data_1I3V # _entry.id 1I3V # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.398 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code _database_2.pdbx_database_accession _database_2.pdbx_DOI PDB 1I3V pdb_00001i3v 10.2210/pdb1i3v/pdb RCSB RCSB012870 ? ? WWPDB D_1000012870 ? ? # 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 2001-08-08 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2023-08-09 5 'Structure model' 1 4 2024-10-30 # _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_details.details ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' 3 4 'Structure model' 'Data collection' 4 4 'Structure model' 'Database references' 5 4 'Structure model' 'Refinement description' 6 5 'Structure model' 'Structure summary' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' chem_comp_atom 2 4 'Structure model' chem_comp_bond 3 4 'Structure model' database_2 4 4 'Structure model' pdbx_initial_refinement_model 5 5 'Structure model' pdbx_entry_details 6 5 'Structure model' pdbx_modification_feature # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 4 'Structure model' '_database_2.pdbx_DOI' 2 4 'Structure model' '_database_2.pdbx_database_accession' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1I3V _pdbx_database_status.recvd_initial_deposition_date 2001-02-16 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.status_code_nmr_data ? _pdbx_database_status.methods_development_category ? # _pdbx_database_related.db_name PDB _pdbx_database_related.db_id 1I3U _pdbx_database_related.details ;Three-dimensional Structure of a Llama VHH Domain Complexed with the Dye RR1 ; _pdbx_database_related.content_type unspecified # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Spinelli, S.' 1 'Tegoni, M.' 2 'Frenken, L.' 3 'van Vliet, C.' 4 'Cambillau, C.' 5 # _citation.id primary _citation.title 'Lateral recognition of a dye hapten by a llama VHH domain.' _citation.journal_abbrev J.Mol.Biol. _citation.journal_volume 311 _citation.page_first 123 _citation.page_last 129 _citation.year 2001 _citation.journal_id_ASTM JMOBAK _citation.country UK _citation.journal_id_ISSN 0022-2836 _citation.journal_id_CSD 0070 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 11469862 _citation.pdbx_database_id_DOI 10.1006/jmbi.2001.4856 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Spinelli, S.' 1 ? primary 'Tegoni, M.' 2 ? primary 'Frenken, L.' 3 ? primary 'van Vliet, C.' 4 ? primary 'Cambillau, C.' 5 ? # 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 'ANTIBODY VHH LAMA DOMAIN' 14049.452 2 ? ? ? ? 2 water nat water 18.015 146 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;QVQLQESGGGLVQAGDSLKLSCEASGDSIGTYVIGWFRQAPGKERIYLATIGRNLVGPSDFYTRYADSVKGRFAVSRDNA KNTVNLQMNSLKPEDTAVYYCAAKTTTWGGNDPNNWNYWGQGTQVTVSS ; _entity_poly.pdbx_seq_one_letter_code_can ;QVQLQESGGGLVQAGDSLKLSCEASGDSIGTYVIGWFRQAPGKERIYLATIGRNLVGPSDFYTRYADSVKGRFAVSRDNA KNTVNLQMNSLKPEDTAVYYCAAKTTTWGGNDPNNWNYWGQGTQVTVSS ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name water _pdbx_entity_nonpoly.comp_id HOH # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLN n 1 2 VAL n 1 3 GLN n 1 4 LEU n 1 5 GLN n 1 6 GLU n 1 7 SER n 1 8 GLY n 1 9 GLY n 1 10 GLY n 1 11 LEU n 1 12 VAL n 1 13 GLN n 1 14 ALA n 1 15 GLY n 1 16 ASP n 1 17 SER n 1 18 LEU n 1 19 LYS n 1 20 LEU n 1 21 SER n 1 22 CYS n 1 23 GLU n 1 24 ALA n 1 25 SER n 1 26 GLY n 1 27 ASP n 1 28 SER n 1 29 ILE n 1 30 GLY n 1 31 THR n 1 32 TYR n 1 33 VAL n 1 34 ILE n 1 35 GLY n 1 36 TRP n 1 37 PHE n 1 38 ARG n 1 39 GLN n 1 40 ALA n 1 41 PRO n 1 42 GLY n 1 43 LYS n 1 44 GLU n 1 45 ARG n 1 46 ILE n 1 47 TYR n 1 48 LEU n 1 49 ALA n 1 50 THR n 1 51 ILE n 1 52 GLY n 1 53 ARG n 1 54 ASN n 1 55 LEU n 1 56 VAL n 1 57 GLY n 1 58 PRO n 1 59 SER n 1 60 ASP n 1 61 PHE n 1 62 TYR n 1 63 THR n 1 64 ARG n 1 65 TYR n 1 66 ALA n 1 67 ASP n 1 68 SER n 1 69 VAL n 1 70 LYS n 1 71 GLY n 1 72 ARG n 1 73 PHE n 1 74 ALA n 1 75 VAL n 1 76 SER n 1 77 ARG n 1 78 ASP n 1 79 ASN n 1 80 ALA n 1 81 LYS n 1 82 ASN n 1 83 THR n 1 84 VAL n 1 85 ASN n 1 86 LEU n 1 87 GLN n 1 88 MET n 1 89 ASN n 1 90 SER n 1 91 LEU n 1 92 LYS n 1 93 PRO n 1 94 GLU n 1 95 ASP n 1 96 THR n 1 97 ALA n 1 98 VAL n 1 99 TYR n 1 100 TYR n 1 101 CYS n 1 102 ALA n 1 103 ALA n 1 104 LYS n 1 105 THR n 1 106 THR n 1 107 THR n 1 108 TRP n 1 109 GLY n 1 110 GLY n 1 111 ASN n 1 112 ASP n 1 113 PRO n 1 114 ASN n 1 115 ASN n 1 116 TRP n 1 117 ASN n 1 118 TYR n 1 119 TRP n 1 120 GLY n 1 121 GLN n 1 122 GLY n 1 123 THR n 1 124 GLN n 1 125 VAL n 1 126 THR n 1 127 VAL n 1 128 SER n 1 129 SER n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name llama _entity_src_gen.gene_src_genus Lama _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 'Lama glama' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9844 _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 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 _entity_src_gen.host_org_genus Escherichia _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 ? # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 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 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 # 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 GLN 1 1 1 GLN GLN A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 GLN 3 3 3 GLN GLN A . n A 1 4 LEU 4 4 4 LEU LEU A . n A 1 5 GLN 5 5 5 GLN GLN A . n A 1 6 GLU 6 6 6 GLU GLU A . n A 1 7 SER 7 7 7 SER SER A . n A 1 8 GLY 8 8 8 GLY GLY A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 GLY 10 10 10 GLY GLY A . n A 1 11 LEU 11 11 11 LEU LEU A . n A 1 12 VAL 12 12 12 VAL VAL A . n A 1 13 GLN 13 13 13 GLN GLN A . n A 1 14 ALA 14 14 14 ALA ALA A . n A 1 15 GLY 15 15 15 GLY GLY A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 LEU 18 18 18 LEU LEU A . n A 1 19 LYS 19 19 19 LYS LYS A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 SER 21 21 21 SER SER A . n A 1 22 CYS 22 22 22 CYS CYS A . n A 1 23 GLU 23 23 23 GLU GLU A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 SER 25 25 25 SER SER A . n A 1 26 GLY 26 26 26 GLY GLY A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 SER 28 28 28 SER SER A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 GLY 30 30 30 GLY GLY A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 TYR 32 32 32 TYR TYR A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 GLY 35 35 35 GLY GLY A . n A 1 36 TRP 36 36 36 TRP TRP A . n A 1 37 PHE 37 37 37 PHE PHE A . n A 1 38 ARG 38 38 38 ARG ARG A . n A 1 39 GLN 39 39 39 GLN GLN A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 PRO 41 41 41 PRO PRO A . n A 1 42 GLY 42 42 42 GLY GLY A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 GLU 44 44 44 GLU GLU A . n A 1 45 ARG 45 45 45 ARG ARG A . n A 1 46 ILE 46 46 46 ILE ILE A . n A 1 47 TYR 47 47 47 TYR TYR A . n A 1 48 LEU 48 48 48 LEU LEU A . n A 1 49 ALA 49 49 49 ALA ALA A . n A 1 50 THR 50 50 50 THR THR A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASN 54 54 54 ASN ASN A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 VAL 56 56 56 VAL VAL A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 PRO 58 58 58 PRO PRO A . n A 1 59 SER 59 59 59 SER SER A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 PHE 61 61 61 PHE PHE A . n A 1 62 TYR 62 62 62 TYR TYR A . n A 1 63 THR 63 63 63 THR THR A . n A 1 64 ARG 64 64 64 ARG ARG A . n A 1 65 TYR 65 65 65 TYR TYR A . n A 1 66 ALA 66 66 66 ALA ALA A . n A 1 67 ASP 67 67 67 ASP ASP A . n A 1 68 SER 68 68 68 SER SER A . n A 1 69 VAL 69 69 69 VAL VAL A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 GLY 71 71 71 GLY GLY A . n A 1 72 ARG 72 72 72 ARG ARG A . n A 1 73 PHE 73 73 73 PHE PHE A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 SER 76 76 76 SER SER A . n A 1 77 ARG 77 77 77 ARG ARG A . n A 1 78 ASP 78 78 78 ASP ASP A . n A 1 79 ASN 79 79 79 ASN ASN A . n A 1 80 ALA 80 80 80 ALA ALA A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 ASN 82 82 82 ASN ASN A . n A 1 83 THR 83 83 83 THR THR A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 GLN 87 87 87 GLN GLN A . n A 1 88 MET 88 88 88 MET MET A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 SER 90 90 90 SER SER A . n A 1 91 LEU 91 91 91 LEU LEU A . n A 1 92 LYS 92 92 92 LYS LYS A . n A 1 93 PRO 93 93 93 PRO PRO A . n A 1 94 GLU 94 94 94 GLU GLU A . n A 1 95 ASP 95 95 95 ASP ASP A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 ALA 97 97 97 ALA ALA A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 TYR 99 99 99 TYR TYR A . n A 1 100 TYR 100 100 100 TYR TYR A . n A 1 101 CYS 101 101 101 CYS CYS A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 ALA 103 103 103 ALA ALA A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 THR 105 105 105 THR THR A . n A 1 106 THR 106 106 106 THR THR A . n A 1 107 THR 107 107 107 THR THR A . n A 1 108 TRP 108 108 108 TRP TRP A . n A 1 109 GLY 109 109 109 GLY GLY A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 ASN 111 111 111 ASN ASN A . n A 1 112 ASP 112 112 112 ASP ASP A . n A 1 113 PRO 113 113 113 PRO PRO A . n A 1 114 ASN 114 114 114 ASN ASN A . n A 1 115 ASN 115 115 115 ASN ASN A . n A 1 116 TRP 116 116 116 TRP TRP A . n A 1 117 ASN 117 117 117 ASN ASN A . n A 1 118 TYR 118 118 118 TYR TYR A . n A 1 119 TRP 119 119 119 TRP TRP A . n A 1 120 GLY 120 120 120 GLY GLY A . n A 1 121 GLN 121 121 121 GLN GLN A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 THR 123 123 123 THR THR A . n A 1 124 GLN 124 124 124 GLN GLN A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 SER 129 129 129 SER SER A . n B 1 1 GLN 1 1 1 GLN GLN B . n B 1 2 VAL 2 2 2 VAL VAL B . n B 1 3 GLN 3 3 3 GLN GLN B . n B 1 4 LEU 4 4 4 LEU LEU B . n B 1 5 GLN 5 5 5 GLN GLN B . n B 1 6 GLU 6 6 6 GLU GLU B . n B 1 7 SER 7 7 7 SER SER B . n B 1 8 GLY 8 8 8 GLY GLY B . n B 1 9 GLY 9 9 9 GLY GLY B . n B 1 10 GLY 10 10 10 GLY GLY B . n B 1 11 LEU 11 11 11 LEU LEU B . n B 1 12 VAL 12 12 12 VAL VAL B . n B 1 13 GLN 13 13 13 GLN GLN B . n B 1 14 ALA 14 14 14 ALA ALA B . n B 1 15 GLY 15 15 15 GLY GLY B . n B 1 16 ASP 16 16 16 ASP ASP B . n B 1 17 SER 17 17 17 SER SER B . n B 1 18 LEU 18 18 18 LEU LEU B . n B 1 19 LYS 19 19 19 LYS LYS B . n B 1 20 LEU 20 20 20 LEU LEU B . n B 1 21 SER 21 21 21 SER SER B . n B 1 22 CYS 22 22 22 CYS CYS B . n B 1 23 GLU 23 23 23 GLU GLU B . n B 1 24 ALA 24 24 24 ALA ALA B . n B 1 25 SER 25 25 25 SER SER B . n B 1 26 GLY 26 26 26 GLY GLY B . n B 1 27 ASP 27 27 27 ASP ASP B . n B 1 28 SER 28 28 28 SER SER B . n B 1 29 ILE 29 29 29 ILE ILE B . n B 1 30 GLY 30 30 30 GLY GLY B . n B 1 31 THR 31 31 31 THR THR B . n B 1 32 TYR 32 32 32 TYR TYR B . n B 1 33 VAL 33 33 33 VAL VAL B . n B 1 34 ILE 34 34 34 ILE ILE B . n B 1 35 GLY 35 35 35 GLY GLY B . n B 1 36 TRP 36 36 36 TRP TRP B . n B 1 37 PHE 37 37 37 PHE PHE B . n B 1 38 ARG 38 38 38 ARG ARG B . n B 1 39 GLN 39 39 39 GLN GLN B . n B 1 40 ALA 40 40 40 ALA ALA B . n B 1 41 PRO 41 41 41 PRO PRO B . n B 1 42 GLY 42 42 42 GLY GLY B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 GLU 44 44 44 GLU GLU B . n B 1 45 ARG 45 45 45 ARG ARG B . n B 1 46 ILE 46 46 46 ILE ILE B . n B 1 47 TYR 47 47 47 TYR TYR B . n B 1 48 LEU 48 48 48 LEU LEU B . n B 1 49 ALA 49 49 49 ALA ALA B . n B 1 50 THR 50 50 50 THR THR B . n B 1 51 ILE 51 51 51 ILE ILE B . n B 1 52 GLY 52 52 52 GLY GLY B . n B 1 53 ARG 53 53 53 ARG ARG B . n B 1 54 ASN 54 54 54 ASN ASN B . n B 1 55 LEU 55 55 55 LEU LEU B . n B 1 56 VAL 56 56 56 VAL VAL B . n B 1 57 GLY 57 57 57 GLY GLY B . n B 1 58 PRO 58 58 58 PRO PRO B . n B 1 59 SER 59 59 59 SER SER B . n B 1 60 ASP 60 60 60 ASP ASP B . n B 1 61 PHE 61 61 61 PHE PHE B . n B 1 62 TYR 62 62 62 TYR TYR B . n B 1 63 THR 63 63 63 THR THR B . n B 1 64 ARG 64 64 64 ARG ALA B . n B 1 65 TYR 65 65 65 TYR TYR B . n B 1 66 ALA 66 66 66 ALA ALA B . n B 1 67 ASP 67 67 67 ASP ASP B . n B 1 68 SER 68 68 68 SER SER B . n B 1 69 VAL 69 69 69 VAL VAL B . n B 1 70 LYS 70 70 70 LYS LYS B . n B 1 71 GLY 71 71 71 GLY GLY B . n B 1 72 ARG 72 72 72 ARG ARG B . n B 1 73 PHE 73 73 73 PHE PHE B . n B 1 74 ALA 74 74 74 ALA ALA B . n B 1 75 VAL 75 75 75 VAL VAL B . n B 1 76 SER 76 76 76 SER SER B . n B 1 77 ARG 77 77 77 ARG ARG B . n B 1 78 ASP 78 78 78 ASP ASP B . n B 1 79 ASN 79 79 79 ASN ASN B . n B 1 80 ALA 80 80 80 ALA ALA B . n B 1 81 LYS 81 81 81 LYS LYS B . n B 1 82 ASN 82 82 82 ASN ASN B . n B 1 83 THR 83 83 83 THR THR B . n B 1 84 VAL 84 84 84 VAL VAL B . n B 1 85 ASN 85 85 85 ASN ASN B . n B 1 86 LEU 86 86 86 LEU LEU B . n B 1 87 GLN 87 87 87 GLN GLN B . n B 1 88 MET 88 88 88 MET MET B . n B 1 89 ASN 89 89 89 ASN ASN B . n B 1 90 SER 90 90 90 SER SER B . n B 1 91 LEU 91 91 91 LEU LEU B . n B 1 92 LYS 92 92 92 LYS LYS B . n B 1 93 PRO 93 93 93 PRO PRO B . n B 1 94 GLU 94 94 94 GLU GLU B . n B 1 95 ASP 95 95 95 ASP ASP B . n B 1 96 THR 96 96 96 THR THR B . n B 1 97 ALA 97 97 97 ALA ALA B . n B 1 98 VAL 98 98 98 VAL VAL B . n B 1 99 TYR 99 99 99 TYR TYR B . n B 1 100 TYR 100 100 100 TYR TYR B . n B 1 101 CYS 101 101 101 CYS CYS B . n B 1 102 ALA 102 102 102 ALA ALA B . n B 1 103 ALA 103 103 103 ALA ALA B . n B 1 104 LYS 104 104 104 LYS LYS B . n B 1 105 THR 105 105 105 THR THR B . n B 1 106 THR 106 106 106 THR THR B . n B 1 107 THR 107 107 107 THR THR B . n B 1 108 TRP 108 108 108 TRP TRP B . n B 1 109 GLY 109 109 109 GLY GLY B . n B 1 110 GLY 110 110 110 GLY GLY B . n B 1 111 ASN 111 111 111 ASN ASN B . n B 1 112 ASP 112 112 112 ASP ASP B . n B 1 113 PRO 113 113 113 PRO PRO B . n B 1 114 ASN 114 114 114 ASN ASN B . n B 1 115 ASN 115 115 115 ASN ASN B . n B 1 116 TRP 116 116 116 TRP TRP B . n B 1 117 ASN 117 117 117 ASN ASN B . n B 1 118 TYR 118 118 118 TYR TYR B . n B 1 119 TRP 119 119 119 TRP TRP B . n B 1 120 GLY 120 120 120 GLY GLY B . n B 1 121 GLN 121 121 121 GLN GLN B . n B 1 122 GLY 122 122 122 GLY GLY B . n B 1 123 THR 123 123 123 THR THR B . n B 1 124 GLN 124 124 124 GLN GLN B . n B 1 125 VAL 125 125 125 VAL VAL B . n B 1 126 THR 126 126 126 THR THR B . n B 1 127 VAL 127 127 127 VAL VAL B . n B 1 128 SER 128 128 128 SER SER B . n B 1 129 SER 129 129 129 SER SER B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 HOH 1 130 1 HOH WAT A . C 2 HOH 2 131 2 HOH WAT A . C 2 HOH 3 132 3 HOH WAT A . C 2 HOH 4 133 4 HOH WAT A . C 2 HOH 5 134 5 HOH WAT A . C 2 HOH 6 135 6 HOH WAT A . C 2 HOH 7 136 7 HOH WAT A . C 2 HOH 8 137 8 HOH WAT A . C 2 HOH 9 138 9 HOH WAT A . C 2 HOH 10 139 10 HOH WAT A . C 2 HOH 11 140 11 HOH WAT A . C 2 HOH 12 141 13 HOH WAT A . C 2 HOH 13 142 14 HOH WAT A . C 2 HOH 14 143 19 HOH WAT A . C 2 HOH 15 144 20 HOH WAT A . C 2 HOH 16 145 34 HOH WAT A . C 2 HOH 17 146 35 HOH WAT A . C 2 HOH 18 147 36 HOH WAT A . C 2 HOH 19 148 38 HOH WAT A . C 2 HOH 20 149 39 HOH WAT A . C 2 HOH 21 150 42 HOH WAT A . C 2 HOH 22 151 44 HOH WAT A . C 2 HOH 23 152 45 HOH WAT A . C 2 HOH 24 153 46 HOH WAT A . C 2 HOH 25 154 49 HOH WAT A . C 2 HOH 26 155 50 HOH WAT A . C 2 HOH 27 156 52 HOH WAT A . C 2 HOH 28 157 54 HOH WAT A . C 2 HOH 29 158 58 HOH WAT A . C 2 HOH 30 159 59 HOH WAT A . C 2 HOH 31 160 63 HOH WAT A . C 2 HOH 32 161 65 HOH WAT A . C 2 HOH 33 162 66 HOH WAT A . C 2 HOH 34 163 67 HOH WAT A . C 2 HOH 35 164 69 HOH WAT A . C 2 HOH 36 165 70 HOH WAT A . C 2 HOH 37 166 71 HOH WAT A . C 2 HOH 38 167 72 HOH WAT A . C 2 HOH 39 168 75 HOH WAT A . C 2 HOH 40 169 76 HOH WAT A . C 2 HOH 41 170 78 HOH WAT A . C 2 HOH 42 171 79 HOH WAT A . C 2 HOH 43 172 80 HOH WAT A . C 2 HOH 44 173 81 HOH WAT A . C 2 HOH 45 174 84 HOH WAT A . C 2 HOH 46 175 86 HOH WAT A . C 2 HOH 47 176 88 HOH WAT A . C 2 HOH 48 177 90 HOH WAT A . C 2 HOH 49 178 91 HOH WAT A . C 2 HOH 50 179 93 HOH WAT A . C 2 HOH 51 180 94 HOH WAT A . C 2 HOH 52 181 95 HOH WAT A . C 2 HOH 53 182 96 HOH WAT A . C 2 HOH 54 183 98 HOH WAT A . C 2 HOH 55 184 99 HOH WAT A . C 2 HOH 56 185 102 HOH WAT A . C 2 HOH 57 186 104 HOH WAT A . C 2 HOH 58 187 107 HOH WAT A . C 2 HOH 59 188 110 HOH WAT A . C 2 HOH 60 189 111 HOH WAT A . C 2 HOH 61 190 114 HOH WAT A . C 2 HOH 62 191 120 HOH WAT A . C 2 HOH 63 192 121 HOH WAT A . C 2 HOH 64 193 123 HOH WAT A . C 2 HOH 65 194 124 HOH WAT A . C 2 HOH 66 195 125 HOH WAT A . C 2 HOH 67 196 130 HOH WAT A . C 2 HOH 68 197 131 HOH WAT A . C 2 HOH 69 198 132 HOH WAT A . C 2 HOH 70 199 133 HOH WAT A . C 2 HOH 71 200 134 HOH WAT A . C 2 HOH 72 201 135 HOH WAT A . C 2 HOH 73 202 136 HOH WAT A . C 2 HOH 74 203 138 HOH WAT A . C 2 HOH 75 204 141 HOH WAT A . C 2 HOH 76 205 144 HOH WAT A . C 2 HOH 77 206 145 HOH WAT A . C 2 HOH 78 207 147 HOH WAT A . D 2 HOH 1 130 12 HOH WAT B . D 2 HOH 2 131 15 HOH WAT B . D 2 HOH 3 132 16 HOH WAT B . D 2 HOH 4 133 17 HOH WAT B . D 2 HOH 5 134 18 HOH WAT B . D 2 HOH 6 135 21 HOH WAT B . D 2 HOH 7 136 22 HOH WAT B . D 2 HOH 8 137 23 HOH WAT B . D 2 HOH 9 138 24 HOH WAT B . D 2 HOH 10 139 25 HOH WAT B . D 2 HOH 11 140 26 HOH WAT B . D 2 HOH 12 141 27 HOH WAT B . D 2 HOH 13 142 28 HOH WAT B . D 2 HOH 14 143 29 HOH WAT B . D 2 HOH 15 144 30 HOH WAT B . D 2 HOH 16 145 31 HOH WAT B . D 2 HOH 17 146 32 HOH WAT B . D 2 HOH 18 147 33 HOH WAT B . D 2 HOH 19 148 37 HOH WAT B . D 2 HOH 20 149 40 HOH WAT B . D 2 HOH 21 150 41 HOH WAT B . D 2 HOH 22 151 43 HOH WAT B . D 2 HOH 23 152 48 HOH WAT B . D 2 HOH 24 153 51 HOH WAT B . D 2 HOH 25 154 53 HOH WAT B . D 2 HOH 26 155 55 HOH WAT B . D 2 HOH 27 156 56 HOH WAT B . D 2 HOH 28 157 57 HOH WAT B . D 2 HOH 29 158 60 HOH WAT B . D 2 HOH 30 159 61 HOH WAT B . D 2 HOH 31 160 62 HOH WAT B . D 2 HOH 32 161 64 HOH WAT B . D 2 HOH 33 162 68 HOH WAT B . D 2 HOH 34 163 73 HOH WAT B . D 2 HOH 35 164 74 HOH WAT B . D 2 HOH 36 165 77 HOH WAT B . D 2 HOH 37 166 82 HOH WAT B . D 2 HOH 38 167 83 HOH WAT B . D 2 HOH 39 168 85 HOH WAT B . D 2 HOH 40 169 87 HOH WAT B . D 2 HOH 41 170 89 HOH WAT B . D 2 HOH 42 171 92 HOH WAT B . D 2 HOH 43 172 97 HOH WAT B . D 2 HOH 44 173 100 HOH WAT B . D 2 HOH 45 174 101 HOH WAT B . D 2 HOH 46 175 103 HOH WAT B . D 2 HOH 47 176 105 HOH WAT B . D 2 HOH 48 177 106 HOH WAT B . D 2 HOH 49 178 108 HOH WAT B . D 2 HOH 50 179 109 HOH WAT B . D 2 HOH 51 180 112 HOH WAT B . D 2 HOH 52 181 113 HOH WAT B . D 2 HOH 53 182 115 HOH WAT B . D 2 HOH 54 183 116 HOH WAT B . D 2 HOH 55 184 117 HOH WAT B . D 2 HOH 56 185 118 HOH WAT B . D 2 HOH 57 186 119 HOH WAT B . D 2 HOH 58 187 122 HOH WAT B . D 2 HOH 59 188 126 HOH WAT B . D 2 HOH 60 189 127 HOH WAT B . D 2 HOH 61 190 128 HOH WAT B . D 2 HOH 62 191 129 HOH WAT B . D 2 HOH 63 192 137 HOH WAT B . D 2 HOH 64 193 139 HOH WAT B . D 2 HOH 65 194 140 HOH WAT B . D 2 HOH 66 195 142 HOH WAT B . D 2 HOH 67 196 143 HOH WAT B . D 2 HOH 68 197 146 HOH WAT B . # 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 ARG 64 ? CG ? B ARG 64 CG 2 1 Y 1 B ARG 64 ? CD ? B ARG 64 CD 3 1 Y 1 B ARG 64 ? NE ? B ARG 64 NE 4 1 Y 1 B ARG 64 ? CZ ? B ARG 64 CZ 5 1 Y 1 B ARG 64 ? NH1 ? B ARG 64 NH1 6 1 Y 1 B ARG 64 ? NH2 ? B ARG 64 NH2 # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 AMoRE phasing . ? 3 CNS refinement 1.0 ? 4 # _cell.entry_id 1I3V _cell.length_a 41.669 _cell.length_b 56.088 _cell.length_c 102.365 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1I3V _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # _exptl.entry_id 1I3V _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.13 _exptl_crystal.density_percent_sol 42.20 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 290 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_details 'PEG MME 5000, Sodium Acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 298.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU200' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1I3V _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 25.0 _reflns.d_resolution_high 2.01 _reflns.number_obs 16273 _reflns.number_all 57618 _reflns.percent_possible_obs 94.6 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.046 _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 24.8 _reflns.pdbx_redundancy 2.2 _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_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 2.01 _reflns_shell.d_res_low 2.12 _reflns_shell.percent_possible_all 94.6 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.169 _reflns_shell.meanI_over_sigI_obs 4 _reflns_shell.pdbx_redundancy 1.9 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 2005 _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 1I3V _refine.ls_number_reflns_obs 15339 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF 1727957.46 _refine.pdbx_data_cutoff_low_absF 0.00 _refine.ls_d_res_low 14.60 _refine.ls_d_res_high 2.03 _refine.ls_percent_reflns_obs 95.4 _refine.ls_R_factor_obs 0.212 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.212 _refine.ls_R_factor_R_free 0.25 _refine.ls_R_factor_R_free_error 0.008 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 6.9 _refine.ls_number_reflns_R_free 1066 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean 26.3 _refine.aniso_B[1][1] -3.63 _refine.aniso_B[2][2] 3.18 _refine.aniso_B[3][3] 0.45 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.350 _refine.solvent_model_param_bsol 42.72 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1I3U' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_analyze.entry_id 1I3V _refine_analyze.Luzzati_coordinate_error_obs 0.25 _refine_analyze.Luzzati_sigma_a_obs 0.21 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.31 _refine_analyze.Luzzati_sigma_a_free 0.27 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1974 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 0 _refine_hist.number_atoms_solvent 147 _refine_hist.number_atoms_total 2121 _refine_hist.d_res_high 2.03 _refine_hist.d_res_low 14.60 # 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 c_bond_d 0.02 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 2.3 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 28.0 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 1.35 ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.17 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 1.97 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 1.72 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 2.64 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.03 _refine_ls_shell.d_res_low 2.16 _refine_ls_shell.number_reflns_R_work 2328 _refine_ls_shell.R_factor_R_work 0.272 _refine_ls_shell.percent_reflns_obs 95.5 _refine_ls_shell.R_factor_R_free 0.345 _refine_ls_shell.R_factor_R_free_error 0.026 _refine_ls_shell.percent_reflns_R_free 7.0 _refine_ls_shell.number_reflns_R_free 174 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 2 WATER_REP.PARAM WATER.TOP 'X-RAY DIFFRACTION' # _database_PDB_matrix.entry_id 1I3V _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 # _struct.entry_id 1I3V _struct.title 'THREE-DIMENSIONAL STRUCTURE OF A LAMA VHH DOMAIN UNLIGANDED' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1I3V _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text 'antibody, domain VHH, Lama, 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 1 ? C N N 2 ? D N N 2 ? # _struct_ref.id 1 _struct_ref.entity_id 1 _struct_ref.db_name PDB _struct_ref.db_code 1I3V _struct_ref.pdbx_db_accession 1I3V _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? # 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 1I3V A 1 ? 129 ? 1I3V 1 ? 129 ? 1 129 2 1 1I3V B 1 ? 129 ? 1I3V 1 ? 129 ? 1 129 # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C 2 1 B,D # _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 # loop_ _struct_biol.id _struct_biol.pdbx_parent_biol_id _struct_biol.details 1 ? ? 2 ? ? # 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 SER A 28 ? TYR A 32 ? SER A 28 TYR A 32 5 ? 5 HELX_P HELX_P2 2 ASN A 79 ? LYS A 81 ? ASN A 79 LYS A 81 5 ? 3 HELX_P HELX_P3 3 LYS A 92 ? THR A 96 ? LYS A 92 THR A 96 5 ? 5 HELX_P HELX_P4 4 SER B 28 ? TYR B 32 ? SER B 28 TYR B 32 5 ? 5 HELX_P HELX_P5 5 ASN B 79 ? LYS B 81 ? ASN B 79 LYS B 81 5 ? 3 HELX_P HELX_P6 6 LYS B 92 ? THR B 96 ? LYS B 92 THR B 96 5 ? 5 HELX_P HELX_P7 7 ASP B 112 ? TRP B 116 ? ASP B 112 TRP B 116 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order _struct_conn.pdbx_role disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 101 SG ? ? A CYS 22 A CYS 101 1_555 ? ? ? ? ? ? ? 2.210 ? ? disulf2 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 101 SG ? ? B CYS 22 B CYS 101 1_555 ? ? ? ? ? ? ? 2.230 ? ? # _struct_conn_type.id disulf _struct_conn_type.criteria ? _struct_conn_type.reference ? # loop_ _pdbx_modification_feature.ordinal _pdbx_modification_feature.label_comp_id _pdbx_modification_feature.label_asym_id _pdbx_modification_feature.label_seq_id _pdbx_modification_feature.label_alt_id _pdbx_modification_feature.modified_residue_label_comp_id _pdbx_modification_feature.modified_residue_label_asym_id _pdbx_modification_feature.modified_residue_label_seq_id _pdbx_modification_feature.modified_residue_label_alt_id _pdbx_modification_feature.auth_comp_id _pdbx_modification_feature.auth_asym_id _pdbx_modification_feature.auth_seq_id _pdbx_modification_feature.PDB_ins_code _pdbx_modification_feature.symmetry _pdbx_modification_feature.modified_residue_auth_comp_id _pdbx_modification_feature.modified_residue_auth_asym_id _pdbx_modification_feature.modified_residue_auth_seq_id _pdbx_modification_feature.modified_residue_PDB_ins_code _pdbx_modification_feature.modified_residue_symmetry _pdbx_modification_feature.comp_id_linking_atom _pdbx_modification_feature.modified_residue_id_linking_atom _pdbx_modification_feature.modified_residue_id _pdbx_modification_feature.ref_pcm_id _pdbx_modification_feature.ref_comp_id _pdbx_modification_feature.type _pdbx_modification_feature.category 1 CYS A 22 ? CYS A 101 ? CYS A 22 ? 1_555 CYS A 101 ? 1_555 SG SG . . . None 'Disulfide bridge' 2 CYS B 22 ? CYS B 101 ? CYS B 22 ? 1_555 CYS B 101 ? 1_555 SG SG . . . None 'Disulfide bridge' # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 5 ? C ? 6 ? D ? 4 ? E ? 5 ? F ? 6 ? # 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 B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? 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 E 4 5 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel F 4 5 ? anti-parallel F 5 6 ? 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 GLN A 3 ? SER A 7 ? GLN A 3 SER A 7 A 2 LEU A 18 ? SER A 25 ? LEU A 18 SER A 25 A 3 THR A 83 ? MET A 88 ? THR A 83 MET A 88 A 4 PHE A 73 ? ASP A 78 ? PHE A 73 ASP A 78 B 1 ASP A 60 ? TYR A 65 ? ASP A 60 TYR A 65 B 2 ILE A 46 ? GLY A 57 ? ILE A 46 GLY A 57 B 3 VAL A 33 ? GLN A 39 ? VAL A 33 GLN A 39 B 4 ALA A 97 ? LYS A 104 ? ALA A 97 LYS A 104 B 5 TYR A 118 ? TRP A 119 ? TYR A 118 TRP A 119 C 1 ASP A 60 ? TYR A 65 ? ASP A 60 TYR A 65 C 2 ILE A 46 ? GLY A 57 ? ILE A 46 GLY A 57 C 3 VAL A 33 ? GLN A 39 ? VAL A 33 GLN A 39 C 4 ALA A 97 ? LYS A 104 ? ALA A 97 LYS A 104 C 5 THR A 123 ? SER A 128 ? THR A 123 SER A 128 C 6 LEU A 11 ? GLN A 13 ? LEU A 11 GLN A 13 D 1 GLN B 3 ? SER B 7 ? GLN B 3 SER B 7 D 2 LEU B 18 ? SER B 25 ? LEU B 18 SER B 25 D 3 THR B 83 ? MET B 88 ? THR B 83 MET B 88 D 4 PHE B 73 ? ASP B 78 ? PHE B 73 ASP B 78 E 1 ASP B 60 ? TYR B 65 ? ASP B 60 TYR B 65 E 2 ILE B 46 ? GLY B 57 ? ILE B 46 GLY B 57 E 3 VAL B 33 ? GLN B 39 ? VAL B 33 GLN B 39 E 4 ALA B 97 ? LYS B 104 ? ALA B 97 LYS B 104 E 5 TYR B 118 ? TRP B 119 ? TYR B 118 TRP B 119 F 1 ASP B 60 ? TYR B 65 ? ASP B 60 TYR B 65 F 2 ILE B 46 ? GLY B 57 ? ILE B 46 GLY B 57 F 3 VAL B 33 ? GLN B 39 ? VAL B 33 GLN B 39 F 4 ALA B 97 ? LYS B 104 ? ALA B 97 LYS B 104 F 5 THR B 123 ? SER B 128 ? THR B 123 SER B 128 F 6 GLY B 10 ? GLN B 13 ? GLY B 10 GLN B 13 # 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 SER A 7 ? O SER A 7 N SER A 21 ? N SER A 21 A 2 3 N CYS A 22 ? N CYS A 22 O VAL A 84 ? O VAL A 84 A 3 4 N GLN A 87 ? N GLN A 87 O ALA A 74 ? O ALA A 74 B 1 2 O ARG A 64 ? O ARG A 64 N THR A 50 ? N THR A 50 B 2 3 N ILE A 51 ? N ILE A 51 O ILE A 34 ? O ILE A 34 B 3 4 N GLN A 39 ? N GLN A 39 O VAL A 98 ? O VAL A 98 B 4 5 N ALA A 103 ? N ALA A 103 O TYR A 118 ? O TYR A 118 C 1 2 O ARG A 64 ? O ARG A 64 N THR A 50 ? N THR A 50 C 2 3 N ILE A 51 ? N ILE A 51 O ILE A 34 ? O ILE A 34 C 3 4 N GLN A 39 ? N GLN A 39 O VAL A 98 ? O VAL A 98 C 4 5 N TYR A 99 ? N TYR A 99 O THR A 123 ? O THR A 123 C 5 6 O THR A 126 ? O THR A 126 N VAL A 12 ? N VAL A 12 D 1 2 O SER B 7 ? O SER B 7 N SER B 21 ? N SER B 21 D 2 3 N CYS B 22 ? N CYS B 22 O VAL B 84 ? O VAL B 84 D 3 4 N GLN B 87 ? N GLN B 87 O ALA B 74 ? O ALA B 74 E 1 2 O ARG B 64 ? O ARG B 64 N THR B 50 ? N THR B 50 E 2 3 N ILE B 51 ? N ILE B 51 O ILE B 34 ? O ILE B 34 E 3 4 N GLN B 39 ? N GLN B 39 O VAL B 98 ? O VAL B 98 E 4 5 N ALA B 103 ? N ALA B 103 O TYR B 118 ? O TYR B 118 F 1 2 O ARG B 64 ? O ARG B 64 N THR B 50 ? N THR B 50 F 2 3 N ILE B 51 ? N ILE B 51 O ILE B 34 ? O ILE B 34 F 3 4 N GLN B 39 ? N GLN B 39 O VAL B 98 ? O VAL B 98 F 4 5 N TYR B 99 ? N TYR B 99 O THR B 123 ? O THR B 123 F 5 6 N THR B 126 ? N THR B 126 O GLY B 10 ? O GLY B 10 # _pdbx_entry_details.entry_id 1I3V _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ? _pdbx_entry_details.has_ligand_of_interest ? _pdbx_entry_details.has_protein_modification Y # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CB _pdbx_validate_rmsd_bond.auth_asym_id_1 B _pdbx_validate_rmsd_bond.auth_comp_id_1 CYS _pdbx_validate_rmsd_bond.auth_seq_id_1 101 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 SG _pdbx_validate_rmsd_bond.auth_asym_id_2 B _pdbx_validate_rmsd_bond.auth_comp_id_2 CYS _pdbx_validate_rmsd_bond.auth_seq_id_2 101 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.715 _pdbx_validate_rmsd_bond.bond_target_value 1.812 _pdbx_validate_rmsd_bond.bond_deviation -0.097 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.016 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A VAL 2 ? ? CA A VAL 2 ? ? C A VAL 2 ? ? 97.92 111.40 -13.48 1.90 N 2 1 NE A ARG 72 ? ? CZ A ARG 72 ? ? NH2 A ARG 72 ? ? 117.29 120.30 -3.01 0.50 N 3 1 CG A ARG 77 ? ? CD A ARG 77 ? ? NE A ARG 77 ? ? 95.14 111.80 -16.66 2.10 N 4 1 CD A ARG 77 ? ? NE A ARG 77 ? ? CZ A ARG 77 ? ? 135.94 123.60 12.34 1.40 N 5 1 NE A ARG 77 ? ? CZ A ARG 77 ? ? NH1 A ARG 77 ? ? 135.37 120.30 15.07 0.50 N 6 1 NE A ARG 77 ? ? CZ A ARG 77 ? ? NH2 A ARG 77 ? ? 104.56 120.30 -15.74 0.50 N 7 1 N A ASP 78 ? ? CA A ASP 78 ? ? CB A ASP 78 ? ? 124.09 110.60 13.49 1.80 N 8 1 CB A ASP 78 ? ? CG A ASP 78 ? ? OD1 A ASP 78 ? ? 124.76 118.30 6.46 0.90 N 9 1 N A GLY 110 ? ? CA A GLY 110 ? ? C A GLY 110 ? ? 128.70 113.10 15.60 2.50 N 10 1 N B GLY 110 ? ? CA B GLY 110 ? ? C B GLY 110 ? ? 131.81 113.10 18.71 2.50 N 11 1 N B ASN 111 ? ? CA B ASN 111 ? ? C B ASN 111 ? ? 129.59 111.00 18.59 2.70 N 12 1 N B SER 129 ? ? CA B SER 129 ? ? C B SER 129 ? ? 93.22 111.00 -17.78 2.70 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PRO A 41 ? ? -25.79 -43.95 2 1 ALA A 97 ? ? 177.96 178.38 3 1 PRO B 41 ? ? -18.87 -60.79 4 1 ALA B 97 ? ? 177.89 -178.56 5 1 ASN B 115 ? ? -120.00 60.60 # loop_ _chem_comp_atom.comp_id _chem_comp_atom.atom_id _chem_comp_atom.type_symbol _chem_comp_atom.pdbx_aromatic_flag _chem_comp_atom.pdbx_stereo_config _chem_comp_atom.pdbx_ordinal ALA N N N N 1 ALA CA C N S 2 ALA C C N N 3 ALA O O N N 4 ALA CB C N N 5 ALA OXT O N N 6 ALA H H N N 7 ALA H2 H N N 8 ALA HA H N N 9 ALA HB1 H N N 10 ALA HB2 H N N 11 ALA HB3 H N N 12 ALA HXT H N N 13 ARG N N N N 14 ARG CA C N S 15 ARG C C N N 16 ARG O O N N 17 ARG CB C N N 18 ARG CG C N N 19 ARG CD C N N 20 ARG NE N N N 21 ARG CZ C N N 22 ARG NH1 N N N 23 ARG NH2 N N N 24 ARG OXT O N N 25 ARG H H N N 26 ARG H2 H N N 27 ARG HA H N N 28 ARG HB2 H N N 29 ARG HB3 H N N 30 ARG HG2 H N N 31 ARG HG3 H N N 32 ARG HD2 H N N 33 ARG HD3 H N N 34 ARG HE H N N 35 ARG HH11 H N N 36 ARG HH12 H N N 37 ARG HH21 H N N 38 ARG HH22 H N N 39 ARG HXT H N N 40 ASN N N N N 41 ASN CA C N S 42 ASN C C N N 43 ASN O O N N 44 ASN CB C N N 45 ASN CG C N N 46 ASN OD1 O N N 47 ASN ND2 N N N 48 ASN OXT O N N 49 ASN H H N N 50 ASN H2 H N N 51 ASN HA H N N 52 ASN HB2 H N N 53 ASN HB3 H N N 54 ASN HD21 H N N 55 ASN HD22 H N N 56 ASN HXT H N N 57 ASP N N N N 58 ASP CA C N S 59 ASP C C N N 60 ASP O O N N 61 ASP CB C N N 62 ASP CG C N N 63 ASP OD1 O N N 64 ASP OD2 O N N 65 ASP OXT O N N 66 ASP H H N N 67 ASP H2 H N N 68 ASP HA H N N 69 ASP HB2 H N N 70 ASP HB3 H N N 71 ASP HD2 H N N 72 ASP HXT H N N 73 CYS N N N N 74 CYS CA C N R 75 CYS C C N N 76 CYS O O N N 77 CYS CB C N N 78 CYS SG S N N 79 CYS OXT O N N 80 CYS H H N N 81 CYS H2 H N N 82 CYS HA H N N 83 CYS HB2 H N N 84 CYS HB3 H N N 85 CYS HG H N N 86 CYS HXT H N N 87 GLN N N N N 88 GLN CA C N S 89 GLN C C N N 90 GLN O O N N 91 GLN CB C N N 92 GLN CG C N N 93 GLN CD C N N 94 GLN OE1 O N N 95 GLN NE2 N N N 96 GLN OXT O N N 97 GLN H H N N 98 GLN H2 H N N 99 GLN HA H N N 100 GLN HB2 H N N 101 GLN HB3 H N N 102 GLN HG2 H N N 103 GLN HG3 H N N 104 GLN HE21 H N N 105 GLN HE22 H N N 106 GLN HXT H N N 107 GLU N N N N 108 GLU CA C N S 109 GLU C C N N 110 GLU O O N N 111 GLU CB C N N 112 GLU CG C N N 113 GLU CD C N N 114 GLU OE1 O N N 115 GLU OE2 O N N 116 GLU OXT O N N 117 GLU H H N N 118 GLU H2 H N N 119 GLU HA H N N 120 GLU HB2 H N N 121 GLU HB3 H N N 122 GLU HG2 H N N 123 GLU HG3 H N N 124 GLU HE2 H N N 125 GLU HXT H N N 126 GLY N N N N 127 GLY CA C N N 128 GLY C C N N 129 GLY O O N N 130 GLY OXT O N N 131 GLY H H N N 132 GLY H2 H N N 133 GLY HA2 H N N 134 GLY HA3 H N N 135 GLY HXT H N N 136 HOH O O N N 137 HOH H1 H N N 138 HOH H2 H N N 139 ILE N N N N 140 ILE CA C N S 141 ILE C C N N 142 ILE O O N N 143 ILE CB C N S 144 ILE CG1 C N N 145 ILE CG2 C N N 146 ILE CD1 C N N 147 ILE OXT O N N 148 ILE H H N N 149 ILE H2 H N N 150 ILE HA H N N 151 ILE HB H N N 152 ILE HG12 H N N 153 ILE HG13 H N N 154 ILE HG21 H N N 155 ILE HG22 H N N 156 ILE HG23 H N N 157 ILE HD11 H N N 158 ILE HD12 H N N 159 ILE HD13 H N N 160 ILE HXT H N N 161 LEU N N N N 162 LEU CA C N S 163 LEU C C N N 164 LEU O O N N 165 LEU CB C N N 166 LEU CG C N N 167 LEU CD1 C N N 168 LEU CD2 C N N 169 LEU OXT O N N 170 LEU H H N N 171 LEU H2 H N N 172 LEU HA H N N 173 LEU HB2 H N N 174 LEU HB3 H N N 175 LEU HG H N N 176 LEU HD11 H N N 177 LEU HD12 H N N 178 LEU HD13 H N N 179 LEU HD21 H N N 180 LEU HD22 H N N 181 LEU HD23 H N N 182 LEU HXT H N N 183 LYS N N N N 184 LYS CA C N S 185 LYS C C N N 186 LYS O O N N 187 LYS CB C N N 188 LYS CG C N N 189 LYS CD C N N 190 LYS CE C N N 191 LYS NZ N N N 192 LYS OXT O N N 193 LYS H H N N 194 LYS H2 H N N 195 LYS HA H N N 196 LYS HB2 H N N 197 LYS HB3 H N N 198 LYS HG2 H N N 199 LYS HG3 H N N 200 LYS HD2 H N N 201 LYS HD3 H N N 202 LYS HE2 H N N 203 LYS HE3 H N N 204 LYS HZ1 H N N 205 LYS HZ2 H N N 206 LYS HZ3 H N N 207 LYS HXT H N N 208 MET N N N N 209 MET CA C N S 210 MET C C N N 211 MET O O N N 212 MET CB C N N 213 MET CG C N N 214 MET SD S N N 215 MET CE C N N 216 MET OXT O N N 217 MET H H N N 218 MET H2 H N N 219 MET HA H N N 220 MET HB2 H N N 221 MET HB3 H N N 222 MET HG2 H N N 223 MET HG3 H N N 224 MET HE1 H N N 225 MET HE2 H N N 226 MET HE3 H N N 227 MET HXT H N N 228 PHE N N N N 229 PHE CA C N S 230 PHE C C N N 231 PHE O O N N 232 PHE CB C N N 233 PHE CG C Y N 234 PHE CD1 C Y N 235 PHE CD2 C Y N 236 PHE CE1 C Y N 237 PHE CE2 C Y N 238 PHE CZ C Y N 239 PHE OXT O N N 240 PHE H H N N 241 PHE H2 H N N 242 PHE HA H N N 243 PHE HB2 H N N 244 PHE HB3 H N N 245 PHE HD1 H N N 246 PHE HD2 H N N 247 PHE HE1 H N N 248 PHE HE2 H N N 249 PHE HZ H N N 250 PHE HXT H N N 251 PRO N N N N 252 PRO CA C N S 253 PRO C C N N 254 PRO O O N N 255 PRO CB C N N 256 PRO CG C N N 257 PRO CD C N N 258 PRO OXT O N N 259 PRO H H N N 260 PRO HA H N N 261 PRO HB2 H N N 262 PRO HB3 H N N 263 PRO HG2 H N N 264 PRO HG3 H N N 265 PRO HD2 H N N 266 PRO HD3 H N N 267 PRO HXT H N N 268 SER N N N N 269 SER CA C N S 270 SER C C N N 271 SER O O N N 272 SER CB C N N 273 SER OG O N N 274 SER OXT O N N 275 SER H H N N 276 SER H2 H N N 277 SER HA H N N 278 SER HB2 H N N 279 SER HB3 H N N 280 SER HG H N N 281 SER HXT H N N 282 THR N N N N 283 THR CA C N S 284 THR C C N N 285 THR O O N N 286 THR CB C N R 287 THR OG1 O N N 288 THR CG2 C N N 289 THR OXT O N N 290 THR H H N N 291 THR H2 H N N 292 THR HA H N N 293 THR HB H N N 294 THR HG1 H N N 295 THR HG21 H N N 296 THR HG22 H N N 297 THR HG23 H N N 298 THR HXT H N N 299 TRP N N N N 300 TRP CA C N S 301 TRP C C N N 302 TRP O O N N 303 TRP CB C N N 304 TRP CG C Y N 305 TRP CD1 C Y N 306 TRP CD2 C Y N 307 TRP NE1 N Y N 308 TRP CE2 C Y N 309 TRP CE3 C Y N 310 TRP CZ2 C Y N 311 TRP CZ3 C Y N 312 TRP CH2 C Y N 313 TRP OXT O N N 314 TRP H H N N 315 TRP H2 H N N 316 TRP HA H N N 317 TRP HB2 H N N 318 TRP HB3 H N N 319 TRP HD1 H N N 320 TRP HE1 H N N 321 TRP HE3 H N N 322 TRP HZ2 H N N 323 TRP HZ3 H N N 324 TRP HH2 H N N 325 TRP HXT H N N 326 TYR N N N N 327 TYR CA C N S 328 TYR C C N N 329 TYR O O N N 330 TYR CB C N N 331 TYR CG C Y N 332 TYR CD1 C Y N 333 TYR CD2 C Y N 334 TYR CE1 C Y N 335 TYR CE2 C Y N 336 TYR CZ C Y N 337 TYR OH O N N 338 TYR OXT O N N 339 TYR H H N N 340 TYR H2 H N N 341 TYR HA H N N 342 TYR HB2 H N N 343 TYR HB3 H N N 344 TYR HD1 H N N 345 TYR HD2 H N N 346 TYR HE1 H N N 347 TYR HE2 H N N 348 TYR HH H N N 349 TYR HXT H N N 350 VAL N N N N 351 VAL CA C N S 352 VAL C C N N 353 VAL O O N N 354 VAL CB C N N 355 VAL CG1 C N N 356 VAL CG2 C N N 357 VAL OXT O N N 358 VAL H H N N 359 VAL H2 H N N 360 VAL HA H N N 361 VAL HB H N N 362 VAL HG11 H N N 363 VAL HG12 H N N 364 VAL HG13 H N N 365 VAL HG21 H N N 366 VAL HG22 H N N 367 VAL HG23 H N N 368 VAL HXT H N N 369 # loop_ _chem_comp_bond.comp_id _chem_comp_bond.atom_id_1 _chem_comp_bond.atom_id_2 _chem_comp_bond.value_order _chem_comp_bond.pdbx_aromatic_flag _chem_comp_bond.pdbx_stereo_config _chem_comp_bond.pdbx_ordinal ALA N CA sing N N 1 ALA N H sing N N 2 ALA N H2 sing N N 3 ALA CA C sing N N 4 ALA CA CB sing N N 5 ALA CA HA sing N N 6 ALA C O doub N N 7 ALA C OXT sing N N 8 ALA CB HB1 sing N N 9 ALA CB HB2 sing N N 10 ALA CB HB3 sing N N 11 ALA OXT HXT sing N N 12 ARG N CA sing N N 13 ARG N H sing N N 14 ARG N H2 sing N N 15 ARG CA C sing N N 16 ARG CA CB sing N N 17 ARG CA HA sing N N 18 ARG C O doub N N 19 ARG C OXT sing N N 20 ARG CB CG sing N N 21 ARG CB HB2 sing N N 22 ARG CB HB3 sing N N 23 ARG CG CD sing N N 24 ARG CG HG2 sing N N 25 ARG CG HG3 sing N N 26 ARG CD NE sing N N 27 ARG CD HD2 sing N N 28 ARG CD HD3 sing N N 29 ARG NE CZ sing N N 30 ARG NE HE sing N N 31 ARG CZ NH1 sing N N 32 ARG CZ NH2 doub N N 33 ARG NH1 HH11 sing N N 34 ARG NH1 HH12 sing N N 35 ARG NH2 HH21 sing N N 36 ARG NH2 HH22 sing N N 37 ARG OXT HXT sing N N 38 ASN N CA sing N N 39 ASN N H sing N N 40 ASN N H2 sing N N 41 ASN CA C sing N N 42 ASN CA CB sing N N 43 ASN CA HA sing N N 44 ASN C O doub N N 45 ASN C OXT sing N N 46 ASN CB CG sing N N 47 ASN CB HB2 sing N N 48 ASN CB HB3 sing N N 49 ASN CG OD1 doub N N 50 ASN CG ND2 sing N N 51 ASN ND2 HD21 sing N N 52 ASN ND2 HD22 sing N N 53 ASN OXT HXT sing N N 54 ASP N CA sing N N 55 ASP N H sing N N 56 ASP N H2 sing N N 57 ASP CA C sing N N 58 ASP CA CB sing N N 59 ASP CA HA sing N N 60 ASP C O doub N N 61 ASP C OXT sing N N 62 ASP CB CG sing N N 63 ASP CB HB2 sing N N 64 ASP CB HB3 sing N N 65 ASP CG OD1 doub N N 66 ASP CG OD2 sing N N 67 ASP OD2 HD2 sing N N 68 ASP OXT HXT sing N N 69 CYS N CA sing N N 70 CYS N H sing N N 71 CYS N H2 sing N N 72 CYS CA C sing N N 73 CYS CA CB sing N N 74 CYS CA HA sing N N 75 CYS C O doub N N 76 CYS C OXT sing N N 77 CYS CB SG sing N N 78 CYS CB HB2 sing N N 79 CYS CB HB3 sing N N 80 CYS SG HG sing N N 81 CYS OXT HXT sing N N 82 GLN N CA sing N N 83 GLN N H sing N N 84 GLN N H2 sing N N 85 GLN CA C sing N N 86 GLN CA CB sing N N 87 GLN CA HA sing N N 88 GLN C O doub N N 89 GLN C OXT sing N N 90 GLN CB CG sing N N 91 GLN CB HB2 sing N N 92 GLN CB HB3 sing N N 93 GLN CG CD sing N N 94 GLN CG HG2 sing N N 95 GLN CG HG3 sing N N 96 GLN CD OE1 doub N N 97 GLN CD NE2 sing N N 98 GLN NE2 HE21 sing N N 99 GLN NE2 HE22 sing N N 100 GLN OXT HXT sing N N 101 GLU N CA sing N N 102 GLU N H sing N N 103 GLU N H2 sing N N 104 GLU CA C sing N N 105 GLU CA CB sing N N 106 GLU CA HA sing N N 107 GLU C O doub N N 108 GLU C OXT sing N N 109 GLU CB CG sing N N 110 GLU CB HB2 sing N N 111 GLU CB HB3 sing N N 112 GLU CG CD sing N N 113 GLU CG HG2 sing N N 114 GLU CG HG3 sing N N 115 GLU CD OE1 doub N N 116 GLU CD OE2 sing N N 117 GLU OE2 HE2 sing N N 118 GLU OXT HXT sing N N 119 GLY N CA sing N N 120 GLY N H sing N N 121 GLY N H2 sing N N 122 GLY CA C sing N N 123 GLY CA HA2 sing N N 124 GLY CA HA3 sing N N 125 GLY C O doub N N 126 GLY C OXT sing N N 127 GLY OXT HXT sing N N 128 HOH O H1 sing N N 129 HOH O H2 sing N N 130 ILE N CA sing N N 131 ILE N H sing N N 132 ILE N H2 sing N N 133 ILE CA C sing N N 134 ILE CA CB sing N N 135 ILE CA HA sing N N 136 ILE C O doub N N 137 ILE C OXT sing N N 138 ILE CB CG1 sing N N 139 ILE CB CG2 sing N N 140 ILE CB HB sing N N 141 ILE CG1 CD1 sing N N 142 ILE CG1 HG12 sing N N 143 ILE CG1 HG13 sing N N 144 ILE CG2 HG21 sing N N 145 ILE CG2 HG22 sing N N 146 ILE CG2 HG23 sing N N 147 ILE CD1 HD11 sing N N 148 ILE CD1 HD12 sing N N 149 ILE CD1 HD13 sing N N 150 ILE OXT HXT sing N N 151 LEU N CA sing N N 152 LEU N H sing N N 153 LEU N H2 sing N N 154 LEU CA C sing N N 155 LEU CA CB sing N N 156 LEU CA HA sing N N 157 LEU C O doub N N 158 LEU C OXT sing N N 159 LEU CB CG sing N N 160 LEU CB HB2 sing N N 161 LEU CB HB3 sing N N 162 LEU CG CD1 sing N N 163 LEU CG CD2 sing N N 164 LEU CG HG sing N N 165 LEU CD1 HD11 sing N N 166 LEU CD1 HD12 sing N N 167 LEU CD1 HD13 sing N N 168 LEU CD2 HD21 sing N N 169 LEU CD2 HD22 sing N N 170 LEU CD2 HD23 sing N N 171 LEU OXT HXT sing N N 172 LYS N CA sing N N 173 LYS N H sing N N 174 LYS N H2 sing N N 175 LYS CA C sing N N 176 LYS CA CB sing N N 177 LYS CA HA sing N N 178 LYS C O doub N N 179 LYS C OXT sing N N 180 LYS CB CG sing N N 181 LYS CB HB2 sing N N 182 LYS CB HB3 sing N N 183 LYS CG CD sing N N 184 LYS CG HG2 sing N N 185 LYS CG HG3 sing N N 186 LYS CD CE sing N N 187 LYS CD HD2 sing N N 188 LYS CD HD3 sing N N 189 LYS CE NZ sing N N 190 LYS CE HE2 sing N N 191 LYS CE HE3 sing N N 192 LYS NZ HZ1 sing N N 193 LYS NZ HZ2 sing N N 194 LYS NZ HZ3 sing N N 195 LYS OXT HXT sing N N 196 MET N CA sing N N 197 MET N H sing N N 198 MET N H2 sing N N 199 MET CA C sing N N 200 MET CA CB sing N N 201 MET CA HA sing N N 202 MET C O doub N N 203 MET C OXT sing N N 204 MET CB CG sing N N 205 MET CB HB2 sing N N 206 MET CB HB3 sing N N 207 MET CG SD sing N N 208 MET CG HG2 sing N N 209 MET CG HG3 sing N N 210 MET SD CE sing N N 211 MET CE HE1 sing N N 212 MET CE HE2 sing N N 213 MET CE HE3 sing N N 214 MET OXT HXT sing N N 215 PHE N CA sing N N 216 PHE N H sing N N 217 PHE N H2 sing N N 218 PHE CA C sing N N 219 PHE CA CB sing N N 220 PHE CA HA sing N N 221 PHE C O doub N N 222 PHE C OXT sing N N 223 PHE CB CG sing N N 224 PHE CB HB2 sing N N 225 PHE CB HB3 sing N N 226 PHE CG CD1 doub Y N 227 PHE CG CD2 sing Y N 228 PHE CD1 CE1 sing Y N 229 PHE CD1 HD1 sing N N 230 PHE CD2 CE2 doub Y N 231 PHE CD2 HD2 sing N N 232 PHE CE1 CZ doub Y N 233 PHE CE1 HE1 sing N N 234 PHE CE2 CZ sing Y N 235 PHE CE2 HE2 sing N N 236 PHE CZ HZ sing N N 237 PHE OXT HXT sing N N 238 PRO N CA sing N N 239 PRO N CD sing N N 240 PRO N H sing N N 241 PRO CA C sing N N 242 PRO CA CB sing N N 243 PRO CA HA sing N N 244 PRO C O doub N N 245 PRO C OXT sing N N 246 PRO CB CG sing N N 247 PRO CB HB2 sing N N 248 PRO CB HB3 sing N N 249 PRO CG CD sing N N 250 PRO CG HG2 sing N N 251 PRO CG HG3 sing N N 252 PRO CD HD2 sing N N 253 PRO CD HD3 sing N N 254 PRO OXT HXT sing N N 255 SER N CA sing N N 256 SER N H sing N N 257 SER N H2 sing N N 258 SER CA C sing N N 259 SER CA CB sing N N 260 SER CA HA sing N N 261 SER C O doub N N 262 SER C OXT sing N N 263 SER CB OG sing N N 264 SER CB HB2 sing N N 265 SER CB HB3 sing N N 266 SER OG HG sing N N 267 SER OXT HXT sing N N 268 THR N CA sing N N 269 THR N H sing N N 270 THR N H2 sing N N 271 THR CA C sing N N 272 THR CA CB sing N N 273 THR CA HA sing N N 274 THR C O doub N N 275 THR C OXT sing N N 276 THR CB OG1 sing N N 277 THR CB CG2 sing N N 278 THR CB HB sing N N 279 THR OG1 HG1 sing N N 280 THR CG2 HG21 sing N N 281 THR CG2 HG22 sing N N 282 THR CG2 HG23 sing N N 283 THR OXT HXT sing N N 284 TRP N CA sing N N 285 TRP N H sing N N 286 TRP N H2 sing N N 287 TRP CA C sing N N 288 TRP CA CB sing N N 289 TRP CA HA sing N N 290 TRP C O doub N N 291 TRP C OXT sing N N 292 TRP CB CG sing N N 293 TRP CB HB2 sing N N 294 TRP CB HB3 sing N N 295 TRP CG CD1 doub Y N 296 TRP CG CD2 sing Y N 297 TRP CD1 NE1 sing Y N 298 TRP CD1 HD1 sing N N 299 TRP CD2 CE2 doub Y N 300 TRP CD2 CE3 sing Y N 301 TRP NE1 CE2 sing Y N 302 TRP NE1 HE1 sing N N 303 TRP CE2 CZ2 sing Y N 304 TRP CE3 CZ3 doub Y N 305 TRP CE3 HE3 sing N N 306 TRP CZ2 CH2 doub Y N 307 TRP CZ2 HZ2 sing N N 308 TRP CZ3 CH2 sing Y N 309 TRP CZ3 HZ3 sing N N 310 TRP CH2 HH2 sing N N 311 TRP OXT HXT sing N N 312 TYR N CA sing N N 313 TYR N H sing N N 314 TYR N H2 sing N N 315 TYR CA C sing N N 316 TYR CA CB sing N N 317 TYR CA HA sing N N 318 TYR C O doub N N 319 TYR C OXT sing N N 320 TYR CB CG sing N N 321 TYR CB HB2 sing N N 322 TYR CB HB3 sing N N 323 TYR CG CD1 doub Y N 324 TYR CG CD2 sing Y N 325 TYR CD1 CE1 sing Y N 326 TYR CD1 HD1 sing N N 327 TYR CD2 CE2 doub Y N 328 TYR CD2 HD2 sing N N 329 TYR CE1 CZ doub Y N 330 TYR CE1 HE1 sing N N 331 TYR CE2 CZ sing Y N 332 TYR CE2 HE2 sing N N 333 TYR CZ OH sing N N 334 TYR OH HH sing N N 335 TYR OXT HXT sing N N 336 VAL N CA sing N N 337 VAL N H sing N N 338 VAL N H2 sing N N 339 VAL CA C sing N N 340 VAL CA CB sing N N 341 VAL CA HA sing N N 342 VAL C O doub N N 343 VAL C OXT sing N N 344 VAL CB CG1 sing N N 345 VAL CB CG2 sing N N 346 VAL CB HB sing N N 347 VAL CG1 HG11 sing N N 348 VAL CG1 HG12 sing N N 349 VAL CG1 HG13 sing N N 350 VAL CG2 HG21 sing N N 351 VAL CG2 HG22 sing N N 352 VAL CG2 HG23 sing N N 353 VAL OXT HXT sing N N 354 # _pdbx_initial_refinement_model.id 1 _pdbx_initial_refinement_model.entity_id_list ? _pdbx_initial_refinement_model.type 'experimental model' _pdbx_initial_refinement_model.source_name PDB _pdbx_initial_refinement_model.accession_code 1I3U _pdbx_initial_refinement_model.details 'PDB ENTRY 1I3U' # _atom_sites.entry_id 1I3V _atom_sites.fract_transf_matrix[1][1] 0.023999 _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] 0.017829 _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] 0.009769 _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 . GLN A 1 1 ? 4.425 32.990 -6.881 1.00 33.99 ? 1 GLN A N 1 ATOM 2 C CA . GLN A 1 1 ? 2.995 32.817 -6.539 1.00 32.82 ? 1 GLN A CA 1 ATOM 3 C C . GLN A 1 1 ? 2.556 33.227 -5.148 1.00 30.68 ? 1 GLN A C 1 ATOM 4 O O . GLN A 1 1 ? 1.536 33.900 -5.045 1.00 30.70 ? 1 GLN A O 1 ATOM 5 C CB . GLN A 1 1 ? 2.583 31.401 -6.854 1.00 33.50 ? 1 GLN A CB 1 ATOM 6 C CG . GLN A 1 1 ? 2.547 31.261 -8.327 1.00 37.00 ? 1 GLN A CG 1 ATOM 7 C CD . GLN A 1 1 ? 1.907 29.994 -8.771 1.00 39.27 ? 1 GLN A CD 1 ATOM 8 O OE1 . GLN A 1 1 ? 1.445 29.907 -9.909 1.00 42.89 ? 1 GLN A OE1 1 ATOM 9 N NE2 . GLN A 1 1 ? 1.875 28.979 -7.890 1.00 41.69 ? 1 GLN A NE2 1 ATOM 10 N N . VAL A 1 2 ? 3.287 32.838 -4.092 1.00 28.63 ? 2 VAL A N 1 ATOM 11 C CA . VAL A 1 2 ? 2.931 33.253 -2.709 1.00 27.17 ? 2 VAL A CA 1 ATOM 12 C C . VAL A 1 2 ? 4.093 33.739 -1.920 1.00 25.85 ? 2 VAL A C 1 ATOM 13 O O . VAL A 1 2 ? 5.187 33.204 -2.055 1.00 25.04 ? 2 VAL A O 1 ATOM 14 C CB . VAL A 1 2 ? 2.478 32.144 -1.756 1.00 27.97 ? 2 VAL A CB 1 ATOM 15 C CG1 . VAL A 1 2 ? 1.061 32.389 -1.314 1.00 27.52 ? 2 VAL A CG1 1 ATOM 16 C CG2 . VAL A 1 2 ? 2.777 30.795 -2.330 1.00 28.97 ? 2 VAL A CG2 1 ATOM 17 N N . GLN A 1 3 ? 3.837 34.694 -1.039 1.00 24.78 ? 3 GLN A N 1 ATOM 18 C CA . GLN A 1 3 ? 4.866 35.192 -0.130 1.00 24.73 ? 3 GLN A CA 1 ATOM 19 C C . GLN A 1 3 ? 4.450 34.692 1.242 1.00 23.12 ? 3 GLN A C 1 ATOM 20 O O . GLN A 1 3 ? 3.287 34.740 1.592 1.00 23.06 ? 3 GLN A O 1 ATOM 21 C CB . GLN A 1 3 ? 4.930 36.720 -0.136 1.00 26.74 ? 3 GLN A CB 1 ATOM 22 C CG . GLN A 1 3 ? 5.539 37.271 -1.386 1.00 31.67 ? 3 GLN A CG 1 ATOM 23 C CD . GLN A 1 3 ? 5.805 38.781 -1.316 1.00 33.84 ? 3 GLN A CD 1 ATOM 24 O OE1 . GLN A 1 3 ? 6.681 39.292 -2.012 1.00 34.93 ? 3 GLN A OE1 1 ATOM 25 N NE2 . GLN A 1 3 ? 5.041 39.492 -0.480 1.00 35.65 ? 3 GLN A NE2 1 ATOM 26 N N . LEU A 1 4 ? 5.394 34.189 2.015 1.00 21.70 ? 4 LEU A N 1 ATOM 27 C CA . LEU A 1 4 ? 5.058 33.662 3.322 1.00 20.84 ? 4 LEU A CA 1 ATOM 28 C C . LEU A 1 4 ? 5.873 34.393 4.366 1.00 21.59 ? 4 LEU A C 1 ATOM 29 O O . LEU A 1 4 ? 7.053 34.701 4.158 1.00 20.85 ? 4 LEU A O 1 ATOM 30 C CB . LEU A 1 4 ? 5.346 32.155 3.372 1.00 19.33 ? 4 LEU A CB 1 ATOM 31 C CG . LEU A 1 4 ? 4.640 31.271 2.330 1.00 18.98 ? 4 LEU A CG 1 ATOM 32 C CD1 . LEU A 1 4 ? 5.263 29.880 2.341 1.00 18.80 ? 4 LEU A CD1 1 ATOM 33 C CD2 . LEU A 1 4 ? 3.140 31.208 2.646 1.00 18.10 ? 4 LEU A CD2 1 ATOM 34 N N . GLN A 1 5 ? 5.236 34.682 5.482 1.00 21.54 ? 5 GLN A N 1 ATOM 35 C CA . GLN A 1 5 ? 5.891 35.397 6.561 1.00 22.29 ? 5 GLN A CA 1 ATOM 36 C C . GLN A 1 5 ? 5.463 34.762 7.848 1.00 22.09 ? 5 GLN A C 1 ATOM 37 O O . GLN A 1 5 ? 4.270 34.716 8.137 1.00 21.72 ? 5 GLN A O 1 ATOM 38 C CB . GLN A 1 5 ? 5.461 36.859 6.589 1.00 24.49 ? 5 GLN A CB 1 ATOM 39 C CG . GLN A 1 5 ? 6.111 37.631 7.762 1.00 27.56 ? 5 GLN A CG 1 ATOM 40 C CD . GLN A 1 5 ? 7.633 37.597 7.658 1.00 30.27 ? 5 GLN A CD 1 ATOM 41 O OE1 . GLN A 1 5 ? 8.182 37.938 6.600 1.00 32.13 ? 5 GLN A OE1 1 ATOM 42 N NE2 . GLN A 1 5 ? 8.323 37.171 8.739 1.00 30.00 ? 5 GLN A NE2 1 ATOM 43 N N . GLU A 1 6 ? 6.418 34.250 8.613 1.00 20.86 ? 6 GLU A N 1 ATOM 44 C CA . GLU A 1 6 ? 6.106 33.636 9.897 1.00 19.40 ? 6 GLU A CA 1 ATOM 45 C C . GLU A 1 6 ? 6.118 34.717 10.973 1.00 19.90 ? 6 GLU A C 1 ATOM 46 O O . GLU A 1 6 ? 6.706 35.773 10.786 1.00 19.95 ? 6 GLU A O 1 ATOM 47 C CB . GLU A 1 6 ? 7.149 32.571 10.253 1.00 19.04 ? 6 GLU A CB 1 ATOM 48 C CG . GLU A 1 6 ? 7.338 31.536 9.179 1.00 17.58 ? 6 GLU A CG 1 ATOM 49 C CD . GLU A 1 6 ? 8.359 31.945 8.118 1.00 18.04 ? 6 GLU A CD 1 ATOM 50 O OE1 . GLU A 1 6 ? 8.698 33.155 8.038 1.00 17.18 ? 6 GLU A OE1 1 ATOM 51 O OE2 . GLU A 1 6 ? 8.808 31.041 7.365 1.00 16.99 ? 6 GLU A OE2 1 ATOM 52 N N . SER A 1 7 ? 5.476 34.462 12.101 1.00 19.53 ? 7 SER A N 1 ATOM 53 C CA . SER A 1 7 ? 5.475 35.416 13.172 1.00 20.30 ? 7 SER A CA 1 ATOM 54 C C . SER A 1 7 ? 5.000 34.702 14.412 1.00 20.41 ? 7 SER A C 1 ATOM 55 O O . SER A 1 7 ? 4.402 33.619 14.325 1.00 19.43 ? 7 SER A O 1 ATOM 56 C CB . SER A 1 7 ? 4.545 36.598 12.855 1.00 22.62 ? 7 SER A CB 1 ATOM 57 O OG . SER A 1 7 ? 3.190 36.209 12.921 1.00 24.45 ? 7 SER A OG 1 ATOM 58 N N . GLY A 1 8 ? 5.297 35.301 15.566 1.00 20.94 ? 8 GLY A N 1 ATOM 59 C CA . GLY A 1 8 ? 4.910 34.730 16.840 1.00 21.83 ? 8 GLY A CA 1 ATOM 60 C C . GLY A 1 8 ? 6.110 34.225 17.617 1.00 23.73 ? 8 GLY A C 1 ATOM 61 O O . GLY A 1 8 ? 5.981 33.772 18.752 1.00 24.03 ? 8 GLY A O 1 ATOM 62 N N . GLY A 1 9 ? 7.291 34.282 17.013 1.00 23.45 ? 9 GLY A N 1 ATOM 63 C CA . GLY A 1 9 ? 8.459 33.806 17.723 1.00 24.32 ? 9 GLY A CA 1 ATOM 64 C C . GLY A 1 9 ? 8.800 34.731 18.887 1.00 25.43 ? 9 GLY A C 1 ATOM 65 O O . GLY A 1 9 ? 8.354 35.891 18.967 1.00 25.47 ? 9 GLY A O 1 ATOM 66 N N . GLY A 1 10 ? 9.582 34.216 19.822 1.00 25.96 ? 10 GLY A N 1 ATOM 67 C CA . GLY A 1 10 ? 9.977 35.035 20.952 1.00 26.74 ? 10 GLY A CA 1 ATOM 68 C C . GLY A 1 10 ? 10.723 34.205 21.966 1.00 27.83 ? 10 GLY A C 1 ATOM 69 O O . GLY A 1 10 ? 11.048 33.037 21.723 1.00 27.28 ? 10 GLY A O 1 ATOM 70 N N . LEU A 1 11 ? 11.013 34.819 23.106 1.00 28.75 ? 11 LEU A N 1 ATOM 71 C CA . LEU A 1 11 ? 11.702 34.125 24.164 1.00 30.02 ? 11 LEU A CA 1 ATOM 72 C C . LEU A 1 11 ? 10.648 33.578 25.116 1.00 30.63 ? 11 LEU A C 1 ATOM 73 O O . LEU A 1 11 ? 9.810 34.303 25.642 1.00 32.22 ? 11 LEU A O 1 ATOM 74 C CB . LEU A 1 11 ? 12.650 35.084 24.892 1.00 31.01 ? 11 LEU A CB 1 ATOM 75 C CG . LEU A 1 11 ? 13.448 34.489 26.053 1.00 32.18 ? 11 LEU A CG 1 ATOM 76 C CD1 . LEU A 1 11 ? 14.177 33.235 25.615 1.00 33.12 ? 11 LEU A CD1 1 ATOM 77 C CD2 . LEU A 1 11 ? 14.452 35.533 26.550 1.00 33.17 ? 11 LEU A CD2 1 ATOM 78 N N . VAL A 1 12 ? 10.676 32.279 25.331 1.00 30.86 ? 12 VAL A N 1 ATOM 79 C CA . VAL A 1 12 ? 9.717 31.666 26.219 1.00 30.51 ? 12 VAL A CA 1 ATOM 80 C C . VAL A 1 12 ? 10.441 30.758 27.217 1.00 29.87 ? 12 VAL A C 1 ATOM 81 O O . VAL A 1 12 ? 11.614 30.401 27.038 1.00 28.15 ? 12 VAL A O 1 ATOM 82 C CB . VAL A 1 12 ? 8.636 30.857 25.401 1.00 31.75 ? 12 VAL A CB 1 ATOM 83 C CG1 . VAL A 1 12 ? 9.200 29.544 24.845 1.00 31.17 ? 12 VAL A CG1 1 ATOM 84 C CG2 . VAL A 1 12 ? 7.470 30.584 26.269 1.00 32.54 ? 12 VAL A CG2 1 ATOM 85 N N . GLN A 1 13 ? 9.741 30.393 28.281 1.00 29.20 ? 13 GLN A N 1 ATOM 86 C CA . GLN A 1 13 ? 10.336 29.539 29.275 1.00 29.45 ? 13 GLN A CA 1 ATOM 87 C C . GLN A 1 13 ? 9.972 28.097 28.982 1.00 28.48 ? 13 GLN A C 1 ATOM 88 O O . GLN A 1 13 ? 8.970 27.811 28.337 1.00 28.12 ? 13 GLN A O 1 ATOM 89 C CB . GLN A 1 13 ? 9.861 29.958 30.654 1.00 32.29 ? 13 GLN A CB 1 ATOM 90 C CG . GLN A 1 13 ? 10.598 29.279 31.789 1.00 36.66 ? 13 GLN A CG 1 ATOM 91 C CD . GLN A 1 13 ? 10.035 29.671 33.161 1.00 39.56 ? 13 GLN A CD 1 ATOM 92 O OE1 . GLN A 1 13 ? 9.450 30.759 33.323 1.00 40.41 ? 13 GLN A OE1 1 ATOM 93 N NE2 . GLN A 1 13 ? 10.222 28.793 34.158 1.00 41.10 ? 13 GLN A NE2 1 ATOM 94 N N . ALA A 1 14 ? 10.813 27.179 29.420 1.00 27.29 ? 14 ALA A N 1 ATOM 95 C CA . ALA A 1 14 ? 10.557 25.780 29.178 1.00 26.84 ? 14 ALA A CA 1 ATOM 96 C C . ALA A 1 14 ? 9.246 25.432 29.845 1.00 26.88 ? 14 ALA A C 1 ATOM 97 O O . ALA A 1 14 ? 8.964 25.892 30.953 1.00 26.26 ? 14 ALA A O 1 ATOM 98 C CB . ALA A 1 14 ? 11.681 24.936 29.743 1.00 27.50 ? 14 ALA A CB 1 ATOM 99 N N . GLY A 1 15 ? 8.439 24.634 29.158 1.00 26.42 ? 15 GLY A N 1 ATOM 100 C CA . GLY A 1 15 ? 7.150 24.242 29.690 1.00 25.63 ? 15 GLY A CA 1 ATOM 101 C C . GLY A 1 15 ? 5.999 25.081 29.154 1.00 24.81 ? 15 GLY A C 1 ATOM 102 O O . GLY A 1 15 ? 4.854 24.659 29.232 1.00 23.83 ? 15 GLY A O 1 ATOM 103 N N . ASP A 1 16 ? 6.307 26.254 28.610 1.00 24.32 ? 16 ASP A N 1 ATOM 104 C CA . ASP A 1 16 ? 5.287 27.149 28.060 1.00 24.18 ? 16 ASP A CA 1 ATOM 105 C C . ASP A 1 16 ? 4.843 26.708 26.659 1.00 23.31 ? 16 ASP A C 1 ATOM 106 O O . ASP A 1 16 ? 5.417 25.798 26.048 1.00 22.78 ? 16 ASP A O 1 ATOM 107 C CB . ASP A 1 16 ? 5.803 28.592 27.923 1.00 25.04 ? 16 ASP A CB 1 ATOM 108 C CG . ASP A 1 16 ? 6.094 29.265 29.250 1.00 27.50 ? 16 ASP A CG 1 ATOM 109 O OD1 . ASP A 1 16 ? 5.560 28.824 30.298 1.00 26.85 ? 16 ASP A OD1 1 ATOM 110 O OD2 . ASP A 1 16 ? 6.849 30.276 29.227 1.00 27.93 ? 16 ASP A OD2 1 ATOM 111 N N . SER A 1 17 ? 3.826 27.394 26.155 1.00 21.58 ? 17 SER A N 1 ATOM 112 C CA . SER A 1 17 ? 3.306 27.109 24.833 1.00 21.16 ? 17 SER A CA 1 ATOM 113 C C . SER A 1 17 ? 3.523 28.363 24.010 1.00 20.63 ? 17 SER A C 1 ATOM 114 O O . SER A 1 17 ? 3.643 29.432 24.550 1.00 20.56 ? 17 SER A O 1 ATOM 115 C CB . SER A 1 17 ? 1.801 26.798 24.925 1.00 20.14 ? 17 SER A CB 1 ATOM 116 O OG . SER A 1 17 ? 1.615 25.485 25.421 1.00 18.68 ? 17 SER A OG 1 ATOM 117 N N . LEU A 1 18 ? 3.592 28.222 22.697 1.00 20.75 ? 18 LEU A N 1 ATOM 118 C CA . LEU A 1 18 ? 3.731 29.377 21.833 1.00 19.94 ? 18 LEU A CA 1 ATOM 119 C C . LEU A 1 18 ? 2.917 29.026 20.583 1.00 19.08 ? 18 LEU A C 1 ATOM 120 O O . LEU A 1 18 ? 2.822 27.869 20.223 1.00 18.76 ? 18 LEU A O 1 ATOM 121 C CB . LEU A 1 18 ? 5.192 29.581 21.465 1.00 21.69 ? 18 LEU A CB 1 ATOM 122 C CG . LEU A 1 18 ? 5.591 30.981 21.045 1.00 25.21 ? 18 LEU A CG 1 ATOM 123 C CD1 . LEU A 1 18 ? 5.278 31.958 22.181 1.00 25.76 ? 18 LEU A CD1 1 ATOM 124 C CD2 . LEU A 1 18 ? 7.108 30.994 20.755 1.00 25.87 ? 18 LEU A CD2 1 ATOM 125 N N . LYS A 1 19 ? 2.362 30.024 19.925 1.00 17.77 ? 19 LYS A N 1 ATOM 126 C CA . LYS A 1 19 ? 1.575 29.793 18.730 1.00 18.17 ? 19 LYS A CA 1 ATOM 127 C C . LYS A 1 19 ? 2.188 30.563 17.596 1.00 17.03 ? 19 LYS A C 1 ATOM 128 O O . LYS A 1 19 ? 2.230 31.777 17.642 1.00 17.92 ? 19 LYS A O 1 ATOM 129 C CB . LYS A 1 19 ? 0.147 30.291 18.932 1.00 18.71 ? 19 LYS A CB 1 ATOM 130 C CG . LYS A 1 19 ? -0.722 30.076 17.696 1.00 21.92 ? 19 LYS A CG 1 ATOM 131 C CD . LYS A 1 19 ? -2.166 30.341 18.030 1.00 24.49 ? 19 LYS A CD 1 ATOM 132 C CE . LYS A 1 19 ? -3.105 29.858 16.965 1.00 27.91 ? 19 LYS A CE 1 ATOM 133 N NZ . LYS A 1 19 ? -4.450 29.796 17.579 1.00 30.19 ? 19 LYS A NZ 1 ATOM 134 N N . LEU A 1 20 ? 2.671 29.871 16.578 1.00 16.02 ? 20 LEU A N 1 ATOM 135 C CA . LEU A 1 20 ? 3.264 30.567 15.442 1.00 15.56 ? 20 LEU A CA 1 ATOM 136 C C . LEU A 1 20 ? 2.247 30.671 14.310 1.00 15.78 ? 20 LEU A C 1 ATOM 137 O O . LEU A 1 20 ? 1.361 29.807 14.178 1.00 14.09 ? 20 LEU A O 1 ATOM 138 C CB . LEU A 1 20 ? 4.502 29.815 14.911 1.00 15.00 ? 20 LEU A CB 1 ATOM 139 C CG . LEU A 1 20 ? 5.595 29.399 15.916 1.00 16.24 ? 20 LEU A CG 1 ATOM 140 C CD1 . LEU A 1 20 ? 6.801 28.757 15.200 1.00 16.12 ? 20 LEU A CD1 1 ATOM 141 C CD2 . LEU A 1 20 ? 6.023 30.606 16.675 1.00 15.52 ? 20 LEU A CD2 1 ATOM 142 N N . SER A 1 21 ? 2.408 31.714 13.499 1.00 15.64 ? 21 SER A N 1 ATOM 143 C CA . SER A 1 21 ? 1.561 31.943 12.332 1.00 17.96 ? 21 SER A CA 1 ATOM 144 C C . SER A 1 21 ? 2.400 32.051 11.077 1.00 18.26 ? 21 SER A C 1 ATOM 145 O O . SER A 1 21 ? 3.473 32.633 11.074 1.00 18.79 ? 21 SER A O 1 ATOM 146 C CB . SER A 1 21 ? 0.783 33.248 12.437 1.00 18.34 ? 21 SER A CB 1 ATOM 147 O OG . SER A 1 21 ? 0.035 33.252 13.614 1.00 22.50 ? 21 SER A OG 1 ATOM 148 N N . CYS A 1 22 ? 1.887 31.471 10.014 1.00 17.41 ? 22 CYS A N 1 ATOM 149 C CA . CYS A 1 22 ? 2.509 31.516 8.710 1.00 17.73 ? 22 CYS A CA 1 ATOM 150 C C . CYS A 1 22 ? 1.408 32.185 7.867 1.00 18.12 ? 22 CYS A C 1 ATOM 151 O O . CYS A 1 22 ? 0.422 31.544 7.538 1.00 16.99 ? 22 CYS A O 1 ATOM 152 C CB . CYS A 1 22 ? 2.773 30.108 8.194 1.00 15.54 ? 22 CYS A CB 1 ATOM 153 S SG . CYS A 1 22 ? 3.182 30.068 6.454 1.00 17.95 ? 22 CYS A SG 1 ATOM 154 N N . GLU A 1 23 ? 1.582 33.465 7.572 1.00 19.01 ? 23 GLU A N 1 ATOM 155 C CA . GLU A 1 23 ? 0.614 34.229 6.803 1.00 20.72 ? 23 GLU A CA 1 ATOM 156 C C . GLU A 1 23 ? 1.141 34.387 5.379 1.00 20.64 ? 23 GLU A C 1 ATOM 157 O O . GLU A 1 23 ? 2.331 34.680 5.159 1.00 18.65 ? 23 GLU A O 1 ATOM 158 C CB . GLU A 1 23 ? 0.399 35.607 7.419 1.00 22.97 ? 23 GLU A CB 1 ATOM 159 C CG . GLU A 1 23 ? -0.651 36.439 6.638 1.00 30.51 ? 23 GLU A CG 1 ATOM 160 C CD . GLU A 1 23 ? -0.672 37.922 6.985 1.00 32.73 ? 23 GLU A CD 1 ATOM 161 O OE1 . GLU A 1 23 ? -1.708 38.416 7.502 1.00 36.92 ? 23 GLU A OE1 1 ATOM 162 O OE2 . GLU A 1 23 ? 0.338 38.603 6.720 1.00 35.81 ? 23 GLU A OE2 1 ATOM 163 N N . ALA A 1 24 ? 0.244 34.171 4.429 1.00 19.18 ? 24 ALA A N 1 ATOM 164 C CA . ALA A 1 24 ? 0.534 34.290 3.018 1.00 18.88 ? 24 ALA A CA 1 ATOM 165 C C . ALA A 1 24 ? 0.056 35.620 2.477 1.00 19.90 ? 24 ALA A C 1 ATOM 166 O O . ALA A 1 24 ? -0.919 36.207 2.974 1.00 19.74 ? 24 ALA A O 1 ATOM 167 C CB . ALA A 1 24 ? -0.156 33.198 2.283 1.00 18.80 ? 24 ALA A CB 1 ATOM 168 N N . SER A 1 25 ? 0.740 36.119 1.462 1.00 19.61 ? 25 SER A N 1 ATOM 169 C CA . SER A 1 25 ? 0.288 37.323 0.826 1.00 20.18 ? 25 SER A CA 1 ATOM 170 C C . SER A 1 25 ? 0.561 37.115 -0.660 1.00 20.59 ? 25 SER A C 1 ATOM 171 O O . SER A 1 25 ? 1.470 36.365 -1.060 1.00 18.87 ? 25 SER A O 1 ATOM 172 C CB . SER A 1 25 ? 0.987 38.579 1.371 1.00 23.16 ? 25 SER A CB 1 ATOM 173 O OG . SER A 1 25 ? 2.390 38.480 1.277 1.00 25.28 ? 25 SER A OG 1 ATOM 174 N N . GLY A 1 26 ? -0.261 37.761 -1.478 1.00 20.28 ? 26 GLY A N 1 ATOM 175 C CA . GLY A 1 26 ? -0.124 37.638 -2.907 1.00 21.10 ? 26 GLY A CA 1 ATOM 176 C C . GLY A 1 26 ? -0.977 36.527 -3.479 1.00 20.44 ? 26 GLY A C 1 ATOM 177 O O . GLY A 1 26 ? -1.195 36.476 -4.674 1.00 22.83 ? 26 GLY A O 1 ATOM 178 N N . ASP A 1 27 ? -1.438 35.617 -2.650 1.00 19.58 ? 27 ASP A N 1 ATOM 179 C CA . ASP A 1 27 ? -2.272 34.533 -3.132 1.00 18.83 ? 27 ASP A CA 1 ATOM 180 C C . ASP A 1 27 ? -2.918 33.985 -1.888 1.00 18.47 ? 27 ASP A C 1 ATOM 181 O O . ASP A 1 27 ? -2.593 34.358 -0.756 1.00 17.88 ? 27 ASP A O 1 ATOM 182 C CB . ASP A 1 27 ? -1.438 33.419 -3.819 1.00 18.86 ? 27 ASP A CB 1 ATOM 183 C CG . ASP A 1 27 ? -2.279 32.508 -4.721 1.00 20.27 ? 27 ASP A CG 1 ATOM 184 O OD1 . ASP A 1 27 ? -3.515 32.632 -4.683 1.00 21.31 ? 27 ASP A OD1 1 ATOM 185 O OD2 . ASP A 1 27 ? -1.725 31.655 -5.459 1.00 21.71 ? 27 ASP A OD2 1 ATOM 186 N N . SER A 1 28 ? -3.846 33.083 -2.116 1.00 18.94 ? 28 SER A N 1 ATOM 187 C CA . SER A 1 28 ? -4.546 32.433 -1.031 1.00 18.90 ? 28 SER A CA 1 ATOM 188 C C . SER A 1 28 ? -3.727 31.213 -0.644 1.00 18.71 ? 28 SER A C 1 ATOM 189 O O . SER A 1 28 ? -3.289 30.460 -1.508 1.00 18.17 ? 28 SER A O 1 ATOM 190 C CB . SER A 1 28 ? -5.912 31.934 -1.497 1.00 17.89 ? 28 SER A CB 1 ATOM 191 O OG . SER A 1 28 ? -6.367 30.894 -0.650 1.00 18.88 ? 28 SER A OG 1 ATOM 192 N N . ILE A 1 29 ? -3.607 31.000 0.650 1.00 18.01 ? 29 ILE A N 1 ATOM 193 C CA . ILE A 1 29 ? -2.923 29.850 1.185 1.00 19.31 ? 29 ILE A CA 1 ATOM 194 C C . ILE A 1 29 ? -3.808 28.595 1.011 1.00 20.04 ? 29 ILE A C 1 ATOM 195 O O . ILE A 1 29 ? -3.340 27.450 1.155 1.00 19.34 ? 29 ILE A O 1 ATOM 196 C CB . ILE A 1 29 ? -2.635 30.119 2.679 1.00 19.44 ? 29 ILE A CB 1 ATOM 197 C CG1 . ILE A 1 29 ? -1.386 29.373 3.126 1.00 20.01 ? 29 ILE A CG1 1 ATOM 198 C CG2 . ILE A 1 29 ? -3.828 29.708 3.541 1.00 19.52 ? 29 ILE A CG2 1 ATOM 199 C CD1 . ILE A 1 29 ? -0.845 29.911 4.398 1.00 19.60 ? 29 ILE A CD1 1 ATOM 200 N N . GLY A 1 30 ? -5.093 28.794 0.674 1.00 20.70 ? 30 GLY A N 1 ATOM 201 C CA . GLY A 1 30 ? -5.986 27.654 0.528 1.00 19.29 ? 30 GLY A CA 1 ATOM 202 C C . GLY A 1 30 ? -5.687 26.596 -0.527 1.00 20.27 ? 30 GLY A C 1 ATOM 203 O O . GLY A 1 30 ? -6.194 25.464 -0.418 1.00 20.37 ? 30 GLY A O 1 ATOM 204 N N . THR A 1 31 ? -4.899 26.910 -1.553 1.00 18.77 ? 31 THR A N 1 ATOM 205 C CA . THR A 1 31 ? -4.602 25.890 -2.565 1.00 20.14 ? 31 THR A CA 1 ATOM 206 C C . THR A 1 31 ? -3.163 25.328 -2.496 1.00 19.53 ? 31 THR A C 1 ATOM 207 O O . THR A 1 31 ? -2.711 24.661 -3.421 1.00 19.96 ? 31 THR A O 1 ATOM 208 C CB . THR A 1 31 ? -4.843 26.443 -3.973 1.00 21.41 ? 31 THR A CB 1 ATOM 209 O OG1 . THR A 1 31 ? -4.336 27.784 -4.014 1.00 23.71 ? 31 THR A OG1 1 ATOM 210 C CG2 . THR A 1 31 ? -6.393 26.433 -4.306 1.00 22.99 ? 31 THR A CG2 1 ATOM 211 N N . TYR A 1 32 ? -2.474 25.582 -1.400 1.00 17.58 ? 32 TYR A N 1 ATOM 212 C CA . TYR A 1 32 ? -1.098 25.110 -1.216 1.00 17.73 ? 32 TYR A CA 1 ATOM 213 C C . TYR A 1 32 ? -1.005 24.196 -0.023 1.00 17.65 ? 32 TYR A C 1 ATOM 214 O O . TYR A 1 32 ? -1.679 24.428 0.970 1.00 17.47 ? 32 TYR A O 1 ATOM 215 C CB . TYR A 1 32 ? -0.163 26.289 -0.932 1.00 19.00 ? 32 TYR A CB 1 ATOM 216 C CG . TYR A 1 32 ? 0.051 27.268 -2.062 1.00 19.08 ? 32 TYR A CG 1 ATOM 217 C CD1 . TYR A 1 32 ? 1.001 27.018 -3.059 1.00 20.04 ? 32 TYR A CD1 1 ATOM 218 C CD2 . TYR A 1 32 ? -0.645 28.469 -2.101 1.00 18.93 ? 32 TYR A CD2 1 ATOM 219 C CE1 . TYR A 1 32 ? 1.250 27.947 -4.064 1.00 20.03 ? 32 TYR A CE1 1 ATOM 220 C CE2 . TYR A 1 32 ? -0.402 29.400 -3.096 1.00 20.12 ? 32 TYR A CE2 1 ATOM 221 C CZ . TYR A 1 32 ? 0.537 29.137 -4.073 1.00 20.16 ? 32 TYR A CZ 1 ATOM 222 O OH . TYR A 1 32 ? 0.734 30.051 -5.082 1.00 22.92 ? 32 TYR A OH 1 ATOM 223 N N . VAL A 1 33 ? -0.190 23.154 -0.124 1.00 16.94 ? 33 VAL A N 1 ATOM 224 C CA . VAL A 1 33 ? 0.055 22.290 1.030 1.00 17.38 ? 33 VAL A CA 1 ATOM 225 C C . VAL A 1 33 ? 1.093 23.129 1.816 1.00 17.63 ? 33 VAL A C 1 ATOM 226 O O . VAL A 1 33 ? 1.978 23.725 1.197 1.00 16.68 ? 33 VAL A O 1 ATOM 227 C CB . VAL A 1 33 ? 0.689 20.970 0.586 1.00 17.89 ? 33 VAL A CB 1 ATOM 228 C CG1 . VAL A 1 33 ? 1.176 20.170 1.801 1.00 19.83 ? 33 VAL A CG1 1 ATOM 229 C CG2 . VAL A 1 33 ? -0.318 20.161 -0.223 1.00 18.23 ? 33 VAL A CG2 1 ATOM 230 N N . ILE A 1 34 ? 0.968 23.209 3.138 1.00 16.31 ? 34 ILE A N 1 ATOM 231 C CA . ILE A 1 34 ? 1.859 24.011 3.948 1.00 15.83 ? 34 ILE A CA 1 ATOM 232 C C . ILE A 1 34 ? 2.634 23.100 4.878 1.00 17.12 ? 34 ILE A C 1 ATOM 233 O O . ILE A 1 34 ? 2.079 22.164 5.457 1.00 18.49 ? 34 ILE A O 1 ATOM 234 C CB . ILE A 1 34 ? 1.088 25.048 4.815 1.00 16.48 ? 34 ILE A CB 1 ATOM 235 C CG1 . ILE A 1 34 ? 0.304 26.021 3.929 1.00 15.42 ? 34 ILE A CG1 1 ATOM 236 C CG2 . ILE A 1 34 ? 2.058 25.830 5.719 1.00 15.65 ? 34 ILE A CG2 1 ATOM 237 C CD1 . ILE A 1 34 ? 1.139 26.933 3.009 1.00 14.68 ? 34 ILE A CD1 1 ATOM 238 N N . GLY A 1 35 ? 3.942 23.354 4.985 1.00 16.84 ? 35 GLY A N 1 ATOM 239 C CA . GLY A 1 35 ? 4.761 22.556 5.860 1.00 15.50 ? 35 GLY A CA 1 ATOM 240 C C . GLY A 1 35 ? 5.538 23.427 6.829 1.00 15.69 ? 35 GLY A C 1 ATOM 241 O O . GLY A 1 35 ? 5.795 24.586 6.539 1.00 16.14 ? 35 GLY A O 1 ATOM 242 N N . TRP A 1 36 ? 5.876 22.868 7.987 1.00 15.23 ? 36 TRP A N 1 ATOM 243 C CA . TRP A 1 36 ? 6.661 23.573 8.991 1.00 15.06 ? 36 TRP A CA 1 ATOM 244 C C . TRP A 1 36 ? 7.996 22.859 9.156 1.00 15.31 ? 36 TRP A C 1 ATOM 245 O O . TRP A 1 36 ? 8.064 21.638 9.225 1.00 14.72 ? 36 TRP A O 1 ATOM 246 C CB . TRP A 1 36 ? 5.975 23.612 10.353 1.00 13.50 ? 36 TRP A CB 1 ATOM 247 C CG . TRP A 1 36 ? 4.883 24.611 10.390 1.00 13.16 ? 36 TRP A CG 1 ATOM 248 C CD1 . TRP A 1 36 ? 3.540 24.379 10.140 1.00 13.71 ? 36 TRP A CD1 1 ATOM 249 C CD2 . TRP A 1 36 ? 4.995 25.994 10.698 1.00 12.98 ? 36 TRP A CD2 1 ATOM 250 N NE1 . TRP A 1 36 ? 2.826 25.548 10.297 1.00 12.74 ? 36 TRP A NE1 1 ATOM 251 C CE2 . TRP A 1 36 ? 3.694 26.552 10.635 1.00 12.23 ? 36 TRP A CE2 1 ATOM 252 C CE3 . TRP A 1 36 ? 6.070 26.832 11.026 1.00 13.39 ? 36 TRP A CE3 1 ATOM 253 C CZ2 . TRP A 1 36 ? 3.449 27.898 10.884 1.00 12.99 ? 36 TRP A CZ2 1 ATOM 254 C CZ3 . TRP A 1 36 ? 5.831 28.164 11.271 1.00 12.09 ? 36 TRP A CZ3 1 ATOM 255 C CH2 . TRP A 1 36 ? 4.530 28.693 11.200 1.00 14.26 ? 36 TRP A CH2 1 ATOM 256 N N . PHE A 1 37 ? 9.045 23.656 9.241 1.00 15.53 ? 37 PHE A N 1 ATOM 257 C CA . PHE A 1 37 ? 10.401 23.159 9.421 1.00 16.11 ? 37 PHE A CA 1 ATOM 258 C C . PHE A 1 37 ? 11.073 24.022 10.511 1.00 15.78 ? 37 PHE A C 1 ATOM 259 O O . PHE A 1 37 ? 10.630 25.132 10.827 1.00 16.21 ? 37 PHE A O 1 ATOM 260 C CB . PHE A 1 37 ? 11.216 23.344 8.116 1.00 16.78 ? 37 PHE A CB 1 ATOM 261 C CG . PHE A 1 37 ? 10.733 22.518 6.959 1.00 17.49 ? 37 PHE A CG 1 ATOM 262 C CD1 . PHE A 1 37 ? 9.570 22.862 6.270 1.00 17.33 ? 37 PHE A CD1 1 ATOM 263 C CD2 . PHE A 1 37 ? 11.386 21.350 6.617 1.00 17.72 ? 37 PHE A CD2 1 ATOM 264 C CE1 . PHE A 1 37 ? 9.084 22.051 5.268 1.00 18.20 ? 37 PHE A CE1 1 ATOM 265 C CE2 . PHE A 1 37 ? 10.895 20.524 5.606 1.00 18.85 ? 37 PHE A CE2 1 ATOM 266 C CZ . PHE A 1 37 ? 9.730 20.876 4.937 1.00 18.54 ? 37 PHE A CZ 1 ATOM 267 N N . ARG A 1 38 ? 12.141 23.528 11.102 1.00 15.76 ? 38 ARG A N 1 ATOM 268 C CA . ARG A 1 38 ? 12.868 24.399 12.041 1.00 16.71 ? 38 ARG A CA 1 ATOM 269 C C . ARG A 1 38 ? 14.351 24.052 11.881 1.00 17.93 ? 38 ARG A C 1 ATOM 270 O O . ARG A 1 38 ? 14.688 22.960 11.447 1.00 16.84 ? 38 ARG A O 1 ATOM 271 C CB . ARG A 1 38 ? 12.437 24.176 13.493 1.00 15.96 ? 38 ARG A CB 1 ATOM 272 C CG . ARG A 1 38 ? 12.913 22.879 14.061 1.00 16.18 ? 38 ARG A CG 1 ATOM 273 C CD . ARG A 1 38 ? 12.621 22.790 15.538 1.00 15.90 ? 38 ARG A CD 1 ATOM 274 N NE . ARG A 1 38 ? 12.961 21.463 16.041 1.00 16.14 ? 38 ARG A NE 1 ATOM 275 C CZ . ARG A 1 38 ? 12.430 20.975 17.155 1.00 17.41 ? 38 ARG A CZ 1 ATOM 276 N NH1 . ARG A 1 38 ? 11.559 21.719 17.801 1.00 14.93 ? 38 ARG A NH1 1 ATOM 277 N NH2 . ARG A 1 38 ? 12.791 19.788 17.643 1.00 16.88 ? 38 ARG A NH2 1 ATOM 278 N N . GLN A 1 39 ? 15.235 24.972 12.230 1.00 21.12 ? 39 GLN A N 1 ATOM 279 C CA . GLN A 1 39 ? 16.657 24.668 12.117 1.00 24.44 ? 39 GLN A CA 1 ATOM 280 C C . GLN A 1 39 ? 17.387 25.221 13.334 1.00 25.74 ? 39 GLN A C 1 ATOM 281 O O . GLN A 1 39 ? 17.364 26.431 13.564 1.00 25.25 ? 39 GLN A O 1 ATOM 282 C CB . GLN A 1 39 ? 17.230 25.267 10.823 1.00 24.65 ? 39 GLN A CB 1 ATOM 283 C CG . GLN A 1 39 ? 18.756 25.126 10.641 1.00 25.71 ? 39 GLN A CG 1 ATOM 284 C CD . GLN A 1 39 ? 19.226 25.650 9.290 1.00 26.11 ? 39 GLN A CD 1 ATOM 285 O OE1 . GLN A 1 39 ? 18.832 26.723 8.860 1.00 25.48 ? 39 GLN A OE1 1 ATOM 286 N NE2 . GLN A 1 39 ? 20.084 24.894 8.632 1.00 27.51 ? 39 GLN A NE2 1 ATOM 287 N N . ALA A 1 40 ? 17.979 24.314 14.117 1.00 28.64 ? 40 ALA A N 1 ATOM 288 C CA . ALA A 1 40 ? 18.750 24.675 15.315 1.00 31.49 ? 40 ALA A CA 1 ATOM 289 C C . ALA A 1 40 ? 20.064 25.276 14.809 1.00 33.80 ? 40 ALA A C 1 ATOM 290 O O . ALA A 1 40 ? 20.597 24.829 13.792 1.00 32.70 ? 40 ALA A O 1 ATOM 291 C CB . ALA A 1 40 ? 19.008 23.446 16.153 1.00 31.81 ? 40 ALA A CB 1 ATOM 292 N N . PRO A 1 41 ? 20.622 26.261 15.548 1.00 36.13 ? 41 PRO A N 1 ATOM 293 C CA . PRO A 1 41 ? 21.862 26.996 15.237 1.00 37.82 ? 41 PRO A CA 1 ATOM 294 C C . PRO A 1 41 ? 22.937 26.329 14.365 1.00 38.92 ? 41 PRO A C 1 ATOM 295 O O . PRO A 1 41 ? 23.490 26.997 13.485 1.00 40.88 ? 41 PRO A O 1 ATOM 296 C CB . PRO A 1 41 ? 22.421 27.390 16.602 1.00 38.05 ? 41 PRO A CB 1 ATOM 297 C CG . PRO A 1 41 ? 21.341 27.228 17.563 1.00 38.06 ? 41 PRO A CG 1 ATOM 298 C CD . PRO A 1 41 ? 20.317 26.291 16.989 1.00 37.61 ? 41 PRO A CD 1 ATOM 299 N N . GLY A 1 42 ? 23.264 25.052 14.591 1.00 38.93 ? 42 GLY A N 1 ATOM 300 C CA . GLY A 1 42 ? 24.276 24.423 13.748 1.00 39.05 ? 42 GLY A CA 1 ATOM 301 C C . GLY A 1 42 ? 23.870 23.064 13.199 1.00 39.32 ? 42 GLY A C 1 ATOM 302 O O . GLY A 1 42 ? 24.710 22.251 12.779 1.00 39.83 ? 42 GLY A O 1 ATOM 303 N N . LYS A 1 43 ? 22.565 22.825 13.177 1.00 38.46 ? 43 LYS A N 1 ATOM 304 C CA . LYS A 1 43 ? 22.012 21.564 12.719 1.00 37.20 ? 43 LYS A CA 1 ATOM 305 C C . LYS A 1 43 ? 21.389 21.661 11.323 1.00 35.68 ? 43 LYS A C 1 ATOM 306 O O . LYS A 1 43 ? 21.358 22.721 10.717 1.00 34.84 ? 43 LYS A O 1 ATOM 307 C CB . LYS A 1 43 ? 20.970 21.107 13.734 1.00 37.63 ? 43 LYS A CB 1 ATOM 308 C CG . LYS A 1 43 ? 21.554 20.665 15.061 1.00 39.57 ? 43 LYS A CG 1 ATOM 309 C CD . LYS A 1 43 ? 22.120 19.259 14.910 1.00 41.26 ? 43 LYS A CD 1 ATOM 310 C CE . LYS A 1 43 ? 21.127 18.371 14.121 1.00 42.11 ? 43 LYS A CE 1 ATOM 311 N NZ . LYS A 1 43 ? 20.725 17.117 14.833 1.00 43.23 ? 43 LYS A NZ 1 ATOM 312 N N . GLU A 1 44 ? 20.911 20.545 10.799 1.00 34.41 ? 44 GLU A N 1 ATOM 313 C CA . GLU A 1 44 ? 20.279 20.605 9.501 1.00 33.46 ? 44 GLU A CA 1 ATOM 314 C C . GLU A 1 44 ? 18.824 21.034 9.723 1.00 31.47 ? 44 GLU A C 1 ATOM 315 O O . GLU A 1 44 ? 18.293 20.918 10.820 1.00 30.32 ? 44 GLU A O 1 ATOM 316 C CB . GLU A 1 44 ? 20.341 19.240 8.823 1.00 34.90 ? 44 GLU A CB 1 ATOM 317 C CG . GLU A 1 44 ? 19.543 18.200 9.510 1.00 37.91 ? 44 GLU A CG 1 ATOM 318 C CD . GLU A 1 44 ? 20.247 16.858 9.569 1.00 40.15 ? 44 GLU A CD 1 ATOM 319 O OE1 . GLU A 1 44 ? 20.338 16.164 8.525 1.00 41.18 ? 44 GLU A OE1 1 ATOM 320 O OE2 . GLU A 1 44 ? 20.727 16.513 10.679 1.00 42.36 ? 44 GLU A OE2 1 ATOM 321 N N . ARG A 1 45 ? 18.196 21.528 8.668 1.00 29.70 ? 45 ARG A N 1 ATOM 322 C CA . ARG A 1 45 ? 16.806 21.961 8.721 1.00 27.47 ? 45 ARG A CA 1 ATOM 323 C C . ARG A 1 45 ? 15.960 20.701 8.760 1.00 26.13 ? 45 ARG A C 1 ATOM 324 O O . ARG A 1 45 ? 16.063 19.865 7.873 1.00 25.47 ? 45 ARG A O 1 ATOM 325 C CB . ARG A 1 45 ? 16.493 22.731 7.469 1.00 28.22 ? 45 ARG A CB 1 ATOM 326 C CG . ARG A 1 45 ? 15.304 23.608 7.545 1.00 30.22 ? 45 ARG A CG 1 ATOM 327 C CD . ARG A 1 45 ? 15.063 24.164 6.172 1.00 32.59 ? 45 ARG A CD 1 ATOM 328 N NE . ARG A 1 45 ? 14.924 25.599 6.217 1.00 35.43 ? 45 ARG A NE 1 ATOM 329 C CZ . ARG A 1 45 ? 15.907 26.449 5.967 1.00 36.24 ? 45 ARG A CZ 1 ATOM 330 N NH1 . ARG A 1 45 ? 17.115 26.004 5.637 1.00 37.39 ? 45 ARG A NH1 1 ATOM 331 N NH2 . ARG A 1 45 ? 15.678 27.749 6.087 1.00 37.45 ? 45 ARG A NH2 1 ATOM 332 N N . ILE A 1 46 ? 15.108 20.576 9.774 1.00 23.92 ? 46 ILE A N 1 ATOM 333 C CA . ILE A 1 46 ? 14.300 19.386 9.906 1.00 22.51 ? 46 ILE A CA 1 ATOM 334 C C . ILE A 1 46 ? 12.787 19.654 9.791 1.00 21.81 ? 46 ILE A C 1 ATOM 335 O O . ILE A 1 46 ? 12.264 20.672 10.247 1.00 20.41 ? 46 ILE A O 1 ATOM 336 C CB . ILE A 1 46 ? 14.544 18.663 11.269 1.00 22.76 ? 46 ILE A CB 1 ATOM 337 C CG1 . ILE A 1 46 ? 14.062 19.570 12.387 1.00 23.53 ? 46 ILE A CG1 1 ATOM 338 C CG2 . ILE A 1 46 ? 16.035 18.338 11.491 1.00 23.63 ? 46 ILE A CG2 1 ATOM 339 C CD1 . ILE A 1 46 ? 13.977 18.876 13.745 1.00 25.21 ? 46 ILE A CD1 1 ATOM 340 N N . TYR A 1 47 ? 12.124 18.693 9.164 1.00 20.91 ? 47 TYR A N 1 ATOM 341 C CA . TYR A 1 47 ? 10.696 18.690 8.949 1.00 21.17 ? 47 TYR A CA 1 ATOM 342 C C . TYR A 1 47 ? 9.917 18.539 10.278 1.00 19.54 ? 47 TYR A C 1 ATOM 343 O O . TYR A 1 47 ? 10.303 17.761 11.142 1.00 19.28 ? 47 TYR A O 1 ATOM 344 C CB . TYR A 1 47 ? 10.369 17.528 8.022 1.00 22.13 ? 47 TYR A CB 1 ATOM 345 C CG . TYR A 1 47 ? 8.905 17.192 7.983 1.00 23.56 ? 47 TYR A CG 1 ATOM 346 C CD1 . TYR A 1 47 ? 8.417 16.049 8.624 1.00 24.41 ? 47 TYR A CD1 1 ATOM 347 C CD2 . TYR A 1 47 ? 8.017 17.989 7.277 1.00 23.90 ? 47 TYR A CD2 1 ATOM 348 C CE1 . TYR A 1 47 ? 7.069 15.708 8.552 1.00 24.93 ? 47 TYR A CE1 1 ATOM 349 C CE2 . TYR A 1 47 ? 6.669 17.656 7.195 1.00 24.27 ? 47 TYR A CE2 1 ATOM 350 C CZ . TYR A 1 47 ? 6.211 16.515 7.829 1.00 24.00 ? 47 TYR A CZ 1 ATOM 351 O OH . TYR A 1 47 ? 4.923 16.107 7.682 1.00 26.23 ? 47 TYR A OH 1 ATOM 352 N N . LEU A 1 48 ? 8.846 19.307 10.450 1.00 18.84 ? 48 LEU A N 1 ATOM 353 C CA . LEU A 1 48 ? 8.029 19.193 11.647 1.00 17.69 ? 48 LEU A CA 1 ATOM 354 C C . LEU A 1 48 ? 6.590 18.716 11.379 1.00 18.01 ? 48 LEU A C 1 ATOM 355 O O . LEU A 1 48 ? 6.120 17.780 12.022 1.00 18.10 ? 48 LEU A O 1 ATOM 356 C CB . LEU A 1 48 ? 7.967 20.524 12.381 1.00 18.58 ? 48 LEU A CB 1 ATOM 357 C CG . LEU A 1 48 ? 9.282 21.077 12.940 1.00 19.61 ? 48 LEU A CG 1 ATOM 358 C CD1 . LEU A 1 48 ? 9.008 22.443 13.494 1.00 18.23 ? 48 LEU A CD1 1 ATOM 359 C CD2 . LEU A 1 48 ? 9.834 20.146 14.022 1.00 19.78 ? 48 LEU A CD2 1 ATOM 360 N N . ALA A 1 49 ? 5.890 19.356 10.448 1.00 17.26 ? 49 ALA A N 1 ATOM 361 C CA . ALA A 1 49 ? 4.493 18.994 10.194 1.00 17.88 ? 49 ALA A CA 1 ATOM 362 C C . ALA A 1 49 ? 3.991 19.465 8.848 1.00 19.01 ? 49 ALA A C 1 ATOM 363 O O . ALA A 1 49 ? 4.548 20.398 8.261 1.00 19.76 ? 49 ALA A O 1 ATOM 364 C CB . ALA A 1 49 ? 3.600 19.615 11.287 1.00 17.23 ? 49 ALA A CB 1 ATOM 365 N N . THR A 1 50 ? 2.941 18.820 8.337 1.00 19.03 ? 50 THR A N 1 ATOM 366 C CA . THR A 1 50 ? 2.358 19.307 7.097 1.00 20.60 ? 50 THR A CA 1 ATOM 367 C C . THR A 1 50 ? 0.839 19.318 7.258 1.00 19.80 ? 50 THR A C 1 ATOM 368 O O . THR A 1 50 ? 0.278 18.557 8.042 1.00 19.17 ? 50 THR A O 1 ATOM 369 C CB . THR A 1 50 ? 2.766 18.479 5.794 1.00 22.06 ? 50 THR A CB 1 ATOM 370 O OG1 . THR A 1 50 ? 1.955 17.321 5.652 1.00 26.95 ? 50 THR A OG1 1 ATOM 371 C CG2 . THR A 1 50 ? 4.135 17.982 5.862 1.00 22.74 ? 50 THR A CG2 1 ATOM 372 N N . ILE A 1 51 ? 0.189 20.247 6.573 1.00 19.47 ? 51 ILE A N 1 ATOM 373 C CA . ILE A 1 51 ? -1.266 20.294 6.608 1.00 19.69 ? 51 ILE A CA 1 ATOM 374 C C . ILE A 1 51 ? -1.778 20.429 5.172 1.00 19.17 ? 51 ILE A C 1 ATOM 375 O O . ILE A 1 51 ? -1.379 21.357 4.440 1.00 20.46 ? 51 ILE A O 1 ATOM 376 C CB . ILE A 1 51 ? -1.771 21.412 7.544 1.00 18.31 ? 51 ILE A CB 1 ATOM 377 C CG1 . ILE A 1 51 ? -3.301 21.350 7.633 1.00 19.81 ? 51 ILE A CG1 1 ATOM 378 C CG2 . ILE A 1 51 ? -1.289 22.744 7.094 1.00 19.49 ? 51 ILE A CG2 1 ATOM 379 C CD1 . ILE A 1 51 ? -3.874 22.157 8.809 1.00 16.28 ? 51 ILE A CD1 1 ATOM 380 N N . GLY A 1 52 ? -2.604 19.462 4.782 1.00 18.68 ? 52 GLY A N 1 ATOM 381 C CA . GLY A 1 52 ? -3.183 19.412 3.454 1.00 18.31 ? 52 GLY A CA 1 ATOM 382 C C . GLY A 1 52 ? -4.139 20.556 3.195 1.00 18.33 ? 52 GLY A C 1 ATOM 383 O O . GLY A 1 52 ? -4.396 21.359 4.090 1.00 16.91 ? 52 GLY A O 1 ATOM 384 N N . ARG A 1 53 ? -4.649 20.657 1.973 1.00 19.75 ? 53 ARG A N 1 ATOM 385 C CA . ARG A 1 53 ? -5.559 21.742 1.651 1.00 21.77 ? 53 ARG A CA 1 ATOM 386 C C . ARG A 1 53 ? -6.982 21.195 1.516 1.00 23.30 ? 53 ARG A C 1 ATOM 387 O O . ARG A 1 53 ? -7.922 21.960 1.398 1.00 25.37 ? 53 ARG A O 1 ATOM 388 C CB . ARG A 1 53 ? -5.139 22.403 0.348 1.00 22.88 ? 53 ARG A CB 1 ATOM 389 C CG . ARG A 1 53 ? -4.386 21.422 -0.531 1.00 24.75 ? 53 ARG A CG 1 ATOM 390 C CD . ARG A 1 53 ? -3.895 21.985 -1.878 1.00 24.33 ? 53 ARG A CD 1 ATOM 391 N NE . ARG A 1 53 ? -3.145 20.908 -2.551 1.00 28.22 ? 53 ARG A NE 1 ATOM 392 C CZ . ARG A 1 53 ? -2.311 21.065 -3.575 1.00 27.35 ? 53 ARG A CZ 1 ATOM 393 N NH1 . ARG A 1 53 ? -2.111 22.279 -4.121 1.00 26.99 ? 53 ARG A NH1 1 ATOM 394 N NH2 . ARG A 1 53 ? -1.620 20.002 -4.008 1.00 29.12 ? 53 ARG A NH2 1 ATOM 395 N N . ASN A 1 54 ? -7.127 19.873 1.547 1.00 24.64 ? 54 ASN A N 1 ATOM 396 C CA . ASN A 1 54 ? -8.414 19.223 1.418 1.00 26.21 ? 54 ASN A CA 1 ATOM 397 C C . ASN A 1 54 ? -9.007 18.817 2.767 1.00 25.90 ? 54 ASN A C 1 ATOM 398 O O . ASN A 1 54 ? -8.309 18.344 3.654 1.00 26.33 ? 54 ASN A O 1 ATOM 399 C CB . ASN A 1 54 ? -8.293 17.952 0.558 1.00 27.96 ? 54 ASN A CB 1 ATOM 400 C CG . ASN A 1 54 ? -8.228 18.235 -0.940 1.00 31.36 ? 54 ASN A CG 1 ATOM 401 O OD1 . ASN A 1 54 ? -8.088 17.298 -1.749 1.00 34.36 ? 54 ASN A OD1 1 ATOM 402 N ND2 . ASN A 1 54 ? -8.335 19.511 -1.332 1.00 31.73 ? 54 ASN A ND2 1 ATOM 403 N N . LEU A 1 55 ? -10.304 19.026 2.911 1.00 27.21 ? 55 LEU A N 1 ATOM 404 C CA . LEU A 1 55 ? -11.018 18.657 4.133 1.00 28.59 ? 55 LEU A CA 1 ATOM 405 C C . LEU A 1 55 ? -11.088 17.131 4.225 1.00 29.04 ? 55 LEU A C 1 ATOM 406 O O . LEU A 1 55 ? -11.358 16.458 3.241 1.00 29.72 ? 55 LEU A O 1 ATOM 407 C CB . LEU A 1 55 ? -12.449 19.197 4.097 1.00 28.51 ? 55 LEU A CB 1 ATOM 408 C CG . LEU A 1 55 ? -12.941 20.571 4.564 1.00 28.82 ? 55 LEU A CG 1 ATOM 409 C CD1 . LEU A 1 55 ? -12.090 21.098 5.705 1.00 28.65 ? 55 LEU A CD1 1 ATOM 410 C CD2 . LEU A 1 55 ? -12.962 21.510 3.425 1.00 30.64 ? 55 LEU A CD2 1 ATOM 411 N N . VAL A 1 56 ? -10.863 16.587 5.408 1.00 30.06 ? 56 VAL A N 1 ATOM 412 C CA . VAL A 1 56 ? -10.930 15.148 5.626 1.00 31.65 ? 56 VAL A CA 1 ATOM 413 C C . VAL A 1 56 ? -12.268 14.891 6.366 1.00 32.50 ? 56 VAL A C 1 ATOM 414 O O . VAL A 1 56 ? -12.835 13.792 6.368 1.00 32.39 ? 56 VAL A O 1 ATOM 415 C CB . VAL A 1 56 ? -9.707 14.712 6.465 1.00 32.32 ? 56 VAL A CB 1 ATOM 416 C CG1 . VAL A 1 56 ? -9.895 13.348 7.006 1.00 33.94 ? 56 VAL A CG1 1 ATOM 417 C CG2 . VAL A 1 56 ? -8.417 14.742 5.571 1.00 33.92 ? 56 VAL A CG2 1 ATOM 418 N N . GLY A 1 57 ? -12.754 15.949 6.991 1.00 32.75 ? 57 GLY A N 1 ATOM 419 C CA . GLY A 1 57 ? -13.995 15.924 7.731 1.00 32.60 ? 57 GLY A CA 1 ATOM 420 C C . GLY A 1 57 ? -14.425 17.376 7.714 1.00 33.02 ? 57 GLY A C 1 ATOM 421 O O . GLY A 1 57 ? -13.673 18.228 7.226 1.00 32.61 ? 57 GLY A O 1 ATOM 422 N N . PRO A 1 58 ? -15.603 17.703 8.261 1.00 33.62 ? 58 PRO A N 1 ATOM 423 C CA . PRO A 1 58 ? -16.114 19.073 8.287 1.00 33.89 ? 58 PRO A CA 1 ATOM 424 C C . PRO A 1 58 ? -15.133 20.112 8.805 1.00 34.39 ? 58 PRO A C 1 ATOM 425 O O . PRO A 1 58 ? -15.005 21.204 8.237 1.00 34.13 ? 58 PRO A O 1 ATOM 426 C CB . PRO A 1 58 ? -17.351 18.958 9.177 1.00 34.00 ? 58 PRO A CB 1 ATOM 427 C CG . PRO A 1 58 ? -17.845 17.598 8.863 1.00 34.26 ? 58 PRO A CG 1 ATOM 428 C CD . PRO A 1 58 ? -16.560 16.785 8.903 1.00 34.04 ? 58 PRO A CD 1 ATOM 429 N N . SER A 1 59 ? -14.429 19.787 9.880 1.00 34.74 ? 59 SER A N 1 ATOM 430 C CA . SER A 1 59 ? -13.504 20.770 10.449 1.00 35.56 ? 59 SER A CA 1 ATOM 431 C C . SER A 1 59 ? -12.028 20.342 10.459 1.00 34.48 ? 59 SER A C 1 ATOM 432 O O . SER A 1 59 ? -11.204 20.964 11.123 1.00 34.24 ? 59 SER A O 1 ATOM 433 C CB . SER A 1 59 ? -13.964 21.102 11.878 1.00 36.26 ? 59 SER A CB 1 ATOM 434 O OG . SER A 1 59 ? -13.343 22.289 12.335 1.00 39.88 ? 59 SER A OG 1 ATOM 435 N N . ASP A 1 60 ? -11.686 19.299 9.719 1.00 33.46 ? 60 ASP A N 1 ATOM 436 C CA . ASP A 1 60 ? -10.312 18.838 9.741 1.00 32.73 ? 60 ASP A CA 1 ATOM 437 C C . ASP A 1 60 ? -9.670 18.634 8.384 1.00 31.44 ? 60 ASP A C 1 ATOM 438 O O . ASP A 1 60 ? -10.206 17.928 7.539 1.00 31.20 ? 60 ASP A O 1 ATOM 439 C CB . ASP A 1 60 ? -10.203 17.535 10.561 1.00 34.42 ? 60 ASP A CB 1 ATOM 440 C CG . ASP A 1 60 ? -10.274 17.777 12.086 1.00 36.70 ? 60 ASP A CG 1 ATOM 441 O OD1 . ASP A 1 60 ? -9.818 16.899 12.871 1.00 38.41 ? 60 ASP A OD1 1 ATOM 442 O OD2 . ASP A 1 60 ? -10.785 18.839 12.505 1.00 38.21 ? 60 ASP A OD2 1 ATOM 443 N N . PHE A 1 61 ? -8.512 19.262 8.189 1.00 29.42 ? 61 PHE A N 1 ATOM 444 C CA . PHE A 1 61 ? -7.763 19.108 6.946 1.00 28.71 ? 61 PHE A CA 1 ATOM 445 C C . PHE A 1 61 ? -6.769 17.965 7.153 1.00 28.50 ? 61 PHE A C 1 ATOM 446 O O . PHE A 1 61 ? -6.508 17.612 8.294 1.00 28.60 ? 61 PHE A O 1 ATOM 447 C CB . PHE A 1 61 ? -7.018 20.391 6.605 1.00 26.83 ? 61 PHE A CB 1 ATOM 448 C CG . PHE A 1 61 ? -7.908 21.526 6.242 1.00 25.79 ? 61 PHE A CG 1 ATOM 449 C CD1 . PHE A 1 61 ? -8.467 22.332 7.230 1.00 25.59 ? 61 PHE A CD1 1 ATOM 450 C CD2 . PHE A 1 61 ? -8.180 21.808 4.906 1.00 24.85 ? 61 PHE A CD2 1 ATOM 451 C CE1 . PHE A 1 61 ? -9.277 23.418 6.902 1.00 24.96 ? 61 PHE A CE1 1 ATOM 452 C CE2 . PHE A 1 61 ? -8.994 22.893 4.557 1.00 24.80 ? 61 PHE A CE2 1 ATOM 453 C CZ . PHE A 1 61 ? -9.547 23.704 5.569 1.00 24.90 ? 61 PHE A CZ 1 ATOM 454 N N . TYR A 1 62 ? -6.258 17.359 6.073 1.00 29.21 ? 62 TYR A N 1 ATOM 455 C CA . TYR A 1 62 ? -5.270 16.280 6.193 1.00 30.36 ? 62 TYR A CA 1 ATOM 456 C C . TYR A 1 62 ? -4.080 16.854 6.966 1.00 29.15 ? 62 TYR A C 1 ATOM 457 O O . TYR A 1 62 ? -3.677 17.992 6.718 1.00 28.43 ? 62 TYR A O 1 ATOM 458 C CB . TYR A 1 62 ? -4.776 15.784 4.821 1.00 34.28 ? 62 TYR A CB 1 ATOM 459 C CG . TYR A 1 62 ? -3.656 14.769 4.981 1.00 37.39 ? 62 TYR A CG 1 ATOM 460 C CD1 . TYR A 1 62 ? -3.904 13.538 5.594 1.00 39.21 ? 62 TYR A CD1 1 ATOM 461 C CD2 . TYR A 1 62 ? -2.326 15.085 4.654 1.00 39.13 ? 62 TYR A CD2 1 ATOM 462 C CE1 . TYR A 1 62 ? -2.867 12.642 5.899 1.00 40.87 ? 62 TYR A CE1 1 ATOM 463 C CE2 . TYR A 1 62 ? -1.263 14.188 4.961 1.00 41.34 ? 62 TYR A CE2 1 ATOM 464 C CZ . TYR A 1 62 ? -1.549 12.965 5.588 1.00 41.85 ? 62 TYR A CZ 1 ATOM 465 O OH . TYR A 1 62 ? -0.559 12.043 5.943 1.00 43.82 ? 62 TYR A OH 1 ATOM 466 N N . THR A 1 63 ? -3.503 16.037 7.841 1.00 27.50 ? 63 THR A N 1 ATOM 467 C CA . THR A 1 63 ? -2.454 16.458 8.742 1.00 27.29 ? 63 THR A CA 1 ATOM 468 C C . THR A 1 63 ? -1.371 15.379 9.034 1.00 27.13 ? 63 THR A C 1 ATOM 469 O O . THR A 1 63 ? -1.714 14.237 9.290 1.00 26.36 ? 63 THR A O 1 ATOM 470 C CB . THR A 1 63 ? -3.194 16.875 10.062 1.00 27.65 ? 63 THR A CB 1 ATOM 471 O OG1 . THR A 1 63 ? -3.150 18.288 10.252 1.00 26.85 ? 63 THR A OG1 1 ATOM 472 C CG2 . THR A 1 63 ? -2.645 16.174 11.229 1.00 27.72 ? 63 THR A CG2 1 ATOM 473 N N . ARG A 1 64 ? -0.079 15.736 8.984 1.00 27.02 ? 64 ARG A N 1 ATOM 474 C CA . ARG A 1 64 ? 1.031 14.806 9.309 1.00 27.44 ? 64 ARG A CA 1 ATOM 475 C C . ARG A 1 64 ? 2.045 15.489 10.258 1.00 26.33 ? 64 ARG A C 1 ATOM 476 O O . ARG A 1 64 ? 2.311 16.680 10.142 1.00 24.82 ? 64 ARG A O 1 ATOM 477 C CB . ARG A 1 64 ? 1.808 14.304 8.052 1.00 29.71 ? 64 ARG A CB 1 ATOM 478 C CG . ARG A 1 64 ? 1.444 12.892 7.534 1.00 33.93 ? 64 ARG A CG 1 ATOM 479 C CD . ARG A 1 64 ? 2.623 12.101 6.871 1.00 37.13 ? 64 ARG A CD 1 ATOM 480 N NE . ARG A 1 64 ? 3.569 12.963 6.129 1.00 40.31 ? 64 ARG A NE 1 ATOM 481 C CZ . ARG A 1 64 ? 3.328 13.561 4.952 1.00 41.68 ? 64 ARG A CZ 1 ATOM 482 N NH1 . ARG A 1 64 ? 2.161 13.427 4.310 1.00 41.88 ? 64 ARG A NH1 1 ATOM 483 N NH2 . ARG A 1 64 ? 4.246 14.363 4.436 1.00 43.17 ? 64 ARG A NH2 1 ATOM 484 N N . TYR A 1 65 ? 2.599 14.723 11.194 1.00 25.87 ? 65 TYR A N 1 ATOM 485 C CA . TYR A 1 65 ? 3.589 15.233 12.138 1.00 26.55 ? 65 TYR A CA 1 ATOM 486 C C . TYR A 1 65 ? 4.797 14.330 12.220 1.00 27.77 ? 65 TYR A C 1 ATOM 487 O O . TYR A 1 65 ? 4.677 13.129 12.051 1.00 29.08 ? 65 TYR A O 1 ATOM 488 C CB . TYR A 1 65 ? 3.034 15.294 13.541 1.00 24.70 ? 65 TYR A CB 1 ATOM 489 C CG . TYR A 1 65 ? 1.859 16.197 13.667 1.00 23.72 ? 65 TYR A CG 1 ATOM 490 C CD1 . TYR A 1 65 ? 2.028 17.562 13.874 1.00 22.89 ? 65 TYR A CD1 1 ATOM 491 C CD2 . TYR A 1 65 ? 0.565 15.696 13.554 1.00 22.14 ? 65 TYR A CD2 1 ATOM 492 C CE1 . TYR A 1 65 ? 0.940 18.401 13.972 1.00 21.38 ? 65 TYR A CE1 1 ATOM 493 C CE2 . TYR A 1 65 ? -0.523 16.532 13.641 1.00 21.99 ? 65 TYR A CE2 1 ATOM 494 C CZ . TYR A 1 65 ? -0.332 17.884 13.856 1.00 21.09 ? 65 TYR A CZ 1 ATOM 495 O OH . TYR A 1 65 ? -1.426 18.708 13.981 1.00 21.02 ? 65 TYR A OH 1 ATOM 496 N N . ALA A 1 66 ? 5.955 14.925 12.507 1.00 28.63 ? 66 ALA A N 1 ATOM 497 C CA . ALA A 1 66 ? 7.197 14.191 12.666 1.00 28.39 ? 66 ALA A CA 1 ATOM 498 C C . ALA A 1 66 ? 7.166 13.640 14.081 1.00 28.89 ? 66 ALA A C 1 ATOM 499 O O . ALA A 1 66 ? 6.605 14.245 14.990 1.00 27.49 ? 66 ALA A O 1 ATOM 500 C CB . ALA A 1 66 ? 8.403 15.129 12.501 1.00 27.43 ? 66 ALA A CB 1 ATOM 501 N N . ASP A 1 67 ? 7.800 12.494 14.266 1.00 30.22 ? 67 ASP A N 1 ATOM 502 C CA . ASP A 1 67 ? 7.871 11.844 15.564 1.00 30.93 ? 67 ASP A CA 1 ATOM 503 C C . ASP A 1 67 ? 8.302 12.709 16.740 1.00 31.59 ? 67 ASP A C 1 ATOM 504 O O . ASP A 1 67 ? 7.740 12.644 17.835 1.00 32.86 ? 67 ASP A O 1 ATOM 505 C CB . ASP A 1 67 ? 8.816 10.660 15.451 1.00 32.22 ? 67 ASP A CB 1 ATOM 506 C CG . ASP A 1 67 ? 8.125 9.361 15.683 1.00 31.40 ? 67 ASP A CG 1 ATOM 507 O OD1 . ASP A 1 67 ? 6.933 9.373 16.047 1.00 32.17 ? 67 ASP A OD1 1 ATOM 508 O OD2 . ASP A 1 67 ? 8.784 8.330 15.508 1.00 32.39 ? 67 ASP A OD2 1 ATOM 509 N N . SER A 1 68 ? 9.325 13.520 16.545 1.00 31.06 ? 68 SER A N 1 ATOM 510 C CA . SER A 1 68 ? 9.800 14.349 17.631 1.00 30.42 ? 68 SER A CA 1 ATOM 511 C C . SER A 1 68 ? 8.782 15.340 18.208 1.00 29.65 ? 68 SER A C 1 ATOM 512 O O . SER A 1 68 ? 8.973 15.826 19.317 1.00 29.27 ? 68 SER A O 1 ATOM 513 C CB . SER A 1 68 ? 11.036 15.132 17.170 1.00 30.82 ? 68 SER A CB 1 ATOM 514 O OG . SER A 1 68 ? 10.696 15.953 16.062 1.00 31.35 ? 68 SER A OG 1 ATOM 515 N N . VAL A 1 69 ? 7.713 15.649 17.472 1.00 28.95 ? 69 VAL A N 1 ATOM 516 C CA . VAL A 1 69 ? 6.747 16.637 17.940 1.00 27.65 ? 69 VAL A CA 1 ATOM 517 C C . VAL A 1 69 ? 5.289 16.143 17.954 1.00 28.64 ? 69 VAL A C 1 ATOM 518 O O . VAL A 1 69 ? 4.403 16.821 18.468 1.00 27.42 ? 69 VAL A O 1 ATOM 519 C CB . VAL A 1 69 ? 6.820 17.906 17.053 1.00 27.55 ? 69 VAL A CB 1 ATOM 520 C CG1 . VAL A 1 69 ? 8.269 18.304 16.826 1.00 27.76 ? 69 VAL A CG1 1 ATOM 521 C CG2 . VAL A 1 69 ? 6.162 17.650 15.701 1.00 26.27 ? 69 VAL A CG2 1 ATOM 522 N N . LYS A 1 70 ? 5.029 14.977 17.380 1.00 29.30 ? 70 LYS A N 1 ATOM 523 C CA . LYS A 1 70 ? 3.654 14.488 17.358 1.00 30.67 ? 70 LYS A CA 1 ATOM 524 C C . LYS A 1 70 ? 3.181 14.456 18.808 1.00 30.55 ? 70 LYS A C 1 ATOM 525 O O . LYS A 1 70 ? 3.931 14.045 19.706 1.00 31.51 ? 70 LYS A O 1 ATOM 526 C CB . LYS A 1 70 ? 3.593 13.100 16.731 1.00 32.59 ? 70 LYS A CB 1 ATOM 527 C CG . LYS A 1 70 ? 2.181 12.616 16.418 1.00 35.13 ? 70 LYS A CG 1 ATOM 528 C CD . LYS A 1 70 ? 2.223 11.277 15.695 1.00 36.89 ? 70 LYS A CD 1 ATOM 529 C CE . LYS A 1 70 ? 0.821 10.807 15.335 1.00 37.28 ? 70 LYS A CE 1 ATOM 530 N NZ . LYS A 1 70 ? 0.813 9.387 14.849 1.00 39.44 ? 70 LYS A NZ 1 ATOM 531 N N . GLY A 1 71 ? 1.969 14.932 19.059 1.00 29.62 ? 71 GLY A N 1 ATOM 532 C CA . GLY A 1 71 ? 1.494 14.924 20.430 1.00 27.84 ? 71 GLY A CA 1 ATOM 533 C C . GLY A 1 71 ? 1.725 16.226 21.167 1.00 26.70 ? 71 GLY A C 1 ATOM 534 O O . GLY A 1 71 ? 0.979 16.530 22.089 1.00 26.99 ? 71 GLY A O 1 ATOM 535 N N . ARG A 1 72 ? 2.751 16.997 20.781 1.00 24.05 ? 72 ARG A N 1 ATOM 536 C CA . ARG A 1 72 ? 3.037 18.280 21.419 1.00 21.85 ? 72 ARG A CA 1 ATOM 537 C C . ARG A 1 72 ? 2.703 19.474 20.530 1.00 20.25 ? 72 ARG A C 1 ATOM 538 O O . ARG A 1 72 ? 2.426 20.553 21.035 1.00 20.46 ? 72 ARG A O 1 ATOM 539 C CB . ARG A 1 72 ? 4.523 18.417 21.795 1.00 21.51 ? 72 ARG A CB 1 ATOM 540 C CG . ARG A 1 72 ? 5.101 17.409 22.757 1.00 23.59 ? 72 ARG A CG 1 ATOM 541 C CD . ARG A 1 72 ? 6.646 17.311 22.543 1.00 23.12 ? 72 ARG A CD 1 ATOM 542 N NE . ARG A 1 72 ? 7.238 18.572 22.890 1.00 23.54 ? 72 ARG A NE 1 ATOM 543 C CZ . ARG A 1 72 ? 8.230 19.195 22.269 1.00 22.68 ? 72 ARG A CZ 1 ATOM 544 N NH1 . ARG A 1 72 ? 8.829 18.696 21.203 1.00 24.09 ? 72 ARG A NH1 1 ATOM 545 N NH2 . ARG A 1 72 ? 8.579 20.370 22.725 1.00 20.46 ? 72 ARG A NH2 1 ATOM 546 N N . PHE A 1 73 ? 2.785 19.295 19.215 1.00 18.60 ? 73 PHE A N 1 ATOM 547 C CA . PHE A 1 73 ? 2.514 20.372 18.269 1.00 18.73 ? 73 PHE A CA 1 ATOM 548 C C . PHE A 1 73 ? 1.231 20.059 17.497 1.00 18.21 ? 73 PHE A C 1 ATOM 549 O O . PHE A 1 73 ? 0.919 18.909 17.226 1.00 17.81 ? 73 PHE A O 1 ATOM 550 C CB . PHE A 1 73 ? 3.660 20.527 17.239 1.00 19.20 ? 73 PHE A CB 1 ATOM 551 C CG . PHE A 1 73 ? 4.945 21.085 17.813 1.00 20.48 ? 73 PHE A CG 1 ATOM 552 C CD1 . PHE A 1 73 ? 5.116 21.212 19.184 1.00 20.48 ? 73 PHE A CD1 1 ATOM 553 C CD2 . PHE A 1 73 ? 6.006 21.428 16.974 1.00 21.58 ? 73 PHE A CD2 1 ATOM 554 C CE1 . PHE A 1 73 ? 6.309 21.663 19.725 1.00 21.84 ? 73 PHE A CE1 1 ATOM 555 C CE2 . PHE A 1 73 ? 7.212 21.879 17.511 1.00 21.31 ? 73 PHE A CE2 1 ATOM 556 C CZ . PHE A 1 73 ? 7.353 21.994 18.893 1.00 21.85 ? 73 PHE A CZ 1 ATOM 557 N N . ALA A 1 74 ? 0.510 21.110 17.132 1.00 17.47 ? 74 ALA A N 1 ATOM 558 C CA . ALA A 1 74 ? -0.729 20.957 16.396 1.00 17.72 ? 74 ALA A CA 1 ATOM 559 C C . ALA A 1 74 ? -0.739 22.023 15.306 1.00 17.07 ? 74 ALA A C 1 ATOM 560 O O . ALA A 1 74 ? -0.590 23.189 15.586 1.00 17.89 ? 74 ALA A O 1 ATOM 561 C CB . ALA A 1 74 ? -1.920 21.155 17.365 1.00 18.22 ? 74 ALA A CB 1 ATOM 562 N N . VAL A 1 75 ? -0.918 21.625 14.058 1.00 17.04 ? 75 VAL A N 1 ATOM 563 C CA . VAL A 1 75 ? -0.947 22.581 12.958 1.00 17.24 ? 75 VAL A CA 1 ATOM 564 C C . VAL A 1 75 ? -2.426 22.775 12.542 1.00 17.98 ? 75 VAL A C 1 ATOM 565 O O . VAL A 1 75 ? -3.187 21.817 12.489 1.00 17.77 ? 75 VAL A O 1 ATOM 566 C CB . VAL A 1 75 ? -0.088 22.043 11.766 1.00 17.49 ? 75 VAL A CB 1 ATOM 567 C CG1 . VAL A 1 75 ? -0.651 20.722 11.297 1.00 17.87 ? 75 VAL A CG1 1 ATOM 568 C CG2 . VAL A 1 75 ? -0.026 23.094 10.614 1.00 18.59 ? 75 VAL A CG2 1 ATOM 569 N N . SER A 1 76 ? -2.829 24.009 12.260 1.00 18.06 ? 76 SER A N 1 ATOM 570 C CA . SER A 1 76 ? -4.209 24.267 11.886 1.00 18.88 ? 76 SER A CA 1 ATOM 571 C C . SER A 1 76 ? -4.302 25.241 10.739 1.00 19.67 ? 76 SER A C 1 ATOM 572 O O . SER A 1 76 ? -3.387 26.037 10.487 1.00 20.93 ? 76 SER A O 1 ATOM 573 C CB . SER A 1 76 ? -4.999 24.792 13.087 1.00 17.99 ? 76 SER A CB 1 ATOM 574 O OG . SER A 1 76 ? -4.498 26.046 13.467 1.00 19.95 ? 76 SER A OG 1 ATOM 575 N N . ARG A 1 77 ? -5.433 25.224 10.084 1.00 19.32 ? 77 ARG A N 1 ATOM 576 C CA . ARG A 1 77 ? -5.636 26.052 8.902 1.00 20.66 ? 77 ARG A CA 1 ATOM 577 C C . ARG A 1 77 ? -6.770 27.085 8.946 1.00 21.31 ? 77 ARG A C 1 ATOM 578 O O . ARG A 1 77 ? -7.876 26.713 9.355 1.00 21.06 ? 77 ARG A O 1 ATOM 579 C CB . ARG A 1 77 ? -5.882 24.986 7.786 1.00 21.75 ? 77 ARG A CB 1 ATOM 580 C CG . ARG A 1 77 ? -6.080 25.348 6.328 1.00 23.96 ? 77 ARG A CG 1 ATOM 581 C CD . ARG A 1 77 ? -5.810 24.034 5.366 1.00 26.58 ? 77 ARG A CD 1 ATOM 582 N NE . ARG A 1 77 ? -5.077 24.780 4.326 1.00 26.46 ? 77 ARG A NE 1 ATOM 583 C CZ . ARG A 1 77 ? -3.914 24.637 3.679 1.00 27.84 ? 77 ARG A CZ 1 ATOM 584 N NH1 . ARG A 1 77 ? -2.905 23.688 3.663 1.00 28.06 ? 77 ARG A NH1 1 ATOM 585 N NH2 . ARG A 1 77 ? -3.711 25.767 3.133 1.00 29.95 ? 77 ARG A NH2 1 ATOM 586 N N . ASP A 1 78 ? -6.464 28.381 8.625 1.00 21.41 ? 78 ASP A N 1 ATOM 587 C CA . ASP A 1 78 ? -7.507 29.406 8.477 1.00 21.67 ? 78 ASP A CA 1 ATOM 588 C C . ASP A 1 78 ? -7.393 30.058 7.151 1.00 22.21 ? 78 ASP A C 1 ATOM 589 O O . ASP A 1 78 ? -6.738 31.156 7.003 1.00 22.67 ? 78 ASP A O 1 ATOM 590 C CB . ASP A 1 78 ? -7.599 30.638 9.323 1.00 23.98 ? 78 ASP A CB 1 ATOM 591 C CG . ASP A 1 78 ? -9.048 31.206 9.311 1.00 25.25 ? 78 ASP A CG 1 ATOM 592 O OD1 . ASP A 1 78 ? -9.561 31.825 8.358 1.00 31.29 ? 78 ASP A OD1 1 ATOM 593 O OD2 . ASP A 1 78 ? -9.663 30.980 10.325 1.00 30.17 ? 78 ASP A OD2 1 ATOM 594 N N . ASN A 1 79 ? -8.085 29.508 6.214 1.00 22.25 ? 79 ASN A N 1 ATOM 595 C CA . ASN A 1 79 ? -8.026 30.084 4.918 1.00 22.25 ? 79 ASN A CA 1 ATOM 596 C C . ASN A 1 79 ? -8.547 31.535 4.961 1.00 21.41 ? 79 ASN A C 1 ATOM 597 O O . ASN A 1 79 ? -8.060 32.409 4.222 1.00 21.56 ? 79 ASN A O 1 ATOM 598 C CB . ASN A 1 79 ? -8.834 29.221 4.021 1.00 22.52 ? 79 ASN A CB 1 ATOM 599 C CG . ASN A 1 79 ? -8.095 27.943 3.623 1.00 24.99 ? 79 ASN A CG 1 ATOM 600 O OD1 . ASN A 1 79 ? -8.713 27.035 3.044 1.00 24.12 ? 79 ASN A OD1 1 ATOM 601 N ND2 . ASN A 1 79 ? -6.771 27.867 3.897 1.00 22.29 ? 79 ASN A ND2 1 ATOM 602 N N . ALA A 1 80 ? -9.574 31.775 5.787 1.00 21.66 ? 80 ALA A N 1 ATOM 603 C CA . ALA A 1 80 ? -10.219 33.084 5.895 1.00 22.49 ? 80 ALA A CA 1 ATOM 604 C C . ALA A 1 80 ? -9.251 34.206 6.259 1.00 22.91 ? 80 ALA A C 1 ATOM 605 O O . ALA A 1 80 ? -9.459 35.366 5.872 1.00 21.98 ? 80 ALA A O 1 ATOM 606 C CB . ALA A 1 80 ? -11.389 33.027 6.931 1.00 22.35 ? 80 ALA A CB 1 ATOM 607 N N . LYS A 1 81 ? -8.222 33.873 7.042 1.00 22.83 ? 81 LYS A N 1 ATOM 608 C CA . LYS A 1 81 ? -7.226 34.869 7.425 1.00 22.75 ? 81 LYS A CA 1 ATOM 609 C C . LYS A 1 81 ? -5.914 34.660 6.674 1.00 21.81 ? 81 LYS A C 1 ATOM 610 O O . LYS A 1 81 ? -4.913 35.306 6.990 1.00 21.83 ? 81 LYS A O 1 ATOM 611 C CB . LYS A 1 81 ? -6.976 34.830 8.938 1.00 24.92 ? 81 LYS A CB 1 ATOM 612 C CG . LYS A 1 81 ? -8.186 35.316 9.756 1.00 28.68 ? 81 LYS A CG 1 ATOM 613 C CD . LYS A 1 81 ? -7.910 35.311 11.256 1.00 32.45 ? 81 LYS A CD 1 ATOM 614 C CE . LYS A 1 81 ? -7.255 33.960 11.717 1.00 34.79 ? 81 LYS A CE 1 ATOM 615 N NZ . LYS A 1 81 ? -7.893 32.676 11.155 1.00 34.52 ? 81 LYS A NZ 1 ATOM 616 N N . ASN A 1 82 ? -5.939 33.784 5.666 1.00 19.84 ? 82 ASN A N 1 ATOM 617 C CA . ASN A 1 82 ? -4.762 33.451 4.828 1.00 18.37 ? 82 ASN A CA 1 ATOM 618 C C . ASN A 1 82 ? -3.608 33.053 5.752 1.00 17.93 ? 82 ASN A C 1 ATOM 619 O O . ASN A 1 82 ? -2.464 33.454 5.530 1.00 16.86 ? 82 ASN A O 1 ATOM 620 C CB . ASN A 1 82 ? -4.331 34.647 3.972 1.00 18.01 ? 82 ASN A CB 1 ATOM 621 C CG . ASN A 1 82 ? -4.000 34.237 2.568 1.00 17.85 ? 82 ASN A CG 1 ATOM 622 O OD1 . ASN A 1 82 ? -4.373 33.159 2.167 1.00 20.63 ? 82 ASN A OD1 1 ATOM 623 N ND2 . ASN A 1 82 ? -3.306 35.086 1.807 1.00 18.71 ? 82 ASN A ND2 1 ATOM 624 N N . THR A 1 83 ? -3.921 32.233 6.749 1.00 16.55 ? 83 THR A N 1 ATOM 625 C CA . THR A 1 83 ? -2.946 31.830 7.737 1.00 16.85 ? 83 THR A CA 1 ATOM 626 C C . THR A 1 83 ? -3.014 30.371 8.133 1.00 16.45 ? 83 THR A C 1 ATOM 627 O O . THR A 1 83 ? -4.102 29.761 8.130 1.00 15.92 ? 83 THR A O 1 ATOM 628 C CB . THR A 1 83 ? -3.167 32.707 8.996 1.00 17.29 ? 83 THR A CB 1 ATOM 629 O OG1 . THR A 1 83 ? -2.927 34.080 8.635 1.00 18.88 ? 83 THR A OG1 1 ATOM 630 C CG2 . THR A 1 83 ? -2.251 32.301 10.145 1.00 16.38 ? 83 THR A CG2 1 ATOM 631 N N . VAL A 1 84 ? -1.851 29.785 8.435 1.00 15.42 ? 84 VAL A N 1 ATOM 632 C CA . VAL A 1 84 ? -1.781 28.404 8.926 1.00 15.66 ? 84 VAL A CA 1 ATOM 633 C C . VAL A 1 84 ? -1.045 28.572 10.266 1.00 17.03 ? 84 VAL A C 1 ATOM 634 O O . VAL A 1 84 ? -0.095 29.350 10.332 1.00 17.17 ? 84 VAL A O 1 ATOM 635 C CB . VAL A 1 84 ? -0.989 27.496 7.967 1.00 15.65 ? 84 VAL A CB 1 ATOM 636 C CG1 . VAL A 1 84 ? -0.528 26.252 8.697 1.00 16.39 ? 84 VAL A CG1 1 ATOM 637 C CG2 . VAL A 1 84 ? -1.895 27.081 6.794 1.00 16.14 ? 84 VAL A CG2 1 ATOM 638 N N . ASN A 1 85 ? -1.486 27.910 11.337 1.00 16.24 ? 85 ASN A N 1 ATOM 639 C CA . ASN A 1 85 ? -0.814 28.093 12.621 1.00 16.91 ? 85 ASN A CA 1 ATOM 640 C C . ASN A 1 85 ? -0.133 26.830 13.124 1.00 16.58 ? 85 ASN A C 1 ATOM 641 O O . ASN A 1 85 ? -0.460 25.705 12.723 1.00 15.35 ? 85 ASN A O 1 ATOM 642 C CB . ASN A 1 85 ? -1.782 28.554 13.707 1.00 17.91 ? 85 ASN A CB 1 ATOM 643 C CG . ASN A 1 85 ? -2.509 29.825 13.346 1.00 19.19 ? 85 ASN A CG 1 ATOM 644 O OD1 . ASN A 1 85 ? -3.684 29.803 13.038 1.00 19.71 ? 85 ASN A OD1 1 ATOM 645 N ND2 . ASN A 1 85 ? -1.811 30.941 13.390 1.00 19.84 ? 85 ASN A ND2 1 ATOM 646 N N . LEU A 1 86 ? 0.832 27.032 14.008 1.00 15.20 ? 86 LEU A N 1 ATOM 647 C CA . LEU A 1 86 ? 1.528 25.908 14.602 1.00 14.95 ? 86 LEU A CA 1 ATOM 648 C C . LEU A 1 86 ? 1.479 26.179 16.091 1.00 14.64 ? 86 LEU A C 1 ATOM 649 O O . LEU A 1 86 ? 2.127 27.121 16.579 1.00 14.74 ? 86 LEU A O 1 ATOM 650 C CB . LEU A 1 86 ? 2.999 25.824 14.141 1.00 14.65 ? 86 LEU A CB 1 ATOM 651 C CG . LEU A 1 86 ? 3.771 24.633 14.736 1.00 15.30 ? 86 LEU A CG 1 ATOM 652 C CD1 . LEU A 1 86 ? 3.205 23.311 14.217 1.00 13.96 ? 86 LEU A CD1 1 ATOM 653 C CD2 . LEU A 1 86 ? 5.277 24.768 14.383 1.00 13.38 ? 86 LEU A CD2 1 ATOM 654 N N . GLN A 1 87 ? 0.698 25.369 16.803 1.00 15.19 ? 87 GLN A N 1 ATOM 655 C CA . GLN A 1 87 ? 0.549 25.489 18.251 1.00 15.16 ? 87 GLN A CA 1 ATOM 656 C C . GLN A 1 87 ? 1.677 24.611 18.824 1.00 15.71 ? 87 GLN A C 1 ATOM 657 O O . GLN A 1 87 ? 1.766 23.452 18.485 1.00 16.24 ? 87 GLN A O 1 ATOM 658 C CB . GLN A 1 87 ? -0.816 24.914 18.663 1.00 17.34 ? 87 GLN A CB 1 ATOM 659 C CG . GLN A 1 87 ? -1.101 24.880 20.175 1.00 15.91 ? 87 GLN A CG 1 ATOM 660 C CD . GLN A 1 87 ? -1.045 26.229 20.786 1.00 18.26 ? 87 GLN A CD 1 ATOM 661 O OE1 . GLN A 1 87 ? -1.553 27.221 20.223 1.00 19.87 ? 87 GLN A OE1 1 ATOM 662 N NE2 . GLN A 1 87 ? -0.431 26.310 21.949 1.00 20.25 ? 87 GLN A NE2 1 ATOM 663 N N . MET A 1 88 ? 2.525 25.159 19.682 1.00 16.28 ? 88 MET A N 1 ATOM 664 C CA . MET A 1 88 ? 3.649 24.377 20.222 1.00 17.19 ? 88 MET A CA 1 ATOM 665 C C . MET A 1 88 ? 3.529 24.309 21.738 1.00 16.21 ? 88 MET A C 1 ATOM 666 O O . MET A 1 88 ? 3.618 25.316 22.397 1.00 16.46 ? 88 MET A O 1 ATOM 667 C CB . MET A 1 88 ? 4.956 25.044 19.810 1.00 17.42 ? 88 MET A CB 1 ATOM 668 C CG . MET A 1 88 ? 5.112 25.159 18.300 1.00 19.45 ? 88 MET A CG 1 ATOM 669 S SD . MET A 1 88 ? 6.754 25.840 17.911 1.00 21.94 ? 88 MET A SD 1 ATOM 670 C CE . MET A 1 88 ? 6.639 27.374 18.503 1.00 18.30 ? 88 MET A CE 1 ATOM 671 N N . ASN A 1 89 ? 3.281 23.111 22.261 1.00 16.61 ? 89 ASN A N 1 ATOM 672 C CA . ASN A 1 89 ? 3.113 22.930 23.685 1.00 17.08 ? 89 ASN A CA 1 ATOM 673 C C . ASN A 1 89 ? 4.294 22.249 24.359 1.00 18.35 ? 89 ASN A C 1 ATOM 674 O O . ASN A 1 89 ? 5.122 21.610 23.689 1.00 17.58 ? 89 ASN A O 1 ATOM 675 C CB . ASN A 1 89 ? 1.806 22.151 23.951 1.00 16.03 ? 89 ASN A CB 1 ATOM 676 C CG . ASN A 1 89 ? 0.578 22.917 23.453 1.00 13.40 ? 89 ASN A CG 1 ATOM 677 O OD1 . ASN A 1 89 ? 0.552 24.131 23.497 1.00 14.13 ? 89 ASN A OD1 1 ATOM 678 N ND2 . ASN A 1 89 ? -0.425 22.209 22.995 1.00 15.49 ? 89 ASN A ND2 1 ATOM 679 N N . SER A 1 90 ? 4.364 22.447 25.677 1.00 18.88 ? 90 SER A N 1 ATOM 680 C CA . SER A 1 90 ? 5.400 21.877 26.533 1.00 21.31 ? 90 SER A CA 1 ATOM 681 C C . SER A 1 90 ? 6.773 22.018 25.894 1.00 20.83 ? 90 SER A C 1 ATOM 682 O O . SER A 1 90 ? 7.433 21.023 25.661 1.00 20.56 ? 90 SER A O 1 ATOM 683 C CB . SER A 1 90 ? 5.103 20.404 26.751 1.00 22.00 ? 90 SER A CB 1 ATOM 684 O OG . SER A 1 90 ? 3.724 20.251 26.926 1.00 26.18 ? 90 SER A OG 1 ATOM 685 N N . LEU A 1 91 ? 7.182 23.248 25.628 1.00 21.77 ? 91 LEU A N 1 ATOM 686 C CA . LEU A 1 91 ? 8.449 23.494 24.983 1.00 23.74 ? 91 LEU A CA 1 ATOM 687 C C . LEU A 1 91 ? 9.673 23.147 25.854 1.00 25.58 ? 91 LEU A C 1 ATOM 688 O O . LEU A 1 91 ? 9.665 23.358 27.073 1.00 25.20 ? 91 LEU A O 1 ATOM 689 C CB . LEU A 1 91 ? 8.514 24.951 24.545 1.00 23.04 ? 91 LEU A CB 1 ATOM 690 C CG . LEU A 1 91 ? 7.615 25.371 23.380 1.00 24.10 ? 91 LEU A CG 1 ATOM 691 C CD1 . LEU A 1 91 ? 7.630 26.874 23.218 1.00 23.56 ? 91 LEU A CD1 1 ATOM 692 C CD2 . LEU A 1 91 ? 8.109 24.697 22.094 1.00 24.10 ? 91 LEU A CD2 1 ATOM 693 N N . LYS A 1 92 ? 10.720 22.638 25.207 1.00 26.70 ? 92 LYS A N 1 ATOM 694 C CA . LYS A 1 92 ? 11.956 22.264 25.898 1.00 28.02 ? 92 LYS A CA 1 ATOM 695 C C . LYS A 1 92 ? 13.100 23.075 25.297 1.00 27.33 ? 92 LYS A C 1 ATOM 696 O O . LYS A 1 92 ? 12.955 23.681 24.233 1.00 26.16 ? 92 LYS A O 1 ATOM 697 C CB . LYS A 1 92 ? 12.232 20.782 25.696 1.00 29.69 ? 92 LYS A CB 1 ATOM 698 C CG . LYS A 1 92 ? 11.091 19.877 26.105 1.00 33.42 ? 92 LYS A CG 1 ATOM 699 C CD . LYS A 1 92 ? 11.251 18.534 25.418 1.00 36.50 ? 92 LYS A CD 1 ATOM 700 C CE . LYS A 1 92 ? 10.081 17.608 25.678 1.00 38.61 ? 92 LYS A CE 1 ATOM 701 N NZ . LYS A 1 92 ? 10.462 16.183 25.394 1.00 41.16 ? 92 LYS A NZ 1 ATOM 702 N N . PRO A 1 93 ? 14.253 23.122 25.979 1.00 27.90 ? 93 PRO A N 1 ATOM 703 C CA . PRO A 1 93 ? 15.327 23.907 25.380 1.00 27.21 ? 93 PRO A CA 1 ATOM 704 C C . PRO A 1 93 ? 15.707 23.383 24.010 1.00 26.69 ? 93 PRO A C 1 ATOM 705 O O . PRO A 1 93 ? 16.105 24.152 23.161 1.00 28.21 ? 93 PRO A O 1 ATOM 706 C CB . PRO A 1 93 ? 16.438 23.785 26.408 1.00 27.75 ? 93 PRO A CB 1 ATOM 707 C CG . PRO A 1 93 ? 15.674 23.825 27.699 1.00 27.63 ? 93 PRO A CG 1 ATOM 708 C CD . PRO A 1 93 ? 14.575 22.794 27.384 1.00 27.83 ? 93 PRO A CD 1 ATOM 709 N N . GLU A 1 94 ? 15.552 22.086 23.790 1.00 26.86 ? 94 GLU A N 1 ATOM 710 C CA . GLU A 1 94 ? 15.896 21.497 22.500 1.00 28.13 ? 94 GLU A CA 1 ATOM 711 C C . GLU A 1 94 ? 14.993 21.996 21.359 1.00 26.91 ? 94 GLU A C 1 ATOM 712 O O . GLU A 1 94 ? 15.223 21.669 20.182 1.00 25.39 ? 94 GLU A O 1 ATOM 713 C CB . GLU A 1 94 ? 15.790 19.976 22.536 1.00 31.60 ? 94 GLU A CB 1 ATOM 714 C CG . GLU A 1 94 ? 16.612 19.264 23.603 1.00 37.99 ? 94 GLU A CG 1 ATOM 715 C CD . GLU A 1 94 ? 16.308 17.744 23.627 1.00 41.48 ? 94 GLU A CD 1 ATOM 716 O OE1 . GLU A 1 94 ? 15.160 17.376 23.266 1.00 43.44 ? 94 GLU A OE1 1 ATOM 717 O OE2 . GLU A 1 94 ? 17.196 16.923 24.007 1.00 43.35 ? 94 GLU A OE2 1 ATOM 718 N N . ASP A 1 95 ? 13.961 22.769 21.697 1.00 24.76 ? 95 ASP A N 1 ATOM 719 C CA . ASP A 1 95 ? 13.071 23.283 20.656 1.00 22.96 ? 95 ASP A CA 1 ATOM 720 C C . ASP A 1 95 ? 13.527 24.620 20.160 1.00 21.75 ? 95 ASP A C 1 ATOM 721 O O . ASP A 1 95 ? 12.915 25.176 19.260 1.00 21.21 ? 95 ASP A O 1 ATOM 722 C CB . ASP A 1 95 ? 11.638 23.411 21.166 1.00 21.53 ? 95 ASP A CB 1 ATOM 723 C CG . ASP A 1 95 ? 11.015 22.087 21.438 1.00 20.80 ? 95 ASP A CG 1 ATOM 724 O OD1 . ASP A 1 95 ? 11.017 21.225 20.549 1.00 20.49 ? 95 ASP A OD1 1 ATOM 725 O OD2 . ASP A 1 95 ? 10.513 21.894 22.555 1.00 20.67 ? 95 ASP A OD2 1 ATOM 726 N N . THR A 1 96 ? 14.593 25.160 20.757 1.00 20.56 ? 96 THR A N 1 ATOM 727 C CA . THR A 1 96 ? 15.119 26.446 20.331 1.00 19.31 ? 96 THR A CA 1 ATOM 728 C C . THR A 1 96 ? 15.586 26.338 18.888 1.00 19.07 ? 96 THR A C 1 ATOM 729 O O . THR A 1 96 ? 16.355 25.448 18.538 1.00 19.19 ? 96 THR A O 1 ATOM 730 C CB . THR A 1 96 ? 16.299 26.876 21.214 1.00 20.56 ? 96 THR A CB 1 ATOM 731 O OG1 . THR A 1 96 ? 15.832 27.193 22.527 1.00 20.48 ? 96 THR A OG1 1 ATOM 732 C CG2 . THR A 1 96 ? 16.958 28.085 20.645 1.00 20.75 ? 96 THR A CG2 1 ATOM 733 N N . ALA A 1 97 ? 15.135 27.263 18.045 1.00 17.90 ? 97 ALA A N 1 ATOM 734 C CA . ALA A 1 97 ? 15.489 27.197 16.641 1.00 18.00 ? 97 ALA A CA 1 ATOM 735 C C . ALA A 1 97 ? 14.813 28.331 15.881 1.00 17.23 ? 97 ALA A C 1 ATOM 736 O O . ALA A 1 97 ? 14.108 29.131 16.484 1.00 17.98 ? 97 ALA A O 1 ATOM 737 C CB . ALA A 1 97 ? 15.034 25.821 16.062 1.00 17.62 ? 97 ALA A CB 1 ATOM 738 N N . VAL A 1 98 ? 15.067 28.426 14.582 1.00 16.39 ? 98 VAL A N 1 ATOM 739 C CA . VAL A 1 98 ? 14.387 29.414 13.743 1.00 15.83 ? 98 VAL A CA 1 ATOM 740 C C . VAL A 1 98 ? 13.331 28.498 13.090 1.00 14.12 ? 98 VAL A C 1 ATOM 741 O O . VAL A 1 98 ? 13.682 27.430 12.623 1.00 14.16 ? 98 VAL A O 1 ATOM 742 C CB . VAL A 1 98 ? 15.321 30.001 12.679 1.00 16.86 ? 98 VAL A CB 1 ATOM 743 C CG1 . VAL A 1 98 ? 14.500 30.815 11.664 1.00 18.52 ? 98 VAL A CG1 1 ATOM 744 C CG2 . VAL A 1 98 ? 16.334 30.962 13.353 1.00 18.31 ? 98 VAL A CG2 1 ATOM 745 N N . TYR A 1 99 ? 12.064 28.899 13.074 1.00 13.67 ? 99 TYR A N 1 ATOM 746 C CA . TYR A 1 99 ? 10.979 28.056 12.525 1.00 11.50 ? 99 TYR A CA 1 ATOM 747 C C . TYR A 1 99 ? 10.527 28.618 11.187 1.00 11.88 ? 99 TYR A C 1 ATOM 748 O O . TYR A 1 99 ? 10.430 29.802 11.043 1.00 11.49 ? 99 TYR A O 1 ATOM 749 C CB . TYR A 1 99 ? 9.841 28.032 13.548 1.00 12.68 ? 99 TYR A CB 1 ATOM 750 C CG . TYR A 1 99 ? 10.118 27.123 14.731 1.00 12.15 ? 99 TYR A CG 1 ATOM 751 C CD1 . TYR A 1 99 ? 11.061 27.449 15.706 1.00 13.05 ? 99 TYR A CD1 1 ATOM 752 C CD2 . TYR A 1 99 ? 9.448 25.902 14.853 1.00 12.21 ? 99 TYR A CD2 1 ATOM 753 C CE1 . TYR A 1 99 ? 11.343 26.563 16.761 1.00 11.07 ? 99 TYR A CE1 1 ATOM 754 C CE2 . TYR A 1 99 ? 9.711 25.059 15.884 1.00 11.95 ? 99 TYR A CE2 1 ATOM 755 C CZ . TYR A 1 99 ? 10.660 25.384 16.828 1.00 11.85 ? 99 TYR A CZ 1 ATOM 756 O OH . TYR A 1 99 ? 10.936 24.418 17.756 1.00 13.77 ? 99 TYR A OH 1 ATOM 757 N N . TYR A 1 100 ? 10.291 27.760 10.200 1.00 12.14 ? 100 TYR A N 1 ATOM 758 C CA . TYR A 1 100 ? 9.930 28.239 8.891 1.00 13.99 ? 100 TYR A CA 1 ATOM 759 C C . TYR A 1 100 ? 8.705 27.527 8.397 1.00 13.58 ? 100 TYR A C 1 ATOM 760 O O . TYR A 1 100 ? 8.524 26.363 8.718 1.00 13.16 ? 100 TYR A O 1 ATOM 761 C CB . TYR A 1 100 ? 11.026 27.862 7.847 1.00 15.44 ? 100 TYR A CB 1 ATOM 762 C CG . TYR A 1 100 ? 12.379 28.461 8.050 1.00 18.84 ? 100 TYR A CG 1 ATOM 763 C CD1 . TYR A 1 100 ? 13.303 27.892 8.959 1.00 20.11 ? 100 TYR A CD1 1 ATOM 764 C CD2 . TYR A 1 100 ? 12.758 29.596 7.344 1.00 18.86 ? 100 TYR A CD2 1 ATOM 765 C CE1 . TYR A 1 100 ? 14.565 28.457 9.145 1.00 19.70 ? 100 TYR A CE1 1 ATOM 766 C CE2 . TYR A 1 100 ? 14.014 30.164 7.521 1.00 19.68 ? 100 TYR A CE2 1 ATOM 767 C CZ . TYR A 1 100 ? 14.917 29.597 8.421 1.00 20.97 ? 100 TYR A CZ 1 ATOM 768 O OH . TYR A 1 100 ? 16.164 30.204 8.569 1.00 21.14 ? 100 TYR A OH 1 ATOM 769 N N . CYS A 1 101 ? 7.881 28.209 7.609 1.00 13.35 ? 101 CYS A N 1 ATOM 770 C CA . CYS A 1 101 ? 6.791 27.485 6.945 1.00 12.99 ? 101 CYS A CA 1 ATOM 771 C C . CYS A 1 101 ? 7.148 27.544 5.454 1.00 13.78 ? 101 CYS A C 1 ATOM 772 O O . CYS A 1 101 ? 7.863 28.451 4.999 1.00 16.20 ? 101 CYS A O 1 ATOM 773 C CB . CYS A 1 101 ? 5.419 28.125 7.176 0.81 12.94 ? 101 CYS A CB 1 ATOM 774 S SG . CYS A 1 101 ? 5.361 29.827 6.733 0.81 11.57 ? 101 CYS A SG 1 ATOM 775 N N . ALA A 1 102 ? 6.684 26.570 4.689 1.00 13.48 ? 102 ALA A N 1 ATOM 776 C CA . ALA A 1 102 ? 6.963 26.519 3.258 1.00 12.80 ? 102 ALA A CA 1 ATOM 777 C C . ALA A 1 102 ? 5.680 26.038 2.595 1.00 12.83 ? 102 ALA A C 1 ATOM 778 O O . ALA A 1 102 ? 4.820 25.456 3.255 1.00 13.27 ? 102 ALA A O 1 ATOM 779 C CB . ALA A 1 102 ? 8.100 25.528 2.984 1.00 12.96 ? 102 ALA A CB 1 ATOM 780 N N . ALA A 1 103 ? 5.585 26.249 1.289 1.00 12.84 ? 103 ALA A N 1 ATOM 781 C CA . ALA A 1 103 ? 4.420 25.862 0.519 1.00 14.18 ? 103 ALA A CA 1 ATOM 782 C C . ALA A 1 103 ? 4.761 25.115 -0.729 1.00 15.54 ? 103 ALA A C 1 ATOM 783 O O . ALA A 1 103 ? 5.740 25.431 -1.442 1.00 15.07 ? 103 ALA A O 1 ATOM 784 C CB . ALA A 1 103 ? 3.617 27.111 0.137 1.00 14.53 ? 103 ALA A CB 1 ATOM 785 N N . LYS A 1 104 ? 3.973 24.098 -1.010 1.00 15.69 ? 104 LYS A N 1 ATOM 786 C CA . LYS A 1 104 ? 4.147 23.373 -2.252 1.00 19.00 ? 104 LYS A CA 1 ATOM 787 C C . LYS A 1 104 ? 2.774 23.061 -2.838 1.00 21.29 ? 104 LYS A C 1 ATOM 788 O O . LYS A 1 104 ? 1.744 23.171 -2.164 1.00 20.12 ? 104 LYS A O 1 ATOM 789 C CB . LYS A 1 104 ? 4.955 22.092 -2.065 1.00 19.24 ? 104 LYS A CB 1 ATOM 790 C CG . LYS A 1 104 ? 4.473 21.186 -0.998 1.00 20.59 ? 104 LYS A CG 1 ATOM 791 C CD . LYS A 1 104 ? 5.249 19.877 -1.093 1.00 23.89 ? 104 LYS A CD 1 ATOM 792 C CE . LYS A 1 104 ? 4.764 18.912 -0.028 1.00 25.05 ? 104 LYS A CE 1 ATOM 793 N NZ . LYS A 1 104 ? 5.307 17.564 -0.211 1.00 26.64 ? 104 LYS A NZ 1 ATOM 794 N N . THR A 1 105 ? 2.759 22.653 -4.093 1.00 23.93 ? 105 THR A N 1 ATOM 795 C CA . THR A 1 105 ? 1.516 22.366 -4.773 1.00 28.25 ? 105 THR A CA 1 ATOM 796 C C . THR A 1 105 ? 1.236 20.894 -5.039 1.00 30.32 ? 105 THR A C 1 ATOM 797 O O . THR A 1 105 ? 0.282 20.566 -5.733 1.00 31.13 ? 105 THR A O 1 ATOM 798 C CB . THR A 1 105 ? 1.478 23.131 -6.062 1.00 28.94 ? 105 THR A CB 1 ATOM 799 O OG1 . THR A 1 105 ? 2.701 22.905 -6.765 1.00 30.40 ? 105 THR A OG1 1 ATOM 800 C CG2 . THR A 1 105 ? 1.400 24.609 -5.780 1.00 31.06 ? 105 THR A CG2 1 ATOM 801 N N . THR A 1 106 ? 2.058 19.996 -4.500 1.00 32.49 ? 106 THR A N 1 ATOM 802 C CA . THR A 1 106 ? 1.804 18.572 -4.695 1.00 35.19 ? 106 THR A CA 1 ATOM 803 C C . THR A 1 106 ? 1.961 17.885 -3.351 1.00 35.92 ? 106 THR A C 1 ATOM 804 O O . THR A 1 106 ? 2.578 18.410 -2.432 1.00 35.29 ? 106 THR A O 1 ATOM 805 C CB . THR A 1 106 ? 2.760 17.904 -5.770 1.00 35.43 ? 106 THR A CB 1 ATOM 806 O OG1 . THR A 1 106 ? 4.019 17.594 -5.179 1.00 36.17 ? 106 THR A OG1 1 ATOM 807 C CG2 . THR A 1 106 ? 3.021 18.857 -6.952 1.00 36.98 ? 106 THR A CG2 1 ATOM 808 N N . THR A 1 107 ? 1.386 16.703 -3.243 1.00 37.81 ? 107 THR A N 1 ATOM 809 C CA . THR A 1 107 ? 1.442 15.947 -2.006 1.00 40.07 ? 107 THR A CA 1 ATOM 810 C C . THR A 1 107 ? 2.706 15.111 -1.891 1.00 40.40 ? 107 THR A C 1 ATOM 811 O O . THR A 1 107 ? 3.053 14.651 -0.806 1.00 40.48 ? 107 THR A O 1 ATOM 812 C CB . THR A 1 107 ? 0.222 15.011 -1.904 1.00 41.55 ? 107 THR A CB 1 ATOM 813 O OG1 . THR A 1 107 ? -0.003 14.400 -3.188 1.00 43.05 ? 107 THR A OG1 1 ATOM 814 C CG2 . THR A 1 107 ? -1.026 15.797 -1.476 1.00 41.92 ? 107 THR A CG2 1 ATOM 815 N N . TRP A 1 108 ? 3.398 14.928 -3.009 1.00 40.77 ? 108 TRP A N 1 ATOM 816 C CA . TRP A 1 108 ? 4.611 14.120 -3.037 1.00 41.79 ? 108 TRP A CA 1 ATOM 817 C C . TRP A 1 108 ? 5.878 14.774 -2.495 1.00 43.09 ? 108 TRP A C 1 ATOM 818 O O . TRP A 1 108 ? 5.880 15.960 -2.163 1.00 42.25 ? 108 TRP A O 1 ATOM 819 C CB . TRP A 1 108 ? 4.872 13.641 -4.462 1.00 40.75 ? 108 TRP A CB 1 ATOM 820 C CG . TRP A 1 108 ? 3.815 12.738 -4.935 1.00 39.87 ? 108 TRP A CG 1 ATOM 821 C CD1 . TRP A 1 108 ? 2.733 13.066 -5.698 1.00 39.39 ? 108 TRP A CD1 1 ATOM 822 C CD2 . TRP A 1 108 ? 3.688 11.360 -4.629 1.00 39.09 ? 108 TRP A CD2 1 ATOM 823 N NE1 . TRP A 1 108 ? 1.933 11.962 -5.881 1.00 39.55 ? 108 TRP A NE1 1 ATOM 824 C CE2 . TRP A 1 108 ? 2.507 10.880 -5.222 1.00 38.79 ? 108 TRP A CE2 1 ATOM 825 C CE3 . TRP A 1 108 ? 4.465 10.446 -3.892 1.00 38.63 ? 108 TRP A CE3 1 ATOM 826 C CZ2 . TRP A 1 108 ? 2.067 9.570 -5.127 1.00 38.71 ? 108 TRP A CZ2 1 ATOM 827 C CZ3 . TRP A 1 108 ? 4.034 9.127 -3.787 1.00 38.03 ? 108 TRP A CZ3 1 ATOM 828 C CH2 . TRP A 1 108 ? 2.850 8.704 -4.403 1.00 38.26 ? 108 TRP A CH2 1 ATOM 829 N N . GLY A 1 109 ? 6.951 13.979 -2.436 1.00 44.64 ? 109 GLY A N 1 ATOM 830 C CA . GLY A 1 109 ? 8.239 14.450 -1.944 1.00 45.90 ? 109 GLY A CA 1 ATOM 831 C C . GLY A 1 109 ? 8.371 13.995 -0.505 1.00 46.96 ? 109 GLY A C 1 ATOM 832 O O . GLY A 1 109 ? 9.358 13.391 -0.091 1.00 47.50 ? 109 GLY A O 1 ATOM 833 N N . GLY A 1 110 ? 7.352 14.315 0.269 1.00 47.77 ? 110 GLY A N 1 ATOM 834 C CA . GLY A 1 110 ? 7.300 13.906 1.657 1.00 48.81 ? 110 GLY A CA 1 ATOM 835 C C . GLY A 1 110 ? 8.359 14.079 2.744 1.00 49.02 ? 110 GLY A C 1 ATOM 836 O O . GLY A 1 110 ? 9.226 13.223 2.918 1.00 49.89 ? 110 GLY A O 1 ATOM 837 N N . ASN A 1 111 ? 8.280 15.179 3.487 1.00 48.17 ? 111 ASN A N 1 ATOM 838 C CA . ASN A 1 111 ? 9.151 15.386 4.636 1.00 47.52 ? 111 ASN A CA 1 ATOM 839 C C . ASN A 1 111 ? 10.622 15.761 4.455 1.00 46.18 ? 111 ASN A C 1 ATOM 840 O O . ASN A 1 111 ? 11.384 15.749 5.422 1.00 46.17 ? 111 ASN A O 1 ATOM 841 C CB . ASN A 1 111 ? 9.016 14.160 5.533 1.00 48.46 ? 111 ASN A CB 1 ATOM 842 C CG . ASN A 1 111 ? 7.545 13.740 5.717 1.00 50.45 ? 111 ASN A CG 1 ATOM 843 O OD1 . ASN A 1 111 ? 6.635 14.306 5.094 1.00 51.25 ? 111 ASN A OD1 1 ATOM 844 N ND2 . ASN A 1 111 ? 7.311 12.747 6.565 1.00 51.22 ? 111 ASN A ND2 1 ATOM 845 N N . ASP A 1 112 ? 11.013 16.077 3.218 1.00 44.83 ? 112 ASP A N 1 ATOM 846 C CA . ASP A 1 112 ? 12.368 16.539 2.907 1.00 43.26 ? 112 ASP A CA 1 ATOM 847 C C . ASP A 1 112 ? 12.149 18.026 2.698 1.00 41.09 ? 112 ASP A C 1 ATOM 848 O O . ASP A 1 112 ? 11.080 18.433 2.255 1.00 39.98 ? 112 ASP A O 1 ATOM 849 C CB . ASP A 1 112 ? 12.860 16.016 1.557 1.00 44.75 ? 112 ASP A CB 1 ATOM 850 C CG . ASP A 1 112 ? 13.280 14.575 1.596 1.00 47.13 ? 112 ASP A CG 1 ATOM 851 O OD1 . ASP A 1 112 ? 14.406 14.290 2.062 1.00 49.09 ? 112 ASP A OD1 1 ATOM 852 O OD2 . ASP A 1 112 ? 12.484 13.720 1.147 1.00 48.55 ? 112 ASP A OD2 1 ATOM 853 N N . PRO A 1 113 ? 13.144 18.856 3.016 1.00 39.52 ? 113 PRO A N 1 ATOM 854 C CA . PRO A 1 113 ? 12.979 20.299 2.814 1.00 38.12 ? 113 PRO A CA 1 ATOM 855 C C . PRO A 1 113 ? 13.385 20.594 1.356 1.00 36.77 ? 113 PRO A C 1 ATOM 856 O O . PRO A 1 113 ? 13.370 21.718 0.875 1.00 36.71 ? 113 PRO A O 1 ATOM 857 C CB . PRO A 1 113 ? 13.964 20.883 3.808 1.00 38.60 ? 113 PRO A CB 1 ATOM 858 C CG . PRO A 1 113 ? 15.088 19.909 3.715 1.00 39.46 ? 113 PRO A CG 1 ATOM 859 C CD . PRO A 1 113 ? 14.385 18.574 3.758 1.00 39.39 ? 113 PRO A CD 1 ATOM 860 N N . ASN A 1 114 ? 13.713 19.545 0.642 1.00 35.67 ? 114 ASN A N 1 ATOM 861 C CA . ASN A 1 114 ? 14.184 19.678 -0.715 1.00 35.23 ? 114 ASN A CA 1 ATOM 862 C C . ASN A 1 114 ? 13.241 20.155 -1.814 1.00 34.68 ? 114 ASN A C 1 ATOM 863 O O . ASN A 1 114 ? 13.635 20.988 -2.633 1.00 34.77 ? 114 ASN A O 1 ATOM 864 C CB . ASN A 1 114 ? 14.851 18.359 -1.097 1.00 36.34 ? 114 ASN A CB 1 ATOM 865 C CG . ASN A 1 114 ? 16.046 18.050 -0.193 1.00 37.73 ? 114 ASN A CG 1 ATOM 866 O OD1 . ASN A 1 114 ? 17.169 18.496 -0.456 1.00 39.56 ? 114 ASN A OD1 1 ATOM 867 N ND2 . ASN A 1 114 ? 15.802 17.325 0.898 1.00 37.80 ? 114 ASN A ND2 1 ATOM 868 N N . ASN A 1 115 ? 11.997 19.691 -1.824 1.00 32.81 ? 115 ASN A N 1 ATOM 869 C CA . ASN A 1 115 ? 11.131 20.072 -2.920 1.00 31.75 ? 115 ASN A CA 1 ATOM 870 C C . ASN A 1 115 ? 9.930 20.982 -2.663 1.00 30.35 ? 115 ASN A C 1 ATOM 871 O O . ASN A 1 115 ? 8.825 20.714 -3.144 1.00 30.82 ? 115 ASN A O 1 ATOM 872 C CB . ASN A 1 115 ? 10.693 18.796 -3.653 1.00 33.41 ? 115 ASN A CB 1 ATOM 873 C CG . ASN A 1 115 ? 11.887 17.846 -3.948 1.00 35.80 ? 115 ASN A CG 1 ATOM 874 O OD1 . ASN A 1 115 ? 12.877 18.233 -4.608 1.00 36.37 ? 115 ASN A OD1 1 ATOM 875 N ND2 . ASN A 1 115 ? 11.796 16.605 -3.453 1.00 37.30 ? 115 ASN A ND2 1 ATOM 876 N N . TRP A 1 116 ? 10.160 22.079 -1.947 1.00 26.88 ? 116 TRP A N 1 ATOM 877 C CA . TRP A 1 116 ? 9.110 23.043 -1.663 1.00 23.75 ? 116 TRP A CA 1 ATOM 878 C C . TRP A 1 116 ? 9.309 24.285 -2.521 1.00 23.17 ? 116 TRP A C 1 ATOM 879 O O . TRP A 1 116 ? 10.434 24.784 -2.676 1.00 21.29 ? 116 TRP A O 1 ATOM 880 C CB . TRP A 1 116 ? 9.111 23.393 -0.176 1.00 22.38 ? 116 TRP A CB 1 ATOM 881 C CG . TRP A 1 116 ? 8.848 22.198 0.674 1.00 20.94 ? 116 TRP A CG 1 ATOM 882 C CD1 . TRP A 1 116 ? 9.706 21.152 0.924 1.00 21.35 ? 116 TRP A CD1 1 ATOM 883 C CD2 . TRP A 1 116 ? 7.603 21.863 1.317 1.00 20.98 ? 116 TRP A CD2 1 ATOM 884 N NE1 . TRP A 1 116 ? 9.068 20.195 1.679 1.00 21.89 ? 116 TRP A NE1 1 ATOM 885 C CE2 . TRP A 1 116 ? 7.783 20.601 1.932 1.00 20.91 ? 116 TRP A CE2 1 ATOM 886 C CE3 . TRP A 1 116 ? 6.365 22.510 1.426 1.00 20.61 ? 116 TRP A CE3 1 ATOM 887 C CZ2 . TRP A 1 116 ? 6.760 19.966 2.648 1.00 21.00 ? 116 TRP A CZ2 1 ATOM 888 C CZ3 . TRP A 1 116 ? 5.333 21.872 2.155 1.00 21.08 ? 116 TRP A CZ3 1 ATOM 889 C CH2 . TRP A 1 116 ? 5.548 20.614 2.752 1.00 20.95 ? 116 TRP A CH2 1 ATOM 890 N N . ASN A 1 117 ? 8.199 24.761 -3.084 1.00 21.98 ? 117 ASN A N 1 ATOM 891 C CA . ASN A 1 117 ? 8.166 25.904 -3.971 1.00 21.04 ? 117 ASN A CA 1 ATOM 892 C C . ASN A 1 117 ? 8.483 27.262 -3.363 1.00 20.20 ? 117 ASN A C 1 ATOM 893 O O . ASN A 1 117 ? 9.232 28.057 -3.932 1.00 18.05 ? 117 ASN A O 1 ATOM 894 C CB . ASN A 1 117 ? 6.773 26.029 -4.626 1.00 22.00 ? 117 ASN A CB 1 ATOM 895 C CG . ASN A 1 117 ? 6.422 24.862 -5.535 1.00 23.87 ? 117 ASN A CG 1 ATOM 896 O OD1 . ASN A 1 117 ? 6.573 24.934 -6.761 1.00 26.34 ? 117 ASN A OD1 1 ATOM 897 N ND2 . ASN A 1 117 ? 5.942 23.793 -4.948 1.00 24.48 ? 117 ASN A ND2 1 ATOM 898 N N . TYR A 1 118 ? 7.843 27.552 -2.236 1.00 18.72 ? 118 TYR A N 1 ATOM 899 C CA . TYR A 1 118 ? 7.971 28.855 -1.611 1.00 18.37 ? 118 TYR A CA 1 ATOM 900 C C . TYR A 1 118 ? 8.298 28.702 -0.139 1.00 18.26 ? 118 TYR A C 1 ATOM 901 O O . TYR A 1 118 ? 7.795 27.781 0.505 1.00 17.82 ? 118 TYR A O 1 ATOM 902 C CB . TYR A 1 118 ? 6.662 29.625 -1.795 1.00 18.82 ? 118 TYR A CB 1 ATOM 903 C CG . TYR A 1 118 ? 6.266 29.753 -3.248 1.00 20.60 ? 118 TYR A CG 1 ATOM 904 C CD1 . TYR A 1 118 ? 5.303 28.926 -3.823 1.00 21.93 ? 118 TYR A CD1 1 ATOM 905 C CD2 . TYR A 1 118 ? 6.876 30.692 -4.058 1.00 22.83 ? 118 TYR A CD2 1 ATOM 906 C CE1 . TYR A 1 118 ? 4.958 29.042 -5.173 1.00 22.51 ? 118 TYR A CE1 1 ATOM 907 C CE2 . TYR A 1 118 ? 6.541 30.812 -5.419 1.00 24.59 ? 118 TYR A CE2 1 ATOM 908 C CZ . TYR A 1 118 ? 5.586 29.987 -5.957 1.00 23.86 ? 118 TYR A CZ 1 ATOM 909 O OH . TYR A 1 118 ? 5.297 30.120 -7.292 1.00 27.29 ? 118 TYR A OH 1 ATOM 910 N N . TRP A 1 119 ? 9.119 29.623 0.374 1.00 17.41 ? 119 TRP A N 1 ATOM 911 C CA . TRP A 1 119 ? 9.611 29.601 1.753 1.00 16.78 ? 119 TRP A CA 1 ATOM 912 C C . TRP A 1 119 ? 9.436 30.914 2.475 1.00 17.61 ? 119 TRP A C 1 ATOM 913 O O . TRP A 1 119 ? 9.492 31.984 1.869 1.00 18.28 ? 119 TRP A O 1 ATOM 914 C CB . TRP A 1 119 ? 11.122 29.277 1.763 1.00 17.11 ? 119 TRP A CB 1 ATOM 915 C CG . TRP A 1 119 ? 11.427 27.867 1.464 1.00 14.41 ? 119 TRP A CG 1 ATOM 916 C CD1 . TRP A 1 119 ? 11.489 27.296 0.254 1.00 15.25 ? 119 TRP A CD1 1 ATOM 917 C CD2 . TRP A 1 119 ? 11.569 26.811 2.421 1.00 14.72 ? 119 TRP A CD2 1 ATOM 918 N NE1 . TRP A 1 119 ? 11.650 25.940 0.375 1.00 14.71 ? 119 TRP A NE1 1 ATOM 919 C CE2 . TRP A 1 119 ? 11.699 25.616 1.693 1.00 13.61 ? 119 TRP A CE2 1 ATOM 920 C CE3 . TRP A 1 119 ? 11.590 26.772 3.819 1.00 13.47 ? 119 TRP A CE3 1 ATOM 921 C CZ2 . TRP A 1 119 ? 11.840 24.378 2.314 1.00 15.29 ? 119 TRP A CZ2 1 ATOM 922 C CZ3 . TRP A 1 119 ? 11.728 25.551 4.437 1.00 14.05 ? 119 TRP A CZ3 1 ATOM 923 C CH2 . TRP A 1 119 ? 11.853 24.365 3.689 1.00 14.43 ? 119 TRP A CH2 1 ATOM 924 N N . GLY A 1 120 ? 9.261 30.837 3.790 1.00 17.41 ? 120 GLY A N 1 ATOM 925 C CA . GLY A 1 120 ? 9.115 32.033 4.579 1.00 18.98 ? 120 GLY A CA 1 ATOM 926 C C . GLY A 1 120 ? 10.478 32.549 4.990 1.00 22.02 ? 120 GLY A C 1 ATOM 927 O O . GLY A 1 120 ? 11.508 31.994 4.583 1.00 21.82 ? 120 GLY A O 1 ATOM 928 N N . GLN A 1 121 ? 10.473 33.593 5.807 1.00 23.41 ? 121 GLN A N 1 ATOM 929 C CA . GLN A 1 121 ? 11.690 34.252 6.278 1.00 25.87 ? 121 GLN A CA 1 ATOM 930 C C . GLN A 1 121 ? 12.280 33.582 7.516 1.00 25.38 ? 121 GLN A C 1 ATOM 931 O O . GLN A 1 121 ? 13.494 33.664 7.771 1.00 25.39 ? 121 GLN A O 1 ATOM 932 C CB . GLN A 1 121 ? 11.361 35.706 6.583 1.00 28.52 ? 121 GLN A CB 1 ATOM 933 C CG . GLN A 1 121 ? 12.455 36.465 7.331 1.00 34.55 ? 121 GLN A CG 1 ATOM 934 C CD . GLN A 1 121 ? 12.120 37.941 7.564 1.00 36.81 ? 121 GLN A CD 1 ATOM 935 O OE1 . GLN A 1 121 ? 12.243 38.778 6.649 1.00 38.57 ? 121 GLN A OE1 1 ATOM 936 N NE2 . GLN A 1 121 ? 11.698 38.269 8.800 1.00 38.98 ? 121 GLN A NE2 1 ATOM 937 N N . GLY A 1 122 ? 11.410 32.920 8.278 1.00 23.83 ? 122 GLY A N 1 ATOM 938 C CA . GLY A 1 122 ? 11.838 32.234 9.486 1.00 21.37 ? 122 GLY A CA 1 ATOM 939 C C . GLY A 1 122 ? 11.565 33.128 10.676 1.00 20.26 ? 122 GLY A C 1 ATOM 940 O O . GLY A 1 122 ? 11.624 34.344 10.579 1.00 19.65 ? 122 GLY A O 1 ATOM 941 N N . THR A 1 123 ? 11.239 32.522 11.798 1.00 20.02 ? 123 THR A N 1 ATOM 942 C CA . THR A 1 123 ? 10.961 33.282 12.999 1.00 21.19 ? 123 THR A CA 1 ATOM 943 C C . THR A 1 123 ? 11.688 32.563 14.122 1.00 20.89 ? 123 THR A C 1 ATOM 944 O O . THR A 1 123 ? 11.593 31.353 14.239 1.00 19.63 ? 123 THR A O 1 ATOM 945 C CB . THR A 1 123 ? 9.436 33.343 13.286 1.00 21.72 ? 123 THR A CB 1 ATOM 946 O OG1 . THR A 1 123 ? 9.188 34.211 14.397 1.00 23.96 ? 123 THR A OG1 1 ATOM 947 C CG2 . THR A 1 123 ? 8.878 31.984 13.630 1.00 22.18 ? 123 THR A CG2 1 ATOM 948 N N . GLN A 1 124 ? 12.423 33.320 14.936 1.00 22.68 ? 124 GLN A N 1 ATOM 949 C CA . GLN A 1 124 ? 13.212 32.765 16.032 1.00 24.40 ? 124 GLN A CA 1 ATOM 950 C C . GLN A 1 124 ? 12.445 32.473 17.311 1.00 23.77 ? 124 GLN A C 1 ATOM 951 O O . GLN A 1 124 ? 11.709 33.306 17.817 1.00 24.20 ? 124 GLN A O 1 ATOM 952 C CB . GLN A 1 124 ? 14.391 33.704 16.358 1.00 27.51 ? 124 GLN A CB 1 ATOM 953 C CG . GLN A 1 124 ? 15.242 33.258 17.555 1.00 30.84 ? 124 GLN A CG 1 ATOM 954 C CD . GLN A 1 124 ? 16.243 32.167 17.197 1.00 32.79 ? 124 GLN A CD 1 ATOM 955 O OE1 . GLN A 1 124 ? 16.325 31.112 17.852 1.00 33.65 ? 124 GLN A OE1 1 ATOM 956 N NE2 . GLN A 1 124 ? 17.023 32.418 16.162 1.00 34.31 ? 124 GLN A NE2 1 ATOM 957 N N . VAL A 1 125 ? 12.651 31.268 17.824 1.00 23.41 ? 125 VAL A N 1 ATOM 958 C CA . VAL A 1 125 ? 12.031 30.803 19.053 1.00 22.88 ? 125 VAL A CA 1 ATOM 959 C C . VAL A 1 125 ? 13.130 30.385 20.014 1.00 22.93 ? 125 VAL A C 1 ATOM 960 O O . VAL A 1 125 ? 13.940 29.509 19.688 1.00 21.95 ? 125 VAL A O 1 ATOM 961 C CB . VAL A 1 125 ? 11.117 29.594 18.802 1.00 21.35 ? 125 VAL A CB 1 ATOM 962 C CG1 . VAL A 1 125 ? 10.719 28.951 20.122 1.00 22.78 ? 125 VAL A CG1 1 ATOM 963 C CG2 . VAL A 1 125 ? 9.861 30.066 18.071 1.00 22.48 ? 125 VAL A CG2 1 ATOM 964 N N . THR A 1 126 ? 13.170 31.010 21.192 1.00 23.85 ? 126 THR A N 1 ATOM 965 C CA . THR A 1 126 ? 14.200 30.645 22.164 1.00 24.72 ? 126 THR A CA 1 ATOM 966 C C . THR A 1 126 ? 13.561 30.146 23.427 1.00 25.49 ? 126 THR A C 1 ATOM 967 O O . THR A 1 126 ? 12.791 30.867 24.086 1.00 25.94 ? 126 THR A O 1 ATOM 968 C CB . THR A 1 126 ? 15.098 31.815 22.552 1.00 24.44 ? 126 THR A CB 1 ATOM 969 O OG1 . THR A 1 126 ? 15.502 32.522 21.376 1.00 25.49 ? 126 THR A OG1 1 ATOM 970 C CG2 . THR A 1 126 ? 16.343 31.284 23.257 1.00 23.92 ? 126 THR A CG2 1 ATOM 971 N N . VAL A 1 127 ? 13.877 28.913 23.776 1.00 26.63 ? 127 VAL A N 1 ATOM 972 C CA . VAL A 1 127 ? 13.316 28.353 24.972 1.00 29.26 ? 127 VAL A CA 1 ATOM 973 C C . VAL A 1 127 ? 14.355 28.280 26.084 1.00 31.91 ? 127 VAL A C 1 ATOM 974 O O . VAL A 1 127 ? 15.300 27.475 26.022 1.00 31.92 ? 127 VAL A O 1 ATOM 975 C CB . VAL A 1 127 ? 12.760 26.956 24.748 1.00 28.30 ? 127 VAL A CB 1 ATOM 976 C CG1 . VAL A 1 127 ? 11.948 26.528 25.993 1.00 28.15 ? 127 VAL A CG1 1 ATOM 977 C CG2 . VAL A 1 127 ? 11.899 26.935 23.480 1.00 28.15 ? 127 VAL A CG2 1 ATOM 978 N N . SER A 1 128 ? 14.184 29.091 27.103 1.00 34.64 ? 128 SER A N 1 ATOM 979 C CA . SER A 1 128 ? 15.146 28.998 28.150 1.00 38.25 ? 128 SER A CA 1 ATOM 980 C C . SER A 1 128 ? 14.593 28.222 29.364 1.00 40.25 ? 128 SER A C 1 ATOM 981 O O . SER A 1 128 ? 13.503 27.663 29.320 1.00 40.46 ? 128 SER A O 1 ATOM 982 C CB . SER A 1 128 ? 15.657 30.411 28.410 1.00 38.26 ? 128 SER A CB 1 ATOM 983 O OG . SER A 1 128 ? 14.632 31.166 28.998 1.00 40.41 ? 128 SER A OG 1 ATOM 984 N N . SER A 1 129 ? 15.393 28.107 30.412 1.00 42.89 ? 129 SER A N 1 ATOM 985 C CA . SER A 1 129 ? 14.984 27.384 31.619 1.00 44.92 ? 129 SER A CA 1 ATOM 986 C C . SER A 1 129 ? 15.660 28.212 32.688 1.00 45.67 ? 129 SER A C 1 ATOM 987 O O . SER A 1 129 ? 16.827 28.567 32.439 1.00 46.63 ? 129 SER A O 1 ATOM 988 C CB . SER A 1 129 ? 15.540 25.943 31.584 1.00 45.21 ? 129 SER A CB 1 ATOM 989 O OG . SER A 1 129 ? 16.855 25.910 31.037 1.00 47.36 ? 129 SER A OG 1 ATOM 990 O OXT . SER A 1 129 ? 15.024 28.539 33.705 1.00 46.89 ? 129 SER A OXT 1 ATOM 991 N N . GLN B 1 1 ? 4.545 61.031 -5.961 1.00 34.90 ? 1 GLN B N 1 ATOM 992 C CA . GLN B 1 1 ? 3.084 60.947 -5.752 1.00 33.29 ? 1 GLN B CA 1 ATOM 993 C C . GLN B 1 1 ? 2.560 61.300 -4.365 1.00 32.19 ? 1 GLN B C 1 ATOM 994 O O . GLN B 1 1 ? 1.432 61.810 -4.265 1.00 32.66 ? 1 GLN B O 1 ATOM 995 C CB . GLN B 1 1 ? 2.601 59.583 -6.196 1.00 34.14 ? 1 GLN B CB 1 ATOM 996 C CG . GLN B 1 1 ? 2.678 59.504 -7.696 1.00 36.34 ? 1 GLN B CG 1 ATOM 997 C CD . GLN B 1 1 ? 1.991 58.295 -8.232 1.00 38.34 ? 1 GLN B CD 1 ATOM 998 O OE1 . GLN B 1 1 ? 1.781 58.168 -9.451 1.00 41.26 ? 1 GLN B OE1 1 ATOM 999 N NE2 . GLN B 1 1 ? 1.629 57.374 -7.337 1.00 40.20 ? 1 GLN B NE2 1 ATOM 1000 N N . VAL B 1 2 ? 3.334 61.050 -3.301 1.00 29.63 ? 2 VAL B N 1 ATOM 1001 C CA . VAL B 1 2 ? 2.897 61.435 -1.951 1.00 27.60 ? 2 VAL B CA 1 ATOM 1002 C C . VAL B 1 2 ? 4.064 61.862 -1.110 1.00 26.32 ? 2 VAL B C 1 ATOM 1003 O O . VAL B 1 2 ? 5.138 61.291 -1.236 1.00 25.04 ? 2 VAL B O 1 ATOM 1004 C CB . VAL B 1 2 ? 2.307 60.288 -1.109 1.00 28.48 ? 2 VAL B CB 1 ATOM 1005 C CG1 . VAL B 1 2 ? 1.041 60.757 -0.377 1.00 27.81 ? 2 VAL B CG1 1 ATOM 1006 C CG2 . VAL B 1 2 ? 2.094 59.111 -1.940 1.00 30.90 ? 2 VAL B CG2 1 ATOM 1007 N N . GLN B 1 3 ? 3.841 62.820 -0.217 1.00 24.33 ? 3 GLN B N 1 ATOM 1008 C CA . GLN B 1 3 ? 4.892 63.254 0.703 1.00 24.67 ? 3 GLN B CA 1 ATOM 1009 C C . GLN B 1 3 ? 4.420 62.816 2.067 1.00 23.21 ? 3 GLN B C 1 ATOM 1010 O O . GLN B 1 3 ? 3.233 62.970 2.408 1.00 22.69 ? 3 GLN B O 1 ATOM 1011 C CB . GLN B 1 3 ? 5.096 64.781 0.711 1.00 26.86 ? 3 GLN B CB 1 ATOM 1012 C CG . GLN B 1 3 ? 5.437 65.403 -0.631 1.00 31.74 ? 3 GLN B CG 1 ATOM 1013 C CD . GLN B 1 3 ? 6.068 66.803 -0.501 1.00 33.76 ? 3 GLN B CD 1 ATOM 1014 O OE1 . GLN B 1 3 ? 5.976 67.622 -1.409 1.00 35.05 ? 3 GLN B OE1 1 ATOM 1015 N NE2 . GLN B 1 3 ? 6.729 67.057 0.625 1.00 35.50 ? 3 GLN B NE2 1 ATOM 1016 N N . LEU B 1 4 ? 5.347 62.279 2.850 1.00 21.25 ? 4 LEU B N 1 ATOM 1017 C CA . LEU B 1 4 ? 5.032 61.775 4.172 1.00 20.45 ? 4 LEU B CA 1 ATOM 1018 C C . LEU B 1 4 ? 5.851 62.521 5.200 1.00 21.32 ? 4 LEU B C 1 ATOM 1019 O O . LEU B 1 4 ? 7.007 62.842 4.945 1.00 20.34 ? 4 LEU B O 1 ATOM 1020 C CB . LEU B 1 4 ? 5.366 60.286 4.244 1.00 18.74 ? 4 LEU B CB 1 ATOM 1021 C CG . LEU B 1 4 ? 4.685 59.376 3.225 1.00 18.50 ? 4 LEU B CG 1 ATOM 1022 C CD1 . LEU B 1 4 ? 5.271 57.985 3.386 1.00 18.64 ? 4 LEU B CD1 1 ATOM 1023 C CD2 . LEU B 1 4 ? 3.152 59.355 3.456 1.00 18.30 ? 4 LEU B CD2 1 ATOM 1024 N N . GLN B 1 5 ? 5.247 62.776 6.352 1.00 21.90 ? 5 GLN B N 1 ATOM 1025 C CA . GLN B 1 5 ? 5.905 63.478 7.434 1.00 23.54 ? 5 GLN B CA 1 ATOM 1026 C C . GLN B 1 5 ? 5.480 62.864 8.772 1.00 22.94 ? 5 GLN B C 1 ATOM 1027 O O . GLN B 1 5 ? 4.285 62.796 9.093 1.00 21.89 ? 5 GLN B O 1 ATOM 1028 C CB . GLN B 1 5 ? 5.511 64.947 7.386 1.00 27.40 ? 5 GLN B CB 1 ATOM 1029 C CG . GLN B 1 5 ? 6.182 65.768 8.455 1.00 32.71 ? 5 GLN B CG 1 ATOM 1030 C CD . GLN B 1 5 ? 7.687 65.816 8.239 1.00 36.27 ? 5 GLN B CD 1 ATOM 1031 O OE1 . GLN B 1 5 ? 8.156 66.059 7.111 1.00 38.14 ? 5 GLN B OE1 1 ATOM 1032 N NE2 . GLN B 1 5 ? 8.458 65.588 9.312 1.00 37.36 ? 5 GLN B NE2 1 ATOM 1033 N N . GLU B 1 6 ? 6.451 62.388 9.540 1.00 21.24 ? 6 GLU B N 1 ATOM 1034 C CA . GLU B 1 6 ? 6.142 61.796 10.829 1.00 20.57 ? 6 GLU B CA 1 ATOM 1035 C C . GLU B 1 6 ? 6.148 62.856 11.922 1.00 20.15 ? 6 GLU B C 1 ATOM 1036 O O . GLU B 1 6 ? 6.812 63.869 11.794 1.00 21.34 ? 6 GLU B O 1 ATOM 1037 C CB . GLU B 1 6 ? 7.166 60.718 11.175 1.00 20.06 ? 6 GLU B CB 1 ATOM 1038 C CG . GLU B 1 6 ? 7.347 59.660 10.134 1.00 19.31 ? 6 GLU B CG 1 ATOM 1039 C CD . GLU B 1 6 ? 8.369 60.046 9.086 1.00 19.17 ? 6 GLU B CD 1 ATOM 1040 O OE1 . GLU B 1 6 ? 8.726 61.242 9.008 1.00 18.35 ? 6 GLU B OE1 1 ATOM 1041 O OE2 . GLU B 1 6 ? 8.805 59.146 8.323 1.00 19.51 ? 6 GLU B OE2 1 ATOM 1042 N N . SER B 1 7 ? 5.417 62.634 12.995 1.00 20.10 ? 7 SER B N 1 ATOM 1043 C CA . SER B 1 7 ? 5.417 63.572 14.101 1.00 20.83 ? 7 SER B CA 1 ATOM 1044 C C . SER B 1 7 ? 5.004 62.812 15.335 1.00 20.56 ? 7 SER B C 1 ATOM 1045 O O . SER B 1 7 ? 4.464 61.717 15.236 1.00 19.53 ? 7 SER B O 1 ATOM 1046 C CB . SER B 1 7 ? 4.458 64.753 13.867 1.00 23.39 ? 7 SER B CB 1 ATOM 1047 O OG . SER B 1 7 ? 3.121 64.317 13.710 1.00 26.03 ? 7 SER B OG 1 ATOM 1048 N N . GLY B 1 8 ? 5.296 63.393 16.498 1.00 21.63 ? 8 GLY B N 1 ATOM 1049 C CA . GLY B 1 8 ? 4.984 62.768 17.769 1.00 22.69 ? 8 GLY B CA 1 ATOM 1050 C C . GLY B 1 8 ? 6.232 62.260 18.468 1.00 24.24 ? 8 GLY B C 1 ATOM 1051 O O . GLY B 1 8 ? 6.164 61.741 19.588 1.00 24.14 ? 8 GLY B O 1 ATOM 1052 N N . GLY B 1 9 ? 7.386 62.392 17.824 1.00 24.96 ? 9 GLY B N 1 ATOM 1053 C CA . GLY B 1 9 ? 8.597 61.912 18.474 1.00 26.97 ? 9 GLY B CA 1 ATOM 1054 C C . GLY B 1 9 ? 8.929 62.741 19.703 1.00 27.99 ? 9 GLY B C 1 ATOM 1055 O O . GLY B 1 9 ? 8.417 63.843 19.864 1.00 28.81 ? 9 GLY B O 1 ATOM 1056 N N . GLY B 1 10 ? 9.757 62.201 20.591 1.00 28.69 ? 10 GLY B N 1 ATOM 1057 C CA . GLY B 1 10 ? 10.160 62.940 21.782 1.00 28.91 ? 10 GLY B CA 1 ATOM 1058 C C . GLY B 1 10 ? 10.778 62.065 22.859 1.00 28.98 ? 10 GLY B C 1 ATOM 1059 O O . GLY B 1 10 ? 10.963 60.864 22.671 1.00 28.86 ? 10 GLY B O 1 ATOM 1060 N N . LEU B 1 11 ? 11.076 62.658 24.010 1.00 29.47 ? 11 LEU B N 1 ATOM 1061 C CA . LEU B 1 11 ? 11.656 61.911 25.110 1.00 30.02 ? 11 LEU B CA 1 ATOM 1062 C C . LEU B 1 11 ? 10.597 61.368 26.085 1.00 29.96 ? 11 LEU B C 1 ATOM 1063 O O . LEU B 1 11 ? 9.780 62.109 26.604 1.00 30.50 ? 11 LEU B O 1 ATOM 1064 C CB . LEU B 1 11 ? 12.658 62.803 25.861 1.00 31.35 ? 11 LEU B CB 1 ATOM 1065 C CG . LEU B 1 11 ? 13.430 62.180 27.044 1.00 32.58 ? 11 LEU B CG 1 ATOM 1066 C CD1 . LEU B 1 11 ? 14.473 61.188 26.525 1.00 33.02 ? 11 LEU B CD1 1 ATOM 1067 C CD2 . LEU B 1 11 ? 14.109 63.286 27.879 1.00 33.48 ? 11 LEU B CD2 1 ATOM 1068 N N . VAL B 1 12 ? 10.605 60.067 26.335 1.00 29.71 ? 12 VAL B N 1 ATOM 1069 C CA . VAL B 1 12 ? 9.667 59.476 27.281 1.00 29.37 ? 12 VAL B CA 1 ATOM 1070 C C . VAL B 1 12 ? 10.459 58.559 28.191 1.00 29.14 ? 12 VAL B C 1 ATOM 1071 O O . VAL B 1 12 ? 11.621 58.266 27.934 1.00 27.49 ? 12 VAL B O 1 ATOM 1072 C CB . VAL B 1 12 ? 8.579 58.621 26.597 1.00 30.37 ? 12 VAL B CB 1 ATOM 1073 C CG1 . VAL B 1 12 ? 7.716 59.487 25.686 1.00 30.12 ? 12 VAL B CG1 1 ATOM 1074 C CG2 . VAL B 1 12 ? 9.234 57.494 25.827 1.00 30.46 ? 12 VAL B CG2 1 ATOM 1075 N N . GLN B 1 13 ? 9.833 58.123 29.272 1.00 29.18 ? 13 GLN B N 1 ATOM 1076 C CA . GLN B 1 13 ? 10.491 57.229 30.185 1.00 30.77 ? 13 GLN B CA 1 ATOM 1077 C C . GLN B 1 13 ? 10.080 55.841 29.819 1.00 30.47 ? 13 GLN B C 1 ATOM 1078 O O . GLN B 1 13 ? 9.055 55.640 29.154 1.00 30.96 ? 13 GLN B O 1 ATOM 1079 C CB . GLN B 1 13 ? 10.068 57.500 31.620 1.00 33.46 ? 13 GLN B CB 1 ATOM 1080 C CG . GLN B 1 13 ? 10.820 56.658 32.645 1.00 37.99 ? 13 GLN B CG 1 ATOM 1081 C CD . GLN B 1 13 ? 10.323 56.937 34.065 1.00 42.05 ? 13 GLN B CD 1 ATOM 1082 O OE1 . GLN B 1 13 ? 10.014 58.105 34.414 1.00 43.15 ? 13 GLN B OE1 1 ATOM 1083 N NE2 . GLN B 1 13 ? 10.230 55.876 34.893 1.00 42.65 ? 13 GLN B NE2 1 ATOM 1084 N N . ALA B 1 14 ? 10.886 54.875 30.223 1.00 29.57 ? 14 ALA B N 1 ATOM 1085 C CA . ALA B 1 14 ? 10.563 53.491 29.957 1.00 29.32 ? 14 ALA B CA 1 ATOM 1086 C C . ALA B 1 14 ? 9.227 53.239 30.631 1.00 29.25 ? 14 ALA B C 1 ATOM 1087 O O . ALA B 1 14 ? 8.998 53.707 31.756 1.00 29.49 ? 14 ALA B O 1 ATOM 1088 C CB . ALA B 1 14 ? 11.616 52.586 30.548 1.00 29.28 ? 14 ALA B CB 1 ATOM 1089 N N . GLY B 1 15 ? 8.356 52.493 29.954 1.00 28.70 ? 15 GLY B N 1 ATOM 1090 C CA . GLY B 1 15 ? 7.046 52.204 30.505 1.00 27.33 ? 15 GLY B CA 1 ATOM 1091 C C . GLY B 1 15 ? 5.927 53.061 29.914 1.00 25.93 ? 15 GLY B C 1 ATOM 1092 O O . GLY B 1 15 ? 4.798 52.591 29.775 1.00 25.64 ? 15 GLY B O 1 ATOM 1093 N N . ASP B 1 16 ? 6.244 54.298 29.556 1.00 25.08 ? 16 ASP B N 1 ATOM 1094 C CA . ASP B 1 16 ? 5.267 55.203 28.965 1.00 24.68 ? 16 ASP B CA 1 ATOM 1095 C C . ASP B 1 16 ? 4.858 54.716 27.574 1.00 23.31 ? 16 ASP B C 1 ATOM 1096 O O . ASP B 1 16 ? 5.407 53.750 27.051 1.00 23.56 ? 16 ASP B O 1 ATOM 1097 C CB . ASP B 1 16 ? 5.828 56.617 28.828 1.00 25.47 ? 16 ASP B CB 1 ATOM 1098 C CG . ASP B 1 16 ? 6.025 57.311 30.161 1.00 28.60 ? 16 ASP B CG 1 ATOM 1099 O OD1 . ASP B 1 16 ? 5.405 56.892 31.174 1.00 28.40 ? 16 ASP B OD1 1 ATOM 1100 O OD2 . ASP B 1 16 ? 6.792 58.306 30.170 1.00 29.34 ? 16 ASP B OD2 1 ATOM 1101 N N . SER B 1 17 ? 3.892 55.411 26.993 1.00 21.38 ? 17 SER B N 1 ATOM 1102 C CA . SER B 1 17 ? 3.372 55.113 25.662 1.00 20.42 ? 17 SER B CA 1 ATOM 1103 C C . SER B 1 17 ? 3.538 56.372 24.855 1.00 20.15 ? 17 SER B C 1 ATOM 1104 O O . SER B 1 17 ? 3.622 57.456 25.410 1.00 19.97 ? 17 SER B O 1 ATOM 1105 C CB . SER B 1 17 ? 1.882 54.750 25.743 1.00 19.16 ? 17 SER B CB 1 ATOM 1106 O OG . SER B 1 17 ? 1.730 53.466 26.296 1.00 18.28 ? 17 SER B OG 1 ATOM 1107 N N . LEU B 1 18 ? 3.592 56.236 23.539 1.00 20.74 ? 18 LEU B N 1 ATOM 1108 C CA . LEU B 1 18 ? 3.742 57.394 22.692 1.00 20.23 ? 18 LEU B CA 1 ATOM 1109 C C . LEU B 1 18 ? 2.949 57.102 21.411 1.00 20.46 ? 18 LEU B C 1 ATOM 1110 O O . LEU B 1 18 ? 2.849 55.962 20.993 1.00 20.57 ? 18 LEU B O 1 ATOM 1111 C CB . LEU B 1 18 ? 5.216 57.582 22.397 1.00 23.29 ? 18 LEU B CB 1 ATOM 1112 C CG . LEU B 1 18 ? 5.693 58.930 21.880 1.00 26.25 ? 18 LEU B CG 1 ATOM 1113 C CD1 . LEU B 1 18 ? 5.121 60.067 22.731 1.00 26.28 ? 18 LEU B CD1 1 ATOM 1114 C CD2 . LEU B 1 18 ? 7.217 58.931 21.938 1.00 27.50 ? 18 LEU B CD2 1 ATOM 1115 N N . LYS B 1 19 ? 2.396 58.124 20.782 1.00 19.21 ? 19 LYS B N 1 ATOM 1116 C CA . LYS B 1 19 ? 1.606 57.904 19.575 1.00 19.47 ? 19 LYS B CA 1 ATOM 1117 C C . LYS B 1 19 ? 2.221 58.638 18.428 1.00 17.61 ? 19 LYS B C 1 ATOM 1118 O O . LYS B 1 19 ? 2.282 59.841 18.478 1.00 17.55 ? 19 LYS B O 1 ATOM 1119 C CB . LYS B 1 19 ? 0.187 58.439 19.782 1.00 20.37 ? 19 LYS B CB 1 ATOM 1120 C CG . LYS B 1 19 ? -0.742 58.204 18.586 1.00 22.91 ? 19 LYS B CG 1 ATOM 1121 C CD . LYS B 1 19 ? -2.197 58.586 18.979 1.00 26.32 ? 19 LYS B CD 1 ATOM 1122 C CE . LYS B 1 19 ? -3.259 57.744 18.269 1.00 27.97 ? 19 LYS B CE 1 ATOM 1123 N NZ . LYS B 1 19 ? -4.611 58.157 18.785 1.00 29.48 ? 19 LYS B NZ 1 ATOM 1124 N N . LEU B 1 20 ? 2.669 57.942 17.390 1.00 16.78 ? 20 LEU B N 1 ATOM 1125 C CA . LEU B 1 20 ? 3.254 58.649 16.249 1.00 17.15 ? 20 LEU B CA 1 ATOM 1126 C C . LEU B 1 20 ? 2.239 58.757 15.126 1.00 16.85 ? 20 LEU B C 1 ATOM 1127 O O . LEU B 1 20 ? 1.338 57.936 15.004 1.00 16.27 ? 20 LEU B O 1 ATOM 1128 C CB . LEU B 1 20 ? 4.507 57.932 15.678 1.00 16.40 ? 20 LEU B CB 1 ATOM 1129 C CG . LEU B 1 20 ? 5.627 57.610 16.651 1.00 18.15 ? 20 LEU B CG 1 ATOM 1130 C CD1 . LEU B 1 20 ? 6.799 56.955 15.899 1.00 18.85 ? 20 LEU B CD1 1 ATOM 1131 C CD2 . LEU B 1 20 ? 6.065 58.893 17.366 1.00 17.89 ? 20 LEU B CD2 1 ATOM 1132 N N . SER B 1 21 ? 2.412 59.793 14.316 1.00 17.30 ? 21 SER B N 1 ATOM 1133 C CA . SER B 1 21 ? 1.557 60.027 13.163 1.00 18.60 ? 21 SER B CA 1 ATOM 1134 C C . SER B 1 21 ? 2.388 60.133 11.919 1.00 18.04 ? 21 SER B C 1 ATOM 1135 O O . SER B 1 21 ? 3.449 60.747 11.911 1.00 18.23 ? 21 SER B O 1 ATOM 1136 C CB . SER B 1 21 ? 0.785 61.346 13.273 1.00 18.49 ? 21 SER B CB 1 ATOM 1137 O OG . SER B 1 21 ? 0.000 61.346 14.433 1.00 22.78 ? 21 SER B OG 1 ATOM 1138 N N . CYS B 1 22 ? 1.865 59.543 10.866 1.00 16.38 ? 22 CYS B N 1 ATOM 1139 C CA . CYS B 1 22 ? 2.488 59.612 9.577 1.00 16.90 ? 22 CYS B CA 1 ATOM 1140 C C . CYS B 1 22 ? 1.414 60.332 8.775 1.00 17.52 ? 22 CYS B C 1 ATOM 1141 O O . CYS B 1 22 ? 0.390 59.724 8.457 1.00 17.03 ? 22 CYS B O 1 ATOM 1142 C CB . CYS B 1 22 ? 2.691 58.225 9.000 1.00 16.23 ? 22 CYS B CB 1 ATOM 1143 S SG . CYS B 1 22 ? 3.133 58.235 7.259 1.00 18.26 ? 22 CYS B SG 1 ATOM 1144 N N . GLU B 1 23 ? 1.617 61.616 8.500 1.00 17.45 ? 23 GLU B N 1 ATOM 1145 C CA . GLU B 1 23 ? 0.659 62.404 7.723 1.00 20.95 ? 23 GLU B CA 1 ATOM 1146 C C . GLU B 1 23 ? 1.153 62.602 6.279 1.00 21.21 ? 23 GLU B C 1 ATOM 1147 O O . GLU B 1 23 ? 2.323 62.964 6.055 1.00 20.79 ? 23 GLU B O 1 ATOM 1148 C CB . GLU B 1 23 ? 0.450 63.785 8.344 1.00 23.21 ? 23 GLU B CB 1 ATOM 1149 C CG . GLU B 1 23 ? 0.176 63.785 9.825 1.00 27.97 ? 23 GLU B CG 1 ATOM 1150 C CD . GLU B 1 23 ? 0.323 65.177 10.455 1.00 30.39 ? 23 GLU B CD 1 ATOM 1151 O OE1 . GLU B 1 23 ? 1.417 65.804 10.414 1.00 31.63 ? 23 GLU B OE1 1 ATOM 1152 O OE2 . GLU B 1 23 ? -0.678 65.656 11.001 1.00 33.40 ? 23 GLU B OE2 1 ATOM 1153 N N . ALA B 1 24 ? 0.252 62.377 5.316 1.00 20.17 ? 24 ALA B N 1 ATOM 1154 C CA . ALA B 1 24 ? 0.532 62.537 3.892 1.00 18.88 ? 24 ALA B CA 1 ATOM 1155 C C . ALA B 1 24 ? 0.040 63.884 3.381 1.00 20.23 ? 24 ALA B C 1 ATOM 1156 O O . ALA B 1 24 ? -0.867 64.522 3.961 1.00 19.30 ? 24 ALA B O 1 ATOM 1157 C CB . ALA B 1 24 ? -0.120 61.439 3.101 1.00 18.64 ? 24 ALA B CB 1 ATOM 1158 N N . SER B 1 25 ? 0.656 64.296 2.278 1.00 20.35 ? 25 SER B N 1 ATOM 1159 C CA . SER B 1 25 ? 0.373 65.554 1.604 1.00 21.55 ? 25 SER B CA 1 ATOM 1160 C C . SER B 1 25 ? 0.561 65.224 0.142 1.00 20.08 ? 25 SER B C 1 ATOM 1161 O O . SER B 1 25 ? 1.383 64.380 -0.182 1.00 20.26 ? 25 SER B O 1 ATOM 1162 C CB . SER B 1 25 ? 1.413 66.623 1.979 1.00 23.75 ? 25 SER B CB 1 ATOM 1163 O OG . SER B 1 25 ? 1.151 67.166 3.250 1.00 29.42 ? 25 SER B OG 1 ATOM 1164 N N . GLY B 1 26 ? -0.182 65.898 -0.729 1.00 19.88 ? 26 GLY B N 1 ATOM 1165 C CA . GLY B 1 26 ? -0.041 65.677 -2.164 1.00 18.74 ? 26 GLY B CA 1 ATOM 1166 C C . GLY B 1 26 ? -0.940 64.623 -2.758 1.00 18.30 ? 26 GLY B C 1 ATOM 1167 O O . GLY B 1 26 ? -1.164 64.589 -3.954 1.00 18.65 ? 26 GLY B O 1 ATOM 1168 N N . ASP B 1 27 ? -1.430 63.734 -1.931 1.00 16.88 ? 27 ASP B N 1 ATOM 1169 C CA . ASP B 1 27 ? -2.294 62.679 -2.403 1.00 17.22 ? 27 ASP B CA 1 ATOM 1170 C C . ASP B 1 27 ? -2.917 62.117 -1.159 1.00 16.89 ? 27 ASP B C 1 ATOM 1171 O O . ASP B 1 27 ? -2.530 62.453 -0.019 1.00 17.32 ? 27 ASP B O 1 ATOM 1172 C CB . ASP B 1 27 ? -1.475 61.580 -3.099 1.00 17.34 ? 27 ASP B CB 1 ATOM 1173 C CG . ASP B 1 27 ? -2.321 60.670 -3.977 1.00 19.36 ? 27 ASP B CG 1 ATOM 1174 O OD1 . ASP B 1 27 ? -3.562 60.804 -3.969 1.00 20.38 ? 27 ASP B OD1 1 ATOM 1175 O OD2 . ASP B 1 27 ? -1.752 59.794 -4.672 1.00 21.49 ? 27 ASP B OD2 1 ATOM 1176 N N . SER B 1 28 ? -3.869 61.225 -1.373 1.00 18.45 ? 28 SER B N 1 ATOM 1177 C CA . SER B 1 28 ? -4.519 60.561 -0.252 1.00 17.84 ? 28 SER B CA 1 ATOM 1178 C C . SER B 1 28 ? -3.714 59.336 0.091 1.00 17.09 ? 28 SER B C 1 ATOM 1179 O O . SER B 1 28 ? -3.314 58.571 -0.791 1.00 15.39 ? 28 SER B O 1 ATOM 1180 C CB . SER B 1 28 ? -5.911 60.067 -0.616 1.00 18.53 ? 28 SER B CB 1 ATOM 1181 O OG . SER B 1 28 ? -6.357 59.138 0.366 1.00 19.26 ? 28 SER B OG 1 ATOM 1182 N N . ILE B 1 29 ? -3.573 59.123 1.387 1.00 17.08 ? 29 ILE B N 1 ATOM 1183 C CA . ILE B 1 29 ? -2.889 57.967 1.910 1.00 17.99 ? 29 ILE B CA 1 ATOM 1184 C C . ILE B 1 29 ? -3.806 56.761 1.779 1.00 18.70 ? 29 ILE B C 1 ATOM 1185 O O . ILE B 1 29 ? -3.388 55.609 1.987 1.00 19.18 ? 29 ILE B O 1 ATOM 1186 C CB . ILE B 1 29 ? -2.550 58.251 3.378 1.00 20.14 ? 29 ILE B CB 1 ATOM 1187 C CG1 . ILE B 1 29 ? -1.358 57.434 3.810 1.00 19.68 ? 29 ILE B CG1 1 ATOM 1188 C CG2 . ILE B 1 29 ? -3.760 57.977 4.286 1.00 19.28 ? 29 ILE B CG2 1 ATOM 1189 C CD1 . ILE B 1 29 ? -0.705 58.065 4.983 1.00 21.18 ? 29 ILE B CD1 1 ATOM 1190 N N . GLY B 1 30 ? -5.066 57.003 1.382 1.00 19.30 ? 30 GLY B N 1 ATOM 1191 C CA . GLY B 1 30 ? -6.015 55.902 1.260 1.00 17.60 ? 30 GLY B CA 1 ATOM 1192 C C . GLY B 1 30 ? -5.739 54.814 0.230 1.00 18.33 ? 30 GLY B C 1 ATOM 1193 O O . GLY B 1 30 ? -6.272 53.703 0.342 1.00 18.15 ? 30 GLY B O 1 ATOM 1194 N N . THR B 1 31 ? -4.939 55.094 -0.801 1.00 18.13 ? 31 THR B N 1 ATOM 1195 C CA . THR B 1 31 ? -4.641 54.053 -1.791 1.00 19.32 ? 31 THR B CA 1 ATOM 1196 C C . THR B 1 31 ? -3.205 53.480 -1.671 1.00 18.18 ? 31 THR B C 1 ATOM 1197 O O . THR B 1 31 ? -2.708 52.798 -2.570 1.00 17.64 ? 31 THR B O 1 ATOM 1198 C CB . THR B 1 31 ? -4.840 54.576 -3.243 1.00 19.62 ? 31 THR B CB 1 ATOM 1199 O OG1 . THR B 1 31 ? -4.251 55.876 -3.352 1.00 22.53 ? 31 THR B OG1 1 ATOM 1200 C CG2 . THR B 1 31 ? -6.347 54.663 -3.584 1.00 22.77 ? 31 THR B CG2 1 ATOM 1201 N N . TYR B 1 32 ? -2.567 53.735 -0.549 1.00 17.64 ? 32 TYR B N 1 ATOM 1202 C CA . TYR B 1 32 ? -1.198 53.232 -0.339 1.00 17.36 ? 32 TYR B CA 1 ATOM 1203 C C . TYR B 1 32 ? -1.099 52.296 0.836 1.00 16.47 ? 32 TYR B C 1 ATOM 1204 O O . TYR B 1 32 ? -1.803 52.480 1.815 1.00 17.36 ? 32 TYR B O 1 ATOM 1205 C CB . TYR B 1 32 ? -0.256 54.381 -0.027 1.00 17.50 ? 32 TYR B CB 1 ATOM 1206 C CG . TYR B 1 32 ? -0.039 55.357 -1.152 1.00 17.62 ? 32 TYR B CG 1 ATOM 1207 C CD1 . TYR B 1 32 ? 0.944 55.132 -2.116 1.00 18.13 ? 32 TYR B CD1 1 ATOM 1208 C CD2 . TYR B 1 32 ? -0.795 56.511 -1.237 1.00 18.02 ? 32 TYR B CD2 1 ATOM 1209 C CE1 . TYR B 1 32 ? 1.172 56.038 -3.139 1.00 19.30 ? 32 TYR B CE1 1 ATOM 1210 C CE2 . TYR B 1 32 ? -0.574 57.429 -2.247 1.00 19.13 ? 32 TYR B CE2 1 ATOM 1211 C CZ . TYR B 1 32 ? 0.402 57.190 -3.192 1.00 19.84 ? 32 TYR B CZ 1 ATOM 1212 O OH . TYR B 1 32 ? 0.603 58.127 -4.178 1.00 22.73 ? 32 TYR B OH 1 ATOM 1213 N N . VAL B 1 33 ? -0.225 51.300 0.736 1.00 16.64 ? 33 VAL B N 1 ATOM 1214 C CA . VAL B 1 33 ? 0.056 50.421 1.857 1.00 16.41 ? 33 VAL B CA 1 ATOM 1215 C C . VAL B 1 33 ? 1.115 51.257 2.630 1.00 16.42 ? 33 VAL B C 1 ATOM 1216 O O . VAL B 1 33 ? 2.022 51.814 2.033 1.00 15.76 ? 33 VAL B O 1 ATOM 1217 C CB . VAL B 1 33 ? 0.663 49.097 1.388 1.00 17.26 ? 33 VAL B CB 1 ATOM 1218 C CG1 . VAL B 1 33 ? 1.217 48.308 2.617 1.00 18.30 ? 33 VAL B CG1 1 ATOM 1219 C CG2 . VAL B 1 33 ? -0.406 48.263 0.658 1.00 17.58 ? 33 VAL B CG2 1 ATOM 1220 N N . ILE B 1 34 ? 0.966 51.383 3.942 1.00 16.31 ? 34 ILE B N 1 ATOM 1221 C CA . ILE B 1 34 ? 1.851 52.206 4.752 1.00 15.91 ? 34 ILE B CA 1 ATOM 1222 C C . ILE B 1 34 ? 2.641 51.296 5.668 1.00 16.26 ? 34 ILE B C 1 ATOM 1223 O O . ILE B 1 34 ? 2.078 50.392 6.263 1.00 16.65 ? 34 ILE B O 1 ATOM 1224 C CB . ILE B 1 34 ? 1.024 53.195 5.629 1.00 16.63 ? 34 ILE B CB 1 ATOM 1225 C CG1 . ILE B 1 34 ? 0.238 54.155 4.745 1.00 15.99 ? 34 ILE B CG1 1 ATOM 1226 C CG2 . ILE B 1 34 ? 1.947 53.996 6.577 1.00 15.49 ? 34 ILE B CG2 1 ATOM 1227 C CD1 . ILE B 1 34 ? 1.119 55.091 3.920 1.00 16.28 ? 34 ILE B CD1 1 ATOM 1228 N N . GLY B 1 35 ? 3.944 51.528 5.767 1.00 16.39 ? 35 GLY B N 1 ATOM 1229 C CA . GLY B 1 35 ? 4.762 50.709 6.637 1.00 14.55 ? 35 GLY B CA 1 ATOM 1230 C C . GLY B 1 35 ? 5.526 51.589 7.617 1.00 14.12 ? 35 GLY B C 1 ATOM 1231 O O . GLY B 1 35 ? 5.780 52.743 7.313 1.00 13.42 ? 35 GLY B O 1 ATOM 1232 N N . TRP B 1 36 ? 5.872 51.034 8.781 1.00 12.77 ? 36 TRP B N 1 ATOM 1233 C CA . TRP B 1 36 ? 6.623 51.732 9.809 1.00 13.17 ? 36 TRP B CA 1 ATOM 1234 C C . TRP B 1 36 ? 7.935 51.006 10.004 1.00 13.55 ? 36 TRP B C 1 ATOM 1235 O O . TRP B 1 36 ? 7.976 49.787 10.064 1.00 11.50 ? 36 TRP B O 1 ATOM 1236 C CB . TRP B 1 36 ? 5.898 51.732 11.153 1.00 13.56 ? 36 TRP B CB 1 ATOM 1237 C CG . TRP B 1 36 ? 4.800 52.728 11.223 1.00 12.03 ? 36 TRP B CG 1 ATOM 1238 C CD1 . TRP B 1 36 ? 3.470 52.507 10.987 1.00 13.27 ? 36 TRP B CD1 1 ATOM 1239 C CD2 . TRP B 1 36 ? 4.935 54.102 11.523 1.00 12.49 ? 36 TRP B CD2 1 ATOM 1240 N NE1 . TRP B 1 36 ? 2.767 53.679 11.130 1.00 11.44 ? 36 TRP B NE1 1 ATOM 1241 C CE2 . TRP B 1 36 ? 3.643 54.674 11.458 1.00 11.32 ? 36 TRP B CE2 1 ATOM 1242 C CE3 . TRP B 1 36 ? 6.028 54.919 11.845 1.00 12.57 ? 36 TRP B CE3 1 ATOM 1243 C CZ2 . TRP B 1 36 ? 3.413 56.016 11.699 1.00 11.67 ? 36 TRP B CZ2 1 ATOM 1244 C CZ3 . TRP B 1 36 ? 5.807 56.255 12.089 1.00 12.30 ? 36 TRP B CZ3 1 ATOM 1245 C CH2 . TRP B 1 36 ? 4.493 56.796 12.015 1.00 13.47 ? 36 TRP B CH2 1 ATOM 1246 N N . PHE B 1 37 ? 8.997 51.796 10.108 1.00 14.58 ? 37 PHE B N 1 ATOM 1247 C CA . PHE B 1 37 ? 10.354 51.298 10.271 1.00 15.55 ? 37 PHE B CA 1 ATOM 1248 C C . PHE B 1 37 ? 11.021 52.135 11.361 1.00 16.12 ? 37 PHE B C 1 ATOM 1249 O O . PHE B 1 37 ? 10.525 53.187 11.739 1.00 15.79 ? 37 PHE B O 1 ATOM 1250 C CB . PHE B 1 37 ? 11.178 51.515 8.974 1.00 16.59 ? 37 PHE B CB 1 ATOM 1251 C CG . PHE B 1 37 ? 10.664 50.757 7.778 1.00 17.23 ? 37 PHE B CG 1 ATOM 1252 C CD1 . PHE B 1 37 ? 9.511 51.167 7.118 1.00 18.22 ? 37 PHE B CD1 1 ATOM 1253 C CD2 . PHE B 1 37 ? 11.281 49.581 7.377 1.00 17.98 ? 37 PHE B CD2 1 ATOM 1254 C CE1 . PHE B 1 37 ? 8.989 50.417 6.076 1.00 18.38 ? 37 PHE B CE1 1 ATOM 1255 C CE2 . PHE B 1 37 ? 10.751 48.812 6.328 1.00 19.51 ? 37 PHE B CE2 1 ATOM 1256 C CZ . PHE B 1 37 ? 9.596 49.235 5.689 1.00 19.59 ? 37 PHE B CZ 1 ATOM 1257 N N . ARG B 1 38 ? 12.145 51.655 11.869 1.00 15.29 ? 38 ARG B N 1 ATOM 1258 C CA . ARG B 1 38 ? 12.902 52.454 12.823 1.00 16.83 ? 38 ARG B CA 1 ATOM 1259 C C . ARG B 1 38 ? 14.356 52.070 12.647 1.00 17.80 ? 38 ARG B C 1 ATOM 1260 O O . ARG B 1 38 ? 14.661 50.962 12.211 1.00 17.14 ? 38 ARG B O 1 ATOM 1261 C CB . ARG B 1 38 ? 12.492 52.205 14.267 1.00 14.70 ? 38 ARG B CB 1 ATOM 1262 C CG . ARG B 1 38 ? 12.969 50.925 14.816 1.00 14.48 ? 38 ARG B CG 1 ATOM 1263 C CD . ARG B 1 38 ? 12.471 50.805 16.240 1.00 14.78 ? 38 ARG B CD 1 ATOM 1264 N NE . ARG B 1 38 ? 12.840 49.515 16.773 1.00 15.08 ? 38 ARG B NE 1 ATOM 1265 C CZ . ARG B 1 38 ? 12.328 49.034 17.896 1.00 17.93 ? 38 ARG B CZ 1 ATOM 1266 N NH1 . ARG B 1 38 ? 11.420 49.746 18.570 1.00 17.32 ? 38 ARG B NH1 1 ATOM 1267 N NH2 . ARG B 1 38 ? 12.765 47.875 18.381 1.00 17.68 ? 38 ARG B NH2 1 ATOM 1268 N N . GLN B 1 39 ? 15.242 52.989 13.001 1.00 20.97 ? 39 GLN B N 1 ATOM 1269 C CA . GLN B 1 39 ? 16.669 52.726 12.875 1.00 24.43 ? 39 GLN B CA 1 ATOM 1270 C C . GLN B 1 39 ? 17.373 53.259 14.110 1.00 25.49 ? 39 GLN B C 1 ATOM 1271 O O . GLN B 1 39 ? 17.304 54.452 14.392 1.00 24.76 ? 39 GLN B O 1 ATOM 1272 C CB . GLN B 1 39 ? 17.213 53.400 11.619 1.00 24.39 ? 39 GLN B CB 1 ATOM 1273 C CG . GLN B 1 39 ? 18.706 53.257 11.425 1.00 26.83 ? 39 GLN B CG 1 ATOM 1274 C CD . GLN B 1 39 ? 19.155 53.794 10.086 1.00 27.73 ? 39 GLN B CD 1 ATOM 1275 O OE1 . GLN B 1 39 ? 18.867 54.945 9.747 1.00 28.64 ? 39 GLN B OE1 1 ATOM 1276 N NE2 . GLN B 1 39 ? 19.864 52.969 9.317 1.00 27.21 ? 39 GLN B NE2 1 ATOM 1277 N N . ALA B 1 40 ? 18.010 52.358 14.855 1.00 28.12 ? 40 ALA B N 1 ATOM 1278 C CA . ALA B 1 40 ? 18.749 52.738 16.058 1.00 31.24 ? 40 ALA B CA 1 ATOM 1279 C C . ALA B 1 40 ? 20.093 53.301 15.600 1.00 33.44 ? 40 ALA B C 1 ATOM 1280 O O . ALA B 1 40 ? 20.624 52.870 14.582 1.00 33.19 ? 40 ALA B O 1 ATOM 1281 C CB . ALA B 1 40 ? 18.957 51.531 16.955 1.00 30.83 ? 40 ALA B CB 1 ATOM 1282 N N . PRO B 1 41 ? 20.652 54.268 16.356 1.00 35.96 ? 41 PRO B N 1 ATOM 1283 C CA . PRO B 1 41 ? 21.923 54.949 16.099 1.00 37.66 ? 41 PRO B CA 1 ATOM 1284 C C . PRO B 1 41 ? 22.880 54.230 15.139 1.00 38.47 ? 41 PRO B C 1 ATOM 1285 O O . PRO B 1 41 ? 23.190 54.774 14.070 1.00 40.04 ? 41 PRO B O 1 ATOM 1286 C CB . PRO B 1 41 ? 22.488 55.118 17.507 1.00 38.02 ? 41 PRO B CB 1 ATOM 1287 C CG . PRO B 1 41 ? 21.284 55.535 18.252 1.00 37.94 ? 41 PRO B CG 1 ATOM 1288 C CD . PRO B 1 41 ? 20.222 54.527 17.746 1.00 37.51 ? 41 PRO B CD 1 ATOM 1289 N N . GLY B 1 42 ? 23.318 53.016 15.476 1.00 38.08 ? 42 GLY B N 1 ATOM 1290 C CA . GLY B 1 42 ? 24.239 52.338 14.581 1.00 39.05 ? 42 GLY B CA 1 ATOM 1291 C C . GLY B 1 42 ? 23.829 51.007 13.984 1.00 39.69 ? 42 GLY B C 1 ATOM 1292 O O . GLY B 1 42 ? 24.693 50.200 13.624 1.00 40.33 ? 42 GLY B O 1 ATOM 1293 N N . LYS B 1 43 ? 22.530 50.762 13.848 1.00 39.31 ? 43 LYS B N 1 ATOM 1294 C CA . LYS B 1 43 ? 22.079 49.493 13.301 1.00 38.10 ? 43 LYS B CA 1 ATOM 1295 C C . LYS B 1 43 ? 21.332 49.630 11.985 1.00 36.24 ? 43 LYS B C 1 ATOM 1296 O O . LYS B 1 43 ? 21.169 50.728 11.472 1.00 35.21 ? 43 LYS B O 1 ATOM 1297 C CB . LYS B 1 43 ? 21.208 48.784 14.337 1.00 39.82 ? 43 LYS B CB 1 ATOM 1298 C CG . LYS B 1 43 ? 21.972 48.494 15.635 1.00 42.78 ? 43 LYS B CG 1 ATOM 1299 C CD . LYS B 1 43 ? 21.092 47.814 16.677 1.00 44.94 ? 43 LYS B CD 1 ATOM 1300 C CE . LYS B 1 43 ? 19.887 48.705 17.031 1.00 47.14 ? 43 LYS B CE 1 ATOM 1301 N NZ . LYS B 1 43 ? 19.164 48.332 18.307 1.00 48.44 ? 43 LYS B NZ 1 ATOM 1302 N N . GLU B 1 44 ? 20.915 48.494 11.431 1.00 34.78 ? 44 GLU B N 1 ATOM 1303 C CA . GLU B 1 44 ? 20.148 48.467 10.192 1.00 33.68 ? 44 GLU B CA 1 ATOM 1304 C C . GLU B 1 44 ? 18.760 49.051 10.423 1.00 31.33 ? 44 GLU B C 1 ATOM 1305 O O . GLU B 1 44 ? 18.249 49.052 11.541 1.00 30.62 ? 44 GLU B O 1 ATOM 1306 C CB . GLU B 1 44 ? 19.990 47.031 9.664 1.00 35.41 ? 44 GLU B CB 1 ATOM 1307 C CG . GLU B 1 44 ? 20.246 45.941 10.678 1.00 39.78 ? 44 GLU B CG 1 ATOM 1308 C CD . GLU B 1 44 ? 20.294 44.552 10.034 1.00 42.62 ? 44 GLU B CD 1 ATOM 1309 O OE1 . GLU B 1 44 ? 20.197 44.418 8.773 1.00 43.86 ? 44 GLU B OE1 1 ATOM 1310 O OE2 . GLU B 1 44 ? 20.445 43.576 10.804 1.00 45.13 ? 44 GLU B OE2 1 ATOM 1311 N N . ARG B 1 45 ? 18.157 49.546 9.357 1.00 29.01 ? 45 ARG B N 1 ATOM 1312 C CA . ARG B 1 45 ? 16.804 50.091 9.418 1.00 26.88 ? 45 ARG B CA 1 ATOM 1313 C C . ARG B 1 45 ? 15.917 48.848 9.374 1.00 25.32 ? 45 ARG B C 1 ATOM 1314 O O . ARG B 1 45 ? 15.993 48.058 8.427 1.00 24.89 ? 45 ARG B O 1 ATOM 1315 C CB . ARG B 1 45 ? 16.579 50.951 8.205 1.00 27.68 ? 45 ARG B CB 1 ATOM 1316 C CG . ARG B 1 45 ? 15.264 51.616 8.094 1.00 28.75 ? 45 ARG B CG 1 ATOM 1317 C CD . ARG B 1 45 ? 15.283 52.250 6.719 1.00 30.96 ? 45 ARG B CD 1 ATOM 1318 N NE . ARG B 1 45 ? 15.016 53.660 6.797 1.00 33.44 ? 45 ARG B NE 1 ATOM 1319 C CZ . ARG B 1 45 ? 15.931 54.612 6.697 1.00 34.66 ? 45 ARG B CZ 1 ATOM 1320 N NH1 . ARG B 1 45 ? 17.220 54.326 6.494 1.00 35.96 ? 45 ARG B NH1 1 ATOM 1321 N NH2 . ARG B 1 45 ? 15.543 55.865 6.868 1.00 36.28 ? 45 ARG B NH2 1 ATOM 1322 N N . ILE B 1 46 ? 15.081 48.678 10.395 1.00 22.45 ? 46 ILE B N 1 ATOM 1323 C CA . ILE B 1 46 ? 14.251 47.496 10.473 1.00 20.83 ? 46 ILE B CA 1 ATOM 1324 C C . ILE B 1 46 ? 12.730 47.770 10.375 1.00 20.01 ? 46 ILE B C 1 ATOM 1325 O O . ILE B 1 46 ? 12.226 48.787 10.834 1.00 18.62 ? 46 ILE B O 1 ATOM 1326 C CB . ILE B 1 46 ? 14.515 46.727 11.777 1.00 21.36 ? 46 ILE B CB 1 ATOM 1327 C CG1 . ILE B 1 46 ? 13.990 47.533 12.939 1.00 21.25 ? 46 ILE B CG1 1 ATOM 1328 C CG2 . ILE B 1 46 ? 16.014 46.501 11.997 1.00 21.86 ? 46 ILE B CG2 1 ATOM 1329 C CD1 . ILE B 1 46 ? 13.707 46.673 14.131 1.00 23.12 ? 46 ILE B CD1 1 ATOM 1330 N N . TYR B 1 47 ? 12.031 46.808 9.792 1.00 19.87 ? 47 TYR B N 1 ATOM 1331 C CA . TYR B 1 47 ? 10.599 46.881 9.583 1.00 19.97 ? 47 TYR B CA 1 ATOM 1332 C C . TYR B 1 47 ? 9.865 46.652 10.883 1.00 18.18 ? 47 TYR B C 1 ATOM 1333 O O . TYR B 1 47 ? 10.266 45.824 11.712 1.00 16.37 ? 47 TYR B O 1 ATOM 1334 C CB . TYR B 1 47 ? 10.202 45.835 8.545 1.00 21.32 ? 47 TYR B CB 1 ATOM 1335 C CG . TYR B 1 47 ? 8.768 45.400 8.628 1.00 22.31 ? 47 TYR B CG 1 ATOM 1336 C CD1 . TYR B 1 47 ? 8.423 44.255 9.332 1.00 23.19 ? 47 TYR B CD1 1 ATOM 1337 C CD2 . TYR B 1 47 ? 7.765 46.111 7.969 1.00 23.35 ? 47 TYR B CD2 1 ATOM 1338 C CE1 . TYR B 1 47 ? 7.129 43.818 9.372 1.00 23.04 ? 47 TYR B CE1 1 ATOM 1339 C CE2 . TYR B 1 47 ? 6.452 45.685 8.003 1.00 23.20 ? 47 TYR B CE2 1 ATOM 1340 C CZ . TYR B 1 47 ? 6.146 44.556 8.693 1.00 23.45 ? 47 TYR B CZ 1 ATOM 1341 O OH . TYR B 1 47 ? 4.846 44.189 8.649 1.00 24.08 ? 47 TYR B OH 1 ATOM 1342 N N . LEU B 1 48 ? 8.793 47.408 11.073 1.00 16.52 ? 48 LEU B N 1 ATOM 1343 C CA . LEU B 1 48 ? 8.012 47.270 12.284 1.00 15.61 ? 48 LEU B CA 1 ATOM 1344 C C . LEU B 1 48 ? 6.585 46.801 12.037 1.00 15.70 ? 48 LEU B C 1 ATOM 1345 O O . LEU B 1 48 ? 6.120 45.872 12.682 1.00 13.93 ? 48 LEU B O 1 ATOM 1346 C CB . LEU B 1 48 ? 7.945 48.604 13.026 1.00 15.05 ? 48 LEU B CB 1 ATOM 1347 C CG . LEU B 1 48 ? 9.263 49.177 13.570 1.00 16.20 ? 48 LEU B CG 1 ATOM 1348 C CD1 . LEU B 1 48 ? 8.992 50.468 14.242 1.00 14.69 ? 48 LEU B CD1 1 ATOM 1349 C CD2 . LEU B 1 48 ? 9.882 48.185 14.526 1.00 13.96 ? 48 LEU B CD2 1 ATOM 1350 N N . ALA B 1 49 ? 5.901 47.459 11.111 1.00 15.16 ? 49 ALA B N 1 ATOM 1351 C CA . ALA B 1 49 ? 4.514 47.102 10.911 1.00 16.74 ? 49 ALA B CA 1 ATOM 1352 C C . ALA B 1 49 ? 3.995 47.622 9.614 1.00 17.37 ? 49 ALA B C 1 ATOM 1353 O O . ALA B 1 49 ? 4.536 48.554 9.028 1.00 18.17 ? 49 ALA B O 1 ATOM 1354 C CB . ALA B 1 49 ? 3.666 47.713 12.066 1.00 15.13 ? 49 ALA B CB 1 ATOM 1355 N N . THR B 1 50 ? 2.910 47.022 9.164 1.00 18.91 ? 50 THR B N 1 ATOM 1356 C CA . THR B 1 50 ? 2.268 47.523 7.971 1.00 19.53 ? 50 THR B CA 1 ATOM 1357 C C . THR B 1 50 ? 0.749 47.579 8.184 1.00 19.49 ? 50 THR B C 1 ATOM 1358 O O . THR B 1 50 ? 0.182 46.825 8.982 1.00 17.01 ? 50 THR B O 1 ATOM 1359 C CB . THR B 1 50 ? 2.603 46.687 6.720 1.00 21.73 ? 50 THR B CB 1 ATOM 1360 O OG1 . THR B 1 50 ? 1.413 46.507 5.941 1.00 26.17 ? 50 THR B OG1 1 ATOM 1361 C CG2 . THR B 1 50 ? 3.134 45.394 7.066 1.00 22.55 ? 50 THR B CG2 1 ATOM 1362 N N . ILE B 1 51 ? 0.125 48.563 7.545 1.00 19.58 ? 51 ILE B N 1 ATOM 1363 C CA . ILE B 1 51 ? -1.326 48.660 7.571 1.00 19.74 ? 51 ILE B CA 1 ATOM 1364 C C . ILE B 1 51 ? -1.786 48.766 6.110 1.00 19.41 ? 51 ILE B C 1 ATOM 1365 O O . ILE B 1 51 ? -1.383 49.674 5.375 1.00 20.65 ? 51 ILE B O 1 ATOM 1366 C CB . ILE B 1 51 ? -1.830 49.813 8.481 1.00 20.01 ? 51 ILE B CB 1 ATOM 1367 C CG1 . ILE B 1 51 ? -3.365 49.707 8.589 1.00 20.03 ? 51 ILE B CG1 1 ATOM 1368 C CG2 . ILE B 1 51 ? -1.312 51.173 8.016 1.00 18.64 ? 51 ILE B CG2 1 ATOM 1369 C CD1 . ILE B 1 51 ? -3.936 50.591 9.648 1.00 20.20 ? 51 ILE B CD1 1 ATOM 1370 N N . GLY B 1 52 ? -2.558 47.772 5.682 1.00 19.63 ? 52 GLY B N 1 ATOM 1371 C CA . GLY B 1 52 ? -3.033 47.705 4.317 1.00 20.04 ? 52 GLY B CA 1 ATOM 1372 C C . GLY B 1 52 ? -4.051 48.788 4.001 1.00 20.52 ? 52 GLY B C 1 ATOM 1373 O O . GLY B 1 52 ? -4.403 49.601 4.868 1.00 17.99 ? 52 GLY B O 1 ATOM 1374 N N . ARG B 1 53 ? -4.549 48.799 2.766 1.00 22.13 ? 53 ARG B N 1 ATOM 1375 C CA . ARG B 1 53 ? -5.514 49.824 2.396 1.00 24.81 ? 53 ARG B CA 1 ATOM 1376 C C . ARG B 1 53 ? -6.913 49.249 2.344 1.00 25.50 ? 53 ARG B C 1 ATOM 1377 O O . ARG B 1 53 ? -7.873 49.984 2.194 1.00 24.55 ? 53 ARG B O 1 ATOM 1378 C CB . ARG B 1 53 ? -5.164 50.433 1.042 1.00 27.39 ? 53 ARG B CB 1 ATOM 1379 C CG . ARG B 1 53 ? -5.005 49.405 -0.040 1.00 31.93 ? 53 ARG B CG 1 ATOM 1380 C CD . ARG B 1 53 ? -4.378 50.019 -1.297 1.00 36.26 ? 53 ARG B CD 1 ATOM 1381 N NE . ARG B 1 53 ? -3.603 49.000 -2.002 1.00 39.65 ? 53 ARG B NE 1 ATOM 1382 C CZ . ARG B 1 53 ? -2.748 49.234 -2.997 1.00 41.27 ? 53 ARG B CZ 1 ATOM 1383 N NH1 . ARG B 1 53 ? -2.530 50.472 -3.445 1.00 41.08 ? 53 ARG B NH1 1 ATOM 1384 N NH2 . ARG B 1 53 ? -2.092 48.210 -3.539 1.00 42.66 ? 53 ARG B NH2 1 ATOM 1385 N N . ASN B 1 54 ? -7.026 47.931 2.476 1.00 26.63 ? 54 ASN B N 1 ATOM 1386 C CA . ASN B 1 54 ? -8.338 47.314 2.414 1.00 28.38 ? 54 ASN B CA 1 ATOM 1387 C C . ASN B 1 54 ? -8.901 46.905 3.748 1.00 28.62 ? 54 ASN B C 1 ATOM 1388 O O . ASN B 1 54 ? -8.187 46.486 4.659 1.00 27.60 ? 54 ASN B O 1 ATOM 1389 C CB . ASN B 1 54 ? -8.350 46.122 1.453 1.00 29.68 ? 54 ASN B CB 1 ATOM 1390 C CG . ASN B 1 54 ? -8.198 46.546 -0.019 1.00 31.35 ? 54 ASN B CG 1 ATOM 1391 O OD1 . ASN B 1 54 ? -8.385 47.715 -0.387 1.00 31.26 ? 54 ASN B OD1 1 ATOM 1392 N ND2 . ASN B 1 54 ? -7.879 45.578 -0.867 1.00 33.02 ? 54 ASN B ND2 1 ATOM 1393 N N . LEU B 1 55 ? -10.209 47.070 3.846 1.00 29.31 ? 55 LEU B N 1 ATOM 1394 C CA . LEU B 1 55 ? -10.946 46.720 5.036 1.00 30.52 ? 55 LEU B CA 1 ATOM 1395 C C . LEU B 1 55 ? -11.017 45.198 5.124 1.00 31.30 ? 55 LEU B C 1 ATOM 1396 O O . LEU B 1 55 ? -11.301 44.541 4.136 1.00 31.08 ? 55 LEU B O 1 ATOM 1397 C CB . LEU B 1 55 ? -12.348 47.294 4.910 1.00 30.71 ? 55 LEU B CB 1 ATOM 1398 C CG . LEU B 1 55 ? -12.813 48.565 5.638 1.00 31.14 ? 55 LEU B CG 1 ATOM 1399 C CD1 . LEU B 1 55 ? -11.759 49.145 6.543 1.00 30.50 ? 55 LEU B CD1 1 ATOM 1400 C CD2 . LEU B 1 55 ? -13.271 49.545 4.621 1.00 31.63 ? 55 LEU B CD2 1 ATOM 1401 N N . VAL B 1 56 ? -10.732 44.652 6.300 1.00 32.77 ? 56 VAL B N 1 ATOM 1402 C CA . VAL B 1 56 ? -10.812 43.207 6.534 1.00 34.67 ? 56 VAL B CA 1 ATOM 1403 C C . VAL B 1 56 ? -12.171 42.962 7.230 1.00 35.76 ? 56 VAL B C 1 ATOM 1404 O O . VAL B 1 56 ? -12.769 41.871 7.149 1.00 36.29 ? 56 VAL B O 1 ATOM 1405 C CB . VAL B 1 56 ? -9.640 42.731 7.440 1.00 35.19 ? 56 VAL B CB 1 ATOM 1406 C CG1 . VAL B 1 56 ? -9.727 43.371 8.802 1.00 35.73 ? 56 VAL B CG1 1 ATOM 1407 C CG2 . VAL B 1 56 ? -9.646 41.232 7.570 1.00 36.74 ? 56 VAL B CG2 1 ATOM 1408 N N . GLY B 1 57 ? -12.643 44.019 7.890 1.00 36.07 ? 57 GLY B N 1 ATOM 1409 C CA . GLY B 1 57 ? -13.911 44.018 8.592 1.00 36.38 ? 57 GLY B CA 1 ATOM 1410 C C . GLY B 1 57 ? -14.389 45.458 8.566 1.00 36.72 ? 57 GLY B C 1 ATOM 1411 O O . GLY B 1 57 ? -13.683 46.314 8.028 1.00 36.74 ? 57 GLY B O 1 ATOM 1412 N N . PRO B 1 58 ? -15.560 45.767 9.153 1.00 37.03 ? 58 PRO B N 1 ATOM 1413 C CA . PRO B 1 58 ? -16.156 47.111 9.203 1.00 36.68 ? 58 PRO B CA 1 ATOM 1414 C C . PRO B 1 58 ? -15.222 48.205 9.688 1.00 36.30 ? 58 PRO B C 1 ATOM 1415 O O . PRO B 1 58 ? -15.171 49.302 9.119 1.00 35.78 ? 58 PRO B O 1 ATOM 1416 C CB . PRO B 1 58 ? -17.346 46.924 10.140 1.00 37.13 ? 58 PRO B CB 1 ATOM 1417 C CG . PRO B 1 58 ? -17.764 45.507 9.840 1.00 37.52 ? 58 PRO B CG 1 ATOM 1418 C CD . PRO B 1 58 ? -16.426 44.789 9.837 1.00 36.97 ? 58 PRO B CD 1 ATOM 1419 N N . SER B 1 59 ? -14.466 47.923 10.739 1.00 35.97 ? 59 SER B N 1 ATOM 1420 C CA . SER B 1 59 ? -13.583 48.958 11.248 1.00 35.29 ? 59 SER B CA 1 ATOM 1421 C C . SER B 1 59 ? -12.119 48.565 11.320 1.00 34.17 ? 59 SER B C 1 ATOM 1422 O O . SER B 1 59 ? -11.340 49.216 11.999 1.00 33.78 ? 59 SER B O 1 ATOM 1423 C CB . SER B 1 59 ? -14.053 49.404 12.623 1.00 35.50 ? 59 SER B CB 1 ATOM 1424 O OG . SER B 1 59 ? -13.325 50.551 13.014 1.00 38.08 ? 59 SER B OG 1 ATOM 1425 N N . ASP B 1 60 ? -11.736 47.508 10.625 1.00 32.48 ? 60 ASP B N 1 ATOM 1426 C CA . ASP B 1 60 ? -10.351 47.103 10.688 1.00 31.76 ? 60 ASP B CA 1 ATOM 1427 C C . ASP B 1 60 ? -9.705 46.939 9.336 1.00 30.12 ? 60 ASP B C 1 ATOM 1428 O O . ASP B 1 60 ? -10.198 46.174 8.503 1.00 29.05 ? 60 ASP B O 1 ATOM 1429 C CB . ASP B 1 60 ? -10.193 45.768 11.423 1.00 33.65 ? 60 ASP B CB 1 ATOM 1430 C CG . ASP B 1 60 ? -10.357 45.890 12.923 1.00 36.17 ? 60 ASP B CG 1 ATOM 1431 O OD1 . ASP B 1 60 ? -10.070 44.873 13.592 1.00 38.66 ? 60 ASP B OD1 1 ATOM 1432 O OD2 . ASP B 1 60 ? -10.762 46.968 13.431 1.00 36.84 ? 60 ASP B OD2 1 ATOM 1433 N N . PHE B 1 61 ? -8.591 47.643 9.133 1.00 27.48 ? 61 PHE B N 1 ATOM 1434 C CA . PHE B 1 61 ? -7.840 47.496 7.901 1.00 25.76 ? 61 PHE B CA 1 ATOM 1435 C C . PHE B 1 61 ? -6.851 46.330 8.119 1.00 25.48 ? 61 PHE B C 1 ATOM 1436 O O . PHE B 1 61 ? -6.565 45.979 9.256 1.00 26.46 ? 61 PHE B O 1 ATOM 1437 C CB . PHE B 1 61 ? -7.090 48.785 7.595 1.00 24.14 ? 61 PHE B CB 1 ATOM 1438 C CG . PHE B 1 61 ? -7.972 49.882 7.116 1.00 22.47 ? 61 PHE B CG 1 ATOM 1439 C CD1 . PHE B 1 61 ? -8.502 50.824 8.010 1.00 21.93 ? 61 PHE B CD1 1 ATOM 1440 C CD2 . PHE B 1 61 ? -8.322 49.949 5.777 1.00 20.56 ? 61 PHE B CD2 1 ATOM 1441 C CE1 . PHE B 1 61 ? -9.344 51.839 7.573 1.00 21.41 ? 61 PHE B CE1 1 ATOM 1442 C CE2 . PHE B 1 61 ? -9.161 50.953 5.320 1.00 20.92 ? 61 PHE B CE2 1 ATOM 1443 C CZ . PHE B 1 61 ? -9.691 51.901 6.222 1.00 21.12 ? 61 PHE B CZ 1 ATOM 1444 N N . TYR B 1 62 ? -6.387 45.688 7.053 1.00 24.10 ? 62 TYR B N 1 ATOM 1445 C CA . TYR B 1 62 ? -5.416 44.622 7.188 1.00 24.56 ? 62 TYR B CA 1 ATOM 1446 C C . TYR B 1 62 ? -4.209 45.164 7.995 1.00 23.95 ? 62 TYR B C 1 ATOM 1447 O O . TYR B 1 62 ? -3.771 46.302 7.793 1.00 23.46 ? 62 TYR B O 1 ATOM 1448 C CB . TYR B 1 62 ? -4.928 44.173 5.817 1.00 26.92 ? 62 TYR B CB 1 ATOM 1449 C CG . TYR B 1 62 ? -3.731 43.269 5.911 1.00 28.03 ? 62 TYR B CG 1 ATOM 1450 C CD1 . TYR B 1 62 ? -3.871 41.925 6.250 1.00 29.13 ? 62 TYR B CD1 1 ATOM 1451 C CD2 . TYR B 1 62 ? -2.447 43.774 5.714 1.00 29.11 ? 62 TYR B CD2 1 ATOM 1452 C CE1 . TYR B 1 62 ? -2.737 41.096 6.396 1.00 30.68 ? 62 TYR B CE1 1 ATOM 1453 C CE2 . TYR B 1 62 ? -1.310 42.966 5.851 1.00 30.20 ? 62 TYR B CE2 1 ATOM 1454 C CZ . TYR B 1 62 ? -1.461 41.633 6.198 1.00 30.77 ? 62 TYR B CZ 1 ATOM 1455 O OH . TYR B 1 62 ? -0.348 40.842 6.389 1.00 31.79 ? 62 TYR B OH 1 ATOM 1456 N N . THR B 1 63 ? -3.662 44.319 8.860 1.00 22.54 ? 63 THR B N 1 ATOM 1457 C CA . THR B 1 63 ? -2.591 44.726 9.743 1.00 22.56 ? 63 THR B CA 1 ATOM 1458 C C . THR B 1 63 ? -1.539 43.630 9.930 1.00 22.03 ? 63 THR B C 1 ATOM 1459 O O . THR B 1 63 ? -1.853 42.447 9.889 1.00 20.68 ? 63 THR B O 1 ATOM 1460 C CB . THR B 1 63 ? -3.289 45.162 11.046 1.00 23.36 ? 63 THR B CB 1 ATOM 1461 O OG1 . THR B 1 63 ? -3.154 46.566 11.195 1.00 22.72 ? 63 THR B OG1 1 ATOM 1462 C CG2 . THR B 1 63 ? -2.831 44.412 12.209 1.00 23.67 ? 63 THR B CG2 1 ATOM 1463 N N . ARG B 1 64 ? -0.278 44.031 10.095 1.00 21.11 ? 64 ARG B N 1 ATOM 1464 C CA . ARG B 1 64 ? 0.810 43.067 10.267 1.00 20.41 ? 64 ARG B CA 1 ATOM 1465 C C . ARG B 1 64 ? 1.901 43.692 11.144 1.00 20.22 ? 64 ARG B C 1 ATOM 1466 O O . ARG B 1 64 ? 2.156 44.885 11.042 1.00 18.28 ? 64 ARG B O 1 ATOM 1467 C CB . ARG B 1 64 ? 1.397 42.693 8.894 1.00 21.21 ? 64 ARG B CB 1 ATOM 1468 N N . TYR B 1 65 ? 2.528 42.874 11.983 1.00 19.53 ? 65 TYR B N 1 ATOM 1469 C CA . TYR B 1 65 ? 3.570 43.333 12.904 1.00 20.34 ? 65 TYR B CA 1 ATOM 1470 C C . TYR B 1 65 ? 4.774 42.415 12.948 1.00 20.43 ? 65 TYR B C 1 ATOM 1471 O O . TYR B 1 65 ? 4.645 41.220 12.771 1.00 22.22 ? 65 TYR B O 1 ATOM 1472 C CB . TYR B 1 65 ? 3.020 43.398 14.322 1.00 20.22 ? 65 TYR B CB 1 ATOM 1473 C CG . TYR B 1 65 ? 1.823 44.308 14.471 1.00 20.51 ? 65 TYR B CG 1 ATOM 1474 C CD1 . TYR B 1 65 ? 1.983 45.684 14.675 1.00 20.69 ? 65 TYR B CD1 1 ATOM 1475 C CD2 . TYR B 1 65 ? 0.527 43.806 14.358 1.00 19.27 ? 65 TYR B CD2 1 ATOM 1476 C CE1 . TYR B 1 65 ? 0.873 46.539 14.766 1.00 19.62 ? 65 TYR B CE1 1 ATOM 1477 C CE2 . TYR B 1 65 ? -0.583 44.658 14.440 1.00 19.54 ? 65 TYR B CE2 1 ATOM 1478 C CZ . TYR B 1 65 ? -0.403 46.016 14.636 1.00 19.77 ? 65 TYR B CZ 1 ATOM 1479 O OH . TYR B 1 65 ? -1.494 46.862 14.650 1.00 19.79 ? 65 TYR B OH 1 ATOM 1480 N N . ALA B 1 66 ? 5.939 42.998 13.217 1.00 21.52 ? 66 ALA B N 1 ATOM 1481 C CA . ALA B 1 66 ? 7.178 42.249 13.329 1.00 21.28 ? 66 ALA B CA 1 ATOM 1482 C C . ALA B 1 66 ? 7.163 41.704 14.736 1.00 21.61 ? 66 ALA B C 1 ATOM 1483 O O . ALA B 1 66 ? 6.573 42.314 15.627 1.00 20.44 ? 66 ALA B O 1 ATOM 1484 C CB . ALA B 1 66 ? 8.393 43.178 13.120 1.00 20.05 ? 66 ALA B CB 1 ATOM 1485 N N . ASP B 1 67 ? 7.830 40.573 14.950 1.00 22.56 ? 67 ASP B N 1 ATOM 1486 C CA . ASP B 1 67 ? 7.851 39.958 16.266 1.00 24.36 ? 67 ASP B CA 1 ATOM 1487 C C . ASP B 1 67 ? 8.348 40.834 17.399 1.00 25.09 ? 67 ASP B C 1 ATOM 1488 O O . ASP B 1 67 ? 7.862 40.727 18.529 1.00 25.34 ? 67 ASP B O 1 ATOM 1489 C CB . ASP B 1 67 ? 8.689 38.685 16.240 1.00 25.78 ? 67 ASP B CB 1 ATOM 1490 C CG . ASP B 1 67 ? 8.024 37.579 15.472 1.00 27.04 ? 67 ASP B CG 1 ATOM 1491 O OD1 . ASP B 1 67 ? 6.778 37.566 15.430 1.00 28.43 ? 67 ASP B OD1 1 ATOM 1492 O OD2 . ASP B 1 67 ? 8.752 36.718 14.931 1.00 28.23 ? 67 ASP B OD2 1 ATOM 1493 N N . SER B 1 68 ? 9.310 41.699 17.120 1.00 25.02 ? 68 SER B N 1 ATOM 1494 C CA . SER B 1 68 ? 9.842 42.557 18.175 1.00 25.83 ? 68 SER B CA 1 ATOM 1495 C C . SER B 1 68 ? 8.796 43.513 18.779 1.00 25.53 ? 68 SER B C 1 ATOM 1496 O O . SER B 1 68 ? 8.955 43.960 19.917 1.00 25.86 ? 68 SER B O 1 ATOM 1497 C CB . SER B 1 68 ? 11.045 43.359 17.645 1.00 25.77 ? 68 SER B CB 1 ATOM 1498 O OG . SER B 1 68 ? 10.674 44.109 16.491 1.00 28.49 ? 68 SER B OG 1 ATOM 1499 N N . VAL B 1 69 ? 7.711 43.808 18.058 1.00 24.68 ? 69 VAL B N 1 ATOM 1500 C CA . VAL B 1 69 ? 6.721 44.753 18.583 1.00 23.35 ? 69 VAL B CA 1 ATOM 1501 C C . VAL B 1 69 ? 5.271 44.274 18.691 1.00 24.48 ? 69 VAL B C 1 ATOM 1502 O O . VAL B 1 69 ? 4.419 44.979 19.210 1.00 23.30 ? 69 VAL B O 1 ATOM 1503 C CB . VAL B 1 69 ? 6.729 46.061 17.763 1.00 23.38 ? 69 VAL B CB 1 ATOM 1504 C CG1 . VAL B 1 69 ? 8.113 46.686 17.780 1.00 22.84 ? 69 VAL B CG1 1 ATOM 1505 C CG2 . VAL B 1 69 ? 6.331 45.795 16.322 1.00 21.44 ? 69 VAL B CG2 1 ATOM 1506 N N . LYS B 1 70 ? 5.000 43.065 18.225 1.00 25.64 ? 70 LYS B N 1 ATOM 1507 C CA . LYS B 1 70 ? 3.652 42.532 18.258 1.00 27.59 ? 70 LYS B CA 1 ATOM 1508 C C . LYS B 1 70 ? 3.156 42.535 19.693 1.00 27.74 ? 70 LYS B C 1 ATOM 1509 O O . LYS B 1 70 ? 3.874 42.137 20.622 1.00 28.45 ? 70 LYS B O 1 ATOM 1510 C CB . LYS B 1 70 ? 3.656 41.115 17.680 1.00 29.47 ? 70 LYS B CB 1 ATOM 1511 C CG . LYS B 1 70 ? 2.294 40.475 17.513 1.00 32.80 ? 70 LYS B CG 1 ATOM 1512 C CD . LYS B 1 70 ? 2.353 39.447 16.387 1.00 35.83 ? 70 LYS B CD 1 ATOM 1513 C CE . LYS B 1 70 ? 0.956 39.018 15.971 1.00 37.22 ? 70 LYS B CE 1 ATOM 1514 N NZ . LYS B 1 70 ? 1.031 37.922 14.968 1.00 39.36 ? 70 LYS B NZ 1 ATOM 1515 N N . GLY B 1 71 ? 1.938 43.015 19.889 1.00 26.79 ? 71 GLY B N 1 ATOM 1516 C CA . GLY B 1 71 ? 1.399 43.026 21.230 1.00 26.12 ? 71 GLY B CA 1 ATOM 1517 C C . GLY B 1 71 ? 1.639 44.337 21.933 1.00 25.45 ? 71 GLY B C 1 ATOM 1518 O O . GLY B 1 71 ? 0.881 44.670 22.830 1.00 26.20 ? 71 GLY B O 1 ATOM 1519 N N . ARG B 1 72 ? 2.670 45.083 21.529 1.00 23.22 ? 72 ARG B N 1 ATOM 1520 C CA . ARG B 1 72 ? 2.977 46.372 22.143 1.00 22.34 ? 72 ARG B CA 1 ATOM 1521 C C . ARG B 1 72 ? 2.631 47.570 21.269 1.00 20.94 ? 72 ARG B C 1 ATOM 1522 O O . ARG B 1 72 ? 2.336 48.642 21.785 1.00 21.05 ? 72 ARG B O 1 ATOM 1523 C CB . ARG B 1 72 ? 4.473 46.476 22.481 1.00 22.68 ? 72 ARG B CB 1 ATOM 1524 C CG . ARG B 1 72 ? 4.936 45.603 23.626 1.00 25.87 ? 72 ARG B CG 1 ATOM 1525 C CD . ARG B 1 72 ? 6.474 45.439 23.653 1.00 26.33 ? 72 ARG B CD 1 ATOM 1526 N NE . ARG B 1 72 ? 7.115 46.717 23.805 1.00 27.93 ? 72 ARG B NE 1 ATOM 1527 C CZ . ARG B 1 72 ? 8.112 47.158 23.051 1.00 27.41 ? 72 ARG B CZ 1 ATOM 1528 N NH1 . ARG B 1 72 ? 8.605 46.420 22.073 1.00 28.86 ? 72 ARG B NH1 1 ATOM 1529 N NH2 . ARG B 1 72 ? 8.596 48.353 23.271 1.00 27.08 ? 72 ARG B NH2 1 ATOM 1530 N N . PHE B 1 73 ? 2.691 47.393 19.956 1.00 18.63 ? 73 PHE B N 1 ATOM 1531 C CA . PHE B 1 73 ? 2.420 48.474 19.029 1.00 18.94 ? 73 PHE B CA 1 ATOM 1532 C C . PHE B 1 73 ? 1.122 48.181 18.271 1.00 18.73 ? 73 PHE B C 1 ATOM 1533 O O . PHE B 1 73 ? 0.774 47.040 17.999 1.00 18.44 ? 73 PHE B O 1 ATOM 1534 C CB . PHE B 1 73 ? 3.533 48.601 17.965 1.00 19.29 ? 73 PHE B CB 1 ATOM 1535 C CG . PHE B 1 73 ? 4.840 49.173 18.472 1.00 19.49 ? 73 PHE B CG 1 ATOM 1536 C CD1 . PHE B 1 73 ? 5.141 49.192 19.832 1.00 19.64 ? 73 PHE B CD1 1 ATOM 1537 C CD2 . PHE B 1 73 ? 5.796 49.631 17.578 1.00 19.62 ? 73 PHE B CD2 1 ATOM 1538 C CE1 . PHE B 1 73 ? 6.381 49.658 20.295 1.00 19.69 ? 73 PHE B CE1 1 ATOM 1539 C CE2 . PHE B 1 73 ? 7.036 50.094 18.024 1.00 19.19 ? 73 PHE B CE2 1 ATOM 1540 C CZ . PHE B 1 73 ? 7.328 50.104 19.386 1.00 19.29 ? 73 PHE B CZ 1 ATOM 1541 N N . ALA B 1 74 ? 0.400 49.231 17.944 1.00 17.94 ? 74 ALA B N 1 ATOM 1542 C CA . ALA B 1 74 ? -0.804 49.036 17.166 1.00 18.57 ? 74 ALA B CA 1 ATOM 1543 C C . ALA B 1 74 ? -0.796 50.159 16.121 1.00 18.18 ? 74 ALA B C 1 ATOM 1544 O O . ALA B 1 74 ? -0.573 51.337 16.429 1.00 18.40 ? 74 ALA B O 1 ATOM 1545 C CB . ALA B 1 74 ? -2.046 49.101 18.077 1.00 18.46 ? 74 ALA B CB 1 ATOM 1546 N N . VAL B 1 75 ? -0.990 49.786 14.871 1.00 17.01 ? 75 VAL B N 1 ATOM 1547 C CA . VAL B 1 75 ? -1.021 50.765 13.809 1.00 17.07 ? 75 VAL B CA 1 ATOM 1548 C C . VAL B 1 75 ? -2.510 50.964 13.407 1.00 17.61 ? 75 VAL B C 1 ATOM 1549 O O . VAL B 1 75 ? -3.279 50.016 13.404 1.00 17.50 ? 75 VAL B O 1 ATOM 1550 C CB . VAL B 1 75 ? -0.171 50.261 12.619 1.00 15.95 ? 75 VAL B CB 1 ATOM 1551 C CG1 . VAL B 1 75 ? -0.714 48.957 12.097 1.00 16.21 ? 75 VAL B CG1 1 ATOM 1552 C CG2 . VAL B 1 75 ? -0.108 51.300 11.536 1.00 17.29 ? 75 VAL B CG2 1 ATOM 1553 N N . SER B 1 76 ? -2.908 52.188 13.085 1.00 17.73 ? 76 SER B N 1 ATOM 1554 C CA . SER B 1 76 ? -4.286 52.432 12.687 1.00 18.23 ? 76 SER B CA 1 ATOM 1555 C C . SER B 1 76 ? -4.340 53.444 11.579 1.00 18.71 ? 76 SER B C 1 ATOM 1556 O O . SER B 1 76 ? -3.471 54.323 11.446 1.00 20.46 ? 76 SER B O 1 ATOM 1557 C CB . SER B 1 76 ? -5.104 52.926 13.875 1.00 17.76 ? 76 SER B CB 1 ATOM 1558 O OG . SER B 1 76 ? -4.579 54.173 14.286 1.00 18.39 ? 76 SER B OG 1 ATOM 1559 N N . ARG B 1 77 ? -5.391 53.367 10.795 1.00 18.76 ? 77 ARG B N 1 ATOM 1560 C CA . ARG B 1 77 ? -5.513 54.270 9.676 1.00 19.05 ? 77 ARG B CA 1 ATOM 1561 C C . ARG B 1 77 ? -6.677 55.252 9.807 1.00 19.45 ? 77 ARG B C 1 ATOM 1562 O O . ARG B 1 77 ? -7.751 54.864 10.220 1.00 19.83 ? 77 ARG B O 1 ATOM 1563 C CB . ARG B 1 77 ? -5.680 53.412 8.432 1.00 17.68 ? 77 ARG B CB 1 ATOM 1564 C CG . ARG B 1 77 ? -5.948 54.173 7.177 1.00 17.75 ? 77 ARG B CG 1 ATOM 1565 C CD . ARG B 1 77 ? -6.205 53.165 6.088 1.00 18.91 ? 77 ARG B CD 1 ATOM 1566 N NE . ARG B 1 77 ? -5.033 52.418 5.613 1.00 17.17 ? 77 ARG B NE 1 ATOM 1567 C CZ . ARG B 1 77 ? -4.184 52.855 4.688 1.00 18.74 ? 77 ARG B CZ 1 ATOM 1568 N NH1 . ARG B 1 77 ? -3.169 52.096 4.294 1.00 16.79 ? 77 ARG B NH1 1 ATOM 1569 N NH2 . ARG B 1 77 ? -4.332 54.065 4.177 1.00 18.22 ? 77 ARG B NH2 1 ATOM 1570 N N . ASP B 1 78 ? -6.456 56.513 9.457 1.00 19.41 ? 78 ASP B N 1 ATOM 1571 C CA . ASP B 1 78 ? -7.514 57.507 9.464 1.00 20.22 ? 78 ASP B CA 1 ATOM 1572 C C . ASP B 1 78 ? -7.402 58.233 8.128 1.00 19.75 ? 78 ASP B C 1 ATOM 1573 O O . ASP B 1 78 ? -6.788 59.293 8.042 1.00 19.61 ? 78 ASP B O 1 ATOM 1574 C CB . ASP B 1 78 ? -7.330 58.498 10.602 1.00 22.24 ? 78 ASP B CB 1 ATOM 1575 C CG . ASP B 1 78 ? -8.482 59.469 10.703 1.00 25.05 ? 78 ASP B CG 1 ATOM 1576 O OD1 . ASP B 1 78 ? -8.402 60.403 11.523 1.00 27.61 ? 78 ASP B OD1 1 ATOM 1577 O OD2 . ASP B 1 78 ? -9.477 59.300 9.960 1.00 25.67 ? 78 ASP B OD2 1 ATOM 1578 N N . ASN B 1 79 ? -7.959 57.634 7.080 1.00 19.29 ? 79 ASN B N 1 ATOM 1579 C CA . ASN B 1 79 ? -7.932 58.220 5.727 1.00 19.00 ? 79 ASN B CA 1 ATOM 1580 C C . ASN B 1 79 ? -8.481 59.636 5.681 1.00 18.77 ? 79 ASN B C 1 ATOM 1581 O O . ASN B 1 79 ? -7.975 60.476 4.939 1.00 18.70 ? 79 ASN B O 1 ATOM 1582 C CB . ASN B 1 79 ? -8.756 57.366 4.749 1.00 18.53 ? 79 ASN B CB 1 ATOM 1583 C CG . ASN B 1 79 ? -8.104 56.043 4.435 1.00 19.98 ? 79 ASN B CG 1 ATOM 1584 O OD1 . ASN B 1 79 ? -8.774 55.105 3.992 1.00 19.72 ? 79 ASN B OD1 1 ATOM 1585 N ND2 . ASN B 1 79 ? -6.787 55.954 4.646 1.00 17.64 ? 79 ASN B ND2 1 ATOM 1586 N N . ALA B 1 80 ? -9.521 59.899 6.483 1.00 19.16 ? 80 ALA B N 1 ATOM 1587 C CA . ALA B 1 80 ? -10.164 61.222 6.519 1.00 19.84 ? 80 ALA B CA 1 ATOM 1588 C C . ALA B 1 80 ? -9.211 62.348 6.910 1.00 20.45 ? 80 ALA B C 1 ATOM 1589 O O . ALA B 1 80 ? -9.379 63.486 6.474 1.00 19.98 ? 80 ALA B O 1 ATOM 1590 C CB . ALA B 1 80 ? -11.393 61.211 7.505 1.00 20.45 ? 80 ALA B CB 1 ATOM 1591 N N . LYS B 1 81 ? -8.230 62.045 7.752 1.00 20.61 ? 81 LYS B N 1 ATOM 1592 C CA . LYS B 1 81 ? -7.266 63.057 8.154 1.00 20.85 ? 81 LYS B CA 1 ATOM 1593 C C . LYS B 1 81 ? -5.966 62.839 7.409 1.00 19.80 ? 81 LYS B C 1 ATOM 1594 O O . LYS B 1 81 ? -4.983 63.513 7.682 1.00 18.49 ? 81 LYS B O 1 ATOM 1595 C CB . LYS B 1 81 ? -7.022 63.027 9.680 1.00 23.48 ? 81 LYS B CB 1 ATOM 1596 C CG . LYS B 1 81 ? -8.255 63.513 10.516 1.00 28.01 ? 81 LYS B CG 1 ATOM 1597 C CD . LYS B 1 81 ? -7.920 63.952 11.966 1.00 30.00 ? 81 LYS B CD 1 ATOM 1598 C CE . LYS B 1 81 ? -9.166 64.540 12.696 1.00 32.38 ? 81 LYS B CE 1 ATOM 1599 N NZ . LYS B 1 81 ? -9.718 65.807 12.039 1.00 34.06 ? 81 LYS B NZ 1 ATOM 1600 N N . ASN B 1 82 ? -5.983 61.911 6.454 1.00 18.19 ? 82 ASN B N 1 ATOM 1601 C CA . ASN B 1 82 ? -4.812 61.577 5.647 1.00 16.67 ? 82 ASN B CA 1 ATOM 1602 C C . ASN B 1 82 ? -3.627 61.204 6.583 1.00 17.13 ? 82 ASN B C 1 ATOM 1603 O O . ASN B 1 82 ? -2.507 61.648 6.370 1.00 16.46 ? 82 ASN B O 1 ATOM 1604 C CB . ASN B 1 82 ? -4.452 62.781 4.770 1.00 16.56 ? 82 ASN B CB 1 ATOM 1605 C CG . ASN B 1 82 ? -4.059 62.369 3.374 1.00 15.35 ? 82 ASN B CG 1 ATOM 1606 O OD1 . ASN B 1 82 ? -4.297 61.245 3.000 1.00 17.67 ? 82 ASN B OD1 1 ATOM 1607 N ND2 . ASN B 1 82 ? -3.480 63.276 2.592 1.00 16.84 ? 82 ASN B ND2 1 ATOM 1608 N N . THR B 1 83 ? -3.892 60.375 7.591 1.00 16.00 ? 83 THR B N 1 ATOM 1609 C CA . THR B 1 83 ? -2.892 60.006 8.588 1.00 16.18 ? 83 THR B CA 1 ATOM 1610 C C . THR B 1 83 ? -2.984 58.527 8.969 1.00 16.39 ? 83 THR B C 1 ATOM 1611 O O . THR B 1 83 ? -4.078 57.934 8.905 1.00 15.59 ? 83 THR B O 1 ATOM 1612 C CB . THR B 1 83 ? -3.133 60.864 9.871 1.00 17.33 ? 83 THR B CB 1 ATOM 1613 O OG1 . THR B 1 83 ? -3.030 62.261 9.550 1.00 18.08 ? 83 THR B OG1 1 ATOM 1614 C CG2 . THR B 1 83 ? -2.160 60.513 10.985 1.00 16.59 ? 83 THR B CG2 1 ATOM 1615 N N . VAL B 1 84 ? -1.838 57.931 9.331 1.00 15.61 ? 84 VAL B N 1 ATOM 1616 C CA . VAL B 1 84 ? -1.748 56.555 9.813 1.00 14.66 ? 84 VAL B CA 1 ATOM 1617 C C . VAL B 1 84 ? -1.042 56.771 11.146 1.00 16.07 ? 84 VAL B C 1 ATOM 1618 O O . VAL B 1 84 ? -0.146 57.607 11.235 1.00 16.70 ? 84 VAL B O 1 ATOM 1619 C CB . VAL B 1 84 ? -0.894 55.666 8.902 1.00 14.87 ? 84 VAL B CB 1 ATOM 1620 C CG1 . VAL B 1 84 ? -0.450 54.412 9.650 1.00 15.47 ? 84 VAL B CG1 1 ATOM 1621 C CG2 . VAL B 1 84 ? -1.683 55.290 7.681 1.00 13.84 ? 84 VAL B CG2 1 ATOM 1622 N N . ASN B 1 85 ? -1.458 56.065 12.186 1.00 15.15 ? 85 ASN B N 1 ATOM 1623 C CA . ASN B 1 85 ? -0.872 56.280 13.496 1.00 16.95 ? 85 ASN B CA 1 ATOM 1624 C C . ASN B 1 85 ? -0.189 55.023 13.948 1.00 16.62 ? 85 ASN B C 1 ATOM 1625 O O . ASN B 1 85 ? -0.554 53.916 13.506 1.00 16.00 ? 85 ASN B O 1 ATOM 1626 C CB . ASN B 1 85 ? -1.950 56.615 14.548 1.00 18.83 ? 85 ASN B CB 1 ATOM 1627 C CG . ASN B 1 85 ? -2.655 57.920 14.271 1.00 21.51 ? 85 ASN B CG 1 ATOM 1628 O OD1 . ASN B 1 85 ? -3.868 57.945 14.090 1.00 24.65 ? 85 ASN B OD1 1 ATOM 1629 N ND2 . ASN B 1 85 ? -1.911 59.012 14.247 1.00 21.09 ? 85 ASN B ND2 1 ATOM 1630 N N . LEU B 1 86 ? 0.795 55.181 14.835 1.00 15.31 ? 86 LEU B N 1 ATOM 1631 C CA . LEU B 1 86 ? 1.487 54.020 15.385 1.00 15.02 ? 86 LEU B CA 1 ATOM 1632 C C . LEU B 1 86 ? 1.427 54.262 16.874 1.00 15.80 ? 86 LEU B C 1 ATOM 1633 O O . LEU B 1 86 ? 2.075 55.181 17.377 1.00 15.94 ? 86 LEU B O 1 ATOM 1634 C CB . LEU B 1 86 ? 2.954 53.954 14.927 1.00 15.46 ? 86 LEU B CB 1 ATOM 1635 C CG . LEU B 1 86 ? 3.740 52.771 15.538 1.00 15.90 ? 86 LEU B CG 1 ATOM 1636 C CD1 . LEU B 1 86 ? 3.138 51.454 15.062 1.00 15.05 ? 86 LEU B CD1 1 ATOM 1637 C CD2 . LEU B 1 86 ? 5.250 52.826 15.131 1.00 16.25 ? 86 LEU B CD2 1 ATOM 1638 N N . GLN B 1 87 ? 0.634 53.460 17.573 1.00 15.24 ? 87 GLN B N 1 ATOM 1639 C CA . GLN B 1 87 ? 0.483 53.605 19.015 1.00 16.35 ? 87 GLN B CA 1 ATOM 1640 C C . GLN B 1 87 ? 1.582 52.714 19.593 1.00 15.86 ? 87 GLN B C 1 ATOM 1641 O O . GLN B 1 87 ? 1.617 51.546 19.285 1.00 16.85 ? 87 GLN B O 1 ATOM 1642 C CB . GLN B 1 87 ? -0.901 53.101 19.459 1.00 16.98 ? 87 GLN B CB 1 ATOM 1643 C CG . GLN B 1 87 ? -1.117 53.064 20.968 1.00 18.33 ? 87 GLN B CG 1 ATOM 1644 C CD . GLN B 1 87 ? -1.094 54.421 21.568 1.00 19.63 ? 87 GLN B CD 1 ATOM 1645 O OE1 . GLN B 1 87 ? -1.686 55.350 21.039 1.00 21.93 ? 87 GLN B OE1 1 ATOM 1646 N NE2 . GLN B 1 87 ? -0.423 54.558 22.687 1.00 21.48 ? 87 GLN B NE2 1 ATOM 1647 N N . MET B 1 88 ? 2.462 53.258 20.421 1.00 15.28 ? 88 MET B N 1 ATOM 1648 C CA . MET B 1 88 ? 3.562 52.459 20.964 1.00 15.54 ? 88 MET B CA 1 ATOM 1649 C C . MET B 1 88 ? 3.436 52.350 22.468 1.00 15.66 ? 88 MET B C 1 ATOM 1650 O O . MET B 1 88 ? 3.521 53.350 23.167 1.00 14.98 ? 88 MET B O 1 ATOM 1651 C CB . MET B 1 88 ? 4.880 53.116 20.572 1.00 16.78 ? 88 MET B CB 1 ATOM 1652 C CG . MET B 1 88 ? 5.088 53.211 19.080 1.00 17.49 ? 88 MET B CG 1 ATOM 1653 S SD . MET B 1 88 ? 6.735 53.982 18.730 1.00 22.47 ? 88 MET B SD 1 ATOM 1654 C CE . MET B 1 88 ? 6.531 55.605 19.193 1.00 16.08 ? 88 MET B CE 1 ATOM 1655 N N . ASN B 1 89 ? 3.247 51.136 22.964 1.00 15.93 ? 89 ASN B N 1 ATOM 1656 C CA . ASN B 1 89 ? 3.060 50.971 24.405 1.00 18.36 ? 89 ASN B CA 1 ATOM 1657 C C . ASN B 1 89 ? 4.236 50.276 25.086 1.00 19.61 ? 89 ASN B C 1 ATOM 1658 O O . ASN B 1 89 ? 5.035 49.627 24.420 1.00 21.33 ? 89 ASN B O 1 ATOM 1659 C CB . ASN B 1 89 ? 1.744 50.197 24.680 1.00 15.70 ? 89 ASN B CB 1 ATOM 1660 C CG . ASN B 1 89 ? 0.520 50.981 24.249 1.00 14.49 ? 89 ASN B CG 1 ATOM 1661 O OD1 . ASN B 1 89 ? 0.500 52.189 24.383 1.00 15.62 ? 89 ASN B OD1 1 ATOM 1662 N ND2 . ASN B 1 89 ? -0.501 50.304 23.756 1.00 16.17 ? 89 ASN B ND2 1 ATOM 1663 N N . SER B 1 90 ? 4.336 50.448 26.407 1.00 20.90 ? 90 SER B N 1 ATOM 1664 C CA . SER B 1 90 ? 5.384 49.840 27.223 1.00 22.05 ? 90 SER B CA 1 ATOM 1665 C C . SER B 1 90 ? 6.762 50.005 26.568 1.00 21.74 ? 90 SER B C 1 ATOM 1666 O O . SER B 1 90 ? 7.441 49.013 26.283 1.00 22.25 ? 90 SER B O 1 ATOM 1667 C CB . SER B 1 90 ? 5.084 48.360 27.392 1.00 23.02 ? 90 SER B CB 1 ATOM 1668 O OG . SER B 1 90 ? 3.706 48.196 27.659 1.00 26.96 ? 90 SER B OG 1 ATOM 1669 N N . LEU B 1 91 ? 7.143 51.252 26.327 1.00 22.02 ? 91 LEU B N 1 ATOM 1670 C CA . LEU B 1 91 ? 8.399 51.586 25.711 1.00 23.27 ? 91 LEU B CA 1 ATOM 1671 C C . LEU B 1 91 ? 9.612 51.221 26.568 1.00 24.65 ? 91 LEU B C 1 ATOM 1672 O O . LEU B 1 91 ? 9.616 51.435 27.792 1.00 23.52 ? 91 LEU B O 1 ATOM 1673 C CB . LEU B 1 91 ? 8.416 53.068 25.397 1.00 23.29 ? 91 LEU B CB 1 ATOM 1674 C CG . LEU B 1 91 ? 7.527 53.446 24.220 1.00 24.40 ? 91 LEU B CG 1 ATOM 1675 C CD1 . LEU B 1 91 ? 7.568 54.949 24.038 1.00 24.33 ? 91 LEU B CD1 1 ATOM 1676 C CD2 . LEU B 1 91 ? 8.003 52.728 22.962 1.00 23.21 ? 91 LEU B CD2 1 ATOM 1677 N N . LYS B 1 92 ? 10.638 50.693 25.894 1.00 25.67 ? 92 LYS B N 1 ATOM 1678 C CA . LYS B 1 92 ? 11.887 50.257 26.520 1.00 26.67 ? 92 LYS B CA 1 ATOM 1679 C C . LYS B 1 92 ? 13.019 51.071 25.917 1.00 27.24 ? 92 LYS B C 1 ATOM 1680 O O . LYS B 1 92 ? 12.906 51.565 24.788 1.00 27.06 ? 92 LYS B O 1 ATOM 1681 C CB . LYS B 1 92 ? 12.139 48.782 26.216 1.00 27.57 ? 92 LYS B CB 1 ATOM 1682 C CG . LYS B 1 92 ? 10.990 47.861 26.529 1.00 29.93 ? 92 LYS B CG 1 ATOM 1683 C CD . LYS B 1 92 ? 11.260 46.486 25.951 1.00 32.41 ? 92 LYS B CD 1 ATOM 1684 C CE . LYS B 1 92 ? 10.234 45.473 26.452 1.00 34.86 ? 92 LYS B CE 1 ATOM 1685 N NZ . LYS B 1 92 ? 10.673 44.058 26.160 1.00 36.68 ? 92 LYS B NZ 1 ATOM 1686 N N . PRO B 1 93 ? 14.146 51.199 26.644 1.00 27.55 ? 93 PRO B N 1 ATOM 1687 C CA . PRO B 1 93 ? 15.260 51.973 26.099 1.00 27.05 ? 93 PRO B CA 1 ATOM 1688 C C . PRO B 1 93 ? 15.649 51.426 24.737 1.00 26.22 ? 93 PRO B C 1 ATOM 1689 O O . PRO B 1 93 ? 16.040 52.173 23.872 1.00 27.03 ? 93 PRO B O 1 ATOM 1690 C CB . PRO B 1 93 ? 16.358 51.790 27.157 1.00 27.84 ? 93 PRO B CB 1 ATOM 1691 C CG . PRO B 1 93 ? 15.579 51.675 28.426 1.00 27.54 ? 93 PRO B CG 1 ATOM 1692 C CD . PRO B 1 93 ? 14.474 50.692 27.992 1.00 27.62 ? 93 PRO B CD 1 ATOM 1693 N N . GLU B 1 94 ? 15.493 50.128 24.543 1.00 26.83 ? 94 GLU B N 1 ATOM 1694 C CA . GLU B 1 94 ? 15.832 49.508 23.273 1.00 28.17 ? 94 GLU B CA 1 ATOM 1695 C C . GLU B 1 94 ? 14.963 49.971 22.097 1.00 27.55 ? 94 GLU B C 1 ATOM 1696 O O . GLU B 1 94 ? 15.217 49.601 20.945 1.00 26.76 ? 94 GLU B O 1 ATOM 1697 C CB . GLU B 1 94 ? 15.703 48.004 23.383 1.00 31.55 ? 94 GLU B CB 1 ATOM 1698 C CG . GLU B 1 94 ? 16.541 47.397 24.481 1.00 37.68 ? 94 GLU B CG 1 ATOM 1699 C CD . GLU B 1 94 ? 16.388 45.874 24.557 1.00 40.53 ? 94 GLU B CD 1 ATOM 1700 O OE1 . GLU B 1 94 ? 15.234 45.417 24.756 1.00 42.19 ? 94 GLU B OE1 1 ATOM 1701 O OE2 . GLU B 1 94 ? 17.414 45.143 24.419 1.00 42.98 ? 94 GLU B OE2 1 ATOM 1702 N N . ASP B 1 95 ? 13.923 50.759 22.392 1.00 25.70 ? 95 ASP B N 1 ATOM 1703 C CA . ASP B 1 95 ? 13.023 51.264 21.357 1.00 22.74 ? 95 ASP B CA 1 ATOM 1704 C C . ASP B 1 95 ? 13.508 52.597 20.870 1.00 21.75 ? 95 ASP B C 1 ATOM 1705 O O . ASP B 1 95 ? 12.920 53.172 19.964 1.00 21.54 ? 95 ASP B O 1 ATOM 1706 C CB . ASP B 1 95 ? 11.591 51.432 21.907 1.00 21.33 ? 95 ASP B CB 1 ATOM 1707 C CG . ASP B 1 95 ? 10.951 50.129 22.235 1.00 18.81 ? 95 ASP B CG 1 ATOM 1708 O OD1 . ASP B 1 95 ? 11.048 49.190 21.430 1.00 19.30 ? 95 ASP B OD1 1 ATOM 1709 O OD2 . ASP B 1 95 ? 10.351 50.026 23.311 1.00 20.25 ? 95 ASP B OD2 1 ATOM 1710 N N . THR B 1 96 ? 14.572 53.110 21.487 1.00 20.47 ? 96 THR B N 1 ATOM 1711 C CA . THR B 1 96 ? 15.108 54.396 21.081 1.00 20.36 ? 96 THR B CA 1 ATOM 1712 C C . THR B 1 96 ? 15.576 54.291 19.657 1.00 19.40 ? 96 THR B C 1 ATOM 1713 O O . THR B 1 96 ? 16.337 53.396 19.333 1.00 20.27 ? 96 THR B O 1 ATOM 1714 C CB . THR B 1 96 ? 16.291 54.813 21.950 1.00 20.40 ? 96 THR B CB 1 ATOM 1715 O OG1 . THR B 1 96 ? 15.804 55.155 23.243 1.00 21.21 ? 96 THR B OG1 1 ATOM 1716 C CG2 . THR B 1 96 ? 16.979 56.017 21.373 1.00 19.26 ? 96 THR B CG2 1 ATOM 1717 N N . ALA B 1 97 ? 15.137 55.216 18.810 1.00 18.38 ? 97 ALA B N 1 ATOM 1718 C CA . ALA B 1 97 ? 15.513 55.180 17.398 1.00 17.92 ? 97 ALA B CA 1 ATOM 1719 C C . ALA B 1 97 ? 14.835 56.312 16.665 1.00 17.73 ? 97 ALA B C 1 ATOM 1720 O O . ALA B 1 97 ? 14.150 57.139 17.269 1.00 18.44 ? 97 ALA B O 1 ATOM 1721 C CB . ALA B 1 97 ? 15.092 53.837 16.780 1.00 16.91 ? 97 ALA B CB 1 ATOM 1722 N N . VAL B 1 98 ? 15.068 56.378 15.363 1.00 16.54 ? 98 VAL B N 1 ATOM 1723 C CA . VAL B 1 98 ? 14.405 57.373 14.530 1.00 15.95 ? 98 VAL B CA 1 ATOM 1724 C C . VAL B 1 98 ? 13.336 56.487 13.914 1.00 14.97 ? 98 VAL B C 1 ATOM 1725 O O . VAL B 1 98 ? 13.648 55.397 13.458 1.00 15.14 ? 98 VAL B O 1 ATOM 1726 C CB . VAL B 1 98 ? 15.343 57.927 13.441 1.00 17.11 ? 98 VAL B CB 1 ATOM 1727 C CG1 . VAL B 1 98 ? 14.588 58.901 12.544 1.00 18.02 ? 98 VAL B CG1 1 ATOM 1728 C CG2 . VAL B 1 98 ? 16.515 58.711 14.110 1.00 18.41 ? 98 VAL B CG2 1 ATOM 1729 N N . TYR B 1 99 ? 12.076 56.915 13.950 1.00 13.56 ? 99 TYR B N 1 ATOM 1730 C CA . TYR B 1 99 ? 10.984 56.087 13.398 1.00 13.02 ? 99 TYR B CA 1 ATOM 1731 C C . TYR B 1 99 ? 10.559 56.686 12.085 1.00 12.25 ? 99 TYR B C 1 ATOM 1732 O O . TYR B 1 99 ? 10.477 57.895 11.990 1.00 12.04 ? 99 TYR B O 1 ATOM 1733 C CB . TYR B 1 99 ? 9.823 56.069 14.390 1.00 13.58 ? 99 TYR B CB 1 ATOM 1734 C CG . TYR B 1 99 ? 10.094 55.127 15.535 1.00 15.15 ? 99 TYR B CG 1 ATOM 1735 C CD1 . TYR B 1 99 ? 11.073 55.411 16.494 1.00 14.99 ? 99 TYR B CD1 1 ATOM 1736 C CD2 . TYR B 1 99 ? 9.404 53.927 15.646 1.00 13.72 ? 99 TYR B CD2 1 ATOM 1737 C CE1 . TYR B 1 99 ? 11.354 54.495 17.544 1.00 12.91 ? 99 TYR B CE1 1 ATOM 1738 C CE2 . TYR B 1 99 ? 9.677 53.055 16.670 1.00 14.44 ? 99 TYR B CE2 1 ATOM 1739 C CZ . TYR B 1 99 ? 10.652 53.345 17.604 1.00 13.86 ? 99 TYR B CZ 1 ATOM 1740 O OH . TYR B 1 99 ? 10.900 52.408 18.567 1.00 14.76 ? 99 TYR B OH 1 ATOM 1741 N N . TYR B 1 100 ? 10.321 55.853 11.072 1.00 11.49 ? 100 TYR B N 1 ATOM 1742 C CA . TYR B 1 100 ? 9.932 56.357 9.754 1.00 12.64 ? 100 TYR B CA 1 ATOM 1743 C C . TYR B 1 100 ? 8.687 55.680 9.244 1.00 11.89 ? 100 TYR B C 1 ATOM 1744 O O . TYR B 1 100 ? 8.476 54.515 9.525 1.00 11.57 ? 100 TYR B O 1 ATOM 1745 C CB . TYR B 1 100 ? 10.970 55.974 8.673 1.00 14.78 ? 100 TYR B CB 1 ATOM 1746 C CG . TYR B 1 100 ? 12.333 56.551 8.862 1.00 19.08 ? 100 TYR B CG 1 ATOM 1747 C CD1 . TYR B 1 100 ? 13.247 55.991 9.790 1.00 20.00 ? 100 TYR B CD1 1 ATOM 1748 C CD2 . TYR B 1 100 ? 12.722 57.673 8.139 1.00 19.61 ? 100 TYR B CD2 1 ATOM 1749 C CE1 . TYR B 1 100 ? 14.530 56.568 9.977 1.00 21.38 ? 100 TYR B CE1 1 ATOM 1750 C CE2 . TYR B 1 100 ? 13.991 58.247 8.317 1.00 21.27 ? 100 TYR B CE2 1 ATOM 1751 C CZ . TYR B 1 100 ? 14.883 57.692 9.236 1.00 22.19 ? 100 TYR B CZ 1 ATOM 1752 O OH . TYR B 1 100 ? 16.121 58.303 9.368 1.00 23.99 ? 100 TYR B OH 1 ATOM 1753 N N . CYS B 1 101 ? 7.888 56.380 8.449 1.00 12.67 ? 101 CYS B N 1 ATOM 1754 C CA . CYS B 1 101 ? 6.774 55.668 7.802 1.00 13.57 ? 101 CYS B CA 1 ATOM 1755 C C . CYS B 1 101 ? 7.120 55.713 6.310 1.00 12.72 ? 101 CYS B C 1 ATOM 1756 O O . CYS B 1 101 ? 7.844 56.602 5.867 1.00 14.78 ? 101 CYS B O 1 ATOM 1757 C CB . CYS B 1 101 ? 5.422 56.313 8.066 0.81 12.04 ? 101 CYS B CB 1 ATOM 1758 S SG . CYS B 1 101 ? 5.323 57.952 7.570 0.81 12.33 ? 101 CYS B SG 1 ATOM 1759 N N . ALA B 1 102 ? 6.653 54.742 5.536 1.00 12.70 ? 102 ALA B N 1 ATOM 1760 C CA . ALA B 1 102 ? 6.913 54.684 4.092 1.00 12.49 ? 102 ALA B CA 1 ATOM 1761 C C . ALA B 1 102 ? 5.635 54.151 3.415 1.00 13.85 ? 102 ALA B C 1 ATOM 1762 O O . ALA B 1 102 ? 4.783 53.522 4.078 1.00 12.64 ? 102 ALA B O 1 ATOM 1763 C CB . ALA B 1 102 ? 8.094 53.749 3.791 1.00 12.39 ? 102 ALA B CB 1 ATOM 1764 N N . ALA B 1 103 ? 5.528 54.393 2.112 1.00 13.19 ? 103 ALA B N 1 ATOM 1765 C CA . ALA B 1 103 ? 4.369 53.995 1.337 1.00 15.73 ? 103 ALA B CA 1 ATOM 1766 C C . ALA B 1 103 ? 4.747 53.281 0.080 1.00 16.42 ? 103 ALA B C 1 ATOM 1767 O O . ALA B 1 103 ? 5.749 53.611 -0.555 1.00 16.94 ? 103 ALA B O 1 ATOM 1768 C CB . ALA B 1 103 ? 3.526 55.238 0.952 1.00 15.24 ? 103 ALA B CB 1 ATOM 1769 N N . LYS B 1 104 ? 3.957 52.277 -0.266 1.00 17.36 ? 104 LYS B N 1 ATOM 1770 C CA . LYS B 1 104 ? 4.123 51.553 -1.508 1.00 20.32 ? 104 LYS B CA 1 ATOM 1771 C C . LYS B 1 104 ? 2.724 51.233 -2.068 1.00 23.02 ? 104 LYS B C 1 ATOM 1772 O O . LYS B 1 104 ? 1.697 51.300 -1.328 1.00 21.32 ? 104 LYS B O 1 ATOM 1773 C CB . LYS B 1 104 ? 4.926 50.268 -1.312 1.00 20.77 ? 104 LYS B CB 1 ATOM 1774 C CG . LYS B 1 104 ? 4.374 49.323 -0.306 1.00 22.01 ? 104 LYS B CG 1 ATOM 1775 C CD . LYS B 1 104 ? 5.209 48.047 -0.348 1.00 25.58 ? 104 LYS B CD 1 ATOM 1776 C CE . LYS B 1 104 ? 4.666 46.998 0.599 1.00 26.01 ? 104 LYS B CE 1 ATOM 1777 N NZ . LYS B 1 104 ? 5.251 45.671 0.287 1.00 28.67 ? 104 LYS B NZ 1 ATOM 1778 N N . THR B 1 105 ? 2.697 50.858 -3.353 1.00 25.12 ? 105 THR B N 1 ATOM 1779 C CA . THR B 1 105 ? 1.466 50.560 -4.074 1.00 29.52 ? 105 THR B CA 1 ATOM 1780 C C . THR B 1 105 ? 1.258 49.101 -4.481 1.00 32.44 ? 105 THR B C 1 ATOM 1781 O O . THR B 1 105 ? 0.345 48.803 -5.250 1.00 32.80 ? 105 THR B O 1 ATOM 1782 C CB . THR B 1 105 ? 1.382 51.402 -5.340 1.00 29.71 ? 105 THR B CB 1 ATOM 1783 O OG1 . THR B 1 105 ? 2.500 51.101 -6.174 1.00 30.87 ? 105 THR B OG1 1 ATOM 1784 C CG2 . THR B 1 105 ? 1.446 52.879 -5.004 1.00 31.37 ? 105 THR B CG2 1 ATOM 1785 N N . THR B 1 106 ? 2.107 48.196 -4.001 1.00 35.24 ? 106 THR B N 1 ATOM 1786 C CA . THR B 1 106 ? 1.965 46.771 -4.322 1.00 38.95 ? 106 THR B CA 1 ATOM 1787 C C . THR B 1 106 ? 2.017 46.009 -3.023 1.00 40.20 ? 106 THR B C 1 ATOM 1788 O O . THR B 1 106 ? 2.400 46.544 -2.002 1.00 39.86 ? 106 THR B O 1 ATOM 1789 C CB . THR B 1 106 ? 3.111 46.239 -5.203 1.00 39.61 ? 106 THR B CB 1 ATOM 1790 O OG1 . THR B 1 106 ? 4.317 46.921 -4.852 1.00 41.17 ? 106 THR B OG1 1 ATOM 1791 C CG2 . THR B 1 106 ? 2.820 46.456 -6.679 1.00 41.18 ? 106 THR B CG2 1 ATOM 1792 N N . THR B 1 107 ? 1.649 44.740 -3.048 1.00 42.31 ? 107 THR B N 1 ATOM 1793 C CA . THR B 1 107 ? 1.692 43.971 -1.813 1.00 44.81 ? 107 THR B CA 1 ATOM 1794 C C . THR B 1 107 ? 2.864 43.004 -1.845 1.00 45.46 ? 107 THR B C 1 ATOM 1795 O O . THR B 1 107 ? 3.142 42.311 -0.864 1.00 45.81 ? 107 THR B O 1 ATOM 1796 C CB . THR B 1 107 ? 0.379 43.146 -1.588 1.00 45.98 ? 107 THR B CB 1 ATOM 1797 O OG1 . THR B 1 107 ? 0.098 42.389 -2.774 1.00 46.94 ? 107 THR B OG1 1 ATOM 1798 C CG2 . THR B 1 107 ? -0.801 44.068 -1.287 1.00 46.06 ? 107 THR B CG2 1 ATOM 1799 N N . TRP B 1 108 ? 3.541 42.963 -2.976 1.00 46.49 ? 108 TRP B N 1 ATOM 1800 C CA . TRP B 1 108 ? 4.646 42.064 -3.140 1.00 48.09 ? 108 TRP B CA 1 ATOM 1801 C C . TRP B 1 108 ? 5.974 42.523 -2.604 1.00 49.07 ? 108 TRP B C 1 ATOM 1802 O O . TRP B 1 108 ? 6.187 43.714 -2.292 1.00 49.38 ? 108 TRP B O 1 ATOM 1803 C CB . TRP B 1 108 ? 4.913 41.757 -4.612 1.00 47.64 ? 108 TRP B CB 1 ATOM 1804 C CG . TRP B 1 108 ? 3.914 40.899 -5.256 1.00 48.02 ? 108 TRP B CG 1 ATOM 1805 C CD1 . TRP B 1 108 ? 2.853 41.322 -6.033 1.00 48.07 ? 108 TRP B CD1 1 ATOM 1806 C CD2 . TRP B 1 108 ? 3.794 39.496 -5.158 1.00 47.76 ? 108 TRP B CD2 1 ATOM 1807 N NE1 . TRP B 1 108 ? 2.087 40.248 -6.407 1.00 48.22 ? 108 TRP B NE1 1 ATOM 1808 C CE2 . TRP B 1 108 ? 2.654 39.097 -5.877 1.00 47.51 ? 108 TRP B CE2 1 ATOM 1809 C CE3 . TRP B 1 108 ? 4.543 38.493 -4.515 1.00 47.44 ? 108 TRP B CE3 1 ATOM 1810 C CZ2 . TRP B 1 108 ? 2.236 37.775 -5.989 1.00 47.18 ? 108 TRP B CZ2 1 ATOM 1811 C CZ3 . TRP B 1 108 ? 4.138 37.182 -4.617 1.00 47.06 ? 108 TRP B CZ3 1 ATOM 1812 C CH2 . TRP B 1 108 ? 2.995 36.833 -5.352 1.00 47.22 ? 108 TRP B CH2 1 ATOM 1813 N N . GLY B 1 109 ? 6.882 41.561 -2.571 1.00 49.84 ? 109 GLY B N 1 ATOM 1814 C CA . GLY B 1 109 ? 8.275 41.820 -2.218 1.00 50.31 ? 109 GLY B CA 1 ATOM 1815 C C . GLY B 1 109 ? 8.429 41.379 -0.845 1.00 50.72 ? 109 GLY B C 1 ATOM 1816 O O . GLY B 1 109 ? 9.223 40.409 -0.561 1.00 52.14 ? 109 GLY B O 1 ATOM 1817 N N . GLY B 1 110 ? 7.858 42.264 -0.059 1.00 50.07 ? 110 GLY B N 1 ATOM 1818 C CA . GLY B 1 110 ? 7.725 42.072 1.359 1.00 50.08 ? 110 GLY B CA 1 ATOM 1819 C C . GLY B 1 110 ? 8.720 41.990 2.431 1.00 50.31 ? 110 GLY B C 1 ATOM 1820 O O . GLY B 1 110 ? 9.570 41.094 2.360 1.00 52.04 ? 110 GLY B O 1 ATOM 1821 N N . ASN B 1 111 ? 8.499 42.936 3.363 1.00 48.70 ? 111 ASN B N 1 ATOM 1822 C CA . ASN B 1 111 ? 9.114 43.309 4.664 1.00 47.51 ? 111 ASN B CA 1 ATOM 1823 C C . ASN B 1 111 ? 10.500 43.748 4.964 1.00 45.78 ? 111 ASN B C 1 ATOM 1824 O O . ASN B 1 111 ? 11.069 43.397 6.023 1.00 45.45 ? 111 ASN B O 1 ATOM 1825 C CB . ASN B 1 111 ? 8.742 42.367 5.761 1.00 48.69 ? 111 ASN B CB 1 ATOM 1826 C CG . ASN B 1 111 ? 7.358 41.962 5.672 1.00 50.46 ? 111 ASN B CG 1 ATOM 1827 O OD1 . ASN B 1 111 ? 6.502 42.737 5.257 1.00 50.92 ? 111 ASN B OD1 1 ATOM 1828 N ND2 . ASN B 1 111 ? 7.092 40.716 6.043 1.00 51.20 ? 111 ASN B ND2 1 ATOM 1829 N N . ASP B 1 112 ? 11.047 44.453 4.011 1.00 43.44 ? 112 ASP B N 1 ATOM 1830 C CA . ASP B 1 112 ? 12.304 44.988 4.109 1.00 41.49 ? 112 ASP B CA 1 ATOM 1831 C C . ASP B 1 112 ? 12.189 46.291 3.519 1.00 38.79 ? 112 ASP B C 1 ATOM 1832 O O . ASP B 1 112 ? 11.257 46.615 2.721 1.00 37.81 ? 112 ASP B O 1 ATOM 1833 C CB . ASP B 1 112 ? 13.384 44.051 3.424 1.00 42.41 ? 112 ASP B CB 1 ATOM 1834 C CG . ASP B 1 112 ? 12.947 43.498 2.172 1.00 44.26 ? 112 ASP B CG 1 ATOM 1835 O OD1 . ASP B 1 112 ? 12.905 42.256 2.107 1.00 45.02 ? 112 ASP B OD1 1 ATOM 1836 O OD2 . ASP B 1 112 ? 12.660 44.301 1.264 1.00 46.08 ? 112 ASP B OD2 1 ATOM 1837 N N . PRO B 1 113 ? 12.998 47.161 4.001 1.00 36.63 ? 113 PRO B N 1 ATOM 1838 C CA . PRO B 1 113 ? 12.953 48.497 3.481 1.00 35.42 ? 113 PRO B CA 1 ATOM 1839 C C . PRO B 1 113 ? 13.300 48.708 2.033 1.00 34.73 ? 113 PRO B C 1 ATOM 1840 O O . PRO B 1 113 ? 13.091 49.781 1.529 1.00 33.66 ? 113 PRO B O 1 ATOM 1841 C CB . PRO B 1 113 ? 13.957 49.243 4.348 1.00 35.54 ? 113 PRO B CB 1 ATOM 1842 C CG . PRO B 1 113 ? 14.758 48.217 5.082 1.00 36.20 ? 113 PRO B CG 1 ATOM 1843 C CD . PRO B 1 113 ? 14.191 46.872 4.820 1.00 36.54 ? 113 PRO B CD 1 ATOM 1844 N N . ASN B 1 114 ? 13.760 47.652 1.408 1.00 34.64 ? 114 ASN B N 1 ATOM 1845 C CA . ASN B 1 114 ? 14.200 47.719 0.042 1.00 34.81 ? 114 ASN B CA 1 ATOM 1846 C C . ASN B 1 114 ? 13.249 48.199 -1.025 1.00 34.49 ? 114 ASN B C 1 ATOM 1847 O O . ASN B 1 114 ? 13.637 48.970 -1.885 1.00 35.01 ? 114 ASN B O 1 ATOM 1848 C CB . ASN B 1 114 ? 14.797 46.370 -0.399 1.00 36.29 ? 114 ASN B CB 1 ATOM 1849 C CG . ASN B 1 114 ? 15.962 45.945 0.485 1.00 38.29 ? 114 ASN B CG 1 ATOM 1850 O OD1 . ASN B 1 114 ? 17.086 46.434 0.333 1.00 40.63 ? 114 ASN B OD1 1 ATOM 1851 N ND2 . ASN B 1 114 ? 15.692 45.053 1.438 1.00 39.06 ? 114 ASN B ND2 1 ATOM 1852 N N . ASN B 1 115 ? 11.997 47.793 -0.984 1.00 33.48 ? 115 ASN B N 1 ATOM 1853 C CA . ASN B 1 115 ? 11.151 48.229 -2.064 1.00 32.41 ? 115 ASN B CA 1 ATOM 1854 C C . ASN B 1 115 ? 9.914 49.068 -1.748 1.00 30.80 ? 115 ASN B C 1 ATOM 1855 O O . ASN B 1 115 ? 8.791 48.674 -2.061 1.00 30.18 ? 115 ASN B O 1 ATOM 1856 C CB . ASN B 1 115 ? 10.781 47.011 -2.897 1.00 34.77 ? 115 ASN B CB 1 ATOM 1857 C CG . ASN B 1 115 ? 12.018 46.168 -3.277 1.00 37.92 ? 115 ASN B CG 1 ATOM 1858 O OD1 . ASN B 1 115 ? 12.978 46.668 -3.915 1.00 38.55 ? 115 ASN B OD1 1 ATOM 1859 N ND2 . ASN B 1 115 ? 12.002 44.885 -2.882 1.00 38.76 ? 115 ASN B ND2 1 ATOM 1860 N N . TRP B 1 116 ? 10.149 50.232 -1.148 1.00 28.64 ? 116 TRP B N 1 ATOM 1861 C CA . TRP B 1 116 ? 9.095 51.177 -0.808 1.00 26.64 ? 116 TRP B CA 1 ATOM 1862 C C . TRP B 1 116 ? 9.292 52.453 -1.636 1.00 26.70 ? 116 TRP B C 1 ATOM 1863 O O . TRP B 1 116 ? 10.399 53.023 -1.698 1.00 25.91 ? 116 TRP B O 1 ATOM 1864 C CB . TRP B 1 116 ? 9.125 51.479 0.697 1.00 25.90 ? 116 TRP B CB 1 ATOM 1865 C CG . TRP B 1 116 ? 8.794 50.297 1.533 1.00 24.25 ? 116 TRP B CG 1 ATOM 1866 C CD1 . TRP B 1 116 ? 9.589 49.196 1.764 1.00 24.67 ? 116 TRP B CD1 1 ATOM 1867 C CD2 . TRP B 1 116 ? 7.529 50.026 2.178 1.00 24.37 ? 116 TRP B CD2 1 ATOM 1868 N NE1 . TRP B 1 116 ? 8.885 48.259 2.504 1.00 25.29 ? 116 TRP B NE1 1 ATOM 1869 C CE2 . TRP B 1 116 ? 7.626 48.741 2.765 1.00 23.70 ? 116 TRP B CE2 1 ATOM 1870 C CE3 . TRP B 1 116 ? 6.328 50.746 2.310 1.00 24.42 ? 116 TRP B CE3 1 ATOM 1871 C CZ2 . TRP B 1 116 ? 6.565 48.156 3.467 1.00 23.85 ? 116 TRP B CZ2 1 ATOM 1872 C CZ3 . TRP B 1 116 ? 5.260 50.157 3.020 1.00 24.06 ? 116 TRP B CZ3 1 ATOM 1873 C CH2 . TRP B 1 116 ? 5.395 48.874 3.587 1.00 23.05 ? 116 TRP B CH2 1 ATOM 1874 N N . ASN B 1 117 ? 8.210 52.866 -2.295 1.00 25.83 ? 117 ASN B N 1 ATOM 1875 C CA . ASN B 1 117 ? 8.175 54.020 -3.182 1.00 25.00 ? 117 ASN B CA 1 ATOM 1876 C C . ASN B 1 117 ? 8.448 55.363 -2.555 1.00 24.07 ? 117 ASN B C 1 ATOM 1877 O O . ASN B 1 117 ? 9.140 56.176 -3.140 1.00 23.54 ? 117 ASN B O 1 ATOM 1878 C CB . ASN B 1 117 ? 6.802 54.132 -3.871 1.00 26.73 ? 117 ASN B CB 1 ATOM 1879 C CG . ASN B 1 117 ? 6.484 52.958 -4.766 1.00 28.63 ? 117 ASN B CG 1 ATOM 1880 O OD1 . ASN B 1 117 ? 6.608 53.046 -5.990 1.00 30.40 ? 117 ASN B OD1 1 ATOM 1881 N ND2 . ASN B 1 117 ? 6.066 51.844 -4.163 1.00 29.69 ? 117 ASN B ND2 1 ATOM 1882 N N . TYR B 1 118 ? 7.881 55.618 -1.377 1.00 23.05 ? 118 TYR B N 1 ATOM 1883 C CA . TYR B 1 118 ? 8.026 56.927 -0.769 1.00 21.82 ? 118 TYR B CA 1 ATOM 1884 C C . TYR B 1 118 ? 8.317 56.798 0.714 1.00 21.78 ? 118 TYR B C 1 ATOM 1885 O O . TYR B 1 118 ? 7.737 55.924 1.388 1.00 21.18 ? 118 TYR B O 1 ATOM 1886 C CB . TYR B 1 118 ? 6.733 57.739 -1.025 1.00 22.86 ? 118 TYR B CB 1 ATOM 1887 C CG . TYR B 1 118 ? 6.339 57.803 -2.497 1.00 24.39 ? 118 TYR B CG 1 ATOM 1888 C CD1 . TYR B 1 118 ? 5.385 56.950 -3.042 1.00 25.66 ? 118 TYR B CD1 1 ATOM 1889 C CD2 . TYR B 1 118 ? 6.937 58.729 -3.350 1.00 26.86 ? 118 TYR B CD2 1 ATOM 1890 C CE1 . TYR B 1 118 ? 5.033 57.029 -4.401 1.00 25.83 ? 118 TYR B CE1 1 ATOM 1891 C CE2 . TYR B 1 118 ? 6.596 58.817 -4.698 1.00 26.93 ? 118 TYR B CE2 1 ATOM 1892 C CZ . TYR B 1 118 ? 5.646 57.974 -5.219 1.00 27.51 ? 118 TYR B CZ 1 ATOM 1893 O OH . TYR B 1 118 ? 5.295 58.115 -6.553 1.00 28.41 ? 118 TYR B OH 1 ATOM 1894 N N . TRP B 1 119 ? 9.183 57.691 1.211 1.00 19.56 ? 119 TRP B N 1 ATOM 1895 C CA . TRP B 1 119 ? 9.636 57.706 2.601 1.00 18.85 ? 119 TRP B CA 1 ATOM 1896 C C . TRP B 1 119 ? 9.431 59.036 3.301 1.00 19.02 ? 119 TRP B C 1 ATOM 1897 O O . TRP B 1 119 ? 9.449 60.084 2.674 1.00 19.79 ? 119 TRP B O 1 ATOM 1898 C CB . TRP B 1 119 ? 11.146 57.371 2.669 1.00 18.34 ? 119 TRP B CB 1 ATOM 1899 C CG . TRP B 1 119 ? 11.441 55.970 2.333 1.00 16.48 ? 119 TRP B CG 1 ATOM 1900 C CD1 . TRP B 1 119 ? 11.503 55.422 1.099 1.00 16.67 ? 119 TRP B CD1 1 ATOM 1901 C CD2 . TRP B 1 119 ? 11.576 54.906 3.249 1.00 16.36 ? 119 TRP B CD2 1 ATOM 1902 N NE1 . TRP B 1 119 ? 11.657 54.070 1.186 1.00 15.53 ? 119 TRP B NE1 1 ATOM 1903 C CE2 . TRP B 1 119 ? 11.707 53.721 2.518 1.00 14.74 ? 119 TRP B CE2 1 ATOM 1904 C CE3 . TRP B 1 119 ? 11.591 54.831 4.657 1.00 16.51 ? 119 TRP B CE3 1 ATOM 1905 C CZ2 . TRP B 1 119 ? 11.852 52.472 3.098 1.00 15.39 ? 119 TRP B CZ2 1 ATOM 1906 C CZ3 . TRP B 1 119 ? 11.725 53.603 5.251 1.00 15.81 ? 119 TRP B CZ3 1 ATOM 1907 C CH2 . TRP B 1 119 ? 11.859 52.429 4.469 1.00 16.93 ? 119 TRP B CH2 1 ATOM 1908 N N . GLY B 1 120 ? 9.233 58.992 4.610 1.00 19.40 ? 120 GLY B N 1 ATOM 1909 C CA . GLY B 1 120 ? 9.079 60.211 5.372 1.00 20.69 ? 120 GLY B CA 1 ATOM 1910 C C . GLY B 1 120 ? 10.466 60.680 5.804 1.00 23.34 ? 120 GLY B C 1 ATOM 1911 O O . GLY B 1 120 ? 11.466 60.103 5.413 1.00 24.07 ? 120 GLY B O 1 ATOM 1912 N N . GLN B 1 121 ? 10.511 61.701 6.640 1.00 25.15 ? 121 GLN B N 1 ATOM 1913 C CA . GLN B 1 121 ? 11.746 62.296 7.126 1.00 27.43 ? 121 GLN B CA 1 ATOM 1914 C C . GLN B 1 121 ? 12.305 61.677 8.422 1.00 27.21 ? 121 GLN B C 1 ATOM 1915 O O . GLN B 1 121 ? 13.498 61.826 8.740 1.00 26.69 ? 121 GLN B O 1 ATOM 1916 C CB . GLN B 1 121 ? 11.469 63.769 7.337 1.00 31.02 ? 121 GLN B CB 1 ATOM 1917 C CG . GLN B 1 121 ? 12.667 64.587 7.691 1.00 37.21 ? 121 GLN B CG 1 ATOM 1918 C CD . GLN B 1 121 ? 12.298 66.005 8.133 1.00 40.10 ? 121 GLN B CD 1 ATOM 1919 O OE1 . GLN B 1 121 ? 11.735 66.208 9.233 1.00 42.13 ? 121 GLN B OE1 1 ATOM 1920 N NE2 . GLN B 1 121 ? 12.610 66.995 7.281 1.00 40.97 ? 121 GLN B NE2 1 ATOM 1921 N N . GLY B 1 122 ? 11.441 60.980 9.162 1.00 25.42 ? 122 GLY B N 1 ATOM 1922 C CA . GLY B 1 122 ? 11.836 60.352 10.410 1.00 22.98 ? 122 GLY B CA 1 ATOM 1923 C C . GLY B 1 122 ? 11.559 61.235 11.613 1.00 21.66 ? 122 GLY B C 1 ATOM 1924 O O . GLY B 1 122 ? 11.626 62.447 11.524 1.00 21.74 ? 122 GLY B O 1 ATOM 1925 N N . THR B 1 123 ? 11.216 60.621 12.734 1.00 21.15 ? 123 THR B N 1 ATOM 1926 C CA . THR B 1 123 ? 10.955 61.366 13.952 1.00 21.88 ? 123 THR B CA 1 ATOM 1927 C C . THR B 1 123 ? 11.716 60.647 15.060 1.00 21.90 ? 123 THR B C 1 ATOM 1928 O O . THR B 1 123 ? 11.647 59.428 15.162 1.00 21.61 ? 123 THR B O 1 ATOM 1929 C CB . THR B 1 123 ? 9.444 61.400 14.278 1.00 21.93 ? 123 THR B CB 1 ATOM 1930 O OG1 . THR B 1 123 ? 9.217 62.115 15.494 1.00 23.88 ? 123 THR B OG1 1 ATOM 1931 C CG2 . THR B 1 123 ? 8.907 60.021 14.436 1.00 21.28 ? 123 THR B CG2 1 ATOM 1932 N N . GLN B 1 124 ? 12.445 61.398 15.880 1.00 22.98 ? 124 GLN B N 1 ATOM 1933 C CA . GLN B 1 124 ? 13.235 60.809 16.950 1.00 24.24 ? 124 GLN B CA 1 ATOM 1934 C C . GLN B 1 124 ? 12.455 60.426 18.184 1.00 23.64 ? 124 GLN B C 1 ATOM 1935 O O . GLN B 1 124 ? 11.671 61.203 18.713 1.00 23.98 ? 124 GLN B O 1 ATOM 1936 C CB . GLN B 1 124 ? 14.358 61.754 17.382 1.00 26.36 ? 124 GLN B CB 1 ATOM 1937 C CG . GLN B 1 124 ? 15.167 61.187 18.557 1.00 30.14 ? 124 GLN B CG 1 ATOM 1938 C CD . GLN B 1 124 ? 16.180 60.126 18.135 1.00 32.05 ? 124 GLN B CD 1 ATOM 1939 O OE1 . GLN B 1 124 ? 16.403 59.132 18.845 1.00 33.30 ? 124 GLN B OE1 1 ATOM 1940 N NE2 . GLN B 1 124 ? 16.813 60.339 16.987 1.00 33.56 ? 124 GLN B NE2 1 ATOM 1941 N N . VAL B 1 125 ? 12.673 59.214 18.648 1.00 22.75 ? 125 VAL B N 1 ATOM 1942 C CA . VAL B 1 125 ? 12.012 58.785 19.852 1.00 23.84 ? 125 VAL B CA 1 ATOM 1943 C C . VAL B 1 125 ? 13.118 58.370 20.794 1.00 24.49 ? 125 VAL B C 1 ATOM 1944 O O . VAL B 1 125 ? 13.932 57.528 20.462 1.00 24.36 ? 125 VAL B O 1 ATOM 1945 C CB . VAL B 1 125 ? 11.057 57.604 19.594 1.00 22.28 ? 125 VAL B CB 1 ATOM 1946 C CG1 . VAL B 1 125 ? 10.791 56.872 20.871 1.00 22.43 ? 125 VAL B CG1 1 ATOM 1947 C CG2 . VAL B 1 125 ? 9.753 58.121 19.008 1.00 22.39 ? 125 VAL B CG2 1 ATOM 1948 N N . THR B 1 126 ? 13.168 58.982 21.962 1.00 26.15 ? 126 THR B N 1 ATOM 1949 C CA . THR B 1 126 ? 14.197 58.606 22.910 1.00 27.26 ? 126 THR B CA 1 ATOM 1950 C C . THR B 1 126 ? 13.554 58.089 24.155 1.00 28.24 ? 126 THR B C 1 ATOM 1951 O O . THR B 1 126 ? 12.732 58.780 24.785 1.00 28.49 ? 126 THR B O 1 ATOM 1952 C CB . THR B 1 126 ? 15.082 59.777 23.272 1.00 27.95 ? 126 THR B CB 1 ATOM 1953 O OG1 . THR B 1 126 ? 15.652 60.320 22.081 1.00 27.36 ? 126 THR B OG1 1 ATOM 1954 C CG2 . THR B 1 126 ? 16.205 59.298 24.186 1.00 28.36 ? 126 THR B CG2 1 ATOM 1955 N N . VAL B 1 127 ? 13.903 56.862 24.511 1.00 29.14 ? 127 VAL B N 1 ATOM 1956 C CA . VAL B 1 127 ? 13.337 56.277 25.709 1.00 31.38 ? 127 VAL B CA 1 ATOM 1957 C C . VAL B 1 127 ? 14.418 56.094 26.769 1.00 34.22 ? 127 VAL B C 1 ATOM 1958 O O . VAL B 1 127 ? 15.387 55.359 26.573 1.00 34.38 ? 127 VAL B O 1 ATOM 1959 C CB . VAL B 1 127 ? 12.714 54.884 25.485 1.00 30.82 ? 127 VAL B CB 1 ATOM 1960 C CG1 . VAL B 1 127 ? 11.925 54.520 26.705 1.00 29.92 ? 127 VAL B CG1 1 ATOM 1961 C CG2 . VAL B 1 127 ? 11.813 54.874 24.241 1.00 29.90 ? 127 VAL B CG2 1 ATOM 1962 N N . SER B 1 128 ? 14.234 56.738 27.905 1.00 36.08 ? 128 SER B N 1 ATOM 1963 C CA . SER B 1 128 ? 15.207 56.598 28.957 1.00 39.17 ? 128 SER B CA 1 ATOM 1964 C C . SER B 1 128 ? 14.635 55.987 30.209 1.00 40.84 ? 128 SER B C 1 ATOM 1965 O O . SER B 1 128 ? 13.414 55.905 30.378 1.00 41.43 ? 128 SER B O 1 ATOM 1966 C CB . SER B 1 128 ? 15.753 57.971 29.319 1.00 39.12 ? 128 SER B CB 1 ATOM 1967 O OG . SER B 1 128 ? 14.744 58.705 30.011 1.00 39.34 ? 128 SER B OG 1 ATOM 1968 N N . SER B 1 129 ? 15.521 55.507 31.074 1.00 42.45 ? 129 SER B N 1 ATOM 1969 C CA . SER B 1 129 ? 15.067 55.054 32.370 1.00 44.07 ? 129 SER B CA 1 ATOM 1970 C C . SER B 1 129 ? 15.751 56.198 33.105 1.00 45.00 ? 129 SER B C 1 ATOM 1971 O O . SER B 1 129 ? 16.075 56.055 34.289 1.00 45.32 ? 129 SER B O 1 ATOM 1972 C CB . SER B 1 129 ? 15.688 53.732 32.779 1.00 44.63 ? 129 SER B CB 1 ATOM 1973 O OG . SER B 1 129 ? 16.101 52.981 31.667 1.00 45.73 ? 129 SER B OG 1 ATOM 1974 O OXT . SER B 1 129 ? 16.007 57.234 32.429 1.00 45.78 ? 129 SER B OXT 1 HETATM 1975 O O . HOH C 2 . ? 8.280 33.725 1.254 1.00 25.41 ? 130 HOH A O 1 HETATM 1976 O O . HOH C 2 . ? 10.131 31.501 -1.832 1.00 21.05 ? 131 HOH A O 1 HETATM 1977 O O . HOH C 2 . ? 7.886 33.570 -1.864 1.00 23.30 ? 132 HOH A O 1 HETATM 1978 O O . HOH C 2 . ? 8.681 35.945 -1.819 1.00 33.52 ? 133 HOH A O 1 HETATM 1979 O O . HOH C 2 . ? 2.675 24.091 27.332 1.00 19.21 ? 134 HOH A O 1 HETATM 1980 O O . HOH C 2 . ? -7.648 24.506 1.699 1.00 19.22 ? 135 HOH A O 1 HETATM 1981 O O . HOH C 2 . ? 17.571 21.614 13.527 1.00 26.87 ? 136 HOH A O 1 HETATM 1982 O O . HOH C 2 . ? 15.788 20.892 15.575 1.00 28.13 ? 137 HOH A O 1 HETATM 1983 O O . HOH C 2 . ? -3.494 18.345 0.013 1.00 23.25 ? 138 HOH A O 1 HETATM 1984 O O . HOH C 2 . ? -2.803 25.185 15.555 1.00 34.06 ? 139 HOH A O 1 HETATM 1985 O O . HOH C 2 . ? -2.611 23.920 22.904 1.00 23.25 ? 140 HOH A O 1 HETATM 1986 O O . HOH C 2 . ? 18.590 29.905 17.104 1.00 47.17 ? 141 HOH A O 1 HETATM 1987 O O . HOH C 2 . ? 12.989 23.181 -2.075 1.00 22.90 ? 142 HOH A O 1 HETATM 1988 O O . HOH C 2 . ? 13.562 16.580 7.841 1.00 39.07 ? 143 HOH A O 1 HETATM 1989 O O . HOH C 2 . ? 11.937 14.907 11.026 1.00 31.66 ? 144 HOH A O 1 HETATM 1990 O O . HOH C 2 . ? 2.674 29.162 27.908 1.00 29.02 ? 145 HOH A O 1 HETATM 1991 O O . HOH C 2 . ? -7.377 23.440 10.750 1.00 25.65 ? 146 HOH A O 1 HETATM 1992 O O . HOH C 2 . ? 19.906 21.624 6.542 1.00 33.71 ? 147 HOH A O 1 HETATM 1993 O O . HOH C 2 . ? 4.112 22.677 30.835 1.00 33.88 ? 148 HOH A O 1 HETATM 1994 O O . HOH C 2 . ? 11.792 36.002 3.620 1.00 45.21 ? 149 HOH A O 1 HETATM 1995 O O . HOH C 2 . ? 0.847 33.587 16.058 1.00 28.48 ? 150 HOH A O 1 HETATM 1996 O O . HOH C 2 . ? -3.843 17.562 14.059 1.00 34.76 ? 151 HOH A O 1 HETATM 1997 O O . HOH C 2 . ? 3.874 27.338 31.622 1.00 46.23 ? 152 HOH A O 1 HETATM 1998 O O . HOH C 2 . ? 7.909 16.972 0.708 1.00 49.00 ? 153 HOH A O 1 HETATM 1999 O O . HOH C 2 . ? 16.364 32.724 8.486 1.00 51.44 ? 154 HOH A O 1 HETATM 2000 O O . HOH C 2 . ? 6.619 20.757 -5.438 1.00 43.67 ? 155 HOH A O 1 HETATM 2001 O O . HOH C 2 . ? 2.927 37.478 3.769 1.00 49.84 ? 156 HOH A O 1 HETATM 2002 O O . HOH C 2 . ? -2.204 38.286 4.054 1.00 50.83 ? 157 HOH A O 1 HETATM 2003 O O . HOH C 2 . ? -9.221 27.361 6.900 1.00 40.21 ? 158 HOH A O 1 HETATM 2004 O O . HOH C 2 . ? 15.733 22.817 17.750 1.00 37.98 ? 159 HOH A O 1 HETATM 2005 O O . HOH C 2 . ? 4.883 16.681 3.073 1.00 44.37 ? 160 HOH A O 1 HETATM 2006 O O . HOH C 2 . ? 0.917 32.249 21.634 1.00 38.61 ? 161 HOH A O 1 HETATM 2007 O O . HOH C 2 . ? -13.366 16.798 10.606 1.00 43.11 ? 162 HOH A O 1 HETATM 2008 O O . HOH C 2 . ? 13.457 32.864 2.014 1.00 47.04 ? 163 HOH A O 1 HETATM 2009 O O . HOH C 2 . ? 0.144 16.372 17.012 1.00 43.02 ? 164 HOH A O 1 HETATM 2010 O O . HOH C 2 . ? 0.207 19.213 23.185 1.00 44.49 ? 165 HOH A O 1 HETATM 2011 O O . HOH C 2 . ? 10.903 38.453 19.318 1.00 53.83 ? 166 HOH A O 1 HETATM 2012 O O . HOH C 2 . ? 2.816 36.029 10.194 1.00 42.80 ? 167 HOH A O 1 HETATM 2013 O O . HOH C 2 . ? 7.085 27.306 32.176 1.00 38.31 ? 168 HOH A O 1 HETATM 2014 O O . HOH C 2 . ? -5.032 13.899 9.191 1.00 44.30 ? 169 HOH A O 1 HETATM 2015 O O . HOH C 2 . ? 6.340 37.639 26.054 1.00 47.87 ? 170 HOH A O 1 HETATM 2016 O O . HOH C 2 . ? 16.480 32.899 30.214 1.00 46.74 ? 171 HOH A O 1 HETATM 2017 O O . HOH C 2 . ? 10.678 38.839 4.951 1.00 47.57 ? 172 HOH A O 1 HETATM 2018 O O . HOH C 2 . ? 11.488 13.309 14.210 1.00 44.37 ? 173 HOH A O 1 HETATM 2019 O O . HOH C 2 . ? 19.259 16.905 5.508 1.00 43.99 ? 174 HOH A O 1 HETATM 2020 O O . HOH C 2 . ? 20.160 28.976 22.467 1.00 47.63 ? 175 HOH A O 1 HETATM 2021 O O . HOH C 2 . ? 16.677 16.667 7.514 1.00 45.84 ? 176 HOH A O 1 HETATM 2022 O O . HOH C 2 . ? -6.264 16.555 10.862 1.00 47.37 ? 177 HOH A O 1 HETATM 2023 O O . HOH C 2 . ? 8.977 18.417 -1.230 1.00 44.06 ? 178 HOH A O 1 HETATM 2024 O O . HOH C 2 . ? -2.060 26.942 -5.659 1.00 37.61 ? 179 HOH A O 1 HETATM 2025 O O . HOH C 2 . ? -2.966 35.920 10.603 1.00 47.11 ? 180 HOH A O 1 HETATM 2026 O O . HOH C 2 . ? 3.255 33.568 19.456 1.00 42.06 ? 181 HOH A O 1 HETATM 2027 O O . HOH C 2 . ? -1.451 39.128 -6.393 1.00 48.18 ? 182 HOH A O 1 HETATM 2028 O O . HOH C 2 . ? -11.082 30.515 12.686 1.00 47.81 ? 183 HOH A O 1 HETATM 2029 O O . HOH C 2 . ? 9.443 21.074 29.696 1.00 44.13 ? 184 HOH A O 1 HETATM 2030 O O . HOH C 2 . ? -1.812 39.806 -0.538 1.00 48.33 ? 185 HOH A O 1 HETATM 2031 O O . HOH C 2 . ? -1.160 16.432 -6.153 1.00 46.10 ? 186 HOH A O 1 HETATM 2032 O O . HOH C 2 . ? 19.790 21.046 17.996 1.00 46.30 ? 187 HOH A O 1 HETATM 2033 O O . HOH C 2 . ? 18.645 32.154 25.991 1.00 46.76 ? 188 HOH A O 1 HETATM 2034 O O . HOH C 2 . ? 15.429 36.940 17.954 1.00 39.77 ? 189 HOH A O 1 HETATM 2035 O O . HOH C 2 . ? 25.148 18.965 12.943 1.00 48.73 ? 190 HOH A O 1 HETATM 2036 O O . HOH C 2 . ? 0.017 29.290 27.187 1.00 49.47 ? 191 HOH A O 1 HETATM 2037 O O . HOH C 2 . ? 18.068 27.523 24.540 1.00 44.45 ? 192 HOH A O 1 HETATM 2038 O O . HOH C 2 . ? 10.363 36.083 28.080 1.00 47.06 ? 193 HOH A O 1 HETATM 2039 O O . HOH C 2 . ? 19.883 19.389 22.315 1.00 37.84 ? 194 HOH A O 1 HETATM 2040 O O . HOH C 2 . ? -9.724 37.833 14.638 1.00 48.02 ? 195 HOH A O 1 HETATM 2041 O O . HOH C 2 . ? -2.784 13.810 -3.888 1.00 47.57 ? 196 HOH A O 1 HETATM 2042 O O . HOH C 2 . ? 11.594 13.464 24.773 1.00 45.38 ? 197 HOH A O 1 HETATM 2043 O O . HOH C 2 . ? 13.284 33.889 33.020 1.00 46.81 ? 198 HOH A O 1 HETATM 2044 O O . HOH C 2 . ? 19.682 25.921 27.103 1.00 48.88 ? 199 HOH A O 1 HETATM 2045 O O . HOH C 2 . ? -4.768 37.938 11.195 1.00 43.47 ? 200 HOH A O 1 HETATM 2046 O O . HOH C 2 . ? -12.782 34.116 13.442 1.00 49.03 ? 201 HOH A O 1 HETATM 2047 O O . HOH C 2 . ? -2.495 19.823 -8.875 1.00 48.15 ? 202 HOH A O 1 HETATM 2048 O O . HOH C 2 . ? 15.681 15.101 14.847 1.00 45.07 ? 203 HOH A O 1 HETATM 2049 O O . HOH C 2 . ? -12.440 21.284 15.359 1.00 50.08 ? 204 HOH A O 1 HETATM 2050 O O . HOH C 2 . ? 7.083 20.920 -7.919 1.00 49.74 ? 205 HOH A O 1 HETATM 2051 O O . HOH C 2 . ? 17.310 34.702 14.513 1.00 48.52 ? 206 HOH A O 1 HETATM 2052 O O . HOH C 2 . ? -0.973 19.025 -10.656 1.00 48.82 ? 207 HOH A O 1 HETATM 2053 O O . HOH D 2 . ? 3.919 50.786 31.574 1.00 28.77 ? 130 HOH B O 1 HETATM 2054 O O . HOH D 2 . ? 2.472 65.604 5.125 1.00 31.08 ? 131 HOH B O 1 HETATM 2055 O O . HOH D 2 . ? -5.861 45.300 2.647 1.00 34.39 ? 132 HOH B O 1 HETATM 2056 O O . HOH D 2 . ? -1.273 40.074 9.930 1.00 37.48 ? 133 HOH B O 1 HETATM 2057 O O . HOH D 2 . ? -4.691 41.806 9.928 1.00 39.05 ? 134 HOH B O 1 HETATM 2058 O O . HOH D 2 . ? -7.721 52.643 2.415 1.00 19.07 ? 135 HOH B O 1 HETATM 2059 O O . HOH D 2 . ? 10.053 59.609 -1.041 1.00 24.40 ? 136 HOH B O 1 HETATM 2060 O O . HOH D 2 . ? 8.279 61.759 1.710 1.00 24.35 ? 137 HOH B O 1 HETATM 2061 O O . HOH D 2 . ? 15.827 48.965 16.457 1.00 23.36 ? 138 HOH B O 1 HETATM 2062 O O . HOH D 2 . ? -7.332 51.595 11.531 1.00 22.20 ? 139 HOH B O 1 HETATM 2063 O O . HOH D 2 . ? -3.514 64.140 11.330 1.00 47.03 ? 140 HOH B O 1 HETATM 2064 O O . HOH D 2 . ? 19.974 49.703 7.119 1.00 32.76 ? 141 HOH B O 1 HETATM 2065 O O . HOH D 2 . ? 2.637 57.219 28.854 1.00 25.88 ? 142 HOH B O 1 HETATM 2066 O O . HOH D 2 . ? -3.386 46.294 1.165 1.00 33.41 ? 143 HOH B O 1 HETATM 2067 O O . HOH D 2 . ? 7.870 61.613 -0.818 1.00 23.18 ? 144 HOH B O 1 HETATM 2068 O O . HOH D 2 . ? 13.098 51.325 -1.404 1.00 32.18 ? 145 HOH B O 1 HETATM 2069 O O . HOH D 2 . ? -2.825 53.388 16.400 1.00 26.81 ? 146 HOH B O 1 HETATM 2070 O O . HOH D 2 . ? 13.496 44.594 8.578 1.00 28.94 ? 147 HOH B O 1 HETATM 2071 O O . HOH D 2 . ? 17.571 49.811 14.166 1.00 34.77 ? 148 HOH B O 1 HETATM 2072 O O . HOH D 2 . ? -9.347 55.431 7.775 1.00 34.51 ? 149 HOH B O 1 HETATM 2073 O O . HOH D 2 . ? 3.283 64.239 11.027 1.00 39.82 ? 150 HOH B O 1 HETATM 2074 O O . HOH D 2 . ? 0.074 46.972 24.250 1.00 40.04 ? 151 HOH B O 1 HETATM 2075 O O . HOH D 2 . ? 15.671 50.798 18.616 1.00 34.79 ? 152 HOH B O 1 HETATM 2076 O O . HOH D 2 . ? -4.017 45.713 14.734 1.00 38.27 ? 153 HOH B O 1 HETATM 2077 O O . HOH D 2 . ? 3.773 55.201 32.535 1.00 42.94 ? 154 HOH B O 1 HETATM 2078 O O . HOH D 2 . ? 11.733 43.210 11.792 1.00 31.22 ? 155 HOH B O 1 HETATM 2079 O O . HOH D 2 . ? 14.030 61.284 3.757 1.00 51.27 ? 156 HOH B O 1 HETATM 2080 O O . HOH D 2 . ? 10.229 46.055 0.171 1.00 51.85 ? 157 HOH B O 1 HETATM 2081 O O . HOH D 2 . ? 9.242 63.973 -0.677 1.00 39.62 ? 158 HOH B O 1 HETATM 2082 O O . HOH D 2 . ? 1.045 61.634 16.837 1.00 31.46 ? 159 HOH B O 1 HETATM 2083 O O . HOH D 2 . ? 1.251 60.328 22.724 1.00 35.33 ? 160 HOH B O 1 HETATM 2084 O O . HOH D 2 . ? -1.637 68.538 -0.231 1.00 43.69 ? 161 HOH B O 1 HETATM 2085 O O . HOH D 2 . ? -6.314 44.148 11.792 1.00 43.81 ? 162 HOH B O 1 HETATM 2086 O O . HOH D 2 . ? 17.624 62.302 15.468 1.00 60.86 ? 163 HOH B O 1 HETATM 2087 O O . HOH D 2 . ? 9.682 36.950 12.161 1.00 44.11 ? 164 HOH B O 1 HETATM 2088 O O . HOH D 2 . ? -6.229 59.993 16.565 1.00 48.34 ? 165 HOH B O 1 HETATM 2089 O O . HOH D 2 . ? 18.575 58.248 17.397 1.00 42.98 ? 166 HOH B O 1 HETATM 2090 O O . HOH D 2 . ? -11.240 61.202 11.311 1.00 40.16 ? 167 HOH B O 1 HETATM 2091 O O . HOH D 2 . ? 15.813 61.691 7.142 1.00 39.72 ? 168 HOH B O 1 HETATM 2092 O O . HOH D 2 . ? 16.897 47.280 19.297 1.00 42.71 ? 169 HOH B O 1 HETATM 2093 O O . HOH D 2 . ? 2.020 60.200 28.702 1.00 42.66 ? 170 HOH B O 1 HETATM 2094 O O . HOH D 2 . ? 12.484 46.546 20.856 1.00 43.92 ? 171 HOH B O 1 HETATM 2095 O O . HOH D 2 . ? -2.562 66.722 13.634 1.00 45.20 ? 172 HOH B O 1 HETATM 2096 O O . HOH D 2 . ? -5.796 48.831 19.123 1.00 40.17 ? 173 HOH B O 1 HETATM 2097 O O . HOH D 2 . ? 0.928 68.187 11.982 1.00 44.77 ? 174 HOH B O 1 HETATM 2098 O O . HOH D 2 . ? 12.184 47.602 30.350 1.00 43.77 ? 175 HOH B O 1 HETATM 2099 O O . HOH D 2 . ? -11.264 57.834 8.256 1.00 47.49 ? 176 HOH B O 1 HETATM 2100 O O . HOH D 2 . ? 3.267 60.374 26.361 1.00 43.88 ? 177 HOH B O 1 HETATM 2101 O O . HOH D 2 . ? -9.940 52.059 11.757 1.00 45.82 ? 178 HOH B O 1 HETATM 2102 O O . HOH D 2 . ? -6.476 56.521 14.140 1.00 43.70 ? 179 HOH B O 1 HETATM 2103 O O . HOH D 2 . ? -11.015 58.681 12.592 1.00 49.05 ? 180 HOH B O 1 HETATM 2104 O O . HOH D 2 . ? 21.676 51.716 19.099 1.00 49.69 ? 181 HOH B O 1 HETATM 2105 O O . HOH D 2 . ? -13.670 64.825 12.284 1.00 47.39 ? 182 HOH B O 1 HETATM 2106 O O . HOH D 2 . ? 9.518 49.102 32.005 1.00 46.17 ? 183 HOH B O 1 HETATM 2107 O O . HOH D 2 . ? 21.793 57.055 12.240 1.00 50.37 ? 184 HOH B O 1 HETATM 2108 O O . HOH D 2 . ? 1.332 40.135 12.591 1.00 44.68 ? 185 HOH B O 1 HETATM 2109 O O . HOH D 2 . ? 8.691 48.690 29.528 1.00 46.91 ? 186 HOH B O 1 HETATM 2110 O O . HOH D 2 . ? 6.467 60.149 35.696 1.00 50.61 ? 187 HOH B O 1 HETATM 2111 O O . HOH D 2 . ? -8.638 44.506 15.800 1.00 46.91 ? 188 HOH B O 1 HETATM 2112 O O . HOH D 2 . ? 15.546 65.017 18.487 1.00 47.38 ? 189 HOH B O 1 HETATM 2113 O O . HOH D 2 . ? 15.042 45.803 16.930 1.00 46.85 ? 190 HOH B O 1 HETATM 2114 O O . HOH D 2 . ? -2.086 54.852 -4.658 1.00 41.15 ? 191 HOH B O 1 HETATM 2115 O O . HOH D 2 . ? -5.353 46.810 17.413 1.00 46.75 ? 192 HOH B O 1 HETATM 2116 O O . HOH D 2 . ? 14.548 44.568 19.235 1.00 42.86 ? 193 HOH B O 1 HETATM 2117 O O . HOH D 2 . ? 19.526 46.697 22.419 1.00 45.00 ? 194 HOH B O 1 HETATM 2118 O O . HOH D 2 . ? 19.985 57.897 9.167 1.00 45.47 ? 195 HOH B O 1 HETATM 2119 O O . HOH D 2 . ? 7.151 59.728 33.254 1.00 48.31 ? 196 HOH B O 1 HETATM 2120 O O . HOH D 2 . ? -5.379 40.534 16.033 1.00 47.29 ? 197 HOH B O 1 #