data_4MCY # _entry.id 4MCY # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4MCY RCSB RCSB081754 WWPDB D_1000081754 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4MCZ . unspecified PDB 4MD0 . unspecified PDB 4MD4 . unspecified PDB 4MD5 . unspecified PDB 4MDI . unspecified PDB 4MDJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4MCY _pdbx_database_status.recvd_initial_deposition_date 2013-08-22 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Scally, S.W.' 1 'Rossjohn, J.' 2 # _citation.id primary _citation.title 'A molecular basis for the association of the HLA-DRB1 locus, citrullination, and rheumatoid arthritis.' _citation.journal_abbrev J.Exp.Med. _citation.journal_volume 210 _citation.page_first 2569 _citation.page_last 2582 _citation.year 2013 _citation.journal_id_ASTM JEMEAV _citation.country US _citation.journal_id_ISSN 0022-1007 _citation.journal_id_CSD 0774 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24190431 _citation.pdbx_database_id_DOI 10.1084/jem.20131241 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Scally, S.W.' 1 primary 'Petersen, J.' 2 primary 'Law, S.C.' 3 primary 'Dudek, N.L.' 4 primary 'Nel, H.J.' 5 primary 'Loh, K.L.' 6 primary 'Wijeyewickrema, L.C.' 7 primary 'Eckle, S.B.' 8 primary 'van Heemst, J.' 9 primary 'Pike, R.N.' 10 primary 'McCluskey, J.' 11 primary 'Toes, R.E.' 12 primary 'La Gruta, N.L.' 13 primary 'Purcell, A.W.' 14 primary 'Reid, H.H.' 15 primary 'Thomas, R.' 16 primary 'Rossjohn, J.' 17 # _cell.entry_id 4MCY _cell.length_a 67.035 _cell.length_b 177.821 _cell.length_c 76.728 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4MCY _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'HLA class II histocompatibility antigen, DR alpha chain' 21919.594 1 ? ? 'Extracellular Domain, UNP residues 26-206' ? 2 polymer man 'HLA class II histocompatibility antigen, DRB1-4 beta chain' 23224.617 1 ? ? 'Extracellular Domain, UNP residues 30-219' ? 3 polymer syn 'Citrullinated Vimentin' 1386.602 1 ? ? 'UNP residues 66-78' ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 5 non-polymer syn 1,2-ETHANEDIOL 62.068 2 ? ? ? ? 6 water nat water 18.015 294 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'MHC class II antigen DRA' 2 'MHC class II antigen DRB1*4, DR-4, DR4' # 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 ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFDTSGDDDDK ; ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFDTSGDDDDK ; A ? 2 'polypeptide(L)' no no ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTY CRHNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; ;GSGDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTY CRHNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTL VMLETVPRSGEVYTCQVEHPSLTSPLTVEWRATGGDDDDK ; B ? 3 'polypeptide(L)' no yes 'SAVRL(CIR)SSVPGVR' SAVRLRSSVPGVR C ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ILE n 1 2 LYS n 1 3 GLU n 1 4 GLU n 1 5 HIS n 1 6 VAL n 1 7 ILE n 1 8 ILE n 1 9 GLN n 1 10 ALA n 1 11 GLU n 1 12 PHE n 1 13 TYR n 1 14 LEU n 1 15 ASN n 1 16 PRO n 1 17 ASP n 1 18 GLN n 1 19 SER n 1 20 GLY n 1 21 GLU n 1 22 PHE n 1 23 MET n 1 24 PHE n 1 25 ASP n 1 26 PHE n 1 27 ASP n 1 28 GLY n 1 29 ASP n 1 30 GLU n 1 31 ILE n 1 32 PHE n 1 33 HIS n 1 34 VAL n 1 35 ASP n 1 36 MET n 1 37 ALA n 1 38 LYS n 1 39 LYS n 1 40 GLU n 1 41 THR n 1 42 VAL n 1 43 TRP n 1 44 ARG n 1 45 LEU n 1 46 GLU n 1 47 GLU n 1 48 PHE n 1 49 GLY n 1 50 ARG n 1 51 PHE n 1 52 ALA n 1 53 SER n 1 54 PHE n 1 55 GLU n 1 56 ALA n 1 57 GLN n 1 58 GLY n 1 59 ALA n 1 60 LEU n 1 61 ALA n 1 62 ASN n 1 63 ILE n 1 64 ALA n 1 65 VAL n 1 66 ASP n 1 67 LYS n 1 68 ALA n 1 69 ASN n 1 70 LEU n 1 71 GLU n 1 72 ILE n 1 73 MET n 1 74 THR n 1 75 LYS n 1 76 ARG n 1 77 SER n 1 78 ASN n 1 79 TYR n 1 80 THR n 1 81 PRO n 1 82 ILE n 1 83 THR n 1 84 ASN n 1 85 VAL n 1 86 PRO n 1 87 PRO n 1 88 GLU n 1 89 VAL n 1 90 THR n 1 91 VAL n 1 92 LEU n 1 93 THR n 1 94 ASN n 1 95 SER n 1 96 PRO n 1 97 VAL n 1 98 GLU n 1 99 LEU n 1 100 ARG n 1 101 GLU n 1 102 PRO n 1 103 ASN n 1 104 VAL n 1 105 LEU n 1 106 ILE n 1 107 CYS n 1 108 PHE n 1 109 ILE n 1 110 ASP n 1 111 LYS n 1 112 PHE n 1 113 THR n 1 114 PRO n 1 115 PRO n 1 116 VAL n 1 117 VAL n 1 118 ASN n 1 119 VAL n 1 120 THR n 1 121 TRP n 1 122 LEU n 1 123 ARG n 1 124 ASN n 1 125 GLY n 1 126 LYS n 1 127 PRO n 1 128 VAL n 1 129 THR n 1 130 THR n 1 131 GLY n 1 132 VAL n 1 133 SER n 1 134 GLU n 1 135 THR n 1 136 VAL n 1 137 PHE n 1 138 LEU n 1 139 PRO n 1 140 ARG n 1 141 GLU n 1 142 ASP n 1 143 HIS n 1 144 LEU n 1 145 PHE n 1 146 ARG n 1 147 LYS n 1 148 PHE n 1 149 HIS n 1 150 TYR n 1 151 LEU n 1 152 PRO n 1 153 PHE n 1 154 LEU n 1 155 PRO n 1 156 SER n 1 157 THR n 1 158 GLU n 1 159 ASP n 1 160 VAL n 1 161 TYR n 1 162 ASP n 1 163 CYS n 1 164 ARG n 1 165 VAL n 1 166 GLU n 1 167 HIS n 1 168 TRP n 1 169 GLY n 1 170 LEU n 1 171 ASP n 1 172 GLU n 1 173 PRO n 1 174 LEU n 1 175 LEU n 1 176 LYS n 1 177 HIS n 1 178 TRP n 1 179 GLU n 1 180 PHE n 1 181 ASP n 1 182 THR n 1 183 SER n 1 184 GLY n 1 185 ASP n 1 186 ASP n 1 187 ASP n 1 188 ASP n 1 189 LYS n 2 1 GLY n 2 2 SER n 2 3 GLY n 2 4 ASP n 2 5 THR n 2 6 ARG n 2 7 PRO n 2 8 ARG n 2 9 PHE n 2 10 LEU n 2 11 GLU n 2 12 GLN n 2 13 VAL n 2 14 LYS n 2 15 HIS n 2 16 GLU n 2 17 CYS n 2 18 HIS n 2 19 PHE n 2 20 PHE n 2 21 ASN n 2 22 GLY n 2 23 THR n 2 24 GLU n 2 25 ARG n 2 26 VAL n 2 27 ARG n 2 28 PHE n 2 29 LEU n 2 30 ASP n 2 31 ARG n 2 32 TYR n 2 33 PHE n 2 34 TYR n 2 35 HIS n 2 36 GLN n 2 37 GLU n 2 38 GLU n 2 39 TYR n 2 40 VAL n 2 41 ARG n 2 42 PHE n 2 43 ASP n 2 44 SER n 2 45 ASP n 2 46 VAL n 2 47 GLY n 2 48 GLU n 2 49 TYR n 2 50 ARG n 2 51 ALA n 2 52 VAL n 2 53 THR n 2 54 GLU n 2 55 LEU n 2 56 GLY n 2 57 ARG n 2 58 PRO n 2 59 ASP n 2 60 ALA n 2 61 GLU n 2 62 TYR n 2 63 TRP n 2 64 ASN n 2 65 SER n 2 66 GLN n 2 67 LYS n 2 68 ASP n 2 69 LEU n 2 70 LEU n 2 71 GLU n 2 72 GLN n 2 73 LYS n 2 74 ARG n 2 75 ALA n 2 76 ALA n 2 77 VAL n 2 78 ASP n 2 79 THR n 2 80 TYR n 2 81 CYS n 2 82 ARG n 2 83 HIS n 2 84 ASN n 2 85 TYR n 2 86 GLY n 2 87 VAL n 2 88 GLY n 2 89 GLU n 2 90 SER n 2 91 PHE n 2 92 THR n 2 93 VAL n 2 94 GLN n 2 95 ARG n 2 96 ARG n 2 97 VAL n 2 98 TYR n 2 99 PRO n 2 100 GLU n 2 101 VAL n 2 102 THR n 2 103 VAL n 2 104 TYR n 2 105 PRO n 2 106 ALA n 2 107 LYS n 2 108 THR n 2 109 GLN n 2 110 PRO n 2 111 LEU n 2 112 GLN n 2 113 HIS n 2 114 HIS n 2 115 ASN n 2 116 LEU n 2 117 LEU n 2 118 VAL n 2 119 CYS n 2 120 SER n 2 121 VAL n 2 122 ASN n 2 123 GLY n 2 124 PHE n 2 125 TYR n 2 126 PRO n 2 127 GLY n 2 128 SER n 2 129 ILE n 2 130 GLU n 2 131 VAL n 2 132 ARG n 2 133 TRP n 2 134 PHE n 2 135 ARG n 2 136 ASN n 2 137 GLY n 2 138 GLN n 2 139 GLU n 2 140 GLU n 2 141 LYS n 2 142 THR n 2 143 GLY n 2 144 VAL n 2 145 VAL n 2 146 SER n 2 147 THR n 2 148 GLY n 2 149 LEU n 2 150 ILE n 2 151 GLN n 2 152 ASN n 2 153 GLY n 2 154 ASP n 2 155 TRP n 2 156 THR n 2 157 PHE n 2 158 GLN n 2 159 THR n 2 160 LEU n 2 161 VAL n 2 162 MET n 2 163 LEU n 2 164 GLU n 2 165 THR n 2 166 VAL n 2 167 PRO n 2 168 ARG n 2 169 SER n 2 170 GLY n 2 171 GLU n 2 172 VAL n 2 173 TYR n 2 174 THR n 2 175 CYS n 2 176 GLN n 2 177 VAL n 2 178 GLU n 2 179 HIS n 2 180 PRO n 2 181 SER n 2 182 LEU n 2 183 THR n 2 184 SER n 2 185 PRO n 2 186 LEU n 2 187 THR n 2 188 VAL n 2 189 GLU n 2 190 TRP n 2 191 ARG n 2 192 ALA n 2 193 THR n 2 194 GLY n 2 195 GLY n 2 196 ASP n 2 197 ASP n 2 198 ASP n 2 199 ASP n 2 200 LYS n 3 1 SER n 3 2 ALA n 3 3 VAL n 3 4 ARG n 3 5 LEU n 3 6 CIR n 3 7 SER n 3 8 SER n 3 9 VAL n 3 10 PRO n 3 11 GLY n 3 12 VAL n 3 13 ARG n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? human ? 'HLA-DRA, HLA-DRA1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? human ? HLA-DRB1 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'Homo sapiens' _pdbx_entity_src_syn.organism_common_name human _pdbx_entity_src_syn.ncbi_taxonomy_id 9606 _pdbx_entity_src_syn.details 'This sequence is from human vimentin and contains citrulline at position 64' # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP DRA_HUMAN P01903 1 ;IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYT PITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDV YDCRVEHWGLDEPLLKHWEFD ; 26 ? 2 UNP 2B14_HUMAN P13760 2 ;GDTRPRFLEQVKHECHFFNGTERVRFLDRYFYHQEEYVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQKRAAVDTYCR HNYGVGESFTVQRRVYPEVTVYPAKTQPLQHHNLLVCSVNGFYPGSIEVRWFRNGQEEKTGVVSTGLIQNGDWTFQTLVM LETVPRSGEVYTCQVEHPSLTSPLTVEWRA ; 30 ? 3 UNP VIME_HUMAN P08670 3 SAVRLRSSVPGVR 66 ? # 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 4MCY A 1 ? 181 ? P01903 26 ? 206 ? 1 181 2 2 4MCY B 3 ? 192 ? P13760 30 ? 219 ? 1 190 3 3 4MCY C 1 ? 13 ? P08670 66 ? 78 ? 1 13 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4MCY THR A 182 ? UNP P01903 ? ? 'EXPRESSION TAG' 182 1 1 4MCY SER A 183 ? UNP P01903 ? ? 'EXPRESSION TAG' 183 2 1 4MCY GLY A 184 ? UNP P01903 ? ? 'EXPRESSION TAG' 184 3 1 4MCY ASP A 185 ? UNP P01903 ? ? 'EXPRESSION TAG' 185 4 1 4MCY ASP A 186 ? UNP P01903 ? ? 'EXPRESSION TAG' 186 5 1 4MCY ASP A 187 ? UNP P01903 ? ? 'EXPRESSION TAG' 187 6 1 4MCY ASP A 188 ? UNP P01903 ? ? 'EXPRESSION TAG' 188 7 1 4MCY LYS A 189 ? UNP P01903 ? ? 'EXPRESSION TAG' 189 8 2 4MCY GLY B 1 ? UNP P13760 ? ? 'EXPRESSION TAG' -1 9 2 4MCY SER B 2 ? UNP P13760 ? ? 'EXPRESSION TAG' 0 10 2 4MCY THR B 193 ? UNP P13760 ? ? 'EXPRESSION TAG' 191 11 2 4MCY GLY B 194 ? UNP P13760 ? ? 'EXPRESSION TAG' 192 12 2 4MCY GLY B 195 ? UNP P13760 ? ? 'EXPRESSION TAG' 193 13 2 4MCY ASP B 196 ? UNP P13760 ? ? 'EXPRESSION TAG' 194 14 2 4MCY ASP B 197 ? UNP P13760 ? ? 'EXPRESSION TAG' 195 15 2 4MCY ASP B 198 ? UNP P13760 ? ? 'EXPRESSION TAG' 196 16 2 4MCY ASP B 199 ? UNP P13760 ? ? 'EXPRESSION TAG' 197 17 2 4MCY LYS B 200 ? UNP P13760 ? ? 'EXPRESSION TAG' 198 18 # 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 CIR 'L-peptide linking' n CITRULLINE ? 'C6 H13 N3 O3' 175.186 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4MCY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.57 _exptl_crystal.density_percent_sol 52.18 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 294 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.3 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '26% PEG 3350, 0.2M Potassium Nitrate, 0.1M Bis-Tris-Propane pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 210r' _diffrn_detector.pdbx_collection_date 2012-08-09 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength .95370 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX1' _diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' _diffrn_source.pdbx_synchrotron_beamline MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list .95370 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4MCY _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 62.73 _reflns.d_resolution_high 2.30 _reflns.number_obs 20836 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs 0.147 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.8 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.3 _reflns_shell.d_res_low 2.42 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs 0.495 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.4 _reflns_shell.pdbx_redundancy 5.9 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4MCY _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 20817 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.38 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 38.432 _refine.ls_d_res_high 2.300 _refine.ls_percent_reflns_obs 99.98 _refine.ls_R_factor_obs 0.1733 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1705 _refine.ls_R_factor_R_free 0.2249 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.11 _refine.ls_number_reflns_R_free 1064 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.27 _refine.pdbx_overall_phase_error 20.08 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3135 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 50 _refine_hist.number_atoms_solvent 294 _refine_hist.number_atoms_total 3479 _refine_hist.d_res_high 2.300 _refine_hist.d_res_low 38.432 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.007 ? ? 3302 'X-RAY DIFFRACTION' ? f_angle_d 1.187 ? ? 4491 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.362 ? ? 1200 'X-RAY DIFFRACTION' ? f_chiral_restr 0.055 ? ? 483 'X-RAY DIFFRACTION' ? f_plane_restr 0.006 ? ? 590 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.3000 2.4047 2458 0.1906 100.00 0.2635 . . 115 . . . . 'X-RAY DIFFRACTION' . 2.4047 2.5314 2417 0.1932 100.00 0.2726 . . 129 . . . . 'X-RAY DIFFRACTION' . 2.5314 2.6900 2440 0.1924 100.00 0.2716 . . 133 . . . . 'X-RAY DIFFRACTION' . 2.6900 2.8976 2430 0.1907 100.00 0.2656 . . 137 . . . . 'X-RAY DIFFRACTION' . 2.8976 3.1891 2458 0.1904 100.00 0.2347 . . 139 . . . . 'X-RAY DIFFRACTION' . 3.1891 3.6503 2470 0.1650 100.00 0.2051 . . 133 . . . . 'X-RAY DIFFRACTION' . 3.6503 4.5977 2479 0.1375 100.00 0.2049 . . 138 . . . . 'X-RAY DIFFRACTION' . 4.5977 38.4378 2601 0.1631 100.00 0.1865 . . 140 . . . . # _struct.entry_id 4MCY _struct.title 'Immune Receptor' _struct.pdbx_descriptor 'HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-4 beta chain, Vimentin' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4MCY _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'HLA-DR, Antigen presentation, T-cell receptor, Citrullination, Membrane, IMMUNE SYSTEM' # 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 4 ? F N N 5 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 6 ? K N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 LEU A 45 ? PHE A 51 ? LEU A 45 PHE A 51 5 ? 7 HELX_P HELX_P2 2 ALA A 56 ? SER A 77 ? ALA A 56 SER A 77 1 ? 22 HELX_P HELX_P3 3 THR B 53 ? LEU B 55 ? THR B 51 LEU B 53 5 ? 3 HELX_P HELX_P4 4 GLY B 56 ? SER B 65 ? GLY B 54 SER B 63 1 ? 10 HELX_P HELX_P5 5 GLN B 66 ? ALA B 75 ? GLN B 64 ALA B 73 1 ? 10 HELX_P HELX_P6 6 ALA B 75 ? TYR B 80 ? ALA B 73 TYR B 78 1 ? 6 HELX_P HELX_P7 7 TYR B 80 ? GLU B 89 ? TYR B 78 GLU B 87 1 ? 10 HELX_P HELX_P8 8 SER B 90 ? THR B 92 ? SER B 88 THR B 90 5 ? 3 # _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 107 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 107 A CYS 163 1_555 ? ? ? ? ? ? ? 2.047 ? disulf2 disulf ? ? B CYS 17 SG ? ? ? 1_555 B CYS 81 SG ? ? B CYS 15 B CYS 79 1_555 ? ? ? ? ? ? ? 2.060 ? disulf3 disulf ? ? B CYS 119 SG ? ? ? 1_555 B CYS 175 SG ? ? B CYS 117 B CYS 173 1_555 ? ? ? ? ? ? ? 2.009 ? covale1 covale ? ? C LEU 5 C ? ? ? 1_555 C CIR 6 N2 ? ? C LEU 5 C CIR 6 1_555 ? ? ? ? ? ? ? 1.329 ? covale2 covale ? ? C CIR 6 C1 ? ? ? 1_555 C SER 7 N ? ? C CIR 6 C SER 7 1_555 ? ? ? ? ? ? ? 1.301 ? covale3 covale ? ? B ASN 21 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 19 B NAG 201 1_555 ? ? ? ? ? ? ? 1.427 ? covale4 covale ? ? A ASN 78 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 78 A NAG 201 1_555 ? ? ? ? ? ? ? 1.448 ? covale5 covale ? ? A ASN 118 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 118 A NAG 202 1_555 ? ? ? ? ? ? ? 1.450 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 15 A . ? ASN 15 A PRO 16 A ? PRO 16 A 1 4.12 2 THR 113 A . ? THR 113 A PRO 114 A ? PRO 114 A 1 -0.30 3 TYR 125 B . ? TYR 123 B PRO 126 B ? PRO 124 B 1 0.87 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLU A 40 ? TRP A 43 ? GLU A 40 TRP A 43 A 2 ASP A 29 ? ASP A 35 ? ASP A 29 ASP A 35 A 3 SER A 19 ? PHE A 26 ? SER A 19 PHE A 26 A 4 HIS A 5 ? ASN A 15 ? HIS A 5 ASN A 15 A 5 PHE B 9 ? PHE B 20 ? PHE B 7 PHE B 18 A 6 ARG B 25 ? TYR B 34 ? ARG B 23 TYR B 32 A 7 GLU B 37 ? ASP B 43 ? GLU B 35 ASP B 41 A 8 TYR B 49 ? ALA B 51 ? TYR B 47 ALA B 49 B 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 B 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 B 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 B 4 SER A 133 ? GLU A 134 ? SER A 133 GLU A 134 C 1 GLU A 88 ? THR A 93 ? GLU A 88 THR A 93 C 2 ASN A 103 ? PHE A 112 ? ASN A 103 PHE A 112 C 3 PHE A 145 ? PHE A 153 ? PHE A 145 PHE A 153 C 4 LEU A 138 ? PRO A 139 ? LEU A 138 PRO A 139 D 1 LYS A 126 ? VAL A 128 ? LYS A 126 VAL A 128 D 2 ASN A 118 ? ARG A 123 ? ASN A 118 ARG A 123 D 3 VAL A 160 ? GLU A 166 ? VAL A 160 GLU A 166 D 4 LEU A 174 ? GLU A 179 ? LEU A 174 GLU A 179 E 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 E 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 E 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 E 4 VAL B 144 ? SER B 146 ? VAL B 142 SER B 144 F 1 GLU B 100 ? ALA B 106 ? GLU B 98 ALA B 104 F 2 LEU B 116 ? PHE B 124 ? LEU B 114 PHE B 122 F 3 PHE B 157 ? GLU B 164 ? PHE B 155 GLU B 162 F 4 ILE B 150 ? GLN B 151 ? ILE B 148 GLN B 149 G 1 GLN B 138 ? GLU B 140 ? GLN B 136 GLU B 138 G 2 GLU B 130 ? ARG B 135 ? GLU B 128 ARG B 133 G 3 VAL B 172 ? GLU B 178 ? VAL B 170 GLU B 176 G 4 LEU B 186 ? ARG B 191 ? LEU B 184 ARG B 189 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O VAL A 42 ? O VAL A 42 N HIS A 33 ? N HIS A 33 A 2 3 O ASP A 29 ? O ASP A 29 N PHE A 26 ? N PHE A 26 A 3 4 O ASP A 25 ? O ASP A 25 N ILE A 8 ? N ILE A 8 A 4 5 N ASN A 15 ? N ASN A 15 O PHE B 9 ? O PHE B 7 A 5 6 N GLN B 12 ? N GLN B 10 O PHE B 33 ? O PHE B 31 A 6 7 N ASP B 30 ? N ASP B 28 O PHE B 42 ? O PHE B 40 A 7 8 N ARG B 41 ? N ARG B 39 O ARG B 50 ? O ARG B 48 B 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 B 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 B 3 4 O TYR A 150 ? O TYR A 150 N SER A 133 ? N SER A 133 C 1 2 N LEU A 92 ? N LEU A 92 O ILE A 106 ? O ILE A 106 C 2 3 N LEU A 105 ? N LEU A 105 O LEU A 151 ? O LEU A 151 C 3 4 O ARG A 146 ? O ARG A 146 N LEU A 138 ? N LEU A 138 D 1 2 O LYS A 126 ? O LYS A 126 N ARG A 123 ? N ARG A 123 D 2 3 N THR A 120 ? N THR A 120 O ARG A 164 ? O ARG A 164 D 3 4 N TYR A 161 ? N TYR A 161 O TRP A 178 ? O TRP A 178 E 1 2 N THR B 102 ? N THR B 100 O SER B 120 ? O SER B 118 E 2 3 N CYS B 119 ? N CYS B 117 O VAL B 161 ? O VAL B 159 E 3 4 O MET B 162 ? O MET B 160 N VAL B 145 ? N VAL B 143 F 1 2 N THR B 102 ? N THR B 100 O SER B 120 ? O SER B 118 F 2 3 N CYS B 119 ? N CYS B 117 O VAL B 161 ? O VAL B 159 F 3 4 O GLN B 158 ? O GLN B 156 N ILE B 150 ? N ILE B 148 G 1 2 O GLU B 140 ? O GLU B 138 N TRP B 133 ? N TRP B 131 G 2 3 N ARG B 132 ? N ARG B 130 O GLN B 176 ? O GLN B 174 G 3 4 N VAL B 177 ? N VAL B 175 O LEU B 186 ? O LEU B 184 # 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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO A 203' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO B 202' AC3 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 201 BOUND TO ASN A 78' AC4 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A 202 BOUND TO ASN A 118' AC5 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 201 BOUND TO ASN B 19' # 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 6 THR A 80 ? THR A 80 . ? 1_555 ? 2 AC1 6 PRO A 81 ? PRO A 81 . ? 1_555 ? 3 AC1 6 ILE A 82 ? ILE A 82 . ? 1_555 ? 4 AC1 6 THR A 83 ? THR A 83 . ? 1_555 ? 5 AC1 6 HOH I . ? HOH A 312 . ? 1_555 ? 6 AC1 6 HIS B 35 ? HIS B 33 . ? 1_555 ? 7 AC2 5 THR B 79 ? THR B 77 . ? 1_555 ? 8 AC2 5 TYR B 80 ? TYR B 78 . ? 1_555 ? 9 AC2 5 HIS B 113 ? HIS B 111 . ? 1_655 ? 10 AC2 5 LEU C 5 ? LEU C 5 . ? 1_555 ? 11 AC2 5 CIR C 6 ? CIR C 6 . ? 1_555 ? 12 AC3 3 ASN A 78 ? ASN A 78 . ? 1_555 ? 13 AC3 3 HOH I . ? HOH A 403 . ? 1_555 ? 14 AC3 3 HOH I . ? HOH A 409 . ? 1_555 ? 15 AC4 5 ASN A 118 ? ASN A 118 . ? 1_555 ? 16 AC4 5 GLU A 166 ? GLU A 166 . ? 1_555 ? 17 AC4 5 TRP A 168 ? TRP A 168 . ? 1_555 ? 18 AC4 5 HOH I . ? HOH A 366 . ? 1_555 ? 19 AC4 5 HOH I . ? HOH A 442 . ? 1_555 ? 20 AC5 2 ASN B 21 ? ASN B 19 . ? 1_555 ? 21 AC5 2 GLU B 24 ? GLU B 22 . ? 1_555 ? # _database_PDB_matrix.entry_id 4MCY _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4MCY _atom_sites.fract_transf_matrix[1][1] 0.014918 _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] 0.005624 _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] 0.013033 _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 . GLU A 1 3 ? 35.791 11.456 -18.798 1.00 47.65 ? 3 GLU A N 1 ATOM 2 C CA . GLU A 1 3 ? 36.613 11.084 -17.647 1.00 58.02 ? 3 GLU A CA 1 ATOM 3 C C . GLU A 1 3 ? 35.792 10.447 -16.530 1.00 47.68 ? 3 GLU A C 1 ATOM 4 O O . GLU A 1 3 ? 34.587 10.675 -16.424 1.00 58.56 ? 3 GLU A O 1 ATOM 5 C CB . GLU A 1 3 ? 37.368 12.308 -17.121 1.00 54.69 ? 3 GLU A CB 1 ATOM 6 C CG . GLU A 1 3 ? 36.503 13.315 -16.403 1.00 48.55 ? 3 GLU A CG 1 ATOM 7 C CD . GLU A 1 3 ? 36.902 14.742 -16.732 1.00 54.43 ? 3 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 3 ? 36.030 15.635 -16.660 1.00 63.89 ? 3 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 3 ? 38.080 14.968 -17.084 1.00 53.00 ? 3 GLU A OE2 1 ATOM 10 N N . GLU A 1 4 ? 36.452 9.645 -15.700 1.00 46.80 ? 4 GLU A N 1 ATOM 11 C CA . GLU A 1 4 ? 35.777 9.008 -14.581 1.00 37.12 ? 4 GLU A CA 1 ATOM 12 C C . GLU A 1 4 ? 35.845 9.881 -13.324 1.00 32.80 ? 4 GLU A C 1 ATOM 13 O O . GLU A 1 4 ? 34.853 10.023 -12.621 1.00 31.33 ? 4 GLU A O 1 ATOM 14 C CB . GLU A 1 4 ? 36.371 7.628 -14.290 1.00 37.78 ? 4 GLU A CB 1 ATOM 15 C CG . GLU A 1 4 ? 36.097 6.564 -15.361 1.00 59.28 ? 4 GLU A CG 1 ATOM 16 C CD . GLU A 1 4 ? 36.548 5.165 -14.935 1.00 54.65 ? 4 GLU A CD 1 ATOM 17 O OE1 . GLU A 1 4 ? 37.250 5.044 -13.907 1.00 41.32 ? 4 GLU A OE1 1 ATOM 18 O OE2 . GLU A 1 4 ? 36.200 4.184 -15.631 1.00 59.44 ? 4 GLU A OE2 1 ATOM 19 N N . HIS A 1 5 ? 37.006 10.458 -13.031 1.00 26.07 ? 5 HIS A N 1 ATOM 20 C CA . HIS A 1 5 ? 37.151 11.249 -11.811 1.00 18.11 ? 5 HIS A CA 1 ATOM 21 C C . HIS A 1 5 ? 38.114 12.412 -11.977 1.00 23.13 ? 5 HIS A C 1 ATOM 22 O O . HIS A 1 5 ? 38.990 12.395 -12.845 1.00 15.16 ? 5 HIS A O 1 ATOM 23 C CB . HIS A 1 5 ? 37.606 10.374 -10.646 1.00 18.24 ? 5 HIS A CB 1 ATOM 24 C CG . HIS A 1 5 ? 36.676 9.243 -10.349 1.00 26.86 ? 5 HIS A CG 1 ATOM 25 N ND1 . HIS A 1 5 ? 35.416 9.433 -9.827 1.00 24.56 ? 5 HIS A ND1 1 ATOM 26 C CD2 . HIS A 1 5 ? 36.813 7.908 -10.528 1.00 27.13 ? 5 HIS A CD2 1 ATOM 27 C CE1 . HIS A 1 5 ? 34.822 8.262 -9.683 1.00 18.16 ? 5 HIS A CE1 1 ATOM 28 N NE2 . HIS A 1 5 ? 35.648 7.321 -10.102 1.00 30.43 ? 5 HIS A NE2 1 ATOM 29 N N . VAL A 1 6 ? 37.924 13.439 -11.156 1.00 18.38 ? 6 VAL A N 1 ATOM 30 C CA . VAL A 1 6 ? 38.840 14.564 -11.137 1.00 11.47 ? 6 VAL A CA 1 ATOM 31 C C . VAL A 1 6 ? 39.202 14.922 -9.709 1.00 10.70 ? 6 VAL A C 1 ATOM 32 O O . VAL A 1 6 ? 38.328 15.087 -8.858 1.00 14.75 ? 6 VAL A O 1 ATOM 33 C CB . VAL A 1 6 ? 38.236 15.812 -11.800 1.00 14.84 ? 6 VAL A CB 1 ATOM 34 C CG1 . VAL A 1 6 ? 39.213 16.955 -11.729 1.00 9.88 ? 6 VAL A CG1 1 ATOM 35 C CG2 . VAL A 1 6 ? 37.836 15.522 -13.230 1.00 14.78 ? 6 VAL A CG2 1 ATOM 36 N N . ILE A 1 7 ? 40.494 15.089 -9.466 1.00 9.56 ? 7 ILE A N 1 ATOM 37 C CA . ILE A 1 7 ? 40.980 15.551 -8.183 1.00 8.24 ? 7 ILE A CA 1 ATOM 38 C C . ILE A 1 7 ? 41.676 16.874 -8.411 1.00 8.64 ? 7 ILE A C 1 ATOM 39 O O . ILE A 1 7 ? 42.544 16.987 -9.281 1.00 8.97 ? 7 ILE A O 1 ATOM 40 C CB . ILE A 1 7 ? 41.957 14.558 -7.519 1.00 8.58 ? 7 ILE A CB 1 ATOM 41 C CG1 . ILE A 1 7 ? 41.289 13.210 -7.276 1.00 14.57 ? 7 ILE A CG1 1 ATOM 42 C CG2 . ILE A 1 7 ? 42.503 15.119 -6.219 1.00 12.39 ? 7 ILE A CG2 1 ATOM 43 C CD1 . ILE A 1 7 ? 42.240 12.185 -6.704 1.00 21.25 ? 7 ILE A CD1 1 ATOM 44 N N . ILE A 1 8 ? 41.257 17.886 -7.662 1.00 9.43 ? 8 ILE A N 1 ATOM 45 C CA . ILE A 1 8 ? 41.816 19.217 -7.807 1.00 6.32 ? 8 ILE A CA 1 ATOM 46 C C . ILE A 1 8 ? 42.344 19.722 -6.472 1.00 12.63 ? 8 ILE A C 1 ATOM 47 O O . ILE A 1 8 ? 41.634 19.686 -5.462 1.00 8.44 ? 8 ILE A O 1 ATOM 48 C CB . ILE A 1 8 ? 40.796 20.219 -8.340 1.00 7.12 ? 8 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 8 ? 40.316 19.801 -9.734 1.00 8.62 ? 8 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 8 ? 41.398 21.582 -8.425 1.00 3.86 ? 8 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 8 ? 39.254 20.687 -10.287 1.00 6.64 ? 8 ILE A CD1 1 ATOM 52 N N . GLN A 1 9 ? 43.590 20.201 -6.500 1.00 6.59 ? 9 GLN A N 1 ATOM 53 C CA . GLN A 1 9 ? 44.185 20.955 -5.416 1.00 5.56 ? 9 GLN A CA 1 ATOM 54 C C . GLN A 1 9 ? 43.945 22.427 -5.765 1.00 7.76 ? 9 GLN A C 1 ATOM 55 O O . GLN A 1 9 ? 44.586 22.988 -6.673 1.00 6.78 ? 9 GLN A O 1 ATOM 56 C CB . GLN A 1 9 ? 45.681 20.657 -5.276 1.00 4.46 ? 9 GLN A CB 1 ATOM 57 C CG . GLN A 1 9 ? 46.417 21.543 -4.298 1.00 7.02 ? 9 GLN A CG 1 ATOM 58 C CD . GLN A 1 9 ? 47.931 21.310 -4.306 1.00 11.27 ? 9 GLN A CD 1 ATOM 59 O OE1 . GLN A 1 9 ? 48.397 20.189 -4.476 1.00 14.43 ? 9 GLN A OE1 1 ATOM 60 N NE2 . GLN A 1 9 ? 48.692 22.387 -4.199 1.00 7.14 ? 9 GLN A NE2 1 ATOM 61 N N . ALA A 1 10 ? 43.038 23.053 -5.028 1.00 4.30 ? 10 ALA A N 1 ATOM 62 C CA . ALA A 1 10 ? 42.618 24.413 -5.348 1.00 8.52 ? 10 ALA A CA 1 ATOM 63 C C . ALA A 1 10 ? 43.103 25.403 -4.304 1.00 5.52 ? 10 ALA A C 1 ATOM 64 O O . ALA A 1 10 ? 42.974 25.167 -3.102 1.00 6.69 ? 10 ALA A O 1 ATOM 65 C CB . ALA A 1 10 ? 41.105 24.481 -5.474 1.00 5.37 ? 10 ALA A CB 1 ATOM 66 N N . GLU A 1 11 ? 43.646 26.517 -4.771 1.00 5.17 ? 11 GLU A N 1 ATOM 67 C CA . GLU A 1 11 ? 44.199 27.519 -3.873 1.00 7.12 ? 11 GLU A CA 1 ATOM 68 C C . GLU A 1 11 ? 43.692 28.904 -4.267 1.00 6.89 ? 11 GLU A C 1 ATOM 69 O O . GLU A 1 11 ? 43.423 29.171 -5.438 1.00 6.88 ? 11 GLU A O 1 ATOM 70 C CB . GLU A 1 11 ? 45.738 27.518 -3.936 1.00 5.22 ? 11 GLU A CB 1 ATOM 71 C CG . GLU A 1 11 ? 46.407 26.172 -3.646 1.00 7.95 ? 11 GLU A CG 1 ATOM 72 C CD . GLU A 1 11 ? 47.860 26.114 -4.138 1.00 13.01 ? 11 GLU A CD 1 ATOM 73 O OE1 . GLU A 1 11 ? 48.460 27.199 -4.320 1.00 10.09 ? 11 GLU A OE1 1 ATOM 74 O OE2 . GLU A 1 11 ? 48.404 24.991 -4.339 1.00 11.63 ? 11 GLU A OE2 1 ATOM 75 N N . PHE A 1 12 ? 43.564 29.800 -3.303 1.00 6.86 ? 12 PHE A N 1 ATOM 76 C CA . PHE A 1 12 ? 43.407 31.202 -3.657 1.00 8.11 ? 12 PHE A CA 1 ATOM 77 C C . PHE A 1 12 ? 44.067 32.101 -2.621 1.00 8.70 ? 12 PHE A C 1 ATOM 78 O O . PHE A 1 12 ? 44.304 31.691 -1.490 1.00 10.45 ? 12 PHE A O 1 ATOM 79 C CB . PHE A 1 12 ? 41.921 31.581 -3.899 1.00 8.31 ? 12 PHE A CB 1 ATOM 80 C CG . PHE A 1 12 ? 41.052 31.649 -2.662 1.00 11.14 ? 12 PHE A CG 1 ATOM 81 C CD1 . PHE A 1 12 ? 41.112 32.733 -1.792 1.00 11.94 ? 12 PHE A CD1 1 ATOM 82 C CD2 . PHE A 1 12 ? 40.076 30.685 -2.444 1.00 14.59 ? 12 PHE A CD2 1 ATOM 83 C CE1 . PHE A 1 12 ? 40.274 32.806 -0.673 1.00 12.72 ? 12 PHE A CE1 1 ATOM 84 C CE2 . PHE A 1 12 ? 39.218 30.766 -1.337 1.00 13.57 ? 12 PHE A CE2 1 ATOM 85 C CZ . PHE A 1 12 ? 39.325 31.819 -0.451 1.00 9.54 ? 12 PHE A CZ 1 ATOM 86 N N . TYR A 1 13 ? 44.383 33.319 -3.043 1.00 8.03 ? 13 TYR A N 1 ATOM 87 C CA . TYR A 1 13 ? 44.816 34.369 -2.142 1.00 8.90 ? 13 TYR A CA 1 ATOM 88 C C . TYR A 1 13 ? 44.106 35.647 -2.563 1.00 9.23 ? 13 TYR A C 1 ATOM 89 O O . TYR A 1 13 ? 44.062 35.987 -3.735 1.00 11.85 ? 13 TYR A O 1 ATOM 90 C CB . TYR A 1 13 ? 46.336 34.550 -2.154 1.00 8.70 ? 13 TYR A CB 1 ATOM 91 C CG . TYR A 1 13 ? 46.785 35.455 -1.047 1.00 13.50 ? 13 TYR A CG 1 ATOM 92 C CD1 . TYR A 1 13 ? 47.081 34.948 0.209 1.00 15.13 ? 13 TYR A CD1 1 ATOM 93 C CD2 . TYR A 1 13 ? 46.870 36.835 -1.241 1.00 13.60 ? 13 TYR A CD2 1 ATOM 94 C CE1 . TYR A 1 13 ? 47.479 35.788 1.243 1.00 18.01 ? 13 TYR A CE1 1 ATOM 95 C CE2 . TYR A 1 13 ? 47.260 37.677 -0.218 1.00 18.89 ? 13 TYR A CE2 1 ATOM 96 C CZ . TYR A 1 13 ? 47.564 37.145 1.021 1.00 20.47 ? 13 TYR A CZ 1 ATOM 97 O OH . TYR A 1 13 ? 47.958 37.970 2.040 1.00 32.39 ? 13 TYR A OH 1 ATOM 98 N N . LEU A 1 14 ? 43.575 36.368 -1.594 1.00 7.93 ? 14 LEU A N 1 ATOM 99 C CA . LEU A 1 14 ? 42.754 37.531 -1.885 1.00 8.91 ? 14 LEU A CA 1 ATOM 100 C C . LEU A 1 14 ? 43.263 38.802 -1.200 1.00 15.29 ? 14 LEU A C 1 ATOM 101 O O . LEU A 1 14 ? 43.507 38.806 0.011 1.00 10.72 ? 14 LEU A O 1 ATOM 102 C CB . LEU A 1 14 ? 41.314 37.265 -1.454 1.00 8.41 ? 14 LEU A CB 1 ATOM 103 C CG . LEU A 1 14 ? 40.370 38.451 -1.646 1.00 9.87 ? 14 LEU A CG 1 ATOM 104 C CD1 . LEU A 1 14 ? 40.124 38.666 -3.130 1.00 6.01 ? 14 LEU A CD1 1 ATOM 105 C CD2 . LEU A 1 14 ? 39.065 38.172 -0.927 1.00 7.73 ? 14 LEU A CD2 1 ATOM 106 N N . ASN A 1 15 ? 43.451 39.862 -1.985 1.00 11.86 ? 15 ASN A N 1 ATOM 107 C CA . ASN A 1 15 ? 43.772 41.174 -1.430 1.00 8.61 ? 15 ASN A CA 1 ATOM 108 C C . ASN A 1 15 ? 42.554 42.116 -1.530 1.00 16.31 ? 15 ASN A C 1 ATOM 109 O O . ASN A 1 15 ? 41.750 41.979 -2.462 1.00 15.66 ? 15 ASN A O 1 ATOM 110 C CB . ASN A 1 15 ? 44.943 41.790 -2.188 1.00 8.17 ? 15 ASN A CB 1 ATOM 111 C CG . ASN A 1 15 ? 46.278 41.357 -1.640 1.00 13.00 ? 15 ASN A CG 1 ATOM 112 O OD1 . ASN A 1 15 ? 46.421 41.067 -0.447 1.00 12.88 ? 15 ASN A OD1 1 ATOM 113 N ND2 . ASN A 1 15 ? 47.286 41.343 -2.510 1.00 15.69 ? 15 ASN A ND2 1 ATOM 114 N N . PRO A 1 16 ? 42.403 43.075 -0.585 1.00 14.14 ? 16 PRO A N 1 ATOM 115 C CA . PRO A 1 16 ? 43.316 43.403 0.516 1.00 14.31 ? 16 PRO A CA 1 ATOM 116 C C . PRO A 1 16 ? 43.016 42.602 1.778 1.00 16.47 ? 16 PRO A C 1 ATOM 117 O O . PRO A 1 16 ? 43.642 42.841 2.810 1.00 19.03 ? 16 PRO A O 1 ATOM 118 C CB . PRO A 1 16 ? 43.040 44.887 0.757 1.00 15.47 ? 16 PRO A CB 1 ATOM 119 C CG . PRO A 1 16 ? 41.580 45.027 0.439 1.00 14.15 ? 16 PRO A CG 1 ATOM 120 C CD . PRO A 1 16 ? 41.341 44.093 -0.728 1.00 14.83 ? 16 PRO A CD 1 ATOM 121 N N . ASP A 1 17 ? 42.100 41.642 1.685 1.00 17.99 ? 17 ASP A N 1 ATOM 122 C CA . ASP A 1 17 ? 41.676 40.878 2.857 1.00 17.97 ? 17 ASP A CA 1 ATOM 123 C C . ASP A 1 17 ? 42.800 40.018 3.426 1.00 15.79 ? 17 ASP A C 1 ATOM 124 O O . ASP A 1 17 ? 42.773 39.641 4.601 1.00 21.45 ? 17 ASP A O 1 ATOM 125 C CB . ASP A 1 17 ? 40.459 40.008 2.518 1.00 16.50 ? 17 ASP A CB 1 ATOM 126 C CG . ASP A 1 17 ? 39.320 40.813 1.918 1.00 20.70 ? 17 ASP A CG 1 ATOM 127 O OD1 . ASP A 1 17 ? 39.406 41.187 0.722 1.00 19.37 ? 17 ASP A OD1 1 ATOM 128 O OD2 . ASP A 1 17 ? 38.338 41.083 2.645 1.00 28.80 ? 17 ASP A OD2 1 ATOM 129 N N . GLN A 1 18 ? 43.780 39.707 2.587 1.00 15.06 ? 18 GLN A N 1 ATOM 130 C CA . GLN A 1 18 ? 44.874 38.814 2.955 1.00 17.12 ? 18 GLN A CA 1 ATOM 131 C C . GLN A 1 18 ? 44.336 37.459 3.405 1.00 22.23 ? 18 GLN A C 1 ATOM 132 O O . GLN A 1 18 ? 44.820 36.862 4.373 1.00 19.13 ? 18 GLN A O 1 ATOM 133 C CB . GLN A 1 18 ? 45.755 39.444 4.035 1.00 20.85 ? 18 GLN A CB 1 ATOM 134 C CG . GLN A 1 18 ? 46.419 40.713 3.567 1.00 25.63 ? 18 GLN A CG 1 ATOM 135 C CD . GLN A 1 18 ? 47.509 41.196 4.496 1.00 34.56 ? 18 GLN A CD 1 ATOM 136 O OE1 . GLN A 1 18 ? 48.653 41.390 4.079 1.00 35.30 ? 18 GLN A OE1 1 ATOM 137 N NE2 . GLN A 1 18 ? 47.158 41.414 5.758 1.00 37.14 ? 18 GLN A NE2 1 ATOM 138 N N . SER A 1 19 ? 43.337 36.976 2.672 1.00 17.31 ? 19 SER A N 1 ATOM 139 C CA . SER A 1 19 ? 42.781 35.651 2.897 1.00 19.36 ? 19 SER A CA 1 ATOM 140 C C . SER A 1 19 ? 43.313 34.666 1.864 1.00 16.96 ? 19 SER A C 1 ATOM 141 O O . SER A 1 19 ? 43.286 34.923 0.662 1.00 20.93 ? 19 SER A O 1 ATOM 142 C CB . SER A 1 19 ? 41.261 35.702 2.842 1.00 18.24 ? 19 SER A CB 1 ATOM 143 O OG . SER A 1 19 ? 40.780 36.576 3.841 1.00 32.04 ? 19 SER A OG 1 ATOM 144 N N . GLY A 1 20 ? 43.792 33.531 2.346 1.00 12.81 ? 20 GLY A N 1 ATOM 145 C CA . GLY A 1 20 ? 44.299 32.479 1.488 1.00 13.55 ? 20 GLY A CA 1 ATOM 146 C C . GLY A 1 20 ? 43.738 31.124 1.868 1.00 25.50 ? 20 GLY A C 1 ATOM 147 O O . GLY A 1 20 ? 43.597 30.820 3.046 1.00 39.61 ? 20 GLY A O 1 ATOM 148 N N . GLU A 1 21 ? 43.354 30.330 0.877 1.00 14.74 ? 21 GLU A N 1 ATOM 149 C CA . GLU A 1 21 ? 42.733 29.045 1.145 1.00 10.71 ? 21 GLU A CA 1 ATOM 150 C C . GLU A 1 21 ? 43.448 27.903 0.409 1.00 8.68 ? 21 GLU A C 1 ATOM 151 O O . GLU A 1 21 ? 44.079 28.123 -0.626 1.00 8.90 ? 21 GLU A O 1 ATOM 152 C CB . GLU A 1 21 ? 41.254 29.127 0.768 1.00 14.01 ? 21 GLU A CB 1 ATOM 153 C CG . GLU A 1 21 ? 40.437 27.905 1.081 1.00 24.30 ? 21 GLU A CG 1 ATOM 154 C CD . GLU A 1 21 ? 39.026 28.036 0.555 1.00 33.33 ? 21 GLU A CD 1 ATOM 155 O OE1 . GLU A 1 21 ? 38.183 28.687 1.227 1.00 23.48 ? 21 GLU A OE1 1 ATOM 156 O OE2 . GLU A 1 21 ? 38.782 27.506 -0.550 1.00 33.92 ? 21 GLU A OE2 1 ATOM 157 N N . PHE A 1 22 ? 43.397 26.693 0.956 1.00 9.43 ? 22 PHE A N 1 ATOM 158 C CA . PHE A 1 22 ? 44.040 25.555 0.308 1.00 7.15 ? 22 PHE A CA 1 ATOM 159 C C . PHE A 1 22 ? 43.151 24.333 0.533 1.00 10.12 ? 22 PHE A C 1 ATOM 160 O O . PHE A 1 22 ? 42.860 23.990 1.673 1.00 9.55 ? 22 PHE A O 1 ATOM 161 C CB . PHE A 1 22 ? 45.446 25.350 0.903 1.00 8.80 ? 22 PHE A CB 1 ATOM 162 C CG . PHE A 1 22 ? 46.222 24.214 0.308 1.00 11.87 ? 22 PHE A CG 1 ATOM 163 C CD1 . PHE A 1 22 ? 47.256 24.466 -0.562 1.00 9.81 ? 22 PHE A CD1 1 ATOM 164 C CD2 . PHE A 1 22 ? 45.922 22.894 0.619 1.00 11.73 ? 22 PHE A CD2 1 ATOM 165 C CE1 . PHE A 1 22 ? 47.992 23.422 -1.117 1.00 11.61 ? 22 PHE A CE1 1 ATOM 166 C CE2 . PHE A 1 22 ? 46.645 21.849 0.061 1.00 14.36 ? 22 PHE A CE2 1 ATOM 167 C CZ . PHE A 1 22 ? 47.681 22.116 -0.808 1.00 13.78 ? 22 PHE A CZ 1 ATOM 168 N N . MET A 1 23 ? 42.741 23.658 -0.538 1.00 11.15 ? 23 MET A N 1 ATOM 169 C CA . MET A 1 23 ? 41.895 22.479 -0.383 1.00 8.48 ? 23 MET A CA 1 ATOM 170 C C . MET A 1 23 ? 42.054 21.470 -1.517 1.00 7.52 ? 23 MET A C 1 ATOM 171 O O . MET A 1 23 ? 42.593 21.784 -2.575 1.00 8.41 ? 23 MET A O 1 ATOM 172 C CB . MET A 1 23 ? 40.418 22.883 -0.278 1.00 11.29 ? 23 MET A CB 1 ATOM 173 C CG . MET A 1 23 ? 39.856 23.615 -1.495 1.00 9.57 ? 23 MET A CG 1 ATOM 174 S SD . MET A 1 23 ? 39.102 22.507 -2.714 1.00 15.85 ? 23 MET A SD 1 ATOM 175 C CE . MET A 1 23 ? 37.679 21.855 -1.822 1.00 11.52 ? 23 MET A CE 1 ATOM 176 N N . PHE A 1 24 ? 41.558 20.262 -1.287 1.00 5.40 ? 24 PHE A N 1 ATOM 177 C CA . PHE A 1 24 ? 41.498 19.231 -2.314 1.00 12.81 ? 24 PHE A CA 1 ATOM 178 C C . PHE A 1 24 ? 40.027 18.932 -2.609 1.00 10.34 ? 24 PHE A C 1 ATOM 179 O O . PHE A 1 24 ? 39.211 18.823 -1.687 1.00 6.81 ? 24 PHE A O 1 ATOM 180 C CB . PHE A 1 24 ? 42.217 17.952 -1.882 1.00 11.19 ? 24 PHE A CB 1 ATOM 181 C CG . PHE A 1 24 ? 43.660 17.861 -2.329 1.00 10.98 ? 24 PHE A CG 1 ATOM 182 C CD1 . PHE A 1 24 ? 44.651 18.578 -1.677 1.00 12.49 ? 24 PHE A CD1 1 ATOM 183 C CD2 . PHE A 1 24 ? 44.029 17.020 -3.361 1.00 9.34 ? 24 PHE A CD2 1 ATOM 184 C CE1 . PHE A 1 24 ? 45.990 18.471 -2.066 1.00 15.36 ? 24 PHE A CE1 1 ATOM 185 C CE2 . PHE A 1 24 ? 45.360 16.907 -3.755 1.00 12.53 ? 24 PHE A CE2 1 ATOM 186 C CZ . PHE A 1 24 ? 46.341 17.636 -3.103 1.00 12.97 ? 24 PHE A CZ 1 ATOM 187 N N . ASP A 1 25 ? 39.706 18.778 -3.892 1.00 11.81 ? 25 ASP A N 1 ATOM 188 C CA . ASP A 1 25 ? 38.337 18.532 -4.331 1.00 10.29 ? 25 ASP A CA 1 ATOM 189 C C . ASP A 1 25 ? 38.344 17.190 -5.082 1.00 14.46 ? 25 ASP A C 1 ATOM 190 O O . ASP A 1 25 ? 39.240 16.918 -5.884 1.00 13.44 ? 25 ASP A O 1 ATOM 191 C CB . ASP A 1 25 ? 37.868 19.659 -5.259 1.00 10.60 ? 25 ASP A CB 1 ATOM 192 C CG . ASP A 1 25 ? 36.457 19.462 -5.783 1.00 18.75 ? 25 ASP A CG 1 ATOM 193 O OD1 . ASP A 1 25 ? 35.554 20.184 -5.297 1.00 19.92 ? 25 ASP A OD1 1 ATOM 194 O OD2 . ASP A 1 25 ? 36.235 18.567 -6.635 1.00 19.20 ? 25 ASP A OD2 1 ATOM 195 N N . PHE A 1 26 ? 37.351 16.353 -4.824 1.00 8.92 ? 26 PHE A N 1 ATOM 196 C CA . PHE A 1 26 ? 37.185 15.122 -5.574 1.00 11.75 ? 26 PHE A CA 1 ATOM 197 C C . PHE A 1 26 ? 35.801 15.154 -6.199 1.00 12.15 ? 26 PHE A C 1 ATOM 198 O O . PHE A 1 26 ? 34.804 15.146 -5.481 1.00 12.20 ? 26 PHE A O 1 ATOM 199 C CB . PHE A 1 26 ? 37.351 13.904 -4.659 1.00 12.74 ? 26 PHE A CB 1 ATOM 200 C CG . PHE A 1 26 ? 37.077 12.591 -5.332 1.00 16.62 ? 26 PHE A CG 1 ATOM 201 C CD1 . PHE A 1 26 ? 38.079 11.921 -6.019 1.00 17.15 ? 26 PHE A CD1 1 ATOM 202 C CD2 . PHE A 1 26 ? 35.814 12.018 -5.270 1.00 13.53 ? 26 PHE A CD2 1 ATOM 203 C CE1 . PHE A 1 26 ? 37.820 10.707 -6.652 1.00 18.60 ? 26 PHE A CE1 1 ATOM 204 C CE2 . PHE A 1 26 ? 35.545 10.806 -5.898 1.00 12.79 ? 26 PHE A CE2 1 ATOM 205 C CZ . PHE A 1 26 ? 36.548 10.148 -6.588 1.00 20.37 ? 26 PHE A CZ 1 ATOM 206 N N . ASP A 1 27 ? 35.749 15.237 -7.527 1.00 14.95 ? 27 ASP A N 1 ATOM 207 C CA . ASP A 1 27 ? 34.478 15.216 -8.247 1.00 19.77 ? 27 ASP A CA 1 ATOM 208 C C . ASP A 1 27 ? 33.476 16.213 -7.673 1.00 14.78 ? 27 ASP A C 1 ATOM 209 O O . ASP A 1 27 ? 32.290 15.939 -7.670 1.00 14.20 ? 27 ASP A O 1 ATOM 210 C CB . ASP A 1 27 ? 33.896 13.796 -8.259 1.00 15.71 ? 27 ASP A CB 1 ATOM 211 C CG . ASP A 1 27 ? 34.698 12.852 -9.138 1.00 14.95 ? 27 ASP A CG 1 ATOM 212 O OD1 . ASP A 1 27 ? 35.605 13.340 -9.838 1.00 25.14 ? 27 ASP A OD1 1 ATOM 213 O OD2 . ASP A 1 27 ? 34.447 11.629 -9.128 1.00 17.72 ? 27 ASP A OD2 1 ATOM 214 N N . GLY A 1 28 ? 33.955 17.343 -7.156 1.00 12.01 ? 28 GLY A N 1 ATOM 215 C CA . GLY A 1 28 ? 33.062 18.370 -6.636 1.00 15.54 ? 28 GLY A CA 1 ATOM 216 C C . GLY A 1 28 ? 32.804 18.366 -5.127 1.00 17.57 ? 28 GLY A C 1 ATOM 217 O O . GLY A 1 28 ? 32.134 19.260 -4.606 1.00 20.30 ? 28 GLY A O 1 ATOM 218 N N . ASP A 1 29 ? 33.350 17.390 -4.410 1.00 13.15 ? 29 ASP A N 1 ATOM 219 C CA . ASP A 1 29 ? 33.248 17.382 -2.950 1.00 13.86 ? 29 ASP A CA 1 ATOM 220 C C . ASP A 1 29 ? 34.598 17.663 -2.297 1.00 12.65 ? 29 ASP A C 1 ATOM 221 O O . ASP A 1 29 ? 35.658 17.351 -2.839 1.00 13.23 ? 29 ASP A O 1 ATOM 222 C CB . ASP A 1 29 ? 32.674 16.052 -2.442 1.00 11.72 ? 29 ASP A CB 1 ATOM 223 C CG . ASP A 1 29 ? 31.153 16.004 -2.543 1.00 14.45 ? 29 ASP A CG 1 ATOM 224 O OD1 . ASP A 1 29 ? 30.456 16.727 -1.786 1.00 13.95 ? 29 ASP A OD1 1 ATOM 225 O OD2 . ASP A 1 29 ? 30.658 15.275 -3.424 1.00 12.04 ? 29 ASP A OD2 1 ATOM 226 N N . GLU A 1 30 ? 34.558 18.280 -1.132 1.00 11.58 ? 30 GLU A N 1 ATOM 227 C CA . GLU A 1 30 ? 35.785 18.645 -0.466 1.00 17.54 ? 30 GLU A CA 1 ATOM 228 C C . GLU A 1 30 ? 36.366 17.432 0.237 1.00 15.62 ? 30 GLU A C 1 ATOM 229 O O . GLU A 1 30 ? 35.659 16.763 0.986 1.00 19.82 ? 30 GLU A O 1 ATOM 230 C CB . GLU A 1 30 ? 35.532 19.763 0.539 1.00 8.51 ? 30 GLU A CB 1 ATOM 231 C CG . GLU A 1 30 ? 36.749 20.059 1.379 1.00 17.15 ? 30 GLU A CG 1 ATOM 232 C CD . GLU A 1 30 ? 36.453 20.947 2.548 1.00 16.74 ? 30 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 30 ? 35.306 21.456 2.646 1.00 14.97 ? 30 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 30 ? 37.373 21.126 3.372 1.00 19.27 ? 30 GLU A OE2 1 ATOM 235 N N . ILE A 1 31 ? 37.625 17.102 -0.057 1.00 17.61 ? 31 ILE A N 1 ATOM 236 C CA . ILE A 1 31 ? 38.312 16.034 0.685 1.00 13.51 ? 31 ILE A CA 1 ATOM 237 C C . ILE A 1 31 ? 38.799 16.583 2.023 1.00 12.02 ? 31 ILE A C 1 ATOM 238 O O . ILE A 1 31 ? 38.524 16.018 3.089 1.00 9.87 ? 31 ILE A O 1 ATOM 239 C CB . ILE A 1 31 ? 39.504 15.444 -0.098 1.00 15.67 ? 31 ILE A CB 1 ATOM 240 C CG1 . ILE A 1 31 ? 39.064 14.953 -1.477 1.00 12.57 ? 31 ILE A CG1 1 ATOM 241 C CG2 . ILE A 1 31 ? 40.153 14.293 0.688 1.00 13.56 ? 31 ILE A CG2 1 ATOM 242 C CD1 . ILE A 1 31 ? 40.210 14.373 -2.289 1.00 12.13 ? 31 ILE A CD1 1 ATOM 243 N N . PHE A 1 32 ? 39.532 17.690 1.949 1.00 10.39 ? 32 PHE A N 1 ATOM 244 C CA . PHE A 1 32 ? 40.001 18.393 3.137 1.00 16.67 ? 32 PHE A CA 1 ATOM 245 C C . PHE A 1 32 ? 40.384 19.825 2.784 1.00 13.89 ? 32 PHE A C 1 ATOM 246 O O . PHE A 1 32 ? 40.530 20.163 1.616 1.00 10.37 ? 32 PHE A O 1 ATOM 247 C CB . PHE A 1 32 ? 41.210 17.682 3.777 1.00 11.34 ? 32 PHE A CB 1 ATOM 248 C CG . PHE A 1 32 ? 42.484 17.777 2.975 1.00 10.18 ? 32 PHE A CG 1 ATOM 249 C CD1 . PHE A 1 32 ? 43.365 18.837 3.170 1.00 20.03 ? 32 PHE A CD1 1 ATOM 250 C CD2 . PHE A 1 32 ? 42.821 16.798 2.050 1.00 16.88 ? 32 PHE A CD2 1 ATOM 251 C CE1 . PHE A 1 32 ? 44.555 18.935 2.443 1.00 14.88 ? 32 PHE A CE1 1 ATOM 252 C CE2 . PHE A 1 32 ? 44.005 16.887 1.318 1.00 13.42 ? 32 PHE A CE2 1 ATOM 253 C CZ . PHE A 1 32 ? 44.874 17.963 1.519 1.00 16.62 ? 32 PHE A CZ 1 ATOM 254 N N . HIS A 1 33 ? 40.545 20.663 3.800 1.00 11.54 ? 33 HIS A N 1 ATOM 255 C CA . HIS A 1 33 ? 41.211 21.937 3.604 1.00 15.64 ? 33 HIS A CA 1 ATOM 256 C C . HIS A 1 33 ? 42.221 22.115 4.720 1.00 17.98 ? 33 HIS A C 1 ATOM 257 O O . HIS A 1 33 ? 42.198 21.381 5.707 1.00 15.27 ? 33 HIS A O 1 ATOM 258 C CB . HIS A 1 33 ? 40.217 23.094 3.577 1.00 11.99 ? 33 HIS A CB 1 ATOM 259 C CG . HIS A 1 33 ? 39.575 23.373 4.901 1.00 16.66 ? 33 HIS A CG 1 ATOM 260 N ND1 . HIS A 1 33 ? 38.405 22.761 5.301 1.00 18.72 ? 33 HIS A ND1 1 ATOM 261 C CD2 . HIS A 1 33 ? 39.924 24.209 5.906 1.00 14.53 ? 33 HIS A CD2 1 ATOM 262 C CE1 . HIS A 1 33 ? 38.065 23.203 6.499 1.00 13.87 ? 33 HIS A CE1 1 ATOM 263 N NE2 . HIS A 1 33 ? 38.971 24.081 6.889 1.00 19.36 ? 33 HIS A NE2 1 ATOM 264 N N . VAL A 1 34 ? 43.090 23.104 4.570 1.00 12.15 ? 34 VAL A N 1 ATOM 265 C CA . VAL A 1 34 ? 44.054 23.425 5.601 1.00 18.98 ? 34 VAL A CA 1 ATOM 266 C C . VAL A 1 34 ? 43.632 24.698 6.288 1.00 19.68 ? 34 VAL A C 1 ATOM 267 O O . VAL A 1 34 ? 43.399 25.713 5.634 1.00 16.34 ? 34 VAL A O 1 ATOM 268 C CB . VAL A 1 34 ? 45.477 23.604 5.027 1.00 18.35 ? 34 VAL A CB 1 ATOM 269 C CG1 . VAL A 1 34 ? 46.402 24.224 6.059 1.00 18.43 ? 34 VAL A CG1 1 ATOM 270 C CG2 . VAL A 1 34 ? 46.014 22.275 4.496 1.00 17.83 ? 34 VAL A CG2 1 ATOM 271 N N . ASP A 1 35 ? 43.460 24.603 7.601 1.00 21.14 ? 35 ASP A N 1 ATOM 272 C CA . ASP A 1 35 ? 43.242 25.753 8.465 1.00 29.34 ? 35 ASP A CA 1 ATOM 273 C C . ASP A 1 35 ? 44.552 26.527 8.590 1.00 30.35 ? 35 ASP A C 1 ATOM 274 O O . ASP A 1 35 ? 45.469 26.059 9.263 1.00 27.75 ? 35 ASP A O 1 ATOM 275 C CB . ASP A 1 35 ? 42.720 25.314 9.838 1.00 27.69 ? 35 ASP A CB 1 ATOM 276 C CG . ASP A 1 35 ? 42.303 26.487 10.717 1.00 35.06 ? 35 ASP A CG 1 ATOM 277 O OD1 . ASP A 1 35 ? 42.930 27.569 10.642 1.00 31.05 ? 35 ASP A OD1 1 ATOM 278 O OD2 . ASP A 1 35 ? 41.323 26.327 11.477 1.00 42.97 ? 35 ASP A OD2 1 ATOM 279 N N . MET A 1 36 ? 44.669 27.667 7.913 1.00 30.47 ? 36 MET A N 1 ATOM 280 C CA . MET A 1 36 ? 45.948 28.385 7.864 1.00 30.55 ? 36 MET A CA 1 ATOM 281 C C . MET A 1 36 ? 46.392 28.939 9.216 1.00 32.61 ? 36 MET A C 1 ATOM 282 O O . MET A 1 36 ? 47.581 28.928 9.530 1.00 43.45 ? 36 MET A O 1 ATOM 283 C CB . MET A 1 36 ? 45.897 29.537 6.860 1.00 35.45 ? 36 MET A CB 1 ATOM 284 C CG . MET A 1 36 ? 45.456 29.155 5.477 1.00 41.98 ? 36 MET A CG 1 ATOM 285 S SD . MET A 1 36 ? 46.536 27.892 4.781 1.00 43.84 ? 36 MET A SD 1 ATOM 286 C CE . MET A 1 36 ? 45.688 27.633 3.253 1.00 33.50 ? 36 MET A CE 1 ATOM 287 N N . ALA A 1 37 ? 45.447 29.433 10.008 1.00 36.42 ? 37 ALA A N 1 ATOM 288 C CA . ALA A 1 37 ? 45.777 30.012 11.309 1.00 36.34 ? 37 ALA A CA 1 ATOM 289 C C . ALA A 1 37 ? 46.265 28.943 12.282 1.00 37.36 ? 37 ALA A C 1 ATOM 290 O O . ALA A 1 37 ? 47.220 29.162 13.028 1.00 45.85 ? 37 ALA A O 1 ATOM 291 C CB . ALA A 1 37 ? 44.581 30.745 11.884 1.00 33.81 ? 37 ALA A CB 1 ATOM 292 N N . LYS A 1 38 ? 45.624 27.780 12.249 1.00 36.81 ? 38 LYS A N 1 ATOM 293 C CA . LYS A 1 38 ? 45.985 26.686 13.138 1.00 34.79 ? 38 LYS A CA 1 ATOM 294 C C . LYS A 1 38 ? 47.053 25.795 12.513 1.00 31.73 ? 38 LYS A C 1 ATOM 295 O O . LYS A 1 38 ? 47.638 24.965 13.205 1.00 32.60 ? 38 LYS A O 1 ATOM 296 C CB . LYS A 1 38 ? 44.747 25.833 13.455 1.00 34.86 ? 38 LYS A CB 1 ATOM 297 C CG . LYS A 1 38 ? 43.635 26.535 14.217 1.00 40.44 ? 38 LYS A CG 1 ATOM 298 C CD . LYS A 1 38 ? 42.582 25.528 14.667 1.00 47.32 ? 38 LYS A CD 1 ATOM 299 C CE . LYS A 1 38 ? 41.466 26.193 15.459 1.00 43.97 ? 38 LYS A CE 1 ATOM 300 N NZ . LYS A 1 38 ? 40.569 25.195 16.103 1.00 41.22 ? 38 LYS A NZ 1 ATOM 301 N N . LYS A 1 39 ? 47.312 25.977 11.217 1.00 29.84 ? 39 LYS A N 1 ATOM 302 C CA . LYS A 1 39 ? 48.267 25.131 10.497 1.00 28.96 ? 39 LYS A CA 1 ATOM 303 C C . LYS A 1 39 ? 47.864 23.672 10.667 1.00 27.56 ? 39 LYS A C 1 ATOM 304 O O . LYS A 1 39 ? 48.693 22.815 10.974 1.00 27.62 ? 39 LYS A O 1 ATOM 305 C CB . LYS A 1 39 ? 49.695 25.383 10.989 1.00 29.51 ? 39 LYS A CB 1 ATOM 306 C CG . LYS A 1 39 ? 50.106 26.832 10.801 1.00 36.47 ? 39 LYS A CG 1 ATOM 307 C CD . LYS A 1 39 ? 51.298 27.220 11.640 1.00 45.10 ? 39 LYS A CD 1 ATOM 308 C CE . LYS A 1 39 ? 51.690 28.663 11.352 1.00 42.86 ? 39 LYS A CE 1 ATOM 309 N NZ . LYS A 1 39 ? 53.035 28.999 11.894 1.00 62.92 ? 39 LYS A NZ 1 ATOM 310 N N . GLU A 1 40 ? 46.584 23.391 10.434 1.00 33.37 ? 40 GLU A N 1 ATOM 311 C CA . GLU A 1 40 ? 46.064 22.034 10.584 1.00 28.79 ? 40 GLU A CA 1 ATOM 312 C C . GLU A 1 40 ? 45.232 21.536 9.413 1.00 25.94 ? 40 GLU A C 1 ATOM 313 O O . GLU A 1 40 ? 44.490 22.293 8.786 1.00 20.41 ? 40 GLU A O 1 ATOM 314 C CB . GLU A 1 40 ? 45.184 21.965 11.844 1.00 27.74 ? 40 GLU A CB 1 ATOM 315 C CG . GLU A 1 40 ? 45.868 22.341 13.156 1.00 51.45 ? 40 GLU A CG 1 ATOM 316 C CD . GLU A 1 40 ? 44.912 22.329 14.349 1.00 56.67 ? 40 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 40 ? 43.899 21.597 14.300 1.00 53.44 ? 40 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 40 ? 45.181 23.051 15.338 1.00 55.80 ? 40 GLU A OE2 1 ATOM 319 N N . THR A 1 41 ? 45.358 20.243 9.137 1.00 17.55 ? 41 THR A N 1 ATOM 320 C CA . THR A 1 41 ? 44.589 19.629 8.082 1.00 22.67 ? 41 THR A CA 1 ATOM 321 C C . THR A 1 41 ? 43.216 19.288 8.638 1.00 27.64 ? 41 THR A C 1 ATOM 322 O O . THR A 1 41 ? 43.120 18.564 9.626 1.00 26.87 ? 41 THR A O 1 ATOM 323 C CB . THR A 1 41 ? 45.257 18.348 7.582 1.00 26.43 ? 41 THR A CB 1 ATOM 324 O OG1 . THR A 1 41 ? 46.542 18.660 7.024 1.00 30.64 ? 41 THR A OG1 1 ATOM 325 C CG2 . THR A 1 41 ? 44.377 17.654 6.549 1.00 24.37 ? 41 THR A CG2 1 ATOM 326 N N . VAL A 1 42 ? 42.163 19.768 7.975 1.00 22.55 ? 42 VAL A N 1 ATOM 327 C CA . VAL A 1 42 ? 40.781 19.520 8.400 1.00 16.58 ? 42 VAL A CA 1 ATOM 328 C C . VAL A 1 42 ? 40.051 18.657 7.375 1.00 17.09 ? 42 VAL A C 1 ATOM 329 O O . VAL A 1 42 ? 39.703 19.125 6.287 1.00 14.84 ? 42 VAL A O 1 ATOM 330 C CB . VAL A 1 42 ? 40.000 20.841 8.621 1.00 21.12 ? 42 VAL A CB 1 ATOM 331 C CG1 . VAL A 1 42 ? 38.583 20.555 9.113 1.00 17.14 ? 42 VAL A CG1 1 ATOM 332 C CG2 . VAL A 1 42 ? 40.744 21.753 9.607 1.00 19.25 ? 42 VAL A CG2 1 ATOM 333 N N . TRP A 1 43 ? 39.825 17.394 7.716 1.00 18.92 ? 43 TRP A N 1 ATOM 334 C CA . TRP A 1 43 ? 39.150 16.480 6.801 1.00 17.11 ? 43 TRP A CA 1 ATOM 335 C C . TRP A 1 43 ? 37.636 16.739 6.809 1.00 24.69 ? 43 TRP A C 1 ATOM 336 O O . TRP A 1 43 ? 37.040 16.986 7.862 1.00 27.12 ? 43 TRP A O 1 ATOM 337 C CB . TRP A 1 43 ? 39.470 15.025 7.175 1.00 21.00 ? 43 TRP A CB 1 ATOM 338 C CG . TRP A 1 43 ? 40.938 14.715 7.108 1.00 20.08 ? 43 TRP A CG 1 ATOM 339 C CD1 . TRP A 1 43 ? 41.834 14.787 8.134 1.00 24.81 ? 43 TRP A CD1 1 ATOM 340 C CD2 . TRP A 1 43 ? 41.686 14.292 5.953 1.00 18.59 ? 43 TRP A CD2 1 ATOM 341 N NE1 . TRP A 1 43 ? 43.093 14.443 7.694 1.00 20.85 ? 43 TRP A NE1 1 ATOM 342 C CE2 . TRP A 1 43 ? 43.031 14.136 6.361 1.00 18.72 ? 43 TRP A CE2 1 ATOM 343 C CE3 . TRP A 1 43 ? 41.353 14.038 4.618 1.00 15.60 ? 43 TRP A CE3 1 ATOM 344 C CZ2 . TRP A 1 43 ? 44.040 13.733 5.483 1.00 18.41 ? 43 TRP A CZ2 1 ATOM 345 C CZ3 . TRP A 1 43 ? 42.352 13.641 3.747 1.00 17.09 ? 43 TRP A CZ3 1 ATOM 346 C CH2 . TRP A 1 43 ? 43.682 13.491 4.182 1.00 22.90 ? 43 TRP A CH2 1 ATOM 347 N N . ARG A 1 44 ? 37.025 16.699 5.627 1.00 17.22 ? 44 ARG A N 1 ATOM 348 C CA . ARG A 1 44 ? 35.618 17.062 5.486 1.00 20.83 ? 44 ARG A CA 1 ATOM 349 C C . ARG A 1 44 ? 34.697 16.073 6.187 1.00 20.02 ? 44 ARG A C 1 ATOM 350 O O . ARG A 1 44 ? 33.698 16.468 6.794 1.00 18.54 ? 44 ARG A O 1 ATOM 351 C CB . ARG A 1 44 ? 35.241 17.190 4.011 1.00 16.49 ? 44 ARG A CB 1 ATOM 352 C CG . ARG A 1 44 ? 33.801 17.596 3.778 1.00 12.98 ? 44 ARG A CG 1 ATOM 353 C CD . ARG A 1 44 ? 33.491 18.930 4.416 1.00 11.26 ? 44 ARG A CD 1 ATOM 354 N NE . ARG A 1 44 ? 32.092 19.306 4.215 1.00 15.95 ? 44 ARG A NE 1 ATOM 355 C CZ . ARG A 1 44 ? 31.090 18.943 5.012 1.00 18.93 ? 44 ARG A CZ 1 ATOM 356 N NH1 . ARG A 1 44 ? 31.330 18.171 6.064 1.00 12.36 ? 44 ARG A NH1 1 ATOM 357 N NH2 . ARG A 1 44 ? 29.842 19.343 4.747 1.00 12.28 ? 44 ARG A NH2 1 ATOM 358 N N . LEU A 1 45 ? 35.030 14.794 6.053 1.00 19.76 ? 45 LEU A N 1 ATOM 359 C CA . LEU A 1 45 ? 34.437 13.727 6.846 1.00 23.64 ? 45 LEU A CA 1 ATOM 360 C C . LEU A 1 45 ? 35.557 13.160 7.716 1.00 33.73 ? 45 LEU A C 1 ATOM 361 O O . LEU A 1 45 ? 36.673 12.928 7.228 1.00 24.94 ? 45 LEU A O 1 ATOM 362 C CB . LEU A 1 45 ? 33.816 12.640 5.961 1.00 27.29 ? 45 LEU A CB 1 ATOM 363 C CG . LEU A 1 45 ? 32.684 13.093 5.028 1.00 23.88 ? 45 LEU A CG 1 ATOM 364 C CD1 . LEU A 1 45 ? 31.958 11.905 4.384 1.00 20.38 ? 45 LEU A CD1 1 ATOM 365 C CD2 . LEU A 1 45 ? 31.702 13.977 5.780 1.00 21.65 ? 45 LEU A CD2 1 ATOM 366 N N . GLU A 1 46 ? 35.265 12.971 9.003 1.00 34.44 ? 46 GLU A N 1 ATOM 367 C CA . GLU A 1 46 ? 36.263 12.538 9.981 1.00 36.83 ? 46 GLU A CA 1 ATOM 368 C C . GLU A 1 46 ? 36.944 11.225 9.630 1.00 33.15 ? 46 GLU A C 1 ATOM 369 O O . GLU A 1 46 ? 38.125 11.035 9.911 1.00 34.57 ? 46 GLU A O 1 ATOM 370 C CB . GLU A 1 46 ? 35.613 12.410 11.360 1.00 55.14 ? 46 GLU A CB 1 ATOM 371 C CG . GLU A 1 46 ? 36.601 12.213 12.501 1.00 64.43 ? 46 GLU A CG 1 ATOM 372 C CD . GLU A 1 46 ? 37.037 13.519 13.143 1.00 79.80 ? 46 GLU A CD 1 ATOM 373 O OE1 . GLU A 1 46 ? 37.364 14.473 12.407 1.00 79.36 ? 46 GLU A OE1 1 ATOM 374 O OE2 . GLU A 1 46 ? 37.062 13.589 14.391 1.00 93.01 ? 46 GLU A OE2 1 ATOM 375 N N . GLU A 1 47 ? 36.195 10.337 8.987 1.00 33.71 ? 47 GLU A N 1 ATOM 376 C CA . GLU A 1 47 ? 36.699 9.029 8.594 1.00 34.54 ? 47 GLU A CA 1 ATOM 377 C C . GLU A 1 47 ? 37.922 9.105 7.683 1.00 39.88 ? 47 GLU A C 1 ATOM 378 O O . GLU A 1 47 ? 38.783 8.226 7.711 1.00 34.58 ? 47 GLU A O 1 ATOM 379 C CB . GLU A 1 47 ? 35.601 8.234 7.890 1.00 34.51 ? 47 GLU A CB 1 ATOM 380 C CG . GLU A 1 47 ? 34.259 8.274 8.589 1.00 55.55 ? 47 GLU A CG 1 ATOM 381 C CD . GLU A 1 47 ? 33.316 9.303 7.987 1.00 55.68 ? 47 GLU A CD 1 ATOM 382 O OE1 . GLU A 1 47 ? 33.108 10.372 8.616 1.00 40.40 ? 47 GLU A OE1 1 ATOM 383 O OE2 . GLU A 1 47 ? 32.781 9.030 6.886 1.00 52.16 ? 47 GLU A OE2 1 ATOM 384 N N . PHE A 1 48 ? 37.983 10.162 6.880 1.00 30.99 ? 48 PHE A N 1 ATOM 385 C CA . PHE A 1 48 ? 39.038 10.348 5.892 1.00 22.43 ? 48 PHE A CA 1 ATOM 386 C C . PHE A 1 48 ? 40.416 10.335 6.546 1.00 27.05 ? 48 PHE A C 1 ATOM 387 O O . PHE A 1 48 ? 41.362 9.764 5.997 1.00 30.13 ? 48 PHE A O 1 ATOM 388 C CB . PHE A 1 48 ? 38.833 11.670 5.120 1.00 25.36 ? 48 PHE A CB 1 ATOM 389 C CG . PHE A 1 48 ? 37.601 11.698 4.237 1.00 20.82 ? 48 PHE A CG 1 ATOM 390 C CD1 . PHE A 1 48 ? 37.233 12.868 3.590 1.00 20.98 ? 48 PHE A CD1 1 ATOM 391 C CD2 . PHE A 1 48 ? 36.830 10.566 4.038 1.00 23.87 ? 48 PHE A CD2 1 ATOM 392 C CE1 . PHE A 1 48 ? 36.117 12.918 2.775 1.00 16.95 ? 48 PHE A CE1 1 ATOM 393 C CE2 . PHE A 1 48 ? 35.708 10.602 3.217 1.00 22.93 ? 48 PHE A CE2 1 ATOM 394 C CZ . PHE A 1 48 ? 35.351 11.782 2.587 1.00 25.35 ? 48 PHE A CZ 1 ATOM 395 N N . GLY A 1 49 ? 40.519 10.928 7.735 1.00 23.33 ? 49 GLY A N 1 ATOM 396 C CA . GLY A 1 49 ? 41.808 11.077 8.388 1.00 29.75 ? 49 GLY A CA 1 ATOM 397 C C . GLY A 1 49 ? 42.356 9.786 8.967 1.00 30.50 ? 49 GLY A C 1 ATOM 398 O O . GLY A 1 49 ? 43.502 9.741 9.402 1.00 33.07 ? 49 GLY A O 1 ATOM 399 N N . ARG A 1 50 ? 41.538 8.738 8.973 1.00 29.47 ? 50 ARG A N 1 ATOM 400 C CA . ARG A 1 50 ? 41.980 7.422 9.420 1.00 44.29 ? 50 ARG A CA 1 ATOM 401 C C . ARG A 1 50 ? 42.694 6.676 8.286 1.00 46.51 ? 50 ARG A C 1 ATOM 402 O O . ARG A 1 50 ? 43.435 5.721 8.530 1.00 41.58 ? 50 ARG A O 1 ATOM 403 C CB . ARG A 1 50 ? 40.801 6.613 9.978 1.00 35.42 ? 50 ARG A CB 1 ATOM 404 C CG . ARG A 1 50 ? 40.203 7.271 11.223 1.00 43.52 ? 50 ARG A CG 1 ATOM 405 C CD . ARG A 1 50 ? 39.323 6.340 12.040 1.00 45.71 ? 50 ARG A CD 1 ATOM 406 N NE . ARG A 1 50 ? 38.194 5.818 11.276 1.00 64.34 ? 50 ARG A NE 1 ATOM 407 C CZ . ARG A 1 50 ? 36.964 6.328 11.324 1.00 71.88 ? 50 ARG A CZ 1 ATOM 408 N NH1 . ARG A 1 50 ? 36.701 7.382 12.096 1.00 52.86 ? 50 ARG A NH1 1 ATOM 409 N NH2 . ARG A 1 50 ? 35.994 5.786 10.595 1.00 57.87 ? 50 ARG A NH2 1 ATOM 410 N N . PHE A 1 51 ? 42.476 7.124 7.050 1.00 37.35 ? 51 PHE A N 1 ATOM 411 C CA . PHE A 1 51 ? 42.998 6.426 5.873 1.00 39.46 ? 51 PHE A CA 1 ATOM 412 C C . PHE A 1 51 ? 44.125 7.204 5.191 1.00 33.05 ? 51 PHE A C 1 ATOM 413 O O . PHE A 1 51 ? 44.920 6.631 4.444 1.00 30.38 ? 51 PHE A O 1 ATOM 414 C CB . PHE A 1 51 ? 41.876 6.134 4.870 1.00 36.52 ? 51 PHE A CB 1 ATOM 415 C CG . PHE A 1 51 ? 40.767 5.295 5.433 1.00 44.39 ? 51 PHE A CG 1 ATOM 416 C CD1 . PHE A 1 51 ? 39.694 5.881 6.084 1.00 43.97 ? 51 PHE A CD1 1 ATOM 417 C CD2 . PHE A 1 51 ? 40.805 3.912 5.321 1.00 49.19 ? 51 PHE A CD2 1 ATOM 418 C CE1 . PHE A 1 51 ? 38.672 5.105 6.610 1.00 55.67 ? 51 PHE A CE1 1 ATOM 419 C CE2 . PHE A 1 51 ? 39.789 3.128 5.843 1.00 53.76 ? 51 PHE A CE2 1 ATOM 420 C CZ . PHE A 1 51 ? 38.719 3.726 6.488 1.00 51.82 ? 51 PHE A CZ 1 ATOM 421 N N . ALA A 1 52 ? 44.172 8.512 5.426 1.00 27.44 ? 52 ALA A N 1 ATOM 422 C CA . ALA A 1 52 ? 45.160 9.362 4.773 1.00 18.14 ? 52 ALA A CA 1 ATOM 423 C C . ALA A 1 52 ? 45.670 10.443 5.704 1.00 18.86 ? 52 ALA A C 1 ATOM 424 O O . ALA A 1 52 ? 45.083 10.704 6.746 1.00 22.33 ? 52 ALA A O 1 ATOM 425 C CB . ALA A 1 52 ? 44.578 9.984 3.521 1.00 26.93 ? 52 ALA A CB 1 ATOM 426 N N . SER A 1 53 ? 46.788 11.053 5.345 1.00 21.58 ? 53 SER A N 1 ATOM 427 C CA . SER A 1 53 ? 47.307 12.168 6.123 1.00 18.70 ? 53 SER A CA 1 ATOM 428 C C . SER A 1 53 ? 47.739 13.256 5.146 1.00 21.87 ? 53 SER A C 1 ATOM 429 O O . SER A 1 53 ? 47.922 12.990 3.959 1.00 23.30 ? 53 SER A O 1 ATOM 430 C CB . SER A 1 53 ? 48.471 11.744 7.016 1.00 26.77 ? 53 SER A CB 1 ATOM 431 O OG . SER A 1 53 ? 49.567 11.304 6.234 1.00 29.10 ? 53 SER A OG 1 ATOM 432 N N . PHE A 1 54 ? 47.904 14.471 5.652 1.00 18.86 ? 54 PHE A N 1 ATOM 433 C CA . PHE A 1 54 ? 48.471 15.557 4.869 1.00 18.10 ? 54 PHE A CA 1 ATOM 434 C C . PHE A 1 54 ? 49.244 16.508 5.770 1.00 21.83 ? 54 PHE A C 1 ATOM 435 O O . PHE A 1 54 ? 48.737 16.977 6.784 1.00 22.35 ? 54 PHE A O 1 ATOM 436 C CB . PHE A 1 54 ? 47.389 16.325 4.113 1.00 18.64 ? 54 PHE A CB 1 ATOM 437 C CG . PHE A 1 54 ? 47.927 17.466 3.307 1.00 19.25 ? 54 PHE A CG 1 ATOM 438 C CD1 . PHE A 1 54 ? 48.581 17.237 2.105 1.00 22.90 ? 54 PHE A CD1 1 ATOM 439 C CD2 . PHE A 1 54 ? 47.830 18.769 3.779 1.00 15.59 ? 54 PHE A CD2 1 ATOM 440 C CE1 . PHE A 1 54 ? 49.093 18.290 1.372 1.00 10.66 ? 54 PHE A CE1 1 ATOM 441 C CE2 . PHE A 1 54 ? 48.335 19.820 3.051 1.00 15.89 ? 54 PHE A CE2 1 ATOM 442 C CZ . PHE A 1 54 ? 48.973 19.580 1.848 1.00 12.46 ? 54 PHE A CZ 1 ATOM 443 N N . GLU A 1 55 ? 50.483 16.780 5.387 1.00 21.94 ? 55 GLU A N 1 ATOM 444 C CA . GLU A 1 55 ? 51.331 17.702 6.125 1.00 29.42 ? 55 GLU A CA 1 ATOM 445 C C . GLU A 1 55 ? 50.900 19.135 5.822 1.00 25.76 ? 55 GLU A C 1 ATOM 446 O O . GLU A 1 55 ? 51.250 19.687 4.775 1.00 25.03 ? 55 GLU A O 1 ATOM 447 C CB . GLU A 1 55 ? 52.806 17.460 5.770 1.00 35.40 ? 55 GLU A CB 1 ATOM 448 C CG . GLU A 1 55 ? 53.803 18.420 6.401 1.00 43.70 ? 55 GLU A CG 1 ATOM 449 C CD . GLU A 1 55 ? 53.651 18.498 7.911 1.00 55.86 ? 55 GLU A CD 1 ATOM 450 O OE1 . GLU A 1 55 ? 53.883 17.471 8.586 1.00 62.45 ? 55 GLU A OE1 1 ATOM 451 O OE2 . GLU A 1 55 ? 53.311 19.587 8.423 1.00 60.30 ? 55 GLU A OE2 1 ATOM 452 N N . ALA A 1 56 ? 50.161 19.738 6.751 1.00 23.68 ? 56 ALA A N 1 ATOM 453 C CA . ALA A 1 56 ? 49.562 21.065 6.554 1.00 19.82 ? 56 ALA A CA 1 ATOM 454 C C . ALA A 1 56 ? 50.568 22.160 6.230 1.00 24.48 ? 56 ALA A C 1 ATOM 455 O O . ALA A 1 56 ? 50.229 23.142 5.575 1.00 24.67 ? 56 ALA A O 1 ATOM 456 C CB . ALA A 1 56 ? 48.752 21.453 7.789 1.00 20.99 ? 56 ALA A CB 1 ATOM 457 N N . GLN A 1 57 ? 51.797 21.999 6.702 1.00 33.64 ? 57 GLN A N 1 ATOM 458 C CA . GLN A 1 57 ? 52.837 23.000 6.507 1.00 25.97 ? 57 GLN A CA 1 ATOM 459 C C . GLN A 1 57 ? 53.100 23.281 5.032 1.00 27.36 ? 57 GLN A C 1 ATOM 460 O O . GLN A 1 57 ? 53.376 24.417 4.654 1.00 31.00 ? 57 GLN A O 1 ATOM 461 C CB . GLN A 1 57 ? 54.128 22.543 7.192 1.00 40.12 ? 57 GLN A CB 1 ATOM 462 C CG . GLN A 1 57 ? 55.201 23.620 7.363 1.00 40.68 ? 57 GLN A CG 1 ATOM 463 C CD . GLN A 1 57 ? 54.753 24.809 8.201 1.00 53.87 ? 57 GLN A CD 1 ATOM 464 O OE1 . GLN A 1 57 ? 54.795 25.956 7.744 1.00 44.75 ? 57 GLN A OE1 1 ATOM 465 N NE2 . GLN A 1 57 ? 54.327 24.541 9.436 1.00 52.35 ? 57 GLN A NE2 1 ATOM 466 N N . GLY A 1 58 ? 52.984 22.252 4.197 1.00 25.12 ? 58 GLY A N 1 ATOM 467 C CA . GLY A 1 58 ? 53.220 22.402 2.768 1.00 17.72 ? 58 GLY A CA 1 ATOM 468 C C . GLY A 1 58 ? 52.275 23.363 2.080 1.00 25.54 ? 58 GLY A C 1 ATOM 469 O O . GLY A 1 58 ? 52.654 24.042 1.126 1.00 25.69 ? 58 GLY A O 1 ATOM 470 N N . ALA A 1 59 ? 51.044 23.436 2.579 1.00 26.56 ? 59 ALA A N 1 ATOM 471 C CA . ALA A 1 59 ? 50.036 24.343 2.035 1.00 21.54 ? 59 ALA A CA 1 ATOM 472 C C . ALA A 1 59 ? 50.462 25.792 2.231 1.00 25.60 ? 59 ALA A C 1 ATOM 473 O O . ALA A 1 59 ? 50.227 26.651 1.380 1.00 20.50 ? 59 ALA A O 1 ATOM 474 C CB . ALA A 1 59 ? 48.676 24.092 2.694 1.00 17.72 ? 59 ALA A CB 1 ATOM 475 N N . LEU A 1 60 ? 51.090 26.043 3.373 1.00 27.18 ? 60 LEU A N 1 ATOM 476 C CA . LEU A 1 60 ? 51.546 27.370 3.754 1.00 29.91 ? 60 LEU A CA 1 ATOM 477 C C . LEU A 1 60 ? 52.551 27.923 2.735 1.00 24.17 ? 60 LEU A C 1 ATOM 478 O O . LEU A 1 60 ? 52.517 29.104 2.391 1.00 20.45 ? 60 LEU A O 1 ATOM 479 C CB . LEU A 1 60 ? 52.173 27.303 5.145 1.00 36.18 ? 60 LEU A CB 1 ATOM 480 C CG . LEU A 1 60 ? 51.186 27.401 6.311 1.00 36.31 ? 60 LEU A CG 1 ATOM 481 C CD1 . LEU A 1 60 ? 51.924 27.571 7.637 1.00 38.12 ? 60 LEU A CD1 1 ATOM 482 C CD2 . LEU A 1 60 ? 50.178 28.513 6.088 1.00 44.18 ? 60 LEU A CD2 1 ATOM 483 N N . ALA A 1 61 ? 53.441 27.062 2.249 1.00 19.47 ? 61 ALA A N 1 ATOM 484 C CA . ALA A 1 61 ? 54.437 27.486 1.277 1.00 21.02 ? 61 ALA A CA 1 ATOM 485 C C . ALA A 1 61 ? 53.786 27.920 -0.044 1.00 19.95 ? 61 ALA A C 1 ATOM 486 O O . ALA A 1 61 ? 54.162 28.939 -0.624 1.00 15.12 ? 61 ALA A O 1 ATOM 487 C CB . ALA A 1 61 ? 55.438 26.367 1.030 1.00 18.68 ? 61 ALA A CB 1 ATOM 488 N N . ASN A 1 62 ? 52.802 27.149 -0.500 1.00 16.40 ? 62 ASN A N 1 ATOM 489 C CA . ASN A 1 62 ? 52.081 27.469 -1.728 1.00 15.58 ? 62 ASN A CA 1 ATOM 490 C C . ASN A 1 62 ? 51.325 28.785 -1.643 1.00 13.28 ? 62 ASN A C 1 ATOM 491 O O . ASN A 1 62 ? 51.320 29.567 -2.595 1.00 10.22 ? 62 ASN A O 1 ATOM 492 C CB . ASN A 1 62 ? 51.129 26.336 -2.112 1.00 12.21 ? 62 ASN A CB 1 ATOM 493 C CG . ASN A 1 62 ? 51.809 25.293 -2.981 1.00 21.58 ? 62 ASN A CG 1 ATOM 494 O OD1 . ASN A 1 62 ? 53.038 25.201 -2.994 1.00 35.27 ? 62 ASN A OD1 1 ATOM 495 N ND2 . ASN A 1 62 ? 51.026 24.538 -3.742 1.00 15.73 ? 62 ASN A ND2 1 ATOM 496 N N . ILE A 1 63 ? 50.672 29.011 -0.508 1.00 16.28 ? 63 ILE A N 1 ATOM 497 C CA . ILE A 1 63 ? 49.897 30.222 -0.306 1.00 11.80 ? 63 ILE A CA 1 ATOM 498 C C . ILE A 1 63 ? 50.816 31.437 -0.320 1.00 13.58 ? 63 ILE A C 1 ATOM 499 O O . ILE A 1 63 ? 50.452 32.494 -0.835 1.00 12.32 ? 63 ILE A O 1 ATOM 500 C CB . ILE A 1 63 ? 49.095 30.170 1.016 1.00 17.76 ? 63 ILE A CB 1 ATOM 501 C CG1 . ILE A 1 63 ? 48.120 28.981 0.991 1.00 25.91 ? 63 ILE A CG1 1 ATOM 502 C CG2 . ILE A 1 63 ? 48.457 31.535 1.354 1.00 11.07 ? 63 ILE A CG2 1 ATOM 503 C CD1 . ILE A 1 63 ? 47.184 28.927 -0.221 1.00 15.89 ? 63 ILE A CD1 1 ATOM 504 N N . ALA A 1 64 ? 52.023 31.279 0.214 1.00 15.54 ? 64 ALA A N 1 ATOM 505 C CA . ALA A 1 64 ? 52.995 32.371 0.186 1.00 19.08 ? 64 ALA A CA 1 ATOM 506 C C . ALA A 1 64 ? 53.389 32.735 -1.241 1.00 13.06 ? 64 ALA A C 1 ATOM 507 O O . ALA A 1 64 ? 53.498 33.909 -1.580 1.00 11.42 ? 64 ALA A O 1 ATOM 508 C CB . ALA A 1 64 ? 54.225 31.999 0.993 1.00 17.86 ? 64 ALA A CB 1 ATOM 509 N N . VAL A 1 65 ? 53.571 31.724 -2.083 1.00 15.30 ? 65 VAL A N 1 ATOM 510 C CA . VAL A 1 65 ? 53.860 31.966 -3.493 1.00 13.80 ? 65 VAL A CA 1 ATOM 511 C C . VAL A 1 65 ? 52.660 32.628 -4.191 1.00 13.02 ? 65 VAL A C 1 ATOM 512 O O . VAL A 1 65 ? 52.829 33.556 -4.982 1.00 11.88 ? 65 VAL A O 1 ATOM 513 C CB . VAL A 1 65 ? 54.231 30.659 -4.233 1.00 14.50 ? 65 VAL A CB 1 ATOM 514 C CG1 . VAL A 1 65 ? 54.257 30.878 -5.735 1.00 10.44 ? 65 VAL A CG1 1 ATOM 515 C CG2 . VAL A 1 65 ? 55.578 30.110 -3.733 1.00 13.39 ? 65 VAL A CG2 1 ATOM 516 N N . ASP A 1 66 ? 51.449 32.167 -3.870 1.00 11.41 ? 66 ASP A N 1 ATOM 517 C CA . ASP A 1 66 ? 50.244 32.723 -4.495 1.00 16.26 ? 66 ASP A CA 1 ATOM 518 C C . ASP A 1 66 ? 50.072 34.188 -4.153 1.00 10.27 ? 66 ASP A C 1 ATOM 519 O O . ASP A 1 66 ? 49.652 34.976 -4.987 1.00 10.47 ? 66 ASP A O 1 ATOM 520 C CB . ASP A 1 66 ? 48.991 31.963 -4.067 1.00 9.33 ? 66 ASP A CB 1 ATOM 521 C CG . ASP A 1 66 ? 49.023 30.517 -4.495 1.00 13.20 ? 66 ASP A CG 1 ATOM 522 O OD1 . ASP A 1 66 ? 49.755 30.188 -5.457 1.00 9.95 ? 66 ASP A OD1 1 ATOM 523 O OD2 . ASP A 1 66 ? 48.292 29.715 -3.875 1.00 14.71 ? 66 ASP A OD2 1 ATOM 524 N N . LYS A 1 67 ? 50.410 34.534 -2.918 1.00 12.61 ? 67 LYS A N 1 ATOM 525 C CA . LYS A 1 67 ? 50.362 35.905 -2.449 1.00 12.23 ? 67 LYS A CA 1 ATOM 526 C C . LYS A 1 67 ? 51.358 36.749 -3.247 1.00 15.64 ? 67 LYS A C 1 ATOM 527 O O . LYS A 1 67 ? 51.019 37.822 -3.743 1.00 11.97 ? 67 LYS A O 1 ATOM 528 C CB . LYS A 1 67 ? 50.669 35.949 -0.951 1.00 15.82 ? 67 LYS A CB 1 ATOM 529 C CG . LYS A 1 67 ? 50.794 37.342 -0.348 1.00 21.74 ? 67 LYS A CG 1 ATOM 530 C CD . LYS A 1 67 ? 51.063 37.236 1.156 1.00 29.60 ? 67 LYS A CD 1 ATOM 531 C CE . LYS A 1 67 ? 51.054 38.599 1.842 1.00 35.37 ? 67 LYS A CE 1 ATOM 532 N NZ . LYS A 1 67 ? 52.281 39.378 1.548 1.00 34.21 ? 67 LYS A NZ 1 ATOM 533 N N . ALA A 1 68 ? 52.575 36.238 -3.403 1.00 11.28 ? 68 ALA A N 1 ATOM 534 C CA . ALA A 1 68 ? 53.591 36.942 -4.182 1.00 16.32 ? 68 ALA A CA 1 ATOM 535 C C . ALA A 1 68 ? 53.185 37.037 -5.654 1.00 16.27 ? 68 ALA A C 1 ATOM 536 O O . ALA A 1 68 ? 53.372 38.079 -6.278 1.00 16.84 ? 68 ALA A O 1 ATOM 537 C CB . ALA A 1 68 ? 54.951 36.257 -4.051 1.00 8.77 ? 68 ALA A CB 1 ATOM 538 N N . ASN A 1 69 ? 52.593 35.973 -6.199 1.00 10.10 ? 69 ASN A N 1 ATOM 539 C CA . ASN A 1 69 ? 52.123 36.011 -7.586 1.00 10.19 ? 69 ASN A CA 1 ATOM 540 C C . ASN A 1 69 ? 50.984 37.012 -7.790 1.00 11.64 ? 69 ASN A C 1 ATOM 541 O O . ASN A 1 69 ? 50.932 37.697 -8.813 1.00 13.71 ? 69 ASN A O 1 ATOM 542 C CB . ASN A 1 69 ? 51.675 34.614 -8.042 1.00 8.00 ? 69 ASN A CB 1 ATOM 543 C CG . ASN A 1 69 ? 52.844 33.692 -8.343 1.00 8.18 ? 69 ASN A CG 1 ATOM 544 O OD1 . ASN A 1 69 ? 53.989 34.120 -8.350 1.00 16.28 ? 69 ASN A OD1 1 ATOM 545 N ND2 . ASN A 1 69 ? 52.556 32.417 -8.591 1.00 13.26 ? 69 ASN A ND2 1 ATOM 546 N N . LEU A 1 70 ? 50.088 37.120 -6.816 1.00 6.26 ? 70 LEU A N 1 ATOM 547 C CA . LEU A 1 70 ? 49.007 38.093 -6.910 1.00 10.55 ? 70 LEU A CA 1 ATOM 548 C C . LEU A 1 70 ? 49.568 39.518 -7.020 1.00 9.94 ? 70 LEU A C 1 ATOM 549 O O . LEU A 1 70 ? 49.081 40.311 -7.821 1.00 8.15 ? 70 LEU A O 1 ATOM 550 C CB . LEU A 1 70 ? 48.063 37.985 -5.707 1.00 7.56 ? 70 LEU A CB 1 ATOM 551 C CG . LEU A 1 70 ? 46.920 38.992 -5.709 1.00 12.94 ? 70 LEU A CG 1 ATOM 552 C CD1 . LEU A 1 70 ? 46.109 38.845 -6.990 1.00 4.72 ? 70 LEU A CD1 1 ATOM 553 C CD2 . LEU A 1 70 ? 46.029 38.796 -4.478 1.00 16.93 ? 70 LEU A CD2 1 ATOM 554 N N . GLU A 1 71 ? 50.604 39.824 -6.238 1.00 9.41 ? 71 GLU A N 1 ATOM 555 C CA . GLU A 1 71 ? 51.252 41.138 -6.318 1.00 12.16 ? 71 GLU A CA 1 ATOM 556 C C . GLU A 1 71 ? 51.727 41.391 -7.735 1.00 10.24 ? 71 GLU A C 1 ATOM 557 O O . GLU A 1 71 ? 51.466 42.446 -8.307 1.00 10.70 ? 71 GLU A O 1 ATOM 558 C CB . GLU A 1 71 ? 52.442 41.248 -5.362 1.00 18.14 ? 71 GLU A CB 1 ATOM 559 C CG . GLU A 1 71 ? 52.086 41.178 -3.882 1.00 38.57 ? 71 GLU A CG 1 ATOM 560 C CD . GLU A 1 71 ? 53.306 41.017 -2.958 1.00 51.56 ? 71 GLU A CD 1 ATOM 561 O OE1 . GLU A 1 71 ? 54.440 41.419 -3.330 1.00 37.02 ? 71 GLU A OE1 1 ATOM 562 O OE2 . GLU A 1 71 ? 53.128 40.448 -1.859 1.00 48.50 ? 71 GLU A OE2 1 ATOM 563 N N . ILE A 1 72 ? 52.406 40.399 -8.308 1.00 9.62 ? 72 ILE A N 1 ATOM 564 C CA . ILE A 1 72 ? 52.912 40.519 -9.672 1.00 14.19 ? 72 ILE A CA 1 ATOM 565 C C . ILE A 1 72 ? 51.781 40.721 -10.702 1.00 19.30 ? 72 ILE A C 1 ATOM 566 O O . ILE A 1 72 ? 51.811 41.677 -11.487 1.00 16.85 ? 72 ILE A O 1 ATOM 567 C CB . ILE A 1 72 ? 53.739 39.278 -10.067 1.00 14.66 ? 72 ILE A CB 1 ATOM 568 C CG1 . ILE A 1 72 ? 55.070 39.246 -9.308 1.00 16.00 ? 72 ILE A CG1 1 ATOM 569 C CG2 . ILE A 1 72 ? 53.946 39.219 -11.577 1.00 12.05 ? 72 ILE A CG2 1 ATOM 570 C CD1 . ILE A 1 72 ? 55.834 37.948 -9.479 1.00 19.06 ? 72 ILE A CD1 1 ATOM 571 N N . MET A 1 73 ? 50.741 39.888 -10.629 1.00 10.36 ? 73 MET A N 1 ATOM 572 C CA . MET A 1 73 ? 49.671 39.925 -11.616 1.00 10.11 ? 73 MET A CA 1 ATOM 573 C C . MET A 1 73 ? 48.823 41.182 -11.486 1.00 10.49 ? 73 MET A C 1 ATOM 574 O O . MET A 1 73 ? 48.318 41.695 -12.483 1.00 9.28 ? 73 MET A O 1 ATOM 575 C CB . MET A 1 73 ? 48.758 38.692 -11.490 1.00 10.00 ? 73 MET A CB 1 ATOM 576 C CG . MET A 1 73 ? 49.449 37.361 -11.670 1.00 10.84 ? 73 MET A CG 1 ATOM 577 S SD . MET A 1 73 ? 50.406 37.322 -13.191 1.00 16.64 ? 73 MET A SD 1 ATOM 578 C CE . MET A 1 73 ? 49.127 37.725 -14.374 1.00 7.21 ? 73 MET A CE 1 ATOM 579 N N . THR A 1 74 ? 48.644 41.661 -10.260 1.00 7.05 ? 74 THR A N 1 ATOM 580 C CA . THR A 1 74 ? 47.918 42.906 -10.060 1.00 18.90 ? 74 THR A CA 1 ATOM 581 C C . THR A 1 74 ? 48.584 44.072 -10.802 1.00 18.20 ? 74 THR A C 1 ATOM 582 O O . THR A 1 74 ? 47.901 44.817 -11.506 1.00 13.20 ? 74 THR A O 1 ATOM 583 C CB . THR A 1 74 ? 47.804 43.260 -8.570 1.00 14.75 ? 74 THR A CB 1 ATOM 584 O OG1 . THR A 1 74 ? 47.097 42.220 -7.883 1.00 10.83 ? 74 THR A OG1 1 ATOM 585 C CG2 . THR A 1 74 ? 47.074 44.576 -8.399 1.00 9.13 ? 74 THR A CG2 1 ATOM 586 N N . LYS A 1 75 ? 49.910 44.206 -10.670 1.00 16.05 ? 75 LYS A N 1 ATOM 587 C CA . LYS A 1 75 ? 50.651 45.238 -11.398 1.00 16.46 ? 75 LYS A CA 1 ATOM 588 C C . LYS A 1 75 ? 50.557 45.044 -12.903 1.00 18.87 ? 75 LYS A C 1 ATOM 589 O O . LYS A 1 75 ? 50.293 45.988 -13.660 1.00 13.45 ? 75 LYS A O 1 ATOM 590 C CB . LYS A 1 75 ? 52.141 45.244 -11.013 1.00 23.69 ? 75 LYS A CB 1 ATOM 591 C CG . LYS A 1 75 ? 52.449 45.700 -9.609 1.00 22.41 ? 75 LYS A CG 1 ATOM 592 C CD . LYS A 1 75 ? 53.934 45.521 -9.283 1.00 23.66 ? 75 LYS A CD 1 ATOM 593 C CE . LYS A 1 75 ? 54.108 45.207 -7.790 1.00 39.61 ? 75 LYS A CE 1 ATOM 594 N NZ . LYS A 1 75 ? 55.518 45.055 -7.339 1.00 29.11 ? 75 LYS A NZ 1 ATOM 595 N N . ARG A 1 76 ? 50.754 43.796 -13.324 1.00 18.92 ? 76 ARG A N 1 ATOM 596 C CA . ARG A 1 76 ? 50.705 43.437 -14.735 1.00 15.42 ? 76 ARG A CA 1 ATOM 597 C C . ARG A 1 76 ? 49.347 43.822 -15.332 1.00 17.32 ? 76 ARG A C 1 ATOM 598 O O . ARG A 1 76 ? 49.284 44.261 -16.479 1.00 14.56 ? 76 ARG A O 1 ATOM 599 C CB . ARG A 1 76 ? 51.046 41.944 -14.874 1.00 13.37 ? 76 ARG A CB 1 ATOM 600 C CG . ARG A 1 76 ? 51.780 41.581 -16.141 1.00 19.52 ? 76 ARG A CG 1 ATOM 601 C CD . ARG A 1 76 ? 51.938 40.071 -16.356 1.00 21.94 ? 76 ARG A CD 1 ATOM 602 N NE . ARG A 1 76 ? 53.116 39.608 -15.602 1.00 24.18 ? 76 ARG A NE 1 ATOM 603 C CZ . ARG A 1 76 ? 53.396 38.343 -15.288 1.00 28.09 ? 76 ARG A CZ 1 ATOM 604 N NH1 . ARG A 1 76 ? 52.617 37.340 -15.694 1.00 28.30 ? 76 ARG A NH1 1 ATOM 605 N NH2 . ARG A 1 76 ? 54.491 38.075 -14.597 1.00 22.32 ? 76 ARG A NH2 1 ATOM 606 N N . SER A 1 77 ? 48.274 43.686 -14.550 1.00 12.01 ? 77 SER A N 1 ATOM 607 C CA . SER A 1 77 ? 46.927 43.998 -15.039 1.00 18.01 ? 77 SER A CA 1 ATOM 608 C C . SER A 1 77 ? 46.620 45.493 -14.941 1.00 18.96 ? 77 SER A C 1 ATOM 609 O O . SER A 1 77 ? 45.489 45.910 -15.211 1.00 16.76 ? 77 SER A O 1 ATOM 610 C CB . SER A 1 77 ? 45.858 43.242 -14.250 1.00 15.63 ? 77 SER A CB 1 ATOM 611 O OG . SER A 1 77 ? 45.651 43.849 -12.980 1.00 11.42 ? 77 SER A OG 1 ATOM 612 N N . ASN A 1 78 ? 47.613 46.278 -14.518 1.00 12.28 ? 78 ASN A N 1 ATOM 613 C CA . ASN A 1 78 ? 47.429 47.697 -14.217 1.00 15.62 ? 78 ASN A CA 1 ATOM 614 C C . ASN A 1 78 ? 46.372 47.937 -13.140 1.00 16.42 ? 78 ASN A C 1 ATOM 615 O O . ASN A 1 78 ? 45.534 48.838 -13.256 1.00 13.77 ? 78 ASN A O 1 ATOM 616 C CB . ASN A 1 78 ? 47.109 48.499 -15.482 1.00 18.80 ? 78 ASN A CB 1 ATOM 617 C CG . ASN A 1 78 ? 48.175 48.326 -16.561 1.00 28.19 ? 78 ASN A CG 1 ATOM 618 O OD1 . ASN A 1 78 ? 49.375 48.372 -16.269 1.00 23.21 ? 78 ASN A OD1 1 ATOM 619 N ND2 . ASN A 1 78 ? 47.747 48.148 -17.806 1.00 31.35 ? 78 ASN A ND2 1 ATOM 620 N N . TYR A 1 79 ? 46.421 47.099 -12.108 1.00 10.28 ? 79 TYR A N 1 ATOM 621 C CA . TYR A 1 79 ? 45.532 47.184 -10.943 1.00 13.42 ? 79 TYR A CA 1 ATOM 622 C C . TYR A 1 79 ? 44.041 47.120 -11.321 1.00 12.50 ? 79 TYR A C 1 ATOM 623 O O . TYR A 1 79 ? 43.218 47.839 -10.763 1.00 14.96 ? 79 TYR A O 1 ATOM 624 C CB . TYR A 1 79 ? 45.845 48.448 -10.125 1.00 15.30 ? 79 TYR A CB 1 ATOM 625 C CG . TYR A 1 79 ? 47.252 48.444 -9.534 1.00 14.06 ? 79 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 79 ? 48.346 48.826 -10.299 1.00 14.19 ? 79 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 79 ? 47.482 48.048 -8.215 1.00 16.23 ? 79 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 79 ? 49.641 48.817 -9.777 1.00 17.54 ? 79 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 79 ? 48.781 48.038 -7.678 1.00 14.38 ? 79 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 79 ? 49.848 48.427 -8.473 1.00 16.70 ? 79 TYR A CZ 1 ATOM 631 O OH . TYR A 1 79 ? 51.124 48.426 -7.982 1.00 20.42 ? 79 TYR A OH 1 ATOM 632 N N . THR A 1 80 ? 43.706 46.220 -12.246 1.00 12.30 ? 80 THR A N 1 ATOM 633 C CA . THR A 1 80 ? 42.318 45.963 -12.629 1.00 9.26 ? 80 THR A CA 1 ATOM 634 C C . THR A 1 80 ? 41.734 45.065 -11.548 1.00 12.38 ? 80 THR A C 1 ATOM 635 O O . THR A 1 80 ? 42.223 43.961 -11.319 1.00 11.31 ? 80 THR A O 1 ATOM 636 C CB . THR A 1 80 ? 42.181 45.283 -14.003 1.00 13.75 ? 80 THR A CB 1 ATOM 637 O OG1 . THR A 1 80 ? 42.754 46.122 -15.011 1.00 17.21 ? 80 THR A OG1 1 ATOM 638 C CG2 . THR A 1 80 ? 40.722 45.049 -14.331 1.00 8.45 ? 80 THR A CG2 1 ATOM 639 N N . PRO A 1 81 ? 40.697 45.550 -10.863 1.00 11.53 ? 81 PRO A N 1 ATOM 640 C CA . PRO A 1 81 ? 40.113 44.815 -9.738 1.00 13.08 ? 81 PRO A CA 1 ATOM 641 C C . PRO A 1 81 ? 39.107 43.786 -10.194 1.00 12.00 ? 81 PRO A C 1 ATOM 642 O O . PRO A 1 81 ? 38.686 43.793 -11.341 1.00 13.46 ? 81 PRO A O 1 ATOM 643 C CB . PRO A 1 81 ? 39.391 45.907 -8.949 1.00 8.14 ? 81 PRO A CB 1 ATOM 644 C CG . PRO A 1 81 ? 38.986 46.888 -9.998 1.00 8.04 ? 81 PRO A CG 1 ATOM 645 C CD . PRO A 1 81 ? 40.057 46.858 -11.068 1.00 9.04 ? 81 PRO A CD 1 ATOM 646 N N . ILE A 1 82 ? 38.714 42.912 -9.286 1.00 11.10 ? 82 ILE A N 1 ATOM 647 C CA . ILE A 1 82 ? 37.715 41.910 -9.604 1.00 12.87 ? 82 ILE A CA 1 ATOM 648 C C . ILE A 1 82 ? 36.334 42.529 -9.779 1.00 11.11 ? 82 ILE A C 1 ATOM 649 O O . ILE A 1 82 ? 35.992 43.535 -9.153 1.00 14.94 ? 82 ILE A O 1 ATOM 650 C CB . ILE A 1 82 ? 37.669 40.799 -8.523 1.00 10.69 ? 82 ILE A CB 1 ATOM 651 C CG1 . ILE A 1 82 ? 37.032 39.523 -9.089 1.00 12.23 ? 82 ILE A CG1 1 ATOM 652 C CG2 . ILE A 1 82 ? 36.959 41.283 -7.252 1.00 7.33 ? 82 ILE A CG2 1 ATOM 653 C CD1 . ILE A 1 82 ? 37.273 38.277 -8.230 1.00 9.93 ? 82 ILE A CD1 1 ATOM 654 N N . THR A 1 83 ? 35.551 41.949 -10.669 1.00 9.69 ? 83 THR A N 1 ATOM 655 C CA . THR A 1 83 ? 34.166 42.351 -10.784 1.00 10.15 ? 83 THR A CA 1 ATOM 656 C C . THR A 1 83 ? 33.342 41.461 -9.861 1.00 10.60 ? 83 THR A C 1 ATOM 657 O O . THR A 1 83 ? 33.472 40.236 -9.888 1.00 15.12 ? 83 THR A O 1 ATOM 658 C CB . THR A 1 83 ? 33.668 42.266 -12.220 1.00 9.84 ? 83 THR A CB 1 ATOM 659 O OG1 . THR A 1 83 ? 34.367 43.249 -12.991 1.00 11.22 ? 83 THR A OG1 1 ATOM 660 C CG2 . THR A 1 83 ? 32.178 42.599 -12.279 1.00 5.77 ? 83 THR A CG2 1 ATOM 661 N N . ASN A 1 84 ? 32.537 42.088 -9.005 1.00 10.44 ? 84 ASN A N 1 ATOM 662 C CA . ASN A 1 84 ? 31.690 41.347 -8.088 1.00 12.98 ? 84 ASN A CA 1 ATOM 663 C C . ASN A 1 84 ? 30.638 40.540 -8.820 1.00 14.44 ? 84 ASN A C 1 ATOM 664 O O . ASN A 1 84 ? 29.962 41.060 -9.709 1.00 15.29 ? 84 ASN A O 1 ATOM 665 C CB . ASN A 1 84 ? 30.975 42.293 -7.121 1.00 16.86 ? 84 ASN A CB 1 ATOM 666 C CG . ASN A 1 84 ? 31.920 43.014 -6.205 1.00 18.44 ? 84 ASN A CG 1 ATOM 667 O OD1 . ASN A 1 84 ? 32.867 42.427 -5.676 1.00 19.45 ? 84 ASN A OD1 1 ATOM 668 N ND2 . ASN A 1 84 ? 31.661 44.298 -5.993 1.00 15.77 ? 84 ASN A ND2 1 ATOM 669 N N . VAL A 1 85 ? 30.501 39.274 -8.443 1.00 10.59 ? 85 VAL A N 1 ATOM 670 C CA . VAL A 1 85 ? 29.432 38.433 -8.955 1.00 9.97 ? 85 VAL A CA 1 ATOM 671 C C . VAL A 1 85 ? 28.596 37.944 -7.777 1.00 12.62 ? 85 VAL A C 1 ATOM 672 O O . VAL A 1 85 ? 29.078 37.176 -6.947 1.00 12.91 ? 85 VAL A O 1 ATOM 673 C CB . VAL A 1 85 ? 29.937 37.230 -9.781 1.00 14.34 ? 85 VAL A CB 1 ATOM 674 C CG1 . VAL A 1 85 ? 28.743 36.361 -10.226 1.00 7.74 ? 85 VAL A CG1 1 ATOM 675 C CG2 . VAL A 1 85 ? 30.735 37.702 -10.989 1.00 6.92 ? 85 VAL A CG2 1 ATOM 676 N N . PRO A 1 86 ? 27.354 38.424 -7.675 1.00 11.23 ? 86 PRO A N 1 ATOM 677 C CA . PRO A 1 86 ? 26.543 38.080 -6.511 1.00 11.67 ? 86 PRO A CA 1 ATOM 678 C C . PRO A 1 86 ? 26.072 36.623 -6.567 1.00 11.39 ? 86 PRO A C 1 ATOM 679 O O . PRO A 1 86 ? 25.901 36.074 -7.662 1.00 9.90 ? 86 PRO A O 1 ATOM 680 C CB . PRO A 1 86 ? 25.368 39.054 -6.614 1.00 16.39 ? 86 PRO A CB 1 ATOM 681 C CG . PRO A 1 86 ? 25.246 39.352 -8.089 1.00 11.01 ? 86 PRO A CG 1 ATOM 682 C CD . PRO A 1 86 ? 26.663 39.354 -8.593 1.00 14.63 ? 86 PRO A CD 1 ATOM 683 N N . PRO A 1 87 ? 25.834 36.011 -5.394 1.00 14.81 ? 87 PRO A N 1 ATOM 684 C CA . PRO A 1 87 ? 25.451 34.595 -5.293 1.00 14.27 ? 87 PRO A CA 1 ATOM 685 C C . PRO A 1 87 ? 24.010 34.273 -5.622 1.00 11.90 ? 87 PRO A C 1 ATOM 686 O O . PRO A 1 87 ? 23.141 35.121 -5.484 1.00 14.14 ? 87 PRO A O 1 ATOM 687 C CB . PRO A 1 87 ? 25.722 34.271 -3.826 1.00 10.43 ? 87 PRO A CB 1 ATOM 688 C CG . PRO A 1 87 ? 25.500 35.554 -3.110 1.00 13.65 ? 87 PRO A CG 1 ATOM 689 C CD . PRO A 1 87 ? 26.008 36.626 -4.064 1.00 13.24 ? 87 PRO A CD 1 ATOM 690 N N . GLU A 1 88 ? 23.774 33.029 -6.031 1.00 14.05 ? 88 GLU A N 1 ATOM 691 C CA . GLU A 1 88 ? 22.433 32.447 -6.016 1.00 14.41 ? 88 GLU A CA 1 ATOM 692 C C . GLU A 1 88 ? 22.292 31.740 -4.697 1.00 9.95 ? 88 GLU A C 1 ATOM 693 O O . GLU A 1 88 ? 23.212 31.052 -4.280 1.00 13.51 ? 88 GLU A O 1 ATOM 694 C CB . GLU A 1 88 ? 22.222 31.437 -7.146 1.00 20.97 ? 88 GLU A CB 1 ATOM 695 C CG . GLU A 1 88 ? 22.351 31.968 -8.551 1.00 33.03 ? 88 GLU A CG 1 ATOM 696 C CD . GLU A 1 88 ? 22.103 30.892 -9.601 1.00 39.77 ? 88 GLU A CD 1 ATOM 697 O OE1 . GLU A 1 88 ? 21.886 29.718 -9.218 1.00 36.55 ? 88 GLU A OE1 1 ATOM 698 O OE2 . GLU A 1 88 ? 22.098 31.225 -10.806 1.00 49.00 ? 88 GLU A OE2 1 ATOM 699 N N . VAL A 1 89 ? 21.158 31.887 -4.030 1.00 9.59 ? 89 VAL A N 1 ATOM 700 C CA . VAL A 1 89 ? 21.023 31.281 -2.716 1.00 9.72 ? 89 VAL A CA 1 ATOM 701 C C . VAL A 1 89 ? 19.814 30.380 -2.715 1.00 13.98 ? 89 VAL A C 1 ATOM 702 O O . VAL A 1 89 ? 18.751 30.750 -3.196 1.00 15.16 ? 89 VAL A O 1 ATOM 703 C CB . VAL A 1 89 ? 20.901 32.333 -1.608 1.00 14.32 ? 89 VAL A CB 1 ATOM 704 C CG1 . VAL A 1 89 ? 20.786 31.658 -0.248 1.00 7.74 ? 89 VAL A CG1 1 ATOM 705 C CG2 . VAL A 1 89 ? 22.112 33.277 -1.630 1.00 12.17 ? 89 VAL A CG2 1 ATOM 706 N N . THR A 1 90 ? 19.995 29.179 -2.187 1.00 12.30 ? 90 THR A N 1 ATOM 707 C CA . THR A 1 90 ? 18.903 28.230 -2.049 1.00 10.41 ? 90 THR A CA 1 ATOM 708 C C . THR A 1 90 ? 18.901 27.639 -0.653 1.00 15.29 ? 90 THR A C 1 ATOM 709 O O . THR A 1 90 ? 19.966 27.328 -0.099 1.00 11.14 ? 90 THR A O 1 ATOM 710 C CB . THR A 1 90 ? 19.020 27.080 -3.079 1.00 11.77 ? 90 THR A CB 1 ATOM 711 O OG1 . THR A 1 90 ? 19.199 27.624 -4.385 1.00 16.01 ? 90 THR A OG1 1 ATOM 712 C CG2 . THR A 1 90 ? 17.778 26.197 -3.076 1.00 9.23 ? 90 THR A CG2 1 ATOM 713 N N . VAL A 1 91 ? 17.708 27.481 -0.087 1.00 14.13 ? 91 VAL A N 1 ATOM 714 C CA . VAL A 1 91 ? 17.570 26.833 1.208 1.00 15.13 ? 91 VAL A CA 1 ATOM 715 C C . VAL A 1 91 ? 16.748 25.567 1.008 1.00 9.79 ? 91 VAL A C 1 ATOM 716 O O . VAL A 1 91 ? 15.727 25.590 0.334 1.00 19.76 ? 91 VAL A O 1 ATOM 717 C CB . VAL A 1 91 ? 16.900 27.740 2.254 1.00 17.06 ? 91 VAL A CB 1 ATOM 718 C CG1 . VAL A 1 91 ? 16.613 26.947 3.529 1.00 14.33 ? 91 VAL A CG1 1 ATOM 719 C CG2 . VAL A 1 91 ? 17.786 28.920 2.569 1.00 12.68 ? 91 VAL A CG2 1 ATOM 720 N N . LEU A 1 92 ? 17.242 24.453 1.532 1.00 17.19 ? 92 LEU A N 1 ATOM 721 C CA . LEU A 1 92 ? 16.552 23.165 1.449 1.00 17.56 ? 92 LEU A CA 1 ATOM 722 C C . LEU A 1 92 ? 16.835 22.310 2.688 1.00 14.97 ? 92 LEU A C 1 ATOM 723 O O . LEU A 1 92 ? 17.728 22.635 3.473 1.00 16.00 ? 92 LEU A O 1 ATOM 724 C CB . LEU A 1 92 ? 16.936 22.450 0.137 1.00 19.98 ? 92 LEU A CB 1 ATOM 725 C CG . LEU A 1 92 ? 18.348 21.968 -0.263 1.00 26.58 ? 92 LEU A CG 1 ATOM 726 C CD1 . LEU A 1 92 ? 19.368 23.122 -0.342 1.00 22.14 ? 92 LEU A CD1 1 ATOM 727 C CD2 . LEU A 1 92 ? 18.905 20.834 0.603 1.00 34.47 ? 92 LEU A CD2 1 ATOM 728 N N . THR A 1 93 ? 16.084 21.227 2.882 1.00 14.19 ? 93 THR A N 1 ATOM 729 C CA . THR A 1 93 ? 16.399 20.311 3.981 1.00 18.68 ? 93 THR A CA 1 ATOM 730 C C . THR A 1 93 ? 17.125 19.115 3.413 1.00 14.73 ? 93 THR A C 1 ATOM 731 O O . THR A 1 93 ? 17.015 18.843 2.225 1.00 12.15 ? 93 THR A O 1 ATOM 732 C CB . THR A 1 93 ? 15.163 19.834 4.747 1.00 14.81 ? 93 THR A CB 1 ATOM 733 O OG1 . THR A 1 93 ? 14.324 19.056 3.888 1.00 16.16 ? 93 THR A OG1 1 ATOM 734 C CG2 . THR A 1 93 ? 14.415 21.020 5.332 1.00 18.45 ? 93 THR A CG2 1 ATOM 735 N N . ASN A 1 94 ? 17.906 18.423 4.230 1.00 15.80 ? 94 ASN A N 1 ATOM 736 C CA . ASN A 1 94 ? 18.624 17.274 3.690 1.00 18.86 ? 94 ASN A CA 1 ATOM 737 C C . ASN A 1 94 ? 17.780 15.998 3.639 1.00 17.32 ? 94 ASN A C 1 ATOM 738 O O . ASN A 1 94 ? 18.188 15.030 3.010 1.00 17.65 ? 94 ASN A O 1 ATOM 739 C CB . ASN A 1 94 ? 19.922 17.023 4.462 1.00 15.58 ? 94 ASN A CB 1 ATOM 740 C CG . ASN A 1 94 ? 19.689 16.457 5.826 1.00 31.01 ? 94 ASN A CG 1 ATOM 741 O OD1 . ASN A 1 94 ? 18.612 16.613 6.406 1.00 26.89 ? 94 ASN A OD1 1 ATOM 742 N ND2 . ASN A 1 94 ? 20.691 15.754 6.345 1.00 28.41 ? 94 ASN A ND2 1 ATOM 743 N N . SER A 1 95 ? 16.595 16.010 4.254 1.00 18.07 ? 95 SER A N 1 ATOM 744 C CA . SER A 1 95 ? 15.660 14.875 4.151 1.00 26.35 ? 95 SER A CA 1 ATOM 745 C C . SER A 1 95 ? 14.233 15.388 4.242 1.00 20.83 ? 95 SER A C 1 ATOM 746 O O . SER A 1 95 ? 14.024 16.502 4.720 1.00 19.05 ? 95 SER A O 1 ATOM 747 C CB . SER A 1 95 ? 15.919 13.822 5.241 1.00 24.85 ? 95 SER A CB 1 ATOM 748 O OG . SER A 1 95 ? 15.729 14.358 6.531 1.00 31.73 ? 95 SER A OG 1 ATOM 749 N N . PRO A 1 96 ? 13.247 14.563 3.820 1.00 28.15 ? 96 PRO A N 1 ATOM 750 C CA . PRO A 1 96 ? 11.833 14.956 3.932 1.00 28.27 ? 96 PRO A CA 1 ATOM 751 C C . PRO A 1 96 ? 11.486 15.360 5.359 1.00 24.58 ? 96 PRO A C 1 ATOM 752 O O . PRO A 1 96 ? 11.943 14.741 6.326 1.00 24.60 ? 96 PRO A O 1 ATOM 753 C CB . PRO A 1 96 ? 11.085 13.682 3.531 1.00 30.02 ? 96 PRO A CB 1 ATOM 754 C CG . PRO A 1 96 ? 12.021 12.986 2.598 1.00 23.83 ? 96 PRO A CG 1 ATOM 755 C CD . PRO A 1 96 ? 13.398 13.261 3.135 1.00 21.09 ? 96 PRO A CD 1 ATOM 756 N N . VAL A 1 97 ? 10.685 16.406 5.482 1.00 20.21 ? 97 VAL A N 1 ATOM 757 C CA . VAL A 1 97 ? 10.412 16.980 6.790 1.00 26.93 ? 97 VAL A CA 1 ATOM 758 C C . VAL A 1 97 ? 9.261 16.251 7.458 1.00 28.17 ? 97 VAL A C 1 ATOM 759 O O . VAL A 1 97 ? 8.210 16.037 6.854 1.00 25.56 ? 97 VAL A O 1 ATOM 760 C CB . VAL A 1 97 ? 10.094 18.476 6.687 1.00 27.09 ? 97 VAL A CB 1 ATOM 761 C CG1 . VAL A 1 97 ? 9.838 19.047 8.071 1.00 26.32 ? 97 VAL A CG1 1 ATOM 762 C CG2 . VAL A 1 97 ? 11.260 19.206 6.051 1.00 20.81 ? 97 VAL A CG2 1 ATOM 763 N N . GLU A 1 98 ? 9.482 15.840 8.698 1.00 26.32 ? 98 GLU A N 1 ATOM 764 C CA . GLU A 1 98 ? 8.408 15.290 9.498 1.00 37.22 ? 98 GLU A CA 1 ATOM 765 C C . GLU A 1 98 ? 8.412 16.072 10.803 1.00 30.38 ? 98 GLU A C 1 ATOM 766 O O . GLU A 1 98 ? 9.478 16.317 11.374 1.00 24.51 ? 98 GLU A O 1 ATOM 767 C CB . GLU A 1 98 ? 8.627 13.793 9.760 1.00 31.96 ? 98 GLU A CB 1 ATOM 768 C CG . GLU A 1 98 ? 8.702 12.902 8.512 1.00 37.64 ? 98 GLU A CG 1 ATOM 769 C CD . GLU A 1 98 ? 7.443 12.916 7.665 1.00 57.60 ? 98 GLU A CD 1 ATOM 770 O OE1 . GLU A 1 98 ? 6.336 12.930 8.245 1.00 61.69 ? 98 GLU A OE1 1 ATOM 771 O OE2 . GLU A 1 98 ? 7.565 12.906 6.414 1.00 53.50 ? 98 GLU A OE2 1 ATOM 772 N N . LEU A 1 99 ? 7.230 16.430 11.290 1.00 29.83 ? 99 LEU A N 1 ATOM 773 C CA . LEU A 1 99 ? 7.111 17.202 12.523 1.00 26.14 ? 99 LEU A CA 1 ATOM 774 C C . LEU A 1 99 ? 7.835 16.540 13.671 1.00 30.07 ? 99 LEU A C 1 ATOM 775 O O . LEU A 1 99 ? 7.733 15.332 13.868 1.00 35.28 ? 99 LEU A O 1 ATOM 776 C CB . LEU A 1 99 ? 5.648 17.425 12.903 1.00 30.07 ? 99 LEU A CB 1 ATOM 777 C CG . LEU A 1 99 ? 4.915 18.420 12.011 1.00 36.37 ? 99 LEU A CG 1 ATOM 778 C CD1 . LEU A 1 99 ? 3.428 18.521 12.369 1.00 27.33 ? 99 LEU A CD1 1 ATOM 779 C CD2 . LEU A 1 99 ? 5.598 19.779 12.146 1.00 32.07 ? 99 LEU A CD2 1 ATOM 780 N N . ARG A 1 100 ? 8.559 17.354 14.428 1.00 33.83 ? 100 ARG A N 1 ATOM 781 C CA . ARG A 1 100 ? 9.371 16.889 15.543 1.00 33.81 ? 100 ARG A CA 1 ATOM 782 C C . ARG A 1 100 ? 10.308 15.717 15.255 1.00 30.90 ? 100 ARG A C 1 ATOM 783 O O . ARG A 1 100 ? 10.685 14.980 16.160 1.00 27.73 ? 100 ARG A O 1 ATOM 784 C CB . ARG A 1 100 ? 8.403 16.507 16.647 1.00 44.93 ? 100 ARG A CB 1 ATOM 785 C CG . ARG A 1 100 ? 7.461 17.643 16.960 1.00 48.70 ? 100 ARG A CG 1 ATOM 786 C CD . ARG A 1 100 ? 6.752 17.444 18.263 1.00 66.25 ? 100 ARG A CD 1 ATOM 787 N NE . ARG A 1 100 ? 5.332 17.541 17.955 1.00 65.34 ? 100 ARG A NE 1 ATOM 788 C CZ . ARG A 1 100 ? 4.593 16.518 17.536 1.00 62.72 ? 100 ARG A CZ 1 ATOM 789 N NH1 . ARG A 1 100 ? 5.149 15.327 17.346 1.00 51.05 ? 100 ARG A NH1 1 ATOM 790 N NH2 . ARG A 1 100 ? 3.305 16.693 17.272 1.00 60.89 ? 100 ARG A NH2 1 ATOM 791 N N . GLU A 1 101 ? 10.731 15.599 14.000 1.00 34.36 ? 101 GLU A N 1 ATOM 792 C CA . GLU A 1 101 ? 11.806 14.686 13.625 1.00 32.74 ? 101 GLU A CA 1 ATOM 793 C C . GLU A 1 101 ? 13.026 15.512 13.217 1.00 37.69 ? 101 GLU A C 1 ATOM 794 O O . GLU A 1 101 ? 12.961 16.299 12.261 1.00 25.77 ? 101 GLU A O 1 ATOM 795 C CB . GLU A 1 101 ? 11.398 13.767 12.459 1.00 38.27 ? 101 GLU A CB 1 ATOM 796 C CG . GLU A 1 101 ? 10.307 12.712 12.705 1.00 40.55 ? 101 GLU A CG 1 ATOM 797 C CD . GLU A 1 101 ? 10.666 11.657 13.752 1.00 61.00 ? 101 GLU A CD 1 ATOM 798 O OE1 . GLU A 1 101 ? 11.614 11.852 14.546 1.00 55.22 ? 101 GLU A OE1 1 ATOM 799 O OE2 . GLU A 1 101 ? 9.998 10.597 13.756 1.00 81.52 ? 101 GLU A OE2 1 ATOM 800 N N . PRO A 1 102 ? 14.131 15.356 13.959 1.00 31.37 ? 102 PRO A N 1 ATOM 801 C CA . PRO A 1 102 ? 15.354 16.134 13.748 1.00 29.94 ? 102 PRO A CA 1 ATOM 802 C C . PRO A 1 102 ? 15.721 16.137 12.267 1.00 31.77 ? 102 PRO A C 1 ATOM 803 O O . PRO A 1 102 ? 15.628 15.088 11.620 1.00 18.34 ? 102 PRO A O 1 ATOM 804 C CB . PRO A 1 102 ? 16.389 15.397 14.591 1.00 30.40 ? 102 PRO A CB 1 ATOM 805 C CG . PRO A 1 102 ? 15.593 14.805 15.698 1.00 26.46 ? 102 PRO A CG 1 ATOM 806 C CD . PRO A 1 102 ? 14.269 14.414 15.084 1.00 31.30 ? 102 PRO A CD 1 ATOM 807 N N . ASN A 1 103 ? 16.034 17.315 11.734 1.00 25.44 ? 103 ASN A N 1 ATOM 808 C CA . ASN A 1 103 ? 16.375 17.481 10.328 1.00 18.96 ? 103 ASN A CA 1 ATOM 809 C C . ASN A 1 103 ? 17.489 18.516 10.243 1.00 14.98 ? 103 ASN A C 1 ATOM 810 O O . ASN A 1 103 ? 17.946 19.039 11.271 1.00 15.41 ? 103 ASN A O 1 ATOM 811 C CB . ASN A 1 103 ? 15.141 17.905 9.517 1.00 19.05 ? 103 ASN A CB 1 ATOM 812 C CG . ASN A 1 103 ? 15.209 17.473 8.056 1.00 21.76 ? 103 ASN A CG 1 ATOM 813 O OD1 . ASN A 1 103 ? 16.228 17.656 7.396 1.00 17.92 ? 103 ASN A OD1 1 ATOM 814 N ND2 . ASN A 1 103 ? 14.107 16.917 7.541 1.00 14.75 ? 103 ASN A ND2 1 ATOM 815 N N . VAL A 1 104 ? 17.925 18.834 9.031 1.00 16.48 ? 104 VAL A N 1 ATOM 816 C CA . VAL A 1 104 ? 18.964 19.843 8.851 1.00 14.09 ? 104 VAL A CA 1 ATOM 817 C C . VAL A 1 104 ? 18.606 20.772 7.704 1.00 14.27 ? 104 VAL A C 1 ATOM 818 O O . VAL A 1 104 ? 18.270 20.319 6.604 1.00 15.57 ? 104 VAL A O 1 ATOM 819 C CB . VAL A 1 104 ? 20.345 19.213 8.562 1.00 18.01 ? 104 VAL A CB 1 ATOM 820 C CG1 . VAL A 1 104 ? 21.387 20.300 8.373 1.00 11.37 ? 104 VAL A CG1 1 ATOM 821 C CG2 . VAL A 1 104 ? 20.768 18.237 9.674 1.00 14.73 ? 104 VAL A CG2 1 ATOM 822 N N . LEU A 1 105 ? 18.634 22.074 7.975 1.00 10.99 ? 105 LEU A N 1 ATOM 823 C CA . LEU A 1 105 ? 18.504 23.066 6.914 1.00 12.34 ? 105 LEU A CA 1 ATOM 824 C C . LEU A 1 105 ? 19.864 23.328 6.256 1.00 14.16 ? 105 LEU A C 1 ATOM 825 O O . LEU A 1 105 ? 20.887 23.490 6.935 1.00 15.32 ? 105 LEU A O 1 ATOM 826 C CB . LEU A 1 105 ? 17.912 24.379 7.455 1.00 16.70 ? 105 LEU A CB 1 ATOM 827 C CG . LEU A 1 105 ? 16.396 24.471 7.685 1.00 13.79 ? 105 LEU A CG 1 ATOM 828 C CD1 . LEU A 1 105 ? 16.058 25.670 8.528 1.00 14.73 ? 105 LEU A CD1 1 ATOM 829 C CD2 . LEU A 1 105 ? 15.653 24.564 6.371 1.00 14.79 ? 105 LEU A CD2 1 ATOM 830 N N . ILE A 1 106 ? 19.857 23.376 4.929 1.00 13.76 ? 106 ILE A N 1 ATOM 831 C CA . ILE A 1 106 ? 21.049 23.681 4.152 1.00 13.08 ? 106 ILE A CA 1 ATOM 832 C C . ILE A 1 106 ? 20.841 24.983 3.408 1.00 11.64 ? 106 ILE A C 1 ATOM 833 O O . ILE A 1 106 ? 19.834 25.158 2.705 1.00 12.65 ? 106 ILE A O 1 ATOM 834 C CB . ILE A 1 106 ? 21.373 22.568 3.137 1.00 9.47 ? 106 ILE A CB 1 ATOM 835 C CG1 . ILE A 1 106 ? 21.471 21.209 3.842 1.00 14.04 ? 106 ILE A CG1 1 ATOM 836 C CG2 . ILE A 1 106 ? 22.660 22.870 2.426 1.00 10.25 ? 106 ILE A CG2 1 ATOM 837 C CD1 . ILE A 1 106 ? 21.567 20.011 2.883 1.00 10.85 ? 106 ILE A CD1 1 ATOM 838 N N . CYS A 1 107 ? 21.795 25.892 3.566 1.00 9.14 ? 107 CYS A N 1 ATOM 839 C CA . CYS A 1 107 ? 21.818 27.123 2.793 1.00 12.88 ? 107 CYS A CA 1 ATOM 840 C C . CYS A 1 107 ? 22.935 26.991 1.782 1.00 11.14 ? 107 CYS A C 1 ATOM 841 O O . CYS A 1 107 ? 24.115 26.941 2.140 1.00 9.63 ? 107 CYS A O 1 ATOM 842 C CB . CYS A 1 107 ? 22.034 28.357 3.679 1.00 10.67 ? 107 CYS A CB 1 ATOM 843 S SG . CYS A 1 107 ? 21.936 29.938 2.784 1.00 12.02 ? 107 CYS A SG 1 ATOM 844 N N . PHE A 1 108 ? 22.564 26.949 0.513 1.00 9.67 ? 108 PHE A N 1 ATOM 845 C CA . PHE A 1 108 ? 23.556 26.790 -0.529 1.00 11.60 ? 108 PHE A CA 1 ATOM 846 C C . PHE A 1 108 ? 23.798 28.145 -1.196 1.00 11.75 ? 108 PHE A C 1 ATOM 847 O O . PHE A 1 108 ? 22.876 28.736 -1.743 1.00 9.61 ? 108 PHE A O 1 ATOM 848 C CB . PHE A 1 108 ? 23.103 25.731 -1.543 1.00 8.09 ? 108 PHE A CB 1 ATOM 849 C CG . PHE A 1 108 ? 24.105 25.478 -2.629 1.00 26.26 ? 108 PHE A CG 1 ATOM 850 C CD1 . PHE A 1 108 ? 25.463 25.348 -2.313 1.00 20.15 ? 108 PHE A CD1 1 ATOM 851 C CD2 . PHE A 1 108 ? 23.708 25.333 -3.950 1.00 22.03 ? 108 PHE A CD2 1 ATOM 852 C CE1 . PHE A 1 108 ? 26.397 25.088 -3.290 1.00 16.23 ? 108 PHE A CE1 1 ATOM 853 C CE2 . PHE A 1 108 ? 24.651 25.074 -4.946 1.00 24.55 ? 108 PHE A CE2 1 ATOM 854 C CZ . PHE A 1 108 ? 25.997 24.951 -4.611 1.00 20.81 ? 108 PHE A CZ 1 ATOM 855 N N . ILE A 1 109 ? 25.036 28.631 -1.129 1.00 10.58 ? 109 ILE A N 1 ATOM 856 C CA . ILE A 1 109 ? 25.400 29.930 -1.686 1.00 8.04 ? 109 ILE A CA 1 ATOM 857 C C . ILE A 1 109 ? 26.324 29.642 -2.868 1.00 10.24 ? 109 ILE A C 1 ATOM 858 O O . ILE A 1 109 ? 27.380 29.033 -2.694 1.00 9.39 ? 109 ILE A O 1 ATOM 859 C CB . ILE A 1 109 ? 26.103 30.851 -0.657 1.00 8.84 ? 109 ILE A CB 1 ATOM 860 C CG1 . ILE A 1 109 ? 25.257 31.055 0.591 1.00 10.68 ? 109 ILE A CG1 1 ATOM 861 C CG2 . ILE A 1 109 ? 26.394 32.182 -1.237 1.00 6.09 ? 109 ILE A CG2 1 ATOM 862 C CD1 . ILE A 1 109 ? 25.644 30.158 1.727 1.00 20.81 ? 109 ILE A CD1 1 ATOM 863 N N . ASP A 1 110 ? 25.934 30.078 -4.060 1.00 5.88 ? 110 ASP A N 1 ATOM 864 C CA . ASP A 1 110 ? 26.536 29.568 -5.293 1.00 10.38 ? 110 ASP A CA 1 ATOM 865 C C . ASP A 1 110 ? 26.859 30.651 -6.334 1.00 8.82 ? 110 ASP A C 1 ATOM 866 O O . ASP A 1 110 ? 26.241 31.715 -6.331 1.00 8.12 ? 110 ASP A O 1 ATOM 867 C CB . ASP A 1 110 ? 25.576 28.531 -5.895 1.00 10.43 ? 110 ASP A CB 1 ATOM 868 C CG . ASP A 1 110 ? 26.230 27.637 -6.947 1.00 21.73 ? 110 ASP A CG 1 ATOM 869 O OD1 . ASP A 1 110 ? 27.479 27.556 -7.010 1.00 18.96 ? 110 ASP A OD1 1 ATOM 870 O OD2 . ASP A 1 110 ? 25.482 26.967 -7.690 1.00 20.09 ? 110 ASP A OD2 1 ATOM 871 N N . LYS A 1 111 ? 27.845 30.373 -7.195 1.00 8.27 ? 111 LYS A N 1 ATOM 872 C CA . LYS A 1 111 ? 28.159 31.185 -8.383 1.00 9.15 ? 111 LYS A CA 1 ATOM 873 C C . LYS A 1 111 ? 28.531 32.620 -8.049 1.00 6.85 ? 111 LYS A C 1 ATOM 874 O O . LYS A 1 111 ? 28.037 33.563 -8.669 1.00 8.35 ? 111 LYS A O 1 ATOM 875 C CB . LYS A 1 111 ? 26.987 31.200 -9.367 1.00 10.93 ? 111 LYS A CB 1 ATOM 876 C CG . LYS A 1 111 ? 26.668 29.853 -9.954 1.00 22.09 ? 111 LYS A CG 1 ATOM 877 C CD . LYS A 1 111 ? 25.325 29.840 -10.664 1.00 24.87 ? 111 LYS A CD 1 ATOM 878 C CE . LYS A 1 111 ? 24.960 28.423 -11.105 1.00 30.38 ? 111 LYS A CE 1 ATOM 879 N NZ . LYS A 1 111 ? 23.641 28.351 -11.805 1.00 31.95 ? 111 LYS A NZ 1 ATOM 880 N N . PHE A 1 112 ? 29.416 32.795 -7.088 1.00 5.88 ? 112 PHE A N 1 ATOM 881 C CA . PHE A 1 112 ? 29.780 34.139 -6.689 1.00 8.84 ? 112 PHE A CA 1 ATOM 882 C C . PHE A 1 112 ? 31.295 34.342 -6.577 1.00 8.35 ? 112 PHE A C 1 ATOM 883 O O . PHE A 1 112 ? 32.064 33.391 -6.430 1.00 3.84 ? 112 PHE A O 1 ATOM 884 C CB . PHE A 1 112 ? 29.110 34.476 -5.362 1.00 6.13 ? 112 PHE A CB 1 ATOM 885 C CG . PHE A 1 112 ? 29.629 33.673 -4.212 1.00 8.49 ? 112 PHE A CG 1 ATOM 886 C CD1 . PHE A 1 112 ? 30.652 34.172 -3.405 1.00 7.31 ? 112 PHE A CD1 1 ATOM 887 C CD2 . PHE A 1 112 ? 29.094 32.418 -3.923 1.00 7.62 ? 112 PHE A CD2 1 ATOM 888 C CE1 . PHE A 1 112 ? 31.142 33.442 -2.346 1.00 7.03 ? 112 PHE A CE1 1 ATOM 889 C CE2 . PHE A 1 112 ? 29.581 31.668 -2.855 1.00 8.46 ? 112 PHE A CE2 1 ATOM 890 C CZ . PHE A 1 112 ? 30.611 32.177 -2.066 1.00 9.46 ? 112 PHE A CZ 1 ATOM 891 N N . THR A 1 113 ? 31.693 35.609 -6.622 1.00 7.60 ? 113 THR A N 1 ATOM 892 C CA . THR A 1 113 ? 33.063 36.008 -6.357 1.00 8.50 ? 113 THR A CA 1 ATOM 893 C C . THR A 1 113 ? 33.093 37.517 -6.063 1.00 11.40 ? 113 THR A C 1 ATOM 894 O O . THR A 1 113 ? 32.258 38.268 -6.569 1.00 9.68 ? 113 THR A O 1 ATOM 895 C CB . THR A 1 113 ? 33.986 35.642 -7.544 1.00 4.95 ? 113 THR A CB 1 ATOM 896 O OG1 . THR A 1 113 ? 35.343 35.571 -7.094 1.00 9.23 ? 113 THR A OG1 1 ATOM 897 C CG2 . THR A 1 113 ? 33.871 36.657 -8.678 1.00 6.03 ? 113 THR A CG2 1 ATOM 898 N N . PRO A 1 114 ? 34.055 37.974 -5.244 1.00 9.48 ? 114 PRO A N 1 ATOM 899 C CA . PRO A 1 114 ? 35.137 37.271 -4.534 1.00 8.83 ? 114 PRO A CA 1 ATOM 900 C C . PRO A 1 114 ? 34.645 36.352 -3.411 1.00 8.70 ? 114 PRO A C 1 ATOM 901 O O . PRO A 1 114 ? 33.493 36.483 -2.999 1.00 11.53 ? 114 PRO A O 1 ATOM 902 C CB . PRO A 1 114 ? 35.990 38.427 -3.972 1.00 6.64 ? 114 PRO A CB 1 ATOM 903 C CG . PRO A 1 114 ? 35.050 39.550 -3.859 1.00 8.61 ? 114 PRO A CG 1 ATOM 904 C CD . PRO A 1 114 ? 34.091 39.426 -4.994 1.00 4.82 ? 114 PRO A CD 1 ATOM 905 N N . PRO A 1 115 ? 35.514 35.445 -2.912 1.00 10.09 ? 115 PRO A N 1 ATOM 906 C CA . PRO A 1 115 ? 35.133 34.508 -1.838 1.00 14.89 ? 115 PRO A CA 1 ATOM 907 C C . PRO A 1 115 ? 35.086 35.176 -0.463 1.00 14.73 ? 115 PRO A C 1 ATOM 908 O O . PRO A 1 115 ? 35.881 34.871 0.427 1.00 16.60 ? 115 PRO A O 1 ATOM 909 C CB . PRO A 1 115 ? 36.234 33.437 -1.900 1.00 9.34 ? 115 PRO A CB 1 ATOM 910 C CG . PRO A 1 115 ? 37.424 34.180 -2.424 1.00 10.11 ? 115 PRO A CG 1 ATOM 911 C CD . PRO A 1 115 ? 36.875 35.164 -3.422 1.00 5.90 ? 115 PRO A CD 1 ATOM 912 N N . VAL A 1 116 ? 34.121 36.077 -0.308 1.00 12.84 ? 116 VAL A N 1 ATOM 913 C CA . VAL A 1 116 ? 33.829 36.745 0.954 1.00 11.09 ? 116 VAL A CA 1 ATOM 914 C C . VAL A 1 116 ? 32.324 36.902 1.069 1.00 12.13 ? 116 VAL A C 1 ATOM 915 O O . VAL A 1 116 ? 31.677 37.433 0.170 1.00 13.21 ? 116 VAL A O 1 ATOM 916 C CB . VAL A 1 116 ? 34.478 38.152 1.049 1.00 15.50 ? 116 VAL A CB 1 ATOM 917 C CG1 . VAL A 1 116 ? 34.138 38.804 2.379 1.00 10.50 ? 116 VAL A CG1 1 ATOM 918 C CG2 . VAL A 1 116 ? 35.992 38.077 0.850 1.00 13.12 ? 116 VAL A CG2 1 ATOM 919 N N . VAL A 1 117 ? 31.759 36.379 2.144 1.00 9.85 ? 117 VAL A N 1 ATOM 920 C CA . VAL A 1 117 ? 30.322 36.453 2.329 1.00 19.18 ? 117 VAL A CA 1 ATOM 921 C C . VAL A 1 117 ? 29.968 36.511 3.826 1.00 18.62 ? 117 VAL A C 1 ATOM 922 O O . VAL A 1 117 ? 30.696 35.965 4.652 1.00 18.14 ? 117 VAL A O 1 ATOM 923 C CB . VAL A 1 117 ? 29.659 35.244 1.626 1.00 9.82 ? 117 VAL A CB 1 ATOM 924 C CG1 . VAL A 1 117 ? 29.761 33.994 2.492 1.00 15.30 ? 117 VAL A CG1 1 ATOM 925 C CG2 . VAL A 1 117 ? 28.259 35.537 1.256 1.00 14.90 ? 117 VAL A CG2 1 ATOM 926 N N . ASN A 1 118 ? 28.902 37.217 4.189 1.00 14.77 ? 118 ASN A N 1 ATOM 927 C CA . ASN A 1 118 ? 28.365 37.103 5.549 1.00 18.03 ? 118 ASN A CA 1 ATOM 928 C C . ASN A 1 118 ? 27.063 36.326 5.457 1.00 18.06 ? 118 ASN A C 1 ATOM 929 O O . ASN A 1 118 ? 26.129 36.732 4.756 1.00 13.07 ? 118 ASN A O 1 ATOM 930 C CB . ASN A 1 118 ? 28.146 38.464 6.228 1.00 25.25 ? 118 ASN A CB 1 ATOM 931 C CG . ASN A 1 118 ? 29.451 39.205 6.518 1.00 28.43 ? 118 ASN A CG 1 ATOM 932 O OD1 . ASN A 1 118 ? 30.478 38.591 6.829 1.00 30.94 ? 118 ASN A OD1 1 ATOM 933 N ND2 . ASN A 1 118 ? 29.406 40.540 6.432 1.00 35.08 ? 118 ASN A ND2 1 ATOM 934 N N . VAL A 1 119 ? 26.990 35.242 6.221 1.00 20.76 ? 119 VAL A N 1 ATOM 935 C CA . VAL A 1 119 ? 25.820 34.383 6.236 1.00 16.55 ? 119 VAL A CA 1 ATOM 936 C C . VAL A 1 119 ? 25.287 34.277 7.645 1.00 14.02 ? 119 VAL A C 1 ATOM 937 O O . VAL A 1 119 ? 26.028 34.000 8.579 1.00 17.14 ? 119 VAL A O 1 ATOM 938 C CB . VAL A 1 119 ? 26.156 32.946 5.699 1.00 18.83 ? 119 VAL A CB 1 ATOM 939 C CG1 . VAL A 1 119 ? 24.929 32.021 5.744 1.00 10.93 ? 119 VAL A CG1 1 ATOM 940 C CG2 . VAL A 1 119 ? 26.698 33.010 4.286 1.00 15.72 ? 119 VAL A CG2 1 ATOM 941 N N . THR A 1 120 ? 23.988 34.521 7.782 1.00 11.13 ? 120 THR A N 1 ATOM 942 C CA . THR A 1 120 ? 23.307 34.423 9.064 1.00 19.05 ? 120 THR A CA 1 ATOM 943 C C . THR A 1 120 ? 22.059 33.555 8.947 1.00 10.65 ? 120 THR A C 1 ATOM 944 O O . THR A 1 120 ? 21.279 33.721 8.016 1.00 17.10 ? 120 THR A O 1 ATOM 945 C CB . THR A 1 120 ? 22.872 35.806 9.609 1.00 17.08 ? 120 THR A CB 1 ATOM 946 O OG1 . THR A 1 120 ? 23.977 36.722 9.612 1.00 16.14 ? 120 THR A OG1 1 ATOM 947 C CG2 . THR A 1 120 ? 22.338 35.655 11.019 1.00 17.43 ? 120 THR A CG2 1 ATOM 948 N N . TRP A 1 121 ? 21.878 32.631 9.881 1.00 10.66 ? 121 TRP A N 1 ATOM 949 C CA . TRP A 1 121 ? 20.625 31.887 9.991 1.00 13.80 ? 121 TRP A CA 1 ATOM 950 C C . TRP A 1 121 ? 19.639 32.672 10.861 1.00 12.91 ? 121 TRP A C 1 ATOM 951 O O . TRP A 1 121 ? 20.020 33.216 11.896 1.00 19.35 ? 121 TRP A O 1 ATOM 952 C CB . TRP A 1 121 ? 20.856 30.504 10.586 1.00 15.68 ? 121 TRP A CB 1 ATOM 953 C CG . TRP A 1 121 ? 21.438 29.491 9.649 1.00 9.93 ? 121 TRP A CG 1 ATOM 954 C CD1 . TRP A 1 121 ? 22.704 28.979 9.682 1.00 12.26 ? 121 TRP A CD1 1 ATOM 955 C CD2 . TRP A 1 121 ? 20.756 28.810 8.586 1.00 11.82 ? 121 TRP A CD2 1 ATOM 956 N NE1 . TRP A 1 121 ? 22.864 28.041 8.683 1.00 17.56 ? 121 TRP A NE1 1 ATOM 957 C CE2 . TRP A 1 121 ? 21.680 27.920 7.998 1.00 12.92 ? 121 TRP A CE2 1 ATOM 958 C CE3 . TRP A 1 121 ? 19.454 28.874 8.066 1.00 11.81 ? 121 TRP A CE3 1 ATOM 959 C CZ2 . TRP A 1 121 ? 21.340 27.096 6.920 1.00 10.83 ? 121 TRP A CZ2 1 ATOM 960 C CZ3 . TRP A 1 121 ? 19.120 28.062 7.002 1.00 9.07 ? 121 TRP A CZ3 1 ATOM 961 C CH2 . TRP A 1 121 ? 20.058 27.186 6.433 1.00 10.18 ? 121 TRP A CH2 1 ATOM 962 N N . LEU A 1 122 ? 18.393 32.790 10.419 1.00 13.12 ? 122 LEU A N 1 ATOM 963 C CA . LEU A 1 122 ? 17.387 33.483 11.218 1.00 14.31 ? 122 LEU A CA 1 ATOM 964 C C . LEU A 1 122 ? 16.241 32.531 11.579 1.00 18.70 ? 122 LEU A C 1 ATOM 965 O O . LEU A 1 122 ? 15.721 31.828 10.709 1.00 18.36 ? 122 LEU A O 1 ATOM 966 C CB . LEU A 1 122 ? 16.840 34.694 10.473 1.00 15.57 ? 122 LEU A CB 1 ATOM 967 C CG . LEU A 1 122 ? 17.862 35.763 10.085 1.00 14.51 ? 122 LEU A CG 1 ATOM 968 C CD1 . LEU A 1 122 ? 17.233 36.741 9.094 1.00 12.58 ? 122 LEU A CD1 1 ATOM 969 C CD2 . LEU A 1 122 ? 18.470 36.466 11.285 1.00 21.10 ? 122 LEU A CD2 1 ATOM 970 N N . ARG A 1 123 ? 15.849 32.510 12.855 1.00 15.11 ? 123 ARG A N 1 ATOM 971 C CA . ARG A 1 123 ? 14.672 31.766 13.280 1.00 17.42 ? 123 ARG A CA 1 ATOM 972 C C . ARG A 1 123 ? 13.672 32.785 13.819 1.00 16.54 ? 123 ARG A C 1 ATOM 973 O O . ARG A 1 123 ? 13.961 33.473 14.796 1.00 19.29 ? 123 ARG A O 1 ATOM 974 C CB . ARG A 1 123 ? 15.015 30.730 14.361 1.00 19.34 ? 123 ARG A CB 1 ATOM 975 C CG . ARG A 1 123 ? 13.799 29.968 14.910 1.00 25.16 ? 123 ARG A CG 1 ATOM 976 C CD . ARG A 1 123 ? 14.112 29.097 16.135 1.00 19.67 ? 123 ARG A CD 1 ATOM 977 N NE . ARG A 1 123 ? 15.082 28.048 15.837 1.00 42.56 ? 123 ARG A NE 1 ATOM 978 C CZ . ARG A 1 123 ? 15.094 26.847 16.411 1.00 62.49 ? 123 ARG A CZ 1 ATOM 979 N NH1 . ARG A 1 123 ? 14.165 26.528 17.309 1.00 60.90 ? 123 ARG A NH1 1 ATOM 980 N NH2 . ARG A 1 123 ? 16.021 25.955 16.068 1.00 42.28 ? 123 ARG A NH2 1 ATOM 981 N N . ASN A 1 124 ? 12.511 32.894 13.172 1.00 14.40 ? 124 ASN A N 1 ATOM 982 C CA . ASN A 1 124 ? 11.529 33.927 13.534 1.00 19.02 ? 124 ASN A CA 1 ATOM 983 C C . ASN A 1 124 ? 12.152 35.323 13.552 1.00 20.55 ? 124 ASN A C 1 ATOM 984 O O . ASN A 1 124 ? 11.901 36.110 14.463 1.00 23.29 ? 124 ASN A O 1 ATOM 985 C CB . ASN A 1 124 ? 10.879 33.606 14.878 1.00 12.78 ? 124 ASN A CB 1 ATOM 986 C CG . ASN A 1 124 ? 10.213 32.246 14.872 1.00 22.71 ? 124 ASN A CG 1 ATOM 987 O OD1 . ASN A 1 124 ? 9.628 31.834 13.859 1.00 17.30 ? 124 ASN A OD1 1 ATOM 988 N ND2 . ASN A 1 124 ? 10.353 31.511 15.972 1.00 20.83 ? 124 ASN A ND2 1 ATOM 989 N N . GLY A 1 125 ? 13.044 35.589 12.600 1.00 16.58 ? 125 GLY A N 1 ATOM 990 C CA . GLY A 1 125 ? 13.636 36.907 12.489 1.00 17.14 ? 125 GLY A CA 1 ATOM 991 C C . GLY A 1 125 ? 14.806 37.158 13.405 1.00 21.30 ? 125 GLY A C 1 ATOM 992 O O . GLY A 1 125 ? 15.339 38.272 13.429 1.00 17.16 ? 125 GLY A O 1 ATOM 993 N N . LYS A 1 126 ? 15.222 36.132 14.148 1.00 17.23 ? 126 LYS A N 1 ATOM 994 C CA . LYS A 1 126 ? 16.330 36.292 15.094 1.00 24.74 ? 126 LYS A CA 1 ATOM 995 C C . LYS A 1 126 ? 17.552 35.439 14.725 1.00 22.38 ? 126 LYS A C 1 ATOM 996 O O . LYS A 1 126 ? 17.416 34.284 14.336 1.00 21.73 ? 126 LYS A O 1 ATOM 997 C CB . LYS A 1 126 ? 15.862 35.926 16.513 1.00 32.41 ? 126 LYS A CB 1 ATOM 998 C CG . LYS A 1 126 ? 14.641 36.706 17.011 1.00 33.09 ? 126 LYS A CG 1 ATOM 999 C CD . LYS A 1 126 ? 14.309 36.362 18.460 1.00 30.93 ? 126 LYS A CD 1 ATOM 1000 C CE . LYS A 1 126 ? 13.081 37.125 18.949 1.00 38.29 ? 126 LYS A CE 1 ATOM 1001 N NZ . LYS A 1 126 ? 12.785 36.856 20.390 1.00 37.73 ? 126 LYS A NZ 1 ATOM 1002 N N . PRO A 1 127 ? 18.756 36.015 14.852 1.00 23.11 ? 127 PRO A N 1 ATOM 1003 C CA . PRO A 1 127 ? 19.981 35.275 14.529 1.00 23.11 ? 127 PRO A CA 1 ATOM 1004 C C . PRO A 1 127 ? 20.140 34.066 15.432 1.00 26.98 ? 127 PRO A C 1 ATOM 1005 O O . PRO A 1 127 ? 19.944 34.177 16.646 1.00 26.77 ? 127 PRO A O 1 ATOM 1006 C CB . PRO A 1 127 ? 21.099 36.293 14.791 1.00 22.11 ? 127 PRO A CB 1 ATOM 1007 C CG . PRO A 1 127 ? 20.428 37.623 14.691 1.00 27.51 ? 127 PRO A CG 1 ATOM 1008 C CD . PRO A 1 127 ? 19.038 37.412 15.220 1.00 20.60 ? 127 PRO A CD 1 ATOM 1009 N N . VAL A 1 128 ? 20.490 32.926 14.850 1.00 15.75 ? 128 VAL A N 1 ATOM 1010 C CA . VAL A 1 128 ? 20.729 31.736 15.645 1.00 23.17 ? 128 VAL A CA 1 ATOM 1011 C C . VAL A 1 128 ? 22.093 31.180 15.299 1.00 28.25 ? 128 VAL A C 1 ATOM 1012 O O . VAL A 1 128 ? 22.539 31.267 14.155 1.00 31.85 ? 128 VAL A O 1 ATOM 1013 C CB . VAL A 1 128 ? 19.657 30.653 15.424 1.00 31.50 ? 128 VAL A CB 1 ATOM 1014 C CG1 . VAL A 1 128 ? 18.278 31.192 15.790 1.00 32.21 ? 128 VAL A CG1 1 ATOM 1015 C CG2 . VAL A 1 128 ? 19.676 30.151 13.991 1.00 22.06 ? 128 VAL A CG2 1 ATOM 1016 N N . THR A 1 129 ? 22.801 30.692 16.312 1.00 36.30 ? 129 THR A N 1 ATOM 1017 C CA . THR A 1 129 ? 24.159 30.208 16.098 1.00 44.33 ? 129 THR A CA 1 ATOM 1018 C C . THR A 1 129 ? 24.363 28.832 16.731 1.00 40.88 ? 129 THR A C 1 ATOM 1019 O O . THR A 1 129 ? 25.377 28.171 16.504 1.00 32.55 ? 129 THR A O 1 ATOM 1020 C CB . THR A 1 129 ? 25.185 31.197 16.680 1.00 32.05 ? 129 THR A CB 1 ATOM 1021 O OG1 . THR A 1 129 ? 24.993 31.288 18.093 1.00 42.47 ? 129 THR A OG1 1 ATOM 1022 C CG2 . THR A 1 129 ? 24.996 32.585 16.087 1.00 32.76 ? 129 THR A CG2 1 ATOM 1023 N N . THR A 1 130 ? 23.389 28.399 17.520 1.00 39.20 ? 130 THR A N 1 ATOM 1024 C CA . THR A 1 130 ? 23.483 27.111 18.186 1.00 39.26 ? 130 THR A CA 1 ATOM 1025 C C . THR A 1 130 ? 23.456 25.970 17.174 1.00 36.47 ? 130 THR A C 1 ATOM 1026 O O . THR A 1 130 ? 22.444 25.739 16.509 1.00 38.09 ? 130 THR A O 1 ATOM 1027 C CB . THR A 1 130 ? 22.352 26.939 19.218 1.00 42.89 ? 130 THR A CB 1 ATOM 1028 O OG1 . THR A 1 130 ? 22.538 27.900 20.263 1.00 44.72 ? 130 THR A OG1 1 ATOM 1029 C CG2 . THR A 1 130 ? 22.383 25.549 19.831 1.00 38.06 ? 130 THR A CG2 1 ATOM 1030 N N . GLY A 1 131 ? 24.560 25.245 17.077 1.00 33.57 ? 131 GLY A N 1 ATOM 1031 C CA . GLY A 1 131 ? 24.619 24.062 16.240 1.00 37.21 ? 131 GLY A CA 1 ATOM 1032 C C . GLY A 1 131 ? 24.931 24.297 14.774 1.00 35.49 ? 131 GLY A C 1 ATOM 1033 O O . GLY A 1 131 ? 24.972 23.346 13.987 1.00 35.97 ? 131 GLY A O 1 ATOM 1034 N N . VAL A 1 132 ? 25.116 25.554 14.389 1.00 27.52 ? 132 VAL A N 1 ATOM 1035 C CA . VAL A 1 132 ? 25.392 25.863 12.993 1.00 22.94 ? 132 VAL A CA 1 ATOM 1036 C C . VAL A 1 132 ? 26.793 25.397 12.617 1.00 26.55 ? 132 VAL A C 1 ATOM 1037 O O . VAL A 1 132 ? 27.677 25.295 13.471 1.00 27.19 ? 132 VAL A O 1 ATOM 1038 C CB . VAL A 1 132 ? 25.231 27.372 12.675 1.00 28.25 ? 132 VAL A CB 1 ATOM 1039 C CG1 . VAL A 1 132 ? 23.818 27.838 13.001 1.00 21.74 ? 132 VAL A CG1 1 ATOM 1040 C CG2 . VAL A 1 132 ? 26.272 28.210 13.408 1.00 28.71 ? 132 VAL A CG2 1 ATOM 1041 N N . SER A 1 133 ? 26.987 25.123 11.332 1.00 21.42 ? 133 SER A N 1 ATOM 1042 C CA . SER A 1 133 ? 28.293 24.761 10.811 1.00 18.32 ? 133 SER A CA 1 ATOM 1043 C C . SER A 1 133 ? 28.364 25.253 9.379 1.00 15.44 ? 133 SER A C 1 ATOM 1044 O O . SER A 1 133 ? 27.352 25.664 8.818 1.00 16.24 ? 133 SER A O 1 ATOM 1045 C CB . SER A 1 133 ? 28.530 23.252 10.892 1.00 9.19 ? 133 SER A CB 1 ATOM 1046 O OG . SER A 1 133 ? 27.585 22.539 10.107 1.00 22.87 ? 133 SER A OG 1 ATOM 1047 N N . GLU A 1 134 ? 29.545 25.189 8.775 1.00 14.44 ? 134 GLU A N 1 ATOM 1048 C CA . GLU A 1 134 ? 29.719 25.725 7.433 1.00 13.96 ? 134 GLU A CA 1 ATOM 1049 C C . GLU A 1 134 ? 30.944 25.144 6.764 1.00 17.73 ? 134 GLU A C 1 ATOM 1050 O O . GLU A 1 134 ? 31.868 24.696 7.440 1.00 16.27 ? 134 GLU A O 1 ATOM 1051 C CB . GLU A 1 134 ? 29.845 27.252 7.471 1.00 14.61 ? 134 GLU A CB 1 ATOM 1052 C CG . GLU A 1 134 ? 31.168 27.772 8.048 1.00 21.01 ? 134 GLU A CG 1 ATOM 1053 C CD . GLU A 1 134 ? 31.163 29.290 8.269 1.00 25.63 ? 134 GLU A CD 1 ATOM 1054 O OE1 . GLU A 1 134 ? 30.455 29.774 9.173 1.00 25.37 ? 134 GLU A OE1 1 ATOM 1055 O OE2 . GLU A 1 134 ? 31.854 30.011 7.522 1.00 27.78 ? 134 GLU A OE2 1 ATOM 1056 N N . THR A 1 135 ? 30.965 25.189 5.438 1.00 11.11 ? 135 THR A N 1 ATOM 1057 C CA . THR A 1 135 ? 32.138 24.769 4.685 1.00 14.28 ? 135 THR A CA 1 ATOM 1058 C C . THR A 1 135 ? 33.023 25.964 4.375 1.00 18.69 ? 135 THR A C 1 ATOM 1059 O O . THR A 1 135 ? 32.602 27.106 4.521 1.00 15.16 ? 135 THR A O 1 ATOM 1060 C CB . THR A 1 135 ? 31.766 24.103 3.369 1.00 10.42 ? 135 THR A CB 1 ATOM 1061 O OG1 . THR A 1 135 ? 31.226 25.089 2.484 1.00 10.97 ? 135 THR A OG1 1 ATOM 1062 C CG2 . THR A 1 135 ? 30.747 22.994 3.604 1.00 14.56 ? 135 THR A CG2 1 ATOM 1063 N N . VAL A 1 136 ? 34.245 25.694 3.927 1.00 14.32 ? 136 VAL A N 1 ATOM 1064 C CA . VAL A 1 136 ? 35.079 26.745 3.364 1.00 21.05 ? 136 VAL A CA 1 ATOM 1065 C C . VAL A 1 136 ? 34.539 27.118 1.986 1.00 15.98 ? 136 VAL A C 1 ATOM 1066 O O . VAL A 1 136 ? 33.506 26.605 1.549 1.00 11.54 ? 136 VAL A O 1 ATOM 1067 C CB . VAL A 1 136 ? 36.574 26.305 3.249 1.00 18.31 ? 136 VAL A CB 1 ATOM 1068 C CG1 . VAL A 1 136 ? 37.167 26.009 4.621 1.00 13.47 ? 136 VAL A CG1 1 ATOM 1069 C CG2 . VAL A 1 136 ? 36.711 25.089 2.334 1.00 14.34 ? 136 VAL A CG2 1 ATOM 1070 N N . PHE A 1 137 ? 35.230 28.017 1.304 1.00 15.01 ? 137 PHE A N 1 ATOM 1071 C CA . PHE A 1 137 ? 34.825 28.390 -0.049 1.00 22.53 ? 137 PHE A CA 1 ATOM 1072 C C . PHE A 1 137 ? 35.220 27.285 -1.017 1.00 16.66 ? 137 PHE A C 1 ATOM 1073 O O . PHE A 1 137 ? 36.351 26.828 -1.025 1.00 14.15 ? 137 PHE A O 1 ATOM 1074 C CB . PHE A 1 137 ? 35.430 29.746 -0.442 1.00 14.25 ? 137 PHE A CB 1 ATOM 1075 C CG . PHE A 1 137 ? 34.930 30.874 0.401 1.00 15.72 ? 137 PHE A CG 1 ATOM 1076 C CD1 . PHE A 1 137 ? 35.605 31.248 1.556 1.00 16.25 ? 137 PHE A CD1 1 ATOM 1077 C CD2 . PHE A 1 137 ? 33.768 31.552 0.051 1.00 10.73 ? 137 PHE A CD2 1 ATOM 1078 C CE1 . PHE A 1 137 ? 35.130 32.271 2.354 1.00 14.31 ? 137 PHE A CE1 1 ATOM 1079 C CE2 . PHE A 1 137 ? 33.288 32.586 0.832 1.00 14.55 ? 137 PHE A CE2 1 ATOM 1080 C CZ . PHE A 1 137 ? 33.972 32.949 1.990 1.00 18.67 ? 137 PHE A CZ 1 ATOM 1081 N N . LEU A 1 138 ? 34.271 26.830 -1.818 1.00 15.41 ? 138 LEU A N 1 ATOM 1082 C CA . LEU A 1 138 ? 34.525 25.697 -2.686 1.00 11.55 ? 138 LEU A CA 1 ATOM 1083 C C . LEU A 1 138 ? 34.623 26.162 -4.136 1.00 11.29 ? 138 LEU A C 1 ATOM 1084 O O . LEU A 1 138 ? 33.878 27.037 -4.547 1.00 12.11 ? 138 LEU A O 1 ATOM 1085 C CB . LEU A 1 138 ? 33.424 24.649 -2.524 1.00 17.37 ? 138 LEU A CB 1 ATOM 1086 C CG . LEU A 1 138 ? 33.216 24.239 -1.067 1.00 17.38 ? 138 LEU A CG 1 ATOM 1087 C CD1 . LEU A 1 138 ? 31.942 23.437 -0.925 1.00 13.22 ? 138 LEU A CD1 1 ATOM 1088 C CD2 . LEU A 1 138 ? 34.409 23.486 -0.530 1.00 11.96 ? 138 LEU A CD2 1 ATOM 1089 N N . PRO A 1 139 ? 35.568 25.596 -4.904 1.00 15.79 ? 139 PRO A N 1 ATOM 1090 C CA . PRO A 1 139 ? 35.818 26.049 -6.275 1.00 10.75 ? 139 PRO A CA 1 ATOM 1091 C C . PRO A 1 139 ? 34.767 25.558 -7.264 1.00 11.40 ? 139 PRO A C 1 ATOM 1092 O O . PRO A 1 139 ? 34.223 24.460 -7.129 1.00 11.32 ? 139 PRO A O 1 ATOM 1093 C CB . PRO A 1 139 ? 37.167 25.418 -6.603 1.00 13.09 ? 139 PRO A CB 1 ATOM 1094 C CG . PRO A 1 139 ? 37.171 24.160 -5.788 1.00 10.11 ? 139 PRO A CG 1 ATOM 1095 C CD . PRO A 1 139 ? 36.475 24.502 -4.511 1.00 10.57 ? 139 PRO A CD 1 ATOM 1096 N N . ARG A 1 140 ? 34.467 26.390 -8.253 1.00 13.15 ? 140 ARG A N 1 ATOM 1097 C CA . ARG A 1 140 ? 33.602 25.988 -9.355 1.00 10.79 ? 140 ARG A CA 1 ATOM 1098 C C . ARG A 1 140 ? 34.409 25.867 -10.643 1.00 10.06 ? 140 ARG A C 1 ATOM 1099 O O . ARG A 1 140 ? 35.465 26.486 -10.768 1.00 10.58 ? 140 ARG A O 1 ATOM 1100 C CB . ARG A 1 140 ? 32.466 26.998 -9.552 1.00 12.18 ? 140 ARG A CB 1 ATOM 1101 C CG . ARG A 1 140 ? 31.397 27.007 -8.477 1.00 9.75 ? 140 ARG A CG 1 ATOM 1102 C CD . ARG A 1 140 ? 30.445 28.172 -8.671 1.00 9.51 ? 140 ARG A CD 1 ATOM 1103 N NE . ARG A 1 140 ? 30.084 28.221 -10.076 1.00 10.46 ? 140 ARG A NE 1 ATOM 1104 C CZ . ARG A 1 140 ? 29.052 27.574 -10.604 1.00 14.22 ? 140 ARG A CZ 1 ATOM 1105 N NH1 . ARG A 1 140 ? 28.283 26.793 -9.845 1.00 8.97 ? 140 ARG A NH1 1 ATOM 1106 N NH2 . ARG A 1 140 ? 28.821 27.674 -11.902 1.00 8.63 ? 140 ARG A NH2 1 ATOM 1107 N N . GLU A 1 141 ? 33.904 25.099 -11.604 1.00 6.36 ? 141 GLU A N 1 ATOM 1108 C CA . GLU A 1 141 ? 34.605 24.927 -12.867 1.00 8.92 ? 141 GLU A CA 1 ATOM 1109 C C . GLU A 1 141 ? 34.641 26.218 -13.666 1.00 10.74 ? 141 GLU A C 1 ATOM 1110 O O . GLU A 1 141 ? 35.429 26.354 -14.594 1.00 10.30 ? 141 GLU A O 1 ATOM 1111 C CB . GLU A 1 141 ? 33.973 23.810 -13.687 1.00 12.06 ? 141 GLU A CB 1 ATOM 1112 C CG . GLU A 1 141 ? 34.087 22.452 -12.995 1.00 30.11 ? 141 GLU A CG 1 ATOM 1113 C CD . GLU A 1 141 ? 33.552 21.301 -13.827 1.00 38.19 ? 141 GLU A CD 1 ATOM 1114 O OE1 . GLU A 1 141 ? 33.840 21.249 -15.043 1.00 40.30 ? 141 GLU A OE1 1 ATOM 1115 O OE2 . GLU A 1 141 ? 32.853 20.439 -13.249 1.00 36.82 ? 141 GLU A OE2 1 ATOM 1116 N N . ASP A 1 142 ? 33.773 27.166 -13.332 1.00 6.17 ? 142 ASP A N 1 ATOM 1117 C CA . ASP A 1 142 ? 33.844 28.464 -13.979 1.00 7.37 ? 142 ASP A CA 1 ATOM 1118 C C . ASP A 1 142 ? 34.660 29.424 -13.138 1.00 9.26 ? 142 ASP A C 1 ATOM 1119 O O . ASP A 1 142 ? 34.703 30.611 -13.438 1.00 5.96 ? 142 ASP A O 1 ATOM 1120 C CB . ASP A 1 142 ? 32.445 29.014 -14.281 1.00 7.03 ? 142 ASP A CB 1 ATOM 1121 C CG . ASP A 1 142 ? 31.590 29.191 -13.033 1.00 13.74 ? 142 ASP A CG 1 ATOM 1122 O OD1 . ASP A 1 142 ? 32.106 29.061 -11.902 1.00 10.32 ? 142 ASP A OD1 1 ATOM 1123 O OD2 . ASP A 1 142 ? 30.370 29.393 -13.198 1.00 13.35 ? 142 ASP A OD2 1 ATOM 1124 N N . HIS A 1 143 ? 35.266 28.893 -12.070 1.00 6.97 ? 143 HIS A N 1 ATOM 1125 C CA . HIS A 1 143 ? 36.243 29.622 -11.257 1.00 11.28 ? 143 HIS A CA 1 ATOM 1126 C C . HIS A 1 143 ? 35.616 30.709 -10.384 1.00 8.30 ? 143 HIS A C 1 ATOM 1127 O O . HIS A 1 143 ? 36.318 31.583 -9.854 1.00 4.34 ? 143 HIS A O 1 ATOM 1128 C CB . HIS A 1 143 ? 37.358 30.161 -12.148 1.00 5.94 ? 143 HIS A CB 1 ATOM 1129 C CG . HIS A 1 143 ? 37.798 29.163 -13.170 1.00 9.90 ? 143 HIS A CG 1 ATOM 1130 N ND1 . HIS A 1 143 ? 38.305 27.930 -12.819 1.00 8.19 ? 143 HIS A ND1 1 ATOM 1131 C CD2 . HIS A 1 143 ? 37.760 29.184 -14.522 1.00 5.31 ? 143 HIS A CD2 1 ATOM 1132 C CE1 . HIS A 1 143 ? 38.595 27.247 -13.911 1.00 7.04 ? 143 HIS A CE1 1 ATOM 1133 N NE2 . HIS A 1 143 ? 38.271 27.984 -14.957 1.00 11.17 ? 143 HIS A NE2 1 ATOM 1134 N N . LEU A 1 144 ? 34.290 30.631 -10.255 1.00 7.29 ? 144 LEU A N 1 ATOM 1135 C CA . LEU A 1 144 ? 33.567 31.303 -9.178 1.00 10.93 ? 144 LEU A CA 1 ATOM 1136 C C . LEU A 1 144 ? 33.595 30.353 -7.972 1.00 10.32 ? 144 LEU A C 1 ATOM 1137 O O . LEU A 1 144 ? 34.341 29.356 -7.974 1.00 7.84 ? 144 LEU A O 1 ATOM 1138 C CB . LEU A 1 144 ? 32.124 31.631 -9.580 1.00 4.78 ? 144 LEU A CB 1 ATOM 1139 C CG . LEU A 1 144 ? 32.042 32.511 -10.841 1.00 9.39 ? 144 LEU A CG 1 ATOM 1140 C CD1 . LEU A 1 144 ? 30.608 32.704 -11.320 1.00 3.20 ? 144 LEU A CD1 1 ATOM 1141 C CD2 . LEU A 1 144 ? 32.715 33.833 -10.635 1.00 7.11 ? 144 LEU A CD2 1 ATOM 1142 N N . PHE A 1 145 ? 32.788 30.646 -6.956 1.00 6.79 ? 145 PHE A N 1 ATOM 1143 C CA . PHE A 1 145 ? 32.828 29.862 -5.730 1.00 5.98 ? 145 PHE A CA 1 ATOM 1144 C C . PHE A 1 145 ? 31.443 29.450 -5.278 1.00 9.88 ? 145 PHE A C 1 ATOM 1145 O O . PHE A 1 145 ? 30.452 30.009 -5.735 1.00 8.49 ? 145 PHE A O 1 ATOM 1146 C CB . PHE A 1 145 ? 33.478 30.668 -4.608 1.00 5.16 ? 145 PHE A CB 1 ATOM 1147 C CG . PHE A 1 145 ? 34.899 31.019 -4.871 1.00 8.82 ? 145 PHE A CG 1 ATOM 1148 C CD1 . PHE A 1 145 ? 35.216 32.208 -5.519 1.00 5.68 ? 145 PHE A CD1 1 ATOM 1149 C CD2 . PHE A 1 145 ? 35.923 30.149 -4.511 1.00 8.77 ? 145 PHE A CD2 1 ATOM 1150 C CE1 . PHE A 1 145 ? 36.533 32.538 -5.779 1.00 9.55 ? 145 PHE A CE1 1 ATOM 1151 C CE2 . PHE A 1 145 ? 37.253 30.475 -4.763 1.00 12.69 ? 145 PHE A CE2 1 ATOM 1152 C CZ . PHE A 1 145 ? 37.560 31.669 -5.393 1.00 11.78 ? 145 PHE A CZ 1 ATOM 1153 N N . ARG A 1 146 ? 31.386 28.462 -4.388 1.00 9.83 ? 146 ARG A N 1 ATOM 1154 C CA . ARG A 1 146 ? 30.135 28.085 -3.728 1.00 11.36 ? 146 ARG A CA 1 ATOM 1155 C C . ARG A 1 146 ? 30.449 27.741 -2.283 1.00 14.09 ? 146 ARG A C 1 ATOM 1156 O O . ARG A 1 146 ? 31.600 27.517 -1.927 1.00 15.05 ? 146 ARG A O 1 ATOM 1157 C CB . ARG A 1 146 ? 29.369 26.968 -4.472 1.00 12.63 ? 146 ARG A CB 1 ATOM 1158 C CG . ARG A 1 146 ? 30.142 26.020 -5.368 1.00 16.60 ? 146 ARG A CG 1 ATOM 1159 C CD . ARG A 1 146 ? 30.034 24.548 -5.023 1.00 22.11 ? 146 ARG A CD 1 ATOM 1160 N NE . ARG A 1 146 ? 31.280 23.868 -5.381 1.00 35.84 ? 146 ARG A NE 1 ATOM 1161 C CZ . ARG A 1 146 ? 31.579 22.603 -5.097 1.00 35.82 ? 146 ARG A CZ 1 ATOM 1162 N NH1 . ARG A 1 146 ? 30.690 21.821 -4.483 1.00 37.28 ? 146 ARG A NH1 1 ATOM 1163 N NH2 . ARG A 1 146 ? 32.768 22.115 -5.454 1.00 21.54 ? 146 ARG A NH2 1 ATOM 1164 N N . LYS A 1 147 ? 29.418 27.650 -1.464 1.00 10.50 ? 147 LYS A N 1 ATOM 1165 C CA . LYS A 1 147 ? 29.607 27.474 -0.039 1.00 14.74 ? 147 LYS A CA 1 ATOM 1166 C C . LYS A 1 147 ? 28.346 26.905 0.589 1.00 12.60 ? 147 LYS A C 1 ATOM 1167 O O . LYS A 1 147 ? 27.242 27.145 0.096 1.00 12.87 ? 147 LYS A O 1 ATOM 1168 C CB . LYS A 1 147 ? 29.958 28.827 0.596 1.00 8.50 ? 147 LYS A CB 1 ATOM 1169 C CG . LYS A 1 147 ? 30.608 28.780 1.965 1.00 12.22 ? 147 LYS A CG 1 ATOM 1170 C CD . LYS A 1 147 ? 30.844 30.212 2.466 1.00 19.10 ? 147 LYS A CD 1 ATOM 1171 C CE . LYS A 1 147 ? 31.870 30.278 3.597 1.00 16.87 ? 147 LYS A CE 1 ATOM 1172 N NZ . LYS A 1 147 ? 31.435 29.563 4.830 1.00 18.65 ? 147 LYS A NZ 1 ATOM 1173 N N . PHE A 1 148 ? 28.507 26.150 1.669 1.00 13.28 ? 148 PHE A N 1 ATOM 1174 C CA . PHE A 1 148 ? 27.358 25.582 2.366 1.00 10.89 ? 148 PHE A CA 1 ATOM 1175 C C . PHE A 1 148 ? 27.300 26.005 3.824 1.00 15.35 ? 148 PHE A C 1 ATOM 1176 O O . PHE A 1 148 ? 28.327 26.060 4.501 1.00 15.25 ? 148 PHE A O 1 ATOM 1177 C CB . PHE A 1 148 ? 27.392 24.062 2.337 1.00 10.20 ? 148 PHE A CB 1 ATOM 1178 C CG . PHE A 1 148 ? 27.302 23.462 0.971 1.00 11.39 ? 148 PHE A CG 1 ATOM 1179 C CD1 . PHE A 1 148 ? 28.425 23.365 0.165 1.00 8.79 ? 148 PHE A CD1 1 ATOM 1180 C CD2 . PHE A 1 148 ? 26.095 22.955 0.507 1.00 9.48 ? 148 PHE A CD2 1 ATOM 1181 C CE1 . PHE A 1 148 ? 28.344 22.791 -1.089 1.00 10.98 ? 148 PHE A CE1 1 ATOM 1182 C CE2 . PHE A 1 148 ? 26.003 22.383 -0.745 1.00 13.93 ? 148 PHE A CE2 1 ATOM 1183 C CZ . PHE A 1 148 ? 27.133 22.294 -1.546 1.00 11.29 ? 148 PHE A CZ 1 ATOM 1184 N N . HIS A 1 149 ? 26.099 26.325 4.296 1.00 10.18 ? 149 HIS A N 1 ATOM 1185 C CA . HIS A 1 149 ? 25.872 26.555 5.718 1.00 12.32 ? 149 HIS A CA 1 ATOM 1186 C C . HIS A 1 149 ? 24.772 25.602 6.193 1.00 15.37 ? 149 HIS A C 1 ATOM 1187 O O . HIS A 1 149 ? 23.839 25.293 5.455 1.00 14.20 ? 149 HIS A O 1 ATOM 1188 C CB . HIS A 1 149 ? 25.510 28.017 6.001 1.00 14.28 ? 149 HIS A CB 1 ATOM 1189 C CG . HIS A 1 149 ? 26.699 28.928 6.026 1.00 20.63 ? 149 HIS A CG 1 ATOM 1190 N ND1 . HIS A 1 149 ? 27.100 29.597 7.161 1.00 19.51 ? 149 HIS A ND1 1 ATOM 1191 C CD2 . HIS A 1 149 ? 27.590 29.258 5.061 1.00 16.37 ? 149 HIS A CD2 1 ATOM 1192 C CE1 . HIS A 1 149 ? 28.184 30.305 6.894 1.00 22.21 ? 149 HIS A CE1 1 ATOM 1193 N NE2 . HIS A 1 149 ? 28.502 30.116 5.626 1.00 21.00 ? 149 HIS A NE2 1 ATOM 1194 N N . TYR A 1 150 ? 24.882 25.136 7.429 1.00 15.37 ? 150 TYR A N 1 ATOM 1195 C CA . TYR A 1 150 ? 23.981 24.108 7.931 1.00 16.19 ? 150 TYR A CA 1 ATOM 1196 C C . TYR A 1 150 ? 23.370 24.506 9.252 1.00 13.27 ? 150 TYR A C 1 ATOM 1197 O O . TYR A 1 150 ? 24.035 25.099 10.095 1.00 15.31 ? 150 TYR A O 1 ATOM 1198 C CB . TYR A 1 150 ? 24.727 22.786 8.114 1.00 12.18 ? 150 TYR A CB 1 ATOM 1199 C CG . TYR A 1 150 ? 25.405 22.285 6.876 1.00 13.38 ? 150 TYR A CG 1 ATOM 1200 C CD1 . TYR A 1 150 ? 26.773 22.403 6.722 1.00 13.52 ? 150 TYR A CD1 1 ATOM 1201 C CD2 . TYR A 1 150 ? 24.679 21.669 5.866 1.00 10.72 ? 150 TYR A CD2 1 ATOM 1202 C CE1 . TYR A 1 150 ? 27.401 21.936 5.593 1.00 14.45 ? 150 TYR A CE1 1 ATOM 1203 C CE2 . TYR A 1 150 ? 25.300 21.197 4.736 1.00 11.31 ? 150 TYR A CE2 1 ATOM 1204 C CZ . TYR A 1 150 ? 26.658 21.335 4.605 1.00 10.86 ? 150 TYR A CZ 1 ATOM 1205 O OH . TYR A 1 150 ? 27.272 20.869 3.483 1.00 13.47 ? 150 TYR A OH 1 ATOM 1206 N N . LEU A 1 151 ? 22.108 24.150 9.437 1.00 16.16 ? 151 LEU A N 1 ATOM 1207 C CA . LEU A 1 151 ? 21.429 24.395 10.700 1.00 14.60 ? 151 LEU A CA 1 ATOM 1208 C C . LEU A 1 151 ? 20.576 23.205 11.069 1.00 11.79 ? 151 LEU A C 1 ATOM 1209 O O . LEU A 1 151 ? 19.516 23.006 10.482 1.00 13.45 ? 151 LEU A O 1 ATOM 1210 C CB . LEU A 1 151 ? 20.564 25.658 10.625 1.00 16.00 ? 151 LEU A CB 1 ATOM 1211 C CG . LEU A 1 151 ? 19.686 25.947 11.845 1.00 16.66 ? 151 LEU A CG 1 ATOM 1212 C CD1 . LEU A 1 151 ? 20.523 26.111 13.111 1.00 15.39 ? 151 LEU A CD1 1 ATOM 1213 C CD2 . LEU A 1 151 ? 18.854 27.191 11.585 1.00 17.29 ? 151 LEU A CD2 1 ATOM 1214 N N . PRO A 1 152 ? 21.043 22.389 12.026 1.00 14.16 ? 152 PRO A N 1 ATOM 1215 C CA . PRO A 1 152 ? 20.192 21.324 12.569 1.00 17.89 ? 152 PRO A CA 1 ATOM 1216 C C . PRO A 1 152 ? 18.988 21.948 13.246 1.00 16.42 ? 152 PRO A C 1 ATOM 1217 O O . PRO A 1 152 ? 19.143 22.939 13.953 1.00 18.33 ? 152 PRO A O 1 ATOM 1218 C CB . PRO A 1 152 ? 21.093 20.630 13.588 1.00 20.53 ? 152 PRO A CB 1 ATOM 1219 C CG . PRO A 1 152 ? 22.480 20.919 13.111 1.00 17.60 ? 152 PRO A CG 1 ATOM 1220 C CD . PRO A 1 152 ? 22.419 22.305 12.535 1.00 23.78 ? 152 PRO A CD 1 ATOM 1221 N N . PHE A 1 153 ? 17.811 21.369 13.066 1.00 23.76 ? 153 PHE A N 1 ATOM 1222 C CA . PHE A 1 153 ? 16.620 21.949 13.660 1.00 18.90 ? 153 PHE A CA 1 ATOM 1223 C C . PHE A 1 153 ? 15.522 20.927 13.892 1.00 25.60 ? 153 PHE A C 1 ATOM 1224 O O . PHE A 1 153 ? 15.500 19.854 13.280 1.00 22.89 ? 153 PHE A O 1 ATOM 1225 C CB . PHE A 1 153 ? 16.101 23.088 12.770 1.00 20.90 ? 153 PHE A CB 1 ATOM 1226 C CG . PHE A 1 153 ? 15.339 22.617 11.559 1.00 21.17 ? 153 PHE A CG 1 ATOM 1227 C CD1 . PHE A 1 153 ? 13.970 22.836 11.452 1.00 18.25 ? 153 PHE A CD1 1 ATOM 1228 C CD2 . PHE A 1 153 ? 15.992 21.933 10.534 1.00 11.26 ? 153 PHE A CD2 1 ATOM 1229 C CE1 . PHE A 1 153 ? 13.265 22.407 10.333 1.00 16.94 ? 153 PHE A CE1 1 ATOM 1230 C CE2 . PHE A 1 153 ? 15.310 21.500 9.424 1.00 11.23 ? 153 PHE A CE2 1 ATOM 1231 C CZ . PHE A 1 153 ? 13.935 21.737 9.315 1.00 18.48 ? 153 PHE A CZ 1 ATOM 1232 N N . LEU A 1 154 ? 14.591 21.293 14.767 1.00 31.76 ? 154 LEU A N 1 ATOM 1233 C CA . LEU A 1 154 ? 13.429 20.466 15.045 1.00 27.27 ? 154 LEU A CA 1 ATOM 1234 C C . LEU A 1 154 ? 12.205 21.119 14.414 1.00 25.81 ? 154 LEU A C 1 ATOM 1235 O O . LEU A 1 154 ? 11.732 22.149 14.881 1.00 25.62 ? 154 LEU A O 1 ATOM 1236 C CB . LEU A 1 154 ? 13.221 20.312 16.553 1.00 26.01 ? 154 LEU A CB 1 ATOM 1237 C CG . LEU A 1 154 ? 13.335 18.929 17.180 1.00 37.32 ? 154 LEU A CG 1 ATOM 1238 C CD1 . LEU A 1 154 ? 12.729 18.937 18.575 1.00 36.66 ? 154 LEU A CD1 1 ATOM 1239 C CD2 . LEU A 1 154 ? 12.673 17.881 16.304 1.00 32.14 ? 154 LEU A CD2 1 ATOM 1240 N N . PRO A 1 155 ? 11.718 20.541 13.315 1.00 22.62 ? 155 PRO A N 1 ATOM 1241 C CA . PRO A 1 155 ? 10.624 21.143 12.554 1.00 22.14 ? 155 PRO A CA 1 ATOM 1242 C C . PRO A 1 155 ? 9.371 21.345 13.412 1.00 31.14 ? 155 PRO A C 1 ATOM 1243 O O . PRO A 1 155 ? 8.993 20.456 14.175 1.00 29.87 ? 155 PRO A O 1 ATOM 1244 C CB . PRO A 1 155 ? 10.361 20.117 11.452 1.00 21.89 ? 155 PRO A CB 1 ATOM 1245 C CG . PRO A 1 155 ? 11.656 19.397 11.293 1.00 28.49 ? 155 PRO A CG 1 ATOM 1246 C CD . PRO A 1 155 ? 12.224 19.314 12.682 1.00 27.46 ? 155 PRO A CD 1 ATOM 1247 N N . SER A 1 156 ? 8.733 22.501 13.280 1.00 38.27 ? 156 SER A N 1 ATOM 1248 C CA . SER A 1 156 ? 7.516 22.794 14.029 1.00 36.41 ? 156 SER A CA 1 ATOM 1249 C C . SER A 1 156 ? 6.714 23.769 13.203 1.00 35.77 ? 156 SER A C 1 ATOM 1250 O O . SER A 1 156 ? 7.260 24.470 12.358 1.00 41.24 ? 156 SER A O 1 ATOM 1251 C CB . SER A 1 156 ? 7.800 23.377 15.420 1.00 34.75 ? 156 SER A CB 1 ATOM 1252 O OG . SER A 1 156 ? 8.401 24.656 15.351 1.00 44.91 ? 156 SER A OG 1 ATOM 1253 N N . THR A 1 157 ? 5.423 23.842 13.475 1.00 35.43 ? 157 THR A N 1 ATOM 1254 C CA . THR A 1 157 ? 4.548 24.773 12.780 1.00 29.86 ? 157 THR A CA 1 ATOM 1255 C C . THR A 1 157 ? 4.771 26.206 13.261 1.00 29.64 ? 157 THR A C 1 ATOM 1256 O O . THR A 1 157 ? 4.289 27.155 12.648 1.00 43.66 ? 157 THR A O 1 ATOM 1257 C CB . THR A 1 157 ? 3.077 24.383 12.964 1.00 34.61 ? 157 THR A CB 1 ATOM 1258 O OG1 . THR A 1 157 ? 2.785 24.292 14.364 1.00 36.78 ? 157 THR A OG1 1 ATOM 1259 C CG2 . THR A 1 157 ? 2.809 23.032 12.318 1.00 32.04 ? 157 THR A CG2 1 ATOM 1260 N N . GLU A 1 158 ? 5.511 26.355 14.355 1.00 33.09 ? 158 GLU A N 1 ATOM 1261 C CA . GLU A 1 158 ? 5.666 27.642 15.027 1.00 38.51 ? 158 GLU A CA 1 ATOM 1262 C C . GLU A 1 158 ? 6.891 28.452 14.586 1.00 45.92 ? 158 GLU A C 1 ATOM 1263 O O . GLU A 1 158 ? 7.008 29.636 14.908 1.00 44.67 ? 158 GLU A O 1 ATOM 1264 C CB . GLU A 1 158 ? 5.736 27.408 16.540 1.00 43.39 ? 158 GLU A CB 1 ATOM 1265 C CG . GLU A 1 158 ? 4.478 26.774 17.109 1.00 47.49 ? 158 GLU A CG 1 ATOM 1266 C CD . GLU A 1 158 ? 3.227 27.525 16.681 1.00 55.02 ? 158 GLU A CD 1 ATOM 1267 O OE1 . GLU A 1 158 ? 2.470 27.007 15.829 1.00 59.02 ? 158 GLU A OE1 1 ATOM 1268 O OE2 . GLU A 1 158 ? 3.005 28.645 17.190 1.00 60.90 ? 158 GLU A OE2 1 ATOM 1269 N N . ASP A 1 159 ? 7.807 27.818 13.866 1.00 30.53 ? 159 ASP A N 1 ATOM 1270 C CA . ASP A 1 159 ? 9.034 28.481 13.448 1.00 31.17 ? 159 ASP A CA 1 ATOM 1271 C C . ASP A 1 159 ? 9.153 28.684 11.939 1.00 29.86 ? 159 ASP A C 1 ATOM 1272 O O . ASP A 1 159 ? 8.796 27.815 11.146 1.00 35.95 ? 159 ASP A O 1 ATOM 1273 C CB . ASP A 1 159 ? 10.263 27.709 13.956 1.00 33.33 ? 159 ASP A CB 1 ATOM 1274 C CG . ASP A 1 159 ? 10.361 27.687 15.473 1.00 36.15 ? 159 ASP A CG 1 ATOM 1275 O OD1 . ASP A 1 159 ? 9.905 28.657 16.118 1.00 30.25 ? 159 ASP A OD1 1 ATOM 1276 O OD2 . ASP A 1 159 ? 10.890 26.698 16.024 1.00 42.72 ? 159 ASP A OD2 1 ATOM 1277 N N . VAL A 1 160 ? 9.642 29.857 11.554 1.00 24.18 ? 160 VAL A N 1 ATOM 1278 C CA . VAL A 1 160 ? 10.050 30.080 10.180 1.00 21.65 ? 160 VAL A CA 1 ATOM 1279 C C . VAL A 1 160 ? 11.543 30.376 10.176 1.00 20.90 ? 160 VAL A C 1 ATOM 1280 O O . VAL A 1 160 ? 12.098 30.838 11.169 1.00 21.04 ? 160 VAL A O 1 ATOM 1281 C CB . VAL A 1 160 ? 9.279 31.229 9.501 1.00 19.59 ? 160 VAL A CB 1 ATOM 1282 C CG1 . VAL A 1 160 ? 7.789 30.943 9.483 1.00 26.14 ? 160 VAL A CG1 1 ATOM 1283 C CG2 . VAL A 1 160 ? 9.615 32.568 10.153 1.00 15.99 ? 160 VAL A CG2 1 ATOM 1284 N N . TYR A 1 161 ? 12.194 30.078 9.059 1.00 18.11 ? 161 TYR A N 1 ATOM 1285 C CA . TYR A 1 161 ? 13.619 30.289 8.940 1.00 15.62 ? 161 TYR A CA 1 ATOM 1286 C C . TYR A 1 161 ? 13.944 31.079 7.692 1.00 18.54 ? 161 TYR A C 1 ATOM 1287 O O . TYR A 1 161 ? 13.212 31.040 6.701 1.00 17.85 ? 161 TYR A O 1 ATOM 1288 C CB . TYR A 1 161 ? 14.363 28.959 8.926 1.00 19.37 ? 161 TYR A CB 1 ATOM 1289 C CG . TYR A 1 161 ? 14.264 28.195 10.218 1.00 13.83 ? 161 TYR A CG 1 ATOM 1290 C CD1 . TYR A 1 161 ? 13.193 27.348 10.467 1.00 21.97 ? 161 TYR A CD1 1 ATOM 1291 C CD2 . TYR A 1 161 ? 15.261 28.297 11.175 1.00 15.36 ? 161 TYR A CD2 1 ATOM 1292 C CE1 . TYR A 1 161 ? 13.105 26.633 11.645 1.00 20.76 ? 161 TYR A CE1 1 ATOM 1293 C CE2 . TYR A 1 161 ? 15.193 27.588 12.353 1.00 22.49 ? 161 TYR A CE2 1 ATOM 1294 C CZ . TYR A 1 161 ? 14.113 26.754 12.585 1.00 26.22 ? 161 TYR A CZ 1 ATOM 1295 O OH . TYR A 1 161 ? 14.041 26.050 13.762 1.00 28.53 ? 161 TYR A OH 1 ATOM 1296 N N . ASP A 1 162 ? 15.074 31.770 7.747 1.00 17.22 ? 162 ASP A N 1 ATOM 1297 C CA . ASP A 1 162 ? 15.628 32.442 6.588 1.00 16.26 ? 162 ASP A CA 1 ATOM 1298 C C . ASP A 1 162 ? 17.122 32.264 6.638 1.00 16.47 ? 162 ASP A C 1 ATOM 1299 O O . ASP A 1 162 ? 17.728 32.274 7.712 1.00 13.82 ? 162 ASP A O 1 ATOM 1300 C CB . ASP A 1 162 ? 15.286 33.945 6.570 1.00 16.58 ? 162 ASP A CB 1 ATOM 1301 C CG . ASP A 1 162 ? 13.795 34.212 6.435 1.00 23.03 ? 162 ASP A CG 1 ATOM 1302 O OD1 . ASP A 1 162 ? 13.275 34.180 5.296 1.00 25.06 ? 162 ASP A OD1 1 ATOM 1303 O OD2 . ASP A 1 162 ? 13.139 34.446 7.476 1.00 20.04 ? 162 ASP A OD2 1 ATOM 1304 N N . CYS A 1 163 ? 17.718 32.107 5.466 1.00 17.74 ? 163 CYS A N 1 ATOM 1305 C CA . CYS A 1 163 ? 19.154 32.227 5.350 1.00 11.04 ? 163 CYS A CA 1 ATOM 1306 C C . CYS A 1 163 ? 19.442 33.601 4.778 1.00 16.33 ? 163 CYS A C 1 ATOM 1307 O O . CYS A 1 163 ? 18.943 33.948 3.703 1.00 16.71 ? 163 CYS A O 1 ATOM 1308 C CB . CYS A 1 163 ? 19.738 31.137 4.460 1.00 14.42 ? 163 CYS A CB 1 ATOM 1309 S SG . CYS A 1 163 ? 21.530 31.268 4.286 1.00 19.79 ? 163 CYS A SG 1 ATOM 1310 N N . ARG A 1 164 ? 20.208 34.403 5.514 1.00 17.85 ? 164 ARG A N 1 ATOM 1311 C CA . ARG A 1 164 ? 20.529 35.752 5.057 1.00 15.21 ? 164 ARG A CA 1 ATOM 1312 C C . ARG A 1 164 ? 21.967 35.860 4.579 1.00 14.25 ? 164 ARG A C 1 ATOM 1313 O O . ARG A 1 164 ? 22.915 35.548 5.311 1.00 14.76 ? 164 ARG A O 1 ATOM 1314 C CB . ARG A 1 164 ? 20.306 36.781 6.159 1.00 10.46 ? 164 ARG A CB 1 ATOM 1315 C CG . ARG A 1 164 ? 20.608 38.200 5.705 1.00 17.06 ? 164 ARG A CG 1 ATOM 1316 C CD . ARG A 1 164 ? 20.356 39.175 6.830 1.00 18.23 ? 164 ARG A CD 1 ATOM 1317 N NE . ARG A 1 164 ? 21.341 39.009 7.898 1.00 13.79 ? 164 ARG A NE 1 ATOM 1318 C CZ . ARG A 1 164 ? 21.103 39.280 9.177 1.00 21.84 ? 164 ARG A CZ 1 ATOM 1319 N NH1 . ARG A 1 164 ? 19.897 39.699 9.555 1.00 16.77 ? 164 ARG A NH1 1 ATOM 1320 N NH2 . ARG A 1 164 ? 22.056 39.104 10.083 1.00 16.45 ? 164 ARG A NH2 1 ATOM 1321 N N . VAL A 1 165 ? 22.125 36.290 3.337 1.00 14.72 ? 165 VAL A N 1 ATOM 1322 C CA . VAL A 1 165 ? 23.445 36.345 2.722 1.00 15.38 ? 165 VAL A CA 1 ATOM 1323 C C . VAL A 1 165 ? 23.809 37.771 2.306 1.00 17.21 ? 165 VAL A C 1 ATOM 1324 O O . VAL A 1 165 ? 23.039 38.437 1.615 1.00 18.47 ? 165 VAL A O 1 ATOM 1325 C CB . VAL A 1 165 ? 23.523 35.420 1.511 1.00 11.74 ? 165 VAL A CB 1 ATOM 1326 C CG1 . VAL A 1 165 ? 24.814 35.640 0.751 1.00 9.81 ? 165 VAL A CG1 1 ATOM 1327 C CG2 . VAL A 1 165 ? 23.359 33.968 1.950 1.00 11.37 ? 165 VAL A CG2 1 ATOM 1328 N N . GLU A 1 166 ? 24.954 38.248 2.775 1.00 12.65 ? 166 GLU A N 1 ATOM 1329 C CA . GLU A 1 166 ? 25.470 39.551 2.364 1.00 17.87 ? 166 GLU A CA 1 ATOM 1330 C C . GLU A 1 166 ? 26.696 39.338 1.487 1.00 16.83 ? 166 GLU A C 1 ATOM 1331 O O . GLU A 1 166 ? 27.594 38.565 1.839 1.00 11.20 ? 166 GLU A O 1 ATOM 1332 C CB . GLU A 1 166 ? 25.820 40.428 3.565 1.00 18.10 ? 166 GLU A CB 1 ATOM 1333 C CG . GLU A 1 166 ? 24.737 40.515 4.635 1.00 25.87 ? 166 GLU A CG 1 ATOM 1334 C CD . GLU A 1 166 ? 25.262 41.092 5.959 1.00 47.95 ? 166 GLU A CD 1 ATOM 1335 O OE1 . GLU A 1 166 ? 26.221 41.904 5.937 1.00 40.85 ? 166 GLU A OE1 1 ATOM 1336 O OE2 . GLU A 1 166 ? 24.723 40.718 7.026 1.00 40.72 ? 166 GLU A OE2 1 ATOM 1337 N N . HIS A 1 167 ? 26.753 40.058 0.375 1.00 15.13 ? 167 HIS A N 1 ATOM 1338 C CA . HIS A 1 167 ? 27.880 39.973 -0.539 1.00 12.07 ? 167 HIS A CA 1 ATOM 1339 C C . HIS A 1 167 ? 28.020 41.307 -1.274 1.00 10.84 ? 167 HIS A C 1 ATOM 1340 O O . HIS A 1 167 ? 27.027 41.961 -1.567 1.00 13.20 ? 167 HIS A O 1 ATOM 1341 C CB . HIS A 1 167 ? 27.672 38.791 -1.509 1.00 8.75 ? 167 HIS A CB 1 ATOM 1342 C CG . HIS A 1 167 ? 28.846 38.519 -2.398 1.00 9.53 ? 167 HIS A CG 1 ATOM 1343 N ND1 . HIS A 1 167 ? 29.007 39.125 -3.626 1.00 12.37 ? 167 HIS A ND1 1 ATOM 1344 C CD2 . HIS A 1 167 ? 29.941 37.741 -2.215 1.00 7.35 ? 167 HIS A CD2 1 ATOM 1345 C CE1 . HIS A 1 167 ? 30.142 38.714 -4.169 1.00 15.53 ? 167 HIS A CE1 1 ATOM 1346 N NE2 . HIS A 1 167 ? 30.729 37.877 -3.330 1.00 10.25 ? 167 HIS A NE2 1 ATOM 1347 N N . TRP A 1 168 ? 29.246 41.701 -1.590 1.00 12.51 ? 168 TRP A N 1 ATOM 1348 C CA . TRP A 1 168 ? 29.484 43.009 -2.207 1.00 17.48 ? 168 TRP A CA 1 ATOM 1349 C C . TRP A 1 168 ? 28.815 43.183 -3.562 1.00 16.18 ? 168 TRP A C 1 ATOM 1350 O O . TRP A 1 168 ? 28.625 44.303 -4.010 1.00 20.15 ? 168 TRP A O 1 ATOM 1351 C CB . TRP A 1 168 ? 30.985 43.287 -2.309 1.00 13.59 ? 168 TRP A CB 1 ATOM 1352 C CG . TRP A 1 168 ? 31.624 43.374 -0.945 1.00 17.02 ? 168 TRP A CG 1 ATOM 1353 C CD1 . TRP A 1 168 ? 31.113 44.015 0.150 1.00 21.09 ? 168 TRP A CD1 1 ATOM 1354 C CD2 . TRP A 1 168 ? 32.879 42.816 -0.532 1.00 15.39 ? 168 TRP A CD2 1 ATOM 1355 N NE1 . TRP A 1 168 ? 31.968 43.888 1.216 1.00 23.53 ? 168 TRP A NE1 1 ATOM 1356 C CE2 . TRP A 1 168 ? 33.059 43.156 0.827 1.00 18.25 ? 168 TRP A CE2 1 ATOM 1357 C CE3 . TRP A 1 168 ? 33.866 42.062 -1.177 1.00 19.22 ? 168 TRP A CE3 1 ATOM 1358 C CZ2 . TRP A 1 168 ? 34.182 42.762 1.555 1.00 17.57 ? 168 TRP A CZ2 1 ATOM 1359 C CZ3 . TRP A 1 168 ? 34.988 41.674 -0.453 1.00 16.16 ? 168 TRP A CZ3 1 ATOM 1360 C CH2 . TRP A 1 168 ? 35.135 42.023 0.899 1.00 18.29 ? 168 TRP A CH2 1 ATOM 1361 N N . GLY A 1 169 ? 28.463 42.083 -4.216 1.00 13.27 ? 169 GLY A N 1 ATOM 1362 C CA . GLY A 1 169 ? 27.769 42.162 -5.488 1.00 17.51 ? 169 GLY A CA 1 ATOM 1363 C C . GLY A 1 169 ? 26.272 42.390 -5.340 1.00 17.06 ? 169 GLY A C 1 ATOM 1364 O O . GLY A 1 169 ? 25.581 42.621 -6.324 1.00 16.18 ? 169 GLY A O 1 ATOM 1365 N N . LEU A 1 170 ? 25.778 42.324 -4.104 1.00 15.58 ? 170 LEU A N 1 ATOM 1366 C CA . LEU A 1 170 ? 24.364 42.541 -3.800 1.00 16.65 ? 170 LEU A CA 1 ATOM 1367 C C . LEU A 1 170 ? 24.089 43.947 -3.277 1.00 22.02 ? 170 LEU A C 1 ATOM 1368 O O . LEU A 1 170 ? 24.854 44.467 -2.467 1.00 26.20 ? 170 LEU A O 1 ATOM 1369 C CB . LEU A 1 170 ? 23.899 41.519 -2.758 1.00 11.62 ? 170 LEU A CB 1 ATOM 1370 C CG . LEU A 1 170 ? 23.890 40.037 -3.128 1.00 17.24 ? 170 LEU A CG 1 ATOM 1371 C CD1 . LEU A 1 170 ? 23.708 39.173 -1.898 1.00 6.72 ? 170 LEU A CD1 1 ATOM 1372 C CD2 . LEU A 1 170 ? 22.771 39.765 -4.124 1.00 14.62 ? 170 LEU A CD2 1 ATOM 1373 N N . ASP A 1 171 ? 22.991 44.549 -3.736 1.00 32.07 ? 171 ASP A N 1 ATOM 1374 C CA . ASP A 1 171 ? 22.553 45.878 -3.272 1.00 35.30 ? 171 ASP A CA 1 ATOM 1375 C C . ASP A 1 171 ? 21.937 45.816 -1.881 1.00 35.79 ? 171 ASP A C 1 ATOM 1376 O O . ASP A 1 171 ? 22.041 46.756 -1.093 1.00 43.52 ? 171 ASP A O 1 ATOM 1377 C CB . ASP A 1 171 ? 21.547 46.500 -4.240 1.00 40.68 ? 171 ASP A CB 1 ATOM 1378 C CG . ASP A 1 171 ? 22.195 47.015 -5.505 1.00 58.10 ? 171 ASP A CG 1 ATOM 1379 O OD1 . ASP A 1 171 ? 23.387 47.387 -5.452 1.00 61.92 ? 171 ASP A OD1 1 ATOM 1380 O OD2 . ASP A 1 171 ? 21.509 47.048 -6.550 1.00 73.77 ? 171 ASP A OD2 1 ATOM 1381 N N A GLU A 1 172 ? 21.284 44.689 -1.609 0.27 31.79 ? 172 GLU A N 1 ATOM 1382 N N B GLU A 1 172 ? 21.306 44.693 -1.572 0.73 31.74 ? 172 GLU A N 1 ATOM 1383 C CA A GLU A 1 172 ? 20.608 44.417 -0.346 0.27 31.11 ? 172 GLU A CA 1 ATOM 1384 C CA B GLU A 1 172 ? 20.723 44.484 -0.260 0.73 30.79 ? 172 GLU A CA 1 ATOM 1385 C C A GLU A 1 172 ? 21.014 43.025 0.127 0.27 28.93 ? 172 GLU A C 1 ATOM 1386 C C B GLU A 1 172 ? 20.983 43.047 0.135 0.73 28.96 ? 172 GLU A C 1 ATOM 1387 O O A GLU A 1 172 ? 21.423 42.198 -0.689 0.27 27.03 ? 172 GLU A O 1 ATOM 1388 O O B GLU A 1 172 ? 21.246 42.208 -0.728 0.73 26.94 ? 172 GLU A O 1 ATOM 1389 C CB A GLU A 1 172 ? 19.086 44.492 -0.523 0.27 34.94 ? 172 GLU A CB 1 ATOM 1390 C CB B GLU A 1 172 ? 19.209 44.754 -0.276 0.73 35.61 ? 172 GLU A CB 1 ATOM 1391 C CG A GLU A 1 172 ? 18.349 45.356 0.486 0.27 38.59 ? 172 GLU A CG 1 ATOM 1392 C CG B GLU A 1 172 ? 18.780 46.093 -0.868 0.73 43.15 ? 172 GLU A CG 1 ATOM 1393 C CD A GLU A 1 172 ? 18.224 46.803 0.040 0.27 39.01 ? 172 GLU A CD 1 ATOM 1394 C CD B GLU A 1 172 ? 17.814 45.937 -2.030 0.73 41.45 ? 172 GLU A CD 1 ATOM 1395 O OE1 A GLU A 1 172 ? 19.134 47.298 -0.658 0.27 40.04 ? 172 GLU A OE1 1 ATOM 1396 O OE1 B GLU A 1 172 ? 17.135 44.889 -2.100 0.73 46.36 ? 172 GLU A OE1 1 ATOM 1397 O OE2 A GLU A 1 172 ? 17.219 47.452 0.396 0.27 34.06 ? 172 GLU A OE2 1 ATOM 1398 O OE2 B GLU A 1 172 ? 17.732 46.865 -2.868 0.73 45.43 ? 172 GLU A OE2 1 ATOM 1399 N N . PRO A 1 173 ? 20.913 42.752 1.438 1.00 26.94 ? 173 PRO A N 1 ATOM 1400 C CA . PRO A 1 173 ? 21.129 41.358 1.832 1.00 26.99 ? 173 PRO A CA 1 ATOM 1401 C C . PRO A 1 173 ? 20.052 40.477 1.201 1.00 23.31 ? 173 PRO A C 1 ATOM 1402 O O . PRO A 1 173 ? 18.918 40.915 1.019 1.00 17.51 ? 173 PRO A O 1 ATOM 1403 C CB . PRO A 1 173 ? 20.999 41.396 3.356 1.00 28.85 ? 173 PRO A CB 1 ATOM 1404 C CG . PRO A 1 173 ? 21.318 42.827 3.728 1.00 28.68 ? 173 PRO A CG 1 ATOM 1405 C CD . PRO A 1 173 ? 20.811 43.660 2.594 1.00 26.70 ? 173 PRO A CD 1 ATOM 1406 N N . LEU A 1 174 ? 20.430 39.263 0.830 1.00 15.83 ? 174 LEU A N 1 ATOM 1407 C CA . LEU A 1 174 ? 19.500 38.338 0.208 1.00 21.33 ? 174 LEU A CA 1 ATOM 1408 C C . LEU A 1 174 ? 18.971 37.404 1.268 1.00 14.65 ? 174 LEU A C 1 ATOM 1409 O O . LEU A 1 174 ? 19.742 36.738 1.951 1.00 16.66 ? 174 LEU A O 1 ATOM 1410 C CB . LEU A 1 174 ? 20.194 37.600 -0.933 1.00 15.34 ? 174 LEU A CB 1 ATOM 1411 C CG . LEU A 1 174 ? 19.448 36.756 -1.947 1.00 20.47 ? 174 LEU A CG 1 ATOM 1412 C CD1 . LEU A 1 174 ? 18.277 37.498 -2.512 1.00 16.65 ? 174 LEU A CD1 1 ATOM 1413 C CD2 . LEU A 1 174 ? 20.432 36.454 -3.058 1.00 20.65 ? 174 LEU A CD2 1 ATOM 1414 N N . LEU A 1 175 ? 17.656 37.361 1.411 1.00 19.61 ? 175 LEU A N 1 ATOM 1415 C CA . LEU A 1 175 ? 17.023 36.447 2.353 1.00 20.13 ? 175 LEU A CA 1 ATOM 1416 C C . LEU A 1 175 ? 16.272 35.358 1.619 1.00 22.46 ? 175 LEU A C 1 ATOM 1417 O O . LEU A 1 175 ? 15.411 35.638 0.782 1.00 23.06 ? 175 LEU A O 1 ATOM 1418 C CB . LEU A 1 175 ? 16.048 37.177 3.277 1.00 16.50 ? 175 LEU A CB 1 ATOM 1419 C CG . LEU A 1 175 ? 16.659 37.767 4.537 1.00 18.79 ? 175 LEU A CG 1 ATOM 1420 C CD1 . LEU A 1 175 ? 17.423 39.027 4.182 1.00 18.47 ? 175 LEU A CD1 1 ATOM 1421 C CD2 . LEU A 1 175 ? 15.593 38.015 5.582 1.00 16.53 ? 175 LEU A CD2 1 ATOM 1422 N N . LYS A 1 176 ? 16.596 34.114 1.938 1.00 17.88 ? 176 LYS A N 1 ATOM 1423 C CA . LYS A 1 176 ? 15.861 32.998 1.383 1.00 12.54 ? 176 LYS A CA 1 ATOM 1424 C C . LYS A 1 176 ? 15.119 32.280 2.489 1.00 13.38 ? 176 LYS A C 1 ATOM 1425 O O . LYS A 1 176 ? 15.707 31.858 3.489 1.00 14.77 ? 176 LYS A O 1 ATOM 1426 C CB . LYS A 1 176 ? 16.804 32.054 0.637 1.00 17.96 ? 176 LYS A CB 1 ATOM 1427 C CG . LYS A 1 176 ? 16.479 31.938 -0.838 1.00 21.28 ? 176 LYS A CG 1 ATOM 1428 C CD . LYS A 1 176 ? 16.603 33.275 -1.547 1.00 23.34 ? 176 LYS A CD 1 ATOM 1429 C CE . LYS A 1 176 ? 16.465 33.123 -3.057 1.00 30.61 ? 176 LYS A CE 1 ATOM 1430 N NZ . LYS A 1 176 ? 16.387 34.432 -3.781 1.00 31.80 ? 176 LYS A NZ 1 ATOM 1431 N N . HIS A 1 177 ? 13.825 32.095 2.274 1.00 18.31 ? 177 HIS A N 1 ATOM 1432 C CA . HIS A 1 177 ? 12.927 31.665 3.332 1.00 19.56 ? 177 HIS A CA 1 ATOM 1433 C C . HIS A 1 177 ? 12.705 30.177 3.332 1.00 17.12 ? 177 HIS A C 1 ATOM 1434 O O . HIS A 1 177 ? 12.762 29.536 2.282 1.00 19.64 ? 177 HIS A O 1 ATOM 1435 C CB . HIS A 1 177 ? 11.585 32.382 3.175 1.00 15.93 ? 177 HIS A CB 1 ATOM 1436 C CG . HIS A 1 177 ? 10.687 32.252 4.361 1.00 20.83 ? 177 HIS A CG 1 ATOM 1437 N ND1 . HIS A 1 177 ? 10.873 32.972 5.521 1.00 20.75 ? 177 HIS A ND1 1 ATOM 1438 C CD2 . HIS A 1 177 ? 9.577 31.501 4.556 1.00 22.11 ? 177 HIS A CD2 1 ATOM 1439 C CE1 . HIS A 1 177 ? 9.923 32.660 6.385 1.00 25.27 ? 177 HIS A CE1 1 ATOM 1440 N NE2 . HIS A 1 177 ? 9.125 31.769 5.824 1.00 25.60 ? 177 HIS A NE2 1 ATOM 1441 N N . TRP A 1 178 ? 12.470 29.624 4.517 1.00 13.94 ? 178 TRP A N 1 ATOM 1442 C CA . TRP A 1 178 ? 11.942 28.271 4.604 1.00 18.63 ? 178 TRP A CA 1 ATOM 1443 C C . TRP A 1 178 ? 10.925 28.169 5.732 1.00 16.45 ? 178 TRP A C 1 ATOM 1444 O O . TRP A 1 178 ? 11.128 28.713 6.814 1.00 19.57 ? 178 TRP A O 1 ATOM 1445 C CB . TRP A 1 178 ? 13.049 27.224 4.817 1.00 14.96 ? 178 TRP A CB 1 ATOM 1446 C CG . TRP A 1 178 ? 12.479 25.834 4.874 1.00 17.02 ? 178 TRP A CG 1 ATOM 1447 C CD1 . TRP A 1 178 ? 12.350 24.976 3.822 1.00 21.79 ? 178 TRP A CD1 1 ATOM 1448 C CD2 . TRP A 1 178 ? 11.922 25.153 6.012 1.00 19.08 ? 178 TRP A CD2 1 ATOM 1449 N NE1 . TRP A 1 178 ? 11.759 23.804 4.225 1.00 19.30 ? 178 TRP A NE1 1 ATOM 1450 C CE2 . TRP A 1 178 ? 11.486 23.882 5.564 1.00 26.58 ? 178 TRP A CE2 1 ATOM 1451 C CE3 . TRP A 1 178 ? 11.753 25.486 7.359 1.00 17.63 ? 178 TRP A CE3 1 ATOM 1452 C CZ2 . TRP A 1 178 ? 10.899 22.944 6.417 1.00 19.89 ? 178 TRP A CZ2 1 ATOM 1453 C CZ3 . TRP A 1 178 ? 11.162 24.558 8.204 1.00 17.01 ? 178 TRP A CZ3 1 ATOM 1454 C CH2 . TRP A 1 178 ? 10.746 23.300 7.730 1.00 24.65 ? 178 TRP A CH2 1 ATOM 1455 N N . GLU A 1 179 ? 9.819 27.492 5.464 1.00 16.57 ? 179 GLU A N 1 ATOM 1456 C CA . GLU A 1 179 ? 8.882 27.131 6.517 1.00 29.94 ? 179 GLU A CA 1 ATOM 1457 C C . GLU A 1 179 ? 8.149 25.827 6.221 1.00 26.39 ? 179 GLU A C 1 ATOM 1458 O O . GLU A 1 179 ? 8.052 25.394 5.069 1.00 25.08 ? 179 GLU A O 1 ATOM 1459 C CB . GLU A 1 179 ? 7.883 28.271 6.740 1.00 27.05 ? 179 GLU A CB 1 ATOM 1460 C CG . GLU A 1 179 ? 6.930 28.479 5.591 1.00 22.33 ? 179 GLU A CG 1 ATOM 1461 C CD . GLU A 1 179 ? 6.023 29.679 5.807 1.00 38.34 ? 179 GLU A CD 1 ATOM 1462 O OE1 . GLU A 1 179 ? 6.539 30.772 6.124 1.00 38.20 ? 179 GLU A OE1 1 ATOM 1463 O OE2 . GLU A 1 179 ? 4.798 29.540 5.627 1.00 41.07 ? 179 GLU A OE2 1 ATOM 1464 N N . PHE A 1 180 ? 7.647 25.213 7.287 1.00 27.40 ? 180 PHE A N 1 ATOM 1465 C CA . PHE A 1 180 ? 6.961 23.928 7.228 1.00 31.47 ? 180 PHE A CA 1 ATOM 1466 C C . PHE A 1 180 ? 5.723 24.063 6.340 1.00 38.44 ? 180 PHE A C 1 ATOM 1467 O O . PHE A 1 180 ? 4.918 24.966 6.568 1.00 42.46 ? 180 PHE A O 1 ATOM 1468 C CB . PHE A 1 180 ? 6.584 23.467 8.641 1.00 38.86 ? 180 PHE A CB 1 ATOM 1469 C CG . PHE A 1 180 ? 5.971 22.102 8.692 1.00 36.66 ? 180 PHE A CG 1 ATOM 1470 C CD1 . PHE A 1 180 ? 4.608 21.953 8.875 1.00 39.09 ? 180 PHE A CD1 1 ATOM 1471 C CD2 . PHE A 1 180 ? 6.758 20.966 8.565 1.00 35.87 ? 180 PHE A CD2 1 ATOM 1472 C CE1 . PHE A 1 180 ? 4.034 20.696 8.924 1.00 46.67 ? 180 PHE A CE1 1 ATOM 1473 C CE2 . PHE A 1 180 ? 6.193 19.703 8.612 1.00 33.64 ? 180 PHE A CE2 1 ATOM 1474 C CZ . PHE A 1 180 ? 4.830 19.567 8.787 1.00 41.64 ? 180 PHE A CZ 1 ATOM 1475 N N . ASP A 1 181 ? 5.626 23.188 5.331 1.00 47.16 ? 181 ASP A N 1 ATOM 1476 C CA . ASP A 1 181 ? 4.600 23.144 4.257 1.00 63.15 ? 181 ASP A CA 1 ATOM 1477 C C . ASP A 1 181 ? 5.183 23.657 2.945 1.00 69.71 ? 181 ASP A C 1 ATOM 1478 O O . ASP A 1 181 ? 4.620 23.422 1.874 1.00 74.98 ? 181 ASP A O 1 ATOM 1479 C CB . ASP A 1 181 ? 3.323 23.940 4.576 1.00 70.21 ? 181 ASP A CB 1 ATOM 1480 C CG . ASP A 1 181 ? 2.219 23.074 5.148 1.00 71.42 ? 181 ASP A CG 1 ATOM 1481 O OD1 . ASP A 1 181 ? 2.220 21.856 4.868 1.00 65.63 ? 181 ASP A OD1 1 ATOM 1482 O OD2 . ASP A 1 181 ? 1.351 23.616 5.868 1.00 63.52 ? 181 ASP A OD2 1 ATOM 1483 N N . ASP B 2 4 ? 32.626 48.425 3.016 1.00 49.57 ? 2 ASP B N 1 ATOM 1484 C CA . ASP B 2 4 ? 33.938 48.266 2.394 1.00 49.21 ? 2 ASP B CA 1 ATOM 1485 C C . ASP B 2 4 ? 33.845 48.212 0.870 1.00 47.70 ? 2 ASP B C 1 ATOM 1486 O O . ASP B 2 4 ? 33.470 47.193 0.282 1.00 44.28 ? 2 ASP B O 1 ATOM 1487 C CB . ASP B 2 4 ? 34.635 47.007 2.937 1.00 49.16 ? 2 ASP B CB 1 ATOM 1488 C CG . ASP B 2 4 ? 36.145 47.012 2.697 1.00 28.40 ? 2 ASP B CG 1 ATOM 1489 O OD1 . ASP B 2 4 ? 36.629 47.781 1.842 1.00 31.42 ? 2 ASP B OD1 1 ATOM 1490 O OD2 . ASP B 2 4 ? 36.858 46.265 3.395 1.00 45.97 ? 2 ASP B OD2 1 ATOM 1491 N N . THR B 2 5 ? 34.204 49.322 0.238 1.00 40.21 ? 3 THR B N 1 ATOM 1492 C CA . THR B 2 5 ? 34.108 49.440 -1.209 1.00 44.89 ? 3 THR B CA 1 ATOM 1493 C C . THR B 2 5 ? 35.497 49.305 -1.861 1.00 37.89 ? 3 THR B C 1 ATOM 1494 O O . THR B 2 5 ? 35.641 49.489 -3.072 1.00 40.79 ? 3 THR B O 1 ATOM 1495 C CB . THR B 2 5 ? 33.439 50.773 -1.638 1.00 43.42 ? 3 THR B CB 1 ATOM 1496 O OG1 . THR B 2 5 ? 34.179 51.883 -1.120 1.00 47.76 ? 3 THR B OG1 1 ATOM 1497 C CG2 . THR B 2 5 ? 32.004 50.838 -1.130 1.00 46.03 ? 3 THR B CG2 1 ATOM 1498 N N . ARG B 2 6 ? 36.519 49.024 -1.052 1.00 24.94 ? 4 ARG B N 1 ATOM 1499 C CA . ARG B 2 6 ? 37.874 48.852 -1.574 1.00 30.66 ? 4 ARG B CA 1 ATOM 1500 C C . ARG B 2 6 ? 37.889 47.743 -2.634 1.00 33.41 ? 4 ARG B C 1 ATOM 1501 O O . ARG B 2 6 ? 37.267 46.690 -2.454 1.00 21.99 ? 4 ARG B O 1 ATOM 1502 C CB . ARG B 2 6 ? 38.857 48.487 -0.460 1.00 26.83 ? 4 ARG B CB 1 ATOM 1503 C CG . ARG B 2 6 ? 39.245 49.604 0.481 1.00 27.74 ? 4 ARG B CG 1 ATOM 1504 C CD . ARG B 2 6 ? 40.240 49.076 1.505 1.00 28.67 ? 4 ARG B CD 1 ATOM 1505 N NE . ARG B 2 6 ? 39.649 48.030 2.341 1.00 33.87 ? 4 ARG B NE 1 ATOM 1506 C CZ . ARG B 2 6 ? 40.353 47.205 3.112 1.00 38.76 ? 4 ARG B CZ 1 ATOM 1507 N NH1 . ARG B 2 6 ? 41.676 47.310 3.159 1.00 29.47 ? 4 ARG B NH1 1 ATOM 1508 N NH2 . ARG B 2 6 ? 39.738 46.283 3.844 1.00 36.20 ? 4 ARG B NH2 1 ATOM 1509 N N . PRO B 2 7 ? 38.619 47.967 -3.732 1.00 28.50 ? 5 PRO B N 1 ATOM 1510 C CA . PRO B 2 7 ? 38.751 46.973 -4.802 1.00 21.33 ? 5 PRO B CA 1 ATOM 1511 C C . PRO B 2 7 ? 39.437 45.696 -4.313 1.00 18.16 ? 5 PRO B C 1 ATOM 1512 O O . PRO B 2 7 ? 40.329 45.740 -3.460 1.00 19.55 ? 5 PRO B O 1 ATOM 1513 C CB . PRO B 2 7 ? 39.601 47.698 -5.858 1.00 24.76 ? 5 PRO B CB 1 ATOM 1514 C CG . PRO B 2 7 ? 40.284 48.810 -5.116 1.00 26.10 ? 5 PRO B CG 1 ATOM 1515 C CD . PRO B 2 7 ? 39.332 49.220 -4.038 1.00 24.73 ? 5 PRO B CD 1 ATOM 1516 N N . ARG B 2 8 ? 38.989 44.561 -4.832 1.00 14.40 ? 6 ARG B N 1 ATOM 1517 C CA . ARG B 2 8 ? 39.573 43.274 -4.488 1.00 12.95 ? 6 ARG B CA 1 ATOM 1518 C C . ARG B 2 8 ? 40.375 42.740 -5.649 1.00 12.25 ? 6 ARG B C 1 ATOM 1519 O O . ARG B 2 8 ? 40.097 43.063 -6.804 1.00 14.80 ? 6 ARG B O 1 ATOM 1520 C CB . ARG B 2 8 ? 38.496 42.262 -4.090 1.00 14.28 ? 6 ARG B CB 1 ATOM 1521 C CG . ARG B 2 8 ? 38.381 42.052 -2.600 1.00 15.66 ? 6 ARG B CG 1 ATOM 1522 C CD . ARG B 2 8 ? 37.987 43.344 -1.901 1.00 13.75 ? 6 ARG B CD 1 ATOM 1523 N NE . ARG B 2 8 ? 38.025 43.192 -0.448 1.00 16.31 ? 6 ARG B NE 1 ATOM 1524 C CZ . ARG B 2 8 ? 37.635 44.129 0.413 1.00 21.28 ? 6 ARG B CZ 1 ATOM 1525 N NH1 . ARG B 2 8 ? 37.189 45.298 -0.027 1.00 21.31 ? 6 ARG B NH1 1 ATOM 1526 N NH2 . ARG B 2 8 ? 37.704 43.899 1.715 1.00 17.28 ? 6 ARG B NH2 1 ATOM 1527 N N . PHE B 2 9 ? 41.379 41.933 -5.322 1.00 10.06 ? 7 PHE B N 1 ATOM 1528 C CA . PHE B 2 9 ? 42.245 41.289 -6.300 1.00 9.61 ? 7 PHE B CA 1 ATOM 1529 C C . PHE B 2 9 ? 42.439 39.840 -5.875 1.00 11.69 ? 7 PHE B C 1 ATOM 1530 O O . PHE B 2 9 ? 42.749 39.552 -4.706 1.00 9.89 ? 7 PHE B O 1 ATOM 1531 C CB . PHE B 2 9 ? 43.577 42.044 -6.387 1.00 11.44 ? 7 PHE B CB 1 ATOM 1532 C CG . PHE B 2 9 ? 43.410 43.528 -6.617 1.00 11.31 ? 7 PHE B CG 1 ATOM 1533 C CD1 . PHE B 2 9 ? 43.300 44.401 -5.545 1.00 12.98 ? 7 PHE B CD1 1 ATOM 1534 C CD2 . PHE B 2 9 ? 43.395 44.054 -7.896 1.00 15.02 ? 7 PHE B CD2 1 ATOM 1535 C CE1 . PHE B 2 9 ? 43.146 45.762 -5.746 1.00 12.28 ? 7 PHE B CE1 1 ATOM 1536 C CE2 . PHE B 2 9 ? 43.256 45.426 -8.102 1.00 14.68 ? 7 PHE B CE2 1 ATOM 1537 C CZ . PHE B 2 9 ? 43.127 46.275 -7.022 1.00 12.27 ? 7 PHE B CZ 1 ATOM 1538 N N . LEU B 2 10 ? 42.226 38.924 -6.811 1.00 10.51 ? 8 LEU B N 1 ATOM 1539 C CA . LEU B 2 10 ? 42.216 37.501 -6.496 1.00 6.69 ? 8 LEU B CA 1 ATOM 1540 C C . LEU B 2 10 ? 43.180 36.687 -7.355 1.00 7.75 ? 8 LEU B C 1 ATOM 1541 O O . LEU B 2 10 ? 43.224 36.846 -8.574 1.00 6.73 ? 8 LEU B O 1 ATOM 1542 C CB . LEU B 2 10 ? 40.793 36.961 -6.623 1.00 8.43 ? 8 LEU B CB 1 ATOM 1543 C CG . LEU B 2 10 ? 40.556 35.478 -6.374 1.00 9.13 ? 8 LEU B CG 1 ATOM 1544 C CD1 . LEU B 2 10 ? 40.715 35.191 -4.896 1.00 8.59 ? 8 LEU B CD1 1 ATOM 1545 C CD2 . LEU B 2 10 ? 39.144 35.121 -6.823 1.00 7.76 ? 8 LEU B CD2 1 ATOM 1546 N N . GLU B 2 11 ? 43.971 35.837 -6.713 1.00 3.57 ? 9 GLU B N 1 ATOM 1547 C CA . GLU B 2 11 ? 44.791 34.879 -7.432 1.00 5.30 ? 9 GLU B CA 1 ATOM 1548 C C . GLU B 2 11 ? 44.252 33.471 -7.156 1.00 7.18 ? 9 GLU B C 1 ATOM 1549 O O . GLU B 2 11 ? 43.906 33.143 -6.015 1.00 8.82 ? 9 GLU B O 1 ATOM 1550 C CB . GLU B 2 11 ? 46.267 34.998 -7.013 1.00 5.71 ? 9 GLU B CB 1 ATOM 1551 C CG . GLU B 2 11 ? 47.189 33.952 -7.640 1.00 8.48 ? 9 GLU B CG 1 ATOM 1552 C CD . GLU B 2 11 ? 47.636 34.274 -9.068 1.00 11.01 ? 9 GLU B CD 1 ATOM 1553 O OE1 . GLU B 2 11 ? 47.407 35.410 -9.551 1.00 4.05 ? 9 GLU B OE1 1 ATOM 1554 O OE2 . GLU B 2 11 ? 48.194 33.357 -9.719 1.00 6.78 ? 9 GLU B OE2 1 ATOM 1555 N N . GLN B 2 12 ? 44.121 32.655 -8.192 1.00 3.98 ? 10 GLN B N 1 ATOM 1556 C CA . GLN B 2 12 ? 43.766 31.255 -7.971 1.00 10.33 ? 10 GLN B CA 1 ATOM 1557 C C . GLN B 2 12 ? 44.746 30.338 -8.658 1.00 4.49 ? 10 GLN B C 1 ATOM 1558 O O . GLN B 2 12 ? 45.256 30.657 -9.726 1.00 5.59 ? 10 GLN B O 1 ATOM 1559 C CB . GLN B 2 12 ? 42.353 30.928 -8.472 1.00 4.90 ? 10 GLN B CB 1 ATOM 1560 C CG . GLN B 2 12 ? 41.244 31.798 -7.951 1.00 4.32 ? 10 GLN B CG 1 ATOM 1561 C CD . GLN B 2 12 ? 39.889 31.244 -8.347 1.00 7.40 ? 10 GLN B CD 1 ATOM 1562 O OE1 . GLN B 2 12 ? 39.510 30.137 -7.961 1.00 8.34 ? 10 GLN B OE1 1 ATOM 1563 N NE2 . GLN B 2 12 ? 39.173 31.995 -9.158 1.00 5.01 ? 10 GLN B NE2 1 ATOM 1564 N N . VAL B 2 13 ? 44.947 29.171 -8.061 1.00 3.15 ? 11 VAL B N 1 ATOM 1565 C CA . VAL B 2 13 ? 45.709 28.104 -8.673 1.00 4.16 ? 11 VAL B CA 1 ATOM 1566 C C . VAL B 2 13 ? 44.942 26.820 -8.527 1.00 4.64 ? 11 VAL B C 1 ATOM 1567 O O . VAL B 2 13 ? 44.418 26.523 -7.450 1.00 5.28 ? 11 VAL B O 1 ATOM 1568 C CB . VAL B 2 13 ? 47.125 27.949 -8.038 1.00 4.25 ? 11 VAL B CB 1 ATOM 1569 C CG1 . VAL B 2 13 ? 47.936 26.890 -8.767 1.00 3.59 ? 11 VAL B CG1 1 ATOM 1570 C CG2 . VAL B 2 13 ? 47.842 29.287 -8.011 1.00 3.65 ? 11 VAL B CG2 1 ATOM 1571 N N . LYS B 2 14 ? 44.867 26.068 -9.615 1.00 5.19 ? 12 LYS B N 1 ATOM 1572 C CA . LYS B 2 14 ? 44.244 24.757 -9.593 1.00 5.45 ? 12 LYS B CA 1 ATOM 1573 C C . LYS B 2 14 ? 45.150 23.699 -10.221 1.00 4.55 ? 12 LYS B C 1 ATOM 1574 O O . LYS B 2 14 ? 45.512 23.784 -11.394 1.00 4.40 ? 12 LYS B O 1 ATOM 1575 C CB . LYS B 2 14 ? 42.883 24.802 -10.310 1.00 6.92 ? 12 LYS B CB 1 ATOM 1576 C CG . LYS B 2 14 ? 41.871 25.706 -9.602 1.00 4.66 ? 12 LYS B CG 1 ATOM 1577 C CD . LYS B 2 14 ? 40.533 25.743 -10.318 1.00 5.52 ? 12 LYS B CD 1 ATOM 1578 C CE . LYS B 2 14 ? 39.536 26.601 -9.546 1.00 7.64 ? 12 LYS B CE 1 ATOM 1579 N NZ . LYS B 2 14 ? 38.189 26.690 -10.190 1.00 5.94 ? 12 LYS B NZ 1 ATOM 1580 N N . HIS B 2 15 ? 45.554 22.730 -9.418 1.00 4.38 ? 13 HIS B N 1 ATOM 1581 C CA . HIS B 2 15 ? 46.367 21.633 -9.905 1.00 4.59 ? 13 HIS B CA 1 ATOM 1582 C C . HIS B 2 15 ? 45.432 20.466 -10.089 1.00 6.67 ? 13 HIS B C 1 ATOM 1583 O O . HIS B 2 15 ? 44.991 19.889 -9.090 1.00 6.86 ? 13 HIS B O 1 ATOM 1584 C CB . HIS B 2 15 ? 47.487 21.256 -8.924 1.00 3.62 ? 13 HIS B CB 1 ATOM 1585 C CG . HIS B 2 15 ? 48.195 22.418 -8.306 1.00 8.24 ? 13 HIS B CG 1 ATOM 1586 N ND1 . HIS B 2 15 ? 49.336 22.973 -8.850 1.00 6.46 ? 13 HIS B ND1 1 ATOM 1587 C CD2 . HIS B 2 15 ? 47.919 23.139 -7.192 1.00 9.82 ? 13 HIS B CD2 1 ATOM 1588 C CE1 . HIS B 2 15 ? 49.748 23.966 -8.084 1.00 6.32 ? 13 HIS B CE1 1 ATOM 1589 N NE2 . HIS B 2 15 ? 48.900 24.093 -7.076 1.00 8.52 ? 13 HIS B NE2 1 ATOM 1590 N N . GLU B 2 16 ? 45.150 20.100 -11.340 1.00 5.61 ? 14 GLU B N 1 ATOM 1591 C CA . GLU B 2 16 ? 44.079 19.152 -11.627 1.00 7.28 ? 14 GLU B CA 1 ATOM 1592 C C . GLU B 2 16 ? 44.610 17.808 -12.127 1.00 15.58 ? 14 GLU B C 1 ATOM 1593 O O . GLU B 2 16 ? 45.551 17.748 -12.936 1.00 13.70 ? 14 GLU B O 1 ATOM 1594 C CB . GLU B 2 16 ? 43.094 19.717 -12.657 1.00 11.69 ? 14 GLU B CB 1 ATOM 1595 C CG . GLU B 2 16 ? 42.540 21.103 -12.330 1.00 6.72 ? 14 GLU B CG 1 ATOM 1596 C CD . GLU B 2 16 ? 41.446 21.540 -13.285 1.00 12.72 ? 14 GLU B CD 1 ATOM 1597 O OE1 . GLU B 2 16 ? 41.188 20.830 -14.290 1.00 12.46 ? 14 GLU B OE1 1 ATOM 1598 O OE2 . GLU B 2 16 ? 40.867 22.620 -13.052 1.00 13.04 ? 14 GLU B OE2 1 ATOM 1599 N N . CYS B 2 17 ? 44.016 16.737 -11.614 1.00 12.25 ? 15 CYS B N 1 ATOM 1600 C CA . CYS B 2 17 ? 44.326 15.394 -12.077 1.00 11.68 ? 15 CYS B CA 1 ATOM 1601 C C . CYS B 2 17 ? 43.061 14.776 -12.640 1.00 16.30 ? 15 CYS B C 1 ATOM 1602 O O . CYS B 2 17 ? 42.061 14.611 -11.926 1.00 13.57 ? 15 CYS B O 1 ATOM 1603 C CB . CYS B 2 17 ? 44.874 14.535 -10.940 1.00 9.11 ? 15 CYS B CB 1 ATOM 1604 S SG . CYS B 2 17 ? 46.493 15.076 -10.367 1.00 17.20 ? 15 CYS B SG 1 ATOM 1605 N N . HIS B 2 18 ? 43.111 14.422 -13.919 1.00 15.34 ? 16 HIS B N 1 ATOM 1606 C CA . HIS B 2 18 ? 41.960 13.853 -14.592 1.00 16.90 ? 16 HIS B CA 1 ATOM 1607 C C . HIS B 2 18 ? 42.217 12.390 -14.879 1.00 15.03 ? 16 HIS B C 1 ATOM 1608 O O . HIS B 2 18 ? 43.225 12.044 -15.501 1.00 16.68 ? 16 HIS B O 1 ATOM 1609 C CB . HIS B 2 18 ? 41.664 14.611 -15.891 1.00 17.76 ? 16 HIS B CB 1 ATOM 1610 C CG . HIS B 2 18 ? 41.298 16.049 -15.681 1.00 18.43 ? 16 HIS B CG 1 ATOM 1611 N ND1 . HIS B 2 18 ? 40.022 16.531 -15.882 1.00 22.73 ? 16 HIS B ND1 1 ATOM 1612 C CD2 . HIS B 2 18 ? 42.034 17.103 -15.259 1.00 15.07 ? 16 HIS B CD2 1 ATOM 1613 C CE1 . HIS B 2 18 ? 39.996 17.824 -15.613 1.00 22.21 ? 16 HIS B CE1 1 ATOM 1614 N NE2 . HIS B 2 18 ? 41.204 18.195 -15.235 1.00 14.87 ? 16 HIS B NE2 1 ATOM 1615 N N . PHE B 2 19 ? 41.297 11.540 -14.430 1.00 17.81 ? 17 PHE B N 1 ATOM 1616 C CA . PHE B 2 19 ? 41.489 10.095 -14.503 1.00 18.37 ? 17 PHE B CA 1 ATOM 1617 C C . PHE B 2 19 ? 40.466 9.452 -15.433 1.00 25.70 ? 17 PHE B C 1 ATOM 1618 O O . PHE B 2 19 ? 39.270 9.757 -15.359 1.00 24.88 ? 17 PHE B O 1 ATOM 1619 C CB . PHE B 2 19 ? 41.380 9.452 -13.115 1.00 14.72 ? 17 PHE B CB 1 ATOM 1620 C CG . PHE B 2 19 ? 42.356 9.998 -12.110 1.00 20.45 ? 17 PHE B CG 1 ATOM 1621 C CD1 . PHE B 2 19 ? 42.018 11.092 -11.319 1.00 14.97 ? 17 PHE B CD1 1 ATOM 1622 C CD2 . PHE B 2 19 ? 43.625 9.447 -11.983 1.00 15.51 ? 17 PHE B CD2 1 ATOM 1623 C CE1 . PHE B 2 19 ? 42.915 11.600 -10.394 1.00 15.73 ? 17 PHE B CE1 1 ATOM 1624 C CE2 . PHE B 2 19 ? 44.526 9.955 -11.061 1.00 14.88 ? 17 PHE B CE2 1 ATOM 1625 C CZ . PHE B 2 19 ? 44.172 11.039 -10.269 1.00 12.43 ? 17 PHE B CZ 1 ATOM 1626 N N . PHE B 2 20 ? 40.933 8.551 -16.289 1.00 20.55 ? 18 PHE B N 1 ATOM 1627 C CA . PHE B 2 20 ? 40.055 7.843 -17.214 1.00 30.98 ? 18 PHE B CA 1 ATOM 1628 C C . PHE B 2 20 ? 40.380 6.368 -17.005 1.00 30.42 ? 18 PHE B C 1 ATOM 1629 O O . PHE B 2 20 ? 41.543 5.979 -17.103 1.00 26.18 ? 18 PHE B O 1 ATOM 1630 C CB . PHE B 2 20 ? 40.310 8.238 -18.676 1.00 30.52 ? 18 PHE B CB 1 ATOM 1631 C CG . PHE B 2 20 ? 40.372 9.731 -18.926 1.00 48.83 ? 18 PHE B CG 1 ATOM 1632 C CD1 . PHE B 2 20 ? 41.512 10.464 -18.604 1.00 41.43 ? 18 PHE B CD1 1 ATOM 1633 C CD2 . PHE B 2 20 ? 39.328 10.385 -19.564 1.00 48.80 ? 18 PHE B CD2 1 ATOM 1634 C CE1 . PHE B 2 20 ? 41.581 11.823 -18.853 1.00 31.13 ? 18 PHE B CE1 1 ATOM 1635 C CE2 . PHE B 2 20 ? 39.394 11.751 -19.821 1.00 54.28 ? 18 PHE B CE2 1 ATOM 1636 C CZ . PHE B 2 20 ? 40.524 12.468 -19.462 1.00 37.15 ? 18 PHE B CZ 1 ATOM 1637 N N . ASN B 2 21 ? 39.368 5.557 -16.718 1.00 34.05 ? 19 ASN B N 1 ATOM 1638 C CA . ASN B 2 21 ? 39.558 4.122 -16.518 1.00 29.21 ? 19 ASN B CA 1 ATOM 1639 C C . ASN B 2 21 ? 40.596 3.832 -15.436 1.00 34.45 ? 19 ASN B C 1 ATOM 1640 O O . ASN B 2 21 ? 41.670 3.288 -15.708 1.00 31.22 ? 19 ASN B O 1 ATOM 1641 C CB . ASN B 2 21 ? 39.957 3.455 -17.821 1.00 37.43 ? 19 ASN B CB 1 ATOM 1642 C CG . ASN B 2 21 ? 40.028 1.945 -17.719 1.00 50.10 ? 19 ASN B CG 1 ATOM 1643 O OD1 . ASN B 2 21 ? 39.632 1.329 -16.727 1.00 36.12 ? 19 ASN B OD1 1 ATOM 1644 N ND2 . ASN B 2 21 ? 40.550 1.350 -18.767 1.00 70.51 ? 19 ASN B ND2 1 ATOM 1645 N N . GLY B 2 22 ? 40.291 4.239 -14.215 1.00 32.43 ? 20 GLY B N 1 ATOM 1646 C CA . GLY B 2 22 ? 41.239 4.148 -13.126 1.00 24.73 ? 20 GLY B CA 1 ATOM 1647 C C . GLY B 2 22 ? 42.410 5.084 -13.327 1.00 26.74 ? 20 GLY B C 1 ATOM 1648 O O . GLY B 2 22 ? 42.228 6.272 -13.561 1.00 30.75 ? 20 GLY B O 1 ATOM 1649 N N . THR B 2 23 ? 43.617 4.533 -13.299 1.00 24.33 ? 21 THR B N 1 ATOM 1650 C CA . THR B 2 23 ? 44.822 5.301 -13.573 1.00 26.44 ? 21 THR B CA 1 ATOM 1651 C C . THR B 2 23 ? 45.464 4.873 -14.897 1.00 25.96 ? 21 THR B C 1 ATOM 1652 O O . THR B 2 23 ? 46.644 5.134 -15.144 1.00 26.22 ? 21 THR B O 1 ATOM 1653 C CB . THR B 2 23 ? 45.830 5.163 -12.429 1.00 21.27 ? 21 THR B CB 1 ATOM 1654 O OG1 . THR B 2 23 ? 45.995 3.777 -12.112 1.00 27.44 ? 21 THR B OG1 1 ATOM 1655 C CG2 . THR B 2 23 ? 45.327 5.885 -11.190 1.00 26.35 ? 21 THR B CG2 1 ATOM 1656 N N . GLU B 2 24 ? 44.671 4.217 -15.741 1.00 23.29 ? 22 GLU B N 1 ATOM 1657 C CA . GLU B 2 24 ? 45.145 3.707 -17.021 1.00 32.53 ? 22 GLU B CA 1 ATOM 1658 C C . GLU B 2 24 ? 45.522 4.866 -17.923 1.00 28.44 ? 22 GLU B C 1 ATOM 1659 O O . GLU B 2 24 ? 46.556 4.847 -18.596 1.00 27.11 ? 22 GLU B O 1 ATOM 1660 C CB . GLU B 2 24 ? 44.057 2.851 -17.686 1.00 36.63 ? 22 GLU B CB 1 ATOM 1661 C CG . GLU B 2 24 ? 44.529 1.925 -18.800 1.00 55.82 ? 22 GLU B CG 1 ATOM 1662 C CD . GLU B 2 24 ? 45.429 0.796 -18.318 1.00 65.31 ? 22 GLU B CD 1 ATOM 1663 O OE1 . GLU B 2 24 ? 45.422 0.487 -17.104 1.00 48.04 ? 22 GLU B OE1 1 ATOM 1664 O OE2 . GLU B 2 24 ? 46.144 0.213 -19.166 1.00 63.07 ? 22 GLU B OE2 1 ATOM 1665 N N . ARG B 2 25 ? 44.684 5.893 -17.898 1.00 22.75 ? 23 ARG B N 1 ATOM 1666 C CA . ARG B 2 25 ? 44.927 7.120 -18.633 1.00 22.96 ? 23 ARG B CA 1 ATOM 1667 C C . ARG B 2 25 ? 44.777 8.298 -17.664 1.00 26.04 ? 23 ARG B C 1 ATOM 1668 O O . ARG B 2 25 ? 43.754 8.441 -17.000 1.00 18.72 ? 23 ARG B O 1 ATOM 1669 C CB . ARG B 2 25 ? 43.960 7.217 -19.821 1.00 28.38 ? 23 ARG B CB 1 ATOM 1670 C CG . ARG B 2 25 ? 43.738 8.617 -20.375 1.00 47.53 ? 23 ARG B CG 1 ATOM 1671 C CD . ARG B 2 25 ? 45.008 9.297 -20.886 1.00 59.95 ? 23 ARG B CD 1 ATOM 1672 N NE . ARG B 2 25 ? 44.707 10.595 -21.501 1.00 69.80 ? 23 ARG B NE 1 ATOM 1673 C CZ . ARG B 2 25 ? 45.580 11.595 -21.630 1.00 52.89 ? 23 ARG B CZ 1 ATOM 1674 N NH1 . ARG B 2 25 ? 46.829 11.461 -21.184 1.00 36.83 ? 23 ARG B NH1 1 ATOM 1675 N NH2 . ARG B 2 25 ? 45.203 12.734 -22.207 1.00 29.32 ? 23 ARG B NH2 1 ATOM 1676 N N . VAL B 2 26 ? 45.801 9.144 -17.587 1.00 17.57 ? 24 VAL B N 1 ATOM 1677 C CA . VAL B 2 26 ? 45.793 10.256 -16.640 1.00 23.14 ? 24 VAL B CA 1 ATOM 1678 C C . VAL B 2 26 ? 46.263 11.556 -17.299 1.00 22.52 ? 24 VAL B C 1 ATOM 1679 O O . VAL B 2 26 ? 47.226 11.554 -18.060 1.00 22.73 ? 24 VAL B O 1 ATOM 1680 C CB . VAL B 2 26 ? 46.683 9.960 -15.397 1.00 19.95 ? 24 VAL B CB 1 ATOM 1681 C CG1 . VAL B 2 26 ? 46.641 11.122 -14.410 1.00 14.20 ? 24 VAL B CG1 1 ATOM 1682 C CG2 . VAL B 2 26 ? 46.246 8.670 -14.705 1.00 19.15 ? 24 VAL B CG2 1 ATOM 1683 N N . ARG B 2 27 ? 45.579 12.658 -17.002 1.00 21.16 ? 25 ARG B N 1 ATOM 1684 C CA . ARG B 2 27 ? 45.971 13.984 -17.481 1.00 12.28 ? 25 ARG B CA 1 ATOM 1685 C C . ARG B 2 27 ? 46.144 14.971 -16.327 1.00 16.47 ? 25 ARG B C 1 ATOM 1686 O O . ARG B 2 27 ? 45.294 15.059 -15.439 1.00 15.31 ? 25 ARG B O 1 ATOM 1687 C CB . ARG B 2 27 ? 44.930 14.534 -18.443 1.00 19.15 ? 25 ARG B CB 1 ATOM 1688 C CG . ARG B 2 27 ? 45.291 15.876 -19.046 1.00 16.67 ? 25 ARG B CG 1 ATOM 1689 C CD . ARG B 2 27 ? 44.323 16.218 -20.168 1.00 14.96 ? 25 ARG B CD 1 ATOM 1690 N NE . ARG B 2 27 ? 44.508 17.581 -20.639 1.00 24.49 ? 25 ARG B NE 1 ATOM 1691 C CZ . ARG B 2 27 ? 43.787 18.141 -21.602 1.00 33.58 ? 25 ARG B CZ 1 ATOM 1692 N NH1 . ARG B 2 27 ? 42.823 17.452 -22.195 1.00 41.83 ? 25 ARG B NH1 1 ATOM 1693 N NH2 . ARG B 2 27 ? 44.024 19.394 -21.966 1.00 27.90 ? 25 ARG B NH2 1 ATOM 1694 N N . PHE B 2 28 ? 47.228 15.736 -16.364 1.00 9.72 ? 26 PHE B N 1 ATOM 1695 C CA . PHE B 2 28 ? 47.549 16.697 -15.316 1.00 8.36 ? 26 PHE B CA 1 ATOM 1696 C C . PHE B 2 28 ? 47.515 18.126 -15.859 1.00 12.58 ? 26 PHE B C 1 ATOM 1697 O O . PHE B 2 28 ? 48.065 18.412 -16.927 1.00 13.05 ? 26 PHE B O 1 ATOM 1698 C CB . PHE B 2 28 ? 48.915 16.393 -14.689 1.00 10.75 ? 26 PHE B CB 1 ATOM 1699 C CG . PHE B 2 28 ? 49.457 17.519 -13.851 1.00 13.03 ? 26 PHE B CG 1 ATOM 1700 C CD1 . PHE B 2 28 ? 48.865 17.848 -12.639 1.00 10.90 ? 26 PHE B CD1 1 ATOM 1701 C CD2 . PHE B 2 28 ? 50.533 18.269 -14.289 1.00 11.27 ? 26 PHE B CD2 1 ATOM 1702 C CE1 . PHE B 2 28 ? 49.362 18.893 -11.868 1.00 11.05 ? 26 PHE B CE1 1 ATOM 1703 C CE2 . PHE B 2 28 ? 51.037 19.326 -13.518 1.00 13.90 ? 26 PHE B CE2 1 ATOM 1704 C CZ . PHE B 2 28 ? 50.449 19.636 -12.310 1.00 8.23 ? 26 PHE B CZ 1 ATOM 1705 N N . LEU B 2 29 ? 46.834 19.014 -15.148 1.00 14.00 ? 27 LEU B N 1 ATOM 1706 C CA . LEU B 2 29 ? 46.788 20.439 -15.509 1.00 8.56 ? 27 LEU B CA 1 ATOM 1707 C C . LEU B 2 29 ? 47.269 21.329 -14.364 1.00 8.64 ? 27 LEU B C 1 ATOM 1708 O O . LEU B 2 29 ? 46.824 21.157 -13.226 1.00 6.87 ? 27 LEU B O 1 ATOM 1709 C CB . LEU B 2 29 ? 45.373 20.854 -15.913 1.00 8.68 ? 27 LEU B CB 1 ATOM 1710 C CG . LEU B 2 29 ? 44.717 20.166 -17.114 1.00 13.67 ? 27 LEU B CG 1 ATOM 1711 C CD1 . LEU B 2 29 ? 43.342 20.765 -17.347 1.00 23.06 ? 27 LEU B CD1 1 ATOM 1712 C CD2 . LEU B 2 29 ? 45.572 20.290 -18.359 1.00 25.41 ? 27 LEU B CD2 1 ATOM 1713 N N . ASP B 2 30 ? 48.253 22.191 -14.627 1.00 10.67 ? 28 ASP B N 1 ATOM 1714 C CA . ASP B 2 30 ? 48.725 23.133 -13.608 1.00 5.30 ? 28 ASP B CA 1 ATOM 1715 C C . ASP B 2 30 ? 48.151 24.496 -14.088 1.00 7.42 ? 28 ASP B C 1 ATOM 1716 O O . ASP B 2 30 ? 48.672 25.071 -15.056 1.00 8.31 ? 28 ASP B O 1 ATOM 1717 C CB . ASP B 2 30 ? 50.265 23.147 -13.569 1.00 9.47 ? 28 ASP B CB 1 ATOM 1718 C CG . ASP B 2 30 ? 50.844 23.436 -12.173 1.00 12.48 ? 28 ASP B CG 1 ATOM 1719 O OD1 . ASP B 2 30 ? 50.307 22.903 -11.173 1.00 14.26 ? 28 ASP B OD1 1 ATOM 1720 O OD2 . ASP B 2 30 ? 51.819 24.205 -12.064 1.00 7.92 ? 28 ASP B OD2 1 ATOM 1721 N N . ARG B 2 31 ? 47.147 25.053 -13.405 1.00 4.03 ? 29 ARG B N 1 ATOM 1722 C CA . ARG B 2 31 ? 46.359 26.192 -13.947 1.00 6.25 ? 29 ARG B CA 1 ATOM 1723 C C . ARG B 2 31 ? 46.464 27.412 -13.026 1.00 6.48 ? 29 ARG B C 1 ATOM 1724 O O . ARG B 2 31 ? 46.260 27.292 -11.814 1.00 6.55 ? 29 ARG B O 1 ATOM 1725 C CB . ARG B 2 31 ? 44.886 25.800 -14.131 1.00 4.18 ? 29 ARG B CB 1 ATOM 1726 C CG . ARG B 2 31 ? 44.679 24.483 -14.859 1.00 6.93 ? 29 ARG B CG 1 ATOM 1727 C CD . ARG B 2 31 ? 43.195 24.109 -14.925 1.00 6.53 ? 29 ARG B CD 1 ATOM 1728 N NE . ARG B 2 31 ? 42.441 24.996 -15.805 1.00 7.22 ? 29 ARG B NE 1 ATOM 1729 C CZ . ARG B 2 31 ? 41.116 25.003 -15.892 1.00 7.08 ? 29 ARG B CZ 1 ATOM 1730 N NH1 . ARG B 2 31 ? 40.393 24.177 -15.142 1.00 7.45 ? 29 ARG B NH1 1 ATOM 1731 N NH2 . ARG B 2 31 ? 40.515 25.834 -16.724 1.00 4.89 ? 29 ARG B NH2 1 ATOM 1732 N N . TYR B 2 32 ? 46.754 28.584 -13.600 1.00 6.53 ? 30 TYR B N 1 ATOM 1733 C CA . TYR B 2 32 ? 46.893 29.799 -12.799 1.00 3.69 ? 30 TYR B CA 1 ATOM 1734 C C . TYR B 2 32 ? 45.846 30.850 -13.189 1.00 7.87 ? 30 TYR B C 1 ATOM 1735 O O . TYR B 2 32 ? 45.626 31.077 -14.377 1.00 5.63 ? 30 TYR B O 1 ATOM 1736 C CB . TYR B 2 32 ? 48.322 30.341 -12.987 1.00 8.72 ? 30 TYR B CB 1 ATOM 1737 C CG . TYR B 2 32 ? 49.322 29.430 -12.292 1.00 9.89 ? 30 TYR B CG 1 ATOM 1738 C CD1 . TYR B 2 32 ? 49.648 28.206 -12.880 1.00 10.09 ? 30 TYR B CD1 1 ATOM 1739 C CD2 . TYR B 2 32 ? 49.848 29.707 -11.035 1.00 7.29 ? 30 TYR B CD2 1 ATOM 1740 C CE1 . TYR B 2 32 ? 50.510 27.306 -12.281 1.00 7.91 ? 30 TYR B CE1 1 ATOM 1741 C CE2 . TYR B 2 32 ? 50.732 28.791 -10.415 1.00 12.03 ? 30 TYR B CE2 1 ATOM 1742 C CZ . TYR B 2 32 ? 51.047 27.596 -11.058 1.00 9.40 ? 30 TYR B CZ 1 ATOM 1743 O OH . TYR B 2 32 ? 51.889 26.659 -10.509 1.00 14.50 ? 30 TYR B OH 1 ATOM 1744 N N . PHE B 2 33 ? 45.235 31.521 -12.211 1.00 6.20 ? 31 PHE B N 1 ATOM 1745 C CA . PHE B 2 33 ? 44.128 32.440 -12.493 1.00 5.52 ? 31 PHE B CA 1 ATOM 1746 C C . PHE B 2 33 ? 44.305 33.818 -11.832 1.00 8.27 ? 31 PHE B C 1 ATOM 1747 O O . PHE B 2 33 ? 44.771 33.928 -10.687 1.00 8.60 ? 31 PHE B O 1 ATOM 1748 C CB . PHE B 2 33 ? 42.802 31.835 -12.001 1.00 8.36 ? 31 PHE B CB 1 ATOM 1749 C CG . PHE B 2 33 ? 42.534 30.435 -12.496 1.00 7.74 ? 31 PHE B CG 1 ATOM 1750 C CD1 . PHE B 2 33 ? 43.129 29.338 -11.874 1.00 4.04 ? 31 PHE B CD1 1 ATOM 1751 C CD2 . PHE B 2 33 ? 41.655 30.211 -13.544 1.00 8.68 ? 31 PHE B CD2 1 ATOM 1752 C CE1 . PHE B 2 33 ? 42.871 28.048 -12.309 1.00 5.63 ? 31 PHE B CE1 1 ATOM 1753 C CE2 . PHE B 2 33 ? 41.397 28.923 -13.991 1.00 8.46 ? 31 PHE B CE2 1 ATOM 1754 C CZ . PHE B 2 33 ? 42.006 27.836 -13.374 1.00 4.78 ? 31 PHE B CZ 1 ATOM 1755 N N . TYR B 2 34 ? 43.917 34.864 -12.553 1.00 4.94 ? 32 TYR B N 1 ATOM 1756 C CA . TYR B 2 34 ? 43.804 36.205 -11.986 1.00 7.14 ? 32 TYR B CA 1 ATOM 1757 C C . TYR B 2 34 ? 42.325 36.606 -12.037 1.00 8.72 ? 32 TYR B C 1 ATOM 1758 O O . TYR B 2 34 ? 41.761 36.720 -13.126 1.00 9.20 ? 32 TYR B O 1 ATOM 1759 C CB . TYR B 2 34 ? 44.680 37.206 -12.763 1.00 4.83 ? 32 TYR B CB 1 ATOM 1760 C CG . TYR B 2 34 ? 44.627 38.622 -12.230 1.00 6.48 ? 32 TYR B CG 1 ATOM 1761 C CD1 . TYR B 2 34 ? 45.115 38.925 -10.962 1.00 6.72 ? 32 TYR B CD1 1 ATOM 1762 C CD2 . TYR B 2 34 ? 44.064 39.645 -12.973 1.00 6.14 ? 32 TYR B CD2 1 ATOM 1763 C CE1 . TYR B 2 34 ? 45.063 40.213 -10.462 1.00 7.57 ? 32 TYR B CE1 1 ATOM 1764 C CE2 . TYR B 2 34 ? 44.007 40.946 -12.478 1.00 9.90 ? 32 TYR B CE2 1 ATOM 1765 C CZ . TYR B 2 34 ? 44.509 41.222 -11.222 1.00 10.72 ? 32 TYR B CZ 1 ATOM 1766 O OH . TYR B 2 34 ? 44.452 42.502 -10.725 1.00 11.07 ? 32 TYR B OH 1 ATOM 1767 N N . HIS B 2 35 ? 41.702 36.796 -10.873 1.00 8.43 ? 33 HIS B N 1 ATOM 1768 C CA . HIS B 2 35 ? 40.232 36.859 -10.741 1.00 9.18 ? 33 HIS B CA 1 ATOM 1769 C C . HIS B 2 35 ? 39.640 35.530 -11.254 1.00 9.84 ? 33 HIS B C 1 ATOM 1770 O O . HIS B 2 35 ? 39.904 34.491 -10.653 1.00 12.73 ? 33 HIS B O 1 ATOM 1771 C CB . HIS B 2 35 ? 39.624 38.076 -11.452 1.00 11.05 ? 33 HIS B CB 1 ATOM 1772 C CG . HIS B 2 35 ? 40.294 39.371 -11.106 1.00 13.49 ? 33 HIS B CG 1 ATOM 1773 N ND1 . HIS B 2 35 ? 40.922 39.586 -9.897 1.00 14.19 ? 33 HIS B ND1 1 ATOM 1774 C CD2 . HIS B 2 35 ? 40.436 40.520 -11.809 1.00 14.77 ? 33 HIS B CD2 1 ATOM 1775 C CE1 . HIS B 2 35 ? 41.437 40.804 -9.875 1.00 10.28 ? 33 HIS B CE1 1 ATOM 1776 N NE2 . HIS B 2 35 ? 41.147 41.396 -11.019 1.00 14.58 ? 33 HIS B NE2 1 ATOM 1777 N N . GLN B 2 36 ? 38.874 35.551 -12.352 1.00 9.80 ? 34 GLN B N 1 ATOM 1778 C CA . GLN B 2 36 ? 38.333 34.317 -12.971 1.00 7.56 ? 34 GLN B CA 1 ATOM 1779 C C . GLN B 2 36 ? 39.070 33.915 -14.242 1.00 10.84 ? 34 GLN B C 1 ATOM 1780 O O . GLN B 2 36 ? 38.755 32.893 -14.851 1.00 23.41 ? 34 GLN B O 1 ATOM 1781 C CB . GLN B 2 36 ? 36.866 34.498 -13.378 1.00 12.07 ? 34 GLN B CB 1 ATOM 1782 C CG . GLN B 2 36 ? 35.864 34.685 -12.264 1.00 19.87 ? 34 GLN B CG 1 ATOM 1783 C CD . GLN B 2 36 ? 34.840 35.784 -12.598 1.00 35.63 ? 34 GLN B CD 1 ATOM 1784 O OE1 . GLN B 2 36 ? 34.906 36.895 -12.063 1.00 39.09 ? 34 GLN B OE1 1 ATOM 1785 N NE2 . GLN B 2 36 ? 33.901 35.475 -13.501 1.00 22.88 ? 34 GLN B NE2 1 ATOM 1786 N N . GLU B 2 37 ? 40.033 34.728 -14.650 1.00 8.67 ? 35 GLU B N 1 ATOM 1787 C CA . GLU B 2 37 ? 40.750 34.561 -15.911 1.00 10.37 ? 35 GLU B CA 1 ATOM 1788 C C . GLU B 2 37 ? 41.977 33.642 -15.837 1.00 12.39 ? 35 GLU B C 1 ATOM 1789 O O . GLU B 2 37 ? 42.973 33.977 -15.196 1.00 10.31 ? 35 GLU B O 1 ATOM 1790 C CB . GLU B 2 37 ? 41.190 35.945 -16.415 1.00 15.53 ? 35 GLU B CB 1 ATOM 1791 C CG . GLU B 2 37 ? 42.200 35.917 -17.571 1.00 24.12 ? 35 GLU B CG 1 ATOM 1792 C CD . GLU B 2 37 ? 42.819 37.288 -17.875 1.00 28.43 ? 35 GLU B CD 1 ATOM 1793 O OE1 . GLU B 2 37 ? 43.872 37.333 -18.549 1.00 30.05 ? 35 GLU B OE1 1 ATOM 1794 O OE2 . GLU B 2 37 ? 42.258 38.323 -17.457 1.00 36.38 ? 35 GLU B OE2 1 ATOM 1795 N N . GLU B 2 38 ? 41.907 32.476 -16.468 1.00 9.15 ? 36 GLU B N 1 ATOM 1796 C CA . GLU B 2 38 ? 43.096 31.632 -16.570 1.00 9.13 ? 36 GLU B CA 1 ATOM 1797 C C . GLU B 2 38 ? 44.112 32.324 -17.474 1.00 10.87 ? 36 GLU B C 1 ATOM 1798 O O . GLU B 2 38 ? 43.768 32.726 -18.579 1.00 15.13 ? 36 GLU B O 1 ATOM 1799 C CB . GLU B 2 38 ? 42.747 30.252 -17.124 1.00 7.40 ? 36 GLU B CB 1 ATOM 1800 C CG . GLU B 2 38 ? 43.884 29.253 -17.074 1.00 9.06 ? 36 GLU B CG 1 ATOM 1801 C CD . GLU B 2 38 ? 43.461 27.877 -17.584 1.00 17.88 ? 36 GLU B CD 1 ATOM 1802 O OE1 . GLU B 2 38 ? 42.376 27.803 -18.205 1.00 17.78 ? 36 GLU B OE1 1 ATOM 1803 O OE2 . GLU B 2 38 ? 44.220 26.887 -17.399 1.00 8.09 ? 36 GLU B OE2 1 ATOM 1804 N N . TYR B 2 39 ? 45.340 32.517 -17.002 1.00 6.40 ? 37 TYR B N 1 ATOM 1805 C CA . TYR B 2 39 ? 46.335 33.232 -17.804 1.00 6.74 ? 37 TYR B CA 1 ATOM 1806 C C . TYR B 2 39 ? 47.503 32.349 -18.281 1.00 6.53 ? 37 TYR B C 1 ATOM 1807 O O . TYR B 2 39 ? 48.144 32.656 -19.284 1.00 7.88 ? 37 TYR B O 1 ATOM 1808 C CB . TYR B 2 39 ? 46.837 34.474 -17.051 1.00 9.71 ? 37 TYR B CB 1 ATOM 1809 C CG . TYR B 2 39 ? 47.518 34.266 -15.709 1.00 8.95 ? 37 TYR B CG 1 ATOM 1810 C CD1 . TYR B 2 39 ? 48.881 34.042 -15.622 1.00 8.37 ? 37 TYR B CD1 1 ATOM 1811 C CD2 . TYR B 2 39 ? 46.779 34.290 -14.527 1.00 6.51 ? 37 TYR B CD2 1 ATOM 1812 C CE1 . TYR B 2 39 ? 49.499 33.872 -14.398 1.00 4.95 ? 37 TYR B CE1 1 ATOM 1813 C CE2 . TYR B 2 39 ? 47.383 34.112 -13.303 1.00 6.80 ? 37 TYR B CE2 1 ATOM 1814 C CZ . TYR B 2 39 ? 48.748 33.910 -13.249 1.00 7.40 ? 37 TYR B CZ 1 ATOM 1815 O OH . TYR B 2 39 ? 49.360 33.741 -12.036 1.00 8.83 ? 37 TYR B OH 1 ATOM 1816 N N . VAL B 2 40 ? 47.773 31.246 -17.595 1.00 6.60 ? 38 VAL B N 1 ATOM 1817 C CA . VAL B 2 40 ? 48.827 30.345 -18.050 1.00 5.88 ? 38 VAL B CA 1 ATOM 1818 C C . VAL B 2 40 ? 48.551 28.931 -17.531 1.00 9.39 ? 38 VAL B C 1 ATOM 1819 O O . VAL B 2 40 ? 47.940 28.780 -16.473 1.00 8.49 ? 38 VAL B O 1 ATOM 1820 C CB . VAL B 2 40 ? 50.216 30.828 -17.586 1.00 6.86 ? 38 VAL B CB 1 ATOM 1821 C CG1 . VAL B 2 40 ? 50.323 30.734 -16.091 1.00 3.32 ? 38 VAL B CG1 1 ATOM 1822 C CG2 . VAL B 2 40 ? 51.305 30.011 -18.257 1.00 6.78 ? 38 VAL B CG2 1 ATOM 1823 N N . ARG B 2 41 ? 48.961 27.898 -18.268 1.00 6.15 ? 39 ARG B N 1 ATOM 1824 C CA . ARG B 2 41 ? 48.693 26.531 -17.810 1.00 10.33 ? 39 ARG B CA 1 ATOM 1825 C C . ARG B 2 41 ? 49.755 25.558 -18.307 1.00 12.23 ? 39 ARG B C 1 ATOM 1826 O O . ARG B 2 41 ? 50.334 25.741 -19.382 1.00 13.42 ? 39 ARG B O 1 ATOM 1827 C CB . ARG B 2 41 ? 47.332 26.030 -18.285 1.00 11.03 ? 39 ARG B CB 1 ATOM 1828 C CG . ARG B 2 41 ? 47.269 25.851 -19.781 1.00 24.61 ? 39 ARG B CG 1 ATOM 1829 C CD . ARG B 2 41 ? 46.193 24.853 -20.222 1.00 12.32 ? 39 ARG B CD 1 ATOM 1830 N NE . ARG B 2 41 ? 44.878 25.291 -19.783 1.00 10.13 ? 39 ARG B NE 1 ATOM 1831 C CZ . ARG B 2 41 ? 43.744 24.734 -20.175 1.00 19.75 ? 39 ARG B CZ 1 ATOM 1832 N NH1 . ARG B 2 41 ? 43.770 23.701 -21.010 1.00 16.54 ? 39 ARG B NH1 1 ATOM 1833 N NH2 . ARG B 2 41 ? 42.588 25.205 -19.733 1.00 16.72 ? 39 ARG B NH2 1 ATOM 1834 N N . PHE B 2 42 ? 50.020 24.539 -17.503 1.00 7.58 ? 40 PHE B N 1 ATOM 1835 C CA . PHE B 2 42 ? 50.769 23.382 -17.959 1.00 9.86 ? 40 PHE B CA 1 ATOM 1836 C C . PHE B 2 42 ? 49.770 22.238 -18.189 1.00 10.37 ? 40 PHE B C 1 ATOM 1837 O O . PHE B 2 42 ? 49.001 21.882 -17.292 1.00 8.97 ? 40 PHE B O 1 ATOM 1838 C CB . PHE B 2 42 ? 51.833 23.000 -16.918 1.00 9.20 ? 40 PHE B CB 1 ATOM 1839 C CG . PHE B 2 42 ? 52.601 21.751 -17.245 1.00 11.40 ? 40 PHE B CG 1 ATOM 1840 C CD1 . PHE B 2 42 ? 53.876 21.841 -17.806 1.00 11.55 ? 40 PHE B CD1 1 ATOM 1841 C CD2 . PHE B 2 42 ? 52.073 20.491 -16.971 1.00 10.80 ? 40 PHE B CD2 1 ATOM 1842 C CE1 . PHE B 2 42 ? 54.594 20.696 -18.109 1.00 13.38 ? 40 PHE B CE1 1 ATOM 1843 C CE2 . PHE B 2 42 ? 52.782 19.344 -17.270 1.00 10.21 ? 40 PHE B CE2 1 ATOM 1844 C CZ . PHE B 2 42 ? 54.049 19.444 -17.837 1.00 11.22 ? 40 PHE B CZ 1 ATOM 1845 N N . ASP B 2 43 ? 49.774 21.690 -19.399 1.00 9.14 ? 41 ASP B N 1 ATOM 1846 C CA . ASP B 2 43 ? 48.949 20.534 -19.767 1.00 10.73 ? 41 ASP B CA 1 ATOM 1847 C C . ASP B 2 43 ? 49.907 19.358 -20.015 1.00 11.30 ? 41 ASP B C 1 ATOM 1848 O O . ASP B 2 43 ? 50.802 19.458 -20.864 1.00 8.53 ? 41 ASP B O 1 ATOM 1849 C CB . ASP B 2 43 ? 48.112 20.866 -21.017 1.00 16.75 ? 41 ASP B CB 1 ATOM 1850 C CG . ASP B 2 43 ? 47.106 19.773 -21.413 1.00 17.04 ? 41 ASP B CG 1 ATOM 1851 O OD1 . ASP B 2 43 ? 47.179 18.598 -20.969 1.00 9.63 ? 41 ASP B OD1 1 ATOM 1852 O OD2 . ASP B 2 43 ? 46.227 20.123 -22.230 1.00 16.71 ? 41 ASP B OD2 1 ATOM 1853 N N . SER B 2 44 ? 49.708 18.244 -19.313 1.00 8.18 ? 42 SER B N 1 ATOM 1854 C CA . SER B 2 44 ? 50.585 17.075 -19.467 1.00 10.68 ? 42 SER B CA 1 ATOM 1855 C C . SER B 2 44 ? 50.539 16.527 -20.891 1.00 12.12 ? 42 SER B C 1 ATOM 1856 O O . SER B 2 44 ? 51.443 15.816 -21.304 1.00 11.60 ? 42 SER B O 1 ATOM 1857 C CB . SER B 2 44 ? 50.216 15.964 -18.475 1.00 10.37 ? 42 SER B CB 1 ATOM 1858 O OG . SER B 2 44 ? 48.903 15.479 -18.724 1.00 10.84 ? 42 SER B OG 1 ATOM 1859 N N . ASP B 2 45 ? 49.477 16.849 -21.634 1.00 13.46 ? 43 ASP B N 1 ATOM 1860 C CA . ASP B 2 45 ? 49.382 16.481 -23.049 1.00 14.65 ? 43 ASP B CA 1 ATOM 1861 C C . ASP B 2 45 ? 50.442 17.192 -23.900 1.00 14.48 ? 43 ASP B C 1 ATOM 1862 O O . ASP B 2 45 ? 50.829 16.714 -24.971 1.00 13.59 ? 43 ASP B O 1 ATOM 1863 C CB . ASP B 2 45 ? 47.997 16.838 -23.597 1.00 21.13 ? 43 ASP B CB 1 ATOM 1864 C CG . ASP B 2 45 ? 46.939 15.826 -23.230 1.00 24.96 ? 43 ASP B CG 1 ATOM 1865 O OD1 . ASP B 2 45 ? 47.231 14.891 -22.445 1.00 21.10 ? 43 ASP B OD1 1 ATOM 1866 O OD2 . ASP B 2 45 ? 45.803 15.980 -23.728 1.00 27.84 ? 43 ASP B OD2 1 ATOM 1867 N N . VAL B 2 46 ? 50.905 18.336 -23.406 1.00 10.02 ? 44 VAL B N 1 ATOM 1868 C CA . VAL B 2 46 ? 51.857 19.176 -24.124 1.00 14.57 ? 44 VAL B CA 1 ATOM 1869 C C . VAL B 2 46 ? 53.257 19.052 -23.519 1.00 15.56 ? 44 VAL B C 1 ATOM 1870 O O . VAL B 2 46 ? 54.232 18.820 -24.241 1.00 16.54 ? 44 VAL B O 1 ATOM 1871 C CB . VAL B 2 46 ? 51.407 20.666 -24.136 1.00 9.84 ? 44 VAL B CB 1 ATOM 1872 C CG1 . VAL B 2 46 ? 52.479 21.552 -24.749 1.00 13.34 ? 44 VAL B CG1 1 ATOM 1873 C CG2 . VAL B 2 46 ? 50.108 20.814 -24.897 1.00 9.79 ? 44 VAL B CG2 1 ATOM 1874 N N . GLY B 2 47 ? 53.369 19.221 -22.202 1.00 13.93 ? 45 GLY B N 1 ATOM 1875 C CA . GLY B 2 47 ? 54.656 19.018 -21.554 1.00 12.17 ? 45 GLY B CA 1 ATOM 1876 C C . GLY B 2 47 ? 55.403 20.326 -21.367 1.00 13.26 ? 45 GLY B C 1 ATOM 1877 O O . GLY B 2 47 ? 56.591 20.346 -21.018 1.00 14.82 ? 45 GLY B O 1 ATOM 1878 N N . GLU B 2 48 ? 54.703 21.422 -21.638 1.00 11.90 ? 46 GLU B N 1 ATOM 1879 C CA . GLU B 2 48 ? 55.223 22.755 -21.414 1.00 9.74 ? 46 GLU B CA 1 ATOM 1880 C C . GLU B 2 48 ? 54.094 23.664 -20.988 1.00 14.03 ? 46 GLU B C 1 ATOM 1881 O O . GLU B 2 48 ? 52.922 23.334 -21.176 1.00 9.38 ? 46 GLU B O 1 ATOM 1882 C CB . GLU B 2 48 ? 55.842 23.317 -22.698 1.00 13.51 ? 46 GLU B CB 1 ATOM 1883 C CG . GLU B 2 48 ? 57.210 22.773 -23.068 1.00 28.89 ? 46 GLU B CG 1 ATOM 1884 C CD . GLU B 2 48 ? 57.797 23.437 -24.322 1.00 30.45 ? 46 GLU B CD 1 ATOM 1885 O OE1 . GLU B 2 48 ? 57.070 24.202 -24.996 1.00 17.56 ? 46 GLU B OE1 1 ATOM 1886 O OE2 . GLU B 2 48 ? 58.995 23.202 -24.613 1.00 34.86 ? 46 GLU B OE2 1 ATOM 1887 N N . TYR B 2 49 ? 54.453 24.795 -20.389 1.00 11.35 ? 47 TYR B N 1 ATOM 1888 C CA . TYR B 2 49 ? 53.498 25.846 -20.082 1.00 10.29 ? 47 TYR B CA 1 ATOM 1889 C C . TYR B 2 49 ? 53.134 26.574 -21.376 1.00 12.10 ? 47 TYR B C 1 ATOM 1890 O O . TYR B 2 49 ? 53.965 26.682 -22.286 1.00 11.00 ? 47 TYR B O 1 ATOM 1891 C CB . TYR B 2 49 ? 54.042 26.812 -19.028 1.00 7.81 ? 47 TYR B CB 1 ATOM 1892 C CG . TYR B 2 49 ? 53.978 26.255 -17.621 1.00 11.92 ? 47 TYR B CG 1 ATOM 1893 C CD1 . TYR B 2 49 ? 55.043 25.541 -17.087 1.00 8.66 ? 47 TYR B CD1 1 ATOM 1894 C CD2 . TYR B 2 49 ? 52.832 26.418 -16.836 1.00 9.31 ? 47 TYR B CD2 1 ATOM 1895 C CE1 . TYR B 2 49 ? 54.989 25.027 -15.801 1.00 11.07 ? 47 TYR B CE1 1 ATOM 1896 C CE2 . TYR B 2 49 ? 52.765 25.910 -15.550 1.00 6.72 ? 47 TYR B CE2 1 ATOM 1897 C CZ . TYR B 2 49 ? 53.841 25.209 -15.039 1.00 13.48 ? 47 TYR B CZ 1 ATOM 1898 O OH . TYR B 2 49 ? 53.787 24.691 -13.765 1.00 8.80 ? 47 TYR B OH 1 ATOM 1899 N N . ARG B 2 50 ? 51.880 27.010 -21.472 1.00 5.39 ? 48 ARG B N 1 ATOM 1900 C CA . ARG B 2 50 ? 51.397 27.827 -22.586 1.00 10.39 ? 48 ARG B CA 1 ATOM 1901 C C . ARG B 2 50 ? 50.583 29.006 -22.039 1.00 9.22 ? 48 ARG B C 1 ATOM 1902 O O . ARG B 2 50 ? 49.767 28.831 -21.126 1.00 16.36 ? 48 ARG B O 1 ATOM 1903 C CB . ARG B 2 50 ? 50.524 26.996 -23.544 1.00 7.21 ? 48 ARG B CB 1 ATOM 1904 C CG . ARG B 2 50 ? 51.251 25.869 -24.277 1.00 20.27 ? 48 ARG B CG 1 ATOM 1905 C CD . ARG B 2 50 ? 52.148 26.376 -25.391 1.00 17.27 ? 48 ARG B CD 1 ATOM 1906 N NE . ARG B 2 50 ? 52.813 25.289 -26.120 1.00 18.57 ? 48 ARG B NE 1 ATOM 1907 C CZ . ARG B 2 50 ? 54.097 24.961 -25.940 1.00 28.17 ? 48 ARG B CZ 1 ATOM 1908 N NH1 . ARG B 2 50 ? 54.827 25.620 -25.052 1.00 23.04 ? 48 ARG B NH1 1 ATOM 1909 N NH2 . ARG B 2 50 ? 54.656 23.967 -26.622 1.00 30.52 ? 48 ARG B NH2 1 ATOM 1910 N N . ALA B 2 51 ? 50.804 30.201 -22.567 1.00 4.14 ? 49 ALA B N 1 ATOM 1911 C CA . ALA B 2 51 ? 50.003 31.355 -22.155 1.00 10.31 ? 49 ALA B CA 1 ATOM 1912 C C . ALA B 2 51 ? 48.564 31.153 -22.627 1.00 9.11 ? 49 ALA B C 1 ATOM 1913 O O . ALA B 2 51 ? 48.336 30.779 -23.779 1.00 11.64 ? 49 ALA B O 1 ATOM 1914 C CB . ALA B 2 51 ? 50.586 32.649 -22.722 1.00 6.73 ? 49 ALA B CB 1 ATOM 1915 N N . VAL B 2 52 ? 47.591 31.413 -21.762 1.00 10.53 ? 50 VAL B N 1 ATOM 1916 C CA . VAL B 2 52 ? 46.182 31.329 -22.166 1.00 6.75 ? 50 VAL B CA 1 ATOM 1917 C C . VAL B 2 52 ? 45.688 32.701 -22.605 1.00 13.64 ? 50 VAL B C 1 ATOM 1918 O O . VAL B 2 52 ? 44.907 32.826 -23.556 1.00 14.59 ? 50 VAL B O 1 ATOM 1919 C CB . VAL B 2 52 ? 45.316 30.767 -21.036 1.00 13.18 ? 50 VAL B CB 1 ATOM 1920 C CG1 . VAL B 2 52 ? 43.821 30.697 -21.462 1.00 11.95 ? 50 VAL B CG1 1 ATOM 1921 C CG2 . VAL B 2 52 ? 45.825 29.379 -20.650 1.00 9.04 ? 50 VAL B CG2 1 ATOM 1922 N N . THR B 2 53 ? 46.199 33.731 -21.934 1.00 12.55 ? 51 THR B N 1 ATOM 1923 C CA . THR B 2 53 ? 45.962 35.108 -22.322 1.00 9.58 ? 51 THR B CA 1 ATOM 1924 C C . THR B 2 53 ? 47.318 35.800 -22.324 1.00 19.11 ? 51 THR B C 1 ATOM 1925 O O . THR B 2 53 ? 48.319 35.223 -21.868 1.00 14.62 ? 51 THR B O 1 ATOM 1926 C CB . THR B 2 53 ? 44.996 35.828 -21.360 1.00 15.50 ? 51 THR B CB 1 ATOM 1927 O OG1 . THR B 2 53 ? 45.614 35.956 -20.075 1.00 15.14 ? 51 THR B OG1 1 ATOM 1928 C CG2 . THR B 2 53 ? 43.684 35.054 -21.209 1.00 10.34 ? 51 THR B CG2 1 ATOM 1929 N N . GLU B 2 54 ? 47.348 37.026 -22.837 1.00 15.05 ? 52 GLU B N 1 ATOM 1930 C CA . GLU B 2 54 ? 48.580 37.806 -22.932 1.00 28.09 ? 52 GLU B CA 1 ATOM 1931 C C . GLU B 2 54 ? 49.233 38.010 -21.578 1.00 15.08 ? 52 GLU B C 1 ATOM 1932 O O . GLU B 2 54 ? 50.454 38.033 -21.460 1.00 14.58 ? 52 GLU B O 1 ATOM 1933 C CB . GLU B 2 54 ? 48.296 39.160 -23.580 1.00 31.11 ? 52 GLU B CB 1 ATOM 1934 C CG . GLU B 2 54 ? 47.669 39.059 -24.961 1.00 48.79 ? 52 GLU B CG 1 ATOM 1935 C CD . GLU B 2 54 ? 47.632 40.395 -25.687 1.00 79.95 ? 52 GLU B CD 1 ATOM 1936 O OE1 . GLU B 2 54 ? 47.843 41.440 -25.031 1.00 75.32 ? 52 GLU B OE1 1 ATOM 1937 O OE2 . GLU B 2 54 ? 47.377 40.403 -26.911 1.00 81.98 ? 52 GLU B OE2 1 ATOM 1938 N N . LEU B 2 55 ? 48.390 38.104 -20.559 1.00 13.78 ? 53 LEU B N 1 ATOM 1939 C CA . LEU B 2 55 ? 48.819 38.293 -19.181 1.00 17.08 ? 53 LEU B CA 1 ATOM 1940 C C . LEU B 2 55 ? 49.777 37.196 -18.698 1.00 13.69 ? 53 LEU B C 1 ATOM 1941 O O . LEU B 2 55 ? 50.583 37.423 -17.807 1.00 13.71 ? 53 LEU B O 1 ATOM 1942 C CB . LEU B 2 55 ? 47.574 38.323 -18.288 1.00 17.84 ? 53 LEU B CB 1 ATOM 1943 C CG . LEU B 2 55 ? 47.461 39.256 -17.093 1.00 22.81 ? 53 LEU B CG 1 ATOM 1944 C CD1 . LEU B 2 55 ? 47.771 40.695 -17.495 1.00 20.43 ? 53 LEU B CD1 1 ATOM 1945 C CD2 . LEU B 2 55 ? 46.070 39.128 -16.496 1.00 23.11 ? 53 LEU B CD2 1 ATOM 1946 N N . GLY B 2 56 ? 49.674 36.005 -19.287 1.00 10.36 ? 54 GLY B N 1 ATOM 1947 C CA . GLY B 2 56 ? 50.470 34.878 -18.843 1.00 10.02 ? 54 GLY B CA 1 ATOM 1948 C C . GLY B 2 56 ? 51.719 34.607 -19.662 1.00 10.11 ? 54 GLY B C 1 ATOM 1949 O O . GLY B 2 56 ? 52.468 33.722 -19.323 1.00 10.91 ? 54 GLY B O 1 ATOM 1950 N N . ARG B 2 57 ? 51.952 35.372 -20.725 1.00 14.00 ? 55 ARG B N 1 ATOM 1951 C CA . ARG B 2 57 ? 53.115 35.143 -21.604 1.00 19.23 ? 55 ARG B CA 1 ATOM 1952 C C . ARG B 2 57 ? 54.465 35.230 -20.873 1.00 14.27 ? 55 ARG B C 1 ATOM 1953 O O . ARG B 2 57 ? 55.335 34.392 -21.106 1.00 15.20 ? 55 ARG B O 1 ATOM 1954 C CB . ARG B 2 57 ? 53.104 36.093 -22.809 1.00 11.47 ? 55 ARG B CB 1 ATOM 1955 C CG . ARG B 2 57 ? 51.967 35.785 -23.771 1.00 22.72 ? 55 ARG B CG 1 ATOM 1956 C CD . ARG B 2 57 ? 51.786 36.813 -24.881 1.00 37.56 ? 55 ARG B CD 1 ATOM 1957 N NE . ARG B 2 57 ? 50.683 36.425 -25.761 1.00 47.50 ? 55 ARG B NE 1 ATOM 1958 C CZ . ARG B 2 57 ? 50.115 37.227 -26.656 1.00 58.13 ? 55 ARG B CZ 1 ATOM 1959 N NH1 . ARG B 2 57 ? 50.521 38.485 -26.775 1.00 67.04 ? 55 ARG B NH1 1 ATOM 1960 N NH2 . ARG B 2 57 ? 49.118 36.782 -27.411 1.00 56.12 ? 55 ARG B NH2 1 ATOM 1961 N N . PRO B 2 58 ? 54.649 36.235 -19.995 1.00 15.41 ? 56 PRO B N 1 ATOM 1962 C CA . PRO B 2 58 ? 55.957 36.266 -19.341 1.00 17.52 ? 56 PRO B CA 1 ATOM 1963 C C . PRO B 2 58 ? 56.215 35.015 -18.492 1.00 14.38 ? 56 PRO B C 1 ATOM 1964 O O . PRO B 2 58 ? 57.337 34.513 -18.467 1.00 12.87 ? 56 PRO B O 1 ATOM 1965 C CB . PRO B 2 58 ? 55.866 37.511 -18.456 1.00 14.67 ? 56 PRO B CB 1 ATOM 1966 C CG . PRO B 2 58 ? 54.879 38.373 -19.115 1.00 18.72 ? 56 PRO B CG 1 ATOM 1967 C CD . PRO B 2 58 ? 53.851 37.431 -19.659 1.00 15.39 ? 56 PRO B CD 1 ATOM 1968 N N . ASP B 2 59 ? 55.190 34.510 -17.816 1.00 17.65 ? 57 ASP B N 1 ATOM 1969 C CA . ASP B 2 59 ? 55.362 33.325 -16.983 1.00 12.81 ? 57 ASP B CA 1 ATOM 1970 C C . ASP B 2 59 ? 55.600 32.070 -17.827 1.00 11.50 ? 57 ASP B C 1 ATOM 1971 O O . ASP B 2 59 ? 56.431 31.246 -17.475 1.00 10.84 ? 57 ASP B O 1 ATOM 1972 C CB . ASP B 2 59 ? 54.163 33.132 -16.062 1.00 14.23 ? 57 ASP B CB 1 ATOM 1973 C CG . ASP B 2 59 ? 54.076 34.198 -14.988 1.00 22.16 ? 57 ASP B CG 1 ATOM 1974 O OD1 . ASP B 2 59 ? 55.137 34.692 -14.556 1.00 17.46 ? 57 ASP B OD1 1 ATOM 1975 O OD2 . ASP B 2 59 ? 52.945 34.549 -14.581 1.00 22.81 ? 57 ASP B OD2 1 ATOM 1976 N N . ALA B 2 60 ? 54.870 31.918 -18.933 1.00 13.51 ? 58 ALA B N 1 ATOM 1977 C CA . ALA B 2 60 ? 55.081 30.774 -19.829 1.00 14.23 ? 58 ALA B CA 1 ATOM 1978 C C . ALA B 2 60 ? 56.545 30.710 -20.305 1.00 16.15 ? 58 ALA B C 1 ATOM 1979 O O . ALA B 2 60 ? 57.170 29.648 -20.285 1.00 16.14 ? 58 ALA B O 1 ATOM 1980 C CB . ALA B 2 60 ? 54.127 30.828 -21.012 1.00 9.22 ? 58 ALA B CB 1 ATOM 1981 N N . GLU B 2 61 ? 57.094 31.843 -20.733 1.00 20.19 ? 59 GLU B N 1 ATOM 1982 C CA . GLU B 2 61 ? 58.470 31.866 -21.229 1.00 21.34 ? 59 GLU B CA 1 ATOM 1983 C C . GLU B 2 61 ? 59.465 31.625 -20.103 1.00 15.40 ? 59 GLU B C 1 ATOM 1984 O O . GLU B 2 61 ? 60.432 30.883 -20.250 1.00 16.97 ? 59 GLU B O 1 ATOM 1985 C CB . GLU B 2 61 ? 58.789 33.204 -21.884 1.00 16.17 ? 59 GLU B CB 1 ATOM 1986 C CG . GLU B 2 61 ? 57.949 33.525 -23.103 1.00 38.43 ? 59 GLU B CG 1 ATOM 1987 C CD . GLU B 2 61 ? 58.293 34.882 -23.671 1.00 56.82 ? 59 GLU B CD 1 ATOM 1988 O OE1 . GLU B 2 61 ? 59.401 35.383 -23.364 1.00 61.20 ? 59 GLU B OE1 1 ATOM 1989 O OE2 . GLU B 2 61 ? 57.456 35.451 -24.407 1.00 49.05 ? 59 GLU B OE2 1 ATOM 1990 N N . TYR B 2 62 ? 59.194 32.222 -18.956 1.00 16.03 ? 60 TYR B N 1 ATOM 1991 C CA . TYR B 2 62 ? 60.088 32.074 -17.828 1.00 18.53 ? 60 TYR B CA 1 ATOM 1992 C C . TYR B 2 62 ? 60.090 30.650 -17.305 1.00 18.86 ? 60 TYR B C 1 ATOM 1993 O O . TYR B 2 62 ? 61.160 30.053 -17.118 1.00 14.44 ? 60 TYR B O 1 ATOM 1994 C CB . TYR B 2 62 ? 59.674 33.045 -16.724 1.00 18.95 ? 60 TYR B CB 1 ATOM 1995 C CG . TYR B 2 62 ? 60.524 32.975 -15.474 1.00 30.74 ? 60 TYR B CG 1 ATOM 1996 C CD1 . TYR B 2 62 ? 61.913 33.036 -15.549 1.00 25.40 ? 60 TYR B CD1 1 ATOM 1997 C CD2 . TYR B 2 62 ? 59.935 32.864 -14.218 1.00 23.49 ? 60 TYR B CD2 1 ATOM 1998 C CE1 . TYR B 2 62 ? 62.692 32.978 -14.409 1.00 18.50 ? 60 TYR B CE1 1 ATOM 1999 C CE2 . TYR B 2 62 ? 60.699 32.808 -13.078 1.00 26.23 ? 60 TYR B CE2 1 ATOM 2000 C CZ . TYR B 2 62 ? 62.080 32.867 -13.177 1.00 32.64 ? 60 TYR B CZ 1 ATOM 2001 O OH . TYR B 2 62 ? 62.843 32.812 -12.034 1.00 41.08 ? 60 TYR B OH 1 ATOM 2002 N N . TRP B 2 63 ? 58.898 30.091 -17.113 1.00 10.60 ? 61 TRP B N 1 ATOM 2003 C CA . TRP B 2 63 ? 58.773 28.738 -16.572 1.00 12.07 ? 61 TRP B CA 1 ATOM 2004 C C . TRP B 2 63 ? 59.291 27.662 -17.530 1.00 10.76 ? 61 TRP B C 1 ATOM 2005 O O . TRP B 2 63 ? 59.874 26.664 -17.104 1.00 12.14 ? 61 TRP B O 1 ATOM 2006 C CB . TRP B 2 63 ? 57.318 28.472 -16.182 1.00 10.50 ? 61 TRP B CB 1 ATOM 2007 C CG . TRP B 2 63 ? 56.860 29.372 -15.045 1.00 16.91 ? 61 TRP B CG 1 ATOM 2008 C CD1 . TRP B 2 63 ? 57.655 30.177 -14.258 1.00 17.12 ? 61 TRP B CD1 1 ATOM 2009 C CD2 . TRP B 2 63 ? 55.516 29.577 -14.594 1.00 14.75 ? 61 TRP B CD2 1 ATOM 2010 N NE1 . TRP B 2 63 ? 56.883 30.853 -13.341 1.00 17.92 ? 61 TRP B NE1 1 ATOM 2011 C CE2 . TRP B 2 63 ? 55.569 30.504 -13.524 1.00 14.61 ? 61 TRP B CE2 1 ATOM 2012 C CE3 . TRP B 2 63 ? 54.270 29.063 -14.984 1.00 11.87 ? 61 TRP B CE3 1 ATOM 2013 C CZ2 . TRP B 2 63 ? 54.429 30.918 -12.836 1.00 11.75 ? 61 TRP B CZ2 1 ATOM 2014 C CZ3 . TRP B 2 63 ? 53.134 29.483 -14.299 1.00 9.39 ? 61 TRP B CZ3 1 ATOM 2015 C CH2 . TRP B 2 63 ? 53.223 30.400 -13.239 1.00 14.71 ? 61 TRP B CH2 1 ATOM 2016 N N . ASN B 2 64 ? 59.072 27.861 -18.824 1.00 14.34 ? 62 ASN B N 1 ATOM 2017 C CA . ASN B 2 64 ? 59.550 26.904 -19.810 1.00 11.53 ? 62 ASN B CA 1 ATOM 2018 C C . ASN B 2 64 ? 61.077 26.930 -19.925 1.00 17.93 ? 62 ASN B C 1 ATOM 2019 O O . ASN B 2 64 ? 61.673 26.008 -20.488 1.00 16.50 ? 62 ASN B O 1 ATOM 2020 C CB . ASN B 2 64 ? 58.908 27.160 -21.179 1.00 14.48 ? 62 ASN B CB 1 ATOM 2021 C CG . ASN B 2 64 ? 57.436 26.717 -21.239 1.00 13.18 ? 62 ASN B CG 1 ATOM 2022 O OD1 . ASN B 2 64 ? 56.972 25.943 -20.404 1.00 10.59 ? 62 ASN B OD1 1 ATOM 2023 N ND2 . ASN B 2 64 ? 56.721 27.177 -22.257 1.00 13.03 ? 62 ASN B ND2 1 ATOM 2024 N N . SER B 2 65 ? 61.716 27.980 -19.407 1.00 14.35 ? 63 SER B N 1 ATOM 2025 C CA . SER B 2 65 ? 63.179 28.041 -19.454 1.00 13.86 ? 63 SER B CA 1 ATOM 2026 C C . SER B 2 65 ? 63.802 27.269 -18.302 1.00 15.33 ? 63 SER B C 1 ATOM 2027 O O . SER B 2 65 ? 65.021 27.134 -18.243 1.00 21.94 ? 63 SER B O 1 ATOM 2028 C CB . SER B 2 65 ? 63.689 29.480 -19.409 1.00 13.23 ? 63 SER B CB 1 ATOM 2029 O OG . SER B 2 65 ? 63.638 29.990 -18.090 1.00 8.90 ? 63 SER B OG 1 ATOM 2030 N N . GLN B 2 66 ? 62.968 26.777 -17.387 1.00 15.28 ? 64 GLN B N 1 ATOM 2031 C CA . GLN B 2 66 ? 63.437 26.027 -16.219 1.00 15.57 ? 64 GLN B CA 1 ATOM 2032 C C . GLN B 2 66 ? 63.201 24.521 -16.404 1.00 21.69 ? 64 GLN B C 1 ATOM 2033 O O . GLN B 2 66 ? 62.108 23.997 -16.143 1.00 11.99 ? 64 GLN B O 1 ATOM 2034 C CB . GLN B 2 66 ? 62.737 26.507 -14.947 1.00 13.40 ? 64 GLN B CB 1 ATOM 2035 C CG . GLN B 2 66 ? 62.874 27.994 -14.653 1.00 21.38 ? 64 GLN B CG 1 ATOM 2036 C CD . GLN B 2 66 ? 62.063 28.409 -13.431 1.00 25.98 ? 64 GLN B CD 1 ATOM 2037 O OE1 . GLN B 2 66 ? 61.968 27.663 -12.461 1.00 30.37 ? 64 GLN B OE1 1 ATOM 2038 N NE2 . GLN B 2 66 ? 61.438 29.585 -13.494 1.00 21.90 ? 64 GLN B NE2 1 ATOM 2039 N N . LYS B 2 67 ? 64.234 23.833 -16.869 1.00 23.17 ? 65 LYS B N 1 ATOM 2040 C CA . LYS B 2 67 ? 64.144 22.417 -17.188 1.00 22.26 ? 65 LYS B CA 1 ATOM 2041 C C . LYS B 2 67 ? 63.769 21.517 -16.008 1.00 17.30 ? 65 LYS B C 1 ATOM 2042 O O . LYS B 2 67 ? 62.958 20.611 -16.160 1.00 11.76 ? 65 LYS B O 1 ATOM 2043 C CB . LYS B 2 67 ? 65.505 22.004 -17.750 1.00 18.14 ? 65 LYS B CB 1 ATOM 2044 C CG . LYS B 2 67 ? 66.650 22.166 -16.704 1.00 40.42 ? 65 LYS B CG 1 ATOM 2045 C CD . LYS B 2 67 ? 68.041 22.134 -17.325 1.00 62.22 ? 65 LYS B CD 1 ATOM 2046 C CE . LYS B 2 67 ? 69.150 22.487 -16.337 1.00 64.93 ? 65 LYS B CE 1 ATOM 2047 N NZ . LYS B 2 67 ? 70.482 22.500 -17.018 1.00 29.15 ? 65 LYS B NZ 1 ATOM 2048 N N . ASP B 2 68 ? 64.293 21.835 -14.828 1.00 15.60 ? 66 ASP B N 1 ATOM 2049 C CA . ASP B 2 68 ? 64.009 21.084 -13.612 1.00 19.04 ? 66 ASP B CA 1 ATOM 2050 C C . ASP B 2 68 ? 62.537 21.216 -13.254 1.00 11.88 ? 66 ASP B C 1 ATOM 2051 O O . ASP B 2 68 ? 61.880 20.237 -12.927 1.00 13.13 ? 66 ASP B O 1 ATOM 2052 C CB . ASP B 2 68 ? 64.902 21.551 -12.452 1.00 17.27 ? 66 ASP B CB 1 ATOM 2053 C CG . ASP B 2 68 ? 64.823 23.058 -12.207 1.00 27.47 ? 66 ASP B CG 1 ATOM 2054 O OD1 . ASP B 2 68 ? 64.445 23.814 -13.131 1.00 25.59 ? 66 ASP B OD1 1 ATOM 2055 O OD2 . ASP B 2 68 ? 65.149 23.489 -11.082 1.00 40.09 ? 66 ASP B OD2 1 ATOM 2056 N N . LEU B 2 69 ? 62.019 22.432 -13.381 1.00 13.47 ? 67 LEU B N 1 ATOM 2057 C CA . LEU B 2 69 ? 60.608 22.690 -13.132 1.00 15.21 ? 67 LEU B CA 1 ATOM 2058 C C . LEU B 2 69 ? 59.708 21.914 -14.079 1.00 17.59 ? 67 LEU B C 1 ATOM 2059 O O . LEU B 2 69 ? 58.764 21.248 -13.639 1.00 11.84 ? 67 LEU B O 1 ATOM 2060 C CB . LEU B 2 69 ? 60.317 24.177 -13.258 1.00 15.57 ? 67 LEU B CB 1 ATOM 2061 C CG . LEU B 2 69 ? 58.838 24.564 -13.295 1.00 17.61 ? 67 LEU B CG 1 ATOM 2062 C CD1 . LEU B 2 69 ? 58.167 24.202 -11.974 1.00 11.85 ? 67 LEU B CD1 1 ATOM 2063 C CD2 . LEU B 2 69 ? 58.686 26.054 -13.601 1.00 15.76 ? 67 LEU B CD2 1 ATOM 2064 N N . LEU B 2 70 ? 60.033 21.949 -15.370 1.00 10.89 ? 68 LEU B N 1 ATOM 2065 C CA . LEU B 2 70 ? 59.224 21.245 -16.350 1.00 13.03 ? 68 LEU B CA 1 ATOM 2066 C C . LEU B 2 70 ? 59.208 19.749 -16.085 1.00 14.07 ? 68 LEU B C 1 ATOM 2067 O O . LEU B 2 70 ? 58.169 19.112 -16.234 1.00 15.87 ? 68 LEU B O 1 ATOM 2068 C CB . LEU B 2 70 ? 59.707 21.528 -17.777 1.00 12.84 ? 68 LEU B CB 1 ATOM 2069 C CG . LEU B 2 70 ? 59.393 22.940 -18.283 1.00 13.51 ? 68 LEU B CG 1 ATOM 2070 C CD1 . LEU B 2 70 ? 59.800 23.084 -19.739 1.00 18.47 ? 68 LEU B CD1 1 ATOM 2071 C CD2 . LEU B 2 70 ? 57.898 23.266 -18.102 1.00 10.24 ? 68 LEU B CD2 1 ATOM 2072 N N . GLU B 2 71 ? 60.352 19.182 -15.716 1.00 12.91 ? 69 GLU B N 1 ATOM 2073 C CA . GLU B 2 71 ? 60.403 17.756 -15.409 1.00 13.49 ? 69 GLU B CA 1 ATOM 2074 C C . GLU B 2 71 ? 59.615 17.420 -14.136 1.00 13.19 ? 69 GLU B C 1 ATOM 2075 O O . GLU B 2 71 ? 59.038 16.328 -14.020 1.00 16.12 ? 69 GLU B O 1 ATOM 2076 C CB . GLU B 2 71 ? 61.859 17.269 -15.306 1.00 16.35 ? 69 GLU B CB 1 ATOM 2077 C CG . GLU B 2 71 ? 62.595 17.284 -16.651 1.00 16.07 ? 69 GLU B CG 1 ATOM 2078 C CD . GLU B 2 71 ? 61.917 16.407 -17.721 1.00 18.95 ? 69 GLU B CD 1 ATOM 2079 O OE1 . GLU B 2 71 ? 61.160 15.475 -17.370 1.00 19.05 ? 69 GLU B OE1 1 ATOM 2080 O OE2 . GLU B 2 71 ? 62.111 16.672 -18.925 1.00 22.08 ? 69 GLU B OE2 1 ATOM 2081 N N . GLN B 2 72 ? 59.559 18.353 -13.192 1.00 9.42 ? 70 GLN B N 1 ATOM 2082 C CA . GLN B 2 72 ? 58.716 18.132 -12.026 1.00 16.10 ? 70 GLN B CA 1 ATOM 2083 C C . GLN B 2 72 ? 57.266 18.011 -12.504 1.00 12.20 ? 70 GLN B C 1 ATOM 2084 O O . GLN B 2 72 ? 56.553 17.086 -12.125 1.00 11.44 ? 70 GLN B O 1 ATOM 2085 C CB . GLN B 2 72 ? 58.846 19.277 -11.020 1.00 16.72 ? 70 GLN B CB 1 ATOM 2086 C CG . GLN B 2 72 ? 60.001 19.141 -10.064 1.00 19.84 ? 70 GLN B CG 1 ATOM 2087 C CD . GLN B 2 72 ? 59.565 18.505 -8.769 1.00 37.70 ? 70 GLN B CD 1 ATOM 2088 O OE1 . GLN B 2 72 ? 59.814 17.324 -8.528 1.00 38.98 ? 70 GLN B OE1 1 ATOM 2089 N NE2 . GLN B 2 72 ? 58.887 19.284 -7.928 1.00 43.09 ? 70 GLN B NE2 1 ATOM 2090 N N . LYS B 2 73 ? 56.847 18.955 -13.344 1.00 10.27 ? 71 LYS B N 1 ATOM 2091 C CA . LYS B 2 73 ? 55.483 18.981 -13.859 1.00 11.65 ? 71 LYS B CA 1 ATOM 2092 C C . LYS B 2 73 ? 55.163 17.806 -14.794 1.00 14.53 ? 71 LYS B C 1 ATOM 2093 O O . LYS B 2 73 ? 54.053 17.282 -14.799 1.00 14.80 ? 71 LYS B O 1 ATOM 2094 C CB . LYS B 2 73 ? 55.242 20.302 -14.589 1.00 9.45 ? 71 LYS B CB 1 ATOM 2095 C CG . LYS B 2 73 ? 55.374 21.493 -13.658 1.00 12.44 ? 71 LYS B CG 1 ATOM 2096 C CD . LYS B 2 73 ? 54.373 21.479 -12.526 1.00 17.38 ? 71 LYS B CD 1 ATOM 2097 C CE . LYS B 2 73 ? 54.705 22.592 -11.525 1.00 13.47 ? 71 LYS B CE 1 ATOM 2098 N NZ . LYS B 2 73 ? 53.743 22.623 -10.397 1.00 10.29 ? 71 LYS B NZ 1 ATOM 2099 N N . ARG B 2 74 ? 56.146 17.403 -15.592 1.00 14.37 ? 72 ARG B N 1 ATOM 2100 C CA . ARG B 2 74 ? 55.977 16.284 -16.513 1.00 12.26 ? 72 ARG B CA 1 ATOM 2101 C C . ARG B 2 74 ? 55.817 14.938 -15.828 1.00 13.68 ? 72 ARG B C 1 ATOM 2102 O O . ARG B 2 74 ? 55.250 14.011 -16.404 1.00 9.06 ? 72 ARG B O 1 ATOM 2103 C CB . ARG B 2 74 ? 57.135 16.212 -17.500 1.00 13.12 ? 72 ARG B CB 1 ATOM 2104 C CG . ARG B 2 74 ? 57.073 17.280 -18.567 1.00 15.75 ? 72 ARG B CG 1 ATOM 2105 C CD . ARG B 2 74 ? 58.393 17.409 -19.289 1.00 12.08 ? 72 ARG B CD 1 ATOM 2106 N NE . ARG B 2 74 ? 58.372 18.561 -20.165 1.00 11.53 ? 72 ARG B NE 1 ATOM 2107 C CZ . ARG B 2 74 ? 59.418 18.982 -20.853 1.00 15.24 ? 72 ARG B CZ 1 ATOM 2108 N NH1 . ARG B 2 74 ? 60.572 18.329 -20.764 1.00 15.00 ? 72 ARG B NH1 1 ATOM 2109 N NH2 . ARG B 2 74 ? 59.303 20.048 -21.636 1.00 18.40 ? 72 ARG B NH2 1 ATOM 2110 N N . ALA B 2 75 ? 56.315 14.829 -14.603 1.00 13.24 ? 73 ALA B N 1 ATOM 2111 C CA . ALA B 2 75 ? 56.233 13.575 -13.874 1.00 14.26 ? 73 ALA B CA 1 ATOM 2112 C C . ALA B 2 75 ? 54.981 13.506 -12.986 1.00 14.33 ? 73 ALA B C 1 ATOM 2113 O O . ALA B 2 75 ? 54.668 12.447 -12.422 1.00 13.36 ? 73 ALA B O 1 ATOM 2114 C CB . ALA B 2 75 ? 57.495 13.377 -13.038 1.00 11.81 ? 73 ALA B CB 1 ATOM 2115 N N . ALA B 2 76 ? 54.254 14.622 -12.902 1.00 12.50 ? 74 ALA B N 1 ATOM 2116 C CA . ALA B 2 76 ? 53.130 14.760 -11.968 1.00 14.02 ? 74 ALA B CA 1 ATOM 2117 C C . ALA B 2 76 ? 52.038 13.703 -12.168 1.00 8.30 ? 74 ALA B C 1 ATOM 2118 O O . ALA B 2 76 ? 51.433 13.255 -11.199 1.00 12.33 ? 74 ALA B O 1 ATOM 2119 C CB . ALA B 2 76 ? 52.524 16.169 -12.066 1.00 11.86 ? 74 ALA B CB 1 ATOM 2120 N N . VAL B 2 77 ? 51.776 13.303 -13.405 1.00 10.16 ? 75 VAL B N 1 ATOM 2121 C CA . VAL B 2 77 ? 50.764 12.275 -13.644 1.00 10.32 ? 75 VAL B CA 1 ATOM 2122 C C . VAL B 2 77 ? 51.098 11.024 -12.836 1.00 17.15 ? 75 VAL B C 1 ATOM 2123 O O . VAL B 2 77 ? 50.206 10.309 -12.392 1.00 16.14 ? 75 VAL B O 1 ATOM 2124 C CB . VAL B 2 77 ? 50.651 11.895 -15.145 1.00 17.56 ? 75 VAL B CB 1 ATOM 2125 C CG1 . VAL B 2 77 ? 49.918 12.978 -15.922 1.00 15.37 ? 75 VAL B CG1 1 ATOM 2126 C CG2 . VAL B 2 77 ? 52.059 11.589 -15.760 1.00 10.80 ? 75 VAL B CG2 1 ATOM 2127 N N . ASP B 2 78 ? 52.390 10.779 -12.621 1.00 13.41 ? 76 ASP B N 1 ATOM 2128 C CA . ASP B 2 78 ? 52.814 9.631 -11.823 1.00 13.67 ? 76 ASP B CA 1 ATOM 2129 C C . ASP B 2 78 ? 52.984 9.960 -10.352 1.00 12.11 ? 76 ASP B C 1 ATOM 2130 O O . ASP B 2 78 ? 52.412 9.297 -9.495 1.00 14.31 ? 76 ASP B O 1 ATOM 2131 C CB . ASP B 2 78 ? 54.126 9.058 -12.357 1.00 11.61 ? 76 ASP B CB 1 ATOM 2132 C CG . ASP B 2 78 ? 53.970 8.414 -13.720 1.00 23.80 ? 76 ASP B CG 1 ATOM 2133 O OD1 . ASP B 2 78 ? 52.854 7.931 -14.026 1.00 15.07 ? 76 ASP B OD1 1 ATOM 2134 O OD2 . ASP B 2 78 ? 54.968 8.398 -14.483 1.00 24.32 ? 76 ASP B OD2 1 ATOM 2135 N N . THR B 2 79 ? 53.801 10.965 -10.058 1.00 12.76 ? 77 THR B N 1 ATOM 2136 C CA . THR B 2 79 ? 54.211 11.236 -8.682 1.00 9.80 ? 77 THR B CA 1 ATOM 2137 C C . THR B 2 79 ? 53.153 11.962 -7.873 1.00 12.19 ? 77 THR B C 1 ATOM 2138 O O . THR B 2 79 ? 53.203 11.982 -6.645 1.00 17.51 ? 77 THR B O 1 ATOM 2139 C CB . THR B 2 79 ? 55.457 12.121 -8.650 1.00 15.76 ? 77 THR B CB 1 ATOM 2140 O OG1 . THR B 2 79 ? 55.127 13.418 -9.189 1.00 11.59 ? 77 THR B OG1 1 ATOM 2141 C CG2 . THR B 2 79 ? 56.600 11.480 -9.443 1.00 12.68 ? 77 THR B CG2 1 ATOM 2142 N N . TYR B 2 80 ? 52.189 12.551 -8.570 1.00 14.44 ? 78 TYR B N 1 ATOM 2143 C CA . TYR B 2 80 ? 51.159 13.358 -7.928 1.00 14.01 ? 78 TYR B CA 1 ATOM 2144 C C . TYR B 2 80 ? 49.769 12.761 -8.151 1.00 11.12 ? 78 TYR B C 1 ATOM 2145 O O . TYR B 2 80 ? 49.149 12.283 -7.217 1.00 11.00 ? 78 TYR B O 1 ATOM 2146 C CB . TYR B 2 80 ? 51.225 14.782 -8.488 1.00 11.32 ? 78 TYR B CB 1 ATOM 2147 C CG . TYR B 2 80 ? 50.170 15.742 -7.999 1.00 9.16 ? 78 TYR B CG 1 ATOM 2148 C CD1 . TYR B 2 80 ? 50.094 16.102 -6.666 1.00 7.30 ? 78 TYR B CD1 1 ATOM 2149 C CD2 . TYR B 2 80 ? 49.260 16.299 -8.884 1.00 11.29 ? 78 TYR B CD2 1 ATOM 2150 C CE1 . TYR B 2 80 ? 49.131 16.985 -6.226 1.00 11.19 ? 78 TYR B CE1 1 ATOM 2151 C CE2 . TYR B 2 80 ? 48.298 17.185 -8.456 1.00 11.73 ? 78 TYR B CE2 1 ATOM 2152 C CZ . TYR B 2 80 ? 48.235 17.525 -7.127 1.00 13.52 ? 78 TYR B CZ 1 ATOM 2153 O OH . TYR B 2 80 ? 47.267 18.414 -6.704 1.00 8.92 ? 78 TYR B OH 1 ATOM 2154 N N . CYS B 2 81 ? 49.335 12.714 -9.405 1.00 8.27 ? 79 CYS B N 1 ATOM 2155 C CA . CYS B 2 81 ? 48.005 12.220 -9.725 1.00 12.88 ? 79 CYS B CA 1 ATOM 2156 C C . CYS B 2 81 ? 47.814 10.741 -9.382 1.00 17.58 ? 79 CYS B C 1 ATOM 2157 O O . CYS B 2 81 ? 46.997 10.420 -8.523 1.00 11.58 ? 79 CYS B O 1 ATOM 2158 C CB . CYS B 2 81 ? 47.695 12.438 -11.209 1.00 11.32 ? 79 CYS B CB 1 ATOM 2159 S SG . CYS B 2 81 ? 47.745 14.172 -11.730 1.00 16.89 ? 79 CYS B SG 1 ATOM 2160 N N . ARG B 2 82 ? 48.618 9.856 -9.979 1.00 17.21 ? 80 ARG B N 1 ATOM 2161 C CA . ARG B 2 82 ? 48.464 8.423 -9.721 1.00 19.13 ? 80 ARG B CA 1 ATOM 2162 C C . ARG B 2 82 ? 48.708 8.151 -8.256 1.00 13.92 ? 80 ARG B C 1 ATOM 2163 O O . ARG B 2 82 ? 48.022 7.324 -7.667 1.00 14.71 ? 80 ARG B O 1 ATOM 2164 C CB . ARG B 2 82 ? 49.402 7.576 -10.601 1.00 17.62 ? 80 ARG B CB 1 ATOM 2165 C CG . ARG B 2 82 ? 48.922 7.439 -12.048 1.00 16.33 ? 80 ARG B CG 1 ATOM 2166 C CD . ARG B 2 82 ? 49.836 6.584 -12.930 1.00 9.49 ? 80 ARG B CD 1 ATOM 2167 N NE . ARG B 2 82 ? 49.216 6.341 -14.231 1.00 11.28 ? 80 ARG B NE 1 ATOM 2168 C CZ . ARG B 2 82 ? 49.432 7.084 -15.313 1.00 19.04 ? 80 ARG B CZ 1 ATOM 2169 N NH1 . ARG B 2 82 ? 48.810 6.806 -16.451 1.00 16.84 ? 80 ARG B NH1 1 ATOM 2170 N NH2 . ARG B 2 82 ? 50.264 8.117 -15.252 1.00 17.47 ? 80 ARG B NH2 1 ATOM 2171 N N . HIS B 2 83 ? 49.664 8.855 -7.658 1.00 12.77 ? 81 HIS B N 1 ATOM 2172 C CA . HIS B 2 83 ? 49.917 8.665 -6.235 1.00 10.22 ? 81 HIS B CA 1 ATOM 2173 C C . HIS B 2 83 ? 48.721 8.991 -5.353 1.00 14.71 ? 81 HIS B C 1 ATOM 2174 O O . HIS B 2 83 ? 48.313 8.169 -4.540 1.00 20.37 ? 81 HIS B O 1 ATOM 2175 C CB . HIS B 2 83 ? 51.085 9.526 -5.764 1.00 10.61 ? 81 HIS B CB 1 ATOM 2176 C CG . HIS B 2 83 ? 51.307 9.451 -4.287 1.00 14.20 ? 81 HIS B CG 1 ATOM 2177 N ND1 . HIS B 2 83 ? 52.094 8.484 -3.698 1.00 16.75 ? 81 HIS B ND1 1 ATOM 2178 C CD2 . HIS B 2 83 ? 50.819 10.205 -3.274 1.00 18.21 ? 81 HIS B CD2 1 ATOM 2179 C CE1 . HIS B 2 83 ? 52.094 8.659 -2.387 1.00 20.88 ? 81 HIS B CE1 1 ATOM 2180 N NE2 . HIS B 2 83 ? 51.330 9.699 -2.104 1.00 16.85 ? 81 HIS B NE2 1 ATOM 2181 N N . ASN B 2 84 ? 48.167 10.194 -5.507 1.00 17.30 ? 82 ASN B N 1 ATOM 2182 C CA . ASN B 2 84 ? 47.064 10.634 -4.657 1.00 17.14 ? 82 ASN B CA 1 ATOM 2183 C C . ASN B 2 84 ? 45.802 9.825 -4.884 1.00 14.81 ? 82 ASN B C 1 ATOM 2184 O O . ASN B 2 84 ? 45.035 9.590 -3.958 1.00 16.82 ? 82 ASN B O 1 ATOM 2185 C CB . ASN B 2 84 ? 46.804 12.124 -4.846 1.00 15.16 ? 82 ASN B CB 1 ATOM 2186 C CG . ASN B 2 84 ? 47.855 12.971 -4.163 1.00 14.58 ? 82 ASN B CG 1 ATOM 2187 O OD1 . ASN B 2 84 ? 48.584 12.488 -3.291 1.00 19.23 ? 82 ASN B OD1 1 ATOM 2188 N ND2 . ASN B 2 84 ? 47.930 14.233 -4.531 1.00 10.51 ? 82 ASN B ND2 1 ATOM 2189 N N . TYR B 2 85 ? 45.606 9.382 -6.118 1.00 16.98 ? 83 TYR B N 1 ATOM 2190 C CA . TYR B 2 85 ? 44.483 8.523 -6.439 1.00 18.60 ? 83 TYR B CA 1 ATOM 2191 C C . TYR B 2 85 ? 44.598 7.263 -5.588 1.00 21.56 ? 83 TYR B C 1 ATOM 2192 O O . TYR B 2 85 ? 43.635 6.832 -4.962 1.00 13.81 ? 83 TYR B O 1 ATOM 2193 C CB . TYR B 2 85 ? 44.497 8.171 -7.917 1.00 17.13 ? 83 TYR B CB 1 ATOM 2194 C CG . TYR B 2 85 ? 43.289 7.424 -8.443 1.00 20.13 ? 83 TYR B CG 1 ATOM 2195 C CD1 . TYR B 2 85 ? 42.261 8.094 -9.103 1.00 19.59 ? 83 TYR B CD1 1 ATOM 2196 C CD2 . TYR B 2 85 ? 43.182 6.043 -8.290 1.00 13.77 ? 83 TYR B CD2 1 ATOM 2197 C CE1 . TYR B 2 85 ? 41.168 7.407 -9.605 1.00 14.19 ? 83 TYR B CE1 1 ATOM 2198 C CE2 . TYR B 2 85 ? 42.089 5.352 -8.779 1.00 15.42 ? 83 TYR B CE2 1 ATOM 2199 C CZ . TYR B 2 85 ? 41.087 6.038 -9.437 1.00 21.06 ? 83 TYR B CZ 1 ATOM 2200 O OH . TYR B 2 85 ? 40.004 5.353 -9.936 1.00 20.69 ? 83 TYR B OH 1 ATOM 2201 N N . GLY B 2 86 ? 45.808 6.709 -5.532 1.00 17.67 ? 84 GLY B N 1 ATOM 2202 C CA . GLY B 2 86 ? 46.063 5.512 -4.752 1.00 19.28 ? 84 GLY B CA 1 ATOM 2203 C C . GLY B 2 86 ? 45.781 5.720 -3.281 1.00 13.97 ? 84 GLY B C 1 ATOM 2204 O O . GLY B 2 86 ? 45.229 4.851 -2.623 1.00 19.43 ? 84 GLY B O 1 ATOM 2205 N N . VAL B 2 87 ? 46.089 6.914 -2.797 1.00 14.19 ? 85 VAL B N 1 ATOM 2206 C CA . VAL B 2 87 ? 45.938 7.266 -1.388 1.00 19.58 ? 85 VAL B CA 1 ATOM 2207 C C . VAL B 2 87 ? 44.475 7.334 -0.941 1.00 23.28 ? 85 VAL B C 1 ATOM 2208 O O . VAL B 2 87 ? 44.125 6.903 0.160 1.00 19.07 ? 85 VAL B O 1 ATOM 2209 C CB . VAL B 2 87 ? 46.614 8.617 -1.082 1.00 21.22 ? 85 VAL B CB 1 ATOM 2210 C CG1 . VAL B 2 87 ? 46.329 9.050 0.357 1.00 19.58 ? 85 VAL B CG1 1 ATOM 2211 C CG2 . VAL B 2 87 ? 48.124 8.525 -1.321 1.00 22.14 ? 85 VAL B CG2 1 ATOM 2212 N N . GLY B 2 88 ? 43.632 7.873 -1.815 1.00 21.44 ? 86 GLY B N 1 ATOM 2213 C CA . GLY B 2 88 ? 42.249 8.218 -1.523 1.00 16.61 ? 86 GLY B CA 1 ATOM 2214 C C . GLY B 2 88 ? 41.203 7.283 -2.101 1.00 23.07 ? 86 GLY B C 1 ATOM 2215 O O . GLY B 2 88 ? 40.008 7.439 -1.841 1.00 20.20 ? 86 GLY B O 1 ATOM 2216 N N . GLU B 2 89 ? 41.647 6.311 -2.891 1.00 24.32 ? 87 GLU B N 1 ATOM 2217 C CA . GLU B 2 89 ? 40.750 5.456 -3.651 1.00 21.25 ? 87 GLU B CA 1 ATOM 2218 C C . GLU B 2 89 ? 39.686 4.773 -2.784 1.00 24.93 ? 87 GLU B C 1 ATOM 2219 O O . GLU B 2 89 ? 38.524 4.683 -3.191 1.00 23.06 ? 87 GLU B O 1 ATOM 2220 C CB . GLU B 2 89 ? 41.568 4.376 -4.360 1.00 23.44 ? 87 GLU B CB 1 ATOM 2221 C CG . GLU B 2 89 ? 40.748 3.448 -5.240 1.00 31.44 ? 87 GLU B CG 1 ATOM 2222 C CD . GLU B 2 89 ? 41.610 2.456 -5.993 1.00 46.38 ? 87 GLU B CD 1 ATOM 2223 O OE1 . GLU B 2 89 ? 42.849 2.633 -5.988 1.00 39.66 ? 87 GLU B OE1 1 ATOM 2224 O OE2 . GLU B 2 89 ? 41.050 1.500 -6.582 1.00 50.87 ? 87 GLU B OE2 1 ATOM 2225 N N . SER B 2 90 ? 40.074 4.260 -1.621 1.00 24.92 ? 88 SER B N 1 ATOM 2226 C CA . SER B 2 90 ? 39.131 3.513 -0.784 1.00 25.46 ? 88 SER B CA 1 ATOM 2227 C C . SER B 2 90 ? 37.953 4.347 -0.254 1.00 27.35 ? 88 SER B C 1 ATOM 2228 O O . SER B 2 90 ? 36.869 3.813 -0.033 1.00 21.23 ? 88 SER B O 1 ATOM 2229 C CB . SER B 2 90 ? 39.854 2.882 0.406 1.00 23.19 ? 88 SER B CB 1 ATOM 2230 O OG . SER B 2 90 ? 40.152 3.861 1.395 1.00 33.04 ? 88 SER B OG 1 ATOM 2231 N N . PHE B 2 91 ? 38.133 5.656 -0.090 1.00 24.80 ? 89 PHE B N 1 ATOM 2232 C CA . PHE B 2 91 ? 37.036 6.454 0.452 1.00 22.23 ? 89 PHE B CA 1 ATOM 2233 C C . PHE B 2 91 ? 36.504 7.515 -0.497 1.00 18.93 ? 89 PHE B C 1 ATOM 2234 O O . PHE B 2 91 ? 35.660 8.317 -0.114 1.00 20.33 ? 89 PHE B O 1 ATOM 2235 C CB . PHE B 2 91 ? 37.446 7.102 1.780 1.00 14.58 ? 89 PHE B CB 1 ATOM 2236 C CG . PHE B 2 91 ? 38.682 7.960 1.710 1.00 25.59 ? 89 PHE B CG 1 ATOM 2237 C CD1 . PHE B 2 91 ? 38.588 9.311 1.389 1.00 20.70 ? 89 PHE B CD1 1 ATOM 2238 C CD2 . PHE B 2 91 ? 39.932 7.428 1.987 1.00 28.79 ? 89 PHE B CD2 1 ATOM 2239 C CE1 . PHE B 2 91 ? 39.712 10.109 1.344 1.00 22.89 ? 89 PHE B CE1 1 ATOM 2240 C CE2 . PHE B 2 91 ? 41.074 8.224 1.937 1.00 25.19 ? 89 PHE B CE2 1 ATOM 2241 C CZ . PHE B 2 91 ? 40.962 9.563 1.613 1.00 30.14 ? 89 PHE B CZ 1 ATOM 2242 N N . THR B 2 92 ? 36.958 7.494 -1.742 1.00 18.68 ? 90 THR B N 1 ATOM 2243 C CA . THR B 2 92 ? 36.455 8.443 -2.714 1.00 13.96 ? 90 THR B CA 1 ATOM 2244 C C . THR B 2 92 ? 35.887 7.705 -3.920 1.00 16.03 ? 90 THR B C 1 ATOM 2245 O O . THR B 2 92 ? 34.668 7.621 -4.089 1.00 17.62 ? 90 THR B O 1 ATOM 2246 C CB . THR B 2 92 ? 37.583 9.406 -3.197 1.00 15.66 ? 90 THR B CB 1 ATOM 2247 O OG1 . THR B 2 92 ? 38.662 8.661 -3.779 1.00 13.79 ? 90 THR B OG1 1 ATOM 2248 C CG2 . THR B 2 92 ? 38.106 10.249 -2.054 1.00 13.95 ? 90 THR B CG2 1 ATOM 2249 N N . VAL B 2 93 ? 36.782 7.146 -4.730 1.00 13.71 ? 91 VAL B N 1 ATOM 2250 C CA . VAL B 2 93 ? 36.433 6.354 -5.910 1.00 16.80 ? 91 VAL B CA 1 ATOM 2251 C C . VAL B 2 93 ? 35.475 5.192 -5.566 1.00 21.20 ? 91 VAL B C 1 ATOM 2252 O O . VAL B 2 93 ? 34.545 4.893 -6.317 1.00 22.83 ? 91 VAL B O 1 ATOM 2253 C CB . VAL B 2 93 ? 37.724 5.828 -6.583 1.00 21.91 ? 91 VAL B CB 1 ATOM 2254 C CG1 . VAL B 2 93 ? 37.403 4.863 -7.712 1.00 22.67 ? 91 VAL B CG1 1 ATOM 2255 C CG2 . VAL B 2 93 ? 38.548 7.004 -7.097 1.00 16.81 ? 91 VAL B CG2 1 ATOM 2256 N N . GLN B 2 94 ? 35.753 4.518 -4.452 1.00 13.80 ? 92 GLN B N 1 ATOM 2257 C CA . GLN B 2 94 ? 34.995 3.348 -4.016 1.00 24.16 ? 92 GLN B CA 1 ATOM 2258 C C . GLN B 2 94 ? 33.859 3.707 -3.051 1.00 18.30 ? 92 GLN B C 1 ATOM 2259 O O . GLN B 2 94 ? 33.232 2.819 -2.492 1.00 17.59 ? 92 GLN B O 1 ATOM 2260 C CB . GLN B 2 94 ? 35.911 2.281 -3.405 1.00 16.69 ? 92 GLN B CB 1 ATOM 2261 C CG . GLN B 2 94 ? 36.921 1.749 -4.416 1.00 25.65 ? 92 GLN B CG 1 ATOM 2262 C CD . GLN B 2 94 ? 37.891 0.762 -3.819 1.00 39.32 ? 92 GLN B CD 1 ATOM 2263 O OE1 . GLN B 2 94 ? 37.753 0.360 -2.663 1.00 45.72 ? 92 GLN B OE1 1 ATOM 2264 N NE2 . GLN B 2 94 ? 38.863 0.332 -4.619 1.00 55.53 ? 92 GLN B NE2 1 ATOM 2265 N N . ARG B 2 95 ? 33.657 4.993 -2.779 1.00 17.16 ? 93 ARG B N 1 ATOM 2266 C CA . ARG B 2 95 ? 32.596 5.394 -1.859 1.00 14.66 ? 93 ARG B CA 1 ATOM 2267 C C . ARG B 2 95 ? 31.231 5.054 -2.460 1.00 14.74 ? 93 ARG B C 1 ATOM 2268 O O . ARG B 2 95 ? 30.942 5.381 -3.614 1.00 17.08 ? 93 ARG B O 1 ATOM 2269 C CB . ARG B 2 95 ? 32.671 6.880 -1.505 1.00 16.95 ? 93 ARG B CB 1 ATOM 2270 C CG . ARG B 2 95 ? 31.554 7.354 -0.548 1.00 16.54 ? 93 ARG B CG 1 ATOM 2271 C CD . ARG B 2 95 ? 31.744 8.821 -0.220 1.00 17.58 ? 93 ARG B CD 1 ATOM 2272 N NE . ARG B 2 95 ? 30.631 9.434 0.496 1.00 14.35 ? 93 ARG B NE 1 ATOM 2273 C CZ . ARG B 2 95 ? 30.422 9.335 1.805 1.00 14.33 ? 93 ARG B CZ 1 ATOM 2274 N NH1 . ARG B 2 95 ? 31.243 8.622 2.568 1.00 10.93 ? 93 ARG B NH1 1 ATOM 2275 N NH2 . ARG B 2 95 ? 29.374 9.943 2.353 1.00 13.60 ? 93 ARG B NH2 1 ATOM 2276 N N . ARG B 2 96 ? 30.417 4.345 -1.684 1.00 15.16 ? 94 ARG B N 1 ATOM 2277 C CA . ARG B 2 96 ? 29.068 3.968 -2.109 1.00 20.37 ? 94 ARG B CA 1 ATOM 2278 C C . ARG B 2 96 ? 28.117 4.138 -0.931 1.00 23.65 ? 94 ARG B C 1 ATOM 2279 O O . ARG B 2 96 ? 28.320 3.536 0.116 1.00 17.15 ? 94 ARG B O 1 ATOM 2280 C CB . ARG B 2 96 ? 29.035 2.523 -2.617 1.00 18.54 ? 94 ARG B CB 1 ATOM 2281 C CG . ARG B 2 96 ? 29.948 2.254 -3.814 1.00 23.50 ? 94 ARG B CG 1 ATOM 2282 C CD . ARG B 2 96 ? 29.334 2.765 -5.102 1.00 25.13 ? 94 ARG B CD 1 ATOM 2283 N NE . ARG B 2 96 ? 30.090 2.375 -6.291 1.00 32.56 ? 94 ARG B NE 1 ATOM 2284 C CZ . ARG B 2 96 ? 29.845 1.287 -7.020 1.00 60.16 ? 94 ARG B CZ 1 ATOM 2285 N NH1 . ARG B 2 96 ? 28.866 0.455 -6.678 1.00 51.18 ? 94 ARG B NH1 1 ATOM 2286 N NH2 . ARG B 2 96 ? 30.584 1.024 -8.094 1.00 59.36 ? 94 ARG B NH2 1 ATOM 2287 N N . VAL B 2 97 ? 27.116 5.008 -1.081 1.00 20.37 ? 95 VAL B N 1 ATOM 2288 C CA . VAL B 2 97 ? 26.121 5.187 -0.030 1.00 16.82 ? 95 VAL B CA 1 ATOM 2289 C C . VAL B 2 97 ? 24.743 5.036 -0.662 1.00 19.88 ? 95 VAL B C 1 ATOM 2290 O O . VAL B 2 97 ? 24.413 5.724 -1.631 1.00 15.21 ? 95 VAL B O 1 ATOM 2291 C CB . VAL B 2 97 ? 26.235 6.561 0.645 1.00 20.25 ? 95 VAL B CB 1 ATOM 2292 C CG1 . VAL B 2 97 ? 25.286 6.646 1.832 1.00 16.65 ? 95 VAL B CG1 1 ATOM 2293 C CG2 . VAL B 2 97 ? 27.660 6.815 1.104 1.00 16.49 ? 95 VAL B CG2 1 ATOM 2294 N N A TYR B 2 98 ? 23.928 4.168 -0.069 0.60 21.69 ? 96 TYR B N 1 ATOM 2295 N N B TYR B 2 98 ? 23.953 4.115 -0.120 0.40 21.71 ? 96 TYR B N 1 ATOM 2296 C CA A TYR B 2 98 ? 22.598 3.838 -0.584 0.60 22.35 ? 96 TYR B CA 1 ATOM 2297 C CA B TYR B 2 98 ? 22.606 3.862 -0.623 0.40 22.46 ? 96 TYR B CA 1 ATOM 2298 C C A TYR B 2 98 ? 21.625 5.004 -0.479 0.60 19.55 ? 96 TYR B C 1 ATOM 2299 C C B TYR B 2 98 ? 21.728 5.095 -0.568 0.40 19.63 ? 96 TYR B C 1 ATOM 2300 O O A TYR B 2 98 ? 21.635 5.741 0.505 0.60 19.90 ? 96 TYR B O 1 ATOM 2301 O O B TYR B 2 98 ? 21.880 5.945 0.306 0.40 20.46 ? 96 TYR B O 1 ATOM 2302 C CB A TYR B 2 98 ? 22.020 2.637 0.178 0.60 25.94 ? 96 TYR B CB 1 ATOM 2303 C CB B TYR B 2 98 ? 21.990 2.681 0.128 0.40 25.89 ? 96 TYR B CB 1 ATOM 2304 C CG A TYR B 2 98 ? 21.491 2.999 1.553 0.60 26.26 ? 96 TYR B CG 1 ATOM 2305 C CG B TYR B 2 98 ? 22.965 1.528 0.225 0.40 23.22 ? 96 TYR B CG 1 ATOM 2306 C CD1 A TYR B 2 98 ? 20.136 2.864 1.864 0.60 26.72 ? 96 TYR B CD1 1 ATOM 2307 C CD1 B TYR B 2 98 ? 23.659 1.094 -0.900 0.40 24.49 ? 96 TYR B CD1 1 ATOM 2308 C CD2 A TYR B 2 98 ? 22.340 3.507 2.531 0.60 29.35 ? 96 TYR B CD2 1 ATOM 2309 C CD2 B TYR B 2 98 ? 23.211 0.891 1.429 0.40 23.74 ? 96 TYR B CD2 1 ATOM 2310 C CE1 A TYR B 2 98 ? 19.648 3.209 3.125 0.60 24.76 ? 96 TYR B CE1 1 ATOM 2311 C CE1 B TYR B 2 98 ? 24.560 0.052 -0.830 0.40 23.48 ? 96 TYR B CE1 1 ATOM 2312 C CE2 A TYR B 2 98 ? 21.865 3.853 3.784 0.60 31.03 ? 96 TYR B CE2 1 ATOM 2313 C CE2 B TYR B 2 98 ? 24.109 -0.154 1.503 0.40 23.92 ? 96 TYR B CE2 1 ATOM 2314 C CZ A TYR B 2 98 ? 20.521 3.698 4.082 0.60 26.77 ? 96 TYR B CZ 1 ATOM 2315 C CZ B TYR B 2 98 ? 24.782 -0.568 0.376 0.40 23.91 ? 96 TYR B CZ 1 ATOM 2316 O OH A TYR B 2 98 ? 20.057 4.047 5.336 0.60 23.49 ? 96 TYR B OH 1 ATOM 2317 O OH B TYR B 2 98 ? 25.681 -1.608 0.462 0.40 24.57 ? 96 TYR B OH 1 ATOM 2318 N N . PRO B 2 99 ? 20.770 5.174 -1.492 1.00 20.60 ? 97 PRO B N 1 ATOM 2319 C CA . PRO B 2 99 ? 19.724 6.183 -1.334 1.00 18.96 ? 97 PRO B CA 1 ATOM 2320 C C . PRO B 2 99 ? 18.588 5.756 -0.394 1.00 22.76 ? 97 PRO B C 1 ATOM 2321 O O . PRO B 2 99 ? 18.173 4.607 -0.422 1.00 21.07 ? 97 PRO B O 1 ATOM 2322 C CB . PRO B 2 99 ? 19.191 6.332 -2.766 1.00 14.15 ? 97 PRO B CB 1 ATOM 2323 C CG . PRO B 2 99 ? 19.451 4.989 -3.397 1.00 20.31 ? 97 PRO B CG 1 ATOM 2324 C CD . PRO B 2 99 ? 20.758 4.529 -2.820 1.00 13.81 ? 97 PRO B CD 1 ATOM 2325 N N . GLU B 2 100 ? 18.054 6.708 0.369 1.00 18.52 ? 98 GLU B N 1 ATOM 2326 C CA . GLU B 2 100 ? 16.786 6.534 1.064 1.00 22.81 ? 98 GLU B CA 1 ATOM 2327 C C . GLU B 2 100 ? 15.700 7.028 0.134 1.00 21.70 ? 98 GLU B C 1 ATOM 2328 O O . GLU B 2 100 ? 15.827 8.096 -0.445 1.00 18.95 ? 98 GLU B O 1 ATOM 2329 C CB . GLU B 2 100 ? 16.716 7.325 2.366 1.00 28.26 ? 98 GLU B CB 1 ATOM 2330 C CG . GLU B 2 100 ? 17.730 7.013 3.433 1.00 38.25 ? 98 GLU B CG 1 ATOM 2331 C CD . GLU B 2 100 ? 17.225 7.480 4.791 1.00 60.74 ? 98 GLU B CD 1 ATOM 2332 O OE1 . GLU B 2 100 ? 16.486 6.711 5.447 1.00 63.45 ? 98 GLU B OE1 1 ATOM 2333 O OE2 . GLU B 2 100 ? 17.532 8.624 5.188 1.00 60.40 ? 98 GLU B OE2 1 ATOM 2334 N N . VAL B 2 101 ? 14.638 6.258 -0.014 1.00 23.91 ? 99 VAL B N 1 ATOM 2335 C CA . VAL B 2 101 ? 13.567 6.632 -0.928 1.00 23.57 ? 99 VAL B CA 1 ATOM 2336 C C . VAL B 2 101 ? 12.254 6.790 -0.176 1.00 19.37 ? 99 VAL B C 1 ATOM 2337 O O . VAL B 2 101 ? 11.804 5.881 0.518 1.00 29.35 ? 99 VAL B O 1 ATOM 2338 C CB . VAL B 2 101 ? 13.412 5.605 -2.061 1.00 18.55 ? 99 VAL B CB 1 ATOM 2339 C CG1 . VAL B 2 101 ? 12.370 6.059 -3.054 1.00 20.21 ? 99 VAL B CG1 1 ATOM 2340 C CG2 . VAL B 2 101 ? 14.745 5.386 -2.748 1.00 17.00 ? 99 VAL B CG2 1 ATOM 2341 N N . THR B 2 102 ? 11.656 7.966 -0.322 1.00 22.19 ? 100 THR B N 1 ATOM 2342 C CA . THR B 2 102 ? 10.389 8.301 0.313 1.00 20.56 ? 100 THR B CA 1 ATOM 2343 C C . THR B 2 102 ? 9.390 8.768 -0.740 1.00 31.30 ? 100 THR B C 1 ATOM 2344 O O . THR B 2 102 ? 9.756 9.544 -1.628 1.00 26.87 ? 100 THR B O 1 ATOM 2345 C CB . THR B 2 102 ? 10.578 9.435 1.342 1.00 19.43 ? 100 THR B CB 1 ATOM 2346 O OG1 . THR B 2 102 ? 11.559 9.052 2.310 1.00 29.38 ? 100 THR B OG1 1 ATOM 2347 C CG2 . THR B 2 102 ? 9.258 9.804 2.035 1.00 24.83 ? 100 THR B CG2 1 ATOM 2348 N N . VAL B 2 103 ? 8.143 8.300 -0.666 1.00 21.15 ? 101 VAL B N 1 ATOM 2349 C CA . VAL B 2 103 ? 7.107 8.834 -1.547 1.00 24.97 ? 101 VAL B CA 1 ATOM 2350 C C . VAL B 2 103 ? 6.031 9.535 -0.717 1.00 31.59 ? 101 VAL B C 1 ATOM 2351 O O . VAL B 2 103 ? 5.505 8.971 0.243 1.00 28.94 ? 101 VAL B O 1 ATOM 2352 C CB . VAL B 2 103 ? 6.453 7.747 -2.413 1.00 25.52 ? 101 VAL B CB 1 ATOM 2353 C CG1 . VAL B 2 103 ? 5.268 8.327 -3.180 1.00 16.87 ? 101 VAL B CG1 1 ATOM 2354 C CG2 . VAL B 2 103 ? 7.464 7.170 -3.387 1.00 22.47 ? 101 VAL B CG2 1 ATOM 2355 N N . TYR B 2 104 ? 5.713 10.769 -1.084 1.00 28.62 ? 102 TYR B N 1 ATOM 2356 C CA . TYR B 2 104 ? 4.637 11.504 -0.438 1.00 23.40 ? 102 TYR B CA 1 ATOM 2357 C C . TYR B 2 104 ? 3.873 12.346 -1.462 1.00 37.35 ? 102 TYR B C 1 ATOM 2358 O O . TYR B 2 104 ? 4.445 12.781 -2.470 1.00 30.65 ? 102 TYR B O 1 ATOM 2359 C CB . TYR B 2 104 ? 5.173 12.367 0.712 1.00 21.84 ? 102 TYR B CB 1 ATOM 2360 C CG . TYR B 2 104 ? 6.174 13.433 0.330 1.00 32.99 ? 102 TYR B CG 1 ATOM 2361 C CD1 . TYR B 2 104 ? 5.759 14.707 -0.053 1.00 23.38 ? 102 TYR B CD1 1 ATOM 2362 C CD2 . TYR B 2 104 ? 7.543 13.175 0.384 1.00 30.18 ? 102 TYR B CD2 1 ATOM 2363 C CE1 . TYR B 2 104 ? 6.679 15.688 -0.384 1.00 26.13 ? 102 TYR B CE1 1 ATOM 2364 C CE2 . TYR B 2 104 ? 8.470 14.150 0.055 1.00 20.93 ? 102 TYR B CE2 1 ATOM 2365 C CZ . TYR B 2 104 ? 8.037 15.403 -0.328 1.00 32.31 ? 102 TYR B CZ 1 ATOM 2366 O OH . TYR B 2 104 ? 8.967 16.369 -0.654 1.00 32.40 ? 102 TYR B OH 1 ATOM 2367 N N . PRO B 2 105 ? 2.570 12.560 -1.220 1.00 28.45 ? 103 PRO B N 1 ATOM 2368 C CA . PRO B 2 105 ? 1.756 13.349 -2.143 1.00 27.65 ? 103 PRO B CA 1 ATOM 2369 C C . PRO B 2 105 ? 1.939 14.827 -1.881 1.00 24.56 ? 103 PRO B C 1 ATOM 2370 O O . PRO B 2 105 ? 2.285 15.204 -0.770 1.00 29.63 ? 103 PRO B O 1 ATOM 2371 C CB . PRO B 2 105 ? 0.324 12.906 -1.814 1.00 34.29 ? 103 PRO B CB 1 ATOM 2372 C CG . PRO B 2 105 ? 0.387 12.552 -0.363 1.00 30.98 ? 103 PRO B CG 1 ATOM 2373 C CD . PRO B 2 105 ? 1.758 11.954 -0.148 1.00 28.09 ? 103 PRO B CD 1 ATOM 2374 N N . ALA B 2 106 ? 1.739 15.645 -2.903 1.00 23.33 ? 104 ALA B N 1 ATOM 2375 C CA . ALA B 2 106 ? 1.837 17.094 -2.774 1.00 27.78 ? 104 ALA B CA 1 ATOM 2376 C C . ALA B 2 106 ? 0.820 17.788 -3.678 1.00 27.21 ? 104 ALA B C 1 ATOM 2377 O O . ALA B 2 106 ? 0.023 17.130 -4.354 1.00 22.01 ? 104 ALA B O 1 ATOM 2378 C CB . ALA B 2 106 ? 3.252 17.569 -3.099 1.00 28.80 ? 104 ALA B CB 1 ATOM 2379 N N . LYS B 2 107 ? 0.866 19.117 -3.702 1.00 27.07 ? 105 LYS B N 1 ATOM 2380 C CA . LYS B 2 107 ? -0.072 19.895 -4.504 1.00 30.74 ? 105 LYS B CA 1 ATOM 2381 C C . LYS B 2 107 ? 0.696 20.859 -5.402 1.00 38.03 ? 105 LYS B C 1 ATOM 2382 O O . LYS B 2 107 ? 1.672 21.459 -4.966 1.00 37.90 ? 105 LYS B O 1 ATOM 2383 C CB . LYS B 2 107 ? -1.021 20.679 -3.603 1.00 26.27 ? 105 LYS B CB 1 ATOM 2384 C CG . LYS B 2 107 ? -1.902 19.834 -2.699 1.00 28.71 ? 105 LYS B CG 1 ATOM 2385 C CD . LYS B 2 107 ? -2.731 20.759 -1.830 1.00 37.43 ? 105 LYS B CD 1 ATOM 2386 C CE . LYS B 2 107 ? -3.720 20.013 -0.948 1.00 49.24 ? 105 LYS B CE 1 ATOM 2387 N NZ . LYS B 2 107 ? -4.557 20.983 -0.173 1.00 61.60 ? 105 LYS B NZ 1 ATOM 2388 N N . THR B 2 108 ? 0.268 21.003 -6.656 1.00 35.75 ? 106 THR B N 1 ATOM 2389 C CA . THR B 2 108 ? 0.875 21.988 -7.546 1.00 33.36 ? 106 THR B CA 1 ATOM 2390 C C . THR B 2 108 ? 0.388 23.397 -7.215 1.00 42.42 ? 106 THR B C 1 ATOM 2391 O O . THR B 2 108 ? 1.132 24.366 -7.340 1.00 46.92 ? 106 THR B O 1 ATOM 2392 C CB . THR B 2 108 ? 0.570 21.696 -9.024 1.00 42.27 ? 106 THR B CB 1 ATOM 2393 O OG1 . THR B 2 108 ? -0.851 21.654 -9.219 1.00 45.34 ? 106 THR B OG1 1 ATOM 2394 C CG2 . THR B 2 108 ? 1.188 20.372 -9.447 1.00 40.99 ? 106 THR B CG2 1 ATOM 2395 N N . GLN B 2 109 ? -0.872 23.516 -6.818 1.00 43.73 ? 107 GLN B N 1 ATOM 2396 C CA . GLN B 2 109 ? -1.369 24.810 -6.393 1.00 55.35 ? 107 GLN B CA 1 ATOM 2397 C C . GLN B 2 109 ? -2.166 24.692 -5.113 1.00 58.92 ? 107 GLN B C 1 ATOM 2398 O O . GLN B 2 109 ? -2.921 23.729 -4.943 1.00 52.46 ? 107 GLN B O 1 ATOM 2399 C CB . GLN B 2 109 ? -2.312 25.399 -7.450 1.00 58.58 ? 107 GLN B CB 1 ATOM 2400 C CG . GLN B 2 109 ? -1.734 25.814 -8.786 1.00 61.41 ? 107 GLN B CG 1 ATOM 2401 C CD . GLN B 2 109 ? -2.801 26.476 -9.657 1.00 63.71 ? 107 GLN B CD 1 ATOM 2402 O OE1 . GLN B 2 109 ? -3.140 25.983 -10.740 1.00 46.09 ? 107 GLN B OE1 1 ATOM 2403 N NE2 . GLN B 2 109 ? -3.341 27.594 -9.180 1.00 67.38 ? 107 GLN B NE2 1 ATOM 2404 N N . PRO B 2 110 ? -2.010 25.672 -4.209 1.00 70.52 ? 108 PRO B N 1 ATOM 2405 C CA . PRO B 2 110 ? -2.673 25.632 -2.901 1.00 76.63 ? 108 PRO B CA 1 ATOM 2406 C C . PRO B 2 110 ? -4.184 25.441 -3.106 1.00 79.50 ? 108 PRO B C 1 ATOM 2407 O O . PRO B 2 110 ? -4.650 25.711 -4.221 1.00 79.39 ? 108 PRO B O 1 ATOM 2408 C CB . PRO B 2 110 ? -2.330 26.996 -2.283 1.00 79.88 ? 108 PRO B CB 1 ATOM 2409 C CG . PRO B 2 110 ? -1.838 27.845 -3.434 1.00 71.71 ? 108 PRO B CG 1 ATOM 2410 C CD . PRO B 2 110 ? -1.177 26.876 -4.362 1.00 63.12 ? 108 PRO B CD 1 ATOM 2411 N N . LEU B 2 111 ? -4.922 24.992 -2.091 1.00 75.36 ? 109 LEU B N 1 ATOM 2412 C CA . LEU B 2 111 ? -6.359 24.694 -2.232 1.00 79.97 ? 109 LEU B CA 1 ATOM 2413 C C . LEU B 2 111 ? -6.714 23.501 -3.136 1.00 75.34 ? 109 LEU B C 1 ATOM 2414 O O . LEU B 2 111 ? -7.745 22.859 -2.924 1.00 76.99 ? 109 LEU B O 1 ATOM 2415 C CB . LEU B 2 111 ? -7.125 25.940 -2.713 1.00 64.70 ? 109 LEU B CB 1 ATOM 2416 N N . GLN B 2 112 ? -5.888 23.188 -4.130 1.00 63.21 ? 110 GLN B N 1 ATOM 2417 C CA . GLN B 2 112 ? -6.275 22.156 -5.083 1.00 56.04 ? 110 GLN B CA 1 ATOM 2418 C C . GLN B 2 112 ? -6.081 20.812 -4.406 1.00 54.76 ? 110 GLN B C 1 ATOM 2419 O O . GLN B 2 112 ? -5.362 20.724 -3.422 1.00 61.29 ? 110 GLN B O 1 ATOM 2420 C CB . GLN B 2 112 ? -5.432 22.227 -6.355 1.00 54.55 ? 110 GLN B CB 1 ATOM 2421 C CG . GLN B 2 112 ? -6.210 21.923 -7.612 1.00 54.91 ? 110 GLN B CG 1 ATOM 2422 C CD . GLN B 2 112 ? -5.645 22.629 -8.826 1.00 52.94 ? 110 GLN B CD 1 ATOM 2423 O OE1 . GLN B 2 112 ? -4.437 22.846 -8.925 1.00 47.02 ? 110 GLN B OE1 1 ATOM 2424 N NE2 . GLN B 2 112 ? -6.522 23.027 -9.741 1.00 47.73 ? 110 GLN B NE2 1 ATOM 2425 N N . HIS B 2 113 ? -6.747 19.773 -4.899 1.00 43.91 ? 111 HIS B N 1 ATOM 2426 C CA . HIS B 2 113 ? -6.525 18.431 -4.366 1.00 49.15 ? 111 HIS B CA 1 ATOM 2427 C C . HIS B 2 113 ? -5.112 17.938 -4.678 1.00 39.96 ? 111 HIS B C 1 ATOM 2428 O O . HIS B 2 113 ? -4.414 18.548 -5.495 1.00 39.68 ? 111 HIS B O 1 ATOM 2429 C CB . HIS B 2 113 ? -7.579 17.466 -4.911 1.00 32.25 ? 111 HIS B CB 1 ATOM 2430 C CG . HIS B 2 113 ? -8.958 17.748 -4.401 1.00 40.31 ? 111 HIS B CG 1 ATOM 2431 N ND1 . HIS B 2 113 ? -9.608 18.941 -4.635 1.00 39.44 ? 111 HIS B ND1 1 ATOM 2432 C CD2 . HIS B 2 113 ? -9.787 17.016 -3.620 1.00 39.16 ? 111 HIS B CD2 1 ATOM 2433 C CE1 . HIS B 2 113 ? -10.795 18.917 -4.055 1.00 34.63 ? 111 HIS B CE1 1 ATOM 2434 N NE2 . HIS B 2 113 ? -10.926 17.762 -3.428 1.00 41.07 ? 111 HIS B NE2 1 ATOM 2435 N N . HIS B 2 114 ? -4.691 16.851 -4.025 1.00 34.80 ? 112 HIS B N 1 ATOM 2436 C CA . HIS B 2 114 ? -3.372 16.252 -4.289 1.00 37.59 ? 112 HIS B CA 1 ATOM 2437 C C . HIS B 2 114 ? -3.191 15.880 -5.754 1.00 23.00 ? 112 HIS B C 1 ATOM 2438 O O . HIS B 2 114 ? -3.927 15.040 -6.276 1.00 31.41 ? 112 HIS B O 1 ATOM 2439 C CB . HIS B 2 114 ? -3.155 15.008 -3.428 1.00 34.07 ? 112 HIS B CB 1 ATOM 2440 C CG . HIS B 2 114 ? -2.786 15.321 -2.014 1.00 45.51 ? 112 HIS B CG 1 ATOM 2441 N ND1 . HIS B 2 114 ? -1.954 16.369 -1.678 1.00 43.13 ? 112 HIS B ND1 1 ATOM 2442 C CD2 . HIS B 2 114 ? -3.124 14.716 -0.851 1.00 37.50 ? 112 HIS B CD2 1 ATOM 2443 C CE1 . HIS B 2 114 ? -1.812 16.409 -0.365 1.00 44.56 ? 112 HIS B CE1 1 ATOM 2444 N NE2 . HIS B 2 114 ? -2.510 15.417 0.161 1.00 50.39 ? 112 HIS B NE2 1 ATOM 2445 N N . ASN B 2 115 ? -2.203 16.475 -6.410 1.00 19.64 ? 113 ASN B N 1 ATOM 2446 C CA . ASN B 2 115 ? -2.007 16.249 -7.841 1.00 21.38 ? 113 ASN B CA 1 ATOM 2447 C C . ASN B 2 115 ? -0.524 16.131 -8.191 1.00 23.37 ? 113 ASN B C 1 ATOM 2448 O O . ASN B 2 115 ? -0.108 16.329 -9.337 1.00 18.41 ? 113 ASN B O 1 ATOM 2449 C CB . ASN B 2 115 ? -2.660 17.358 -8.659 1.00 22.01 ? 113 ASN B CB 1 ATOM 2450 C CG . ASN B 2 115 ? -2.008 18.715 -8.440 1.00 27.81 ? 113 ASN B CG 1 ATOM 2451 O OD1 . ASN B 2 115 ? -1.210 18.908 -7.518 1.00 25.90 ? 113 ASN B OD1 1 ATOM 2452 N ND2 . ASN B 2 115 ? -2.348 19.666 -9.300 1.00 39.39 ? 113 ASN B ND2 1 ATOM 2453 N N . LEU B 2 116 ? 0.274 15.851 -7.175 1.00 18.88 ? 114 LEU B N 1 ATOM 2454 C CA . LEU B 2 116 ? 1.700 15.688 -7.356 1.00 20.19 ? 114 LEU B CA 1 ATOM 2455 C C . LEU B 2 116 ? 2.242 14.535 -6.508 1.00 20.38 ? 114 LEU B C 1 ATOM 2456 O O . LEU B 2 116 ? 1.995 14.480 -5.303 1.00 24.77 ? 114 LEU B O 1 ATOM 2457 C CB . LEU B 2 116 ? 2.372 17.005 -7.000 1.00 20.17 ? 114 LEU B CB 1 ATOM 2458 C CG . LEU B 2 116 ? 3.755 17.335 -7.511 1.00 36.29 ? 114 LEU B CG 1 ATOM 2459 C CD1 . LEU B 2 116 ? 3.687 17.377 -9.016 1.00 23.16 ? 114 LEU B CD1 1 ATOM 2460 C CD2 . LEU B 2 116 ? 4.156 18.694 -6.955 1.00 40.29 ? 114 LEU B CD2 1 ATOM 2461 N N . LEU B 2 117 ? 2.964 13.602 -7.114 1.00 18.19 ? 115 LEU B N 1 ATOM 2462 C CA . LEU B 2 117 ? 3.598 12.561 -6.309 1.00 18.57 ? 115 LEU B CA 1 ATOM 2463 C C . LEU B 2 117 ? 5.085 12.818 -6.266 1.00 17.31 ? 115 LEU B C 1 ATOM 2464 O O . LEU B 2 117 ? 5.755 12.828 -7.298 1.00 13.65 ? 115 LEU B O 1 ATOM 2465 C CB . LEU B 2 117 ? 3.335 11.158 -6.862 1.00 17.95 ? 115 LEU B CB 1 ATOM 2466 C CG . LEU B 2 117 ? 1.892 10.670 -6.848 1.00 20.91 ? 115 LEU B CG 1 ATOM 2467 C CD1 . LEU B 2 117 ? 1.828 9.243 -7.325 1.00 17.51 ? 115 LEU B CD1 1 ATOM 2468 C CD2 . LEU B 2 117 ? 1.321 10.802 -5.448 1.00 21.33 ? 115 LEU B CD2 1 ATOM 2469 N N . VAL B 2 118 ? 5.614 12.954 -5.057 1.00 19.43 ? 116 VAL B N 1 ATOM 2470 C CA . VAL B 2 118 ? 7.028 13.236 -4.905 1.00 17.07 ? 116 VAL B CA 1 ATOM 2471 C C . VAL B 2 118 ? 7.809 11.980 -4.543 1.00 25.78 ? 116 VAL B C 1 ATOM 2472 O O . VAL B 2 118 ? 7.523 11.315 -3.546 1.00 23.82 ? 116 VAL B O 1 ATOM 2473 C CB . VAL B 2 118 ? 7.278 14.303 -3.830 1.00 15.18 ? 116 VAL B CB 1 ATOM 2474 C CG1 . VAL B 2 118 ? 8.765 14.634 -3.760 1.00 17.99 ? 116 VAL B CG1 1 ATOM 2475 C CG2 . VAL B 2 118 ? 6.471 15.561 -4.121 1.00 19.23 ? 116 VAL B CG2 1 ATOM 2476 N N . CYS B 2 119 ? 8.814 11.671 -5.355 1.00 17.99 ? 117 CYS B N 1 ATOM 2477 C CA . CYS B 2 119 ? 9.759 10.620 -5.008 1.00 17.41 ? 117 CYS B CA 1 ATOM 2478 C C . CYS B 2 119 ? 11.005 11.280 -4.490 1.00 13.15 ? 117 CYS B C 1 ATOM 2479 O O . CYS B 2 119 ? 11.754 11.892 -5.256 1.00 12.50 ? 117 CYS B O 1 ATOM 2480 C CB . CYS B 2 119 ? 10.101 9.733 -6.200 1.00 14.37 ? 117 CYS B CB 1 ATOM 2481 S SG . CYS B 2 119 ? 11.157 8.322 -5.719 1.00 18.12 ? 117 CYS B SG 1 ATOM 2482 N N . SER B 2 120 ? 11.197 11.195 -3.178 1.00 13.91 ? 118 SER B N 1 ATOM 2483 C CA . SER B 2 120 ? 12.347 11.820 -2.541 1.00 16.12 ? 118 SER B CA 1 ATOM 2484 C C . SER B 2 120 ? 13.475 10.811 -2.347 1.00 25.82 ? 118 SER B C 1 ATOM 2485 O O . SER B 2 120 ? 13.328 9.810 -1.628 1.00 19.72 ? 118 SER B O 1 ATOM 2486 C CB . SER B 2 120 ? 11.946 12.437 -1.203 1.00 13.14 ? 118 SER B CB 1 ATOM 2487 O OG . SER B 2 120 ? 13.012 13.172 -0.634 1.00 20.15 ? 118 SER B OG 1 ATOM 2488 N N . VAL B 2 121 ? 14.598 11.087 -2.997 1.00 15.06 ? 119 VAL B N 1 ATOM 2489 C CA . VAL B 2 121 ? 15.741 10.204 -2.963 1.00 8.05 ? 119 VAL B CA 1 ATOM 2490 C C . VAL B 2 121 ? 16.885 10.906 -2.249 1.00 13.39 ? 119 VAL B C 1 ATOM 2491 O O . VAL B 2 121 ? 17.410 11.895 -2.756 1.00 14.86 ? 119 VAL B O 1 ATOM 2492 C CB . VAL B 2 121 ? 16.166 9.809 -4.389 1.00 15.58 ? 119 VAL B CB 1 ATOM 2493 C CG1 . VAL B 2 121 ? 17.251 8.765 -4.352 1.00 16.26 ? 119 VAL B CG1 1 ATOM 2494 C CG2 . VAL B 2 121 ? 14.966 9.298 -5.176 1.00 12.27 ? 119 VAL B CG2 1 ATOM 2495 N N . ASN B 2 122 ? 17.262 10.417 -1.071 1.00 9.55 ? 120 ASN B N 1 ATOM 2496 C CA . ASN B 2 122 ? 18.160 11.163 -0.190 1.00 11.88 ? 120 ASN B CA 1 ATOM 2497 C C . ASN B 2 122 ? 19.373 10.389 0.271 1.00 17.01 ? 120 ASN B C 1 ATOM 2498 O O . ASN B 2 122 ? 19.308 9.176 0.503 1.00 16.92 ? 120 ASN B O 1 ATOM 2499 C CB . ASN B 2 122 ? 17.425 11.660 1.057 1.00 11.65 ? 120 ASN B CB 1 ATOM 2500 C CG . ASN B 2 122 ? 16.270 12.559 0.727 1.00 17.05 ? 120 ASN B CG 1 ATOM 2501 O OD1 . ASN B 2 122 ? 15.160 12.096 0.483 1.00 18.25 ? 120 ASN B OD1 1 ATOM 2502 N ND2 . ASN B 2 122 ? 16.517 13.869 0.751 1.00 17.10 ? 120 ASN B ND2 1 ATOM 2503 N N . GLY B 2 123 ? 20.479 11.109 0.404 1.00 10.47 ? 121 GLY B N 1 ATOM 2504 C CA . GLY B 2 123 ? 21.646 10.609 1.098 1.00 11.72 ? 121 GLY B CA 1 ATOM 2505 C C . GLY B 2 123 ? 22.550 9.691 0.299 1.00 12.02 ? 121 GLY B C 1 ATOM 2506 O O . GLY B 2 123 ? 23.333 8.964 0.897 1.00 16.11 ? 121 GLY B O 1 ATOM 2507 N N . PHE B 2 124 ? 22.446 9.702 -1.029 1.00 11.74 ? 122 PHE B N 1 ATOM 2508 C CA . PHE B 2 124 ? 23.187 8.734 -1.832 1.00 14.41 ? 122 PHE B CA 1 ATOM 2509 C C . PHE B 2 124 ? 24.518 9.296 -2.326 1.00 15.93 ? 122 PHE B C 1 ATOM 2510 O O . PHE B 2 124 ? 24.732 10.511 -2.355 1.00 12.45 ? 122 PHE B O 1 ATOM 2511 C CB . PHE B 2 124 ? 22.357 8.216 -3.012 1.00 13.23 ? 122 PHE B CB 1 ATOM 2512 C CG . PHE B 2 124 ? 21.864 9.280 -3.961 1.00 12.04 ? 122 PHE B CG 1 ATOM 2513 C CD1 . PHE B 2 124 ? 22.612 9.643 -5.071 1.00 14.30 ? 122 PHE B CD1 1 ATOM 2514 C CD2 . PHE B 2 124 ? 20.616 9.866 -3.781 1.00 11.48 ? 122 PHE B CD2 1 ATOM 2515 C CE1 . PHE B 2 124 ? 22.141 10.592 -5.959 1.00 12.31 ? 122 PHE B CE1 1 ATOM 2516 C CE2 . PHE B 2 124 ? 20.143 10.829 -4.663 1.00 11.01 ? 122 PHE B CE2 1 ATOM 2517 C CZ . PHE B 2 124 ? 20.901 11.186 -5.752 1.00 9.24 ? 122 PHE B CZ 1 ATOM 2518 N N . TYR B 2 125 ? 25.416 8.379 -2.670 1.00 16.94 ? 123 TYR B N 1 ATOM 2519 C CA . TYR B 2 125 ? 26.707 8.686 -3.279 1.00 14.84 ? 123 TYR B CA 1 ATOM 2520 C C . TYR B 2 125 ? 27.180 7.459 -4.081 1.00 17.63 ? 123 TYR B C 1 ATOM 2521 O O . TYR B 2 125 ? 27.054 6.324 -3.607 1.00 16.07 ? 123 TYR B O 1 ATOM 2522 C CB . TYR B 2 125 ? 27.745 9.039 -2.214 1.00 12.34 ? 123 TYR B CB 1 ATOM 2523 C CG . TYR B 2 125 ? 29.009 9.641 -2.795 1.00 18.43 ? 123 TYR B CG 1 ATOM 2524 C CD1 . TYR B 2 125 ? 29.142 11.020 -2.922 1.00 18.50 ? 123 TYR B CD1 1 ATOM 2525 C CD2 . TYR B 2 125 ? 30.034 8.836 -3.280 1.00 14.46 ? 123 TYR B CD2 1 ATOM 2526 C CE1 . TYR B 2 125 ? 30.281 11.591 -3.472 1.00 15.55 ? 123 TYR B CE1 1 ATOM 2527 C CE2 . TYR B 2 125 ? 31.179 9.396 -3.843 1.00 18.28 ? 123 TYR B CE2 1 ATOM 2528 C CZ . TYR B 2 125 ? 31.294 10.778 -3.935 1.00 20.30 ? 123 TYR B CZ 1 ATOM 2529 O OH . TYR B 2 125 ? 32.419 11.358 -4.489 1.00 19.72 ? 123 TYR B OH 1 ATOM 2530 N N . PRO B 2 126 ? 27.726 7.672 -5.294 1.00 21.01 ? 124 PRO B N 1 ATOM 2531 C CA . PRO B 2 126 ? 27.950 8.965 -5.962 1.00 22.73 ? 124 PRO B CA 1 ATOM 2532 C C . PRO B 2 126 ? 26.680 9.537 -6.608 1.00 18.11 ? 124 PRO B C 1 ATOM 2533 O O . PRO B 2 126 ? 25.567 9.059 -6.361 1.00 11.27 ? 124 PRO B O 1 ATOM 2534 C CB . PRO B 2 126 ? 29.011 8.628 -7.019 1.00 13.93 ? 124 PRO B CB 1 ATOM 2535 C CG . PRO B 2 126 ? 28.758 7.201 -7.341 1.00 15.90 ? 124 PRO B CG 1 ATOM 2536 C CD . PRO B 2 126 ? 28.330 6.556 -6.047 1.00 16.95 ? 124 PRO B CD 1 ATOM 2537 N N . GLY B 2 127 ? 26.853 10.570 -7.424 1.00 18.64 ? 125 GLY B N 1 ATOM 2538 C CA . GLY B 2 127 ? 25.718 11.319 -7.926 1.00 15.71 ? 125 GLY B CA 1 ATOM 2539 C C . GLY B 2 127 ? 24.882 10.705 -9.028 1.00 15.20 ? 125 GLY B C 1 ATOM 2540 O O . GLY B 2 127 ? 23.705 11.031 -9.144 1.00 16.13 ? 125 GLY B O 1 ATOM 2541 N N . SER B 2 128 ? 25.476 9.827 -9.834 1.00 13.44 ? 126 SER B N 1 ATOM 2542 C CA . SER B 2 128 ? 24.776 9.210 -10.966 1.00 12.94 ? 126 SER B CA 1 ATOM 2543 C C . SER B 2 128 ? 23.590 8.366 -10.486 1.00 19.27 ? 126 SER B C 1 ATOM 2544 O O . SER B 2 128 ? 23.740 7.396 -9.741 1.00 22.22 ? 126 SER B O 1 ATOM 2545 C CB . SER B 2 128 ? 25.728 8.371 -11.812 1.00 14.47 ? 126 SER B CB 1 ATOM 2546 O OG . SER B 2 128 ? 26.502 7.523 -10.988 1.00 31.07 ? 126 SER B OG 1 ATOM 2547 N N . ILE B 2 129 ? 22.405 8.745 -10.922 1.00 16.10 ? 127 ILE B N 1 ATOM 2548 C CA . ILE B 2 129 ? 21.200 8.054 -10.516 1.00 13.77 ? 127 ILE B CA 1 ATOM 2549 C C . ILE B 2 129 ? 20.150 8.188 -11.593 1.00 15.79 ? 127 ILE B C 1 ATOM 2550 O O . ILE B 2 129 ? 20.112 9.174 -12.332 1.00 21.32 ? 127 ILE B O 1 ATOM 2551 C CB . ILE B 2 129 ? 20.690 8.618 -9.175 1.00 18.59 ? 127 ILE B CB 1 ATOM 2552 C CG1 . ILE B 2 129 ? 19.772 7.626 -8.473 1.00 20.55 ? 127 ILE B CG1 1 ATOM 2553 C CG2 . ILE B 2 129 ? 19.967 9.947 -9.379 1.00 17.94 ? 127 ILE B CG2 1 ATOM 2554 C CD1 . ILE B 2 129 ? 19.566 7.957 -7.018 1.00 16.07 ? 127 ILE B CD1 1 ATOM 2555 N N . GLU B 2 130 ? 19.282 7.190 -11.671 1.00 24.63 ? 128 GLU B N 1 ATOM 2556 C CA . GLU B 2 130 ? 18.171 7.219 -12.603 1.00 21.39 ? 128 GLU B CA 1 ATOM 2557 C C . GLU B 2 130 ? 16.908 6.924 -11.827 1.00 20.94 ? 128 GLU B C 1 ATOM 2558 O O . GLU B 2 130 ? 16.788 5.889 -11.171 1.00 19.46 ? 128 GLU B O 1 ATOM 2559 C CB . GLU B 2 130 ? 18.367 6.199 -13.728 1.00 22.66 ? 128 GLU B CB 1 ATOM 2560 C CG . GLU B 2 130 ? 17.222 6.156 -14.727 1.00 34.73 ? 128 GLU B CG 1 ATOM 2561 C CD . GLU B 2 130 ? 17.396 7.138 -15.875 1.00 42.01 ? 128 GLU B CD 1 ATOM 2562 O OE1 . GLU B 2 130 ? 16.368 7.658 -16.377 1.00 50.03 ? 128 GLU B OE1 1 ATOM 2563 O OE2 . GLU B 2 130 ? 18.555 7.369 -16.291 1.00 39.16 ? 128 GLU B OE2 1 ATOM 2564 N N . VAL B 2 131 ? 15.965 7.852 -11.898 1.00 18.83 ? 129 VAL B N 1 ATOM 2565 C CA . VAL B 2 131 ? 14.707 7.700 -11.191 1.00 14.40 ? 129 VAL B CA 1 ATOM 2566 C C . VAL B 2 131 ? 13.566 7.728 -12.195 1.00 18.84 ? 129 VAL B C 1 ATOM 2567 O O . VAL B 2 131 ? 13.482 8.642 -13.025 1.00 18.45 ? 129 VAL B O 1 ATOM 2568 C CB . VAL B 2 131 ? 14.551 8.807 -10.131 1.00 14.99 ? 129 VAL B CB 1 ATOM 2569 C CG1 . VAL B 2 131 ? 13.289 8.617 -9.319 1.00 13.63 ? 129 VAL B CG1 1 ATOM 2570 C CG2 . VAL B 2 131 ? 15.781 8.828 -9.210 1.00 11.68 ? 129 VAL B CG2 1 ATOM 2571 N N . ARG B 2 132 ? 12.707 6.708 -12.141 1.00 20.30 ? 130 ARG B N 1 ATOM 2572 C CA . ARG B 2 132 ? 11.589 6.595 -13.082 1.00 20.05 ? 130 ARG B CA 1 ATOM 2573 C C . ARG B 2 132 ? 10.274 6.307 -12.362 1.00 17.07 ? 130 ARG B C 1 ATOM 2574 O O . ARG B 2 132 ? 10.241 5.647 -11.327 1.00 13.86 ? 130 ARG B O 1 ATOM 2575 C CB . ARG B 2 132 ? 11.894 5.534 -14.148 1.00 17.35 ? 130 ARG B CB 1 ATOM 2576 C CG . ARG B 2 132 ? 13.076 5.940 -15.047 1.00 30.72 ? 130 ARG B CG 1 ATOM 2577 C CD . ARG B 2 132 ? 13.467 4.904 -16.096 1.00 29.56 ? 130 ARG B CD 1 ATOM 2578 N NE . ARG B 2 132 ? 13.274 3.536 -15.623 1.00 38.65 ? 130 ARG B NE 1 ATOM 2579 C CZ . ARG B 2 132 ? 13.626 2.453 -16.313 1.00 64.78 ? 130 ARG B CZ 1 ATOM 2580 N NH1 . ARG B 2 132 ? 14.204 2.585 -17.502 1.00 75.45 ? 130 ARG B NH1 1 ATOM 2581 N NH2 . ARG B 2 132 ? 13.416 1.237 -15.815 1.00 41.36 ? 130 ARG B NH2 1 ATOM 2582 N N . TRP B 2 133 ? 9.184 6.801 -12.927 1.00 17.52 ? 131 TRP B N 1 ATOM 2583 C CA . TRP B 2 133 ? 7.871 6.594 -12.343 1.00 18.01 ? 131 TRP B CA 1 ATOM 2584 C C . TRP B 2 133 ? 7.061 5.560 -13.101 1.00 19.81 ? 131 TRP B C 1 ATOM 2585 O O . TRP B 2 133 ? 7.124 5.494 -14.326 1.00 20.59 ? 131 TRP B O 1 ATOM 2586 C CB . TRP B 2 133 ? 7.097 7.908 -12.312 1.00 9.34 ? 131 TRP B CB 1 ATOM 2587 C CG . TRP B 2 133 ? 7.325 8.746 -11.094 1.00 21.40 ? 131 TRP B CG 1 ATOM 2588 C CD1 . TRP B 2 133 ? 8.037 9.922 -11.023 1.00 12.66 ? 131 TRP B CD1 1 ATOM 2589 C CD2 . TRP B 2 133 ? 6.823 8.502 -9.772 1.00 14.42 ? 131 TRP B CD2 1 ATOM 2590 N NE1 . TRP B 2 133 ? 8.019 10.408 -9.737 1.00 9.12 ? 131 TRP B NE1 1 ATOM 2591 C CE2 . TRP B 2 133 ? 7.279 9.560 -8.950 1.00 19.33 ? 131 TRP B CE2 1 ATOM 2592 C CE3 . TRP B 2 133 ? 6.042 7.492 -9.202 1.00 15.04 ? 131 TRP B CE3 1 ATOM 2593 C CZ2 . TRP B 2 133 ? 6.966 9.637 -7.588 1.00 13.81 ? 131 TRP B CZ2 1 ATOM 2594 C CZ3 . TRP B 2 133 ? 5.745 7.561 -7.852 1.00 19.02 ? 131 TRP B CZ3 1 ATOM 2595 C CH2 . TRP B 2 133 ? 6.202 8.636 -7.059 1.00 16.36 ? 131 TRP B CH2 1 ATOM 2596 N N . PHE B 2 134 ? 6.278 4.776 -12.363 1.00 16.83 ? 132 PHE B N 1 ATOM 2597 C CA . PHE B 2 134 ? 5.407 3.783 -12.974 1.00 20.53 ? 132 PHE B CA 1 ATOM 2598 C C . PHE B 2 134 ? 3.990 3.878 -12.418 1.00 23.65 ? 132 PHE B C 1 ATOM 2599 O O . PHE B 2 134 ? 3.792 4.068 -11.224 1.00 20.65 ? 132 PHE B O 1 ATOM 2600 C CB . PHE B 2 134 ? 5.959 2.371 -12.723 1.00 20.64 ? 132 PHE B CB 1 ATOM 2601 C CG . PHE B 2 134 ? 7.264 2.103 -13.412 1.00 22.74 ? 132 PHE B CG 1 ATOM 2602 C CD1 . PHE B 2 134 ? 8.464 2.545 -12.859 1.00 19.00 ? 132 PHE B CD1 1 ATOM 2603 C CD2 . PHE B 2 134 ? 7.295 1.428 -14.621 1.00 19.86 ? 132 PHE B CD2 1 ATOM 2604 C CE1 . PHE B 2 134 ? 9.669 2.318 -13.497 1.00 17.31 ? 132 PHE B CE1 1 ATOM 2605 C CE2 . PHE B 2 134 ? 8.503 1.194 -15.274 1.00 23.13 ? 132 PHE B CE2 1 ATOM 2606 C CZ . PHE B 2 134 ? 9.695 1.642 -14.709 1.00 18.25 ? 132 PHE B CZ 1 ATOM 2607 N N . ARG B 2 135 ? 3.007 3.737 -13.297 1.00 22.94 ? 133 ARG B N 1 ATOM 2608 C CA . ARG B 2 135 ? 1.612 3.659 -12.895 1.00 30.06 ? 133 ARG B CA 1 ATOM 2609 C C . ARG B 2 135 ? 1.072 2.308 -13.330 1.00 28.05 ? 133 ARG B C 1 ATOM 2610 O O . ARG B 2 135 ? 1.018 2.012 -14.528 1.00 30.93 ? 133 ARG B O 1 ATOM 2611 C CB . ARG B 2 135 ? 0.776 4.792 -13.487 1.00 25.48 ? 133 ARG B CB 1 ATOM 2612 C CG . ARG B 2 135 ? -0.673 4.738 -13.051 1.00 27.42 ? 133 ARG B CG 1 ATOM 2613 C CD . ARG B 2 135 ? -1.531 5.673 -13.860 1.00 32.27 ? 133 ARG B CD 1 ATOM 2614 N NE . ARG B 2 135 ? -1.222 7.069 -13.573 1.00 40.46 ? 133 ARG B NE 1 ATOM 2615 C CZ . ARG B 2 135 ? -0.519 7.850 -14.388 1.00 48.25 ? 133 ARG B CZ 1 ATOM 2616 N NH1 . ARG B 2 135 ? -0.042 7.355 -15.524 1.00 49.33 ? 133 ARG B NH1 1 ATOM 2617 N NH2 . ARG B 2 135 ? -0.275 9.116 -14.065 1.00 44.01 ? 133 ARG B NH2 1 ATOM 2618 N N . ASN B 2 136 ? 0.692 1.483 -12.363 1.00 41.93 ? 134 ASN B N 1 ATOM 2619 C CA . ASN B 2 136 ? 0.247 0.117 -12.641 1.00 42.10 ? 134 ASN B CA 1 ATOM 2620 C C . ASN B 2 136 ? 1.194 -0.673 -13.566 1.00 39.81 ? 134 ASN B C 1 ATOM 2621 O O . ASN B 2 136 ? 0.749 -1.338 -14.501 1.00 37.30 ? 134 ASN B O 1 ATOM 2622 C CB . ASN B 2 136 ? -1.162 0.152 -13.262 1.00 35.47 ? 134 ASN B CB 1 ATOM 2623 C CG . ASN B 2 136 ? -2.203 0.745 -12.321 1.00 37.06 ? 134 ASN B CG 1 ATOM 2624 O OD1 . ASN B 2 136 ? -2.165 0.535 -11.104 1.00 44.52 ? 134 ASN B OD1 1 ATOM 2625 N ND2 . ASN B 2 136 ? -3.129 1.512 -12.883 1.00 37.92 ? 134 ASN B ND2 1 ATOM 2626 N N . GLY B 2 137 ? 2.501 -0.570 -13.335 1.00 37.59 ? 135 GLY B N 1 ATOM 2627 C CA . GLY B 2 137 ? 3.446 -1.371 -14.098 1.00 29.26 ? 135 GLY B CA 1 ATOM 2628 C C . GLY B 2 137 ? 3.900 -0.797 -15.423 1.00 38.32 ? 135 GLY B C 1 ATOM 2629 O O . GLY B 2 137 ? 4.710 -1.404 -16.124 1.00 43.40 ? 135 GLY B O 1 ATOM 2630 N N . GLN B 2 138 ? 3.364 0.365 -15.776 1.00 35.04 ? 136 GLN B N 1 ATOM 2631 C CA . GLN B 2 138 ? 3.730 1.056 -17.012 1.00 38.82 ? 136 GLN B CA 1 ATOM 2632 C C . GLN B 2 138 ? 4.553 2.292 -16.702 1.00 28.65 ? 136 GLN B C 1 ATOM 2633 O O . GLN B 2 138 ? 4.192 3.057 -15.811 1.00 25.77 ? 136 GLN B O 1 ATOM 2634 C CB . GLN B 2 138 ? 2.485 1.454 -17.812 1.00 46.86 ? 136 GLN B CB 1 ATOM 2635 C CG . GLN B 2 138 ? 1.552 0.309 -18.144 1.00 53.25 ? 136 GLN B CG 1 ATOM 2636 C CD . GLN B 2 138 ? 2.176 -0.656 -19.129 1.00 57.01 ? 136 GLN B CD 1 ATOM 2637 O OE1 . GLN B 2 138 ? 3.074 -0.284 -19.889 1.00 43.88 ? 136 GLN B OE1 1 ATOM 2638 N NE2 . GLN B 2 138 ? 1.711 -1.903 -19.120 1.00 63.17 ? 136 GLN B NE2 1 ATOM 2639 N N . GLU B 2 139 ? 5.679 2.475 -17.386 1.00 24.99 ? 137 GLU B N 1 ATOM 2640 C CA . GLU B 2 139 ? 6.488 3.650 -17.090 1.00 30.60 ? 137 GLU B CA 1 ATOM 2641 C C . GLU B 2 139 ? 5.690 4.886 -17.499 1.00 29.87 ? 137 GLU B C 1 ATOM 2642 O O . GLU B 2 139 ? 5.121 4.959 -18.591 1.00 21.71 ? 137 GLU B O 1 ATOM 2643 C CB . GLU B 2 139 ? 7.865 3.643 -17.760 1.00 19.97 ? 137 GLU B CB 1 ATOM 2644 C CG . GLU B 2 139 ? 8.652 4.885 -17.338 1.00 17.07 ? 137 GLU B CG 1 ATOM 2645 C CD . GLU B 2 139 ? 10.076 4.936 -17.867 1.00 38.13 ? 137 GLU B CD 1 ATOM 2646 O OE1 . GLU B 2 139 ? 10.506 3.971 -18.538 1.00 34.98 ? 137 GLU B OE1 1 ATOM 2647 O OE2 . GLU B 2 139 ? 10.763 5.957 -17.607 1.00 28.79 ? 137 GLU B OE2 1 ATOM 2648 N N . GLU B 2 140 ? 5.670 5.865 -16.610 1.00 23.57 ? 138 GLU B N 1 ATOM 2649 C CA . GLU B 2 140 ? 5.018 7.112 -16.916 1.00 28.31 ? 138 GLU B CA 1 ATOM 2650 C C . GLU B 2 140 ? 6.111 8.130 -17.200 1.00 30.17 ? 138 GLU B C 1 ATOM 2651 O O . GLU B 2 140 ? 6.916 8.476 -16.326 1.00 18.98 ? 138 GLU B O 1 ATOM 2652 C CB . GLU B 2 140 ? 4.150 7.538 -15.736 1.00 23.50 ? 138 GLU B CB 1 ATOM 2653 C CG . GLU B 2 140 ? 3.353 8.773 -15.991 1.00 41.04 ? 138 GLU B CG 1 ATOM 2654 C CD . GLU B 2 140 ? 2.477 8.600 -17.208 1.00 51.86 ? 138 GLU B CD 1 ATOM 2655 O OE1 . GLU B 2 140 ? 2.799 9.197 -18.259 1.00 45.27 ? 138 GLU B OE1 1 ATOM 2656 O OE2 . GLU B 2 140 ? 1.491 7.831 -17.119 1.00 50.13 ? 138 GLU B OE2 1 ATOM 2657 N N . LYS B 2 141 ? 6.160 8.571 -18.453 1.00 25.22 ? 139 LYS B N 1 ATOM 2658 C CA . LYS B 2 141 ? 7.179 9.524 -18.876 1.00 29.95 ? 139 LYS B CA 1 ATOM 2659 C C . LYS B 2 141 ? 6.688 10.966 -19.038 1.00 30.33 ? 139 LYS B C 1 ATOM 2660 O O . LYS B 2 141 ? 7.496 11.886 -19.194 1.00 27.03 ? 139 LYS B O 1 ATOM 2661 C CB . LYS B 2 141 ? 7.802 9.042 -20.188 1.00 26.10 ? 139 LYS B CB 1 ATOM 2662 C CG . LYS B 2 141 ? 8.705 7.820 -20.024 1.00 24.38 ? 139 LYS B CG 1 ATOM 2663 C CD . LYS B 2 141 ? 9.395 7.454 -21.336 1.00 33.98 ? 139 LYS B CD 1 ATOM 2664 C CE . LYS B 2 141 ? 10.354 6.280 -21.163 1.00 34.94 ? 139 LYS B CE 1 ATOM 2665 N NZ . LYS B 2 141 ? 10.886 5.802 -22.476 1.00 32.04 ? 139 LYS B NZ 1 ATOM 2666 N N . THR B 2 142 ? 5.375 11.171 -18.999 1.00 23.93 ? 140 THR B N 1 ATOM 2667 C CA . THR B 2 142 ? 4.831 12.522 -19.120 1.00 22.20 ? 140 THR B CA 1 ATOM 2668 C C . THR B 2 142 ? 4.591 13.152 -17.753 1.00 21.94 ? 140 THR B C 1 ATOM 2669 O O . THR B 2 142 ? 4.289 12.457 -16.779 1.00 26.76 ? 140 THR B O 1 ATOM 2670 C CB . THR B 2 142 ? 3.519 12.538 -19.910 1.00 30.46 ? 140 THR B CB 1 ATOM 2671 O OG1 . THR B 2 142 ? 2.493 11.904 -19.135 1.00 43.49 ? 140 THR B OG1 1 ATOM 2672 C CG2 . THR B 2 142 ? 3.689 11.806 -21.232 1.00 20.27 ? 140 THR B CG2 1 ATOM 2673 N N . GLY B 2 143 ? 4.721 14.470 -17.681 1.00 18.29 ? 141 GLY B N 1 ATOM 2674 C CA . GLY B 2 143 ? 4.457 15.178 -16.447 1.00 19.75 ? 141 GLY B CA 1 ATOM 2675 C C . GLY B 2 143 ? 5.471 14.928 -15.347 1.00 20.62 ? 141 GLY B C 1 ATOM 2676 O O . GLY B 2 143 ? 5.143 15.056 -14.169 1.00 24.04 ? 141 GLY B O 1 ATOM 2677 N N . VAL B 2 144 ? 6.714 14.624 -15.715 1.00 18.76 ? 142 VAL B N 1 ATOM 2678 C CA . VAL B 2 144 ? 7.749 14.392 -14.709 1.00 19.68 ? 142 VAL B CA 1 ATOM 2679 C C . VAL B 2 144 ? 8.661 15.609 -14.653 1.00 14.43 ? 142 VAL B C 1 ATOM 2680 O O . VAL B 2 144 ? 9.155 16.090 -15.670 1.00 17.93 ? 142 VAL B O 1 ATOM 2681 C CB . VAL B 2 144 ? 8.586 13.124 -15.002 1.00 24.27 ? 142 VAL B CB 1 ATOM 2682 C CG1 . VAL B 2 144 ? 9.710 12.984 -13.979 1.00 13.15 ? 142 VAL B CG1 1 ATOM 2683 C CG2 . VAL B 2 144 ? 7.698 11.892 -14.984 1.00 18.97 ? 142 VAL B CG2 1 ATOM 2684 N N . VAL B 2 145 ? 8.804 16.150 -13.452 1.00 11.13 ? 143 VAL B N 1 ATOM 2685 C CA . VAL B 2 145 ? 9.653 17.297 -13.217 1.00 13.47 ? 143 VAL B CA 1 ATOM 2686 C C . VAL B 2 145 ? 10.535 16.996 -12.004 1.00 12.78 ? 143 VAL B C 1 ATOM 2687 O O . VAL B 2 145 ? 10.157 16.218 -11.132 1.00 15.51 ? 143 VAL B O 1 ATOM 2688 C CB . VAL B 2 145 ? 8.808 18.566 -13.012 1.00 12.78 ? 143 VAL B CB 1 ATOM 2689 C CG1 . VAL B 2 145 ? 8.037 18.481 -11.702 1.00 19.01 ? 143 VAL B CG1 1 ATOM 2690 C CG2 . VAL B 2 145 ? 9.668 19.790 -13.042 1.00 12.52 ? 143 VAL B CG2 1 ATOM 2691 N N . SER B 2 146 ? 11.739 17.555 -11.982 1.00 14.64 ? 144 SER B N 1 ATOM 2692 C CA . SER B 2 146 ? 12.668 17.284 -10.891 1.00 16.69 ? 144 SER B CA 1 ATOM 2693 C C . SER B 2 146 ? 13.439 18.507 -10.394 1.00 15.76 ? 144 SER B C 1 ATOM 2694 O O . SER B 2 146 ? 13.552 19.514 -11.085 1.00 13.94 ? 144 SER B O 1 ATOM 2695 C CB . SER B 2 146 ? 13.667 16.204 -11.317 1.00 10.66 ? 144 SER B CB 1 ATOM 2696 O OG . SER B 2 146 ? 14.624 15.988 -10.308 1.00 9.94 ? 144 SER B OG 1 ATOM 2697 N N . THR B 2 147 ? 13.996 18.388 -9.199 1.00 10.08 ? 145 THR B N 1 ATOM 2698 C CA . THR B 2 147 ? 14.930 19.373 -8.694 1.00 11.39 ? 145 THR B CA 1 ATOM 2699 C C . THR B 2 147 ? 16.239 19.255 -9.465 1.00 16.53 ? 145 THR B C 1 ATOM 2700 O O . THR B 2 147 ? 17.069 20.164 -9.445 1.00 13.47 ? 145 THR B O 1 ATOM 2701 C CB . THR B 2 147 ? 15.220 19.159 -7.206 1.00 13.87 ? 145 THR B CB 1 ATOM 2702 O OG1 . THR B 2 147 ? 15.652 17.802 -7.011 1.00 11.67 ? 145 THR B OG1 1 ATOM 2703 C CG2 . THR B 2 147 ? 13.972 19.414 -6.373 1.00 6.95 ? 145 THR B CG2 1 ATOM 2704 N N . GLY B 2 148 ? 16.437 18.112 -10.120 1.00 12.70 ? 146 GLY B N 1 ATOM 2705 C CA . GLY B 2 148 ? 17.742 17.779 -10.659 1.00 7.26 ? 146 GLY B CA 1 ATOM 2706 C C . GLY B 2 148 ? 18.611 17.200 -9.549 1.00 12.95 ? 146 GLY B C 1 ATOM 2707 O O . GLY B 2 148 ? 18.132 16.955 -8.436 1.00 12.12 ? 146 GLY B O 1 ATOM 2708 N N . LEU B 2 149 ? 19.888 16.974 -9.841 1.00 9.37 ? 147 LEU B N 1 ATOM 2709 C CA . LEU B 2 149 ? 20.802 16.400 -8.857 1.00 9.01 ? 147 LEU B CA 1 ATOM 2710 C C . LEU B 2 149 ? 21.309 17.487 -7.912 1.00 14.09 ? 147 LEU B C 1 ATOM 2711 O O . LEU B 2 149 ? 21.866 18.499 -8.342 1.00 14.54 ? 147 LEU B O 1 ATOM 2712 C CB . LEU B 2 149 ? 21.979 15.699 -9.538 1.00 10.52 ? 147 LEU B CB 1 ATOM 2713 C CG . LEU B 2 149 ? 22.923 15.000 -8.562 1.00 16.40 ? 147 LEU B CG 1 ATOM 2714 C CD1 . LEU B 2 149 ? 22.164 13.872 -7.874 1.00 8.02 ? 147 LEU B CD1 1 ATOM 2715 C CD2 . LEU B 2 149 ? 24.166 14.468 -9.264 1.00 17.18 ? 147 LEU B CD2 1 ATOM 2716 N N . ILE B 2 150 ? 21.083 17.292 -6.624 1.00 11.71 ? 148 ILE B N 1 ATOM 2717 C CA . ILE B 2 150 ? 21.508 18.263 -5.626 1.00 12.83 ? 148 ILE B CA 1 ATOM 2718 C C . ILE B 2 150 ? 22.670 17.743 -4.775 1.00 14.08 ? 148 ILE B C 1 ATOM 2719 O O . ILE B 2 150 ? 22.556 16.697 -4.130 1.00 10.52 ? 148 ILE B O 1 ATOM 2720 C CB . ILE B 2 150 ? 20.333 18.623 -4.716 1.00 8.90 ? 148 ILE B CB 1 ATOM 2721 C CG1 . ILE B 2 150 ? 19.185 19.193 -5.542 1.00 12.64 ? 148 ILE B CG1 1 ATOM 2722 C CG2 . ILE B 2 150 ? 20.764 19.601 -3.638 1.00 16.39 ? 148 ILE B CG2 1 ATOM 2723 C CD1 . ILE B 2 150 ? 17.920 19.403 -4.735 1.00 14.37 ? 148 ILE B CD1 1 ATOM 2724 N N . GLN B 2 151 ? 23.782 18.468 -4.770 1.00 15.97 ? 149 GLN B N 1 ATOM 2725 C CA . GLN B 2 151 ? 24.879 18.148 -3.870 1.00 13.62 ? 149 GLN B CA 1 ATOM 2726 C C . GLN B 2 151 ? 24.559 18.748 -2.493 1.00 19.77 ? 149 GLN B C 1 ATOM 2727 O O . GLN B 2 151 ? 24.138 19.896 -2.401 1.00 16.74 ? 149 GLN B O 1 ATOM 2728 C CB . GLN B 2 151 ? 26.205 18.675 -4.447 1.00 17.79 ? 149 GLN B CB 1 ATOM 2729 C CG . GLN B 2 151 ? 27.387 17.703 -4.325 1.00 23.50 ? 149 GLN B CG 1 ATOM 2730 C CD . GLN B 2 151 ? 28.560 18.042 -5.250 1.00 37.96 ? 149 GLN B CD 1 ATOM 2731 O OE1 . GLN B 2 151 ? 28.642 19.142 -5.798 1.00 31.48 ? 149 GLN B OE1 1 ATOM 2732 N NE2 . GLN B 2 151 ? 29.488 17.093 -5.401 1.00 28.97 ? 149 GLN B NE2 1 ATOM 2733 N N . ASN B 2 152 ? 24.739 17.971 -1.427 1.00 11.79 ? 150 ASN B N 1 ATOM 2734 C CA . ASN B 2 152 ? 24.474 18.467 -0.079 1.00 9.47 ? 150 ASN B CA 1 ATOM 2735 C C . ASN B 2 152 ? 25.712 19.056 0.580 1.00 11.40 ? 150 ASN B C 1 ATOM 2736 O O . ASN B 2 152 ? 25.622 19.679 1.635 1.00 12.56 ? 150 ASN B O 1 ATOM 2737 C CB . ASN B 2 152 ? 23.909 17.359 0.809 1.00 11.49 ? 150 ASN B CB 1 ATOM 2738 C CG . ASN B 2 152 ? 22.510 16.942 0.404 1.00 18.46 ? 150 ASN B CG 1 ATOM 2739 O OD1 . ASN B 2 152 ? 21.672 17.773 0.026 1.00 13.14 ? 150 ASN B OD1 1 ATOM 2740 N ND2 . ASN B 2 152 ? 22.255 15.642 0.458 1.00 14.48 ? 150 ASN B ND2 1 ATOM 2741 N N . GLY B 2 153 ? 26.866 18.852 -0.050 1.00 10.99 ? 151 GLY B N 1 ATOM 2742 C CA . GLY B 2 153 ? 28.123 19.406 0.422 1.00 13.85 ? 151 GLY B CA 1 ATOM 2743 C C . GLY B 2 153 ? 28.853 18.527 1.430 1.00 15.87 ? 151 GLY B C 1 ATOM 2744 O O . GLY B 2 153 ? 29.941 18.876 1.904 1.00 14.80 ? 151 GLY B O 1 ATOM 2745 N N . ASP B 2 154 ? 28.251 17.390 1.764 1.00 12.56 ? 152 ASP B N 1 ATOM 2746 C CA . ASP B 2 154 ? 28.784 16.501 2.798 1.00 13.85 ? 152 ASP B CA 1 ATOM 2747 C C . ASP B 2 154 ? 28.990 15.087 2.258 1.00 10.41 ? 152 ASP B C 1 ATOM 2748 O O . ASP B 2 154 ? 28.823 14.100 2.984 1.00 12.75 ? 152 ASP B O 1 ATOM 2749 C CB . ASP B 2 154 ? 27.868 16.484 4.035 1.00 13.17 ? 152 ASP B CB 1 ATOM 2750 C CG . ASP B 2 154 ? 26.469 15.904 3.747 1.00 16.38 ? 152 ASP B CG 1 ATOM 2751 O OD1 . ASP B 2 154 ? 26.122 15.661 2.567 1.00 12.29 ? 152 ASP B OD1 1 ATOM 2752 O OD2 . ASP B 2 154 ? 25.719 15.664 4.721 1.00 20.07 ? 152 ASP B OD2 1 ATOM 2753 N N . TRP B 2 155 ? 29.322 15.001 0.974 1.00 7.59 ? 153 TRP B N 1 ATOM 2754 C CA . TRP B 2 155 ? 29.522 13.714 0.296 1.00 13.30 ? 153 TRP B CA 1 ATOM 2755 C C . TRP B 2 155 ? 28.249 12.884 0.173 1.00 13.29 ? 153 TRP B C 1 ATOM 2756 O O . TRP B 2 155 ? 28.298 11.658 0.124 1.00 16.98 ? 153 TRP B O 1 ATOM 2757 C CB . TRP B 2 155 ? 30.629 12.902 0.974 1.00 8.47 ? 153 TRP B CB 1 ATOM 2758 C CG . TRP B 2 155 ? 31.982 13.506 0.752 1.00 13.78 ? 153 TRP B CG 1 ATOM 2759 C CD1 . TRP B 2 155 ? 32.516 14.591 1.391 1.00 9.92 ? 153 TRP B CD1 1 ATOM 2760 C CD2 . TRP B 2 155 ? 32.961 13.089 -0.216 1.00 11.47 ? 153 TRP B CD2 1 ATOM 2761 N NE1 . TRP B 2 155 ? 33.775 14.858 0.899 1.00 11.53 ? 153 TRP B NE1 1 ATOM 2762 C CE2 . TRP B 2 155 ? 34.073 13.950 -0.083 1.00 15.19 ? 153 TRP B CE2 1 ATOM 2763 C CE3 . TRP B 2 155 ? 33.008 12.070 -1.166 1.00 8.79 ? 153 TRP B CE3 1 ATOM 2764 C CZ2 . TRP B 2 155 ? 35.225 13.811 -0.862 1.00 14.64 ? 153 TRP B CZ2 1 ATOM 2765 C CZ3 . TRP B 2 155 ? 34.153 11.933 -1.942 1.00 12.25 ? 153 TRP B CZ3 1 ATOM 2766 C CH2 . TRP B 2 155 ? 35.245 12.799 -1.785 1.00 13.83 ? 153 TRP B CH2 1 ATOM 2767 N N . THR B 2 156 ? 27.110 13.564 0.128 1.00 8.96 ? 154 THR B N 1 ATOM 2768 C CA . THR B 2 156 ? 25.854 12.918 -0.223 1.00 12.41 ? 154 THR B CA 1 ATOM 2769 C C . THR B 2 156 ? 25.094 13.795 -1.214 1.00 11.04 ? 154 THR B C 1 ATOM 2770 O O . THR B 2 156 ? 25.285 15.007 -1.276 1.00 11.47 ? 154 THR B O 1 ATOM 2771 C CB . THR B 2 156 ? 24.931 12.643 1.004 1.00 8.91 ? 154 THR B CB 1 ATOM 2772 O OG1 . THR B 2 156 ? 24.501 13.888 1.570 1.00 15.32 ? 154 THR B OG1 1 ATOM 2773 C CG2 . THR B 2 156 ? 25.631 11.836 2.068 1.00 10.29 ? 154 THR B CG2 1 ATOM 2774 N N . PHE B 2 157 ? 24.216 13.162 -1.972 1.00 9.19 ? 155 PHE B N 1 ATOM 2775 C CA . PHE B 2 157 ? 23.370 13.866 -2.897 1.00 8.98 ? 155 PHE B CA 1 ATOM 2776 C C . PHE B 2 157 ? 21.925 13.626 -2.471 1.00 15.49 ? 155 PHE B C 1 ATOM 2777 O O . PHE B 2 157 ? 21.641 12.751 -1.650 1.00 14.16 ? 155 PHE B O 1 ATOM 2778 C CB . PHE B 2 157 ? 23.555 13.356 -4.327 1.00 8.86 ? 155 PHE B CB 1 ATOM 2779 C CG . PHE B 2 157 ? 24.899 13.649 -4.924 1.00 14.70 ? 155 PHE B CG 1 ATOM 2780 C CD1 . PHE B 2 157 ? 25.956 12.755 -4.764 1.00 15.38 ? 155 PHE B CD1 1 ATOM 2781 C CD2 . PHE B 2 157 ? 25.105 14.797 -5.674 1.00 10.31 ? 155 PHE B CD2 1 ATOM 2782 C CE1 . PHE B 2 157 ? 27.211 13.012 -5.342 1.00 21.45 ? 155 PHE B CE1 1 ATOM 2783 C CE2 . PHE B 2 157 ? 26.349 15.064 -6.251 1.00 18.30 ? 155 PHE B CE2 1 ATOM 2784 C CZ . PHE B 2 157 ? 27.406 14.171 -6.084 1.00 13.62 ? 155 PHE B CZ 1 ATOM 2785 N N . GLN B 2 158 ? 21.022 14.402 -3.050 1.00 8.65 ? 156 GLN B N 1 ATOM 2786 C CA . GLN B 2 158 ? 19.602 14.114 -2.986 1.00 14.99 ? 156 GLN B CA 1 ATOM 2787 C C . GLN B 2 158 ? 18.980 14.574 -4.286 1.00 10.78 ? 156 GLN B C 1 ATOM 2788 O O . GLN B 2 158 ? 19.596 15.318 -5.048 1.00 12.03 ? 156 GLN B O 1 ATOM 2789 C CB . GLN B 2 158 ? 18.929 14.791 -1.789 1.00 9.73 ? 156 GLN B CB 1 ATOM 2790 C CG . GLN B 2 158 ? 18.983 16.304 -1.818 1.00 8.86 ? 156 GLN B CG 1 ATOM 2791 C CD . GLN B 2 158 ? 18.153 16.917 -0.712 1.00 13.50 ? 156 GLN B CD 1 ATOM 2792 O OE1 . GLN B 2 158 ? 16.924 16.822 -0.724 1.00 16.55 ? 156 GLN B OE1 1 ATOM 2793 N NE2 . GLN B 2 158 ? 18.814 17.509 0.274 1.00 9.83 ? 156 GLN B NE2 1 ATOM 2794 N N . THR B 2 159 ? 17.769 14.109 -4.552 1.00 13.35 ? 157 THR B N 1 ATOM 2795 C CA . THR B 2 159 ? 16.998 14.612 -5.680 1.00 11.75 ? 157 THR B CA 1 ATOM 2796 C C . THR B 2 159 ? 15.509 14.378 -5.458 1.00 13.14 ? 157 THR B C 1 ATOM 2797 O O . THR B 2 159 ? 15.120 13.337 -4.921 1.00 12.05 ? 157 THR B O 1 ATOM 2798 C CB . THR B 2 159 ? 17.465 13.948 -7.004 1.00 11.13 ? 157 THR B CB 1 ATOM 2799 O OG1 . THR B 2 159 ? 16.725 14.489 -8.105 1.00 15.39 ? 157 THR B OG1 1 ATOM 2800 C CG2 . THR B 2 159 ? 17.261 12.433 -6.965 1.00 15.67 ? 157 THR B CG2 1 ATOM 2801 N N . LEU B 2 160 ? 14.670 15.319 -5.885 1.00 9.81 ? 158 LEU B N 1 ATOM 2802 C CA . LEU B 2 160 ? 13.223 15.062 -5.849 1.00 17.18 ? 158 LEU B CA 1 ATOM 2803 C C . LEU B 2 160 ? 12.719 14.856 -7.257 1.00 13.06 ? 158 LEU B C 1 ATOM 2804 O O . LEU B 2 160 ? 12.987 15.659 -8.151 1.00 13.37 ? 158 LEU B O 1 ATOM 2805 C CB . LEU B 2 160 ? 12.441 16.206 -5.197 1.00 11.73 ? 158 LEU B CB 1 ATOM 2806 C CG . LEU B 2 160 ? 12.812 16.674 -3.791 1.00 21.67 ? 158 LEU B CG 1 ATOM 2807 C CD1 . LEU B 2 160 ? 11.727 17.584 -3.260 1.00 11.77 ? 158 LEU B CD1 1 ATOM 2808 C CD2 . LEU B 2 160 ? 13.007 15.501 -2.871 1.00 17.60 ? 158 LEU B CD2 1 ATOM 2809 N N . VAL B 2 161 ? 11.987 13.772 -7.460 1.00 14.38 ? 159 VAL B N 1 ATOM 2810 C CA . VAL B 2 161 ? 11.411 13.522 -8.766 1.00 13.84 ? 159 VAL B CA 1 ATOM 2811 C C . VAL B 2 161 ? 9.906 13.423 -8.621 1.00 25.46 ? 159 VAL B C 1 ATOM 2812 O O . VAL B 2 161 ? 9.358 12.495 -8.009 1.00 23.54 ? 159 VAL B O 1 ATOM 2813 C CB . VAL B 2 161 ? 11.971 12.273 -9.415 1.00 14.87 ? 159 VAL B CB 1 ATOM 2814 C CG1 . VAL B 2 161 ? 11.324 12.076 -10.779 1.00 12.74 ? 159 VAL B CG1 1 ATOM 2815 C CG2 . VAL B 2 161 ? 13.483 12.380 -9.520 1.00 6.76 ? 159 VAL B CG2 1 ATOM 2816 N N . MET B 2 162 ? 9.245 14.397 -9.219 1.00 18.26 ? 160 MET B N 1 ATOM 2817 C CA . MET B 2 162 ? 7.823 14.554 -9.075 1.00 15.51 ? 160 MET B CA 1 ATOM 2818 C C . MET B 2 162 ? 7.040 14.112 -10.292 1.00 20.35 ? 160 MET B C 1 ATOM 2819 O O . MET B 2 162 ? 7.475 14.303 -11.427 1.00 16.13 ? 160 MET B O 1 ATOM 2820 C CB . MET B 2 162 ? 7.586 16.016 -8.746 1.00 19.87 ? 160 MET B CB 1 ATOM 2821 C CG . MET B 2 162 ? 8.311 16.333 -7.449 1.00 19.00 ? 160 MET B CG 1 ATOM 2822 S SD . MET B 2 162 ? 8.586 18.056 -7.156 1.00 37.06 ? 160 MET B SD 1 ATOM 2823 C CE . MET B 2 162 ? 10.104 18.226 -8.108 1.00 21.73 ? 160 MET B CE 1 ATOM 2824 N N . LEU B 2 163 ? 5.881 13.508 -10.046 1.00 18.22 ? 161 LEU B N 1 ATOM 2825 C CA . LEU B 2 163 ? 5.009 13.091 -11.127 1.00 14.59 ? 161 LEU B CA 1 ATOM 2826 C C . LEU B 2 163 ? 3.713 13.879 -10.997 1.00 15.43 ? 161 LEU B C 1 ATOM 2827 O O . LEU B 2 163 ? 3.006 13.733 -10.003 1.00 12.72 ? 161 LEU B O 1 ATOM 2828 C CB . LEU B 2 163 ? 4.733 11.588 -11.051 1.00 11.14 ? 161 LEU B CB 1 ATOM 2829 C CG . LEU B 2 163 ? 3.732 11.027 -12.054 1.00 16.16 ? 161 LEU B CG 1 ATOM 2830 C CD1 . LEU B 2 163 ? 4.256 11.155 -13.481 1.00 11.56 ? 161 LEU B CD1 1 ATOM 2831 C CD2 . LEU B 2 163 ? 3.321 9.601 -11.708 1.00 16.44 ? 161 LEU B CD2 1 ATOM 2832 N N . GLU B 2 164 ? 3.389 14.691 -12.003 1.00 16.65 ? 162 GLU B N 1 ATOM 2833 C CA . GLU B 2 164 ? 2.099 15.379 -12.020 1.00 21.15 ? 162 GLU B CA 1 ATOM 2834 C C . GLU B 2 164 ? 1.053 14.390 -12.502 1.00 15.97 ? 162 GLU B C 1 ATOM 2835 O O . GLU B 2 164 ? 1.111 13.888 -13.630 1.00 20.60 ? 162 GLU B O 1 ATOM 2836 C CB . GLU B 2 164 ? 2.136 16.617 -12.914 1.00 23.30 ? 162 GLU B CB 1 ATOM 2837 C CG . GLU B 2 164 ? 3.224 17.609 -12.514 1.00 37.47 ? 162 GLU B CG 1 ATOM 2838 C CD . GLU B 2 164 ? 3.515 18.661 -13.573 1.00 46.32 ? 162 GLU B CD 1 ATOM 2839 O OE1 . GLU B 2 164 ? 4.709 18.952 -13.798 1.00 43.21 ? 162 GLU B OE1 1 ATOM 2840 O OE2 . GLU B 2 164 ? 2.558 19.212 -14.160 1.00 54.28 ? 162 GLU B OE2 1 ATOM 2841 N N . THR B 2 165 ? 0.094 14.118 -11.634 1.00 14.42 ? 163 THR B N 1 ATOM 2842 C CA . THR B 2 165 ? -0.908 13.099 -11.898 1.00 20.66 ? 163 THR B CA 1 ATOM 2843 C C . THR B 2 165 ? -2.082 13.325 -10.967 1.00 20.24 ? 163 THR B C 1 ATOM 2844 O O . THR B 2 165 ? -1.929 13.939 -9.917 1.00 20.67 ? 163 THR B O 1 ATOM 2845 C CB . THR B 2 165 ? -0.337 11.673 -11.730 1.00 20.90 ? 163 THR B CB 1 ATOM 2846 O OG1 . THR B 2 165 ? -1.306 10.710 -12.158 1.00 30.97 ? 163 THR B OG1 1 ATOM 2847 C CG2 . THR B 2 165 ? 0.032 11.412 -10.295 1.00 13.60 ? 163 THR B CG2 1 ATOM 2848 N N . VAL B 2 166 ? -3.257 12.870 -11.382 1.00 22.06 ? 164 VAL B N 1 ATOM 2849 C CA . VAL B 2 166 ? -4.441 12.869 -10.532 1.00 15.97 ? 164 VAL B CA 1 ATOM 2850 C C . VAL B 2 166 ? -4.705 11.435 -10.084 1.00 24.55 ? 164 VAL B C 1 ATOM 2851 O O . VAL B 2 166 ? -5.222 10.627 -10.853 1.00 26.57 ? 164 VAL B O 1 ATOM 2852 C CB . VAL B 2 166 ? -5.670 13.412 -11.269 1.00 20.77 ? 164 VAL B CB 1 ATOM 2853 C CG1 . VAL B 2 166 ? -6.860 13.462 -10.326 1.00 18.63 ? 164 VAL B CG1 1 ATOM 2854 C CG2 . VAL B 2 166 ? -5.377 14.782 -11.847 1.00 17.45 ? 164 VAL B CG2 1 ATOM 2855 N N . PRO B 2 167 ? -4.312 11.107 -8.841 1.00 24.50 ? 165 PRO B N 1 ATOM 2856 C CA . PRO B 2 167 ? -4.447 9.734 -8.345 1.00 23.78 ? 165 PRO B CA 1 ATOM 2857 C C . PRO B 2 167 ? -5.892 9.255 -8.310 1.00 31.13 ? 165 PRO B C 1 ATOM 2858 O O . PRO B 2 167 ? -6.755 9.937 -7.771 1.00 20.08 ? 165 PRO B O 1 ATOM 2859 C CB . PRO B 2 167 ? -3.917 9.832 -6.914 1.00 22.69 ? 165 PRO B CB 1 ATOM 2860 C CG . PRO B 2 167 ? -3.022 11.033 -6.918 1.00 26.24 ? 165 PRO B CG 1 ATOM 2861 C CD . PRO B 2 167 ? -3.700 11.999 -7.840 1.00 19.13 ? 165 PRO B CD 1 ATOM 2862 N N . ARG B 2 168 ? -6.137 8.059 -8.821 1.00 31.92 ? 166 ARG B N 1 ATOM 2863 C CA . ARG B 2 168 ? -7.464 7.488 -8.738 1.00 37.20 ? 166 ARG B CA 1 ATOM 2864 C C . ARG B 2 168 ? -7.403 6.313 -7.768 1.00 36.22 ? 166 ARG B C 1 ATOM 2865 O O . ARG B 2 168 ? -6.373 5.649 -7.667 1.00 27.78 ? 166 ARG B O 1 ATOM 2866 C CB . ARG B 2 168 ? -7.935 7.058 -10.129 1.00 42.43 ? 166 ARG B CB 1 ATOM 2867 C CG . ARG B 2 168 ? -8.387 8.215 -11.017 1.00 35.47 ? 166 ARG B CG 1 ATOM 2868 C CD . ARG B 2 168 ? -8.635 7.733 -12.433 1.00 39.69 ? 166 ARG B CD 1 ATOM 2869 N NE . ARG B 2 168 ? -9.402 8.674 -13.249 1.00 35.95 ? 166 ARG B NE 1 ATOM 2870 C CZ . ARG B 2 168 ? -8.876 9.704 -13.913 1.00 28.95 ? 166 ARG B CZ 1 ATOM 2871 N NH1 . ARG B 2 168 ? -7.576 9.959 -13.852 1.00 32.55 ? 166 ARG B NH1 1 ATOM 2872 N NH2 . ARG B 2 168 ? -9.659 10.494 -14.634 1.00 36.62 ? 166 ARG B NH2 1 ATOM 2873 N N . SER B 2 169 ? -8.498 6.067 -7.056 1.00 35.44 ? 167 SER B N 1 ATOM 2874 C CA . SER B 2 169 ? -8.569 4.973 -6.088 1.00 43.48 ? 167 SER B CA 1 ATOM 2875 C C . SER B 2 169 ? -8.194 3.654 -6.754 1.00 33.26 ? 167 SER B C 1 ATOM 2876 O O . SER B 2 169 ? -8.654 3.355 -7.854 1.00 36.78 ? 167 SER B O 1 ATOM 2877 C CB . SER B 2 169 ? -9.960 4.879 -5.462 1.00 46.94 ? 167 SER B CB 1 ATOM 2878 O OG . SER B 2 169 ? -10.946 4.705 -6.463 1.00 70.95 ? 167 SER B OG 1 ATOM 2879 N N . GLY B 2 170 ? -7.326 2.886 -6.111 1.00 41.33 ? 168 GLY B N 1 ATOM 2880 C CA . GLY B 2 170 ? -6.920 1.605 -6.659 1.00 50.63 ? 168 GLY B CA 1 ATOM 2881 C C . GLY B 2 170 ? -5.571 1.647 -7.353 1.00 53.49 ? 168 GLY B C 1 ATOM 2882 O O . GLY B 2 170 ? -4.865 0.635 -7.385 1.00 45.83 ? 168 GLY B O 1 ATOM 2883 N N . GLU B 2 171 ? -5.228 2.800 -7.930 1.00 43.00 ? 169 GLU B N 1 ATOM 2884 C CA . GLU B 2 171 ? -3.962 2.952 -8.647 1.00 42.47 ? 169 GLU B CA 1 ATOM 2885 C C . GLU B 2 171 ? -2.783 2.680 -7.737 1.00 31.60 ? 169 GLU B C 1 ATOM 2886 O O . GLU B 2 171 ? -2.742 3.162 -6.600 1.00 28.23 ? 169 GLU B O 1 ATOM 2887 C CB . GLU B 2 171 ? -3.825 4.343 -9.258 1.00 38.04 ? 169 GLU B CB 1 ATOM 2888 C CG . GLU B 2 171 ? -4.667 4.561 -10.499 1.00 38.94 ? 169 GLU B CG 1 ATOM 2889 C CD . GLU B 2 171 ? -4.506 5.955 -11.069 1.00 36.52 ? 169 GLU B CD 1 ATOM 2890 O OE1 . GLU B 2 171 ? -4.063 6.860 -10.328 1.00 40.12 ? 169 GLU B OE1 1 ATOM 2891 O OE2 . GLU B 2 171 ? -4.798 6.140 -12.266 1.00 45.55 ? 169 GLU B OE2 1 ATOM 2892 N N . VAL B 2 172 ? -1.781 1.995 -8.276 1.00 38.53 ? 170 VAL B N 1 ATOM 2893 C CA . VAL B 2 172 ? -0.529 1.831 -7.550 1.00 42.97 ? 170 VAL B CA 1 ATOM 2894 C C . VAL B 2 172 ? 0.577 2.486 -8.354 1.00 27.20 ? 170 VAL B C 1 ATOM 2895 O O . VAL B 2 172 ? 0.807 2.146 -9.520 1.00 31.10 ? 170 VAL B O 1 ATOM 2896 C CB . VAL B 2 172 ? -0.178 0.338 -7.330 1.00 42.38 ? 170 VAL B CB 1 ATOM 2897 C CG1 . VAL B 2 172 ? 1.223 0.198 -6.727 1.00 29.44 ? 170 VAL B CG1 1 ATOM 2898 C CG2 . VAL B 2 172 ? -1.210 -0.333 -6.436 1.00 43.35 ? 170 VAL B CG2 1 ATOM 2899 N N . TYR B 2 173 ? 1.247 3.443 -7.720 1.00 28.89 ? 171 TYR B N 1 ATOM 2900 C CA . TYR B 2 173 ? 2.368 4.131 -8.350 1.00 30.43 ? 171 TYR B CA 1 ATOM 2901 C C . TYR B 2 173 ? 3.676 3.572 -7.830 1.00 23.91 ? 171 TYR B C 1 ATOM 2902 O O . TYR B 2 173 ? 3.779 3.215 -6.661 1.00 27.82 ? 171 TYR B O 1 ATOM 2903 C CB . TYR B 2 173 ? 2.306 5.627 -8.081 1.00 16.72 ? 171 TYR B CB 1 ATOM 2904 C CG . TYR B 2 173 ? 1.143 6.299 -8.764 1.00 23.09 ? 171 TYR B CG 1 ATOM 2905 C CD1 . TYR B 2 173 ? -0.135 6.234 -8.213 1.00 25.73 ? 171 TYR B CD1 1 ATOM 2906 C CD2 . TYR B 2 173 ? 1.304 6.967 -9.970 1.00 24.76 ? 171 TYR B CD2 1 ATOM 2907 C CE1 . TYR B 2 173 ? -1.216 6.841 -8.835 1.00 28.51 ? 171 TYR B CE1 1 ATOM 2908 C CE2 . TYR B 2 173 ? 0.241 7.574 -10.595 1.00 18.03 ? 171 TYR B CE2 1 ATOM 2909 C CZ . TYR B 2 173 ? -1.021 7.507 -10.025 1.00 28.45 ? 171 TYR B CZ 1 ATOM 2910 O OH . TYR B 2 173 ? -2.080 8.112 -10.653 1.00 32.19 ? 171 TYR B OH 1 ATOM 2911 N N . THR B 2 174 ? 4.692 3.530 -8.676 1.00 21.89 ? 172 THR B N 1 ATOM 2912 C CA . THR B 2 174 ? 5.963 2.996 -8.227 1.00 24.36 ? 172 THR B CA 1 ATOM 2913 C C . THR B 2 174 ? 7.081 3.937 -8.620 1.00 17.08 ? 172 THR B C 1 ATOM 2914 O O . THR B 2 174 ? 7.225 4.311 -9.776 1.00 15.30 ? 172 THR B O 1 ATOM 2915 C CB . THR B 2 174 ? 6.224 1.604 -8.821 1.00 24.08 ? 172 THR B CB 1 ATOM 2916 O OG1 . THR B 2 174 ? 5.158 0.732 -8.441 1.00 22.49 ? 172 THR B OG1 1 ATOM 2917 C CG2 . THR B 2 174 ? 7.566 1.032 -8.329 1.00 13.39 ? 172 THR B CG2 1 ATOM 2918 N N . CYS B 2 175 ? 7.902 4.282 -7.647 1.00 19.81 ? 173 CYS B N 1 ATOM 2919 C CA . CYS B 2 175 ? 9.108 5.012 -7.943 1.00 19.97 ? 173 CYS B CA 1 ATOM 2920 C C . CYS B 2 175 ? 10.257 4.012 -7.985 1.00 24.63 ? 173 CYS B C 1 ATOM 2921 O O . CYS B 2 175 ? 10.449 3.236 -7.045 1.00 19.32 ? 173 CYS B O 1 ATOM 2922 C CB . CYS B 2 175 ? 9.352 6.091 -6.895 1.00 18.08 ? 173 CYS B CB 1 ATOM 2923 S SG . CYS B 2 175 ? 10.834 7.027 -7.221 1.00 18.25 ? 173 CYS B SG 1 ATOM 2924 N N . GLN B 2 176 ? 11.019 4.040 -9.074 1.00 20.11 ? 174 GLN B N 1 ATOM 2925 C CA . GLN B 2 176 ? 12.103 3.089 -9.265 1.00 20.14 ? 174 GLN B CA 1 ATOM 2926 C C . GLN B 2 176 ? 13.445 3.807 -9.352 1.00 25.64 ? 174 GLN B C 1 ATOM 2927 O O . GLN B 2 176 ? 13.603 4.756 -10.116 1.00 20.81 ? 174 GLN B O 1 ATOM 2928 C CB . GLN B 2 176 ? 11.866 2.261 -10.527 1.00 17.85 ? 174 GLN B CB 1 ATOM 2929 C CG . GLN B 2 176 ? 12.938 1.221 -10.795 1.00 24.16 ? 174 GLN B CG 1 ATOM 2930 C CD . GLN B 2 176 ? 12.867 0.647 -12.198 1.00 31.58 ? 174 GLN B CD 1 ATOM 2931 O OE1 . GLN B 2 176 ? 13.371 1.235 -13.159 1.00 35.06 ? 174 GLN B OE1 1 ATOM 2932 N NE2 . GLN B 2 176 ? 12.225 -0.509 -12.323 1.00 26.26 ? 174 GLN B NE2 1 ATOM 2933 N N . VAL B 2 177 ? 14.417 3.318 -8.595 1.00 19.95 ? 175 VAL B N 1 ATOM 2934 C CA . VAL B 2 177 ? 15.702 3.983 -8.491 1.00 25.24 ? 175 VAL B CA 1 ATOM 2935 C C . VAL B 2 177 ? 16.834 3.035 -8.871 1.00 26.08 ? 175 VAL B C 1 ATOM 2936 O O . VAL B 2 177 ? 16.943 1.927 -8.329 1.00 21.39 ? 175 VAL B O 1 ATOM 2937 C CB . VAL B 2 177 ? 15.954 4.505 -7.055 1.00 18.54 ? 175 VAL B CB 1 ATOM 2938 C CG1 . VAL B 2 177 ? 17.345 5.070 -6.928 1.00 20.87 ? 175 VAL B CG1 1 ATOM 2939 C CG2 . VAL B 2 177 ? 14.917 5.545 -6.667 1.00 19.77 ? 175 VAL B CG2 1 ATOM 2940 N N . GLU B 2 178 ? 17.676 3.487 -9.797 1.00 20.26 ? 176 GLU B N 1 ATOM 2941 C CA . GLU B 2 178 ? 18.875 2.756 -10.184 1.00 20.93 ? 176 GLU B CA 1 ATOM 2942 C C . GLU B 2 178 ? 20.072 3.615 -9.808 1.00 21.94 ? 176 GLU B C 1 ATOM 2943 O O . GLU B 2 178 ? 20.047 4.837 -10.004 1.00 21.07 ? 176 GLU B O 1 ATOM 2944 C CB . GLU B 2 178 ? 18.897 2.449 -11.688 1.00 18.01 ? 176 GLU B CB 1 ATOM 2945 C CG . GLU B 2 178 ? 17.881 1.410 -12.146 1.00 37.17 ? 176 GLU B CG 1 ATOM 2946 C CD . GLU B 2 178 ? 17.622 1.450 -13.648 1.00 45.72 ? 176 GLU B CD 1 ATOM 2947 O OE1 . GLU B 2 178 ? 17.812 0.404 -14.302 1.00 51.05 ? 176 GLU B OE1 1 ATOM 2948 O OE2 . GLU B 2 178 ? 17.231 2.512 -14.178 1.00 41.12 ? 176 GLU B OE2 1 ATOM 2949 N N . HIS B 2 179 ? 21.118 2.977 -9.287 1.00 19.85 ? 177 HIS B N 1 ATOM 2950 C CA . HIS B 2 179 ? 22.268 3.673 -8.705 1.00 16.65 ? 177 HIS B CA 1 ATOM 2951 C C . HIS B 2 179 ? 23.409 2.668 -8.611 1.00 24.74 ? 177 HIS B C 1 ATOM 2952 O O . HIS B 2 179 ? 23.158 1.481 -8.432 1.00 25.49 ? 177 HIS B O 1 ATOM 2953 C CB . HIS B 2 179 ? 21.901 4.259 -7.329 1.00 20.78 ? 177 HIS B CB 1 ATOM 2954 C CG . HIS B 2 179 ? 22.976 5.100 -6.704 1.00 23.48 ? 177 HIS B CG 1 ATOM 2955 N ND1 . HIS B 2 179 ? 23.827 4.616 -5.733 1.00 19.71 ? 177 HIS B ND1 1 ATOM 2956 C CD2 . HIS B 2 179 ? 23.345 6.387 -6.917 1.00 17.34 ? 177 HIS B CD2 1 ATOM 2957 C CE1 . HIS B 2 179 ? 24.666 5.569 -5.369 1.00 17.28 ? 177 HIS B CE1 1 ATOM 2958 N NE2 . HIS B 2 179 ? 24.394 6.654 -6.072 1.00 15.86 ? 177 HIS B NE2 1 ATOM 2959 N N . PRO B 2 180 ? 24.664 3.136 -8.747 1.00 26.10 ? 178 PRO B N 1 ATOM 2960 C CA . PRO B 2 180 ? 25.823 2.228 -8.711 1.00 27.90 ? 178 PRO B CA 1 ATOM 2961 C C . PRO B 2 180 ? 25.967 1.410 -7.428 1.00 28.19 ? 178 PRO B C 1 ATOM 2962 O O . PRO B 2 180 ? 26.557 0.330 -7.446 1.00 32.80 ? 178 PRO B O 1 ATOM 2963 C CB . PRO B 2 180 ? 27.015 3.181 -8.873 1.00 25.39 ? 178 PRO B CB 1 ATOM 2964 C CG . PRO B 2 180 ? 26.457 4.342 -9.637 1.00 24.72 ? 178 PRO B CG 1 ATOM 2965 C CD . PRO B 2 180 ? 25.050 4.506 -9.137 1.00 26.24 ? 178 PRO B CD 1 ATOM 2966 N N . SER B 2 181 ? 25.402 1.898 -6.334 1.00 22.32 ? 179 SER B N 1 ATOM 2967 C CA . SER B 2 181 ? 25.525 1.197 -5.073 1.00 21.18 ? 179 SER B CA 1 ATOM 2968 C C . SER B 2 181 ? 24.571 -0.002 -4.997 1.00 29.50 ? 179 SER B C 1 ATOM 2969 O O . SER B 2 181 ? 24.719 -0.869 -4.137 1.00 30.78 ? 179 SER B O 1 ATOM 2970 C CB . SER B 2 181 ? 25.264 2.159 -3.913 1.00 17.87 ? 179 SER B CB 1 ATOM 2971 O OG . SER B 2 181 ? 23.910 2.570 -3.894 1.00 21.06 ? 179 SER B OG 1 ATOM 2972 N N . LEU B 2 182 ? 23.627 -0.068 -5.934 1.00 28.36 ? 180 LEU B N 1 ATOM 2973 C CA . LEU B 2 182 ? 22.599 -1.103 -5.937 1.00 22.85 ? 180 LEU B CA 1 ATOM 2974 C C . LEU B 2 182 ? 22.911 -2.149 -6.984 1.00 28.14 ? 180 LEU B C 1 ATOM 2975 O O . LEU B 2 182 ? 23.495 -1.835 -8.018 1.00 30.04 ? 180 LEU B O 1 ATOM 2976 C CB . LEU B 2 182 ? 21.213 -0.514 -6.227 1.00 18.99 ? 180 LEU B CB 1 ATOM 2977 C CG . LEU B 2 182 ? 20.693 0.616 -5.337 1.00 21.55 ? 180 LEU B CG 1 ATOM 2978 C CD1 . LEU B 2 182 ? 19.395 1.167 -5.906 1.00 19.30 ? 180 LEU B CD1 1 ATOM 2979 C CD2 . LEU B 2 182 ? 20.522 0.168 -3.892 1.00 18.72 ? 180 LEU B CD2 1 ATOM 2980 N N . THR B 2 183 ? 22.517 -3.391 -6.707 1.00 31.34 ? 181 THR B N 1 ATOM 2981 C CA . THR B 2 183 ? 22.732 -4.509 -7.621 1.00 31.18 ? 181 THR B CA 1 ATOM 2982 C C . THR B 2 183 ? 21.433 -4.802 -8.381 1.00 27.54 ? 181 THR B C 1 ATOM 2983 O O . THR B 2 183 ? 21.424 -5.557 -9.356 1.00 35.90 ? 181 THR B O 1 ATOM 2984 C CB . THR B 2 183 ? 23.210 -5.793 -6.879 1.00 31.60 ? 181 THR B CB 1 ATOM 2985 O OG1 . THR B 2 183 ? 22.349 -6.075 -5.768 1.00 35.48 ? 181 THR B OG1 1 ATOM 2986 C CG2 . THR B 2 183 ? 24.631 -5.623 -6.381 1.00 29.01 ? 181 THR B CG2 1 ATOM 2987 N N . SER B 2 184 ? 20.342 -4.180 -7.943 1.00 24.83 ? 182 SER B N 1 ATOM 2988 C CA . SER B 2 184 ? 19.058 -4.277 -8.634 1.00 26.17 ? 182 SER B CA 1 ATOM 2989 C C . SER B 2 184 ? 18.218 -3.047 -8.297 1.00 27.49 ? 182 SER B C 1 ATOM 2990 O O . SER B 2 184 ? 18.452 -2.414 -7.269 1.00 31.82 ? 182 SER B O 1 ATOM 2991 C CB . SER B 2 184 ? 18.332 -5.551 -8.221 1.00 31.67 ? 182 SER B CB 1 ATOM 2992 O OG . SER B 2 184 ? 17.942 -5.460 -6.864 1.00 38.06 ? 182 SER B OG 1 ATOM 2993 N N . PRO B 2 185 ? 17.217 -2.724 -9.136 1.00 26.86 ? 183 PRO B N 1 ATOM 2994 C CA . PRO B 2 185 ? 16.432 -1.506 -8.894 1.00 23.80 ? 183 PRO B CA 1 ATOM 2995 C C . PRO B 2 185 ? 15.737 -1.498 -7.547 1.00 24.64 ? 183 PRO B C 1 ATOM 2996 O O . PRO B 2 185 ? 15.252 -2.523 -7.082 1.00 22.28 ? 183 PRO B O 1 ATOM 2997 C CB . PRO B 2 185 ? 15.399 -1.521 -10.026 1.00 22.33 ? 183 PRO B CB 1 ATOM 2998 C CG . PRO B 2 185 ? 16.045 -2.308 -11.114 1.00 34.59 ? 183 PRO B CG 1 ATOM 2999 C CD . PRO B 2 185 ? 16.844 -3.372 -10.408 1.00 34.47 ? 183 PRO B CD 1 ATOM 3000 N N . LEU B 2 186 ? 15.727 -0.327 -6.927 1.00 23.99 ? 184 LEU B N 1 ATOM 3001 C CA . LEU B 2 186 ? 15.017 -0.100 -5.685 1.00 20.44 ? 184 LEU B CA 1 ATOM 3002 C C . LEU B 2 186 ? 13.641 0.463 -6.050 1.00 30.82 ? 184 LEU B C 1 ATOM 3003 O O . LEU B 2 186 ? 13.554 1.456 -6.773 1.00 27.43 ? 184 LEU B O 1 ATOM 3004 C CB . LEU B 2 186 ? 15.810 0.865 -4.792 1.00 23.65 ? 184 LEU B CB 1 ATOM 3005 C CG . LEU B 2 186 ? 15.339 1.312 -3.401 1.00 30.98 ? 184 LEU B CG 1 ATOM 3006 C CD1 . LEU B 2 186 ? 14.948 0.145 -2.515 1.00 32.60 ? 184 LEU B CD1 1 ATOM 3007 C CD2 . LEU B 2 186 ? 16.409 2.177 -2.716 1.00 16.89 ? 184 LEU B CD2 1 ATOM 3008 N N . THR B 2 187 ? 12.567 -0.178 -5.586 1.00 28.45 ? 185 THR B N 1 ATOM 3009 C CA . THR B 2 187 ? 11.221 0.292 -5.929 1.00 21.21 ? 185 THR B CA 1 ATOM 3010 C C . THR B 2 187 ? 10.453 0.623 -4.661 1.00 28.40 ? 185 THR B C 1 ATOM 3011 O O . THR B 2 187 ? 10.584 -0.072 -3.646 1.00 22.37 ? 185 THR B O 1 ATOM 3012 C CB . THR B 2 187 ? 10.439 -0.750 -6.732 1.00 20.37 ? 185 THR B CB 1 ATOM 3013 O OG1 . THR B 2 187 ? 10.317 -1.963 -5.967 1.00 16.33 ? 185 THR B OG1 1 ATOM 3014 C CG2 . THR B 2 187 ? 11.140 -1.027 -8.057 1.00 19.15 ? 185 THR B CG2 1 ATOM 3015 N N . VAL B 2 188 ? 9.675 1.704 -4.714 1.00 20.56 ? 186 VAL B N 1 ATOM 3016 C CA . VAL B 2 188 ? 8.795 2.073 -3.613 1.00 17.23 ? 186 VAL B CA 1 ATOM 3017 C C . VAL B 2 188 ? 7.390 2.339 -4.130 1.00 26.71 ? 186 VAL B C 1 ATOM 3018 O O . VAL B 2 188 ? 7.210 3.135 -5.051 1.00 18.17 ? 186 VAL B O 1 ATOM 3019 C CB . VAL B 2 188 ? 9.313 3.300 -2.874 1.00 22.34 ? 186 VAL B CB 1 ATOM 3020 C CG1 . VAL B 2 188 ? 8.298 3.753 -1.834 1.00 20.17 ? 186 VAL B CG1 1 ATOM 3021 C CG2 . VAL B 2 188 ? 10.619 2.965 -2.202 1.00 20.49 ? 186 VAL B CG2 1 ATOM 3022 N N . GLU B 2 189 ? 6.395 1.686 -3.538 1.00 28.30 ? 187 GLU B N 1 ATOM 3023 C CA . GLU B 2 189 ? 5.027 1.872 -3.987 1.00 26.60 ? 187 GLU B CA 1 ATOM 3024 C C . GLU B 2 189 ? 4.271 2.905 -3.179 1.00 23.37 ? 187 GLU B C 1 ATOM 3025 O O . GLU B 2 189 ? 4.563 3.154 -2.005 1.00 22.95 ? 187 GLU B O 1 ATOM 3026 C CB . GLU B 2 189 ? 4.255 0.556 -3.975 1.00 30.72 ? 187 GLU B CB 1 ATOM 3027 C CG . GLU B 2 189 ? 4.749 -0.444 -4.997 1.00 32.71 ? 187 GLU B CG 1 ATOM 3028 C CD . GLU B 2 189 ? 3.948 -1.719 -4.972 1.00 43.42 ? 187 GLU B CD 1 ATOM 3029 O OE1 . GLU B 2 189 ? 4.146 -2.554 -5.880 1.00 42.32 ? 187 GLU B OE1 1 ATOM 3030 O OE2 . GLU B 2 189 ? 3.113 -1.875 -4.050 1.00 43.17 ? 187 GLU B OE2 1 ATOM 3031 N N . TRP B 2 190 ? 3.304 3.518 -3.845 1.00 21.42 ? 188 TRP B N 1 ATOM 3032 C CA . TRP B 2 190 ? 2.359 4.414 -3.201 1.00 24.63 ? 188 TRP B CA 1 ATOM 3033 C C . TRP B 2 190 ? 0.965 4.114 -3.741 1.00 26.70 ? 188 TRP B C 1 ATOM 3034 O O . TRP B 2 190 ? 0.778 3.993 -4.952 1.00 26.57 ? 188 TRP B O 1 ATOM 3035 C CB . TRP B 2 190 ? 2.729 5.865 -3.432 1.00 21.88 ? 188 TRP B CB 1 ATOM 3036 C CG . TRP B 2 190 ? 1.801 6.822 -2.769 1.00 25.52 ? 188 TRP B CG 1 ATOM 3037 C CD1 . TRP B 2 190 ? 1.907 7.318 -1.498 1.00 24.98 ? 188 TRP B CD1 1 ATOM 3038 C CD2 . TRP B 2 190 ? 0.623 7.403 -3.329 1.00 15.40 ? 188 TRP B CD2 1 ATOM 3039 N NE1 . TRP B 2 190 ? 0.874 8.184 -1.240 1.00 24.47 ? 188 TRP B NE1 1 ATOM 3040 C CE2 . TRP B 2 190 ? 0.068 8.252 -2.347 1.00 25.50 ? 188 TRP B CE2 1 ATOM 3041 C CE3 . TRP B 2 190 ? -0.010 7.301 -4.564 1.00 18.17 ? 188 TRP B CE3 1 ATOM 3042 C CZ2 . TRP B 2 190 ? -1.097 8.990 -2.567 1.00 26.64 ? 188 TRP B CZ2 1 ATOM 3043 C CZ3 . TRP B 2 190 ? -1.168 8.034 -4.781 1.00 21.33 ? 188 TRP B CZ3 1 ATOM 3044 C CH2 . TRP B 2 190 ? -1.699 8.865 -3.787 1.00 19.95 ? 188 TRP B CH2 1 ATOM 3045 N N . ARG B 2 191 ? 0.003 3.951 -2.838 1.00 35.82 ? 189 ARG B N 1 ATOM 3046 C CA . ARG B 2 191 ? -1.379 3.651 -3.215 1.00 31.33 ? 189 ARG B CA 1 ATOM 3047 C C . ARG B 2 191 ? -2.299 4.803 -2.857 1.00 26.52 ? 189 ARG B C 1 ATOM 3048 O O . ARG B 2 191 ? -2.157 5.438 -1.809 1.00 28.40 ? 189 ARG B O 1 ATOM 3049 C CB . ARG B 2 191 ? -1.870 2.369 -2.536 1.00 41.00 ? 189 ARG B CB 1 ATOM 3050 C CG . ARG B 2 191 ? -1.618 1.100 -3.336 1.00 49.59 ? 189 ARG B CG 1 ATOM 3051 C CD . ARG B 2 191 ? -1.707 -0.158 -2.472 1.00 70.96 ? 189 ARG B CD 1 ATOM 3052 N NE . ARG B 2 191 ? -1.273 -1.359 -3.191 1.00 69.55 ? 189 ARG B NE 1 ATOM 3053 C CZ . ARG B 2 191 ? -0.003 -1.742 -3.322 1.00 76.68 ? 189 ARG B CZ 1 ATOM 3054 N NH1 . ARG B 2 191 ? 0.974 -1.014 -2.788 1.00 59.25 ? 189 ARG B NH1 1 ATOM 3055 N NH2 . ARG B 2 191 ? 0.295 -2.853 -3.992 1.00 60.50 ? 189 ARG B NH2 1 ATOM 3056 N N . ALA B 2 192 ? -3.239 5.072 -3.755 1.00 33.94 ? 190 ALA B N 1 ATOM 3057 C CA . ALA B 2 192 ? -4.333 5.989 -3.471 1.00 31.64 ? 190 ALA B CA 1 ATOM 3058 C C . ALA B 2 192 ? -5.455 5.299 -2.705 1.00 32.48 ? 190 ALA B C 1 ATOM 3059 O O . ALA B 2 192 ? -5.573 5.477 -1.493 1.00 28.41 ? 190 ALA B O 1 ATOM 3060 C CB . ALA B 2 192 ? -4.866 6.565 -4.766 1.00 36.09 ? 190 ALA B CB 1 ATOM 3061 N N . SER C 3 1 ? 47.859 6.612 3.622 1.00 35.87 ? 1 SER C N 1 ATOM 3062 C CA . SER C 3 1 ? 49.196 7.196 3.674 1.00 30.85 ? 1 SER C CA 1 ATOM 3063 C C . SER C 3 1 ? 49.148 8.683 3.346 1.00 26.51 ? 1 SER C C 1 ATOM 3064 O O . SER C 3 1 ? 48.107 9.321 3.507 1.00 36.91 ? 1 SER C O 1 ATOM 3065 C CB . SER C 3 1 ? 50.135 6.463 2.721 1.00 39.02 ? 1 SER C CB 1 ATOM 3066 O OG . SER C 3 1 ? 49.561 6.356 1.435 1.00 39.14 ? 1 SER C OG 1 ATOM 3067 N N . ALA C 3 2 ? 50.265 9.237 2.884 1.00 21.97 ? 2 ALA C N 1 ATOM 3068 C CA . ALA C 3 2 ? 50.385 10.687 2.751 1.00 22.50 ? 2 ALA C CA 1 ATOM 3069 C C . ALA C 3 2 ? 49.942 11.219 1.382 1.00 19.44 ? 2 ALA C C 1 ATOM 3070 O O . ALA C 3 2 ? 50.393 10.756 0.335 1.00 17.98 ? 2 ALA C O 1 ATOM 3071 C CB . ALA C 3 2 ? 51.818 11.120 3.041 1.00 17.48 ? 2 ALA C CB 1 ATOM 3072 N N . VAL C 3 3 ? 49.045 12.198 1.416 1.00 21.57 ? 3 VAL C N 1 ATOM 3073 C CA . VAL C 3 3 ? 48.642 12.935 0.224 1.00 20.26 ? 3 VAL C CA 1 ATOM 3074 C C . VAL C 3 3 ? 49.774 13.899 -0.130 1.00 12.44 ? 3 VAL C C 1 ATOM 3075 O O . VAL C 3 3 ? 50.282 14.587 0.750 1.00 14.38 ? 3 VAL C O 1 ATOM 3076 C CB . VAL C 3 3 ? 47.308 13.718 0.464 1.00 15.62 ? 3 VAL C CB 1 ATOM 3077 C CG1 . VAL C 3 3 ? 47.096 14.783 -0.597 1.00 16.15 ? 3 VAL C CG1 1 ATOM 3078 C CG2 . VAL C 3 3 ? 46.132 12.763 0.511 1.00 14.10 ? 3 VAL C CG2 1 ATOM 3079 N N . ARG C 3 4 ? 50.195 13.917 -1.390 1.00 10.76 ? 4 ARG C N 1 ATOM 3080 C CA . ARG C 3 4 ? 51.239 14.840 -1.834 1.00 11.27 ? 4 ARG C CA 1 ATOM 3081 C C . ARG C 3 4 ? 50.624 16.079 -2.473 1.00 15.67 ? 4 ARG C C 1 ATOM 3082 O O . ARG C 3 4 ? 49.552 16.006 -3.084 1.00 14.36 ? 4 ARG C O 1 ATOM 3083 C CB . ARG C 3 4 ? 52.183 14.175 -2.837 1.00 15.10 ? 4 ARG C CB 1 ATOM 3084 C CG . ARG C 3 4 ? 52.954 12.991 -2.285 1.00 13.12 ? 4 ARG C CG 1 ATOM 3085 C CD . ARG C 3 4 ? 53.461 12.133 -3.425 1.00 21.82 ? 4 ARG C CD 1 ATOM 3086 N NE . ARG C 3 4 ? 54.417 11.122 -2.980 1.00 22.91 ? 4 ARG C NE 1 ATOM 3087 C CZ . ARG C 3 4 ? 54.998 10.239 -3.789 1.00 21.56 ? 4 ARG C CZ 1 ATOM 3088 N NH1 . ARG C 3 4 ? 54.709 10.229 -5.087 1.00 15.18 ? 4 ARG C NH1 1 ATOM 3089 N NH2 . ARG C 3 4 ? 55.868 9.364 -3.299 1.00 31.93 ? 4 ARG C NH2 1 ATOM 3090 N N . LEU C 3 5 ? 51.305 17.211 -2.329 1.00 11.16 ? 5 LEU C N 1 ATOM 3091 C CA . LEU C 3 5 ? 50.884 18.429 -2.998 1.00 13.60 ? 5 LEU C CA 1 ATOM 3092 C C . LEU C 3 5 ? 51.800 18.763 -4.149 1.00 16.26 ? 5 LEU C C 1 ATOM 3093 O O . LEU C 3 5 ? 52.967 18.314 -4.179 1.00 11.04 ? 5 LEU C O 1 ATOM 3094 C CB . LEU C 3 5 ? 50.783 19.602 -1.995 1.00 15.06 ? 5 LEU C CB 1 ATOM 3095 C CG . LEU C 3 5 ? 51.957 20.379 -1.392 1.00 19.13 ? 5 LEU C CG 1 ATOM 3096 C CD1 . LEU C 3 5 ? 53.121 19.480 -1.021 1.00 26.46 ? 5 LEU C CD1 1 ATOM 3097 C CD2 . LEU C 3 5 ? 52.423 21.505 -2.300 1.00 27.04 ? 5 LEU C CD2 1 HETATM 3098 C C1 . CIR C 3 6 ? 52.320 21.398 -5.949 1.00 12.69 ? 6 CIR C C1 1 HETATM 3099 O O1 . CIR C 3 6 ? 51.637 22.238 -5.320 1.00 13.08 ? 6 CIR C O1 1 HETATM 3100 C C2 . CIR C 3 6 ? 51.805 20.017 -6.208 1.00 17.21 ? 6 CIR C C2 1 HETATM 3101 N N2 . CIR C 3 6 ? 51.164 19.546 -5.015 1.00 12.77 ? 6 CIR C N2 1 HETATM 3102 C C3 . CIR C 3 6 ? 50.877 19.936 -7.382 1.00 9.93 ? 6 CIR C C3 1 HETATM 3103 C C4 . CIR C 3 6 ? 51.608 20.364 -8.629 1.00 15.84 ? 6 CIR C C4 1 HETATM 3104 C C5 . CIR C 3 6 ? 52.106 19.163 -9.432 1.00 17.05 ? 6 CIR C C5 1 HETATM 3105 N N6 . CIR C 3 6 ? 53.239 18.516 -8.777 1.00 10.53 ? 6 CIR C N6 1 HETATM 3106 C C7 . CIR C 3 6 ? 54.466 19.242 -8.565 1.00 17.25 ? 6 CIR C C7 1 HETATM 3107 O O7 . CIR C 3 6 ? 54.574 20.400 -8.944 1.00 17.57 ? 6 CIR C O7 1 HETATM 3108 N N8 . CIR C 3 6 ? 55.582 18.609 -7.909 1.00 19.38 ? 6 CIR C N8 1 ATOM 3109 N N . SER C 3 7 ? 53.492 21.793 -6.352 1.00 12.25 ? 7 SER C N 1 ATOM 3110 C CA . SER C 3 7 ? 54.000 23.149 -6.085 1.00 16.01 ? 7 SER C CA 1 ATOM 3111 C C . SER C 3 7 ? 53.313 24.191 -6.942 1.00 12.58 ? 7 SER C C 1 ATOM 3112 O O . SER C 3 7 ? 52.998 23.945 -8.115 1.00 11.26 ? 7 SER C O 1 ATOM 3113 C CB . SER C 3 7 ? 55.492 23.209 -6.337 1.00 17.93 ? 7 SER C CB 1 ATOM 3114 O OG . SER C 3 7 ? 55.757 23.151 -7.733 1.00 24.17 ? 7 SER C OG 1 ATOM 3115 N N . SER C 3 8 ? 53.102 25.363 -6.357 1.00 8.42 ? 8 SER C N 1 ATOM 3116 C CA . SER C 3 8 ? 52.730 26.550 -7.116 1.00 12.91 ? 8 SER C CA 1 ATOM 3117 C C . SER C 3 8 ? 53.996 27.296 -7.521 1.00 17.67 ? 8 SER C C 1 ATOM 3118 O O . SER C 3 8 ? 54.901 27.490 -6.714 1.00 18.30 ? 8 SER C O 1 ATOM 3119 C CB . SER C 3 8 ? 51.792 27.444 -6.307 1.00 14.70 ? 8 SER C CB 1 ATOM 3120 O OG . SER C 3 8 ? 50.532 26.808 -6.131 1.00 13.30 ? 8 SER C OG 1 ATOM 3121 N N . VAL C 3 9 ? 54.059 27.708 -8.779 1.00 15.91 ? 9 VAL C N 1 ATOM 3122 C CA . VAL C 3 9 ? 55.288 28.255 -9.329 1.00 12.88 ? 9 VAL C CA 1 ATOM 3123 C C . VAL C 3 9 ? 55.379 29.781 -9.195 1.00 17.11 ? 9 VAL C C 1 ATOM 3124 O O . VAL C 3 9 ? 54.498 30.499 -9.670 1.00 10.75 ? 9 VAL C O 1 ATOM 3125 C CB . VAL C 3 9 ? 55.439 27.876 -10.817 1.00 14.98 ? 9 VAL C CB 1 ATOM 3126 C CG1 . VAL C 3 9 ? 56.860 28.189 -11.310 1.00 15.39 ? 9 VAL C CG1 1 ATOM 3127 C CG2 . VAL C 3 9 ? 55.114 26.408 -11.033 1.00 7.34 ? 9 VAL C CG2 1 ATOM 3128 N N . PRO C 3 10 ? 56.461 30.277 -8.560 1.00 20.42 ? 10 PRO C N 1 ATOM 3129 C CA . PRO C 3 10 ? 56.683 31.725 -8.457 1.00 19.15 ? 10 PRO C CA 1 ATOM 3130 C C . PRO C 3 10 ? 56.740 32.382 -9.827 1.00 14.06 ? 10 PRO C C 1 ATOM 3131 O O . PRO C 3 10 ? 57.402 31.880 -10.738 1.00 11.35 ? 10 PRO C O 1 ATOM 3132 C CB . PRO C 3 10 ? 58.031 31.840 -7.727 1.00 19.11 ? 10 PRO C CB 1 ATOM 3133 C CG . PRO C 3 10 ? 58.584 30.464 -7.648 1.00 17.42 ? 10 PRO C CG 1 ATOM 3134 C CD . PRO C 3 10 ? 57.461 29.506 -7.806 1.00 15.93 ? 10 PRO C CD 1 ATOM 3135 N N . GLY C 3 11 ? 56.029 33.495 -9.965 1.00 12.40 ? 11 GLY C N 1 ATOM 3136 C CA . GLY C 3 11 ? 55.912 34.165 -11.245 1.00 15.50 ? 11 GLY C CA 1 ATOM 3137 C C . GLY C 3 11 ? 57.128 35.005 -11.542 1.00 19.04 ? 11 GLY C C 1 ATOM 3138 O O . GLY C 3 11 ? 57.974 35.210 -10.675 1.00 15.93 ? 11 GLY C O 1 ATOM 3139 N N . VAL C 3 12 ? 57.207 35.499 -12.772 1.00 21.91 ? 12 VAL C N 1 ATOM 3140 C CA . VAL C 3 12 ? 58.334 36.305 -13.207 1.00 18.44 ? 12 VAL C CA 1 ATOM 3141 C C . VAL C 3 12 ? 58.196 37.751 -12.713 1.00 24.37 ? 12 VAL C C 1 ATOM 3142 O O . VAL C 3 12 ? 57.092 38.233 -12.457 1.00 29.97 ? 12 VAL C O 1 ATOM 3143 C CB . VAL C 3 12 ? 58.479 36.256 -14.754 1.00 24.51 ? 12 VAL C CB 1 ATOM 3144 C CG1 . VAL C 3 12 ? 57.527 37.222 -15.408 1.00 31.11 ? 12 VAL C CG1 1 ATOM 3145 C CG2 . VAL C 3 12 ? 59.908 36.552 -15.181 1.00 26.78 ? 12 VAL C CG2 1 ATOM 3146 N N . ARG C 3 13 ? 59.337 38.423 -12.585 1.00 35.83 ? 13 ARG C N 1 ATOM 3147 C CA . ARG C 3 13 ? 59.453 39.755 -11.987 1.00 40.81 ? 13 ARG C CA 1 ATOM 3148 C C . ARG C 3 13 ? 58.894 39.800 -10.568 1.00 37.99 ? 13 ARG C C 1 ATOM 3149 O O . ARG C 3 13 ? 59.516 40.375 -9.666 1.00 33.04 ? 13 ARG C O 1 ATOM 3150 C CB . ARG C 3 13 ? 58.772 40.814 -12.856 1.00 21.54 ? 13 ARG C CB 1 ATOM 3151 C CG . ARG C 3 13 ? 58.581 42.146 -12.142 1.00 30.86 ? 13 ARG C CG 1 ATOM 3152 C CD . ARG C 3 13 ? 57.107 42.417 -11.807 1.00 36.25 ? 13 ARG C CD 1 ATOM 3153 N NE . ARG C 3 13 ? 56.429 43.125 -12.896 1.00 66.71 ? 13 ARG C NE 1 ATOM 3154 C CZ . ARG C 3 13 ? 55.110 43.139 -13.090 1.00 49.35 ? 13 ARG C CZ 1 ATOM 3155 N NH1 . ARG C 3 13 ? 54.595 43.818 -14.117 1.00 30.56 ? 13 ARG C NH1 1 ATOM 3156 N NH2 . ARG C 3 13 ? 54.307 42.471 -12.265 1.00 16.68 ? 13 ARG C NH2 1 HETATM 3157 C C1 . NAG D 4 . ? 48.679 47.988 -18.902 1.00 49.33 ? 201 NAG A C1 1 HETATM 3158 C C2 . NAG D 4 . ? 47.953 47.489 -20.136 1.00 54.93 ? 201 NAG A C2 1 HETATM 3159 C C3 . NAG D 4 . ? 48.951 47.252 -21.284 1.00 63.95 ? 201 NAG A C3 1 HETATM 3160 C C4 . NAG D 4 . ? 49.785 48.511 -21.521 1.00 61.48 ? 201 NAG A C4 1 HETATM 3161 C C5 . NAG D 4 . ? 50.397 49.002 -20.203 1.00 62.70 ? 201 NAG A C5 1 HETATM 3162 C C6 . NAG D 4 . ? 51.096 50.341 -20.311 1.00 58.21 ? 201 NAG A C6 1 HETATM 3163 C C7 . NAG D 4 . ? 45.938 46.071 -20.200 1.00 64.05 ? 201 NAG A C7 1 HETATM 3164 C C8 . NAG D 4 . ? 45.332 47.126 -21.084 1.00 74.89 ? 201 NAG A C8 1 HETATM 3165 N N2 . NAG D 4 . ? 47.199 46.287 -19.810 1.00 47.60 ? 201 NAG A N2 1 HETATM 3166 O O3 . NAG D 4 . ? 48.269 46.901 -22.485 1.00 69.21 ? 201 NAG A O3 1 HETATM 3167 O O4 . NAG D 4 . ? 50.806 48.290 -22.492 1.00 61.04 ? 201 NAG A O4 1 HETATM 3168 O O5 . NAG D 4 . ? 49.373 49.168 -19.210 1.00 46.79 ? 201 NAG A O5 1 HETATM 3169 O O6 . NAG D 4 . ? 51.580 50.774 -19.045 1.00 47.86 ? 201 NAG A O6 1 HETATM 3170 O O7 . NAG D 4 . ? 45.315 45.066 -19.858 1.00 62.16 ? 201 NAG A O7 1 HETATM 3171 C C1 . NAG E 4 . ? 30.527 41.428 6.670 1.00 42.48 ? 202 NAG A C1 1 HETATM 3172 C C2 . NAG E 4 . ? 30.774 42.334 5.458 1.00 42.50 ? 202 NAG A C2 1 HETATM 3173 C C3 . NAG E 4 . ? 31.904 43.329 5.738 1.00 44.44 ? 202 NAG A C3 1 HETATM 3174 C C4 . NAG E 4 . ? 31.669 44.067 7.048 1.00 49.47 ? 202 NAG A C4 1 HETATM 3175 C C5 . NAG E 4 . ? 31.439 43.063 8.172 1.00 46.91 ? 202 NAG A C5 1 HETATM 3176 C C6 . NAG E 4 . ? 31.097 43.725 9.484 1.00 59.06 ? 202 NAG A C6 1 HETATM 3177 C C7 . NAG E 4 . ? 30.230 41.382 3.265 1.00 32.12 ? 202 NAG A C7 1 HETATM 3178 C C8 . NAG E 4 . ? 30.710 40.520 2.135 1.00 24.74 ? 202 NAG A C8 1 HETATM 3179 N N2 . NAG E 4 . ? 31.082 41.536 4.283 1.00 34.31 ? 202 NAG A N2 1 HETATM 3180 O O3 . NAG E 4 . ? 31.958 44.277 4.677 1.00 44.32 ? 202 NAG A O3 1 HETATM 3181 O O4 . NAG E 4 . ? 32.778 44.909 7.349 1.00 53.19 ? 202 NAG A O4 1 HETATM 3182 O O5 . NAG E 4 . ? 30.322 42.227 7.834 1.00 50.83 ? 202 NAG A O5 1 HETATM 3183 O O6 . NAG E 4 . ? 29.881 44.455 9.382 1.00 52.75 ? 202 NAG A O6 1 HETATM 3184 O O7 . NAG E 4 . ? 29.122 41.916 3.256 1.00 33.21 ? 202 NAG A O7 1 HETATM 3185 C C1 . EDO F 5 . ? 38.476 42.183 -14.422 1.00 27.88 ? 203 EDO A C1 1 HETATM 3186 O O1 . EDO F 5 . ? 38.479 41.722 -15.780 1.00 43.49 ? 203 EDO A O1 1 HETATM 3187 C C2 . EDO F 5 . ? 37.068 42.642 -14.082 1.00 23.86 ? 203 EDO A C2 1 HETATM 3188 O O2 . EDO F 5 . ? 37.033 43.325 -12.823 1.00 32.78 ? 203 EDO A O2 1 HETATM 3189 C C1 . NAG G 4 . ? 40.748 -0.045 -18.993 1.00 73.08 ? 201 NAG B C1 1 HETATM 3190 C C2 . NAG G 4 . ? 41.545 -0.148 -20.276 1.00 75.14 ? 201 NAG B C2 1 HETATM 3191 C C3 . NAG G 4 . ? 41.612 -1.603 -20.721 1.00 82.73 ? 201 NAG B C3 1 HETATM 3192 C C4 . NAG G 4 . ? 42.172 -2.481 -19.608 1.00 83.44 ? 201 NAG B C4 1 HETATM 3193 C C5 . NAG G 4 . ? 41.471 -2.224 -18.266 1.00 80.21 ? 201 NAG B C5 1 HETATM 3194 C C6 . NAG G 4 . ? 42.212 -2.850 -17.110 1.00 81.00 ? 201 NAG B C6 1 HETATM 3195 C C7 . NAG G 4 . ? 41.661 1.639 -21.970 1.00 86.82 ? 201 NAG B C7 1 HETATM 3196 C C8 . NAG G 4 . ? 40.912 2.371 -23.047 1.00 79.36 ? 201 NAG B C8 1 HETATM 3197 N N2 . NAG G 4 . ? 40.976 0.683 -21.328 1.00 84.34 ? 201 NAG B N2 1 HETATM 3198 O O3 . NAG G 4 . ? 42.433 -1.705 -21.880 1.00 87.73 ? 201 NAG B O3 1 HETATM 3199 O O4 . NAG G 4 . ? 41.992 -3.848 -19.967 1.00 73.59 ? 201 NAG B O4 1 HETATM 3200 O O5 . NAG G 4 . ? 41.387 -0.816 -17.971 1.00 76.13 ? 201 NAG B O5 1 HETATM 3201 O O6 . NAG G 4 . ? 43.414 -2.134 -16.862 1.00 66.96 ? 201 NAG B O6 1 HETATM 3202 O O7 . NAG G 4 . ? 42.840 1.888 -21.709 1.00 77.19 ? 201 NAG B O7 1 HETATM 3203 C C1 . EDO H 5 . ? 54.023 15.212 -6.637 1.00 20.83 ? 202 EDO B C1 1 HETATM 3204 O O1 . EDO H 5 . ? 54.451 15.699 -7.919 1.00 26.33 ? 202 EDO B O1 1 HETATM 3205 C C2 . EDO H 5 . ? 55.025 15.590 -5.558 1.00 27.70 ? 202 EDO B C2 1 HETATM 3206 O O2 . EDO H 5 . ? 56.266 14.898 -5.759 1.00 33.39 ? 202 EDO B O2 1 HETATM 3207 O O . HOH I 6 . ? 13.344 33.844 10.239 1.00 17.78 ? 301 HOH A O 1 HETATM 3208 O O . HOH I 6 . ? 22.711 27.261 -7.101 1.00 18.56 ? 302 HOH A O 1 HETATM 3209 O O . HOH I 6 . ? 34.831 22.979 4.839 1.00 16.11 ? 303 HOH A O 1 HETATM 3210 O O . HOH I 6 . ? 15.279 28.240 -1.716 1.00 13.43 ? 304 HOH A O 1 HETATM 3211 O O . HOH I 6 . ? 23.503 33.360 -11.036 1.00 21.81 ? 305 HOH A O 1 HETATM 3212 O O . HOH I 6 . ? 24.293 38.040 7.178 1.00 13.91 ? 306 HOH A O 1 HETATM 3213 O O . HOH I 6 . ? 46.813 43.122 -5.092 1.00 11.83 ? 307 HOH A O 1 HETATM 3214 O O . HOH I 6 . ? 31.430 39.950 -0.986 1.00 14.50 ? 308 HOH A O 1 HETATM 3215 O O . HOH I 6 . ? 32.721 20.968 1.942 1.00 13.22 ? 309 HOH A O 1 HETATM 3216 O O . HOH I 6 . ? 31.640 24.622 10.750 1.00 20.45 ? 310 HOH A O 1 HETATM 3217 O O . HOH I 6 . ? 11.065 36.370 8.390 1.00 25.29 ? 311 HOH A O 1 HETATM 3218 O O . HOH I 6 . ? 36.838 39.877 -12.743 1.00 13.63 ? 312 HOH A O 1 HETATM 3219 O O . HOH I 6 . ? 11.906 24.739 14.133 1.00 20.97 ? 313 HOH A O 1 HETATM 3220 O O . HOH I 6 . ? 46.785 14.581 8.276 1.00 21.10 ? 314 HOH A O 1 HETATM 3221 O O . HOH I 6 . ? 37.235 17.827 -8.796 1.00 15.75 ? 315 HOH A O 1 HETATM 3222 O O . HOH I 6 . ? 37.162 19.857 5.839 1.00 16.78 ? 316 HOH A O 1 HETATM 3223 O O . HOH I 6 . ? 12.636 32.657 -0.298 1.00 20.45 ? 317 HOH A O 1 HETATM 3224 O O . HOH I 6 . ? 41.321 29.863 3.897 1.00 25.15 ? 318 HOH A O 1 HETATM 3225 O O . HOH I 6 . ? 48.543 40.830 0.956 1.00 28.30 ? 319 HOH A O 1 HETATM 3226 O O . HOH I 6 . ? 19.039 33.581 -5.596 1.00 16.30 ? 320 HOH A O 1 HETATM 3227 O O . HOH I 6 . ? 32.439 45.419 -8.786 1.00 14.41 ? 321 HOH A O 1 HETATM 3228 O O . HOH I 6 . ? 19.948 40.537 12.414 1.00 21.12 ? 322 HOH A O 1 HETATM 3229 O O . HOH I 6 . ? 35.175 43.582 -4.703 1.00 21.29 ? 323 HOH A O 1 HETATM 3230 O O . HOH I 6 . ? 55.738 39.457 -5.306 1.00 16.52 ? 324 HOH A O 1 HETATM 3231 O O . HOH I 6 . ? 28.515 40.800 -11.909 1.00 19.50 ? 325 HOH A O 1 HETATM 3232 O O . HOH I 6 . ? 52.614 18.726 2.530 1.00 22.43 ? 326 HOH A O 1 HETATM 3233 O O . HOH I 6 . ? 23.578 32.389 11.959 1.00 20.55 ? 327 HOH A O 1 HETATM 3234 O O . HOH I 6 . ? 12.123 15.881 9.918 1.00 26.23 ? 328 HOH A O 1 HETATM 3235 O O . HOH I 6 . ? 32.114 10.507 -7.603 1.00 14.98 ? 329 HOH A O 1 HETATM 3236 O O . HOH I 6 . ? 10.589 24.450 12.319 1.00 24.73 ? 330 HOH A O 1 HETATM 3237 O O . HOH I 6 . ? 25.732 34.444 -10.145 1.00 14.92 ? 331 HOH A O 1 HETATM 3238 O O . HOH I 6 . ? 51.284 46.792 -5.669 1.00 30.97 ? 332 HOH A O 1 HETATM 3239 O O . HOH I 6 . ? 28.347 21.818 -5.203 1.00 30.43 ? 333 HOH A O 1 HETATM 3240 O O . HOH I 6 . ? 29.528 34.130 7.690 1.00 27.78 ? 334 HOH A O 1 HETATM 3241 O O . HOH I 6 . ? 29.432 45.282 -7.692 1.00 18.98 ? 335 HOH A O 1 HETATM 3242 O O . HOH I 6 . ? 21.836 28.358 -4.784 1.00 11.69 ? 336 HOH A O 1 HETATM 3243 O O . HOH I 6 . ? 28.731 28.342 10.929 1.00 18.85 ? 337 HOH A O 1 HETATM 3244 O O . HOH I 6 . ? 12.451 12.806 8.794 1.00 30.12 ? 338 HOH A O 1 HETATM 3245 O O . HOH I 6 . ? 14.651 36.672 -1.885 1.00 26.28 ? 339 HOH A O 1 HETATM 3246 O O . HOH I 6 . ? 43.065 42.171 -16.699 1.00 25.20 ? 340 HOH A O 1 HETATM 3247 O O . HOH I 6 . ? 51.509 31.104 3.576 1.00 19.99 ? 341 HOH A O 1 HETATM 3248 O O . HOH I 6 . ? 17.777 14.624 8.189 1.00 26.28 ? 342 HOH A O 1 HETATM 3249 O O . HOH I 6 . ? 49.058 30.615 8.369 1.00 33.79 ? 343 HOH A O 1 HETATM 3250 O O . HOH I 6 . ? 56.287 34.584 -6.588 1.00 25.46 ? 344 HOH A O 1 HETATM 3251 O O . HOH I 6 . ? 16.849 42.131 2.839 1.00 29.38 ? 345 HOH A O 1 HETATM 3252 O O . HOH I 6 . ? 40.007 16.502 10.751 1.00 26.98 ? 346 HOH A O 1 HETATM 3253 O O . HOH I 6 . ? 17.539 40.179 13.440 1.00 22.93 ? 347 HOH A O 1 HETATM 3254 O O . HOH I 6 . ? 51.253 13.193 5.718 1.00 27.39 ? 348 HOH A O 1 HETATM 3255 O O . HOH I 6 . ? 34.383 4.814 -9.563 1.00 24.86 ? 349 HOH A O 1 HETATM 3256 O O . HOH I 6 . ? 23.397 31.149 -13.514 1.00 29.67 ? 350 HOH A O 1 HETATM 3257 O O . HOH I 6 . ? 41.502 41.589 -15.020 1.00 21.53 ? 351 HOH A O 1 HETATM 3258 O O . HOH I 6 . ? 52.045 15.066 7.867 1.00 36.34 ? 352 HOH A O 1 HETATM 3259 O O . HOH I 6 . ? 43.927 4.994 11.300 1.00 27.60 ? 353 HOH A O 1 HETATM 3260 O O . HOH I 6 . ? 19.077 17.663 13.501 1.00 26.34 ? 354 HOH A O 1 HETATM 3261 O O . HOH I 6 . ? 33.843 35.238 4.237 1.00 20.32 ? 355 HOH A O 1 HETATM 3262 O O . HOH I 6 . ? 30.523 19.616 -2.267 1.00 23.15 ? 356 HOH A O 1 HETATM 3263 O O . HOH I 6 . ? 55.668 24.747 -2.394 1.00 32.76 ? 357 HOH A O 1 HETATM 3264 O O . HOH I 6 . ? 28.394 18.514 6.927 1.00 23.30 ? 358 HOH A O 1 HETATM 3265 O O . HOH I 6 . ? 38.621 32.251 3.517 1.00 30.28 ? 359 HOH A O 1 HETATM 3266 O O . HOH I 6 . ? 54.574 36.028 -0.357 1.00 22.30 ? 360 HOH A O 1 HETATM 3267 O O . HOH I 6 . ? 35.158 21.079 7.370 1.00 18.54 ? 361 HOH A O 1 HETATM 3268 O O . HOH I 6 . ? 13.400 29.680 -0.505 1.00 22.64 ? 362 HOH A O 1 HETATM 3269 O O . HOH I 6 . ? 33.228 37.598 6.205 1.00 32.16 ? 363 HOH A O 1 HETATM 3270 O O . HOH I 6 . ? 56.690 29.875 -0.457 1.00 23.28 ? 364 HOH A O 1 HETATM 3271 O O . HOH I 6 . ? 45.646 11.570 9.050 1.00 38.18 ? 365 HOH A O 1 HETATM 3272 O O . HOH I 6 . ? 33.380 40.126 5.404 1.00 32.10 ? 366 HOH A O 1 HETATM 3273 O O . HOH I 6 . ? 36.814 44.601 -6.703 1.00 8.35 ? 367 HOH A O 1 HETATM 3274 O O . HOH I 6 . ? 27.889 16.708 -1.344 1.00 11.79 ? 368 HOH A O 1 HETATM 3275 O O . HOH I 6 . ? 19.922 14.024 1.192 1.00 11.61 ? 369 HOH A O 1 HETATM 3276 O O . HOH I 6 . ? 42.235 26.565 3.536 1.00 18.69 ? 370 HOH A O 1 HETATM 3277 O O . HOH I 6 . ? 6.910 14.629 4.124 1.00 24.71 ? 371 HOH A O 1 HETATM 3278 O O . HOH I 6 . ? 25.704 21.792 11.688 1.00 15.04 ? 372 HOH A O 1 HETATM 3279 O O . HOH I 6 . ? 31.060 23.749 -11.448 1.00 21.25 ? 373 HOH A O 1 HETATM 3280 O O . HOH I 6 . ? 14.896 23.445 16.458 1.00 31.13 ? 374 HOH A O 1 HETATM 3281 O O . HOH I 6 . ? 38.558 25.219 9.425 1.00 32.83 ? 375 HOH A O 1 HETATM 3282 O O . HOH I 6 . ? 42.163 49.734 -8.955 1.00 28.00 ? 376 HOH A O 1 HETATM 3283 O O . HOH I 6 . ? 36.322 47.422 -7.414 1.00 27.06 ? 377 HOH A O 1 HETATM 3284 O O . HOH I 6 . ? 19.398 40.921 -2.697 1.00 25.53 ? 378 HOH A O 1 HETATM 3285 O O . HOH I 6 . ? 49.971 31.852 -7.968 1.00 9.29 ? 379 HOH A O 1 HETATM 3286 O O . HOH I 6 . ? 30.856 25.723 -13.111 1.00 16.29 ? 380 HOH A O 1 HETATM 3287 O O . HOH I 6 . ? 26.685 38.680 -12.443 1.00 28.68 ? 381 HOH A O 1 HETATM 3288 O O . HOH I 6 . ? 25.312 19.208 11.101 1.00 31.24 ? 382 HOH A O 1 HETATM 3289 O O . HOH I 6 . ? 14.889 37.270 21.771 1.00 41.21 ? 383 HOH A O 1 HETATM 3290 O O . HOH I 6 . ? 28.159 14.599 -2.936 1.00 19.20 ? 384 HOH A O 1 HETATM 3291 O O . HOH I 6 . ? 51.719 34.021 3.161 1.00 34.52 ? 385 HOH A O 1 HETATM 3292 O O . HOH I 6 . ? 37.985 34.447 2.337 1.00 37.05 ? 386 HOH A O 1 HETATM 3293 O O . HOH I 6 . ? 59.902 32.752 -4.755 1.00 33.21 ? 387 HOH A O 1 HETATM 3294 O O . HOH I 6 . ? 35.901 18.516 -11.065 1.00 20.09 ? 388 HOH A O 1 HETATM 3295 O O . HOH I 6 . ? 57.613 33.626 -4.487 1.00 28.84 ? 389 HOH A O 1 HETATM 3296 O O . HOH I 6 . ? 34.534 28.904 7.183 1.00 22.55 ? 390 HOH A O 1 HETATM 3297 O O . HOH I 6 . ? 42.238 28.576 7.221 1.00 36.02 ? 391 HOH A O 1 HETATM 3298 O O . HOH I 6 . ? 25.219 37.209 -11.183 1.00 26.08 ? 392 HOH A O 1 HETATM 3299 O O . HOH I 6 . ? 36.403 35.582 4.216 1.00 23.72 ? 393 HOH A O 1 HETATM 3300 O O . HOH I 6 . ? 37.067 28.705 -8.462 1.00 6.92 ? 394 HOH A O 1 HETATM 3301 O O . HOH I 6 . ? 21.721 37.230 -7.312 1.00 24.14 ? 395 HOH A O 1 HETATM 3302 O O . HOH I 6 . ? 38.900 6.378 -12.843 1.00 32.89 ? 396 HOH A O 1 HETATM 3303 O O . HOH I 6 . ? 17.985 24.542 16.018 1.00 40.12 ? 397 HOH A O 1 HETATM 3304 O O . HOH I 6 . ? 54.454 38.555 -0.430 1.00 32.74 ? 398 HOH A O 1 HETATM 3305 O O . HOH I 6 . ? 38.112 27.273 -17.588 1.00 17.36 ? 399 HOH A O 1 HETATM 3306 O O . HOH I 6 . ? 11.641 32.894 18.174 1.00 28.07 ? 400 HOH A O 1 HETATM 3307 O O . HOH I 6 . ? 52.225 48.084 -16.537 1.00 33.88 ? 401 HOH A O 1 HETATM 3308 O O . HOH I 6 . ? 36.876 3.569 -12.006 1.00 36.81 ? 402 HOH A O 1 HETATM 3309 O O . HOH I 6 . ? 43.950 44.427 -17.997 1.00 40.22 ? 403 HOH A O 1 HETATM 3310 O O . HOH I 6 . ? 14.219 32.507 17.559 1.00 32.56 ? 404 HOH A O 1 HETATM 3311 O O . HOH I 6 . ? 28.013 24.014 15.962 1.00 37.21 ? 405 HOH A O 1 HETATM 3312 O O . HOH I 6 . ? 27.926 19.670 9.057 1.00 32.77 ? 406 HOH A O 1 HETATM 3313 O O . HOH I 6 . ? 22.266 25.969 -12.255 1.00 45.70 ? 407 HOH A O 1 HETATM 3314 O O . HOH I 6 . ? 13.448 11.951 6.818 1.00 35.07 ? 408 HOH A O 1 HETATM 3315 O O . HOH I 6 . ? 47.888 44.232 -18.766 1.00 45.41 ? 409 HOH A O 1 HETATM 3316 O O . HOH I 6 . ? 21.550 15.024 8.772 1.00 34.64 ? 410 HOH A O 1 HETATM 3317 O O . HOH I 6 . ? 15.053 10.187 8.344 1.00 40.49 ? 411 HOH A O 1 HETATM 3318 O O . HOH I 6 . ? 17.707 28.351 17.419 1.00 45.17 ? 412 HOH A O 1 HETATM 3319 O O . HOH I 6 . ? 49.668 18.511 9.094 1.00 28.58 ? 413 HOH A O 1 HETATM 3320 O O . HOH I 6 . ? 25.981 43.315 -9.261 1.00 27.01 ? 414 HOH A O 1 HETATM 3321 O O . HOH I 6 . ? 20.071 43.321 -3.588 1.00 37.42 ? 415 HOH A O 1 HETATM 3322 O O . HOH I 6 . ? 34.387 37.115 8.609 1.00 34.68 ? 416 HOH A O 1 HETATM 3323 O O . HOH I 6 . ? 16.948 35.937 -5.743 1.00 30.03 ? 417 HOH A O 1 HETATM 3324 O O . HOH I 6 . ? 18.008 20.797 16.791 1.00 28.40 ? 418 HOH A O 1 HETATM 3325 O O . HOH I 6 . ? 18.794 18.837 16.215 1.00 32.61 ? 419 HOH A O 1 HETATM 3326 O O . HOH I 6 . ? 29.426 29.305 -15.587 1.00 30.64 ? 420 HOH A O 1 HETATM 3327 O O . HOH I 6 . ? 28.209 43.596 -9.365 1.00 26.40 ? 421 HOH A O 1 HETATM 3328 O O . HOH I 6 . ? 30.815 11.459 9.429 1.00 41.20 ? 422 HOH A O 1 HETATM 3329 O O . HOH I 6 . ? 26.324 28.771 9.415 1.00 25.22 ? 423 HOH A O 1 HETATM 3330 O O . HOH I 6 . ? 31.059 33.140 6.213 1.00 36.06 ? 424 HOH A O 1 HETATM 3331 O O . HOH I 6 . ? 39.316 27.118 8.484 1.00 36.40 ? 425 HOH A O 1 HETATM 3332 O O . HOH I 6 . ? 16.481 36.327 -7.954 1.00 41.37 ? 426 HOH A O 1 HETATM 3333 O O . HOH I 6 . ? 53.812 35.650 2.693 1.00 32.29 ? 427 HOH A O 1 HETATM 3334 O O . HOH I 6 . ? 35.934 41.737 4.690 1.00 28.11 ? 428 HOH A O 1 HETATM 3335 O O . HOH I 6 . ? 16.799 32.846 18.206 1.00 26.49 ? 429 HOH A O 1 HETATM 3336 O O . HOH I 6 . ? 16.471 48.709 1.982 1.00 30.30 ? 430 HOH A O 1 HETATM 3337 O O . HOH I 6 . ? 10.591 35.416 18.193 1.00 41.50 ? 431 HOH A O 1 HETATM 3338 O O . HOH I 6 . ? 29.601 32.256 9.717 1.00 37.33 ? 432 HOH A O 1 HETATM 3339 O O . HOH I 6 . ? 36.359 29.828 4.563 1.00 32.30 ? 433 HOH A O 1 HETATM 3340 O O . HOH I 6 . ? 51.532 19.694 10.209 1.00 43.04 ? 434 HOH A O 1 HETATM 3341 O O . HOH I 6 . ? 12.543 9.025 7.814 1.00 38.35 ? 435 HOH A O 1 HETATM 3342 O O . HOH I 6 . ? 33.676 31.534 8.332 1.00 42.82 ? 436 HOH A O 1 HETATM 3343 O O . HOH I 6 . ? 11.069 9.425 16.653 1.00 39.84 ? 437 HOH A O 1 HETATM 3344 O O . HOH I 6 . ? 59.013 36.501 -4.144 1.00 40.66 ? 438 HOH A O 1 HETATM 3345 O O . HOH I 6 . ? 15.606 38.588 -0.194 1.00 22.67 ? 439 HOH A O 1 HETATM 3346 O O . HOH I 6 . ? 34.428 32.386 5.724 1.00 40.60 ? 440 HOH A O 1 HETATM 3347 O O . HOH I 6 . ? 31.552 36.205 7.748 1.00 34.10 ? 441 HOH A O 1 HETATM 3348 O O . HOH I 6 . ? 30.026 45.410 3.922 1.00 39.48 ? 442 HOH A O 1 HETATM 3349 O O . HOH I 6 . ? 10.364 38.564 20.609 1.00 44.53 ? 443 HOH A O 1 HETATM 3350 O O . HOH I 6 . ? 5.727 14.544 19.713 1.00 42.59 ? 444 HOH A O 1 HETATM 3351 O O . HOH I 6 . ? 37.461 24.629 -15.288 1.00 10.59 ? 445 HOH A O 1 HETATM 3352 O O . HOH I 6 . ? 46.487 45.324 -3.899 1.00 19.29 ? 446 HOH A O 1 HETATM 3353 O O . HOH I 6 . ? 35.099 22.116 -9.236 1.00 16.57 ? 447 HOH A O 1 HETATM 3354 O O . HOH I 6 . ? 17.902 31.548 -7.130 1.00 19.72 ? 448 HOH A O 1 HETATM 3355 O O . HOH I 6 . ? 20.557 29.860 18.909 1.00 36.75 ? 449 HOH A O 1 HETATM 3356 O O . HOH I 6 . ? 49.386 35.434 4.197 1.00 38.02 ? 450 HOH A O 1 HETATM 3357 O O . HOH I 6 . ? 3.718 11.763 7.166 1.00 32.87 ? 451 HOH A O 1 HETATM 3358 O O . HOH I 6 . ? 13.791 26.198 20.004 1.00 34.78 ? 452 HOH A O 1 HETATM 3359 O O . HOH I 6 . ? 34.255 34.454 7.770 1.00 37.34 ? 453 HOH A O 1 HETATM 3360 O O . HOH I 6 . ? 55.292 42.909 -5.021 1.00 37.05 ? 454 HOH A O 1 HETATM 3361 O O . HOH I 6 . ? 36.537 34.325 -8.985 1.00 8.12 ? 455 HOH A O 1 HETATM 3362 O O . HOH I 6 . ? 44.257 50.052 -6.463 1.00 23.74 ? 456 HOH A O 1 HETATM 3363 O O . HOH I 6 . ? 49.198 43.091 7.164 1.00 42.75 ? 457 HOH A O 1 HETATM 3364 O O . HOH I 6 . ? 47.780 44.682 6.337 1.00 37.06 ? 458 HOH A O 1 HETATM 3365 O O . HOH J 6 . ? 48.684 13.682 -20.731 1.00 16.98 ? 301 HOH B O 1 HETATM 3366 O O . HOH J 6 . ? 37.379 24.157 -10.360 1.00 8.76 ? 302 HOH B O 1 HETATM 3367 O O . HOH J 6 . ? 53.290 14.434 -18.061 1.00 11.32 ? 303 HOH B O 1 HETATM 3368 O O . HOH J 6 . ? 50.254 23.279 -21.722 1.00 10.87 ? 304 HOH B O 1 HETATM 3369 O O . HOH J 6 . ? 21.219 17.782 -12.135 1.00 17.48 ? 305 HOH B O 1 HETATM 3370 O O . HOH J 6 . ? 38.424 37.584 -14.405 1.00 19.16 ? 306 HOH B O 1 HETATM 3371 O O . HOH J 6 . ? 52.430 15.256 -15.581 1.00 12.86 ? 307 HOH B O 1 HETATM 3372 O O . HOH J 6 . ? 62.993 18.215 -11.579 1.00 17.74 ? 308 HOH B O 1 HETATM 3373 O O . HOH J 6 . ? 32.273 13.910 -5.151 1.00 13.95 ? 309 HOH B O 1 HETATM 3374 O O . HOH J 6 . ? 38.270 23.029 -12.735 1.00 12.44 ? 310 HOH B O 1 HETATM 3375 O O . HOH J 6 . ? 56.944 15.202 -10.147 1.00 11.22 ? 311 HOH B O 1 HETATM 3376 O O . HOH J 6 . ? 50.869 24.353 -27.456 1.00 23.37 ? 312 HOH B O 1 HETATM 3377 O O . HOH J 6 . ? 9.389 7.986 -15.479 1.00 23.40 ? 313 HOH B O 1 HETATM 3378 O O . HOH J 6 . ? 46.105 15.053 -6.666 1.00 12.24 ? 314 HOH B O 1 HETATM 3379 O O . HOH J 6 . ? 22.742 11.599 -11.622 1.00 16.13 ? 315 HOH B O 1 HETATM 3380 O O . HOH J 6 . ? 52.801 30.536 -24.685 1.00 13.70 ? 316 HOH B O 1 HETATM 3381 O O . HOH J 6 . ? 61.229 29.610 -22.794 1.00 23.50 ? 317 HOH B O 1 HETATM 3382 O O . HOH J 6 . ? 13.906 9.735 1.555 1.00 18.71 ? 318 HOH B O 1 HETATM 3383 O O . HOH J 6 . ? 38.862 21.151 -15.939 1.00 27.16 ? 319 HOH B O 1 HETATM 3384 O O . HOH J 6 . ? 59.798 14.243 -15.482 1.00 17.55 ? 320 HOH B O 1 HETATM 3385 O O . HOH J 6 . ? 7.479 14.461 -18.689 1.00 22.69 ? 321 HOH B O 1 HETATM 3386 O O . HOH J 6 . ? 40.756 28.352 -6.173 1.00 10.40 ? 322 HOH B O 1 HETATM 3387 O O . HOH J 6 . ? 60.177 30.508 -10.875 1.00 20.46 ? 323 HOH B O 1 HETATM 3388 O O . HOH J 6 . ? 28.058 12.704 5.350 1.00 18.74 ? 324 HOH B O 1 HETATM 3389 O O . HOH J 6 . ? 14.849 3.889 -12.183 1.00 26.37 ? 325 HOH B O 1 HETATM 3390 O O . HOH J 6 . ? 51.248 8.941 -18.423 1.00 33.60 ? 326 HOH B O 1 HETATM 3391 O O . HOH J 6 . ? 48.126 24.100 -23.229 1.00 15.41 ? 327 HOH B O 1 HETATM 3392 O O . HOH J 6 . ? 41.278 32.735 -19.845 1.00 14.75 ? 328 HOH B O 1 HETATM 3393 O O . HOH J 6 . ? 10.490 12.344 -18.484 1.00 25.48 ? 329 HOH B O 1 HETATM 3394 O O . HOH J 6 . ? 34.090 7.363 2.433 1.00 14.18 ? 330 HOH B O 1 HETATM 3395 O O . HOH J 6 . ? 3.243 0.780 -10.442 1.00 22.11 ? 331 HOH B O 1 HETATM 3396 O O . HOH J 6 . ? 10.793 14.933 -17.290 1.00 19.37 ? 332 HOH B O 1 HETATM 3397 O O . HOH J 6 . ? 31.983 19.374 -0.123 1.00 16.17 ? 333 HOH B O 1 HETATM 3398 O O . HOH J 6 . ? 7.538 6.055 1.243 1.00 21.53 ? 334 HOH B O 1 HETATM 3399 O O . HOH J 6 . ? 23.628 9.148 3.555 1.00 23.84 ? 335 HOH B O 1 HETATM 3400 O O . HOH J 6 . ? 24.175 21.404 -5.516 1.00 13.75 ? 336 HOH B O 1 HETATM 3401 O O . HOH J 6 . ? 47.598 9.667 -22.699 1.00 36.43 ? 337 HOH B O 1 HETATM 3402 O O . HOH J 6 . ? 24.819 13.348 5.506 1.00 34.18 ? 338 HOH B O 1 HETATM 3403 O O . HOH J 6 . ? -4.884 9.197 -12.900 1.00 33.37 ? 339 HOH B O 1 HETATM 3404 O O . HOH J 6 . ? 67.035 28.810 -19.182 0.50 17.06 ? 340 HOH B O 1 HETATM 3405 O O . HOH J 6 . ? 59.377 35.878 -19.231 1.00 22.24 ? 341 HOH B O 1 HETATM 3406 O O . HOH J 6 . ? 40.094 30.725 -21.918 1.00 26.87 ? 342 HOH B O 1 HETATM 3407 O O . HOH J 6 . ? 64.730 17.565 -19.695 1.00 25.95 ? 343 HOH B O 1 HETATM 3408 O O . HOH J 6 . ? 54.889 29.029 -24.686 1.00 24.25 ? 344 HOH B O 1 HETATM 3409 O O . HOH J 6 . ? 48.280 8.425 -18.968 1.00 28.76 ? 345 HOH B O 1 HETATM 3410 O O . HOH J 6 . ? 14.329 3.224 1.152 1.00 22.03 ? 346 HOH B O 1 HETATM 3411 O O . HOH J 6 . ? 44.779 45.440 -2.050 1.00 14.69 ? 347 HOH B O 1 HETATM 3412 O O . HOH J 6 . ? 17.210 13.552 -11.550 1.00 18.68 ? 348 HOH B O 1 HETATM 3413 O O . HOH J 6 . ? 41.005 38.843 -14.854 1.00 20.46 ? 349 HOH B O 1 HETATM 3414 O O . HOH J 6 . ? 34.102 4.843 2.323 1.00 23.73 ? 350 HOH B O 1 HETATM 3415 O O . HOH J 6 . ? 11.612 11.138 -20.737 1.00 29.77 ? 351 HOH B O 1 HETATM 3416 O O . HOH J 6 . ? 28.472 0.944 0.980 1.00 20.62 ? 352 HOH B O 1 HETATM 3417 O O . HOH J 6 . ? 15.394 10.224 3.833 1.00 31.19 ? 353 HOH B O 1 HETATM 3418 O O . HOH J 6 . ? 42.442 47.193 -2.442 1.00 20.18 ? 354 HOH B O 1 HETATM 3419 O O . HOH J 6 . ? 61.593 32.523 -9.573 1.00 31.80 ? 355 HOH B O 1 HETATM 3420 O O . HOH J 6 . ? 19.109 12.355 -12.721 1.00 37.36 ? 356 HOH B O 1 HETATM 3421 O O . HOH J 6 . ? 29.586 11.723 -7.782 1.00 9.09 ? 357 HOH B O 1 HETATM 3422 O O . HOH J 6 . ? 39.536 31.448 -17.842 1.00 20.88 ? 358 HOH B O 1 HETATM 3423 O O . HOH J 6 . ? 42.601 4.383 0.016 1.00 30.78 ? 359 HOH B O 1 HETATM 3424 O O . HOH J 6 . ? -7.181 3.938 -12.609 1.00 36.86 ? 360 HOH B O 1 HETATM 3425 O O . HOH J 6 . ? -7.308 6.251 -0.322 1.00 35.15 ? 361 HOH B O 1 HETATM 3426 O O . HOH J 6 . ? 41.424 9.352 -4.438 1.00 25.72 ? 362 HOH B O 1 HETATM 3427 O O . HOH J 6 . ? 24.585 -0.855 -10.419 1.00 33.35 ? 363 HOH B O 1 HETATM 3428 O O . HOH J 6 . ? 59.456 38.849 -18.643 1.00 35.43 ? 364 HOH B O 1 HETATM 3429 O O . HOH J 6 . ? 53.835 16.208 -20.068 1.00 10.95 ? 365 HOH B O 1 HETATM 3430 O O . HOH J 6 . ? -8.741 12.083 -16.140 1.00 26.96 ? 366 HOH B O 1 HETATM 3431 O O . HOH J 6 . ? 28.515 47.349 0.924 1.00 34.93 ? 367 HOH B O 1 HETATM 3432 O O . HOH J 6 . ? 43.239 15.388 -23.709 1.00 38.82 ? 368 HOH B O 1 HETATM 3433 O O . HOH J 6 . ? -8.433 2.789 -10.033 1.00 40.00 ? 369 HOH B O 1 HETATM 3434 O O . HOH J 6 . ? 22.551 13.408 3.879 1.00 25.17 ? 370 HOH B O 1 HETATM 3435 O O . HOH J 6 . ? 48.423 4.385 -7.647 1.00 29.94 ? 371 HOH B O 1 HETATM 3436 O O . HOH J 6 . ? 13.085 8.889 -21.028 1.00 35.25 ? 372 HOH B O 1 HETATM 3437 O O . HOH J 6 . ? 40.473 33.069 -22.061 1.00 29.52 ? 373 HOH B O 1 HETATM 3438 O O . HOH J 6 . ? -5.560 4.464 -14.371 1.00 39.57 ? 374 HOH B O 1 HETATM 3439 O O . HOH J 6 . ? 3.330 21.201 -2.624 1.00 37.24 ? 375 HOH B O 1 HETATM 3440 O O . HOH J 6 . ? 60.224 27.406 -10.031 1.00 23.78 ? 376 HOH B O 1 HETATM 3441 O O . HOH J 6 . ? 40.171 35.502 -20.581 1.00 29.25 ? 377 HOH B O 1 HETATM 3442 O O . HOH J 6 . ? 16.761 10.341 -17.381 1.00 39.25 ? 378 HOH B O 1 HETATM 3443 O O . HOH J 6 . ? 48.801 3.566 -10.290 1.00 27.68 ? 379 HOH B O 1 HETATM 3444 O O . HOH J 6 . ? 44.887 17.138 -7.632 1.00 5.50 ? 380 HOH B O 1 HETATM 3445 O O . HOH J 6 . ? 16.505 1.393 -17.703 1.00 33.79 ? 381 HOH B O 1 HETATM 3446 O O . HOH J 6 . ? 11.350 5.645 -25.317 1.00 43.47 ? 382 HOH B O 1 HETATM 3447 O O . HOH J 6 . ? 66.497 15.417 -21.098 1.00 21.98 ? 383 HOH B O 1 HETATM 3448 O O . HOH J 6 . ? 12.998 2.436 3.394 1.00 23.11 ? 384 HOH B O 1 HETATM 3449 O O . HOH J 6 . ? 15.147 12.314 -18.810 1.00 24.41 ? 385 HOH B O 1 HETATM 3450 O O . HOH J 6 . ? 28.731 10.150 -10.073 1.00 27.74 ? 386 HOH B O 1 HETATM 3451 O O . HOH J 6 . ? 32.974 51.265 2.769 1.00 37.65 ? 387 HOH B O 1 HETATM 3452 O O . HOH J 6 . ? 30.732 48.000 -0.236 1.00 48.90 ? 388 HOH B O 1 HETATM 3453 O O . HOH J 6 . ? 15.951 12.538 -16.165 1.00 28.49 ? 389 HOH B O 1 HETATM 3454 O O . HOH J 6 . ? 15.310 17.191 1.103 1.00 26.52 ? 390 HOH B O 1 HETATM 3455 O O . HOH J 6 . ? 26.493 48.737 2.020 1.00 37.81 ? 391 HOH B O 1 HETATM 3456 O O . HOH J 6 . ? 32.850 7.624 -6.536 1.00 23.15 ? 392 HOH B O 1 HETATM 3457 O O . HOH J 6 . ? 49.496 5.465 -3.346 1.00 26.96 ? 393 HOH B O 1 HETATM 3458 O O . HOH J 6 . ? 7.906 -2.632 -4.426 1.00 24.47 ? 394 HOH B O 1 HETATM 3459 O O . HOH J 6 . ? 52.099 34.024 -12.028 1.00 12.43 ? 395 HOH B O 1 HETATM 3460 O O . HOH J 6 . ? 16.975 10.831 -12.880 1.00 17.83 ? 396 HOH B O 1 HETATM 3461 O O . HOH J 6 . ? 39.754 29.154 -19.103 1.00 24.85 ? 397 HOH B O 1 HETATM 3462 O O . HOH J 6 . ? 52.279 40.219 -21.024 1.00 27.05 ? 398 HOH B O 1 HETATM 3463 O O . HOH J 6 . ? 14.682 10.191 -15.100 1.00 36.52 ? 399 HOH B O 1 HETATM 3464 O O . HOH J 6 . ? 7.634 -1.121 -2.131 1.00 32.37 ? 400 HOH B O 1 HETATM 3465 O O . HOH J 6 . ? 13.022 16.039 0.907 1.00 26.19 ? 401 HOH B O 1 HETATM 3466 O O . HOH J 6 . ? 44.477 14.012 -25.146 1.00 37.23 ? 402 HOH B O 1 HETATM 3467 O O . HOH J 6 . ? 29.947 48.653 3.043 1.00 51.79 ? 403 HOH B O 1 HETATM 3468 O O . HOH J 6 . ? 52.939 6.158 -16.377 1.00 28.34 ? 404 HOH B O 1 HETATM 3469 O O . HOH J 6 . ? 61.412 21.849 -23.028 1.00 41.53 ? 405 HOH B O 1 HETATM 3470 O O . HOH J 6 . ? 46.965 28.340 -25.044 1.00 25.20 ? 406 HOH B O 1 HETATM 3471 O O . HOH J 6 . ? 27.519 0.895 3.527 1.00 28.88 ? 407 HOH B O 1 HETATM 3472 O O . HOH J 6 . ? 46.955 42.734 -22.730 1.00 42.48 ? 408 HOH B O 1 HETATM 3473 O O . HOH J 6 . ? 20.648 19.896 -12.622 1.00 32.36 ? 409 HOH B O 1 HETATM 3474 O O . HOH J 6 . ? 61.299 25.017 -23.853 1.00 35.47 ? 410 HOH B O 1 HETATM 3475 O O . HOH J 6 . ? -7.127 12.420 -6.793 1.00 28.86 ? 411 HOH B O 1 HETATM 3476 O O . HOH J 6 . ? 45.627 22.765 -22.991 1.00 11.37 ? 412 HOH B O 1 HETATM 3477 O O . HOH J 6 . ? 44.846 39.318 -20.850 1.00 26.84 ? 413 HOH B O 1 HETATM 3478 O O . HOH J 6 . ? 43.314 41.001 -19.072 1.00 33.64 ? 414 HOH B O 1 HETATM 3479 O O . HOH J 6 . ? 9.554 4.069 1.718 1.00 34.20 ? 415 HOH B O 1 HETATM 3480 O O . HOH J 6 . ? 48.068 32.745 -26.551 1.00 36.69 ? 416 HOH B O 1 HETATM 3481 O O . HOH J 6 . ? 47.522 34.753 -25.707 1.00 37.65 ? 417 HOH B O 1 HETATM 3482 O O . HOH J 6 . ? 14.129 13.251 -15.330 1.00 21.02 ? 418 HOH B O 1 HETATM 3483 O O . HOH J 6 . ? 34.225 45.971 -3.274 1.00 29.07 ? 419 HOH B O 1 HETATM 3484 O O . HOH J 6 . ? 41.113 30.590 -24.384 1.00 27.60 ? 420 HOH B O 1 HETATM 3485 O O . HOH J 6 . ? 57.394 29.754 -23.987 1.00 30.75 ? 421 HOH B O 1 HETATM 3486 O O . HOH J 6 . ? 62.066 34.754 -19.500 1.00 29.42 ? 422 HOH B O 1 HETATM 3487 O O . HOH J 6 . ? 48.287 23.967 -26.540 1.00 30.66 ? 423 HOH B O 1 HETATM 3488 O O . HOH J 6 . ? 28.487 10.241 5.364 1.00 27.12 ? 424 HOH B O 1 HETATM 3489 O O . HOH J 6 . ? 35.197 2.172 2.269 1.00 43.82 ? 425 HOH B O 1 HETATM 3490 O O . HOH J 6 . ? -8.031 8.040 -1.644 1.00 32.30 ? 426 HOH B O 1 HETATM 3491 O O . HOH J 6 . ? 23.862 18.458 -11.712 1.00 33.62 ? 427 HOH B O 1 HETATM 3492 O O . HOH J 6 . ? 60.033 26.290 -26.014 1.00 38.36 ? 428 HOH B O 1 HETATM 3493 O O . HOH K 6 . ? 56.702 26.514 -4.877 1.00 19.58 ? 101 HOH C O 1 HETATM 3494 O O . HOH K 6 . ? 58.028 35.445 -7.937 1.00 26.08 ? 102 HOH C O 1 HETATM 3495 O O . HOH K 6 . ? 51.361 14.995 3.312 1.00 28.87 ? 103 HOH C O 1 HETATM 3496 O O . HOH K 6 . ? 60.658 34.223 -7.023 1.00 35.33 ? 104 HOH C O 1 HETATM 3497 O O . HOH K 6 . ? 61.446 36.923 -11.117 1.00 21.39 ? 105 HOH C O 1 HETATM 3498 O O . HOH K 6 . ? 50.470 4.653 -1.607 1.00 31.75 ? 106 HOH C O 1 HETATM 3499 O O . HOH K 6 . ? 54.711 10.633 -0.195 1.00 31.54 ? 107 HOH C O 1 HETATM 3500 O O . HOH K 6 . ? 58.291 37.724 -6.173 1.00 31.77 ? 108 HOH C 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 ILE 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 GLU 3 3 3 GLU GLU A . n A 1 4 GLU 4 4 4 GLU GLU A . n A 1 5 HIS 5 5 5 HIS HIS A . n A 1 6 VAL 6 6 6 VAL VAL A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 ILE 8 8 8 ILE ILE A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 GLU 11 11 11 GLU GLU A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 TYR 13 13 13 TYR TYR A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 ASN 15 15 15 ASN ASN A . n A 1 16 PRO 16 16 16 PRO PRO A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 GLN 18 18 18 GLN GLN A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 GLY 20 20 20 GLY GLY A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 PHE 22 22 22 PHE PHE A . n A 1 23 MET 23 23 23 MET MET A . n A 1 24 PHE 24 24 24 PHE PHE A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 PHE 26 26 26 PHE PHE A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 GLY 28 28 28 GLY GLY A . n A 1 29 ASP 29 29 29 ASP ASP A . n A 1 30 GLU 30 30 30 GLU GLU A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PHE 32 32 32 PHE PHE A . n A 1 33 HIS 33 33 33 HIS HIS A . n A 1 34 VAL 34 34 34 VAL VAL A . n A 1 35 ASP 35 35 35 ASP ASP A . n A 1 36 MET 36 36 36 MET MET A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 LYS 38 38 38 LYS LYS A . n A 1 39 LYS 39 39 39 LYS LYS A . n A 1 40 GLU 40 40 40 GLU GLU A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 TRP 43 43 43 TRP TRP A . n A 1 44 ARG 44 44 44 ARG ARG A . n A 1 45 LEU 45 45 45 LEU LEU A . n A 1 46 GLU 46 46 46 GLU GLU A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 PHE 48 48 48 PHE PHE A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 SER 53 53 53 SER SER A . n A 1 54 PHE 54 54 54 PHE PHE A . n A 1 55 GLU 55 55 55 GLU GLU A . n A 1 56 ALA 56 56 56 ALA ALA A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 LEU 60 60 60 LEU LEU A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 ALA 64 64 64 ALA ALA A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 ASP 66 66 66 ASP ASP A . n A 1 67 LYS 67 67 67 LYS LYS A . n A 1 68 ALA 68 68 68 ALA ALA A . n A 1 69 ASN 69 69 69 ASN ASN A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 ILE 72 72 72 ILE ILE A . n A 1 73 MET 73 73 73 MET MET A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 LYS 75 75 75 LYS LYS A . n A 1 76 ARG 76 76 76 ARG ARG A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 ASN 78 78 78 ASN ASN A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 PRO 81 81 81 PRO PRO A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 PRO 87 87 87 PRO PRO A . n A 1 88 GLU 88 88 88 GLU GLU A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 THR 90 90 90 THR THR A . n A 1 91 VAL 91 91 91 VAL VAL A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 THR 93 93 93 THR THR A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 VAL 97 97 97 VAL VAL A . n A 1 98 GLU 98 98 98 GLU GLU A . n A 1 99 LEU 99 99 99 LEU LEU A . n A 1 100 ARG 100 100 100 ARG ARG A . n A 1 101 GLU 101 101 101 GLU GLU A . n A 1 102 PRO 102 102 102 PRO PRO A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 CYS 107 107 107 CYS CYS A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ILE 109 109 109 ILE ILE A . n A 1 110 ASP 110 110 110 ASP ASP A . n A 1 111 LYS 111 111 111 LYS LYS A . n A 1 112 PHE 112 112 112 PHE PHE A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 PRO 114 114 114 PRO PRO A . n A 1 115 PRO 115 115 115 PRO PRO A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 THR 120 120 120 THR THR A . n A 1 121 TRP 121 121 121 TRP TRP A . n A 1 122 LEU 122 122 122 LEU LEU A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 ASN 124 124 124 ASN ASN A . n A 1 125 GLY 125 125 125 GLY GLY A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 PRO 127 127 127 PRO PRO A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 THR 129 129 129 THR THR A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 GLY 131 131 131 GLY GLY A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 LEU 138 138 138 LEU LEU A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 ARG 140 140 140 ARG ARG A . n A 1 141 GLU 141 141 141 GLU GLU A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 HIS 143 143 143 HIS HIS A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 PHE 145 145 145 PHE PHE A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 LYS 147 147 147 LYS LYS A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 HIS 149 149 149 HIS HIS A . n A 1 150 TYR 150 150 150 TYR TYR A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 PRO 152 152 152 PRO PRO A . n A 1 153 PHE 153 153 153 PHE PHE A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 PRO 155 155 155 PRO PRO A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 THR 157 157 157 THR THR A . n A 1 158 GLU 158 158 158 GLU GLU A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 CYS 163 163 163 CYS CYS A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 GLU 166 166 166 GLU GLU A . n A 1 167 HIS 167 167 167 HIS HIS A . n A 1 168 TRP 168 168 168 TRP TRP A . n A 1 169 GLY 169 169 169 GLY GLY A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 PRO 173 173 173 PRO PRO A . n A 1 174 LEU 174 174 174 LEU LEU A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 HIS 177 177 177 HIS HIS A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 PHE 180 180 180 PHE PHE A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 THR 182 182 ? ? ? A . n A 1 183 SER 183 183 ? ? ? A . n A 1 184 GLY 184 184 ? ? ? A . n A 1 185 ASP 185 185 ? ? ? A . n A 1 186 ASP 186 186 ? ? ? A . n A 1 187 ASP 187 187 ? ? ? A . n A 1 188 ASP 188 188 ? ? ? A . n A 1 189 LYS 189 189 ? ? ? A . n B 2 1 GLY 1 -1 ? ? ? B . n B 2 2 SER 2 0 ? ? ? B . n B 2 3 GLY 3 1 ? ? ? B . n B 2 4 ASP 4 2 2 ASP ASP B . n B 2 5 THR 5 3 3 THR THR B . n B 2 6 ARG 6 4 4 ARG ARG B . n B 2 7 PRO 7 5 5 PRO PRO B . n B 2 8 ARG 8 6 6 ARG ARG B . n B 2 9 PHE 9 7 7 PHE PHE B . n B 2 10 LEU 10 8 8 LEU LEU B . n B 2 11 GLU 11 9 9 GLU GLU B . n B 2 12 GLN 12 10 10 GLN GLN B . n B 2 13 VAL 13 11 11 VAL VAL B . n B 2 14 LYS 14 12 12 LYS LYS B . n B 2 15 HIS 15 13 13 HIS HIS B . n B 2 16 GLU 16 14 14 GLU GLU B . n B 2 17 CYS 17 15 15 CYS CYS B . n B 2 18 HIS 18 16 16 HIS HIS B . n B 2 19 PHE 19 17 17 PHE PHE B . n B 2 20 PHE 20 18 18 PHE PHE B . n B 2 21 ASN 21 19 19 ASN ASN B . n B 2 22 GLY 22 20 20 GLY GLY B . n B 2 23 THR 23 21 21 THR THR B . n B 2 24 GLU 24 22 22 GLU GLU B . n B 2 25 ARG 25 23 23 ARG ARG B . n B 2 26 VAL 26 24 24 VAL VAL B . n B 2 27 ARG 27 25 25 ARG ARG B . n B 2 28 PHE 28 26 26 PHE PHE B . n B 2 29 LEU 29 27 27 LEU LEU B . n B 2 30 ASP 30 28 28 ASP ASP B . n B 2 31 ARG 31 29 29 ARG ARG B . n B 2 32 TYR 32 30 30 TYR TYR B . n B 2 33 PHE 33 31 31 PHE PHE B . n B 2 34 TYR 34 32 32 TYR TYR B . n B 2 35 HIS 35 33 33 HIS HIS B . n B 2 36 GLN 36 34 34 GLN GLN B . n B 2 37 GLU 37 35 35 GLU GLU B . n B 2 38 GLU 38 36 36 GLU GLU B . n B 2 39 TYR 39 37 37 TYR TYR B . n B 2 40 VAL 40 38 38 VAL VAL B . n B 2 41 ARG 41 39 39 ARG ARG B . n B 2 42 PHE 42 40 40 PHE PHE B . n B 2 43 ASP 43 41 41 ASP ASP B . n B 2 44 SER 44 42 42 SER SER B . n B 2 45 ASP 45 43 43 ASP ASP B . n B 2 46 VAL 46 44 44 VAL VAL B . n B 2 47 GLY 47 45 45 GLY GLY B . n B 2 48 GLU 48 46 46 GLU GLU B . n B 2 49 TYR 49 47 47 TYR TYR B . n B 2 50 ARG 50 48 48 ARG ARG B . n B 2 51 ALA 51 49 49 ALA ALA B . n B 2 52 VAL 52 50 50 VAL VAL B . n B 2 53 THR 53 51 51 THR THR B . n B 2 54 GLU 54 52 52 GLU GLU B . n B 2 55 LEU 55 53 53 LEU LEU B . n B 2 56 GLY 56 54 54 GLY GLY B . n B 2 57 ARG 57 55 55 ARG ARG B . n B 2 58 PRO 58 56 56 PRO PRO B . n B 2 59 ASP 59 57 57 ASP ASP B . n B 2 60 ALA 60 58 58 ALA ALA B . n B 2 61 GLU 61 59 59 GLU GLU B . n B 2 62 TYR 62 60 60 TYR TYR B . n B 2 63 TRP 63 61 61 TRP TRP B . n B 2 64 ASN 64 62 62 ASN ASN B . n B 2 65 SER 65 63 63 SER SER B . n B 2 66 GLN 66 64 64 GLN GLN B . n B 2 67 LYS 67 65 65 LYS LYS B . n B 2 68 ASP 68 66 66 ASP ASP B . n B 2 69 LEU 69 67 67 LEU LEU B . n B 2 70 LEU 70 68 68 LEU LEU B . n B 2 71 GLU 71 69 69 GLU GLU B . n B 2 72 GLN 72 70 70 GLN GLN B . n B 2 73 LYS 73 71 71 LYS LYS B . n B 2 74 ARG 74 72 72 ARG ARG B . n B 2 75 ALA 75 73 73 ALA ALA B . n B 2 76 ALA 76 74 74 ALA ALA B . n B 2 77 VAL 77 75 75 VAL VAL B . n B 2 78 ASP 78 76 76 ASP ASP B . n B 2 79 THR 79 77 77 THR THR B . n B 2 80 TYR 80 78 78 TYR TYR B . n B 2 81 CYS 81 79 79 CYS CYS B . n B 2 82 ARG 82 80 80 ARG ARG B . n B 2 83 HIS 83 81 81 HIS HIS B . n B 2 84 ASN 84 82 82 ASN ASN B . n B 2 85 TYR 85 83 83 TYR TYR B . n B 2 86 GLY 86 84 84 GLY GLY B . n B 2 87 VAL 87 85 85 VAL VAL B . n B 2 88 GLY 88 86 86 GLY GLY B . n B 2 89 GLU 89 87 87 GLU GLU B . n B 2 90 SER 90 88 88 SER SER B . n B 2 91 PHE 91 89 89 PHE PHE B . n B 2 92 THR 92 90 90 THR THR B . n B 2 93 VAL 93 91 91 VAL VAL B . n B 2 94 GLN 94 92 92 GLN GLN B . n B 2 95 ARG 95 93 93 ARG ARG B . n B 2 96 ARG 96 94 94 ARG ARG B . n B 2 97 VAL 97 95 95 VAL VAL B . n B 2 98 TYR 98 96 96 TYR TYR B . n B 2 99 PRO 99 97 97 PRO PRO B . n B 2 100 GLU 100 98 98 GLU GLU B . n B 2 101 VAL 101 99 99 VAL VAL B . n B 2 102 THR 102 100 100 THR THR B . n B 2 103 VAL 103 101 101 VAL VAL B . n B 2 104 TYR 104 102 102 TYR TYR B . n B 2 105 PRO 105 103 103 PRO PRO B . n B 2 106 ALA 106 104 104 ALA ALA B . n B 2 107 LYS 107 105 105 LYS LYS B . n B 2 108 THR 108 106 106 THR THR B . n B 2 109 GLN 109 107 107 GLN GLN B . n B 2 110 PRO 110 108 108 PRO PRO B . n B 2 111 LEU 111 109 109 LEU LEU B . n B 2 112 GLN 112 110 110 GLN GLN B . n B 2 113 HIS 113 111 111 HIS HIS B . n B 2 114 HIS 114 112 112 HIS HIS B . n B 2 115 ASN 115 113 113 ASN ASN B . n B 2 116 LEU 116 114 114 LEU LEU B . n B 2 117 LEU 117 115 115 LEU LEU B . n B 2 118 VAL 118 116 116 VAL VAL B . n B 2 119 CYS 119 117 117 CYS CYS B . n B 2 120 SER 120 118 118 SER SER B . n B 2 121 VAL 121 119 119 VAL VAL B . n B 2 122 ASN 122 120 120 ASN ASN B . n B 2 123 GLY 123 121 121 GLY GLY B . n B 2 124 PHE 124 122 122 PHE PHE B . n B 2 125 TYR 125 123 123 TYR TYR B . n B 2 126 PRO 126 124 124 PRO PRO B . n B 2 127 GLY 127 125 125 GLY GLY B . n B 2 128 SER 128 126 126 SER SER B . n B 2 129 ILE 129 127 127 ILE ILE B . n B 2 130 GLU 130 128 128 GLU GLU B . n B 2 131 VAL 131 129 129 VAL VAL B . n B 2 132 ARG 132 130 130 ARG ARG B . n B 2 133 TRP 133 131 131 TRP TRP B . n B 2 134 PHE 134 132 132 PHE PHE B . n B 2 135 ARG 135 133 133 ARG ARG B . n B 2 136 ASN 136 134 134 ASN ASN B . n B 2 137 GLY 137 135 135 GLY GLY B . n B 2 138 GLN 138 136 136 GLN GLN B . n B 2 139 GLU 139 137 137 GLU GLU B . n B 2 140 GLU 140 138 138 GLU GLU B . n B 2 141 LYS 141 139 139 LYS LYS B . n B 2 142 THR 142 140 140 THR THR B . n B 2 143 GLY 143 141 141 GLY GLY B . n B 2 144 VAL 144 142 142 VAL VAL B . n B 2 145 VAL 145 143 143 VAL VAL B . n B 2 146 SER 146 144 144 SER SER B . n B 2 147 THR 147 145 145 THR THR B . n B 2 148 GLY 148 146 146 GLY GLY B . n B 2 149 LEU 149 147 147 LEU LEU B . n B 2 150 ILE 150 148 148 ILE ILE B . n B 2 151 GLN 151 149 149 GLN GLN B . n B 2 152 ASN 152 150 150 ASN ASN B . n B 2 153 GLY 153 151 151 GLY GLY B . n B 2 154 ASP 154 152 152 ASP ASP B . n B 2 155 TRP 155 153 153 TRP TRP B . n B 2 156 THR 156 154 154 THR THR B . n B 2 157 PHE 157 155 155 PHE PHE B . n B 2 158 GLN 158 156 156 GLN GLN B . n B 2 159 THR 159 157 157 THR THR B . n B 2 160 LEU 160 158 158 LEU LEU B . n B 2 161 VAL 161 159 159 VAL VAL B . n B 2 162 MET 162 160 160 MET MET B . n B 2 163 LEU 163 161 161 LEU LEU B . n B 2 164 GLU 164 162 162 GLU GLU B . n B 2 165 THR 165 163 163 THR THR B . n B 2 166 VAL 166 164 164 VAL VAL B . n B 2 167 PRO 167 165 165 PRO PRO B . n B 2 168 ARG 168 166 166 ARG ARG B . n B 2 169 SER 169 167 167 SER SER B . n B 2 170 GLY 170 168 168 GLY GLY B . n B 2 171 GLU 171 169 169 GLU GLU B . n B 2 172 VAL 172 170 170 VAL VAL B . n B 2 173 TYR 173 171 171 TYR TYR B . n B 2 174 THR 174 172 172 THR THR B . n B 2 175 CYS 175 173 173 CYS CYS B . n B 2 176 GLN 176 174 174 GLN GLN B . n B 2 177 VAL 177 175 175 VAL VAL B . n B 2 178 GLU 178 176 176 GLU GLU B . n B 2 179 HIS 179 177 177 HIS HIS B . n B 2 180 PRO 180 178 178 PRO PRO B . n B 2 181 SER 181 179 179 SER SER B . n B 2 182 LEU 182 180 180 LEU LEU B . n B 2 183 THR 183 181 181 THR THR B . n B 2 184 SER 184 182 182 SER SER B . n B 2 185 PRO 185 183 183 PRO PRO B . n B 2 186 LEU 186 184 184 LEU LEU B . n B 2 187 THR 187 185 185 THR THR B . n B 2 188 VAL 188 186 186 VAL VAL B . n B 2 189 GLU 189 187 187 GLU GLU B . n B 2 190 TRP 190 188 188 TRP TRP B . n B 2 191 ARG 191 189 189 ARG ARG B . n B 2 192 ALA 192 190 190 ALA ALA B . n B 2 193 THR 193 191 ? ? ? B . n B 2 194 GLY 194 192 ? ? ? B . n B 2 195 GLY 195 193 ? ? ? B . n B 2 196 ASP 196 194 ? ? ? B . n B 2 197 ASP 197 195 ? ? ? B . n B 2 198 ASP 198 196 ? ? ? B . n B 2 199 ASP 199 197 ? ? ? B . n B 2 200 LYS 200 198 ? ? ? B . n C 3 1 SER 1 1 1 SER SER C . n C 3 2 ALA 2 2 2 ALA ALA C . n C 3 3 VAL 3 3 3 VAL VAL C . n C 3 4 ARG 4 4 4 ARG ARG C . n C 3 5 LEU 5 5 5 LEU LEU C . n C 3 6 CIR 6 6 6 CIR CIR C . n C 3 7 SER 7 7 7 SER SER C . n C 3 8 SER 8 8 8 SER SER C . n C 3 9 VAL 9 9 9 VAL VAL C . n C 3 10 PRO 10 10 10 PRO PRO C . n C 3 11 GLY 11 11 11 GLY GLY C . n C 3 12 VAL 12 12 12 VAL VAL C . n C 3 13 ARG 13 13 13 ARG ARG C . n # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 B ASN 21 B ASN 19 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 78 A ASN 78 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 118 A ASN 118 ? ASN 'GLYCOSYLATION SITE' 4 C CIR 6 C CIR 6 ? ARG CITRULLINE # _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 trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K # 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)' 7290 ? 1 MORE -26 ? 1 'SSA (A^2)' 18030 ? # _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_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id B _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 340 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id J _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-11-27 2 'Structure model' 1 1 2013-12-04 # _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 ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal Blu-Ice 'data collection' . ? 1 PHASER phasing . ? 2 PHENIX refinement '(phenix.refine: 1.8.2_1309)' ? 3 MOSFLM 'data reduction' . ? 4 SCALA 'data scaling' . ? 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O B HOH 389 ? ? O B HOH 418 ? ? 2.13 2 1 O B HOH 393 ? ? O C HOH 106 ? ? 2.15 3 1 OE2 A GLU 172 ? A O A HOH 430 ? ? 2.16 4 1 O A HOH 418 ? ? O A HOH 419 ? ? 2.19 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ARG A 100 ? ? 49.80 27.70 2 1 HIS B 33 ? ? 59.15 -114.51 3 1 THR B 90 ? ? -123.74 -72.84 4 1 LEU B 109 ? ? 67.33 -28.18 5 1 ASN B 113 ? ? -140.17 19.27 6 1 PRO B 124 ? ? -79.23 -168.43 # 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 B LEU 109 ? CG ? B LEU 111 CG 2 1 Y 1 B LEU 109 ? CD1 ? B LEU 111 CD1 3 1 Y 1 B LEU 109 ? CD2 ? B LEU 111 CD2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ILE 1 ? A ILE 1 2 1 Y 1 A LYS 2 ? A LYS 2 3 1 Y 1 A THR 182 ? A THR 182 4 1 Y 1 A SER 183 ? A SER 183 5 1 Y 1 A GLY 184 ? A GLY 184 6 1 Y 1 A ASP 185 ? A ASP 185 7 1 Y 1 A ASP 186 ? A ASP 186 8 1 Y 1 A ASP 187 ? A ASP 187 9 1 Y 1 A ASP 188 ? A ASP 188 10 1 Y 1 A LYS 189 ? A LYS 189 11 1 Y 1 B GLY -1 ? B GLY 1 12 1 Y 1 B SER 0 ? B SER 2 13 1 Y 1 B GLY 1 ? B GLY 3 14 1 Y 1 B THR 191 ? B THR 193 15 1 Y 1 B GLY 192 ? B GLY 194 16 1 Y 1 B GLY 193 ? B GLY 195 17 1 Y 1 B ASP 194 ? B ASP 196 18 1 Y 1 B ASP 195 ? B ASP 197 19 1 Y 1 B ASP 196 ? B ASP 198 20 1 Y 1 B ASP 197 ? B ASP 199 21 1 Y 1 B LYS 198 ? B LYS 200 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 1,2-ETHANEDIOL EDO 6 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 4 NAG 1 201 500 NAG NAG A . E 4 NAG 1 202 501 NAG NAG A . F 5 EDO 1 203 2 EDO EDO A . G 4 NAG 1 201 500 NAG NAG B . H 5 EDO 1 202 1 EDO EDO B . I 6 HOH 1 301 4 HOH HOH A . I 6 HOH 2 302 6 HOH HOH A . I 6 HOH 3 303 7 HOH HOH A . I 6 HOH 4 304 8 HOH HOH A . I 6 HOH 5 305 9 HOH HOH A . I 6 HOH 6 306 10 HOH HOH A . I 6 HOH 7 307 12 HOH HOH A . I 6 HOH 8 308 14 HOH HOH A . I 6 HOH 9 309 16 HOH HOH A . I 6 HOH 10 310 18 HOH HOH A . I 6 HOH 11 311 19 HOH HOH A . I 6 HOH 12 312 22 HOH HOH A . I 6 HOH 13 313 23 HOH HOH A . I 6 HOH 14 314 24 HOH HOH A . I 6 HOH 15 315 25 HOH HOH A . I 6 HOH 16 316 26 HOH HOH A . I 6 HOH 17 317 31 HOH HOH A . I 6 HOH 18 318 32 HOH HOH A . I 6 HOH 19 319 33 HOH HOH A . I 6 HOH 20 320 34 HOH HOH A . I 6 HOH 21 321 36 HOH HOH A . I 6 HOH 22 322 40 HOH HOH A . I 6 HOH 23 323 50 HOH HOH A . I 6 HOH 24 324 51 HOH HOH A . I 6 HOH 25 325 54 HOH HOH A . I 6 HOH 26 326 55 HOH HOH A . I 6 HOH 27 327 57 HOH HOH A . I 6 HOH 28 328 58 HOH HOH A . I 6 HOH 29 329 61 HOH HOH A . I 6 HOH 30 330 66 HOH HOH A . I 6 HOH 31 331 68 HOH HOH A . I 6 HOH 32 332 69 HOH HOH A . I 6 HOH 33 333 70 HOH HOH A . I 6 HOH 34 334 72 HOH HOH A . I 6 HOH 35 335 73 HOH HOH A . I 6 HOH 36 336 74 HOH HOH A . I 6 HOH 37 337 78 HOH HOH A . I 6 HOH 38 338 79 HOH HOH A . I 6 HOH 39 339 80 HOH HOH A . I 6 HOH 40 340 82 HOH HOH A . I 6 HOH 41 341 83 HOH HOH A . I 6 HOH 42 342 84 HOH HOH A . I 6 HOH 43 343 85 HOH HOH A . I 6 HOH 44 344 86 HOH HOH A . I 6 HOH 45 345 87 HOH HOH A . I 6 HOH 46 346 88 HOH HOH A . I 6 HOH 47 347 89 HOH HOH A . I 6 HOH 48 348 91 HOH HOH A . I 6 HOH 49 349 93 HOH HOH A . I 6 HOH 50 350 94 HOH HOH A . I 6 HOH 51 351 95 HOH HOH A . I 6 HOH 52 352 97 HOH HOH A . I 6 HOH 53 353 100 HOH HOH A . I 6 HOH 54 354 102 HOH HOH A . I 6 HOH 55 355 106 HOH HOH A . I 6 HOH 56 356 108 HOH HOH A . I 6 HOH 57 357 110 HOH HOH A . I 6 HOH 58 358 116 HOH HOH A . I 6 HOH 59 359 117 HOH HOH A . I 6 HOH 60 360 118 HOH HOH A . I 6 HOH 61 361 119 HOH HOH A . I 6 HOH 62 362 120 HOH HOH A . I 6 HOH 63 363 123 HOH HOH A . I 6 HOH 64 364 124 HOH HOH A . I 6 HOH 65 365 125 HOH HOH A . I 6 HOH 66 366 126 HOH HOH A . I 6 HOH 67 367 127 HOH HOH A . I 6 HOH 68 368 128 HOH HOH A . I 6 HOH 69 369 129 HOH HOH A . I 6 HOH 70 370 132 HOH HOH A . I 6 HOH 71 371 133 HOH HOH A . I 6 HOH 72 372 134 HOH HOH A . I 6 HOH 73 373 135 HOH HOH A . I 6 HOH 74 374 137 HOH HOH A . I 6 HOH 75 375 138 HOH HOH A . I 6 HOH 76 376 140 HOH HOH A . I 6 HOH 77 377 144 HOH HOH A . I 6 HOH 78 378 146 HOH HOH A . I 6 HOH 79 379 151 HOH HOH A . I 6 HOH 80 380 155 HOH HOH A . I 6 HOH 81 381 156 HOH HOH A . I 6 HOH 82 382 157 HOH HOH A . I 6 HOH 83 383 161 HOH HOH A . I 6 HOH 84 384 162 HOH HOH A . I 6 HOH 85 385 163 HOH HOH A . I 6 HOH 86 386 165 HOH HOH A . I 6 HOH 87 387 166 HOH HOH A . I 6 HOH 88 388 168 HOH HOH A . I 6 HOH 89 389 170 HOH HOH A . I 6 HOH 90 390 173 HOH HOH A . I 6 HOH 91 391 174 HOH HOH A . I 6 HOH 92 392 175 HOH HOH A . I 6 HOH 93 393 177 HOH HOH A . I 6 HOH 94 394 178 HOH HOH A . I 6 HOH 95 395 181 HOH HOH A . I 6 HOH 96 396 182 HOH HOH A . I 6 HOH 97 397 184 HOH HOH A . I 6 HOH 98 398 187 HOH HOH A . I 6 HOH 99 399 189 HOH HOH A . I 6 HOH 100 400 190 HOH HOH A . I 6 HOH 101 401 191 HOH HOH A . I 6 HOH 102 402 193 HOH HOH A . I 6 HOH 103 403 196 HOH HOH A . I 6 HOH 104 404 198 HOH HOH A . I 6 HOH 105 405 199 HOH HOH A . I 6 HOH 106 406 201 HOH HOH A . I 6 HOH 107 407 202 HOH HOH A . I 6 HOH 108 408 208 HOH HOH A . I 6 HOH 109 409 210 HOH HOH A . I 6 HOH 110 410 214 HOH HOH A . I 6 HOH 111 411 215 HOH HOH A . I 6 HOH 112 412 217 HOH HOH A . I 6 HOH 113 413 220 HOH HOH A . I 6 HOH 114 414 221 HOH HOH A . I 6 HOH 115 415 223 HOH HOH A . I 6 HOH 116 416 227 HOH HOH A . I 6 HOH 117 417 228 HOH HOH A . I 6 HOH 118 418 229 HOH HOH A . I 6 HOH 119 419 233 HOH HOH A . I 6 HOH 120 420 234 HOH HOH A . I 6 HOH 121 421 235 HOH HOH A . I 6 HOH 122 422 236 HOH HOH A . I 6 HOH 123 423 237 HOH HOH A . I 6 HOH 124 424 240 HOH HOH A . I 6 HOH 125 425 245 HOH HOH A . I 6 HOH 126 426 247 HOH HOH A . I 6 HOH 127 427 250 HOH HOH A . I 6 HOH 128 428 251 HOH HOH A . I 6 HOH 129 429 253 HOH HOH A . I 6 HOH 130 430 254 HOH HOH A . I 6 HOH 131 431 258 HOH HOH A . I 6 HOH 132 432 259 HOH HOH A . I 6 HOH 133 433 262 HOH HOH A . I 6 HOH 134 434 263 HOH HOH A . I 6 HOH 135 435 265 HOH HOH A . I 6 HOH 136 436 267 HOH HOH A . I 6 HOH 137 437 272 HOH HOH A . I 6 HOH 138 438 273 HOH HOH A . I 6 HOH 139 439 275 HOH HOH A . I 6 HOH 140 440 276 HOH HOH A . I 6 HOH 141 441 277 HOH HOH A . I 6 HOH 142 442 282 HOH HOH A . I 6 HOH 143 443 284 HOH HOH A . I 6 HOH 144 444 285 HOH HOH A . I 6 HOH 145 445 286 HOH HOH A . I 6 HOH 146 446 288 HOH HOH A . I 6 HOH 147 447 289 HOH HOH A . I 6 HOH 148 448 290 HOH HOH A . I 6 HOH 149 449 291 HOH HOH A . I 6 HOH 150 450 294 HOH HOH A . I 6 HOH 151 451 295 HOH HOH A . I 6 HOH 152 452 301 HOH HOH A . I 6 HOH 153 453 304 HOH HOH A . I 6 HOH 154 454 305 HOH HOH A . I 6 HOH 155 455 306 HOH HOH A . I 6 HOH 156 456 310 HOH HOH A . I 6 HOH 157 457 321 HOH HOH A . I 6 HOH 158 458 324 HOH HOH A . J 6 HOH 1 301 1 HOH HOH B . J 6 HOH 2 302 2 HOH HOH B . J 6 HOH 3 303 3 HOH HOH B . J 6 HOH 4 304 5 HOH HOH B . J 6 HOH 5 305 11 HOH HOH B . J 6 HOH 6 306 13 HOH HOH B . J 6 HOH 7 307 15 HOH HOH B . J 6 HOH 8 308 17 HOH HOH B . J 6 HOH 9 309 20 HOH HOH B . J 6 HOH 10 310 21 HOH HOH B . J 6 HOH 11 311 27 HOH HOH B . J 6 HOH 12 312 28 HOH HOH B . J 6 HOH 13 313 29 HOH HOH B . J 6 HOH 14 314 30 HOH HOH B . J 6 HOH 15 315 35 HOH HOH B . J 6 HOH 16 316 37 HOH HOH B . J 6 HOH 17 317 38 HOH HOH B . J 6 HOH 18 318 39 HOH HOH B . J 6 HOH 19 319 41 HOH HOH B . J 6 HOH 20 320 42 HOH HOH B . J 6 HOH 21 321 43 HOH HOH B . J 6 HOH 22 322 44 HOH HOH B . J 6 HOH 23 323 45 HOH HOH B . J 6 HOH 24 324 46 HOH HOH B . J 6 HOH 25 325 47 HOH HOH B . J 6 HOH 26 326 48 HOH HOH B . J 6 HOH 27 327 49 HOH HOH B . J 6 HOH 28 328 52 HOH HOH B . J 6 HOH 29 329 53 HOH HOH B . J 6 HOH 30 330 56 HOH HOH B . J 6 HOH 31 331 59 HOH HOH B . J 6 HOH 32 332 60 HOH HOH B . J 6 HOH 33 333 62 HOH HOH B . J 6 HOH 34 334 64 HOH HOH B . J 6 HOH 35 335 65 HOH HOH B . J 6 HOH 36 336 67 HOH HOH B . J 6 HOH 37 337 71 HOH HOH B . J 6 HOH 38 338 75 HOH HOH B . J 6 HOH 39 339 76 HOH HOH B . J 6 HOH 40 340 77 HOH HOH B . J 6 HOH 41 341 81 HOH HOH B . J 6 HOH 42 342 92 HOH HOH B . J 6 HOH 43 343 96 HOH HOH B . J 6 HOH 44 344 98 HOH HOH B . J 6 HOH 45 345 99 HOH HOH B . J 6 HOH 46 346 101 HOH HOH B . J 6 HOH 47 347 103 HOH HOH B . J 6 HOH 48 348 104 HOH HOH B . J 6 HOH 49 349 105 HOH HOH B . J 6 HOH 50 350 111 HOH HOH B . J 6 HOH 51 351 112 HOH HOH B . J 6 HOH 52 352 113 HOH HOH B . J 6 HOH 53 353 114 HOH HOH B . J 6 HOH 54 354 115 HOH HOH B . J 6 HOH 55 355 121 HOH HOH B . J 6 HOH 56 356 122 HOH HOH B . J 6 HOH 57 357 130 HOH HOH B . J 6 HOH 58 358 131 HOH HOH B . J 6 HOH 59 359 139 HOH HOH B . J 6 HOH 60 360 141 HOH HOH B . J 6 HOH 61 361 145 HOH HOH B . J 6 HOH 62 362 148 HOH HOH B . J 6 HOH 63 363 149 HOH HOH B . J 6 HOH 64 364 150 HOH HOH B . J 6 HOH 65 365 152 HOH HOH B . J 6 HOH 66 366 154 HOH HOH B . J 6 HOH 67 367 158 HOH HOH B . J 6 HOH 68 368 159 HOH HOH B . J 6 HOH 69 369 160 HOH HOH B . J 6 HOH 70 370 164 HOH HOH B . J 6 HOH 71 371 167 HOH HOH B . J 6 HOH 72 372 169 HOH HOH B . J 6 HOH 73 373 171 HOH HOH B . J 6 HOH 74 374 172 HOH HOH B . J 6 HOH 75 375 176 HOH HOH B . J 6 HOH 76 376 180 HOH HOH B . J 6 HOH 77 377 183 HOH HOH B . J 6 HOH 78 378 185 HOH HOH B . J 6 HOH 79 379 186 HOH HOH B . J 6 HOH 80 380 188 HOH HOH B . J 6 HOH 81 381 194 HOH HOH B . J 6 HOH 82 382 195 HOH HOH B . J 6 HOH 83 383 203 HOH HOH B . J 6 HOH 84 384 204 HOH HOH B . J 6 HOH 85 385 206 HOH HOH B . J 6 HOH 86 386 207 HOH HOH B . J 6 HOH 87 387 211 HOH HOH B . J 6 HOH 88 388 213 HOH HOH B . J 6 HOH 89 389 216 HOH HOH B . J 6 HOH 90 390 219 HOH HOH B . J 6 HOH 91 391 222 HOH HOH B . J 6 HOH 92 392 225 HOH HOH B . J 6 HOH 93 393 230 HOH HOH B . J 6 HOH 94 394 232 HOH HOH B . J 6 HOH 95 395 238 HOH HOH B . J 6 HOH 96 396 239 HOH HOH B . J 6 HOH 97 397 241 HOH HOH B . J 6 HOH 98 398 242 HOH HOH B . J 6 HOH 99 399 243 HOH HOH B . J 6 HOH 100 400 244 HOH HOH B . J 6 HOH 101 401 246 HOH HOH B . J 6 HOH 102 402 248 HOH HOH B . J 6 HOH 103 403 249 HOH HOH B . J 6 HOH 104 404 255 HOH HOH B . J 6 HOH 105 405 256 HOH HOH B . J 6 HOH 106 406 260 HOH HOH B . J 6 HOH 107 407 266 HOH HOH B . J 6 HOH 108 408 268 HOH HOH B . J 6 HOH 109 409 278 HOH HOH B . J 6 HOH 110 410 279 HOH HOH B . J 6 HOH 111 411 283 HOH HOH B . J 6 HOH 112 412 287 HOH HOH B . J 6 HOH 113 413 296 HOH HOH B . J 6 HOH 114 414 298 HOH HOH B . J 6 HOH 115 415 299 HOH HOH B . J 6 HOH 116 416 300 HOH HOH B . J 6 HOH 117 417 303 HOH HOH B . J 6 HOH 118 418 307 HOH HOH B . J 6 HOH 119 419 308 HOH HOH B . J 6 HOH 120 420 312 HOH HOH B . J 6 HOH 121 421 313 HOH HOH B . J 6 HOH 122 422 314 HOH HOH B . J 6 HOH 123 423 315 HOH HOH B . J 6 HOH 124 424 317 HOH HOH B . J 6 HOH 125 425 319 HOH HOH B . J 6 HOH 126 426 320 HOH HOH B . J 6 HOH 127 427 322 HOH HOH B . J 6 HOH 128 428 323 HOH HOH B . K 6 HOH 1 101 63 HOH HOH C . K 6 HOH 2 102 107 HOH HOH C . K 6 HOH 3 103 142 HOH HOH C . K 6 HOH 4 104 153 HOH HOH C . K 6 HOH 5 105 179 HOH HOH C . K 6 HOH 6 106 224 HOH HOH C . K 6 HOH 7 107 226 HOH HOH C . K 6 HOH 8 108 231 HOH HOH C . #