data_4ZBV # _entry.id 4ZBV # _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 4ZBV WWPDB D_1000209008 # _pdbx_database_related.db_name PDB _pdbx_database_related.details 'same protein in its native form' _pdbx_database_related.db_id 4ZA3 _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 4ZBV _pdbx_database_status.recvd_initial_deposition_date 2015-04-15 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Chandran, T.' 1 'Sharma, A.' 2 'Vijayan, M.' 3 # loop_ _citation.abstract _citation.abstract_id_CAS _citation.book_id_ISBN _citation.book_publisher _citation.book_publisher_city _citation.book_title _citation.coordinate_linkage _citation.country _citation.database_id_Medline _citation.details _citation.id _citation.journal_abbrev _citation.journal_id_ASTM _citation.journal_id_CSD _citation.journal_id_ISSN _citation.journal_full _citation.journal_issue _citation.journal_volume _citation.language _citation.page_first _citation.page_last _citation.title _citation.year _citation.database_id_CSD _citation.pdbx_database_id_DOI _citation.pdbx_database_id_PubMed _citation.unpublished_flag ? ? ? ? ? ? ? II ? ? primary J.Biosci. JOBSDN 1073 0250-4774 ? ? 40 ? 929 941 ;Structural studies on a non-toxic homologue of type II RIPs from bitter gourd: Molecular basis of non-toxicity, conformational selection and glycan structure. ; 2015 ? ? 26648038 ? ? ? ? ? ? ? ? DK ? ? 1 'Acta Crystallogr. F Biol. Crystallogr.' ? ? 1744-3091 ? ? 66 ? 1037 1040 'Crystallization and preliminary X-ray studies of a galactose-specific lectin from the seeds of bitter gourd (Momordica charantia).' 2010 ? 10.1107/S174430911002659X 20823520 ? ? ? ? ? ? ? ? US ? ? 2 'Acta Crystallogr. D Biol. Crystallogr.' ABCRE6 ? 1399-0047 ? ? 69 ? 1493 1503 'The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs' 2013 ? 10.1107/S0907444913010020 23897472 ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Chandran, T.' 1 primary 'Sharma, A.' 2 primary 'Vijayan, M.' 3 1 'Sharma, A.' 4 1 'Pohlentz, G.' 5 1 'Bobbili, K.B.' 6 1 'Jeyaprakash, A.A.' 7 1 'Chandran, T.' 8 1 'Mormann, M.' 9 1 'Swamy, M.J.' 10 1 'Vijayan, M.' 11 2 'Sharma, A.' 12 2 'Pohlentz, G.' 13 2 'Bobbili, K.B.' 14 2 'Jeyaprakash, A.A.' 15 2 'Chandran, T.' 16 2 'Mormann, M.' 17 2 'Swamy, M.J.' 18 2 'Vijayan, M.' 19 # _cell.entry_id 4ZBV _cell.length_a 130.310 _cell.length_b 138.400 _cell.length_c 44.940 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4ZBV _symmetry.space_group_name_H-M 'P 21 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 18 # 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 nat 'rRNA N-glycosidase' 27642.234 1 3.2.2.22 ? 'UNP RESIDUES 24-270' ? 2 polymer nat 'rRNA N-glycosidase' 29017.416 1 3.2.2.22 ? 'UNP RESIDUES 287-547' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 4 non-polymer syn 'PHOSPHATE ION' 94.971 1 ? ? ? ? 5 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 non-polymer syn 1,2-ETHANEDIOL 62.068 1 ? ? ? ? 8 non-polymer syn 'TRIETHYLENE GLYCOL' 150.173 1 ? ? ? ? 9 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 10 non-polymer man N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE 221.208 1 ? ? ? ? 11 non-polymer syn TOLUENE 92.138 1 ? ? ? ? 12 water nat water 18.015 303 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;NLSLSQSNFSADTYKSFIKNLRKQLTIGASYGSAGIPILKHSVPICERFLLVDLTNGDNETITLAINVEDAGFAAYRAAD RSYFFQNAPPIASYVIFTDTNQNIMNFNNTFESIEIVGGTTRSETPLGIMHFEASIFHLFVHDENYVPTSFLVLIQMVLE AAKFKFIEQKVIHSIMDMEDFTPGLAMLSLEENWTQLSLQLQASESLNGVFGDSVSLYNSMDEPIGVDSMYYPILTANMA FQLYQCP ; ;NLSLSQSNFSADTYKSFIKNLRKQLTIGASYGSAGIPILKHSVPICERFLLVDLTNGDNETITLAINVEDAGFAAYRAAD RSYFFQNAPPIASYVIFTDTNQNIMNFNNTFESIEIVGGTTRSETPLGIMHFEASIFHLFVHDENYVPTSFLVLIQMVLE AAKFKFIEQKVIHSIMDMEDFTPGLAMLSLEENWTQLSLQLQASESLNGVFGDSVSLYNSMDEPIGVDSMYYPILTANMA FQLYQCP ; A ? 2 'polypeptide(L)' no no ;NEQCSPQQRTTRISGRDGLCVDVYGALTADGSRVILYPCGQQQNQQWTFYPDNTIRSLGKCLATSALSSGSNVVITNCDY LRYDDGWMVSSSGTMMNKSSHLVLTANAATSRTNLTGENNVFAAKQAWRIGNYVEPIVTTIIGLRHMCLEATDNDTNVWL ESCVKNKTKQYWALYSDDTIRVNNNRNLCVSSSTDSSSKLIVIRRCDGSINQRWVFTPQGTISNPGYEAVMDVAQNDVYL KKIVLSSATDKGNGQQWTVFY ; ;NEQCSPQQRTTRISGRDGLCVDVYGALTADGSRVILYPCGQQQNQQWTFYPDNTIRSLGKCLATSALSSGSNVVITNCDY LRYDDGWMVSSSGTMMNKSSHLVLTANAATSRTNLTGENNVFAAKQAWRIGNYVEPIVTTIIGLRHMCLEATDNDTNVWL ESCVKNKTKQYWALYSDDTIRVNNNRNLCVSSSTDSSSKLIVIRRCDGSINQRWVFTPQGTISNPGYEAVMDVAQNDVYL KKIVLSSATDKGNGQQWTVFY ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASN n 1 2 LEU n 1 3 SER n 1 4 LEU n 1 5 SER n 1 6 GLN n 1 7 SER n 1 8 ASN n 1 9 PHE n 1 10 SER n 1 11 ALA n 1 12 ASP n 1 13 THR n 1 14 TYR n 1 15 LYS n 1 16 SER n 1 17 PHE n 1 18 ILE n 1 19 LYS n 1 20 ASN n 1 21 LEU n 1 22 ARG n 1 23 LYS n 1 24 GLN n 1 25 LEU n 1 26 THR n 1 27 ILE n 1 28 GLY n 1 29 ALA n 1 30 SER n 1 31 TYR n 1 32 GLY n 1 33 SER n 1 34 ALA n 1 35 GLY n 1 36 ILE n 1 37 PRO n 1 38 ILE n 1 39 LEU n 1 40 LYS n 1 41 HIS n 1 42 SER n 1 43 VAL n 1 44 PRO n 1 45 ILE n 1 46 CYS n 1 47 GLU n 1 48 ARG n 1 49 PHE n 1 50 LEU n 1 51 LEU n 1 52 VAL n 1 53 ASP n 1 54 LEU n 1 55 THR n 1 56 ASN n 1 57 GLY n 1 58 ASP n 1 59 ASN n 1 60 GLU n 1 61 THR n 1 62 ILE n 1 63 THR n 1 64 LEU n 1 65 ALA n 1 66 ILE n 1 67 ASN n 1 68 VAL n 1 69 GLU n 1 70 ASP n 1 71 ALA n 1 72 GLY n 1 73 PHE n 1 74 ALA n 1 75 ALA n 1 76 TYR n 1 77 ARG n 1 78 ALA n 1 79 ALA n 1 80 ASP n 1 81 ARG n 1 82 SER n 1 83 TYR n 1 84 PHE n 1 85 PHE n 1 86 GLN n 1 87 ASN n 1 88 ALA n 1 89 PRO n 1 90 PRO n 1 91 ILE n 1 92 ALA n 1 93 SER n 1 94 TYR n 1 95 VAL n 1 96 ILE n 1 97 PHE n 1 98 THR n 1 99 ASP n 1 100 THR n 1 101 ASN n 1 102 GLN n 1 103 ASN n 1 104 ILE n 1 105 MET n 1 106 ASN n 1 107 PHE n 1 108 ASN n 1 109 ASN n 1 110 THR n 1 111 PHE n 1 112 GLU n 1 113 SER n 1 114 ILE n 1 115 GLU n 1 116 ILE n 1 117 VAL n 1 118 GLY n 1 119 GLY n 1 120 THR n 1 121 THR n 1 122 ARG n 1 123 SER n 1 124 GLU n 1 125 THR n 1 126 PRO n 1 127 LEU n 1 128 GLY n 1 129 ILE n 1 130 MET n 1 131 HIS n 1 132 PHE n 1 133 GLU n 1 134 ALA n 1 135 SER n 1 136 ILE n 1 137 PHE n 1 138 HIS n 1 139 LEU n 1 140 PHE n 1 141 VAL n 1 142 HIS n 1 143 ASP n 1 144 GLU n 1 145 ASN n 1 146 TYR n 1 147 VAL n 1 148 PRO n 1 149 THR n 1 150 SER n 1 151 PHE n 1 152 LEU n 1 153 VAL n 1 154 LEU n 1 155 ILE n 1 156 GLN n 1 157 MET n 1 158 VAL n 1 159 LEU n 1 160 GLU n 1 161 ALA n 1 162 ALA n 1 163 LYS n 1 164 PHE n 1 165 LYS n 1 166 PHE n 1 167 ILE n 1 168 GLU n 1 169 GLN n 1 170 LYS n 1 171 VAL n 1 172 ILE n 1 173 HIS n 1 174 SER n 1 175 ILE n 1 176 MET n 1 177 ASP n 1 178 MET n 1 179 GLU n 1 180 ASP n 1 181 PHE n 1 182 THR n 1 183 PRO n 1 184 GLY n 1 185 LEU n 1 186 ALA n 1 187 MET n 1 188 LEU n 1 189 SER n 1 190 LEU n 1 191 GLU n 1 192 GLU n 1 193 ASN n 1 194 TRP n 1 195 THR n 1 196 GLN n 1 197 LEU n 1 198 SER n 1 199 LEU n 1 200 GLN n 1 201 LEU n 1 202 GLN n 1 203 ALA n 1 204 SER n 1 205 GLU n 1 206 SER n 1 207 LEU n 1 208 ASN n 1 209 GLY n 1 210 VAL n 1 211 PHE n 1 212 GLY n 1 213 ASP n 1 214 SER n 1 215 VAL n 1 216 SER n 1 217 LEU n 1 218 TYR n 1 219 ASN n 1 220 SER n 1 221 MET n 1 222 ASP n 1 223 GLU n 1 224 PRO n 1 225 ILE n 1 226 GLY n 1 227 VAL n 1 228 ASP n 1 229 SER n 1 230 MET n 1 231 TYR n 1 232 TYR n 1 233 PRO n 1 234 ILE n 1 235 LEU n 1 236 THR n 1 237 ALA n 1 238 ASN n 1 239 MET n 1 240 ALA n 1 241 PHE n 1 242 GLN n 1 243 LEU n 1 244 TYR n 1 245 GLN n 1 246 CYS n 1 247 PRO n 2 1 ASN n 2 2 GLU n 2 3 GLN n 2 4 CYS n 2 5 SER n 2 6 PRO n 2 7 GLN n 2 8 GLN n 2 9 ARG n 2 10 THR n 2 11 THR n 2 12 ARG n 2 13 ILE n 2 14 SER n 2 15 GLY n 2 16 ARG n 2 17 ASP n 2 18 GLY n 2 19 LEU n 2 20 CYS n 2 21 VAL n 2 22 ASP n 2 23 VAL n 2 24 TYR n 2 25 GLY n 2 26 ALA n 2 27 LEU n 2 28 THR n 2 29 ALA n 2 30 ASP n 2 31 GLY n 2 32 SER n 2 33 ARG n 2 34 VAL n 2 35 ILE n 2 36 LEU n 2 37 TYR n 2 38 PRO n 2 39 CYS n 2 40 GLY n 2 41 GLN n 2 42 GLN n 2 43 GLN n 2 44 ASN n 2 45 GLN n 2 46 GLN n 2 47 TRP n 2 48 THR n 2 49 PHE n 2 50 TYR n 2 51 PRO n 2 52 ASP n 2 53 ASN n 2 54 THR n 2 55 ILE n 2 56 ARG n 2 57 SER n 2 58 LEU n 2 59 GLY n 2 60 LYS n 2 61 CYS n 2 62 LEU n 2 63 ALA n 2 64 THR n 2 65 SER n 2 66 ALA n 2 67 LEU n 2 68 SER n 2 69 SER n 2 70 GLY n 2 71 SER n 2 72 ASN n 2 73 VAL n 2 74 VAL n 2 75 ILE n 2 76 THR n 2 77 ASN n 2 78 CYS n 2 79 ASP n 2 80 TYR n 2 81 LEU n 2 82 ARG n 2 83 TYR n 2 84 ASP n 2 85 ASP n 2 86 GLY n 2 87 TRP n 2 88 MET n 2 89 VAL n 2 90 SER n 2 91 SER n 2 92 SER n 2 93 GLY n 2 94 THR n 2 95 MET n 2 96 MET n 2 97 ASN n 2 98 LYS n 2 99 SER n 2 100 SER n 2 101 HIS n 2 102 LEU n 2 103 VAL n 2 104 LEU n 2 105 THR n 2 106 ALA n 2 107 ASN n 2 108 ALA n 2 109 ALA n 2 110 THR n 2 111 SER n 2 112 ARG n 2 113 THR n 2 114 ASN n 2 115 LEU n 2 116 THR n 2 117 GLY n 2 118 GLU n 2 119 ASN n 2 120 ASN n 2 121 VAL n 2 122 PHE n 2 123 ALA n 2 124 ALA n 2 125 LYS n 2 126 GLN n 2 127 ALA n 2 128 TRP n 2 129 ARG n 2 130 ILE n 2 131 GLY n 2 132 ASN n 2 133 TYR n 2 134 VAL n 2 135 GLU n 2 136 PRO n 2 137 ILE n 2 138 VAL n 2 139 THR n 2 140 THR n 2 141 ILE n 2 142 ILE n 2 143 GLY n 2 144 LEU n 2 145 ARG n 2 146 HIS n 2 147 MET n 2 148 CYS n 2 149 LEU n 2 150 GLU n 2 151 ALA n 2 152 THR n 2 153 ASP n 2 154 ASN n 2 155 ASP n 2 156 THR n 2 157 ASN n 2 158 VAL n 2 159 TRP n 2 160 LEU n 2 161 GLU n 2 162 SER n 2 163 CYS n 2 164 VAL n 2 165 LYS n 2 166 ASN n 2 167 LYS n 2 168 THR n 2 169 LYS n 2 170 GLN n 2 171 TYR n 2 172 TRP n 2 173 ALA n 2 174 LEU n 2 175 TYR n 2 176 SER n 2 177 ASP n 2 178 ASP n 2 179 THR n 2 180 ILE n 2 181 ARG n 2 182 VAL n 2 183 ASN n 2 184 ASN n 2 185 ASN n 2 186 ARG n 2 187 ASN n 2 188 LEU n 2 189 CYS n 2 190 VAL n 2 191 SER n 2 192 SER n 2 193 SER n 2 194 THR n 2 195 ASP n 2 196 SER n 2 197 SER n 2 198 SER n 2 199 LYS n 2 200 LEU n 2 201 ILE n 2 202 VAL n 2 203 ILE n 2 204 ARG n 2 205 ARG n 2 206 CYS n 2 207 ASP n 2 208 GLY n 2 209 SER n 2 210 ILE n 2 211 ASN n 2 212 GLN n 2 213 ARG n 2 214 TRP n 2 215 VAL n 2 216 PHE n 2 217 THR n 2 218 PRO n 2 219 GLN n 2 220 GLY n 2 221 THR n 2 222 ILE n 2 223 SER n 2 224 ASN n 2 225 PRO n 2 226 GLY n 2 227 TYR n 2 228 GLU n 2 229 ALA n 2 230 VAL n 2 231 MET n 2 232 ASP n 2 233 VAL n 2 234 ALA n 2 235 GLN n 2 236 ASN n 2 237 ASP n 2 238 VAL n 2 239 TYR n 2 240 LEU n 2 241 LYS n 2 242 LYS n 2 243 ILE n 2 244 VAL n 2 245 LEU n 2 246 SER n 2 247 SER n 2 248 ALA n 2 249 THR n 2 250 ASP n 2 251 LYS n 2 252 GLY n 2 253 ASN n 2 254 GLY n 2 255 GLN n 2 256 GLN n 2 257 TRP n 2 258 THR n 2 259 VAL n 2 260 PHE n 2 261 TYR 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 1 1 sample 1 247 'Bitter gourd' 'Momordica charantia' 3673 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample 1 261 'Bitter gourd' 'Momordica charantia' 3673 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.db_code _struct_ref.db_name _struct_ref.details _struct_ref.entity_id _struct_ref.id _struct_ref.seq_align _struct_ref.seq_dif _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_align_end B7X8M2_MOMCH UNP ? 1 1 ? ? B7X8M2 ? ;NLSLSQSNFSADTYKSFIKNLRKQLTIGASYGSAGIPILKHSVPICERFLLVDLTNGDNETITLAINVEDAGFAAYRAAD RSYFFQNAPPIASYVIFTDTNQNIMNFNNTFESIEIVGGTTRSETPLGIMHFEASIFHLFVHDENYVPTSFLVLIQMVLE AAKFKFIEQKVIHSIMDMEDFTPGLAMLSLEENWTQLSLQLQASESLNGVFGDSVSLYNSMDEPIGVDSMYYPILTANMA FQLYQCP ; 24 ? B7X8M2_MOMCH UNP ? 2 2 ? ? B7X8M2 ? ;NEQCSPQQRTTRISGRDGLCVDVYGALTADGSRVILYPCGQQQNQQWTFYPDNTIRSLGKCLATSALSSGSNVVITNCDY LRYDDGWMVSSSGTMMNKSSHLVLTANAATSRTNLTGENNVFAAKQAWRIGNYVEPIVTTIIGLRHMCLEATDNDTNVWL ESCVKNKTKQYWALYSDDTIRVNNNRNLCVSSSTDSSSKLIVIRRCDGSINQRWVFTPQGTISNPGYEAVMDVAQNDVYL KKIVLSSATDKGNGQQWTVFY ; 287 ? # 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 4ZBV A 1 ? 247 ? B7X8M2 24 ? 270 ? 1 247 2 2 4ZBV B 1 ? 261 ? B7X8M2 287 ? 547 ? 1 261 # 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 A2G saccharide . N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE ? 'C8 H15 N O6' 221.208 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 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 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MBN non-polymer . TOLUENE ? 'C7 H8' 92.138 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 PGE non-polymer . 'TRIETHYLENE GLYCOL' ? 'C6 H14 O4' 150.173 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PO4 non-polymer . 'PHOSPHATE ION' ? 'O4 P -3' 94.971 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 4ZBV _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.38 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 63.60 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 7.3 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '0.1 M HEPES, 25% w/v PEG 10000, No-cryo protectant used' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2014-04-18 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator 'Si(111)' _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.95 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'ESRF BEAMLINE BM14' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.95 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BM14 _diffrn_source.pdbx_synchrotron_site ESRF # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4ZBV _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 94.874 _reflns.d_resolution_high 2.000 _reflns.number_obs 56031 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.27900 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 6.6000 _reflns.B_iso_Wilson_estimate 31.80 _reflns.pdbx_redundancy 8.900 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.11 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.01246 _reflns_shell.pdbx_Rsym_value 1.24600 _reflns_shell.meanI_over_sigI_obs 0.500 _reflns_shell.pdbx_redundancy 8.90 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4ZBV _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 52897 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 32.62 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 99.5 _refine.ls_R_factor_obs 0.233 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.231 _refine.ls_R_factor_R_free 0.266 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.100 _refine.ls_number_reflns_R_free 2829 _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 28.65 _refine.aniso_B[1][1] 4.98000 _refine.aniso_B[2][2] -2.90000 _refine.aniso_B[3][3] -2.08000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] 0.00000 _refine.aniso_B[2][3] 0.00000 _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 THROUGHOUT _refine.details ;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES ; _refine.pdbx_starting_model 4Z8S _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.166 _refine.pdbx_overall_ESU_R_Free 0.156 _refine.overall_SU_ML 0.165 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 6.676 _refine.overall_SU_R_Cruickshank_DPI ? _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 3945 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 143 _refine_hist.number_atoms_solvent 303 _refine_hist.number_atoms_total 4391 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 32.62 # _struct.entry_id 4ZBV _struct.title ;Structural studies on a non-toxic homologue of type II RIPs from Momordica charantia (bitter gourd) in complex with benzyl T-antigen ; _struct.pdbx_descriptor 'rRNA-N-glycosidase (E.C.3.2.2.22)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 4ZBV _struct_keywords.text 'beta-trefoil, Type II RIPs, Galactose specific lectin, HYDROLASE' _struct_keywords.pdbx_keywords HYDROLASE # 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 3 ? F N N 5 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 6 ? K N N 7 ? L N N 8 ? M N N 9 ? N N N 10 ? O N N 11 ? P N N 12 ? Q N N 12 ? # _struct_biol.details 'The symmetry related halves are covalently linked through a disulphide bridge. Therefore, the whole molecule is formally a monomer.' _struct_biol.id 1 _struct_biol.pdbx_aggregation_state ? _struct_biol.pdbx_assembly_method ? _struct_biol.pdbx_formula_weight ? _struct_biol.pdbx_formula_weight_method ? _struct_biol.pdbx_parent_biol_id ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 SER A 7 ? PHE A 9 ? SER A 7 PHE A 9 5 ? 3 HELX_P HELX_P2 AA2 SER A 10 ? THR A 26 ? SER A 10 THR A 26 1 ? 17 HELX_P HELX_P3 AA3 PRO A 44 ? GLU A 47 ? PRO A 44 GLU A 47 5 ? 4 HELX_P HELX_P4 AA4 ILE A 91 ? VAL A 95 ? ILE A 91 VAL A 95 5 ? 5 HELX_P HELX_P5 AA5 THR A 110 ? GLY A 119 ? THR A 110 GLY A 119 1 ? 10 HELX_P HELX_P6 AA6 THR A 121 ? THR A 125 ? THR A 121 THR A 125 5 ? 5 HELX_P HELX_P7 AA7 GLY A 128 ? HIS A 142 ? GLY A 128 HIS A 142 1 ? 15 HELX_P HELX_P8 AA8 TYR A 146 ? PHE A 164 ? TYR A 146 PHE A 164 1 ? 19 HELX_P HELX_P9 AA9 PHE A 164 ? MET A 178 ? PHE A 164 MET A 178 1 ? 15 HELX_P HELX_P10 AB1 GLY A 184 ? SER A 204 ? GLY A 184 SER A 204 1 ? 21 HELX_P HELX_P11 AB2 GLU A 205 ? ASN A 208 ? GLU A 205 ASN A 208 5 ? 4 HELX_P HELX_P12 AB3 TYR A 232 ? ALA A 237 ? TYR A 232 ALA A 237 1 ? 6 HELX_P HELX_P13 AB4 ASN B 1 ? SER B 5 ? ASN B 1 SER B 5 5 ? 5 HELX_P HELX_P14 AB5 GLY B 15 ? LEU B 19 ? GLY B 15 LEU B 19 5 ? 5 HELX_P HELX_P15 AB6 GLY B 25 ? LEU B 27 ? GLY B 25 LEU B 27 5 ? 3 HELX_P HELX_P16 AB7 GLN B 42 ? GLN B 46 ? GLN B 42 GLN B 46 5 ? 5 HELX_P HELX_P17 AB8 ASN B 77 ? ARG B 82 ? ASN B 77 ARG B 82 5 ? 6 HELX_P HELX_P18 AB9 ALA B 123 ? ALA B 127 ? ALA B 123 ALA B 127 5 ? 5 HELX_P HELX_P19 AC1 GLY B 143 ? ARG B 145 ? GLY B 143 ARG B 145 5 ? 3 HELX_P HELX_P20 AC2 LYS B 167 ? GLN B 170 ? LYS B 167 GLN B 170 5 ? 4 HELX_P HELX_P21 AC3 SER B 209 ? ARG B 213 ? SER B 209 ARG B 213 5 ? 5 HELX_P HELX_P22 AC4 GLN B 235 ? LYS B 241 ? GLN B 235 LYS B 241 5 ? 7 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 246 SG ? ? ? 1_555 B CYS 4 SG ? ? A CYS 246 B CYS 4 1_555 ? ? ? ? ? ? ? 2.078 ? disulf2 disulf ? ? B CYS 20 SG ? ? ? 1_555 B CYS 39 SG ? ? B CYS 20 B CYS 39 1_555 ? ? ? ? ? ? ? 2.040 ? disulf3 disulf ? ? B CYS 61 SG ? ? ? 1_555 B CYS 78 SG ? ? B CYS 61 B CYS 78 1_555 ? ? ? ? ? ? ? 2.040 ? disulf4 disulf ? ? B CYS 148 SG ? ? ? 1_555 B CYS 163 SG ? ? B CYS 148 B CYS 163 1_555 ? ? ? ? ? ? ? 2.075 ? disulf5 disulf ? ? B CYS 189 SG ? ? ? 1_555 B CYS 206 SG ? ? B CYS 189 B CYS 206 1_555 ? ? ? ? ? ? ? 2.041 ? disulf6 disulf ? ? A CYS 46 SG ? ? ? 1_555 A CYS 46 SG ? ? A CYS 46 A CYS 46 2_665 ? ? ? ? ? ? ? 1.869 ? covale1 covale one ? B ASN 97 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 97 B NAG 305 1_555 ? ? ? ? ? ? ? 1.393 ? covale2 covale one ? B ASN 114 ND2 ? ? ? 1_555 E NAG . C1 ? ? B ASN 114 B NAG 301 1_555 ? ? ? ? ? ? ? 1.363 ? covale3 covale one ? E NAG . O3 ? ? ? 1_555 F FUC . C1 ? ? B NAG 301 B FUC 302 1_555 ? ? ? ? ? ? ? 1.444 ? covale4 covale both ? H NAG . C1 ? ? ? 1_555 I NAG . O4 ? ? B NAG 304 B NAG 305 1_555 ? ? ? ? ? ? ? 1.449 ? covale5 covale none ? N A2G . O1 ? ? ? 1_555 O MBN . C ? ? B A2G 310 B MBN 311 1_555 ? ? ? ? ? ? ? 1.160 ? # 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 AA1 ? 6 ? AA2 ? 2 ? AA3 ? 7 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 2 ? AA7 ? 6 ? AA8 ? 2 ? AA9 ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA1 4 5 ? anti-parallel AA1 5 6 ? parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA3 2 3 ? anti-parallel AA3 3 4 ? anti-parallel AA3 4 5 ? anti-parallel AA3 5 6 ? anti-parallel AA3 6 7 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? anti-parallel AA6 1 2 ? anti-parallel AA7 1 2 ? anti-parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA7 5 6 ? anti-parallel AA8 1 2 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 LEU A 2 ? SER A 5 ? LEU A 2 SER A 5 AA1 2 PHE A 49 ? THR A 55 ? PHE A 49 THR A 55 AA1 3 THR A 61 ? ASN A 67 ? THR A 61 ASN A 67 AA1 4 GLY A 72 ? ALA A 78 ? GLY A 72 ALA A 78 AA1 5 ARG A 81 ? PHE A 84 ? ARG A 81 PHE A 84 AA1 6 ASN A 101 ? ILE A 104 ? ASN A 101 ILE A 104 AA2 1 VAL A 210 ? TYR A 218 ? VAL A 210 TYR A 218 AA2 2 PRO A 224 ? SER A 229 ? PRO A 224 SER A 229 AA3 1 ARG B 9 ? THR B 11 ? ARG B 9 THR B 11 AA3 2 TRP B 47 ? PHE B 49 ? TRP B 47 PHE B 49 AA3 3 ILE B 55 ? SER B 57 ? ILE B 55 SER B 57 AA3 4 LYS B 60 ? THR B 64 ? LYS B 60 THR B 64 AA3 5 VAL B 73 ? THR B 76 ? VAL B 73 THR B 76 AA3 6 SER B 32 ? TYR B 37 ? SER B 32 TYR B 37 AA3 7 CYS B 20 ? VAL B 23 ? CYS B 20 VAL B 23 AA4 1 ILE B 13 ? SER B 14 ? ILE B 13 SER B 14 AA4 2 ARG B 129 ? ILE B 130 ? ARG B 129 ILE B 130 AA5 1 TRP B 87 ? VAL B 89 ? TRP B 87 VAL B 89 AA5 2 MET B 95 ? ASN B 97 ? MET B 95 ASN B 97 AA6 1 LEU B 102 ? ALA B 106 ? LEU B 102 ALA B 106 AA6 2 LEU B 115 ? ASN B 119 ? LEU B 115 ASN B 119 AA7 1 VAL B 202 ? ARG B 205 ? VAL B 202 ARG B 205 AA7 2 ASN B 185 ? SER B 191 ? ASN B 185 SER B 191 AA7 3 ILE B 180 ? VAL B 182 ? ILE B 180 VAL B 182 AA7 4 TRP B 172 ? LEU B 174 ? TRP B 172 LEU B 174 AA7 5 ILE B 137 ? ILE B 142 ? ILE B 137 ILE B 142 AA7 6 THR B 258 ? PHE B 260 ? THR B 258 PHE B 260 AA8 1 MET B 147 ? THR B 152 ? MET B 147 THR B 152 AA8 2 ASN B 157 ? SER B 162 ? ASN B 157 SER B 162 AA9 1 VAL B 215 ? PHE B 216 ? VAL B 215 PHE B 216 AA9 2 ILE B 222 ? ASN B 224 ? ILE B 222 ASN B 224 AA9 3 ALA B 229 ? VAL B 233 ? ALA B 229 VAL B 233 AA9 4 ILE B 243 ? SER B 246 ? ILE B 243 SER B 246 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N LEU A 2 ? N LEU A 2 O ASP A 53 ? O ASP A 53 AA1 2 3 N LEU A 50 ? N LEU A 50 O ILE A 66 ? O ILE A 66 AA1 3 4 N ALA A 65 ? N ALA A 65 O ALA A 75 ? O ALA A 75 AA1 4 5 N ALA A 78 ? N ALA A 78 O ARG A 81 ? O ARG A 81 AA1 5 6 N PHE A 84 ? N PHE A 84 O ASN A 103 ? O ASN A 103 AA2 1 2 N VAL A 215 ? N VAL A 215 O VAL A 227 ? O VAL A 227 AA3 1 2 N THR B 11 ? N THR B 11 O TRP B 47 ? O TRP B 47 AA3 2 3 N THR B 48 ? N THR B 48 O ARG B 56 ? O ARG B 56 AA3 3 4 N ILE B 55 ? N ILE B 55 O LEU B 62 ? O LEU B 62 AA3 4 5 N ALA B 63 ? N ALA B 63 O VAL B 74 ? O VAL B 74 AA3 5 6 O VAL B 73 ? O VAL B 73 N VAL B 34 ? N VAL B 34 AA3 6 7 O ILE B 35 ? O ILE B 35 N ASP B 22 ? N ASP B 22 AA4 1 2 N SER B 14 ? N SER B 14 O ARG B 129 ? O ARG B 129 AA5 1 2 N MET B 88 ? N MET B 88 O MET B 96 ? O MET B 96 AA6 1 2 N VAL B 103 ? N VAL B 103 O GLU B 118 ? O GLU B 118 AA7 1 2 O VAL B 202 ? O VAL B 202 N SER B 191 ? N SER B 191 AA7 2 3 O VAL B 190 ? O VAL B 190 N ILE B 180 ? N ILE B 180 AA7 3 4 O ARG B 181 ? O ARG B 181 N ALA B 173 ? N ALA B 173 AA7 4 5 O TRP B 172 ? O TRP B 172 N THR B 139 ? N THR B 139 AA7 5 6 N ILE B 142 ? N ILE B 142 O THR B 258 ? O THR B 258 AA8 1 2 N CYS B 148 ? N CYS B 148 O GLU B 161 ? O GLU B 161 AA9 1 2 N VAL B 215 ? N VAL B 215 O SER B 223 ? O SER B 223 AA9 2 3 N ASN B 224 ? N ASN B 224 O ALA B 229 ? O ALA B 229 AA9 3 4 N VAL B 230 ? N VAL B 230 O SER B 246 ? O SER 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 A NAG 301 ? 3 'binding site for residue NAG A 301' AC2 Software A PO4 302 ? 5 'binding site for residue PO4 A 302' AC3 Software B NAG 303 ? 4 'binding site for residue NAG B 303' AC4 Software B BMA 306 ? 2 'binding site for residue BMA B 306' AC5 Software B EDO 307 ? 5 'binding site for residue EDO B 307' AC6 Software B PGE 308 ? 4 'binding site for residue PGE B 308' AC7 Software B GAL 309 ? 9 'binding site for residue GAL B 309' AC8 Software B ASN 97 ? 9 'binding site for Poly-Saccharide residues NAG B 304 through NAG B 305 bound to ASN B 97' AC9 Software B ASN 114 ? 7 'binding site for Poly-Saccharide residues NAG B 301 through FUC B 302 bound to ASN B 114' AD1 Software B A2G 310 ? 9 'binding site for Poly-Saccharide residues A2G B 310 through MBN B 311' # 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 3 GLN A 86 ? GLN A 86 . ? 1_555 ? 2 AC1 3 ASN A 108 ? ASN A 108 . ? 1_555 ? 3 AC1 3 HOH P . ? HOH A 467 . ? 1_555 ? 4 AC2 5 ILE A 45 ? ILE A 45 . ? 1_555 ? 5 AC2 5 ARG A 48 ? ARG A 48 . ? 1_555 ? 6 AC2 5 PRO A 89 ? PRO A 89 . ? 1_555 ? 7 AC2 5 PRO A 90 ? PRO A 90 . ? 1_555 ? 8 AC2 5 ILE A 91 ? ILE A 91 . ? 1_555 ? 9 AC3 4 NAG E . ? NAG B 301 . ? 1_555 ? 10 AC3 4 FUC F . ? FUC B 302 . ? 1_555 ? 11 AC3 4 BMA J . ? BMA B 306 . ? 1_555 ? 12 AC3 4 HOH Q . ? HOH B 522 . ? 1_555 ? 13 AC4 2 NAG G . ? NAG B 303 . ? 1_555 ? 14 AC4 2 HOH Q . ? HOH B 537 . ? 1_555 ? 15 AC5 5 ASN B 183 ? ASN B 183 . ? 1_555 ? 16 AC5 5 ASN B 184 ? ASN B 184 . ? 1_555 ? 17 AC5 5 ASN B 185 ? ASN B 185 . ? 1_555 ? 18 AC5 5 ARG B 186 ? ARG B 186 . ? 1_555 ? 19 AC5 5 PGE L . ? PGE B 308 . ? 1_555 ? 20 AC6 4 VAL B 138 ? VAL B 138 . ? 1_555 ? 21 AC6 4 ASN B 183 ? ASN B 183 . ? 1_555 ? 22 AC6 4 EDO K . ? EDO B 307 . ? 1_555 ? 23 AC6 4 HOH Q . ? HOH B 481 . ? 1_555 ? 24 AC7 9 ASP A 58 ? ASP A 58 . ? 3_556 ? 25 AC7 9 ASP B 22 ? ASP B 22 . ? 1_555 ? 26 AC7 9 VAL B 23 ? VAL B 23 . ? 1_555 ? 27 AC7 9 TYR B 24 ? TYR B 24 . ? 1_555 ? 28 AC7 9 GLY B 25 ? GLY B 25 . ? 1_555 ? 29 AC7 9 TYR B 37 ? TYR B 37 . ? 1_555 ? 30 AC7 9 GLN B 42 ? GLN B 42 . ? 1_555 ? 31 AC7 9 ASN B 44 ? ASN B 44 . ? 1_555 ? 32 AC7 9 A2G N . ? A2G B 310 . ? 1_555 ? 33 AC8 9 ALA B 63 ? ALA B 63 . ? 1_555 ? 34 AC8 9 THR B 64 ? THR B 64 . ? 1_555 ? 35 AC8 9 LEU B 67 ? LEU B 67 . ? 1_555 ? 36 AC8 9 LEU B 81 ? LEU B 81 . ? 1_555 ? 37 AC8 9 ASP B 84 ? ASP B 84 . ? 1_555 ? 38 AC8 9 TRP B 87 ? TRP B 87 . ? 1_555 ? 39 AC8 9 ASN B 97 ? ASN B 97 . ? 1_555 ? 40 AC8 9 SER B 100 ? SER B 100 . ? 1_555 ? 41 AC8 9 HOH Q . ? HOH B 441 . ? 1_555 ? 42 AC9 7 TYR A 146 ? TYR A 146 . ? 3_556 ? 43 AC9 7 ARG B 33 ? ARG B 33 . ? 1_555 ? 44 AC9 7 ASN B 72 ? ASN B 72 . ? 1_555 ? 45 AC9 7 ASN B 114 ? ASN B 114 . ? 1_555 ? 46 AC9 7 NAG G . ? NAG B 303 . ? 1_555 ? 47 AC9 7 HOH Q . ? HOH B 464 . ? 1_555 ? 48 AC9 7 HOH Q . ? HOH B 484 . ? 1_555 ? 49 AD1 9 SER A 5 ? SER A 5 . ? 3_556 ? 50 AD1 9 GLN A 6 ? GLN A 6 . ? 3_556 ? 51 AD1 9 SER A 7 ? SER A 7 . ? 3_556 ? 52 AD1 9 ASN A 56 ? ASN A 56 . ? 3_556 ? 53 AD1 9 GLY A 57 ? GLY A 57 . ? 3_556 ? 54 AD1 9 ASN A 59 ? ASN A 59 . ? 3_556 ? 55 AD1 9 GLU A 133 ? GLU A 133 . ? 3_556 ? 56 AD1 9 GLY B 25 ? GLY B 25 . ? 1_555 ? 57 AD1 9 GAL M . ? GAL B 309 . ? 1_555 ? # _atom_sites.entry_id 4ZBV _atom_sites.fract_transf_matrix[1][1] 0.007674 _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] 0.007225 _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] 0.022252 _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 N N . ASN A 1 1 ? 51.386 67.243 30.082 1.00 41.46 ? 1 ASN A N 1 ATOM 2 C CA . ASN A 1 1 ? 50.926 68.384 29.239 1.00 40.41 ? 1 ASN A CA 1 ATOM 3 C C . ASN A 1 1 ? 49.748 69.098 29.880 1.00 38.41 ? 1 ASN A C 1 ATOM 4 O O . ASN A 1 1 ? 48.960 68.484 30.595 1.00 39.56 ? 1 ASN A O 1 ATOM 5 C CB . ASN A 1 1 ? 50.512 67.898 27.843 1.00 41.17 ? 1 ASN A CB 1 ATOM 6 C CG . ASN A 1 1 ? 51.647 67.222 27.089 1.00 42.97 ? 1 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 1 ? 52.827 67.448 27.369 1.00 45.74 ? 1 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 1 ? 51.290 66.386 26.119 1.00 43.30 ? 1 ASN A ND2 1 ATOM 9 N N . LEU A 1 2 ? 49.631 70.394 29.608 1.00 36.54 ? 2 LEU A N 1 ATOM 10 C CA . LEU A 1 2 ? 48.467 71.183 30.024 1.00 34.86 ? 2 LEU A CA 1 ATOM 11 C C . LEU A 1 2 ? 47.232 70.574 29.369 1.00 32.29 ? 2 LEU A C 1 ATOM 12 O O . LEU A 1 2 ? 47.293 70.176 28.215 1.00 31.51 ? 2 LEU A O 1 ATOM 13 C CB . LEU A 1 2 ? 48.648 72.645 29.597 1.00 34.79 ? 2 LEU A CB 1 ATOM 14 C CG . LEU A 1 2 ? 47.623 73.678 30.062 1.00 35.95 ? 2 LEU A CG 1 ATOM 15 C CD1 . LEU A 1 2 ? 47.613 73.826 31.578 1.00 36.67 ? 2 LEU A CD1 1 ATOM 16 C CD2 . LEU A 1 2 ? 47.928 75.012 29.398 1.00 36.99 ? 2 LEU A CD2 1 ATOM 17 N N . SER A 1 3 ? 46.125 70.464 30.090 1.00 30.93 ? 3 SER A N 1 ATOM 18 C CA . SER A 1 3 ? 44.967 69.813 29.504 1.00 31.12 ? 3 SER A CA 1 ATOM 19 C C . SER A 1 3 ? 43.619 70.247 30.030 1.00 30.10 ? 3 SER A C 1 ATOM 20 O O . SER A 1 3 ? 43.503 70.838 31.095 1.00 30.19 ? 3 SER A O 1 ATOM 21 C CB . SER A 1 3 ? 45.101 68.298 29.659 1.00 32.05 ? 3 SER A CB 1 ATOM 22 O OG . SER A 1 3 ? 44.923 67.930 31.001 1.00 33.63 ? 3 SER A OG 1 ATOM 23 N N . LEU A 1 4 ? 42.602 69.907 29.250 1.00 30.55 ? 4 LEU A N 1 ATOM 24 C CA . LEU A 1 4 ? 41.212 70.194 29.557 1.00 31.63 ? 4 LEU A CA 1 ATOM 25 C C . LEU A 1 4 ? 40.370 68.999 29.132 1.00 32.36 ? 4 LEU A C 1 ATOM 26 O O . LEU A 1 4 ? 40.537 68.477 28.022 1.00 31.75 ? 4 LEU A O 1 ATOM 27 C CB . LEU A 1 4 ? 40.787 71.451 28.802 1.00 32.34 ? 4 LEU A CB 1 ATOM 28 C CG . LEU A 1 4 ? 39.444 72.118 29.108 1.00 33.75 ? 4 LEU A CG 1 ATOM 29 C CD1 . LEU A 1 4 ? 39.307 72.585 30.555 1.00 34.27 ? 4 LEU A CD1 1 ATOM 30 C CD2 . LEU A 1 4 ? 39.252 73.287 28.157 1.00 34.27 ? 4 LEU A CD2 1 ATOM 31 N N . SER A 1 5 ? 39.468 68.565 30.007 1.00 34.30 ? 5 SER A N 1 ATOM 32 C CA . SER A 1 5 ? 38.623 67.402 29.734 1.00 36.25 ? 5 SER A CA 1 ATOM 33 C C . SER A 1 5 ? 37.139 67.711 29.864 1.00 38.50 ? 5 SER A C 1 ATOM 34 O O . SER A 1 5 ? 36.731 68.559 30.656 1.00 37.27 ? 5 SER A O 1 ATOM 35 C CB . SER A 1 5 ? 38.983 66.247 30.666 1.00 35.49 ? 5 SER A CB 1 ATOM 36 O OG . SER A 1 5 ? 38.178 65.121 30.391 1.00 34.38 ? 5 SER A OG 1 ATOM 37 N N . GLN A 1 6 ? 36.336 66.981 29.093 1.00 40.93 ? 6 GLN A N 1 ATOM 38 C CA . GLN A 1 6 ? 34.881 67.075 29.188 1.00 42.19 ? 6 GLN A CA 1 ATOM 39 C C . GLN A 1 6 ? 34.312 66.542 30.501 1.00 43.57 ? 6 GLN A C 1 ATOM 40 O O . GLN A 1 6 ? 33.204 66.937 30.887 1.00 43.04 ? 6 GLN A O 1 ATOM 41 C CB . GLN A 1 6 ? 34.215 66.379 27.998 1.00 42.11 ? 6 GLN A CB 1 ATOM 42 C CG . GLN A 1 6 ? 34.444 67.127 26.699 1.00 43.36 ? 6 GLN A CG 1 ATOM 43 C CD . GLN A 1 6 ? 33.981 68.574 26.771 1.00 42.79 ? 6 GLN A CD 1 ATOM 44 O OE1 . GLN A 1 6 ? 32.805 68.849 27.033 1.00 43.65 ? 6 GLN A OE1 1 ATOM 45 N NE2 . GLN A 1 6 ? 34.903 69.503 26.562 1.00 43.08 ? 6 GLN A NE2 1 ATOM 46 N N . SER A 1 7 ? 35.061 65.670 31.183 1.00 44.65 ? 7 SER A N 1 ATOM 47 C CA . SER A 1 7 ? 34.687 65.212 32.535 1.00 48.11 ? 7 SER A CA 1 ATOM 48 C C . SER A 1 7 ? 34.434 66.377 33.491 1.00 47.48 ? 7 SER A C 1 ATOM 49 O O . SER A 1 7 ? 33.461 66.371 34.241 1.00 50.05 ? 7 SER A O 1 ATOM 50 C CB . SER A 1 7 ? 35.763 64.292 33.135 1.00 46.46 ? 7 SER A CB 1 ATOM 51 O OG . SER A 1 7 ? 36.985 64.979 33.350 1.00 47.54 ? 7 SER A OG 1 ATOM 52 N N . ASN A 1 8 ? 35.324 67.364 33.444 1.00 48.44 ? 8 ASN A N 1 ATOM 53 C CA . ASN A 1 8 ? 35.255 68.540 34.297 1.00 48.97 ? 8 ASN A CA 1 ATOM 54 C C . ASN A 1 8 ? 35.499 69.785 33.438 1.00 46.79 ? 8 ASN A C 1 ATOM 55 O O . ASN A 1 8 ? 36.611 70.332 33.388 1.00 46.44 ? 8 ASN A O 1 ATOM 56 C CB . ASN A 1 8 ? 36.278 68.401 35.430 1.00 51.57 ? 8 ASN A CB 1 ATOM 57 C CG . ASN A 1 8 ? 36.162 69.497 36.472 1.00 55.31 ? 8 ASN A CG 1 ATOM 58 O OD1 . ASN A 1 8 ? 35.066 69.995 36.765 1.00 54.22 ? 8 ASN A OD1 1 ATOM 59 N ND2 . ASN A 1 8 ? 37.303 69.876 37.053 1.00 58.00 ? 8 ASN A ND2 1 ATOM 60 N N . PHE A 1 9 ? 34.439 70.187 32.735 1.00 42.75 ? 9 PHE A N 1 ATOM 61 C CA . PHE A 1 9 ? 34.466 71.316 31.824 1.00 39.87 ? 9 PHE A CA 1 ATOM 62 C C . PHE A 1 9 ? 33.437 72.340 32.285 1.00 35.89 ? 9 PHE A C 1 ATOM 63 O O . PHE A 1 9 ? 32.274 72.279 31.911 1.00 37.44 ? 9 PHE A O 1 ATOM 64 C CB . PHE A 1 9 ? 34.183 70.855 30.395 1.00 40.86 ? 9 PHE A CB 1 ATOM 65 C CG . PHE A 1 9 ? 34.373 71.936 29.358 1.00 42.73 ? 9 PHE A CG 1 ATOM 66 C CD1 . PHE A 1 9 ? 35.630 72.191 28.821 1.00 43.66 ? 9 PHE A CD1 1 ATOM 67 C CD2 . PHE A 1 9 ? 33.296 72.692 28.909 1.00 43.13 ? 9 PHE A CD2 1 ATOM 68 C CE1 . PHE A 1 9 ? 35.802 73.174 27.859 1.00 43.57 ? 9 PHE A CE1 1 ATOM 69 C CE2 . PHE A 1 9 ? 33.470 73.674 27.950 1.00 43.36 ? 9 PHE A CE2 1 ATOM 70 C CZ . PHE A 1 9 ? 34.724 73.915 27.426 1.00 43.62 ? 9 PHE A CZ 1 ATOM 71 N N . SER A 1 10 ? 33.876 73.276 33.113 1.00 31.72 ? 10 SER A N 1 ATOM 72 C CA . SER A 1 10 ? 33.010 74.331 33.627 1.00 29.86 ? 10 SER A CA 1 ATOM 73 C C . SER A 1 10 ? 33.638 75.652 33.282 1.00 28.42 ? 10 SER A C 1 ATOM 74 O O . SER A 1 10 ? 34.794 75.706 32.848 1.00 28.03 ? 10 SER A O 1 ATOM 75 C CB . SER A 1 10 ? 32.900 74.227 35.148 1.00 28.83 ? 10 SER A CB 1 ATOM 76 O OG . SER A 1 10 ? 34.176 74.409 35.740 1.00 27.80 ? 10 SER A OG 1 ATOM 77 N N . ALA A 1 11 ? 32.889 76.718 33.518 1.00 27.80 ? 11 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? 33.439 78.069 33.426 1.00 26.83 ? 11 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? 34.796 78.190 34.151 1.00 26.06 ? 11 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? 35.759 78.741 33.596 1.00 25.40 ? 11 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? 32.441 79.086 33.966 1.00 26.86 ? 11 ALA A CB 1 ATOM 82 N N . ASP A 1 12 ? 34.880 77.653 35.372 1.00 24.99 ? 12 ASP A N 1 ATOM 83 C CA . ASP A 1 12 ? 36.121 77.720 36.160 1.00 23.75 ? 12 ASP A CA 1 ATOM 84 C C . ASP A 1 12 ? 37.276 76.946 35.534 1.00 22.81 ? 12 ASP A C 1 ATOM 85 O O . ASP A 1 12 ? 38.398 77.438 35.459 1.00 22.24 ? 12 ASP A O 1 ATOM 86 C CB . ASP A 1 12 ? 35.897 77.179 37.575 1.00 25.03 ? 12 ASP A CB 1 ATOM 87 C CG . ASP A 1 12 ? 35.084 78.104 38.446 1.00 25.95 ? 12 ASP A CG 1 ATOM 88 O OD1 . ASP A 1 12 ? 34.879 79.296 38.117 1.00 26.35 ? 12 ASP A OD1 1 ATOM 89 O OD2 . ASP A 1 12 ? 34.664 77.624 39.515 1.00 29.86 ? 12 ASP A OD2 1 ATOM 90 N N . THR A 1 13 ? 37.013 75.719 35.110 1.00 21.56 ? 13 THR A N 1 ATOM 91 C CA . THR A 1 13 ? 38.084 74.875 34.596 1.00 21.14 ? 13 THR A CA 1 ATOM 92 C C . THR A 1 13 ? 38.549 75.394 33.241 1.00 20.77 ? 13 THR A C 1 ATOM 93 O O . THR A 1 13 ? 39.732 75.374 32.945 1.00 20.44 ? 13 THR A O 1 ATOM 94 C CB . THR A 1 13 ? 37.702 73.371 34.549 1.00 20.89 ? 13 THR A CB 1 ATOM 95 O OG1 . THR A 1 13 ? 36.650 73.137 33.612 1.00 21.35 ? 13 THR A OG1 1 ATOM 96 C CG2 . THR A 1 13 ? 37.246 72.908 35.908 1.00 20.89 ? 13 THR A CG2 1 ATOM 97 N N . TYR A 1 14 ? 37.620 75.904 32.443 1.00 20.73 ? 14 TYR A N 1 ATOM 98 C CA . TYR A 1 14 ? 37.980 76.547 31.181 1.00 21.35 ? 14 TYR A CA 1 ATOM 99 C C . TYR A 1 14 ? 38.871 77.784 31.395 1.00 21.49 ? 14 TYR A C 1 ATOM 100 O O . TYR A 1 14 ? 39.907 77.939 30.740 1.00 20.51 ? 14 TYR A O 1 ATOM 101 C CB . TYR A 1 14 ? 36.719 76.942 30.398 1.00 20.97 ? 14 TYR A CB 1 ATOM 102 C CG . TYR A 1 14 ? 37.043 77.678 29.127 1.00 20.41 ? 14 TYR A CG 1 ATOM 103 C CD1 . TYR A 1 14 ? 37.576 77.006 28.034 1.00 20.25 ? 14 TYR A CD1 1 ATOM 104 C CD2 . TYR A 1 14 ? 36.865 79.055 29.036 1.00 20.65 ? 14 TYR A CD2 1 ATOM 105 C CE1 . TYR A 1 14 ? 37.884 77.675 26.866 1.00 20.09 ? 14 TYR A CE1 1 ATOM 106 C CE2 . TYR A 1 14 ? 37.175 79.736 27.878 1.00 20.68 ? 14 TYR A CE2 1 ATOM 107 C CZ . TYR A 1 14 ? 37.683 79.044 26.796 1.00 20.44 ? 14 TYR A CZ 1 ATOM 108 O OH . TYR A 1 14 ? 37.983 79.728 25.651 1.00 19.74 ? 14 TYR A OH 1 ATOM 109 N N . LYS A 1 15 ? 38.444 78.648 32.307 1.00 22.17 ? 15 LYS A N 1 ATOM 110 C CA . LYS A 1 15 ? 39.205 79.843 32.681 1.00 23.40 ? 15 LYS A CA 1 ATOM 111 C C . LYS A 1 15 ? 40.616 79.498 33.174 1.00 23.24 ? 15 LYS A C 1 ATOM 112 O O . LYS A 1 15 ? 41.574 80.142 32.781 1.00 21.31 ? 15 LYS A O 1 ATOM 113 C CB . LYS A 1 15 ? 38.439 80.635 33.752 1.00 25.66 ? 15 LYS A CB 1 ATOM 114 C CG . LYS A 1 15 ? 39.011 82.016 34.048 1.00 27.31 ? 15 LYS A CG 1 ATOM 115 C CD . LYS A 1 15 ? 38.017 82.883 34.811 1.00 28.80 ? 15 LYS A CD 1 ATOM 116 C CE . LYS A 1 15 ? 38.442 84.335 34.806 1.00 29.74 ? 15 LYS A CE 1 ATOM 117 N NZ . LYS A 1 15 ? 38.236 84.979 33.480 1.00 30.05 ? 15 LYS A NZ 1 ATOM 118 N N . SER A 1 16 ? 40.739 78.453 34.002 1.00 23.61 ? 16 SER A N 1 ATOM 119 C CA . SER A 1 16 ? 42.040 78.031 34.519 1.00 23.76 ? 16 SER A CA 1 ATOM 120 C C . SER A 1 16 ? 42.956 77.539 33.416 1.00 22.72 ? 16 SER A C 1 ATOM 121 O O . SER A 1 16 ? 44.149 77.845 33.393 1.00 21.19 ? 16 SER A O 1 ATOM 122 C CB . SER A 1 16 ? 41.881 76.923 35.539 1.00 24.64 ? 16 SER A CB 1 ATOM 123 O OG . SER A 1 16 ? 40.995 77.333 36.546 1.00 27.68 ? 16 SER A OG 1 ATOM 124 N N . PHE A 1 17 ? 42.389 76.744 32.524 1.00 23.32 ? 17 PHE A N 1 ATOM 125 C CA . PHE A 1 17 ? 43.108 76.250 31.364 1.00 23.59 ? 17 PHE A CA 1 ATOM 126 C C . PHE A 1 17 ? 43.654 77.379 30.471 1.00 23.21 ? 17 PHE A C 1 ATOM 127 O O . PHE A 1 17 ? 44.838 77.397 30.127 1.00 23.65 ? 17 PHE A O 1 ATOM 128 C CB . PHE A 1 17 ? 42.195 75.313 30.585 1.00 24.09 ? 17 PHE A CB 1 ATOM 129 C CG . PHE A 1 17 ? 42.749 74.891 29.268 1.00 24.31 ? 17 PHE A CG 1 ATOM 130 C CD1 . PHE A 1 17 ? 43.744 73.934 29.198 1.00 24.54 ? 17 PHE A CD1 1 ATOM 131 C CD2 . PHE A 1 17 ? 42.273 75.466 28.090 1.00 24.82 ? 17 PHE A CD2 1 ATOM 132 C CE1 . PHE A 1 17 ? 44.248 73.545 27.970 1.00 25.45 ? 17 PHE A CE1 1 ATOM 133 C CE2 . PHE A 1 17 ? 42.771 75.086 26.867 1.00 24.76 ? 17 PHE A CE2 1 ATOM 134 C CZ . PHE A 1 17 ? 43.762 74.129 26.805 1.00 25.50 ? 17 PHE A CZ 1 ATOM 135 N N . ILE A 1 18 ? 42.798 78.332 30.128 1.00 23.49 ? 18 ILE A N 1 ATOM 136 C CA . ILE A 1 18 ? 43.222 79.490 29.325 1.00 22.96 ? 18 ILE A CA 1 ATOM 137 C C . ILE A 1 18 ? 44.283 80.294 30.072 1.00 23.31 ? 18 ILE A C 1 ATOM 138 O O . ILE A 1 18 ? 45.296 80.669 29.494 1.00 22.99 ? 18 ILE A O 1 ATOM 139 C CB . ILE A 1 18 ? 42.021 80.390 28.934 1.00 22.53 ? 18 ILE A CB 1 ATOM 140 C CG1 . ILE A 1 18 ? 41.057 79.631 28.001 1.00 22.10 ? 18 ILE A CG1 1 ATOM 141 C CG2 . ILE A 1 18 ? 42.489 81.706 28.293 1.00 22.17 ? 18 ILE A CG2 1 ATOM 142 C CD1 . ILE A 1 18 ? 41.655 79.150 26.689 1.00 21.96 ? 18 ILE A CD1 1 ATOM 143 N N . LYS A 1 19 ? 44.058 80.517 31.363 1.00 25.26 ? 19 LYS A N 1 ATOM 144 C CA . LYS A 1 19 ? 45.019 81.223 32.220 1.00 26.85 ? 19 LYS A CA 1 ATOM 145 C C . LYS A 1 19 ? 46.391 80.559 32.189 1.00 25.65 ? 19 LYS A C 1 ATOM 146 O O . LYS A 1 19 ? 47.401 81.230 31.952 1.00 24.99 ? 19 LYS A O 1 ATOM 147 C CB . LYS A 1 19 ? 44.491 81.308 33.668 1.00 29.48 ? 19 LYS A CB 1 ATOM 148 C CG . LYS A 1 19 ? 45.298 82.200 34.599 1.00 32.95 ? 19 LYS A CG 1 ATOM 149 C CD . LYS A 1 19 ? 45.015 81.898 36.069 1.00 35.97 ? 19 LYS A CD 1 ATOM 150 C CE . LYS A 1 19 ? 46.050 82.567 36.968 1.00 38.63 ? 19 LYS A CE 1 ATOM 151 N NZ . LYS A 1 19 ? 45.672 82.594 38.412 1.00 39.57 ? 19 LYS A NZ 1 ATOM 152 N N . ASN A 1 20 ? 46.435 79.242 32.390 1.00 24.86 ? 20 ASN A N 1 ATOM 153 C CA . ASN A 1 20 ? 47.717 78.535 32.367 1.00 24.72 ? 20 ASN A CA 1 ATOM 154 C C . ASN A 1 20 ? 48.326 78.456 30.981 1.00 23.48 ? 20 ASN A C 1 ATOM 155 O O . ASN A 1 20 ? 49.545 78.532 30.842 1.00 23.01 ? 20 ASN A O 1 ATOM 156 C CB . ASN A 1 20 ? 47.601 77.146 32.966 1.00 26.25 ? 20 ASN A CB 1 ATOM 157 C CG . ASN A 1 20 ? 47.318 77.172 34.460 1.00 28.97 ? 20 ASN A CG 1 ATOM 158 O OD1 . ASN A 1 20 ? 47.645 78.131 35.172 1.00 30.33 ? 20 ASN A OD1 1 ATOM 159 N ND2 . ASN A 1 20 ? 46.711 76.098 34.949 1.00 31.03 ? 20 ASN A ND2 1 ATOM 160 N N . LEU A 1 21 ? 47.493 78.317 29.955 1.00 22.68 ? 21 LEU A N 1 ATOM 161 C CA . LEU A 1 21 ? 47.988 78.378 28.571 1.00 21.66 ? 21 LEU A CA 1 ATOM 162 C C . LEU A 1 21 ? 48.733 79.698 28.317 1.00 21.07 ? 21 LEU A C 1 ATOM 163 O O . LEU A 1 21 ? 49.851 79.682 27.797 1.00 20.24 ? 21 LEU A O 1 ATOM 164 C CB . LEU A 1 21 ? 46.848 78.185 27.567 1.00 21.62 ? 21 LEU A CB 1 ATOM 165 C CG . LEU A 1 21 ? 47.173 78.212 26.062 1.00 21.68 ? 21 LEU A CG 1 ATOM 166 C CD1 . LEU A 1 21 ? 48.339 77.283 25.730 1.00 21.36 ? 21 LEU A CD1 1 ATOM 167 C CD2 . LEU A 1 21 ? 45.936 77.822 25.260 1.00 21.40 ? 21 LEU A CD2 1 ATOM 168 N N . ARG A 1 22 ? 48.150 80.826 28.725 1.00 21.03 ? 22 ARG A N 1 ATOM 169 C CA . ARG A 1 22 ? 48.852 82.120 28.590 1.00 21.25 ? 22 ARG A CA 1 ATOM 170 C C . ARG A 1 22 ? 50.192 82.128 29.328 1.00 22.18 ? 22 ARG A C 1 ATOM 171 O O . ARG A 1 22 ? 51.195 82.622 28.798 1.00 20.56 ? 22 ARG A O 1 ATOM 172 C CB . ARG A 1 22 ? 48.004 83.283 29.092 1.00 20.99 ? 22 ARG A CB 1 ATOM 173 C CG . ARG A 1 22 ? 46.837 83.638 28.192 1.00 20.71 ? 22 ARG A CG 1 ATOM 174 C CD . ARG A 1 22 ? 45.867 84.545 28.915 1.00 19.77 ? 22 ARG A CD 1 ATOM 175 N NE . ARG A 1 22 ? 44.642 84.729 28.150 1.00 18.67 ? 22 ARG A NE 1 ATOM 176 C CZ . ARG A 1 22 ? 43.438 84.961 28.673 1.00 18.52 ? 22 ARG A CZ 1 ATOM 177 N NH1 . ARG A 1 22 ? 43.248 85.056 29.998 1.00 18.73 ? 22 ARG A NH1 1 ATOM 178 N NH2 . ARG A 1 22 ? 42.393 85.099 27.863 1.00 18.07 ? 22 ARG A NH2 1 ATOM 179 N N . LYS A 1 23 ? 50.204 81.562 30.535 1.00 24.24 ? 23 LYS A N 1 ATOM 180 C CA . LYS A 1 23 ? 51.428 81.488 31.320 1.00 26.97 ? 23 LYS A CA 1 ATOM 181 C C . LYS A 1 23 ? 52.520 80.727 30.590 1.00 26.34 ? 23 LYS A C 1 ATOM 182 O O . LYS A 1 23 ? 53.625 81.254 30.437 1.00 24.67 ? 23 LYS A O 1 ATOM 183 C CB . LYS A 1 23 ? 51.179 80.885 32.709 1.00 30.69 ? 23 LYS A CB 1 ATOM 184 C CG . LYS A 1 23 ? 50.446 81.848 33.625 1.00 35.42 ? 23 LYS A CG 1 ATOM 185 C CD . LYS A 1 23 ? 50.270 81.299 35.034 1.00 39.08 ? 23 LYS A CD 1 ATOM 186 C CE . LYS A 1 23 ? 49.599 82.328 35.932 1.00 41.61 ? 23 LYS A CE 1 ATOM 187 N NZ . LYS A 1 23 ? 49.497 81.848 37.340 1.00 43.10 ? 23 LYS A NZ 1 ATOM 188 N N . GLN A 1 24 ? 52.210 79.521 30.114 1.00 26.91 ? 24 GLN A N 1 ATOM 189 C CA . GLN A 1 24 ? 53.220 78.703 29.412 1.00 28.85 ? 24 GLN A CA 1 ATOM 190 C C . GLN A 1 24 ? 53.744 79.433 28.187 1.00 26.31 ? 24 GLN A C 1 ATOM 191 O O . GLN A 1 24 ? 54.944 79.441 27.931 1.00 24.72 ? 24 GLN A O 1 ATOM 192 C CB . GLN A 1 24 ? 52.669 77.339 28.949 1.00 32.14 ? 24 GLN A CB 1 ATOM 193 C CG . GLN A 1 24 ? 52.034 76.440 29.998 1.00 35.59 ? 24 GLN A CG 1 ATOM 194 C CD . GLN A 1 24 ? 52.660 76.582 31.364 1.00 41.02 ? 24 GLN A CD 1 ATOM 195 O OE1 . GLN A 1 24 ? 52.012 77.044 32.315 1.00 48.20 ? 24 GLN A OE1 1 ATOM 196 N NE2 . GLN A 1 24 ? 53.937 76.219 31.471 1.00 43.54 ? 24 GLN A NE2 1 ATOM 197 N N . LEU A 1 25 ? 52.833 80.050 27.439 1.00 25.16 ? 25 LEU A N 1 ATOM 198 C CA . LEU A 1 25 ? 53.203 80.749 26.211 1.00 24.74 ? 25 LEU A CA 1 ATOM 199 C C . LEU A 1 25 ? 54.061 81.978 26.460 1.00 24.14 ? 25 LEU A C 1 ATOM 200 O O . LEU A 1 25 ? 54.872 82.334 25.604 1.00 23.49 ? 25 LEU A O 1 ATOM 201 C CB . LEU A 1 25 ? 51.970 81.159 25.418 1.00 25.05 ? 25 LEU A CB 1 ATOM 202 C CG . LEU A 1 25 ? 51.294 80.066 24.603 1.00 25.26 ? 25 LEU A CG 1 ATOM 203 C CD1 . LEU A 1 25 ? 49.965 80.592 24.078 1.00 25.53 ? 25 LEU A CD1 1 ATOM 204 C CD2 . LEU A 1 25 ? 52.173 79.618 23.448 1.00 25.67 ? 25 LEU A CD2 1 ATOM 205 N N . THR A 1 26 ? 53.885 82.613 27.618 1.00 23.57 ? 26 THR A N 1 ATOM 206 C CA . THR A 1 26 ? 54.601 83.850 27.936 1.00 24.04 ? 26 THR A CA 1 ATOM 207 C C . THR A 1 26 ? 55.839 83.635 28.809 1.00 24.99 ? 26 THR A C 1 ATOM 208 O O . THR A 1 26 ? 56.416 84.598 29.292 1.00 26.40 ? 26 THR A O 1 ATOM 209 C CB . THR A 1 26 ? 53.652 84.916 28.550 1.00 23.43 ? 26 THR A CB 1 ATOM 210 O OG1 . THR A 1 26 ? 52.961 84.391 29.688 1.00 22.27 ? 26 THR A OG1 1 ATOM 211 C CG2 . THR A 1 26 ? 52.622 85.368 27.529 1.00 22.73 ? 26 THR A CG2 1 ATOM 212 N N . ILE A 1 27 ? 56.276 82.387 28.980 1.00 26.18 ? 27 ILE A N 1 ATOM 213 C CA . ILE A 1 27 ? 57.600 82.100 29.566 1.00 26.55 ? 27 ILE A CA 1 ATOM 214 C C . ILE A 1 27 ? 58.644 82.720 28.648 1.00 26.22 ? 27 ILE A C 1 ATOM 215 O O . ILE A 1 27 ? 58.586 82.526 27.432 1.00 27.34 ? 27 ILE A O 1 ATOM 216 C CB . ILE A 1 27 ? 57.880 80.578 29.687 1.00 27.84 ? 27 ILE A CB 1 ATOM 217 C CG1 . ILE A 1 27 ? 56.956 79.930 30.722 1.00 27.72 ? 27 ILE A CG1 1 ATOM 218 C CG2 . ILE A 1 27 ? 59.339 80.318 30.066 1.00 28.87 ? 27 ILE A CG2 1 ATOM 219 C CD1 . ILE A 1 27 ? 56.839 78.428 30.582 1.00 28.35 ? 27 ILE A CD1 1 ATOM 220 N N . GLY A 1 28 ? 59.579 83.477 29.222 1.00 25.50 ? 28 GLY A N 1 ATOM 221 C CA . GLY A 1 28 ? 60.619 84.141 28.440 1.00 24.96 ? 28 GLY A CA 1 ATOM 222 C C . GLY A 1 28 ? 60.142 85.257 27.518 1.00 25.06 ? 28 GLY A C 1 ATOM 223 O O . GLY A 1 28 ? 60.846 85.637 26.580 1.00 24.67 ? 28 GLY A O 1 ATOM 224 N N . ALA A 1 29 ? 58.961 85.803 27.799 1.00 25.63 ? 29 ALA A N 1 ATOM 225 C CA . ALA A 1 29 ? 58.394 86.883 27.001 1.00 25.46 ? 29 ALA A CA 1 ATOM 226 C C . ALA A 1 29 ? 59.117 88.183 27.280 1.00 25.41 ? 29 ALA A C 1 ATOM 227 O O . ALA A 1 29 ? 59.561 88.420 28.401 1.00 25.49 ? 29 ALA A O 1 ATOM 228 C CB . ALA A 1 29 ? 56.924 87.047 27.332 1.00 26.28 ? 29 ALA A CB 1 ATOM 229 N N . SER A 1 30 ? 59.231 89.025 26.260 1.00 26.01 ? 30 SER A N 1 ATOM 230 C CA . SER A 1 30 ? 59.707 90.389 26.461 1.00 27.32 ? 30 SER A CA 1 ATOM 231 C C . SER A 1 30 ? 58.496 91.286 26.760 1.00 27.94 ? 30 SER A C 1 ATOM 232 O O . SER A 1 30 ? 57.349 90.880 26.536 1.00 26.62 ? 30 SER A O 1 ATOM 233 C CB . SER A 1 30 ? 60.518 90.876 25.263 1.00 27.31 ? 30 SER A CB 1 ATOM 234 O OG . SER A 1 30 ? 59.755 90.895 24.082 1.00 29.25 ? 30 SER A OG 1 ATOM 235 N N . TYR A 1 31 ? 58.763 92.463 27.327 1.00 27.20 ? 31 TYR A N 1 ATOM 236 C CA . TYR A 1 31 ? 57.728 93.430 27.701 1.00 28.60 ? 31 TYR A CA 1 ATOM 237 C C . TYR A 1 31 ? 58.089 94.830 27.221 1.00 28.84 ? 31 TYR A C 1 ATOM 238 O O . TYR A 1 31 ? 59.262 95.193 27.176 1.00 29.79 ? 31 TYR A O 1 ATOM 239 C CB . TYR A 1 31 ? 57.542 93.462 29.219 1.00 29.02 ? 31 TYR A CB 1 ATOM 240 C CG . TYR A 1 31 ? 56.931 92.211 29.779 1.00 28.81 ? 31 TYR A CG 1 ATOM 241 C CD1 . TYR A 1 31 ? 57.685 91.039 29.893 1.00 29.70 ? 31 TYR A CD1 1 ATOM 242 C CD2 . TYR A 1 31 ? 55.613 92.182 30.197 1.00 28.45 ? 31 TYR A CD2 1 ATOM 243 C CE1 . TYR A 1 31 ? 57.131 89.872 30.384 1.00 29.75 ? 31 TYR A CE1 1 ATOM 244 C CE2 . TYR A 1 31 ? 55.052 91.016 30.711 1.00 29.26 ? 31 TYR A CE2 1 ATOM 245 C CZ . TYR A 1 31 ? 55.822 89.869 30.804 1.00 29.74 ? 31 TYR A CZ 1 ATOM 246 O OH . TYR A 1 31 ? 55.298 88.704 31.299 1.00 31.89 ? 31 TYR A OH 1 ATOM 247 N N . GLY A 1 32 ? 57.068 95.609 26.872 1.00 29.59 ? 32 GLY A N 1 ATOM 248 C CA . GLY A 1 32 ? 57.227 97.022 26.490 1.00 29.69 ? 32 GLY A CA 1 ATOM 249 C C . GLY A 1 32 ? 56.522 97.936 27.476 1.00 29.20 ? 32 GLY A C 1 ATOM 250 O O . GLY A 1 32 ? 56.204 97.515 28.584 1.00 28.21 ? 32 GLY A O 1 ATOM 251 N N . SER A 1 33 ? 56.271 99.178 27.057 1.00 29.23 ? 33 SER A N 1 ATOM 252 C CA . SER A 1 33 ? 55.550 100.181 27.868 1.00 29.83 ? 33 SER A CA 1 ATOM 253 C C . SER A 1 33 ? 54.149 99.755 28.231 1.00 29.33 ? 33 SER A C 1 ATOM 254 O O . SER A 1 33 ? 53.676 100.032 29.335 1.00 29.38 ? 33 SER A O 1 ATOM 255 C CB . SER A 1 33 ? 55.425 101.503 27.109 1.00 29.43 ? 33 SER A CB 1 ATOM 256 O OG . SER A 1 33 ? 56.704 102.018 26.837 1.00 31.26 ? 33 SER A OG 1 ATOM 257 N N . ALA A 1 34 ? 53.479 99.111 27.282 1.00 27.80 ? 34 ALA A N 1 ATOM 258 C CA . ALA A 1 34 ? 52.131 98.616 27.496 1.00 27.76 ? 34 ALA A CA 1 ATOM 259 C C . ALA A 1 34 ? 52.048 97.540 28.568 1.00 26.90 ? 34 ALA A C 1 ATOM 260 O O . ALA A 1 34 ? 50.994 97.353 29.159 1.00 28.37 ? 34 ALA A O 1 ATOM 261 C CB . ALA A 1 34 ? 51.550 98.096 26.191 1.00 28.12 ? 34 ALA A CB 1 ATOM 262 N N . GLY A 1 35 ? 53.143 96.830 28.816 1.00 25.99 ? 35 GLY A N 1 ATOM 263 C CA . GLY A 1 35 ? 53.157 95.768 29.822 1.00 25.21 ? 35 GLY A CA 1 ATOM 264 C C . GLY A 1 35 ? 52.339 94.557 29.402 1.00 24.04 ? 35 GLY A C 1 ATOM 265 O O . GLY A 1 35 ? 51.843 93.835 30.252 1.00 23.62 ? 35 GLY A O 1 ATOM 266 N N . ILE A 1 36 ? 52.171 94.364 28.094 1.00 23.41 ? 36 ILE A N 1 ATOM 267 C CA . ILE A 1 36 ? 51.517 93.182 27.549 1.00 22.61 ? 36 ILE A CA 1 ATOM 268 C C . ILE A 1 36 ? 52.663 92.318 27.025 1.00 21.94 ? 36 ILE A C 1 ATOM 269 O O . ILE A 1 36 ? 53.411 92.758 26.157 1.00 21.58 ? 36 ILE A O 1 ATOM 270 C CB . ILE A 1 36 ? 50.539 93.512 26.393 1.00 22.35 ? 36 ILE A CB 1 ATOM 271 C CG1 . ILE A 1 36 ? 49.396 94.426 26.871 1.00 22.12 ? 36 ILE A CG1 1 ATOM 272 C CG2 . ILE A 1 36 ? 49.952 92.234 25.798 1.00 21.33 ? 36 ILE A CG2 1 ATOM 273 C CD1 . ILE A 1 36 ? 48.506 94.945 25.763 1.00 21.62 ? 36 ILE A CD1 1 ATOM 274 N N . PRO A 1 37 ? 52.805 91.086 27.538 1.00 21.33 ? 37 PRO A N 1 ATOM 275 C CA . PRO A 1 37 ? 53.937 90.260 27.106 1.00 21.40 ? 37 PRO A CA 1 ATOM 276 C C . PRO A 1 37 ? 53.987 89.986 25.593 1.00 21.18 ? 37 PRO A C 1 ATOM 277 O O . PRO A 1 37 ? 52.946 89.780 24.955 1.00 21.49 ? 37 PRO A O 1 ATOM 278 C CB . PRO A 1 37 ? 53.724 88.954 27.877 1.00 20.75 ? 37 PRO A CB 1 ATOM 279 C CG . PRO A 1 37 ? 52.273 88.918 28.154 1.00 21.10 ? 37 PRO A CG 1 ATOM 280 C CD . PRO A 1 37 ? 51.916 90.339 28.439 1.00 21.75 ? 37 PRO A CD 1 ATOM 281 N N . ILE A 1 38 ? 55.200 89.971 25.058 1.00 20.95 ? 38 ILE A N 1 ATOM 282 C CA . ILE A 1 38 ? 55.465 89.744 23.651 1.00 22.24 ? 38 ILE A CA 1 ATOM 283 C C . ILE A 1 38 ? 56.059 88.353 23.567 1.00 22.23 ? 38 ILE A C 1 ATOM 284 O O . ILE A 1 38 ? 56.982 88.038 24.310 1.00 22.11 ? 38 ILE A O 1 ATOM 285 C CB . ILE A 1 38 ? 56.514 90.742 23.132 1.00 23.77 ? 38 ILE A CB 1 ATOM 286 C CG1 . ILE A 1 38 ? 56.018 92.190 23.273 1.00 24.72 ? 38 ILE A CG1 1 ATOM 287 C CG2 . ILE A 1 38 ? 56.894 90.435 21.684 1.00 24.78 ? 38 ILE A CG2 1 ATOM 288 C CD1 . ILE A 1 38 ? 57.156 93.202 23.340 1.00 25.06 ? 38 ILE A CD1 1 ATOM 289 N N . LEU A 1 39 ? 55.541 87.523 22.675 1.00 23.17 ? 39 LEU A N 1 ATOM 290 C CA . LEU A 1 39 ? 55.994 86.134 22.572 1.00 23.09 ? 39 LEU A CA 1 ATOM 291 C C . LEU A 1 39 ? 57.435 86.036 22.123 1.00 23.68 ? 39 LEU A C 1 ATOM 292 O O . LEU A 1 39 ? 57.992 86.966 21.526 1.00 23.20 ? 39 LEU A O 1 ATOM 293 C CB . LEU A 1 39 ? 55.135 85.351 21.585 1.00 23.66 ? 39 LEU A CB 1 ATOM 294 C CG . LEU A 1 39 ? 53.678 85.134 21.964 1.00 23.35 ? 39 LEU A CG 1 ATOM 295 C CD1 . LEU A 1 39 ? 52.911 84.584 20.767 1.00 24.00 ? 39 LEU A CD1 1 ATOM 296 C CD2 . LEU A 1 39 ? 53.574 84.201 23.149 1.00 23.12 ? 39 LEU A CD2 1 ATOM 297 N N . LYS A 1 40 ? 58.021 84.875 22.392 1.00 25.09 ? 40 LYS A N 1 ATOM 298 C CA . LYS A 1 40 ? 59.403 84.598 22.015 1.00 25.32 ? 40 LYS A CA 1 ATOM 299 C C . LYS A 1 40 ? 59.553 84.526 20.494 1.00 25.71 ? 40 LYS A C 1 ATOM 300 O O . LYS A 1 40 ? 58.610 84.205 19.776 1.00 25.22 ? 40 LYS A O 1 ATOM 301 C CB . LYS A 1 40 ? 59.887 83.291 22.648 1.00 25.29 ? 40 LYS A CB 1 ATOM 302 C CG . LYS A 1 40 ? 59.930 83.325 24.164 1.00 25.93 ? 40 LYS A CG 1 ATOM 303 C CD . LYS A 1 40 ? 60.516 82.050 24.776 1.00 26.68 ? 40 LYS A CD 1 ATOM 304 C CE . LYS A 1 40 ? 59.606 80.834 24.630 1.00 26.70 ? 40 LYS A CE 1 ATOM 305 N NZ . LYS A 1 40 ? 58.223 81.033 25.164 1.00 26.73 ? 40 LYS A NZ 1 ATOM 306 N N . HIS A 1 41 ? 60.751 84.831 20.021 1.00 27.00 ? 41 HIS A N 1 ATOM 307 C CA . HIS A 1 41 ? 61.069 84.793 18.598 1.00 28.96 ? 41 HIS A CA 1 ATOM 308 C C . HIS A 1 41 ? 62.434 84.133 18.442 1.00 29.07 ? 41 HIS A C 1 ATOM 309 O O . HIS A 1 41 ? 63.217 84.098 19.394 1.00 28.07 ? 41 HIS A O 1 ATOM 310 C CB . HIS A 1 41 ? 61.100 86.219 18.028 1.00 29.48 ? 41 HIS A CB 1 ATOM 311 C CG . HIS A 1 41 ? 62.121 87.092 18.681 1.00 30.12 ? 41 HIS A CG 1 ATOM 312 N ND1 . HIS A 1 41 ? 61.909 87.691 19.904 1.00 32.25 ? 41 HIS A ND1 1 ATOM 313 C CD2 . HIS A 1 41 ? 63.387 87.412 18.319 1.00 31.54 ? 41 HIS A CD2 1 ATOM 314 C CE1 . HIS A 1 41 ? 62.987 88.373 20.253 1.00 32.11 ? 41 HIS A CE1 1 ATOM 315 N NE2 . HIS A 1 41 ? 63.901 88.213 19.312 1.00 31.79 ? 41 HIS A NE2 1 ATOM 316 N N . SER A 1 42 ? 62.712 83.626 17.239 1.00 31.19 ? 42 SER A N 1 ATOM 317 C CA . SER A 1 42 ? 63.955 82.883 16.958 1.00 31.77 ? 42 SER A CA 1 ATOM 318 C C . SER A 1 42 ? 64.147 81.735 17.958 1.00 30.75 ? 42 SER A C 1 ATOM 319 O O . SER A 1 42 ? 65.208 81.580 18.553 1.00 31.65 ? 42 SER A O 1 ATOM 320 C CB . SER A 1 42 ? 65.159 83.829 16.986 1.00 33.56 ? 42 SER A CB 1 ATOM 321 O OG . SER A 1 42 ? 64.944 84.943 16.138 1.00 36.63 ? 42 SER A OG 1 ATOM 322 N N . VAL A 1 43 ? 63.093 80.961 18.176 1.00 30.21 ? 43 VAL A N 1 ATOM 323 C CA . VAL A 1 43 ? 63.156 79.828 19.084 1.00 30.02 ? 43 VAL A CA 1 ATOM 324 C C . VAL A 1 43 ? 63.720 78.636 18.306 1.00 29.07 ? 43 VAL A C 1 ATOM 325 O O . VAL A 1 43 ? 63.234 78.332 17.220 1.00 27.90 ? 43 VAL A O 1 ATOM 326 C CB . VAL A 1 43 ? 61.775 79.497 19.671 1.00 29.48 ? 43 VAL A CB 1 ATOM 327 C CG1 . VAL A 1 43 ? 61.823 78.232 20.516 1.00 29.89 ? 43 VAL A CG1 1 ATOM 328 C CG2 . VAL A 1 43 ? 61.279 80.669 20.509 1.00 30.77 ? 43 VAL A CG2 1 ATOM 329 N N . PRO A 1 44 ? 64.758 77.970 18.849 1.00 30.42 ? 44 PRO A N 1 ATOM 330 C CA . PRO A 1 44 ? 65.239 76.708 18.264 1.00 29.99 ? 44 PRO A CA 1 ATOM 331 C C . PRO A 1 44 ? 64.099 75.712 18.124 1.00 29.06 ? 44 PRO A C 1 ATOM 332 O O . PRO A 1 44 ? 63.325 75.545 19.054 1.00 30.22 ? 44 PRO A O 1 ATOM 333 C CB . PRO A 1 44 ? 66.255 76.197 19.291 1.00 30.64 ? 44 PRO A CB 1 ATOM 334 C CG . PRO A 1 44 ? 66.678 77.393 20.066 1.00 31.22 ? 44 PRO A CG 1 ATOM 335 C CD . PRO A 1 44 ? 65.543 78.370 20.033 1.00 30.93 ? 44 PRO A CD 1 ATOM 336 N N . ILE A 1 45 ? 64.005 75.068 16.971 1.00 29.85 ? 45 ILE A N 1 ATOM 337 C CA . ILE A 1 45 ? 62.893 74.169 16.644 1.00 30.65 ? 45 ILE A CA 1 ATOM 338 C C . ILE A 1 45 ? 62.612 73.086 17.696 1.00 31.48 ? 45 ILE A C 1 ATOM 339 O O . ILE A 1 45 ? 61.474 72.662 17.849 1.00 31.11 ? 45 ILE A O 1 ATOM 340 C CB . ILE A 1 45 ? 63.110 73.521 15.252 1.00 31.88 ? 45 ILE A CB 1 ATOM 341 C CG1 . ILE A 1 45 ? 61.822 72.893 14.710 1.00 32.37 ? 45 ILE A CG1 1 ATOM 342 C CG2 . ILE A 1 45 ? 64.252 72.505 15.275 1.00 32.76 ? 45 ILE A CG2 1 ATOM 343 C CD1 . ILE A 1 45 ? 60.817 73.903 14.217 1.00 32.90 ? 45 ILE A CD1 1 ATOM 344 N N . CYS A 1 46 ? 63.617 72.670 18.426 1.00 33.28 ? 46 CYS A N 1 ATOM 345 C CA . CYS A 1 46 ? 63.475 71.685 19.468 1.00 34.64 ? 46 CYS A CA 1 ATOM 346 C C . CYS A 1 46 ? 62.629 72.188 20.636 1.00 34.45 ? 46 CYS A C 1 ATOM 347 O O . CYS A 1 46 ? 61.998 71.409 21.273 1.00 34.00 ? 46 CYS A O 1 ATOM 348 C CB . CYS A 1 46 ? 64.854 71.165 19.916 1.00 34.65 ? 46 CYS A CB 1 ATOM 349 S SG . CYS A 1 46 ? 65.623 70.009 18.759 1.00 41.41 ? 46 CYS A SG 1 ATOM 350 N N . GLU A 1 47 ? 62.605 73.491 20.884 1.00 35.42 ? 47 GLU A N 1 ATOM 351 C CA . GLU A 1 47 ? 61.826 74.092 21.976 1.00 36.32 ? 47 GLU A CA 1 ATOM 352 C C . GLU A 1 47 ? 60.653 74.972 21.495 1.00 34.04 ? 47 GLU A C 1 ATOM 353 O O . GLU A 1 47 ? 60.030 75.666 22.303 1.00 33.99 ? 47 GLU A O 1 ATOM 354 C CB . GLU A 1 47 ? 62.751 74.952 22.847 1.00 39.38 ? 47 GLU A CB 1 ATOM 355 C CG . GLU A 1 47 ? 64.019 74.256 23.327 1.00 42.45 ? 47 GLU A CG 1 ATOM 356 C CD . GLU A 1 47 ? 65.238 75.151 23.215 1.00 45.99 ? 47 GLU A CD 1 ATOM 357 O OE1 . GLU A 1 47 ? 65.194 76.299 23.723 1.00 44.66 ? 47 GLU A OE1 1 ATOM 358 O OE2 . GLU A 1 47 ? 66.239 74.706 22.607 1.00 50.95 ? 47 GLU A OE2 1 ATOM 359 N N . ARG A 1 48 ? 60.338 74.942 20.203 1.00 30.86 ? 48 ARG A N 1 ATOM 360 C CA . ARG A 1 48 ? 59.338 75.855 19.661 1.00 29.32 ? 48 ARG A CA 1 ATOM 361 C C . ARG A 1 48 ? 57.885 75.406 19.884 1.00 28.13 ? 48 ARG A C 1 ATOM 362 O O . ARG A 1 48 ? 56.964 76.185 19.652 1.00 26.14 ? 48 ARG A O 1 ATOM 363 C CB . ARG A 1 48 ? 59.584 76.099 18.173 1.00 29.40 ? 48 ARG A CB 1 ATOM 364 C CG . ARG A 1 48 ? 58.969 77.405 17.679 1.00 29.27 ? 48 ARG A CG 1 ATOM 365 C CD . ARG A 1 48 ? 59.285 77.678 16.230 1.00 28.90 ? 48 ARG A CD 1 ATOM 366 N NE . ARG A 1 48 ? 60.719 77.607 15.987 1.00 28.88 ? 48 ARG A NE 1 ATOM 367 C CZ . ARG A 1 48 ? 61.272 77.438 14.790 1.00 28.91 ? 48 ARG A CZ 1 ATOM 368 N NH1 . ARG A 1 48 ? 62.587 77.355 14.698 1.00 29.28 ? 48 ARG A NH1 1 ATOM 369 N NH2 . ARG A 1 48 ? 60.530 77.345 13.685 1.00 29.56 ? 48 ARG A NH2 1 ATOM 370 N N . PHE A 1 49 ? 57.667 74.171 20.333 1.00 26.22 ? 49 PHE A N 1 ATOM 371 C CA . PHE A 1 49 ? 56.307 73.657 20.457 1.00 25.37 ? 49 PHE A CA 1 ATOM 372 C C . PHE A 1 49 ? 55.890 73.391 21.898 1.00 24.71 ? 49 PHE A C 1 ATOM 373 O O . PHE A 1 49 ? 56.687 72.944 22.727 1.00 25.00 ? 49 PHE A O 1 ATOM 374 C CB . PHE A 1 49 ? 56.145 72.439 19.576 1.00 25.65 ? 49 PHE A CB 1 ATOM 375 C CG . PHE A 1 49 ? 56.499 72.714 18.149 1.00 25.77 ? 49 PHE A CG 1 ATOM 376 C CD1 . PHE A 1 49 ? 55.597 73.380 17.309 1.00 25.95 ? 49 PHE A CD1 1 ATOM 377 C CD2 . PHE A 1 49 ? 57.754 72.377 17.652 1.00 25.34 ? 49 PHE A CD2 1 ATOM 378 C CE1 . PHE A 1 49 ? 55.935 73.663 15.988 1.00 25.40 ? 49 PHE A CE1 1 ATOM 379 C CE2 . PHE A 1 49 ? 58.091 72.653 16.334 1.00 24.77 ? 49 PHE A CE2 1 ATOM 380 C CZ . PHE A 1 49 ? 57.181 73.301 15.504 1.00 25.12 ? 49 PHE A CZ 1 ATOM 381 N N . LEU A 1 50 ? 54.639 73.736 22.176 1.00 24.02 ? 50 LEU A N 1 ATOM 382 C CA . LEU A 1 50 ? 53.995 73.533 23.462 1.00 24.19 ? 50 LEU A CA 1 ATOM 383 C C . LEU A 1 50 ? 52.848 72.575 23.189 1.00 24.09 ? 50 LEU A C 1 ATOM 384 O O . LEU A 1 50 ? 52.044 72.823 22.287 1.00 22.53 ? 50 LEU A O 1 ATOM 385 C CB . LEU A 1 50 ? 53.470 74.864 23.988 1.00 24.09 ? 50 LEU A CB 1 ATOM 386 C CG . LEU A 1 50 ? 52.574 74.878 25.216 1.00 24.60 ? 50 LEU A CG 1 ATOM 387 C CD1 . LEU A 1 50 ? 53.227 74.166 26.386 1.00 25.04 ? 50 LEU A CD1 1 ATOM 388 C CD2 . LEU A 1 50 ? 52.242 76.321 25.578 1.00 24.89 ? 50 LEU A CD2 1 ATOM 389 N N . LEU A 1 51 ? 52.792 71.487 23.956 1.00 25.23 ? 51 LEU A N 1 ATOM 390 C CA . LEU A 1 51 ? 51.794 70.437 23.768 1.00 25.58 ? 51 LEU A CA 1 ATOM 391 C C . LEU A 1 51 ? 50.663 70.622 24.754 1.00 25.59 ? 51 LEU A C 1 ATOM 392 O O . LEU A 1 51 ? 50.880 70.827 25.949 1.00 25.97 ? 51 LEU A O 1 ATOM 393 C CB . LEU A 1 51 ? 52.416 69.046 23.933 1.00 26.59 ? 51 LEU A CB 1 ATOM 394 C CG . LEU A 1 51 ? 53.648 68.775 23.061 1.00 28.28 ? 51 LEU A CG 1 ATOM 395 C CD1 . LEU A 1 51 ? 54.115 67.333 23.208 1.00 29.66 ? 51 LEU A CD1 1 ATOM 396 C CD2 . LEU A 1 51 ? 53.417 69.089 21.588 1.00 28.36 ? 51 LEU A CD2 1 ATOM 397 N N . VAL A 1 52 ? 49.449 70.547 24.231 1.00 26.09 ? 52 VAL A N 1 ATOM 398 C CA . VAL A 1 52 ? 48.247 70.711 25.008 1.00 25.64 ? 52 VAL A CA 1 ATOM 399 C C . VAL A 1 52 ? 47.324 69.526 24.683 1.00 25.13 ? 52 VAL A C 1 ATOM 400 O O . VAL A 1 52 ? 47.131 69.190 23.512 1.00 24.20 ? 52 VAL A O 1 ATOM 401 C CB . VAL A 1 52 ? 47.610 72.079 24.681 1.00 26.73 ? 52 VAL A CB 1 ATOM 402 C CG1 . VAL A 1 52 ? 46.216 72.205 25.282 1.00 27.78 ? 52 VAL A CG1 1 ATOM 403 C CG2 . VAL A 1 52 ? 48.515 73.204 25.182 1.00 27.00 ? 52 VAL A CG2 1 ATOM 404 N N . ASP A 1 53 ? 46.771 68.897 25.719 1.00 24.65 ? 53 ASP A N 1 ATOM 405 C CA . ASP A 1 53 ? 45.864 67.761 25.553 1.00 26.06 ? 53 ASP A CA 1 ATOM 406 C C . ASP A 1 53 ? 44.409 68.172 25.749 1.00 24.95 ? 53 ASP A C 1 ATOM 407 O O . ASP A 1 53 ? 44.092 68.863 26.707 1.00 23.02 ? 53 ASP A O 1 ATOM 408 C CB . ASP A 1 53 ? 46.204 66.660 26.556 1.00 29.15 ? 53 ASP A CB 1 ATOM 409 C CG . ASP A 1 53 ? 47.560 66.010 26.297 1.00 32.03 ? 53 ASP A CG 1 ATOM 410 O OD1 . ASP A 1 53 ? 48.253 66.317 25.298 1.00 35.43 ? 53 ASP A OD1 1 ATOM 411 O OD2 . ASP A 1 53 ? 47.944 65.172 27.127 1.00 36.39 ? 53 ASP A OD2 1 ATOM 412 N N . LEU A 1 54 ? 43.537 67.765 24.825 1.00 23.96 ? 54 LEU A N 1 ATOM 413 C CA . LEU A 1 54 ? 42.093 67.930 24.978 1.00 24.63 ? 54 LEU A CA 1 ATOM 414 C C . LEU A 1 54 ? 41.430 66.568 24.870 1.00 25.65 ? 54 LEU A C 1 ATOM 415 O O . LEU A 1 54 ? 41.720 65.811 23.951 1.00 26.39 ? 54 LEU A O 1 ATOM 416 C CB . LEU A 1 54 ? 41.513 68.838 23.906 1.00 24.16 ? 54 LEU A CB 1 ATOM 417 C CG . LEU A 1 54 ? 42.094 70.242 23.756 1.00 23.42 ? 54 LEU A CG 1 ATOM 418 C CD1 . LEU A 1 54 ? 41.389 70.919 22.597 1.00 23.21 ? 54 LEU A CD1 1 ATOM 419 C CD2 . LEU A 1 54 ? 41.956 71.068 25.024 1.00 23.26 ? 54 LEU A CD2 1 ATOM 420 N N . THR A 1 55 ? 40.522 66.284 25.800 1.00 26.51 ? 55 THR A N 1 ATOM 421 C CA . THR A 1 55 ? 39.888 64.981 25.915 1.00 26.83 ? 55 THR A CA 1 ATOM 422 C C . THR A 1 55 ? 38.385 65.131 25.773 1.00 26.06 ? 55 THR A C 1 ATOM 423 O O . THR A 1 55 ? 37.768 65.933 26.460 1.00 25.28 ? 55 THR A O 1 ATOM 424 C CB . THR A 1 55 ? 40.206 64.324 27.274 1.00 27.13 ? 55 THR A CB 1 ATOM 425 O OG1 . THR A 1 55 ? 41.620 64.312 27.473 1.00 27.64 ? 55 THR A OG1 1 ATOM 426 C CG2 . THR A 1 55 ? 39.707 62.892 27.310 1.00 27.80 ? 55 THR A CG2 1 ATOM 427 N N . ASN A 1 56 ? 37.799 64.338 24.893 1.00 26.29 ? 56 ASN A N 1 ATOM 428 C CA . ASN A 1 56 ? 36.378 64.461 24.587 1.00 28.31 ? 56 ASN A CA 1 ATOM 429 C C . ASN A 1 56 ? 35.517 63.649 25.566 1.00 29.71 ? 56 ASN A C 1 ATOM 430 O O . ASN A 1 56 ? 36.037 63.068 26.536 1.00 29.43 ? 56 ASN A O 1 ATOM 431 C CB . ASN A 1 56 ? 36.118 64.100 23.106 1.00 28.84 ? 56 ASN A CB 1 ATOM 432 C CG . ASN A 1 56 ? 36.451 62.654 22.768 1.00 29.10 ? 56 ASN A CG 1 ATOM 433 O OD1 . ASN A 1 56 ? 36.322 61.764 23.599 1.00 27.94 ? 56 ASN A OD1 1 ATOM 434 N ND2 . ASN A 1 56 ? 36.879 62.416 21.532 1.00 31.00 ? 56 ASN A ND2 1 ATOM 435 N N . GLY A 1 57 ? 34.212 63.604 25.299 1.00 31.05 ? 57 GLY A N 1 ATOM 436 C CA . GLY A 1 57 ? 33.256 62.883 26.135 1.00 33.09 ? 57 GLY A CA 1 ATOM 437 C C . GLY A 1 57 ? 33.317 61.369 26.017 1.00 33.27 ? 57 GLY A C 1 ATOM 438 O O . GLY A 1 57 ? 32.622 60.677 26.755 1.00 34.84 ? 57 GLY A O 1 ATOM 439 N N . ASP A 1 58 ? 34.118 60.861 25.074 1.00 32.78 ? 58 ASP A N 1 ATOM 440 C CA . ASP A 1 58 ? 34.457 59.429 24.987 1.00 33.47 ? 58 ASP A CA 1 ATOM 441 C C . ASP A 1 58 ? 35.757 59.087 25.728 1.00 35.01 ? 58 ASP A C 1 ATOM 442 O O . ASP A 1 58 ? 36.225 57.952 25.643 1.00 38.90 ? 58 ASP A O 1 ATOM 443 C CB . ASP A 1 58 ? 34.590 58.991 23.513 1.00 31.42 ? 58 ASP A CB 1 ATOM 444 C CG . ASP A 1 58 ? 33.383 59.382 22.666 1.00 30.91 ? 58 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 58 ? 32.237 59.331 23.164 1.00 26.85 ? 58 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 58 ? 33.589 59.758 21.485 1.00 34.37 ? 58 ASP A OD2 1 ATOM 447 N N . ASN A 1 59 ? 36.334 60.056 26.447 1.00 35.73 ? 59 ASN A N 1 ATOM 448 C CA . ASN A 1 59 ? 37.649 59.925 27.081 1.00 36.10 ? 59 ASN A CA 1 ATOM 449 C C . ASN A 1 59 ? 38.776 59.600 26.100 1.00 35.27 ? 59 ASN A C 1 ATOM 450 O O . ASN A 1 59 ? 39.739 58.945 26.475 1.00 36.96 ? 59 ASN A O 1 ATOM 451 C CB . ASN A 1 59 ? 37.623 58.904 28.240 1.00 37.19 ? 59 ASN A CB 1 ATOM 452 C CG . ASN A 1 59 ? 38.736 59.150 29.263 1.00 39.27 ? 59 ASN A CG 1 ATOM 453 O OD1 . ASN A 1 59 ? 38.812 60.222 29.853 1.00 42.33 ? 59 ASN A OD1 1 ATOM 454 N ND2 . ASN A 1 59 ? 39.607 58.164 29.468 1.00 41.22 ? 59 ASN A ND2 1 ATOM 455 N N . GLU A 1 60 ? 38.647 60.050 24.850 1.00 35.12 ? 60 GLU A N 1 ATOM 456 C CA . GLU A 1 60 ? 39.730 59.988 23.862 1.00 36.14 ? 60 GLU A CA 1 ATOM 457 C C . GLU A 1 60 ? 40.360 61.373 23.782 1.00 34.84 ? 60 GLU A C 1 ATOM 458 O O . GLU A 1 60 ? 39.646 62.391 23.798 1.00 32.54 ? 60 GLU A O 1 ATOM 459 C CB . GLU A 1 60 ? 39.218 59.580 22.477 1.00 38.72 ? 60 GLU A CB 1 ATOM 460 C CG . GLU A 1 60 ? 38.536 58.217 22.404 1.00 43.05 ? 60 GLU A CG 1 ATOM 461 C CD . GLU A 1 60 ? 39.453 57.058 22.792 1.00 46.59 ? 60 GLU A CD 1 ATOM 462 O OE1 . GLU A 1 60 ? 39.867 56.288 21.901 1.00 50.51 ? 60 GLU A OE1 1 ATOM 463 O OE2 . GLU A 1 60 ? 39.763 56.909 23.991 1.00 50.66 ? 60 GLU A OE2 1 ATOM 464 N N . THR A 1 61 ? 41.690 61.392 23.679 1.00 32.04 ? 61 THR A N 1 ATOM 465 C CA . THR A 1 61 ? 42.477 62.605 23.795 1.00 30.90 ? 61 THR A CA 1 ATOM 466 C C . THR A 1 61 ? 43.222 62.894 22.496 1.00 30.03 ? 61 THR A C 1 ATOM 467 O O . THR A 1 61 ? 43.718 61.965 21.851 1.00 30.28 ? 61 THR A O 1 ATOM 468 C CB . THR A 1 61 ? 43.486 62.460 24.944 1.00 30.50 ? 61 THR A CB 1 ATOM 469 O OG1 . THR A 1 61 ? 42.766 62.281 26.164 1.00 30.25 ? 61 THR A OG1 1 ATOM 470 C CG2 . THR A 1 61 ? 44.386 63.702 25.068 1.00 30.63 ? 61 THR A CG2 1 ATOM 471 N N . ILE A 1 62 ? 43.263 64.178 22.114 1.00 27.40 ? 62 ILE A N 1 ATOM 472 C CA . ILE A 1 62 ? 44.164 64.662 21.068 1.00 25.51 ? 62 ILE A CA 1 ATOM 473 C C . ILE A 1 62 ? 45.197 65.532 21.738 1.00 25.45 ? 62 ILE A C 1 ATOM 474 O O . ILE A 1 62 ? 44.894 66.178 22.748 1.00 25.51 ? 62 ILE A O 1 ATOM 475 C CB . ILE A 1 62 ? 43.451 65.442 19.923 1.00 25.64 ? 62 ILE A CB 1 ATOM 476 C CG1 . ILE A 1 62 ? 42.733 66.711 20.415 1.00 25.24 ? 62 ILE A CG1 1 ATOM 477 C CG2 . ILE A 1 62 ? 42.480 64.540 19.171 1.00 25.13 ? 62 ILE A CG2 1 ATOM 478 C CD1 . ILE A 1 62 ? 42.025 67.468 19.318 1.00 24.46 ? 62 ILE A CD1 1 ATOM 479 N N . THR A 1 63 ? 46.416 65.525 21.210 1.00 24.19 ? 63 THR A N 1 ATOM 480 C CA . THR A 1 63 ? 47.453 66.435 21.667 1.00 24.59 ? 63 THR A CA 1 ATOM 481 C C . THR A 1 63 ? 47.751 67.427 20.554 1.00 23.61 ? 63 THR A C 1 ATOM 482 O O . THR A 1 63 ? 48.145 67.025 19.471 1.00 22.76 ? 63 THR A O 1 ATOM 483 C CB . THR A 1 63 ? 48.737 65.694 22.080 1.00 25.31 ? 63 THR A CB 1 ATOM 484 O OG1 . THR A 1 63 ? 48.448 64.824 23.178 1.00 27.19 ? 63 THR A OG1 1 ATOM 485 C CG2 . THR A 1 63 ? 49.830 66.684 22.508 1.00 25.02 ? 63 THR A CG2 1 ATOM 486 N N . LEU A 1 64 ? 47.555 68.716 20.837 1.00 23.08 ? 64 LEU A N 1 ATOM 487 C CA . LEU A 1 64 ? 47.793 69.771 19.864 1.00 23.18 ? 64 LEU A CA 1 ATOM 488 C C . LEU A 1 64 ? 49.154 70.412 20.128 1.00 22.58 ? 64 LEU A C 1 ATOM 489 O O . LEU A 1 64 ? 49.476 70.739 21.280 1.00 21.94 ? 64 LEU A O 1 ATOM 490 C CB . LEU A 1 64 ? 46.702 70.829 19.968 1.00 24.62 ? 64 LEU A CB 1 ATOM 491 C CG . LEU A 1 64 ? 45.286 70.411 19.547 1.00 25.71 ? 64 LEU A CG 1 ATOM 492 C CD1 . LEU A 1 64 ? 44.233 71.056 20.440 1.00 26.77 ? 64 LEU A CD1 1 ATOM 493 C CD2 . LEU A 1 64 ? 45.037 70.787 18.099 1.00 25.59 ? 64 LEU A CD2 1 ATOM 494 N N . ALA A 1 65 ? 49.943 70.589 19.066 1.00 21.55 ? 65 ALA A N 1 ATOM 495 C CA . ALA A 1 65 ? 51.241 71.247 19.167 1.00 21.55 ? 65 ALA A CA 1 ATOM 496 C C . ALA A 1 65 ? 51.101 72.710 18.741 1.00 21.24 ? 65 ALA A C 1 ATOM 497 O O . ALA A 1 65 ? 50.810 73.003 17.580 1.00 20.98 ? 65 ALA A O 1 ATOM 498 C CB . ALA A 1 65 ? 52.276 70.528 18.309 1.00 21.30 ? 65 ALA A CB 1 ATOM 499 N N . ILE A 1 66 ? 51.300 73.606 19.703 1.00 21.40 ? 66 ILE A N 1 ATOM 500 C CA . ILE A 1 66 ? 51.212 75.051 19.503 1.00 22.19 ? 66 ILE A CA 1 ATOM 501 C C . ILE A 1 66 ? 52.611 75.638 19.371 1.00 22.09 ? 66 ILE A C 1 ATOM 502 O O . ILE A 1 66 ? 53.453 75.448 20.239 1.00 23.69 ? 66 ILE A O 1 ATOM 503 C CB . ILE A 1 66 ? 50.525 75.760 20.696 1.00 21.69 ? 66 ILE A CB 1 ATOM 504 C CG1 . ILE A 1 66 ? 49.122 75.208 20.911 1.00 21.84 ? 66 ILE A CG1 1 ATOM 505 C CG2 . ILE A 1 66 ? 50.456 77.272 20.464 1.00 21.84 ? 66 ILE A CG2 1 ATOM 506 C CD1 . ILE A 1 66 ? 48.544 75.532 22.269 1.00 22.71 ? 66 ILE A CD1 1 ATOM 507 N N . ASN A 1 67 ? 52.828 76.375 18.295 1.00 21.32 ? 67 ASN A N 1 ATOM 508 C CA . ASN A 1 67 ? 54.071 77.073 18.053 1.00 21.40 ? 67 ASN A CA 1 ATOM 509 C C . ASN A 1 67 ? 54.109 78.270 18.981 1.00 22.40 ? 67 ASN A C 1 ATOM 510 O O . ASN A 1 67 ? 53.215 79.126 18.922 1.00 22.14 ? 67 ASN A O 1 ATOM 511 C CB . ASN A 1 67 ? 54.089 77.523 16.594 1.00 21.56 ? 67 ASN A CB 1 ATOM 512 C CG . ASN A 1 67 ? 55.394 78.163 16.166 1.00 21.67 ? 67 ASN A CG 1 ATOM 513 O OD1 . ASN A 1 67 ? 56.092 78.821 16.941 1.00 21.97 ? 67 ASN A OD1 1 ATOM 514 N ND2 . ASN A 1 67 ? 55.710 77.997 14.889 1.00 22.29 ? 67 ASN A ND2 1 ATOM 515 N N . VAL A 1 68 ? 55.151 78.338 19.810 1.00 22.33 ? 68 VAL A N 1 ATOM 516 C CA . VAL A 1 68 ? 55.249 79.349 20.860 1.00 23.12 ? 68 VAL A CA 1 ATOM 517 C C . VAL A 1 68 ? 55.604 80.738 20.341 1.00 23.07 ? 68 VAL A C 1 ATOM 518 O O . VAL A 1 68 ? 55.517 81.689 21.095 1.00 23.04 ? 68 VAL A O 1 ATOM 519 C CB . VAL A 1 68 ? 56.265 78.980 21.972 1.00 23.53 ? 68 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 68 ? 55.912 77.639 22.608 1.00 24.34 ? 68 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 68 ? 57.708 79.012 21.465 1.00 23.56 ? 68 VAL A CG2 1 ATOM 522 N N . GLU A 1 69 ? 56.016 80.839 19.078 1.00 24.95 ? 69 GLU A N 1 ATOM 523 C CA . GLU A 1 69 ? 56.327 82.120 18.445 1.00 25.69 ? 69 GLU A CA 1 ATOM 524 C C . GLU A 1 69 ? 55.085 82.859 17.960 1.00 25.75 ? 69 GLU A C 1 ATOM 525 O O . GLU A 1 69 ? 55.054 84.091 17.991 1.00 25.27 ? 69 GLU A O 1 ATOM 526 C CB . GLU A 1 69 ? 57.293 81.924 17.282 1.00 26.60 ? 69 GLU A CB 1 ATOM 527 C CG . GLU A 1 69 ? 58.618 81.300 17.696 1.00 28.52 ? 69 GLU A CG 1 ATOM 528 C CD . GLU A 1 69 ? 59.630 81.208 16.563 1.00 31.33 ? 69 GLU A CD 1 ATOM 529 O OE1 . GLU A 1 69 ? 59.257 81.402 15.383 1.00 31.99 ? 69 GLU A OE1 1 ATOM 530 O OE2 . GLU A 1 69 ? 60.814 80.925 16.854 1.00 34.76 ? 69 GLU A OE2 1 ATOM 531 N N . ASP A 1 70 ? 54.076 82.126 17.496 1.00 25.70 ? 70 ASP A N 1 ATOM 532 C CA . ASP A 1 70 ? 52.859 82.763 16.994 1.00 26.55 ? 70 ASP A CA 1 ATOM 533 C C . ASP A 1 70 ? 51.533 82.232 17.539 1.00 25.53 ? 70 ASP A C 1 ATOM 534 O O . ASP A 1 70 ? 50.487 82.658 17.083 1.00 25.17 ? 70 ASP A O 1 ATOM 535 C CB . ASP A 1 70 ? 52.859 82.782 15.454 1.00 27.46 ? 70 ASP A CB 1 ATOM 536 C CG . ASP A 1 70 ? 52.755 81.409 14.835 1.00 28.45 ? 70 ASP A CG 1 ATOM 537 O OD1 . ASP A 1 70 ? 52.514 80.424 15.553 1.00 30.12 ? 70 ASP A OD1 1 ATOM 538 O OD2 . ASP A 1 70 ? 52.901 81.323 13.603 1.00 28.86 ? 70 ASP A OD2 1 ATOM 539 N N . ALA A 1 71 ? 51.569 81.334 18.522 1.00 24.73 ? 71 ALA A N 1 ATOM 540 C CA . ALA A 1 71 ? 50.352 80.794 19.120 1.00 24.56 ? 71 ALA A CA 1 ATOM 541 C C . ALA A 1 71 ? 49.363 80.262 18.086 1.00 24.07 ? 71 ALA A C 1 ATOM 542 O O . ALA A 1 71 ? 48.170 80.545 18.161 1.00 25.73 ? 71 ALA A O 1 ATOM 543 C CB . ALA A 1 71 ? 49.687 81.843 20.002 1.00 25.29 ? 71 ALA A CB 1 ATOM 544 N N . GLY A 1 72 ? 49.880 79.510 17.119 1.00 23.03 ? 72 GLY A N 1 ATOM 545 C CA . GLY A 1 72 ? 49.072 78.817 16.127 1.00 22.34 ? 72 GLY A CA 1 ATOM 546 C C . GLY A 1 72 ? 49.366 77.333 16.190 1.00 22.72 ? 72 GLY A C 1 ATOM 547 O O . GLY A 1 72 ? 50.480 76.942 16.567 1.00 21.76 ? 72 GLY A O 1 ATOM 548 N N . PHE A 1 73 ? 48.378 76.503 15.832 1.00 22.40 ? 73 PHE A N 1 ATOM 549 C CA . PHE A 1 73 ? 48.592 75.059 15.769 1.00 23.27 ? 73 PHE A CA 1 ATOM 550 C C . PHE A 1 73 ? 49.481 74.719 14.593 1.00 24.52 ? 73 PHE A C 1 ATOM 551 O O . PHE A 1 73 ? 49.222 75.160 13.468 1.00 24.76 ? 73 PHE A O 1 ATOM 552 C CB . PHE A 1 73 ? 47.281 74.287 15.639 1.00 23.47 ? 73 PHE A CB 1 ATOM 553 C CG . PHE A 1 73 ? 46.394 74.392 16.841 1.00 23.10 ? 73 PHE A CG 1 ATOM 554 C CD1 . PHE A 1 73 ? 46.900 74.212 18.122 1.00 23.16 ? 73 PHE A CD1 1 ATOM 555 C CD2 . PHE A 1 73 ? 45.042 74.656 16.692 1.00 23.31 ? 73 PHE A CD2 1 ATOM 556 C CE1 . PHE A 1 73 ? 46.073 74.303 19.229 1.00 23.72 ? 73 PHE A CE1 1 ATOM 557 C CE2 . PHE A 1 73 ? 44.210 74.749 17.792 1.00 23.67 ? 73 PHE A CE2 1 ATOM 558 C CZ . PHE A 1 73 ? 44.725 74.565 19.067 1.00 23.60 ? 73 PHE A CZ 1 ATOM 559 N N . ALA A 1 74 ? 50.547 73.971 14.874 1.00 24.86 ? 74 ALA A N 1 ATOM 560 C CA . ALA A 1 74 ? 51.433 73.435 13.854 1.00 24.85 ? 74 ALA A CA 1 ATOM 561 C C . ALA A 1 74 ? 51.003 72.028 13.444 1.00 24.67 ? 74 ALA A C 1 ATOM 562 O O . ALA A 1 74 ? 51.079 71.681 12.274 1.00 26.15 ? 74 ALA A O 1 ATOM 563 C CB . ALA A 1 74 ? 52.863 73.423 14.368 1.00 25.70 ? 74 ALA A CB 1 ATOM 564 N N . ALA A 1 75 ? 50.552 71.230 14.410 1.00 24.09 ? 75 ALA A N 1 ATOM 565 C CA . ALA A 1 75 ? 50.187 69.840 14.184 1.00 23.58 ? 75 ALA A CA 1 ATOM 566 C C . ALA A 1 75 ? 49.353 69.282 15.338 1.00 24.27 ? 75 ALA A C 1 ATOM 567 O O . ALA A 1 75 ? 49.217 69.912 16.396 1.00 24.26 ? 75 ALA A O 1 ATOM 568 C CB . ALA A 1 75 ? 51.452 69.015 14.036 1.00 24.17 ? 75 ALA A CB 1 ATOM 569 N N . TYR A 1 76 ? 48.811 68.087 15.158 1.00 24.07 ? 76 TYR A N 1 ATOM 570 C CA . TYR A 1 76 ? 48.214 67.383 16.294 1.00 25.15 ? 76 TYR A CA 1 ATOM 571 C C . TYR A 1 76 ? 48.358 65.867 16.221 1.00 25.97 ? 76 TYR A C 1 ATOM 572 O O . TYR A 1 76 ? 48.536 65.298 15.143 1.00 26.22 ? 76 TYR A O 1 ATOM 573 C CB . TYR A 1 76 ? 46.754 67.804 16.477 1.00 25.16 ? 76 TYR A CB 1 ATOM 574 C CG . TYR A 1 76 ? 45.734 67.081 15.630 1.00 24.24 ? 76 TYR A CG 1 ATOM 575 C CD1 . TYR A 1 76 ? 45.466 67.484 14.327 1.00 23.37 ? 76 TYR A CD1 1 ATOM 576 C CD2 . TYR A 1 76 ? 45.031 65.998 16.140 1.00 23.47 ? 76 TYR A CD2 1 ATOM 577 C CE1 . TYR A 1 76 ? 44.529 66.823 13.550 1.00 22.77 ? 76 TYR A CE1 1 ATOM 578 C CE2 . TYR A 1 76 ? 44.102 65.331 15.373 1.00 22.97 ? 76 TYR A CE2 1 ATOM 579 C CZ . TYR A 1 76 ? 43.853 65.747 14.080 1.00 22.62 ? 76 TYR A CZ 1 ATOM 580 O OH . TYR A 1 76 ? 42.901 65.096 13.356 1.00 21.13 ? 76 TYR A OH 1 ATOM 581 N N . ARG A 1 77 ? 48.297 65.233 17.384 1.00 27.14 ? 77 ARG A N 1 ATOM 582 C CA . ARG A 1 77 ? 48.381 63.776 17.495 1.00 29.53 ? 77 ARG A CA 1 ATOM 583 C C . ARG A 1 77 ? 47.074 63.239 18.055 1.00 29.88 ? 77 ARG A C 1 ATOM 584 O O . ARG A 1 77 ? 46.440 63.870 18.913 1.00 28.85 ? 77 ARG A O 1 ATOM 585 C CB . ARG A 1 77 ? 49.553 63.347 18.393 1.00 31.13 ? 77 ARG A CB 1 ATOM 586 C CG . ARG A 1 77 ? 49.658 61.834 18.643 1.00 32.98 ? 77 ARG A CG 1 ATOM 587 C CD . ARG A 1 77 ? 50.765 61.490 19.628 1.00 35.45 ? 77 ARG A CD 1 ATOM 588 N NE . ARG A 1 77 ? 50.562 62.185 20.904 1.00 39.33 ? 77 ARG A NE 1 ATOM 589 C CZ . ARG A 1 77 ? 51.527 62.643 21.716 1.00 43.48 ? 77 ARG A CZ 1 ATOM 590 N NH1 . ARG A 1 77 ? 52.832 62.480 21.443 1.00 44.76 ? 77 ARG A NH1 1 ATOM 591 N NH2 . ARG A 1 77 ? 51.183 63.282 22.833 1.00 44.06 ? 77 ARG A NH2 1 ATOM 592 N N . ALA A 1 78 ? 46.687 62.077 17.541 1.00 29.61 ? 78 ALA A N 1 ATOM 593 C CA . ALA A 1 78 ? 45.575 61.294 18.051 1.00 30.63 ? 78 ALA A CA 1 ATOM 594 C C . ALA A 1 78 ? 46.047 59.851 17.996 1.00 32.75 ? 78 ALA A C 1 ATOM 595 O O . ALA A 1 78 ? 46.279 59.330 16.904 1.00 31.43 ? 78 ALA A O 1 ATOM 596 C CB . ALA A 1 78 ? 44.350 61.483 17.179 1.00 30.43 ? 78 ALA A CB 1 ATOM 597 N N . ALA A 1 79 ? 46.224 59.233 19.166 1.00 35.07 ? 79 ALA A N 1 ATOM 598 C CA . ALA A 1 79 ? 46.698 57.846 19.284 1.00 36.46 ? 79 ALA A CA 1 ATOM 599 C C . ALA A 1 79 ? 48.079 57.677 18.611 1.00 37.11 ? 79 ALA A C 1 ATOM 600 O O . ALA A 1 79 ? 49.041 58.318 19.039 1.00 38.04 ? 79 ALA A O 1 ATOM 601 C CB . ALA A 1 79 ? 45.639 56.868 18.750 1.00 36.54 ? 79 ALA A CB 1 ATOM 602 N N . ASP A 1 80 ? 48.184 56.870 17.554 1.00 38.39 ? 80 ASP A N 1 ATOM 603 C CA . ASP A 1 80 ? 49.476 56.640 16.874 1.00 39.74 ? 80 ASP A CA 1 ATOM 604 C C . ASP A 1 80 ? 49.554 57.383 15.522 1.00 37.27 ? 80 ASP A C 1 ATOM 605 O O . ASP A 1 80 ? 50.485 57.169 14.740 1.00 36.28 ? 80 ASP A O 1 ATOM 606 C CB . ASP A 1 80 ? 49.742 55.126 16.710 1.00 42.25 ? 80 ASP A CB 1 ATOM 607 C CG . ASP A 1 80 ? 48.584 54.378 16.031 1.00 44.60 ? 80 ASP A CG 1 ATOM 608 O OD1 . ASP A 1 80 ? 47.766 55.018 15.339 1.00 46.07 ? 80 ASP A OD1 1 ATOM 609 O OD2 . ASP A 1 80 ? 48.486 53.140 16.198 1.00 47.86 ? 80 ASP A OD2 1 ATOM 610 N N . ARG A 1 81 ? 48.569 58.248 15.266 1.00 34.32 ? 81 ARG A N 1 ATOM 611 C CA . ARG A 1 81 ? 48.521 59.095 14.076 1.00 32.89 ? 81 ARG A CA 1 ATOM 612 C C . ARG A 1 81 ? 48.794 60.557 14.458 1.00 31.72 ? 81 ARG A C 1 ATOM 613 O O . ARG A 1 81 ? 48.489 60.993 15.585 1.00 29.26 ? 81 ARG A O 1 ATOM 614 C CB . ARG A 1 81 ? 47.145 58.976 13.408 1.00 33.15 ? 81 ARG A CB 1 ATOM 615 C CG . ARG A 1 81 ? 46.807 57.559 12.941 1.00 32.88 ? 81 ARG A CG 1 ATOM 616 C CD . ARG A 1 81 ? 45.319 57.353 12.705 1.00 32.78 ? 81 ARG A CD 1 ATOM 617 N NE . ARG A 1 81 ? 44.556 57.373 13.964 1.00 33.10 ? 81 ARG A NE 1 ATOM 618 C CZ . ARG A 1 81 ? 43.708 58.332 14.368 1.00 32.29 ? 81 ARG A CZ 1 ATOM 619 N NH1 . ARG A 1 81 ? 43.453 59.409 13.633 1.00 32.50 ? 81 ARG A NH1 1 ATOM 620 N NH2 . ARG A 1 81 ? 43.094 58.210 15.541 1.00 31.24 ? 81 ARG A NH2 1 ATOM 621 N N . SER A 1 82 ? 49.395 61.295 13.527 1.00 30.23 ? 82 SER A N 1 ATOM 622 C CA . SER A 1 82 ? 49.588 62.732 13.685 1.00 29.82 ? 82 SER A CA 1 ATOM 623 C C . SER A 1 82 ? 49.388 63.433 12.360 1.00 29.62 ? 82 SER A C 1 ATOM 624 O O . SER A 1 82 ? 49.515 62.820 11.294 1.00 28.97 ? 82 SER A O 1 ATOM 625 C CB . SER A 1 82 ? 50.961 63.053 14.270 1.00 29.60 ? 82 SER A CB 1 ATOM 626 O OG . SER A 1 82 ? 51.993 62.683 13.386 1.00 29.01 ? 82 SER A OG 1 ATOM 627 N N . TYR A 1 83 ? 49.054 64.719 12.445 1.00 28.28 ? 83 TYR A N 1 ATOM 628 C CA . TYR A 1 83 ? 48.621 65.493 11.294 1.00 26.52 ? 83 TYR A CA 1 ATOM 629 C C . TYR A 1 83 ? 49.216 66.880 11.376 1.00 26.46 ? 83 TYR A C 1 ATOM 630 O O . TYR A 1 83 ? 49.030 67.566 12.381 1.00 25.44 ? 83 TYR A O 1 ATOM 631 C CB . TYR A 1 83 ? 47.108 65.599 11.269 1.00 26.47 ? 83 TYR A CB 1 ATOM 632 C CG . TYR A 1 83 ? 46.427 64.262 11.301 1.00 27.99 ? 83 TYR A CG 1 ATOM 633 C CD1 . TYR A 1 83 ? 46.181 63.549 10.124 1.00 28.30 ? 83 TYR A CD1 1 ATOM 634 C CD2 . TYR A 1 83 ? 46.054 63.689 12.506 1.00 28.16 ? 83 TYR A CD2 1 ATOM 635 C CE1 . TYR A 1 83 ? 45.553 62.315 10.155 1.00 28.74 ? 83 TYR A CE1 1 ATOM 636 C CE2 . TYR A 1 83 ? 45.432 62.454 12.550 1.00 29.18 ? 83 TYR A CE2 1 ATOM 637 C CZ . TYR A 1 83 ? 45.183 61.776 11.376 1.00 29.21 ? 83 TYR A CZ 1 ATOM 638 O OH . TYR A 1 83 ? 44.565 60.564 11.444 1.00 29.43 ? 83 TYR A OH 1 ATOM 639 N N . PHE A 1 84 ? 49.916 67.273 10.312 1.00 25.93 ? 84 PHE A N 1 ATOM 640 C CA . PHE A 1 84 ? 50.655 68.525 10.232 1.00 26.62 ? 84 PHE A CA 1 ATOM 641 C C . PHE A 1 84 ? 49.970 69.447 9.231 1.00 26.81 ? 84 PHE A C 1 ATOM 642 O O . PHE A 1 84 ? 49.498 69.001 8.191 1.00 27.53 ? 84 PHE A O 1 ATOM 643 C CB . PHE A 1 84 ? 52.109 68.257 9.797 1.00 26.08 ? 84 PHE A CB 1 ATOM 644 C CG . PHE A 1 84 ? 52.949 67.635 10.874 1.00 25.36 ? 84 PHE A CG 1 ATOM 645 C CD1 . PHE A 1 84 ? 52.739 66.309 11.265 1.00 25.60 ? 84 PHE A CD1 1 ATOM 646 C CD2 . PHE A 1 84 ? 53.927 68.381 11.531 1.00 24.84 ? 84 PHE A CD2 1 ATOM 647 C CE1 . PHE A 1 84 ? 53.495 65.739 12.278 1.00 25.10 ? 84 PHE A CE1 1 ATOM 648 C CE2 . PHE A 1 84 ? 54.680 67.821 12.547 1.00 24.47 ? 84 PHE A CE2 1 ATOM 649 C CZ . PHE A 1 84 ? 54.472 66.496 12.917 1.00 25.03 ? 84 PHE A CZ 1 ATOM 650 N N . PHE A 1 85 ? 49.906 70.732 9.557 1.00 26.23 ? 85 PHE A N 1 ATOM 651 C CA . PHE A 1 85 ? 49.452 71.727 8.600 1.00 26.01 ? 85 PHE A CA 1 ATOM 652 C C . PHE A 1 85 ? 50.488 71.869 7.505 1.00 27.43 ? 85 PHE A C 1 ATOM 653 O O . PHE A 1 85 ? 51.688 71.687 7.724 1.00 25.51 ? 85 PHE A O 1 ATOM 654 C CB . PHE A 1 85 ? 49.174 73.089 9.259 1.00 24.44 ? 85 PHE A CB 1 ATOM 655 C CG . PHE A 1 85 ? 47.912 73.104 10.061 1.00 23.44 ? 85 PHE A CG 1 ATOM 656 C CD1 . PHE A 1 85 ? 46.688 73.323 9.443 1.00 23.26 ? 85 PHE A CD1 1 ATOM 657 C CD2 . PHE A 1 85 ? 47.939 72.866 11.425 1.00 22.38 ? 85 PHE A CD2 1 ATOM 658 C CE1 . PHE A 1 85 ? 45.513 73.325 10.179 1.00 23.07 ? 85 PHE A CE1 1 ATOM 659 C CE2 . PHE A 1 85 ? 46.772 72.858 12.172 1.00 22.49 ? 85 PHE A CE2 1 ATOM 660 C CZ . PHE A 1 85 ? 45.557 73.093 11.551 1.00 22.85 ? 85 PHE A CZ 1 ATOM 661 N N . GLN A 1 86 ? 49.997 72.223 6.328 1.00 29.84 ? 86 GLN A N 1 ATOM 662 C CA . GLN A 1 86 ? 50.835 72.409 5.163 1.00 32.51 ? 86 GLN A CA 1 ATOM 663 C C . GLN A 1 86 ? 51.866 73.517 5.346 1.00 32.65 ? 86 GLN A C 1 ATOM 664 O O . GLN A 1 86 ? 52.889 73.499 4.681 1.00 35.88 ? 86 GLN A O 1 ATOM 665 C CB . GLN A 1 86 ? 49.956 72.710 3.964 1.00 35.76 ? 86 GLN A CB 1 ATOM 666 C CG . GLN A 1 86 ? 50.633 72.531 2.636 1.00 39.08 ? 86 GLN A CG 1 ATOM 667 C CD . GLN A 1 86 ? 49.615 72.534 1.531 1.00 42.13 ? 86 GLN A CD 1 ATOM 668 O OE1 . GLN A 1 86 ? 49.328 71.495 0.937 1.00 45.33 ? 86 GLN A OE1 1 ATOM 669 N NE2 . GLN A 1 86 ? 49.020 73.697 1.279 1.00 43.36 ? 86 GLN A NE2 1 ATOM 670 N N . ASN A 1 87 ? 51.598 74.475 6.231 1.00 31.01 ? 87 ASN A N 1 ATOM 671 C CA . ASN A 1 87 ? 52.572 75.515 6.572 1.00 30.55 ? 87 ASN A CA 1 ATOM 672 C C . ASN A 1 87 ? 53.263 75.334 7.932 1.00 29.37 ? 87 ASN A C 1 ATOM 673 O O . ASN A 1 87 ? 53.892 76.257 8.418 1.00 28.37 ? 87 ASN A O 1 ATOM 674 C CB . ASN A 1 87 ? 51.911 76.900 6.508 1.00 31.07 ? 87 ASN A CB 1 ATOM 675 C CG . ASN A 1 87 ? 50.819 77.071 7.546 1.00 32.05 ? 87 ASN A CG 1 ATOM 676 O OD1 . ASN A 1 87 ? 50.223 76.094 8.009 1.00 30.63 ? 87 ASN A OD1 1 ATOM 677 N ND2 . ASN A 1 87 ? 50.550 78.310 7.919 1.00 33.12 ? 87 ASN A ND2 1 ATOM 678 N N . ALA A 1 88 ? 53.178 74.155 8.543 1.00 29.98 ? 88 ALA A N 1 ATOM 679 C CA . ALA A 1 88 ? 53.989 73.868 9.723 1.00 30.38 ? 88 ALA A CA 1 ATOM 680 C C . ALA A 1 88 ? 55.477 74.075 9.367 1.00 30.90 ? 88 ALA A C 1 ATOM 681 O O . ALA A 1 88 ? 55.858 73.919 8.201 1.00 31.06 ? 88 ALA A O 1 ATOM 682 C CB . ALA A 1 88 ? 53.750 72.450 10.213 1.00 30.06 ? 88 ALA A CB 1 ATOM 683 N N . PRO A 1 89 ? 56.317 74.456 10.349 1.00 31.64 ? 89 PRO A N 1 ATOM 684 C CA . PRO A 1 89 ? 57.734 74.631 10.030 1.00 32.34 ? 89 PRO A CA 1 ATOM 685 C C . PRO A 1 89 ? 58.303 73.299 9.558 1.00 33.44 ? 89 PRO A C 1 ATOM 686 O O . PRO A 1 89 ? 58.023 72.283 10.198 1.00 34.20 ? 89 PRO A O 1 ATOM 687 C CB . PRO A 1 89 ? 58.356 75.058 11.360 1.00 31.71 ? 89 PRO A CB 1 ATOM 688 C CG . PRO A 1 89 ? 57.225 75.526 12.198 1.00 31.07 ? 89 PRO A CG 1 ATOM 689 C CD . PRO A 1 89 ? 56.041 74.726 11.767 1.00 31.15 ? 89 PRO A CD 1 ATOM 690 N N . PRO A 1 90 ? 59.066 73.288 8.438 1.00 35.14 ? 90 PRO A N 1 ATOM 691 C CA . PRO A 1 90 ? 59.444 72.006 7.778 1.00 35.38 ? 90 PRO A CA 1 ATOM 692 C C . PRO A 1 90 ? 60.201 70.979 8.635 1.00 34.91 ? 90 PRO A C 1 ATOM 693 O O . PRO A 1 90 ? 60.114 69.783 8.361 1.00 37.80 ? 90 PRO A O 1 ATOM 694 C CB . PRO A 1 90 ? 60.316 72.443 6.593 1.00 35.52 ? 90 PRO A CB 1 ATOM 695 C CG . PRO A 1 90 ? 60.009 73.881 6.367 1.00 36.44 ? 90 PRO A CG 1 ATOM 696 C CD . PRO A 1 90 ? 59.493 74.466 7.652 1.00 36.15 ? 90 PRO A CD 1 ATOM 697 N N . ILE A 1 91 ? 60.909 71.443 9.660 1.00 33.43 ? 91 ILE A N 1 ATOM 698 C CA . ILE A 1 91 ? 61.696 70.587 10.537 1.00 33.57 ? 91 ILE A CA 1 ATOM 699 C C . ILE A 1 91 ? 60.864 70.048 11.713 1.00 32.45 ? 91 ILE A C 1 ATOM 700 O O . ILE A 1 91 ? 61.338 69.205 12.472 1.00 31.62 ? 91 ILE A O 1 ATOM 701 C CB . ILE A 1 91 ? 62.944 71.358 11.045 1.00 35.78 ? 91 ILE A CB 1 ATOM 702 C CG1 . ILE A 1 91 ? 63.722 71.972 9.866 1.00 36.79 ? 91 ILE A CG1 1 ATOM 703 C CG2 . ILE A 1 91 ? 63.878 70.467 11.866 1.00 36.27 ? 91 ILE A CG2 1 ATOM 704 C CD1 . ILE A 1 91 ? 64.190 70.969 8.828 1.00 37.35 ? 91 ILE A CD1 1 ATOM 705 N N . ALA A 1 92 ? 59.616 70.507 11.846 1.00 31.15 ? 92 ALA A N 1 ATOM 706 C CA . ALA A 1 92 ? 58.754 70.133 12.972 1.00 29.81 ? 92 ALA A CA 1 ATOM 707 C C . ALA A 1 92 ? 58.486 68.647 13.063 1.00 28.55 ? 92 ALA A C 1 ATOM 708 O O . ALA A 1 92 ? 58.434 68.120 14.165 1.00 28.15 ? 92 ALA A O 1 ATOM 709 C CB . ALA A 1 92 ? 57.438 70.891 12.907 1.00 29.97 ? 92 ALA A CB 1 ATOM 710 N N . SER A 1 93 ? 58.343 67.971 11.921 1.00 28.62 ? 93 SER A N 1 ATOM 711 C CA . SER A 1 93 ? 58.139 66.502 11.895 1.00 30.72 ? 93 SER A CA 1 ATOM 712 C C . SER A 1 93 ? 59.273 65.652 12.507 1.00 31.13 ? 93 SER A C 1 ATOM 713 O O . SER A 1 93 ? 59.050 64.491 12.841 1.00 31.83 ? 93 SER A O 1 ATOM 714 C CB . SER A 1 93 ? 57.856 66.002 10.470 1.00 30.85 ? 93 SER A CB 1 ATOM 715 O OG . SER A 1 93 ? 58.725 66.600 9.533 1.00 31.68 ? 93 SER A OG 1 ATOM 716 N N . TYR A 1 94 ? 60.466 66.226 12.645 1.00 32.07 ? 94 TYR A N 1 ATOM 717 C CA . TYR A 1 94 ? 61.596 65.558 13.288 1.00 32.91 ? 94 TYR A CA 1 ATOM 718 C C . TYR A 1 94 ? 61.648 65.791 14.797 1.00 33.01 ? 94 TYR A C 1 ATOM 719 O O . TYR A 1 94 ? 62.420 65.127 15.503 1.00 30.82 ? 94 TYR A O 1 ATOM 720 C CB . TYR A 1 94 ? 62.902 66.030 12.644 1.00 33.99 ? 94 TYR A CB 1 ATOM 721 C CG . TYR A 1 94 ? 62.934 65.789 11.152 1.00 35.35 ? 94 TYR A CG 1 ATOM 722 C CD1 . TYR A 1 94 ? 63.228 64.525 10.634 1.00 35.85 ? 94 TYR A CD1 1 ATOM 723 C CD2 . TYR A 1 94 ? 62.648 66.818 10.255 1.00 36.24 ? 94 TYR A CD2 1 ATOM 724 C CE1 . TYR A 1 94 ? 63.253 64.302 9.269 1.00 36.67 ? 94 TYR A CE1 1 ATOM 725 C CE2 . TYR A 1 94 ? 62.665 66.602 8.884 1.00 36.79 ? 94 TYR A CE2 1 ATOM 726 C CZ . TYR A 1 94 ? 62.973 65.345 8.398 1.00 37.61 ? 94 TYR A CZ 1 ATOM 727 O OH . TYR A 1 94 ? 62.995 65.133 7.042 1.00 38.95 ? 94 TYR A OH 1 ATOM 728 N N . VAL A 1 95 ? 60.820 66.728 15.277 1.00 32.75 ? 95 VAL A N 1 ATOM 729 C CA . VAL A 1 95 ? 60.804 67.162 16.674 1.00 31.54 ? 95 VAL A CA 1 ATOM 730 C C . VAL A 1 95 ? 59.553 66.738 17.451 1.00 29.83 ? 95 VAL A C 1 ATOM 731 O O . VAL A 1 95 ? 59.656 66.465 18.642 1.00 30.90 ? 95 VAL A O 1 ATOM 732 C CB . VAL A 1 95 ? 60.939 68.697 16.752 1.00 32.51 ? 95 VAL A CB 1 ATOM 733 C CG1 . VAL A 1 95 ? 60.910 69.182 18.200 1.00 33.11 ? 95 VAL A CG1 1 ATOM 734 C CG2 . VAL A 1 95 ? 62.216 69.141 16.055 1.00 33.36 ? 95 VAL A CG2 1 ATOM 735 N N . ILE A 1 96 ? 58.383 66.719 16.816 1.00 28.30 ? 96 ILE A N 1 ATOM 736 C CA . ILE A 1 96 ? 57.129 66.380 17.519 1.00 27.95 ? 96 ILE A CA 1 ATOM 737 C C . ILE A 1 96 ? 56.455 65.184 16.883 1.00 26.21 ? 96 ILE A C 1 ATOM 738 O O . ILE A 1 96 ? 56.493 65.021 15.665 1.00 24.45 ? 96 ILE A O 1 ATOM 739 C CB . ILE A 1 96 ? 56.121 67.568 17.584 1.00 28.45 ? 96 ILE A CB 1 ATOM 740 C CG1 . ILE A 1 96 ? 55.823 68.144 16.190 1.00 28.37 ? 96 ILE A CG1 1 ATOM 741 C CG2 . ILE A 1 96 ? 56.679 68.660 18.484 1.00 29.45 ? 96 ILE A CG2 1 ATOM 742 C CD1 . ILE A 1 96 ? 54.653 69.101 16.138 1.00 28.86 ? 96 ILE A CD1 1 ATOM 743 N N . PHE A 1 97 ? 55.839 64.353 17.720 1.00 26.66 ? 97 PHE A N 1 ATOM 744 C CA . PHE A 1 97 ? 55.094 63.179 17.256 1.00 27.87 ? 97 PHE A CA 1 ATOM 745 C C . PHE A 1 97 ? 55.943 62.282 16.339 1.00 29.00 ? 97 PHE A C 1 ATOM 746 O O . PHE A 1 97 ? 55.461 61.759 15.331 1.00 29.37 ? 97 PHE A O 1 ATOM 747 C CB . PHE A 1 97 ? 53.806 63.619 16.536 1.00 27.41 ? 97 PHE A CB 1 ATOM 748 C CG . PHE A 1 97 ? 53.027 64.698 17.257 1.00 26.76 ? 97 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 97 ? 52.866 64.673 18.637 1.00 26.20 ? 97 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 97 ? 52.418 65.721 16.542 1.00 26.24 ? 97 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 97 ? 52.147 65.664 19.288 1.00 26.28 ? 97 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 97 ? 51.697 66.708 17.190 1.00 25.76 ? 97 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 97 ? 51.557 66.678 18.562 1.00 25.30 ? 97 PHE A CZ 1 ATOM 754 N N . THR A 1 98 ? 57.214 62.128 16.690 1.00 31.18 ? 98 THR A N 1 ATOM 755 C CA . THR A 1 98 ? 58.160 61.389 15.849 1.00 34.44 ? 98 THR A CA 1 ATOM 756 C C . THR A 1 98 ? 57.810 59.897 15.812 1.00 35.00 ? 98 THR A C 1 ATOM 757 O O . THR A 1 98 ? 57.826 59.293 14.741 1.00 36.99 ? 98 THR A O 1 ATOM 758 C CB . THR A 1 98 ? 59.601 61.588 16.332 1.00 34.31 ? 98 THR A CB 1 ATOM 759 O OG1 . THR A 1 98 ? 59.691 61.232 17.713 1.00 34.23 ? 98 THR A OG1 1 ATOM 760 C CG2 . THR A 1 98 ? 60.016 63.046 16.170 1.00 34.63 ? 98 THR A CG2 1 ATOM 761 N N . ASP A 1 99 ? 57.430 59.334 16.962 1.00 35.87 ? 99 ASP A N 1 ATOM 762 C CA . ASP A 1 99 ? 56.953 57.944 17.055 1.00 35.78 ? 99 ASP A CA 1 ATOM 763 C C . ASP A 1 99 ? 55.449 57.813 16.712 1.00 36.04 ? 99 ASP A C 1 ATOM 764 O O . ASP A 1 99 ? 54.676 57.232 17.483 1.00 36.76 ? 99 ASP A O 1 ATOM 765 C CB . ASP A 1 99 ? 57.240 57.378 18.461 1.00 35.04 ? 99 ASP A CB 1 ATOM 766 N N . THR A 1 100 ? 55.038 58.365 15.565 1.00 35.00 ? 100 THR A N 1 ATOM 767 C CA . THR A 1 100 ? 53.665 58.232 15.048 1.00 32.96 ? 100 THR A CA 1 ATOM 768 C C . THR A 1 100 ? 53.697 58.165 13.536 1.00 33.30 ? 100 THR A C 1 ATOM 769 O O . THR A 1 100 ? 54.716 58.437 12.926 1.00 32.88 ? 100 THR A O 1 ATOM 770 C CB . THR A 1 100 ? 52.740 59.428 15.423 1.00 32.27 ? 100 THR A CB 1 ATOM 771 O OG1 . THR A 1 100 ? 53.113 60.599 14.678 1.00 30.84 ? 100 THR A OG1 1 ATOM 772 C CG2 . THR A 1 100 ? 52.765 59.718 16.917 1.00 31.71 ? 100 THR A CG2 1 ATOM 773 N N . ASN A 1 101 ? 52.551 57.842 12.945 1.00 36.15 ? 101 ASN A N 1 ATOM 774 C CA . ASN A 1 101 ? 52.372 57.873 11.503 1.00 37.67 ? 101 ASN A CA 1 ATOM 775 C C . ASN A 1 101 ? 51.938 59.286 11.080 1.00 37.78 ? 101 ASN A C 1 ATOM 776 O O . ASN A 1 101 ? 50.789 59.699 11.274 1.00 36.31 ? 101 ASN A O 1 ATOM 777 C CB . ASN A 1 101 ? 51.359 56.805 11.080 1.00 40.89 ? 101 ASN A CB 1 ATOM 778 C CG . ASN A 1 101 ? 51.754 55.411 11.562 1.00 44.44 ? 101 ASN A CG 1 ATOM 779 O OD1 . ASN A 1 101 ? 51.072 54.804 12.396 1.00 46.65 ? 101 ASN A OD1 1 ATOM 780 N ND2 . ASN A 1 101 ? 52.888 54.919 11.071 1.00 44.80 ? 101 ASN A ND2 1 ATOM 781 N N . GLN A 1 102 ? 52.877 60.021 10.500 1.00 36.57 ? 102 GLN A N 1 ATOM 782 C CA . GLN A 1 102 ? 52.687 61.438 10.205 1.00 36.52 ? 102 GLN A CA 1 ATOM 783 C C . GLN A 1 102 ? 51.982 61.636 8.870 1.00 36.17 ? 102 GLN A C 1 ATOM 784 O O . GLN A 1 102 ? 52.330 60.989 7.883 1.00 36.57 ? 102 GLN A O 1 ATOM 785 C CB . GLN A 1 102 ? 54.041 62.154 10.218 1.00 35.23 ? 102 GLN A CB 1 ATOM 786 C CG . GLN A 1 102 ? 54.749 62.007 11.557 1.00 35.06 ? 102 GLN A CG 1 ATOM 787 C CD . GLN A 1 102 ? 56.061 62.748 11.630 1.00 35.47 ? 102 GLN A CD 1 ATOM 788 O OE1 . GLN A 1 102 ? 56.759 62.879 10.636 1.00 37.16 ? 102 GLN A OE1 1 ATOM 789 N NE2 . GLN A 1 102 ? 56.414 63.230 12.826 1.00 35.95 ? 102 GLN A NE2 1 ATOM 790 N N . ASN A 1 103 ? 50.979 62.514 8.862 1.00 34.48 ? 103 ASN A N 1 ATOM 791 C CA . ASN A 1 103 ? 50.292 62.943 7.646 1.00 33.03 ? 103 ASN A CA 1 ATOM 792 C C . ASN A 1 103 ? 50.387 64.452 7.529 1.00 33.15 ? 103 ASN A C 1 ATOM 793 O O . ASN A 1 103 ? 50.480 65.150 8.539 1.00 32.45 ? 103 ASN A O 1 ATOM 794 C CB . ASN A 1 103 ? 48.819 62.565 7.690 1.00 32.72 ? 103 ASN A CB 1 ATOM 795 C CG . ASN A 1 103 ? 48.595 61.085 7.937 1.00 33.26 ? 103 ASN A CG 1 ATOM 796 O OD1 . ASN A 1 103 ? 48.324 60.331 7.005 1.00 34.12 ? 103 ASN A OD1 1 ATOM 797 N ND2 . ASN A 1 103 ? 48.685 60.666 9.197 1.00 32.55 ? 103 ASN A ND2 1 ATOM 798 N N . ILE A 1 104 ? 50.356 64.950 6.300 1.00 32.45 ? 104 ILE A N 1 ATOM 799 C CA . ILE A 1 104 ? 50.271 66.385 6.041 1.00 33.54 ? 104 ILE A CA 1 ATOM 800 C C . ILE A 1 104 ? 48.861 66.690 5.555 1.00 33.01 ? 104 ILE A C 1 ATOM 801 O O . ILE A 1 104 ? 48.378 66.069 4.615 1.00 35.43 ? 104 ILE A O 1 ATOM 802 C CB . ILE A 1 104 ? 51.339 66.858 5.020 1.00 34.35 ? 104 ILE A CB 1 ATOM 803 C CG1 . ILE A 1 104 ? 52.738 66.664 5.623 1.00 34.87 ? 104 ILE A CG1 1 ATOM 804 C CG2 . ILE A 1 104 ? 51.122 68.329 4.622 1.00 34.19 ? 104 ILE A CG2 1 ATOM 805 C CD1 . ILE A 1 104 ? 53.878 66.897 4.651 1.00 36.23 ? 104 ILE A CD1 1 ATOM 806 N N . MET A 1 105 ? 48.200 67.637 6.211 1.00 31.87 ? 105 MET A N 1 ATOM 807 C CA . MET A 1 105 ? 46.879 68.070 5.793 1.00 31.57 ? 105 MET A CA 1 ATOM 808 C C . MET A 1 105 ? 47.021 68.974 4.578 1.00 32.96 ? 105 MET A C 1 ATOM 809 O O . MET A 1 105 ? 48.051 69.603 4.362 1.00 34.72 ? 105 MET A O 1 ATOM 810 C CB . MET A 1 105 ? 46.144 68.780 6.939 1.00 30.22 ? 105 MET A CB 1 ATOM 811 C CG . MET A 1 105 ? 45.768 67.840 8.074 1.00 29.09 ? 105 MET A CG 1 ATOM 812 S SD . MET A 1 105 ? 45.002 68.623 9.508 1.00 28.60 ? 105 MET A SD 1 ATOM 813 C CE . MET A 1 105 ? 46.362 69.613 10.132 1.00 27.61 ? 105 MET A CE 1 ATOM 814 N N . ASN A 1 106 ? 45.958 69.044 3.800 1.00 35.26 ? 106 ASN A N 1 ATOM 815 C CA . ASN A 1 106 ? 45.975 69.710 2.497 1.00 37.94 ? 106 ASN A CA 1 ATOM 816 C C . ASN A 1 106 ? 45.862 71.246 2.566 1.00 38.51 ? 106 ASN A C 1 ATOM 817 O O . ASN A 1 106 ? 45.626 71.874 1.537 1.00 38.32 ? 106 ASN A O 1 ATOM 818 C CB . ASN A 1 106 ? 44.875 69.115 1.575 1.00 40.39 ? 106 ASN A CB 1 ATOM 819 C CG . ASN A 1 106 ? 43.518 68.960 2.277 1.00 42.99 ? 106 ASN A CG 1 ATOM 820 O OD1 . ASN A 1 106 ? 43.429 68.335 3.342 1.00 45.48 ? 106 ASN A OD1 1 ATOM 821 N ND2 . ASN A 1 106 ? 42.462 69.515 1.687 1.00 45.23 ? 106 ASN A ND2 1 ATOM 822 N N . PHE A 1 107 ? 46.068 71.847 3.750 1.00 37.53 ? 107 PHE A N 1 ATOM 823 C CA . PHE A 1 107 ? 45.858 73.287 3.959 1.00 36.04 ? 107 PHE A CA 1 ATOM 824 C C . PHE A 1 107 ? 46.723 73.869 5.083 1.00 34.66 ? 107 PHE A C 1 ATOM 825 O O . PHE A 1 107 ? 47.336 73.144 5.869 1.00 32.45 ? 107 PHE A O 1 ATOM 826 C CB . PHE A 1 107 ? 44.376 73.569 4.248 1.00 35.46 ? 107 PHE A CB 1 ATOM 827 C CG . PHE A 1 107 ? 43.769 72.629 5.241 1.00 35.45 ? 107 PHE A CG 1 ATOM 828 C CD1 . PHE A 1 107 ? 43.205 71.435 4.820 1.00 37.26 ? 107 PHE A CD1 1 ATOM 829 C CD2 . PHE A 1 107 ? 43.783 72.920 6.593 1.00 35.63 ? 107 PHE A CD2 1 ATOM 830 C CE1 . PHE A 1 107 ? 42.661 70.544 5.727 1.00 36.44 ? 107 PHE A CE1 1 ATOM 831 C CE2 . PHE A 1 107 ? 43.234 72.040 7.507 1.00 36.66 ? 107 PHE A CE2 1 ATOM 832 C CZ . PHE A 1 107 ? 42.673 70.847 7.073 1.00 36.36 ? 107 PHE A CZ 1 ATOM 833 N N . ASN A 1 108 ? 46.751 75.197 5.126 1.00 33.15 ? 108 ASN A N 1 ATOM 834 C CA . ASN A 1 108 ? 47.486 75.942 6.123 1.00 33.05 ? 108 ASN A CA 1 ATOM 835 C C . ASN A 1 108 ? 46.673 76.129 7.405 1.00 31.24 ? 108 ASN A C 1 ATOM 836 O O . ASN A 1 108 ? 45.448 75.993 7.416 1.00 31.51 ? 108 ASN A O 1 ATOM 837 C CB . ASN A 1 108 ? 47.883 77.315 5.551 1.00 35.46 ? 108 ASN A CB 1 ATOM 838 C CG . ASN A 1 108 ? 48.956 77.224 4.474 1.00 38.27 ? 108 ASN A CG 1 ATOM 839 O OD1 . ASN A 1 108 ? 49.598 76.189 4.305 1.00 38.32 ? 108 ASN A OD1 1 ATOM 840 N ND2 . ASN A 1 108 ? 49.158 78.320 3.746 1.00 43.04 ? 108 ASN A ND2 1 ATOM 841 N N . ASN A 1 109 ? 47.372 76.480 8.480 1.00 29.69 ? 109 ASN A N 1 ATOM 842 C CA . ASN A 1 109 ? 46.752 76.761 9.780 1.00 28.43 ? 109 ASN A CA 1 ATOM 843 C C . ASN A 1 109 ? 46.075 78.143 9.925 1.00 27.02 ? 109 ASN A C 1 ATOM 844 O O . ASN A 1 109 ? 45.712 78.524 11.042 1.00 28.43 ? 109 ASN A O 1 ATOM 845 C CB . ASN A 1 109 ? 47.788 76.555 10.903 1.00 27.64 ? 109 ASN A CB 1 ATOM 846 C CG . ASN A 1 109 ? 48.835 77.657 10.968 1.00 27.30 ? 109 ASN A CG 1 ATOM 847 O OD1 . ASN A 1 109 ? 49.004 78.454 10.036 1.00 26.83 ? 109 ASN A OD1 1 ATOM 848 N ND2 . ASN A 1 109 ? 49.555 77.697 12.071 1.00 26.84 ? 109 ASN A ND2 1 ATOM 849 N N . THR A 1 110 ? 45.929 78.885 8.824 1.00 25.15 ? 110 THR A N 1 ATOM 850 C CA . THR A 1 110 ? 45.277 80.199 8.824 1.00 24.87 ? 110 THR A CA 1 ATOM 851 C C . THR A 1 110 ? 43.802 80.006 8.606 1.00 24.50 ? 110 THR A C 1 ATOM 852 O O . THR A 1 110 ? 43.408 79.000 8.020 1.00 26.36 ? 110 THR A O 1 ATOM 853 C CB . THR A 1 110 ? 45.785 81.087 7.676 1.00 24.92 ? 110 THR A CB 1 ATOM 854 O OG1 . THR A 1 110 ? 45.419 80.504 6.418 1.00 25.21 ? 110 THR A OG1 1 ATOM 855 C CG2 . THR A 1 110 ? 47.286 81.250 7.738 1.00 25.04 ? 110 THR A CG2 1 ATOM 856 N N . PHE A 1 111 ? 42.984 80.964 9.044 1.00 23.63 ? 111 PHE A N 1 ATOM 857 C CA . PHE A 1 111 ? 41.523 80.874 8.846 1.00 23.65 ? 111 PHE A CA 1 ATOM 858 C C . PHE A 1 111 ? 41.142 80.940 7.365 1.00 24.58 ? 111 PHE A C 1 ATOM 859 O O . PHE A 1 111 ? 40.229 80.262 6.912 1.00 25.71 ? 111 PHE A O 1 ATOM 860 C CB . PHE A 1 111 ? 40.790 81.999 9.575 1.00 23.63 ? 111 PHE A CB 1 ATOM 861 C CG . PHE A 1 111 ? 40.901 81.934 11.063 1.00 22.59 ? 111 PHE A CG 1 ATOM 862 C CD1 . PHE A 1 111 ? 40.422 80.832 11.753 1.00 23.10 ? 111 PHE A CD1 1 ATOM 863 C CD2 . PHE A 1 111 ? 41.461 82.981 11.774 1.00 22.42 ? 111 PHE A CD2 1 ATOM 864 C CE1 . PHE A 1 111 ? 40.514 80.770 13.137 1.00 23.47 ? 111 PHE A CE1 1 ATOM 865 C CE2 . PHE A 1 111 ? 41.549 82.930 13.157 1.00 22.22 ? 111 PHE A CE2 1 ATOM 866 C CZ . PHE A 1 111 ? 41.079 81.825 13.834 1.00 22.65 ? 111 PHE A CZ 1 ATOM 867 N N . GLU A 1 112 ? 41.874 81.752 6.622 1.00 25.43 ? 112 GLU A N 1 ATOM 868 C CA . GLU A 1 112 ? 41.644 81.951 5.190 1.00 26.74 ? 112 GLU A CA 1 ATOM 869 C C . GLU A 1 112 ? 41.725 80.626 4.415 1.00 24.70 ? 112 GLU A C 1 ATOM 870 O O . GLU A 1 112 ? 40.849 80.320 3.604 1.00 23.55 ? 112 GLU A O 1 ATOM 871 C CB . GLU A 1 112 ? 42.672 82.944 4.623 1.00 29.45 ? 112 GLU A CB 1 ATOM 872 C CG . GLU A 1 112 ? 42.505 84.384 5.101 1.00 34.04 ? 112 GLU A CG 1 ATOM 873 C CD . GLU A 1 112 ? 42.834 84.621 6.587 1.00 37.41 ? 112 GLU A CD 1 ATOM 874 O OE1 . GLU A 1 112 ? 43.591 83.817 7.195 1.00 37.56 ? 112 GLU A OE1 1 ATOM 875 O OE2 . GLU A 1 112 ? 42.323 85.624 7.152 1.00 42.43 ? 112 GLU A OE2 1 ATOM 876 N N . SER A 1 113 ? 42.786 79.860 4.678 1.00 23.59 ? 113 SER A N 1 ATOM 877 C CA . SER A 1 113 ? 42.981 78.528 4.087 1.00 23.58 ? 113 SER A CA 1 ATOM 878 C C . SER A 1 113 ? 41.912 77.548 4.538 1.00 23.60 ? 113 SER A C 1 ATOM 879 O O . SER A 1 113 ? 41.289 76.893 3.720 1.00 23.77 ? 113 SER A O 1 ATOM 880 C CB . SER A 1 113 ? 44.358 77.972 4.472 1.00 24.14 ? 113 SER A CB 1 ATOM 881 O OG . SER A 1 113 ? 44.711 76.852 3.690 1.00 24.29 ? 113 SER A OG 1 ATOM 882 N N . ILE A 1 114 ? 41.692 77.471 5.848 1.00 24.18 ? 114 ILE A N 1 ATOM 883 C CA . ILE A 1 114 ? 40.737 76.520 6.431 1.00 24.18 ? 114 ILE A CA 1 ATOM 884 C C . ILE A 1 114 ? 39.312 76.747 5.923 1.00 24.81 ? 114 ILE A C 1 ATOM 885 O O . ILE A 1 114 ? 38.578 75.787 5.660 1.00 24.13 ? 114 ILE A O 1 ATOM 886 C CB . ILE A 1 114 ? 40.750 76.578 7.980 1.00 24.51 ? 114 ILE A CB 1 ATOM 887 C CG1 . ILE A 1 114 ? 42.097 76.111 8.527 1.00 24.68 ? 114 ILE A CG1 1 ATOM 888 C CG2 . ILE A 1 114 ? 39.661 75.682 8.577 1.00 24.60 ? 114 ILE A CG2 1 ATOM 889 C CD1 . ILE A 1 114 ? 42.338 76.521 9.960 1.00 25.06 ? 114 ILE A CD1 1 ATOM 890 N N . GLU A 1 115 ? 38.924 78.016 5.809 1.00 26.22 ? 115 GLU A N 1 ATOM 891 C CA . GLU A 1 115 ? 37.605 78.381 5.305 1.00 26.33 ? 115 GLU A CA 1 ATOM 892 C C . GLU A 1 115 ? 37.461 78.014 3.814 1.00 27.31 ? 115 GLU A C 1 ATOM 893 O O . GLU A 1 115 ? 36.393 77.572 3.391 1.00 28.56 ? 115 GLU A O 1 ATOM 894 C CB . GLU A 1 115 ? 37.327 79.880 5.555 1.00 27.29 ? 115 GLU A CB 1 ATOM 895 C CG . GLU A 1 115 ? 37.109 80.227 7.031 1.00 28.08 ? 115 GLU A CG 1 ATOM 896 C CD . GLU A 1 115 ? 36.772 81.695 7.303 1.00 29.27 ? 115 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 115 ? 36.908 82.559 6.419 1.00 29.19 ? 115 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 115 ? 36.341 81.995 8.433 1.00 31.78 ? 115 GLU A OE2 1 ATOM 899 N N . ILE A 1 116 ? 38.527 78.172 3.027 1.00 27.90 ? 116 ILE A N 1 ATOM 900 C CA . ILE A 1 116 ? 38.486 77.806 1.596 1.00 29.48 ? 116 ILE A CA 1 ATOM 901 C C . ILE A 1 116 ? 38.327 76.288 1.444 1.00 31.06 ? 116 ILE A C 1 ATOM 902 O O . ILE A 1 116 ? 37.441 75.838 0.733 1.00 32.93 ? 116 ILE A O 1 ATOM 903 C CB . ILE A 1 116 ? 39.710 78.350 0.810 1.00 30.55 ? 116 ILE A CB 1 ATOM 904 C CG1 . ILE A 1 116 ? 39.584 79.870 0.659 1.00 31.12 ? 116 ILE A CG1 1 ATOM 905 C CG2 . ILE A 1 116 ? 39.816 77.724 -0.580 1.00 30.88 ? 116 ILE A CG2 1 ATOM 906 C CD1 . ILE A 1 116 ? 40.855 80.564 0.208 1.00 32.51 ? 116 ILE A CD1 1 ATOM 907 N N . VAL A 1 117 ? 39.146 75.510 2.142 1.00 31.62 ? 117 VAL A N 1 ATOM 908 C CA . VAL A 1 117 ? 39.046 74.048 2.090 1.00 33.31 ? 117 VAL A CA 1 ATOM 909 C C . VAL A 1 117 ? 37.758 73.543 2.730 1.00 34.52 ? 117 VAL A C 1 ATOM 910 O O . VAL A 1 117 ? 37.123 72.637 2.202 1.00 37.87 ? 117 VAL A O 1 ATOM 911 C CB . VAL A 1 117 ? 40.288 73.376 2.731 1.00 34.28 ? 117 VAL A CB 1 ATOM 912 C CG1 . VAL A 1 117 ? 40.115 71.859 2.841 1.00 35.10 ? 117 VAL A CG1 1 ATOM 913 C CG2 . VAL A 1 117 ? 41.533 73.730 1.917 1.00 34.24 ? 117 VAL A CG2 1 ATOM 914 N N . GLY A 1 118 ? 37.366 74.128 3.853 1.00 33.64 ? 118 GLY A N 1 ATOM 915 C CA . GLY A 1 118 ? 36.111 73.762 4.499 1.00 34.18 ? 118 GLY A CA 1 ATOM 916 C C . GLY A 1 118 ? 34.858 74.217 3.765 1.00 34.27 ? 118 GLY A C 1 ATOM 917 O O . GLY A 1 118 ? 33.786 73.653 3.969 1.00 33.92 ? 118 GLY A O 1 ATOM 918 N N . GLY A 1 119 ? 34.983 75.252 2.936 1.00 36.85 ? 119 GLY A N 1 ATOM 919 C CA . GLY A 1 119 ? 33.831 75.890 2.283 1.00 38.18 ? 119 GLY A CA 1 ATOM 920 C C . GLY A 1 119 ? 32.821 76.474 3.267 1.00 39.29 ? 119 GLY A C 1 ATOM 921 O O . GLY A 1 119 ? 31.635 76.551 2.968 1.00 43.78 ? 119 GLY A O 1 ATOM 922 N N . THR A 1 120 ? 33.295 76.881 4.442 1.00 38.81 ? 120 THR A N 1 ATOM 923 C CA . THR A 1 120 ? 32.435 77.358 5.516 1.00 37.64 ? 120 THR A CA 1 ATOM 924 C C . THR A 1 120 ? 33.214 78.346 6.379 1.00 34.75 ? 120 THR A C 1 ATOM 925 O O . THR A 1 120 ? 34.377 78.087 6.709 1.00 35.37 ? 120 THR A O 1 ATOM 926 C CB . THR A 1 120 ? 31.905 76.195 6.375 1.00 39.32 ? 120 THR A CB 1 ATOM 927 O OG1 . THR A 1 120 ? 30.930 76.697 7.288 1.00 42.16 ? 120 THR A OG1 1 ATOM 928 C CG2 . THR A 1 120 ? 33.028 75.493 7.163 1.00 41.06 ? 120 THR A CG2 1 ATOM 929 N N . THR A 1 121 ? 32.570 79.456 6.741 1.00 31.36 ? 121 THR A N 1 ATOM 930 C CA . THR A 1 121 ? 33.230 80.568 7.426 1.00 28.99 ? 121 THR A CA 1 ATOM 931 C C . THR A 1 121 ? 33.028 80.529 8.950 1.00 27.65 ? 121 THR A C 1 ATOM 932 O O . THR A 1 121 ? 32.170 79.824 9.467 1.00 26.86 ? 121 THR A O 1 ATOM 933 C CB . THR A 1 121 ? 32.769 81.934 6.859 1.00 29.56 ? 121 THR A CB 1 ATOM 934 O OG1 . THR A 1 121 ? 31.376 82.150 7.122 1.00 28.60 ? 121 THR A OG1 1 ATOM 935 C CG2 . THR A 1 121 ? 33.012 81.993 5.349 1.00 29.91 ? 121 THR A CG2 1 ATOM 936 N N . ARG A 1 122 ? 33.842 81.297 9.658 1.00 25.81 ? 122 ARG A N 1 ATOM 937 C CA . ARG A 1 122 ? 33.702 81.431 11.111 1.00 24.62 ? 122 ARG A CA 1 ATOM 938 C C . ARG A 1 122 ? 32.343 82.011 11.474 1.00 24.30 ? 122 ARG A C 1 ATOM 939 O O . ARG A 1 122 ? 31.723 81.547 12.408 1.00 23.49 ? 122 ARG A O 1 ATOM 940 C CB . ARG A 1 122 ? 34.801 82.315 11.674 1.00 23.04 ? 122 ARG A CB 1 ATOM 941 C CG . ARG A 1 122 ? 36.146 81.644 11.722 1.00 22.33 ? 122 ARG A CG 1 ATOM 942 C CD . ARG A 1 122 ? 37.220 82.690 11.942 1.00 22.10 ? 122 ARG A CD 1 ATOM 943 N NE . ARG A 1 122 ? 37.506 83.472 10.742 1.00 21.03 ? 122 ARG A NE 1 ATOM 944 C CZ . ARG A 1 122 ? 38.276 84.563 10.706 1.00 20.97 ? 122 ARG A CZ 1 ATOM 945 N NH1 . ARG A 1 122 ? 38.843 85.050 11.808 1.00 20.00 ? 122 ARG A NH1 1 ATOM 946 N NH2 . ARG A 1 122 ? 38.461 85.198 9.553 1.00 20.67 ? 122 ARG A NH2 1 ATOM 947 N N . SER A 1 123 ? 31.876 82.996 10.708 1.00 25.47 ? 123 SER A N 1 ATOM 948 C CA . SER A 1 123 ? 30.526 83.564 10.874 1.00 26.26 ? 123 SER A CA 1 ATOM 949 C C . SER A 1 123 ? 29.384 82.549 10.859 1.00 27.81 ? 123 SER A C 1 ATOM 950 O O . SER A 1 123 ? 28.364 82.780 11.489 1.00 29.15 ? 123 SER A O 1 ATOM 951 C CB . SER A 1 123 ? 30.258 84.604 9.798 1.00 26.96 ? 123 SER A CB 1 ATOM 952 O OG . SER A 1 123 ? 30.996 85.779 10.053 1.00 28.38 ? 123 SER A OG 1 ATOM 953 N N . GLU A 1 124 ? 29.548 81.444 10.136 1.00 28.97 ? 124 GLU A N 1 ATOM 954 C CA . GLU A 1 124 ? 28.532 80.402 10.072 1.00 29.45 ? 124 GLU A CA 1 ATOM 955 C C . GLU A 1 124 ? 28.824 79.207 10.968 1.00 29.14 ? 124 GLU A C 1 ATOM 956 O O . GLU A 1 124 ? 28.070 78.246 10.927 1.00 31.64 ? 124 GLU A O 1 ATOM 957 C CB . GLU A 1 124 ? 28.374 79.930 8.626 1.00 29.87 ? 124 GLU A CB 1 ATOM 958 N N . THR A 1 125 ? 29.890 79.238 11.772 1.00 27.97 ? 125 THR A N 1 ATOM 959 C CA . THR A 1 125 ? 30.296 78.055 12.545 1.00 27.14 ? 125 THR A CA 1 ATOM 960 C C . THR A 1 125 ? 29.999 78.271 14.036 1.00 27.78 ? 125 THR A C 1 ATOM 961 O O . THR A 1 125 ? 30.635 79.118 14.676 1.00 27.73 ? 125 THR A O 1 ATOM 962 C CB . THR A 1 125 ? 31.784 77.721 12.360 1.00 26.55 ? 125 THR A CB 1 ATOM 963 O OG1 . THR A 1 125 ? 32.089 77.617 10.964 1.00 27.11 ? 125 THR A OG1 1 ATOM 964 C CG2 . THR A 1 125 ? 32.132 76.390 13.052 1.00 26.62 ? 125 THR A CG2 1 ATOM 965 N N . PRO A 1 126 ? 29.025 77.521 14.594 1.00 27.46 ? 126 PRO A N 1 ATOM 966 C CA . PRO A 1 126 ? 28.701 77.750 16.001 1.00 26.38 ? 126 PRO A CA 1 ATOM 967 C C . PRO A 1 126 ? 29.807 77.315 16.945 1.00 24.36 ? 126 PRO A C 1 ATOM 968 O O . PRO A 1 126 ? 30.540 76.361 16.653 1.00 22.36 ? 126 PRO A O 1 ATOM 969 C CB . PRO A 1 126 ? 27.435 76.906 16.219 1.00 27.46 ? 126 PRO A CB 1 ATOM 970 C CG . PRO A 1 126 ? 26.830 76.795 14.862 1.00 28.54 ? 126 PRO A CG 1 ATOM 971 C CD . PRO A 1 126 ? 28.030 76.630 13.962 1.00 28.55 ? 126 PRO A CD 1 ATOM 972 N N . LEU A 1 127 ? 29.920 78.032 18.062 1.00 22.52 ? 127 LEU A N 1 ATOM 973 C CA . LEU A 1 127 ? 30.856 77.678 19.128 1.00 22.28 ? 127 LEU A CA 1 ATOM 974 C C . LEU A 1 127 ? 30.095 77.437 20.426 1.00 22.16 ? 127 LEU A C 1 ATOM 975 O O . LEU A 1 127 ? 29.054 78.046 20.679 1.00 23.27 ? 127 LEU A O 1 ATOM 976 C CB . LEU A 1 127 ? 31.903 78.776 19.332 1.00 21.84 ? 127 LEU A CB 1 ATOM 977 C CG . LEU A 1 127 ? 32.557 79.365 18.077 1.00 21.73 ? 127 LEU A CG 1 ATOM 978 C CD1 . LEU A 1 127 ? 33.275 80.648 18.451 1.00 21.80 ? 127 LEU A CD1 1 ATOM 979 C CD2 . LEU A 1 127 ? 33.501 78.384 17.416 1.00 21.26 ? 127 LEU A CD2 1 ATOM 980 N N . GLY A 1 128 ? 30.662 76.580 21.259 1.00 21.79 ? 128 GLY A N 1 ATOM 981 C CA . GLY A 1 128 ? 30.066 76.192 22.518 1.00 23.32 ? 128 GLY A CA 1 ATOM 982 C C . GLY A 1 128 ? 30.562 74.820 22.938 1.00 24.20 ? 128 GLY A C 1 ATOM 983 O O . GLY A 1 128 ? 31.412 74.220 22.273 1.00 23.32 ? 128 GLY A O 1 ATOM 984 N N . ILE A 1 129 ? 29.992 74.309 24.019 1.00 26.18 ? 129 ILE A N 1 ATOM 985 C CA . ILE A 1 129 ? 30.517 73.120 24.669 1.00 28.47 ? 129 ILE A CA 1 ATOM 986 C C . ILE A 1 129 ? 30.379 71.905 23.763 1.00 27.25 ? 129 ILE A C 1 ATOM 987 O O . ILE A 1 129 ? 31.323 71.136 23.629 1.00 26.48 ? 129 ILE A O 1 ATOM 988 C CB . ILE A 1 129 ? 29.796 72.782 26.003 1.00 30.87 ? 129 ILE A CB 1 ATOM 989 C CG1 . ILE A 1 129 ? 29.843 73.962 26.988 1.00 32.56 ? 129 ILE A CG1 1 ATOM 990 C CG2 . ILE A 1 129 ? 30.408 71.526 26.645 1.00 30.11 ? 129 ILE A CG2 1 ATOM 991 C CD1 . ILE A 1 129 ? 28.644 74.013 27.922 1.00 33.67 ? 129 ILE A CD1 1 ATOM 992 N N . MET A 1 130 ? 29.198 71.719 23.183 1.00 28.02 ? 130 MET A N 1 ATOM 993 C CA . MET A 1 130 ? 28.963 70.556 22.317 1.00 30.79 ? 130 MET A CA 1 ATOM 994 C C . MET A 1 130 ? 29.864 70.600 21.086 1.00 27.44 ? 130 MET A C 1 ATOM 995 O O . MET A 1 130 ? 30.396 69.570 20.668 1.00 25.80 ? 130 MET A O 1 ATOM 996 C CB . MET A 1 130 ? 27.482 70.435 21.946 1.00 35.59 ? 130 MET A CB 1 ATOM 997 C CG . MET A 1 130 ? 26.645 70.034 23.159 1.00 41.68 ? 130 MET A CG 1 ATOM 998 S SD . MET A 1 130 ? 24.864 69.848 22.904 1.00 50.85 ? 130 MET A SD 1 ATOM 999 C CE . MET A 1 130 ? 24.348 69.303 24.539 1.00 50.08 ? 130 MET A CE 1 ATOM 1000 N N . HIS A 1 131 ? 30.086 71.805 20.562 1.00 24.26 ? 131 HIS A N 1 ATOM 1001 C CA . HIS A 1 131 ? 30.895 71.992 19.363 1.00 23.87 ? 131 HIS A CA 1 ATOM 1002 C C . HIS A 1 131 ? 32.378 71.813 19.658 1.00 22.70 ? 131 HIS A C 1 ATOM 1003 O O . HIS A 1 131 ? 33.131 71.329 18.818 1.00 21.77 ? 131 HIS A O 1 ATOM 1004 C CB . HIS A 1 131 ? 30.593 73.351 18.732 1.00 24.61 ? 131 HIS A CB 1 ATOM 1005 C CG . HIS A 1 131 ? 29.136 73.551 18.440 1.00 25.62 ? 131 HIS A CG 1 ATOM 1006 N ND1 . HIS A 1 131 ? 28.497 72.937 17.381 1.00 26.35 ? 131 HIS A ND1 1 ATOM 1007 C CD2 . HIS A 1 131 ? 28.184 74.266 19.088 1.00 25.32 ? 131 HIS A CD2 1 ATOM 1008 C CE1 . HIS A 1 131 ? 27.222 73.281 17.379 1.00 25.22 ? 131 HIS A CE1 1 ATOM 1009 N NE2 . HIS A 1 131 ? 27.006 74.085 18.404 1.00 24.79 ? 131 HIS A NE2 1 ATOM 1010 N N . PHE A 1 132 ? 32.783 72.174 20.869 1.00 22.24 ? 132 PHE A N 1 ATOM 1011 C CA . PHE A 1 132 ? 34.118 71.879 21.368 1.00 22.65 ? 132 PHE A CA 1 ATOM 1012 C C . PHE A 1 132 ? 34.351 70.363 21.479 1.00 22.33 ? 132 PHE A C 1 ATOM 1013 O O . PHE A 1 132 ? 35.356 69.825 20.992 1.00 21.60 ? 132 PHE A O 1 ATOM 1014 C CB . PHE A 1 132 ? 34.291 72.534 22.738 1.00 23.95 ? 132 PHE A CB 1 ATOM 1015 C CG . PHE A 1 132 ? 35.716 72.598 23.214 1.00 25.15 ? 132 PHE A CG 1 ATOM 1016 C CD1 . PHE A 1 132 ? 36.281 71.541 23.914 1.00 24.78 ? 132 PHE A CD1 1 ATOM 1017 C CD2 . PHE A 1 132 ? 36.484 73.740 22.996 1.00 25.39 ? 132 PHE A CD2 1 ATOM 1018 C CE1 . PHE A 1 132 ? 37.590 71.617 24.369 1.00 25.98 ? 132 PHE A CE1 1 ATOM 1019 C CE2 . PHE A 1 132 ? 37.793 73.819 23.451 1.00 25.40 ? 132 PHE A CE2 1 ATOM 1020 C CZ . PHE A 1 132 ? 38.348 72.760 24.137 1.00 26.00 ? 132 PHE A CZ 1 ATOM 1021 N N . GLU A 1 133 ? 33.413 69.686 22.130 1.00 23.06 ? 133 GLU A N 1 ATOM 1022 C CA . GLU A 1 133 ? 33.517 68.242 22.340 1.00 23.93 ? 133 GLU A CA 1 ATOM 1023 C C . GLU A 1 133 ? 33.533 67.531 20.995 1.00 23.60 ? 133 GLU A C 1 ATOM 1024 O O . GLU A 1 133 ? 34.388 66.667 20.761 1.00 23.11 ? 133 GLU A O 1 ATOM 1025 C CB . GLU A 1 133 ? 32.357 67.716 23.189 1.00 24.01 ? 133 GLU A CB 1 ATOM 1026 C CG . GLU A 1 133 ? 32.550 66.273 23.659 1.00 25.18 ? 133 GLU A CG 1 ATOM 1027 C CD . GLU A 1 133 ? 32.262 65.194 22.602 1.00 26.26 ? 133 GLU A CD 1 ATOM 1028 O OE1 . GLU A 1 133 ? 31.422 65.415 21.703 1.00 25.16 ? 133 GLU A OE1 1 ATOM 1029 O OE2 . GLU A 1 133 ? 32.886 64.106 22.681 1.00 26.54 ? 133 GLU A OE2 1 ATOM 1030 N N . ALA A 1 134 ? 32.585 67.907 20.132 1.00 22.43 ? 134 ALA A N 1 ATOM 1031 C CA . ALA A 1 134 ? 32.448 67.299 18.807 1.00 23.07 ? 134 ALA A CA 1 ATOM 1032 C C . ALA A 1 134 ? 33.697 67.457 17.939 1.00 22.96 ? 134 ALA A C 1 ATOM 1033 O O . ALA A 1 134 ? 34.040 66.552 17.189 1.00 24.27 ? 134 ALA A O 1 ATOM 1034 C CB . ALA A 1 134 ? 31.232 67.866 18.081 1.00 22.86 ? 134 ALA A CB 1 ATOM 1035 N N . SER A 1 135 ? 34.360 68.604 18.043 1.00 22.36 ? 135 SER A N 1 ATOM 1036 C CA . SER A 1 135 ? 35.546 68.898 17.245 1.00 21.82 ? 135 SER A CA 1 ATOM 1037 C C . SER A 1 135 ? 36.722 68.033 17.647 1.00 21.98 ? 135 SER A C 1 ATOM 1038 O O . SER A 1 135 ? 37.503 67.614 16.793 1.00 22.72 ? 135 SER A O 1 ATOM 1039 C CB . SER A 1 135 ? 35.914 70.380 17.366 1.00 21.76 ? 135 SER A CB 1 ATOM 1040 O OG . SER A 1 135 ? 34.869 71.184 16.853 1.00 21.45 ? 135 SER A OG 1 ATOM 1041 N N . ILE A 1 136 ? 36.842 67.755 18.943 1.00 21.98 ? 136 ILE A N 1 ATOM 1042 C CA . ILE A 1 136 ? 37.884 66.858 19.439 1.00 22.27 ? 136 ILE A CA 1 ATOM 1043 C C . ILE A 1 136 ? 37.612 65.451 18.923 1.00 22.81 ? 136 ILE A C 1 ATOM 1044 O O . ILE A 1 136 ? 38.549 64.738 18.563 1.00 22.03 ? 136 ILE A O 1 ATOM 1045 C CB . ILE A 1 136 ? 37.953 66.796 20.985 1.00 22.17 ? 136 ILE A CB 1 ATOM 1046 C CG1 . ILE A 1 136 ? 38.246 68.166 21.591 1.00 22.30 ? 136 ILE A CG1 1 ATOM 1047 C CG2 . ILE A 1 136 ? 39.030 65.813 21.452 1.00 22.55 ? 136 ILE A CG2 1 ATOM 1048 C CD1 . ILE A 1 136 ? 37.770 68.265 23.028 1.00 22.72 ? 136 ILE A CD1 1 ATOM 1049 N N . PHE A 1 137 ? 36.337 65.060 18.905 1.00 23.53 ? 137 PHE A N 1 ATOM 1050 C CA . PHE A 1 137 ? 35.942 63.774 18.310 1.00 25.54 ? 137 PHE A CA 1 ATOM 1051 C C . PHE A 1 137 ? 36.300 63.688 16.812 1.00 24.59 ? 137 PHE A C 1 ATOM 1052 O O . PHE A 1 137 ? 36.936 62.736 16.370 1.00 22.18 ? 137 PHE A O 1 ATOM 1053 C CB . PHE A 1 137 ? 34.444 63.493 18.541 1.00 27.47 ? 137 PHE A CB 1 ATOM 1054 C CG . PHE A 1 137 ? 33.892 62.394 17.671 1.00 29.66 ? 137 PHE A CG 1 ATOM 1055 C CD1 . PHE A 1 137 ? 34.314 61.069 17.850 1.00 30.23 ? 137 PHE A CD1 1 ATOM 1056 C CD2 . PHE A 1 137 ? 32.963 62.679 16.660 1.00 31.23 ? 137 PHE A CD2 1 ATOM 1057 C CE1 . PHE A 1 137 ? 33.822 60.050 17.036 1.00 31.73 ? 137 PHE A CE1 1 ATOM 1058 C CE2 . PHE A 1 137 ? 32.462 61.661 15.849 1.00 32.48 ? 137 PHE A CE2 1 ATOM 1059 C CZ . PHE A 1 137 ? 32.895 60.342 16.040 1.00 32.16 ? 137 PHE A CZ 1 ATOM 1060 N N . HIS A 1 138 ? 35.923 64.701 16.044 1.00 24.40 ? 138 HIS A N 1 ATOM 1061 C CA . HIS A 1 138 ? 36.171 64.665 14.590 1.00 25.26 ? 138 HIS A CA 1 ATOM 1062 C C . HIS A 1 138 ? 37.670 64.649 14.275 1.00 25.35 ? 138 HIS A C 1 ATOM 1063 O O . HIS A 1 138 ? 38.103 63.949 13.377 1.00 26.08 ? 138 HIS A O 1 ATOM 1064 C CB . HIS A 1 138 ? 35.494 65.834 13.886 1.00 25.43 ? 138 HIS A CB 1 ATOM 1065 C CG . HIS A 1 138 ? 33.997 65.785 13.925 1.00 25.99 ? 138 HIS A CG 1 ATOM 1066 N ND1 . HIS A 1 138 ? 33.224 66.841 14.364 1.00 27.27 ? 138 HIS A ND1 1 ATOM 1067 C CD2 . HIS A 1 138 ? 33.133 64.792 13.621 1.00 26.15 ? 138 HIS A CD2 1 ATOM 1068 C CE1 . HIS A 1 138 ? 31.949 66.501 14.314 1.00 26.06 ? 138 HIS A CE1 1 ATOM 1069 N NE2 . HIS A 1 138 ? 31.867 65.264 13.864 1.00 26.29 ? 138 HIS A NE2 1 ATOM 1070 N N . LEU A 1 139 ? 38.457 65.396 15.039 1.00 25.39 ? 139 LEU A N 1 ATOM 1071 C CA . LEU A 1 139 ? 39.899 65.354 14.894 1.00 25.62 ? 139 LEU A CA 1 ATOM 1072 C C . LEU A 1 139 ? 40.482 64.018 15.337 1.00 26.78 ? 139 LEU A C 1 ATOM 1073 O O . LEU A 1 139 ? 41.398 63.517 14.681 1.00 26.68 ? 139 LEU A O 1 ATOM 1074 C CB . LEU A 1 139 ? 40.570 66.493 15.662 1.00 25.38 ? 139 LEU A CB 1 ATOM 1075 C CG . LEU A 1 139 ? 40.383 67.933 15.147 1.00 25.79 ? 139 LEU A CG 1 ATOM 1076 C CD1 . LEU A 1 139 ? 41.376 68.845 15.860 1.00 25.93 ? 139 LEU A CD1 1 ATOM 1077 C CD2 . LEU A 1 139 ? 40.543 68.071 13.640 1.00 25.20 ? 139 LEU A CD2 1 ATOM 1078 N N . PHE A 1 140 ? 39.970 63.432 16.421 1.00 27.45 ? 140 PHE A N 1 ATOM 1079 C CA . PHE A 1 140 ? 40.519 62.159 16.901 1.00 28.89 ? 140 PHE A CA 1 ATOM 1080 C C . PHE A 1 140 ? 40.457 61.059 15.827 1.00 29.56 ? 140 PHE A C 1 ATOM 1081 O O . PHE A 1 140 ? 41.472 60.437 15.520 1.00 30.55 ? 140 PHE A O 1 ATOM 1082 C CB . PHE A 1 140 ? 39.850 61.671 18.187 1.00 28.87 ? 140 PHE A CB 1 ATOM 1083 C CG . PHE A 1 140 ? 40.513 60.447 18.762 1.00 30.08 ? 140 PHE A CG 1 ATOM 1084 C CD1 . PHE A 1 140 ? 41.681 60.561 19.509 1.00 30.24 ? 140 PHE A CD1 1 ATOM 1085 C CD2 . PHE A 1 140 ? 40.005 59.174 18.510 1.00 30.60 ? 140 PHE A CD2 1 ATOM 1086 C CE1 . PHE A 1 140 ? 42.314 59.438 20.011 1.00 30.74 ? 140 PHE A CE1 1 ATOM 1087 C CE2 . PHE A 1 140 ? 40.639 58.045 19.007 1.00 30.25 ? 140 PHE A CE2 1 ATOM 1088 C CZ . PHE A 1 140 ? 41.789 58.177 19.764 1.00 30.14 ? 140 PHE A CZ 1 ATOM 1089 N N . VAL A 1 141 ? 39.282 60.856 15.243 1.00 30.05 ? 141 VAL A N 1 ATOM 1090 C CA . VAL A 1 141 ? 39.112 59.891 14.140 1.00 30.92 ? 141 VAL A CA 1 ATOM 1091 C C . VAL A 1 141 ? 39.566 60.438 12.773 1.00 31.14 ? 141 VAL A C 1 ATOM 1092 O O . VAL A 1 141 ? 39.622 59.694 11.806 1.00 33.06 ? 141 VAL A O 1 ATOM 1093 C CB . VAL A 1 141 ? 37.646 59.366 14.049 1.00 31.82 ? 141 VAL A CB 1 ATOM 1094 C CG1 . VAL A 1 141 ? 37.165 58.884 15.413 1.00 32.10 ? 141 VAL A CG1 1 ATOM 1095 C CG2 . VAL A 1 141 ? 36.681 60.417 13.492 1.00 31.96 ? 141 VAL A CG2 1 ATOM 1096 N N . HIS A 1 142 ? 39.870 61.736 12.699 1.00 32.05 ? 142 HIS A N 1 ATOM 1097 C CA . HIS A 1 142 ? 40.228 62.455 11.458 1.00 31.34 ? 142 HIS A CA 1 ATOM 1098 C C . HIS A 1 142 ? 39.237 62.257 10.301 1.00 31.42 ? 142 HIS A C 1 ATOM 1099 O O . HIS A 1 142 ? 39.610 61.830 9.219 1.00 32.79 ? 142 HIS A O 1 ATOM 1100 C CB . HIS A 1 142 ? 41.679 62.165 11.026 1.00 30.73 ? 142 HIS A CB 1 ATOM 1101 C CG . HIS A 1 142 ? 42.300 63.269 10.211 1.00 30.87 ? 142 HIS A CG 1 ATOM 1102 N ND1 . HIS A 1 142 ? 42.999 64.317 10.775 1.00 32.15 ? 142 HIS A ND1 1 ATOM 1103 C CD2 . HIS A 1 142 ? 42.329 63.486 8.874 1.00 29.90 ? 142 HIS A CD2 1 ATOM 1104 C CE1 . HIS A 1 142 ? 43.422 65.133 9.823 1.00 31.35 ? 142 HIS A CE1 1 ATOM 1105 N NE2 . HIS A 1 142 ? 43.020 64.653 8.661 1.00 31.29 ? 142 HIS A NE2 1 ATOM 1106 N N . ASP A 1 143 ? 37.972 62.555 10.554 1.00 31.85 ? 143 ASP A N 1 ATOM 1107 C CA . ASP A 1 143 ? 36.951 62.574 9.508 1.00 34.49 ? 143 ASP A CA 1 ATOM 1108 C C . ASP A 1 143 ? 37.107 63.872 8.703 1.00 35.24 ? 143 ASP A C 1 ATOM 1109 O O . ASP A 1 143 ? 36.684 64.960 9.145 1.00 34.10 ? 143 ASP A O 1 ATOM 1110 C CB . ASP A 1 143 ? 35.548 62.463 10.123 1.00 35.87 ? 143 ASP A CB 1 ATOM 1111 C CG . ASP A 1 143 ? 34.409 62.444 9.076 1.00 39.94 ? 143 ASP A CG 1 ATOM 1112 O OD1 . ASP A 1 143 ? 34.627 62.706 7.857 1.00 42.33 ? 143 ASP A OD1 1 ATOM 1113 O OD2 . ASP A 1 143 ? 33.259 62.168 9.503 1.00 41.87 ? 143 ASP A OD2 1 ATOM 1114 N N . GLU A 1 144 ? 37.651 63.725 7.497 1.00 34.84 ? 144 GLU A N 1 ATOM 1115 C CA . GLU A 1 144 ? 38.030 64.855 6.642 1.00 36.14 ? 144 GLU A CA 1 ATOM 1116 C C . GLU A 1 144 ? 36.898 65.847 6.344 1.00 34.53 ? 144 GLU A C 1 ATOM 1117 O O . GLU A 1 144 ? 37.159 67.043 6.201 1.00 35.51 ? 144 GLU A O 1 ATOM 1118 C CB . GLU A 1 144 ? 38.647 64.354 5.333 1.00 38.76 ? 144 GLU A CB 1 ATOM 1119 C CG . GLU A 1 144 ? 39.832 63.417 5.538 1.00 41.47 ? 144 GLU A CG 1 ATOM 1120 C CD . GLU A 1 144 ? 40.855 63.503 4.429 1.00 45.11 ? 144 GLU A CD 1 ATOM 1121 O OE2 . GLU A 1 144 ? 42.055 63.586 4.771 1.00 51.12 ? 144 GLU A OE2 1 ATOM 1122 N N . ASN A 1 145 ? 35.652 65.371 6.291 1.00 32.99 ? 145 ASN A N 1 ATOM 1123 C CA . ASN A 1 145 ? 34.484 66.270 6.135 1.00 33.14 ? 145 ASN A CA 1 ATOM 1124 C C . ASN A 1 145 ? 34.345 67.297 7.268 1.00 30.79 ? 145 ASN A C 1 ATOM 1125 O O . ASN A 1 145 ? 33.799 68.384 7.066 1.00 30.10 ? 145 ASN A O 1 ATOM 1126 C CB . ASN A 1 145 ? 33.160 65.491 6.056 1.00 34.84 ? 145 ASN A CB 1 ATOM 1127 C CG . ASN A 1 145 ? 33.130 64.467 4.933 1.00 38.17 ? 145 ASN A CG 1 ATOM 1128 O OD1 . ASN A 1 145 ? 32.819 63.300 5.169 1.00 43.67 ? 145 ASN A OD1 1 ATOM 1129 N ND2 . ASN A 1 145 ? 33.463 64.888 3.713 1.00 37.50 ? 145 ASN A ND2 1 ATOM 1130 N N . TYR A 1 146 ? 34.816 66.933 8.457 1.00 28.65 ? 146 TYR A N 1 ATOM 1131 C CA . TYR A 1 146 ? 34.705 67.775 9.632 1.00 28.61 ? 146 TYR A CA 1 ATOM 1132 C C . TYR A 1 146 ? 36.025 68.349 10.149 1.00 26.93 ? 146 TYR A C 1 ATOM 1133 O O . TYR A 1 146 ? 35.995 69.136 11.086 1.00 28.16 ? 146 TYR A O 1 ATOM 1134 C CB . TYR A 1 146 ? 34.041 66.975 10.753 1.00 29.64 ? 146 TYR A CB 1 ATOM 1135 C CG . TYR A 1 146 ? 32.586 66.644 10.501 1.00 31.08 ? 146 TYR A CG 1 ATOM 1136 C CD1 . TYR A 1 146 ? 31.587 67.605 10.685 1.00 31.42 ? 146 TYR A CD1 1 ATOM 1137 C CD2 . TYR A 1 146 ? 32.204 65.366 10.098 1.00 31.22 ? 146 TYR A CD2 1 ATOM 1138 C CE1 . TYR A 1 146 ? 30.251 67.297 10.468 1.00 32.39 ? 146 TYR A CE1 1 ATOM 1139 C CE2 . TYR A 1 146 ? 30.871 65.046 9.882 1.00 31.92 ? 146 TYR A CE2 1 ATOM 1140 C CZ . TYR A 1 146 ? 29.899 66.008 10.064 1.00 32.89 ? 146 TYR A CZ 1 ATOM 1141 O OH . TYR A 1 146 ? 28.578 65.683 9.853 1.00 34.01 ? 146 TYR A OH 1 ATOM 1142 N N . VAL A 1 147 ? 37.171 67.965 9.588 1.00 25.51 ? 147 VAL A N 1 ATOM 1143 C CA . VAL A 1 147 ? 38.451 68.449 10.116 1.00 24.84 ? 147 VAL A CA 1 ATOM 1144 C C . VAL A 1 147 ? 38.550 69.979 10.050 1.00 24.66 ? 147 VAL A C 1 ATOM 1145 O O . VAL A 1 147 ? 38.848 70.609 11.066 1.00 25.20 ? 147 VAL A O 1 ATOM 1146 C CB . VAL A 1 147 ? 39.673 67.731 9.482 1.00 24.99 ? 147 VAL A CB 1 ATOM 1147 C CG1 . VAL A 1 147 ? 40.969 68.496 9.696 1.00 24.03 ? 147 VAL A CG1 1 ATOM 1148 C CG2 . VAL A 1 147 ? 39.815 66.322 10.066 1.00 25.50 ? 147 VAL A CG2 1 ATOM 1149 N N . PRO A 1 148 ? 38.276 70.578 8.881 1.00 24.16 ? 148 PRO A N 1 ATOM 1150 C CA . PRO A 1 148 ? 38.432 72.032 8.790 1.00 24.38 ? 148 PRO A CA 1 ATOM 1151 C C . PRO A 1 148 ? 37.591 72.813 9.793 1.00 23.92 ? 148 PRO A C 1 ATOM 1152 O O . PRO A 1 148 ? 38.138 73.632 10.538 1.00 22.65 ? 148 PRO A O 1 ATOM 1153 C CB . PRO A 1 148 ? 38.003 72.343 7.348 1.00 25.08 ? 148 PRO A CB 1 ATOM 1154 C CG . PRO A 1 148 ? 38.293 71.081 6.601 1.00 24.63 ? 148 PRO A CG 1 ATOM 1155 C CD . PRO A 1 148 ? 37.946 69.988 7.567 1.00 24.24 ? 148 PRO A CD 1 ATOM 1156 N N . THR A 1 149 ? 36.292 72.537 9.813 1.00 23.57 ? 149 THR A N 1 ATOM 1157 C CA . THR A 1 149 ? 35.365 73.169 10.750 1.00 24.59 ? 149 THR A CA 1 ATOM 1158 C C . THR A 1 149 ? 35.757 72.933 12.226 1.00 24.06 ? 149 THR A C 1 ATOM 1159 O O . THR A 1 149 ? 35.625 73.838 13.056 1.00 24.11 ? 149 THR A O 1 ATOM 1160 C CB . THR A 1 149 ? 33.912 72.733 10.470 1.00 25.70 ? 149 THR A CB 1 ATOM 1161 O OG1 . THR A 1 149 ? 33.015 73.510 11.271 1.00 28.71 ? 149 THR A OG1 1 ATOM 1162 C CG2 . THR A 1 149 ? 33.694 71.270 10.781 1.00 27.01 ? 149 THR A CG2 1 ATOM 1163 N N . SER A 1 150 ? 36.265 71.735 12.533 1.00 22.00 ? 150 SER A N 1 ATOM 1164 C CA . SER A 1 150 ? 36.753 71.416 13.872 1.00 21.56 ? 150 SER A CA 1 ATOM 1165 C C . SER A 1 150 ? 37.926 72.299 14.281 1.00 20.48 ? 150 SER A C 1 ATOM 1166 O O . SER A 1 150 ? 38.073 72.637 15.456 1.00 18.76 ? 150 SER A O 1 ATOM 1167 C CB . SER A 1 150 ? 37.163 69.940 13.978 1.00 21.10 ? 150 SER A CB 1 ATOM 1168 O OG . SER A 1 150 ? 36.049 69.103 13.752 1.00 21.59 ? 150 SER A OG 1 ATOM 1169 N N . PHE A 1 151 ? 38.757 72.668 13.317 1.00 19.62 ? 151 PHE A N 1 ATOM 1170 C CA . PHE A 1 151 ? 39.830 73.599 13.590 1.00 20.17 ? 151 PHE A CA 1 ATOM 1171 C C . PHE A 1 151 ? 39.356 75.034 13.807 1.00 19.03 ? 151 PHE A C 1 ATOM 1172 O O . PHE A 1 151 ? 39.856 75.702 14.701 1.00 17.43 ? 151 PHE A O 1 ATOM 1173 C CB . PHE A 1 151 ? 40.925 73.518 12.528 1.00 21.52 ? 151 PHE A CB 1 ATOM 1174 C CG . PHE A 1 151 ? 41.959 72.485 12.838 1.00 22.21 ? 151 PHE A CG 1 ATOM 1175 C CD1 . PHE A 1 151 ? 42.732 72.601 13.980 1.00 23.04 ? 151 PHE A CD1 1 ATOM 1176 C CD2 . PHE A 1 151 ? 42.145 71.390 12.009 1.00 23.29 ? 151 PHE A CD2 1 ATOM 1177 C CE1 . PHE A 1 151 ? 43.677 71.646 14.287 1.00 24.06 ? 151 PHE A CE1 1 ATOM 1178 C CE2 . PHE A 1 151 ? 43.097 70.440 12.300 1.00 22.92 ? 151 PHE A CE2 1 ATOM 1179 C CZ . PHE A 1 151 ? 43.856 70.560 13.442 1.00 23.49 ? 151 PHE A CZ 1 ATOM 1180 N N . LEU A 1 152 ? 38.382 75.485 13.015 1.00 19.32 ? 152 LEU A N 1 ATOM 1181 C CA . LEU A 1 152 ? 37.738 76.783 13.236 1.00 19.22 ? 152 LEU A CA 1 ATOM 1182 C C . LEU A 1 152 ? 37.210 76.885 14.669 1.00 19.16 ? 152 LEU A C 1 ATOM 1183 O O . LEU A 1 152 ? 37.309 77.934 15.320 1.00 19.02 ? 152 LEU A O 1 ATOM 1184 C CB . LEU A 1 152 ? 36.583 77.016 12.260 1.00 19.00 ? 152 LEU A CB 1 ATOM 1185 C CG . LEU A 1 152 ? 36.874 77.182 10.761 1.00 19.62 ? 152 LEU A CG 1 ATOM 1186 C CD1 . LEU A 1 152 ? 35.586 77.577 10.043 1.00 20.33 ? 152 LEU A CD1 1 ATOM 1187 C CD2 . LEU A 1 152 ? 37.943 78.233 10.507 1.00 19.32 ? 152 LEU A CD2 1 ATOM 1188 N N . VAL A 1 153 ? 36.652 75.786 15.144 1.00 18.57 ? 153 VAL A N 1 ATOM 1189 C CA . VAL A 1 153 ? 36.094 75.729 16.481 1.00 18.76 ? 153 VAL A CA 1 ATOM 1190 C C . VAL A 1 153 ? 37.202 75.820 17.517 1.00 18.74 ? 153 VAL A C 1 ATOM 1191 O O . VAL A 1 153 ? 37.129 76.669 18.406 1.00 19.59 ? 153 VAL A O 1 ATOM 1192 C CB . VAL A 1 153 ? 35.254 74.448 16.694 1.00 17.52 ? 153 VAL A CB 1 ATOM 1193 C CG1 . VAL A 1 153 ? 34.849 74.286 18.149 1.00 18.14 ? 153 VAL A CG1 1 ATOM 1194 C CG2 . VAL A 1 153 ? 34.011 74.501 15.839 1.00 17.63 ? 153 VAL A CG2 1 ATOM 1195 N N . LEU A 1 154 ? 38.210 74.949 17.402 1.00 19.17 ? 154 LEU A N 1 ATOM 1196 C CA . LEU A 1 154 ? 39.252 74.834 18.435 1.00 19.44 ? 154 LEU A CA 1 ATOM 1197 C C . LEU A 1 154 ? 40.286 75.955 18.396 1.00 18.32 ? 154 LEU A C 1 ATOM 1198 O O . LEU A 1 154 ? 40.710 76.417 19.445 1.00 17.40 ? 154 LEU A O 1 ATOM 1199 C CB . LEU A 1 154 ? 39.943 73.473 18.393 1.00 20.07 ? 154 LEU A CB 1 ATOM 1200 C CG . LEU A 1 154 ? 39.066 72.260 18.732 1.00 20.98 ? 154 LEU A CG 1 ATOM 1201 C CD1 . LEU A 1 154 ? 39.894 70.987 18.654 1.00 21.95 ? 154 LEU A CD1 1 ATOM 1202 C CD2 . LEU A 1 154 ? 38.439 72.366 20.111 1.00 21.38 ? 154 LEU A CD2 1 ATOM 1203 N N . ILE A 1 155 ? 40.690 76.399 17.212 1.00 17.34 ? 155 ILE A N 1 ATOM 1204 C CA . ILE A 1 155 ? 41.597 77.553 17.121 1.00 17.08 ? 155 ILE A CA 1 ATOM 1205 C C . ILE A 1 155 ? 40.970 78.730 17.874 1.00 17.01 ? 155 ILE A C 1 ATOM 1206 O O . ILE A 1 155 ? 41.656 79.428 18.628 1.00 17.10 ? 155 ILE A O 1 ATOM 1207 C CB . ILE A 1 155 ? 41.937 77.962 15.660 1.00 17.16 ? 155 ILE A CB 1 ATOM 1208 C CG1 . ILE A 1 155 ? 42.830 76.912 14.998 1.00 17.36 ? 155 ILE A CG1 1 ATOM 1209 C CG2 . ILE A 1 155 ? 42.686 79.309 15.624 1.00 17.04 ? 155 ILE A CG2 1 ATOM 1210 C CD1 . ILE A 1 155 ? 43.078 77.159 13.518 1.00 17.39 ? 155 ILE A CD1 1 ATOM 1211 N N . GLN A 1 156 ? 39.667 78.919 17.704 1.00 15.95 ? 156 GLN A N 1 ATOM 1212 C CA . GLN A 1 156 ? 38.997 80.018 18.364 1.00 16.28 ? 156 GLN A CA 1 ATOM 1213 C C . GLN A 1 156 ? 38.778 79.828 19.863 1.00 16.53 ? 156 GLN A C 1 ATOM 1214 O O . GLN A 1 156 ? 38.994 80.762 20.635 1.00 15.35 ? 156 GLN A O 1 ATOM 1215 C CB . GLN A 1 156 ? 37.687 80.322 17.687 1.00 16.08 ? 156 GLN A CB 1 ATOM 1216 C CG . GLN A 1 156 ? 37.878 80.913 16.296 1.00 16.00 ? 156 GLN A CG 1 ATOM 1217 C CD . GLN A 1 156 ? 36.547 81.117 15.642 1.00 15.73 ? 156 GLN A CD 1 ATOM 1218 O OE1 . GLN A 1 156 ? 35.886 80.149 15.257 1.00 16.25 ? 156 GLN A OE1 1 ATOM 1219 N NE2 . GLN A 1 156 ? 36.113 82.361 15.561 1.00 15.49 ? 156 GLN A NE2 1 ATOM 1220 N N . MET A 1 157 ? 38.353 78.635 20.269 1.00 16.55 ? 157 MET A N 1 ATOM 1221 C CA . MET A 1 157 ? 38.011 78.411 21.672 1.00 17.21 ? 157 MET A CA 1 ATOM 1222 C C . MET A 1 157 ? 39.263 78.253 22.533 1.00 17.08 ? 157 MET A C 1 ATOM 1223 O O . MET A 1 157 ? 39.205 78.461 23.755 1.00 17.99 ? 157 MET A O 1 ATOM 1224 C CB . MET A 1 157 ? 37.007 77.251 21.823 1.00 17.65 ? 157 MET A CB 1 ATOM 1225 C CG . MET A 1 157 ? 35.632 77.638 21.267 1.00 18.15 ? 157 MET A CG 1 ATOM 1226 S SD . MET A 1 157 ? 34.353 76.365 21.301 1.00 18.84 ? 157 MET A SD 1 ATOM 1227 C CE . MET A 1 157 ? 34.000 76.356 23.064 1.00 19.39 ? 157 MET A CE 1 ATOM 1228 N N . VAL A 1 158 ? 40.395 77.936 21.905 1.00 16.81 ? 158 VAL A N 1 ATOM 1229 C CA . VAL A 1 158 ? 41.656 77.751 22.606 1.00 16.93 ? 158 VAL A CA 1 ATOM 1230 C C . VAL A 1 158 ? 42.634 78.905 22.332 1.00 17.02 ? 158 VAL A C 1 ATOM 1231 O O . VAL A 1 158 ? 42.981 79.636 23.252 1.00 16.52 ? 158 VAL A O 1 ATOM 1232 C CB . VAL A 1 158 ? 42.247 76.361 22.282 1.00 17.13 ? 158 VAL A CB 1 ATOM 1233 C CG1 . VAL A 1 158 ? 43.575 76.123 23.000 1.00 17.58 ? 158 VAL A CG1 1 ATOM 1234 C CG2 . VAL A 1 158 ? 41.240 75.282 22.661 1.00 17.19 ? 158 VAL A CG2 1 ATOM 1235 N N . LEU A 1 159 ? 43.058 79.090 21.086 1.00 17.46 ? 159 LEU A N 1 ATOM 1236 C CA . LEU A 1 159 ? 44.139 80.043 20.789 1.00 18.42 ? 159 LEU A CA 1 ATOM 1237 C C . LEU A 1 159 ? 43.660 81.498 20.746 1.00 18.75 ? 159 LEU A C 1 ATOM 1238 O O . LEU A 1 159 ? 44.334 82.393 21.277 1.00 19.24 ? 159 LEU A O 1 ATOM 1239 C CB . LEU A 1 159 ? 44.860 79.688 19.485 1.00 18.83 ? 159 LEU A CB 1 ATOM 1240 C CG . LEU A 1 159 ? 45.427 78.265 19.450 1.00 19.94 ? 159 LEU A CG 1 ATOM 1241 C CD1 . LEU A 1 159 ? 45.971 77.948 18.065 1.00 20.27 ? 159 LEU A CD1 1 ATOM 1242 C CD2 . LEU A 1 159 ? 46.481 78.073 20.530 1.00 20.27 ? 159 LEU A CD2 1 ATOM 1243 N N . GLU A 1 160 ? 42.502 81.738 20.144 1.00 18.28 ? 160 GLU A N 1 ATOM 1244 C CA . GLU A 1 160 ? 41.971 83.112 20.061 1.00 18.50 ? 160 GLU A CA 1 ATOM 1245 C C . GLU A 1 160 ? 41.484 83.580 21.430 1.00 17.23 ? 160 GLU A C 1 ATOM 1246 O O . GLU A 1 160 ? 41.666 84.740 21.800 1.00 17.71 ? 160 GLU A O 1 ATOM 1247 C CB . GLU A 1 160 ? 40.883 83.217 18.989 1.00 19.45 ? 160 GLU A CB 1 ATOM 1248 C CG . GLU A 1 160 ? 41.341 82.776 17.591 1.00 20.22 ? 160 GLU A CG 1 ATOM 1249 C CD . GLU A 1 160 ? 42.606 83.493 17.149 1.00 21.67 ? 160 GLU A CD 1 ATOM 1250 O OE1 . GLU A 1 160 ? 42.590 84.740 17.115 1.00 21.93 ? 160 GLU A OE1 1 ATOM 1251 O OE2 . GLU A 1 160 ? 43.632 82.825 16.862 1.00 24.31 ? 160 GLU A OE2 1 ATOM 1252 N N . ALA A 1 161 ? 40.883 82.663 22.174 1.00 16.80 ? 161 ALA A N 1 ATOM 1253 C CA . ALA A 1 161 ? 40.537 82.880 23.576 1.00 16.52 ? 161 ALA A CA 1 ATOM 1254 C C . ALA A 1 161 ? 41.754 83.180 24.438 1.00 16.69 ? 161 ALA A C 1 ATOM 1255 O O . ALA A 1 161 ? 41.685 84.041 25.320 1.00 16.52 ? 161 ALA A O 1 ATOM 1256 C CB . ALA A 1 161 ? 39.830 81.668 24.110 1.00 16.86 ? 161 ALA A CB 1 ATOM 1257 N N . ALA A 1 162 ? 42.862 82.470 24.200 1.00 16.38 ? 162 ALA A N 1 ATOM 1258 C CA . ALA A 1 162 ? 44.098 82.752 24.917 1.00 16.74 ? 162 ALA A CA 1 ATOM 1259 C C . ALA A 1 162 ? 44.595 84.149 24.597 1.00 16.47 ? 162 ALA A C 1 ATOM 1260 O O . ALA A 1 162 ? 44.937 84.901 25.501 1.00 15.94 ? 162 ALA A O 1 ATOM 1261 C CB . ALA A 1 162 ? 45.174 81.721 24.588 1.00 17.41 ? 162 ALA A CB 1 ATOM 1262 N N . LYS A 1 163 ? 44.615 84.483 23.307 1.00 16.08 ? 163 LYS A N 1 ATOM 1263 C CA . LYS A 1 163 ? 45.050 85.781 22.833 1.00 15.71 ? 163 LYS A CA 1 ATOM 1264 C C . LYS A 1 163 ? 44.213 86.942 23.338 1.00 15.50 ? 163 LYS A C 1 ATOM 1265 O O . LYS A 1 163 ? 44.745 88.027 23.531 1.00 14.92 ? 163 LYS A O 1 ATOM 1266 C CB . LYS A 1 163 ? 45.034 85.817 21.301 1.00 16.15 ? 163 LYS A CB 1 ATOM 1267 C CG . LYS A 1 163 ? 46.157 85.063 20.628 1.00 16.63 ? 163 LYS A CG 1 ATOM 1268 C CD . LYS A 1 163 ? 45.909 85.067 19.129 1.00 17.70 ? 163 LYS A CD 1 ATOM 1269 C CE . LYS A 1 163 ? 46.937 84.280 18.339 1.00 17.81 ? 163 LYS A CE 1 ATOM 1270 N NZ . LYS A 1 163 ? 46.414 84.169 16.947 1.00 18.35 ? 163 LYS A NZ 1 ATOM 1271 N N . PHE A 1 164 ? 42.911 86.726 23.509 1.00 15.99 ? 164 PHE A N 1 ATOM 1272 C CA . PHE A 1 164 ? 41.971 87.815 23.824 1.00 15.92 ? 164 PHE A CA 1 ATOM 1273 C C . PHE A 1 164 ? 41.010 87.480 24.954 1.00 17.16 ? 164 PHE A C 1 ATOM 1274 O O . PHE A 1 164 ? 40.189 86.557 24.834 1.00 16.83 ? 164 PHE A O 1 ATOM 1275 C CB . PHE A 1 164 ? 41.155 88.194 22.593 1.00 15.40 ? 164 PHE A CB 1 ATOM 1276 C CG . PHE A 1 164 ? 41.957 88.870 21.521 1.00 14.72 ? 164 PHE A CG 1 ATOM 1277 C CD1 . PHE A 1 164 ? 42.379 90.194 21.682 1.00 14.55 ? 164 PHE A CD1 1 ATOM 1278 C CD2 . PHE A 1 164 ? 42.279 88.207 20.355 1.00 14.41 ? 164 PHE A CD2 1 ATOM 1279 C CE1 . PHE A 1 164 ? 43.122 90.825 20.707 1.00 14.40 ? 164 PHE A CE1 1 ATOM 1280 C CE2 . PHE A 1 164 ? 43.021 88.837 19.359 1.00 14.50 ? 164 PHE A CE2 1 ATOM 1281 C CZ . PHE A 1 164 ? 43.435 90.148 19.529 1.00 14.43 ? 164 PHE A CZ 1 ATOM 1282 N N . LYS A 1 165 ? 41.077 88.263 26.035 1.00 18.25 ? 165 LYS A N 1 ATOM 1283 C CA . LYS A 1 165 ? 40.135 88.100 27.149 1.00 19.23 ? 165 LYS A CA 1 ATOM 1284 C C . LYS A 1 165 ? 38.674 88.290 26.760 1.00 18.78 ? 165 LYS A C 1 ATOM 1285 O O . LYS A 1 165 ? 37.794 87.662 27.352 1.00 18.68 ? 165 LYS A O 1 ATOM 1286 C CB . LYS A 1 165 ? 40.478 89.031 28.303 1.00 20.78 ? 165 LYS A CB 1 ATOM 1287 C CG . LYS A 1 165 ? 41.764 88.660 28.983 1.00 23.14 ? 165 LYS A CG 1 ATOM 1288 C CD . LYS A 1 165 ? 41.952 89.395 30.292 1.00 26.22 ? 165 LYS A CD 1 ATOM 1289 C CE . LYS A 1 165 ? 43.338 89.095 30.842 1.00 29.20 ? 165 LYS A CE 1 ATOM 1290 N NZ . LYS A 1 165 ? 43.665 89.923 32.035 1.00 32.05 ? 165 LYS A NZ 1 ATOM 1291 N N . PHE A 1 166 ? 38.404 89.134 25.771 1.00 18.61 ? 166 PHE A N 1 ATOM 1292 C CA . PHE A 1 166 ? 37.034 89.286 25.266 1.00 19.05 ? 166 PHE A CA 1 ATOM 1293 C C . PHE A 1 166 ? 36.508 87.953 24.695 1.00 18.90 ? 166 PHE A C 1 ATOM 1294 O O . PHE A 1 166 ? 35.342 87.622 24.900 1.00 19.86 ? 166 PHE A O 1 ATOM 1295 C CB . PHE A 1 166 ? 36.961 90.419 24.234 1.00 19.54 ? 166 PHE A CB 1 ATOM 1296 C CG . PHE A 1 166 ? 35.616 90.575 23.580 1.00 19.74 ? 166 PHE A CG 1 ATOM 1297 C CD1 . PHE A 1 166 ? 35.281 89.828 22.468 1.00 20.16 ? 166 PHE A CD1 1 ATOM 1298 C CD2 . PHE A 1 166 ? 34.699 91.484 24.069 1.00 20.52 ? 166 PHE A CD2 1 ATOM 1299 C CE1 . PHE A 1 166 ? 34.046 89.973 21.857 1.00 21.05 ? 166 PHE A CE1 1 ATOM 1300 C CE2 . PHE A 1 166 ? 33.461 91.644 23.471 1.00 20.69 ? 166 PHE A CE2 1 ATOM 1301 C CZ . PHE A 1 166 ? 33.129 90.883 22.362 1.00 20.82 ? 166 PHE A CZ 1 ATOM 1302 N N . ILE A 1 167 ? 37.368 87.184 24.026 1.00 18.27 ? 167 ILE A N 1 ATOM 1303 C CA . ILE A 1 167 ? 36.954 85.925 23.393 1.00 18.17 ? 167 ILE A CA 1 ATOM 1304 C C . ILE A 1 167 ? 36.781 84.825 24.426 1.00 17.80 ? 167 ILE A C 1 ATOM 1305 O O . ILE A 1 167 ? 35.818 84.079 24.373 1.00 17.48 ? 167 ILE A O 1 ATOM 1306 C CB . ILE A 1 167 ? 37.932 85.523 22.249 1.00 18.00 ? 167 ILE A CB 1 ATOM 1307 C CG1 . ILE A 1 167 ? 37.784 86.559 21.133 1.00 17.79 ? 167 ILE A CG1 1 ATOM 1308 C CG2 . ILE A 1 167 ? 37.678 84.086 21.754 1.00 17.37 ? 167 ILE A CG2 1 ATOM 1309 C CD1 . ILE A 1 167 ? 38.753 86.442 19.981 1.00 18.19 ? 167 ILE A CD1 1 ATOM 1310 N N . GLU A 1 168 ? 37.738 84.718 25.342 1.00 18.94 ? 168 GLU A N 1 ATOM 1311 C CA . GLU A 1 168 ? 37.627 83.871 26.549 1.00 18.73 ? 168 GLU A CA 1 ATOM 1312 C C . GLU A 1 168 ? 36.280 84.067 27.262 1.00 18.74 ? 168 GLU A C 1 ATOM 1313 O O . GLU A 1 168 ? 35.564 83.101 27.581 1.00 17.86 ? 168 GLU A O 1 ATOM 1314 C CB . GLU A 1 168 ? 38.759 84.226 27.516 1.00 19.32 ? 168 GLU A CB 1 ATOM 1315 C CG . GLU A 1 168 ? 38.910 83.266 28.689 1.00 19.95 ? 168 GLU A CG 1 ATOM 1316 C CD . GLU A 1 168 ? 39.561 83.876 29.912 1.00 20.18 ? 168 GLU A CD 1 ATOM 1317 O OE1 . GLU A 1 168 ? 40.171 84.968 29.866 1.00 21.10 ? 168 GLU A OE1 1 ATOM 1318 O OE2 . GLU A 1 168 ? 39.475 83.218 30.952 1.00 22.62 ? 168 GLU A OE2 1 ATOM 1319 N N . GLN A 1 169 ? 35.935 85.330 27.479 1.00 18.97 ? 169 GLN A N 1 ATOM 1320 C CA . GLN A 1 169 ? 34.663 85.696 28.105 1.00 19.73 ? 169 GLN A CA 1 ATOM 1321 C C . GLN A 1 169 ? 33.415 85.356 27.286 1.00 19.69 ? 169 GLN A C 1 ATOM 1322 O O . GLN A 1 169 ? 32.392 85.015 27.871 1.00 20.08 ? 169 GLN A O 1 ATOM 1323 C CB . GLN A 1 169 ? 34.651 87.181 28.498 1.00 20.50 ? 169 GLN A CB 1 ATOM 1324 C CG . GLN A 1 169 ? 33.539 87.553 29.474 1.00 21.38 ? 169 GLN A CG 1 ATOM 1325 C CD . GLN A 1 169 ? 33.552 86.717 30.757 1.00 22.20 ? 169 GLN A CD 1 ATOM 1326 O OE1 . GLN A 1 169 ? 34.613 86.415 31.302 1.00 22.43 ? 169 GLN A OE1 1 ATOM 1327 N NE2 . GLN A 1 169 ? 32.371 86.330 31.228 1.00 23.47 ? 169 GLN A NE2 1 ATOM 1328 N N . LYS A 1 170 ? 33.481 85.431 25.956 1.00 20.01 ? 170 LYS A N 1 ATOM 1329 C CA . LYS A 1 170 ? 32.375 84.924 25.123 1.00 20.41 ? 170 LYS A CA 1 ATOM 1330 C C . LYS A 1 170 ? 32.145 83.436 25.374 1.00 18.85 ? 170 LYS A C 1 ATOM 1331 O O . LYS A 1 170 ? 31.005 82.988 25.486 1.00 19.23 ? 170 LYS A O 1 ATOM 1332 C CB . LYS A 1 170 ? 32.632 85.135 23.630 1.00 21.53 ? 170 LYS A CB 1 ATOM 1333 C CG . LYS A 1 170 ? 32.656 86.587 23.180 1.00 23.56 ? 170 LYS A CG 1 ATOM 1334 C CD . LYS A 1 170 ? 31.268 87.209 23.105 1.00 24.55 ? 170 LYS A CD 1 ATOM 1335 C CE . LYS A 1 170 ? 30.546 86.869 21.820 1.00 26.10 ? 170 LYS A CE 1 ATOM 1336 N NZ . LYS A 1 170 ? 29.127 87.323 21.953 1.00 27.74 ? 170 LYS A NZ 1 ATOM 1337 N N . VAL A 1 171 ? 33.232 82.684 25.470 1.00 18.43 ? 171 VAL A N 1 ATOM 1338 C CA . VAL A 1 171 ? 33.163 81.236 25.676 1.00 18.86 ? 171 VAL A CA 1 ATOM 1339 C C . VAL A 1 171 ? 32.620 80.919 27.066 1.00 19.78 ? 171 VAL A C 1 ATOM 1340 O O . VAL A 1 171 ? 31.752 80.044 27.225 1.00 19.77 ? 171 VAL A O 1 ATOM 1341 C CB . VAL A 1 171 ? 34.530 80.558 25.493 1.00 18.50 ? 171 VAL A CB 1 ATOM 1342 C CG1 . VAL A 1 171 ? 34.452 79.080 25.861 1.00 19.01 ? 171 VAL A CG1 1 ATOM 1343 C CG2 . VAL A 1 171 ? 35.007 80.706 24.062 1.00 18.91 ? 171 VAL A CG2 1 ATOM 1344 N N . ILE A 1 172 ? 33.126 81.636 28.067 1.00 21.12 ? 172 ILE A N 1 ATOM 1345 C CA . ILE A 1 172 ? 32.618 81.505 29.442 1.00 21.69 ? 172 ILE A CA 1 ATOM 1346 C C . ILE A 1 172 ? 31.113 81.768 29.458 1.00 23.31 ? 172 ILE A C 1 ATOM 1347 O O . ILE A 1 172 ? 30.367 80.995 30.047 1.00 22.57 ? 172 ILE A O 1 ATOM 1348 C CB . ILE A 1 172 ? 33.376 82.435 30.421 1.00 20.90 ? 172 ILE A CB 1 ATOM 1349 C CG1 . ILE A 1 172 ? 34.805 81.905 30.624 1.00 20.82 ? 172 ILE A CG1 1 ATOM 1350 C CG2 . ILE A 1 172 ? 32.656 82.539 31.763 1.00 20.63 ? 172 ILE A CG2 1 ATOM 1351 C CD1 . ILE A 1 172 ? 35.747 82.858 31.330 1.00 20.70 ? 172 ILE A CD1 1 ATOM 1352 N N . HIS A 1 173 ? 30.666 82.833 28.790 1.00 26.86 ? 173 HIS A N 1 ATOM 1353 C CA . HIS A 1 173 ? 29.231 83.145 28.732 1.00 29.27 ? 173 HIS A CA 1 ATOM 1354 C C . HIS A 1 173 ? 28.437 81.975 28.128 1.00 29.90 ? 173 HIS A C 1 ATOM 1355 O O . HIS A 1 173 ? 27.397 81.609 28.666 1.00 32.13 ? 173 HIS A O 1 ATOM 1356 C CB . HIS A 1 173 ? 28.947 84.448 27.967 1.00 32.90 ? 173 HIS A CB 1 ATOM 1357 C CG . HIS A 1 173 ? 29.137 85.701 28.778 1.00 36.85 ? 173 HIS A CG 1 ATOM 1358 N ND1 . HIS A 1 173 ? 28.502 85.917 29.986 1.00 39.88 ? 173 HIS A ND1 1 ATOM 1359 C CD2 . HIS A 1 173 ? 29.845 86.827 28.523 1.00 38.20 ? 173 HIS A CD2 1 ATOM 1360 C CE1 . HIS A 1 173 ? 28.836 87.107 30.454 1.00 39.13 ? 173 HIS A CE1 1 ATOM 1361 N NE2 . HIS A 1 173 ? 29.649 87.680 29.585 1.00 39.47 ? 173 HIS A NE2 1 ATOM 1362 N N . SER A 1 174 ? 28.943 81.369 27.053 1.00 29.22 ? 174 SER A N 1 ATOM 1363 C CA . SER A 1 174 ? 28.285 80.198 26.444 1.00 29.21 ? 174 SER A CA 1 ATOM 1364 C C . SER A 1 174 ? 28.284 78.972 27.339 1.00 28.94 ? 174 SER A C 1 ATOM 1365 O O . SER A 1 174 ? 27.326 78.213 27.323 1.00 31.31 ? 174 SER A O 1 ATOM 1366 C CB . SER A 1 174 ? 28.920 79.810 25.096 1.00 29.38 ? 174 SER A CB 1 ATOM 1367 O OG . SER A 1 174 ? 30.162 79.140 25.262 1.00 30.05 ? 174 SER A OG 1 ATOM 1368 N N . ILE A 1 175 ? 29.366 78.754 28.082 1.00 28.85 ? 175 ILE A N 1 ATOM 1369 C CA . ILE A 1 175 ? 29.469 77.600 28.970 1.00 29.64 ? 175 ILE A CA 1 ATOM 1370 C C . ILE A 1 175 ? 28.394 77.678 30.059 1.00 30.58 ? 175 ILE A C 1 ATOM 1371 O O . ILE A 1 175 ? 27.587 76.765 30.206 1.00 29.75 ? 175 ILE A O 1 ATOM 1372 C CB . ILE A 1 175 ? 30.884 77.477 29.587 1.00 29.81 ? 175 ILE A CB 1 ATOM 1373 C CG1 . ILE A 1 175 ? 31.889 77.093 28.506 1.00 29.67 ? 175 ILE A CG1 1 ATOM 1374 C CG2 . ILE A 1 175 ? 30.920 76.422 30.693 1.00 30.84 ? 175 ILE A CG2 1 ATOM 1375 C CD1 . ILE A 1 175 ? 33.334 77.369 28.868 1.00 29.42 ? 175 ILE A CD1 1 ATOM 1376 N N . MET A 1 176 ? 28.351 78.783 30.790 1.00 32.80 ? 176 MET A N 1 ATOM 1377 C CA . MET A 1 176 ? 27.386 78.901 31.889 1.00 35.89 ? 176 MET A CA 1 ATOM 1378 C C . MET A 1 176 ? 25.946 79.291 31.498 1.00 35.37 ? 176 MET A C 1 ATOM 1379 O O . MET A 1 176 ? 25.033 79.066 32.283 1.00 36.65 ? 176 MET A O 1 ATOM 1380 C CB . MET A 1 176 ? 27.932 79.782 33.000 1.00 37.96 ? 176 MET A CB 1 ATOM 1381 C CG . MET A 1 176 ? 28.150 81.237 32.669 1.00 39.56 ? 176 MET A CG 1 ATOM 1382 S SD . MET A 1 176 ? 29.342 81.863 33.863 1.00 43.36 ? 176 MET A SD 1 ATOM 1383 C CE . MET A 1 176 ? 28.318 81.979 35.332 1.00 44.06 ? 176 MET A CE 1 ATOM 1384 N N . ASP A 1 177 ? 25.729 79.834 30.303 1.00 35.52 ? 177 ASP A N 1 ATOM 1385 C CA . ASP A 1 177 ? 24.370 79.933 29.742 1.00 35.80 ? 177 ASP A CA 1 ATOM 1386 C C . ASP A 1 177 ? 23.926 78.657 29.017 1.00 35.61 ? 177 ASP A C 1 ATOM 1387 O O . ASP A 1 177 ? 22.756 78.527 28.687 1.00 32.95 ? 177 ASP A O 1 ATOM 1388 C CB . ASP A 1 177 ? 24.252 81.105 28.764 1.00 36.95 ? 177 ASP A CB 1 ATOM 1389 C CG . ASP A 1 177 ? 24.538 82.445 29.413 1.00 39.83 ? 177 ASP A CG 1 ATOM 1390 O OD1 . ASP A 1 177 ? 24.534 82.501 30.659 1.00 39.83 ? 177 ASP A OD1 1 ATOM 1391 O OD2 . ASP A 1 177 ? 24.767 83.438 28.672 1.00 41.52 ? 177 ASP A OD2 1 ATOM 1392 N N . MET A 1 178 ? 24.852 77.733 28.759 1.00 36.89 ? 178 MET A N 1 ATOM 1393 C CA . MET A 1 178 ? 24.593 76.559 27.917 1.00 39.91 ? 178 MET A CA 1 ATOM 1394 C C . MET A 1 178 ? 23.919 76.972 26.604 1.00 39.14 ? 178 MET A C 1 ATOM 1395 O O . MET A 1 178 ? 22.949 76.357 26.154 1.00 40.26 ? 178 MET A O 1 ATOM 1396 C CB . MET A 1 178 ? 23.754 75.514 28.657 1.00 44.41 ? 178 MET A CB 1 ATOM 1397 C CG . MET A 1 178 ? 24.443 74.854 29.841 1.00 48.98 ? 178 MET A CG 1 ATOM 1398 S SD . MET A 1 178 ? 23.251 74.161 31.016 1.00 55.18 ? 178 MET A SD 1 ATOM 1399 C CE . MET A 1 178 ? 22.521 75.664 31.688 1.00 52.79 ? 178 MET A CE 1 ATOM 1400 N N . GLU A 1 179 ? 24.446 78.034 26.005 1.00 37.30 ? 179 GLU A N 1 ATOM 1401 C CA . GLU A 1 179 ? 23.893 78.599 24.796 1.00 36.12 ? 179 GLU A CA 1 ATOM 1402 C C . GLU A 1 179 ? 25.024 78.809 23.806 1.00 32.32 ? 179 GLU A C 1 ATOM 1403 O O . GLU A 1 179 ? 26.006 79.480 24.112 1.00 29.03 ? 179 GLU A O 1 ATOM 1404 C CB . GLU A 1 179 ? 23.204 79.915 25.127 1.00 40.22 ? 179 GLU A CB 1 ATOM 1405 C CG . GLU A 1 179 ? 22.658 80.651 23.916 1.00 44.73 ? 179 GLU A CG 1 ATOM 1406 C CD . GLU A 1 179 ? 21.514 81.590 24.255 1.00 49.59 ? 179 GLU A CD 1 ATOM 1407 O OE1 . GLU A 1 179 ? 21.478 82.113 25.398 1.00 51.07 ? 179 GLU A OE1 1 ATOM 1408 O OE2 . GLU A 1 179 ? 20.645 81.800 23.371 1.00 52.47 ? 179 GLU A OE2 1 ATOM 1409 N N . ASP A 1 180 ? 24.877 78.228 22.619 1.00 30.04 ? 180 ASP A N 1 ATOM 1410 C CA . ASP A 1 180 ? 25.874 78.368 21.559 1.00 29.11 ? 180 ASP A CA 1 ATOM 1411 C C . ASP A 1 180 ? 25.869 79.770 21.004 1.00 26.15 ? 180 ASP A C 1 ATOM 1412 O O . ASP A 1 180 ? 24.911 80.503 21.176 1.00 24.99 ? 180 ASP A O 1 ATOM 1413 C CB . ASP A 1 180 ? 25.593 77.381 20.421 1.00 31.78 ? 180 ASP A CB 1 ATOM 1414 C CG . ASP A 1 180 ? 25.704 75.935 20.864 1.00 34.78 ? 180 ASP A CG 1 ATOM 1415 O OD1 . ASP A 1 180 ? 26.347 75.664 21.900 1.00 37.91 ? 180 ASP A OD1 1 ATOM 1416 O OD2 . ASP A 1 180 ? 25.143 75.060 20.176 1.00 39.37 ? 180 ASP A OD2 1 ATOM 1417 N N . PHE A 1 181 ? 26.957 80.138 20.349 1.00 25.61 ? 181 PHE A N 1 ATOM 1418 C CA . PHE A 1 181 ? 27.036 81.414 19.638 1.00 24.74 ? 181 PHE A CA 1 ATOM 1419 C C . PHE A 1 181 ? 27.891 81.259 18.412 1.00 24.05 ? 181 PHE A C 1 ATOM 1420 O O . PHE A 1 181 ? 28.676 80.316 18.315 1.00 23.41 ? 181 PHE A O 1 ATOM 1421 C CB . PHE A 1 181 ? 27.608 82.526 20.529 1.00 24.70 ? 181 PHE A CB 1 ATOM 1422 C CG . PHE A 1 181 ? 29.082 82.380 20.843 1.00 24.75 ? 181 PHE A CG 1 ATOM 1423 C CD1 . PHE A 1 181 ? 29.536 81.382 21.720 1.00 25.50 ? 181 PHE A CD1 1 ATOM 1424 C CD2 . PHE A 1 181 ? 30.020 83.235 20.270 1.00 23.84 ? 181 PHE A CD2 1 ATOM 1425 C CE1 . PHE A 1 181 ? 30.897 81.253 22.012 1.00 24.89 ? 181 PHE A CE1 1 ATOM 1426 C CE2 . PHE A 1 181 ? 31.377 83.103 20.552 1.00 23.18 ? 181 PHE A CE2 1 ATOM 1427 C CZ . PHE A 1 181 ? 31.816 82.122 21.420 1.00 24.17 ? 181 PHE A CZ 1 ATOM 1428 N N . THR A 1 182 ? 27.721 82.188 17.477 1.00 24.02 ? 182 THR A N 1 ATOM 1429 C CA . THR A 1 182 ? 28.623 82.324 16.349 1.00 24.53 ? 182 THR A CA 1 ATOM 1430 C C . THR A 1 182 ? 29.317 83.659 16.493 1.00 23.94 ? 182 THR A C 1 ATOM 1431 O O . THR A 1 182 ? 28.678 84.619 16.868 1.00 24.05 ? 182 THR A O 1 ATOM 1432 C CB . THR A 1 182 ? 27.877 82.347 15.021 1.00 25.36 ? 182 THR A CB 1 ATOM 1433 O OG1 . THR A 1 182 ? 26.867 83.366 15.071 1.00 26.67 ? 182 THR A OG1 1 ATOM 1434 C CG2 . THR A 1 182 ? 27.252 80.985 14.728 1.00 25.89 ? 182 THR A CG2 1 ATOM 1435 N N . PRO A 1 183 ? 30.613 83.731 16.164 1.00 24.67 ? 183 PRO A N 1 ATOM 1436 C CA . PRO A 1 183 ? 31.346 84.973 16.330 1.00 25.87 ? 183 PRO A CA 1 ATOM 1437 C C . PRO A 1 183 ? 30.825 86.111 15.449 1.00 26.08 ? 183 PRO A C 1 ATOM 1438 O O . PRO A 1 183 ? 30.554 85.896 14.269 1.00 26.49 ? 183 PRO A O 1 ATOM 1439 C CB . PRO A 1 183 ? 32.774 84.583 15.918 1.00 25.96 ? 183 PRO A CB 1 ATOM 1440 C CG . PRO A 1 183 ? 32.593 83.427 15.010 1.00 25.91 ? 183 PRO A CG 1 ATOM 1441 C CD . PRO A 1 183 ? 31.489 82.668 15.641 1.00 25.55 ? 183 PRO A CD 1 ATOM 1442 N N . GLY A 1 184 ? 30.680 87.293 16.040 1.00 25.28 ? 184 GLY A N 1 ATOM 1443 C CA . GLY A 1 184 ? 30.268 88.495 15.321 1.00 24.37 ? 184 GLY A CA 1 ATOM 1444 C C . GLY A 1 184 ? 31.467 89.381 15.060 1.00 23.28 ? 184 GLY A C 1 ATOM 1445 O O . GLY A 1 184 ? 32.597 88.949 15.218 1.00 24.49 ? 184 GLY A O 1 ATOM 1446 N N . LEU A 1 185 ? 31.208 90.627 14.672 1.00 22.53 ? 185 LEU A N 1 ATOM 1447 C CA . LEU A 1 185 ? 32.254 91.563 14.224 1.00 21.78 ? 185 LEU A CA 1 ATOM 1448 C C . LEU A 1 185 ? 33.268 91.888 15.314 1.00 20.39 ? 185 LEU A C 1 ATOM 1449 O O . LEU A 1 185 ? 34.450 92.091 15.023 1.00 19.17 ? 185 LEU A O 1 ATOM 1450 C CB . LEU A 1 185 ? 31.618 92.861 13.714 1.00 22.49 ? 185 LEU A CB 1 ATOM 1451 C CG . LEU A 1 185 ? 30.833 92.762 12.403 1.00 23.07 ? 185 LEU A CG 1 ATOM 1452 C CD1 . LEU A 1 185 ? 30.091 94.053 12.115 1.00 23.13 ? 185 LEU A CD1 1 ATOM 1453 C CD2 . LEU A 1 185 ? 31.750 92.432 11.245 1.00 24.07 ? 185 LEU A CD2 1 ATOM 1454 N N . ALA A 1 186 ? 32.804 91.907 16.568 1.00 18.89 ? 186 ALA A N 1 ATOM 1455 C CA . ALA A 1 186 ? 33.674 92.154 17.707 1.00 17.94 ? 186 ALA A CA 1 ATOM 1456 C C . ALA A 1 186 ? 34.799 91.123 17.798 1.00 17.61 ? 186 ALA A C 1 ATOM 1457 O O . ALA A 1 186 ? 35.982 91.465 17.769 1.00 16.13 ? 186 ALA A O 1 ATOM 1458 C CB . ALA A 1 186 ? 32.854 92.171 18.996 1.00 17.91 ? 186 ALA A CB 1 ATOM 1459 N N . MET A 1 187 ? 34.399 89.857 17.863 1.00 18.26 ? 187 MET A N 1 ATOM 1460 C CA . MET A 1 187 ? 35.316 88.736 17.933 1.00 18.50 ? 187 MET A CA 1 ATOM 1461 C C . MET A 1 187 ? 36.208 88.609 16.696 1.00 18.45 ? 187 MET A C 1 ATOM 1462 O O . MET A 1 187 ? 37.424 88.461 16.827 1.00 18.54 ? 187 MET A O 1 ATOM 1463 C CB . MET A 1 187 ? 34.513 87.461 18.122 1.00 19.89 ? 187 MET A CB 1 ATOM 1464 C CG . MET A 1 187 ? 35.358 86.223 18.314 1.00 21.41 ? 187 MET A CG 1 ATOM 1465 S SD . MET A 1 187 ? 34.458 84.947 19.212 1.00 23.80 ? 187 MET A SD 1 ATOM 1466 C CE . MET A 1 187 ? 35.565 83.554 18.980 1.00 23.74 ? 187 MET A CE 1 ATOM 1467 N N . LEU A 1 188 ? 35.619 88.691 15.504 1.00 17.69 ? 188 LEU A N 1 ATOM 1468 C CA . LEU A 1 188 ? 36.399 88.513 14.266 1.00 17.94 ? 188 LEU A CA 1 ATOM 1469 C C . LEU A 1 188 ? 37.374 89.656 14.027 1.00 17.54 ? 188 LEU A C 1 ATOM 1470 O O . LEU A 1 188 ? 38.485 89.415 13.546 1.00 17.90 ? 188 LEU A O 1 ATOM 1471 C CB . LEU A 1 188 ? 35.492 88.345 13.048 1.00 18.54 ? 188 LEU A CB 1 ATOM 1472 C CG . LEU A 1 188 ? 34.491 87.183 13.113 1.00 19.08 ? 188 LEU A CG 1 ATOM 1473 C CD1 . LEU A 1 188 ? 33.479 87.301 11.982 1.00 20.19 ? 188 LEU A CD1 1 ATOM 1474 C CD2 . LEU A 1 188 ? 35.201 85.846 13.079 1.00 18.88 ? 188 LEU A CD2 1 ATOM 1475 N N . SER A 1 189 ? 36.984 90.891 14.378 1.00 17.20 ? 189 SER A N 1 ATOM 1476 C CA . SER A 1 189 ? 37.899 92.027 14.273 1.00 16.25 ? 189 SER A CA 1 ATOM 1477 C C . SER A 1 189 ? 39.109 91.820 15.158 1.00 16.05 ? 189 SER A C 1 ATOM 1478 O O . SER A 1 189 ? 40.218 92.176 14.770 1.00 16.52 ? 189 SER A O 1 ATOM 1479 C CB . SER A 1 189 ? 37.204 93.378 14.566 1.00 16.48 ? 189 SER A CB 1 ATOM 1480 O OG . SER A 1 189 ? 36.790 93.532 15.929 1.00 16.53 ? 189 SER A OG 1 ATOM 1481 N N . LEU A 1 190 ? 38.923 91.237 16.342 1.00 15.98 ? 190 LEU A N 1 ATOM 1482 C CA . LEU A 1 190 ? 40.070 90.914 17.190 1.00 16.36 ? 190 LEU A CA 1 ATOM 1483 C C . LEU A 1 190 ? 40.977 89.883 16.537 1.00 16.61 ? 190 LEU A C 1 ATOM 1484 O O . LEU A 1 190 ? 42.171 90.120 16.396 1.00 15.94 ? 190 LEU A O 1 ATOM 1485 C CB . LEU A 1 190 ? 39.638 90.405 18.577 1.00 16.49 ? 190 LEU A CB 1 ATOM 1486 C CG . LEU A 1 190 ? 38.945 91.435 19.476 1.00 15.99 ? 190 LEU A CG 1 ATOM 1487 C CD1 . LEU A 1 190 ? 38.383 90.766 20.717 1.00 16.18 ? 190 LEU A CD1 1 ATOM 1488 C CD2 . LEU A 1 190 ? 39.874 92.593 19.853 1.00 15.89 ? 190 LEU A CD2 1 ATOM 1489 N N . GLU A 1 191 ? 40.402 88.745 16.155 1.00 18.39 ? 191 GLU A N 1 ATOM 1490 C CA . GLU A 1 191 ? 41.147 87.650 15.518 1.00 19.55 ? 191 GLU A CA 1 ATOM 1491 C C . GLU A 1 191 ? 41.934 88.177 14.312 1.00 21.25 ? 191 GLU A C 1 ATOM 1492 O O . GLU A 1 191 ? 43.118 87.886 14.139 1.00 21.88 ? 191 GLU A O 1 ATOM 1493 C CB . GLU A 1 191 ? 40.201 86.534 15.045 1.00 19.95 ? 191 GLU A CB 1 ATOM 1494 C CG . GLU A 1 191 ? 39.493 85.775 16.158 1.00 20.71 ? 191 GLU A CG 1 ATOM 1495 C CD . GLU A 1 191 ? 38.537 84.683 15.683 1.00 21.65 ? 191 GLU A CD 1 ATOM 1496 O OE1 . GLU A 1 191 ? 38.552 84.273 14.503 1.00 22.80 ? 191 GLU A OE1 1 ATOM 1497 O OE2 . GLU A 1 191 ? 37.749 84.217 16.525 1.00 21.57 ? 191 GLU A OE2 1 ATOM 1498 N N . GLU A 1 192 ? 41.271 88.974 13.489 1.00 22.39 ? 192 GLU A N 1 ATOM 1499 C CA . GLU A 1 192 ? 41.876 89.452 12.262 1.00 24.96 ? 192 GLU A CA 1 ATOM 1500 C C . GLU A 1 192 ? 43.085 90.363 12.498 1.00 23.30 ? 192 GLU A C 1 ATOM 1501 O O . GLU A 1 192 ? 44.032 90.340 11.713 1.00 22.72 ? 192 GLU A O 1 ATOM 1502 C CB . GLU A 1 192 ? 40.839 90.179 11.409 1.00 28.64 ? 192 GLU A CB 1 ATOM 1503 C CG . GLU A 1 192 ? 41.329 90.408 9.990 1.00 34.34 ? 192 GLU A CG 1 ATOM 1504 C CD . GLU A 1 192 ? 40.286 91.043 9.103 1.00 39.34 ? 192 GLU A CD 1 ATOM 1505 O OE1 . GLU A 1 192 ? 39.811 92.152 9.464 1.00 43.85 ? 192 GLU A OE1 1 ATOM 1506 O OE2 . GLU A 1 192 ? 39.962 90.432 8.049 1.00 43.95 ? 192 GLU A OE2 1 ATOM 1507 N N . ASN A 1 193 ? 43.056 91.143 13.579 1.00 21.35 ? 193 ASN A N 1 ATOM 1508 C CA . ASN A 1 193 ? 44.044 92.200 13.811 1.00 20.56 ? 193 ASN A CA 1 ATOM 1509 C C . ASN A 1 193 ? 45.127 91.940 14.851 1.00 20.47 ? 193 ASN A C 1 ATOM 1510 O O . ASN A 1 193 ? 45.950 92.836 15.108 1.00 18.97 ? 193 ASN A O 1 ATOM 1511 C CB . ASN A 1 193 ? 43.300 93.490 14.152 1.00 21.11 ? 193 ASN A CB 1 ATOM 1512 C CG . ASN A 1 193 ? 42.713 94.146 12.921 1.00 20.41 ? 193 ASN A CG 1 ATOM 1513 O OD1 . ASN A 1 193 ? 43.438 94.702 12.118 1.00 20.62 ? 193 ASN A OD1 1 ATOM 1514 N ND2 . ASN A 1 193 ? 41.406 94.085 12.773 1.00 19.96 ? 193 ASN A ND2 1 ATOM 1515 N N . TRP A 1 194 ? 45.161 90.727 15.430 1.00 20.08 ? 194 TRP A N 1 ATOM 1516 C CA . TRP A 1 194 ? 46.154 90.387 16.460 1.00 20.18 ? 194 TRP A CA 1 ATOM 1517 C C . TRP A 1 194 ? 47.589 90.725 16.029 1.00 20.14 ? 194 TRP A C 1 ATOM 1518 O O . TRP A 1 194 ? 48.353 91.302 16.785 1.00 19.32 ? 194 TRP A O 1 ATOM 1519 C CB . TRP A 1 194 ? 46.070 88.909 16.828 1.00 20.13 ? 194 TRP A CB 1 ATOM 1520 C CG . TRP A 1 194 ? 47.055 88.498 17.852 1.00 20.10 ? 194 TRP A CG 1 ATOM 1521 C CD1 . TRP A 1 194 ? 47.075 88.870 19.161 1.00 19.85 ? 194 TRP A CD1 1 ATOM 1522 C CD2 . TRP A 1 194 ? 48.165 87.616 17.665 1.00 19.99 ? 194 TRP A CD2 1 ATOM 1523 N NE1 . TRP A 1 194 ? 48.131 88.279 19.805 1.00 19.57 ? 194 TRP A NE1 1 ATOM 1524 C CE2 . TRP A 1 194 ? 48.817 87.501 18.913 1.00 20.05 ? 194 TRP A CE2 1 ATOM 1525 C CE3 . TRP A 1 194 ? 48.671 86.904 16.564 1.00 20.56 ? 194 TRP A CE3 1 ATOM 1526 C CZ2 . TRP A 1 194 ? 49.968 86.705 19.095 1.00 20.26 ? 194 TRP A CZ2 1 ATOM 1527 C CZ3 . TRP A 1 194 ? 49.822 86.106 16.744 1.00 20.19 ? 194 TRP A CZ3 1 ATOM 1528 C CH2 . TRP A 1 194 ? 50.446 86.014 18.005 1.00 20.10 ? 194 TRP A CH2 1 ATOM 1529 N N . THR A 1 195 ? 47.933 90.373 14.803 1.00 20.66 ? 195 THR A N 1 ATOM 1530 C CA . THR A 1 195 ? 49.252 90.693 14.265 1.00 21.69 ? 195 THR A CA 1 ATOM 1531 C C . THR A 1 195 ? 49.446 92.201 14.078 1.00 21.64 ? 195 THR A C 1 ATOM 1532 O O . THR A 1 195 ? 50.510 92.730 14.404 1.00 22.35 ? 195 THR A O 1 ATOM 1533 C CB . THR A 1 195 ? 49.494 89.944 12.942 1.00 22.63 ? 195 THR A CB 1 ATOM 1534 O OG1 . THR A 1 195 ? 49.561 88.534 13.221 1.00 24.12 ? 195 THR A OG1 1 ATOM 1535 C CG2 . THR A 1 195 ? 50.783 90.378 12.296 1.00 23.60 ? 195 THR A CG2 1 ATOM 1536 N N . GLN A 1 196 ? 48.441 92.887 13.539 1.00 22.01 ? 196 GLN A N 1 ATOM 1537 C CA . GLN A 1 196 ? 48.559 94.343 13.312 1.00 21.95 ? 196 GLN A CA 1 ATOM 1538 C C . GLN A 1 196 ? 48.623 95.093 14.650 1.00 19.90 ? 196 GLN A C 1 ATOM 1539 O O . GLN A 1 196 ? 49.461 95.978 14.832 1.00 19.71 ? 196 GLN A O 1 ATOM 1540 C CB . GLN A 1 196 ? 47.432 94.851 12.403 1.00 23.08 ? 196 GLN A CB 1 ATOM 1541 C CG . GLN A 1 196 ? 47.326 96.369 12.239 1.00 25.96 ? 196 GLN A CG 1 ATOM 1542 C CD . GLN A 1 196 ? 48.509 97.057 11.542 1.00 27.80 ? 196 GLN A CD 1 ATOM 1543 O OE1 . GLN A 1 196 ? 49.630 96.553 11.505 1.00 28.81 ? 196 GLN A OE1 1 ATOM 1544 N NE2 . GLN A 1 196 ? 48.248 98.247 11.000 1.00 28.95 ? 196 GLN A NE2 1 ATOM 1545 N N . LEU A 1 197 ? 47.772 94.704 15.588 1.00 18.37 ? 197 LEU A N 1 ATOM 1546 C CA . LEU A 1 197 ? 47.798 95.248 16.953 1.00 17.85 ? 197 LEU A CA 1 ATOM 1547 C C . LEU A 1 197 ? 49.122 95.018 17.668 1.00 17.28 ? 197 LEU A C 1 ATOM 1548 O O . LEU A 1 197 ? 49.585 95.886 18.398 1.00 17.20 ? 197 LEU A O 1 ATOM 1549 C CB . LEU A 1 197 ? 46.658 94.656 17.782 1.00 18.08 ? 197 LEU A CB 1 ATOM 1550 C CG . LEU A 1 197 ? 45.239 95.115 17.439 1.00 17.86 ? 197 LEU A CG 1 ATOM 1551 C CD1 . LEU A 1 197 ? 44.208 94.160 18.016 1.00 17.73 ? 197 LEU A CD1 1 ATOM 1552 C CD2 . LEU A 1 197 ? 44.985 96.540 17.931 1.00 18.07 ? 197 LEU A CD2 1 ATOM 1553 N N . SER A 1 198 ? 49.734 93.855 17.446 1.00 17.00 ? 198 SER A N 1 ATOM 1554 C CA . SER A 1 198 ? 51.083 93.573 17.924 1.00 16.68 ? 198 SER A CA 1 ATOM 1555 C C . SER A 1 198 ? 52.105 94.572 17.357 1.00 17.15 ? 198 SER A C 1 ATOM 1556 O O . SER A 1 198 ? 52.868 95.196 18.106 1.00 16.93 ? 198 SER A O 1 ATOM 1557 C CB . SER A 1 198 ? 51.503 92.142 17.543 1.00 16.68 ? 198 SER A CB 1 ATOM 1558 O OG . SER A 1 198 ? 50.729 91.166 18.195 1.00 15.56 ? 198 SER A OG 1 ATOM 1559 N N . LEU A 1 199 ? 52.120 94.715 16.038 1.00 17.76 ? 199 LEU A N 1 ATOM 1560 C CA . LEU A 1 199 ? 53.032 95.647 15.384 1.00 19.23 ? 199 LEU A CA 1 ATOM 1561 C C . LEU A 1 199 ? 52.866 97.084 15.906 1.00 19.83 ? 199 LEU A C 1 ATOM 1562 O O . LEU A 1 199 ? 53.868 97.744 16.229 1.00 20.24 ? 199 LEU A O 1 ATOM 1563 C CB . LEU A 1 199 ? 52.842 95.619 13.857 1.00 20.56 ? 199 LEU A CB 1 ATOM 1564 C CG . LEU A 1 199 ? 53.625 96.624 12.999 1.00 21.59 ? 199 LEU A CG 1 ATOM 1565 C CD1 . LEU A 1 199 ? 55.112 96.485 13.252 1.00 22.55 ? 199 LEU A CD1 1 ATOM 1566 C CD2 . LEU A 1 199 ? 53.332 96.451 11.511 1.00 22.00 ? 199 LEU A CD2 1 ATOM 1567 N N . GLN A 1 200 ? 51.619 97.546 16.009 1.00 19.17 ? 200 GLN A N 1 ATOM 1568 C CA . GLN A 1 200 ? 51.353 98.930 16.398 1.00 20.60 ? 200 GLN A CA 1 ATOM 1569 C C . GLN A 1 200 ? 51.683 99.233 17.849 1.00 20.97 ? 200 GLN A C 1 ATOM 1570 O O . GLN A 1 200 ? 52.249 100.286 18.144 1.00 21.20 ? 200 GLN A O 1 ATOM 1571 C CB . GLN A 1 200 ? 49.902 99.330 16.116 1.00 20.74 ? 200 GLN A CB 1 ATOM 1572 C CG . GLN A 1 200 ? 49.483 99.280 14.661 1.00 21.18 ? 200 GLN A CG 1 ATOM 1573 C CD . GLN A 1 200 ? 50.358 100.128 13.754 1.00 23.13 ? 200 GLN A CD 1 ATOM 1574 O OE1 . GLN A 1 200 ? 50.814 101.199 14.134 1.00 21.61 ? 200 GLN A OE1 1 ATOM 1575 N NE2 . GLN A 1 200 ? 50.596 99.643 12.539 1.00 26.18 ? 200 GLN A NE2 1 ATOM 1576 N N . LEU A 1 201 ? 51.340 98.324 18.752 1.00 21.97 ? 201 LEU A N 1 ATOM 1577 C CA . LEU A 1 201 ? 51.735 98.483 20.154 1.00 23.91 ? 201 LEU A CA 1 ATOM 1578 C C . LEU A 1 201 ? 53.247 98.592 20.305 1.00 24.44 ? 201 LEU A C 1 ATOM 1579 O O . LEU A 1 201 ? 53.729 99.454 21.028 1.00 25.33 ? 201 LEU A O 1 ATOM 1580 C CB . LEU A 1 201 ? 51.241 97.321 21.000 1.00 25.19 ? 201 LEU A CB 1 ATOM 1581 C CG . LEU A 1 201 ? 49.812 97.376 21.511 1.00 27.12 ? 201 LEU A CG 1 ATOM 1582 C CD1 . LEU A 1 201 ? 49.383 95.980 21.942 1.00 27.44 ? 201 LEU A CD1 1 ATOM 1583 C CD2 . LEU A 1 201 ? 49.707 98.349 22.667 1.00 28.12 ? 201 LEU A CD2 1 ATOM 1584 N N . GLN A 1 202 ? 53.986 97.725 19.618 1.00 24.71 ? 202 GLN A N 1 ATOM 1585 C CA . GLN A 1 202 ? 55.448 97.724 19.690 1.00 25.21 ? 202 GLN A CA 1 ATOM 1586 C C . GLN A 1 202 ? 56.088 98.911 18.984 1.00 25.86 ? 202 GLN A C 1 ATOM 1587 O O . GLN A 1 202 ? 57.069 99.461 19.483 1.00 27.60 ? 202 GLN A O 1 ATOM 1588 C CB . GLN A 1 202 ? 56.014 96.405 19.159 1.00 26.01 ? 202 GLN A CB 1 ATOM 1589 C CG . GLN A 1 202 ? 55.659 95.265 20.104 1.00 26.45 ? 202 GLN A CG 1 ATOM 1590 C CD . GLN A 1 202 ? 55.927 93.905 19.524 1.00 25.83 ? 202 GLN A CD 1 ATOM 1591 O OE1 . GLN A 1 202 ? 57.076 93.509 19.322 1.00 25.37 ? 202 GLN A OE1 1 ATOM 1592 N NE2 . GLN A 1 202 ? 54.867 93.200 19.213 1.00 26.84 ? 202 GLN A NE2 1 ATOM 1593 N N . ALA A 1 203 ? 55.541 99.301 17.837 1.00 24.92 ? 203 ALA A N 1 ATOM 1594 C CA . ALA A 1 203 ? 55.968 100.522 17.145 1.00 25.48 ? 203 ALA A CA 1 ATOM 1595 C C . ALA A 1 203 ? 55.698 101.801 17.942 1.00 27.09 ? 203 ALA A C 1 ATOM 1596 O O . ALA A 1 203 ? 56.451 102.760 17.817 1.00 27.16 ? 203 ALA A O 1 ATOM 1597 C CB . ALA A 1 203 ? 55.295 100.628 15.778 1.00 25.59 ? 203 ALA A CB 1 ATOM 1598 N N . SER A 1 204 ? 54.640 101.799 18.760 1.00 28.57 ? 204 SER A N 1 ATOM 1599 C CA . SER A 1 204 ? 54.200 102.984 19.491 1.00 28.84 ? 204 SER A CA 1 ATOM 1600 C C . SER A 1 204 ? 55.137 103.455 20.598 1.00 30.92 ? 204 SER A C 1 ATOM 1601 O O . SER A 1 204 ? 54.981 104.572 21.104 1.00 31.62 ? 204 SER A O 1 ATOM 1602 C CB . SER A 1 204 ? 52.818 102.749 20.087 1.00 29.35 ? 204 SER A CB 1 ATOM 1603 O OG . SER A 1 204 ? 52.880 101.889 21.204 1.00 28.61 ? 204 SER A OG 1 ATOM 1604 N N . GLU A 1 205 ? 56.086 102.610 20.992 1.00 31.71 ? 205 GLU A N 1 ATOM 1605 C CA . GLU A 1 205 ? 57.172 103.009 21.894 1.00 33.83 ? 205 GLU A CA 1 ATOM 1606 C C . GLU A 1 205 ? 57.803 104.367 21.499 1.00 33.26 ? 205 GLU A C 1 ATOM 1607 O O . GLU A 1 205 ? 58.082 105.201 22.360 1.00 34.67 ? 205 GLU A O 1 ATOM 1608 C CB . GLU A 1 205 ? 58.273 101.944 21.891 1.00 35.81 ? 205 GLU A CB 1 ATOM 1609 C CG . GLU A 1 205 ? 57.891 100.584 22.474 1.00 37.32 ? 205 GLU A CG 1 ATOM 1610 C CD . GLU A 1 205 ? 57.744 100.584 23.981 1.00 39.13 ? 205 GLU A CD 1 ATOM 1611 O OE1 . GLU A 1 205 ? 58.183 101.544 24.650 1.00 40.56 ? 205 GLU A OE1 1 ATOM 1612 O OE2 . GLU A 1 205 ? 57.172 99.606 24.503 1.00 40.76 ? 205 GLU A OE2 1 ATOM 1613 N N . SER A 1 206 ? 58.014 104.569 20.200 1.00 31.54 ? 206 SER A N 1 ATOM 1614 C CA . SER A 1 206 ? 58.636 105.784 19.678 1.00 32.08 ? 206 SER A CA 1 ATOM 1615 C C . SER A 1 206 ? 57.698 107.001 19.530 1.00 31.17 ? 206 SER A C 1 ATOM 1616 O O . SER A 1 206 ? 58.173 108.090 19.253 1.00 31.61 ? 206 SER A O 1 ATOM 1617 C CB . SER A 1 206 ? 59.316 105.486 18.328 1.00 32.24 ? 206 SER A CB 1 ATOM 1618 O OG . SER A 1 206 ? 58.402 104.982 17.371 1.00 31.38 ? 206 SER A OG 1 ATOM 1619 N N . LEU A 1 207 ? 56.387 106.826 19.692 1.00 31.14 ? 207 LEU A N 1 ATOM 1620 C CA . LEU A 1 207 ? 55.424 107.929 19.542 1.00 30.30 ? 207 LEU A CA 1 ATOM 1621 C C . LEU A 1 207 ? 54.547 108.088 20.769 1.00 29.36 ? 207 LEU A C 1 ATOM 1622 O O . LEU A 1 207 ? 53.359 108.348 20.640 1.00 29.05 ? 207 LEU A O 1 ATOM 1623 C CB . LEU A 1 207 ? 54.525 107.720 18.317 1.00 29.82 ? 207 LEU A CB 1 ATOM 1624 C CG . LEU A 1 207 ? 55.017 108.112 16.931 1.00 31.60 ? 207 LEU A CG 1 ATOM 1625 C CD1 . LEU A 1 207 ? 53.813 108.121 16.004 1.00 31.76 ? 207 LEU A CD1 1 ATOM 1626 C CD2 . LEU A 1 207 ? 55.723 109.465 16.910 1.00 31.71 ? 207 LEU A CD2 1 ATOM 1627 N N . ASN A 1 208 ? 55.121 107.955 21.958 1.00 29.16 ? 208 ASN A N 1 ATOM 1628 C CA . ASN A 1 208 ? 54.371 108.153 23.198 1.00 28.29 ? 208 ASN A CA 1 ATOM 1629 C C . ASN A 1 208 ? 53.103 107.295 23.303 1.00 26.91 ? 208 ASN A C 1 ATOM 1630 O O . ASN A 1 208 ? 52.079 107.738 23.832 1.00 25.58 ? 208 ASN A O 1 ATOM 1631 C CB . ASN A 1 208 ? 54.037 109.657 23.373 1.00 29.65 ? 208 ASN A CB 1 ATOM 1632 C CG . ASN A 1 208 ? 55.085 110.399 24.174 1.00 31.08 ? 208 ASN A CG 1 ATOM 1633 O OD1 . ASN A 1 208 ? 55.528 109.924 25.217 1.00 30.80 ? 208 ASN A OD1 1 ATOM 1634 N ND2 . ASN A 1 208 ? 55.462 111.590 23.709 1.00 33.40 ? 208 ASN A ND2 1 ATOM 1635 N N . GLY A 1 209 ? 53.181 106.060 22.806 1.00 25.79 ? 209 GLY A N 1 ATOM 1636 C CA . GLY A 1 209 ? 52.046 105.134 22.851 1.00 25.11 ? 209 GLY A CA 1 ATOM 1637 C C . GLY A 1 209 ? 51.007 105.339 21.760 1.00 24.69 ? 209 GLY A C 1 ATOM 1638 O O . GLY A 1 209 ? 49.935 104.739 21.820 1.00 24.91 ? 209 GLY A O 1 ATOM 1639 N N . VAL A 1 210 ? 51.328 106.157 20.754 1.00 23.88 ? 210 VAL A N 1 ATOM 1640 C CA . VAL A 1 210 ? 50.433 106.419 19.629 1.00 23.52 ? 210 VAL A CA 1 ATOM 1641 C C . VAL A 1 210 ? 50.804 105.518 18.452 1.00 22.73 ? 210 VAL A C 1 ATOM 1642 O O . VAL A 1 210 ? 51.974 105.319 18.146 1.00 22.73 ? 210 VAL A O 1 ATOM 1643 C CB . VAL A 1 210 ? 50.473 107.906 19.182 1.00 23.49 ? 210 VAL A CB 1 ATOM 1644 C CG1 . VAL A 1 210 ? 49.505 108.152 18.029 1.00 23.26 ? 210 VAL A CG1 1 ATOM 1645 C CG2 . VAL A 1 210 ? 50.138 108.827 20.342 1.00 23.92 ? 210 VAL A CG2 1 ATOM 1646 N N . PHE A 1 211 ? 49.795 104.998 17.777 1.00 22.42 ? 211 PHE A N 1 ATOM 1647 C CA . PHE A 1 211 ? 50.013 104.028 16.704 1.00 23.51 ? 211 PHE A CA 1 ATOM 1648 C C . PHE A 1 211 ? 50.470 104.702 15.402 1.00 26.57 ? 211 PHE A C 1 ATOM 1649 O O . PHE A 1 211 ? 50.270 105.899 15.196 1.00 28.76 ? 211 PHE A O 1 ATOM 1650 C CB . PHE A 1 211 ? 48.720 103.248 16.442 1.00 22.21 ? 211 PHE A CB 1 ATOM 1651 C CG . PHE A 1 211 ? 48.401 102.189 17.470 1.00 21.81 ? 211 PHE A CG 1 ATOM 1652 C CD1 . PHE A 1 211 ? 49.070 102.096 18.695 1.00 21.96 ? 211 PHE A CD1 1 ATOM 1653 C CD2 . PHE A 1 211 ? 47.413 101.257 17.195 1.00 22.03 ? 211 PHE A CD2 1 ATOM 1654 C CE1 . PHE A 1 211 ? 48.755 101.091 19.598 1.00 22.24 ? 211 PHE A CE1 1 ATOM 1655 C CE2 . PHE A 1 211 ? 47.091 100.260 18.105 1.00 22.21 ? 211 PHE A CE2 1 ATOM 1656 C CZ . PHE A 1 211 ? 47.760 100.183 19.306 1.00 21.86 ? 211 PHE A CZ 1 ATOM 1657 N N . GLY A 1 212 ? 51.094 103.923 14.528 1.00 27.46 ? 212 GLY A N 1 ATOM 1658 C CA . GLY A 1 212 ? 51.305 104.337 13.143 1.00 27.90 ? 212 GLY A CA 1 ATOM 1659 C C . GLY A 1 212 ? 50.014 104.276 12.351 1.00 28.97 ? 212 GLY A C 1 ATOM 1660 O O . GLY A 1 212 ? 49.757 105.137 11.511 1.00 30.12 ? 212 GLY A O 1 ATOM 1661 N N . ASP A 1 213 ? 49.199 103.258 12.621 1.00 29.49 ? 213 ASP A N 1 ATOM 1662 C CA . ASP A 1 213 ? 47.973 103.011 11.885 1.00 31.88 ? 213 ASP A CA 1 ATOM 1663 C C . ASP A 1 213 ? 46.870 102.656 12.844 1.00 30.03 ? 213 ASP A C 1 ATOM 1664 O O . ASP A 1 213 ? 47.092 101.927 13.815 1.00 32.43 ? 213 ASP A O 1 ATOM 1665 C CB . ASP A 1 213 ? 48.164 101.859 10.898 1.00 35.51 ? 213 ASP A CB 1 ATOM 1666 C CG . ASP A 1 213 ? 48.670 102.332 9.553 1.00 40.81 ? 213 ASP A CG 1 ATOM 1667 O OD1 . ASP A 1 213 ? 47.825 102.718 8.704 1.00 45.81 ? 213 ASP A OD1 1 ATOM 1668 O OD2 . ASP A 1 213 ? 49.907 102.325 9.347 1.00 45.06 ? 213 ASP A OD2 1 ATOM 1669 N N . SER A 1 214 ? 45.676 103.154 12.556 1.00 26.71 ? 214 SER A N 1 ATOM 1670 C CA . SER A 1 214 ? 44.515 102.861 13.368 1.00 25.50 ? 214 SER A CA 1 ATOM 1671 C C . SER A 1 214 ? 43.972 101.481 13.018 1.00 23.85 ? 214 SER A C 1 ATOM 1672 O O . SER A 1 214 ? 44.021 101.071 11.866 1.00 22.99 ? 214 SER A O 1 ATOM 1673 C CB . SER A 1 214 ? 43.434 103.916 13.160 1.00 25.30 ? 214 SER A CB 1 ATOM 1674 O OG . SER A 1 214 ? 42.304 103.600 13.949 1.00 26.37 ? 214 SER A OG 1 ATOM 1675 N N . VAL A 1 215 ? 43.444 100.783 14.021 1.00 23.00 ? 215 VAL A N 1 ATOM 1676 C CA . VAL A 1 215 ? 42.867 99.454 13.848 1.00 22.83 ? 215 VAL A CA 1 ATOM 1677 C C . VAL A 1 215 ? 41.409 99.544 14.237 1.00 22.64 ? 215 VAL A C 1 ATOM 1678 O O . VAL A 1 215 ? 41.085 100.145 15.255 1.00 24.23 ? 215 VAL A O 1 ATOM 1679 C CB . VAL A 1 215 ? 43.566 98.430 14.768 1.00 24.19 ? 215 VAL A CB 1 ATOM 1680 C CG1 . VAL A 1 215 ? 42.922 97.051 14.632 1.00 23.96 ? 215 VAL A CG1 1 ATOM 1681 C CG2 . VAL A 1 215 ? 45.067 98.389 14.478 1.00 24.49 ? 215 VAL A CG2 1 ATOM 1682 N N . SER A 1 216 ? 40.526 98.953 13.443 1.00 21.62 ? 216 SER A N 1 ATOM 1683 C CA . SER A 1 216 ? 39.098 98.973 13.753 1.00 21.80 ? 216 SER A CA 1 ATOM 1684 C C . SER A 1 216 ? 38.693 97.718 14.481 1.00 21.12 ? 216 SER A C 1 ATOM 1685 O O . SER A 1 216 ? 38.737 96.638 13.930 1.00 20.24 ? 216 SER A O 1 ATOM 1686 C CB . SER A 1 216 ? 38.252 99.134 12.496 1.00 22.24 ? 216 SER A CB 1 ATOM 1687 O OG . SER A 1 216 ? 38.464 100.426 11.949 1.00 22.87 ? 216 SER A OG 1 ATOM 1688 N N . LEU A 1 217 ? 38.304 97.887 15.735 1.00 21.74 ? 217 LEU A N 1 ATOM 1689 C CA . LEU A 1 217 ? 37.746 96.827 16.543 1.00 21.39 ? 217 LEU A CA 1 ATOM 1690 C C . LEU A 1 217 ? 36.279 97.126 16.794 1.00 21.78 ? 217 LEU A C 1 ATOM 1691 O O . LEU A 1 217 ? 35.944 98.201 17.297 1.00 22.68 ? 217 LEU A O 1 ATOM 1692 C CB . LEU A 1 217 ? 38.491 96.779 17.865 1.00 21.45 ? 217 LEU A CB 1 ATOM 1693 C CG . LEU A 1 217 ? 39.992 96.499 17.763 1.00 21.83 ? 217 LEU A CG 1 ATOM 1694 C CD1 . LEU A 1 217 ? 40.546 96.231 19.154 1.00 22.02 ? 217 LEU A CD1 1 ATOM 1695 C CD2 . LEU A 1 217 ? 40.274 95.316 16.845 1.00 22.41 ? 217 LEU A CD2 1 ATOM 1696 N N . TYR A 1 218 ? 35.407 96.188 16.455 1.00 20.58 ? 218 TYR A N 1 ATOM 1697 C CA . TYR A 1 218 ? 33.987 96.365 16.686 1.00 20.96 ? 218 TYR A CA 1 ATOM 1698 C C . TYR A 1 218 ? 33.592 96.033 18.127 1.00 21.01 ? 218 TYR A C 1 ATOM 1699 O O . TYR A 1 218 ? 34.152 95.137 18.748 1.00 19.30 ? 218 TYR A O 1 ATOM 1700 C CB . TYR A 1 218 ? 33.177 95.526 15.697 1.00 21.09 ? 218 TYR A CB 1 ATOM 1701 C CG . TYR A 1 218 ? 33.226 96.105 14.300 1.00 21.34 ? 218 TYR A CG 1 ATOM 1702 C CD1 . TYR A 1 218 ? 34.352 95.933 13.481 1.00 21.98 ? 218 TYR A CD1 1 ATOM 1703 C CD2 . TYR A 1 218 ? 32.166 96.865 13.818 1.00 21.87 ? 218 TYR A CD2 1 ATOM 1704 C CE1 . TYR A 1 218 ? 34.398 96.477 12.197 1.00 22.17 ? 218 TYR A CE1 1 ATOM 1705 C CE2 . TYR A 1 218 ? 32.197 97.432 12.555 1.00 22.17 ? 218 TYR A CE2 1 ATOM 1706 C CZ . TYR A 1 218 ? 33.304 97.240 11.744 1.00 22.55 ? 218 TYR A CZ 1 ATOM 1707 O OH . TYR A 1 218 ? 33.298 97.818 10.497 1.00 22.97 ? 218 TYR A OH 1 ATOM 1708 N N . ASN A 1 219 ? 32.610 96.761 18.647 1.00 21.58 ? 219 ASN A N 1 ATOM 1709 C CA . ASN A 1 219 ? 32.001 96.412 19.931 1.00 22.76 ? 219 ASN A CA 1 ATOM 1710 C C . ASN A 1 219 ? 30.808 95.483 19.707 1.00 22.74 ? 219 ASN A C 1 ATOM 1711 O O . ASN A 1 219 ? 30.536 95.104 18.567 1.00 20.81 ? 219 ASN A O 1 ATOM 1712 C CB . ASN A 1 219 ? 31.626 97.680 20.713 1.00 23.57 ? 219 ASN A CB 1 ATOM 1713 C CG . ASN A 1 219 ? 30.502 98.476 20.069 1.00 24.51 ? 219 ASN A CG 1 ATOM 1714 O OD1 . ASN A 1 219 ? 29.803 98.010 19.156 1.00 24.21 ? 219 ASN A OD1 1 ATOM 1715 N ND2 . ASN A 1 219 ? 30.311 99.690 20.563 1.00 25.25 ? 219 ASN A ND2 1 ATOM 1716 N N . SER A 1 220 ? 30.093 95.130 20.774 1.00 23.84 ? 220 SER A N 1 ATOM 1717 C CA . SER A 1 220 ? 28.973 94.175 20.662 1.00 27.23 ? 220 SER A CA 1 ATOM 1718 C C . SER A 1 220 ? 27.697 94.772 20.022 1.00 28.67 ? 220 SER A C 1 ATOM 1719 O O . SER A 1 220 ? 26.766 94.032 19.703 1.00 30.73 ? 220 SER A O 1 ATOM 1720 C CB . SER A 1 220 ? 28.652 93.532 22.021 1.00 27.58 ? 220 SER A CB 1 ATOM 1721 O OG . SER A 1 220 ? 29.719 92.705 22.446 1.00 28.68 ? 220 SER A OG 1 ATOM 1722 N N . MET A 1 221 ? 27.672 96.089 19.827 1.00 30.06 ? 221 MET A N 1 ATOM 1723 C CA . MET A 1 221 ? 26.615 96.772 19.074 1.00 31.84 ? 221 MET A CA 1 ATOM 1724 C C . MET A 1 221 ? 26.962 96.924 17.593 1.00 30.34 ? 221 MET A C 1 ATOM 1725 O O . MET A 1 221 ? 26.304 97.689 16.890 1.00 29.28 ? 221 MET A O 1 ATOM 1726 C CB . MET A 1 221 ? 26.388 98.167 19.660 1.00 34.51 ? 221 MET A CB 1 ATOM 1727 C CG . MET A 1 221 ? 26.100 98.205 21.155 1.00 37.85 ? 221 MET A CG 1 ATOM 1728 S SD . MET A 1 221 ? 24.368 97.908 21.551 1.00 46.30 ? 221 MET A SD 1 ATOM 1729 C CE . MET A 1 221 ? 24.186 96.135 21.283 1.00 44.85 ? 221 MET A CE 1 ATOM 1730 N N . ASP A 1 222 ? 28.000 96.217 17.126 1.00 28.74 ? 222 ASP A N 1 ATOM 1731 C CA . ASP A 1 222 ? 28.505 96.334 15.762 1.00 27.26 ? 222 ASP A CA 1 ATOM 1732 C C . ASP A 1 222 ? 28.952 97.745 15.359 1.00 25.69 ? 222 ASP A C 1 ATOM 1733 O O . ASP A 1 222 ? 28.937 98.066 14.178 1.00 24.63 ? 222 ASP A O 1 ATOM 1734 C CB . ASP A 1 222 ? 27.477 95.759 14.770 1.00 27.97 ? 222 ASP A CB 1 ATOM 1735 C CG . ASP A 1 222 ? 27.230 94.267 14.986 1.00 30.63 ? 222 ASP A CG 1 ATOM 1736 O OD1 . ASP A 1 222 ? 28.203 93.509 15.193 1.00 31.24 ? 222 ASP A OD1 1 ATOM 1737 O OD2 . ASP A 1 222 ? 26.059 93.832 14.952 1.00 34.15 ? 222 ASP A OD2 1 ATOM 1738 N N . GLU A 1 223 ? 29.371 98.569 16.327 1.00 25.13 ? 223 GLU A N 1 ATOM 1739 C CA . GLU A 1 223 ? 29.988 99.877 16.053 1.00 26.27 ? 223 GLU A CA 1 ATOM 1740 C C . GLU A 1 223 ? 31.492 99.699 15.968 1.00 24.63 ? 223 GLU A C 1 ATOM 1741 O O . GLU A 1 223 ? 32.091 99.063 16.839 1.00 23.11 ? 223 GLU A O 1 ATOM 1742 C CB . GLU A 1 223 ? 29.764 100.902 17.165 1.00 28.57 ? 223 GLU A CB 1 ATOM 1743 C CG . GLU A 1 223 ? 28.332 101.226 17.541 1.00 33.27 ? 223 GLU A CG 1 ATOM 1744 C CD . GLU A 1 223 ? 28.251 101.887 18.928 1.00 37.44 ? 223 GLU A CD 1 ATOM 1745 O OE1 . GLU A 1 223 ? 28.760 103.022 19.086 1.00 41.41 ? 223 GLU A OE1 1 ATOM 1746 O OE2 . GLU A 1 223 ? 27.703 101.262 19.873 1.00 39.64 ? 223 GLU A OE2 1 ATOM 1747 N N . PRO A 1 224 ? 32.123 100.308 14.960 1.00 23.87 ? 224 PRO A N 1 ATOM 1748 C CA . PRO A 1 224 ? 33.586 100.259 14.879 1.00 23.89 ? 224 PRO A CA 1 ATOM 1749 C C . PRO A 1 224 ? 34.235 101.244 15.843 1.00 23.11 ? 224 PRO A C 1 ATOM 1750 O O . PRO A 1 224 ? 33.816 102.398 15.917 1.00 23.16 ? 224 PRO A O 1 ATOM 1751 C CB . PRO A 1 224 ? 33.865 100.659 13.426 1.00 24.33 ? 224 PRO A CB 1 ATOM 1752 C CG . PRO A 1 224 ? 32.704 101.519 13.040 1.00 23.90 ? 224 PRO A CG 1 ATOM 1753 C CD . PRO A 1 224 ? 31.525 101.079 13.854 1.00 23.90 ? 224 PRO A CD 1 ATOM 1754 N N . ILE A 1 225 ? 35.231 100.788 16.585 1.00 21.73 ? 225 ILE A N 1 ATOM 1755 C CA . ILE A 1 225 ? 36.003 101.660 17.430 1.00 21.93 ? 225 ILE A CA 1 ATOM 1756 C C . ILE A 1 225 ? 37.415 101.689 16.889 1.00 21.94 ? 225 ILE A C 1 ATOM 1757 O O . ILE A 1 225 ? 38.070 100.655 16.767 1.00 21.57 ? 225 ILE A O 1 ATOM 1758 C CB . ILE A 1 225 ? 35.974 101.220 18.905 1.00 22.81 ? 225 ILE A CB 1 ATOM 1759 C CG1 . ILE A 1 225 ? 34.536 101.263 19.425 1.00 23.66 ? 225 ILE A CG1 1 ATOM 1760 C CG2 . ILE A 1 225 ? 36.872 102.128 19.748 1.00 22.97 ? 225 ILE A CG2 1 ATOM 1761 C CD1 . ILE A 1 225 ? 34.334 100.550 20.746 1.00 25.11 ? 225 ILE A CD1 1 ATOM 1762 N N . GLY A 1 226 ? 37.869 102.890 16.547 1.00 21.39 ? 226 GLY A N 1 ATOM 1763 C CA . GLY A 1 226 ? 39.190 103.091 16.020 1.00 21.18 ? 226 GLY A CA 1 ATOM 1764 C C . GLY A 1 226 ? 40.143 103.116 17.179 1.00 21.71 ? 226 GLY A C 1 ATOM 1765 O O . GLY A 1 226 ? 40.032 103.991 18.035 1.00 22.97 ? 226 GLY A O 1 ATOM 1766 N N . VAL A 1 227 ? 41.040 102.130 17.221 1.00 21.47 ? 227 VAL A N 1 ATOM 1767 C CA . VAL A 1 227 ? 42.092 102.052 18.210 1.00 20.64 ? 227 VAL A CA 1 ATOM 1768 C C . VAL A 1 227 ? 43.361 102.489 17.515 1.00 21.13 ? 227 VAL A C 1 ATOM 1769 O O . VAL A 1 227 ? 43.944 101.739 16.739 1.00 21.82 ? 227 VAL A O 1 ATOM 1770 C CB . VAL A 1 227 ? 42.235 100.624 18.768 1.00 20.69 ? 227 VAL A CB 1 ATOM 1771 C CG1 . VAL A 1 227 ? 43.398 100.533 19.757 1.00 20.54 ? 227 VAL A CG1 1 ATOM 1772 C CG2 . VAL A 1 227 ? 40.929 100.192 19.417 1.00 20.57 ? 227 VAL A CG2 1 ATOM 1773 N N . ASP A 1 228 ? 43.782 103.715 17.799 1.00 22.07 ? 228 ASP A N 1 ATOM 1774 C CA . ASP A 1 228 ? 45.011 104.280 17.248 1.00 22.04 ? 228 ASP A CA 1 ATOM 1775 C C . ASP A 1 228 ? 46.030 104.594 18.332 1.00 20.77 ? 228 ASP A C 1 ATOM 1776 O O . ASP A 1 228 ? 46.940 105.403 18.135 1.00 20.96 ? 228 ASP A O 1 ATOM 1777 C CB . ASP A 1 228 ? 44.682 105.537 16.433 1.00 24.27 ? 228 ASP A CB 1 ATOM 1778 C CG . ASP A 1 228 ? 44.008 106.631 17.265 1.00 25.34 ? 228 ASP A CG 1 ATOM 1779 O OD1 . ASP A 1 228 ? 43.393 106.326 18.321 1.00 24.46 ? 228 ASP A OD1 1 ATOM 1780 O OD2 . ASP A 1 228 ? 44.078 107.804 16.832 1.00 26.99 ? 228 ASP A OD2 1 ATOM 1781 N N . SER A 1 229 ? 45.893 103.955 19.481 1.00 19.66 ? 229 SER A N 1 ATOM 1782 C CA . SER A 1 229 ? 46.866 104.115 20.537 1.00 19.54 ? 229 SER A CA 1 ATOM 1783 C C . SER A 1 229 ? 46.688 103.010 21.555 1.00 20.62 ? 229 SER A C 1 ATOM 1784 O O . SER A 1 229 ? 45.701 102.278 21.527 1.00 20.01 ? 229 SER A O 1 ATOM 1785 C CB . SER A 1 229 ? 46.678 105.455 21.242 1.00 18.81 ? 229 SER A CB 1 ATOM 1786 O OG . SER A 1 229 ? 45.491 105.438 22.011 1.00 18.43 ? 229 SER A OG 1 ATOM 1787 N N . MET A 1 230 ? 47.630 102.946 22.484 1.00 22.33 ? 230 MET A N 1 ATOM 1788 C CA . MET A 1 230 ? 47.562 102.016 23.605 1.00 24.91 ? 230 MET A CA 1 ATOM 1789 C C . MET A 1 230 ? 46.602 102.470 24.710 1.00 24.96 ? 230 MET A C 1 ATOM 1790 O O . MET A 1 230 ? 46.545 101.819 25.747 1.00 25.27 ? 230 MET A O 1 ATOM 1791 C CB . MET A 1 230 ? 48.967 101.813 24.215 1.00 27.34 ? 230 MET A CB 1 ATOM 1792 C CG . MET A 1 230 ? 49.519 103.035 24.961 1.00 29.20 ? 230 MET A CG 1 ATOM 1793 S SD . MET A 1 230 ? 51.025 102.769 25.898 1.00 32.25 ? 230 MET A SD 1 ATOM 1794 C CE . MET A 1 230 ? 50.366 101.839 27.281 1.00 32.61 ? 230 MET A CE 1 ATOM 1795 N N . TYR A 1 231 ? 45.871 103.580 24.538 1.00 24.20 ? 231 TYR A N 1 ATOM 1796 C CA . TYR A 1 231 ? 45.086 104.130 25.641 1.00 22.94 ? 231 TYR A CA 1 ATOM 1797 C C . TYR A 1 231 ? 43.630 103.691 25.567 1.00 24.24 ? 231 TYR A C 1 ATOM 1798 O O . TYR A 1 231 ? 42.739 104.423 25.984 1.00 26.55 ? 231 TYR A O 1 ATOM 1799 C CB . TYR A 1 231 ? 45.252 105.664 25.693 1.00 23.11 ? 231 TYR A CB 1 ATOM 1800 C CG . TYR A 1 231 ? 46.712 106.007 25.775 1.00 21.39 ? 231 TYR A CG 1 ATOM 1801 C CD1 . TYR A 1 231 ? 47.425 105.767 26.937 1.00 21.31 ? 231 TYR A CD1 1 ATOM 1802 C CD2 . TYR A 1 231 ? 47.396 106.465 24.666 1.00 20.58 ? 231 TYR A CD2 1 ATOM 1803 C CE1 . TYR A 1 231 ? 48.776 106.012 27.007 1.00 21.09 ? 231 TYR A CE1 1 ATOM 1804 C CE2 . TYR A 1 231 ? 48.739 106.721 24.725 1.00 21.59 ? 231 TYR A CE2 1 ATOM 1805 C CZ . TYR A 1 231 ? 49.430 106.490 25.899 1.00 21.49 ? 231 TYR A CZ 1 ATOM 1806 O OH . TYR A 1 231 ? 50.780 106.735 25.938 1.00 22.64 ? 231 TYR A OH 1 ATOM 1807 N N . TYR A 1 232 ? 43.390 102.478 25.071 1.00 23.90 ? 232 TYR A N 1 ATOM 1808 C CA . TYR A 1 232 ? 42.046 101.938 24.954 1.00 23.56 ? 232 TYR A CA 1 ATOM 1809 C C . TYR A 1 232 ? 41.962 100.677 25.800 1.00 23.50 ? 232 TYR A C 1 ATOM 1810 O O . TYR A 1 232 ? 42.671 99.726 25.531 1.00 23.62 ? 232 TYR A O 1 ATOM 1811 C CB . TYR A 1 232 ? 41.715 101.641 23.485 1.00 23.78 ? 232 TYR A CB 1 ATOM 1812 C CG . TYR A 1 232 ? 41.470 102.905 22.686 1.00 23.01 ? 232 TYR A CG 1 ATOM 1813 C CD1 . TYR A 1 232 ? 42.529 103.573 22.066 1.00 22.78 ? 232 TYR A CD1 1 ATOM 1814 C CD2 . TYR A 1 232 ? 40.192 103.447 22.573 1.00 22.04 ? 232 TYR A CD2 1 ATOM 1815 C CE1 . TYR A 1 232 ? 42.323 104.752 21.355 1.00 23.67 ? 232 TYR A CE1 1 ATOM 1816 C CE2 . TYR A 1 232 ? 39.971 104.625 21.853 1.00 23.34 ? 232 TYR A CE2 1 ATOM 1817 C CZ . TYR A 1 232 ? 41.040 105.274 21.246 1.00 23.26 ? 232 TYR A CZ 1 ATOM 1818 O OH . TYR A 1 232 ? 40.847 106.434 20.529 1.00 24.94 ? 232 TYR A OH 1 ATOM 1819 N N . PRO A 1 233 ? 41.097 100.667 26.830 1.00 24.20 ? 233 PRO A N 1 ATOM 1820 C CA . PRO A 1 233 ? 40.885 99.458 27.651 1.00 24.13 ? 233 PRO A CA 1 ATOM 1821 C C . PRO A 1 233 ? 40.425 98.225 26.890 1.00 23.90 ? 233 PRO A C 1 ATOM 1822 O O . PRO A 1 233 ? 40.740 97.109 27.305 1.00 25.12 ? 233 PRO A O 1 ATOM 1823 C CB . PRO A 1 233 ? 39.796 99.893 28.632 1.00 23.78 ? 233 PRO A CB 1 ATOM 1824 C CG . PRO A 1 233 ? 39.960 101.360 28.741 1.00 23.95 ? 233 PRO A CG 1 ATOM 1825 C CD . PRO A 1 233 ? 40.352 101.821 27.372 1.00 23.52 ? 233 PRO A CD 1 ATOM 1826 N N . ILE A 1 234 ? 39.702 98.422 25.790 1.00 23.44 ? 234 ILE A N 1 ATOM 1827 C CA . ILE A 1 234 ? 39.283 97.318 24.941 1.00 23.50 ? 234 ILE A CA 1 ATOM 1828 C C . ILE A 1 234 ? 40.422 96.633 24.211 1.00 23.14 ? 234 ILE A C 1 ATOM 1829 O O . ILE A 1 234 ? 40.218 95.558 23.671 1.00 23.18 ? 234 ILE A O 1 ATOM 1830 C CB . ILE A 1 234 ? 38.238 97.729 23.888 1.00 24.87 ? 234 ILE A CB 1 ATOM 1831 C CG1 . ILE A 1 234 ? 38.846 98.639 22.812 1.00 25.38 ? 234 ILE A CG1 1 ATOM 1832 C CG2 . ILE A 1 234 ? 37.025 98.352 24.574 1.00 24.94 ? 234 ILE A CG2 1 ATOM 1833 C CD1 . ILE A 1 234 ? 37.960 98.777 21.599 1.00 26.96 ? 234 ILE A CD1 1 ATOM 1834 N N . LEU A 1 235 ? 41.577 97.290 24.132 1.00 22.92 ? 235 LEU A N 1 ATOM 1835 C CA . LEU A 1 235 ? 42.825 96.659 23.714 1.00 23.35 ? 235 LEU A CA 1 ATOM 1836 C C . LEU A 1 235 ? 43.664 96.214 24.913 1.00 23.51 ? 235 LEU A C 1 ATOM 1837 O O . LEU A 1 235 ? 43.924 95.025 25.077 1.00 23.46 ? 235 LEU A O 1 ATOM 1838 C CB . LEU A 1 235 ? 43.664 97.617 22.855 1.00 23.17 ? 235 LEU A CB 1 ATOM 1839 C CG . LEU A 1 235 ? 45.071 97.117 22.495 1.00 23.03 ? 235 LEU A CG 1 ATOM 1840 C CD1 . LEU A 1 235 ? 44.995 95.793 21.739 1.00 23.10 ? 235 LEU A CD1 1 ATOM 1841 C CD2 . LEU A 1 235 ? 45.837 98.166 21.718 1.00 22.26 ? 235 LEU A CD2 1 ATOM 1842 N N . THR A 1 236 ? 44.105 97.156 25.741 1.00 23.70 ? 236 THR A N 1 ATOM 1843 C CA . THR A 1 236 ? 45.153 96.844 26.709 1.00 24.73 ? 236 THR A CA 1 ATOM 1844 C C . THR A 1 236 ? 44.734 95.999 27.899 1.00 23.85 ? 236 THR A C 1 ATOM 1845 O O . THR A 1 236 ? 45.593 95.369 28.497 1.00 24.15 ? 236 THR A O 1 ATOM 1846 C CB . THR A 1 236 ? 45.900 98.084 27.208 1.00 27.29 ? 236 THR A CB 1 ATOM 1847 O OG1 . THR A 1 236 ? 45.014 98.910 27.963 1.00 31.36 ? 236 THR A OG1 1 ATOM 1848 C CG2 . THR A 1 236 ? 46.487 98.843 26.035 1.00 27.44 ? 236 THR A CG2 1 ATOM 1849 N N . ALA A 1 237 ? 43.445 95.962 28.236 1.00 23.32 ? 237 ALA A N 1 ATOM 1850 C CA . ALA A 1 237 ? 42.922 94.959 29.177 1.00 23.87 ? 237 ALA A CA 1 ATOM 1851 C C . ALA A 1 237 ? 42.265 93.771 28.465 1.00 24.60 ? 237 ALA A C 1 ATOM 1852 O O . ALA A 1 237 ? 41.511 93.048 29.078 1.00 28.53 ? 237 ALA A O 1 ATOM 1853 C CB . ALA A 1 237 ? 41.928 95.591 30.136 1.00 23.65 ? 237 ALA A CB 1 ATOM 1854 N N . ASN A 1 238 ? 42.552 93.569 27.183 1.00 24.17 ? 238 ASN A N 1 ATOM 1855 C CA . ASN A 1 238 ? 41.933 92.528 26.381 1.00 22.87 ? 238 ASN A CA 1 ATOM 1856 C C . ASN A 1 238 ? 42.991 91.563 25.802 1.00 22.74 ? 238 ASN A C 1 ATOM 1857 O O . ASN A 1 238 ? 42.951 90.362 26.081 1.00 21.10 ? 238 ASN A O 1 ATOM 1858 C CB . ASN A 1 238 ? 41.146 93.222 25.281 1.00 22.43 ? 238 ASN A CB 1 ATOM 1859 C CG . ASN A 1 238 ? 40.328 92.283 24.436 1.00 22.28 ? 238 ASN A CG 1 ATOM 1860 O OD1 . ASN A 1 238 ? 40.282 91.063 24.650 1.00 21.16 ? 238 ASN A OD1 1 ATOM 1861 N ND2 . ASN A 1 238 ? 39.665 92.860 23.448 1.00 21.64 ? 238 ASN A ND2 1 ATOM 1862 N N . MET A 1 239 ? 43.911 92.102 24.996 1.00 22.43 ? 239 MET A N 1 ATOM 1863 C CA . MET A 1 239 ? 44.967 91.327 24.345 1.00 23.46 ? 239 MET A CA 1 ATOM 1864 C C . MET A 1 239 ? 45.983 90.850 25.386 1.00 22.02 ? 239 MET A C 1 ATOM 1865 O O . MET A 1 239 ? 46.716 91.649 25.951 1.00 20.90 ? 239 MET A O 1 ATOM 1866 C CB . MET A 1 239 ? 45.675 92.169 23.268 1.00 25.29 ? 239 MET A CB 1 ATOM 1867 C CG . MET A 1 239 ? 46.902 91.526 22.608 1.00 27.78 ? 239 MET A CG 1 ATOM 1868 S SD . MET A 1 239 ? 47.605 92.463 21.211 1.00 30.73 ? 239 MET A SD 1 ATOM 1869 C CE . MET A 1 239 ? 46.300 92.251 20.041 1.00 30.27 ? 239 MET A CE 1 ATOM 1870 N N . ALA A 1 240 ? 46.045 89.541 25.577 1.00 21.14 ? 240 ALA A N 1 ATOM 1871 C CA . ALA A 1 240 ? 46.827 88.928 26.650 1.00 20.36 ? 240 ALA A CA 1 ATOM 1872 C C . ALA A 1 240 ? 48.306 88.845 26.316 1.00 19.35 ? 240 ALA A C 1 ATOM 1873 O O . ALA A 1 240 ? 49.149 88.890 27.208 1.00 19.52 ? 240 ALA A O 1 ATOM 1874 C CB . ALA A 1 240 ? 46.289 87.545 26.938 1.00 20.09 ? 240 ALA A CB 1 ATOM 1875 N N . PHE A 1 241 ? 48.616 88.704 25.030 1.00 18.21 ? 241 PHE A N 1 ATOM 1876 C CA . PHE A 1 241 ? 49.991 88.701 24.571 1.00 17.72 ? 241 PHE A CA 1 ATOM 1877 C C . PHE A 1 241 ? 50.076 89.078 23.096 1.00 18.12 ? 241 PHE A C 1 ATOM 1878 O O . PHE A 1 241 ? 49.063 89.053 22.389 1.00 17.47 ? 241 PHE A O 1 ATOM 1879 C CB . PHE A 1 241 ? 50.667 87.334 24.837 1.00 17.18 ? 241 PHE A CB 1 ATOM 1880 C CG . PHE A 1 241 ? 49.934 86.166 24.256 1.00 16.35 ? 241 PHE A CG 1 ATOM 1881 C CD1 . PHE A 1 241 ? 50.062 85.843 22.914 1.00 16.41 ? 241 PHE A CD1 1 ATOM 1882 C CD2 . PHE A 1 241 ? 49.127 85.371 25.054 1.00 16.57 ? 241 PHE A CD2 1 ATOM 1883 C CE1 . PHE A 1 241 ? 49.374 84.761 22.379 1.00 16.19 ? 241 PHE A CE1 1 ATOM 1884 C CE2 . PHE A 1 241 ? 48.450 84.284 24.531 1.00 16.12 ? 241 PHE A CE2 1 ATOM 1885 C CZ . PHE A 1 241 ? 48.568 83.986 23.184 1.00 15.99 ? 241 PHE A CZ 1 ATOM 1886 N N . GLN A 1 242 ? 51.290 89.414 22.652 1.00 18.47 ? 242 GLN A N 1 ATOM 1887 C CA . GLN A 1 242 ? 51.537 89.882 21.283 1.00 18.70 ? 242 GLN A CA 1 ATOM 1888 C C . GLN A 1 242 ? 52.524 89.011 20.539 1.00 18.71 ? 242 GLN A C 1 ATOM 1889 O O . GLN A 1 242 ? 53.418 88.437 21.139 1.00 19.17 ? 242 GLN A O 1 ATOM 1890 C CB . GLN A 1 242 ? 52.149 91.292 21.289 1.00 19.28 ? 242 GLN A CB 1 ATOM 1891 C CG . GLN A 1 242 ? 51.716 92.256 22.373 1.00 19.18 ? 242 GLN A CG 1 ATOM 1892 C CD . GLN A 1 242 ? 52.495 93.580 22.340 1.00 19.39 ? 242 GLN A CD 1 ATOM 1893 O OE1 . GLN A 1 242 ? 52.700 94.171 21.263 1.00 20.34 ? 242 GLN A OE1 1 ATOM 1894 N NE2 . GLN A 1 242 ? 52.938 94.048 23.501 1.00 18.02 ? 242 GLN A NE2 1 ATOM 1895 N N . LEU A 1 243 ? 52.375 88.971 19.218 1.00 20.18 ? 243 LEU A N 1 ATOM 1896 C CA . LEU A 1 243 ? 53.408 88.502 18.296 1.00 20.73 ? 243 LEU A CA 1 ATOM 1897 C C . LEU A 1 243 ? 54.633 89.418 18.317 1.00 21.81 ? 243 LEU A C 1 ATOM 1898 O O . LEU A 1 243 ? 54.484 90.641 18.263 1.00 20.91 ? 243 LEU A O 1 ATOM 1899 C CB . LEU A 1 243 ? 52.848 88.491 16.870 1.00 21.04 ? 243 LEU A CB 1 ATOM 1900 C CG . LEU A 1 243 ? 53.708 87.837 15.783 1.00 21.65 ? 243 LEU A CG 1 ATOM 1901 C CD1 . LEU A 1 243 ? 53.641 86.327 15.911 1.00 21.61 ? 243 LEU A CD1 1 ATOM 1902 C CD2 . LEU A 1 243 ? 53.278 88.283 14.382 1.00 21.63 ? 243 LEU A CD2 1 ATOM 1903 N N . TYR A 1 244 ? 55.842 88.848 18.355 1.00 22.43 ? 244 TYR A N 1 ATOM 1904 C CA . TYR A 1 244 ? 57.042 89.673 18.246 1.00 24.11 ? 244 TYR A CA 1 ATOM 1905 C C . TYR A 1 244 ? 57.071 90.314 16.864 1.00 24.90 ? 244 TYR A C 1 ATOM 1906 O O . TYR A 1 244 ? 56.746 89.667 15.874 1.00 23.20 ? 244 TYR A O 1 ATOM 1907 C CB . TYR A 1 244 ? 58.328 88.879 18.488 1.00 25.60 ? 244 TYR A CB 1 ATOM 1908 C CG . TYR A 1 244 ? 59.589 89.688 18.219 1.00 27.30 ? 244 TYR A CG 1 ATOM 1909 C CD1 . TYR A 1 244 ? 60.131 90.519 19.204 1.00 28.28 ? 244 TYR A CD1 1 ATOM 1910 C CD2 . TYR A 1 244 ? 60.220 89.650 16.970 1.00 27.68 ? 244 TYR A CD2 1 ATOM 1911 C CE1 . TYR A 1 244 ? 61.272 91.271 18.962 1.00 29.11 ? 244 TYR A CE1 1 ATOM 1912 C CE2 . TYR A 1 244 ? 61.359 90.400 16.719 1.00 28.87 ? 244 TYR A CE2 1 ATOM 1913 C CZ . TYR A 1 244 ? 61.880 91.201 17.721 1.00 29.46 ? 244 TYR A CZ 1 ATOM 1914 O OH . TYR A 1 244 ? 63.003 91.943 17.487 1.00 31.95 ? 244 TYR A OH 1 ATOM 1915 N N . GLN A 1 245 ? 57.471 91.584 16.813 1.00 26.07 ? 245 GLN A N 1 ATOM 1916 C CA . GLN A 1 245 ? 57.415 92.391 15.583 1.00 27.85 ? 245 GLN A CA 1 ATOM 1917 C C . GLN A 1 245 ? 58.593 93.344 15.438 1.00 29.66 ? 245 GLN A C 1 ATOM 1918 O O . GLN A 1 245 ? 59.199 93.389 14.387 1.00 30.07 ? 245 GLN A O 1 ATOM 1919 C CB . GLN A 1 245 ? 56.125 93.205 15.519 1.00 27.95 ? 245 GLN A CB 1 ATOM 1920 C CG . GLN A 1 245 ? 54.858 92.408 15.279 1.00 28.23 ? 245 GLN A CG 1 ATOM 1921 C CD . GLN A 1 245 ? 54.655 92.027 13.829 1.00 29.01 ? 245 GLN A CD 1 ATOM 1922 O OE1 . GLN A 1 245 ? 55.600 91.756 13.112 1.00 31.52 ? 245 GLN A OE1 1 ATOM 1923 N NE2 . GLN A 1 245 ? 53.411 92.004 13.395 1.00 30.23 ? 245 GLN A NE2 1 ATOM 1924 N N . CYS A 1 246 ? 58.885 94.118 16.479 1.00 33.87 ? 246 CYS A N 1 ATOM 1925 C CA . CYS A 1 246 ? 59.869 95.200 16.441 1.00 37.55 ? 246 CYS A CA 1 ATOM 1926 C C . CYS A 1 246 ? 60.912 95.061 17.544 1.00 38.72 ? 246 CYS A C 1 ATOM 1927 O O . CYS A 1 246 ? 60.575 94.681 18.663 1.00 41.62 ? 246 CYS A O 1 ATOM 1928 C CB . CYS A 1 246 ? 59.153 96.538 16.641 1.00 38.95 ? 246 CYS A CB 1 ATOM 1929 S SG . CYS A 1 246 ? 57.844 96.863 15.439 1.00 42.19 ? 246 CYS A SG 1 ATOM 1930 N N . PRO A 1 247 ? 62.179 95.385 17.243 1.00 40.07 ? 247 PRO A N 1 ATOM 1931 C CA . PRO A 1 247 ? 63.135 95.605 18.332 1.00 40.68 ? 247 PRO A CA 1 ATOM 1932 C C . PRO A 1 247 ? 62.902 96.938 19.051 1.00 41.03 ? 247 PRO A C 1 ATOM 1933 O O . PRO A 1 247 ? 63.060 97.008 20.273 1.00 44.42 ? 247 PRO A O 1 ATOM 1934 C CB . PRO A 1 247 ? 64.489 95.595 17.619 1.00 40.98 ? 247 PRO A CB 1 ATOM 1935 C CG . PRO A 1 247 ? 64.194 95.955 16.207 1.00 39.74 ? 247 PRO A CG 1 ATOM 1936 C CD . PRO A 1 247 ? 62.816 95.455 15.913 1.00 39.35 ? 247 PRO A CD 1 ATOM 1937 N N . ASN B 2 1 ? 62.083 97.211 8.274 1.00 73.78 ? 1 ASN B N 1 ATOM 1938 C CA . ASN B 2 1 ? 60.626 97.461 8.502 1.00 71.36 ? 1 ASN B CA 1 ATOM 1939 C C . ASN B 2 1 ? 60.369 98.891 9.010 1.00 68.08 ? 1 ASN B C 1 ATOM 1940 O O . ASN B 2 1 ? 60.324 99.131 10.223 1.00 69.34 ? 1 ASN B O 1 ATOM 1941 C CB . ASN B 2 1 ? 60.056 96.401 9.472 1.00 70.72 ? 1 ASN B CB 1 ATOM 1942 C CG . ASN B 2 1 ? 58.530 96.309 9.438 1.00 72.21 ? 1 ASN B CG 1 ATOM 1943 O OD1 . ASN B 2 1 ? 57.856 96.956 8.631 1.00 72.77 ? 1 ASN B OD1 1 ATOM 1944 N ND2 . ASN B 2 1 ? 57.980 95.478 10.315 1.00 71.68 ? 1 ASN B ND2 1 ATOM 1945 N N . GLU B 2 2 ? 60.201 99.830 8.069 1.00 64.78 ? 2 GLU B N 1 ATOM 1946 C CA . GLU B 2 2 ? 59.874 101.242 8.377 1.00 58.80 ? 2 GLU B CA 1 ATOM 1947 C C . GLU B 2 2 ? 58.630 101.406 9.274 1.00 55.35 ? 2 GLU B C 1 ATOM 1948 O O . GLU B 2 2 ? 58.527 102.384 10.017 1.00 52.99 ? 2 GLU B O 1 ATOM 1949 C CB . GLU B 2 2 ? 59.693 102.054 7.085 1.00 56.19 ? 2 GLU B CB 1 ATOM 1950 N N . GLN B 2 3 ? 57.703 100.444 9.215 1.00 51.01 ? 3 GLN B N 1 ATOM 1951 C CA . GLN B 2 3 ? 56.521 100.431 10.086 1.00 46.99 ? 3 GLN B CA 1 ATOM 1952 C C . GLN B 2 3 ? 56.803 100.374 11.584 1.00 43.96 ? 3 GLN B C 1 ATOM 1953 O O . GLN B 2 3 ? 55.964 100.808 12.372 1.00 43.98 ? 3 GLN B O 1 ATOM 1954 C CB . GLN B 2 3 ? 55.614 99.268 9.737 1.00 48.34 ? 3 GLN B CB 1 ATOM 1955 C CG . GLN B 2 3 ? 54.881 99.437 8.430 1.00 50.83 ? 3 GLN B CG 1 ATOM 1956 C CD . GLN B 2 3 ? 53.857 98.343 8.247 1.00 53.02 ? 3 GLN B CD 1 ATOM 1957 O OE1 . GLN B 2 3 ? 54.212 97.178 8.032 1.00 55.03 ? 3 GLN B OE1 1 ATOM 1958 N NE2 . GLN B 2 3 ? 52.580 98.700 8.365 1.00 52.72 ? 3 GLN B NE2 1 ATOM 1959 N N . CYS B 2 4 ? 57.959 99.846 11.982 1.00 41.31 ? 4 CYS B N 1 ATOM 1960 C CA . CYS B 2 4 ? 58.360 99.862 13.402 1.00 41.72 ? 4 CYS B CA 1 ATOM 1961 C C . CYS B 2 4 ? 58.781 101.244 13.916 1.00 38.87 ? 4 CYS B C 1 ATOM 1962 O O . CYS B 2 4 ? 58.907 101.433 15.128 1.00 36.26 ? 4 CYS B O 1 ATOM 1963 C CB . CYS B 2 4 ? 59.461 98.822 13.679 1.00 42.49 ? 4 CYS B CB 1 ATOM 1964 S SG . CYS B 2 4 ? 58.856 97.107 13.641 1.00 47.38 ? 4 CYS B SG 1 ATOM 1965 N N . SER B 2 5 ? 59.001 102.190 13.000 1.00 37.96 ? 5 SER B N 1 ATOM 1966 C CA . SER B 2 5 ? 59.391 103.565 13.332 1.00 38.37 ? 5 SER B CA 1 ATOM 1967 C C . SER B 2 5 ? 58.532 104.583 12.562 1.00 37.48 ? 5 SER B C 1 ATOM 1968 O O . SER B 2 5 ? 59.041 105.285 11.688 1.00 36.46 ? 5 SER B O 1 ATOM 1969 C CB . SER B 2 5 ? 60.873 103.770 12.994 1.00 37.85 ? 5 SER B CB 1 ATOM 1970 O OG . SER B 2 5 ? 61.702 102.984 13.833 1.00 39.34 ? 5 SER B OG 1 ATOM 1971 N N . PRO B 2 6 ? 57.228 104.665 12.880 1.00 35.89 ? 6 PRO B N 1 ATOM 1972 C CA . PRO B 2 6 ? 56.372 105.627 12.183 1.00 36.03 ? 6 PRO B CA 1 ATOM 1973 C C . PRO B 2 6 ? 56.802 107.059 12.520 1.00 36.02 ? 6 PRO B C 1 ATOM 1974 O O . PRO B 2 6 ? 57.224 107.326 13.645 1.00 36.56 ? 6 PRO B O 1 ATOM 1975 C CB . PRO B 2 6 ? 54.971 105.306 12.710 1.00 35.58 ? 6 PRO B CB 1 ATOM 1976 C CG . PRO B 2 6 ? 55.197 104.731 14.059 1.00 36.09 ? 6 PRO B CG 1 ATOM 1977 C CD . PRO B 2 6 ? 56.547 104.052 14.033 1.00 37.00 ? 6 PRO B CD 1 ATOM 1978 N N . GLN B 2 7 ? 56.727 107.950 11.538 1.00 36.54 ? 7 GLN B N 1 ATOM 1979 C CA . GLN B 2 7 ? 57.329 109.280 11.637 1.00 37.62 ? 7 GLN B CA 1 ATOM 1980 C C . GLN B 2 7 ? 56.408 110.333 12.250 1.00 35.01 ? 7 GLN B C 1 ATOM 1981 O O . GLN B 2 7 ? 56.878 111.312 12.820 1.00 31.61 ? 7 GLN B O 1 ATOM 1982 C CB . GLN B 2 7 ? 57.813 109.730 10.252 1.00 40.45 ? 7 GLN B CB 1 ATOM 1983 C CG . GLN B 2 7 ? 58.877 108.809 9.651 1.00 43.13 ? 7 GLN B CG 1 ATOM 1984 C CD . GLN B 2 7 ? 60.137 108.743 10.505 1.00 46.64 ? 7 GLN B CD 1 ATOM 1985 O OE1 . GLN B 2 7 ? 60.919 109.695 10.570 1.00 47.64 ? 7 GLN B OE1 1 ATOM 1986 N NE2 . GLN B 2 7 ? 60.363 107.594 11.129 1.00 48.80 ? 7 GLN B NE2 1 ATOM 1987 N N . GLN B 2 8 ? 55.105 110.133 12.120 1.00 34.16 ? 8 GLN B N 1 ATOM 1988 C CA . GLN B 2 8 ? 54.129 111.001 12.754 1.00 34.49 ? 8 GLN B CA 1 ATOM 1989 C C . GLN B 2 8 ? 52.786 110.326 12.848 1.00 33.27 ? 8 GLN B C 1 ATOM 1990 O O . GLN B 2 8 ? 52.529 109.329 12.162 1.00 33.95 ? 8 GLN B O 1 ATOM 1991 C CB . GLN B 2 8 ? 53.970 112.293 11.965 1.00 36.58 ? 8 GLN B CB 1 ATOM 1992 C CG . GLN B 2 8 ? 53.383 112.118 10.573 1.00 39.50 ? 8 GLN B CG 1 ATOM 1993 C CD . GLN B 2 8 ? 53.650 113.329 9.700 1.00 43.02 ? 8 GLN B CD 1 ATOM 1994 O OE1 . GLN B 2 8 ? 54.790 113.579 9.315 1.00 49.40 ? 8 GLN B OE1 1 ATOM 1995 N NE2 . GLN B 2 8 ? 52.606 114.094 9.391 1.00 43.48 ? 8 GLN B NE2 1 ATOM 1996 N N . ARG B 2 9 ? 51.925 110.873 13.699 1.00 30.29 ? 9 ARG B N 1 ATOM 1997 C CA . ARG B 2 9 ? 50.528 110.458 13.732 1.00 28.85 ? 9 ARG B CA 1 ATOM 1998 C C . ARG B 2 9 ? 49.645 111.562 14.253 1.00 26.67 ? 9 ARG B C 1 ATOM 1999 O O . ARG B 2 9 ? 49.921 112.126 15.311 1.00 26.10 ? 9 ARG B O 1 ATOM 2000 C CB . ARG B 2 9 ? 50.334 109.215 14.600 1.00 28.69 ? 9 ARG B CB 1 ATOM 2001 C CG . ARG B 2 9 ? 48.907 108.674 14.602 1.00 29.06 ? 9 ARG B CG 1 ATOM 2002 C CD . ARG B 2 9 ? 48.546 108.035 13.281 1.00 28.90 ? 9 ARG B CD 1 ATOM 2003 N NE . ARG B 2 9 ? 47.117 107.748 13.200 1.00 29.91 ? 9 ARG B NE 1 ATOM 2004 C CZ . ARG B 2 9 ? 46.521 107.218 12.131 1.00 29.84 ? 9 ARG B CZ 1 ATOM 2005 N NH1 . ARG B 2 9 ? 47.216 106.902 11.043 1.00 30.23 ? 9 ARG B NH1 1 ATOM 2006 N NH2 . ARG B 2 9 ? 45.216 106.995 12.154 1.00 30.77 ? 9 ARG B NH2 1 ATOM 2007 N N . THR B 2 10 ? 48.559 111.813 13.533 1.00 26.18 ? 10 THR B N 1 ATOM 2008 C CA . THR B 2 10 ? 47.585 112.834 13.913 1.00 26.85 ? 10 THR B CA 1 ATOM 2009 C C . THR B 2 10 ? 46.367 112.182 14.552 1.00 26.41 ? 10 THR B C 1 ATOM 2010 O O . THR B 2 10 ? 45.756 111.278 13.981 1.00 25.45 ? 10 THR B O 1 ATOM 2011 C CB . THR B 2 10 ? 47.140 113.687 12.712 1.00 27.12 ? 10 THR B CB 1 ATOM 2012 O OG1 . THR B 2 10 ? 48.290 114.270 12.103 1.00 26.61 ? 10 THR B OG1 1 ATOM 2013 C CG2 . THR B 2 10 ? 46.171 114.817 13.158 1.00 27.92 ? 10 THR B CG2 1 ATOM 2014 N N . THR B 2 11 ? 46.019 112.671 15.735 1.00 26.66 ? 11 THR B N 1 ATOM 2015 C CA . THR B 2 11 ? 44.908 112.128 16.508 1.00 27.48 ? 11 THR B CA 1 ATOM 2016 C C . THR B 2 11 ? 44.257 113.258 17.325 1.00 25.61 ? 11 THR B C 1 ATOM 2017 O O . THR B 2 11 ? 44.599 114.422 17.151 1.00 26.07 ? 11 THR B O 1 ATOM 2018 C CB . THR B 2 11 ? 45.420 110.965 17.392 1.00 27.93 ? 11 THR B CB 1 ATOM 2019 O OG1 . THR B 2 11 ? 44.319 110.220 17.899 1.00 30.96 ? 11 THR B OG1 1 ATOM 2020 C CG2 . THR B 2 11 ? 46.265 111.460 18.547 1.00 28.52 ? 11 THR B CG2 1 ATOM 2021 N N . ARG B 2 12 ? 43.309 112.917 18.188 1.00 23.60 ? 12 ARG B N 1 ATOM 2022 C CA . ARG B 2 12 ? 42.713 113.892 19.117 1.00 22.16 ? 12 ARG B CA 1 ATOM 2023 C C . ARG B 2 12 ? 43.056 113.454 20.527 1.00 21.30 ? 12 ARG B C 1 ATOM 2024 O O . ARG B 2 12 ? 43.564 112.351 20.730 1.00 21.00 ? 12 ARG B O 1 ATOM 2025 C CB . ARG B 2 12 ? 41.196 113.968 18.930 1.00 21.82 ? 12 ARG B CB 1 ATOM 2026 C CG . ARG B 2 12 ? 40.751 114.330 17.522 1.00 20.82 ? 12 ARG B CG 1 ATOM 2027 C CD . ARG B 2 12 ? 39.258 114.642 17.462 1.00 20.78 ? 12 ARG B CD 1 ATOM 2028 N NE . ARG B 2 12 ? 38.390 113.460 17.444 1.00 20.94 ? 12 ARG B NE 1 ATOM 2029 C CZ . ARG B 2 12 ? 37.058 113.498 17.432 1.00 21.11 ? 12 ARG B CZ 1 ATOM 2030 N NH1 . ARG B 2 12 ? 36.401 114.661 17.437 1.00 21.92 ? 12 ARG B NH1 1 ATOM 2031 N NH2 . ARG B 2 12 ? 36.363 112.370 17.426 1.00 21.18 ? 12 ARG B NH2 1 ATOM 2032 N N . ILE B 2 13 ? 42.808 114.334 21.490 1.00 19.76 ? 13 ILE B N 1 ATOM 2033 C CA . ILE B 2 13 ? 43.109 114.071 22.891 1.00 19.51 ? 13 ILE B CA 1 ATOM 2034 C C . ILE B 2 13 ? 41.893 114.471 23.691 1.00 19.54 ? 13 ILE B C 1 ATOM 2035 O O . ILE B 2 13 ? 41.539 115.646 23.727 1.00 19.68 ? 13 ILE B O 1 ATOM 2036 C CB . ILE B 2 13 ? 44.346 114.871 23.379 1.00 19.60 ? 13 ILE B CB 1 ATOM 2037 C CG1 . ILE B 2 13 ? 45.563 114.589 22.491 1.00 19.21 ? 13 ILE B CG1 1 ATOM 2038 C CG2 . ILE B 2 13 ? 44.671 114.541 24.836 1.00 19.79 ? 13 ILE B CG2 1 ATOM 2039 C CD1 . ILE B 2 13 ? 46.816 115.324 22.916 1.00 19.40 ? 13 ILE B CD1 1 ATOM 2040 N N . SER B 2 14 ? 41.249 113.497 24.326 1.00 18.80 ? 14 SER B N 1 ATOM 2041 C CA . SER B 2 14 ? 40.069 113.751 25.147 1.00 18.19 ? 14 SER B CA 1 ATOM 2042 C C . SER B 2 14 ? 40.405 113.479 26.602 1.00 18.54 ? 14 SER B C 1 ATOM 2043 O O . SER B 2 14 ? 41.397 112.798 26.907 1.00 18.28 ? 14 SER B O 1 ATOM 2044 C CB . SER B 2 14 ? 38.902 112.880 24.688 1.00 17.61 ? 14 SER B CB 1 ATOM 2045 O OG . SER B 2 14 ? 39.273 111.517 24.667 1.00 16.76 ? 14 SER B OG 1 ATOM 2046 N N . GLY B 2 15 ? 39.583 114.004 27.503 1.00 18.70 ? 15 GLY B N 1 ATOM 2047 C CA . GLY B 2 15 ? 39.845 113.858 28.933 1.00 18.68 ? 15 GLY B CA 1 ATOM 2048 C C . GLY B 2 15 ? 38.607 114.102 29.761 1.00 19.16 ? 15 GLY B C 1 ATOM 2049 O O . GLY B 2 15 ? 37.563 113.485 29.528 1.00 18.39 ? 15 GLY B O 1 ATOM 2050 N N . ARG B 2 16 ? 38.731 115.007 30.730 1.00 20.36 ? 16 ARG B N 1 ATOM 2051 C CA . ARG B 2 16 ? 37.661 115.289 31.676 1.00 21.25 ? 16 ARG B CA 1 ATOM 2052 C C . ARG B 2 16 ? 36.302 115.453 30.985 1.00 21.96 ? 16 ARG B C 1 ATOM 2053 O O . ARG B 2 16 ? 36.186 116.182 29.977 1.00 24.10 ? 16 ARG B O 1 ATOM 2054 C CB . ARG B 2 16 ? 38.008 116.511 32.517 1.00 22.45 ? 16 ARG B CB 1 ATOM 2055 C CG . ARG B 2 16 ? 36.999 116.767 33.610 1.00 22.95 ? 16 ARG B CG 1 ATOM 2056 C CD . ARG B 2 16 ? 37.568 117.574 34.753 1.00 23.78 ? 16 ARG B CD 1 ATOM 2057 N NE . ARG B 2 16 ? 36.643 117.585 35.891 1.00 24.08 ? 16 ARG B NE 1 ATOM 2058 C CZ . ARG B 2 16 ? 36.790 118.346 36.971 1.00 25.87 ? 16 ARG B CZ 1 ATOM 2059 N NH1 . ARG B 2 16 ? 37.820 119.193 37.078 1.00 26.46 ? 16 ARG B NH1 1 ATOM 2060 N NH2 . ARG B 2 16 ? 35.889 118.274 37.954 1.00 26.64 ? 16 ARG B NH2 1 ATOM 2061 N N . ASP B 2 17 ? 35.313 114.713 31.506 1.00 22.07 ? 17 ASP B N 1 ATOM 2062 C CA . ASP B 2 17 ? 33.943 114.621 30.990 1.00 22.94 ? 17 ASP B CA 1 ATOM 2063 C C . ASP B 2 17 ? 33.810 114.316 29.484 1.00 23.22 ? 17 ASP B C 1 ATOM 2064 O O . ASP B 2 17 ? 32.759 114.563 28.899 1.00 23.60 ? 17 ASP B O 1 ATOM 2065 C CB . ASP B 2 17 ? 33.132 115.873 31.384 1.00 24.11 ? 17 ASP B CB 1 ATOM 2066 C CG . ASP B 2 17 ? 32.671 115.843 32.831 1.00 25.77 ? 17 ASP B CG 1 ATOM 2067 O OD1 . ASP B 2 17 ? 33.177 115.011 33.613 1.00 27.61 ? 17 ASP B OD1 1 ATOM 2068 O OD2 . ASP B 2 17 ? 31.794 116.652 33.201 1.00 26.75 ? 17 ASP B OD2 1 ATOM 2069 N N . GLY B 2 18 ? 34.840 113.727 28.882 1.00 22.22 ? 18 GLY B N 1 ATOM 2070 C CA . GLY B 2 18 ? 34.816 113.413 27.452 1.00 22.65 ? 18 GLY B CA 1 ATOM 2071 C C . GLY B 2 18 ? 35.094 114.585 26.520 1.00 22.16 ? 18 GLY B C 1 ATOM 2072 O O . GLY B 2 18 ? 34.877 114.466 25.325 1.00 21.62 ? 18 GLY B O 1 ATOM 2073 N N . LEU B 2 19 ? 35.589 115.701 27.057 1.00 22.42 ? 19 LEU B N 1 ATOM 2074 C CA . LEU B 2 19 ? 35.896 116.878 26.250 1.00 22.89 ? 19 LEU B CA 1 ATOM 2075 C C . LEU B 2 19 ? 37.309 116.742 25.728 1.00 22.87 ? 19 LEU B C 1 ATOM 2076 O O . LEU B 2 19 ? 38.115 115.985 26.279 1.00 22.09 ? 19 LEU B O 1 ATOM 2077 C CB . LEU B 2 19 ? 35.717 118.190 27.038 1.00 22.90 ? 19 LEU B CB 1 ATOM 2078 C CG . LEU B 2 19 ? 34.298 118.780 27.032 1.00 23.91 ? 19 LEU B CG 1 ATOM 2079 C CD1 . LEU B 2 19 ? 33.311 117.864 27.740 1.00 24.37 ? 19 LEU B CD1 1 ATOM 2080 C CD2 . LEU B 2 19 ? 34.286 120.165 27.667 1.00 24.43 ? 19 LEU B CD2 1 ATOM 2081 N N . CYS B 2 20 ? 37.593 117.505 24.671 1.00 23.18 ? 20 CYS B N 1 ATOM 2082 C CA . CYS B 2 20 ? 38.825 117.390 23.895 1.00 22.54 ? 20 CYS B CA 1 ATOM 2083 C C . CYS B 2 20 ? 39.779 118.518 24.188 1.00 21.02 ? 20 CYS B C 1 ATOM 2084 O O . CYS B 2 20 ? 39.373 119.586 24.610 1.00 21.12 ? 20 CYS B O 1 ATOM 2085 C CB . CYS B 2 20 ? 38.491 117.363 22.399 1.00 23.65 ? 20 CYS B CB 1 ATOM 2086 S SG . CYS B 2 20 ? 38.063 115.717 21.784 1.00 25.28 ? 20 CYS B SG 1 ATOM 2087 N N . VAL B 2 21 ? 41.055 118.272 23.942 1.00 21.58 ? 21 VAL B N 1 ATOM 2088 C CA . VAL B 2 21 ? 42.115 119.287 24.043 1.00 21.77 ? 21 VAL B CA 1 ATOM 2089 C C . VAL B 2 21 ? 42.060 120.132 22.759 1.00 23.06 ? 21 VAL B C 1 ATOM 2090 O O . VAL B 2 21 ? 42.101 119.599 21.643 1.00 22.91 ? 21 VAL B O 1 ATOM 2091 C CB . VAL B 2 21 ? 43.501 118.628 24.232 1.00 21.93 ? 21 VAL B CB 1 ATOM 2092 C CG1 . VAL B 2 21 ? 44.611 119.655 24.358 1.00 22.49 ? 21 VAL B CG1 1 ATOM 2093 C CG2 . VAL B 2 21 ? 43.517 117.756 25.490 1.00 22.30 ? 21 VAL B CG2 1 ATOM 2094 N N . ASP B 2 22 ? 41.981 121.451 22.937 1.00 22.79 ? 22 ASP B N 1 ATOM 2095 C CA . ASP B 2 22 ? 41.543 122.376 21.895 1.00 22.73 ? 22 ASP B CA 1 ATOM 2096 C C . ASP B 2 22 ? 42.341 123.672 22.070 1.00 23.50 ? 22 ASP B C 1 ATOM 2097 O O . ASP B 2 22 ? 42.386 124.221 23.174 1.00 22.46 ? 22 ASP B O 1 ATOM 2098 C CB . ASP B 2 22 ? 40.025 122.592 22.074 1.00 22.41 ? 22 ASP B CB 1 ATOM 2099 C CG . ASP B 2 22 ? 39.413 123.641 21.124 1.00 21.64 ? 22 ASP B CG 1 ATOM 2100 O OD1 . ASP B 2 22 ? 39.833 124.817 21.160 1.00 22.58 ? 22 ASP B OD1 1 ATOM 2101 O OD2 . ASP B 2 22 ? 38.451 123.297 20.400 1.00 20.16 ? 22 ASP B OD2 1 ATOM 2102 N N . VAL B 2 23 ? 42.979 124.144 21.000 1.00 23.95 ? 23 VAL B N 1 ATOM 2103 C CA . VAL B 2 23 ? 43.624 125.457 21.025 1.00 26.21 ? 23 VAL B CA 1 ATOM 2104 C C . VAL B 2 23 ? 42.483 126.474 20.894 1.00 26.30 ? 23 VAL B C 1 ATOM 2105 O O . VAL B 2 23 ? 41.788 126.483 19.882 1.00 26.06 ? 23 VAL B O 1 ATOM 2106 C CB . VAL B 2 23 ? 44.651 125.663 19.885 1.00 27.59 ? 23 VAL B CB 1 ATOM 2107 C CG1 . VAL B 2 23 ? 45.419 126.967 20.084 1.00 28.05 ? 23 VAL B CG1 1 ATOM 2108 C CG2 . VAL B 2 23 ? 45.626 124.493 19.803 1.00 28.93 ? 23 VAL B CG2 1 ATOM 2109 N N . TYR B 2 24 ? 42.275 127.274 21.941 1.00 27.61 ? 24 TYR B N 1 ATOM 2110 C CA . TYR B 2 24 ? 41.168 128.252 22.023 1.00 29.55 ? 24 TYR B CA 1 ATOM 2111 C C . TYR B 2 24 ? 41.121 129.179 20.813 1.00 29.91 ? 24 TYR B C 1 ATOM 2112 O O . TYR B 2 24 ? 42.077 129.890 20.540 1.00 29.92 ? 24 TYR B O 1 ATOM 2113 C CB . TYR B 2 24 ? 41.289 129.094 23.299 1.00 30.26 ? 24 TYR B CB 1 ATOM 2114 C CG . TYR B 2 24 ? 40.321 130.246 23.371 1.00 32.14 ? 24 TYR B CG 1 ATOM 2115 C CD1 . TYR B 2 24 ? 38.988 130.034 23.725 1.00 32.40 ? 24 TYR B CD1 1 ATOM 2116 C CD2 . TYR B 2 24 ? 40.734 131.557 23.085 1.00 33.85 ? 24 TYR B CD2 1 ATOM 2117 C CE1 . TYR B 2 24 ? 38.085 131.087 23.785 1.00 34.61 ? 24 TYR B CE1 1 ATOM 2118 C CE2 . TYR B 2 24 ? 39.839 132.626 23.150 1.00 34.10 ? 24 TYR B CE2 1 ATOM 2119 C CZ . TYR B 2 24 ? 38.518 132.384 23.497 1.00 34.70 ? 24 TYR B CZ 1 ATOM 2120 O OH . TYR B 2 24 ? 37.625 133.417 23.567 1.00 35.59 ? 24 TYR B OH 1 ATOM 2121 N N . GLY B 2 25 ? 40.006 129.142 20.091 1.00 32.00 ? 25 GLY B N 1 ATOM 2122 C CA . GLY B 2 25 ? 39.792 130.014 18.941 1.00 34.57 ? 25 GLY B CA 1 ATOM 2123 C C . GLY B 2 25 ? 40.733 129.795 17.768 1.00 35.43 ? 25 GLY B C 1 ATOM 2124 O O . GLY B 2 25 ? 40.914 130.694 16.959 1.00 36.66 ? 25 GLY B O 1 ATOM 2125 N N . ALA B 2 26 ? 41.341 128.609 17.681 1.00 35.28 ? 26 ALA B N 1 ATOM 2126 C CA . ALA B 2 26 ? 42.354 128.299 16.657 1.00 35.02 ? 26 ALA B CA 1 ATOM 2127 C C . ALA B 2 26 ? 43.436 129.375 16.513 1.00 35.59 ? 26 ALA B C 1 ATOM 2128 O O . ALA B 2 26 ? 43.925 129.621 15.411 1.00 35.71 ? 26 ALA B O 1 ATOM 2129 C CB . ALA B 2 26 ? 41.675 128.042 15.320 1.00 33.72 ? 26 ALA B CB 1 ATOM 2130 N N . LEU B 2 27 ? 43.804 130.017 17.622 1.00 35.40 ? 27 LEU B N 1 ATOM 2131 C CA . LEU B 2 27 ? 44.751 131.117 17.573 1.00 35.60 ? 27 LEU B CA 1 ATOM 2132 C C . LEU B 2 27 ? 46.154 130.544 17.452 1.00 38.22 ? 27 LEU B C 1 ATOM 2133 O O . LEU B 2 27 ? 46.529 129.646 18.207 1.00 42.25 ? 27 LEU B O 1 ATOM 2134 C CB . LEU B 2 27 ? 44.620 132.003 18.815 1.00 35.57 ? 27 LEU B CB 1 ATOM 2135 C CG . LEU B 2 27 ? 43.251 132.659 19.016 1.00 35.83 ? 27 LEU B CG 1 ATOM 2136 C CD1 . LEU B 2 27 ? 43.233 133.466 20.305 1.00 35.73 ? 27 LEU B CD1 1 ATOM 2137 C CD2 . LEU B 2 27 ? 42.856 133.536 17.833 1.00 36.43 ? 27 LEU B CD2 1 ATOM 2138 N N . THR B 2 28 ? 46.924 131.051 16.494 1.00 38.35 ? 28 THR B N 1 ATOM 2139 C CA . THR B 2 28 ? 48.244 130.509 16.182 1.00 38.24 ? 28 THR B CA 1 ATOM 2140 C C . THR B 2 28 ? 49.385 131.215 16.898 1.00 38.54 ? 28 THR B C 1 ATOM 2141 O O . THR B 2 28 ? 50.522 130.746 16.838 1.00 40.23 ? 28 THR B O 1 ATOM 2142 C CB . THR B 2 28 ? 48.509 130.567 14.673 1.00 38.10 ? 28 THR B CB 1 ATOM 2143 O OG1 . THR B 2 28 ? 48.310 131.909 14.203 1.00 38.44 ? 28 THR B OG1 1 ATOM 2144 C CG2 . THR B 2 28 ? 47.567 129.630 13.946 1.00 38.72 ? 28 THR B CG2 1 ATOM 2145 N N . ALA B 2 29 ? 49.099 132.326 17.571 1.00 37.54 ? 29 ALA B N 1 ATOM 2146 C CA . ALA B 2 29 ? 50.135 133.091 18.268 1.00 38.56 ? 29 ALA B CA 1 ATOM 2147 C C . ALA B 2 29 ? 50.802 132.265 19.367 1.00 38.50 ? 29 ALA B C 1 ATOM 2148 O O . ALA B 2 29 ? 50.159 131.433 19.996 1.00 40.26 ? 29 ALA B O 1 ATOM 2149 C CB . ALA B 2 29 ? 49.547 134.370 18.858 1.00 39.16 ? 29 ALA B CB 1 ATOM 2150 N N . ASP B 2 30 ? 52.093 132.498 19.588 1.00 38.66 ? 30 ASP B N 1 ATOM 2151 C CA . ASP B 2 30 ? 52.821 131.814 20.643 1.00 39.42 ? 30 ASP B CA 1 ATOM 2152 C C . ASP B 2 30 ? 52.191 132.162 21.982 1.00 39.88 ? 30 ASP B C 1 ATOM 2153 O O . ASP B 2 30 ? 51.827 133.318 22.222 1.00 41.22 ? 30 ASP B O 1 ATOM 2154 C CB . ASP B 2 30 ? 54.298 132.204 20.637 1.00 42.68 ? 30 ASP B CB 1 ATOM 2155 C CG . ASP B 2 30 ? 55.025 131.743 19.381 1.00 44.68 ? 30 ASP B CG 1 ATOM 2156 O OD1 . ASP B 2 30 ? 54.729 130.649 18.855 1.00 46.85 ? 30 ASP B OD1 1 ATOM 2157 O OD2 . ASP B 2 30 ? 55.916 132.475 18.914 1.00 49.95 ? 30 ASP B OD2 1 ATOM 2158 N N . GLY B 2 31 ? 52.020 131.151 22.829 1.00 36.78 ? 31 GLY B N 1 ATOM 2159 C CA . GLY B 2 31 ? 51.328 131.311 24.100 1.00 35.21 ? 31 GLY B CA 1 ATOM 2160 C C . GLY B 2 31 ? 49.816 131.218 24.013 1.00 34.04 ? 31 GLY B C 1 ATOM 2161 O O . GLY B 2 31 ? 49.141 131.412 25.026 1.00 35.03 ? 31 GLY B O 1 ATOM 2162 N N . SER B 2 32 ? 49.277 130.921 22.826 1.00 32.62 ? 32 SER B N 1 ATOM 2163 C CA . SER B 2 32 ? 47.841 130.676 22.654 1.00 32.28 ? 32 SER B CA 1 ATOM 2164 C C . SER B 2 32 ? 47.446 129.476 23.502 1.00 32.66 ? 32 SER B C 1 ATOM 2165 O O . SER B 2 32 ? 47.889 128.359 23.250 1.00 31.30 ? 32 SER B O 1 ATOM 2166 C CB . SER B 2 32 ? 47.496 130.383 21.191 1.00 32.87 ? 32 SER B CB 1 ATOM 2167 O OG . SER B 2 32 ? 47.745 131.499 20.356 1.00 32.79 ? 32 SER B OG 1 ATOM 2168 N N . ARG B 2 33 ? 46.634 129.723 24.524 1.00 32.80 ? 33 ARG B N 1 ATOM 2169 C CA . ARG B 2 33 ? 46.255 128.680 25.479 1.00 31.98 ? 33 ARG B CA 1 ATOM 2170 C C . ARG B 2 33 ? 45.384 127.555 24.896 1.00 30.00 ? 33 ARG B C 1 ATOM 2171 O O . ARG B 2 33 ? 44.712 127.704 23.879 1.00 29.18 ? 33 ARG B O 1 ATOM 2172 C CB . ARG B 2 33 ? 45.535 129.299 26.671 1.00 31.83 ? 33 ARG B CB 1 ATOM 2173 C CG . ARG B 2 33 ? 44.119 129.765 26.384 1.00 32.52 ? 33 ARG B CG 1 ATOM 2174 C CD . ARG B 2 33 ? 43.541 130.474 27.585 1.00 33.22 ? 33 ARG B CD 1 ATOM 2175 N NE . ARG B 2 33 ? 42.109 130.689 27.410 1.00 33.99 ? 33 ARG B NE 1 ATOM 2176 C CZ . ARG B 2 33 ? 41.572 131.670 26.688 1.00 35.86 ? 33 ARG B CZ 1 ATOM 2177 N NH1 . ARG B 2 33 ? 42.339 132.568 26.066 1.00 36.97 ? 33 ARG B NH1 1 ATOM 2178 N NH2 . ARG B 2 33 ? 40.246 131.765 26.593 1.00 37.89 ? 33 ARG B NH2 1 ATOM 2179 N N . VAL B 2 34 ? 45.384 126.442 25.607 1.00 28.81 ? 34 VAL B N 1 ATOM 2180 C CA . VAL B 2 34 ? 44.645 125.260 25.227 1.00 27.22 ? 34 VAL B CA 1 ATOM 2181 C C . VAL B 2 34 ? 43.551 125.056 26.271 1.00 25.17 ? 34 VAL B C 1 ATOM 2182 O O . VAL B 2 34 ? 43.778 125.301 27.451 1.00 23.41 ? 34 VAL B O 1 ATOM 2183 C CB . VAL B 2 34 ? 45.627 124.074 25.127 1.00 28.84 ? 34 VAL B CB 1 ATOM 2184 C CG1 . VAL B 2 34 ? 44.974 122.753 25.471 1.00 29.01 ? 34 VAL B CG1 1 ATOM 2185 C CG2 . VAL B 2 34 ? 46.254 124.038 23.738 1.00 29.51 ? 34 VAL B CG2 1 ATOM 2186 N N . ILE B 2 35 ? 42.382 124.601 25.821 1.00 24.36 ? 35 ILE B N 1 ATOM 2187 C CA . ILE B 2 35 ? 41.189 124.437 26.664 1.00 24.30 ? 35 ILE B CA 1 ATOM 2188 C C . ILE B 2 35 ? 40.541 123.078 26.469 1.00 24.01 ? 35 ILE B C 1 ATOM 2189 O O . ILE B 2 35 ? 40.899 122.348 25.551 1.00 23.60 ? 35 ILE B O 1 ATOM 2190 C CB . ILE B 2 35 ? 40.093 125.485 26.339 1.00 24.27 ? 35 ILE B CB 1 ATOM 2191 C CG1 . ILE B 2 35 ? 39.773 125.486 24.838 1.00 23.69 ? 35 ILE B CG1 1 ATOM 2192 C CG2 . ILE B 2 35 ? 40.530 126.868 26.792 1.00 24.98 ? 35 ILE B CG2 1 ATOM 2193 C CD1 . ILE B 2 35 ? 38.506 126.212 24.471 1.00 23.34 ? 35 ILE B CD1 1 ATOM 2194 N N . LEU B 2 36 ? 39.576 122.771 27.338 1.00 23.96 ? 36 LEU B N 1 ATOM 2195 C CA . LEU B 2 36 ? 38.557 121.756 27.057 1.00 24.14 ? 36 LEU B CA 1 ATOM 2196 C C . LEU B 2 36 ? 37.501 122.347 26.127 1.00 23.76 ? 36 LEU B C 1 ATOM 2197 O O . LEU B 2 36 ? 37.037 123.485 26.315 1.00 23.80 ? 36 LEU B O 1 ATOM 2198 C CB . LEU B 2 36 ? 37.837 121.285 28.326 1.00 24.34 ? 36 LEU B CB 1 ATOM 2199 C CG . LEU B 2 36 ? 38.580 120.509 29.396 1.00 25.31 ? 36 LEU B CG 1 ATOM 2200 C CD1 . LEU B 2 36 ? 37.658 120.271 30.584 1.00 24.80 ? 36 LEU B CD1 1 ATOM 2201 C CD2 . LEU B 2 36 ? 39.127 119.197 28.831 1.00 26.13 ? 36 LEU B CD2 1 ATOM 2202 N N . TYR B 2 37 ? 37.091 121.551 25.151 1.00 23.37 ? 37 TYR B N 1 ATOM 2203 C CA . TYR B 2 37 ? 35.992 121.912 24.270 1.00 23.18 ? 37 TYR B CA 1 ATOM 2204 C C . TYR B 2 37 ? 35.288 120.651 23.785 1.00 22.68 ? 37 TYR B C 1 ATOM 2205 O O . TYR B 2 37 ? 35.931 119.609 23.668 1.00 22.46 ? 37 TYR B O 1 ATOM 2206 C CB . TYR B 2 37 ? 36.540 122.724 23.097 1.00 24.01 ? 37 TYR B CB 1 ATOM 2207 C CG . TYR B 2 37 ? 35.514 123.612 22.444 1.00 24.64 ? 37 TYR B CG 1 ATOM 2208 C CD1 . TYR B 2 37 ? 35.080 124.780 23.076 1.00 25.40 ? 37 TYR B CD1 1 ATOM 2209 C CD2 . TYR B 2 37 ? 34.982 123.301 21.187 1.00 24.64 ? 37 TYR B CD2 1 ATOM 2210 C CE1 . TYR B 2 37 ? 34.141 125.614 22.476 1.00 25.31 ? 37 TYR B CE1 1 ATOM 2211 C CE2 . TYR B 2 37 ? 34.046 124.128 20.581 1.00 25.20 ? 37 TYR B CE2 1 ATOM 2212 C CZ . TYR B 2 37 ? 33.636 125.288 21.227 1.00 25.99 ? 37 TYR B CZ 1 ATOM 2213 O OH . TYR B 2 37 ? 32.702 126.105 20.639 1.00 25.73 ? 37 TYR B OH 1 ATOM 2214 N N . PRO B 2 38 ? 33.970 120.727 23.500 1.00 22.89 ? 38 PRO B N 1 ATOM 2215 C CA . PRO B 2 38 ? 33.334 119.541 22.946 1.00 22.92 ? 38 PRO B CA 1 ATOM 2216 C C . PRO B 2 38 ? 34.061 119.083 21.700 1.00 23.18 ? 38 PRO B C 1 ATOM 2217 O O . PRO B 2 38 ? 34.484 119.903 20.884 1.00 22.69 ? 38 PRO B O 1 ATOM 2218 C CB . PRO B 2 38 ? 31.926 120.017 22.601 1.00 23.28 ? 38 PRO B CB 1 ATOM 2219 C CG . PRO B 2 38 ? 31.660 121.101 23.577 1.00 22.85 ? 38 PRO B CG 1 ATOM 2220 C CD . PRO B 2 38 ? 32.981 121.792 23.760 1.00 23.29 ? 38 PRO B CD 1 ATOM 2221 N N . CYS B 2 39 ? 34.246 117.778 21.604 1.00 24.03 ? 39 CYS B N 1 ATOM 2222 C CA . CYS B 2 39 ? 35.062 117.188 20.568 1.00 24.84 ? 39 CYS B CA 1 ATOM 2223 C C . CYS B 2 39 ? 34.481 117.442 19.193 1.00 23.69 ? 39 CYS B C 1 ATOM 2224 O O . CYS B 2 39 ? 33.283 117.352 19.022 1.00 24.20 ? 39 CYS B O 1 ATOM 2225 C CB . CYS B 2 39 ? 35.185 115.691 20.825 1.00 26.23 ? 39 CYS B CB 1 ATOM 2226 S SG . CYS B 2 39 ? 36.126 115.398 22.339 1.00 29.27 ? 39 CYS B SG 1 ATOM 2227 N N . GLY B 2 40 ? 35.332 117.772 18.230 1.00 24.10 ? 40 GLY B N 1 ATOM 2228 C CA . GLY B 2 40 ? 34.910 117.894 16.823 1.00 25.59 ? 40 GLY B CA 1 ATOM 2229 C C . GLY B 2 40 ? 36.060 117.679 15.850 1.00 26.68 ? 40 GLY B C 1 ATOM 2230 O O . GLY B 2 40 ? 37.182 117.372 16.263 1.00 26.57 ? 40 GLY B O 1 ATOM 2231 N N . GLN B 2 41 ? 35.780 117.881 14.562 1.00 28.69 ? 41 GLN B N 1 ATOM 2232 C CA . GLN B 2 41 ? 36.742 117.650 13.474 1.00 30.33 ? 41 GLN B CA 1 ATOM 2233 C C . GLN B 2 41 ? 37.697 118.804 13.164 1.00 29.56 ? 41 GLN B C 1 ATOM 2234 O O . GLN B 2 41 ? 38.530 118.670 12.280 1.00 29.76 ? 41 GLN B O 1 ATOM 2235 C CB . GLN B 2 41 ? 35.990 117.268 12.186 1.00 33.42 ? 41 GLN B CB 1 ATOM 2236 C CG . GLN B 2 41 ? 35.060 116.062 12.326 1.00 36.46 ? 41 GLN B CG 1 ATOM 2237 C CD . GLN B 2 41 ? 35.758 114.864 12.958 1.00 40.66 ? 41 GLN B CD 1 ATOM 2238 O OE1 . GLN B 2 41 ? 36.880 114.521 12.585 1.00 45.38 ? 41 GLN B OE1 1 ATOM 2239 N NE2 . GLN B 2 41 ? 35.111 114.243 13.939 1.00 43.33 ? 41 GLN B NE2 1 ATOM 2240 N N . GLN B 2 42 ? 37.592 119.920 13.881 1.00 28.32 ? 42 GLN B N 1 ATOM 2241 C CA . GLN B 2 42 ? 38.425 121.094 13.605 1.00 28.06 ? 42 GLN B CA 1 ATOM 2242 C C . GLN B 2 42 ? 39.912 120.824 13.783 1.00 29.22 ? 42 GLN B C 1 ATOM 2243 O O . GLN B 2 42 ? 40.308 120.030 14.630 1.00 29.01 ? 42 GLN B O 1 ATOM 2244 C CB . GLN B 2 42 ? 38.008 122.297 14.468 1.00 27.85 ? 42 GLN B CB 1 ATOM 2245 C CG . GLN B 2 42 ? 37.959 122.049 15.976 1.00 27.40 ? 42 GLN B CG 1 ATOM 2246 C CD . GLN B 2 42 ? 36.557 121.757 16.482 1.00 27.17 ? 42 GLN B CD 1 ATOM 2247 O OE1 . GLN B 2 42 ? 35.886 120.860 15.988 1.00 26.67 ? 42 GLN B OE1 1 ATOM 2248 N NE2 . GLN B 2 42 ? 36.114 122.514 17.475 1.00 27.87 ? 42 GLN B NE2 1 ATOM 2249 N N . GLN B 2 43 ? 40.725 121.531 13.003 1.00 31.14 ? 43 GLN B N 1 ATOM 2250 C CA . GLN B 2 43 ? 42.185 121.339 12.977 1.00 32.43 ? 43 GLN B CA 1 ATOM 2251 C C . GLN B 2 43 ? 42.845 121.687 14.307 1.00 30.63 ? 43 GLN B C 1 ATOM 2252 O O . GLN B 2 43 ? 43.898 121.134 14.636 1.00 28.11 ? 43 GLN B O 1 ATOM 2253 C CB . GLN B 2 43 ? 42.856 122.173 11.867 1.00 36.37 ? 43 GLN B CB 1 ATOM 2254 C CG . GLN B 2 43 ? 42.216 122.150 10.472 1.00 41.22 ? 43 GLN B CG 1 ATOM 2255 C CD . GLN B 2 43 ? 41.785 120.763 10.001 1.00 46.30 ? 43 GLN B CD 1 ATOM 2256 O OE1 . GLN B 2 43 ? 42.628 119.884 9.776 1.00 50.90 ? 43 GLN B OE1 1 ATOM 2257 N NE2 . GLN B 2 43 ? 40.468 120.565 9.826 1.00 46.68 ? 43 GLN B NE2 1 ATOM 2258 N N . ASN B 2 44 ? 42.234 122.607 15.065 1.00 28.59 ? 44 ASN B N 1 ATOM 2259 C CA . ASN B 2 44 ? 42.764 123.017 16.379 1.00 27.55 ? 44 ASN B CA 1 ATOM 2260 C C . ASN B 2 44 ? 42.506 122.017 17.531 1.00 26.67 ? 44 ASN B C 1 ATOM 2261 O O . ASN B 2 44 ? 42.918 122.267 18.669 1.00 25.89 ? 44 ASN B O 1 ATOM 2262 C CB . ASN B 2 44 ? 42.288 124.437 16.751 1.00 27.68 ? 44 ASN B CB 1 ATOM 2263 C CG . ASN B 2 44 ? 40.780 124.546 16.863 1.00 28.02 ? 44 ASN B CG 1 ATOM 2264 O OD1 . ASN B 2 44 ? 40.067 124.314 15.889 1.00 28.05 ? 44 ASN B OD1 1 ATOM 2265 N ND2 . ASN B 2 44 ? 40.283 124.894 18.050 1.00 27.63 ? 44 ASN B ND2 1 ATOM 2266 N N . GLN B 2 45 ? 41.816 120.909 17.231 1.00 26.48 ? 45 GLN B N 1 ATOM 2267 C CA . GLN B 2 45 ? 41.793 119.701 18.080 1.00 25.36 ? 45 GLN B CA 1 ATOM 2268 C C . GLN B 2 45 ? 42.577 118.502 17.500 1.00 26.10 ? 45 GLN B C 1 ATOM 2269 O O . GLN B 2 45 ? 42.578 117.419 18.095 1.00 27.69 ? 45 GLN B O 1 ATOM 2270 C CB . GLN B 2 45 ? 40.350 119.276 18.332 1.00 25.03 ? 45 GLN B CB 1 ATOM 2271 C CG . GLN B 2 45 ? 39.557 120.251 19.187 1.00 24.70 ? 45 GLN B CG 1 ATOM 2272 C CD . GLN B 2 45 ? 38.164 119.764 19.489 1.00 24.34 ? 45 GLN B CD 1 ATOM 2273 O OE1 . GLN B 2 45 ? 37.804 118.626 19.179 1.00 24.32 ? 45 GLN B OE1 1 ATOM 2274 N NE2 . GLN B 2 45 ? 37.366 120.620 20.104 1.00 25.61 ? 45 GLN B NE2 1 ATOM 2275 N N . GLN B 2 46 ? 43.235 118.681 16.358 1.00 26.16 ? 46 GLN B N 1 ATOM 2276 C CA . GLN B 2 46 ? 44.118 117.659 15.789 1.00 27.12 ? 46 GLN B CA 1 ATOM 2277 C C . GLN B 2 46 ? 45.506 117.819 16.365 1.00 26.27 ? 46 GLN B C 1 ATOM 2278 O O . GLN B 2 46 ? 46.079 118.903 16.311 1.00 27.34 ? 46 GLN B O 1 ATOM 2279 C CB . GLN B 2 46 ? 44.198 117.767 14.276 1.00 28.45 ? 46 GLN B CB 1 ATOM 2280 C CG . GLN B 2 46 ? 42.983 117.220 13.584 1.00 30.59 ? 46 GLN B CG 1 ATOM 2281 C CD . GLN B 2 46 ? 42.959 117.592 12.124 1.00 33.75 ? 46 GLN B CD 1 ATOM 2282 O OE1 . GLN B 2 46 ? 43.993 117.884 11.535 1.00 38.86 ? 46 GLN B OE1 1 ATOM 2283 N NE2 . GLN B 2 46 ? 41.779 117.583 11.525 1.00 35.81 ? 46 GLN B NE2 1 ATOM 2284 N N . TRP B 2 47 ? 46.040 116.731 16.910 1.00 24.64 ? 47 TRP B N 1 ATOM 2285 C CA . TRP B 2 47 ? 47.328 116.739 17.576 1.00 24.27 ? 47 TRP B CA 1 ATOM 2286 C C . TRP B 2 47 ? 48.212 115.696 16.912 1.00 24.55 ? 47 TRP B C 1 ATOM 2287 O O . TRP B 2 47 ? 47.842 114.509 16.845 1.00 24.12 ? 47 TRP B O 1 ATOM 2288 C CB . TRP B 2 47 ? 47.162 116.471 19.075 1.00 24.55 ? 47 TRP B CB 1 ATOM 2289 C CG . TRP B 2 47 ? 46.443 117.577 19.746 1.00 23.85 ? 47 TRP B CG 1 ATOM 2290 C CD1 . TRP B 2 47 ? 45.125 117.620 20.066 1.00 23.50 ? 47 TRP B CD1 1 ATOM 2291 C CD2 . TRP B 2 47 ? 46.996 118.834 20.130 1.00 24.16 ? 47 TRP B CD2 1 ATOM 2292 N NE1 . TRP B 2 47 ? 44.816 118.827 20.640 1.00 23.29 ? 47 TRP B NE1 1 ATOM 2293 C CE2 . TRP B 2 47 ? 45.950 119.588 20.708 1.00 24.19 ? 47 TRP B CE2 1 ATOM 2294 C CE3 . TRP B 2 47 ? 48.283 119.389 20.068 1.00 24.16 ? 47 TRP B CE3 1 ATOM 2295 C CZ2 . TRP B 2 47 ? 46.143 120.886 21.208 1.00 24.78 ? 47 TRP B CZ2 1 ATOM 2296 C CZ3 . TRP B 2 47 ? 48.483 120.674 20.568 1.00 25.16 ? 47 TRP B CZ3 1 ATOM 2297 C CH2 . TRP B 2 47 ? 47.407 121.417 21.123 1.00 25.51 ? 47 TRP B CH2 1 ATOM 2298 N N . THR B 2 48 ? 49.359 116.149 16.401 1.00 23.68 ? 48 THR B N 1 ATOM 2299 C CA . THR B 2 48 ? 50.303 115.283 15.728 1.00 24.22 ? 48 THR B CA 1 ATOM 2300 C C . THR B 2 48 ? 51.479 114.999 16.638 1.00 24.61 ? 48 THR B C 1 ATOM 2301 O O . THR B 2 48 ? 52.104 115.918 17.162 1.00 25.76 ? 48 THR B O 1 ATOM 2302 C CB . THR B 2 48 ? 50.770 115.890 14.398 1.00 24.04 ? 48 THR B CB 1 ATOM 2303 O OG1 . THR B 2 48 ? 49.622 116.114 13.584 1.00 23.36 ? 48 THR B OG1 1 ATOM 2304 C CG2 . THR B 2 48 ? 51.679 114.927 13.657 1.00 24.65 ? 48 THR B CG2 1 ATOM 2305 N N . PHE B 2 49 ? 51.778 113.715 16.799 1.00 24.93 ? 49 PHE B N 1 ATOM 2306 C CA . PHE B 2 49 ? 52.866 113.252 17.647 1.00 25.24 ? 49 PHE B CA 1 ATOM 2307 C C . PHE B 2 49 ? 54.036 112.880 16.768 1.00 26.01 ? 49 PHE B C 1 ATOM 2308 O O . PHE B 2 49 ? 53.859 112.326 15.688 1.00 24.62 ? 49 PHE B O 1 ATOM 2309 C CB . PHE B 2 49 ? 52.433 112.033 18.458 1.00 25.48 ? 49 PHE B CB 1 ATOM 2310 C CG . PHE B 2 49 ? 51.407 112.340 19.500 1.00 24.61 ? 49 PHE B CG 1 ATOM 2311 C CD1 . PHE B 2 49 ? 50.110 112.697 19.136 1.00 23.91 ? 49 PHE B CD1 1 ATOM 2312 C CD2 . PHE B 2 49 ? 51.733 112.278 20.850 1.00 24.42 ? 49 PHE B CD2 1 ATOM 2313 C CE1 . PHE B 2 49 ? 49.164 112.995 20.093 1.00 23.21 ? 49 PHE B CE1 1 ATOM 2314 C CE2 . PHE B 2 49 ? 50.783 112.562 21.809 1.00 24.53 ? 49 PHE B CE2 1 ATOM 2315 C CZ . PHE B 2 49 ? 49.497 112.932 21.429 1.00 23.57 ? 49 PHE B CZ 1 ATOM 2316 N N . TYR B 2 50 ? 55.230 113.177 17.260 1.00 27.96 ? 50 TYR B N 1 ATOM 2317 C CA . TYR B 2 50 ? 56.460 112.969 16.523 1.00 29.77 ? 50 TYR B CA 1 ATOM 2318 C C . TYR B 2 50 ? 57.453 112.266 17.426 1.00 30.86 ? 50 TYR B C 1 ATOM 2319 O O . TYR B 2 50 ? 57.329 112.350 18.652 1.00 30.61 ? 50 TYR B O 1 ATOM 2320 C CB . TYR B 2 50 ? 57.031 114.315 16.078 1.00 29.68 ? 50 TYR B CB 1 ATOM 2321 C CG . TYR B 2 50 ? 56.186 115.042 15.052 1.00 29.81 ? 50 TYR B CG 1 ATOM 2322 C CD1 . TYR B 2 50 ? 56.344 114.798 13.687 1.00 29.36 ? 50 TYR B CD1 1 ATOM 2323 C CD2 . TYR B 2 50 ? 55.237 115.981 15.441 1.00 29.44 ? 50 TYR B CD2 1 ATOM 2324 C CE1 . TYR B 2 50 ? 55.586 115.474 12.739 1.00 29.59 ? 50 TYR B CE1 1 ATOM 2325 C CE2 . TYR B 2 50 ? 54.472 116.658 14.499 1.00 30.51 ? 50 TYR B CE2 1 ATOM 2326 C CZ . TYR B 2 50 ? 54.655 116.407 13.151 1.00 30.18 ? 50 TYR B CZ 1 ATOM 2327 O OH . TYR B 2 50 ? 53.896 117.068 12.226 1.00 29.71 ? 50 TYR B OH 1 ATOM 2328 N N . PRO B 2 51 ? 58.454 111.581 16.834 1.00 32.39 ? 51 PRO B N 1 ATOM 2329 C CA . PRO B 2 51 ? 59.413 110.868 17.673 1.00 32.77 ? 51 PRO B CA 1 ATOM 2330 C C . PRO B 2 51 ? 60.367 111.742 18.488 1.00 33.96 ? 51 PRO B C 1 ATOM 2331 O O . PRO B 2 51 ? 61.060 111.217 19.357 1.00 36.62 ? 51 PRO B O 1 ATOM 2332 C CB . PRO B 2 51 ? 60.175 109.989 16.674 1.00 32.94 ? 51 PRO B CB 1 ATOM 2333 C CG . PRO B 2 51 ? 59.297 109.909 15.477 1.00 32.29 ? 51 PRO B CG 1 ATOM 2334 C CD . PRO B 2 51 ? 58.653 111.253 15.413 1.00 31.98 ? 51 PRO B CD 1 ATOM 2335 N N . ASP B 2 52 ? 60.383 113.053 18.249 1.00 34.51 ? 52 ASP B N 1 ATOM 2336 C CA . ASP B 2 52 ? 61.080 113.991 19.139 1.00 35.68 ? 52 ASP B CA 1 ATOM 2337 C C . ASP B 2 52 ? 60.306 114.371 20.416 1.00 36.56 ? 52 ASP B C 1 ATOM 2338 O O . ASP B 2 52 ? 60.661 115.351 21.077 1.00 36.79 ? 52 ASP B O 1 ATOM 2339 C CB . ASP B 2 52 ? 61.505 115.259 18.369 1.00 37.38 ? 52 ASP B CB 1 ATOM 2340 C CG . ASP B 2 52 ? 60.332 116.123 17.916 1.00 38.52 ? 52 ASP B CG 1 ATOM 2341 O OD1 . ASP B 2 52 ? 59.160 115.686 17.976 1.00 38.78 ? 52 ASP B OD1 1 ATOM 2342 O OD2 . ASP B 2 52 ? 60.601 117.261 17.485 1.00 38.81 ? 52 ASP B OD2 1 ATOM 2343 N N . ASN B 2 53 ? 59.260 113.605 20.755 1.00 35.68 ? 53 ASN B N 1 ATOM 2344 C CA . ASN B 2 53 ? 58.416 113.845 21.925 1.00 35.00 ? 53 ASN B CA 1 ATOM 2345 C C . ASN B 2 53 ? 57.648 115.175 21.920 1.00 34.83 ? 53 ASN B C 1 ATOM 2346 O O . ASN B 2 53 ? 57.302 115.696 22.985 1.00 35.02 ? 53 ASN B O 1 ATOM 2347 C CB . ASN B 2 53 ? 59.213 113.683 23.226 1.00 36.01 ? 53 ASN B CB 1 ATOM 2348 C CG . ASN B 2 53 ? 59.812 112.299 23.382 1.00 36.29 ? 53 ASN B CG 1 ATOM 2349 O OD1 . ASN B 2 53 ? 60.938 112.163 23.853 1.00 39.38 ? 53 ASN B OD1 1 ATOM 2350 N ND2 . ASN B 2 53 ? 59.060 111.269 23.014 1.00 34.79 ? 53 ASN B ND2 1 ATOM 2351 N N . THR B 2 54 ? 57.362 115.708 20.731 1.00 32.99 ? 54 THR B N 1 ATOM 2352 C CA . THR B 2 54 ? 56.503 116.874 20.608 1.00 31.47 ? 54 THR B CA 1 ATOM 2353 C C . THR B 2 54 ? 55.093 116.425 20.266 1.00 30.37 ? 54 THR B C 1 ATOM 2354 O O . THR B 2 54 ? 54.870 115.312 19.780 1.00 27.63 ? 54 THR B O 1 ATOM 2355 C CB . THR B 2 54 ? 57.009 117.892 19.558 1.00 32.58 ? 54 THR B CB 1 ATOM 2356 O OG1 . THR B 2 54 ? 57.052 117.307 18.246 1.00 31.81 ? 54 THR B OG1 1 ATOM 2357 C CG2 . THR B 2 54 ? 58.381 118.424 19.942 1.00 32.81 ? 54 THR B CG2 1 ATOM 2358 N N . ILE B 2 55 ? 54.150 117.308 20.568 1.00 29.43 ? 55 ILE B N 1 ATOM 2359 C CA . ILE B 2 55 ? 52.738 117.115 20.293 1.00 29.01 ? 55 ILE B CA 1 ATOM 2360 C C . ILE B 2 55 ? 52.267 118.442 19.709 1.00 29.74 ? 55 ILE B C 1 ATOM 2361 O O . ILE B 2 55 ? 52.379 119.490 20.370 1.00 29.59 ? 55 ILE B O 1 ATOM 2362 C CB . ILE B 2 55 ? 51.947 116.765 21.577 1.00 27.52 ? 55 ILE B CB 1 ATOM 2363 C CG1 . ILE B 2 55 ? 52.658 115.648 22.368 1.00 27.85 ? 55 ILE B CG1 1 ATOM 2364 C CG2 . ILE B 2 55 ? 50.522 116.348 21.226 1.00 26.94 ? 55 ILE B CG2 1 ATOM 2365 C CD1 . ILE B 2 55 ? 51.999 115.286 23.685 1.00 27.86 ? 55 ILE B CD1 1 ATOM 2366 N N . ARG B 2 56 ? 51.752 118.404 18.481 1.00 29.49 ? 56 ARG B N 1 ATOM 2367 C CA . ARG B 2 56 ? 51.574 119.623 17.698 1.00 29.54 ? 56 ARG B CA 1 ATOM 2368 C C . ARG B 2 56 ? 50.175 119.800 17.133 1.00 29.57 ? 56 ARG B C 1 ATOM 2369 O O . ARG B 2 56 ? 49.561 118.841 16.665 1.00 27.31 ? 56 ARG B O 1 ATOM 2370 C CB . ARG B 2 56 ? 52.581 119.647 16.547 1.00 30.49 ? 56 ARG B CB 1 ATOM 2371 C CG . ARG B 2 56 ? 54.020 119.475 17.000 1.00 30.61 ? 56 ARG B CG 1 ATOM 2372 C CD . ARG B 2 56 ? 55.023 119.786 15.900 1.00 30.50 ? 56 ARG B CD 1 ATOM 2373 N NE . ARG B 2 56 ? 56.383 119.435 16.323 1.00 31.68 ? 56 ARG B NE 1 ATOM 2374 C CZ . ARG B 2 56 ? 57.497 119.708 15.644 1.00 30.90 ? 56 ARG B CZ 1 ATOM 2375 N NH1 . ARG B 2 56 ? 57.453 120.315 14.463 1.00 32.83 ? 56 ARG B NH1 1 ATOM 2376 N NH2 . ARG B 2 56 ? 58.671 119.358 16.151 1.00 30.42 ? 56 ARG B NH2 1 ATOM 2377 N N . SER B 2 57 ? 49.686 121.041 17.187 1.00 28.64 ? 57 SER B N 1 ATOM 2378 C CA . SER B 2 57 ? 48.487 121.465 16.456 1.00 28.61 ? 57 SER B CA 1 ATOM 2379 C C . SER B 2 57 ? 48.758 122.828 15.814 1.00 30.51 ? 57 SER B C 1 ATOM 2380 O O . SER B 2 57 ? 49.472 123.671 16.394 1.00 29.78 ? 57 SER B O 1 ATOM 2381 C CB . SER B 2 57 ? 47.265 121.553 17.368 1.00 26.99 ? 57 SER B CB 1 ATOM 2382 O OG . SER B 2 57 ? 46.087 121.640 16.594 1.00 26.44 ? 57 SER B OG 1 ATOM 2383 N N . LEU B 2 58 ? 48.214 123.018 14.610 1.00 31.52 ? 58 LEU B N 1 ATOM 2384 C CA . LEU B 2 58 ? 48.412 124.242 13.832 1.00 33.09 ? 58 LEU B CA 1 ATOM 2385 C C . LEU B 2 58 ? 49.912 124.550 13.646 1.00 33.52 ? 58 LEU B C 1 ATOM 2386 O O . LEU B 2 58 ? 50.322 125.707 13.653 1.00 33.31 ? 58 LEU B O 1 ATOM 2387 C CB . LEU B 2 58 ? 47.672 125.414 14.508 1.00 34.14 ? 58 LEU B CB 1 ATOM 2388 C CG . LEU B 2 58 ? 46.276 125.111 15.094 1.00 34.08 ? 58 LEU B CG 1 ATOM 2389 C CD1 . LEU B 2 58 ? 45.800 126.234 16.006 1.00 34.59 ? 58 LEU B CD1 1 ATOM 2390 C CD2 . LEU B 2 58 ? 45.263 124.838 13.991 1.00 34.22 ? 58 LEU B CD2 1 ATOM 2391 N N . GLY B 2 59 ? 50.721 123.499 13.495 1.00 32.89 ? 59 GLY B N 1 ATOM 2392 C CA . GLY B 2 59 ? 52.159 123.626 13.273 1.00 32.49 ? 59 GLY B CA 1 ATOM 2393 C C . GLY B 2 59 ? 53.013 123.998 14.471 1.00 32.82 ? 59 GLY B C 1 ATOM 2394 O O . GLY B 2 59 ? 54.224 124.161 14.332 1.00 31.20 ? 59 GLY B O 1 ATOM 2395 N N . LYS B 2 60 ? 52.408 124.113 15.652 1.00 34.66 ? 60 LYS B N 1 ATOM 2396 C CA . LYS B 2 60 ? 53.132 124.532 16.846 1.00 35.92 ? 60 LYS B CA 1 ATOM 2397 C C . LYS B 2 60 ? 52.977 123.518 17.974 1.00 35.80 ? 60 LYS B C 1 ATOM 2398 O O . LYS B 2 60 ? 52.013 122.755 18.007 1.00 34.04 ? 60 LYS B O 1 ATOM 2399 C CB . LYS B 2 60 ? 52.661 125.919 17.274 1.00 37.31 ? 60 LYS B CB 1 ATOM 2400 C CG . LYS B 2 60 ? 53.245 127.017 16.399 1.00 39.06 ? 60 LYS B CG 1 ATOM 2401 C CD . LYS B 2 60 ? 53.023 128.408 16.974 1.00 40.79 ? 60 LYS B CD 1 ATOM 2402 C CE . LYS B 2 60 ? 53.619 129.468 16.054 1.00 41.72 ? 60 LYS B CE 1 ATOM 2403 N NZ . LYS B 2 60 ? 53.013 130.800 16.299 1.00 42.50 ? 60 LYS B NZ 1 ATOM 2404 N N . CYS B 2 61 ? 53.932 123.559 18.902 1.00 35.65 ? 61 CYS B N 1 ATOM 2405 C CA . CYS B 2 61 ? 54.104 122.550 19.931 1.00 37.17 ? 61 CYS B CA 1 ATOM 2406 C C . CYS B 2 61 ? 53.369 122.879 21.225 1.00 36.58 ? 61 CYS B C 1 ATOM 2407 O O . CYS B 2 61 ? 53.554 123.963 21.795 1.00 35.22 ? 61 CYS B O 1 ATOM 2408 C CB . CYS B 2 61 ? 55.592 122.380 20.244 1.00 40.89 ? 61 CYS B CB 1 ATOM 2409 S SG . CYS B 2 61 ? 56.519 121.545 18.938 1.00 46.81 ? 61 CYS B SG 1 ATOM 2410 N N . LEU B 2 62 ? 52.557 121.922 21.686 1.00 33.98 ? 62 LEU B N 1 ATOM 2411 C CA . LEU B 2 62 ? 51.961 121.942 23.021 1.00 31.89 ? 62 LEU B CA 1 ATOM 2412 C C . LEU B 2 62 ? 53.064 122.073 24.060 1.00 31.96 ? 62 LEU B C 1 ATOM 2413 O O . LEU B 2 62 ? 54.061 121.363 23.977 1.00 32.98 ? 62 LEU B O 1 ATOM 2414 C CB . LEU B 2 62 ? 51.174 120.651 23.272 1.00 31.12 ? 62 LEU B CB 1 ATOM 2415 C CG . LEU B 2 62 ? 50.353 120.559 24.558 1.00 31.32 ? 62 LEU B CG 1 ATOM 2416 C CD1 . LEU B 2 62 ? 49.072 121.374 24.422 1.00 30.72 ? 62 LEU B CD1 1 ATOM 2417 C CD2 . LEU B 2 62 ? 50.042 119.102 24.897 1.00 31.63 ? 62 LEU B CD2 1 ATOM 2418 N N . ALA B 2 63 ? 52.899 122.981 25.023 1.00 32.07 ? 63 ALA B N 1 ATOM 2419 C CA . ALA B 2 63 ? 53.908 123.198 26.064 1.00 32.88 ? 63 ALA B CA 1 ATOM 2420 C C . ALA B 2 63 ? 53.369 123.900 27.295 1.00 33.05 ? 63 ALA B C 1 ATOM 2421 O O . ALA B 2 63 ? 52.391 124.647 27.221 1.00 32.91 ? 63 ALA B O 1 ATOM 2422 C CB . ALA B 2 63 ? 55.079 124.000 25.511 1.00 34.01 ? 63 ALA B CB 1 ATOM 2423 N N . THR B 2 64 ? 54.038 123.661 28.422 1.00 35.17 ? 64 THR B N 1 ATOM 2424 C CA . THR B 2 64 ? 53.784 124.393 29.661 1.00 36.50 ? 64 THR B CA 1 ATOM 2425 C C . THR B 2 64 ? 54.292 125.817 29.480 1.00 37.65 ? 64 THR B C 1 ATOM 2426 O O . THR B 2 64 ? 55.189 126.060 28.661 1.00 37.92 ? 64 THR B O 1 ATOM 2427 C CB . THR B 2 64 ? 54.478 123.743 30.885 1.00 37.00 ? 64 THR B CB 1 ATOM 2428 O OG1 . THR B 2 64 ? 55.873 123.547 30.627 1.00 37.19 ? 64 THR B OG1 1 ATOM 2429 C CG2 . THR B 2 64 ? 53.855 122.412 31.200 1.00 37.21 ? 64 THR B CG2 1 ATOM 2430 N N . SER B 2 65 ? 53.698 126.752 30.215 1.00 38.02 ? 65 SER B N 1 ATOM 2431 C CA . SER B 2 65 ? 54.121 128.153 30.164 1.00 38.21 ? 65 SER B CA 1 ATOM 2432 C C . SER B 2 65 ? 54.888 128.618 31.415 1.00 39.35 ? 65 SER B C 1 ATOM 2433 O O . SER B 2 65 ? 55.293 129.772 31.471 1.00 43.01 ? 65 SER B O 1 ATOM 2434 C CB . SER B 2 65 ? 52.915 129.062 29.880 1.00 36.79 ? 65 SER B CB 1 ATOM 2435 O OG . SER B 2 65 ? 51.961 129.023 30.920 1.00 35.87 ? 65 SER B OG 1 ATOM 2436 N N . ALA B 2 66 ? 55.101 127.743 32.399 1.00 40.27 ? 66 ALA B N 1 ATOM 2437 C CA . ALA B 2 66 ? 55.907 128.080 33.591 1.00 41.15 ? 66 ALA B CA 1 ATOM 2438 C C . ALA B 2 66 ? 56.487 126.846 34.257 1.00 43.06 ? 66 ALA B C 1 ATOM 2439 O O . ALA B 2 66 ? 55.972 125.740 34.094 1.00 45.67 ? 66 ALA B O 1 ATOM 2440 C CB . ALA B 2 66 ? 55.073 128.841 34.606 1.00 41.34 ? 66 ALA B CB 1 ATOM 2441 N N . LEU B 2 67 ? 57.551 127.053 35.024 1.00 43.30 ? 67 LEU B N 1 ATOM 2442 C CA . LEU B 2 67 ? 58.169 125.983 35.814 1.00 42.10 ? 67 LEU B CA 1 ATOM 2443 C C . LEU B 2 67 ? 57.288 125.575 36.992 1.00 41.33 ? 67 LEU B C 1 ATOM 2444 O O . LEU B 2 67 ? 57.185 124.390 37.307 1.00 42.50 ? 67 LEU B O 1 ATOM 2445 C CB . LEU B 2 67 ? 59.556 126.413 36.307 1.00 41.92 ? 67 LEU B CB 1 ATOM 2446 C CG . LEU B 2 67 ? 60.323 125.496 37.267 1.00 42.59 ? 67 LEU B CG 1 ATOM 2447 C CD1 . LEU B 2 67 ? 60.527 124.101 36.701 1.00 43.14 ? 67 LEU B CD1 1 ATOM 2448 C CD2 . LEU B 2 67 ? 61.664 126.126 37.594 1.00 42.39 ? 67 LEU B CD2 1 ATOM 2449 N N . SER B 2 68 ? 56.669 126.558 37.643 1.00 41.75 ? 68 SER B N 1 ATOM 2450 C CA . SER B 2 68 ? 55.761 126.307 38.771 1.00 42.14 ? 68 SER B CA 1 ATOM 2451 C C . SER B 2 68 ? 54.359 125.923 38.294 1.00 40.56 ? 68 SER B C 1 ATOM 2452 O O . SER B 2 68 ? 53.991 126.125 37.135 1.00 41.75 ? 68 SER B O 1 ATOM 2453 C CB . SER B 2 68 ? 55.677 127.538 39.690 1.00 43.12 ? 68 SER B CB 1 ATOM 2454 O OG . SER B 2 68 ? 55.141 128.656 39.001 1.00 45.22 ? 68 SER B OG 1 ATOM 2455 N N . SER B 2 69 ? 53.577 125.393 39.219 1.00 39.04 ? 69 SER B N 1 ATOM 2456 C CA . SER B 2 69 ? 52.264 124.860 38.909 1.00 39.05 ? 69 SER B CA 1 ATOM 2457 C C . SER B 2 69 ? 51.222 125.964 38.773 1.00 38.16 ? 69 SER B C 1 ATOM 2458 O O . SER B 2 69 ? 51.385 127.045 39.320 1.00 41.37 ? 69 SER B O 1 ATOM 2459 C CB . SER B 2 69 ? 51.839 123.900 40.012 1.00 38.84 ? 69 SER B CB 1 ATOM 2460 O OG . SER B 2 69 ? 51.556 124.609 41.205 1.00 38.22 ? 69 SER B OG 1 ATOM 2461 N N . GLY B 2 70 ? 50.148 125.664 38.048 1.00 37.63 ? 70 GLY B N 1 ATOM 2462 C CA . GLY B 2 70 ? 48.989 126.551 37.924 1.00 37.70 ? 70 GLY B CA 1 ATOM 2463 C C . GLY B 2 70 ? 48.912 127.419 36.679 1.00 36.45 ? 70 GLY B C 1 ATOM 2464 O O . GLY B 2 70 ? 47.881 128.056 36.449 1.00 36.66 ? 70 GLY B O 1 ATOM 2465 N N . SER B 2 71 ? 49.983 127.465 35.890 1.00 34.94 ? 71 SER B N 1 ATOM 2466 C CA . SER B 2 71 ? 49.991 128.223 34.642 1.00 36.32 ? 71 SER B CA 1 ATOM 2467 C C . SER B 2 71 ? 49.364 127.437 33.490 1.00 35.84 ? 71 SER B C 1 ATOM 2468 O O . SER B 2 71 ? 49.350 126.196 33.490 1.00 33.85 ? 71 SER B O 1 ATOM 2469 C CB . SER B 2 71 ? 51.421 128.614 34.248 1.00 38.88 ? 71 SER B CB 1 ATOM 2470 O OG . SER B 2 71 ? 51.991 129.496 35.193 1.00 40.68 ? 71 SER B OG 1 ATOM 2471 N N . ASN B 2 72 ? 48.880 128.179 32.497 1.00 33.63 ? 72 ASN B N 1 ATOM 2472 C CA . ASN B 2 72 ? 48.265 127.582 31.322 1.00 32.99 ? 72 ASN B CA 1 ATOM 2473 C C . ASN B 2 72 ? 49.248 126.730 30.512 1.00 32.53 ? 72 ASN B C 1 ATOM 2474 O O . ASN B 2 72 ? 50.451 127.033 30.436 1.00 31.70 ? 72 ASN B O 1 ATOM 2475 C CB . ASN B 2 72 ? 47.685 128.662 30.404 1.00 32.38 ? 72 ASN B CB 1 ATOM 2476 C CG . ASN B 2 72 ? 46.431 129.314 30.964 1.00 31.32 ? 72 ASN B CG 1 ATOM 2477 O OD1 . ASN B 2 72 ? 45.752 128.762 31.828 1.00 31.18 ? 72 ASN B OD1 1 ATOM 2478 N ND2 . ASN B 2 72 ? 46.091 130.479 30.431 1.00 29.83 ? 72 ASN B ND2 1 ATOM 2479 N N . VAL B 2 73 ? 48.725 125.651 29.934 1.00 30.84 ? 73 VAL B N 1 ATOM 2480 C CA . VAL B 2 73 ? 49.431 124.920 28.883 1.00 31.01 ? 73 VAL B CA 1 ATOM 2481 C C . VAL B 2 73 ? 49.054 125.593 27.560 1.00 29.88 ? 73 VAL B C 1 ATOM 2482 O O . VAL B 2 73 ? 47.907 125.978 27.361 1.00 28.37 ? 73 VAL B O 1 ATOM 2483 C CB . VAL B 2 73 ? 49.088 123.416 28.905 1.00 30.41 ? 73 VAL B CB 1 ATOM 2484 C CG1 . VAL B 2 73 ? 49.584 122.712 27.655 1.00 30.48 ? 73 VAL B CG1 1 ATOM 2485 C CG2 . VAL B 2 73 ? 49.696 122.780 30.148 1.00 30.47 ? 73 VAL B CG2 1 ATOM 2486 N N . VAL B 2 74 ? 50.037 125.743 26.679 1.00 30.11 ? 74 VAL B N 1 ATOM 2487 C CA . VAL B 2 74 ? 49.900 126.567 25.474 1.00 32.06 ? 74 VAL B CA 1 ATOM 2488 C C . VAL B 2 74 ? 50.505 125.881 24.255 1.00 33.87 ? 74 VAL B C 1 ATOM 2489 O O . VAL B 2 74 ? 51.165 124.853 24.382 1.00 35.44 ? 74 VAL B O 1 ATOM 2490 C CB . VAL B 2 74 ? 50.574 127.949 25.680 1.00 31.14 ? 74 VAL B CB 1 ATOM 2491 C CG1 . VAL B 2 74 ? 49.968 128.659 26.892 1.00 30.89 ? 74 VAL B CG1 1 ATOM 2492 C CG2 . VAL B 2 74 ? 52.087 127.823 25.849 1.00 30.81 ? 74 VAL B CG2 1 ATOM 2493 N N . ILE B 2 75 ? 50.257 126.440 23.075 1.00 35.70 ? 75 ILE B N 1 ATOM 2494 C CA . ILE B 2 75 ? 51.069 126.107 21.900 1.00 35.56 ? 75 ILE B CA 1 ATOM 2495 C C . ILE B 2 75 ? 52.087 127.214 21.674 1.00 37.91 ? 75 ILE B C 1 ATOM 2496 O O . ILE B 2 75 ? 51.815 128.387 21.940 1.00 38.22 ? 75 ILE B O 1 ATOM 2497 C CB . ILE B 2 75 ? 50.257 125.856 20.616 1.00 34.87 ? 75 ILE B CB 1 ATOM 2498 C CG1 . ILE B 2 75 ? 49.329 127.030 20.290 1.00 34.13 ? 75 ILE B CG1 1 ATOM 2499 C CG2 . ILE B 2 75 ? 49.487 124.539 20.731 1.00 34.77 ? 75 ILE B CG2 1 ATOM 2500 C CD1 . ILE B 2 75 ? 48.908 127.068 18.843 1.00 34.84 ? 75 ILE B CD1 1 ATOM 2501 N N . THR B 2 76 ? 53.259 126.826 21.189 1.00 40.38 ? 76 THR B N 1 ATOM 2502 C CA . THR B 2 76 ? 54.364 127.751 20.978 1.00 42.53 ? 76 THR B CA 1 ATOM 2503 C C . THR B 2 76 ? 55.260 127.260 19.850 1.00 43.44 ? 76 THR B C 1 ATOM 2504 O O . THR B 2 76 ? 55.210 126.089 19.471 1.00 42.05 ? 76 THR B O 1 ATOM 2505 C CB . THR B 2 76 ? 55.177 127.944 22.277 1.00 42.47 ? 76 THR B CB 1 ATOM 2506 O OG1 . THR B 2 76 ? 55.913 129.169 22.200 1.00 43.34 ? 76 THR B OG1 1 ATOM 2507 C CG2 . THR B 2 76 ? 56.125 126.754 22.546 1.00 42.73 ? 76 THR B CG2 1 ATOM 2508 N N . ASN B 2 77 ? 56.084 128.160 19.325 1.00 46.60 ? 77 ASN B N 1 ATOM 2509 C CA . ASN B 2 77 ? 56.980 127.828 18.216 1.00 47.27 ? 77 ASN B CA 1 ATOM 2510 C C . ASN B 2 77 ? 57.853 126.663 18.634 1.00 47.09 ? 77 ASN B C 1 ATOM 2511 O O . ASN B 2 77 ? 58.435 126.679 19.720 1.00 46.20 ? 77 ASN B O 1 ATOM 2512 C CB . ASN B 2 77 ? 57.856 129.030 17.823 1.00 48.61 ? 77 ASN B CB 1 ATOM 2513 C CG . ASN B 2 77 ? 58.534 128.845 16.478 1.00 47.57 ? 77 ASN B CG 1 ATOM 2514 O OD1 . ASN B 2 77 ? 59.458 128.045 16.345 1.00 47.99 ? 77 ASN B OD1 1 ATOM 2515 N ND2 . ASN B 2 77 ? 58.082 129.584 15.477 1.00 47.88 ? 77 ASN B ND2 1 ATOM 2516 N N . CYS B 2 78 ? 57.927 125.654 17.775 1.00 49.58 ? 78 CYS B N 1 ATOM 2517 C CA . CYS B 2 78 ? 58.631 124.418 18.107 1.00 51.81 ? 78 CYS B CA 1 ATOM 2518 C C . CYS B 2 78 ? 60.145 124.588 18.191 1.00 52.17 ? 78 CYS B C 1 ATOM 2519 O O . CYS B 2 78 ? 60.809 123.813 18.872 1.00 52.20 ? 78 CYS B O 1 ATOM 2520 C CB . CYS B 2 78 ? 58.235 123.304 17.138 1.00 53.30 ? 78 CYS B CB 1 ATOM 2521 S SG . CYS B 2 78 ? 56.486 122.821 17.347 1.00 57.64 ? 78 CYS B SG 1 ATOM 2522 N N . ASP B 2 79 ? 60.681 125.630 17.556 1.00 55.25 ? 79 ASP B N 1 ATOM 2523 C CA . ASP B 2 79 ? 62.111 125.949 17.665 1.00 56.30 ? 79 ASP B CA 1 ATOM 2524 C C . ASP B 2 79 ? 62.546 126.368 19.076 1.00 57.31 ? 79 ASP B C 1 ATOM 2525 O O . ASP B 2 79 ? 63.716 126.222 19.404 1.00 61.12 ? 79 ASP B O 1 ATOM 2526 C CB . ASP B 2 79 ? 62.522 127.030 16.656 1.00 57.22 ? 79 ASP B CB 1 ATOM 2527 C CG . ASP B 2 79 ? 62.230 126.638 15.208 1.00 58.32 ? 79 ASP B CG 1 ATOM 2528 O OD1 . ASP B 2 79 ? 62.082 125.432 14.912 1.00 60.00 ? 79 ASP B OD1 1 ATOM 2529 O OD2 . ASP B 2 79 ? 62.146 127.548 14.360 1.00 60.29 ? 79 ASP B OD2 1 ATOM 2530 N N . TYR B 2 80 ? 61.622 126.860 19.909 1.00 59.66 ? 80 TYR B N 1 ATOM 2531 C CA . TYR B 2 80 ? 61.925 127.151 21.330 1.00 61.99 ? 80 TYR B CA 1 ATOM 2532 C C . TYR B 2 80 ? 62.168 125.905 22.183 1.00 60.76 ? 80 TYR B C 1 ATOM 2533 O O . TYR B 2 80 ? 62.704 126.007 23.282 1.00 62.11 ? 80 TYR B O 1 ATOM 2534 C CB . TYR B 2 80 ? 60.798 127.941 22.009 1.00 66.13 ? 80 TYR B CB 1 ATOM 2535 C CG . TYR B 2 80 ? 60.411 129.245 21.350 1.00 70.36 ? 80 TYR B CG 1 ATOM 2536 C CD1 . TYR B 2 80 ? 61.380 130.149 20.898 1.00 74.45 ? 80 TYR B CD1 1 ATOM 2537 C CD2 . TYR B 2 80 ? 59.069 129.591 21.203 1.00 72.80 ? 80 TYR B CD2 1 ATOM 2538 C CE1 . TYR B 2 80 ? 61.017 131.349 20.299 1.00 77.34 ? 80 TYR B CE1 1 ATOM 2539 C CE2 . TYR B 2 80 ? 58.694 130.790 20.612 1.00 75.97 ? 80 TYR B CE2 1 ATOM 2540 C CZ . TYR B 2 80 ? 59.669 131.666 20.160 1.00 78.14 ? 80 TYR B CZ 1 ATOM 2541 O OH . TYR B 2 80 ? 59.302 132.854 19.572 1.00 76.69 ? 80 TYR B OH 1 ATOM 2542 N N . LEU B 2 81 ? 61.734 124.746 21.699 1.00 61.30 ? 81 LEU B N 1 ATOM 2543 C CA . LEU B 2 81 ? 61.941 123.481 22.384 1.00 62.10 ? 81 LEU B CA 1 ATOM 2544 C C . LEU B 2 81 ? 63.060 122.673 21.728 1.00 61.96 ? 81 LEU B C 1 ATOM 2545 O O . LEU B 2 81 ? 63.160 121.469 21.975 1.00 60.52 ? 81 LEU B O 1 ATOM 2546 C CB . LEU B 2 81 ? 60.632 122.676 22.372 1.00 63.61 ? 81 LEU B CB 1 ATOM 2547 C CG . LEU B 2 81 ? 59.338 123.442 22.701 1.00 63.32 ? 81 LEU B CG 1 ATOM 2548 C CD1 . LEU B 2 81 ? 58.129 122.521 22.609 1.00 62.48 ? 81 LEU B CD1 1 ATOM 2549 C CD2 . LEU B 2 81 ? 59.433 124.094 24.074 1.00 62.41 ? 81 LEU B CD2 1 ATOM 2550 N N . ARG B 2 82 ? 63.909 123.334 20.929 1.00 61.95 ? 82 ARG B N 1 ATOM 2551 C CA . ARG B 2 82 ? 64.987 122.693 20.171 1.00 62.24 ? 82 ARG B CA 1 ATOM 2552 C C . ARG B 2 82 ? 65.821 121.689 20.945 1.00 64.66 ? 82 ARG B C 1 ATOM 2553 O O . ARG B 2 82 ? 66.117 120.608 20.432 1.00 62.97 ? 82 ARG B O 1 ATOM 2554 N N . TYR B 2 83 ? 66.180 122.039 22.182 1.00 67.44 ? 83 TYR B N 1 ATOM 2555 C CA . TYR B 2 83 ? 66.989 121.168 23.051 1.00 71.20 ? 83 TYR B CA 1 ATOM 2556 C C . TYR B 2 83 ? 66.175 120.476 24.146 1.00 67.90 ? 83 TYR B C 1 ATOM 2557 O O . TYR B 2 83 ? 66.740 119.766 24.970 1.00 67.43 ? 83 TYR B O 1 ATOM 2558 C CB . TYR B 2 83 ? 68.123 121.963 23.707 1.00 74.75 ? 83 TYR B CB 1 ATOM 2559 C CG . TYR B 2 83 ? 68.779 122.961 22.787 1.00 78.17 ? 83 TYR B CG 1 ATOM 2560 C CD1 . TYR B 2 83 ? 69.506 122.535 21.674 1.00 79.35 ? 83 TYR B CD1 1 ATOM 2561 C CD2 . TYR B 2 83 ? 68.662 124.336 23.020 1.00 80.10 ? 83 TYR B CD2 1 ATOM 2562 C CE1 . TYR B 2 83 ? 70.104 123.449 20.822 1.00 80.84 ? 83 TYR B CE1 1 ATOM 2563 C CE2 . TYR B 2 83 ? 69.257 125.256 22.175 1.00 81.09 ? 83 TYR B CE2 1 ATOM 2564 C CZ . TYR B 2 83 ? 69.977 124.808 21.080 1.00 82.73 ? 83 TYR B CZ 1 ATOM 2565 O OH . TYR B 2 83 ? 70.570 125.716 20.242 1.00 89.49 ? 83 TYR B OH 1 ATOM 2566 N N . ASP B 2 84 ? 64.861 120.678 24.149 1.00 66.05 ? 84 ASP B N 1 ATOM 2567 C CA . ASP B 2 84 ? 63.995 120.135 25.184 1.00 64.81 ? 84 ASP B CA 1 ATOM 2568 C C . ASP B 2 84 ? 63.669 118.653 24.949 1.00 62.43 ? 84 ASP B C 1 ATOM 2569 O O . ASP B 2 84 ? 63.519 118.213 23.803 1.00 61.87 ? 84 ASP B O 1 ATOM 2570 C CB . ASP B 2 84 ? 62.705 120.947 25.249 1.00 64.80 ? 84 ASP B CB 1 ATOM 2571 C CG . ASP B 2 84 ? 61.831 120.563 26.424 1.00 65.27 ? 84 ASP B CG 1 ATOM 2572 O OD1 . ASP B 2 84 ? 62.363 120.370 27.540 1.00 65.57 ? 84 ASP B OD1 1 ATOM 2573 O OD2 . ASP B 2 84 ? 60.603 120.449 26.229 1.00 66.57 ? 84 ASP B OD2 1 ATOM 2574 N N . ASP B 2 85 ? 63.560 117.903 26.047 1.00 59.14 ? 85 ASP B N 1 ATOM 2575 C CA . ASP B 2 85 ? 63.183 116.483 26.014 1.00 59.30 ? 85 ASP B CA 1 ATOM 2576 C C . ASP B 2 85 ? 61.708 116.275 25.689 1.00 54.51 ? 85 ASP B C 1 ATOM 2577 O O . ASP B 2 85 ? 61.355 115.254 25.108 1.00 55.67 ? 85 ASP B O 1 ATOM 2578 C CB . ASP B 2 85 ? 63.477 115.814 27.358 1.00 62.76 ? 85 ASP B CB 1 ATOM 2579 C CG . ASP B 2 85 ? 64.959 115.722 27.663 1.00 65.48 ? 85 ASP B CG 1 ATOM 2580 O OD1 . ASP B 2 85 ? 65.794 115.873 26.744 1.00 66.91 ? 85 ASP B OD1 1 ATOM 2581 O OD2 . ASP B 2 85 ? 65.288 115.491 28.844 1.00 71.75 ? 85 ASP B OD2 1 ATOM 2582 N N . GLY B 2 86 ? 60.854 117.205 26.127 1.00 48.43 ? 86 GLY B N 1 ATOM 2583 C CA . GLY B 2 86 ? 59.456 117.284 25.685 1.00 43.20 ? 86 GLY B CA 1 ATOM 2584 C C . GLY B 2 86 ? 58.434 116.605 26.593 1.00 39.37 ? 86 GLY B C 1 ATOM 2585 O O . GLY B 2 86 ? 58.492 116.734 27.828 1.00 37.27 ? 86 GLY B O 1 ATOM 2586 N N . TRP B 2 87 ? 57.491 115.893 25.970 1.00 34.86 ? 87 TRP B N 1 ATOM 2587 C CA . TRP B 2 87 ? 56.372 115.255 26.681 1.00 34.86 ? 87 TRP B CA 1 ATOM 2588 C C . TRP B 2 87 ? 56.545 113.755 26.819 1.00 34.25 ? 87 TRP B C 1 ATOM 2589 O O . TRP B 2 87 ? 56.983 113.082 25.890 1.00 31.92 ? 87 TRP B O 1 ATOM 2590 C CB . TRP B 2 87 ? 55.056 115.508 25.952 1.00 34.35 ? 87 TRP B CB 1 ATOM 2591 C CG . TRP B 2 87 ? 54.569 116.916 26.062 1.00 33.82 ? 87 TRP B CG 1 ATOM 2592 C CD1 . TRP B 2 87 ? 54.755 117.916 25.158 1.00 32.77 ? 87 TRP B CD1 1 ATOM 2593 C CD2 . TRP B 2 87 ? 53.810 117.477 27.139 1.00 32.59 ? 87 TRP B CD2 1 ATOM 2594 N NE1 . TRP B 2 87 ? 54.154 119.066 25.603 1.00 33.87 ? 87 TRP B NE1 1 ATOM 2595 C CE2 . TRP B 2 87 ? 53.566 118.825 26.816 1.00 33.02 ? 87 TRP B CE2 1 ATOM 2596 C CE3 . TRP B 2 87 ? 53.313 116.969 28.347 1.00 32.54 ? 87 TRP B CE3 1 ATOM 2597 C CZ2 . TRP B 2 87 ? 52.851 119.680 27.659 1.00 33.25 ? 87 TRP B CZ2 1 ATOM 2598 C CZ3 . TRP B 2 87 ? 52.594 117.813 29.182 1.00 32.03 ? 87 TRP B CZ3 1 ATOM 2599 C CH2 . TRP B 2 87 ? 52.371 119.155 28.834 1.00 33.38 ? 87 TRP B CH2 1 ATOM 2600 N N . MET B 2 88 ? 56.176 113.247 27.986 1.00 35.46 ? 88 MET B N 1 ATOM 2601 C CA . MET B 2 88 ? 56.147 111.823 28.251 1.00 36.95 ? 88 MET B CA 1 ATOM 2602 C C . MET B 2 88 ? 54.734 111.493 28.714 1.00 33.96 ? 88 MET B C 1 ATOM 2603 O O . MET B 2 88 ? 54.207 112.147 29.606 1.00 32.31 ? 88 MET B O 1 ATOM 2604 C CB . MET B 2 88 ? 57.181 111.505 29.317 1.00 42.07 ? 88 MET B CB 1 ATOM 2605 C CG . MET B 2 88 ? 57.099 110.124 29.947 1.00 48.37 ? 88 MET B CG 1 ATOM 2606 S SD . MET B 2 88 ? 58.544 109.851 31.003 1.00 57.86 ? 88 MET B SD 1 ATOM 2607 C CE . MET B 2 88 ? 58.412 111.178 32.208 1.00 52.05 ? 88 MET B CE 1 ATOM 2608 N N . VAL B 2 89 ? 54.139 110.479 28.092 1.00 31.53 ? 89 VAL B N 1 ATOM 2609 C CA . VAL B 2 89 ? 52.795 110.012 28.411 1.00 29.22 ? 89 VAL B CA 1 ATOM 2610 C C . VAL B 2 89 ? 52.866 108.652 29.119 1.00 28.70 ? 89 VAL B C 1 ATOM 2611 O O . VAL B 2 89 ? 53.361 107.687 28.549 1.00 28.91 ? 89 VAL B O 1 ATOM 2612 C CB . VAL B 2 89 ? 51.953 109.890 27.128 1.00 28.40 ? 89 VAL B CB 1 ATOM 2613 C CG1 . VAL B 2 89 ? 50.506 109.556 27.457 1.00 28.42 ? 89 VAL B CG1 1 ATOM 2614 C CG2 . VAL B 2 89 ? 52.033 111.182 26.324 1.00 28.91 ? 89 VAL B CG2 1 ATOM 2615 N N . SER B 2 90 ? 52.359 108.565 30.347 1.00 28.45 ? 90 SER B N 1 ATOM 2616 C CA . SER B 2 90 ? 52.408 107.308 31.126 1.00 29.46 ? 90 SER B CA 1 ATOM 2617 C C . SER B 2 90 ? 51.487 106.253 30.534 1.00 30.05 ? 90 SER B C 1 ATOM 2618 O O . SER B 2 90 ? 50.674 106.557 29.677 1.00 29.71 ? 90 SER B O 1 ATOM 2619 C CB . SER B 2 90 ? 52.005 107.550 32.584 1.00 29.09 ? 90 SER B CB 1 ATOM 2620 O OG . SER B 2 90 ? 50.605 107.755 32.718 1.00 28.81 ? 90 SER B OG 1 ATOM 2621 N N . SER B 2 91 ? 51.610 105.018 31.012 1.00 30.60 ? 91 SER B N 1 ATOM 2622 C CA . SER B 2 91 ? 50.661 103.947 30.669 1.00 31.59 ? 91 SER B CA 1 ATOM 2623 C C . SER B 2 91 ? 49.218 104.361 30.887 1.00 30.71 ? 91 SER B C 1 ATOM 2624 O O . SER B 2 91 ? 48.360 104.041 30.079 1.00 33.18 ? 91 SER B O 1 ATOM 2625 C CB . SER B 2 91 ? 50.902 102.707 31.536 1.00 31.19 ? 91 SER B CB 1 ATOM 2626 O OG . SER B 2 91 ? 51.984 101.970 31.050 1.00 32.25 ? 91 SER B OG 1 ATOM 2627 N N . SER B 2 92 ? 48.967 105.051 31.994 1.00 29.06 ? 92 SER B N 1 ATOM 2628 C CA . SER B 2 92 ? 47.611 105.366 32.429 1.00 29.48 ? 92 SER B CA 1 ATOM 2629 C C . SER B 2 92 ? 47.013 106.640 31.816 1.00 28.10 ? 92 SER B C 1 ATOM 2630 O O . SER B 2 92 ? 45.848 106.954 32.077 1.00 29.68 ? 92 SER B O 1 ATOM 2631 C CB . SER B 2 92 ? 47.578 105.443 33.950 1.00 29.98 ? 92 SER B CB 1 ATOM 2632 O OG . SER B 2 92 ? 48.644 106.239 34.424 1.00 34.00 ? 92 SER B OG 1 ATOM 2633 N N . GLY B 2 93 ? 47.770 107.341 30.976 1.00 27.12 ? 93 GLY B N 1 ATOM 2634 C CA . GLY B 2 93 ? 47.265 108.539 30.280 1.00 27.16 ? 93 GLY B CA 1 ATOM 2635 C C . GLY B 2 93 ? 47.561 109.852 30.998 1.00 26.44 ? 93 GLY B C 1 ATOM 2636 O O . GLY B 2 93 ? 46.848 110.838 30.816 1.00 24.44 ? 93 GLY B O 1 ATOM 2637 N N . THR B 2 94 ? 48.612 109.857 31.814 1.00 25.87 ? 94 THR B N 1 ATOM 2638 C CA . THR B 2 94 ? 49.126 111.076 32.385 1.00 27.05 ? 94 THR B CA 1 ATOM 2639 C C . THR B 2 94 ? 50.095 111.662 31.381 1.00 26.87 ? 94 THR B C 1 ATOM 2640 O O . THR B 2 94 ? 51.008 110.977 30.933 1.00 25.91 ? 94 THR B O 1 ATOM 2641 C CB . THR B 2 94 ? 49.858 110.822 33.710 1.00 27.69 ? 94 THR B CB 1 ATOM 2642 O OG1 . THR B 2 94 ? 48.954 110.194 34.627 1.00 28.11 ? 94 THR B OG1 1 ATOM 2643 C CG2 . THR B 2 94 ? 50.355 112.134 34.299 1.00 27.41 ? 94 THR B CG2 1 ATOM 2644 N N . MET B 2 95 ? 49.881 112.923 31.022 1.00 25.79 ? 95 MET B N 1 ATOM 2645 C CA . MET B 2 95 ? 50.736 113.603 30.071 1.00 26.88 ? 95 MET B CA 1 ATOM 2646 C C . MET B 2 95 ? 51.627 114.573 30.825 1.00 27.99 ? 95 MET B C 1 ATOM 2647 O O . MET B 2 95 ? 51.146 115.583 31.350 1.00 26.18 ? 95 MET B O 1 ATOM 2648 C CB . MET B 2 95 ? 49.882 114.334 29.047 1.00 27.92 ? 95 MET B CB 1 ATOM 2649 C CG . MET B 2 95 ? 49.148 113.380 28.132 1.00 28.34 ? 95 MET B CG 1 ATOM 2650 S SD . MET B 2 95 ? 48.072 114.253 26.998 1.00 30.11 ? 95 MET B SD 1 ATOM 2651 C CE . MET B 2 95 ? 49.279 115.014 25.909 1.00 29.88 ? 95 MET B CE 1 ATOM 2652 N N . MET B 2 96 ? 52.922 114.249 30.868 1.00 29.50 ? 96 MET B N 1 ATOM 2653 C CA . MET B 2 96 ? 53.893 114.916 31.734 1.00 31.10 ? 96 MET B CA 1 ATOM 2654 C C . MET B 2 96 ? 55.016 115.584 30.943 1.00 31.49 ? 96 MET B C 1 ATOM 2655 O O . MET B 2 96 ? 55.616 114.968 30.056 1.00 31.93 ? 96 MET B O 1 ATOM 2656 C CB . MET B 2 96 ? 54.506 113.895 32.702 1.00 32.23 ? 96 MET B CB 1 ATOM 2657 C CG . MET B 2 96 ? 55.428 114.506 33.754 1.00 32.93 ? 96 MET B CG 1 ATOM 2658 S SD . MET B 2 96 ? 56.077 113.348 34.974 1.00 33.16 ? 96 MET B SD 1 ATOM 2659 C CE . MET B 2 96 ? 54.740 113.220 36.168 1.00 31.93 ? 96 MET B CE 1 ATOM 2660 N N . ASN B 2 97 ? 55.292 116.845 31.272 1.00 32.44 ? 97 ASN B N 1 ATOM 2661 C CA . ASN B 2 97 ? 56.532 117.504 30.851 1.00 33.38 ? 97 ASN B CA 1 ATOM 2662 C C . ASN B 2 97 ? 57.724 116.822 31.532 1.00 32.82 ? 97 ASN B C 1 ATOM 2663 O O . ASN B 2 97 ? 57.791 116.799 32.759 1.00 31.62 ? 97 ASN B O 1 ATOM 2664 C CB . ASN B 2 97 ? 56.479 118.993 31.210 1.00 33.52 ? 97 ASN B CB 1 ATOM 2665 C CG . ASN B 2 97 ? 57.806 119.715 30.997 1.00 34.94 ? 97 ASN B CG 1 ATOM 2666 O OD1 . ASN B 2 97 ? 58.866 119.277 31.458 1.00 32.97 ? 97 ASN B OD1 1 ATOM 2667 N ND2 . ASN B 2 97 ? 57.749 120.844 30.306 1.00 37.39 ? 97 ASN B ND2 1 ATOM 2668 N N . LYS B 2 98 ? 58.664 116.304 30.739 1.00 35.19 ? 98 LYS B N 1 ATOM 2669 C CA . LYS B 2 98 ? 59.777 115.480 31.271 1.00 38.17 ? 98 LYS B CA 1 ATOM 2670 C C . LYS B 2 98 ? 60.737 116.236 32.173 1.00 37.54 ? 98 LYS B C 1 ATOM 2671 O O . LYS B 2 98 ? 61.210 115.693 33.164 1.00 37.04 ? 98 LYS B O 1 ATOM 2672 C CB . LYS B 2 98 ? 60.573 114.830 30.136 1.00 40.81 ? 98 LYS B CB 1 ATOM 2673 C CG . LYS B 2 98 ? 59.795 113.775 29.361 1.00 43.79 ? 98 LYS B CG 1 ATOM 2674 C CD . LYS B 2 98 ? 60.488 113.394 28.058 1.00 46.53 ? 98 LYS B CD 1 ATOM 2675 C CE . LYS B 2 98 ? 61.659 112.447 28.283 1.00 47.25 ? 98 LYS B CE 1 ATOM 2676 N NZ . LYS B 2 98 ? 61.260 111.025 28.087 1.00 49.30 ? 98 LYS B NZ 1 ATOM 2677 N N . SER B 2 99 ? 61.029 117.479 31.812 1.00 39.17 ? 99 SER B N 1 ATOM 2678 C CA . SER B 2 99 ? 61.890 118.350 32.619 1.00 41.40 ? 99 SER B CA 1 ATOM 2679 C C . SER B 2 99 ? 61.276 118.743 33.982 1.00 40.68 ? 99 SER B C 1 ATOM 2680 O O . SER B 2 99 ? 61.871 118.499 35.028 1.00 39.33 ? 99 SER B O 1 ATOM 2681 C CB . SER B 2 99 ? 62.257 119.610 31.816 1.00 43.40 ? 99 SER B CB 1 ATOM 2682 O OG . SER B 2 99 ? 62.771 120.630 32.655 1.00 46.43 ? 99 SER B OG 1 ATOM 2683 N N . SER B 2 100 ? 60.089 119.345 33.957 1.00 40.49 ? 100 SER B N 1 ATOM 2684 C CA . SER B 2 100 ? 59.473 119.934 35.156 1.00 40.57 ? 100 SER B CA 1 ATOM 2685 C C . SER B 2 100 ? 58.562 118.998 35.954 1.00 40.60 ? 100 SER B C 1 ATOM 2686 O O . SER B 2 100 ? 58.206 119.313 37.091 1.00 40.10 ? 100 SER B O 1 ATOM 2687 C CB . SER B 2 100 ? 58.663 121.174 34.763 1.00 41.43 ? 100 SER B CB 1 ATOM 2688 O OG . SER B 2 100 ? 57.438 120.831 34.127 1.00 43.02 ? 100 SER B OG 1 ATOM 2689 N N . HIS B 2 101 ? 58.147 117.888 35.341 1.00 40.58 ? 101 HIS B N 1 ATOM 2690 C CA . HIS B 2 101 ? 57.208 116.914 35.943 1.00 39.12 ? 101 HIS B CA 1 ATOM 2691 C C . HIS B 2 101 ? 55.767 117.427 36.109 1.00 35.19 ? 101 HIS B C 1 ATOM 2692 O O . HIS B 2 101 ? 54.934 116.712 36.670 1.00 33.45 ? 101 HIS B O 1 ATOM 2693 C CB . HIS B 2 101 ? 57.725 116.329 37.284 1.00 41.06 ? 101 HIS B CB 1 ATOM 2694 C CG . HIS B 2 101 ? 59.143 115.846 37.232 1.00 44.54 ? 101 HIS B CG 1 ATOM 2695 N ND1 . HIS B 2 101 ? 59.578 114.915 36.314 1.00 45.93 ? 101 HIS B ND1 1 ATOM 2696 C CD2 . HIS B 2 101 ? 60.223 116.165 37.984 1.00 45.80 ? 101 HIS B CD2 1 ATOM 2697 C CE1 . HIS B 2 101 ? 60.866 114.685 36.497 1.00 46.65 ? 101 HIS B CE1 1 ATOM 2698 N NE2 . HIS B 2 101 ? 61.281 115.432 37.503 1.00 47.77 ? 101 HIS B NE2 1 ATOM 2699 N N . LEU B 2 102 ? 55.453 118.631 35.614 1.00 31.21 ? 102 LEU B N 1 ATOM 2700 C CA . LEU B 2 102 ? 54.069 119.097 35.638 1.00 29.43 ? 102 LEU B CA 1 ATOM 2701 C C . LEU B 2 102 ? 53.241 118.306 34.623 1.00 26.72 ? 102 LEU B C 1 ATOM 2702 O O . LEU B 2 102 ? 53.754 117.845 33.601 1.00 25.59 ? 102 LEU B O 1 ATOM 2703 C CB . LEU B 2 102 ? 53.950 120.602 35.354 1.00 29.85 ? 102 LEU B CB 1 ATOM 2704 C CG . LEU B 2 102 ? 54.479 121.610 36.381 1.00 29.90 ? 102 LEU B CG 1 ATOM 2705 C CD1 . LEU B 2 102 ? 54.226 123.011 35.857 1.00 30.41 ? 102 LEU B CD1 1 ATOM 2706 C CD2 . LEU B 2 102 ? 53.860 121.467 37.764 1.00 29.61 ? 102 LEU B CD2 1 ATOM 2707 N N . VAL B 2 103 ? 51.961 118.146 34.923 1.00 24.89 ? 103 VAL B N 1 ATOM 2708 C CA . VAL B 2 103 ? 51.083 117.346 34.080 1.00 24.82 ? 103 VAL B CA 1 ATOM 2709 C C . VAL B 2 103 ? 49.861 118.123 33.610 1.00 24.25 ? 103 VAL B C 1 ATOM 2710 O O . VAL B 2 103 ? 49.372 119.028 34.296 1.00 22.98 ? 103 VAL B O 1 ATOM 2711 C CB . VAL B 2 103 ? 50.667 116.026 34.767 1.00 24.45 ? 103 VAL B CB 1 ATOM 2712 C CG1 . VAL B 2 103 ? 51.905 115.236 35.165 1.00 24.38 ? 103 VAL B CG1 1 ATOM 2713 C CG2 . VAL B 2 103 ? 49.753 116.258 35.964 1.00 24.64 ? 103 VAL B CG2 1 ATOM 2714 N N . LEU B 2 104 ? 49.375 117.737 32.431 1.00 23.77 ? 104 LEU B N 1 ATOM 2715 C CA . LEU B 2 104 ? 48.226 118.364 31.828 1.00 23.15 ? 104 LEU B CA 1 ATOM 2716 C C . LEU B 2 104 ? 47.014 118.104 32.720 1.00 23.80 ? 104 LEU B C 1 ATOM 2717 O O . LEU B 2 104 ? 46.719 116.948 33.066 1.00 22.06 ? 104 LEU B O 1 ATOM 2718 C CB . LEU B 2 104 ? 48.008 117.830 30.406 1.00 23.78 ? 104 LEU B CB 1 ATOM 2719 C CG . LEU B 2 104 ? 46.991 118.549 29.517 1.00 24.27 ? 104 LEU B CG 1 ATOM 2720 C CD1 . LEU B 2 104 ? 47.342 120.028 29.372 1.00 25.06 ? 104 LEU B CD1 1 ATOM 2721 C CD2 . LEU B 2 104 ? 46.920 117.895 28.149 1.00 24.20 ? 104 LEU B CD2 1 ATOM 2722 N N . THR B 2 105 ? 46.336 119.194 33.098 1.00 23.19 ? 105 THR B N 1 ATOM 2723 C CA . THR B 2 105 ? 45.267 119.167 34.078 1.00 23.01 ? 105 THR B CA 1 ATOM 2724 C C . THR B 2 105 ? 44.101 120.043 33.666 1.00 22.43 ? 105 THR B C 1 ATOM 2725 O O . THR B 2 105 ? 44.312 121.147 33.169 1.00 21.94 ? 105 THR B O 1 ATOM 2726 C CB . THR B 2 105 ? 45.780 119.715 35.421 1.00 23.01 ? 105 THR B CB 1 ATOM 2727 O OG1 . THR B 2 105 ? 47.037 119.106 35.742 1.00 24.33 ? 105 THR B OG1 1 ATOM 2728 C CG2 . THR B 2 105 ? 44.778 119.460 36.525 1.00 22.75 ? 105 THR B CG2 1 ATOM 2729 N N . ALA B 2 106 ? 42.882 119.570 33.924 1.00 22.56 ? 106 ALA B N 1 ATOM 2730 C CA . ALA B 2 106 ? 41.664 120.371 33.758 1.00 23.41 ? 106 ALA B CA 1 ATOM 2731 C C . ALA B 2 106 ? 40.984 120.656 35.111 1.00 23.42 ? 106 ALA B C 1 ATOM 2732 O O . ALA B 2 106 ? 40.248 119.814 35.642 1.00 22.92 ? 106 ALA B O 1 ATOM 2733 C CB . ALA B 2 106 ? 40.700 119.664 32.821 1.00 23.70 ? 106 ALA B CB 1 ATOM 2734 N N . ASN B 2 107 ? 41.189 121.860 35.644 1.00 24.10 ? 107 ASN B N 1 ATOM 2735 C CA . ASN B 2 107 ? 40.654 122.209 36.974 1.00 25.78 ? 107 ASN B CA 1 ATOM 2736 C C . ASN B 2 107 ? 39.134 122.403 37.066 1.00 26.03 ? 107 ASN B C 1 ATOM 2737 O O . ASN B 2 107 ? 38.598 122.489 38.162 1.00 27.13 ? 107 ASN B O 1 ATOM 2738 C CB . ASN B 2 107 ? 41.363 123.433 37.546 1.00 26.35 ? 107 ASN B CB 1 ATOM 2739 C CG . ASN B 2 107 ? 42.835 123.193 37.798 1.00 27.58 ? 107 ASN B CG 1 ATOM 2740 O OD1 . ASN B 2 107 ? 43.655 124.046 37.492 1.00 32.05 ? 107 ASN B OD1 1 ATOM 2741 N ND2 . ASN B 2 107 ? 43.180 122.052 38.368 1.00 27.86 ? 107 ASN B ND2 1 ATOM 2742 N N . ALA B 2 108 ? 38.453 122.455 35.929 1.00 25.79 ? 108 ALA B N 1 ATOM 2743 C CA . ALA B 2 108 ? 36.990 122.334 35.861 1.00 25.82 ? 108 ALA B CA 1 ATOM 2744 C C . ALA B 2 108 ? 36.628 121.411 34.707 1.00 25.59 ? 108 ALA B C 1 ATOM 2745 O O . ALA B 2 108 ? 37.476 121.076 33.884 1.00 25.90 ? 108 ALA B O 1 ATOM 2746 C CB . ALA B 2 108 ? 36.331 123.694 35.668 1.00 26.06 ? 108 ALA B CB 1 ATOM 2747 N N . ALA B 2 109 ? 35.363 121.014 34.659 1.00 25.91 ? 109 ALA B N 1 ATOM 2748 C CA . ALA B 2 109 ? 34.862 120.085 33.658 1.00 26.91 ? 109 ALA B CA 1 ATOM 2749 C C . ALA B 2 109 ? 34.174 120.747 32.457 1.00 26.92 ? 109 ALA B C 1 ATOM 2750 O O . ALA B 2 109 ? 33.783 120.055 31.528 1.00 26.53 ? 109 ALA B O 1 ATOM 2751 C CB . ALA B 2 109 ? 33.890 119.124 34.321 1.00 27.72 ? 109 ALA B CB 1 ATOM 2752 N N . THR B 2 110 ? 34.026 122.071 32.472 1.00 27.66 ? 110 THR B N 1 ATOM 2753 C CA . THR B 2 110 ? 33.159 122.764 31.518 1.00 27.77 ? 110 THR B CA 1 ATOM 2754 C C . THR B 2 110 ? 33.914 123.219 30.271 1.00 27.31 ? 110 THR B C 1 ATOM 2755 O O . THR B 2 110 ? 35.157 123.388 30.290 1.00 25.47 ? 110 THR B O 1 ATOM 2756 C CB . THR B 2 110 ? 32.510 123.994 32.173 1.00 29.20 ? 110 THR B CB 1 ATOM 2757 O OG1 . THR B 2 110 ? 33.514 124.756 32.849 1.00 29.10 ? 110 THR B OG1 1 ATOM 2758 C CG2 . THR B 2 110 ? 31.442 123.555 33.174 1.00 30.56 ? 110 THR B CG2 1 ATOM 2759 N N . SER B 2 111 ? 33.158 123.434 29.194 1.00 25.33 ? 111 SER B N 1 ATOM 2760 C CA . SER B 2 111 ? 33.732 123.933 27.956 1.00 25.68 ? 111 SER B CA 1 ATOM 2761 C C . SER B 2 111 ? 34.410 125.287 28.177 1.00 25.55 ? 111 SER B C 1 ATOM 2762 O O . SER B 2 111 ? 33.956 126.104 28.973 1.00 25.93 ? 111 SER B O 1 ATOM 2763 C CB . SER B 2 111 ? 32.683 124.043 26.859 1.00 26.89 ? 111 SER B CB 1 ATOM 2764 O OG . SER B 2 111 ? 33.246 124.663 25.709 1.00 27.03 ? 111 SER B OG 1 ATOM 2765 N N . ARG B 2 112 ? 35.541 125.462 27.508 1.00 25.58 ? 112 ARG B N 1 ATOM 2766 C CA . ARG B 2 112 ? 36.410 126.633 27.625 1.00 26.22 ? 112 ARG B CA 1 ATOM 2767 C C . ARG B 2 112 ? 37.193 126.772 28.919 1.00 25.76 ? 112 ARG B C 1 ATOM 2768 O O . ARG B 2 112 ? 37.872 127.781 29.118 1.00 26.32 ? 112 ARG B O 1 ATOM 2769 C CB . ARG B 2 112 ? 35.660 127.927 27.272 1.00 26.83 ? 112 ARG B CB 1 ATOM 2770 C CG . ARG B 2 112 ? 35.321 127.967 25.796 1.00 27.64 ? 112 ARG B CG 1 ATOM 2771 C CD . ARG B 2 112 ? 34.184 128.904 25.468 1.00 28.70 ? 112 ARG B CD 1 ATOM 2772 N NE . ARG B 2 112 ? 34.581 130.305 25.556 1.00 28.26 ? 112 ARG B NE 1 ATOM 2773 C CZ . ARG B 2 112 ? 33.951 131.316 24.955 1.00 27.97 ? 112 ARG B CZ 1 ATOM 2774 N NH1 . ARG B 2 112 ? 32.873 131.106 24.186 1.00 26.48 ? 112 ARG B NH1 1 ATOM 2775 N NH2 . ARG B 2 112 ? 34.409 132.553 25.126 1.00 26.83 ? 112 ARG B NH2 1 ATOM 2776 N N . THR B 2 113 ? 37.158 125.749 29.768 1.00 26.23 ? 113 THR B N 1 ATOM 2777 C CA . THR B 2 113 ? 38.101 125.649 30.885 1.00 26.15 ? 113 THR B CA 1 ATOM 2778 C C . THR B 2 113 ? 39.534 125.662 30.350 1.00 26.42 ? 113 THR B C 1 ATOM 2779 O O . THR B 2 113 ? 39.864 124.870 29.472 1.00 27.21 ? 113 THR B O 1 ATOM 2780 C CB . THR B 2 113 ? 37.925 124.321 31.653 1.00 25.19 ? 113 THR B CB 1 ATOM 2781 O OG1 . THR B 2 113 ? 36.616 124.252 32.221 1.00 24.95 ? 113 THR B OG1 1 ATOM 2782 C CG2 . THR B 2 113 ? 38.943 124.202 32.756 1.00 25.02 ? 113 THR B CG2 1 ATOM 2783 N N . ASN B 2 114 ? 40.374 126.536 30.895 1.00 26.16 ? 114 ASN B N 1 ATOM 2784 C CA . ASN B 2 114 ? 41.801 126.519 30.615 1.00 26.59 ? 114 ASN B CA 1 ATOM 2785 C C . ASN B 2 114 ? 42.465 125.264 31.161 1.00 26.86 ? 114 ASN B C 1 ATOM 2786 O O . ASN B 2 114 ? 42.237 124.906 32.312 1.00 26.77 ? 114 ASN B O 1 ATOM 2787 C CB . ASN B 2 114 ? 42.480 127.690 31.292 1.00 28.40 ? 114 ASN B CB 1 ATOM 2788 C CG . ASN B 2 114 ? 42.135 129.024 30.667 1.00 31.42 ? 114 ASN B CG 1 ATOM 2789 O OD1 . ASN B 2 114 ? 41.559 129.114 29.576 1.00 31.03 ? 114 ASN B OD1 1 ATOM 2790 N ND2 . ASN B 2 114 ? 42.509 130.079 31.372 1.00 35.55 ? 114 ASN B ND2 1 ATOM 2791 N N . LEU B 2 115 ? 43.292 124.615 30.351 1.00 24.82 ? 115 LEU B N 1 ATOM 2792 C CA . LEU B 2 115 ? 44.099 123.505 30.834 1.00 25.72 ? 115 LEU B CA 1 ATOM 2793 C C . LEU B 2 115 ? 45.406 124.040 31.412 1.00 25.78 ? 115 LEU B C 1 ATOM 2794 O O . LEU B 2 115 ? 46.009 124.951 30.846 1.00 25.98 ? 115 LEU B O 1 ATOM 2795 C CB . LEU B 2 115 ? 44.399 122.506 29.715 1.00 25.24 ? 115 LEU B CB 1 ATOM 2796 C CG . LEU B 2 115 ? 43.219 121.931 28.924 1.00 24.93 ? 115 LEU B CG 1 ATOM 2797 C CD1 . LEU B 2 115 ? 43.695 120.787 28.034 1.00 25.31 ? 115 LEU B CD1 1 ATOM 2798 C CD2 . LEU B 2 115 ? 42.112 121.451 29.846 1.00 25.16 ? 115 LEU B CD2 1 ATOM 2799 N N . THR B 2 116 ? 45.842 123.454 32.521 1.00 25.89 ? 116 THR B N 1 ATOM 2800 C CA . THR B 2 116 ? 47.024 123.916 33.232 1.00 27.72 ? 116 THR B CA 1 ATOM 2801 C C . THR B 2 116 ? 48.043 122.798 33.473 1.00 28.27 ? 116 THR B C 1 ATOM 2802 O O . THR B 2 116 ? 47.720 121.603 33.390 1.00 27.21 ? 116 THR B O 1 ATOM 2803 C CB . THR B 2 116 ? 46.640 124.607 34.571 1.00 27.94 ? 116 THR B CB 1 ATOM 2804 O OG1 . THR B 2 116 ? 45.770 123.771 35.334 1.00 27.58 ? 116 THR B OG1 1 ATOM 2805 C CG2 . THR B 2 116 ? 45.921 125.921 34.297 1.00 27.82 ? 116 THR B CG2 1 ATOM 2806 N N . GLY B 2 117 ? 49.284 123.217 33.712 1.00 29.27 ? 117 GLY B N 1 ATOM 2807 C CA . GLY B 2 117 ? 50.362 122.325 34.116 1.00 30.15 ? 117 GLY B CA 1 ATOM 2808 C C . GLY B 2 117 ? 50.382 122.329 35.630 1.00 31.54 ? 117 GLY B C 1 ATOM 2809 O O . GLY B 2 117 ? 50.563 123.381 36.236 1.00 31.25 ? 117 GLY B O 1 ATOM 2810 N N . GLU B 2 118 ? 50.168 121.166 36.240 1.00 32.95 ? 118 GLU B N 1 ATOM 2811 C CA . GLU B 2 118 ? 50.048 121.055 37.690 1.00 34.53 ? 118 GLU B CA 1 ATOM 2812 C C . GLU B 2 118 ? 50.887 119.903 38.192 1.00 35.42 ? 118 GLU B C 1 ATOM 2813 O O . GLU B 2 118 ? 51.372 119.086 37.400 1.00 36.41 ? 118 GLU B O 1 ATOM 2814 C CB . GLU B 2 118 ? 48.588 120.800 38.085 1.00 36.75 ? 118 GLU B CB 1 ATOM 2815 C CG . GLU B 2 118 ? 47.555 121.778 37.527 1.00 37.45 ? 118 GLU B CG 1 ATOM 2816 C CD . GLU B 2 118 ? 47.572 123.143 38.203 1.00 39.29 ? 118 GLU B CD 1 ATOM 2817 O OE1 . GLU B 2 118 ? 48.509 123.430 38.985 1.00 39.36 ? 118 GLU B OE1 1 ATOM 2818 O OE2 . GLU B 2 118 ? 46.634 123.934 37.944 1.00 39.99 ? 118 GLU B OE2 1 ATOM 2819 N N . ASN B 2 119 ? 51.042 119.828 39.514 1.00 35.18 ? 119 ASN B N 1 ATOM 2820 C CA . ASN B 2 119 ? 51.713 118.689 40.140 1.00 33.65 ? 119 ASN B CA 1 ATOM 2821 C C . ASN B 2 119 ? 50.815 117.486 40.009 1.00 32.75 ? 119 ASN B C 1 ATOM 2822 O O . ASN B 2 119 ? 49.609 117.585 40.251 1.00 33.41 ? 119 ASN B O 1 ATOM 2823 C CB . ASN B 2 119 ? 51.998 118.944 41.618 1.00 34.36 ? 119 ASN B CB 1 ATOM 2824 C CG . ASN B 2 119 ? 52.875 120.150 41.832 1.00 35.58 ? 119 ASN B CG 1 ATOM 2825 O OD1 . ASN B 2 119 ? 52.517 121.057 42.569 1.00 38.30 ? 119 ASN B OD1 1 ATOM 2826 N ND2 . ASN B 2 119 ? 54.014 120.184 41.159 1.00 36.21 ? 119 ASN B ND2 1 ATOM 2827 N N . ASN B 2 120 ? 51.397 116.357 39.619 1.00 32.18 ? 120 ASN B N 1 ATOM 2828 C CA . ASN B 2 120 ? 50.633 115.133 39.436 1.00 30.77 ? 120 ASN B CA 1 ATOM 2829 C C . ASN B 2 120 ? 50.212 114.547 40.758 1.00 29.77 ? 120 ASN B C 1 ATOM 2830 O O . ASN B 2 120 ? 51.046 114.221 41.579 1.00 30.84 ? 120 ASN B O 1 ATOM 2831 C CB . ASN B 2 120 ? 51.431 114.075 38.675 1.00 29.83 ? 120 ASN B CB 1 ATOM 2832 C CG . ASN B 2 120 ? 50.595 112.845 38.346 1.00 30.25 ? 120 ASN B CG 1 ATOM 2833 O OD1 . ASN B 2 120 ? 49.391 112.943 38.054 1.00 30.02 ? 120 ASN B OD1 1 ATOM 2834 N ND2 . ASN B 2 120 ? 51.220 111.683 38.403 1.00 29.99 ? 120 ASN B ND2 1 ATOM 2835 N N . VAL B 2 121 ? 48.909 114.409 40.935 1.00 30.43 ? 121 VAL B N 1 ATOM 2836 C CA . VAL B 2 121 ? 48.339 113.677 42.045 1.00 29.91 ? 121 VAL B CA 1 ATOM 2837 C C . VAL B 2 121 ? 47.521 112.479 41.559 1.00 29.69 ? 121 VAL B C 1 ATOM 2838 O O . VAL B 2 121 ? 46.800 111.870 42.351 1.00 29.87 ? 121 VAL B O 1 ATOM 2839 C CB . VAL B 2 121 ? 47.491 114.607 42.944 1.00 31.82 ? 121 VAL B CB 1 ATOM 2840 C CG1 . VAL B 2 121 ? 48.374 115.710 43.527 1.00 32.07 ? 121 VAL B CG1 1 ATOM 2841 C CG2 . VAL B 2 121 ? 46.301 115.211 42.191 1.00 32.73 ? 121 VAL B CG2 1 ATOM 2842 N N . PHE B 2 122 ? 47.639 112.131 40.272 1.00 28.54 ? 122 PHE B N 1 ATOM 2843 C CA . PHE B 2 122 ? 46.861 111.038 39.660 1.00 27.58 ? 122 PHE B CA 1 ATOM 2844 C C . PHE B 2 122 ? 45.336 111.230 39.747 1.00 25.70 ? 122 PHE B C 1 ATOM 2845 O O . PHE B 2 122 ? 44.584 110.262 39.831 1.00 25.35 ? 122 PHE B O 1 ATOM 2846 C CB . PHE B 2 122 ? 47.275 109.677 40.241 1.00 29.12 ? 122 PHE B CB 1 ATOM 2847 C CG . PHE B 2 122 ? 48.734 109.343 40.045 1.00 29.59 ? 122 PHE B CG 1 ATOM 2848 C CD1 . PHE B 2 122 ? 49.172 108.741 38.862 1.00 29.94 ? 122 PHE B CD1 1 ATOM 2849 C CD2 . PHE B 2 122 ? 49.669 109.617 41.041 1.00 29.97 ? 122 PHE B CD2 1 ATOM 2850 C CE1 . PHE B 2 122 ? 50.514 108.426 38.670 1.00 29.18 ? 122 PHE B CE1 1 ATOM 2851 C CE2 . PHE B 2 122 ? 51.011 109.300 40.857 1.00 29.61 ? 122 PHE B CE2 1 ATOM 2852 C CZ . PHE B 2 122 ? 51.434 108.702 39.673 1.00 29.60 ? 122 PHE B CZ 1 ATOM 2853 N N . ALA B 2 123 ? 44.884 112.482 39.697 1.00 23.98 ? 123 ALA B N 1 ATOM 2854 C CA . ALA B 2 123 ? 43.453 112.783 39.696 1.00 22.76 ? 123 ALA B CA 1 ATOM 2855 C C . ALA B 2 123 ? 42.865 112.416 38.336 1.00 22.22 ? 123 ALA B C 1 ATOM 2856 O O . ALA B 2 123 ? 43.586 112.351 37.348 1.00 21.68 ? 123 ALA B O 1 ATOM 2857 C CB . ALA B 2 123 ? 43.216 114.262 39.998 1.00 22.40 ? 123 ALA B CB 1 ATOM 2858 N N . ALA B 2 124 ? 41.560 112.188 38.288 1.00 22.16 ? 124 ALA B N 1 ATOM 2859 C CA . ALA B 2 124 ? 40.869 111.918 37.023 1.00 22.28 ? 124 ALA B CA 1 ATOM 2860 C C . ALA B 2 124 ? 40.991 113.088 36.052 1.00 22.85 ? 124 ALA B C 1 ATOM 2861 O O . ALA B 2 124 ? 41.128 112.895 34.840 1.00 22.38 ? 124 ALA B O 1 ATOM 2862 C CB . ALA B 2 124 ? 39.413 111.591 37.279 1.00 22.16 ? 124 ALA B CB 1 ATOM 2863 N N . LYS B 2 125 ? 40.990 114.297 36.606 1.00 23.14 ? 125 LYS B N 1 ATOM 2864 C CA . LYS B 2 125 ? 41.206 115.527 35.838 1.00 23.86 ? 125 LYS B CA 1 ATOM 2865 C C . LYS B 2 125 ? 42.617 115.679 35.281 1.00 23.22 ? 125 LYS B C 1 ATOM 2866 O O . LYS B 2 125 ? 42.935 116.711 34.681 1.00 22.08 ? 125 LYS B O 1 ATOM 2867 C CB . LYS B 2 125 ? 40.860 116.750 36.698 1.00 25.18 ? 125 LYS B CB 1 ATOM 2868 C CG . LYS B 2 125 ? 41.808 117.033 37.864 1.00 26.32 ? 125 LYS B CG 1 ATOM 2869 C CD . LYS B 2 125 ? 41.226 118.095 38.786 1.00 27.74 ? 125 LYS B CD 1 ATOM 2870 C CE . LYS B 2 125 ? 42.258 118.677 39.741 1.00 28.51 ? 125 LYS B CE 1 ATOM 2871 N NZ . LYS B 2 125 ? 41.657 119.770 40.562 1.00 29.86 ? 125 LYS B NZ 1 ATOM 2872 N N . GLN B 2 126 ? 43.463 114.676 35.520 1.00 23.25 ? 126 GLN B N 1 ATOM 2873 C CA . GLN B 2 126 ? 44.811 114.595 34.986 1.00 23.03 ? 126 GLN B CA 1 ATOM 2874 C C . GLN B 2 126 ? 44.996 113.341 34.114 1.00 22.89 ? 126 GLN B C 1 ATOM 2875 O O . GLN B 2 126 ? 46.123 113.003 33.765 1.00 23.47 ? 126 GLN B O 1 ATOM 2876 C CB . GLN B 2 126 ? 45.795 114.586 36.146 1.00 23.57 ? 126 GLN B CB 1 ATOM 2877 C CG . GLN B 2 126 ? 45.630 115.772 37.085 1.00 24.20 ? 126 GLN B CG 1 ATOM 2878 C CD . GLN B 2 126 ? 46.694 115.829 38.182 1.00 24.87 ? 126 GLN B CD 1 ATOM 2879 O OE1 . GLN B 2 126 ? 46.828 114.894 38.988 1.00 24.89 ? 126 GLN B OE1 1 ATOM 2880 N NE2 . GLN B 2 126 ? 47.437 116.945 38.238 1.00 24.67 ? 126 GLN B NE2 1 ATOM 2881 N N . ALA B 2 127 ? 43.883 112.686 33.750 1.00 22.02 ? 127 ALA B N 1 ATOM 2882 C CA . ALA B 2 127 ? 43.872 111.484 32.923 1.00 20.44 ? 127 ALA B CA 1 ATOM 2883 C C . ALA B 2 127 ? 43.337 111.854 31.552 1.00 20.29 ? 127 ALA B C 1 ATOM 2884 O O . ALA B 2 127 ? 42.318 112.538 31.449 1.00 18.88 ? 127 ALA B O 1 ATOM 2885 C CB . ALA B 2 127 ? 42.978 110.428 33.541 1.00 20.29 ? 127 ALA B CB 1 ATOM 2886 N N . TRP B 2 128 ? 44.025 111.381 30.513 1.00 20.66 ? 128 TRP B N 1 ATOM 2887 C CA . TRP B 2 128 ? 43.735 111.711 29.115 1.00 20.79 ? 128 TRP B CA 1 ATOM 2888 C C . TRP B 2 128 ? 43.769 110.455 28.241 1.00 20.97 ? 128 TRP B C 1 ATOM 2889 O O . TRP B 2 128 ? 44.619 109.589 28.446 1.00 21.32 ? 128 TRP B O 1 ATOM 2890 C CB . TRP B 2 128 ? 44.774 112.710 28.601 1.00 21.15 ? 128 TRP B CB 1 ATOM 2891 C CG . TRP B 2 128 ? 44.812 113.932 29.450 1.00 21.56 ? 128 TRP B CG 1 ATOM 2892 C CD1 . TRP B 2 128 ? 45.616 114.158 30.522 1.00 22.26 ? 128 TRP B CD1 1 ATOM 2893 C CD2 . TRP B 2 128 ? 43.947 115.050 29.349 1.00 21.32 ? 128 TRP B CD2 1 ATOM 2894 N NE1 . TRP B 2 128 ? 45.331 115.371 31.079 1.00 22.27 ? 128 TRP B NE1 1 ATOM 2895 C CE2 . TRP B 2 128 ? 44.303 115.944 30.381 1.00 22.00 ? 128 TRP B CE2 1 ATOM 2896 C CE3 . TRP B 2 128 ? 42.915 115.398 28.474 1.00 20.82 ? 128 TRP B CE3 1 ATOM 2897 C CZ2 . TRP B 2 128 ? 43.658 117.164 30.567 1.00 21.19 ? 128 TRP B CZ2 1 ATOM 2898 C CZ3 . TRP B 2 128 ? 42.272 116.608 28.653 1.00 21.21 ? 128 TRP B CZ3 1 ATOM 2899 C CH2 . TRP B 2 128 ? 42.646 117.481 29.690 1.00 21.47 ? 128 TRP B CH2 1 ATOM 2900 N N . ARG B 2 129 ? 42.844 110.373 27.280 1.00 20.50 ? 129 ARG B N 1 ATOM 2901 C CA . ARG B 2 129 ? 42.903 109.391 26.223 1.00 20.75 ? 129 ARG B CA 1 ATOM 2902 C C . ARG B 2 129 ? 43.445 110.061 24.962 1.00 20.83 ? 129 ARG B C 1 ATOM 2903 O O . ARG B 2 129 ? 42.784 110.913 24.375 1.00 21.68 ? 129 ARG B O 1 ATOM 2904 C CB . ARG B 2 129 ? 41.524 108.800 25.939 1.00 21.17 ? 129 ARG B CB 1 ATOM 2905 C CG . ARG B 2 129 ? 41.554 107.668 24.905 1.00 20.91 ? 129 ARG B CG 1 ATOM 2906 C CD . ARG B 2 129 ? 40.184 107.348 24.350 1.00 21.20 ? 129 ARG B CD 1 ATOM 2907 N NE . ARG B 2 129 ? 39.276 106.850 25.370 1.00 21.38 ? 129 ARG B NE 1 ATOM 2908 C CZ . ARG B 2 129 ? 37.965 106.707 25.213 1.00 21.51 ? 129 ARG B CZ 1 ATOM 2909 N NH1 . ARG B 2 129 ? 37.372 107.011 24.063 1.00 22.59 ? 129 ARG B NH1 1 ATOM 2910 N NH2 . ARG B 2 129 ? 37.232 106.259 26.218 1.00 21.62 ? 129 ARG B NH2 1 ATOM 2911 N N . ILE B 2 130 ? 44.647 109.678 24.550 1.00 20.59 ? 130 ILE B N 1 ATOM 2912 C CA . ILE B 2 130 ? 45.174 110.080 23.254 1.00 20.00 ? 130 ILE B CA 1 ATOM 2913 C C . ILE B 2 130 ? 44.585 109.104 22.274 1.00 20.48 ? 130 ILE B C 1 ATOM 2914 O O . ILE B 2 130 ? 44.839 107.907 22.347 1.00 19.36 ? 130 ILE B O 1 ATOM 2915 C CB . ILE B 2 130 ? 46.699 110.037 23.193 1.00 19.88 ? 130 ILE B CB 1 ATOM 2916 C CG1 . ILE B 2 130 ? 47.247 111.042 24.189 1.00 20.00 ? 130 ILE B CG1 1 ATOM 2917 C CG2 . ILE B 2 130 ? 47.195 110.339 21.769 1.00 19.85 ? 130 ILE B CG2 1 ATOM 2918 C CD1 . ILE B 2 130 ? 48.726 110.956 24.422 1.00 20.72 ? 130 ILE B CD1 1 ATOM 2919 N N . GLY B 2 131 ? 43.759 109.598 21.387 1.00 21.06 ? 131 GLY B N 1 ATOM 2920 C CA . GLY B 2 131 ? 43.110 108.761 20.425 1.00 22.25 ? 131 GLY B CA 1 ATOM 2921 C C . GLY B 2 131 ? 42.091 109.465 19.595 1.00 22.50 ? 131 GLY B C 1 ATOM 2922 O O . GLY B 2 131 ? 41.550 110.392 20.016 1.00 23.26 ? 131 GLY B O 1 ATOM 2923 N N . ASN B 2 132 ? 41.861 109.002 18.384 1.00 23.16 ? 132 ASN B N 1 ATOM 2924 C CA . ASN B 2 132 ? 40.893 109.613 17.520 1.00 23.94 ? 132 ASN B CA 1 ATOM 2925 C C . ASN B 2 132 ? 39.476 109.373 17.988 1.00 22.66 ? 132 ASN B C 1 ATOM 2926 O O . ASN B 2 132 ? 38.666 110.206 17.871 1.00 24.01 ? 132 ASN B O 1 ATOM 2927 C CB . ASN B 2 132 ? 41.088 109.167 16.088 1.00 26.30 ? 132 ASN B CB 1 ATOM 2928 C CG . ASN B 2 132 ? 41.146 110.318 15.152 1.00 29.62 ? 132 ASN B CG 1 ATOM 2929 O OD1 . ASN B 2 132 ? 40.297 111.156 15.171 1.00 32.36 ? 132 ASN B OD1 1 ATOM 2930 N ND2 . ASN B 2 132 ? 42.163 110.370 14.350 1.00 32.46 ? 132 ASN B ND2 1 ATOM 2931 N N . TYR B 2 133 ? 39.207 108.207 18.508 1.00 21.13 ? 133 TYR B N 1 ATOM 2932 C CA . TYR B 2 133 ? 37.898 107.840 19.020 1.00 21.06 ? 133 TYR B CA 1 ATOM 2933 C C . TYR B 2 133 ? 37.720 108.325 20.465 1.00 20.97 ? 133 TYR B C 1 ATOM 2934 O O . TYR B 2 133 ? 38.355 107.802 21.381 1.00 21.29 ? 133 TYR B O 1 ATOM 2935 C CB . TYR B 2 133 ? 37.723 106.331 18.931 1.00 21.04 ? 133 TYR B CB 1 ATOM 2936 C CG . TYR B 2 133 ? 36.358 105.862 19.316 1.00 20.62 ? 133 TYR B CG 1 ATOM 2937 C CD1 . TYR B 2 133 ? 35.337 105.836 18.391 1.00 20.64 ? 133 TYR B CD1 1 ATOM 2938 C CD2 . TYR B 2 133 ? 36.088 105.427 20.608 1.00 21.00 ? 133 TYR B CD2 1 ATOM 2939 C CE1 . TYR B 2 133 ? 34.075 105.382 18.729 1.00 20.89 ? 133 TYR B CE1 1 ATOM 2940 C CE2 . TYR B 2 133 ? 34.816 104.979 20.962 1.00 20.80 ? 133 TYR B CE2 1 ATOM 2941 C CZ . TYR B 2 133 ? 33.819 104.961 20.013 1.00 20.46 ? 133 TYR B CZ 1 ATOM 2942 O OH . TYR B 2 133 ? 32.563 104.528 20.330 1.00 20.22 ? 133 TYR B OH 1 ATOM 2943 N N . VAL B 2 134 ? 36.835 109.305 20.651 1.00 20.65 ? 134 VAL B N 1 ATOM 2944 C CA . VAL B 2 134 ? 36.709 110.023 21.930 1.00 21.04 ? 134 VAL B CA 1 ATOM 2945 C C . VAL B 2 134 ? 35.503 109.605 22.766 1.00 21.29 ? 134 VAL B C 1 ATOM 2946 O O . VAL B 2 134 ? 35.338 110.101 23.865 1.00 20.26 ? 134 VAL B O 1 ATOM 2947 C CB . VAL B 2 134 ? 36.675 111.560 21.719 1.00 21.05 ? 134 VAL B CB 1 ATOM 2948 C CG1 . VAL B 2 134 ? 37.855 111.994 20.871 1.00 20.85 ? 134 VAL B CG1 1 ATOM 2949 C CG2 . VAL B 2 134 ? 35.358 112.025 21.098 1.00 21.33 ? 134 VAL B CG2 1 ATOM 2950 N N . GLU B 2 135 ? 34.690 108.673 22.264 1.00 22.88 ? 135 GLU B N 1 ATOM 2951 C CA . GLU B 2 135 ? 33.434 108.323 22.920 1.00 25.03 ? 135 GLU B CA 1 ATOM 2952 C C . GLU B 2 135 ? 33.653 107.477 24.169 1.00 24.99 ? 135 GLU B C 1 ATOM 2953 O O . GLU B 2 135 ? 34.607 106.708 24.233 1.00 25.06 ? 135 GLU B O 1 ATOM 2954 C CB . GLU B 2 135 ? 32.512 107.513 22.013 1.00 26.81 ? 135 GLU B CB 1 ATOM 2955 C CG . GLU B 2 135 ? 32.266 108.073 20.622 1.00 29.47 ? 135 GLU B CG 1 ATOM 2956 C CD . GLU B 2 135 ? 31.745 109.493 20.644 1.00 31.14 ? 135 GLU B CD 1 ATOM 2957 O OE1 . GLU B 2 135 ? 31.012 109.837 21.600 1.00 33.17 ? 135 GLU B OE1 1 ATOM 2958 O OE2 . GLU B 2 135 ? 32.071 110.259 19.705 1.00 34.55 ? 135 GLU B OE2 1 ATOM 2959 N N . PRO B 2 136 ? 32.747 107.602 25.148 1.00 24.75 ? 136 PRO B N 1 ATOM 2960 C CA . PRO B 2 136 ? 32.742 106.639 26.229 1.00 24.88 ? 136 PRO B CA 1 ATOM 2961 C C . PRO B 2 136 ? 32.475 105.232 25.696 1.00 24.41 ? 136 PRO B C 1 ATOM 2962 O O . PRO B 2 136 ? 31.635 105.059 24.822 1.00 25.15 ? 136 PRO B O 1 ATOM 2963 C CB . PRO B 2 136 ? 31.586 107.104 27.123 1.00 25.09 ? 136 PRO B CB 1 ATOM 2964 C CG . PRO B 2 136 ? 31.463 108.557 26.853 1.00 25.82 ? 136 PRO B CG 1 ATOM 2965 C CD . PRO B 2 136 ? 31.830 108.731 25.408 1.00 25.14 ? 136 PRO B CD 1 ATOM 2966 N N . ILE B 2 137 ? 33.202 104.255 26.229 1.00 22.74 ? 137 ILE B N 1 ATOM 2967 C CA . ILE B 2 137 ? 33.091 102.868 25.816 1.00 21.22 ? 137 ILE B CA 1 ATOM 2968 C C . ILE B 2 137 ? 32.143 102.165 26.779 1.00 20.42 ? 137 ILE B C 1 ATOM 2969 O O . ILE B 2 137 ? 32.430 102.021 27.968 1.00 19.69 ? 137 ILE B O 1 ATOM 2970 C CB . ILE B 2 137 ? 34.483 102.214 25.772 1.00 21.39 ? 137 ILE B CB 1 ATOM 2971 C CG1 . ILE B 2 137 ? 35.270 102.817 24.605 1.00 22.29 ? 137 ILE B CG1 1 ATOM 2972 C CG2 . ILE B 2 137 ? 34.395 100.700 25.611 1.00 21.64 ? 137 ILE B CG2 1 ATOM 2973 C CD1 . ILE B 2 137 ? 36.769 102.721 24.763 1.00 23.28 ? 137 ILE B CD1 1 ATOM 2974 N N . VAL B 2 138 ? 31.016 101.720 26.250 1.00 20.26 ? 138 VAL B N 1 ATOM 2975 C CA . VAL B 2 138 ? 29.988 101.084 27.054 1.00 20.84 ? 138 VAL B CA 1 ATOM 2976 C C . VAL B 2 138 ? 30.386 99.626 27.260 1.00 21.39 ? 138 VAL B C 1 ATOM 2977 O O . VAL B 2 138 ? 30.719 98.933 26.320 1.00 20.94 ? 138 VAL B O 1 ATOM 2978 C CB . VAL B 2 138 ? 28.617 101.236 26.383 1.00 20.92 ? 138 VAL B CB 1 ATOM 2979 C CG1 . VAL B 2 138 ? 27.511 100.615 27.222 1.00 20.88 ? 138 VAL B CG1 1 ATOM 2980 C CG2 . VAL B 2 138 ? 28.350 102.720 26.133 1.00 20.88 ? 138 VAL B CG2 1 ATOM 2981 N N . THR B 2 139 ? 30.387 99.174 28.502 1.00 22.38 ? 139 THR B N 1 ATOM 2982 C CA . THR B 2 139 ? 30.833 97.814 28.791 1.00 23.68 ? 139 THR B CA 1 ATOM 2983 C C . THR B 2 139 ? 30.155 97.231 30.013 1.00 22.57 ? 139 THR B C 1 ATOM 2984 O O . THR B 2 139 ? 29.516 97.953 30.778 1.00 21.34 ? 139 THR B O 1 ATOM 2985 C CB . THR B 2 139 ? 32.364 97.777 29.009 1.00 25.50 ? 139 THR B CB 1 ATOM 2986 O OG1 . THR B 2 139 ? 32.807 96.416 29.012 1.00 28.53 ? 139 THR B OG1 1 ATOM 2987 C CG2 . THR B 2 139 ? 32.781 98.456 30.342 1.00 25.46 ? 139 THR B CG2 1 ATOM 2988 N N . THR B 2 140 ? 30.291 95.913 30.166 1.00 21.83 ? 140 THR B N 1 ATOM 2989 C CA . THR B 2 140 ? 30.089 95.254 31.445 1.00 20.82 ? 140 THR B CA 1 ATOM 2990 C C . THR B 2 140 ? 31.462 94.979 32.031 1.00 20.28 ? 140 THR B C 1 ATOM 2991 O O . THR B 2 140 ? 32.459 94.913 31.310 1.00 19.31 ? 140 THR B O 1 ATOM 2992 C CB . THR B 2 140 ? 29.242 93.955 31.353 1.00 21.37 ? 140 THR B CB 1 ATOM 2993 O OG1 . THR B 2 140 ? 29.877 92.981 30.514 1.00 21.37 ? 140 THR B OG1 1 ATOM 2994 C CG2 . THR B 2 140 ? 27.876 94.256 30.808 1.00 21.98 ? 140 THR B CG2 1 ATOM 2995 N N . ILE B 2 141 ? 31.503 94.856 33.355 1.00 20.38 ? 141 ILE B N 1 ATOM 2996 C CA . ILE B 2 141 ? 32.748 94.650 34.098 1.00 20.46 ? 141 ILE B CA 1 ATOM 2997 C C . ILE B 2 141 ? 32.526 93.374 34.888 1.00 21.47 ? 141 ILE B C 1 ATOM 2998 O O . ILE B 2 141 ? 31.659 93.328 35.767 1.00 21.77 ? 141 ILE B O 1 ATOM 2999 C CB . ILE B 2 141 ? 33.106 95.856 34.991 1.00 20.29 ? 141 ILE B CB 1 ATOM 3000 C CG1 . ILE B 2 141 ? 33.439 97.071 34.118 1.00 19.59 ? 141 ILE B CG1 1 ATOM 3001 C CG2 . ILE B 2 141 ? 34.280 95.537 35.913 1.00 20.75 ? 141 ILE B CG2 1 ATOM 3002 C CD1 . ILE B 2 141 ? 33.509 98.390 34.860 1.00 19.87 ? 141 ILE B CD1 1 ATOM 3003 N N . ILE B 2 142 ? 33.270 92.332 34.512 1.00 22.14 ? 142 ILE B N 1 ATOM 3004 C CA . ILE B 2 142 ? 33.072 90.988 35.044 1.00 22.19 ? 142 ILE B CA 1 ATOM 3005 C C . ILE B 2 142 ? 34.147 90.712 36.087 1.00 22.08 ? 142 ILE B C 1 ATOM 3006 O O . ILE B 2 142 ? 35.330 90.970 35.858 1.00 21.86 ? 142 ILE B O 1 ATOM 3007 C CB . ILE B 2 142 ? 33.193 89.870 33.987 1.00 23.02 ? 142 ILE B CB 1 ATOM 3008 C CG1 . ILE B 2 142 ? 32.589 90.254 32.617 1.00 24.04 ? 142 ILE B CG1 1 ATOM 3009 C CG2 . ILE B 2 142 ? 32.557 88.587 34.516 1.00 22.83 ? 142 ILE B CG2 1 ATOM 3010 C CD1 . ILE B 2 142 ? 31.099 90.496 32.620 1.00 24.55 ? 142 ILE B CD1 1 ATOM 3011 N N . GLY B 2 143 ? 33.738 90.154 37.220 1.00 22.46 ? 143 GLY B N 1 ATOM 3012 C CA . GLY B 2 143 ? 34.667 89.854 38.291 1.00 22.51 ? 143 GLY B CA 1 ATOM 3013 C C . GLY B 2 143 ? 34.535 88.426 38.765 1.00 22.83 ? 143 GLY B C 1 ATOM 3014 O O . GLY B 2 143 ? 34.162 87.526 37.995 1.00 20.54 ? 143 GLY B O 1 ATOM 3015 N N . LEU B 2 144 ? 34.831 88.257 40.061 1.00 23.96 ? 144 LEU B N 1 ATOM 3016 C CA . LEU B 2 144 ? 34.880 86.963 40.738 1.00 23.88 ? 144 LEU B CA 1 ATOM 3017 C C . LEU B 2 144 ? 33.566 86.203 40.574 1.00 24.65 ? 144 LEU B C 1 ATOM 3018 O O . LEU B 2 144 ? 32.489 86.798 40.583 1.00 24.72 ? 144 LEU B O 1 ATOM 3019 C CB . LEU B 2 144 ? 35.210 87.167 42.237 1.00 23.14 ? 144 LEU B CB 1 ATOM 3020 C CG . LEU B 2 144 ? 35.607 85.963 43.100 1.00 22.41 ? 144 LEU B CG 1 ATOM 3021 C CD1 . LEU B 2 144 ? 36.957 85.423 42.676 1.00 22.52 ? 144 LEU B CD1 1 ATOM 3022 C CD2 . LEU B 2 144 ? 35.677 86.359 44.568 1.00 22.73 ? 144 LEU B CD2 1 ATOM 3023 N N . ARG B 2 145 ? 33.680 84.883 40.424 1.00 27.55 ? 145 ARG B N 1 ATOM 3024 C CA . ARG B 2 145 ? 32.557 83.996 40.106 1.00 29.11 ? 145 ARG B CA 1 ATOM 3025 C C . ARG B 2 145 ? 31.784 84.404 38.829 1.00 27.51 ? 145 ARG B C 1 ATOM 3026 O O . ARG B 2 145 ? 30.579 84.153 38.704 1.00 25.75 ? 145 ARG B O 1 ATOM 3027 C CB . ARG B 2 145 ? 31.630 83.862 41.311 1.00 32.53 ? 145 ARG B CB 1 ATOM 3028 C CG . ARG B 2 145 ? 32.353 83.393 42.565 1.00 38.09 ? 145 ARG B CG 1 ATOM 3029 C CD . ARG B 2 145 ? 31.386 82.772 43.567 1.00 43.46 ? 145 ARG B CD 1 ATOM 3030 N NE . ARG B 2 145 ? 30.887 81.473 43.100 1.00 49.02 ? 145 ARG B NE 1 ATOM 3031 C CZ . ARG B 2 145 ? 30.119 80.636 43.804 1.00 53.53 ? 145 ARG B CZ 1 ATOM 3032 N NH1 . ARG B 2 145 ? 29.724 80.931 45.046 1.00 55.67 ? 145 ARG B NH1 1 ATOM 3033 N NH2 . ARG B 2 145 ? 29.742 79.479 43.256 1.00 56.38 ? 145 ARG B NH2 1 ATOM 3034 N N . HIS B 2 146 ? 32.489 85.027 37.883 1.00 26.14 ? 146 HIS B N 1 ATOM 3035 C CA . HIS B 2 146 ? 31.912 85.398 36.586 1.00 26.15 ? 146 HIS B CA 1 ATOM 3036 C C . HIS B 2 146 ? 30.692 86.281 36.737 1.00 26.66 ? 146 HIS B C 1 ATOM 3037 O O . HIS B 2 146 ? 29.778 86.203 35.923 1.00 28.39 ? 146 HIS B O 1 ATOM 3038 C CB . HIS B 2 146 ? 31.545 84.134 35.794 1.00 25.22 ? 146 HIS B CB 1 ATOM 3039 C CG . HIS B 2 146 ? 32.522 83.023 35.968 1.00 24.83 ? 146 HIS B CG 1 ATOM 3040 N ND1 . HIS B 2 146 ? 33.795 83.068 35.445 1.00 25.34 ? 146 HIS B ND1 1 ATOM 3041 C CD2 . HIS B 2 146 ? 32.434 81.859 36.657 1.00 24.92 ? 146 HIS B CD2 1 ATOM 3042 C CE1 . HIS B 2 146 ? 34.437 81.958 35.772 1.00 25.69 ? 146 HIS B CE1 1 ATOM 3043 N NE2 . HIS B 2 146 ? 33.633 81.208 36.507 1.00 25.36 ? 146 HIS B NE2 1 ATOM 3044 N N . MET B 2 147 ? 30.683 87.113 37.780 1.00 26.99 ? 147 MET B N 1 ATOM 3045 C CA . MET B 2 147 ? 29.564 87.995 38.074 1.00 27.61 ? 147 MET B CA 1 ATOM 3046 C C . MET B 2 147 ? 29.903 89.385 37.556 1.00 26.64 ? 147 MET B C 1 ATOM 3047 O O . MET B 2 147 ? 31.060 89.691 37.268 1.00 25.70 ? 147 MET B O 1 ATOM 3048 C CB . MET B 2 147 ? 29.285 88.037 39.584 1.00 28.91 ? 147 MET B CB 1 ATOM 3049 C CG . MET B 2 147 ? 28.868 86.697 40.189 1.00 31.24 ? 147 MET B CG 1 ATOM 3050 S SD . MET B 2 147 ? 28.183 86.819 41.867 1.00 35.37 ? 147 MET B SD 1 ATOM 3051 C CE . MET B 2 147 ? 26.432 86.623 41.598 1.00 36.15 ? 147 MET B CE 1 ATOM 3052 N N . CYS B 2 148 ? 28.877 90.219 37.478 1.00 26.56 ? 148 CYS B N 1 ATOM 3053 C CA . CYS B 2 148 ? 28.935 91.539 36.861 1.00 27.57 ? 148 CYS B CA 1 ATOM 3054 C C . CYS B 2 148 ? 28.797 92.624 37.916 1.00 25.56 ? 148 CYS B C 1 ATOM 3055 O O . CYS B 2 148 ? 27.944 92.509 38.793 1.00 24.79 ? 148 CYS B O 1 ATOM 3056 C CB . CYS B 2 148 ? 27.769 91.665 35.871 1.00 29.29 ? 148 CYS B CB 1 ATOM 3057 S SG . CYS B 2 148 ? 28.085 90.935 34.249 1.00 35.06 ? 148 CYS B SG 1 ATOM 3058 N N . LEU B 2 149 ? 29.615 93.673 37.837 1.00 24.29 ? 149 LEU B N 1 ATOM 3059 C CA . LEU B 2 149 ? 29.390 94.857 38.674 1.00 23.63 ? 149 LEU B CA 1 ATOM 3060 C C . LEU B 2 149 ? 28.058 95.495 38.320 1.00 22.96 ? 149 LEU B C 1 ATOM 3061 O O . LEU B 2 149 ? 27.755 95.700 37.150 1.00 23.43 ? 149 LEU B O 1 ATOM 3062 C CB . LEU B 2 149 ? 30.480 95.914 38.505 1.00 23.66 ? 149 LEU B CB 1 ATOM 3063 C CG . LEU B 2 149 ? 31.793 95.713 39.240 1.00 24.31 ? 149 LEU B CG 1 ATOM 3064 C CD1 . LEU B 2 149 ? 32.712 96.901 38.996 1.00 24.11 ? 149 LEU B CD1 1 ATOM 3065 C CD2 . LEU B 2 149 ? 31.555 95.508 40.731 1.00 25.08 ? 149 LEU B CD2 1 ATOM 3066 N N . GLU B 2 150 ? 27.279 95.807 39.343 1.00 22.52 ? 150 GLU B N 1 ATOM 3067 C CA . GLU B 2 150 ? 25.980 96.416 39.188 1.00 22.90 ? 150 GLU B CA 1 ATOM 3068 C C . GLU B 2 150 ? 25.899 97.648 40.080 1.00 23.16 ? 150 GLU B C 1 ATOM 3069 O O . GLU B 2 150 ? 26.378 97.612 41.220 1.00 22.19 ? 150 GLU B O 1 ATOM 3070 C CB . GLU B 2 150 ? 24.905 95.402 39.581 1.00 23.44 ? 150 GLU B CB 1 ATOM 3071 C CG . GLU B 2 150 ? 23.494 95.792 39.170 1.00 24.02 ? 150 GLU B CG 1 ATOM 3072 C CD . GLU B 2 150 ? 22.475 94.720 39.518 1.00 24.84 ? 150 GLU B CD 1 ATOM 3073 O OE1 . GLU B 2 150 ? 22.590 93.583 39.022 1.00 24.59 ? 150 GLU B OE1 1 ATOM 3074 O OE2 . GLU B 2 150 ? 21.543 95.009 40.284 1.00 26.43 ? 150 GLU B OE2 1 ATOM 3075 N N . ALA B 2 151 ? 25.294 98.716 39.556 1.00 23.83 ? 151 ALA B N 1 ATOM 3076 C CA . ALA B 2 151 ? 24.991 99.939 40.320 1.00 24.64 ? 151 ALA B CA 1 ATOM 3077 C C . ALA B 2 151 ? 23.716 99.706 41.105 1.00 25.43 ? 151 ALA B C 1 ATOM 3078 O O . ALA B 2 151 ? 22.682 99.408 40.522 1.00 25.66 ? 151 ALA B O 1 ATOM 3079 C CB . ALA B 2 151 ? 24.813 101.121 39.394 1.00 24.64 ? 151 ALA B CB 1 ATOM 3080 N N . THR B 2 152 ? 23.803 99.837 42.426 1.00 26.76 ? 152 THR B N 1 ATOM 3081 C CA . THR B 2 152 ? 22.723 99.458 43.339 1.00 27.40 ? 152 THR B CA 1 ATOM 3082 C C . THR B 2 152 ? 22.381 100.618 44.263 1.00 27.91 ? 152 THR B C 1 ATOM 3083 O O . THR B 2 152 ? 23.090 101.620 44.293 1.00 27.27 ? 152 THR B O 1 ATOM 3084 C CB . THR B 2 152 ? 23.127 98.235 44.189 1.00 26.75 ? 152 THR B CB 1 ATOM 3085 O OG1 . THR B 2 152 ? 24.299 98.543 44.959 1.00 25.82 ? 152 THR B OG1 1 ATOM 3086 C CG2 . THR B 2 152 ? 23.403 97.018 43.306 1.00 26.54 ? 152 THR B CG2 1 ATOM 3087 N N . ASP B 2 153 ? 21.289 100.454 45.012 1.00 29.92 ? 153 ASP B N 1 ATOM 3088 C CA . ASP B 2 153 ? 20.830 101.414 46.019 1.00 31.09 ? 153 ASP B CA 1 ATOM 3089 C C . ASP B 2 153 ? 20.654 102.812 45.434 1.00 31.68 ? 153 ASP B C 1 ATOM 3090 O O . ASP B 2 153 ? 21.178 103.803 45.951 1.00 30.81 ? 153 ASP B O 1 ATOM 3091 C CB . ASP B 2 153 ? 21.789 101.431 47.219 1.00 32.53 ? 153 ASP B CB 1 ATOM 3092 C CG . ASP B 2 153 ? 21.849 100.099 47.947 1.00 32.54 ? 153 ASP B CG 1 ATOM 3093 O OD1 . ASP B 2 153 ? 20.872 99.323 47.886 1.00 32.65 ? 153 ASP B OD1 1 ATOM 3094 O OD2 . ASP B 2 153 ? 22.879 99.835 48.597 1.00 34.09 ? 153 ASP B OD2 1 ATOM 3095 N N . ASN B 2 154 ? 19.919 102.868 44.331 1.00 34.09 ? 154 ASN B N 1 ATOM 3096 C CA . ASN B 2 154 ? 19.644 104.121 43.632 1.00 34.72 ? 154 ASN B CA 1 ATOM 3097 C C . ASN B 2 154 ? 20.914 104.807 43.103 1.00 32.23 ? 154 ASN B C 1 ATOM 3098 O O . ASN B 2 154 ? 21.080 106.026 43.222 1.00 30.16 ? 154 ASN B O 1 ATOM 3099 C CB . ASN B 2 154 ? 18.829 105.053 44.547 1.00 38.58 ? 154 ASN B CB 1 ATOM 3100 C CG . ASN B 2 154 ? 17.692 105.706 43.818 1.00 41.98 ? 154 ASN B CG 1 ATOM 3101 O OD1 . ASN B 2 154 ? 16.661 105.064 43.577 1.00 47.01 ? 154 ASN B OD1 1 ATOM 3102 N ND2 . ASN B 2 154 ? 17.870 106.972 43.436 1.00 41.67 ? 154 ASN B ND2 1 ATOM 3103 N N . ASP B 2 155 ? 21.794 103.998 42.502 1.00 31.59 ? 155 ASP B N 1 ATOM 3104 C CA . ASP B 2 155 ? 23.116 104.440 42.014 1.00 29.91 ? 155 ASP B CA 1 ATOM 3105 C C . ASP B 2 155 ? 24.007 105.115 43.078 1.00 27.36 ? 155 ASP B C 1 ATOM 3106 O O . ASP B 2 155 ? 24.649 106.123 42.805 1.00 26.21 ? 155 ASP B O 1 ATOM 3107 C CB . ASP B 2 155 ? 22.969 105.360 40.785 1.00 29.97 ? 155 ASP B CB 1 ATOM 3108 C CG . ASP B 2 155 ? 22.152 104.725 39.658 1.00 31.60 ? 155 ASP B CG 1 ATOM 3109 O OD1 . ASP B 2 155 ? 21.947 103.482 39.659 1.00 34.14 ? 155 ASP B OD1 1 ATOM 3110 O OD2 . ASP B 2 155 ? 21.723 105.469 38.748 1.00 30.09 ? 155 ASP B OD2 1 ATOM 3111 N N . THR B 2 156 ? 24.038 104.552 44.280 1.00 25.94 ? 156 THR B N 1 ATOM 3112 C CA . THR B 2 156 ? 24.966 104.986 45.349 1.00 26.00 ? 156 THR B CA 1 ATOM 3113 C C . THR B 2 156 ? 26.010 103.913 45.722 1.00 25.32 ? 156 THR B C 1 ATOM 3114 O O . THR B 2 156 ? 27.087 104.242 46.226 1.00 25.92 ? 156 THR B O 1 ATOM 3115 C CB . THR B 2 156 ? 24.190 105.358 46.631 1.00 26.03 ? 156 THR B CB 1 ATOM 3116 O OG1 . THR B 2 156 ? 23.429 104.228 47.078 1.00 26.18 ? 156 THR B OG1 1 ATOM 3117 C CG2 . THR B 2 156 ? 23.245 106.512 46.372 1.00 26.88 ? 156 THR B CG2 1 ATOM 3118 N N . ASN B 2 157 ? 25.679 102.641 45.509 1.00 23.89 ? 157 ASN B N 1 ATOM 3119 C CA . ASN B 2 157 ? 26.583 101.544 45.791 1.00 23.94 ? 157 ASN B CA 1 ATOM 3120 C C . ASN B 2 157 ? 26.801 100.710 44.558 1.00 23.77 ? 157 ASN B C 1 ATOM 3121 O O . ASN B 2 157 ? 26.125 100.883 43.553 1.00 24.55 ? 157 ASN B O 1 ATOM 3122 C CB . ASN B 2 157 ? 26.027 100.671 46.930 1.00 23.74 ? 157 ASN B CB 1 ATOM 3123 C CG . ASN B 2 157 ? 26.113 101.360 48.279 1.00 24.05 ? 157 ASN B CG 1 ATOM 3124 O OD1 . ASN B 2 157 ? 27.158 101.886 48.641 1.00 25.36 ? 157 ASN B OD1 1 ATOM 3125 N ND2 . ASN B 2 157 ? 25.023 101.336 49.040 1.00 23.00 ? 157 ASN B ND2 1 ATOM 3126 N N . VAL B 2 158 ? 27.753 99.798 44.664 1.00 24.04 ? 158 VAL B N 1 ATOM 3127 C CA . VAL B 2 158 ? 28.148 98.934 43.578 1.00 24.63 ? 158 VAL B CA 1 ATOM 3128 C C . VAL B 2 158 ? 28.614 97.604 44.150 1.00 24.67 ? 158 VAL B C 1 ATOM 3129 O O . VAL B 2 158 ? 29.389 97.579 45.095 1.00 25.94 ? 158 VAL B O 1 ATOM 3130 C CB . VAL B 2 158 ? 29.257 99.608 42.733 1.00 25.41 ? 158 VAL B CB 1 ATOM 3131 C CG1 . VAL B 2 158 ? 30.417 100.099 43.602 1.00 26.13 ? 158 VAL B CG1 1 ATOM 3132 C CG2 . VAL B 2 158 ? 29.746 98.694 41.613 1.00 26.44 ? 158 VAL B CG2 1 ATOM 3133 N N . TRP B 2 159 ? 28.118 96.500 43.602 1.00 24.45 ? 159 TRP B N 1 ATOM 3134 C CA . TRP B 2 159 ? 28.608 95.173 43.975 1.00 24.53 ? 159 TRP B CA 1 ATOM 3135 C C . TRP B 2 159 ? 28.355 94.134 42.873 1.00 24.38 ? 159 TRP B C 1 ATOM 3136 O O . TRP B 2 159 ? 27.800 94.458 41.817 1.00 25.06 ? 159 TRP B O 1 ATOM 3137 C CB . TRP B 2 159 ? 28.047 94.736 45.346 1.00 24.45 ? 159 TRP B CB 1 ATOM 3138 C CG . TRP B 2 159 ? 26.562 94.577 45.422 1.00 24.57 ? 159 TRP B CG 1 ATOM 3139 C CD1 . TRP B 2 159 ? 25.797 93.617 44.813 1.00 25.00 ? 159 TRP B CD1 1 ATOM 3140 C CD2 . TRP B 2 159 ? 25.663 95.380 46.183 1.00 24.36 ? 159 TRP B CD2 1 ATOM 3141 N NE1 . TRP B 2 159 ? 24.474 93.788 45.133 1.00 25.21 ? 159 TRP B NE1 1 ATOM 3142 C CE2 . TRP B 2 159 ? 24.361 94.855 45.985 1.00 24.79 ? 159 TRP B CE2 1 ATOM 3143 C CE3 . TRP B 2 159 ? 25.827 96.485 47.027 1.00 23.96 ? 159 TRP B CE3 1 ATOM 3144 C CZ2 . TRP B 2 159 ? 23.227 95.413 46.587 1.00 24.55 ? 159 TRP B CZ2 1 ATOM 3145 C CZ3 . TRP B 2 159 ? 24.696 97.037 47.632 1.00 24.42 ? 159 TRP B CZ3 1 ATOM 3146 C CH2 . TRP B 2 159 ? 23.415 96.500 47.404 1.00 24.34 ? 159 TRP B CH2 1 ATOM 3147 N N . LEU B 2 160 ? 28.799 92.904 43.102 1.00 24.10 ? 160 LEU B N 1 ATOM 3148 C CA . LEU B 2 160 ? 28.675 91.842 42.105 1.00 25.43 ? 160 LEU B CA 1 ATOM 3149 C C . LEU B 2 160 ? 27.313 91.171 42.137 1.00 25.32 ? 160 LEU B C 1 ATOM 3150 O O . LEU B 2 160 ? 26.836 90.772 43.190 1.00 24.61 ? 160 LEU B O 1 ATOM 3151 C CB . LEU B 2 160 ? 29.804 90.790 42.248 1.00 24.86 ? 160 LEU B CB 1 ATOM 3152 C CG . LEU B 2 160 ? 31.175 91.289 41.773 1.00 25.13 ? 160 LEU B CG 1 ATOM 3153 C CD1 . LEU B 2 160 ? 32.318 90.429 42.274 1.00 25.37 ? 160 LEU B CD1 1 ATOM 3154 C CD2 . LEU B 2 160 ? 31.239 91.378 40.253 1.00 25.67 ? 160 LEU B CD2 1 ATOM 3155 N N . GLU B 2 161 ? 26.698 91.065 40.962 1.00 26.67 ? 161 GLU B N 1 ATOM 3156 C CA . GLU B 2 161 ? 25.490 90.267 40.754 1.00 27.53 ? 161 GLU B CA 1 ATOM 3157 C C . GLU B 2 161 ? 25.717 89.402 39.532 1.00 28.26 ? 161 GLU B C 1 ATOM 3158 O O . GLU B 2 161 ? 26.558 89.730 38.678 1.00 28.17 ? 161 GLU B O 1 ATOM 3159 C CB . GLU B 2 161 ? 24.268 91.160 40.526 1.00 28.26 ? 161 GLU B CB 1 ATOM 3160 C CG . GLU B 2 161 ? 23.847 91.980 41.742 1.00 29.62 ? 161 GLU B CG 1 ATOM 3161 C CD . GLU B 2 161 ? 23.220 91.163 42.872 1.00 30.44 ? 161 GLU B CD 1 ATOM 3162 O OE1 . GLU B 2 161 ? 23.021 89.943 42.729 1.00 33.19 ? 161 GLU B OE1 1 ATOM 3163 O OE2 . GLU B 2 161 ? 22.920 91.754 43.922 1.00 31.50 ? 161 GLU B OE2 1 ATOM 3164 N N . SER B 2 162 ? 24.968 88.310 39.432 1.00 27.13 ? 162 SER B N 1 ATOM 3165 C CA . SER B 2 162 ? 25.097 87.427 38.281 1.00 27.81 ? 162 SER B CA 1 ATOM 3166 C C . SER B 2 162 ? 24.663 88.179 37.011 1.00 26.52 ? 162 SER B C 1 ATOM 3167 O O . SER B 2 162 ? 23.708 88.957 37.030 1.00 25.62 ? 162 SER B O 1 ATOM 3168 C CB . SER B 2 162 ? 24.304 86.125 38.482 1.00 28.62 ? 162 SER B CB 1 ATOM 3169 O OG . SER B 2 162 ? 22.919 86.381 38.562 1.00 29.59 ? 162 SER B OG 1 ATOM 3170 N N . CYS B 2 163 ? 25.402 87.962 35.930 1.00 26.57 ? 163 CYS B N 1 ATOM 3171 C CA . CYS B 2 163 ? 25.206 88.695 34.683 1.00 28.50 ? 163 CYS B CA 1 ATOM 3172 C C . CYS B 2 163 ? 23.864 88.358 34.026 1.00 27.24 ? 163 CYS B C 1 ATOM 3173 O O . CYS B 2 163 ? 23.486 87.202 33.946 1.00 27.35 ? 163 CYS B O 1 ATOM 3174 C CB . CYS B 2 163 ? 26.374 88.423 33.717 1.00 30.74 ? 163 CYS B CB 1 ATOM 3175 S SG . CYS B 2 163 ? 28.008 88.867 34.395 1.00 34.82 ? 163 CYS B SG 1 ATOM 3176 N N . VAL B 2 164 ? 23.145 89.398 33.612 1.00 27.59 ? 164 VAL B N 1 ATOM 3177 C CA . VAL B 2 164 ? 21.893 89.310 32.873 1.00 28.24 ? 164 VAL B CA 1 ATOM 3178 C C . VAL B 2 164 ? 21.996 90.332 31.741 1.00 29.37 ? 164 VAL B C 1 ATOM 3179 O O . VAL B 2 164 ? 22.150 91.526 32.006 1.00 28.19 ? 164 VAL B O 1 ATOM 3180 C CB . VAL B 2 164 ? 20.696 89.672 33.781 1.00 29.22 ? 164 VAL B CB 1 ATOM 3181 C CG1 . VAL B 2 164 ? 19.398 89.783 32.981 1.00 29.21 ? 164 VAL B CG1 1 ATOM 3182 C CG2 . VAL B 2 164 ? 20.553 88.680 34.932 1.00 28.67 ? 164 VAL B CG2 1 ATOM 3183 N N . LYS B 2 165 ? 21.906 89.872 30.490 1.00 30.95 ? 165 LYS B N 1 ATOM 3184 C CA . LYS B 2 165 ? 22.236 90.711 29.336 1.00 31.66 ? 165 LYS B CA 1 ATOM 3185 C C . LYS B 2 165 ? 21.389 91.978 29.254 1.00 33.55 ? 165 LYS B C 1 ATOM 3186 O O . LYS B 2 165 ? 21.899 93.046 28.908 1.00 33.88 ? 165 LYS B O 1 ATOM 3187 C CB . LYS B 2 165 ? 22.158 89.917 28.025 1.00 32.05 ? 165 LYS B CB 1 ATOM 3188 C CG . LYS B 2 165 ? 22.667 90.681 26.802 1.00 31.74 ? 165 LYS B CG 1 ATOM 3189 C CD . LYS B 2 165 ? 22.980 89.758 25.639 1.00 32.43 ? 165 LYS B CD 1 ATOM 3190 N N . ASN B 2 166 ? 20.112 91.875 29.596 1.00 35.60 ? 166 ASN B N 1 ATOM 3191 C CA . ASN B 2 166 ? 19.230 93.061 29.566 1.00 40.22 ? 166 ASN B CA 1 ATOM 3192 C C . ASN B 2 166 ? 19.520 94.118 30.657 1.00 38.75 ? 166 ASN B C 1 ATOM 3193 O O . ASN B 2 166 ? 19.255 95.303 30.456 1.00 39.92 ? 166 ASN B O 1 ATOM 3194 C CB . ASN B 2 166 ? 17.735 92.655 29.576 1.00 42.63 ? 166 ASN B CB 1 ATOM 3195 C CG . ASN B 2 166 ? 17.375 91.722 30.724 1.00 45.96 ? 166 ASN B CG 1 ATOM 3196 O OD1 . ASN B 2 166 ? 17.286 90.508 30.541 1.00 50.92 ? 166 ASN B OD1 1 ATOM 3197 N ND2 . ASN B 2 166 ? 17.184 92.281 31.913 1.00 48.45 ? 166 ASN B ND2 1 ATOM 3198 N N . LYS B 2 167 ? 20.116 93.692 31.770 1.00 37.06 ? 167 LYS B N 1 ATOM 3199 C CA . LYS B 2 167 ? 20.054 94.428 33.026 1.00 35.54 ? 167 LYS B CA 1 ATOM 3200 C C . LYS B 2 167 ? 20.759 95.788 32.949 1.00 33.60 ? 167 LYS B C 1 ATOM 3201 O O . LYS B 2 167 ? 21.981 95.893 32.980 1.00 31.70 ? 167 LYS B O 1 ATOM 3202 C CB . LYS B 2 167 ? 20.594 93.561 34.164 1.00 37.59 ? 167 LYS B CB 1 ATOM 3203 C CG . LYS B 2 167 ? 19.860 93.706 35.488 1.00 39.05 ? 167 LYS B CG 1 ATOM 3204 C CD . LYS B 2 167 ? 20.090 92.470 36.360 1.00 42.54 ? 167 LYS B CD 1 ATOM 3205 C CE . LYS B 2 167 ? 19.181 92.424 37.582 1.00 44.93 ? 167 LYS B CE 1 ATOM 3206 N NZ . LYS B 2 167 ? 19.539 93.424 38.628 1.00 45.56 ? 167 LYS B NZ 1 ATOM 3207 N N . THR B 2 168 ? 19.942 96.824 32.819 1.00 33.25 ? 168 THR B N 1 ATOM 3208 C CA . THR B 2 168 ? 20.398 98.207 32.616 1.00 32.57 ? 168 THR B CA 1 ATOM 3209 C C . THR B 2 168 ? 21.490 98.712 33.585 1.00 29.21 ? 168 THR B C 1 ATOM 3210 O O . THR B 2 168 ? 22.351 99.503 33.197 1.00 27.58 ? 168 THR B O 1 ATOM 3211 C CB . THR B 2 168 ? 19.190 99.198 32.565 1.00 33.46 ? 168 THR B CB 1 ATOM 3212 O OG1 . THR B 2 168 ? 19.676 100.538 32.452 1.00 37.41 ? 168 THR B OG1 1 ATOM 3213 C CG2 . THR B 2 168 ? 18.303 99.111 33.795 1.00 34.16 ? 168 THR B CG2 1 ATOM 3214 N N . LYS B 2 169 ? 21.459 98.249 34.829 1.00 28.12 ? 169 LYS B N 1 ATOM 3215 C CA . LYS B 2 169 ? 22.400 98.718 35.848 1.00 26.41 ? 169 LYS B CA 1 ATOM 3216 C C . LYS B 2 169 ? 23.745 97.988 35.883 1.00 24.84 ? 169 LYS B C 1 ATOM 3217 O O . LYS B 2 169 ? 24.645 98.398 36.615 1.00 22.90 ? 169 LYS B O 1 ATOM 3218 C CB . LYS B 2 169 ? 21.726 98.703 37.227 1.00 27.17 ? 169 LYS B CB 1 ATOM 3219 C CG . LYS B 2 169 ? 20.591 99.710 37.365 1.00 26.98 ? 169 LYS B CG 1 ATOM 3220 C CD . LYS B 2 169 ? 21.094 101.129 37.158 1.00 26.71 ? 169 LYS B CD 1 ATOM 3221 C CE . LYS B 2 169 ? 20.054 102.142 37.576 1.00 27.66 ? 169 LYS B CE 1 ATOM 3222 N NZ . LYS B 2 169 ? 20.481 103.508 37.197 1.00 27.90 ? 169 LYS B NZ 1 ATOM 3223 N N . GLN B 2 170 ? 23.884 96.931 35.084 1.00 24.76 ? 170 GLN B N 1 ATOM 3224 C CA . GLN B 2 170 ? 25.165 96.243 34.906 1.00 24.56 ? 170 GLN B CA 1 ATOM 3225 C C . GLN B 2 170 ? 26.052 96.840 33.811 1.00 23.85 ? 170 GLN B C 1 ATOM 3226 O O . GLN B 2 170 ? 27.066 96.254 33.501 1.00 24.55 ? 170 GLN B O 1 ATOM 3227 C CB . GLN B 2 170 ? 24.927 94.746 34.635 1.00 25.26 ? 170 GLN B CB 1 ATOM 3228 C CG . GLN B 2 170 ? 24.153 94.051 35.743 1.00 25.23 ? 170 GLN B CG 1 ATOM 3229 C CD . GLN B 2 170 ? 24.101 92.548 35.591 1.00 25.59 ? 170 GLN B CD 1 ATOM 3230 O OE1 . GLN B 2 170 ? 24.239 92.025 34.490 1.00 24.92 ? 170 GLN B OE1 1 ATOM 3231 N NE2 . GLN B 2 170 ? 23.896 91.833 36.713 1.00 25.66 ? 170 GLN B NE2 1 ATOM 3232 N N . TYR B 2 171 ? 25.684 97.993 33.236 1.00 23.48 ? 171 TYR B N 1 ATOM 3233 C CA . TYR B 2 171 ? 26.443 98.614 32.150 1.00 23.69 ? 171 TYR B CA 1 ATOM 3234 C C . TYR B 2 171 ? 27.124 99.896 32.617 1.00 23.28 ? 171 TYR B C 1 ATOM 3235 O O . TYR B 2 171 ? 26.536 100.707 33.345 1.00 23.58 ? 171 TYR B O 1 ATOM 3236 C CB . TYR B 2 171 ? 25.541 98.875 30.923 1.00 24.56 ? 171 TYR B CB 1 ATOM 3237 C CG . TYR B 2 171 ? 25.164 97.587 30.231 1.00 24.97 ? 171 TYR B CG 1 ATOM 3238 C CD1 . TYR B 2 171 ? 25.978 97.036 29.233 1.00 24.86 ? 171 TYR B CD1 1 ATOM 3239 C CD2 . TYR B 2 171 ? 24.024 96.882 30.617 1.00 25.07 ? 171 TYR B CD2 1 ATOM 3240 C CE1 . TYR B 2 171 ? 25.644 95.837 28.626 1.00 25.71 ? 171 TYR B CE1 1 ATOM 3241 C CE2 . TYR B 2 171 ? 23.687 95.681 30.024 1.00 25.13 ? 171 TYR B CE2 1 ATOM 3242 C CZ . TYR B 2 171 ? 24.493 95.161 29.028 1.00 26.36 ? 171 TYR B CZ 1 ATOM 3243 O OH . TYR B 2 171 ? 24.151 93.957 28.448 1.00 28.61 ? 171 TYR B OH 1 ATOM 3244 N N . TRP B 2 172 ? 28.369 100.060 32.185 1.00 21.89 ? 172 TRP B N 1 ATOM 3245 C CA . TRP B 2 172 ? 29.214 101.182 32.566 1.00 22.10 ? 172 TRP B CA 1 ATOM 3246 C C . TRP B 2 172 ? 29.813 101.843 31.322 1.00 22.89 ? 172 TRP B C 1 ATOM 3247 O O . TRP B 2 172 ? 30.063 101.179 30.320 1.00 23.28 ? 172 TRP B O 1 ATOM 3248 C CB . TRP B 2 172 ? 30.338 100.692 33.480 1.00 21.30 ? 172 TRP B CB 1 ATOM 3249 C CG . TRP B 2 172 ? 29.830 99.890 34.618 1.00 20.74 ? 172 TRP B CG 1 ATOM 3250 C CD1 . TRP B 2 172 ? 29.651 98.550 34.648 1.00 21.38 ? 172 TRP B CD1 1 ATOM 3251 C CD2 . TRP B 2 172 ? 29.384 100.384 35.873 1.00 20.74 ? 172 TRP B CD2 1 ATOM 3252 N NE1 . TRP B 2 172 ? 29.142 98.163 35.856 1.00 21.13 ? 172 TRP B NE1 1 ATOM 3253 C CE2 . TRP B 2 172 ? 28.964 99.270 36.632 1.00 21.50 ? 172 TRP B CE2 1 ATOM 3254 C CE3 . TRP B 2 172 ? 29.315 101.656 36.443 1.00 21.02 ? 172 TRP B CE3 1 ATOM 3255 C CZ2 . TRP B 2 172 ? 28.466 99.387 37.941 1.00 21.65 ? 172 TRP B CZ2 1 ATOM 3256 C CZ3 . TRP B 2 172 ? 28.807 101.778 37.739 1.00 21.68 ? 172 TRP B CZ3 1 ATOM 3257 C CH2 . TRP B 2 172 ? 28.396 100.645 38.472 1.00 21.85 ? 172 TRP B CH2 1 ATOM 3258 N N . ALA B 2 173 ? 30.046 103.146 31.407 1.00 23.33 ? 173 ALA B N 1 ATOM 3259 C CA . ALA B 2 173 ? 30.656 103.911 30.337 1.00 23.74 ? 173 ALA B CA 1 ATOM 3260 C C . ALA B 2 173 ? 32.046 104.308 30.799 1.00 23.43 ? 173 ALA B C 1 ATOM 3261 O O . ALA B 2 173 ? 32.174 105.087 31.744 1.00 22.55 ? 173 ALA B O 1 ATOM 3262 C CB . ALA B 2 173 ? 29.827 105.152 30.042 1.00 24.76 ? 173 ALA B CB 1 ATOM 3263 N N . LEU B 2 174 ? 33.079 103.747 30.154 1.00 22.19 ? 174 LEU B N 1 ATOM 3264 C CA . LEU B 2 174 ? 34.463 104.095 30.461 1.00 20.71 ? 174 LEU B CA 1 ATOM 3265 C C . LEU B 2 174 ? 34.814 105.362 29.693 1.00 20.24 ? 174 LEU B C 1 ATOM 3266 O O . LEU B 2 174 ? 34.770 105.371 28.468 1.00 20.86 ? 174 LEU B O 1 ATOM 3267 C CB . LEU B 2 174 ? 35.415 102.968 30.075 1.00 20.48 ? 174 LEU B CB 1 ATOM 3268 C CG . LEU B 2 174 ? 35.048 101.543 30.495 1.00 20.01 ? 174 LEU B CG 1 ATOM 3269 C CD1 . LEU B 2 174 ? 36.221 100.629 30.160 1.00 19.51 ? 174 LEU B CD1 1 ATOM 3270 C CD2 . LEU B 2 174 ? 34.698 101.484 31.965 1.00 20.51 ? 174 LEU B CD2 1 ATOM 3271 N N . TYR B 2 175 ? 35.167 106.415 30.419 1.00 19.41 ? 175 TYR B N 1 ATOM 3272 C CA . TYR B 2 175 ? 35.416 107.734 29.845 1.00 18.77 ? 175 TYR B CA 1 ATOM 3273 C C . TYR B 2 175 ? 36.899 108.010 29.684 1.00 18.95 ? 175 TYR B C 1 ATOM 3274 O O . TYR B 2 175 ? 37.751 107.347 30.281 1.00 18.48 ? 175 TYR B O 1 ATOM 3275 C CB . TYR B 2 175 ? 34.804 108.826 30.727 1.00 18.97 ? 175 TYR B CB 1 ATOM 3276 C CG . TYR B 2 175 ? 33.397 109.237 30.393 1.00 18.44 ? 175 TYR B CG 1 ATOM 3277 C CD1 . TYR B 2 175 ? 32.324 108.379 30.623 1.00 18.96 ? 175 TYR B CD1 1 ATOM 3278 C CD2 . TYR B 2 175 ? 33.126 110.514 29.897 1.00 19.04 ? 175 TYR B CD2 1 ATOM 3279 C CE1 . TYR B 2 175 ? 31.018 108.760 30.334 1.00 18.91 ? 175 TYR B CE1 1 ATOM 3280 C CE2 . TYR B 2 175 ? 31.826 110.918 29.617 1.00 18.67 ? 175 TYR B CE2 1 ATOM 3281 C CZ . TYR B 2 175 ? 30.781 110.049 29.825 1.00 19.22 ? 175 TYR B CZ 1 ATOM 3282 O OH . TYR B 2 175 ? 29.514 110.482 29.527 1.00 20.09 ? 175 TYR B OH 1 ATOM 3283 N N . SER B 2 176 ? 37.194 109.045 28.903 1.00 18.47 ? 176 SER B N 1 ATOM 3284 C CA . SER B 2 176 ? 38.573 109.399 28.551 1.00 18.82 ? 176 SER B CA 1 ATOM 3285 C C . SER B 2 176 ? 39.409 109.926 29.709 1.00 18.37 ? 176 SER B C 1 ATOM 3286 O O . SER B 2 176 ? 40.617 109.949 29.614 1.00 18.52 ? 176 SER B O 1 ATOM 3287 C CB . SER B 2 176 ? 38.587 110.398 27.403 1.00 18.59 ? 176 SER B CB 1 ATOM 3288 O OG . SER B 2 176 ? 37.880 109.860 26.297 1.00 18.57 ? 176 SER B OG 1 ATOM 3289 N N . ASP B 2 177 ? 38.752 110.335 30.789 1.00 18.71 ? 177 ASP B N 1 ATOM 3290 C CA . ASP B 2 177 ? 39.417 110.718 32.051 1.00 18.82 ? 177 ASP B CA 1 ATOM 3291 C C . ASP B 2 177 ? 39.595 109.565 33.039 1.00 18.89 ? 177 ASP B C 1 ATOM 3292 O O . ASP B 2 177 ? 39.703 109.805 34.242 1.00 17.63 ? 177 ASP B O 1 ATOM 3293 C CB . ASP B 2 177 ? 38.652 111.861 32.733 1.00 18.22 ? 177 ASP B CB 1 ATOM 3294 C CG . ASP B 2 177 ? 37.182 111.535 32.982 1.00 18.42 ? 177 ASP B CG 1 ATOM 3295 O OD1 . ASP B 2 177 ? 36.786 110.347 32.840 1.00 16.84 ? 177 ASP B OD1 1 ATOM 3296 O OD2 . ASP B 2 177 ? 36.414 112.483 33.294 1.00 17.38 ? 177 ASP B OD2 1 ATOM 3297 N N . ASP B 2 178 ? 39.617 108.324 32.541 1.00 19.43 ? 178 ASP B N 1 ATOM 3298 C CA . ASP B 2 178 ? 39.760 107.132 33.388 1.00 19.70 ? 178 ASP B CA 1 ATOM 3299 C C . ASP B 2 178 ? 38.625 106.914 34.404 1.00 19.28 ? 178 ASP B C 1 ATOM 3300 O O . ASP B 2 178 ? 38.790 106.135 35.347 1.00 19.50 ? 178 ASP B O 1 ATOM 3301 C CB . ASP B 2 178 ? 41.129 107.134 34.101 1.00 20.03 ? 178 ASP B CB 1 ATOM 3302 C CG . ASP B 2 178 ? 42.292 106.839 33.174 1.00 20.82 ? 178 ASP B CG 1 ATOM 3303 O OD1 . ASP B 2 178 ? 42.096 106.379 32.032 1.00 23.04 ? 178 ASP B OD1 1 ATOM 3304 O OD2 . ASP B 2 178 ? 43.436 107.042 33.611 1.00 20.77 ? 178 ASP B OD2 1 ATOM 3305 N N . THR B 2 179 ? 37.470 107.553 34.196 1.00 18.21 ? 179 THR B N 1 ATOM 3306 C CA . THR B 2 179 ? 36.335 107.386 35.091 1.00 18.30 ? 179 THR B CA 1 ATOM 3307 C C . THR B 2 179 ? 35.485 106.214 34.611 1.00 18.09 ? 179 THR B C 1 ATOM 3308 O O . THR B 2 179 ? 35.466 105.910 33.409 1.00 19.57 ? 179 THR B O 1 ATOM 3309 C CB . THR B 2 179 ? 35.467 108.673 35.206 1.00 18.85 ? 179 THR B CB 1 ATOM 3310 O OG1 . THR B 2 179 ? 34.983 109.074 33.913 1.00 19.35 ? 179 THR B OG1 1 ATOM 3311 C CG2 . THR B 2 179 ? 36.264 109.822 35.821 1.00 18.58 ? 179 THR B CG2 1 ATOM 3312 N N . ILE B 2 180 ? 34.810 105.561 35.548 1.00 16.49 ? 180 ILE B N 1 ATOM 3313 C CA . ILE B 2 180 ? 33.904 104.477 35.265 1.00 17.42 ? 180 ILE B CA 1 ATOM 3314 C C . ILE B 2 180 ? 32.553 105.016 35.688 1.00 17.57 ? 180 ILE B C 1 ATOM 3315 O O . ILE B 2 180 ? 32.297 105.167 36.886 1.00 18.60 ? 180 ILE B O 1 ATOM 3316 C CB . ILE B 2 180 ? 34.243 103.185 36.061 1.00 16.72 ? 180 ILE B CB 1 ATOM 3317 C CG1 . ILE B 2 180 ? 35.645 102.690 35.710 1.00 16.97 ? 180 ILE B CG1 1 ATOM 3318 C CG2 . ILE B 2 180 ? 33.202 102.107 35.816 1.00 16.72 ? 180 ILE B CG2 1 ATOM 3319 C CD1 . ILE B 2 180 ? 36.187 101.628 36.647 1.00 16.80 ? 180 ILE B CD1 1 ATOM 3320 N N . ARG B 2 181 ? 31.695 105.305 34.712 1.00 17.04 ? 181 ARG B N 1 ATOM 3321 C CA . ARG B 2 181 ? 30.444 105.976 34.972 1.00 17.50 ? 181 ARG B CA 1 ATOM 3322 C C . ARG B 2 181 ? 29.251 105.066 34.761 1.00 18.83 ? 181 ARG B C 1 ATOM 3323 O O . ARG B 2 181 ? 29.301 104.152 33.940 1.00 20.30 ? 181 ARG B O 1 ATOM 3324 C CB . ARG B 2 181 ? 30.335 107.206 34.086 1.00 17.12 ? 181 ARG B CB 1 ATOM 3325 C CG . ARG B 2 181 ? 31.578 108.061 34.122 1.00 16.66 ? 181 ARG B CG 1 ATOM 3326 C CD . ARG B 2 181 ? 31.274 109.515 33.834 1.00 16.50 ? 181 ARG B CD 1 ATOM 3327 N NE . ARG B 2 181 ? 32.497 110.319 33.819 1.00 16.11 ? 181 ARG B NE 1 ATOM 3328 C CZ . ARG B 2 181 ? 32.524 111.643 33.726 1.00 16.47 ? 181 ARG B CZ 1 ATOM 3329 N NH1 . ARG B 2 181 ? 31.379 112.329 33.647 1.00 17.25 ? 181 ARG B NH1 1 ATOM 3330 N NH2 . ARG B 2 181 ? 33.688 112.290 33.726 1.00 15.32 ? 181 ARG B NH2 1 ATOM 3331 N N . VAL B 2 182 ? 28.182 105.331 35.514 1.00 20.03 ? 182 VAL B N 1 ATOM 3332 C CA . VAL B 2 182 ? 26.928 104.589 35.414 1.00 21.35 ? 182 VAL B CA 1 ATOM 3333 C C . VAL B 2 182 ? 26.425 104.873 34.009 1.00 22.45 ? 182 VAL B C 1 ATOM 3334 O O . VAL B 2 182 ? 26.407 106.028 33.587 1.00 24.07 ? 182 VAL B O 1 ATOM 3335 C CB . VAL B 2 182 ? 25.875 105.058 36.468 1.00 21.25 ? 182 VAL B CB 1 ATOM 3336 C CG1 . VAL B 2 182 ? 24.515 104.409 36.237 1.00 20.65 ? 182 VAL B CG1 1 ATOM 3337 C CG2 . VAL B 2 182 ? 26.368 104.798 37.897 1.00 21.29 ? 182 VAL B CG2 1 ATOM 3338 N N . ASN B 2 183 ? 26.040 103.837 33.274 1.00 23.86 ? 183 ASN B N 1 ATOM 3339 C CA . ASN B 2 183 ? 25.763 104.037 31.849 1.00 25.25 ? 183 ASN B CA 1 ATOM 3340 C C . ASN B 2 183 ? 24.521 104.906 31.594 1.00 26.24 ? 183 ASN B C 1 ATOM 3341 O O . ASN B 2 183 ? 24.535 105.728 30.684 1.00 25.99 ? 183 ASN B O 1 ATOM 3342 C CB . ASN B 2 183 ? 25.672 102.724 31.080 1.00 23.12 ? 183 ASN B CB 1 ATOM 3343 C CG . ASN B 2 183 ? 25.489 102.948 29.586 1.00 23.02 ? 183 ASN B CG 1 ATOM 3344 O OD1 . ASN B 2 183 ? 26.155 103.774 28.980 1.00 22.16 ? 183 ASN B OD1 1 ATOM 3345 N ND2 . ASN B 2 183 ? 24.579 102.213 29.002 1.00 23.54 ? 183 ASN B ND2 1 ATOM 3346 N N . ASN B 2 184 ? 23.470 104.730 32.389 1.00 28.14 ? 184 ASN B N 1 ATOM 3347 C CA . ASN B 2 184 ? 22.264 105.556 32.223 1.00 30.59 ? 184 ASN B CA 1 ATOM 3348 C C . ASN B 2 184 ? 22.221 106.812 33.126 1.00 28.78 ? 184 ASN B C 1 ATOM 3349 O O . ASN B 2 184 ? 21.185 107.461 33.226 1.00 29.49 ? 184 ASN B O 1 ATOM 3350 C CB . ASN B 2 184 ? 21.003 104.696 32.349 1.00 32.35 ? 184 ASN B CB 1 ATOM 3351 C CG . ASN B 2 184 ? 20.550 104.531 33.771 1.00 35.84 ? 184 ASN B CG 1 ATOM 3352 O OD1 . ASN B 2 184 ? 21.366 104.412 34.684 1.00 40.13 ? 184 ASN B OD1 1 ATOM 3353 N ND2 . ASN B 2 184 ? 19.232 104.539 33.979 1.00 38.16 ? 184 ASN B ND2 1 ATOM 3354 N N . ASN B 2 185 ? 23.348 107.158 33.756 1.00 27.99 ? 185 ASN B N 1 ATOM 3355 C CA . ASN B 2 185 ? 23.490 108.425 34.486 1.00 26.48 ? 185 ASN B CA 1 ATOM 3356 C C . ASN B 2 185 ? 24.936 108.845 34.533 1.00 25.05 ? 185 ASN B C 1 ATOM 3357 O O . ASN B 2 185 ? 25.657 108.572 35.497 1.00 25.12 ? 185 ASN B O 1 ATOM 3358 C CB . ASN B 2 185 ? 22.904 108.337 35.903 1.00 26.74 ? 185 ASN B CB 1 ATOM 3359 C CG . ASN B 2 185 ? 22.799 109.698 36.581 1.00 27.83 ? 185 ASN B CG 1 ATOM 3360 O OD1 . ASN B 2 185 ? 23.487 110.665 36.217 1.00 28.27 ? 185 ASN B OD1 1 ATOM 3361 N ND2 . ASN B 2 185 ? 21.948 109.774 37.588 1.00 28.67 ? 185 ASN B ND2 1 ATOM 3362 N N . ARG B 2 186 ? 25.329 109.584 33.509 1.00 24.80 ? 186 ARG B N 1 ATOM 3363 C CA . ARG B 2 186 ? 26.727 109.884 33.245 1.00 24.89 ? 186 ARG B CA 1 ATOM 3364 C C . ARG B 2 186 ? 27.332 110.965 34.128 1.00 24.59 ? 186 ARG B C 1 ATOM 3365 O O . ARG B 2 186 ? 28.507 111.282 33.959 1.00 24.89 ? 186 ARG B O 1 ATOM 3366 C CB . ARG B 2 186 ? 26.910 110.284 31.773 1.00 25.78 ? 186 ARG B CB 1 ATOM 3367 C CG . ARG B 2 186 ? 26.407 109.283 30.742 1.00 27.02 ? 186 ARG B CG 1 ATOM 3368 C CD . ARG B 2 186 ? 27.284 108.063 30.647 1.00 27.39 ? 186 ARG B CD 1 ATOM 3369 N NE . ARG B 2 186 ? 26.833 107.076 29.645 1.00 28.74 ? 186 ARG B NE 1 ATOM 3370 C CZ . ARG B 2 186 ? 27.185 107.028 28.351 1.00 29.26 ? 186 ARG B CZ 1 ATOM 3371 N NH1 . ARG B 2 186 ? 27.971 107.948 27.796 1.00 29.94 ? 186 ARG B NH1 1 ATOM 3372 N NH2 . ARG B 2 186 ? 26.727 106.039 27.584 1.00 29.61 ? 186 ARG B NH2 1 ATOM 3373 N N . ASN B 2 187 ? 26.557 111.557 35.035 1.00 25.78 ? 187 ASN B N 1 ATOM 3374 C CA . ASN B 2 187 ? 27.122 112.418 36.092 1.00 28.10 ? 187 ASN B CA 1 ATOM 3375 C C . ASN B 2 187 ? 27.638 111.641 37.325 1.00 27.44 ? 187 ASN B C 1 ATOM 3376 O O . ASN B 2 187 ? 28.244 112.259 38.213 1.00 28.33 ? 187 ASN B O 1 ATOM 3377 C CB . ASN B 2 187 ? 26.097 113.459 36.572 1.00 30.06 ? 187 ASN B CB 1 ATOM 3378 C CG . ASN B 2 187 ? 25.719 114.466 35.498 1.00 31.83 ? 187 ASN B CG 1 ATOM 3379 O OD1 . ASN B 2 187 ? 24.535 114.690 35.242 1.00 34.28 ? 187 ASN B OD1 1 ATOM 3380 N ND2 . ASN B 2 187 ? 26.715 115.083 34.870 1.00 32.88 ? 187 ASN B ND2 1 ATOM 3381 N N . LEU B 2 188 ? 27.387 110.325 37.387 1.00 25.75 ? 188 LEU B N 1 ATOM 3382 C CA . LEU B 2 188 ? 27.799 109.473 38.512 1.00 25.53 ? 188 LEU B CA 1 ATOM 3383 C C . LEU B 2 188 ? 28.957 108.553 38.141 1.00 25.82 ? 188 LEU B C 1 ATOM 3384 O O . LEU B 2 188 ? 28.923 107.895 37.092 1.00 26.13 ? 188 LEU B O 1 ATOM 3385 C CB . LEU B 2 188 ? 26.638 108.600 38.966 1.00 25.04 ? 188 LEU B CB 1 ATOM 3386 C CG . LEU B 2 188 ? 25.365 109.333 39.374 1.00 25.75 ? 188 LEU B CG 1 ATOM 3387 C CD1 . LEU B 2 188 ? 24.356 108.316 39.873 1.00 25.38 ? 188 LEU B CD1 1 ATOM 3388 C CD2 . LEU B 2 188 ? 25.633 110.408 40.434 1.00 25.54 ? 188 LEU B CD2 1 ATOM 3389 N N . CYS B 2 189 ? 29.934 108.481 39.046 1.00 24.80 ? 189 CYS B N 1 ATOM 3390 C CA . CYS B 2 189 ? 31.233 107.849 38.836 1.00 24.85 ? 189 CYS B CA 1 ATOM 3391 C C . CYS B 2 189 ? 31.500 106.837 39.941 1.00 23.21 ? 189 CYS B C 1 ATOM 3392 O O . CYS B 2 189 ? 31.231 107.116 41.116 1.00 21.49 ? 189 CYS B O 1 ATOM 3393 C CB . CYS B 2 189 ? 32.329 108.924 38.895 1.00 26.23 ? 189 CYS B CB 1 ATOM 3394 S SG . CYS B 2 189 ? 32.566 109.867 37.364 1.00 32.20 ? 189 CYS B SG 1 ATOM 3395 N N . VAL B 2 190 ? 32.071 105.690 39.581 1.00 22.14 ? 190 VAL B N 1 ATOM 3396 C CA . VAL B 2 190 ? 32.565 104.736 40.584 1.00 20.93 ? 190 VAL B CA 1 ATOM 3397 C C . VAL B 2 190 ? 33.715 105.417 41.340 1.00 20.11 ? 190 VAL B C 1 ATOM 3398 O O . VAL B 2 190 ? 34.611 106.023 40.729 1.00 17.99 ? 190 VAL B O 1 ATOM 3399 C CB . VAL B 2 190 ? 33.039 103.408 39.950 1.00 20.79 ? 190 VAL B CB 1 ATOM 3400 C CG1 . VAL B 2 190 ? 33.674 102.494 40.994 1.00 20.95 ? 190 VAL B CG1 1 ATOM 3401 C CG2 . VAL B 2 190 ? 31.876 102.701 39.281 1.00 20.89 ? 190 VAL B CG2 1 ATOM 3402 N N . SER B 2 191 ? 33.674 105.320 42.670 1.00 19.36 ? 191 SER B N 1 ATOM 3403 C CA . SER B 2 191 ? 34.563 106.091 43.525 1.00 20.26 ? 191 SER B CA 1 ATOM 3404 C C . SER B 2 191 ? 35.082 105.333 44.746 1.00 20.22 ? 191 SER B C 1 ATOM 3405 O O . SER B 2 191 ? 34.333 104.650 45.428 1.00 22.02 ? 191 SER B O 1 ATOM 3406 C CB . SER B 2 191 ? 33.847 107.347 44.022 1.00 20.32 ? 191 SER B CB 1 ATOM 3407 O OG . SER B 2 191 ? 34.708 108.066 44.903 1.00 20.69 ? 191 SER B OG 1 ATOM 3408 N N . SER B 2 192 ? 36.367 105.512 45.029 1.00 20.39 ? 192 SER B N 1 ATOM 3409 C CA . SER B 2 192 ? 36.994 104.983 46.229 1.00 19.99 ? 192 SER B CA 1 ATOM 3410 C C . SER B 2 192 ? 36.497 105.810 47.402 1.00 19.77 ? 192 SER B C 1 ATOM 3411 O O . SER B 2 192 ? 36.197 106.998 47.247 1.00 19.13 ? 192 SER B O 1 ATOM 3412 C CB . SER B 2 192 ? 38.510 105.081 46.105 1.00 19.44 ? 192 SER B CB 1 ATOM 3413 O OG . SER B 2 192 ? 38.934 106.406 46.297 1.00 20.15 ? 192 SER B OG 1 ATOM 3414 N N . SER B 2 193 ? 36.400 105.181 48.564 1.00 19.66 ? 193 SER B N 1 ATOM 3415 C CA . SER B 2 193 ? 35.907 105.833 49.777 1.00 19.98 ? 193 SER B CA 1 ATOM 3416 C C . SER B 2 193 ? 36.457 107.241 50.025 1.00 20.43 ? 193 SER B C 1 ATOM 3417 O O . SER B 2 193 ? 37.670 107.472 49.954 1.00 20.68 ? 193 SER B O 1 ATOM 3418 C CB . SER B 2 193 ? 36.222 104.966 51.002 1.00 20.46 ? 193 SER B CB 1 ATOM 3419 O OG . SER B 2 193 ? 35.676 105.537 52.185 1.00 20.27 ? 193 SER B OG 1 ATOM 3420 N N . THR B 2 194 ? 35.559 108.176 50.317 1.00 21.74 ? 194 THR B N 1 ATOM 3421 C CA . THR B 2 194 ? 35.963 109.474 50.871 1.00 24.62 ? 194 THR B CA 1 ATOM 3422 C C . THR B 2 194 ? 35.996 109.454 52.421 1.00 27.14 ? 194 THR B C 1 ATOM 3423 O O . THR B 2 194 ? 36.388 110.442 53.032 1.00 28.69 ? 194 THR B O 1 ATOM 3424 C CB . THR B 2 194 ? 35.025 110.584 50.414 1.00 24.27 ? 194 THR B CB 1 ATOM 3425 O OG1 . THR B 2 194 ? 33.693 110.241 50.788 1.00 23.67 ? 194 THR B OG1 1 ATOM 3426 C CG2 . THR B 2 194 ? 35.099 110.761 48.876 1.00 25.47 ? 194 THR B CG2 1 ATOM 3427 N N . ASP B 2 195 ? 35.591 108.337 53.038 1.00 28.42 ? 195 ASP B N 1 ATOM 3428 C CA . ASP B 2 195 ? 35.685 108.157 54.494 1.00 30.33 ? 195 ASP B CA 1 ATOM 3429 C C . ASP B 2 195 ? 36.910 107.307 54.867 1.00 29.02 ? 195 ASP B C 1 ATOM 3430 O O . ASP B 2 195 ? 36.993 106.123 54.509 1.00 27.84 ? 195 ASP B O 1 ATOM 3431 C CB . ASP B 2 195 ? 34.404 107.507 55.031 1.00 32.90 ? 195 ASP B CB 1 ATOM 3432 C CG . ASP B 2 195 ? 34.428 107.305 56.559 1.00 37.28 ? 195 ASP B CG 1 ATOM 3433 O OD1 . ASP B 2 195 ? 35.355 107.829 57.240 1.00 40.52 ? 195 ASP B OD1 1 ATOM 3434 O OD2 . ASP B 2 195 ? 33.517 106.614 57.080 1.00 37.62 ? 195 ASP B OD2 1 ATOM 3435 N N . SER B 2 196 ? 37.833 107.915 55.610 1.00 27.46 ? 196 SER B N 1 ATOM 3436 C CA . SER B 2 196 ? 39.047 107.255 56.093 1.00 28.61 ? 196 SER B CA 1 ATOM 3437 C C . SER B 2 196 ? 38.802 105.904 56.787 1.00 26.83 ? 196 SER B C 1 ATOM 3438 O O . SER B 2 196 ? 39.624 104.997 56.680 1.00 26.34 ? 196 SER B O 1 ATOM 3439 C CB . SER B 2 196 ? 39.781 108.178 57.067 1.00 30.20 ? 196 SER B CB 1 ATOM 3440 O OG . SER B 2 196 ? 41.008 107.598 57.493 1.00 33.92 ? 196 SER B OG 1 ATOM 3441 N N . SER B 2 197 ? 37.686 105.793 57.502 1.00 25.65 ? 197 SER B N 1 ATOM 3442 C CA . SER B 2 197 ? 37.319 104.559 58.210 1.00 25.41 ? 197 SER B CA 1 ATOM 3443 C C . SER B 2 197 ? 36.849 103.411 57.308 1.00 24.62 ? 197 SER B C 1 ATOM 3444 O O . SER B 2 197 ? 36.809 102.261 57.764 1.00 23.93 ? 197 SER B O 1 ATOM 3445 C CB . SER B 2 197 ? 36.242 104.850 59.259 1.00 24.77 ? 197 SER B CB 1 ATOM 3446 O OG . SER B 2 197 ? 36.726 105.774 60.221 1.00 25.99 ? 197 SER B OG 1 ATOM 3447 N N . SER B 2 198 ? 36.464 103.722 56.067 1.00 23.82 ? 198 SER B N 1 ATOM 3448 C CA . SER B 2 198 ? 35.948 102.730 55.127 1.00 24.27 ? 198 SER B CA 1 ATOM 3449 C C . SER B 2 198 ? 36.884 102.522 53.931 1.00 23.24 ? 198 SER B C 1 ATOM 3450 O O . SER B 2 198 ? 37.543 103.459 53.457 1.00 21.78 ? 198 SER B O 1 ATOM 3451 C CB . SER B 2 198 ? 34.564 103.133 54.628 1.00 24.50 ? 198 SER B CB 1 ATOM 3452 O OG . SER B 2 198 ? 33.960 102.053 53.929 1.00 25.11 ? 198 SER B OG 1 ATOM 3453 N N . LYS B 2 199 ? 36.955 101.276 53.471 1.00 22.23 ? 199 LYS B N 1 ATOM 3454 C CA . LYS B 2 199 ? 37.623 100.956 52.213 1.00 21.79 ? 199 LYS B CA 1 ATOM 3455 C C . LYS B 2 199 ? 36.609 100.713 51.095 1.00 20.11 ? 199 LYS B C 1 ATOM 3456 O O . LYS B 2 199 ? 36.997 100.335 49.998 1.00 19.89 ? 199 LYS B O 1 ATOM 3457 C CB . LYS B 2 199 ? 38.510 99.713 52.358 1.00 22.64 ? 199 LYS B CB 1 ATOM 3458 C CG . LYS B 2 199 ? 39.505 99.750 53.493 1.00 23.93 ? 199 LYS B CG 1 ATOM 3459 C CD . LYS B 2 199 ? 40.493 100.885 53.352 1.00 25.02 ? 199 LYS B CD 1 ATOM 3460 C CE . LYS B 2 199 ? 41.596 100.711 54.388 1.00 26.24 ? 199 LYS B CE 1 ATOM 3461 N NZ . LYS B 2 199 ? 42.532 101.865 54.428 1.00 26.87 ? 199 LYS B NZ 1 ATOM 3462 N N . LEU B 2 200 ? 35.325 100.943 51.358 1.00 19.03 ? 200 LEU B N 1 ATOM 3463 C CA . LEU B 2 200 ? 34.274 100.539 50.451 1.00 18.97 ? 200 LEU B CA 1 ATOM 3464 C C . LEU B 2 200 ? 34.226 101.431 49.205 1.00 19.66 ? 200 LEU B C 1 ATOM 3465 O O . LEU B 2 200 ? 34.193 102.656 49.310 1.00 18.79 ? 200 LEU B O 1 ATOM 3466 C CB . LEU B 2 200 ? 32.942 100.582 51.169 1.00 19.37 ? 200 LEU B CB 1 ATOM 3467 C CG . LEU B 2 200 ? 31.757 99.934 50.484 1.00 19.84 ? 200 LEU B CG 1 ATOM 3468 C CD1 . LEU B 2 200 ? 31.929 98.420 50.405 1.00 20.07 ? 200 LEU B CD1 1 ATOM 3469 C CD2 . LEU B 2 200 ? 30.490 100.322 51.245 1.00 20.23 ? 200 LEU B CD2 1 ATOM 3470 N N . ILE B 2 201 ? 34.247 100.796 48.034 1.00 19.56 ? 201 ILE B N 1 ATOM 3471 C CA . ILE B 2 201 ? 34.096 101.494 46.771 1.00 19.64 ? 201 ILE B CA 1 ATOM 3472 C C . ILE B 2 201 ? 32.607 101.756 46.607 1.00 19.44 ? 201 ILE B C 1 ATOM 3473 O O . ILE B 2 201 ? 31.793 100.880 46.874 1.00 19.27 ? 201 ILE B O 1 ATOM 3474 C CB . ILE B 2 201 ? 34.689 100.678 45.606 1.00 19.26 ? 201 ILE B CB 1 ATOM 3475 C CG1 . ILE B 2 201 ? 36.217 100.681 45.727 1.00 19.82 ? 201 ILE B CG1 1 ATOM 3476 C CG2 . ILE B 2 201 ? 34.292 101.259 44.257 1.00 19.32 ? 201 ILE B CG2 1 ATOM 3477 C CD1 . ILE B 2 201 ? 36.866 99.517 45.026 1.00 19.69 ? 201 ILE B CD1 1 ATOM 3478 N N . VAL B 2 202 ? 32.268 102.974 46.205 1.00 20.03 ? 202 VAL B N 1 ATOM 3479 C CA . VAL B 2 202 ? 30.870 103.436 46.113 1.00 21.18 ? 202 VAL B CA 1 ATOM 3480 C C . VAL B 2 202 ? 30.647 104.239 44.806 1.00 22.05 ? 202 VAL B C 1 ATOM 3481 O O . VAL B 2 202 ? 31.556 104.340 43.975 1.00 21.31 ? 202 VAL B O 1 ATOM 3482 C CB . VAL B 2 202 ? 30.500 104.283 47.355 1.00 22.35 ? 202 VAL B CB 1 ATOM 3483 C CG1 . VAL B 2 202 ? 30.495 103.421 48.620 1.00 22.15 ? 202 VAL B CG1 1 ATOM 3484 C CG2 . VAL B 2 202 ? 31.444 105.475 47.523 1.00 22.69 ? 202 VAL B CG2 1 ATOM 3485 N N . ILE B 2 203 ? 29.441 104.782 44.614 1.00 22.75 ? 203 ILE B N 1 ATOM 3486 C CA . ILE B 2 203 ? 29.129 105.611 43.448 1.00 23.46 ? 203 ILE B CA 1 ATOM 3487 C C . ILE B 2 203 ? 28.826 107.032 43.912 1.00 23.48 ? 203 ILE B C 1 ATOM 3488 O O . ILE B 2 203 ? 28.013 107.228 44.804 1.00 22.96 ? 203 ILE B O 1 ATOM 3489 C CB . ILE B 2 203 ? 27.954 105.033 42.638 1.00 24.35 ? 203 ILE B CB 1 ATOM 3490 C CG1 . ILE B 2 203 ? 28.341 103.661 42.077 1.00 24.59 ? 203 ILE B CG1 1 ATOM 3491 C CG2 . ILE B 2 203 ? 27.576 105.975 41.492 1.00 24.29 ? 203 ILE B CG2 1 ATOM 3492 C CD1 . ILE B 2 203 ? 27.183 102.900 41.468 1.00 25.99 ? 203 ILE B CD1 1 ATOM 3493 N N . ARG B 2 204 ? 29.513 108.009 43.328 1.00 23.35 ? 204 ARG B N 1 ATOM 3494 C CA . ARG B 2 204 ? 29.357 109.419 43.699 1.00 23.68 ? 204 ARG B CA 1 ATOM 3495 C C . ARG B 2 204 ? 29.368 110.285 42.458 1.00 23.79 ? 204 ARG B C 1 ATOM 3496 O O . ARG B 2 204 ? 29.923 109.891 41.422 1.00 21.84 ? 204 ARG B O 1 ATOM 3497 C CB . ARG B 2 204 ? 30.495 109.880 44.605 1.00 24.66 ? 204 ARG B CB 1 ATOM 3498 C CG . ARG B 2 204 ? 30.608 109.163 45.942 1.00 25.93 ? 204 ARG B CG 1 ATOM 3499 C CD . ARG B 2 204 ? 29.548 109.641 46.927 1.00 27.25 ? 204 ARG B CD 1 ATOM 3500 N NE . ARG B 2 204 ? 29.638 108.916 48.198 1.00 28.48 ? 204 ARG B NE 1 ATOM 3501 C CZ . ARG B 2 204 ? 29.053 107.746 48.477 1.00 29.50 ? 204 ARG B CZ 1 ATOM 3502 N NH1 . ARG B 2 204 ? 28.288 107.094 47.588 1.00 28.35 ? 204 ARG B NH1 1 ATOM 3503 N NH2 . ARG B 2 204 ? 29.234 107.208 49.687 1.00 31.63 ? 204 ARG B NH2 1 ATOM 3504 N N . ARG B 2 205 ? 28.783 111.477 42.586 1.00 24.33 ? 205 ARG B N 1 ATOM 3505 C CA . ARG B 2 205 ? 28.805 112.480 41.537 1.00 24.37 ? 205 ARG B CA 1 ATOM 3506 C C . ARG B 2 205 ? 30.249 112.728 41.108 1.00 24.12 ? 205 ARG B C 1 ATOM 3507 O O . ARG B 2 205 ? 31.134 112.858 41.950 1.00 21.73 ? 205 ARG B O 1 ATOM 3508 C CB . ARG B 2 205 ? 28.170 113.783 42.040 1.00 27.14 ? 205 ARG B CB 1 ATOM 3509 C CG . ARG B 2 205 ? 28.154 114.925 41.023 1.00 29.15 ? 205 ARG B CG 1 ATOM 3510 C CD . ARG B 2 205 ? 27.803 116.258 41.683 1.00 32.01 ? 205 ARG B CD 1 ATOM 3511 N N . CYS B 2 206 ? 30.489 112.784 39.797 1.00 24.82 ? 206 CYS B N 1 ATOM 3512 C CA . CYS B 2 206 ? 31.848 112.987 39.275 1.00 25.51 ? 206 CYS B CA 1 ATOM 3513 C C . CYS B 2 206 ? 32.417 114.342 39.710 1.00 24.02 ? 206 CYS B C 1 ATOM 3514 O O . CYS B 2 206 ? 31.711 115.335 39.686 1.00 23.99 ? 206 CYS B O 1 ATOM 3515 C CB . CYS B 2 206 ? 31.859 112.834 37.746 1.00 27.93 ? 206 CYS B CB 1 ATOM 3516 S SG . CYS B 2 206 ? 31.090 111.268 37.205 1.00 31.36 ? 206 CYS B SG 1 ATOM 3517 N N . ASP B 2 207 ? 33.665 114.356 40.173 1.00 23.24 ? 207 ASP B N 1 ATOM 3518 C CA . ASP B 2 207 ? 34.326 115.585 40.633 1.00 23.85 ? 207 ASP B CA 1 ATOM 3519 C C . ASP B 2 207 ? 35.789 115.673 40.228 1.00 22.84 ? 207 ASP B C 1 ATOM 3520 O O . ASP B 2 207 ? 36.505 116.537 40.718 1.00 22.67 ? 207 ASP B O 1 ATOM 3521 C CB . ASP B 2 207 ? 34.200 115.729 42.172 1.00 25.56 ? 207 ASP B CB 1 ATOM 3522 C CG . ASP B 2 207 ? 34.759 114.512 42.941 1.00 27.99 ? 207 ASP B CG 1 ATOM 3523 O OD1 . ASP B 2 207 ? 35.399 113.630 42.311 1.00 30.00 ? 207 ASP B OD1 1 ATOM 3524 O OD2 . ASP B 2 207 ? 34.534 114.419 44.178 1.00 30.35 ? 207 ASP B OD2 1 ATOM 3525 N N . GLY B 2 208 ? 36.242 114.790 39.344 1.00 22.26 ? 208 GLY B N 1 ATOM 3526 C CA . GLY B 2 208 ? 37.625 114.803 38.871 1.00 22.60 ? 208 GLY B CA 1 ATOM 3527 C C . GLY B 2 208 ? 38.689 114.372 39.866 1.00 22.36 ? 208 GLY B C 1 ATOM 3528 O O . GLY B 2 208 ? 39.882 114.604 39.641 1.00 22.08 ? 208 GLY B O 1 ATOM 3529 N N . SER B 2 209 ? 38.260 113.730 40.949 1.00 22.60 ? 209 SER B N 1 ATOM 3530 C CA . SER B 2 209 ? 39.146 113.389 42.052 1.00 23.03 ? 209 SER B CA 1 ATOM 3531 C C . SER B 2 209 ? 40.039 112.189 41.750 1.00 22.98 ? 209 SER B C 1 ATOM 3532 O O . SER B 2 209 ? 39.835 111.450 40.773 1.00 22.78 ? 209 SER B O 1 ATOM 3533 C CB . SER B 2 209 ? 38.328 113.109 43.323 1.00 23.68 ? 209 SER B CB 1 ATOM 3534 O OG . SER B 2 209 ? 37.490 111.956 43.191 1.00 23.25 ? 209 SER B OG 1 ATOM 3535 N N . ILE B 2 210 ? 41.025 112.012 42.626 1.00 23.53 ? 210 ILE B N 1 ATOM 3536 C CA . ILE B 2 210 ? 41.870 110.819 42.675 1.00 24.14 ? 210 ILE B CA 1 ATOM 3537 C C . ILE B 2 210 ? 40.999 109.596 42.878 1.00 23.60 ? 210 ILE B C 1 ATOM 3538 O O . ILE B 2 210 ? 41.305 108.526 42.339 1.00 23.24 ? 210 ILE B O 1 ATOM 3539 C CB . ILE B 2 210 ? 42.897 110.876 43.835 1.00 24.74 ? 210 ILE B CB 1 ATOM 3540 C CG1 . ILE B 2 210 ? 43.852 112.059 43.657 1.00 25.51 ? 210 ILE B CG1 1 ATOM 3541 C CG2 . ILE B 2 210 ? 43.730 109.599 43.894 1.00 24.62 ? 210 ILE B CG2 1 ATOM 3542 C CD1 . ILE B 2 210 ? 44.459 112.558 44.953 1.00 25.78 ? 210 ILE B CD1 1 ATOM 3543 N N . ASN B 2 211 ? 39.902 109.780 43.619 1.00 22.19 ? 211 ASN B N 1 ATOM 3544 C CA . ASN B 2 211 ? 39.037 108.678 44.026 1.00 22.64 ? 211 ASN B CA 1 ATOM 3545 C C . ASN B 2 211 ? 38.331 108.008 42.850 1.00 22.67 ? 211 ASN B C 1 ATOM 3546 O O . ASN B 2 211 ? 37.889 106.866 42.971 1.00 21.52 ? 211 ASN B O 1 ATOM 3547 C CB . ASN B 2 211 ? 37.955 109.146 45.023 1.00 22.44 ? 211 ASN B CB 1 ATOM 3548 C CG . ASN B 2 211 ? 38.523 109.618 46.352 1.00 22.50 ? 211 ASN B CG 1 ATOM 3549 O OD1 . ASN B 2 211 ? 39.262 110.599 46.401 1.00 23.24 ? 211 ASN B OD1 1 ATOM 3550 N ND2 . ASN B 2 211 ? 38.197 108.922 47.419 1.00 21.95 ? 211 ASN B ND2 1 ATOM 3551 N N . GLN B 2 212 ? 38.198 108.744 41.744 1.00 21.80 ? 212 GLN B N 1 ATOM 3552 C CA . GLN B 2 212 ? 37.406 108.329 40.602 1.00 21.33 ? 212 GLN B CA 1 ATOM 3553 C C . GLN B 2 212 ? 38.271 107.994 39.384 1.00 20.41 ? 212 GLN B C 1 ATOM 3554 O O . GLN B 2 212 ? 37.734 107.700 38.328 1.00 19.19 ? 212 GLN B O 1 ATOM 3555 C CB . GLN B 2 212 ? 36.379 109.439 40.283 1.00 21.80 ? 212 GLN B CB 1 ATOM 3556 C CG . GLN B 2 212 ? 35.277 109.527 41.330 1.00 21.87 ? 212 GLN B CG 1 ATOM 3557 C CD . GLN B 2 212 ? 34.434 110.795 41.269 1.00 22.82 ? 212 GLN B CD 1 ATOM 3558 O OE1 . GLN B 2 212 ? 34.605 111.642 40.397 1.00 21.76 ? 212 GLN B OE1 1 ATOM 3559 N NE2 . GLN B 2 212 ? 33.507 110.927 42.226 1.00 22.93 ? 212 GLN B NE2 1 ATOM 3560 N N . ARG B 2 213 ? 39.579 107.985 39.536 1.00 20.82 ? 213 ARG B N 1 ATOM 3561 C CA . ARG B 2 213 ? 40.519 107.616 38.496 1.00 21.59 ? 213 ARG B CA 1 ATOM 3562 C C . ARG B 2 213 ? 40.892 106.132 38.516 1.00 20.70 ? 213 ARG B C 1 ATOM 3563 O O . ARG B 2 213 ? 41.546 105.694 39.420 1.00 20.93 ? 213 ARG B O 1 ATOM 3564 C CB . ARG B 2 213 ? 41.792 108.437 38.589 1.00 22.50 ? 213 ARG B CB 1 ATOM 3565 C CG . ARG B 2 213 ? 42.454 108.707 37.258 1.00 23.99 ? 213 ARG B CG 1 ATOM 3566 C CD . ARG B 2 213 ? 43.532 107.687 37.012 1.00 25.60 ? 213 ARG B CD 1 ATOM 3567 N NE . ARG B 2 213 ? 44.406 107.939 35.877 1.00 26.49 ? 213 ARG B NE 1 ATOM 3568 C CZ . ARG B 2 213 ? 45.383 108.830 35.814 1.00 26.69 ? 213 ARG B CZ 1 ATOM 3569 N NH1 . ARG B 2 213 ? 45.624 109.635 36.795 1.00 28.04 ? 213 ARG B NH1 1 ATOM 3570 N NH2 . ARG B 2 213 ? 46.100 108.920 34.741 1.00 27.95 ? 213 ARG B NH2 1 ATOM 3571 N N . TRP B 2 214 ? 40.473 105.397 37.502 1.00 19.31 ? 214 TRP B N 1 ATOM 3572 C CA . TRP B 2 214 ? 40.720 103.952 37.433 1.00 18.90 ? 214 TRP B CA 1 ATOM 3573 C C . TRP B 2 214 ? 41.452 103.537 36.163 1.00 18.91 ? 214 TRP B C 1 ATOM 3574 O O . TRP B 2 214 ? 41.168 104.051 35.089 1.00 18.26 ? 214 TRP B O 1 ATOM 3575 C CB . TRP B 2 214 ? 39.403 103.206 37.508 1.00 19.11 ? 214 TRP B CB 1 ATOM 3576 C CG . TRP B 2 214 ? 38.643 103.534 38.711 1.00 19.90 ? 214 TRP B CG 1 ATOM 3577 C CD1 . TRP B 2 214 ? 37.597 104.407 38.809 1.00 20.90 ? 214 TRP B CD1 1 ATOM 3578 C CD2 . TRP B 2 214 ? 38.877 103.033 40.025 1.00 20.08 ? 214 TRP B CD2 1 ATOM 3579 N NE1 . TRP B 2 214 ? 37.147 104.463 40.105 1.00 21.15 ? 214 TRP B NE1 1 ATOM 3580 C CE2 . TRP B 2 214 ? 37.916 103.630 40.874 1.00 20.82 ? 214 TRP B CE2 1 ATOM 3581 C CE3 . TRP B 2 214 ? 39.803 102.133 40.570 1.00 19.30 ? 214 TRP B CE3 1 ATOM 3582 C CZ2 . TRP B 2 214 ? 37.847 103.347 42.241 1.00 20.77 ? 214 TRP B CZ2 1 ATOM 3583 C CZ3 . TRP B 2 214 ? 39.741 101.858 41.917 1.00 19.42 ? 214 TRP B CZ3 1 ATOM 3584 C CH2 . TRP B 2 214 ? 38.766 102.457 42.743 1.00 20.45 ? 214 TRP B CH2 1 ATOM 3585 N N . VAL B 2 215 ? 42.369 102.580 36.301 1.00 18.49 ? 215 VAL B N 1 ATOM 3586 C CA . VAL B 2 215 ? 43.187 102.098 35.203 1.00 18.13 ? 215 VAL B CA 1 ATOM 3587 C C . VAL B 2 215 ? 42.992 100.586 35.063 1.00 17.71 ? 215 VAL B C 1 ATOM 3588 O O . VAL B 2 215 ? 43.228 99.833 36.005 1.00 15.96 ? 215 VAL B O 1 ATOM 3589 C CB . VAL B 2 215 ? 44.686 102.424 35.434 1.00 18.65 ? 215 VAL B CB 1 ATOM 3590 C CG1 . VAL B 2 215 ? 45.536 101.842 34.312 1.00 18.94 ? 215 VAL B CG1 1 ATOM 3591 C CG2 . VAL B 2 215 ? 44.912 103.930 35.531 1.00 18.88 ? 215 VAL B CG2 1 ATOM 3592 N N . PHE B 2 216 ? 42.556 100.159 33.880 1.00 18.21 ? 216 PHE B N 1 ATOM 3593 C CA . PHE B 2 216 ? 42.410 98.747 33.573 1.00 18.61 ? 216 PHE B CA 1 ATOM 3594 C C . PHE B 2 216 ? 43.769 98.273 33.098 1.00 19.21 ? 216 PHE B C 1 ATOM 3595 O O . PHE B 2 216 ? 44.175 98.573 31.977 1.00 20.75 ? 216 PHE B O 1 ATOM 3596 C CB . PHE B 2 216 ? 41.326 98.511 32.528 1.00 18.62 ? 216 PHE B CB 1 ATOM 3597 C CG . PHE B 2 216 ? 39.937 98.785 33.030 1.00 18.32 ? 216 PHE B CG 1 ATOM 3598 C CD1 . PHE B 2 216 ? 39.442 100.079 33.062 1.00 18.25 ? 216 PHE B CD1 1 ATOM 3599 C CD2 . PHE B 2 216 ? 39.127 97.749 33.473 1.00 17.99 ? 216 PHE B CD2 1 ATOM 3600 C CE1 . PHE B 2 216 ? 38.165 100.336 33.537 1.00 18.59 ? 216 PHE B CE1 1 ATOM 3601 C CE2 . PHE B 2 216 ? 37.853 97.990 33.941 1.00 17.88 ? 216 PHE B CE2 1 ATOM 3602 C CZ . PHE B 2 216 ? 37.367 99.290 33.972 1.00 18.83 ? 216 PHE B CZ 1 ATOM 3603 N N . THR B 2 217 ? 44.486 97.570 33.972 1.00 18.61 ? 217 THR B N 1 ATOM 3604 C CA . THR B 2 217 ? 45.866 97.187 33.703 1.00 18.99 ? 217 THR B CA 1 ATOM 3605 C C . THR B 2 217 ? 45.891 95.912 32.871 1.00 19.46 ? 217 THR B C 1 ATOM 3606 O O . THR B 2 217 ? 44.935 95.162 32.908 1.00 19.73 ? 217 THR B O 1 ATOM 3607 C CB . THR B 2 217 ? 46.624 96.888 34.998 1.00 18.69 ? 217 THR B CB 1 ATOM 3608 O OG1 . THR B 2 217 ? 46.051 95.732 35.627 1.00 17.47 ? 217 THR B OG1 1 ATOM 3609 C CG2 . THR B 2 217 ? 46.580 98.092 35.945 1.00 18.58 ? 217 THR B CG2 1 ATOM 3610 N N . PRO B 2 218 ? 47.000 95.634 32.163 1.00 20.57 ? 218 PRO B N 1 ATOM 3611 C CA . PRO B 2 218 ? 47.063 94.374 31.394 1.00 21.47 ? 218 PRO B CA 1 ATOM 3612 C C . PRO B 2 218 ? 47.055 93.125 32.274 1.00 21.59 ? 218 PRO B C 1 ATOM 3613 O O . PRO B 2 218 ? 46.556 92.111 31.836 1.00 22.64 ? 218 PRO B O 1 ATOM 3614 C CB . PRO B 2 218 ? 48.374 94.472 30.613 1.00 20.95 ? 218 PRO B CB 1 ATOM 3615 C CG . PRO B 2 218 ? 48.898 95.834 30.856 1.00 21.76 ? 218 PRO B CG 1 ATOM 3616 C CD . PRO B 2 218 ? 48.259 96.387 32.081 1.00 20.91 ? 218 PRO B CD 1 ATOM 3617 N N . GLN B 2 219 ? 47.547 93.223 33.506 1.00 21.72 ? 219 GLN B N 1 ATOM 3618 C CA . GLN B 2 219 ? 47.454 92.119 34.465 1.00 22.13 ? 219 GLN B CA 1 ATOM 3619 C C . GLN B 2 219 ? 46.040 91.847 34.991 1.00 22.02 ? 219 GLN B C 1 ATOM 3620 O O . GLN B 2 219 ? 45.852 90.936 35.796 1.00 23.73 ? 219 GLN B O 1 ATOM 3621 C CB . GLN B 2 219 ? 48.443 92.287 35.623 1.00 22.95 ? 219 GLN B CB 1 ATOM 3622 C CG . GLN B 2 219 ? 48.276 93.512 36.508 1.00 23.36 ? 219 GLN B CG 1 ATOM 3623 C CD . GLN B 2 219 ? 49.129 94.709 36.079 1.00 24.01 ? 219 GLN B CD 1 ATOM 3624 O OE1 . GLN B 2 219 ? 49.476 94.866 34.906 1.00 24.60 ? 219 GLN B OE1 1 ATOM 3625 N NE2 . GLN B 2 219 ? 49.446 95.574 37.033 1.00 23.61 ? 219 GLN B NE2 1 ATOM 3626 N N . GLY B 2 220 ? 45.057 92.628 34.550 1.00 20.63 ? 220 GLY B N 1 ATOM 3627 C CA . GLY B 2 220 ? 43.661 92.340 34.805 1.00 19.64 ? 220 GLY B CA 1 ATOM 3628 C C . GLY B 2 220 ? 43.174 92.856 36.149 1.00 19.38 ? 220 GLY B C 1 ATOM 3629 O O . GLY B 2 220 ? 42.235 92.306 36.713 1.00 19.04 ? 220 GLY B O 1 ATOM 3630 N N . THR B 2 221 ? 43.806 93.904 36.663 1.00 18.49 ? 221 THR B N 1 ATOM 3631 C CA . THR B 2 221 ? 43.298 94.607 37.849 1.00 18.81 ? 221 THR B CA 1 ATOM 3632 C C . THR B 2 221 ? 42.638 95.907 37.400 1.00 18.26 ? 221 THR B C 1 ATOM 3633 O O . THR B 2 221 ? 42.793 96.311 36.246 1.00 16.41 ? 221 THR B O 1 ATOM 3634 C CB . THR B 2 221 ? 44.426 94.894 38.853 1.00 18.98 ? 221 THR B CB 1 ATOM 3635 O OG1 . THR B 2 221 ? 45.465 95.664 38.221 1.00 18.79 ? 221 THR B OG1 1 ATOM 3636 C CG2 . THR B 2 221 ? 45.021 93.576 39.376 1.00 19.27 ? 221 THR B CG2 1 ATOM 3637 N N . ILE B 2 222 ? 41.846 96.497 38.293 1.00 17.96 ? 222 ILE B N 1 ATOM 3638 C CA . ILE B 2 222 ? 41.304 97.841 38.119 1.00 17.93 ? 222 ILE B CA 1 ATOM 3639 C C . ILE B 2 222 ? 42.009 98.699 39.178 1.00 18.28 ? 222 ILE B C 1 ATOM 3640 O O . ILE B 2 222 ? 41.667 98.655 40.351 1.00 17.48 ? 222 ILE B O 1 ATOM 3641 C CB . ILE B 2 222 ? 39.774 97.889 38.250 1.00 18.73 ? 222 ILE B CB 1 ATOM 3642 C CG1 . ILE B 2 222 ? 39.115 96.919 37.243 1.00 19.13 ? 222 ILE B CG1 1 ATOM 3643 C CG2 . ILE B 2 222 ? 39.269 99.312 38.013 1.00 18.62 ? 222 ILE B CG2 1 ATOM 3644 C CD1 . ILE B 2 222 ? 37.632 96.677 37.471 1.00 19.16 ? 222 ILE B CD1 1 ATOM 3645 N N . SER B 2 223 ? 43.026 99.441 38.740 1.00 18.22 ? 223 SER B N 1 ATOM 3646 C CA . SER B 2 223 ? 43.966 100.117 39.625 1.00 19.10 ? 223 SER B CA 1 ATOM 3647 C C . SER B 2 223 ? 43.600 101.581 39.837 1.00 19.72 ? 223 SER B C 1 ATOM 3648 O O . SER B 2 223 ? 43.227 102.272 38.906 1.00 19.23 ? 223 SER B O 1 ATOM 3649 C CB . SER B 2 223 ? 45.370 100.032 39.057 1.00 18.82 ? 223 SER B CB 1 ATOM 3650 O OG . SER B 2 223 ? 46.202 101.005 39.658 1.00 21.32 ? 223 SER B OG 1 ATOM 3651 N N . ASN B 2 224 ? 43.697 102.041 41.077 1.00 21.41 ? 224 ASN B N 1 ATOM 3652 C CA . ASN B 2 224 ? 43.652 103.477 41.373 1.00 23.34 ? 224 ASN B CA 1 ATOM 3653 C C . ASN B 2 224 ? 45.083 103.927 41.596 1.00 23.46 ? 224 ASN B C 1 ATOM 3654 O O . ASN B 2 224 ? 45.619 103.727 42.673 1.00 24.90 ? 224 ASN B O 1 ATOM 3655 C CB . ASN B 2 224 ? 42.786 103.750 42.599 1.00 23.87 ? 224 ASN B CB 1 ATOM 3656 C CG . ASN B 2 224 ? 42.542 105.234 42.821 1.00 23.98 ? 224 ASN B CG 1 ATOM 3657 O OD1 . ASN B 2 224 ? 43.491 106.006 42.939 1.00 25.24 ? 224 ASN B OD1 1 ATOM 3658 N ND2 . ASN B 2 224 ? 41.277 105.637 42.882 1.00 22.92 ? 224 ASN B ND2 1 ATOM 3659 N N . PRO B 2 225 ? 45.717 104.525 40.579 1.00 24.42 ? 225 PRO B N 1 ATOM 3660 C CA . PRO B 2 225 ? 47.157 104.799 40.684 1.00 25.71 ? 225 PRO B CA 1 ATOM 3661 C C . PRO B 2 225 ? 47.542 105.871 41.725 1.00 28.14 ? 225 PRO B C 1 ATOM 3662 O O . PRO B 2 225 ? 48.700 105.920 42.144 1.00 29.04 ? 225 PRO B O 1 ATOM 3663 C CB . PRO B 2 225 ? 47.521 105.269 39.274 1.00 25.12 ? 225 PRO B CB 1 ATOM 3664 C CG . PRO B 2 225 ? 46.266 105.897 38.775 1.00 25.15 ? 225 PRO B CG 1 ATOM 3665 C CD . PRO B 2 225 ? 45.163 105.022 39.307 1.00 24.57 ? 225 PRO B CD 1 ATOM 3666 N N . GLY B 2 226 ? 46.590 106.718 42.119 1.00 28.87 ? 226 GLY B N 1 ATOM 3667 C CA . GLY B 2 226 ? 46.822 107.713 43.162 1.00 30.21 ? 226 GLY B CA 1 ATOM 3668 C C . GLY B 2 226 ? 46.956 107.122 44.550 1.00 30.55 ? 226 GLY B C 1 ATOM 3669 O O . GLY B 2 226 ? 47.798 107.568 45.320 1.00 30.45 ? 226 GLY B O 1 ATOM 3670 N N . TYR B 2 227 ? 46.129 106.120 44.861 1.00 30.90 ? 227 TYR B N 1 ATOM 3671 C CA . TYR B 2 227 ? 46.164 105.436 46.152 1.00 31.39 ? 227 TYR B CA 1 ATOM 3672 C C . TYR B 2 227 ? 46.917 104.116 46.118 1.00 30.62 ? 227 TYR B C 1 ATOM 3673 O O . TYR B 2 227 ? 46.820 103.340 47.059 1.00 29.97 ? 227 TYR B O 1 ATOM 3674 C CB . TYR B 2 227 ? 44.740 105.200 46.669 1.00 32.85 ? 227 TYR B CB 1 ATOM 3675 C CG . TYR B 2 227 ? 43.950 106.464 46.872 1.00 35.17 ? 227 TYR B CG 1 ATOM 3676 C CD1 . TYR B 2 227 ? 44.503 107.547 47.560 1.00 37.71 ? 227 TYR B CD1 1 ATOM 3677 C CD2 . TYR B 2 227 ? 42.644 106.587 46.399 1.00 35.90 ? 227 TYR B CD2 1 ATOM 3678 C CE1 . TYR B 2 227 ? 43.790 108.716 47.755 1.00 38.75 ? 227 TYR B CE1 1 ATOM 3679 C CE2 . TYR B 2 227 ? 41.924 107.758 46.600 1.00 37.15 ? 227 TYR B CE2 1 ATOM 3680 C CZ . TYR B 2 227 ? 42.508 108.817 47.277 1.00 37.43 ? 227 TYR B CZ 1 ATOM 3681 O OH . TYR B 2 227 ? 41.831 109.990 47.496 1.00 40.91 ? 227 TYR B OH 1 ATOM 3682 N N . GLU B 2 228 ? 47.661 103.867 45.042 1.00 32.40 ? 228 GLU B N 1 ATOM 3683 C CA . GLU B 2 228 ? 48.452 102.651 44.873 1.00 33.41 ? 228 GLU B CA 1 ATOM 3684 C C . GLU B 2 228 ? 47.723 101.404 45.367 1.00 30.68 ? 228 GLU B C 1 ATOM 3685 O O . GLU B 2 228 ? 48.254 100.642 46.169 1.00 30.90 ? 228 GLU B O 1 ATOM 3686 C CB . GLU B 2 228 ? 49.790 102.819 45.584 1.00 37.80 ? 228 GLU B CB 1 ATOM 3687 C CG . GLU B 2 228 ? 50.557 104.041 45.121 1.00 42.24 ? 228 GLU B CG 1 ATOM 3688 C CD . GLU B 2 228 ? 51.948 104.099 45.704 1.00 47.10 ? 228 GLU B CD 1 ATOM 3689 O OE1 . GLU B 2 228 ? 52.914 104.267 44.926 1.00 53.47 ? 228 GLU B OE1 1 ATOM 3690 O OE2 . GLU B 2 228 ? 52.073 103.972 46.940 1.00 49.18 ? 228 GLU B OE2 1 ATOM 3691 N N . ALA B 2 229 ? 46.489 101.229 44.908 1.00 27.69 ? 229 ALA B N 1 ATOM 3692 C CA . ALA B 2 229 ? 45.667 100.088 45.307 1.00 26.42 ? 229 ALA B CA 1 ATOM 3693 C C . ALA B 2 229 ? 44.730 99.663 44.166 1.00 25.26 ? 229 ALA B C 1 ATOM 3694 O O . ALA B 2 229 ? 44.671 100.337 43.145 1.00 25.28 ? 229 ALA B O 1 ATOM 3695 C CB . ALA B 2 229 ? 44.900 100.434 46.564 1.00 26.33 ? 229 ALA B CB 1 ATOM 3696 N N . VAL B 2 230 ? 44.027 98.537 44.337 1.00 23.28 ? 230 VAL B N 1 ATOM 3697 C CA . VAL B 2 230 ? 43.207 97.945 43.285 1.00 21.27 ? 230 VAL B CA 1 ATOM 3698 C C . VAL B 2 230 ? 41.834 97.568 43.821 1.00 21.10 ? 230 VAL B C 1 ATOM 3699 O O . VAL B 2 230 ? 41.661 97.456 45.040 1.00 20.02 ? 230 VAL B O 1 ATOM 3700 C CB . VAL B 2 230 ? 43.909 96.723 42.631 1.00 20.86 ? 230 VAL B CB 1 ATOM 3701 C CG1 . VAL B 2 230 ? 45.327 97.094 42.203 1.00 20.50 ? 230 VAL B CG1 1 ATOM 3702 C CG2 . VAL B 2 230 ? 43.925 95.495 43.538 1.00 20.29 ? 230 VAL B CG2 1 ATOM 3703 N N . MET B 2 231 ? 40.864 97.393 42.920 1.00 19.84 ? 231 MET B N 1 ATOM 3704 C CA . MET B 2 231 ? 39.541 96.945 43.315 1.00 21.26 ? 231 MET B CA 1 ATOM 3705 C C . MET B 2 231 ? 39.590 95.480 43.719 1.00 21.60 ? 231 MET B C 1 ATOM 3706 O O . MET B 2 231 ? 40.218 94.670 43.045 1.00 19.94 ? 231 MET B O 1 ATOM 3707 C CB . MET B 2 231 ? 38.521 97.076 42.192 1.00 22.27 ? 231 MET B CB 1 ATOM 3708 C CG . MET B 2 231 ? 38.149 98.494 41.848 1.00 23.84 ? 231 MET B CG 1 ATOM 3709 S SD . MET B 2 231 ? 36.791 98.620 40.678 1.00 24.71 ? 231 MET B SD 1 ATOM 3710 C CE . MET B 2 231 ? 35.470 97.707 41.429 1.00 26.58 ? 231 MET B CE 1 ATOM 3711 N N . ASP B 2 232 ? 38.881 95.150 44.792 1.00 22.63 ? 232 ASP B N 1 ATOM 3712 C CA . ASP B 2 232 ? 38.911 93.810 45.356 1.00 23.24 ? 232 ASP B CA 1 ATOM 3713 C C . ASP B 2 232 ? 37.534 93.456 45.894 1.00 22.68 ? 232 ASP B C 1 ATOM 3714 O O . ASP B 2 232 ? 36.862 94.292 46.490 1.00 23.89 ? 232 ASP B O 1 ATOM 3715 C CB . ASP B 2 232 ? 39.967 93.759 46.466 1.00 25.28 ? 232 ASP B CB 1 ATOM 3716 C CG . ASP B 2 232 ? 40.435 92.323 46.812 1.00 28.42 ? 232 ASP B CG 1 ATOM 3717 O OD1 . ASP B 2 232 ? 39.970 91.306 46.227 1.00 31.74 ? 232 ASP B OD1 1 ATOM 3718 O OD2 . ASP B 2 232 ? 41.297 92.215 47.699 1.00 29.67 ? 232 ASP B OD2 1 ATOM 3719 N N . VAL B 2 233 ? 37.123 92.212 45.684 1.00 21.81 ? 233 VAL B N 1 ATOM 3720 C CA . VAL B 2 233 ? 35.898 91.700 46.262 1.00 21.83 ? 233 VAL B CA 1 ATOM 3721 C C . VAL B 2 233 ? 36.209 91.408 47.735 1.00 22.83 ? 233 VAL B C 1 ATOM 3722 O O . VAL B 2 233 ? 37.161 90.685 48.032 1.00 21.99 ? 233 VAL B O 1 ATOM 3723 C CB . VAL B 2 233 ? 35.424 90.418 45.548 1.00 22.13 ? 233 VAL B CB 1 ATOM 3724 C CG1 . VAL B 2 233 ? 34.148 89.883 46.196 1.00 22.02 ? 233 VAL B CG1 1 ATOM 3725 C CG2 . VAL B 2 233 ? 35.212 90.667 44.047 1.00 21.66 ? 233 VAL B CG2 1 ATOM 3726 N N . ALA B 2 234 ? 35.418 91.977 48.644 1.00 23.11 ? 234 ALA B N 1 ATOM 3727 C CA . ALA B 2 234 ? 35.698 91.878 50.082 1.00 24.29 ? 234 ALA B CA 1 ATOM 3728 C C . ALA B 2 234 ? 35.728 90.426 50.502 1.00 25.47 ? 234 ALA B C 1 ATOM 3729 O O . ALA B 2 234 ? 34.800 89.686 50.188 1.00 26.98 ? 234 ALA B O 1 ATOM 3730 C CB . ALA B 2 234 ? 34.659 92.632 50.887 1.00 23.17 ? 234 ALA B CB 1 ATOM 3731 N N . GLN B 2 235 ? 36.817 90.012 51.156 1.00 27.81 ? 235 GLN B N 1 ATOM 3732 C CA . GLN B 2 235 ? 36.994 88.622 51.651 1.00 28.39 ? 235 GLN B CA 1 ATOM 3733 C C . GLN B 2 235 ? 36.934 87.559 50.553 1.00 27.04 ? 235 GLN B C 1 ATOM 3734 O O . GLN B 2 235 ? 36.680 86.393 50.848 1.00 26.01 ? 235 GLN B O 1 ATOM 3735 C CB . GLN B 2 235 ? 35.930 88.279 52.720 1.00 29.28 ? 235 GLN B CB 1 ATOM 3736 C CG . GLN B 2 235 ? 35.766 89.301 53.826 1.00 31.12 ? 235 GLN B CG 1 ATOM 3737 C CD . GLN B 2 235 ? 37.004 89.428 54.692 1.00 33.46 ? 235 GLN B CD 1 ATOM 3738 O OE1 . GLN B 2 235 ? 37.716 88.448 54.926 1.00 36.38 ? 235 GLN B OE1 1 ATOM 3739 N NE2 . GLN B 2 235 ? 37.258 90.631 55.191 1.00 34.95 ? 235 GLN B NE2 1 ATOM 3740 N N . ASN B 2 236 ? 37.164 87.958 49.299 1.00 26.95 ? 236 ASN B N 1 ATOM 3741 C CA . ASN B 2 236 ? 36.857 87.130 48.127 1.00 26.32 ? 236 ASN B CA 1 ATOM 3742 C C . ASN B 2 236 ? 35.488 86.476 48.226 1.00 26.18 ? 236 ASN B C 1 ATOM 3743 O O . ASN B 2 236 ? 35.332 85.309 47.900 1.00 25.06 ? 236 ASN B O 1 ATOM 3744 C CB . ASN B 2 236 ? 37.947 86.073 47.907 1.00 26.93 ? 236 ASN B CB 1 ATOM 3745 C CG . ASN B 2 236 ? 39.283 86.685 47.564 1.00 28.00 ? 236 ASN B CG 1 ATOM 3746 O OD1 . ASN B 2 236 ? 39.620 86.855 46.399 1.00 29.55 ? 236 ASN B OD1 1 ATOM 3747 N ND2 . ASN B 2 236 ? 40.056 87.019 48.579 1.00 29.70 ? 236 ASN B ND2 1 ATOM 3748 N N . ASP B 2 237 ? 34.504 87.233 48.704 1.00 27.54 ? 237 ASP B N 1 ATOM 3749 C CA . ASP B 2 237 ? 33.156 86.714 48.929 1.00 28.70 ? 237 ASP B CA 1 ATOM 3750 C C . ASP B 2 237 ? 32.151 87.652 48.279 1.00 27.50 ? 237 ASP B C 1 ATOM 3751 O O . ASP B 2 237 ? 31.867 88.717 48.803 1.00 26.03 ? 237 ASP B O 1 ATOM 3752 C CB . ASP B 2 237 ? 32.872 86.570 50.434 1.00 30.83 ? 237 ASP B CB 1 ATOM 3753 C CG . ASP B 2 237 ? 31.529 85.892 50.722 1.00 33.33 ? 237 ASP B CG 1 ATOM 3754 O OD1 . ASP B 2 237 ? 30.727 85.654 49.776 1.00 33.78 ? 237 ASP B OD1 1 ATOM 3755 O OD2 . ASP B 2 237 ? 31.279 85.597 51.914 1.00 35.49 ? 237 ASP B OD2 1 ATOM 3756 N N . VAL B 2 238 ? 31.630 87.236 47.126 1.00 27.32 ? 238 VAL B N 1 ATOM 3757 C CA . VAL B 2 238 ? 30.672 88.031 46.366 1.00 26.52 ? 238 VAL B CA 1 ATOM 3758 C C . VAL B 2 238 ? 29.372 88.260 47.107 1.00 27.08 ? 238 VAL B C 1 ATOM 3759 O O . VAL B 2 238 ? 28.698 89.245 46.850 1.00 25.98 ? 238 VAL B O 1 ATOM 3760 C CB . VAL B 2 238 ? 30.354 87.428 44.964 1.00 26.10 ? 238 VAL B CB 1 ATOM 3761 C CG1 . VAL B 2 238 ? 31.596 87.406 44.101 1.00 25.68 ? 238 VAL B CG1 1 ATOM 3762 C CG2 . VAL B 2 238 ? 29.707 86.040 45.052 1.00 26.46 ? 238 VAL B CG2 1 ATOM 3763 N N . TYR B 2 239 ? 29.021 87.361 48.023 1.00 29.65 ? 239 TYR B N 1 ATOM 3764 C CA . TYR B 2 239 ? 27.780 87.497 48.780 1.00 31.42 ? 239 TYR B CA 1 ATOM 3765 C C . TYR B 2 239 ? 27.837 88.544 49.900 1.00 29.23 ? 239 TYR B C 1 ATOM 3766 O O . TYR B 2 239 ? 26.801 88.941 50.394 1.00 30.52 ? 239 TYR B O 1 ATOM 3767 C CB . TYR B 2 239 ? 27.280 86.118 49.249 1.00 35.18 ? 239 TYR B CB 1 ATOM 3768 C CG . TYR B 2 239 ? 27.009 85.227 48.049 1.00 39.13 ? 239 TYR B CG 1 ATOM 3769 C CD1 . TYR B 2 239 ? 25.967 85.527 47.159 1.00 42.05 ? 239 TYR B CD1 1 ATOM 3770 C CD2 . TYR B 2 239 ? 27.832 84.134 47.757 1.00 41.66 ? 239 TYR B CD2 1 ATOM 3771 C CE1 . TYR B 2 239 ? 25.735 84.752 46.030 1.00 44.01 ? 239 TYR B CE1 1 ATOM 3772 C CE2 . TYR B 2 239 ? 27.609 83.347 46.629 1.00 42.98 ? 239 TYR B CE2 1 ATOM 3773 C CZ . TYR B 2 239 ? 26.559 83.658 45.771 1.00 45.86 ? 239 TYR B CZ 1 ATOM 3774 O OH . TYR B 2 239 ? 26.319 82.886 44.656 1.00 49.85 ? 239 TYR B OH 1 ATOM 3775 N N . LEU B 2 240 ? 29.022 89.042 50.255 1.00 28.26 ? 240 LEU B N 1 ATOM 3776 C CA . LEU B 2 240 ? 29.121 90.221 51.131 1.00 26.04 ? 240 LEU B CA 1 ATOM 3777 C C . LEU B 2 240 ? 28.686 91.535 50.471 1.00 25.18 ? 240 LEU B C 1 ATOM 3778 O O . LEU B 2 240 ? 28.449 92.516 51.176 1.00 23.97 ? 240 LEU B O 1 ATOM 3779 C CB . LEU B 2 240 ? 30.535 90.376 51.680 1.00 26.51 ? 240 LEU B CB 1 ATOM 3780 C CG . LEU B 2 240 ? 31.027 89.241 52.578 1.00 27.45 ? 240 LEU B CG 1 ATOM 3781 C CD1 . LEU B 2 240 ? 32.488 89.460 52.906 1.00 27.44 ? 240 LEU B CD1 1 ATOM 3782 C CD2 . LEU B 2 240 ? 30.201 89.138 53.859 1.00 27.34 ? 240 LEU B CD2 1 ATOM 3783 N N . LYS B 2 241 ? 28.602 91.568 49.136 1.00 23.98 ? 241 LYS B N 1 ATOM 3784 C CA . LYS B 2 241 ? 28.101 92.739 48.394 1.00 23.10 ? 241 LYS B CA 1 ATOM 3785 C C . LYS B 2 241 ? 28.890 94.000 48.711 1.00 20.52 ? 241 LYS B C 1 ATOM 3786 O O . LYS B 2 241 ? 28.337 95.086 48.895 1.00 20.16 ? 241 LYS B O 1 ATOM 3787 C CB . LYS B 2 241 ? 26.612 92.941 48.649 1.00 25.23 ? 241 LYS B CB 1 ATOM 3788 C CG . LYS B 2 241 ? 25.757 91.781 48.167 1.00 27.74 ? 241 LYS B CG 1 ATOM 3789 C CD . LYS B 2 241 ? 24.300 92.057 48.460 1.00 30.37 ? 241 LYS B CD 1 ATOM 3790 C CE . LYS B 2 241 ? 23.414 90.987 47.861 1.00 32.91 ? 241 LYS B CE 1 ATOM 3791 N NZ . LYS B 2 241 ? 21.995 91.447 47.858 1.00 36.09 ? 241 LYS B NZ 1 ATOM 3792 N N . LYS B 2 242 ? 30.201 93.827 48.751 1.00 19.11 ? 242 LYS B N 1 ATOM 3793 C CA . LYS B 2 242 ? 31.134 94.881 49.093 1.00 19.17 ? 242 LYS B CA 1 ATOM 3794 C C . LYS B 2 242 ? 32.375 94.745 48.224 1.00 18.63 ? 242 LYS B C 1 ATOM 3795 O O . LYS B 2 242 ? 33.007 93.685 48.199 1.00 17.09 ? 242 LYS B O 1 ATOM 3796 C CB . LYS B 2 242 ? 31.530 94.786 50.567 1.00 19.22 ? 242 LYS B CB 1 ATOM 3797 C CG . LYS B 2 242 ? 30.497 95.350 51.515 1.00 19.04 ? 242 LYS B CG 1 ATOM 3798 C CD . LYS B 2 242 ? 30.994 95.294 52.959 1.00 19.12 ? 242 LYS B CD 1 ATOM 3799 C CE . LYS B 2 242 ? 30.110 96.109 53.878 1.00 19.26 ? 242 LYS B CE 1 ATOM 3800 N NZ . LYS B 2 242 ? 28.690 95.665 53.823 1.00 19.51 ? 242 LYS B NZ 1 ATOM 3801 N N . ILE B 2 243 ? 32.698 95.825 47.505 1.00 17.57 ? 243 ILE B N 1 ATOM 3802 C CA . ILE B 2 243 ? 33.922 95.897 46.730 1.00 17.60 ? 243 ILE B CA 1 ATOM 3803 C C . ILE B 2 243 ? 34.746 96.932 47.422 1.00 17.08 ? 243 ILE B C 1 ATOM 3804 O O . ILE B 2 243 ? 34.231 98.006 47.736 1.00 17.15 ? 243 ILE B O 1 ATOM 3805 C CB . ILE B 2 243 ? 33.682 96.342 45.263 1.00 17.81 ? 243 ILE B CB 1 ATOM 3806 C CG1 . ILE B 2 243 ? 32.546 95.547 44.630 1.00 18.10 ? 243 ILE B CG1 1 ATOM 3807 C CG2 . ILE B 2 243 ? 34.967 96.213 44.451 1.00 18.33 ? 243 ILE B CG2 1 ATOM 3808 C CD1 . ILE B 2 243 ? 32.750 94.031 44.626 1.00 18.98 ? 243 ILE B CD1 1 ATOM 3809 N N . VAL B 2 244 ? 36.022 96.622 47.641 1.00 17.30 ? 244 VAL B N 1 ATOM 3810 C CA . VAL B 2 244 ? 36.895 97.484 48.403 1.00 17.66 ? 244 VAL B CA 1 ATOM 3811 C C . VAL B 2 244 ? 38.164 97.750 47.659 1.00 18.04 ? 244 VAL B C 1 ATOM 3812 O O . VAL B 2 244 ? 38.499 97.067 46.702 1.00 17.96 ? 244 VAL B O 1 ATOM 3813 C CB . VAL B 2 244 ? 37.236 96.926 49.820 1.00 18.07 ? 244 VAL B CB 1 ATOM 3814 C CG1 . VAL B 2 244 ? 35.970 96.733 50.643 1.00 18.39 ? 244 VAL B CG1 1 ATOM 3815 C CG2 . VAL B 2 244 ? 38.044 95.630 49.765 1.00 17.97 ? 244 VAL B CG2 1 ATOM 3816 N N . LEU B 2 245 ? 38.851 98.785 48.110 1.00 19.44 ? 245 LEU B N 1 ATOM 3817 C CA . LEU B 2 245 ? 40.180 99.122 47.623 1.00 21.13 ? 245 LEU B CA 1 ATOM 3818 C C . LEU B 2 245 ? 41.229 98.445 48.516 1.00 22.31 ? 245 LEU B C 1 ATOM 3819 O O . LEU B 2 245 ? 41.157 98.540 49.744 1.00 24.23 ? 245 LEU B O 1 ATOM 3820 C CB . LEU B 2 245 ? 40.334 100.631 47.642 1.00 21.06 ? 245 LEU B CB 1 ATOM 3821 C CG . LEU B 2 245 ? 41.405 101.227 46.754 1.00 22.14 ? 245 LEU B CG 1 ATOM 3822 C CD1 . LEU B 2 245 ? 41.032 101.073 45.282 1.00 22.54 ? 245 LEU B CD1 1 ATOM 3823 C CD2 . LEU B 2 245 ? 41.670 102.687 47.104 1.00 22.68 ? 245 LEU B CD2 1 ATOM 3824 N N . SER B 2 246 ? 42.179 97.751 47.899 1.00 24.27 ? 246 SER B N 1 ATOM 3825 C CA . SER B 2 246 ? 43.233 97.000 48.605 1.00 25.97 ? 246 SER B CA 1 ATOM 3826 C C . SER B 2 246 ? 44.558 97.045 47.850 1.00 27.09 ? 246 SER B C 1 ATOM 3827 O O . SER B 2 246 ? 44.585 97.155 46.612 1.00 25.39 ? 246 SER B O 1 ATOM 3828 C CB . SER B 2 246 ? 42.837 95.533 48.748 1.00 26.73 ? 246 SER B CB 1 ATOM 3829 O OG . SER B 2 246 ? 41.501 95.423 49.173 1.00 29.62 ? 246 SER B OG 1 ATOM 3830 N N . SER B 2 247 ? 45.659 96.908 48.579 1.00 28.87 ? 247 SER B N 1 ATOM 3831 C CA . SER B 2 247 ? 46.968 96.796 47.941 1.00 32.82 ? 247 SER B CA 1 ATOM 3832 C C . SER B 2 247 ? 46.978 95.501 47.111 1.00 34.31 ? 247 SER B C 1 ATOM 3833 O O . SER B 2 247 ? 46.420 94.490 47.537 1.00 35.87 ? 247 SER B O 1 ATOM 3834 C CB . SER B 2 247 ? 48.069 96.781 48.986 1.00 33.45 ? 247 SER B CB 1 ATOM 3835 O OG . SER B 2 247 ? 48.002 95.575 49.711 1.00 36.36 ? 247 SER B OG 1 ATOM 3836 N N . ALA B 2 248 ? 47.576 95.546 45.924 1.00 36.00 ? 248 ALA B N 1 ATOM 3837 C CA . ALA B 2 248 ? 47.533 94.407 45.000 1.00 39.38 ? 248 ALA B CA 1 ATOM 3838 C C . ALA B 2 248 ? 48.229 93.172 45.575 1.00 43.39 ? 248 ALA B C 1 ATOM 3839 O O . ALA B 2 248 ? 49.333 93.264 46.093 1.00 44.38 ? 248 ALA B O 1 ATOM 3840 C CB . ALA B 2 248 ? 48.154 94.768 43.660 1.00 38.79 ? 248 ALA B CB 1 ATOM 3841 N N . THR B 2 249 ? 47.564 92.028 45.499 1.00 48.44 ? 249 THR B N 1 ATOM 3842 C CA . THR B 2 249 ? 48.156 90.757 45.900 1.00 53.35 ? 249 THR B CA 1 ATOM 3843 C C . THR B 2 249 ? 47.362 89.631 45.253 1.00 57.63 ? 249 THR B C 1 ATOM 3844 O O . THR B 2 249 ? 46.135 89.733 45.110 1.00 59.27 ? 249 THR B O 1 ATOM 3845 C CB . THR B 2 249 ? 48.197 90.597 47.446 1.00 53.99 ? 249 THR B CB 1 ATOM 3846 O OG1 . THR B 2 249 ? 49.080 89.519 47.799 1.00 55.56 ? 249 THR B OG1 1 ATOM 3847 C CG2 . THR B 2 249 ? 46.796 90.356 48.042 1.00 52.09 ? 249 THR B CG2 1 ATOM 3848 N N . ASP B 2 250 ? 48.050 88.567 44.850 1.00 62.17 ? 250 ASP B N 1 ATOM 3849 C CA . ASP B 2 250 ? 47.362 87.384 44.338 1.00 66.27 ? 250 ASP B CA 1 ATOM 3850 C C . ASP B 2 250 ? 47.053 86.423 45.504 1.00 65.65 ? 250 ASP B C 1 ATOM 3851 O O . ASP B 2 250 ? 47.647 85.349 45.614 1.00 66.84 ? 250 ASP B O 1 ATOM 3852 C CB . ASP B 2 250 ? 48.179 86.726 43.212 1.00 68.27 ? 250 ASP B CB 1 ATOM 3853 C CG . ASP B 2 250 ? 47.303 85.985 42.202 1.00 71.09 ? 250 ASP B CG 1 ATOM 3854 O OD1 . ASP B 2 250 ? 46.240 85.436 42.578 1.00 72.30 ? 250 ASP B OD1 1 ATOM 3855 O OD2 . ASP B 2 250 ? 47.684 85.953 41.017 1.00 72.45 ? 250 ASP B OD2 1 ATOM 3856 N N . LYS B 2 251 ? 46.124 86.839 46.376 1.00 64.74 ? 251 LYS B N 1 ATOM 3857 C CA . LYS B 2 251 ? 45.667 86.025 47.509 1.00 63.92 ? 251 LYS B CA 1 ATOM 3858 C C . LYS B 2 251 ? 44.591 85.070 47.010 1.00 62.28 ? 251 LYS B C 1 ATOM 3859 O O . LYS B 2 251 ? 44.656 83.868 47.244 1.00 66.53 ? 251 LYS B O 1 ATOM 3860 C CB . LYS B 2 251 ? 45.115 86.903 48.637 1.00 64.92 ? 251 LYS B CB 1 ATOM 3861 N N . GLY B 2 252 ? 43.598 85.630 46.330 1.00 58.31 ? 252 GLY B N 1 ATOM 3862 C CA . GLY B 2 252 ? 42.601 84.858 45.596 1.00 52.58 ? 252 GLY B CA 1 ATOM 3863 C C . GLY B 2 252 ? 42.508 85.391 44.172 1.00 47.17 ? 252 GLY B C 1 ATOM 3864 O O . GLY B 2 252 ? 43.532 85.757 43.569 1.00 43.33 ? 252 GLY B O 1 ATOM 3865 N N . ASN B 2 253 ? 41.282 85.410 43.642 1.00 40.41 ? 253 ASN B N 1 ATOM 3866 C CA . ASN B 2 253 ? 40.969 85.996 42.331 1.00 36.64 ? 253 ASN B CA 1 ATOM 3867 C C . ASN B 2 253 ? 40.074 87.238 42.459 1.00 30.70 ? 253 ASN B C 1 ATOM 3868 O O . ASN B 2 253 ? 39.596 87.761 41.465 1.00 27.46 ? 253 ASN B O 1 ATOM 3869 C CB . ASN B 2 253 ? 40.300 84.952 41.428 1.00 37.99 ? 253 ASN B CB 1 ATOM 3870 C CG . ASN B 2 253 ? 41.270 83.891 40.966 1.00 40.75 ? 253 ASN B CG 1 ATOM 3871 O OD1 . ASN B 2 253 ? 41.893 83.202 41.778 1.00 43.53 ? 253 ASN B OD1 1 ATOM 3872 N ND2 . ASN B 2 253 ? 41.386 83.736 39.651 1.00 40.32 ? 253 ASN B ND2 1 ATOM 3873 N N . GLY B 2 254 ? 39.873 87.717 43.684 1.00 25.62 ? 254 GLY B N 1 ATOM 3874 C CA . GLY B 2 254 ? 39.050 88.864 43.923 1.00 24.54 ? 254 GLY B CA 1 ATOM 3875 C C . GLY B 2 254 ? 39.540 90.136 43.269 1.00 23.59 ? 254 GLY B C 1 ATOM 3876 O O . GLY B 2 254 ? 38.757 91.066 43.128 1.00 23.32 ? 254 GLY B O 1 ATOM 3877 N N . GLN B 2 255 ? 40.815 90.184 42.865 1.00 21.90 ? 255 GLN B N 1 ATOM 3878 C CA . GLN B 2 255 ? 41.371 91.359 42.194 1.00 20.93 ? 255 GLN B CA 1 ATOM 3879 C C . GLN B 2 255 ? 41.455 91.239 40.668 1.00 20.33 ? 255 GLN B C 1 ATOM 3880 O O . GLN B 2 255 ? 41.992 92.132 40.006 1.00 19.76 ? 255 GLN B O 1 ATOM 3881 C CB . GLN B 2 255 ? 42.744 91.684 42.785 1.00 20.66 ? 255 GLN B CB 1 ATOM 3882 C CG . GLN B 2 255 ? 42.666 91.967 44.280 1.00 20.12 ? 255 GLN B CG 1 ATOM 3883 C CD . GLN B 2 255 ? 43.981 92.374 44.891 1.00 20.49 ? 255 GLN B CD 1 ATOM 3884 O OE1 . GLN B 2 255 ? 45.006 92.425 44.224 1.00 21.67 ? 255 GLN B OE1 1 ATOM 3885 N NE2 . GLN B 2 255 ? 43.957 92.676 46.173 1.00 21.43 ? 255 GLN B NE2 1 ATOM 3886 N N . GLN B 2 256 ? 40.914 90.152 40.113 1.00 20.16 ? 256 GLN B N 1 ATOM 3887 C CA . GLN B 2 256 ? 40.896 89.958 38.663 1.00 19.70 ? 256 GLN B CA 1 ATOM 3888 C C . GLN B 2 256 ? 39.581 90.418 38.055 1.00 18.94 ? 256 GLN B C 1 ATOM 3889 O O . GLN B 2 256 ? 38.512 90.063 38.538 1.00 19.51 ? 256 GLN B O 1 ATOM 3890 C CB . GLN B 2 256 ? 41.158 88.493 38.302 1.00 20.63 ? 256 GLN B CB 1 ATOM 3891 C CG . GLN B 2 256 ? 42.622 88.089 38.400 1.00 21.27 ? 256 GLN B CG 1 ATOM 3892 C CD . GLN B 2 256 ? 43.525 88.914 37.496 1.00 21.71 ? 256 GLN B CD 1 ATOM 3893 O OE1 . GLN B 2 256 ? 43.438 88.824 36.270 1.00 24.55 ? 256 GLN B OE1 1 ATOM 3894 N NE2 . GLN B 2 256 ? 44.404 89.700 38.089 1.00 21.17 ? 256 GLN B NE2 1 ATOM 3895 N N . TRP B 2 257 ? 39.671 91.192 36.975 1.00 18.37 ? 257 TRP B N 1 ATOM 3896 C CA . TRP B 2 257 ? 38.506 91.732 36.297 1.00 18.26 ? 257 TRP B CA 1 ATOM 3897 C C . TRP B 2 257 ? 38.608 91.623 34.768 1.00 19.08 ? 257 TRP B C 1 ATOM 3898 O O . TRP B 2 257 ? 39.703 91.559 34.203 1.00 17.51 ? 257 TRP B O 1 ATOM 3899 C CB . TRP B 2 257 ? 38.309 93.202 36.705 1.00 18.41 ? 257 TRP B CB 1 ATOM 3900 C CG . TRP B 2 257 ? 38.160 93.391 38.185 1.00 17.35 ? 257 TRP B CG 1 ATOM 3901 C CD1 . TRP B 2 257 ? 39.157 93.584 39.083 1.00 17.36 ? 257 TRP B CD1 1 ATOM 3902 C CD2 . TRP B 2 257 ? 36.944 93.380 38.927 1.00 17.50 ? 257 TRP B CD2 1 ATOM 3903 N NE1 . TRP B 2 257 ? 38.644 93.710 40.355 1.00 17.23 ? 257 TRP B NE1 1 ATOM 3904 C CE2 . TRP B 2 257 ? 37.282 93.587 40.288 1.00 17.62 ? 257 TRP B CE2 1 ATOM 3905 C CE3 . TRP B 2 257 ? 35.598 93.215 38.582 1.00 17.38 ? 257 TRP B CE3 1 ATOM 3906 C CZ2 . TRP B 2 257 ? 36.318 93.643 41.299 1.00 17.56 ? 257 TRP B CZ2 1 ATOM 3907 C CZ3 . TRP B 2 257 ? 34.643 93.260 39.582 1.00 17.76 ? 257 TRP B CZ3 1 ATOM 3908 C CH2 . TRP B 2 257 ? 35.008 93.479 40.933 1.00 17.99 ? 257 TRP B CH2 1 ATOM 3909 N N . THR B 2 258 ? 37.443 91.599 34.120 1.00 20.52 ? 258 THR B N 1 ATOM 3910 C CA . THR B 2 258 ? 37.340 91.603 32.662 1.00 22.58 ? 258 THR B CA 1 ATOM 3911 C C . THR B 2 258 ? 36.395 92.726 32.171 1.00 23.39 ? 258 THR B C 1 ATOM 3912 O O . THR B 2 258 ? 35.310 92.938 32.727 1.00 22.52 ? 258 THR B O 1 ATOM 3913 C CB . THR B 2 258 ? 36.828 90.255 32.127 1.00 22.14 ? 258 THR B CB 1 ATOM 3914 O OG1 . THR B 2 258 ? 37.654 89.203 32.636 1.00 22.86 ? 258 THR B OG1 1 ATOM 3915 C CG2 . THR B 2 258 ? 36.877 90.212 30.608 1.00 23.37 ? 258 THR B CG2 1 ATOM 3916 N N . VAL B 2 259 ? 36.823 93.409 31.113 1.00 24.12 ? 259 VAL B N 1 ATOM 3917 C CA . VAL B 2 259 ? 35.990 94.375 30.393 1.00 25.13 ? 259 VAL B CA 1 ATOM 3918 C C . VAL B 2 259 ? 35.331 93.645 29.234 1.00 25.15 ? 259 VAL B C 1 ATOM 3919 O O . VAL B 2 259 ? 36.018 93.169 28.330 1.00 25.71 ? 259 VAL B O 1 ATOM 3920 C CB . VAL B 2 259 ? 36.845 95.531 29.867 1.00 25.44 ? 259 VAL B CB 1 ATOM 3921 C CG1 . VAL B 2 259 ? 35.968 96.606 29.238 1.00 26.42 ? 259 VAL B CG1 1 ATOM 3922 C CG2 . VAL B 2 259 ? 37.671 96.106 31.007 1.00 24.93 ? 259 VAL B CG2 1 ATOM 3923 N N . PHE B 2 260 ? 34.007 93.526 29.288 1.00 25.45 ? 260 PHE B N 1 ATOM 3924 C CA . PHE B 2 260 ? 33.233 92.896 28.227 1.00 26.06 ? 260 PHE B CA 1 ATOM 3925 C C . PHE B 2 260 ? 32.337 93.936 27.521 1.00 24.84 ? 260 PHE B C 1 ATOM 3926 O O . PHE B 2 260 ? 31.350 94.413 28.069 1.00 24.52 ? 260 PHE B O 1 ATOM 3927 C CB . PHE B 2 260 ? 32.444 91.727 28.799 1.00 27.82 ? 260 PHE B CB 1 ATOM 3928 C CG . PHE B 2 260 ? 31.784 90.880 27.767 1.00 30.77 ? 260 PHE B CG 1 ATOM 3929 C CD1 . PHE B 2 260 ? 32.541 90.062 26.938 1.00 32.61 ? 260 PHE B CD1 1 ATOM 3930 C CD2 . PHE B 2 260 ? 30.406 90.896 27.616 1.00 34.69 ? 260 PHE B CD2 1 ATOM 3931 C CE1 . PHE B 2 260 ? 31.934 89.263 25.983 1.00 34.36 ? 260 PHE B CE1 1 ATOM 3932 C CE2 . PHE B 2 260 ? 29.789 90.105 26.655 1.00 36.70 ? 260 PHE B CE2 1 ATOM 3933 C CZ . PHE B 2 260 ? 30.556 89.288 25.838 1.00 36.53 ? 260 PHE B CZ 1 ATOM 3934 N N . TYR B 2 261 ? 32.699 94.261 26.286 1.00 23.27 ? 261 TYR B N 1 ATOM 3935 C CA . TYR B 2 261 ? 32.184 95.431 25.564 1.00 22.09 ? 261 TYR B CA 1 ATOM 3936 C C . TYR B 2 261 ? 31.512 94.955 24.283 1.00 22.85 ? 261 TYR B C 1 ATOM 3937 O O . TYR B 2 261 ? 30.996 95.768 23.503 1.00 24.11 ? 261 TYR B O 1 ATOM 3938 C CB . TYR B 2 261 ? 33.340 96.397 25.226 1.00 21.48 ? 261 TYR B CB 1 ATOM 3939 C CG . TYR B 2 261 ? 34.394 95.751 24.346 1.00 20.87 ? 261 TYR B CG 1 ATOM 3940 C CD1 . TYR B 2 261 ? 34.232 95.702 22.965 1.00 20.26 ? 261 TYR B CD1 1 ATOM 3941 C CD2 . TYR B 2 261 ? 35.524 95.122 24.896 1.00 20.76 ? 261 TYR B CD2 1 ATOM 3942 C CE1 . TYR B 2 261 ? 35.166 95.080 22.157 1.00 19.86 ? 261 TYR B CE1 1 ATOM 3943 C CE2 . TYR B 2 261 ? 36.467 94.490 24.089 1.00 19.83 ? 261 TYR B CE2 1 ATOM 3944 C CZ . TYR B 2 261 ? 36.277 94.470 22.714 1.00 19.82 ? 261 TYR B CZ 1 ATOM 3945 O OH . TYR B 2 261 ? 37.180 93.861 21.866 1.00 18.23 ? 261 TYR B OH 1 HETATM 3946 C C1 . NAG C 3 . ? 50.031 78.505 2.988 1.00 54.64 ? 301 NAG A C1 1 HETATM 3947 C C2 . NAG C 3 . ? 49.661 78.772 1.544 1.00 60.67 ? 301 NAG A C2 1 HETATM 3948 C C3 . NAG C 3 . ? 50.798 79.144 0.597 1.00 59.76 ? 301 NAG A C3 1 HETATM 3949 C C4 . NAG C 3 . ? 51.942 79.911 1.230 1.00 58.81 ? 301 NAG A C4 1 HETATM 3950 C C5 . NAG C 3 . ? 52.184 79.485 2.648 1.00 58.77 ? 301 NAG A C5 1 HETATM 3951 C C6 . NAG C 3 . ? 53.038 80.514 3.331 1.00 61.56 ? 301 NAG A C6 1 HETATM 3952 C C7 . NAG C 3 . ? 47.653 77.722 0.831 1.00 65.06 ? 301 NAG A C7 1 HETATM 3953 C C8 . NAG C 3 . ? 46.942 76.428 0.686 1.00 63.71 ? 301 NAG A C8 1 HETATM 3954 N N2 . NAG C 3 . ? 48.945 77.626 1.031 1.00 63.83 ? 301 NAG A N2 1 HETATM 3955 O O3 . NAG C 3 . ? 50.245 79.890 -0.484 1.00 59.32 ? 301 NAG A O3 1 HETATM 3956 O O4 . NAG C 3 . ? 53.101 79.606 0.482 1.00 58.55 ? 301 NAG A O4 1 HETATM 3957 O O5 . NAG C 3 . ? 50.962 79.514 3.312 1.00 56.21 ? 301 NAG A O5 1 HETATM 3958 O O6 . NAG C 3 . ? 53.493 80.022 4.589 1.00 62.70 ? 301 NAG A O6 1 HETATM 3959 O O7 . NAG C 3 . ? 47.089 78.799 0.790 1.00 70.08 ? 301 NAG A O7 1 HETATM 3960 P P . PO4 D 4 . ? 62.093 75.188 10.428 1.00 55.15 ? 302 PO4 A P 1 HETATM 3961 O O1 . PO4 D 4 . ? 62.542 75.317 8.990 1.00 58.14 ? 302 PO4 A O1 1 HETATM 3962 O O2 . PO4 D 4 . ? 61.358 76.443 10.842 1.00 55.79 ? 302 PO4 A O2 1 HETATM 3963 O O3 . PO4 D 4 . ? 63.313 75.020 11.302 1.00 56.23 ? 302 PO4 A O3 1 HETATM 3964 O O4 . PO4 D 4 . ? 61.187 73.987 10.561 1.00 54.52 ? 302 PO4 A O4 1 HETATM 3965 C C1 . NAG E 3 . ? 42.266 131.415 31.258 1.00 41.89 ? 301 NAG B C1 1 HETATM 3966 C C2 . NAG E 3 . ? 41.902 132.281 32.452 1.00 45.12 ? 301 NAG B C2 1 HETATM 3967 C C3 . NAG E 3 . ? 41.687 133.732 32.106 1.00 45.73 ? 301 NAG B C3 1 HETATM 3968 C C4 . NAG E 3 . ? 42.853 134.236 31.292 1.00 45.32 ? 301 NAG B C4 1 HETATM 3969 C C5 . NAG E 3 . ? 43.171 133.309 30.113 1.00 42.72 ? 301 NAG B C5 1 HETATM 3970 C C6 . NAG E 3 . ? 44.514 133.605 29.493 1.00 41.04 ? 301 NAG B C6 1 HETATM 3971 C C7 . NAG E 3 . ? 40.672 131.299 34.298 1.00 49.74 ? 301 NAG B C7 1 HETATM 3972 C C8 . NAG E 3 . ? 41.890 131.347 35.146 1.00 49.25 ? 301 NAG B C8 1 HETATM 3973 N N2 . NAG E 3 . ? 40.723 131.762 33.061 1.00 46.93 ? 301 NAG B N2 1 HETATM 3974 O O3 . NAG E 3 . ? 41.673 134.451 33.335 1.00 50.20 ? 301 NAG B O3 1 HETATM 3975 O O4 . NAG E 3 . ? 42.612 135.587 30.905 1.00 47.79 ? 301 NAG B O4 1 HETATM 3976 O O5 . NAG E 3 . ? 43.309 131.972 30.513 1.00 40.92 ? 301 NAG B O5 1 HETATM 3977 O O6 . NAG E 3 . ? 45.499 133.863 30.471 1.00 39.29 ? 301 NAG B O6 1 HETATM 3978 O O7 . NAG E 3 . ? 39.668 130.852 34.767 1.00 52.34 ? 301 NAG B O7 1 HETATM 3979 C C1 . FUC F 5 . ? 40.370 134.480 33.956 1.00 57.59 ? 302 FUC B C1 1 HETATM 3980 C C2 . FUC F 5 . ? 40.325 135.190 35.307 1.00 60.18 ? 302 FUC B C2 1 HETATM 3981 C C3 . FUC F 5 . ? 40.850 136.586 35.052 1.00 62.07 ? 302 FUC B C3 1 HETATM 3982 C C4 . FUC F 5 . ? 39.894 137.280 34.103 1.00 61.15 ? 302 FUC B C4 1 HETATM 3983 C C5 . FUC F 5 . ? 40.000 136.510 32.814 1.00 59.21 ? 302 FUC B C5 1 HETATM 3984 C C6 . FUC F 5 . ? 39.160 137.096 31.706 1.00 57.76 ? 302 FUC B C6 1 HETATM 3985 O O2 . FUC F 5 . ? 41.056 134.576 36.348 1.00 56.40 ? 302 FUC B O2 1 HETATM 3986 O O3 . FUC F 5 . ? 41.052 137.271 36.275 1.00 62.91 ? 302 FUC B O3 1 HETATM 3987 O O4 . FUC F 5 . ? 38.580 137.138 34.618 1.00 60.66 ? 302 FUC B O4 1 HETATM 3988 O O5 . FUC F 5 . ? 39.527 135.224 33.127 1.00 58.40 ? 302 FUC B O5 1 HETATM 3989 C C1 . NAG G 3 . ? 43.739 136.617 31.371 1.00 63.19 ? 303 NAG B C1 1 HETATM 3990 C C2 . NAG G 3 . ? 43.949 137.927 30.618 1.00 65.06 ? 303 NAG B C2 1 HETATM 3991 C C3 . NAG G 3 . ? 45.121 138.714 31.188 1.00 68.01 ? 303 NAG B C3 1 HETATM 3992 C C4 . NAG G 3 . ? 44.956 138.868 32.691 1.00 68.11 ? 303 NAG B C4 1 HETATM 3993 C C5 . NAG G 3 . ? 44.769 137.502 33.337 1.00 66.42 ? 303 NAG B C5 1 HETATM 3994 C C6 . NAG G 3 . ? 44.586 137.634 34.845 1.00 64.77 ? 303 NAG B C6 1 HETATM 3995 C C7 . NAG G 3 . ? 43.155 137.440 28.378 1.00 60.93 ? 303 NAG B C7 1 HETATM 3996 C C8 . NAG G 3 . ? 43.534 137.133 26.959 1.00 58.56 ? 303 NAG B C8 1 HETATM 3997 N N2 . NAG G 3 . ? 44.169 137.661 29.210 1.00 63.27 ? 303 NAG B N2 1 HETATM 3998 O O3 . NAG G 3 . ? 45.174 140.008 30.576 1.00 66.75 ? 303 NAG B O3 1 HETATM 3999 O O4 . NAG G 3 . ? 46.117 139.503 33.239 1.00 70.50 ? 303 NAG B O4 1 HETATM 4000 O O5 . NAG G 3 . ? 43.632 136.843 32.778 1.00 64.17 ? 303 NAG B O5 1 HETATM 4001 O O6 . NAG G 3 . ? 44.576 136.331 35.440 1.00 64.86 ? 303 NAG B O6 1 HETATM 4002 O O7 . NAG G 3 . ? 41.992 137.483 28.745 1.00 57.85 ? 303 NAG B O7 1 HETATM 4003 C C1 . NAG H 3 . ? 62.091 125.861 29.965 1.00 66.08 ? 304 NAG B C1 1 HETATM 4004 C C2 . NAG H 3 . ? 63.560 126.287 30.102 1.00 66.42 ? 304 NAG B C2 1 HETATM 4005 C C3 . NAG H 3 . ? 63.736 127.801 30.034 1.00 66.76 ? 304 NAG B C3 1 HETATM 4006 C C4 . NAG H 3 . ? 62.948 128.407 28.912 1.00 66.67 ? 304 NAG B C4 1 HETATM 4007 C C5 . NAG H 3 . ? 61.511 127.992 29.125 1.00 68.07 ? 304 NAG B C5 1 HETATM 4008 C C6 . NAG H 3 . ? 60.584 128.708 28.171 1.00 67.07 ? 304 NAG B C6 1 HETATM 4009 C C7 . NAG H 3 . ? 64.555 124.720 31.558 1.00 63.67 ? 304 NAG B C7 1 HETATM 4010 C C8 . NAG H 3 . ? 64.648 124.313 32.976 1.00 63.19 ? 304 NAG B C8 1 HETATM 4011 N N2 . NAG H 3 . ? 64.038 125.901 31.380 1.00 65.13 ? 304 NAG B N2 1 HETATM 4012 O O3 . NAG H 3 . ? 65.092 128.164 29.857 1.00 67.84 ? 304 NAG B O3 1 HETATM 4013 O O4 . NAG H 3 . ? 63.137 129.799 29.002 1.00 67.86 ? 304 NAG B O4 1 HETATM 4014 O O5 . NAG H 3 . ? 61.487 126.583 28.911 1.00 67.32 ? 304 NAG B O5 1 HETATM 4015 O O6 . NAG H 3 . ? 61.153 128.642 26.879 1.00 64.62 ? 304 NAG B O6 1 HETATM 4016 O O7 . NAG H 3 . ? 64.931 124.025 30.655 1.00 63.30 ? 304 NAG B O7 1 HETATM 4017 C C1 . NAG I 3 . ? 58.836 121.665 30.015 1.00 40.36 ? 305 NAG B C1 1 HETATM 4018 C C2 . NAG I 3 . ? 58.779 122.541 28.806 1.00 40.99 ? 305 NAG B C2 1 HETATM 4019 C C3 . NAG I 3 . ? 60.050 123.374 28.620 1.00 42.78 ? 305 NAG B C3 1 HETATM 4020 C C4 . NAG I 3 . ? 60.516 124.089 29.879 1.00 43.42 ? 305 NAG B C4 1 HETATM 4021 C C5 . NAG I 3 . ? 60.217 123.353 31.162 1.00 44.25 ? 305 NAG B C5 1 HETATM 4022 C C6 . NAG I 3 . ? 59.851 124.485 32.093 1.00 44.70 ? 305 NAG B C6 1 HETATM 4023 C C7 . NAG I 3 . ? 57.362 121.412 27.212 1.00 40.50 ? 305 NAG B C7 1 HETATM 4024 C C8 . NAG I 3 . ? 57.290 120.597 25.972 1.00 40.36 ? 305 NAG B C8 1 HETATM 4025 N N2 . NAG I 3 . ? 58.563 121.712 27.654 1.00 40.29 ? 305 NAG B N2 1 HETATM 4026 O O3 . NAG I 3 . ? 59.805 124.353 27.628 1.00 42.54 ? 305 NAG B O3 1 HETATM 4027 O O4 . NAG I 3 . ? 61.902 124.427 29.878 1.00 44.24 ? 305 NAG B O4 1 HETATM 4028 O O5 . NAG I 3 . ? 59.137 122.426 31.159 1.00 41.88 ? 305 NAG B O5 1 HETATM 4029 O O6 . NAG I 3 . ? 60.036 124.112 33.425 1.00 46.58 ? 305 NAG B O6 1 HETATM 4030 O O7 . NAG I 3 . ? 56.367 121.759 27.762 1.00 39.99 ? 305 NAG B O7 1 HETATM 4031 C C1 . BMA J 6 . ? 47.276 141.284 33.756 0.50 40.09 ? 306 BMA B C1 1 HETATM 4032 C C2 . BMA J 6 . ? 47.623 141.817 32.385 0.50 40.11 ? 306 BMA B C2 1 HETATM 4033 C C3 . BMA J 6 . ? 48.649 140.914 31.729 0.50 40.53 ? 306 BMA B C3 1 HETATM 4034 C C4 . BMA J 6 . ? 49.911 140.817 32.571 0.50 40.71 ? 306 BMA B C4 1 HETATM 4035 C C5 . BMA J 6 . ? 49.517 140.381 33.967 0.50 41.06 ? 306 BMA B C5 1 HETATM 4036 C C6 . BMA J 6 . ? 50.768 140.399 34.828 0.50 40.79 ? 306 BMA B C6 1 HETATM 4037 O O2 . BMA J 6 . ? 48.125 143.137 32.496 0.50 39.52 ? 306 BMA B O2 1 HETATM 4038 O O3 . BMA J 6 . ? 48.927 141.424 30.424 0.50 42.12 ? 306 BMA B O3 1 HETATM 4039 O O4 . BMA J 6 . ? 50.812 139.816 32.076 0.50 40.37 ? 306 BMA B O4 1 HETATM 4040 O O5 . BMA J 6 . ? 48.479 141.196 34.514 0.50 41.50 ? 306 BMA B O5 1 HETATM 4041 O O6 . BMA J 6 . ? 50.721 139.361 35.798 0.50 41.33 ? 306 BMA B O6 1 HETATM 4042 C C1 . EDO K 7 . ? 22.820 109.362 30.780 1.00 42.85 ? 307 EDO B C1 1 HETATM 4043 O O1 . EDO K 7 . ? 23.312 110.479 31.540 1.00 38.42 ? 307 EDO B O1 1 HETATM 4044 C C2 . EDO K 7 . ? 23.162 109.515 29.297 1.00 44.47 ? 307 EDO B C2 1 HETATM 4045 O O2 . EDO K 7 . ? 23.395 108.220 28.720 1.00 46.31 ? 307 EDO B O2 1 HETATM 4046 C C1 . PGE L 8 . ? 22.610 105.281 27.278 1.00 35.49 ? 308 PGE B C1 1 HETATM 4047 O O1 . PGE L 8 . ? 21.351 105.351 27.951 1.00 34.28 ? 308 PGE B O1 1 HETATM 4048 C C2 . PGE L 8 . ? 22.683 103.969 26.504 1.00 36.60 ? 308 PGE B C2 1 HETATM 4049 O O2 . PGE L 8 . ? 23.962 103.846 25.871 1.00 37.26 ? 308 PGE B O2 1 HETATM 4050 C C3 . PGE L 8 . ? 24.553 102.547 25.730 1.00 36.95 ? 308 PGE B C3 1 HETATM 4051 C C4 . PGE L 8 . ? 23.655 101.432 25.208 1.00 38.32 ? 308 PGE B C4 1 HETATM 4052 O O4 . PGE L 8 . ? 21.752 98.618 27.509 1.00 43.87 ? 308 PGE B O4 1 HETATM 4053 C C6 . PGE L 8 . ? 23.078 99.093 27.294 1.00 40.71 ? 308 PGE B C6 1 HETATM 4054 C C5 . PGE L 8 . ? 23.379 99.106 25.809 1.00 40.44 ? 308 PGE B C5 1 HETATM 4055 O O3 . PGE L 8 . ? 24.274 100.184 25.532 1.00 40.96 ? 308 PGE B O3 1 HETATM 4056 C C1 . GAL M 9 . ? 36.403 128.348 17.823 1.00 35.48 ? 309 GAL B C1 1 HETATM 4057 C C2 . GAL M 9 . ? 36.892 126.923 17.613 1.00 34.19 ? 309 GAL B C2 1 HETATM 4058 C C3 . GAL M 9 . ? 36.597 125.985 18.788 1.00 32.61 ? 309 GAL B C3 1 HETATM 4059 C C4 . GAL M 9 . ? 36.930 126.618 20.130 1.00 31.09 ? 309 GAL B C4 1 HETATM 4060 C C5 . GAL M 9 . ? 36.161 127.918 20.183 1.00 31.15 ? 309 GAL B C5 1 HETATM 4061 C C6 . GAL M 9 . ? 36.310 128.559 21.552 1.00 30.25 ? 309 GAL B C6 1 HETATM 4062 O O2 . GAL M 9 . ? 36.336 126.351 16.439 1.00 36.47 ? 309 GAL B O2 1 HETATM 4063 O O3 . GAL M 9 . ? 37.333 124.809 18.644 1.00 31.21 ? 309 GAL B O3 1 HETATM 4064 O O4 . GAL M 9 . ? 38.314 126.838 20.318 1.00 28.40 ? 309 GAL B O4 1 HETATM 4065 O O5 . GAL M 9 . ? 36.623 128.754 19.150 1.00 32.32 ? 309 GAL B O5 1 HETATM 4066 O O6 . GAL M 9 . ? 35.201 129.373 21.860 1.00 29.49 ? 309 GAL B O6 1 HETATM 4067 O O . A2G N 10 . ? 35.781 133.250 16.076 1.00 42.60 ? 310 A2G B O 1 HETATM 4068 C C1 . A2G N 10 . ? 35.573 132.249 15.105 1.00 44.63 ? 310 A2G B C1 1 HETATM 4069 O O1 . A2G N 10 . ? 34.182 132.054 14.977 1.00 49.27 ? 310 A2G B O1 1 HETATM 4070 C C2 . A2G N 10 . ? 36.259 130.938 15.521 1.00 44.92 ? 310 A2G B C2 1 HETATM 4071 N N2 . A2G N 10 . ? 35.950 129.937 14.572 1.00 47.96 ? 310 A2G B N2 1 HETATM 4072 C C3 . A2G N 10 . ? 35.798 130.463 16.887 1.00 43.16 ? 310 A2G B C3 1 HETATM 4073 O O3 . A2G N 10 . ? 36.493 129.296 17.356 1.00 42.91 ? 310 A2G B O3 1 HETATM 4074 C C4 . A2G N 10 . ? 35.943 131.618 17.847 1.00 42.19 ? 310 A2G B C4 1 HETATM 4075 O O4 . A2G N 10 . ? 37.316 131.903 17.905 1.00 42.41 ? 310 A2G B O4 1 HETATM 4076 C C5 . A2G N 10 . ? 35.238 132.874 17.326 1.00 43.24 ? 310 A2G B C5 1 HETATM 4077 C C6 . A2G N 10 . ? 35.370 134.023 18.281 1.00 42.97 ? 310 A2G B C6 1 HETATM 4078 O O6 . A2G N 10 . ? 34.304 134.926 18.073 1.00 44.38 ? 310 A2G B O6 1 HETATM 4079 C C7 . A2G N 10 . ? 36.875 129.396 13.803 1.00 52.17 ? 310 A2G B C7 1 HETATM 4080 O O7 . A2G N 10 . ? 37.998 129.825 13.711 1.00 52.77 ? 310 A2G B O7 1 HETATM 4081 C C8 . A2G N 10 . ? 36.418 128.204 13.026 1.00 51.90 ? 310 A2G B C8 1 HETATM 4082 C C . MBN O 11 . ? 33.053 131.789 14.951 1.00 58.26 ? 311 MBN B C 1 HETATM 4083 C C1 . MBN O 11 . ? 31.641 131.434 14.520 1.00 58.79 ? 311 MBN B C1 1 HETATM 4084 C C2 . MBN O 11 . ? 31.416 130.594 13.437 1.00 57.04 ? 311 MBN B C2 1 HETATM 4085 C C3 . MBN O 11 . ? 30.126 130.262 13.052 1.00 56.23 ? 311 MBN B C3 1 HETATM 4086 C C4 . MBN O 11 . ? 29.034 130.751 13.736 1.00 55.36 ? 311 MBN B C4 1 HETATM 4087 C C5 . MBN O 11 . ? 29.249 131.584 14.814 1.00 55.72 ? 311 MBN B C5 1 HETATM 4088 C C6 . MBN O 11 . ? 30.537 131.924 15.192 1.00 57.40 ? 311 MBN B C6 1 HETATM 4089 O O . HOH P 12 . ? 60.479 62.721 19.358 1.00 41.31 ? 401 HOH A O 1 HETATM 4090 O O . HOH P 12 . ? 26.988 73.688 23.061 1.00 30.65 ? 402 HOH A O 1 HETATM 4091 O O . HOH P 12 . ? 28.224 91.141 14.373 1.00 21.01 ? 403 HOH A O 1 HETATM 4092 O O . HOH P 12 . ? 44.677 88.563 33.887 1.00 37.34 ? 404 HOH A O 1 HETATM 4093 O O . HOH P 12 . ? 34.346 73.096 37.896 1.00 31.64 ? 405 HOH A O 1 HETATM 4094 O O . HOH P 12 . ? 38.321 95.701 11.537 1.00 26.32 ? 406 HOH A O 1 HETATM 4095 O O . HOH P 12 . ? 56.739 86.016 18.475 1.00 22.90 ? 407 HOH A O 1 HETATM 4096 O O . HOH P 12 . ? 43.093 65.631 29.194 1.00 43.31 ? 408 HOH A O 1 HETATM 4097 O O . HOH P 12 . ? 54.495 95.255 26.414 1.00 25.56 ? 409 HOH A O 1 HETATM 4098 O O . HOH P 12 . ? 48.501 82.827 15.346 1.00 27.79 ? 410 HOH A O 1 HETATM 4099 O O . HOH P 12 . ? 30.265 74.157 15.218 1.00 24.84 ? 411 HOH A O 1 HETATM 4100 O O . HOH P 12 . ? 32.885 59.248 28.979 1.00 38.96 ? 412 HOH A O 1 HETATM 4101 O O . HOH P 12 . ? 52.663 105.331 27.186 1.00 26.81 ? 413 HOH A O 1 HETATM 4102 O O . HOH P 12 . ? 29.404 67.141 21.117 1.00 21.03 ? 414 HOH A O 1 HETATM 4103 O O . HOH P 12 . ? 41.172 57.013 31.311 1.00 47.67 ? 415 HOH A O 1 HETATM 4104 O O . HOH P 12 . ? 30.240 92.857 17.139 1.00 21.31 ? 416 HOH A O 1 HETATM 4105 O O . HOH P 12 . ? 46.105 92.741 28.343 1.00 22.68 ? 417 HOH A O 1 HETATM 4106 O O . HOH P 12 . ? 44.405 89.075 9.376 1.00 40.42 ? 418 HOH A O 1 HETATM 4107 O O . HOH P 12 . ? 64.439 92.697 19.628 1.00 46.82 ? 419 HOH A O 1 HETATM 4108 O O . HOH P 12 . ? 36.574 59.960 20.475 1.00 27.51 ? 420 HOH A O 1 HETATM 4109 O O . HOH P 12 . ? 46.601 77.910 14.379 1.00 31.87 ? 421 HOH A O 1 HETATM 4110 O O . HOH P 12 . ? 42.485 59.730 27.010 1.00 42.10 ? 422 HOH A O 1 HETATM 4111 O O . HOH P 12 . ? 62.595 80.729 14.828 1.00 42.50 ? 423 HOH A O 1 HETATM 4112 O O . HOH P 12 . ? 57.427 87.055 15.697 1.00 31.00 ? 424 HOH A O 1 HETATM 4113 O O . HOH P 12 . ? 28.762 84.076 24.420 1.00 23.97 ? 425 HOH A O 1 HETATM 4114 O O . HOH P 12 . ? 45.683 60.012 21.711 1.00 31.71 ? 426 HOH A O 1 HETATM 4115 O O . HOH P 12 . ? 52.697 64.288 24.851 1.00 36.54 ? 427 HOH A O 1 HETATM 4116 O O . HOH P 12 . ? 46.752 70.159 32.722 1.00 40.04 ? 428 HOH A O 1 HETATM 4117 O O . HOH P 12 . ? 44.505 86.140 15.772 1.00 18.33 ? 429 HOH A O 1 HETATM 4118 O O . HOH P 12 . ? 63.907 62.901 14.984 1.00 29.54 ? 430 HOH A O 1 HETATM 4119 O O . HOH P 12 . ? 40.467 102.291 12.401 1.00 18.82 ? 431 HOH A O 1 HETATM 4120 O O . HOH P 12 . ? 32.262 104.600 15.436 1.00 33.52 ? 432 HOH A O 1 HETATM 4121 O O . HOH P 12 . ? 28.186 85.132 13.115 1.00 40.57 ? 433 HOH A O 1 HETATM 4122 O O . HOH P 12 . ? 40.992 105.799 27.594 1.00 20.41 ? 434 HOH A O 1 HETATM 4123 O O . HOH P 12 . ? 41.347 73.366 33.899 1.00 25.93 ? 435 HOH A O 1 HETATM 4124 O O . HOH P 12 . ? 33.149 80.200 14.424 1.00 23.75 ? 436 HOH A O 1 HETATM 4125 O O . HOH P 12 . ? 40.993 105.830 14.878 1.00 36.07 ? 437 HOH A O 1 HETATM 4126 O O . HOH P 12 . ? 57.598 107.980 23.150 1.00 35.12 ? 438 HOH A O 1 HETATM 4127 O O . HOH P 12 . ? 57.620 69.326 9.640 1.00 40.37 ? 439 HOH A O 1 HETATM 4128 O O . HOH P 12 . ? 60.771 108.385 20.116 1.00 35.05 ? 440 HOH A O 1 HETATM 4129 O O . HOH P 12 . ? 56.346 79.053 25.561 1.00 36.02 ? 441 HOH A O 1 HETATM 4130 O O . HOH P 12 . ? 39.423 69.574 32.576 1.00 37.76 ? 442 HOH A O 1 HETATM 4131 O O . HOH P 12 . ? 57.550 62.859 19.358 1.00 39.71 ? 443 HOH A O 1 HETATM 4132 O O . HOH P 12 . ? 49.360 99.540 29.723 1.00 41.23 ? 444 HOH A O 1 HETATM 4133 O O . HOH P 12 . ? 36.650 82.904 3.664 1.00 31.80 ? 445 HOH A O 1 HETATM 4134 O O . HOH P 12 . ? 35.768 99.057 10.046 1.00 21.90 ? 446 HOH A O 1 HETATM 4135 O O . HOH P 12 . ? 33.975 57.218 20.371 1.00 40.62 ? 447 HOH A O 1 HETATM 4136 O O . HOH P 12 . ? 62.410 85.662 22.125 1.00 41.63 ? 448 HOH A O 1 HETATM 4137 O O . HOH P 12 . ? 54.999 83.083 32.063 1.00 34.77 ? 449 HOH A O 1 HETATM 4138 O O . HOH P 12 . ? 44.839 101.709 28.097 1.00 22.17 ? 450 HOH A O 1 HETATM 4139 O O . HOH P 12 . ? 63.777 65.271 17.976 1.00 38.51 ? 451 HOH A O 1 HETATM 4140 O O . HOH P 12 . ? 45.498 98.848 10.757 1.00 27.79 ? 452 HOH A O 1 HETATM 4141 O O . HOH P 12 . ? 47.600 83.915 32.817 1.00 24.54 ? 453 HOH A O 1 HETATM 4142 O O . HOH P 12 . ? 47.316 80.576 4.321 1.00 32.58 ? 454 HOH A O 1 HETATM 4143 O O . HOH P 12 . ? 29.354 70.301 16.816 1.00 37.50 ? 455 HOH A O 1 HETATM 4144 O O . HOH P 12 . ? 51.645 78.117 14.163 1.00 24.56 ? 456 HOH A O 1 HETATM 4145 O O . HOH P 12 . ? 39.189 79.294 37.505 1.00 25.06 ? 457 HOH A O 1 HETATM 4146 O O . HOH P 12 . ? 46.680 91.363 11.800 1.00 22.31 ? 458 HOH A O 1 HETATM 4147 O O . HOH P 12 . ? 50.407 76.745 34.641 1.00 43.15 ? 459 HOH A O 1 HETATM 4148 O O . HOH P 12 . ? 54.306 99.282 24.568 1.00 34.08 ? 460 HOH A O 1 HETATM 4149 O O . HOH P 12 . ? 59.219 72.073 21.467 1.00 44.82 ? 461 HOH A O 1 HETATM 4150 O O . HOH P 12 . ? 40.703 55.555 26.312 1.00 39.67 ? 462 HOH A O 1 HETATM 4151 O O . HOH P 12 . ? 60.564 83.991 15.405 1.00 29.48 ? 463 HOH A O 1 HETATM 4152 O O . HOH P 12 . ? 45.866 80.918 16.528 1.00 47.43 ? 464 HOH A O 1 HETATM 4153 O O . HOH P 12 . ? 43.285 100.232 29.806 1.00 27.35 ? 465 HOH A O 1 HETATM 4154 O O . HOH P 12 . ? 34.622 71.019 7.800 1.00 23.56 ? 466 HOH A O 1 HETATM 4155 O O . HOH P 12 . ? 54.065 82.291 0.282 1.00 49.53 ? 467 HOH A O 1 HETATM 4156 O O . HOH P 12 . ? 39.965 70.778 36.512 1.00 55.50 ? 468 HOH A O 1 HETATM 4157 O O . HOH P 12 . ? 55.442 112.738 21.083 1.00 25.32 ? 469 HOH A O 1 HETATM 4158 O O . HOH P 12 . ? 26.425 82.314 23.994 1.00 24.85 ? 470 HOH A O 1 HETATM 4159 O O . HOH P 12 . ? 37.868 68.799 26.598 1.00 32.58 ? 471 HOH A O 1 HETATM 4160 O O . HOH P 12 . ? 60.702 77.743 24.179 1.00 30.42 ? 472 HOH A O 1 HETATM 4161 O O . HOH P 12 . ? 39.462 82.745 2.905 1.00 27.92 ? 473 HOH A O 1 HETATM 4162 O O . HOH P 12 . ? 45.298 85.513 31.975 1.00 21.85 ? 474 HOH A O 1 HETATM 4163 O O . HOH P 12 . ? 58.179 78.984 13.318 1.00 35.35 ? 475 HOH A O 1 HETATM 4164 O O . HOH P 12 . ? 33.460 84.716 8.975 1.00 31.36 ? 476 HOH A O 1 HETATM 4165 O O . HOH P 12 . ? 54.852 70.868 25.904 1.00 28.50 ? 477 HOH A O 1 HETATM 4166 O O . HOH P 12 . ? 59.320 87.021 30.940 1.00 32.40 ? 478 HOH A O 1 HETATM 4167 O O . HOH P 12 . ? 45.608 64.220 28.579 1.00 42.64 ? 479 HOH A O 1 HETATM 4168 O O . HOH P 12 . ? 53.646 76.600 13.384 1.00 28.31 ? 480 HOH A O 1 HETATM 4169 O O . HOH P 12 . ? 38.219 92.543 7.041 1.00 36.96 ? 481 HOH A O 1 HETATM 4170 O O . HOH P 12 . ? 44.594 82.338 14.151 1.00 38.49 ? 482 HOH A O 1 HETATM 4171 O O . HOH P 12 . ? 54.451 96.544 23.675 1.00 28.76 ? 483 HOH A O 1 HETATM 4172 O O . HOH P 12 . ? 33.281 69.874 14.412 1.00 29.61 ? 484 HOH A O 1 HETATM 4173 O O . HOH P 12 . ? 59.313 101.042 18.400 1.00 46.88 ? 485 HOH A O 1 HETATM 4174 O O . HOH P 12 . ? 25.562 84.154 17.905 1.00 30.42 ? 486 HOH A O 1 HETATM 4175 O O . HOH P 12 . ? 61.473 92.706 28.480 1.00 33.40 ? 487 HOH A O 1 HETATM 4176 O O . HOH P 12 . ? 57.875 74.930 24.572 1.00 35.76 ? 488 HOH A O 1 HETATM 4177 O O . HOH P 12 . ? 44.364 83.468 10.033 1.00 35.80 ? 489 HOH A O 1 HETATM 4178 O O . HOH P 12 . ? 22.240 76.917 22.209 1.00 47.75 ? 490 HOH A O 1 HETATM 4179 O O . HOH P 12 . ? 43.054 58.749 23.624 1.00 35.36 ? 491 HOH A O 1 HETATM 4180 O O . HOH P 12 . ? 52.725 76.193 3.409 1.00 44.76 ? 492 HOH A O 1 HETATM 4181 O O . HOH P 12 . ? 57.110 97.015 22.973 1.00 27.37 ? 493 HOH A O 1 HETATM 4182 O O . HOH P 12 . ? 46.176 88.586 13.134 1.00 22.21 ? 494 HOH A O 1 HETATM 4183 O O . HOH P 12 . ? 33.588 61.837 12.478 1.00 46.00 ? 495 HOH A O 1 HETATM 4184 O O . HOH P 12 . ? 41.008 59.534 7.855 1.00 52.58 ? 496 HOH A O 1 HETATM 4185 O O . HOH P 12 . ? 41.730 97.333 11.184 1.00 26.40 ? 497 HOH A O 1 HETATM 4186 O O . HOH P 12 . ? 55.313 101.328 31.533 1.00 45.59 ? 498 HOH A O 1 HETATM 4187 O O . HOH P 12 . ? 27.604 76.045 24.806 1.00 34.12 ? 499 HOH A O 1 HETATM 4188 O O . HOH P 12 . ? 37.738 71.222 39.764 1.00 33.40 ? 500 HOH A O 1 HETATM 4189 O O . HOH P 12 . ? 20.285 79.818 29.949 1.00 55.28 ? 501 HOH A O 1 HETATM 4190 O O . HOH P 12 . ? 31.894 62.773 2.095 1.00 54.96 ? 502 HOH A O 1 HETATM 4191 O O . HOH P 12 . ? 57.516 104.682 28.225 1.00 44.69 ? 503 HOH A O 1 HETATM 4192 O O . HOH P 12 . ? 32.066 77.252 36.697 1.00 29.33 ? 504 HOH A O 1 HETATM 4193 O O . HOH P 12 . ? 56.081 64.760 20.830 1.00 23.44 ? 505 HOH A O 1 HETATM 4194 O O . HOH P 12 . ? 60.615 62.336 11.157 1.00 40.28 ? 506 HOH A O 1 HETATM 4195 O O . HOH P 12 . ? 62.625 89.173 28.834 1.00 38.82 ? 507 HOH A O 1 HETATM 4196 O O . HOH P 12 . ? 31.213 88.855 18.776 1.00 11.28 ? 508 HOH A O 1 HETATM 4197 O O . HOH P 12 . ? 43.238 85.934 11.608 1.00 28.20 ? 509 HOH A O 1 HETATM 4198 O O . HOH P 12 . ? 56.493 81.980 13.774 1.00 51.33 ? 510 HOH A O 1 HETATM 4199 O O . HOH P 12 . ? 26.144 86.722 16.518 1.00 48.57 ? 511 HOH A O 1 HETATM 4200 O O . HOH P 12 . ? 30.544 68.854 7.645 1.00 36.10 ? 512 HOH A O 1 HETATM 4201 O O . HOH P 12 . ? 62.415 65.520 20.271 1.00 44.98 ? 513 HOH A O 1 HETATM 4202 O O . HOH P 12 . ? 38.382 56.595 32.191 1.00 46.94 ? 514 HOH A O 1 HETATM 4203 O O . HOH P 12 . ? 40.740 73.893 36.711 1.00 46.49 ? 515 HOH A O 1 HETATM 4204 O O . HOH P 12 . ? 29.515 63.019 12.541 1.00 28.79 ? 516 HOH A O 1 HETATM 4205 O O . HOH P 12 . ? 54.544 84.224 12.432 1.00 48.07 ? 517 HOH A O 1 HETATM 4206 O O . HOH P 12 . ? 21.483 78.733 32.430 1.00 39.90 ? 518 HOH A O 1 HETATM 4207 O O . HOH P 12 . ? 36.608 65.705 2.145 1.00 41.84 ? 519 HOH A O 1 HETATM 4208 O O . HOH P 12 . ? 67.476 86.878 17.947 1.00 48.14 ? 520 HOH A O 1 HETATM 4209 O O . HOH P 12 . ? 48.217 80.916 13.528 1.00 38.27 ? 521 HOH A O 1 HETATM 4210 O O . HOH P 12 . ? 41.809 65.257 32.053 1.00 46.91 ? 522 HOH A O 1 HETATM 4211 O O . HOH P 12 . ? 51.331 105.070 6.712 1.00 40.49 ? 523 HOH A O 1 HETATM 4212 O O . HOH P 12 . ? 29.715 66.600 6.042 1.00 44.88 ? 524 HOH A O 1 HETATM 4213 O O . HOH P 12 . ? 37.102 96.784 9.417 1.00 21.98 ? 525 HOH A O 1 HETATM 4214 O O . HOH P 12 . ? 61.721 79.837 27.436 1.00 44.52 ? 526 HOH A O 1 HETATM 4215 O O . HOH P 12 . ? 32.001 69.184 2.678 1.00 44.13 ? 527 HOH A O 1 HETATM 4216 O O . HOH P 12 . ? 60.149 92.515 31.812 1.00 45.54 ? 528 HOH A O 1 HETATM 4217 O O . HOH P 12 . ? 57.257 92.158 33.836 1.00 44.97 ? 529 HOH A O 1 HETATM 4218 O O . HOH P 12 . ? 28.210 78.542 35.906 1.00 48.40 ? 530 HOH A O 1 HETATM 4219 O O . HOH P 12 . ? 24.947 89.017 18.911 1.00 52.34 ? 531 HOH A O 1 HETATM 4220 O O . HOH P 12 . ? 41.701 54.796 33.158 1.00 45.30 ? 532 HOH A O 1 HETATM 4221 O O . HOH P 12 . ? 43.752 53.684 7.242 1.00 48.92 ? 533 HOH A O 1 HETATM 4222 O O . HOH Q 12 . ? 57.251 113.669 9.716 1.00 39.79 ? 401 HOH B O 1 HETATM 4223 O O . HOH Q 12 . ? 20.932 97.388 40.781 1.00 34.21 ? 402 HOH B O 1 HETATM 4224 O O . HOH Q 12 . ? 52.581 129.029 37.591 1.00 43.91 ? 403 HOH B O 1 HETATM 4225 O O . HOH Q 12 . ? 38.876 130.118 27.975 1.00 33.45 ? 404 HOH B O 1 HETATM 4226 O O . HOH Q 12 . ? 47.620 111.579 36.308 1.00 25.92 ? 405 HOH B O 1 HETATM 4227 O O . HOH Q 12 . ? 40.507 110.403 22.725 1.00 18.31 ? 406 HOH B O 1 HETATM 4228 O O . HOH Q 12 . ? 35.347 109.790 26.777 1.00 20.62 ? 407 HOH B O 1 HETATM 4229 O O . HOH Q 12 . ? 31.594 118.700 31.199 1.00 31.79 ? 408 HOH B O 1 HETATM 4230 O O . HOH Q 12 . ? 36.623 93.867 19.330 1.00 18.05 ? 409 HOH B O 1 HETATM 4231 O O . HOH Q 12 . ? 44.635 108.519 14.177 1.00 34.07 ? 410 HOH B O 1 HETATM 4232 O O . HOH Q 12 . ? 39.233 92.703 30.444 1.00 29.99 ? 411 HOH B O 1 HETATM 4233 O O . HOH Q 12 . ? 35.383 112.680 38.072 1.00 23.11 ? 412 HOH B O 1 HETATM 4234 O O . HOH Q 12 . ? 35.263 106.873 38.165 1.00 12.87 ? 413 HOH B O 1 HETATM 4235 O O . HOH Q 12 . ? 33.219 104.164 51.207 1.00 25.00 ? 414 HOH B O 1 HETATM 4236 O O . HOH Q 12 . ? 46.229 121.165 13.442 1.00 26.28 ? 415 HOH B O 1 HETATM 4237 O O . HOH Q 12 . ? 31.120 98.984 23.725 1.00 32.47 ? 416 HOH B O 1 HETATM 4238 O O . HOH Q 12 . ? 41.823 107.374 29.610 1.00 17.28 ? 417 HOH B O 1 HETATM 4239 O O . HOH Q 12 . ? 33.559 121.227 18.801 1.00 27.75 ? 418 HOH B O 1 HETATM 4240 O O . HOH Q 12 . ? 48.087 114.469 32.786 1.00 21.90 ? 419 HOH B O 1 HETATM 4241 O O . HOH Q 12 . ? 44.278 129.316 33.950 1.00 37.85 ? 420 HOH B O 1 HETATM 4242 O O . HOH Q 12 . ? 35.639 83.125 40.674 1.00 33.57 ? 421 HOH B O 1 HETATM 4243 O O . HOH Q 12 . ? 30.697 122.468 29.115 1.00 31.04 ? 422 HOH B O 1 HETATM 4244 O O . HOH Q 12 . ? 53.793 103.998 32.121 1.00 48.18 ? 423 HOH B O 1 HETATM 4245 O O . HOH Q 12 . ? 38.568 104.834 28.024 1.00 25.12 ? 424 HOH B O 1 HETATM 4246 O O . HOH Q 12 . ? 46.754 133.777 21.320 1.00 32.78 ? 425 HOH B O 1 HETATM 4247 O O . HOH Q 12 . ? 36.052 131.232 27.577 1.00 24.01 ? 426 HOH B O 1 HETATM 4248 O O . HOH Q 12 . ? 32.261 125.483 18.081 1.00 33.64 ? 427 HOH B O 1 HETATM 4249 O O . HOH Q 12 . ? 33.672 112.241 24.464 1.00 23.11 ? 428 HOH B O 1 HETATM 4250 O O . HOH Q 12 . ? 41.525 104.319 54.770 1.00 25.16 ? 429 HOH B O 1 HETATM 4251 O O . HOH Q 12 . ? 29.210 100.327 47.312 1.00 20.28 ? 430 HOH B O 1 HETATM 4252 O O . HOH Q 12 . ? 28.962 94.867 34.805 1.00 26.53 ? 431 HOH B O 1 HETATM 4253 O O . HOH Q 12 . ? 46.546 91.712 42.140 1.00 29.55 ? 432 HOH B O 1 HETATM 4254 O O . HOH Q 12 . ? 39.717 117.389 15.356 1.00 23.47 ? 433 HOH B O 1 HETATM 4255 O O . HOH Q 12 . ? 49.828 105.532 36.744 1.00 42.48 ? 434 HOH B O 1 HETATM 4256 O O . HOH Q 12 . ? 27.061 85.837 36.077 1.00 21.34 ? 435 HOH B O 1 HETATM 4257 O O . HOH Q 12 . ? 34.593 127.737 31.027 1.00 28.61 ? 436 HOH B O 1 HETATM 4258 O O . HOH Q 12 . ? 41.664 94.760 40.765 1.00 21.41 ? 437 HOH B O 1 HETATM 4259 O O . HOH Q 12 . ? 33.268 116.185 23.557 1.00 24.59 ? 438 HOH B O 1 HETATM 4260 O O . HOH Q 12 . ? 36.532 113.596 35.756 1.00 26.12 ? 439 HOH B O 1 HETATM 4261 O O . HOH Q 12 . ? 30.992 98.180 47.189 1.00 17.75 ? 440 HOH B O 1 HETATM 4262 O O . HOH Q 12 . ? 57.010 123.296 33.070 1.00 34.23 ? 441 HOH B O 1 HETATM 4263 O O . HOH Q 12 . ? 40.782 112.724 47.107 1.00 47.77 ? 442 HOH B O 1 HETATM 4264 O O . HOH Q 12 . ? 39.595 83.919 45.146 1.00 39.08 ? 443 HOH B O 1 HETATM 4265 O O . HOH Q 12 . ? 40.078 106.124 48.740 1.00 24.21 ? 444 HOH B O 1 HETATM 4266 O O . HOH Q 12 . ? 42.323 95.435 33.610 1.00 15.65 ? 445 HOH B O 1 HETATM 4267 O O . HOH Q 12 . ? 35.893 86.211 36.357 1.00 36.82 ? 446 HOH B O 1 HETATM 4268 O O . HOH Q 12 . ? 55.575 121.996 13.355 1.00 35.46 ? 447 HOH B O 1 HETATM 4269 O O . HOH Q 12 . ? 28.885 113.141 29.631 1.00 38.06 ? 448 HOH B O 1 HETATM 4270 O O . HOH Q 12 . ? 36.820 108.497 59.958 1.00 41.38 ? 449 HOH B O 1 HETATM 4271 O O . HOH Q 12 . ? 51.153 99.559 32.051 1.00 34.21 ? 450 HOH B O 1 HETATM 4272 O O . HOH Q 12 . ? 34.664 115.569 35.852 1.00 24.26 ? 451 HOH B O 1 HETATM 4273 O O . HOH Q 12 . ? 43.104 123.609 34.575 1.00 26.11 ? 452 HOH B O 1 HETATM 4274 O O . HOH Q 12 . ? 40.789 104.333 30.736 1.00 27.70 ? 453 HOH B O 1 HETATM 4275 O O . HOH Q 12 . ? 27.081 95.595 51.294 1.00 24.84 ? 454 HOH B O 1 HETATM 4276 O O . HOH Q 12 . ? 61.028 118.399 29.212 1.00 51.72 ? 455 HOH B O 1 HETATM 4277 O O . HOH Q 12 . ? 39.654 105.108 52.792 1.00 31.96 ? 456 HOH B O 1 HETATM 4278 O O . HOH Q 12 . ? 44.135 107.741 40.889 1.00 23.54 ? 457 HOH B O 1 HETATM 4279 O O . HOH Q 12 . ? 31.195 113.528 44.631 1.00 22.93 ? 458 HOH B O 1 HETATM 4280 O O . HOH Q 12 . ? 37.985 104.730 31.143 1.00 33.57 ? 459 HOH B O 1 HETATM 4281 O O . HOH Q 12 . ? 41.464 115.076 32.141 1.00 16.33 ? 460 HOH B O 1 HETATM 4282 O O . HOH Q 12 . ? 43.152 88.238 42.406 1.00 29.13 ? 461 HOH B O 1 HETATM 4283 O O . HOH Q 12 . ? 48.578 110.955 10.901 1.00 36.76 ? 462 HOH B O 1 HETATM 4284 O O . HOH Q 12 . ? 44.388 130.044 22.430 1.00 24.33 ? 463 HOH B O 1 HETATM 4285 O O . HOH Q 12 . ? 39.646 133.306 38.369 1.00 50.33 ? 464 HOH B O 1 HETATM 4286 O O . HOH Q 12 . ? 26.331 89.155 45.408 1.00 31.32 ? 465 HOH B O 1 HETATM 4287 O O . HOH Q 12 . ? 31.428 91.348 48.043 1.00 21.27 ? 466 HOH B O 1 HETATM 4288 O O . HOH Q 12 . ? 25.251 101.014 35.901 1.00 12.90 ? 467 HOH B O 1 HETATM 4289 O O . HOH Q 12 . ? 41.321 89.318 34.488 1.00 31.65 ? 468 HOH B O 1 HETATM 4290 O O . HOH Q 12 . ? 23.333 87.310 41.449 1.00 43.00 ? 469 HOH B O 1 HETATM 4291 O O . HOH Q 12 . ? 30.790 117.005 20.211 1.00 40.53 ? 470 HOH B O 1 HETATM 4292 O O . HOH Q 12 . ? 54.903 125.071 41.653 1.00 52.73 ? 471 HOH B O 1 HETATM 4293 O O . HOH Q 12 . ? 28.584 97.865 48.832 1.00 24.64 ? 472 HOH B O 1 HETATM 4294 O O . HOH Q 12 . ? 37.814 87.272 39.371 1.00 34.59 ? 473 HOH B O 1 HETATM 4295 O O . HOH Q 12 . ? 41.425 114.192 44.328 1.00 33.46 ? 474 HOH B O 1 HETATM 4296 O O . HOH Q 12 . ? 34.437 85.359 33.966 1.00 31.08 ? 475 HOH B O 1 HETATM 4297 O O . HOH Q 12 . ? 41.703 116.914 20.709 1.00 17.25 ? 476 HOH B O 1 HETATM 4298 O O . HOH Q 12 . ? 23.111 102.303 34.051 1.00 34.19 ? 477 HOH B O 1 HETATM 4299 O O . HOH Q 12 . ? 31.233 126.355 29.694 1.00 28.93 ? 478 HOH B O 1 HETATM 4300 O O . HOH Q 12 . ? 45.002 127.132 29.230 1.00 35.76 ? 479 HOH B O 1 HETATM 4301 O O . HOH Q 12 . ? 47.056 134.164 16.879 1.00 34.95 ? 480 HOH B O 1 HETATM 4302 O O . HOH Q 12 . ? 20.887 101.319 27.468 1.00 39.74 ? 481 HOH B O 1 HETATM 4303 O O . HOH Q 12 . ? 33.377 116.958 37.744 1.00 24.93 ? 482 HOH B O 1 HETATM 4304 O O . HOH Q 12 . ? 22.678 100.957 30.772 1.00 27.61 ? 483 HOH B O 1 HETATM 4305 O O . HOH Q 12 . ? 39.530 128.521 32.758 1.00 27.89 ? 484 HOH B O 1 HETATM 4306 O O . HOH Q 12 . ? 37.920 102.775 48.752 1.00 30.00 ? 485 HOH B O 1 HETATM 4307 O O . HOH Q 12 . ? 58.807 113.185 11.863 1.00 45.89 ? 486 HOH B O 1 HETATM 4308 O O . HOH Q 12 . ? 34.743 109.643 18.739 1.00 23.35 ? 487 HOH B O 1 HETATM 4309 O O . HOH Q 12 . ? 24.991 92.049 31.735 1.00 26.19 ? 488 HOH B O 1 HETATM 4310 O O . HOH Q 12 . ? 27.010 104.700 49.132 1.00 24.37 ? 489 HOH B O 1 HETATM 4311 O O . HOH Q 12 . ? 32.679 84.704 46.289 1.00 29.32 ? 490 HOH B O 1 HETATM 4312 O O . HOH Q 12 . ? 33.691 113.732 17.278 1.00 35.55 ? 491 HOH B O 1 HETATM 4313 O O . HOH Q 12 . ? 36.906 90.334 40.918 1.00 16.72 ? 492 HOH B O 1 HETATM 4314 O O . HOH Q 12 . ? 29.779 91.576 45.475 1.00 24.52 ? 493 HOH B O 1 HETATM 4315 O O . HOH Q 12 . ? 27.987 112.395 45.210 1.00 28.50 ? 494 HOH B O 1 HETATM 4316 O O . HOH Q 12 . ? 35.798 112.102 45.534 1.00 24.02 ? 495 HOH B O 1 HETATM 4317 O O . HOH Q 12 . ? 48.095 118.533 14.104 1.00 23.11 ? 496 HOH B O 1 HETATM 4318 O O . HOH Q 12 . ? 38.989 107.915 52.511 1.00 35.71 ? 497 HOH B O 1 HETATM 4319 O O . HOH Q 12 . ? 48.515 131.041 32.891 1.00 26.07 ? 498 HOH B O 1 HETATM 4320 O O . HOH Q 12 . ? 46.694 118.970 11.775 1.00 34.40 ? 499 HOH B O 1 HETATM 4321 O O . HOH Q 12 . ? 38.761 103.857 33.443 1.00 46.15 ? 500 HOH B O 1 HETATM 4322 O O . HOH Q 12 . ? 39.144 130.327 30.694 1.00 47.61 ? 501 HOH B O 1 HETATM 4323 O O . HOH Q 12 . ? 49.039 97.981 45.228 1.00 30.81 ? 502 HOH B O 1 HETATM 4324 O O . HOH Q 12 . ? 42.223 102.133 31.747 1.00 22.25 ? 503 HOH B O 1 HETATM 4325 O O . HOH Q 12 . ? 28.591 94.499 27.089 1.00 42.37 ? 504 HOH B O 1 HETATM 4326 O O . HOH Q 12 . ? 38.745 92.699 27.309 1.00 41.68 ? 505 HOH B O 1 HETATM 4327 O O . HOH Q 12 . ? 38.514 115.381 10.283 1.00 63.56 ? 506 HOH B O 1 HETATM 4328 O O . HOH Q 12 . ? 49.629 121.804 41.193 1.00 28.96 ? 507 HOH B O 1 HETATM 4329 O O . HOH Q 12 . ? 52.966 106.076 42.592 1.00 38.60 ? 508 HOH B O 1 HETATM 4330 O O . HOH Q 12 . ? 38.606 120.270 40.117 1.00 40.83 ? 509 HOH B O 1 HETATM 4331 O O . HOH Q 12 . ? 30.931 101.737 23.293 1.00 30.76 ? 510 HOH B O 1 HETATM 4332 O O . HOH Q 12 . ? 47.900 88.883 36.400 1.00 41.02 ? 511 HOH B O 1 HETATM 4333 O O . HOH Q 12 . ? 50.587 120.572 13.937 1.00 37.35 ? 512 HOH B O 1 HETATM 4334 O O . HOH Q 12 . ? 21.188 89.471 38.503 1.00 43.22 ? 513 HOH B O 1 HETATM 4335 O O . HOH Q 12 . ? 44.399 104.408 31.615 1.00 41.35 ? 514 HOH B O 1 HETATM 4336 O O . HOH Q 12 . ? 26.532 105.411 24.682 1.00 35.63 ? 515 HOH B O 1 HETATM 4337 O O . HOH Q 12 . ? 19.499 108.730 35.328 1.00 47.63 ? 516 HOH B O 1 HETATM 4338 O O . HOH Q 12 . ? 39.340 110.423 49.727 1.00 34.93 ? 517 HOH B O 1 HETATM 4339 O O . HOH Q 12 . ? 45.154 89.503 40.973 1.00 41.28 ? 518 HOH B O 1 HETATM 4340 O O . HOH Q 12 . ? 33.352 121.700 36.763 1.00 34.54 ? 519 HOH B O 1 HETATM 4341 O O . HOH Q 12 . ? 52.110 125.416 32.612 1.00 31.12 ? 520 HOH B O 1 HETATM 4342 O O . HOH Q 12 . ? 26.726 92.456 27.930 1.00 38.25 ? 521 HOH B O 1 HETATM 4343 O O . HOH Q 12 . ? 39.853 135.349 28.930 1.00 35.47 ? 522 HOH B O 1 HETATM 4344 O O . HOH Q 12 . ? 32.853 120.723 15.942 1.00 38.57 ? 523 HOH B O 1 HETATM 4345 O O . HOH Q 12 . ? 18.943 97.066 36.061 1.00 28.94 ? 524 HOH B O 1 HETATM 4346 O O . HOH Q 12 . ? 37.369 120.640 9.703 1.00 40.98 ? 525 HOH B O 1 HETATM 4347 O O . HOH Q 12 . ? 39.160 123.366 11.041 1.00 26.06 ? 526 HOH B O 1 HETATM 4348 O O . HOH Q 12 . ? 22.245 83.781 40.151 1.00 51.11 ? 527 HOH B O 1 HETATM 4349 O O . HOH Q 12 . ? 59.897 119.434 23.331 1.00 38.63 ? 528 HOH B O 1 HETATM 4350 O O . HOH Q 12 . ? 44.379 106.513 29.163 1.00 21.57 ? 529 HOH B O 1 HETATM 4351 O O . HOH Q 12 . ? 41.899 126.453 38.788 1.00 37.45 ? 530 HOH B O 1 HETATM 4352 O O . HOH Q 12 . ? 19.734 86.885 37.985 1.00 36.32 ? 531 HOH B O 1 HETATM 4353 O O . HOH Q 12 . ? 50.911 107.514 44.024 1.00 40.09 ? 532 HOH B O 1 HETATM 4354 O O . HOH Q 12 . ? 64.259 112.997 26.056 1.00 62.24 ? 533 HOH B O 1 HETATM 4355 O O . HOH Q 12 . ? 27.602 117.834 33.170 1.00 46.90 ? 534 HOH B O 1 HETATM 4356 O O . HOH Q 12 . ? 30.508 118.005 41.341 1.00 31.20 ? 535 HOH B O 1 HETATM 4357 O O . HOH Q 12 . ? 40.632 115.388 13.843 1.00 28.49 ? 536 HOH B O 1 HETATM 4358 O O . HOH Q 12 . ? 44.746 142.712 32.601 1.00 42.59 ? 537 HOH B O 1 HETATM 4359 O O . HOH Q 12 . ? 28.967 115.281 31.864 1.00 37.26 ? 538 HOH B O 1 HETATM 4360 O O . HOH Q 12 . ? 66.449 125.203 17.626 1.00 54.66 ? 539 HOH B O 1 HETATM 4361 O O . HOH Q 12 . ? 52.179 91.573 45.031 1.00 46.03 ? 540 HOH B O 1 HETATM 4362 O O . HOH Q 12 . ? 37.405 126.994 34.233 1.00 46.76 ? 541 HOH B O 1 HETATM 4363 O O . HOH Q 12 . ? 44.628 132.501 23.416 1.00 42.31 ? 542 HOH B O 1 HETATM 4364 O O . HOH Q 12 . ? 57.416 118.430 11.422 1.00 35.98 ? 543 HOH B O 1 HETATM 4365 O O . HOH Q 12 . ? 36.184 83.879 38.035 1.00 50.92 ? 544 HOH B O 1 HETATM 4366 O O . HOH Q 12 . ? 48.800 129.426 40.125 1.00 55.43 ? 545 HOH B O 1 HETATM 4367 O O . HOH Q 12 . ? 43.109 125.216 41.006 1.00 40.51 ? 546 HOH B O 1 HETATM 4368 O O . HOH Q 12 . ? 31.826 128.127 31.994 1.00 40.44 ? 547 HOH B O 1 HETATM 4369 O O . HOH Q 12 . ? 31.074 122.818 19.371 1.00 35.34 ? 548 HOH B O 1 HETATM 4370 O O . HOH Q 12 . ? 18.335 97.018 26.330 1.00 51.27 ? 549 HOH B O 1 HETATM 4371 O O . HOH Q 12 . ? 35.170 124.448 13.160 1.00 40.58 ? 550 HOH B O 1 HETATM 4372 O O . HOH Q 12 . ? 46.504 86.357 37.126 1.00 39.27 ? 551 HOH B O 1 HETATM 4373 O O . HOH Q 12 . ? 32.503 111.964 46.643 1.00 26.17 ? 552 HOH B O 1 HETATM 4374 O O . HOH Q 12 . ? 38.024 82.221 42.327 1.00 46.73 ? 553 HOH B O 1 HETATM 4375 O O . HOH Q 12 . ? 26.548 83.937 38.243 1.00 36.05 ? 554 HOH B O 1 HETATM 4376 O O . HOH Q 12 . ? 40.407 103.768 50.469 1.00 30.00 ? 555 HOH B O 1 HETATM 4377 O O . HOH Q 12 . ? 48.555 93.447 40.503 1.00 35.81 ? 556 HOH B O 1 HETATM 4378 O O . HOH Q 12 . ? 30.200 121.374 26.814 1.00 32.64 ? 557 HOH B O 1 HETATM 4379 O O . HOH Q 12 . ? 59.266 116.889 12.482 1.00 40.79 ? 558 HOH B O 1 HETATM 4380 O O . HOH Q 12 . ? 50.277 131.375 38.861 1.00 42.67 ? 559 HOH B O 1 HETATM 4381 O O . HOH Q 12 . ? 46.181 135.592 19.226 1.00 37.83 ? 560 HOH B O 1 HETATM 4382 O O . HOH Q 12 . ? 20.013 96.056 44.419 1.00 46.68 ? 561 HOH B O 1 HETATM 4383 O O . HOH Q 12 . ? 36.279 123.152 10.865 1.00 41.38 ? 562 HOH B O 1 HETATM 4384 O O . HOH Q 12 . ? 55.915 105.847 32.547 1.00 56.44 ? 563 HOH B O 1 HETATM 4385 O O . HOH Q 12 . ? 51.352 94.256 41.787 1.00 44.99 ? 564 HOH B O 1 HETATM 4386 O O . HOH Q 12 . ? 49.309 87.992 33.980 1.00 39.44 ? 565 HOH B O 1 HETATM 4387 O O . HOH Q 12 . ? 36.932 122.439 42.815 1.00 45.10 ? 566 HOH B O 1 HETATM 4388 O O . HOH Q 12 . ? 34.456 126.455 11.274 1.00 53.46 ? 567 HOH B O 1 HETATM 4389 O O . HOH Q 12 . ? 52.727 86.168 39.005 1.00 42.40 ? 568 HOH B O 1 HETATM 4390 O O . HOH Q 12 . ? 43.949 125.262 10.453 1.00 50.42 ? 569 HOH B O 1 HETATM 4391 O O . HOH Q 12 . ? 26.472 118.348 40.124 1.00 63.79 ? 570 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASN 1 1 1 ASN ASN A . n A 1 2 LEU 2 2 2 LEU LEU A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 LEU 4 4 4 LEU LEU A . n A 1 5 SER 5 5 5 SER SER A . n A 1 6 GLN 6 6 6 GLN GLN A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 PHE 9 9 9 PHE PHE A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 ALA 11 11 11 ALA ALA A . n A 1 12 ASP 12 12 12 ASP ASP A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 TYR 14 14 14 TYR TYR A . n A 1 15 LYS 15 15 15 LYS LYS A . n A 1 16 SER 16 16 16 SER SER A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ILE 18 18 18 ILE ILE A . n A 1 19 LYS 19 19 19 LYS LYS A . n A 1 20 ASN 20 20 20 ASN ASN A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 LYS 23 23 23 LYS LYS A . n A 1 24 GLN 24 24 24 GLN GLN A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 ILE 27 27 27 ILE ILE A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 SER 30 30 30 SER SER A . n A 1 31 TYR 31 31 31 TYR TYR A . n A 1 32 GLY 32 32 32 GLY GLY A . n A 1 33 SER 33 33 33 SER SER A . n A 1 34 ALA 34 34 34 ALA ALA A . n A 1 35 GLY 35 35 35 GLY GLY A . n A 1 36 ILE 36 36 36 ILE ILE A . n A 1 37 PRO 37 37 37 PRO PRO A . n A 1 38 ILE 38 38 38 ILE ILE A . n A 1 39 LEU 39 39 39 LEU LEU A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 HIS 41 41 41 HIS HIS A . n A 1 42 SER 42 42 42 SER SER A . n A 1 43 VAL 43 43 43 VAL VAL A . n A 1 44 PRO 44 44 44 PRO PRO A . n A 1 45 ILE 45 45 45 ILE ILE A . n A 1 46 CYS 46 46 46 CYS CYS A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 ARG 48 48 48 ARG ARG A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 LEU 51 51 51 LEU LEU A . n A 1 52 VAL 52 52 52 VAL VAL A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 LEU 54 54 54 LEU LEU A . n A 1 55 THR 55 55 55 THR THR A . n A 1 56 ASN 56 56 56 ASN ASN A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 ASP 58 58 58 ASP ASP A . n A 1 59 ASN 59 59 59 ASN ASN A . n A 1 60 GLU 60 60 60 GLU GLU A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 ILE 62 62 62 ILE ILE A . n A 1 63 THR 63 63 63 THR THR A . n A 1 64 LEU 64 64 64 LEU LEU A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 ILE 66 66 66 ILE ILE A . n A 1 67 ASN 67 67 67 ASN ASN A . n A 1 68 VAL 68 68 68 VAL VAL A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 ASP 70 70 70 ASP ASP A . n A 1 71 ALA 71 71 71 ALA ALA A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 PHE 73 73 73 PHE PHE A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 ALA 75 75 75 ALA ALA A . n A 1 76 TYR 76 76 76 TYR TYR A . n A 1 77 ARG 77 77 77 ARG ARG A . n A 1 78 ALA 78 78 78 ALA ALA A . n A 1 79 ALA 79 79 79 ALA ALA A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 SER 82 82 82 SER SER A . n A 1 83 TYR 83 83 83 TYR TYR A . n A 1 84 PHE 84 84 84 PHE PHE A . n A 1 85 PHE 85 85 85 PHE PHE A . n A 1 86 GLN 86 86 86 GLN GLN A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 PRO 89 89 89 PRO PRO A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 ALA 92 92 92 ALA ALA A . n A 1 93 SER 93 93 93 SER SER A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 VAL 95 95 95 VAL VAL A . n A 1 96 ILE 96 96 96 ILE ILE A . n A 1 97 PHE 97 97 97 PHE PHE A . n A 1 98 THR 98 98 98 THR THR A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 THR 100 100 100 THR THR A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 GLN 102 102 102 GLN GLN A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 ILE 104 104 104 ILE ILE A . n A 1 105 MET 105 105 105 MET MET A . n A 1 106 ASN 106 106 106 ASN ASN A . n A 1 107 PHE 107 107 107 PHE PHE A . n A 1 108 ASN 108 108 108 ASN ASN A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 THR 110 110 110 THR THR A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 SER 113 113 113 SER SER A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLU 115 115 115 GLU GLU A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 THR 121 121 121 THR THR A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 THR 125 125 125 THR THR A . n A 1 126 PRO 126 126 126 PRO PRO A . n A 1 127 LEU 127 127 127 LEU LEU A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 ILE 129 129 129 ILE ILE A . n A 1 130 MET 130 130 130 MET MET A . n A 1 131 HIS 131 131 131 HIS HIS A . n A 1 132 PHE 132 132 132 PHE PHE A . n A 1 133 GLU 133 133 133 GLU GLU A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 ILE 136 136 136 ILE ILE A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 HIS 138 138 138 HIS HIS A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 VAL 141 141 141 VAL VAL A . n A 1 142 HIS 142 142 142 HIS HIS A . n A 1 143 ASP 143 143 143 ASP ASP A . n A 1 144 GLU 144 144 144 GLU GLU A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 TYR 146 146 146 TYR TYR A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 PRO 148 148 148 PRO PRO A . n A 1 149 THR 149 149 149 THR THR A . n A 1 150 SER 150 150 150 SER SER A . n A 1 151 PHE 151 151 151 PHE PHE A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 VAL 153 153 153 VAL VAL A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 GLN 156 156 156 GLN GLN A . n A 1 157 MET 157 157 157 MET MET A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 GLU 160 160 160 GLU GLU A . n A 1 161 ALA 161 161 161 ALA ALA A . n A 1 162 ALA 162 162 162 ALA ALA A . n A 1 163 LYS 163 163 163 LYS LYS A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 LYS 165 165 165 LYS LYS A . n A 1 166 PHE 166 166 166 PHE PHE A . n A 1 167 ILE 167 167 167 ILE ILE A . n A 1 168 GLU 168 168 168 GLU GLU A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 LYS 170 170 170 LYS LYS A . n A 1 171 VAL 171 171 171 VAL VAL A . n A 1 172 ILE 172 172 172 ILE ILE A . n A 1 173 HIS 173 173 173 HIS HIS A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 ILE 175 175 175 ILE ILE A . n A 1 176 MET 176 176 176 MET MET A . n A 1 177 ASP 177 177 177 ASP ASP A . n A 1 178 MET 178 178 178 MET MET A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 ASP 180 180 180 ASP ASP A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 THR 182 182 182 THR THR A . n A 1 183 PRO 183 183 183 PRO PRO A . n A 1 184 GLY 184 184 184 GLY GLY A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 ALA 186 186 186 ALA ALA A . n A 1 187 MET 187 187 187 MET MET A . n A 1 188 LEU 188 188 188 LEU LEU A . n A 1 189 SER 189 189 189 SER SER A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 GLU 191 191 191 GLU GLU A . n A 1 192 GLU 192 192 192 GLU GLU A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 TRP 194 194 194 TRP TRP A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 GLN 196 196 196 GLN GLN A . n A 1 197 LEU 197 197 197 LEU LEU A . n A 1 198 SER 198 198 198 SER SER A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 GLN 200 200 200 GLN GLN A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 GLN 202 202 202 GLN GLN A . n A 1 203 ALA 203 203 203 ALA ALA A . n A 1 204 SER 204 204 204 SER SER A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 ASN 208 208 208 ASN ASN A . n A 1 209 GLY 209 209 209 GLY GLY A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PHE 211 211 211 PHE PHE A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 ASP 213 213 213 ASP ASP A . n A 1 214 SER 214 214 214 SER SER A . n A 1 215 VAL 215 215 215 VAL VAL A . n A 1 216 SER 216 216 216 SER SER A . n A 1 217 LEU 217 217 217 LEU LEU A . n A 1 218 TYR 218 218 218 TYR TYR A . n A 1 219 ASN 219 219 219 ASN ASN A . n A 1 220 SER 220 220 220 SER SER A . n A 1 221 MET 221 221 221 MET MET A . n A 1 222 ASP 222 222 222 ASP ASP A . n A 1 223 GLU 223 223 223 GLU GLU A . n A 1 224 PRO 224 224 224 PRO PRO A . n A 1 225 ILE 225 225 225 ILE ILE A . n A 1 226 GLY 226 226 226 GLY GLY A . n A 1 227 VAL 227 227 227 VAL VAL A . n A 1 228 ASP 228 228 228 ASP ASP A . n A 1 229 SER 229 229 229 SER SER A . n A 1 230 MET 230 230 230 MET MET A . n A 1 231 TYR 231 231 231 TYR TYR A . n A 1 232 TYR 232 232 232 TYR TYR A . n A 1 233 PRO 233 233 233 PRO PRO A . n A 1 234 ILE 234 234 234 ILE ILE A . n A 1 235 LEU 235 235 235 LEU LEU A . n A 1 236 THR 236 236 236 THR THR A . n A 1 237 ALA 237 237 237 ALA ALA A . n A 1 238 ASN 238 238 238 ASN ASN A . n A 1 239 MET 239 239 239 MET MET A . n A 1 240 ALA 240 240 240 ALA ALA A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLN 242 242 242 GLN GLN A . n A 1 243 LEU 243 243 243 LEU LEU A . n A 1 244 TYR 244 244 244 TYR TYR A . n A 1 245 GLN 245 245 245 GLN GLN A . n A 1 246 CYS 246 246 246 CYS CYS A . n A 1 247 PRO 247 247 247 PRO PRO A . n B 2 1 ASN 1 1 1 ASN ASN B . n B 2 2 GLU 2 2 2 GLU GLU B . n B 2 3 GLN 3 3 3 GLN GLN B . n B 2 4 CYS 4 4 4 CYS CYS B . n B 2 5 SER 5 5 5 SER SER B . n B 2 6 PRO 6 6 6 PRO PRO B . n B 2 7 GLN 7 7 7 GLN GLN B . n B 2 8 GLN 8 8 8 GLN GLN B . n B 2 9 ARG 9 9 9 ARG ARG B . n B 2 10 THR 10 10 10 THR THR B . n B 2 11 THR 11 11 11 THR THR B . n B 2 12 ARG 12 12 12 ARG ARG B . n B 2 13 ILE 13 13 13 ILE ILE B . n B 2 14 SER 14 14 14 SER SER B . n B 2 15 GLY 15 15 15 GLY GLY B . n B 2 16 ARG 16 16 16 ARG ARG B . n B 2 17 ASP 17 17 17 ASP ASP B . n B 2 18 GLY 18 18 18 GLY GLY B . n B 2 19 LEU 19 19 19 LEU LEU B . n B 2 20 CYS 20 20 20 CYS CYS B . n B 2 21 VAL 21 21 21 VAL VAL B . n B 2 22 ASP 22 22 22 ASP ASP B . n B 2 23 VAL 23 23 23 VAL VAL B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 GLY 25 25 25 GLY GLY B . n B 2 26 ALA 26 26 26 ALA ALA B . n B 2 27 LEU 27 27 27 LEU LEU B . n B 2 28 THR 28 28 28 THR THR B . n B 2 29 ALA 29 29 29 ALA ALA B . n B 2 30 ASP 30 30 30 ASP ASP B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 ARG 33 33 33 ARG ARG B . n B 2 34 VAL 34 34 34 VAL VAL B . n B 2 35 ILE 35 35 35 ILE ILE B . n B 2 36 LEU 36 36 36 LEU LEU B . n B 2 37 TYR 37 37 37 TYR TYR B . n B 2 38 PRO 38 38 38 PRO PRO B . n B 2 39 CYS 39 39 39 CYS CYS B . n B 2 40 GLY 40 40 40 GLY GLY B . n B 2 41 GLN 41 41 41 GLN GLN B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 GLN 43 43 43 GLN GLN B . n B 2 44 ASN 44 44 44 ASN ASN B . n B 2 45 GLN 45 45 45 GLN GLN B . n B 2 46 GLN 46 46 46 GLN GLN B . n B 2 47 TRP 47 47 47 TRP TRP B . n B 2 48 THR 48 48 48 THR THR B . n B 2 49 PHE 49 49 49 PHE PHE B . n B 2 50 TYR 50 50 50 TYR TYR B . n B 2 51 PRO 51 51 51 PRO PRO B . n B 2 52 ASP 52 52 52 ASP ASP B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 THR 54 54 54 THR THR B . n B 2 55 ILE 55 55 55 ILE ILE B . n B 2 56 ARG 56 56 56 ARG ARG B . n B 2 57 SER 57 57 57 SER SER B . n B 2 58 LEU 58 58 58 LEU LEU B . n B 2 59 GLY 59 59 59 GLY GLY B . n B 2 60 LYS 60 60 60 LYS LYS B . n B 2 61 CYS 61 61 61 CYS CYS B . n B 2 62 LEU 62 62 62 LEU LEU B . n B 2 63 ALA 63 63 63 ALA ALA B . n B 2 64 THR 64 64 64 THR THR B . n B 2 65 SER 65 65 65 SER SER B . n B 2 66 ALA 66 66 66 ALA ALA B . n B 2 67 LEU 67 67 67 LEU LEU B . n B 2 68 SER 68 68 68 SER SER B . n B 2 69 SER 69 69 69 SER SER B . n B 2 70 GLY 70 70 70 GLY GLY B . n B 2 71 SER 71 71 71 SER SER B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 VAL 73 73 73 VAL VAL B . n B 2 74 VAL 74 74 74 VAL VAL B . n B 2 75 ILE 75 75 75 ILE ILE B . n B 2 76 THR 76 76 76 THR THR B . n B 2 77 ASN 77 77 77 ASN ASN B . n B 2 78 CYS 78 78 78 CYS CYS B . n B 2 79 ASP 79 79 79 ASP ASP B . n B 2 80 TYR 80 80 80 TYR TYR B . n B 2 81 LEU 81 81 81 LEU LEU B . n B 2 82 ARG 82 82 82 ARG ARG B . n B 2 83 TYR 83 83 83 TYR TYR B . n B 2 84 ASP 84 84 84 ASP ASP B . n B 2 85 ASP 85 85 85 ASP ASP B . n B 2 86 GLY 86 86 86 GLY GLY B . n B 2 87 TRP 87 87 87 TRP TRP B . n B 2 88 MET 88 88 88 MET MET B . n B 2 89 VAL 89 89 89 VAL VAL B . n B 2 90 SER 90 90 90 SER SER B . n B 2 91 SER 91 91 91 SER SER B . n B 2 92 SER 92 92 92 SER SER B . n B 2 93 GLY 93 93 93 GLY GLY B . n B 2 94 THR 94 94 94 THR THR B . n B 2 95 MET 95 95 95 MET MET B . n B 2 96 MET 96 96 96 MET MET B . n B 2 97 ASN 97 97 97 ASN ASN B . n B 2 98 LYS 98 98 98 LYS LYS B . n B 2 99 SER 99 99 99 SER SER B . n B 2 100 SER 100 100 100 SER SER B . n B 2 101 HIS 101 101 101 HIS HIS B . n B 2 102 LEU 102 102 102 LEU LEU B . n B 2 103 VAL 103 103 103 VAL VAL B . n B 2 104 LEU 104 104 104 LEU LEU B . n B 2 105 THR 105 105 105 THR THR B . n B 2 106 ALA 106 106 106 ALA ALA B . n B 2 107 ASN 107 107 107 ASN ASN B . n B 2 108 ALA 108 108 108 ALA ALA B . n B 2 109 ALA 109 109 109 ALA ALA B . n B 2 110 THR 110 110 110 THR THR B . n B 2 111 SER 111 111 111 SER SER B . n B 2 112 ARG 112 112 112 ARG ARG B . n B 2 113 THR 113 113 113 THR THR B . n B 2 114 ASN 114 114 114 ASN ASN B . n B 2 115 LEU 115 115 115 LEU LEU B . n B 2 116 THR 116 116 116 THR THR B . n B 2 117 GLY 117 117 117 GLY GLY B . n B 2 118 GLU 118 118 118 GLU GLU B . n B 2 119 ASN 119 119 119 ASN ASN B . n B 2 120 ASN 120 120 120 ASN ASN B . n B 2 121 VAL 121 121 121 VAL VAL B . n B 2 122 PHE 122 122 122 PHE PHE B . n B 2 123 ALA 123 123 123 ALA ALA B . n B 2 124 ALA 124 124 124 ALA ALA B . n B 2 125 LYS 125 125 125 LYS LYS B . n B 2 126 GLN 126 126 126 GLN GLN B . n B 2 127 ALA 127 127 127 ALA ALA B . n B 2 128 TRP 128 128 128 TRP TRP B . n B 2 129 ARG 129 129 129 ARG ARG B . n B 2 130 ILE 130 130 130 ILE ILE B . n B 2 131 GLY 131 131 131 GLY GLY B . n B 2 132 ASN 132 132 132 ASN ASN B . n B 2 133 TYR 133 133 133 TYR TYR B . n B 2 134 VAL 134 134 134 VAL VAL B . n B 2 135 GLU 135 135 135 GLU GLU B . n B 2 136 PRO 136 136 136 PRO PRO B . n B 2 137 ILE 137 137 137 ILE ILE B . n B 2 138 VAL 138 138 138 VAL VAL B . n B 2 139 THR 139 139 139 THR THR B . n B 2 140 THR 140 140 140 THR THR B . n B 2 141 ILE 141 141 141 ILE ILE B . n B 2 142 ILE 142 142 142 ILE ILE B . n B 2 143 GLY 143 143 143 GLY GLY B . n B 2 144 LEU 144 144 144 LEU LEU B . n B 2 145 ARG 145 145 145 ARG ARG B . n B 2 146 HIS 146 146 146 HIS HIS B . n B 2 147 MET 147 147 147 MET MET B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 LEU 149 149 149 LEU LEU B . n B 2 150 GLU 150 150 150 GLU GLU B . n B 2 151 ALA 151 151 151 ALA ALA B . n B 2 152 THR 152 152 152 THR THR B . n B 2 153 ASP 153 153 153 ASP ASP B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 ASP 155 155 155 ASP ASP B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 ASN 157 157 157 ASN ASN B . n B 2 158 VAL 158 158 158 VAL VAL B . n B 2 159 TRP 159 159 159 TRP TRP B . n B 2 160 LEU 160 160 160 LEU LEU B . n B 2 161 GLU 161 161 161 GLU GLU B . n B 2 162 SER 162 162 162 SER SER B . n B 2 163 CYS 163 163 163 CYS CYS B . n B 2 164 VAL 164 164 164 VAL VAL B . n B 2 165 LYS 165 165 165 LYS LYS B . n B 2 166 ASN 166 166 166 ASN ASN B . n B 2 167 LYS 167 167 167 LYS LYS B . n B 2 168 THR 168 168 168 THR THR B . n B 2 169 LYS 169 169 169 LYS LYS B . n B 2 170 GLN 170 170 170 GLN GLN B . n B 2 171 TYR 171 171 171 TYR TYR B . n B 2 172 TRP 172 172 172 TRP TRP B . n B 2 173 ALA 173 173 173 ALA ALA B . n B 2 174 LEU 174 174 174 LEU LEU B . n B 2 175 TYR 175 175 175 TYR TYR B . n B 2 176 SER 176 176 176 SER SER B . n B 2 177 ASP 177 177 177 ASP ASP B . n B 2 178 ASP 178 178 178 ASP ASP B . n B 2 179 THR 179 179 179 THR THR B . n B 2 180 ILE 180 180 180 ILE ILE B . n B 2 181 ARG 181 181 181 ARG ARG B . n B 2 182 VAL 182 182 182 VAL VAL B . n B 2 183 ASN 183 183 183 ASN ASN B . n B 2 184 ASN 184 184 184 ASN ASN B . n B 2 185 ASN 185 185 185 ASN ASN B . n B 2 186 ARG 186 186 186 ARG ARG B . n B 2 187 ASN 187 187 187 ASN ASN B . n B 2 188 LEU 188 188 188 LEU LEU B . n B 2 189 CYS 189 189 189 CYS CYS B . n B 2 190 VAL 190 190 190 VAL VAL B . n B 2 191 SER 191 191 191 SER SER B . n B 2 192 SER 192 192 192 SER SER B . n B 2 193 SER 193 193 193 SER SER B . n B 2 194 THR 194 194 194 THR THR B . n B 2 195 ASP 195 195 195 ASP ASP B . n B 2 196 SER 196 196 196 SER SER B . n B 2 197 SER 197 197 197 SER SER B . n B 2 198 SER 198 198 198 SER SER B . n B 2 199 LYS 199 199 199 LYS LYS B . n B 2 200 LEU 200 200 200 LEU LEU B . n B 2 201 ILE 201 201 201 ILE ILE B . n B 2 202 VAL 202 202 202 VAL VAL B . n B 2 203 ILE 203 203 203 ILE ILE B . n B 2 204 ARG 204 204 204 ARG ARG B . n B 2 205 ARG 205 205 205 ARG ARG B . n B 2 206 CYS 206 206 206 CYS CYS B . n B 2 207 ASP 207 207 207 ASP ASP B . n B 2 208 GLY 208 208 208 GLY GLY B . n B 2 209 SER 209 209 209 SER SER B . n B 2 210 ILE 210 210 210 ILE ILE B . n B 2 211 ASN 211 211 211 ASN ASN B . n B 2 212 GLN 212 212 212 GLN GLN B . n B 2 213 ARG 213 213 213 ARG ARG B . n B 2 214 TRP 214 214 214 TRP TRP B . n B 2 215 VAL 215 215 215 VAL VAL B . n B 2 216 PHE 216 216 216 PHE PHE B . n B 2 217 THR 217 217 217 THR THR B . n B 2 218 PRO 218 218 218 PRO PRO B . n B 2 219 GLN 219 219 219 GLN GLN B . n B 2 220 GLY 220 220 220 GLY GLY B . n B 2 221 THR 221 221 221 THR THR B . n B 2 222 ILE 222 222 222 ILE ILE B . n B 2 223 SER 223 223 223 SER SER B . n B 2 224 ASN 224 224 224 ASN ASN B . n B 2 225 PRO 225 225 225 PRO PRO B . n B 2 226 GLY 226 226 226 GLY GLY B . n B 2 227 TYR 227 227 227 TYR TYR B . n B 2 228 GLU 228 228 228 GLU GLU B . n B 2 229 ALA 229 229 229 ALA ALA B . n B 2 230 VAL 230 230 230 VAL VAL B . n B 2 231 MET 231 231 231 MET MET B . n B 2 232 ASP 232 232 232 ASP ASP B . n B 2 233 VAL 233 233 233 VAL VAL B . n B 2 234 ALA 234 234 234 ALA ALA B . n B 2 235 GLN 235 235 235 GLN GLN B . n B 2 236 ASN 236 236 236 ASN ASN B . n B 2 237 ASP 237 237 237 ASP ASP B . n B 2 238 VAL 238 238 238 VAL VAL B . n B 2 239 TYR 239 239 239 TYR TYR B . n B 2 240 LEU 240 240 240 LEU LEU B . n B 2 241 LYS 241 241 241 LYS LYS B . n B 2 242 LYS 242 242 242 LYS LYS B . n B 2 243 ILE 243 243 243 ILE ILE B . n B 2 244 VAL 244 244 244 VAL VAL B . n B 2 245 LEU 245 245 245 LEU LEU B . n B 2 246 SER 246 246 246 SER SER B . n B 2 247 SER 247 247 247 SER SER B . n B 2 248 ALA 248 248 248 ALA ALA B . n B 2 249 THR 249 249 249 THR THR B . n B 2 250 ASP 250 250 250 ASP ASP B . n B 2 251 LYS 251 251 251 LYS LYS B . n B 2 252 GLY 252 252 252 GLY GLY B . n B 2 253 ASN 253 253 253 ASN ASN B . n B 2 254 GLY 254 254 254 GLY GLY B . n B 2 255 GLN 255 255 255 GLN GLN B . n B 2 256 GLN 256 256 256 GLN GLN B . n B 2 257 TRP 257 257 257 TRP TRP B . n B 2 258 THR 258 258 258 THR THR B . n B 2 259 VAL 259 259 259 VAL VAL B . n B 2 260 PHE 260 260 260 PHE PHE B . n B 2 261 TYR 261 261 261 TYR TYR 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 C 3 NAG 1 301 301 NAG NAG A . D 4 PO4 1 302 302 PO4 PO4 A . E 3 NAG 1 301 301 NAG NAG B . F 5 FUC 2 302 302 FUC FUC B . G 3 NAG 1 303 303 NAG NAG B . H 3 NAG 1 304 304 NAG NAG B . I 3 NAG 2 305 305 NAG NAG B . J 6 BMA 1 306 306 BMA BMA B . K 7 EDO 1 307 307 EDO EDO B . L 8 PGE 1 308 308 PGE PGE B . M 9 GAL 1 309 309 GAL GAL B . N 10 A2G 1 310 310 A2G A2G B . O 11 MBN 1 311 311 MBN MBN B . P 12 HOH 1 401 401 HOH HOH A . P 12 HOH 2 402 402 HOH HOH A . P 12 HOH 3 403 403 HOH HOH A . P 12 HOH 4 404 404 HOH HOH A . P 12 HOH 5 405 405 HOH HOH A . P 12 HOH 6 406 406 HOH HOH A . P 12 HOH 7 407 407 HOH HOH A . P 12 HOH 8 408 408 HOH HOH A . P 12 HOH 9 409 409 HOH HOH A . P 12 HOH 10 410 410 HOH HOH A . P 12 HOH 11 411 411 HOH HOH A . P 12 HOH 12 412 412 HOH HOH A . P 12 HOH 13 413 413 HOH HOH A . P 12 HOH 14 414 414 HOH HOH A . P 12 HOH 15 415 415 HOH HOH A . P 12 HOH 16 416 416 HOH HOH A . P 12 HOH 17 417 417 HOH HOH A . P 12 HOH 18 418 418 HOH HOH A . P 12 HOH 19 419 419 HOH HOH A . P 12 HOH 20 420 420 HOH HOH A . P 12 HOH 21 421 421 HOH HOH A . P 12 HOH 22 422 422 HOH HOH A . P 12 HOH 23 423 423 HOH HOH A . P 12 HOH 24 424 424 HOH HOH A . P 12 HOH 25 425 425 HOH HOH A . P 12 HOH 26 426 426 HOH HOH A . P 12 HOH 27 427 427 HOH HOH A . P 12 HOH 28 428 428 HOH HOH A . P 12 HOH 29 429 429 HOH HOH A . P 12 HOH 30 430 430 HOH HOH A . P 12 HOH 31 431 431 HOH HOH A . P 12 HOH 32 432 432 HOH HOH A . P 12 HOH 33 433 433 HOH HOH A . P 12 HOH 34 434 434 HOH HOH A . P 12 HOH 35 435 435 HOH HOH A . P 12 HOH 36 436 436 HOH HOH A . P 12 HOH 37 437 437 HOH HOH A . P 12 HOH 38 438 438 HOH HOH A . P 12 HOH 39 439 439 HOH HOH A . P 12 HOH 40 440 440 HOH HOH A . P 12 HOH 41 441 441 HOH HOH A . P 12 HOH 42 442 442 HOH HOH A . P 12 HOH 43 443 443 HOH HOH A . P 12 HOH 44 444 444 HOH HOH A . P 12 HOH 45 445 445 HOH HOH A . P 12 HOH 46 446 446 HOH HOH A . P 12 HOH 47 447 447 HOH HOH A . P 12 HOH 48 448 448 HOH HOH A . P 12 HOH 49 449 449 HOH HOH A . P 12 HOH 50 450 450 HOH HOH A . P 12 HOH 51 451 451 HOH HOH A . P 12 HOH 52 452 452 HOH HOH A . P 12 HOH 53 453 453 HOH HOH A . P 12 HOH 54 454 454 HOH HOH A . P 12 HOH 55 455 455 HOH HOH A . P 12 HOH 56 456 456 HOH HOH A . P 12 HOH 57 457 457 HOH HOH A . P 12 HOH 58 458 458 HOH HOH A . P 12 HOH 59 459 459 HOH HOH A . P 12 HOH 60 460 460 HOH HOH A . P 12 HOH 61 461 461 HOH HOH A . P 12 HOH 62 462 462 HOH HOH A . P 12 HOH 63 463 463 HOH HOH A . P 12 HOH 64 464 464 HOH HOH A . P 12 HOH 65 465 465 HOH HOH A . P 12 HOH 66 466 466 HOH HOH A . P 12 HOH 67 467 467 HOH HOH A . P 12 HOH 68 468 468 HOH HOH A . P 12 HOH 69 469 469 HOH HOH A . P 12 HOH 70 470 470 HOH HOH A . P 12 HOH 71 471 471 HOH HOH A . P 12 HOH 72 472 472 HOH HOH A . P 12 HOH 73 473 473 HOH HOH A . P 12 HOH 74 474 474 HOH HOH A . P 12 HOH 75 475 475 HOH HOH A . P 12 HOH 76 476 476 HOH HOH A . P 12 HOH 77 477 477 HOH HOH A . P 12 HOH 78 478 478 HOH HOH A . P 12 HOH 79 479 479 HOH HOH A . P 12 HOH 80 480 480 HOH HOH A . P 12 HOH 81 481 481 HOH HOH A . P 12 HOH 82 482 482 HOH HOH A . P 12 HOH 83 483 483 HOH HOH A . P 12 HOH 84 484 484 HOH HOH A . P 12 HOH 85 485 485 HOH HOH A . P 12 HOH 86 486 486 HOH HOH A . P 12 HOH 87 487 487 HOH HOH A . P 12 HOH 88 488 488 HOH HOH A . P 12 HOH 89 489 489 HOH HOH A . P 12 HOH 90 490 490 HOH HOH A . P 12 HOH 91 491 491 HOH HOH A . P 12 HOH 92 492 492 HOH HOH A . P 12 HOH 93 493 493 HOH HOH A . P 12 HOH 94 494 494 HOH HOH A . P 12 HOH 95 495 495 HOH HOH A . P 12 HOH 96 496 496 HOH HOH A . P 12 HOH 97 497 497 HOH HOH A . P 12 HOH 98 498 498 HOH HOH A . P 12 HOH 99 499 499 HOH HOH A . P 12 HOH 100 500 500 HOH HOH A . P 12 HOH 101 501 501 HOH HOH A . P 12 HOH 102 502 502 HOH HOH A . P 12 HOH 103 503 503 HOH HOH A . P 12 HOH 104 504 504 HOH HOH A . P 12 HOH 105 505 505 HOH HOH A . P 12 HOH 106 506 506 HOH HOH A . P 12 HOH 107 507 507 HOH HOH A . P 12 HOH 108 508 508 HOH HOH A . P 12 HOH 109 509 509 HOH HOH A . P 12 HOH 110 510 510 HOH HOH A . P 12 HOH 111 511 511 HOH HOH A . P 12 HOH 112 512 512 HOH HOH A . P 12 HOH 113 513 513 HOH HOH A . P 12 HOH 114 514 514 HOH HOH A . P 12 HOH 115 515 515 HOH HOH A . P 12 HOH 116 516 516 HOH HOH A . P 12 HOH 117 517 517 HOH HOH A . P 12 HOH 118 518 518 HOH HOH A . P 12 HOH 119 519 519 HOH HOH A . P 12 HOH 120 520 520 HOH HOH A . P 12 HOH 121 521 521 HOH HOH A . P 12 HOH 122 522 522 HOH HOH A . P 12 HOH 123 523 523 HOH HOH A . P 12 HOH 124 524 524 HOH HOH A . P 12 HOH 125 525 525 HOH HOH A . P 12 HOH 126 526 526 HOH HOH A . P 12 HOH 127 527 527 HOH HOH A . P 12 HOH 128 528 528 HOH HOH A . P 12 HOH 129 529 529 HOH HOH A . P 12 HOH 130 530 530 HOH HOH A . P 12 HOH 131 531 531 HOH HOH A . P 12 HOH 132 532 532 HOH HOH A . P 12 HOH 133 533 533 HOH HOH A . Q 12 HOH 1 401 401 HOH HOH B . Q 12 HOH 2 402 402 HOH HOH B . Q 12 HOH 3 403 403 HOH HOH B . Q 12 HOH 4 404 404 HOH HOH B . Q 12 HOH 5 405 405 HOH HOH B . Q 12 HOH 6 406 406 HOH HOH B . Q 12 HOH 7 407 407 HOH HOH B . Q 12 HOH 8 408 408 HOH HOH B . Q 12 HOH 9 409 409 HOH HOH B . Q 12 HOH 10 410 410 HOH HOH B . Q 12 HOH 11 411 411 HOH HOH B . Q 12 HOH 12 412 412 HOH HOH B . Q 12 HOH 13 413 413 HOH HOH B . Q 12 HOH 14 414 414 HOH HOH B . Q 12 HOH 15 415 415 HOH HOH B . Q 12 HOH 16 416 416 HOH HOH B . Q 12 HOH 17 417 417 HOH HOH B . Q 12 HOH 18 418 418 HOH HOH B . Q 12 HOH 19 419 419 HOH HOH B . Q 12 HOH 20 420 420 HOH HOH B . Q 12 HOH 21 421 421 HOH HOH B . Q 12 HOH 22 422 422 HOH HOH B . Q 12 HOH 23 423 423 HOH HOH B . Q 12 HOH 24 424 424 HOH HOH B . Q 12 HOH 25 425 425 HOH HOH B . Q 12 HOH 26 426 426 HOH HOH B . Q 12 HOH 27 427 427 HOH HOH B . Q 12 HOH 28 428 428 HOH HOH B . Q 12 HOH 29 429 429 HOH HOH B . Q 12 HOH 30 430 430 HOH HOH B . Q 12 HOH 31 431 431 HOH HOH B . Q 12 HOH 32 432 432 HOH HOH B . Q 12 HOH 33 433 433 HOH HOH B . Q 12 HOH 34 434 434 HOH HOH B . Q 12 HOH 35 435 435 HOH HOH B . Q 12 HOH 36 436 436 HOH HOH B . Q 12 HOH 37 437 437 HOH HOH B . Q 12 HOH 38 438 438 HOH HOH B . Q 12 HOH 39 439 439 HOH HOH B . Q 12 HOH 40 440 440 HOH HOH B . Q 12 HOH 41 441 441 HOH HOH B . Q 12 HOH 42 442 442 HOH HOH B . Q 12 HOH 43 443 443 HOH HOH B . Q 12 HOH 44 444 444 HOH HOH B . Q 12 HOH 45 445 445 HOH HOH B . Q 12 HOH 46 446 446 HOH HOH B . Q 12 HOH 47 447 447 HOH HOH B . Q 12 HOH 48 448 448 HOH HOH B . Q 12 HOH 49 449 449 HOH HOH B . Q 12 HOH 50 450 450 HOH HOH B . Q 12 HOH 51 451 451 HOH HOH B . Q 12 HOH 52 452 452 HOH HOH B . Q 12 HOH 53 453 453 HOH HOH B . Q 12 HOH 54 454 454 HOH HOH B . Q 12 HOH 55 455 455 HOH HOH B . Q 12 HOH 56 456 456 HOH HOH B . Q 12 HOH 57 457 457 HOH HOH B . Q 12 HOH 58 458 458 HOH HOH B . Q 12 HOH 59 459 459 HOH HOH B . Q 12 HOH 60 460 460 HOH HOH B . Q 12 HOH 61 461 461 HOH HOH B . Q 12 HOH 62 462 462 HOH HOH B . Q 12 HOH 63 463 463 HOH HOH B . Q 12 HOH 64 464 464 HOH HOH B . Q 12 HOH 65 465 465 HOH HOH B . Q 12 HOH 66 466 466 HOH HOH B . Q 12 HOH 67 467 467 HOH HOH B . Q 12 HOH 68 468 468 HOH HOH B . Q 12 HOH 69 469 469 HOH HOH B . Q 12 HOH 70 470 470 HOH HOH B . Q 12 HOH 71 471 471 HOH HOH B . Q 12 HOH 72 472 472 HOH HOH B . Q 12 HOH 73 473 473 HOH HOH B . Q 12 HOH 74 474 474 HOH HOH B . Q 12 HOH 75 475 475 HOH HOH B . Q 12 HOH 76 476 476 HOH HOH B . Q 12 HOH 77 477 477 HOH HOH B . Q 12 HOH 78 478 478 HOH HOH B . Q 12 HOH 79 479 479 HOH HOH B . Q 12 HOH 80 480 480 HOH HOH B . Q 12 HOH 81 481 481 HOH HOH B . Q 12 HOH 82 482 482 HOH HOH B . Q 12 HOH 83 483 483 HOH HOH B . Q 12 HOH 84 484 484 HOH HOH B . Q 12 HOH 85 485 485 HOH HOH B . Q 12 HOH 86 486 486 HOH HOH B . Q 12 HOH 87 487 487 HOH HOH B . Q 12 HOH 88 488 488 HOH HOH B . Q 12 HOH 89 489 489 HOH HOH B . Q 12 HOH 90 490 490 HOH HOH B . Q 12 HOH 91 491 491 HOH HOH B . Q 12 HOH 92 492 492 HOH HOH B . Q 12 HOH 93 493 493 HOH HOH B . Q 12 HOH 94 494 494 HOH HOH B . Q 12 HOH 95 495 495 HOH HOH B . Q 12 HOH 96 496 496 HOH HOH B . Q 12 HOH 97 497 497 HOH HOH B . Q 12 HOH 98 498 498 HOH HOH B . Q 12 HOH 99 499 499 HOH HOH B . Q 12 HOH 100 500 500 HOH HOH B . Q 12 HOH 101 501 501 HOH HOH B . Q 12 HOH 102 502 502 HOH HOH B . Q 12 HOH 103 503 503 HOH HOH B . Q 12 HOH 104 504 504 HOH HOH B . Q 12 HOH 105 505 505 HOH HOH B . Q 12 HOH 106 506 506 HOH HOH B . Q 12 HOH 107 507 507 HOH HOH B . Q 12 HOH 108 508 508 HOH HOH B . Q 12 HOH 109 509 509 HOH HOH B . Q 12 HOH 110 510 510 HOH HOH B . Q 12 HOH 111 511 511 HOH HOH B . Q 12 HOH 112 512 512 HOH HOH B . Q 12 HOH 113 513 513 HOH HOH B . Q 12 HOH 114 514 514 HOH HOH B . Q 12 HOH 115 515 515 HOH HOH B . Q 12 HOH 116 516 516 HOH HOH B . Q 12 HOH 117 517 517 HOH HOH B . Q 12 HOH 118 518 518 HOH HOH B . Q 12 HOH 119 519 519 HOH HOH B . Q 12 HOH 120 520 520 HOH HOH B . Q 12 HOH 121 521 521 HOH HOH B . Q 12 HOH 122 522 522 HOH HOH B . Q 12 HOH 123 523 523 HOH HOH B . Q 12 HOH 124 524 524 HOH HOH B . Q 12 HOH 125 525 525 HOH HOH B . Q 12 HOH 126 526 526 HOH HOH B . Q 12 HOH 127 527 527 HOH HOH B . Q 12 HOH 128 528 528 HOH HOH B . Q 12 HOH 129 529 529 HOH HOH B . Q 12 HOH 130 530 530 HOH HOH B . Q 12 HOH 131 531 531 HOH HOH B . Q 12 HOH 132 532 532 HOH HOH B . Q 12 HOH 133 533 533 HOH HOH B . Q 12 HOH 134 534 534 HOH HOH B . Q 12 HOH 135 535 535 HOH HOH B . Q 12 HOH 136 536 536 HOH HOH B . Q 12 HOH 137 537 537 HOH HOH B . Q 12 HOH 138 538 538 HOH HOH B . Q 12 HOH 139 539 539 HOH HOH B . Q 12 HOH 140 540 540 HOH HOH B . Q 12 HOH 141 541 541 HOH HOH B . Q 12 HOH 142 542 542 HOH HOH B . Q 12 HOH 143 543 543 HOH HOH B . Q 12 HOH 144 544 544 HOH HOH B . Q 12 HOH 145 545 545 HOH HOH B . Q 12 HOH 146 546 546 HOH HOH B . Q 12 HOH 147 547 547 HOH HOH B . Q 12 HOH 148 548 548 HOH HOH B . Q 12 HOH 149 549 549 HOH HOH B . Q 12 HOH 150 550 550 HOH HOH B . Q 12 HOH 151 551 551 HOH HOH B . Q 12 HOH 152 552 552 HOH HOH B . Q 12 HOH 153 553 553 HOH HOH B . Q 12 HOH 154 554 554 HOH HOH B . Q 12 HOH 155 555 555 HOH HOH B . Q 12 HOH 156 556 556 HOH HOH B . Q 12 HOH 157 557 557 HOH HOH B . Q 12 HOH 158 558 558 HOH HOH B . Q 12 HOH 159 559 559 HOH HOH B . Q 12 HOH 160 560 560 HOH HOH B . Q 12 HOH 161 561 561 HOH HOH B . Q 12 HOH 162 562 562 HOH HOH B . Q 12 HOH 163 563 563 HOH HOH B . Q 12 HOH 164 564 564 HOH HOH B . Q 12 HOH 165 565 565 HOH HOH B . Q 12 HOH 166 566 566 HOH HOH B . Q 12 HOH 167 567 567 HOH HOH B . Q 12 HOH 168 568 568 HOH HOH B . Q 12 HOH 169 569 569 HOH HOH B . Q 12 HOH 170 570 570 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 6420 ? 1 MORE 4 ? 1 'SSA (A^2)' 21370 ? # _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 2016-03-23 # _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 ? # _diffrn_reflns.diffrn_id 1 _diffrn_reflns.pdbx_d_res_high 2.000 _diffrn_reflns.pdbx_d_res_low 94.874 _diffrn_reflns.pdbx_number_obs 56031 _diffrn_reflns.pdbx_Rmerge_I_obs ? _diffrn_reflns.pdbx_Rsym_value 0.279 _diffrn_reflns.pdbx_chi_squared ? _diffrn_reflns.pdbx_redundancy 8.90 _diffrn_reflns.pdbx_rejects ? _diffrn_reflns.pdbx_percent_possible_obs 100.00 _diffrn_reflns.pdbx_observed_criterion ? _diffrn_reflns.number 499074 _diffrn_reflns.limit_h_max ? _diffrn_reflns.limit_h_min ? _diffrn_reflns.limit_k_max ? _diffrn_reflns.limit_k_min ? _diffrn_reflns.limit_l_max ? _diffrn_reflns.limit_l_min ? # loop_ _pdbx_diffrn_reflns_shell.diffrn_id _pdbx_diffrn_reflns_shell.d_res_high _pdbx_diffrn_reflns_shell.d_res_low _pdbx_diffrn_reflns_shell.number_obs _pdbx_diffrn_reflns_shell.rejects _pdbx_diffrn_reflns_shell.Rmerge_I_obs _pdbx_diffrn_reflns_shell.Rsym_value _pdbx_diffrn_reflns_shell.chi_squared _pdbx_diffrn_reflns_shell.redundancy _pdbx_diffrn_reflns_shell.percent_possible_obs 1 6.32 32.62 ? ? 0.081 0.081 ? 8.00 ? 1 4.47 6.32 ? ? 0.111 0.111 ? 8.70 ? 1 3.65 4.47 ? ? 0.125 0.125 ? 8.90 ? 1 3.16 3.65 ? ? 0.165 0.165 ? 9.00 ? 1 2.83 3.16 ? ? 0.249 0.249 ? 9.00 ? 1 2.58 2.83 ? ? 0.377 0.377 ? 9.00 ? 1 2.39 2.58 ? ? 0.541 0.541 ? 9.00 ? 1 2.24 2.39 ? ? 0.758 0.758 ? 8.90 ? 1 2.11 2.24 ? ? 0.947 0.947 ? 8.90 ? 1 2.00 2.11 ? ? 1.246 1.246 ? 8.90 ? # _phasing.method MR # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0107 1 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALA ? ? ? 3.3.21 2 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.5.2 3 ? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 C1 B GAL 309 ? ? O3 B A2G 310 ? ? 1.06 2 1 ND2 A ASN 108 ? ? C1 A NAG 301 ? ? 1.17 3 1 O4 B NAG 301 ? ? C1 B NAG 303 ? ? 1.60 4 1 O5 B GAL 309 ? ? O3 B A2G 310 ? ? 1.88 5 1 O4 B NAG 303 ? ? C1 B BMA 306 ? ? 2.19 # 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 79 ? ? 58.45 -116.15 2 1 VAL A 158 ? ? -108.34 -63.21 3 1 TYR A 231 ? ? -97.31 33.16 4 1 LEU A 235 ? ? -96.18 -63.05 5 1 ASN A 238 ? ? -121.35 -60.48 6 1 GLN A 245 ? ? -143.31 -50.05 7 1 LYS B 125 ? ? -68.02 1.85 8 1 ASN B 185 ? ? -153.77 88.69 9 1 ASP B 207 ? ? -140.42 11.09 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 533 ? 7.71 . 2 1 O ? B HOH 570 ? 6.06 . # 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 ASP 99 ? CG ? A ASP 99 CG 2 1 Y 1 A ASP 99 ? OD1 ? A ASP 99 OD1 3 1 Y 1 A ASP 99 ? OD2 ? A ASP 99 OD2 4 1 Y 1 A GLU 124 ? CG ? A GLU 124 CG 5 1 Y 1 A GLU 124 ? CD ? A GLU 124 CD 6 1 Y 1 A GLU 124 ? OE1 ? A GLU 124 OE1 7 1 Y 1 A GLU 124 ? OE2 ? A GLU 124 OE2 8 1 Y 1 A GLU 144 ? OE1 ? A GLU 144 OE1 9 1 Y 1 B GLU 2 ? CG ? B GLU 2 CG 10 1 Y 1 B GLU 2 ? CD ? B GLU 2 CD 11 1 Y 1 B GLU 2 ? OE1 ? B GLU 2 OE1 12 1 Y 1 B GLU 2 ? OE2 ? B GLU 2 OE2 13 1 Y 1 B ARG 82 ? CB ? B ARG 82 CB 14 1 Y 1 B ARG 82 ? CG ? B ARG 82 CG 15 1 Y 1 B ARG 82 ? CD ? B ARG 82 CD 16 1 Y 1 B ARG 82 ? NE ? B ARG 82 NE 17 1 Y 1 B ARG 82 ? CZ ? B ARG 82 CZ 18 1 Y 1 B ARG 82 ? NH1 ? B ARG 82 NH1 19 1 Y 1 B ARG 82 ? NH2 ? B ARG 82 NH2 20 1 Y 1 B LYS 165 ? CE ? B LYS 165 CE 21 1 Y 1 B LYS 165 ? NZ ? B LYS 165 NZ 22 1 Y 1 B ARG 205 ? NE ? B ARG 205 NE 23 1 Y 1 B ARG 205 ? CZ ? B ARG 205 CZ 24 1 Y 1 B ARG 205 ? NH1 ? B ARG 205 NH1 25 1 Y 1 B ARG 205 ? NH2 ? B ARG 205 NH2 26 1 Y 1 B LYS 251 ? CG ? B LYS 251 CG 27 1 Y 1 B LYS 251 ? CD ? B LYS 251 CD 28 1 Y 1 B LYS 251 ? CE ? B LYS 251 CE 29 1 Y 1 B LYS 251 ? NZ ? B LYS 251 NZ 30 1 N 1 A NAG 301 ? O1 ? C NAG 1 O1 31 1 N 1 B NAG 303 ? O1 ? G NAG 1 O1 32 1 N 1 B BMA 306 ? O1 ? J BMA 1 O1 33 1 N 1 B GAL 309 ? O1 ? M GAL 1 O1 # _pdbx_audit_support.funding_organization 'Science and Engineering Research Board, Department of Science and Technology' _pdbx_audit_support.country India _pdbx_audit_support.grant_number ? _pdbx_audit_support.ordinal 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'PHOSPHATE ION' PO4 5 ALPHA-L-FUCOSE FUC 6 BETA-D-MANNOSE BMA 7 1,2-ETHANEDIOL EDO 8 'TRIETHYLENE GLYCOL' PGE 9 BETA-D-GALACTOSE GAL 10 N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE A2G 11 TOLUENE MBN 12 water HOH #