data_4ZGR # _entry.id 4ZGR # _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 4ZGR WWPDB D_1000209230 # _pdbx_database_related.db_name PDB _pdbx_database_related.details 'the same protein in native form' _pdbx_database_related.db_id 4Z8S _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 4ZGR _pdbx_database_status.recvd_initial_deposition_date 2015-04-23 _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 ? ? ? ? ? ? ? ? US ? ? 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.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 90.00 _cell.angle_beta_esd ? _cell.angle_gamma 90.00 _cell.angle_gamma_esd ? _cell.entry_id 4ZGR _cell.details ? _cell.formula_units_Z ? _cell.length_a 144.370 _cell.length_a_esd ? _cell.length_b 135.800 _cell.length_b_esd ? _cell.length_c 44.890 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 4 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 4ZGR _symmetry.cell_setting ? _symmetry.Int_Tables_number 18 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 21 21 2' _symmetry.pdbx_full_space_group_name_H-M ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer 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 GLYCEROL 92.094 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GALACTOSAMINE 221.208 1 ? ? ? ? 6 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 7 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 8 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 9 non-polymer man BETA-D-XYLOPYRANOSE 150.130 1 ? ? ? ? 10 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 11 water nat water 18.015 397 ? ? ? ? # 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.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin 1 UNP B7X8M2_MOMCH B7X8M2 ? 1 ;NLSLSQSNFSADTYKSFIKNLRKQLTIGASYGSAGIPILKHSVPICERFLLVDLTNGDNETITLAINVEDAGFAAYRAAD RSYFFQNAPPIASYVIFTDTNQNIMNFNNTFESIEIVGGTTRSETPLGIMHFEASIFHLFVHDENYVPTSFLVLIQMVLE AAKFKFIEQKVIHSIMDMEDFTPGLAMLSLEENWTQLSLQLQASESLNGVFGDSVSLYNSMDEPIGVDSMYYPILTANMA FQLYQCP ; 24 2 UNP B7X8M2_MOMCH B7X8M2 ? 2 ;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 4ZGR A 1 ? 247 ? B7X8M2 24 ? 270 ? 1 247 2 2 4ZGR 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 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 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 NGA D-saccharide . N-ACETYL-D-GALACTOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 XYP D-saccharide . BETA-D-XYLOPYRANOSE ? 'C5 H10 O5' 150.130 # _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 4ZGR _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.88 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 68.33 _exptl_crystal.description orthorhombic _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 '0.1M HEPES, 20% w/v PEG 10000, glycerol' _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 2013-07-09 # _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 0.95372 _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 0.95372 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BM14 _diffrn_source.pdbx_synchrotron_site ESRF # _reflns.B_iso_Wilson_estimate 25.9 _reflns.entry_id 4ZGR _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.97 _reflns.d_resolution_low 39.26 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all 63830 _reflns.number_obs 63830 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 100 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 7.3 _reflns.pdbx_Rmerge_I_obs 0.085 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 14.5 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 1.97 _reflns_shell.d_res_low 2.07 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 4.4 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all 100 _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy 7.1 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.aniso_B[1][1] 2.69 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][2] -1.18 _refine.aniso_B[2][3] 0.00 _refine.aniso_B[3][3] -1.51 _refine.B_iso_max ? _refine.B_iso_mean 28.773 _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc 0.957 _refine.correlation_coeff_Fo_to_Fc_free 0.948 _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 4ZGR _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 1.97 _refine.ls_d_res_low 39.26 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 60530 _refine.ls_number_reflns_R_free 3232 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 99.98 _refine.ls_percent_reflns_R_free 5.1 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.17958 _refine.ls_R_factor_R_free 0.19769 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.17857 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details MASK _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 4Z8S _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.117 _refine.pdbx_overall_ESU_R_Free 0.108 _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B 2.898 _refine.overall_SU_ML 0.081 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_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 397 _refine_hist.number_atoms_total 4485 _refine_hist.d_res_high 1.97 _refine_hist.d_res_low 39.26 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.011 0.020 4212 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 0.010 0.020 3860 ? r_bond_other_d ? ? 'X-RAY DIFFRACTION' ? 1.516 1.977 5737 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 2.121 3.000 8889 ? r_angle_other_deg ? ? 'X-RAY DIFFRACTION' ? 6.597 5.000 506 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 33.948 24.974 191 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 10.954 15.000 670 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 16.720 15.000 19 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.092 0.200 678 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.006 0.020 4722 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 0.001 0.020 969 ? r_gen_planes_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? 1.408 2.621 2030 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 1.408 2.621 2029 ? r_mcbond_other ? ? 'X-RAY DIFFRACTION' ? 2.115 3.923 2534 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 2.114 3.923 2535 ? r_mcangle_other ? ? 'X-RAY DIFFRACTION' ? 2.268 3.068 2180 ? r_scbond_it ? ? 'X-RAY DIFFRACTION' ? 2.268 3.068 2180 ? r_scbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_scangle_it ? ? 'X-RAY DIFFRACTION' ? 3.533 4.503 3204 ? r_scangle_other ? ? 'X-RAY DIFFRACTION' ? 5.371 22.888 4985 ? r_long_range_B_refined ? ? 'X-RAY DIFFRACTION' ? 5.371 22.888 4985 ? r_long_range_B_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_rigid_bond_restr ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_free ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_bonded ? ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.d_res_high 1.967 _refine_ls_shell.d_res_low 2.018 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free 239 _refine_ls_shell.number_reflns_R_work 4376 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_obs ? _refine_ls_shell.R_factor_R_free 0.268 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.R_factor_R_work 0.250 _refine_ls_shell.redundancy_reflns_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.wR_factor_all ? _refine_ls_shell.wR_factor_obs ? _refine_ls_shell.wR_factor_R_free ? _refine_ls_shell.wR_factor_R_work ? _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.pdbx_phase_error ? _refine_ls_shell.pdbx_fsc_work ? _refine_ls_shell.pdbx_fsc_free ? # _struct.entry_id 4ZGR _struct.title 'Structural studies on a non-toxic homologue of type II RIPs from Momordica charantia (bitter gourd) in complex with 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 4ZGR _struct_keywords.text 'beta-trefoil, Type II RIPs, Galactose binding 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 5 ? F N N 6 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 7 ? K N N 3 ? L N N 8 ? M N N 9 ? N N N 10 ? O N N 11 ? P N N 11 ? # 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 ? LEU A 207 ? GLU A 205 LEU A 207 5 ? 3 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 ? MET B 147 ? GLY B 143 MET B 147 5 ? 5 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 ? ? ? ? ? ? ? 2.296 ? disulf2 disulf ? ? B CYS 20 SG ? ? ? 1_555 B CYS 39 SG ? ? B CYS 20 B CYS 39 1_555 ? ? ? ? ? ? ? 2.052 ? disulf3 disulf ? ? B CYS 61 SG ? ? ? 1_555 B CYS 78 SG ? ? B CYS 61 B CYS 78 1_555 ? ? ? ? ? ? ? 2.408 ? disulf4 disulf ? ? B CYS 148 SG ? ? ? 1_555 B CYS 163 SG ? ? B CYS 148 B CYS 163 1_555 ? ? ? ? ? ? ? 2.092 ? disulf5 disulf ? ? B CYS 189 SG ? ? ? 1_555 B CYS 206 SG ? ? B CYS 189 B CYS 206 1_555 ? ? ? ? ? ? ? 2.037 ? disulf6 disulf ? ? A CYS 46 SG ? ? ? 1_555 A CYS 46 SG ? ? A CYS 46 A CYS 46 2_665 ? ? ? ? ? ? ? 2.055 ? covale1 covale one ? B ASN 97 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 97 B NAG 303 1_555 ? ? ? ? ? ? ? 1.322 ? covale2 covale one ? B ASN 114 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 114 B NAG 305 1_555 ? ? ? ? ? ? ? 1.372 ? covale3 covale one ? E NGA . O3 ? ? ? 1_555 F GAL . C1 ? ? B NGA 301 B GAL 302 1_555 ? ? ? ? ? ? ? 1.472 ? covale4 covale both ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? B NAG 303 B NAG 304 1_555 ? ? ? ? ? ? ? 1.422 ? covale5 covale one ? I NAG . O3 ? ? ? 1_555 J FUC . C1 ? ? B NAG 305 B FUC 306 1_555 ? ? ? ? ? ? ? 1.421 ? covale6 covale both ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? B NAG 307 B BMA 308 1_555 ? ? ? ? ? ? ? 1.439 ? # 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 ? 7 ? 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 AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA4 4 5 ? anti-parallel AA4 5 6 ? anti-parallel AA4 6 7 ? 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 PHE A 73 ? ALA A 78 ? PHE A 73 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 SER B 71 ? THR B 76 ? SER B 71 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 ARG B 9 ? THR B 11 ? ARG B 9 THR B 11 AA4 2 TRP B 47 ? PHE B 49 ? TRP B 47 PHE B 49 AA4 3 ILE B 55 ? SER B 57 ? ILE B 55 SER B 57 AA4 4 LYS B 60 ? THR B 64 ? LYS B 60 THR B 64 AA4 5 SER B 71 ? THR B 76 ? SER B 71 THR B 76 AA4 6 LEU B 115 ? GLU B 118 ? LEU B 115 GLU B 118 AA4 7 VAL B 103 ? ALA B 106 ? VAL B 103 ALA B 106 AA5 1 ILE B 13 ? SER B 14 ? ILE B 13 SER B 14 AA5 2 ARG B 129 ? ILE B 130 ? ARG B 129 ILE B 130 AA6 1 TRP B 87 ? VAL B 89 ? TRP B 87 VAL B 89 AA6 2 MET B 95 ? ASN B 97 ? MET B 95 ASN B 97 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 CYS B 148 ? THR B 152 ? CYS B 148 THR B 152 AA8 2 ASN B 157 ? GLU B 161 ? ASN B 157 GLU B 161 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 VAL A 52 ? N VAL A 52 O LEU A 64 ? O LEU A 64 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 TYR B 37 ? O TYR B 37 N CYS B 20 ? N CYS B 20 AA4 1 2 N THR B 11 ? N THR B 11 O TRP B 47 ? O TRP B 47 AA4 2 3 N THR B 48 ? N THR B 48 O ARG B 56 ? O ARG B 56 AA4 3 4 N ILE B 55 ? N ILE B 55 O LEU B 62 ? O LEU B 62 AA4 4 5 N ALA B 63 ? N ALA B 63 O VAL B 74 ? O VAL B 74 AA4 5 6 N VAL B 73 ? N VAL B 73 O LEU B 115 ? O LEU B 115 AA4 6 7 O GLU B 118 ? O GLU B 118 N VAL B 103 ? N VAL B 103 AA5 1 2 N SER B 14 ? N SER B 14 O ARG B 129 ? O ARG B 129 AA6 1 2 N MET B 88 ? N MET B 88 O MET B 96 ? O MET B 96 AA7 1 2 O ARG B 204 ? O ARG B 204 N CYS B 189 ? N CYS B 189 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 ASP B 232 ? N ASP B 232 O VAL B 244 ? O VAL B 244 # 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 ? 5 'binding site for residue NAG A 301' AC2 Software A GOL 302 ? 7 'binding site for residue GOL A 302' AC3 Software B XYP 309 ? 2 'binding site for residue XYP B 309' AC4 Software B MAN 310 ? 3 'binding site for residue MAN B 310' AC5 Software B ASN 97 ? 9 'binding site for Poly-Saccharide residues NAG B 303 through NAG B 304 bound to ASN B 97' AC6 Software B ASN 114 ? 6 'binding site for Poly-Saccharide residues NAG B 305 through FUC B 306 bound to ASN B 114' AC7 Software B NGA 301 ? 15 'binding site for Poly-Saccharide residues NGA B 301 through GAL B 302' AC8 Software B NAG 307 ? 6 'binding site for Poly-Saccharide residues NAG B 307 through BMA B 308' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 GLN A 86 ? GLN A 86 . ? 1_555 ? 2 AC1 5 ASN A 108 ? ASN A 108 . ? 1_555 ? 3 AC1 5 HOH O . ? HOH A 439 . ? 1_555 ? 4 AC1 5 HOH O . ? HOH A 525 . ? 1_555 ? 5 AC1 5 HOH O . ? HOH A 533 . ? 1_555 ? 6 AC2 7 GLY A 72 ? GLY A 72 . ? 1_555 ? 7 AC2 7 ASN A 109 ? ASN A 109 . ? 1_555 ? 8 AC2 7 THR A 110 ? THR A 110 . ? 1_555 ? 9 AC2 7 PHE A 111 ? PHE A 111 . ? 1_555 ? 10 AC2 7 HOH O . ? HOH A 444 . ? 1_555 ? 11 AC2 7 HOH O . ? HOH A 464 . ? 1_555 ? 12 AC2 7 HOH O . ? HOH A 476 . ? 1_555 ? 13 AC3 2 NAG K . ? NAG B 307 . ? 1_555 ? 14 AC3 2 BMA L . ? BMA B 308 . ? 1_555 ? 15 AC4 3 SER A 123 ? SER A 123 . ? 3_556 ? 16 AC4 3 THR A 182 ? THR A 182 . ? 3_556 ? 17 AC4 3 BMA L . ? BMA B 308 . ? 1_555 ? 18 AC5 9 ALA B 63 ? ALA B 63 . ? 1_555 ? 19 AC5 9 THR B 64 ? THR B 64 . ? 1_555 ? 20 AC5 9 LEU B 67 ? LEU B 67 . ? 1_555 ? 21 AC5 9 TYR B 80 ? TYR B 80 . ? 1_555 ? 22 AC5 9 LEU B 81 ? LEU B 81 . ? 1_555 ? 23 AC5 9 ASP B 84 ? ASP B 84 . ? 1_555 ? 24 AC5 9 TRP B 87 ? TRP B 87 . ? 1_555 ? 25 AC5 9 ASN B 97 ? ASN B 97 . ? 1_555 ? 26 AC5 9 HOH P . ? HOH B 425 . ? 1_555 ? 27 AC6 6 TYR A 146 ? TYR A 146 . ? 3_556 ? 28 AC6 6 ARG B 33 ? ARG B 33 . ? 1_555 ? 29 AC6 6 ASN B 72 ? ASN B 72 . ? 1_555 ? 30 AC6 6 ASN B 114 ? ASN B 114 . ? 1_555 ? 31 AC6 6 NAG K . ? NAG B 307 . ? 1_555 ? 32 AC6 6 HOH P . ? HOH B 519 . ? 1_555 ? 33 AC7 15 GLN A 6 ? GLN A 6 . ? 3_556 ? 34 AC7 15 SER A 7 ? SER A 7 . ? 3_556 ? 35 AC7 15 GLY A 57 ? GLY A 57 . ? 3_556 ? 36 AC7 15 ASP A 58 ? ASP A 58 . ? 3_556 ? 37 AC7 15 MET A 130 ? MET A 130 . ? 3_556 ? 38 AC7 15 HOH O . ? HOH A 497 . ? 3_556 ? 39 AC7 15 ASP B 22 ? ASP B 22 . ? 1_555 ? 40 AC7 15 VAL B 23 ? VAL B 23 . ? 1_555 ? 41 AC7 15 TYR B 24 ? TYR B 24 . ? 1_555 ? 42 AC7 15 GLY B 25 ? GLY B 25 . ? 1_555 ? 43 AC7 15 GLN B 42 ? GLN B 42 . ? 1_555 ? 44 AC7 15 ASN B 44 ? ASN B 44 . ? 1_555 ? 45 AC7 15 ARG B 112 ? ARG B 112 . ? 1_555 ? 46 AC7 15 HOH P . ? HOH B 409 . ? 1_555 ? 47 AC7 15 HOH P . ? HOH B 422 . ? 1_555 ? 48 AC8 6 GLU A 124 ? GLU A 124 . ? 3_556 ? 49 AC8 6 HIS A 131 ? HIS A 131 . ? 3_556 ? 50 AC8 6 NAG I . ? NAG B 305 . ? 1_555 ? 51 AC8 6 FUC J . ? FUC B 306 . ? 1_555 ? 52 AC8 6 XYP M . ? XYP B 309 . ? 1_555 ? 53 AC8 6 MAN N . ? MAN B 310 . ? 1_555 ? # _atom_sites.entry_id 4ZGR _atom_sites.fract_transf_matrix[1][1] 0.006927 _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] 0.007364 _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] 0.022277 _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 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 ? 58.578 63.517 30.271 1.00 39.20 ? 1 ASN A N 1 ATOM 2 C CA . ASN A 1 1 ? 58.027 64.648 29.475 1.00 36.54 ? 1 ASN A CA 1 ATOM 3 C C . ASN A 1 1 ? 56.770 65.194 30.124 1.00 36.19 ? 1 ASN A C 1 ATOM 4 O O . ASN A 1 1 ? 55.972 64.453 30.731 1.00 36.63 ? 1 ASN A O 1 ATOM 5 C CB . ASN A 1 1 ? 57.677 64.211 28.048 1.00 36.42 ? 1 ASN A CB 1 ATOM 6 C CG . ASN A 1 1 ? 58.849 63.586 27.315 1.00 34.99 ? 1 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 1 ? 60.003 63.900 27.584 1.00 35.71 ? 1 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 1 ? 58.558 62.697 26.388 1.00 34.10 ? 1 ASN A ND2 1 ATOM 9 N N . LEU A 1 2 ? 56.579 66.493 29.973 1.00 33.86 ? 2 LEU A N 1 ATOM 10 C CA . LEU A 1 2 ? 55.294 67.095 30.275 1.00 34.36 ? 2 LEU A CA 1 ATOM 11 C C . LEU A 1 2 ? 54.212 66.275 29.546 1.00 32.42 ? 2 LEU A C 1 ATOM 12 O O . LEU A 1 2 ? 54.399 65.898 28.386 1.00 31.91 ? 2 LEU A O 1 ATOM 13 C CB . LEU A 1 2 ? 55.292 68.541 29.786 1.00 36.06 ? 2 LEU A CB 1 ATOM 14 C CG . LEU A 1 2 ? 54.153 69.460 30.203 1.00 39.33 ? 2 LEU A CG 1 ATOM 15 C CD1 . LEU A 1 2 ? 53.788 69.310 31.676 1.00 40.93 ? 2 LEU A CD1 1 ATOM 16 C CD2 . LEU A 1 2 ? 54.567 70.901 29.895 1.00 40.85 ? 2 LEU A CD2 1 ATOM 17 N N . SER A 1 3 ? 53.117 65.962 30.228 1.00 32.15 ? 3 SER A N 1 ATOM 18 C CA . SER A 1 3 ? 52.085 65.142 29.619 1.00 32.62 ? 3 SER A CA 1 ATOM 19 C C . SER A 1 3 ? 50.679 65.493 30.049 1.00 31.92 ? 3 SER A C 1 ATOM 20 O O . SER A 1 3 ? 50.443 66.044 31.121 1.00 30.52 ? 3 SER A O 1 ATOM 21 C CB . SER A 1 3 ? 52.362 63.647 29.840 1.00 35.79 ? 3 SER A CB 1 ATOM 22 O OG . SER A 1 3 ? 52.272 63.308 31.203 1.00 38.24 ? 3 SER A OG 1 ATOM 23 N N . LEU A 1 4 ? 49.755 65.190 29.146 1.00 30.47 ? 4 LEU A N 1 ATOM 24 C CA . LEU A 1 4 ? 48.333 65.348 29.371 1.00 30.97 ? 4 LEU A CA 1 ATOM 25 C C . LEU A 1 4 ? 47.707 64.064 28.869 1.00 32.74 ? 4 LEU A C 1 ATOM 26 O O . LEU A 1 4 ? 47.974 63.644 27.728 1.00 29.49 ? 4 LEU A O 1 ATOM 27 C CB . LEU A 1 4 ? 47.773 66.544 28.600 1.00 31.44 ? 4 LEU A CB 1 ATOM 28 C CG . LEU A 1 4 ? 46.283 66.870 28.770 1.00 32.59 ? 4 LEU A CG 1 ATOM 29 C CD1 . LEU A 1 4 ? 45.960 67.293 30.191 1.00 33.39 ? 4 LEU A CD1 1 ATOM 30 C CD2 . LEU A 1 4 ? 45.893 67.971 27.812 1.00 34.15 ? 4 LEU A CD2 1 ATOM 31 N N . SER A 1 5 ? 46.877 63.458 29.717 1.00 34.21 ? 5 SER A N 1 ATOM 32 C CA . SER A 1 5 ? 46.255 62.184 29.408 1.00 37.36 ? 5 SER A CA 1 ATOM 33 C C . SER A 1 5 ? 44.743 62.278 29.479 1.00 37.47 ? 5 SER A C 1 ATOM 34 O O . SER A 1 5 ? 44.172 62.921 30.372 1.00 35.85 ? 5 SER A O 1 ATOM 35 C CB . SER A 1 5 ? 46.753 61.092 30.354 1.00 38.91 ? 5 SER A CB 1 ATOM 36 O OG . SER A 1 5 ? 46.095 59.861 30.084 1.00 38.27 ? 5 SER A OG 1 ATOM 37 N N . GLN A 1 6 ? 44.099 61.606 28.533 1.00 38.97 ? 6 GLN A N 1 ATOM 38 C CA . GLN A 1 6 ? 42.643 61.484 28.505 1.00 40.98 ? 6 GLN A CA 1 ATOM 39 C C . GLN A 1 6 ? 42.056 61.002 29.834 1.00 39.98 ? 6 GLN A C 1 ATOM 40 O O . GLN A 1 6 ? 40.984 61.456 30.252 1.00 42.91 ? 6 GLN A O 1 ATOM 41 C CB . GLN A 1 6 ? 42.248 60.503 27.392 1.00 44.32 ? 6 GLN A CB 1 ATOM 42 C CG . GLN A 1 6 ? 40.766 60.167 27.314 1.00 46.11 ? 6 GLN A CG 1 ATOM 43 C CD . GLN A 1 6 ? 39.902 61.356 26.945 1.00 49.36 ? 6 GLN A CD 1 ATOM 44 O OE1 . GLN A 1 6 ? 40.394 62.403 26.518 1.00 47.06 ? 6 GLN A OE1 1 ATOM 45 N NE2 . GLN A 1 6 ? 38.592 61.186 27.092 1.00 56.59 ? 6 GLN A NE2 1 ATOM 46 N N . SER A 1 7 ? 42.763 60.080 30.486 1.00 38.91 ? 7 SER A N 1 ATOM 47 C CA . SER A 1 7 ? 42.329 59.515 31.760 1.00 40.25 ? 7 SER A CA 1 ATOM 48 C C . SER A 1 7 ? 42.275 60.506 32.929 1.00 41.54 ? 7 SER A C 1 ATOM 49 O O . SER A 1 7 ? 41.631 60.226 33.941 1.00 40.60 ? 7 SER A O 1 ATOM 50 C CB . SER A 1 7 ? 43.232 58.345 32.134 1.00 39.93 ? 7 SER A CB 1 ATOM 51 O OG . SER A 1 7 ? 44.545 58.795 32.369 1.00 44.22 ? 7 SER A OG 1 ATOM 52 N N . ASN A 1 8 ? 42.942 61.651 32.795 1.00 41.42 ? 8 ASN A N 1 ATOM 53 C CA . ASN A 1 8 ? 43.007 62.644 33.859 1.00 42.97 ? 8 ASN A CA 1 ATOM 54 C C . ASN A 1 8 ? 42.906 64.026 33.205 1.00 40.76 ? 8 ASN A C 1 ATOM 55 O O . ASN A 1 8 ? 43.847 64.823 33.258 1.00 42.36 ? 8 ASN A O 1 ATOM 56 C CB . ASN A 1 8 ? 44.325 62.443 34.626 1.00 43.94 ? 8 ASN A CB 1 ATOM 57 C CG . ASN A 1 8 ? 44.417 63.271 35.895 1.00 46.62 ? 8 ASN A CG 1 ATOM 58 O OD1 . ASN A 1 8 ? 43.404 63.645 36.497 1.00 46.97 ? 8 ASN A OD1 1 ATOM 59 N ND2 . ASN A 1 8 ? 45.651 63.562 36.315 1.00 48.43 ? 8 ASN A ND2 1 ATOM 60 N N . PHE A 1 9 ? 41.768 64.269 32.549 1.00 39.01 ? 9 PHE A N 1 ATOM 61 C CA . PHE A 1 9 ? 41.556 65.465 31.720 1.00 38.17 ? 9 PHE A CA 1 ATOM 62 C C . PHE A 1 9 ? 40.450 66.347 32.287 1.00 34.94 ? 9 PHE A C 1 ATOM 63 O O . PHE A 1 9 ? 39.382 66.478 31.720 1.00 38.74 ? 9 PHE A O 1 ATOM 64 C CB . PHE A 1 9 ? 41.248 65.078 30.258 1.00 39.78 ? 9 PHE A CB 1 ATOM 65 C CG . PHE A 1 9 ? 41.603 66.153 29.245 1.00 41.93 ? 9 PHE A CG 1 ATOM 66 C CD1 . PHE A 1 9 ? 41.209 67.486 29.412 1.00 44.74 ? 9 PHE A CD1 1 ATOM 67 C CD2 . PHE A 1 9 ? 42.340 65.839 28.117 1.00 42.70 ? 9 PHE A CD2 1 ATOM 68 C CE1 . PHE A 1 9 ? 41.536 68.459 28.474 1.00 44.33 ? 9 PHE A CE1 1 ATOM 69 C CE2 . PHE A 1 9 ? 42.660 66.816 27.180 1.00 42.91 ? 9 PHE A CE2 1 ATOM 70 C CZ . PHE A 1 9 ? 42.255 68.119 27.354 1.00 42.90 ? 9 PHE A CZ 1 ATOM 71 N N . SER A 1 10 ? 40.735 66.990 33.396 1.00 31.74 ? 10 SER A N 1 ATOM 72 C CA . SER A 1 10 ? 39.803 67.927 33.977 1.00 30.18 ? 10 SER A CA 1 ATOM 73 C C . SER A 1 10 ? 40.273 69.344 33.658 1.00 27.18 ? 10 SER A C 1 ATOM 74 O O . SER A 1 10 ? 41.383 69.555 33.166 1.00 24.91 ? 10 SER A O 1 ATOM 75 C CB . SER A 1 10 ? 39.748 67.729 35.483 1.00 29.24 ? 10 SER A CB 1 ATOM 76 O OG . SER A 1 10 ? 40.982 68.092 36.060 1.00 27.57 ? 10 SER A OG 1 ATOM 77 N N . ALA A 1 11 ? 39.414 70.290 33.976 1.00 26.00 ? 11 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? 39.724 71.697 33.880 1.00 26.67 ? 11 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? 41.007 72.021 34.648 1.00 27.36 ? 11 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? 41.862 72.748 34.149 1.00 23.58 ? 11 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? 38.571 72.519 34.419 1.00 27.13 ? 11 ALA A CB 1 ATOM 82 N N . ASP A 1 12 ? 41.129 71.457 35.858 1.00 26.38 ? 12 ASP A N 1 ATOM 83 C CA . ASP A 1 12 ? 42.286 71.682 36.706 1.00 26.77 ? 12 ASP A CA 1 ATOM 84 C C . ASP A 1 12 ? 43.532 71.082 36.076 1.00 25.28 ? 12 ASP A C 1 ATOM 85 O O . ASP A 1 12 ? 44.553 71.736 36.052 1.00 26.29 ? 12 ASP A O 1 ATOM 86 C CB . ASP A 1 12 ? 42.078 71.099 38.124 1.00 28.72 ? 12 ASP A CB 1 ATOM 87 C CG . ASP A 1 12 ? 41.160 71.949 39.009 1.00 31.32 ? 12 ASP A CG 1 ATOM 88 O OD1 . ASP A 1 12 ? 40.750 73.071 38.623 1.00 29.96 ? 12 ASP A OD1 1 ATOM 89 O OD2 . ASP A 1 12 ? 40.843 71.476 40.136 1.00 33.09 ? 12 ASP A OD2 1 ATOM 90 N N . THR A 1 13 ? 43.466 69.854 35.569 1.00 25.23 ? 13 THR A N 1 ATOM 91 C CA . THR A 1 13 ? 44.697 69.224 35.017 1.00 25.82 ? 13 THR A CA 1 ATOM 92 C C . THR A 1 13 ? 45.086 69.848 33.675 1.00 24.47 ? 13 THR A C 1 ATOM 93 O O . THR A 1 13 ? 46.269 70.036 33.397 1.00 23.71 ? 13 THR A O 1 ATOM 94 C CB . THR A 1 13 ? 44.615 67.703 34.866 1.00 27.31 ? 13 THR A CB 1 ATOM 95 O OG1 . THR A 1 13 ? 43.571 67.362 33.936 1.00 31.57 ? 13 THR A OG1 1 ATOM 96 C CG2 . THR A 1 13 ? 44.324 67.056 36.218 1.00 27.66 ? 13 THR A CG2 1 ATOM 97 N N . TYR A 1 14 ? 44.094 70.203 32.873 1.00 23.92 ? 14 TYR A N 1 ATOM 98 C CA . TYR A 1 14 ? 44.353 70.924 31.620 1.00 23.99 ? 14 TYR A CA 1 ATOM 99 C C . TYR A 1 14 ? 45.024 72.256 31.907 1.00 22.91 ? 14 TYR A C 1 ATOM 100 O O . TYR A 1 14 ? 46.057 72.564 31.310 1.00 23.65 ? 14 TYR A O 1 ATOM 101 C CB . TYR A 1 14 ? 43.070 71.133 30.807 1.00 23.20 ? 14 TYR A CB 1 ATOM 102 C CG . TYR A 1 14 ? 43.285 71.947 29.519 1.00 21.85 ? 14 TYR A CG 1 ATOM 103 C CD1 . TYR A 1 14 ? 43.902 71.381 28.402 1.00 22.32 ? 14 TYR A CD1 1 ATOM 104 C CD2 . TYR A 1 14 ? 42.860 73.270 29.430 1.00 21.90 ? 14 TYR A CD2 1 ATOM 105 C CE1 . TYR A 1 14 ? 44.091 72.109 27.232 1.00 21.56 ? 14 TYR A CE1 1 ATOM 106 C CE2 . TYR A 1 14 ? 43.044 74.014 28.271 1.00 22.01 ? 14 TYR A CE2 1 ATOM 107 C CZ . TYR A 1 14 ? 43.661 73.428 27.181 1.00 21.89 ? 14 TYR A CZ 1 ATOM 108 O OH . TYR A 1 14 ? 43.825 74.152 26.046 1.00 22.17 ? 14 TYR A OH 1 ATOM 109 N N . LYS A 1 15 ? 44.457 73.029 32.824 1.00 23.94 ? 15 LYS A N 1 ATOM 110 C CA . LYS A 1 15 ? 45.032 74.335 33.177 1.00 25.54 ? 15 LYS A CA 1 ATOM 111 C C . LYS A 1 15 ? 46.490 74.202 33.656 1.00 25.33 ? 15 LYS A C 1 ATOM 112 O O . LYS A 1 15 ? 47.337 74.966 33.243 1.00 23.27 ? 15 LYS A O 1 ATOM 113 C CB . LYS A 1 15 ? 44.159 75.076 34.205 1.00 27.85 ? 15 LYS A CB 1 ATOM 114 C CG . LYS A 1 15 ? 44.724 76.426 34.625 1.00 30.79 ? 15 LYS A CG 1 ATOM 115 C CD . LYS A 1 15 ? 43.824 77.219 35.569 1.00 32.46 ? 15 LYS A CD 1 ATOM 116 C CE . LYS A 1 15 ? 42.911 78.208 34.870 1.00 33.73 ? 15 LYS A CE 1 ATOM 117 N NZ . LYS A 1 15 ? 43.566 79.166 33.928 1.00 32.94 ? 15 LYS A NZ 1 ATOM 118 N N . SER A 1 16 ? 46.773 73.220 34.513 1.00 25.37 ? 16 SER A N 1 ATOM 119 C CA . SER A 1 16 ? 48.164 72.962 34.957 1.00 25.59 ? 16 SER A CA 1 ATOM 120 C C . SER A 1 16 ? 49.102 72.577 33.824 1.00 23.14 ? 16 SER A C 1 ATOM 121 O O . SER A 1 16 ? 50.233 73.031 33.764 1.00 23.38 ? 16 SER A O 1 ATOM 122 C CB . SER A 1 16 ? 48.209 71.863 36.033 1.00 27.34 ? 16 SER A CB 1 ATOM 123 O OG . SER A 1 16 ? 47.395 72.254 37.118 1.00 32.47 ? 16 SER A OG 1 ATOM 124 N N . PHE A 1 17 ? 48.637 71.730 32.926 1.00 22.91 ? 17 PHE A N 1 ATOM 125 C CA . PHE A 1 17 ? 49.429 71.355 31.770 1.00 23.21 ? 17 PHE A CA 1 ATOM 126 C C . PHE A 1 17 ? 49.807 72.582 30.894 1.00 22.53 ? 17 PHE A C 1 ATOM 127 O O . PHE A 1 17 ? 50.975 72.770 30.538 1.00 21.49 ? 17 PHE A O 1 ATOM 128 C CB . PHE A 1 17 ? 48.685 70.300 30.954 1.00 24.65 ? 17 PHE A CB 1 ATOM 129 C CG . PHE A 1 17 ? 49.310 70.020 29.620 1.00 25.46 ? 17 PHE A CG 1 ATOM 130 C CD1 . PHE A 1 17 ? 50.375 69.139 29.505 1.00 26.05 ? 17 PHE A CD1 1 ATOM 131 C CD2 . PHE A 1 17 ? 48.821 70.627 28.474 1.00 26.13 ? 17 PHE A CD2 1 ATOM 132 C CE1 . PHE A 1 17 ? 50.956 68.876 28.276 1.00 26.42 ? 17 PHE A CE1 1 ATOM 133 C CE2 . PHE A 1 17 ? 49.391 70.360 27.237 1.00 27.92 ? 17 PHE A CE2 1 ATOM 134 C CZ . PHE A 1 17 ? 50.466 69.490 27.136 1.00 28.16 ? 17 PHE A CZ 1 ATOM 135 N N . ILE A 1 18 ? 48.831 73.425 30.587 1.00 21.63 ? 18 ILE A N 1 ATOM 136 C CA . ILE A 1 18 ? 49.087 74.627 29.789 1.00 21.52 ? 18 ILE A CA 1 ATOM 137 C C . ILE A 1 18 ? 50.011 75.614 30.525 1.00 22.19 ? 18 ILE A C 1 ATOM 138 O O . ILE A 1 18 ? 50.917 76.175 29.931 1.00 21.28 ? 18 ILE A O 1 ATOM 139 C CB . ILE A 1 18 ? 47.767 75.314 29.375 1.00 21.88 ? 18 ILE A CB 1 ATOM 140 C CG1 . ILE A 1 18 ? 46.929 74.415 28.448 1.00 21.90 ? 18 ILE A CG1 1 ATOM 141 C CG2 . ILE A 1 18 ? 48.019 76.683 28.735 1.00 21.98 ? 18 ILE A CG2 1 ATOM 142 C CD1 . ILE A 1 18 ? 47.584 73.981 27.153 1.00 22.27 ? 18 ILE A CD1 1 ATOM 143 N N . LYS A 1 19 ? 49.777 75.806 31.815 1.00 24.14 ? 19 LYS A N 1 ATOM 144 C CA . LYS A 1 19 ? 50.652 76.639 32.654 1.00 26.67 ? 19 LYS A CA 1 ATOM 145 C C . LYS A 1 19 ? 52.111 76.127 32.610 1.00 25.35 ? 19 LYS A C 1 ATOM 146 O O . LYS A 1 19 ? 53.042 76.901 32.407 1.00 22.73 ? 19 LYS A O 1 ATOM 147 C CB . LYS A 1 19 ? 50.117 76.649 34.087 1.00 29.84 ? 19 LYS A CB 1 ATOM 148 C CG . LYS A 1 19 ? 50.849 77.564 35.067 1.00 35.42 ? 19 LYS A CG 1 ATOM 149 C CD . LYS A 1 19 ? 50.346 77.351 36.493 1.00 39.63 ? 19 LYS A CD 1 ATOM 150 C CE . LYS A 1 19 ? 51.399 77.775 37.509 1.00 45.53 ? 19 LYS A CE 1 ATOM 151 N NZ . LYS A 1 19 ? 50.910 77.575 38.899 1.00 48.82 ? 19 LYS A NZ 1 ATOM 152 N N . ASN A 1 20 ? 52.282 74.822 32.773 1.00 24.46 ? 20 ASN A N 1 ATOM 153 C CA . ASN A 1 20 ? 53.618 74.204 32.722 1.00 24.50 ? 20 ASN A CA 1 ATOM 154 C C . ASN A 1 20 ? 54.251 74.268 31.355 1.00 24.38 ? 20 ASN A C 1 ATOM 155 O O . ASN A 1 20 ? 55.446 74.518 31.238 1.00 22.93 ? 20 ASN A O 1 ATOM 156 C CB . ASN A 1 20 ? 53.576 72.756 33.224 1.00 27.20 ? 20 ASN A CB 1 ATOM 157 C CG . ASN A 1 20 ? 53.328 72.655 34.720 1.00 31.84 ? 20 ASN A CG 1 ATOM 158 O OD1 . ASN A 1 20 ? 53.820 73.480 35.493 1.00 39.90 ? 20 ASN A OD1 1 ATOM 159 N ND2 . ASN A 1 20 ? 52.553 71.665 35.145 1.00 31.22 ? 20 ASN A ND2 1 ATOM 160 N N . LEU A 1 21 ? 53.451 74.061 30.310 1.00 22.45 ? 21 LEU A N 1 ATOM 161 C CA . LEU A 1 21 ? 53.940 74.196 28.954 1.00 22.60 ? 21 LEU A CA 1 ATOM 162 C C . LEU A 1 21 ? 54.456 75.628 28.674 1.00 21.34 ? 21 LEU A C 1 ATOM 163 O O . LEU A 1 21 ? 55.523 75.805 28.108 1.00 19.90 ? 21 LEU A O 1 ATOM 164 C CB . LEU A 1 21 ? 52.844 73.785 27.956 1.00 23.45 ? 21 LEU A CB 1 ATOM 165 C CG . LEU A 1 21 ? 53.146 73.919 26.465 1.00 24.80 ? 21 LEU A CG 1 ATOM 166 C CD1 . LEU A 1 21 ? 54.443 73.214 26.080 1.00 25.87 ? 21 LEU A CD1 1 ATOM 167 C CD2 . LEU A 1 21 ? 51.987 73.331 25.673 1.00 24.32 ? 21 LEU A CD2 1 ATOM 168 N N . ARG A 1 22 ? 53.688 76.639 29.074 1.00 20.90 ? 22 ARG A N 1 ATOM 169 C CA . ARG A 1 22 ? 54.142 78.025 28.953 1.00 21.65 ? 22 ARG A CA 1 ATOM 170 C C . ARG A 1 22 ? 55.472 78.253 29.695 1.00 22.30 ? 22 ARG A C 1 ATOM 171 O O . ARG A 1 22 ? 56.370 78.887 29.165 1.00 21.58 ? 22 ARG A O 1 ATOM 172 C CB . ARG A 1 22 ? 53.108 78.989 29.502 1.00 21.99 ? 22 ARG A CB 1 ATOM 173 C CG . ARG A 1 22 ? 51.878 79.142 28.632 1.00 21.66 ? 22 ARG A CG 1 ATOM 174 C CD . ARG A 1 22 ? 50.855 80.007 29.342 1.00 21.68 ? 22 ARG A CD 1 ATOM 175 N NE . ARG A 1 22 ? 49.620 80.074 28.567 1.00 21.41 ? 22 ARG A NE 1 ATOM 176 C CZ . ARG A 1 22 ? 48.388 80.137 29.069 1.00 21.23 ? 22 ARG A CZ 1 ATOM 177 N NH1 . ARG A 1 22 ? 48.168 80.170 30.384 1.00 20.50 ? 22 ARG A NH1 1 ATOM 178 N NH2 . ARG A 1 22 ? 47.342 80.188 28.238 1.00 21.41 ? 22 ARG A NH2 1 ATOM 179 N N . LYS A 1 23 ? 55.560 77.738 30.918 1.00 22.56 ? 23 LYS A N 1 ATOM 180 C CA . LYS A 1 23 ? 56.770 77.887 31.721 1.00 26.74 ? 23 LYS A CA 1 ATOM 181 C C . LYS A 1 23 ? 57.959 77.276 31.021 1.00 25.30 ? 23 LYS A C 1 ATOM 182 O O . LYS A 1 23 ? 59.004 77.904 30.947 1.00 22.84 ? 23 LYS A O 1 ATOM 183 C CB . LYS A 1 23 ? 56.623 77.238 33.094 1.00 30.18 ? 23 LYS A CB 1 ATOM 184 C CG . LYS A 1 23 ? 55.819 78.059 34.070 1.00 35.33 ? 23 LYS A CG 1 ATOM 185 C CD . LYS A 1 23 ? 55.913 77.459 35.466 1.00 41.48 ? 23 LYS A CD 1 ATOM 186 C CE . LYS A 1 23 ? 54.985 78.184 36.424 1.00 47.32 ? 23 LYS A CE 1 ATOM 187 N NZ . LYS A 1 23 ? 55.265 77.766 37.829 1.00 50.09 ? 23 LYS A NZ 1 ATOM 188 N N . GLN A 1 24 ? 57.787 76.070 30.487 1.00 23.95 ? 24 GLN A N 1 ATOM 189 C CA . GLN A 1 24 ? 58.882 75.403 29.780 1.00 26.69 ? 24 GLN A CA 1 ATOM 190 C C . GLN A 1 24 ? 59.294 76.133 28.515 1.00 26.10 ? 24 GLN A C 1 ATOM 191 O O . GLN A 1 24 ? 60.478 76.261 28.228 1.00 25.02 ? 24 GLN A O 1 ATOM 192 C CB . GLN A 1 24 ? 58.513 73.954 29.446 1.00 29.50 ? 24 GLN A CB 1 ATOM 193 C CG . GLN A 1 24 ? 58.453 73.044 30.648 1.00 34.38 ? 24 GLN A CG 1 ATOM 194 C CD . GLN A 1 24 ? 59.810 72.936 31.317 1.00 40.58 ? 24 GLN A CD 1 ATOM 195 O OE1 . GLN A 1 24 ? 60.768 72.434 30.720 1.00 49.64 ? 24 GLN A OE1 1 ATOM 196 N NE2 . GLN A 1 24 ? 59.916 73.454 32.532 1.00 45.87 ? 24 GLN A NE2 1 ATOM 197 N N . LEU A 1 25 ? 58.316 76.620 27.752 1.00 24.17 ? 25 LEU A N 1 ATOM 198 C CA . LEU A 1 25 ? 58.623 77.373 26.536 1.00 23.51 ? 25 LEU A CA 1 ATOM 199 C C . LEU A 1 25 ? 59.327 78.698 26.790 1.00 22.70 ? 25 LEU A C 1 ATOM 200 O O . LEU A 1 25 ? 60.063 79.172 25.934 1.00 23.49 ? 25 LEU A O 1 ATOM 201 C CB . LEU A 1 25 ? 57.351 77.637 25.737 1.00 22.92 ? 25 LEU A CB 1 ATOM 202 C CG . LEU A 1 25 ? 56.805 76.421 24.994 1.00 23.91 ? 25 LEU A CG 1 ATOM 203 C CD1 . LEU A 1 25 ? 55.406 76.692 24.459 1.00 24.69 ? 25 LEU A CD1 1 ATOM 204 C CD2 . LEU A 1 25 ? 57.705 75.998 23.855 1.00 24.24 ? 25 LEU A CD2 1 ATOM 205 N N . THR A 1 26 ? 59.066 79.301 27.941 1.00 23.40 ? 26 THR A N 1 ATOM 206 C CA . THR A 1 26 ? 59.599 80.629 28.260 1.00 23.97 ? 26 THR A CA 1 ATOM 207 C C . THR A 1 26 ? 60.862 80.602 29.114 1.00 25.67 ? 26 THR A C 1 ATOM 208 O O . THR A 1 26 ? 61.350 81.657 29.514 1.00 25.39 ? 26 THR A O 1 ATOM 209 C CB . THR A 1 26 ? 58.524 81.534 28.899 1.00 24.25 ? 26 THR A CB 1 ATOM 210 O OG1 . THR A 1 26 ? 57.967 80.902 30.056 1.00 23.96 ? 26 THR A OG1 1 ATOM 211 C CG2 . THR A 1 26 ? 57.416 81.821 27.885 1.00 24.01 ? 26 THR A CG2 1 ATOM 212 N N . ILE A 1 27 ? 61.443 79.418 29.346 1.00 27.06 ? 27 ILE A N 1 ATOM 213 C CA . ILE A 1 27 ? 62.778 79.366 29.956 1.00 27.78 ? 27 ILE A CA 1 ATOM 214 C C . ILE A 1 27 ? 63.731 80.151 29.071 1.00 25.11 ? 27 ILE A C 1 ATOM 215 O O . ILE A 1 27 ? 63.768 79.934 27.875 1.00 25.23 ? 27 ILE A O 1 ATOM 216 C CB . ILE A 1 27 ? 63.310 77.926 30.135 1.00 30.31 ? 27 ILE A CB 1 ATOM 217 C CG1 . ILE A 1 27 ? 62.445 77.168 31.145 1.00 31.36 ? 27 ILE A CG1 1 ATOM 218 C CG2 . ILE A 1 27 ? 64.755 77.949 30.652 1.00 31.24 ? 27 ILE A CG2 1 ATOM 219 C CD1 . ILE A 1 27 ? 62.692 75.667 31.158 1.00 33.04 ? 27 ILE A CD1 1 ATOM 220 N N . GLY A 1 28 ? 64.489 81.073 29.667 1.00 25.17 ? 28 GLY A N 1 ATOM 221 C CA . GLY A 1 28 ? 65.409 81.927 28.913 1.00 24.72 ? 28 GLY A CA 1 ATOM 222 C C . GLY A 1 28 ? 64.759 82.959 27.990 1.00 25.79 ? 28 GLY A C 1 ATOM 223 O O . GLY A 1 28 ? 65.416 83.498 27.104 1.00 26.60 ? 28 GLY A O 1 ATOM 224 N N . ALA A 1 29 ? 63.467 83.237 28.171 1.00 25.55 ? 29 ALA A N 1 ATOM 225 C CA . ALA A 1 29 ? 62.789 84.239 27.344 1.00 25.74 ? 29 ALA A CA 1 ATOM 226 C C . ALA A 1 29 ? 63.352 85.626 27.614 1.00 25.14 ? 29 ALA A C 1 ATOM 227 O O . ALA A 1 29 ? 63.878 85.872 28.675 1.00 25.53 ? 29 ALA A O 1 ATOM 228 C CB . ALA A 1 29 ? 61.297 84.220 27.636 1.00 26.37 ? 29 ALA A CB 1 ATOM 229 N N . SER A 1 30 ? 63.226 86.535 26.661 1.00 25.34 ? 30 SER A N 1 ATOM 230 C CA . SER A 1 30 ? 63.499 87.956 26.924 1.00 26.82 ? 30 SER A CA 1 ATOM 231 C C . SER A 1 30 ? 62.178 88.715 27.194 1.00 27.97 ? 30 SER A C 1 ATOM 232 O O . SER A 1 30 ? 61.077 88.210 26.912 1.00 25.18 ? 30 SER A O 1 ATOM 233 C CB . SER A 1 30 ? 64.274 88.577 25.772 1.00 27.25 ? 30 SER A CB 1 ATOM 234 O OG . SER A 1 30 ? 63.553 88.498 24.552 1.00 28.59 ? 30 SER A OG 1 ATOM 235 N N . TYR A 1 31 ? 62.304 89.908 27.771 1.00 27.04 ? 31 TYR A N 1 ATOM 236 C CA . TYR A 1 31 ? 61.157 90.703 28.193 1.00 27.16 ? 31 TYR A CA 1 ATOM 237 C C . TYR A 1 31 ? 61.326 92.126 27.730 1.00 29.59 ? 31 TYR A C 1 ATOM 238 O O . TYR A 1 31 ? 62.438 92.675 27.777 1.00 28.56 ? 31 TYR A O 1 ATOM 239 C CB . TYR A 1 31 ? 60.998 90.699 29.705 1.00 27.96 ? 31 TYR A CB 1 ATOM 240 C CG . TYR A 1 31 ? 60.554 89.374 30.237 1.00 28.26 ? 31 TYR A CG 1 ATOM 241 C CD1 . TYR A 1 31 ? 61.484 88.359 30.449 1.00 28.16 ? 31 TYR A CD1 1 ATOM 242 C CD2 . TYR A 1 31 ? 59.210 89.104 30.501 1.00 28.21 ? 31 TYR A CD2 1 ATOM 243 C CE1 . TYR A 1 31 ? 61.103 87.123 30.905 1.00 27.83 ? 31 TYR A CE1 1 ATOM 244 C CE2 . TYR A 1 31 ? 58.823 87.856 30.986 1.00 28.54 ? 31 TYR A CE2 1 ATOM 245 C CZ . TYR A 1 31 ? 59.781 86.875 31.170 1.00 28.63 ? 31 TYR A CZ 1 ATOM 246 O OH . TYR A 1 31 ? 59.447 85.636 31.635 1.00 28.37 ? 31 TYR A OH 1 ATOM 247 N N . GLY A 1 32 ? 60.221 92.709 27.272 1.00 26.96 ? 32 GLY A N 1 ATOM 248 C CA . GLY A 1 32 ? 60.150 94.128 26.971 1.00 27.72 ? 32 GLY A CA 1 ATOM 249 C C . GLY A 1 32 ? 59.256 94.855 27.955 1.00 27.67 ? 32 GLY A C 1 ATOM 250 O O . GLY A 1 32 ? 58.856 94.305 28.979 1.00 27.13 ? 32 GLY A O 1 ATOM 251 N N . SER A 1 33 ? 58.938 96.102 27.613 1.00 29.23 ? 33 SER A N 1 ATOM 252 C CA . SER A 1 33 ? 58.039 96.974 28.392 1.00 29.16 ? 33 SER A CA 1 ATOM 253 C C . SER A 1 33 ? 56.701 96.355 28.693 1.00 28.00 ? 33 SER A C 1 ATOM 254 O O . SER A 1 33 ? 56.148 96.566 29.760 1.00 29.72 ? 33 SER A O 1 ATOM 255 C CB . SER A 1 33 ? 57.731 98.238 27.599 1.00 29.29 ? 33 SER A CB 1 ATOM 256 O OG . SER A 1 33 ? 58.885 99.007 27.519 1.00 31.85 ? 33 SER A OG 1 ATOM 257 N N . ALA A 1 34 ? 56.162 95.627 27.725 1.00 27.70 ? 34 ALA A N 1 ATOM 258 C CA . ALA A 1 34 ? 54.885 94.968 27.915 1.00 28.19 ? 34 ALA A CA 1 ATOM 259 C C . ALA A 1 34 ? 54.918 93.879 28.972 1.00 27.35 ? 34 ALA A C 1 ATOM 260 O O . ALA A 1 34 ? 53.883 93.550 29.510 1.00 28.28 ? 34 ALA A O 1 ATOM 261 C CB . ALA A 1 34 ? 54.360 94.424 26.597 1.00 29.26 ? 34 ALA A CB 1 ATOM 262 N N . GLY A 1 35 ? 56.086 93.312 29.266 1.00 25.50 ? 35 GLY A N 1 ATOM 263 C CA . GLY A 1 35 ? 56.185 92.251 30.262 1.00 25.01 ? 35 GLY A CA 1 ATOM 264 C C . GLY A 1 35 ? 55.681 90.898 29.756 1.00 24.92 ? 35 GLY A C 1 ATOM 265 O O . GLY A 1 35 ? 55.428 90.008 30.552 1.00 24.86 ? 35 GLY A O 1 ATOM 266 N N . ILE A 1 36 ? 55.539 90.741 28.438 1.00 24.29 ? 36 ILE A N 1 ATOM 267 C CA . ILE A 1 36 ? 55.097 89.475 27.851 1.00 24.61 ? 36 ILE A CA 1 ATOM 268 C C . ILE A 1 36 ? 56.346 88.756 27.355 1.00 23.73 ? 36 ILE A C 1 ATOM 269 O O . ILE A 1 36 ? 57.050 89.284 26.508 1.00 23.36 ? 36 ILE A O 1 ATOM 270 C CB . ILE A 1 36 ? 54.095 89.672 26.705 1.00 23.92 ? 36 ILE A CB 1 ATOM 271 C CG1 . ILE A 1 36 ? 52.811 90.321 27.261 1.00 23.63 ? 36 ILE A CG1 1 ATOM 272 C CG2 . ILE A 1 36 ? 53.768 88.340 26.024 1.00 24.01 ? 36 ILE A CG2 1 ATOM 273 C CD1 . ILE A 1 36 ? 51.837 90.759 26.199 1.00 23.14 ? 36 ILE A CD1 1 ATOM 274 N N . PRO A 1 37 ? 56.610 87.547 27.876 1.00 24.17 ? 37 PRO A N 1 ATOM 275 C CA . PRO A 1 37 ? 57.861 86.870 27.501 1.00 23.14 ? 37 PRO A CA 1 ATOM 276 C C . PRO A 1 37 ? 57.985 86.620 26.007 1.00 22.72 ? 37 PRO A C 1 ATOM 277 O O . PRO A 1 37 ? 57.000 86.277 25.347 1.00 21.76 ? 37 PRO A O 1 ATOM 278 C CB . PRO A 1 37 ? 57.818 85.550 28.289 1.00 23.61 ? 37 PRO A CB 1 ATOM 279 C CG . PRO A 1 37 ? 56.423 85.393 28.756 1.00 24.27 ? 37 PRO A CG 1 ATOM 280 C CD . PRO A 1 37 ? 55.812 86.758 28.841 1.00 23.99 ? 37 PRO A CD 1 ATOM 281 N N . ILE A 1 38 ? 59.189 86.827 25.481 1.00 22.10 ? 38 ILE A N 1 ATOM 282 C CA . ILE A 1 38 ? 59.492 86.655 24.073 1.00 21.99 ? 38 ILE A CA 1 ATOM 283 C C . ILE A 1 38 ? 60.331 85.360 23.963 1.00 23.17 ? 38 ILE A C 1 ATOM 284 O O . ILE A 1 38 ? 61.388 85.240 24.592 1.00 22.25 ? 38 ILE A O 1 ATOM 285 C CB . ILE A 1 38 ? 60.306 87.857 23.534 1.00 22.92 ? 38 ILE A CB 1 ATOM 286 C CG1 . ILE A 1 38 ? 59.521 89.179 23.680 1.00 24.11 ? 38 ILE A CG1 1 ATOM 287 C CG2 . ILE A 1 38 ? 60.721 87.642 22.090 1.00 22.92 ? 38 ILE A CG2 1 ATOM 288 C CD1 . ILE A 1 38 ? 60.407 90.408 23.639 1.00 25.72 ? 38 ILE A CD1 1 ATOM 289 N N . LEU A 1 39 ? 59.852 84.412 23.167 1.00 22.98 ? 39 LEU A N 1 ATOM 290 C CA . LEU A 1 39 ? 60.498 83.123 23.004 1.00 23.30 ? 39 LEU A CA 1 ATOM 291 C C . LEU A 1 39 ? 61.951 83.267 22.572 1.00 23.56 ? 39 LEU A C 1 ATOM 292 O O . LEU A 1 39 ? 62.335 84.246 21.927 1.00 22.40 ? 39 LEU A O 1 ATOM 293 C CB . LEU A 1 39 ? 59.762 82.280 21.964 1.00 23.15 ? 39 LEU A CB 1 ATOM 294 C CG . LEU A 1 39 ? 58.333 81.839 22.286 1.00 22.69 ? 39 LEU A CG 1 ATOM 295 C CD1 . LEU A 1 39 ? 57.772 81.107 21.087 1.00 22.69 ? 39 LEU A CD1 1 ATOM 296 C CD2 . LEU A 1 39 ? 58.254 81.001 23.560 1.00 23.09 ? 39 LEU A CD2 1 ATOM 297 N N . LYS A 1 40 ? 62.737 82.247 22.891 1.00 25.11 ? 40 LYS A N 1 ATOM 298 C CA . LYS A 1 40 ? 64.155 82.202 22.488 1.00 25.93 ? 40 LYS A CA 1 ATOM 299 C C . LYS A 1 40 ? 64.329 82.195 20.984 1.00 26.18 ? 40 LYS A C 1 ATOM 300 O O . LYS A 1 40 ? 63.450 81.781 20.232 1.00 25.53 ? 40 LYS A O 1 ATOM 301 C CB . LYS A 1 40 ? 64.846 80.979 23.105 1.00 25.38 ? 40 LYS A CB 1 ATOM 302 C CG . LYS A 1 40 ? 64.859 80.974 24.619 1.00 25.34 ? 40 LYS A CG 1 ATOM 303 C CD . LYS A 1 40 ? 65.656 79.798 25.199 1.00 26.56 ? 40 LYS A CD 1 ATOM 304 C CE . LYS A 1 40 ? 64.978 78.447 24.986 1.00 26.60 ? 40 LYS A CE 1 ATOM 305 N NZ . LYS A 1 40 ? 63.610 78.361 25.588 1.00 27.42 ? 40 LYS A NZ 1 ATOM 306 N N . HIS A 1 41 ? 65.474 82.691 20.536 1.00 27.54 ? 41 HIS A N 1 ATOM 307 C CA . HIS A 1 41 ? 65.806 82.693 19.127 1.00 27.26 ? 41 HIS A CA 1 ATOM 308 C C . HIS A 1 41 ? 67.247 82.200 18.931 1.00 26.27 ? 41 HIS A C 1 ATOM 309 O O . HIS A 1 41 ? 68.014 82.175 19.864 1.00 26.11 ? 41 HIS A O 1 ATOM 310 C CB . HIS A 1 41 ? 65.598 84.107 18.545 1.00 30.24 ? 41 HIS A CB 1 ATOM 311 C CG . HIS A 1 41 ? 66.552 85.133 19.073 1.00 31.11 ? 41 HIS A CG 1 ATOM 312 N ND1 . HIS A 1 41 ? 66.353 85.793 20.266 1.00 34.34 ? 41 HIS A ND1 1 ATOM 313 C CD2 . HIS A 1 41 ? 67.708 85.620 18.562 1.00 34.80 ? 41 HIS A CD2 1 ATOM 314 C CE1 . HIS A 1 41 ? 67.353 86.635 20.476 1.00 34.55 ? 41 HIS A CE1 1 ATOM 315 N NE2 . HIS A 1 41 ? 68.185 86.555 19.453 1.00 34.78 ? 41 HIS A NE2 1 ATOM 316 N N . SER A 1 42 ? 67.570 81.789 17.716 1.00 28.49 ? 42 SER A N 1 ATOM 317 C CA . SER A 1 42 ? 68.900 81.245 17.362 1.00 30.46 ? 42 SER A CA 1 ATOM 318 C C . SER A 1 42 ? 69.310 80.117 18.300 1.00 29.36 ? 42 SER A C 1 ATOM 319 O O . SER A 1 42 ? 70.405 80.125 18.854 1.00 30.92 ? 42 SER A O 1 ATOM 320 C CB . SER A 1 42 ? 69.953 82.362 17.377 1.00 31.63 ? 42 SER A CB 1 ATOM 321 O OG . SER A 1 42 ? 69.641 83.317 16.384 1.00 32.99 ? 42 SER A OG 1 ATOM 322 N N . VAL A 1 43 ? 68.391 79.187 18.536 1.00 28.25 ? 43 VAL A N 1 ATOM 323 C CA . VAL A 1 43 ? 68.616 78.132 19.509 1.00 27.28 ? 43 VAL A CA 1 ATOM 324 C C . VAL A 1 43 ? 69.329 77.004 18.753 1.00 25.31 ? 43 VAL A C 1 ATOM 325 O O . VAL A 1 43 ? 68.869 76.594 17.691 1.00 25.14 ? 43 VAL A O 1 ATOM 326 C CB . VAL A 1 43 ? 67.293 77.654 20.152 1.00 27.00 ? 43 VAL A CB 1 ATOM 327 C CG1 . VAL A 1 43 ? 67.519 76.472 21.084 1.00 25.67 ? 43 VAL A CG1 1 ATOM 328 C CG2 . VAL A 1 43 ? 66.640 78.808 20.920 1.00 26.76 ? 43 VAL A CG2 1 ATOM 329 N N . PRO A 1 44 ? 70.468 76.513 19.289 1.00 26.41 ? 44 PRO A N 1 ATOM 330 C CA . PRO A 1 44 ? 71.147 75.352 18.659 1.00 26.17 ? 44 PRO A CA 1 ATOM 331 C C . PRO A 1 44 ? 70.181 74.206 18.455 1.00 24.50 ? 44 PRO A C 1 ATOM 332 O O . PRO A 1 44 ? 69.343 73.961 19.318 1.00 26.15 ? 44 PRO A O 1 ATOM 333 C CB . PRO A 1 44 ? 72.204 74.971 19.705 1.00 26.22 ? 44 PRO A CB 1 ATOM 334 C CG . PRO A 1 44 ? 72.544 76.265 20.343 1.00 27.13 ? 44 PRO A CG 1 ATOM 335 C CD . PRO A 1 44 ? 71.202 76.975 20.476 1.00 26.52 ? 44 PRO A CD 1 ATOM 336 N N . ILE A 1 45 ? 70.270 73.540 17.314 1.00 25.02 ? 45 ILE A N 1 ATOM 337 C CA . ILE A 1 45 ? 69.309 72.517 16.941 1.00 25.12 ? 45 ILE A CA 1 ATOM 338 C C . ILE A 1 45 ? 69.120 71.450 18.012 1.00 27.23 ? 45 ILE A C 1 ATOM 339 O O . ILE A 1 45 ? 67.993 70.997 18.272 1.00 27.43 ? 45 ILE A O 1 ATOM 340 C CB . ILE A 1 45 ? 69.613 71.925 15.553 1.00 25.92 ? 45 ILE A CB 1 ATOM 341 C CG1 . ILE A 1 45 ? 68.459 71.042 15.079 1.00 26.19 ? 45 ILE A CG1 1 ATOM 342 C CG2 . ILE A 1 45 ? 70.897 71.085 15.562 1.00 26.71 ? 45 ILE A CG2 1 ATOM 343 C CD1 . ILE A 1 45 ? 67.164 71.767 14.818 1.00 26.38 ? 45 ILE A CD1 1 ATOM 344 N N . CYS A 1 46 ? 70.204 71.056 18.659 1.00 26.04 ? 46 CYS A N 1 ATOM 345 C CA . CYS A 1 46 ? 70.144 70.102 19.753 1.00 26.81 ? 46 CYS A CA 1 ATOM 346 C C . CYS A 1 46 ? 69.312 70.507 20.956 1.00 26.25 ? 46 CYS A C 1 ATOM 347 O O . CYS A 1 46 ? 68.966 69.674 21.762 1.00 23.79 ? 46 CYS A O 1 ATOM 348 C CB . CYS A 1 46 ? 71.574 69.768 20.226 1.00 27.91 ? 46 CYS A CB 1 ATOM 349 S SG . CYS A 1 46 ? 72.529 68.868 18.971 1.00 36.04 ? 46 CYS A SG 1 ATOM 350 N N . GLU A 1 47 ? 69.025 71.783 21.136 1.00 26.29 ? 47 GLU A N 1 ATOM 351 C CA . GLU A 1 47 ? 68.241 72.224 22.273 1.00 26.55 ? 47 GLU A CA 1 ATOM 352 C C . GLU A 1 47 ? 66.933 72.852 21.797 1.00 26.24 ? 47 GLU A C 1 ATOM 353 O O . GLU A 1 47 ? 66.285 73.538 22.552 1.00 25.29 ? 47 GLU A O 1 ATOM 354 C CB . GLU A 1 47 ? 69.028 73.308 23.026 1.00 29.80 ? 47 GLU A CB 1 ATOM 355 C CG . GLU A 1 47 ? 70.369 72.870 23.588 1.00 34.48 ? 47 GLU A CG 1 ATOM 356 C CD . GLU A 1 47 ? 71.298 74.049 23.882 1.00 40.30 ? 47 GLU A CD 1 ATOM 357 O OE1 . GLU A 1 47 ? 70.838 75.120 24.339 1.00 42.77 ? 47 GLU A OE1 1 ATOM 358 O OE2 . GLU A 1 47 ? 72.510 73.912 23.653 1.00 43.15 ? 47 GLU A OE2 1 ATOM 359 N N . ARG A 1 48 ? 66.561 72.664 20.551 1.00 25.24 ? 48 ARG A N 1 ATOM 360 C CA . ARG A 1 48 ? 65.476 73.452 20.003 1.00 25.02 ? 48 ARG A CA 1 ATOM 361 C C . ARG A 1 48 ? 64.099 72.826 20.225 1.00 25.33 ? 48 ARG A C 1 ATOM 362 O O . ARG A 1 48 ? 63.086 73.453 19.894 1.00 23.99 ? 48 ARG A O 1 ATOM 363 C CB . ARG A 1 48 ? 65.682 73.714 18.523 1.00 25.16 ? 48 ARG A CB 1 ATOM 364 C CG . ARG A 1 48 ? 64.914 74.960 18.074 1.00 26.04 ? 48 ARG A CG 1 ATOM 365 C CD . ARG A 1 48 ? 65.186 75.330 16.646 1.00 26.81 ? 48 ARG A CD 1 ATOM 366 N NE . ARG A 1 48 ? 66.612 75.537 16.399 1.00 27.06 ? 48 ARG A NE 1 ATOM 367 C CZ . ARG A 1 48 ? 67.169 75.516 15.191 1.00 28.00 ? 48 ARG A CZ 1 ATOM 368 N NH1 . ARG A 1 48 ? 66.428 75.340 14.111 1.00 27.55 ? 48 ARG A NH1 1 ATOM 369 N NH2 . ARG A 1 48 ? 68.488 75.672 15.069 1.00 28.64 ? 48 ARG A NH2 1 ATOM 370 N N . PHE A 1 49 ? 64.042 71.616 20.782 1.00 24.88 ? 49 PHE A N 1 ATOM 371 C CA . PHE A 1 49 ? 62.766 70.881 20.843 1.00 25.45 ? 49 PHE A CA 1 ATOM 372 C C . PHE A 1 49 ? 62.374 70.531 22.258 1.00 27.01 ? 49 PHE A C 1 ATOM 373 O O . PHE A 1 49 ? 63.196 70.063 23.042 1.00 28.38 ? 49 PHE A O 1 ATOM 374 C CB . PHE A 1 49 ? 62.818 69.647 19.944 1.00 24.79 ? 49 PHE A CB 1 ATOM 375 C CG . PHE A 1 49 ? 63.131 69.983 18.526 1.00 25.02 ? 49 PHE A CG 1 ATOM 376 C CD1 . PHE A 1 49 ? 62.178 70.594 17.715 1.00 24.89 ? 49 PHE A CD1 1 ATOM 377 C CD2 . PHE A 1 49 ? 64.406 69.773 18.018 1.00 24.79 ? 49 PHE A CD2 1 ATOM 378 C CE1 . PHE A 1 49 ? 62.484 70.946 16.412 1.00 25.21 ? 49 PHE A CE1 1 ATOM 379 C CE2 . PHE A 1 49 ? 64.716 70.112 16.722 1.00 25.40 ? 49 PHE A CE2 1 ATOM 380 C CZ . PHE A 1 49 ? 63.756 70.701 15.913 1.00 26.09 ? 49 PHE A CZ 1 ATOM 381 N N . LEU A 1 50 ? 61.112 70.800 22.580 1.00 25.62 ? 50 LEU A N 1 ATOM 382 C CA . LEU A 1 50 ? 60.505 70.431 23.828 1.00 26.28 ? 50 LEU A CA 1 ATOM 383 C C . LEU A 1 50 ? 59.533 69.293 23.509 1.00 26.57 ? 50 LEU A C 1 ATOM 384 O O . LEU A 1 50 ? 58.664 69.451 22.640 1.00 25.20 ? 50 LEU A O 1 ATOM 385 C CB . LEU A 1 50 ? 59.741 71.619 24.414 1.00 27.51 ? 50 LEU A CB 1 ATOM 386 C CG . LEU A 1 50 ? 58.925 71.397 25.683 1.00 30.01 ? 50 LEU A CG 1 ATOM 387 C CD1 . LEU A 1 50 ? 59.800 70.967 26.860 1.00 30.55 ? 50 LEU A CD1 1 ATOM 388 C CD2 . LEU A 1 50 ? 58.197 72.689 26.004 1.00 32.05 ? 50 LEU A CD2 1 ATOM 389 N N . LEU A 1 51 ? 59.669 68.172 24.214 1.00 25.09 ? 51 LEU A N 1 ATOM 390 C CA . LEU A 1 51 ? 58.838 67.005 23.969 1.00 26.47 ? 51 LEU A CA 1 ATOM 391 C C . LEU A 1 51 ? 57.679 66.964 24.927 1.00 27.53 ? 51 LEU A C 1 ATOM 392 O O . LEU A 1 51 ? 57.849 67.191 26.125 1.00 26.15 ? 51 LEU A O 1 ATOM 393 C CB . LEU A 1 51 ? 59.641 65.721 24.121 1.00 27.38 ? 51 LEU A CB 1 ATOM 394 C CG . LEU A 1 51 ? 60.876 65.613 23.244 1.00 27.87 ? 51 LEU A CG 1 ATOM 395 C CD1 . LEU A 1 51 ? 61.521 64.246 23.452 1.00 30.59 ? 51 LEU A CD1 1 ATOM 396 C CD2 . LEU A 1 51 ? 60.589 65.822 21.779 1.00 27.67 ? 51 LEU A CD2 1 ATOM 397 N N . VAL A 1 52 ? 56.504 66.654 24.390 1.00 26.75 ? 52 VAL A N 1 ATOM 398 C CA . VAL A 1 52 ? 55.289 66.590 25.157 1.00 27.09 ? 52 VAL A CA 1 ATOM 399 C C . VAL A 1 52 ? 54.554 65.275 24.825 1.00 26.32 ? 52 VAL A C 1 ATOM 400 O O . VAL A 1 52 ? 54.405 64.932 23.672 1.00 24.21 ? 52 VAL A O 1 ATOM 401 C CB . VAL A 1 52 ? 54.414 67.832 24.849 1.00 30.23 ? 52 VAL A CB 1 ATOM 402 C CG1 . VAL A 1 52 ? 53.028 67.670 25.410 1.00 33.13 ? 52 VAL A CG1 1 ATOM 403 C CG2 . VAL A 1 52 ? 55.029 69.099 25.441 1.00 31.70 ? 52 VAL A CG2 1 ATOM 404 N N . ASP A 1 53 ? 54.082 64.568 25.856 1.00 27.01 ? 53 ASP A N 1 ATOM 405 C CA . ASP A 1 53 ? 53.340 63.299 25.691 1.00 27.80 ? 53 ASP A CA 1 ATOM 406 C C . ASP A 1 53 ? 51.842 63.507 25.850 1.00 26.19 ? 53 ASP A C 1 ATOM 407 O O . ASP A 1 53 ? 51.379 64.096 26.823 1.00 25.98 ? 53 ASP A O 1 ATOM 408 C CB . ASP A 1 53 ? 53.772 62.235 26.717 1.00 28.23 ? 53 ASP A CB 1 ATOM 409 C CG . ASP A 1 53 ? 55.179 61.726 26.499 1.00 29.59 ? 53 ASP A CG 1 ATOM 410 O OD1 . ASP A 1 53 ? 55.842 62.035 25.496 1.00 29.74 ? 53 ASP A OD1 1 ATOM 411 O OD2 . ASP A 1 53 ? 55.659 61.003 27.385 1.00 33.02 ? 53 ASP A OD2 1 ATOM 412 N N . LEU A 1 54 ? 51.090 63.013 24.881 1.00 25.07 ? 54 LEU A N 1 ATOM 413 C CA . LEU A 1 54 ? 49.648 63.016 24.943 1.00 25.51 ? 54 LEU A CA 1 ATOM 414 C C . LEU A 1 54 ? 49.186 61.556 24.887 1.00 25.80 ? 54 LEU A C 1 ATOM 415 O O . LEU A 1 54 ? 49.648 60.794 24.026 1.00 23.75 ? 54 LEU A O 1 ATOM 416 C CB . LEU A 1 54 ? 49.057 63.807 23.778 1.00 25.92 ? 54 LEU A CB 1 ATOM 417 C CG . LEU A 1 54 ? 49.501 65.274 23.651 1.00 26.43 ? 54 LEU A CG 1 ATOM 418 C CD1 . LEU A 1 54 ? 48.838 65.893 22.433 1.00 27.35 ? 54 LEU A CD1 1 ATOM 419 C CD2 . LEU A 1 54 ? 49.181 66.089 24.889 1.00 26.52 ? 54 LEU A CD2 1 ATOM 420 N N . THR A 1 55 ? 48.294 61.193 25.807 1.00 26.36 ? 55 THR A N 1 ATOM 421 C CA . THR A 1 55 ? 47.776 59.825 25.925 1.00 27.53 ? 55 THR A CA 1 ATOM 422 C C . THR A 1 55 ? 46.263 59.839 25.752 1.00 27.02 ? 55 THR A C 1 ATOM 423 O O . THR A 1 55 ? 45.578 60.666 26.341 1.00 26.38 ? 55 THR A O 1 ATOM 424 C CB . THR A 1 55 ? 48.162 59.218 27.278 1.00 28.46 ? 55 THR A CB 1 ATOM 425 O OG1 . THR A 1 55 ? 49.582 59.180 27.345 1.00 27.61 ? 55 THR A OG1 1 ATOM 426 C CG2 . THR A 1 55 ? 47.624 57.765 27.426 1.00 28.00 ? 55 THR A CG2 1 ATOM 427 N N . ASN A 1 56 ? 45.760 58.944 24.905 1.00 27.90 ? 56 ASN A N 1 ATOM 428 C CA . ASN A 1 56 ? 44.333 58.910 24.555 1.00 28.70 ? 56 ASN A CA 1 ATOM 429 C C . ASN A 1 56 ? 43.612 57.869 25.415 1.00 29.62 ? 56 ASN A C 1 ATOM 430 O O . ASN A 1 56 ? 44.186 57.342 26.362 1.00 28.17 ? 56 ASN A O 1 ATOM 431 C CB . ASN A 1 56 ? 44.146 58.642 23.051 1.00 29.64 ? 56 ASN A CB 1 ATOM 432 C CG . ASN A 1 56 ? 44.578 57.247 22.637 1.00 32.13 ? 56 ASN A CG 1 ATOM 433 O OD1 . ASN A 1 56 ? 44.684 56.316 23.476 1.00 31.71 ? 56 ASN A OD1 1 ATOM 434 N ND2 . ASN A 1 56 ? 44.871 57.088 21.344 1.00 31.75 ? 56 ASN A ND2 1 ATOM 435 N N . GLY A 1 57 ? 42.368 57.578 25.049 1.00 30.17 ? 57 GLY A N 1 ATOM 436 C CA . GLY A 1 57 ? 41.489 56.720 25.818 1.00 30.81 ? 57 GLY A CA 1 ATOM 437 C C . GLY A 1 57 ? 41.726 55.241 25.578 1.00 32.10 ? 57 GLY A C 1 ATOM 438 O O . GLY A 1 57 ? 41.117 54.406 26.252 1.00 33.59 ? 57 GLY A O 1 ATOM 439 N N . ASP A 1 58 ? 42.572 54.910 24.604 1.00 31.66 ? 58 ASP A N 1 ATOM 440 C CA . ASP A 1 58 ? 43.102 53.559 24.447 1.00 32.64 ? 58 ASP A CA 1 ATOM 441 C C . ASP A 1 58 ? 44.402 53.361 25.233 1.00 32.06 ? 58 ASP A C 1 ATOM 442 O O . ASP A 1 58 ? 45.087 52.369 25.031 1.00 30.26 ? 58 ASP A O 1 ATOM 443 C CB . ASP A 1 58 ? 43.397 53.241 22.972 1.00 32.17 ? 58 ASP A CB 1 ATOM 444 C CG . ASP A 1 58 ? 42.194 53.455 22.037 1.00 32.68 ? 58 ASP A CG 1 ATOM 445 O OD1 . ASP A 1 58 ? 41.028 53.459 22.478 1.00 32.00 ? 58 ASP A OD1 1 ATOM 446 O OD2 . ASP A 1 58 ? 42.450 53.635 20.830 1.00 32.20 ? 58 ASP A OD2 1 ATOM 447 N N . ASN A 1 59 ? 44.759 54.301 26.108 1.00 34.12 ? 59 ASN A N 1 ATOM 448 C CA . ASN A 1 59 ? 46.081 54.326 26.733 1.00 34.33 ? 59 ASN A CA 1 ATOM 449 C C . ASN A 1 59 ? 47.275 54.250 25.772 1.00 32.85 ? 59 ASN A C 1 ATOM 450 O O . ASN A 1 59 ? 48.304 53.677 26.106 1.00 34.13 ? 59 ASN A O 1 ATOM 451 C CB . ASN A 1 59 ? 46.192 53.210 27.788 1.00 37.59 ? 59 ASN A CB 1 ATOM 452 C CG . ASN A 1 59 ? 47.245 53.515 28.838 1.00 41.10 ? 59 ASN A CG 1 ATOM 453 O OD1 . ASN A 1 59 ? 47.360 54.656 29.288 1.00 40.80 ? 59 ASN A OD1 1 ATOM 454 N ND2 . ASN A 1 59 ? 48.026 52.508 29.225 1.00 45.45 ? 59 ASN A ND2 1 ATOM 455 N N . GLU A 1 60 ? 47.127 54.790 24.567 1.00 32.62 ? 60 GLU A N 1 ATOM 456 C CA . GLU A 1 60 ? 48.237 54.863 23.625 1.00 33.07 ? 60 GLU A CA 1 ATOM 457 C C . GLU A 1 60 ? 48.719 56.303 23.640 1.00 29.57 ? 60 GLU A C 1 ATOM 458 O O . GLU A 1 60 ? 47.910 57.230 23.777 1.00 26.36 ? 60 GLU A O 1 ATOM 459 C CB . GLU A 1 60 ? 47.816 54.431 22.219 1.00 37.11 ? 60 GLU A CB 1 ATOM 460 C CG . GLU A 1 60 ? 47.340 52.977 22.110 1.00 42.26 ? 60 GLU A CG 1 ATOM 461 C CD . GLU A 1 60 ? 48.460 51.928 22.158 1.00 48.57 ? 60 GLU A CD 1 ATOM 462 O OE1 . GLU A 1 60 ? 49.591 52.224 22.634 1.00 52.74 ? 60 GLU A OE1 1 ATOM 463 O OE2 . GLU A 1 60 ? 48.203 50.777 21.713 1.00 49.86 ? 60 GLU A OE2 1 ATOM 464 N N . THR A 1 61 ? 50.027 56.470 23.504 1.00 28.69 ? 61 THR A N 1 ATOM 465 C CA . THR A 1 61 ? 50.700 57.755 23.729 1.00 28.38 ? 61 THR A CA 1 ATOM 466 C C . THR A 1 61 ? 51.450 58.157 22.471 1.00 27.09 ? 61 THR A C 1 ATOM 467 O O . THR A 1 61 ? 52.024 57.310 21.790 1.00 25.30 ? 61 THR A O 1 ATOM 468 C CB . THR A 1 61 ? 51.669 57.640 24.926 1.00 28.54 ? 61 THR A CB 1 ATOM 469 O OG1 . THR A 1 61 ? 50.910 57.363 26.100 1.00 29.47 ? 61 THR A OG1 1 ATOM 470 C CG2 . THR A 1 61 ? 52.476 58.943 25.177 1.00 29.58 ? 61 THR A CG2 1 ATOM 471 N N . ILE A 1 62 ? 51.383 59.448 22.140 1.00 25.39 ? 62 ILE A N 1 ATOM 472 C CA . ILE A 1 62 ? 52.260 60.042 21.135 1.00 23.69 ? 62 ILE A CA 1 ATOM 473 C C . ILE A 1 62 ? 53.139 61.079 21.824 1.00 23.31 ? 62 ILE A C 1 ATOM 474 O O . ILE A 1 62 ? 52.728 61.666 22.814 1.00 24.46 ? 62 ILE A O 1 ATOM 475 C CB . ILE A 1 62 ? 51.514 60.687 19.956 1.00 23.03 ? 62 ILE A CB 1 ATOM 476 C CG1 . ILE A 1 62 ? 50.565 61.819 20.420 1.00 23.09 ? 62 ILE A CG1 1 ATOM 477 C CG2 . ILE A 1 62 ? 50.797 59.609 19.156 1.00 22.71 ? 62 ILE A CG2 1 ATOM 478 C CD1 . ILE A 1 62 ? 49.937 62.580 19.282 1.00 22.93 ? 62 ILE A CD1 1 ATOM 479 N N . THR A 1 63 ? 54.345 61.265 21.303 1.00 23.62 ? 63 THR A N 1 ATOM 480 C CA . THR A 1 63 ? 55.249 62.307 21.772 1.00 23.59 ? 63 THR A CA 1 ATOM 481 C C . THR A 1 63 ? 55.412 63.327 20.676 1.00 23.25 ? 63 THR A C 1 ATOM 482 O O . THR A 1 63 ? 55.895 62.990 19.598 1.00 24.05 ? 63 THR A O 1 ATOM 483 C CB . THR A 1 63 ? 56.624 61.726 22.148 1.00 24.35 ? 63 THR A CB 1 ATOM 484 O OG1 . THR A 1 63 ? 56.444 60.812 23.237 1.00 25.47 ? 63 THR A OG1 1 ATOM 485 C CG2 . THR A 1 63 ? 57.557 62.843 22.623 1.00 24.74 ? 63 THR A CG2 1 ATOM 486 N N . LEU A 1 64 ? 55.018 64.571 20.949 1.00 23.06 ? 64 LEU A N 1 ATOM 487 C CA . LEU A 1 64 ? 55.182 65.663 19.987 1.00 24.20 ? 64 LEU A CA 1 ATOM 488 C C . LEU A 1 64 ? 56.402 66.513 20.307 1.00 23.60 ? 64 LEU A C 1 ATOM 489 O O . LEU A 1 64 ? 56.666 66.823 21.471 1.00 23.40 ? 64 LEU A O 1 ATOM 490 C CB . LEU A 1 64 ? 53.950 66.557 19.978 1.00 25.79 ? 64 LEU A CB 1 ATOM 491 C CG . LEU A 1 64 ? 52.697 65.831 19.453 1.00 26.85 ? 64 LEU A CG 1 ATOM 492 C CD1 . LEU A 1 64 ? 51.587 65.895 20.477 1.00 28.50 ? 64 LEU A CD1 1 ATOM 493 C CD2 . LEU A 1 64 ? 52.270 66.388 18.098 1.00 27.36 ? 64 LEU A CD2 1 ATOM 494 N N . ALA A 1 65 ? 57.109 66.903 19.254 1.00 22.92 ? 65 ALA A N 1 ATOM 495 C CA . ALA A 1 65 ? 58.274 67.780 19.354 1.00 23.30 ? 65 ALA A CA 1 ATOM 496 C C . ALA A 1 65 ? 57.851 69.202 18.986 1.00 22.04 ? 65 ALA A C 1 ATOM 497 O O . ALA A 1 65 ? 57.417 69.455 17.864 1.00 22.17 ? 65 ALA A O 1 ATOM 498 C CB . ALA A 1 65 ? 59.377 67.285 18.439 1.00 23.52 ? 65 ALA A CB 1 ATOM 499 N N . ILE A 1 66 ? 57.945 70.097 19.963 1.00 21.85 ? 66 ILE A N 1 ATOM 500 C CA . ILE A 1 66 ? 57.582 71.491 19.806 1.00 21.79 ? 66 ILE A CA 1 ATOM 501 C C . ILE A 1 66 ? 58.867 72.274 19.612 1.00 21.70 ? 66 ILE A C 1 ATOM 502 O O . ILE A 1 66 ? 59.771 72.153 20.404 1.00 21.67 ? 66 ILE A O 1 ATOM 503 C CB . ILE A 1 66 ? 56.846 72.014 21.048 1.00 22.05 ? 66 ILE A CB 1 ATOM 504 C CG1 . ILE A 1 66 ? 55.533 71.240 21.269 1.00 22.80 ? 66 ILE A CG1 1 ATOM 505 C CG2 . ILE A 1 66 ? 56.517 73.495 20.918 1.00 22.35 ? 66 ILE A CG2 1 ATOM 506 C CD1 . ILE A 1 66 ? 55.008 71.350 22.684 1.00 23.47 ? 66 ILE A CD1 1 ATOM 507 N N . ASN A 1 67 ? 58.927 73.075 18.557 1.00 21.58 ? 67 ASN A N 1 ATOM 508 C CA . ASN A 1 67 ? 60.031 73.995 18.345 1.00 22.82 ? 67 ASN A CA 1 ATOM 509 C C . ASN A 1 67 ? 59.911 75.146 19.340 1.00 23.05 ? 67 ASN A C 1 ATOM 510 O O . ASN A 1 67 ? 58.933 75.912 19.306 1.00 22.31 ? 67 ASN A O 1 ATOM 511 C CB . ASN A 1 67 ? 59.967 74.507 16.913 1.00 23.57 ? 67 ASN A CB 1 ATOM 512 C CG . ASN A 1 67 ? 61.155 75.352 16.523 1.00 23.48 ? 67 ASN A CG 1 ATOM 513 O OD1 . ASN A 1 67 ? 61.764 76.047 17.340 1.00 24.68 ? 67 ASN A OD1 1 ATOM 514 N ND2 . ASN A 1 67 ? 61.483 75.306 15.249 1.00 24.27 ? 67 ASN A ND2 1 ATOM 515 N N . VAL A 1 68 ? 60.893 75.274 20.217 1.00 22.84 ? 68 VAL A N 1 ATOM 516 C CA . VAL A 1 68 ? 60.834 76.283 21.265 1.00 23.51 ? 68 VAL A CA 1 ATOM 517 C C . VAL A 1 68 ? 60.962 77.711 20.739 1.00 23.24 ? 68 VAL A C 1 ATOM 518 O O . VAL A 1 68 ? 60.700 78.635 21.492 1.00 24.03 ? 68 VAL A O 1 ATOM 519 C CB . VAL A 1 68 ? 61.888 76.070 22.380 1.00 24.38 ? 68 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 68 ? 61.770 74.667 22.977 1.00 25.02 ? 68 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 68 ? 63.305 76.340 21.866 1.00 24.31 ? 68 VAL A CG2 1 ATOM 522 N N . GLU A 1 69 ? 61.383 77.888 19.488 1.00 24.02 ? 69 GLU A N 1 ATOM 523 C CA . GLU A 1 69 ? 61.489 79.235 18.887 1.00 25.66 ? 69 GLU A CA 1 ATOM 524 C C . GLU A 1 69 ? 60.149 79.799 18.433 1.00 26.31 ? 69 GLU A C 1 ATOM 525 O O . GLU A 1 69 ? 59.972 81.015 18.431 1.00 24.91 ? 69 GLU A O 1 ATOM 526 C CB . GLU A 1 69 ? 62.430 79.261 17.692 1.00 26.21 ? 69 GLU A CB 1 ATOM 527 C CG . GLU A 1 69 ? 63.867 78.913 18.045 1.00 29.03 ? 69 GLU A CG 1 ATOM 528 C CD . GLU A 1 69 ? 64.829 78.972 16.866 1.00 30.10 ? 69 GLU A CD 1 ATOM 529 O OE1 . GLU A 1 69 ? 64.400 79.054 15.696 1.00 32.91 ? 69 GLU A OE1 1 ATOM 530 O OE2 . GLU A 1 69 ? 66.039 78.910 17.122 1.00 33.64 ? 69 GLU A OE2 1 ATOM 531 N N . ASP A 1 70 ? 59.244 78.932 17.984 1.00 24.87 ? 70 ASP A N 1 ATOM 532 C CA . ASP A 1 70 ? 57.942 79.394 17.486 1.00 25.79 ? 70 ASP A CA 1 ATOM 533 C C . ASP A 1 70 ? 56.710 78.674 18.046 1.00 25.14 ? 70 ASP A C 1 ATOM 534 O O . ASP A 1 70 ? 55.614 78.961 17.612 1.00 24.46 ? 70 ASP A O 1 ATOM 535 C CB . ASP A 1 70 ? 57.929 79.397 15.949 1.00 26.47 ? 70 ASP A CB 1 ATOM 536 C CG . ASP A 1 70 ? 58.063 78.009 15.339 1.00 27.10 ? 70 ASP A CG 1 ATOM 537 O OD1 . ASP A 1 70 ? 57.905 76.991 16.030 1.00 27.28 ? 70 ASP A OD1 1 ATOM 538 O OD2 . ASP A 1 70 ? 58.284 77.949 14.130 1.00 30.32 ? 70 ASP A OD2 1 ATOM 539 N N . ALA A 1 71 ? 56.889 77.774 19.018 1.00 23.27 ? 71 ALA A N 1 ATOM 540 C CA . ALA A 1 71 ? 55.780 77.056 19.627 1.00 23.94 ? 71 ALA A CA 1 ATOM 541 C C . ALA A 1 71 ? 54.888 76.358 18.570 1.00 24.28 ? 71 ALA A C 1 ATOM 542 O O . ALA A 1 71 ? 53.653 76.404 18.644 1.00 26.61 ? 71 ALA A O 1 ATOM 543 C CB . ALA A 1 71 ? 54.956 78.002 20.521 1.00 24.84 ? 71 ALA A CB 1 ATOM 544 N N . GLY A 1 72 ? 55.525 75.761 17.568 1.00 23.96 ? 72 GLY A N 1 ATOM 545 C CA . GLY A 1 72 ? 54.853 74.940 16.556 1.00 24.88 ? 72 GLY A CA 1 ATOM 546 C C . GLY A 1 72 ? 55.372 73.513 16.615 1.00 24.89 ? 72 GLY A C 1 ATOM 547 O O . GLY A 1 72 ? 56.499 73.275 17.060 1.00 23.43 ? 72 GLY A O 1 ATOM 548 N N . PHE A 1 73 ? 54.556 72.566 16.164 1.00 24.49 ? 73 PHE A N 1 ATOM 549 C CA . PHE A 1 73 ? 54.976 71.177 16.097 1.00 25.34 ? 73 PHE A CA 1 ATOM 550 C C . PHE A 1 73 ? 55.915 70.993 14.924 1.00 25.46 ? 73 PHE A C 1 ATOM 551 O O . PHE A 1 73 ? 55.631 71.434 13.802 1.00 25.45 ? 73 PHE A O 1 ATOM 552 C CB . PHE A 1 73 ? 53.781 70.225 15.945 1.00 26.13 ? 73 PHE A CB 1 ATOM 553 C CG . PHE A 1 73 ? 52.927 70.099 17.179 1.00 27.23 ? 73 PHE A CG 1 ATOM 554 C CD1 . PHE A 1 73 ? 53.492 69.917 18.451 1.00 26.47 ? 73 PHE A CD1 1 ATOM 555 C CD2 . PHE A 1 73 ? 51.537 70.122 17.071 1.00 28.00 ? 73 PHE A CD2 1 ATOM 556 C CE1 . PHE A 1 73 ? 52.689 69.803 19.578 1.00 27.10 ? 73 PHE A CE1 1 ATOM 557 C CE2 . PHE A 1 73 ? 50.737 70.000 18.199 1.00 27.34 ? 73 PHE A CE2 1 ATOM 558 C CZ . PHE A 1 73 ? 51.310 69.853 19.449 1.00 27.25 ? 73 PHE A CZ 1 ATOM 559 N N . ALA A 1 74 ? 57.044 70.348 15.187 1.00 24.52 ? 74 ALA A N 1 ATOM 560 C CA . ALA A 1 74 ? 57.977 69.951 14.133 1.00 24.99 ? 74 ALA A CA 1 ATOM 561 C C . ALA A 1 74 ? 57.777 68.501 13.676 1.00 24.55 ? 74 ALA A C 1 ATOM 562 O O . ALA A 1 74 ? 57.963 68.188 12.503 1.00 24.37 ? 74 ALA A O 1 ATOM 563 C CB . ALA A 1 74 ? 59.407 70.138 14.616 1.00 25.91 ? 74 ALA A CB 1 ATOM 564 N N . ALA A 1 75 ? 57.438 67.631 14.620 1.00 24.12 ? 75 ALA A N 1 ATOM 565 C CA . ALA A 1 75 ? 57.317 66.205 14.359 1.00 24.34 ? 75 ALA A CA 1 ATOM 566 C C . ALA A 1 75 ? 56.623 65.522 15.536 1.00 23.41 ? 75 ALA A C 1 ATOM 567 O O . ALA A 1 75 ? 56.437 66.123 16.604 1.00 22.13 ? 75 ALA A O 1 ATOM 568 C CB . ALA A 1 75 ? 58.707 65.606 14.173 1.00 23.77 ? 75 ALA A CB 1 ATOM 569 N N . TYR A 1 76 ? 56.285 64.251 15.351 1.00 22.54 ? 76 TYR A N 1 ATOM 570 C CA . TYR A 1 76 ? 55.838 63.416 16.460 1.00 23.35 ? 76 TYR A CA 1 ATOM 571 C C . TYR A 1 76 ? 56.239 61.959 16.304 1.00 23.46 ? 76 TYR A C 1 ATOM 572 O O . TYR A 1 76 ? 56.505 61.491 15.190 1.00 23.62 ? 76 TYR A O 1 ATOM 573 C CB . TYR A 1 76 ? 54.323 63.508 16.677 1.00 24.35 ? 76 TYR A CB 1 ATOM 574 C CG . TYR A 1 76 ? 53.477 62.664 15.746 1.00 23.16 ? 76 TYR A CG 1 ATOM 575 C CD1 . TYR A 1 76 ? 53.177 63.103 14.463 1.00 23.56 ? 76 TYR A CD1 1 ATOM 576 C CD2 . TYR A 1 76 ? 52.958 61.441 16.162 1.00 23.41 ? 76 TYR A CD2 1 ATOM 577 C CE1 . TYR A 1 76 ? 52.390 62.360 13.608 1.00 22.64 ? 76 TYR A CE1 1 ATOM 578 C CE2 . TYR A 1 76 ? 52.177 60.671 15.315 1.00 24.05 ? 76 TYR A CE2 1 ATOM 579 C CZ . TYR A 1 76 ? 51.887 61.141 14.040 1.00 23.28 ? 76 TYR A CZ 1 ATOM 580 O OH . TYR A 1 76 ? 51.115 60.414 13.180 1.00 24.91 ? 76 TYR A OH 1 ATOM 581 N N . ARG A 1 77 ? 56.247 61.267 17.439 1.00 24.68 ? 77 ARG A N 1 ATOM 582 C CA . ARG A 1 77 ? 56.552 59.821 17.510 1.00 26.26 ? 77 ARG A CA 1 ATOM 583 C C . ARG A 1 77 ? 55.320 59.051 17.999 1.00 25.86 ? 77 ARG A C 1 ATOM 584 O O . ARG A 1 77 ? 54.620 59.503 18.914 1.00 26.04 ? 77 ARG A O 1 ATOM 585 C CB . ARG A 1 77 ? 57.733 59.569 18.454 1.00 29.21 ? 77 ARG A CB 1 ATOM 586 C CG . ARG A 1 77 ? 58.086 58.099 18.745 1.00 31.77 ? 77 ARG A CG 1 ATOM 587 C CD . ARG A 1 77 ? 59.294 57.969 19.682 1.00 33.44 ? 77 ARG A CD 1 ATOM 588 N NE . ARG A 1 77 ? 59.048 58.615 20.977 1.00 37.63 ? 77 ARG A NE 1 ATOM 589 C CZ . ARG A 1 77 ? 59.967 59.175 21.789 1.00 42.24 ? 77 ARG A CZ 1 ATOM 590 N NH1 . ARG A 1 77 ? 61.273 59.208 21.493 1.00 47.41 ? 77 ARG A NH1 1 ATOM 591 N NH2 . ARG A 1 77 ? 59.573 59.732 22.926 1.00 41.72 ? 77 ARG A NH2 1 ATOM 592 N N . ALA A 1 78 ? 55.104 57.885 17.402 1.00 24.81 ? 78 ALA A N 1 ATOM 593 C CA . ALA A 1 78 ? 54.084 56.939 17.800 1.00 24.70 ? 78 ALA A CA 1 ATOM 594 C C . ALA A 1 78 ? 54.822 55.595 17.844 1.00 25.31 ? 78 ALA A C 1 ATOM 595 O O . ALA A 1 78 ? 55.278 55.128 16.821 1.00 24.45 ? 78 ALA A O 1 ATOM 596 C CB . ALA A 1 78 ? 52.962 56.898 16.794 1.00 25.63 ? 78 ALA A CB 1 ATOM 597 N N . ALA A 1 79 ? 54.959 54.994 19.016 1.00 27.50 ? 79 ALA A N 1 ATOM 598 C CA . ALA A 1 79 ? 55.655 53.720 19.066 1.00 29.67 ? 79 ALA A CA 1 ATOM 599 C C . ALA A 1 79 ? 57.053 53.887 18.475 1.00 30.25 ? 79 ALA A C 1 ATOM 600 O O . ALA A 1 79 ? 57.814 54.762 18.888 1.00 30.19 ? 79 ALA A O 1 ATOM 601 C CB . ALA A 1 79 ? 54.877 52.658 18.307 1.00 28.84 ? 79 ALA A CB 1 ATOM 602 N N . ASP A 1 80 ? 57.375 53.053 17.496 1.00 31.60 ? 80 ASP A N 1 ATOM 603 C CA . ASP A 1 80 ? 58.681 53.070 16.844 1.00 32.95 ? 80 ASP A CA 1 ATOM 604 C C . ASP A 1 80 ? 58.696 53.793 15.499 1.00 31.39 ? 80 ASP A C 1 ATOM 605 O O . ASP A 1 80 ? 59.579 53.579 14.683 1.00 31.15 ? 80 ASP A O 1 ATOM 606 C CB . ASP A 1 80 ? 59.279 51.662 16.736 1.00 37.08 ? 80 ASP A CB 1 ATOM 607 C CG . ASP A 1 80 ? 58.369 50.681 16.028 1.00 41.15 ? 80 ASP A CG 1 ATOM 608 O OD1 . ASP A 1 80 ? 57.323 51.081 15.489 1.00 42.22 ? 80 ASP A OD1 1 ATOM 609 O OD2 . ASP A 1 80 ? 58.702 49.481 16.021 1.00 48.56 ? 80 ASP A OD2 1 ATOM 610 N N . ARG A 1 81 ? 57.689 54.625 15.284 1.00 28.74 ? 81 ARG A N 1 ATOM 611 C CA . ARG A 1 81 ? 57.513 55.393 14.064 1.00 27.20 ? 81 ARG A CA 1 ATOM 612 C C . ARG A 1 81 ? 57.562 56.885 14.414 1.00 26.44 ? 81 ARG A C 1 ATOM 613 O O . ARG A 1 81 ? 57.151 57.288 15.505 1.00 27.42 ? 81 ARG A O 1 ATOM 614 C CB . ARG A 1 81 ? 56.156 55.061 13.446 1.00 28.81 ? 81 ARG A CB 1 ATOM 615 C CG . ARG A 1 81 ? 56.056 53.612 12.964 1.00 28.83 ? 81 ARG A CG 1 ATOM 616 C CD . ARG A 1 81 ? 54.628 53.177 12.664 1.00 28.17 ? 81 ARG A CD 1 ATOM 617 N NE . ARG A 1 81 ? 53.898 52.994 13.911 1.00 27.71 ? 81 ARG A NE 1 ATOM 618 C CZ . ARG A 1 81 ? 52.915 53.767 14.382 1.00 27.66 ? 81 ARG A CZ 1 ATOM 619 N NH1 . ARG A 1 81 ? 52.468 54.846 13.724 1.00 26.89 ? 81 ARG A NH1 1 ATOM 620 N NH2 . ARG A 1 81 ? 52.366 53.449 15.550 1.00 28.07 ? 81 ARG A NH2 1 ATOM 621 N N . SER A 1 82 ? 58.078 57.695 13.510 1.00 26.36 ? 82 SER A N 1 ATOM 622 C CA . SER A 1 82 ? 57.968 59.136 13.672 1.00 25.98 ? 82 SER A CA 1 ATOM 623 C C . SER A 1 82 ? 57.624 59.767 12.345 1.00 26.94 ? 82 SER A C 1 ATOM 624 O O . SER A 1 82 ? 57.770 59.147 11.273 1.00 26.44 ? 82 SER A O 1 ATOM 625 C CB . SER A 1 82 ? 59.236 59.707 14.302 1.00 26.34 ? 82 SER A CB 1 ATOM 626 O OG . SER A 1 82 ? 60.343 59.497 13.444 1.00 26.87 ? 82 SER A OG 1 ATOM 627 N N . TYR A 1 83 ? 57.116 60.998 12.435 1.00 25.89 ? 83 TYR A N 1 ATOM 628 C CA . TYR A 1 83 ? 56.585 61.742 11.313 1.00 24.36 ? 83 TYR A CA 1 ATOM 629 C C . TYR A 1 83 ? 57.012 63.197 11.468 1.00 25.18 ? 83 TYR A C 1 ATOM 630 O O . TYR A 1 83 ? 56.763 63.799 12.515 1.00 24.02 ? 83 TYR A O 1 ATOM 631 C CB . TYR A 1 83 ? 55.063 61.627 11.279 1.00 25.37 ? 83 TYR A CB 1 ATOM 632 C CG . TYR A 1 83 ? 54.602 60.189 11.304 1.00 25.46 ? 83 TYR A CG 1 ATOM 633 C CD1 . TYR A 1 83 ? 54.459 59.463 10.122 1.00 27.50 ? 83 TYR A CD1 1 ATOM 634 C CD2 . TYR A 1 83 ? 54.384 59.537 12.501 1.00 26.39 ? 83 TYR A CD2 1 ATOM 635 C CE1 . TYR A 1 83 ? 54.084 58.128 10.131 1.00 27.79 ? 83 TYR A CE1 1 ATOM 636 C CE2 . TYR A 1 83 ? 54.003 58.204 12.533 1.00 27.60 ? 83 TYR A CE2 1 ATOM 637 C CZ . TYR A 1 83 ? 53.870 57.503 11.339 1.00 29.00 ? 83 TYR A CZ 1 ATOM 638 O OH . TYR A 1 83 ? 53.476 56.181 11.371 1.00 29.19 ? 83 TYR A OH 1 ATOM 639 N N . PHE A 1 84 ? 57.645 63.738 10.425 1.00 25.34 ? 84 PHE A N 1 ATOM 640 C CA . PHE A 1 84 ? 58.204 65.094 10.403 1.00 26.06 ? 84 PHE A CA 1 ATOM 641 C C . PHE A 1 84 ? 57.439 65.901 9.365 1.00 28.31 ? 84 PHE A C 1 ATOM 642 O O . PHE A 1 84 ? 57.192 65.407 8.262 1.00 27.19 ? 84 PHE A O 1 ATOM 643 C CB . PHE A 1 84 ? 59.706 65.053 10.022 1.00 26.17 ? 84 PHE A CB 1 ATOM 644 C CG . PHE A 1 84 ? 60.579 64.503 11.110 1.00 25.35 ? 84 PHE A CG 1 ATOM 645 C CD1 . PHE A 1 84 ? 60.557 63.157 11.404 1.00 25.82 ? 84 PHE A CD1 1 ATOM 646 C CD2 . PHE A 1 84 ? 61.393 65.330 11.862 1.00 25.86 ? 84 PHE A CD2 1 ATOM 647 C CE1 . PHE A 1 84 ? 61.323 62.640 12.430 1.00 25.97 ? 84 PHE A CE1 1 ATOM 648 C CE2 . PHE A 1 84 ? 62.169 64.823 12.891 1.00 26.78 ? 84 PHE A CE2 1 ATOM 649 C CZ . PHE A 1 84 ? 62.128 63.466 13.179 1.00 26.84 ? 84 PHE A CZ 1 ATOM 650 N N . PHE A 1 85 ? 57.037 67.125 9.712 1.00 26.65 ? 85 PHE A N 1 ATOM 651 C CA . PHE A 1 85 ? 56.496 68.047 8.717 1.00 27.92 ? 85 PHE A CA 1 ATOM 652 C C . PHE A 1 85 ? 57.588 68.410 7.705 1.00 29.99 ? 85 PHE A C 1 ATOM 653 O O . PHE A 1 85 ? 58.774 68.405 8.030 1.00 29.79 ? 85 PHE A O 1 ATOM 654 C CB . PHE A 1 85 ? 55.983 69.317 9.382 1.00 27.32 ? 85 PHE A CB 1 ATOM 655 C CG . PHE A 1 85 ? 54.707 69.126 10.150 1.00 26.23 ? 85 PHE A CG 1 ATOM 656 C CD1 . PHE A 1 85 ? 53.484 69.096 9.490 1.00 26.84 ? 85 PHE A CD1 1 ATOM 657 C CD2 . PHE A 1 85 ? 54.730 68.983 11.532 1.00 26.18 ? 85 PHE A CD2 1 ATOM 658 C CE1 . PHE A 1 85 ? 52.309 68.935 10.193 1.00 26.71 ? 85 PHE A CE1 1 ATOM 659 C CE2 . PHE A 1 85 ? 53.567 68.816 12.241 1.00 25.19 ? 85 PHE A CE2 1 ATOM 660 C CZ . PHE A 1 85 ? 52.349 68.804 11.571 1.00 26.56 ? 85 PHE A CZ 1 ATOM 661 N N . GLN A 1 86 ? 57.206 68.733 6.480 1.00 32.72 ? 86 GLN A N 1 ATOM 662 C CA . GLN A 1 86 ? 58.241 68.980 5.483 1.00 36.20 ? 86 GLN A CA 1 ATOM 663 C C . GLN A 1 86 ? 58.951 70.329 5.675 1.00 35.05 ? 86 GLN A C 1 ATOM 664 O O . GLN A 1 86 ? 60.027 70.543 5.128 1.00 36.13 ? 86 GLN A O 1 ATOM 665 C CB . GLN A 1 86 ? 57.740 68.743 4.078 1.00 39.27 ? 86 GLN A CB 1 ATOM 666 C CG . GLN A 1 86 ? 56.890 69.830 3.528 1.00 43.44 ? 86 GLN A CG 1 ATOM 667 C CD . GLN A 1 86 ? 56.482 69.566 2.101 1.00 47.41 ? 86 GLN A CD 1 ATOM 668 O OE1 . GLN A 1 86 ? 55.916 70.417 1.404 1.00 50.59 ? 86 GLN A OE1 1 ATOM 669 N NE2 . GLN A 1 86 ? 56.756 68.364 1.663 1.00 51.06 ? 86 GLN A NE2 1 ATOM 670 N N . ASN A 1 87 ? 58.368 71.213 6.481 1.00 33.70 ? 87 ASN A N 1 ATOM 671 C CA . ASN A 1 87 ? 59.059 72.426 6.931 1.00 32.35 ? 87 ASN A CA 1 ATOM 672 C C . ASN A 1 87 ? 59.659 72.353 8.337 1.00 31.58 ? 87 ASN A C 1 ATOM 673 O O . ASN A 1 87 ? 60.001 73.382 8.896 1.00 31.71 ? 87 ASN A O 1 ATOM 674 C CB . ASN A 1 87 ? 58.142 73.650 6.808 1.00 32.55 ? 87 ASN A CB 1 ATOM 675 C CG . ASN A 1 87 ? 56.982 73.625 7.792 1.00 32.41 ? 87 ASN A CG 1 ATOM 676 O OD1 . ASN A 1 87 ? 56.578 72.573 8.280 1.00 31.41 ? 87 ASN A OD1 1 ATOM 677 N ND2 . ASN A 1 87 ? 56.447 74.792 8.086 1.00 32.78 ? 87 ASN A ND2 1 ATOM 678 N N . ALA A 1 88 ? 59.804 71.152 8.905 1.00 31.35 ? 88 ALA A N 1 ATOM 679 C CA . ALA A 1 88 ? 60.568 70.964 10.145 1.00 31.24 ? 88 ALA A CA 1 ATOM 680 C C . ALA A 1 88 ? 61.976 71.472 9.887 1.00 31.22 ? 88 ALA A C 1 ATOM 681 O O . ALA A 1 88 ? 62.404 71.474 8.741 1.00 30.67 ? 88 ALA A O 1 ATOM 682 C CB . ALA A 1 88 ? 60.631 69.509 10.535 1.00 31.12 ? 88 ALA A CB 1 ATOM 683 N N . PRO A 1 89 ? 62.689 71.933 10.926 1.00 31.50 ? 89 PRO A N 1 ATOM 684 C CA . PRO A 1 89 ? 64.040 72.391 10.606 1.00 34.63 ? 89 PRO A CA 1 ATOM 685 C C . PRO A 1 89 ? 64.826 71.267 9.935 1.00 36.52 ? 89 PRO A C 1 ATOM 686 O O . PRO A 1 89 ? 64.671 70.105 10.326 1.00 35.16 ? 89 PRO A O 1 ATOM 687 C CB . PRO A 1 89 ? 64.625 72.762 11.964 1.00 33.69 ? 89 PRO A CB 1 ATOM 688 C CG . PRO A 1 89 ? 63.428 73.085 12.799 1.00 32.93 ? 89 PRO A CG 1 ATOM 689 C CD . PRO A 1 89 ? 62.362 72.136 12.343 1.00 30.95 ? 89 PRO A CD 1 ATOM 690 N N . PRO A 1 90 ? 65.612 71.593 8.888 1.00 40.10 ? 90 PRO A N 1 ATOM 691 C CA . PRO A 1 90 ? 66.201 70.526 8.052 1.00 40.01 ? 90 PRO A CA 1 ATOM 692 C C . PRO A 1 90 ? 67.007 69.422 8.793 1.00 39.04 ? 90 PRO A C 1 ATOM 693 O O . PRO A 1 90 ? 66.999 68.259 8.355 1.00 40.47 ? 90 PRO A O 1 ATOM 694 C CB . PRO A 1 90 ? 67.092 71.292 7.053 1.00 41.83 ? 90 PRO A CB 1 ATOM 695 C CG . PRO A 1 90 ? 66.688 72.724 7.126 1.00 41.98 ? 90 PRO A CG 1 ATOM 696 C CD . PRO A 1 90 ? 65.844 72.949 8.343 1.00 40.71 ? 90 PRO A CD 1 ATOM 697 N N . ILE A 1 91 ? 67.664 69.779 9.902 1.00 35.18 ? 91 ILE A N 1 ATOM 698 C CA . ILE A 1 91 ? 68.522 68.860 10.671 1.00 31.87 ? 91 ILE A CA 1 ATOM 699 C C . ILE A 1 91 ? 67.758 68.162 11.806 1.00 30.54 ? 91 ILE A C 1 ATOM 700 O O . ILE A 1 91 ? 68.317 67.309 12.512 1.00 28.40 ? 91 ILE A O 1 ATOM 701 C CB . ILE A 1 91 ? 69.755 69.659 11.206 1.00 33.56 ? 91 ILE A CB 1 ATOM 702 C CG1 . ILE A 1 91 ? 70.490 70.358 10.047 1.00 33.35 ? 91 ILE A CG1 1 ATOM 703 C CG2 . ILE A 1 91 ? 70.738 68.804 11.991 1.00 34.30 ? 91 ILE A CG2 1 ATOM 704 C CD1 . ILE A 1 91 ? 70.939 69.440 8.918 1.00 34.18 ? 91 ILE A CD1 1 ATOM 705 N N . ALA A 1 92 ? 66.471 68.479 11.977 1.00 27.27 ? 92 ALA A N 1 ATOM 706 C CA . ALA A 1 92 ? 65.720 67.957 13.121 1.00 27.65 ? 92 ALA A CA 1 ATOM 707 C C . ALA A 1 92 ? 65.744 66.429 13.212 1.00 26.46 ? 92 ALA A C 1 ATOM 708 O O . ALA A 1 92 ? 65.833 65.867 14.309 1.00 26.44 ? 92 ALA A O 1 ATOM 709 C CB . ALA A 1 92 ? 64.275 68.447 13.094 1.00 28.95 ? 92 ALA A CB 1 ATOM 710 N N . SER A 1 93 ? 65.667 65.755 12.078 1.00 26.93 ? 93 SER A N 1 ATOM 711 C CA . SER A 1 93 ? 65.624 64.292 12.091 1.00 28.05 ? 93 SER A CA 1 ATOM 712 C C . SER A 1 93 ? 66.875 63.608 12.682 1.00 29.16 ? 93 SER A C 1 ATOM 713 O O . SER A 1 93 ? 66.788 62.452 13.063 1.00 28.01 ? 93 SER A O 1 ATOM 714 C CB . SER A 1 93 ? 65.301 63.750 10.702 1.00 28.83 ? 93 SER A CB 1 ATOM 715 O OG . SER A 1 93 ? 66.317 64.064 9.784 1.00 31.88 ? 93 SER A OG 1 ATOM 716 N N . TYR A 1 94 ? 67.994 64.332 12.813 1.00 29.23 ? 94 TYR A N 1 ATOM 717 C CA . TYR A 1 94 ? 69.223 63.841 13.472 1.00 29.94 ? 94 TYR A CA 1 ATOM 718 C C . TYR A 1 94 ? 69.261 64.057 14.959 1.00 30.07 ? 94 TYR A C 1 ATOM 719 O O . TYR A 1 94 ? 70.161 63.569 15.640 1.00 30.14 ? 94 TYR A O 1 ATOM 720 C CB . TYR A 1 94 ? 70.434 64.540 12.851 1.00 31.47 ? 94 TYR A CB 1 ATOM 721 C CG . TYR A 1 94 ? 70.545 64.228 11.392 1.00 34.43 ? 94 TYR A CG 1 ATOM 722 C CD1 . TYR A 1 94 ? 71.116 63.028 10.956 1.00 38.39 ? 94 TYR A CD1 1 ATOM 723 C CD2 . TYR A 1 94 ? 70.048 65.101 10.440 1.00 38.38 ? 94 TYR A CD2 1 ATOM 724 C CE1 . TYR A 1 94 ? 71.209 62.729 9.598 1.00 40.25 ? 94 TYR A CE1 1 ATOM 725 C CE2 . TYR A 1 94 ? 70.131 64.814 9.085 1.00 41.39 ? 94 TYR A CE2 1 ATOM 726 C CZ . TYR A 1 94 ? 70.709 63.635 8.671 1.00 41.67 ? 94 TYR A CZ 1 ATOM 727 O OH . TYR A 1 94 ? 70.766 63.393 7.326 1.00 46.72 ? 94 TYR A OH 1 ATOM 728 N N . VAL A 1 95 ? 68.299 64.814 15.472 1.00 26.85 ? 95 VAL A N 1 ATOM 729 C CA . VAL A 1 95 ? 68.292 65.258 16.854 1.00 27.61 ? 95 VAL A CA 1 ATOM 730 C C . VAL A 1 95 ? 67.150 64.639 17.645 1.00 26.97 ? 95 VAL A C 1 ATOM 731 O O . VAL A 1 95 ? 67.296 64.390 18.831 1.00 27.25 ? 95 VAL A O 1 ATOM 732 C CB . VAL A 1 95 ? 68.163 66.803 16.862 1.00 28.76 ? 95 VAL A CB 1 ATOM 733 C CG1 . VAL A 1 95 ? 67.933 67.357 18.255 1.00 31.76 ? 95 VAL A CG1 1 ATOM 734 C CG2 . VAL A 1 95 ? 69.411 67.417 16.271 1.00 30.35 ? 95 VAL A CG2 1 ATOM 735 N N . ILE A 1 96 ? 65.993 64.455 17.007 1.00 27.49 ? 96 ILE A N 1 ATOM 736 C CA . ILE A 1 96 ? 64.810 63.906 17.684 1.00 26.76 ? 96 ILE A CA 1 ATOM 737 C C . ILE A 1 96 ? 64.343 62.620 17.010 1.00 24.48 ? 96 ILE A C 1 ATOM 738 O O . ILE A 1 96 ? 64.389 62.495 15.791 1.00 24.97 ? 96 ILE A O 1 ATOM 739 C CB . ILE A 1 96 ? 63.626 64.921 17.778 1.00 27.22 ? 96 ILE A CB 1 ATOM 740 C CG1 . ILE A 1 96 ? 63.271 65.499 16.411 1.00 28.25 ? 96 ILE A CG1 1 ATOM 741 C CG2 . ILE A 1 96 ? 63.962 66.013 18.775 1.00 28.83 ? 96 ILE A CG2 1 ATOM 742 C CD1 . ILE A 1 96 ? 62.069 66.435 16.414 1.00 28.41 ? 96 ILE A CD1 1 ATOM 743 N N . PHE A 1 97 ? 63.851 61.698 17.830 1.00 24.88 ? 97 PHE A N 1 ATOM 744 C CA . PHE A 1 97 ? 63.278 60.438 17.369 1.00 25.81 ? 97 PHE A CA 1 ATOM 745 C C . PHE A 1 97 ? 64.235 59.657 16.456 1.00 26.91 ? 97 PHE A C 1 ATOM 746 O O . PHE A 1 97 ? 63.824 59.055 15.454 1.00 27.17 ? 97 PHE A O 1 ATOM 747 C CB . PHE A 1 97 ? 61.933 60.697 16.669 1.00 25.39 ? 97 PHE A CB 1 ATOM 748 C CG . PHE A 1 97 ? 60.998 61.587 17.447 1.00 23.80 ? 97 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 97 ? 60.865 61.463 18.826 1.00 23.40 ? 97 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 97 ? 60.232 62.538 16.784 1.00 23.97 ? 97 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 97 ? 60.010 62.279 19.541 1.00 24.23 ? 97 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 97 ? 59.367 63.352 17.494 1.00 22.88 ? 97 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 97 ? 59.244 63.212 18.869 1.00 22.68 ? 97 PHE A CZ 1 ATOM 754 N N . THR A 1 98 ? 65.517 59.710 16.787 1.00 29.25 ? 98 THR A N 1 ATOM 755 C CA . THR A 1 98 ? 66.540 59.052 15.988 1.00 31.97 ? 98 THR A CA 1 ATOM 756 C C . THR A 1 98 ? 66.353 57.546 15.942 1.00 33.89 ? 98 THR A C 1 ATOM 757 O O . THR A 1 98 ? 66.534 56.937 14.905 1.00 35.66 ? 98 THR A O 1 ATOM 758 C CB . THR A 1 98 ? 67.968 59.405 16.453 1.00 30.98 ? 98 THR A CB 1 ATOM 759 O OG1 . THR A 1 98 ? 68.114 59.127 17.844 1.00 31.54 ? 98 THR A OG1 1 ATOM 760 C CG2 . THR A 1 98 ? 68.247 60.868 16.226 1.00 32.11 ? 98 THR A CG2 1 ATOM 761 N N . ASP A 1 99 ? 65.985 56.954 17.066 1.00 34.87 ? 99 ASP A N 1 ATOM 762 C CA . ASP A 1 99 ? 65.781 55.514 17.108 1.00 39.14 ? 99 ASP A CA 1 ATOM 763 C C . ASP A 1 99 ? 64.369 55.093 16.694 1.00 37.16 ? 99 ASP A C 1 ATOM 764 O O . ASP A 1 99 ? 63.678 54.442 17.451 1.00 42.04 ? 99 ASP A O 1 ATOM 765 C CB . ASP A 1 99 ? 66.100 54.996 18.513 1.00 40.82 ? 99 ASP A CB 1 ATOM 766 C CG . ASP A 1 99 ? 65.615 55.936 19.610 1.00 50.61 ? 99 ASP A CG 1 ATOM 767 O OD1 . ASP A 1 99 ? 65.162 57.065 19.289 1.00 57.23 ? 99 ASP A OD1 1 ATOM 768 O OD2 . ASP A 1 99 ? 65.692 55.549 20.797 1.00 55.09 ? 99 ASP A OD2 1 ATOM 769 N N . THR A 1 100 ? 63.956 55.455 15.487 1.00 35.76 ? 100 THR A N 1 ATOM 770 C CA . THR A 1 100 ? 62.634 55.108 14.984 1.00 32.59 ? 100 THR A CA 1 ATOM 771 C C . THR A 1 100 ? 62.601 55.133 13.472 1.00 32.33 ? 100 THR A C 1 ATOM 772 O O . THR A 1 100 ? 63.496 55.667 12.840 1.00 32.59 ? 100 THR A O 1 ATOM 773 C CB . THR A 1 100 ? 61.538 56.125 15.421 1.00 31.74 ? 100 THR A CB 1 ATOM 774 O OG1 . THR A 1 100 ? 61.713 57.358 14.723 1.00 28.79 ? 100 THR A OG1 1 ATOM 775 C CG2 . THR A 1 100 ? 61.549 56.386 16.904 1.00 31.47 ? 100 THR A CG2 1 ATOM 776 N N . ASN A 1 101 ? 61.555 54.555 12.897 1.00 33.20 ? 101 ASN A N 1 ATOM 777 C CA . ASN A 1 101 ? 61.336 54.656 11.457 1.00 33.52 ? 101 ASN A CA 1 ATOM 778 C C . ASN A 1 101 ? 60.712 56.019 11.147 1.00 33.08 ? 101 ASN A C 1 ATOM 779 O O . ASN A 1 101 ? 59.540 56.262 11.448 1.00 32.07 ? 101 ASN A O 1 ATOM 780 C CB . ASN A 1 101 ? 60.440 53.529 10.945 1.00 35.31 ? 101 ASN A CB 1 ATOM 781 C CG . ASN A 1 101 ? 61.008 52.157 11.271 1.00 40.85 ? 101 ASN A CG 1 ATOM 782 O OD1 . ASN A 1 101 ? 62.143 51.851 10.901 1.00 44.91 ? 101 ASN A OD1 1 ATOM 783 N ND2 . ASN A 1 101 ? 60.256 51.346 12.016 1.00 42.32 ? 101 ASN A ND2 1 ATOM 784 N N . GLN A 1 102 ? 61.509 56.879 10.516 1.00 32.60 ? 102 GLN A N 1 ATOM 785 C CA . GLN A 1 102 ? 61.159 58.262 10.270 1.00 32.18 ? 102 GLN A CA 1 ATOM 786 C C . GLN A 1 102 ? 60.455 58.392 8.955 1.00 32.80 ? 102 GLN A C 1 ATOM 787 O O . GLN A 1 102 ? 60.822 57.745 7.972 1.00 33.14 ? 102 GLN A O 1 ATOM 788 C CB . GLN A 1 102 ? 62.413 59.138 10.264 1.00 31.09 ? 102 GLN A CB 1 ATOM 789 C CG . GLN A 1 102 ? 63.157 59.115 11.583 1.00 30.94 ? 102 GLN A CG 1 ATOM 790 C CD . GLN A 1 102 ? 64.283 60.126 11.634 1.00 31.03 ? 102 GLN A CD 1 ATOM 791 O OE1 . GLN A 1 102 ? 64.845 60.475 10.603 1.00 33.13 ? 102 GLN A OE1 1 ATOM 792 N NE2 . GLN A 1 102 ? 64.618 60.597 12.827 1.00 31.31 ? 102 GLN A NE2 1 ATOM 793 N N . ASN A 1 103 ? 59.439 59.245 8.936 1.00 31.18 ? 103 ASN A N 1 ATOM 794 C CA . ASN A 1 103 ? 58.641 59.487 7.765 1.00 30.34 ? 103 ASN A CA 1 ATOM 795 C C . ASN A 1 103 ? 58.463 60.994 7.605 1.00 32.97 ? 103 ASN A C 1 ATOM 796 O O . ASN A 1 103 ? 58.456 61.747 8.600 1.00 30.13 ? 103 ASN A O 1 ATOM 797 C CB . ASN A 1 103 ? 57.283 58.813 7.960 1.00 31.35 ? 103 ASN A CB 1 ATOM 798 C CG . ASN A 1 103 ? 57.396 57.298 8.167 1.00 31.93 ? 103 ASN A CG 1 ATOM 799 O OD1 . ASN A 1 103 ? 57.529 56.553 7.201 1.00 33.96 ? 103 ASN A OD1 1 ATOM 800 N ND2 . ASN A 1 103 ? 57.331 56.839 9.418 1.00 30.56 ? 103 ASN A ND2 1 ATOM 801 N N . ILE A 1 104 ? 58.306 61.437 6.364 1.00 32.96 ? 104 ILE A N 1 ATOM 802 C CA . ILE A 1 104 ? 58.078 62.845 6.089 1.00 35.08 ? 104 ILE A CA 1 ATOM 803 C C . ILE A 1 104 ? 56.639 63.010 5.645 1.00 35.72 ? 104 ILE A C 1 ATOM 804 O O . ILE A 1 104 ? 56.210 62.361 4.704 1.00 35.16 ? 104 ILE A O 1 ATOM 805 C CB . ILE A 1 104 ? 59.082 63.396 5.055 1.00 35.57 ? 104 ILE A CB 1 ATOM 806 C CG1 . ILE A 1 104 ? 60.480 63.402 5.685 1.00 36.67 ? 104 ILE A CG1 1 ATOM 807 C CG2 . ILE A 1 104 ? 58.706 64.810 4.602 1.00 36.08 ? 104 ILE A CG2 1 ATOM 808 C CD1 . ILE A 1 104 ? 61.605 63.630 4.704 1.00 38.36 ? 104 ILE A CD1 1 ATOM 809 N N . MET A 1 105 ? 55.918 63.897 6.316 1.00 33.58 ? 105 MET A N 1 ATOM 810 C CA . MET A 1 105 ? 54.554 64.204 5.959 1.00 32.91 ? 105 MET A CA 1 ATOM 811 C C . MET A 1 105 ? 54.686 65.210 4.836 1.00 33.99 ? 105 MET A C 1 ATOM 812 O O . MET A 1 105 ? 55.479 66.127 4.929 1.00 36.06 ? 105 MET A O 1 ATOM 813 C CB . MET A 1 105 ? 53.814 64.788 7.145 1.00 31.64 ? 105 MET A CB 1 ATOM 814 C CG . MET A 1 105 ? 53.578 63.768 8.232 1.00 30.66 ? 105 MET A CG 1 ATOM 815 S SD . MET A 1 105 ? 52.702 64.395 9.657 1.00 30.49 ? 105 MET A SD 1 ATOM 816 C CE . MET A 1 105 ? 53.913 65.491 10.370 1.00 29.84 ? 105 MET A CE 1 ATOM 817 N N . ASN A 1 106 ? 53.923 65.041 3.771 1.00 35.28 ? 106 ASN A N 1 ATOM 818 C CA . ASN A 1 106 ? 54.052 65.934 2.639 1.00 39.72 ? 106 ASN A CA 1 ATOM 819 C C . ASN A 1 106 ? 53.272 67.239 2.717 1.00 38.86 ? 106 ASN A C 1 ATOM 820 O O . ASN A 1 106 ? 52.610 67.637 1.774 1.00 38.93 ? 106 ASN A O 1 ATOM 821 C CB . ASN A 1 106 ? 53.696 65.175 1.360 1.00 45.29 ? 106 ASN A CB 1 ATOM 822 N N . PHE A 1 107 ? 53.392 67.912 3.851 1.00 36.61 ? 107 PHE A N 1 ATOM 823 C CA . PHE A 1 107 ? 52.761 69.201 4.069 1.00 33.38 ? 107 PHE A CA 1 ATOM 824 C C . PHE A 1 107 ? 53.444 69.923 5.219 1.00 32.14 ? 107 PHE A C 1 ATOM 825 O O . PHE A 1 107 ? 54.150 69.322 6.012 1.00 28.35 ? 107 PHE A O 1 ATOM 826 C CB . PHE A 1 107 ? 51.253 69.098 4.263 1.00 33.70 ? 107 PHE A CB 1 ATOM 827 C CG . PHE A 1 107 ? 50.839 68.116 5.302 1.00 35.32 ? 107 PHE A CG 1 ATOM 828 C CD1 . PHE A 1 107 ? 50.656 66.791 4.980 1.00 35.98 ? 107 PHE A CD1 1 ATOM 829 C CD2 . PHE A 1 107 ? 50.619 68.517 6.597 1.00 35.28 ? 107 PHE A CD2 1 ATOM 830 C CE1 . PHE A 1 107 ? 50.269 65.883 5.934 1.00 35.33 ? 107 PHE A CE1 1 ATOM 831 C CE2 . PHE A 1 107 ? 50.234 67.613 7.557 1.00 35.20 ? 107 PHE A CE2 1 ATOM 832 C CZ . PHE A 1 107 ? 50.061 66.294 7.225 1.00 34.92 ? 107 PHE A CZ 1 ATOM 833 N N . ASN A 1 108 ? 53.227 71.221 5.290 1.00 31.96 ? 108 ASN A N 1 ATOM 834 C CA . ASN A 1 108 ? 53.828 72.033 6.333 1.00 32.01 ? 108 ASN A CA 1 ATOM 835 C C . ASN A 1 108 ? 52.997 72.037 7.598 1.00 29.86 ? 108 ASN A C 1 ATOM 836 O O . ASN A 1 108 ? 51.829 71.678 7.572 1.00 29.20 ? 108 ASN A O 1 ATOM 837 C CB . ASN A 1 108 ? 54.018 73.440 5.818 1.00 32.82 ? 108 ASN A CB 1 ATOM 838 C CG . ASN A 1 108 ? 55.111 73.523 4.769 1.00 38.19 ? 108 ASN A CG 1 ATOM 839 O OD1 . ASN A 1 108 ? 55.941 72.612 4.611 1.00 34.58 ? 108 ASN A OD1 1 ATOM 840 N ND2 . ASN A 1 108 ? 55.122 74.610 4.053 1.00 43.56 ? 108 ASN A ND2 1 ATOM 841 N N . ASN A 1 109 ? 53.614 72.473 8.695 1.00 27.90 ? 109 ASN A N 1 ATOM 842 C CA . ASN A 1 109 ? 52.942 72.571 9.984 1.00 27.61 ? 109 ASN A CA 1 ATOM 843 C C . ASN A 1 109 ? 52.059 73.827 10.153 1.00 27.96 ? 109 ASN A C 1 ATOM 844 O O . ASN A 1 109 ? 51.610 74.096 11.261 1.00 28.80 ? 109 ASN A O 1 ATOM 845 C CB . ASN A 1 109 ? 53.962 72.510 11.113 1.00 28.30 ? 109 ASN A CB 1 ATOM 846 C CG . ASN A 1 109 ? 54.761 73.792 11.257 1.00 29.07 ? 109 ASN A CG 1 ATOM 847 O OD1 . ASN A 1 109 ? 54.741 74.670 10.390 1.00 27.11 ? 109 ASN A OD1 1 ATOM 848 N ND2 . ASN A 1 109 ? 55.469 73.903 12.365 1.00 30.26 ? 109 ASN A ND2 1 ATOM 849 N N . THR A 1 110 ? 51.840 74.587 9.076 1.00 25.80 ? 110 THR A N 1 ATOM 850 C CA . THR A 1 110 ? 50.989 75.782 9.111 1.00 25.99 ? 110 THR A CA 1 ATOM 851 C C . THR A 1 110 ? 49.532 75.399 8.923 1.00 25.05 ? 110 THR A C 1 ATOM 852 O O . THR A 1 110 ? 49.230 74.406 8.256 1.00 22.72 ? 110 THR A O 1 ATOM 853 C CB . THR A 1 110 ? 51.370 76.765 7.995 1.00 26.11 ? 110 THR A CB 1 ATOM 854 O OG1 . THR A 1 110 ? 51.294 76.102 6.732 1.00 27.31 ? 110 THR A OG1 1 ATOM 855 C CG2 . THR A 1 110 ? 52.786 77.290 8.184 1.00 27.18 ? 110 THR A CG2 1 ATOM 856 N N . PHE A 1 111 ? 48.627 76.195 9.491 1.00 23.92 ? 111 PHE A N 1 ATOM 857 C CA . PHE A 1 111 ? 47.207 75.970 9.293 1.00 25.10 ? 111 PHE A CA 1 ATOM 858 C C . PHE A 1 111 ? 46.825 76.001 7.808 1.00 24.67 ? 111 PHE A C 1 ATOM 859 O O . PHE A 1 111 ? 46.046 75.176 7.358 1.00 23.79 ? 111 PHE A O 1 ATOM 860 C CB . PHE A 1 111 ? 46.356 76.988 10.055 1.00 25.44 ? 111 PHE A CB 1 ATOM 861 C CG . PHE A 1 111 ? 46.421 76.844 11.547 1.00 24.83 ? 111 PHE A CG 1 ATOM 862 C CD1 . PHE A 1 111 ? 46.127 75.633 12.157 1.00 25.34 ? 111 PHE A CD1 1 ATOM 863 C CD2 . PHE A 1 111 ? 46.734 77.937 12.347 1.00 26.20 ? 111 PHE A CD2 1 ATOM 864 C CE1 . PHE A 1 111 ? 46.174 75.504 13.542 1.00 26.24 ? 111 PHE A CE1 1 ATOM 865 C CE2 . PHE A 1 111 ? 46.785 77.818 13.728 1.00 25.85 ? 111 PHE A CE2 1 ATOM 866 C CZ . PHE A 1 111 ? 46.496 76.608 14.327 1.00 25.40 ? 111 PHE A CZ 1 ATOM 867 N N . GLU A 1 112 ? 47.417 76.916 7.055 1.00 25.53 ? 112 GLU A N 1 ATOM 868 C CA . GLU A 1 112 ? 47.076 77.062 5.644 1.00 27.40 ? 112 GLU A CA 1 ATOM 869 C C . GLU A 1 112 ? 47.405 75.799 4.882 1.00 25.80 ? 112 GLU A C 1 ATOM 870 O O . GLU A 1 112 ? 46.592 75.326 4.119 1.00 25.18 ? 112 GLU A O 1 ATOM 871 C CB . GLU A 1 112 ? 47.783 78.254 5.021 1.00 30.10 ? 112 GLU A CB 1 ATOM 872 C CG . GLU A 1 112 ? 47.229 79.592 5.502 1.00 34.36 ? 112 GLU A CG 1 ATOM 873 C CD . GLU A 1 112 ? 47.754 80.058 6.868 1.00 38.53 ? 112 GLU A CD 1 ATOM 874 O OE1 . GLU A 1 112 ? 48.644 79.400 7.482 1.00 41.16 ? 112 GLU A OE1 1 ATOM 875 O OE2 . GLU A 1 112 ? 47.263 81.106 7.336 1.00 40.77 ? 112 GLU A OE2 1 ATOM 876 N N . SER A 1 113 ? 48.579 75.233 5.135 1.00 25.92 ? 113 SER A N 1 ATOM 877 C CA . SER A 1 113 ? 49.007 74.013 4.450 1.00 25.82 ? 113 SER A CA 1 ATOM 878 C C . SER A 1 113 ? 48.184 72.796 4.909 1.00 25.28 ? 113 SER A C 1 ATOM 879 O O . SER A 1 113 ? 47.727 72.009 4.093 1.00 24.26 ? 113 SER A O 1 ATOM 880 C CB . SER A 1 113 ? 50.514 73.810 4.645 1.00 26.03 ? 113 SER A CB 1 ATOM 881 O OG . SER A 1 113 ? 50.905 72.521 4.202 1.00 28.92 ? 113 SER A OG 1 ATOM 882 N N . ILE A 1 114 ? 47.958 72.669 6.212 1.00 24.26 ? 114 ILE A N 1 ATOM 883 C CA . ILE A 1 114 ? 47.194 71.546 6.749 1.00 23.60 ? 114 ILE A CA 1 ATOM 884 C C . ILE A 1 114 ? 45.763 71.553 6.230 1.00 23.80 ? 114 ILE A C 1 ATOM 885 O O . ILE A 1 114 ? 45.196 70.487 5.894 1.00 23.07 ? 114 ILE A O 1 ATOM 886 C CB . ILE A 1 114 ? 47.213 71.554 8.286 1.00 23.77 ? 114 ILE A CB 1 ATOM 887 C CG1 . ILE A 1 114 ? 48.614 71.268 8.784 1.00 23.24 ? 114 ILE A CG1 1 ATOM 888 C CG2 . ILE A 1 114 ? 46.265 70.512 8.873 1.00 23.40 ? 114 ILE A CG2 1 ATOM 889 C CD1 . ILE A 1 114 ? 48.833 71.685 10.218 1.00 23.83 ? 114 ILE A CD1 1 ATOM 890 N N . GLU A 1 115 ? 45.185 72.748 6.167 1.00 23.72 ? 115 GLU A N 1 ATOM 891 C CA . GLU A 1 115 ? 43.824 72.914 5.660 1.00 24.83 ? 115 GLU A CA 1 ATOM 892 C C . GLU A 1 115 ? 43.735 72.563 4.157 1.00 26.94 ? 115 GLU A C 1 ATOM 893 O O . GLU A 1 115 ? 42.811 71.897 3.748 1.00 27.94 ? 115 GLU A O 1 ATOM 894 C CB . GLU A 1 115 ? 43.319 74.330 5.940 1.00 25.60 ? 115 GLU A CB 1 ATOM 895 C CG . GLU A 1 115 ? 43.001 74.539 7.427 1.00 26.86 ? 115 GLU A CG 1 ATOM 896 C CD . GLU A 1 115 ? 42.363 75.880 7.749 1.00 30.12 ? 115 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 115 ? 42.248 76.722 6.832 1.00 29.78 ? 115 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 115 ? 41.945 76.072 8.918 1.00 26.88 ? 115 GLU A OE2 1 ATOM 899 N N . ILE A 1 116 ? 44.711 72.980 3.362 1.00 27.62 ? 116 ILE A N 1 ATOM 900 C CA . ILE A 1 116 ? 44.755 72.586 1.933 1.00 29.52 ? 116 ILE A CA 1 ATOM 901 C C . ILE A 1 116 ? 44.856 71.081 1.722 1.00 30.86 ? 116 ILE A C 1 ATOM 902 O O . ILE A 1 116 ? 44.110 70.537 0.922 1.00 32.43 ? 116 ILE A O 1 ATOM 903 C CB . ILE A 1 116 ? 45.881 73.314 1.184 1.00 30.09 ? 116 ILE A CB 1 ATOM 904 C CG1 . ILE A 1 116 ? 45.465 74.772 1.009 1.00 29.99 ? 116 ILE A CG1 1 ATOM 905 C CG2 . ILE A 1 116 ? 46.187 72.644 -0.176 1.00 30.77 ? 116 ILE A CG2 1 ATOM 906 C CD1 . ILE A 1 116 ? 46.606 75.709 0.707 1.00 31.11 ? 116 ILE A CD1 1 ATOM 907 N N . VAL A 1 117 ? 45.760 70.397 2.416 1.00 32.02 ? 117 VAL A N 1 ATOM 908 C CA . VAL A 1 117 ? 45.866 68.939 2.234 1.00 33.53 ? 117 VAL A CA 1 ATOM 909 C C . VAL A 1 117 ? 44.703 68.155 2.811 1.00 33.32 ? 117 VAL A C 1 ATOM 910 O O . VAL A 1 117 ? 44.282 67.166 2.214 1.00 32.45 ? 117 VAL A O 1 ATOM 911 C CB . VAL A 1 117 ? 47.185 68.345 2.755 1.00 35.29 ? 117 VAL A CB 1 ATOM 912 C CG1 . VAL A 1 117 ? 48.344 69.008 2.049 1.00 37.16 ? 117 VAL A CG1 1 ATOM 913 C CG2 . VAL A 1 117 ? 47.314 68.469 4.268 1.00 36.66 ? 117 VAL A CG2 1 ATOM 914 N N . GLY A 1 118 ? 44.191 68.575 3.968 1.00 30.06 ? 118 GLY A N 1 ATOM 915 C CA . GLY A 1 118 ? 43.066 67.907 4.582 1.00 29.68 ? 118 GLY A CA 1 ATOM 916 C C . GLY A 1 118 ? 41.739 68.199 3.915 1.00 31.02 ? 118 GLY A C 1 ATOM 917 O O . GLY A 1 118 ? 40.783 67.432 4.065 1.00 32.33 ? 118 GLY A O 1 ATOM 918 N N . GLY A 1 119 ? 41.668 69.319 3.199 1.00 32.45 ? 119 GLY A N 1 ATOM 919 C CA . GLY A 1 119 ? 40.425 69.792 2.593 1.00 31.97 ? 119 GLY A CA 1 ATOM 920 C C . GLY A 1 119 ? 39.395 70.263 3.599 1.00 32.59 ? 119 GLY A C 1 ATOM 921 O O . GLY A 1 119 ? 38.223 70.382 3.260 1.00 34.79 ? 119 GLY A O 1 ATOM 922 N N . THR A 1 120 ? 39.818 70.558 4.832 1.00 30.95 ? 120 THR A N 1 ATOM 923 C CA . THR A 1 120 ? 38.906 70.939 5.910 1.00 31.12 ? 120 THR A CA 1 ATOM 924 C C . THR A 1 120 ? 39.503 72.101 6.706 1.00 29.44 ? 120 THR A C 1 ATOM 925 O O . THR A 1 120 ? 40.692 72.068 7.036 1.00 29.11 ? 120 THR A O 1 ATOM 926 C CB . THR A 1 120 ? 38.678 69.755 6.856 1.00 32.65 ? 120 THR A CB 1 ATOM 927 O OG1 . THR A 1 120 ? 38.245 68.632 6.088 1.00 38.31 ? 120 THR A OG1 1 ATOM 928 C CG2 . THR A 1 120 ? 37.601 70.044 7.884 1.00 33.90 ? 120 THR A CG2 1 ATOM 929 N N . THR A 1 121 ? 38.687 73.101 7.017 1.00 26.54 ? 121 THR A N 1 ATOM 930 C CA . THR A 1 121 ? 39.133 74.272 7.780 1.00 25.53 ? 121 THR A CA 1 ATOM 931 C C . THR A 1 121 ? 38.914 74.150 9.308 1.00 24.63 ? 121 THR A C 1 ATOM 932 O O . THR A 1 121 ? 38.156 73.299 9.800 1.00 23.29 ? 121 THR A O 1 ATOM 933 C CB . THR A 1 121 ? 38.450 75.552 7.298 1.00 25.89 ? 121 THR A CB 1 ATOM 934 O OG1 . THR A 1 121 ? 37.070 75.514 7.666 1.00 27.67 ? 121 THR A OG1 1 ATOM 935 C CG2 . THR A 1 121 ? 38.582 75.713 5.774 1.00 27.03 ? 121 THR A CG2 1 ATOM 936 N N . ARG A 1 122 ? 39.572 75.034 10.047 1.00 23.82 ? 122 ARG A N 1 ATOM 937 C CA . ARG A 1 122 ? 39.409 75.102 11.485 1.00 24.14 ? 122 ARG A CA 1 ATOM 938 C C . ARG A 1 122 ? 37.950 75.375 11.866 1.00 25.24 ? 122 ARG A C 1 ATOM 939 O O . ARG A 1 122 ? 37.456 74.774 12.795 1.00 23.72 ? 122 ARG A O 1 ATOM 940 C CB . ARG A 1 122 ? 40.312 76.173 12.060 1.00 24.12 ? 122 ARG A CB 1 ATOM 941 C CG . ARG A 1 122 ? 41.764 75.736 12.109 1.00 24.19 ? 122 ARG A CG 1 ATOM 942 C CD . ARG A 1 122 ? 42.660 76.927 12.305 1.00 24.13 ? 122 ARG A CD 1 ATOM 943 N NE . ARG A 1 122 ? 42.723 77.724 11.099 1.00 23.36 ? 122 ARG A NE 1 ATOM 944 C CZ . ARG A 1 122 ? 43.203 78.951 11.018 1.00 23.81 ? 122 ARG A CZ 1 ATOM 945 N NH1 . ARG A 1 122 ? 43.692 79.574 12.085 1.00 23.77 ? 122 ARG A NH1 1 ATOM 946 N NH2 . ARG A 1 122 ? 43.193 79.558 9.838 1.00 24.69 ? 122 ARG A NH2 1 ATOM 947 N N . SER A 1 123 ? 37.263 76.251 11.128 1.00 24.98 ? 123 SER A N 1 ATOM 948 C CA . SER A 1 123 ? 35.869 76.610 11.429 1.00 27.18 ? 123 SER A CA 1 ATOM 949 C C . SER A 1 123 ? 34.904 75.444 11.363 1.00 28.40 ? 123 SER A C 1 ATOM 950 O O . SER A 1 123 ? 33.830 75.494 11.954 1.00 28.11 ? 123 SER A O 1 ATOM 951 C CB . SER A 1 123 ? 35.362 77.693 10.477 1.00 27.82 ? 123 SER A CB 1 ATOM 952 O OG . SER A 1 123 ? 35.976 78.914 10.807 1.00 30.46 ? 123 SER A OG 1 ATOM 953 N N . GLU A 1 124 ? 35.283 74.402 10.640 1.00 26.87 ? 124 GLU A N 1 ATOM 954 C CA . GLU A 1 124 ? 34.457 73.237 10.537 1.00 29.87 ? 124 GLU A CA 1 ATOM 955 C C . GLU A 1 124 ? 35.014 72.035 11.318 1.00 29.91 ? 124 GLU A C 1 ATOM 956 O O . GLU A 1 124 ? 34.423 70.969 11.244 1.00 27.24 ? 124 GLU A O 1 ATOM 957 C CB . GLU A 1 124 ? 34.155 72.919 9.059 1.00 33.40 ? 124 GLU A CB 1 ATOM 958 C CG . GLU A 1 124 ? 35.354 72.597 8.199 1.00 37.86 ? 124 GLU A CG 1 ATOM 959 C CD . GLU A 1 124 ? 35.050 72.533 6.699 1.00 40.90 ? 124 GLU A CD 1 ATOM 960 O OE1 . GLU A 1 124 ? 33.874 72.322 6.319 1.00 43.56 ? 124 GLU A OE1 1 ATOM 961 O OE2 . GLU A 1 124 ? 36.005 72.690 5.906 1.00 38.04 ? 124 GLU A OE2 1 ATOM 962 N N . THR A 1 125 ? 36.081 72.224 12.115 1.00 26.42 ? 125 THR A N 1 ATOM 963 C CA . THR A 1 125 ? 36.698 71.122 12.891 1.00 25.77 ? 125 THR A CA 1 ATOM 964 C C . THR A 1 125 ? 36.358 71.242 14.395 1.00 25.20 ? 125 THR A C 1 ATOM 965 O O . THR A 1 125 ? 36.846 72.140 15.083 1.00 25.84 ? 125 THR A O 1 ATOM 966 C CB . THR A 1 125 ? 38.227 71.066 12.645 1.00 25.23 ? 125 THR A CB 1 ATOM 967 O OG1 . THR A 1 125 ? 38.454 70.984 11.241 1.00 24.81 ? 125 THR A OG1 1 ATOM 968 C CG2 . THR A 1 125 ? 38.891 69.863 13.311 1.00 24.52 ? 125 THR A CG2 1 ATOM 969 N N . PRO A 1 126 ? 35.505 70.341 14.913 1.00 24.97 ? 126 PRO A N 1 ATOM 970 C CA . PRO A 1 126 ? 35.170 70.434 16.337 1.00 24.99 ? 126 PRO A CA 1 ATOM 971 C C . PRO A 1 126 ? 36.340 70.205 17.277 1.00 23.11 ? 126 PRO A C 1 ATOM 972 O O . PRO A 1 126 ? 37.192 69.366 17.017 1.00 22.11 ? 126 PRO A O 1 ATOM 973 C CB . PRO A 1 126 ? 34.126 69.323 16.533 1.00 25.92 ? 126 PRO A CB 1 ATOM 974 C CG . PRO A 1 126 ? 33.583 69.057 15.182 1.00 26.67 ? 126 PRO A CG 1 ATOM 975 C CD . PRO A 1 126 ? 34.703 69.309 14.226 1.00 25.52 ? 126 PRO A CD 1 ATOM 976 N N . LEU A 1 127 ? 36.325 70.928 18.387 1.00 22.80 ? 127 LEU A N 1 ATOM 977 C CA . LEU A 1 127 ? 37.325 70.823 19.434 1.00 23.19 ? 127 LEU A CA 1 ATOM 978 C C . LEU A 1 127 ? 36.619 70.398 20.696 1.00 22.88 ? 127 LEU A C 1 ATOM 979 O O . LEU A 1 127 ? 35.462 70.753 20.903 1.00 23.86 ? 127 LEU A O 1 ATOM 980 C CB . LEU A 1 127 ? 38.018 72.179 19.658 1.00 22.20 ? 127 LEU A CB 1 ATOM 981 C CG . LEU A 1 127 ? 38.690 72.786 18.416 1.00 23.62 ? 127 LEU A CG 1 ATOM 982 C CD1 . LEU A 1 127 ? 39.318 74.133 18.748 1.00 23.68 ? 127 LEU A CD1 1 ATOM 983 C CD2 . LEU A 1 127 ? 39.743 71.863 17.830 1.00 22.85 ? 127 LEU A CD2 1 ATOM 984 N N . GLY A 1 128 ? 37.323 69.682 21.553 1.00 23.09 ? 128 GLY A N 1 ATOM 985 C CA . GLY A 1 128 ? 36.765 69.228 22.836 1.00 22.92 ? 128 GLY A CA 1 ATOM 986 C C . GLY A 1 128 ? 37.488 67.975 23.253 1.00 24.65 ? 128 GLY A C 1 ATOM 987 O O . GLY A 1 128 ? 38.398 67.512 22.549 1.00 23.00 ? 128 GLY A O 1 ATOM 988 N N . ILE A 1 129 ? 37.083 67.413 24.388 1.00 26.59 ? 129 ILE A N 1 ATOM 989 C CA . ILE A 1 129 ? 37.811 66.304 24.985 1.00 29.74 ? 129 ILE A CA 1 ATOM 990 C C . ILE A 1 129 ? 37.882 65.115 24.056 1.00 26.52 ? 129 ILE A C 1 ATOM 991 O O . ILE A 1 129 ? 38.943 64.528 23.888 1.00 25.37 ? 129 ILE A O 1 ATOM 992 C CB . ILE A 1 129 ? 37.176 65.838 26.321 1.00 35.39 ? 129 ILE A CB 1 ATOM 993 C CG1 . ILE A 1 129 ? 37.237 66.951 27.364 1.00 39.73 ? 129 ILE A CG1 1 ATOM 994 C CG2 . ILE A 1 129 ? 37.885 64.598 26.865 1.00 37.00 ? 129 ILE A CG2 1 ATOM 995 C CD1 . ILE A 1 129 ? 38.645 67.434 27.628 1.00 43.04 ? 129 ILE A CD1 1 ATOM 996 N N . MET A 1 130 ? 36.753 64.738 23.485 1.00 25.78 ? 130 MET A N 1 ATOM 997 C CA . MET A 1 130 ? 36.702 63.519 22.693 1.00 27.21 ? 130 MET A CA 1 ATOM 998 C C . MET A 1 130 ? 37.408 63.690 21.332 1.00 25.30 ? 130 MET A C 1 ATOM 999 O O . MET A 1 130 ? 37.906 62.729 20.764 1.00 25.30 ? 130 MET A O 1 ATOM 1000 C CB . MET A 1 130 ? 35.251 63.028 22.577 1.00 29.22 ? 130 MET A CB 1 ATOM 1001 C CG . MET A 1 130 ? 34.585 62.788 23.952 1.00 32.97 ? 130 MET A CG 1 ATOM 1002 S SD . MET A 1 130 ? 35.465 61.722 25.155 1.00 38.52 ? 130 MET A SD 1 ATOM 1003 C CE . MET A 1 130 ? 35.477 60.124 24.335 1.00 40.09 ? 130 MET A CE 1 ATOM 1004 N N . HIS A 1 131 ? 37.473 64.920 20.838 1.00 24.27 ? 131 HIS A N 1 ATOM 1005 C CA . HIS A 1 131 ? 38.242 65.214 19.619 1.00 24.17 ? 131 HIS A CA 1 ATOM 1006 C C . HIS A 1 131 ? 39.729 65.211 19.886 1.00 23.08 ? 131 HIS A C 1 ATOM 1007 O O . HIS A 1 131 ? 40.488 64.773 19.054 1.00 22.18 ? 131 HIS A O 1 ATOM 1008 C CB . HIS A 1 131 ? 37.790 66.537 19.055 1.00 24.74 ? 131 HIS A CB 1 ATOM 1009 C CG . HIS A 1 131 ? 36.323 66.555 18.798 1.00 26.17 ? 131 HIS A CG 1 ATOM 1010 N ND1 . HIS A 1 131 ? 35.752 65.822 17.782 1.00 25.48 ? 131 HIS A ND1 1 ATOM 1011 C CD2 . HIS A 1 131 ? 35.299 67.111 19.486 1.00 27.48 ? 131 HIS A CD2 1 ATOM 1012 C CE1 . HIS A 1 131 ? 34.440 65.965 17.821 1.00 25.65 ? 131 HIS A CE1 1 ATOM 1013 N NE2 . HIS A 1 131 ? 34.138 66.747 18.840 1.00 27.05 ? 131 HIS A NE2 1 ATOM 1014 N N . PHE A 1 132 ? 40.123 65.682 21.071 1.00 23.70 ? 132 PHE A N 1 ATOM 1015 C CA . PHE A 1 132 ? 41.516 65.573 21.531 1.00 25.37 ? 132 PHE A CA 1 ATOM 1016 C C . PHE A 1 132 ? 41.910 64.092 21.550 1.00 24.67 ? 132 PHE A C 1 ATOM 1017 O O . PHE A 1 132 ? 42.928 63.687 20.999 1.00 23.74 ? 132 PHE A O 1 ATOM 1018 C CB . PHE A 1 132 ? 41.623 66.232 22.913 1.00 26.84 ? 132 PHE A CB 1 ATOM 1019 C CG . PHE A 1 132 ? 42.942 66.049 23.588 1.00 30.01 ? 132 PHE A CG 1 ATOM 1020 C CD1 . PHE A 1 132 ? 43.168 64.942 24.386 1.00 32.47 ? 132 PHE A CD1 1 ATOM 1021 C CD2 . PHE A 1 132 ? 43.940 67.001 23.462 1.00 32.95 ? 132 PHE A CD2 1 ATOM 1022 C CE1 . PHE A 1 132 ? 44.378 64.769 25.036 1.00 36.68 ? 132 PHE A CE1 1 ATOM 1023 C CE2 . PHE A 1 132 ? 45.159 66.838 24.108 1.00 32.33 ? 132 PHE A CE2 1 ATOM 1024 C CZ . PHE A 1 132 ? 45.381 65.723 24.889 1.00 34.27 ? 132 PHE A CZ 1 ATOM 1025 N N . GLU A 1 133 ? 41.040 63.289 22.153 1.00 24.47 ? 133 GLU A N 1 ATOM 1026 C CA . GLU A 1 133 ? 41.229 61.849 22.325 1.00 24.21 ? 133 GLU A CA 1 ATOM 1027 C C . GLU A 1 133 ? 41.376 61.141 20.970 1.00 22.41 ? 133 GLU A C 1 ATOM 1028 O O . GLU A 1 133 ? 42.314 60.371 20.751 1.00 22.28 ? 133 GLU A O 1 ATOM 1029 C CB . GLU A 1 133 ? 39.997 61.338 23.107 1.00 26.36 ? 133 GLU A CB 1 ATOM 1030 C CG . GLU A 1 133 ? 40.020 59.947 23.649 1.00 26.62 ? 133 GLU A CG 1 ATOM 1031 C CD . GLU A 1 133 ? 39.984 58.861 22.585 1.00 27.27 ? 133 GLU A CD 1 ATOM 1032 O OE1 . GLU A 1 133 ? 39.013 58.804 21.773 1.00 29.39 ? 133 GLU A OE1 1 ATOM 1033 O OE2 . GLU A 1 133 ? 40.916 58.036 22.593 1.00 26.98 ? 133 GLU A OE2 1 ATOM 1034 N N . ALA A 1 134 ? 40.441 61.406 20.067 1.00 22.00 ? 134 ALA A N 1 ATOM 1035 C CA . ALA A 1 134 ? 40.424 60.755 18.752 1.00 22.57 ? 134 ALA A CA 1 ATOM 1036 C C . ALA A 1 134 ? 41.598 61.190 17.876 1.00 22.60 ? 134 ALA A C 1 ATOM 1037 O O . ALA A 1 134 ? 42.156 60.386 17.135 1.00 22.22 ? 134 ALA A O 1 ATOM 1038 C CB . ALA A 1 134 ? 39.113 61.037 18.026 1.00 23.27 ? 134 ALA A CB 1 ATOM 1039 N N . SER A 1 135 ? 41.979 62.461 17.988 1.00 22.23 ? 135 SER A N 1 ATOM 1040 C CA . SER A 1 135 ? 43.132 62.982 17.268 1.00 22.54 ? 135 SER A CA 1 ATOM 1041 C C . SER A 1 135 ? 44.406 62.257 17.648 1.00 22.44 ? 135 SER A C 1 ATOM 1042 O O . SER A 1 135 ? 45.214 61.938 16.778 1.00 24.61 ? 135 SER A O 1 ATOM 1043 C CB . SER A 1 135 ? 43.257 64.490 17.484 1.00 23.38 ? 135 SER A CB 1 ATOM 1044 O OG . SER A 1 135 ? 42.153 65.149 16.879 1.00 22.83 ? 135 SER A OG 1 ATOM 1045 N N . ILE A 1 136 ? 44.569 61.946 18.925 1.00 23.20 ? 136 ILE A N 1 ATOM 1046 C CA . ILE A 1 136 ? 45.748 61.196 19.360 1.00 24.07 ? 136 ILE A CA 1 ATOM 1047 C C . ILE A 1 136 ? 45.766 59.790 18.706 1.00 24.40 ? 136 ILE A C 1 ATOM 1048 O O . ILE A 1 136 ? 46.797 59.349 18.250 1.00 24.75 ? 136 ILE A O 1 ATOM 1049 C CB . ILE A 1 136 ? 45.836 61.087 20.891 1.00 24.42 ? 136 ILE A CB 1 ATOM 1050 C CG1 . ILE A 1 136 ? 46.050 62.461 21.536 1.00 24.93 ? 136 ILE A CG1 1 ATOM 1051 C CG2 . ILE A 1 136 ? 46.986 60.180 21.309 1.00 24.39 ? 136 ILE A CG2 1 ATOM 1052 C CD1 . ILE A 1 136 ? 45.721 62.492 23.007 1.00 24.64 ? 136 ILE A CD1 1 ATOM 1053 N N . PHE A 1 137 ? 44.614 59.113 18.682 1.00 25.28 ? 137 PHE A N 1 ATOM 1054 C CA . PHE A 1 137 ? 44.460 57.798 18.030 1.00 24.69 ? 137 PHE A CA 1 ATOM 1055 C C . PHE A 1 137 ? 44.841 57.858 16.583 1.00 24.49 ? 137 PHE A C 1 ATOM 1056 O O . PHE A 1 137 ? 45.687 57.080 16.140 1.00 26.36 ? 137 PHE A O 1 ATOM 1057 C CB . PHE A 1 137 ? 43.028 57.262 18.203 1.00 26.15 ? 137 PHE A CB 1 ATOM 1058 C CG . PHE A 1 137 ? 42.622 56.210 17.178 1.00 26.32 ? 137 PHE A CG 1 ATOM 1059 C CD1 . PHE A 1 137 ? 43.141 54.945 17.237 1.00 27.25 ? 137 PHE A CD1 1 ATOM 1060 C CD2 . PHE A 1 137 ? 41.737 56.517 16.157 1.00 27.23 ? 137 PHE A CD2 1 ATOM 1061 C CE1 . PHE A 1 137 ? 42.787 53.982 16.292 1.00 27.77 ? 137 PHE A CE1 1 ATOM 1062 C CE2 . PHE A 1 137 ? 41.370 55.563 15.214 1.00 27.58 ? 137 PHE A CE2 1 ATOM 1063 C CZ . PHE A 1 137 ? 41.905 54.297 15.281 1.00 26.99 ? 137 PHE A CZ 1 ATOM 1064 N N . HIS A 1 138 ? 44.245 58.789 15.847 1.00 24.31 ? 138 HIS A N 1 ATOM 1065 C CA . HIS A 1 138 ? 44.519 58.924 14.409 1.00 25.47 ? 138 HIS A CA 1 ATOM 1066 C C . HIS A 1 138 ? 45.979 59.159 14.099 1.00 24.94 ? 138 HIS A C 1 ATOM 1067 O O . HIS A 1 138 ? 46.503 58.603 13.133 1.00 25.58 ? 138 HIS A O 1 ATOM 1068 C CB . HIS A 1 138 ? 43.696 60.045 13.786 1.00 25.78 ? 138 HIS A CB 1 ATOM 1069 C CG . HIS A 1 138 ? 42.242 59.745 13.746 1.00 28.03 ? 138 HIS A CG 1 ATOM 1070 N ND1 . HIS A 1 138 ? 41.752 58.546 13.279 1.00 29.93 ? 138 HIS A ND1 1 ATOM 1071 C CD2 . HIS A 1 138 ? 41.167 60.472 14.128 1.00 28.98 ? 138 HIS A CD2 1 ATOM 1072 C CE1 . HIS A 1 138 ? 40.434 58.549 13.369 1.00 29.99 ? 138 HIS A CE1 1 ATOM 1073 N NE2 . HIS A 1 138 ? 40.057 59.705 13.890 1.00 30.49 ? 138 HIS A NE2 1 ATOM 1074 N N . LEU A 1 139 ? 46.630 59.985 14.915 1.00 24.22 ? 139 LEU A N 1 ATOM 1075 C CA . LEU A 1 139 ? 48.063 60.188 14.803 1.00 24.13 ? 139 LEU A CA 1 ATOM 1076 C C . LEU A 1 139 ? 48.853 58.948 15.200 1.00 24.24 ? 139 LEU A C 1 ATOM 1077 O O . LEU A 1 139 ? 49.864 58.622 14.562 1.00 24.48 ? 139 LEU A O 1 ATOM 1078 C CB . LEU A 1 139 ? 48.495 61.396 15.649 1.00 24.69 ? 139 LEU A CB 1 ATOM 1079 C CG . LEU A 1 139 ? 48.037 62.777 15.170 1.00 23.87 ? 139 LEU A CG 1 ATOM 1080 C CD1 . LEU A 1 139 ? 48.820 63.844 15.923 1.00 24.67 ? 139 LEU A CD1 1 ATOM 1081 C CD2 . LEU A 1 139 ? 48.221 62.981 13.682 1.00 24.36 ? 139 LEU A CD2 1 ATOM 1082 N N . PHE A 1 140 ? 48.399 58.254 16.237 1.00 25.57 ? 140 PHE A N 1 ATOM 1083 C CA . PHE A 1 140 ? 49.103 57.070 16.706 1.00 26.60 ? 140 PHE A CA 1 ATOM 1084 C C . PHE A 1 140 ? 49.154 55.988 15.619 1.00 27.12 ? 140 PHE A C 1 ATOM 1085 O O . PHE A 1 140 ? 50.205 55.400 15.351 1.00 27.43 ? 140 PHE A O 1 ATOM 1086 C CB . PHE A 1 140 ? 48.493 56.498 17.985 1.00 26.67 ? 140 PHE A CB 1 ATOM 1087 C CG . PHE A 1 140 ? 49.287 55.337 18.541 1.00 29.25 ? 140 PHE A CG 1 ATOM 1088 C CD1 . PHE A 1 140 ? 50.369 55.556 19.393 1.00 30.27 ? 140 PHE A CD1 1 ATOM 1089 C CD2 . PHE A 1 140 ? 48.990 54.023 18.163 1.00 30.14 ? 140 PHE A CD2 1 ATOM 1090 C CE1 . PHE A 1 140 ? 51.119 54.490 19.881 1.00 30.83 ? 140 PHE A CE1 1 ATOM 1091 C CE2 . PHE A 1 140 ? 49.736 52.958 18.641 1.00 31.26 ? 140 PHE A CE2 1 ATOM 1092 C CZ . PHE A 1 140 ? 50.806 53.189 19.495 1.00 30.87 ? 140 PHE A CZ 1 ATOM 1093 N N . VAL A 1 141 ? 48.019 55.729 14.987 1.00 27.63 ? 141 VAL A N 1 ATOM 1094 C CA . VAL A 1 141 ? 48.004 54.765 13.879 1.00 28.24 ? 141 VAL A CA 1 ATOM 1095 C C . VAL A 1 141 ? 48.378 55.396 12.538 1.00 28.23 ? 141 VAL A C 1 ATOM 1096 O O . VAL A 1 141 ? 48.531 54.685 11.558 1.00 28.82 ? 141 VAL A O 1 ATOM 1097 C CB . VAL A 1 141 ? 46.663 53.971 13.782 1.00 28.42 ? 141 VAL A CB 1 ATOM 1098 C CG1 . VAL A 1 141 ? 46.387 53.249 15.096 1.00 28.90 ? 141 VAL A CG1 1 ATOM 1099 C CG2 . VAL A 1 141 ? 45.480 54.853 13.384 1.00 28.35 ? 141 VAL A CG2 1 ATOM 1100 N N . HIS A 1 142 ? 48.564 56.718 12.508 1.00 27.64 ? 142 HIS A N 1 ATOM 1101 C CA . HIS A 1 142 ? 48.833 57.497 11.291 1.00 28.05 ? 142 HIS A CA 1 ATOM 1102 C C . HIS A 1 142 ? 47.895 57.166 10.135 1.00 29.14 ? 142 HIS A C 1 ATOM 1103 O O . HIS A 1 142 ? 48.312 56.723 9.052 1.00 28.17 ? 142 HIS A O 1 ATOM 1104 C CB . HIS A 1 142 ? 50.307 57.455 10.857 1.00 26.78 ? 142 HIS A CB 1 ATOM 1105 C CG . HIS A 1 142 ? 50.700 58.609 9.979 1.00 26.73 ? 142 HIS A CG 1 ATOM 1106 N ND1 . HIS A 1 142 ? 51.094 59.833 10.480 1.00 26.81 ? 142 HIS A ND1 1 ATOM 1107 C CD2 . HIS A 1 142 ? 50.738 58.731 8.632 1.00 27.95 ? 142 HIS A CD2 1 ATOM 1108 C CE1 . HIS A 1 142 ? 51.368 60.651 9.482 1.00 27.14 ? 142 HIS A CE1 1 ATOM 1109 N NE2 . HIS A 1 142 ? 51.172 60.003 8.347 1.00 26.85 ? 142 HIS A NE2 1 ATOM 1110 N N . ASP A 1 143 ? 46.613 57.398 10.387 1.00 29.52 ? 143 ASP A N 1 ATOM 1111 C CA . ASP A 1 143 ? 45.594 57.279 9.357 1.00 30.86 ? 143 ASP A CA 1 ATOM 1112 C C . ASP A 1 143 ? 45.632 58.536 8.523 1.00 31.35 ? 143 ASP A C 1 ATOM 1113 O O . ASP A 1 143 ? 45.117 59.582 8.948 1.00 30.07 ? 143 ASP A O 1 ATOM 1114 C CB . ASP A 1 143 ? 44.206 57.121 9.969 1.00 30.98 ? 143 ASP A CB 1 ATOM 1115 C CG . ASP A 1 143 ? 43.160 56.749 8.934 1.00 32.40 ? 143 ASP A CG 1 ATOM 1116 O OD1 . ASP A 1 143 ? 43.312 57.112 7.757 1.00 35.73 ? 143 ASP A OD1 1 ATOM 1117 O OD2 . ASP A 1 143 ? 42.180 56.078 9.303 1.00 34.24 ? 143 ASP A OD2 1 ATOM 1118 N N . GLU A 1 144 ? 46.216 58.444 7.333 1.00 31.47 ? 144 GLU A N 1 ATOM 1119 C CA . GLU A 1 144 ? 46.489 59.629 6.525 1.00 33.77 ? 144 GLU A CA 1 ATOM 1120 C C . GLU A 1 144 ? 45.261 60.485 6.213 1.00 32.35 ? 144 GLU A C 1 ATOM 1121 O O . GLU A 1 144 ? 45.386 61.688 6.087 1.00 32.70 ? 144 GLU A O 1 ATOM 1122 C CB . GLU A 1 144 ? 47.253 59.260 5.250 1.00 39.33 ? 144 GLU A CB 1 ATOM 1123 C CG . GLU A 1 144 ? 48.708 58.925 5.536 1.00 43.40 ? 144 GLU A CG 1 ATOM 1124 C CD . GLU A 1 144 ? 49.453 58.351 4.341 1.00 50.77 ? 144 GLU A CD 1 ATOM 1125 O OE1 . GLU A 1 144 ? 49.374 58.941 3.239 1.00 56.02 ? 144 GLU A OE1 1 ATOM 1126 O OE2 . GLU A 1 144 ? 50.145 57.318 4.512 1.00 57.98 ? 144 GLU A OE2 1 ATOM 1127 N N . ASN A 1 145 ? 44.085 59.875 6.122 1.00 32.05 ? 145 ASN A N 1 ATOM 1128 C CA . ASN A 1 145 ? 42.850 60.621 5.896 1.00 33.20 ? 145 ASN A CA 1 ATOM 1129 C C . ASN A 1 145 ? 42.507 61.573 7.037 1.00 30.83 ? 145 ASN A C 1 ATOM 1130 O O . ASN A 1 145 ? 41.853 62.575 6.789 1.00 29.96 ? 145 ASN A O 1 ATOM 1131 C CB . ASN A 1 145 ? 41.643 59.689 5.728 1.00 35.79 ? 145 ASN A CB 1 ATOM 1132 C CG . ASN A 1 145 ? 41.673 58.884 4.437 1.00 40.04 ? 145 ASN A CG 1 ATOM 1133 O OD1 . ASN A 1 145 ? 42.235 59.307 3.416 1.00 42.04 ? 145 ASN A OD1 1 ATOM 1134 N ND2 . ASN A 1 145 ? 41.051 57.709 4.476 1.00 43.22 ? 145 ASN A ND2 1 ATOM 1135 N N . TYR A 1 146 ? 42.910 61.228 8.265 1.00 29.54 ? 146 TYR A N 1 ATOM 1136 C CA . TYR A 1 146 ? 42.618 62.022 9.467 1.00 29.44 ? 146 TYR A CA 1 ATOM 1137 C C . TYR A 1 146 ? 43.799 62.728 10.094 1.00 27.67 ? 146 TYR A C 1 ATOM 1138 O O . TYR A 1 146 ? 43.609 63.481 11.045 1.00 28.07 ? 146 TYR A O 1 ATOM 1139 C CB . TYR A 1 146 ? 41.989 61.144 10.538 1.00 30.81 ? 146 TYR A CB 1 ATOM 1140 C CG . TYR A 1 146 ? 40.699 60.588 10.092 1.00 34.03 ? 146 TYR A CG 1 ATOM 1141 C CD1 . TYR A 1 146 ? 39.558 61.375 10.071 1.00 36.13 ? 146 TYR A CD1 1 ATOM 1142 C CD2 . TYR A 1 146 ? 40.615 59.277 9.632 1.00 38.34 ? 146 TYR A CD2 1 ATOM 1143 C CE1 . TYR A 1 146 ? 38.353 60.857 9.625 1.00 41.01 ? 146 TYR A CE1 1 ATOM 1144 C CE2 . TYR A 1 146 ? 39.420 58.753 9.176 1.00 40.06 ? 146 TYR A CE2 1 ATOM 1145 C CZ . TYR A 1 146 ? 38.296 59.541 9.173 1.00 41.32 ? 146 TYR A CZ 1 ATOM 1146 O OH . TYR A 1 146 ? 37.112 58.994 8.734 1.00 49.53 ? 146 TYR A OH 1 ATOM 1147 N N . VAL A 1 147 ? 45.002 62.504 9.594 1.00 27.53 ? 147 VAL A N 1 ATOM 1148 C CA . VAL A 1 147 ? 46.178 63.199 10.116 1.00 26.75 ? 147 VAL A CA 1 ATOM 1149 C C . VAL A 1 147 ? 46.035 64.739 10.084 1.00 25.61 ? 147 VAL A C 1 ATOM 1150 O O . VAL A 1 147 ? 46.300 65.381 11.095 1.00 24.66 ? 147 VAL A O 1 ATOM 1151 C CB . VAL A 1 147 ? 47.484 62.673 9.486 1.00 27.45 ? 147 VAL A CB 1 ATOM 1152 C CG1 . VAL A 1 147 ? 48.671 63.572 9.814 1.00 27.96 ? 147 VAL A CG1 1 ATOM 1153 C CG2 . VAL A 1 147 ? 47.766 61.265 10.001 1.00 28.23 ? 147 VAL A CG2 1 ATOM 1154 N N . PRO A 1 148 ? 45.566 65.329 8.969 1.00 25.97 ? 148 PRO A N 1 ATOM 1155 C CA . PRO A 1 148 ? 45.485 66.800 8.963 1.00 25.62 ? 148 PRO A CA 1 ATOM 1156 C C . PRO A 1 148 ? 44.527 67.386 10.001 1.00 25.98 ? 148 PRO A C 1 ATOM 1157 O O . PRO A 1 148 ? 44.926 68.265 10.767 1.00 24.26 ? 148 PRO A O 1 ATOM 1158 C CB . PRO A 1 148 ? 45.045 67.118 7.530 1.00 25.89 ? 148 PRO A CB 1 ATOM 1159 C CG . PRO A 1 148 ? 45.667 65.999 6.740 1.00 25.56 ? 148 PRO A CG 1 ATOM 1160 C CD . PRO A 1 148 ? 45.457 64.785 7.594 1.00 26.76 ? 148 PRO A CD 1 ATOM 1161 N N . THR A 1 149 ? 43.299 66.889 10.068 1.00 24.85 ? 149 THR A N 1 ATOM 1162 C CA . THR A 1 149 ? 42.348 67.427 11.029 1.00 25.00 ? 149 THR A CA 1 ATOM 1163 C C . THR A 1 149 ? 42.770 67.142 12.461 1.00 24.08 ? 149 THR A C 1 ATOM 1164 O O . THR A 1 149 ? 42.530 67.961 13.336 1.00 22.08 ? 149 THR A O 1 ATOM 1165 C CB . THR A 1 149 ? 40.905 66.947 10.793 1.00 27.58 ? 149 THR A CB 1 ATOM 1166 O OG1 . THR A 1 149 ? 40.892 65.538 10.714 1.00 28.42 ? 149 THR A OG1 1 ATOM 1167 C CG2 . THR A 1 149 ? 40.381 67.500 9.497 1.00 30.34 ? 149 THR A CG2 1 ATOM 1168 N N . SER A 1 150 ? 43.456 66.023 12.682 1.00 23.32 ? 150 SER A N 1 ATOM 1169 C CA . SER A 1 150 ? 44.013 65.708 14.004 1.00 22.98 ? 150 SER A CA 1 ATOM 1170 C C . SER A 1 150 ? 45.034 66.757 14.460 1.00 22.93 ? 150 SER A C 1 ATOM 1171 O O . SER A 1 150 ? 45.025 67.178 15.619 1.00 21.10 ? 150 SER A O 1 ATOM 1172 C CB . SER A 1 150 ? 44.626 64.312 14.034 1.00 22.75 ? 150 SER A CB 1 ATOM 1173 O OG . SER A 1 150 ? 43.630 63.315 13.783 1.00 23.62 ? 150 SER A OG 1 ATOM 1174 N N . PHE A 1 151 ? 45.898 67.186 13.545 1.00 22.42 ? 151 PHE A N 1 ATOM 1175 C CA . PHE A 1 151 ? 46.771 68.316 13.821 1.00 22.96 ? 151 PHE A CA 1 ATOM 1176 C C . PHE A 1 151 ? 46.018 69.628 14.061 1.00 23.10 ? 151 PHE A C 1 ATOM 1177 O O . PHE A 1 151 ? 46.389 70.371 14.968 1.00 21.29 ? 151 PHE A O 1 ATOM 1178 C CB . PHE A 1 151 ? 47.860 68.469 12.763 1.00 23.63 ? 151 PHE A CB 1 ATOM 1179 C CG . PHE A 1 151 ? 49.060 67.630 13.058 1.00 24.92 ? 151 PHE A CG 1 ATOM 1180 C CD1 . PHE A 1 151 ? 49.829 67.893 14.202 1.00 26.73 ? 151 PHE A CD1 1 ATOM 1181 C CD2 . PHE A 1 151 ? 49.417 66.574 12.235 1.00 27.26 ? 151 PHE A CD2 1 ATOM 1182 C CE1 . PHE A 1 151 ? 50.932 67.120 14.515 1.00 27.58 ? 151 PHE A CE1 1 ATOM 1183 C CE2 . PHE A 1 151 ? 50.528 65.780 12.546 1.00 27.59 ? 151 PHE A CE2 1 ATOM 1184 C CZ . PHE A 1 151 ? 51.284 66.057 13.681 1.00 27.84 ? 151 PHE A CZ 1 ATOM 1185 N N . LEU A 1 152 ? 44.965 69.899 13.292 1.00 21.78 ? 152 LEU A N 1 ATOM 1186 C CA . LEU A 1 152 ? 44.142 71.099 13.560 1.00 23.05 ? 152 LEU A CA 1 ATOM 1187 C C . LEU A 1 152 ? 43.604 71.116 14.998 1.00 23.04 ? 152 LEU A C 1 ATOM 1188 O O . LEU A 1 152 ? 43.695 72.131 15.692 1.00 22.73 ? 152 LEU A O 1 ATOM 1189 C CB . LEU A 1 152 ? 42.992 71.225 12.574 1.00 23.39 ? 152 LEU A CB 1 ATOM 1190 C CG . LEU A 1 152 ? 43.324 71.477 11.104 1.00 23.82 ? 152 LEU A CG 1 ATOM 1191 C CD1 . LEU A 1 152 ? 42.029 71.773 10.361 1.00 24.21 ? 152 LEU A CD1 1 ATOM 1192 C CD2 . LEU A 1 152 ? 44.307 72.624 10.904 1.00 25.15 ? 152 LEU A CD2 1 ATOM 1193 N N . VAL A 1 153 ? 43.098 69.975 15.448 1.00 21.53 ? 153 VAL A N 1 ATOM 1194 C CA . VAL A 1 153 ? 42.643 69.830 16.815 1.00 22.11 ? 153 VAL A CA 1 ATOM 1195 C C . VAL A 1 153 ? 43.780 70.035 17.843 1.00 21.60 ? 153 VAL A C 1 ATOM 1196 O O . VAL A 1 153 ? 43.652 70.855 18.765 1.00 20.84 ? 153 VAL A O 1 ATOM 1197 C CB . VAL A 1 153 ? 41.959 68.460 17.060 1.00 22.51 ? 153 VAL A CB 1 ATOM 1198 C CG1 . VAL A 1 153 ? 41.543 68.322 18.513 1.00 22.54 ? 153 VAL A CG1 1 ATOM 1199 C CG2 . VAL A 1 153 ? 40.726 68.263 16.166 1.00 22.63 ? 153 VAL A CG2 1 ATOM 1200 N N . LEU A 1 154 ? 44.867 69.289 17.694 1.00 21.57 ? 154 LEU A N 1 ATOM 1201 C CA . LEU A 1 154 ? 45.914 69.271 18.721 1.00 22.16 ? 154 LEU A CA 1 ATOM 1202 C C . LEU A 1 154 ? 46.745 70.554 18.745 1.00 21.62 ? 154 LEU A C 1 ATOM 1203 O O . LEU A 1 154 ? 47.066 71.052 19.811 1.00 21.46 ? 154 LEU A O 1 ATOM 1204 C CB . LEU A 1 154 ? 46.796 68.021 18.568 1.00 23.44 ? 154 LEU A CB 1 ATOM 1205 C CG . LEU A 1 154 ? 46.052 66.687 18.812 1.00 23.92 ? 154 LEU A CG 1 ATOM 1206 C CD1 . LEU A 1 154 ? 46.967 65.503 18.539 1.00 24.73 ? 154 LEU A CD1 1 ATOM 1207 C CD2 . LEU A 1 154 ? 45.493 66.589 20.222 1.00 24.62 ? 154 LEU A CD2 1 ATOM 1208 N N . ILE A 1 155 ? 47.056 71.108 17.577 1.00 20.77 ? 155 ILE A N 1 ATOM 1209 C CA . ILE A 1 155 ? 47.721 72.402 17.511 1.00 20.96 ? 155 ILE A CA 1 ATOM 1210 C C . ILE A 1 155 ? 46.895 73.437 18.278 1.00 20.93 ? 155 ILE A C 1 ATOM 1211 O O . ILE A 1 155 ? 47.436 74.207 19.051 1.00 20.92 ? 155 ILE A O 1 ATOM 1212 C CB . ILE A 1 155 ? 47.985 72.886 16.063 1.00 21.28 ? 155 ILE A CB 1 ATOM 1213 C CG1 . ILE A 1 155 ? 49.049 72.005 15.406 1.00 21.91 ? 155 ILE A CG1 1 ATOM 1214 C CG2 . ILE A 1 155 ? 48.474 74.346 16.033 1.00 21.66 ? 155 ILE A CG2 1 ATOM 1215 C CD1 . ILE A 1 155 ? 49.169 72.172 13.907 1.00 22.07 ? 155 ILE A CD1 1 ATOM 1216 N N . GLN A 1 156 ? 45.591 73.459 18.057 1.00 20.58 ? 156 GLN A N 1 ATOM 1217 C CA . GLN A 1 156 ? 44.769 74.469 18.712 1.00 22.02 ? 156 GLN A CA 1 ATOM 1218 C C . GLN A 1 156 ? 44.590 74.236 20.218 1.00 21.74 ? 156 GLN A C 1 ATOM 1219 O O . GLN A 1 156 ? 44.754 75.160 20.997 1.00 21.79 ? 156 GLN A O 1 ATOM 1220 C CB . GLN A 1 156 ? 43.434 74.626 18.023 1.00 21.74 ? 156 GLN A CB 1 ATOM 1221 C CG . GLN A 1 156 ? 43.573 75.226 16.636 1.00 21.57 ? 156 GLN A CG 1 ATOM 1222 C CD . GLN A 1 156 ? 42.222 75.360 16.006 1.00 21.43 ? 156 GLN A CD 1 ATOM 1223 O OE1 . GLN A 1 156 ? 41.623 76.447 15.999 1.00 20.36 ? 156 GLN A OE1 1 ATOM 1224 N NE2 . GLN A 1 156 ? 41.693 74.231 15.530 1.00 21.24 ? 156 GLN A NE2 1 ATOM 1225 N N . MET A 1 157 ? 44.318 72.997 20.609 1.00 21.22 ? 157 MET A N 1 ATOM 1226 C CA . MET A 1 157 ? 44.026 72.693 22.004 1.00 21.11 ? 157 MET A CA 1 ATOM 1227 C C . MET A 1 157 ? 45.262 72.688 22.923 1.00 20.49 ? 157 MET A C 1 ATOM 1228 O O . MET A 1 157 ? 45.108 72.842 24.132 1.00 19.22 ? 157 MET A O 1 ATOM 1229 C CB . MET A 1 157 ? 43.266 71.367 22.109 1.00 22.03 ? 157 MET A CB 1 ATOM 1230 C CG . MET A 1 157 ? 41.862 71.436 21.532 1.00 21.68 ? 157 MET A CG 1 ATOM 1231 S SD . MET A 1 157 ? 40.942 69.889 21.787 1.00 22.50 ? 157 MET A SD 1 ATOM 1232 C CE . MET A 1 157 ? 40.561 69.970 23.525 1.00 22.13 ? 157 MET A CE 1 ATOM 1233 N N . VAL A 1 158 ? 46.454 72.509 22.344 1.00 19.73 ? 158 VAL A N 1 ATOM 1234 C CA . VAL A 1 158 ? 47.710 72.507 23.079 1.00 20.60 ? 158 VAL A CA 1 ATOM 1235 C C . VAL A 1 158 ? 48.497 73.819 22.846 1.00 20.82 ? 158 VAL A C 1 ATOM 1236 O O . VAL A 1 158 ? 48.716 74.582 23.788 1.00 20.61 ? 158 VAL A O 1 ATOM 1237 C CB . VAL A 1 158 ? 48.579 71.277 22.704 1.00 21.62 ? 158 VAL A CB 1 ATOM 1238 C CG1 . VAL A 1 158 ? 49.936 71.304 23.406 1.00 21.94 ? 158 VAL A CG1 1 ATOM 1239 C CG2 . VAL A 1 158 ? 47.846 69.982 23.053 1.00 21.94 ? 158 VAL A CG2 1 ATOM 1240 N N . LEU A 1 159 ? 48.907 74.066 21.606 1.00 20.07 ? 159 LEU A N 1 ATOM 1241 C CA . LEU A 1 159 ? 49.848 75.171 21.291 1.00 20.98 ? 159 LEU A CA 1 ATOM 1242 C C . LEU A 1 159 ? 49.194 76.553 21.240 1.00 20.77 ? 159 LEU A C 1 ATOM 1243 O O . LEU A 1 159 ? 49.707 77.526 21.826 1.00 19.14 ? 159 LEU A O 1 ATOM 1244 C CB . LEU A 1 159 ? 50.589 74.895 19.991 1.00 20.91 ? 159 LEU A CB 1 ATOM 1245 C CG . LEU A 1 159 ? 51.448 73.623 20.025 1.00 23.09 ? 159 LEU A CG 1 ATOM 1246 C CD1 . LEU A 1 159 ? 52.045 73.323 18.662 1.00 22.88 ? 159 LEU A CD1 1 ATOM 1247 C CD2 . LEU A 1 159 ? 52.532 73.720 21.082 1.00 23.05 ? 159 LEU A CD2 1 ATOM 1248 N N . GLU A 1 160 ? 48.048 76.636 20.567 1.00 20.13 ? 160 GLU A N 1 ATOM 1249 C CA . GLU A 1 160 ? 47.344 77.912 20.477 1.00 20.55 ? 160 GLU A CA 1 ATOM 1250 C C . GLU A 1 160 ? 46.795 78.317 21.849 1.00 20.20 ? 160 GLU A C 1 ATOM 1251 O O . GLU A 1 160 ? 46.839 79.481 22.202 1.00 19.61 ? 160 GLU A O 1 ATOM 1252 C CB . GLU A 1 160 ? 46.284 77.910 19.371 1.00 21.49 ? 160 GLU A CB 1 ATOM 1253 C CG . GLU A 1 160 ? 46.860 77.592 17.992 1.00 22.26 ? 160 GLU A CG 1 ATOM 1254 C CD . GLU A 1 160 ? 47.967 78.551 17.580 1.00 24.12 ? 160 GLU A CD 1 ATOM 1255 O OE1 . GLU A 1 160 ? 47.651 79.747 17.384 1.00 24.00 ? 160 GLU A OE1 1 ATOM 1256 O OE2 . GLU A 1 160 ? 49.150 78.118 17.433 1.00 23.36 ? 160 GLU A OE2 1 ATOM 1257 N N . ALA A 1 161 ? 46.318 77.342 22.620 1.00 19.91 ? 161 ALA A N 1 ATOM 1258 C CA . ALA A 1 161 ? 45.933 77.561 24.008 1.00 21.10 ? 161 ALA A CA 1 ATOM 1259 C C . ALA A 1 161 ? 47.099 78.067 24.863 1.00 19.50 ? 161 ALA A C 1 ATOM 1260 O O . ALA A 1 161 ? 46.913 78.945 25.689 1.00 19.19 ? 161 ALA A O 1 ATOM 1261 C CB . ALA A 1 161 ? 45.365 76.284 24.602 1.00 21.85 ? 161 ALA A CB 1 ATOM 1262 N N . ALA A 1 162 ? 48.293 77.520 24.654 1.00 18.81 ? 162 ALA A N 1 ATOM 1263 C CA . ALA A 1 162 ? 49.460 78.022 25.349 1.00 19.62 ? 162 ALA A CA 1 ATOM 1264 C C . ALA A 1 162 ? 49.737 79.474 24.975 1.00 19.50 ? 162 ALA A C 1 ATOM 1265 O O . ALA A 1 162 ? 50.050 80.278 25.863 1.00 18.88 ? 162 ALA A O 1 ATOM 1266 C CB . ALA A 1 162 ? 50.687 77.165 25.080 1.00 19.98 ? 162 ALA A CB 1 ATOM 1267 N N . LYS A 1 163 ? 49.644 79.798 23.684 1.00 18.42 ? 163 LYS A N 1 ATOM 1268 C CA . LYS A 1 163 ? 49.887 81.166 23.224 1.00 18.83 ? 163 LYS A CA 1 ATOM 1269 C C . LYS A 1 163 ? 48.861 82.194 23.790 1.00 18.68 ? 163 LYS A C 1 ATOM 1270 O O . LYS A 1 163 ? 49.210 83.330 24.055 1.00 18.50 ? 163 LYS A O 1 ATOM 1271 C CB . LYS A 1 163 ? 49.855 81.259 21.693 1.00 19.61 ? 163 LYS A CB 1 ATOM 1272 C CG . LYS A 1 163 ? 51.016 80.613 20.938 1.00 20.03 ? 163 LYS A CG 1 ATOM 1273 C CD . LYS A 1 163 ? 50.687 80.517 19.446 1.00 20.89 ? 163 LYS A CD 1 ATOM 1274 C CE . LYS A 1 163 ? 51.741 79.767 18.645 1.00 21.45 ? 163 LYS A CE 1 ATOM 1275 N NZ . LYS A 1 163 ? 51.411 79.774 17.192 1.00 22.70 ? 163 LYS A NZ 1 ATOM 1276 N N . PHE A 1 164 ? 47.611 81.780 23.951 1.00 17.94 ? 164 PHE A N 1 ATOM 1277 C CA . PHE A 1 164 ? 46.515 82.715 24.285 1.00 19.37 ? 164 PHE A CA 1 ATOM 1278 C C . PHE A 1 164 ? 45.615 82.198 25.402 1.00 18.53 ? 164 PHE A C 1 ATOM 1279 O O . PHE A 1 164 ? 44.965 81.165 25.261 1.00 19.29 ? 164 PHE A O 1 ATOM 1280 C CB . PHE A 1 164 ? 45.667 83.009 23.043 1.00 19.10 ? 164 PHE A CB 1 ATOM 1281 C CG . PHE A 1 164 ? 46.409 83.728 21.945 1.00 18.77 ? 164 PHE A CG 1 ATOM 1282 C CD1 . PHE A 1 164 ? 46.650 85.091 22.022 1.00 18.55 ? 164 PHE A CD1 1 ATOM 1283 C CD2 . PHE A 1 164 ? 46.851 83.032 20.811 1.00 19.71 ? 164 PHE A CD2 1 ATOM 1284 C CE1 . PHE A 1 164 ? 47.327 85.759 20.999 1.00 18.76 ? 164 PHE A CE1 1 ATOM 1285 C CE2 . PHE A 1 164 ? 47.524 83.691 19.779 1.00 18.94 ? 164 PHE A CE2 1 ATOM 1286 C CZ . PHE A 1 164 ? 47.773 85.053 19.879 1.00 18.99 ? 164 PHE A CZ 1 ATOM 1287 N N . LYS A 1 165 ? 45.565 82.927 26.505 1.00 19.55 ? 165 LYS A N 1 ATOM 1288 C CA . LYS A 1 165 ? 44.668 82.584 27.616 1.00 20.53 ? 165 LYS A CA 1 ATOM 1289 C C . LYS A 1 165 ? 43.197 82.514 27.177 1.00 19.92 ? 165 LYS A C 1 ATOM 1290 O O . LYS A 1 165 ? 42.454 81.693 27.681 1.00 18.14 ? 165 LYS A O 1 ATOM 1291 C CB . LYS A 1 165 ? 44.854 83.566 28.783 1.00 22.18 ? 165 LYS A CB 1 ATOM 1292 C CG . LYS A 1 165 ? 46.188 83.390 29.470 1.00 26.70 ? 165 LYS A CG 1 ATOM 1293 C CD . LYS A 1 165 ? 46.346 84.353 30.640 1.00 30.29 ? 165 LYS A CD 1 ATOM 1294 C CE . LYS A 1 165 ? 47.528 83.925 31.506 1.00 35.13 ? 165 LYS A CE 1 ATOM 1295 N NZ . LYS A 1 165 ? 47.873 84.926 32.556 1.00 37.79 ? 165 LYS A NZ 1 ATOM 1296 N N . PHE A 1 166 ? 42.806 83.336 26.194 1.00 19.38 ? 166 PHE A N 1 ATOM 1297 C CA . PHE A 1 166 ? 41.450 83.264 25.666 1.00 19.82 ? 166 PHE A CA 1 ATOM 1298 C C . PHE A 1 166 ? 41.140 81.868 25.135 1.00 19.97 ? 166 PHE A C 1 ATOM 1299 O O . PHE A 1 166 ? 40.074 81.329 25.385 1.00 19.42 ? 166 PHE A O 1 ATOM 1300 C CB . PHE A 1 166 ? 41.228 84.315 24.563 1.00 20.80 ? 166 PHE A CB 1 ATOM 1301 C CG . PHE A 1 166 ? 39.860 84.258 23.945 1.00 21.18 ? 166 PHE A CG 1 ATOM 1302 C CD1 . PHE A 1 166 ? 38.795 84.981 24.501 1.00 22.49 ? 166 PHE A CD1 1 ATOM 1303 C CD2 . PHE A 1 166 ? 39.618 83.475 22.825 1.00 21.90 ? 166 PHE A CD2 1 ATOM 1304 C CE1 . PHE A 1 166 ? 37.527 84.930 23.931 1.00 22.54 ? 166 PHE A CE1 1 ATOM 1305 C CE2 . PHE A 1 166 ? 38.346 83.423 22.250 1.00 22.29 ? 166 PHE A CE2 1 ATOM 1306 C CZ . PHE A 1 166 ? 37.310 84.148 22.808 1.00 22.40 ? 166 PHE A CZ 1 ATOM 1307 N N . ILE A 1 167 ? 42.078 81.300 24.392 1.00 19.49 ? 167 ILE A N 1 ATOM 1308 C CA . ILE A 1 167 ? 41.901 79.983 23.791 1.00 20.27 ? 167 ILE A CA 1 ATOM 1309 C C . ILE A 1 167 ? 41.930 78.886 24.856 1.00 19.60 ? 167 ILE A C 1 ATOM 1310 O O . ILE A 1 167 ? 41.098 77.973 24.836 1.00 18.98 ? 167 ILE A O 1 ATOM 1311 C CB . ILE A 1 167 ? 42.945 79.725 22.666 1.00 19.41 ? 167 ILE A CB 1 ATOM 1312 C CG1 . ILE A 1 167 ? 42.689 80.723 21.521 1.00 20.99 ? 167 ILE A CG1 1 ATOM 1313 C CG2 . ILE A 1 167 ? 42.893 78.288 22.189 1.00 19.62 ? 167 ILE A CG2 1 ATOM 1314 C CD1 . ILE A 1 167 ? 43.668 80.688 20.361 1.00 20.55 ? 167 ILE A CD1 1 ATOM 1315 N N . GLU A 1 168 ? 42.888 78.970 25.767 1.00 20.07 ? 168 GLU A N 1 ATOM 1316 C CA . GLU A 1 168 ? 42.898 78.100 26.946 1.00 20.39 ? 168 GLU A CA 1 ATOM 1317 C C . GLU A 1 168 ? 41.501 78.063 27.618 1.00 20.61 ? 168 GLU A C 1 ATOM 1318 O O . GLU A 1 168 ? 40.943 77.000 27.930 1.00 20.34 ? 168 GLU A O 1 ATOM 1319 C CB . GLU A 1 168 ? 43.919 78.614 27.943 1.00 20.81 ? 168 GLU A CB 1 ATOM 1320 C CG . GLU A 1 168 ? 44.039 77.762 29.179 1.00 21.59 ? 168 GLU A CG 1 ATOM 1321 C CD . GLU A 1 168 ? 44.779 78.433 30.327 1.00 24.51 ? 168 GLU A CD 1 ATOM 1322 O OE1 . GLU A 1 168 ? 45.391 79.515 30.180 1.00 23.61 ? 168 GLU A OE1 1 ATOM 1323 O OE2 . GLU A 1 168 ? 44.738 77.824 31.408 1.00 28.36 ? 168 GLU A OE2 1 ATOM 1324 N N . GLN A 1 169 ? 40.960 79.245 27.840 1.00 21.50 ? 169 GLN A N 1 ATOM 1325 C CA . GLN A 1 169 ? 39.674 79.376 28.481 1.00 23.03 ? 169 GLN A CA 1 ATOM 1326 C C . GLN A 1 169 ? 38.527 78.767 27.654 1.00 23.17 ? 169 GLN A C 1 ATOM 1327 O O . GLN A 1 169 ? 37.585 78.177 28.223 1.00 21.53 ? 169 GLN A O 1 ATOM 1328 C CB . GLN A 1 169 ? 39.393 80.830 28.808 1.00 24.17 ? 169 GLN A CB 1 ATOM 1329 C CG . GLN A 1 169 ? 38.225 81.000 29.765 1.00 26.75 ? 169 GLN A CG 1 ATOM 1330 C CD . GLN A 1 169 ? 38.422 80.263 31.078 1.00 26.86 ? 169 GLN A CD 1 ATOM 1331 O OE1 . GLN A 1 169 ? 39.510 80.222 31.627 1.00 26.88 ? 169 GLN A OE1 1 ATOM 1332 N NE2 . GLN A 1 169 ? 37.363 79.660 31.562 1.00 31.20 ? 169 GLN A NE2 1 ATOM 1333 N N . LYS A 1 170 ? 38.606 78.878 26.331 1.00 22.61 ? 170 LYS A N 1 ATOM 1334 C CA . LYS A 1 170 ? 37.615 78.206 25.462 1.00 23.77 ? 170 LYS A CA 1 ATOM 1335 C C . LYS A 1 170 ? 37.619 76.708 25.690 1.00 23.06 ? 170 LYS A C 1 ATOM 1336 O O . LYS A 1 170 ? 36.567 76.079 25.758 1.00 23.01 ? 170 LYS A O 1 ATOM 1337 C CB . LYS A 1 170 ? 37.887 78.461 23.983 1.00 24.86 ? 170 LYS A CB 1 ATOM 1338 C CG . LYS A 1 170 ? 37.684 79.885 23.528 1.00 27.32 ? 170 LYS A CG 1 ATOM 1339 C CD . LYS A 1 170 ? 36.226 80.243 23.380 1.00 29.71 ? 170 LYS A CD 1 ATOM 1340 C CE . LYS A 1 170 ? 35.609 79.652 22.133 1.00 30.77 ? 170 LYS A CE 1 ATOM 1341 N NZ . LYS A 1 170 ? 34.164 79.994 22.142 1.00 32.22 ? 170 LYS A NZ 1 ATOM 1342 N N . VAL A 1 171 ? 38.815 76.135 25.793 1.00 20.60 ? 171 VAL A N 1 ATOM 1343 C CA . VAL A 1 171 ? 38.929 74.721 26.018 1.00 22.06 ? 171 VAL A CA 1 ATOM 1344 C C . VAL A 1 171 ? 38.377 74.373 27.419 1.00 22.90 ? 171 VAL A C 1 ATOM 1345 O O . VAL A 1 171 ? 37.707 73.351 27.585 1.00 21.47 ? 171 VAL A O 1 ATOM 1346 C CB . VAL A 1 171 ? 40.377 74.244 25.868 1.00 22.04 ? 171 VAL A CB 1 ATOM 1347 C CG1 . VAL A 1 171 ? 40.492 72.778 26.226 1.00 22.61 ? 171 VAL A CG1 1 ATOM 1348 C CG2 . VAL A 1 171 ? 40.851 74.467 24.430 1.00 22.55 ? 171 VAL A CG2 1 ATOM 1349 N N . ILE A 1 172 ? 38.673 75.220 28.406 1.00 21.68 ? 172 ILE A N 1 ATOM 1350 C CA . ILE A 1 172 ? 38.225 74.989 29.778 1.00 22.55 ? 172 ILE A CA 1 ATOM 1351 C C . ILE A 1 172 ? 36.712 74.996 29.837 1.00 24.37 ? 172 ILE A C 1 ATOM 1352 O O . ILE A 1 172 ? 36.122 74.145 30.502 1.00 24.82 ? 172 ILE A O 1 ATOM 1353 C CB . ILE A 1 172 ? 38.825 76.019 30.755 1.00 22.46 ? 172 ILE A CB 1 ATOM 1354 C CG1 . ILE A 1 172 ? 40.317 75.700 30.970 1.00 22.42 ? 172 ILE A CG1 1 ATOM 1355 C CG2 . ILE A 1 172 ? 38.035 76.081 32.084 1.00 23.04 ? 172 ILE A CG2 1 ATOM 1356 C CD1 . ILE A 1 172 ? 41.059 76.734 31.799 1.00 23.99 ? 172 ILE A CD1 1 ATOM 1357 N N . HIS A 1 173 ? 36.090 75.955 29.161 1.00 25.65 ? 173 HIS A N 1 ATOM 1358 C CA . HIS A 1 173 ? 34.642 75.968 29.047 1.00 26.78 ? 173 HIS A CA 1 ATOM 1359 C C . HIS A 1 173 ? 34.096 74.682 28.446 1.00 27.72 ? 173 HIS A C 1 ATOM 1360 O O . HIS A 1 173 ? 33.103 74.130 28.938 1.00 27.57 ? 173 HIS A O 1 ATOM 1361 C CB . HIS A 1 173 ? 34.173 77.166 28.240 1.00 28.97 ? 173 HIS A CB 1 ATOM 1362 C CG . HIS A 1 173 ? 34.216 78.457 28.988 1.00 30.55 ? 173 HIS A CG 1 ATOM 1363 N ND1 . HIS A 1 173 ? 34.582 79.646 28.397 1.00 32.32 ? 173 HIS A ND1 1 ATOM 1364 C CD2 . HIS A 1 173 ? 33.916 78.756 30.272 1.00 33.33 ? 173 HIS A CD2 1 ATOM 1365 C CE1 . HIS A 1 173 ? 34.510 80.621 29.283 1.00 32.27 ? 173 HIS A CE1 1 ATOM 1366 N NE2 . HIS A 1 173 ? 34.102 80.109 30.429 1.00 35.99 ? 173 HIS A NE2 1 ATOM 1367 N N . SER A 1 174 ? 34.739 74.207 27.390 1.00 26.84 ? 174 SER A N 1 ATOM 1368 C CA . SER A 1 174 ? 34.369 72.974 26.744 1.00 27.96 ? 174 SER A CA 1 ATOM 1369 C C . SER A 1 174 ? 34.388 71.758 27.695 1.00 30.22 ? 174 SER A C 1 ATOM 1370 O O . SER A 1 174 ? 33.444 70.943 27.692 1.00 27.55 ? 174 SER A O 1 ATOM 1371 C CB . SER A 1 174 ? 35.312 72.713 25.581 1.00 29.38 ? 174 SER A CB 1 ATOM 1372 O OG . SER A 1 174 ? 34.932 71.553 24.912 1.00 32.47 ? 174 SER A OG 1 ATOM 1373 N N . ILE A 1 175 ? 35.458 71.649 28.480 1.00 27.93 ? 175 ILE A N 1 ATOM 1374 C CA . ILE A 1 175 ? 35.612 70.571 29.448 1.00 31.01 ? 175 ILE A CA 1 ATOM 1375 C C . ILE A 1 175 ? 34.476 70.626 30.451 1.00 32.56 ? 175 ILE A C 1 ATOM 1376 O O . ILE A 1 175 ? 33.791 69.635 30.688 1.00 33.96 ? 175 ILE A O 1 ATOM 1377 C CB . ILE A 1 175 ? 36.935 70.680 30.238 1.00 30.78 ? 175 ILE A CB 1 ATOM 1378 C CG1 . ILE A 1 175 ? 38.115 70.459 29.305 1.00 30.52 ? 175 ILE A CG1 1 ATOM 1379 C CG2 . ILE A 1 175 ? 36.968 69.645 31.375 1.00 30.05 ? 175 ILE A CG2 1 ATOM 1380 C CD1 . ILE A 1 175 ? 39.435 70.941 29.862 1.00 31.26 ? 175 ILE A CD1 1 ATOM 1381 N N . MET A 1 176 ? 34.277 71.799 31.023 1.00 32.34 ? 176 MET A N 1 ATOM 1382 C CA . MET A 1 176 ? 33.324 71.975 32.108 1.00 33.30 ? 176 MET A CA 1 ATOM 1383 C C . MET A 1 176 ? 31.865 71.888 31.686 1.00 34.49 ? 176 MET A C 1 ATOM 1384 O O . MET A 1 176 ? 31.042 71.356 32.434 1.00 33.25 ? 176 MET A O 1 ATOM 1385 C CB . MET A 1 176 ? 33.577 73.307 32.780 1.00 33.06 ? 176 MET A CB 1 ATOM 1386 C CG . MET A 1 176 ? 34.881 73.271 33.531 1.00 36.72 ? 176 MET A CG 1 ATOM 1387 S SD . MET A 1 176 ? 35.182 74.749 34.488 1.00 37.07 ? 176 MET A SD 1 ATOM 1388 C CE . MET A 1 176 ? 33.982 74.553 35.811 1.00 37.39 ? 176 MET A CE 1 ATOM 1389 N N . ASP A 1 177 ? 31.548 72.431 30.517 1.00 31.75 ? 177 ASP A N 1 ATOM 1390 C CA . ASP A 1 177 ? 30.217 72.322 29.952 1.00 32.71 ? 177 ASP A CA 1 ATOM 1391 C C . ASP A 1 177 ? 29.972 70.963 29.301 1.00 32.86 ? 177 ASP A C 1 ATOM 1392 O O . ASP A 1 177 ? 28.833 70.657 28.987 1.00 36.31 ? 177 ASP A O 1 ATOM 1393 C CB . ASP A 1 177 ? 29.979 73.428 28.913 1.00 33.99 ? 177 ASP A CB 1 ATOM 1394 C CG . ASP A 1 177 ? 30.038 74.828 29.499 1.00 34.77 ? 177 ASP A CG 1 ATOM 1395 O OD1 . ASP A 1 177 ? 30.006 74.965 30.721 1.00 37.87 ? 177 ASP A OD1 1 ATOM 1396 O OD2 . ASP A 1 177 ? 30.112 75.821 28.736 1.00 36.31 ? 177 ASP A OD2 1 ATOM 1397 N N . MET A 1 178 ? 31.024 70.164 29.096 1.00 33.11 ? 178 MET A N 1 ATOM 1398 C CA . MET A 1 178 ? 30.981 68.905 28.342 1.00 36.88 ? 178 MET A CA 1 ATOM 1399 C C . MET A 1 178 ? 30.339 69.138 26.990 1.00 35.96 ? 178 MET A C 1 ATOM 1400 O O . MET A 1 178 ? 29.328 68.551 26.643 1.00 34.45 ? 178 MET A O 1 ATOM 1401 C CB . MET A 1 178 ? 30.274 67.797 29.131 1.00 41.26 ? 178 MET A CB 1 ATOM 1402 C CG . MET A 1 178 ? 31.068 67.367 30.352 1.00 45.64 ? 178 MET A CG 1 ATOM 1403 S SD . MET A 1 178 ? 30.493 65.802 31.026 1.00 57.21 ? 178 MET A SD 1 ATOM 1404 C CE . MET A 1 178 ? 31.755 64.673 30.422 1.00 56.07 ? 178 MET A CE 1 ATOM 1405 N N . GLU A 1 179 ? 30.949 70.049 26.249 1.00 34.73 ? 179 GLU A N 1 ATOM 1406 C CA . GLU A 1 179 ? 30.336 70.640 25.086 1.00 35.39 ? 179 GLU A CA 1 ATOM 1407 C C . GLU A 1 179 ? 31.422 71.023 24.100 1.00 34.08 ? 179 GLU A C 1 ATOM 1408 O O . GLU A 1 179 ? 32.287 71.844 24.404 1.00 30.68 ? 179 GLU A O 1 ATOM 1409 C CB . GLU A 1 179 ? 29.555 71.865 25.523 1.00 38.45 ? 179 GLU A CB 1 ATOM 1410 C CG . GLU A 1 179 ? 28.598 72.398 24.500 1.00 44.92 ? 179 GLU A CG 1 ATOM 1411 C CD . GLU A 1 179 ? 27.645 73.396 25.128 1.00 49.80 ? 179 GLU A CD 1 ATOM 1412 O OE1 . GLU A 1 179 ? 26.778 72.965 25.923 1.00 55.02 ? 179 GLU A OE1 1 ATOM 1413 O OE2 . GLU A 1 179 ? 27.779 74.603 24.850 1.00 53.09 ? 179 GLU A OE2 1 ATOM 1414 N N . ASP A 1 180 ? 31.375 70.402 22.928 1.00 32.29 ? 180 ASP A N 1 ATOM 1415 C CA . ASP A 1 180 ? 32.315 70.688 21.866 1.00 33.21 ? 180 ASP A CA 1 ATOM 1416 C C . ASP A 1 180 ? 32.057 72.058 21.302 1.00 30.19 ? 180 ASP A C 1 ATOM 1417 O O . ASP A 1 180 ? 31.000 72.629 21.496 1.00 30.37 ? 180 ASP A O 1 ATOM 1418 C CB . ASP A 1 180 ? 32.162 69.661 20.755 1.00 36.89 ? 180 ASP A CB 1 ATOM 1419 C CG . ASP A 1 180 ? 32.526 68.285 21.197 1.00 41.59 ? 180 ASP A CG 1 ATOM 1420 O OD1 . ASP A 1 180 ? 33.254 68.141 22.217 1.00 44.92 ? 180 ASP A OD1 1 ATOM 1421 O OD2 . ASP A 1 180 ? 32.085 67.338 20.505 1.00 46.75 ? 180 ASP A OD2 1 ATOM 1422 N N . PHE A 1 181 ? 33.038 72.595 20.604 1.00 28.49 ? 181 PHE A N 1 ATOM 1423 C CA . PHE A 1 181 ? 32.880 73.891 19.950 1.00 27.17 ? 181 PHE A CA 1 ATOM 1424 C C . PHE A 1 181 ? 33.769 73.932 18.713 1.00 25.28 ? 181 PHE A C 1 ATOM 1425 O O . PHE A 1 181 ? 34.683 73.138 18.576 1.00 24.17 ? 181 PHE A O 1 ATOM 1426 C CB . PHE A 1 181 ? 33.240 75.018 20.926 1.00 26.87 ? 181 PHE A CB 1 ATOM 1427 C CG . PHE A 1 181 ? 34.723 75.098 21.249 1.00 26.91 ? 181 PHE A CG 1 ATOM 1428 C CD1 . PHE A 1 181 ? 35.313 74.181 22.130 1.00 26.90 ? 181 PHE A CD1 1 ATOM 1429 C CD2 . PHE A 1 181 ? 35.528 76.082 20.674 1.00 25.86 ? 181 PHE A CD2 1 ATOM 1430 C CE1 . PHE A 1 181 ? 36.667 74.241 22.435 1.00 26.83 ? 181 PHE A CE1 1 ATOM 1431 C CE2 . PHE A 1 181 ? 36.896 76.141 20.969 1.00 25.92 ? 181 PHE A CE2 1 ATOM 1432 C CZ . PHE A 1 181 ? 37.465 75.221 21.845 1.00 25.70 ? 181 PHE A CZ 1 ATOM 1433 N N . THR A 1 182 ? 33.479 74.850 17.803 1.00 25.61 ? 182 THR A N 1 ATOM 1434 C CA . THR A 1 182 ? 34.382 75.149 16.707 1.00 26.02 ? 182 THR A CA 1 ATOM 1435 C C . THR A 1 182 ? 34.849 76.571 16.945 1.00 25.36 ? 182 THR A C 1 ATOM 1436 O O . THR A 1 182 ? 34.075 77.386 17.443 1.00 26.41 ? 182 THR A O 1 ATOM 1437 C CB . THR A 1 182 ? 33.700 75.032 15.344 1.00 27.12 ? 182 THR A CB 1 ATOM 1438 O OG1 . THR A 1 182 ? 32.493 75.787 15.362 1.00 27.79 ? 182 THR A OG1 1 ATOM 1439 C CG2 . THR A 1 182 ? 33.375 73.574 15.055 1.00 27.88 ? 182 THR A CG2 1 ATOM 1440 N N . PRO A 1 183 ? 36.109 76.871 16.612 1.00 24.33 ? 183 PRO A N 1 ATOM 1441 C CA . PRO A 1 183 ? 36.592 78.230 16.838 1.00 25.04 ? 183 PRO A CA 1 ATOM 1442 C C . PRO A 1 183 ? 35.832 79.223 15.985 1.00 26.31 ? 183 PRO A C 1 ATOM 1443 O O . PRO A 1 183 ? 35.581 78.942 14.804 1.00 26.51 ? 183 PRO A O 1 ATOM 1444 C CB . PRO A 1 183 ? 38.053 78.174 16.371 1.00 25.07 ? 183 PRO A CB 1 ATOM 1445 C CG . PRO A 1 183 ? 38.100 77.041 15.415 1.00 25.52 ? 183 PRO A CG 1 ATOM 1446 C CD . PRO A 1 183 ? 37.126 76.025 15.959 1.00 24.08 ? 183 PRO A CD 1 ATOM 1447 N N . GLY A 1 184 ? 35.482 80.352 16.586 1.00 25.61 ? 184 GLY A N 1 ATOM 1448 C CA . GLY A 1 184 ? 34.850 81.448 15.889 1.00 26.03 ? 184 GLY A CA 1 ATOM 1449 C C . GLY A 1 184 ? 35.896 82.475 15.559 1.00 25.44 ? 184 GLY A C 1 ATOM 1450 O O . GLY A 1 184 ? 37.105 82.214 15.698 1.00 24.55 ? 184 GLY A O 1 ATOM 1451 N N . LEU A 1 185 ? 35.432 83.642 15.131 1.00 24.27 ? 185 LEU A N 1 ATOM 1452 C CA . LEU A 1 185 ? 36.321 84.727 14.727 1.00 23.46 ? 185 LEU A CA 1 ATOM 1453 C C . LEU A 1 185 ? 37.287 85.188 15.815 1.00 22.17 ? 185 LEU A C 1 ATOM 1454 O O . LEU A 1 185 ? 38.398 85.575 15.487 1.00 20.33 ? 185 LEU A O 1 ATOM 1455 C CB . LEU A 1 185 ? 35.521 85.922 14.212 1.00 24.58 ? 185 LEU A CB 1 ATOM 1456 C CG . LEU A 1 185 ? 34.725 85.664 12.915 1.00 26.32 ? 185 LEU A CG 1 ATOM 1457 C CD1 . LEU A 1 185 ? 33.926 86.889 12.508 1.00 26.01 ? 185 LEU A CD1 1 ATOM 1458 C CD2 . LEU A 1 185 ? 35.627 85.264 11.772 1.00 26.55 ? 185 LEU A CD2 1 ATOM 1459 N N . ALA A 1 186 ? 36.846 85.184 17.077 1.00 21.11 ? 186 ALA A N 1 ATOM 1460 C CA . ALA A 1 186 ? 37.709 85.588 18.194 1.00 21.60 ? 186 ALA A CA 1 ATOM 1461 C C . ALA A 1 186 ? 38.955 84.710 18.261 1.00 20.75 ? 186 ALA A C 1 ATOM 1462 O O . ALA A 1 186 ? 40.088 85.205 18.229 1.00 21.57 ? 186 ALA A O 1 ATOM 1463 C CB . ALA A 1 186 ? 36.944 85.537 19.510 1.00 21.59 ? 186 ALA A CB 1 ATOM 1464 N N . MET A 1 187 ? 38.733 83.405 18.291 1.00 21.01 ? 187 MET A N 1 ATOM 1465 C CA . MET A 1 187 ? 39.823 82.464 18.377 1.00 21.75 ? 187 MET A CA 1 ATOM 1466 C C . MET A 1 187 ? 40.706 82.479 17.109 1.00 22.70 ? 187 MET A C 1 ATOM 1467 O O . MET A 1 187 ? 41.933 82.537 17.204 1.00 22.05 ? 187 MET A O 1 ATOM 1468 C CB . MET A 1 187 ? 39.261 81.084 18.697 1.00 22.91 ? 187 MET A CB 1 ATOM 1469 C CG . MET A 1 187 ? 40.287 79.983 18.748 1.00 24.56 ? 187 MET A CG 1 ATOM 1470 S SD . MET A 1 187 ? 39.671 78.610 19.731 1.00 24.98 ? 187 MET A SD 1 ATOM 1471 C CE . MET A 1 187 ? 40.874 77.361 19.309 1.00 23.57 ? 187 MET A CE 1 ATOM 1472 N N . LEU A 1 188 ? 40.084 82.467 15.931 1.00 22.65 ? 188 LEU A N 1 ATOM 1473 C CA . LEU A 1 188 ? 40.838 82.485 14.680 1.00 22.89 ? 188 LEU A CA 1 ATOM 1474 C C . LEU A 1 188 ? 41.665 83.759 14.503 1.00 22.27 ? 188 LEU A C 1 ATOM 1475 O O . LEU A 1 188 ? 42.798 83.685 14.037 1.00 21.20 ? 188 LEU A O 1 ATOM 1476 C CB . LEU A 1 188 ? 39.917 82.259 13.485 1.00 23.80 ? 188 LEU A CB 1 ATOM 1477 C CG . LEU A 1 188 ? 39.167 80.918 13.443 1.00 25.11 ? 188 LEU A CG 1 ATOM 1478 C CD1 . LEU A 1 188 ? 38.214 80.910 12.264 1.00 27.88 ? 188 LEU A CD1 1 ATOM 1479 C CD2 . LEU A 1 188 ? 40.080 79.706 13.374 1.00 26.58 ? 188 LEU A CD2 1 ATOM 1480 N N . SER A 1 189 ? 41.138 84.909 14.925 1.00 21.11 ? 189 SER A N 1 ATOM 1481 C CA . SER A 1 189 ? 41.866 86.166 14.776 1.00 20.13 ? 189 SER A CA 1 ATOM 1482 C C . SER A 1 189 ? 43.130 86.225 15.655 1.00 19.98 ? 189 SER A C 1 ATOM 1483 O O . SER A 1 189 ? 44.132 86.804 15.267 1.00 19.80 ? 189 SER A O 1 ATOM 1484 C CB . SER A 1 189 ? 40.966 87.379 15.026 1.00 21.40 ? 189 SER A CB 1 ATOM 1485 O OG . SER A 1 189 ? 40.541 87.475 16.382 1.00 20.21 ? 189 SER A OG 1 ATOM 1486 N N . LEU A 1 190 ? 43.089 85.583 16.822 1.00 19.75 ? 190 LEU A N 1 ATOM 1487 C CA . LEU A 1 190 ? 44.275 85.409 17.641 1.00 18.98 ? 190 LEU A CA 1 ATOM 1488 C C . LEU A 1 190 ? 45.336 84.524 16.952 1.00 18.84 ? 190 LEU A C 1 ATOM 1489 O O . LEU A 1 190 ? 46.487 84.933 16.784 1.00 17.43 ? 190 LEU A O 1 ATOM 1490 C CB . LEU A 1 190 ? 43.878 84.821 18.990 1.00 19.61 ? 190 LEU A CB 1 ATOM 1491 C CG . LEU A 1 190 ? 42.996 85.734 19.864 1.00 19.62 ? 190 LEU A CG 1 ATOM 1492 C CD1 . LEU A 1 190 ? 42.478 84.946 21.054 1.00 20.16 ? 190 LEU A CD1 1 ATOM 1493 C CD2 . LEU A 1 190 ? 43.747 86.983 20.297 1.00 18.67 ? 190 LEU A CD2 1 ATOM 1494 N N . GLU A 1 191 ? 44.908 83.347 16.528 1.00 19.15 ? 191 GLU A N 1 ATOM 1495 C CA . GLU A 1 191 ? 45.777 82.396 15.827 1.00 21.51 ? 191 GLU A CA 1 ATOM 1496 C C . GLU A 1 191 ? 46.430 83.051 14.594 1.00 22.86 ? 191 GLU A C 1 ATOM 1497 O O . GLU A 1 191 ? 47.648 83.022 14.433 1.00 22.43 ? 191 GLU A O 1 ATOM 1498 C CB . GLU A 1 191 ? 44.961 81.183 15.389 1.00 21.91 ? 191 GLU A CB 1 ATOM 1499 C CG . GLU A 1 191 ? 44.392 80.339 16.529 1.00 22.50 ? 191 GLU A CG 1 ATOM 1500 C CD . GLU A 1 191 ? 43.566 79.154 16.043 1.00 22.93 ? 191 GLU A CD 1 ATOM 1501 O OE1 . GLU A 1 191 ? 43.546 78.860 14.839 1.00 24.25 ? 191 GLU A OE1 1 ATOM 1502 O OE2 . GLU A 1 191 ? 42.964 78.493 16.885 1.00 23.80 ? 191 GLU A OE2 1 ATOM 1503 N N . GLU A 1 192 ? 45.597 83.706 13.780 1.00 22.48 ? 192 GLU A N 1 ATOM 1504 C CA . GLU A 1 192 ? 46.020 84.437 12.585 1.00 23.91 ? 192 GLU A CA 1 ATOM 1505 C C . GLU A 1 192 ? 47.104 85.477 12.891 1.00 22.23 ? 192 GLU A C 1 ATOM 1506 O O . GLU A 1 192 ? 48.029 85.620 12.130 1.00 22.74 ? 192 GLU A O 1 ATOM 1507 C CB . GLU A 1 192 ? 44.787 85.131 11.968 1.00 27.51 ? 192 GLU A CB 1 ATOM 1508 C CG . GLU A 1 192 ? 45.034 86.118 10.821 1.00 31.66 ? 192 GLU A CG 1 ATOM 1509 C CD . GLU A 1 192 ? 43.923 87.172 10.638 1.00 33.98 ? 192 GLU A CD 1 ATOM 1510 O OE1 . GLU A 1 192 ? 42.894 87.205 11.377 1.00 34.35 ? 192 GLU A OE1 1 ATOM 1511 O OE2 . GLU A 1 192 ? 44.108 88.028 9.750 1.00 38.86 ? 192 GLU A OE2 1 ATOM 1512 N N . ASN A 1 193 ? 46.966 86.199 13.990 1.00 21.23 ? 193 ASN A N 1 ATOM 1513 C CA . ASN A 1 193 ? 47.800 87.373 14.275 1.00 21.92 ? 193 ASN A CA 1 ATOM 1514 C C . ASN A 1 193 ? 48.933 87.240 15.288 1.00 21.66 ? 193 ASN A C 1 ATOM 1515 O O . ASN A 1 193 ? 49.575 88.230 15.620 1.00 20.95 ? 193 ASN A O 1 ATOM 1516 C CB . ASN A 1 193 ? 46.885 88.524 14.679 1.00 22.45 ? 193 ASN A CB 1 ATOM 1517 C CG . ASN A 1 193 ? 46.167 89.112 13.480 1.00 23.32 ? 193 ASN A CG 1 ATOM 1518 O OD1 . ASN A 1 193 ? 46.793 89.761 12.661 1.00 23.30 ? 193 ASN A OD1 1 ATOM 1519 N ND2 . ASN A 1 193 ? 44.880 88.880 13.370 1.00 23.70 ? 193 ASN A ND2 1 ATOM 1520 N N . TRP A 1 194 ? 49.182 86.036 15.784 1.00 20.88 ? 194 TRP A N 1 ATOM 1521 C CA . TRP A 1 194 ? 50.219 85.853 16.792 1.00 21.97 ? 194 TRP A CA 1 ATOM 1522 C C . TRP A 1 194 ? 51.581 86.449 16.366 1.00 21.53 ? 194 TRP A C 1 ATOM 1523 O O . TRP A 1 194 ? 52.183 87.194 17.132 1.00 21.08 ? 194 TRP A O 1 ATOM 1524 C CB . TRP A 1 194 ? 50.367 84.375 17.153 1.00 21.59 ? 194 TRP A CB 1 ATOM 1525 C CG . TRP A 1 194 ? 51.365 84.112 18.199 1.00 22.40 ? 194 TRP A CG 1 ATOM 1526 C CD1 . TRP A 1 194 ? 51.287 84.465 19.515 1.00 24.28 ? 194 TRP A CD1 1 ATOM 1527 C CD2 . TRP A 1 194 ? 52.596 83.403 18.045 1.00 22.53 ? 194 TRP A CD2 1 ATOM 1528 N NE1 . TRP A 1 194 ? 52.410 84.023 20.187 1.00 23.41 ? 194 TRP A NE1 1 ATOM 1529 C CE2 . TRP A 1 194 ? 53.228 83.375 19.303 1.00 23.37 ? 194 TRP A CE2 1 ATOM 1530 C CE3 . TRP A 1 194 ? 53.231 82.788 16.959 1.00 23.76 ? 194 TRP A CE3 1 ATOM 1531 C CZ2 . TRP A 1 194 ? 54.483 82.755 19.506 1.00 23.37 ? 194 TRP A CZ2 1 ATOM 1532 C CZ3 . TRP A 1 194 ? 54.475 82.157 17.165 1.00 23.33 ? 194 TRP A CZ3 1 ATOM 1533 C CH2 . TRP A 1 194 ? 55.074 82.146 18.425 1.00 23.09 ? 194 TRP A CH2 1 ATOM 1534 N N . THR A 1 195 ? 52.021 86.159 15.146 1.00 21.04 ? 195 THR A N 1 ATOM 1535 C CA . THR A 1 195 ? 53.317 86.676 14.690 1.00 22.93 ? 195 THR A CA 1 ATOM 1536 C C . THR A 1 195 ? 53.259 88.205 14.501 1.00 22.54 ? 195 THR A C 1 ATOM 1537 O O . THR A 1 195 ? 54.211 88.914 14.868 1.00 22.11 ? 195 THR A O 1 ATOM 1538 C CB . THR A 1 195 ? 53.869 85.955 13.420 1.00 23.59 ? 195 THR A CB 1 ATOM 1539 O OG1 . THR A 1 195 ? 53.028 86.203 12.299 1.00 25.50 ? 195 THR A OG1 1 ATOM 1540 C CG2 . THR A 1 195 ? 53.947 84.480 13.635 1.00 23.91 ? 195 THR A CG2 1 ATOM 1541 N N . GLN A 1 196 ? 52.146 88.706 13.966 1.00 22.61 ? 196 GLN A N 1 ATOM 1542 C CA . GLN A 1 196 ? 51.985 90.164 13.764 1.00 23.55 ? 196 GLN A CA 1 ATOM 1543 C C . GLN A 1 196 ? 51.903 90.926 15.106 1.00 21.39 ? 196 GLN A C 1 ATOM 1544 O O . GLN A 1 196 ? 52.512 91.971 15.248 1.00 20.65 ? 196 GLN A O 1 ATOM 1545 C CB . GLN A 1 196 ? 50.801 90.471 12.844 1.00 25.49 ? 196 GLN A CB 1 ATOM 1546 C CG . GLN A 1 196 ? 50.388 91.948 12.744 1.00 27.72 ? 196 GLN A CG 1 ATOM 1547 C CD . GLN A 1 196 ? 51.320 92.807 11.886 1.00 30.96 ? 196 GLN A CD 1 ATOM 1548 O OE1 . GLN A 1 196 ? 52.522 92.591 11.829 1.00 33.16 ? 196 GLN A OE1 1 ATOM 1549 N NE2 . GLN A 1 196 ? 50.756 93.809 11.235 1.00 33.78 ? 196 GLN A NE2 1 ATOM 1550 N N . LEU A 1 197 ? 51.173 90.389 16.088 1.00 21.25 ? 197 LEU A N 1 ATOM 1551 C CA . LEU A 1 197 ? 51.130 90.982 17.434 1.00 20.80 ? 197 LEU A CA 1 ATOM 1552 C C . LEU A 1 197 ? 52.531 90.999 18.077 1.00 20.45 ? 197 LEU A C 1 ATOM 1553 O O . LEU A 1 197 ? 52.900 91.961 18.740 1.00 18.74 ? 197 LEU A O 1 ATOM 1554 C CB . LEU A 1 197 ? 50.143 90.220 18.341 1.00 22.24 ? 197 LEU A CB 1 ATOM 1555 C CG . LEU A 1 197 ? 48.674 90.346 17.958 1.00 22.20 ? 197 LEU A CG 1 ATOM 1556 C CD1 . LEU A 1 197 ? 47.887 89.231 18.617 1.00 22.89 ? 197 LEU A CD1 1 ATOM 1557 C CD2 . LEU A 1 197 ? 48.130 91.721 18.313 1.00 23.51 ? 197 LEU A CD2 1 ATOM 1558 N N . SER A 1 198 ? 53.304 89.929 17.852 1.00 20.17 ? 198 SER A N 1 ATOM 1559 C CA . SER A 1 198 ? 54.677 89.833 18.373 1.00 19.99 ? 198 SER A CA 1 ATOM 1560 C C . SER A 1 198 ? 55.533 90.953 17.788 1.00 19.75 ? 198 SER A C 1 ATOM 1561 O O . SER A 1 198 ? 56.262 91.633 18.504 1.00 20.21 ? 198 SER A O 1 ATOM 1562 C CB . SER A 1 198 ? 55.306 88.461 18.037 1.00 20.73 ? 198 SER A CB 1 ATOM 1563 O OG . SER A 1 198 ? 54.591 87.372 18.633 1.00 19.84 ? 198 SER A OG 1 ATOM 1564 N N . LEU A 1 199 ? 55.420 91.140 16.488 1.00 19.70 ? 199 LEU A N 1 ATOM 1565 C CA . LEU A 1 199 ? 56.157 92.185 15.790 1.00 22.04 ? 199 LEU A CA 1 ATOM 1566 C C . LEU A 1 199 ? 55.746 93.581 16.307 1.00 20.97 ? 199 LEU A C 1 ATOM 1567 O O . LEU A 1 199 ? 56.601 94.363 16.734 1.00 20.44 ? 199 LEU A O 1 ATOM 1568 C CB . LEU A 1 199 ? 55.926 92.085 14.287 1.00 23.63 ? 199 LEU A CB 1 ATOM 1569 C CG . LEU A 1 199 ? 56.446 93.255 13.433 1.00 25.04 ? 199 LEU A CG 1 ATOM 1570 C CD1 . LEU A 1 199 ? 57.947 93.417 13.632 1.00 27.52 ? 199 LEU A CD1 1 ATOM 1571 C CD2 . LEU A 1 199 ? 56.091 93.048 11.976 1.00 25.46 ? 199 LEU A CD2 1 ATOM 1572 N N . GLN A 1 200 ? 54.445 93.848 16.348 1.00 21.53 ? 200 GLN A N 1 ATOM 1573 C CA . GLN A 1 200 ? 53.977 95.185 16.772 1.00 22.57 ? 200 GLN A CA 1 ATOM 1574 C C . GLN A 1 200 ? 54.313 95.512 18.236 1.00 21.78 ? 200 GLN A C 1 ATOM 1575 O O . GLN A 1 200 ? 54.782 96.596 18.534 1.00 21.87 ? 200 GLN A O 1 ATOM 1576 C CB . GLN A 1 200 ? 52.492 95.372 16.485 1.00 22.70 ? 200 GLN A CB 1 ATOM 1577 C CG . GLN A 1 200 ? 52.103 95.247 15.028 1.00 23.83 ? 200 GLN A CG 1 ATOM 1578 C CD . GLN A 1 200 ? 52.890 96.161 14.105 1.00 25.98 ? 200 GLN A CD 1 ATOM 1579 O OE1 . GLN A 1 200 ? 53.259 97.270 14.470 1.00 26.23 ? 200 GLN A OE1 1 ATOM 1580 N NE2 . GLN A 1 200 ? 53.163 95.688 12.911 1.00 28.61 ? 200 GLN A NE2 1 ATOM 1581 N N . LEU A 1 201 ? 54.151 94.551 19.136 1.00 23.46 ? 201 LEU A N 1 ATOM 1582 C CA . LEU A 1 201 ? 54.531 94.748 20.541 1.00 23.98 ? 201 LEU A CA 1 ATOM 1583 C C . LEU A 1 201 ? 55.994 95.148 20.700 1.00 23.76 ? 201 LEU A C 1 ATOM 1584 O O . LEU A 1 201 ? 56.316 96.112 21.393 1.00 21.56 ? 201 LEU A O 1 ATOM 1585 C CB . LEU A 1 201 ? 54.289 93.496 21.369 1.00 24.50 ? 201 LEU A CB 1 ATOM 1586 C CG . LEU A 1 201 ? 52.878 93.278 21.864 1.00 27.24 ? 201 LEU A CG 1 ATOM 1587 C CD1 . LEU A 1 201 ? 52.678 91.820 22.286 1.00 27.86 ? 201 LEU A CD1 1 ATOM 1588 C CD2 . LEU A 1 201 ? 52.562 94.255 22.996 1.00 27.88 ? 201 LEU A CD2 1 ATOM 1589 N N . GLN A 1 202 ? 56.867 94.381 20.047 1.00 23.16 ? 202 GLN A N 1 ATOM 1590 C CA . GLN A 1 202 ? 58.291 94.634 20.109 1.00 23.57 ? 202 GLN A CA 1 ATOM 1591 C C . GLN A 1 202 ? 58.649 95.952 19.425 1.00 22.72 ? 202 GLN A C 1 ATOM 1592 O O . GLN A 1 202 ? 59.369 96.731 19.982 1.00 25.07 ? 202 GLN A O 1 ATOM 1593 C CB . GLN A 1 202 ? 59.053 93.432 19.541 1.00 22.94 ? 202 GLN A CB 1 ATOM 1594 C CG . GLN A 1 202 ? 58.964 92.245 20.525 1.00 23.94 ? 202 GLN A CG 1 ATOM 1595 C CD . GLN A 1 202 ? 59.348 90.906 19.906 1.00 23.88 ? 202 GLN A CD 1 ATOM 1596 O OE1 . GLN A 1 202 ? 60.456 90.741 19.427 1.00 24.28 ? 202 GLN A OE1 1 ATOM 1597 N NE2 . GLN A 1 202 ? 58.424 89.954 19.902 1.00 23.39 ? 202 GLN A NE2 1 ATOM 1598 N N . ALA A 1 203 ? 58.095 96.200 18.250 1.00 23.15 ? 203 ALA A N 1 ATOM 1599 C CA . ALA A 1 203 ? 58.311 97.462 17.541 1.00 24.04 ? 203 ALA A CA 1 ATOM 1600 C C . ALA A 1 203 ? 57.816 98.672 18.339 1.00 25.86 ? 203 ALA A C 1 ATOM 1601 O O . ALA A 1 203 ? 58.427 99.731 18.288 1.00 26.33 ? 203 ALA A O 1 ATOM 1602 C CB . ALA A 1 203 ? 57.627 97.427 16.197 1.00 24.26 ? 203 ALA A CB 1 ATOM 1603 N N . SER A 1 204 ? 56.733 98.502 19.092 1.00 25.06 ? 204 SER A N 1 ATOM 1604 C CA . SER A 1 204 ? 56.139 99.601 19.853 1.00 25.52 ? 204 SER A CA 1 ATOM 1605 C C . SER A 1 204 ? 57.009 100.202 20.946 1.00 27.00 ? 204 SER A C 1 ATOM 1606 O O . SER A 1 204 ? 56.672 101.258 21.456 1.00 27.18 ? 204 SER A O 1 ATOM 1607 C CB . SER A 1 204 ? 54.831 99.169 20.489 1.00 24.96 ? 204 SER A CB 1 ATOM 1608 O OG . SER A 1 204 ? 55.030 98.366 21.636 1.00 23.39 ? 204 SER A OG 1 ATOM 1609 N N . GLU A 1 205 ? 58.102 99.527 21.316 1.00 29.52 ? 205 GLU A N 1 ATOM 1610 C CA . GLU A 1 205 ? 59.083 100.048 22.271 1.00 31.08 ? 205 GLU A CA 1 ATOM 1611 C C . GLU A 1 205 ? 59.610 101.436 21.891 1.00 30.63 ? 205 GLU A C 1 ATOM 1612 O O . GLU A 1 205 ? 59.920 102.218 22.767 1.00 31.63 ? 205 GLU A O 1 ATOM 1613 C CB . GLU A 1 205 ? 60.297 99.099 22.390 1.00 33.64 ? 205 GLU A CB 1 ATOM 1614 C CG . GLU A 1 205 ? 60.020 97.708 22.950 1.00 35.09 ? 205 GLU A CG 1 ATOM 1615 C CD . GLU A 1 205 ? 59.877 97.662 24.461 1.00 37.57 ? 205 GLU A CD 1 ATOM 1616 O OE1 . GLU A 1 205 ? 60.063 98.696 25.151 1.00 38.69 ? 205 GLU A OE1 1 ATOM 1617 O OE2 . GLU A 1 205 ? 59.560 96.568 24.982 1.00 36.00 ? 205 GLU A OE2 1 ATOM 1618 N N . SER A 1 206 ? 59.735 101.714 20.598 1.00 29.75 ? 206 SER A N 1 ATOM 1619 C CA . SER A 1 206 ? 60.217 103.011 20.116 1.00 30.36 ? 206 SER A CA 1 ATOM 1620 C C . SER A 1 206 ? 59.118 104.078 19.951 1.00 29.24 ? 206 SER A C 1 ATOM 1621 O O . SER A 1 206 ? 59.436 105.212 19.636 1.00 29.49 ? 206 SER A O 1 ATOM 1622 C CB . SER A 1 206 ? 60.927 102.821 18.775 1.00 31.09 ? 206 SER A CB 1 ATOM 1623 O OG . SER A 1 206 ? 60.036 102.245 17.818 1.00 31.21 ? 206 SER A OG 1 ATOM 1624 N N . LEU A 1 207 ? 57.846 103.719 20.139 1.00 27.67 ? 207 LEU A N 1 ATOM 1625 C CA . LEU A 1 207 ? 56.729 104.631 19.926 1.00 26.56 ? 207 LEU A CA 1 ATOM 1626 C C . LEU A 1 207 ? 55.816 104.684 21.122 1.00 25.37 ? 207 LEU A C 1 ATOM 1627 O O . LEU A 1 207 ? 54.605 104.749 20.941 1.00 24.99 ? 207 LEU A O 1 ATOM 1628 C CB . LEU A 1 207 ? 55.886 104.206 18.717 1.00 28.45 ? 207 LEU A CB 1 ATOM 1629 C CG . LEU A 1 207 ? 56.090 104.715 17.294 1.00 32.19 ? 207 LEU A CG 1 ATOM 1630 C CD1 . LEU A 1 207 ? 54.831 104.460 16.471 1.00 31.86 ? 207 LEU A CD1 1 ATOM 1631 C CD2 . LEU A 1 207 ? 56.476 106.184 17.243 1.00 32.04 ? 207 LEU A CD2 1 ATOM 1632 N N . ASN A 1 208 ? 56.371 104.697 22.334 1.00 24.66 ? 208 ASN A N 1 ATOM 1633 C CA . ASN A 1 208 ? 55.565 104.796 23.554 1.00 24.72 ? 208 ASN A CA 1 ATOM 1634 C C . ASN A 1 208 ? 54.414 103.782 23.629 1.00 24.84 ? 208 ASN A C 1 ATOM 1635 O O . ASN A 1 208 ? 53.332 104.072 24.155 1.00 24.91 ? 208 ASN A O 1 ATOM 1636 C CB . ASN A 1 208 ? 55.040 106.239 23.719 1.00 25.18 ? 208 ASN A CB 1 ATOM 1637 C CG . ASN A 1 208 ? 55.904 107.067 24.635 1.00 24.68 ? 208 ASN A CG 1 ATOM 1638 O OD1 . ASN A 1 208 ? 56.288 106.610 25.704 1.00 25.30 ? 208 ASN A OD1 1 ATOM 1639 N ND2 . ASN A 1 208 ? 56.202 108.288 24.239 1.00 26.06 ? 208 ASN A ND2 1 ATOM 1640 N N . GLY A 1 209 ? 54.670 102.577 23.112 1.00 24.24 ? 209 GLY A N 1 ATOM 1641 C CA . GLY A 1 209 ? 53.714 101.472 23.211 1.00 24.05 ? 209 GLY A CA 1 ATOM 1642 C C . GLY A 1 209 ? 52.669 101.436 22.134 1.00 22.71 ? 209 GLY A C 1 ATOM 1643 O O . GLY A 1 209 ? 51.787 100.597 22.172 1.00 23.56 ? 209 GLY A O 1 ATOM 1644 N N . VAL A 1 210 ? 52.803 102.307 21.136 1.00 22.18 ? 210 VAL A N 1 ATOM 1645 C CA . VAL A 1 210 ? 51.890 102.363 20.013 1.00 21.92 ? 210 VAL A CA 1 ATOM 1646 C C . VAL A 1 210 ? 52.479 101.515 18.872 1.00 21.54 ? 210 VAL A C 1 ATOM 1647 O O . VAL A 1 210 ? 53.673 101.535 18.646 1.00 21.75 ? 210 VAL A O 1 ATOM 1648 C CB . VAL A 1 210 ? 51.697 103.823 19.567 1.00 23.14 ? 210 VAL A CB 1 ATOM 1649 C CG1 . VAL A 1 210 ? 50.798 103.943 18.335 1.00 23.64 ? 210 VAL A CG1 1 ATOM 1650 C CG2 . VAL A 1 210 ? 51.113 104.646 20.721 1.00 23.67 ? 210 VAL A CG2 1 ATOM 1651 N N . PHE A 1 211 ? 51.614 100.817 18.159 1.00 21.33 ? 211 PHE A N 1 ATOM 1652 C CA . PHE A 1 211 ? 51.983 99.926 17.069 1.00 21.52 ? 211 PHE A CA 1 ATOM 1653 C C . PHE A 1 211 ? 52.213 100.703 15.764 1.00 23.49 ? 211 PHE A C 1 ATOM 1654 O O . PHE A 1 211 ? 51.650 101.791 15.562 1.00 23.41 ? 211 PHE A O 1 ATOM 1655 C CB . PHE A 1 211 ? 50.839 98.940 16.820 1.00 21.13 ? 211 PHE A CB 1 ATOM 1656 C CG . PHE A 1 211 ? 50.627 97.892 17.891 1.00 21.53 ? 211 PHE A CG 1 ATOM 1657 C CD1 . PHE A 1 211 ? 51.360 97.857 19.093 1.00 22.19 ? 211 PHE A CD1 1 ATOM 1658 C CD2 . PHE A 1 211 ? 49.681 96.904 17.676 1.00 21.80 ? 211 PHE A CD2 1 ATOM 1659 C CE1 . PHE A 1 211 ? 51.136 96.869 20.029 1.00 22.24 ? 211 PHE A CE1 1 ATOM 1660 C CE2 . PHE A 1 211 ? 49.454 95.903 18.625 1.00 22.06 ? 211 PHE A CE2 1 ATOM 1661 C CZ . PHE A 1 211 ? 50.175 95.893 19.803 1.00 22.30 ? 211 PHE A CZ 1 ATOM 1662 N N . GLY A 1 212 ? 53.002 100.128 14.861 1.00 22.47 ? 212 GLY A N 1 ATOM 1663 C CA . GLY A 1 212 ? 53.092 100.617 13.488 1.00 24.57 ? 212 GLY A CA 1 ATOM 1664 C C . GLY A 1 212 ? 51.884 100.295 12.651 1.00 26.02 ? 212 GLY A C 1 ATOM 1665 O O . GLY A 1 212 ? 51.574 101.000 11.687 1.00 26.40 ? 212 GLY A O 1 ATOM 1666 N N . ASP A 1 213 ? 51.195 99.213 12.990 1.00 27.39 ? 213 ASP A N 1 ATOM 1667 C CA . ASP A 1 213 ? 50.014 98.793 12.264 1.00 29.21 ? 213 ASP A CA 1 ATOM 1668 C C . ASP A 1 213 ? 49.017 98.245 13.251 1.00 27.54 ? 213 ASP A C 1 ATOM 1669 O O . ASP A 1 213 ? 49.406 97.632 14.251 1.00 27.45 ? 213 ASP A O 1 ATOM 1670 C CB . ASP A 1 213 ? 50.363 97.718 11.223 1.00 34.01 ? 213 ASP A CB 1 ATOM 1671 C CG . ASP A 1 213 ? 50.969 98.307 9.957 1.00 43.70 ? 213 ASP A CG 1 ATOM 1672 O OD1 . ASP A 1 213 ? 50.199 98.853 9.129 1.00 54.31 ? 213 ASP A OD1 1 ATOM 1673 O OD2 . ASP A 1 213 ? 52.209 98.241 9.784 1.00 44.76 ? 213 ASP A OD2 1 ATOM 1674 N N . SER A 1 214 ? 47.737 98.439 12.954 1.00 24.68 ? 214 SER A N 1 ATOM 1675 C CA . SER A 1 214 ? 46.661 97.941 13.789 1.00 23.76 ? 214 SER A CA 1 ATOM 1676 C C . SER A 1 214 ? 46.383 96.481 13.457 1.00 23.49 ? 214 SER A C 1 ATOM 1677 O O . SER A 1 214 ? 46.525 96.053 12.304 1.00 23.17 ? 214 SER A O 1 ATOM 1678 C CB . SER A 1 214 ? 45.403 98.795 13.596 1.00 24.25 ? 214 SER A CB 1 ATOM 1679 O OG . SER A 1 214 ? 44.353 98.352 14.433 1.00 23.97 ? 214 SER A OG 1 ATOM 1680 N N . VAL A 1 215 ? 46.016 95.713 14.476 1.00 22.61 ? 215 VAL A N 1 ATOM 1681 C CA . VAL A 1 215 ? 45.638 94.313 14.315 1.00 23.41 ? 215 VAL A CA 1 ATOM 1682 C C . VAL A 1 215 ? 44.188 94.177 14.729 1.00 22.87 ? 215 VAL A C 1 ATOM 1683 O O . VAL A 1 215 ? 43.800 94.687 15.786 1.00 22.69 ? 215 VAL A O 1 ATOM 1684 C CB . VAL A 1 215 ? 46.554 93.412 15.184 1.00 24.25 ? 215 VAL A CB 1 ATOM 1685 C CG1 . VAL A 1 215 ? 46.099 91.967 15.156 1.00 24.17 ? 215 VAL A CG1 1 ATOM 1686 C CG2 . VAL A 1 215 ? 48.009 93.559 14.743 1.00 25.00 ? 215 VAL A CG2 1 ATOM 1687 N N . SER A 1 216 ? 43.384 93.492 13.925 1.00 23.06 ? 216 SER A N 1 ATOM 1688 C CA . SER A 1 216 ? 41.974 93.299 14.229 1.00 23.45 ? 216 SER A CA 1 ATOM 1689 C C . SER A 1 216 ? 41.751 91.992 14.968 1.00 23.74 ? 216 SER A C 1 ATOM 1690 O O . SER A 1 216 ? 41.929 90.908 14.409 1.00 22.91 ? 216 SER A O 1 ATOM 1691 C CB . SER A 1 216 ? 41.099 93.321 12.973 1.00 24.52 ? 216 SER A CB 1 ATOM 1692 O OG . SER A 1 216 ? 41.117 94.595 12.367 1.00 26.29 ? 216 SER A OG 1 ATOM 1693 N N . LEU A 1 217 ? 41.355 92.110 16.232 1.00 22.24 ? 217 LEU A N 1 ATOM 1694 C CA . LEU A 1 217 ? 40.976 90.967 17.043 1.00 22.44 ? 217 LEU A CA 1 ATOM 1695 C C . LEU A 1 217 ? 39.485 90.976 17.295 1.00 24.44 ? 217 LEU A C 1 ATOM 1696 O O . LEU A 1 217 ? 38.958 91.920 17.897 1.00 26.53 ? 217 LEU A O 1 ATOM 1697 C CB . LEU A 1 217 ? 41.702 91.009 18.382 1.00 22.80 ? 217 LEU A CB 1 ATOM 1698 C CG . LEU A 1 217 ? 43.226 90.980 18.345 1.00 23.26 ? 217 LEU A CG 1 ATOM 1699 C CD1 . LEU A 1 217 ? 43.802 90.830 19.743 1.00 22.76 ? 217 LEU A CD1 1 ATOM 1700 C CD2 . LEU A 1 217 ? 43.692 89.848 17.432 1.00 22.99 ? 217 LEU A CD2 1 ATOM 1701 N N . TYR A 1 218 ? 38.809 89.913 16.889 1.00 21.78 ? 218 TYR A N 1 ATOM 1702 C CA . TYR A 1 218 ? 37.381 89.816 17.106 1.00 21.62 ? 218 TYR A CA 1 ATOM 1703 C C . TYR A 1 218 ? 37.025 89.403 18.545 1.00 22.94 ? 218 TYR A C 1 ATOM 1704 O O . TYR A 1 218 ? 37.731 88.641 19.202 1.00 20.26 ? 218 TYR A O 1 ATOM 1705 C CB . TYR A 1 218 ? 36.769 88.845 16.088 1.00 22.22 ? 218 TYR A CB 1 ATOM 1706 C CG . TYR A 1 218 ? 36.691 89.431 14.688 1.00 22.54 ? 218 TYR A CG 1 ATOM 1707 C CD1 . TYR A 1 218 ? 37.806 89.447 13.841 1.00 22.80 ? 218 TYR A CD1 1 ATOM 1708 C CD2 . TYR A 1 218 ? 35.500 90.013 14.223 1.00 23.22 ? 218 TYR A CD2 1 ATOM 1709 C CE1 . TYR A 1 218 ? 37.733 90.008 12.545 1.00 22.91 ? 218 TYR A CE1 1 ATOM 1710 C CE2 . TYR A 1 218 ? 35.414 90.566 12.946 1.00 22.50 ? 218 TYR A CE2 1 ATOM 1711 C CZ . TYR A 1 218 ? 36.533 90.560 12.111 1.00 22.61 ? 218 TYR A CZ 1 ATOM 1712 O OH . TYR A 1 218 ? 36.429 91.115 10.858 1.00 22.96 ? 218 TYR A OH 1 ATOM 1713 N N . ASN A 1 219 ? 35.912 89.934 19.037 1.00 23.84 ? 219 ASN A N 1 ATOM 1714 C CA . ASN A 1 219 ? 35.365 89.508 20.313 1.00 22.50 ? 219 ASN A CA 1 ATOM 1715 C C . ASN A 1 219 ? 34.344 88.400 20.091 1.00 23.40 ? 219 ASN A C 1 ATOM 1716 O O . ASN A 1 219 ? 34.108 87.965 18.968 1.00 22.73 ? 219 ASN A O 1 ATOM 1717 C CB . ASN A 1 219 ? 34.844 90.708 21.128 1.00 23.12 ? 219 ASN A CB 1 ATOM 1718 C CG . ASN A 1 219 ? 33.609 91.363 20.535 1.00 23.55 ? 219 ASN A CG 1 ATOM 1719 O OD1 . ASN A 1 219 ? 32.899 90.792 19.705 1.00 23.14 ? 219 ASN A OD1 1 ATOM 1720 N ND2 . ASN A 1 219 ? 33.333 92.558 20.998 1.00 24.34 ? 219 ASN A ND2 1 ATOM 1721 N N . SER A 1 220 ? 33.779 87.895 21.174 1.00 24.29 ? 220 SER A N 1 ATOM 1722 C CA . SER A 1 220 ? 32.833 86.796 21.086 1.00 25.54 ? 220 SER A CA 1 ATOM 1723 C C . SER A 1 220 ? 31.475 87.169 20.440 1.00 26.40 ? 220 SER A C 1 ATOM 1724 O O . SER A 1 220 ? 30.716 86.280 20.085 1.00 25.97 ? 220 SER A O 1 ATOM 1725 C CB . SER A 1 220 ? 32.613 86.179 22.476 1.00 26.60 ? 220 SER A CB 1 ATOM 1726 O OG . SER A 1 220 ? 33.702 85.328 22.788 1.00 27.28 ? 220 SER A OG 1 ATOM 1727 N N . MET A 1 221 ? 31.193 88.458 20.285 1.00 26.07 ? 221 MET A N 1 ATOM 1728 C CA . MET A 1 221 ? 30.035 88.922 19.513 1.00 30.79 ? 221 MET A CA 1 ATOM 1729 C C . MET A 1 221 ? 30.392 89.198 18.034 1.00 29.47 ? 221 MET A C 1 ATOM 1730 O O . MET A 1 221 ? 29.623 89.838 17.332 1.00 28.06 ? 221 MET A O 1 ATOM 1731 C CB . MET A 1 221 ? 29.455 90.192 20.162 1.00 34.40 ? 221 MET A CB 1 ATOM 1732 C CG . MET A 1 221 ? 28.782 89.949 21.516 1.00 39.38 ? 221 MET A CG 1 ATOM 1733 S SD . MET A 1 221 ? 27.259 88.986 21.355 1.00 49.25 ? 221 MET A SD 1 ATOM 1734 C CE . MET A 1 221 ? 26.121 90.207 20.695 1.00 48.20 ? 221 MET A CE 1 ATOM 1735 N N . ASP A 1 222 ? 31.554 88.720 17.573 1.00 27.07 ? 222 ASP A N 1 ATOM 1736 C CA . ASP A 1 222 ? 32.040 88.930 16.197 1.00 26.98 ? 222 ASP A CA 1 ATOM 1737 C C . ASP A 1 222 ? 32.227 90.387 15.798 1.00 25.87 ? 222 ASP A C 1 ATOM 1738 O O . ASP A 1 222 ? 32.139 90.723 14.627 1.00 24.20 ? 222 ASP A O 1 ATOM 1739 C CB . ASP A 1 222 ? 31.139 88.233 15.164 1.00 28.50 ? 222 ASP A CB 1 ATOM 1740 C CG . ASP A 1 222 ? 31.085 86.742 15.330 1.00 29.52 ? 222 ASP A CG 1 ATOM 1741 O OD1 . ASP A 1 222 ? 32.063 86.106 15.760 1.00 29.44 ? 222 ASP A OD1 1 ATOM 1742 O OD2 . ASP A 1 222 ? 30.039 86.166 14.993 1.00 33.74 ? 222 ASP A OD2 1 ATOM 1743 N N . GLU A 1 223 ? 32.528 91.243 16.758 1.00 25.20 ? 223 GLU A N 1 ATOM 1744 C CA . GLU A 1 223 ? 32.858 92.628 16.493 1.00 26.51 ? 223 GLU A CA 1 ATOM 1745 C C . GLU A 1 223 ? 34.387 92.731 16.428 1.00 26.08 ? 223 GLU A C 1 ATOM 1746 O O . GLU A 1 223 ? 35.071 92.254 17.345 1.00 25.02 ? 223 GLU A O 1 ATOM 1747 C CB . GLU A 1 223 ? 32.336 93.530 17.616 1.00 29.21 ? 223 GLU A CB 1 ATOM 1748 C CG . GLU A 1 223 ? 30.811 93.629 17.699 1.00 33.29 ? 223 GLU A CG 1 ATOM 1749 C CD . GLU A 1 223 ? 30.239 94.027 19.076 1.00 38.79 ? 223 GLU A CD 1 ATOM 1750 O OE1 . GLU A 1 223 ? 30.946 94.054 20.132 1.00 34.10 ? 223 GLU A OE1 1 ATOM 1751 O OE2 . GLU A 1 223 ? 29.007 94.279 19.104 1.00 43.77 ? 223 GLU A OE2 1 ATOM 1752 N N . PRO A 1 224 ? 34.934 93.382 15.382 1.00 25.73 ? 224 PRO A N 1 ATOM 1753 C CA . PRO A 1 224 ? 36.382 93.528 15.354 1.00 25.10 ? 224 PRO A CA 1 ATOM 1754 C C . PRO A 1 224 ? 36.844 94.648 16.279 1.00 24.99 ? 224 PRO A C 1 ATOM 1755 O O . PRO A 1 224 ? 36.290 95.727 16.251 1.00 23.69 ? 224 PRO A O 1 ATOM 1756 C CB . PRO A 1 224 ? 36.675 93.865 13.894 1.00 26.28 ? 224 PRO A CB 1 ATOM 1757 C CG . PRO A 1 224 ? 35.455 94.583 13.422 1.00 26.64 ? 224 PRO A CG 1 ATOM 1758 C CD . PRO A 1 224 ? 34.287 94.134 14.281 1.00 27.58 ? 224 PRO A CD 1 ATOM 1759 N N . ILE A 1 225 ? 37.836 94.369 17.115 1.00 22.81 ? 225 ILE A N 1 ATOM 1760 C CA . ILE A 1 225 ? 38.433 95.377 17.953 1.00 23.47 ? 225 ILE A CA 1 ATOM 1761 C C . ILE A 1 225 ? 39.820 95.694 17.415 1.00 22.46 ? 225 ILE A C 1 ATOM 1762 O O . ILE A 1 225 ? 40.653 94.799 17.287 1.00 21.28 ? 225 ILE A O 1 ATOM 1763 C CB . ILE A 1 225 ? 38.525 94.902 19.421 1.00 24.09 ? 225 ILE A CB 1 ATOM 1764 C CG1 . ILE A 1 225 ? 37.137 94.602 19.964 1.00 25.38 ? 225 ILE A CG1 1 ATOM 1765 C CG2 . ILE A 1 225 ? 39.212 95.964 20.278 1.00 24.16 ? 225 ILE A CG2 1 ATOM 1766 C CD1 . ILE A 1 225 ? 37.147 93.862 21.282 1.00 26.70 ? 225 ILE A CD1 1 ATOM 1767 N N . GLY A 1 226 ? 40.061 96.970 17.121 1.00 22.50 ? 226 GLY A N 1 ATOM 1768 C CA . GLY A 1 226 ? 41.341 97.429 16.603 1.00 22.53 ? 226 GLY A CA 1 ATOM 1769 C C . GLY A 1 226 ? 42.342 97.493 17.732 1.00 23.35 ? 226 GLY A C 1 ATOM 1770 O O . GLY A 1 226 ? 42.158 98.237 18.698 1.00 22.71 ? 226 GLY A O 1 ATOM 1771 N N . VAL A 1 227 ? 43.376 96.673 17.649 1.00 22.43 ? 227 VAL A N 1 ATOM 1772 C CA . VAL A 1 227 ? 44.457 96.713 18.610 1.00 22.51 ? 227 VAL A CA 1 ATOM 1773 C C . VAL A 1 227 ? 45.658 97.356 17.928 1.00 22.89 ? 227 VAL A C 1 ATOM 1774 O O . VAL A 1 227 ? 46.338 96.721 17.104 1.00 22.17 ? 227 VAL A O 1 ATOM 1775 C CB . VAL A 1 227 ? 44.770 95.314 19.177 1.00 22.78 ? 227 VAL A CB 1 ATOM 1776 C CG1 . VAL A 1 227 ? 45.961 95.378 20.118 1.00 23.59 ? 227 VAL A CG1 1 ATOM 1777 C CG2 . VAL A 1 227 ? 43.575 94.775 19.928 1.00 22.98 ? 227 VAL A CG2 1 ATOM 1778 N N . ASP A 1 228 ? 45.889 98.634 18.247 1.00 22.25 ? 228 ASP A N 1 ATOM 1779 C CA . ASP A 1 228 ? 46.966 99.418 17.649 1.00 22.81 ? 228 ASP A CA 1 ATOM 1780 C C . ASP A 1 228 ? 47.958 99.951 18.685 1.00 21.40 ? 228 ASP A C 1 ATOM 1781 O O . ASP A 1 228 ? 48.688 100.902 18.433 1.00 21.02 ? 228 ASP A O 1 ATOM 1782 C CB . ASP A 1 228 ? 46.394 100.563 16.807 1.00 23.74 ? 228 ASP A CB 1 ATOM 1783 C CG . ASP A 1 228 ? 45.608 101.587 17.638 1.00 25.07 ? 228 ASP A CG 1 ATOM 1784 O OD1 . ASP A 1 228 ? 45.172 101.265 18.762 1.00 24.61 ? 228 ASP A OD1 1 ATOM 1785 O OD2 . ASP A 1 228 ? 45.394 102.709 17.136 1.00 26.71 ? 228 ASP A OD2 1 ATOM 1786 N N . SER A 1 229 ? 47.983 99.305 19.843 1.00 21.65 ? 229 SER A N 1 ATOM 1787 C CA . SER A 1 229 ? 48.899 99.618 20.910 1.00 21.89 ? 229 SER A CA 1 ATOM 1788 C C . SER A 1 229 ? 48.889 98.473 21.898 1.00 21.93 ? 229 SER A C 1 ATOM 1789 O O . SER A 1 229 ? 48.053 97.574 21.837 1.00 20.80 ? 229 SER A O 1 ATOM 1790 C CB . SER A 1 229 ? 48.454 100.891 21.664 1.00 22.35 ? 229 SER A CB 1 ATOM 1791 O OG . SER A 1 229 ? 47.331 100.598 22.482 1.00 21.11 ? 229 SER A OG 1 ATOM 1792 N N . MET A 1 230 ? 49.785 98.575 22.860 1.00 22.75 ? 230 MET A N 1 ATOM 1793 C CA . MET A 1 230 ? 49.840 97.626 23.968 1.00 24.13 ? 230 MET A CA 1 ATOM 1794 C C . MET A 1 230 ? 48.804 97.878 25.083 1.00 23.30 ? 230 MET A C 1 ATOM 1795 O O . MET A 1 230 ? 48.798 97.155 26.057 1.00 22.50 ? 230 MET A O 1 ATOM 1796 C CB . MET A 1 230 ? 51.231 97.649 24.581 1.00 26.37 ? 230 MET A CB 1 ATOM 1797 C CG . MET A 1 230 ? 51.568 98.939 25.328 1.00 30.15 ? 230 MET A CG 1 ATOM 1798 S SD . MET A 1 230 ? 53.138 98.895 26.203 1.00 34.70 ? 230 MET A SD 1 ATOM 1799 C CE . MET A 1 230 ? 52.743 97.811 27.543 1.00 34.57 ? 230 MET A CE 1 ATOM 1800 N N . TYR A 1 231 ? 47.940 98.886 24.949 1.00 21.30 ? 231 TYR A N 1 ATOM 1801 C CA . TYR A 1 231 ? 47.061 99.303 26.051 1.00 21.72 ? 231 TYR A CA 1 ATOM 1802 C C . TYR A 1 231 ? 45.682 98.650 25.971 1.00 22.16 ? 231 TYR A C 1 ATOM 1803 O O . TYR A 1 231 ? 44.711 99.265 26.338 1.00 26.15 ? 231 TYR A O 1 ATOM 1804 C CB . TYR A 1 231 ? 47.019 100.857 26.074 1.00 22.01 ? 231 TYR A CB 1 ATOM 1805 C CG . TYR A 1 231 ? 48.439 101.427 26.111 1.00 20.93 ? 231 TYR A CG 1 ATOM 1806 C CD1 . TYR A 1 231 ? 49.229 101.248 27.233 1.00 21.04 ? 231 TYR A CD1 1 ATOM 1807 C CD2 . TYR A 1 231 ? 48.999 102.087 25.021 1.00 21.28 ? 231 TYR A CD2 1 ATOM 1808 C CE1 . TYR A 1 231 ? 50.525 101.711 27.288 1.00 20.85 ? 231 TYR A CE1 1 ATOM 1809 C CE2 . TYR A 1 231 ? 50.303 102.568 25.061 1.00 21.48 ? 231 TYR A CE2 1 ATOM 1810 C CZ . TYR A 1 231 ? 51.066 102.359 26.202 1.00 21.44 ? 231 TYR A CZ 1 ATOM 1811 O OH . TYR A 1 231 ? 52.341 102.805 26.302 1.00 21.49 ? 231 TYR A OH 1 ATOM 1812 N N . TYR A 1 232 ? 45.589 97.433 25.435 1.00 21.60 ? 232 TYR A N 1 ATOM 1813 C CA . TYR A 1 232 ? 44.332 96.684 25.316 1.00 20.93 ? 232 TYR A CA 1 ATOM 1814 C C . TYR A 1 232 ? 44.420 95.423 26.183 1.00 22.74 ? 232 TYR A C 1 ATOM 1815 O O . TYR A 1 232 ? 45.255 94.571 25.916 1.00 20.01 ? 232 TYR A O 1 ATOM 1816 C CB . TYR A 1 232 ? 44.041 96.325 23.851 1.00 20.82 ? 232 TYR A CB 1 ATOM 1817 C CG . TYR A 1 232 ? 43.635 97.533 23.055 1.00 20.96 ? 232 TYR A CG 1 ATOM 1818 C CD1 . TYR A 1 232 ? 42.303 97.908 22.980 1.00 19.62 ? 232 TYR A CD1 1 ATOM 1819 C CD2 . TYR A 1 232 ? 44.591 98.361 22.458 1.00 20.51 ? 232 TYR A CD2 1 ATOM 1820 C CE1 . TYR A 1 232 ? 41.914 99.048 22.296 1.00 20.66 ? 232 TYR A CE1 1 ATOM 1821 C CE2 . TYR A 1 232 ? 44.197 99.515 21.765 1.00 20.79 ? 232 TYR A CE2 1 ATOM 1822 C CZ . TYR A 1 232 ? 42.852 99.847 21.698 1.00 19.94 ? 232 TYR A CZ 1 ATOM 1823 O OH . TYR A 1 232 ? 42.424 100.973 21.025 1.00 20.00 ? 232 TYR A OH 1 ATOM 1824 N N . PRO A 1 233 ? 43.562 95.293 27.225 1.00 24.56 ? 233 PRO A N 1 ATOM 1825 C CA . PRO A 1 233 ? 43.608 94.079 28.063 1.00 25.06 ? 233 PRO A CA 1 ATOM 1826 C C . PRO A 1 233 ? 43.372 92.764 27.316 1.00 26.24 ? 233 PRO A C 1 ATOM 1827 O O . PRO A 1 233 ? 43.902 91.720 27.727 1.00 25.50 ? 233 PRO A O 1 ATOM 1828 C CB . PRO A 1 233 ? 42.477 94.303 29.071 1.00 25.92 ? 233 PRO A CB 1 ATOM 1829 C CG . PRO A 1 233 ? 42.346 95.784 29.150 1.00 26.80 ? 233 PRO A CG 1 ATOM 1830 C CD . PRO A 1 233 ? 42.567 96.256 27.741 1.00 25.72 ? 233 PRO A CD 1 ATOM 1831 N N . ILE A 1 234 ? 42.625 92.824 26.216 1.00 25.30 ? 234 ILE A N 1 ATOM 1832 C CA . ILE A 1 234 ? 42.412 91.646 25.376 1.00 25.89 ? 234 ILE A CA 1 ATOM 1833 C C . ILE A 1 234 ? 43.669 91.162 24.675 1.00 23.73 ? 234 ILE A C 1 ATOM 1834 O O . ILE A 1 234 ? 43.659 90.098 24.118 1.00 24.41 ? 234 ILE A O 1 ATOM 1835 C CB . ILE A 1 234 ? 41.297 91.842 24.319 1.00 26.93 ? 234 ILE A CB 1 ATOM 1836 C CG1 . ILE A 1 234 ? 41.695 92.889 23.256 1.00 27.80 ? 234 ILE A CG1 1 ATOM 1837 C CG2 . ILE A 1 234 ? 39.979 92.158 25.016 1.00 26.86 ? 234 ILE A CG2 1 ATOM 1838 C CD1 . ILE A 1 234 ? 40.845 92.810 22.005 1.00 28.93 ? 234 ILE A CD1 1 ATOM 1839 N N . LEU A 1 235 ? 44.704 91.980 24.634 1.00 22.71 ? 235 LEU A N 1 ATOM 1840 C CA . LEU A 1 235 ? 46.008 91.555 24.190 1.00 25.09 ? 235 LEU A CA 1 ATOM 1841 C C . LEU A 1 235 ? 46.907 91.203 25.377 1.00 25.35 ? 235 LEU A C 1 ATOM 1842 O O . LEU A 1 235 ? 47.392 90.084 25.510 1.00 22.55 ? 235 LEU A O 1 ATOM 1843 C CB . LEU A 1 235 ? 46.691 92.643 23.361 1.00 24.58 ? 235 LEU A CB 1 ATOM 1844 C CG . LEU A 1 235 ? 48.116 92.318 22.891 1.00 26.20 ? 235 LEU A CG 1 ATOM 1845 C CD1 . LEU A 1 235 ? 48.156 90.996 22.130 1.00 27.11 ? 235 LEU A CD1 1 ATOM 1846 C CD2 . LEU A 1 235 ? 48.673 93.440 22.038 1.00 26.21 ? 235 LEU A CD2 1 ATOM 1847 N N . THR A 1 236 ? 47.127 92.183 26.229 1.00 25.85 ? 236 THR A N 1 ATOM 1848 C CA . THR A 1 236 ? 48.224 92.096 27.166 1.00 28.12 ? 236 THR A CA 1 ATOM 1849 C C . THR A 1 236 ? 47.927 91.165 28.357 1.00 26.09 ? 236 THR A C 1 ATOM 1850 O O . THR A 1 236 ? 48.852 90.644 28.942 1.00 27.56 ? 236 THR A O 1 ATOM 1851 C CB . THR A 1 236 ? 48.736 93.493 27.557 1.00 31.10 ? 236 THR A CB 1 ATOM 1852 O OG1 . THR A 1 236 ? 47.706 94.202 28.213 1.00 35.99 ? 236 THR A OG1 1 ATOM 1853 C CG2 . THR A 1 236 ? 49.161 94.275 26.328 1.00 31.34 ? 236 THR A CG2 1 ATOM 1854 N N . ALA A 1 237 ? 46.658 90.916 28.669 1.00 24.68 ? 237 ALA A N 1 ATOM 1855 C CA . ALA A 1 237 ? 46.259 89.850 29.598 1.00 27.66 ? 237 ALA A CA 1 ATOM 1856 C C . ALA A 1 237 ? 45.847 88.531 28.916 1.00 27.45 ? 237 ALA A C 1 ATOM 1857 O O . ALA A 1 237 ? 45.251 87.668 29.561 1.00 32.61 ? 237 ALA A O 1 ATOM 1858 C CB . ALA A 1 237 ? 45.120 90.319 30.494 1.00 27.53 ? 237 ALA A CB 1 ATOM 1859 N N . ASN A 1 238 ? 46.220 88.347 27.653 1.00 24.69 ? 238 ASN A N 1 ATOM 1860 C CA . ASN A 1 238 ? 45.742 87.218 26.849 1.00 22.70 ? 238 ASN A CA 1 ATOM 1861 C C . ASN A 1 238 ? 46.955 86.481 26.259 1.00 22.61 ? 238 ASN A C 1 ATOM 1862 O O . ASN A 1 238 ? 47.213 85.315 26.601 1.00 20.89 ? 238 ASN A O 1 ATOM 1863 C CB . ASN A 1 238 ? 44.815 87.780 25.758 1.00 22.13 ? 238 ASN A CB 1 ATOM 1864 C CG . ASN A 1 238 ? 44.184 86.712 24.877 1.00 21.46 ? 238 ASN A CG 1 ATOM 1865 O OD1 . ASN A 1 238 ? 44.387 85.505 25.058 1.00 21.58 ? 238 ASN A OD1 1 ATOM 1866 N ND2 . ASN A 1 238 ? 43.412 87.168 23.907 1.00 20.31 ? 238 ASN A ND2 1 ATOM 1867 N N . MET A 1 239 ? 47.676 87.168 25.378 1.00 21.11 ? 239 MET A N 1 ATOM 1868 C CA . MET A 1 239 ? 48.857 86.606 24.718 1.00 24.32 ? 239 MET A CA 1 ATOM 1869 C C . MET A 1 239 ? 49.923 86.307 25.771 1.00 23.00 ? 239 MET A C 1 ATOM 1870 O O . MET A 1 239 ? 50.416 87.207 26.450 1.00 23.11 ? 239 MET A O 1 ATOM 1871 C CB . MET A 1 239 ? 49.408 87.554 23.658 1.00 26.07 ? 239 MET A CB 1 ATOM 1872 C CG . MET A 1 239 ? 50.497 86.973 22.771 1.00 28.96 ? 239 MET A CG 1 ATOM 1873 S SD . MET A 1 239 ? 50.931 88.179 21.488 1.00 33.72 ? 239 MET A SD 1 ATOM 1874 C CE . MET A 1 239 ? 52.295 87.503 20.618 1.00 34.16 ? 239 MET A CE 1 ATOM 1875 N N . ALA A 1 240 ? 50.260 85.036 25.894 1.00 21.71 ? 240 ALA A N 1 ATOM 1876 C CA . ALA A 1 240 ? 51.113 84.560 26.982 1.00 21.75 ? 240 ALA A CA 1 ATOM 1877 C C . ALA A 1 240 ? 52.587 84.644 26.656 1.00 20.87 ? 240 ALA A C 1 ATOM 1878 O O . ALA A 1 240 ? 53.407 84.748 27.553 1.00 20.73 ? 240 ALA A O 1 ATOM 1879 C CB . ALA A 1 240 ? 50.747 83.131 27.344 1.00 21.46 ? 240 ALA A CB 1 ATOM 1880 N N . PHE A 1 241 ? 52.923 84.549 25.383 1.00 19.90 ? 241 PHE A N 1 ATOM 1881 C CA . PHE A 1 241 ? 54.283 84.739 24.950 1.00 20.37 ? 241 PHE A CA 1 ATOM 1882 C C . PHE A 1 241 ? 54.305 85.112 23.491 1.00 20.88 ? 241 PHE A C 1 ATOM 1883 O O . PHE A 1 241 ? 53.328 84.907 22.788 1.00 20.57 ? 241 PHE A O 1 ATOM 1884 C CB . PHE A 1 241 ? 55.157 83.478 25.221 1.00 20.72 ? 241 PHE A CB 1 ATOM 1885 C CG . PHE A 1 241 ? 54.595 82.213 24.655 1.00 20.09 ? 241 PHE A CG 1 ATOM 1886 C CD1 . PHE A 1 241 ? 54.748 81.905 23.311 1.00 19.87 ? 241 PHE A CD1 1 ATOM 1887 C CD2 . PHE A 1 241 ? 53.897 81.337 25.463 1.00 20.92 ? 241 PHE A CD2 1 ATOM 1888 C CE1 . PHE A 1 241 ? 54.218 80.735 22.787 1.00 20.86 ? 241 PHE A CE1 1 ATOM 1889 C CE2 . PHE A 1 241 ? 53.360 80.152 24.946 1.00 21.24 ? 241 PHE A CE2 1 ATOM 1890 C CZ . PHE A 1 241 ? 53.517 79.849 23.612 1.00 20.12 ? 241 PHE A CZ 1 ATOM 1891 N N . GLN A 1 242 ? 55.439 85.647 23.049 1.00 20.92 ? 242 GLN A N 1 ATOM 1892 C CA . GLN A 1 242 ? 55.602 86.181 21.700 1.00 21.46 ? 242 GLN A CA 1 ATOM 1893 C C . GLN A 1 242 ? 56.718 85.506 20.916 1.00 20.77 ? 242 GLN A C 1 ATOM 1894 O O . GLN A 1 242 ? 57.677 85.048 21.511 1.00 21.20 ? 242 GLN A O 1 ATOM 1895 C CB . GLN A 1 242 ? 56.038 87.637 21.742 1.00 21.98 ? 242 GLN A CB 1 ATOM 1896 C CG . GLN A 1 242 ? 55.360 88.572 22.688 1.00 22.89 ? 242 GLN A CG 1 ATOM 1897 C CD . GLN A 1 242 ? 55.953 89.966 22.577 1.00 21.88 ? 242 GLN A CD 1 ATOM 1898 O OE1 . GLN A 1 242 ? 56.065 90.522 21.477 1.00 21.01 ? 242 GLN A OE1 1 ATOM 1899 N NE2 . GLN A 1 242 ? 56.328 90.538 23.713 1.00 21.72 ? 242 GLN A NE2 1 ATOM 1900 N N . LEU A 1 243 ? 56.602 85.543 19.596 1.00 20.22 ? 243 LEU A N 1 ATOM 1901 C CA . LEU A 1 243 ? 57.672 85.197 18.685 1.00 22.47 ? 243 LEU A CA 1 ATOM 1902 C C . LEU A 1 243 ? 58.763 86.300 18.693 1.00 23.51 ? 243 LEU A C 1 ATOM 1903 O O . LEU A 1 243 ? 58.446 87.492 18.653 1.00 20.74 ? 243 LEU A O 1 ATOM 1904 C CB . LEU A 1 243 ? 57.110 85.033 17.281 1.00 23.38 ? 243 LEU A CB 1 ATOM 1905 C CG . LEU A 1 243 ? 58.089 84.605 16.184 1.00 24.90 ? 243 LEU A CG 1 ATOM 1906 C CD1 . LEU A 1 243 ? 58.486 83.155 16.405 1.00 25.54 ? 243 LEU A CD1 1 ATOM 1907 C CD2 . LEU A 1 243 ? 57.526 84.800 14.783 1.00 25.99 ? 243 LEU A CD2 1 ATOM 1908 N N . TYR A 1 244 ? 60.036 85.903 18.742 1.00 22.25 ? 244 TYR A N 1 ATOM 1909 C CA . TYR A 1 244 ? 61.115 86.887 18.620 1.00 23.32 ? 244 TYR A CA 1 ATOM 1910 C C . TYR A 1 244 ? 61.019 87.597 17.281 1.00 24.18 ? 244 TYR A C 1 ATOM 1911 O O . TYR A 1 244 ? 60.900 86.953 16.249 1.00 23.17 ? 244 TYR A O 1 ATOM 1912 C CB . TYR A 1 244 ? 62.496 86.259 18.787 1.00 25.03 ? 244 TYR A CB 1 ATOM 1913 C CG . TYR A 1 244 ? 63.606 87.259 18.564 1.00 25.51 ? 244 TYR A CG 1 ATOM 1914 C CD1 . TYR A 1 244 ? 63.968 88.150 19.564 1.00 26.83 ? 244 TYR A CD1 1 ATOM 1915 C CD2 . TYR A 1 244 ? 64.278 87.315 17.346 1.00 27.16 ? 244 TYR A CD2 1 ATOM 1916 C CE1 . TYR A 1 244 ? 64.988 89.077 19.354 1.00 28.56 ? 244 TYR A CE1 1 ATOM 1917 C CE2 . TYR A 1 244 ? 65.292 88.233 17.122 1.00 29.09 ? 244 TYR A CE2 1 ATOM 1918 C CZ . TYR A 1 244 ? 65.642 89.100 18.130 1.00 29.63 ? 244 TYR A CZ 1 ATOM 1919 O OH . TYR A 1 244 ? 66.644 90.011 17.918 1.00 35.23 ? 244 TYR A OH 1 ATOM 1920 N N . GLN A 1 245 ? 61.004 88.931 17.312 1.00 25.40 ? 245 GLN A N 1 ATOM 1921 C CA . GLN A 1 245 ? 60.854 89.724 16.090 1.00 27.37 ? 245 GLN A CA 1 ATOM 1922 C C . GLN A 1 245 ? 61.879 90.863 15.887 1.00 29.42 ? 245 GLN A C 1 ATOM 1923 O O . GLN A 1 245 ? 62.325 91.061 14.785 1.00 30.88 ? 245 GLN A O 1 ATOM 1924 C CB . GLN A 1 245 ? 59.424 90.267 15.952 1.00 28.33 ? 245 GLN A CB 1 ATOM 1925 C CG . GLN A 1 245 ? 58.342 89.232 15.635 1.00 28.63 ? 245 GLN A CG 1 ATOM 1926 C CD . GLN A 1 245 ? 58.329 88.798 14.167 1.00 30.65 ? 245 GLN A CD 1 ATOM 1927 O OE1 . GLN A 1 245 ? 59.358 88.641 13.554 1.00 34.17 ? 245 GLN A OE1 1 ATOM 1928 N NE2 . GLN A 1 245 ? 57.160 88.581 13.623 1.00 33.61 ? 245 GLN A NE2 1 ATOM 1929 N N . CYS A 1 246 ? 62.270 91.597 16.928 1.00 31.47 ? 246 CYS A N 1 ATOM 1930 C CA . CYS A 1 246 ? 63.010 92.877 16.807 1.00 33.71 ? 246 CYS A CA 1 ATOM 1931 C C . CYS A 1 246 ? 64.240 92.843 17.710 1.00 34.86 ? 246 CYS A C 1 ATOM 1932 O O . CYS A 1 246 ? 64.154 92.338 18.808 1.00 32.93 ? 246 CYS A O 1 ATOM 1933 C CB . CYS A 1 246 ? 62.089 94.042 17.213 1.00 33.26 ? 246 CYS A CB 1 ATOM 1934 S SG . CYS A 1 246 ? 60.780 94.258 15.977 1.00 36.46 ? 246 CYS A SG 1 ATOM 1935 N N . PRO A 1 247 ? 65.403 93.366 17.263 1.00 37.94 ? 247 PRO A N 1 ATOM 1936 C CA . PRO A 1 247 ? 66.667 93.412 18.028 1.00 39.79 ? 247 PRO A CA 1 ATOM 1937 C C . PRO A 1 247 ? 66.587 93.894 19.479 1.00 38.69 ? 247 PRO A C 1 ATOM 1938 O O . PRO A 1 247 ? 65.826 94.809 19.763 1.00 45.21 ? 247 PRO A O 1 ATOM 1939 C CB . PRO A 1 247 ? 67.501 94.374 17.198 1.00 41.10 ? 247 PRO A CB 1 ATOM 1940 C CG . PRO A 1 247 ? 67.100 94.052 15.800 1.00 40.29 ? 247 PRO A CG 1 ATOM 1941 C CD . PRO A 1 247 ? 65.628 93.728 15.856 1.00 39.42 ? 247 PRO A CD 1 ATOM 1942 N N . ASN B 2 1 ? 64.757 94.705 9.285 1.00 65.87 ? 1 ASN B N 1 ATOM 1943 C CA . ASN B 2 1 ? 63.299 94.746 9.244 1.00 62.32 ? 1 ASN B CA 1 ATOM 1944 C C . ASN B 2 1 ? 62.813 96.085 9.700 1.00 60.02 ? 1 ASN B C 1 ATOM 1945 O O . ASN B 2 1 ? 62.576 96.271 10.867 1.00 62.81 ? 1 ASN B O 1 ATOM 1946 C CB . ASN B 2 1 ? 62.711 93.672 10.130 1.00 59.21 ? 1 ASN B CB 1 ATOM 1947 C CG . ASN B 2 1 ? 61.263 93.456 9.862 1.00 60.49 ? 1 ASN B CG 1 ATOM 1948 O OD1 . ASN B 2 1 ? 60.641 94.236 9.154 1.00 58.96 ? 1 ASN B OD1 1 ATOM 1949 N ND2 . ASN B 2 1 ? 60.711 92.401 10.422 1.00 60.06 ? 1 ASN B ND2 1 ATOM 1950 N N . GLU B 2 2 ? 62.671 97.012 8.768 1.00 58.43 ? 2 GLU B N 1 ATOM 1951 C CA . GLU B 2 2 ? 62.246 98.392 9.082 1.00 55.37 ? 2 GLU B CA 1 ATOM 1952 C C . GLU B 2 2 ? 60.873 98.500 9.755 1.00 48.13 ? 2 GLU B C 1 ATOM 1953 O O . GLU B 2 2 ? 60.551 99.534 10.341 1.00 42.68 ? 2 GLU B O 1 ATOM 1954 C CB . GLU B 2 2 ? 62.280 99.257 7.822 1.00 58.67 ? 2 GLU B CB 1 ATOM 1955 N N . GLN B 2 3 ? 60.080 97.433 9.680 1.00 42.57 ? 3 GLN B N 1 ATOM 1956 C CA . GLN B 2 3 ? 58.887 97.292 10.521 1.00 39.90 ? 3 GLN B CA 1 ATOM 1957 C C . GLN B 2 3 ? 59.175 97.266 12.031 1.00 35.26 ? 3 GLN B C 1 ATOM 1958 O O . GLN B 2 3 ? 58.276 97.542 12.811 1.00 36.64 ? 3 GLN B O 1 ATOM 1959 C CB . GLN B 2 3 ? 58.074 96.068 10.105 1.00 42.84 ? 3 GLN B CB 1 ATOM 1960 C CG . GLN B 2 3 ? 57.228 96.289 8.865 1.00 46.60 ? 3 GLN B CG 1 ATOM 1961 C CD . GLN B 2 3 ? 56.266 95.141 8.620 1.00 50.91 ? 3 GLN B CD 1 ATOM 1962 O OE1 . GLN B 2 3 ? 55.094 95.200 9.008 1.00 54.22 ? 3 GLN B OE1 1 ATOM 1963 N NE2 . GLN B 2 3 ? 56.763 94.073 8.004 1.00 52.99 ? 3 GLN B NE2 1 ATOM 1964 N N . CYS B 2 4 ? 60.407 96.973 12.446 1.00 31.64 ? 4 CYS B N 1 ATOM 1965 C CA . CYS B 2 4 ? 60.827 97.143 13.852 1.00 32.63 ? 4 CYS B CA 1 ATOM 1966 C C . CYS B 2 4 ? 60.926 98.594 14.338 1.00 30.84 ? 4 CYS B C 1 ATOM 1967 O O . CYS B 2 4 ? 60.913 98.847 15.548 1.00 30.87 ? 4 CYS B O 1 ATOM 1968 C CB . CYS B 2 4 ? 62.152 96.413 14.111 1.00 35.24 ? 4 CYS B CB 1 ATOM 1969 S SG . CYS B 2 4 ? 61.884 94.583 13.990 1.00 40.01 ? 4 CYS B SG 1 ATOM 1970 N N . SER B 2 5 ? 61.009 99.536 13.397 1.00 30.25 ? 5 SER B N 1 ATOM 1971 C CA . SER B 2 5 ? 61.176 100.964 13.686 1.00 29.55 ? 5 SER B CA 1 ATOM 1972 C C . SER B 2 5 ? 60.123 101.812 12.982 1.00 29.64 ? 5 SER B C 1 ATOM 1973 O O . SER B 2 5 ? 60.439 102.557 12.058 1.00 28.21 ? 5 SER B O 1 ATOM 1974 C CB . SER B 2 5 ? 62.553 101.385 13.193 1.00 30.67 ? 5 SER B CB 1 ATOM 1975 O OG . SER B 2 5 ? 63.549 100.597 13.817 1.00 31.87 ? 5 SER B OG 1 ATOM 1976 N N . PRO B 2 6 ? 58.873 101.735 13.385 1.00 28.41 ? 6 PRO B N 1 ATOM 1977 C CA . PRO B 2 6 ? 57.817 102.535 12.767 1.00 28.21 ? 6 PRO B CA 1 ATOM 1978 C C . PRO B 2 6 ? 58.106 104.009 12.918 1.00 28.54 ? 6 PRO B C 1 ATOM 1979 O O . PRO B 2 6 ? 58.485 104.418 13.955 1.00 30.35 ? 6 PRO B O 1 ATOM 1980 C CB . PRO B 2 6 ? 56.580 102.144 13.551 1.00 28.11 ? 6 PRO B CB 1 ATOM 1981 C CG . PRO B 2 6 ? 57.068 101.590 14.816 1.00 26.57 ? 6 PRO B CG 1 ATOM 1982 C CD . PRO B 2 6 ? 58.381 100.962 14.518 1.00 27.90 ? 6 PRO B CD 1 ATOM 1983 N N . GLN B 2 7 ? 57.953 104.776 11.871 1.00 29.76 ? 7 GLN B N 1 ATOM 1984 C CA . GLN B 2 7 ? 58.267 106.182 11.930 1.00 30.18 ? 7 GLN B CA 1 ATOM 1985 C C . GLN B 2 7 ? 57.204 107.037 12.582 1.00 28.92 ? 7 GLN B C 1 ATOM 1986 O O . GLN B 2 7 ? 57.488 108.057 13.102 1.00 28.22 ? 7 GLN B O 1 ATOM 1987 C CB . GLN B 2 7 ? 58.706 106.683 10.570 1.00 32.98 ? 7 GLN B CB 1 ATOM 1988 C CG . GLN B 2 7 ? 60.067 106.108 10.176 1.00 35.26 ? 7 GLN B CG 1 ATOM 1989 C CD . GLN B 2 7 ? 61.116 106.272 11.274 1.00 39.50 ? 7 GLN B CD 1 ATOM 1990 O OE1 . GLN B 2 7 ? 61.455 105.332 11.988 1.00 44.59 ? 7 GLN B OE1 1 ATOM 1991 N NE2 . GLN B 2 7 ? 61.595 107.484 11.435 1.00 40.02 ? 7 GLN B NE2 1 ATOM 1992 N N . GLN B 2 8 ? 55.974 106.576 12.570 1.00 27.92 ? 8 GLN B N 1 ATOM 1993 C CA . GLN B 2 8 ? 54.897 107.294 13.213 1.00 28.02 ? 8 GLN B CA 1 ATOM 1994 C C . GLN B 2 8 ? 53.609 106.489 13.220 1.00 27.80 ? 8 GLN B C 1 ATOM 1995 O O . GLN B 2 8 ? 53.463 105.575 12.458 1.00 27.07 ? 8 GLN B O 1 ATOM 1996 C CB . GLN B 2 8 ? 54.628 108.613 12.480 1.00 28.52 ? 8 GLN B CB 1 ATOM 1997 C CG . GLN B 2 8 ? 54.136 108.446 11.059 1.00 30.31 ? 8 GLN B CG 1 ATOM 1998 C CD . GLN B 2 8 ? 53.958 109.768 10.328 1.00 33.26 ? 8 GLN B CD 1 ATOM 1999 O OE1 . GLN B 2 8 ? 54.911 110.444 10.012 1.00 38.61 ? 8 GLN B OE1 1 ATOM 2000 N NE2 . GLN B 2 8 ? 52.735 110.124 10.066 1.00 32.76 ? 8 GLN B NE2 1 ATOM 2001 N N . ARG B 2 9 ? 52.690 106.864 14.097 1.00 25.09 ? 9 ARG B N 1 ATOM 2002 C CA . ARG B 2 9 ? 51.357 106.280 14.068 1.00 24.63 ? 9 ARG B CA 1 ATOM 2003 C C . ARG B 2 9 ? 50.381 107.297 14.640 1.00 24.48 ? 9 ARG B C 1 ATOM 2004 O O . ARG B 2 9 ? 50.635 107.879 15.693 1.00 24.01 ? 9 ARG B O 1 ATOM 2005 C CB . ARG B 2 9 ? 51.303 104.990 14.895 1.00 25.28 ? 9 ARG B CB 1 ATOM 2006 C CG . ARG B 2 9 ? 49.954 104.277 14.858 1.00 25.52 ? 9 ARG B CG 1 ATOM 2007 C CD . ARG B 2 9 ? 49.757 103.543 13.551 1.00 28.59 ? 9 ARG B CD 1 ATOM 2008 N NE . ARG B 2 9 ? 48.381 103.076 13.368 1.00 30.97 ? 9 ARG B NE 1 ATOM 2009 C CZ . ARG B 2 9 ? 47.939 102.456 12.276 1.00 32.84 ? 9 ARG B CZ 1 ATOM 2010 N NH1 . ARG B 2 9 ? 48.756 102.205 11.253 1.00 35.69 ? 9 ARG B NH1 1 ATOM 2011 N NH2 . ARG B 2 9 ? 46.675 102.096 12.193 1.00 32.31 ? 9 ARG B NH2 1 ATOM 2012 N N . THR B 2 10 ? 49.269 107.462 13.943 1.00 23.31 ? 10 THR B N 1 ATOM 2013 C CA . THR B 2 10 ? 48.198 108.338 14.363 1.00 23.17 ? 10 THR B CA 1 ATOM 2014 C C . THR B 2 10 ? 47.129 107.518 15.038 1.00 22.32 ? 10 THR B C 1 ATOM 2015 O O . THR B 2 10 ? 46.688 106.505 14.503 1.00 21.50 ? 10 THR B O 1 ATOM 2016 C CB . THR B 2 10 ? 47.607 109.071 13.148 1.00 23.06 ? 10 THR B CB 1 ATOM 2017 O OG1 . THR B 2 10 ? 48.645 109.841 12.553 1.00 22.96 ? 10 THR B OG1 1 ATOM 2018 C CG2 . THR B 2 10 ? 46.524 110.042 13.593 1.00 24.31 ? 10 THR B CG2 1 ATOM 2019 N N . THR B 2 11 ? 46.710 107.960 16.221 1.00 22.59 ? 11 THR B N 1 ATOM 2020 C CA . THR B 2 11 ? 45.722 107.235 16.967 1.00 24.52 ? 11 THR B CA 1 ATOM 2021 C C . THR B 2 11 ? 44.894 108.225 17.802 1.00 25.37 ? 11 THR B C 1 ATOM 2022 O O . THR B 2 11 ? 45.151 109.421 17.748 1.00 26.67 ? 11 THR B O 1 ATOM 2023 C CB . THR B 2 11 ? 46.421 106.195 17.856 1.00 25.57 ? 11 THR B CB 1 ATOM 2024 O OG1 . THR B 2 11 ? 45.447 105.311 18.395 1.00 26.97 ? 11 THR B OG1 1 ATOM 2025 C CG2 . THR B 2 11 ? 47.182 106.855 18.967 1.00 26.57 ? 11 THR B CG2 1 ATOM 2026 N N . ARG B 2 12 ? 43.911 107.731 18.557 1.00 23.03 ? 12 ARG B N 1 ATOM 2027 C CA . ARG B 2 12 ? 43.200 108.571 19.536 1.00 22.83 ? 12 ARG B CA 1 ATOM 2028 C C . ARG B 2 12 ? 43.693 108.228 20.938 1.00 23.02 ? 12 ARG B C 1 ATOM 2029 O O . ARG B 2 12 ? 44.501 107.304 21.132 1.00 21.78 ? 12 ARG B O 1 ATOM 2030 C CB . ARG B 2 12 ? 41.689 108.409 19.416 1.00 22.95 ? 12 ARG B CB 1 ATOM 2031 C CG . ARG B 2 12 ? 41.181 108.919 18.079 1.00 23.31 ? 12 ARG B CG 1 ATOM 2032 C CD . ARG B 2 12 ? 39.682 108.889 17.955 1.00 22.20 ? 12 ARG B CD 1 ATOM 2033 N NE . ARG B 2 12 ? 39.127 107.548 17.936 1.00 21.04 ? 12 ARG B NE 1 ATOM 2034 C CZ . ARG B 2 12 ? 37.833 107.291 17.903 1.00 21.27 ? 12 ARG B CZ 1 ATOM 2035 N NH1 . ARG B 2 12 ? 36.943 108.276 17.899 1.00 23.03 ? 12 ARG B NH1 1 ATOM 2036 N NH2 . ARG B 2 12 ? 37.403 106.052 17.901 1.00 22.60 ? 12 ARG B NH2 1 ATOM 2037 N N . ILE B 2 13 ? 43.269 109.027 21.904 1.00 22.24 ? 13 ILE B N 1 ATOM 2038 C CA . ILE B 2 13 ? 43.612 108.786 23.291 1.00 21.85 ? 13 ILE B CA 1 ATOM 2039 C C . ILE B 2 13 ? 42.365 109.022 24.098 1.00 22.51 ? 13 ILE B C 1 ATOM 2040 O O . ILE B 2 13 ? 41.816 110.131 24.072 1.00 21.46 ? 13 ILE B O 1 ATOM 2041 C CB . ILE B 2 13 ? 44.705 109.727 23.816 1.00 22.44 ? 13 ILE B CB 1 ATOM 2042 C CG1 . ILE B 2 13 ? 45.917 109.746 22.896 1.00 22.80 ? 13 ILE B CG1 1 ATOM 2043 C CG2 . ILE B 2 13 ? 45.106 109.325 25.239 1.00 22.98 ? 13 ILE B CG2 1 ATOM 2044 C CD1 . ILE B 2 13 ? 46.943 110.796 23.262 1.00 22.80 ? 13 ILE B CD1 1 ATOM 2045 N N . SER B 2 14 ? 41.931 107.987 24.815 1.00 21.81 ? 14 SER B N 1 ATOM 2046 C CA . SER B 2 14 ? 40.780 108.068 25.685 1.00 21.30 ? 14 SER B CA 1 ATOM 2047 C C . SER B 2 14 ? 41.117 107.724 27.137 1.00 22.25 ? 14 SER B C 1 ATOM 2048 O O . SER B 2 14 ? 42.128 107.091 27.435 1.00 20.65 ? 14 SER B O 1 ATOM 2049 C CB . SER B 2 14 ? 39.659 107.172 25.177 1.00 21.65 ? 14 SER B CB 1 ATOM 2050 O OG . SER B 2 14 ? 40.046 105.814 25.007 1.00 20.79 ? 14 SER B OG 1 ATOM 2051 N N . GLY B 2 15 ? 40.326 108.291 28.030 1.00 21.74 ? 15 GLY B N 1 ATOM 2052 C CA . GLY B 2 15 ? 40.531 108.148 29.444 1.00 22.22 ? 15 GLY B CA 1 ATOM 2053 C C . GLY B 2 15 ? 39.283 108.121 30.288 1.00 21.28 ? 15 GLY B C 1 ATOM 2054 O O . GLY B 2 15 ? 38.391 107.323 30.077 1.00 21.10 ? 15 GLY B O 1 ATOM 2055 N N . ARG B 2 16 ? 39.218 109.057 31.222 1.00 22.33 ? 16 ARG B N 1 ATOM 2056 C CA . ARG B 2 16 ? 38.126 109.104 32.169 1.00 21.90 ? 16 ARG B CA 1 ATOM 2057 C C . ARG B 2 16 ? 36.765 109.095 31.490 1.00 22.31 ? 16 ARG B C 1 ATOM 2058 O O . ARG B 2 16 ? 36.481 109.878 30.600 1.00 21.78 ? 16 ARG B O 1 ATOM 2059 C CB . ARG B 2 16 ? 38.278 110.343 33.048 1.00 23.68 ? 16 ARG B CB 1 ATOM 2060 C CG . ARG B 2 16 ? 37.277 110.429 34.176 1.00 23.43 ? 16 ARG B CG 1 ATOM 2061 C CD . ARG B 2 16 ? 37.654 111.487 35.191 1.00 23.80 ? 16 ARG B CD 1 ATOM 2062 N NE . ARG B 2 16 ? 36.819 111.366 36.371 1.00 23.59 ? 16 ARG B NE 1 ATOM 2063 C CZ . ARG B 2 16 ? 36.915 112.134 37.442 1.00 23.81 ? 16 ARG B CZ 1 ATOM 2064 N NH1 . ARG B 2 16 ? 37.813 113.099 37.490 1.00 23.32 ? 16 ARG B NH1 1 ATOM 2065 N NH2 . ARG B 2 16 ? 36.102 111.935 38.460 1.00 25.38 ? 16 ARG B NH2 1 ATOM 2066 N N . ASP B 2 17 ? 35.943 108.168 31.964 1.00 22.19 ? 17 ASP B N 1 ATOM 2067 C CA . ASP B 2 17 ? 34.590 107.929 31.489 1.00 24.35 ? 17 ASP B CA 1 ATOM 2068 C C . ASP B 2 17 ? 34.511 107.605 29.986 1.00 24.80 ? 17 ASP B C 1 ATOM 2069 O O . ASP B 2 17 ? 33.458 107.715 29.394 1.00 23.70 ? 17 ASP B O 1 ATOM 2070 C CB . ASP B 2 17 ? 33.681 109.135 31.840 1.00 26.27 ? 17 ASP B CB 1 ATOM 2071 C CG . ASP B 2 17 ? 33.199 109.122 33.290 1.00 28.34 ? 17 ASP B CG 1 ATOM 2072 O OD1 . ASP B 2 17 ? 33.660 108.301 34.141 1.00 24.45 ? 17 ASP B OD1 1 ATOM 2073 O OD2 . ASP B 2 17 ? 32.330 109.978 33.566 1.00 29.23 ? 17 ASP B OD2 1 ATOM 2074 N N . GLY B 2 18 ? 35.612 107.152 29.390 1.00 24.61 ? 18 GLY B N 1 ATOM 2075 C CA . GLY B 2 18 ? 35.643 106.876 27.963 1.00 24.41 ? 18 GLY B CA 1 ATOM 2076 C C . GLY B 2 18 ? 35.692 108.103 27.078 1.00 25.03 ? 18 GLY B C 1 ATOM 2077 O O . GLY B 2 18 ? 35.509 107.968 25.877 1.00 25.19 ? 18 GLY B O 1 ATOM 2078 N N . LEU B 2 19 ? 35.956 109.289 27.638 1.00 24.77 ? 19 LEU B N 1 ATOM 2079 C CA . LEU B 2 19 ? 36.082 110.494 26.830 1.00 25.53 ? 19 LEU B CA 1 ATOM 2080 C C . LEU B 2 19 ? 37.485 110.596 26.257 1.00 24.56 ? 19 LEU B C 1 ATOM 2081 O O . LEU B 2 19 ? 38.414 109.972 26.780 1.00 23.59 ? 19 LEU B O 1 ATOM 2082 C CB . LEU B 2 19 ? 35.732 111.748 27.635 1.00 26.74 ? 19 LEU B CB 1 ATOM 2083 C CG . LEU B 2 19 ? 34.300 111.857 28.177 1.00 28.37 ? 19 LEU B CG 1 ATOM 2084 C CD1 . LEU B 2 19 ? 34.120 113.212 28.852 1.00 30.01 ? 19 LEU B CD1 1 ATOM 2085 C CD2 . LEU B 2 19 ? 33.254 111.711 27.094 1.00 30.74 ? 19 LEU B CD2 1 ATOM 2086 N N . CYS B 2 20 ? 37.619 111.390 25.186 1.00 23.26 ? 20 CYS B N 1 ATOM 2087 C CA . CYS B 2 20 ? 38.878 111.524 24.439 1.00 24.25 ? 20 CYS B CA 1 ATOM 2088 C C . CYS B 2 20 ? 39.648 112.771 24.750 1.00 22.47 ? 20 CYS B C 1 ATOM 2089 O O . CYS B 2 20 ? 39.088 113.776 25.178 1.00 23.44 ? 20 CYS B O 1 ATOM 2090 C CB . CYS B 2 20 ? 38.616 111.479 22.930 1.00 26.34 ? 20 CYS B CB 1 ATOM 2091 S SG . CYS B 2 20 ? 38.453 109.795 22.287 1.00 28.04 ? 20 CYS B SG 1 ATOM 2092 N N . VAL B 2 21 ? 40.952 112.711 24.500 1.00 22.10 ? 21 VAL B N 1 ATOM 2093 C CA . VAL B 2 21 ? 41.841 113.853 24.595 1.00 21.07 ? 21 VAL B CA 1 ATOM 2094 C C . VAL B 2 21 ? 41.658 114.680 23.302 1.00 22.93 ? 21 VAL B C 1 ATOM 2095 O O . VAL B 2 21 ? 41.824 114.173 22.175 1.00 21.33 ? 21 VAL B O 1 ATOM 2096 C CB . VAL B 2 21 ? 43.307 113.392 24.758 1.00 21.62 ? 21 VAL B CB 1 ATOM 2097 C CG1 . VAL B 2 21 ? 44.259 114.572 24.802 1.00 21.59 ? 21 VAL B CG1 1 ATOM 2098 C CG2 . VAL B 2 21 ? 43.475 112.529 26.025 1.00 21.63 ? 21 VAL B CG2 1 ATOM 2099 N N . ASP B 2 22 ? 41.319 115.954 23.478 1.00 23.35 ? 22 ASP B N 1 ATOM 2100 C CA . ASP B 2 22 ? 40.766 116.796 22.398 1.00 22.76 ? 22 ASP B CA 1 ATOM 2101 C C . ASP B 2 22 ? 41.374 118.202 22.538 1.00 23.06 ? 22 ASP B C 1 ATOM 2102 O O . ASP B 2 22 ? 41.392 118.761 23.639 1.00 23.36 ? 22 ASP B O 1 ATOM 2103 C CB . ASP B 2 22 ? 39.232 116.779 22.585 1.00 23.76 ? 22 ASP B CB 1 ATOM 2104 C CG . ASP B 2 22 ? 38.463 117.724 21.649 1.00 23.34 ? 22 ASP B CG 1 ATOM 2105 O OD1 . ASP B 2 22 ? 38.710 118.937 21.638 1.00 23.55 ? 22 ASP B OD1 1 ATOM 2106 O OD2 . ASP B 2 22 ? 37.547 117.220 20.989 1.00 24.92 ? 22 ASP B OD2 1 ATOM 2107 N N . VAL B 2 23 ? 41.892 118.774 21.450 1.00 23.01 ? 23 VAL B N 1 ATOM 2108 C CA . VAL B 2 23 ? 42.347 120.165 21.466 1.00 23.27 ? 23 VAL B CA 1 ATOM 2109 C C . VAL B 2 23 ? 41.099 121.037 21.332 1.00 23.82 ? 23 VAL B C 1 ATOM 2110 O O . VAL B 2 23 ? 40.412 120.999 20.294 1.00 24.59 ? 23 VAL B O 1 ATOM 2111 C CB . VAL B 2 23 ? 43.295 120.505 20.309 1.00 23.75 ? 23 VAL B CB 1 ATOM 2112 C CG1 . VAL B 2 23 ? 43.812 121.931 20.444 1.00 24.84 ? 23 VAL B CG1 1 ATOM 2113 C CG2 . VAL B 2 23 ? 44.466 119.542 20.281 1.00 24.30 ? 23 VAL B CG2 1 ATOM 2114 N N . TYR B 2 24 ? 40.802 121.790 22.390 1.00 23.90 ? 24 TYR B N 1 ATOM 2115 C CA . TYR B 2 24 ? 39.548 122.516 22.500 1.00 24.40 ? 24 TYR B CA 1 ATOM 2116 C C . TYR B 2 24 ? 39.384 123.442 21.288 1.00 24.07 ? 24 TYR B C 1 ATOM 2117 O O . TYR B 2 24 ? 40.279 124.200 20.954 1.00 23.53 ? 24 TYR B O 1 ATOM 2118 C CB . TYR B 2 24 ? 39.479 123.326 23.824 1.00 25.79 ? 24 TYR B CB 1 ATOM 2119 C CG . TYR B 2 24 ? 38.428 124.427 23.789 1.00 25.38 ? 24 TYR B CG 1 ATOM 2120 C CD1 . TYR B 2 24 ? 37.079 124.127 23.914 1.00 25.95 ? 24 TYR B CD1 1 ATOM 2121 C CD2 . TYR B 2 24 ? 38.787 125.760 23.560 1.00 27.03 ? 24 TYR B CD2 1 ATOM 2122 C CE1 . TYR B 2 24 ? 36.107 125.137 23.843 1.00 27.56 ? 24 TYR B CE1 1 ATOM 2123 C CE2 . TYR B 2 24 ? 37.820 126.777 23.490 1.00 26.83 ? 24 TYR B CE2 1 ATOM 2124 C CZ . TYR B 2 24 ? 36.491 126.472 23.642 1.00 27.75 ? 24 TYR B CZ 1 ATOM 2125 O OH . TYR B 2 24 ? 35.530 127.511 23.562 1.00 28.93 ? 24 TYR B OH 1 ATOM 2126 N N . GLY B 2 25 ? 38.247 123.306 20.622 1.00 25.65 ? 25 GLY B N 1 ATOM 2127 C CA . GLY B 2 25 ? 37.869 124.165 19.480 1.00 26.85 ? 25 GLY B CA 1 ATOM 2128 C C . GLY B 2 25 ? 38.725 123.949 18.248 1.00 27.85 ? 25 GLY B C 1 ATOM 2129 O O . GLY B 2 25 ? 38.686 124.748 17.317 1.00 25.64 ? 25 GLY B O 1 ATOM 2130 N N . ALA B 2 26 ? 39.542 122.896 18.248 1.00 26.68 ? 26 ALA B N 1 ATOM 2131 C CA . ALA B 2 26 ? 40.586 122.711 17.229 1.00 26.18 ? 26 ALA B CA 1 ATOM 2132 C C . ALA B 2 26 ? 41.464 123.941 17.030 1.00 26.80 ? 26 ALA B C 1 ATOM 2133 O O . ALA B 2 26 ? 41.923 124.196 15.930 1.00 26.89 ? 26 ALA B O 1 ATOM 2134 C CB . ALA B 2 26 ? 39.962 122.264 15.911 1.00 25.83 ? 26 ALA B CB 1 ATOM 2135 N N . LEU B 2 27 ? 41.716 124.697 18.098 1.00 27.98 ? 27 LEU B N 1 ATOM 2136 C CA . LEU B 2 27 ? 42.550 125.895 18.028 1.00 27.09 ? 27 LEU B CA 1 ATOM 2137 C C . LEU B 2 27 ? 44.012 125.540 17.948 1.00 29.96 ? 27 LEU B C 1 ATOM 2138 O O . LEU B 2 27 ? 44.465 124.571 18.580 1.00 29.21 ? 27 LEU B O 1 ATOM 2139 C CB . LEU B 2 27 ? 42.290 126.797 19.235 1.00 28.60 ? 27 LEU B CB 1 ATOM 2140 C CG . LEU B 2 27 ? 40.853 127.299 19.402 1.00 28.96 ? 27 LEU B CG 1 ATOM 2141 C CD1 . LEU B 2 27 ? 40.711 127.989 20.758 1.00 30.67 ? 27 LEU B CD1 1 ATOM 2142 C CD2 . LEU B 2 27 ? 40.462 128.238 18.261 1.00 30.48 ? 27 LEU B CD2 1 ATOM 2143 N N . THR B 2 28 ? 44.767 126.324 17.175 1.00 30.20 ? 28 THR B N 1 ATOM 2144 C CA . THR B 2 28 ? 46.129 125.953 16.805 1.00 30.15 ? 28 THR B CA 1 ATOM 2145 C C . THR B 2 28 ? 47.181 126.845 17.409 1.00 29.89 ? 28 THR B C 1 ATOM 2146 O O . THR B 2 28 ? 48.377 126.562 17.269 1.00 31.74 ? 28 THR B O 1 ATOM 2147 C CB . THR B 2 28 ? 46.316 125.959 15.277 1.00 31.01 ? 28 THR B CB 1 ATOM 2148 O OG1 . THR B 2 28 ? 46.015 127.265 14.766 1.00 32.04 ? 28 THR B OG1 1 ATOM 2149 C CG2 . THR B 2 28 ? 45.396 124.963 14.610 1.00 32.52 ? 28 THR B CG2 1 ATOM 2150 N N . ALA B 2 29 ? 46.766 127.911 18.092 1.00 30.89 ? 29 ALA B N 1 ATOM 2151 C CA . ALA B 2 29 ? 47.723 128.832 18.691 1.00 31.56 ? 29 ALA B CA 1 ATOM 2152 C C . ALA B 2 29 ? 48.490 128.124 19.801 1.00 33.33 ? 29 ALA B C 1 ATOM 2153 O O . ALA B 2 29 ? 47.929 127.277 20.516 1.00 32.95 ? 29 ALA B O 1 ATOM 2154 C CB . ALA B 2 29 ? 46.998 130.053 19.246 1.00 32.80 ? 29 ALA B CB 1 ATOM 2155 N N . ASP B 2 30 ? 49.760 128.482 19.943 1.00 32.96 ? 30 ASP B N 1 ATOM 2156 C CA . ASP B 2 30 ? 50.590 127.997 21.026 1.00 33.29 ? 30 ASP B CA 1 ATOM 2157 C C . ASP B 2 30 ? 49.880 128.199 22.341 1.00 34.38 ? 30 ASP B C 1 ATOM 2158 O O . ASP B 2 30 ? 49.350 129.288 22.608 1.00 37.07 ? 30 ASP B O 1 ATOM 2159 C CB . ASP B 2 30 ? 51.920 128.751 21.036 1.00 34.71 ? 30 ASP B CB 1 ATOM 2160 C CG . ASP B 2 30 ? 52.816 128.381 19.873 1.00 37.55 ? 30 ASP B CG 1 ATOM 2161 O OD1 . ASP B 2 30 ? 52.481 127.427 19.126 1.00 37.24 ? 30 ASP B OD1 1 ATOM 2162 O OD2 . ASP B 2 30 ? 53.881 129.049 19.709 1.00 42.20 ? 30 ASP B OD2 1 ATOM 2163 N N . GLY B 2 31 ? 49.827 127.148 23.166 1.00 30.43 ? 31 GLY B N 1 ATOM 2164 C CA . GLY B 2 31 ? 49.162 127.223 24.450 1.00 27.75 ? 31 GLY B CA 1 ATOM 2165 C C . GLY B 2 31 ? 47.706 126.848 24.424 1.00 28.45 ? 31 GLY B C 1 ATOM 2166 O O . GLY B 2 31 ? 47.049 126.884 25.457 1.00 30.38 ? 31 GLY B O 1 ATOM 2167 N N . SER B 2 32 ? 47.181 126.499 23.254 1.00 29.48 ? 32 SER B N 1 ATOM 2168 C CA . SER B 2 32 ? 45.818 126.042 23.125 1.00 27.72 ? 32 SER B CA 1 ATOM 2169 C C . SER B 2 32 ? 45.573 124.811 24.005 1.00 29.15 ? 32 SER B C 1 ATOM 2170 O O . SER B 2 32 ? 46.293 123.821 23.892 1.00 27.68 ? 32 SER B O 1 ATOM 2171 C CB . SER B 2 32 ? 45.546 125.671 21.684 1.00 29.01 ? 32 SER B CB 1 ATOM 2172 O OG . SER B 2 32 ? 45.453 126.820 20.860 1.00 28.96 ? 32 SER B OG 1 ATOM 2173 N N . ARG B 2 33 ? 44.548 124.863 24.851 1.00 27.51 ? 33 ARG B N 1 ATOM 2174 C CA . ARG B 2 33 ? 44.369 123.837 25.867 1.00 28.20 ? 33 ARG B CA 1 ATOM 2175 C C . ARG B 2 33 ? 43.776 122.555 25.316 1.00 27.95 ? 33 ARG B C 1 ATOM 2176 O O . ARG B 2 33 ? 43.061 122.565 24.304 1.00 25.65 ? 33 ARG B O 1 ATOM 2177 C CB . ARG B 2 33 ? 43.503 124.359 27.016 1.00 28.62 ? 33 ARG B CB 1 ATOM 2178 C CG . ARG B 2 33 ? 42.044 124.618 26.687 1.00 28.67 ? 33 ARG B CG 1 ATOM 2179 C CD . ARG B 2 33 ? 41.377 125.180 27.908 1.00 30.20 ? 33 ARG B CD 1 ATOM 2180 N NE . ARG B 2 33 ? 39.926 125.262 27.775 1.00 31.78 ? 33 ARG B NE 1 ATOM 2181 C CZ . ARG B 2 33 ? 39.277 126.259 27.197 1.00 31.92 ? 33 ARG B CZ 1 ATOM 2182 N NH1 . ARG B 2 33 ? 39.939 127.276 26.643 1.00 33.31 ? 33 ARG B NH1 1 ATOM 2183 N NH2 . ARG B 2 33 ? 37.958 126.221 27.152 1.00 33.79 ? 33 ARG B NH2 1 ATOM 2184 N N . VAL B 2 34 ? 44.062 121.445 26.006 1.00 27.65 ? 34 VAL B N 1 ATOM 2185 C CA . VAL B 2 34 ? 43.408 120.174 25.705 1.00 26.47 ? 34 VAL B CA 1 ATOM 2186 C C . VAL B 2 34 ? 42.400 119.806 26.803 1.00 24.18 ? 34 VAL B C 1 ATOM 2187 O O . VAL B 2 34 ? 42.628 120.036 27.992 1.00 23.99 ? 34 VAL B O 1 ATOM 2188 C CB . VAL B 2 34 ? 44.432 119.028 25.435 1.00 29.42 ? 34 VAL B CB 1 ATOM 2189 C CG1 . VAL B 2 34 ? 45.518 119.503 24.475 1.00 30.26 ? 34 VAL B CG1 1 ATOM 2190 C CG2 . VAL B 2 34 ? 45.072 118.529 26.711 1.00 31.28 ? 34 VAL B CG2 1 ATOM 2191 N N . ILE B 2 35 ? 41.308 119.186 26.388 1.00 23.60 ? 35 ILE B N 1 ATOM 2192 C CA . ILE B 2 35 ? 40.182 118.880 27.248 1.00 23.67 ? 35 ILE B CA 1 ATOM 2193 C C . ILE B 2 35 ? 39.753 117.440 27.062 1.00 24.88 ? 35 ILE B C 1 ATOM 2194 O O . ILE B 2 35 ? 40.190 116.811 26.099 1.00 27.49 ? 35 ILE B O 1 ATOM 2195 C CB . ILE B 2 35 ? 38.967 119.798 26.901 1.00 23.34 ? 35 ILE B CB 1 ATOM 2196 C CG1 . ILE B 2 35 ? 38.529 119.652 25.434 1.00 24.15 ? 35 ILE B CG1 1 ATOM 2197 C CG2 . ILE B 2 35 ? 39.310 121.243 27.218 1.00 25.27 ? 35 ILE B CG2 1 ATOM 2198 C CD1 . ILE B 2 35 ? 37.176 120.272 25.080 1.00 23.49 ? 35 ILE B CD1 1 ATOM 2199 N N . LEU B 2 36 ? 38.875 116.948 27.937 1.00 22.76 ? 36 LEU B N 1 ATOM 2200 C CA . LEU B 2 36 ? 38.033 115.804 27.634 1.00 24.43 ? 36 LEU B CA 1 ATOM 2201 C C . LEU B 2 36 ? 36.902 116.167 26.677 1.00 24.33 ? 36 LEU B C 1 ATOM 2202 O O . LEU B 2 36 ? 36.275 117.223 26.810 1.00 22.53 ? 36 LEU B O 1 ATOM 2203 C CB . LEU B 2 36 ? 37.368 115.239 28.890 1.00 25.32 ? 36 LEU B CB 1 ATOM 2204 C CG . LEU B 2 36 ? 38.184 114.533 29.950 1.00 26.48 ? 36 LEU B CG 1 ATOM 2205 C CD1 . LEU B 2 36 ? 37.234 114.069 31.043 1.00 27.07 ? 36 LEU B CD1 1 ATOM 2206 C CD2 . LEU B 2 36 ? 38.957 113.356 29.350 1.00 26.10 ? 36 LEU B CD2 1 ATOM 2207 N N . TYR B 2 37 ? 36.587 115.257 25.764 1.00 24.08 ? 37 TYR B N 1 ATOM 2208 C CA . TYR B 2 37 ? 35.469 115.480 24.857 1.00 24.24 ? 37 TYR B CA 1 ATOM 2209 C C . TYR B 2 37 ? 34.961 114.167 24.345 1.00 24.29 ? 37 TYR B C 1 ATOM 2210 O O . TYR B 2 37 ? 35.766 113.211 24.231 1.00 23.51 ? 37 TYR B O 1 ATOM 2211 C CB . TYR B 2 37 ? 35.902 116.410 23.710 1.00 24.60 ? 37 TYR B CB 1 ATOM 2212 C CG . TYR B 2 37 ? 34.742 117.141 23.073 1.00 24.95 ? 37 TYR B CG 1 ATOM 2213 C CD1 . TYR B 2 37 ? 34.114 118.206 23.738 1.00 25.07 ? 37 TYR B CD1 1 ATOM 2214 C CD2 . TYR B 2 37 ? 34.258 116.761 21.817 1.00 25.35 ? 37 TYR B CD2 1 ATOM 2215 C CE1 . TYR B 2 37 ? 33.031 118.874 23.147 1.00 25.40 ? 37 TYR B CE1 1 ATOM 2216 C CE2 . TYR B 2 37 ? 33.184 117.413 21.219 1.00 25.40 ? 37 TYR B CE2 1 ATOM 2217 C CZ . TYR B 2 37 ? 32.565 118.469 21.885 1.00 26.55 ? 37 TYR B CZ 1 ATOM 2218 O OH . TYR B 2 37 ? 31.482 119.089 21.255 1.00 26.05 ? 37 TYR B OH 1 ATOM 2219 N N . PRO B 2 38 ? 33.643 114.076 24.050 1.00 23.37 ? 38 PRO B N 1 ATOM 2220 C CA . PRO B 2 38 ? 33.186 112.812 23.479 1.00 24.74 ? 38 PRO B CA 1 ATOM 2221 C C . PRO B 2 38 ? 33.967 112.448 22.218 1.00 25.73 ? 38 PRO B C 1 ATOM 2222 O O . PRO B 2 38 ? 34.302 113.329 21.407 1.00 22.72 ? 38 PRO B O 1 ATOM 2223 C CB . PRO B 2 38 ? 31.692 113.058 23.174 1.00 24.91 ? 38 PRO B CB 1 ATOM 2224 C CG . PRO B 2 38 ? 31.282 114.173 24.087 1.00 25.12 ? 38 PRO B CG 1 ATOM 2225 C CD . PRO B 2 38 ? 32.511 114.996 24.347 1.00 24.02 ? 38 PRO B CD 1 ATOM 2226 N N . CYS B 2 39 ? 34.270 111.154 22.085 1.00 25.15 ? 39 CYS B N 1 ATOM 2227 C CA . CYS B 2 39 ? 35.155 110.687 21.042 1.00 25.87 ? 39 CYS B CA 1 ATOM 2228 C C . CYS B 2 39 ? 34.528 110.825 19.659 1.00 25.25 ? 39 CYS B C 1 ATOM 2229 O O . CYS B 2 39 ? 33.383 110.481 19.465 1.00 24.34 ? 39 CYS B O 1 ATOM 2230 C CB . CYS B 2 39 ? 35.548 109.237 21.330 1.00 28.56 ? 39 CYS B CB 1 ATOM 2231 S SG . CYS B 2 39 ? 36.593 109.128 22.840 1.00 30.37 ? 39 CYS B SG 1 ATOM 2232 N N . GLY B 2 40 ? 35.292 111.315 18.698 1.00 25.58 ? 40 GLY B N 1 ATOM 2233 C CA . GLY B 2 40 ? 34.837 111.337 17.303 1.00 26.12 ? 40 GLY B CA 1 ATOM 2234 C C . GLY B 2 40 ? 36.008 111.255 16.336 1.00 26.96 ? 40 GLY B C 1 ATOM 2235 O O . GLY B 2 40 ? 37.142 110.941 16.739 1.00 26.41 ? 40 GLY B O 1 ATOM 2236 N N . GLN B 2 41 ? 35.734 111.571 15.069 1.00 26.78 ? 41 GLN B N 1 ATOM 2237 C CA . GLN B 2 41 ? 36.716 111.482 13.992 1.00 29.30 ? 41 GLN B CA 1 ATOM 2238 C C . GLN B 2 41 ? 37.476 112.745 13.711 1.00 27.60 ? 41 GLN B C 1 ATOM 2239 O O . GLN B 2 41 ? 38.359 112.741 12.874 1.00 27.69 ? 41 GLN B O 1 ATOM 2240 C CB . GLN B 2 41 ? 36.014 111.048 12.696 1.00 33.81 ? 41 GLN B CB 1 ATOM 2241 C CG . GLN B 2 41 ? 35.184 109.789 12.853 1.00 37.75 ? 41 GLN B CG 1 ATOM 2242 C CD . GLN B 2 41 ? 36.022 108.697 13.447 1.00 41.67 ? 41 GLN B CD 1 ATOM 2243 O OE1 . GLN B 2 41 ? 37.128 108.465 12.976 1.00 49.57 ? 41 GLN B OE1 1 ATOM 2244 N NE2 . GLN B 2 41 ? 35.553 108.076 14.531 1.00 43.29 ? 41 GLN B NE2 1 ATOM 2245 N N . GLN B 2 42 ? 37.156 113.828 14.400 1.00 27.10 ? 42 GLN B N 1 ATOM 2246 C CA . GLN B 2 42 ? 37.760 115.126 14.097 1.00 26.42 ? 42 GLN B CA 1 ATOM 2247 C C . GLN B 2 42 ? 39.262 115.105 14.309 1.00 27.26 ? 42 GLN B C 1 ATOM 2248 O O . GLN B 2 42 ? 39.770 114.391 15.195 1.00 26.40 ? 42 GLN B O 1 ATOM 2249 C CB . GLN B 2 42 ? 37.106 116.247 14.930 1.00 26.68 ? 42 GLN B CB 1 ATOM 2250 C CG . GLN B 2 42 ? 37.107 116.023 16.450 1.00 25.61 ? 42 GLN B CG 1 ATOM 2251 C CD . GLN B 2 42 ? 35.817 115.443 16.997 1.00 25.77 ? 42 GLN B CD 1 ATOM 2252 O OE1 . GLN B 2 42 ? 35.332 114.404 16.543 1.00 26.15 ? 42 GLN B OE1 1 ATOM 2253 N NE2 . GLN B 2 42 ? 35.270 116.089 18.009 1.00 26.16 ? 42 GLN B NE2 1 ATOM 2254 N N . GLN B 2 43 ? 39.961 115.922 13.524 1.00 27.08 ? 43 GLN B N 1 ATOM 2255 C CA . GLN B 2 43 ? 41.429 115.989 13.496 1.00 28.32 ? 43 GLN B CA 1 ATOM 2256 C C . GLN B 2 43 ? 42.081 116.367 14.816 1.00 26.96 ? 43 GLN B C 1 ATOM 2257 O O . GLN B 2 43 ? 43.222 115.942 15.113 1.00 25.00 ? 43 GLN B O 1 ATOM 2258 C CB . GLN B 2 43 ? 41.886 117.021 12.451 1.00 31.95 ? 43 GLN B CB 1 ATOM 2259 C CG . GLN B 2 43 ? 41.533 116.673 11.013 1.00 35.83 ? 43 GLN B CG 1 ATOM 2260 C CD . GLN B 2 43 ? 42.330 115.499 10.527 1.00 41.66 ? 43 GLN B CD 1 ATOM 2261 O OE1 . GLN B 2 43 ? 41.844 114.370 10.542 1.00 49.43 ? 43 GLN B OE1 1 ATOM 2262 N NE2 . GLN B 2 43 ? 43.574 115.747 10.111 1.00 46.87 ? 43 GLN B NE2 1 ATOM 2263 N N . ASN B 2 44 ? 41.388 117.216 15.582 1.00 24.52 ? 44 ASN B N 1 ATOM 2264 C CA . ASN B 2 44 ? 41.875 117.644 16.893 1.00 24.39 ? 44 ASN B CA 1 ATOM 2265 C C . ASN B 2 44 ? 41.748 116.566 17.987 1.00 23.20 ? 44 ASN B C 1 ATOM 2266 O O . ASN B 2 44 ? 42.061 116.837 19.156 1.00 23.17 ? 44 ASN B O 1 ATOM 2267 C CB . ASN B 2 44 ? 41.186 118.963 17.323 1.00 24.79 ? 44 ASN B CB 1 ATOM 2268 C CG . ASN B 2 44 ? 39.680 118.842 17.354 1.00 24.17 ? 44 ASN B CG 1 ATOM 2269 O OD1 . ASN B 2 44 ? 39.074 118.457 16.368 1.00 24.67 ? 44 ASN B OD1 1 ATOM 2270 N ND2 . ASN B 2 44 ? 39.080 119.101 18.492 1.00 26.30 ? 44 ASN B ND2 1 ATOM 2271 N N . GLN B 2 45 ? 41.259 115.368 17.640 1.00 22.80 ? 45 GLN B N 1 ATOM 2272 C CA . GLN B 2 45 ? 41.386 114.194 18.523 1.00 22.94 ? 45 GLN B CA 1 ATOM 2273 C C . GLN B 2 45 ? 42.391 113.155 17.998 1.00 23.75 ? 45 GLN B C 1 ATOM 2274 O O . GLN B 2 45 ? 42.503 112.071 18.572 1.00 23.14 ? 45 GLN B O 1 ATOM 2275 C CB . GLN B 2 45 ? 40.043 113.530 18.761 1.00 22.94 ? 45 GLN B CB 1 ATOM 2276 C CG . GLN B 2 45 ? 39.138 114.333 19.699 1.00 24.00 ? 45 GLN B CG 1 ATOM 2277 C CD . GLN B 2 45 ? 37.833 113.640 19.941 1.00 23.65 ? 45 GLN B CD 1 ATOM 2278 O OE1 . GLN B 2 45 ? 37.644 112.509 19.516 1.00 24.83 ? 45 GLN B OE1 1 ATOM 2279 N NE2 . GLN B 2 45 ? 36.910 114.309 20.611 1.00 25.43 ? 45 GLN B NE2 1 ATOM 2280 N N . GLN B 2 46 ? 43.105 113.482 16.923 1.00 23.88 ? 46 GLN B N 1 ATOM 2281 C CA . GLN B 2 46 ? 44.080 112.579 16.315 1.00 24.82 ? 46 GLN B CA 1 ATOM 2282 C C . GLN B 2 46 ? 45.437 112.960 16.813 1.00 23.75 ? 46 GLN B C 1 ATOM 2283 O O . GLN B 2 46 ? 45.881 114.097 16.622 1.00 24.13 ? 46 GLN B O 1 ATOM 2284 C CB . GLN B 2 46 ? 44.042 112.661 14.792 1.00 26.07 ? 46 GLN B CB 1 ATOM 2285 C CG . GLN B 2 46 ? 42.763 112.132 14.212 1.00 27.78 ? 46 GLN B CG 1 ATOM 2286 C CD . GLN B 2 46 ? 42.709 112.283 12.706 1.00 33.64 ? 46 GLN B CD 1 ATOM 2287 O OE1 . GLN B 2 46 ? 43.716 112.576 12.052 1.00 38.82 ? 46 GLN B OE1 1 ATOM 2288 N NE2 . GLN B 2 46 ? 41.531 112.086 12.142 1.00 38.84 ? 46 GLN B NE2 1 ATOM 2289 N N . TRP B 2 47 ? 46.083 112.005 17.489 1.00 22.56 ? 47 TRP B N 1 ATOM 2290 C CA . TRP B 2 47 ? 47.362 112.209 18.111 1.00 21.92 ? 47 TRP B CA 1 ATOM 2291 C C . TRP B 2 47 ? 48.369 111.319 17.407 1.00 22.78 ? 47 TRP B C 1 ATOM 2292 O O . TRP B 2 47 ? 48.167 110.103 17.338 1.00 22.49 ? 47 TRP B O 1 ATOM 2293 C CB . TRP B 2 47 ? 47.249 111.886 19.603 1.00 22.62 ? 47 TRP B CB 1 ATOM 2294 C CG . TRP B 2 47 ? 46.365 112.878 20.269 1.00 22.28 ? 47 TRP B CG 1 ATOM 2295 C CD1 . TRP B 2 47 ? 45.048 112.735 20.537 1.00 21.49 ? 47 TRP B CD1 1 ATOM 2296 C CD2 . TRP B 2 47 ? 46.714 114.210 20.624 1.00 21.31 ? 47 TRP B CD2 1 ATOM 2297 N NE1 . TRP B 2 47 ? 44.557 113.886 21.100 1.00 22.34 ? 47 TRP B NE1 1 ATOM 2298 C CE2 . TRP B 2 47 ? 45.561 114.813 21.157 1.00 22.27 ? 47 TRP B CE2 1 ATOM 2299 C CE3 . TRP B 2 47 ? 47.895 114.954 20.550 1.00 22.17 ? 47 TRP B CE3 1 ATOM 2300 C CZ2 . TRP B 2 47 ? 45.548 116.129 21.623 1.00 22.00 ? 47 TRP B CZ2 1 ATOM 2301 C CZ3 . TRP B 2 47 ? 47.892 116.267 21.024 1.00 22.70 ? 47 TRP B CZ3 1 ATOM 2302 C CH2 . TRP B 2 47 ? 46.719 116.836 21.552 1.00 22.25 ? 47 TRP B CH2 1 ATOM 2303 N N . THR B 2 48 ? 49.415 111.922 16.855 1.00 22.45 ? 48 THR B N 1 ATOM 2304 C CA . THR B 2 48 ? 50.431 111.200 16.132 1.00 23.72 ? 48 THR B CA 1 ATOM 2305 C C . THR B 2 48 ? 51.657 111.071 17.004 1.00 24.48 ? 48 THR B C 1 ATOM 2306 O O . THR B 2 48 ? 52.228 112.072 17.481 1.00 24.70 ? 48 THR B O 1 ATOM 2307 C CB . THR B 2 48 ? 50.765 111.857 14.761 1.00 23.60 ? 48 THR B CB 1 ATOM 2308 O OG1 . THR B 2 48 ? 49.564 111.919 13.988 1.00 22.99 ? 48 THR B OG1 1 ATOM 2309 C CG2 . THR B 2 48 ? 51.797 111.028 13.978 1.00 22.97 ? 48 THR B CG2 1 ATOM 2310 N N . PHE B 2 49 ? 52.048 109.817 17.216 1.00 23.88 ? 49 PHE B N 1 ATOM 2311 C CA . PHE B 2 49 ? 53.200 109.469 18.026 1.00 23.39 ? 49 PHE B CA 1 ATOM 2312 C C . PHE B 2 49 ? 54.428 109.289 17.141 1.00 23.40 ? 49 PHE B C 1 ATOM 2313 O O . PHE B 2 49 ? 54.343 108.651 16.091 1.00 24.60 ? 49 PHE B O 1 ATOM 2314 C CB . PHE B 2 49 ? 52.925 108.176 18.788 1.00 23.75 ? 49 PHE B CB 1 ATOM 2315 C CG . PHE B 2 49 ? 51.945 108.347 19.911 1.00 23.56 ? 49 PHE B CG 1 ATOM 2316 C CD1 . PHE B 2 49 ? 50.598 108.522 19.637 1.00 23.26 ? 49 PHE B CD1 1 ATOM 2317 C CD2 . PHE B 2 49 ? 52.360 108.336 21.224 1.00 22.78 ? 49 PHE B CD2 1 ATOM 2318 C CE1 . PHE B 2 49 ? 49.683 108.695 20.659 1.00 23.08 ? 49 PHE B CE1 1 ATOM 2319 C CE2 . PHE B 2 49 ? 51.455 108.497 22.257 1.00 22.73 ? 49 PHE B CE2 1 ATOM 2320 C CZ . PHE B 2 49 ? 50.108 108.684 21.964 1.00 23.54 ? 49 PHE B CZ 1 ATOM 2321 N N . TYR B 2 50 ? 55.554 109.852 17.577 1.00 24.45 ? 50 TYR B N 1 ATOM 2322 C CA . TYR B 2 50 ? 56.823 109.749 16.846 1.00 25.83 ? 50 TYR B CA 1 ATOM 2323 C C . TYR B 2 50 ? 57.889 109.204 17.780 1.00 25.85 ? 50 TYR B C 1 ATOM 2324 O O . TYR B 2 50 ? 57.748 109.310 18.993 1.00 25.36 ? 50 TYR B O 1 ATOM 2325 C CB . TYR B 2 50 ? 57.267 111.118 16.307 1.00 26.22 ? 50 TYR B CB 1 ATOM 2326 C CG . TYR B 2 50 ? 56.314 111.754 15.335 1.00 26.60 ? 50 TYR B CG 1 ATOM 2327 C CD1 . TYR B 2 50 ? 55.253 112.532 15.793 1.00 26.88 ? 50 TYR B CD1 1 ATOM 2328 C CD2 . TYR B 2 50 ? 56.489 111.620 13.959 1.00 27.26 ? 50 TYR B CD2 1 ATOM 2329 C CE1 . TYR B 2 50 ? 54.385 113.147 14.912 1.00 27.59 ? 50 TYR B CE1 1 ATOM 2330 C CE2 . TYR B 2 50 ? 55.623 112.241 13.061 1.00 27.89 ? 50 TYR B CE2 1 ATOM 2331 C CZ . TYR B 2 50 ? 54.564 112.995 13.552 1.00 28.55 ? 50 TYR B CZ 1 ATOM 2332 O OH . TYR B 2 50 ? 53.671 113.608 12.695 1.00 29.61 ? 50 TYR B OH 1 ATOM 2333 N N . PRO B 2 51 ? 58.986 108.648 17.220 1.00 27.29 ? 51 PRO B N 1 ATOM 2334 C CA . PRO B 2 51 ? 60.043 108.103 18.087 1.00 27.87 ? 51 PRO B CA 1 ATOM 2335 C C . PRO B 2 51 ? 60.883 109.112 18.846 1.00 28.22 ? 51 PRO B C 1 ATOM 2336 O O . PRO B 2 51 ? 61.663 108.722 19.698 1.00 30.21 ? 51 PRO B O 1 ATOM 2337 C CB . PRO B 2 51 ? 60.906 107.279 17.142 1.00 27.55 ? 51 PRO B CB 1 ATOM 2338 C CG . PRO B 2 51 ? 60.587 107.731 15.784 1.00 27.92 ? 51 PRO B CG 1 ATOM 2339 C CD . PRO B 2 51 ? 59.218 108.345 15.801 1.00 27.71 ? 51 PRO B CD 1 ATOM 2340 N N . ASP B 2 52 ? 60.697 110.401 18.586 1.00 29.01 ? 52 ASP B N 1 ATOM 2341 C CA . ASP B 2 52 ? 61.266 111.441 19.453 1.00 28.86 ? 52 ASP B CA 1 ATOM 2342 C C . ASP B 2 52 ? 60.457 111.711 20.743 1.00 29.97 ? 52 ASP B C 1 ATOM 2343 O O . ASP B 2 52 ? 60.718 112.695 21.447 1.00 29.88 ? 52 ASP B O 1 ATOM 2344 C CB . ASP B 2 52 ? 61.406 112.734 18.646 1.00 29.83 ? 52 ASP B CB 1 ATOM 2345 C CG . ASP B 2 52 ? 60.069 113.290 18.183 1.00 30.25 ? 52 ASP B CG 1 ATOM 2346 O OD1 . ASP B 2 52 ? 58.994 112.697 18.497 1.00 29.69 ? 52 ASP B OD1 1 ATOM 2347 O OD2 . ASP B 2 52 ? 60.096 114.313 17.480 1.00 30.04 ? 52 ASP B OD2 1 ATOM 2348 N N . ASN B 2 53 ? 59.460 110.871 21.044 1.00 29.39 ? 53 ASN B N 1 ATOM 2349 C CA . ASN B 2 53 ? 58.627 111.012 22.257 1.00 27.52 ? 53 ASN B CA 1 ATOM 2350 C C . ASN B 2 53 ? 57.730 112.238 22.251 1.00 27.08 ? 53 ASN B C 1 ATOM 2351 O O . ASN B 2 53 ? 57.342 112.760 23.311 1.00 27.08 ? 53 ASN B O 1 ATOM 2352 C CB . ASN B 2 53 ? 59.474 110.967 23.532 1.00 30.00 ? 53 ASN B CB 1 ATOM 2353 C CG . ASN B 2 53 ? 60.237 109.662 23.665 1.00 32.35 ? 53 ASN B CG 1 ATOM 2354 O OD1 . ASN B 2 53 ? 59.706 108.590 23.372 1.00 33.47 ? 53 ASN B OD1 1 ATOM 2355 N ND2 . ASN B 2 53 ? 61.479 109.744 24.119 1.00 34.07 ? 53 ASN B ND2 1 ATOM 2356 N N . THR B 2 54 ? 57.356 112.674 21.058 1.00 25.65 ? 54 THR B N 1 ATOM 2357 C CA . THR B 2 54 ? 56.355 113.709 20.923 1.00 25.03 ? 54 THR B CA 1 ATOM 2358 C C . THR B 2 54 ? 55.053 113.058 20.581 1.00 24.36 ? 54 THR B C 1 ATOM 2359 O O . THR B 2 54 ? 55.003 111.940 20.015 1.00 23.98 ? 54 THR B O 1 ATOM 2360 C CB . THR B 2 54 ? 56.716 114.761 19.858 1.00 24.43 ? 54 THR B CB 1 ATOM 2361 O OG1 . THR B 2 54 ? 56.830 114.139 18.573 1.00 25.29 ? 54 THR B OG1 1 ATOM 2362 C CG2 . THR B 2 54 ? 58.008 115.456 20.215 1.00 24.16 ? 54 THR B CG2 1 ATOM 2363 N N . ILE B 2 55 ? 53.993 113.753 20.971 1.00 23.53 ? 55 ILE B N 1 ATOM 2364 C CA . ILE B 2 55 ? 52.632 113.345 20.734 1.00 23.29 ? 55 ILE B CA 1 ATOM 2365 C C . ILE B 2 55 ? 51.942 114.577 20.160 1.00 23.37 ? 55 ILE B C 1 ATOM 2366 O O . ILE B 2 55 ? 51.825 115.602 20.854 1.00 24.33 ? 55 ILE B O 1 ATOM 2367 C CB . ILE B 2 55 ? 51.950 112.899 22.041 1.00 23.65 ? 55 ILE B CB 1 ATOM 2368 C CG1 . ILE B 2 55 ? 52.789 111.816 22.730 1.00 24.36 ? 55 ILE B CG1 1 ATOM 2369 C CG2 . ILE B 2 55 ? 50.532 112.410 21.751 1.00 23.80 ? 55 ILE B CG2 1 ATOM 2370 C CD1 . ILE B 2 55 ? 52.257 111.357 24.077 1.00 23.58 ? 55 ILE B CD1 1 ATOM 2371 N N . ARG B 2 56 ? 51.482 114.480 18.915 1.00 24.30 ? 56 ARG B N 1 ATOM 2372 C CA . ARG B 2 56 ? 51.107 115.677 18.127 1.00 24.27 ? 56 ARG B CA 1 ATOM 2373 C C . ARG B 2 56 ? 49.710 115.667 17.601 1.00 24.03 ? 56 ARG B C 1 ATOM 2374 O O . ARG B 2 56 ? 49.233 114.637 17.123 1.00 25.38 ? 56 ARG B O 1 ATOM 2375 C CB . ARG B 2 56 ? 52.054 115.847 16.943 1.00 24.57 ? 56 ARG B CB 1 ATOM 2376 C CG . ARG B 2 56 ? 53.506 115.824 17.369 1.00 24.41 ? 56 ARG B CG 1 ATOM 2377 C CD . ARG B 2 56 ? 54.420 116.366 16.287 1.00 25.31 ? 56 ARG B CD 1 ATOM 2378 N NE . ARG B 2 56 ? 55.827 116.052 16.572 1.00 26.07 ? 56 ARG B NE 1 ATOM 2379 C CZ . ARG B 2 56 ? 56.878 116.605 15.970 1.00 27.53 ? 56 ARG B CZ 1 ATOM 2380 N NH1 . ARG B 2 56 ? 56.712 117.535 15.036 1.00 29.13 ? 56 ARG B NH1 1 ATOM 2381 N NH2 . ARG B 2 56 ? 58.110 116.241 16.317 1.00 28.61 ? 56 ARG B NH2 1 ATOM 2382 N N . SER B 2 57 ? 49.047 116.824 17.649 1.00 24.65 ? 57 SER B N 1 ATOM 2383 C CA . SER B 2 57 ? 47.778 117.011 16.946 1.00 23.99 ? 57 SER B CA 1 ATOM 2384 C C . SER B 2 57 ? 47.799 118.389 16.311 1.00 24.96 ? 57 SER B C 1 ATOM 2385 O O . SER B 2 57 ? 48.389 119.312 16.870 1.00 25.27 ? 57 SER B O 1 ATOM 2386 C CB . SER B 2 57 ? 46.579 116.913 17.874 1.00 24.23 ? 57 SER B CB 1 ATOM 2387 O OG . SER B 2 57 ? 45.352 116.870 17.141 1.00 24.31 ? 57 SER B OG 1 ATOM 2388 N N . LEU B 2 58 ? 47.155 118.501 15.153 1.00 25.51 ? 58 LEU B N 1 ATOM 2389 C CA . LEU B 2 58 ? 47.126 119.751 14.367 1.00 26.68 ? 58 LEU B CA 1 ATOM 2390 C C . LEU B 2 58 ? 48.526 120.230 14.035 1.00 28.18 ? 58 LEU B C 1 ATOM 2391 O O . LEU B 2 58 ? 48.746 121.420 13.910 1.00 28.89 ? 58 LEU B O 1 ATOM 2392 C CB . LEU B 2 58 ? 46.358 120.834 15.145 1.00 26.42 ? 58 LEU B CB 1 ATOM 2393 C CG . LEU B 2 58 ? 45.020 120.340 15.706 1.00 26.19 ? 58 LEU B CG 1 ATOM 2394 C CD1 . LEU B 2 58 ? 44.354 121.422 16.537 1.00 27.97 ? 58 LEU B CD1 1 ATOM 2395 C CD2 . LEU B 2 58 ? 44.114 119.895 14.569 1.00 27.08 ? 58 LEU B CD2 1 ATOM 2396 N N . GLY B 2 59 ? 49.478 119.298 13.933 1.00 28.45 ? 59 GLY B N 1 ATOM 2397 C CA . GLY B 2 59 ? 50.881 119.620 13.688 1.00 28.18 ? 59 GLY B CA 1 ATOM 2398 C C . GLY B 2 59 ? 51.671 120.190 14.851 1.00 29.00 ? 59 GLY B C 1 ATOM 2399 O O . GLY B 2 59 ? 52.805 120.608 14.662 1.00 29.25 ? 59 GLY B O 1 ATOM 2400 N N . LYS B 2 60 ? 51.092 120.214 16.052 1.00 29.08 ? 60 LYS B N 1 ATOM 2401 C CA . LYS B 2 60 ? 51.764 120.741 17.239 1.00 28.23 ? 60 LYS B CA 1 ATOM 2402 C C . LYS B 2 60 ? 51.798 119.685 18.355 1.00 27.98 ? 60 LYS B C 1 ATOM 2403 O O . LYS B 2 60 ? 51.111 118.672 18.282 1.00 27.59 ? 60 LYS B O 1 ATOM 2404 C CB . LYS B 2 60 ? 51.075 122.047 17.683 1.00 31.06 ? 60 LYS B CB 1 ATOM 2405 C CG . LYS B 2 60 ? 51.498 123.230 16.802 1.00 31.39 ? 60 LYS B CG 1 ATOM 2406 C CD . LYS B 2 60 ? 50.948 124.565 17.260 1.00 33.54 ? 60 LYS B CD 1 ATOM 2407 C CE . LYS B 2 60 ? 51.198 125.635 16.191 1.00 33.79 ? 60 LYS B CE 1 ATOM 2408 N NZ . LYS B 2 60 ? 51.015 126.976 16.811 1.00 35.84 ? 60 LYS B NZ 1 ATOM 2409 N N . CYS B 2 61 ? 52.663 119.915 19.327 1.00 29.23 ? 61 CYS B N 1 ATOM 2410 C CA . CYS B 2 61 ? 52.922 118.995 20.408 1.00 30.20 ? 61 CYS B CA 1 ATOM 2411 C C . CYS B 2 61 ? 52.223 119.138 21.744 1.00 29.42 ? 61 CYS B C 1 ATOM 2412 O O . CYS B 2 61 ? 52.183 120.186 22.317 1.00 28.12 ? 61 CYS B O 1 ATOM 2413 C CB . CYS B 2 61 ? 54.416 118.959 20.709 1.00 32.79 ? 61 CYS B CB 1 ATOM 2414 S SG . CYS B 2 61 ? 55.505 118.403 19.410 1.00 35.81 ? 61 CYS B SG 1 ATOM 2415 N N . LEU B 2 62 ? 51.713 118.026 22.231 1.00 26.66 ? 62 LEU B N 1 ATOM 2416 C CA . LEU B 2 62 ? 51.103 117.942 23.530 1.00 26.31 ? 62 LEU B CA 1 ATOM 2417 C C . LEU B 2 62 ? 52.215 118.278 24.511 1.00 26.27 ? 62 LEU B C 1 ATOM 2418 O O . LEU B 2 62 ? 53.307 117.798 24.368 1.00 26.03 ? 62 LEU B O 1 ATOM 2419 C CB . LEU B 2 62 ? 50.602 116.526 23.787 1.00 25.96 ? 62 LEU B CB 1 ATOM 2420 C CG . LEU B 2 62 ? 49.778 116.318 25.039 1.00 25.18 ? 62 LEU B CG 1 ATOM 2421 C CD1 . LEU B 2 62 ? 48.399 116.875 24.814 1.00 25.11 ? 62 LEU B CD1 1 ATOM 2422 C CD2 . LEU B 2 62 ? 49.717 114.872 25.474 1.00 26.17 ? 62 LEU B CD2 1 ATOM 2423 N N . ALA B 2 63 ? 51.918 119.099 25.506 1.00 25.83 ? 63 ALA B N 1 ATOM 2424 C CA . ALA B 2 63 ? 52.909 119.540 26.482 1.00 25.86 ? 63 ALA B CA 1 ATOM 2425 C C . ALA B 2 63 ? 52.271 120.075 27.741 1.00 26.75 ? 63 ALA B C 1 ATOM 2426 O O . ALA B 2 63 ? 51.163 120.635 27.716 1.00 27.94 ? 63 ALA B O 1 ATOM 2427 C CB . ALA B 2 63 ? 53.805 120.618 25.876 1.00 27.63 ? 63 ALA B CB 1 ATOM 2428 N N . THR B 2 64 ? 52.967 119.896 28.854 1.00 26.21 ? 64 THR B N 1 ATOM 2429 C CA . THR B 2 64 ? 52.602 120.577 30.092 1.00 27.31 ? 64 THR B CA 1 ATOM 2430 C C . THR B 2 64 ? 52.883 122.089 29.907 1.00 28.07 ? 64 THR B C 1 ATOM 2431 O O . THR B 2 64 ? 53.635 122.490 28.999 1.00 28.76 ? 64 THR B O 1 ATOM 2432 C CB . THR B 2 64 ? 53.390 120.009 31.287 1.00 26.86 ? 64 THR B CB 1 ATOM 2433 O OG1 . THR B 2 64 ? 54.778 120.051 31.004 1.00 26.42 ? 64 THR B OG1 1 ATOM 2434 C CG2 . THR B 2 64 ? 53.017 118.566 31.530 1.00 27.60 ? 64 THR B CG2 1 ATOM 2435 N N . SER B 2 65 ? 52.264 122.921 30.742 1.00 30.22 ? 65 SER B N 1 ATOM 2436 C CA . SER B 2 65 ? 52.456 124.386 30.676 1.00 29.71 ? 65 SER B CA 1 ATOM 2437 C C . SER B 2 65 ? 53.149 124.973 31.904 1.00 32.16 ? 65 SER B C 1 ATOM 2438 O O . SER B 2 65 ? 53.331 126.185 31.968 1.00 33.84 ? 65 SER B O 1 ATOM 2439 C CB . SER B 2 65 ? 51.108 125.098 30.404 1.00 29.12 ? 65 SER B CB 1 ATOM 2440 O OG . SER B 2 65 ? 50.153 124.804 31.407 1.00 28.89 ? 65 SER B OG 1 ATOM 2441 N N . ALA B 2 66 ? 53.566 124.140 32.863 1.00 32.13 ? 66 ALA B N 1 ATOM 2442 C CA . ALA B 2 66 ? 54.299 124.604 34.042 1.00 30.85 ? 66 ALA B CA 1 ATOM 2443 C C . ALA B 2 66 ? 55.074 123.452 34.637 1.00 32.58 ? 66 ALA B C 1 ATOM 2444 O O . ALA B 2 66 ? 54.730 122.284 34.392 1.00 31.35 ? 66 ALA B O 1 ATOM 2445 C CB . ALA B 2 66 ? 53.331 125.137 35.078 1.00 31.19 ? 66 ALA B CB 1 ATOM 2446 N N . LEU B 2 67 ? 56.084 123.782 35.448 1.00 31.78 ? 67 LEU B N 1 ATOM 2447 C CA . LEU B 2 67 ? 56.808 122.807 36.253 1.00 31.71 ? 67 LEU B CA 1 ATOM 2448 C C . LEU B 2 67 ? 55.954 122.299 37.414 1.00 32.79 ? 67 LEU B C 1 ATOM 2449 O O . LEU B 2 67 ? 55.968 121.109 37.731 1.00 33.63 ? 67 LEU B O 1 ATOM 2450 C CB . LEU B 2 67 ? 58.107 123.422 36.786 1.00 33.73 ? 67 LEU B CB 1 ATOM 2451 C CG . LEU B 2 67 ? 59.050 122.511 37.597 1.00 34.32 ? 67 LEU B CG 1 ATOM 2452 C CD1 . LEU B 2 67 ? 59.512 121.289 36.805 1.00 35.43 ? 67 LEU B CD1 1 ATOM 2453 C CD2 . LEU B 2 67 ? 60.278 123.297 38.033 1.00 34.97 ? 67 LEU B CD2 1 ATOM 2454 N N . SER B 2 68 ? 55.184 123.188 38.032 1.00 31.93 ? 68 SER B N 1 ATOM 2455 C CA . SER B 2 68 ? 54.362 122.840 39.170 1.00 31.98 ? 68 SER B CA 1 ATOM 2456 C C . SER B 2 68 ? 53.076 122.156 38.721 1.00 29.63 ? 68 SER B C 1 ATOM 2457 O O . SER B 2 68 ? 52.605 122.388 37.629 1.00 29.92 ? 68 SER B O 1 ATOM 2458 C CB . SER B 2 68 ? 54.055 124.115 39.973 1.00 32.45 ? 68 SER B CB 1 ATOM 2459 O OG . SER B 2 68 ? 53.688 125.161 39.073 1.00 36.29 ? 68 SER B OG 1 ATOM 2460 N N . SER B 2 69 ? 52.501 121.336 39.589 1.00 29.00 ? 69 SER B N 1 ATOM 2461 C CA . SER B 2 69 ? 51.239 120.678 39.319 1.00 28.65 ? 69 SER B CA 1 ATOM 2462 C C . SER B 2 69 ? 50.111 121.691 39.177 1.00 29.88 ? 69 SER B C 1 ATOM 2463 O O . SER B 2 69 ? 50.209 122.810 39.680 1.00 29.72 ? 69 SER B O 1 ATOM 2464 C CB . SER B 2 69 ? 50.898 119.715 40.446 1.00 28.87 ? 69 SER B CB 1 ATOM 2465 O OG . SER B 2 69 ? 50.776 120.411 41.670 1.00 29.65 ? 69 SER B OG 1 ATOM 2466 N N . GLY B 2 70 ? 49.053 121.302 38.475 1.00 27.67 ? 70 GLY B N 1 ATOM 2467 C CA . GLY B 2 70 ? 47.830 122.081 38.453 1.00 28.04 ? 70 GLY B CA 1 ATOM 2468 C C . GLY B 2 70 ? 47.562 122.913 37.217 1.00 27.06 ? 70 GLY B C 1 ATOM 2469 O O . GLY B 2 70 ? 46.477 123.452 37.092 1.00 28.28 ? 70 GLY B O 1 ATOM 2470 N N . SER B 2 71 ? 48.523 123.041 36.317 1.00 26.84 ? 71 SER B N 1 ATOM 2471 C CA . SER B 2 71 ? 48.330 123.831 35.092 1.00 26.64 ? 71 SER B CA 1 ATOM 2472 C C . SER B 2 71 ? 47.933 122.981 33.898 1.00 26.93 ? 71 SER B C 1 ATOM 2473 O O . SER B 2 71 ? 48.146 121.752 33.877 1.00 26.67 ? 71 SER B O 1 ATOM 2474 C CB . SER B 2 71 ? 49.580 124.599 34.751 1.00 27.78 ? 71 SER B CB 1 ATOM 2475 O OG . SER B 2 71 ? 49.799 125.584 35.733 1.00 27.86 ? 71 SER B OG 1 ATOM 2476 N N . ASN B 2 72 ? 47.360 123.648 32.900 1.00 26.35 ? 72 ASN B N 1 ATOM 2477 C CA . ASN B 2 72 ? 46.779 122.980 31.742 1.00 25.54 ? 72 ASN B CA 1 ATOM 2478 C C . ASN B 2 72 ? 47.835 122.244 30.927 1.00 25.05 ? 72 ASN B C 1 ATOM 2479 O O . ASN B 2 72 ? 49.004 122.664 30.821 1.00 24.25 ? 72 ASN B O 1 ATOM 2480 C CB . ASN B 2 72 ? 46.069 123.993 30.824 1.00 25.92 ? 72 ASN B CB 1 ATOM 2481 C CG . ASN B 2 72 ? 44.715 124.439 31.353 1.00 27.13 ? 72 ASN B CG 1 ATOM 2482 O OD1 . ASN B 2 72 ? 44.198 123.884 32.302 1.00 27.83 ? 72 ASN B OD1 1 ATOM 2483 N ND2 . ASN B 2 72 ? 44.123 125.443 30.703 1.00 27.22 ? 72 ASN B ND2 1 ATOM 2484 N N . VAL B 2 73 ? 47.410 121.130 30.347 1.00 24.75 ? 73 VAL B N 1 ATOM 2485 C CA . VAL B 2 73 ? 48.144 120.536 29.252 1.00 24.46 ? 73 VAL B CA 1 ATOM 2486 C C . VAL B 2 73 ? 47.629 121.183 27.964 1.00 23.66 ? 73 VAL B C 1 ATOM 2487 O O . VAL B 2 73 ? 46.421 121.408 27.797 1.00 25.20 ? 73 VAL B O 1 ATOM 2488 C CB . VAL B 2 73 ? 48.011 119.000 29.269 1.00 23.96 ? 73 VAL B CB 1 ATOM 2489 C CG1 . VAL B 2 73 ? 48.607 118.381 28.015 1.00 24.91 ? 73 VAL B CG1 1 ATOM 2490 C CG2 . VAL B 2 73 ? 48.724 118.460 30.506 1.00 24.14 ? 73 VAL B CG2 1 ATOM 2491 N N . VAL B 2 74 ? 48.575 121.491 27.090 1.00 24.69 ? 74 VAL B N 1 ATOM 2492 C CA . VAL B 2 74 ? 48.358 122.304 25.889 1.00 25.07 ? 74 VAL B CA 1 ATOM 2493 C C . VAL B 2 74 ? 48.994 121.659 24.669 1.00 25.77 ? 74 VAL B C 1 ATOM 2494 O O . VAL B 2 74 ? 49.710 120.639 24.765 1.00 24.14 ? 74 VAL B O 1 ATOM 2495 C CB . VAL B 2 74 ? 48.986 123.723 26.039 1.00 26.42 ? 74 VAL B CB 1 ATOM 2496 C CG1 . VAL B 2 74 ? 48.409 124.438 27.260 1.00 27.64 ? 74 VAL B CG1 1 ATOM 2497 C CG2 . VAL B 2 74 ? 50.508 123.674 26.128 1.00 26.84 ? 74 VAL B CG2 1 ATOM 2498 N N . ILE B 2 75 ? 48.752 122.266 23.513 1.00 26.23 ? 75 ILE B N 1 ATOM 2499 C CA . ILE B 2 75 ? 49.576 121.988 22.347 1.00 27.18 ? 75 ILE B CA 1 ATOM 2500 C C . ILE B 2 75 ? 50.415 123.215 22.084 1.00 28.98 ? 75 ILE B C 1 ATOM 2501 O O . ILE B 2 75 ? 49.970 124.350 22.298 1.00 30.10 ? 75 ILE B O 1 ATOM 2502 C CB . ILE B 2 75 ? 48.789 121.571 21.091 1.00 27.59 ? 75 ILE B CB 1 ATOM 2503 C CG1 . ILE B 2 75 ? 47.720 122.585 20.719 1.00 27.17 ? 75 ILE B CG1 1 ATOM 2504 C CG2 . ILE B 2 75 ? 48.137 120.214 21.294 1.00 28.02 ? 75 ILE B CG2 1 ATOM 2505 C CD1 . ILE B 2 75 ? 47.307 122.460 19.275 1.00 28.10 ? 75 ILE B CD1 1 ATOM 2506 N N . THR B 2 76 ? 51.652 122.992 21.674 1.00 30.62 ? 76 THR B N 1 ATOM 2507 C CA . THR B 2 76 ? 52.530 124.092 21.333 1.00 31.96 ? 76 THR B CA 1 ATOM 2508 C C . THR B 2 76 ? 53.488 123.714 20.217 1.00 34.09 ? 76 THR B C 1 ATOM 2509 O O . THR B 2 76 ? 53.617 122.523 19.836 1.00 33.14 ? 76 THR B O 1 ATOM 2510 C CB . THR B 2 76 ? 53.283 124.614 22.577 1.00 34.08 ? 76 THR B CB 1 ATOM 2511 O OG1 . THR B 2 76 ? 53.884 125.880 22.262 1.00 36.10 ? 76 THR B OG1 1 ATOM 2512 C CG2 . THR B 2 76 ? 54.347 123.641 23.048 1.00 33.87 ? 76 THR B CG2 1 ATOM 2513 N N . ASN B 2 77 ? 54.154 124.725 19.689 1.00 34.05 ? 77 ASN B N 1 ATOM 2514 C CA . ASN B 2 77 ? 55.107 124.585 18.612 1.00 33.91 ? 77 ASN B CA 1 ATOM 2515 C C . ASN B 2 77 ? 56.177 123.599 18.993 1.00 34.96 ? 77 ASN B C 1 ATOM 2516 O O . ASN B 2 77 ? 56.813 123.746 19.990 1.00 33.56 ? 77 ASN B O 1 ATOM 2517 C CB . ASN B 2 77 ? 55.722 125.949 18.272 1.00 35.08 ? 77 ASN B CB 1 ATOM 2518 C CG . ASN B 2 77 ? 56.557 125.927 17.011 1.00 36.73 ? 77 ASN B CG 1 ATOM 2519 O OD1 . ASN B 2 77 ? 57.295 125.020 16.775 1.00 37.83 ? 77 ASN B OD1 1 ATOM 2520 N ND2 . ASN B 2 77 ? 56.442 126.958 16.217 1.00 39.17 ? 77 ASN B ND2 1 ATOM 2521 N N . CYS B 2 78 ? 56.359 122.591 18.168 1.00 36.73 ? 78 CYS B N 1 ATOM 2522 C CA . CYS B 2 78 ? 57.330 121.556 18.438 1.00 38.27 ? 78 CYS B CA 1 ATOM 2523 C C . CYS B 2 78 ? 58.769 121.996 18.568 1.00 39.31 ? 78 CYS B C 1 ATOM 2524 O O . CYS B 2 78 ? 59.516 121.356 19.242 1.00 37.21 ? 78 CYS B O 1 ATOM 2525 C CB . CYS B 2 78 ? 57.206 120.457 17.407 1.00 39.37 ? 78 CYS B CB 1 ATOM 2526 S SG . CYS B 2 78 ? 55.572 119.700 17.382 1.00 47.64 ? 78 CYS B SG 1 ATOM 2527 N N . ASP B 2 79 ? 59.156 123.085 17.924 1.00 42.10 ? 79 ASP B N 1 ATOM 2528 C CA . ASP B 2 79 ? 60.534 123.542 17.994 1.00 44.15 ? 79 ASP B CA 1 ATOM 2529 C C . ASP B 2 79 ? 60.891 123.980 19.374 1.00 44.87 ? 79 ASP B C 1 ATOM 2530 O O . ASP B 2 79 ? 62.005 123.870 19.769 1.00 46.10 ? 79 ASP B O 1 ATOM 2531 C CB . ASP B 2 79 ? 60.833 124.600 16.949 1.00 47.64 ? 79 ASP B CB 1 ATOM 2532 C CG . ASP B 2 79 ? 60.573 124.110 15.565 1.00 50.40 ? 79 ASP B CG 1 ATOM 2533 O OD1 . ASP B 2 79 ? 61.178 123.117 15.174 1.00 53.56 ? 79 ASP B OD1 1 ATOM 2534 O OD2 . ASP B 2 79 ? 59.745 124.685 14.867 1.00 54.91 ? 79 ASP B OD2 1 ATOM 2535 N N . TYR B 2 80 ? 59.916 124.468 20.110 1.00 46.86 ? 80 TYR B N 1 ATOM 2536 C CA . TYR B 2 80 ? 60.121 124.836 21.521 1.00 49.11 ? 80 TYR B CA 1 ATOM 2537 C C . TYR B 2 80 ? 60.607 123.701 22.406 1.00 47.96 ? 80 TYR B C 1 ATOM 2538 O O . TYR B 2 80 ? 61.225 123.961 23.435 1.00 46.64 ? 80 TYR B O 1 ATOM 2539 C CB . TYR B 2 80 ? 58.834 125.408 22.142 1.00 52.15 ? 80 TYR B CB 1 ATOM 2540 C CG . TYR B 2 80 ? 58.311 126.698 21.529 1.00 55.08 ? 80 TYR B CG 1 ATOM 2541 C CD1 . TYR B 2 80 ? 59.043 127.417 20.556 1.00 58.20 ? 80 TYR B CD1 1 ATOM 2542 C CD2 . TYR B 2 80 ? 57.090 127.225 21.953 1.00 56.77 ? 80 TYR B CD2 1 ATOM 2543 C CE1 . TYR B 2 80 ? 58.550 128.601 20.017 1.00 59.15 ? 80 TYR B CE1 1 ATOM 2544 C CE2 . TYR B 2 80 ? 56.594 128.410 21.422 1.00 59.14 ? 80 TYR B CE2 1 ATOM 2545 C CZ . TYR B 2 80 ? 57.324 129.093 20.458 1.00 60.33 ? 80 TYR B CZ 1 ATOM 2546 O OH . TYR B 2 80 ? 56.827 130.263 19.932 1.00 62.08 ? 80 TYR B OH 1 ATOM 2547 N N . LEU B 2 81 ? 60.309 122.458 22.017 1.00 46.14 ? 81 LEU B N 1 ATOM 2548 C CA . LEU B 2 81 ? 60.681 121.268 22.780 1.00 46.72 ? 81 LEU B CA 1 ATOM 2549 C C . LEU B 2 81 ? 61.913 120.557 22.207 1.00 50.39 ? 81 LEU B C 1 ATOM 2550 O O . LEU B 2 81 ? 62.224 119.441 22.637 1.00 50.52 ? 81 LEU B O 1 ATOM 2551 C CB . LEU B 2 81 ? 59.491 120.294 22.824 1.00 46.17 ? 81 LEU B CB 1 ATOM 2552 C CG . LEU B 2 81 ? 58.156 120.887 23.304 1.00 45.77 ? 81 LEU B CG 1 ATOM 2553 C CD1 . LEU B 2 81 ? 56.999 119.948 23.007 1.00 45.64 ? 81 LEU B CD1 1 ATOM 2554 C CD2 . LEU B 2 81 ? 58.217 121.210 24.787 1.00 46.84 ? 81 LEU B CD2 1 ATOM 2555 N N . ARG B 2 82 ? 62.630 121.194 21.273 1.00 53.58 ? 82 ARG B N 1 ATOM 2556 C CA . ARG B 2 82 ? 63.823 120.585 20.634 1.00 57.81 ? 82 ARG B CA 1 ATOM 2557 C C . ARG B 2 82 ? 64.816 119.946 21.624 1.00 57.67 ? 82 ARG B C 1 ATOM 2558 O O . ARG B 2 82 ? 65.400 118.903 21.318 1.00 59.58 ? 82 ARG B O 1 ATOM 2559 C CB . ARG B 2 82 ? 64.572 121.595 19.740 1.00 63.68 ? 82 ARG B CB 1 ATOM 2560 N N . TYR B 2 83 ? 64.973 120.546 22.793 1.00 56.65 ? 83 TYR B N 1 ATOM 2561 C CA . TYR B 2 83 ? 65.886 120.033 23.790 1.00 56.35 ? 83 TYR B CA 1 ATOM 2562 C C . TYR B 2 83 ? 65.162 119.326 24.912 1.00 53.78 ? 83 TYR B C 1 ATOM 2563 O O . TYR B 2 83 ? 65.719 119.127 25.970 1.00 54.92 ? 83 TYR B O 1 ATOM 2564 C CB . TYR B 2 83 ? 66.734 121.169 24.366 1.00 60.26 ? 83 TYR B CB 1 ATOM 2565 N N . ASP B 2 84 ? 63.920 118.943 24.679 1.00 50.41 ? 84 ASP B N 1 ATOM 2566 C CA . ASP B 2 84 ? 63.141 118.277 25.708 1.00 48.50 ? 84 ASP B CA 1 ATOM 2567 C C . ASP B 2 84 ? 63.044 116.795 25.448 1.00 46.59 ? 84 ASP B C 1 ATOM 2568 O O . ASP B 2 84 ? 62.999 116.363 24.314 1.00 45.43 ? 84 ASP B O 1 ATOM 2569 C CB . ASP B 2 84 ? 61.759 118.903 25.809 1.00 46.82 ? 84 ASP B CB 1 ATOM 2570 C CG . ASP B 2 84 ? 60.866 118.205 26.812 1.00 46.06 ? 84 ASP B CG 1 ATOM 2571 O OD1 . ASP B 2 84 ? 61.144 118.264 28.008 1.00 43.07 ? 84 ASP B OD1 1 ATOM 2572 O OD2 . ASP B 2 84 ? 59.888 117.606 26.383 1.00 44.74 ? 84 ASP B OD2 1 ATOM 2573 N N . ASP B 2 85 ? 63.005 116.021 26.515 1.00 45.40 ? 85 ASP B N 1 ATOM 2574 C CA . ASP B 2 85 ? 62.938 114.585 26.369 1.00 44.75 ? 85 ASP B CA 1 ATOM 2575 C C . ASP B 2 85 ? 61.560 114.007 26.095 1.00 40.61 ? 85 ASP B C 1 ATOM 2576 O O . ASP B 2 85 ? 61.449 112.866 25.747 1.00 41.24 ? 85 ASP B O 1 ATOM 2577 C CB . ASP B 2 85 ? 63.649 113.905 27.502 1.00 48.09 ? 85 ASP B CB 1 ATOM 2578 C CG . ASP B 2 85 ? 65.133 114.063 27.399 1.00 51.55 ? 85 ASP B CG 1 ATOM 2579 O OD1 . ASP B 2 85 ? 65.635 114.422 26.322 1.00 53.20 ? 85 ASP B OD1 1 ATOM 2580 O OD2 . ASP B 2 85 ? 65.804 113.832 28.404 1.00 58.18 ? 85 ASP B OD2 1 ATOM 2581 N N . GLY B 2 86 ? 60.525 114.812 26.229 1.00 34.80 ? 86 GLY B N 1 ATOM 2582 C CA . GLY B 2 86 ? 59.195 114.378 25.857 1.00 30.34 ? 86 GLY B CA 1 ATOM 2583 C C . GLY B 2 86 ? 58.371 113.588 26.845 1.00 27.56 ? 86 GLY B C 1 ATOM 2584 O O . GLY B 2 86 ? 58.550 113.697 28.043 1.00 25.71 ? 86 GLY B O 1 ATOM 2585 N N . TRP B 2 87 ? 57.433 112.817 26.308 1.00 26.82 ? 87 TRP B N 1 ATOM 2586 C CA . TRP B 2 87 ? 56.519 112.008 27.104 1.00 25.80 ? 87 TRP B CA 1 ATOM 2587 C C . TRP B 2 87 ? 57.001 110.567 27.183 1.00 26.10 ? 87 TRP B C 1 ATOM 2588 O O . TRP B 2 87 ? 57.589 110.057 26.238 1.00 26.78 ? 87 TRP B O 1 ATOM 2589 C CB . TRP B 2 87 ? 55.140 112.002 26.476 1.00 26.28 ? 87 TRP B CB 1 ATOM 2590 C CG . TRP B 2 87 ? 54.462 113.300 26.505 1.00 27.04 ? 87 TRP B CG 1 ATOM 2591 C CD1 . TRP B 2 87 ? 54.505 114.270 25.541 1.00 27.69 ? 87 TRP B CD1 1 ATOM 2592 C CD2 . TRP B 2 87 ? 53.630 113.804 27.550 1.00 26.53 ? 87 TRP B CD2 1 ATOM 2593 N NE1 . TRP B 2 87 ? 53.742 115.347 25.927 1.00 27.64 ? 87 TRP B NE1 1 ATOM 2594 C CE2 . TRP B 2 87 ? 53.197 115.088 27.155 1.00 26.96 ? 87 TRP B CE2 1 ATOM 2595 C CE3 . TRP B 2 87 ? 53.201 113.295 28.781 1.00 26.72 ? 87 TRP B CE3 1 ATOM 2596 C CZ2 . TRP B 2 87 ? 52.355 115.869 27.951 1.00 27.38 ? 87 TRP B CZ2 1 ATOM 2597 C CZ3 . TRP B 2 87 ? 52.365 114.067 29.566 1.00 27.55 ? 87 TRP B CZ3 1 ATOM 2598 C CH2 . TRP B 2 87 ? 51.963 115.350 29.155 1.00 27.74 ? 87 TRP B CH2 1 ATOM 2599 N N . MET B 2 88 ? 56.726 109.937 28.313 1.00 27.52 ? 88 MET B N 1 ATOM 2600 C CA . MET B 2 88 ? 56.886 108.507 28.502 1.00 30.26 ? 88 MET B CA 1 ATOM 2601 C C . MET B 2 88 ? 55.556 107.971 29.011 1.00 27.07 ? 88 MET B C 1 ATOM 2602 O O . MET B 2 88 ? 54.994 108.482 30.001 1.00 26.48 ? 88 MET B O 1 ATOM 2603 C CB . MET B 2 88 ? 57.972 108.264 29.531 1.00 35.10 ? 88 MET B CB 1 ATOM 2604 C CG . MET B 2 88 ? 58.046 106.847 30.074 1.00 43.12 ? 88 MET B CG 1 ATOM 2605 S SD . MET B 2 88 ? 59.529 106.677 31.092 1.00 58.17 ? 88 MET B SD 1 ATOM 2606 C CE . MET B 2 88 ? 59.368 108.040 32.271 1.00 52.96 ? 88 MET B CE 1 ATOM 2607 N N . VAL B 2 89 ? 55.074 106.924 28.351 1.00 25.04 ? 89 VAL B N 1 ATOM 2608 C CA . VAL B 2 89 ? 53.838 106.276 28.710 1.00 24.39 ? 89 VAL B CA 1 ATOM 2609 C C . VAL B 2 89 ? 54.196 104.947 29.376 1.00 25.15 ? 89 VAL B C 1 ATOM 2610 O O . VAL B 2 89 ? 54.903 104.142 28.798 1.00 26.04 ? 89 VAL B O 1 ATOM 2611 C CB . VAL B 2 89 ? 52.952 106.047 27.479 1.00 24.55 ? 89 VAL B CB 1 ATOM 2612 C CG1 . VAL B 2 89 ? 51.612 105.455 27.884 1.00 24.34 ? 89 VAL B CG1 1 ATOM 2613 C CG2 . VAL B 2 89 ? 52.757 107.358 26.720 1.00 24.70 ? 89 VAL B CG2 1 ATOM 2614 N N . SER B 2 90 ? 53.724 104.732 30.585 1.00 24.26 ? 90 SER B N 1 ATOM 2615 C CA . SER B 2 90 ? 53.987 103.496 31.310 1.00 25.43 ? 90 SER B CA 1 ATOM 2616 C C . SER B 2 90 ? 53.140 102.391 30.687 1.00 27.60 ? 90 SER B C 1 ATOM 2617 O O . SER B 2 90 ? 52.125 102.666 30.019 1.00 24.58 ? 90 SER B O 1 ATOM 2618 C CB . SER B 2 90 ? 53.604 103.658 32.777 1.00 25.36 ? 90 SER B CB 1 ATOM 2619 O OG . SER B 2 90 ? 52.190 103.572 32.951 1.00 25.47 ? 90 SER B OG 1 ATOM 2620 N N . SER B 2 91 ? 53.509 101.142 30.956 1.00 26.90 ? 91 SER B N 1 ATOM 2621 C CA . SER B 2 91 ? 52.741 100.022 30.445 1.00 29.72 ? 91 SER B CA 1 ATOM 2622 C C . SER B 2 91 ? 51.292 100.012 30.957 1.00 29.47 ? 91 SER B C 1 ATOM 2623 O O . SER B 2 91 ? 50.434 99.413 30.322 1.00 31.50 ? 91 SER B O 1 ATOM 2624 C CB . SER B 2 91 ? 53.442 98.700 30.769 1.00 30.42 ? 91 SER B CB 1 ATOM 2625 O OG . SER B 2 91 ? 53.553 98.546 32.147 1.00 31.46 ? 91 SER B OG 1 ATOM 2626 N N . SER B 2 92 ? 51.009 100.685 32.073 1.00 28.63 ? 92 SER B N 1 ATOM 2627 C CA . SER B 2 92 ? 49.634 100.794 32.562 1.00 30.27 ? 92 SER B CA 1 ATOM 2628 C C . SER B 2 92 ? 48.865 102.055 32.095 1.00 27.00 ? 92 SER B C 1 ATOM 2629 O O . SER B 2 92 ? 47.755 102.293 32.552 1.00 27.52 ? 92 SER B O 1 ATOM 2630 C CB . SER B 2 92 ? 49.631 100.698 34.091 1.00 33.29 ? 92 SER B CB 1 ATOM 2631 O OG . SER B 2 92 ? 50.259 101.817 34.643 1.00 37.38 ? 92 SER B OG 1 ATOM 2632 N N . GLY B 2 93 ? 49.434 102.836 31.183 1.00 26.02 ? 93 GLY B N 1 ATOM 2633 C CA . GLY B 2 93 ? 48.725 103.996 30.568 1.00 25.87 ? 93 GLY B CA 1 ATOM 2634 C C . GLY B 2 93 ? 48.799 105.327 31.323 1.00 24.70 ? 93 GLY B C 1 ATOM 2635 O O . GLY B 2 93 ? 47.959 106.221 31.128 1.00 25.63 ? 93 GLY B O 1 ATOM 2636 N N . THR B 2 94 ? 49.812 105.465 32.167 1.00 23.79 ? 94 THR B N 1 ATOM 2637 C CA . THR B 2 94 ? 50.148 106.742 32.791 1.00 24.17 ? 94 THR B CA 1 ATOM 2638 C C . THR B 2 94 ? 50.997 107.508 31.797 1.00 24.30 ? 94 THR B C 1 ATOM 2639 O O . THR B 2 94 ? 52.044 107.013 31.371 1.00 24.10 ? 94 THR B O 1 ATOM 2640 C CB . THR B 2 94 ? 50.938 106.531 34.092 1.00 23.53 ? 94 THR B CB 1 ATOM 2641 O OG1 . THR B 2 94 ? 50.175 105.710 34.979 1.00 25.25 ? 94 THR B OG1 1 ATOM 2642 C CG2 . THR B 2 94 ? 51.266 107.873 34.791 1.00 24.76 ? 94 THR B CG2 1 ATOM 2643 N N . MET B 2 95 ? 50.560 108.711 31.436 1.00 23.46 ? 95 MET B N 1 ATOM 2644 C CA . MET B 2 95 ? 51.291 109.545 30.492 1.00 24.41 ? 95 MET B CA 1 ATOM 2645 C C . MET B 2 95 ? 52.052 110.627 31.252 1.00 24.84 ? 95 MET B C 1 ATOM 2646 O O . MET B 2 95 ? 51.432 111.559 31.803 1.00 23.97 ? 95 MET B O 1 ATOM 2647 C CB . MET B 2 95 ? 50.323 110.179 29.512 1.00 25.01 ? 95 MET B CB 1 ATOM 2648 C CG . MET B 2 95 ? 49.605 109.138 28.682 1.00 25.92 ? 95 MET B CG 1 ATOM 2649 S SD . MET B 2 95 ? 48.470 109.833 27.483 1.00 26.33 ? 95 MET B SD 1 ATOM 2650 C CE . MET B 2 95 ? 49.629 110.623 26.366 1.00 27.05 ? 95 MET B CE 1 ATOM 2651 N N . MET B 2 96 ? 53.380 110.509 31.244 1.00 24.66 ? 96 MET B N 1 ATOM 2652 C CA . MET B 2 96 ? 54.240 111.304 32.109 1.00 26.05 ? 96 MET B CA 1 ATOM 2653 C C . MET B 2 96 ? 55.208 112.173 31.321 1.00 26.04 ? 96 MET B C 1 ATOM 2654 O O . MET B 2 96 ? 55.865 111.709 30.386 1.00 25.71 ? 96 MET B O 1 ATOM 2655 C CB . MET B 2 96 ? 55.031 110.384 33.040 1.00 27.38 ? 96 MET B CB 1 ATOM 2656 C CG . MET B 2 96 ? 55.806 111.138 34.106 1.00 28.57 ? 96 MET B CG 1 ATOM 2657 S SD . MET B 2 96 ? 56.684 110.058 35.245 1.00 29.80 ? 96 MET B SD 1 ATOM 2658 C CE . MET B 2 96 ? 55.407 109.620 36.391 1.00 28.41 ? 96 MET B CE 1 ATOM 2659 N N . ASN B 2 97 ? 55.310 113.436 31.728 1.00 26.50 ? 97 ASN B N 1 ATOM 2660 C CA . ASN B 2 97 ? 56.389 114.297 31.254 1.00 27.35 ? 97 ASN B CA 1 ATOM 2661 C C . ASN B 2 97 ? 57.694 113.805 31.892 1.00 27.42 ? 97 ASN B C 1 ATOM 2662 O O . ASN B 2 97 ? 57.805 113.766 33.112 1.00 28.39 ? 97 ASN B O 1 ATOM 2663 C CB . ASN B 2 97 ? 56.070 115.731 31.649 1.00 29.23 ? 97 ASN B CB 1 ATOM 2664 C CG . ASN B 2 97 ? 57.192 116.684 31.347 1.00 30.15 ? 97 ASN B CG 1 ATOM 2665 O OD1 . ASN B 2 97 ? 58.350 116.457 31.750 1.00 29.90 ? 97 ASN B OD1 1 ATOM 2666 N ND2 . ASN B 2 97 ? 56.872 117.760 30.647 1.00 31.81 ? 97 ASN B ND2 1 ATOM 2667 N N . LYS B 2 98 ? 58.674 113.423 31.084 1.00 28.79 ? 98 LYS B N 1 ATOM 2668 C CA . LYS B 2 98 ? 59.874 112.741 31.628 1.00 32.07 ? 98 LYS B CA 1 ATOM 2669 C C . LYS B 2 98 ? 60.723 113.617 32.556 1.00 33.15 ? 98 LYS B C 1 ATOM 2670 O O . LYS B 2 98 ? 61.299 113.138 33.534 1.00 33.74 ? 98 LYS B O 1 ATOM 2671 C CB . LYS B 2 98 ? 60.754 112.203 30.503 1.00 34.14 ? 98 LYS B CB 1 ATOM 2672 C CG . LYS B 2 98 ? 60.069 111.160 29.649 1.00 34.83 ? 98 LYS B CG 1 ATOM 2673 C CD . LYS B 2 98 ? 60.909 110.768 28.448 1.00 37.67 ? 98 LYS B CD 1 ATOM 2674 C CE . LYS B 2 98 ? 62.208 110.096 28.873 1.00 39.45 ? 98 LYS B CE 1 ATOM 2675 N NZ . LYS B 2 98 ? 62.632 109.163 27.806 1.00 42.27 ? 98 LYS B NZ 1 ATOM 2676 N N . SER B 2 99 ? 60.754 114.906 32.263 1.00 33.64 ? 99 SER B N 1 ATOM 2677 C CA . SER B 2 99 ? 61.526 115.867 33.045 1.00 33.60 ? 99 SER B CA 1 ATOM 2678 C C . SER B 2 99 ? 60.868 116.258 34.365 1.00 31.55 ? 99 SER B C 1 ATOM 2679 O O . SER B 2 99 ? 61.481 116.190 35.421 1.00 31.30 ? 99 SER B O 1 ATOM 2680 C CB . SER B 2 99 ? 61.745 117.107 32.181 1.00 34.52 ? 99 SER B CB 1 ATOM 2681 O OG . SER B 2 99 ? 62.194 118.165 32.990 1.00 39.56 ? 99 SER B OG 1 ATOM 2682 N N . SER B 2 100 ? 59.607 116.668 34.319 1.00 29.86 ? 100 SER B N 1 ATOM 2683 C CA . SER B 2 100 ? 58.900 117.122 35.522 1.00 28.12 ? 100 SER B CA 1 ATOM 2684 C C . SER B 2 100 ? 58.186 116.030 36.328 1.00 29.17 ? 100 SER B C 1 ATOM 2685 O O . SER B 2 100 ? 57.816 116.247 37.487 1.00 28.36 ? 100 SER B O 1 ATOM 2686 C CB . SER B 2 100 ? 57.878 118.189 35.118 1.00 28.69 ? 100 SER B CB 1 ATOM 2687 O OG . SER B 2 100 ? 56.783 117.602 34.414 1.00 29.04 ? 100 SER B OG 1 ATOM 2688 N N . HIS B 2 101 ? 57.957 114.881 35.691 1.00 29.31 ? 101 HIS B N 1 ATOM 2689 C CA . HIS B 2 101 ? 57.182 113.757 36.241 1.00 30.05 ? 101 HIS B CA 1 ATOM 2690 C C . HIS B 2 101 ? 55.688 114.006 36.390 1.00 27.14 ? 101 HIS B C 1 ATOM 2691 O O . HIS B 2 101 ? 54.993 113.158 36.927 1.00 27.19 ? 101 HIS B O 1 ATOM 2692 C CB . HIS B 2 101 ? 57.732 113.204 37.571 1.00 33.21 ? 101 HIS B CB 1 ATOM 2693 C CG . HIS B 2 101 ? 59.199 112.932 37.567 1.00 37.29 ? 101 HIS B CG 1 ATOM 2694 N ND1 . HIS B 2 101 ? 59.930 112.739 36.413 1.00 41.93 ? 101 HIS B ND1 1 ATOM 2695 C CD2 . HIS B 2 101 ? 60.074 112.800 38.593 1.00 40.78 ? 101 HIS B CD2 1 ATOM 2696 C CE1 . HIS B 2 101 ? 61.193 112.513 36.726 1.00 41.42 ? 101 HIS B CE1 1 ATOM 2697 N NE2 . HIS B 2 101 ? 61.307 112.551 38.041 1.00 43.56 ? 101 HIS B NE2 1 ATOM 2698 N N . LEU B 2 102 ? 55.179 115.133 35.903 1.00 26.45 ? 102 LEU B N 1 ATOM 2699 C CA . LEU B 2 102 ? 53.744 115.398 35.956 1.00 24.39 ? 102 LEU B CA 1 ATOM 2700 C C . LEU B 2 102 ? 53.069 114.477 34.974 1.00 23.66 ? 102 LEU B C 1 ATOM 2701 O O . LEU B 2 102 ? 53.628 114.165 33.912 1.00 23.24 ? 102 LEU B O 1 ATOM 2702 C CB . LEU B 2 102 ? 53.442 116.849 35.577 1.00 25.78 ? 102 LEU B CB 1 ATOM 2703 C CG . LEU B 2 102 ? 53.996 117.942 36.500 1.00 25.65 ? 102 LEU B CG 1 ATOM 2704 C CD1 . LEU B 2 102 ? 53.527 119.299 35.990 1.00 26.06 ? 102 LEU B CD1 1 ATOM 2705 C CD2 . LEU B 2 102 ? 53.602 117.740 37.954 1.00 25.57 ? 102 LEU B CD2 1 ATOM 2706 N N . VAL B 2 103 ? 51.871 114.028 35.325 1.00 23.39 ? 103 VAL B N 1 ATOM 2707 C CA . VAL B 2 103 ? 51.131 113.129 34.472 1.00 23.25 ? 103 VAL B CA 1 ATOM 2708 C C . VAL B 2 103 ? 49.817 113.772 34.034 1.00 24.30 ? 103 VAL B C 1 ATOM 2709 O O . VAL B 2 103 ? 49.244 114.595 34.756 1.00 24.26 ? 103 VAL B O 1 ATOM 2710 C CB . VAL B 2 103 ? 50.888 111.759 35.150 1.00 22.69 ? 103 VAL B CB 1 ATOM 2711 C CG1 . VAL B 2 103 ? 52.220 111.156 35.590 1.00 22.79 ? 103 VAL B CG1 1 ATOM 2712 C CG2 . VAL B 2 103 ? 49.915 111.844 36.311 1.00 22.14 ? 103 VAL B CG2 1 ATOM 2713 N N . LEU B 2 104 ? 49.370 113.363 32.850 1.00 23.24 ? 104 LEU B N 1 ATOM 2714 C CA . LEU B 2 104 ? 48.111 113.787 32.274 1.00 23.21 ? 104 LEU B CA 1 ATOM 2715 C C . LEU B 2 104 ? 46.955 113.359 33.168 1.00 23.43 ? 104 LEU B C 1 ATOM 2716 O O . LEU B 2 104 ? 46.834 112.172 33.531 1.00 23.39 ? 104 LEU B O 1 ATOM 2717 C CB . LEU B 2 104 ? 47.968 113.200 30.860 1.00 22.97 ? 104 LEU B CB 1 ATOM 2718 C CG . LEU B 2 104 ? 46.818 113.739 30.017 1.00 23.80 ? 104 LEU B CG 1 ATOM 2719 C CD1 . LEU B 2 104 ? 47.022 115.220 29.721 1.00 23.77 ? 104 LEU B CD1 1 ATOM 2720 C CD2 . LEU B 2 104 ? 46.659 112.941 28.731 1.00 23.78 ? 104 LEU B CD2 1 ATOM 2721 N N . THR B 2 105 ? 46.115 114.328 33.548 1.00 22.39 ? 105 THR B N 1 ATOM 2722 C CA . THR B 2 105 ? 45.076 114.134 34.546 1.00 22.67 ? 105 THR B CA 1 ATOM 2723 C C . THR B 2 105 ? 43.777 114.838 34.131 1.00 23.20 ? 105 THR B C 1 ATOM 2724 O O . THR B 2 105 ? 43.811 115.938 33.560 1.00 24.33 ? 105 THR B O 1 ATOM 2725 C CB . THR B 2 105 ? 45.532 114.684 35.916 1.00 24.07 ? 105 THR B CB 1 ATOM 2726 O OG1 . THR B 2 105 ? 46.794 114.103 36.284 1.00 24.65 ? 105 THR B OG1 1 ATOM 2727 C CG2 . THR B 2 105 ? 44.505 114.397 36.998 1.00 24.37 ? 105 THR B CG2 1 ATOM 2728 N N . ALA B 2 106 ? 42.652 114.169 34.359 1.00 22.81 ? 106 ALA B N 1 ATOM 2729 C CA . ALA B 2 106 ? 41.334 114.767 34.232 1.00 22.84 ? 106 ALA B CA 1 ATOM 2730 C C . ALA B 2 106 ? 40.719 114.946 35.615 1.00 23.79 ? 106 ALA B C 1 ATOM 2731 O O . ALA B 2 106 ? 40.143 114.000 36.157 1.00 23.04 ? 106 ALA B O 1 ATOM 2732 C CB . ALA B 2 106 ? 40.443 113.886 33.379 1.00 23.44 ? 106 ALA B CB 1 ATOM 2733 N N . ASN B 2 107 ? 40.788 116.164 36.165 1.00 24.69 ? 107 ASN B N 1 ATOM 2734 C CA . ASN B 2 107 ? 40.243 116.416 37.522 1.00 25.52 ? 107 ASN B CA 1 ATOM 2735 C C . ASN B 2 107 ? 38.736 116.366 37.671 1.00 26.53 ? 107 ASN B C 1 ATOM 2736 O O . ASN B 2 107 ? 38.233 116.227 38.784 1.00 27.55 ? 107 ASN B O 1 ATOM 2737 C CB . ASN B 2 107 ? 40.809 117.697 38.109 1.00 26.19 ? 107 ASN B CB 1 ATOM 2738 C CG . ASN B 2 107 ? 42.267 117.543 38.481 1.00 27.95 ? 107 ASN B CG 1 ATOM 2739 O OD1 . ASN B 2 107 ? 42.684 116.463 38.918 1.00 30.23 ? 107 ASN B OD1 1 ATOM 2740 N ND2 . ASN B 2 107 ? 43.043 118.596 38.330 1.00 28.05 ? 107 ASN B ND2 1 ATOM 2741 N N . ALA B 2 108 ? 38.016 116.436 36.566 1.00 25.37 ? 108 ALA B N 1 ATOM 2742 C CA . ALA B 2 108 ? 36.590 116.113 36.554 1.00 25.15 ? 108 ALA B CA 1 ATOM 2743 C C . ALA B 2 108 ? 36.296 115.185 35.382 1.00 24.97 ? 108 ALA B C 1 ATOM 2744 O O . ALA B 2 108 ? 37.135 115.000 34.510 1.00 24.81 ? 108 ALA B O 1 ATOM 2745 C CB . ALA B 2 108 ? 35.746 117.394 36.486 1.00 25.44 ? 108 ALA B CB 1 ATOM 2746 N N . ALA B 2 109 ? 35.101 114.608 35.385 1.00 25.40 ? 109 ALA B N 1 ATOM 2747 C CA . ALA B 2 109 ? 34.666 113.621 34.397 1.00 27.46 ? 109 ALA B CA 1 ATOM 2748 C C . ALA B 2 109 ? 33.897 114.223 33.203 1.00 28.62 ? 109 ALA B C 1 ATOM 2749 O O . ALA B 2 109 ? 33.687 113.543 32.206 1.00 30.11 ? 109 ALA B O 1 ATOM 2750 C CB . ALA B 2 109 ? 33.798 112.575 35.077 1.00 27.94 ? 109 ALA B CB 1 ATOM 2751 N N . THR B 2 110 ? 33.488 115.480 33.317 1.00 27.92 ? 110 THR B N 1 ATOM 2752 C CA . THR B 2 110 ? 32.538 116.076 32.387 1.00 28.79 ? 110 THR B CA 1 ATOM 2753 C C . THR B 2 110 ? 33.222 116.517 31.096 1.00 26.43 ? 110 THR B C 1 ATOM 2754 O O . THR B 2 110 ? 34.372 116.954 31.087 1.00 27.07 ? 110 THR B O 1 ATOM 2755 C CB . THR B 2 110 ? 31.813 117.292 33.034 1.00 29.65 ? 110 THR B CB 1 ATOM 2756 O OG1 . THR B 2 110 ? 32.775 118.229 33.519 1.00 32.03 ? 110 THR B OG1 1 ATOM 2757 C CG2 . THR B 2 110 ? 30.998 116.847 34.201 1.00 32.07 ? 110 THR B CG2 1 ATOM 2758 N N . SER B 2 111 ? 32.495 116.402 29.999 1.00 26.95 ? 111 SER B N 1 ATOM 2759 C CA . SER B 2 111 ? 32.938 116.967 28.737 1.00 25.84 ? 111 SER B CA 1 ATOM 2760 C C . SER B 2 111 ? 33.384 118.408 28.909 1.00 24.80 ? 111 SER B C 1 ATOM 2761 O O . SER B 2 111 ? 32.775 119.167 29.671 1.00 23.85 ? 111 SER B O 1 ATOM 2762 C CB . SER B 2 111 ? 31.833 116.876 27.691 1.00 27.71 ? 111 SER B CB 1 ATOM 2763 O OG . SER B 2 111 ? 32.279 117.535 26.509 1.00 27.14 ? 111 SER B OG 1 ATOM 2764 N N . ARG B 2 112 ? 34.482 118.747 28.236 1.00 23.73 ? 112 ARG B N 1 ATOM 2765 C CA . ARG B 2 112 ? 35.136 120.059 28.264 1.00 24.14 ? 112 ARG B CA 1 ATOM 2766 C C . ARG B 2 112 ? 36.004 120.343 29.491 1.00 24.64 ? 112 ARG B C 1 ATOM 2767 O O . ARG B 2 112 ? 36.574 121.427 29.628 1.00 23.33 ? 112 ARG B O 1 ATOM 2768 C CB . ARG B 2 112 ? 34.121 121.195 27.978 1.00 26.13 ? 112 ARG B CB 1 ATOM 2769 C CG . ARG B 2 112 ? 33.415 120.983 26.632 1.00 26.90 ? 112 ARG B CG 1 ATOM 2770 C CD . ARG B 2 112 ? 32.211 121.897 26.389 1.00 27.19 ? 112 ARG B CD 1 ATOM 2771 N NE . ARG B 2 112 ? 32.669 123.267 26.324 1.00 26.51 ? 112 ARG B NE 1 ATOM 2772 C CZ . ARG B 2 112 ? 32.422 124.144 25.346 1.00 26.63 ? 112 ARG B CZ 1 ATOM 2773 N NH1 . ARG B 2 112 ? 31.647 123.864 24.290 1.00 26.86 ? 112 ARG B NH1 1 ATOM 2774 N NH2 . ARG B 2 112 ? 32.960 125.341 25.465 1.00 26.37 ? 112 ARG B NH2 1 ATOM 2775 N N . THR B 2 113 ? 36.175 119.346 30.357 1.00 24.61 ? 113 THR B N 1 ATOM 2776 C CA . THR B 2 113 ? 37.085 119.477 31.483 1.00 24.11 ? 113 THR B CA 1 ATOM 2777 C C . THR B 2 113 ? 38.479 119.737 30.945 1.00 23.07 ? 113 THR B C 1 ATOM 2778 O O . THR B 2 113 ? 38.925 119.054 30.023 1.00 24.12 ? 113 THR B O 1 ATOM 2779 C CB . THR B 2 113 ? 37.089 118.178 32.323 1.00 24.23 ? 113 THR B CB 1 ATOM 2780 O OG1 . THR B 2 113 ? 35.857 118.042 33.033 1.00 23.89 ? 113 THR B OG1 1 ATOM 2781 C CG2 . THR B 2 113 ? 38.204 118.161 33.303 1.00 24.93 ? 113 THR B CG2 1 ATOM 2782 N N . ASN B 2 114 ? 39.159 120.717 31.515 1.00 22.67 ? 114 ASN B N 1 ATOM 2783 C CA . ASN B 2 114 ? 40.539 120.992 31.183 1.00 23.93 ? 114 ASN B CA 1 ATOM 2784 C C . ASN B 2 114 ? 41.470 119.893 31.720 1.00 25.45 ? 114 ASN B C 1 ATOM 2785 O O . ASN B 2 114 ? 41.453 119.628 32.935 1.00 24.38 ? 114 ASN B O 1 ATOM 2786 C CB . ASN B 2 114 ? 40.987 122.268 31.877 1.00 25.76 ? 114 ASN B CB 1 ATOM 2787 C CG . ASN B 2 114 ? 40.450 123.539 31.235 1.00 27.39 ? 114 ASN B CG 1 ATOM 2788 O OD1 . ASN B 2 114 ? 39.916 123.540 30.122 1.00 24.97 ? 114 ASN B OD1 1 ATOM 2789 N ND2 . ASN B 2 114 ? 40.624 124.654 31.961 1.00 30.49 ? 114 ASN B ND2 1 ATOM 2790 N N . LEU B 2 115 ? 42.315 119.320 30.858 1.00 23.43 ? 115 LEU B N 1 ATOM 2791 C CA . LEU B 2 115 ? 43.303 118.358 31.314 1.00 24.26 ? 115 LEU B CA 1 ATOM 2792 C C . LEU B 2 115 ? 44.483 119.113 31.864 1.00 24.13 ? 115 LEU B C 1 ATOM 2793 O O . LEU B 2 115 ? 44.874 120.152 31.318 1.00 22.88 ? 115 LEU B O 1 ATOM 2794 C CB . LEU B 2 115 ? 43.735 117.436 30.188 1.00 23.67 ? 115 LEU B CB 1 ATOM 2795 C CG . LEU B 2 115 ? 42.570 116.694 29.548 1.00 25.04 ? 115 LEU B CG 1 ATOM 2796 C CD1 . LEU B 2 115 ? 43.098 115.704 28.519 1.00 27.65 ? 115 LEU B CD1 1 ATOM 2797 C CD2 . LEU B 2 115 ? 41.698 115.960 30.557 1.00 24.84 ? 115 LEU B CD2 1 ATOM 2798 N N . THR B 2 116 ? 45.042 118.587 32.945 1.00 23.25 ? 116 THR B N 1 ATOM 2799 C CA . THR B 2 116 ? 46.144 119.221 33.659 1.00 24.12 ? 116 THR B CA 1 ATOM 2800 C C . THR B 2 116 ? 47.308 118.245 33.901 1.00 24.70 ? 116 THR B C 1 ATOM 2801 O O . THR B 2 116 ? 47.133 117.039 33.805 1.00 26.38 ? 116 THR B O 1 ATOM 2802 C CB . THR B 2 116 ? 45.689 119.757 35.016 1.00 24.53 ? 116 THR B CB 1 ATOM 2803 O OG1 . THR B 2 116 ? 44.962 118.746 35.722 1.00 24.30 ? 116 THR B OG1 1 ATOM 2804 C CG2 . THR B 2 116 ? 44.780 121.021 34.837 1.00 24.79 ? 116 THR B CG2 1 ATOM 2805 N N . GLY B 2 117 ? 48.483 118.807 34.155 1.00 23.98 ? 117 GLY B N 1 ATOM 2806 C CA . GLY B 2 117 ? 49.669 118.068 34.610 1.00 25.79 ? 117 GLY B CA 1 ATOM 2807 C C . GLY B 2 117 ? 49.678 118.038 36.128 1.00 24.99 ? 117 GLY B C 1 ATOM 2808 O O . GLY B 2 117 ? 49.743 119.085 36.764 1.00 25.58 ? 117 GLY B O 1 ATOM 2809 N N . GLU B 2 118 ? 49.583 116.846 36.707 1.00 24.75 ? 118 GLU B N 1 ATOM 2810 C CA . GLU B 2 118 ? 49.471 116.672 38.166 1.00 24.91 ? 118 GLU B CA 1 ATOM 2811 C C . GLU B 2 118 ? 50.465 115.618 38.656 1.00 25.57 ? 118 GLU B C 1 ATOM 2812 O O . GLU B 2 118 ? 50.986 114.806 37.867 1.00 23.88 ? 118 GLU B O 1 ATOM 2813 C CB . GLU B 2 118 ? 48.064 116.238 38.571 1.00 25.19 ? 118 GLU B CB 1 ATOM 2814 C CG . GLU B 2 118 ? 46.900 117.096 38.062 1.00 26.12 ? 118 GLU B CG 1 ATOM 2815 C CD . GLU B 2 118 ? 46.707 118.417 38.812 1.00 27.60 ? 118 GLU B CD 1 ATOM 2816 O OE1 . GLU B 2 118 ? 47.463 118.681 39.770 1.00 29.42 ? 118 GLU B OE1 1 ATOM 2817 O OE2 . GLU B 2 118 ? 45.814 119.199 38.408 1.00 28.07 ? 118 GLU B OE2 1 ATOM 2818 N N . ASN B 2 119 ? 50.696 115.619 39.962 1.00 24.90 ? 119 ASN B N 1 ATOM 2819 C CA . ASN B 2 119 ? 51.535 114.617 40.592 1.00 26.59 ? 119 ASN B CA 1 ATOM 2820 C C . ASN B 2 119 ? 50.864 113.265 40.482 1.00 26.45 ? 119 ASN B C 1 ATOM 2821 O O . ASN B 2 119 ? 49.650 113.147 40.684 1.00 26.94 ? 119 ASN B O 1 ATOM 2822 C CB . ASN B 2 119 ? 51.782 114.962 42.057 1.00 28.21 ? 119 ASN B CB 1 ATOM 2823 C CG . ASN B 2 119 ? 52.525 116.278 42.223 1.00 30.37 ? 119 ASN B CG 1 ATOM 2824 O OD1 . ASN B 2 119 ? 53.488 116.562 41.509 1.00 31.77 ? 119 ASN B OD1 1 ATOM 2825 N ND2 . ASN B 2 119 ? 52.078 117.086 43.160 1.00 33.03 ? 119 ASN B ND2 1 ATOM 2826 N N . ASN B 2 120 ? 51.635 112.245 40.123 1.00 26.97 ? 120 ASN B N 1 ATOM 2827 C CA . ASN B 2 120 ? 51.053 110.913 39.933 1.00 27.52 ? 120 ASN B CA 1 ATOM 2828 C C . ASN B 2 120 ? 50.687 110.261 41.249 1.00 28.08 ? 120 ASN B C 1 ATOM 2829 O O . ASN B 2 120 ? 51.548 110.077 42.104 1.00 29.96 ? 120 ASN B O 1 ATOM 2830 C CB . ASN B 2 120 ? 52.028 110.005 39.204 1.00 27.25 ? 120 ASN B CB 1 ATOM 2831 C CG . ASN B 2 120 ? 51.389 108.702 38.768 1.00 28.18 ? 120 ASN B CG 1 ATOM 2832 O OD1 . ASN B 2 120 ? 50.199 108.639 38.435 1.00 27.65 ? 120 ASN B OD1 1 ATOM 2833 N ND2 . ASN B 2 120 ? 52.178 107.652 38.760 1.00 30.05 ? 120 ASN B ND2 1 ATOM 2834 N N . VAL B 2 121 ? 49.419 109.930 41.415 1.00 27.05 ? 121 VAL B N 1 ATOM 2835 C CA . VAL B 2 121 ? 48.971 109.084 42.522 1.00 28.01 ? 121 VAL B CA 1 ATOM 2836 C C . VAL B 2 121 ? 48.338 107.788 42.007 1.00 27.49 ? 121 VAL B C 1 ATOM 2837 O O . VAL B 2 121 ? 47.771 107.030 42.787 1.00 27.68 ? 121 VAL B O 1 ATOM 2838 C CB . VAL B 2 121 ? 48.025 109.839 43.484 1.00 28.71 ? 121 VAL B CB 1 ATOM 2839 C CG1 . VAL B 2 121 ? 48.745 111.035 44.104 1.00 30.86 ? 121 VAL B CG1 1 ATOM 2840 C CG2 . VAL B 2 121 ? 46.770 110.322 42.785 1.00 28.60 ? 121 VAL B CG2 1 ATOM 2841 N N . PHE B 2 122 ? 48.451 107.533 40.700 1.00 24.85 ? 122 PHE B N 1 ATOM 2842 C CA . PHE B 2 122 ? 47.879 106.344 40.058 1.00 25.40 ? 122 PHE B CA 1 ATOM 2843 C C . PHE B 2 122 ? 46.357 106.287 40.136 1.00 24.13 ? 122 PHE B C 1 ATOM 2844 O O . PHE B 2 122 ? 45.774 105.203 40.143 1.00 22.86 ? 122 PHE B O 1 ATOM 2845 C CB . PHE B 2 122 ? 48.481 105.020 40.603 1.00 27.08 ? 122 PHE B CB 1 ATOM 2846 C CG . PHE B 2 122 ? 49.986 104.924 40.499 1.00 26.55 ? 122 PHE B CG 1 ATOM 2847 C CD1 . PHE B 2 122 ? 50.797 105.357 41.548 1.00 29.09 ? 122 PHE B CD1 1 ATOM 2848 C CD2 . PHE B 2 122 ? 50.587 104.379 39.371 1.00 28.92 ? 122 PHE B CD2 1 ATOM 2849 C CE1 . PHE B 2 122 ? 52.184 105.255 41.466 1.00 29.16 ? 122 PHE B CE1 1 ATOM 2850 C CE2 . PHE B 2 122 ? 51.981 104.272 39.268 1.00 29.12 ? 122 PHE B CE2 1 ATOM 2851 C CZ . PHE B 2 122 ? 52.775 104.707 40.318 1.00 29.10 ? 122 PHE B CZ 1 ATOM 2852 N N . ALA B 2 123 ? 45.693 107.446 40.179 1.00 23.19 ? 123 ALA B N 1 ATOM 2853 C CA . ALA B 2 123 ? 44.243 107.453 40.137 1.00 21.65 ? 123 ALA B CA 1 ATOM 2854 C C . ALA B 2 123 ? 43.717 107.048 38.745 1.00 21.11 ? 123 ALA B C 1 ATOM 2855 O O . ALA B 2 123 ? 44.391 107.227 37.735 1.00 22.12 ? 123 ALA B O 1 ATOM 2856 C CB . ALA B 2 123 ? 43.719 108.815 40.542 1.00 23.27 ? 123 ALA B CB 1 ATOM 2857 N N . ALA B 2 124 ? 42.510 106.523 38.701 1.00 21.71 ? 124 ALA B N 1 ATOM 2858 C CA . ALA B 2 124 ? 41.816 106.253 37.438 1.00 22.82 ? 124 ALA B CA 1 ATOM 2859 C C . ALA B 2 124 ? 41.740 107.489 36.510 1.00 23.55 ? 124 ALA B C 1 ATOM 2860 O O . ALA B 2 124 ? 41.913 107.353 35.294 1.00 24.77 ? 124 ALA B O 1 ATOM 2861 C CB . ALA B 2 124 ? 40.436 105.681 37.707 1.00 22.97 ? 124 ALA B CB 1 ATOM 2862 N N . LYS B 2 125 ? 41.600 108.683 37.094 1.00 23.28 ? 125 LYS B N 1 ATOM 2863 C CA . LYS B 2 125 ? 41.608 109.939 36.348 1.00 24.07 ? 125 LYS B CA 1 ATOM 2864 C C . LYS B 2 125 ? 42.979 110.308 35.758 1.00 24.01 ? 125 LYS B C 1 ATOM 2865 O O . LYS B 2 125 ? 43.120 111.327 35.075 1.00 23.22 ? 125 LYS B O 1 ATOM 2866 C CB . LYS B 2 125 ? 41.065 111.079 37.218 1.00 24.89 ? 125 LYS B CB 1 ATOM 2867 C CG . LYS B 2 125 ? 41.948 111.458 38.391 1.00 25.95 ? 125 LYS B CG 1 ATOM 2868 C CD . LYS B 2 125 ? 41.443 112.693 39.101 1.00 29.12 ? 125 LYS B CD 1 ATOM 2869 C CE . LYS B 2 125 ? 42.263 112.931 40.359 1.00 30.97 ? 125 LYS B CE 1 ATOM 2870 N NZ . LYS B 2 125 ? 42.186 114.331 40.838 1.00 33.99 ? 125 LYS B NZ 1 ATOM 2871 N N . GLN B 2 126 ? 43.981 109.485 36.055 1.00 22.89 ? 126 GLN B N 1 ATOM 2872 C CA . GLN B 2 126 ? 45.317 109.596 35.500 1.00 22.79 ? 126 GLN B CA 1 ATOM 2873 C C . GLN B 2 126 ? 45.708 108.388 34.637 1.00 21.63 ? 126 GLN B C 1 ATOM 2874 O O . GLN B 2 126 ? 46.873 108.181 34.368 1.00 22.86 ? 126 GLN B O 1 ATOM 2875 C CB . GLN B 2 126 ? 46.305 109.742 36.648 1.00 24.06 ? 126 GLN B CB 1 ATOM 2876 C CG . GLN B 2 126 ? 45.997 110.935 37.519 1.00 24.72 ? 126 GLN B CG 1 ATOM 2877 C CD . GLN B 2 126 ? 47.023 111.141 38.600 1.00 25.04 ? 126 GLN B CD 1 ATOM 2878 O OE1 . GLN B 2 126 ? 47.324 110.219 39.363 1.00 24.72 ? 126 GLN B OE1 1 ATOM 2879 N NE2 . GLN B 2 126 ? 47.560 112.359 38.690 1.00 26.24 ? 126 GLN B NE2 1 ATOM 2880 N N . ALA B 2 127 ? 44.725 107.613 34.209 1.00 22.60 ? 127 ALA B N 1 ATOM 2881 C CA . ALA B 2 127 ? 44.913 106.455 33.342 1.00 22.07 ? 127 ALA B CA 1 ATOM 2882 C C . ALA B 2 127 ? 44.273 106.695 31.978 1.00 21.39 ? 127 ALA B C 1 ATOM 2883 O O . ALA B 2 127 ? 43.165 107.222 31.891 1.00 19.91 ? 127 ALA B O 1 ATOM 2884 C CB . ALA B 2 127 ? 44.277 105.240 33.962 1.00 22.34 ? 127 ALA B CB 1 ATOM 2885 N N . TRP B 2 128 ? 44.965 106.251 30.932 1.00 20.94 ? 128 TRP B N 1 ATOM 2886 C CA . TRP B 2 128 ? 44.596 106.518 29.540 1.00 21.16 ? 128 TRP B CA 1 ATOM 2887 C C . TRP B 2 128 ? 44.842 105.275 28.702 1.00 21.49 ? 128 TRP B C 1 ATOM 2888 O O . TRP B 2 128 ? 45.781 104.539 28.960 1.00 21.81 ? 128 TRP B O 1 ATOM 2889 C CB . TRP B 2 128 ? 45.426 107.680 28.988 1.00 20.64 ? 128 TRP B CB 1 ATOM 2890 C CG . TRP B 2 128 ? 45.310 108.889 29.860 1.00 21.89 ? 128 TRP B CG 1 ATOM 2891 C CD1 . TRP B 2 128 ? 46.116 109.217 30.925 1.00 22.38 ? 128 TRP B CD1 1 ATOM 2892 C CD2 . TRP B 2 128 ? 44.290 109.897 29.806 1.00 22.02 ? 128 TRP B CD2 1 ATOM 2893 N NE1 . TRP B 2 128 ? 45.648 110.363 31.537 1.00 22.19 ? 128 TRP B NE1 1 ATOM 2894 C CE2 . TRP B 2 128 ? 44.545 110.810 30.859 1.00 22.10 ? 128 TRP B CE2 1 ATOM 2895 C CE3 . TRP B 2 128 ? 43.200 110.133 28.960 1.00 22.72 ? 128 TRP B CE3 1 ATOM 2896 C CZ2 . TRP B 2 128 ? 43.742 111.941 31.084 1.00 22.71 ? 128 TRP B CZ2 1 ATOM 2897 C CZ3 . TRP B 2 128 ? 42.398 111.264 29.184 1.00 22.07 ? 128 TRP B CZ3 1 ATOM 2898 C CH2 . TRP B 2 128 ? 42.674 112.146 30.239 1.00 22.02 ? 128 TRP B CH2 1 ATOM 2899 N N . ARG B 2 129 ? 43.986 105.066 27.717 1.00 20.74 ? 129 ARG B N 1 ATOM 2900 C CA . ARG B 2 129 ? 44.174 104.110 26.668 1.00 20.73 ? 129 ARG B CA 1 ATOM 2901 C C . ARG B 2 129 ? 44.557 104.878 25.401 1.00 21.69 ? 129 ARG B C 1 ATOM 2902 O O . ARG B 2 129 ? 43.732 105.635 24.828 1.00 20.90 ? 129 ARG B O 1 ATOM 2903 C CB . ARG B 2 129 ? 42.894 103.323 26.431 1.00 21.17 ? 129 ARG B CB 1 ATOM 2904 C CG . ARG B 2 129 ? 43.050 102.276 25.338 1.00 21.30 ? 129 ARG B CG 1 ATOM 2905 C CD . ARG B 2 129 ? 41.739 101.786 24.810 1.00 21.49 ? 129 ARG B CD 1 ATOM 2906 N NE . ARG B 2 129 ? 40.959 101.079 25.801 1.00 21.81 ? 129 ARG B NE 1 ATOM 2907 C CZ . ARG B 2 129 ? 39.693 100.730 25.640 1.00 21.76 ? 129 ARG B CZ 1 ATOM 2908 N NH1 . ARG B 2 129 ? 39.029 101.055 24.523 1.00 23.93 ? 129 ARG B NH1 1 ATOM 2909 N NH2 . ARG B 2 129 ? 39.074 100.081 26.602 1.00 21.03 ? 129 ARG B NH2 1 ATOM 2910 N N . ILE B 2 130 ? 45.806 104.713 24.979 1.00 20.76 ? 130 ILE B N 1 ATOM 2911 C CA . ILE B 2 130 ? 46.233 105.188 23.663 1.00 21.40 ? 130 ILE B CA 1 ATOM 2912 C C . ILE B 2 130 ? 45.793 104.139 22.647 1.00 22.72 ? 130 ILE B C 1 ATOM 2913 O O . ILE B 2 130 ? 46.218 102.973 22.714 1.00 20.55 ? 130 ILE B O 1 ATOM 2914 C CB . ILE B 2 130 ? 47.736 105.407 23.596 1.00 22.19 ? 130 ILE B CB 1 ATOM 2915 C CG1 . ILE B 2 130 ? 48.119 106.467 24.623 1.00 22.53 ? 130 ILE B CG1 1 ATOM 2916 C CG2 . ILE B 2 130 ? 48.146 105.825 22.176 1.00 22.58 ? 130 ILE B CG2 1 ATOM 2917 C CD1 . ILE B 2 130 ? 49.588 106.627 24.860 1.00 23.89 ? 130 ILE B CD1 1 ATOM 2918 N N . GLY B 2 131 ? 44.926 104.551 21.729 1.00 22.27 ? 131 GLY B N 1 ATOM 2919 C CA . GLY B 2 131 ? 44.386 103.652 20.741 1.00 24.28 ? 131 GLY B CA 1 ATOM 2920 C C . GLY B 2 131 ? 43.171 104.176 20.005 1.00 24.52 ? 131 GLY B C 1 ATOM 2921 O O . GLY B 2 131 ? 42.370 104.935 20.550 1.00 22.35 ? 131 GLY B O 1 ATOM 2922 N N . ASN B 2 132 ? 43.010 103.727 18.763 1.00 24.39 ? 132 ASN B N 1 ATOM 2923 C CA . ASN B 2 132 ? 41.886 104.167 17.940 1.00 24.80 ? 132 ASN B CA 1 ATOM 2924 C C . ASN B 2 132 ? 40.558 103.664 18.412 1.00 24.37 ? 132 ASN B C 1 ATOM 2925 O O . ASN B 2 132 ? 39.555 104.372 18.284 1.00 25.96 ? 132 ASN B O 1 ATOM 2926 C CB . ASN B 2 132 ? 42.071 103.802 16.442 1.00 27.41 ? 132 ASN B CB 1 ATOM 2927 C CG . ASN B 2 132 ? 42.419 104.997 15.558 1.00 30.06 ? 132 ASN B CG 1 ATOM 2928 O OD1 . ASN B 2 132 ? 42.317 106.143 16.006 1.00 36.74 ? 132 ASN B OD1 1 ATOM 2929 N ND2 . ASN B 2 132 ? 42.823 104.768 14.336 1.00 31.48 ? 132 ASN B ND2 1 ATOM 2930 N N . TYR B 2 133 ? 40.538 102.450 18.941 1.00 21.92 ? 133 TYR B N 1 ATOM 2931 C CA . TYR B 2 133 ? 39.327 101.854 19.446 1.00 23.04 ? 133 TYR B CA 1 ATOM 2932 C C . TYR B 2 133 ? 39.154 102.302 20.907 1.00 23.57 ? 133 TYR B C 1 ATOM 2933 O O . TYR B 2 133 ? 39.929 101.892 21.792 1.00 21.07 ? 133 TYR B O 1 ATOM 2934 C CB . TYR B 2 133 ? 39.419 100.344 19.370 1.00 23.81 ? 133 TYR B CB 1 ATOM 2935 C CG . TYR B 2 133 ? 38.149 99.650 19.754 1.00 23.80 ? 133 TYR B CG 1 ATOM 2936 C CD1 . TYR B 2 133 ? 37.878 99.324 21.091 1.00 23.83 ? 133 TYR B CD1 1 ATOM 2937 C CD2 . TYR B 2 133 ? 37.220 99.320 18.799 1.00 25.07 ? 133 TYR B CD2 1 ATOM 2938 C CE1 . TYR B 2 133 ? 36.716 98.664 21.441 1.00 26.50 ? 133 TYR B CE1 1 ATOM 2939 C CE2 . TYR B 2 133 ? 36.052 98.652 19.138 1.00 25.49 ? 133 TYR B CE2 1 ATOM 2940 C CZ . TYR B 2 133 ? 35.805 98.336 20.447 1.00 25.37 ? 133 TYR B CZ 1 ATOM 2941 O OH . TYR B 2 133 ? 34.637 97.703 20.755 1.00 28.11 ? 133 TYR B OH 1 ATOM 2942 N N . VAL B 2 134 ? 38.163 103.164 21.119 1.00 21.92 ? 134 VAL B N 1 ATOM 2943 C CA . VAL B 2 134 ? 37.969 103.886 22.395 1.00 21.99 ? 134 VAL B CA 1 ATOM 2944 C C . VAL B 2 134 ? 36.845 103.302 23.255 1.00 22.67 ? 134 VAL B C 1 ATOM 2945 O O . VAL B 2 134 ? 36.660 103.738 24.372 1.00 22.46 ? 134 VAL B O 1 ATOM 2946 C CB . VAL B 2 134 ? 37.646 105.380 22.179 1.00 22.49 ? 134 VAL B CB 1 ATOM 2947 C CG1 . VAL B 2 134 ? 38.798 106.070 21.471 1.00 22.33 ? 134 VAL B CG1 1 ATOM 2948 C CG2 . VAL B 2 134 ? 36.302 105.594 21.433 1.00 23.00 ? 134 VAL B CG2 1 ATOM 2949 N N . GLU B 2 135 ? 36.110 102.322 22.740 1.00 23.00 ? 135 GLU B N 1 ATOM 2950 C CA . GLU B 2 135 ? 34.931 101.809 23.431 1.00 25.65 ? 135 GLU B CA 1 ATOM 2951 C C . GLU B 2 135 ? 35.316 100.960 24.626 1.00 25.42 ? 135 GLU B C 1 ATOM 2952 O O . GLU B 2 135 ? 36.374 100.290 24.601 1.00 23.26 ? 135 GLU B O 1 ATOM 2953 C CB . GLU B 2 135 ? 34.063 100.901 22.557 1.00 28.08 ? 135 GLU B CB 1 ATOM 2954 C CG . GLU B 2 135 ? 33.746 101.385 21.158 1.00 33.49 ? 135 GLU B CG 1 ATOM 2955 C CD . GLU B 2 135 ? 33.121 102.742 21.138 1.00 36.82 ? 135 GLU B CD 1 ATOM 2956 O OE1 . GLU B 2 135 ? 32.303 103.013 22.047 1.00 42.89 ? 135 GLU B OE1 1 ATOM 2957 O OE2 . GLU B 2 135 ? 33.442 103.529 20.211 1.00 44.18 ? 135 GLU B OE2 1 ATOM 2958 N N . PRO B 2 136 ? 34.418 100.899 25.618 1.00 24.82 ? 136 PRO B N 1 ATOM 2959 C CA . PRO B 2 136 ? 34.610 99.925 26.666 1.00 25.11 ? 136 PRO B CA 1 ATOM 2960 C C . PRO B 2 136 ? 34.596 98.515 26.109 1.00 25.74 ? 136 PRO B C 1 ATOM 2961 O O . PRO B 2 136 ? 33.833 98.212 25.187 1.00 25.17 ? 136 PRO B O 1 ATOM 2962 C CB . PRO B 2 136 ? 33.397 100.150 27.594 1.00 26.02 ? 136 PRO B CB 1 ATOM 2963 C CG . PRO B 2 136 ? 32.943 101.546 27.308 1.00 25.95 ? 136 PRO B CG 1 ATOM 2964 C CD . PRO B 2 136 ? 33.176 101.680 25.825 1.00 25.02 ? 136 PRO B CD 1 ATOM 2965 N N . ILE B 2 137 ? 35.446 97.656 26.651 1.00 23.99 ? 137 ILE B N 1 ATOM 2966 C CA . ILE B 2 137 ? 35.512 96.277 26.208 1.00 24.17 ? 137 ILE B CA 1 ATOM 2967 C C . ILE B 2 137 ? 34.683 95.437 27.164 1.00 24.14 ? 137 ILE B C 1 ATOM 2968 O O . ILE B 2 137 ? 34.972 95.393 28.375 1.00 23.33 ? 137 ILE B O 1 ATOM 2969 C CB . ILE B 2 137 ? 36.976 95.802 26.160 1.00 27.05 ? 137 ILE B CB 1 ATOM 2970 C CG1 . ILE B 2 137 ? 37.741 96.605 25.097 1.00 29.17 ? 137 ILE B CG1 1 ATOM 2971 C CG2 . ILE B 2 137 ? 37.055 94.313 25.822 1.00 27.20 ? 137 ILE B CG2 1 ATOM 2972 C CD1 . ILE B 2 137 ? 39.238 96.611 25.280 1.00 31.65 ? 137 ILE B CD1 1 ATOM 2973 N N . VAL B 2 138 ? 33.681 94.752 26.635 1.00 21.79 ? 138 VAL B N 1 ATOM 2974 C CA . VAL B 2 138 ? 32.759 93.988 27.450 1.00 23.69 ? 138 VAL B CA 1 ATOM 2975 C C . VAL B 2 138 ? 33.291 92.583 27.667 1.00 23.83 ? 138 VAL B C 1 ATOM 2976 O O . VAL B 2 138 ? 33.664 91.927 26.720 1.00 23.55 ? 138 VAL B O 1 ATOM 2977 C CB . VAL B 2 138 ? 31.368 93.936 26.822 1.00 24.47 ? 138 VAL B CB 1 ATOM 2978 C CG1 . VAL B 2 138 ? 30.409 93.081 27.653 1.00 25.40 ? 138 VAL B CG1 1 ATOM 2979 C CG2 . VAL B 2 138 ? 30.844 95.352 26.676 1.00 25.06 ? 138 VAL B CG2 1 ATOM 2980 N N . THR B 2 139 ? 33.333 92.125 28.919 1.00 22.84 ? 139 THR B N 1 ATOM 2981 C CA . THR B 2 139 ? 33.994 90.866 29.225 1.00 24.25 ? 139 THR B CA 1 ATOM 2982 C C . THR B 2 139 ? 33.443 90.159 30.462 1.00 23.55 ? 139 THR B C 1 ATOM 2983 O O . THR B 2 139 ? 32.712 90.751 31.271 1.00 21.96 ? 139 THR B O 1 ATOM 2984 C CB . THR B 2 139 ? 35.519 91.105 29.409 1.00 26.15 ? 139 THR B CB 1 ATOM 2985 O OG1 . THR B 2 139 ? 36.196 89.838 29.345 1.00 32.38 ? 139 THR B OG1 1 ATOM 2986 C CG2 . THR B 2 139 ? 35.813 91.802 30.738 1.00 24.89 ? 139 THR B CG2 1 ATOM 2987 N N . THR B 2 140 ? 33.778 88.881 30.587 1.00 23.09 ? 140 THR B N 1 ATOM 2988 C CA . THR B 2 140 ? 33.699 88.190 31.874 1.00 22.29 ? 140 THR B CA 1 ATOM 2989 C C . THR B 2 140 ? 35.117 88.141 32.434 1.00 21.99 ? 140 THR B C 1 ATOM 2990 O O . THR B 2 140 ? 36.101 88.286 31.703 1.00 20.36 ? 140 THR B O 1 ATOM 2991 C CB . THR B 2 140 ? 33.084 86.788 31.774 1.00 23.07 ? 140 THR B CB 1 ATOM 2992 O OG1 . THR B 2 140 ? 33.890 85.955 30.948 1.00 23.41 ? 140 THR B OG1 1 ATOM 2993 C CG2 . THR B 2 140 ? 31.662 86.851 31.181 1.00 24.48 ? 140 THR B CG2 1 ATOM 2994 N N . ILE B 2 141 ? 35.197 87.969 33.748 1.00 22.02 ? 141 ILE B N 1 ATOM 2995 C CA . ILE B 2 141 ? 36.461 87.967 34.468 1.00 21.95 ? 141 ILE B CA 1 ATOM 2996 C C . ILE B 2 141 ? 36.454 86.691 35.276 1.00 22.10 ? 141 ILE B C 1 ATOM 2997 O O . ILE B 2 141 ? 35.658 86.548 36.200 1.00 22.98 ? 141 ILE B O 1 ATOM 2998 C CB . ILE B 2 141 ? 36.608 89.179 35.378 1.00 21.99 ? 141 ILE B CB 1 ATOM 2999 C CG1 . ILE B 2 141 ? 36.685 90.459 34.535 1.00 21.62 ? 141 ILE B CG1 1 ATOM 3000 C CG2 . ILE B 2 141 ? 37.867 89.033 36.226 1.00 23.21 ? 141 ILE B CG2 1 ATOM 3001 C CD1 . ILE B 2 141 ? 36.677 91.738 35.326 1.00 21.62 ? 141 ILE B CD1 1 ATOM 3002 N N . ILE B 2 142 ? 37.330 85.776 34.909 1.00 21.00 ? 142 ILE B N 1 ATOM 3003 C CA . ILE B 2 142 ? 37.326 84.430 35.431 1.00 22.67 ? 142 ILE B CA 1 ATOM 3004 C C . ILE B 2 142 ? 38.451 84.277 36.422 1.00 23.33 ? 142 ILE B C 1 ATOM 3005 O O . ILE B 2 142 ? 39.551 84.741 36.176 1.00 24.21 ? 142 ILE B O 1 ATOM 3006 C CB . ILE B 2 142 ? 37.479 83.415 34.299 1.00 24.33 ? 142 ILE B CB 1 ATOM 3007 C CG1 . ILE B 2 142 ? 36.363 83.708 33.294 1.00 25.61 ? 142 ILE B CG1 1 ATOM 3008 C CG2 . ILE B 2 142 ? 37.384 81.983 34.835 1.00 24.13 ? 142 ILE B CG2 1 ATOM 3009 C CD1 . ILE B 2 142 ? 36.365 82.851 32.066 1.00 28.29 ? 142 ILE B CD1 1 ATOM 3010 N N . GLY B 2 143 ? 38.154 83.623 37.539 1.00 23.60 ? 143 GLY B N 1 ATOM 3011 C CA . GLY B 2 143 ? 39.105 83.499 38.641 1.00 22.65 ? 143 GLY B CA 1 ATOM 3012 C C . GLY B 2 143 ? 39.125 82.104 39.200 1.00 22.30 ? 143 GLY B C 1 ATOM 3013 O O . GLY B 2 143 ? 38.869 81.131 38.509 1.00 21.67 ? 143 GLY B O 1 ATOM 3014 N N . LEU B 2 144 ? 39.418 82.027 40.490 1.00 22.88 ? 144 LEU B N 1 ATOM 3015 C CA . LEU B 2 144 ? 39.608 80.775 41.191 1.00 22.82 ? 144 LEU B CA 1 ATOM 3016 C C . LEU B 2 144 ? 38.461 79.789 41.007 1.00 23.04 ? 144 LEU B C 1 ATOM 3017 O O . LEU B 2 144 ? 37.290 80.181 40.951 1.00 22.61 ? 144 LEU B O 1 ATOM 3018 C CB . LEU B 2 144 ? 39.826 81.079 42.684 1.00 23.84 ? 144 LEU B CB 1 ATOM 3019 C CG . LEU B 2 144 ? 40.362 79.970 43.579 1.00 23.54 ? 144 LEU B CG 1 ATOM 3020 C CD1 . LEU B 2 144 ? 41.720 79.481 43.083 1.00 23.92 ? 144 LEU B CD1 1 ATOM 3021 C CD2 . LEU B 2 144 ? 40.474 80.504 45.006 1.00 23.71 ? 144 LEU B CD2 1 ATOM 3022 N N . ARG B 2 145 ? 38.814 78.511 40.861 1.00 24.38 ? 145 ARG B N 1 ATOM 3023 C CA . ARG B 2 145 ? 37.851 77.438 40.591 1.00 27.14 ? 145 ARG B CA 1 ATOM 3024 C C . ARG B 2 145 ? 37.068 77.631 39.266 1.00 26.16 ? 145 ARG B C 1 ATOM 3025 O O . ARG B 2 145 ? 35.965 77.082 39.082 1.00 25.59 ? 145 ARG B O 1 ATOM 3026 C CB . ARG B 2 145 ? 36.917 77.201 41.802 1.00 30.51 ? 145 ARG B CB 1 ATOM 3027 C CG . ARG B 2 145 ? 37.639 76.521 42.973 1.00 35.94 ? 145 ARG B CG 1 ATOM 3028 C CD . ARG B 2 145 ? 36.696 76.107 44.104 1.00 41.19 ? 145 ARG B CD 1 ATOM 3029 N NE . ARG B 2 145 ? 35.813 74.981 43.766 1.00 46.69 ? 145 ARG B NE 1 ATOM 3030 C CZ . ARG B 2 145 ? 36.004 73.692 44.092 1.00 52.62 ? 145 ARG B CZ 1 ATOM 3031 N NH1 . ARG B 2 145 ? 37.075 73.276 44.775 1.00 53.01 ? 145 ARG B NH1 1 ATOM 3032 N NH2 . ARG B 2 145 ? 35.108 72.788 43.710 1.00 56.44 ? 145 ARG B NH2 1 ATOM 3033 N N . HIS B 2 146 ? 37.660 78.383 38.338 1.00 24.95 ? 146 HIS B N 1 ATOM 3034 C CA . HIS B 2 146 ? 37.064 78.637 37.013 1.00 25.11 ? 146 HIS B CA 1 ATOM 3035 C C . HIS B 2 146 ? 35.697 79.343 37.139 1.00 25.90 ? 146 HIS B C 1 ATOM 3036 O O . HIS B 2 146 ? 34.830 79.191 36.277 1.00 25.09 ? 146 HIS B O 1 ATOM 3037 C CB . HIS B 2 146 ? 36.917 77.336 36.207 1.00 25.59 ? 146 HIS B CB 1 ATOM 3038 C CG . HIS B 2 146 ? 38.084 76.397 36.339 1.00 25.22 ? 146 HIS B CG 1 ATOM 3039 N ND1 . HIS B 2 146 ? 39.281 76.597 35.690 1.00 26.06 ? 146 HIS B ND1 1 ATOM 3040 C CD2 . HIS B 2 146 ? 38.234 75.262 37.062 1.00 24.83 ? 146 HIS B CD2 1 ATOM 3041 C CE1 . HIS B 2 146 ? 40.124 75.633 36.014 1.00 26.44 ? 146 HIS B CE1 1 ATOM 3042 N NE2 . HIS B 2 146 ? 39.514 74.812 36.853 1.00 25.05 ? 146 HIS B NE2 1 ATOM 3043 N N . MET B 2 147 ? 35.526 80.117 38.212 1.00 26.10 ? 147 MET B N 1 ATOM 3044 C CA . MET B 2 147 ? 34.299 80.883 38.453 1.00 26.67 ? 147 MET B CA 1 ATOM 3045 C C . MET B 2 147 ? 34.427 82.301 37.901 1.00 26.07 ? 147 MET B C 1 ATOM 3046 O O . MET B 2 147 ? 35.515 82.740 37.564 1.00 25.39 ? 147 MET B O 1 ATOM 3047 C CB . MET B 2 147 ? 33.961 80.882 39.942 1.00 27.74 ? 147 MET B CB 1 ATOM 3048 C CG . MET B 2 147 ? 33.506 79.513 40.440 1.00 29.81 ? 147 MET B CG 1 ATOM 3049 S SD . MET B 2 147 ? 33.179 79.532 42.220 1.00 34.93 ? 147 MET B SD 1 ATOM 3050 C CE . MET B 2 147 ? 32.424 77.938 42.435 1.00 36.25 ? 147 MET B CE 1 ATOM 3051 N N . CYS B 2 148 ? 33.290 82.992 37.817 1.00 26.81 ? 148 CYS B N 1 ATOM 3052 C CA . CYS B 2 148 ? 33.169 84.331 37.215 1.00 28.15 ? 148 CYS B CA 1 ATOM 3053 C C . CYS B 2 148 ? 32.892 85.378 38.291 1.00 24.73 ? 148 CYS B C 1 ATOM 3054 O O . CYS B 2 148 ? 32.089 85.129 39.185 1.00 23.52 ? 148 CYS B O 1 ATOM 3055 C CB . CYS B 2 148 ? 31.993 84.339 36.182 1.00 29.69 ? 148 CYS B CB 1 ATOM 3056 S SG . CYS B 2 148 ? 32.415 83.664 34.541 1.00 38.51 ? 148 CYS B SG 1 ATOM 3057 N N . LEU B 2 149 ? 33.504 86.556 38.196 1.00 23.06 ? 149 LEU B N 1 ATOM 3058 C CA . LEU B 2 149 ? 33.113 87.653 39.075 1.00 23.75 ? 149 LEU B CA 1 ATOM 3059 C C . LEU B 2 149 ? 31.695 88.081 38.721 1.00 23.04 ? 149 LEU B C 1 ATOM 3060 O O . LEU B 2 149 ? 31.362 88.197 37.539 1.00 22.92 ? 149 LEU B O 1 ATOM 3061 C CB . LEU B 2 149 ? 34.021 88.866 38.932 1.00 24.96 ? 149 LEU B CB 1 ATOM 3062 C CG . LEU B 2 149 ? 35.392 88.857 39.579 1.00 27.47 ? 149 LEU B CG 1 ATOM 3063 C CD1 . LEU B 2 149 ? 36.029 90.215 39.335 1.00 28.78 ? 149 LEU B CD1 1 ATOM 3064 C CD2 . LEU B 2 149 ? 35.339 88.549 41.076 1.00 27.12 ? 149 LEU B CD2 1 ATOM 3065 N N . GLU B 2 150 ? 30.890 88.335 39.740 1.00 22.52 ? 150 GLU B N 1 ATOM 3066 C CA . GLU B 2 150 ? 29.497 88.732 39.569 1.00 22.87 ? 150 GLU B CA 1 ATOM 3067 C C . GLU B 2 150 ? 29.177 89.915 40.476 1.00 22.85 ? 150 GLU B C 1 ATOM 3068 O O . GLU B 2 150 ? 29.627 89.975 41.615 1.00 22.40 ? 150 GLU B O 1 ATOM 3069 C CB . GLU B 2 150 ? 28.588 87.531 39.856 1.00 24.55 ? 150 GLU B CB 1 ATOM 3070 C CG . GLU B 2 150 ? 27.097 87.807 39.654 1.00 25.75 ? 150 GLU B CG 1 ATOM 3071 C CD . GLU B 2 150 ? 26.236 86.579 39.841 1.00 27.19 ? 150 GLU B CD 1 ATOM 3072 O OE1 . GLU B 2 150 ? 26.565 85.518 39.285 1.00 28.15 ? 150 GLU B OE1 1 ATOM 3073 O OE2 . GLU B 2 150 ? 25.215 86.672 40.550 1.00 29.98 ? 150 GLU B OE2 1 ATOM 3074 N N . ALA B 2 151 ? 28.442 90.882 39.943 1.00 22.52 ? 151 ALA B N 1 ATOM 3075 C CA . ALA B 2 151 ? 27.960 92.020 40.693 1.00 22.85 ? 151 ALA B CA 1 ATOM 3076 C C . ALA B 2 151 ? 26.742 91.560 41.471 1.00 24.24 ? 151 ALA B C 1 ATOM 3077 O O . ALA B 2 151 ? 25.802 90.998 40.892 1.00 24.36 ? 151 ALA B O 1 ATOM 3078 C CB . ALA B 2 151 ? 27.607 93.166 39.749 1.00 23.47 ? 151 ALA B CB 1 ATOM 3079 N N . THR B 2 152 ? 26.770 91.764 42.788 1.00 24.71 ? 152 THR B N 1 ATOM 3080 C CA . THR B 2 152 ? 25.746 91.229 43.685 1.00 25.28 ? 152 THR B CA 1 ATOM 3081 C C . THR B 2 152 ? 25.186 92.306 44.606 1.00 25.73 ? 152 THR B C 1 ATOM 3082 O O . THR B 2 152 ? 25.733 93.416 44.687 1.00 24.62 ? 152 THR B O 1 ATOM 3083 C CB . THR B 2 152 ? 26.334 90.106 44.555 1.00 25.48 ? 152 THR B CB 1 ATOM 3084 O OG1 . THR B 2 152 ? 27.442 90.612 45.316 1.00 25.32 ? 152 THR B OG1 1 ATOM 3085 C CG2 . THR B 2 152 ? 26.786 88.962 43.681 1.00 26.22 ? 152 THR B CG2 1 ATOM 3086 N N . ASP B 2 153 ? 24.118 91.948 45.326 1.00 27.41 ? 153 ASP B N 1 ATOM 3087 C CA . ASP B 2 153 ? 23.514 92.840 46.348 1.00 27.80 ? 153 ASP B CA 1 ATOM 3088 C C . ASP B 2 153 ? 23.201 94.190 45.741 1.00 27.19 ? 153 ASP B C 1 ATOM 3089 O O . ASP B 2 153 ? 23.670 95.240 46.209 1.00 28.27 ? 153 ASP B O 1 ATOM 3090 C CB . ASP B 2 153 ? 24.434 93.018 47.563 1.00 27.90 ? 153 ASP B CB 1 ATOM 3091 C CG . ASP B 2 153 ? 24.687 91.733 48.289 1.00 28.85 ? 153 ASP B CG 1 ATOM 3092 O OD1 . ASP B 2 153 ? 23.857 90.819 48.201 1.00 31.32 ? 153 ASP B OD1 1 ATOM 3093 O OD2 . ASP B 2 153 ? 25.742 91.621 48.947 1.00 30.35 ? 153 ASP B OD2 1 ATOM 3094 N N . ASN B 2 154 ? 22.417 94.173 44.669 1.00 29.25 ? 154 ASN B N 1 ATOM 3095 C CA . ASN B 2 154 ? 22.044 95.399 43.974 1.00 32.01 ? 154 ASN B CA 1 ATOM 3096 C C . ASN B 2 154 ? 23.259 96.205 43.515 1.00 29.11 ? 154 ASN B C 1 ATOM 3097 O O . ASN B 2 154 ? 23.311 97.421 43.698 1.00 27.73 ? 154 ASN B O 1 ATOM 3098 C CB . ASN B 2 154 ? 21.145 96.264 44.860 1.00 35.95 ? 154 ASN B CB 1 ATOM 3099 C CG . ASN B 2 154 ? 19.790 95.630 45.110 1.00 40.61 ? 154 ASN B CG 1 ATOM 3100 O OD1 . ASN B 2 154 ? 19.394 95.417 46.256 1.00 48.80 ? 154 ASN B OD1 1 ATOM 3101 N ND2 . ASN B 2 154 ? 19.073 95.325 44.035 1.00 45.30 ? 154 ASN B ND2 1 ATOM 3102 N N . ASP B 2 155 ? 24.233 95.523 42.918 1.00 28.47 ? 155 ASP B N 1 ATOM 3103 C CA . ASP B 2 155 ? 25.448 96.185 42.431 1.00 27.35 ? 155 ASP B CA 1 ATOM 3104 C C . ASP B 2 155 ? 26.205 96.958 43.483 1.00 24.92 ? 155 ASP B C 1 ATOM 3105 O O . ASP B 2 155 ? 26.710 98.029 43.205 1.00 25.43 ? 155 ASP B O 1 ATOM 3106 C CB . ASP B 2 155 ? 25.131 97.125 41.248 1.00 29.10 ? 155 ASP B CB 1 ATOM 3107 C CG . ASP B 2 155 ? 24.462 96.418 40.087 1.00 30.31 ? 155 ASP B CG 1 ATOM 3108 O OD1 . ASP B 2 155 ? 24.566 95.183 39.945 1.00 32.23 ? 155 ASP B OD1 1 ATOM 3109 O OD2 . ASP B 2 155 ? 23.838 97.121 39.263 1.00 34.69 ? 155 ASP B OD2 1 ATOM 3110 N N . THR B 2 156 ? 26.305 96.407 44.691 1.00 25.28 ? 156 THR B N 1 ATOM 3111 C CA . THR B 2 156 ? 27.174 96.991 45.704 1.00 25.13 ? 156 THR B CA 1 ATOM 3112 C C . THR B 2 156 ? 28.328 96.095 46.107 1.00 23.64 ? 156 THR B C 1 ATOM 3113 O O . THR B 2 156 ? 29.282 96.581 46.683 1.00 27.30 ? 156 THR B O 1 ATOM 3114 C CB . THR B 2 156 ? 26.404 97.362 46.996 1.00 26.36 ? 156 THR B CB 1 ATOM 3115 O OG1 . THR B 2 156 ? 25.826 96.182 47.547 1.00 26.36 ? 156 THR B OG1 1 ATOM 3116 C CG2 . THR B 2 156 ? 25.310 98.410 46.708 1.00 27.45 ? 156 THR B CG2 1 ATOM 3117 N N . ASN B 2 157 ? 28.228 94.801 45.844 1.00 24.55 ? 157 ASN B N 1 ATOM 3118 C CA . ASN B 2 157 ? 29.278 93.846 46.181 1.00 24.04 ? 157 ASN B CA 1 ATOM 3119 C C . ASN B 2 157 ? 29.675 93.028 44.965 1.00 24.11 ? 157 ASN B C 1 ATOM 3120 O O . ASN B 2 157 ? 29.039 93.104 43.902 1.00 23.43 ? 157 ASN B O 1 ATOM 3121 C CB . ASN B 2 157 ? 28.810 92.937 47.312 1.00 23.04 ? 157 ASN B CB 1 ATOM 3122 C CG . ASN B 2 157 ? 28.883 93.621 48.666 1.00 24.28 ? 157 ASN B CG 1 ATOM 3123 O OD1 . ASN B 2 157 ? 29.847 94.333 48.979 1.00 22.18 ? 157 ASN B OD1 1 ATOM 3124 N ND2 . ASN B 2 157 ? 27.837 93.429 49.475 1.00 25.77 ? 157 ASN B ND2 1 ATOM 3125 N N . VAL B 2 158 ? 30.736 92.245 45.132 1.00 23.25 ? 158 VAL B N 1 ATOM 3126 C CA . VAL B 2 158 ? 31.270 91.446 44.049 1.00 22.84 ? 158 VAL B CA 1 ATOM 3127 C C . VAL B 2 158 ? 31.916 90.209 44.616 1.00 22.61 ? 158 VAL B C 1 ATOM 3128 O O . VAL B 2 158 ? 32.640 90.284 45.600 1.00 23.54 ? 158 VAL B O 1 ATOM 3129 C CB . VAL B 2 158 ? 32.239 92.283 43.161 1.00 23.35 ? 158 VAL B CB 1 ATOM 3130 C CG1 . VAL B 2 158 ? 33.428 92.815 43.950 1.00 24.46 ? 158 VAL B CG1 1 ATOM 3131 C CG2 . VAL B 2 158 ? 32.701 91.475 41.956 1.00 24.46 ? 158 VAL B CG2 1 ATOM 3132 N N . TRP B 2 159 ? 31.607 89.069 44.027 1.00 22.34 ? 159 TRP B N 1 ATOM 3133 C CA . TRP B 2 159 ? 32.289 87.815 44.366 1.00 23.49 ? 159 TRP B CA 1 ATOM 3134 C C . TRP B 2 159 ? 32.154 86.816 43.232 1.00 22.94 ? 159 TRP B C 1 ATOM 3135 O O . TRP B 2 159 ? 31.524 87.119 42.213 1.00 23.28 ? 159 TRP B O 1 ATOM 3136 C CB . TRP B 2 159 ? 31.781 87.246 45.707 1.00 23.15 ? 159 TRP B CB 1 ATOM 3137 C CG . TRP B 2 159 ? 30.335 86.908 45.771 1.00 24.55 ? 159 TRP B CG 1 ATOM 3138 C CD1 . TRP B 2 159 ? 29.715 85.862 45.176 1.00 24.37 ? 159 TRP B CD1 1 ATOM 3139 C CD2 . TRP B 2 159 ? 29.326 87.594 46.522 1.00 24.28 ? 159 TRP B CD2 1 ATOM 3140 N NE1 . TRP B 2 159 ? 28.381 85.856 45.476 1.00 24.88 ? 159 TRP B NE1 1 ATOM 3141 C CE2 . TRP B 2 159 ? 28.112 86.904 46.311 1.00 24.72 ? 159 TRP B CE2 1 ATOM 3142 C CE3 . TRP B 2 159 ? 29.331 88.706 47.372 1.00 25.00 ? 159 TRP B CE3 1 ATOM 3143 C CZ2 . TRP B 2 159 ? 26.899 87.298 46.910 1.00 25.09 ? 159 TRP B CZ2 1 ATOM 3144 C CZ3 . TRP B 2 159 ? 28.113 89.099 47.975 1.00 24.76 ? 159 TRP B CZ3 1 ATOM 3145 C CH2 . TRP B 2 159 ? 26.925 88.399 47.730 1.00 24.35 ? 159 TRP B CH2 1 ATOM 3146 N N . LEU B 2 160 ? 32.760 85.642 43.411 1.00 22.96 ? 160 LEU B N 1 ATOM 3147 C CA . LEU B 2 160 ? 32.777 84.587 42.416 1.00 23.55 ? 160 LEU B CA 1 ATOM 3148 C C . LEU B 2 160 ? 31.556 83.688 42.458 1.00 24.01 ? 160 LEU B C 1 ATOM 3149 O O . LEU B 2 160 ? 31.130 83.247 43.511 1.00 23.07 ? 160 LEU B O 1 ATOM 3150 C CB . LEU B 2 160 ? 34.025 83.725 42.593 1.00 23.09 ? 160 LEU B CB 1 ATOM 3151 C CG . LEU B 2 160 ? 35.326 84.414 42.205 1.00 24.71 ? 160 LEU B CG 1 ATOM 3152 C CD1 . LEU B 2 160 ? 36.503 83.628 42.737 1.00 26.58 ? 160 LEU B CD1 1 ATOM 3153 C CD2 . LEU B 2 160 ? 35.452 84.558 40.688 1.00 25.95 ? 160 LEU B CD2 1 ATOM 3154 N N . GLU B 2 161 ? 31.009 83.411 41.287 1.00 24.17 ? 161 GLU B N 1 ATOM 3155 C CA . GLU B 2 161 ? 29.918 82.466 41.126 1.00 24.31 ? 161 GLU B CA 1 ATOM 3156 C C . GLU B 2 161 ? 30.227 81.638 39.902 1.00 24.87 ? 161 GLU B C 1 ATOM 3157 O O . GLU B 2 161 ? 30.986 82.069 39.023 1.00 24.72 ? 161 GLU B O 1 ATOM 3158 C CB . GLU B 2 161 ? 28.603 83.211 40.888 1.00 24.55 ? 161 GLU B CB 1 ATOM 3159 C CG . GLU B 2 161 ? 28.065 84.010 42.056 1.00 25.85 ? 161 GLU B CG 1 ATOM 3160 C CD . GLU B 2 161 ? 27.465 83.161 43.166 1.00 28.49 ? 161 GLU B CD 1 ATOM 3161 O OE1 . GLU B 2 161 ? 27.337 81.934 43.018 1.00 31.28 ? 161 GLU B OE1 1 ATOM 3162 O OE2 . GLU B 2 161 ? 27.145 83.726 44.225 1.00 29.89 ? 161 GLU B OE2 1 ATOM 3163 N N . SER B 2 162 ? 29.593 80.480 39.802 1.00 25.27 ? 162 SER B N 1 ATOM 3164 C CA . SER B 2 162 ? 29.739 79.635 38.615 1.00 27.44 ? 162 SER B CA 1 ATOM 3165 C C . SER B 2 162 ? 29.341 80.390 37.360 1.00 26.35 ? 162 SER B C 1 ATOM 3166 O O . SER B 2 162 ? 28.345 81.090 37.366 1.00 25.92 ? 162 SER B O 1 ATOM 3167 C CB . SER B 2 162 ? 28.913 78.357 38.735 1.00 27.68 ? 162 SER B CB 1 ATOM 3168 O OG . SER B 2 162 ? 29.567 77.489 39.636 1.00 31.38 ? 162 SER B OG 1 ATOM 3169 N N . CYS B 2 163 ? 30.154 80.263 36.311 1.00 26.88 ? 163 CYS B N 1 ATOM 3170 C CA . CYS B 2 163 ? 29.969 81.034 35.088 1.00 27.86 ? 163 CYS B CA 1 ATOM 3171 C C . CYS B 2 163 ? 28.707 80.556 34.374 1.00 27.35 ? 163 CYS B C 1 ATOM 3172 O O . CYS B 2 163 ? 28.517 79.355 34.204 1.00 25.76 ? 163 CYS B O 1 ATOM 3173 C CB . CYS B 2 163 ? 31.154 80.833 34.161 1.00 31.64 ? 163 CYS B CB 1 ATOM 3174 S SG . CYS B 2 163 ? 32.685 81.598 34.733 1.00 35.95 ? 163 CYS B SG 1 ATOM 3175 N N . VAL B 2 164 ? 27.848 81.493 33.996 1.00 27.11 ? 164 VAL B N 1 ATOM 3176 C CA . VAL B 2 164 ? 26.619 81.202 33.258 1.00 29.31 ? 164 VAL B CA 1 ATOM 3177 C C . VAL B 2 164 ? 26.566 82.192 32.100 1.00 29.09 ? 164 VAL B C 1 ATOM 3178 O O . VAL B 2 164 ? 26.494 83.401 32.314 1.00 29.24 ? 164 VAL B O 1 ATOM 3179 C CB . VAL B 2 164 ? 25.359 81.324 34.149 1.00 29.42 ? 164 VAL B CB 1 ATOM 3180 C CG1 . VAL B 2 164 ? 24.079 81.118 33.344 1.00 30.25 ? 164 VAL B CG1 1 ATOM 3181 C CG2 . VAL B 2 164 ? 25.405 80.298 35.275 1.00 30.35 ? 164 VAL B CG2 1 ATOM 3182 N N . LYS B 2 165 ? 26.608 81.660 30.883 1.00 31.12 ? 165 LYS B N 1 ATOM 3183 C CA . LYS B 2 165 ? 26.644 82.455 29.660 1.00 33.57 ? 165 LYS B CA 1 ATOM 3184 C C . LYS B 2 165 ? 25.501 83.458 29.668 1.00 34.63 ? 165 LYS B C 1 ATOM 3185 O O . LYS B 2 165 ? 24.376 83.112 30.011 1.00 33.66 ? 165 LYS B O 1 ATOM 3186 C CB . LYS B 2 165 ? 26.524 81.532 28.451 1.00 37.44 ? 165 LYS B CB 1 ATOM 3187 C CG . LYS B 2 165 ? 26.751 82.193 27.102 1.00 42.63 ? 165 LYS B CG 1 ATOM 3188 C CD . LYS B 2 165 ? 26.912 81.138 26.003 1.00 46.89 ? 165 LYS B CD 1 ATOM 3189 C CE . LYS B 2 165 ? 26.610 81.701 24.619 1.00 51.25 ? 165 LYS B CE 1 ATOM 3190 N NZ . LYS B 2 165 ? 27.276 83.014 24.344 1.00 53.41 ? 165 LYS B NZ 1 ATOM 3191 N N . ASN B 2 166 ? 25.794 84.704 29.393 1.00 34.97 ? 166 ASN B N 1 ATOM 3192 C CA . ASN B 2 166 ? 24.756 85.707 29.331 1.00 43.41 ? 166 ASN B CA 1 ATOM 3193 C C . ASN B 2 166 ? 24.070 86.068 30.649 1.00 43.03 ? 166 ASN B C 1 ATOM 3194 O O . ASN B 2 166 ? 23.138 86.851 30.634 1.00 44.88 ? 166 ASN B O 1 ATOM 3195 C CB . ASN B 2 166 ? 23.730 85.396 28.239 1.00 49.76 ? 166 ASN B CB 1 ATOM 3196 N N . LYS B 2 167 ? 24.528 85.530 31.779 1.00 39.68 ? 167 LYS B N 1 ATOM 3197 C CA . LYS B 2 167 ? 23.986 85.973 33.062 1.00 35.55 ? 167 LYS B CA 1 ATOM 3198 C C . LYS B 2 167 ? 24.502 87.405 33.190 1.00 31.23 ? 167 LYS B C 1 ATOM 3199 O O . LYS B 2 167 ? 25.707 87.644 33.248 1.00 29.61 ? 167 LYS B O 1 ATOM 3200 C CB . LYS B 2 167 ? 24.424 85.064 34.211 1.00 36.86 ? 167 LYS B CB 1 ATOM 3201 C CG . LYS B 2 167 ? 23.870 85.473 35.563 1.00 38.50 ? 167 LYS B CG 1 ATOM 3202 C CD . LYS B 2 167 ? 23.964 84.329 36.569 1.00 40.63 ? 167 LYS B CD 1 ATOM 3203 C CE . LYS B 2 167 ? 23.591 84.768 37.984 1.00 41.57 ? 167 LYS B CE 1 ATOM 3204 N NZ . LYS B 2 167 ? 24.321 83.943 38.995 1.00 43.66 ? 167 LYS B NZ 1 ATOM 3205 N N . THR B 2 168 ? 23.568 88.353 33.164 1.00 29.69 ? 168 THR B N 1 ATOM 3206 C CA . THR B 2 168 ? 23.828 89.787 33.003 1.00 28.74 ? 168 THR B CA 1 ATOM 3207 C C . THR B 2 168 ? 24.865 90.363 33.950 1.00 26.56 ? 168 THR B C 1 ATOM 3208 O O . THR B 2 168 ? 25.733 91.142 33.533 1.00 24.13 ? 168 THR B O 1 ATOM 3209 C CB . THR B 2 168 ? 22.498 90.568 33.196 1.00 30.75 ? 168 THR B CB 1 ATOM 3210 O OG1 . THR B 2 168 ? 21.615 90.235 32.116 1.00 35.12 ? 168 THR B OG1 1 ATOM 3211 C CG2 . THR B 2 168 ? 22.686 92.054 33.175 1.00 32.87 ? 168 THR B CG2 1 ATOM 3212 N N . LYS B 2 169 ? 24.756 90.007 35.228 1.00 25.21 ? 169 LYS B N 1 ATOM 3213 C CA . LYS B 2 169 ? 25.618 90.607 36.259 1.00 25.42 ? 169 LYS B CA 1 ATOM 3214 C C . LYS B 2 169 ? 27.064 90.043 36.258 1.00 23.77 ? 169 LYS B C 1 ATOM 3215 O O . LYS B 2 169 ? 27.892 90.483 37.050 1.00 24.18 ? 169 LYS B O 1 ATOM 3216 C CB . LYS B 2 169 ? 24.972 90.460 37.655 1.00 26.13 ? 169 LYS B CB 1 ATOM 3217 C CG . LYS B 2 169 ? 23.705 91.301 37.893 1.00 26.47 ? 169 LYS B CG 1 ATOM 3218 C CD . LYS B 2 169 ? 23.868 92.780 37.575 1.00 26.53 ? 169 LYS B CD 1 ATOM 3219 C CE . LYS B 2 169 ? 22.605 93.577 37.921 1.00 28.26 ? 169 LYS B CE 1 ATOM 3220 N NZ . LYS B 2 169 ? 22.856 94.975 37.502 1.00 28.38 ? 169 LYS B NZ 1 ATOM 3221 N N . GLN B 2 170 ? 27.345 89.071 35.397 1.00 24.01 ? 170 GLN B N 1 ATOM 3222 C CA . GLN B 2 170 ? 28.706 88.548 35.227 1.00 23.62 ? 170 GLN B CA 1 ATOM 3223 C C . GLN B 2 170 ? 29.517 89.264 34.143 1.00 24.04 ? 170 GLN B C 1 ATOM 3224 O O . GLN B 2 170 ? 30.649 88.878 33.883 1.00 25.04 ? 170 GLN B O 1 ATOM 3225 C CB . GLN B 2 170 ? 28.652 87.054 34.961 1.00 23.49 ? 170 GLN B CB 1 ATOM 3226 C CG . GLN B 2 170 ? 28.157 86.292 36.160 1.00 22.87 ? 170 GLN B CG 1 ATOM 3227 C CD . GLN B 2 170 ? 28.211 84.792 36.030 1.00 23.27 ? 170 GLN B CD 1 ATOM 3228 O OE1 . GLN B 2 170 ? 28.482 84.231 34.973 1.00 24.42 ? 170 GLN B OE1 1 ATOM 3229 N NE2 . GLN B 2 170 ? 27.949 84.117 37.140 1.00 24.45 ? 170 GLN B NE2 1 ATOM 3230 N N . TYR B 2 171 ? 28.940 90.286 33.505 1.00 23.87 ? 171 TYR B N 1 ATOM 3231 C CA . TYR B 2 171 ? 29.612 91.047 32.444 1.00 23.32 ? 171 TYR B CA 1 ATOM 3232 C C . TYR B 2 171 ? 30.115 92.354 32.976 1.00 22.21 ? 171 TYR B C 1 ATOM 3233 O O . TYR B 2 171 ? 29.431 93.021 33.775 1.00 22.38 ? 171 TYR B O 1 ATOM 3234 C CB . TYR B 2 171 ? 28.693 91.235 31.202 1.00 23.08 ? 171 TYR B CB 1 ATOM 3235 C CG . TYR B 2 171 ? 28.528 89.907 30.525 1.00 25.07 ? 171 TYR B CG 1 ATOM 3236 C CD1 . TYR B 2 171 ? 27.655 88.973 31.043 1.00 26.60 ? 171 TYR B CD1 1 ATOM 3237 C CD2 . TYR B 2 171 ? 29.328 89.530 29.446 1.00 25.33 ? 171 TYR B CD2 1 ATOM 3238 C CE1 . TYR B 2 171 ? 27.539 87.710 30.505 1.00 26.73 ? 171 TYR B CE1 1 ATOM 3239 C CE2 . TYR B 2 171 ? 29.207 88.263 28.880 1.00 26.68 ? 171 TYR B CE2 1 ATOM 3240 C CZ . TYR B 2 171 ? 28.310 87.359 29.422 1.00 26.91 ? 171 TYR B CZ 1 ATOM 3241 O OH . TYR B 2 171 ? 28.143 86.082 28.910 1.00 28.43 ? 171 TYR B OH 1 ATOM 3242 N N . TRP B 2 172 ? 31.316 92.711 32.530 1.00 20.77 ? 172 TRP B N 1 ATOM 3243 C CA . TRP B 2 172 ? 32.019 93.898 32.968 1.00 21.48 ? 172 TRP B CA 1 ATOM 3244 C C . TRP B 2 172 ? 32.476 94.702 31.761 1.00 21.76 ? 172 TRP B C 1 ATOM 3245 O O . TRP B 2 172 ? 32.811 94.124 30.717 1.00 22.01 ? 172 TRP B O 1 ATOM 3246 C CB . TRP B 2 172 ? 33.217 93.501 33.838 1.00 21.84 ? 172 TRP B CB 1 ATOM 3247 C CG . TRP B 2 172 ? 32.807 92.674 35.004 1.00 21.58 ? 172 TRP B CG 1 ATOM 3248 C CD1 . TRP B 2 172 ? 32.732 91.316 35.051 1.00 22.05 ? 172 TRP B CD1 1 ATOM 3249 C CD2 . TRP B 2 172 ? 32.335 93.147 36.266 1.00 22.50 ? 172 TRP B CD2 1 ATOM 3250 N NE1 . TRP B 2 172 ? 32.275 90.908 36.276 1.00 22.75 ? 172 TRP B NE1 1 ATOM 3251 C CE2 . TRP B 2 172 ? 32.018 92.009 37.045 1.00 22.29 ? 172 TRP B CE2 1 ATOM 3252 C CE3 . TRP B 2 172 ? 32.142 94.416 36.814 1.00 21.60 ? 172 TRP B CE3 1 ATOM 3253 C CZ2 . TRP B 2 172 ? 31.524 92.103 38.364 1.00 22.53 ? 172 TRP B CZ2 1 ATOM 3254 C CZ3 . TRP B 2 172 ? 31.662 94.508 38.134 1.00 22.68 ? 172 TRP B CZ3 1 ATOM 3255 C CH2 . TRP B 2 172 ? 31.358 93.354 38.884 1.00 21.88 ? 172 TRP B CH2 1 ATOM 3256 N N . ALA B 2 173 ? 32.465 96.019 31.904 1.00 20.23 ? 173 ALA B N 1 ATOM 3257 C CA . ALA B 2 173 ? 32.911 96.906 30.845 1.00 20.77 ? 173 ALA B CA 1 ATOM 3258 C C . ALA B 2 173 ? 34.222 97.501 31.262 1.00 21.07 ? 173 ALA B C 1 ATOM 3259 O O . ALA B 2 173 ? 34.293 98.241 32.243 1.00 20.41 ? 173 ALA B O 1 ATOM 3260 C CB . ALA B 2 173 ? 31.881 97.998 30.568 1.00 20.59 ? 173 ALA B CB 1 ATOM 3261 N N . LEU B 2 174 ? 35.280 97.139 30.536 1.00 21.67 ? 174 LEU B N 1 ATOM 3262 C CA . LEU B 2 174 ? 36.617 97.641 30.798 1.00 21.69 ? 174 LEU B CA 1 ATOM 3263 C C . LEU B 2 174 ? 36.801 98.956 30.067 1.00 22.19 ? 174 LEU B C 1 ATOM 3264 O O . LEU B 2 174 ? 36.817 98.963 28.843 1.00 21.12 ? 174 LEU B O 1 ATOM 3265 C CB . LEU B 2 174 ? 37.663 96.598 30.336 1.00 22.67 ? 174 LEU B CB 1 ATOM 3266 C CG . LEU B 2 174 ? 37.538 95.172 30.882 1.00 22.87 ? 174 LEU B CG 1 ATOM 3267 C CD1 . LEU B 2 174 ? 38.786 94.370 30.550 1.00 22.53 ? 174 LEU B CD1 1 ATOM 3268 C CD2 . LEU B 2 174 ? 37.326 95.199 32.400 1.00 23.83 ? 174 LEU B CD2 1 ATOM 3269 N N . TYR B 2 175 ? 36.973 100.048 30.816 1.00 20.74 ? 175 TYR B N 1 ATOM 3270 C CA . TYR B 2 175 ? 37.028 101.407 30.268 1.00 21.39 ? 175 TYR B CA 1 ATOM 3271 C C . TYR B 2 175 ? 38.467 101.868 30.096 1.00 21.06 ? 175 TYR B C 1 ATOM 3272 O O . TYR B 2 175 ? 39.389 101.333 30.688 1.00 18.73 ? 175 TYR B O 1 ATOM 3273 C CB . TYR B 2 175 ? 36.298 102.419 31.193 1.00 21.44 ? 175 TYR B CB 1 ATOM 3274 C CG . TYR B 2 175 ? 34.850 102.616 30.888 1.00 22.11 ? 175 TYR B CG 1 ATOM 3275 C CD1 . TYR B 2 175 ? 33.963 101.573 31.002 1.00 22.71 ? 175 TYR B CD1 1 ATOM 3276 C CD2 . TYR B 2 175 ? 34.359 103.874 30.475 1.00 23.25 ? 175 TYR B CD2 1 ATOM 3277 C CE1 . TYR B 2 175 ? 32.633 101.745 30.710 1.00 24.22 ? 175 TYR B CE1 1 ATOM 3278 C CE2 . TYR B 2 175 ? 33.018 104.062 30.206 1.00 22.95 ? 175 TYR B CE2 1 ATOM 3279 C CZ . TYR B 2 175 ? 32.171 103.006 30.308 1.00 24.17 ? 175 TYR B CZ 1 ATOM 3280 O OH . TYR B 2 175 ? 30.841 103.150 30.028 1.00 25.58 ? 175 TYR B OH 1 ATOM 3281 N N . SER B 2 176 ? 38.619 102.932 29.329 1.00 19.00 ? 176 SER B N 1 ATOM 3282 C CA . SER B 2 176 ? 39.903 103.473 28.971 1.00 20.28 ? 176 SER B CA 1 ATOM 3283 C C . SER B 2 176 ? 40.652 104.091 30.146 1.00 20.59 ? 176 SER B C 1 ATOM 3284 O O . SER B 2 176 ? 41.853 104.261 30.082 1.00 21.71 ? 176 SER B O 1 ATOM 3285 C CB . SER B 2 176 ? 39.727 104.496 27.832 1.00 20.20 ? 176 SER B CB 1 ATOM 3286 O OG . SER B 2 176 ? 39.139 103.883 26.678 1.00 20.35 ? 176 SER B OG 1 ATOM 3287 N N . ASP B 2 177 ? 39.936 104.411 31.218 1.00 20.69 ? 177 ASP B N 1 ATOM 3288 C CA . ASP B 2 177 ? 40.567 104.906 32.467 1.00 21.57 ? 177 ASP B CA 1 ATOM 3289 C C . ASP B 2 177 ? 40.933 103.788 33.459 1.00 20.93 ? 177 ASP B C 1 ATOM 3290 O O . ASP B 2 177 ? 41.061 104.039 34.646 1.00 21.36 ? 177 ASP B O 1 ATOM 3291 C CB . ASP B 2 177 ? 39.648 105.924 33.142 1.00 21.03 ? 177 ASP B CB 1 ATOM 3292 C CG . ASP B 2 177 ? 38.263 105.369 33.413 1.00 21.57 ? 177 ASP B CG 1 ATOM 3293 O OD1 . ASP B 2 177 ? 38.042 104.149 33.219 1.00 21.61 ? 177 ASP B OD1 1 ATOM 3294 O OD2 . ASP B 2 177 ? 37.374 106.160 33.799 1.00 22.85 ? 177 ASP B OD2 1 ATOM 3295 N N . ASP B 2 178 ? 41.054 102.559 32.972 1.00 21.32 ? 178 ASP B N 1 ATOM 3296 C CA . ASP B 2 178 ? 41.368 101.389 33.799 1.00 22.98 ? 178 ASP B CA 1 ATOM 3297 C C . ASP B 2 178 ? 40.300 101.017 34.841 1.00 23.84 ? 178 ASP B C 1 ATOM 3298 O O . ASP B 2 178 ? 40.582 100.231 35.753 1.00 22.82 ? 178 ASP B O 1 ATOM 3299 C CB . ASP B 2 178 ? 42.743 101.537 34.477 1.00 22.62 ? 178 ASP B CB 1 ATOM 3300 C CG . ASP B 2 178 ? 43.895 101.403 33.521 1.00 23.22 ? 178 ASP B CG 1 ATOM 3301 O OD1 . ASP B 2 178 ? 43.684 100.954 32.378 1.00 24.44 ? 178 ASP B OD1 1 ATOM 3302 O OD2 . ASP B 2 178 ? 45.043 101.744 33.924 1.00 24.17 ? 178 ASP B OD2 1 ATOM 3303 N N . THR B 2 179 ? 39.068 101.518 34.669 1.00 22.54 ? 179 THR B N 1 ATOM 3304 C CA . THR B 2 179 ? 37.974 101.141 35.545 1.00 21.39 ? 179 THR B CA 1 ATOM 3305 C C . THR B 2 179 ? 37.333 99.868 35.032 1.00 21.08 ? 179 THR B C 1 ATOM 3306 O O . THR B 2 179 ? 37.405 99.550 33.822 1.00 22.15 ? 179 THR B O 1 ATOM 3307 C CB . THR B 2 179 ? 36.924 102.272 35.730 1.00 22.41 ? 179 THR B CB 1 ATOM 3308 O OG1 . THR B 2 179 ? 36.352 102.667 34.469 1.00 21.21 ? 179 THR B OG1 1 ATOM 3309 C CG2 . THR B 2 179 ? 37.549 103.478 36.408 1.00 22.27 ? 179 THR B CG2 1 ATOM 3310 N N . ILE B 2 180 ? 36.762 99.109 35.956 1.00 19.54 ? 180 ILE B N 1 ATOM 3311 C CA . ILE B 2 180 ? 36.043 97.889 35.655 1.00 21.05 ? 180 ILE B CA 1 ATOM 3312 C C . ILE B 2 180 ? 34.613 98.144 36.064 1.00 20.73 ? 180 ILE B C 1 ATOM 3313 O O . ILE B 2 180 ? 34.321 98.199 37.266 1.00 19.91 ? 180 ILE B O 1 ATOM 3314 C CB . ILE B 2 180 ? 36.576 96.670 36.452 1.00 20.67 ? 180 ILE B CB 1 ATOM 3315 C CG1 . ILE B 2 180 ? 38.063 96.467 36.167 1.00 21.26 ? 180 ILE B CG1 1 ATOM 3316 C CG2 . ILE B 2 180 ? 35.774 95.405 36.131 1.00 20.37 ? 180 ILE B CG2 1 ATOM 3317 C CD1 . ILE B 2 180 ? 38.700 95.458 37.107 1.00 22.06 ? 180 ILE B CD1 1 ATOM 3318 N N . ARG B 2 181 ? 33.723 98.266 35.081 1.00 20.90 ? 181 ARG B N 1 ATOM 3319 C CA . ARG B 2 181 ? 32.374 98.807 35.335 1.00 20.82 ? 181 ARG B CA 1 ATOM 3320 C C . ARG B 2 181 ? 31.324 97.750 35.193 1.00 20.77 ? 181 ARG B C 1 ATOM 3321 O O . ARG B 2 181 ? 31.461 96.816 34.387 1.00 20.81 ? 181 ARG B O 1 ATOM 3322 C CB . ARG B 2 181 ? 32.082 100.003 34.435 1.00 21.13 ? 181 ARG B CB 1 ATOM 3323 C CG . ARG B 2 181 ? 33.153 101.061 34.509 1.00 21.18 ? 181 ARG B CG 1 ATOM 3324 C CD . ARG B 2 181 ? 32.633 102.458 34.288 1.00 21.18 ? 181 ARG B CD 1 ATOM 3325 N NE . ARG B 2 181 ? 33.698 103.459 34.277 1.00 22.08 ? 181 ARG B NE 1 ATOM 3326 C CZ . ARG B 2 181 ? 33.513 104.777 34.228 1.00 23.73 ? 181 ARG B CZ 1 ATOM 3327 N NH1 . ARG B 2 181 ? 32.279 105.290 34.164 1.00 26.22 ? 181 ARG B NH1 1 ATOM 3328 N NH2 . ARG B 2 181 ? 34.551 105.594 34.231 1.00 23.72 ? 181 ARG B NH2 1 ATOM 3329 N N . VAL B 2 182 ? 30.259 97.877 35.986 1.00 21.67 ? 182 VAL B N 1 ATOM 3330 C CA . VAL B 2 182 ? 29.120 96.969 35.885 1.00 22.07 ? 182 VAL B CA 1 ATOM 3331 C C . VAL B 2 182 ? 28.562 97.187 34.467 1.00 23.10 ? 182 VAL B C 1 ATOM 3332 O O . VAL B 2 182 ? 28.298 98.327 34.073 1.00 21.73 ? 182 VAL B O 1 ATOM 3333 C CB . VAL B 2 182 ? 28.053 97.269 36.958 1.00 23.53 ? 182 VAL B CB 1 ATOM 3334 C CG1 . VAL B 2 182 ? 26.809 96.410 36.752 1.00 23.38 ? 182 VAL B CG1 1 ATOM 3335 C CG2 . VAL B 2 182 ? 28.632 97.029 38.356 1.00 23.73 ? 182 VAL B CG2 1 ATOM 3336 N N . ASN B 2 183 ? 28.444 96.115 33.693 1.00 23.47 ? 183 ASN B N 1 ATOM 3337 C CA . ASN B 2 183 ? 28.175 96.293 32.277 1.00 24.69 ? 183 ASN B CA 1 ATOM 3338 C C . ASN B 2 183 ? 26.818 96.982 32.006 1.00 26.54 ? 183 ASN B C 1 ATOM 3339 O O . ASN B 2 183 ? 26.724 97.855 31.147 1.00 25.97 ? 183 ASN B O 1 ATOM 3340 C CB . ASN B 2 183 ? 28.273 94.997 31.506 1.00 25.55 ? 183 ASN B CB 1 ATOM 3341 C CG . ASN B 2 183 ? 28.186 95.227 30.015 1.00 25.05 ? 183 ASN B CG 1 ATOM 3342 O OD1 . ASN B 2 183 ? 28.863 96.109 29.473 1.00 25.29 ? 183 ASN B OD1 1 ATOM 3343 N ND2 . ASN B 2 183 ? 27.341 94.466 29.352 1.00 25.03 ? 183 ASN B ND2 1 ATOM 3344 N N . ASN B 2 184 ? 25.790 96.616 32.757 1.00 27.83 ? 184 ASN B N 1 ATOM 3345 C CA . ASN B 2 184 ? 24.490 97.300 32.592 1.00 30.52 ? 184 ASN B CA 1 ATOM 3346 C C . ASN B 2 184 ? 24.229 98.448 33.568 1.00 29.36 ? 184 ASN B C 1 ATOM 3347 O O . ASN B 2 184 ? 23.109 98.935 33.674 1.00 31.47 ? 184 ASN B O 1 ATOM 3348 C CB . ASN B 2 184 ? 23.368 96.275 32.582 1.00 32.78 ? 184 ASN B CB 1 ATOM 3349 C CG . ASN B 2 184 ? 23.000 95.786 33.960 1.00 35.59 ? 184 ASN B CG 1 ATOM 3350 O OD1 . ASN B 2 184 ? 23.743 95.940 34.932 1.00 39.33 ? 184 ASN B OD1 1 ATOM 3351 N ND2 . ASN B 2 184 ? 21.828 95.183 34.055 1.00 38.37 ? 184 ASN B ND2 1 ATOM 3352 N N . ASN B 2 185 ? 25.254 98.882 34.283 1.00 26.55 ? 185 ASN B N 1 ATOM 3353 C CA . ASN B 2 185 ? 25.217 100.149 34.971 1.00 27.41 ? 185 ASN B CA 1 ATOM 3354 C C . ASN B 2 185 ? 26.591 100.745 35.025 1.00 26.97 ? 185 ASN B C 1 ATOM 3355 O O . ASN B 2 185 ? 27.348 100.574 36.017 1.00 25.55 ? 185 ASN B O 1 ATOM 3356 C CB . ASN B 2 185 ? 24.652 100.033 36.385 1.00 28.24 ? 185 ASN B CB 1 ATOM 3357 C CG . ASN B 2 185 ? 24.394 101.391 37.003 1.00 28.83 ? 185 ASN B CG 1 ATOM 3358 O OD1 . ASN B 2 185 ? 24.899 102.427 36.538 1.00 28.96 ? 185 ASN B OD1 1 ATOM 3359 N ND2 . ASN B 2 185 ? 23.637 101.397 38.077 1.00 30.95 ? 185 ASN B ND2 1 ATOM 3360 N N . ARG B 2 186 ? 26.896 101.503 33.984 1.00 24.92 ? 186 ARG B N 1 ATOM 3361 C CA . ARG B 2 186 ? 28.247 102.009 33.759 1.00 26.05 ? 186 ARG B CA 1 ATOM 3362 C C . ARG B 2 186 ? 28.664 103.238 34.553 1.00 25.29 ? 186 ARG B C 1 ATOM 3363 O O . ARG B 2 186 ? 29.761 103.764 34.376 1.00 24.78 ? 186 ARG B O 1 ATOM 3364 C CB . ARG B 2 186 ? 28.447 102.160 32.247 1.00 28.06 ? 186 ARG B CB 1 ATOM 3365 C CG . ARG B 2 186 ? 28.408 100.778 31.609 1.00 28.80 ? 186 ARG B CG 1 ATOM 3366 C CD . ARG B 2 186 ? 28.763 100.792 30.162 1.00 32.43 ? 186 ARG B CD 1 ATOM 3367 N NE . ARG B 2 186 ? 28.641 99.481 29.541 1.00 31.30 ? 186 ARG B NE 1 ATOM 3368 C CZ . ARG B 2 186 ? 28.945 99.259 28.271 1.00 32.46 ? 186 ARG B CZ 1 ATOM 3369 N NH1 . ARG B 2 186 ? 29.374 100.259 27.512 1.00 35.74 ? 186 ARG B NH1 1 ATOM 3370 N NH2 . ARG B 2 186 ? 28.807 98.051 27.742 1.00 31.99 ? 186 ARG B NH2 1 ATOM 3371 N N . ASN B 2 187 ? 27.797 103.684 35.456 1.00 25.96 ? 187 ASN B N 1 ATOM 3372 C CA . ASN B 2 187 ? 28.170 104.617 36.502 1.00 28.29 ? 187 ASN B CA 1 ATOM 3373 C C . ASN B 2 187 ? 28.794 103.958 37.729 1.00 26.11 ? 187 ASN B C 1 ATOM 3374 O O . ASN B 2 187 ? 29.217 104.672 38.618 1.00 26.52 ? 187 ASN B O 1 ATOM 3375 C CB . ASN B 2 187 ? 26.947 105.402 36.986 1.00 31.48 ? 187 ASN B CB 1 ATOM 3376 C CG . ASN B 2 187 ? 26.345 106.259 35.909 1.00 36.10 ? 187 ASN B CG 1 ATOM 3377 O OD1 . ASN B 2 187 ? 25.138 106.171 35.655 1.00 43.35 ? 187 ASN B OD1 1 ATOM 3378 N ND2 . ASN B 2 187 ? 27.168 107.070 35.249 1.00 36.72 ? 187 ASN B ND2 1 ATOM 3379 N N . LEU B 2 188 ? 28.809 102.624 37.774 1.00 25.54 ? 188 LEU B N 1 ATOM 3380 C CA . LEU B 2 188 ? 29.316 101.843 38.916 1.00 24.80 ? 188 LEU B CA 1 ATOM 3381 C C . LEU B 2 188 ? 30.594 101.078 38.545 1.00 25.12 ? 188 LEU B C 1 ATOM 3382 O O . LEU B 2 188 ? 30.667 100.475 37.469 1.00 21.99 ? 188 LEU B O 1 ATOM 3383 C CB . LEU B 2 188 ? 28.258 100.855 39.382 1.00 25.30 ? 188 LEU B CB 1 ATOM 3384 C CG . LEU B 2 188 ? 26.911 101.463 39.808 1.00 26.53 ? 188 LEU B CG 1 ATOM 3385 C CD1 . LEU B 2 188 ? 25.991 100.387 40.350 1.00 27.23 ? 188 LEU B CD1 1 ATOM 3386 C CD2 . LEU B 2 188 ? 27.077 102.555 40.855 1.00 27.17 ? 188 LEU B CD2 1 ATOM 3387 N N . CYS B 2 189 ? 31.570 101.131 39.458 1.00 24.77 ? 189 CYS B N 1 ATOM 3388 C CA . CYS B 2 189 ? 32.960 100.711 39.237 1.00 26.78 ? 189 CYS B CA 1 ATOM 3389 C C . CYS B 2 189 ? 33.371 99.763 40.375 1.00 25.45 ? 189 CYS B C 1 ATOM 3390 O O . CYS B 2 189 ? 33.043 100.011 41.542 1.00 22.57 ? 189 CYS B O 1 ATOM 3391 C CB . CYS B 2 189 ? 33.869 101.970 39.284 1.00 27.38 ? 189 CYS B CB 1 ATOM 3392 S SG . CYS B 2 189 ? 33.938 102.961 37.753 1.00 37.39 ? 189 CYS B SG 1 ATOM 3393 N N . VAL B 2 190 ? 34.106 98.706 40.049 1.00 23.75 ? 190 VAL B N 1 ATOM 3394 C CA . VAL B 2 190 ? 34.785 97.896 41.076 1.00 21.76 ? 190 VAL B CA 1 ATOM 3395 C C . VAL B 2 190 ? 35.798 98.769 41.841 1.00 20.47 ? 190 VAL B C 1 ATOM 3396 O O . VAL B 2 190 ? 36.630 99.470 41.251 1.00 19.88 ? 190 VAL B O 1 ATOM 3397 C CB . VAL B 2 190 ? 35.500 96.682 40.461 1.00 20.55 ? 190 VAL B CB 1 ATOM 3398 C CG1 . VAL B 2 190 ? 36.261 95.902 41.531 1.00 20.59 ? 190 VAL B CG1 1 ATOM 3399 C CG2 . VAL B 2 190 ? 34.497 95.755 39.795 1.00 20.71 ? 190 VAL B CG2 1 ATOM 3400 N N . SER B 2 191 ? 35.718 98.723 43.163 1.00 21.21 ? 191 SER B N 1 ATOM 3401 C CA . SER B 2 191 ? 36.485 99.630 44.019 1.00 22.93 ? 191 SER B CA 1 ATOM 3402 C C . SER B 2 191 ? 37.140 98.879 45.183 1.00 22.60 ? 191 SER B C 1 ATOM 3403 O O . SER B 2 191 ? 36.505 98.047 45.824 1.00 22.83 ? 191 SER B O 1 ATOM 3404 C CB . SER B 2 191 ? 35.580 100.729 44.596 1.00 24.00 ? 191 SER B CB 1 ATOM 3405 O OG . SER B 2 191 ? 36.335 101.507 45.516 1.00 25.57 ? 191 SER B OG 1 ATOM 3406 N N . SER B 2 192 ? 38.399 99.202 45.446 1.00 21.93 ? 192 SER B N 1 ATOM 3407 C CA . SER B 2 192 ? 39.066 98.742 46.654 1.00 22.67 ? 192 SER B CA 1 ATOM 3408 C C . SER B 2 192 ? 38.425 99.506 47.827 1.00 22.71 ? 192 SER B C 1 ATOM 3409 O O . SER B 2 192 ? 37.817 100.566 47.645 1.00 21.28 ? 192 SER B O 1 ATOM 3410 C CB . SER B 2 192 ? 40.556 99.001 46.585 1.00 22.23 ? 192 SER B CB 1 ATOM 3411 O OG . SER B 2 192 ? 40.887 100.369 46.717 1.00 22.18 ? 192 SER B OG 1 ATOM 3412 N N . SER B 2 193 ? 38.517 98.924 49.012 1.00 22.36 ? 193 SER B N 1 ATOM 3413 C CA . SER B 2 193 ? 37.882 99.490 50.202 1.00 22.11 ? 193 SER B CA 1 ATOM 3414 C C . SER B 2 193 ? 38.223 100.950 50.467 1.00 20.30 ? 193 SER B C 1 ATOM 3415 O O . SER B 2 193 ? 39.368 101.378 50.314 1.00 20.69 ? 193 SER B O 1 ATOM 3416 C CB . SER B 2 193 ? 38.280 98.668 51.439 1.00 23.06 ? 193 SER B CB 1 ATOM 3417 O OG . SER B 2 193 ? 37.688 99.249 52.594 1.00 22.75 ? 193 SER B OG 1 ATOM 3418 N N . THR B 2 194 ? 37.210 101.718 50.855 1.00 21.35 ? 194 THR B N 1 ATOM 3419 C CA . THR B 2 194 ? 37.398 103.098 51.340 1.00 23.62 ? 194 THR B CA 1 ATOM 3420 C C . THR B 2 194 ? 37.438 103.165 52.874 1.00 25.69 ? 194 THR B C 1 ATOM 3421 O O . THR B 2 194 ? 37.601 104.240 53.445 1.00 27.12 ? 194 THR B O 1 ATOM 3422 C CB . THR B 2 194 ? 36.280 104.042 50.833 1.00 23.29 ? 194 THR B CB 1 ATOM 3423 O OG1 . THR B 2 194 ? 35.004 103.513 51.197 1.00 22.07 ? 194 THR B OG1 1 ATOM 3424 C CG2 . THR B 2 194 ? 36.357 104.154 49.307 1.00 24.51 ? 194 THR B CG2 1 ATOM 3425 N N . ASP B 2 195 ? 37.286 102.007 53.515 1.00 26.92 ? 195 ASP B N 1 ATOM 3426 C CA . ASP B 2 195 ? 37.331 101.846 54.976 1.00 28.16 ? 195 ASP B CA 1 ATOM 3427 C C . ASP B 2 195 ? 38.598 101.060 55.301 1.00 27.14 ? 195 ASP B C 1 ATOM 3428 O O . ASP B 2 195 ? 38.730 99.902 54.956 1.00 24.97 ? 195 ASP B O 1 ATOM 3429 C CB . ASP B 2 195 ? 36.080 101.113 55.451 1.00 29.37 ? 195 ASP B CB 1 ATOM 3430 C CG . ASP B 2 195 ? 36.094 100.799 56.961 1.00 33.65 ? 195 ASP B CG 1 ATOM 3431 O OD1 . ASP B 2 195 ? 37.035 101.199 57.685 1.00 34.02 ? 195 ASP B OD1 1 ATOM 3432 O OD2 . ASP B 2 195 ? 35.151 100.117 57.405 1.00 36.51 ? 195 ASP B OD2 1 ATOM 3433 N N . SER B 2 196 ? 39.546 101.781 55.874 1.00 26.44 ? 196 SER B N 1 ATOM 3434 C CA . SER B 2 196 ? 40.763 101.322 56.496 1.00 27.31 ? 196 SER B CA 1 ATOM 3435 C C . SER B 2 196 ? 40.686 99.961 57.194 1.00 25.04 ? 196 SER B C 1 ATOM 3436 O O . SER B 2 196 ? 41.613 99.152 57.088 1.00 25.84 ? 196 SER B O 1 ATOM 3437 C CB . SER B 2 196 ? 41.079 102.427 57.525 1.00 30.82 ? 196 SER B CB 1 ATOM 3438 O OG . SER B 2 196 ? 42.063 102.123 58.447 1.00 33.14 ? 196 SER B OG 1 ATOM 3439 N N . SER B 2 197 ? 39.587 99.724 57.898 1.00 21.69 ? 197 SER B N 1 ATOM 3440 C CA . SER B 2 197 ? 39.355 98.479 58.616 1.00 21.87 ? 197 SER B CA 1 ATOM 3441 C C . SER B 2 197 ? 39.086 97.255 57.751 1.00 22.19 ? 197 SER B C 1 ATOM 3442 O O . SER B 2 197 ? 39.187 96.127 58.250 1.00 20.38 ? 197 SER B O 1 ATOM 3443 C CB . SER B 2 197 ? 38.197 98.634 59.614 1.00 21.06 ? 197 SER B CB 1 ATOM 3444 O OG . SER B 2 197 ? 38.655 99.324 60.755 1.00 21.29 ? 197 SER B OG 1 ATOM 3445 N N . SER B 2 198 ? 38.695 97.482 56.488 1.00 20.74 ? 198 SER B N 1 ATOM 3446 C CA . SER B 2 198 ? 38.314 96.411 55.584 1.00 21.17 ? 198 SER B CA 1 ATOM 3447 C C . SER B 2 198 ? 39.219 96.360 54.338 1.00 20.33 ? 198 SER B C 1 ATOM 3448 O O . SER B 2 198 ? 39.572 97.382 53.756 1.00 19.29 ? 198 SER B O 1 ATOM 3449 C CB . SER B 2 198 ? 36.873 96.636 55.127 1.00 21.66 ? 198 SER B CB 1 ATOM 3450 O OG . SER B 2 198 ? 36.480 95.598 54.254 1.00 21.33 ? 198 SER B OG 1 ATOM 3451 N N . LYS B 2 199 ? 39.592 95.154 53.941 1.00 20.96 ? 199 LYS B N 1 ATOM 3452 C CA . LYS B 2 199 ? 40.278 94.947 52.658 1.00 21.18 ? 199 LYS B CA 1 ATOM 3453 C C . LYS B 2 199 ? 39.312 94.553 51.536 1.00 21.21 ? 199 LYS B C 1 ATOM 3454 O O . LYS B 2 199 ? 39.753 94.212 50.419 1.00 19.79 ? 199 LYS B O 1 ATOM 3455 C CB . LYS B 2 199 ? 41.311 93.824 52.790 1.00 22.06 ? 199 LYS B CB 1 ATOM 3456 C CG . LYS B 2 199 ? 42.297 94.002 53.921 1.00 22.38 ? 199 LYS B CG 1 ATOM 3457 C CD . LYS B 2 199 ? 43.173 95.205 53.692 1.00 23.10 ? 199 LYS B CD 1 ATOM 3458 C CE . LYS B 2 199 ? 44.179 95.293 54.818 1.00 23.50 ? 199 LYS B CE 1 ATOM 3459 N NZ . LYS B 2 199 ? 44.962 96.549 54.753 1.00 23.87 ? 199 LYS B NZ 1 ATOM 3460 N N . LEU B 2 200 ? 38.018 94.561 51.826 1.00 20.40 ? 200 LEU B N 1 ATOM 3461 C CA . LEU B 2 200 ? 37.024 94.043 50.916 1.00 21.07 ? 200 LEU B CA 1 ATOM 3462 C C . LEU B 2 200 ? 36.821 94.923 49.668 1.00 20.59 ? 200 LEU B C 1 ATOM 3463 O O . LEU B 2 200 ? 36.640 96.111 49.769 1.00 19.97 ? 200 LEU B O 1 ATOM 3464 C CB . LEU B 2 200 ? 35.713 93.853 51.643 1.00 21.27 ? 200 LEU B CB 1 ATOM 3465 C CG . LEU B 2 200 ? 34.616 93.098 50.900 1.00 21.87 ? 200 LEU B CG 1 ATOM 3466 C CD1 . LEU B 2 200 ? 34.941 91.627 50.843 1.00 22.56 ? 200 LEU B CD1 1 ATOM 3467 C CD2 . LEU B 2 200 ? 33.273 93.328 51.582 1.00 23.68 ? 200 LEU B CD2 1 ATOM 3468 N N . ILE B 2 201 ? 36.886 94.291 48.504 1.00 20.61 ? 201 ILE B N 1 ATOM 3469 C CA . ILE B 2 201 ? 36.617 94.949 47.226 1.00 20.71 ? 201 ILE B CA 1 ATOM 3470 C C . ILE B 2 201 ? 35.118 94.959 47.028 1.00 19.43 ? 201 ILE B C 1 ATOM 3471 O O . ILE B 2 201 ? 34.459 93.959 47.294 1.00 20.56 ? 201 ILE B O 1 ATOM 3472 C CB . ILE B 2 201 ? 37.370 94.255 46.078 1.00 22.01 ? 201 ILE B CB 1 ATOM 3473 C CG1 . ILE B 2 201 ? 38.873 94.543 46.284 1.00 22.96 ? 201 ILE B CG1 1 ATOM 3474 C CG2 . ILE B 2 201 ? 36.942 94.791 44.716 1.00 21.28 ? 201 ILE B CG2 1 ATOM 3475 C CD1 . ILE B 2 201 ? 39.767 93.640 45.488 1.00 24.47 ? 201 ILE B CD1 1 ATOM 3476 N N . VAL B 2 202 ? 34.608 96.115 46.597 1.00 19.66 ? 202 VAL B N 1 ATOM 3477 C CA . VAL B 2 202 ? 33.176 96.392 46.510 1.00 20.07 ? 202 VAL B CA 1 ATOM 3478 C C . VAL B 2 202 ? 32.861 97.088 45.168 1.00 21.31 ? 202 VAL B C 1 ATOM 3479 O O . VAL B 2 202 ? 33.727 97.196 44.303 1.00 20.61 ? 202 VAL B O 1 ATOM 3480 C CB . VAL B 2 202 ? 32.704 97.240 47.733 1.00 20.86 ? 202 VAL B CB 1 ATOM 3481 C CG1 . VAL B 2 202 ? 32.810 96.431 49.020 1.00 20.49 ? 202 VAL B CG1 1 ATOM 3482 C CG2 . VAL B 2 202 ? 33.517 98.518 47.855 1.00 20.81 ? 202 VAL B CG2 1 ATOM 3483 N N . ILE B 2 203 ? 31.602 97.506 44.987 1.00 22.73 ? 203 ILE B N 1 ATOM 3484 C CA . ILE B 2 203 ? 31.180 98.279 43.807 1.00 22.44 ? 203 ILE B CA 1 ATOM 3485 C C . ILE B 2 203 ? 30.642 99.618 44.276 1.00 23.16 ? 203 ILE B C 1 ATOM 3486 O O . ILE B 2 203 ? 29.772 99.653 45.141 1.00 22.92 ? 203 ILE B O 1 ATOM 3487 C CB . ILE B 2 203 ? 30.094 97.548 43.014 1.00 22.43 ? 203 ILE B CB 1 ATOM 3488 C CG1 . ILE B 2 203 ? 30.666 96.236 42.511 1.00 24.65 ? 203 ILE B CG1 1 ATOM 3489 C CG2 . ILE B 2 203 ? 29.619 98.433 41.858 1.00 23.16 ? 203 ILE B CG2 1 ATOM 3490 C CD1 . ILE B 2 203 ? 29.670 95.363 41.778 1.00 26.43 ? 203 ILE B CD1 1 ATOM 3491 N N . ARG B 2 204 ? 31.181 100.704 43.730 1.00 22.33 ? 204 ARG B N 1 ATOM 3492 C CA . ARG B 2 204 ? 30.780 102.037 44.119 1.00 23.95 ? 204 ARG B CA 1 ATOM 3493 C C . ARG B 2 204 ? 30.634 102.916 42.869 1.00 25.68 ? 204 ARG B C 1 ATOM 3494 O O . ARG B 2 204 ? 31.139 102.595 41.768 1.00 23.65 ? 204 ARG B O 1 ATOM 3495 C CB . ARG B 2 204 ? 31.811 102.660 45.079 1.00 24.42 ? 204 ARG B CB 1 ATOM 3496 C CG . ARG B 2 204 ? 32.029 101.888 46.391 1.00 24.28 ? 204 ARG B CG 1 ATOM 3497 C CD . ARG B 2 204 ? 30.827 102.086 47.332 1.00 25.34 ? 204 ARG B CD 1 ATOM 3498 N NE . ARG B 2 204 ? 30.897 101.353 48.610 1.00 25.81 ? 204 ARG B NE 1 ATOM 3499 C CZ . ARG B 2 204 ? 30.353 100.154 48.873 1.00 26.99 ? 204 ARG B CZ 1 ATOM 3500 N NH1 . ARG B 2 204 ? 29.697 99.446 47.957 1.00 25.48 ? 204 ARG B NH1 1 ATOM 3501 N NH2 . ARG B 2 204 ? 30.488 99.621 50.104 1.00 30.34 ? 204 ARG B NH2 1 ATOM 3502 N N . ARG B 2 205 ? 29.986 104.055 43.071 1.00 25.85 ? 205 ARG B N 1 ATOM 3503 C CA . ARG B 2 205 ? 29.868 105.065 42.044 1.00 28.55 ? 205 ARG B CA 1 ATOM 3504 C C . ARG B 2 205 ? 31.256 105.488 41.557 1.00 26.97 ? 205 ARG B C 1 ATOM 3505 O O . ARG B 2 205 ? 32.161 105.730 42.360 1.00 22.68 ? 205 ARG B O 1 ATOM 3506 C CB . ARG B 2 205 ? 29.108 106.279 42.595 1.00 32.51 ? 205 ARG B CB 1 ATOM 3507 C CG . ARG B 2 205 ? 29.050 107.476 41.655 1.00 39.89 ? 205 ARG B CG 1 ATOM 3508 C CD . ARG B 2 205 ? 28.205 107.206 40.413 1.00 45.44 ? 205 ARG B CD 1 ATOM 3509 N NE . ARG B 2 205 ? 28.109 108.413 39.569 1.00 54.38 ? 205 ARG B NE 1 ATOM 3510 C CZ . ARG B 2 205 ? 28.809 108.674 38.452 1.00 58.26 ? 205 ARG B CZ 1 ATOM 3511 N NH1 . ARG B 2 205 ? 29.688 107.811 37.935 1.00 59.52 ? 205 ARG B NH1 1 ATOM 3512 N NH2 . ARG B 2 205 ? 28.614 109.835 37.820 1.00 61.11 ? 205 ARG B NH2 1 ATOM 3513 N N . CYS B 2 206 ? 31.420 105.562 40.234 1.00 26.74 ? 206 CYS B N 1 ATOM 3514 C CA . CYS B 2 206 ? 32.717 105.913 39.648 1.00 27.84 ? 206 CYS B CA 1 ATOM 3515 C C . CYS B 2 206 ? 33.114 107.311 40.059 1.00 26.49 ? 206 CYS B C 1 ATOM 3516 O O . CYS B 2 206 ? 32.298 108.216 40.026 1.00 26.53 ? 206 CYS B O 1 ATOM 3517 C CB . CYS B 2 206 ? 32.705 105.774 38.112 1.00 31.96 ? 206 CYS B CB 1 ATOM 3518 S SG . CYS B 2 206 ? 32.261 104.099 37.546 1.00 35.72 ? 206 CYS B SG 1 ATOM 3519 N N . ASP B 2 207 ? 34.358 107.483 40.484 1.00 25.18 ? 207 ASP B N 1 ATOM 3520 C CA . ASP B 2 207 ? 34.803 108.759 41.036 1.00 24.83 ? 207 ASP B CA 1 ATOM 3521 C C . ASP B 2 207 ? 36.214 109.170 40.676 1.00 23.61 ? 207 ASP B C 1 ATOM 3522 O O . ASP B 2 207 ? 36.735 110.134 41.216 1.00 23.23 ? 207 ASP B O 1 ATOM 3523 C CB . ASP B 2 207 ? 34.628 108.729 42.566 1.00 26.45 ? 207 ASP B CB 1 ATOM 3524 C CG . ASP B 2 207 ? 35.610 107.791 43.265 1.00 27.89 ? 207 ASP B CG 1 ATOM 3525 O OD1 . ASP B 2 207 ? 36.445 107.116 42.605 1.00 28.04 ? 207 ASP B OD1 1 ATOM 3526 O OD2 . ASP B 2 207 ? 35.536 107.742 44.509 1.00 29.18 ? 207 ASP B OD2 1 ATOM 3527 N N . GLY B 2 208 ? 36.835 108.457 39.741 1.00 23.62 ? 208 GLY B N 1 ATOM 3528 C CA . GLY B 2 208 ? 38.183 108.774 39.312 1.00 23.40 ? 208 GLY B CA 1 ATOM 3529 C C . GLY B 2 208 ? 39.313 108.413 40.264 1.00 23.29 ? 208 GLY B C 1 ATOM 3530 O O . GLY B 2 208 ? 40.452 108.764 39.982 1.00 23.58 ? 208 GLY B O 1 ATOM 3531 N N . SER B 2 209 ? 39.007 107.716 41.362 1.00 22.75 ? 209 SER B N 1 ATOM 3532 C CA . SER B 2 209 ? 39.965 107.539 42.457 1.00 23.62 ? 209 SER B CA 1 ATOM 3533 C C . SER B 2 209 ? 40.992 106.433 42.178 1.00 24.22 ? 209 SER B C 1 ATOM 3534 O O . SER B 2 209 ? 40.823 105.607 41.274 1.00 23.43 ? 209 SER B O 1 ATOM 3535 C CB . SER B 2 209 ? 39.249 107.181 43.763 1.00 23.29 ? 209 SER B CB 1 ATOM 3536 O OG . SER B 2 209 ? 38.564 105.942 43.692 1.00 21.39 ? 209 SER B OG 1 ATOM 3537 N N . ILE B 2 210 ? 42.032 106.432 43.003 1.00 24.08 ? 210 ILE B N 1 ATOM 3538 C CA . ILE B 2 210 ? 43.022 105.332 43.093 1.00 25.18 ? 210 ILE B CA 1 ATOM 3539 C C . ILE B 2 210 ? 42.335 103.986 43.303 1.00 23.57 ? 210 ILE B C 1 ATOM 3540 O O . ILE B 2 210 ? 42.735 102.992 42.691 1.00 23.18 ? 210 ILE B O 1 ATOM 3541 C CB . ILE B 2 210 ? 44.025 105.562 44.246 1.00 27.19 ? 210 ILE B CB 1 ATOM 3542 C CG1 . ILE B 2 210 ? 44.782 106.872 44.045 1.00 28.07 ? 210 ILE B CG1 1 ATOM 3543 C CG2 . ILE B 2 210 ? 45.031 104.403 44.359 1.00 27.56 ? 210 ILE B CG2 1 ATOM 3544 C CD1 . ILE B 2 210 ? 45.349 107.448 45.324 1.00 29.82 ? 210 ILE B CD1 1 ATOM 3545 N N . ASN B 2 211 ? 41.272 103.982 44.108 1.00 22.21 ? 211 ASN B N 1 ATOM 3546 C CA . ASN B 2 211 ? 40.553 102.759 44.479 1.00 23.81 ? 211 ASN B CA 1 ATOM 3547 C C . ASN B 2 211 ? 39.931 102.018 43.288 1.00 22.37 ? 211 ASN B C 1 ATOM 3548 O O . ASN B 2 211 ? 39.680 100.828 43.378 1.00 20.79 ? 211 ASN B O 1 ATOM 3549 C CB . ASN B 2 211 ? 39.431 103.027 45.505 1.00 24.76 ? 211 ASN B CB 1 ATOM 3550 C CG . ASN B 2 211 ? 39.925 103.762 46.747 1.00 25.56 ? 211 ASN B CG 1 ATOM 3551 O OD1 . ASN B 2 211 ? 40.476 104.855 46.639 1.00 26.58 ? 211 ASN B OD1 1 ATOM 3552 N ND2 . ASN B 2 211 ? 39.761 103.150 47.919 1.00 25.17 ? 211 ASN B ND2 1 ATOM 3553 N N . GLN B 2 212 ? 39.690 102.748 42.194 1.00 22.11 ? 212 GLN B N 1 ATOM 3554 C CA . GLN B 2 212 ? 38.942 102.239 41.052 1.00 21.60 ? 212 GLN B CA 1 ATOM 3555 C C . GLN B 2 212 ? 39.799 101.982 39.819 1.00 21.85 ? 212 GLN B C 1 ATOM 3556 O O . GLN B 2 212 ? 39.270 101.648 38.761 1.00 21.52 ? 212 GLN B O 1 ATOM 3557 C CB . GLN B 2 212 ? 37.779 103.204 40.737 1.00 21.34 ? 212 GLN B CB 1 ATOM 3558 C CG . GLN B 2 212 ? 36.731 103.165 41.841 1.00 21.73 ? 212 GLN B CG 1 ATOM 3559 C CD . GLN B 2 212 ? 35.635 104.202 41.678 1.00 23.23 ? 212 GLN B CD 1 ATOM 3560 O OE1 . GLN B 2 212 ? 35.631 104.980 40.709 1.00 22.62 ? 212 GLN B OE1 1 ATOM 3561 N NE2 . GLN B 2 212 ? 34.694 104.221 42.621 1.00 22.38 ? 212 GLN B NE2 1 ATOM 3562 N N . ARG B 2 213 ? 41.117 102.119 39.968 1.00 22.50 ? 213 ARG B N 1 ATOM 3563 C CA . ARG B 2 213 ? 42.056 101.969 38.880 1.00 22.69 ? 213 ARG B CA 1 ATOM 3564 C C . ARG B 2 213 ? 42.678 100.565 38.949 1.00 22.91 ? 213 ARG B C 1 ATOM 3565 O O . ARG B 2 213 ? 43.349 100.244 39.929 1.00 22.20 ? 213 ARG B O 1 ATOM 3566 C CB . ARG B 2 213 ? 43.109 103.061 39.004 1.00 24.51 ? 213 ARG B CB 1 ATOM 3567 C CG . ARG B 2 213 ? 43.894 103.394 37.749 1.00 25.75 ? 213 ARG B CG 1 ATOM 3568 C CD . ARG B 2 213 ? 45.037 102.431 37.499 1.00 26.69 ? 213 ARG B CD 1 ATOM 3569 N NE . ARG B 2 213 ? 45.804 102.764 36.291 1.00 28.31 ? 213 ARG B NE 1 ATOM 3570 C CZ . ARG B 2 213 ? 46.695 103.748 36.171 1.00 27.35 ? 213 ARG B CZ 1 ATOM 3571 N NH1 . ARG B 2 213 ? 46.949 104.570 37.171 1.00 29.64 ? 213 ARG B NH1 1 ATOM 3572 N NH2 . ARG B 2 213 ? 47.321 103.928 35.011 1.00 28.65 ? 213 ARG B NH2 1 ATOM 3573 N N . TRP B 2 214 ? 42.440 99.753 37.915 1.00 21.43 ? 214 TRP B N 1 ATOM 3574 C CA . TRP B 2 214 ? 42.850 98.337 37.856 1.00 21.56 ? 214 TRP B CA 1 ATOM 3575 C C . TRP B 2 214 ? 43.615 98.022 36.563 1.00 22.87 ? 214 TRP B C 1 ATOM 3576 O O . TRP B 2 214 ? 43.195 98.438 35.490 1.00 22.03 ? 214 TRP B O 1 ATOM 3577 C CB . TRP B 2 214 ? 41.638 97.414 37.917 1.00 21.13 ? 214 TRP B CB 1 ATOM 3578 C CG . TRP B 2 214 ? 40.843 97.637 39.134 1.00 22.24 ? 214 TRP B CG 1 ATOM 3579 C CD1 . TRP B 2 214 ? 39.685 98.370 39.245 1.00 21.64 ? 214 TRP B CD1 1 ATOM 3580 C CD2 . TRP B 2 214 ? 41.160 97.183 40.446 1.00 21.35 ? 214 TRP B CD2 1 ATOM 3581 N NE1 . TRP B 2 214 ? 39.266 98.378 40.540 1.00 22.00 ? 214 TRP B NE1 1 ATOM 3582 C CE2 . TRP B 2 214 ? 40.154 97.661 41.305 1.00 22.35 ? 214 TRP B CE2 1 ATOM 3583 C CE3 . TRP B 2 214 ? 42.196 96.420 40.982 1.00 21.26 ? 214 TRP B CE3 1 ATOM 3584 C CZ2 . TRP B 2 214 ? 40.150 97.379 42.683 1.00 22.25 ? 214 TRP B CZ2 1 ATOM 3585 C CZ3 . TRP B 2 214 ? 42.188 96.134 42.342 1.00 21.88 ? 214 TRP B CZ3 1 ATOM 3586 C CH2 . TRP B 2 214 ? 41.177 96.613 43.176 1.00 21.97 ? 214 TRP B CH2 1 ATOM 3587 N N . VAL B 2 215 ? 44.718 97.290 36.681 1.00 21.35 ? 215 VAL B N 1 ATOM 3588 C CA . VAL B 2 215 ? 45.574 96.949 35.551 1.00 21.77 ? 215 VAL B CA 1 ATOM 3589 C C . VAL B 2 215 ? 45.596 95.449 35.439 1.00 21.84 ? 215 VAL B C 1 ATOM 3590 O O . VAL B 2 215 ? 45.963 94.741 36.422 1.00 21.13 ? 215 VAL B O 1 ATOM 3591 C CB . VAL B 2 215 ? 47.007 97.457 35.768 1.00 22.44 ? 215 VAL B CB 1 ATOM 3592 C CG1 . VAL B 2 215 ? 47.957 96.971 34.665 1.00 22.71 ? 215 VAL B CG1 1 ATOM 3593 C CG2 . VAL B 2 215 ? 46.992 98.966 35.903 1.00 23.26 ? 215 VAL B CG2 1 ATOM 3594 N N . PHE B 2 216 ? 45.209 94.964 34.262 1.00 20.88 ? 216 PHE B N 1 ATOM 3595 C CA . PHE B 2 216 ? 45.284 93.544 33.964 1.00 21.45 ? 216 PHE B CA 1 ATOM 3596 C C . PHE B 2 216 ? 46.703 93.255 33.517 1.00 21.49 ? 216 PHE B C 1 ATOM 3597 O O . PHE B 2 216 ? 47.090 93.608 32.423 1.00 20.80 ? 216 PHE B O 1 ATOM 3598 C CB . PHE B 2 216 ? 44.271 93.137 32.924 1.00 22.03 ? 216 PHE B CB 1 ATOM 3599 C CG . PHE B 2 216 ? 42.859 93.217 33.417 1.00 21.98 ? 216 PHE B CG 1 ATOM 3600 C CD1 . PHE B 2 216 ? 42.186 94.434 33.420 1.00 22.53 ? 216 PHE B CD1 1 ATOM 3601 C CD2 . PHE B 2 216 ? 42.212 92.090 33.893 1.00 22.33 ? 216 PHE B CD2 1 ATOM 3602 C CE1 . PHE B 2 216 ? 40.891 94.518 33.883 1.00 22.58 ? 216 PHE B CE1 1 ATOM 3603 C CE2 . PHE B 2 216 ? 40.918 92.171 34.381 1.00 22.94 ? 216 PHE B CE2 1 ATOM 3604 C CZ . PHE B 2 216 ? 40.258 93.391 34.370 1.00 22.73 ? 216 PHE B CZ 1 ATOM 3605 N N . THR B 2 217 ? 47.486 92.629 34.389 1.00 21.00 ? 217 THR B N 1 ATOM 3606 C CA . THR B 2 217 ? 48.905 92.481 34.122 1.00 21.76 ? 217 THR B CA 1 ATOM 3607 C C . THR B 2 217 ? 49.152 91.244 33.238 1.00 22.35 ? 217 THR B C 1 ATOM 3608 O O . THR B 2 217 ? 48.358 90.311 33.220 1.00 21.51 ? 217 THR B O 1 ATOM 3609 C CB . THR B 2 217 ? 49.707 92.326 35.427 1.00 21.54 ? 217 THR B CB 1 ATOM 3610 O OG1 . THR B 2 217 ? 49.381 91.067 36.031 1.00 20.39 ? 217 THR B OG1 1 ATOM 3611 C CG2 . THR B 2 217 ? 49.411 93.500 36.385 1.00 22.59 ? 217 THR B CG2 1 ATOM 3612 N N . PRO B 2 218 ? 50.302 91.203 32.558 1.00 23.88 ? 218 PRO B N 1 ATOM 3613 C CA . PRO B 2 218 ? 50.651 90.011 31.778 1.00 25.00 ? 218 PRO B CA 1 ATOM 3614 C C . PRO B 2 218 ? 50.907 88.777 32.667 1.00 24.86 ? 218 PRO B C 1 ATOM 3615 O O . PRO B 2 218 ? 50.683 87.671 32.232 1.00 24.04 ? 218 PRO B O 1 ATOM 3616 C CB . PRO B 2 218 ? 51.911 90.440 31.020 1.00 25.25 ? 218 PRO B CB 1 ATOM 3617 C CG . PRO B 2 218 ? 52.465 91.542 31.812 1.00 26.28 ? 218 PRO B CG 1 ATOM 3618 C CD . PRO B 2 218 ? 51.298 92.269 32.397 1.00 25.07 ? 218 PRO B CD 1 ATOM 3619 N N . GLN B 2 219 ? 51.261 88.975 33.929 1.00 24.23 ? 219 GLN B N 1 ATOM 3620 C CA . GLN B 2 219 ? 51.400 87.843 34.849 1.00 24.79 ? 219 GLN B CA 1 ATOM 3621 C C . GLN B 2 219 ? 50.076 87.286 35.377 1.00 23.83 ? 219 GLN B C 1 ATOM 3622 O O . GLN B 2 219 ? 50.060 86.366 36.173 1.00 23.66 ? 219 GLN B O 1 ATOM 3623 C CB . GLN B 2 219 ? 52.399 88.139 35.980 1.00 27.09 ? 219 GLN B CB 1 ATOM 3624 C CG . GLN B 2 219 ? 52.077 89.270 36.929 1.00 27.69 ? 219 GLN B CG 1 ATOM 3625 C CD . GLN B 2 219 ? 52.492 90.643 36.416 1.00 29.14 ? 219 GLN B CD 1 ATOM 3626 O OE1 . GLN B 2 219 ? 52.742 90.845 35.210 1.00 29.00 ? 219 GLN B OE1 1 ATOM 3627 N NE2 . GLN B 2 219 ? 52.525 91.611 37.323 1.00 30.16 ? 219 GLN B NE2 1 ATOM 3628 N N . GLY B 2 220 ? 48.959 87.816 34.903 1.00 22.23 ? 220 GLY B N 1 ATOM 3629 C CA . GLY B 2 220 ? 47.656 87.262 35.207 1.00 20.85 ? 220 GLY B CA 1 ATOM 3630 C C . GLY B 2 220 ? 46.985 87.816 36.458 1.00 20.48 ? 220 GLY B C 1 ATOM 3631 O O . GLY B 2 220 ? 45.998 87.242 36.915 1.00 20.33 ? 220 GLY B O 1 ATOM 3632 N N . THR B 2 221 ? 47.499 88.919 37.008 1.00 19.46 ? 221 THR B N 1 ATOM 3633 C CA . THR B 2 221 ? 46.894 89.530 38.190 1.00 18.24 ? 221 THR B CA 1 ATOM 3634 C C . THR B 2 221 ? 46.034 90.724 37.752 1.00 19.09 ? 221 THR B C 1 ATOM 3635 O O . THR B 2 221 ? 46.150 91.207 36.599 1.00 17.74 ? 221 THR B O 1 ATOM 3636 C CB . THR B 2 221 ? 47.952 89.967 39.213 1.00 18.58 ? 221 THR B CB 1 ATOM 3637 O OG1 . THR B 2 221 ? 48.813 90.970 38.661 1.00 18.01 ? 221 THR B OG1 1 ATOM 3638 C CG2 . THR B 2 221 ? 48.801 88.749 39.701 1.00 19.89 ? 221 THR B CG2 1 ATOM 3639 N N . ILE B 2 222 ? 45.182 91.173 38.672 1.00 19.17 ? 222 ILE B N 1 ATOM 3640 C CA . ILE B 2 222 ? 44.449 92.430 38.529 1.00 20.13 ? 222 ILE B CA 1 ATOM 3641 C C . ILE B 2 222 ? 44.989 93.368 39.598 1.00 19.97 ? 222 ILE B C 1 ATOM 3642 O O . ILE B 2 222 ? 44.710 93.202 40.778 1.00 20.02 ? 222 ILE B O 1 ATOM 3643 C CB . ILE B 2 222 ? 42.928 92.252 38.623 1.00 20.59 ? 222 ILE B CB 1 ATOM 3644 C CG1 . ILE B 2 222 ? 42.454 91.249 37.569 1.00 21.25 ? 222 ILE B CG1 1 ATOM 3645 C CG2 . ILE B 2 222 ? 42.241 93.594 38.402 1.00 21.18 ? 222 ILE B CG2 1 ATOM 3646 C CD1 . ILE B 2 222 ? 41.003 90.823 37.679 1.00 20.86 ? 222 ILE B CD1 1 ATOM 3647 N N . SER B 2 223 ? 45.818 94.297 39.163 1.00 20.19 ? 223 SER B N 1 ATOM 3648 C CA . SER B 2 223 ? 46.635 95.111 40.038 1.00 21.79 ? 223 SER B CA 1 ATOM 3649 C C . SER B 2 223 ? 46.017 96.489 40.264 1.00 21.96 ? 223 SER B C 1 ATOM 3650 O O . SER B 2 223 ? 45.497 97.111 39.337 1.00 20.62 ? 223 SER B O 1 ATOM 3651 C CB . SER B 2 223 ? 48.032 95.252 39.432 1.00 22.71 ? 223 SER B CB 1 ATOM 3652 O OG . SER B 2 223 ? 48.742 96.342 39.963 1.00 24.81 ? 223 SER B OG 1 ATOM 3653 N N . ASN B 2 224 ? 46.093 96.955 41.504 1.00 22.42 ? 224 ASN B N 1 ATOM 3654 C CA . ASN B 2 224 ? 45.837 98.351 41.823 1.00 22.02 ? 224 ASN B CA 1 ATOM 3655 C C . ASN B 2 224 ? 47.190 98.999 42.052 1.00 22.44 ? 224 ASN B C 1 ATOM 3656 O O . ASN B 2 224 ? 47.786 98.829 43.131 1.00 24.33 ? 224 ASN B O 1 ATOM 3657 C CB . ASN B 2 224 ? 44.934 98.483 43.035 1.00 23.11 ? 224 ASN B CB 1 ATOM 3658 C CG . ASN B 2 224 ? 44.510 99.930 43.284 1.00 22.98 ? 224 ASN B CG 1 ATOM 3659 O OD1 . ASN B 2 224 ? 45.348 100.808 43.494 1.00 23.10 ? 224 ASN B OD1 1 ATOM 3660 N ND2 . ASN B 2 224 ? 43.227 100.180 43.231 1.00 22.85 ? 224 ASN B ND2 1 ATOM 3661 N N . PRO B 2 225 ? 47.698 99.746 41.059 1.00 22.77 ? 225 PRO B N 1 ATOM 3662 C CA . PRO B 2 225 ? 49.096 100.153 41.192 1.00 22.73 ? 225 PRO B CA 1 ATOM 3663 C C . PRO B 2 225 ? 49.330 101.207 42.266 1.00 24.65 ? 225 PRO B C 1 ATOM 3664 O O . PRO B 2 225 ? 50.380 101.197 42.891 1.00 26.84 ? 225 PRO B O 1 ATOM 3665 C CB . PRO B 2 225 ? 49.454 100.674 39.796 1.00 23.57 ? 225 PRO B CB 1 ATOM 3666 C CG . PRO B 2 225 ? 48.149 101.049 39.170 1.00 22.42 ? 225 PRO B CG 1 ATOM 3667 C CD . PRO B 2 225 ? 47.164 100.059 39.716 1.00 22.27 ? 225 PRO B CD 1 ATOM 3668 N N . GLY B 2 226 ? 48.371 102.087 42.515 1.00 25.25 ? 226 GLY B N 1 ATOM 3669 C CA . GLY B 2 226 ? 48.539 103.087 43.584 1.00 26.30 ? 226 GLY B CA 1 ATOM 3670 C C . GLY B 2 226 ? 48.612 102.472 44.978 1.00 26.50 ? 226 GLY B C 1 ATOM 3671 O O . GLY B 2 226 ? 49.316 102.977 45.841 1.00 26.71 ? 226 GLY B O 1 ATOM 3672 N N . TYR B 2 227 ? 47.890 101.381 45.203 1.00 26.13 ? 227 TYR B N 1 ATOM 3673 C CA . TYR B 2 227 ? 47.974 100.672 46.480 1.00 26.81 ? 227 TYR B CA 1 ATOM 3674 C C . TYR B 2 227 ? 48.944 99.482 46.469 1.00 26.07 ? 227 TYR B C 1 ATOM 3675 O O . TYR B 2 227 ? 49.061 98.780 47.465 1.00 25.93 ? 227 TYR B O 1 ATOM 3676 C CB . TYR B 2 227 ? 46.574 100.294 46.986 1.00 27.29 ? 227 TYR B CB 1 ATOM 3677 C CG . TYR B 2 227 ? 45.663 101.499 47.248 1.00 29.01 ? 227 TYR B CG 1 ATOM 3678 C CD1 . TYR B 2 227 ? 46.150 102.662 47.868 1.00 31.60 ? 227 TYR B CD1 1 ATOM 3679 C CD2 . TYR B 2 227 ? 44.328 101.482 46.874 1.00 29.34 ? 227 TYR B CD2 1 ATOM 3680 C CE1 . TYR B 2 227 ? 45.331 103.755 48.109 1.00 33.52 ? 227 TYR B CE1 1 ATOM 3681 C CE2 . TYR B 2 227 ? 43.492 102.578 47.109 1.00 31.30 ? 227 TYR B CE2 1 ATOM 3682 C CZ . TYR B 2 227 ? 44.002 103.707 47.730 1.00 33.66 ? 227 TYR B CZ 1 ATOM 3683 O OH . TYR B 2 227 ? 43.220 104.801 47.977 1.00 34.62 ? 227 TYR B OH 1 ATOM 3684 N N . GLU B 2 228 ? 49.661 99.278 45.367 1.00 26.24 ? 228 GLU B N 1 ATOM 3685 C CA . GLU B 2 228 ? 50.680 98.223 45.242 1.00 27.70 ? 228 GLU B CA 1 ATOM 3686 C C . GLU B 2 228 ? 50.181 96.866 45.735 1.00 26.75 ? 228 GLU B C 1 ATOM 3687 O O . GLU B 2 228 ? 50.827 96.175 46.541 1.00 24.70 ? 228 GLU B O 1 ATOM 3688 C CB . GLU B 2 228 ? 51.954 98.649 45.986 1.00 30.91 ? 228 GLU B CB 1 ATOM 3689 C CG . GLU B 2 228 ? 52.539 99.948 45.448 1.00 35.40 ? 228 GLU B CG 1 ATOM 3690 C CD . GLU B 2 228 ? 53.730 100.438 46.247 1.00 40.91 ? 228 GLU B CD 1 ATOM 3691 O OE1 . GLU B 2 228 ? 54.510 99.599 46.748 1.00 44.27 ? 228 GLU B OE1 1 ATOM 3692 O OE2 . GLU B 2 228 ? 53.896 101.677 46.356 1.00 48.58 ? 228 GLU B OE2 1 ATOM 3693 N N . ALA B 2 229 ? 48.989 96.517 45.276 1.00 23.58 ? 229 ALA B N 1 ATOM 3694 C CA . ALA B 2 229 ? 48.324 95.315 45.708 1.00 22.99 ? 229 ALA B CA 1 ATOM 3695 C C . ALA B 2 229 ? 47.496 94.760 44.558 1.00 21.45 ? 229 ALA B C 1 ATOM 3696 O O . ALA B 2 229 ? 47.382 95.414 43.494 1.00 21.25 ? 229 ALA B O 1 ATOM 3697 C CB . ALA B 2 229 ? 47.470 95.616 46.932 1.00 22.54 ? 229 ALA B CB 1 ATOM 3698 N N . VAL B 2 230 ? 46.948 93.567 44.758 1.00 19.87 ? 230 VAL B N 1 ATOM 3699 C CA . VAL B 2 230 ? 46.210 92.864 43.698 1.00 20.23 ? 230 VAL B CA 1 ATOM 3700 C C . VAL B 2 230 ? 44.923 92.263 44.214 1.00 21.28 ? 230 VAL B C 1 ATOM 3701 O O . VAL B 2 230 ? 44.828 92.003 45.406 1.00 21.20 ? 230 VAL B O 1 ATOM 3702 C CB . VAL B 2 230 ? 47.046 91.759 42.996 1.00 19.12 ? 230 VAL B CB 1 ATOM 3703 C CG1 . VAL B 2 230 ? 48.364 92.305 42.488 1.00 19.97 ? 230 VAL B CG1 1 ATOM 3704 C CG2 . VAL B 2 230 ? 47.276 90.544 43.898 1.00 19.75 ? 230 VAL B CG2 1 ATOM 3705 N N . MET B 2 231 ? 43.956 92.011 43.319 1.00 20.60 ? 231 MET B N 1 ATOM 3706 C CA . MET B 2 231 ? 42.731 91.320 43.692 1.00 22.43 ? 231 MET B CA 1 ATOM 3707 C C . MET B 2 231 ? 43.004 89.888 44.067 1.00 21.80 ? 231 MET B C 1 ATOM 3708 O O . MET B 2 231 ? 43.720 89.162 43.367 1.00 21.09 ? 231 MET B O 1 ATOM 3709 C CB . MET B 2 231 ? 41.726 91.223 42.547 1.00 24.64 ? 231 MET B CB 1 ATOM 3710 C CG . MET B 2 231 ? 41.106 92.513 42.122 1.00 28.08 ? 231 MET B CG 1 ATOM 3711 S SD . MET B 2 231 ? 39.554 92.198 41.258 1.00 30.16 ? 231 MET B SD 1 ATOM 3712 C CE . MET B 2 231 ? 39.286 93.926 40.920 1.00 30.56 ? 231 MET B CE 1 ATOM 3713 N N . ASP B 2 232 ? 42.367 89.454 45.131 1.00 22.30 ? 232 ASP B N 1 ATOM 3714 C CA . ASP B 2 232 ? 42.595 88.125 45.663 1.00 22.83 ? 232 ASP B CA 1 ATOM 3715 C C . ASP B 2 232 ? 41.301 87.577 46.221 1.00 24.47 ? 232 ASP B C 1 ATOM 3716 O O . ASP B 2 232 ? 40.487 88.327 46.720 1.00 26.65 ? 232 ASP B O 1 ATOM 3717 C CB . ASP B 2 232 ? 43.632 88.228 46.761 1.00 23.79 ? 232 ASP B CB 1 ATOM 3718 C CG . ASP B 2 232 ? 44.278 86.892 47.107 1.00 25.91 ? 232 ASP B CG 1 ATOM 3719 O OD1 . ASP B 2 232 ? 43.904 85.811 46.549 1.00 27.22 ? 232 ASP B OD1 1 ATOM 3720 O OD2 . ASP B 2 232 ? 45.206 86.962 47.929 1.00 25.97 ? 232 ASP B OD2 1 ATOM 3721 N N . VAL B 2 233 ? 41.122 86.270 46.144 1.00 23.34 ? 233 VAL B N 1 ATOM 3722 C CA . VAL B 2 233 ? 39.957 85.611 46.704 1.00 24.10 ? 233 VAL B CA 1 ATOM 3723 C C . VAL B 2 233 ? 40.272 85.367 48.180 1.00 24.61 ? 233 VAL B C 1 ATOM 3724 O O . VAL B 2 233 ? 41.258 84.717 48.487 1.00 23.52 ? 233 VAL B O 1 ATOM 3725 C CB . VAL B 2 233 ? 39.682 84.282 46.002 1.00 24.42 ? 233 VAL B CB 1 ATOM 3726 C CG1 . VAL B 2 233 ? 38.482 83.551 46.616 1.00 25.45 ? 233 VAL B CG1 1 ATOM 3727 C CG2 . VAL B 2 233 ? 39.467 84.509 44.514 1.00 24.16 ? 233 VAL B CG2 1 ATOM 3728 N N . ALA B 2 234 ? 39.444 85.897 49.082 1.00 24.27 ? 234 ALA B N 1 ATOM 3729 C CA . ALA B 2 234 ? 39.685 85.754 50.545 1.00 25.37 ? 234 ALA B CA 1 ATOM 3730 C C . ALA B 2 234 ? 39.951 84.306 50.927 1.00 24.17 ? 234 ALA B C 1 ATOM 3731 O O . ALA B 2 234 ? 39.193 83.430 50.573 1.00 24.38 ? 234 ALA B O 1 ATOM 3732 C CB . ALA B 2 234 ? 38.515 86.300 51.359 1.00 24.32 ? 234 ALA B CB 1 ATOM 3733 N N . GLN B 2 235 ? 41.072 84.070 51.607 1.00 26.25 ? 235 GLN B N 1 ATOM 3734 C CA . GLN B 2 235 ? 41.481 82.736 52.105 1.00 26.50 ? 235 GLN B CA 1 ATOM 3735 C C . GLN B 2 235 ? 41.536 81.665 51.017 1.00 25.84 ? 235 GLN B C 1 ATOM 3736 O O . GLN B 2 235 ? 41.382 80.474 51.304 1.00 25.82 ? 235 GLN B O 1 ATOM 3737 C CB . GLN B 2 235 ? 40.553 82.278 53.239 1.00 27.94 ? 235 GLN B CB 1 ATOM 3738 C CG . GLN B 2 235 ? 40.237 83.346 54.277 1.00 30.64 ? 235 GLN B CG 1 ATOM 3739 C CD . GLN B 2 235 ? 41.460 83.809 55.063 1.00 34.07 ? 235 GLN B CD 1 ATOM 3740 O OE1 . GLN B 2 235 ? 42.447 83.085 55.192 1.00 41.45 ? 235 GLN B OE1 1 ATOM 3741 N NE2 . GLN B 2 235 ? 41.391 85.008 55.596 1.00 35.61 ? 235 GLN B NE2 1 ATOM 3742 N N . ASN B 2 236 ? 41.722 82.088 49.760 1.00 26.02 ? 236 ASN B N 1 ATOM 3743 C CA . ASN B 2 236 ? 41.576 81.198 48.613 1.00 26.09 ? 236 ASN B CA 1 ATOM 3744 C C . ASN B 2 236 ? 40.335 80.324 48.680 1.00 24.39 ? 236 ASN B C 1 ATOM 3745 O O . ASN B 2 236 ? 40.352 79.167 48.262 1.00 24.54 ? 236 ASN B O 1 ATOM 3746 C CB . ASN B 2 236 ? 42.834 80.346 48.461 1.00 27.85 ? 236 ASN B CB 1 ATOM 3747 C CG . ASN B 2 236 ? 43.991 81.144 47.907 1.00 31.72 ? 236 ASN B CG 1 ATOM 3748 O OD1 . ASN B 2 236 ? 44.100 81.332 46.696 1.00 31.73 ? 236 ASN B OD1 1 ATOM 3749 N ND2 . ASN B 2 236 ? 44.844 81.633 48.783 1.00 33.49 ? 236 ASN B ND2 1 ATOM 3750 N N . ASP B 2 237 ? 39.252 80.880 49.199 1.00 23.28 ? 237 ASP B N 1 ATOM 3751 C CA . ASP B 2 237 ? 38.015 80.133 49.343 1.00 24.41 ? 237 ASP B CA 1 ATOM 3752 C C . ASP B 2 237 ? 36.872 80.890 48.677 1.00 23.65 ? 237 ASP B C 1 ATOM 3753 O O . ASP B 2 237 ? 36.372 81.872 49.210 1.00 23.44 ? 237 ASP B O 1 ATOM 3754 C CB . ASP B 2 237 ? 37.712 79.881 50.825 1.00 25.74 ? 237 ASP B CB 1 ATOM 3755 C CG . ASP B 2 237 ? 36.528 78.958 51.024 1.00 27.56 ? 237 ASP B CG 1 ATOM 3756 O OD1 . ASP B 2 237 ? 35.731 78.747 50.091 1.00 27.03 ? 237 ASP B OD1 1 ATOM 3757 O OD2 . ASP B 2 237 ? 36.412 78.396 52.121 1.00 30.43 ? 237 ASP B OD2 1 ATOM 3758 N N . VAL B 2 238 ? 36.444 80.401 47.529 1.00 23.85 ? 238 VAL B N 1 ATOM 3759 C CA . VAL B 2 238 ? 35.382 81.075 46.756 1.00 24.60 ? 238 VAL B CA 1 ATOM 3760 C C . VAL B 2 238 ? 34.058 81.157 47.501 1.00 24.57 ? 238 VAL B C 1 ATOM 3761 O O . VAL B 2 238 ? 33.275 82.079 47.285 1.00 24.34 ? 238 VAL B O 1 ATOM 3762 C CB . VAL B 2 238 ? 35.118 80.386 45.390 1.00 24.98 ? 238 VAL B CB 1 ATOM 3763 C CG1 . VAL B 2 238 ? 36.375 80.416 44.532 1.00 24.99 ? 238 VAL B CG1 1 ATOM 3764 C CG2 . VAL B 2 238 ? 34.593 78.952 45.561 1.00 25.65 ? 238 VAL B CG2 1 ATOM 3765 N N . TYR B 2 239 ? 33.817 80.206 48.397 1.00 25.81 ? 239 TYR B N 1 ATOM 3766 C CA . TYR B 2 239 ? 32.561 80.165 49.151 1.00 26.83 ? 239 TYR B CA 1 ATOM 3767 C C . TYR B 2 239 ? 32.448 81.193 50.254 1.00 25.45 ? 239 TYR B C 1 ATOM 3768 O O . TYR B 2 239 ? 31.360 81.408 50.750 1.00 25.59 ? 239 TYR B O 1 ATOM 3769 C CB . TYR B 2 239 ? 32.261 78.720 49.609 1.00 28.56 ? 239 TYR B CB 1 ATOM 3770 C CG . TYR B 2 239 ? 32.089 77.855 48.380 1.00 32.47 ? 239 TYR B CG 1 ATOM 3771 C CD1 . TYR B 2 239 ? 31.041 78.108 47.480 1.00 36.03 ? 239 TYR B CD1 1 ATOM 3772 C CD2 . TYR B 2 239 ? 33.021 76.867 48.049 1.00 33.68 ? 239 TYR B CD2 1 ATOM 3773 C CE1 . TYR B 2 239 ? 30.891 77.357 46.319 1.00 37.55 ? 239 TYR B CE1 1 ATOM 3774 C CE2 . TYR B 2 239 ? 32.891 76.124 46.886 1.00 35.75 ? 239 TYR B CE2 1 ATOM 3775 C CZ . TYR B 2 239 ? 31.817 76.366 46.028 1.00 38.86 ? 239 TYR B CZ 1 ATOM 3776 O OH . TYR B 2 239 ? 31.665 75.643 44.864 1.00 40.69 ? 239 TYR B OH 1 ATOM 3777 N N . LEU B 2 240 ? 33.527 81.899 50.582 1.00 23.48 ? 240 LEU B N 1 ATOM 3778 C CA . LEU B 2 240 ? 33.447 83.029 51.501 1.00 23.46 ? 240 LEU B CA 1 ATOM 3779 C C . LEU B 2 240 ? 32.806 84.261 50.860 1.00 24.03 ? 240 LEU B C 1 ATOM 3780 O O . LEU B 2 240 ? 32.399 85.193 51.567 1.00 22.52 ? 240 LEU B O 1 ATOM 3781 C CB . LEU B 2 240 ? 34.832 83.359 52.059 1.00 23.54 ? 240 LEU B CB 1 ATOM 3782 C CG . LEU B 2 240 ? 35.488 82.275 52.933 1.00 24.33 ? 240 LEU B CG 1 ATOM 3783 C CD1 . LEU B 2 240 ? 36.864 82.753 53.378 1.00 24.65 ? 240 LEU B CD1 1 ATOM 3784 C CD2 . LEU B 2 240 ? 34.653 81.914 54.169 1.00 25.84 ? 240 LEU B CD2 1 ATOM 3785 N N . LYS B 2 241 ? 32.709 84.271 49.526 1.00 24.40 ? 241 LYS B N 1 ATOM 3786 C CA . LYS B 2 241 ? 32.071 85.364 48.792 1.00 24.37 ? 241 LYS B CA 1 ATOM 3787 C C . LYS B 2 241 ? 32.727 86.693 49.114 1.00 23.24 ? 241 LYS B C 1 ATOM 3788 O O . LYS B 2 241 ? 32.065 87.706 49.364 1.00 23.99 ? 241 LYS B O 1 ATOM 3789 C CB . LYS B 2 241 ? 30.570 85.386 49.079 1.00 26.43 ? 241 LYS B CB 1 ATOM 3790 C CG . LYS B 2 241 ? 29.831 84.133 48.623 1.00 29.58 ? 241 LYS B CG 1 ATOM 3791 C CD . LYS B 2 241 ? 28.337 84.294 48.924 1.00 32.93 ? 241 LYS B CD 1 ATOM 3792 C CE . LYS B 2 241 ? 27.495 83.060 48.614 1.00 35.82 ? 241 LYS B CE 1 ATOM 3793 N NZ . LYS B 2 241 ? 27.634 82.471 47.253 1.00 39.49 ? 241 LYS B NZ 1 ATOM 3794 N N . LYS B 2 242 ? 34.051 86.681 49.123 1.00 22.10 ? 242 LYS B N 1 ATOM 3795 C CA . LYS B 2 242 ? 34.827 87.863 49.464 1.00 21.78 ? 242 LYS B CA 1 ATOM 3796 C C . LYS B 2 242 ? 36.066 87.934 48.589 1.00 21.24 ? 242 LYS B C 1 ATOM 3797 O O . LYS B 2 242 ? 36.891 87.006 48.565 1.00 20.18 ? 242 LYS B O 1 ATOM 3798 C CB . LYS B 2 242 ? 35.223 87.862 50.955 1.00 22.64 ? 242 LYS B CB 1 ATOM 3799 C CG . LYS B 2 242 ? 34.103 88.283 51.900 1.00 22.67 ? 242 LYS B CG 1 ATOM 3800 C CD . LYS B 2 242 ? 34.608 88.505 53.331 1.00 23.68 ? 242 LYS B CD 1 ATOM 3801 C CE . LYS B 2 242 ? 33.530 89.131 54.227 1.00 23.13 ? 242 LYS B CE 1 ATOM 3802 N NZ . LYS B 2 242 ? 32.333 88.269 54.274 1.00 23.05 ? 242 LYS B NZ 1 ATOM 3803 N N . ILE B 2 243 ? 36.164 89.042 47.861 1.00 21.03 ? 243 ILE B N 1 ATOM 3804 C CA . ILE B 2 243 ? 37.342 89.403 47.104 1.00 21.39 ? 243 ILE B CA 1 ATOM 3805 C C . ILE B 2 243 ? 38.003 90.541 47.837 1.00 20.84 ? 243 ILE B C 1 ATOM 3806 O O . ILE B 2 243 ? 37.340 91.516 48.219 1.00 20.62 ? 243 ILE B O 1 ATOM 3807 C CB . ILE B 2 243 ? 36.971 89.862 45.667 1.00 21.15 ? 243 ILE B CB 1 ATOM 3808 C CG1 . ILE B 2 243 ? 35.982 88.894 45.034 1.00 21.91 ? 243 ILE B CG1 1 ATOM 3809 C CG2 . ILE B 2 243 ? 38.229 90.043 44.820 1.00 21.68 ? 243 ILE B CG2 1 ATOM 3810 C CD1 . ILE B 2 243 ? 36.458 87.458 44.929 1.00 22.70 ? 243 ILE B CD1 1 ATOM 3811 N N . VAL B 2 244 ? 39.318 90.436 48.015 1.00 19.95 ? 244 VAL B N 1 ATOM 3812 C CA . VAL B 2 244 ? 40.066 91.404 48.783 1.00 20.39 ? 244 VAL B CA 1 ATOM 3813 C C . VAL B 2 244 ? 41.275 91.891 48.032 1.00 21.33 ? 244 VAL B C 1 ATOM 3814 O O . VAL B 2 244 ? 41.719 91.263 47.051 1.00 21.93 ? 244 VAL B O 1 ATOM 3815 C CB . VAL B 2 244 ? 40.517 90.847 50.166 1.00 21.41 ? 244 VAL B CB 1 ATOM 3816 C CG1 . VAL B 2 244 ? 39.309 90.449 51.005 1.00 22.22 ? 244 VAL B CG1 1 ATOM 3817 C CG2 . VAL B 2 244 ? 41.460 89.638 50.006 1.00 21.54 ? 244 VAL B CG2 1 ATOM 3818 N N . LEU B 2 245 ? 41.812 93.005 48.514 1.00 20.58 ? 245 LEU B N 1 ATOM 3819 C CA . LEU B 2 245 ? 43.066 93.565 48.021 1.00 22.58 ? 245 LEU B CA 1 ATOM 3820 C C . LEU B 2 245 ? 44.210 93.051 48.896 1.00 23.83 ? 245 LEU B C 1 ATOM 3821 O O . LEU B 2 245 ? 44.173 93.242 50.115 1.00 23.96 ? 245 LEU B O 1 ATOM 3822 C CB . LEU B 2 245 ? 43.009 95.085 48.070 1.00 23.58 ? 245 LEU B CB 1 ATOM 3823 C CG . LEU B 2 245 ? 43.989 95.883 47.233 1.00 25.34 ? 245 LEU B CG 1 ATOM 3824 C CD1 . LEU B 2 245 ? 43.868 95.557 45.752 1.00 25.30 ? 245 LEU B CD1 1 ATOM 3825 C CD2 . LEU B 2 245 ? 43.815 97.377 47.448 1.00 25.98 ? 245 LEU B CD2 1 ATOM 3826 N N . SER B 2 246 ? 45.182 92.376 48.287 1.00 23.26 ? 246 SER B N 1 ATOM 3827 C CA . SER B 2 246 ? 46.331 91.820 49.005 1.00 24.82 ? 246 SER B CA 1 ATOM 3828 C C . SER B 2 246 ? 47.643 92.127 48.301 1.00 24.61 ? 246 SER B C 1 ATOM 3829 O O . SER B 2 246 ? 47.686 92.313 47.085 1.00 22.78 ? 246 SER B O 1 ATOM 3830 C CB . SER B 2 246 ? 46.242 90.299 49.092 1.00 26.05 ? 246 SER B CB 1 ATOM 3831 O OG . SER B 2 246 ? 44.965 89.830 49.462 1.00 28.99 ? 246 SER B OG 1 ATOM 3832 N N . SER B 2 247 ? 48.730 92.087 49.052 1.00 25.38 ? 247 SER B N 1 ATOM 3833 C CA . SER B 2 247 ? 50.070 92.040 48.449 1.00 29.09 ? 247 SER B CA 1 ATOM 3834 C C . SER B 2 247 ? 50.195 90.816 47.554 1.00 27.56 ? 247 SER B C 1 ATOM 3835 O O . SER B 2 247 ? 49.717 89.754 47.911 1.00 27.68 ? 247 SER B O 1 ATOM 3836 C CB . SER B 2 247 ? 51.135 91.987 49.533 1.00 29.07 ? 247 SER B CB 1 ATOM 3837 O OG . SER B 2 247 ? 51.135 93.255 50.143 1.00 33.06 ? 247 SER B OG 1 ATOM 3838 N N . ALA B 2 248 ? 50.797 90.994 46.384 1.00 28.49 ? 248 ALA B N 1 ATOM 3839 C CA . ALA B 2 248 ? 51.022 89.888 45.453 1.00 30.93 ? 248 ALA B CA 1 ATOM 3840 C C . ALA B 2 248 ? 51.869 88.808 46.133 1.00 32.40 ? 248 ALA B C 1 ATOM 3841 O O . ALA B 2 248 ? 52.861 89.127 46.777 1.00 32.13 ? 248 ALA B O 1 ATOM 3842 C CB . ALA B 2 248 ? 51.705 90.375 44.184 1.00 31.26 ? 248 ALA B CB 1 ATOM 3843 N N . THR B 2 249 ? 51.448 87.554 46.015 1.00 34.84 ? 249 THR B N 1 ATOM 3844 C CA . THR B 2 249 ? 52.145 86.387 46.601 1.00 38.59 ? 249 THR B CA 1 ATOM 3845 C C . THR B 2 249 ? 51.930 85.214 45.660 1.00 41.30 ? 249 THR B C 1 ATOM 3846 O O . THR B 2 249 ? 50.929 85.187 44.946 1.00 43.22 ? 249 THR B O 1 ATOM 3847 C CB . THR B 2 249 ? 51.587 86.041 48.014 1.00 40.45 ? 249 THR B CB 1 ATOM 3848 O OG1 . THR B 2 249 ? 52.297 84.935 48.579 1.00 48.07 ? 249 THR B OG1 1 ATOM 3849 C CG2 . THR B 2 249 ? 50.108 85.671 47.982 1.00 40.65 ? 249 THR B CG2 1 ATOM 3850 N N . ASP B 2 250 ? 52.832 84.236 45.650 1.00 45.33 ? 250 ASP B N 1 ATOM 3851 C CA . ASP B 2 250 ? 52.565 82.976 44.905 1.00 50.42 ? 250 ASP B CA 1 ATOM 3852 C C . ASP B 2 250 ? 51.894 81.873 45.736 1.00 49.85 ? 250 ASP B C 1 ATOM 3853 O O . ASP B 2 250 ? 51.781 80.750 45.263 1.00 52.33 ? 250 ASP B O 1 ATOM 3854 C CB . ASP B 2 250 ? 53.848 82.407 44.294 1.00 53.70 ? 250 ASP B CB 1 ATOM 3855 N N . LYS B 2 251 ? 51.501 82.164 46.961 1.00 52.59 ? 251 LYS B N 1 ATOM 3856 C CA . LYS B 2 251 ? 50.990 81.142 47.845 1.00 55.85 ? 251 LYS B CA 1 ATOM 3857 C C . LYS B 2 251 ? 49.787 80.319 47.380 1.00 55.92 ? 251 LYS B C 1 ATOM 3858 O O . LYS B 2 251 ? 49.741 79.115 47.583 1.00 69.29 ? 251 LYS B O 1 ATOM 3859 C CB . LYS B 2 251 ? 50.809 81.688 49.260 1.00 60.80 ? 251 LYS B CB 1 ATOM 3860 C CG . LYS B 2 251 ? 51.461 80.851 50.346 1.00 66.42 ? 251 LYS B CG 1 ATOM 3861 N N . GLY B 2 252 ? 48.807 80.963 46.782 1.00 46.20 ? 252 GLY B N 1 ATOM 3862 C CA . GLY B 2 252 ? 47.618 80.277 46.310 1.00 40.13 ? 252 GLY B CA 1 ATOM 3863 C C . GLY B 2 252 ? 47.333 80.671 44.884 1.00 36.78 ? 252 GLY B C 1 ATOM 3864 O O . GLY B 2 252 ? 48.107 81.405 44.287 1.00 34.17 ? 252 GLY B O 1 ATOM 3865 N N . ASN B 2 253 ? 46.248 80.169 44.314 1.00 31.86 ? 253 ASN B N 1 ATOM 3866 C CA . ASN B 2 253 ? 45.867 80.544 42.962 1.00 28.67 ? 253 ASN B CA 1 ATOM 3867 C C . ASN B 2 253 ? 44.849 81.695 42.931 1.00 24.37 ? 253 ASN B C 1 ATOM 3868 O O . ASN B 2 253 ? 44.410 82.094 41.874 1.00 22.17 ? 253 ASN B O 1 ATOM 3869 C CB . ASN B 2 253 ? 45.292 79.341 42.220 1.00 30.89 ? 253 ASN B CB 1 ATOM 3870 C CG . ASN B 2 253 ? 46.325 78.267 41.960 1.00 33.29 ? 253 ASN B CG 1 ATOM 3871 O OD1 . ASN B 2 253 ? 47.491 78.559 41.771 1.00 35.03 ? 253 ASN B OD1 1 ATOM 3872 N ND2 . ASN B 2 253 ? 45.890 77.018 41.949 1.00 34.06 ? 253 ASN B ND2 1 ATOM 3873 N N . GLY B 2 254 ? 44.487 82.215 44.097 1.00 21.67 ? 254 GLY B N 1 ATOM 3874 C CA . GLY B 2 254 ? 43.459 83.242 44.210 1.00 21.39 ? 254 GLY B CA 1 ATOM 3875 C C . GLY B 2 254 ? 43.761 84.599 43.604 1.00 21.19 ? 254 GLY B C 1 ATOM 3876 O O . GLY B 2 254 ? 42.858 85.458 43.550 1.00 21.14 ? 254 GLY B O 1 ATOM 3877 N N . GLN B 2 255 ? 45.012 84.835 43.193 1.00 20.70 ? 255 GLN B N 1 ATOM 3878 C CA . GLN B 2 255 ? 45.425 86.096 42.548 1.00 20.55 ? 255 GLN B CA 1 ATOM 3879 C C . GLN B 2 255 ? 45.477 86.029 41.010 1.00 20.99 ? 255 GLN B C 1 ATOM 3880 O O . GLN B 2 255 ? 45.847 87.003 40.342 1.00 19.82 ? 255 GLN B O 1 ATOM 3881 C CB . GLN B 2 255 ? 46.760 86.579 43.131 1.00 21.35 ? 255 GLN B CB 1 ATOM 3882 C CG . GLN B 2 255 ? 46.646 86.867 44.632 1.00 21.28 ? 255 GLN B CG 1 ATOM 3883 C CD . GLN B 2 255 ? 47.891 87.478 45.255 1.00 22.27 ? 255 GLN B CD 1 ATOM 3884 O OE1 . GLN B 2 255 ? 48.912 87.628 44.605 1.00 23.60 ? 255 GLN B OE1 1 ATOM 3885 N NE2 . GLN B 2 255 ? 47.794 87.856 46.533 1.00 23.23 ? 255 GLN B NE2 1 ATOM 3886 N N . GLN B 2 256 ? 45.085 84.875 40.464 1.00 21.46 ? 256 GLN B N 1 ATOM 3887 C CA . GLN B 2 256 ? 45.069 84.648 39.024 1.00 21.36 ? 256 GLN B CA 1 ATOM 3888 C C . GLN B 2 256 ? 43.684 84.842 38.438 1.00 20.69 ? 256 GLN B C 1 ATOM 3889 O O . GLN B 2 256 ? 42.696 84.258 38.907 1.00 19.95 ? 256 GLN B O 1 ATOM 3890 C CB . GLN B 2 256 ? 45.603 83.253 38.682 1.00 21.38 ? 256 GLN B CB 1 ATOM 3891 C CG . GLN B 2 256 ? 47.107 83.166 38.906 1.00 22.66 ? 256 GLN B CG 1 ATOM 3892 C CD . GLN B 2 256 ? 47.879 83.979 37.883 1.00 22.35 ? 256 GLN B CD 1 ATOM 3893 O OE1 . GLN B 2 256 ? 47.682 83.815 36.692 1.00 23.30 ? 256 GLN B OE1 1 ATOM 3894 N NE2 . GLN B 2 256 ? 48.721 84.889 38.342 1.00 23.27 ? 256 GLN B NE2 1 ATOM 3895 N N . TRP B 2 257 ? 43.646 85.608 37.359 1.00 20.86 ? 257 TRP B N 1 ATOM 3896 C CA . TRP B 2 257 ? 42.397 85.973 36.701 1.00 22.07 ? 257 TRP B CA 1 ATOM 3897 C C . TRP B 2 257 ? 42.592 85.897 35.191 1.00 23.71 ? 257 TRP B C 1 ATOM 3898 O O . TRP B 2 257 ? 43.711 86.023 34.705 1.00 22.25 ? 257 TRP B O 1 ATOM 3899 C CB . TRP B 2 257 ? 41.989 87.389 37.096 1.00 21.46 ? 257 TRP B CB 1 ATOM 3900 C CG . TRP B 2 257 ? 41.874 87.587 38.572 1.00 21.95 ? 257 TRP B CG 1 ATOM 3901 C CD1 . TRP B 2 257 ? 42.871 87.945 39.418 1.00 23.15 ? 257 TRP B CD1 1 ATOM 3902 C CD2 . TRP B 2 257 ? 40.716 87.393 39.378 1.00 22.12 ? 257 TRP B CD2 1 ATOM 3903 N NE1 . TRP B 2 257 ? 42.403 88.011 40.711 1.00 23.02 ? 257 TRP B NE1 1 ATOM 3904 C CE2 . TRP B 2 257 ? 41.084 87.666 40.719 1.00 23.18 ? 257 TRP B CE2 1 ATOM 3905 C CE3 . TRP B 2 257 ? 39.403 87.039 39.104 1.00 22.25 ? 257 TRP B CE3 1 ATOM 3906 C CZ2 . TRP B 2 257 ? 40.172 87.605 41.776 1.00 23.13 ? 257 TRP B CZ2 1 ATOM 3907 C CZ3 . TRP B 2 257 ? 38.500 86.958 40.158 1.00 23.78 ? 257 TRP B CZ3 1 ATOM 3908 C CH2 . TRP B 2 257 ? 38.890 87.242 41.482 1.00 23.10 ? 257 TRP B CH2 1 ATOM 3909 N N . THR B 2 258 ? 41.487 85.684 34.476 1.00 24.16 ? 258 THR B N 1 ATOM 3910 C CA . THR B 2 258 ? 41.463 85.642 32.998 1.00 25.95 ? 258 THR B CA 1 ATOM 3911 C C . THR B 2 258 ? 40.355 86.570 32.479 1.00 24.91 ? 258 THR B C 1 ATOM 3912 O O . THR B 2 258 ? 39.245 86.560 32.992 1.00 23.69 ? 258 THR B O 1 ATOM 3913 C CB . THR B 2 258 ? 41.148 84.211 32.483 1.00 27.84 ? 258 THR B CB 1 ATOM 3914 O OG1 . THR B 2 258 ? 42.133 83.294 32.953 1.00 28.22 ? 258 THR B OG1 1 ATOM 3915 C CG2 . THR B 2 258 ? 41.118 84.150 30.957 1.00 29.72 ? 258 THR B CG2 1 ATOM 3916 N N . VAL B 2 259 ? 40.658 87.330 31.438 1.00 23.26 ? 259 VAL B N 1 ATOM 3917 C CA . VAL B 2 259 ? 39.673 88.135 30.757 1.00 25.47 ? 259 VAL B CA 1 ATOM 3918 C C . VAL B 2 259 ? 39.073 87.295 29.637 1.00 25.63 ? 259 VAL B C 1 ATOM 3919 O O . VAL B 2 259 ? 39.803 86.879 28.740 1.00 26.05 ? 259 VAL B O 1 ATOM 3920 C CB . VAL B 2 259 ? 40.336 89.388 30.201 1.00 26.10 ? 259 VAL B CB 1 ATOM 3921 C CG1 . VAL B 2 259 ? 39.365 90.181 29.340 1.00 28.26 ? 259 VAL B CG1 1 ATOM 3922 C CG2 . VAL B 2 259 ? 40.809 90.252 31.348 1.00 26.60 ? 259 VAL B CG2 1 ATOM 3923 N N . PHE B 2 260 ? 37.776 87.014 29.701 1.00 23.99 ? 260 PHE B N 1 ATOM 3924 C CA . PHE B 2 260 ? 37.119 86.243 28.650 1.00 25.44 ? 260 PHE B CA 1 ATOM 3925 C C . PHE B 2 260 ? 36.078 87.104 27.922 1.00 26.40 ? 260 PHE B C 1 ATOM 3926 O O . PHE B 2 260 ? 35.011 87.379 28.440 1.00 28.59 ? 260 PHE B O 1 ATOM 3927 C CB . PHE B 2 260 ? 36.508 84.948 29.159 1.00 26.05 ? 260 PHE B CB 1 ATOM 3928 C CG . PHE B 2 260 ? 36.044 84.047 28.060 1.00 27.03 ? 260 PHE B CG 1 ATOM 3929 C CD1 . PHE B 2 260 ? 36.954 83.294 27.351 1.00 27.88 ? 260 PHE B CD1 1 ATOM 3930 C CD2 . PHE B 2 260 ? 34.705 84.014 27.680 1.00 29.45 ? 260 PHE B CD2 1 ATOM 3931 C CE1 . PHE B 2 260 ? 36.548 82.475 26.310 1.00 29.82 ? 260 PHE B CE1 1 ATOM 3932 C CE2 . PHE B 2 260 ? 34.287 83.201 26.635 1.00 31.39 ? 260 PHE B CE2 1 ATOM 3933 C CZ . PHE B 2 260 ? 35.212 82.435 25.938 1.00 29.33 ? 260 PHE B CZ 1 ATOM 3934 N N . TYR B 2 261 ? 36.424 87.508 26.714 1.00 25.54 ? 261 TYR B N 1 ATOM 3935 C CA . TYR B 2 261 ? 35.685 88.524 25.961 1.00 24.36 ? 261 TYR B CA 1 ATOM 3936 C C . TYR B 2 261 ? 34.972 87.871 24.765 1.00 25.27 ? 261 TYR B C 1 ATOM 3937 O O . TYR B 2 261 ? 34.485 88.623 23.898 1.00 27.11 ? 261 TYR B O 1 ATOM 3938 C CB . TYR B 2 261 ? 36.640 89.667 25.563 1.00 23.15 ? 261 TYR B CB 1 ATOM 3939 C CG . TYR B 2 261 ? 37.825 89.205 24.706 1.00 22.49 ? 261 TYR B CG 1 ATOM 3940 C CD1 . TYR B 2 261 ? 39.007 88.722 25.285 1.00 21.04 ? 261 TYR B CD1 1 ATOM 3941 C CD2 . TYR B 2 261 ? 37.741 89.225 23.311 1.00 22.62 ? 261 TYR B CD2 1 ATOM 3942 C CE1 . TYR B 2 261 ? 40.068 88.268 24.509 1.00 20.53 ? 261 TYR B CE1 1 ATOM 3943 C CE2 . TYR B 2 261 ? 38.798 88.785 22.521 1.00 21.57 ? 261 TYR B CE2 1 ATOM 3944 C CZ . TYR B 2 261 ? 39.955 88.295 23.116 1.00 21.38 ? 261 TYR B CZ 1 ATOM 3945 O OH . TYR B 2 261 ? 40.971 87.856 22.301 1.00 20.04 ? 261 TYR B OH 1 HETATM 3946 C C1 . NAG C 3 . ? 55.959 74.776 3.219 1.00 56.70 ? 301 NAG A C1 1 HETATM 3947 C C2 . NAG C 3 . ? 55.566 75.076 1.784 1.00 63.79 ? 301 NAG A C2 1 HETATM 3948 C C3 . NAG C 3 . ? 56.747 75.533 0.945 1.00 65.74 ? 301 NAG A C3 1 HETATM 3949 C C4 . NAG C 3 . ? 57.484 76.653 1.618 1.00 64.21 ? 301 NAG A C4 1 HETATM 3950 C C5 . NAG C 3 . ? 57.917 76.164 2.974 1.00 62.89 ? 301 NAG A C5 1 HETATM 3951 C C6 . NAG C 3 . ? 58.665 77.269 3.685 1.00 61.22 ? 301 NAG A C6 1 HETATM 3952 C C7 . NAG C 3 . ? 53.838 73.470 1.140 1.00 69.22 ? 301 NAG A C7 1 HETATM 3953 C C8 . NAG C 3 . ? 53.602 72.074 0.665 1.00 67.36 ? 301 NAG A C8 1 HETATM 3954 N N2 . NAG C 3 . ? 55.103 73.852 1.180 1.00 67.86 ? 301 NAG A N2 1 HETATM 3955 O O3 . NAG C 3 . ? 56.309 75.989 -0.329 1.00 67.14 ? 301 NAG A O3 1 HETATM 3956 O O4 . NAG C 3 . ? 58.623 76.943 0.833 1.00 66.83 ? 301 NAG A O4 1 HETATM 3957 O O5 . NAG C 3 . ? 56.775 75.807 3.730 1.00 58.51 ? 301 NAG A O5 1 HETATM 3958 O O6 . NAG C 3 . ? 59.538 76.670 4.629 1.00 60.89 ? 301 NAG A O6 1 HETATM 3959 O O7 . NAG C 3 . ? 52.929 74.196 1.468 1.00 72.79 ? 301 NAG A O7 1 HETATM 3960 C C1 . GOL D 4 . ? 51.230 77.972 12.557 1.00 36.78 ? 302 GOL A C1 1 HETATM 3961 O O1 . GOL D 4 . ? 50.016 77.339 12.270 1.00 36.97 ? 302 GOL A O1 1 HETATM 3962 C C2 . GOL D 4 . ? 51.815 77.037 13.561 1.00 35.91 ? 302 GOL A C2 1 HETATM 3963 O O2 . GOL D 4 . ? 50.969 75.938 13.476 1.00 34.96 ? 302 GOL A O2 1 HETATM 3964 C C3 . GOL D 4 . ? 53.233 76.708 13.099 1.00 36.22 ? 302 GOL A C3 1 HETATM 3965 O O3 . GOL D 4 . ? 54.151 76.789 14.157 1.00 33.03 ? 302 GOL A O3 1 HETATM 3966 C C1 . NGA E 5 . ? 33.245 124.998 14.583 1.00 61.37 ? 301 NGA B C1 1 HETATM 3967 C C2 . NGA E 5 . ? 33.849 124.729 15.964 1.00 56.29 ? 301 NGA B C2 1 HETATM 3968 C C3 . NGA E 5 . ? 34.338 123.250 16.032 1.00 53.15 ? 301 NGA B C3 1 HETATM 3969 C C4 . NGA E 5 . ? 33.141 122.389 15.708 1.00 56.57 ? 301 NGA B C4 1 HETATM 3970 C C5 . NGA E 5 . ? 32.725 122.703 14.301 1.00 64.20 ? 301 NGA B C5 1 HETATM 3971 C C6 . NGA E 5 . ? 31.555 121.821 13.914 1.00 66.96 ? 301 NGA B C6 1 HETATM 3972 C C7 . NGA E 5 . ? 35.288 126.175 17.248 1.00 61.48 ? 301 NGA B C7 1 HETATM 3973 C C8 . NGA E 5 . ? 36.731 126.553 17.346 1.00 55.90 ? 301 NGA B C8 1 HETATM 3974 N N2 . NGA E 5 . ? 34.914 125.665 16.103 1.00 59.32 ? 301 NGA B N2 1 HETATM 3975 O O1 . NGA E 5 . ? 32.611 126.250 14.538 1.00 61.88 ? 301 NGA B O1 1 HETATM 3976 O O3 . NGA E 5 . ? 35.263 122.789 17.066 1.00 35.77 ? 301 NGA B O3 1 HETATM 3977 O O4 . NGA E 5 . ? 32.006 122.824 16.407 1.00 65.13 ? 301 NGA B O4 1 HETATM 3978 O O5 . NGA E 5 . ? 32.272 124.045 14.213 1.00 63.77 ? 301 NGA B O5 1 HETATM 3979 O O6 . NGA E 5 . ? 31.797 120.487 14.335 1.00 68.00 ? 301 NGA B O6 1 HETATM 3980 O O7 . NGA E 5 . ? 34.503 126.350 18.148 1.00 65.88 ? 301 NGA B O7 1 HETATM 3981 C C1 . GAL F 6 . ? 34.885 121.795 18.084 1.00 38.83 ? 302 GAL B C1 1 HETATM 3982 C C2 . GAL F 6 . ? 35.678 120.468 17.964 1.00 36.30 ? 302 GAL B C2 1 HETATM 3983 C C3 . GAL F 6 . ? 35.524 119.511 19.180 1.00 34.81 ? 302 GAL B C3 1 HETATM 3984 C C4 . GAL F 6 . ? 35.598 120.219 20.542 1.00 32.15 ? 302 GAL B C4 1 HETATM 3985 C C5 . GAL F 6 . ? 34.678 121.446 20.509 1.00 35.22 ? 302 GAL B C5 1 HETATM 3986 C C6 . GAL F 6 . ? 34.793 122.249 21.802 1.00 35.04 ? 302 GAL B C6 1 HETATM 3987 O O2 . GAL F 6 . ? 35.236 119.719 16.820 1.00 36.02 ? 302 GAL B O2 1 HETATM 3988 O O3 . GAL F 6 . ? 36.493 118.428 19.110 1.00 30.56 ? 302 GAL B O3 1 HETATM 3989 O O4 . GAL F 6 . ? 36.933 120.627 20.854 1.00 28.53 ? 302 GAL B O4 1 HETATM 3990 O O5 . GAL F 6 . ? 35.054 122.302 19.412 1.00 34.74 ? 302 GAL B O5 1 HETATM 3991 O O6 . GAL F 6 . ? 33.578 122.963 22.035 1.00 40.52 ? 302 GAL B O6 1 HETATM 3992 C C1 . NAG G 3 . ? 57.767 118.705 30.418 1.00 36.11 ? 303 NAG B C1 1 HETATM 3993 C C2 . NAG G 3 . ? 57.673 119.571 29.173 1.00 38.22 ? 303 NAG B C2 1 HETATM 3994 C C3 . NAG G 3 . ? 58.848 120.549 29.021 1.00 40.02 ? 303 NAG B C3 1 HETATM 3995 C C4 . NAG G 3 . ? 59.154 121.317 30.287 1.00 41.88 ? 303 NAG B C4 1 HETATM 3996 C C5 . NAG G 3 . ? 59.246 120.318 31.428 1.00 40.30 ? 303 NAG B C5 1 HETATM 3997 C C6 . NAG G 3 . ? 59.488 121.044 32.740 1.00 40.36 ? 303 NAG B C6 1 HETATM 3998 C C7 . NAG G 3 . ? 56.480 118.233 27.560 1.00 36.11 ? 303 NAG B C7 1 HETATM 3999 C C8 . NAG G 3 . ? 56.607 117.467 26.296 1.00 34.78 ? 303 NAG B C8 1 HETATM 4000 N N2 . NAG G 3 . ? 57.580 118.788 27.985 1.00 35.59 ? 303 NAG B N2 1 HETATM 4001 O O3 . NAG G 3 . ? 58.517 121.456 28.002 1.00 38.35 ? 303 NAG B O3 1 HETATM 4002 O O4 . NAG G 3 . ? 60.382 122.034 30.128 1.00 49.90 ? 303 NAG B O4 1 HETATM 4003 O O5 . NAG G 3 . ? 58.079 119.521 31.527 1.00 36.89 ? 303 NAG B O5 1 HETATM 4004 O O6 . NAG G 3 . ? 58.353 121.719 33.216 1.00 37.93 ? 303 NAG B O6 1 HETATM 4005 O O7 . NAG G 3 . ? 55.451 118.320 28.125 1.00 32.27 ? 303 NAG B O7 1 HETATM 4006 C C1 . NAG H 3 . ? 60.240 123.445 30.018 1.00 55.41 ? 304 NAG B C1 1 HETATM 4007 C C2 . NAG H 3 . ? 61.520 124.138 30.428 1.00 57.97 ? 304 NAG B C2 1 HETATM 4008 C C3 . NAG H 3 . ? 61.408 125.650 30.243 1.00 62.26 ? 304 NAG B C3 1 HETATM 4009 C C4 . NAG H 3 . ? 60.835 126.016 28.900 1.00 64.84 ? 304 NAG B C4 1 HETATM 4010 C C5 . NAG H 3 . ? 59.597 125.206 28.617 1.00 64.57 ? 304 NAG B C5 1 HETATM 4011 C C6 . NAG H 3 . ? 59.118 125.555 27.225 1.00 63.08 ? 304 NAG B C6 1 HETATM 4012 C C7 . NAG H 3 . ? 62.697 123.032 32.182 1.00 58.10 ? 304 NAG B C7 1 HETATM 4013 C C8 . NAG H 3 . ? 63.021 123.010 33.631 1.00 58.24 ? 304 NAG B C8 1 HETATM 4014 N N2 . NAG H 3 . ? 61.766 123.873 31.805 1.00 57.18 ? 304 NAG B N2 1 HETATM 4015 O O3 . NAG H 3 . ? 62.693 126.250 30.309 1.00 63.63 ? 304 NAG B O3 1 HETATM 4016 O O4 . NAG H 3 . ? 60.535 127.408 28.833 1.00 68.02 ? 304 NAG B O4 1 HETATM 4017 O O5 . NAG H 3 . ? 59.959 123.837 28.703 1.00 59.88 ? 304 NAG B O5 1 HETATM 4018 O O6 . NAG H 3 . ? 59.988 124.954 26.303 1.00 63.61 ? 304 NAG B O6 1 HETATM 4019 O O7 . NAG H 3 . ? 63.253 122.309 31.408 1.00 61.12 ? 304 NAG B O7 1 HETATM 4020 C C1 . NAG I 3 . ? 40.305 125.927 31.561 1.00 34.82 ? 305 NAG B C1 1 HETATM 4021 C C2 . NAG I 3 . ? 39.601 126.857 32.526 1.00 39.68 ? 305 NAG B C2 1 HETATM 4022 C C3 . NAG I 3 . ? 39.422 128.266 31.968 1.00 39.70 ? 305 NAG B C3 1 HETATM 4023 C C4 . NAG I 3 . ? 40.739 128.813 31.526 1.00 40.13 ? 305 NAG B C4 1 HETATM 4024 C C5 . NAG I 3 . ? 41.250 127.866 30.443 1.00 38.25 ? 305 NAG B C5 1 HETATM 4025 C C6 . NAG I 3 . ? 42.571 128.314 29.914 1.00 35.67 ? 305 NAG B C6 1 HETATM 4026 C C7 . NAG I 3 . ? 38.029 125.718 33.919 1.00 46.51 ? 305 NAG B C7 1 HETATM 4027 C C8 . NAG I 3 . ? 36.696 125.075 33.867 1.00 48.59 ? 305 NAG B C8 1 HETATM 4028 N N2 . NAG I 3 . ? 38.352 126.262 32.772 1.00 41.08 ? 305 NAG B N2 1 HETATM 4029 O O3 . NAG I 3 . ? 38.977 129.166 32.932 1.00 40.04 ? 305 NAG B O3 1 HETATM 4030 O O4 . NAG I 3 . ? 40.626 130.189 31.151 1.00 43.56 ? 305 NAG B O4 1 HETATM 4031 O O5 . NAG I 3 . ? 41.395 126.550 30.954 1.00 35.70 ? 305 NAG B O5 1 HETATM 4032 O O6 . NAG I 3 . ? 43.385 128.604 31.009 1.00 37.41 ? 305 NAG B O6 1 HETATM 4033 O O7 . NAG I 3 . ? 38.708 125.708 34.913 1.00 47.73 ? 305 NAG B O7 1 HETATM 4034 C C1 . FUC J 7 . ? 37.579 129.378 32.796 1.00 43.20 ? 306 FUC B C1 1 HETATM 4035 C C2 . FUC J 7 . ? 37.026 129.775 34.137 1.00 43.83 ? 306 FUC B C2 1 HETATM 4036 C C3 . FUC J 7 . ? 37.643 131.126 34.461 1.00 44.03 ? 306 FUC B C3 1 HETATM 4037 C C4 . FUC J 7 . ? 37.192 132.130 33.444 1.00 44.75 ? 306 FUC B C4 1 HETATM 4038 C C5 . FUC J 7 . ? 37.737 131.659 32.112 1.00 46.24 ? 306 FUC B C5 1 HETATM 4039 C C6 . FUC J 7 . ? 37.393 132.600 30.965 1.00 47.58 ? 306 FUC B C6 1 HETATM 4040 O O2 . FUC J 7 . ? 37.388 128.821 35.103 1.00 43.12 ? 306 FUC B O2 1 HETATM 4041 O O3 . FUC J 7 . ? 37.270 131.568 35.726 1.00 45.31 ? 306 FUC B O3 1 HETATM 4042 O O4 . FUC J 7 . ? 35.773 132.170 33.411 1.00 44.06 ? 306 FUC B O4 1 HETATM 4043 O O5 . FUC J 7 . ? 37.232 130.375 31.855 1.00 44.21 ? 306 FUC B O5 1 HETATM 4044 C C1 . NAG K 3 . ? 41.134 131.113 31.356 1.00 45.69 ? 307 NAG B C1 1 HETATM 4045 C C2 . NAG K 3 . ? 41.141 132.391 30.513 1.00 46.99 ? 307 NAG B C2 1 HETATM 4046 C C3 . NAG K 3 . ? 41.861 133.562 31.186 1.00 48.59 ? 307 NAG B C3 1 HETATM 4047 C C4 . NAG K 3 . ? 41.557 133.740 32.642 1.00 50.11 ? 307 NAG B C4 1 HETATM 4048 C C5 . NAG K 3 . ? 41.831 132.396 33.276 1.00 50.45 ? 307 NAG B C5 1 HETATM 4049 C C6 . NAG K 3 . ? 41.652 132.526 34.761 1.00 51.16 ? 307 NAG B C6 1 HETATM 4050 C C7 . NAG K 3 . ? 41.106 131.853 28.156 1.00 42.19 ? 307 NAG B C7 1 HETATM 4051 C C8 . NAG K 3 . ? 41.949 131.678 26.947 1.00 42.07 ? 307 NAG B C8 1 HETATM 4052 N N2 . NAG K 3 . ? 41.769 132.232 29.222 1.00 43.22 ? 307 NAG B N2 1 HETATM 4053 O O3 . NAG K 3 . ? 41.485 134.741 30.513 1.00 49.42 ? 307 NAG B O3 1 HETATM 4054 O O4 . NAG K 3 . ? 42.480 134.706 33.133 1.00 56.54 ? 307 NAG B O4 1 HETATM 4055 O O5 . NAG K 3 . ? 40.953 131.424 32.729 1.00 45.98 ? 307 NAG B O5 1 HETATM 4056 O O6 . NAG K 3 . ? 42.106 131.361 35.413 1.00 53.87 ? 307 NAG B O6 1 HETATM 4057 O O7 . NAG K 3 . ? 39.939 131.608 28.148 1.00 39.17 ? 307 NAG B O7 1 HETATM 4058 C C1 . BMA L 8 . ? 41.754 135.702 33.875 1.00 61.61 ? 308 BMA B C1 1 HETATM 4059 C C2 . BMA L 8 . ? 42.478 135.988 35.185 1.00 64.03 ? 308 BMA B C2 1 HETATM 4060 C C3 . BMA L 8 . ? 41.744 137.051 35.994 1.00 65.34 ? 308 BMA B C3 1 HETATM 4061 C C4 . BMA L 8 . ? 41.417 138.264 35.131 1.00 63.51 ? 308 BMA B C4 1 HETATM 4062 C C5 . BMA L 8 . ? 40.756 137.842 33.824 1.00 62.97 ? 308 BMA B C5 1 HETATM 4063 C C6 . BMA L 8 . ? 40.497 139.048 32.929 1.00 63.76 ? 308 BMA B C6 1 HETATM 4064 O O2 . BMA L 8 . ? 43.809 136.435 34.906 1.00 68.10 ? 308 BMA B O2 1 HETATM 4065 O O3 . BMA L 8 . ? 42.559 137.457 37.099 1.00 65.15 ? 308 BMA B O3 1 HETATM 4066 O O4 . BMA L 8 . ? 40.539 139.138 35.850 1.00 61.63 ? 308 BMA B O4 1 HETATM 4067 O O5 . BMA L 8 . ? 41.599 136.916 33.143 1.00 59.67 ? 308 BMA B O5 1 HETATM 4068 O O6 . BMA L 8 . ? 41.673 139.336 32.164 1.00 65.87 ? 308 BMA B O6 1 HETATM 4069 C C1B . XYP M 9 . ? 45.194 135.673 34.574 1.00 77.10 ? 309 XYP B C1B 1 HETATM 4070 C C2B . XYP M 9 . ? 46.164 135.916 33.372 1.00 78.62 ? 309 XYP B C2B 1 HETATM 4071 C C3B . XYP M 9 . ? 47.373 134.897 33.314 1.00 83.36 ? 309 XYP B C3B 1 HETATM 4072 C C4B . XYP M 9 . ? 48.054 134.772 34.686 1.00 86.02 ? 309 XYP B C4B 1 HETATM 4073 C C5B . XYP M 9 . ? 47.034 134.747 35.837 1.00 84.87 ? 309 XYP B C5B 1 HETATM 4074 O O2B . XYP M 9 . ? 45.470 135.893 32.093 1.00 71.90 ? 309 XYP B O2B 1 HETATM 4075 O O3B . XYP M 9 . ? 48.330 135.334 32.340 1.00 80.85 ? 309 XYP B O3B 1 HETATM 4076 O O4B . XYP M 9 . ? 48.860 133.585 34.677 1.00 92.07 ? 309 XYP B O4B 1 HETATM 4077 O O5B . XYP M 9 . ? 46.087 135.813 35.699 1.00 82.70 ? 309 XYP B O5B 1 HETATM 4078 C C1 . MAN N 10 . ? 42.459 140.507 31.217 1.00 72.52 ? 310 MAN B C1 1 HETATM 4079 C C2 . MAN N 10 . ? 43.765 140.886 30.528 1.00 74.11 ? 310 MAN B C2 1 HETATM 4080 C C3 . MAN N 10 . ? 44.638 141.738 31.443 1.00 75.46 ? 310 MAN B C3 1 HETATM 4081 C C4 . MAN N 10 . ? 43.839 142.888 32.043 1.00 74.30 ? 310 MAN B C4 1 HETATM 4082 C C5 . MAN N 10 . ? 42.529 142.389 32.641 1.00 72.30 ? 310 MAN B C5 1 HETATM 4083 C C6 . MAN N 10 . ? 41.695 143.549 33.174 1.00 70.91 ? 310 MAN B C6 1 HETATM 4084 O O2 . MAN N 10 . ? 43.479 141.613 29.329 1.00 74.92 ? 310 MAN B O2 1 HETATM 4085 O O3 . MAN N 10 . ? 45.742 142.261 30.697 1.00 78.81 ? 310 MAN B O3 1 HETATM 4086 O O4 . MAN N 10 . ? 44.615 143.528 33.062 1.00 73.99 ? 310 MAN B O4 1 HETATM 4087 O O5 . MAN N 10 . ? 41.787 141.690 31.644 1.00 73.14 ? 310 MAN B O5 1 HETATM 4088 O O6 . MAN N 10 . ? 41.204 143.223 34.479 1.00 69.31 ? 310 MAN B O6 1 HETATM 4089 O O . HOH O 11 . ? 42.584 100.653 18.080 1.00 29.56 ? 401 HOH A O 1 HETATM 4090 O O . HOH O 11 . ? 49.876 88.212 28.719 1.00 32.40 ? 402 HOH A O 1 HETATM 4091 O O . HOH O 11 . ? 59.940 74.809 11.014 1.00 48.98 ? 403 HOH A O 1 HETATM 4092 O O . HOH O 11 . ? 62.851 60.754 22.806 1.00 45.51 ? 404 HOH A O 1 HETATM 4093 O O . HOH O 11 . ? 63.997 90.443 22.882 1.00 44.48 ? 405 HOH A O 1 HETATM 4094 O O . HOH O 11 . ? 68.752 60.341 20.055 1.00 42.66 ? 406 HOH A O 1 HETATM 4095 O O . HOH O 11 . ? 47.807 58.150 31.040 1.00 49.68 ? 407 HOH A O 1 HETATM 4096 O O . HOH O 11 . ? 41.728 89.701 12.103 1.00 33.71 ? 408 HOH A O 1 HETATM 4097 O O . HOH O 11 . ? 34.435 66.176 23.471 1.00 46.93 ? 409 HOH A O 1 HETATM 4098 O O . HOH O 11 . ? 33.929 82.858 21.957 1.00 36.75 ? 410 HOH A O 1 HETATM 4099 O O . HOH O 11 . ? 52.767 77.003 4.762 1.00 44.76 ? 411 HOH A O 1 HETATM 4100 O O . HOH O 11 . ? 62.571 91.528 20.763 1.00 30.14 ? 412 HOH A O 1 HETATM 4101 O O . HOH O 11 . ? 54.394 56.229 21.464 1.00 35.37 ? 413 HOH A O 1 HETATM 4102 O O . HOH O 11 . ? 46.058 103.574 14.745 1.00 36.73 ? 414 HOH A O 1 HETATM 4103 O O . HOH O 11 . ? 51.158 69.634 34.214 1.00 41.79 ? 415 HOH A O 1 HETATM 4104 O O . HOH O 11 . ? 47.187 96.769 28.520 1.00 33.65 ? 416 HOH A O 1 HETATM 4105 O O . HOH O 11 . ? 33.852 85.470 17.590 1.00 25.62 ? 417 HOH A O 1 HETATM 4106 O O . HOH O 11 . ? 61.324 83.253 18.797 1.00 21.53 ? 418 HOH A O 1 HETATM 4107 O O . HOH O 11 . ? 62.271 76.127 26.050 1.00 29.29 ? 419 HOH A O 1 HETATM 4108 O O . HOH O 11 . ? 49.268 81.232 15.900 1.00 20.45 ? 420 HOH A O 1 HETATM 4109 O O . HOH O 11 . ? 34.113 92.321 10.402 1.00 33.62 ? 421 HOH A O 1 HETATM 4110 O O . HOH O 11 . ? 61.736 84.774 14.986 1.00 48.12 ? 422 HOH A O 1 HETATM 4111 O O . HOH O 11 . ? 59.951 79.734 32.628 1.00 36.26 ? 423 HOH A O 1 HETATM 4112 O O . HOH O 11 . ? 47.094 77.704 32.644 1.00 33.40 ? 424 HOH A O 1 HETATM 4113 O O . HOH O 11 . ? 42.730 100.059 27.938 1.00 25.09 ? 425 HOH A O 1 HETATM 4114 O O . HOH O 11 . ? 42.124 71.570 -0.529 1.00 41.60 ? 426 HOH A O 1 HETATM 4115 O O . HOH O 11 . ? 41.479 67.178 38.518 1.00 52.13 ? 427 HOH A O 1 HETATM 4116 O O . HOH O 11 . ? 30.290 75.539 26.085 1.00 39.46 ? 428 HOH A O 1 HETATM 4117 O O . HOH O 11 . ? 52.589 103.412 11.109 1.00 40.68 ? 429 HOH A O 1 HETATM 4118 O O . HOH O 11 . ? 58.603 67.953 28.587 1.00 40.65 ? 430 HOH A O 1 HETATM 4119 O O . HOH O 11 . ? 66.200 75.377 24.510 1.00 37.45 ? 431 HOH A O 1 HETATM 4120 O O . HOH O 11 . ? 61.292 83.688 31.474 1.00 41.96 ? 432 HOH A O 1 HETATM 4121 O O . HOH O 11 . ? 59.258 93.986 31.618 1.00 50.88 ? 433 HOH A O 1 HETATM 4122 O O . HOH O 11 . ? 32.575 83.605 14.906 1.00 33.43 ? 434 HOH A O 1 HETATM 4123 O O . HOH O 11 . ? 71.992 61.627 15.279 1.00 34.71 ? 435 HOH A O 1 HETATM 4124 O O . HOH O 11 . ? 42.892 96.738 12.847 1.00 25.65 ? 436 HOH A O 1 HETATM 4125 O O . HOH O 11 . ? 65.804 84.838 24.799 1.00 34.30 ? 437 HOH A O 1 HETATM 4126 O O . HOH O 11 . ? 33.359 79.197 19.305 1.00 42.53 ? 438 HOH A O 1 HETATM 4127 O O . HOH O 11 . ? 59.235 76.295 -1.711 1.00 73.28 ? 439 HOH A O 1 HETATM 4128 O O . HOH O 11 . ? 55.802 98.585 24.210 1.00 38.69 ? 440 HOH A O 1 HETATM 4129 O O . HOH O 11 . ? 61.839 106.061 20.520 1.00 41.18 ? 441 HOH A O 1 HETATM 4130 O O . HOH O 11 . ? 39.049 73.667 14.776 1.00 21.08 ? 442 HOH A O 1 HETATM 4131 O O . HOH O 11 . ? 41.982 77.084 4.171 1.00 34.20 ? 443 HOH A O 1 HETATM 4132 O O . HOH O 11 . ? 53.590 78.848 15.826 1.00 24.74 ? 444 HOH A O 1 HETATM 4133 O O . HOH O 11 . ? 50.461 87.053 12.249 1.00 25.19 ? 445 HOH A O 1 HETATM 4134 O O . HOH O 11 . ? 58.934 64.844 32.605 1.00 60.81 ? 446 HOH A O 1 HETATM 4135 O O . HOH O 11 . ? 46.756 91.787 10.859 1.00 37.84 ? 447 HOH A O 1 HETATM 4136 O O . HOH O 11 . ? 57.684 91.954 26.671 1.00 22.83 ? 448 HOH A O 1 HETATM 4137 O O . HOH O 11 . ? 40.268 87.778 19.636 1.00 20.22 ? 449 HOH A O 1 HETATM 4138 O O . HOH O 11 . ? 54.491 101.631 27.472 1.00 36.84 ? 450 HOH A O 1 HETATM 4139 O O . HOH O 11 . ? 67.518 78.906 14.838 1.00 37.04 ? 451 HOH A O 1 HETATM 4140 O O . HOH O 11 . ? 53.500 82.957 29.604 1.00 31.39 ? 452 HOH A O 1 HETATM 4141 O O . HOH O 11 . ? 64.334 81.468 32.363 1.00 44.07 ? 453 HOH A O 1 HETATM 4142 O O . HOH O 11 . ? 52.969 55.293 8.837 1.00 58.64 ? 454 HOH A O 1 HETATM 4143 O O . HOH O 11 . ? 46.465 64.447 32.233 1.00 39.09 ? 455 HOH A O 1 HETATM 4144 O O . HOH O 11 . ? 50.210 54.958 8.172 1.00 50.15 ? 456 HOH A O 1 HETATM 4145 O O . HOH O 11 . ? 48.043 94.100 11.010 1.00 30.55 ? 457 HOH A O 1 HETATM 4146 O O . HOH O 11 . ? 61.697 79.731 23.795 1.00 25.51 ? 458 HOH A O 1 HETATM 4147 O O . HOH O 11 . ? 56.899 95.912 24.812 1.00 29.15 ? 459 HOH A O 1 HETATM 4148 O O . HOH O 11 . ? 47.807 62.950 5.769 1.00 40.50 ? 460 HOH A O 1 HETATM 4149 O O . HOH O 11 . ? 37.386 67.143 15.399 1.00 28.72 ? 461 HOH A O 1 HETATM 4150 O O . HOH O 11 . ? 34.197 76.697 24.489 1.00 26.18 ? 462 HOH A O 1 HETATM 4151 O O . HOH O 11 . ? 64.034 86.116 23.236 1.00 30.02 ? 463 HOH A O 1 HETATM 4152 O O . HOH O 11 . ? 55.232 77.313 11.037 1.00 46.57 ? 464 HOH A O 1 HETATM 4153 O O . HOH O 11 . ? 56.228 58.223 22.287 1.00 40.01 ? 465 HOH A O 1 HETATM 4154 O O . HOH O 11 . ? 47.231 87.546 31.914 1.00 41.95 ? 466 HOH A O 1 HETATM 4155 O O . HOH O 11 . ? 42.147 65.071 7.962 1.00 31.18 ? 467 HOH A O 1 HETATM 4156 O O . HOH O 11 . ? 56.966 98.128 31.904 1.00 42.04 ? 468 HOH A O 1 HETATM 4157 O O . HOH O 11 . ? 45.035 54.552 20.218 1.00 44.92 ? 469 HOH A O 1 HETATM 4158 O O . HOH O 11 . ? 64.085 84.475 31.070 1.00 46.55 ? 470 HOH A O 1 HETATM 4159 O O . HOH O 11 . ? 48.458 68.564 34.296 1.00 27.33 ? 471 HOH A O 1 HETATM 4160 O O . HOH O 11 . ? 52.411 50.804 16.428 1.00 44.15 ? 472 HOH A O 1 HETATM 4161 O O . HOH O 11 . ? 51.318 76.420 16.984 1.00 28.06 ? 473 HOH A O 1 HETATM 4162 O O . HOH O 11 . ? 47.602 98.955 10.212 1.00 42.20 ? 474 HOH A O 1 HETATM 4163 O O . HOH O 11 . ? 59.089 59.821 4.206 1.00 48.56 ? 475 HOH A O 1 HETATM 4164 O O . HOH O 11 . ? 52.219 73.594 14.994 1.00 38.87 ? 476 HOH A O 1 HETATM 4165 O O . HOH O 11 . ? 42.816 90.440 9.111 1.00 40.54 ? 477 HOH A O 1 HETATM 4166 O O . HOH O 11 . ? 40.674 63.764 14.924 1.00 43.64 ? 478 HOH A O 1 HETATM 4167 O O . HOH O 11 . ? 34.838 68.729 25.469 1.00 36.96 ? 479 HOH A O 1 HETATM 4168 O O . HOH O 11 . ? 59.817 94.262 23.382 1.00 30.80 ? 480 HOH A O 1 HETATM 4169 O O . HOH O 11 . ? 32.221 74.666 24.506 1.00 31.06 ? 481 HOH A O 1 HETATM 4170 O O . HOH O 11 . ? 42.756 72.514 41.938 1.00 61.05 ? 482 HOH A O 1 HETATM 4171 O O . HOH O 11 . ? 44.962 73.927 37.801 1.00 32.91 ? 483 HOH A O 1 HETATM 4172 O O . HOH O 11 . ? 38.708 92.757 10.464 1.00 22.28 ? 484 HOH A O 1 HETATM 4173 O O . HOH O 11 . ? 68.184 82.932 26.852 1.00 44.16 ? 485 HOH A O 1 HETATM 4174 O O . HOH O 11 . ? 51.568 54.077 23.474 1.00 34.15 ? 486 HOH A O 1 HETATM 4175 O O . HOH O 11 . ? 56.405 90.142 33.212 1.00 51.91 ? 487 HOH A O 1 HETATM 4176 O O . HOH O 11 . ? 48.892 83.899 10.042 1.00 51.22 ? 488 HOH A O 1 HETATM 4177 O O . HOH O 11 . ? 57.466 74.738 14.357 1.00 33.90 ? 489 HOH A O 1 HETATM 4178 O O . HOH O 11 . ? 27.526 87.463 14.717 1.00 57.41 ? 490 HOH A O 1 HETATM 4179 O O . HOH O 11 . ? 39.677 74.390 40.907 1.00 40.39 ? 491 HOH A O 1 HETATM 4180 O O . HOH O 11 . ? 34.148 68.241 10.456 1.00 54.05 ? 492 HOH A O 1 HETATM 4181 O O . HOH O 11 . ? 64.108 56.117 9.586 1.00 44.56 ? 493 HOH A O 1 HETATM 4182 O O . HOH O 11 . ? 59.168 104.966 23.090 1.00 37.70 ? 494 HOH A O 1 HETATM 4183 O O . HOH O 11 . ? 31.116 76.291 18.560 1.00 43.22 ? 495 HOH A O 1 HETATM 4184 O O . HOH O 11 . ? 44.629 77.283 3.375 1.00 30.54 ? 496 HOH A O 1 HETATM 4185 O O . HOH O 11 . ? 41.958 52.281 27.989 1.00 50.48 ? 497 HOH A O 1 HETATM 4186 O O . HOH O 11 . ? 29.378 68.350 22.596 1.00 38.18 ? 498 HOH A O 1 HETATM 4187 O O . HOH O 11 . ? 44.263 91.961 11.643 1.00 28.93 ? 499 HOH A O 1 HETATM 4188 O O . HOH O 11 . ? 52.573 79.658 33.120 1.00 29.85 ? 500 HOH A O 1 HETATM 4189 O O . HOH O 11 . ? 31.121 77.554 31.361 1.00 59.64 ? 501 HOH A O 1 HETATM 4190 O O . HOH O 11 . ? 57.352 93.208 24.136 1.00 28.57 ? 502 HOH A O 1 HETATM 4191 O O . HOH O 11 . ? 26.608 68.725 27.610 1.00 56.95 ? 503 HOH A O 1 HETATM 4192 O O . HOH O 11 . ? 65.498 81.938 15.692 1.00 42.43 ? 504 HOH A O 1 HETATM 4193 O O . HOH O 11 . ? 63.800 76.550 13.898 1.00 33.27 ? 505 HOH A O 1 HETATM 4194 O O . HOH O 11 . ? 67.704 61.516 9.877 1.00 57.15 ? 506 HOH A O 1 HETATM 4195 O O . HOH O 11 . ? 46.417 53.722 9.817 1.00 52.22 ? 507 HOH A O 1 HETATM 4196 O O . HOH O 11 . ? 46.823 55.993 5.899 1.00 40.01 ? 508 HOH A O 1 HETATM 4197 O O . HOH O 11 . ? 72.958 71.928 18.346 1.00 35.57 ? 509 HOH A O 1 HETATM 4198 O O . HOH O 11 . ? 53.709 59.953 29.267 1.00 52.77 ? 510 HOH A O 1 HETATM 4199 O O . HOH O 11 . ? 61.765 67.882 26.213 1.00 29.04 ? 511 HOH A O 1 HETATM 4200 O O . HOH O 11 . ? 67.193 83.414 22.775 1.00 38.57 ? 512 HOH A O 1 HETATM 4201 O O . HOH O 11 . ? 38.758 70.515 37.286 1.00 35.39 ? 513 HOH A O 1 HETATM 4202 O O . HOH O 11 . ? 46.839 88.360 8.752 1.00 52.53 ? 514 HOH A O 1 HETATM 4203 O O . HOH O 11 . ? 65.968 69.651 21.785 1.00 36.63 ? 515 HOH A O 1 HETATM 4204 O O . HOH O 11 . ? 63.962 62.198 20.732 1.00 35.04 ? 516 HOH A O 1 HETATM 4205 O O . HOH O 11 . ? 64.959 90.504 28.909 1.00 37.74 ? 517 HOH A O 1 HETATM 4206 O O . HOH O 11 . ? 61.221 67.123 6.979 1.00 45.37 ? 518 HOH A O 1 HETATM 4207 O O . HOH O 11 . ? 51.742 95.380 8.916 1.00 50.31 ? 519 HOH A O 1 HETATM 4208 O O . HOH O 11 . ? 31.855 79.096 16.456 1.00 48.75 ? 520 HOH A O 1 HETATM 4209 O O . HOH O 11 . ? 50.198 80.912 32.424 1.00 30.32 ? 521 HOH A O 1 HETATM 4210 O O . HOH O 11 . ? 49.769 52.083 12.322 1.00 52.36 ? 522 HOH A O 1 HETATM 4211 O O . HOH O 11 . ? 42.777 86.622 7.482 1.00 35.98 ? 523 HOH A O 1 HETATM 4212 O O . HOH O 11 . ? 57.808 76.004 11.918 1.00 44.63 ? 524 HOH A O 1 HETATM 4213 O O . HOH O 11 . ? 57.783 77.236 6.992 1.00 42.18 ? 525 HOH A O 1 HETATM 4214 O O . HOH O 11 . ? 51.971 62.799 4.151 1.00 47.40 ? 526 HOH A O 1 HETATM 4215 O O . HOH O 11 . ? 36.679 69.716 35.133 1.00 35.53 ? 527 HOH A O 1 HETATM 4216 O O . HOH O 11 . ? 65.956 60.501 19.679 1.00 47.56 ? 528 HOH A O 1 HETATM 4217 O O . HOH O 11 . ? 64.444 67.103 9.652 1.00 38.25 ? 529 HOH A O 1 HETATM 4218 O O . HOH O 11 . ? 30.515 93.760 23.121 1.00 45.52 ? 530 HOH A O 1 HETATM 4219 O O . HOH O 11 . ? 46.073 69.800 38.330 1.00 46.59 ? 531 HOH A O 1 HETATM 4220 O O . HOH O 11 . ? 49.043 50.735 25.848 1.00 66.07 ? 532 HOH A O 1 HETATM 4221 O O . HOH O 11 . ? 61.652 77.338 0.718 1.00 52.72 ? 533 HOH A O 1 HETATM 4222 O O . HOH O 11 . ? 52.775 66.593 33.219 1.00 48.17 ? 534 HOH A O 1 HETATM 4223 O O . HOH O 11 . ? 50.502 84.007 13.536 1.00 25.85 ? 535 HOH A O 1 HETATM 4224 O O . HOH O 11 . ? 61.986 80.575 14.501 1.00 61.38 ? 536 HOH A O 1 HETATM 4225 O O . HOH O 11 . ? 57.825 67.465 32.636 1.00 60.33 ? 537 HOH A O 1 HETATM 4226 O O . HOH O 11 . ? 57.294 53.722 9.348 1.00 46.24 ? 538 HOH A O 1 HETATM 4227 O O . HOH O 11 . ? 33.229 79.320 25.046 1.00 40.66 ? 539 HOH A O 1 HETATM 4228 O O . HOH O 11 . ? 68.482 59.963 12.166 1.00 58.98 ? 540 HOH A O 1 HETATM 4229 O O . HOH O 11 . ? 52.400 86.882 29.661 1.00 31.52 ? 541 HOH A O 1 HETATM 4230 O O . HOH O 11 . ? 35.869 81.902 19.319 1.00 10.93 ? 542 HOH A O 1 HETATM 4231 O O . HOH O 11 . ? 59.524 73.582 13.335 1.00 38.90 ? 543 HOH A O 1 HETATM 4232 O O . HOH O 11 . ? 40.250 55.862 1.933 1.00 66.96 ? 544 HOH A O 1 HETATM 4233 O O . HOH O 11 . ? 64.486 67.091 22.610 1.00 43.37 ? 545 HOH A O 1 HETATM 4234 O O . HOH O 11 . ? 37.186 59.569 15.464 1.00 47.68 ? 546 HOH A O 1 HETATM 4235 O O . HOH O 11 . ? 72.465 78.546 16.842 1.00 59.70 ? 547 HOH A O 1 HETATM 4236 O O . HOH O 11 . ? 31.756 66.192 24.436 1.00 64.42 ? 548 HOH A O 1 HETATM 4237 O O . HOH O 11 . ? 56.648 100.921 25.738 1.00 41.14 ? 549 HOH A O 1 HETATM 4238 O O . HOH O 11 . ? 70.294 78.715 14.933 1.00 49.26 ? 550 HOH A O 1 HETATM 4239 O O . HOH O 11 . ? 30.313 80.145 30.407 1.00 52.80 ? 551 HOH A O 1 HETATM 4240 O O . HOH O 11 . ? 68.207 73.358 11.060 1.00 38.46 ? 552 HOH A O 1 HETATM 4241 O O . HOH O 11 . ? 40.963 74.991 2.349 1.00 48.48 ? 553 HOH A O 1 HETATM 4242 O O . HOH O 11 . ? 51.049 83.296 31.059 1.00 41.04 ? 554 HOH A O 1 HETATM 4243 O O . HOH O 11 . ? 55.515 94.520 33.013 1.00 51.32 ? 555 HOH A O 1 HETATM 4244 O O . HOH O 11 . ? 43.973 68.403 39.158 1.00 65.82 ? 556 HOH A O 1 HETATM 4245 O O . HOH O 11 . ? 53.510 56.938 6.457 1.00 57.79 ? 557 HOH A O 1 HETATM 4246 O O . HOH O 11 . ? 62.744 82.940 16.464 1.00 38.91 ? 558 HOH A O 1 HETATM 4247 O O . HOH O 11 . ? 36.933 72.078 38.617 1.00 45.20 ? 559 HOH A O 1 HETATM 4248 O O . HOH O 11 . ? 61.978 94.217 21.606 1.00 41.59 ? 560 HOH A O 1 HETATM 4249 O O . HOH O 11 . ? 48.187 68.316 37.184 1.00 46.79 ? 561 HOH A O 1 HETATM 4250 O O . HOH O 11 . ? 42.263 53.199 12.130 1.00 46.81 ? 562 HOH A O 1 HETATM 4251 O O . HOH O 11 . ? 63.563 96.001 24.710 1.00 62.42 ? 563 HOH A O 1 HETATM 4252 O O . HOH O 11 . ? 33.339 83.335 19.029 1.00 33.86 ? 564 HOH A O 1 HETATM 4253 O O . HOH O 11 . ? 54.066 80.870 13.835 1.00 37.70 ? 565 HOH A O 1 HETATM 4254 O O . HOH O 11 . ? 50.279 88.245 9.834 1.00 48.43 ? 566 HOH A O 1 HETATM 4255 O O . HOH O 11 . ? 31.628 81.819 17.270 1.00 54.07 ? 567 HOH A O 1 HETATM 4256 O O . HOH O 11 . ? 40.463 90.689 9.847 1.00 28.93 ? 568 HOH A O 1 HETATM 4257 O O . HOH O 11 . ? 63.444 50.744 15.446 1.00 53.23 ? 569 HOH A O 1 HETATM 4258 O O . HOH O 11 . ? 62.522 76.249 11.144 1.00 58.29 ? 570 HOH A O 1 HETATM 4259 O O . HOH O 11 . ? 63.624 73.721 26.619 1.00 51.11 ? 571 HOH A O 1 HETATM 4260 O O . HOH O 11 . ? 47.360 50.532 12.486 1.00 61.15 ? 572 HOH A O 1 HETATM 4261 O O . HOH O 11 . ? 29.367 87.181 24.285 1.00 56.48 ? 573 HOH A O 1 HETATM 4262 O O . HOH O 11 . ? 63.045 70.067 27.544 1.00 51.68 ? 574 HOH A O 1 HETATM 4263 O O . HOH O 11 . ? 52.657 50.044 19.144 1.00 51.12 ? 575 HOH A O 1 HETATM 4264 O O . HOH O 11 . ? 60.472 83.460 12.640 1.00 56.25 ? 576 HOH A O 1 HETATM 4265 O O . HOH O 11 . ? 28.530 81.202 13.890 1.00 67.52 ? 577 HOH A O 1 HETATM 4266 O O . HOH P 11 . ? 46.040 100.945 31.716 1.00 27.53 ? 401 HOH B O 1 HETATM 4267 O O . HOH P 11 . ? 42.718 100.418 60.009 1.00 23.71 ? 402 HOH B O 1 HETATM 4268 O O . HOH P 11 . ? 44.231 128.841 21.774 1.00 38.99 ? 403 HOH B O 1 HETATM 4269 O O . HOH P 11 . ? 34.863 105.709 24.880 1.00 32.95 ? 404 HOH B O 1 HETATM 4270 O O . HOH P 11 . ? 50.737 125.068 38.050 1.00 40.85 ? 405 HOH B O 1 HETATM 4271 O O . HOH P 11 . ? 34.049 95.066 54.854 1.00 32.48 ? 406 HOH B O 1 HETATM 4272 O O . HOH P 11 . ? 44.312 91.400 51.896 1.00 39.41 ? 407 HOH B O 1 HETATM 4273 O O . HOH P 11 . ? 24.081 89.084 41.027 1.00 32.46 ? 408 HOH B O 1 HETATM 4274 O O . HOH P 11 . ? 33.969 124.905 20.215 1.00 40.42 ? 409 HOH B O 1 HETATM 4275 O O . HOH P 11 . ? 50.052 95.885 42.142 1.00 35.81 ? 410 HOH B O 1 HETATM 4276 O O . HOH P 11 . ? 31.670 111.979 31.794 1.00 30.86 ? 411 HOH B O 1 HETATM 4277 O O . HOH P 11 . ? 34.927 120.172 34.198 1.00 53.26 ? 412 HOH B O 1 HETATM 4278 O O . HOH P 11 . ? 48.665 106.998 36.686 1.00 31.98 ? 413 HOH B O 1 HETATM 4279 O O . HOH P 11 . ? 41.713 104.915 23.194 1.00 22.51 ? 414 HOH B O 1 HETATM 4280 O O . HOH P 11 . ? 33.917 75.645 39.876 1.00 36.23 ? 415 HOH B O 1 HETATM 4281 O O . HOH P 11 . ? 39.533 111.652 15.919 1.00 25.50 ? 416 HOH B O 1 HETATM 4282 O O . HOH P 11 . ? 32.702 103.082 49.420 1.00 44.78 ? 417 HOH B O 1 HETATM 4283 O O . HOH P 11 . ? 22.542 99.431 39.438 1.00 47.13 ? 418 HOH B O 1 HETATM 4284 O O . HOH P 11 . ? 31.690 76.433 38.484 1.00 35.77 ? 419 HOH B O 1 HETATM 4285 O O . HOH P 11 . ? 42.585 124.738 34.212 1.00 35.33 ? 420 HOH B O 1 HETATM 4286 O O . HOH P 11 . ? 30.181 117.827 24.922 1.00 45.69 ? 421 HOH B O 1 HETATM 4287 O O . HOH P 11 . ? 32.787 118.800 16.414 1.00 51.48 ? 422 HOH B O 1 HETATM 4288 O O . HOH P 11 . ? 60.419 103.682 15.613 1.00 36.69 ? 423 HOH B O 1 HETATM 4289 O O . HOH P 11 . ? 41.497 99.110 53.173 1.00 23.46 ? 424 HOH B O 1 HETATM 4290 O O . HOH P 11 . ? 55.961 120.088 33.556 1.00 32.45 ? 425 HOH B O 1 HETATM 4291 O O . HOH P 11 . ? 31.958 106.490 44.894 1.00 32.01 ? 426 HOH B O 1 HETATM 4292 O O . HOH P 11 . ? 44.475 106.899 49.009 1.00 50.01 ? 427 HOH B O 1 HETATM 4293 O O . HOH P 11 . ? 54.403 112.567 39.448 1.00 32.71 ? 428 HOH B O 1 HETATM 4294 O O . HOH P 11 . ? 48.868 106.541 45.161 1.00 40.70 ? 429 HOH B O 1 HETATM 4295 O O . HOH P 11 . ? 32.662 87.663 35.131 1.00 21.84 ? 430 HOH B O 1 HETATM 4296 O O . HOH P 11 . ? 51.118 91.234 39.969 1.00 30.53 ? 431 HOH B O 1 HETATM 4297 O O . HOH P 11 . ? 36.210 106.164 38.387 1.00 28.63 ? 432 HOH B O 1 HETATM 4298 O O . HOH P 11 . ? 23.903 93.088 41.470 1.00 35.42 ? 433 HOH B O 1 HETATM 4299 O O . HOH P 11 . ? 34.156 91.035 47.672 1.00 22.31 ? 434 HOH B O 1 HETATM 4300 O O . HOH P 11 . ? 36.973 100.282 38.587 1.00 20.73 ? 435 HOH B O 1 HETATM 4301 O O . HOH P 11 . ? 51.023 121.495 35.661 1.00 32.24 ? 436 HOH B O 1 HETATM 4302 O O . HOH P 11 . ? 41.964 120.928 37.551 1.00 41.20 ? 437 HOH B O 1 HETATM 4303 O O . HOH P 11 . ? 29.171 84.449 32.379 1.00 30.79 ? 438 HOH B O 1 HETATM 4304 O O . HOH P 11 . ? 37.177 124.036 28.523 1.00 34.01 ? 439 HOH B O 1 HETATM 4305 O O . HOH P 11 . ? 39.816 115.596 41.093 1.00 50.56 ? 440 HOH B O 1 HETATM 4306 O O . HOH P 11 . ? 35.332 104.009 45.694 1.00 34.22 ? 441 HOH B O 1 HETATM 4307 O O . HOH P 11 . ? 52.712 128.484 15.346 1.00 53.52 ? 442 HOH B O 1 HETATM 4308 O O . HOH P 11 . ? 52.933 94.237 36.833 1.00 51.57 ? 443 HOH B O 1 HETATM 4309 O O . HOH P 11 . ? 27.797 79.614 41.709 1.00 43.00 ? 444 HOH B O 1 HETATM 4310 O O . HOH P 11 . ? 51.950 103.791 35.671 1.00 34.79 ? 445 HOH B O 1 HETATM 4311 O O . HOH P 11 . ? 34.133 92.011 24.058 1.00 43.21 ? 446 HOH B O 1 HETATM 4312 O O . HOH P 11 . ? 35.245 97.504 51.622 1.00 27.25 ? 447 HOH B O 1 HETATM 4313 O O . HOH P 11 . ? 50.458 87.011 42.472 1.00 26.63 ? 448 HOH B O 1 HETATM 4314 O O . HOH P 11 . ? 32.913 120.534 32.003 1.00 46.50 ? 449 HOH B O 1 HETATM 4315 O O . HOH P 11 . ? 29.931 115.542 30.156 1.00 35.33 ? 450 HOH B O 1 HETATM 4316 O O . HOH P 11 . ? 50.547 97.368 38.222 1.00 37.08 ? 451 HOH B O 1 HETATM 4317 O O . HOH P 11 . ? 32.531 86.783 27.522 1.00 44.17 ? 452 HOH B O 1 HETATM 4318 O O . HOH P 11 . ? 40.792 78.651 53.222 1.00 26.49 ? 453 HOH B O 1 HETATM 4319 O O . HOH P 11 . ? 43.417 98.873 55.083 1.00 30.30 ? 454 HOH B O 1 HETATM 4320 O O . HOH P 11 . ? 47.711 104.226 27.079 1.00 30.03 ? 455 HOH B O 1 HETATM 4321 O O . HOH P 11 . ? 35.083 109.159 36.288 1.00 23.40 ? 456 HOH B O 1 HETATM 4322 O O . HOH P 11 . ? 21.246 91.858 43.865 1.00 44.23 ? 457 HOH B O 1 HETATM 4323 O O . HOH P 11 . ? 32.714 85.579 54.244 1.00 28.70 ? 458 HOH B O 1 HETATM 4324 O O . HOH P 11 . ? 43.535 121.998 29.639 1.00 29.08 ? 459 HOH B O 1 HETATM 4325 O O . HOH P 11 . ? 47.784 120.654 41.612 1.00 47.29 ? 460 HOH B O 1 HETATM 4326 O O . HOH P 11 . ? 39.608 78.983 34.429 1.00 27.46 ? 461 HOH B O 1 HETATM 4327 O O . HOH P 11 . ? 47.870 113.972 14.554 1.00 27.43 ? 462 HOH B O 1 HETATM 4328 O O . HOH P 11 . ? 34.242 104.267 53.699 1.00 50.12 ? 463 HOH B O 1 HETATM 4329 O O . HOH P 11 . ? 30.466 84.981 28.000 1.00 43.08 ? 464 HOH B O 1 HETATM 4330 O O . HOH P 11 . ? 47.289 74.707 41.561 1.00 45.18 ? 465 HOH B O 1 HETATM 4331 O O . HOH P 11 . ? 48.556 109.933 33.117 1.00 22.85 ? 466 HOH B O 1 HETATM 4332 O O . HOH P 11 . ? 31.883 92.977 47.759 1.00 20.50 ? 467 HOH B O 1 HETATM 4333 O O . HOH P 11 . ? 38.275 78.397 54.124 1.00 29.35 ? 468 HOH B O 1 HETATM 4334 O O . HOH P 11 . ? 42.313 118.278 35.211 1.00 26.92 ? 469 HOH B O 1 HETATM 4335 O O . HOH P 11 . ? 45.992 94.950 30.302 1.00 34.17 ? 470 HOH B O 1 HETATM 4336 O O . HOH P 11 . ? 45.915 84.305 34.653 1.00 32.98 ? 471 HOH B O 1 HETATM 4337 O O . HOH P 11 . ? 45.281 89.587 41.067 1.00 20.35 ? 472 HOH B O 1 HETATM 4338 O O . HOH P 11 . ? 57.242 103.711 9.445 1.00 46.10 ? 473 HOH B O 1 HETATM 4339 O O . HOH P 11 . ? 41.775 100.357 49.318 1.00 27.20 ? 474 HOH B O 1 HETATM 4340 O O . HOH P 11 . ? 46.017 114.063 12.312 1.00 34.96 ? 475 HOH B O 1 HETATM 4341 O O . HOH P 11 . ? 35.660 84.398 48.370 1.00 24.90 ? 476 HOH B O 1 HETATM 4342 O O . HOH P 11 . ? 30.587 88.873 56.320 1.00 40.66 ? 477 HOH B O 1 HETATM 4343 O O . HOH P 11 . ? 32.223 78.318 36.513 1.00 31.01 ? 478 HOH B O 1 HETATM 4344 O O . HOH P 11 . ? 45.716 90.025 34.143 1.00 19.75 ? 479 HOH B O 1 HETATM 4345 O O . HOH P 11 . ? 42.378 124.808 22.642 1.00 31.22 ? 480 HOH B O 1 HETATM 4346 O O . HOH P 11 . ? 54.954 92.151 34.190 1.00 43.67 ? 481 HOH B O 1 HETATM 4347 O O . HOH P 11 . ? 44.807 115.971 40.620 1.00 51.93 ? 482 HOH B O 1 HETATM 4348 O O . HOH P 11 . ? 59.616 109.736 12.552 1.00 46.09 ? 483 HOH B O 1 HETATM 4349 O O . HOH P 11 . ? 33.214 112.535 14.459 1.00 42.53 ? 484 HOH B O 1 HETATM 4350 O O . HOH P 11 . ? 47.774 114.573 42.135 1.00 38.26 ? 485 HOH B O 1 HETATM 4351 O O . HOH P 11 . ? 42.263 123.314 13.328 1.00 46.53 ? 486 HOH B O 1 HETATM 4352 O O . HOH P 11 . ? 41.882 111.414 21.189 1.00 22.61 ? 487 HOH B O 1 HETATM 4353 O O . HOH P 11 . ? 29.219 96.925 49.728 1.00 30.63 ? 488 HOH B O 1 HETATM 4354 O O . HOH P 11 . ? 42.296 86.506 27.589 1.00 27.54 ? 489 HOH B O 1 HETATM 4355 O O . HOH P 11 . ? 56.036 100.817 32.046 1.00 40.36 ? 490 HOH B O 1 HETATM 4356 O O . HOH P 11 . ? 52.220 115.891 13.307 1.00 43.33 ? 491 HOH B O 1 HETATM 4357 O O . HOH P 11 . ? 37.595 70.602 45.322 1.00 54.40 ? 492 HOH B O 1 HETATM 4358 O O . HOH P 11 . ? 45.777 102.670 41.287 1.00 25.16 ? 493 HOH B O 1 HETATM 4359 O O . HOH P 11 . ? 31.477 110.299 36.193 1.00 46.20 ? 494 HOH B O 1 HETATM 4360 O O . HOH P 11 . ? 43.395 101.965 29.787 1.00 23.53 ? 495 HOH B O 1 HETATM 4361 O O . HOH P 11 . ? 55.408 114.594 41.070 1.00 49.54 ? 496 HOH B O 1 HETATM 4362 O O . HOH P 11 . ? 41.742 109.549 32.450 1.00 22.65 ? 497 HOH B O 1 HETATM 4363 O O . HOH P 11 . ? 28.074 93.162 36.203 1.00 26.83 ? 498 HOH B O 1 HETATM 4364 O O . HOH P 11 . ? 45.580 116.536 13.754 1.00 28.25 ? 499 HOH B O 1 HETATM 4365 O O . HOH P 11 . ? 26.027 81.154 38.910 1.00 39.69 ? 500 HOH B O 1 HETATM 4366 O O . HOH P 11 . ? 44.819 96.764 32.170 1.00 25.82 ? 501 HOH B O 1 HETATM 4367 O O . HOH P 11 . ? 33.655 109.322 24.293 1.00 33.34 ? 502 HOH B O 1 HETATM 4368 O O . HOH P 11 . ? 40.247 96.740 49.233 1.00 20.81 ? 503 HOH B O 1 HETATM 4369 O O . HOH P 11 . ? 37.333 107.424 36.292 1.00 24.26 ? 504 HOH B O 1 HETATM 4370 O O . HOH P 11 . ? 55.653 98.505 12.717 1.00 44.57 ? 505 HOH B O 1 HETATM 4371 O O . HOH P 11 . ? 48.741 117.159 41.737 1.00 31.79 ? 506 HOH B O 1 HETATM 4372 O O . HOH P 11 . ? 32.855 114.382 19.257 1.00 26.02 ? 507 HOH B O 1 HETATM 4373 O O . HOH P 11 . ? 38.422 117.486 11.783 1.00 39.32 ? 508 HOH B O 1 HETATM 4374 O O . HOH P 11 . ? 33.105 94.805 23.894 1.00 33.07 ? 509 HOH B O 1 HETATM 4375 O O . HOH P 11 . ? 39.026 106.366 52.304 1.00 58.79 ? 510 HOH B O 1 HETATM 4376 O O . HOH P 11 . ? 44.969 101.190 10.156 1.00 40.44 ? 511 HOH B O 1 HETATM 4377 O O . HOH P 11 . ? 51.822 93.630 45.887 1.00 34.64 ? 512 HOH B O 1 HETATM 4378 O O . HOH P 11 . ? 26.605 78.879 30.473 1.00 47.54 ? 513 HOH B O 1 HETATM 4379 O O . HOH P 11 . ? 33.008 83.286 30.915 1.00 35.42 ? 514 HOH B O 1 HETATM 4380 O O . HOH P 11 . ? 36.015 102.974 19.218 1.00 30.77 ? 515 HOH B O 1 HETATM 4381 O O . HOH P 11 . ? 40.470 120.952 35.220 1.00 38.07 ? 516 HOH B O 1 HETATM 4382 O O . HOH P 11 . ? 42.894 108.531 14.619 1.00 38.71 ? 517 HOH B O 1 HETATM 4383 O O . HOH P 11 . ? 41.148 76.920 40.791 1.00 31.51 ? 518 HOH B O 1 HETATM 4384 O O . HOH P 11 . ? 38.103 122.356 33.566 1.00 39.37 ? 519 HOH B O 1 HETATM 4385 O O . HOH P 11 . ? 37.049 105.910 46.090 1.00 38.61 ? 520 HOH B O 1 HETATM 4386 O O . HOH P 11 . ? 22.567 88.534 36.274 1.00 36.35 ? 521 HOH B O 1 HETATM 4387 O O . HOH P 11 . ? 43.277 76.136 42.625 1.00 40.17 ? 522 HOH B O 1 HETATM 4388 O O . HOH P 11 . ? 40.505 104.646 50.216 1.00 39.05 ? 523 HOH B O 1 HETATM 4389 O O . HOH P 11 . ? 30.448 88.058 51.674 1.00 29.63 ? 524 HOH B O 1 HETATM 4390 O O . HOH P 11 . ? 40.859 97.909 33.957 1.00 36.14 ? 525 HOH B O 1 HETATM 4391 O O . HOH P 11 . ? 42.106 82.625 35.719 1.00 40.55 ? 526 HOH B O 1 HETATM 4392 O O . HOH P 11 . ? 51.413 123.588 42.141 1.00 55.37 ? 527 HOH B O 1 HETATM 4393 O O . HOH P 11 . ? 53.467 95.699 32.081 1.00 45.89 ? 528 HOH B O 1 HETATM 4394 O O . HOH P 11 . ? 31.145 98.941 24.568 1.00 55.63 ? 529 HOH B O 1 HETATM 4395 O O . HOH P 11 . ? 49.379 84.795 41.121 1.00 29.82 ? 530 HOH B O 1 HETATM 4396 O O . HOH P 11 . ? 36.481 128.846 25.908 1.00 32.16 ? 531 HOH B O 1 HETATM 4397 O O . HOH P 11 . ? 34.265 107.281 18.114 1.00 47.72 ? 532 HOH B O 1 HETATM 4398 O O . HOH P 11 . ? 46.742 130.162 23.445 1.00 53.02 ? 533 HOH B O 1 HETATM 4399 O O . HOH P 11 . ? 40.481 98.584 28.614 1.00 30.33 ? 534 HOH B O 1 HETATM 4400 O O . HOH P 11 . ? 35.115 78.971 33.424 1.00 30.37 ? 535 HOH B O 1 HETATM 4401 O O . HOH P 11 . ? 57.158 115.609 23.661 1.00 36.38 ? 536 HOH B O 1 HETATM 4402 O O . HOH P 11 . ? 36.400 103.372 27.411 1.00 24.78 ? 537 HOH B O 1 HETATM 4403 O O . HOH P 11 . ? 25.422 92.688 31.118 1.00 40.14 ? 538 HOH B O 1 HETATM 4404 O O . HOH P 11 . ? 40.719 80.544 36.374 1.00 34.76 ? 539 HOH B O 1 HETATM 4405 O O . HOH P 11 . ? 54.734 116.167 22.461 1.00 29.08 ? 540 HOH B O 1 HETATM 4406 O O . HOH P 11 . ? 54.793 107.766 39.983 1.00 42.64 ? 541 HOH B O 1 HETATM 4407 O O . HOH P 11 . ? 31.146 109.889 21.197 1.00 45.59 ? 542 HOH B O 1 HETATM 4408 O O . HOH P 11 . ? 59.569 116.872 23.601 1.00 40.51 ? 543 HOH B O 1 HETATM 4409 O O . HOH P 11 . ? 33.380 115.150 37.650 1.00 41.03 ? 544 HOH B O 1 HETATM 4410 O O . HOH P 11 . ? 28.555 104.340 45.573 1.00 34.45 ? 545 HOH B O 1 HETATM 4411 O O . HOH P 11 . ? 42.494 81.485 39.725 1.00 31.45 ? 546 HOH B O 1 HETATM 4412 O O . HOH P 11 . ? 33.471 110.160 38.224 1.00 29.95 ? 547 HOH B O 1 HETATM 4413 O O . HOH P 11 . ? 31.521 90.556 49.282 1.00 30.79 ? 548 HOH B O 1 HETATM 4414 O O . HOH P 11 . ? 41.067 84.253 41.359 1.00 21.70 ? 549 HOH B O 1 HETATM 4415 O O . HOH P 11 . ? 36.260 105.734 55.544 1.00 54.63 ? 550 HOH B O 1 HETATM 4416 O O . HOH P 11 . ? 24.922 101.918 31.893 1.00 37.76 ? 551 HOH B O 1 HETATM 4417 O O . HOH P 11 . ? 53.140 108.208 43.662 1.00 49.92 ? 552 HOH B O 1 HETATM 4418 O O . HOH P 11 . ? 32.439 118.808 36.349 1.00 60.63 ? 553 HOH B O 1 HETATM 4419 O O . HOH P 11 . ? 34.072 84.529 45.936 1.00 25.23 ? 554 HOH B O 1 HETATM 4420 O O . HOH P 11 . ? 50.880 121.404 32.947 1.00 29.99 ? 555 HOH B O 1 HETATM 4421 O O . HOH P 11 . ? 54.371 118.411 13.548 1.00 40.11 ? 556 HOH B O 1 HETATM 4422 O O . HOH P 11 . ? 44.285 78.511 45.699 1.00 30.09 ? 557 HOH B O 1 HETATM 4423 O O . HOH P 11 . ? 45.756 127.012 28.858 1.00 44.81 ? 558 HOH B O 1 HETATM 4424 O O . HOH P 11 . ? 44.540 120.977 40.351 1.00 52.53 ? 559 HOH B O 1 HETATM 4425 O O . HOH P 11 . ? 38.112 78.153 46.674 1.00 34.09 ? 560 HOH B O 1 HETATM 4426 O O . HOH P 11 . ? 39.046 104.507 56.819 1.00 39.01 ? 561 HOH B O 1 HETATM 4427 O O . HOH P 11 . ? 26.006 94.137 34.314 1.00 32.11 ? 562 HOH B O 1 HETATM 4428 O O . HOH P 11 . ? 40.969 101.842 52.732 1.00 35.59 ? 563 HOH B O 1 HETATM 4429 O O . HOH P 11 . ? 42.088 108.704 44.870 1.00 30.40 ? 564 HOH B O 1 HETATM 4430 O O . HOH P 11 . ? 48.931 106.151 11.329 1.00 30.70 ? 565 HOH B O 1 HETATM 4431 O O . HOH P 11 . ? 46.781 126.499 33.366 1.00 35.86 ? 566 HOH B O 1 HETATM 4432 O O . HOH P 11 . ? 45.066 117.935 11.405 1.00 56.89 ? 567 HOH B O 1 HETATM 4433 O O . HOH P 11 . ? 60.544 115.734 29.420 1.00 48.15 ? 568 HOH B O 1 HETATM 4434 O O . HOH P 11 . ? 53.137 100.500 34.336 1.00 41.69 ? 569 HOH B O 1 HETATM 4435 O O . HOH P 11 . ? 46.075 101.623 29.458 1.00 27.21 ? 570 HOH B O 1 HETATM 4436 O O . HOH P 11 . ? 31.940 89.497 26.670 1.00 43.85 ? 571 HOH B O 1 HETATM 4437 O O . HOH P 11 . ? 49.603 116.320 13.986 1.00 30.68 ? 572 HOH B O 1 HETATM 4438 O O . HOH P 11 . ? 52.171 119.849 44.285 1.00 54.96 ? 573 HOH B O 1 HETATM 4439 O O . HOH P 11 . ? 21.620 83.307 31.148 1.00 49.85 ? 574 HOH B O 1 HETATM 4440 O O . HOH P 11 . ? 26.052 85.496 25.496 1.00 67.07 ? 575 HOH B O 1 HETATM 4441 O O . HOH P 11 . ? 55.804 109.369 21.389 1.00 28.31 ? 576 HOH B O 1 HETATM 4442 O O . HOH P 11 . ? 20.085 96.034 38.110 1.00 61.55 ? 577 HOH B O 1 HETATM 4443 O O . HOH P 11 . ? 53.071 112.162 43.699 1.00 49.32 ? 578 HOH B O 1 HETATM 4444 O O . HOH P 11 . ? 34.493 125.021 28.095 1.00 32.23 ? 579 HOH B O 1 HETATM 4445 O O . HOH P 11 . ? 24.231 85.066 42.966 1.00 56.25 ? 580 HOH B O 1 HETATM 4446 O O . HOH P 11 . ? 35.416 116.274 40.119 1.00 53.07 ? 581 HOH B O 1 HETATM 4447 O O . HOH P 11 . ? 50.810 128.364 34.667 1.00 65.79 ? 582 HOH B O 1 HETATM 4448 O O . HOH P 11 . ? 32.219 113.840 16.592 1.00 54.59 ? 583 HOH B O 1 HETATM 4449 O O . HOH P 11 . ? 29.502 116.853 22.370 1.00 45.50 ? 584 HOH B O 1 HETATM 4450 O O . HOH P 11 . ? 44.095 129.442 17.155 1.00 42.40 ? 585 HOH B O 1 HETATM 4451 O O . HOH P 11 . ? 22.896 89.322 43.926 1.00 58.05 ? 586 HOH B O 1 HETATM 4452 O O . HOH P 11 . ? 54.950 106.924 32.878 1.00 43.43 ? 587 HOH B O 1 HETATM 4453 O O . HOH P 11 . ? 28.792 97.347 24.530 1.00 54.78 ? 588 HOH B O 1 HETATM 4454 O O . HOH P 11 . ? 29.503 118.643 29.889 1.00 52.89 ? 589 HOH B O 1 HETATM 4455 O O . HOH P 11 . ? 42.483 127.303 23.788 1.00 47.04 ? 590 HOH B O 1 HETATM 4456 O O . HOH P 11 . ? 61.488 117.027 20.341 1.00 56.94 ? 591 HOH B O 1 HETATM 4457 O O . HOH P 11 . ? 40.434 109.658 14.345 1.00 39.26 ? 592 HOH B O 1 HETATM 4458 O O . HOH P 11 . ? 64.183 112.650 22.021 1.00 62.21 ? 593 HOH B O 1 HETATM 4459 O O . HOH P 11 . ? 44.286 85.413 51.097 1.00 40.70 ? 594 HOH B O 1 HETATM 4460 O O . HOH P 11 . ? 23.563 104.627 39.518 1.00 47.47 ? 595 HOH B O 1 HETATM 4461 O O . HOH P 11 . ? 43.944 128.076 26.691 1.00 60.20 ? 596 HOH B O 1 HETATM 4462 O O . HOH P 11 . ? 25.682 100.545 27.563 1.00 52.24 ? 597 HOH B O 1 HETATM 4463 O O . HOH P 11 . ? 33.003 96.822 52.795 1.00 31.35 ? 598 HOH B O 1 HETATM 4464 O O . HOH P 11 . ? 42.228 97.898 50.808 1.00 24.77 ? 599 HOH B O 1 HETATM 4465 O O . HOH P 11 . ? 44.198 118.041 42.276 1.00 56.18 ? 600 HOH B O 1 HETATM 4466 O O . HOH P 11 . ? 52.209 97.706 42.120 1.00 49.74 ? 601 HOH B O 1 HETATM 4467 O O . HOH P 11 . ? 45.102 73.146 40.887 1.00 50.55 ? 602 HOH B O 1 HETATM 4468 O O . HOH P 11 . ? 39.877 129.976 23.462 1.00 45.48 ? 603 HOH B O 1 HETATM 4469 O O . HOH P 11 . ? 51.621 93.621 41.355 1.00 45.02 ? 604 HOH B O 1 HETATM 4470 O O . HOH P 11 . ? 48.976 114.681 44.745 1.00 58.39 ? 605 HOH B O 1 HETATM 4471 O O . HOH P 11 . ? 34.559 73.086 38.947 1.00 58.14 ? 606 HOH B O 1 HETATM 4472 O O . HOH P 11 . ? 53.041 84.244 34.000 1.00 53.74 ? 607 HOH B O 1 HETATM 4473 O O . HOH P 11 . ? 51.375 113.504 45.405 1.00 51.90 ? 608 HOH B O 1 HETATM 4474 O O . HOH P 11 . ? 55.993 110.149 39.851 1.00 52.70 ? 609 HOH B O 1 HETATM 4475 O O . HOH P 11 . ? 30.261 110.777 29.810 1.00 51.73 ? 610 HOH B O 1 HETATM 4476 O O . HOH P 11 . ? 33.159 104.918 47.289 1.00 38.51 ? 611 HOH B O 1 HETATM 4477 O O . HOH P 11 . ? 53.465 127.178 12.907 1.00 66.27 ? 612 HOH B O 1 HETATM 4478 O O . HOH P 11 . ? 32.787 96.312 57.132 1.00 50.19 ? 613 HOH B O 1 HETATM 4479 O O . HOH P 11 . ? 42.385 76.620 45.058 1.00 40.54 ? 614 HOH B O 1 HETATM 4480 O O . HOH P 11 . ? 37.942 114.628 43.073 1.00 61.68 ? 615 HOH B O 1 HETATM 4481 O O . HOH P 11 . ? 26.017 90.366 27.571 1.00 53.25 ? 616 HOH B O 1 HETATM 4482 O O . HOH P 11 . ? 52.163 88.622 40.940 1.00 39.20 ? 617 HOH B O 1 HETATM 4483 O O . HOH P 11 . ? 52.949 100.989 38.931 1.00 48.00 ? 618 HOH B O 1 HETATM 4484 O O . HOH P 11 . ? 40.867 120.891 12.506 1.00 53.08 ? 619 HOH B O 1 HETATM 4485 O O . HOH P 11 . ? 24.288 86.030 21.741 1.00 63.48 ? 620 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 1 NAG NAG A . D 4 GOL 1 302 2 GOL GOL A . E 5 NGA 1 301 1 NGA NGA B . F 6 GAL 2 302 2 GAL GAL B . G 3 NAG 1 303 1 NAG NAG B . H 3 NAG 2 304 2 NAG NAG B . I 3 NAG 1 305 1 NAG NAG B . J 7 FUC 2 306 2 FUC FUC B . K 3 NAG 1 307 3 NAG NAG B . L 8 BMA 2 308 4 BMA BMA B . M 9 XYP 1 309 5 XYP XYP B . N 10 MAN 1 310 6 MAN MAN B . O 11 HOH 1 401 372 HOH HOH A . O 11 HOH 2 402 376 HOH HOH A . O 11 HOH 3 403 433 HOH HOH A . O 11 HOH 4 404 409 HOH HOH A . O 11 HOH 5 405 125 HOH HOH A . O 11 HOH 6 406 94 HOH HOH A . O 11 HOH 7 407 312 HOH HOH A . O 11 HOH 8 408 200 HOH HOH A . O 11 HOH 9 409 115 HOH HOH A . O 11 HOH 10 410 155 HOH HOH A . O 11 HOH 11 411 97 HOH HOH A . O 11 HOH 12 412 411 HOH HOH A . O 11 HOH 13 413 417 HOH HOH A . O 11 HOH 14 414 225 HOH HOH A . O 11 HOH 15 415 410 HOH HOH A . O 11 HOH 16 416 167 HOH HOH A . O 11 HOH 17 417 25 HOH HOH A . O 11 HOH 18 418 16 HOH HOH A . O 11 HOH 19 419 140 HOH HOH A . O 11 HOH 20 420 37 HOH HOH A . O 11 HOH 21 421 141 HOH HOH A . O 11 HOH 22 422 425 HOH HOH A . O 11 HOH 23 423 63 HOH HOH A . O 11 HOH 24 424 124 HOH HOH A . O 11 HOH 25 425 51 HOH HOH A . O 11 HOH 26 426 149 HOH HOH A . O 11 HOH 27 427 237 HOH HOH A . O 11 HOH 28 428 208 HOH HOH A . O 11 HOH 29 429 443 HOH HOH A . O 11 HOH 30 430 168 HOH HOH A . O 11 HOH 31 431 170 HOH HOH A . O 11 HOH 32 432 232 HOH HOH A . O 11 HOH 33 433 147 HOH HOH A . O 11 HOH 34 434 50 HOH HOH A . O 11 HOH 35 435 184 HOH HOH A . O 11 HOH 36 436 13 HOH HOH A . O 11 HOH 37 437 395 HOH HOH A . O 11 HOH 38 438 444 HOH HOH A . O 11 HOH 39 439 252 HOH HOH A . O 11 HOH 40 440 199 HOH HOH A . O 11 HOH 41 441 137 HOH HOH A . O 11 HOH 42 442 5 HOH HOH A . O 11 HOH 43 443 401 HOH HOH A . O 11 HOH 44 444 42 HOH HOH A . O 11 HOH 45 445 35 HOH HOH A . O 11 HOH 46 446 429 HOH HOH A . O 11 HOH 47 447 285 HOH HOH A . O 11 HOH 48 448 89 HOH HOH A . O 11 HOH 49 449 362 HOH HOH A . O 11 HOH 50 450 121 HOH HOH A . O 11 HOH 51 451 14 HOH HOH A . O 11 HOH 52 452 139 HOH HOH A . O 11 HOH 53 453 423 HOH HOH A . O 11 HOH 54 454 297 HOH HOH A . O 11 HOH 55 455 256 HOH HOH A . O 11 HOH 56 456 113 HOH HOH A . O 11 HOH 57 457 136 HOH HOH A . O 11 HOH 58 458 6 HOH HOH A . O 11 HOH 59 459 95 HOH HOH A . O 11 HOH 60 460 404 HOH HOH A . O 11 HOH 61 461 143 HOH HOH A . O 11 HOH 62 462 61 HOH HOH A . O 11 HOH 63 463 108 HOH HOH A . O 11 HOH 64 464 99 HOH HOH A . O 11 HOH 65 465 214 HOH HOH A . O 11 HOH 66 466 398 HOH HOH A . O 11 HOH 67 467 389 HOH HOH A . O 11 HOH 68 468 123 HOH HOH A . O 11 HOH 69 469 22 HOH HOH A . O 11 HOH 70 470 138 HOH HOH A . O 11 HOH 71 471 8 HOH HOH A . O 11 HOH 72 472 203 HOH HOH A . O 11 HOH 73 473 24 HOH HOH A . O 11 HOH 74 474 413 HOH HOH A . O 11 HOH 75 475 243 HOH HOH A . O 11 HOH 76 476 202 HOH HOH A . O 11 HOH 77 477 305 HOH HOH A . O 11 HOH 78 478 317 HOH HOH A . O 11 HOH 79 479 90 HOH HOH A . O 11 HOH 80 480 49 HOH HOH A . O 11 HOH 81 481 71 HOH HOH A . O 11 HOH 82 482 450 HOH HOH A . O 11 HOH 83 483 80 HOH HOH A . O 11 HOH 84 484 54 HOH HOH A . O 11 HOH 85 485 222 HOH HOH A . O 11 HOH 86 486 64 HOH HOH A . O 11 HOH 87 487 309 HOH HOH A . O 11 HOH 88 488 291 HOH HOH A . O 11 HOH 89 489 159 HOH HOH A . O 11 HOH 90 490 272 HOH HOH A . O 11 HOH 91 491 83 HOH HOH A . O 11 HOH 92 492 224 HOH HOH A . O 11 HOH 93 493 180 HOH HOH A . O 11 HOH 94 494 87 HOH HOH A . O 11 HOH 95 495 85 HOH HOH A . O 11 HOH 96 496 152 HOH HOH A . O 11 HOH 97 497 437 HOH HOH A . O 11 HOH 98 498 32 HOH HOH A . O 11 HOH 99 499 96 HOH HOH A . O 11 HOH 100 500 10 HOH HOH A . O 11 HOH 101 501 445 HOH HOH A . O 11 HOH 102 502 191 HOH HOH A . O 11 HOH 103 503 192 HOH HOH A . O 11 HOH 104 504 88 HOH HOH A . O 11 HOH 105 505 100 HOH HOH A . O 11 HOH 106 506 183 HOH HOH A . O 11 HOH 107 507 314 HOH HOH A . O 11 HOH 108 508 75 HOH HOH A . O 11 HOH 109 509 58 HOH HOH A . O 11 HOH 110 510 463 HOH HOH A . O 11 HOH 111 511 45 HOH HOH A . O 11 HOH 112 512 12 HOH HOH A . O 11 HOH 113 513 21 HOH HOH A . O 11 HOH 114 514 268 HOH HOH A . O 11 HOH 115 515 460 HOH HOH A . O 11 HOH 116 516 27 HOH HOH A . O 11 HOH 117 517 109 HOH HOH A . O 11 HOH 118 518 248 HOH HOH A . O 11 HOH 119 519 277 HOH HOH A . O 11 HOH 120 520 274 HOH HOH A . O 11 HOH 121 521 387 HOH HOH A . O 11 HOH 122 522 206 HOH HOH A . O 11 HOH 123 523 499 HOH HOH A . O 11 HOH 124 524 41 HOH HOH A . O 11 HOH 125 525 74 HOH HOH A . O 11 HOH 126 526 279 HOH HOH A . O 11 HOH 127 527 105 HOH HOH A . O 11 HOH 128 528 187 HOH HOH A . O 11 HOH 129 529 86 HOH HOH A . O 11 HOH 130 530 236 HOH HOH A . O 11 HOH 131 531 228 HOH HOH A . O 11 HOH 132 532 48 HOH HOH A . O 11 HOH 133 533 494 HOH HOH A . O 11 HOH 134 534 46 HOH HOH A . O 11 HOH 135 535 26 HOH HOH A . O 11 HOH 136 536 343 HOH HOH A . O 11 HOH 137 537 479 HOH HOH A . O 11 HOH 138 538 238 HOH HOH A . O 11 HOH 139 539 76 HOH HOH A . O 11 HOH 140 540 490 HOH HOH A . O 11 HOH 141 541 57 HOH HOH A . O 11 HOH 142 542 356 HOH HOH A . O 11 HOH 143 543 341 HOH HOH A . O 11 HOH 144 544 320 HOH HOH A . O 11 HOH 145 545 70 HOH HOH A . O 11 HOH 146 546 323 HOH HOH A . O 11 HOH 147 547 247 HOH HOH A . O 11 HOH 148 548 276 HOH HOH A . O 11 HOH 149 549 333 HOH HOH A . O 11 HOH 150 550 447 HOH HOH A . O 11 HOH 151 551 482 HOH HOH A . O 11 HOH 152 552 379 HOH HOH A . O 11 HOH 153 553 332 HOH HOH A . O 11 HOH 154 554 273 HOH HOH A . O 11 HOH 155 555 334 HOH HOH A . O 11 HOH 156 556 342 HOH HOH A . O 11 HOH 157 557 345 HOH HOH A . O 11 HOH 158 558 117 HOH HOH A . O 11 HOH 159 559 497 HOH HOH A . O 11 HOH 160 560 286 HOH HOH A . O 11 HOH 161 561 215 HOH HOH A . O 11 HOH 162 562 226 HOH HOH A . O 11 HOH 163 563 351 HOH HOH A . O 11 HOH 164 564 145 HOH HOH A . O 11 HOH 165 565 102 HOH HOH A . O 11 HOH 166 566 163 HOH HOH A . O 11 HOH 167 567 169 HOH HOH A . O 11 HOH 168 568 153 HOH HOH A . O 11 HOH 169 569 495 HOH HOH A . O 11 HOH 170 570 179 HOH HOH A . O 11 HOH 171 571 157 HOH HOH A . O 11 HOH 172 572 327 HOH HOH A . O 11 HOH 173 573 484 HOH HOH A . O 11 HOH 174 574 331 HOH HOH A . O 11 HOH 175 575 229 HOH HOH A . O 11 HOH 176 576 440 HOH HOH A . O 11 HOH 177 577 347 HOH HOH A . P 11 HOH 1 401 369 HOH HOH B . P 11 HOH 2 402 36 HOH HOH B . P 11 HOH 3 403 176 HOH HOH B . P 11 HOH 4 404 126 HOH HOH B . P 11 HOH 5 405 431 HOH HOH B . P 11 HOH 6 406 337 HOH HOH B . P 11 HOH 7 407 348 HOH HOH B . P 11 HOH 8 408 392 HOH HOH B . P 11 HOH 9 409 388 HOH HOH B . P 11 HOH 10 410 422 HOH HOH B . P 11 HOH 11 411 110 HOH HOH B . P 11 HOH 12 412 432 HOH HOH B . P 11 HOH 13 413 363 HOH HOH B . P 11 HOH 14 414 1 HOH HOH B . P 11 HOH 15 415 164 HOH HOH B . P 11 HOH 16 416 20 HOH HOH B . P 11 HOH 17 417 406 HOH HOH B . P 11 HOH 18 418 253 HOH HOH B . P 11 HOH 19 419 118 HOH HOH B . P 11 HOH 20 420 30 HOH HOH B . P 11 HOH 21 421 174 HOH HOH B . P 11 HOH 22 422 189 HOH HOH B . P 11 HOH 23 423 421 HOH HOH B . P 11 HOH 24 424 355 HOH HOH B . P 11 HOH 25 425 116 HOH HOH B . P 11 HOH 26 426 158 HOH HOH B . P 11 HOH 27 427 280 HOH HOH B . P 11 HOH 28 428 60 HOH HOH B . P 11 HOH 29 429 196 HOH HOH B . P 11 HOH 30 430 430 HOH HOH B . P 11 HOH 31 431 112 HOH HOH B . P 11 HOH 32 432 361 HOH HOH B . P 11 HOH 33 433 93 HOH HOH B . P 11 HOH 34 434 375 HOH HOH B . P 11 HOH 35 435 3 HOH HOH B . P 11 HOH 36 436 373 HOH HOH B . P 11 HOH 37 437 59 HOH HOH B . P 11 HOH 38 438 186 HOH HOH B . P 11 HOH 39 439 193 HOH HOH B . P 11 HOH 40 440 134 HOH HOH B . P 11 HOH 41 441 172 HOH HOH B . P 11 HOH 42 442 185 HOH HOH B . P 11 HOH 43 443 446 HOH HOH B . P 11 HOH 44 444 197 HOH HOH B . P 11 HOH 45 445 39 HOH HOH B . P 11 HOH 46 446 427 HOH HOH B . P 11 HOH 47 447 385 HOH HOH B . P 11 HOH 48 448 101 HOH HOH B . P 11 HOH 49 449 251 HOH HOH B . P 11 HOH 50 450 130 HOH HOH B . P 11 HOH 51 451 204 HOH HOH B . P 11 HOH 52 452 9 HOH HOH B . P 11 HOH 53 453 366 HOH HOH B . P 11 HOH 54 454 339 HOH HOH B . P 11 HOH 55 455 15 HOH HOH B . P 11 HOH 56 456 40 HOH HOH B . P 11 HOH 57 457 78 HOH HOH B . P 11 HOH 58 458 381 HOH HOH B . P 11 HOH 59 459 368 HOH HOH B . P 11 HOH 60 460 122 HOH HOH B . P 11 HOH 61 461 43 HOH HOH B . P 11 HOH 62 462 77 HOH HOH B . P 11 HOH 63 463 465 HOH HOH B . P 11 HOH 64 464 471 HOH HOH B . P 11 HOH 65 465 458 HOH HOH B . P 11 HOH 66 466 359 HOH HOH B . P 11 HOH 67 467 370 HOH HOH B . P 11 HOH 68 468 367 HOH HOH B . P 11 HOH 69 469 38 HOH HOH B . P 11 HOH 70 470 428 HOH HOH B . P 11 HOH 71 471 73 HOH HOH B . P 11 HOH 72 472 2 HOH HOH B . P 11 HOH 73 473 321 HOH HOH B . P 11 HOH 74 474 390 HOH HOH B . P 11 HOH 75 475 182 HOH HOH B . P 11 HOH 76 476 377 HOH HOH B . P 11 HOH 77 477 265 HOH HOH B . P 11 HOH 78 478 66 HOH HOH B . P 11 HOH 79 479 11 HOH HOH B . P 11 HOH 80 480 18 HOH HOH B . P 11 HOH 81 481 295 HOH HOH B . P 11 HOH 82 482 135 HOH HOH B . P 11 HOH 83 483 442 HOH HOH B . P 11 HOH 84 484 146 HOH HOH B . P 11 HOH 85 485 403 HOH HOH B . P 11 HOH 86 486 454 HOH HOH B . P 11 HOH 87 487 4 HOH HOH B . P 11 HOH 88 488 405 HOH HOH B . P 11 HOH 89 489 56 HOH HOH B . P 11 HOH 90 490 234 HOH HOH B . P 11 HOH 91 491 133 HOH HOH B . P 11 HOH 92 492 311 HOH HOH B . P 11 HOH 93 493 364 HOH HOH B . P 11 HOH 94 494 142 HOH HOH B . P 11 HOH 95 495 52 HOH HOH B . P 11 HOH 96 496 474 HOH HOH B . P 11 HOH 97 497 358 HOH HOH B . P 11 HOH 98 498 67 HOH HOH B . P 11 HOH 99 499 92 HOH HOH B . P 11 HOH 100 500 261 HOH HOH B . P 11 HOH 101 501 106 HOH HOH B . P 11 HOH 102 502 23 HOH HOH B . P 11 HOH 103 503 374 HOH HOH B . P 11 HOH 104 504 360 HOH HOH B . P 11 HOH 105 505 328 HOH HOH B . P 11 HOH 106 506 393 HOH HOH B . P 11 HOH 107 507 17 HOH HOH B . P 11 HOH 108 508 235 HOH HOH B . P 11 HOH 109 509 47 HOH HOH B . P 11 HOH 110 510 306 HOH HOH B . P 11 HOH 111 511 219 HOH HOH B . P 11 HOH 112 512 396 HOH HOH B . P 11 HOH 113 513 154 HOH HOH B . P 11 HOH 114 514 190 HOH HOH B . P 11 HOH 115 515 62 HOH HOH B . P 11 HOH 116 516 435 HOH HOH B . P 11 HOH 117 517 416 HOH HOH B . P 11 HOH 118 518 382 HOH HOH B . P 11 HOH 119 519 91 HOH HOH B . P 11 HOH 120 520 310 HOH HOH B . P 11 HOH 121 521 111 HOH HOH B . P 11 HOH 122 522 175 HOH HOH B . P 11 HOH 123 523 69 HOH HOH B . P 11 HOH 124 524 400 HOH HOH B . P 11 HOH 125 525 161 HOH HOH B . P 11 HOH 126 526 19 HOH HOH B . P 11 HOH 127 527 269 HOH HOH B . P 11 HOH 128 528 408 HOH HOH B . P 11 HOH 129 529 254 HOH HOH B . P 11 HOH 130 530 84 HOH HOH B . P 11 HOH 131 531 127 HOH HOH B . P 11 HOH 132 532 194 HOH HOH B . P 11 HOH 133 533 131 HOH HOH B . P 11 HOH 134 534 223 HOH HOH B . P 11 HOH 135 535 240 HOH HOH B . P 11 HOH 136 536 103 HOH HOH B . P 11 HOH 137 537 72 HOH HOH B . P 11 HOH 138 538 211 HOH HOH B . P 11 HOH 139 539 407 HOH HOH B . P 11 HOH 140 540 114 HOH HOH B . P 11 HOH 141 541 414 HOH HOH B . P 11 HOH 142 542 120 HOH HOH B . P 11 HOH 143 543 128 HOH HOH B . P 11 HOH 144 544 207 HOH HOH B . P 11 HOH 145 545 7 HOH HOH B . P 11 HOH 146 546 148 HOH HOH B . P 11 HOH 147 547 55 HOH HOH B . P 11 HOH 148 548 384 HOH HOH B . P 11 HOH 149 549 44 HOH HOH B . P 11 HOH 150 550 453 HOH HOH B . P 11 HOH 151 551 31 HOH HOH B . P 11 HOH 152 552 188 HOH HOH B . P 11 HOH 153 553 326 HOH HOH B . P 11 HOH 154 554 378 HOH HOH B . P 11 HOH 155 555 365 HOH HOH B . P 11 HOH 156 556 68 HOH HOH B . P 11 HOH 157 557 218 HOH HOH B . P 11 HOH 158 558 209 HOH HOH B . P 11 HOH 159 559 438 HOH HOH B . P 11 HOH 160 560 383 HOH HOH B . P 11 HOH 161 561 98 HOH HOH B . P 11 HOH 162 562 144 HOH HOH B . P 11 HOH 163 563 402 HOH HOH B . P 11 HOH 164 564 33 HOH HOH B . P 11 HOH 165 565 371 HOH HOH B . P 11 HOH 166 566 65 HOH HOH B . P 11 HOH 167 567 424 HOH HOH B . P 11 HOH 168 568 241 HOH HOH B . P 11 HOH 169 569 53 HOH HOH B . P 11 HOH 170 570 419 HOH HOH B . P 11 HOH 171 571 293 HOH HOH B . P 11 HOH 172 572 104 HOH HOH B . P 11 HOH 173 573 132 HOH HOH B . P 11 HOH 174 574 496 HOH HOH B . P 11 HOH 175 575 420 HOH HOH B . P 11 HOH 176 576 79 HOH HOH B . P 11 HOH 177 577 439 HOH HOH B . P 11 HOH 178 578 217 HOH HOH B . P 11 HOH 179 579 162 HOH HOH B . P 11 HOH 180 580 81 HOH HOH B . P 11 HOH 181 581 270 HOH HOH B . P 11 HOH 182 582 349 HOH HOH B . P 11 HOH 183 583 418 HOH HOH B . P 11 HOH 184 584 264 HOH HOH B . P 11 HOH 185 585 415 HOH HOH B . P 11 HOH 186 586 119 HOH HOH B . P 11 HOH 187 587 233 HOH HOH B . P 11 HOH 188 588 282 HOH HOH B . P 11 HOH 189 589 205 HOH HOH B . P 11 HOH 190 590 173 HOH HOH B . P 11 HOH 191 591 486 HOH HOH B . P 11 HOH 192 592 28 HOH HOH B . P 11 HOH 193 593 481 HOH HOH B . P 11 HOH 194 594 498 HOH HOH B . P 11 HOH 195 595 397 HOH HOH B . P 11 HOH 196 596 478 HOH HOH B . P 11 HOH 197 597 483 HOH HOH B . P 11 HOH 198 598 391 HOH HOH B . P 11 HOH 199 599 380 HOH HOH B . P 11 HOH 200 600 335 HOH HOH B . P 11 HOH 201 601 455 HOH HOH B . P 11 HOH 202 602 250 HOH HOH B . P 11 HOH 203 603 493 HOH HOH B . P 11 HOH 204 604 271 HOH HOH B . P 11 HOH 205 605 346 HOH HOH B . P 11 HOH 206 606 259 HOH HOH B . P 11 HOH 207 607 336 HOH HOH B . P 11 HOH 208 608 287 HOH HOH B . P 11 HOH 209 609 177 HOH HOH B . P 11 HOH 210 610 201 HOH HOH B . P 11 HOH 211 611 210 HOH HOH B . P 11 HOH 212 612 245 HOH HOH B . P 11 HOH 213 613 340 HOH HOH B . P 11 HOH 214 614 267 HOH HOH B . P 11 HOH 215 615 178 HOH HOH B . P 11 HOH 216 616 399 HOH HOH B . P 11 HOH 217 617 107 HOH HOH B . P 11 HOH 218 618 258 HOH HOH B . P 11 HOH 219 619 470 HOH HOH B . P 11 HOH 220 620 480 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P # 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)' 6230 ? 1 MORE 9 ? 1 'SSA (A^2)' 21400 ? # _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 ? # 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 ? ? ? 3.3.20 2 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.5.1 3 # 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 O4 B NAG 305 ? ? C1 B NAG 307 ? ? 1.07 2 1 ND2 A ASN 108 ? ? C1 A NAG 301 ? ? 1.19 3 1 O2 B BMA 308 ? ? C1B B XYP 309 ? ? 1.62 4 1 O6 B BMA 308 ? ? C1 B MAN 310 ? ? 1.70 5 1 O4 B NAG 305 ? ? O5 B NAG 307 ? ? 2.03 6 1 ND2 A ASN 108 ? ? O5 A NAG 301 ? ? 2.07 7 1 CG A ASN 108 ? ? C1 A NAG 301 ? ? 2.17 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 B _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 112 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 B _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 112 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 B _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 112 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 117.03 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.27 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 9 ? ? -115.94 71.15 2 1 ALA A 79 ? ? 56.73 -125.95 3 1 ASN A 106 ? ? -84.34 48.06 4 1 VAL A 158 ? ? -105.33 -63.56 5 1 TYR A 231 ? ? -94.90 30.97 6 1 ASN A 238 ? ? -126.87 -65.66 7 1 GLN A 245 ? ? -130.38 -39.22 8 1 ASP B 207 ? ? -142.28 10.19 # 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 ASN 106 ? CG ? A ASN 106 CG 2 1 Y 1 A ASN 106 ? OD1 ? A ASN 106 OD1 3 1 Y 1 A ASN 106 ? ND2 ? A ASN 106 ND2 4 1 Y 1 B GLU 2 ? CG ? B GLU 2 CG 5 1 Y 1 B GLU 2 ? CD ? B GLU 2 CD 6 1 Y 1 B GLU 2 ? OE1 ? B GLU 2 OE1 7 1 Y 1 B GLU 2 ? OE2 ? B GLU 2 OE2 8 1 Y 1 B ARG 82 ? CG ? B ARG 82 CG 9 1 Y 1 B ARG 82 ? CD ? B ARG 82 CD 10 1 Y 1 B ARG 82 ? NE ? B ARG 82 NE 11 1 Y 1 B ARG 82 ? CZ ? B ARG 82 CZ 12 1 Y 1 B ARG 82 ? NH1 ? B ARG 82 NH1 13 1 Y 1 B ARG 82 ? NH2 ? B ARG 82 NH2 14 1 Y 1 B TYR 83 ? CG ? B TYR 83 CG 15 1 Y 1 B TYR 83 ? CD1 ? B TYR 83 CD1 16 1 Y 1 B TYR 83 ? CD2 ? B TYR 83 CD2 17 1 Y 1 B TYR 83 ? CE1 ? B TYR 83 CE1 18 1 Y 1 B TYR 83 ? CE2 ? B TYR 83 CE2 19 1 Y 1 B TYR 83 ? CZ ? B TYR 83 CZ 20 1 Y 1 B TYR 83 ? OH ? B TYR 83 OH 21 1 Y 1 B ASN 166 ? CG ? B ASN 166 CG 22 1 Y 1 B ASN 166 ? OD1 ? B ASN 166 OD1 23 1 Y 1 B ASN 166 ? ND2 ? B ASN 166 ND2 24 1 Y 1 B ASP 250 ? CG ? B ASP 250 CG 25 1 Y 1 B ASP 250 ? OD1 ? B ASP 250 OD1 26 1 Y 1 B ASP 250 ? OD2 ? B ASP 250 OD2 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 307 ? O1 ? K NAG 1 O1 32 1 N 1 B XYP 309 ? O4A ? M XYP 1 O4A 33 1 N 1 B MAN 310 ? O1 ? N MAN 1 O1 # _pdbx_audit_support.funding_organization 'SERB, DST' _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 GLYCEROL GOL 5 N-ACETYL-D-GALACTOSAMINE NGA 6 BETA-D-GALACTOSE GAL 7 ALPHA-L-FUCOSE FUC 8 BETA-D-MANNOSE BMA 9 BETA-D-XYLOPYRANOSE XYP 10 ALPHA-D-MANNOSE MAN 11 water HOH #