.24 ? 67 TYR B CA 1 ATOM 2583 C C . TYR C 3 67 ? 9.382 48.071 8.314 1.00 39.79 ? 67 TYR B C 1 ATOM 2584 O O . TYR C 3 67 ? 9.066 48.682 7.288 1.00 39.90 ? 67 TYR B O 1 ATOM 2585 C CB . TYR C 3 67 ? 11.018 46.204 8.182 1.00 39.59 ? 67 TYR B CB 1 ATOM 2586 C CG . TYR C 3 67 ? 10.752 45.890 6.724 1.00 41.88 ? 67 TYR B CG 1 ATOM 2587 C CD1 . TYR C 3 67 ? 11.647 46.286 5.728 1.00 41.99 ? 67 TYR B CD1 1 ATOM 2588 C CD2 . TYR C 3 67 ? 9.633 45.144 6.343 1.00 44.11 ? 67 TYR B CD2 1 ATOM 2589 C CE1 . TYR C 3 67 ? 11.447 45.941 4.390 1.00 43.94 ? 67 TYR B CE1 1 ATOM 2590 C CE2 . TYR C 3 67 ? 9.415 44.790 5.001 1.00 44.90 ? 67 TYR B CE2 1 ATOM 2591 C CZ . TYR C 3 67 ? 10.328 45.189 4.030 1.00 45.31 ? 67 TYR B CZ 1 ATOM 2592 O OH . TYR C 3 67 ? 10.124 44.829 2.713 1.00 45.43 ? 67 TYR B OH 1 ATOM 2593 N N . GLY C 3 68 ? 8.508 47.708 9.248 1.00 41.11 ? 68 GLY B N 1 ATOM 2594 C CA . GLY C 3 68 ? 7.093 48.018 9.127 1.00 42.37 ? 68 GLY B CA 1 ATOM 2595 C C . GLY C 3 68 ? 6.422 47.986 10.487 1.00 42.96 ? 68 GLY B C 1 ATOM 2596 O O . GLY C 3 68 ? 7.071 47.707 11.494 1.00 44.05 ? 68 GLY B O 1 ATOM 2597 N N . TYR C 3 69 ? 5.124 48.265 10.530 1.00 42.27 ? 69 TYR B N 1 ATOM 2598 C CA . TYR C 3 69 ? 4.409 48.273 11.797 1.00 40.83 ? 69 TYR B CA 1 ATOM 2599 C C . TYR C 3 69 ? 3.569 47.014 11.927 1.00 40.70 ? 69 TYR B C 1 ATOM 2600 O O . TYR C 3 69 ? 2.390 47.069 12.273 1.00 40.97 ? 69 TYR B O 1 ATOM 2601 C CB . TYR C 3 69 ? 3.543 49.531 11.888 1.00 39.22 ? 69 TYR B CB 1 ATOM 2602 C CG . TYR C 3 69 ? 4.279 50.754 11.389 1.00 39.98 ? 69 TYR B CG 1 ATOM 2603 C CD1 . TYR C 3 69 ? 5.529 51.099 11.906 1.00 41.75 ? 69 TYR B CD1 1 ATOM 2604 C CD2 . TYR C 3 69 ? 3.765 51.523 10.353 1.00 39.87 ? 69 TYR B CD2 1 ATOM 2605 C CE1 . TYR C 3 69 ? 6.249 52.178 11.392 1.00 42.71 ? 69 TYR B CE1 1 ATOM 2606 C CE2 . TYR C 3 69 ? 4.472 52.600 9.834 1.00 40.72 ? 69 TYR B CE2 1 ATOM 2607 C CZ . TYR C 3 69 ? 5.712 52.921 10.353 1.00 42.18 ? 69 TYR B CZ 1 ATOM 2608 O OH . TYR C 3 69 ? 6.411 53.978 9.819 1.00 44.92 ? 69 TYR B OH 1 ATOM 2609 N N . SER C 3 70 ? 4.196 45.875 11.645 1.00 40.45 ? 70 SER B N 1 ATOM 2610 C CA . SER C 3 70 ? 3.531 44.579 11.719 1.00 40.30 ? 70 SER B CA 1 ATOM 2611 C C . SER C 3 70 ? 4.372 43.614 12.556 1.00 39.72 ? 70 SER B C 1 ATOM 2612 O O . SER C 3 70 ? 5.592 43.523 12.386 1.00 39.68 ? 70 SER B O 1 ATOM 2613 C CB . SER C 3 70 ? 3.333 44.004 10.309 1.00 40.19 ? 70 SER B CB 1 ATOM 2614 O OG . SER C 3 70 ? 2.669 44.924 9.459 1.00 41.34 ? 70 SER B OG 1 ATOM 2615 N N . PRO C 3 71 ? 3.728 42.882 13.476 1.00 37.94 ? 71 PRO B N 1 ATOM 2616 C CA . PRO C 3 71 ? 4.435 41.929 14.330 1.00 37.93 ? 71 PRO B CA 1 ATOM 2617 C C . PRO C 3 71 ? 5.199 40.891 13.522 1.00 37.94 ? 71 PRO B C 1 ATOM 2618 O O . PRO C 3 71 ? 4.608 39.954 12.987 1.00 39.10 ? 71 PRO B O 1 ATOM 2619 C CB . PRO C 3 71 ? 3.311 41.304 15.146 1.00 37.19 ? 71 PRO B CB 1 ATOM 2620 C CG . PRO C 3 71 ? 2.316 42.412 15.238 1.00 38.26 ? 71 PRO B CG 1 ATOM 2621 C CD . PRO C 3 71 ? 2.302 42.944 13.836 1.00 37.51 ? 71 PRO B CD 1 ATOM 2622 N N . GLY C 3 72 ? 6.511 41.055 13.429 1.00 37.03 ? 72 GLY B N 1 ATOM 2623 C CA . GLY C 3 72 ? 7.289 40.093 12.681 1.00 36.47 ? 72 GLY B CA 1 ATOM 2624 C C . GLY C 3 72 ? 8.351 40.712 11.799 1.00 36.44 ? 72 GLY B C 1 ATOM 2625 O O . GLY C 3 72 ? 9.364 40.069 11.524 1.00 38.02 ? 72 GLY B O 1 ATOM 2626 N N . VAL C 3 73 ? 8.131 41.943 11.342 1.00 35.65 ? 73 VAL B N 1 ATOM 2627 C CA . VAL C 3 73 ? 9.113 42.614 10.493 1.00 34.48 ? 73 VAL B CA 1 ATOM 2628 C C . VAL C 3 73 ? 10.407 42.764 11.291 1.00 34.66 ? 73 VAL B C 1 ATOM 2629 O O . VAL C 3 73 ? 10.376 42.781 12.521 1.00 34.53 ? 73 VAL B O 1 ATOM 2630 C CB . VAL C 3 73 ? 8.615 44.004 10.050 1.00 33.68 ? 73 VAL B CB 1 ATOM 2631 C CG1 . VAL C 3 73 ? 7.295 43.869 9.317 1.00 33.33 ? 73 VAL B CG1 1 ATOM 2632 C CG2 . VAL C 3 73 ? 8.464 44.912 11.254 1.00 34.45 ? 73 VAL B CG2 1 ATOM 2633 N N . TYR C 3 74 ? 11.543 42.856 10.608 1.00 34.95 ? 74 TYR B N 1 ATOM 2634 C CA . TYR C 3 74 ? 12.812 42.983 11.319 1.00 35.87 ? 74 TYR B CA 1 ATOM 2635 C C . TYR C 3 74 ? 13.219 44.437 11.487 1.00 35.74 ? 74 TYR B C 1 ATOM 2636 O O . TYR C 3 74 ? 12.627 45.330 10.887 1.00 35.95 ? 74 TYR B O 1 ATOM 2637 C CB . TYR C 3 74 ? 13.925 42.202 10.597 1.00 36.76 ? 74 TYR B CB 1 ATOM 2638 C CG . TYR C 3 74 ? 14.502 42.883 9.371 1.00 39.12 ? 74 TYR B CG 1 ATOM 2639 C CD1 . TYR C 3 74 ? 13.689 43.241 8.291 1.00 40.63 ? 74 TYR B CD1 1 ATOM 2640 C CD2 . TYR C 3 74 ? 15.863 43.191 9.298 1.00 40.53 ? 74 TYR B CD2 1 ATOM 2641 C CE1 . TYR C 3 74 ? 14.213 43.893 7.173 1.00 38.71 ? 74 TYR B CE1 1 ATOM 2642 C CE2 . TYR C 3 74 ? 16.396 43.844 8.183 1.00 40.16 ? 74 TYR B CE2 1 ATOM 2643 C CZ . TYR C 3 74 ? 15.561 44.192 7.132 1.00 39.42 ? 74 TYR B CZ 1 ATOM 2644 O OH . TYR C 3 74 ? 16.077 44.870 6.056 1.00 41.58 ? 74 TYR B OH 1 ATOM 2645 N N . VAL C 3 75 ? 14.221 44.661 12.329 1.00 35.71 ? 75 VAL B N 1 ATOM 2646 C CA . VAL C 3 75 ? 14.741 45.994 12.590 1.00 35.89 ? 75 VAL B CA 1 ATOM 2647 C C . VAL C 3 75 ? 16.053 46.106 11.824 1.00 36.69 ? 75 VAL B C 1 ATOM 2648 O O . VAL C 3 75 ? 16.925 45.241 11.939 1.00 36.99 ? 75 VAL B O 1 ATOM 2649 C CB . VAL C 3 75 ? 14.998 46.206 14.098 1.00 36.67 ? 75 VAL B CB 1 ATOM 2650 C CG1 . VAL C 3 75 ? 15.562 47.598 14.351 1.00 35.15 ? 75 VAL B CG1 1 ATOM 2651 C CG2 . VAL C 3 75 ? 13.709 46.016 14.866 1.00 35.99 ? 75 VAL B CG2 1 ATOM 2652 N N . MET C 3 76 ? 16.183 47.180 11.053 1.00 36.88 ? 76 MET B N 1 ATOM 2653 C CA . MET C 3 76 ? 17.357 47.422 10.221 1.00 37.76 ? 76 MET B CA 1 ATOM 2654 C C . MET C 3 76 ? 18.042 48.744 10.550 1.00 38.42 ? 76 MET B C 1 ATOM 2655 O O . MET C 3 76 ? 17.489 49.579 11.258 1.00 39.06 ? 76 MET B O 1 ATOM 2656 C CB . MET C 3 76 ? 16.909 47.484 8.769 1.00 38.31 ? 76 MET B CB 1 ATOM 2657 C CG . MET C 3 76 ? 15.993 48.685 8.535 1.00 39.75 ? 76 MET B CG 1 ATOM 2658 S SD . MET C 3 76 ? 15.169 48.779 6.941 1.00 37.53 ? 76 MET B SD 1 ATOM 2659 C CE . MET C 3 76 ? 13.925 47.618 7.223 1.00 40.25 ? 76 MET B CE 1 ATOM 2660 N N . ILE C 3 77 ? 19.247 48.934 10.022 1.00 39.83 ? 77 ILE B N 1 ATOM 2661 C CA . ILE C 3 77 ? 19.963 50.191 10.212 1.00 40.90 ? 77 ILE B CA 1 ATOM 2662 C C . ILE C 3 77 ? 19.528 50.992 8.988 1.00 42.09 ? 77 ILE B C 1 ATOM 2663 O O . ILE C 3 77 ? 19.274 50.406 7.941 1.00 42.64 ? 77 ILE B O 1 ATOM 2664 C CB . ILE C 3 77 ? 21.501 49.993 10.190 1.00 40.17 ? 77 ILE B CB 1 ATOM 2665 C CG1 . ILE C 3 77 ? 22.196 51.296 10.583 1.00 39.35 ? 77 ILE B CG1 1 ATOM 2666 C CG2 . ILE C 3 77 ? 21.959 49.560 8.808 1.00 40.98 ? 77 ILE B CG2 1 ATOM 2667 C CD1 . ILE C 3 77 ? 21.782 51.804 11.942 1.00 39.44 ? 77 ILE B CD1 1 ATOM 2668 N N . TYR C 3 78 ? 19.425 52.311 9.098 1.00 43.84 ? 78 TYR B N 1 ATOM 2669 C CA . TYR C 3 78 ? 18.984 53.094 7.945 1.00 45.28 ? 78 TYR B CA 1 ATOM 2670 C C . TYR C 3 78 ? 19.352 54.573 8.043 1.00 46.51 ? 78 TYR B C 1 ATOM 2671 O O . TYR C 3 78 ? 19.666 55.079 9.122 1.00 46.23 ? 78 TYR B O 1 ATOM 2672 C CB . TYR C 3 78 ? 17.462 52.968 7.793 1.00 45.30 ? 78 TYR B CB 1 ATOM 2673 C CG . TYR C 3 78 ? 16.979 52.909 6.363 1.00 44.91 ? 78 TYR B CG 1 ATOM 2674 C CD1 . TYR C 3 78 ? 17.090 51.733 5.621 1.00 46.12 ? 78 TYR B CD1 1 ATOM 2675 C CD2 . TYR C 3 78 ? 16.420 54.025 5.748 1.00 44.42 ? 78 TYR B CD2 1 ATOM 2676 C CE1 . TYR C 3 78 ? 16.654 51.669 4.301 1.00 45.73 ? 78 TYR B CE1 1 ATOM 2677 C CE2 . TYR C 3 78 ? 15.981 53.974 4.424 1.00 45.10 ? 78 TYR B CE2 1 ATOM 2678 C CZ . TYR C 3 78 ? 16.103 52.790 3.711 1.00 45.49 ? 78 TYR B CZ 1 ATOM 2679 O OH . TYR C 3 78 ? 15.680 52.719 2.407 1.00 44.91 ? 78 TYR B OH 1 ATOM 2680 N N . ASP C 3 79 ? 19.317 55.260 6.904 1.00 47.26 ? 79 ASP B N 1 ATOM 2681 C CA . ASP C 3 79 ? 19.614 56.686 6.876 1.00 47.68 ? 79 ASP B CA 1 ATOM 2682 C C . ASP C 3 79 ? 18.452 57.340 7.610 1.00 47.48 ? 79 ASP B C 1 ATOM 2683 O O . ASP C 3 79 ? 17.289 57.085 7.284 1.00 46.14 ? 79 ASP B O 1 ATOM 2684 C CB . ASP C 3 79 ? 19.649 57.202 5.442 1.00 50.02 ? 79 ASP B CB 1 ATOM 2685 C CG . ASP C 3 79 ? 20.078 58.647 5.361 1.00 51.99 ? 79 ASP B CG 1 ATOM 2686 O OD1 . ASP C 3 79 ? 19.708 59.430 6.262 1.00 53.97 ? 79 ASP B OD1 1 ATOM 2687 O OD2 . ASP C 3 79 ? 20.776 59.005 4.393 1.00 53.81 ? 79 ASP B OD2 1 ATOM 2688 N N . CYS C 3 80 ? 18.767 58.186 8.587 1.00 47.25 ? 80 CYS B N 1 ATOM 2689 C CA . CYS C 3 80 ? 17.747 58.852 9.390 1.00 47.20 ? 80 CYS B CA 1 ATOM 2690 C C . CYS C 3 80 ? 16.778 59.769 8.638 1.00 48.37 ? 80 CYS B C 1 ATOM 2691 O O . CYS C 3 80 ? 15.618 59.902 9.035 1.00 49.31 ? 80 CYS B O 1 ATOM 2692 C CB . CYS C 3 80 ? 18.408 59.648 10.509 1.00 46.18 ? 80 CYS B CB 1 ATOM 2693 S SG . CYS C 3 80 ? 19.392 58.709 11.722 1.00 46.54 ? 80 CYS B SG 1 ATOM 2694 N N . ASN C 3 81 ? 17.243 60.408 7.567 1.00 49.54 ? 81 ASN B N 1 ATOM 2695 C CA . ASN C 3 81 ? 16.388 61.308 6.794 1.00 49.59 ? 81 ASN B CA 1 ATOM 2696 C C . ASN C 3 81 ? 15.565 60.589 5.740 1.00 49.46 ? 81 ASN B C 1 ATOM 2697 O O . ASN C 3 81 ? 14.449 61.004 5.423 1.00 50.13 ? 81 ASN B O 1 ATOM 2698 C CB . ASN C 3 81 ? 17.231 62.383 6.128 1.00 50.03 ? 81 ASN B CB 1 ATOM 2699 C CG . ASN C 3 81 ? 17.968 63.222 7.132 1.00 52.04 ? 81 ASN B CG 1 ATOM 2700 O OD1 . ASN C 3 81 ? 17.354 63.849 8.000 1.00 52.13 ? 81 ASN B OD1 1 ATOM 2701 N ND2 . ASN C 3 81 ? 19.297 63.233 7.036 1.00 52.46 ? 81 ASN B ND2 1 ATOM 2702 N N . THR C 3 82 ? 16.124 59.510 5.203 1.00 48.65 ? 82 THR B N 1 ATOM 2703 C CA . THR C 3 82 ? 15.457 58.718 4.181 1.00 47.33 ? 82 THR B CA 1 ATOM 2704 C C . THR C 3 82 ? 14.309 57.921 4.803 1.00 46.01 ? 82 THR B C 1 ATOM 2705 O O . THR C 3 82 ? 13.180 57.955 4.322 1.00 44.26 ? 82 THR B O 1 ATOM 2706 C CB . THR C 3 82 ? 16.449 57.721 3.531 1.00 49.47 ? 82 THR B CB 1 ATOM 2707 O OG1 . THR C 3 82 ? 17.674 58.398 3.217 1.00 50.55 ? 82 THR B OG1 1 ATOM 2708 C CG2 . THR C 3 82 ? 15.855 57.118 2.257 1.00 49.37 ? 82 THR B CG2 1 ATOM 2709 N N . ALA C 3 83 ? 14.620 57.211 5.884 1.00 45.82 ? 83 ALA B N 1 ATOM 2710 C CA . ALA C 3 83 ? 13.655 56.369 6.584 1.00 46.68 ? 83 ALA B CA 1 ATOM 2711 C C . ALA C 3 83 ? 12.347 57.072 6.907 1.00 47.45 ? 83 ALA B C 1 ATOM 2712 O O . ALA C 3 83 ? 12.328 58.281 7.147 1.00 49.25 ? 83 ALA B O 1 ATOM 2713 C CB . ALA C 3 83 ? 14.277 55.827 7.869 1.00 45.74 ? 83 ALA B CB 1 ATOM 2714 N N . ALA C 3 84 ? 11.251 56.313 6.908 1.00 46.95 ? 84 ALA B N 1 ATOM 2715 C CA . ALA C 3 84 ? 9.954 56.886 7.245 1.00 46.77 ? 84 ALA B CA 1 ATOM 2716 C C . ALA C 3 84 ? 10.180 57.501 8.621 1.00 47.07 ? 84 ALA B C 1 ATOM 2717 O O . ALA C 3 84 ? 10.739 56.859 9.508 1.00 47.82 ? 84 ALA B O 1 ATOM 2718 C CB . ALA C 3 84 ? 8.891 55.800 7.311 1.00 46.10 ? 84 ALA B CB 1 ATOM 2719 N N . THR C 3 85 ? 9.761 58.746 8.800 1.00 47.29 ? 85 THR B N 1 ATOM 2720 C CA . THR C 3 85 ? 9.979 59.424 10.067 1.00 46.82 ? 85 THR B CA 1 ATOM 2721 C C . THR C 3 85 ? 9.635 58.644 11.352 1.00 47.34 ? 85 THR B C 1 ATOM 2722 O O . THR C 3 85 ? 10.552 58.227 12.068 1.00 47.71 ? 85 THR B O 1 ATOM 2723 C CB . THR C 3 85 ? 9.275 60.798 10.076 1.00 46.33 ? 85 THR B CB 1 ATOM 2724 O OG1 . THR C 3 85 ? 9.742 61.558 11.196 1.00 44.86 ? 85 THR B OG1 1 ATOM 2725 C CG2 . THR C 3 85 ? 7.758 60.637 10.147 1.00 46.78 ? 85 THR B CG2 1 ATOM 2726 N N . ASP C 3 86 ? 8.353 58.420 11.655 1.00 47.07 ? 86 ASP B N 1 ATOM 2727 C CA . ASP C 3 86 ? 8.024 57.712 12.894 1.00 47.73 ? 86 ASP B CA 1 ATOM 2728 C C . ASP C 3 86 ? 8.321 56.206 12.942 1.00 46.63 ? 86 ASP B C 1 ATOM 2729 O O . ASP C 3 86 ? 7.715 55.450 13.712 1.00 46.34 ? 86 ASP B O 1 ATOM 2730 C CB . ASP C 3 86 ? 6.572 57.996 13.334 1.00 50.69 ? 86 ASP B CB 1 ATOM 2731 C CG . ASP C 3 86 ? 5.552 57.813 12.221 1.00 53.38 ? 86 ASP B CG 1 ATOM 2732 O OD1 . ASP C 3 86 ? 5.588 56.781 11.513 1.00 54.78 ? 86 ASP B OD1 1 ATOM 2733 O OD2 . ASP C 3 86 ? 4.689 58.709 12.071 1.00 54.71 ? 86 ASP B OD2 1 ATOM 2734 N N . ALA C 3 87 ? 9.281 55.777 12.132 1.00 45.37 ? 87 ALA B N 1 ATOM 2735 C CA . ALA C 3 87 ? 9.691 54.381 12.127 1.00 43.49 ? 87 ALA B CA 1 ATOM 2736 C C . ALA C 3 87 ? 11.114 54.331 12.677 1.00 42.64 ? 87 ALA B C 1 ATOM 2737 O O . ALA C 3 87 ? 11.771 53.293 12.628 1.00 43.17 ? 87 ALA B O 1 ATOM 2738 C CB . ALA C 3 87 ? 9.639 53.807 10.721 1.00 44.21 ? 87 ALA B CB 1 ATOM 2739 N N . THR C 3 88 ? 11.585 55.471 13.182 1.00 41.69 ? 88 THR B N 1 ATOM 2740 C CA . THR C 3 88 ? 12.916 55.585 13.778 1.00 40.87 ? 88 THR B CA 1 ATOM 2741 C C . THR C 3 88 ? 12.780 56.033 15.229 1.00 40.96 ? 88 THR B C 1 ATOM 2742 O O . THR C 3 88 ? 13.784 56.163 15.934 1.00 40.41 ? 88 THR B O 1 ATOM 2743 C CB . THR C 3 88 ? 13.784 56.631 13.070 1.00 40.13 ? 88 THR B CB 1 ATOM 2744 O OG1 . THR C 3 88 ? 13.129 57.902 13.116 1.00 38.77 ? 88 THR B OG1 1 ATOM 2745 C CG2 . THR C 3 88 ? 14.034 56.233 11.635 1.00 39.88 ? 88 THR B CG2 1 ATOM 2746 N N . ARG C 3 89 ? 11.536 56.267 15.651 1.00 41.99 ? 89 ARG B N 1 ATOM 2747 C CA . ARG C 3 89 ? 11.201 56.717 17.004 1.00 43.52 ? 89 ARG B CA 1 ATOM 2748 C C . ARG C 3 89 ? 10.987 55.581 18.010 1.00 43.18 ? 89 ARG B C 1 ATOM 2749 O O . ARG C 3 89 ? 10.200 54.659 17.764 1.00 42.64 ? 89 ARG B O 1 ATOM 2750 C CB . ARG C 3 89 ? 9.926 57.575 16.969 1.00 46.34 ? 89 ARG B CB 1 ATOM 2751 C CG . ARG C 3 89 ? 10.058 58.871 16.205 1.00 50.63 ? 89 ARG B CG 1 ATOM 2752 C CD . ARG C 3 89 ? 11.060 59.792 16.889 1.00 55.74 ? 89 ARG B CD 1 ATOM 2753 N NE . ARG C 3 89 ? 11.831 60.566 15.922 1.00 60.16 ? 89 ARG B NE 1 ATOM 2754 C CZ . ARG C 3 89 ? 11.313 61.480 15.109 1.00 61.00 ? 89 ARG B CZ 1 ATOM 2755 N NH1 . ARG C 3 89 ? 10.009 61.747 15.150 1.00 61.54 ? 89 ARG B NH1 1 ATOM 2756 N NH2 . ARG C 3 89 ? 12.098 62.110 14.239 1.00 60.41 ? 89 ARG B NH2 1 ATOM 2757 N N . TRP C 3 90 ? 11.679 55.662 19.150 1.00 42.14 ? 90 TRP B N 1 ATOM 2758 C CA . TRP C 3 90 ? 11.554 54.663 20.217 1.00 40.32 ? 90 TRP B CA 1 ATOM 2759 C C . TRP C 3 90 ? 11.632 55.306 21.605 1.00 39.46 ? 90 TRP B C 1 ATOM 2760 O O . TRP C 3 90 ? 12.303 56.320 21.799 1.00 40.41 ? 90 TRP B O 1 ATOM 2761 C CB . TRP C 3 90 ? 12.667 53.604 20.137 1.00 39.41 ? 90 TRP B CB 1 ATOM 2762 C CG . TRP C 3 90 ? 12.887 52.992 18.802 1.00 38.55 ? 90 TRP B CG 1 ATOM 2763 C CD1 . TRP C 3 90 ? 13.631 53.506 17.787 1.00 38.47 ? 90 TRP B CD1 1 ATOM 2764 C CD2 . TRP C 3 90 ? 12.371 51.736 18.327 1.00 38.53 ? 90 TRP B CD2 1 ATOM 2765 N NE1 . TRP C 3 90 ? 13.618 52.652 16.708 1.00 38.91 ? 90 TRP B NE1 1 ATOM 2766 C CE2 . TRP C 3 90 ? 12.851 51.559 17.012 1.00 37.77 ? 90 TRP B CE2 1 ATOM 2767 C CE3 . TRP C 3 90 ? 11.552 50.745 18.885 1.00 38.74 ? 90 TRP B CE3 1 ATOM 2768 C CZ2 . TRP C 3 90 ? 12.539 50.430 16.244 1.00 37.06 ? 90 TRP B CZ2 1 ATOM 2769 C CZ3 . TRP C 3 90 ? 11.242 49.615 18.115 1.00 37.66 ? 90 TRP B CZ3 1 ATOM 2770 C CH2 . TRP C 3 90 ? 11.736 49.472 16.813 1.00 36.28 ? 90 TRP B CH2 1 ATOM 2771 N N . GLN C 3 91 ? 10.940 54.707 22.569 1.00 37.45 ? 91 GLN B N 1 ATOM 2772 C CA . GLN C 3 91 ? 10.978 55.183 23.944 1.00 35.35 ? 91 GLN B CA 1 ATOM 2773 C C . GLN C 3 91 ? 11.551 54.035 24.747 1.00 33.62 ? 91 GLN B C 1 ATOM 2774 O O . GLN C 3 91 ? 11.170 52.885 24.542 1.00 34.12 ? 91 GLN B O 1 ATOM 2775 C CB . GLN C 3 91 ? 9.585 55.468 24.487 1.00 35.24 ? 91 GLN B CB 1 ATOM 2776 C CG . GLN C 3 91 ? 8.689 56.237 23.575 1.00 38.91 ? 91 GLN B CG 1 ATOM 2777 C CD . GLN C 3 91 ? 7.362 56.564 24.236 1.00 42.84 ? 91 GLN B CD 1 ATOM 2778 O OE1 . GLN C 3 91 ? 6.746 55.716 24.902 1.00 44.60 ? 91 GLN B OE1 1 ATOM 2779 N NE2 . GLN C 3 91 ? 6.905 57.797 24.049 1.00 43.88 ? 91 GLN B NE2 1 ATOM 2780 N N . ILE C 3 92 ? 12.469 54.333 25.652 1.00 31.79 ? 92 ILE B N 1 ATOM 2781 C CA . ILE C 3 92 ? 13.042 53.296 26.494 1.00 30.68 ? 92 ILE B CA 1 ATOM 2782 C C . ILE C 3 92 ? 12.419 53.433 27.873 1.00 31.61 ? 92 ILE B C 1 ATOM 2783 O O . ILE C 3 92 ? 12.608 54.440 28.550 1.00 33.86 ? 92 ILE B O 1 ATOM 2784 C CB . ILE C 3 92 ? 14.563 53.434 26.565 1.00 27.92 ? 92 ILE B CB 1 ATOM 2785 C CG1 . ILE C 3 92 ? 15.121 53.283 25.151 1.00 26.94 ? 92 ILE B CG1 1 ATOM 2786 C CG2 . ILE C 3 92 ? 15.148 52.389 27.493 1.00 24.65 ? 92 ILE B CG2 1 ATOM 2787 C CD1 . ILE C 3 92 ? 16.606 53.345 25.061 1.00 28.70 ? 92 ILE B CD1 1 ATOM 2788 N N . TRP C 3 93 ? 11.655 52.424 28.274 1.00 31.81 ? 93 TRP B N 1 ATOM 2789 C CA . TRP C 3 93 ? 10.970 52.437 29.559 1.00 32.46 ? 93 TRP B CA 1 ATOM 2790 C C . TRP C 3 93 ? 11.790 51.912 30.723 1.00 34.39 ? 93 TRP B C 1 ATOM 2791 O O . TRP C 3 93 ? 12.729 51.133 30.538 1.00 35.46 ? 93 TRP B O 1 ATOM 2792 C CB . TRP C 3 93 ? 9.690 51.625 29.466 1.00 30.55 ? 93 TRP B CB 1 ATOM 2793 C CG . TRP C 3 93 ? 8.717 52.157 28.498 1.00 28.05 ? 93 TRP B CG 1 ATOM 2794 C CD1 . TRP C 3 93 ? 8.762 53.358 27.858 1.00 26.97 ? 93 TRP B CD1 1 ATOM 2795 C CD2 . TRP C 3 93 ? 7.506 51.524 28.089 1.00 27.83 ? 93 TRP B CD2 1 ATOM 2796 N NE1 . TRP C 3 93 ? 7.647 53.514 27.075 1.00 27.81 ? 93 TRP B NE1 1 ATOM 2797 C CE2 . TRP C 3 93 ? 6.861 52.403 27.199 1.00 27.85 ? 93 TRP B CE2 1 ATOM 2798 C CE3 . TRP C 3 93 ? 6.905 50.298 28.390 1.00 29.29 ? 93 TRP B CE3 1 ATOM 2799 C CZ2 . TRP C 3 93 ? 5.637 52.092 26.604 1.00 29.22 ? 93 TRP B CZ2 1 ATOM 2800 C CZ3 . TRP C 3 93 ? 5.682 49.989 27.797 1.00 29.42 ? 93 TRP B CZ3 1 ATOM 2801 C CH2 . TRP C 3 93 ? 5.063 50.884 26.914 1.00 28.71 ? 93 TRP B CH2 1 ATOM 2802 N N . ASP C 3 94 ? 11.407 52.325 31.931 1.00 36.81 ? 94 ASP B N 1 ATOM 2803 C CA . ASP C 3 94 ? 12.108 51.906 33.142 1.00 38.12 ? 94 ASP B CA 1 ATOM 2804 C C . ASP C 3 94 ? 12.038 50.407 33.381 1.00 38.11 ? 94 ASP B C 1 ATOM 2805 O O . ASP C 3 94 ? 12.830 49.868 34.165 1.00 37.60 ? 94 ASP B O 1 ATOM 2806 C CB . ASP C 3 94 ? 11.579 52.650 34.369 1.00 39.53 ? 94 ASP B CB 1 ATOM 2807 C CG . ASP C 3 94 ? 11.946 54.121 34.353 1.00 40.77 ? 94 ASP B CG 1 ATOM 2808 O OD1 . ASP C 3 94 ? 13.075 54.445 33.908 1.00 38.16 ? 94 ASP B OD1 1 ATOM 2809 O OD2 . ASP C 3 94 ? 11.111 54.946 34.791 1.00 40.68 ? 94 ASP B OD2 1 ATOM 2810 N N . ASN C 3 95 ? 11.092 49.738 32.715 1.00 36.77 ? 95 ASN B N 1 ATOM 2811 C CA . ASN C 3 95 ? 10.968 48.291 32.839 1.00 35.09 ? 95 ASN B CA 1 ATOM 2812 C C . ASN C 3 95 ? 11.617 47.567 31.666 1.00 33.31 ? 95 ASN B C 1 ATOM 2813 O O . ASN C 3 95 ? 11.099 46.568 31.175 1.00 32.93 ? 95 ASN B O 1 ATOM 2814 C CB . ASN C 3 95 ? 9.505 47.843 32.985 1.00 36.07 ? 95 ASN B CB 1 ATOM 2815 C CG . ASN C 3 95 ? 8.540 48.635 32.124 1.00 38.10 ? 95 ASN B CG 1 ATOM 2816 O OD1 . ASN C 3 95 ? 8.725 48.786 30.915 1.00 38.25 ? 95 ASN B OD1 1 ATOM 2817 N ND2 . ASN C 3 95 ? 7.484 49.122 32.769 1.00 40.14 ? 95 ASN B ND2 1 ATOM 2818 N N . GLY C 3 96 ? 12.758 48.092 31.229 1.00 32.49 ? 96 GLY B N 1 ATOM 2819 C CA . GLY C 3 96 ? 13.510 47.497 30.139 1.00 32.10 ? 96 GLY B CA 1 ATOM 2820 C C . GLY C 3 96 ? 12.813 47.257 28.812 1.00 31.96 ? 96 GLY B C 1 ATOM 2821 O O . GLY C 3 96 ? 13.306 46.480 28.000 1.00 33.21 ? 96 GLY B O 1 ATOM 2822 N N . THR C 3 97 ? 11.671 47.888 28.571 1.00 31.34 ? 97 THR B N 1 ATOM 2823 C CA . THR C 3 97 ? 11.002 47.695 27.296 1.00 31.45 ? 97 THR B CA 1 ATOM 2824 C C . THR C 3 97 ? 11.369 48.832 26.354 1.00 31.64 ? 97 THR B C 1 ATOM 2825 O O . THR C 3 97 ? 11.428 49.984 26.769 1.00 32.90 ? 97 THR B O 1 ATOM 2826 C CB . THR C 3 97 ? 9.459 47.641 27.452 1.00 30.47 ? 97 THR B CB 1 ATOM 2827 O OG1 . THR C 3 97 ? 9.053 46.303 27.779 1.00 30.59 ? 97 THR B OG1 1 ATOM 2828 C CG2 . THR C 3 97 ? 8.778 48.049 26.164 1.00 28.42 ? 97 THR B CG2 1 ATOM 2829 N N . ILE C 3 98 ? 11.656 48.507 25.098 1.00 31.80 ? 98 ILE B N 1 ATOM 2830 C CA . ILE C 3 98 ? 11.965 49.532 24.103 1.00 30.95 ? 98 ILE B CA 1 ATOM 2831 C C . ILE C 3 98 ? 10.841 49.404 23.090 1.00 31.94 ? 98 ILE B C 1 ATOM 2832 O O . ILE C 3 98 ? 10.783 48.438 22.326 1.00 32.11 ? 98 ILE B O 1 ATOM 2833 C CB . ILE C 3 98 ? 13.327 49.299 23.424 1.00 28.91 ? 98 ILE B CB 1 ATOM 2834 C CG1 . ILE C 3 98 ? 14.445 49.489 24.449 1.00 26.48 ? 98 ILE B CG1 1 ATOM 2835 C CG2 . ILE C 3 98 ? 13.510 50.272 22.263 1.00 27.42 ? 98 ILE B CG2 1 ATOM 2836 C CD1 . ILE C 3 98 ? 15.826 49.423 23.859 1.00 26.03 ? 98 ILE B CD1 1 ATOM 2837 N N . ILE C 3 99 ? 9.944 50.386 23.103 1.00 32.46 ? 99 ILE B N 1 ATOM 2838 C CA . ILE C 3 99 ? 8.775 50.376 22.236 1.00 32.76 ? 99 ILE B CA 1 ATOM 2839 C C . ILE C 3 99 ? 8.795 51.403 21.127 1.00 33.62 ? 99 ILE B C 1 ATOM 2840 O O . ILE C 3 99 ? 9.358 52.485 21.275 1.00 33.53 ? 99 ILE B O 1 ATOM 2841 C CB . ILE C 3 99 ? 7.489 50.607 23.064 1.00 32.54 ? 99 ILE B CB 1 ATOM 2842 C CG1 . ILE C 3 99 ? 6.252 50.265 22.240 1.00 31.96 ? 99 ILE B CG1 1 ATOM 2843 C CG2 . ILE C 3 99 ? 7.406 52.055 23.501 1.00 32.49 ? 99 ILE B CG2 1 ATOM 2844 C CD1 . ILE C 3 99 ? 5.006 50.158 23.076 1.00 32.54 ? 99 ILE B CD1 1 ATOM 2845 N N . ASN C 3 100 ? 8.170 51.043 20.012 1.00 35.32 ? 100 ASN B N 1 ATOM 2846 C CA . ASN C 3 100 ? 8.059 51.925 18.862 1.00 36.97 ? 100 ASN B CA 1 ATOM 2847 C C . ASN C 3 100 ? 6.692 52.585 18.980 1.00 38.64 ? 100 ASN B C 1 ATOM 2848 O O . ASN C 3 100 ? 5.664 51.961 18.715 1.00 38.98 ? 100 ASN B O 1 ATOM 2849 C CB . ASN C 3 100 ? 8.151 51.130 17.554 1.00 36.76 ? 100 ASN B CB 1 ATOM 2850 C CG . ASN C 3 100 ? 7.775 51.960 16.335 1.00 37.85 ? 100 ASN B CG 1 ATOM 2851 O OD1 . ASN C 3 100 ? 8.408 52.974 16.029 1.00 40.40 ? 100 ASN B OD1 1 ATOM 2852 N ND2 . ASN C 3 100 ? 6.737 51.531 15.634 1.00 38.78 ? 100 ASN B ND2 1 ATOM 2853 N N . PRO C 3 101 ? 6.660 53.850 19.419 1.00 40.13 ? 101 PRO B N 1 ATOM 2854 C CA . PRO C 3 101 ? 5.383 54.553 19.557 1.00 40.86 ? 101 PRO B CA 1 ATOM 2855 C C . PRO C 3 101 ? 4.875 54.834 18.147 1.00 43.06 ? 101 PRO B C 1 ATOM 2856 O O . PRO C 3 101 ? 5.486 55.620 17.418 1.00 44.93 ? 101 PRO B O 1 ATOM 2857 C CB . PRO C 3 101 ? 5.780 55.820 20.302 1.00 39.51 ? 101 PRO B CB 1 ATOM 2858 C CG . PRO C 3 101 ? 7.132 56.113 19.729 1.00 39.61 ? 101 PRO B CG 1 ATOM 2859 C CD . PRO C 3 101 ? 7.795 54.748 19.705 1.00 39.32 ? 101 PRO B CD 1 ATOM 2860 N N . ARG C 3 102 ? 3.782 54.184 17.757 1.00 44.36 ? 102 ARG B N 1 ATOM 2861 C CA . ARG C 3 102 ? 3.231 54.355 16.413 1.00 45.04 ? 102 ARG B CA 1 ATOM 2862 C C . ARG C 3 102 ? 2.655 53.011 15.996 1.00 44.93 ? 102 ARG B C 1 ATOM 2863 O O . ARG C 3 102 ? 1.677 52.939 15.251 1.00 46.49 ? 102 ARG B O 1 ATOM 2864 C CB . ARG C 3 102 ? 4.335 54.740 15.422 1.00 46.38 ? 102 ARG B CB 1 ATOM 2865 C CG . ARG C 3 102 ? 3.875 55.517 14.212 1.00 50.41 ? 102 ARG B CG 1 ATOM 2866 C CD . ARG C 3 102 ? 2.835 54.764 13.410 1.00 54.18 ? 102 ARG B CD 1 ATOM 2867 N NE . ARG C 3 102 ? 2.657 55.352 12.087 1.00 56.85 ? 102 ARG B NE 1 ATOM 2868 C CZ . ARG C 3 102 ? 1.806 54.896 11.173 1.00 57.27 ? 102 ARG B CZ 1 ATOM 2869 N NH1 . ARG C 3 102 ? 1.042 53.840 11.438 1.00 56.12 ? 102 ARG B NH1 1 ATOM 2870 N NH2 . ARG C 3 102 ? 1.735 55.488 9.987 1.00 58.17 ? 102 ARG B NH2 1 ATOM 2871 N N . SER C 3 103 ? 3.293 51.945 16.467 1.00 43.81 ? 103 SER B N 1 ATOM 2872 C CA . SER C 3 103 ? 2.855 50.592 16.166 1.00 41.99 ? 103 SER B CA 1 ATOM 2873 C C . SER C 3 103 ? 2.658 49.814 17.469 1.00 42.32 ? 103 SER B C 1 ATOM 2874 O O . SER C 3 103 ? 1.983 48.782 17.486 1.00 43.77 ? 103 SER B O 1 ATOM 2875 C CB . SER C 3 103 ? 3.887 49.890 15.290 1.00 40.63 ? 103 SER B CB 1 ATOM 2876 O OG . SER C 3 103 ? 5.082 49.690 16.010 1.00 38.81 ? 103 SER B OG 1 ATOM 2877 N N . SER C 3 104 ? 3.248 50.320 18.555 1.00 41.54 ? 104 SER B N 1 ATOM 2878 C CA . SER C 3 104 ? 3.147 49.695 19.879 1.00 39.64 ? 104 SER B CA 1 ATOM 2879 C C . SER C 3 104 ? 3.858 48.354 19.912 1.00 37.62 ? 104 SER B C 1 ATOM 2880 O O . SER C 3 104 ? 3.659 47.550 20.825 1.00 36.52 ? 104 SER B O 1 ATOM 2881 C CB . SER C 3 104 ? 1.683 49.482 20.265 1.00 40.51 ? 104 SER B CB 1 ATOM 2882 O OG . SER C 3 104 ? 0.941 50.683 20.187 1.00 42.94 ? 104 SER B OG 1 ATOM 2883 N N . LEU C 3 105 ? 4.668 48.107 18.893 1.00 35.40 ? 105 LEU B N 1 ATOM 2884 C CA . LEU C 3 105 ? 5.399 46.864 18.822 1.00 34.70 ? 105 LEU B CA 1 ATOM 2885 C C . LEU C 3 105 ? 6.743 47.098 19.490 1.00 35.24 ? 105 LEU B C 1 ATOM 2886 O O . LEU C 3 105 ? 7.411 48.093 19.231 1.00 35.13 ? 105 LEU B O 1 ATOM 2887 C CB . LEU C 3 105 ? 5.555 46.439 17.363 1.00 33.16 ? 105 LEU B CB 1 ATOM 2888 C CG . LEU C 3 105 ? 4.199 46.290 16.665 1.00 31.82 ? 105 LEU B CG 1 ATOM 2889 C CD1 . LEU C 3 105 ? 4.395 45.906 15.219 1.00 30.78 ? 105 LEU B CD1 1 ATOM 2890 C CD2 . LEU C 3 105 ? 3.369 45.245 17.389 1.00 31.72 ? 105 LEU B CD2 1 ATOM 2891 N N . VAL C 3 106 ? 7.118 46.180 20.370 1.00 35.49 ? 106 VAL B N 1 ATOM 2892 C CA . VAL C 3 106 ? 8.357 46.274 21.118 1.00 36.31 ? 106 VAL B CA 1 ATOM 2893 C C . VAL C 3 106 ? 9.535 45.615 20.412 1.00 35.61 ? 106 VAL B C 1 ATOM 2894 O O . VAL C 3 106 ? 9.367 44.629 19.701 1.00 36.99 ? 106 VAL B O 1 ATOM 2895 C CB . VAL C 3 106 ? 8.179 45.607 22.495 1.00 37.22 ? 106 VAL B CB 1 ATOM 2896 C CG1 . VAL C 3 106 ? 9.456 45.775 23.342 1.00 41.65 ? 106 VAL B CG1 1 ATOM 2897 C CG2 . VAL C 3 106 ? 6.971 46.210 23.198 1.00 36.39 ? 106 VAL B CG2 1 ATOM 2898 N N . LEU C 3 107 ? 10.728 46.170 20.597 1.00 34.85 ? 107 LEU B N 1 ATOM 2899 C CA . LEU C 3 107 ? 11.923 45.581 20.007 1.00 33.29 ? 107 LEU B CA 1 ATOM 2900 C C . LEU C 3 107 ? 12.081 44.226 20.712 1.00 32.42 ? 107 LEU B C 1 ATOM 2901 O O . LEU C 3 107 ? 12.024 44.144 21.947 1.00 32.30 ? 107 LEU B O 1 ATOM 2902 C CB . LEU C 3 107 ? 13.142 46.462 20.289 1.00 32.45 ? 107 LEU B CB 1 ATOM 2903 C CG . LEU C 3 107 ? 14.474 46.031 19.670 1.00 32.48 ? 107 LEU B CG 1 ATOM 2904 C CD1 . LEU C 3 107 ? 14.479 46.331 18.183 1.00 31.24 ? 107 LEU B CD1 1 ATOM 2905 C CD2 . LEU C 3 107 ? 15.606 46.771 20.353 1.00 30.85 ? 107 LEU B CD2 1 ATOM 2906 N N . ALA C 3 108 ? 12.265 43.165 19.930 1.00 30.61 ? 108 ALA B N 1 ATOM 2907 C CA . ALA C 3 108 ? 12.407 41.826 20.487 1.00 28.80 ? 108 ALA B CA 1 ATOM 2908 C C . ALA C 3 108 ? 13.490 41.033 19.787 1.00 28.77 ? 108 ALA B C 1 ATOM 2909 O O . ALA C 3 108 ? 14.042 41.464 18.782 1.00 29.93 ? 108 ALA B O 1 ATOM 2910 C CB . ALA C 3 108 ? 11.090 41.084 20.384 1.00 26.87 ? 108 ALA B CB 1 ATOM 2911 N N . ALA C 3 109 ? 13.799 39.872 20.346 1.00 29.67 ? 109 ALA B N 1 ATOM 2912 C CA . ALA C 3 109 ? 14.795 38.955 19.794 1.00 30.28 ? 109 ALA B CA 1 ATOM 2913 C C . ALA C 3 109 ? 14.192 37.575 20.039 1.00 30.87 ? 109 ALA B C 1 ATOM 2914 O O . ALA C 3 109 ? 14.374 36.990 21.109 1.00 30.62 ? 109 ALA B O 1 ATOM 2915 C CB . ALA C 3 109 ? 16.129 39.098 20.531 1.00 29.54 ? 109 ALA B CB 1 ATOM 2916 N N . THR C 3 110 ? 13.457 37.076 19.046 1.00 30.77 ? 110 THR B N 1 ATOM 2917 C CA . THR C 3 110 ? 12.770 35.788 19.138 1.00 30.06 ? 110 THR B CA 1 ATOM 2918 C C . THR C 3 110 ? 13.646 34.540 19.052 1.00 30.90 ? 110 THR B C 1 ATOM 2919 O O . THR C 3 110 ? 13.242 33.518 18.509 1.00 29.35 ? 110 THR B O 1 ATOM 2920 C CB . THR C 3 110 ? 11.676 35.709 18.072 1.00 29.49 ? 110 THR B CB 1 ATOM 2921 O OG1 . THR C 3 110 ? 12.243 35.969 16.784 1.00 30.15 ? 110 THR B OG1 1 ATOM 2922 C CG2 . THR C 3 110 ? 10.606 36.748 18.352 1.00 28.55 ? 110 THR B CG2 1 ATOM 2923 N N . SER C 3 111 ? 14.845 34.638 19.608 1.00 32.59 ? 111 SER B N 1 ATOM 2924 C CA . SER C 3 111 ? 15.802 33.542 19.633 1.00 35.59 ? 111 SER B CA 1 ATOM 2925 C C . SER C 3 111 ? 16.991 34.023 20.453 1.00 36.63 ? 111 SER B C 1 ATOM 2926 O O . SER C 3 111 ? 17.457 35.147 20.279 1.00 36.58 ? 111 SER B O 1 ATOM 2927 C CB . SER C 3 111 ? 16.257 33.190 18.222 1.00 36.18 ? 111 SER B CB 1 ATOM 2928 O OG . SER C 3 111 ? 17.127 32.071 18.256 1.00 40.61 ? 111 SER B OG 1 ATOM 2929 N N . GLY C 3 112 ? 17.475 33.179 21.355 1.00 37.08 ? 112 GLY B N 1 ATOM 2930 C CA . GLY C 3 112 ? 18.593 33.576 22.191 1.00 38.92 ? 112 GLY B CA 1 ATOM 2931 C C . GLY C 3 112 ? 19.937 33.276 21.568 1.00 39.97 ? 112 GLY B C 1 ATOM 2932 O O . GLY C 3 112 ? 20.979 33.447 22.197 1.00 40.44 ? 112 GLY B O 1 ATOM 2933 N N . ASN C 3 113 ? 19.901 32.826 20.319 1.00 39.78 ? 113 ASN B N 1 ATOM 2934 C CA . ASN C 3 113 ? 21.099 32.484 19.573 1.00 38.56 ? 113 ASN B CA 1 ATOM 2935 C C . ASN C 3 113 ? 21.860 33.705 19.098 1.00 37.03 ? 113 ASN B C 1 ATOM 2936 O O . ASN C 3 113 ? 21.273 34.718 18.729 1.00 35.77 ? 113 ASN B O 1 ATOM 2937 C CB . ASN C 3 113 ? 20.728 31.641 18.357 1.00 40.43 ? 113 ASN B CB 1 ATOM 2938 C CG . ASN C 3 113 ? 20.123 30.317 18.735 1.00 42.91 ? 113 ASN B CG 1 ATOM 2939 O OD1 . ASN C 3 113 ? 20.672 29.588 19.564 1.00 45.57 ? 113 ASN B OD1 1 ATOM 2940 N ND2 . ASN C 3 113 ? 18.986 29.990 18.129 1.00 43.34 ? 113 ASN B ND2 1 ATOM 2941 N N . SER C 3 114 ? 23.177 33.595 19.105 1.00 35.23 ? 114 SER B N 1 ATOM 2942 C CA . SER C 3 114 ? 24.022 34.674 18.644 1.00 35.30 ? 114 SER B CA 1 ATOM 2943 C C . SER C 3 114 ? 23.794 34.835 17.143 1.00 34.15 ? 114 SER B C 1 ATOM 2944 O O . SER C 3 114 ? 23.832 33.854 16.399 1.00 34.07 ? 114 SER B O 1 ATOM 2945 C CB . SER C 3 114 ? 25.484 34.334 18.916 1.00 35.23 ? 114 SER B CB 1 ATOM 2946 O OG . SER C 3 114 ? 26.332 35.366 18.461 1.00 38.28 ? 114 SER B OG 1 ATOM 2947 N N . GLY C 3 115 ? 23.541 36.065 16.706 1.00 33.59 ? 115 GLY B N 1 ATOM 2948 C CA . GLY C 3 115 ? 23.317 36.324 15.294 1.00 31.90 ? 115 GLY B CA 1 ATOM 2949 C C . GLY C 3 115 ? 21.859 36.489 14.912 1.00 31.56 ? 115 GLY B C 1 ATOM 2950 O O . GLY C 3 115 ? 21.558 36.842 13.778 1.00 31.82 ? 115 GLY B O 1 ATOM 2951 N N . THR C 3 116 ? 20.950 36.236 15.847 1.00 31.02 ? 116 THR B N 1 ATOM 2952 C CA . THR C 3 116 ? 19.513 36.362 15.583 1.00 30.94 ? 116 THR B CA 1 ATOM 2953 C C . THR C 3 116 ? 19.094 37.780 15.211 1.00 31.20 ? 116 THR B C 1 ATOM 2954 O O . THR C 3 116 ? 19.441 38.738 15.901 1.00 31.87 ? 116 THR B O 1 ATOM 2955 C CB . THR C 3 116 ? 18.686 35.934 16.810 1.00 30.25 ? 116 THR B CB 1 ATOM 2956 O OG1 . THR C 3 116 ? 18.852 34.526 17.022 1.00 31.36 ? 116 THR B OG1 1 ATOM 2957 C CG2 . THR C 3 116 ? 17.208 36.241 16.595 1.00 28.76 ? 116 THR B CG2 1 ATOM 2958 N N . THR C 3 117 ? 18.332 37.911 14.130 1.00 30.40 ? 117 THR B N 1 ATOM 2959 C CA . THR C 3 117 ? 17.876 39.228 13.685 1.00 30.55 ? 117 THR B CA 1 ATOM 2960 C C . THR C 3 117 ? 16.790 39.832 14.579 1.00 30.58 ? 117 THR B C 1 ATOM 2961 O O . THR C 3 117 ? 15.791 39.179 14.892 1.00 32.44 ? 117 THR B O 1 ATOM 2962 C CB . THR C 3 117 ? 17.331 39.174 12.246 1.00 30.71 ? 117 THR B CB 1 ATOM 2963 O OG1 . THR C 3 117 ? 18.398 38.868 11.335 1.00 29.86 ? 117 THR B OG1 1 ATOM 2964 C CG2 . THR C 3 117 ? 16.710 40.516 11.871 1.00 31.06 ? 117 THR B CG2 1 ATOM 2965 N N . LEU C 3 118 ? 16.986 41.082 14.986 1.00 30.11 ? 118 LEU B N 1 ATOM 2966 C CA . LEU C 3 118 ? 16.006 41.759 15.826 1.00 29.32 ? 118 LEU B CA 1 ATOM 2967 C C . LEU C 3 118 ? 14.729 41.990 15.037 1.00 29.40 ? 118 LEU B C 1 ATOM 2968 O O . LEU C 3 118 ? 14.753 42.139 13.821 1.00 29.47 ? 118 LEU B O 1 ATOM 2969 C CB . LEU C 3 118 ? 16.562 43.093 16.339 1.00 28.69 ? 118 LEU B CB 1 ATOM 2970 C CG . LEU C 3 118 ? 17.380 43.052 17.634 1.00 28.37 ? 118 LEU B CG 1 ATOM 2971 C CD1 . LEU C 3 118 ? 18.427 41.960 17.575 1.00 28.22 ? 118 LEU B CD1 1 ATOM 2972 C CD2 . LEU C 3 118 ? 18.031 44.398 17.852 1.00 28.33 ? 118 LEU B CD2 1 ATOM 2973 N N . THR C 3 119 ? 13.612 42.017 15.743 1.00 29.92 ? 119 THR B N 1 ATOM 2974 C CA . THR C 3 119 ? 12.316 42.201 15.122 1.00 31.57 ? 119 THR B CA 1 ATOM 2975 C C . THR C 3 119 ? 11.448 43.044 16.059 1.00 32.70 ? 119 THR B C 1 ATOM 2976 O O . THR C 3 119 ? 11.928 43.504 17.098 1.00 35.02 ? 119 THR B O 1 ATOM 2977 C CB . THR C 3 119 ? 11.636 40.836 14.913 1.00 31.37 ? 119 THR B CB 1 ATOM 2978 O OG1 . THR C 3 119 ? 11.395 40.221 16.188 1.00 29.78 ? 119 THR B OG1 1 ATOM 2979 C CG2 . THR C 3 119 ? 12.527 39.919 14.096 1.00 29.91 ? 119 THR B CG2 1 ATOM 2980 N N . VAL C 3 120 ? 10.185 43.259 15.685 1.00 32.42 ? 120 VAL B N 1 ATOM 2981 C CA . VAL C 3 120 ? 9.243 44.013 16.518 1.00 31.26 ? 120 VAL B CA 1 ATOM 2982 C C . VAL C 3 120 ? 8.027 43.117 16.748 1.00 32.07 ? 120 VAL B C 1 ATOM 2983 O O . VAL C 3 120 ? 7.290 42.799 15.814 1.00 32.90 ? 120 VAL B O 1 ATOM 2984 C CB . VAL C 3 120 ? 8.791 45.352 15.862 1.00 28.02 ? 120 VAL B CB 1 ATOM 2985 C CG1 . VAL C 3 120 ? 9.961 46.318 15.779 1.00 24.81 ? 120 VAL B CG1 1 ATOM 2986 C CG2 . VAL C 3 120 ? 8.223 45.098 14.495 1.00 25.40 ? 120 VAL B CG2 1 ATOM 2987 N N . GLN C 3 121 ? 7.837 42.695 17.996 1.00 32.81 ? 121 GLN B N 1 ATOM 2988 C CA . GLN C 3 121 ? 6.731 41.814 18.358 1.00 34.30 ? 121 GLN B CA 1 ATOM 2989 C C . GLN C 3 121 ? 5.651 42.535 19.158 1.00 34.69 ? 121 GLN B C 1 ATOM 2990 O O . GLN C 3 121 ? 5.804 43.694 19.533 1.00 33.53 ? 121 GLN B O 1 ATOM 2991 C CB . GLN C 3 121 ? 7.253 40.629 19.185 1.00 34.27 ? 121 GLN B CB 1 ATOM 2992 C CG . GLN C 3 121 ? 8.359 39.811 18.527 1.00 35.28 ? 121 GLN B CG 1 ATOM 2993 C CD . GLN C 3 121 ? 7.992 39.322 17.130 1.00 35.93 ? 121 GLN B CD 1 ATOM 2994 O OE1 . GLN C 3 121 ? 6.951 38.694 16.928 1.00 35.14 ? 121 GLN B OE1 1 ATOM 2995 N NE2 . GLN C 3 121 ? 8.856 39.605 16.161 1.00 35.03 ? 121 GLN B NE2 1 ATOM 2996 N N . THR C 3 122 ? 4.546 41.840 19.406 1.00 36.64 ? 122 THR B N 1 ATOM 2997 C CA . THR C 3 122 ? 3.470 42.416 20.198 1.00 37.77 ? 122 THR B CA 1 ATOM 2998 C C . THR C 3 122 ? 3.957 42.317 21.641 1.00 37.92 ? 122 THR B C 1 ATOM 2999 O O . THR C 3 122 ? 4.457 41.271 22.071 1.00 38.08 ? 122 THR B O 1 ATOM 3000 C CB . THR C 3 122 ? 2.156 41.628 20.027 1.00 37.49 ? 122 THR B CB 1 ATOM 3001 O OG1 . THR C 3 122 ? 1.801 41.595 18.643 1.00 39.11 ? 122 THR B OG1 1 ATOM 3002 C CG2 . THR C 3 122 ? 1.030 42.291 20.802 1.00 37.43 ? 122 THR B CG2 1 ATOM 3003 N N . ASN C 3 123 ? 3.822 43.409 22.382 1.00 36.68 ? 123 ASN B N 1 ATOM 3004 C CA . ASN C 3 123 ? 4.283 43.459 23.765 1.00 35.77 ? 123 ASN B CA 1 ATOM 3005 C C . ASN C 3 123 ? 3.618 42.474 24.737 1.00 33.45 ? 123 ASN B C 1 ATOM 3006 O O . ASN C 3 123 ? 2.400 42.489 24.920 1.00 32.39 ? 123 ASN B O 1 ATOM 3007 C CB . ASN C 3 123 ? 4.120 44.892 24.294 1.00 38.33 ? 123 ASN B CB 1 ATOM 3008 C CG . ASN C 3 123 ? 4.977 45.174 25.521 1.00 39.92 ? 123 ASN B CG 1 ATOM 3009 O OD1 . ASN C 3 123 ? 5.605 44.276 26.086 1.00 41.53 ? 123 ASN B OD1 1 ATOM 3010 N ND2 . ASN C 3 123 ? 5.001 46.435 25.939 1.00 40.31 ? 123 ASN B ND2 1 ATOM 3011 N N . ILE C 3 124 ? 4.427 41.612 25.351 1.00 31.62 ? 124 ILE B N 1 ATOM 3012 C CA . ILE C 3 124 ? 3.938 40.657 26.349 1.00 29.31 ? 124 ILE B CA 1 ATOM 3013 C C . ILE C 3 124 ? 4.968 40.571 27.487 1.00 29.12 ? 124 ILE B C 1 ATOM 3014 O O . ILE C 3 124 ? 5.030 39.575 28.209 1.00 29.61 ? 124 ILE B O 1 ATOM 3015 C CB . ILE C 3 124 ? 3.702 39.211 25.779 1.00 26.86 ? 124 ILE B CB 1 ATOM 3016 C CG1 . ILE C 3 124 ? 5.032 38.567 25.376 1.00 25.51 ? 124 ILE B CG1 1 ATOM 3017 C CG2 . ILE C 3 124 ? 2.732 39.253 24.617 1.00 26.04 ? 124 ILE B CG2 1 ATOM 3018 C CD1 . ILE C 3 124 ? 4.931 37.094 25.093 1.00 21.54 ? 124 ILE B CD1 1 ATOM 3019 N N . TYR C 3 125 ? 5.777 41.618 27.632 1.00 28.23 ? 125 TYR B N 1 ATOM 3020 C CA . TYR C 3 125 ? 6.793 41.672 28.680 1.00 27.86 ? 125 TYR B CA 1 ATOM 3021 C C . TYR C 3 125 ? 7.496 40.344 28.898 1.00 27.95 ? 125 TYR B C 1 ATOM 3022 O O . TYR C 3 125 ? 7.484 39.805 30.003 1.00 28.15 ? 125 TYR B O 1 ATOM 3023 C CB . TYR C 3 125 ? 6.161 42.120 29.990 1.00 27.73 ? 125 TYR B CB 1 ATOM 3024 C CG . TYR C 3 125 ? 5.602 43.507 29.909 1.00 27.93 ? 125 TYR B CG 1 ATOM 3025 C CD1 . TYR C 3 125 ? 6.440 44.620 29.930 1.00 29.17 ? 125 TYR B CD1 1 ATOM 3026 C CD2 . TYR C 3 125 ? 4.240 43.711 29.750 1.00 27.39 ? 125 TYR B CD2 1 ATOM 3027 C CE1 . TYR C 3 125 ? 5.929 45.904 29.792 1.00 29.50 ? 125 TYR B CE1 1 ATOM 3028 C CE2 . TYR C 3 125 ? 3.722 44.984 29.610 1.00 29.60 ? 125 TYR B CE2 1 ATOM 3029 C CZ . TYR C 3 125 ? 4.566 46.076 29.631 1.00 29.38 ? 125 TYR B CZ 1 ATOM 3030 O OH . TYR C 3 125 ? 4.035 47.333 29.486 1.00 31.56 ? 125 TYR B OH 1 ATOM 3031 N N . ALA C 3 126 ? 8.102 39.818 27.839 1.00 26.46 ? 126 ALA B N 1 ATOM 3032 C CA . ALA C 3 126 ? 8.810 38.552 27.913 1.00 24.94 ? 126 ALA B CA 1 ATOM 3033 C C . ALA C 3 126 ? 10.282 38.858 28.045 1.00 24.80 ? 126 ALA B C 1 ATOM 3034 O O . ALA C 3 126 ? 10.698 39.994 27.841 1.00 25.60 ? 126 ALA B O 1 ATOM 3035 C CB . ALA C 3 126 ? 8.559 37.742 26.655 1.00 25.31 ? 126 ALA B CB 1 ATOM 3036 N N . VAL C 3 127 ? 11.069 37.849 28.399 1.00 24.09 ? 127 VAL B N 1 ATOM 3037 C CA . VAL C 3 127 ? 12.506 38.032 28.533 1.00 24.76 ? 127 VAL B CA 1 ATOM 3038 C C . VAL C 3 127 ? 13.068 38.361 27.146 1.00 25.84 ? 127 VAL B C 1 ATOM 3039 O O . VAL C 3 127 ? 14.113 38.993 27.010 1.00 27.25 ? 127 VAL B O 1 ATOM 3040 C CB . VAL C 3 127 ? 13.186 36.755 29.088 1.00 23.59 ? 127 VAL B CB 1 ATOM 3041 C CG1 . VAL C 3 127 ? 14.705 36.867 28.968 1.00 21.47 ? 127 VAL B CG1 1 ATOM 3042 C CG2 . VAL C 3 127 ? 12.796 36.554 30.542 1.00 22.44 ? 127 VAL B CG2 1 ATOM 3043 N N . SER C 3 128 ? 12.351 37.944 26.113 1.00 25.94 ? 128 SER B N 1 ATOM 3044 C CA . SER C 3 128 ? 12.785 38.192 24.750 1.00 26.64 ? 128 SER B CA 1 ATOM 3045 C C . SER C 3 128 ? 12.498 39.616 24.296 1.00 27.52 ? 128 SER B C 1 ATOM 3046 O O . SER C 3 128 ? 12.678 39.940 23.129 1.00 28.66 ? 128 SER B O 1 ATOM 3047 C CB . SER C 3 128 ? 12.109 37.199 23.803 1.00 26.27 ? 128 SER B CB 1 ATOM 3048 O OG . SER C 3 128 ? 10.710 37.136 24.021 1.00 24.03 ? 128 SER B OG 1 ATOM 3049 N N . GLN C 3 129 ? 12.069 40.474 25.212 1.00 28.41 ? 129 GLN B N 1 ATOM 3050 C CA . GLN C 3 129 ? 11.754 41.851 24.846 1.00 29.79 ? 129 GLN B CA 1 ATOM 3051 C C . GLN C 3 129 ? 12.298 42.855 25.869 1.00 30.99 ? 129 GLN B C 1 ATOM 3052 O O . GLN C 3 129 ? 12.009 44.058 25.794 1.00 33.06 ? 129 GLN B O 1 ATOM 3053 C CB . GLN C 3 129 ? 10.234 42.016 24.700 1.00 27.90 ? 129 GLN B CB 1 ATOM 3054 C CG . GLN C 3 129 ? 9.560 40.953 23.839 1.00 25.25 ? 129 GLN B CG 1 ATOM 3055 C CD . GLN C 3 129 ? 8.053 41.095 23.829 1.00 24.64 ? 129 GLN B CD 1 ATOM 3056 O OE1 . GLN C 3 129 ? 7.425 41.167 24.876 1.00 26.04 ? 129 GLN B OE1 1 ATOM 3057 N NE2 . GLN C 3 129 ? 7.465 41.126 22.644 1.00 25.34 ? 129 GLN B NE2 1 ATOM 3058 N N . GLY C 3 130 ? 13.085 42.353 26.820 1.00 30.04 ? 130 GLY B N 1 ATOM 3059 C CA . GLY C 3 130 ? 13.672 43.206 27.841 1.00 28.29 ? 130 GLY B CA 1 ATOM 3060 C C . GLY C 3 130 ? 15.068 43.620 27.423 1.00 27.76 ? 130 GLY B C 1 ATOM 3061 O O . GLY C 3 130 ? 15.847 42.783 26.965 1.00 27.39 ? 130 GLY B O 1 ATOM 3062 N N . TRP C 3 131 ? 15.375 44.908 27.573 1.00 26.71 ? 131 TRP B N 1 ATOM 3063 C CA . TRP C 3 131 ? 16.676 45.460 27.207 1.00 24.99 ? 131 TRP B CA 1 ATOM 3064 C C . TRP C 3 131 ? 17.128 46.465 28.236 1.00 24.19 ? 131 TRP B C 1 ATOM 3065 O O . TRP C 3 131 ? 16.335 46.938 29.040 1.00 24.17 ? 131 TRP B O 1 ATOM 3066 C CB . TRP C 3 131 ? 16.612 46.175 25.859 1.00 25.51 ? 131 TRP B CB 1 ATOM 3067 C CG . TRP C 3 131 ? 15.903 45.416 24.821 1.00 27.75 ? 131 TRP B CG 1 ATOM 3068 C CD1 . TRP C 3 131 ? 14.566 45.423 24.571 1.00 28.73 ? 131 TRP B CD1 1 ATOM 3069 C CD2 . TRP C 3 131 ? 16.479 44.482 23.914 1.00 28.96 ? 131 TRP B CD2 1 ATOM 3070 N NE1 . TRP C 3 131 ? 14.270 44.544 23.560 1.00 30.48 ? 131 TRP B NE1 1 ATOM 3071 C CE2 . TRP C 3 131 ? 15.431 43.950 23.141 1.00 30.15 ? 131 TRP B CE2 1 ATOM 3072 C CE3 . TRP C 3 131 ? 17.783 44.037 23.682 1.00 29.55 ? 131 TRP B CE3 1 ATOM 3073 C CZ2 . TRP C 3 131 ? 15.645 42.997 22.151 1.00 31.61 ? 131 TRP B CZ2 1 ATOM 3074 C CZ3 . TRP C 3 131 ? 17.997 43.089 22.698 1.00 30.74 ? 131 TRP B CZ3 1 ATOM 3075 C CH2 . TRP C 3 131 ? 16.934 42.578 21.945 1.00 32.52 ? 131 TRP B CH2 1 ATOM 3076 N N . LEU C 3 132 ? 18.406 46.819 28.178 1.00 24.06 ? 132 LEU B N 1 ATOM 3077 C CA . LEU C 3 132 ? 18.983 47.770 29.114 1.00 25.27 ? 132 LEU B CA 1 ATOM 3078 C C . LEU C 3 132 ? 20.167 48.539 28.526 1.00 25.65 ? 132 LEU B C 1 ATOM 3079 O O . LEU C 3 132 ? 21.102 47.937 28.008 1.00 25.76 ? 132 LEU B O 1 ATOM 3080 C CB . LEU C 3 132 ? 19.423 47.010 30.362 1.00 25.85 ? 132 LEU B CB 1 ATOM 3081 C CG . LEU C 3 132 ? 20.411 47.617 31.356 1.00 27.84 ? 132 LEU B CG 1 ATOM 3082 C CD1 . LEU C 3 132 ? 19.825 48.847 32.026 1.00 28.74 ? 132 LEU B CD1 1 ATOM 3083 C CD2 . LEU C 3 132 ? 20.749 46.555 32.388 1.00 26.60 ? 132 LEU B CD2 1 ATOM 3084 N N . PRO C 3 133 ? 20.120 49.886 28.572 1.00 27.17 ? 133 PRO B N 1 ATOM 3085 C CA . PRO C 3 133 ? 21.199 50.735 28.054 1.00 28.72 ? 133 PRO B CA 1 ATOM 3086 C C . PRO C 3 133 ? 22.284 50.784 29.126 1.00 29.32 ? 133 PRO B C 1 ATOM 3087 O O . PRO C 3 133 ? 22.069 51.325 30.208 1.00 29.45 ? 133 PRO B O 1 ATOM 3088 C CB . PRO C 3 133 ? 20.527 52.099 27.885 1.00 28.37 ? 133 PRO B CB 1 ATOM 3089 C CG . PRO C 3 133 ? 19.070 51.778 27.788 1.00 26.62 ? 133 PRO B CG 1 ATOM 3090 C CD . PRO C 3 133 ? 18.920 50.702 28.821 1.00 28.25 ? 133 PRO B CD 1 ATOM 3091 N N . THR C 3 134 ? 23.439 50.205 28.830 1.00 30.15 ? 134 THR B N 1 ATOM 3092 C CA . THR C 3 134 ? 24.534 50.174 29.783 1.00 31.11 ? 134 THR B CA 1 ATOM 3093 C C . THR C 3 134 ? 25.815 49.730 29.085 1.00 32.82 ? 134 THR B C 1 ATOM 3094 O O . THR C 3 134 ? 25.763 49.020 28.086 1.00 33.68 ? 134 THR B O 1 ATOM 3095 C CB . THR C 3 134 ? 24.216 49.200 30.940 1.00 30.66 ? 134 THR B CB 1 ATOM 3096 O OG1 . THR C 3 134 ? 25.315 49.177 31.856 1.00 32.12 ? 134 THR B OG1 1 ATOM 3097 C CG2 . THR C 3 134 ? 23.971 47.789 30.419 1.00 27.20 ? 134 THR B CG2 1 ATOM 3098 N N . ASN C 3 135 ? 26.960 50.182 29.588 1.00 34.21 ? 135 ASN B N 1 ATOM 3099 C CA . ASN C 3 135 ? 28.247 49.785 29.030 1.00 35.26 ? 135 ASN B CA 1 ATOM 3100 C C . ASN C 3 135 ? 28.661 48.566 29.824 1.00 35.64 ? 135 ASN B C 1 ATOM 3101 O O . ASN C 3 135 ? 29.697 47.956 29.568 1.00 35.75 ? 135 ASN B O 1 ATOM 3102 C CB . ASN C 3 135 ? 29.281 50.887 29.210 1.00 37.27 ? 135 ASN B CB 1 ATOM 3103 C CG . ASN C 3 135 ? 29.220 51.916 28.110 1.00 41.38 ? 135 ASN B CG 1 ATOM 3104 O OD1 . ASN C 3 135 ? 28.162 52.142 27.532 1.00 44.47 ? 135 ASN B OD1 1 ATOM 3105 N ND2 . ASN C 3 135 ? 30.352 52.552 27.824 1.00 41.88 ? 135 ASN B ND2 1 ATOM 3106 N N . ASN C 3 136 ? 27.830 48.234 30.806 1.00 36.11 ? 136 ASN B N 1 ATOM 3107 C CA . ASN C 3 136 ? 28.058 47.087 31.661 1.00 36.84 ? 136 ASN B CA 1 ATOM 3108 C C . ASN C 3 136 ? 27.552 45.859 30.916 1.00 38.55 ? 136 ASN B C 1 ATOM 3109 O O . ASN C 3 136 ? 26.356 45.710 30.674 1.00 39.71 ? 136 ASN B O 1 ATOM 3110 C CB . ASN C 3 136 ? 27.311 47.268 32.977 1.00 36.34 ? 136 ASN B CB 1 ATOM 3111 C CG . ASN C 3 136 ? 28.212 47.132 34.182 1.00 35.34 ? 136 ASN B CG 1 ATOM 3112 O OD1 . ASN C 3 136 ? 29.424 47.307 34.083 1.00 35.72 ? 136 ASN B OD1 1 ATOM 3113 N ND2 . ASN C 3 136 ? 27.618 46.833 35.337 1.00 33.58 ? 136 ASN B ND2 1 ATOM 3114 N N . THR C 3 137 ? 28.481 44.989 30.545 1.00 40.00 ? 137 THR B N 1 ATOM 3115 C CA . THR C 3 137 ? 28.170 43.775 29.809 1.00 41.69 ? 137 THR B CA 1 ATOM 3116 C C . THR C 3 137 ? 27.888 42.575 30.715 1.00 42.95 ? 137 THR B C 1 ATOM 3117 O O . THR C 3 137 ? 27.373 41.545 30.258 1.00 43.91 ? 137 THR B O 1 ATOM 3118 C CB . THR C 3 137 ? 29.330 43.445 28.848 1.00 40.57 ? 137 THR B CB 1 ATOM 3119 O OG1 . THR C 3 137 ? 29.211 44.264 27.679 1.00 40.18 ? 137 THR B OG1 1 ATOM 3120 C CG2 . THR C 3 137 ? 29.327 41.970 28.456 1.00 42.25 ? 137 THR B CG2 1 ATOM 3121 N N . GLN C 3 138 ? 28.209 42.711 31.997 1.00 43.34 ? 138 GLN B N 1 ATOM 3122 C CA . GLN C 3 138 ? 27.998 41.623 32.945 1.00 43.52 ? 138 GLN B CA 1 ATOM 3123 C C . GLN C 3 138 ? 26.739 41.769 33.793 1.00 42.47 ? 138 GLN B C 1 ATOM 3124 O O . GLN C 3 138 ? 26.378 42.873 34.202 1.00 42.71 ? 138 GLN B O 1 ATOM 3125 C CB . GLN C 3 138 ? 29.218 41.493 33.862 1.00 45.47 ? 138 GLN B CB 1 ATOM 3126 C CG . GLN C 3 138 ? 30.467 41.034 33.139 1.00 48.63 ? 138 GLN B CG 1 ATOM 3127 C CD . GLN C 3 138 ? 30.221 39.769 32.337 1.00 51.58 ? 138 GLN B CD 1 ATOM 3128 O OE1 . GLN C 3 138 ? 30.071 38.672 32.893 1.00 51.90 ? 138 GLN B OE1 1 ATOM 3129 N NE2 . GLN C 3 138 ? 30.159 39.919 31.016 1.00 53.65 ? 138 GLN B NE2 1 ATOM 3130 N N . PRO C 3 139 ? 26.049 40.649 34.065 1.00 41.03 ? 139 PRO B N 1 ATOM 3131 C CA . PRO C 3 139 ? 24.834 40.707 34.876 1.00 40.97 ? 139 PRO B CA 1 ATOM 3132 C C . PRO C 3 139 ? 25.217 40.995 36.315 1.00 40.68 ? 139 PRO B C 1 ATOM 3133 O O . PRO C 3 139 ? 26.303 40.618 36.755 1.00 40.78 ? 139 PRO B O 1 ATOM 3134 C CB . PRO C 3 139 ? 24.230 39.321 34.688 1.00 40.78 ? 139 PRO B CB 1 ATOM 3135 C CG . PRO C 3 139 ? 25.422 38.465 34.558 1.00 41.04 ? 139 PRO B CG 1 ATOM 3136 C CD . PRO C 3 139 ? 26.315 39.268 33.630 1.00 41.24 ? 139 PRO B CD 1 ATOM 3137 N N . PHE C 3 140 ? 24.326 41.668 37.039 1.00 40.49 ? 140 PHE B N 1 ATOM 3138 C CA . PHE C 3 140 ? 24.568 42.039 38.430 1.00 40.51 ? 140 PHE B CA 1 ATOM 3139 C C . PHE C 3 140 ? 24.323 40.879 39.395 1.00 39.47 ? 140 PHE B C 1 ATOM 3140 O O . PHE C 3 140 ? 23.229 40.316 39.430 1.00 40.04 ? 140 PHE B O 1 ATOM 3141 C CB . PHE C 3 140 ? 23.675 43.225 38.803 1.00 42.16 ? 140 PHE B CB 1 ATOM 3142 C CG . PHE C 3 140 ? 24.108 43.939 40.047 1.00 45.34 ? 140 PHE B CG 1 ATOM 3143 C CD1 . PHE C 3 140 ? 25.356 44.562 40.106 1.00 47.24 ? 140 PHE B CD1 1 ATOM 3144 C CD2 . PHE C 3 140 ? 23.278 43.987 41.166 1.00 45.61 ? 140 PHE B CD2 1 ATOM 3145 C CE1 . PHE C 3 140 ? 25.774 45.223 41.263 1.00 47.81 ? 140 PHE B CE1 1 ATOM 3146 C CE2 . PHE C 3 140 ? 23.684 44.647 42.328 1.00 45.88 ? 140 PHE B CE2 1 ATOM 3147 C CZ . PHE C 3 140 ? 24.932 45.265 42.378 1.00 47.44 ? 140 PHE B CZ 1 ATOM 3148 N N . VAL C 3 141 ? 25.337 40.530 40.185 1.00 37.33 ? 141 VAL B N 1 ATOM 3149 C CA . VAL C 3 141 ? 25.208 39.422 41.131 1.00 36.23 ? 141 VAL B CA 1 ATOM 3150 C C . VAL C 3 141 ? 24.972 39.858 42.577 1.00 36.65 ? 141 VAL B C 1 ATOM 3151 O O . VAL C 3 141 ? 25.801 40.556 43.162 1.00 37.31 ? 141 VAL B O 1 ATOM 3152 C CB . VAL C 3 141 ? 26.464 38.529 41.127 1.00 34.70 ? 141 VAL B CB 1 ATOM 3153 C CG1 . VAL C 3 141 ? 26.241 37.339 42.035 1.00 33.28 ? 141 VAL B CG1 1 ATOM 3154 C CG2 . VAL C 3 141 ? 26.785 38.075 39.719 1.00 34.59 ? 141 VAL B CG2 1 ATOM 3155 N N . THR C 3 142 ? 23.846 39.445 43.155 1.00 35.91 ? 142 THR B N 1 ATOM 3156 C CA . THR C 3 142 ? 23.553 39.788 44.544 1.00 34.65 ? 142 THR B CA 1 ATOM 3157 C C . THR C 3 142 ? 22.909 38.675 45.309 1.00 34.24 ? 142 THR B C 1 ATOM 3158 O O . THR C 3 142 ? 22.712 37.564 44.815 1.00 32.78 ? 142 THR B O 1 ATOM 3159 C CB . THR C 3 142 ? 22.582 40.973 44.707 1.00 34.94 ? 142 THR B CB 1 ATOM 3160 O OG1 . THR C 3 142 ? 21.370 40.703 43.994 1.00 34.39 ? 142 THR B OG1 1 ATOM 3161 C CG2 . THR C 3 142 ? 23.205 42.236 44.220 1.00 37.51 ? 142 THR B CG2 1 ATOM 3162 N N . THR C 3 143 ? 22.583 39.028 46.542 1.00 33.07 ? 143 THR B N 1 ATOM 3163 C CA . THR C 3 143 ? 21.917 38.155 47.474 1.00 31.84 ? 143 THR B CA 1 ATOM 3164 C C . THR C 3 143 ? 20.565 38.821 47.575 1.00 31.48 ? 143 THR B C 1 ATOM 3165 O O . THR C 3 143 ? 20.477 40.044 47.564 1.00 32.58 ? 143 THR B O 1 ATOM 3166 C CB . THR C 3 143 ? 22.611 38.197 48.837 1.00 32.59 ? 143 THR B CB 1 ATOM 3167 O OG1 . THR C 3 143 ? 23.862 37.508 48.755 1.00 32.59 ? 143 THR B OG1 1 ATOM 3168 C CG2 . THR C 3 143 ? 21.746 37.558 49.888 1.00 35.03 ? 143 THR B CG2 1 ATOM 3169 N N . ILE C 3 144 ? 19.506 38.036 47.634 1.00 29.83 ? 144 ILE B N 1 ATOM 3170 C CA . ILE C 3 144 ? 18.187 38.624 47.747 1.00 26.89 ? 144 ILE B CA 1 ATOM 3171 C C . ILE C 3 144 ? 17.688 38.232 49.130 1.00 26.87 ? 144 ILE B C 1 ATOM 3172 O O . ILE C 3 144 ? 17.474 37.055 49.408 1.00 27.87 ? 144 ILE B O 1 ATOM 3173 C CB . ILE C 3 144 ? 17.260 38.096 46.631 1.00 26.20 ? 144 ILE B CB 1 ATOM 3174 C CG1 . ILE C 3 144 ? 17.797 38.556 45.269 1.00 26.02 ? 144 ILE B CG1 1 ATOM 3175 C CG2 . ILE C 3 144 ? 15.849 38.597 46.842 1.00 27.74 ? 144 ILE B CG2 1 ATOM 3176 C CD1 . ILE C 3 144 ? 17.032 38.033 44.087 1.00 22.21 ? 144 ILE B CD1 1 ATOM 3177 N N . VAL C 3 145 ? 17.546 39.222 50.006 1.00 24.54 ? 145 VAL B N 1 ATOM 3178 C CA . VAL C 3 145 ? 17.099 38.979 51.364 1.00 22.66 ? 145 VAL B CA 1 ATOM 3179 C C . VAL C 3 145 ? 15.640 39.351 51.478 1.00 23.09 ? 145 VAL B C 1 ATOM 3180 O O . VAL C 3 145 ? 15.220 40.387 50.980 1.00 23.80 ? 145 VAL B O 1 ATOM 3181 C CB . VAL C 3 145 ? 17.912 39.810 52.362 1.00 22.67 ? 145 VAL B CB 1 ATOM 3182 C CG1 . VAL C 3 145 ? 17.835 39.191 53.735 1.00 23.42 ? 145 VAL B CG1 1 ATOM 3183 C CG2 . VAL C 3 145 ? 19.344 39.880 51.919 1.00 25.40 ? 145 VAL B CG2 1 ATOM 3184 N N . GLY C 3 146 ? 14.864 38.501 52.132 1.00 22.88 ? 146 GLY B N 1 ATOM 3185 C CA . GLY C 3 146 ? 13.450 38.773 52.267 1.00 24.94 ? 146 GLY B CA 1 ATOM 3186 C C . GLY C 3 146 ? 12.939 38.480 53.656 1.00 25.89 ? 146 GLY B C 1 ATOM 3187 O O . GLY C 3 146 ? 13.683 38.616 54.617 1.00 26.28 ? 146 GLY B O 1 ATOM 3188 N N . LEU C 3 147 ? 11.675 38.070 53.748 1.00 26.47 ? 147 LEU B N 1 ATOM 3189 C CA . LEU C 3 147 ? 11.016 37.760 55.018 1.00 27.50 ? 147 LEU B CA 1 ATOM 3190 C C . LEU C 3 147 ? 11.908 37.154 56.093 1.00 27.76 ? 147 LEU B C 1 ATOM 3191 O O . LEU C 3 147 ? 12.635 36.192 55.841 1.00 28.21 ? 147 LEU B O 1 ATOM 3192 C CB . LEU C 3 147 ? 9.833 36.818 54.777 1.00 28.21 ? 147 LEU B CB 1 ATOM 3193 C CG . LEU C 3 147 ? 9.000 36.442 56.006 1.00 28.46 ? 147 LEU B CG 1 ATOM 3194 C CD1 . LEU C 3 147 ? 8.323 37.691 56.544 1.00 27.30 ? 147 LEU B CD1 1 ATOM 3195 C CD2 . LEU C 3 147 ? 7.968 35.379 55.638 1.00 27.99 ? 147 LEU B CD2 1 ATOM 3196 N N . TYR C 3 148 ? 11.818 37.727 57.293 1.00 28.80 ? 148 TYR B N 1 ATOM 3197 C CA . TYR C 3 148 ? 12.575 37.311 58.482 1.00 29.23 ? 148 TYR B CA 1 ATOM 3198 C C . TYR C 3 148 ? 14.099 37.373 58.358 1.00 28.18 ? 148 TYR B C 1 ATOM 3199 O O . TYR C 3 148 ? 14.817 36.776 59.158 1.00 28.70 ? 148 TYR B O 1 ATOM 3200 C CB . TYR C 3 148 ? 12.142 35.901 58.927 1.00 31.31 ? 148 TYR B CB 1 ATOM 3201 C CG . TYR C 3 148 ? 10.674 35.816 59.285 1.00 33.79 ? 148 TYR B CG 1 ATOM 3202 C CD1 . TYR C 3 148 ? 10.099 36.748 60.148 1.00 35.36 ? 148 TYR B CD1 1 ATOM 3203 C CD2 . TYR C 3 148 ? 9.849 34.832 58.734 1.00 34.59 ? 148 TYR B CD2 1 ATOM 3204 C CE1 . TYR C 3 148 ? 8.744 36.715 60.451 1.00 36.58 ? 148 TYR B CE1 1 ATOM 3205 C CE2 . TYR C 3 148 ? 8.483 34.786 59.031 1.00 35.94 ? 148 TYR B CE2 1 ATOM 3206 C CZ . TYR C 3 148 ? 7.941 35.736 59.891 1.00 37.55 ? 148 TYR B CZ 1 ATOM 3207 O OH . TYR C 3 148 ? 6.596 35.723 60.195 1.00 38.60 ? 148 TYR B OH 1 ATOM 3208 N N . GLY C 3 149 ? 14.587 38.103 57.361 1.00 27.54 ? 149 GLY B N 1 ATOM 3209 C CA . GLY C 3 149 ? 16.020 38.236 57.159 1.00 26.26 ? 149 GLY B CA 1 ATOM 3210 C C . GLY C 3 149 ? 16.642 37.060 56.441 1.00 25.17 ? 149 GLY B C 1 ATOM 3211 O O . GLY C 3 149 ? 17.858 36.985 56.301 1.00 24.69 ? 149 GLY B O 1 ATOM 3212 N N . LEU C 3 150 ? 15.802 36.143 55.981 1.00 25.60 ? 150 LEU B N 1 ATOM 3213 C CA . LEU C 3 150 ? 16.261 34.948 55.289 1.00 26.80 ? 150 LEU B CA 1 ATOM 3214 C C . LEU C 3 150 ? 16.572 35.252 53.831 1.00 29.00 ? 150 LEU B C 1 ATOM 3215 O O . LEU C 3 150 ? 16.019 36.188 53.263 1.00 29.86 ? 150 LEU B O 1 ATOM 3216 C CB . LEU C 3 150 ? 15.190 33.863 55.393 1.00 24.72 ? 150 LEU B CB 1 ATOM 3217 C CG . LEU C 3 150 ? 14.722 33.542 56.818 1.00 22.58 ? 150 LEU B CG 1 ATOM 3218 C CD1 . LEU C 3 150 ? 13.503 32.667 56.731 1.00 22.59 ? 150 LEU B CD1 1 ATOM 3219 C CD2 . LEU C 3 150 ? 15.818 32.863 57.621 1.00 20.74 ? 150 LEU B CD2 1 ATOM 3220 N N . CYS C 3 151 ? 17.463 34.457 53.238 1.00 31.15 ? 151 CYS B N 1 ATOM 3221 C CA . CYS C 3 151 ? 17.887 34.624 51.845 1.00 33.52 ? 151 CYS B CA 1 ATOM 3222 C C . CYS C 3 151 ? 17.131 33.782 50.841 1.00 34.74 ? 151 CYS B C 1 ATOM 3223 O O . CYS C 3 151 ? 16.598 32.730 51.175 1.00 36.33 ? 151 CYS B O 1 ATOM 3224 C CB . CYS C 3 151 ? 19.380 34.323 51.712 1.00 34.06 ? 151 CYS B CB 1 ATOM 3225 S SG . CYS C 3 151 ? 20.388 35.746 52.210 1.00 36.95 ? 151 CYS B SG 1 ATOM 3226 N N . LEU C 3 152 ? 17.072 34.262 49.605 1.00 36.31 ? 152 LEU B N 1 ATOM 3227 C CA . LEU C 3 152 ? 16.401 33.520 48.549 1.00 37.78 ? 152 LEU B CA 1 ATOM 3228 C C . LEU C 3 152 ? 17.449 32.507 48.135 1.00 39.49 ? 152 LEU B C 1 ATOM 3229 O O . LEU C 3 152 ? 18.608 32.872 47.915 1.00 39.78 ? 152 LEU B O 1 ATOM 3230 C CB . LEU C 3 152 ? 16.062 34.433 47.370 1.00 36.59 ? 152 LEU B CB 1 ATOM 3231 C CG . LEU C 3 152 ? 15.176 33.841 46.273 1.00 34.48 ? 152 LEU B CG 1 ATOM 3232 C CD1 . LEU C 3 152 ? 13.807 33.529 46.847 1.00 33.08 ? 152 LEU B CD1 1 ATOM 3233 C CD2 . LEU C 3 152 ? 15.052 34.829 45.125 1.00 33.85 ? 152 LEU B CD2 1 ATOM 3234 N N . GLN C 3 153 ? 17.057 31.241 48.048 1.00 41.12 ? 153 GLN B N 1 ATOM 3235 C CA . GLN C 3 153 ? 17.997 30.193 47.683 1.00 42.83 ? 153 GLN B CA 1 ATOM 3236 C C . GLN C 3 153 ? 17.403 29.169 46.724 1.00 43.30 ? 153 GLN B C 1 ATOM 3237 O O . GLN C 3 153 ? 16.219 28.843 46.797 1.00 43.21 ? 153 GLN B O 1 ATOM 3238 C CB . GLN C 3 153 ? 18.495 29.499 48.945 1.00 43.29 ? 153 GLN B CB 1 ATOM 3239 C CG . GLN C 3 153 ? 19.407 28.331 48.685 1.00 47.39 ? 153 GLN B CG 1 ATOM 3240 C CD . GLN C 3 153 ? 19.914 27.709 49.964 1.00 49.01 ? 153 GLN B CD 1 ATOM 3241 O OE1 . GLN C 3 153 ? 20.687 28.319 50.709 1.00 48.55 ? 153 GLN B OE1 1 ATOM 3242 N NE2 . GLN C 3 153 ? 19.474 26.491 50.232 1.00 50.40 ? 153 GLN B NE2 1 ATOM 3243 N N . ALA C 3 154 ? 18.238 28.660 45.825 1.00 43.99 ? 154 ALA B N 1 ATOM 3244 C CA . ALA C 3 154 ? 17.786 27.683 44.849 1.00 44.96 ? 154 ALA B CA 1 ATOM 3245 C C . ALA C 3 154 ? 18.494 26.345 44.979 1.00 46.37 ? 154 ALA B C 1 ATOM 3246 O O . ALA C 3 154 ? 19.706 26.282 45.205 1.00 46.56 ? 154 ALA B O 1 ATOM 3247 C CB . ALA C 3 154 ? 17.982 28.227 43.448 1.00 44.73 ? 154 ALA B CB 1 ATOM 3248 N N . ASN C 3 155 ? 17.717 25.277 44.832 1.00 48.41 ? 155 ASN B N 1 ATOM 3249 C CA . ASN C 3 155 ? 18.226 23.909 44.897 1.00 49.89 ? 155 ASN B CA 1 ATOM 3250 C C . ASN C 3 155 ? 17.668 23.107 43.713 1.00 50.82 ? 155 ASN B C 1 ATOM 3251 O O . ASN C 3 155 ? 16.586 22.500 43.795 1.00 49.49 ? 155 ASN B O 1 ATOM 3252 C CB . ASN C 3 155 ? 17.835 23.255 46.218 1.00 50.74 ? 155 ASN B CB 1 ATOM 3253 N N . SER C 3 156 ? 18.428 23.125 42.618 1.00 52.16 ? 156 SER B N 1 ATOM 3254 C CA . SER C 3 156 ? 18.076 22.440 41.375 1.00 53.03 ? 156 SER B CA 1 ATOM 3255 C C . SER C 3 156 ? 16.900 23.103 40.674 1.00 53.11 ? 156 SER B C 1 ATOM 3256 O O . SER C 3 156 ? 17.036 24.208 40.144 1.00 53.46 ? 156 SER B O 1 ATOM 3257 C CB . SER C 3 156 ? 17.777 20.954 41.625 1.00 53.81 ? 156 SER B CB 1 ATOM 3258 O OG . SER C 3 156 ? 18.949 20.174 41.440 1.00 53.33 ? 156 SER B OG 1 ATOM 3259 N N . GLY C 3 157 ? 15.750 22.440 40.663 1.00 52.64 ? 157 GLY B N 1 ATOM 3260 C CA . GLY C 3 157 ? 14.600 23.019 39.997 1.00 51.67 ? 157 GLY B CA 1 ATOM 3261 C C . GLY C 3 157 ? 13.666 23.758 40.931 1.00 50.74 ? 157 GLY B C 1 ATOM 3262 O O . GLY C 3 157 ? 12.572 24.150 40.527 1.00 50.45 ? 157 GLY B O 1 ATOM 3263 N N . GLN C 3 158 ? 14.088 23.959 42.175 1.00 50.77 ? 158 GLN B N 1 ATOM 3264 C CA . GLN C 3 158 ? 13.241 24.647 43.144 1.00 52.29 ? 158 GLN B CA 1 ATOM 3265 C C . GLN C 3 158 ? 13.882 25.852 43.809 1.00 51.67 ? 158 GLN B C 1 ATOM 3266 O O . GLN C 3 158 ? 15.109 25.953 43.911 1.00 51.58 ? 158 GLN B O 1 ATOM 3267 C CB . GLN C 3 158 ? 12.795 23.684 44.236 1.00 53.87 ? 158 GLN B CB 1 ATOM 3268 C CG . GLN C 3 158 ? 11.986 22.507 43.751 1.00 56.54 ? 158 GLN B CG 1 ATOM 3269 C CD . GLN C 3 158 ? 11.518 21.663 44.907 1.00 58.84 ? 158 GLN B CD 1 ATOM 3270 O OE1 . GLN C 3 158 ? 12.305 21.325 45.798 1.00 59.49 ? 158 GLN B OE1 1 ATOM 3271 N NE2 . GLN C 3 158 ? 10.233 21.316 44.909 1.00 57.98 ? 158 GLN B NE2 1 ATOM 3272 N N . VAL C 3 159 ? 13.025 26.755 44.280 1.00 51.27 ? 159 VAL B N 1 ATOM 3273 C CA . VAL C 3 159 ? 13.470 27.971 44.954 1.00 50.19 ? 159 VAL B CA 1 ATOM 3274 C C . VAL C 3 159 ? 12.626 28.260 46.191 1.00 49.64 ? 159 VAL B C 1 ATOM 3275 O O . VAL C 3 159 ? 11.396 28.293 46.124 1.00 49.23 ? 159 VAL B O 1 ATOM 3276 C CB . VAL C 3 159 ? 13.407 29.198 44.001 1.00 50.32 ? 159 VAL B CB 1 ATOM 3277 C CG1 . VAL C 3 159 ? 11.987 29.392 43.477 1.00 49.41 ? 159 VAL B CG1 1 ATOM 3278 C CG2 . VAL C 3 159 ? 13.883 30.442 44.725 1.00 48.68 ? 159 VAL B CG2 1 ATOM 3279 N N . TRP C 3 160 ? 13.300 28.451 47.320 1.00 49.66 ? 160 TRP B N 1 ATOM 3280 C CA . TRP C 3 160 ? 12.626 28.759 48.576 1.00 49.40 ? 160 TRP B CA 1 ATOM 3281 C C . TRP C 3 160 ? 13.475 29.749 49.354 1.00 47.99 ? 160 TRP B C 1 ATOM 3282 O O . TRP C 3 160 ? 14.556 30.137 48.903 1.00 46.70 ? 160 TRP B O 1 ATOM 3283 C CB . TRP C 3 160 ? 12.384 27.483 49.408 1.00 51.70 ? 160 TRP B CB 1 ATOM 3284 C CG . TRP C 3 160 ? 13.629 26.774 49.884 1.00 54.27 ? 160 TRP B CG 1 ATOM 3285 C CD1 . TRP C 3 160 ? 14.350 27.041 51.015 1.00 55.16 ? 160 TRP B CD1 1 ATOM 3286 C CD2 . TRP C 3 160 ? 14.285 25.673 49.243 1.00 56.06 ? 160 TRP B CD2 1 ATOM 3287 N NE1 . TRP C 3 160 ? 15.413 26.172 51.120 1.00 55.56 ? 160 TRP B NE1 1 ATOM 3288 C CE2 . TRP C 3 160 ? 15.396 25.323 50.047 1.00 56.72 ? 160 TRP B CE2 1 ATOM 3289 C CE3 . TRP C 3 160 ? 14.042 24.947 48.069 1.00 56.96 ? 160 TRP B CE3 1 ATOM 3290 C CZ2 . TRP C 3 160 ? 16.262 24.275 49.710 1.00 58.01 ? 160 TRP B CZ2 1 ATOM 3291 C CZ3 . TRP C 3 160 ? 14.903 23.906 47.737 1.00 57.77 ? 160 TRP B CZ3 1 ATOM 3292 C CH2 . TRP C 3 160 ? 15.999 23.582 48.559 1.00 57.71 ? 160 TRP B CH2 1 ATOM 3293 N N . ILE C 3 161 ? 12.982 30.160 50.516 1.00 47.44 ? 161 ILE B N 1 ATOM 3294 C CA . ILE C 3 161 ? 13.703 31.109 51.354 1.00 47.62 ? 161 ILE B CA 1 ATOM 3295 C C . ILE C 3 161 ? 14.321 30.342 52.532 1.00 47.51 ? 161 ILE B C 1 ATOM 3296 O O . ILE C 3 161 ? 13.701 29.428 53.073 1.00 47.83 ? 161 ILE B O 1 ATOM 3297 C CB . ILE C 3 161 ? 12.742 32.220 51.843 1.00 47.28 ? 161 ILE B CB 1 ATOM 3298 C CG1 . ILE C 3 161 ? 13.546 33.433 52.291 1.00 47.59 ? 161 ILE B CG1 1 ATOM 3299 C CG2 . ILE C 3 161 ? 11.847 31.701 52.966 1.00 46.94 ? 161 ILE B CG2 1 ATOM 3300 C CD1 . ILE C 3 161 ? 12.687 34.612 52.669 1.00 49.87 ? 161 ILE B CD1 1 ATOM 3301 N N . GLU C 3 162 ? 15.539 30.702 52.923 1.00 46.57 ? 162 GLU B N 1 ATOM 3302 C CA . GLU C 3 162 ? 16.214 29.996 54.003 1.00 46.75 ? 162 GLU B CA 1 ATOM 3303 C C . GLU C 3 162 ? 17.287 30.890 54.624 1.00 46.64 ? 162 GLU B C 1 ATOM 3304 O O . GLU C 3 162 ? 17.666 31.886 54.020 1.00 46.93 ? 162 GLU B O 1 ATOM 3305 C CB . GLU C 3 162 ? 16.825 28.731 53.419 1.00 47.34 ? 162 GLU B CB 1 ATOM 3306 C CG . GLU C 3 162 ? 17.481 27.803 54.400 1.00 51.70 ? 162 GLU B CG 1 ATOM 3307 C CD . GLU C 3 162 ? 17.904 26.516 53.728 1.00 53.58 ? 162 GLU B CD 1 ATOM 3308 O OE1 . GLU C 3 162 ? 18.761 26.569 52.823 1.00 54.42 ? 162 GLU B OE1 1 ATOM 3309 O OE2 . GLU C 3 162 ? 17.370 25.450 54.093 1.00 56.47 ? 162 GLU B OE2 1 ATOM 3310 N N . ASP C 3 163 ? 17.795 30.551 55.810 1.00 47.51 ? 163 ASP B N 1 ATOM 3311 C CA . ASP C 3 163 ? 18.796 31.426 56.431 1.00 48.10 ? 163 ASP B CA 1 ATOM 3312 C C . ASP C 3 163 ? 20.074 31.638 55.603 1.00 47.06 ? 163 ASP B C 1 ATOM 3313 O O . ASP C 3 163 ? 20.620 30.713 54.996 1.00 45.30 ? 163 ASP B O 1 ATOM 3314 C CB . ASP C 3 163 ? 19.115 30.988 57.882 1.00 49.58 ? 163 ASP B CB 1 ATOM 3315 C CG . ASP C 3 163 ? 19.808 29.644 57.969 1.00 50.65 ? 163 ASP B CG 1 ATOM 3316 O OD1 . ASP C 3 163 ? 19.288 28.659 57.391 1.00 50.97 ? 163 ASP B OD1 1 ATOM 3317 O OD2 . ASP C 3 163 ? 20.868 29.580 58.640 1.00 49.07 ? 163 ASP B OD2 1 ATOM 3318 N N . CYS C 3 164 ? 20.521 32.891 55.587 1.00 46.93 ? 164 CYS B N 1 ATOM 3319 C CA . CYS C 3 164 ? 21.679 33.326 54.817 1.00 47.57 ? 164 CYS B CA 1 ATOM 3320 C C . CYS C 3 164 ? 23.044 32.846 55.250 1.00 48.98 ? 164 CYS B C 1 ATOM 3321 O O . CYS C 3 164 ? 23.613 33.361 56.213 1.00 50.08 ? 164 CYS B O 1 ATOM 3322 C CB . CYS C 3 164 ? 21.743 34.854 54.775 1.00 45.27 ? 164 CYS B CB 1 ATOM 3323 S SG . CYS C 3 164 ? 20.251 35.744 54.229 1.00 44.30 ? 164 CYS B SG 1 ATOM 3324 N N . SER C 3 165 ? 23.583 31.871 54.534 1.00 51.50 ? 165 SER B N 1 ATOM 3325 C CA . SER C 3 165 ? 24.930 31.405 54.831 1.00 53.23 ? 165 SER B CA 1 ATOM 3326 C C . SER C 3 165 ? 25.759 32.113 53.762 1.00 54.02 ? 165 SER B C 1 ATOM 3327 O O . SER C 3 165 ? 25.578 31.864 52.570 1.00 52.80 ? 165 SER B O 1 ATOM 3328 C CB . SER C 3 165 ? 25.034 29.885 54.679 1.00 53.59 ? 165 SER B CB 1 ATOM 3329 N N . SER C 3 166 ? 26.626 33.025 54.191 1.00 56.33 ? 166 SER B N 1 ATOM 3330 C CA . SER C 3 166 ? 27.477 33.779 53.280 1.00 59.38 ? 166 SER B CA 1 ATOM 3331 C C . SER C 3 166 ? 28.448 32.877 52.516 1.00 61.77 ? 166 SER B C 1 ATOM 3332 O O . SER C 3 166 ? 29.623 33.227 52.346 1.00 61.61 ? 166 SER B O 1 ATOM 3333 C CB . SER C 3 166 ? 28.243 34.858 54.066 1.00 58.46 ? 166 SER B CB 1 ATOM 3334 O OG . SER C 3 166 ? 29.008 35.681 53.206 1.00 58.59 ? 166 SER B OG 1 ATOM 3335 N N . GLU C 3 167 ? 27.943 31.734 52.040 1.00 64.45 ? 167 GLU B N 1 ATOM 3336 C CA . GLU C 3 167 ? 28.754 30.763 51.304 1.00 66.80 ? 167 GLU B CA 1 ATOM 3337 C C . GLU C 3 167 ? 27.892 29.589 50.798 1.00 66.83 ? 167 GLU B C 1 ATOM 3338 O O . GLU C 3 167 ? 28.223 28.947 49.794 1.00 67.32 ? 167 GLU B O 1 ATOM 3339 C CB . GLU C 3 167 ? 29.883 30.246 52.226 1.00 68.70 ? 167 GLU B CB 1 ATOM 3340 C CG . GLU C 3 167 ? 31.123 29.694 51.520 1.00 72.37 ? 167 GLU B CG 1 ATOM 3341 C CD . GLU C 3 167 ? 30.997 28.223 51.128 1.00 74.76 ? 167 GLU B CD 1 ATOM 3342 O OE1 . GLU C 3 167 ? 30.912 27.367 52.041 1.00 75.18 ? 167 GLU B OE1 1 ATOM 3343 O OE2 . GLU C 3 167 ? 30.989 27.923 49.909 1.00 75.82 ? 167 GLU B OE2 1 ATOM 3344 N N . LYS C 3 168 ? 26.777 29.338 51.486 1.00 66.27 ? 168 LYS B N 1 ATOM 3345 C CA . LYS C 3 168 ? 25.853 28.241 51.165 1.00 65.22 ? 168 LYS B CA 1 ATOM 3346 C C . LYS C 3 168 ? 25.633 27.953 49.679 1.00 64.65 ? 168 LYS B C 1 ATOM 3347 O O . LYS C 3 168 ? 26.123 28.683 48.810 1.00 64.38 ? 168 LYS B O 1 ATOM 3348 C CB . LYS C 3 168 ? 24.493 28.488 51.839 1.00 64.85 ? 168 LYS B CB 1 ATOM 3349 C CG . LYS C 3 168 ? 24.091 27.377 52.813 1.00 64.23 ? 168 LYS B CG 1 ATOM 3350 C CD . LYS C 3 168 ? 22.735 26.775 52.462 1.00 64.32 ? 168 LYS B CD 1 ATOM 3351 C CE . LYS C 3 168 ? 22.671 25.318 52.880 1.00 64.09 ? 168 LYS B CE 1 ATOM 3352 N NZ . LYS C 3 168 ? 23.623 24.507 52.056 1.00 63.53 ? 168 LYS B NZ 1 ATOM 3353 N N . ALA C 3 169 ? 24.890 26.871 49.417 1.00 63.67 ? 169 ALA B N 1 ATOM 3354 C CA . ALA C 3 169 ? 24.530 26.394 48.065 1.00 61.70 ? 169 ALA B CA 1 ATOM 3355 C C . ALA C 3 169 ? 23.991 27.470 47.107 1.00 59.42 ? 169 ALA B C 1 ATOM 3356 O O . ALA C 3 169 ? 22.822 27.416 46.701 1.00 59.03 ? 169 ALA B O 1 ATOM 3357 C CB . ALA C 3 169 ? 23.503 25.265 48.185 1.00 61.95 ? 169 ALA B CB 1 ATOM 3358 N N . GLU C 3 170 ? 24.847 28.426 46.738 1.00 56.27 ? 170 GLU B N 1 ATOM 3359 C CA . GLU C 3 170 ? 24.461 29.503 45.831 1.00 52.62 ? 170 GLU B CA 1 ATOM 3360 C C . GLU C 3 170 ? 23.121 30.174 46.187 1.00 50.13 ? 170 GLU B C 1 ATOM 3361 O O . GLU C 3 170 ? 22.032 29.719 45.813 1.00 48.74 ? 170 GLU B O 1 ATOM 3362 C CB . GLU C 3 170 ? 24.426 28.985 44.386 1.00 52.27 ? 170 GLU B CB 1 ATOM 3363 N N . GLN C 3 171 ? 23.239 31.251 46.952 1.00 47.58 ? 171 GLN B N 1 ATOM 3364 C CA . GLN C 3 171 ? 22.123 32.086 47.352 1.00 44.43 ? 171 GLN B CA 1 ATOM 3365 C C . GLN C 3 171 ? 22.405 33.370 46.592 1.00 43.63 ? 171 GLN B C 1 ATOM 3366 O O . GLN C 3 171 ? 21.711 34.377 46.760 1.00 43.43 ? 171 GLN B O 1 ATOM 3367 C CB . GLN C 3 171 ? 22.157 32.353 48.844 1.00 42.95 ? 171 GLN B CB 1 ATOM 3368 C CG . GLN C 3 171 ? 22.030 31.119 49.673 1.00 40.73 ? 171 GLN B CG 1 ATOM 3369 C CD . GLN C 3 171 ? 21.726 31.455 51.098 1.00 42.07 ? 171 GLN B CD 1 ATOM 3370 O OE1 . GLN C 3 171 ? 22.377 32.320 51.693 1.00 41.92 ? 171 GLN B OE1 1 ATOM 3371 N NE2 . GLN C 3 171 ? 20.735 30.777 51.667 1.00 41.39 ? 171 GLN B NE2 1 ATOM 3372 N N . GLN C 3 172 ? 23.459 33.315 45.775 1.00 42.13 ? 172 GLN B N 1 ATOM 3373 C CA . GLN C 3 172 ? 23.864 34.434 44.939 1.00 40.13 ? 172 GLN B CA 1 ATOM 3374 C C . GLN C 3 172 ? 23.090 34.317 43.631 1.00 39.12 ? 172 GLN B C 1 ATOM 3375 O O . GLN C 3 172 ? 23.005 33.232 43.057 1.00 38.74 ? 172 GLN B O 1 ATOM 3376 C CB . GLN C 3 172 ? 25.379 34.385 44.679 1.00 38.41 ? 172 GLN B CB 1 ATOM 3377 N N . TRP C 3 173 ? 22.512 35.429 43.179 1.00 36.95 ? 173 TRP B N 1 ATOM 3378 C CA . TRP C 3 173 ? 21.745 35.449 41.937 1.00 33.97 ? 173 TRP B CA 1 ATOM 3379 C C . TRP C 3 173 ? 22.306 36.488 40.986 1.00 32.96 ? 173 TRP B C 1 ATOM 3380 O O . TRP C 3 173 ? 22.892 37.483 41.412 1.00 34.14 ? 173 TRP B O 1 ATOM 3381 C CB . TRP C 3 173 ? 20.282 35.783 42.204 1.00 31.50 ? 173 TRP B CB 1 ATOM 3382 C CG . TRP C 3 173 ? 19.617 34.855 43.129 1.00 29.77 ? 173 TRP B CG 1 ATOM 3383 C CD1 . TRP C 3 173 ? 19.698 34.858 44.486 1.00 29.35 ? 173 TRP B CD1 1 ATOM 3384 C CD2 . TRP C 3 173 ? 18.762 33.762 42.778 1.00 28.98 ? 173 TRP B CD2 1 ATOM 3385 N NE1 . TRP C 3 173 ? 18.944 33.837 45.008 1.00 29.76 ? 173 TRP B NE1 1 ATOM 3386 C CE2 . TRP C 3 173 ? 18.358 33.147 43.977 1.00 28.66 ? 173 TRP B CE2 1 ATOM 3387 C CE3 . TRP C 3 173 ? 18.297 33.240 41.562 1.00 27.91 ? 173 TRP B CE3 1 ATOM 3388 C CZ2 . TRP C 3 173 ? 17.510 32.037 43.998 1.00 27.58 ? 173 TRP B CZ2 1 ATOM 3389 C CZ3 . TRP C 3 173 ? 17.456 32.137 41.584 1.00 24.81 ? 173 TRP B CZ3 1 ATOM 3390 C CH2 . TRP C 3 173 ? 17.072 31.550 42.790 1.00 25.70 ? 173 TRP B CH2 1 ATOM 3391 N N . ALA C 3 174 ? 22.118 36.261 39.694 1.00 30.46 ? 174 ALA B N 1 ATOM 3392 C CA . ALA C 3 174 ? 22.603 37.194 38.699 1.00 28.42 ? 174 ALA B CA 1 ATOM 3393 C C . ALA C 3 174 ? 21.401 37.797 37.989 1.00 27.38 ? 174 ALA B C 1 ATOM 3394 O O . ALA C 3 174 ? 20.555 37.079 37.468 1.00 26.72 ? 174 ALA B O 1 ATOM 3395 C CB . ALA C 3 174 ? 23.504 36.475 37.713 1.00 29.28 ? 174 ALA B CB 1 ATOM 3396 N N . LEU C 3 175 ? 21.323 39.121 37.985 1.00 27.47 ? 175 LEU B N 1 ATOM 3397 C CA . LEU C 3 175 ? 20.221 39.813 37.335 1.00 27.53 ? 175 LEU B CA 1 ATOM 3398 C C . LEU C 3 175 ? 20.657 40.213 35.931 1.00 27.67 ? 175 LEU B C 1 ATOM 3399 O O . LEU C 3 175 ? 21.603 40.978 35.774 1.00 27.96 ? 175 LEU B O 1 ATOM 3400 C CB . LEU C 3 175 ? 19.834 41.055 38.141 1.00 26.99 ? 175 LEU B CB 1 ATOM 3401 C CG . LEU C 3 175 ? 19.742 40.925 39.670 1.00 26.70 ? 175 LEU B CG 1 ATOM 3402 C CD1 . LEU C 3 175 ? 19.057 42.169 40.197 1.00 25.05 ? 175 LEU B CD1 1 ATOM 3403 C CD2 . LEU C 3 175 ? 18.963 39.680 40.098 1.00 24.87 ? 175 LEU B CD2 1 ATOM 3404 N N . TYR C 3 176 ? 19.967 39.693 34.917 1.00 28.52 ? 176 TYR B N 1 ATOM 3405 C CA . TYR C 3 176 ? 20.298 39.978 33.518 1.00 29.59 ? 176 TYR B CA 1 ATOM 3406 C C . TYR C 3 176 ? 19.621 41.206 32.943 1.00 29.17 ? 176 TYR B C 1 ATOM 3407 O O . TYR C 3 176 ? 18.617 41.673 33.465 1.00 29.22 ? 176 TYR B O 1 ATOM 3408 C CB . TYR C 3 176 ? 19.962 38.773 32.632 1.00 30.51 ? 176 TYR B CB 1 ATOM 3409 C CG . TYR C 3 176 ? 21.050 37.733 32.612 1.00 32.95 ? 176 TYR B CG 1 ATOM 3410 C CD1 . TYR C 3 176 ? 21.490 37.143 33.792 1.00 34.72 ? 176 TYR B CD1 1 ATOM 3411 C CD2 . TYR C 3 176 ? 21.663 37.358 31.421 1.00 33.64 ? 176 TYR B CD2 1 ATOM 3412 C CE1 . TYR C 3 176 ? 22.515 36.213 33.789 1.00 36.66 ? 176 TYR B CE1 1 ATOM 3413 C CE2 . TYR C 3 176 ? 22.686 36.427 31.408 1.00 35.22 ? 176 TYR B CE2 1 ATOM 3414 C CZ . TYR C 3 176 ? 23.108 35.862 32.596 1.00 36.46 ? 176 TYR B CZ 1 ATOM 3415 O OH . TYR C 3 176 ? 24.131 34.951 32.605 1.00 38.76 ? 176 TYR B OH 1 ATOM 3416 N N . ALA C 3 177 ? 20.185 41.721 31.856 1.00 28.39 ? 177 ALA B N 1 ATOM 3417 C CA . ALA C 3 177 ? 19.637 42.893 31.195 1.00 28.24 ? 177 ALA B CA 1 ATOM 3418 C C . ALA C 3 177 ? 18.228 42.591 30.688 1.00 27.99 ? 177 ALA B C 1 ATOM 3419 O O . ALA C 3 177 ? 17.370 43.479 30.632 1.00 27.45 ? 177 ALA B O 1 ATOM 3420 C CB . ALA C 3 177 ? 20.546 43.313 30.031 1.00 27.39 ? 177 ALA B CB 1 ATOM 3421 N N . ASP C 3 178 ? 17.986 41.330 30.333 1.00 28.17 ? 178 ASP B N 1 ATOM 3422 C CA . ASP C 3 178 ? 16.680 40.927 29.820 1.00 28.95 ? 178 ASP B CA 1 ATOM 3423 C C . ASP C 3 178 ? 15.611 40.775 30.887 1.00 28.82 ? 178 ASP B C 1 ATOM 3424 O O . ASP C 3 178 ? 14.498 40.353 30.594 1.00 30.30 ? 178 ASP B O 1 ATOM 3425 C CB . ASP C 3 178 ? 16.775 39.628 29.009 1.00 29.28 ? 178 ASP B CB 1 ATOM 3426 C CG . ASP C 3 178 ? 17.504 38.530 29.737 1.00 29.37 ? 178 ASP B CG 1 ATOM 3427 O OD1 . ASP C 3 178 ? 17.334 38.393 30.965 1.00 30.29 ? 178 ASP B OD1 1 ATOM 3428 O OD2 . ASP C 3 178 ? 18.245 37.788 29.062 1.00 29.69 ? 178 ASP B OD2 1 ATOM 3429 N N . GLY C 3 179 ? 15.949 41.115 32.124 1.00 27.88 ? 179 GLY B N 1 ATOM 3430 C CA . GLY C 3 179 ? 14.978 41.037 33.194 1.00 26.09 ? 179 GLY B CA 1 ATOM 3431 C C . GLY C 3 179 ? 14.781 39.668 33.792 1.00 25.99 ? 179 GLY B C 1 ATOM 3432 O O . GLY C 3 179 ? 13.841 39.463 34.549 1.00 26.27 ? 179 GLY B O 1 ATOM 3433 N N . SER C 3 180 ? 15.647 38.721 33.454 1.00 25.43 ? 180 SER B N 1 ATOM 3434 C CA . SER C 3 180 ? 15.528 37.381 34.012 1.00 26.35 ? 180 SER B CA 1 ATOM 3435 C C . SER C 3 180 ? 16.416 37.325 35.254 1.00 26.84 ? 180 SER B C 1 ATOM 3436 O O . SER C 3 180 ? 17.408 38.042 35.331 1.00 26.75 ? 180 SER B O 1 ATOM 3437 C CB . SER C 3 180 ? 15.968 36.330 32.982 1.00 25.74 ? 180 SER B CB 1 ATOM 3438 O OG . SER C 3 180 ? 17.315 36.517 32.586 1.00 23.61 ? 180 SER B OG 1 ATOM 3439 N N . ILE C 3 181 ? 16.040 36.516 36.242 1.00 26.85 ? 181 ILE B N 1 ATOM 3440 C CA . ILE C 3 181 ? 16.840 36.378 37.461 1.00 26.74 ? 181 ILE B CA 1 ATOM 3441 C C . ILE C 3 181 ? 17.418 34.972 37.386 1.00 28.01 ? 181 ILE B C 1 ATOM 3442 O O . ILE C 3 181 ? 16.683 33.989 37.415 1.00 28.68 ? 181 ILE B O 1 ATOM 3443 C CB . ILE C 3 181 ? 15.978 36.544 38.736 1.00 24.88 ? 181 ILE B CB 1 ATOM 3444 C CG1 . ILE C 3 181 ? 15.434 37.973 38.802 1.00 23.10 ? 181 ILE B CG1 1 ATOM 3445 C CG2 . ILE C 3 181 ? 16.805 36.261 39.968 1.00 23.37 ? 181 ILE B CG2 1 ATOM 3446 C CD1 . ILE C 3 181 ? 14.588 38.262 40.018 1.00 22.27 ? 181 ILE B CD1 1 ATOM 3447 N N . ARG C 3 182 ? 18.738 34.882 37.279 1.00 29.48 ? 182 ARG B N 1 ATOM 3448 C CA . ARG C 3 182 ? 19.382 33.595 37.118 1.00 30.63 ? 182 ARG B CA 1 ATOM 3449 C C . ARG C 3 182 ? 20.277 33.145 38.245 1.00 34.05 ? 182 ARG B C 1 ATOM 3450 O O . ARG C 3 182 ? 21.070 33.927 38.769 1.00 34.31 ? 182 ARG B O 1 ATOM 3451 C CB . ARG C 3 182 ? 20.180 33.593 35.814 1.00 28.73 ? 182 ARG B CB 1 ATOM 3452 C CG . ARG C 3 182 ? 19.399 34.140 34.645 1.00 27.84 ? 182 ARG B CG 1 ATOM 3453 C CD . ARG C 3 182 ? 20.038 33.795 33.328 1.00 28.37 ? 182 ARG B CD 1 ATOM 3454 N NE . ARG C 3 182 ? 19.345 34.450 32.224 1.00 30.05 ? 182 ARG B NE 1 ATOM 3455 C CZ . ARG C 3 182 ? 19.411 34.065 30.954 1.00 29.03 ? 182 ARG B CZ 1 ATOM 3456 N NH1 . ARG C 3 182 ? 20.140 33.018 30.602 1.00 28.78 ? 182 ARG B NH1 1 ATOM 3457 N NH2 . ARG C 3 182 ? 18.736 34.728 30.034 1.00 27.36 ? 182 ARG B NH2 1 ATOM 3458 N N . PRO C 3 183 ? 20.162 31.858 38.635 1.00 37.78 ? 183 PRO B N 1 ATOM 3459 C CA . PRO C 3 183 ? 20.974 31.281 39.712 1.00 38.86 ? 183 PRO B CA 1 ATOM 3460 C C . PRO C 3 183 ? 22.449 31.293 39.316 1.00 41.38 ? 183 PRO B C 1 ATOM 3461 O O . PRO C 3 183 ? 22.852 30.664 38.339 1.00 42.02 ? 183 PRO B O 1 ATOM 3462 C CB . PRO C 3 183 ? 20.397 29.871 39.864 1.00 38.59 ? 183 PRO B CB 1 ATOM 3463 C CG . PRO C 3 183 ? 19.844 29.572 38.509 1.00 37.38 ? 183 PRO B CG 1 ATOM 3464 C CD . PRO C 3 183 ? 19.190 30.866 38.135 1.00 37.47 ? 183 PRO B CD 1 ATOM 3465 N N . GLN C 3 184 ? 23.237 32.034 40.086 1.00 43.85 ? 184 GLN B N 1 ATOM 3466 C CA . GLN C 3 184 ? 24.671 32.202 39.862 1.00 45.50 ? 184 GLN B CA 1 ATOM 3467 C C . GLN C 3 184 ? 25.446 31.022 39.301 1.00 46.34 ? 184 GLN B C 1 ATOM 3468 O O . GLN C 3 184 ? 26.200 31.174 38.342 1.00 46.03 ? 184 GLN B O 1 ATOM 3469 C CB . GLN C 3 184 ? 25.342 32.651 41.161 1.00 46.76 ? 184 GLN B CB 1 ATOM 3470 C CG . GLN C 3 184 ? 26.129 33.936 41.016 1.00 47.85 ? 184 GLN B CG 1 ATOM 3471 C CD . GLN C 3 184 ? 27.321 33.785 40.090 1.00 47.73 ? 184 GLN B CD 1 ATOM 3472 O OE1 . GLN C 3 184 ? 28.306 33.152 40.445 1.00 48.72 ? 184 GLN B OE1 1 ATOM 3473 N NE2 . GLN C 3 184 ? 27.230 34.361 38.894 1.00 47.47 ? 184 GLN B NE2 1 ATOM 3474 N N . GLN C 3 185 ? 25.274 29.852 39.902 1.00 48.53 ? 185 GLN B N 1 ATOM 3475 C CA . GLN C 3 185 ? 25.995 28.661 39.464 1.00 51.86 ? 185 GLN B CA 1 ATOM 3476 C C . GLN C 3 185 ? 25.520 28.025 38.153 1.00 51.81 ? 185 GLN B C 1 ATOM 3477 O O . GLN C 3 185 ? 26.267 27.283 37.518 1.00 52.06 ? 185 GLN B O 1 ATOM 3478 C CB . GLN C 3 185 ? 25.959 27.612 40.567 1.00 54.91 ? 185 GLN B CB 1 ATOM 3479 C CG . GLN C 3 185 ? 24.560 27.232 40.981 1.00 60.76 ? 185 GLN B CG 1 ATOM 3480 C CD . GLN C 3 185 ? 24.536 25.919 41.725 1.00 64.61 ? 185 GLN B CD 1 ATOM 3481 O OE1 . GLN C 3 185 ? 25.243 25.747 42.726 1.00 66.47 ? 185 GLN B OE1 1 ATOM 3482 N NE2 . GLN C 3 185 ? 23.725 24.975 41.239 1.00 65.24 ? 185 GLN B NE2 1 ATOM 3483 N N . ASN C 3 186 ? 24.285 28.302 37.751 1.00 51.66 ? 186 ASN B N 1 ATOM 3484 C CA . ASN C 3 186 ? 23.749 27.742 36.512 1.00 51.05 ? 186 ASN B CA 1 ATOM 3485 C C . ASN C 3 186 ? 23.018 28.840 35.727 1.00 48.70 ? 186 ASN B C 1 ATOM 3486 O O . ASN C 3 186 ? 21.787 28.909 35.716 1.00 47.60 ? 186 ASN B O 1 ATOM 3487 C CB . ASN C 3 186 ? 22.805 26.581 36.842 1.00 53.85 ? 186 ASN B CB 1 ATOM 3488 C CG . ASN C 3 186 ? 22.532 25.704 35.641 1.00 56.94 ? 186 ASN B CG 1 ATOM 3489 O OD1 . ASN C 3 186 ? 23.462 25.273 34.956 1.00 58.34 ? 186 ASN B OD1 1 ATOM 3490 N ND2 . ASN C 3 186 ? 21.257 25.432 35.375 1.00 57.50 ? 186 ASN B ND2 1 ATOM 3491 N N . ARG C 3 187 ? 23.795 29.680 35.050 1.00 46.52 ? 187 ARG B N 1 ATOM 3492 C CA . ARG C 3 187 ? 23.251 30.815 34.319 1.00 45.17 ? 187 ARG B CA 1 ATOM 3493 C C . ARG C 3 187 ? 22.309 30.665 33.131 1.00 45.06 ? 187 ARG B C 1 ATOM 3494 O O . ARG C 3 187 ? 21.917 31.672 32.548 1.00 44.98 ? 187 ARG B O 1 ATOM 3495 C CB . ARG C 3 187 ? 24.384 31.767 33.951 1.00 43.41 ? 187 ARG B CB 1 ATOM 3496 C CG . ARG C 3 187 ? 24.891 32.529 35.158 1.00 43.73 ? 187 ARG B CG 1 ATOM 3497 C CD . ARG C 3 187 ? 25.884 33.595 34.768 1.00 45.11 ? 187 ARG B CD 1 ATOM 3498 N NE . ARG C 3 187 ? 26.201 34.470 35.891 1.00 46.85 ? 187 ARG B NE 1 ATOM 3499 C CZ . ARG C 3 187 ? 27.111 35.442 35.849 1.00 48.46 ? 187 ARG B CZ 1 ATOM 3500 N NH1 . ARG C 3 187 ? 27.805 35.666 34.736 1.00 47.58 ? 187 ARG B NH1 1 ATOM 3501 N NH2 . ARG C 3 187 ? 27.322 36.200 36.922 1.00 48.13 ? 187 ARG B NH2 1 ATOM 3502 N N . ASP C 3 188 ? 21.941 29.449 32.745 1.00 45.34 ? 188 ASP B N 1 ATOM 3503 C CA . ASP C 3 188 ? 20.980 29.329 31.655 1.00 46.70 ? 188 ASP B CA 1 ATOM 3504 C C . ASP C 3 188 ? 19.691 28.762 32.231 1.00 45.70 ? 188 ASP B C 1 ATOM 3505 O O . ASP C 3 188 ? 18.911 28.081 31.557 1.00 45.09 ? 188 ASP B O 1 ATOM 3506 C CB . ASP C 3 188 ? 21.499 28.470 30.499 1.00 49.94 ? 188 ASP B CB 1 ATOM 3507 C CG . ASP C 3 188 ? 22.107 27.187 30.959 1.00 54.51 ? 188 ASP B CG 1 ATOM 3508 O OD1 . ASP C 3 188 ? 21.660 26.678 32.017 1.00 58.08 ? 188 ASP B OD1 1 ATOM 3509 O OD2 . ASP C 3 188 ? 23.018 26.689 30.254 1.00 55.13 ? 188 ASP B OD2 1 ATOM 3510 N N . ASN C 3 189 ? 19.500 29.062 33.513 1.00 45.14 ? 189 ASN B N 1 ATOM 3511 C CA . ASN C 3 189 ? 18.311 28.684 34.263 1.00 43.96 ? 189 ASN B CA 1 ATOM 3512 C C . ASN C 3 189 ? 17.670 29.981 34.752 1.00 42.59 ? 189 ASN B C 1 ATOM 3513 O O . ASN C 3 189 ? 18.349 30.862 35.272 1.00 42.12 ? 189 ASN B O 1 ATOM 3514 C CB . ASN C 3 189 ? 18.672 27.783 35.439 1.00 44.78 ? 189 ASN B CB 1 ATOM 3515 C CG . ASN C 3 189 ? 18.558 26.316 35.089 1.00 45.99 ? 189 ASN B CG 1 ATOM 3516 O OD1 . ASN C 3 189 ? 18.187 25.967 33.967 1.00 45.18 ? 189 ASN B OD1 1 ATOM 3517 N ND2 . ASN C 3 189 ? 18.868 25.446 36.049 1.00 46.23 ? 189 ASN B ND2 1 ATOM 3518 N N . CYS C 3 190 ? 16.361 30.094 34.568 1.00 40.78 ? 190 CYS B N 1 ATOM 3519 C CA . CYS C 3 190 ? 15.631 31.295 34.943 1.00 39.77 ? 190 CYS B CA 1 ATOM 3520 C C . CYS C 3 190 ? 14.660 31.123 36.091 1.00 39.20 ? 190 CYS B C 1 ATOM 3521 O O . CYS C 3 190 ? 14.096 30.053 36.266 1.00 40.98 ? 190 CYS B O 1 ATOM 3522 C CB . CYS C 3 190 ? 14.864 31.809 33.727 1.00 38.49 ? 190 CYS B CB 1 ATOM 3523 S SG . CYS C 3 190 ? 15.864 32.916 32.701 1.00 39.30 ? 190 CYS B SG 1 ATOM 3524 N N . LEU C 3 191 ? 14.472 32.172 36.883 1.00 38.27 ? 191 LEU B N 1 ATOM 3525 C CA . LEU C 3 191 ? 13.497 32.103 37.965 1.00 37.23 ? 191 LEU B CA 1 ATOM 3526 C C . LEU C 3 191 ? 12.195 32.141 37.159 1.00 36.07 ? 191 LEU B C 1 ATOM 3527 O O . LEU C 3 191 ? 11.811 33.187 36.632 1.00 35.57 ? 191 LEU B O 1 ATOM 3528 C CB . LEU C 3 191 ? 13.620 33.329 38.884 1.00 36.65 ? 191 LEU B CB 1 ATOM 3529 C CG . LEU C 3 191 ? 12.687 33.419 40.099 1.00 35.38 ? 191 LEU B CG 1 ATOM 3530 C CD1 . LEU C 3 191 ? 12.887 32.217 40.990 1.00 36.08 ? 191 LEU B CD1 1 ATOM 3531 C CD2 . LEU C 3 191 ? 12.970 34.691 40.869 1.00 34.45 ? 191 LEU B CD2 1 ATOM 3532 N N . THR C 3 192 ? 11.540 30.991 37.046 1.00 34.93 ? 192 THR B N 1 ATOM 3533 C CA . THR C 3 192 ? 10.329 30.871 36.240 1.00 35.00 ? 192 THR B CA 1 ATOM 3534 C C . THR C 3 192 ? 9.010 30.671 36.971 1.00 36.47 ? 192 THR B C 1 ATOM 3535 O O . THR C 3 192 ? 8.955 30.120 38.069 1.00 36.32 ? 192 THR B O 1 ATOM 3536 C CB . THR C 3 192 ? 10.487 29.723 35.223 1.00 33.83 ? 192 THR B CB 1 ATOM 3537 O OG1 . THR C 3 192 ? 11.587 30.013 34.351 1.00 32.76 ? 192 THR B OG1 1 ATOM 3538 C CG2 . THR C 3 192 ? 9.219 29.538 34.405 1.00 32.82 ? 192 THR B CG2 1 ATOM 3539 N N . SER C 3 193 ? 7.943 31.122 36.326 1.00 38.02 ? 193 SER B N 1 ATOM 3540 C CA . SER C 3 193 ? 6.602 31.011 36.860 1.00 41.73 ? 193 SER B CA 1 ATOM 3541 C C . SER C 3 193 ? 5.672 30.480 35.760 1.00 45.20 ? 193 SER B C 1 ATOM 3542 O O . SER C 3 193 ? 5.287 31.232 34.867 1.00 46.05 ? 193 SER B O 1 ATOM 3543 C CB . SER C 3 193 ? 6.127 32.383 37.332 1.00 40.96 ? 193 SER B CB 1 ATOM 3544 O OG . SER C 3 193 ? 4.787 32.330 37.792 1.00 42.95 ? 193 SER B OG 1 ATOM 3545 N N . ASP C 3 194 ? 5.320 29.191 35.838 1.00 48.74 ? 194 ASP B N 1 ATOM 3546 C CA . ASP C 3 194 ? 4.447 28.502 34.865 1.00 50.81 ? 194 ASP B CA 1 ATOM 3547 C C . ASP C 3 194 ? 3.205 29.239 34.366 1.00 51.64 ? 194 ASP B C 1 ATOM 3548 O O . ASP C 3 194 ? 3.049 29.486 33.168 1.00 52.06 ? 194 ASP B O 1 ATOM 3549 C CB . ASP C 3 194 ? 3.992 27.161 35.441 1.00 52.85 ? 194 ASP B CB 1 ATOM 3550 C CG . ASP C 3 194 ? 5.047 26.089 35.318 1.00 55.86 ? 194 ASP B CG 1 ATOM 3551 O OD1 . ASP C 3 194 ? 5.069 25.179 36.179 1.00 57.18 ? 194 ASP B OD1 1 ATOM 3552 O OD2 . ASP C 3 194 ? 5.844 26.155 34.354 1.00 57.08 ? 194 ASP B OD2 1 ATOM 3553 N N . SER C 3 195 ? 2.299 29.553 35.283 1.00 52.06 ? 195 SER B N 1 ATOM 3554 C CA . SER C 3 195 ? 1.082 30.246 34.905 1.00 52.17 ? 195 SER B CA 1 ATOM 3555 C C . SER C 3 195 ? 1.089 31.630 35.528 1.00 52.90 ? 195 SER B C 1 ATOM 3556 O O . SER C 3 195 ? 1.973 31.956 36.325 1.00 52.25 ? 195 SER B O 1 ATOM 3557 C CB . SER C 3 195 ? -0.142 29.456 35.375 1.00 51.15 ? 195 SER B CB 1 ATOM 3558 N N . ASN C 3 196 ? 0.112 32.445 35.145 1.00 54.00 ? 196 ASN B N 1 ATOM 3559 C CA . ASN C 3 196 ? -0.020 33.787 35.689 1.00 55.02 ? 196 ASN B CA 1 ATOM 3560 C C . ASN C 3 196 ? -1.199 33.730 36.674 1.00 54.92 ? 196 ASN B C 1 ATOM 3561 O O . ASN C 3 196 ? -1.910 34.719 36.897 1.00 54.64 ? 196 ASN B O 1 ATOM 3562 C CB . ASN C 3 196 ? -0.276 34.790 34.558 1.00 56.18 ? 196 ASN B CB 1 ATOM 3563 C CG . ASN C 3 196 ? -1.561 34.511 33.819 1.00 58.88 ? 196 ASN B CG 1 ATOM 3564 O OD1 . ASN C 3 196 ? -1.824 33.371 33.426 1.00 60.40 ? 196 ASN B OD1 1 ATOM 3565 N ND2 . ASN C 3 196 ? -2.376 35.551 33.622 1.00 59.76 ? 196 ASN B ND2 1 ATOM 3566 N N . ILE C 3 197 ? -1.379 32.548 37.266 1.00 55.32 ? 197 ILE B N 1 ATOM 3567 C CA . ILE C 3 197 ? -2.452 32.303 38.222 1.00 55.95 ? 197 ILE B CA 1 ATOM 3568 C C . ILE C 3 197 ? -2.107 32.691 39.662 1.00 56.04 ? 197 ILE B C 1 ATOM 3569 O O . ILE C 3 197 ? -0.975 32.517 40.126 1.00 56.12 ? 197 ILE B O 1 ATOM 3570 C CB . ILE C 3 197 ? -2.910 30.816 38.178 1.00 56.13 ? 197 ILE B CB 1 ATOM 3571 C CG1 . ILE C 3 197 ? -3.575 30.529 36.829 1.00 56.04 ? 197 ILE B CG1 1 ATOM 3572 C CG2 . ILE C 3 197 ? -3.905 30.521 39.313 1.00 55.13 ? 197 ILE B CG2 1 ATOM 3573 C CD1 . ILE C 3 197 ? -4.790 31.413 36.535 1.00 54.65 ? 197 ILE B CD1 1 ATOM 3574 N N . ARG C 3 198 ? -3.126 33.199 40.349 1.00 55.79 ? 198 ARG B N 1 ATOM 3575 C CA . ARG C 3 198 ? -3.055 33.673 41.721 1.00 55.06 ? 198 ARG B CA 1 ATOM 3576 C C . ARG C 3 198 ? -2.380 32.798 42.791 1.00 54.58 ? 198 ARG B C 1 ATOM 3577 O O . ARG C 3 198 ? -2.618 33.009 43.979 1.00 57.33 ? 198 ARG B O 1 ATOM 3578 C CB . ARG C 3 198 ? -4.474 34.046 42.183 1.00 55.15 ? 198 ARG B CB 1 ATOM 3579 C CG . ARG C 3 198 ? -4.534 34.729 43.534 1.00 56.00 ? 198 ARG B CG 1 ATOM 3580 C CD . ARG C 3 198 ? -5.938 35.119 43.949 1.00 56.83 ? 198 ARG B CD 1 ATOM 3581 N NE . ARG C 3 198 ? -5.947 35.510 45.358 1.00 62.40 ? 198 ARG B NE 1 ATOM 3582 C CZ . ARG C 3 198 ? -6.919 36.200 45.951 1.00 64.00 ? 198 ARG B CZ 1 ATOM 3583 N NH1 . ARG C 3 198 ? -7.984 36.588 45.260 1.00 65.57 ? 198 ARG B NH1 1 ATOM 3584 N NH2 . ARG C 3 198 ? -6.825 36.505 47.241 1.00 65.18 ? 198 ARG B NH2 1 ATOM 3585 N N . GLU C 3 199 ? -1.547 31.831 42.412 1.00 52.60 ? 199 GLU B N 1 ATOM 3586 C CA . GLU C 3 199 ? -0.866 31.020 43.427 1.00 49.59 ? 199 GLU B CA 1 ATOM 3587 C C . GLU C 3 199 ? 0.102 29.975 42.915 1.00 48.30 ? 199 GLU B C 1 ATOM 3588 O O . GLU C 3 199 ? 0.526 29.096 43.675 1.00 48.08 ? 199 GLU B O 1 ATOM 3589 C CB . GLU C 3 199 ? -1.871 30.341 44.361 1.00 48.46 ? 199 GLU B CB 1 ATOM 3590 C CG . GLU C 3 199 ? -1.871 30.946 45.755 1.00 48.62 ? 199 GLU B CG 1 ATOM 3591 C CD . GLU C 3 199 ? -2.994 30.435 46.637 1.00 48.36 ? 199 GLU B CD 1 ATOM 3592 O OE1 . GLU C 3 199 ? -2.948 29.259 47.045 1.00 48.69 ? 199 GLU B OE1 1 ATOM 3593 O OE2 . GLU C 3 199 ? -3.927 31.215 46.921 1.00 48.66 ? 199 GLU B OE2 1 ATOM 3594 N N . THR C 3 200 ? 0.464 30.075 41.639 1.00 46.60 ? 200 THR B N 1 ATOM 3595 C CA . THR C 3 200 ? 1.392 29.122 41.048 1.00 44.74 ? 200 THR B CA 1 ATOM 3596 C C . THR C 3 200 ? 2.740 29.205 41.767 1.00 42.56 ? 200 THR B C 1 ATOM 3597 O O . THR C 3 200 ? 3.189 30.290 42.127 1.00 41.86 ? 200 THR B O 1 ATOM 3598 C CB . THR C 3 200 ? 1.564 29.398 39.534 1.00 45.95 ? 200 THR B CB 1 ATOM 3599 O OG1 . THR C 3 200 ? 2.016 30.742 39.338 1.00 48.89 ? 200 THR B OG1 1 ATOM 3600 C CG2 . THR C 3 200 ? 0.232 29.224 38.809 1.00 46.94 ? 200 THR B CG2 1 ATOM 3601 N N . VAL C 3 201 ? 3.375 28.061 41.994 1.00 40.23 ? 201 VAL B N 1 ATOM 3602 C CA . VAL C 3 201 ? 4.666 28.046 42.676 1.00 39.09 ? 201 VAL B CA 1 ATOM 3603 C C . VAL C 3 201 ? 5.826 28.339 41.730 1.00 39.89 ? 201 VAL B C 1 ATOM 3604 O O . VAL C 3 201 ? 6.023 27.645 40.729 1.00 41.34 ? 201 VAL B O 1 ATOM 3605 C CB . VAL C 3 201 ? 4.927 26.689 43.380 1.00 37.25 ? 201 VAL B CB 1 ATOM 3606 C CG1 . VAL C 3 201 ? 6.339 26.644 43.932 1.00 34.13 ? 201 VAL B CG1 1 ATOM 3607 C CG2 . VAL C 3 201 ? 3.933 26.495 44.510 1.00 36.68 ? 201 VAL B CG2 1 ATOM 3608 N N . VAL C 3 202 ? 6.588 29.378 42.063 1.00 39.60 ? 202 VAL B N 1 ATOM 3609 C CA . VAL C 3 202 ? 7.748 29.786 41.278 1.00 38.05 ? 202 VAL B CA 1 ATOM 3610 C C . VAL C 3 202 ? 8.816 28.698 41.342 1.00 38.49 ? 202 VAL B C 1 ATOM 3611 O O . VAL C 3 202 ? 9.104 28.168 42.420 1.00 39.55 ? 202 VAL B O 1 ATOM 3612 C CB . VAL C 3 202 ? 8.347 31.098 41.827 1.00 37.14 ? 202 VAL B CB 1 ATOM 3613 C CG1 . VAL C 3 202 ? 9.601 31.471 41.053 1.00 36.13 ? 202 VAL B CG1 1 ATOM 3614 C CG2 . VAL C 3 202 ? 7.323 32.207 41.740 1.00 34.63 ? 202 VAL B CG2 1 ATOM 3615 N N . LYS C 3 203 ? 9.396 28.358 40.194 1.00 38.20 ? 203 LYS B N 1 ATOM 3616 C CA . LYS C 3 203 ? 10.439 27.337 40.158 1.00 38.49 ? 203 LYS B CA 1 ATOM 3617 C C . LYS C 3 203 ? 11.623 27.744 39.288 1.00 37.21 ? 203 LYS B C 1 ATOM 3618 O O . LYS C 3 203 ? 11.672 28.867 38.794 1.00 37.84 ? 203 LYS B O 1 ATOM 3619 C CB . LYS C 3 203 ? 9.858 26.004 39.679 1.00 40.27 ? 203 LYS B CB 1 ATOM 3620 C CG . LYS C 3 203 ? 8.986 26.093 38.443 1.00 45.32 ? 203 LYS B CG 1 ATOM 3621 C CD . LYS C 3 203 ? 8.041 24.899 38.376 1.00 49.87 ? 203 LYS B CD 1 ATOM 3622 C CE . LYS C 3 203 ? 7.227 24.789 39.674 1.00 52.98 ? 203 LYS B CE 1 ATOM 3623 N NZ . LYS C 3 203 ? 6.328 23.591 39.743 1.00 54.90 ? 203 LYS B NZ 1 ATOM 3624 N N . ILE C 3 204 ? 12.588 26.843 39.128 1.00 36.48 ? 204 ILE B N 1 ATOM 3625 C CA . ILE C 3 204 ? 13.764 27.122 38.305 1.00 35.61 ? 204 ILE B CA 1 ATOM 3626 C C . ILE C 3 204 ? 13.780 26.204 37.072 1.00 37.25 ? 204 ILE B C 1 ATOM 3627 O O . ILE C 3 204 ? 14.064 25.006 37.178 1.00 39.16 ? 204 ILE B O 1 ATOM 3628 C CB . ILE C 3 204 ? 15.090 26.910 39.093 1.00 32.87 ? 204 ILE B CB 1 ATOM 3629 C CG1 . ILE C 3 204 ? 15.157 27.845 40.300 1.00 31.02 ? 204 ILE B CG1 1 ATOM 3630 C CG2 . ILE C 3 204 ? 16.281 27.175 38.190 1.00 30.68 ? 204 ILE B CG2 1 ATOM 3631 C CD1 . ILE C 3 204 ? 15.283 29.292 39.939 1.00 32.46 ? 204 ILE B CD1 1 ATOM 3632 N N . LEU C 3 205 ? 13.462 26.763 35.907 1.00 37.12 ? 205 LEU B N 1 ATOM 3633 C CA . LEU C 3 205 ? 13.457 26.000 34.666 1.00 36.99 ? 205 LEU B CA 1 ATOM 3634 C C . LEU C 3 205 ? 14.489 26.645 33.744 1.00 38.18 ? 205 LEU B C 1 ATOM 3635 O O . LEU C 3 205 ? 15.161 27.587 34.150 1.00 39.43 ? 205 LEU B O 1 ATOM 3636 C CB . LEU C 3 205 ? 12.052 26.018 34.062 1.00 34.58 ? 205 LEU B CB 1 ATOM 3637 C CG . LEU C 3 205 ? 11.008 25.599 35.108 1.00 33.37 ? 205 LEU B CG 1 ATOM 3638 C CD1 . LEU C 3 205 ? 9.610 25.613 34.523 1.00 31.90 ? 205 LEU B CD1 1 ATOM 3639 C CD2 . LEU C 3 205 ? 11.354 24.223 35.631 1.00 33.01 ? 205 LEU B CD2 1 ATOM 3640 N N . SER C 3 206 ? 14.646 26.157 32.519 1.00 38.59 ? 206 SER B N 1 ATOM 3641 C CA . SER C 3 206 ? 15.655 26.757 31.650 1.00 38.79 ? 206 SER B CA 1 ATOM 3642 C C . SER C 3 206 ? 15.153 28.042 31.020 1.00 38.48 ? 206 SER B C 1 ATOM 3643 O O . SER C 3 206 ? 13.969 28.172 30.696 1.00 37.44 ? 206 SER B O 1 ATOM 3644 C CB . SER C 3 206 ? 16.092 25.785 30.548 1.00 40.10 ? 206 SER B CB 1 ATOM 3645 O OG . SER C 3 206 ? 15.275 25.909 29.402 1.00 40.24 ? 206 SER B OG 1 ATOM 3646 N N . CYS C 3 207 ? 16.067 28.990 30.848 1.00 37.50 ? 207 CYS B N 1 ATOM 3647 C CA . CYS C 3 207 ? 15.725 30.275 30.256 1.00 37.48 ? 207 CYS B CA 1 ATOM 3648 C C . CYS C 3 207 ? 15.365 30.116 28.782 1.00 36.08 ? 207 CYS B C 1 ATOM 3649 O O . CYS C 3 207 ? 14.976 31.081 28.130 1.00 37.02 ? 207 CYS B O 1 ATOM 3650 C CB . CYS C 3 207 ? 16.896 31.245 30.375 1.00 37.16 ? 207 CYS B CB 1 ATOM 3651 S SG . CYS C 3 207 ? 17.387 31.744 32.055 1.00 38.86 ? 207 CYS B SG 1 ATOM 3652 N N . GLY C 3 208 ? 15.504 28.899 28.268 1.00 34.58 ? 208 GLY B N 1 ATOM 3653 C CA . GLY C 3 208 ? 15.204 28.626 26.874 1.00 32.93 ? 208 GLY B CA 1 ATOM 3654 C C . GLY C 3 208 ? 14.069 29.419 26.251 1.00 32.42 ? 208 GLY B C 1 ATOM 3655 O O . GLY C 3 208 ? 14.300 30.203 25.338 1.00 32.16 ? 208 GLY B O 1 ATOM 3656 N N . PRO C 3 209 ? 12.827 29.238 26.718 1.00 32.72 ? 209 PRO B N 1 ATOM 3657 C CA . PRO C 3 209 ? 11.691 29.974 26.153 1.00 33.21 ? 209 PRO B CA 1 ATOM 3658 C C . PRO C 3 209 ? 11.707 31.498 26.344 1.00 32.89 ? 209 PRO B C 1 ATOM 3659 O O . PRO C 3 209 ? 11.027 32.218 25.610 1.00 34.22 ? 209 PRO B O 1 ATOM 3660 C CB . PRO C 3 209 ? 10.486 29.306 26.818 1.00 32.48 ? 209 PRO B CB 1 ATOM 3661 C CG . PRO C 3 209 ? 11.029 28.867 28.145 1.00 33.40 ? 209 PRO B CG 1 ATOM 3662 C CD . PRO C 3 209 ? 12.385 28.313 27.778 1.00 33.33 ? 209 PRO B CD 1 ATOM 3663 N N . ALA C 3 210 ? 12.483 31.984 27.311 1.00 32.37 ? 210 ALA B N 1 ATOM 3664 C CA . ALA C 3 210 ? 12.568 33.419 27.579 1.00 31.83 ? 210 ALA B CA 1 ATOM 3665 C C . ALA C 3 210 ? 11.164 33.993 27.673 1.00 32.52 ? 210 ALA B C 1 ATOM 3666 O O . ALA C 3 210 ? 10.922 35.116 27.245 1.00 32.77 ? 210 ALA B O 1 ATOM 3667 C CB . ALA C 3 210 ? 13.339 34.123 26.461 1.00 30.25 ? 210 ALA B CB 1 ATOM 3668 N N . SER C 3 211 ? 10.246 33.212 28.236 1.00 33.03 ? 211 SER B N 1 ATOM 3669 C CA . SER C 3 211 ? 8.844 33.607 28.370 1.00 34.17 ? 211 SER B CA 1 ATOM 3670 C C . SER C 3 211 ? 8.590 34.864 29.196 1.00 34.28 ? 211 SER B C 1 ATOM 3671 O O . SER C 3 211 ? 9.516 35.478 29.728 1.00 34.97 ? 211 SER B O 1 ATOM 3672 C CB . SER C 3 211 ? 8.035 32.452 28.968 1.00 35.27 ? 211 SER B CB 1 ATOM 3673 O OG . SER C 3 211 ? 8.523 32.093 30.253 1.00 36.14 ? 211 SER B OG 1 ATOM 3674 N N . SER C 3 212 ? 7.318 35.237 29.298 1.00 33.41 ? 212 SER B N 1 ATOM 3675 C CA . SER C 3 212 ? 6.918 36.409 30.064 1.00 32.65 ? 212 SER B CA 1 ATOM 3676 C C . SER C 3 212 ? 6.714 36.055 31.534 1.00 31.57 ? 212 SER B C 1 ATOM 3677 O O . SER C 3 212 ? 6.206 36.858 32.317 1.00 31.04 ? 212 SER B O 1 ATOM 3678 C CB . SER C 3 212 ? 5.637 37.006 29.475 1.00 32.84 ? 212 SER B CB 1 ATOM 3679 O OG . SER C 3 212 ? 4.842 36.008 28.857 1.00 33.90 ? 212 SER B OG 1 ATOM 3680 N N . GLY C 3 213 ? 7.113 34.840 31.898 1.00 30.62 ? 213 GLY B N 1 ATOM 3681 C CA . GLY C 3 213 ? 6.992 34.384 33.271 1.00 30.02 ? 213 GLY B CA 1 ATOM 3682 C C . GLY C 3 213 ? 8.378 34.169 33.844 1.00 29.99 ? 213 GLY B C 1 ATOM 3683 O O . GLY C 3 213 ? 8.543 33.547 34.892 1.00 30.06 ? 213 GLY B O 1 ATOM 3684 N N . GLN C 3 214 ? 9.375 34.694 33.135 1.00 30.50 ? 214 GLN B N 1 ATOM 3685 C CA . GLN C 3 214 ? 10.776 34.586 33.528 1.00 30.17 ? 214 GLN B CA 1 ATOM 3686 C C . GLN C 3 214 ? 11.415 35.968 33.628 1.00 30.24 ? 214 GLN B C 1 ATOM 3687 O O . GLN C 3 214 ? 12.620 36.097 33.901 1.00 30.78 ? 214 GLN B O 1 ATOM 3688 C CB . GLN C 3 214 ? 11.536 33.746 32.510 1.00 29.72 ? 214 GLN B CB 1 ATOM 3689 C CG . GLN C 3 214 ? 11.055 32.323 32.442 1.00 29.70 ? 214 GLN B CG 1 ATOM 3690 C CD . GLN C 3 214 ? 11.785 31.528 31.399 1.00 31.13 ? 214 GLN B CD 1 ATOM 3691 O OE1 . GLN C 3 214 ? 11.729 31.847 30.212 1.00 31.81 ? 214 GLN B OE1 1 ATOM 3692 N NE2 . GLN C 3 214 ? 12.483 30.484 31.831 1.00 32.84 ? 214 GLN B NE2 1 ATOM 3693 N N . ARG C 3 215 ? 10.591 36.991 33.400 1.00 28.88 ? 215 ARG B N 1 ATOM 3694 C CA . ARG C 3 215 ? 11.020 38.382 33.461 1.00 27.36 ? 215 ARG B CA 1 ATOM 3695 C C . ARG C 3 215 ? 10.362 39.073 34.644 1.00 27.87 ? 215 ARG B C 1 ATOM 3696 O O . ARG C 3 215 ? 9.136 39.102 34.756 1.00 27.40 ? 215 ARG B O 1 ATOM 3697 C CB . ARG C 3 215 ? 10.646 39.099 32.169 1.00 25.09 ? 215 ARG B CB 1 ATOM 3698 C CG . ARG C 3 215 ? 11.054 40.539 32.102 1.00 21.26 ? 215 ARG B CG 1 ATOM 3699 C CD . ARG C 3 215 ? 10.742 41.063 30.727 1.00 22.55 ? 215 ARG B CD 1 ATOM 3700 N NE . ARG C 3 215 ? 11.039 42.481 30.589 1.00 25.15 ? 215 ARG B NE 1 ATOM 3701 C CZ . ARG C 3 215 ? 10.599 43.240 29.590 1.00 26.36 ? 215 ARG B CZ 1 ATOM 3702 N NH1 . ARG C 3 215 ? 9.840 42.716 28.638 1.00 29.06 ? 215 ARG B NH1 1 ATOM 3703 N NH2 . ARG C 3 215 ? 10.909 44.527 29.548 1.00 26.59 ? 215 ARG B NH2 1 ATOM 3704 N N . TRP C 3 216 ? 11.199 39.622 35.522 1.00 28.71 ? 216 TRP B N 1 ATOM 3705 C CA . TRP C 3 216 ? 10.751 40.315 36.723 1.00 28.86 ? 216 TRP B CA 1 ATOM 3706 C C . TRP C 3 216 ? 11.398 41.694 36.818 1.00 28.94 ? 216 TRP B C 1 ATOM 3707 O O . TRP C 3 216 ? 12.325 42.001 36.071 1.00 28.47 ? 216 TRP B O 1 ATOM 3708 C CB . TRP C 3 216 ? 11.137 39.512 37.966 1.00 30.45 ? 216 TRP B CB 1 ATOM 3709 C CG . TRP C 3 216 ? 10.908 38.046 37.851 1.00 30.26 ? 216 TRP B CG 1 ATOM 3710 C CD1 . TRP C 3 216 ? 11.661 37.155 37.152 1.00 31.21 ? 216 TRP B CD1 1 ATOM 3711 C CD2 . TRP C 3 216 ? 9.844 37.297 38.445 1.00 30.30 ? 216 TRP B CD2 1 ATOM 3712 N NE1 . TRP C 3 216 ? 11.134 35.891 37.272 1.00 31.44 ? 216 TRP B NE1 1 ATOM 3713 C CE2 . TRP C 3 216 ? 10.018 35.952 38.060 1.00 30.50 ? 216 TRP B CE2 1 ATOM 3714 C CE3 . TRP C 3 216 ? 8.758 37.634 39.264 1.00 30.08 ? 216 TRP B CE3 1 ATOM 3715 C CZ2 . TRP C 3 216 ? 9.146 34.940 38.468 1.00 31.51 ? 216 TRP B CZ2 1 ATOM 3716 C CZ3 . TRP C 3 216 ? 7.894 36.631 39.668 1.00 30.83 ? 216 TRP B CZ3 1 ATOM 3717 C CH2 . TRP C 3 216 ? 8.092 35.299 39.270 1.00 31.89 ? 216 TRP B CH2 1 ATOM 3718 N N . MET C 3 217 ? 10.909 42.512 37.751 1.00 29.46 ? 217 MET B N 1 ATOM 3719 C CA . MET C 3 217 ? 11.440 43.858 37.974 1.00 29.68 ? 217 MET B CA 1 ATOM 3720 C C . MET C 3 217 ? 11.407 44.212 39.462 1.00 30.94 ? 217 MET B C 1 ATOM 3721 O O . MET C 3 217 ? 10.437 43.898 40.145 1.00 31.79 ? 217 MET B O 1 ATOM 3722 C CB . MET C 3 217 ? 10.615 44.902 37.218 1.00 26.65 ? 217 MET B CB 1 ATOM 3723 C CG . MET C 3 217 ? 11.225 46.290 37.280 1.00 25.13 ? 217 MET B CG 1 ATOM 3724 S SD . MET C 3 217 ? 10.056 47.596 36.935 1.00 24.58 ? 217 MET B SD 1 ATOM 3725 C CE . MET C 3 217 ? 10.963 49.025 37.473 1.00 24.65 ? 217 MET B CE 1 ATOM 3726 N N . PHE C 3 218 ? 12.462 44.858 39.963 1.00 32.23 ? 218 PHE B N 1 ATOM 3727 C CA . PHE C 3 218 ? 12.508 45.276 41.373 1.00 32.99 ? 218 PHE B CA 1 ATOM 3728 C C . PHE C 3 218 ? 11.856 46.652 41.512 1.00 31.83 ? 218 PHE B C 1 ATOM 3729 O O . PHE C 3 218 ? 12.380 47.650 41.005 1.00 32.38 ? 218 PHE B O 1 ATOM 3730 C CB . PHE C 3 218 ? 13.952 45.363 41.894 1.00 34.45 ? 218 PHE B CB 1 ATOM 3731 C CG . PHE C 3 218 ? 14.528 44.042 42.335 1.00 35.97 ? 218 PHE B CG 1 ATOM 3732 C CD1 . PHE C 3 218 ? 14.996 43.124 41.401 1.00 36.21 ? 218 PHE B CD1 1 ATOM 3733 C CD2 . PHE C 3 218 ? 14.590 43.711 43.690 1.00 36.74 ? 218 PHE B CD2 1 ATOM 3734 C CE1 . PHE C 3 218 ? 15.521 41.893 41.804 1.00 36.93 ? 218 PHE B CE1 1 ATOM 3735 C CE2 . PHE C 3 218 ? 15.112 42.481 44.105 1.00 36.34 ? 218 PHE B CE2 1 ATOM 3736 C CZ . PHE C 3 218 ? 15.578 41.571 43.158 1.00 36.56 ? 218 PHE B CZ 1 ATOM 3737 N N . LYS C 3 219 ? 10.722 46.706 42.204 1.00 29.85 ? 219 LYS B N 1 ATOM 3738 C CA . LYS C 3 219 ? 10.009 47.963 42.379 1.00 29.42 ? 219 LYS B CA 1 ATOM 3739 C C . LYS C 3 219 ? 10.615 48.806 43.483 1.00 28.38 ? 219 LYS B C 1 ATOM 3740 O O . LYS C 3 219 ? 11.427 48.325 44.272 1.00 29.48 ? 219 LYS B O 1 ATOM 3741 C CB . LYS C 3 219 ? 8.538 47.706 42.695 1.00 30.67 ? 219 LYS B CB 1 ATOM 3742 C CG . LYS C 3 219 ? 7.860 46.775 41.725 1.00 33.72 ? 219 LYS B CG 1 ATOM 3743 C CD . LYS C 3 219 ? 7.967 47.275 40.296 1.00 36.53 ? 219 LYS B CD 1 ATOM 3744 C CE . LYS C 3 219 ? 7.125 48.514 40.060 1.00 38.64 ? 219 LYS B CE 1 ATOM 3745 N NZ . LYS C 3 219 ? 7.187 48.905 38.618 1.00 42.34 ? 219 LYS B NZ 1 ATOM 3746 N N . ASN C 3 220 ? 10.214 50.069 43.538 1.00 26.21 ? 220 ASN B N 1 ATOM 3747 C CA . ASN C 3 220 ? 10.731 50.954 44.558 1.00 25.17 ? 220 ASN B CA 1 ATOM 3748 C C . ASN C 3 220 ? 10.192 50.563 45.922 1.00 24.94 ? 220 ASN B C 1 ATOM 3749 O O . ASN C 3 220 ? 10.793 50.880 46.947 1.00 24.40 ? 220 ASN B O 1 ATOM 3750 C CB . ASN C 3 220 ? 10.342 52.399 44.269 1.00 26.20 ? 220 ASN B CB 1 ATOM 3751 C CG . ASN C 3 220 ? 11.001 53.374 45.224 1.00 28.01 ? 220 ASN B CG 1 ATOM 3752 O OD1 . ASN C 3 220 ? 12.201 53.647 45.121 1.00 27.77 ? 220 ASN B OD1 1 ATOM 3753 N ND2 . ASN C 3 220 ? 10.225 53.887 46.178 1.00 27.88 ? 220 ASN B ND2 1 ATOM 3754 N N . ASP C 3 221 ? 9.055 49.875 45.941 1.00 24.86 ? 221 ASP B N 1 ATOM 3755 C CA . ASP C 3 221 ? 8.456 49.476 47.205 1.00 24.38 ? 221 ASP B CA 1 ATOM 3756 C C . ASP C 3 221 ? 9.011 48.175 47.752 1.00 24.12 ? 221 ASP B C 1 ATOM 3757 O O . ASP C 3 221 ? 8.437 47.582 48.660 1.00 24.62 ? 221 ASP B O 1 ATOM 3758 C CB . ASP C 3 221 ? 6.926 49.404 47.086 1.00 24.98 ? 221 ASP B CB 1 ATOM 3759 C CG . ASP C 3 221 ? 6.456 48.403 46.053 1.00 27.84 ? 221 ASP B CG 1 ATOM 3760 O OD1 . ASP C 3 221 ? 7.266 47.550 45.642 1.00 31.01 ? 221 ASP B OD1 1 ATOM 3761 O OD2 . ASP C 3 221 ? 5.267 48.457 45.663 1.00 27.75 ? 221 ASP B OD2 1 ATOM 3762 N N . GLY C 3 222 ? 10.134 47.734 47.197 1.00 24.01 ? 222 GLY B N 1 ATOM 3763 C CA . GLY C 3 222 ? 10.765 46.511 47.668 1.00 24.97 ? 222 GLY B CA 1 ATOM 3764 C C . GLY C 3 222 ? 10.154 45.179 47.258 1.00 25.98 ? 222 GLY B C 1 ATOM 3765 O O . GLY C 3 222 ? 10.517 44.145 47.814 1.00 27.51 ? 222 GLY B O 1 ATOM 3766 N N . THR C 3 223 ? 9.223 45.186 46.310 1.00 25.64 ? 223 THR B N 1 ATOM 3767 C CA . THR C 3 223 ? 8.615 43.945 45.841 1.00 24.65 ? 223 THR B CA 1 ATOM 3768 C C . THR C 3 223 ? 9.348 43.562 44.561 1.00 24.73 ? 223 THR B C 1 ATOM 3769 O O . THR C 3 223 ? 10.160 44.339 44.049 1.00 26.24 ? 223 THR B O 1 ATOM 3770 C CB . THR C 3 223 ? 7.105 44.119 45.505 1.00 24.50 ? 223 THR B CB 1 ATOM 3771 O OG1 . THR C 3 223 ? 6.951 45.085 44.455 1.00 22.15 ? 223 THR B OG1 1 ATOM 3772 C CG2 . THR C 3 223 ? 6.328 44.581 46.726 1.00 23.02 ? 223 THR B CG2 1 ATOM 3773 N N . ILE C 3 224 ? 9.082 42.357 44.068 1.00 23.80 ? 224 ILE B N 1 ATOM 3774 C CA . ILE C 3 224 ? 9.676 41.869 42.828 1.00 22.14 ? 224 ILE B CA 1 ATOM 3775 C C . ILE C 3 224 ? 8.473 41.553 41.950 1.00 22.51 ? 224 ILE B C 1 ATOM 3776 O O . ILE C 3 224 ? 7.800 40.538 42.140 1.00 23.28 ? 224 ILE B O 1 ATOM 3777 C CB . ILE C 3 224 ? 10.503 40.597 43.053 1.00 20.80 ? 224 ILE B CB 1 ATOM 3778 C CG1 . ILE C 3 224 ? 11.691 40.909 43.963 1.00 18.82 ? 224 ILE B CG1 1 ATOM 3779 C CG2 . ILE C 3 224 ? 10.990 40.058 41.726 1.00 21.32 ? 224 ILE B CG2 1 ATOM 3780 C CD1 . ILE C 3 224 ? 12.632 39.751 44.138 1.00 18.10 ? 224 ILE B CD1 1 ATOM 3781 N N . LEU C 3 225 ? 8.204 42.438 40.997 1.00 22.46 ? 225 LEU B N 1 ATOM 3782 C CA . LEU C 3 225 ? 7.053 42.323 40.107 1.00 22.33 ? 225 LEU B CA 1 ATOM 3783 C C . LEU C 3 225 ? 7.236 41.524 38.815 1.00 24.36 ? 225 LEU B C 1 ATOM 3784 O O . LEU C 3 225 ? 8.252 41.645 38.139 1.00 25.52 ? 225 LEU B O 1 ATOM 3785 C CB . LEU C 3 225 ? 6.575 43.731 39.748 1.00 18.26 ? 225 LEU B CB 1 ATOM 3786 C CG . LEU C 3 225 ? 5.475 43.819 38.695 1.00 15.96 ? 225 LEU B CG 1 ATOM 3787 C CD1 . LEU C 3 225 ? 4.135 43.530 39.356 1.00 15.59 ? 225 LEU B CD1 1 ATOM 3788 C CD2 . LEU C 3 225 ? 5.493 45.186 38.049 1.00 12.21 ? 225 LEU B CD2 1 ATOM 3789 N N . ASN C 3 226 ? 6.239 40.711 38.479 1.00 25.91 ? 226 ASN B N 1 ATOM 3790 C CA . ASN C 3 226 ? 6.264 39.937 37.243 1.00 27.96 ? 226 ASN B CA 1 ATOM 3791 C C . ASN C 3 226 ? 5.520 40.810 36.240 1.00 29.58 ? 226 ASN B C 1 ATOM 3792 O O . ASN C 3 226 ? 4.297 40.742 36.130 1.00 30.01 ? 226 ASN B O 1 ATOM 3793 C CB . ASN C 3 226 ? 5.530 38.600 37.418 1.00 27.50 ? 226 ASN B CB 1 ATOM 3794 C CG . ASN C 3 226 ? 5.395 37.835 36.114 1.00 27.11 ? 226 ASN B CG 1 ATOM 3795 O OD1 . ASN C 3 226 ? 6.391 37.511 35.466 1.00 26.82 ? 226 ASN B OD1 1 ATOM 3796 N ND2 . ASN C 3 226 ? 4.159 37.548 35.719 1.00 25.96 ? 226 ASN B ND2 1 ATOM 3797 N N . LEU C 3 227 ? 6.265 41.559 35.495 1.00 27.12 ? 227 LEU B N 1 ATOM 3798 C CA . LEU C 3 227 ? 5.689 42.479 34.527 1.00 29.57 ? 227 LEU B CA 1 ATOM 3799 C C . LEU C 3 227 ? 4.458 42.008 33.769 1.00 31.78 ? 227 LEU B C 1 ATOM 3800 O O . LEU C 3 227 ? 3.442 42.707 33.746 1.00 33.43 ? 227 LEU B O 1 ATOM 3801 C CB . LEU C 3 227 ? 6.766 42.992 33.544 1.00 27.87 ? 227 LEU B CB 1 ATOM 3802 C CG . LEU C 3 227 ? 7.788 43.942 34.195 1.00 26.64 ? 227 LEU B CG 1 ATOM 3803 C CD1 . LEU C 3 227 ? 8.701 44.512 33.150 1.00 26.31 ? 227 LEU B CD1 1 ATOM 3804 C CD2 . LEU C 3 227 ? 7.056 45.054 34.916 1.00 27.45 ? 227 LEU B CD2 1 ATOM 3805 N N . TYR C 3 228 ? 4.474 40.904 33.207 1.00 35.55 ? 228 TYR B N 1 ATOM 3806 C CA . TYR C 3 228 ? 3.307 40.444 32.463 1.00 34.79 ? 228 TYR B CA 1 ATOM 3807 C C . TYR C 3 228 ? 2.007 40.225 33.242 1.00 33.53 ? 228 TYR B C 1 ATOM 3808 O O . TYR C 3 228 ? 0.947 40.679 32.815 1.00 33.32 ? 228 TYR B O 1 ATOM 3809 C CB . TYR C 3 228 ? 3.622 39.159 31.700 1.00 37.29 ? 228 TYR B CB 1 ATOM 3810 C CG . TYR C 3 228 ? 2.448 38.682 30.869 1.00 39.61 ? 228 TYR B CG 1 ATOM 3811 C CD1 . TYR C 3 228 ? 2.004 39.424 29.777 1.00 40.90 ? 228 TYR B CD1 1 ATOM 3812 C CD2 . TYR C 3 228 ? 1.754 37.514 31.198 1.00 41.26 ? 228 TYR B CD2 1 ATOM 3813 C CE1 . TYR C 3 228 ? 0.903 39.025 29.031 1.00 41.76 ? 228 TYR B CE1 1 ATOM 3814 C CE2 . TYR C 3 228 ? 0.643 37.103 30.456 1.00 41.72 ? 228 TYR B CE2 1 ATOM 3815 C CZ . TYR C 3 228 ? 0.228 37.867 29.373 1.00 42.26 ? 228 TYR B CZ 1 ATOM 3816 O OH . TYR C 3 228 ? -0.859 37.487 28.620 1.00 43.29 ? 228 TYR B OH 1 ATOM 3817 N N . SER C 3 229 ? 2.077 39.525 34.370 1.00 31.98 ? 229 SER B N 1 ATOM 3818 C CA . SER C 3 229 ? 0.877 39.223 35.151 1.00 30.56 ? 229 SER B CA 1 ATOM 3819 C C . SER C 3 229 ? 0.482 40.253 36.201 1.00 31.23 ? 229 SER B C 1 ATOM 3820 O O . SER C 3 229 ? -0.679 40.320 36.603 1.00 32.22 ? 229 SER B O 1 ATOM 3821 C CB . SER C 3 229 ? 1.028 37.859 35.832 1.00 28.81 ? 229 SER B CB 1 ATOM 3822 O OG . SER C 3 229 ? 2.019 37.887 36.841 1.00 26.20 ? 229 SER B OG 1 ATOM 3823 N N . GLY C 3 230 ? 1.444 41.048 36.655 1.00 30.98 ? 230 GLY B N 1 ATOM 3824 C CA . GLY C 3 230 ? 1.143 42.042 37.666 1.00 30.61 ? 230 GLY B CA 1 ATOM 3825 C C . GLY C 3 230 ? 1.227 41.469 39.068 1.00 30.59 ? 230 GLY B C 1 ATOM 3826 O O . GLY C 3 230 ? 0.969 42.172 40.040 1.00 31.47 ? 230 GLY B O 1 ATOM 3827 N N . LEU C 3 231 ? 1.584 40.193 39.177 1.00 29.73 ? 231 LEU B N 1 ATOM 3828 C CA . LEU C 3 231 ? 1.709 39.535 40.477 1.00 28.68 ? 231 LEU B CA 1 ATOM 3829 C C . LEU C 3 231 ? 3.150 39.643 40.971 1.00 28.68 ? 231 LEU B C 1 ATOM 3830 O O . LEU C 3 231 ? 4.084 39.674 40.170 1.00 27.59 ? 231 LEU B O 1 ATOM 3831 C CB . LEU C 3 231 ? 1.303 38.061 40.371 1.00 26.98 ? 231 LEU B CB 1 ATOM 3832 C CG . LEU C 3 231 ? -0.138 37.806 39.927 1.00 24.16 ? 231 LEU B CG 1 ATOM 3833 C CD1 . LEU C 3 231 ? -0.340 36.332 39.677 1.00 23.58 ? 231 LEU B CD1 1 ATOM 3834 C CD2 . LEU C 3 231 ? -1.091 38.309 40.983 1.00 21.79 ? 231 LEU B CD2 1 ATOM 3835 N N . VAL C 3 232 ? 3.318 39.693 42.290 1.00 27.78 ? 232 VAL B N 1 ATOM 3836 C CA . VAL C 3 232 ? 4.635 39.834 42.911 1.00 28.03 ? 232 VAL B CA 1 ATOM 3837 C C . VAL C 3 232 ? 5.098 38.587 43.671 1.00 29.48 ? 232 VAL B C 1 ATOM 3838 O O . VAL C 3 232 ? 4.275 37.785 44.096 1.00 30.27 ? 232 VAL B O 1 ATOM 3839 C CB . VAL C 3 232 ? 4.621 41.007 43.895 1.00 27.43 ? 232 VAL B CB 1 ATOM 3840 C CG1 . VAL C 3 232 ? 4.083 42.253 43.203 1.00 24.65 ? 232 VAL B CG1 1 ATOM 3841 C CG2 . VAL C 3 232 ? 3.770 40.651 45.098 1.00 25.42 ? 232 VAL B CG2 1 ATOM 3842 N N . LEU C 3 233 ? 6.410 38.423 43.845 1.00 30.28 ? 233 LEU B N 1 ATOM 3843 C CA . LEU C 3 233 ? 6.924 37.264 44.577 1.00 31.42 ? 233 LEU B CA 1 ATOM 3844 C C . LEU C 3 233 ? 6.357 37.305 45.974 1.00 33.45 ? 233 LEU B C 1 ATOM 3845 O O . LEU C 3 233 ? 6.381 38.355 46.622 1.00 37.56 ? 233 LEU B O 1 ATOM 3846 C CB . LEU C 3 233 ? 8.444 37.282 44.657 1.00 30.14 ? 233 LEU B CB 1 ATOM 3847 C CG . LEU C 3 233 ? 9.180 36.581 43.522 1.00 29.81 ? 233 LEU B CG 1 ATOM 3848 C CD1 . LEU C 3 233 ? 10.603 36.304 43.970 1.00 27.40 ? 233 LEU B CD1 1 ATOM 3849 C CD2 . LEU C 3 233 ? 8.473 35.281 43.165 1.00 29.03 ? 233 LEU B CD2 1 ATOM 3850 N N . ASP C 3 234 ? 5.881 36.157 46.447 1.00 33.90 ? 234 ASP B N 1 ATOM 3851 C CA . ASP C 3 234 ? 5.233 36.057 47.752 1.00 33.00 ? 234 ASP B CA 1 ATOM 3852 C C . ASP C 3 234 ? 5.596 34.781 48.494 1.00 33.88 ? 234 ASP B C 1 ATOM 3853 O O . ASP C 3 234 ? 5.411 33.696 47.958 1.00 34.99 ? 234 ASP B O 1 ATOM 3854 C CB . ASP C 3 234 ? 3.719 36.093 47.518 1.00 32.51 ? 234 ASP B CB 1 ATOM 3855 C CG . ASP C 3 234 ? 2.911 35.946 48.788 1.00 34.60 ? 234 ASP B CG 1 ATOM 3856 O OD1 . ASP C 3 234 ? 3.092 34.951 49.525 1.00 35.03 ? 234 ASP B OD1 1 ATOM 3857 O OD2 . ASP C 3 234 ? 2.070 36.835 49.037 1.00 36.51 ? 234 ASP B OD2 1 ATOM 3858 N N . VAL C 3 235 ? 6.101 34.898 49.720 1.00 34.35 ? 235 VAL B N 1 ATOM 3859 C CA . VAL C 3 235 ? 6.433 33.707 50.501 1.00 35.42 ? 235 VAL B CA 1 ATOM 3860 C C . VAL C 3 235 ? 5.128 33.185 51.109 1.00 37.43 ? 235 VAL B C 1 ATOM 3861 O O . VAL C 3 235 ? 4.544 33.811 51.994 1.00 38.07 ? 235 VAL B O 1 ATOM 3862 C CB . VAL C 3 235 ? 7.442 34.016 51.611 1.00 34.89 ? 235 VAL B CB 1 ATOM 3863 C CG1 . VAL C 3 235 ? 7.746 32.749 52.383 1.00 36.63 ? 235 VAL B CG1 1 ATOM 3864 C CG2 . VAL C 3 235 ? 8.727 34.575 51.009 1.00 34.14 ? 235 VAL B CG2 1 ATOM 3865 N N . ARG C 3 236 ? 4.685 32.029 50.620 1.00 39.87 ? 236 ARG B N 1 ATOM 3866 C CA . ARG C 3 236 ? 3.419 31.412 51.024 1.00 42.24 ? 236 ARG B CA 1 ATOM 3867 C C . ARG C 3 236 ? 3.028 31.429 52.500 1.00 41.46 ? 236 ARG B C 1 ATOM 3868 O O . ARG C 3 236 ? 3.634 30.752 53.335 1.00 41.30 ? 236 ARG B O 1 ATOM 3869 C CB . ARG C 3 236 ? 3.349 29.976 50.497 1.00 43.76 ? 236 ARG B CB 1 ATOM 3870 C CG . ARG C 3 236 ? 1.940 29.427 50.468 1.00 46.72 ? 236 ARG B CG 1 ATOM 3871 C CD . ARG C 3 236 ? 1.854 28.192 49.608 1.00 49.89 ? 236 ARG B CD 1 ATOM 3872 N NE . ARG C 3 236 ? 0.525 28.040 49.030 1.00 54.80 ? 236 ARG B NE 1 ATOM 3873 C CZ . ARG C 3 236 ? 0.266 27.300 47.956 1.00 56.52 ? 236 ARG B CZ 1 ATOM 3874 N NH1 . ARG C 3 236 ? 1.252 26.643 47.350 1.00 58.09 ? 236 ARG B NH1 1 ATOM 3875 N NH2 . ARG C 3 236 ? -0.971 27.232 47.470 1.00 55.58 ? 236 ARG B NH2 1 ATOM 3876 N N . ALA C 3 237 ? 1.986 32.201 52.801 1.00 40.55 ? 237 ALA B N 1 ATOM 3877 C CA . ALA C 3 237 ? 1.478 32.324 54.159 1.00 38.99 ? 237 ALA B CA 1 ATOM 3878 C C . ALA C 3 237 ? 2.619 32.591 55.141 1.00 39.68 ? 237 ALA B C 1 ATOM 3879 O O . ALA C 3 237 ? 2.816 31.820 56.081 1.00 40.54 ? 237 ALA B O 1 ATOM 3880 C CB . ALA C 3 237 ? 0.743 31.048 54.538 1.00 37.53 ? 237 ALA B CB 1 ATOM 3881 N N . SER C 3 238 ? 3.365 33.676 54.917 1.00 39.26 ? 238 SER B N 1 ATOM 3882 C CA . SER C 3 238 ? 4.503 34.045 55.766 1.00 38.19 ? 238 SER B CA 1 ATOM 3883 C C . SER C 3 238 ? 5.142 32.846 56.455 1.00 38.81 ? 238 SER B C 1 ATOM 3884 O O . SER C 3 238 ? 5.550 32.929 57.610 1.00 38.93 ? 238 SER B O 1 ATOM 3885 C CB . SER C 3 238 ? 4.062 35.057 56.815 1.00 36.55 ? 238 SER B CB 1 ATOM 3886 O OG . SER C 3 238 ? 3.800 36.301 56.205 1.00 37.62 ? 238 SER B OG 1 ATOM 3887 N N . ASP C 3 239 ? 5.245 31.737 55.730 1.00 39.63 ? 239 ASP B N 1 ATOM 3888 C CA . ASP C 3 239 ? 5.798 30.515 56.290 1.00 40.98 ? 239 ASP B CA 1 ATOM 3889 C C . ASP C 3 239 ? 7.034 30.007 55.538 1.00 41.26 ? 239 ASP B C 1 ATOM 3890 O O . ASP C 3 239 ? 6.927 29.252 54.567 1.00 40.98 ? 239 ASP B O 1 ATOM 3891 C CB . ASP C 3 239 ? 4.712 29.431 56.290 1.00 42.33 ? 239 ASP B CB 1 ATOM 3892 C CG . ASP C 3 239 ? 4.949 28.358 57.345 1.00 44.16 ? 239 ASP B CG 1 ATOM 3893 O OD1 . ASP C 3 239 ? 6.122 27.993 57.573 1.00 43.25 ? 239 ASP B OD1 1 ATOM 3894 O OD2 . ASP C 3 239 ? 3.954 27.874 57.934 1.00 44.31 ? 239 ASP B OD2 1 ATOM 3895 N N . PRO C 3 240 ? 8.229 30.418 55.979 1.00 41.43 ? 240 PRO B N 1 ATOM 3896 C CA . PRO C 3 240 ? 9.448 29.965 55.310 1.00 42.54 ? 240 PRO B CA 1 ATOM 3897 C C . PRO C 3 240 ? 9.542 28.439 55.305 1.00 43.77 ? 240 PRO B C 1 ATOM 3898 O O . PRO C 3 240 ? 10.168 27.845 54.425 1.00 44.27 ? 240 PRO B O 1 ATOM 3899 C CB . PRO C 3 240 ? 10.553 30.597 56.153 1.00 41.06 ? 240 PRO B CB 1 ATOM 3900 C CG . PRO C 3 240 ? 9.935 31.858 56.612 1.00 41.16 ? 240 PRO B CG 1 ATOM 3901 C CD . PRO C 3 240 ? 8.546 31.419 57.010 1.00 41.85 ? 240 PRO B CD 1 ATOM 3902 N N . SER C 3 241 ? 8.919 27.811 56.296 1.00 45.52 ? 241 SER B N 1 ATOM 3903 C CA . SER C 3 241 ? 8.961 26.363 56.416 1.00 46.23 ? 241 SER B CA 1 ATOM 3904 C C . SER C 3 241 ? 8.358 25.682 55.203 1.00 45.26 ? 241 SER B C 1 ATOM 3905 O O . SER C 3 241 ? 8.940 24.734 54.683 1.00 47.04 ? 241 SER B O 1 ATOM 3906 C CB . SER C 3 241 ? 8.218 25.897 57.671 1.00 48.09 ? 241 SER B CB 1 ATOM 3907 O OG . SER C 3 241 ? 6.842 25.686 57.396 1.00 49.93 ? 241 SER B OG 1 ATOM 3908 N N . LEU C 3 242 ? 7.198 26.155 54.754 1.00 43.67 ? 242 LEU B N 1 ATOM 3909 C CA . LEU C 3 242 ? 6.534 25.558 53.595 1.00 42.18 ? 242 LEU B CA 1 ATOM 3910 C C . LEU C 3 242 ? 7.437 25.412 52.361 1.00 41.44 ? 242 LEU B C 1 ATOM 3911 O O . LEU C 3 242 ? 7.143 24.622 51.463 1.00 41.02 ? 242 LEU B O 1 ATOM 3912 C CB . LEU C 3 242 ? 5.288 26.368 53.219 1.00 40.92 ? 242 LEU B CB 1 ATOM 3913 C CG . LEU C 3 242 ? 4.050 26.261 54.113 1.00 39.10 ? 242 LEU B CG 1 ATOM 3914 C CD1 . LEU C 3 242 ? 2.970 27.176 53.580 1.00 39.42 ? 242 LEU B CD1 1 ATOM 3915 C CD2 . LEU C 3 242 ? 3.546 24.834 54.140 1.00 37.93 ? 242 LEU B CD2 1 ATOM 3916 N N . LYS C 3 243 ? 8.532 26.166 52.323 1.00 41.76 ? 243 LYS B N 1 ATOM 3917 C CA . LYS C 3 243 ? 9.465 26.117 51.201 1.00 41.44 ? 243 LYS B CA 1 ATOM 3918 C C . LYS C 3 243 ? 8.766 26.333 49.869 1.00 41.19 ? 243 LYS B C 1 ATOM 3919 O O . LYS C 3 243 ? 8.943 25.549 48.938 1.00 41.26 ? 243 LYS B O 1 ATOM 3920 C CB . LYS C 3 243 ? 10.203 24.776 51.163 1.00 41.95 ? 243 LYS B CB 1 ATOM 3921 C CG . LYS C 3 243 ? 11.290 24.626 52.200 1.00 43.62 ? 243 LYS B CG 1 ATOM 3922 C CD . LYS C 3 243 ? 11.993 23.289 52.038 1.00 47.42 ? 243 LYS B CD 1 ATOM 3923 C CE . LYS C 3 243 ? 13.092 23.094 53.082 1.00 49.91 ? 243 LYS B CE 1 ATOM 3924 N NZ . LYS C 3 243 ? 14.247 24.026 52.879 1.00 52.38 ? 243 LYS B NZ 1 ATOM 3925 N N . GLN C 3 244 ? 7.969 27.393 49.775 1.00 41.29 ? 244 GLN B N 1 ATOM 3926 C CA . GLN C 3 244 ? 7.268 27.686 48.531 1.00 40.75 ? 244 GLN B CA 1 ATOM 3927 C C . GLN C 3 244 ? 7.080 29.172 48.262 1.00 39.82 ? 244 GLN B C 1 ATOM 3928 O O . GLN C 3 244 ? 6.422 29.867 49.036 1.00 40.36 ? 244 GLN B O 1 ATOM 3929 C CB . GLN C 3 244 ? 5.890 27.020 48.510 1.00 41.45 ? 244 GLN B CB 1 ATOM 3930 C CG . GLN C 3 244 ? 5.908 25.506 48.577 1.00 42.38 ? 244 GLN B CG 1 ATOM 3931 C CD . GLN C 3 244 ? 4.673 24.887 47.949 1.00 42.59 ? 244 GLN B CD 1 ATOM 3932 O OE1 . GLN C 3 244 ? 3.583 25.472 47.973 1.00 41.43 ? 244 GLN B OE1 1 ATOM 3933 N NE2 . GLN C 3 244 ? 4.834 23.691 47.390 1.00 41.35 ? 244 GLN B NE2 1 ATOM 3934 N N . ILE C 3 245 ? 7.660 29.647 47.162 1.00 37.98 ? 245 ILE B N 1 ATOM 3935 C CA . ILE C 3 245 ? 7.520 31.041 46.764 1.00 35.99 ? 245 ILE B CA 1 ATOM 3936 C C . ILE C 3 245 ? 6.477 31.023 45.662 1.00 35.07 ? 245 ILE B C 1 ATOM 3937 O O . ILE C 3 245 ? 6.642 30.333 44.658 1.00 36.67 ? 245 ILE B O 1 ATOM 3938 C CB . ILE C 3 245 ? 8.835 31.620 46.209 1.00 34.60 ? 245 ILE B CB 1 ATOM 3939 C CG1 . ILE C 3 245 ? 9.948 31.444 47.242 1.00 34.35 ? 245 ILE B CG1 1 ATOM 3940 C CG2 . ILE C 3 245 ? 8.656 33.093 45.864 1.00 31.86 ? 245 ILE B CG2 1 ATOM 3941 C CD1 . ILE C 3 245 ? 9.610 31.995 48.608 1.00 34.01 ? 245 ILE B CD1 1 ATOM 3942 N N . ILE C 3 246 ? 5.400 31.775 45.859 1.00 33.15 ? 246 ILE B N 1 ATOM 3943 C CA . ILE C 3 246 ? 4.314 31.820 44.895 1.00 31.55 ? 246 ILE B CA 1 ATOM 3944 C C . ILE C 3 246 ? 4.150 33.204 44.295 1.00 31.20 ? 246 ILE B C 1 ATOM 3945 O O . ILE C 3 246 ? 4.756 34.168 44.743 1.00 30.80 ? 246 ILE B O 1 ATOM 3946 C CB . ILE C 3 246 ? 2.957 31.439 45.555 1.00 31.42 ? 246 ILE B CB 1 ATOM 3947 C CG1 . ILE C 3 246 ? 2.565 32.509 46.574 1.00 31.18 ? 246 ILE B CG1 1 ATOM 3948 C CG2 . ILE C 3 246 ? 3.057 30.091 46.258 1.00 29.63 ? 246 ILE B CG2 1 ATOM 3949 C CD1 . ILE C 3 246 ? 1.145 32.411 47.069 1.00 32.74 ? 246 ILE B CD1 1 ATOM 3950 N N . LEU C 3 247 ? 3.318 33.277 43.266 1.00 31.91 ? 247 LEU B N 1 ATOM 3951 C CA . LEU C 3 247 ? 2.988 34.525 42.595 1.00 32.82 ? 247 LEU B CA 1 ATOM 3952 C C . LEU C 3 247 ? 1.680 34.904 43.290 1.00 33.45 ? 247 LEU B C 1 ATOM 3953 O O . LEU C 3 247 ? 0.769 34.078 43.404 1.00 34.37 ? 247 LEU B O 1 ATOM 3954 C CB . LEU C 3 247 ? 2.741 34.265 41.114 1.00 32.65 ? 247 LEU B CB 1 ATOM 3955 C CG . LEU C 3 247 ? 3.388 35.203 40.105 1.00 32.97 ? 247 LEU B CG 1 ATOM 3956 C CD1 . LEU C 3 247 ? 4.895 35.174 40.269 1.00 31.71 ? 247 LEU B CD1 1 ATOM 3957 C CD2 . LEU C 3 247 ? 2.993 34.763 38.711 1.00 31.59 ? 247 LEU B CD2 1 ATOM 3958 N N . TYR C 3 248 ? 1.574 36.134 43.768 1.00 33.51 ? 248 TYR B N 1 ATOM 3959 C CA . TYR C 3 248 ? 0.370 36.534 44.479 1.00 33.15 ? 248 TYR B CA 1 ATOM 3960 C C . TYR C 3 248 ? 0.121 38.020 44.276 1.00 32.12 ? 248 TYR B C 1 ATOM 3961 O O . TYR C 3 248 ? 1.055 38.781 44.053 1.00 32.54 ? 248 TYR B O 1 ATOM 3962 C CB . TYR C 3 248 ? 0.556 36.228 45.969 1.00 35.56 ? 248 TYR B CB 1 ATOM 3963 C CG . TYR C 3 248 ? -0.723 36.103 46.756 1.00 40.06 ? 248 TYR B CG 1 ATOM 3964 C CD1 . TYR C 3 248 ? -1.557 34.996 46.599 1.00 41.50 ? 248 TYR B CD1 1 ATOM 3965 C CD2 . TYR C 3 248 ? -1.121 37.108 47.636 1.00 41.53 ? 248 TYR B CD2 1 ATOM 3966 C CE1 . TYR C 3 248 ? -2.763 34.893 47.297 1.00 42.22 ? 248 TYR B CE1 1 ATOM 3967 C CE2 . TYR C 3 248 ? -2.324 37.016 48.338 1.00 42.38 ? 248 TYR B CE2 1 ATOM 3968 C CZ . TYR C 3 248 ? -3.140 35.909 48.163 1.00 42.83 ? 248 TYR B CZ 1 ATOM 3969 O OH . TYR C 3 248 ? -4.337 35.829 48.846 1.00 43.83 ? 248 TYR B OH 1 ATOM 3970 N N . PRO C 3 249 ? -1.146 38.454 44.316 1.00 31.86 ? 249 PRO B N 1 ATOM 3971 C CA . PRO C 3 249 ? -1.398 39.885 44.130 1.00 31.13 ? 249 PRO B CA 1 ATOM 3972 C C . PRO C 3 249 ? -0.779 40.694 45.272 1.00 30.82 ? 249 PRO B C 1 ATOM 3973 O O . PRO C 3 249 ? -0.592 40.187 46.376 1.00 30.79 ? 249 PRO B O 1 ATOM 3974 C CB . PRO C 3 249 ? -2.924 39.967 44.088 1.00 31.00 ? 249 PRO B CB 1 ATOM 3975 C CG . PRO C 3 249 ? -3.357 38.783 44.896 1.00 31.61 ? 249 PRO B CG 1 ATOM 3976 C CD . PRO C 3 249 ? -2.410 37.709 44.432 1.00 31.89 ? 249 PRO B CD 1 ATOM 3977 N N . LEU C 3 250 ? -0.463 41.952 44.994 1.00 30.15 ? 250 LEU B N 1 ATOM 3978 C CA . LEU C 3 250 ? 0.168 42.841 45.962 1.00 29.85 ? 250 LEU B CA 1 ATOM 3979 C C . LEU C 3 250 ? -0.678 43.295 47.158 1.00 30.53 ? 250 LEU B C 1 ATOM 3980 O O . LEU C 3 250 ? -1.820 43.727 46.994 1.00 31.22 ? 250 LEU B O 1 ATOM 3981 C CB . LEU C 3 250 ? 0.683 44.084 45.228 1.00 29.86 ? 250 LEU B CB 1 ATOM 3982 C CG . LEU C 3 250 ? 1.141 45.257 46.097 1.00 29.58 ? 250 LEU B CG 1 ATOM 3983 C CD1 . LEU C 3 250 ? 2.469 44.894 46.742 1.00 33.04 ? 250 LEU B CD1 1 ATOM 3984 C CD2 . LEU C 3 250 ? 1.276 46.518 45.258 1.00 28.23 ? 250 LEU B CD2 1 ATOM 3985 N N . HIS C 3 251 ? -0.108 43.188 48.359 1.00 31.59 ? 251 HIS B N 1 ATOM 3986 C CA . HIS C 3 251 ? -0.767 43.654 49.577 1.00 31.29 ? 251 HIS B CA 1 ATOM 3987 C C . HIS C 3 251 ? 0.253 44.349 50.476 1.00 31.47 ? 251 HIS B C 1 ATOM 3988 O O . HIS C 3 251 ? -0.101 44.979 51.470 1.00 32.50 ? 251 HIS B O 1 ATOM 3989 C CB . HIS C 3 251 ? -1.520 42.527 50.323 1.00 31.79 ? 251 HIS B CB 1 ATOM 3990 C CG . HIS C 3 251 ? -0.679 41.353 50.715 1.00 32.33 ? 251 HIS B CG 1 ATOM 3991 N ND1 . HIS C 3 251 ? 0.437 41.464 51.515 1.00 33.78 ? 251 HIS B ND1 1 ATOM 3992 C CD2 . HIS C 3 251 ? -0.841 40.030 50.477 1.00 32.62 ? 251 HIS B CD2 1 ATOM 3993 C CE1 . HIS C 3 251 ? 0.926 40.260 51.756 1.00 33.54 ? 251 HIS B CE1 1 ATOM 3994 N NE2 . HIS C 3 251 ? 0.169 39.373 51.138 1.00 34.55 ? 251 HIS B NE2 1 ATOM 3995 N N . GLY C 3 252 ? 1.525 44.236 50.105 1.00 30.42 ? 252 GLY B N 1 ATOM 3996 C CA . GLY C 3 252 ? 2.585 44.904 50.840 1.00 29.80 ? 252 GLY B CA 1 ATOM 3997 C C . GLY C 3 252 ? 3.138 44.398 52.161 1.00 29.79 ? 252 GLY B C 1 ATOM 3998 O O . GLY C 3 252 ? 4.030 45.039 52.710 1.00 28.36 ? 252 GLY B O 1 ATOM 3999 N N . ASP C 3 253 ? 2.647 43.283 52.691 1.00 30.84 ? 253 ASP B N 1 ATOM 4000 C CA . ASP C 3 253 ? 3.181 42.782 53.964 1.00 33.24 ? 253 ASP B CA 1 ATOM 4001 C C . ASP C 3 253 ? 4.647 42.373 53.845 1.00 33.53 ? 253 ASP B C 1 ATOM 4002 O O . ASP C 3 253 ? 5.213 42.370 52.755 1.00 35.45 ? 253 ASP B O 1 ATOM 4003 C CB . ASP C 3 253 ? 2.382 41.578 54.472 1.00 36.31 ? 253 ASP B CB 1 ATOM 4004 C CG . ASP C 3 253 ? 1.057 41.969 55.081 1.00 39.52 ? 253 ASP B CG 1 ATOM 4005 O OD1 . ASP C 3 253 ? 1.027 42.952 55.857 1.00 40.72 ? 253 ASP B OD1 1 ATOM 4006 O OD2 . ASP C 3 253 ? 0.053 41.280 54.791 1.00 41.19 ? 253 ASP B OD2 1 ATOM 4007 N N . PRO C 3 254 ? 5.282 42.015 54.973 1.00 33.16 ? 254 PRO B N 1 ATOM 4008 C CA . PRO C 3 254 ? 6.692 41.606 54.962 1.00 31.85 ? 254 PRO B CA 1 ATOM 4009 C C . PRO C 3 254 ? 7.033 40.391 54.090 1.00 31.34 ? 254 PRO B C 1 ATOM 4010 O O . PRO C 3 254 ? 8.194 40.192 53.733 1.00 32.43 ? 254 PRO B O 1 ATOM 4011 C CB . PRO C 3 254 ? 6.984 41.351 56.440 1.00 31.91 ? 254 PRO B CB 1 ATOM 4012 C CG . PRO C 3 254 ? 6.099 42.329 57.125 1.00 33.04 ? 254 PRO B CG 1 ATOM 4013 C CD . PRO C 3 254 ? 4.804 42.182 56.358 1.00 33.62 ? 254 PRO B CD 1 ATOM 4014 N N . ASN C 3 255 ? 6.035 39.581 53.744 1.00 28.98 ? 255 ASN B N 1 ATOM 4015 C CA . ASN C 3 255 ? 6.287 38.397 52.929 1.00 27.16 ? 255 ASN B CA 1 ATOM 4016 C C . ASN C 3 255 ? 6.307 38.679 51.421 1.00 26.67 ? 255 ASN B C 1 ATOM 4017 O O . ASN C 3 255 ? 6.340 37.756 50.613 1.00 26.76 ? 255 ASN B O 1 ATOM 4018 C CB . ASN C 3 255 ? 5.262 37.303 53.254 1.00 25.27 ? 255 ASN B CB 1 ATOM 4019 C CG . ASN C 3 255 ? 3.856 37.682 52.851 1.00 25.19 ? 255 ASN B CG 1 ATOM 4020 O OD1 . ASN C 3 255 ? 3.308 38.665 53.330 1.00 27.74 ? 255 ASN B OD1 1 ATOM 4021 N ND2 . ASN C 3 255 ? 3.261 36.895 51.967 1.00 24.88 ? 255 ASN B ND2 1 ATOM 4022 N N . GLN C 3 256 ? 6.297 39.951 51.044 1.00 26.08 ? 256 GLN B N 1 ATOM 4023 C CA . GLN C 3 256 ? 6.334 40.320 49.635 1.00 26.38 ? 256 GLN B CA 1 ATOM 4024 C C . GLN C 3 256 ? 7.424 41.354 49.378 1.00 27.33 ? 256 GLN B C 1 ATOM 4025 O O . GLN C 3 256 ? 7.583 41.835 48.246 1.00 28.73 ? 256 GLN B O 1 ATOM 4026 C CB . GLN C 3 256 ? 5.005 40.916 49.189 1.00 24.81 ? 256 GLN B CB 1 ATOM 4027 C CG . GLN C 3 256 ? 3.807 40.018 49.335 1.00 23.91 ? 256 GLN B CG 1 ATOM 4028 C CD . GLN C 3 256 ? 2.601 40.589 48.626 1.00 23.78 ? 256 GLN B CD 1 ATOM 4029 O OE1 . GLN C 3 256 ? 2.342 41.797 48.691 1.00 24.19 ? 256 GLN B OE1 1 ATOM 4030 N NE2 . GLN C 3 256 ? 1.851 39.731 47.950 1.00 22.73 ? 256 GLN B NE2 1 ATOM 4031 N N . ILE C 3 257 ? 8.162 41.693 50.434 1.00 26.96 ? 257 ILE B N 1 ATOM 4032 C CA . ILE C 3 257 ? 9.236 42.685 50.372 1.00 26.52 ? 257 ILE B CA 1 ATOM 4033 C C . ILE C 3 257 ? 10.618 42.030 50.318 1.00 27.84 ? 257 ILE B C 1 ATOM 4034 O O . ILE C 3 257 ? 10.936 41.167 51.142 1.00 29.99 ? 257 ILE B O 1 ATOM 4035 C CB . ILE C 3 257 ? 9.206 43.605 51.609 1.00 24.68 ? 257 ILE B CB 1 ATOM 4036 C CG1 . ILE C 3 257 ? 7.783 44.102 51.863 1.00 23.06 ? 257 ILE B CG1 1 ATOM 4037 C CG2 . ILE C 3 257 ? 10.158 44.770 51.415 1.00 23.09 ? 257 ILE B CG2 1 ATOM 4038 C CD1 . ILE C 3 257 ? 7.221 44.960 50.767 1.00 24.07 ? 257 ILE B CD1 1 ATOM 4039 N N . TRP C 3 258 ? 11.434 42.455 49.355 1.00 28.03 ? 258 TRP B N 1 ATOM 4040 C CA . TRP C 3 258 ? 12.780 41.925 49.189 1.00 28.00 ? 258 TRP B CA 1 ATOM 4041 C C . TRP C 3 258 ? 13.773 43.059 49.022 1.00 29.05 ? 258 TRP B C 1 ATOM 4042 O O . TRP C 3 258 ? 13.430 44.155 48.584 1.00 30.03 ? 258 TRP B O 1 ATOM 4043 C CB . TRP C 3 258 ? 12.863 41.035 47.951 1.00 27.78 ? 258 TRP B CB 1 ATOM 4044 C CG . TRP C 3 258 ? 11.754 40.065 47.823 1.00 27.59 ? 258 TRP B CG 1 ATOM 4045 C CD1 . TRP C 3 258 ? 10.496 40.320 47.367 1.00 27.10 ? 258 TRP B CD1 1 ATOM 4046 C CD2 . TRP C 3 258 ? 11.774 38.686 48.207 1.00 27.80 ? 258 TRP B CD2 1 ATOM 4047 N NE1 . TRP C 3 258 ? 9.726 39.188 47.446 1.00 28.16 ? 258 TRP B NE1 1 ATOM 4048 C CE2 . TRP C 3 258 ? 10.486 38.168 47.959 1.00 28.00 ? 258 TRP B CE2 1 ATOM 4049 C CE3 . TRP C 3 258 ? 12.755 37.839 48.737 1.00 28.70 ? 258 TRP B CE3 1 ATOM 4050 C CZ2 . TRP C 3 258 ? 10.149 36.835 48.227 1.00 26.52 ? 258 TRP B CZ2 1 ATOM 4051 C CZ3 . TRP C 3 258 ? 12.419 36.514 49.004 1.00 28.89 ? 258 TRP B CZ3 1 ATOM 4052 C CH2 . TRP C 3 258 ? 11.123 36.027 48.747 1.00 27.13 ? 258 TRP B CH2 1 ATOM 4053 N N . LEU C 3 259 ? 15.021 42.787 49.358 1.00 30.38 ? 259 LEU B N 1 ATOM 4054 C CA . LEU C 3 259 ? 16.053 43.792 49.223 1.00 32.82 ? 259 LEU B CA 1 ATOM 4055 C C . LEU C 3 259 ? 17.289 43.161 48.616 1.00 34.86 ? 259 LEU B C 1 ATOM 4056 O O . LEU C 3 259 ? 17.765 42.126 49.093 1.00 36.03 ? 259 LEU B O 1 ATOM 4057 C CB . LEU C 3 259 ? 16.404 44.385 50.589 1.00 32.59 ? 259 LEU B CB 1 ATOM 4058 C CG . LEU C 3 259 ? 17.573 45.377 50.616 1.00 33.23 ? 259 LEU B CG 1 ATOM 4059 C CD1 . LEU C 3 259 ? 17.235 46.604 49.773 1.00 31.92 ? 259 LEU B CD1 1 ATOM 4060 C CD2 . LEU C 3 259 ? 17.880 45.769 52.055 1.00 31.97 ? 259 LEU B CD2 1 ATOM 4061 N N . PRO C 3 260 ? 17.812 43.755 47.534 1.00 35.13 ? 260 PRO B N 1 ATOM 4062 C CA . PRO C 3 260 ? 19.014 43.207 46.901 1.00 37.03 ? 260 PRO B CA 1 ATOM 4063 C C . PRO C 3 260 ? 20.252 43.643 47.696 1.00 38.53 ? 260 PRO B C 1 ATOM 4064 O O . PRO C 3 260 ? 20.577 44.828 47.760 1.00 39.86 ? 260 PRO B O 1 ATOM 4065 C CB . PRO C 3 260 ? 18.961 43.800 45.495 1.00 34.83 ? 260 PRO B CB 1 ATOM 4066 C CG . PRO C 3 260 ? 18.307 45.129 45.723 1.00 35.18 ? 260 PRO B CG 1 ATOM 4067 C CD . PRO C 3 260 ? 17.199 44.805 46.701 1.00 35.82 ? 260 PRO B CD 1 ATOM 4068 N N . LEU C 3 261 ? 20.920 42.678 48.319 1.00 40.21 ? 261 LEU B N 1 ATOM 4069 C CA . LEU C 3 261 ? 22.109 42.938 49.124 1.00 42.48 ? 261 LEU B CA 1 ATOM 4070 C C . LEU C 3 261 ? 23.357 42.617 48.313 1.00 43.83 ? 261 LEU B C 1 ATOM 4071 O O . LEU C 3 261 ? 23.654 41.448 48.069 1.00 45.42 ? 261 LEU B O 1 ATOM 4072 C CB . LEU C 3 261 ? 22.077 42.061 50.378 1.00 42.06 ? 261 LEU B CB 1 ATOM 4073 C CG . LEU C 3 261 ? 22.214 42.741 51.742 1.00 44.02 ? 261 LEU B CG 1 ATOM 4074 C CD1 . LEU C 3 261 ? 21.104 43.781 51.953 1.00 41.57 ? 261 LEU B CD1 1 ATOM 4075 C CD2 . LEU C 3 261 ? 22.165 41.660 52.822 1.00 43.70 ? 261 LEU B CD2 1 ATOM 4076 N N . PHE C 3 262 ? 24.084 43.646 47.889 1.00 44.71 ? 262 PHE B N 1 ATOM 4077 C CA . PHE C 3 262 ? 25.301 43.437 47.103 1.00 46.13 ? 262 PHE B CA 1 ATOM 4078 C C . PHE C 3 262 ? 26.545 43.841 47.865 1.00 47.57 ? 262 PHE B C 1 ATOM 4079 O O . PHE C 3 262 ? 27.622 43.281 47.568 1.00 49.96 ? 262 PHE B O 1 ATOM 4080 C CB . PHE C 3 262 ? 25.244 44.214 45.789 1.00 44.66 ? 262 PHE B CB 1 ATOM 4081 C CG . PHE C 3 262 ? 24.953 45.674 45.958 1.00 43.87 ? 262 PHE B CG 1 ATOM 4082 C CD1 . PHE C 3 262 ? 25.929 46.548 46.423 1.00 42.95 ? 262 PHE B CD1 1 ATOM 4083 C CD2 . PHE C 3 262 ? 23.689 46.176 45.655 1.00 43.12 ? 262 PHE B CD2 1 ATOM 4084 C CE1 . PHE C 3 262 ? 25.651 47.905 46.581 1.00 43.01 ? 262 PHE B CE1 1 ATOM 4085 C CE2 . PHE C 3 262 ? 23.403 47.526 45.809 1.00 43.07 ? 262 PHE B CE2 1 ATOM 4086 C CZ . PHE C 3 262 ? 24.385 48.393 46.275 1.00 42.45 ? 262 PHE B CZ 1 ATOM 4087 O OXT . PHE C 3 262 ? 26.428 44.730 48.731 1.00 48.70 ? 262 PHE B OXT 1 HETATM 4088 C C1 . GAL D 4 . ? 31.728 41.402 12.750 1.00 47.99 ? 264 GAL B C1 1 HETATM 4089 C C2 . GAL D 4 . ? 31.268 42.551 13.672 1.00 45.80 ? 264 GAL B C2 1 HETATM 4090 C C3 . GAL D 4 . ? 30.509 42.013 14.883 1.00 43.74 ? 264 GAL B C3 1 HETATM 4091 C C4 . GAL D 4 . ? 29.355 41.114 14.416 1.00 43.09 ? 264 GAL B C4 1 HETATM 4092 C C5 . GAL D 4 . ? 29.917 39.998 13.521 1.00 43.60 ? 264 GAL B C5 1 HETATM 4093 C C6 . GAL D 4 . ? 28.851 39.051 12.981 1.00 42.40 ? 264 GAL B C6 1 HETATM 4094 O O2 . GAL D 4 . ? 32.389 43.302 14.113 1.00 44.49 ? 264 GAL B O2 1 HETATM 4095 O O3 . GAL D 4 . ? 30.009 43.100 15.647 1.00 41.39 ? 264 GAL B O3 1 HETATM 4096 O O4 . GAL D 4 . ? 28.403 41.883 13.691 1.00 40.72 ? 264 GAL B O4 1 HETATM 4097 O O5 . GAL D 4 . ? 30.609 40.566 12.382 1.00 46.69 ? 264 GAL B O5 1 HETATM 4098 O O6 . GAL D 4 . ? 27.861 39.741 12.234 1.00 41.21 ? 264 GAL B O6 1 HETATM 4099 C C2 . BGC E 5 . ? 33.410 40.034 8.526 1.00 54.19 ? 265 BGC B C2 1 HETATM 4100 C C3 . BGC E 5 . ? 32.456 40.500 9.637 1.00 53.91 ? 265 BGC B C3 1 HETATM 4101 C C4 . BGC E 5 . ? 33.197 41.186 10.810 1.00 54.25 ? 265 BGC B C4 1 HETATM 4102 C C5 . BGC E 5 . ? 34.307 42.149 10.329 1.00 54.95 ? 265 BGC B C5 1 HETATM 4103 C C6 . BGC E 5 . ? 35.241 42.550 11.458 1.00 55.79 ? 265 BGC B C6 1 HETATM 4104 C C1 . BGC E 5 . ? 34.351 41.179 8.154 1.00 54.63 ? 265 BGC B C1 1 HETATM 4105 O O1 . BGC E 5 . ? 35.222 40.789 7.150 1.00 56.17 ? 265 BGC B O1 1 HETATM 4106 O O2 . BGC E 5 . ? 32.666 39.623 7.384 1.00 50.72 ? 265 BGC B O2 1 HETATM 4107 O O3 . BGC E 5 . ? 31.736 39.384 10.139 1.00 53.66 ? 265 BGC B O3 1 HETATM 4108 O O4 . BGC E 5 . ? 32.246 41.954 11.586 1.00 51.78 ? 265 BGC B O4 1 HETATM 4109 O O5 . BGC E 5 . ? 35.122 41.540 9.301 1.00 55.70 ? 265 BGC B O5 1 HETATM 4110 O O6 . BGC E 5 . ? 35.589 41.431 12.264 1.00 55.25 ? 265 BGC B O6 1 HETATM 4111 C C1 . GAL F 4 . ? -1.674 34.235 53.050 1.00 51.20 ? 267 GAL B C1 1 HETATM 4112 C C2 . GAL F 4 . ? -0.681 35.377 52.787 1.00 50.54 ? 267 GAL B C2 1 HETATM 4113 C C3 . GAL F 4 . ? -0.625 35.739 51.305 1.00 49.87 ? 267 GAL B C3 1 HETATM 4114 C C4 . GAL F 4 . ? -0.390 34.490 50.453 1.00 50.48 ? 267 GAL B C4 1 HETATM 4115 C C5 . GAL F 4 . ? -1.453 33.443 50.790 1.00 50.55 ? 267 GAL B C5 1 HETATM 4116 C C6 . GAL F 4 . ? -1.284 32.148 50.019 1.00 50.21 ? 267 GAL B C6 1 HETATM 4117 O O2 . GAL F 4 . ? -1.062 36.524 53.532 1.00 50.13 ? 267 GAL B O2 1 HETATM 4118 O O3 . GAL F 4 . ? 0.430 36.664 51.091 1.00 50.52 ? 267 GAL B O3 1 HETATM 4119 O O4 . GAL F 4 . ? 0.907 33.968 50.715 1.00 49.59 ? 267 GAL B O4 1 HETATM 4120 O O5 . GAL F 4 . ? -1.393 33.113 52.195 1.00 51.18 ? 267 GAL B O5 1 HETATM 4121 O O6 . GAL F 4 . ? -2.525 31.471 49.889 1.00 50.93 ? 267 GAL B O6 1 HETATM 4122 C C2 . BGC G 5 . ? -3.145 30.938 56.104 1.00 57.05 ? 268 BGC B C2 1 HETATM 4123 C C3 . BGC G 5 . ? -2.636 31.669 54.832 1.00 56.50 ? 268 BGC B C3 1 HETATM 4124 C C4 . BGC G 5 . ? -2.676 33.199 55.000 1.00 55.92 ? 268 BGC B C4 1 HETATM 4125 C C5 . BGC G 5 . ? -2.667 33.541 56.492 1.00 56.91 ? 268 BGC B C5 1 HETATM 4126 C C6 . BGC G 5 . ? -2.528 35.034 56.758 1.00 57.04 ? 268 BGC B C6 1 HETATM 4127 C C1 . BGC G 5 . ? -4.270 31.723 56.820 1.00 57.48 ? 268 BGC B C1 1 HETATM 4128 O O1 . BGC G 5 . ? -5.414 31.742 56.035 1.00 57.33 ? 268 BGC B O1 1 HETATM 4129 O O2 . BGC G 5 . ? -2.062 30.712 57.005 1.00 55.37 ? 268 BGC B O2 1 HETATM 4130 O O3 . BGC G 5 . ? -3.414 31.286 53.701 1.00 56.43 ? 268 BGC B O3 1 HETATM 4131 O O4 . BGC G 5 . ? -1.530 33.806 54.361 1.00 53.97 ? 268 BGC B O4 1 HETATM 4132 O O5 . BGC G 5 . ? -3.897 33.093 57.121 1.00 58.67 ? 268 BGC B O5 1 HETATM 4133 O O6 . BGC G 5 . ? -3.108 35.805 55.713 1.00 56.15 ? 268 BGC B O6 1 HETATM 4134 C C1 . NAG H 6 . ? 6.501 49.928 32.078 1.00 40.99 ? 270 NAG B C1 1 HETATM 4135 C C2 . NAG H 6 . ? 5.104 49.599 32.603 1.00 41.50 ? 270 NAG B C2 1 HETATM 4136 C C3 . NAG H 6 . ? 4.098 50.372 31.759 1.00 43.50 ? 270 NAG B C3 1 HETATM 4137 C C4 . NAG H 6 . ? 4.388 51.880 31.807 1.00 45.78 ? 270 NAG B C4 1 HETATM 4138 C C5 . NAG H 6 . ? 5.889 52.197 31.535 1.00 44.66 ? 270 NAG B C5 1 HETATM 4139 C C6 . NAG H 6 . ? 6.257 53.605 31.966 1.00 43.16 ? 270 NAG B C6 1 HETATM 4140 C C7 . NAG H 6 . ? 4.329 47.529 33.593 1.00 40.03 ? 270 NAG B C7 1 HETATM 4141 C C8 . NAG H 6 . ? 3.313 46.429 33.315 1.00 38.75 ? 270 NAG B C8 1 HETATM 4142 N N2 . NAG H 6 . ? 4.850 48.170 32.543 1.00 39.70 ? 270 NAG B N2 1 HETATM 4143 O O3 . NAG H 6 . ? 2.785 50.128 32.237 1.00 44.10 ? 270 NAG B O3 1 HETATM 4144 O O4 . NAG H 6 . ? 3.557 52.529 30.816 1.00 50.50 ? 270 NAG B O4 1 HETATM 4145 O O5 . NAG H 6 . ? 6.765 51.321 32.290 1.00 42.93 ? 270 NAG B O5 1 HETATM 4146 O O6 . NAG H 6 . ? 6.368 54.472 30.854 1.00 45.01 ? 270 NAG B O6 1 HETATM 4147 O O7 . NAG H 6 . ? 4.638 47.788 34.760 1.00 39.04 ? 270 NAG B O7 1 HETATM 4148 C C1 . NAG I 6 . ? 3.011 53.784 31.095 1.00 55.10 ? 271 NAG B C1 1 HETATM 4149 C C2 . NAG I 6 . ? 1.905 54.117 30.073 1.00 57.99 ? 271 NAG B C2 1 HETATM 4150 C C3 . NAG I 6 . ? 1.272 55.487 30.406 1.00 60.28 ? 271 NAG B C3 1 HETATM 4151 C C4 . NAG I 6 . ? 0.829 55.547 31.882 1.00 59.98 ? 271 NAG B C4 1 HETATM 4152 C C5 . NAG I 6 . ? 1.943 55.051 32.832 1.00 57.95 ? 271 NAG B C5 1 HETATM 4153 C C6 . NAG I 6 . ? 1.439 54.879 34.253 1.00 57.02 ? 271 NAG B C6 1 HETATM 4154 C C7 . NAG I 6 . ? 3.284 55.004 28.281 1.00 56.39 ? 271 NAG B C7 1 HETATM 4155 C C8 . NAG I 6 . ? 3.735 54.905 26.832 1.00 55.62 ? 271 NAG B C8 1 HETATM 4156 N N2 . NAG I 6 . ? 2.410 54.093 28.705 1.00 57.02 ? 271 NAG B N2 1 HETATM 4157 O O3 . NAG I 6 . ? 0.140 55.716 29.566 1.00 62.35 ? 271 NAG B O3 1 HETATM 4158 O O4 . NAG I 6 . ? 0.469 56.886 32.222 1.00 61.12 ? 271 NAG B O4 1 HETATM 4159 O O5 . NAG I 6 . ? 2.443 53.757 32.412 1.00 55.97 ? 271 NAG B O5 1 HETATM 4160 O O6 . NAG I 6 . ? 2.468 54.402 35.108 1.00 56.84 ? 271 NAG B O6 1 HETATM 4161 O O7 . NAG I 6 . ? 3.732 55.901 29.004 1.00 56.38 ? 271 NAG B O7 1 HETATM 4162 C C1 . NAG J 6 . ? 30.383 53.558 26.781 1.00 42.09 ? 280 NAG B C1 1 HETATM 4163 C C2 . NAG J 6 . ? 30.186 54.946 27.387 1.00 43.21 ? 280 NAG B C2 1 HETATM 4164 C C3 . NAG J 6 . ? 30.265 56.024 26.296 1.00 44.93 ? 280 NAG B C3 1 HETATM 4165 C C4 . NAG J 6 . ? 31.560 55.868 25.484 1.00 46.08 ? 280 NAG B C4 1 HETATM 4166 C C5 . NAG J 6 . ? 31.713 54.426 24.995 1.00 44.61 ? 280 NAG B C5 1 HETATM 4167 C C6 . NAG J 6 . ? 33.045 54.187 24.323 1.00 43.67 ? 280 NAG B C6 1 HETATM 4168 C C7 . NAG J 6 . ? 28.805 55.792 29.161 1.00 42.33 ? 280 NAG B C7 1 HETATM 4169 C C8 . NAG J 6 . ? 27.564 56.670 29.272 1.00 41.25 ? 280 NAG B C8 1 HETATM 4170 N N2 . NAG J 6 . ? 28.919 55.016 28.086 1.00 42.25 ? 280 NAG B N2 1 HETATM 4171 O O3 . NAG J 6 . ? 30.227 57.315 26.895 1.00 45.25 ? 280 NAG B O3 1 HETATM 4172 O O4 . NAG J 6 . ? 31.533 56.751 24.345 1.00 51.90 ? 280 NAG B O4 1 HETATM 4173 O O5 . NAG J 6 . ? 31.639 53.509 26.102 1.00 43.08 ? 280 NAG B O5 1 HETATM 4174 O O6 . NAG J 6 . ? 33.892 53.398 25.144 1.00 44.52 ? 280 NAG B O6 1 HETATM 4175 O O7 . NAG J 6 . ? 29.663 55.832 30.045 1.00 41.67 ? 280 NAG B O7 1 HETATM 4176 C C1 . NAG K 6 . ? 32.482 57.763 24.311 1.00 56.27 ? 281 NAG B C1 1 HETATM 4177 C C2 . NAG K 6 . ? 32.804 58.106 22.845 1.00 57.44 ? 281 NAG B C2 1 HETATM 4178 C C3 . NAG K 6 . ? 33.630 59.401 22.721 1.00 58.74 ? 281 NAG B C3 1 HETATM 4179 C C4 . NAG K 6 . ? 33.025 60.532 23.555 1.00 60.09 ? 281 NAG B C4 1 HETATM 4180 C C5 . NAG K 6 . ? 32.816 60.045 24.996 1.00 59.94 ? 281 NAG B C5 1 HETATM 4181 C C6 . NAG K 6 . ? 32.181 61.094 25.893 1.00 59.82 ? 281 NAG B C6 1 HETATM 4182 C C7 . NAG K 6 . ? 33.404 56.714 20.970 1.00 58.14 ? 281 NAG B C7 1 HETATM 4183 C C8 . NAG K 6 . ? 32.353 55.682 20.594 1.00 56.22 ? 281 NAG B C8 1 HETATM 4184 N N2 . NAG K 6 . ? 33.546 57.006 22.258 1.00 57.61 ? 281 NAG B N2 1 HETATM 4185 O O3 . NAG K 6 . ? 33.681 59.805 21.360 1.00 57.68 ? 281 NAG B O3 1 HETATM 4186 O O4 . NAG K 6 . ? 33.889 61.665 23.531 1.00 61.57 ? 281 NAG B O4 1 HETATM 4187 O O5 . NAG K 6 . ? 31.933 58.899 24.998 1.00 58.81 ? 281 NAG B O5 1 HETATM 4188 O O6 . NAG K 6 . ? 30.825 60.776 26.178 1.00 58.82 ? 281 NAG B O6 1 HETATM 4189 O O7 . NAG K 6 . ? 34.085 57.240 20.091 1.00 59.98 ? 281 NAG B O7 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 A 1 701 701 A A D . n A 1 2 G 2 702 702 G G D . n B 2 1 ILE 1 1 ? ? ? A . n B 2 2 PHE 2 2 ? ? ? A . n B 2 3 PRO 3 3 ? ? ? A . n B 2 4 LYS 4 4 ? ? ? A . n B 2 5 GLN 5 5 5 GLN GLN A . n B 2 6 TYR 6 6 6 TYR TYR A . n B 2 7 PRO 7 7 7 PRO PRO A . n B 2 8 ILE 8 8 8 ILE ILE A . n B 2 9 ILE 9 9 9 ILE ILE A . n B 2 10 ASN 10 10 10 ASN ASN A . n B 2 11 PHE 11 11 11 PHE PHE A . n B 2 12 THR 12 12 12 THR THR A . n B 2 13 THR 13 13 13 THR THR A . n B 2 14 ALA 14 14 14 ALA ALA A . n B 2 15 GLY 15 15 15 GLY GLY A . n B 2 16 ALA 16 16 16 ALA ALA A . n B 2 17 THR 17 17 17 THR THR A . n B 2 18 VAL 18 18 18 VAL VAL A . n B 2 19 GLN 19 19 19 GLN GLN A . n B 2 20 SER 20 20 20 SER SER A . n B 2 21 TYR 21 21 21 TYR TYR A . n B 2 22 THR 22 22 22 THR THR A . n B 2 23 ASN 23 23 23 ASN ASN A . n B 2 24 PHE 24 24 24 PHE PHE A . n B 2 25 ILE 25 25 25 ILE ILE A . n B 2 26 ARG 26 26 26 ARG ARG A . n B 2 27 ALA 27 27 27 ALA ALA A . n B 2 28 VAL 28 28 28 VAL VAL A . n B 2 29 ARG 29 29 29 ARG ARG A . n B 2 30 GLY 30 30 30 GLY GLY A . n B 2 31 ARG 31 31 31 ARG ARG A . n B 2 32 LEU 32 32 32 LEU LEU A . n B 2 33 THR 33 33 33 THR THR A . n B 2 34 THR 34 34 34 THR THR A . n B 2 35 GLY 35 35 35 GLY GLY A . n B 2 36 ALA 36 36 36 ALA ALA A . n B 2 37 ASP 37 37 37 ASP ASP A . n B 2 38 VAL 38 38 38 VAL VAL A . n B 2 39 ARG 39 39 39 ARG ARG A . n B 2 40 HIS 40 40 40 HIS HIS A . n B 2 41 GLU 41 41 41 GLU GLU A . n B 2 42 ILE 42 42 42 ILE ILE A . n B 2 43 PRO 43 43 43 PRO PRO A . n B 2 44 VAL 44 44 44 VAL VAL A . n B 2 45 LEU 45 45 45 LEU LEU A . n B 2 46 PRO 46 46 46 PRO PRO A . n B 2 47 ASN 47 47 47 ASN ASN A . n B 2 48 ARG 48 48 48 ARG ARG A . n B 2 49 VAL 49 49 49 VAL VAL A . n B 2 50 GLY 50 50 50 GLY GLY A . n B 2 51 LEU 51 51 51 LEU LEU A . n B 2 52 PRO 52 52 52 PRO PRO A . n B 2 53 ILE 53 53 53 ILE ILE A . n B 2 54 ASN 54 54 54 ASN ASN A . n B 2 55 GLN 55 55 55 GLN GLN A . n B 2 56 ARG 56 56 56 ARG ARG A . n B 2 57 PHE 57 57 57 PHE PHE A . n B 2 58 ILE 58 58 58 ILE ILE A . n B 2 59 LEU 59 59 59 LEU LEU A . n B 2 60 VAL 60 60 60 VAL VAL A . n B 2 61 GLU 61 61 61 GLU GLU A . n B 2 62 LEU 62 62 62 LEU LEU A . n B 2 63 SER 63 63 63 SER SER A . n B 2 64 ASN 64 64 64 ASN ASN A . n B 2 65 HIS 65 65 65 HIS HIS A . n B 2 66 ALA 66 66 66 ALA ALA A . n B 2 67 GLU 67 67 67 GLU GLU A . n B 2 68 LEU 68 68 68 LEU LEU A . n B 2 69 SER 69 69 69 SER SER A . n B 2 70 VAL 70 70 70 VAL VAL A . n B 2 71 THR 71 71 71 THR THR A . n B 2 72 LEU 72 72 72 LEU LEU A . n B 2 73 ALA 73 73 73 ALA ALA A . n B 2 74 LEU 74 74 74 LEU LEU A . n B 2 75 ASP 75 75 75 ASP ASP A . n B 2 76 VAL 76 76 76 VAL VAL A . n B 2 77 THR 77 77 77 THR THR A . n B 2 78 ASN 78 78 78 ASN ASN A . n B 2 79 ALA 79 79 79 ALA ALA A . n B 2 80 TYR 80 80 80 TYR TYR A . n B 2 81 VAL 81 81 81 VAL VAL A . n B 2 82 VAL 82 82 82 VAL VAL A . n B 2 83 GLY 83 83 83 GLY GLY A . n B 2 84 TYR 84 84 84 TYR TYR A . n B 2 85 ARG 85 85 85 ARG ARG A . n B 2 86 ALA 86 86 86 ALA ALA A . n B 2 87 GLY 87 87 87 GLY GLY A . n B 2 88 ASN 88 88 88 ASN ASN A . n B 2 89 SER 89 89 89 SER SER A . n B 2 90 ALA 90 90 90 ALA ALA A . n B 2 91 TYR 91 91 91 TYR TYR A . n B 2 92 PHE 92 92 92 PHE PHE A . n B 2 93 PHE 93 93 93 PHE PHE A . n B 2 94 HIS 94 94 94 HIS HIS A . n B 2 95 PRO 95 95 95 PRO PRO A . n B 2 96 ASP 96 96 96 ASP ASP A . n B 2 97 ASN 97 97 97 ASN ASN A . n B 2 98 GLN 98 98 98 GLN ALA A . n B 2 99 GLU 99 99 99 GLU ALA A . n B 2 100 ASP 100 100 100 ASP ASP A . n B 2 101 ALA 101 101 101 ALA ALA A . n B 2 102 GLU 102 102 102 GLU ALA A . n B 2 103 ALA 103 103 103 ALA ALA A . n B 2 104 ILE 104 104 104 ILE ILE A . n B 2 105 THR 105 105 105 THR THR A . n B 2 106 HIS 106 106 106 HIS HIS A . n B 2 107 LEU 107 107 107 LEU LEU A . n B 2 108 PHE 108 108 108 PHE PHE A . n B 2 109 THR 109 109 109 THR THR A . n B 2 110 ASP 110 110 110 ASP ASP A . n B 2 111 VAL 111 111 111 VAL VAL A . n B 2 112 GLN 112 112 112 GLN ALA A . n B 2 113 ASN 113 113 113 ASN ASN A . n B 2 114 ARG 114 114 114 ARG ARG A . n B 2 115 TYR 115 115 115 TYR TYR A . n B 2 116 THR 116 116 116 THR THR A . n B 2 117 PHE 117 117 117 PHE PHE A . n B 2 118 ALA 118 118 118 ALA ALA A . n B 2 119 PHE 119 119 119 PHE PHE A . n B 2 120 GLY 120 120 120 GLY GLY A . n B 2 121 GLY 121 121 121 GLY GLY A . n B 2 122 ASN 122 122 122 ASN ASN A . n B 2 123 TYR 123 123 123 TYR TYR A . n B 2 124 ASP 124 124 124 ASP ASP A . n B 2 125 ARG 125 125 125 ARG ARG A . n B 2 126 LEU 126 126 126 LEU LEU A . n B 2 127 GLU 127 127 127 GLU GLU A . n B 2 128 GLN 128 128 128 GLN GLN A . n B 2 129 LEU 129 129 129 LEU LEU A . n B 2 130 ALA 130 130 130 ALA ALA A . n B 2 131 GLY 131 131 131 GLY GLY A . n B 2 132 ASN 132 132 132 ASN ASN A . n B 2 133 LEU 133 133 133 LEU LEU A . n B 2 134 ARG 134 134 134 ARG ARG A . n B 2 135 GLU 135 135 135 GLU GLU A . n B 2 136 ASN 136 136 136 ASN ASN A . n B 2 137 ILE 137 137 137 ILE ILE A . n B 2 138 GLU 138 138 138 GLU GLU A . n B 2 139 LEU 139 139 139 LEU LEU A . n B 2 140 GLY 140 140 140 GLY GLY A . n B 2 141 ASN 141 141 141 ASN ASN A . n B 2 142 GLY 142 142 142 GLY GLY A . n B 2 143 PRO 143 143 143 PRO PRO A . n B 2 144 LEU 144 144 144 LEU LEU A . n B 2 145 GLU 145 145 145 GLU GLU A . n B 2 146 GLU 146 146 146 GLU GLU A . n B 2 147 ALA 147 147 147 ALA ALA A . n B 2 148 ILE 148 148 148 ILE ILE A . n B 2 149 SER 149 149 149 SER SER A . n B 2 150 ALA 150 150 150 ALA ALA A . n B 2 151 LEU 151 151 151 LEU LEU A . n B 2 152 TYR 152 152 152 TYR TYR A . n B 2 153 TYR 153 153 153 TYR TYR A . n B 2 154 TYR 154 154 154 TYR TYR A . n B 2 155 SER 155 155 155 SER SER A . n B 2 156 THR 156 156 156 THR THR A . n B 2 157 GLY 157 157 157 GLY GLY A . n B 2 158 GLY 158 158 158 GLY GLY A . n B 2 159 THR 159 159 159 THR THR A . n B 2 160 GLN 160 160 160 GLN GLN A . n B 2 161 LEU 161 161 161 LEU LEU A . n B 2 162 PRO 162 162 162 PRO PRO A . n B 2 163 THR 163 163 163 THR THR A . n B 2 164 LEU 164 164 164 LEU LEU A . n B 2 165 ALA 165 165 165 ALA ALA A . n B 2 166 ARG 166 166 166 ARG ARG A . n B 2 167 SER 167 167 167 SER SER A . n B 2 168 PHE 168 168 168 PHE PHE A . n B 2 169 ILE 169 169 169 ILE ILE A . n B 2 170 ILE 170 170 170 ILE ILE A . n B 2 171 CYS 171 171 171 CYS CYS A . n B 2 172 ILE 172 172 172 ILE ILE A . n B 2 173 GLN 173 173 173 GLN GLN A . n B 2 174 MET 174 174 174 MET MET A . n B 2 175 ILE 175 175 175 ILE ILE A . n B 2 176 SER 176 176 176 SER SER A . n B 2 177 GLU 177 177 177 GLU GLU A . n B 2 178 ALA 178 178 178 ALA ALA A . n B 2 179 ALA 179 179 179 ALA ALA A . n B 2 180 ARG 180 180 180 ARG ARG A . n B 2 181 PHE 181 181 181 PHE PHE A . n B 2 182 GLN 182 182 182 GLN GLN A . n B 2 183 TYR 183 183 183 TYR TYR A . n B 2 184 ILE 184 184 184 ILE ILE A . n B 2 185 GLU 185 185 185 GLU GLU A . n B 2 186 GLY 186 186 186 GLY GLY A . n B 2 187 GLU 187 187 187 GLU GLU A . n B 2 188 MET 188 188 188 MET MET A . n B 2 189 ARG 189 189 189 ARG ARG A . n B 2 190 THR 190 190 190 THR THR A . n B 2 191 ARG 191 191 191 ARG ARG A . n B 2 192 ILE 192 192 192 ILE ILE A . n B 2 193 ARG 193 193 193 ARG ARG A . n B 2 194 TYR 194 194 194 TYR TYR A . n B 2 195 ASN 195 195 195 ASN ASN A . n B 2 196 ARG 196 196 196 ARG ARG A . n B 2 197 ARG 197 197 197 ARG ARG A . n B 2 198 SER 198 198 198 SER SER A . n B 2 199 ALA 199 199 199 ALA ALA A . n B 2 200 PRO 200 200 200 PRO PRO A . n B 2 201 ASP 201 201 201 ASP ASP A . n B 2 202 PRO 202 202 202 PRO PRO A . n B 2 203 SER 203 203 203 SER SER A . n B 2 204 VAL 204 204 204 VAL VAL A . n B 2 205 ILE 205 205 205 ILE ILE A . n B 2 206 THR 206 206 206 THR THR A . n B 2 207 LEU 207 207 207 LEU LEU A . n B 2 208 GLU 208 208 208 GLU GLU A . n B 2 209 ASN 209 209 209 ASN ASN A . n B 2 210 SER 210 210 210 SER SER A . n B 2 211 TRP 211 211 211 TRP TRP A . n B 2 212 GLY 212 212 212 GLY GLY A . n B 2 213 ARG 213 213 213 ARG ARG A . n B 2 214 LEU 214 214 214 LEU LEU A . n B 2 215 SER 215 215 215 SER SER A . n B 2 216 THR 216 216 216 THR THR A . n B 2 217 ALA 217 217 217 ALA ALA A . n B 2 218 ILE 218 218 218 ILE ILE A . n B 2 219 GLN 219 219 219 GLN GLN A . n B 2 220 GLU 220 220 220 GLU GLU A . n B 2 221 SER 221 221 221 SER SER A . n B 2 222 ASN 222 222 222 ASN ASN A . n B 2 223 GLN 223 223 223 GLN GLN A . n B 2 224 GLY 224 224 224 GLY GLY A . n B 2 225 ALA 225 225 225 ALA ALA A . n B 2 226 PHE 226 226 226 PHE PHE A . n B 2 227 ALA 227 227 227 ALA ALA A . n B 2 228 SER 228 228 228 SER SER A . n B 2 229 PRO 229 229 229 PRO PRO A . n B 2 230 ILE 230 230 230 ILE ILE A . n B 2 231 GLN 231 231 231 GLN GLN A . n B 2 232 LEU 232 232 232 LEU LEU A . n B 2 233 GLN 233 233 233 GLN GLN A . n B 2 234 ARG 234 234 234 ARG ARG A . n B 2 235 ARG 235 235 235 ARG ARG A . n B 2 236 ASN 236 236 236 ASN ASN A . n B 2 237 GLY 237 237 237 GLY GLY A . n B 2 238 SER 238 238 238 SER SER A . n B 2 239 LYS 239 239 239 LYS LYS A . n B 2 240 PHE 240 240 240 PHE PHE A . n B 2 241 SER 241 241 241 SER SER A . n B 2 242 VAL 242 242 242 VAL VAL A . n B 2 243 TYR 243 243 243 TYR TYR A . n B 2 244 ASP 244 244 244 ASP ASP A . n B 2 245 VAL 245 245 245 VAL VAL A . n B 2 246 SER 246 246 246 SER SER A . n B 2 247 ILE 247 247 247 ILE ILE A . n B 2 248 LEU 248 248 248 LEU LEU A . n B 2 249 ILE 249 249 249 ILE ILE A . n B 2 250 PRO 250 250 250 PRO PRO A . n B 2 251 ILE 251 251 251 ILE ILE A . n B 2 252 ILE 252 252 252 ILE ILE A . n B 2 253 ALA 253 253 253 ALA ALA A . n B 2 254 LEU 254 254 254 LEU LEU A . n B 2 255 MET 255 255 255 MET MET A . n B 2 256 VAL 256 256 256 VAL VAL A . n B 2 257 TYR 257 257 257 TYR TYR A . n B 2 258 ARG 258 258 258 ARG ARG A . n B 2 259 CYS 259 259 259 CYS CYS A . n B 2 260 ALA 260 260 260 ALA ALA A . n B 2 261 PRO 261 261 261 PRO PRO A . n B 2 262 PRO 262 262 262 PRO PRO A . n B 2 263 PRO 263 263 ? ? ? A . n B 2 264 SER 264 264 ? ? ? A . n B 2 265 SER 265 265 ? ? ? A . n B 2 266 GLN 266 266 ? ? ? A . n B 2 267 PHE 267 267 ? ? ? A . n C 3 1 ALA 1 1 1 ALA ALA B . n C 3 2 ASP 2 2 2 ASP ASP B . n C 3 3 VAL 3 3 3 VAL VAL B . n C 3 4 CYS 4 4 4 CYS CYS B . n C 3 5 MET 5 5 5 MET MET B . n C 3 6 ASP 6 6 6 ASP ASP B . n C 3 7 PRO 7 7 7 PRO PRO B . n C 3 8 GLU 8 8 8 GLU GLU B . n C 3 9 PRO 9 9 9 PRO PRO B . n C 3 10 ILE 10 10 10 ILE ILE B . n C 3 11 VAL 11 11 11 VAL VAL B . n C 3 12 ARG 12 12 12 ARG ARG B . n C 3 13 ILE 13 13 13 ILE ILE B . n C 3 14 VAL 14 14 14 VAL VAL B . n C 3 15 GLY 15 15 15 GLY GLY B . n C 3 16 ARG 16 16 16 ARG ARG B . n C 3 17 ASN 17 17 17 ASN ASN B . n C 3 18 GLY 18 18 18 GLY GLY B . n C 3 19 LEU 19 19 19 LEU LEU B . n C 3 20 CYS 20 20 20 CYS CYS B . n C 3 21 VAL 21 21 21 VAL VAL B . n C 3 22 ASP 22 22 22 ASP ASP B . n C 3 23 VAL 23 23 23 VAL VAL B . n C 3 24 ARG 24 24 24 ARG ARG B . n C 3 25 ASP 25 25 25 ASP ASP B . n C 3 26 GLY 26 26 26 GLY GLY B . n C 3 27 ARG 27 27 27 ARG ARG B . n C 3 28 PHE 28 28 28 PHE PHE B . n C 3 29 HIS 29 29 29 HIS HIS B . n C 3 30 ASN 30 30 30 ASN ASN B . n C 3 31 GLY 31 31 31 GLY GLY B . n C 3 32 ASN 32 32 32 ASN ASN B . n C 3 33 ALA 33 33 33 ALA ALA B . n C 3 34 ILE 34 34 34 ILE ILE B . n C 3 35 GLN 35 35 35 GLN GLN B . n C 3 36 LEU 36 36 36 LEU LEU B . n C 3 37 TRP 37 37 37 TRP TRP B . n C 3 38 PRO 38 38 38 PRO PRO B . n C 3 39 CYS 39 39 39 CYS CYS B . n C 3 40 LYS 40 40 40 LYS LYS B . n C 3 41 SER 41 41 41 SER SER B . n C 3 42 ASN 42 42 42 ASN ASN B . n C 3 43 THR 43 43 43 THR THR B . n C 3 44 ASP 44 44 44 ASP ASP B . n C 3 45 ALA 45 45 45 ALA ALA B . n C 3 46 ASN 46 46 46 ASN ASN B . n C 3 47 GLN 47 47 47 GLN GLN B . n C 3 48 LEU 48 48 48 LEU LEU B . n C 3 49 TRP 49 49 49 TRP TRP B . n C 3 50 THR 50 50 50 THR THR B . n C 3 51 LEU 51 51 51 LEU LEU B . n C 3 52 LYS 52 52 52 LYS LYS B . n C 3 53 ARG 53 53 53 ARG ARG B . n C 3 54 ASP 54 54 54 ASP ASP B . n C 3 55 ASN 55 55 55 ASN ASN B . n C 3 56 THR 56 56 56 THR THR B . n C 3 57 ILE 57 57 57 ILE ILE B . n C 3 58 ARG 58 58 58 ARG ARG B . n C 3 59 SER 59 59 59 SER SER B . n C 3 60 ASN 60 60 60 ASN ASN B . n C 3 61 GLY 61 61 61 GLY GLY B . n C 3 62 LYS 62 62 62 LYS LYS B . n C 3 63 CYS 63 63 63 CYS CYS B . n C 3 64 LEU 64 64 64 LEU LEU B . n C 3 65 THR 65 65 65 THR THR B . n C 3 66 THR 66 66 66 THR THR B . n C 3 67 TYR 67 67 67 TYR TYR B . n C 3 68 GLY 68 68 68 GLY GLY B . n C 3 69 TYR 69 69 69 TYR TYR B . n C 3 70 SER 70 70 70 SER SER B . n C 3 71 PRO 71 71 71 PRO PRO B . n C 3 72 GLY 72 72 72 GLY GLY B . n C 3 73 VAL 73 73 73 VAL VAL B . n C 3 74 TYR 74 74 74 TYR TYR B . n C 3 75 VAL 75 75 75 VAL VAL B . n C 3 76 MET 76 76 76 MET MET B . n C 3 77 ILE 77 77 77 ILE ILE B . n C 3 78 TYR 78 78 78 TYR TYR B . n C 3 79 ASP 79 79 79 ASP ASP B . n C 3 80 CYS 80 80 80 CYS CYS B . n C 3 81 ASN 81 81 81 ASN ASN B . n C 3 82 THR 82 82 82 THR THR B . n C 3 83 ALA 83 83 83 ALA ALA B . n C 3 84 ALA 84 84 84 ALA ALA B . n C 3 85 THR 85 85 85 THR THR B . n C 3 86 ASP 86 86 86 ASP ASP B . n C 3 87 ALA 87 87 87 ALA ALA B . n C 3 88 THR 88 88 88 THR THR B . n C 3 89 ARG 89 89 89 ARG ARG B . n C 3 90 TRP 90 90 90 TRP TRP B . n C 3 91 GLN 91 91 91 GLN GLN B . n C 3 92 ILE 92 92 92 ILE ILE B . n C 3 93 TRP 93 93 93 TRP TRP B . n C 3 94 ASP 94 94 94 ASP ASP B . n C 3 95 ASN 95 95 95 ASN ASN B . n C 3 96 GLY 96 96 96 GLY GLY B . n C 3 97 THR 97 97 97 THR THR B . n C 3 98 ILE 98 98 98 ILE ILE B . n C 3 99 ILE 99 99 99 ILE ILE B . n C 3 100 ASN 100 100 100 ASN ASN B . n C 3 101 PRO 101 101 101 PRO PRO B . n C 3 102 ARG 102 102 102 ARG ARG B . n C 3 103 SER 103 103 103 SER SER B . n C 3 104 SER 104 104 104 SER SER B . n C 3 105 LEU 105 105 105 LEU LEU B . n C 3 106 VAL 106 106 106 VAL VAL B . n C 3 107 LEU 107 107 107 LEU LEU B . n C 3 108 ALA 108 108 108 ALA ALA B . n C 3 109 ALA 109 109 109 ALA ALA B . n C 3 110 THR 110 110 110 THR THR B . n C 3 111 SER 111 111 111 SER SER B . n C 3 112 GLY 112 112 112 GLY GLY B . n C 3 113 ASN 113 113 113 ASN ASN B . n C 3 114 SER 114 114 114 SER SER B . n C 3 115 GLY 115 115 115 GLY GLY B . n C 3 116 THR 116 116 116 THR THR B . n C 3 117 THR 117 117 117 THR THR B . n C 3 118 LEU 118 118 118 LEU LEU B . n C 3 119 THR 119 119 119 THR THR B . n C 3 120 VAL 120 120 120 VAL VAL B . n C 3 121 GLN 121 121 121 GLN GLN B . n C 3 122 THR 122 122 122 THR THR B . n C 3 123 ASN 123 123 123 ASN ASN B . n C 3 124 ILE 124 124 124 ILE ILE B . n C 3 125 TYR 125 125 125 TYR TYR B . n C 3 126 ALA 126 126 126 ALA ALA B . n C 3 127 VAL 127 127 127 VAL VAL B . n C 3 128 SER 128 128 128 SER SER B . n C 3 129 GLN 129 129 129 GLN GLN B . n C 3 130 GLY 130 130 130 GLY GLY B . n C 3 131 TRP 131 131 131 TRP TRP B . n C 3 132 LEU 132 132 132 LEU LEU B . n C 3 133 PRO 133 133 133 PRO PRO B . n C 3 134 THR 134 134 134 THR THR B . n C 3 135 ASN 135 135 135 ASN ASN B . n C 3 136 ASN 136 136 136 ASN ASN B . n C 3 137 THR 137 137 137 THR THR B . n C 3 138 GLN 138 138 138 GLN GLN B . n C 3 139 PRO 139 139 139 PRO PRO B . n C 3 140 PHE 140 140 140 PHE PHE B . n C 3 141 VAL 141 141 141 VAL VAL B . n C 3 142 THR 142 142 142 THR THR B . n C 3 143 THR 143 143 143 THR THR B . n C 3 144 ILE 144 144 144 ILE ILE B . n C 3 145 VAL 145 145 145 VAL VAL B . n C 3 146 GLY 146 146 146 GLY GLY B . n C 3 147 LEU 147 147 147 LEU LEU B . n C 3 148 TYR 148 148 148 TYR TYR B . n C 3 149 GLY 149 149 149 GLY GLY B . n C 3 150 LEU 150 150 150 LEU LEU B . n C 3 151 CYS 151 151 151 CYS CYS B . n C 3 152 LEU 152 152 152 LEU LEU B . n C 3 153 GLN 153 153 153 GLN GLN B . n C 3 154 ALA 154 154 154 ALA ALA B . n C 3 155 ASN 155 155 155 ASN ALA B . n C 3 156 SER 156 156 156 SER SER B . n C 3 157 GLY 157 157 157 GLY GLY B . n C 3 158 GLN 158 158 158 GLN GLN B . n C 3 159 VAL 159 159 159 VAL VAL B . n C 3 160 TRP 160 160 160 TRP TRP B . n C 3 161 ILE 161 161 161 ILE ILE B . n C 3 162 GLU 162 162 162 GLU GLU B . n C 3 163 ASP 163 163 163 ASP ASP B . n C 3 164 CYS 164 164 164 CYS CYS B . n C 3 165 SER 165 165 165 SER ALA B . n C 3 166 SER 166 166 166 SER SER B . n C 3 167 GLU 167 167 167 GLU GLU B . n C 3 168 LYS 168 168 168 LYS LYS B . n C 3 169 ALA 169 169 169 ALA ALA B . n C 3 170 GLU 170 170 170 GLU ALA B . n C 3 171 GLN 171 171 171 GLN GLN B . n C 3 172 GLN 172 172 172 GLN ALA B . n C 3 173 TRP 173 173 173 TRP TRP B . n C 3 174 ALA 174 174 174 ALA ALA B . n C 3 175 LEU 175 175 175 LEU LEU B . n C 3 176 TYR 176 176 176 TYR TYR B . n C 3 177 ALA 177 177 177 ALA ALA B . n C 3 178 ASP 178 178 178 ASP ASP B . n C 3 179 GLY 179 179 179 GLY GLY B . n C 3 180 SER 180 180 180 SER SER B . n C 3 181 ILE 181 181 181 ILE ILE B . n C 3 182 ARG 182 182 182 ARG ARG B . n C 3 183 PRO 183 183 183 PRO PRO B . n C 3 184 GLN 184 184 184 GLN GLN B . n C 3 185 GLN 185 185 185 GLN GLN B . n C 3 186 ASN 186 186 186 ASN ASN B . n C 3 187 ARG 187 187 187 ARG ARG B . n C 3 188 ASP 188 188 188 ASP ASP B . n C 3 189 ASN 189 189 189 ASN ASN B . n C 3 190 CYS 190 190 190 CYS CYS B . n C 3 191 LEU 191 191 191 LEU LEU B . n C 3 192 THR 192 192 192 THR THR B . n C 3 193 SER 193 193 193 SER SER B . n C 3 194 ASP 194 194 194 ASP ASP B . n C 3 195 SER 195 195 195 SER ALA B . n C 3 196 ASN 196 196 196 ASN ASN B . n C 3 197 ILE 197 197 197 ILE ILE B . n C 3 198 ARG 198 198 198 ARG ARG B . n C 3 199 GLU 199 199 199 GLU GLU B . n C 3 200 THR 200 200 200 THR THR B . n C 3 201 VAL 201 201 201 VAL VAL B . n C 3 202 VAL 202 202 202 VAL VAL B . n C 3 203 LYS 203 203 203 LYS LYS B . n C 3 204 ILE 204 204 204 ILE ILE B . n C 3 205 LEU 205 205 205 LEU LEU B . n C 3 206 SER 206 206 206 SER SER B . n C 3 207 CYS 207 207 207 CYS CYS B . n C 3 208 GLY 208 208 208 GLY GLY B . n C 3 209 PRO 209 209 209 PRO PRO B . n C 3 210 ALA 210 210 210 ALA ALA B . n C 3 211 SER 211 211 211 SER SER B . n C 3 212 SER 212 212 212 SER SER B . n C 3 213 GLY 213 213 213 GLY GLY B . n C 3 214 GLN 214 214 214 GLN GLN B . n C 3 215 ARG 215 215 215 ARG ARG B . n C 3 216 TRP 216 216 216 TRP TRP B . n C 3 217 MET 217 217 217 MET MET B . n C 3 218 PHE 218 218 218 PHE PHE B . n C 3 219 LYS 219 219 219 LYS LYS B . n C 3 220 ASN 220 220 220 ASN ASN B . n C 3 221 ASP 221 221 221 ASP ASP B . n C 3 222 GLY 222 222 222 GLY GLY B . n C 3 223 THR 223 223 223 THR THR B . n C 3 224 ILE 224 224 224 ILE ILE B . n C 3 225 LEU 225 225 225 LEU LEU B . n C 3 226 ASN 226 226 226 ASN ASN B . n C 3 227 LEU 227 227 227 LEU LEU B . n C 3 228 TYR 228 228 228 TYR TYR B . n C 3 229 SER 229 229 229 SER SER B . n C 3 230 GLY 230 230 230 GLY GLY B . n C 3 231 LEU 231 231 231 LEU LEU B . n C 3 232 VAL 232 232 232 VAL VAL B . n C 3 233 LEU 233 233 233 LEU LEU B . n C 3 234 ASP 234 234 234 ASP ASP B . n C 3 235 VAL 235 235 235 VAL VAL B . n C 3 236 ARG 236 236 236 ARG ARG B . n C 3 237 ALA 237 237 237 ALA ALA B . n C 3 238 SER 238 238 238 SER SER B . n C 3 239 ASP 239 239 239 ASP ASP B . n C 3 240 PRO 240 240 240 PRO PRO B . n C 3 241 SER 241 241 241 SER SER B . n C 3 242 LEU 242 242 242 LEU LEU B . n C 3 243 LYS 243 243 243 LYS LYS B . n C 3 244 GLN 244 244 244 GLN GLN B . n C 3 245 ILE 245 245 245 ILE ILE B . n C 3 246 ILE 246 246 246 ILE ILE B . n C 3 247 LEU 247 247 247 LEU LEU B . n C 3 248 TYR 248 248 248 TYR TYR B . n C 3 249 PRO 249 249 249 PRO PRO B . n C 3 250 LEU 250 250 250 LEU LEU B . n C 3 251 HIS 251 251 251 HIS HIS B . n C 3 252 GLY 252 252 252 GLY GLY B . n C 3 253 ASP 253 253 253 ASP ASP B . n C 3 254 PRO 254 254 254 PRO PRO B . n C 3 255 ASN 255 255 255 ASN ASN B . n C 3 256 GLN 256 256 256 GLN GLN B . n C 3 257 ILE 257 257 257 ILE ILE B . n C 3 258 TRP 258 258 258 TRP TRP B . n C 3 259 LEU 259 259 259 LEU LEU B . n C 3 260 PRO 260 260 260 PRO PRO B . n C 3 261 LEU 261 261 261 LEU LEU B . n C 3 262 PHE 262 262 262 PHE PHE B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 4 GAL 1 264 264 GAL GAL B . E 5 BGC 2 265 265 BGC BGC B . F 4 GAL 1 267 267 GAL GAL B . G 5 BGC 2 268 268 BGC BGC B . H 6 NAG 1 270 270 NAG NAG B . I 6 NAG 2 271 271 NAG NAG B . J 6 NAG 1 280 280 NAG NAG B . K 6 NAG 2 281 281 NAG NAG B . # 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 C ASN 95 B ASN 95 ? ASN 'GLYCOSYLATION SITE' 2 C ASN 135 B ASN 135 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2011-08-31 # _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_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal San 'data collection' 'Diego Multiwire Systems' ? 1 X-PLOR 'model building' . ? 2 X-PLOR refinement . ? 3 San 'data reduction' 'Diego Multiwire Systems' ? 4 San 'data scaling' 'Diego Multiwire Systems' ? 5 X-PLOR phasing . ? 6 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 N9 _pdbx_validate_rmsd_angle.auth_asym_id_1 D _pdbx_validate_rmsd_angle.auth_comp_id_1 A _pdbx_validate_rmsd_angle.auth_seq_id_1 701 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 "C1'" _pdbx_validate_rmsd_angle.auth_asym_id_2 D _pdbx_validate_rmsd_angle.auth_comp_id_2 A _pdbx_validate_rmsd_angle.auth_seq_id_2 701 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 "C2'" _pdbx_validate_rmsd_angle.auth_asym_id_3 D _pdbx_validate_rmsd_angle.auth_comp_id_3 A _pdbx_validate_rmsd_angle.auth_seq_id_3 701 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 123.50 _pdbx_validate_rmsd_angle.angle_target_value 114.00 _pdbx_validate_rmsd_angle.angle_deviation 9.50 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.30 _pdbx_validate_rmsd_angle.linker_flag 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 ALA A 14 ? ? -60.49 -77.79 2 1 PRO A 46 ? ? -49.92 151.29 3 1 ILE A 53 ? ? -45.84 -6.04 4 1 ASN A 64 ? ? -112.58 -169.86 5 1 ALA A 66 ? ? -69.82 5.86 6 1 VAL A 111 ? ? -26.03 140.05 7 1 ASN A 122 ? ? -42.72 151.91 8 1 ASP B 2 ? ? 64.92 -164.05 9 1 ARG B 16 ? ? -37.63 130.40 10 1 ASN B 17 ? ? 56.71 18.78 11 1 ARG B 24 ? ? -39.41 129.32 12 1 ASP B 25 ? ? 49.39 24.75 13 1 ASN B 30 ? ? -52.72 109.12 14 1 ASN B 42 ? ? -178.12 -155.38 15 1 ASP B 44 ? ? -55.93 106.34 16 1 ALA B 45 ? ? -53.20 -9.01 17 1 ASN B 55 ? ? 86.23 27.74 18 1 TYR B 69 ? ? -103.95 47.94 19 1 PRO B 71 ? ? -56.85 103.08 20 1 THR B 85 ? ? -46.80 -71.43 21 1 ASP B 86 ? ? -72.19 25.36 22 1 ASN B 95 ? ? -99.36 38.92 23 1 ARG B 102 ? ? 145.39 -32.82 24 1 THR B 110 ? ? -73.74 35.25 25 1 SER B 111 ? ? -175.49 134.74 26 1 ILE B 124 ? ? -140.06 23.05 27 1 TYR B 125 ? ? 39.81 57.48 28 1 LEU B 147 ? ? -33.89 131.10 29 1 TYR B 148 ? ? 59.73 16.98 30 1 SER B 156 ? ? 70.03 -109.77 31 1 SER B 166 ? ? -63.15 42.99 32 1 GLU B 167 ? ? -176.27 -25.32 33 1 LYS B 168 ? ? -37.73 173.89 34 1 ALA B 169 ? ? -47.84 66.12 35 1 GLU B 170 ? ? 47.20 93.45 36 1 ARG B 187 ? ? -63.61 1.09 37 1 ARG B 198 ? ? -47.90 19.27 38 1 GLU B 199 ? ? -177.87 14.03 39 1 SER B 238 ? ? 26.87 39.46 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id A _pdbx_validate_planes.auth_asym_id D _pdbx_validate_planes.auth_seq_id 701 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.069 _pdbx_validate_planes.type 'SIDE CHAIN' # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A GLN 98 ? CG ? B GLN 98 CG 2 1 Y 1 A GLN 98 ? CD ? B GLN 98 CD 3 1 Y 1 A GLN 98 ? OE1 ? B GLN 98 OE1 4 1 Y 1 A GLN 98 ? NE2 ? B GLN 98 NE2 5 1 Y 1 A GLU 99 ? CG ? B GLU 99 CG 6 1 Y 1 A GLU 99 ? CD ? B GLU 99 CD 7 1 Y 1 A GLU 99 ? OE1 ? B GLU 99 OE1 8 1 Y 1 A GLU 99 ? OE2 ? B GLU 99 OE2 9 1 Y 1 A GLU 102 ? CG ? B GLU 102 CG 10 1 Y 1 A GLU 102 ? CD ? B GLU 102 CD 11 1 Y 1 A GLU 102 ? OE1 ? B GLU 102 OE1 12 1 Y 1 A GLU 102 ? OE2 ? B GLU 102 OE2 13 1 Y 1 A GLN 112 ? CG ? B GLN 112 CG 14 1 Y 1 A GLN 112 ? CD ? B GLN 112 CD 15 1 Y 1 A GLN 112 ? OE1 ? B GLN 112 OE1 16 1 Y 1 A GLN 112 ? NE2 ? B GLN 112 NE2 17 1 Y 1 B ASN 155 ? CG ? C ASN 155 CG 18 1 Y 1 B ASN 155 ? OD1 ? C ASN 155 OD1 19 1 Y 1 B ASN 155 ? ND2 ? C ASN 155 ND2 20 1 Y 1 B SER 165 ? OG ? C SER 165 OG 21 1 Y 1 B GLU 170 ? CG ? C GLU 170 CG 22 1 Y 1 B GLU 170 ? CD ? C GLU 170 CD 23 1 Y 1 B GLU 170 ? OE1 ? C GLU 170 OE1 24 1 Y 1 B GLU 170 ? OE2 ? C GLU 170 OE2 25 1 Y 1 B GLN 172 ? CG ? C GLN 172 CG 26 1 Y 1 B GLN 172 ? CD ? C GLN 172 CD 27 1 Y 1 B GLN 172 ? OE1 ? C GLN 172 OE1 28 1 Y 1 B GLN 172 ? NE2 ? C GLN 172 NE2 29 1 Y 1 B SER 195 ? OG ? C SER 195 OG # 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 ILE 1 ? B ILE 1 2 1 Y 1 A PHE 2 ? B PHE 2 3 1 Y 1 A PRO 3 ? B PRO 3 4 1 Y 1 A LYS 4 ? B LYS 4 5 1 Y 1 A PRO 263 ? B PRO 263 6 1 Y 1 A SER 264 ? B SER 264 7 1 Y 1 A SER 265 ? B SER 265 8 1 Y 1 A GLN 266 ? B GLN 266 9 1 Y 1 A PHE 267 ? B PHE 267 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 BETA-D-GALACTOSE GAL 5 BETA-D-GLUCOSE BGC 6 N-ACETYL-D-GLUCOSAMINE NAG #