data_3PHX # _entry.id 3PHX # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.403 _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 3PHX pdb_00003phx 10.2210/pdb3phx/pdb RCSB RCSB062392 ? ? WWPDB D_1000062392 ? ? # 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 _pdbx_audit_revision_history.part_number 1 'Structure model' 1 0 2011-02-02 ? 2 'Structure model' 1 1 2011-07-13 ? 3 'Structure model' 1 2 2014-08-06 ? 4 'Structure model' 1 3 2025-03-26 ? # _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' 'Database references' 3 4 'Structure model' 'Data collection' 4 4 'Structure model' 'Database references' 5 4 'Structure model' 'Derived calculations' 6 4 '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_entry_details 5 4 'Structure model' pdbx_struct_conn_angle 6 4 'Structure model' struct_conn 7 4 'Structure model' struct_conn_type 8 4 'Structure model' struct_ref_seq_dif 9 4 'Structure model' struct_site # 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' 3 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id' 4 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id' 5 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 6 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 7 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 8 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id' 9 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id' 10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id' 12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id' 13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id' 17 4 'Structure model' '_pdbx_struct_conn_angle.value' 18 4 'Structure model' '_struct_conn.conn_type_id' 19 4 'Structure model' '_struct_conn.id' 20 4 'Structure model' '_struct_conn.pdbx_dist_value' 21 4 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' 22 4 'Structure model' '_struct_conn.ptnr1_auth_asym_id' 23 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id' 24 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id' 25 4 'Structure model' '_struct_conn.ptnr1_label_asym_id' 26 4 'Structure model' '_struct_conn.ptnr1_label_atom_id' 27 4 'Structure model' '_struct_conn.ptnr1_label_comp_id' 28 4 'Structure model' '_struct_conn.ptnr1_label_seq_id' 29 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id' 30 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id' 31 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id' 32 4 'Structure model' '_struct_conn.ptnr2_label_asym_id' 33 4 'Structure model' '_struct_conn.ptnr2_label_atom_id' 34 4 'Structure model' '_struct_conn.ptnr2_label_comp_id' 35 4 'Structure model' '_struct_conn.ptnr2_label_seq_id' 36 4 'Structure model' '_struct_conn_type.id' 37 4 'Structure model' '_struct_ref_seq_dif.details' 38 4 'Structure model' '_struct_site.pdbx_auth_asym_id' 39 4 'Structure model' '_struct_site.pdbx_auth_comp_id' 40 4 'Structure model' '_struct_site.pdbx_auth_seq_id' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3PHX _pdbx_database_status.recvd_initial_deposition_date 2010-11-04 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_nmr_data ? _pdbx_database_status.methods_development_category ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3PHW . unspecified PDB 3PHU . unspecified # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Akutsu, M.' 1 'Ye, Y.' 2 'Virdee, S.' 3 'Komander, D.' 4 # _citation.id primary _citation.title 'Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 108 _citation.page_first 2228 _citation.page_last 2233 _citation.year 2011 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 21266548 _citation.pdbx_database_id_DOI 10.1073/pnas.1015287108 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal _citation_author.identifier_ORCID primary 'Akutsu, M.' 1 ? primary 'Ye, Y.' 2 ? primary 'Virdee, S.' 3 ? primary 'Chin, J.W.' 4 ? primary 'Komander, D.' 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 'RNA-directed RNA polymerase L' 21011.580 1 '3.4.19.12, 2.7.7.48' ? 'UNP residues 1-183' ? 2 polymer man 'Ubiquitin-like protein ISG15' 8985.266 1 ? ? 'UNP residues 79-156' ? 3 non-polymer syn 'ZINC ION' 65.409 12 ? ? ? ? 4 non-polymer syn 'ACETIC ACID' 60.052 2 ? ? ? ? 5 non-polymer syn ETHANAMINE 45.084 1 ? ? ? ? 6 water nat water 18.015 192 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Protein L, Large structural protein, Replicase, Transcriptase, Ubiquitin thiolesterase, RNA-directed RNA polymerase' 2 'Interferon-induced 15 kDa protein, Interferon-induced 17 kDa protein, IP17, Ubiquitin cross-reactive protein, hUCRP' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;GPMDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSYHYIKRLTESAARKYYQEEPE ARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIIIWTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRIL PQFETDTREALSLMDRVIAVDQLTS ; ;GPMDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSYHYIKRLTESAARKYYQEEPE ARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIIIWTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRIL PQFETDTREALSLMDRVIAVDQLTS ; A ? 2 'polypeptide(L)' no no MDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRG MDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRG B ? # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'ZINC ION' ZN 4 'ACETIC ACID' ACY 5 ETHANAMINE NEH 6 water HOH # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 PRO n 1 3 MET n 1 4 ASP n 1 5 PHE n 1 6 LEU n 1 7 ARG n 1 8 SER n 1 9 LEU n 1 10 ASP n 1 11 TRP n 1 12 THR n 1 13 GLN n 1 14 VAL n 1 15 ILE n 1 16 ALA n 1 17 GLY n 1 18 GLN n 1 19 TYR n 1 20 VAL n 1 21 SER n 1 22 ASN n 1 23 PRO n 1 24 ARG n 1 25 PHE n 1 26 ASN n 1 27 ILE n 1 28 SER n 1 29 ASP n 1 30 TYR n 1 31 PHE n 1 32 GLU n 1 33 ILE n 1 34 VAL n 1 35 ARG n 1 36 GLN n 1 37 PRO n 1 38 GLY n 1 39 ASP n 1 40 GLY n 1 41 ASN n 1 42 CYS n 1 43 PHE n 1 44 TYR n 1 45 HIS n 1 46 SER n 1 47 ILE n 1 48 ALA n 1 49 GLU n 1 50 LEU n 1 51 THR n 1 52 MET n 1 53 PRO n 1 54 ASN n 1 55 LYS n 1 56 THR n 1 57 ASP n 1 58 HIS n 1 59 SER n 1 60 TYR n 1 61 HIS n 1 62 TYR n 1 63 ILE n 1 64 LYS n 1 65 ARG n 1 66 LEU n 1 67 THR n 1 68 GLU n 1 69 SER n 1 70 ALA n 1 71 ALA n 1 72 ARG n 1 73 LYS n 1 74 TYR n 1 75 TYR n 1 76 GLN n 1 77 GLU n 1 78 GLU n 1 79 PRO n 1 80 GLU n 1 81 ALA n 1 82 ARG n 1 83 LEU n 1 84 VAL n 1 85 GLY n 1 86 LEU n 1 87 SER n 1 88 LEU n 1 89 GLU n 1 90 ASP n 1 91 TYR n 1 92 LEU n 1 93 LYS n 1 94 ARG n 1 95 MET n 1 96 LEU n 1 97 SER n 1 98 ASP n 1 99 ASN n 1 100 GLU n 1 101 TRP n 1 102 GLY n 1 103 SER n 1 104 THR n 1 105 LEU n 1 106 GLU n 1 107 ALA n 1 108 SER n 1 109 MET n 1 110 LEU n 1 111 ALA n 1 112 LYS n 1 113 GLU n 1 114 MET n 1 115 GLY n 1 116 ILE n 1 117 THR n 1 118 ILE n 1 119 ILE n 1 120 ILE n 1 121 TRP n 1 122 THR n 1 123 VAL n 1 124 ALA n 1 125 ALA n 1 126 SER n 1 127 ASP n 1 128 GLU n 1 129 VAL n 1 130 GLU n 1 131 ALA n 1 132 GLY n 1 133 ILE n 1 134 LYS n 1 135 PHE n 1 136 GLY n 1 137 ASP n 1 138 GLY n 1 139 ASP n 1 140 VAL n 1 141 PHE n 1 142 THR n 1 143 ALA n 1 144 VAL n 1 145 ASN n 1 146 LEU n 1 147 LEU n 1 148 HIS n 1 149 SER n 1 150 GLY n 1 151 GLN n 1 152 THR n 1 153 HIS n 1 154 PHE n 1 155 ASP n 1 156 ALA n 1 157 LEU n 1 158 ARG n 1 159 ILE n 1 160 LEU n 1 161 PRO n 1 162 GLN n 1 163 PHE n 1 164 GLU n 1 165 THR n 1 166 ASP n 1 167 THR n 1 168 ARG n 1 169 GLU n 1 170 ALA n 1 171 LEU n 1 172 SER n 1 173 LEU n 1 174 MET n 1 175 ASP n 1 176 ARG n 1 177 VAL n 1 178 ILE n 1 179 ALA n 1 180 VAL n 1 181 ASP n 1 182 GLN n 1 183 LEU n 1 184 THR n 1 185 SER n 2 1 MET n 2 2 ASP n 2 3 GLU n 2 4 PRO n 2 5 LEU n 2 6 SER n 2 7 ILE n 2 8 LEU n 2 9 VAL n 2 10 ARG n 2 11 ASN n 2 12 ASN n 2 13 LYS n 2 14 GLY n 2 15 ARG n 2 16 SER n 2 17 SER n 2 18 THR n 2 19 TYR n 2 20 GLU n 2 21 VAL n 2 22 ARG n 2 23 LEU n 2 24 THR n 2 25 GLN n 2 26 THR n 2 27 VAL n 2 28 ALA n 2 29 HIS n 2 30 LEU n 2 31 LYS n 2 32 GLN n 2 33 GLN n 2 34 VAL n 2 35 SER n 2 36 GLY n 2 37 LEU n 2 38 GLU n 2 39 GLY n 2 40 VAL n 2 41 GLN n 2 42 ASP n 2 43 ASP n 2 44 LEU n 2 45 PHE n 2 46 TRP n 2 47 LEU n 2 48 THR n 2 49 PHE n 2 50 GLU n 2 51 GLY n 2 52 LYS n 2 53 PRO n 2 54 LEU n 2 55 GLU n 2 56 ASP n 2 57 GLN n 2 58 LEU n 2 59 PRO n 2 60 LEU n 2 61 GLY n 2 62 GLU n 2 63 TYR n 2 64 GLY n 2 65 LEU n 2 66 LYS n 2 67 PRO n 2 68 LEU n 2 69 SER n 2 70 THR n 2 71 VAL n 2 72 PHE n 2 73 MET n 2 74 ASN n 2 75 LEU n 2 76 ARG n 2 77 LEU n 2 78 ARG n 2 79 GLY n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? CCHFV ? L ? Nigeria/IbAr10200/1970 ? ? ? ? 'Crimean-Congo hemorrhagic fever virus' 652961 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? human ? 'ISG15, G1P2, UCRP' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # 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 ACY non-polymer . 'ACETIC ACID' ? 'C2 H4 O2' 60.052 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 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NEH non-polymer . ETHANAMINE ? 'C2 H7 N' 45.084 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # 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 GLY 1 -1 -1 GLY GLY A . n A 1 2 PRO 2 0 0 PRO PRO A . n A 1 3 MET 3 1 1 MET MET A . n A 1 4 ASP 4 2 2 ASP ASP A . n A 1 5 PHE 5 3 3 PHE PHE A . n A 1 6 LEU 6 4 4 LEU LEU A . n A 1 7 ARG 7 5 5 ARG ARG A . n A 1 8 SER 8 6 6 SER SER A . n A 1 9 LEU 9 7 7 LEU LEU A . n A 1 10 ASP 10 8 8 ASP ASP A . n A 1 11 TRP 11 9 9 TRP TRP A . n A 1 12 THR 12 10 10 THR THR A . n A 1 13 GLN 13 11 11 GLN GLN A . n A 1 14 VAL 14 12 12 VAL VAL A . n A 1 15 ILE 15 13 13 ILE ILE A . n A 1 16 ALA 16 14 14 ALA ALA A . n A 1 17 GLY 17 15 15 GLY GLY A . n A 1 18 GLN 18 16 16 GLN GLN A . n A 1 19 TYR 19 17 17 TYR TYR A . n A 1 20 VAL 20 18 18 VAL VAL A . n A 1 21 SER 21 19 19 SER SER A . n A 1 22 ASN 22 20 20 ASN ASN A . n A 1 23 PRO 23 21 21 PRO PRO A . n A 1 24 ARG 24 22 22 ARG ARG A . n A 1 25 PHE 25 23 23 PHE PHE A . n A 1 26 ASN 26 24 24 ASN ASN A . n A 1 27 ILE 27 25 25 ILE ILE A . n A 1 28 SER 28 26 26 SER SER A . n A 1 29 ASP 29 27 27 ASP ASP A . n A 1 30 TYR 30 28 28 TYR TYR A . n A 1 31 PHE 31 29 29 PHE PHE A . n A 1 32 GLU 32 30 30 GLU GLU A . n A 1 33 ILE 33 31 31 ILE ILE A . n A 1 34 VAL 34 32 32 VAL VAL A . n A 1 35 ARG 35 33 33 ARG ARG A . n A 1 36 GLN 36 34 34 GLN GLN A . n A 1 37 PRO 37 35 35 PRO PRO A . n A 1 38 GLY 38 36 36 GLY GLY A . n A 1 39 ASP 39 37 37 ASP ASP A . n A 1 40 GLY 40 38 38 GLY GLY A . n A 1 41 ASN 41 39 39 ASN ASN A . n A 1 42 CYS 42 40 40 CYS CYS A . n A 1 43 PHE 43 41 41 PHE PHE A . n A 1 44 TYR 44 42 42 TYR TYR A . n A 1 45 HIS 45 43 43 HIS HIS A . n A 1 46 SER 46 44 44 SER SER A . n A 1 47 ILE 47 45 45 ILE ILE A . n A 1 48 ALA 48 46 46 ALA ALA A . n A 1 49 GLU 49 47 47 GLU GLU A . n A 1 50 LEU 50 48 48 LEU LEU A . n A 1 51 THR 51 49 49 THR THR A . n A 1 52 MET 52 50 50 MET MET A . n A 1 53 PRO 53 51 51 PRO PRO A . n A 1 54 ASN 54 52 52 ASN ASN A . n A 1 55 LYS 55 53 53 LYS LYS A . n A 1 56 THR 56 54 54 THR THR A . n A 1 57 ASP 57 55 55 ASP ASP A . n A 1 58 HIS 58 56 56 HIS HIS A . n A 1 59 SER 59 57 57 SER SER A . n A 1 60 TYR 60 58 58 TYR TYR A . n A 1 61 HIS 61 59 59 HIS HIS A . n A 1 62 TYR 62 60 60 TYR TYR A . n A 1 63 ILE 63 61 61 ILE ILE A . n A 1 64 LYS 64 62 62 LYS LYS A . n A 1 65 ARG 65 63 63 ARG ARG A . n A 1 66 LEU 66 64 64 LEU LEU A . n A 1 67 THR 67 65 65 THR THR A . n A 1 68 GLU 68 66 66 GLU GLU A . n A 1 69 SER 69 67 67 SER SER A . n A 1 70 ALA 70 68 68 ALA ALA A . n A 1 71 ALA 71 69 69 ALA ALA A . n A 1 72 ARG 72 70 70 ARG ARG A . n A 1 73 LYS 73 71 71 LYS LYS A . n A 1 74 TYR 74 72 72 TYR TYR A . n A 1 75 TYR 75 73 73 TYR TYR A . n A 1 76 GLN 76 74 74 GLN GLN A . n A 1 77 GLU 77 75 75 GLU GLU A . n A 1 78 GLU 78 76 76 GLU GLU A . n A 1 79 PRO 79 77 77 PRO PRO A . n A 1 80 GLU 80 78 78 GLU GLU A . n A 1 81 ALA 81 79 79 ALA ALA A . n A 1 82 ARG 82 80 80 ARG ARG A . n A 1 83 LEU 83 81 81 LEU LEU A . n A 1 84 VAL 84 82 82 VAL VAL A . n A 1 85 GLY 85 83 83 GLY GLY A . n A 1 86 LEU 86 84 84 LEU LEU A . n A 1 87 SER 87 85 85 SER SER A . n A 1 88 LEU 88 86 86 LEU LEU A . n A 1 89 GLU 89 87 87 GLU GLU A . n A 1 90 ASP 90 88 88 ASP ASP A . n A 1 91 TYR 91 89 89 TYR TYR A . n A 1 92 LEU 92 90 90 LEU LEU A . n A 1 93 LYS 93 91 91 LYS LYS A . n A 1 94 ARG 94 92 92 ARG ARG A . n A 1 95 MET 95 93 93 MET MET A . n A 1 96 LEU 96 94 94 LEU LEU A . n A 1 97 SER 97 95 95 SER SER A . n A 1 98 ASP 98 96 96 ASP ASP A . n A 1 99 ASN 99 97 97 ASN ASN A . n A 1 100 GLU 100 98 98 GLU GLU A . n A 1 101 TRP 101 99 99 TRP TRP A . n A 1 102 GLY 102 100 100 GLY GLY A . n A 1 103 SER 103 101 101 SER SER A . n A 1 104 THR 104 102 102 THR THR A . n A 1 105 LEU 105 103 103 LEU LEU A . n A 1 106 GLU 106 104 104 GLU GLU A . n A 1 107 ALA 107 105 105 ALA ALA A . n A 1 108 SER 108 106 106 SER SER A . n A 1 109 MET 109 107 107 MET MET A . n A 1 110 LEU 110 108 108 LEU LEU A . n A 1 111 ALA 111 109 109 ALA ALA A . n A 1 112 LYS 112 110 110 LYS LYS A . n A 1 113 GLU 113 111 111 GLU GLU A . n A 1 114 MET 114 112 112 MET MET A . n A 1 115 GLY 115 113 113 GLY GLY A . n A 1 116 ILE 116 114 114 ILE ILE A . n A 1 117 THR 117 115 115 THR THR A . n A 1 118 ILE 118 116 116 ILE ILE A . n A 1 119 ILE 119 117 117 ILE ILE A . n A 1 120 ILE 120 118 118 ILE ILE A . n A 1 121 TRP 121 119 119 TRP TRP A . n A 1 122 THR 122 120 120 THR THR A . n A 1 123 VAL 123 121 121 VAL VAL A . n A 1 124 ALA 124 122 ? ? ? A . n A 1 125 ALA 125 123 ? ? ? A . n A 1 126 SER 126 124 124 SER SER A . n A 1 127 ASP 127 125 125 ASP ASP A . n A 1 128 GLU 128 126 126 GLU GLU A . n A 1 129 VAL 129 127 127 VAL VAL A . n A 1 130 GLU 130 128 128 GLU GLU A . n A 1 131 ALA 131 129 129 ALA ALA A . n A 1 132 GLY 132 130 130 GLY GLY A . n A 1 133 ILE 133 131 131 ILE ILE A . n A 1 134 LYS 134 132 132 LYS LYS A . n A 1 135 PHE 135 133 133 PHE PHE A . n A 1 136 GLY 136 134 134 GLY GLY A . n A 1 137 ASP 137 135 135 ASP ASP A . n A 1 138 GLY 138 136 136 GLY GLY A . n A 1 139 ASP 139 137 137 ASP ASP A . n A 1 140 VAL 140 138 138 VAL VAL A . n A 1 141 PHE 141 139 139 PHE PHE A . n A 1 142 THR 142 140 140 THR THR A . n A 1 143 ALA 143 141 141 ALA ALA A . n A 1 144 VAL 144 142 142 VAL VAL A . n A 1 145 ASN 145 143 143 ASN ASN A . n A 1 146 LEU 146 144 144 LEU LEU A . n A 1 147 LEU 147 145 145 LEU LEU A . n A 1 148 HIS 148 146 146 HIS HIS A . n A 1 149 SER 149 147 147 SER SER A . n A 1 150 GLY 150 148 148 GLY GLY A . n A 1 151 GLN 151 149 149 GLN GLN A . n A 1 152 THR 152 150 150 THR THR A . n A 1 153 HIS 153 151 151 HIS HIS A . n A 1 154 PHE 154 152 152 PHE PHE A . n A 1 155 ASP 155 153 153 ASP ASP A . n A 1 156 ALA 156 154 154 ALA ALA A . n A 1 157 LEU 157 155 155 LEU LEU A . n A 1 158 ARG 158 156 156 ARG ARG A . n A 1 159 ILE 159 157 157 ILE ILE A . n A 1 160 LEU 160 158 158 LEU LEU A . n A 1 161 PRO 161 159 159 PRO PRO A . n A 1 162 GLN 162 160 160 GLN GLN A . n A 1 163 PHE 163 161 161 PHE PHE A . n A 1 164 GLU 164 162 162 GLU GLU A . n A 1 165 THR 165 163 ? ? ? A . n A 1 166 ASP 166 164 ? ? ? A . n A 1 167 THR 167 165 ? ? ? A . n A 1 168 ARG 168 166 ? ? ? A . n A 1 169 GLU 169 167 ? ? ? A . n A 1 170 ALA 170 168 ? ? ? A . n A 1 171 LEU 171 169 ? ? ? A . n A 1 172 SER 172 170 ? ? ? A . n A 1 173 LEU 173 171 ? ? ? A . n A 1 174 MET 174 172 ? ? ? A . n A 1 175 ASP 175 173 ? ? ? A . n A 1 176 ARG 176 174 ? ? ? A . n A 1 177 VAL 177 175 ? ? ? A . n A 1 178 ILE 178 176 ? ? ? A . n A 1 179 ALA 179 177 ? ? ? A . n A 1 180 VAL 180 178 ? ? ? A . n A 1 181 ASP 181 179 ? ? ? A . n A 1 182 GLN 182 180 ? ? ? A . n A 1 183 LEU 183 181 ? ? ? A . n A 1 184 THR 184 182 ? ? ? A . n A 1 185 SER 185 183 ? ? ? A . n B 2 1 MET 1 78 ? ? ? B . n B 2 2 ASP 2 79 ? ? ? B . n B 2 3 GLU 3 80 80 GLU GLU B . n B 2 4 PRO 4 81 81 PRO PRO B . n B 2 5 LEU 5 82 82 LEU LEU B . n B 2 6 SER 6 83 83 SER SER B . n B 2 7 ILE 7 84 84 ILE ILE B . n B 2 8 LEU 8 85 85 LEU LEU B . n B 2 9 VAL 9 86 86 VAL VAL B . n B 2 10 ARG 10 87 87 ARG ARG B . n B 2 11 ASN 11 88 88 ASN ASN B . n B 2 12 ASN 12 89 89 ASN ASN B . n B 2 13 LYS 13 90 90 LYS LYS B . n B 2 14 GLY 14 91 91 GLY GLY B . n B 2 15 ARG 15 92 92 ARG ARG B . n B 2 16 SER 16 93 93 SER SER B . n B 2 17 SER 17 94 94 SER SER B . n B 2 18 THR 18 95 95 THR THR B . n B 2 19 TYR 19 96 96 TYR TYR B . n B 2 20 GLU 20 97 97 GLU GLU B . n B 2 21 VAL 21 98 98 VAL VAL B . n B 2 22 ARG 22 99 99 ARG ARG B . n B 2 23 LEU 23 100 100 LEU LEU B . n B 2 24 THR 24 101 101 THR THR B . n B 2 25 GLN 25 102 102 GLN GLN B . n B 2 26 THR 26 103 103 THR THR B . n B 2 27 VAL 27 104 104 VAL VAL B . n B 2 28 ALA 28 105 105 ALA ALA B . n B 2 29 HIS 29 106 106 HIS HIS B . n B 2 30 LEU 30 107 107 LEU LEU B . n B 2 31 LYS 31 108 108 LYS LYS B . n B 2 32 GLN 32 109 109 GLN GLN B . n B 2 33 GLN 33 110 110 GLN GLN B . n B 2 34 VAL 34 111 111 VAL VAL B . n B 2 35 SER 35 112 112 SER SER B . n B 2 36 GLY 36 113 113 GLY GLY B . n B 2 37 LEU 37 114 114 LEU LEU B . n B 2 38 GLU 38 115 115 GLU GLU B . n B 2 39 GLY 39 116 116 GLY GLY B . n B 2 40 VAL 40 117 117 VAL VAL B . n B 2 41 GLN 41 118 118 GLN GLN B . n B 2 42 ASP 42 119 119 ASP ASP B . n B 2 43 ASP 43 120 120 ASP ASP B . n B 2 44 LEU 44 121 121 LEU LEU B . n B 2 45 PHE 45 122 122 PHE PHE B . n B 2 46 TRP 46 123 123 TRP TRP B . n B 2 47 LEU 47 124 124 LEU LEU B . n B 2 48 THR 48 125 125 THR THR B . n B 2 49 PHE 49 126 126 PHE PHE B . n B 2 50 GLU 50 127 127 GLU GLU B . n B 2 51 GLY 51 128 128 GLY GLY B . n B 2 52 LYS 52 129 129 LYS LYS B . n B 2 53 PRO 53 130 130 PRO PRO B . n B 2 54 LEU 54 131 131 LEU LEU B . n B 2 55 GLU 55 132 132 GLU GLU B . n B 2 56 ASP 56 133 133 ASP ASP B . n B 2 57 GLN 57 134 134 GLN GLN B . n B 2 58 LEU 58 135 135 LEU LEU B . n B 2 59 PRO 59 136 136 PRO PRO B . n B 2 60 LEU 60 137 137 LEU LEU B . n B 2 61 GLY 61 138 138 GLY GLY B . n B 2 62 GLU 62 139 139 GLU GLU B . n B 2 63 TYR 63 140 140 TYR TYR B . n B 2 64 GLY 64 141 141 GLY GLY B . n B 2 65 LEU 65 142 142 LEU LEU B . n B 2 66 LYS 66 143 143 LYS LYS B . n B 2 67 PRO 67 144 144 PRO PRO B . n B 2 68 LEU 68 145 145 LEU LEU B . n B 2 69 SER 69 146 146 SER SER B . n B 2 70 THR 70 147 147 THR THR B . n B 2 71 VAL 71 148 148 VAL VAL B . n B 2 72 PHE 72 149 149 PHE PHE B . n B 2 73 MET 73 150 150 MET MET B . n B 2 74 ASN 74 151 151 ASN ASN B . n B 2 75 LEU 75 152 152 LEU LEU B . n B 2 76 ARG 76 153 153 ARG ARG B . n B 2 77 LEU 77 154 154 LEU LEU B . n B 2 78 ARG 78 155 155 ARG ARG B . n B 2 79 GLY 79 156 156 GLY GLY B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 ZN 1 184 184 ZN ZN A . D 3 ZN 1 185 185 ZN ZN A . E 3 ZN 1 186 186 ZN ZN A . F 3 ZN 1 187 187 ZN ZN A . G 3 ZN 1 188 188 ZN ZN A . H 3 ZN 1 189 189 ZN ZN A . I 3 ZN 1 190 190 ZN ZN A . J 3 ZN 1 191 191 ZN ZN A . K 3 ZN 1 192 192 ZN ZN A . L 4 ACY 1 193 193 ACY ACY A . M 5 NEH 1 157 157 NEH NEH B . N 3 ZN 1 1 1 ZN ZN B . O 3 ZN 1 2 2 ZN ZN B . P 3 ZN 1 3 3 ZN ZN B . Q 4 ACY 1 4 4 ACY ACY B . R 6 HOH 1 201 201 HOH HOH A . R 6 HOH 2 202 202 HOH HOH A . R 6 HOH 3 203 203 HOH HOH A . R 6 HOH 4 204 204 HOH HOH A . R 6 HOH 5 205 205 HOH HOH A . R 6 HOH 6 206 206 HOH HOH A . R 6 HOH 7 207 207 HOH HOH A . R 6 HOH 8 208 208 HOH HOH A . R 6 HOH 9 209 209 HOH HOH A . R 6 HOH 10 210 210 HOH HOH A . R 6 HOH 11 211 211 HOH HOH A . R 6 HOH 12 212 212 HOH HOH A . R 6 HOH 13 213 213 HOH HOH A . R 6 HOH 14 214 214 HOH HOH A . R 6 HOH 15 215 215 HOH HOH A . R 6 HOH 16 216 216 HOH HOH A . R 6 HOH 17 217 217 HOH HOH A . R 6 HOH 18 218 218 HOH HOH A . R 6 HOH 19 219 219 HOH HOH A . R 6 HOH 20 220 220 HOH HOH A . R 6 HOH 21 221 221 HOH HOH A . R 6 HOH 22 222 222 HOH HOH A . R 6 HOH 23 223 223 HOH HOH A . R 6 HOH 24 224 224 HOH HOH A . R 6 HOH 25 225 225 HOH HOH A . R 6 HOH 26 226 226 HOH HOH A . R 6 HOH 27 227 227 HOH HOH A . R 6 HOH 28 228 228 HOH HOH A . R 6 HOH 29 229 229 HOH HOH A . R 6 HOH 30 230 230 HOH HOH A . R 6 HOH 31 231 231 HOH HOH A . R 6 HOH 32 232 232 HOH HOH A . R 6 HOH 33 233 233 HOH HOH A . R 6 HOH 34 234 234 HOH HOH A . R 6 HOH 35 235 235 HOH HOH A . R 6 HOH 36 236 236 HOH HOH A . R 6 HOH 37 237 237 HOH HOH A . R 6 HOH 38 238 238 HOH HOH A . R 6 HOH 39 239 239 HOH HOH A . R 6 HOH 40 240 240 HOH HOH A . R 6 HOH 41 241 241 HOH HOH A . R 6 HOH 42 242 242 HOH HOH A . R 6 HOH 43 243 243 HOH HOH A . R 6 HOH 44 244 244 HOH HOH A . R 6 HOH 45 245 245 HOH HOH A . R 6 HOH 46 246 246 HOH HOH A . R 6 HOH 47 247 247 HOH HOH A . R 6 HOH 48 248 248 HOH HOH A . R 6 HOH 49 249 249 HOH HOH A . R 6 HOH 50 250 250 HOH HOH A . R 6 HOH 51 251 251 HOH HOH A . R 6 HOH 52 252 252 HOH HOH A . R 6 HOH 53 253 253 HOH HOH A . R 6 HOH 54 254 254 HOH HOH A . R 6 HOH 55 255 255 HOH HOH A . R 6 HOH 56 256 256 HOH HOH A . R 6 HOH 57 257 257 HOH HOH A . R 6 HOH 58 258 258 HOH HOH A . R 6 HOH 59 259 259 HOH HOH A . R 6 HOH 60 260 260 HOH HOH A . R 6 HOH 61 261 261 HOH HOH A . R 6 HOH 62 262 262 HOH HOH A . R 6 HOH 63 263 263 HOH HOH A . R 6 HOH 64 264 264 HOH HOH A . R 6 HOH 65 265 265 HOH HOH A . R 6 HOH 66 266 266 HOH HOH A . R 6 HOH 67 267 267 HOH HOH A . R 6 HOH 68 268 268 HOH HOH A . R 6 HOH 69 269 269 HOH HOH A . R 6 HOH 70 270 270 HOH HOH A . R 6 HOH 71 271 271 HOH HOH A . R 6 HOH 72 272 272 HOH HOH A . R 6 HOH 73 273 273 HOH HOH A . R 6 HOH 74 274 274 HOH HOH A . R 6 HOH 75 275 275 HOH HOH A . R 6 HOH 76 276 276 HOH HOH A . R 6 HOH 77 277 277 HOH HOH A . R 6 HOH 78 278 278 HOH HOH A . R 6 HOH 79 279 279 HOH HOH A . R 6 HOH 80 280 280 HOH HOH A . R 6 HOH 81 281 281 HOH HOH A . R 6 HOH 82 282 282 HOH HOH A . R 6 HOH 83 283 283 HOH HOH A . R 6 HOH 84 284 284 HOH HOH A . R 6 HOH 85 285 285 HOH HOH A . R 6 HOH 86 286 286 HOH HOH A . R 6 HOH 87 287 287 HOH HOH A . R 6 HOH 88 288 288 HOH HOH A . R 6 HOH 89 289 289 HOH HOH A . R 6 HOH 90 290 290 HOH HOH A . R 6 HOH 91 291 291 HOH HOH A . R 6 HOH 92 292 292 HOH HOH A . R 6 HOH 93 293 293 HOH HOH A . R 6 HOH 94 294 294 HOH HOH A . R 6 HOH 95 295 295 HOH HOH A . R 6 HOH 96 296 296 HOH HOH A . R 6 HOH 97 297 297 HOH HOH A . R 6 HOH 98 298 298 HOH HOH A . R 6 HOH 99 299 299 HOH HOH A . R 6 HOH 100 300 300 HOH HOH A . R 6 HOH 101 301 301 HOH HOH A . R 6 HOH 102 302 302 HOH HOH A . R 6 HOH 103 303 303 HOH HOH A . R 6 HOH 104 304 304 HOH HOH A . R 6 HOH 105 305 305 HOH HOH A . R 6 HOH 106 306 306 HOH HOH A . R 6 HOH 107 307 307 HOH HOH A . R 6 HOH 108 308 308 HOH HOH A . R 6 HOH 109 309 309 HOH HOH A . R 6 HOH 110 310 310 HOH HOH A . R 6 HOH 111 311 311 HOH HOH A . R 6 HOH 112 312 312 HOH HOH A . R 6 HOH 113 313 313 HOH HOH A . R 6 HOH 114 314 314 HOH HOH A . R 6 HOH 115 315 315 HOH HOH A . R 6 HOH 116 316 316 HOH HOH A . R 6 HOH 117 317 317 HOH HOH A . R 6 HOH 118 318 318 HOH HOH A . R 6 HOH 119 319 319 HOH HOH A . R 6 HOH 120 320 320 HOH HOH A . R 6 HOH 121 321 321 HOH HOH A . R 6 HOH 122 322 322 HOH HOH A . R 6 HOH 123 323 323 HOH HOH A . R 6 HOH 124 324 324 HOH HOH A . R 6 HOH 125 325 325 HOH HOH A . R 6 HOH 126 326 326 HOH HOH A . R 6 HOH 127 327 327 HOH HOH A . R 6 HOH 128 328 328 HOH HOH A . R 6 HOH 129 329 329 HOH HOH A . R 6 HOH 130 330 330 HOH HOH A . R 6 HOH 131 331 331 HOH HOH A . S 6 HOH 1 201 201 HOH HOH B . S 6 HOH 2 202 202 HOH HOH B . S 6 HOH 3 203 203 HOH HOH B . S 6 HOH 4 204 204 HOH HOH B . S 6 HOH 5 205 205 HOH HOH B . S 6 HOH 6 206 206 HOH HOH B . S 6 HOH 7 207 207 HOH HOH B . S 6 HOH 8 208 208 HOH HOH B . S 6 HOH 9 209 209 HOH HOH B . S 6 HOH 10 210 210 HOH HOH B . S 6 HOH 11 211 211 HOH HOH B . S 6 HOH 12 212 212 HOH HOH B . S 6 HOH 13 213 213 HOH HOH B . S 6 HOH 14 214 214 HOH HOH B . S 6 HOH 15 215 215 HOH HOH B . S 6 HOH 16 216 216 HOH HOH B . S 6 HOH 17 217 217 HOH HOH B . S 6 HOH 18 218 218 HOH HOH B . S 6 HOH 19 219 219 HOH HOH B . S 6 HOH 20 220 220 HOH HOH B . S 6 HOH 21 221 221 HOH HOH B . S 6 HOH 22 222 222 HOH HOH B . S 6 HOH 23 223 223 HOH HOH B . S 6 HOH 24 224 224 HOH HOH B . S 6 HOH 25 225 225 HOH HOH B . S 6 HOH 26 226 226 HOH HOH B . S 6 HOH 27 227 227 HOH HOH B . S 6 HOH 28 228 228 HOH HOH B . S 6 HOH 29 229 229 HOH HOH B . S 6 HOH 30 230 230 HOH HOH B . S 6 HOH 31 231 231 HOH HOH B . S 6 HOH 32 232 232 HOH HOH B . S 6 HOH 33 233 233 HOH HOH B . S 6 HOH 34 234 234 HOH HOH B . S 6 HOH 35 235 235 HOH HOH B . S 6 HOH 36 236 236 HOH HOH B . S 6 HOH 37 237 237 HOH HOH B . S 6 HOH 38 238 238 HOH HOH B . S 6 HOH 39 239 239 HOH HOH B . S 6 HOH 40 240 240 HOH HOH B . S 6 HOH 41 241 241 HOH HOH B . S 6 HOH 42 242 242 HOH HOH B . S 6 HOH 43 243 243 HOH HOH B . S 6 HOH 44 244 244 HOH HOH B . S 6 HOH 45 245 245 HOH HOH B . S 6 HOH 46 246 246 HOH HOH B . S 6 HOH 47 247 247 HOH HOH B . S 6 HOH 48 248 248 HOH HOH B . S 6 HOH 49 249 249 HOH HOH B . S 6 HOH 50 250 250 HOH HOH B . S 6 HOH 51 251 251 HOH HOH B . S 6 HOH 52 252 252 HOH HOH B . S 6 HOH 53 253 253 HOH HOH B . S 6 HOH 54 254 254 HOH HOH B . S 6 HOH 55 255 255 HOH HOH B . S 6 HOH 56 256 256 HOH HOH B . S 6 HOH 57 257 257 HOH HOH B . S 6 HOH 58 258 258 HOH HOH B . S 6 HOH 59 259 259 HOH HOH B . S 6 HOH 60 260 260 HOH HOH B . S 6 HOH 61 261 261 HOH HOH 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 0 A ARG 33 ? NE ? A ARG 35 NE 2 1 Y 0 A ARG 33 ? CZ ? A ARG 35 CZ 3 1 Y 0 A ARG 33 ? NH1 ? A ARG 35 NH1 4 1 Y 0 A ARG 33 ? NH2 ? A ARG 35 NH2 5 1 Y 0 A ASN 52 ? CG ? A ASN 54 CG 6 1 Y 0 A ASN 52 ? OD1 ? A ASN 54 OD1 7 1 Y 0 A ASN 52 ? ND2 ? A ASN 54 ND2 8 1 Y 0 A GLU 75 ? CG ? A GLU 77 CG 9 1 Y 0 A GLU 75 ? CD ? A GLU 77 CD 10 1 Y 0 A GLU 75 ? OE1 ? A GLU 77 OE1 11 1 Y 0 A GLU 75 ? OE2 ? A GLU 77 OE2 12 1 Y 0 A GLU 87 ? CG ? A GLU 89 CG 13 1 Y 0 A GLU 87 ? CD ? A GLU 89 CD 14 1 Y 0 A GLU 87 ? OE1 ? A GLU 89 OE1 15 1 Y 0 A GLU 87 ? OE2 ? A GLU 89 OE2 16 1 Y 0 A LYS 91 ? CG ? A LYS 93 CG 17 1 Y 0 A LYS 91 ? CD ? A LYS 93 CD 18 1 Y 0 A LYS 91 ? CE ? A LYS 93 CE 19 1 Y 0 A LYS 91 ? NZ ? A LYS 93 NZ 20 1 Y 0 A GLN 149 ? CG ? A GLN 151 CG 21 1 Y 0 A GLN 149 ? CD ? A GLN 151 CD 22 1 Y 0 A GLN 149 ? OE1 ? A GLN 151 OE1 23 1 Y 0 A GLN 149 ? NE2 ? A GLN 151 NE2 24 1 Y 0 B GLU 80 ? CB ? B GLU 3 CB 25 1 Y 0 B GLU 80 ? CG ? B GLU 3 CG 26 1 Y 0 B GLU 80 ? CD ? B GLU 3 CD 27 1 Y 0 B GLU 80 ? OE1 ? B GLU 3 OE1 28 1 Y 0 B GLU 80 ? OE2 ? B GLU 3 OE2 29 1 Y 0 B ARG 87 ? NE ? B ARG 10 NE 30 1 Y 0 B ARG 87 ? CZ ? B ARG 10 CZ 31 1 Y 0 B ARG 87 ? NH1 ? B ARG 10 NH1 32 1 Y 0 B ARG 87 ? NH2 ? B ARG 10 NH2 33 1 Y 0 B LYS 90 ? CG ? B LYS 13 CG 34 1 Y 0 B LYS 90 ? CD ? B LYS 13 CD 35 1 Y 0 B LYS 90 ? CE ? B LYS 13 CE 36 1 Y 0 B LYS 90 ? NZ ? B LYS 13 NZ 37 1 Y 0 B GLU 97 ? CG ? B GLU 20 CG 38 1 Y 0 B GLU 97 ? CD ? B GLU 20 CD 39 1 Y 0 B GLU 97 ? OE1 ? B GLU 20 OE1 40 1 Y 0 B GLU 97 ? OE2 ? B GLU 20 OE2 41 1 Y 0 B ARG 99 ? CD ? B ARG 22 CD 42 1 Y 0 B ARG 99 ? NE ? B ARG 22 NE 43 1 Y 0 B ARG 99 ? CZ ? B ARG 22 CZ 44 1 Y 0 B ARG 99 ? NH1 ? B ARG 22 NH1 45 1 Y 0 B ARG 99 ? NH2 ? B ARG 22 NH2 46 1 Y 0 B GLN 118 ? CD ? B GLN 41 CD 47 1 Y 0 B GLN 118 ? OE1 ? B GLN 41 OE1 48 1 Y 0 B GLN 118 ? NE2 ? B GLN 41 NE2 49 1 Y 0 B GLN 134 ? CD ? B GLN 57 CD 50 1 Y 0 B GLN 134 ? OE1 ? B GLN 57 OE1 51 1 Y 0 B GLN 134 ? NE2 ? B GLN 57 NE2 52 1 Y 0 B LYS 143 ? CE ? B LYS 66 CE 53 1 Y 0 B LYS 143 ? NZ ? B LYS 66 NZ # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(phenix.refine: 1.4_122)' ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 # _cell.entry_id 3PHX _cell.length_a 41.520 _cell.length_b 37.100 _cell.length_c 84.350 _cell.angle_alpha 90.00 _cell.angle_beta 94.24 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3PHX _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 _symmetry.space_group_name_Hall ? # _exptl.entry_id 3PHX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.15 _exptl_crystal.density_percent_sol 42.84 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '10% PEG8K, 0.2M zinc acetate, 0.1M MES sodium salt, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' # _diffrn.id 1 _diffrn.ambient_temp 77 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.pdbx_collection_date 2010-06-12 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l ? _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9800 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-4' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-4 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.9800 # _reflns.entry_id 3PHX _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.0 _reflns.d_resolution_high 1.6 _reflns.number_obs 33549 _reflns.number_all ? _reflns.percent_possible_obs ? _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3PHX _refine.ls_number_reflns_obs 32537 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.0 _refine.ls_d_res_high 1.600 _refine.ls_percent_reflns_obs 95.15 _refine.ls_R_factor_obs 0.1421 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1395 _refine.ls_R_factor_R_free 0.1919 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.94 _refine.ls_number_reflns_R_free 1607 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] 1.7409 _refine.aniso_B[2][2] -2.2719 _refine.aniso_B[3][3] -1.3003 _refine.aniso_B[1][2] -0.0000 _refine.aniso_B[1][3] -1.5703 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.438 _refine.solvent_model_param_bsol 55.659 _refine.pdbx_solvent_vdw_probe_radii 1.10 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.83 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.18 _refine.pdbx_overall_phase_error 17.27 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1921 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 23 _refine_hist.number_atoms_solvent 192 _refine_hist.number_atoms_total 2136 _refine_hist.d_res_high 1.600 _refine_hist.d_res_low 30.0 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.016 ? ? 1980 'X-RAY DIFFRACTION' ? f_angle_d 1.395 ? ? 2679 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.955 ? ? 728 'X-RAY DIFFRACTION' ? f_chiral_restr 0.104 ? ? 291 'X-RAY DIFFRACTION' ? f_plane_restr 0.007 ? ? 347 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 1.6000 1.6572 2837 0.1778 89.00 0.2558 . . 172 . . . . 'X-RAY DIFFRACTION' . 1.6572 1.7235 2937 0.1575 91.00 0.2486 . . 170 . . . . 'X-RAY DIFFRACTION' . 1.7235 1.8020 2988 0.1265 93.00 0.2147 . . 144 . . . . 'X-RAY DIFFRACTION' . 1.8020 1.8970 3063 0.1078 94.00 0.1848 . . 132 . . . . 'X-RAY DIFFRACTION' . 1.8970 2.0158 3097 0.1050 96.00 0.1694 . . 153 . . . . 'X-RAY DIFFRACTION' . 2.0158 2.1714 3143 0.1154 97.00 0.2072 . . 185 . . . . 'X-RAY DIFFRACTION' . 2.1714 2.3898 3165 0.1169 98.00 0.1795 . . 161 . . . . 'X-RAY DIFFRACTION' . 2.3898 2.7354 3206 0.1276 98.00 0.1593 . . 166 . . . . 'X-RAY DIFFRACTION' . 2.7354 3.4456 3211 0.1349 98.00 0.1818 . . 157 . . . . 'X-RAY DIFFRACTION' . 3.4456 30.0 3283 0.1762 97.00 0.1959 . . 167 . . . . # _database_PDB_matrix.entry_id 3PHX _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 3PHX _struct.title 'OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with ISG15' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3PHX _struct_keywords.pdbx_keywords 'Hydrolase/Protein Binding' _struct_keywords.text 'OTU domain, De-ubiquitinase, De-ISGylase, Hydrolase-Protein Binding complex' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 3 ? K N N 3 ? L N N 4 ? M N N 5 ? N N N 3 ? O N N 3 ? P N N 3 ? Q N N 4 ? R N N 6 ? S N N 6 ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP L_CCHFI Q6TQR6 1 ;MDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSYHYIKRLTESAARKYYQEEPEAR LVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIIIWTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQ FETDTREALSLMDRVIAVDQLTS ; 1 ? 2 UNP ISG15_HUMAN P05161 2 DEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRG 79 ? # 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 3PHX A 3 ? 185 ? Q6TQR6 1 ? 183 ? 1 183 2 2 3PHX B 2 ? 79 ? P05161 79 ? 156 ? 79 156 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3PHX GLY A 1 ? UNP Q6TQR6 ? ? 'expression tag' -1 1 1 3PHX PRO A 2 ? UNP Q6TQR6 ? ? 'expression tag' 0 2 2 3PHX MET B 1 ? UNP P05161 ? ? 'expression tag' 78 3 # 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 ? dimeric 2 2 software_defined_assembly PISA dimeric 2 # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 2 'ABSA (A^2)' 1520 ? 2 MORE -336 ? 2 'SSA (A^2)' 13430 ? # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S 2 1 A,C,D,E,F,G,H,I,J,K,L,R 2 2 B,M,N,O,P,Q,S # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 1_455 x-1,y,z 1.0000000000 0.0000000000 0.0000000000 -41.5200000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 4 ? LEU A 9 ? ASP A 2 LEU A 7 5 ? 6 HELX_P HELX_P2 2 ASN A 26 ? TYR A 30 ? ASN A 24 TYR A 28 1 ? 5 HELX_P HELX_P3 3 ASN A 41 ? MET A 52 ? ASN A 39 MET A 50 1 ? 12 HELX_P HELX_P4 4 SER A 59 ? TYR A 75 ? SER A 57 TYR A 73 1 ? 17 HELX_P HELX_P5 5 GLN A 76 ? PRO A 79 ? GLN A 74 PRO A 77 5 ? 4 HELX_P HELX_P6 6 GLU A 80 ? GLY A 85 ? GLU A 78 GLY A 83 1 ? 6 HELX_P HELX_P7 7 SER A 87 ? LEU A 96 ? SER A 85 LEU A 94 1 ? 10 HELX_P HELX_P8 8 THR A 104 ? GLY A 115 ? THR A 102 GLY A 113 1 ? 12 HELX_P HELX_P9 9 PRO A 161 ? GLU A 164 ? PRO A 159 GLU A 162 5 ? 4 HELX_P HELX_P10 10 THR B 26 ? GLY B 39 ? THR B 103 GLY B 116 1 ? 14 HELX_P HELX_P11 11 GLN B 41 ? ASP B 43 ? GLN B 118 ASP B 120 5 ? 3 HELX_P HELX_P12 12 PRO B 59 ? GLY B 64 ? PRO B 136 GLY B 141 5 ? 6 # _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 covale1 covale none ? A CYS 42 SG ? ? ? 1_555 M NEH . CB ? ? A CYS 40 B NEH 157 1_555 ? ? ? ? ? ? ? 1.779 ? ? covale2 covale both ? B GLY 79 C ? ? ? 1_555 M NEH . N ? ? B GLY 156 B NEH 157 1_555 ? ? ? ? ? ? ? 1.461 ? ? metalc1 metalc ? ? A GLY 1 N ? ? ? 1_555 K ZN . ZN ? ? A GLY -1 A ZN 192 1_555 ? ? ? ? ? ? ? 2.001 ? ? metalc2 metalc ? ? A GLY 1 O ? ? ? 1_555 K ZN . ZN ? ? A GLY -1 A ZN 192 1_555 ? ? ? ? ? ? ? 2.224 ? ? metalc3 metalc ? ? A ASP 4 OD1 ? ? ? 1_555 K ZN . ZN ? ? A ASP 2 A ZN 192 1_555 ? ? ? ? ? ? ? 2.054 ? ? metalc4 metalc ? ? A ASP 10 OD1 ? ? ? 1_555 D ZN . ZN ? ? A ASP 8 A ZN 185 1_555 ? ? ? ? ? ? ? 1.987 ? ? metalc5 metalc ? ? A ASP 10 OD2 ? ? ? 1_555 E ZN . ZN ? ? A ASP 8 A ZN 186 1_555 ? ? ? ? ? ? ? 2.069 ? ? metalc6 metalc ? ? A ASN 26 ND2 ? ? ? 1_555 F ZN . ZN ? ? A ASN 24 A ZN 187 1_555 ? ? ? ? ? ? ? 2.122 ? ? metalc7 metalc ? ? A ASP 39 OD2 ? ? ? 1_555 J ZN . ZN ? ? A ASP 37 A ZN 191 1_555 ? ? ? ? ? ? ? 1.946 ? ? metalc8 metalc ? ? A HIS 45 NE2 ? ? ? 1_555 J ZN . ZN ? ? A HIS 43 A ZN 191 1_555 ? ? ? ? ? ? ? 2.055 ? ? metalc9 metalc ? ? A GLU 49 OE2 ? ? ? 1_555 I ZN . ZN ? ? A GLU 47 A ZN 190 1_555 ? ? ? ? ? ? ? 2.194 ? ? metalc10 metalc ? ? A ASP 90 OD1 ? ? ? 1_555 H ZN . ZN ? ? A ASP 88 A ZN 189 1_555 ? ? ? ? ? ? ? 2.128 ? ? metalc11 metalc ? ? A HIS 153 NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS 151 A ZN 188 1_555 ? ? ? ? ? ? ? 2.008 ? ? metalc12 metalc ? ? A ASP 155 OD1 ? ? ? 1_555 G ZN . ZN ? ? A ASP 153 A ZN 188 1_555 ? ? ? ? ? ? ? 2.027 ? ? metalc13 metalc ? ? A ASP 155 OD2 ? ? ? 1_555 G ZN . ZN ? ? A ASP 153 A ZN 188 1_555 ? ? ? ? ? ? ? 2.630 ? ? metalc14 metalc ? ? C ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 184 A HOH 318 1_555 ? ? ? ? ? ? ? 2.080 ? ? metalc15 metalc ? ? D ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 185 A HOH 255 1_555 ? ? ? ? ? ? ? 2.238 ? ? metalc16 metalc ? ? D ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 185 A HOH 268 1_555 ? ? ? ? ? ? ? 1.982 ? ? metalc17 metalc ? ? E ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 186 A HOH 262 1_555 ? ? ? ? ? ? ? 1.991 ? ? metalc18 metalc ? ? E ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 186 A HOH 266 1_555 ? ? ? ? ? ? ? 2.030 ? ? metalc19 metalc ? ? F ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 187 A HOH 320 1_555 ? ? ? ? ? ? ? 2.274 ? ? metalc20 metalc ? ? G ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 188 A HOH 258 1_555 ? ? ? ? ? ? ? 2.204 ? ? metalc21 metalc ? ? G ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 188 A HOH 259 1_555 ? ? ? ? ? ? ? 2.062 ? ? metalc22 metalc ? ? H ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 189 A HOH 330 1_555 ? ? ? ? ? ? ? 2.574 ? ? metalc23 metalc ? ? H ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 189 A HOH 331 1_555 ? ? ? ? ? ? ? 2.583 ? ? metalc24 metalc ? ? J ZN . ZN ? ? ? 1_555 L ACY . OXT ? ? A ZN 191 A ACY 193 1_555 ? ? ? ? ? ? ? 1.926 ? ? metalc25 metalc ? ? J ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 191 A HOH 254 1_555 ? ? ? ? ? ? ? 2.246 ? ? metalc26 metalc ? ? K ZN . ZN ? ? ? 1_555 R HOH . O ? ? A ZN 192 A HOH 270 1_555 ? ? ? ? ? ? ? 2.427 ? ? metalc27 metalc ? ? N ZN . ZN ? ? ? 1_555 B HIS 29 NE2 ? ? B ZN 1 B HIS 106 1_555 ? ? ? ? ? ? ? 1.992 ? ? metalc28 metalc ? ? O ZN . ZN ? ? ? 1_555 B HIS 29 ND1 ? ? B ZN 2 B HIS 106 1_555 ? ? ? ? ? ? ? 2.359 ? ? metalc29 metalc ? ? O ZN . ZN ? ? ? 1_555 B GLN 32 OE1 ? ? B ZN 2 B GLN 109 1_555 ? ? ? ? ? ? ? 2.052 ? ? metalc30 metalc ? ? P ZN . ZN ? ? ? 1_555 Q ACY . O ? ? B ZN 3 B ACY 4 1_555 ? ? ? ? ? ? ? 2.067 ? ? metalc31 metalc ? ? P ZN . ZN ? ? ? 1_555 B ASP 42 OD2 ? ? B ZN 3 B ASP 119 1_555 ? ? ? ? ? ? ? 2.051 ? ? metalc32 metalc ? ? P ZN . ZN ? ? ? 1_555 S HOH . O ? ? B ZN 3 B HOH 240 1_555 ? ? ? ? ? ? ? 2.255 ? ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference covale ? ? metalc ? ? # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 N ? A GLY 1 ? A GLY -1 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 O ? A GLY 1 ? A GLY -1 ? 1_555 80.2 ? 2 N ? A GLY 1 ? A GLY -1 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 OD1 ? A ASP 4 ? A ASP 2 ? 1_555 133.9 ? 3 O ? A GLY 1 ? A GLY -1 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 OD1 ? A ASP 4 ? A ASP 2 ? 1_555 85.4 ? 4 N ? A GLY 1 ? A GLY -1 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 O ? R HOH . ? A HOH 270 ? 1_555 129.9 ? 5 O ? A GLY 1 ? A GLY -1 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 O ? R HOH . ? A HOH 270 ? 1_555 96.2 ? 6 OD1 ? A ASP 4 ? A ASP 2 ? 1_555 ZN ? K ZN . ? A ZN 192 ? 1_555 O ? R HOH . ? A HOH 270 ? 1_555 94.9 ? 7 OD1 ? A ASP 10 ? A ASP 8 ? 1_555 ZN ? D ZN . ? A ZN 185 ? 1_555 O ? R HOH . ? A HOH 255 ? 1_555 110.6 ? 8 OD1 ? A ASP 10 ? A ASP 8 ? 1_555 ZN ? D ZN . ? A ZN 185 ? 1_555 O ? R HOH . ? A HOH 268 ? 1_555 75.9 ? 9 O ? R HOH . ? A HOH 255 ? 1_555 ZN ? D ZN . ? A ZN 185 ? 1_555 O ? R HOH . ? A HOH 268 ? 1_555 172.5 ? 10 OD2 ? A ASP 10 ? A ASP 8 ? 1_555 ZN ? E ZN . ? A ZN 186 ? 1_555 O ? R HOH . ? A HOH 262 ? 1_555 93.7 ? 11 OD2 ? A ASP 10 ? A ASP 8 ? 1_555 ZN ? E ZN . ? A ZN 186 ? 1_555 O ? R HOH . ? A HOH 266 ? 1_555 172.0 ? 12 O ? R HOH . ? A HOH 262 ? 1_555 ZN ? E ZN . ? A ZN 186 ? 1_555 O ? R HOH . ? A HOH 266 ? 1_555 85.7 ? 13 ND2 ? A ASN 26 ? A ASN 24 ? 1_555 ZN ? F ZN . ? A ZN 187 ? 1_555 O ? R HOH . ? A HOH 320 ? 1_555 104.4 ? 14 OD2 ? A ASP 39 ? A ASP 37 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 NE2 ? A HIS 45 ? A HIS 43 ? 1_555 123.8 ? 15 OD2 ? A ASP 39 ? A ASP 37 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 OXT ? L ACY . ? A ACY 193 ? 1_555 102.8 ? 16 NE2 ? A HIS 45 ? A HIS 43 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 OXT ? L ACY . ? A ACY 193 ? 1_555 107.2 ? 17 OD2 ? A ASP 39 ? A ASP 37 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 O ? R HOH . ? A HOH 254 ? 1_555 106.7 ? 18 NE2 ? A HIS 45 ? A HIS 43 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 O ? R HOH . ? A HOH 254 ? 1_555 106.1 ? 19 OXT ? L ACY . ? A ACY 193 ? 1_555 ZN ? J ZN . ? A ZN 191 ? 1_555 O ? R HOH . ? A HOH 254 ? 1_555 109.8 ? 20 OD1 ? A ASP 90 ? A ASP 88 ? 1_555 ZN ? H ZN . ? A ZN 189 ? 1_555 O ? R HOH . ? A HOH 330 ? 1_555 129.8 ? 21 OD1 ? A ASP 90 ? A ASP 88 ? 1_555 ZN ? H ZN . ? A ZN 189 ? 1_555 O ? R HOH . ? A HOH 331 ? 1_555 92.6 ? 22 O ? R HOH . ? A HOH 330 ? 1_555 ZN ? H ZN . ? A ZN 189 ? 1_555 O ? R HOH . ? A HOH 331 ? 1_555 60.6 ? 23 NE2 ? A HIS 153 ? A HIS 151 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 OD1 ? A ASP 155 ? A ASP 153 ? 1_555 109.1 ? 24 NE2 ? A HIS 153 ? A HIS 151 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 OD2 ? A ASP 155 ? A ASP 153 ? 1_555 86.0 ? 25 OD1 ? A ASP 155 ? A ASP 153 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 OD2 ? A ASP 155 ? A ASP 153 ? 1_555 55.3 ? 26 NE2 ? A HIS 153 ? A HIS 151 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 258 ? 1_555 118.3 ? 27 OD1 ? A ASP 155 ? A ASP 153 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 258 ? 1_555 116.8 ? 28 OD2 ? A ASP 155 ? A ASP 153 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 258 ? 1_555 88.2 ? 29 NE2 ? A HIS 153 ? A HIS 151 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 259 ? 1_555 110.1 ? 30 OD1 ? A ASP 155 ? A ASP 153 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 259 ? 1_555 101.7 ? 31 OD2 ? A ASP 155 ? A ASP 153 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 259 ? 1_555 156.1 ? 32 O ? R HOH . ? A HOH 258 ? 1_555 ZN ? G ZN . ? A ZN 188 ? 1_555 O ? R HOH . ? A HOH 259 ? 1_555 98.7 ? 33 ND1 ? B HIS 29 ? B HIS 106 ? 1_555 ZN ? O ZN . ? B ZN 2 ? 1_555 OE1 ? B GLN 32 ? B GLN 109 ? 1_555 81.8 ? 34 O ? Q ACY . ? B ACY 4 ? 1_555 ZN ? P ZN . ? B ZN 3 ? 1_555 OD2 ? B ASP 42 ? B ASP 119 ? 1_555 107.8 ? 35 O ? Q ACY . ? B ACY 4 ? 1_555 ZN ? P ZN . ? B ZN 3 ? 1_555 O ? S HOH . ? B HOH 240 ? 1_555 154.0 ? 36 OD2 ? B ASP 42 ? B ASP 119 ? 1_555 ZN ? P ZN . ? B ZN 3 ? 1_555 O ? S HOH . ? B HOH 240 ? 1_555 86.8 ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 2 ? C ? 5 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 THR A 12 ? ILE A 15 ? THR A 10 ILE A 13 A 2 GLN A 18 ? SER A 21 ? GLN A 16 SER A 19 A 3 ALA A 131 ? PHE A 135 ? ALA A 129 PHE A 133 A 4 ILE A 118 ? THR A 122 ? ILE A 116 THR A 120 A 5 VAL A 144 ? SER A 149 ? VAL A 142 SER A 147 A 6 HIS A 153 ? ILE A 159 ? HIS A 151 ILE A 157 A 7 PHE A 31 ? VAL A 34 ? PHE A 29 VAL A 32 B 1 GLY A 102 ? SER A 103 ? GLY A 100 SER A 101 B 2 ARG B 78 ? GLY B 79 ? ARG B 155 GLY B 156 C 1 SER B 16 ? VAL B 21 ? SER B 93 VAL B 98 C 2 LEU B 5 ? ARG B 10 ? LEU B 82 ARG B 87 C 3 THR B 70 ? LEU B 75 ? THR B 147 LEU B 152 C 4 PHE B 45 ? PHE B 49 ? PHE B 122 PHE B 126 C 5 LYS B 52 ? PRO B 53 ? LYS B 129 PRO B 130 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N THR A 12 ? N THR A 10 O VAL A 20 ? O VAL A 18 A 2 3 N TYR A 19 ? N TYR A 17 O LYS A 134 ? O LYS A 132 A 3 4 O PHE A 135 ? O PHE A 133 N ILE A 118 ? N ILE A 116 A 4 5 N ILE A 119 ? N ILE A 117 O LEU A 146 ? O LEU A 144 A 5 6 N LEU A 147 ? N LEU A 145 O ASP A 155 ? O ASP A 153 A 6 7 O ARG A 158 ? O ARG A 156 N GLU A 32 ? N GLU A 30 B 1 2 N GLY A 102 ? N GLY A 100 O GLY B 79 ? O GLY B 156 C 1 2 O VAL B 21 ? O VAL B 98 N LEU B 5 ? N LEU B 82 C 2 3 N ARG B 10 ? N ARG B 87 O VAL B 71 ? O VAL B 148 C 3 4 O ASN B 74 ? O ASN B 151 N TRP B 46 ? N TRP B 123 C 4 5 N PHE B 49 ? N PHE B 126 O LYS B 52 ? O LYS B 129 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software A ZN 184 ? 6 'BINDING SITE FOR RESIDUE ZN A 184' AC2 Software A ZN 185 ? 6 'BINDING SITE FOR RESIDUE ZN A 185' AC3 Software A ZN 186 ? 5 'BINDING SITE FOR RESIDUE ZN A 186' AC4 Software A ZN 187 ? 3 'BINDING SITE FOR RESIDUE ZN A 187' AC5 Software A ZN 188 ? 4 'BINDING SITE FOR RESIDUE ZN A 188' AC6 Software A ZN 189 ? 5 'BINDING SITE FOR RESIDUE ZN A 189' AC7 Software A ZN 190 ? 1 'BINDING SITE FOR RESIDUE ZN A 190' AC8 Software A ZN 191 ? 5 'BINDING SITE FOR RESIDUE ZN A 191' AC9 Software A ZN 192 ? 4 'BINDING SITE FOR RESIDUE ZN A 192' BC1 Software A ACY 193 ? 11 'BINDING SITE FOR RESIDUE ACY A 193' BC2 Software B NEH 157 ? 5 'BINDING SITE FOR RESIDUE NEH B 157' BC3 Software B ZN 1 ? 1 'BINDING SITE FOR RESIDUE ZN B 1' BC4 Software B ZN 2 ? 2 'BINDING SITE FOR RESIDUE ZN B 2' BC5 Software B ZN 3 ? 3 'BINDING SITE FOR RESIDUE ZN B 3' BC6 Software B ACY 4 ? 2 'BINDING SITE FOR RESIDUE ACY B 4' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 HIS A 45 ? HIS A 43 . ? 1_555 ? 2 AC1 6 LYS A 55 ? LYS A 53 . ? 1_555 ? 3 AC1 6 ASP A 57 ? ASP A 55 . ? 1_555 ? 4 AC1 6 SER A 59 ? SER A 57 . ? 1_555 ? 5 AC1 6 TYR A 60 ? TYR A 58 . ? 1_555 ? 6 AC1 6 HOH R . ? HOH A 318 . ? 1_555 ? 7 AC2 6 SER A 8 ? SER A 6 . ? 1_555 ? 8 AC2 6 ASP A 10 ? ASP A 8 . ? 1_555 ? 9 AC2 6 HIS A 58 ? HIS A 56 . ? 1_655 ? 10 AC2 6 HIS A 61 ? HIS A 59 . ? 1_655 ? 11 AC2 6 HOH R . ? HOH A 255 . ? 1_555 ? 12 AC2 6 HOH R . ? HOH A 268 . ? 1_555 ? 13 AC3 5 ASP A 10 ? ASP A 8 . ? 1_555 ? 14 AC3 5 ASP A 98 ? ASP A 96 . ? 1_655 ? 15 AC3 5 ACY L . ? ACY A 193 . ? 1_655 ? 16 AC3 5 HOH R . ? HOH A 262 . ? 1_555 ? 17 AC3 5 HOH R . ? HOH A 266 . ? 1_555 ? 18 AC4 3 ASN A 26 ? ASN A 24 . ? 1_555 ? 19 AC4 3 GLU A 128 ? GLU A 126 . ? 1_555 ? 20 AC4 3 HOH R . ? HOH A 320 . ? 1_555 ? 21 AC5 4 HIS A 153 ? HIS A 151 . ? 1_555 ? 22 AC5 4 ASP A 155 ? ASP A 153 . ? 1_555 ? 23 AC5 4 HOH R . ? HOH A 258 . ? 1_555 ? 24 AC5 4 HOH R . ? HOH A 259 . ? 1_555 ? 25 AC6 5 ASP A 90 ? ASP A 88 . ? 1_555 ? 26 AC6 5 HOH R . ? HOH A 234 . ? 1_555 ? 27 AC6 5 HOH R . ? HOH A 330 . ? 1_555 ? 28 AC6 5 HOH R . ? HOH A 331 . ? 1_555 ? 29 AC6 5 GLU B 50 ? GLU B 127 . ? 1_455 ? 30 AC7 1 GLU A 49 ? GLU A 47 . ? 1_555 ? 31 AC8 5 PRO A 37 ? PRO A 35 . ? 1_555 ? 32 AC8 5 ASP A 39 ? ASP A 37 . ? 1_555 ? 33 AC8 5 HIS A 45 ? HIS A 43 . ? 1_555 ? 34 AC8 5 ACY L . ? ACY A 193 . ? 1_555 ? 35 AC8 5 HOH R . ? HOH A 254 . ? 1_555 ? 36 AC9 4 GLY A 1 ? GLY A -1 . ? 1_555 ? 37 AC9 4 ASP A 4 ? ASP A 2 . ? 1_555 ? 38 AC9 4 ASP A 57 ? ASP A 55 . ? 1_655 ? 39 AC9 4 HOH R . ? HOH A 270 . ? 1_555 ? 40 BC1 11 ASP A 10 ? ASP A 8 . ? 1_455 ? 41 BC1 11 ASP A 39 ? ASP A 37 . ? 1_555 ? 42 BC1 11 ASN A 41 ? ASN A 39 . ? 1_555 ? 43 BC1 11 HIS A 45 ? HIS A 43 . ? 1_555 ? 44 BC1 11 HIS A 58 ? HIS A 56 . ? 1_555 ? 45 BC1 11 TYR A 60 ? TYR A 58 . ? 1_555 ? 46 BC1 11 ASP A 98 ? ASP A 96 . ? 1_555 ? 47 BC1 11 ZN E . ? ZN A 186 . ? 1_455 ? 48 BC1 11 ZN J . ? ZN A 191 . ? 1_555 ? 49 BC1 11 HOH R . ? HOH A 266 . ? 1_455 ? 50 BC1 11 HOH R . ? HOH A 268 . ? 1_455 ? 51 BC2 5 ASP A 39 ? ASP A 37 . ? 1_555 ? 52 BC2 5 CYS A 42 ? CYS A 40 . ? 1_555 ? 53 BC2 5 TRP A 101 ? TRP A 99 . ? 1_555 ? 54 BC2 5 THR A 152 ? THR A 150 . ? 1_555 ? 55 BC2 5 GLY B 79 ? GLY B 156 . ? 1_555 ? 56 BC3 1 HIS B 29 ? HIS B 106 . ? 1_555 ? 57 BC4 2 HIS B 29 ? HIS B 106 . ? 1_555 ? 58 BC4 2 GLN B 32 ? GLN B 109 . ? 1_555 ? 59 BC5 3 ACY Q . ? ACY B 4 . ? 1_555 ? 60 BC5 3 ASP B 42 ? ASP B 119 . ? 1_555 ? 61 BC5 3 HOH S . ? HOH B 240 . ? 1_555 ? 62 BC6 2 ZN P . ? ZN B 3 . ? 1_555 ? 63 BC6 2 ASP B 42 ? ASP B 119 . ? 1_555 ? # _pdbx_entry_details.entry_id 3PHX _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 N # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 OD2 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 ASP _pdbx_validate_close_contact.auth_seq_id_1 137 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 257 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.17 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 NE _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ARG _pdbx_validate_rmsd_angle.auth_seq_id_1 80 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CZ _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ARG _pdbx_validate_rmsd_angle.auth_seq_id_2 80 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 NH2 _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 ARG _pdbx_validate_rmsd_angle.auth_seq_id_3 80 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 116.88 _pdbx_validate_rmsd_angle.angle_target_value 120.30 _pdbx_validate_rmsd_angle.angle_deviation -3.42 _pdbx_validate_rmsd_angle.angle_standard_deviation 0.50 _pdbx_validate_rmsd_angle.linker_flag N # _pdbx_validate_torsion.id 1 _pdbx_validate_torsion.PDB_model_num 1 _pdbx_validate_torsion.auth_comp_id THR _pdbx_validate_torsion.auth_asym_id A _pdbx_validate_torsion.auth_seq_id 150 _pdbx_validate_torsion.PDB_ins_code ? _pdbx_validate_torsion.label_alt_id ? _pdbx_validate_torsion.phi -145.19 _pdbx_validate_torsion.psi 12.28 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ALA 122 ? A ALA 124 2 1 Y 1 A ALA 123 ? A ALA 125 3 1 Y 1 A THR 163 ? A THR 165 4 1 Y 1 A ASP 164 ? A ASP 166 5 1 Y 1 A THR 165 ? A THR 167 6 1 Y 1 A ARG 166 ? A ARG 168 7 1 Y 1 A GLU 167 ? A GLU 169 8 1 Y 1 A ALA 168 ? A ALA 170 9 1 Y 1 A LEU 169 ? A LEU 171 10 1 Y 1 A SER 170 ? A SER 172 11 1 Y 1 A LEU 171 ? A LEU 173 12 1 Y 1 A MET 172 ? A MET 174 13 1 Y 1 A ASP 173 ? A ASP 175 14 1 Y 1 A ARG 174 ? A ARG 176 15 1 Y 1 A VAL 175 ? A VAL 177 16 1 Y 1 A ILE 176 ? A ILE 178 17 1 Y 1 A ALA 177 ? A ALA 179 18 1 Y 1 A VAL 178 ? A VAL 180 19 1 Y 1 A ASP 179 ? A ASP 181 20 1 Y 1 A GLN 180 ? A GLN 182 21 1 Y 1 A LEU 181 ? A LEU 183 22 1 Y 1 A THR 182 ? A THR 184 23 1 Y 1 A SER 183 ? A SER 185 24 1 Y 1 B MET 78 ? B MET 1 25 1 Y 1 B ASP 79 ? B ASP 2 # 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 ACY C C N N 1 ACY O O N N 2 ACY OXT O N N 3 ACY CH3 C N N 4 ACY HXT H N N 5 ACY H1 H N N 6 ACY H2 H N N 7 ACY H3 H N N 8 ALA N N N N 9 ALA CA C N S 10 ALA C C N N 11 ALA O O N N 12 ALA CB C N N 13 ALA OXT O N N 14 ALA H H N N 15 ALA H2 H N N 16 ALA HA H N N 17 ALA HB1 H N N 18 ALA HB2 H N N 19 ALA HB3 H N N 20 ALA HXT H N N 21 ARG N N N N 22 ARG CA C N S 23 ARG C C N N 24 ARG O O N N 25 ARG CB C N N 26 ARG CG C N N 27 ARG CD C N N 28 ARG NE N N N 29 ARG CZ C N N 30 ARG NH1 N N N 31 ARG NH2 N N N 32 ARG OXT O N N 33 ARG H H N N 34 ARG H2 H N N 35 ARG HA H N N 36 ARG HB2 H N N 37 ARG HB3 H N N 38 ARG HG2 H N N 39 ARG HG3 H N N 40 ARG HD2 H N N 41 ARG HD3 H N N 42 ARG HE H N N 43 ARG HH11 H N N 44 ARG HH12 H N N 45 ARG HH21 H N N 46 ARG HH22 H N N 47 ARG HXT H N N 48 ASN N N N N 49 ASN CA C N S 50 ASN C C N N 51 ASN O O N N 52 ASN CB C N N 53 ASN CG C N N 54 ASN OD1 O N N 55 ASN ND2 N N N 56 ASN OXT O N N 57 ASN H H N N 58 ASN H2 H N N 59 ASN HA H N N 60 ASN HB2 H N N 61 ASN HB3 H N N 62 ASN HD21 H N N 63 ASN HD22 H N N 64 ASN HXT H N N 65 ASP N N N N 66 ASP CA C N S 67 ASP C C N N 68 ASP O O N N 69 ASP CB C N N 70 ASP CG C N N 71 ASP OD1 O N N 72 ASP OD2 O N N 73 ASP OXT O N N 74 ASP H H N N 75 ASP H2 H N N 76 ASP HA H N N 77 ASP HB2 H N N 78 ASP HB3 H N N 79 ASP HD2 H N N 80 ASP HXT H N N 81 CYS N N N N 82 CYS CA C N R 83 CYS C C N N 84 CYS O O N N 85 CYS CB C N N 86 CYS SG S N N 87 CYS OXT O N N 88 CYS H H N N 89 CYS H2 H N N 90 CYS HA H N N 91 CYS HB2 H N N 92 CYS HB3 H N N 93 CYS HG H N N 94 CYS HXT H N N 95 GLN N N N N 96 GLN CA C N S 97 GLN C C N N 98 GLN O O N N 99 GLN CB C N N 100 GLN CG C N N 101 GLN CD C N N 102 GLN OE1 O N N 103 GLN NE2 N N N 104 GLN OXT O N N 105 GLN H H N N 106 GLN H2 H N N 107 GLN HA H N N 108 GLN HB2 H N N 109 GLN HB3 H N N 110 GLN HG2 H N N 111 GLN HG3 H N N 112 GLN HE21 H N N 113 GLN HE22 H N N 114 GLN HXT H N N 115 GLU N N N N 116 GLU CA C N S 117 GLU C C N N 118 GLU O O N N 119 GLU CB C N N 120 GLU CG C N N 121 GLU CD C N N 122 GLU OE1 O N N 123 GLU OE2 O N N 124 GLU OXT O N N 125 GLU H H N N 126 GLU H2 H N N 127 GLU HA H N N 128 GLU HB2 H N N 129 GLU HB3 H N N 130 GLU HG2 H N N 131 GLU HG3 H N N 132 GLU HE2 H N N 133 GLU HXT H N N 134 GLY N N N N 135 GLY CA C N N 136 GLY C C N N 137 GLY O O N N 138 GLY OXT O N N 139 GLY H H N N 140 GLY H2 H N N 141 GLY HA2 H N N 142 GLY HA3 H N N 143 GLY HXT H N N 144 HIS N N N N 145 HIS CA C N S 146 HIS C C N N 147 HIS O O N N 148 HIS CB C N N 149 HIS CG C Y N 150 HIS ND1 N Y N 151 HIS CD2 C Y N 152 HIS CE1 C Y N 153 HIS NE2 N Y N 154 HIS OXT O N N 155 HIS H H N N 156 HIS H2 H N N 157 HIS HA H N N 158 HIS HB2 H N N 159 HIS HB3 H N N 160 HIS HD1 H N N 161 HIS HD2 H N N 162 HIS HE1 H N N 163 HIS HE2 H N N 164 HIS HXT H N N 165 HOH O O N N 166 HOH H1 H N N 167 HOH H2 H N N 168 ILE N N N N 169 ILE CA C N S 170 ILE C C N N 171 ILE O O N N 172 ILE CB C N S 173 ILE CG1 C N N 174 ILE CG2 C N N 175 ILE CD1 C N N 176 ILE OXT O N N 177 ILE H H N N 178 ILE H2 H N N 179 ILE HA H N N 180 ILE HB H N N 181 ILE HG12 H N N 182 ILE HG13 H N N 183 ILE HG21 H N N 184 ILE HG22 H N N 185 ILE HG23 H N N 186 ILE HD11 H N N 187 ILE HD12 H N N 188 ILE HD13 H N N 189 ILE HXT H N N 190 LEU N N N N 191 LEU CA C N S 192 LEU C C N N 193 LEU O O N N 194 LEU CB C N N 195 LEU CG C N N 196 LEU CD1 C N N 197 LEU CD2 C N N 198 LEU OXT O N N 199 LEU H H N N 200 LEU H2 H N N 201 LEU HA H N N 202 LEU HB2 H N N 203 LEU HB3 H N N 204 LEU HG H N N 205 LEU HD11 H N N 206 LEU HD12 H N N 207 LEU HD13 H N N 208 LEU HD21 H N N 209 LEU HD22 H N N 210 LEU HD23 H N N 211 LEU HXT H N N 212 LYS N N N N 213 LYS CA C N S 214 LYS C C N N 215 LYS O O N N 216 LYS CB C N N 217 LYS CG C N N 218 LYS CD C N N 219 LYS CE C N N 220 LYS NZ N N N 221 LYS OXT O N N 222 LYS H H N N 223 LYS H2 H N N 224 LYS HA H N N 225 LYS HB2 H N N 226 LYS HB3 H N N 227 LYS HG2 H N N 228 LYS HG3 H N N 229 LYS HD2 H N N 230 LYS HD3 H N N 231 LYS HE2 H N N 232 LYS HE3 H N N 233 LYS HZ1 H N N 234 LYS HZ2 H N N 235 LYS HZ3 H N N 236 LYS HXT H N N 237 MET N N N N 238 MET CA C N S 239 MET C C N N 240 MET O O N N 241 MET CB C N N 242 MET CG C N N 243 MET SD S N N 244 MET CE C N N 245 MET OXT O N N 246 MET H H N N 247 MET H2 H N N 248 MET HA H N N 249 MET HB2 H N N 250 MET HB3 H N N 251 MET HG2 H N N 252 MET HG3 H N N 253 MET HE1 H N N 254 MET HE2 H N N 255 MET HE3 H N N 256 MET HXT H N N 257 NEH N N N N 258 NEH CA C N N 259 NEH CB C N N 260 NEH H H N N 261 NEH HA2 H N N 262 NEH HA3 H N N 263 NEH HB1 H N N 264 NEH HB2 H N N 265 NEH HB3 H N N 266 NEH H2 H N N 267 PHE N N N N 268 PHE CA C N S 269 PHE C C N N 270 PHE O O N N 271 PHE CB C N N 272 PHE CG C Y N 273 PHE CD1 C Y N 274 PHE CD2 C Y N 275 PHE CE1 C Y N 276 PHE CE2 C Y N 277 PHE CZ C Y N 278 PHE OXT O N N 279 PHE H H N N 280 PHE H2 H N N 281 PHE HA H N N 282 PHE HB2 H N N 283 PHE HB3 H N N 284 PHE HD1 H N N 285 PHE HD2 H N N 286 PHE HE1 H N N 287 PHE HE2 H N N 288 PHE HZ H N N 289 PHE HXT H N N 290 PRO N N N N 291 PRO CA C N S 292 PRO C C N N 293 PRO O O N N 294 PRO CB C N N 295 PRO CG C N N 296 PRO CD C N N 297 PRO OXT O N N 298 PRO H H N N 299 PRO HA H N N 300 PRO HB2 H N N 301 PRO HB3 H N N 302 PRO HG2 H N N 303 PRO HG3 H N N 304 PRO HD2 H N N 305 PRO HD3 H N N 306 PRO HXT H N N 307 SER N N N N 308 SER CA C N S 309 SER C C N N 310 SER O O N N 311 SER CB C N N 312 SER OG O N N 313 SER OXT O N N 314 SER H H N N 315 SER H2 H N N 316 SER HA H N N 317 SER HB2 H N N 318 SER HB3 H N N 319 SER HG H N N 320 SER HXT H N N 321 THR N N N N 322 THR CA C N S 323 THR C C N N 324 THR O O N N 325 THR CB C N R 326 THR OG1 O N N 327 THR CG2 C N N 328 THR OXT O N N 329 THR H H N N 330 THR H2 H N N 331 THR HA H N N 332 THR HB H N N 333 THR HG1 H N N 334 THR HG21 H N N 335 THR HG22 H N N 336 THR HG23 H N N 337 THR HXT H N N 338 TRP N N N N 339 TRP CA C N S 340 TRP C C N N 341 TRP O O N N 342 TRP CB C N N 343 TRP CG C Y N 344 TRP CD1 C Y N 345 TRP CD2 C Y N 346 TRP NE1 N Y N 347 TRP CE2 C Y N 348 TRP CE3 C Y N 349 TRP CZ2 C Y N 350 TRP CZ3 C Y N 351 TRP CH2 C Y N 352 TRP OXT O N N 353 TRP H H N N 354 TRP H2 H N N 355 TRP HA H N N 356 TRP HB2 H N N 357 TRP HB3 H N N 358 TRP HD1 H N N 359 TRP HE1 H N N 360 TRP HE3 H N N 361 TRP HZ2 H N N 362 TRP HZ3 H N N 363 TRP HH2 H N N 364 TRP HXT H N N 365 TYR N N N N 366 TYR CA C N S 367 TYR C C N N 368 TYR O O N N 369 TYR CB C N N 370 TYR CG C Y N 371 TYR CD1 C Y N 372 TYR CD2 C Y N 373 TYR CE1 C Y N 374 TYR CE2 C Y N 375 TYR CZ C Y N 376 TYR OH O N N 377 TYR OXT O N N 378 TYR H H N N 379 TYR H2 H N N 380 TYR HA H N N 381 TYR HB2 H N N 382 TYR HB3 H N N 383 TYR HD1 H N N 384 TYR HD2 H N N 385 TYR HE1 H N N 386 TYR HE2 H N N 387 TYR HH H N N 388 TYR HXT H N N 389 VAL N N N N 390 VAL CA C N S 391 VAL C C N N 392 VAL O O N N 393 VAL CB C N N 394 VAL CG1 C N N 395 VAL CG2 C N N 396 VAL OXT O N N 397 VAL H H N N 398 VAL H2 H N N 399 VAL HA H N N 400 VAL HB H N N 401 VAL HG11 H N N 402 VAL HG12 H N N 403 VAL HG13 H N N 404 VAL HG21 H N N 405 VAL HG22 H N N 406 VAL HG23 H N N 407 VAL HXT H N N 408 ZN ZN ZN N N 409 # 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 ACY C O doub N N 1 ACY C OXT sing N N 2 ACY C CH3 sing N N 3 ACY OXT HXT sing N N 4 ACY CH3 H1 sing N N 5 ACY CH3 H2 sing N N 6 ACY CH3 H3 sing N N 7 ALA N CA sing N N 8 ALA N H sing N N 9 ALA N H2 sing N N 10 ALA CA C sing N N 11 ALA CA CB sing N N 12 ALA CA HA sing N N 13 ALA C O doub N N 14 ALA C OXT sing N N 15 ALA CB HB1 sing N N 16 ALA CB HB2 sing N N 17 ALA CB HB3 sing N N 18 ALA OXT HXT sing N N 19 ARG N CA sing N N 20 ARG N H sing N N 21 ARG N H2 sing N N 22 ARG CA C sing N N 23 ARG CA CB sing N N 24 ARG CA HA sing N N 25 ARG C O doub N N 26 ARG C OXT sing N N 27 ARG CB CG sing N N 28 ARG CB HB2 sing N N 29 ARG CB HB3 sing N N 30 ARG CG CD sing N N 31 ARG CG HG2 sing N N 32 ARG CG HG3 sing N N 33 ARG CD NE sing N N 34 ARG CD HD2 sing N N 35 ARG CD HD3 sing N N 36 ARG NE CZ sing N N 37 ARG NE HE sing N N 38 ARG CZ NH1 sing N N 39 ARG CZ NH2 doub N N 40 ARG NH1 HH11 sing N N 41 ARG NH1 HH12 sing N N 42 ARG NH2 HH21 sing N N 43 ARG NH2 HH22 sing N N 44 ARG OXT HXT sing N N 45 ASN N CA sing N N 46 ASN N H sing N N 47 ASN N H2 sing N N 48 ASN CA C sing N N 49 ASN CA CB sing N N 50 ASN CA HA sing N N 51 ASN C O doub N N 52 ASN C OXT sing N N 53 ASN CB CG sing N N 54 ASN CB HB2 sing N N 55 ASN CB HB3 sing N N 56 ASN CG OD1 doub N N 57 ASN CG ND2 sing N N 58 ASN ND2 HD21 sing N N 59 ASN ND2 HD22 sing N N 60 ASN OXT HXT sing N N 61 ASP N CA sing N N 62 ASP N H sing N N 63 ASP N H2 sing N N 64 ASP CA C sing N N 65 ASP CA CB sing N N 66 ASP CA HA sing N N 67 ASP C O doub N N 68 ASP C OXT sing N N 69 ASP CB CG sing N N 70 ASP CB HB2 sing N N 71 ASP CB HB3 sing N N 72 ASP CG OD1 doub N N 73 ASP CG OD2 sing N N 74 ASP OD2 HD2 sing N N 75 ASP OXT HXT sing N N 76 CYS N CA sing N N 77 CYS N H sing N N 78 CYS N H2 sing N N 79 CYS CA C sing N N 80 CYS CA CB sing N N 81 CYS CA HA sing N N 82 CYS C O doub N N 83 CYS C OXT sing N N 84 CYS CB SG sing N N 85 CYS CB HB2 sing N N 86 CYS CB HB3 sing N N 87 CYS SG HG sing N N 88 CYS OXT HXT sing N N 89 GLN N CA sing N N 90 GLN N H sing N N 91 GLN N H2 sing N N 92 GLN CA C sing N N 93 GLN CA CB sing N N 94 GLN CA HA sing N N 95 GLN C O doub N N 96 GLN C OXT sing N N 97 GLN CB CG sing N N 98 GLN CB HB2 sing N N 99 GLN CB HB3 sing N N 100 GLN CG CD sing N N 101 GLN CG HG2 sing N N 102 GLN CG HG3 sing N N 103 GLN CD OE1 doub N N 104 GLN CD NE2 sing N N 105 GLN NE2 HE21 sing N N 106 GLN NE2 HE22 sing N N 107 GLN OXT HXT sing N N 108 GLU N CA sing N N 109 GLU N H sing N N 110 GLU N H2 sing N N 111 GLU CA C sing N N 112 GLU CA CB sing N N 113 GLU CA HA sing N N 114 GLU C O doub N N 115 GLU C OXT sing N N 116 GLU CB CG sing N N 117 GLU CB HB2 sing N N 118 GLU CB HB3 sing N N 119 GLU CG CD sing N N 120 GLU CG HG2 sing N N 121 GLU CG HG3 sing N N 122 GLU CD OE1 doub N N 123 GLU CD OE2 sing N N 124 GLU OE2 HE2 sing N N 125 GLU OXT HXT sing N N 126 GLY N CA sing N N 127 GLY N H sing N N 128 GLY N H2 sing N N 129 GLY CA C sing N N 130 GLY CA HA2 sing N N 131 GLY CA HA3 sing N N 132 GLY C O doub N N 133 GLY C OXT sing N N 134 GLY OXT HXT sing N N 135 HIS N CA sing N N 136 HIS N H sing N N 137 HIS N H2 sing N N 138 HIS CA C sing N N 139 HIS CA CB sing N N 140 HIS CA HA sing N N 141 HIS C O doub N N 142 HIS C OXT sing N N 143 HIS CB CG sing N N 144 HIS CB HB2 sing N N 145 HIS CB HB3 sing N N 146 HIS CG ND1 sing Y N 147 HIS CG CD2 doub Y N 148 HIS ND1 CE1 doub Y N 149 HIS ND1 HD1 sing N N 150 HIS CD2 NE2 sing Y N 151 HIS CD2 HD2 sing N N 152 HIS CE1 NE2 sing Y N 153 HIS CE1 HE1 sing N N 154 HIS NE2 HE2 sing N N 155 HIS OXT HXT sing N N 156 HOH O H1 sing N N 157 HOH O H2 sing N N 158 ILE N CA sing N N 159 ILE N H sing N N 160 ILE N H2 sing N N 161 ILE CA C sing N N 162 ILE CA CB sing N N 163 ILE CA HA sing N N 164 ILE C O doub N N 165 ILE C OXT sing N N 166 ILE CB CG1 sing N N 167 ILE CB CG2 sing N N 168 ILE CB HB sing N N 169 ILE CG1 CD1 sing N N 170 ILE CG1 HG12 sing N N 171 ILE CG1 HG13 sing N N 172 ILE CG2 HG21 sing N N 173 ILE CG2 HG22 sing N N 174 ILE CG2 HG23 sing N N 175 ILE CD1 HD11 sing N N 176 ILE CD1 HD12 sing N N 177 ILE CD1 HD13 sing N N 178 ILE OXT HXT sing N N 179 LEU N CA sing N N 180 LEU N H sing N N 181 LEU N H2 sing N N 182 LEU CA C sing N N 183 LEU CA CB sing N N 184 LEU CA HA sing N N 185 LEU C O doub N N 186 LEU C OXT sing N N 187 LEU CB CG sing N N 188 LEU CB HB2 sing N N 189 LEU CB HB3 sing N N 190 LEU CG CD1 sing N N 191 LEU CG CD2 sing N N 192 LEU CG HG sing N N 193 LEU CD1 HD11 sing N N 194 LEU CD1 HD12 sing N N 195 LEU CD1 HD13 sing N N 196 LEU CD2 HD21 sing N N 197 LEU CD2 HD22 sing N N 198 LEU CD2 HD23 sing N N 199 LEU OXT HXT sing N N 200 LYS N CA sing N N 201 LYS N H sing N N 202 LYS N H2 sing N N 203 LYS CA C sing N N 204 LYS CA CB sing N N 205 LYS CA HA sing N N 206 LYS C O doub N N 207 LYS C OXT sing N N 208 LYS CB CG sing N N 209 LYS CB HB2 sing N N 210 LYS CB HB3 sing N N 211 LYS CG CD sing N N 212 LYS CG HG2 sing N N 213 LYS CG HG3 sing N N 214 LYS CD CE sing N N 215 LYS CD HD2 sing N N 216 LYS CD HD3 sing N N 217 LYS CE NZ sing N N 218 LYS CE HE2 sing N N 219 LYS CE HE3 sing N N 220 LYS NZ HZ1 sing N N 221 LYS NZ HZ2 sing N N 222 LYS NZ HZ3 sing N N 223 LYS OXT HXT sing N N 224 MET N CA sing N N 225 MET N H sing N N 226 MET N H2 sing N N 227 MET CA C sing N N 228 MET CA CB sing N N 229 MET CA HA sing N N 230 MET C O doub N N 231 MET C OXT sing N N 232 MET CB CG sing N N 233 MET CB HB2 sing N N 234 MET CB HB3 sing N N 235 MET CG SD sing N N 236 MET CG HG2 sing N N 237 MET CG HG3 sing N N 238 MET SD CE sing N N 239 MET CE HE1 sing N N 240 MET CE HE2 sing N N 241 MET CE HE3 sing N N 242 MET OXT HXT sing N N 243 NEH N CA sing N N 244 NEH N H sing N N 245 NEH CA CB sing N N 246 NEH CA HA2 sing N N 247 NEH CA HA3 sing N N 248 NEH CB HB1 sing N N 249 NEH CB HB2 sing N N 250 NEH CB HB3 sing N N 251 NEH H2 N sing N N 252 PHE N CA sing N N 253 PHE N H sing N N 254 PHE N H2 sing N N 255 PHE CA C sing N N 256 PHE CA CB sing N N 257 PHE CA HA sing N N 258 PHE C O doub N N 259 PHE C OXT sing N N 260 PHE CB CG sing N N 261 PHE CB HB2 sing N N 262 PHE CB HB3 sing N N 263 PHE CG CD1 doub Y N 264 PHE CG CD2 sing Y N 265 PHE CD1 CE1 sing Y N 266 PHE CD1 HD1 sing N N 267 PHE CD2 CE2 doub Y N 268 PHE CD2 HD2 sing N N 269 PHE CE1 CZ doub Y N 270 PHE CE1 HE1 sing N N 271 PHE CE2 CZ sing Y N 272 PHE CE2 HE2 sing N N 273 PHE CZ HZ sing N N 274 PHE OXT HXT sing N N 275 PRO N CA sing N N 276 PRO N CD sing N N 277 PRO N H sing N N 278 PRO CA C sing N N 279 PRO CA CB sing N N 280 PRO CA HA sing N N 281 PRO C O doub N N 282 PRO C OXT sing N N 283 PRO CB CG sing N N 284 PRO CB HB2 sing N N 285 PRO CB HB3 sing N N 286 PRO CG CD sing N N 287 PRO CG HG2 sing N N 288 PRO CG HG3 sing N N 289 PRO CD HD2 sing N N 290 PRO CD HD3 sing N N 291 PRO OXT HXT sing N N 292 SER N CA sing N N 293 SER N H sing N N 294 SER N H2 sing N N 295 SER CA C sing N N 296 SER CA CB sing N N 297 SER CA HA sing N N 298 SER C O doub N N 299 SER C OXT sing N N 300 SER CB OG sing N N 301 SER CB HB2 sing N N 302 SER CB HB3 sing N N 303 SER OG HG sing N N 304 SER OXT HXT sing N N 305 THR N CA sing N N 306 THR N H sing N N 307 THR N H2 sing N N 308 THR CA C sing N N 309 THR CA CB sing N N 310 THR CA HA sing N N 311 THR C O doub N N 312 THR C OXT sing N N 313 THR CB OG1 sing N N 314 THR CB CG2 sing N N 315 THR CB HB sing N N 316 THR OG1 HG1 sing N N 317 THR CG2 HG21 sing N N 318 THR CG2 HG22 sing N N 319 THR CG2 HG23 sing N N 320 THR OXT HXT sing N N 321 TRP N CA sing N N 322 TRP N H sing N N 323 TRP N H2 sing N N 324 TRP CA C sing N N 325 TRP CA CB sing N N 326 TRP CA HA sing N N 327 TRP C O doub N N 328 TRP C OXT sing N N 329 TRP CB CG sing N N 330 TRP CB HB2 sing N N 331 TRP CB HB3 sing N N 332 TRP CG CD1 doub Y N 333 TRP CG CD2 sing Y N 334 TRP CD1 NE1 sing Y N 335 TRP CD1 HD1 sing N N 336 TRP CD2 CE2 doub Y N 337 TRP CD2 CE3 sing Y N 338 TRP NE1 CE2 sing Y N 339 TRP NE1 HE1 sing N N 340 TRP CE2 CZ2 sing Y N 341 TRP CE3 CZ3 doub Y N 342 TRP CE3 HE3 sing N N 343 TRP CZ2 CH2 doub Y N 344 TRP CZ2 HZ2 sing N N 345 TRP CZ3 CH2 sing Y N 346 TRP CZ3 HZ3 sing N N 347 TRP CH2 HH2 sing N N 348 TRP OXT HXT sing N N 349 TYR N CA sing N N 350 TYR N H sing N N 351 TYR N H2 sing N N 352 TYR CA C sing N N 353 TYR CA CB sing N N 354 TYR CA HA sing N N 355 TYR C O doub N N 356 TYR C OXT sing N N 357 TYR CB CG sing N N 358 TYR CB HB2 sing N N 359 TYR CB HB3 sing N N 360 TYR CG CD1 doub Y N 361 TYR CG CD2 sing Y N 362 TYR CD1 CE1 sing Y N 363 TYR CD1 HD1 sing N N 364 TYR CD2 CE2 doub Y N 365 TYR CD2 HD2 sing N N 366 TYR CE1 CZ doub Y N 367 TYR CE1 HE1 sing N N 368 TYR CE2 CZ sing Y N 369 TYR CE2 HE2 sing N N 370 TYR CZ OH sing N N 371 TYR OH HH sing N N 372 TYR OXT HXT sing N N 373 VAL N CA sing N N 374 VAL N H sing N N 375 VAL N H2 sing N N 376 VAL CA C sing N N 377 VAL CA CB sing N N 378 VAL CA HA sing N N 379 VAL C O doub N N 380 VAL C OXT sing N N 381 VAL CB CG1 sing N N 382 VAL CB CG2 sing N N 383 VAL CB HB sing N N 384 VAL CG1 HG11 sing N N 385 VAL CG1 HG12 sing N N 386 VAL CG1 HG13 sing N N 387 VAL CG2 HG21 sing N N 388 VAL CG2 HG22 sing N N 389 VAL CG2 HG23 sing N N 390 VAL OXT HXT sing N N 391 # _atom_sites.entry_id 3PHX _atom_sites.fract_transf_matrix[1][1] 0.024085 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001786 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.026954 _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] 0.011888 _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 ZN # 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 . GLY A 1 1 ? 55.398 12.799 84.186 1.00 32.79 ? -1 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 54.860 12.672 85.524 1.00 34.08 ? -1 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 53.759 11.637 85.604 1.00 32.67 ? -1 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 53.179 11.268 84.592 1.00 28.09 ? -1 GLY A O 1 ATOM 5 N N . PRO A 1 2 ? 53.468 11.153 86.828 1.00 34.63 ? 0 PRO A N 1 ATOM 6 C CA . PRO A 1 2 ? 52.331 10.248 86.917 1.00 35.11 ? 0 PRO A CA 1 ATOM 7 C C . PRO A 1 2 ? 51.004 11.007 86.738 1.00 35.58 ? 0 PRO A C 1 ATOM 8 O O . PRO A 1 2 ? 50.819 12.182 87.181 1.00 36.44 ? 0 PRO A O 1 ATOM 9 C CB . PRO A 1 2 ? 52.453 9.666 88.338 1.00 34.30 ? 0 PRO A CB 1 ATOM 10 C CG . PRO A 1 2 ? 53.490 10.544 89.063 1.00 35.85 ? 0 PRO A CG 1 ATOM 11 C CD . PRO A 1 2 ? 53.890 11.648 88.153 1.00 35.10 ? 0 PRO A CD 1 ATOM 12 N N . MET A 1 3 ? 50.119 10.349 86.000 1.00 31.27 ? 1 MET A N 1 ATOM 13 C CA . MET A 1 3 ? 48.744 10.718 85.975 1.00 28.96 ? 1 MET A CA 1 ATOM 14 C C . MET A 1 3 ? 48.473 12.086 85.268 1.00 26.57 ? 1 MET A C 1 ATOM 15 O O . MET A 1 3 ? 47.430 12.707 85.470 1.00 27.05 ? 1 MET A O 1 ATOM 16 C CB . MET A 1 3 ? 48.144 10.517 87.388 1.00 31.08 ? 1 MET A CB 1 ATOM 17 C CG . MET A 1 3 ? 47.802 8.975 87.629 1.00 26.01 ? 1 MET A CG 1 ATOM 18 S SD . MET A 1 3 ? 46.109 8.870 88.162 1.00 41.73 ? 1 MET A SD 1 ATOM 19 C CE . MET A 1 3 ? 46.303 9.482 89.801 1.00 38.34 ? 1 MET A CE 1 ATOM 20 N N . ASP A 1 4 ? 49.389 12.516 84.396 1.00 23.19 ? 2 ASP A N 1 ATOM 21 C CA . ASP A 1 4 ? 49.254 13.848 83.784 1.00 20.68 ? 2 ASP A CA 1 ATOM 22 C C . ASP A 1 4 ? 49.253 13.817 82.256 1.00 18.84 ? 2 ASP A C 1 ATOM 23 O O . ASP A 1 4 ? 49.547 14.830 81.590 1.00 19.38 ? 2 ASP A O 1 ATOM 24 C CB . ASP A 1 4 ? 50.324 14.835 84.270 1.00 23.53 ? 2 ASP A CB 1 ATOM 25 C CG . ASP A 1 4 ? 51.715 14.418 83.873 1.00 24.58 ? 2 ASP A CG 1 ATOM 26 O OD1 . ASP A 1 4 ? 51.866 13.428 83.161 1.00 25.20 ? 2 ASP A OD1 1 ATOM 27 O OD2 . ASP A 1 4 ? 52.677 15.052 84.319 1.00 28.72 ? 2 ASP A OD2 1 ATOM 28 N N . PHE A 1 5 ? 48.939 12.649 81.700 1.00 18.97 ? 3 PHE A N 1 ATOM 29 C CA . PHE A 1 5 ? 48.825 12.470 80.227 1.00 19.37 ? 3 PHE A CA 1 ATOM 30 C C . PHE A 1 5 ? 47.997 13.572 79.558 1.00 18.70 ? 3 PHE A C 1 ATOM 31 O O . PHE A 1 5 ? 48.405 14.155 78.535 1.00 18.49 ? 3 PHE A O 1 ATOM 32 C CB . PHE A 1 5 ? 48.185 11.094 79.978 1.00 22.27 ? 3 PHE A CB 1 ATOM 33 C CG . PHE A 1 5 ? 47.897 10.761 78.519 1.00 23.66 ? 3 PHE A CG 1 ATOM 34 C CD1 . PHE A 1 5 ? 48.860 10.131 77.734 1.00 27.60 ? 3 PHE A CD1 1 ATOM 35 C CD2 . PHE A 1 5 ? 46.616 11.000 77.965 1.00 22.48 ? 3 PHE A CD2 1 ATOM 36 C CE1 . PHE A 1 5 ? 48.573 9.804 76.368 1.00 27.77 ? 3 PHE A CE1 1 ATOM 37 C CE2 . PHE A 1 5 ? 46.321 10.665 76.637 1.00 25.67 ? 3 PHE A CE2 1 ATOM 38 C CZ . PHE A 1 5 ? 47.290 10.085 75.829 1.00 26.63 ? 3 PHE A CZ 1 ATOM 39 N N . LEU A 1 6 ? 46.858 13.900 80.155 1.00 17.22 ? 4 LEU A N 1 ATOM 40 C CA . LEU A 1 6 ? 45.961 14.881 79.536 1.00 16.67 ? 4 LEU A CA 1 ATOM 41 C C . LEU A 1 6 ? 46.539 16.283 79.464 1.00 16.37 ? 4 LEU A C 1 ATOM 42 O O . LEU A 1 6 ? 46.084 17.102 78.676 1.00 19.06 ? 4 LEU A O 1 ATOM 43 C CB . LEU A 1 6 ? 44.614 14.936 80.260 1.00 17.70 ? 4 LEU A CB 1 ATOM 44 C CG . LEU A 1 6 ? 43.737 13.676 80.174 1.00 16.18 ? 4 LEU A CG 1 ATOM 45 C CD1 . LEU A 1 6 ? 42.499 13.932 81.037 1.00 15.10 ? 4 LEU A CD1 1 ATOM 46 C CD2 . LEU A 1 6 ? 43.378 13.347 78.692 1.00 15.88 ? 4 LEU A CD2 1 ATOM 47 N N . ARG A 1 7 ? 47.556 16.563 80.270 1.00 18.11 ? 5 ARG A N 1 ATOM 48 C CA . ARG A 1 7 ? 48.191 17.875 80.268 1.00 20.98 ? 5 ARG A CA 1 ATOM 49 C C . ARG A 1 7 ? 49.101 18.091 79.080 1.00 21.69 ? 5 ARG A C 1 ATOM 50 O O . ARG A 1 7 ? 49.528 19.234 78.852 1.00 23.98 ? 5 ARG A O 1 ATOM 51 C CB . ARG A 1 7 ? 49.023 18.082 81.551 1.00 23.66 ? 5 ARG A CB 1 ATOM 52 C CG . ARG A 1 7 ? 48.166 18.199 82.798 1.00 31.02 ? 5 ARG A CG 1 ATOM 53 C CD . ARG A 1 7 ? 48.413 19.566 83.505 1.00 39.41 ? 5 ARG A CD 1 ATOM 54 N NE . ARG A 1 7 ? 47.680 20.671 82.851 1.00 44.09 ? 5 ARG A NE 1 ATOM 55 C CZ . ARG A 1 7 ? 48.099 21.334 81.767 1.00 47.86 ? 5 ARG A CZ 1 ATOM 56 N NH1 . ARG A 1 7 ? 49.257 21.034 81.177 1.00 49.31 ? 5 ARG A NH1 1 ATOM 57 N NH2 . ARG A 1 7 ? 47.351 22.300 81.250 1.00 48.82 ? 5 ARG A NH2 1 ATOM 58 N N . SER A 1 8 ? 49.413 17.020 78.343 1.00 18.31 ? 6 SER A N 1 ATOM 59 C CA . SER A 1 8 ? 50.364 17.149 77.232 1.00 18.24 ? 6 SER A CA 1 ATOM 60 C C . SER A 1 8 ? 49.806 16.772 75.848 1.00 18.14 ? 6 SER A C 1 ATOM 61 O O . SER A 1 8 ? 50.546 16.329 74.958 1.00 19.04 ? 6 SER A O 1 ATOM 62 C CB . SER A 1 8 ? 51.603 16.319 77.553 1.00 21.86 ? 6 SER A CB 1 ATOM 63 O OG . SER A 1 8 ? 52.229 16.786 78.754 1.00 26.16 ? 6 SER A OG 1 ATOM 64 N N . LEU A 1 9 ? 48.511 16.970 75.656 1.00 17.25 ? 7 LEU A N 1 ATOM 65 C CA . LEU A 1 9 ? 47.919 16.741 74.322 1.00 15.74 ? 7 LEU A CA 1 ATOM 66 C C . LEU A 1 9 ? 48.515 17.732 73.321 1.00 18.32 ? 7 LEU A C 1 ATOM 67 O O . LEU A 1 9 ? 48.594 18.946 73.591 1.00 20.53 ? 7 LEU A O 1 ATOM 68 C CB . LEU A 1 9 ? 46.382 16.921 74.385 1.00 14.22 ? 7 LEU A CB 1 ATOM 69 C CG . LEU A 1 9 ? 45.667 15.871 75.279 1.00 15.59 ? 7 LEU A CG 1 ATOM 70 C CD1 . LEU A 1 9 ? 44.230 16.236 75.450 1.00 16.59 ? 7 LEU A CD1 1 ATOM 71 C CD2 . LEU A 1 9 ? 45.805 14.460 74.701 1.00 16.92 ? 7 LEU A CD2 1 ATOM 72 N N . ASP A 1 10 ? 48.892 17.202 72.155 1.00 16.70 ? 8 ASP A N 1 ATOM 73 C CA . ASP A 1 10 ? 49.446 18.018 71.061 1.00 15.58 ? 8 ASP A CA 1 ATOM 74 C C . ASP A 1 10 ? 48.436 18.275 69.974 1.00 14.71 ? 8 ASP A C 1 ATOM 75 O O . ASP A 1 10 ? 47.988 17.347 69.261 1.00 15.67 ? 8 ASP A O 1 ATOM 76 C CB . ASP A 1 10 ? 50.680 17.370 70.487 1.00 17.59 ? 8 ASP A CB 1 ATOM 77 C CG . ASP A 1 10 ? 51.829 17.423 71.460 1.00 18.69 ? 8 ASP A CG 1 ATOM 78 O OD1 . ASP A 1 10 ? 51.827 18.349 72.296 1.00 20.29 ? 8 ASP A OD1 1 ATOM 79 O OD2 . ASP A 1 10 ? 52.683 16.538 71.427 1.00 18.72 ? 8 ASP A OD2 1 ATOM 80 N N . TRP A 1 11 ? 48.081 19.538 69.837 1.00 13.16 ? 9 TRP A N 1 ATOM 81 C CA . TRP A 1 11 ? 47.043 19.976 68.878 1.00 14.66 ? 9 TRP A CA 1 ATOM 82 C C . TRP A 1 11 ? 47.700 20.648 67.691 1.00 15.76 ? 9 TRP A C 1 ATOM 83 O O . TRP A 1 11 ? 48.484 21.578 67.869 1.00 20.48 ? 9 TRP A O 1 ATOM 84 C CB . TRP A 1 11 ? 46.113 20.985 69.568 1.00 14.00 ? 9 TRP A CB 1 ATOM 85 C CG . TRP A 1 11 ? 45.314 20.354 70.674 1.00 15.04 ? 9 TRP A CG 1 ATOM 86 C CD1 . TRP A 1 11 ? 45.535 20.457 72.046 1.00 15.71 ? 9 TRP A CD1 1 ATOM 87 C CD2 . TRP A 1 11 ? 44.203 19.491 70.515 1.00 11.48 ? 9 TRP A CD2 1 ATOM 88 N NE1 . TRP A 1 11 ? 44.605 19.712 72.728 1.00 16.10 ? 9 TRP A NE1 1 ATOM 89 C CE2 . TRP A 1 11 ? 43.765 19.118 71.813 1.00 13.75 ? 9 TRP A CE2 1 ATOM 90 C CE3 . TRP A 1 11 ? 43.522 18.998 69.399 1.00 13.10 ? 9 TRP A CE3 1 ATOM 91 C CZ2 . TRP A 1 11 ? 42.689 18.244 72.015 1.00 13.55 ? 9 TRP A CZ2 1 ATOM 92 C CZ3 . TRP A 1 11 ? 42.444 18.187 69.587 1.00 11.86 ? 9 TRP A CZ3 1 ATOM 93 C CH2 . TRP A 1 11 ? 42.018 17.813 70.907 1.00 13.49 ? 9 TRP A CH2 1 ATOM 94 N N . THR A 1 12 ? 47.371 20.169 66.479 1.00 13.61 ? 10 THR A N 1 ATOM 95 C CA . THR A 1 12 ? 47.860 20.770 65.231 1.00 14.53 ? 10 THR A CA 1 ATOM 96 C C . THR A 1 12 ? 46.750 21.623 64.628 1.00 14.62 ? 10 THR A C 1 ATOM 97 O O . THR A 1 12 ? 45.603 21.183 64.537 1.00 14.61 ? 10 THR A O 1 ATOM 98 C CB . THR A 1 12 ? 48.304 19.701 64.233 1.00 14.04 ? 10 THR A CB 1 ATOM 99 O OG1 . THR A 1 12 ? 49.398 18.946 64.804 1.00 17.20 ? 10 THR A OG1 1 ATOM 100 C CG2 . THR A 1 12 ? 48.797 20.376 62.915 1.00 15.26 ? 10 THR A CG2 1 ATOM 101 N N . GLN A 1 13 ? 47.092 22.855 64.232 1.00 13.98 ? 11 GLN A N 1 ATOM 102 C CA . GLN A 1 13 ? 46.126 23.750 63.600 1.00 14.74 ? 11 GLN A CA 1 ATOM 103 C C . GLN A 1 13 ? 45.617 23.247 62.247 1.00 14.64 ? 11 GLN A C 1 ATOM 104 O O . GLN A 1 13 ? 46.400 22.803 61.378 1.00 17.66 ? 11 GLN A O 1 ATOM 105 C CB . GLN A 1 13 ? 46.708 25.149 63.442 1.00 17.74 ? 11 GLN A CB 1 ATOM 106 C CG . GLN A 1 13 ? 45.662 26.050 62.839 1.00 26.07 ? 11 GLN A CG 1 ATOM 107 C CD . GLN A 1 13 ? 45.942 27.474 63.032 1.00 34.28 ? 11 GLN A CD 1 ATOM 108 O OE1 . GLN A 1 13 ? 46.471 27.869 64.041 1.00 38.33 ? 11 GLN A OE1 1 ATOM 109 N NE2 . GLN A 1 13 ? 45.598 28.283 62.025 1.00 38.75 ? 11 GLN A NE2 1 ATOM 110 N N . VAL A 1 14 ? 44.297 23.272 62.093 1.00 13.43 ? 12 VAL A N 1 ATOM 111 C CA . VAL A 1 14 ? 43.633 22.914 60.826 1.00 13.09 ? 12 VAL A CA 1 ATOM 112 C C . VAL A 1 14 ? 43.303 24.231 60.132 1.00 13.16 ? 12 VAL A C 1 ATOM 113 O O . VAL A 1 14 ? 43.776 24.484 59.003 1.00 14.71 ? 12 VAL A O 1 ATOM 114 C CB . VAL A 1 14 ? 42.316 22.088 61.115 1.00 13.88 ? 12 VAL A CB 1 ATOM 115 C CG1 . VAL A 1 14 ? 41.461 21.895 59.857 1.00 13.78 ? 12 VAL A CG1 1 ATOM 116 C CG2 . VAL A 1 14 ? 42.647 20.718 61.779 1.00 15.23 ? 12 VAL A CG2 1 ATOM 117 N N . ILE A 1 15 ? 42.502 25.071 60.790 1.00 13.46 ? 13 ILE A N 1 ATOM 118 C CA . ILE A 1 15 ? 42.341 26.470 60.421 1.00 13.39 ? 13 ILE A CA 1 ATOM 119 C C . ILE A 1 15 ? 42.346 27.207 61.717 1.00 13.21 ? 13 ILE A C 1 ATOM 120 O O . ILE A 1 15 ? 42.283 26.574 62.750 1.00 13.92 ? 13 ILE A O 1 ATOM 121 C CB . ILE A 1 15 ? 40.991 26.778 59.670 1.00 13.23 ? 13 ILE A CB 1 ATOM 122 C CG1 . ILE A 1 15 ? 39.770 26.268 60.487 1.00 15.52 ? 13 ILE A CG1 1 ATOM 123 C CG2 . ILE A 1 15 ? 41.021 26.117 58.263 1.00 14.83 ? 13 ILE A CG2 1 ATOM 124 C CD1 . ILE A 1 15 ? 38.397 26.751 59.932 1.00 16.04 ? 13 ILE A CD1 1 ATOM 125 N N . ALA A 1 16 ? 42.373 28.529 61.683 1.00 14.07 ? 14 ALA A N 1 ATOM 126 C CA . ALA A 1 16 ? 42.374 29.294 62.940 1.00 16.01 ? 14 ALA A CA 1 ATOM 127 C C . ALA A 1 16 ? 41.179 28.845 63.804 1.00 16.20 ? 14 ALA A C 1 ATOM 128 O O . ALA A 1 16 ? 40.041 28.815 63.322 1.00 17.78 ? 14 ALA A O 1 ATOM 129 C CB . ALA A 1 16 ? 42.331 30.816 62.656 1.00 18.08 ? 14 ALA A CB 1 ATOM 130 N N . GLY A 1 17 ? 41.448 28.397 65.040 1.00 16.07 ? 15 GLY A N 1 ATOM 131 C CA . GLY A 1 17 ? 40.371 27.956 65.902 1.00 15.53 ? 15 GLY A CA 1 ATOM 132 C C . GLY A 1 17 ? 39.889 26.515 65.785 1.00 14.91 ? 15 GLY A C 1 ATOM 133 O O . GLY A 1 17 ? 38.986 26.099 66.516 1.00 15.18 ? 15 GLY A O 1 ATOM 134 N N . GLN A 1 18 ? 40.461 25.740 64.870 1.00 14.40 ? 16 GLN A N 1 ATOM 135 C CA . GLN A 1 18 ? 40.116 24.339 64.812 1.00 14.07 ? 16 GLN A CA 1 ATOM 136 C C . GLN A 1 18 ? 41.404 23.543 64.807 1.00 11.89 ? 16 GLN A C 1 ATOM 137 O O . GLN A 1 18 ? 42.320 23.903 64.066 1.00 12.76 ? 16 GLN A O 1 ATOM 138 C CB . GLN A 1 18 ? 39.261 24.011 63.554 1.00 14.28 ? 16 GLN A CB 1 ATOM 139 C CG . GLN A 1 18 ? 38.817 22.545 63.496 1.00 13.02 ? 16 GLN A CG 1 ATOM 140 C CD . GLN A 1 18 ? 37.767 22.272 62.375 1.00 14.66 ? 16 GLN A CD 1 ATOM 141 O OE1 . GLN A 1 18 ? 36.985 23.169 61.988 1.00 15.61 ? 16 GLN A OE1 1 ATOM 142 N NE2 . GLN A 1 18 ? 37.707 21.024 61.910 1.00 15.35 ? 16 GLN A NE2 1 ATOM 143 N N . TYR A 1 19 ? 41.459 22.449 65.569 1.00 10.86 ? 17 TYR A N 1 ATOM 144 C CA . TYR A 1 19 ? 42.710 21.708 65.705 1.00 11.15 ? 17 TYR A CA 1 ATOM 145 C C . TYR A 1 19 ? 42.457 20.242 65.679 1.00 10.50 ? 17 TYR A C 1 ATOM 146 O O . TYR A 1 19 ? 41.327 19.791 65.901 1.00 11.47 ? 17 TYR A O 1 ATOM 147 C CB . TYR A 1 19 ? 43.408 22.019 67.066 1.00 10.84 ? 17 TYR A CB 1 ATOM 148 C CG . TYR A 1 19 ? 43.550 23.504 67.286 1.00 13.25 ? 17 TYR A CG 1 ATOM 149 C CD1 . TYR A 1 19 ? 44.710 24.162 66.900 1.00 15.85 ? 17 TYR A CD1 1 ATOM 150 C CD2 . TYR A 1 19 ? 42.495 24.252 67.810 1.00 14.99 ? 17 TYR A CD2 1 ATOM 151 C CE1 . TYR A 1 19 ? 44.826 25.539 67.036 1.00 18.57 ? 17 TYR A CE1 1 ATOM 152 C CE2 . TYR A 1 19 ? 42.583 25.645 67.961 1.00 16.49 ? 17 TYR A CE2 1 ATOM 153 C CZ . TYR A 1 19 ? 43.761 26.274 67.558 1.00 19.84 ? 17 TYR A CZ 1 ATOM 154 O OH . TYR A 1 19 ? 43.921 27.631 67.701 1.00 24.61 ? 17 TYR A OH 1 ATOM 155 N N . VAL A 1 20 ? 43.512 19.464 65.422 1.00 10.28 ? 18 VAL A N 1 ATOM 156 C CA . VAL A 1 20 ? 43.390 18.014 65.496 1.00 10.43 ? 18 VAL A CA 1 ATOM 157 C C . VAL A 1 20 ? 44.490 17.440 66.355 1.00 12.58 ? 18 VAL A C 1 ATOM 158 O O . VAL A 1 20 ? 45.606 17.998 66.428 1.00 13.52 ? 18 VAL A O 1 ATOM 159 C CB . VAL A 1 20 ? 43.442 17.365 64.062 1.00 12.37 ? 18 VAL A CB 1 ATOM 160 C CG1 . VAL A 1 20 ? 44.782 17.722 63.313 1.00 12.20 ? 18 VAL A CG1 1 ATOM 161 C CG2 . VAL A 1 20 ? 43.259 15.848 64.100 1.00 15.87 ? 18 VAL A CG2 1 ATOM 162 N N A SER A 1 21 ? 44.176 16.351 67.042 0.60 10.87 ? 19 SER A N 1 ATOM 163 N N B SER A 1 21 ? 44.194 16.322 67.001 0.40 12.17 ? 19 SER A N 1 ATOM 164 C CA A SER A 1 21 ? 45.217 15.588 67.740 0.60 12.28 ? 19 SER A CA 1 ATOM 165 C CA B SER A 1 21 ? 45.225 15.594 67.734 0.40 13.35 ? 19 SER A CA 1 ATOM 166 C C A SER A 1 21 ? 45.057 14.103 67.422 0.60 13.27 ? 19 SER A C 1 ATOM 167 C C B SER A 1 21 ? 45.029 14.087 67.570 0.40 14.38 ? 19 SER A C 1 ATOM 168 O O A SER A 1 21 ? 43.967 13.669 67.019 0.60 12.73 ? 19 SER A O 1 ATOM 169 O O B SER A 1 21 ? 43.891 13.622 67.430 0.40 14.34 ? 19 SER A O 1 ATOM 170 C CB A SER A 1 21 ? 45.147 15.829 69.250 0.60 14.48 ? 19 SER A CB 1 ATOM 171 C CB B SER A 1 21 ? 45.202 15.992 69.209 0.40 14.75 ? 19 SER A CB 1 ATOM 172 O OG A SER A 1 21 ? 43.966 15.272 69.802 0.60 15.23 ? 19 SER A OG 1 ATOM 173 O OG B SER A 1 21 ? 46.212 15.312 69.921 0.40 15.02 ? 19 SER A OG 1 ATOM 174 N N . ASN A 1 22 ? 46.123 13.328 67.596 1.00 15.15 ? 20 ASN A N 1 ATOM 175 C CA . ASN A 1 22 ? 46.049 11.864 67.473 1.00 15.13 ? 20 ASN A CA 1 ATOM 176 C C . ASN A 1 22 ? 46.754 11.142 68.623 1.00 16.15 ? 20 ASN A C 1 ATOM 177 O O . ASN A 1 22 ? 47.713 10.380 68.416 1.00 19.84 ? 20 ASN A O 1 ATOM 178 C CB . ASN A 1 22 ? 46.626 11.377 66.135 1.00 16.08 ? 20 ASN A CB 1 ATOM 179 C CG . ASN A 1 22 ? 45.845 11.930 64.940 1.00 19.65 ? 20 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 22 ? 44.706 11.478 64.645 1.00 22.77 ? 20 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 22 ? 46.442 12.899 64.239 1.00 17.20 ? 20 ASN A ND2 1 ATOM 182 N N . PRO A 1 23 ? 46.279 11.382 69.851 1.00 18.19 ? 21 PRO A N 1 ATOM 183 C CA . PRO A 1 23 ? 46.856 10.690 71.004 1.00 17.23 ? 21 PRO A CA 1 ATOM 184 C C . PRO A 1 23 ? 46.409 9.260 70.974 1.00 19.63 ? 21 PRO A C 1 ATOM 185 O O . PRO A 1 23 ? 45.406 8.941 70.378 1.00 18.96 ? 21 PRO A O 1 ATOM 186 C CB . PRO A 1 23 ? 46.251 11.431 72.198 1.00 17.18 ? 21 PRO A CB 1 ATOM 187 C CG . PRO A 1 23 ? 44.940 11.976 71.676 1.00 17.50 ? 21 PRO A CG 1 ATOM 188 C CD . PRO A 1 23 ? 45.073 12.150 70.186 1.00 18.14 ? 21 PRO A CD 1 ATOM 189 N N . ARG A 1 24 ? 47.176 8.385 71.583 1.00 22.59 ? 22 ARG A N 1 ATOM 190 C CA . ARG A 1 24 ? 46.804 6.987 71.638 1.00 25.85 ? 22 ARG A CA 1 ATOM 191 C C . ARG A 1 24 ? 46.380 6.647 73.066 1.00 22.69 ? 22 ARG A C 1 ATOM 192 O O . ARG A 1 24 ? 47.209 6.577 73.969 1.00 21.95 ? 22 ARG A O 1 ATOM 193 C CB . ARG A 1 24 ? 47.974 6.100 71.156 1.00 32.12 ? 22 ARG A CB 1 ATOM 194 C CG . ARG A 1 24 ? 48.092 6.012 69.603 1.00 40.02 ? 22 ARG A CG 1 ATOM 195 C CD . ARG A 1 24 ? 48.947 4.770 69.141 1.00 50.13 ? 22 ARG A CD 1 ATOM 196 N NE . ARG A 1 24 ? 48.150 3.616 68.677 1.00 56.19 ? 22 ARG A NE 1 ATOM 197 C CZ . ARG A 1 24 ? 48.130 3.144 67.423 1.00 59.91 ? 22 ARG A CZ 1 ATOM 198 N NH1 . ARG A 1 24 ? 48.869 3.706 66.466 1.00 61.49 ? 22 ARG A NH1 1 ATOM 199 N NH2 . ARG A 1 24 ? 47.364 2.097 67.120 1.00 61.05 ? 22 ARG A NH2 1 ATOM 200 N N . PHE A 1 25 ? 45.086 6.425 73.264 1.00 19.28 ? 23 PHE A N 1 ATOM 201 C CA . PHE A 1 25 ? 44.578 6.034 74.572 1.00 19.17 ? 23 PHE A CA 1 ATOM 202 C C . PHE A 1 25 ? 43.193 5.501 74.406 1.00 19.29 ? 23 PHE A C 1 ATOM 203 O O . PHE A 1 25 ? 42.591 5.712 73.358 1.00 19.52 ? 23 PHE A O 1 ATOM 204 C CB . PHE A 1 25 ? 44.607 7.202 75.578 1.00 19.25 ? 23 PHE A CB 1 ATOM 205 C CG . PHE A 1 25 ? 43.635 8.333 75.302 1.00 17.61 ? 23 PHE A CG 1 ATOM 206 C CD1 . PHE A 1 25 ? 42.435 8.419 75.998 1.00 17.27 ? 23 PHE A CD1 1 ATOM 207 C CD2 . PHE A 1 25 ? 43.948 9.353 74.405 1.00 16.98 ? 23 PHE A CD2 1 ATOM 208 C CE1 . PHE A 1 25 ? 41.552 9.456 75.797 1.00 13.66 ? 23 PHE A CE1 1 ATOM 209 C CE2 . PHE A 1 25 ? 43.048 10.429 74.188 1.00 17.47 ? 23 PHE A CE2 1 ATOM 210 C CZ . PHE A 1 25 ? 41.839 10.476 74.920 1.00 16.95 ? 23 PHE A CZ 1 ATOM 211 N N . ASN A 1 26 ? 42.700 4.782 75.413 1.00 16.28 ? 24 ASN A N 1 ATOM 212 C CA . ASN A 1 26 ? 41.306 4.369 75.447 1.00 16.53 ? 24 ASN A CA 1 ATOM 213 C C . ASN A 1 26 ? 40.521 5.399 76.216 1.00 14.36 ? 24 ASN A C 1 ATOM 214 O O . ASN A 1 26 ? 40.953 5.858 77.292 1.00 16.29 ? 24 ASN A O 1 ATOM 215 C CB . ASN A 1 26 ? 41.159 2.986 76.099 1.00 20.67 ? 24 ASN A CB 1 ATOM 216 C CG . ASN A 1 26 ? 41.836 1.916 75.280 1.00 28.23 ? 24 ASN A CG 1 ATOM 217 O OD1 . ASN A 1 26 ? 41.247 1.359 74.342 1.00 32.72 ? 24 ASN A OD1 1 ATOM 218 N ND2 . ASN A 1 26 ? 43.081 1.658 75.588 1.00 31.33 ? 24 ASN A ND2 1 ATOM 219 N N . ILE A 1 27 ? 39.371 5.769 75.661 1.00 14.09 ? 25 ILE A N 1 ATOM 220 C CA . ILE A 1 27 ? 38.580 6.827 76.239 1.00 15.08 ? 25 ILE A CA 1 ATOM 221 C C . ILE A 1 27 ? 38.324 6.561 77.719 1.00 16.62 ? 25 ILE A C 1 ATOM 222 O O . ILE A 1 27 ? 38.410 7.490 78.522 1.00 15.94 ? 25 ILE A O 1 ATOM 223 C CB . ILE A 1 27 ? 37.224 6.988 75.503 1.00 18.82 ? 25 ILE A CB 1 ATOM 224 C CG1 . ILE A 1 27 ? 37.398 7.822 74.223 1.00 20.90 ? 25 ILE A CG1 1 ATOM 225 C CG2 . ILE A 1 27 ? 36.159 7.661 76.404 1.00 22.86 ? 25 ILE A CG2 1 ATOM 226 C CD1 . ILE A 1 27 ? 37.822 9.313 74.414 1.00 20.84 ? 25 ILE A CD1 1 ATOM 227 N N . SER A 1 28 ? 37.995 5.313 78.066 1.00 17.02 ? 26 SER A N 1 ATOM 228 C CA . SER A 1 28 ? 37.495 5.012 79.420 1.00 17.19 ? 26 SER A CA 1 ATOM 229 C C . SER A 1 28 ? 38.613 4.980 80.450 1.00 17.62 ? 26 SER A C 1 ATOM 230 O O . SER A 1 28 ? 38.367 4.896 81.674 1.00 18.27 ? 26 SER A O 1 ATOM 231 C CB . SER A 1 28 ? 36.689 3.711 79.428 1.00 21.78 ? 26 SER A CB 1 ATOM 232 O OG . SER A 1 28 ? 37.478 2.641 78.968 1.00 27.71 ? 26 SER A OG 1 ATOM 233 N N . ASP A 1 29 ? 39.841 5.115 79.975 1.00 16.23 ? 27 ASP A N 1 ATOM 234 C CA . ASP A 1 29 ? 40.978 5.193 80.909 1.00 15.09 ? 27 ASP A CA 1 ATOM 235 C C . ASP A 1 29 ? 41.077 6.578 81.505 1.00 14.46 ? 27 ASP A C 1 ATOM 236 O O . ASP A 1 29 ? 41.619 6.732 82.633 1.00 17.07 ? 27 ASP A O 1 ATOM 237 C CB . ASP A 1 29 ? 42.261 4.819 80.215 1.00 18.58 ? 27 ASP A CB 1 ATOM 238 C CG . ASP A 1 29 ? 42.445 3.322 80.082 1.00 22.94 ? 27 ASP A CG 1 ATOM 239 O OD1 . ASP A 1 29 ? 41.714 2.510 80.715 1.00 24.93 ? 27 ASP A OD1 1 ATOM 240 O OD2 . ASP A 1 29 ? 43.410 2.952 79.389 1.00 28.02 ? 27 ASP A OD2 1 ATOM 241 N N . TYR A 1 30 ? 40.517 7.583 80.795 1.00 12.64 ? 28 TYR A N 1 ATOM 242 C CA . TYR A 1 30 ? 40.648 8.980 81.237 1.00 13.62 ? 28 TYR A CA 1 ATOM 243 C C . TYR A 1 30 ? 39.321 9.690 81.448 1.00 12.81 ? 28 TYR A C 1 ATOM 244 O O . TYR A 1 30 ? 39.270 10.739 82.089 1.00 13.20 ? 28 TYR A O 1 ATOM 245 C CB . TYR A 1 30 ? 41.525 9.800 80.267 1.00 13.62 ? 28 TYR A CB 1 ATOM 246 C CG . TYR A 1 30 ? 42.960 9.429 80.366 1.00 14.45 ? 28 TYR A CG 1 ATOM 247 C CD1 . TYR A 1 30 ? 43.771 9.954 81.392 1.00 15.77 ? 28 TYR A CD1 1 ATOM 248 C CD2 . TYR A 1 30 ? 43.512 8.485 79.493 1.00 14.36 ? 28 TYR A CD2 1 ATOM 249 C CE1 . TYR A 1 30 ? 45.093 9.593 81.506 1.00 16.11 ? 28 TYR A CE1 1 ATOM 250 C CE2 . TYR A 1 30 ? 44.837 8.117 79.627 1.00 17.41 ? 28 TYR A CE2 1 ATOM 251 C CZ . TYR A 1 30 ? 45.608 8.675 80.641 1.00 17.60 ? 28 TYR A CZ 1 ATOM 252 O OH . TYR A 1 30 ? 46.907 8.289 80.710 1.00 20.64 ? 28 TYR A OH 1 ATOM 253 N N . PHE A 1 31 ? 38.243 9.122 80.893 1.00 13.10 ? 29 PHE A N 1 ATOM 254 C CA . PHE A 1 31 ? 36.936 9.765 80.936 1.00 13.70 ? 29 PHE A CA 1 ATOM 255 C C . PHE A 1 31 ? 35.864 8.818 81.410 1.00 14.20 ? 29 PHE A C 1 ATOM 256 O O . PHE A 1 31 ? 35.903 7.606 81.156 1.00 14.32 ? 29 PHE A O 1 ATOM 257 C CB . PHE A 1 31 ? 36.488 10.249 79.522 1.00 11.46 ? 29 PHE A CB 1 ATOM 258 C CG . PHE A 1 31 ? 37.332 11.349 78.918 1.00 12.13 ? 29 PHE A CG 1 ATOM 259 C CD1 . PHE A 1 31 ? 37.052 12.701 79.175 1.00 12.15 ? 29 PHE A CD1 1 ATOM 260 C CD2 . PHE A 1 31 ? 38.426 11.025 78.123 1.00 13.48 ? 29 PHE A CD2 1 ATOM 261 C CE1 . PHE A 1 31 ? 37.806 13.722 78.586 1.00 12.75 ? 29 PHE A CE1 1 ATOM 262 C CE2 . PHE A 1 31 ? 39.208 12.043 77.532 1.00 14.53 ? 29 PHE A CE2 1 ATOM 263 C CZ . PHE A 1 31 ? 38.911 13.402 77.775 1.00 13.13 ? 29 PHE A CZ 1 ATOM 264 N N . GLU A 1 32 ? 34.900 9.405 82.106 1.00 13.90 ? 30 GLU A N 1 ATOM 265 C CA . GLU A 1 32 ? 33.614 8.780 82.348 1.00 14.72 ? 30 GLU A CA 1 ATOM 266 C C . GLU A 1 32 ? 32.774 9.012 81.086 1.00 13.66 ? 30 GLU A C 1 ATOM 267 O O . GLU A 1 32 ? 32.711 10.132 80.581 1.00 14.53 ? 30 GLU A O 1 ATOM 268 C CB . GLU A 1 32 ? 32.933 9.432 83.558 1.00 17.01 ? 30 GLU A CB 1 ATOM 269 C CG . GLU A 1 32 ? 31.494 8.923 83.795 1.00 20.00 ? 30 GLU A CG 1 ATOM 270 C CD . GLU A 1 32 ? 30.720 9.791 84.789 1.00 24.58 ? 30 GLU A CD 1 ATOM 271 O OE1 . GLU A 1 32 ? 31.297 10.768 85.329 1.00 29.89 ? 30 GLU A OE1 1 ATOM 272 O OE2 . GLU A 1 32 ? 29.530 9.500 85.040 1.00 27.28 ? 30 GLU A OE2 1 ATOM 273 N N . ILE A 1 33 ? 32.117 7.972 80.581 1.00 13.66 ? 31 ILE A N 1 ATOM 274 C CA . ILE A 1 33 ? 31.179 8.174 79.481 1.00 14.40 ? 31 ILE A CA 1 ATOM 275 C C . ILE A 1 33 ? 29.781 8.410 80.044 1.00 13.65 ? 31 ILE A C 1 ATOM 276 O O . ILE A 1 33 ? 29.226 7.550 80.733 1.00 16.35 ? 31 ILE A O 1 ATOM 277 C CB . ILE A 1 33 ? 31.165 6.967 78.494 1.00 14.23 ? 31 ILE A CB 1 ATOM 278 C CG1 . ILE A 1 33 ? 32.587 6.681 77.955 1.00 15.38 ? 31 ILE A CG1 1 ATOM 279 C CG2 . ILE A 1 33 ? 30.234 7.234 77.290 1.00 17.61 ? 31 ILE A CG2 1 ATOM 280 C CD1 . ILE A 1 33 ? 32.628 5.372 77.179 1.00 16.67 ? 31 ILE A CD1 1 ATOM 281 N N . VAL A 1 34 ? 29.222 9.588 79.769 1.00 12.55 ? 32 VAL A N 1 ATOM 282 C CA . VAL A 1 34 ? 27.890 9.933 80.249 1.00 14.40 ? 32 VAL A CA 1 ATOM 283 C C . VAL A 1 34 ? 26.941 9.697 79.084 1.00 16.08 ? 32 VAL A C 1 ATOM 284 O O . VAL A 1 34 ? 26.809 10.526 78.193 1.00 14.91 ? 32 VAL A O 1 ATOM 285 C CB . VAL A 1 34 ? 27.838 11.395 80.719 1.00 13.81 ? 32 VAL A CB 1 ATOM 286 C CG1 . VAL A 1 34 ? 26.512 11.687 81.358 1.00 16.52 ? 32 VAL A CG1 1 ATOM 287 C CG2 . VAL A 1 34 ? 28.995 11.641 81.717 1.00 13.97 ? 32 VAL A CG2 1 ATOM 288 N N . ARG A 1 35 ? 26.334 8.522 79.091 1.00 17.62 ? 33 ARG A N 1 ATOM 289 C CA . ARG A 1 35 ? 25.498 8.053 78.001 1.00 18.08 ? 33 ARG A CA 1 ATOM 290 C C . ARG A 1 35 ? 24.288 8.926 77.785 1.00 17.41 ? 33 ARG A C 1 ATOM 291 O O . ARG A 1 35 ? 23.597 9.304 78.754 1.00 19.21 ? 33 ARG A O 1 ATOM 292 C CB . ARG A 1 35 ? 25.030 6.627 78.290 1.00 21.11 ? 33 ARG A CB 1 ATOM 293 C CG . ARG A 1 35 ? 26.176 5.666 78.646 1.00 27.56 ? 33 ARG A CG 1 ATOM 294 C CD . ARG A 1 35 ? 26.147 4.423 77.804 1.00 32.74 ? 33 ARG A CD 1 ATOM 295 N NE . ARG A 1 35 ? 27.277 4.373 76.880 0.0000 35.34 ? 33 ARG A NE 1 ATOM 296 C CZ . ARG A 1 35 ? 28.486 3.920 77.196 0.0000 37.41 ? 33 ARG A CZ 1 ATOM 297 N NH1 . ARG A 1 35 ? 28.734 3.475 78.421 0.0000 38.11 ? 33 ARG A NH1 1 ATOM 298 N NH2 . ARG A 1 35 ? 29.450 3.915 76.286 0.0000 38.11 ? 33 ARG A NH2 1 ATOM 299 N N . GLN A 1 36 ? 24.004 9.227 76.520 1.00 16.23 ? 34 GLN A N 1 ATOM 300 C CA . GLN A 1 36 ? 22.926 10.128 76.175 1.00 15.22 ? 34 GLN A CA 1 ATOM 301 C C . GLN A 1 36 ? 21.829 9.360 75.499 1.00 18.57 ? 34 GLN A C 1 ATOM 302 O O . GLN A 1 36 ? 22.038 8.243 75.020 1.00 20.51 ? 34 GLN A O 1 ATOM 303 C CB . GLN A 1 36 ? 23.501 11.230 75.251 1.00 14.20 ? 34 GLN A CB 1 ATOM 304 C CG . GLN A 1 36 ? 24.575 12.095 75.961 1.00 13.94 ? 34 GLN A CG 1 ATOM 305 C CD . GLN A 1 36 ? 23.970 12.839 77.168 1.00 13.91 ? 34 GLN A CD 1 ATOM 306 O OE1 . GLN A 1 36 ? 22.931 13.469 77.042 1.00 15.31 ? 34 GLN A OE1 1 ATOM 307 N NE2 . GLN A 1 36 ? 24.610 12.716 78.358 1.00 15.33 ? 34 GLN A NE2 1 ATOM 308 N N . PRO A 1 37 ? 20.626 9.932 75.473 1.00 18.72 ? 35 PRO A N 1 ATOM 309 C CA . PRO A 1 37 ? 19.539 9.281 74.721 1.00 20.98 ? 35 PRO A CA 1 ATOM 310 C C . PRO A 1 37 ? 19.949 8.954 73.270 1.00 22.54 ? 35 PRO A C 1 ATOM 311 O O . PRO A 1 37 ? 20.614 9.770 72.641 1.00 21.94 ? 35 PRO A O 1 ATOM 312 C CB . PRO A 1 37 ? 18.422 10.345 74.755 1.00 21.01 ? 35 PRO A CB 1 ATOM 313 C CG . PRO A 1 37 ? 18.685 11.094 76.073 1.00 18.39 ? 35 PRO A CG 1 ATOM 314 C CD . PRO A 1 37 ? 20.202 11.202 76.091 1.00 17.90 ? 35 PRO A CD 1 ATOM 315 N N . GLY A 1 38 ? 19.563 7.777 72.763 1.00 23.54 ? 36 GLY A N 1 ATOM 316 C CA . GLY A 1 38 ? 19.891 7.357 71.404 1.00 24.80 ? 36 GLY A CA 1 ATOM 317 C C . GLY A 1 38 ? 19.146 8.083 70.299 1.00 25.40 ? 36 GLY A C 1 ATOM 318 O O . GLY A 1 38 ? 19.452 7.877 69.077 1.00 29.73 ? 36 GLY A O 1 ATOM 319 N N . ASP A 1 39 ? 18.197 8.944 70.670 1.00 18.26 ? 37 ASP A N 1 ATOM 320 C CA . ASP A 1 39 ? 17.408 9.627 69.638 1.00 17.28 ? 37 ASP A CA 1 ATOM 321 C C . ASP A 1 39 ? 18.285 10.576 68.830 1.00 14.40 ? 37 ASP A C 1 ATOM 322 O O . ASP A 1 39 ? 19.451 10.787 69.167 1.00 15.90 ? 37 ASP A O 1 ATOM 323 C CB . ASP A 1 39 ? 16.204 10.376 70.225 1.00 15.84 ? 37 ASP A CB 1 ATOM 324 C CG . ASP A 1 39 ? 16.610 11.420 71.270 1.00 17.11 ? 37 ASP A CG 1 ATOM 325 O OD1 . ASP A 1 39 ? 17.321 12.363 70.914 1.00 16.50 ? 37 ASP A OD1 1 ATOM 326 O OD2 . ASP A 1 39 ? 16.168 11.326 72.435 1.00 16.57 ? 37 ASP A OD2 1 ATOM 327 N N . GLY A 1 40 ? 17.707 11.155 67.776 1.00 13.95 ? 38 GLY A N 1 ATOM 328 C CA . GLY A 1 40 ? 18.457 11.986 66.853 1.00 11.43 ? 38 GLY A CA 1 ATOM 329 C C . GLY A 1 40 ? 18.995 13.283 67.416 1.00 11.25 ? 38 GLY A C 1 ATOM 330 O O . GLY A 1 40 ? 19.758 13.962 66.721 1.00 13.12 ? 38 GLY A O 1 ATOM 331 N N . ASN A 1 41 ? 18.626 13.620 68.656 1.00 11.79 ? 39 ASN A N 1 ATOM 332 C CA . ASN A 1 41 ? 19.142 14.835 69.277 1.00 11.23 ? 39 ASN A CA 1 ATOM 333 C C . ASN A 1 41 ? 20.378 14.626 70.126 1.00 10.90 ? 39 ASN A C 1 ATOM 334 O O . ASN A 1 41 ? 20.754 15.544 70.845 1.00 11.65 ? 39 ASN A O 1 ATOM 335 C CB . ASN A 1 41 ? 18.024 15.501 70.126 1.00 11.75 ? 39 ASN A CB 1 ATOM 336 C CG . ASN A 1 41 ? 16.725 15.660 69.332 1.00 11.29 ? 39 ASN A CG 1 ATOM 337 O OD1 . ASN A 1 41 ? 16.762 16.154 68.223 1.00 15.04 ? 39 ASN A OD1 1 ATOM 338 N ND2 . ASN A 1 41 ? 15.587 15.254 69.901 1.00 13.00 ? 39 ASN A ND2 1 ATOM 339 N N . CYS A 1 42 ? 20.993 13.457 70.058 1.00 10.64 ? 40 CYS A N 1 ATOM 340 C CA . CYS A 1 42 ? 22.100 13.120 70.976 1.00 11.16 ? 40 CYS A CA 1 ATOM 341 C C . CYS A 1 42 ? 23.247 14.152 70.990 1.00 11.23 ? 40 CYS A C 1 ATOM 342 O O . CYS A 1 42 ? 23.853 14.359 72.014 1.00 11.61 ? 40 CYS A O 1 ATOM 343 C CB . CYS A 1 42 ? 22.665 11.700 70.660 1.00 11.90 ? 40 CYS A CB 1 ATOM 344 S SG . CYS A 1 42 ? 23.486 11.552 69.037 1.00 11.47 ? 40 CYS A SG 1 ATOM 345 N N . PHE A 1 43 ? 23.579 14.765 69.854 1.00 10.71 ? 41 PHE A N 1 ATOM 346 C CA . PHE A 1 43 ? 24.647 15.772 69.838 1.00 9.67 ? 41 PHE A CA 1 ATOM 347 C C . PHE A 1 43 ? 24.283 16.906 70.804 1.00 11.85 ? 41 PHE A C 1 ATOM 348 O O . PHE A 1 43 ? 25.095 17.325 71.609 1.00 10.82 ? 41 PHE A O 1 ATOM 349 C CB . PHE A 1 43 ? 24.835 16.373 68.423 1.00 10.73 ? 41 PHE A CB 1 ATOM 350 C CG . PHE A 1 43 ? 25.773 17.538 68.403 1.00 11.27 ? 41 PHE A CG 1 ATOM 351 C CD1 . PHE A 1 43 ? 27.179 17.344 68.397 1.00 10.76 ? 41 PHE A CD1 1 ATOM 352 C CD2 . PHE A 1 43 ? 25.278 18.827 68.342 1.00 10.09 ? 41 PHE A CD2 1 ATOM 353 C CE1 . PHE A 1 43 ? 28.058 18.440 68.383 1.00 10.34 ? 41 PHE A CE1 1 ATOM 354 C CE2 . PHE A 1 43 ? 26.172 19.935 68.320 1.00 11.45 ? 41 PHE A CE2 1 ATOM 355 C CZ . PHE A 1 43 ? 27.577 19.719 68.345 1.00 10.89 ? 41 PHE A CZ 1 ATOM 356 N N . TYR A 1 44 ? 23.073 17.429 70.678 1.00 10.26 ? 42 TYR A N 1 ATOM 357 C CA . TYR A 1 44 ? 22.683 18.547 71.516 1.00 9.84 ? 42 TYR A CA 1 ATOM 358 C C . TYR A 1 44 ? 22.429 18.141 72.969 1.00 10.93 ? 42 TYR A C 1 ATOM 359 O O . TYR A 1 44 ? 22.687 18.943 73.885 1.00 10.82 ? 42 TYR A O 1 ATOM 360 C CB . TYR A 1 44 ? 21.415 19.229 70.939 1.00 9.39 ? 42 TYR A CB 1 ATOM 361 C CG . TYR A 1 44 ? 21.630 19.606 69.484 1.00 10.60 ? 42 TYR A CG 1 ATOM 362 C CD1 . TYR A 1 44 ? 22.304 20.793 69.135 1.00 9.69 ? 42 TYR A CD1 1 ATOM 363 C CD2 . TYR A 1 44 ? 21.161 18.794 68.455 1.00 11.00 ? 42 TYR A CD2 1 ATOM 364 C CE1 . TYR A 1 44 ? 22.495 21.146 67.794 1.00 11.20 ? 42 TYR A CE1 1 ATOM 365 C CE2 . TYR A 1 44 ? 21.403 19.142 67.106 1.00 11.27 ? 42 TYR A CE2 1 ATOM 366 C CZ . TYR A 1 44 ? 22.025 20.327 66.801 1.00 11.83 ? 42 TYR A CZ 1 ATOM 367 O OH . TYR A 1 44 ? 22.236 20.702 65.480 1.00 12.02 ? 42 TYR A OH 1 ATOM 368 N N . HIS A 1 45 ? 21.951 16.919 73.173 1.00 10.13 ? 43 HIS A N 1 ATOM 369 C CA . HIS A 1 45 ? 21.823 16.364 74.538 1.00 9.74 ? 43 HIS A CA 1 ATOM 370 C C . HIS A 1 45 ? 23.213 16.386 75.197 1.00 10.96 ? 43 HIS A C 1 ATOM 371 O O . HIS A 1 45 ? 23.360 16.752 76.366 1.00 11.57 ? 43 HIS A O 1 ATOM 372 C CB . HIS A 1 45 ? 21.381 14.888 74.455 1.00 10.02 ? 43 HIS A CB 1 ATOM 373 C CG . HIS A 1 45 ? 19.899 14.690 74.365 1.00 11.99 ? 43 HIS A CG 1 ATOM 374 N ND1 . HIS A 1 45 ? 19.034 15.139 75.339 1.00 14.27 ? 43 HIS A ND1 1 ATOM 375 C CD2 . HIS A 1 45 ? 19.150 13.936 73.534 1.00 11.52 ? 43 HIS A CD2 1 ATOM 376 C CE1 . HIS A 1 45 ? 17.797 14.755 75.067 1.00 13.15 ? 43 HIS A CE1 1 ATOM 377 N NE2 . HIS A 1 45 ? 17.835 14.034 73.967 1.00 12.68 ? 43 HIS A NE2 1 ATOM 378 N N . SER A 1 46 ? 24.225 15.964 74.448 1.00 11.62 ? 44 SER A N 1 ATOM 379 C CA . SER A 1 46 ? 25.594 15.865 74.990 1.00 10.44 ? 44 SER A CA 1 ATOM 380 C C . SER A 1 46 ? 26.147 17.251 75.356 1.00 11.16 ? 44 SER A C 1 ATOM 381 O O . SER A 1 46 ? 26.802 17.425 76.403 1.00 13.52 ? 44 SER A O 1 ATOM 382 C CB . SER A 1 46 ? 26.522 15.212 73.952 1.00 8.20 ? 44 SER A CB 1 ATOM 383 O OG . SER A 1 46 ? 26.132 13.873 73.702 1.00 10.26 ? 44 SER A OG 1 ATOM 384 N N . ILE A 1 47 ? 25.937 18.236 74.483 1.00 10.96 ? 45 ILE A N 1 ATOM 385 C CA . ILE A 1 47 ? 26.384 19.571 74.786 1.00 12.23 ? 45 ILE A CA 1 ATOM 386 C C . ILE A 1 47 ? 25.681 20.100 76.027 1.00 10.97 ? 45 ILE A C 1 ATOM 387 O O . ILE A 1 47 ? 26.330 20.700 76.921 1.00 12.69 ? 45 ILE A O 1 ATOM 388 C CB . ILE A 1 47 ? 26.152 20.574 73.579 1.00 11.31 ? 45 ILE A CB 1 ATOM 389 C CG1 . ILE A 1 47 ? 26.924 20.156 72.309 1.00 15.88 ? 45 ILE A CG1 1 ATOM 390 C CG2 . ILE A 1 47 ? 26.556 21.961 74.007 1.00 10.34 ? 45 ILE A CG2 1 ATOM 391 C CD1 . ILE A 1 47 ? 28.409 20.249 72.498 1.00 19.50 ? 45 ILE A CD1 1 ATOM 392 N N . ALA A 1 48 ? 24.370 19.886 76.085 1.00 9.68 ? 46 ALA A N 1 ATOM 393 C CA . ALA A 1 48 ? 23.592 20.374 77.230 1.00 11.75 ? 46 ALA A CA 1 ATOM 394 C C . ALA A 1 48 ? 24.081 19.731 78.545 1.00 12.28 ? 46 ALA A C 1 ATOM 395 O O . ALA A 1 48 ? 24.193 20.401 79.579 1.00 12.48 ? 46 ALA A O 1 ATOM 396 C CB . ALA A 1 48 ? 22.059 20.093 77.014 1.00 14.16 ? 46 ALA A CB 1 ATOM 397 N N . GLU A 1 49 ? 24.399 18.444 78.469 1.00 11.13 ? 47 GLU A N 1 ATOM 398 C CA . GLU A 1 49 ? 24.852 17.709 79.644 1.00 11.07 ? 47 GLU A CA 1 ATOM 399 C C . GLU A 1 49 ? 26.052 18.423 80.253 1.00 11.85 ? 47 GLU A C 1 ATOM 400 O O . GLU A 1 49 ? 26.190 18.521 81.478 1.00 15.24 ? 47 GLU A O 1 ATOM 401 C CB . GLU A 1 49 ? 25.248 16.289 79.239 1.00 13.10 ? 47 GLU A CB 1 ATOM 402 C CG . GLU A 1 49 ? 25.865 15.431 80.333 1.00 18.26 ? 47 GLU A CG 1 ATOM 403 C CD . GLU A 1 49 ? 24.823 14.970 81.331 1.00 23.95 ? 47 GLU A CD 1 ATOM 404 O OE1 . GLU A 1 49 ? 23.780 14.389 80.884 1.00 28.33 ? 47 GLU A OE1 1 ATOM 405 O OE2 . GLU A 1 49 ? 25.055 15.179 82.535 1.00 23.66 ? 47 GLU A OE2 1 ATOM 406 N N . LEU A 1 50 ? 26.936 18.911 79.392 1.00 11.35 ? 48 LEU A N 1 ATOM 407 C CA . LEU A 1 50 ? 28.226 19.413 79.854 1.00 10.83 ? 48 LEU A CA 1 ATOM 408 C C . LEU A 1 50 ? 28.272 20.932 80.055 1.00 13.56 ? 48 LEU A C 1 ATOM 409 O O . LEU A 1 50 ? 29.295 21.457 80.536 1.00 14.88 ? 48 LEU A O 1 ATOM 410 C CB . LEU A 1 50 ? 29.330 18.998 78.865 1.00 10.52 ? 48 LEU A CB 1 ATOM 411 C CG . LEU A 1 50 ? 29.579 17.463 78.870 1.00 12.13 ? 48 LEU A CG 1 ATOM 412 C CD1 . LEU A 1 50 ? 30.542 17.095 77.737 1.00 12.48 ? 48 LEU A CD1 1 ATOM 413 C CD2 . LEU A 1 50 ? 30.066 16.928 80.237 1.00 11.69 ? 48 LEU A CD2 1 ATOM 414 N N . THR A 1 51 ? 27.208 21.649 79.659 1.00 11.08 ? 49 THR A N 1 ATOM 415 C CA . THR A 1 51 ? 27.203 23.117 79.765 1.00 10.57 ? 49 THR A CA 1 ATOM 416 C C . THR A 1 51 ? 26.083 23.686 80.614 1.00 11.27 ? 49 THR A C 1 ATOM 417 O O . THR A 1 51 ? 26.142 24.844 80.989 1.00 13.06 ? 49 THR A O 1 ATOM 418 C CB . THR A 1 51 ? 27.079 23.774 78.368 1.00 11.30 ? 49 THR A CB 1 ATOM 419 O OG1 . THR A 1 51 ? 25.888 23.293 77.697 1.00 11.96 ? 49 THR A OG1 1 ATOM 420 C CG2 . THR A 1 51 ? 28.292 23.438 77.557 1.00 13.30 ? 49 THR A CG2 1 ATOM 421 N N . MET A 1 52 ? 25.058 22.887 80.891 1.00 11.86 ? 50 MET A N 1 ATOM 422 C CA . MET A 1 52 ? 23.858 23.373 81.600 1.00 12.28 ? 50 MET A CA 1 ATOM 423 C C . MET A 1 52 ? 23.679 22.655 82.928 1.00 14.48 ? 50 MET A C 1 ATOM 424 O O . MET A 1 52 ? 23.140 21.551 82.974 1.00 15.66 ? 50 MET A O 1 ATOM 425 C CB . MET A 1 52 ? 22.604 23.170 80.720 1.00 12.87 ? 50 MET A CB 1 ATOM 426 C CG . MET A 1 52 ? 22.725 23.906 79.382 1.00 12.33 ? 50 MET A CG 1 ATOM 427 S SD . MET A 1 52 ? 21.305 23.633 78.272 1.00 15.17 ? 50 MET A SD 1 ATOM 428 C CE . MET A 1 52 ? 20.046 24.548 79.204 1.00 13.97 ? 50 MET A CE 1 ATOM 429 N N . PRO A 1 53 ? 24.094 23.294 84.022 1.00 15.47 ? 51 PRO A N 1 ATOM 430 C CA . PRO A 1 53 ? 24.008 22.611 85.331 1.00 20.02 ? 51 PRO A CA 1 ATOM 431 C C . PRO A 1 53 ? 22.598 22.245 85.776 1.00 23.73 ? 51 PRO A C 1 ATOM 432 O O . PRO A 1 53 ? 21.642 22.984 85.489 1.00 25.04 ? 51 PRO A O 1 ATOM 433 C CB . PRO A 1 53 ? 24.635 23.621 86.290 1.00 20.38 ? 51 PRO A CB 1 ATOM 434 C CG . PRO A 1 53 ? 25.602 24.398 85.443 1.00 19.35 ? 51 PRO A CG 1 ATOM 435 C CD . PRO A 1 53 ? 24.826 24.568 84.112 1.00 16.94 ? 51 PRO A CD 1 ATOM 436 N N . ASN A 1 54 ? 22.466 21.095 86.430 1.00 26.67 ? 52 ASN A N 1 ATOM 437 C CA . ASN A 1 54 ? 21.154 20.575 86.838 1.00 32.90 ? 52 ASN A CA 1 ATOM 438 C C . ASN A 1 54 ? 20.057 20.661 85.757 1.00 35.00 ? 52 ASN A C 1 ATOM 439 O O . ASN A 1 54 ? 18.903 21.004 86.043 1.00 38.30 ? 52 ASN A O 1 ATOM 440 C CB . ASN A 1 54 ? 20.692 21.253 88.147 1.00 36.02 ? 52 ASN A CB 1 ATOM 441 C CG . ASN A 1 54 ? 21.638 20.988 89.305 0.0000 37.68 ? 52 ASN A CG 1 ATOM 442 O OD1 . ASN A 1 54 ? 22.064 21.913 89.997 0.0000 38.28 ? 52 ASN A OD1 1 ATOM 443 N ND2 . ASN A 1 54 ? 21.975 19.721 89.516 0.0000 38.29 ? 52 ASN A ND2 1 ATOM 444 N N . LYS A 1 55 ? 20.428 20.343 84.523 1.00 32.43 ? 53 LYS A N 1 ATOM 445 C CA . LYS A 1 55 ? 19.529 20.424 83.376 1.00 30.96 ? 53 LYS A CA 1 ATOM 446 C C . LYS A 1 55 ? 18.241 19.568 83.485 1.00 31.80 ? 53 LYS A C 1 ATOM 447 O O . LYS A 1 55 ? 18.066 18.771 84.409 1.00 32.66 ? 53 LYS A O 1 ATOM 448 C CB . LYS A 1 55 ? 20.304 20.077 82.118 1.00 30.01 ? 53 LYS A CB 1 ATOM 449 C CG . LYS A 1 55 ? 20.691 18.612 81.981 1.00 29.93 ? 53 LYS A CG 1 ATOM 450 C CD . LYS A 1 55 ? 21.237 18.363 80.540 1.00 27.25 ? 53 LYS A CD 1 ATOM 451 C CE . LYS A 1 55 ? 21.281 16.891 80.164 1.00 25.95 ? 53 LYS A CE 1 ATOM 452 N NZ . LYS A 1 55 ? 19.887 16.361 79.998 1.00 26.67 ? 53 LYS A NZ 1 ATOM 453 N N . THR A 1 56 ? 17.326 19.788 82.555 1.00 30.93 ? 54 THR A N 1 ATOM 454 C CA . THR A 1 56 ? 16.075 19.035 82.450 1.00 28.82 ? 54 THR A CA 1 ATOM 455 C C . THR A 1 56 ? 16.200 18.053 81.292 1.00 26.22 ? 54 THR A C 1 ATOM 456 O O . THR A 1 56 ? 17.186 18.085 80.587 1.00 26.56 ? 54 THR A O 1 ATOM 457 C CB . THR A 1 56 ? 14.913 19.990 82.133 1.00 32.30 ? 54 THR A CB 1 ATOM 458 O OG1 . THR A 1 56 ? 14.789 20.931 83.226 1.00 35.54 ? 54 THR A OG1 1 ATOM 459 C CG2 . THR A 1 56 ? 13.631 19.205 81.996 1.00 36.35 ? 54 THR A CG2 1 ATOM 460 N N . ASP A 1 57 ? 15.212 17.188 81.094 1.00 24.27 ? 55 ASP A N 1 ATOM 461 C CA . ASP A 1 57 ? 15.290 16.143 80.091 1.00 26.32 ? 55 ASP A CA 1 ATOM 462 C C . ASP A 1 57 ? 15.541 16.626 78.689 1.00 24.85 ? 55 ASP A C 1 ATOM 463 O O . ASP A 1 57 ? 16.187 15.918 77.874 1.00 26.49 ? 55 ASP A O 1 ATOM 464 C CB . ASP A 1 57 ? 13.993 15.342 80.072 1.00 28.37 ? 55 ASP A CB 1 ATOM 465 C CG . ASP A 1 57 ? 13.815 14.525 81.311 1.00 30.07 ? 55 ASP A CG 1 ATOM 466 O OD1 . ASP A 1 57 ? 14.810 14.327 82.049 1.00 31.71 ? 55 ASP A OD1 1 ATOM 467 O OD2 . ASP A 1 57 ? 12.672 14.078 81.541 1.00 30.30 ? 55 ASP A OD2 1 ATOM 468 N N . HIS A 1 58 ? 14.980 17.793 78.392 1.00 18.85 ? 56 HIS A N 1 ATOM 469 C CA . HIS A 1 58 ? 15.113 18.369 77.058 1.00 17.50 ? 56 HIS A CA 1 ATOM 470 C C . HIS A 1 58 ? 15.720 19.769 77.126 1.00 16.65 ? 56 HIS A C 1 ATOM 471 O O . HIS A 1 58 ? 15.301 20.669 76.386 1.00 18.05 ? 56 HIS A O 1 ATOM 472 C CB . HIS A 1 58 ? 13.749 18.494 76.386 1.00 16.15 ? 56 HIS A CB 1 ATOM 473 C CG . HIS A 1 58 ? 13.220 17.243 75.761 1.00 16.36 ? 56 HIS A CG 1 ATOM 474 N ND1 . HIS A 1 58 ? 13.573 15.959 76.152 1.00 19.10 ? 56 HIS A ND1 1 ATOM 475 C CD2 . HIS A 1 58 ? 12.300 17.099 74.772 1.00 12.88 ? 56 HIS A CD2 1 ATOM 476 C CE1 . HIS A 1 58 ? 12.913 15.086 75.408 1.00 16.43 ? 56 HIS A CE1 1 ATOM 477 N NE2 . HIS A 1 58 ? 12.144 15.755 74.558 1.00 19.41 ? 56 HIS A NE2 1 ATOM 478 N N . SER A 1 59 ? 16.711 19.969 77.984 1.00 15.60 ? 57 SER A N 1 ATOM 479 C CA . SER A 1 59 ? 17.471 21.216 77.976 1.00 14.80 ? 57 SER A CA 1 ATOM 480 C C . SER A 1 59 ? 18.169 21.468 76.638 1.00 13.77 ? 57 SER A C 1 ATOM 481 O O . SER A 1 59 ? 18.521 22.593 76.340 1.00 14.46 ? 57 SER A O 1 ATOM 482 C CB . SER A 1 59 ? 18.520 21.182 79.099 1.00 18.00 ? 57 SER A CB 1 ATOM 483 O OG . SER A 1 59 ? 17.900 21.313 80.374 1.00 20.72 ? 57 SER A OG 1 ATOM 484 N N . TYR A 1 60 ? 18.337 20.419 75.827 1.00 12.77 ? 58 TYR A N 1 ATOM 485 C CA . TYR A 1 60 ? 18.956 20.589 74.530 1.00 12.65 ? 58 TYR A CA 1 ATOM 486 C C . TYR A 1 60 ? 18.251 21.604 73.637 1.00 14.13 ? 58 TYR A C 1 ATOM 487 O O . TYR A 1 60 ? 18.890 22.155 72.719 1.00 14.03 ? 58 TYR A O 1 ATOM 488 C CB . TYR A 1 60 ? 19.063 19.256 73.771 1.00 10.85 ? 58 TYR A CB 1 ATOM 489 C CG . TYR A 1 60 ? 17.785 18.764 73.183 1.00 12.38 ? 58 TYR A CG 1 ATOM 490 C CD1 . TYR A 1 60 ? 17.388 19.180 71.902 1.00 13.99 ? 58 TYR A CD1 1 ATOM 491 C CD2 . TYR A 1 60 ? 16.974 17.881 73.881 1.00 13.50 ? 58 TYR A CD2 1 ATOM 492 C CE1 . TYR A 1 60 ? 16.200 18.729 71.347 1.00 15.06 ? 58 TYR A CE1 1 ATOM 493 C CE2 . TYR A 1 60 ? 15.774 17.433 73.311 1.00 14.30 ? 58 TYR A CE2 1 ATOM 494 C CZ . TYR A 1 60 ? 15.417 17.865 72.041 1.00 17.25 ? 58 TYR A CZ 1 ATOM 495 O OH . TYR A 1 60 ? 14.263 17.430 71.458 1.00 18.57 ? 58 TYR A OH 1 ATOM 496 N N . HIS A 1 61 ? 16.958 21.841 73.854 1.00 13.77 ? 59 HIS A N 1 ATOM 497 C CA . HIS A 1 61 ? 16.297 22.880 73.035 1.00 14.25 ? 59 HIS A CA 1 ATOM 498 C C . HIS A 1 61 ? 17.024 24.227 73.140 1.00 13.45 ? 59 HIS A C 1 ATOM 499 O O . HIS A 1 61 ? 17.133 24.942 72.140 1.00 14.65 ? 59 HIS A O 1 ATOM 500 C CB . HIS A 1 61 ? 14.816 23.074 73.397 1.00 14.09 ? 59 HIS A CB 1 ATOM 501 C CG . HIS A 1 61 ? 13.986 21.863 73.161 1.00 14.89 ? 59 HIS A CG 1 ATOM 502 N ND1 . HIS A 1 61 ? 13.787 21.342 71.897 1.00 15.24 ? 59 HIS A ND1 1 ATOM 503 C CD2 . HIS A 1 61 ? 13.273 21.086 74.014 1.00 15.33 ? 59 HIS A CD2 1 ATOM 504 C CE1 . HIS A 1 61 ? 12.984 20.295 71.980 1.00 16.90 ? 59 HIS A CE1 1 ATOM 505 N NE2 . HIS A 1 61 ? 12.685 20.096 73.253 1.00 15.62 ? 59 HIS A NE2 1 ATOM 506 N N . TYR A 1 62 ? 17.537 24.577 74.325 1.00 12.44 ? 60 TYR A N 1 ATOM 507 C CA . TYR A 1 62 ? 18.245 25.821 74.481 1.00 12.72 ? 60 TYR A CA 1 ATOM 508 C C . TYR A 1 62 ? 19.513 25.808 73.605 1.00 12.52 ? 60 TYR A C 1 ATOM 509 O O . TYR A 1 62 ? 19.862 26.819 72.973 1.00 12.42 ? 60 TYR A O 1 ATOM 510 C CB . TYR A 1 62 ? 18.614 26.015 75.958 1.00 15.99 ? 60 TYR A CB 1 ATOM 511 C CG . TYR A 1 62 ? 19.501 27.236 76.222 1.00 20.88 ? 60 TYR A CG 1 ATOM 512 C CD1 . TYR A 1 62 ? 19.019 28.513 76.071 1.00 25.85 ? 60 TYR A CD1 1 ATOM 513 C CD2 . TYR A 1 62 ? 20.836 27.090 76.569 1.00 23.51 ? 60 TYR A CD2 1 ATOM 514 C CE1 . TYR A 1 62 ? 19.834 29.623 76.330 1.00 27.82 ? 60 TYR A CE1 1 ATOM 515 C CE2 . TYR A 1 62 ? 21.639 28.177 76.823 1.00 26.60 ? 60 TYR A CE2 1 ATOM 516 C CZ . TYR A 1 62 ? 21.145 29.446 76.687 1.00 29.93 ? 60 TYR A CZ 1 ATOM 517 O OH . TYR A 1 62 ? 21.980 30.550 76.933 1.00 33.58 ? 60 TYR A OH 1 ATOM 518 N N . ILE A 1 63 ? 20.221 24.682 73.601 1.00 11.63 ? 61 ILE A N 1 ATOM 519 C CA . ILE A 1 63 ? 21.428 24.577 72.772 1.00 8.83 ? 61 ILE A CA 1 ATOM 520 C C . ILE A 1 63 ? 21.062 24.740 71.296 1.00 10.07 ? 61 ILE A C 1 ATOM 521 O O . ILE A 1 63 ? 21.796 25.392 70.530 1.00 12.18 ? 61 ILE A O 1 ATOM 522 C CB . ILE A 1 63 ? 22.179 23.228 73.010 1.00 9.97 ? 61 ILE A CB 1 ATOM 523 C CG1 . ILE A 1 63 ? 22.529 23.040 74.514 1.00 10.85 ? 61 ILE A CG1 1 ATOM 524 C CG2 . ILE A 1 63 ? 23.461 23.125 72.122 1.00 11.08 ? 61 ILE A CG2 1 ATOM 525 C CD1 . ILE A 1 63 ? 23.436 24.137 75.074 1.00 12.79 ? 61 ILE A CD1 1 ATOM 526 N N . LYS A 1 64 ? 19.948 24.152 70.878 1.00 10.54 ? 62 LYS A N 1 ATOM 527 C CA . LYS A 1 64 ? 19.538 24.316 69.464 1.00 10.59 ? 62 LYS A CA 1 ATOM 528 C C . LYS A 1 64 ? 19.142 25.736 69.166 1.00 11.54 ? 62 LYS A C 1 ATOM 529 O O . LYS A 1 64 ? 19.397 26.225 68.044 1.00 11.49 ? 62 LYS A O 1 ATOM 530 C CB . LYS A 1 64 ? 18.441 23.298 69.057 1.00 11.54 ? 62 LYS A CB 1 ATOM 531 C CG . LYS A 1 64 ? 18.925 21.844 69.161 1.00 11.66 ? 62 LYS A CG 1 ATOM 532 C CD . LYS A 1 64 ? 17.902 20.834 68.581 1.00 11.51 ? 62 LYS A CD 1 ATOM 533 C CE . LYS A 1 64 ? 17.836 20.966 67.044 1.00 11.46 ? 62 LYS A CE 1 ATOM 534 N NZ . LYS A 1 64 ? 17.053 19.874 66.427 1.00 13.24 ? 62 LYS A NZ 1 ATOM 535 N N . ARG A 1 65 ? 18.533 26.432 70.138 1.00 12.07 ? 63 ARG A N 1 ATOM 536 C CA . ARG A 1 65 ? 18.306 27.870 69.965 1.00 14.03 ? 63 ARG A CA 1 ATOM 537 C C . ARG A 1 65 ? 19.603 28.681 69.799 1.00 13.79 ? 63 ARG A C 1 ATOM 538 O O . ARG A 1 65 ? 19.650 29.643 68.977 1.00 14.24 ? 63 ARG A O 1 ATOM 539 C CB . ARG A 1 65 ? 17.420 28.460 71.078 1.00 17.19 ? 63 ARG A CB 1 ATOM 540 C CG . ARG A 1 65 ? 16.009 27.880 71.041 1.00 21.81 ? 63 ARG A CG 1 ATOM 541 C CD . ARG A 1 65 ? 15.006 28.655 71.925 1.00 27.81 ? 63 ARG A CD 1 ATOM 542 N NE . ARG A 1 65 ? 15.369 28.651 73.348 1.00 33.38 ? 63 ARG A NE 1 ATOM 543 C CZ . ARG A 1 65 ? 15.047 27.692 74.218 1.00 35.64 ? 63 ARG A CZ 1 ATOM 544 N NH1 . ARG A 1 65 ? 14.372 26.618 73.825 1.00 35.39 ? 63 ARG A NH1 1 ATOM 545 N NH2 . ARG A 1 65 ? 15.420 27.794 75.480 1.00 37.10 ? 63 ARG A NH2 1 ATOM 546 N N . LEU A 1 66 ? 20.631 28.303 70.575 1.00 12.11 ? 64 LEU A N 1 ATOM 547 C CA . LEU A 1 66 ? 21.911 28.954 70.451 1.00 14.68 ? 64 LEU A CA 1 ATOM 548 C C . LEU A 1 66 ? 22.552 28.632 69.101 1.00 12.93 ? 64 LEU A C 1 ATOM 549 O O . LEU A 1 66 ? 23.264 29.456 68.511 1.00 13.75 ? 64 LEU A O 1 ATOM 550 C CB . LEU A 1 66 ? 22.871 28.520 71.569 1.00 15.49 ? 64 LEU A CB 1 ATOM 551 C CG . LEU A 1 66 ? 22.454 29.066 72.950 1.00 16.99 ? 64 LEU A CG 1 ATOM 552 C CD1 . LEU A 1 66 ? 23.379 28.524 74.070 1.00 18.68 ? 64 LEU A CD1 1 ATOM 553 C CD2 . LEU A 1 66 ? 22.500 30.569 72.918 1.00 22.08 ? 64 LEU A CD2 1 ATOM 554 N N . THR A 1 67 ? 22.280 27.438 68.604 1.00 10.58 ? 65 THR A N 1 ATOM 555 C CA . THR A 1 67 ? 22.794 27.018 67.283 1.00 11.52 ? 65 THR A CA 1 ATOM 556 C C . THR A 1 67 ? 22.174 27.862 66.184 1.00 11.36 ? 65 THR A C 1 ATOM 557 O O . THR A 1 67 ? 22.864 28.276 65.253 1.00 12.04 ? 65 THR A O 1 ATOM 558 C CB . THR A 1 67 ? 22.566 25.500 67.054 1.00 10.41 ? 65 THR A CB 1 ATOM 559 O OG1 . THR A 1 67 ? 23.165 24.768 68.140 1.00 11.78 ? 65 THR A OG1 1 ATOM 560 C CG2 . THR A 1 67 ? 23.224 25.006 65.755 1.00 11.18 ? 65 THR A CG2 1 ATOM 561 N N . GLU A 1 68 ? 20.891 28.161 66.325 1.00 13.20 ? 66 GLU A N 1 ATOM 562 C CA . GLU A 1 68 ? 20.208 29.015 65.373 1.00 12.45 ? 66 GLU A CA 1 ATOM 563 C C . GLU A 1 68 ? 20.846 30.416 65.355 1.00 14.68 ? 66 GLU A C 1 ATOM 564 O O . GLU A 1 68 ? 21.133 30.983 64.289 1.00 14.22 ? 66 GLU A O 1 ATOM 565 C CB . GLU A 1 68 ? 18.715 29.093 65.709 1.00 13.19 ? 66 GLU A CB 1 ATOM 566 C CG . GLU A 1 68 ? 17.960 30.103 64.881 1.00 19.98 ? 66 GLU A CG 1 ATOM 567 C CD . GLU A 1 68 ? 16.504 30.168 65.280 1.00 24.92 ? 66 GLU A CD 1 ATOM 568 O OE1 . GLU A 1 68 ? 16.113 29.528 66.273 1.00 27.42 ? 66 GLU A OE1 1 ATOM 569 O OE2 . GLU A 1 68 ? 15.753 30.864 64.606 1.00 29.55 ? 66 GLU A OE2 1 ATOM 570 N N . SER A 1 69 ? 21.034 30.981 66.543 1.00 13.82 ? 67 SER A N 1 ATOM 571 C CA . SER A 1 69 ? 21.603 32.307 66.680 1.00 16.80 ? 67 SER A CA 1 ATOM 572 C C . SER A 1 69 ? 23.028 32.327 66.085 1.00 16.01 ? 67 SER A C 1 ATOM 573 O O . SER A 1 69 ? 23.418 33.255 65.319 1.00 15.25 ? 67 SER A O 1 ATOM 574 C CB . SER A 1 69 ? 21.594 32.678 68.173 1.00 20.52 ? 67 SER A CB 1 ATOM 575 O OG . SER A 1 69 ? 22.221 33.919 68.360 1.00 27.25 ? 67 SER A OG 1 ATOM 576 N N . ALA A 1 70 ? 23.782 31.277 66.420 1.00 14.74 ? 68 ALA A N 1 ATOM 577 C CA . ALA A 1 70 ? 25.147 31.127 65.903 1.00 13.31 ? 68 ALA A CA 1 ATOM 578 C C . ALA A 1 70 ? 25.128 31.056 64.368 1.00 14.14 ? 68 ALA A C 1 ATOM 579 O O . ALA A 1 70 ? 25.979 31.673 63.696 1.00 15.02 ? 68 ALA A O 1 ATOM 580 C CB . ALA A 1 70 ? 25.782 29.852 66.462 1.00 13.30 ? 68 ALA A CB 1 ATOM 581 N N . ALA A 1 71 ? 24.219 30.249 63.824 1.00 12.69 ? 69 ALA A N 1 ATOM 582 C CA . ALA A 1 71 ? 24.169 30.043 62.349 1.00 10.96 ? 69 ALA A CA 1 ATOM 583 C C . ALA A 1 71 ? 23.865 31.351 61.640 1.00 14.70 ? 69 ALA A C 1 ATOM 584 O O . ALA A 1 71 ? 24.427 31.620 60.576 1.00 15.09 ? 69 ALA A O 1 ATOM 585 C CB . ALA A 1 71 ? 23.128 28.952 61.974 1.00 11.62 ? 69 ALA A CB 1 ATOM 586 N N . ARG A 1 72 ? 22.986 32.172 62.206 1.00 15.83 ? 70 ARG A N 1 ATOM 587 C CA . ARG A 1 72 ? 22.659 33.445 61.565 1.00 17.99 ? 70 ARG A CA 1 ATOM 588 C C . ARG A 1 72 ? 23.887 34.352 61.408 1.00 20.46 ? 70 ARG A C 1 ATOM 589 O O . ARG A 1 72 ? 23.961 35.162 60.470 1.00 21.68 ? 70 ARG A O 1 ATOM 590 C CB . ARG A 1 72 ? 21.540 34.165 62.322 1.00 19.28 ? 70 ARG A CB 1 ATOM 591 C CG . ARG A 1 72 ? 20.212 33.448 62.263 1.00 23.41 ? 70 ARG A CG 1 ATOM 592 C CD . ARG A 1 72 ? 19.094 34.294 62.866 1.00 27.25 ? 70 ARG A CD 1 ATOM 593 N NE . ARG A 1 72 ? 17.889 33.502 63.076 1.00 30.96 ? 70 ARG A NE 1 ATOM 594 C CZ . ARG A 1 72 ? 16.987 33.252 62.134 1.00 33.63 ? 70 ARG A CZ 1 ATOM 595 N NH1 . ARG A 1 72 ? 17.153 33.737 60.896 1.00 33.58 ? 70 ARG A NH1 1 ATOM 596 N NH2 . ARG A 1 72 ? 15.916 32.508 62.438 1.00 34.17 ? 70 ARG A NH2 1 ATOM 597 N N . LYS A 1 73 ? 24.843 34.216 62.341 1.00 17.22 ? 71 LYS A N 1 ATOM 598 C CA . LYS A 1 73 ? 26.074 34.977 62.294 1.00 18.79 ? 71 LYS A CA 1 ATOM 599 C C . LYS A 1 73 ? 27.166 34.314 61.462 1.00 16.92 ? 71 LYS A C 1 ATOM 600 O O . LYS A 1 73 ? 27.937 35.011 60.794 1.00 21.07 ? 71 LYS A O 1 ATOM 601 C CB . LYS A 1 73 ? 26.613 35.167 63.708 1.00 20.07 ? 71 LYS A CB 1 ATOM 602 C CG . LYS A 1 73 ? 25.626 35.833 64.632 1.00 24.72 ? 71 LYS A CG 1 ATOM 603 C CD . LYS A 1 73 ? 26.358 36.460 65.777 1.00 29.24 ? 71 LYS A CD 1 ATOM 604 C CE . LYS A 1 73 ? 26.270 35.637 66.988 1.00 33.35 ? 71 LYS A CE 1 ATOM 605 N NZ . LYS A 1 73 ? 24.946 35.850 67.652 1.00 35.36 ? 71 LYS A NZ 1 ATOM 606 N N . TYR A 1 74 ? 27.287 32.987 61.571 1.00 14.84 ? 72 TYR A N 1 ATOM 607 C CA . TYR A 1 74 ? 28.520 32.309 61.139 1.00 14.99 ? 72 TYR A CA 1 ATOM 608 C C . TYR A 1 74 ? 28.328 31.309 59.992 1.00 15.55 ? 72 TYR A C 1 ATOM 609 O O . TYR A 1 74 ? 29.287 30.985 59.339 1.00 17.52 ? 72 TYR A O 1 ATOM 610 C CB . TYR A 1 74 ? 29.127 31.530 62.310 1.00 13.65 ? 72 TYR A CB 1 ATOM 611 C CG . TYR A 1 74 ? 29.436 32.415 63.478 1.00 16.73 ? 72 TYR A CG 1 ATOM 612 C CD1 . TYR A 1 74 ? 30.247 33.528 63.327 1.00 22.38 ? 72 TYR A CD1 1 ATOM 613 C CD2 . TYR A 1 74 ? 28.894 32.159 64.750 1.00 17.46 ? 72 TYR A CD2 1 ATOM 614 C CE1 . TYR A 1 74 ? 30.525 34.377 64.396 1.00 23.94 ? 72 TYR A CE1 1 ATOM 615 C CE2 . TYR A 1 74 ? 29.184 32.999 65.828 1.00 20.29 ? 72 TYR A CE2 1 ATOM 616 C CZ . TYR A 1 74 ? 30.005 34.111 65.641 1.00 24.00 ? 72 TYR A CZ 1 ATOM 617 O OH . TYR A 1 74 ? 30.297 34.980 66.718 1.00 25.02 ? 72 TYR A OH 1 ATOM 618 N N . TYR A 1 75 ? 27.104 30.833 59.750 1.00 13.68 ? 73 TYR A N 1 ATOM 619 C CA . TYR A 1 75 ? 26.913 29.721 58.819 1.00 14.68 ? 73 TYR A CA 1 ATOM 620 C C . TYR A 1 75 ? 27.531 29.993 57.421 1.00 16.97 ? 73 TYR A C 1 ATOM 621 O O . TYR A 1 75 ? 28.236 29.140 56.841 1.00 18.55 ? 73 TYR A O 1 ATOM 622 C CB . TYR A 1 75 ? 25.418 29.404 58.684 1.00 15.20 ? 73 TYR A CB 1 ATOM 623 C CG . TYR A 1 75 ? 25.066 28.329 57.632 1.00 16.16 ? 73 TYR A CG 1 ATOM 624 C CD1 . TYR A 1 75 ? 25.258 26.978 57.882 1.00 13.99 ? 73 TYR A CD1 1 ATOM 625 C CD2 . TYR A 1 75 ? 24.524 28.680 56.412 1.00 16.27 ? 73 TYR A CD2 1 ATOM 626 C CE1 . TYR A 1 75 ? 24.957 26.005 56.957 1.00 15.26 ? 73 TYR A CE1 1 ATOM 627 C CE2 . TYR A 1 75 ? 24.207 27.702 55.456 1.00 17.06 ? 73 TYR A CE2 1 ATOM 628 C CZ . TYR A 1 75 ? 24.405 26.366 55.736 1.00 15.35 ? 73 TYR A CZ 1 ATOM 629 O OH . TYR A 1 75 ? 24.072 25.402 54.797 1.00 16.05 ? 73 TYR A OH 1 ATOM 630 N N . GLN A 1 76 ? 27.295 31.173 56.874 1.00 19.64 ? 74 GLN A N 1 ATOM 631 C CA . GLN A 1 76 ? 27.803 31.434 55.503 1.00 24.09 ? 74 GLN A CA 1 ATOM 632 C C . GLN A 1 76 ? 29.326 31.361 55.377 1.00 24.49 ? 74 GLN A C 1 ATOM 633 O O . GLN A 1 76 ? 29.833 31.140 54.273 1.00 27.63 ? 74 GLN A O 1 ATOM 634 C CB . GLN A 1 76 ? 27.320 32.786 54.970 1.00 29.33 ? 74 GLN A CB 1 ATOM 635 C CG . GLN A 1 76 ? 25.934 33.150 55.430 1.00 37.77 ? 74 GLN A CG 1 ATOM 636 C CD . GLN A 1 76 ? 24.865 32.934 54.385 1.00 43.69 ? 74 GLN A CD 1 ATOM 637 O OE1 . GLN A 1 76 ? 25.076 32.243 53.387 1.00 47.06 ? 74 GLN A OE1 1 ATOM 638 N NE2 . GLN A 1 76 ? 23.696 33.541 54.608 1.00 44.27 ? 74 GLN A NE2 1 ATOM 639 N N . GLU A 1 77 ? 30.055 31.585 56.473 1.00 22.82 ? 75 GLU A N 1 ATOM 640 C CA . GLU A 1 77 ? 31.530 31.557 56.447 1.00 24.18 ? 75 GLU A CA 1 ATOM 641 C C . GLU A 1 77 ? 32.146 30.254 56.951 1.00 21.47 ? 75 GLU A C 1 ATOM 642 O O . GLU A 1 77 ? 33.371 30.102 56.925 1.00 23.21 ? 75 GLU A O 1 ATOM 643 C CB . GLU A 1 77 ? 32.112 32.729 57.234 1.00 29.23 ? 75 GLU A CB 1 ATOM 644 C CG . GLU A 1 77 ? 31.986 34.041 56.489 0.0000 31.98 ? 75 GLU A CG 1 ATOM 645 C CD . GLU A 1 77 ? 31.936 35.226 57.414 0.0000 34.29 ? 75 GLU A CD 1 ATOM 646 O OE1 . GLU A 1 77 ? 31.032 35.259 58.275 0.0000 35.09 ? 75 GLU A OE1 1 ATOM 647 O OE2 . GLU A 1 77 ? 32.800 36.119 57.282 0.0000 35.09 ? 75 GLU A OE2 1 ATOM 648 N N . GLU A 1 78 ? 31.313 29.302 57.379 1.00 16.29 ? 76 GLU A N 1 ATOM 649 C CA . GLU A 1 78 ? 31.844 27.992 57.838 1.00 13.58 ? 76 GLU A CA 1 ATOM 650 C C . GLU A 1 78 ? 32.240 27.125 56.664 1.00 14.00 ? 76 GLU A C 1 ATOM 651 O O . GLU A 1 78 ? 31.458 26.910 55.763 1.00 15.06 ? 76 GLU A O 1 ATOM 652 C CB . GLU A 1 78 ? 30.790 27.235 58.638 1.00 12.71 ? 76 GLU A CB 1 ATOM 653 C CG . GLU A 1 78 ? 30.420 27.966 59.968 1.00 12.95 ? 76 GLU A CG 1 ATOM 654 C CD . GLU A 1 78 ? 31.497 27.784 61.042 1.00 15.58 ? 76 GLU A CD 1 ATOM 655 O OE1 . GLU A 1 78 ? 32.258 26.790 60.990 1.00 18.16 ? 76 GLU A OE1 1 ATOM 656 O OE2 . GLU A 1 78 ? 31.570 28.636 61.930 1.00 17.70 ? 76 GLU A OE2 1 ATOM 657 N N . PRO A 1 79 ? 33.472 26.601 56.664 1.00 16.31 ? 77 PRO A N 1 ATOM 658 C CA . PRO A 1 79 ? 33.847 25.705 55.564 1.00 16.92 ? 77 PRO A CA 1 ATOM 659 C C . PRO A 1 79 ? 32.927 24.486 55.450 1.00 16.19 ? 77 PRO A C 1 ATOM 660 O O . PRO A 1 79 ? 32.656 24.021 54.356 1.00 16.13 ? 77 PRO A O 1 ATOM 661 C CB . PRO A 1 79 ? 35.309 25.321 55.912 1.00 19.84 ? 77 PRO A CB 1 ATOM 662 C CG . PRO A 1 79 ? 35.777 26.517 56.702 1.00 20.96 ? 77 PRO A CG 1 ATOM 663 C CD . PRO A 1 79 ? 34.587 26.898 57.559 1.00 18.23 ? 77 PRO A CD 1 ATOM 664 N N . GLU A 1 80 ? 32.427 23.958 56.549 1.00 16.46 ? 78 GLU A N 1 ATOM 665 C CA . GLU A 1 80 ? 31.527 22.796 56.454 1.00 16.65 ? 78 GLU A CA 1 ATOM 666 C C . GLU A 1 80 ? 30.174 23.188 55.918 1.00 17.46 ? 78 GLU A C 1 ATOM 667 O O . GLU A 1 80 ? 29.429 22.309 55.430 1.00 17.72 ? 78 GLU A O 1 ATOM 668 C CB . GLU A 1 80 ? 31.321 22.112 57.818 1.00 17.57 ? 78 GLU A CB 1 ATOM 669 C CG . GLU A 1 80 ? 32.312 21.077 58.055 1.00 17.88 ? 78 GLU A CG 1 ATOM 670 C CD . GLU A 1 80 ? 32.094 20.351 59.366 1.00 16.54 ? 78 GLU A CD 1 ATOM 671 O OE1 . GLU A 1 80 ? 31.122 19.581 59.499 1.00 15.84 ? 78 GLU A OE1 1 ATOM 672 O OE2 . GLU A 1 80 ? 32.904 20.529 60.270 1.00 18.57 ? 78 GLU A OE2 1 ATOM 673 N N . ALA A 1 81 ? 29.824 24.473 55.995 1.00 17.01 ? 79 ALA A N 1 ATOM 674 C CA . ALA A 1 81 ? 28.531 24.886 55.370 1.00 18.21 ? 79 ALA A CA 1 ATOM 675 C C . ALA A 1 81 ? 28.473 24.474 53.911 1.00 19.14 ? 79 ALA A C 1 ATOM 676 O O . ALA A 1 81 ? 27.422 24.101 53.395 1.00 19.03 ? 79 ALA A O 1 ATOM 677 C CB . ALA A 1 81 ? 28.253 26.377 55.507 1.00 20.08 ? 79 ALA A CB 1 ATOM 678 N N . ARG A 1 82 ? 29.612 24.541 53.242 1.00 18.86 ? 80 ARG A N 1 ATOM 679 C CA . ARG A 1 82 ? 29.649 24.207 51.817 1.00 22.48 ? 80 ARG A CA 1 ATOM 680 C C . ARG A 1 82 ? 29.285 22.755 51.550 1.00 21.62 ? 80 ARG A C 1 ATOM 681 O O . ARG A 1 82 ? 28.733 22.425 50.489 1.00 25.43 ? 80 ARG A O 1 ATOM 682 C CB . ARG A 1 82 ? 31.025 24.540 51.241 1.00 26.52 ? 80 ARG A CB 1 ATOM 683 C CG . ARG A 1 82 ? 31.279 26.049 51.298 1.00 33.17 ? 80 ARG A CG 1 ATOM 684 C CD . ARG A 1 82 ? 32.445 26.476 50.472 1.00 39.24 ? 80 ARG A CD 1 ATOM 685 N NE . ARG A 1 82 ? 33.707 25.948 51.010 1.00 41.99 ? 80 ARG A NE 1 ATOM 686 C CZ . ARG A 1 82 ? 34.606 25.226 50.327 1.00 40.59 ? 80 ARG A CZ 1 ATOM 687 N NH1 . ARG A 1 82 ? 34.428 24.901 49.007 1.00 37.83 ? 80 ARG A NH1 1 ATOM 688 N NH2 . ARG A 1 82 ? 35.703 24.831 50.996 1.00 39.47 ? 80 ARG A NH2 1 ATOM 689 N N . LEU A 1 83 ? 29.568 21.884 52.508 1.00 17.19 ? 81 LEU A N 1 ATOM 690 C CA . LEU A 1 83 ? 29.257 20.461 52.380 1.00 16.84 ? 81 LEU A CA 1 ATOM 691 C C . LEU A 1 83 ? 27.759 20.201 52.555 1.00 18.56 ? 81 LEU A C 1 ATOM 692 O O . LEU A 1 83 ? 27.233 19.266 51.972 1.00 21.72 ? 81 LEU A O 1 ATOM 693 C CB . LEU A 1 83 ? 30.022 19.629 53.432 1.00 15.71 ? 81 LEU A CB 1 ATOM 694 C CG . LEU A 1 83 ? 31.526 19.795 53.404 1.00 14.07 ? 81 LEU A CG 1 ATOM 695 C CD1 . LEU A 1 83 ? 32.175 18.946 54.504 1.00 13.15 ? 81 LEU A CD1 1 ATOM 696 C CD2 . LEU A 1 83 ? 32.157 19.420 52.030 1.00 14.45 ? 81 LEU A CD2 1 ATOM 697 N N . VAL A 1 84 ? 27.094 21.017 53.363 1.00 19.82 ? 82 VAL A N 1 ATOM 698 C CA . VAL A 1 84 ? 25.660 20.876 53.625 1.00 19.87 ? 82 VAL A CA 1 ATOM 699 C C . VAL A 1 84 ? 24.896 21.287 52.365 1.00 21.79 ? 82 VAL A C 1 ATOM 700 O O . VAL A 1 84 ? 23.962 20.611 51.917 1.00 22.03 ? 82 VAL A O 1 ATOM 701 C CB . VAL A 1 84 ? 25.243 21.745 54.865 1.00 18.35 ? 82 VAL A CB 1 ATOM 702 C CG1 . VAL A 1 84 ? 23.704 21.874 55.001 1.00 19.14 ? 82 VAL A CG1 1 ATOM 703 C CG2 . VAL A 1 84 ? 25.822 21.128 56.128 1.00 18.67 ? 82 VAL A CG2 1 ATOM 704 N N . GLY A 1 85 ? 25.297 22.413 51.806 1.00 21.51 ? 83 GLY A N 1 ATOM 705 C CA . GLY A 1 85 ? 24.796 22.800 50.506 1.00 24.70 ? 83 GLY A CA 1 ATOM 706 C C . GLY A 1 85 ? 23.429 23.484 50.523 1.00 24.67 ? 83 GLY A C 1 ATOM 707 O O . GLY A 1 85 ? 22.768 23.597 49.491 1.00 29.78 ? 83 GLY A O 1 ATOM 708 N N . LEU A 1 86 ? 23.002 23.948 51.685 1.00 19.90 ? 84 LEU A N 1 ATOM 709 C CA . LEU A 1 86 ? 21.701 24.595 51.815 1.00 18.84 ? 84 LEU A CA 1 ATOM 710 C C . LEU A 1 86 ? 21.864 26.101 52.070 1.00 16.83 ? 84 LEU A C 1 ATOM 711 O O . LEU A 1 86 ? 22.883 26.554 52.622 1.00 18.90 ? 84 LEU A O 1 ATOM 712 C CB . LEU A 1 86 ? 20.922 23.978 53.000 1.00 20.20 ? 84 LEU A CB 1 ATOM 713 C CG . LEU A 1 86 ? 20.650 22.472 52.946 1.00 20.21 ? 84 LEU A CG 1 ATOM 714 C CD1 . LEU A 1 86 ? 20.081 21.914 54.287 1.00 19.41 ? 84 LEU A CD1 1 ATOM 715 C CD2 . LEU A 1 86 ? 19.720 22.129 51.731 1.00 23.83 ? 84 LEU A CD2 1 ATOM 716 N N . SER A 1 87 ? 20.852 26.878 51.690 1.00 18.18 ? 85 SER A N 1 ATOM 717 C CA . SER A 1 87 ? 20.786 28.281 52.081 1.00 18.38 ? 85 SER A CA 1 ATOM 718 C C . SER A 1 87 ? 20.657 28.324 53.604 1.00 18.13 ? 85 SER A C 1 ATOM 719 O O . SER A 1 87 ? 20.259 27.314 54.231 1.00 18.54 ? 85 SER A O 1 ATOM 720 C CB . SER A 1 87 ? 19.552 28.927 51.486 1.00 21.42 ? 85 SER A CB 1 ATOM 721 O OG . SER A 1 87 ? 18.376 28.348 52.030 1.00 22.15 ? 85 SER A OG 1 ATOM 722 N N . LEU A 1 88 ? 20.965 29.475 54.200 1.00 17.26 ? 86 LEU A N 1 ATOM 723 C CA . LEU A 1 88 ? 20.821 29.621 55.643 1.00 17.53 ? 86 LEU A CA 1 ATOM 724 C C . LEU A 1 88 ? 19.399 29.258 56.081 1.00 17.85 ? 86 LEU A C 1 ATOM 725 O O . LEU A 1 88 ? 19.216 28.536 57.060 1.00 19.05 ? 86 LEU A O 1 ATOM 726 C CB . LEU A 1 88 ? 21.165 31.047 56.078 1.00 17.77 ? 86 LEU A CB 1 ATOM 727 C CG . LEU A 1 88 ? 20.803 31.375 57.549 1.00 18.68 ? 86 LEU A CG 1 ATOM 728 C CD1 . LEU A 1 88 ? 21.647 30.531 58.571 1.00 16.17 ? 86 LEU A CD1 1 ATOM 729 C CD2 . LEU A 1 88 ? 20.948 32.888 57.856 1.00 20.84 ? 86 LEU A CD2 1 ATOM 730 N N . GLU A 1 89 ? 18.387 29.702 55.344 1.00 18.33 ? 87 GLU A N 1 ATOM 731 C CA . GLU A 1 89 ? 16.992 29.497 55.787 1.00 19.79 ? 87 GLU A CA 1 ATOM 732 C C . GLU A 1 89 ? 16.612 28.020 55.731 1.00 17.86 ? 87 GLU A C 1 ATOM 733 O O . GLU A 1 89 ? 15.926 27.507 56.625 1.00 18.35 ? 87 GLU A O 1 ATOM 734 C CB . GLU A 1 89 ? 16.022 30.365 54.950 1.00 23.93 ? 87 GLU A CB 1 ATOM 735 C CG . GLU A 1 89 ? 16.177 31.853 55.230 0.0000 27.33 ? 87 GLU A CG 1 ATOM 736 C CD . GLU A 1 89 ? 16.232 32.160 56.717 0.0000 30.12 ? 87 GLU A CD 1 ATOM 737 O OE1 . GLU A 1 89 ? 15.353 31.673 57.460 0.0000 31.08 ? 87 GLU A OE1 1 ATOM 738 O OE2 . GLU A 1 89 ? 17.159 32.880 57.147 0.0000 31.08 ? 87 GLU A OE2 1 ATOM 739 N N . ASP A 1 90 ? 17.030 27.342 54.660 1.00 17.59 ? 88 ASP A N 1 ATOM 740 C CA . ASP A 1 90 ? 16.796 25.907 54.529 1.00 18.64 ? 88 ASP A CA 1 ATOM 741 C C . ASP A 1 90 ? 17.612 25.078 55.541 1.00 17.40 ? 88 ASP A C 1 ATOM 742 O O . ASP A 1 90 ? 17.120 24.072 56.074 1.00 17.40 ? 88 ASP A O 1 ATOM 743 C CB . ASP A 1 90 ? 17.097 25.455 53.092 1.00 20.65 ? 88 ASP A CB 1 ATOM 744 C CG . ASP A 1 90 ? 15.962 25.772 52.141 1.00 25.83 ? 88 ASP A CG 1 ATOM 745 O OD1 . ASP A 1 90 ? 14.811 25.836 52.617 1.00 28.22 ? 88 ASP A OD1 1 ATOM 746 O OD2 . ASP A 1 90 ? 16.237 25.940 50.933 1.00 27.20 ? 88 ASP A OD2 1 ATOM 747 N N . TYR A 1 91 ? 18.832 25.513 55.815 1.00 15.54 ? 89 TYR A N 1 ATOM 748 C CA . TYR A 1 91 ? 19.656 24.900 56.849 1.00 13.76 ? 89 TYR A CA 1 ATOM 749 C C . TYR A 1 91 ? 18.958 24.988 58.201 1.00 13.28 ? 89 TYR A C 1 ATOM 750 O O . TYR A 1 91 ? 18.920 23.996 58.955 1.00 14.92 ? 89 TYR A O 1 ATOM 751 C CB . TYR A 1 91 ? 21.046 25.548 56.901 1.00 14.68 ? 89 TYR A CB 1 ATOM 752 C CG . TYR A 1 91 ? 21.768 25.202 58.191 1.00 12.98 ? 89 TYR A CG 1 ATOM 753 C CD1 . TYR A 1 91 ? 22.445 24.005 58.318 1.00 14.49 ? 89 TYR A CD1 1 ATOM 754 C CD2 . TYR A 1 91 ? 21.698 26.038 59.315 1.00 13.07 ? 89 TYR A CD2 1 ATOM 755 C CE1 . TYR A 1 91 ? 23.059 23.666 59.500 1.00 15.24 ? 89 TYR A CE1 1 ATOM 756 C CE2 . TYR A 1 91 ? 22.328 25.695 60.487 1.00 13.46 ? 89 TYR A CE2 1 ATOM 757 C CZ . TYR A 1 91 ? 22.991 24.525 60.574 1.00 12.68 ? 89 TYR A CZ 1 ATOM 758 O OH . TYR A 1 91 ? 23.586 24.182 61.769 1.00 13.34 ? 89 TYR A OH 1 ATOM 759 N N . LEU A 1 92 ? 18.432 26.166 58.521 1.00 14.99 ? 90 LEU A N 1 ATOM 760 C CA . LEU A 1 92 ? 17.816 26.368 59.842 1.00 15.82 ? 90 LEU A CA 1 ATOM 761 C C . LEU A 1 92 ? 16.562 25.509 60.001 1.00 17.78 ? 90 LEU A C 1 ATOM 762 O O . LEU A 1 92 ? 16.326 24.939 61.064 1.00 17.06 ? 90 LEU A O 1 ATOM 763 C CB . LEU A 1 92 ? 17.461 27.838 60.071 1.00 16.07 ? 90 LEU A CB 1 ATOM 764 C CG . LEU A 1 92 ? 18.632 28.785 60.274 1.00 16.22 ? 90 LEU A CG 1 ATOM 765 C CD1 . LEU A 1 92 ? 18.082 30.187 60.427 1.00 15.78 ? 90 LEU A CD1 1 ATOM 766 C CD2 . LEU A 1 92 ? 19.436 28.401 61.571 1.00 15.56 ? 90 LEU A CD2 1 ATOM 767 N N . LYS A 1 93 ? 15.751 25.425 58.944 1.00 16.74 ? 91 LYS A N 1 ATOM 768 C CA . LYS A 1 93 ? 14.541 24.574 58.976 1.00 16.12 ? 91 LYS A CA 1 ATOM 769 C C . LYS A 1 93 ? 14.914 23.120 59.229 1.00 16.39 ? 91 LYS A C 1 ATOM 770 O O . LYS A 1 93 ? 14.288 22.452 60.041 1.00 17.91 ? 91 LYS A O 1 ATOM 771 C CB . LYS A 1 93 ? 13.707 24.687 57.668 1.00 18.57 ? 91 LYS A CB 1 ATOM 772 C CG . LYS A 1 93 ? 13.081 26.057 57.461 0.0000 20.52 ? 91 LYS A CG 1 ATOM 773 C CD . LYS A 1 93 ? 12.081 26.041 56.318 0.0000 22.35 ? 91 LYS A CD 1 ATOM 774 C CE . LYS A 1 93 ? 11.244 27.311 56.298 0.0000 23.75 ? 91 LYS A CE 1 ATOM 775 N NZ . LYS A 1 93 ? 12.067 28.527 56.049 0.0000 24.47 ? 91 LYS A NZ 1 ATOM 776 N N . ARG A 1 94 ? 15.966 22.649 58.564 1.00 14.83 ? 92 ARG A N 1 ATOM 777 C CA . ARG A 1 94 ? 16.429 21.279 58.758 1.00 15.81 ? 92 ARG A CA 1 ATOM 778 C C . ARG A 1 94 ? 17.039 21.116 60.157 1.00 15.19 ? 92 ARG A C 1 ATOM 779 O O . ARG A 1 94 ? 16.646 20.207 60.921 1.00 17.04 ? 92 ARG A O 1 ATOM 780 C CB . ARG A 1 94 ? 17.478 20.926 57.691 1.00 16.83 ? 92 ARG A CB 1 ATOM 781 C CG . ARG A 1 94 ? 17.958 19.518 57.836 1.00 22.96 ? 92 ARG A CG 1 ATOM 782 C CD . ARG A 1 94 ? 18.916 19.120 56.724 1.00 27.88 ? 92 ARG A CD 1 ATOM 783 N NE . ARG A 1 94 ? 18.208 19.063 55.437 1.00 31.24 ? 92 ARG A NE 1 ATOM 784 C CZ . ARG A 1 94 ? 18.732 18.602 54.298 1.00 35.59 ? 92 ARG A CZ 1 ATOM 785 N NH1 . ARG A 1 94 ? 19.985 18.169 54.257 1.00 36.38 ? 92 ARG A NH1 1 ATOM 786 N NH2 . ARG A 1 94 ? 18.007 18.591 53.187 1.00 36.19 ? 92 ARG A NH2 1 ATOM 787 N N . MET A 1 95 ? 18.006 21.979 60.502 1.00 14.15 ? 93 MET A N 1 ATOM 788 C CA . MET A 1 95 ? 18.694 21.851 61.783 1.00 12.83 ? 93 MET A CA 1 ATOM 789 C C . MET A 1 95 ? 17.753 21.842 62.990 1.00 12.21 ? 93 MET A C 1 ATOM 790 O O . MET A 1 95 ? 17.944 21.056 63.931 1.00 12.38 ? 93 MET A O 1 ATOM 791 C CB . MET A 1 95 ? 19.717 23.000 61.918 1.00 12.68 ? 93 MET A CB 1 ATOM 792 C CG . MET A 1 95 ? 20.560 23.004 63.225 1.00 13.98 ? 93 MET A CG 1 ATOM 793 S SD . MET A 1 95 ? 19.771 23.750 64.648 1.00 14.13 ? 93 MET A SD 1 ATOM 794 C CE . MET A 1 95 ? 19.858 25.455 64.207 1.00 13.40 ? 93 MET A CE 1 ATOM 795 N N . LEU A 1 96 ? 16.742 22.705 62.964 1.00 12.55 ? 94 LEU A N 1 ATOM 796 C CA . LEU A 1 96 ? 15.797 22.827 64.088 1.00 12.68 ? 94 LEU A CA 1 ATOM 797 C C . LEU A 1 96 ? 14.749 21.743 64.160 1.00 14.33 ? 94 LEU A C 1 ATOM 798 O O . LEU A 1 96 ? 13.961 21.720 65.087 1.00 17.58 ? 94 LEU A O 1 ATOM 799 C CB . LEU A 1 96 ? 15.110 24.198 64.072 1.00 15.19 ? 94 LEU A CB 1 ATOM 800 C CG . LEU A 1 96 ? 16.017 25.380 64.420 1.00 18.76 ? 94 LEU A CG 1 ATOM 801 C CD1 . LEU A 1 96 ? 15.348 26.697 64.006 1.00 19.23 ? 94 LEU A CD1 1 ATOM 802 C CD2 . LEU A 1 96 ? 16.376 25.412 65.914 1.00 20.39 ? 94 LEU A CD2 1 ATOM 803 N N . SER A 1 97 ? 14.703 20.862 63.177 1.00 13.73 ? 95 SER A N 1 ATOM 804 C CA . SER A 1 97 ? 13.749 19.753 63.191 1.00 13.73 ? 95 SER A CA 1 ATOM 805 C C . SER A 1 97 ? 14.112 18.756 64.279 1.00 13.99 ? 95 SER A C 1 ATOM 806 O O . SER A 1 97 ? 15.309 18.504 64.539 1.00 13.80 ? 95 SER A O 1 ATOM 807 C CB . SER A 1 97 ? 13.755 19.050 61.820 1.00 17.09 ? 95 SER A CB 1 ATOM 808 O OG . SER A 1 97 ? 13.246 19.895 60.814 1.00 21.36 ? 95 SER A OG 1 ATOM 809 N N . ASP A 1 98 ? 13.095 18.190 64.929 1.00 15.34 ? 96 ASP A N 1 ATOM 810 C CA . ASP A 1 98 ? 13.343 17.189 65.967 1.00 15.42 ? 96 ASP A CA 1 ATOM 811 C C . ASP A 1 98 ? 14.077 16.012 65.340 1.00 14.95 ? 96 ASP A C 1 ATOM 812 O O . ASP A 1 98 ? 13.754 15.607 64.210 1.00 16.67 ? 96 ASP A O 1 ATOM 813 C CB . ASP A 1 98 ? 11.995 16.718 66.569 1.00 17.25 ? 96 ASP A CB 1 ATOM 814 C CG . ASP A 1 98 ? 12.153 16.001 67.934 1.00 20.73 ? 96 ASP A CG 1 ATOM 815 O OD1 . ASP A 1 98 ? 13.261 16.005 68.503 1.00 19.91 ? 96 ASP A OD1 1 ATOM 816 O OD2 . ASP A 1 98 ? 11.125 15.487 68.453 1.00 21.68 ? 96 ASP A OD2 1 ATOM 817 N N . ASN A 1 99 ? 15.097 15.512 66.043 1.00 14.81 ? 97 ASN A N 1 ATOM 818 C CA . ASN A 1 99 ? 15.862 14.336 65.652 1.00 13.87 ? 97 ASN A CA 1 ATOM 819 C C . ASN A 1 99 ? 16.828 14.533 64.497 1.00 14.65 ? 97 ASN A C 1 ATOM 820 O O . ASN A 1 99 ? 17.406 13.557 64.023 1.00 15.44 ? 97 ASN A O 1 ATOM 821 C CB . ASN A 1 99 ? 14.980 13.117 65.400 1.00 15.37 ? 97 ASN A CB 1 ATOM 822 C CG . ASN A 1 99 ? 14.084 12.813 66.594 1.00 18.98 ? 97 ASN A CG 1 ATOM 823 O OD1 . ASN A 1 99 ? 14.565 12.768 67.716 1.00 21.40 ? 97 ASN A OD1 1 ATOM 824 N ND2 . ASN A 1 99 ? 12.802 12.641 66.365 1.00 22.06 ? 97 ASN A ND2 1 ATOM 825 N N . GLU A 1 100 ? 17.031 15.780 64.059 1.00 14.30 ? 98 GLU A N 1 ATOM 826 C CA . GLU A 1 100 ? 18.002 16.008 62.995 1.00 14.42 ? 98 GLU A CA 1 ATOM 827 C C . GLU A 1 100 ? 19.397 16.018 63.594 1.00 12.44 ? 98 GLU A C 1 ATOM 828 O O . GLU A 1 100 ? 19.690 16.827 64.498 1.00 14.41 ? 98 GLU A O 1 ATOM 829 C CB . GLU A 1 100 ? 17.742 17.355 62.324 1.00 17.90 ? 98 GLU A CB 1 ATOM 830 C CG . GLU A 1 100 ? 18.648 17.720 61.169 1.00 19.60 ? 98 GLU A CG 1 ATOM 831 C CD . GLU A 1 100 ? 18.516 16.776 59.989 1.00 24.98 ? 98 GLU A CD 1 ATOM 832 O OE1 . GLU A 1 100 ? 17.439 16.180 59.788 1.00 26.22 ? 98 GLU A OE1 1 ATOM 833 O OE2 . GLU A 1 100 ? 19.497 16.630 59.266 1.00 27.14 ? 98 GLU A OE2 1 ATOM 834 N N . TRP A 1 101 ? 20.276 15.177 63.064 1.00 11.63 ? 99 TRP A N 1 ATOM 835 C CA . TRP A 1 101 ? 21.597 14.951 63.687 1.00 10.59 ? 99 TRP A CA 1 ATOM 836 C C . TRP A 1 101 ? 22.434 16.232 63.680 1.00 12.41 ? 99 TRP A C 1 ATOM 837 O O . TRP A 1 101 ? 22.530 16.952 62.630 1.00 14.36 ? 99 TRP A O 1 ATOM 838 C CB . TRP A 1 101 ? 22.366 13.882 62.930 1.00 11.46 ? 99 TRP A CB 1 ATOM 839 C CG . TRP A 1 101 ? 21.818 12.487 63.072 1.00 12.85 ? 99 TRP A CG 1 ATOM 840 C CD1 . TRP A 1 101 ? 20.676 12.111 63.720 1.00 13.68 ? 99 TRP A CD1 1 ATOM 841 C CD2 . TRP A 1 101 ? 22.394 11.293 62.554 1.00 16.99 ? 99 TRP A CD2 1 ATOM 842 N NE1 . TRP A 1 101 ? 20.495 10.763 63.637 1.00 16.10 ? 99 TRP A NE1 1 ATOM 843 C CE2 . TRP A 1 101 ? 21.544 10.221 62.932 1.00 18.33 ? 99 TRP A CE2 1 ATOM 844 C CE3 . TRP A 1 101 ? 23.573 11.016 61.846 1.00 21.19 ? 99 TRP A CE3 1 ATOM 845 C CZ2 . TRP A 1 101 ? 21.813 8.879 62.569 1.00 21.22 ? 99 TRP A CZ2 1 ATOM 846 C CZ3 . TRP A 1 101 ? 23.839 9.705 61.485 1.00 23.44 ? 99 TRP A CZ3 1 ATOM 847 C CH2 . TRP A 1 101 ? 22.957 8.646 61.847 1.00 24.26 ? 99 TRP A CH2 1 ATOM 848 N N . GLY A 1 102 ? 23.077 16.515 64.822 1.00 11.05 ? 100 GLY A N 1 ATOM 849 C CA . GLY A 1 102 ? 24.071 17.576 64.905 1.00 10.75 ? 100 GLY A CA 1 ATOM 850 C C . GLY A 1 102 ? 25.404 17.035 64.450 1.00 10.79 ? 100 GLY A C 1 ATOM 851 O O . GLY A 1 102 ? 25.535 15.839 64.120 1.00 10.84 ? 100 GLY A O 1 ATOM 852 N N . SER A 1 103 ? 26.388 17.906 64.413 1.00 9.25 ? 101 SER A N 1 ATOM 853 C CA . SER A 1 103 ? 27.631 17.592 63.740 1.00 10.17 ? 101 SER A CA 1 ATOM 854 C C . SER A 1 103 ? 28.733 18.557 64.118 1.00 9.52 ? 101 SER A C 1 ATOM 855 O O . SER A 1 103 ? 28.524 19.545 64.836 1.00 10.30 ? 101 SER A O 1 ATOM 856 C CB . SER A 1 103 ? 27.456 17.677 62.218 1.00 10.83 ? 101 SER A CB 1 ATOM 857 O OG . SER A 1 103 ? 27.367 19.042 61.766 1.00 10.27 ? 101 SER A OG 1 ATOM 858 N N . THR A 1 104 ? 29.914 18.286 63.575 1.00 11.23 ? 102 THR A N 1 ATOM 859 C CA . THR A 1 104 ? 31.050 19.194 63.667 1.00 10.04 ? 102 THR A CA 1 ATOM 860 C C . THR A 1 104 ? 30.749 20.628 63.218 1.00 9.67 ? 102 THR A C 1 ATOM 861 O O . THR A 1 104 ? 31.361 21.560 63.698 1.00 9.47 ? 102 THR A O 1 ATOM 862 C CB . THR A 1 104 ? 32.227 18.617 62.809 1.00 10.04 ? 102 THR A CB 1 ATOM 863 O OG1 . THR A 1 104 ? 31.675 18.024 61.604 1.00 10.45 ? 102 THR A OG1 1 ATOM 864 C CG2 . THR A 1 104 ? 32.929 17.543 63.599 1.00 12.63 ? 102 THR A CG2 1 ATOM 865 N N . LEU A 1 105 ? 29.795 20.817 62.308 1.00 9.44 ? 103 LEU A N 1 ATOM 866 C CA . LEU A 1 105 ? 29.459 22.172 61.866 1.00 8.39 ? 103 LEU A CA 1 ATOM 867 C C . LEU A 1 105 ? 28.790 22.943 63.003 1.00 9.94 ? 103 LEU A C 1 ATOM 868 O O . LEU A 1 105 ? 29.132 24.099 63.274 1.00 8.50 ? 103 LEU A O 1 ATOM 869 C CB . LEU A 1 105 ? 28.498 22.128 60.660 1.00 8.99 ? 103 LEU A CB 1 ATOM 870 C CG . LEU A 1 105 ? 27.811 23.442 60.263 1.00 11.11 ? 103 LEU A CG 1 ATOM 871 C CD1 . LEU A 1 105 ? 28.875 24.511 59.998 1.00 11.43 ? 103 LEU A CD1 1 ATOM 872 C CD2 . LEU A 1 105 ? 26.919 23.245 58.997 1.00 13.01 ? 103 LEU A CD2 1 ATOM 873 N N . GLU A 1 106 ? 27.850 22.283 63.685 1.00 11.01 ? 104 GLU A N 1 ATOM 874 C CA . GLU A 1 106 ? 27.239 22.952 64.828 1.00 9.26 ? 104 GLU A CA 1 ATOM 875 C C . GLU A 1 106 ? 28.235 23.121 65.971 1.00 8.63 ? 104 GLU A C 1 ATOM 876 O O . GLU A 1 106 ? 28.155 24.125 66.704 1.00 9.82 ? 104 GLU A O 1 ATOM 877 C CB . GLU A 1 106 ? 25.971 22.223 65.307 1.00 9.65 ? 104 GLU A CB 1 ATOM 878 C CG . GLU A 1 106 ? 24.843 22.301 64.243 1.00 11.55 ? 104 GLU A CG 1 ATOM 879 C CD . GLU A 1 106 ? 25.091 21.418 63.037 1.00 12.19 ? 104 GLU A CD 1 ATOM 880 O OE1 . GLU A 1 106 ? 25.668 20.328 63.188 1.00 12.01 ? 104 GLU A OE1 1 ATOM 881 O OE2 . GLU A 1 106 ? 24.682 21.838 61.912 1.00 12.91 ? 104 GLU A OE2 1 ATOM 882 N N . ALA A 1 107 ? 29.172 22.178 66.117 1.00 8.72 ? 105 ALA A N 1 ATOM 883 C CA . ALA A 1 107 ? 30.182 22.349 67.167 1.00 9.43 ? 105 ALA A CA 1 ATOM 884 C C . ALA A 1 107 ? 31.021 23.627 66.868 1.00 10.38 ? 105 ALA A C 1 ATOM 885 O O . ALA A 1 107 ? 31.326 24.424 67.743 1.00 9.70 ? 105 ALA A O 1 ATOM 886 C CB . ALA A 1 107 ? 31.105 21.130 67.248 1.00 10.55 ? 105 ALA A CB 1 ATOM 887 N N . SER A 1 108 ? 31.425 23.784 65.618 1.00 9.39 ? 106 SER A N 1 ATOM 888 C CA . SER A 1 108 ? 32.226 24.920 65.202 1.00 10.72 ? 106 SER A CA 1 ATOM 889 C C . SER A 1 108 ? 31.504 26.245 65.510 1.00 11.30 ? 106 SER A C 1 ATOM 890 O O . SER A 1 108 ? 32.089 27.206 66.092 1.00 11.24 ? 106 SER A O 1 ATOM 891 C CB . SER A 1 108 ? 32.496 24.840 63.681 1.00 10.84 ? 106 SER A CB 1 ATOM 892 O OG . SER A 1 108 ? 33.311 25.942 63.346 1.00 10.80 ? 106 SER A OG 1 ATOM 893 N N . MET A 1 109 ? 30.221 26.278 65.162 1.00 11.75 ? 107 MET A N 1 ATOM 894 C CA . MET A 1 109 ? 29.422 27.501 65.352 1.00 10.31 ? 107 MET A CA 1 ATOM 895 C C . MET A 1 109 ? 29.113 27.785 66.847 1.00 10.72 ? 107 MET A C 1 ATOM 896 O O . MET A 1 109 ? 29.121 28.943 67.285 1.00 11.68 ? 107 MET A O 1 ATOM 897 C CB . MET A 1 109 ? 28.130 27.471 64.513 1.00 12.23 ? 107 MET A CB 1 ATOM 898 C CG . MET A 1 109 ? 28.500 27.363 63.017 1.00 11.99 ? 107 MET A CG 1 ATOM 899 S SD . MET A 1 109 ? 27.020 27.687 61.986 1.00 12.58 ? 107 MET A SD 1 ATOM 900 C CE . MET A 1 109 ? 25.989 26.247 62.400 1.00 12.86 ? 107 MET A CE 1 ATOM 901 N N . LEU A 1 110 ? 28.851 26.715 67.602 1.00 12.01 ? 108 LEU A N 1 ATOM 902 C CA . LEU A 1 110 ? 28.534 26.874 69.013 1.00 10.85 ? 108 LEU A CA 1 ATOM 903 C C . LEU A 1 110 ? 29.748 27.309 69.824 1.00 11.46 ? 108 LEU A C 1 ATOM 904 O O . LEU A 1 110 ? 29.615 28.066 70.797 1.00 13.49 ? 108 LEU A O 1 ATOM 905 C CB . LEU A 1 110 ? 27.984 25.582 69.604 1.00 11.14 ? 108 LEU A CB 1 ATOM 906 C CG . LEU A 1 110 ? 26.498 25.295 69.289 1.00 9.96 ? 108 LEU A CG 1 ATOM 907 C CD1 . LEU A 1 110 ? 26.149 23.853 69.636 1.00 11.43 ? 108 LEU A CD1 1 ATOM 908 C CD2 . LEU A 1 110 ? 25.620 26.348 70.008 1.00 12.51 ? 108 LEU A CD2 1 ATOM 909 N N . ALA A 1 111 ? 30.925 26.857 69.420 1.00 12.30 ? 109 ALA A N 1 ATOM 910 C CA . ALA A 1 111 ? 32.164 27.289 70.079 1.00 13.23 ? 109 ALA A CA 1 ATOM 911 C C . ALA A 1 111 ? 32.303 28.800 69.953 1.00 13.82 ? 109 ALA A C 1 ATOM 912 O O . ALA A 1 111 ? 32.631 29.490 70.917 1.00 14.54 ? 109 ALA A O 1 ATOM 913 C CB . ALA A 1 111 ? 33.408 26.561 69.471 1.00 12.90 ? 109 ALA A CB 1 ATOM 914 N N . LYS A 1 112 ? 31.986 29.331 68.783 1.00 12.62 ? 110 LYS A N 1 ATOM 915 C CA . LYS A 1 112 ? 32.020 30.776 68.583 1.00 13.91 ? 110 LYS A CA 1 ATOM 916 C C . LYS A 1 112 ? 30.942 31.503 69.386 1.00 14.39 ? 110 LYS A C 1 ATOM 917 O O . LYS A 1 112 ? 31.185 32.538 70.032 1.00 16.38 ? 110 LYS A O 1 ATOM 918 C CB . LYS A 1 112 ? 31.861 31.109 67.096 1.00 17.27 ? 110 LYS A CB 1 ATOM 919 C CG . LYS A 1 112 ? 33.042 30.612 66.238 1.00 19.62 ? 110 LYS A CG 1 ATOM 920 C CD . LYS A 1 112 ? 32.799 31.035 64.762 1.00 20.32 ? 110 LYS A CD 1 ATOM 921 C CE . LYS A 1 112 ? 33.828 30.430 63.843 1.00 21.97 ? 110 LYS A CE 1 ATOM 922 N NZ . LYS A 1 112 ? 33.587 28.971 63.711 1.00 21.54 ? 110 LYS A NZ 1 ATOM 923 N N . GLU A 1 113 ? 29.727 30.979 69.319 1.00 14.25 ? 111 GLU A N 1 ATOM 924 C CA . GLU A 1 113 ? 28.551 31.638 69.912 1.00 14.91 ? 111 GLU A CA 1 ATOM 925 C C . GLU A 1 113 ? 28.594 31.639 71.431 1.00 15.87 ? 111 GLU A C 1 ATOM 926 O O . GLU A 1 113 ? 28.264 32.654 72.051 1.00 18.92 ? 111 GLU A O 1 ATOM 927 C CB . GLU A 1 113 ? 27.271 30.930 69.400 1.00 13.57 ? 111 GLU A CB 1 ATOM 928 C CG . GLU A 1 113 ? 25.948 31.460 69.982 1.00 15.93 ? 111 GLU A CG 1 ATOM 929 C CD . GLU A 1 113 ? 25.546 32.794 69.425 1.00 23.03 ? 111 GLU A CD 1 ATOM 930 O OE1 . GLU A 1 113 ? 26.243 33.341 68.556 1.00 25.06 ? 111 GLU A OE1 1 ATOM 931 O OE2 . GLU A 1 113 ? 24.513 33.316 69.887 1.00 27.08 ? 111 GLU A OE2 1 ATOM 932 N N . MET A 1 114 ? 29.024 30.512 72.014 1.00 13.52 ? 112 MET A N 1 ATOM 933 C CA . MET A 1 114 ? 29.002 30.360 73.479 1.00 13.75 ? 112 MET A CA 1 ATOM 934 C C . MET A 1 114 ? 30.335 30.701 74.110 1.00 15.35 ? 112 MET A C 1 ATOM 935 O O . MET A 1 114 ? 30.418 30.850 75.324 1.00 17.37 ? 112 MET A O 1 ATOM 936 C CB . MET A 1 114 ? 28.605 28.926 73.872 1.00 13.70 ? 112 MET A CB 1 ATOM 937 C CG . MET A 1 114 ? 27.187 28.534 73.384 1.00 14.32 ? 112 MET A CG 1 ATOM 938 S SD . MET A 1 114 ? 26.810 26.788 73.753 1.00 18.31 ? 112 MET A SD 1 ATOM 939 C CE . MET A 1 114 ? 26.624 26.762 75.525 1.00 16.23 ? 112 MET A CE 1 ATOM 940 N N . GLY A 1 115 ? 31.383 30.809 73.288 1.00 13.95 ? 113 GLY A N 1 ATOM 941 C CA . GLY A 1 115 ? 32.743 31.043 73.793 1.00 12.04 ? 113 GLY A CA 1 ATOM 942 C C . GLY A 1 115 ? 33.365 29.840 74.455 1.00 13.07 ? 113 GLY A C 1 ATOM 943 O O . GLY A 1 115 ? 34.396 29.968 75.130 1.00 14.84 ? 113 GLY A O 1 ATOM 944 N N . ILE A 1 116 ? 32.777 28.673 74.250 1.00 14.73 ? 114 ILE A N 1 ATOM 945 C CA . ILE A 1 116 ? 33.292 27.428 74.821 1.00 14.09 ? 114 ILE A CA 1 ATOM 946 C C . ILE A 1 116 ? 34.268 26.766 73.840 1.00 12.40 ? 114 ILE A C 1 ATOM 947 O O . ILE A 1 116 ? 34.352 27.133 72.651 1.00 14.12 ? 114 ILE A O 1 ATOM 948 C CB . ILE A 1 116 ? 32.165 26.407 75.107 1.00 15.24 ? 114 ILE A CB 1 ATOM 949 C CG1 . ILE A 1 116 ? 31.394 26.042 73.819 1.00 15.73 ? 114 ILE A CG1 1 ATOM 950 C CG2 . ILE A 1 116 ? 31.200 26.943 76.199 1.00 16.97 ? 114 ILE A CG2 1 ATOM 951 C CD1 . ILE A 1 116 ? 30.291 24.993 74.045 1.00 17.11 ? 114 ILE A CD1 1 ATOM 952 N N . THR A 1 117 ? 34.994 25.766 74.323 1.00 9.80 ? 115 THR A N 1 ATOM 953 C CA . THR A 1 117 ? 35.820 24.919 73.473 1.00 12.16 ? 115 THR A CA 1 ATOM 954 C C . THR A 1 117 ? 35.194 23.550 73.479 1.00 10.09 ? 115 THR A C 1 ATOM 955 O O . THR A 1 117 ? 34.804 23.053 74.547 1.00 12.77 ? 115 THR A O 1 ATOM 956 C CB . THR A 1 117 ? 37.247 24.865 73.996 1.00 12.27 ? 115 THR A CB 1 ATOM 957 O OG1 . THR A 1 117 ? 37.814 26.180 73.893 1.00 15.16 ? 115 THR A OG1 1 ATOM 958 C CG2 . THR A 1 117 ? 38.116 23.854 73.200 1.00 12.00 ? 115 THR A CG2 1 ATOM 959 N N . ILE A 1 118 ? 35.029 22.941 72.286 1.00 8.19 ? 116 ILE A N 1 ATOM 960 C CA . ILE A 1 118 ? 34.427 21.630 72.179 1.00 9.90 ? 116 ILE A CA 1 ATOM 961 C C . ILE A 1 118 ? 35.433 20.703 71.540 1.00 11.28 ? 116 ILE A C 1 ATOM 962 O O . ILE A 1 118 ? 36.068 21.061 70.529 1.00 11.75 ? 116 ILE A O 1 ATOM 963 C CB . ILE A 1 118 ? 33.159 21.665 71.270 1.00 9.89 ? 116 ILE A CB 1 ATOM 964 C CG1 . ILE A 1 118 ? 32.059 22.550 71.918 1.00 9.88 ? 116 ILE A CG1 1 ATOM 965 C CG2 . ILE A 1 118 ? 32.654 20.261 70.962 1.00 8.81 ? 116 ILE A CG2 1 ATOM 966 C CD1 . ILE A 1 118 ? 30.937 22.899 70.896 1.00 9.75 ? 116 ILE A CD1 1 ATOM 967 N N . ILE A 1 119 ? 35.615 19.524 72.129 1.00 9.71 ? 117 ILE A N 1 ATOM 968 C CA . ILE A 1 119 ? 36.468 18.528 71.529 1.00 10.37 ? 117 ILE A CA 1 ATOM 969 C C . ILE A 1 119 ? 35.601 17.330 71.202 1.00 10.84 ? 117 ILE A C 1 ATOM 970 O O . ILE A 1 119 ? 34.885 16.790 72.079 1.00 10.55 ? 117 ILE A O 1 ATOM 971 C CB . ILE A 1 119 ? 37.544 18.059 72.483 1.00 7.21 ? 117 ILE A CB 1 ATOM 972 C CG1 . ILE A 1 119 ? 38.489 19.240 72.831 1.00 8.54 ? 117 ILE A CG1 1 ATOM 973 C CG2 . ILE A 1 119 ? 38.382 16.922 71.788 1.00 11.11 ? 117 ILE A CG2 1 ATOM 974 C CD1 . ILE A 1 119 ? 39.487 18.902 73.967 1.00 10.79 ? 117 ILE A CD1 1 ATOM 975 N N . ILE A 1 120 ? 35.677 16.865 69.953 1.00 9.95 ? 118 ILE A N 1 ATOM 976 C CA . ILE A 1 120 ? 34.994 15.634 69.591 1.00 10.92 ? 118 ILE A CA 1 ATOM 977 C C . ILE A 1 120 ? 36.060 14.540 69.426 1.00 10.22 ? 118 ILE A C 1 ATOM 978 O O . ILE A 1 120 ? 36.980 14.654 68.570 1.00 10.35 ? 118 ILE A O 1 ATOM 979 C CB . ILE A 1 120 ? 34.179 15.790 68.273 1.00 10.55 ? 118 ILE A CB 1 ATOM 980 C CG1 . ILE A 1 120 ? 33.104 16.890 68.445 1.00 13.15 ? 118 ILE A CG1 1 ATOM 981 C CG2 . ILE A 1 120 ? 33.606 14.421 67.850 1.00 11.23 ? 118 ILE A CG2 1 ATOM 982 C CD1 . ILE A 1 120 ? 32.337 17.203 67.173 1.00 13.41 ? 118 ILE A CD1 1 ATOM 983 N N . TRP A 1 121 ? 36.000 13.544 70.317 1.00 9.85 ? 119 TRP A N 1 ATOM 984 C CA . TRP A 1 121 ? 36.866 12.380 70.247 1.00 10.55 ? 119 TRP A CA 1 ATOM 985 C C . TRP A 1 121 ? 36.184 11.318 69.442 1.00 12.55 ? 119 TRP A C 1 ATOM 986 O O . TRP A 1 121 ? 35.074 10.880 69.764 1.00 14.95 ? 119 TRP A O 1 ATOM 987 C CB . TRP A 1 121 ? 37.143 11.862 71.660 1.00 10.65 ? 119 TRP A CB 1 ATOM 988 C CG . TRP A 1 121 ? 37.830 12.898 72.545 1.00 10.41 ? 119 TRP A CG 1 ATOM 989 C CD1 . TRP A 1 121 ? 37.258 13.689 73.510 1.00 11.71 ? 119 TRP A CD1 1 ATOM 990 C CD2 . TRP A 1 121 ? 39.231 13.188 72.568 1.00 10.20 ? 119 TRP A CD2 1 ATOM 991 N NE1 . TRP A 1 121 ? 38.232 14.466 74.123 1.00 10.92 ? 119 TRP A NE1 1 ATOM 992 C CE2 . TRP A 1 121 ? 39.440 14.206 73.533 1.00 12.16 ? 119 TRP A CE2 1 ATOM 993 C CE3 . TRP A 1 121 ? 40.316 12.753 71.785 1.00 11.77 ? 119 TRP A CE3 1 ATOM 994 C CZ2 . TRP A 1 121 ? 40.714 14.747 73.802 1.00 12.43 ? 119 TRP A CZ2 1 ATOM 995 C CZ3 . TRP A 1 121 ? 41.576 13.293 72.029 1.00 12.10 ? 119 TRP A CZ3 1 ATOM 996 C CH2 . TRP A 1 121 ? 41.767 14.304 73.022 1.00 12.92 ? 119 TRP A CH2 1 ATOM 997 N N . THR A 1 122 ? 36.873 10.829 68.429 1.00 13.65 ? 120 THR A N 1 ATOM 998 C CA . THR A 1 122 ? 36.257 9.844 67.600 1.00 17.08 ? 120 THR A CA 1 ATOM 999 C C . THR A 1 122 ? 36.978 8.505 67.817 1.00 19.96 ? 120 THR A C 1 ATOM 1000 O O . THR A 1 122 ? 38.217 8.450 67.998 1.00 20.95 ? 120 THR A O 1 ATOM 1001 C CB . THR A 1 122 ? 36.250 10.354 66.131 1.00 22.97 ? 120 THR A CB 1 ATOM 1002 O OG1 . THR A 1 122 ? 35.382 9.523 65.340 1.00 29.52 ? 120 THR A OG1 1 ATOM 1003 C CG2 . THR A 1 122 ? 37.660 10.331 65.629 1.00 22.46 ? 120 THR A CG2 1 ATOM 1004 N N . VAL A 1 123 ? 36.174 7.443 67.890 1.00 20.78 ? 121 VAL A N 1 ATOM 1005 C CA . VAL A 1 123 ? 36.665 6.092 68.128 1.00 21.37 ? 121 VAL A CA 1 ATOM 1006 C C . VAL A 1 123 ? 36.070 5.145 67.073 1.00 24.94 ? 121 VAL A C 1 ATOM 1007 O O . VAL A 1 123 ? 34.970 5.397 66.549 1.00 28.99 ? 121 VAL A O 1 ATOM 1008 C CB . VAL A 1 123 ? 36.230 5.584 69.525 1.00 19.02 ? 121 VAL A CB 1 ATOM 1009 C CG1 . VAL A 1 123 ? 36.917 6.389 70.613 1.00 17.41 ? 121 VAL A CG1 1 ATOM 1010 C CG2 . VAL A 1 123 ? 34.703 5.664 69.647 1.00 19.56 ? 121 VAL A CG2 1 ATOM 1011 N N . SER A 1 126 ? 35.752 -0.372 69.545 1.00 37.26 ? 124 SER A N 1 ATOM 1012 C CA . SER A 1 126 ? 36.496 -0.227 70.784 1.00 37.31 ? 124 SER A CA 1 ATOM 1013 C C . SER A 1 126 ? 36.266 1.190 71.321 1.00 34.89 ? 124 SER A C 1 ATOM 1014 O O . SER A 1 126 ? 35.498 1.983 70.750 1.00 34.21 ? 124 SER A O 1 ATOM 1015 C CB . SER A 1 126 ? 37.983 -0.324 70.448 1.00 41.09 ? 124 SER A CB 1 ATOM 1016 O OG . SER A 1 126 ? 38.314 0.688 69.478 1.00 40.43 ? 124 SER A OG 1 ATOM 1017 N N . ASP A 1 127 ? 36.956 1.531 72.396 1.00 30.17 ? 125 ASP A N 1 ATOM 1018 C CA . ASP A 1 127 ? 37.047 2.932 72.756 1.00 28.02 ? 125 ASP A CA 1 ATOM 1019 C C . ASP A 1 127 ? 38.472 3.465 72.518 1.00 23.99 ? 125 ASP A C 1 ATOM 1020 O O . ASP A 1 127 ? 38.913 4.404 73.179 1.00 22.85 ? 125 ASP A O 1 ATOM 1021 C CB . ASP A 1 127 ? 36.596 3.173 74.198 1.00 29.27 ? 125 ASP A CB 1 ATOM 1022 C CG . ASP A 1 127 ? 37.541 2.548 75.204 1.00 30.23 ? 125 ASP A CG 1 ATOM 1023 O OD1 . ASP A 1 127 ? 38.257 1.590 74.801 1.00 28.90 ? 125 ASP A OD1 1 ATOM 1024 O OD2 . ASP A 1 127 ? 37.566 3.015 76.369 1.00 31.60 ? 125 ASP A OD2 1 ATOM 1025 N N . GLU A 1 128 ? 39.180 2.886 71.550 1.00 21.99 ? 126 GLU A N 1 ATOM 1026 C CA . GLU A 1 128 ? 40.511 3.381 71.201 1.00 20.41 ? 126 GLU A CA 1 ATOM 1027 C C . GLU A 1 128 ? 40.378 4.645 70.375 1.00 16.43 ? 126 GLU A C 1 ATOM 1028 O O . GLU A 1 128 ? 39.719 4.664 69.326 1.00 18.78 ? 126 GLU A O 1 ATOM 1029 C CB . GLU A 1 128 ? 41.325 2.309 70.434 1.00 24.97 ? 126 GLU A CB 1 ATOM 1030 C CG . GLU A 1 128 ? 42.659 2.792 69.786 1.00 31.72 ? 126 GLU A CG 1 ATOM 1031 C CD . GLU A 1 128 ? 43.606 3.526 70.787 1.00 36.82 ? 126 GLU A CD 1 ATOM 1032 O OE1 . GLU A 1 128 ? 44.101 4.689 70.457 1.00 35.37 ? 126 GLU A OE1 1 ATOM 1033 O OE2 . GLU A 1 128 ? 43.846 2.914 71.880 1.00 38.44 ? 126 GLU A OE2 1 ATOM 1034 N N . VAL A 1 129 ? 40.984 5.723 70.861 1.00 14.77 ? 127 VAL A N 1 ATOM 1035 C CA . VAL A 1 129 ? 40.876 7.016 70.189 1.00 14.73 ? 127 VAL A CA 1 ATOM 1036 C C . VAL A 1 129 ? 41.571 6.976 68.832 1.00 16.21 ? 127 VAL A C 1 ATOM 1037 O O . VAL A 1 129 ? 42.725 6.539 68.726 1.00 17.11 ? 127 VAL A O 1 ATOM 1038 C CB . VAL A 1 129 ? 41.525 8.090 71.044 1.00 15.05 ? 127 VAL A CB 1 ATOM 1039 C CG1 . VAL A 1 129 ? 41.634 9.449 70.295 1.00 15.67 ? 127 VAL A CG1 1 ATOM 1040 C CG2 . VAL A 1 129 ? 40.741 8.221 72.323 1.00 16.59 ? 127 VAL A CG2 1 ATOM 1041 N N . GLU A 1 130 ? 40.874 7.470 67.811 1.00 16.61 ? 128 GLU A N 1 ATOM 1042 C CA . GLU A 1 130 ? 41.502 7.697 66.512 1.00 19.30 ? 128 GLU A CA 1 ATOM 1043 C C . GLU A 1 130 ? 42.009 9.168 66.379 1.00 17.75 ? 128 GLU A C 1 ATOM 1044 O O . GLU A 1 130 ? 43.127 9.424 65.903 1.00 18.34 ? 128 GLU A O 1 ATOM 1045 C CB . GLU A 1 130 ? 40.507 7.368 65.395 1.00 22.36 ? 128 GLU A CB 1 ATOM 1046 C CG . GLU A 1 130 ? 40.989 7.761 64.019 1.00 29.00 ? 128 GLU A CG 1 ATOM 1047 C CD . GLU A 1 130 ? 40.168 7.077 62.907 1.00 33.94 ? 128 GLU A CD 1 ATOM 1048 O OE1 . GLU A 1 130 ? 39.941 5.840 63.060 1.00 35.89 ? 128 GLU A OE1 1 ATOM 1049 O OE2 . GLU A 1 130 ? 39.751 7.768 61.906 1.00 33.50 ? 128 GLU A OE2 1 ATOM 1050 N N . ALA A 1 131 ? 41.180 10.119 66.794 1.00 15.53 ? 129 ALA A N 1 ATOM 1051 C CA . ALA A 1 131 ? 41.540 11.518 66.709 1.00 14.59 ? 129 ALA A CA 1 ATOM 1052 C C . ALA A 1 131 ? 40.693 12.298 67.696 1.00 13.21 ? 129 ALA A C 1 ATOM 1053 O O . ALA A 1 131 ? 39.590 11.841 68.118 1.00 15.33 ? 129 ALA A O 1 ATOM 1054 C CB . ALA A 1 131 ? 41.271 12.052 65.271 1.00 16.96 ? 129 ALA A CB 1 ATOM 1055 N N . GLY A 1 132 ? 41.205 13.454 68.079 1.00 13.00 ? 130 GLY A N 1 ATOM 1056 C CA . GLY A 1 132 ? 40.386 14.485 68.704 1.00 11.84 ? 130 GLY A CA 1 ATOM 1057 C C . GLY A 1 132 ? 40.341 15.679 67.769 1.00 10.91 ? 130 GLY A C 1 ATOM 1058 O O . GLY A 1 132 ? 41.371 16.061 67.160 1.00 12.32 ? 130 GLY A O 1 ATOM 1059 N N . ILE A 1 133 ? 39.150 16.246 67.602 1.00 10.26 ? 131 ILE A N 1 ATOM 1060 C CA . ILE A 1 133 ? 39.004 17.444 66.804 1.00 9.92 ? 131 ILE A CA 1 ATOM 1061 C C . ILE A 1 133 ? 38.499 18.548 67.753 1.00 10.56 ? 131 ILE A C 1 ATOM 1062 O O . ILE A 1 133 ? 37.471 18.381 68.439 1.00 11.04 ? 131 ILE A O 1 ATOM 1063 C CB . ILE A 1 133 ? 37.966 17.256 65.653 1.00 12.73 ? 131 ILE A CB 1 ATOM 1064 C CG1 . ILE A 1 133 ? 38.383 16.113 64.736 1.00 17.77 ? 131 ILE A CG1 1 ATOM 1065 C CG2 . ILE A 1 133 ? 37.817 18.566 64.885 1.00 14.96 ? 131 ILE A CG2 1 ATOM 1066 C CD1 . ILE A 1 133 ? 39.765 16.250 64.248 1.00 22.24 ? 131 ILE A CD1 1 ATOM 1067 N N . LYS A 1 134 ? 39.210 19.667 67.795 1.00 10.33 ? 132 LYS A N 1 ATOM 1068 C CA . LYS A 1 134 ? 38.929 20.687 68.791 1.00 10.62 ? 132 LYS A CA 1 ATOM 1069 C C . LYS A 1 134 ? 38.464 21.972 68.117 1.00 9.85 ? 132 LYS A C 1 ATOM 1070 O O . LYS A 1 134 ? 39.108 22.452 67.179 1.00 12.73 ? 132 LYS A O 1 ATOM 1071 C CB . LYS A 1 134 ? 40.182 20.928 69.652 1.00 11.03 ? 132 LYS A CB 1 ATOM 1072 C CG . LYS A 1 134 ? 39.945 21.999 70.747 1.00 10.30 ? 132 LYS A CG 1 ATOM 1073 C CD . LYS A 1 134 ? 41.021 21.831 71.867 1.00 11.23 ? 132 LYS A CD 1 ATOM 1074 C CE . LYS A 1 134 ? 42.348 22.485 71.487 1.00 12.36 ? 132 LYS A CE 1 ATOM 1075 N NZ . LYS A 1 134 ? 42.293 23.996 71.639 1.00 15.81 ? 132 LYS A NZ 1 ATOM 1076 N N . PHE A 1 135 ? 37.359 22.527 68.617 1.00 9.20 ? 133 PHE A N 1 ATOM 1077 C CA . PHE A 1 135 ? 36.827 23.797 68.164 1.00 8.85 ? 133 PHE A CA 1 ATOM 1078 C C . PHE A 1 135 ? 36.955 24.767 69.299 1.00 10.98 ? 133 PHE A C 1 ATOM 1079 O O . PHE A 1 135 ? 36.292 24.579 70.361 1.00 11.96 ? 133 PHE A O 1 ATOM 1080 C CB . PHE A 1 135 ? 35.322 23.645 67.779 1.00 10.75 ? 133 PHE A CB 1 ATOM 1081 C CG . PHE A 1 135 ? 35.093 22.575 66.762 1.00 10.59 ? 133 PHE A CG 1 ATOM 1082 C CD1 . PHE A 1 135 ? 35.146 22.908 65.408 1.00 11.21 ? 133 PHE A CD1 1 ATOM 1083 C CD2 . PHE A 1 135 ? 34.903 21.241 67.131 1.00 12.35 ? 133 PHE A CD2 1 ATOM 1084 C CE1 . PHE A 1 135 ? 34.989 21.910 64.426 1.00 12.25 ? 133 PHE A CE1 1 ATOM 1085 C CE2 . PHE A 1 135 ? 34.742 20.212 66.121 1.00 12.19 ? 133 PHE A CE2 1 ATOM 1086 C CZ . PHE A 1 135 ? 34.800 20.568 64.776 1.00 13.33 ? 133 PHE A CZ 1 ATOM 1087 N N . GLY A 1 136 ? 37.767 25.809 69.098 1.00 11.82 ? 134 GLY A N 1 ATOM 1088 C CA . GLY A 1 136 ? 38.070 26.773 70.165 1.00 10.92 ? 134 GLY A CA 1 ATOM 1089 C C . GLY A 1 136 ? 39.494 26.569 70.654 1.00 11.94 ? 134 GLY A C 1 ATOM 1090 O O . GLY A 1 136 ? 40.137 25.566 70.353 1.00 14.30 ? 134 GLY A O 1 ATOM 1091 N N . ASP A 1 137 ? 39.974 27.514 71.444 1.00 14.55 ? 135 ASP A N 1 ATOM 1092 C CA . ASP A 1 137 ? 41.378 27.573 71.834 1.00 15.60 ? 135 ASP A CA 1 ATOM 1093 C C . ASP A 1 137 ? 41.680 27.069 73.252 1.00 15.95 ? 135 ASP A C 1 ATOM 1094 O O . ASP A 1 137 ? 42.829 27.066 73.686 1.00 19.15 ? 135 ASP A O 1 ATOM 1095 C CB . ASP A 1 137 ? 41.913 29.009 71.677 1.00 19.12 ? 135 ASP A CB 1 ATOM 1096 C CG . ASP A 1 137 ? 41.990 29.433 70.224 1.00 24.75 ? 135 ASP A CG 1 ATOM 1097 O OD1 . ASP A 1 137 ? 42.002 28.565 69.308 1.00 26.05 ? 135 ASP A OD1 1 ATOM 1098 O OD2 . ASP A 1 137 ? 42.005 30.641 69.994 1.00 28.17 ? 135 ASP A OD2 1 ATOM 1099 N N . GLY A 1 138 ? 40.656 26.621 73.965 1.00 15.79 ? 136 GLY A N 1 ATOM 1100 C CA . GLY A 1 138 ? 40.844 26.142 75.326 1.00 14.25 ? 136 GLY A CA 1 ATOM 1101 C C . GLY A 1 138 ? 41.473 24.759 75.376 1.00 14.58 ? 136 GLY A C 1 ATOM 1102 O O . GLY A 1 138 ? 41.629 24.076 74.357 1.00 16.10 ? 136 GLY A O 1 ATOM 1103 N N . ASP A 1 139 ? 41.818 24.307 76.574 1.00 15.25 ? 137 ASP A N 1 ATOM 1104 C CA . ASP A 1 139 ? 42.378 22.980 76.699 1.00 14.47 ? 137 ASP A CA 1 ATOM 1105 C C . ASP A 1 139 ? 41.316 21.995 77.143 1.00 15.06 ? 137 ASP A C 1 ATOM 1106 O O . ASP A 1 139 ? 40.159 22.377 77.410 1.00 14.56 ? 137 ASP A O 1 ATOM 1107 C CB . ASP A 1 139 ? 43.622 22.948 77.605 1.00 17.58 ? 137 ASP A CB 1 ATOM 1108 C CG . ASP A 1 139 ? 43.330 23.315 79.062 1.00 20.21 ? 137 ASP A CG 1 ATOM 1109 O OD1 . ASP A 1 139 ? 42.283 23.027 79.611 1.00 18.31 ? 137 ASP A OD1 1 ATOM 1110 O OD2 . ASP A 1 139 ? 44.233 23.836 79.707 1.00 26.92 ? 137 ASP A OD2 1 ATOM 1111 N N . VAL A 1 140 ? 41.738 20.743 77.244 1.00 13.30 ? 138 VAL A N 1 ATOM 1112 C CA . VAL A 1 140 ? 40.843 19.621 77.484 1.00 12.42 ? 138 VAL A CA 1 ATOM 1113 C C . VAL A 1 140 ? 40.153 19.740 78.829 1.00 13.00 ? 138 VAL A C 1 ATOM 1114 O O . VAL A 1 140 ? 39.035 19.235 79.011 1.00 13.46 ? 138 VAL A O 1 ATOM 1115 C CB . VAL A 1 140 ? 41.614 18.289 77.390 1.00 12.41 ? 138 VAL A CB 1 ATOM 1116 C CG1 . VAL A 1 140 ? 42.709 18.165 78.460 1.00 13.98 ? 138 VAL A CG1 1 ATOM 1117 C CG2 . VAL A 1 140 ? 40.653 17.123 77.464 1.00 13.34 ? 138 VAL A CG2 1 ATOM 1118 N N . PHE A 1 141 ? 40.804 20.418 79.767 1.00 12.41 ? 139 PHE A N 1 ATOM 1119 C CA . PHE A 1 141 ? 40.260 20.501 81.147 1.00 15.29 ? 139 PHE A CA 1 ATOM 1120 C C . PHE A 1 141 ? 39.058 21.431 81.317 1.00 17.35 ? 139 PHE A C 1 ATOM 1121 O O . PHE A 1 141 ? 38.278 21.268 82.264 1.00 21.39 ? 139 PHE A O 1 ATOM 1122 C CB . PHE A 1 141 ? 41.374 20.893 82.122 1.00 18.34 ? 139 PHE A CB 1 ATOM 1123 C CG . PHE A 1 141 ? 42.452 19.874 82.202 1.00 18.96 ? 139 PHE A CG 1 ATOM 1124 C CD1 . PHE A 1 141 ? 42.270 18.718 82.966 1.00 19.60 ? 139 PHE A CD1 1 ATOM 1125 C CD2 . PHE A 1 141 ? 43.662 20.058 81.513 1.00 20.28 ? 139 PHE A CD2 1 ATOM 1126 C CE1 . PHE A 1 141 ? 43.313 17.758 83.037 1.00 21.34 ? 139 PHE A CE1 1 ATOM 1127 C CE2 . PHE A 1 141 ? 44.674 19.127 81.571 1.00 20.48 ? 139 PHE A CE2 1 ATOM 1128 C CZ . PHE A 1 141 ? 44.497 17.972 82.303 1.00 21.30 ? 139 PHE A CZ 1 ATOM 1129 N N . THR A 1 142 ? 38.896 22.428 80.445 1.00 16.64 ? 140 THR A N 1 ATOM 1130 C CA . THR A 1 142 ? 37.640 23.192 80.462 1.00 18.33 ? 140 THR A CA 1 ATOM 1131 C C . THR A 1 142 ? 36.842 22.965 79.167 1.00 16.07 ? 140 THR A C 1 ATOM 1132 O O . THR A 1 142 ? 35.778 23.581 78.963 1.00 18.15 ? 140 THR A O 1 ATOM 1133 C CB . THR A 1 142 ? 37.871 24.700 80.660 1.00 23.63 ? 140 THR A CB 1 ATOM 1134 O OG1 . THR A 1 142 ? 38.674 25.200 79.593 1.00 26.77 ? 140 THR A OG1 1 ATOM 1135 C CG2 . THR A 1 142 ? 38.496 25.028 82.036 1.00 26.71 ? 140 THR A CG2 1 ATOM 1136 N N . ALA A 1 143 ? 37.289 22.027 78.346 1.00 11.30 ? 141 ALA A N 1 ATOM 1137 C CA . ALA A 1 143 ? 36.544 21.726 77.116 1.00 10.88 ? 141 ALA A CA 1 ATOM 1138 C C . ALA A 1 143 ? 35.260 20.936 77.388 1.00 11.19 ? 141 ALA A C 1 ATOM 1139 O O . ALA A 1 143 ? 35.123 20.213 78.396 1.00 11.31 ? 141 ALA A O 1 ATOM 1140 C CB . ALA A 1 143 ? 37.428 20.979 76.115 1.00 11.19 ? 141 ALA A CB 1 ATOM 1141 N N . VAL A 1 144 ? 34.322 21.056 76.457 1.00 10.91 ? 142 VAL A N 1 ATOM 1142 C CA . VAL A 1 144 ? 33.133 20.189 76.375 1.00 11.13 ? 142 VAL A CA 1 ATOM 1143 C C . VAL A 1 144 ? 33.575 18.985 75.549 1.00 10.23 ? 142 VAL A C 1 ATOM 1144 O O . VAL A 1 144 ? 33.721 19.081 74.319 1.00 11.45 ? 142 VAL A O 1 ATOM 1145 C CB . VAL A 1 144 ? 31.984 20.949 75.688 1.00 12.91 ? 142 VAL A CB 1 ATOM 1146 C CG1 . VAL A 1 144 ? 30.852 19.982 75.268 1.00 13.18 ? 142 VAL A CG1 1 ATOM 1147 C CG2 . VAL A 1 144 ? 31.423 22.032 76.665 1.00 13.92 ? 142 VAL A CG2 1 ATOM 1148 N N . ASN A 1 145 ? 33.864 17.862 76.214 1.00 9.64 ? 143 ASN A N 1 ATOM 1149 C CA . ASN A 1 145 ? 34.388 16.682 75.537 1.00 8.89 ? 143 ASN A CA 1 ATOM 1150 C C . ASN A 1 145 ? 33.262 15.764 75.125 1.00 10.05 ? 143 ASN A C 1 ATOM 1151 O O . ASN A 1 145 ? 32.467 15.329 75.972 1.00 10.48 ? 143 ASN A O 1 ATOM 1152 C CB . ASN A 1 145 ? 35.356 15.902 76.450 1.00 9.91 ? 143 ASN A CB 1 ATOM 1153 C CG . ASN A 1 145 ? 36.637 16.674 76.728 1.00 10.59 ? 143 ASN A CG 1 ATOM 1154 O OD1 . ASN A 1 145 ? 37.572 16.629 75.923 1.00 10.15 ? 143 ASN A OD1 1 ATOM 1155 N ND2 . ASN A 1 145 ? 36.705 17.389 77.875 1.00 11.01 ? 143 ASN A ND2 1 ATOM 1156 N N . LEU A 1 146 ? 33.189 15.485 73.814 1.00 9.14 ? 144 LEU A N 1 ATOM 1157 C CA . LEU A 1 146 ? 32.154 14.609 73.262 1.00 8.03 ? 144 LEU A CA 1 ATOM 1158 C C . LEU A 1 146 ? 32.788 13.365 72.725 1.00 8.76 ? 144 LEU A C 1 ATOM 1159 O O . LEU A 1 146 ? 33.947 13.402 72.273 1.00 10.61 ? 144 LEU A O 1 ATOM 1160 C CB . LEU A 1 146 ? 31.393 15.277 72.115 1.00 9.29 ? 144 LEU A CB 1 ATOM 1161 C CG . LEU A 1 146 ? 30.660 16.583 72.433 1.00 14.43 ? 144 LEU A CG 1 ATOM 1162 C CD1 . LEU A 1 146 ? 29.797 16.973 71.280 1.00 17.29 ? 144 LEU A CD1 1 ATOM 1163 C CD2 . LEU A 1 146 ? 29.852 16.628 73.716 1.00 11.78 ? 144 LEU A CD2 1 ATOM 1164 N N . LEU A 1 147 ? 32.048 12.259 72.800 1.00 8.62 ? 145 LEU A N 1 ATOM 1165 C CA . LEU A 1 147 ? 32.493 11.007 72.172 1.00 9.76 ? 145 LEU A CA 1 ATOM 1166 C C . LEU A 1 147 ? 31.623 10.729 70.951 1.00 9.48 ? 145 LEU A C 1 ATOM 1167 O O . LEU A 1 147 ? 30.387 10.704 71.049 1.00 12.90 ? 145 LEU A O 1 ATOM 1168 C CB . LEU A 1 147 ? 32.375 9.845 73.140 1.00 12.61 ? 145 LEU A CB 1 ATOM 1169 C CG . LEU A 1 147 ? 32.791 8.459 72.597 1.00 12.32 ? 145 LEU A CG 1 ATOM 1170 C CD1 . LEU A 1 147 ? 34.307 8.429 72.280 1.00 12.44 ? 145 LEU A CD1 1 ATOM 1171 C CD2 . LEU A 1 147 ? 32.460 7.321 73.609 1.00 15.26 ? 145 LEU A CD2 1 ATOM 1172 N N . HIS A 1 148 ? 32.289 10.583 69.802 1.00 10.65 ? 146 HIS A N 1 ATOM 1173 C CA . HIS A 1 148 ? 31.615 10.214 68.562 1.00 11.13 ? 146 HIS A CA 1 ATOM 1174 C C . HIS A 1 148 ? 31.968 8.759 68.287 1.00 10.84 ? 146 HIS A C 1 ATOM 1175 O O . HIS A 1 148 ? 33.156 8.433 68.097 1.00 13.02 ? 146 HIS A O 1 ATOM 1176 C CB . HIS A 1 148 ? 32.106 11.139 67.431 1.00 12.40 ? 146 HIS A CB 1 ATOM 1177 C CG . HIS A 1 148 ? 31.524 10.814 66.086 1.00 12.65 ? 146 HIS A CG 1 ATOM 1178 N ND1 . HIS A 1 148 ? 30.237 11.152 65.719 1.00 17.16 ? 146 HIS A ND1 1 ATOM 1179 C CD2 . HIS A 1 148 ? 32.065 10.188 65.006 1.00 11.92 ? 146 HIS A CD2 1 ATOM 1180 C CE1 . HIS A 1 148 ? 30.010 10.717 64.482 1.00 10.91 ? 146 HIS A CE1 1 ATOM 1181 N NE2 . HIS A 1 148 ? 31.098 10.129 64.048 1.00 15.42 ? 146 HIS A NE2 1 ATOM 1182 N N . SER A 1 149 ? 30.961 7.874 68.264 1.00 13.84 ? 147 SER A N 1 ATOM 1183 C CA . SER A 1 149 ? 31.242 6.462 68.025 1.00 14.58 ? 147 SER A CA 1 ATOM 1184 C C . SER A 1 149 ? 30.279 5.836 66.994 1.00 17.65 ? 147 SER A C 1 ATOM 1185 O O . SER A 1 149 ? 29.173 6.354 66.728 1.00 16.23 ? 147 SER A O 1 ATOM 1186 C CB . SER A 1 149 ? 31.169 5.673 69.333 1.00 17.26 ? 147 SER A CB 1 ATOM 1187 O OG . SER A 1 149 ? 29.912 5.822 69.952 1.00 21.36 ? 147 SER A OG 1 ATOM 1188 N N . GLY A 1 150 ? 30.718 4.712 66.427 1.00 20.86 ? 148 GLY A N 1 ATOM 1189 C CA . GLY A 1 150 ? 29.960 4.006 65.411 1.00 20.73 ? 148 GLY A CA 1 ATOM 1190 C C . GLY A 1 150 ? 29.651 4.856 64.216 1.00 21.80 ? 148 GLY A C 1 ATOM 1191 O O . GLY A 1 150 ? 28.727 4.547 63.487 1.00 24.69 ? 148 GLY A O 1 ATOM 1192 N N . GLN A 1 151 ? 30.398 5.939 64.037 1.00 20.97 ? 149 GLN A N 1 ATOM 1193 C CA . GLN A 1 151 ? 30.164 6.880 62.935 1.00 19.47 ? 149 GLN A CA 1 ATOM 1194 C C . GLN A 1 151 ? 28.833 7.622 63.001 1.00 19.29 ? 149 GLN A C 1 ATOM 1195 O O . GLN A 1 151 ? 28.559 8.442 62.130 1.00 20.63 ? 149 GLN A O 1 ATOM 1196 C CB . GLN A 1 151 ? 30.340 6.212 61.563 1.00 24.25 ? 149 GLN A CB 1 ATOM 1197 C CG . GLN A 1 151 ? 31.753 5.725 61.288 0.0000 27.08 ? 149 GLN A CG 1 ATOM 1198 C CD . GLN A 1 151 ? 31.897 5.108 59.910 0.0000 29.45 ? 149 GLN A CD 1 ATOM 1199 O OE1 . GLN A 1 151 ? 30.972 4.478 59.398 0.0000 30.28 ? 149 GLN A OE1 1 ATOM 1200 N NE2 . GLN A 1 151 ? 33.061 5.294 59.298 0.0000 30.28 ? 149 GLN A NE2 1 ATOM 1201 N N . THR A 1 152 ? 28.011 7.369 64.020 1.00 18.50 ? 150 THR A N 1 ATOM 1202 C CA . THR A 1 152 ? 26.643 7.868 64.006 1.00 18.31 ? 150 THR A CA 1 ATOM 1203 C C . THR A 1 152 ? 26.069 8.281 65.370 1.00 17.76 ? 150 THR A C 1 ATOM 1204 O O . THR A 1 152 ? 24.856 8.477 65.487 1.00 16.53 ? 150 THR A O 1 ATOM 1205 C CB . THR A 1 152 ? 25.662 6.800 63.498 1.00 24.87 ? 150 THR A CB 1 ATOM 1206 O OG1 . THR A 1 152 ? 25.632 5.736 64.451 1.00 29.40 ? 150 THR A OG1 1 ATOM 1207 C CG2 . THR A 1 152 ? 26.085 6.269 62.164 1.00 26.51 ? 150 THR A CG2 1 ATOM 1208 N N . HIS A 1 153 ? 26.898 8.396 66.396 1.00 15.95 ? 151 HIS A N 1 ATOM 1209 C CA . HIS A 1 153 ? 26.358 8.536 67.768 1.00 13.61 ? 151 HIS A CA 1 ATOM 1210 C C . HIS A 1 153 ? 27.272 9.450 68.625 1.00 12.85 ? 151 HIS A C 1 ATOM 1211 O O . HIS A 1 153 ? 28.497 9.357 68.550 1.00 15.74 ? 151 HIS A O 1 ATOM 1212 C CB . HIS A 1 153 ? 26.277 7.136 68.370 1.00 17.02 ? 151 HIS A CB 1 ATOM 1213 C CG . HIS A 1 153 ? 25.681 7.104 69.736 1.00 18.24 ? 151 HIS A CG 1 ATOM 1214 N ND1 . HIS A 1 153 ? 24.326 7.222 69.960 1.00 21.81 ? 151 HIS A ND1 1 ATOM 1215 C CD2 . HIS A 1 153 ? 26.264 7.035 70.954 1.00 20.69 ? 151 HIS A CD2 1 ATOM 1216 C CE1 . HIS A 1 153 ? 24.092 7.159 71.259 1.00 23.31 ? 151 HIS A CE1 1 ATOM 1217 N NE2 . HIS A 1 153 ? 25.250 7.062 71.886 1.00 21.46 ? 151 HIS A NE2 1 ATOM 1218 N N . PHE A 1 154 ? 26.665 10.318 69.436 1.00 11.25 ? 152 PHE A N 1 ATOM 1219 C CA . PHE A 1 154 ? 27.380 11.162 70.378 1.00 11.01 ? 152 PHE A CA 1 ATOM 1220 C C . PHE A 1 154 ? 27.010 10.840 71.815 1.00 12.73 ? 152 PHE A C 1 ATOM 1221 O O . PHE A 1 154 ? 25.829 10.616 72.122 1.00 12.54 ? 152 PHE A O 1 ATOM 1222 C CB . PHE A 1 154 ? 27.044 12.636 70.160 1.00 11.66 ? 152 PHE A CB 1 ATOM 1223 C CG . PHE A 1 154 ? 27.692 13.234 68.924 1.00 12.14 ? 152 PHE A CG 1 ATOM 1224 C CD1 . PHE A 1 154 ? 29.058 13.505 68.887 1.00 12.60 ? 152 PHE A CD1 1 ATOM 1225 C CD2 . PHE A 1 154 ? 26.920 13.567 67.830 1.00 11.63 ? 152 PHE A CD2 1 ATOM 1226 C CE1 . PHE A 1 154 ? 29.645 14.078 67.774 1.00 11.35 ? 152 PHE A CE1 1 ATOM 1227 C CE2 . PHE A 1 154 ? 27.511 14.144 66.684 1.00 11.10 ? 152 PHE A CE2 1 ATOM 1228 C CZ . PHE A 1 154 ? 28.874 14.409 66.652 1.00 11.25 ? 152 PHE A CZ 1 ATOM 1229 N N . ASP A 1 155 ? 28.029 10.851 72.688 1.00 11.85 ? 153 ASP A N 1 ATOM 1230 C CA . ASP A 1 155 ? 27.809 10.876 74.147 1.00 11.95 ? 153 ASP A CA 1 ATOM 1231 C C . ASP A 1 155 ? 28.643 12.003 74.722 1.00 11.56 ? 153 ASP A C 1 ATOM 1232 O O . ASP A 1 155 ? 29.500 12.565 74.054 1.00 13.43 ? 153 ASP A O 1 ATOM 1233 C CB . ASP A 1 155 ? 28.205 9.553 74.853 1.00 12.42 ? 153 ASP A CB 1 ATOM 1234 C CG . ASP A 1 155 ? 27.396 8.371 74.365 1.00 14.25 ? 153 ASP A CG 1 ATOM 1235 O OD1 . ASP A 1 155 ? 26.212 8.252 74.795 1.00 15.10 ? 153 ASP A OD1 1 ATOM 1236 O OD2 . ASP A 1 155 ? 27.928 7.560 73.557 1.00 17.08 ? 153 ASP A OD2 1 ATOM 1237 N N . ALA A 1 156 ? 28.353 12.341 75.974 1.00 9.63 ? 154 ALA A N 1 ATOM 1238 C CA . ALA A 1 156 ? 29.153 13.299 76.701 1.00 10.13 ? 154 ALA A CA 1 ATOM 1239 C C . ALA A 1 156 ? 30.260 12.579 77.457 1.00 10.61 ? 154 ALA A C 1 ATOM 1240 O O . ALA A 1 156 ? 30.094 11.401 77.795 1.00 11.63 ? 154 ALA A O 1 ATOM 1241 C CB . ALA A 1 156 ? 28.274 14.134 77.663 1.00 9.54 ? 154 ALA A CB 1 ATOM 1242 N N . LEU A 1 157 ? 31.398 13.269 77.682 1.00 8.83 ? 155 LEU A N 1 ATOM 1243 C CA . LEU A 1 157 ? 32.499 12.699 78.486 1.00 8.78 ? 155 LEU A CA 1 ATOM 1244 C C . LEU A 1 157 ? 32.855 13.648 79.626 1.00 11.22 ? 155 LEU A C 1 ATOM 1245 O O . LEU A 1 157 ? 32.811 14.868 79.468 1.00 12.33 ? 155 LEU A O 1 ATOM 1246 C CB . LEU A 1 157 ? 33.760 12.539 77.647 1.00 10.20 ? 155 LEU A CB 1 ATOM 1247 C CG . LEU A 1 157 ? 33.635 11.613 76.426 1.00 9.47 ? 155 LEU A CG 1 ATOM 1248 C CD1 . LEU A 1 157 ? 34.919 11.764 75.599 1.00 12.94 ? 155 LEU A CD1 1 ATOM 1249 C CD2 . LEU A 1 157 ? 33.407 10.173 76.883 1.00 11.22 ? 155 LEU A CD2 1 ATOM 1250 N N . ARG A 1 158 ? 33.219 13.080 80.773 1.00 11.81 ? 156 ARG A N 1 ATOM 1251 C CA . ARG A 1 158 ? 33.751 13.877 81.879 1.00 12.38 ? 156 ARG A CA 1 ATOM 1252 C C . ARG A 1 158 ? 35.100 13.293 82.286 1.00 13.04 ? 156 ARG A C 1 ATOM 1253 O O . ARG A 1 158 ? 35.243 12.077 82.446 1.00 13.30 ? 156 ARG A O 1 ATOM 1254 C CB . ARG A 1 158 ? 32.772 13.889 83.097 1.00 12.41 ? 156 ARG A CB 1 ATOM 1255 C CG . ARG A 1 158 ? 31.555 14.787 82.857 1.00 13.84 ? 156 ARG A CG 1 ATOM 1256 C CD . ARG A 1 158 ? 30.771 15.074 84.137 1.00 20.29 ? 156 ARG A CD 1 ATOM 1257 N NE . ARG A 1 158 ? 29.720 16.076 83.909 1.00 25.46 ? 156 ARG A NE 1 ATOM 1258 C CZ . ARG A 1 158 ? 28.451 15.749 83.743 1.00 29.34 ? 156 ARG A CZ 1 ATOM 1259 N NH1 . ARG A 1 158 ? 28.094 14.469 83.907 1.00 32.49 ? 156 ARG A NH1 1 ATOM 1260 N NH2 . ARG A 1 158 ? 27.545 16.681 83.495 1.00 29.41 ? 156 ARG A NH2 1 ATOM 1261 N N . ILE A 1 159 ? 36.096 14.162 82.425 1.00 12.01 ? 157 ILE A N 1 ATOM 1262 C CA . ILE A 1 159 ? 37.391 13.703 82.894 1.00 11.71 ? 157 ILE A CA 1 ATOM 1263 C C . ILE A 1 159 ? 37.232 13.019 84.266 1.00 11.27 ? 157 ILE A C 1 ATOM 1264 O O . ILE A 1 159 ? 36.564 13.555 85.173 1.00 12.78 ? 157 ILE A O 1 ATOM 1265 C CB . ILE A 1 159 ? 38.375 14.881 83.010 1.00 12.34 ? 157 ILE A CB 1 ATOM 1266 C CG1 . ILE A 1 159 ? 38.601 15.472 81.577 1.00 11.99 ? 157 ILE A CG1 1 ATOM 1267 C CG2 . ILE A 1 159 ? 39.727 14.389 83.615 1.00 14.34 ? 157 ILE A CG2 1 ATOM 1268 C CD1 . ILE A 1 159 ? 39.380 16.757 81.533 1.00 15.20 ? 157 ILE A CD1 1 ATOM 1269 N N . LEU A 1 160 ? 37.881 11.867 84.419 1.00 10.30 ? 158 LEU A N 1 ATOM 1270 C CA . LEU A 1 160 ? 37.812 11.124 85.683 1.00 12.68 ? 158 LEU A CA 1 ATOM 1271 C C . LEU A 1 160 ? 38.529 11.926 86.759 1.00 14.12 ? 158 LEU A C 1 ATOM 1272 O O . LEU A 1 160 ? 39.518 12.601 86.467 1.00 14.28 ? 158 LEU A O 1 ATOM 1273 C CB . LEU A 1 160 ? 38.416 9.741 85.533 1.00 13.87 ? 158 LEU A CB 1 ATOM 1274 C CG . LEU A 1 160 ? 37.561 8.792 84.645 1.00 17.31 ? 158 LEU A CG 1 ATOM 1275 C CD1 . LEU A 1 160 ? 38.380 7.516 84.279 1.00 15.19 ? 158 LEU A CD1 1 ATOM 1276 C CD2 . LEU A 1 160 ? 36.235 8.454 85.346 1.00 17.98 ? 158 LEU A CD2 1 ATOM 1277 N N . PRO A 1 161 ? 38.020 11.860 88.012 1.00 14.33 ? 159 PRO A N 1 ATOM 1278 C CA . PRO A 1 161 ? 38.466 12.756 89.104 1.00 16.52 ? 159 PRO A CA 1 ATOM 1279 C C . PRO A 1 161 ? 39.968 12.734 89.377 1.00 16.20 ? 159 PRO A C 1 ATOM 1280 O O . PRO A 1 161 ? 40.527 13.809 89.678 1.00 18.82 ? 159 PRO A O 1 ATOM 1281 C CB . PRO A 1 161 ? 37.701 12.262 90.348 1.00 18.32 ? 159 PRO A CB 1 ATOM 1282 C CG . PRO A 1 161 ? 36.645 11.359 89.848 1.00 19.22 ? 159 PRO A CG 1 ATOM 1283 C CD . PRO A 1 161 ? 36.993 10.891 88.444 1.00 15.31 ? 159 PRO A CD 1 ATOM 1284 N N . GLN A 1 162 ? 40.629 11.585 89.259 1.00 12.86 ? 160 GLN A N 1 ATOM 1285 C CA . GLN A 1 162 ? 42.037 11.519 89.625 1.00 12.60 ? 160 GLN A CA 1 ATOM 1286 C C . GLN A 1 162 ? 42.912 12.326 88.684 1.00 14.28 ? 160 GLN A C 1 ATOM 1287 O O . GLN A 1 162 ? 44.049 12.649 89.038 1.00 17.64 ? 160 GLN A O 1 ATOM 1288 C CB . GLN A 1 162 ? 42.533 10.046 89.715 1.00 13.62 ? 160 GLN A CB 1 ATOM 1289 C CG . GLN A 1 162 ? 42.573 9.345 88.334 1.00 13.69 ? 160 GLN A CG 1 ATOM 1290 C CD . GLN A 1 162 ? 41.386 8.439 88.073 1.00 13.07 ? 160 GLN A CD 1 ATOM 1291 O OE1 . GLN A 1 162 ? 41.528 7.343 87.461 1.00 16.22 ? 160 GLN A OE1 1 ATOM 1292 N NE2 . GLN A 1 162 ? 40.221 8.868 88.501 1.00 10.39 ? 160 GLN A NE2 1 ATOM 1293 N N . PHE A 1 163 ? 42.368 12.734 87.527 1.00 14.29 ? 161 PHE A N 1 ATOM 1294 C CA . PHE A 1 163 ? 43.172 13.503 86.568 1.00 16.39 ? 161 PHE A CA 1 ATOM 1295 C C . PHE A 1 163 ? 42.908 14.995 86.728 1.00 20.22 ? 161 PHE A C 1 ATOM 1296 O O . PHE A 1 163 ? 43.561 15.813 86.071 1.00 22.34 ? 161 PHE A O 1 ATOM 1297 C CB . PHE A 1 163 ? 42.877 13.023 85.123 1.00 13.86 ? 161 PHE A CB 1 ATOM 1298 C CG . PHE A 1 163 ? 43.109 11.552 84.967 1.00 15.16 ? 161 PHE A CG 1 ATOM 1299 C CD1 . PHE A 1 163 ? 44.383 11.024 85.177 1.00 15.25 ? 161 PHE A CD1 1 ATOM 1300 C CD2 . PHE A 1 163 ? 42.052 10.694 84.722 1.00 14.59 ? 161 PHE A CD2 1 ATOM 1301 C CE1 . PHE A 1 163 ? 44.603 9.647 85.097 1.00 14.48 ? 161 PHE A CE1 1 ATOM 1302 C CE2 . PHE A 1 163 ? 42.243 9.340 84.631 1.00 15.11 ? 161 PHE A CE2 1 ATOM 1303 C CZ . PHE A 1 163 ? 43.541 8.798 84.820 1.00 15.73 ? 161 PHE A CZ 1 ATOM 1304 N N . GLU A 1 164 ? 41.982 15.331 87.635 1.00 24.42 ? 162 GLU A N 1 ATOM 1305 C CA . GLU A 1 164 ? 41.394 16.667 87.756 1.00 33.72 ? 162 GLU A CA 1 ATOM 1306 C C . GLU A 1 164 ? 40.191 16.858 86.815 1.00 38.41 ? 162 GLU A C 1 ATOM 1307 O O . GLU A 1 164 ? 39.073 16.366 87.081 1.00 42.12 ? 162 GLU A O 1 ATOM 1308 C CB . GLU A 1 164 ? 42.448 17.740 87.511 1.00 37.88 ? 162 GLU A CB 1 ATOM 1309 C CG . GLU A 1 164 ? 43.647 17.639 88.445 1.00 40.95 ? 162 GLU A CG 1 ATOM 1310 C CD . GLU A 1 164 ? 43.234 17.464 89.873 1.00 44.04 ? 162 GLU A CD 1 ATOM 1311 O OE1 . GLU A 1 164 ? 42.021 17.240 90.087 1.00 41.96 ? 162 GLU A OE1 1 ATOM 1312 O OE2 . GLU A 1 164 ? 44.127 17.571 90.786 1.00 47.15 ? 162 GLU A OE2 1 ATOM 1313 N N . GLU B 2 3 ? 51.814 19.192 34.058 1.00 48.59 ? 80 GLU B N 1 ATOM 1314 C CA . GLU B 2 3 ? 52.818 18.204 34.474 1.00 48.37 ? 80 GLU B CA 1 ATOM 1315 C C . GLU B 2 3 ? 52.390 17.554 35.796 1.00 44.56 ? 80 GLU B C 1 ATOM 1316 O O . GLU B 2 3 ? 51.988 18.241 36.742 1.00 45.08 ? 80 GLU B O 1 ATOM 1317 C CB . GLU B 2 3 ? 54.213 18.828 34.585 0.0000 50.97 ? 80 GLU B CB 1 ATOM 1318 C CG . GLU B 2 3 ? 54.943 18.980 33.250 0.0000 53.20 ? 80 GLU B CG 1 ATOM 1319 C CD . GLU B 2 3 ? 55.407 17.651 32.671 0.0000 54.98 ? 80 GLU B CD 1 ATOM 1320 O OE1 . GLU B 2 3 ? 56.252 16.984 33.304 0.0000 55.59 ? 80 GLU B OE1 1 ATOM 1321 O OE2 . GLU B 2 3 ? 54.928 17.275 31.580 0.0000 55.59 ? 80 GLU B OE2 1 ATOM 1322 N N . PRO B 2 4 ? 52.432 16.222 35.853 1.00 40.72 ? 81 PRO B N 1 ATOM 1323 C CA . PRO B 2 4 ? 51.961 15.522 37.061 1.00 38.54 ? 81 PRO B CA 1 ATOM 1324 C C . PRO B 2 4 ? 52.882 15.752 38.274 1.00 34.64 ? 81 PRO B C 1 ATOM 1325 O O . PRO B 2 4 ? 54.116 15.826 38.116 1.00 36.42 ? 81 PRO B O 1 ATOM 1326 C CB . PRO B 2 4 ? 51.995 14.043 36.636 1.00 40.55 ? 81 PRO B CB 1 ATOM 1327 C CG . PRO B 2 4 ? 51.937 14.068 35.141 1.00 41.44 ? 81 PRO B CG 1 ATOM 1328 C CD . PRO B 2 4 ? 52.685 15.304 34.731 1.00 41.41 ? 81 PRO B CD 1 ATOM 1329 N N . LEU B 2 5 ? 52.316 15.900 39.465 1.00 28.61 ? 82 LEU B N 1 ATOM 1330 C CA . LEU B 2 5 ? 53.137 15.844 40.666 1.00 26.91 ? 82 LEU B CA 1 ATOM 1331 C C . LEU B 2 5 ? 52.443 15.013 41.753 1.00 23.15 ? 82 LEU B C 1 ATOM 1332 O O . LEU B 2 5 ? 51.240 14.779 41.691 1.00 21.58 ? 82 LEU B O 1 ATOM 1333 C CB . LEU B 2 5 ? 53.439 17.239 41.192 1.00 26.77 ? 82 LEU B CB 1 ATOM 1334 C CG . LEU B 2 5 ? 52.261 18.072 41.719 1.00 26.25 ? 82 LEU B CG 1 ATOM 1335 C CD1 . LEU B 2 5 ? 52.693 18.945 42.849 1.00 27.83 ? 82 LEU B CD1 1 ATOM 1336 C CD2 . LEU B 2 5 ? 51.596 18.926 40.643 1.00 27.66 ? 82 LEU B CD2 1 ATOM 1337 N N . SER B 2 6 ? 53.218 14.571 42.738 1.00 24.01 ? 83 SER B N 1 ATOM 1338 C CA . SER B 2 6 ? 52.718 13.836 43.906 1.00 21.93 ? 83 SER B CA 1 ATOM 1339 C C . SER B 2 6 ? 52.575 14.755 45.093 1.00 19.55 ? 83 SER B C 1 ATOM 1340 O O . SER B 2 6 ? 53.489 15.508 45.422 1.00 21.51 ? 83 SER B O 1 ATOM 1341 C CB . SER B 2 6 ? 53.743 12.779 44.313 1.00 26.35 ? 83 SER B CB 1 ATOM 1342 O OG . SER B 2 6 ? 53.971 11.892 43.252 1.00 27.93 ? 83 SER B OG 1 ATOM 1343 N N . ILE B 2 7 ? 51.418 14.692 45.740 1.00 17.40 ? 84 ILE B N 1 ATOM 1344 C CA . ILE B 2 7 ? 51.197 15.365 46.998 1.00 17.97 ? 84 ILE B CA 1 ATOM 1345 C C . ILE B 2 7 ? 50.729 14.355 48.032 1.00 18.24 ? 84 ILE B C 1 ATOM 1346 O O . ILE B 2 7 ? 50.458 13.200 47.723 1.00 19.43 ? 84 ILE B O 1 ATOM 1347 C CB . ILE B 2 7 ? 50.155 16.510 46.875 1.00 16.81 ? 84 ILE B CB 1 ATOM 1348 C CG1 . ILE B 2 7 ? 48.783 15.942 46.520 1.00 16.78 ? 84 ILE B CG1 1 ATOM 1349 C CG2 . ILE B 2 7 ? 50.651 17.614 45.852 1.00 16.58 ? 84 ILE B CG2 1 ATOM 1350 C CD1 . ILE B 2 7 ? 47.677 16.970 46.578 1.00 18.62 ? 84 ILE B CD1 1 ATOM 1351 N N . LEU B 2 8 ? 50.677 14.788 49.282 1.00 16.92 ? 85 LEU B N 1 ATOM 1352 C CA . LEU B 2 8 ? 50.212 13.900 50.366 1.00 16.95 ? 85 LEU B CA 1 ATOM 1353 C C . LEU B 2 8 ? 48.893 14.428 50.898 1.00 16.51 ? 85 LEU B C 1 ATOM 1354 O O . LEU B 2 8 ? 48.737 15.622 51.061 1.00 17.44 ? 85 LEU B O 1 ATOM 1355 C CB . LEU B 2 8 ? 51.233 13.889 51.506 1.00 19.92 ? 85 LEU B CB 1 ATOM 1356 C CG . LEU B 2 8 ? 52.653 13.418 51.138 1.00 23.39 ? 85 LEU B CG 1 ATOM 1357 C CD1 . LEU B 2 8 ? 53.539 13.478 52.345 1.00 22.45 ? 85 LEU B CD1 1 ATOM 1358 C CD2 . LEU B 2 8 ? 52.586 12.017 50.636 1.00 27.06 ? 85 LEU B CD2 1 ATOM 1359 N N . VAL B 2 9 ? 47.950 13.549 51.189 1.00 16.00 ? 86 VAL B N 1 ATOM 1360 C CA . VAL B 2 9 ? 46.755 13.929 51.936 1.00 14.49 ? 86 VAL B CA 1 ATOM 1361 C C . VAL B 2 9 ? 46.661 13.099 53.213 1.00 16.49 ? 86 VAL B C 1 ATOM 1362 O O . VAL B 2 9 ? 46.699 11.880 53.164 1.00 17.02 ? 86 VAL B O 1 ATOM 1363 C CB . VAL B 2 9 ? 45.436 13.795 51.117 1.00 12.74 ? 86 VAL B CB 1 ATOM 1364 C CG1 . VAL B 2 9 ? 44.225 14.286 51.962 1.00 11.48 ? 86 VAL B CG1 1 ATOM 1365 C CG2 . VAL B 2 9 ? 45.542 14.626 49.835 1.00 12.71 ? 86 VAL B CG2 1 ATOM 1366 N N . ARG B 2 10 ? 46.570 13.796 54.351 1.00 17.10 ? 87 ARG B N 1 ATOM 1367 C CA . ARG B 2 10 ? 46.602 13.165 55.677 1.00 16.16 ? 87 ARG B CA 1 ATOM 1368 C C . ARG B 2 10 ? 45.182 12.956 56.180 1.00 16.54 ? 87 ARG B C 1 ATOM 1369 O O . ARG B 2 10 ? 44.374 13.873 56.176 1.00 16.30 ? 87 ARG B O 1 ATOM 1370 C CB . ARG B 2 10 ? 47.397 14.042 56.652 1.00 17.65 ? 87 ARG B CB 1 ATOM 1371 C CG . ARG B 2 10 ? 47.631 13.371 58.032 1.00 20.32 ? 87 ARG B CG 1 ATOM 1372 C CD . ARG B 2 10 ? 48.515 14.254 58.934 1.00 24.02 ? 87 ARG B CD 1 ATOM 1373 N NE . ARG B 2 10 ? 49.884 14.342 58.438 0.0000 26.08 ? 87 ARG B NE 1 ATOM 1374 C CZ . ARG B 2 10 ? 50.811 15.146 58.947 0.0000 27.90 ? 87 ARG B CZ 1 ATOM 1375 N NH1 . ARG B 2 10 ? 50.516 15.940 59.967 0.0000 28.53 ? 87 ARG B NH1 1 ATOM 1376 N NH2 . ARG B 2 10 ? 52.033 15.159 58.434 0.0000 28.53 ? 87 ARG B NH2 1 ATOM 1377 N N . ASN B 2 11 ? 44.863 11.740 56.588 1.00 13.40 ? 88 ASN B N 1 ATOM 1378 C CA . ASN B 2 11 ? 43.501 11.483 57.051 1.00 15.31 ? 88 ASN B CA 1 ATOM 1379 C C . ASN B 2 11 ? 43.328 11.696 58.579 1.00 16.87 ? 88 ASN B C 1 ATOM 1380 O O . ASN B 2 11 ? 44.260 12.119 59.266 1.00 19.04 ? 88 ASN B O 1 ATOM 1381 C CB . ASN B 2 11 ? 43.028 10.098 56.617 1.00 14.75 ? 88 ASN B CB 1 ATOM 1382 C CG . ASN B 2 11 ? 43.758 8.955 57.364 1.00 16.77 ? 88 ASN B CG 1 ATOM 1383 O OD1 . ASN B 2 11 ? 44.402 9.176 58.394 1.00 17.69 ? 88 ASN B OD1 1 ATOM 1384 N ND2 . ASN B 2 11 ? 43.594 7.727 56.880 1.00 19.23 ? 88 ASN B ND2 1 ATOM 1385 N N . ASN B 2 12 ? 42.117 11.426 59.063 1.00 16.53 ? 89 ASN B N 1 ATOM 1386 C CA . ASN B 2 12 ? 41.715 11.633 60.478 1.00 18.40 ? 89 ASN B CA 1 ATOM 1387 C C . ASN B 2 12 ? 42.606 10.897 61.460 1.00 20.21 ? 89 ASN B C 1 ATOM 1388 O O . ASN B 2 12 ? 42.909 11.414 62.559 1.00 20.70 ? 89 ASN B O 1 ATOM 1389 C CB . ASN B 2 12 ? 40.274 11.135 60.665 1.00 18.30 ? 89 ASN B CB 1 ATOM 1390 C CG . ASN B 2 12 ? 39.716 11.444 62.033 1.00 19.10 ? 89 ASN B CG 1 ATOM 1391 O OD1 . ASN B 2 12 ? 39.460 10.536 62.831 1.00 20.05 ? 89 ASN B OD1 1 ATOM 1392 N ND2 . ASN B 2 12 ? 39.537 12.713 62.325 1.00 17.16 ? 89 ASN B ND2 1 ATOM 1393 N N . LYS B 2 13 ? 43.029 9.692 61.077 1.00 21.18 ? 90 LYS B N 1 ATOM 1394 C CA . LYS B 2 13 ? 43.896 8.877 61.935 1.00 22.10 ? 90 LYS B CA 1 ATOM 1395 C C . LYS B 2 13 ? 45.338 9.356 61.951 1.00 21.60 ? 90 LYS B C 1 ATOM 1396 O O . LYS B 2 13 ? 46.126 8.882 62.782 1.00 22.97 ? 90 LYS B O 1 ATOM 1397 C CB . LYS B 2 13 ? 43.881 7.386 61.490 1.00 24.51 ? 90 LYS B CB 1 ATOM 1398 C CG . LYS B 2 13 ? 42.530 6.842 61.092 0.0000 27.01 ? 90 LYS B CG 1 ATOM 1399 C CD . LYS B 2 13 ? 42.582 5.331 60.938 0.0000 29.22 ? 90 LYS B CD 1 ATOM 1400 C CE . LYS B 2 13 ? 41.476 4.839 60.027 0.0000 30.88 ? 90 LYS B CE 1 ATOM 1401 N NZ . LYS B 2 13 ? 41.593 5.447 58.673 0.0000 31.73 ? 90 LYS B NZ 1 ATOM 1402 N N . GLY B 2 14 ? 45.678 10.292 61.052 1.00 21.91 ? 91 GLY B N 1 ATOM 1403 C CA . GLY B 2 14 ? 47.030 10.827 60.901 1.00 19.10 ? 91 GLY B CA 1 ATOM 1404 C C . GLY B 2 14 ? 47.892 10.115 59.857 1.00 19.83 ? 91 GLY B C 1 ATOM 1405 O O . GLY B 2 14 ? 49.115 10.302 59.819 1.00 23.18 ? 91 GLY B O 1 ATOM 1406 N N . ARG B 2 15 ? 47.276 9.276 59.028 1.00 18.88 ? 92 ARG B N 1 ATOM 1407 C CA . ARG B 2 15 ? 48.006 8.539 57.991 1.00 20.39 ? 92 ARG B CA 1 ATOM 1408 C C . ARG B 2 15 ? 48.004 9.350 56.695 1.00 20.64 ? 92 ARG B C 1 ATOM 1409 O O . ARG B 2 15 ? 46.926 9.717 56.210 1.00 20.62 ? 92 ARG B O 1 ATOM 1410 C CB . ARG B 2 15 ? 47.322 7.168 57.749 1.00 22.89 ? 92 ARG B CB 1 ATOM 1411 C CG . ARG B 2 15 ? 47.875 6.395 56.512 1.00 26.74 ? 92 ARG B CG 1 ATOM 1412 C CD . ARG B 2 15 ? 47.047 5.137 56.117 1.00 29.56 ? 92 ARG B CD 1 ATOM 1413 N NE . ARG B 2 15 ? 45.829 5.467 55.359 1.00 32.51 ? 92 ARG B NE 1 ATOM 1414 C CZ . ARG B 2 15 ? 44.842 4.605 55.066 1.00 33.33 ? 92 ARG B CZ 1 ATOM 1415 N NH1 . ARG B 2 15 ? 44.890 3.341 55.466 1.00 33.91 ? 92 ARG B NH1 1 ATOM 1416 N NH2 . ARG B 2 15 ? 43.779 5.010 54.394 1.00 31.88 ? 92 ARG B NH2 1 ATOM 1417 N N . SER B 2 16 ? 49.183 9.632 56.133 1.00 20.20 ? 93 SER B N 1 ATOM 1418 C CA . SER B 2 16 ? 49.254 10.297 54.811 1.00 20.57 ? 93 SER B CA 1 ATOM 1419 C C . SER B 2 16 ? 49.351 9.291 53.669 1.00 22.03 ? 93 SER B C 1 ATOM 1420 O O . SER B 2 16 ? 50.078 8.276 53.770 1.00 25.52 ? 93 SER B O 1 ATOM 1421 C CB . SER B 2 16 ? 50.445 11.288 54.743 1.00 20.65 ? 93 SER B CB 1 ATOM 1422 O OG . SER B 2 16 ? 50.268 12.322 55.720 1.00 24.36 ? 93 SER B OG 1 ATOM 1423 N N . SER B 2 17 ? 48.604 9.549 52.598 1.00 19.00 ? 94 SER B N 1 ATOM 1424 C CA . SER B 2 17 ? 48.713 8.758 51.379 1.00 19.12 ? 94 SER B CA 1 ATOM 1425 C C . SER B 2 17 ? 49.162 9.667 50.244 1.00 19.31 ? 94 SER B C 1 ATOM 1426 O O . SER B 2 17 ? 48.900 10.860 50.262 1.00 19.47 ? 94 SER B O 1 ATOM 1427 C CB . SER B 2 17 ? 47.361 8.117 51.044 1.00 19.68 ? 94 SER B CB 1 ATOM 1428 O OG . SER B 2 17 ? 47.041 7.102 52.018 1.00 20.67 ? 94 SER B OG 1 ATOM 1429 N N . THR B 2 18 ? 49.812 9.094 49.243 1.00 20.83 ? 95 THR B N 1 ATOM 1430 C CA . THR B 2 18 ? 50.313 9.846 48.096 1.00 21.83 ? 95 THR B CA 1 ATOM 1431 C C . THR B 2 18 ? 49.297 9.864 46.940 1.00 21.02 ? 95 THR B C 1 ATOM 1432 O O . THR B 2 18 ? 48.625 8.864 46.683 1.00 20.56 ? 95 THR B O 1 ATOM 1433 C CB . THR B 2 18 ? 51.634 9.227 47.652 1.00 25.24 ? 95 THR B CB 1 ATOM 1434 O OG1 . THR B 2 18 ? 52.500 9.206 48.781 1.00 26.97 ? 95 THR B OG1 1 ATOM 1435 C CG2 . THR B 2 18 ? 52.274 10.027 46.578 1.00 26.61 ? 95 THR B CG2 1 ATOM 1436 N N . TYR B 2 19 ? 49.154 11.024 46.290 1.00 19.48 ? 96 TYR B N 1 ATOM 1437 C CA . TYR B 2 19 ? 48.259 11.172 45.143 1.00 20.33 ? 96 TYR B CA 1 ATOM 1438 C C . TYR B 2 19 ? 49.002 11.854 44.021 1.00 20.59 ? 96 TYR B C 1 ATOM 1439 O O . TYR B 2 19 ? 49.701 12.840 44.254 1.00 22.15 ? 96 TYR B O 1 ATOM 1440 C CB . TYR B 2 19 ? 47.032 12.043 45.497 1.00 19.78 ? 96 TYR B CB 1 ATOM 1441 C CG . TYR B 2 19 ? 46.150 11.465 46.600 1.00 16.97 ? 96 TYR B CG 1 ATOM 1442 C CD1 . TYR B 2 19 ? 44.976 10.781 46.276 1.00 16.21 ? 96 TYR B CD1 1 ATOM 1443 C CD2 . TYR B 2 19 ? 46.528 11.540 47.942 1.00 12.53 ? 96 TYR B CD2 1 ATOM 1444 C CE1 . TYR B 2 19 ? 44.166 10.237 47.231 1.00 15.67 ? 96 TYR B CE1 1 ATOM 1445 C CE2 . TYR B 2 19 ? 45.720 11.006 48.933 1.00 13.51 ? 96 TYR B CE2 1 ATOM 1446 C CZ . TYR B 2 19 ? 44.551 10.351 48.580 1.00 14.70 ? 96 TYR B CZ 1 ATOM 1447 O OH . TYR B 2 19 ? 43.757 9.841 49.558 1.00 15.16 ? 96 TYR B OH 1 ATOM 1448 N N . GLU B 2 20 ? 48.839 11.327 42.803 1.00 19.70 ? 97 GLU B N 1 ATOM 1449 C CA . GLU B 2 20 ? 49.313 12.018 41.603 1.00 21.48 ? 97 GLU B CA 1 ATOM 1450 C C . GLU B 2 20 ? 48.197 12.997 41.183 1.00 19.07 ? 97 GLU B C 1 ATOM 1451 O O . GLU B 2 20 ? 47.056 12.600 41.053 1.00 19.62 ? 97 GLU B O 1 ATOM 1452 C CB . GLU B 2 20 ? 49.684 11.042 40.456 1.00 24.50 ? 97 GLU B CB 1 ATOM 1453 C CG . GLU B 2 20 ? 50.975 10.270 40.630 0.0000 27.64 ? 97 GLU B CG 1 ATOM 1454 C CD . GLU B 2 20 ? 51.455 9.683 39.315 0.0000 30.24 ? 97 GLU B CD 1 ATOM 1455 O OE1 . GLU B 2 20 ? 51.101 10.245 38.256 0.0000 31.12 ? 97 GLU B OE1 1 ATOM 1456 O OE2 . GLU B 2 20 ? 52.174 8.662 39.335 0.0000 31.12 ? 97 GLU B OE2 1 ATOM 1457 N N . VAL B 2 21 ? 48.549 14.271 41.026 1.00 18.42 ? 98 VAL B N 1 ATOM 1458 C CA . VAL B 2 21 ? 47.630 15.341 40.657 1.00 16.98 ? 98 VAL B CA 1 ATOM 1459 C C . VAL B 2 21 ? 48.265 16.238 39.597 1.00 18.70 ? 98 VAL B C 1 ATOM 1460 O O . VAL B 2 21 ? 49.471 16.126 39.305 1.00 20.92 ? 98 VAL B O 1 ATOM 1461 C CB . VAL B 2 21 ? 47.276 16.239 41.904 1.00 16.11 ? 98 VAL B CB 1 ATOM 1462 C CG1 . VAL B 2 21 ? 46.559 15.401 42.996 1.00 16.08 ? 98 VAL B CG1 1 ATOM 1463 C CG2 . VAL B 2 21 ? 48.519 16.915 42.469 1.00 18.52 ? 98 VAL B CG2 1 ATOM 1464 N N . ARG B 2 22 ? 47.457 17.122 39.020 1.00 16.64 ? 99 ARG B N 1 ATOM 1465 C CA . ARG B 2 22 ? 47.960 18.197 38.175 1.00 20.26 ? 99 ARG B CA 1 ATOM 1466 C C . ARG B 2 22 ? 47.462 19.506 38.791 1.00 18.74 ? 99 ARG B C 1 ATOM 1467 O O . ARG B 2 22 ? 46.357 19.548 39.370 1.00 19.07 ? 99 ARG B O 1 ATOM 1468 C CB . ARG B 2 22 ? 47.441 18.067 36.732 1.00 21.22 ? 99 ARG B CB 1 ATOM 1469 C CG . ARG B 2 22 ? 47.905 16.809 35.979 1.00 24.47 ? 99 ARG B CG 1 ATOM 1470 C CD . ARG B 2 22 ? 47.341 16.788 34.569 0.0000 28.33 ? 99 ARG B CD 1 ATOM 1471 N NE . ARG B 2 22 ? 47.945 15.735 33.760 0.0000 31.76 ? 99 ARG B NE 1 ATOM 1472 C CZ . ARG B 2 22 ? 49.189 15.780 33.295 0.0000 34.50 ? 99 ARG B CZ 1 ATOM 1473 N NH1 . ARG B 2 22 ? 49.962 16.822 33.567 0.0000 35.44 ? 99 ARG B NH1 1 ATOM 1474 N NH2 . ARG B 2 22 ? 49.664 14.781 32.564 0.0000 35.44 ? 99 ARG B NH2 1 ATOM 1475 N N . LEU B 2 23 ? 48.251 20.576 38.701 1.00 19.71 ? 100 LEU B N 1 ATOM 1476 C CA . LEU B 2 23 ? 47.842 21.819 39.362 1.00 19.48 ? 100 LEU B CA 1 ATOM 1477 C C . LEU B 2 23 ? 46.658 22.438 38.678 1.00 17.89 ? 100 LEU B C 1 ATOM 1478 O O . LEU B 2 23 ? 46.011 23.324 39.242 1.00 16.78 ? 100 LEU B O 1 ATOM 1479 C CB . LEU B 2 23 ? 49.002 22.820 39.454 1.00 20.13 ? 100 LEU B CB 1 ATOM 1480 C CG . LEU B 2 23 ? 50.116 22.319 40.363 1.00 21.95 ? 100 LEU B CG 1 ATOM 1481 C CD1 . LEU B 2 23 ? 51.198 23.387 40.360 1.00 26.20 ? 100 LEU B CD1 1 ATOM 1482 C CD2 . LEU B 2 23 ? 49.640 21.998 41.797 1.00 21.94 ? 100 LEU B CD2 1 ATOM 1483 N N . THR B 2 24 ? 46.364 21.994 37.464 1.00 18.97 ? 101 THR B N 1 ATOM 1484 C CA . THR B 2 24 ? 45.168 22.495 36.781 1.00 18.80 ? 101 THR B CA 1 ATOM 1485 C C . THR B 2 24 ? 43.858 21.843 37.235 1.00 17.30 ? 101 THR B C 1 ATOM 1486 O O . THR B 2 24 ? 42.782 22.386 36.973 1.00 17.82 ? 101 THR B O 1 ATOM 1487 C CB . THR B 2 24 ? 45.266 22.322 35.259 1.00 20.97 ? 101 THR B CB 1 ATOM 1488 O OG1 . THR B 2 24 ? 45.662 20.984 34.982 1.00 21.62 ? 101 THR B OG1 1 ATOM 1489 C CG2 . THR B 2 24 ? 46.304 23.279 34.680 1.00 23.10 ? 101 THR B CG2 1 ATOM 1490 N N . GLN B 2 25 ? 43.938 20.697 37.914 1.00 15.06 ? 102 GLN B N 1 ATOM 1491 C CA . GLN B 2 25 ? 42.701 20.021 38.345 1.00 13.99 ? 102 GLN B CA 1 ATOM 1492 C C . GLN B 2 25 ? 42.099 20.750 39.540 1.00 12.49 ? 102 GLN B C 1 ATOM 1493 O O . GLN B 2 25 ? 42.799 21.471 40.257 1.00 13.41 ? 102 GLN B O 1 ATOM 1494 C CB . GLN B 2 25 ? 42.928 18.567 38.718 1.00 14.40 ? 102 GLN B CB 1 ATOM 1495 C CG . GLN B 2 25 ? 43.471 18.376 40.187 1.00 14.49 ? 102 GLN B CG 1 ATOM 1496 C CD . GLN B 2 25 ? 43.805 16.921 40.448 1.00 15.10 ? 102 GLN B CD 1 ATOM 1497 O OE1 . GLN B 2 25 ? 44.686 16.356 39.781 1.00 17.26 ? 102 GLN B OE1 1 ATOM 1498 N NE2 . GLN B 2 25 ? 43.086 16.288 41.385 1.00 14.64 ? 102 GLN B NE2 1 ATOM 1499 N N . THR B 2 26 ? 40.811 20.563 39.753 1.00 13.17 ? 103 THR B N 1 ATOM 1500 C CA . THR B 2 26 ? 40.147 21.240 40.853 1.00 12.51 ? 103 THR B CA 1 ATOM 1501 C C . THR B 2 26 ? 40.345 20.556 42.210 1.00 13.03 ? 103 THR B C 1 ATOM 1502 O O . THR B 2 26 ? 40.720 19.375 42.307 1.00 13.42 ? 103 THR B O 1 ATOM 1503 C CB . THR B 2 26 ? 38.613 21.331 40.617 1.00 13.03 ? 103 THR B CB 1 ATOM 1504 O OG1 . THR B 2 26 ? 38.110 19.989 40.503 1.00 14.95 ? 103 THR B OG1 1 ATOM 1505 C CG2 . THR B 2 26 ? 38.234 22.179 39.363 1.00 12.84 ? 103 THR B CG2 1 ATOM 1506 N N . VAL B 2 27 ? 40.089 21.332 43.258 1.00 10.70 ? 104 VAL B N 1 ATOM 1507 C CA . VAL B 2 27 ? 40.051 20.780 44.608 1.00 11.20 ? 104 VAL B CA 1 ATOM 1508 C C . VAL B 2 27 ? 38.984 19.685 44.674 1.00 10.00 ? 104 VAL B C 1 ATOM 1509 O O . VAL B 2 27 ? 39.200 18.620 45.248 1.00 11.08 ? 104 VAL B O 1 ATOM 1510 C CB . VAL B 2 27 ? 39.747 21.897 45.627 1.00 11.00 ? 104 VAL B CB 1 ATOM 1511 C CG1 . VAL B 2 27 ? 39.324 21.332 47.000 1.00 10.94 ? 104 VAL B CG1 1 ATOM 1512 C CG2 . VAL B 2 27 ? 40.950 22.837 45.793 1.00 13.04 ? 104 VAL B CG2 1 ATOM 1513 N N . ALA B 2 28 ? 37.843 19.932 44.030 1.00 11.56 ? 105 ALA B N 1 ATOM 1514 C CA . ALA B 2 28 ? 36.784 18.937 43.989 1.00 12.53 ? 105 ALA B CA 1 ATOM 1515 C C . ALA B 2 28 ? 37.274 17.617 43.417 1.00 11.64 ? 105 ALA B C 1 ATOM 1516 O O . ALA B 2 28 ? 36.914 16.522 43.892 1.00 13.92 ? 105 ALA B O 1 ATOM 1517 C CB . ALA B 2 28 ? 35.568 19.461 43.172 1.00 15.25 ? 105 ALA B CB 1 ATOM 1518 N N . HIS B 2 29 ? 38.083 17.684 42.380 1.00 10.10 ? 106 HIS B N 1 ATOM 1519 C CA . HIS B 2 29 ? 38.562 16.425 41.787 1.00 10.88 ? 106 HIS B CA 1 ATOM 1520 C C . HIS B 2 29 ? 39.572 15.705 42.710 1.00 10.77 ? 106 HIS B C 1 ATOM 1521 O O . HIS B 2 29 ? 39.580 14.472 42.792 1.00 11.33 ? 106 HIS B O 1 ATOM 1522 C CB . HIS B 2 29 ? 39.248 16.725 40.464 1.00 12.05 ? 106 HIS B CB 1 ATOM 1523 C CG . HIS B 2 29 ? 39.518 15.517 39.644 1.00 16.41 ? 106 HIS B CG 1 ATOM 1524 N ND1 . HIS B 2 29 ? 38.534 14.613 39.306 1.00 18.66 ? 106 HIS B ND1 1 ATOM 1525 C CD2 . HIS B 2 29 ? 40.654 15.079 39.066 1.00 17.78 ? 106 HIS B CD2 1 ATOM 1526 C CE1 . HIS B 2 29 ? 39.057 13.660 38.543 1.00 19.89 ? 106 HIS B CE1 1 ATOM 1527 N NE2 . HIS B 2 29 ? 40.347 13.918 38.392 1.00 17.40 ? 106 HIS B NE2 1 ATOM 1528 N N . LEU B 2 30 ? 40.415 16.483 43.414 1.00 11.45 ? 107 LEU B N 1 ATOM 1529 C CA . LEU B 2 30 ? 41.276 15.867 44.437 1.00 10.72 ? 107 LEU B CA 1 ATOM 1530 C C . LEU B 2 30 ? 40.392 15.200 45.536 1.00 12.92 ? 107 LEU B C 1 ATOM 1531 O O . LEU B 2 30 ? 40.677 14.077 45.974 1.00 11.94 ? 107 LEU B O 1 ATOM 1532 C CB . LEU B 2 30 ? 42.226 16.916 45.035 1.00 11.75 ? 107 LEU B CB 1 ATOM 1533 C CG . LEU B 2 30 ? 43.040 16.448 46.237 1.00 10.57 ? 107 LEU B CG 1 ATOM 1534 C CD1 . LEU B 2 30 ? 43.893 15.199 45.887 1.00 12.17 ? 107 LEU B CD1 1 ATOM 1535 C CD2 . LEU B 2 30 ? 43.910 17.600 46.786 1.00 11.55 ? 107 LEU B CD2 1 ATOM 1536 N N . LYS B 2 31 ? 39.332 15.888 45.952 1.00 13.47 ? 108 LYS B N 1 ATOM 1537 C CA . LYS B 2 31 ? 38.412 15.278 46.909 1.00 11.53 ? 108 LYS B CA 1 ATOM 1538 C C . LYS B 2 31 ? 37.834 13.945 46.383 1.00 11.64 ? 108 LYS B C 1 ATOM 1539 O O . LYS B 2 31 ? 37.665 12.986 47.160 1.00 11.88 ? 108 LYS B O 1 ATOM 1540 C CB . LYS B 2 31 ? 37.265 16.221 47.297 1.00 12.55 ? 108 LYS B CB 1 ATOM 1541 C CG . LYS B 2 31 ? 37.709 17.459 48.080 1.00 12.56 ? 108 LYS B CG 1 ATOM 1542 C CD . LYS B 2 31 ? 36.544 18.309 48.521 1.00 13.97 ? 108 LYS B CD 1 ATOM 1543 C CE . LYS B 2 31 ? 35.678 17.587 49.514 1.00 14.47 ? 108 LYS B CE 1 ATOM 1544 N NZ . LYS B 2 31 ? 34.410 18.336 49.871 1.00 11.28 ? 108 LYS B NZ 1 ATOM 1545 N N . GLN B 2 32 ? 37.549 13.866 45.077 1.00 12.18 ? 109 GLN B N 1 ATOM 1546 C CA . GLN B 2 32 ? 37.070 12.584 44.515 1.00 12.81 ? 109 GLN B CA 1 ATOM 1547 C C . GLN B 2 32 ? 38.121 11.480 44.612 1.00 13.09 ? 109 GLN B C 1 ATOM 1548 O O . GLN B 2 32 ? 37.788 10.327 44.876 1.00 13.86 ? 109 GLN B O 1 ATOM 1549 C CB . GLN B 2 32 ? 36.617 12.725 43.059 1.00 11.69 ? 109 GLN B CB 1 ATOM 1550 C CG . GLN B 2 32 ? 35.369 13.652 42.887 1.00 13.21 ? 109 GLN B CG 1 ATOM 1551 C CD . GLN B 2 32 ? 35.091 13.950 41.422 1.00 14.62 ? 109 GLN B CD 1 ATOM 1552 O OE1 . GLN B 2 32 ? 35.996 14.395 40.689 1.00 15.13 ? 109 GLN B OE1 1 ATOM 1553 N NE2 . GLN B 2 32 ? 33.845 13.728 40.979 1.00 16.69 ? 109 GLN B NE2 1 ATOM 1554 N N . GLN B 2 33 ? 39.391 11.821 44.391 1.00 11.87 ? 110 GLN B N 1 ATOM 1555 C CA . GLN B 2 33 ? 40.469 10.827 44.550 1.00 11.27 ? 110 GLN B CA 1 ATOM 1556 C C . GLN B 2 33 ? 40.590 10.392 46.007 1.00 13.86 ? 110 GLN B C 1 ATOM 1557 O O . GLN B 2 33 ? 40.691 9.208 46.301 1.00 16.02 ? 110 GLN B O 1 ATOM 1558 C CB . GLN B 2 33 ? 41.821 11.397 44.122 1.00 12.39 ? 110 GLN B CB 1 ATOM 1559 C CG . GLN B 2 33 ? 41.899 11.789 42.641 1.00 16.20 ? 110 GLN B CG 1 ATOM 1560 C CD . GLN B 2 33 ? 43.255 12.463 42.363 1.00 20.40 ? 110 GLN B CD 1 ATOM 1561 O OE1 . GLN B 2 33 ? 44.291 11.809 42.250 1.00 24.52 ? 110 GLN B OE1 1 ATOM 1562 N NE2 . GLN B 2 33 ? 43.260 13.750 42.354 1.00 19.36 ? 110 GLN B NE2 1 ATOM 1563 N N . VAL B 2 34 ? 40.553 11.362 46.912 1.00 12.57 ? 111 VAL B N 1 ATOM 1564 C CA . VAL B 2 34 ? 40.669 11.069 48.360 1.00 12.71 ? 111 VAL B CA 1 ATOM 1565 C C . VAL B 2 34 ? 39.465 10.252 48.797 1.00 13.49 ? 111 VAL B C 1 ATOM 1566 O O . VAL B 2 34 ? 39.602 9.298 49.561 1.00 13.26 ? 111 VAL B O 1 ATOM 1567 C CB . VAL B 2 34 ? 40.726 12.358 49.174 1.00 11.85 ? 111 VAL B CB 1 ATOM 1568 C CG1 . VAL B 2 34 ? 40.581 12.095 50.674 1.00 13.73 ? 111 VAL B CG1 1 ATOM 1569 C CG2 . VAL B 2 34 ? 42.013 13.136 48.871 1.00 11.94 ? 111 VAL B CG2 1 ATOM 1570 N N . SER B 2 35 ? 38.275 10.601 48.302 1.00 13.18 ? 112 SER B N 1 ATOM 1571 C CA . SER B 2 35 ? 37.057 9.802 48.603 1.00 14.08 ? 112 SER B CA 1 ATOM 1572 C C . SER B 2 35 ? 37.195 8.337 48.190 1.00 14.09 ? 112 SER B C 1 ATOM 1573 O O . SER B 2 35 ? 36.810 7.411 48.929 1.00 14.69 ? 112 SER B O 1 ATOM 1574 C CB . SER B 2 35 ? 35.848 10.446 47.920 1.00 14.42 ? 112 SER B CB 1 ATOM 1575 O OG . SER B 2 35 ? 34.705 9.625 48.030 1.00 14.69 ? 112 SER B OG 1 ATOM 1576 N N . GLY B 2 36 ? 37.788 8.106 47.018 1.00 13.45 ? 113 GLY B N 1 ATOM 1577 C CA . GLY B 2 36 ? 38.014 6.733 46.582 1.00 12.28 ? 113 GLY B CA 1 ATOM 1578 C C . GLY B 2 36 ? 39.040 5.975 47.425 1.00 13.97 ? 113 GLY B C 1 ATOM 1579 O O . GLY B 2 36 ? 38.820 4.826 47.819 1.00 17.01 ? 113 GLY B O 1 ATOM 1580 N N . LEU B 2 37 ? 40.164 6.616 47.710 1.00 13.03 ? 114 LEU B N 1 ATOM 1581 C CA . LEU B 2 37 ? 41.206 5.966 48.541 1.00 13.47 ? 114 LEU B CA 1 ATOM 1582 C C . LEU B 2 37 ? 40.755 5.717 49.979 1.00 15.62 ? 114 LEU B C 1 ATOM 1583 O O . LEU B 2 37 ? 40.968 4.607 50.524 1.00 17.28 ? 114 LEU B O 1 ATOM 1584 C CB . LEU B 2 37 ? 42.497 6.780 48.521 1.00 14.93 ? 114 LEU B CB 1 ATOM 1585 C CG . LEU B 2 37 ? 43.727 6.164 49.220 1.00 18.77 ? 114 LEU B CG 1 ATOM 1586 C CD1 . LEU B 2 37 ? 45.040 6.598 48.555 1.00 21.39 ? 114 LEU B CD1 1 ATOM 1587 C CD2 . LEU B 2 37 ? 43.698 6.501 50.741 1.00 18.69 ? 114 LEU B CD2 1 ATOM 1588 N N . GLU B 2 38 ? 40.147 6.727 50.592 1.00 15.00 ? 115 GLU B N 1 ATOM 1589 C CA . GLU B 2 38 ? 39.783 6.649 52.029 1.00 14.85 ? 115 GLU B CA 1 ATOM 1590 C C . GLU B 2 38 ? 38.394 6.023 52.272 1.00 16.99 ? 115 GLU B C 1 ATOM 1591 O O . GLU B 2 38 ? 38.066 5.639 53.401 1.00 19.47 ? 115 GLU B O 1 ATOM 1592 C CB . GLU B 2 38 ? 39.841 8.057 52.598 1.00 16.33 ? 115 GLU B CB 1 ATOM 1593 C CG . GLU B 2 38 ? 41.234 8.689 52.549 1.00 16.90 ? 115 GLU B CG 1 ATOM 1594 C CD . GLU B 2 38 ? 42.190 8.129 53.601 1.00 18.82 ? 115 GLU B CD 1 ATOM 1595 O OE1 . GLU B 2 38 ? 41.805 7.239 54.396 1.00 19.72 ? 115 GLU B OE1 1 ATOM 1596 O OE2 . GLU B 2 38 ? 43.352 8.563 53.606 1.00 20.12 ? 115 GLU B OE2 1 ATOM 1597 N N . GLY B 2 39 ? 37.558 5.913 51.229 1.00 16.25 ? 116 GLY B N 1 ATOM 1598 C CA . GLY B 2 39 ? 36.245 5.274 51.388 1.00 16.37 ? 116 GLY B CA 1 ATOM 1599 C C . GLY B 2 39 ? 35.275 6.151 52.178 1.00 17.05 ? 116 GLY B C 1 ATOM 1600 O O . GLY B 2 39 ? 34.443 5.646 52.948 1.00 20.39 ? 116 GLY B O 1 ATOM 1601 N N . VAL B 2 40 ? 35.376 7.468 52.002 1.00 15.82 ? 117 VAL B N 1 ATOM 1602 C CA . VAL B 2 40 ? 34.488 8.395 52.691 1.00 14.61 ? 117 VAL B CA 1 ATOM 1603 C C . VAL B 2 40 ? 33.859 9.294 51.622 1.00 13.59 ? 117 VAL B C 1 ATOM 1604 O O . VAL B 2 40 ? 34.583 9.791 50.750 1.00 13.60 ? 117 VAL B O 1 ATOM 1605 C CB . VAL B 2 40 ? 35.281 9.324 53.681 1.00 14.24 ? 117 VAL B CB 1 ATOM 1606 C CG1 . VAL B 2 40 ? 34.355 10.410 54.316 1.00 15.65 ? 117 VAL B CG1 1 ATOM 1607 C CG2 . VAL B 2 40 ? 35.933 8.490 54.777 1.00 15.53 ? 117 VAL B CG2 1 ATOM 1608 N N . GLN B 2 41 ? 32.555 9.535 51.707 1.00 13.64 ? 118 GLN B N 1 ATOM 1609 C CA . GLN B 2 41 ? 31.866 10.378 50.709 1.00 16.15 ? 118 GLN B CA 1 ATOM 1610 C C . GLN B 2 41 ? 32.465 11.786 50.676 1.00 15.77 ? 118 GLN B C 1 ATOM 1611 O O . GLN B 2 41 ? 32.845 12.353 51.713 1.00 14.41 ? 118 GLN B O 1 ATOM 1612 C CB . GLN B 2 41 ? 30.349 10.452 50.995 1.00 17.37 ? 118 GLN B CB 1 ATOM 1613 C CG . GLN B 2 41 ? 29.690 9.129 50.975 1.00 22.50 ? 118 GLN B CG 1 ATOM 1614 C CD . GLN B 2 41 ? 28.288 9.183 51.553 0.0000 25.72 ? 118 GLN B CD 1 ATOM 1615 O OE1 . GLN B 2 41 ? 27.825 10.237 51.990 0.0000 26.87 ? 118 GLN B OE1 1 ATOM 1616 N NE2 . GLN B 2 41 ? 27.606 8.044 51.562 0.0000 26.87 ? 118 GLN B NE2 1 ATOM 1617 N N . ASP B 2 42 ? 32.561 12.362 49.476 1.00 13.99 ? 119 ASP B N 1 ATOM 1618 C CA . ASP B 2 42 ? 33.216 13.660 49.350 1.00 14.93 ? 119 ASP B CA 1 ATOM 1619 C C . ASP B 2 42 ? 32.419 14.826 49.938 1.00 15.69 ? 119 ASP B C 1 ATOM 1620 O O . ASP B 2 42 ? 32.977 15.918 50.082 1.00 16.59 ? 119 ASP B O 1 ATOM 1621 C CB . ASP B 2 42 ? 33.643 13.935 47.897 1.00 16.11 ? 119 ASP B CB 1 ATOM 1622 C CG . ASP B 2 42 ? 32.465 13.990 46.937 1.00 19.22 ? 119 ASP B CG 1 ATOM 1623 O OD1 . ASP B 2 42 ? 31.323 14.171 47.374 1.00 23.04 ? 119 ASP B OD1 1 ATOM 1624 O OD2 . ASP B 2 42 ? 32.698 13.851 45.729 1.00 22.94 ? 119 ASP B OD2 1 ATOM 1625 N N . ASP B 2 43 ? 31.146 14.604 50.316 1.00 14.71 ? 120 ASP B N 1 ATOM 1626 C CA . ASP B 2 43 ? 30.429 15.635 51.079 1.00 15.81 ? 120 ASP B CA 1 ATOM 1627 C C . ASP B 2 43 ? 30.542 15.419 52.608 1.00 15.71 ? 120 ASP B C 1 ATOM 1628 O O . ASP B 2 43 ? 29.880 16.113 53.430 1.00 14.78 ? 120 ASP B O 1 ATOM 1629 C CB . ASP B 2 43 ? 28.977 15.745 50.632 1.00 20.32 ? 120 ASP B CB 1 ATOM 1630 C CG . ASP B 2 43 ? 28.162 14.524 50.957 1.00 24.11 ? 120 ASP B CG 1 ATOM 1631 O OD1 . ASP B 2 43 ? 28.718 13.481 51.359 1.00 23.13 ? 120 ASP B OD1 1 ATOM 1632 O OD2 . ASP B 2 43 ? 26.929 14.616 50.789 1.00 28.70 ? 120 ASP B OD2 1 ATOM 1633 N N . LEU B 2 44 ? 31.406 14.494 52.996 1.00 13.74 ? 121 LEU B N 1 ATOM 1634 C CA . LEU B 2 44 ? 31.618 14.280 54.430 1.00 12.22 ? 121 LEU B CA 1 ATOM 1635 C C . LEU B 2 44 ? 33.052 14.637 54.836 1.00 14.01 ? 121 LEU B C 1 ATOM 1636 O O . LEU B 2 44 ? 33.513 14.218 55.869 1.00 13.69 ? 121 LEU B O 1 ATOM 1637 C CB . LEU B 2 44 ? 31.273 12.840 54.829 1.00 14.66 ? 121 LEU B CB 1 ATOM 1638 C CG . LEU B 2 44 ? 29.771 12.609 54.857 1.00 15.39 ? 121 LEU B CG 1 ATOM 1639 C CD1 . LEU B 2 44 ? 29.434 11.116 55.117 1.00 16.77 ? 121 LEU B CD1 1 ATOM 1640 C CD2 . LEU B 2 44 ? 29.049 13.544 55.868 1.00 19.92 ? 121 LEU B CD2 1 ATOM 1641 N N . PHE B 2 45 ? 33.764 15.402 54.015 1.00 12.51 ? 122 PHE B N 1 ATOM 1642 C CA . PHE B 2 45 ? 35.059 15.945 54.431 1.00 10.32 ? 122 PHE B CA 1 ATOM 1643 C C . PHE B 2 45 ? 35.421 17.179 53.645 1.00 10.55 ? 122 PHE B C 1 ATOM 1644 O O . PHE B 2 45 ? 34.838 17.423 52.608 1.00 11.93 ? 122 PHE B O 1 ATOM 1645 C CB . PHE B 2 45 ? 36.197 14.899 54.340 1.00 11.58 ? 122 PHE B CB 1 ATOM 1646 C CG . PHE B 2 45 ? 36.514 14.421 52.920 1.00 12.20 ? 122 PHE B CG 1 ATOM 1647 C CD1 . PHE B 2 45 ? 37.451 15.096 52.155 1.00 11.74 ? 122 PHE B CD1 1 ATOM 1648 C CD2 . PHE B 2 45 ? 35.862 13.333 52.386 1.00 11.47 ? 122 PHE B CD2 1 ATOM 1649 C CE1 . PHE B 2 45 ? 37.771 14.678 50.855 1.00 9.11 ? 122 PHE B CE1 1 ATOM 1650 C CE2 . PHE B 2 45 ? 36.136 12.881 51.073 1.00 9.86 ? 122 PHE B CE2 1 ATOM 1651 C CZ . PHE B 2 45 ? 37.117 13.544 50.315 1.00 9.94 ? 122 PHE B CZ 1 ATOM 1652 N N . TRP B 2 46 ? 36.353 17.966 54.169 1.00 11.04 ? 123 TRP B N 1 ATOM 1653 C CA . TRP B 2 46 ? 36.837 19.119 53.458 1.00 12.46 ? 123 TRP B CA 1 ATOM 1654 C C . TRP B 2 46 ? 38.347 19.197 53.608 1.00 13.28 ? 123 TRP B C 1 ATOM 1655 O O . TRP B 2 46 ? 38.922 18.616 54.519 1.00 13.04 ? 123 TRP B O 1 ATOM 1656 C CB . TRP B 2 46 ? 36.139 20.418 53.960 1.00 11.64 ? 123 TRP B CB 1 ATOM 1657 C CG . TRP B 2 46 ? 36.232 20.640 55.453 1.00 11.42 ? 123 TRP B CG 1 ATOM 1658 C CD1 . TRP B 2 46 ? 35.628 19.885 56.447 1.00 12.28 ? 123 TRP B CD1 1 ATOM 1659 C CD2 . TRP B 2 46 ? 36.988 21.660 56.117 1.00 11.92 ? 123 TRP B CD2 1 ATOM 1660 N NE1 . TRP B 2 46 ? 35.958 20.414 57.690 1.00 12.38 ? 123 TRP B NE1 1 ATOM 1661 C CE2 . TRP B 2 46 ? 36.775 21.501 57.517 1.00 11.75 ? 123 TRP B CE2 1 ATOM 1662 C CE3 . TRP B 2 46 ? 37.791 22.713 55.670 1.00 12.61 ? 123 TRP B CE3 1 ATOM 1663 C CZ2 . TRP B 2 46 ? 37.379 22.331 58.472 1.00 13.76 ? 123 TRP B CZ2 1 ATOM 1664 C CZ3 . TRP B 2 46 ? 38.383 23.562 56.641 1.00 13.22 ? 123 TRP B CZ3 1 ATOM 1665 C CH2 . TRP B 2 46 ? 38.149 23.373 58.013 1.00 14.07 ? 123 TRP B CH2 1 ATOM 1666 N N . LEU B 2 47 ? 38.999 19.904 52.695 1.00 11.40 ? 124 LEU B N 1 ATOM 1667 C CA . LEU B 2 47 ? 40.462 19.907 52.677 1.00 10.06 ? 124 LEU B CA 1 ATOM 1668 C C . LEU B 2 47 ? 41.040 21.240 53.106 1.00 11.53 ? 124 LEU B C 1 ATOM 1669 O O . LEU B 2 47 ? 40.437 22.284 52.855 1.00 12.49 ? 124 LEU B O 1 ATOM 1670 C CB . LEU B 2 47 ? 40.980 19.571 51.254 1.00 9.92 ? 124 LEU B CB 1 ATOM 1671 C CG . LEU B 2 47 ? 40.529 18.228 50.657 1.00 10.30 ? 124 LEU B CG 1 ATOM 1672 C CD1 . LEU B 2 47 ? 41.183 18.043 49.223 1.00 10.55 ? 124 LEU B CD1 1 ATOM 1673 C CD2 . LEU B 2 47 ? 40.853 17.001 51.540 1.00 11.93 ? 124 LEU B CD2 1 ATOM 1674 N N . THR B 2 48 ? 42.222 21.191 53.744 1.00 12.03 ? 125 THR B N 1 ATOM 1675 C CA . THR B 2 48 ? 42.951 22.405 54.069 1.00 11.49 ? 125 THR B CA 1 ATOM 1676 C C . THR B 2 48 ? 44.400 22.308 53.681 1.00 12.25 ? 125 THR B C 1 ATOM 1677 O O . THR B 2 48 ? 44.941 21.215 53.598 1.00 14.27 ? 125 THR B O 1 ATOM 1678 C CB . THR B 2 48 ? 42.891 22.750 55.570 1.00 11.98 ? 125 THR B CB 1 ATOM 1679 O OG1 . THR B 2 48 ? 43.319 21.610 56.334 1.00 14.44 ? 125 THR B OG1 1 ATOM 1680 C CG2 . THR B 2 48 ? 41.475 23.146 56.002 1.00 11.49 ? 125 THR B CG2 1 ATOM 1681 N N . PHE B 2 49 ? 45.001 23.460 53.405 1.00 11.75 ? 126 PHE B N 1 ATOM 1682 C CA . PHE B 2 49 ? 46.445 23.526 53.187 1.00 12.43 ? 126 PHE B CA 1 ATOM 1683 C C . PHE B 2 49 ? 46.965 24.753 53.885 1.00 13.29 ? 126 PHE B C 1 ATOM 1684 O O . PHE B 2 49 ? 46.512 25.862 53.633 1.00 13.79 ? 126 PHE B O 1 ATOM 1685 C CB . PHE B 2 49 ? 46.764 23.585 51.678 1.00 13.46 ? 126 PHE B CB 1 ATOM 1686 C CG . PHE B 2 49 ? 48.227 23.655 51.366 1.00 14.48 ? 126 PHE B CG 1 ATOM 1687 C CD1 . PHE B 2 49 ? 49.088 22.650 51.778 1.00 16.07 ? 126 PHE B CD1 1 ATOM 1688 C CD2 . PHE B 2 49 ? 48.764 24.765 50.665 1.00 14.75 ? 126 PHE B CD2 1 ATOM 1689 C CE1 . PHE B 2 49 ? 50.453 22.730 51.495 1.00 17.64 ? 126 PHE B CE1 1 ATOM 1690 C CE2 . PHE B 2 49 ? 50.130 24.824 50.342 1.00 16.45 ? 126 PHE B CE2 1 ATOM 1691 C CZ . PHE B 2 49 ? 50.970 23.823 50.787 1.00 16.28 ? 126 PHE B CZ 1 ATOM 1692 N N . GLU B 2 50 ? 47.952 24.528 54.762 1.00 15.81 ? 127 GLU B N 1 ATOM 1693 C CA . GLU B 2 50 ? 48.596 25.595 55.499 1.00 19.72 ? 127 GLU B CA 1 ATOM 1694 C C . GLU B 2 50 ? 47.583 26.541 56.156 1.00 19.25 ? 127 GLU B C 1 ATOM 1695 O O . GLU B 2 50 ? 47.737 27.756 56.085 1.00 22.42 ? 127 GLU B O 1 ATOM 1696 C CB . GLU B 2 50 ? 49.598 26.354 54.614 1.00 22.19 ? 127 GLU B CB 1 ATOM 1697 C CG . GLU B 2 50 ? 50.713 25.442 54.063 1.00 23.83 ? 127 GLU B CG 1 ATOM 1698 C CD . GLU B 2 50 ? 51.773 26.189 53.285 1.00 27.41 ? 127 GLU B CD 1 ATOM 1699 O OE1 . GLU B 2 50 ? 51.490 27.264 52.694 1.00 30.64 ? 127 GLU B OE1 1 ATOM 1700 O OE2 . GLU B 2 50 ? 52.900 25.677 53.242 1.00 29.41 ? 127 GLU B OE2 1 ATOM 1701 N N . GLY B 2 51 ? 46.550 25.968 56.782 1.00 17.18 ? 128 GLY B N 1 ATOM 1702 C CA . GLY B 2 51 ? 45.593 26.746 57.546 1.00 16.82 ? 128 GLY B CA 1 ATOM 1703 C C . GLY B 2 51 ? 44.488 27.404 56.742 1.00 17.86 ? 128 GLY B C 1 ATOM 1704 O O . GLY B 2 51 ? 43.722 28.178 57.275 1.00 20.99 ? 128 GLY B O 1 ATOM 1705 N N . LYS B 2 52 ? 44.413 27.111 55.452 1.00 16.05 ? 129 LYS B N 1 ATOM 1706 C CA . LYS B 2 52 ? 43.422 27.694 54.560 1.00 17.25 ? 129 LYS B CA 1 ATOM 1707 C C . LYS B 2 52 ? 42.517 26.589 54.027 1.00 14.27 ? 129 LYS B C 1 ATOM 1708 O O . LYS B 2 52 ? 42.996 25.554 53.563 1.00 15.28 ? 129 LYS B O 1 ATOM 1709 C CB . LYS B 2 52 ? 44.122 28.368 53.375 1.00 24.36 ? 129 LYS B CB 1 ATOM 1710 C CG . LYS B 2 52 ? 44.778 29.676 53.707 1.00 33.33 ? 129 LYS B CG 1 ATOM 1711 C CD . LYS B 2 52 ? 45.047 30.450 52.385 1.00 39.00 ? 129 LYS B CD 1 ATOM 1712 C CE . LYS B 2 52 ? 46.289 29.964 51.672 1.00 42.15 ? 129 LYS B CE 1 ATOM 1713 N NZ . LYS B 2 52 ? 46.418 28.470 51.606 1.00 43.07 ? 129 LYS B NZ 1 ATOM 1714 N N . PRO B 2 53 ? 41.192 26.794 54.121 1.00 13.90 ? 130 PRO B N 1 ATOM 1715 C CA . PRO B 2 53 ? 40.303 25.842 53.459 1.00 14.59 ? 130 PRO B CA 1 ATOM 1716 C C . PRO B 2 53 ? 40.513 25.849 51.926 1.00 15.78 ? 130 PRO B C 1 ATOM 1717 O O . PRO B 2 53 ? 40.732 26.917 51.321 1.00 16.24 ? 130 PRO B O 1 ATOM 1718 C CB . PRO B 2 53 ? 38.901 26.389 53.778 1.00 15.59 ? 130 PRO B CB 1 ATOM 1719 C CG . PRO B 2 53 ? 39.068 27.377 54.861 1.00 14.59 ? 130 PRO B CG 1 ATOM 1720 C CD . PRO B 2 53 ? 40.464 27.893 54.785 1.00 12.67 ? 130 PRO B CD 1 ATOM 1721 N N . LEU B 2 54 ? 40.426 24.679 51.326 1.00 14.21 ? 131 LEU B N 1 ATOM 1722 C CA . LEU B 2 54 ? 40.518 24.574 49.854 1.00 13.40 ? 131 LEU B CA 1 ATOM 1723 C C . LEU B 2 54 ? 39.120 24.627 49.306 1.00 13.38 ? 131 LEU B C 1 ATOM 1724 O O . LEU B 2 54 ? 38.245 23.887 49.796 1.00 14.79 ? 131 LEU B O 1 ATOM 1725 C CB . LEU B 2 54 ? 41.169 23.256 49.456 1.00 12.10 ? 131 LEU B CB 1 ATOM 1726 C CG . LEU B 2 54 ? 42.599 23.068 49.983 1.00 14.63 ? 131 LEU B CG 1 ATOM 1727 C CD1 . LEU B 2 54 ? 43.227 21.855 49.258 1.00 15.99 ? 131 LEU B CD1 1 ATOM 1728 C CD2 . LEU B 2 54 ? 43.442 24.342 49.768 1.00 16.63 ? 131 LEU B CD2 1 ATOM 1729 N N . GLU B 2 55 ? 38.870 25.510 48.343 1.00 11.26 ? 132 GLU B N 1 ATOM 1730 C CA . GLU B 2 55 ? 37.520 25.630 47.760 1.00 11.33 ? 132 GLU B CA 1 ATOM 1731 C C . GLU B 2 55 ? 37.358 24.706 46.559 1.00 12.39 ? 132 GLU B C 1 ATOM 1732 O O . GLU B 2 55 ? 38.195 24.713 45.639 1.00 12.70 ? 132 GLU B O 1 ATOM 1733 C CB . GLU B 2 55 ? 37.279 27.060 47.315 1.00 14.52 ? 132 GLU B CB 1 ATOM 1734 C CG . GLU B 2 55 ? 37.271 28.040 48.449 1.00 19.44 ? 132 GLU B CG 1 ATOM 1735 C CD . GLU B 2 55 ? 37.000 29.449 47.922 1.00 25.17 ? 132 GLU B CD 1 ATOM 1736 O OE1 . GLU B 2 55 ? 35.930 29.674 47.346 1.00 26.42 ? 132 GLU B OE1 1 ATOM 1737 O OE2 . GLU B 2 55 ? 37.873 30.305 48.037 1.00 29.88 ? 132 GLU B OE2 1 ATOM 1738 N N . ASP B 2 56 ? 36.277 23.935 46.566 1.00 14.55 ? 133 ASP B N 1 ATOM 1739 C CA . ASP B 2 56 ? 36.017 22.877 45.596 1.00 13.55 ? 133 ASP B CA 1 ATOM 1740 C C . ASP B 2 56 ? 36.271 23.306 44.116 1.00 13.00 ? 133 ASP B C 1 ATOM 1741 O O . ASP B 2 56 ? 36.885 22.572 43.357 1.00 13.35 ? 133 ASP B O 1 ATOM 1742 C CB . ASP B 2 56 ? 34.535 22.473 45.716 1.00 16.28 ? 133 ASP B CB 1 ATOM 1743 C CG . ASP B 2 56 ? 34.250 21.710 46.945 1.00 23.24 ? 133 ASP B CG 1 ATOM 1744 O OD1 . ASP B 2 56 ? 35.029 21.816 47.898 1.00 27.85 ? 133 ASP B OD1 1 ATOM 1745 O OD2 . ASP B 2 56 ? 33.231 21.003 46.979 1.00 27.11 ? 133 ASP B OD2 1 ATOM 1746 N N . GLN B 2 57 ? 35.786 24.477 43.726 1.00 14.00 ? 134 GLN B N 1 ATOM 1747 C CA . GLN B 2 57 ? 35.818 24.884 42.309 1.00 15.99 ? 134 GLN B CA 1 ATOM 1748 C C . GLN B 2 57 ? 37.208 25.366 41.833 1.00 14.96 ? 134 GLN B C 1 ATOM 1749 O O . GLN B 2 57 ? 37.442 25.482 40.623 1.00 16.87 ? 134 GLN B O 1 ATOM 1750 C CB . GLN B 2 57 ? 34.789 25.993 42.050 1.00 19.01 ? 134 GLN B CB 1 ATOM 1751 C CG . GLN B 2 57 ? 34.434 26.138 40.593 1.00 23.70 ? 134 GLN B CG 1 ATOM 1752 C CD . GLN B 2 57 ? 33.035 26.679 40.402 0.0000 25.39 ? 134 GLN B CD 1 ATOM 1753 O OE1 . GLN B 2 57 ? 32.582 27.544 41.153 0.0000 26.03 ? 134 GLN B OE1 1 ATOM 1754 N NE2 . GLN B 2 57 ? 32.335 26.163 39.402 0.0000 26.02 ? 134 GLN B NE2 1 ATOM 1755 N N . LEU B 2 58 ? 38.128 25.631 42.754 1.00 12.60 ? 135 LEU B N 1 ATOM 1756 C CA . LEU B 2 58 ? 39.391 26.242 42.370 1.00 12.47 ? 135 LEU B CA 1 ATOM 1757 C C . LEU B 2 58 ? 40.409 25.188 41.951 1.00 13.32 ? 135 LEU B C 1 ATOM 1758 O O . LEU B 2 58 ? 40.428 24.080 42.477 1.00 14.78 ? 135 LEU B O 1 ATOM 1759 C CB . LEU B 2 58 ? 39.983 27.097 43.516 1.00 12.49 ? 135 LEU B CB 1 ATOM 1760 C CG . LEU B 2 58 ? 39.623 28.571 43.459 1.00 14.06 ? 135 LEU B CG 1 ATOM 1761 C CD1 . LEU B 2 58 ? 38.118 28.733 43.534 1.00 13.00 ? 135 LEU B CD1 1 ATOM 1762 C CD2 . LEU B 2 58 ? 40.304 29.350 44.554 1.00 15.59 ? 135 LEU B CD2 1 ATOM 1763 N N . PRO B 2 59 ? 41.271 25.523 40.971 1.00 13.05 ? 136 PRO B N 1 ATOM 1764 C CA . PRO B 2 59 ? 42.409 24.643 40.697 1.00 13.51 ? 136 PRO B CA 1 ATOM 1765 C C . PRO B 2 59 ? 43.407 24.566 41.859 1.00 12.11 ? 136 PRO B C 1 ATOM 1766 O O . PRO B 2 59 ? 43.613 25.542 42.579 1.00 13.34 ? 136 PRO B O 1 ATOM 1767 C CB . PRO B 2 59 ? 43.110 25.321 39.497 1.00 14.72 ? 136 PRO B CB 1 ATOM 1768 C CG . PRO B 2 59 ? 42.169 26.315 38.955 1.00 13.50 ? 136 PRO B CG 1 ATOM 1769 C CD . PRO B 2 59 ? 41.275 26.719 40.118 1.00 11.02 ? 136 PRO B CD 1 ATOM 1770 N N . LEU B 2 60 ? 44.028 23.393 42.025 1.00 12.21 ? 137 LEU B N 1 ATOM 1771 C CA . LEU B 2 60 ? 45.058 23.186 43.052 1.00 11.97 ? 137 LEU B CA 1 ATOM 1772 C C . LEU B 2 60 ? 46.188 24.216 43.000 1.00 14.47 ? 137 LEU B C 1 ATOM 1773 O O . LEU B 2 60 ? 46.759 24.622 44.045 1.00 14.07 ? 137 LEU B O 1 ATOM 1774 C CB . LEU B 2 60 ? 45.618 21.769 42.914 1.00 12.25 ? 137 LEU B CB 1 ATOM 1775 C CG . LEU B 2 60 ? 44.629 20.619 43.165 1.00 13.93 ? 137 LEU B CG 1 ATOM 1776 C CD1 . LEU B 2 60 ? 45.396 19.307 43.058 1.00 14.16 ? 137 LEU B CD1 1 ATOM 1777 C CD2 . LEU B 2 60 ? 43.863 20.722 44.532 1.00 16.29 ? 137 LEU B CD2 1 ATOM 1778 N N . GLY B 2 61 ? 46.559 24.612 41.781 1.00 15.29 ? 138 GLY B N 1 ATOM 1779 C CA . GLY B 2 61 ? 47.636 25.577 41.621 1.00 16.69 ? 138 GLY B CA 1 ATOM 1780 C C . GLY B 2 61 ? 47.375 26.941 42.228 1.00 16.07 ? 138 GLY B C 1 ATOM 1781 O O . GLY B 2 61 ? 48.318 27.705 42.401 1.00 19.51 ? 138 GLY B O 1 ATOM 1782 N N . GLU B 2 62 ? 46.127 27.262 42.568 1.00 13.34 ? 139 GLU B N 1 ATOM 1783 C CA . GLU B 2 62 ? 45.864 28.572 43.159 1.00 15.02 ? 139 GLU B CA 1 ATOM 1784 C C . GLU B 2 62 ? 46.383 28.620 44.584 1.00 15.61 ? 139 GLU B C 1 ATOM 1785 O O . GLU B 2 62 ? 46.484 29.699 45.173 1.00 18.78 ? 139 GLU B O 1 ATOM 1786 C CB . GLU B 2 62 ? 44.348 28.880 43.201 1.00 14.34 ? 139 GLU B CB 1 ATOM 1787 C CG . GLU B 2 62 ? 43.742 28.986 41.804 1.00 16.09 ? 139 GLU B CG 1 ATOM 1788 C CD . GLU B 2 62 ? 44.525 29.899 40.915 1.00 18.42 ? 139 GLU B CD 1 ATOM 1789 O OE1 . GLU B 2 62 ? 44.653 31.092 41.237 1.00 18.43 ? 139 GLU B OE1 1 ATOM 1790 O OE2 . GLU B 2 62 ? 45.042 29.423 39.891 1.00 24.39 ? 139 GLU B OE2 1 ATOM 1791 N N . TYR B 2 63 ? 46.717 27.449 45.130 1.00 14.76 ? 140 TYR B N 1 ATOM 1792 C CA . TYR B 2 63 ? 47.135 27.296 46.540 1.00 15.84 ? 140 TYR B CA 1 ATOM 1793 C C . TYR B 2 63 ? 48.612 27.102 46.729 1.00 18.99 ? 140 TYR B C 1 ATOM 1794 O O . TYR B 2 63 ? 49.060 27.014 47.867 1.00 21.52 ? 140 TYR B O 1 ATOM 1795 C CB . TYR B 2 63 ? 46.365 26.134 47.200 1.00 13.76 ? 140 TYR B CB 1 ATOM 1796 C CG . TYR B 2 63 ? 44.875 26.439 47.277 1.00 14.28 ? 140 TYR B CG 1 ATOM 1797 C CD1 . TYR B 2 63 ? 44.354 27.303 48.262 1.00 15.13 ? 140 TYR B CD1 1 ATOM 1798 C CD2 . TYR B 2 63 ? 43.987 25.925 46.332 1.00 14.11 ? 140 TYR B CD2 1 ATOM 1799 C CE1 . TYR B 2 63 ? 42.984 27.613 48.309 1.00 13.71 ? 140 TYR B CE1 1 ATOM 1800 C CE2 . TYR B 2 63 ? 42.623 26.226 46.380 1.00 14.14 ? 140 TYR B CE2 1 ATOM 1801 C CZ . TYR B 2 63 ? 42.131 27.065 47.371 1.00 13.60 ? 140 TYR B CZ 1 ATOM 1802 O OH . TYR B 2 63 ? 40.793 27.367 47.411 1.00 14.52 ? 140 TYR B OH 1 ATOM 1803 N N . GLY B 2 64 ? 49.371 27.041 45.630 1.00 19.30 ? 141 GLY B N 1 ATOM 1804 C CA . GLY B 2 64 ? 50.819 26.927 45.758 1.00 20.22 ? 141 GLY B CA 1 ATOM 1805 C C . GLY B 2 64 ? 51.284 25.565 46.252 1.00 21.68 ? 141 GLY B C 1 ATOM 1806 O O . GLY B 2 64 ? 52.319 25.464 46.890 1.00 24.40 ? 141 GLY B O 1 ATOM 1807 N N . LEU B 2 65 ? 50.525 24.514 45.992 1.00 19.84 ? 142 LEU B N 1 ATOM 1808 C CA . LEU B 2 65 ? 51.036 23.183 46.281 1.00 18.51 ? 142 LEU B CA 1 ATOM 1809 C C . LEU B 2 65 ? 52.325 22.872 45.535 1.00 20.06 ? 142 LEU B C 1 ATOM 1810 O O . LEU B 2 65 ? 52.511 23.294 44.370 1.00 23.19 ? 142 LEU B O 1 ATOM 1811 C CB . LEU B 2 65 ? 50.001 22.120 45.963 1.00 18.05 ? 142 LEU B CB 1 ATOM 1812 C CG . LEU B 2 65 ? 48.704 22.293 46.722 1.00 20.87 ? 142 LEU B CG 1 ATOM 1813 C CD1 . LEU B 2 65 ? 47.587 21.385 46.211 1.00 24.15 ? 142 LEU B CD1 1 ATOM 1814 C CD2 . LEU B 2 65 ? 48.953 22.030 48.137 1.00 21.88 ? 142 LEU B CD2 1 ATOM 1815 N N . LYS B 2 66 ? 53.201 22.116 46.200 1.00 19.19 ? 143 LYS B N 1 ATOM 1816 C CA . LYS B 2 66 ? 54.471 21.685 45.632 1.00 22.08 ? 143 LYS B CA 1 ATOM 1817 C C . LYS B 2 66 ? 54.579 20.169 45.772 1.00 21.86 ? 143 LYS B C 1 ATOM 1818 O O . LYS B 2 66 ? 53.783 19.535 46.462 1.00 20.96 ? 143 LYS B O 1 ATOM 1819 C CB . LYS B 2 66 ? 55.624 22.345 46.405 1.00 26.47 ? 143 LYS B CB 1 ATOM 1820 C CG . LYS B 2 66 ? 55.744 23.880 46.211 1.00 31.02 ? 143 LYS B CG 1 ATOM 1821 C CD . LYS B 2 66 ? 56.438 24.554 47.414 1.00 34.14 ? 143 LYS B CD 1 ATOM 1822 C CE . LYS B 2 66 ? 56.394 26.066 47.256 0.0000 34.97 ? 143 LYS B CE 1 ATOM 1823 N NZ . LYS B 2 66 ? 57.134 26.768 48.335 0.0000 35.40 ? 143 LYS B NZ 1 ATOM 1824 N N . PRO B 2 67 ? 55.561 19.554 45.097 1.00 24.38 ? 144 PRO B N 1 ATOM 1825 C CA . PRO B 2 67 ? 55.770 18.117 45.310 1.00 24.93 ? 144 PRO B CA 1 ATOM 1826 C C . PRO B 2 67 ? 55.913 17.770 46.792 1.00 24.31 ? 144 PRO B C 1 ATOM 1827 O O . PRO B 2 67 ? 56.732 18.357 47.530 1.00 24.22 ? 144 PRO B O 1 ATOM 1828 C CB . PRO B 2 67 ? 57.082 17.845 44.552 1.00 25.83 ? 144 PRO B CB 1 ATOM 1829 C CG . PRO B 2 67 ? 57.019 18.838 43.399 1.00 25.62 ? 144 PRO B CG 1 ATOM 1830 C CD . PRO B 2 67 ? 56.503 20.103 44.100 1.00 24.16 ? 144 PRO B CD 1 ATOM 1831 N N . LEU B 2 68 ? 55.087 16.806 47.202 1.00 24.48 ? 145 LEU B N 1 ATOM 1832 C CA . LEU B 2 68 ? 55.002 16.271 48.559 1.00 23.44 ? 145 LEU B CA 1 ATOM 1833 C C . LEU B 2 68 ? 54.535 17.272 49.625 1.00 21.34 ? 145 LEU B C 1 ATOM 1834 O O . LEU B 2 68 ? 54.829 17.097 50.802 1.00 23.47 ? 145 LEU B O 1 ATOM 1835 C CB . LEU B 2 68 ? 56.302 15.593 48.979 1.00 26.27 ? 145 LEU B CB 1 ATOM 1836 C CG . LEU B 2 68 ? 56.734 14.471 48.036 1.00 30.08 ? 145 LEU B CG 1 ATOM 1837 C CD1 . LEU B 2 68 ? 58.059 13.916 48.518 1.00 31.41 ? 145 LEU B CD1 1 ATOM 1838 C CD2 . LEU B 2 68 ? 55.659 13.376 47.873 1.00 32.42 ? 145 LEU B CD2 1 ATOM 1839 N N . SER B 2 69 ? 53.807 18.307 49.208 1.00 21.44 ? 146 SER B N 1 ATOM 1840 C CA . SER B 2 69 ? 53.038 19.116 50.127 1.00 19.39 ? 146 SER B CA 1 ATOM 1841 C C . SER B 2 69 ? 52.035 18.221 50.807 1.00 18.76 ? 146 SER B C 1 ATOM 1842 O O . SER B 2 69 ? 51.546 17.281 50.223 1.00 18.33 ? 146 SER B O 1 ATOM 1843 C CB . SER B 2 69 ? 52.284 20.210 49.377 1.00 18.89 ? 146 SER B CB 1 ATOM 1844 O OG . SER B 2 69 ? 53.160 21.256 49.051 1.00 21.08 ? 146 SER B OG 1 ATOM 1845 N N . THR B 2 70 ? 51.718 18.544 52.052 1.00 17.39 ? 147 THR B N 1 ATOM 1846 C CA . THR B 2 70 ? 50.705 17.823 52.768 1.00 16.40 ? 147 THR B CA 1 ATOM 1847 C C . THR B 2 70 ? 49.439 18.648 52.888 1.00 15.59 ? 147 THR B C 1 ATOM 1848 O O . THR B 2 70 ? 49.466 19.797 53.345 1.00 16.65 ? 147 THR B O 1 ATOM 1849 C CB . THR B 2 70 ? 51.206 17.455 54.175 1.00 19.13 ? 147 THR B CB 1 ATOM 1850 O OG1 . THR B 2 70 ? 52.313 16.527 54.071 1.00 20.10 ? 147 THR B OG1 1 ATOM 1851 C CG2 . THR B 2 70 ? 50.071 16.789 54.981 1.00 20.12 ? 147 THR B CG2 1 ATOM 1852 N N . VAL B 2 71 ? 48.333 18.047 52.472 1.00 13.90 ? 148 VAL B N 1 ATOM 1853 C CA . VAL B 2 71 ? 47.003 18.612 52.609 1.00 12.74 ? 148 VAL B CA 1 ATOM 1854 C C . VAL B 2 71 ? 46.302 17.786 53.684 1.00 13.39 ? 148 VAL B C 1 ATOM 1855 O O . VAL B 2 71 ? 46.512 16.559 53.772 1.00 15.14 ? 148 VAL B O 1 ATOM 1856 C CB . VAL B 2 71 ? 46.254 18.503 51.223 1.00 13.37 ? 148 VAL B CB 1 ATOM 1857 C CG1 . VAL B 2 71 ? 44.734 18.727 51.331 1.00 12.79 ? 148 VAL B CG1 1 ATOM 1858 C CG2 . VAL B 2 71 ? 46.910 19.420 50.201 1.00 14.42 ? 148 VAL B CG2 1 ATOM 1859 N N . PHE B 2 72 ? 45.464 18.436 54.510 1.00 12.35 ? 149 PHE B N 1 ATOM 1860 C CA . PHE B 2 72 ? 44.651 17.688 55.488 1.00 13.50 ? 149 PHE B CA 1 ATOM 1861 C C . PHE B 2 72 ? 43.261 17.333 54.941 1.00 14.05 ? 149 PHE B C 1 ATOM 1862 O O . PHE B 2 72 ? 42.590 18.165 54.329 1.00 13.53 ? 149 PHE B O 1 ATOM 1863 C CB . PHE B 2 72 ? 44.434 18.504 56.759 1.00 13.56 ? 149 PHE B CB 1 ATOM 1864 C CG . PHE B 2 72 ? 45.594 18.510 57.713 1.00 16.18 ? 149 PHE B CG 1 ATOM 1865 C CD1 . PHE B 2 72 ? 46.846 18.015 57.356 1.00 18.56 ? 149 PHE B CD1 1 ATOM 1866 C CD2 . PHE B 2 72 ? 45.395 19.022 58.989 1.00 18.75 ? 149 PHE B CD2 1 ATOM 1867 C CE1 . PHE B 2 72 ? 47.902 18.050 58.263 1.00 20.50 ? 149 PHE B CE1 1 ATOM 1868 C CE2 . PHE B 2 72 ? 46.422 19.064 59.898 1.00 20.57 ? 149 PHE B CE2 1 ATOM 1869 C CZ . PHE B 2 72 ? 47.693 18.576 59.542 1.00 21.66 ? 149 PHE B CZ 1 ATOM 1870 N N . MET B 2 73 ? 42.814 16.116 55.221 1.00 13.35 ? 150 MET B N 1 ATOM 1871 C CA . MET B 2 73 ? 41.439 15.688 54.997 1.00 11.81 ? 150 MET B CA 1 ATOM 1872 C C . MET B 2 73 ? 40.691 15.788 56.308 1.00 13.18 ? 150 MET B C 1 ATOM 1873 O O . MET B 2 73 ? 40.882 14.973 57.212 1.00 15.79 ? 150 MET B O 1 ATOM 1874 C CB . MET B 2 73 ? 41.423 14.229 54.499 1.00 10.12 ? 150 MET B CB 1 ATOM 1875 C CG . MET B 2 73 ? 40.048 13.665 54.323 1.00 12.26 ? 150 MET B CG 1 ATOM 1876 S SD . MET B 2 73 ? 40.158 11.865 54.283 1.00 14.72 ? 150 MET B SD 1 ATOM 1877 C CE . MET B 2 73 ? 38.451 11.427 53.853 1.00 14.21 ? 150 MET B CE 1 ATOM 1878 N N . ASN B 2 74 ? 39.836 16.786 56.420 1.00 12.79 ? 151 ASN B N 1 ATOM 1879 C CA . ASN B 2 74 ? 39.129 17.073 57.678 1.00 12.40 ? 151 ASN B CA 1 ATOM 1880 C C . ASN B 2 74 ? 37.704 16.490 57.667 1.00 12.51 ? 151 ASN B C 1 ATOM 1881 O O . ASN B 2 74 ? 36.847 16.897 56.837 1.00 13.55 ? 151 ASN B O 1 ATOM 1882 C CB . ASN B 2 74 ? 39.101 18.569 57.914 1.00 13.15 ? 151 ASN B CB 1 ATOM 1883 C CG . ASN B 2 74 ? 40.483 19.179 57.838 1.00 14.79 ? 151 ASN B CG 1 ATOM 1884 O OD1 . ASN B 2 74 ? 41.346 18.823 58.620 1.00 17.43 ? 151 ASN B OD1 1 ATOM 1885 N ND2 . ASN B 2 74 ? 40.710 20.073 56.900 1.00 14.04 ? 151 ASN B ND2 1 ATOM 1886 N N . LEU B 2 75 ? 37.451 15.518 58.551 1.00 12.95 ? 152 LEU B N 1 ATOM 1887 C CA . LEU B 2 75 ? 36.165 14.822 58.518 1.00 14.55 ? 152 LEU B CA 1 ATOM 1888 C C . LEU B 2 75 ? 35.044 15.711 59.031 1.00 14.04 ? 152 LEU B C 1 ATOM 1889 O O . LEU B 2 75 ? 35.211 16.492 60.011 1.00 16.67 ? 152 LEU B O 1 ATOM 1890 C CB . LEU B 2 75 ? 36.204 13.567 59.387 1.00 14.82 ? 152 LEU B CB 1 ATOM 1891 C CG . LEU B 2 75 ? 37.067 12.429 58.856 1.00 16.42 ? 152 LEU B CG 1 ATOM 1892 C CD1 . LEU B 2 75 ? 36.976 11.216 59.767 1.00 15.92 ? 152 LEU B CD1 1 ATOM 1893 C CD2 . LEU B 2 75 ? 36.575 12.068 57.432 1.00 18.88 ? 152 LEU B CD2 1 ATOM 1894 N N . ARG B 2 76 ? 33.894 15.567 58.382 1.00 11.60 ? 153 ARG B N 1 ATOM 1895 C CA . ARG B 2 76 ? 32.638 16.057 58.916 1.00 11.39 ? 153 ARG B CA 1 ATOM 1896 C C . ARG B 2 76 ? 32.034 14.888 59.671 1.00 13.23 ? 153 ARG B C 1 ATOM 1897 O O . ARG B 2 76 ? 31.840 13.814 59.109 1.00 16.97 ? 153 ARG B O 1 ATOM 1898 C CB . ARG B 2 76 ? 31.738 16.524 57.740 1.00 13.17 ? 153 ARG B CB 1 ATOM 1899 C CG . ARG B 2 76 ? 30.293 16.750 58.099 1.00 13.06 ? 153 ARG B CG 1 ATOM 1900 C CD . ARG B 2 76 ? 29.632 17.686 57.021 1.00 14.58 ? 153 ARG B CD 1 ATOM 1901 N NE . ARG B 2 76 ? 28.183 17.683 57.209 1.00 14.75 ? 153 ARG B NE 1 ATOM 1902 C CZ . ARG B 2 76 ? 27.572 18.352 58.184 1.00 14.76 ? 153 ARG B CZ 1 ATOM 1903 N NH1 . ARG B 2 76 ? 28.286 19.075 59.051 1.00 14.26 ? 153 ARG B NH1 1 ATOM 1904 N NH2 . ARG B 2 76 ? 26.268 18.276 58.320 1.00 14.53 ? 153 ARG B NH2 1 ATOM 1905 N N . LEU B 2 77 ? 31.743 15.081 60.965 1.00 11.55 ? 154 LEU B N 1 ATOM 1906 C CA . LEU B 2 77 ? 31.212 13.978 61.794 1.00 10.57 ? 154 LEU B CA 1 ATOM 1907 C C . LEU B 2 77 ? 29.791 14.308 62.203 1.00 13.34 ? 154 LEU B C 1 ATOM 1908 O O . LEU B 2 77 ? 29.519 15.417 62.705 1.00 12.74 ? 154 LEU B O 1 ATOM 1909 C CB . LEU B 2 77 ? 32.077 13.761 63.062 1.00 11.83 ? 154 LEU B CB 1 ATOM 1910 C CG . LEU B 2 77 ? 33.588 13.577 62.863 1.00 13.70 ? 154 LEU B CG 1 ATOM 1911 C CD1 . LEU B 2 77 ? 34.284 13.724 64.223 1.00 16.74 ? 154 LEU B CD1 1 ATOM 1912 C CD2 . LEU B 2 77 ? 33.843 12.212 62.255 1.00 14.48 ? 154 LEU B CD2 1 ATOM 1913 N N . ARG B 2 78 ? 28.866 13.369 61.962 1.00 12.29 ? 155 ARG B N 1 ATOM 1914 C CA . ARG B 2 78 ? 27.468 13.603 62.301 1.00 12.84 ? 155 ARG B CA 1 ATOM 1915 C C . ARG B 2 78 ? 26.993 12.491 63.216 1.00 12.30 ? 155 ARG B C 1 ATOM 1916 O O . ARG B 2 78 ? 27.574 11.410 63.215 1.00 14.44 ? 155 ARG B O 1 ATOM 1917 C CB . ARG B 2 78 ? 26.600 13.616 61.038 1.00 15.99 ? 155 ARG B CB 1 ATOM 1918 C CG . ARG B 2 78 ? 27.048 14.600 59.949 1.00 19.04 ? 155 ARG B CG 1 ATOM 1919 C CD . ARG B 2 78 ? 26.173 14.417 58.732 1.00 22.95 ? 155 ARG B CD 1 ATOM 1920 N NE . ARG B 2 78 ? 24.788 14.811 58.995 1.00 26.55 ? 155 ARG B NE 1 ATOM 1921 C CZ . ARG B 2 78 ? 23.725 14.030 58.817 1.00 31.26 ? 155 ARG B CZ 1 ATOM 1922 N NH1 . ARG B 2 78 ? 23.868 12.778 58.392 1.00 33.75 ? 155 ARG B NH1 1 ATOM 1923 N NH2 . ARG B 2 78 ? 22.513 14.505 59.092 1.00 33.10 ? 155 ARG B NH2 1 ATOM 1924 N N . GLY B 2 79 ? 25.932 12.727 63.988 1.00 12.11 ? 156 GLY B N 1 ATOM 1925 C CA . GLY B 2 79 ? 25.441 11.641 64.800 1.00 12.40 ? 156 GLY B CA 1 ATOM 1926 C C . GLY B 2 79 ? 24.298 12.045 65.681 1.00 12.06 ? 156 GLY B C 1 ATOM 1927 O O . GLY B 2 79 ? 23.852 13.179 65.742 1.00 11.84 ? 156 GLY B O 1 HETATM 1928 ZN ZN . ZN C 3 . ? 19.154 17.680 77.308 0.53 19.77 ? 184 ZN A ZN 1 HETATM 1929 ZN ZN . ZN D 3 . ? 52.982 18.671 73.881 0.88 17.33 ? 185 ZN A ZN 1 HETATM 1930 ZN ZN . ZN E 3 . ? 53.155 14.874 70.291 0.86 18.46 ? 186 ZN A ZN 1 HETATM 1931 ZN ZN . ZN F 3 . ? 44.450 0.807 74.208 0.49 33.45 ? 187 ZN A ZN 1 HETATM 1932 ZN ZN . ZN G 3 . ? 25.486 6.624 73.831 0.78 20.85 ? 188 ZN A ZN 1 HETATM 1933 ZN ZN . ZN H 3 . ? 12.906 26.671 52.169 0.52 21.23 ? 189 ZN A ZN 1 HETATM 1934 ZN ZN . ZN I 3 . ? 23.590 14.998 84.158 0.53 48.32 ? 190 ZN A ZN 1 HETATM 1935 ZN ZN . ZN J 3 . ? 16.153 12.941 73.521 0.87 14.76 ? 191 ZN A ZN 1 HETATM 1936 ZN ZN . ZN K 3 . ? 53.783 12.707 83.008 0.79 23.32 ? 192 ZN A ZN 1 HETATM 1937 C C . ACY L 4 . ? 13.749 14.060 72.236 0.85 16.78 ? 193 ACY A C 1 HETATM 1938 O O . ACY L 4 . ? 13.189 14.950 71.570 0.85 16.72 ? 193 ACY A O 1 HETATM 1939 O OXT . ACY L 4 . ? 14.963 14.100 72.547 0.85 12.44 ? 193 ACY A OXT 1 HETATM 1940 C CH3 . ACY L 4 . ? 12.916 12.880 72.635 0.85 18.70 ? 193 ACY A CH3 1 HETATM 1941 N N . NEH M 5 . ? 23.434 10.887 65.897 1.00 11.54 ? 157 NEH B N 1 HETATM 1942 C CA . NEH M 5 . ? 22.251 11.149 66.717 1.00 11.77 ? 157 NEH B CA 1 HETATM 1943 C CB . NEH M 5 . ? 22.425 10.489 68.084 1.00 12.05 ? 157 NEH B CB 1 HETATM 1944 ZN ZN . ZN N 3 . ? 41.528 12.912 37.143 0.67 28.29 ? 1 ZN B ZN 1 HETATM 1945 ZN ZN . ZN O 3 . ? 36.310 15.254 38.852 0.35 19.90 ? 2 ZN B ZN 1 HETATM 1946 ZN ZN . ZN P 3 . ? 31.322 13.819 44.209 0.86 23.13 ? 3 ZN B ZN 1 HETATM 1947 C C . ACY Q 4 . ? 29.263 12.884 46.067 0.52 28.13 ? 4 ACY B C 1 HETATM 1948 O O . ACY Q 4 . ? 29.670 12.769 44.874 0.84 29.17 ? 4 ACY B O 1 HETATM 1949 O OXT . ACY Q 4 . ? 29.116 13.988 46.643 1.00 24.44 ? 4 ACY B OXT 1 HETATM 1950 C CH3 . ACY Q 4 . ? 28.944 11.638 46.863 0.61 29.74 ? 4 ACY B CH3 1 HETATM 1951 O O . HOH R 6 . ? 19.542 13.444 60.486 1.00 24.51 ? 201 HOH A O 1 HETATM 1952 O O . HOH R 6 . ? 24.607 20.000 59.986 1.00 16.88 ? 202 HOH A O 1 HETATM 1953 O O . HOH R 6 . ? 33.899 17.335 79.163 1.00 13.33 ? 203 HOH A O 1 HETATM 1954 O O . HOH R 6 . ? 18.398 17.674 66.767 1.00 13.30 ? 204 HOH A O 1 HETATM 1955 O O . HOH R 6 . ? 22.282 14.888 67.224 1.00 12.61 ? 205 HOH A O 1 HETATM 1956 O O . HOH R 6 . ? 48.236 9.649 82.983 1.00 29.13 ? 206 HOH A O 1 HETATM 1957 O O . HOH R 6 . ? 35.387 17.004 82.140 1.00 20.19 ? 207 HOH A O 1 HETATM 1958 O O . HOH R 6 . ? 20.343 19.449 63.857 1.00 15.40 ? 208 HOH A O 1 HETATM 1959 O O . HOH R 6 . ? 35.959 25.544 62.743 1.00 18.39 ? 209 HOH A O 1 HETATM 1960 O O . HOH R 6 . ? 35.325 19.405 60.301 1.00 19.37 ? 210 HOH A O 1 HETATM 1961 O O . HOH R 6 . ? 29.545 7.973 71.424 0.96 17.50 ? 211 HOH A O 1 HETATM 1962 O O . HOH R 6 . ? 48.794 17.108 66.510 1.00 30.07 ? 212 HOH A O 1 HETATM 1963 O O . HOH R 6 . ? 34.816 27.728 66.221 1.00 24.83 ? 213 HOH A O 1 HETATM 1964 O O . HOH R 6 . ? 32.582 25.768 79.408 1.00 22.29 ? 214 HOH A O 1 HETATM 1965 O O . HOH R 6 . ? 32.154 5.356 82.055 1.00 33.66 ? 215 HOH A O 1 HETATM 1966 O O . HOH R 6 . ? 12.132 23.322 61.721 1.00 29.59 ? 216 HOH A O 1 HETATM 1967 O O . HOH R 6 . ? 34.704 25.471 77.390 1.00 26.09 ? 217 HOH A O 1 HETATM 1968 O O . HOH R 6 . ? 32.872 24.536 59.459 1.00 23.69 ? 218 HOH A O 1 HETATM 1969 O O . HOH R 6 . ? 13.089 18.964 68.954 1.00 24.64 ? 219 HOH A O 1 HETATM 1970 O O . HOH R 6 . ? 35.634 29.341 71.356 1.00 20.72 ? 220 HOH A O 1 HETATM 1971 O O . HOH R 6 . ? 15.348 9.794 66.738 1.00 27.92 ? 221 HOH A O 1 HETATM 1972 O O . HOH R 6 . ? 34.369 22.992 52.312 1.00 21.42 ? 222 HOH A O 1 HETATM 1973 O O . HOH R 6 . ? 25.455 33.129 58.175 1.00 23.52 ? 223 HOH A O 1 HETATM 1974 O O . HOH R 6 . ? 45.853 13.198 82.790 1.00 22.34 ? 224 HOH A O 1 HETATM 1975 O O . HOH R 6 . ? 34.290 22.856 60.967 1.00 20.18 ? 225 HOH A O 1 HETATM 1976 O O . HOH R 6 . ? 18.924 25.646 49.963 0.96 25.42 ? 226 HOH A O 1 HETATM 1977 O O . HOH R 6 . ? 14.857 22.639 69.525 1.00 21.48 ? 227 HOH A O 1 HETATM 1978 O O . HOH R 6 . ? 14.525 20.530 67.579 1.00 22.86 ? 228 HOH A O 1 HETATM 1979 O O . HOH R 6 . ? 35.874 29.212 68.367 0.92 25.13 ? 229 HOH A O 1 HETATM 1980 O O . HOH R 6 . ? 24.334 19.060 83.292 1.00 25.41 ? 230 HOH A O 1 HETATM 1981 O O . HOH R 6 . ? 19.309 35.736 59.506 1.00 43.42 ? 231 HOH A O 1 HETATM 1982 O O . HOH R 6 . ? 18.721 32.111 53.352 1.00 31.70 ? 232 HOH A O 1 HETATM 1983 O O . HOH R 6 . ? 32.693 7.282 65.164 0.90 24.05 ? 233 HOH A O 1 HETATM 1984 O O . HOH R 6 . ? 14.798 28.082 50.399 0.85 23.24 ? 234 HOH A O 1 HETATM 1985 O O . HOH R 6 . ? 35.369 5.356 82.605 1.00 25.30 ? 235 HOH A O 1 HETATM 1986 O O . HOH R 6 . ? 18.115 14.224 78.644 1.00 31.82 ? 236 HOH A O 1 HETATM 1987 O O . HOH R 6 . ? 49.798 9.505 72.610 0.99 31.58 ? 237 HOH A O 1 HETATM 1988 O O . HOH R 6 . ? 48.503 14.418 68.630 0.96 28.53 ? 238 HOH A O 1 HETATM 1989 O O . HOH R 6 . ? 22.311 17.808 56.165 1.00 35.94 ? 239 HOH A O 1 HETATM 1990 O O . HOH R 6 . ? 48.439 14.178 71.557 0.97 21.49 ? 240 HOH A O 1 HETATM 1991 O O . HOH R 6 . ? 24.904 30.268 77.018 0.87 28.48 ? 241 HOH A O 1 HETATM 1992 O O . HOH R 6 . ? 51.031 13.841 73.808 1.00 41.23 ? 242 HOH A O 1 HETATM 1993 O O . HOH R 6 . ? 32.130 31.291 60.620 0.82 24.80 ? 243 HOH A O 1 HETATM 1994 O O . HOH R 6 . ? 47.906 6.380 78.918 1.00 40.36 ? 244 HOH A O 1 HETATM 1995 O O . HOH R 6 . ? 50.375 15.009 67.060 1.00 32.83 ? 245 HOH A O 1 HETATM 1996 O O . HOH R 6 . ? 16.681 29.226 50.098 0.89 34.55 ? 246 HOH A O 1 HETATM 1997 O O . HOH R 6 . ? 36.452 26.014 65.505 0.89 22.45 ? 247 HOH A O 1 HETATM 1998 O O . HOH R 6 . ? 14.591 9.251 73.397 1.00 37.37 ? 248 HOH A O 1 HETATM 1999 O O . HOH R 6 . ? 21.926 20.104 60.983 1.00 37.31 ? 249 HOH A O 1 HETATM 2000 O O . HOH R 6 . ? 22.149 35.730 65.685 0.97 29.57 ? 250 HOH A O 1 HETATM 2001 O O . HOH R 6 . ? 46.495 14.147 61.886 0.91 25.53 ? 251 HOH A O 1 HETATM 2002 O O . HOH R 6 . ? 44.464 4.488 77.743 1.00 28.92 ? 252 HOH A O 1 HETATM 2003 O O . HOH R 6 . ? 33.074 3.101 67.192 1.00 32.39 ? 253 HOH A O 1 HETATM 2004 O O . HOH R 6 . ? 15.230 12.385 75.492 1.00 11.21 ? 254 HOH A O 1 HETATM 2005 O O . HOH R 6 . ? 51.848 19.756 75.476 1.00 12.58 ? 255 HOH A O 1 HETATM 2006 O O . HOH R 6 . ? 44.351 20.287 75.661 1.00 12.42 ? 256 HOH A O 1 HETATM 2007 O O . HOH R 6 . ? 43.951 24.610 81.713 1.00 24.30 ? 257 HOH A O 1 HETATM 2008 O O . HOH R 6 . ? 26.367 4.676 74.365 1.00 25.35 ? 258 HOH A O 1 HETATM 2009 O O . HOH R 6 . ? 23.646 6.392 74.732 1.00 25.24 ? 259 HOH A O 1 HETATM 2010 O O . HOH R 6 . ? 36.537 19.296 80.589 0.91 17.80 ? 260 HOH A O 1 HETATM 2011 O O . HOH R 6 . ? 45.519 22.941 57.490 1.00 25.07 ? 261 HOH A O 1 HETATM 2012 O O . HOH R 6 . ? 51.560 13.849 70.898 0.87 21.72 ? 262 HOH A O 1 HETATM 2013 O O . HOH R 6 . ? 45.269 22.896 74.537 1.00 27.28 ? 263 HOH A O 1 HETATM 2014 O O . HOH R 6 . ? 46.315 19.449 77.224 1.00 22.85 ? 264 HOH A O 1 HETATM 2015 O O . HOH R 6 . ? 39.522 5.284 87.155 1.00 22.38 ? 265 HOH A O 1 HETATM 2016 O O . HOH R 6 . ? 53.742 13.141 69.412 1.00 32.35 ? 266 HOH A O 1 HETATM 2017 O O . HOH R 6 . ? 38.188 29.689 72.095 1.00 28.69 ? 267 HOH A O 1 HETATM 2018 O O . HOH R 6 . ? 54.196 17.829 72.560 0.49 18.25 ? 268 HOH A O 1 HETATM 2019 O O . HOH R 6 . ? 36.869 28.421 75.186 0.82 20.66 ? 269 HOH A O 1 HETATM 2020 O O . HOH R 6 . ? 53.307 11.245 81.130 1.00 44.30 ? 270 HOH A O 1 HETATM 2021 O O . HOH R 6 . ? 22.048 6.783 68.408 1.00 33.04 ? 271 HOH A O 1 HETATM 2022 O O . HOH R 6 . ? 51.904 19.545 64.490 1.00 39.32 ? 272 HOH A O 1 HETATM 2023 O O . HOH R 6 . ? 10.518 15.225 80.607 0.90 34.49 ? 273 HOH A O 1 HETATM 2024 O O . HOH R 6 . ? 41.734 5.031 84.960 1.00 27.96 ? 274 HOH A O 1 HETATM 2025 O O . HOH R 6 . ? 18.001 33.573 66.238 1.00 37.93 ? 275 HOH A O 1 HETATM 2026 O O . HOH R 6 . ? 49.212 21.740 71.571 1.00 33.03 ? 276 HOH A O 1 HETATM 2027 O O . HOH R 6 . ? 17.651 31.458 68.444 0.90 29.22 ? 277 HOH A O 1 HETATM 2028 O O . HOH R 6 . ? 35.682 27.531 52.229 0.90 36.14 ? 278 HOH A O 1 HETATM 2029 O O . HOH R 6 . ? 44.438 29.645 66.102 1.00 40.24 ? 279 HOH A O 1 HETATM 2030 O O . HOH R 6 . ? 25.165 33.381 73.355 1.00 45.59 ? 280 HOH A O 1 HETATM 2031 O O . HOH R 6 . ? 39.984 19.415 63.057 0.51 18.62 ? 281 HOH A O 1 HETATM 2032 O O . HOH R 6 . ? 39.299 3.442 66.970 1.00 37.36 ? 282 HOH A O 1 HETATM 2033 O O . HOH R 6 . ? 33.440 33.485 70.737 1.00 39.42 ? 283 HOH A O 1 HETATM 2034 O O . HOH R 6 . ? 33.283 23.467 80.913 1.00 43.30 ? 284 HOH A O 1 HETATM 2035 O O . HOH R 6 . ? 31.668 37.223 59.303 1.00 37.55 ? 285 HOH A O 1 HETATM 2036 O O . HOH R 6 . ? 18.550 9.178 64.783 1.00 34.95 ? 286 HOH A O 1 HETATM 2037 O O . HOH R 6 . ? 46.106 30.809 64.624 1.00 45.30 ? 287 HOH A O 1 HETATM 2038 O O . HOH R 6 . ? 22.376 6.998 66.015 1.00 43.65 ? 288 HOH A O 1 HETATM 2039 O O . HOH R 6 . ? 48.851 23.534 60.516 0.92 27.29 ? 289 HOH A O 1 HETATM 2040 O O . HOH R 6 . ? 24.137 17.426 60.729 0.65 30.93 ? 290 HOH A O 1 HETATM 2041 O O . HOH R 6 . ? 38.953 30.194 61.188 0.77 31.44 ? 291 HOH A O 1 HETATM 2042 O O . HOH R 6 . ? 15.630 22.309 54.652 1.00 33.70 ? 292 HOH A O 1 HETATM 2043 O O . HOH R 6 . ? 37.272 1.454 66.854 1.00 40.54 ? 293 HOH A O 1 HETATM 2044 O O . HOH R 6 . ? 42.603 31.308 67.893 1.00 40.92 ? 294 HOH A O 1 HETATM 2045 O O . HOH R 6 . ? 22.081 31.694 52.383 1.00 40.85 ? 295 HOH A O 1 HETATM 2046 O O . HOH R 6 . ? 28.146 32.808 76.154 1.00 41.29 ? 296 HOH A O 1 HETATM 2047 O O . HOH R 6 . ? 49.891 23.807 64.570 1.00 29.49 ? 297 HOH A O 1 HETATM 2048 O O . HOH R 6 . ? 48.270 20.480 75.878 1.00 33.05 ? 298 HOH A O 1 HETATM 2049 O O . HOH R 6 . ? 38.702 24.885 77.328 0.72 27.41 ? 299 HOH A O 1 HETATM 2050 O O . HOH R 6 . ? 11.442 15.563 62.745 0.81 39.10 ? 300 HOH A O 1 HETATM 2051 O O . HOH R 6 . ? 35.627 32.384 75.775 0.71 27.46 ? 301 HOH A O 1 HETATM 2052 O O . HOH R 6 . ? 26.159 31.512 75.195 1.00 38.33 ? 302 HOH A O 1 HETATM 2053 O O . HOH R 6 . ? 37.268 29.815 51.575 1.00 39.70 ? 303 HOH A O 1 HETATM 2054 O O . HOH R 6 . ? 33.115 19.501 80.729 1.00 39.60 ? 304 HOH A O 1 HETATM 2055 O O . HOH R 6 . ? 45.798 15.678 84.647 0.88 27.56 ? 305 HOH A O 1 HETATM 2056 O O . HOH R 6 . ? 35.898 28.120 61.993 0.58 30.32 ? 306 HOH A O 1 HETATM 2057 O O . HOH R 6 . ? 35.174 20.542 82.765 0.79 25.53 ? 307 HOH A O 1 HETATM 2058 O O . HOH R 6 . ? 34.032 11.996 86.267 1.00 42.61 ? 308 HOH A O 1 HETATM 2059 O O . HOH R 6 . ? 44.848 25.473 74.967 0.84 28.17 ? 309 HOH A O 1 HETATM 2060 O O . HOH R 6 . ? 39.087 3.959 84.215 0.82 35.49 ? 310 HOH A O 1 HETATM 2061 O O . HOH R 6 . ? 19.476 23.929 48.044 1.00 53.55 ? 311 HOH A O 1 HETATM 2062 O O . HOH R 6 . ? 41.472 26.337 78.797 0.98 36.78 ? 312 HOH A O 1 HETATM 2063 O O . HOH R 6 . ? 26.002 7.050 81.704 1.00 27.70 ? 313 HOH A O 1 HETATM 2064 O O . HOH R 6 . ? 10.455 19.740 68.288 1.00 36.81 ? 314 HOH A O 1 HETATM 2065 O O . HOH R 6 . ? 37.128 26.835 77.348 1.00 44.56 ? 315 HOH A O 1 HETATM 2066 O O . HOH R 6 . ? 27.862 3.522 69.826 1.00 49.44 ? 316 HOH A O 1 HETATM 2067 O O . HOH R 6 . ? 12.773 16.581 83.118 1.00 46.37 ? 317 HOH A O 1 HETATM 2068 O O . HOH R 6 . ? 19.420 15.618 77.350 0.81 9.42 ? 318 HOH A O 1 HETATM 2069 O O . HOH R 6 . ? 21.428 25.359 83.388 0.85 34.11 ? 319 HOH A O 1 HETATM 2070 O O . HOH R 6 . ? 45.735 2.558 73.536 1.00 36.74 ? 320 HOH A O 1 HETATM 2071 O O . HOH R 6 . ? 44.865 25.043 71.242 1.00 37.34 ? 321 HOH A O 1 HETATM 2072 O O . HOH R 6 . ? 13.493 19.266 79.368 1.00 39.74 ? 322 HOH A O 1 HETATM 2073 O O . HOH R 6 . ? 43.440 2.500 84.487 1.00 40.33 ? 323 HOH A O 1 HETATM 2074 O O . HOH R 6 . ? 50.853 11.451 69.920 1.00 39.71 ? 324 HOH A O 1 HETATM 2075 O O . HOH R 6 . ? 52.958 12.658 75.883 0.99 33.46 ? 325 HOH A O 1 HETATM 2076 O O . HOH R 6 . ? 22.517 12.477 81.272 1.00 42.91 ? 326 HOH A O 1 HETATM 2077 O O . HOH R 6 . ? 26.332 27.832 52.042 1.00 52.89 ? 327 HOH A O 1 HETATM 2078 O O . HOH R 6 . ? 35.796 8.558 62.229 1.00 44.77 ? 328 HOH A O 1 HETATM 2079 O O . HOH R 6 . ? 23.543 37.497 53.870 1.00 65.91 ? 329 HOH A O 1 HETATM 2080 O O . HOH R 6 . ? 12.124 27.973 50.091 1.00 56.93 ? 330 HOH A O 1 HETATM 2081 O O . HOH R 6 . ? 12.782 25.463 49.889 1.00 41.34 ? 331 HOH A O 1 HETATM 2082 O O . HOH S 6 . ? 37.701 21.284 50.530 1.00 15.11 ? 201 HOH B O 1 HETATM 2083 O O . HOH S 6 . ? 44.414 10.539 51.998 1.00 18.59 ? 202 HOH B O 1 HETATM 2084 O O . HOH S 6 . ? 34.239 16.524 45.238 1.00 21.12 ? 203 HOH B O 1 HETATM 2085 O O . HOH S 6 . ? 39.385 14.996 60.668 1.00 21.19 ? 204 HOH B O 1 HETATM 2086 O O . HOH S 6 . ? 39.556 19.100 37.440 1.00 19.72 ? 205 HOH B O 1 HETATM 2087 O O . HOH S 6 . ? 54.650 17.459 53.498 1.00 27.03 ? 206 HOH B O 1 HETATM 2088 O O . HOH S 6 . ? 34.179 6.349 48.530 1.00 23.16 ? 207 HOH B O 1 HETATM 2089 O O . HOH S 6 . ? 39.776 10.817 57.370 1.00 20.58 ? 208 HOH B O 1 HETATM 2090 O O . HOH S 6 . ? 35.751 19.794 39.270 1.00 31.97 ? 209 HOH B O 1 HETATM 2091 O O . HOH S 6 . ? 52.290 14.129 55.617 1.00 25.03 ? 210 HOH B O 1 HETATM 2092 O O . HOH S 6 . ? 29.787 10.809 60.970 0.89 21.75 ? 211 HOH B O 1 HETATM 2093 O O . HOH S 6 . ? 45.774 8.090 54.254 1.00 22.94 ? 212 HOH B O 1 HETATM 2094 O O . HOH S 6 . ? 27.441 16.535 54.636 1.00 27.91 ? 213 HOH B O 1 HETATM 2095 O O . HOH S 6 . ? 31.038 8.139 53.742 0.84 26.32 ? 214 HOH B O 1 HETATM 2096 O O . HOH S 6 . ? 36.638 3.241 48.188 1.00 24.02 ? 215 HOH B O 1 HETATM 2097 O O . HOH S 6 . ? 33.897 26.113 45.417 1.00 25.51 ? 216 HOH B O 1 HETATM 2098 O O . HOH S 6 . ? 34.366 29.002 44.952 1.00 39.32 ? 217 HOH B O 1 HETATM 2099 O O . HOH S 6 . ? 36.287 1.850 50.453 0.83 41.18 ? 218 HOH B O 1 HETATM 2100 O O . HOH S 6 . ? 56.181 14.987 42.416 1.00 34.79 ? 219 HOH B O 1 HETATM 2101 O O . HOH S 6 . ? 40.916 17.308 60.927 1.00 36.45 ? 220 HOH B O 1 HETATM 2102 O O . HOH S 6 . ? 57.466 16.664 40.614 1.00 41.17 ? 221 HOH B O 1 HETATM 2103 O O . HOH S 6 . ? 33.088 11.953 57.701 0.52 19.01 ? 222 HOH B O 1 HETATM 2104 O O . HOH S 6 . ? 39.520 6.277 55.670 0.91 27.32 ? 223 HOH B O 1 HETATM 2105 O O . HOH S 6 . ? 35.050 21.053 50.363 1.00 14.76 ? 224 HOH B O 1 HETATM 2106 O O . HOH S 6 . ? 38.669 8.377 57.425 1.00 29.28 ? 225 HOH B O 1 HETATM 2107 O O . HOH S 6 . ? 24.868 16.968 56.005 1.00 30.81 ? 226 HOH B O 1 HETATM 2108 O O . HOH S 6 . ? 25.482 12.691 50.978 1.00 44.24 ? 227 HOH B O 1 HETATM 2109 O O . HOH S 6 . ? 53.104 20.644 53.438 0.89 32.89 ? 228 HOH B O 1 HETATM 2110 O O . HOH S 6 . ? 41.733 3.701 53.223 1.00 47.22 ? 229 HOH B O 1 HETATM 2111 O O . HOH S 6 . ? 33.577 9.231 58.255 1.00 37.05 ? 230 HOH B O 1 HETATM 2112 O O . HOH S 6 . ? 36.360 7.895 58.420 1.00 37.47 ? 231 HOH B O 1 HETATM 2113 O O . HOH S 6 . ? 40.207 29.681 48.514 1.00 18.83 ? 232 HOH B O 1 HETATM 2114 O O . HOH S 6 . ? 31.803 7.885 47.613 1.00 33.72 ? 233 HOH B O 1 HETATM 2115 O O . HOH S 6 . ? 51.525 8.600 57.329 1.00 41.05 ? 234 HOH B O 1 HETATM 2116 O O . HOH S 6 . ? 42.430 15.097 59.522 1.00 33.72 ? 235 HOH B O 1 HETATM 2117 O O . HOH S 6 . ? 54.440 22.624 50.967 1.00 24.63 ? 236 HOH B O 1 HETATM 2118 O O . HOH S 6 . ? 50.792 20.389 37.341 1.00 26.35 ? 237 HOH B O 1 HETATM 2119 O O . HOH S 6 . ? 44.628 14.789 60.576 1.00 32.22 ? 238 HOH B O 1 HETATM 2120 O O . HOH S 6 . ? 33.330 28.896 49.262 1.00 48.47 ? 239 HOH B O 1 HETATM 2121 O O . HOH S 6 . ? 32.372 15.639 43.391 0.87 21.46 ? 240 HOH B O 1 HETATM 2122 O O . HOH S 6 . ? 32.160 10.590 47.070 0.85 25.35 ? 241 HOH B O 1 HETATM 2123 O O . HOH S 6 . ? 54.259 12.439 40.304 1.00 44.92 ? 242 HOH B O 1 HETATM 2124 O O . HOH S 6 . ? 48.100 22.806 57.743 1.00 37.41 ? 243 HOH B O 1 HETATM 2125 O O . HOH S 6 . ? 43.245 29.729 59.238 1.00 29.71 ? 244 HOH B O 1 HETATM 2126 O O . HOH S 6 . ? 32.776 21.886 42.101 1.00 42.37 ? 245 HOH B O 1 HETATM 2127 O O . HOH S 6 . ? 46.844 7.606 45.314 1.00 39.67 ? 246 HOH B O 1 HETATM 2128 O O . HOH S 6 . ? 53.224 12.621 63.578 1.00 41.26 ? 247 HOH B O 1 HETATM 2129 O O . HOH S 6 . ? 53.907 23.287 53.964 1.00 41.78 ? 248 HOH B O 1 HETATM 2130 O O . HOH S 6 . ? 50.193 6.290 49.499 0.87 35.32 ? 249 HOH B O 1 HETATM 2131 O O . HOH S 6 . ? 40.178 29.468 51.256 1.00 35.23 ? 250 HOH B O 1 HETATM 2132 O O . HOH S 6 . ? 48.696 21.907 55.211 1.00 31.69 ? 251 HOH B O 1 HETATM 2133 O O . HOH S 6 . ? 35.122 24.377 39.035 0.97 39.71 ? 252 HOH B O 1 HETATM 2134 O O . HOH S 6 . ? 40.815 30.552 57.632 1.00 48.08 ? 253 HOH B O 1 HETATM 2135 O O . HOH S 6 . ? 44.338 5.017 58.058 1.00 35.26 ? 254 HOH B O 1 HETATM 2136 O O . HOH S 6 . ? 46.694 27.179 38.962 1.00 37.38 ? 255 HOH B O 1 HETATM 2137 O O . HOH S 6 . ? 46.964 9.149 42.533 0.87 32.25 ? 256 HOH B O 1 HETATM 2138 O O . HOH S 6 . ? 43.734 19.389 34.760 1.00 39.85 ? 257 HOH B O 1 HETATM 2139 O O . HOH S 6 . ? 32.956 17.833 47.306 0.73 28.76 ? 258 HOH B O 1 HETATM 2140 O O . HOH S 6 . ? 37.130 16.849 61.571 0.64 27.27 ? 259 HOH B O 1 HETATM 2141 O O . HOH S 6 . ? 48.054 28.498 49.785 0.74 31.11 ? 260 HOH B O 1 HETATM 2142 O O . HOH S 6 . ? 31.336 11.064 59.113 1.00 46.36 ? 261 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . GLY A 1 ? 0.3001 0.5815 0.3643 -0.0939 0.0057 0.1383 -1 GLY A N 2 C CA . GLY A 1 ? 0.3318 0.5930 0.3700 -0.0898 0.0168 0.1352 -1 GLY A CA 3 C C . GLY A 1 ? 0.3131 0.5684 0.3599 -0.0415 0.0101 0.1713 -1 GLY A C 4 O O . GLY A 1 ? 0.2421 0.4655 0.3598 -0.0273 -0.0228 0.2131 -1 GLY A O 5 N N . PRO A 2 ? 0.3379 0.6248 0.3531 -0.0447 0.0081 0.1751 0 PRO A N 6 C CA . PRO A 2 ? 0.3529 0.6372 0.3439 0.0032 -0.0065 0.1748 0 PRO A CA 7 C C . PRO A 2 ? 0.3794 0.6562 0.3163 0.0536 0.0056 0.1506 0 PRO A C 8 O O . PRO A 2 ? 0.3777 0.7083 0.2986 0.1700 0.0358 0.1404 0 PRO A O 9 C CB . PRO A 2 ? 0.3326 0.6330 0.3378 -0.0367 -0.0152 0.1853 0 PRO A CB 10 C CG . PRO A 2 ? 0.3663 0.6543 0.3416 -0.0418 -0.0042 0.1767 0 PRO A CG 11 C CD . PRO A 2 ? 0.3485 0.6467 0.3383 -0.0605 0.0004 0.1878 0 PRO A CD 12 N N . MET A 3 ? 0.3192 0.5843 0.2845 -0.0178 -0.0299 0.1584 1 MET A N 13 C CA . MET A 3 ? 0.3096 0.5207 0.2702 -0.0392 0.0137 0.1573 1 MET A CA 14 C C . MET A 3 ? 0.2875 0.4508 0.2714 -0.0646 0.0156 0.1174 1 MET A C 15 O O . MET A 3 ? 0.2780 0.4622 0.2877 -0.0197 0.0128 0.1425 1 MET A O 16 C CB . MET A 3 ? 0.3272 0.5660 0.2877 -0.0175 0.0690 0.1575 1 MET A CB 17 C CG . MET A 3 ? 0.2317 0.4814 0.2752 -0.0006 0.1376 0.2584 1 MET A CG 18 S SD . MET A 3 ? 0.4986 0.7167 0.3701 0.0083 0.0314 0.1265 1 MET A SD 19 C CE . MET A 3 ? 0.4500 0.6882 0.3184 -0.0328 0.0375 0.1146 1 MET A CE 20 N N . ASP A 4 ? 0.2283 0.4296 0.2234 -0.0313 0.0022 0.0834 2 ASP A N 21 C CA . ASP A 4 ? 0.1826 0.3986 0.2046 -0.0807 -0.0318 0.0746 2 ASP A CA 22 C C . ASP A 4 ? 0.1719 0.3619 0.1821 -0.0609 -0.0168 0.0966 2 ASP A C 23 O O . ASP A 4 ? 0.1488 0.4002 0.1874 -0.0612 -0.0177 0.1281 2 ASP A O 24 C CB . ASP A 4 ? 0.2197 0.4530 0.2212 -0.0990 -0.0084 0.0636 2 ASP A CB 25 C CG . ASP A 4 ? 0.2293 0.4837 0.2210 -0.1476 0.0063 0.0600 2 ASP A CG 26 O OD1 . ASP A 4 ? 0.2339 0.5103 0.2134 -0.1153 -0.0198 0.0918 2 ASP A OD1 27 O OD2 . ASP A 4 ? 0.2780 0.5604 0.2529 -0.1257 0.0696 0.0136 2 ASP A OD2 28 N N . PHE A 5 ? 0.1887 0.3580 0.1742 -0.0271 -0.0112 0.0847 3 PHE A N 29 C CA . PHE A 5 ? 0.2014 0.3777 0.1569 0.0382 -0.0044 0.0765 3 PHE A CA 30 C C . PHE A 5 ? 0.1701 0.3764 0.1639 0.0085 0.0085 0.0798 3 PHE A C 31 O O . PHE A 5 ? 0.1391 0.4069 0.1565 -0.0142 -0.0077 0.0960 3 PHE A O 32 C CB . PHE A 5 ? 0.2893 0.3892 0.1675 0.0259 0.0158 0.0602 3 PHE A CB 33 C CG . PHE A 5 ? 0.3138 0.4038 0.1814 0.0619 0.0203 0.0432 3 PHE A CG 34 C CD1 . PHE A 5 ? 0.3714 0.4684 0.2089 0.0665 0.0157 0.0384 3 PHE A CD1 35 C CD2 . PHE A 5 ? 0.3062 0.3665 0.1815 0.0730 -0.0172 0.0368 3 PHE A CD2 36 C CE1 . PHE A 5 ? 0.3715 0.4657 0.2178 0.0630 0.0024 0.0385 3 PHE A CE1 37 C CE2 . PHE A 5 ? 0.3471 0.4107 0.2177 0.0667 -0.0015 0.0403 3 PHE A CE2 38 C CZ . PHE A 5 ? 0.3512 0.4361 0.2247 0.0861 0.0032 0.0322 3 PHE A CZ 39 N N . LEU A 6 ? 0.1428 0.3348 0.1765 0.0226 -0.0192 0.0786 4 LEU A N 40 C CA . LEU A 6 ? 0.1490 0.2982 0.1863 -0.0079 -0.0314 0.0890 4 LEU A CA 41 C C . LEU A 6 ? 0.1150 0.3181 0.1890 -0.0472 -0.0467 0.0442 4 LEU A C 42 O O . LEU A 6 ? 0.1597 0.3536 0.2108 0.0250 -0.0766 0.0160 4 LEU A O 43 C CB . LEU A 6 ? 0.1671 0.3028 0.2025 -0.0111 -0.0178 0.0605 4 LEU A CB 44 C CG . LEU A 6 ? 0.1387 0.2793 0.1969 -0.0344 -0.0091 0.0152 4 LEU A CG 45 C CD1 . LEU A 6 ? 0.1012 0.2785 0.1940 0.0144 0.0342 0.0034 4 LEU A CD1 46 C CD2 . LEU A 6 ? 0.1645 0.2494 0.1895 -0.0047 -0.0208 -0.0193 4 LEU A CD2 47 N N . ARG A 7 ? 0.1265 0.3545 0.2071 -0.0861 -0.0242 0.0534 5 ARG A N 48 C CA . ARG A 7 ? 0.1801 0.3984 0.2186 -0.0692 -0.0177 0.0466 5 ARG A CA 49 C C . ARG A 7 ? 0.1901 0.4252 0.2089 -0.0770 -0.0121 0.0552 5 ARG A C 50 O O . ARG A 7 ? 0.2332 0.4309 0.2472 -0.0480 -0.0043 0.0317 5 ARG A O 51 C CB . ARG A 7 ? 0.2511 0.3971 0.2509 -0.0662 -0.0184 0.0411 5 ARG A CB 52 C CG . ARG A 7 ? 0.3502 0.5036 0.3248 -0.0631 -0.0127 0.0159 5 ARG A CG 53 C CD . ARG A 7 ? 0.4809 0.6255 0.3911 -0.0265 0.0154 0.0203 5 ARG A CD 54 N NE . ARG A 7 ? 0.5384 0.6976 0.4394 -0.0044 0.0139 0.0503 5 ARG A NE 55 C CZ . ARG A 7 ? 0.5841 0.7423 0.4920 0.0181 0.0194 0.0531 5 ARG A CZ 56 N NH1 . ARG A 7 ? 0.5977 0.7687 0.5072 0.0167 0.0259 0.0260 5 ARG A NH1 57 N NH2 . ARG A 7 ? 0.6057 0.7387 0.5104 0.0428 0.0193 0.0702 5 ARG A NH2 58 N N . SER A 8 ? 0.1133 0.4116 0.1707 -0.0530 0.0153 0.0455 6 SER A N 59 C CA . SER A 8 ? 0.0864 0.4528 0.1537 -0.0580 -0.0096 0.0141 6 SER A CA 60 C C . SER A 8 ? 0.0894 0.4385 0.1612 -0.0555 -0.0143 0.0335 6 SER A C 61 O O . SER A 8 ? 0.1164 0.4244 0.1825 -0.0011 -0.0007 0.0290 6 SER A O 62 C CB . SER A 8 ? 0.1616 0.5069 0.1619 -0.0421 0.0062 0.0060 6 SER A CB 63 O OG . SER A 8 ? 0.2551 0.5463 0.1926 -0.1089 0.0339 0.0069 6 SER A OG 64 N N . LEU A 9 ? 0.0951 0.4122 0.1481 -0.0635 -0.0555 0.0663 7 LEU A N 65 C CA . LEU A 9 ? 0.0983 0.3511 0.1485 -0.0956 -0.0222 0.0418 7 LEU A CA 66 C C . LEU A 9 ? 0.1466 0.3917 0.1579 -0.0530 -0.0156 0.0357 7 LEU A C 67 O O . LEU A 9 ? 0.1989 0.4179 0.1633 -0.0351 -0.0094 0.0269 7 LEU A O 68 C CB . LEU A 9 ? 0.0683 0.2981 0.1740 -0.0711 0.0186 0.0524 7 LEU A CB 69 C CG . LEU A 9 ? 0.1195 0.2739 0.1988 -0.0556 0.0531 0.0335 7 LEU A CG 70 C CD1 . LEU A 9 ? 0.0961 0.3337 0.2005 -0.0228 0.0417 0.0395 7 LEU A CD1 71 C CD2 . LEU A 9 ? 0.1872 0.2417 0.2139 -0.0452 0.0793 0.0692 7 LEU A CD2 72 N N . ASP A 10 ? 0.0821 0.4065 0.1460 -0.0337 -0.0081 0.0436 8 ASP A N 73 C CA . ASP A 10 ? 0.0929 0.3430 0.1559 -0.0004 -0.0164 0.0653 8 ASP A CA 74 C C . ASP A 10 ? 0.1304 0.2861 0.1426 -0.0272 -0.0329 0.0482 8 ASP A C 75 O O . ASP A 10 ? 0.1430 0.2967 0.1555 -0.0141 -0.0463 0.0297 8 ASP A O 76 C CB . ASP A 10 ? 0.1139 0.3780 0.1765 -0.0396 -0.0169 0.0399 8 ASP A CB 77 C CG . ASP A 10 ? 0.1358 0.3787 0.1956 -0.0396 -0.0283 0.0146 8 ASP A CG 78 O OD1 . ASP A 10 ? 0.1316 0.4339 0.2056 -0.0662 -0.0430 0.0096 8 ASP A OD1 79 O OD2 . ASP A 10 ? 0.1172 0.4024 0.1917 0.0015 -0.0522 0.0198 8 ASP A OD2 80 N N . TRP A 11 ? 0.1155 0.2579 0.1268 -0.0201 -0.0206 0.0308 9 TRP A N 81 C CA . TRP A 11 ? 0.1047 0.3317 0.1205 -0.0103 -0.0176 0.0453 9 TRP A CA 82 C C . TRP A 11 ? 0.1326 0.3269 0.1392 -0.0737 -0.0101 0.0548 9 TRP A C 83 O O . TRP A 11 ? 0.1992 0.4177 0.1613 -0.1558 0.0110 0.0461 9 TRP A O 84 C CB . TRP A 11 ? 0.1331 0.2809 0.1180 -0.0169 0.0137 0.0413 9 TRP A CB 85 C CG . TRP A 11 ? 0.1583 0.2996 0.1136 0.0238 0.0068 0.0336 9 TRP A CG 86 C CD1 . TRP A 11 ? 0.1544 0.3314 0.1112 -0.0037 0.0406 0.0250 9 TRP A CD1 87 C CD2 . TRP A 11 ? 0.1026 0.2280 0.1056 0.0062 -0.0145 0.0407 9 TRP A CD2 88 N NE1 . TRP A 11 ? 0.1494 0.3365 0.1258 0.0092 0.0036 0.0314 9 TRP A NE1 89 C CE2 . TRP A 11 ? 0.1255 0.2775 0.1195 0.0177 -0.0060 0.0319 9 TRP A CE2 90 C CE3 . TRP A 11 ? 0.1579 0.2286 0.1111 -0.0064 0.0027 0.0022 9 TRP A CE3 91 C CZ2 . TRP A 11 ? 0.0935 0.2954 0.1259 0.0534 0.0068 0.0268 9 TRP A CZ2 92 C CZ3 . TRP A 11 ? 0.1075 0.2195 0.1236 0.0365 0.0333 0.0525 9 TRP A CZ3 93 C CH2 . TRP A 11 ? 0.1303 0.2693 0.1131 0.0306 0.0142 0.0428 9 TRP A CH2 94 N N . THR A 12 ? 0.1413 0.2628 0.1131 -0.0112 0.0035 0.0661 10 THR A N 95 C CA . THR A 12 ? 0.1372 0.2868 0.1279 0.0057 0.0244 0.0542 10 THR A CA 96 C C . THR A 12 ? 0.1347 0.2723 0.1486 -0.0149 0.0043 0.0539 10 THR A C 97 O O . THR A 12 ? 0.1145 0.2935 0.1472 -0.0230 -0.0259 0.0586 10 THR A O 98 C CB . THR A 12 ? 0.1093 0.3030 0.1213 0.0577 -0.0054 0.0566 10 THR A CB 99 O OG1 . THR A 12 ? 0.1552 0.3683 0.1301 0.0430 -0.0202 0.0208 10 THR A OG1 100 C CG2 . THR A 12 ? 0.1083 0.3339 0.1377 0.0394 0.0219 0.0498 10 THR A CG2 101 N N . GLN A 13 ? 0.1403 0.2189 0.1720 -0.0125 0.0054 0.0522 11 GLN A N 102 C CA . GLN A 13 ? 0.1631 0.2206 0.1762 -0.0128 -0.0213 0.0333 11 GLN A CA 103 C C . GLN A 13 ? 0.1557 0.2544 0.1463 -0.0080 -0.0118 0.0524 11 GLN A C 104 O O . GLN A 13 ? 0.1890 0.3371 0.1448 0.0015 0.0107 0.0257 11 GLN A O 105 C CB . GLN A 13 ? 0.2174 0.2457 0.2111 0.0476 -0.0291 0.0401 11 GLN A CB 106 C CG . GLN A 13 ? 0.3312 0.3652 0.2942 0.0286 -0.0009 0.0686 11 GLN A CG 107 C CD . GLN A 13 ? 0.4458 0.5113 0.3453 -0.0063 0.0157 0.0786 11 GLN A CD 108 O OE1 . GLN A 13 ? 0.5071 0.5758 0.3736 -0.0100 0.0456 0.0803 11 GLN A OE1 109 N NE2 . GLN A 13 ? 0.5232 0.5707 0.3784 -0.0132 0.0185 0.1056 11 GLN A NE2 110 N N . VAL A 14 ? 0.1317 0.2465 0.1320 0.0060 -0.0347 0.0377 12 VAL A N 111 C CA . VAL A 14 ? 0.1635 0.2046 0.1292 -0.0399 -0.0251 0.0271 12 VAL A CA 112 C C . VAL A 14 ? 0.1956 0.1875 0.1168 0.0110 0.0168 0.0394 12 VAL A C 113 O O . VAL A 14 ? 0.2245 0.2016 0.1329 -0.0127 0.0347 0.0278 12 VAL A O 114 C CB . VAL A 14 ? 0.1480 0.2351 0.1442 -0.0371 -0.0395 0.0227 12 VAL A CB 115 C CG1 . VAL A 14 ? 0.1632 0.2207 0.1396 -0.0618 -0.0500 0.0042 12 VAL A CG1 116 C CG2 . VAL A 14 ? 0.1768 0.2602 0.1417 0.0019 -0.0280 0.0509 12 VAL A CG2 117 N N . ILE A 15 ? 0.2214 0.2013 0.0886 -0.0321 0.0166 0.0185 13 ILE A N 118 C CA . ILE A 15 ? 0.1748 0.2384 0.0955 -0.0199 0.0128 -0.0136 13 ILE A CA 119 C C . ILE A 15 ? 0.1730 0.2202 0.1086 -0.0362 -0.0105 -0.0098 13 ILE A C 120 O O . ILE A 15 ? 0.2010 0.2008 0.1270 -0.0338 0.0075 0.0271 13 ILE A O 121 C CB . ILE A 15 ? 0.1361 0.2731 0.0933 -0.0376 -0.0013 -0.0300 13 ILE A CB 122 C CG1 . ILE A 15 ? 0.1894 0.2825 0.1179 0.0139 -0.0224 -0.0052 13 ILE A CG1 123 C CG2 . ILE A 15 ? 0.2045 0.2647 0.0942 -0.0104 0.0085 -0.0340 13 ILE A CG2 124 C CD1 . ILE A 15 ? 0.1992 0.2688 0.1416 0.0514 -0.0205 -0.0205 13 ILE A CD1 125 N N . ALA A 16 ? 0.2056 0.2081 0.1210 -0.0277 0.0082 -0.0249 14 ALA A N 126 C CA . ALA A 16 ? 0.2714 0.2050 0.1319 -0.0121 0.0179 -0.0109 14 ALA A CA 127 C C . ALA A 16 ? 0.2750 0.2045 0.1361 0.0108 0.0148 0.0223 14 ALA A C 128 O O . ALA A 16 ? 0.3123 0.2124 0.1508 0.0455 0.0122 0.0000 14 ALA A O 129 C CB . ALA A 16 ? 0.3277 0.2265 0.1327 0.0052 0.0049 0.0172 14 ALA A CB 130 N N . GLY A 17 ? 0.2596 0.2292 0.1219 -0.0048 0.0460 0.0180 15 GLY A N 131 C CA . GLY A 17 ? 0.2187 0.2440 0.1272 0.0217 0.0603 0.0046 15 GLY A CA 132 C C . GLY A 17 ? 0.1935 0.2471 0.1261 0.0605 0.0442 0.0216 15 GLY A C 133 O O . GLY A 17 ? 0.1893 0.2578 0.1295 0.0314 0.0459 0.0034 15 GLY A O 134 N N . GLN A 18 ? 0.1776 0.2525 0.1171 0.0075 -0.0053 0.0394 16 GLN A N 135 C CA . GLN A 18 ? 0.1528 0.2625 0.1192 -0.0148 0.0055 0.0315 16 GLN A CA 136 C C . GLN A 18 ? 0.1167 0.2189 0.1161 0.0233 -0.0147 0.0410 16 GLN A C 137 O O . GLN A 18 ? 0.1329 0.2162 0.1359 0.0160 -0.0071 0.0323 16 GLN A O 138 C CB . GLN A 18 ? 0.1334 0.2936 0.1156 -0.1002 -0.0007 0.0022 16 GLN A CB 139 C CG . GLN A 18 ? 0.1008 0.2697 0.1241 -0.0849 -0.0040 -0.0362 16 GLN A CG 140 C CD . GLN A 18 ? 0.1814 0.2417 0.1340 0.0098 0.0214 0.0115 16 GLN A CD 141 O OE1 . GLN A 18 ? 0.2035 0.2435 0.1462 0.0240 0.0202 0.0218 16 GLN A OE1 142 N NE2 . GLN A 18 ? 0.2219 0.2238 0.1377 0.0092 0.0520 0.0579 16 GLN A NE2 143 N N . TYR A 19 ? 0.1271 0.1875 0.0982 0.0212 -0.0122 0.0230 17 TYR A N 144 C CA . TYR A 19 ? 0.1276 0.1995 0.0966 0.0178 -0.0168 0.0092 17 TYR A CA 145 C C . TYR A 19 ? 0.1060 0.1750 0.1178 -0.0361 0.0018 -0.0038 17 TYR A C 146 O O . TYR A 19 ? 0.0880 0.1933 0.1544 -0.0370 0.0115 0.0184 17 TYR A O 147 C CB . TYR A 19 ? 0.1225 0.2026 0.0869 -0.0154 -0.0531 -0.0023 17 TYR A CB 148 C CG . TYR A 19 ? 0.1859 0.2038 0.1139 -0.0554 -0.0171 0.0053 17 TYR A CG 149 C CD1 . TYR A 19 ? 0.2176 0.2197 0.1649 -0.0758 0.0229 -0.0349 17 TYR A CD1 150 C CD2 . TYR A 19 ? 0.2117 0.2334 0.1243 -0.0684 0.0020 -0.0073 17 TYR A CD2 151 C CE1 . TYR A 19 ? 0.2859 0.2165 0.2030 -0.1007 0.0771 -0.0594 17 TYR A CE1 152 C CE2 . TYR A 19 ? 0.2552 0.2103 0.1611 -0.0864 0.0485 -0.0119 17 TYR A CE2 153 C CZ . TYR A 19 ? 0.3230 0.2228 0.2079 -0.1104 0.0810 -0.0380 17 TYR A CZ 154 O OH . TYR A 19 ? 0.4281 0.2709 0.2359 -0.0784 0.1306 -0.0098 17 TYR A OH 155 N N . VAL A 20 ? 0.0918 0.1898 0.1089 -0.0468 -0.0048 0.0019 18 VAL A N 156 C CA . VAL A 20 ? 0.1311 0.1484 0.1169 -0.0028 0.0122 -0.0058 18 VAL A CA 157 C C . VAL A 20 ? 0.1528 0.1886 0.1364 0.0099 0.0055 0.0390 18 VAL A C 158 O O . VAL A 20 ? 0.1804 0.1980 0.1354 -0.0354 0.0057 0.0361 18 VAL A O 159 C CB . VAL A 20 ? 0.1702 0.1744 0.1255 -0.0482 0.0778 0.0021 18 VAL A CB 160 C CG1 . VAL A 20 ? 0.1456 0.1816 0.1363 -0.0332 0.0704 0.0177 18 VAL A CG1 161 C CG2 . VAL A 20 ? 0.2150 0.2488 0.1390 -0.0762 0.0741 0.0334 18 VAL A CG2 162 N N A SER A 21 ? 0.1119 0.1720 0.1292 0.0451 0.0199 0.0830 19 SER A N 163 N N B SER A 21 ? 0.1326 0.1899 0.1399 0.0385 0.0106 0.0654 19 SER A N 164 C CA A SER A 21 ? 0.1322 0.1953 0.1390 0.0466 0.0020 0.0603 19 SER A CA 165 C CA B SER A 21 ? 0.1395 0.2141 0.1536 0.0507 -0.0035 0.0524 19 SER A CA 166 C C A SER A 21 ? 0.1243 0.2264 0.1535 0.0308 0.0120 0.0595 19 SER A C 167 C C B SER A 21 ? 0.1419 0.2405 0.1638 0.0520 0.0017 0.0350 19 SER A C 168 O O A SER A 21 ? 0.1074 0.2163 0.1599 -0.0269 0.0114 0.0626 19 SER A O 169 O O B SER A 21 ? 0.1443 0.2297 0.1709 0.0455 -0.0037 0.0012 19 SER A O 170 C CB A SER A 21 ? 0.1841 0.2210 0.1451 0.0517 0.0045 0.0716 19 SER A CB 171 C CB B SER A 21 ? 0.1595 0.2355 0.1655 0.0637 -0.0016 0.0797 19 SER A CB 172 O OG A SER A 21 ? 0.2216 0.2189 0.1380 0.0566 0.0049 0.0576 19 SER A OG 173 O OG B SER A 21 ? 0.1721 0.2286 0.1701 0.0711 0.0007 0.0934 19 SER A OG 174 N N . ASN A 22 ? 0.1451 0.2567 0.1738 0.0644 0.0241 0.0415 20 ASN A N 175 C CA . ASN A 22 ? 0.1261 0.2540 0.1949 0.0600 0.0147 0.0325 20 ASN A CA 176 C C . ASN A 22 ? 0.0992 0.2884 0.2262 0.0996 0.0300 0.0405 20 ASN A C 177 O O . ASN A 22 ? 0.1444 0.3412 0.2682 0.0917 0.0367 0.0493 20 ASN A O 178 C CB . ASN A 22 ? 0.1471 0.2592 0.2047 0.0332 -0.0132 0.0157 20 ASN A CB 179 C CG . ASN A 22 ? 0.2107 0.3100 0.2258 0.0100 -0.0035 0.0113 20 ASN A CG 180 O OD1 . ASN A 22 ? 0.2555 0.3772 0.2325 0.0296 0.0169 0.0098 20 ASN A OD1 181 N ND2 . ASN A 22 ? 0.1948 0.2222 0.2367 0.0070 -0.0235 0.0284 20 ASN A ND2 182 N N . PRO A 23 ? 0.1480 0.3250 0.2180 0.0477 -0.0059 0.0351 21 PRO A N 183 C CA . PRO A 23 ? 0.1249 0.2897 0.2399 0.0749 -0.0108 0.0513 21 PRO A CA 184 C C . PRO A 23 ? 0.1840 0.2853 0.2765 0.1025 0.0180 0.0440 21 PRO A C 185 O O . PRO A 23 ? 0.1855 0.2458 0.2890 0.0576 -0.0209 0.0386 21 PRO A O 186 C CB . PRO A 23 ? 0.1275 0.3093 0.2159 0.0532 -0.0175 0.0399 21 PRO A CB 187 C CG . PRO A 23 ? 0.1243 0.3282 0.2125 0.0791 0.0033 0.0514 21 PRO A CG 188 C CD . PRO A 23 ? 0.1410 0.3384 0.2097 0.0570 0.0017 0.0083 21 PRO A CD 189 N N . ARG A 24 ? 0.2495 0.3124 0.2963 0.1262 0.0527 0.0708 22 ARG A N 190 C CA . ARG A 24 ? 0.3014 0.3489 0.3319 0.1114 0.0722 0.0803 22 ARG A CA 191 C C . ARG A 24 ? 0.2399 0.3314 0.2908 0.0805 0.0429 0.0909 22 ARG A C 192 O O . ARG A 24 ? 0.2476 0.3077 0.2788 0.0400 0.0268 0.0996 22 ARG A O 193 C CB . ARG A 24 ? 0.3823 0.4277 0.4104 0.1153 0.1118 0.0735 22 ARG A CB 194 C CG . ARG A 24 ? 0.4974 0.5402 0.4828 0.1184 0.1289 0.0342 22 ARG A CG 195 C CD . ARG A 24 ? 0.6570 0.6961 0.5517 0.0510 0.1055 0.0213 22 ARG A CD 196 N NE . ARG A 24 ? 0.7555 0.7785 0.6010 0.0297 0.0930 0.0137 22 ARG A NE 197 C CZ . ARG A 24 ? 0.8153 0.8277 0.6334 0.0459 0.0894 0.0120 22 ARG A CZ 198 N NH1 . ARG A 24 ? 0.8378 0.8528 0.6457 0.0473 0.0886 0.0112 22 ARG A NH1 199 N NH2 . ARG A 24 ? 0.8341 0.8417 0.6438 0.0527 0.0876 0.0089 22 ARG A NH2 200 N N . PHE A 25 ? 0.1992 0.2813 0.2521 0.0668 0.0050 0.0852 23 PHE A N 201 C CA . PHE A 25 ? 0.2075 0.3036 0.2172 0.0304 -0.0180 0.0486 23 PHE A CA 202 C C . PHE A 25 ? 0.2129 0.3087 0.2112 0.0498 0.0055 0.0513 23 PHE A C 203 O O . PHE A 25 ? 0.2387 0.2936 0.2092 0.0576 0.0056 0.0733 23 PHE A O 204 C CB . PHE A 25 ? 0.2309 0.2898 0.2106 0.0571 -0.0201 0.0459 23 PHE A CB 205 C CG . PHE A 25 ? 0.1761 0.2937 0.1994 0.0093 -0.0051 0.0545 23 PHE A CG 206 C CD1 . PHE A 25 ? 0.1854 0.2899 0.1808 0.0397 -0.0120 0.0197 23 PHE A CD1 207 C CD2 . PHE A 25 ? 0.1693 0.2480 0.2278 -0.0001 0.0083 0.0782 23 PHE A CD2 208 C CE1 . PHE A 25 ? 0.1409 0.2183 0.1599 0.0197 -0.0180 0.0247 23 PHE A CE1 209 C CE2 . PHE A 25 ? 0.1353 0.3069 0.2216 -0.0105 0.0119 0.0547 23 PHE A CE2 210 C CZ . PHE A 25 ? 0.1747 0.2810 0.1882 0.0210 0.0104 0.0203 23 PHE A CZ 211 N N . ASN A 26 ? 0.1811 0.2482 0.1892 0.0217 -0.0296 0.0690 24 ASN A N 212 C CA . ASN A 26 ? 0.2164 0.2015 0.2101 0.0816 -0.0087 0.0856 24 ASN A CA 213 C C . ASN A 26 ? 0.1459 0.2143 0.1855 0.0668 -0.0216 0.0581 24 ASN A C 214 O O . ASN A 26 ? 0.1607 0.2712 0.1870 0.0282 -0.0159 0.0496 24 ASN A O 215 C CB . ASN A 26 ? 0.3379 0.2070 0.2404 0.1244 -0.0287 0.0480 24 ASN A CB 216 C CG . ASN A 26 ? 0.4191 0.3553 0.2984 0.1637 -0.0598 0.0245 24 ASN A CG 217 O OD1 . ASN A 26 ? 0.5011 0.4153 0.3269 0.1634 -0.0490 0.0192 24 ASN A OD1 218 N ND2 . ASN A 26 ? 0.4255 0.4405 0.3245 0.1587 -0.0485 0.0038 24 ASN A ND2 219 N N . ILE A 27 ? 0.1146 0.2396 0.1813 0.0597 -0.0382 0.0382 25 ILE A N 220 C CA . ILE A 27 ? 0.1625 0.2230 0.1873 0.0912 -0.0300 0.0429 25 ILE A CA 221 C C . ILE A 27 ? 0.1943 0.2609 0.1764 0.0381 -0.0538 0.0200 25 ILE A C 222 O O . ILE A 27 ? 0.1582 0.2575 0.1898 0.0176 -0.0386 0.0020 25 ILE A O 223 C CB . ILE A 27 ? 0.1955 0.3069 0.2126 0.0984 -0.0511 0.0431 25 ILE A CB 224 C CG1 . ILE A 27 ? 0.2564 0.2927 0.2451 0.0481 -0.0405 0.0565 25 ILE A CG1 225 C CG2 . ILE A 27 ? 0.2475 0.3937 0.2273 0.0792 -0.0709 0.0344 25 ILE A CG2 226 C CD1 . ILE A 27 ? 0.2820 0.2489 0.2611 0.1104 -0.0330 0.0598 25 ILE A CD1 227 N N . SER A 28 ? 0.2086 0.2688 0.1692 0.0223 -0.0322 0.0065 26 SER A N 228 C CA . SER A 28 ? 0.2018 0.2609 0.1906 -0.0117 -0.0121 0.0203 26 SER A CA 229 C C . SER A 28 ? 0.2026 0.2783 0.1884 0.0157 -0.0108 0.0188 26 SER A C 230 O O . SER A 28 ? 0.2277 0.3079 0.1587 0.0281 -0.0147 0.0053 26 SER A O 231 C CB . SER A 28 ? 0.2983 0.2847 0.2445 0.0139 0.0462 -0.0208 26 SER A CB 232 O OG . SER A 28 ? 0.3912 0.3720 0.2897 0.0044 0.0208 -0.0027 26 SER A OG 233 N N . ASP A 29 ? 0.1590 0.2609 0.1968 0.0823 -0.0424 0.0098 27 ASP A N 234 C CA . ASP A 29 ? 0.1518 0.2145 0.2071 0.0329 -0.0645 0.0140 27 ASP A CA 235 C C . ASP A 29 ? 0.1466 0.2209 0.1819 -0.0026 -0.0592 0.0155 27 ASP A C 236 O O . ASP A 29 ? 0.1899 0.2792 0.1794 0.0294 -0.0603 0.0236 27 ASP A O 237 C CB . ASP A 29 ? 0.1868 0.2674 0.2518 0.0278 -0.0421 0.0149 27 ASP A CB 238 C CG . ASP A 29 ? 0.2765 0.3105 0.2848 0.0457 0.0071 0.0454 27 ASP A CG 239 O OD1 . ASP A 29 ? 0.3351 0.2890 0.3230 0.0791 0.0091 0.0373 27 ASP A OD1 240 O OD2 . ASP A 29 ? 0.3964 0.3813 0.2868 0.0574 0.0105 0.0519 27 ASP A OD2 241 N N . TYR A 30 ? 0.1403 0.1758 0.1643 0.0554 -0.0265 0.0115 28 TYR A N 242 C CA . TYR A 30 ? 0.1331 0.2250 0.1595 0.0233 -0.0072 0.0513 28 TYR A CA 243 C C . TYR A 30 ? 0.1283 0.2043 0.1540 0.0249 -0.0226 0.0200 28 TYR A C 244 O O . TYR A 30 ? 0.1464 0.2049 0.1504 0.0459 -0.0124 -0.0019 28 TYR A O 245 C CB . TYR A 30 ? 0.1249 0.2613 0.1312 0.0226 -0.0111 0.0727 28 TYR A CB 246 C CG . TYR A 30 ? 0.1081 0.3054 0.1356 0.0528 -0.0023 0.0556 28 TYR A CG 247 C CD1 . TYR A 30 ? 0.1370 0.3392 0.1228 0.0000 0.0054 0.0499 28 TYR A CD1 248 C CD2 . TYR A 30 ? 0.0816 0.3187 0.1455 0.0844 0.0032 0.0286 28 TYR A CD2 249 C CE1 . TYR A 30 ? 0.1355 0.3480 0.1286 -0.0059 -0.0070 0.0699 28 TYR A CE1 250 C CE2 . TYR A 30 ? 0.1274 0.3751 0.1590 0.0705 -0.0282 0.0266 28 TYR A CE2 251 C CZ . TYR A 30 ? 0.1280 0.3797 0.1612 0.0209 -0.0040 0.0474 28 TYR A CZ 252 O OH . TYR A 30 ? 0.1455 0.4461 0.1925 0.0234 0.0057 0.0535 28 TYR A OH 253 N N . PHE A 31 ? 0.1120 0.2361 0.1497 -0.0219 -0.0382 0.0305 29 PHE A N 254 C CA . PHE A 31 ? 0.1490 0.2407 0.1309 -0.0305 -0.0118 0.0529 29 PHE A CA 255 C C . PHE A 31 ? 0.1572 0.2441 0.1381 -0.0115 -0.0243 0.0368 29 PHE A C 256 O O . PHE A 31 ? 0.1716 0.2115 0.1609 0.0186 0.0268 0.0252 29 PHE A O 257 C CB . PHE A 31 ? 0.1433 0.1899 0.1024 -0.0378 -0.0159 0.0557 29 PHE A CB 258 C CG . PHE A 31 ? 0.1477 0.2010 0.1122 -0.0171 -0.0199 0.0376 29 PHE A CG 259 C CD1 . PHE A 31 ? 0.1645 0.1888 0.1084 -0.0267 -0.0571 0.0134 29 PHE A CD1 260 C CD2 . PHE A 31 ? 0.1892 0.2208 0.1022 0.0088 0.0369 0.0405 29 PHE A CD2 261 C CE1 . PHE A 31 ? 0.1945 0.1818 0.1083 0.0099 -0.0379 0.0086 29 PHE A CE1 262 C CE2 . PHE A 31 ? 0.2222 0.1959 0.1340 -0.0093 0.0485 0.0063 29 PHE A CE2 263 C CZ . PHE A 31 ? 0.2188 0.1579 0.1220 0.0552 0.0056 0.0006 29 PHE A CZ 264 N N . GLU A 32 ? 0.1281 0.2557 0.1444 0.0021 -0.0235 0.0731 30 GLU A N 265 C CA . GLU A 32 ? 0.1341 0.2689 0.1562 0.0010 -0.0023 0.0738 30 GLU A CA 266 C C . GLU A 32 ? 0.1622 0.2082 0.1487 -0.0186 -0.0234 0.0520 30 GLU A C 267 O O . GLU A 32 ? 0.1745 0.2353 0.1423 -0.0371 -0.0643 0.0485 30 GLU A O 268 C CB . GLU A 32 ? 0.1517 0.3231 0.1716 -0.0036 0.0132 0.0980 30 GLU A CB 269 C CG . GLU A 32 ? 0.1806 0.4002 0.1790 -0.0361 0.0420 0.0686 30 GLU A CG 270 C CD . GLU A 32 ? 0.2244 0.4937 0.2160 -0.0242 0.0548 0.0546 30 GLU A CD 271 O OE1 . GLU A 32 ? 0.2844 0.6090 0.2422 0.0334 0.0717 0.0409 30 GLU A OE1 272 O OE2 . GLU A 32 ? 0.2676 0.5473 0.2218 -0.0023 0.0543 0.0381 30 GLU A OE2 273 N N . ILE A 33 ? 0.1610 0.1971 0.1609 0.0007 -0.0319 0.0571 31 ILE A N 274 C CA . ILE A 33 ? 0.1672 0.2091 0.1710 -0.0372 -0.0145 0.0575 31 ILE A CA 275 C C . ILE A 33 ? 0.1335 0.2111 0.1740 -0.0598 -0.0235 0.0684 31 ILE A C 276 O O . ILE A 33 ? 0.1756 0.2317 0.2140 -0.0546 -0.0112 0.1171 31 ILE A O 277 C CB . ILE A 33 ? 0.1696 0.1886 0.1826 -0.0450 -0.0090 0.0200 31 ILE A CB 278 C CG1 . ILE A 33 ? 0.1940 0.1937 0.1966 -0.0197 0.0216 0.0023 31 ILE A CG1 279 C CG2 . ILE A 33 ? 0.2183 0.2633 0.1876 -0.0665 -0.0383 0.0043 31 ILE A CG2 280 C CD1 . ILE A 33 ? 0.2017 0.2197 0.2118 -0.0418 0.0323 0.0252 31 ILE A CD1 281 N N . VAL A 34 ? 0.0777 0.2409 0.1584 -0.0294 -0.0158 0.0507 32 VAL A N 282 C CA . VAL A 34 ? 0.1027 0.2787 0.1657 -0.0542 -0.0264 0.0413 32 VAL A CA 283 C C . VAL A 34 ? 0.1402 0.2730 0.1977 -0.0564 -0.0304 0.0536 32 VAL A C 284 O O . VAL A 34 ? 0.1340 0.2486 0.1840 -0.0700 -0.0203 0.0436 32 VAL A O 285 C CB . VAL A 34 ? 0.0972 0.2784 0.1490 0.0515 -0.0088 0.0443 32 VAL A CB 286 C CG1 . VAL A 34 ? 0.1260 0.3429 0.1587 0.0974 0.0343 0.0245 32 VAL A CG1 287 C CG2 . VAL A 34 ? 0.1001 0.2800 0.1507 0.0429 -0.0143 0.0529 32 VAL A CG2 288 N N . ARG A 35 ? 0.1601 0.2812 0.2281 -0.0711 -0.0347 0.0687 33 ARG A N 289 C CA . ARG A 35 ? 0.1840 0.2614 0.2416 -0.0140 -0.0325 0.0538 33 ARG A CA 290 C C . ARG A 35 ? 0.1847 0.2692 0.2075 -0.0323 0.0044 0.0651 33 ARG A C 291 O O . ARG A 35 ? 0.1845 0.3458 0.1997 -0.0324 0.0462 0.0573 33 ARG A O 292 C CB . ARG A 35 ? 0.2338 0.2760 0.2922 -0.0028 -0.0560 0.0840 33 ARG A CB 293 C CG . ARG A 35 ? 0.3424 0.3745 0.3303 -0.0129 -0.0538 0.0368 33 ARG A CG 294 C CD . ARG A 35 ? 0.4412 0.4482 0.3547 0.0099 -0.0069 0.0252 33 ARG A CD 295 N NE . ARG A 35 ? 0.4837 0.4956 0.3636 -0.0263 0.0019 0.0221 33 ARG A NE 296 C CZ . ARG A 35 ? 0.5175 0.5338 0.3701 -0.0519 0.0085 0.0202 33 ARG A CZ 297 N NH1 . ARG A 35 ? 0.5289 0.5468 0.3722 -0.0599 0.0105 0.0197 33 ARG A NH1 298 N NH2 . ARG A 35 ? 0.5289 0.5468 0.3722 -0.0599 0.0107 0.0196 33 ARG A NH2 299 N N . GLN A 36 ? 0.2026 0.2241 0.1901 -0.0817 0.0063 0.0449 34 GLN A N 300 C CA . GLN A 36 ? 0.1739 0.2133 0.1910 -0.1055 0.0109 0.0482 34 GLN A CA 301 C C . GLN A 36 ? 0.1999 0.2763 0.2295 -0.0503 0.0041 0.0322 34 GLN A C 302 O O . GLN A 36 ? 0.2249 0.2993 0.2551 -0.0779 0.0107 0.0138 34 GLN A O 303 C CB . GLN A 36 ? 0.1795 0.1897 0.1703 -0.1057 0.0152 0.0351 34 GLN A CB 304 C CG . GLN A 36 ? 0.1819 0.1801 0.1676 -0.0658 0.0147 0.0264 34 GLN A CG 305 C CD . GLN A 36 ? 0.1829 0.1883 0.1573 0.0108 0.0035 0.0324 34 GLN A CD 306 O OE1 . GLN A 36 ? 0.1870 0.2269 0.1679 0.0274 0.0092 0.0228 34 GLN A OE1 307 N NE2 . GLN A 36 ? 0.1761 0.2562 0.1501 0.0059 -0.0009 0.0188 34 GLN A NE2 308 N N . PRO A 37 ? 0.1610 0.3003 0.2498 -0.0596 -0.0436 0.0225 35 PRO A N 309 C CA . PRO A 37 ? 0.2053 0.3271 0.2646 -0.0510 -0.0593 0.0030 35 PRO A CA 310 C C . PRO A 37 ? 0.2482 0.3379 0.2704 -0.0204 -0.0530 -0.0016 35 PRO A C 311 O O . PRO A 37 ? 0.2253 0.3311 0.2773 -0.0131 -0.0500 0.0052 35 PRO A O 312 C CB . PRO A 37 ? 0.1767 0.3519 0.2698 -0.0508 -0.0553 0.0122 35 PRO A CB 313 C CG . PRO A 37 ? 0.1319 0.3137 0.2533 -0.0405 -0.0739 0.0225 35 PRO A CG 314 C CD . PRO A 37 ? 0.1314 0.3043 0.2443 -0.0388 -0.0623 0.0057 35 PRO A CD 315 N N . GLY A 38 ? 0.2968 0.3381 0.2595 0.0193 -0.0597 -0.0021 36 GLY A N 316 C CA . GLY A 38 ? 0.3110 0.3737 0.2575 0.0321 -0.0561 -0.0223 36 GLY A CA 317 C C . GLY A 38 ? 0.3069 0.4193 0.2390 0.0039 -0.0419 -0.0498 36 GLY A C 318 O O . GLY A 38 ? 0.4090 0.4549 0.2658 -0.0179 -0.0445 -0.0958 36 GLY A O 319 N N . ASP A 39 ? 0.1412 0.3414 0.2112 -0.0136 -0.0461 -0.0276 37 ASP A N 320 C CA . ASP A 39 ? 0.1383 0.3127 0.2056 -0.0260 -0.0172 -0.0114 37 ASP A CA 321 C C . ASP A 39 ? 0.0767 0.2816 0.1887 -0.0229 -0.0186 0.0083 37 ASP A C 322 O O . ASP A 39 ? 0.0923 0.2960 0.2157 -0.0156 -0.0186 0.0134 37 ASP A O 323 C CB . ASP A 39 ? 0.1029 0.2900 0.2091 -0.0129 -0.0303 -0.0143 37 ASP A CB 324 C CG . ASP A 39 ? 0.1347 0.3085 0.2070 -0.0217 -0.0112 0.0066 37 ASP A CG 325 O OD1 . ASP A 39 ? 0.1639 0.2496 0.2133 -0.0336 0.0097 0.0038 37 ASP A OD1 326 O OD2 . ASP A 39 ? 0.1484 0.2984 0.1826 -0.0473 0.0157 -0.0097 37 ASP A OD2 327 N N . GLY A 40 ? 0.1065 0.2626 0.1609 -0.0554 0.0107 0.0287 38 GLY A N 328 C CA . GLY A 40 ? 0.1010 0.1747 0.1587 -0.0657 0.0200 0.0070 38 GLY A CA 329 C C . GLY A 40 ? 0.1079 0.1972 0.1224 -0.0593 0.0143 -0.0382 38 GLY A C 330 O O . GLY A 40 ? 0.1367 0.2580 0.1038 -0.0573 0.0228 -0.0228 38 GLY A O 331 N N . ASN A 41 ? 0.1015 0.2126 0.1338 -0.0477 0.0113 -0.0386 39 ASN A N 332 C CA . ASN A 41 ? 0.0660 0.2451 0.1154 -0.0458 0.0300 -0.0373 39 ASN A CA 333 C C . ASN A 41 ? 0.0833 0.2310 0.0999 -0.0223 0.0258 0.0104 39 ASN A C 334 O O . ASN A 41 ? 0.0944 0.2165 0.1319 -0.0316 -0.0056 -0.0077 39 ASN A O 335 C CB . ASN A 41 ? 0.0776 0.2448 0.1239 -0.0226 0.0206 -0.0469 39 ASN A CB 336 C CG . ASN A 41 ? 0.0486 0.2414 0.1391 -0.0439 0.0189 -0.0077 39 ASN A CG 337 O OD1 . ASN A 41 ? 0.1098 0.3169 0.1447 -0.0337 0.0316 -0.0065 39 ASN A OD1 338 N ND2 . ASN A 41 ? 0.0813 0.2525 0.1600 -0.0473 0.0301 -0.0249 39 ASN A ND2 339 N N . CYS A 42 ? 0.1042 0.2301 0.0698 0.0161 0.0170 0.0227 40 CYS A N 340 C CA . CYS A 42 ? 0.0764 0.2404 0.1073 -0.0014 -0.0132 0.0025 40 CYS A CA 341 C C . CYS A 42 ? 0.1106 0.2152 0.1010 -0.0102 -0.0209 0.0341 40 CYS A C 342 O O . CYS A 42 ? 0.1127 0.2429 0.0857 0.0023 -0.0012 0.0260 40 CYS A O 343 C CB . CYS A 42 ? 0.1119 0.2343 0.1060 -0.0056 0.0328 -0.0286 40 CYS A CB 344 S SG . CYS A 42 ? 0.1049 0.2284 0.1025 -0.0131 0.0069 -0.0044 40 CYS A SG 345 N N . PHE A 43 ? 0.1177 0.1885 0.1006 -0.0190 0.0086 0.0360 41 PHE A N 346 C CA . PHE A 43 ? 0.1460 0.1333 0.0883 -0.0317 0.0379 0.0361 41 PHE A CA 347 C C . PHE A 43 ? 0.1328 0.2266 0.0907 0.0026 0.0147 -0.0152 41 PHE A C 348 O O . PHE A 43 ? 0.1138 0.2027 0.0945 -0.0170 -0.0140 0.0073 41 PHE A O 349 C CB . PHE A 43 ? 0.1202 0.2068 0.0806 0.0017 0.0406 0.0344 41 PHE A CB 350 C CG . PHE A 43 ? 0.1354 0.2009 0.0920 -0.0270 0.0161 0.0095 41 PHE A CG 351 C CD1 . PHE A 43 ? 0.0855 0.2141 0.1093 -0.0718 0.0286 -0.0100 41 PHE A CD1 352 C CD2 . PHE A 43 ? 0.1479 0.1265 0.1091 -0.0380 0.0308 0.0148 41 PHE A CD2 353 C CE1 . PHE A 43 ? 0.0472 0.2148 0.1310 0.0037 0.0436 0.0207 41 PHE A CE1 354 C CE2 . PHE A 43 ? 0.1068 0.1994 0.1288 -0.0120 0.0075 0.0156 41 PHE A CE2 355 C CZ . PHE A 43 ? 0.0749 0.1959 0.1429 0.0137 0.0230 0.0233 41 PHE A CZ 356 N N . TYR A 44 ? 0.0932 0.1993 0.0972 0.0253 0.0376 0.0130 42 TYR A N 357 C CA . TYR A 44 ? 0.0946 0.2019 0.0772 0.0337 0.0201 0.0202 42 TYR A CA 358 C C . TYR A 44 ? 0.1045 0.2279 0.0829 0.0051 0.0125 0.0532 42 TYR A C 359 O O . TYR A 44 ? 0.0931 0.2237 0.0944 0.0008 0.0207 0.0405 42 TYR A O 360 C CB . TYR A 44 ? 0.0799 0.1956 0.0813 0.0202 0.0097 0.0178 42 TYR A CB 361 C CG . TYR A 44 ? 0.1114 0.2124 0.0789 -0.0113 0.0372 -0.0355 42 TYR A CG 362 C CD1 . TYR A 44 ? 0.0603 0.2223 0.0857 -0.0292 0.0083 -0.0228 42 TYR A CD1 363 C CD2 . TYR A 44 ? 0.0982 0.2499 0.0700 -0.0045 0.0137 -0.0398 42 TYR A CD2 364 C CE1 . TYR A 44 ? 0.0743 0.2567 0.0945 -0.0074 -0.0002 -0.0488 42 TYR A CE1 365 C CE2 . TYR A 44 ? 0.0930 0.2576 0.0776 0.0047 0.0138 -0.0176 42 TYR A CE2 366 C CZ . TYR A 44 ? 0.0899 0.2829 0.0767 -0.0454 0.0153 -0.0170 42 TYR A CZ 367 O OH . TYR A 44 ? 0.1164 0.2633 0.0771 -0.0361 0.0266 0.0083 42 TYR A OH 368 N N . HIS A 45 ? 0.0765 0.2230 0.0854 -0.0115 0.0141 0.0368 43 HIS A N 369 C CA . HIS A 45 ? 0.0619 0.2056 0.1026 -0.0399 0.0153 0.0423 43 HIS A CA 370 C C . HIS A 45 ? 0.1073 0.2131 0.0959 -0.0110 0.0197 0.0168 43 HIS A C 371 O O . HIS A 45 ? 0.1464 0.2129 0.0802 -0.0205 0.0106 0.0347 43 HIS A O 372 C CB . HIS A 45 ? 0.0437 0.2171 0.1201 -0.0219 0.0162 0.0674 43 HIS A CB 373 C CG . HIS A 45 ? 0.0726 0.2492 0.1337 -0.0152 0.0135 0.0215 43 HIS A CG 374 N ND1 . HIS A 45 ? 0.0888 0.2915 0.1618 0.0245 0.0129 0.0137 43 HIS A ND1 375 C CD2 . HIS A 45 ? 0.0336 0.2593 0.1448 -0.0535 -0.0250 -0.0034 43 HIS A CD2 376 C CE1 . HIS A 45 ? 0.1075 0.2385 0.1536 0.0099 -0.0144 0.0185 43 HIS A CE1 377 N NE2 . HIS A 45 ? 0.0764 0.2687 0.1366 -0.0382 -0.0575 -0.0130 43 HIS A NE2 378 N N . SER A 46 ? 0.0879 0.2462 0.1073 -0.0058 0.0170 -0.0001 44 SER A N 379 C CA . SER A 46 ? 0.1052 0.1926 0.0987 -0.0334 0.0034 -0.0366 44 SER A CA 380 C C . SER A 46 ? 0.1332 0.1932 0.0978 -0.0261 -0.0010 -0.0080 44 SER A C 381 O O . SER A 46 ? 0.1587 0.2597 0.0954 -0.0462 -0.0009 -0.0140 44 SER A O 382 C CB . SER A 46 ? 0.0796 0.1226 0.1093 0.0093 0.0010 -0.0338 44 SER A CB 383 O OG . SER A 46 ? 0.0924 0.1849 0.1127 0.0002 0.0022 -0.0106 44 SER A OG 384 N N . ILE A 47 ? 0.1018 0.1731 0.1417 -0.0122 0.0238 -0.0008 45 ILE A N 385 C CA . ILE A 47 ? 0.1357 0.1849 0.1439 -0.0136 0.0218 -0.0067 45 ILE A CA 386 C C . ILE A 47 ? 0.0932 0.2026 0.1211 -0.0083 0.0336 -0.0085 45 ILE A C 387 O O . ILE A 47 ? 0.1028 0.2693 0.1099 0.0247 0.0319 -0.0148 45 ILE A O 388 C CB . ILE A 47 ? 0.1504 0.1114 0.1679 -0.0325 0.0057 0.0009 45 ILE A CB 389 C CG1 . ILE A 47 ? 0.1521 0.2235 0.2279 -0.0003 -0.0127 -0.0362 45 ILE A CG1 390 C CG2 . ILE A 47 ? 0.1462 0.0834 0.1634 -0.0505 -0.0100 0.0029 45 ILE A CG2 391 C CD1 . ILE A 47 ? 0.2022 0.2961 0.2428 -0.0113 -0.0172 -0.0573 45 ILE A CD1 392 N N . ALA A 48 ? 0.0637 0.2016 0.1026 -0.0139 0.0428 -0.0048 46 ALA A N 393 C CA . ALA A 48 ? 0.0658 0.3069 0.0737 0.0295 -0.0104 0.0042 46 ALA A CA 394 C C . ALA A 48 ? 0.1281 0.2415 0.0968 0.0149 0.0112 0.0163 46 ALA A C 395 O O . ALA A 48 ? 0.1501 0.2389 0.0851 0.0025 0.0174 -0.0270 46 ALA A O 396 C CB . ALA A 48 ? 0.0947 0.3605 0.0828 0.0376 0.0012 0.0005 46 ALA A CB 397 N N . GLU A 49 ? 0.0963 0.2021 0.1243 0.0168 0.0046 0.0338 47 GLU A N 398 C CA . GLU A 49 ? 0.1189 0.1910 0.1107 -0.0087 -0.0025 0.0234 47 GLU A CA 399 C C . GLU A 49 ? 0.0863 0.2595 0.1044 -0.0455 -0.0136 0.0328 47 GLU A C 400 O O . GLU A 49 ? 0.1540 0.3211 0.1038 -0.0368 -0.0067 0.0419 47 GLU A O 401 C CB . GLU A 49 ? 0.1992 0.1645 0.1339 0.0175 -0.0084 0.0470 47 GLU A CB 402 C CG . GLU A 49 ? 0.2382 0.2902 0.1655 0.0123 0.0292 0.0644 47 GLU A CG 403 C CD . GLU A 49 ? 0.3162 0.3853 0.2086 0.0008 0.0394 0.1054 47 GLU A CD 404 O OE1 . GLU A 49 ? 0.3249 0.4994 0.2522 0.0363 0.0288 0.1344 47 GLU A OE1 405 O OE2 . GLU A 49 ? 0.3598 0.3510 0.1880 0.0074 0.0941 0.1101 47 GLU A OE2 406 N N . LEU A 50 ? 0.1018 0.2096 0.1198 -0.0400 0.0082 0.0053 48 LEU A N 407 C CA . LEU A 50 ? 0.0636 0.2209 0.1270 -0.0092 -0.0131 -0.0235 48 LEU A CA 408 C C . LEU A 50 ? 0.1044 0.2569 0.1541 0.0336 -0.0330 -0.0225 48 LEU A C 409 O O . LEU A 50 ? 0.1264 0.2795 0.1595 0.0110 -0.0653 -0.0316 48 LEU A O 410 C CB . LEU A 50 ? 0.0717 0.1999 0.1283 0.0382 0.0281 -0.0058 48 LEU A CB 411 C CG . LEU A 50 ? 0.1514 0.1933 0.1160 0.0649 0.0546 0.0198 48 LEU A CG 412 C CD1 . LEU A 50 ? 0.1401 0.1759 0.1583 0.0335 0.0737 0.0262 48 LEU A CD1 413 C CD2 . LEU A 50 ? 0.1735 0.1912 0.0796 0.0549 0.0348 0.0219 48 LEU A CD2 414 N N . THR A 51 ? 0.1000 0.1847 0.1362 0.0220 0.0064 0.0131 49 THR A N 415 C CA . THR A 51 ? 0.0898 0.1816 0.1301 0.0113 0.0392 0.0013 49 THR A CA 416 C C . THR A 51 ? 0.1188 0.1936 0.1159 -0.0062 0.0151 -0.0514 49 THR A C 417 O O . THR A 51 ? 0.1892 0.1921 0.1148 -0.0008 0.0262 -0.0370 49 THR A O 418 C CB . THR A 51 ? 0.0748 0.2164 0.1380 -0.0347 0.0267 0.0135 49 THR A CB 419 O OG1 . THR A 51 ? 0.1434 0.1974 0.1136 -0.0112 0.0087 0.0138 49 THR A OG1 420 C CG2 . THR A 51 ? 0.0433 0.2641 0.1978 0.0076 0.0220 0.0024 49 THR A CG2 421 N N . MET A 52 ? 0.1202 0.2258 0.1048 -0.0216 0.0277 -0.0428 50 MET A N 422 C CA . MET A 52 ? 0.1098 0.2486 0.1082 -0.0391 0.0150 -0.0448 50 MET A CA 423 C C . MET A 52 ? 0.1534 0.2881 0.1088 -0.0670 0.0243 -0.0312 50 MET A C 424 O O . MET A 52 ? 0.1826 0.3085 0.1040 -0.0698 0.0275 0.0017 50 MET A O 425 C CB . MET A 52 ? 0.0826 0.2912 0.1152 0.0004 0.0111 0.0003 50 MET A CB 426 C CG . MET A 52 ? 0.0317 0.3130 0.1237 -0.0276 0.0069 0.0155 50 MET A CG 427 S SD . MET A 52 ? 0.0963 0.3437 0.1363 0.0081 0.0059 -0.0153 50 MET A SD 428 C CE . MET A 52 ? 0.0998 0.2720 0.1591 0.0271 0.0067 -0.0057 50 MET A CE 429 N N . PRO A 53 ? 0.1594 0.3267 0.1018 -0.0960 0.0303 -0.0214 51 PRO A N 430 C CA . PRO A 53 ? 0.2208 0.4135 0.1263 -0.0740 0.0372 -0.0433 51 PRO A CA 431 C C . PRO A 53 ? 0.2491 0.4789 0.1737 -0.0650 0.0448 -0.0727 51 PRO A C 432 O O . PRO A 53 ? 0.2739 0.5005 0.1770 -0.0776 0.0572 -0.1293 51 PRO A O 433 C CB . PRO A 53 ? 0.2384 0.4191 0.1167 -0.1134 0.0442 -0.0332 51 PRO A CB 434 C CG . PRO A 53 ? 0.2412 0.3984 0.0957 -0.0776 0.0476 -0.0164 51 PRO A CG 435 C CD . PRO A 53 ? 0.1976 0.3513 0.0946 -0.0904 0.0164 0.0079 51 PRO A CD 436 N N . ASN A 54 ? 0.2499 0.5438 0.2195 -0.0624 0.0627 -0.0255 52 ASN A N 437 C CA . ASN A 54 ? 0.3315 0.6441 0.2746 -0.0926 0.0393 -0.0290 52 ASN A CA 438 C C . ASN A 54 ? 0.3501 0.6722 0.3075 -0.1073 0.0163 -0.0215 52 ASN A C 439 O O . ASN A 54 ? 0.4082 0.7155 0.3317 -0.1018 0.0252 -0.0099 52 ASN A O 440 C CB . ASN A 54 ? 0.3904 0.6769 0.3013 -0.0430 0.0485 -0.0342 52 ASN A CB 441 C CG . ASN A 54 ? 0.4456 0.6802 0.3059 -0.0288 0.0559 -0.0358 52 ASN A CG 442 O OD1 . ASN A 54 ? 0.4648 0.6819 0.3079 -0.0243 0.0590 -0.0367 52 ASN A OD1 443 N ND2 . ASN A 54 ? 0.4648 0.6820 0.3079 -0.0243 0.0590 -0.0367 52 ASN A ND2 444 N N . LYS A 55 ? 0.3055 0.6345 0.2923 -0.1363 -0.0370 -0.0239 53 LYS A N 445 C CA . LYS A 55 ? 0.2835 0.5867 0.3061 -0.1110 -0.0419 -0.0024 53 LYS A CA 446 C C . LYS A 55 ? 0.3100 0.5856 0.3126 -0.0934 -0.0386 0.0324 53 LYS A C 447 O O . LYS A 55 ? 0.3336 0.5854 0.3219 -0.0838 -0.0390 0.0729 53 LYS A O 448 C CB . LYS A 55 ? 0.3065 0.5197 0.3139 -0.0954 -0.0452 -0.0119 53 LYS A CB 449 C CG . LYS A 55 ? 0.3275 0.4794 0.3302 -0.0686 -0.0350 0.0187 53 LYS A CG 450 C CD . LYS A 55 ? 0.2969 0.4146 0.3237 -0.0867 -0.0320 0.0212 53 LYS A CD 451 C CE . LYS A 55 ? 0.2771 0.3820 0.3267 -0.0957 -0.0293 0.0229 53 LYS A CE 452 N NZ . LYS A 55 ? 0.3299 0.3589 0.3244 -0.0376 -0.0325 0.0499 53 LYS A NZ 453 N N . THR A 56 ? 0.3041 0.5709 0.3002 -0.0884 -0.0354 0.0095 54 THR A N 454 C CA . THR A 56 ? 0.2405 0.5565 0.2980 -0.0655 -0.0170 -0.0062 54 THR A CA 455 C C . THR A 56 ? 0.2054 0.5541 0.2369 -0.1002 -0.0682 0.0663 54 THR A C 456 O O . THR A 56 ? 0.2092 0.6154 0.1845 -0.0988 -0.0619 0.0455 54 THR A O 457 C CB . THR A 56 ? 0.2618 0.6117 0.3536 -0.0460 0.0137 -0.1001 54 THR A CB 458 O OG1 . THR A 56 ? 0.3132 0.6415 0.3955 -0.0014 0.0179 -0.1229 54 THR A OG1 459 C CG2 . THR A 56 ? 0.3702 0.6362 0.3746 -0.0254 0.0749 -0.1049 54 THR A CG2 460 N N . ASP A 57 ? 0.1909 0.5005 0.2307 -0.1306 -0.0688 0.1121 55 ASP A N 461 C CA . ASP A 57 ? 0.2475 0.5102 0.2423 -0.1216 -0.0078 0.1166 55 ASP A CA 462 C C . ASP A 57 ? 0.2363 0.4921 0.2156 -0.1049 0.0176 0.0842 55 ASP A C 463 O O . ASP A 57 ? 0.2484 0.5338 0.2244 -0.1356 0.0395 0.0625 55 ASP A O 464 C CB . ASP A 57 ? 0.2351 0.5709 0.2719 -0.1053 -0.0287 0.1283 55 ASP A CB 465 C CG . ASP A 57 ? 0.2257 0.6197 0.2970 -0.1073 -0.0353 0.1691 55 ASP A CG 466 O OD1 . ASP A 57 ? 0.2169 0.6700 0.3179 -0.1283 -0.0375 0.1626 55 ASP A OD1 467 O OD2 . ASP A 57 ? 0.2091 0.6385 0.3035 -0.1135 -0.0296 0.1944 55 ASP A OD2 468 N N . HIS A 58 ? 0.1482 0.3826 0.1855 -0.0421 -0.0134 0.0844 56 HIS A N 469 C CA . HIS A 58 ? 0.1324 0.3681 0.1645 -0.0121 -0.0222 0.0570 56 HIS A CA 470 C C . HIS A 58 ? 0.1167 0.3653 0.1506 0.0095 -0.0071 0.0152 56 HIS A C 471 O O . HIS A 58 ? 0.1211 0.4098 0.1551 0.0206 0.0111 0.0126 56 HIS A O 472 C CB . HIS A 58 ? 0.1243 0.3350 0.1543 0.0034 -0.0726 0.0436 56 HIS A CB 473 C CG . HIS A 58 ? 0.1168 0.3495 0.1553 0.0321 -0.0597 0.0953 56 HIS A CG 474 N ND1 . HIS A 58 ? 0.1787 0.3818 0.1654 -0.0310 0.0183 0.0777 56 HIS A ND1 475 C CD2 . HIS A 58 ? 0.0336 0.3114 0.1445 -0.0476 -0.0503 0.1141 56 HIS A CD2 476 C CE1 . HIS A 58 ? 0.0957 0.3986 0.1301 -0.0292 -0.0394 0.1019 56 HIS A CE1 477 N NE2 . HIS A 58 ? 0.1297 0.4454 0.1625 -0.0447 0.0068 0.0384 56 HIS A NE2 478 N N . SER A 59 ? 0.1220 0.3428 0.1279 -0.0248 -0.0089 -0.0331 57 SER A N 479 C CA . SER A 59 ? 0.1108 0.3401 0.1114 -0.0078 0.0113 -0.0677 57 SER A CA 480 C C . SER A 59 ? 0.0912 0.3101 0.1219 -0.0103 0.0096 -0.0449 57 SER A C 481 O O . SER A 59 ? 0.1075 0.3116 0.1304 -0.0071 0.0181 -0.0327 57 SER A O 482 C CB . SER A 59 ? 0.1836 0.3900 0.1104 -0.0412 0.0245 -0.0770 57 SER A CB 483 O OG . SER A 59 ? 0.2326 0.4263 0.1285 -0.0560 0.0456 -0.0605 57 SER A OG 484 N N . TYR A 60 ? 0.0690 0.3026 0.1135 0.0201 0.0181 -0.0405 58 TYR A N 485 C CA . TYR A 60 ? 0.0975 0.2662 0.1169 0.0418 0.0405 -0.0046 58 TYR A CA 486 C C . TYR A 60 ? 0.1309 0.2915 0.1146 0.0502 0.0164 -0.0117 58 TYR A C 487 O O . TYR A 60 ? 0.1212 0.3281 0.0839 -0.0096 0.0204 -0.0047 58 TYR A O 488 C CB . TYR A 60 ? 0.0389 0.2545 0.1189 0.0215 0.0304 -0.0168 58 TYR A CB 489 C CG . TYR A 60 ? 0.0649 0.2648 0.1407 -0.0278 0.0174 -0.0153 58 TYR A CG 490 C CD1 . TYR A 60 ? 0.0789 0.2976 0.1549 0.0074 -0.0007 -0.0091 58 TYR A CD1 491 C CD2 . TYR A 60 ? 0.0625 0.2829 0.1677 -0.0416 0.0065 -0.0472 58 TYR A CD2 492 C CE1 . TYR A 60 ? 0.0981 0.2973 0.1769 -0.0214 0.0390 0.0237 58 TYR A CE1 493 C CE2 . TYR A 60 ? 0.0712 0.2906 0.1815 -0.0458 -0.0042 -0.0188 58 TYR A CE2 494 C CZ . TYR A 60 ? 0.1214 0.3341 0.2000 -0.0528 0.0217 -0.0295 58 TYR A CZ 495 O OH . TYR A 60 ? 0.1245 0.3540 0.2271 -0.0467 0.0665 -0.0432 58 TYR A OH 496 N N . HIS A 61 ? 0.1237 0.2773 0.1221 0.0856 -0.0075 0.0020 59 HIS A N 497 C CA . HIS A 61 ? 0.1066 0.2913 0.1437 0.0401 0.0073 0.0377 59 HIS A CA 498 C C . HIS A 61 ? 0.1063 0.2749 0.1297 -0.0159 -0.0034 0.0314 59 HIS A C 499 O O . HIS A 61 ? 0.1456 0.2841 0.1270 -0.0064 -0.0044 0.0581 59 HIS A O 500 C CB . HIS A 61 ? 0.0780 0.2844 0.1731 -0.0153 -0.0155 0.0012 59 HIS A CB 501 C CG . HIS A 61 ? 0.0992 0.2937 0.1727 -0.0339 -0.0191 -0.0159 59 HIS A CG 502 N ND1 . HIS A 61 ? 0.1212 0.2728 0.1850 -0.0125 -0.0010 -0.0475 59 HIS A ND1 503 C CD2 . HIS A 61 ? 0.1473 0.2610 0.1742 -0.0657 -0.0060 0.0059 59 HIS A CD2 504 C CE1 . HIS A 61 ? 0.1711 0.2924 0.1786 -0.0060 -0.0015 -0.0249 59 HIS A CE1 505 N NE2 . HIS A 61 ? 0.1364 0.2902 0.1670 -0.0526 0.0181 -0.0121 59 HIS A NE2 506 N N . TYR A 62 ? 0.0703 0.2624 0.1399 -0.0306 0.0061 0.0067 60 TYR A N 507 C CA . TYR A 62 ? 0.1195 0.2371 0.1266 -0.0119 0.0188 -0.0367 60 TYR A CA 508 C C . TYR A 62 ? 0.1372 0.2315 0.1071 0.0235 0.0423 -0.0139 60 TYR A C 509 O O . TYR A 62 ? 0.1575 0.1963 0.1181 -0.0087 0.0335 -0.0013 60 TYR A O 510 C CB . TYR A 62 ? 0.2321 0.2434 0.1319 -0.0321 0.0215 -0.0290 60 TYR A CB 511 C CG . TYR A 62 ? 0.3550 0.2786 0.1598 -0.0194 0.0459 -0.0508 60 TYR A CG 512 C CD1 . TYR A 62 ? 0.4345 0.3457 0.2019 -0.0393 0.0636 -0.0710 60 TYR A CD1 513 C CD2 . TYR A 62 ? 0.4015 0.3166 0.1753 -0.0623 0.0545 -0.0377 60 TYR A CD2 514 C CE1 . TYR A 62 ? 0.4605 0.3805 0.2160 -0.0668 0.0324 -0.0792 60 TYR A CE1 515 C CE2 . TYR A 62 ? 0.4515 0.3549 0.2042 -0.0414 0.0530 -0.0411 60 TYR A CE2 516 C CZ . TYR A 62 ? 0.5077 0.3983 0.2313 -0.0570 0.0458 -0.0815 60 TYR A CZ 517 O OH . TYR A 62 ? 0.5748 0.4509 0.2503 -0.0415 0.0368 -0.0909 60 TYR A OH 518 N N . ILE A 63 ? 0.1423 0.2197 0.0799 0.0258 0.0290 -0.0241 61 ILE A N 519 C CA . ILE A 63 ? 0.0678 0.2042 0.0636 0.0495 -0.0096 0.0057 61 ILE A CA 520 C C . ILE A 63 ? 0.0894 0.2028 0.0904 -0.0029 -0.0009 -0.0018 61 ILE A C 521 O O . ILE A 63 ? 0.0992 0.2703 0.0931 0.0193 0.0264 0.0205 61 ILE A O 522 C CB . ILE A 63 ? 0.0953 0.2220 0.0615 0.0438 0.0006 -0.0146 61 ILE A CB 523 C CG1 . ILE A 63 ? 0.1084 0.2200 0.0838 -0.0389 -0.0296 -0.0469 61 ILE A CG1 524 C CG2 . ILE A 63 ? 0.1090 0.2308 0.0812 0.0700 0.0290 -0.0134 61 ILE A CG2 525 C CD1 . ILE A 63 ? 0.1449 0.2271 0.1141 -0.0572 -0.0242 -0.0302 61 ILE A CD1 526 N N . LYS A 64 ? 0.0853 0.2230 0.0920 -0.0003 -0.0363 -0.0488 62 LYS A N 527 C CA . LYS A 64 ? 0.1234 0.1813 0.0978 -0.0215 -0.0232 -0.0307 62 LYS A CA 528 C C . LYS A 64 ? 0.1213 0.1924 0.1248 0.0108 -0.0088 -0.0337 62 LYS A C 529 O O . LYS A 64 ? 0.1048 0.1890 0.1428 0.0241 0.0003 -0.0023 62 LYS A O 530 C CB . LYS A 64 ? 0.1421 0.2053 0.0909 0.0542 -0.0257 -0.0724 62 LYS A CB 531 C CG . LYS A 64 ? 0.1539 0.2157 0.0734 0.0503 -0.0143 -0.0913 62 LYS A CG 532 C CD . LYS A 64 ? 0.1639 0.2089 0.0647 -0.0158 -0.0435 -0.0664 62 LYS A CD 533 C CE . LYS A 64 ? 0.1786 0.1825 0.0744 0.0098 -0.0315 -0.0490 62 LYS A CE 534 N NZ . LYS A 64 ? 0.1739 0.2497 0.0796 -0.0006 -0.0469 -0.0382 62 LYS A NZ 535 N N . ARG A 65 ? 0.1307 0.1700 0.1578 0.0162 -0.0025 -0.0089 63 ARG A N 536 C CA . ARG A 65 ? 0.1597 0.2070 0.1665 0.0343 0.0118 0.0182 63 ARG A CA 537 C C . ARG A 65 ? 0.1457 0.2257 0.1525 0.0700 -0.0218 0.0224 63 ARG A C 538 O O . ARG A 65 ? 0.1826 0.2127 0.1456 0.0764 -0.0077 -0.0179 63 ARG A O 539 C CB . ARG A 65 ? 0.1475 0.3176 0.1882 0.0742 0.0139 0.0016 63 ARG A CB 540 C CG . ARG A 65 ? 0.2171 0.3851 0.2266 0.1060 0.0334 -0.0062 63 ARG A CG 541 C CD . ARG A 65 ? 0.3089 0.4755 0.2723 0.0792 0.0378 -0.0057 63 ARG A CD 542 N NE . ARG A 65 ? 0.3741 0.5781 0.3161 0.0592 0.0283 0.0110 63 ARG A NE 543 C CZ . ARG A 65 ? 0.3832 0.6273 0.3437 0.0808 0.0139 0.0188 63 ARG A CZ 544 N NH1 . ARG A 65 ? 0.3588 0.6140 0.3719 0.0642 0.0223 0.0319 63 ARG A NH1 545 N NH2 . ARG A 65 ? 0.4005 0.6688 0.3403 0.1047 0.0014 0.0286 63 ARG A NH2 546 N N . LEU A 66 ? 0.1296 0.1924 0.1383 0.0382 -0.0118 -0.0365 64 LEU A N 547 C CA . LEU A 66 ? 0.1561 0.2719 0.1299 -0.0069 -0.0040 -0.0493 64 LEU A CA 548 C C . LEU A 66 ? 0.1289 0.2569 0.1054 -0.0158 -0.0069 -0.0267 64 LEU A C 549 O O . LEU A 66 ? 0.1438 0.2559 0.1228 0.0002 0.0058 0.0020 64 LEU A O 550 C CB . LEU A 66 ? 0.2065 0.2596 0.1226 -0.0102 -0.0170 -0.0392 64 LEU A CB 551 C CG . LEU A 66 ? 0.2383 0.2600 0.1471 0.0792 0.0100 -0.0560 64 LEU A CG 552 C CD1 . LEU A 66 ? 0.1976 0.3482 0.1640 0.0847 -0.0123 -0.0680 64 LEU A CD1 553 C CD2 . LEU A 66 ? 0.3299 0.3317 0.1772 0.0589 0.0263 -0.0708 64 LEU A CD2 554 N N . THR A 67 ? 0.0849 0.2286 0.0884 0.0096 -0.0251 -0.0216 65 THR A N 555 C CA . THR A 67 ? 0.1222 0.2191 0.0963 0.0248 0.0033 0.0086 65 THR A CA 556 C C . THR A 67 ? 0.1072 0.2108 0.1135 -0.0006 -0.0048 -0.0120 65 THR A C 557 O O . THR A 67 ? 0.1442 0.2084 0.1048 0.0243 0.0173 0.0189 65 THR A O 558 C CB . THR A 67 ? 0.1119 0.1898 0.0939 0.0544 -0.0053 -0.0274 65 THR A CB 559 O OG1 . THR A 67 ? 0.1413 0.1974 0.1088 0.0081 -0.0109 -0.0216 65 THR A OG1 560 C CG2 . THR A 67 ? 0.1169 0.2207 0.0872 0.0406 0.0143 -0.0256 65 THR A CG2 561 N N . GLU A 68 ? 0.1334 0.2285 0.1395 0.0240 -0.0022 -0.0122 66 GLU A N 562 C CA . GLU A 68 ? 0.1194 0.1924 0.1614 0.0686 -0.0145 0.0371 66 GLU A CA 563 C C . GLU A 68 ? 0.1849 0.2124 0.1606 0.0709 -0.0043 0.0159 66 GLU A C 564 O O . GLU A 68 ? 0.1877 0.2096 0.1431 0.0151 0.0084 0.0418 66 GLU A O 565 C CB . GLU A 68 ? 0.0934 0.2225 0.1853 0.0765 -0.0435 0.0473 66 GLU A CB 566 C CG . GLU A 68 ? 0.1892 0.3177 0.2524 0.1075 -0.0086 0.0069 66 GLU A CG 567 C CD . GLU A 68 ? 0.2309 0.4088 0.3070 0.1110 -0.0211 0.0040 66 GLU A CD 568 O OE1 . GLU A 68 ? 0.2336 0.4665 0.3419 0.0372 0.0028 -0.0051 66 GLU A OE1 569 O OE2 . GLU A 68 ? 0.2844 0.5003 0.3382 0.1467 -0.0173 -0.0030 66 GLU A OE2 570 N N . SER A 69 ? 0.1747 0.1868 0.1635 0.0565 -0.0222 -0.0058 67 SER A N 571 C CA . SER A 69 ? 0.2317 0.2285 0.1783 0.0469 -0.0040 -0.0196 67 SER A CA 572 C C . SER A 69 ? 0.2180 0.2219 0.1684 0.0360 -0.0128 0.0002 67 SER A C 573 O O . SER A 69 ? 0.2656 0.1530 0.1608 0.0292 0.0265 -0.0102 67 SER A O 574 C CB . SER A 69 ? 0.3341 0.2406 0.2050 -0.0395 -0.0193 -0.0669 67 SER A CB 575 O OG . SER A 69 ? 0.4012 0.3879 0.2462 0.0496 0.0234 -0.0566 67 SER A OG 576 N N . ALA A 70 ? 0.1419 0.2525 0.1657 0.0372 -0.0558 -0.0236 68 ALA A N 577 C CA . ALA A 70 ? 0.1019 0.2500 0.1538 0.0668 -0.0428 0.0030 68 ALA A CA 578 C C . ALA A 70 ? 0.1538 0.2376 0.1458 0.0186 -0.0171 0.0050 68 ALA A C 579 O O . ALA A 70 ? 0.1851 0.2260 0.1595 0.0399 -0.0338 -0.0022 68 ALA A O 580 C CB . ALA A 70 ? 0.1313 0.2092 0.1649 0.0614 -0.0432 0.0087 68 ALA A CB 581 N N . ALA A 71 ? 0.1486 0.2129 0.1206 0.0259 -0.0046 -0.0168 69 ALA A N 582 C CA . ALA A 71 ? 0.1551 0.1409 0.1205 0.0176 -0.0284 -0.0031 69 ALA A CA 583 C C . ALA A 71 ? 0.1919 0.2144 0.1522 0.0141 -0.0090 0.0218 69 ALA A C 584 O O . ALA A 71 ? 0.1970 0.2343 0.1421 0.0231 0.0137 0.0363 69 ALA A O 585 C CB . ALA A 71 ? 0.1740 0.1436 0.1238 0.0033 -0.0402 -0.0439 69 ALA A CB 586 N N . ARG A 72 ? 0.2169 0.1980 0.1865 0.0671 -0.0149 0.0403 70 ARG A N 587 C CA . ARG A 72 ? 0.2215 0.2219 0.2403 0.0441 -0.0075 0.0353 70 ARG A CA 588 C C . ARG A 72 ? 0.2565 0.2685 0.2522 0.0387 -0.0084 0.0519 70 ARG A C 589 O O . ARG A 72 ? 0.2681 0.2907 0.2651 0.0334 -0.0203 0.0700 70 ARG A O 590 C CB . ARG A 72 ? 0.1929 0.2574 0.2823 0.0757 -0.0067 0.0106 70 ARG A CB 591 C CG . ARG A 72 ? 0.2540 0.3087 0.3269 0.0851 -0.0109 -0.0227 70 ARG A CG 592 C CD . ARG A 72 ? 0.2871 0.3806 0.3677 0.0805 -0.0280 -0.0195 70 ARG A CD 593 N NE . ARG A 72 ? 0.3380 0.4453 0.3931 0.1346 -0.0330 -0.0257 70 ARG A NE 594 C CZ . ARG A 72 ? 0.3921 0.4690 0.4167 0.1637 -0.0174 -0.0154 70 ARG A CZ 595 N NH1 . ARG A 72 ? 0.4000 0.4624 0.4136 0.1815 -0.0146 0.0119 70 ARG A NH1 596 N NH2 . ARG A 72 ? 0.4073 0.4594 0.4317 0.1622 -0.0026 -0.0253 70 ARG A NH2 597 N N . LYS A 73 ? 0.1966 0.2119 0.2458 0.0087 -0.0072 0.0268 71 LYS A N 598 C CA . LYS A 73 ? 0.2304 0.2395 0.2441 0.0493 0.0008 0.0027 71 LYS A CA 599 C C . LYS A 73 ? 0.2393 0.1917 0.2118 0.0756 0.0259 0.0471 71 LYS A C 600 O O . LYS A 73 ? 0.3247 0.2353 0.2406 0.0469 0.0477 0.0575 71 LYS A O 601 C CB . LYS A 73 ? 0.2512 0.2441 0.2673 0.0515 0.0209 0.0096 71 LYS A CB 602 C CG . LYS A 73 ? 0.3133 0.3168 0.3093 0.0801 0.0389 -0.0358 71 LYS A CG 603 C CD . LYS A 73 ? 0.3670 0.3899 0.3541 0.0620 0.0510 -0.0468 71 LYS A CD 604 C CE . LYS A 73 ? 0.4050 0.4659 0.3963 0.0507 0.0973 -0.0616 71 LYS A CE 605 N NZ . LYS A 73 ? 0.4303 0.4988 0.4146 0.1407 0.1246 -0.0985 71 LYS A NZ 606 N N . TYR A 74 ? 0.2536 0.1324 0.1779 0.0379 0.0051 0.0042 72 TYR A N 607 C CA . TYR A 74 ? 0.2126 0.1980 0.1591 0.0053 -0.0178 0.0363 72 TYR A CA 608 C C . TYR A 74 ? 0.2064 0.2353 0.1493 0.0137 0.0057 0.0290 72 TYR A C 609 O O . TYR A 74 ? 0.2125 0.2847 0.1683 0.0101 0.0129 0.0372 72 TYR A O 610 C CB . TYR A 74 ? 0.1739 0.1868 0.1580 -0.0197 -0.0512 0.0604 72 TYR A CB 611 C CG . TYR A 74 ? 0.2574 0.2057 0.1726 -0.0025 -0.0306 0.0488 72 TYR A CG 612 C CD1 . TYR A 74 ? 0.3505 0.3103 0.1895 -0.0443 -0.0132 0.0394 72 TYR A CD1 613 C CD2 . TYR A 74 ? 0.2591 0.2234 0.1810 0.0105 -0.0314 0.0540 72 TYR A CD2 614 C CE1 . TYR A 74 ? 0.3585 0.3400 0.2110 -0.0624 -0.0275 0.0195 72 TYR A CE1 615 C CE2 . TYR A 74 ? 0.2860 0.2799 0.2050 -0.0186 -0.0519 0.0263 72 TYR A CE2 616 C CZ . TYR A 74 ? 0.3437 0.3503 0.2180 -0.0548 -0.0466 -0.0083 72 TYR A CZ 617 O OH . TYR A 74 ? 0.3416 0.3655 0.2435 -0.0798 -0.0562 -0.0559 72 TYR A OH 618 N N . TYR A 75 ? 0.1754 0.2139 0.1304 0.0032 -0.0056 0.0503 73 TYR A N 619 C CA . TYR A 75 ? 0.1640 0.2559 0.1378 0.0099 -0.0081 0.0520 73 TYR A CA 620 C C . TYR A 75 ? 0.2099 0.2645 0.1704 0.0199 0.0183 0.0621 73 TYR A C 621 O O . TYR A 75 ? 0.2364 0.2746 0.1939 0.0144 0.0208 0.0438 73 TYR A O 622 C CB . TYR A 75 ? 0.1309 0.3146 0.1319 -0.0024 0.0024 0.0041 73 TYR A CB 623 C CG . TYR A 75 ? 0.1687 0.3135 0.1319 0.0269 0.0064 -0.0061 73 TYR A CG 624 C CD1 . TYR A 75 ? 0.1443 0.2562 0.1309 -0.0082 0.0164 -0.0169 73 TYR A CD1 625 C CD2 . TYR A 75 ? 0.1671 0.3260 0.1249 0.0301 -0.0055 -0.0241 73 TYR A CD2 626 C CE1 . TYR A 75 ? 0.1887 0.2724 0.1186 -0.0172 0.0173 0.0075 73 TYR A CE1 627 C CE2 . TYR A 75 ? 0.2056 0.3192 0.1233 -0.0051 0.0305 -0.0171 73 TYR A CE2 628 C CZ . TYR A 75 ? 0.2032 0.2627 0.1173 -0.0166 0.0154 -0.0313 73 TYR A CZ 629 O OH . TYR A 75 ? 0.2028 0.2613 0.1457 -0.0135 0.0088 -0.0157 73 TYR A OH 630 N N . GLN A 76 ? 0.2788 0.2709 0.1966 0.0874 0.0660 0.0931 74 GLN A N 631 C CA . GLN A 76 ? 0.3480 0.3377 0.2298 0.0989 0.0885 0.1300 74 GLN A CA 632 C C . GLN A 76 ? 0.3684 0.3291 0.2331 0.0529 0.1223 0.1135 74 GLN A C 633 O O . GLN A 76 ? 0.4047 0.4141 0.2311 0.0179 0.1517 0.0592 74 GLN A O 634 C CB . GLN A 76 ? 0.4176 0.4085 0.2884 0.1407 0.0881 0.1263 74 GLN A CB 635 C CG . GLN A 76 ? 0.5421 0.5398 0.3530 0.1094 0.0717 0.1062 74 GLN A CG 636 C CD . GLN A 76 ? 0.6201 0.6332 0.4069 0.0803 0.0868 0.0508 74 GLN A CD 637 O OE1 . GLN A 76 ? 0.6793 0.6835 0.4253 0.0606 0.1025 0.0328 74 GLN A OE1 638 N NE2 . GLN A 76 ? 0.6133 0.6341 0.4348 0.0905 0.0887 0.0566 74 GLN A NE2 639 N N . GLU A 77 ? 0.3353 0.2923 0.2396 0.0422 0.0888 0.1217 75 GLU A N 640 C CA . GLU A 77 ? 0.3488 0.3101 0.2597 -0.0001 0.0942 0.0755 75 GLU A CA 641 C C . GLU A 77 ? 0.2696 0.2982 0.2481 0.0366 0.0535 0.0840 75 GLU A C 642 O O . GLU A 77 ? 0.3020 0.3046 0.2753 -0.0010 0.0277 0.0951 75 GLU A O 643 C CB . GLU A 77 ? 0.4088 0.4059 0.2959 -0.0319 0.1064 0.0466 75 GLU A CB 644 C CG . GLU A 77 ? 0.4590 0.4546 0.3015 -0.0185 0.1060 0.0449 75 GLU A CG 645 C CD . GLU A 77 ? 0.5001 0.4963 0.3066 -0.0069 0.1061 0.0422 75 GLU A CD 646 O OE1 . GLU A 77 ? 0.5141 0.5106 0.3085 -0.0030 0.1061 0.0411 75 GLU A OE1 647 O OE2 . GLU A 77 ? 0.5141 0.5106 0.3085 -0.0030 0.1061 0.0411 75 GLU A OE2 648 N N . GLU A 78 ? 0.1791 0.2360 0.2037 0.0191 0.0361 0.0846 76 GLU A N 649 C CA . GLU A 78 ? 0.1527 0.2031 0.1602 -0.0071 0.0399 0.0755 76 GLU A CA 650 C C . GLU A 78 ? 0.1180 0.2462 0.1676 -0.0220 0.0317 0.0352 76 GLU A C 651 O O . GLU A 78 ? 0.1739 0.2566 0.1417 -0.0213 0.0236 0.0360 76 GLU A O 652 C CB . GLU A 78 ? 0.0910 0.2615 0.1305 -0.0058 0.0233 0.0415 76 GLU A CB 653 C CG . GLU A 78 ? 0.1102 0.2546 0.1272 0.0133 -0.0347 0.0152 76 GLU A CG 654 C CD . GLU A 78 ? 0.1670 0.2779 0.1469 0.0437 -0.0116 -0.0025 76 GLU A CD 655 O OE1 . GLU A 78 ? 0.2257 0.3156 0.1488 0.0694 0.0056 -0.0035 76 GLU A OE1 656 O OE2 . GLU A 78 ? 0.2029 0.2836 0.1862 -0.0068 0.0044 -0.0121 76 GLU A OE2 657 N N . PRO A 79 ? 0.1106 0.3289 0.1802 0.0045 0.0071 -0.0143 77 PRO A N 658 C CA . PRO A 79 ? 0.1148 0.3352 0.1928 0.0244 0.0012 -0.0251 77 PRO A CA 659 C C . PRO A 79 ? 0.1952 0.2796 0.1403 0.0142 0.0257 -0.0267 77 PRO A C 660 O O . PRO A 79 ? 0.2274 0.2724 0.1129 0.0062 0.0415 -0.0155 77 PRO A O 661 C CB . PRO A 79 ? 0.1444 0.3904 0.2192 0.0354 -0.0101 -0.0560 77 PRO A CB 662 C CG . PRO A 79 ? 0.1662 0.3966 0.2336 0.0348 0.0291 -0.0814 77 PRO A CG 663 C CD . PRO A 79 ? 0.0855 0.3756 0.2315 0.0028 0.0143 -0.0533 77 PRO A CD 664 N N . GLU A 80 ? 0.2622 0.2495 0.1137 0.0327 0.0183 0.0008 78 GLU A N 665 C CA . GLU A 80 ? 0.2948 0.2332 0.1046 0.0642 0.0345 0.0468 78 GLU A CA 666 C C . GLU A 80 ? 0.2781 0.2636 0.1216 0.0264 0.0396 0.0377 78 GLU A C 667 O O . GLU A 80 ? 0.3102 0.2451 0.1181 -0.0123 0.0329 0.0231 78 GLU A O 668 C CB . GLU A 80 ? 0.3350 0.2221 0.1105 0.1002 0.0272 0.0597 78 GLU A CB 669 C CG . GLU A 80 ? 0.3094 0.2447 0.1252 0.0827 0.0206 0.0692 78 GLU A CG 670 C CD . GLU A 80 ? 0.2506 0.2531 0.1248 0.0358 0.0164 0.0478 78 GLU A CD 671 O OE1 . GLU A 80 ? 0.2383 0.2399 0.1237 0.0283 0.0056 -0.0040 78 GLU A OE1 672 O OE2 . GLU A 80 ? 0.2350 0.3190 0.1515 -0.0633 0.0112 0.0281 78 GLU A OE2 673 N N . ALA A 81 ? 0.2437 0.2491 0.1535 0.0447 0.0470 0.0091 79 ALA A N 674 C CA . ALA A 81 ? 0.2336 0.2698 0.1884 0.0525 0.0255 0.0108 79 ALA A CA 675 C C . ALA A 81 ? 0.2350 0.2958 0.1963 0.0352 0.0257 0.0190 79 ALA A C 676 O O . ALA A 81 ? 0.2144 0.3100 0.1986 0.0335 -0.0121 0.0013 79 ALA A O 677 C CB . ALA A 81 ? 0.2111 0.3267 0.2250 0.0821 0.0341 -0.0196 79 ALA A CB 678 N N . ARG A 82 ? 0.2296 0.2983 0.1888 0.0335 0.0609 0.0143 80 ARG A N 679 C CA . ARG A 82 ? 0.2934 0.3815 0.1792 0.0126 0.0537 0.0209 80 ARG A CA 680 C C . ARG A 82 ? 0.2873 0.3899 0.1444 0.0358 0.0138 0.0131 80 ARG A C 681 O O . ARG A 82 ? 0.3673 0.4560 0.1430 0.0065 -0.0028 0.0341 80 ARG A O 682 C CB . ARG A 82 ? 0.3314 0.4568 0.2195 0.0567 0.0852 0.0210 80 ARG A CB 683 C CG . ARG A 82 ? 0.4056 0.5651 0.2897 0.0572 0.1066 -0.0132 80 ARG A CG 684 C CD . ARG A 82 ? 0.4702 0.6521 0.3686 0.0822 0.1136 -0.0205 80 ARG A CD 685 N NE . ARG A 82 ? 0.5034 0.6756 0.4163 0.1432 0.1541 -0.0362 80 ARG A NE 686 C CZ . ARG A 82 ? 0.4702 0.6431 0.4289 0.1517 0.2199 -0.0704 80 ARG A CZ 687 N NH1 . ARG A 82 ? 0.4583 0.5770 0.4020 0.0884 0.2701 -0.0943 80 ARG A NH1 688 N NH2 . ARG A 82 ? 0.3970 0.6541 0.4485 0.1855 0.2063 -0.0807 80 ARG A NH2 689 N N . LEU A 83 ? 0.2004 0.3321 0.1208 0.0518 0.0213 0.0211 81 LEU A N 690 C CA . LEU A 83 ? 0.1455 0.3651 0.1293 0.0213 -0.0147 -0.0207 81 LEU A CA 691 C C . LEU A 83 ? 0.1525 0.3917 0.1611 -0.0119 -0.0066 -0.0624 81 LEU A C 692 O O . LEU A 83 ? 0.1891 0.4434 0.1927 -0.0149 0.0154 -0.1286 81 LEU A O 693 C CB . LEU A 83 ? 0.1933 0.2986 0.1049 0.0141 0.0067 -0.0126 81 LEU A CB 694 C CG . LEU A 83 ? 0.1649 0.2773 0.0924 0.0157 0.0192 -0.0382 81 LEU A CG 695 C CD1 . LEU A 83 ? 0.1061 0.3041 0.0896 0.0102 -0.0035 0.0171 81 LEU A CD1 696 C CD2 . LEU A 83 ? 0.1966 0.2589 0.0934 0.0439 0.0714 -0.0167 81 LEU A CD2 697 N N . VAL A 84 ? 0.1743 0.4106 0.1680 0.0290 -0.0033 -0.0134 82 VAL A N 698 C CA . VAL A 84 ? 0.1758 0.4115 0.1675 0.0414 -0.0267 -0.0113 82 VAL A CA 699 C C . VAL A 84 ? 0.2206 0.4376 0.1696 0.0459 -0.0031 -0.0061 82 VAL A C 700 O O . VAL A 84 ? 0.2212 0.4594 0.1566 0.0229 -0.0629 -0.0261 82 VAL A O 701 C CB . VAL A 84 ? 0.1257 0.4016 0.1701 0.0664 -0.0578 -0.0280 82 VAL A CB 702 C CG1 . VAL A 84 ? 0.1633 0.3866 0.1772 0.0672 -0.0547 -0.0316 82 VAL A CG1 703 C CG2 . VAL A 84 ? 0.1175 0.4186 0.1734 0.0153 -0.0769 -0.0342 82 VAL A CG2 704 N N . GLY A 85 ? 0.2416 0.4141 0.1614 0.0517 0.0386 0.0584 83 GLY A N 705 C CA . GLY A 85 ? 0.2927 0.4801 0.1656 0.0866 0.0047 0.0409 83 GLY A CA 706 C C . GLY A 85 ? 0.2640 0.4975 0.1759 0.0315 -0.0259 0.0370 83 GLY A C 707 O O . GLY A 85 ? 0.3313 0.5951 0.2051 0.0381 -0.0429 -0.0095 83 GLY A O 708 N N . LEU A 86 ? 0.1960 0.3942 0.1659 0.0029 -0.0167 0.0337 84 LEU A N 709 C CA . LEU A 86 ? 0.1846 0.3769 0.1543 -0.0248 -0.0356 0.0696 84 LEU A CA 710 C C . LEU A 86 ? 0.1767 0.3197 0.1432 -0.0143 -0.0366 0.0771 84 LEU A C 711 O O . LEU A 86 ? 0.2148 0.3565 0.1469 -0.0179 -0.0171 0.0569 84 LEU A O 712 C CB . LEU A 86 ? 0.2142 0.3910 0.1623 -0.0627 -0.0398 0.0531 84 LEU A CB 713 C CG . LEU A 86 ? 0.2527 0.3493 0.1658 0.0354 -0.0395 0.0234 84 LEU A CG 714 C CD1 . LEU A 86 ? 0.2331 0.3250 0.1793 -0.0088 0.0078 0.0153 84 LEU A CD1 715 C CD2 . LEU A 86 ? 0.2878 0.4230 0.1945 0.0253 -0.0585 0.0035 84 LEU A CD2 716 N N . SER A 87 ? 0.2058 0.3472 0.1376 -0.0139 -0.0122 0.0727 85 SER A N 717 C CA . SER A 87 ? 0.2194 0.3363 0.1425 -0.0063 -0.0200 0.0701 85 SER A CA 718 C C . SER A 87 ? 0.2321 0.3180 0.1389 -0.0095 -0.0270 0.0524 85 SER A C 719 O O . SER A 87 ? 0.2505 0.3252 0.1289 -0.0226 -0.0317 0.0698 85 SER A O 720 C CB . SER A 87 ? 0.2581 0.3944 0.1613 0.0516 0.0062 0.0900 85 SER A CB 721 O OG . SER A 87 ? 0.2676 0.4038 0.1701 0.0827 0.0124 0.0909 85 SER A OG 722 N N . LEU A 88 ? 0.2060 0.3067 0.1430 0.0208 -0.0269 0.0339 86 LEU A N 723 C CA . LEU A 88 ? 0.2195 0.3006 0.1458 -0.0081 -0.0254 0.0235 86 LEU A CA 724 C C . LEU A 88 ? 0.1862 0.3274 0.1647 0.0562 -0.0397 0.0310 86 LEU A C 725 O O . LEU A 88 ? 0.2058 0.3612 0.1567 0.0433 -0.0228 0.0512 86 LEU A O 726 C CB . LEU A 88 ? 0.2437 0.2819 0.1496 0.0089 -0.0323 0.0244 86 LEU A CB 727 C CG . LEU A 88 ? 0.2573 0.2845 0.1678 0.0206 -0.0122 0.0212 86 LEU A CG 728 C CD1 . LEU A 88 ? 0.2108 0.2410 0.1624 0.0141 -0.0818 0.0389 86 LEU A CD1 729 C CD2 . LEU A 88 ? 0.2857 0.3124 0.1938 0.0167 0.0028 -0.0059 86 LEU A CD2 730 N N . GLU A 89 ? 0.1615 0.3348 0.2003 0.0667 -0.0141 0.0581 87 GLU A N 731 C CA . GLU A 89 ? 0.1706 0.3624 0.2188 0.0357 -0.0211 0.0581 87 GLU A CA 732 C C . GLU A 89 ? 0.1376 0.3499 0.1911 0.0241 -0.0185 0.0519 87 GLU A C 733 O O . GLU A 89 ? 0.1462 0.3847 0.1664 -0.0223 -0.0059 0.0358 87 GLU A O 734 C CB . GLU A 89 ? 0.2375 0.4398 0.2319 0.0733 -0.0035 0.0665 87 GLU A CB 735 C CG . GLU A 89 ? 0.2996 0.4975 0.2414 0.0676 0.0031 0.0593 87 GLU A CG 736 C CD . GLU A 89 ? 0.3513 0.5445 0.2486 0.0631 0.0083 0.0540 87 GLU A CD 737 O OE1 . GLU A 89 ? 0.3695 0.5606 0.2508 0.0614 0.0104 0.0520 87 GLU A OE1 738 O OE2 . GLU A 89 ? 0.3695 0.5607 0.2508 0.0614 0.0104 0.0520 87 GLU A OE2 739 N N . ASP A 90 ? 0.1628 0.3258 0.1798 0.0334 -0.0320 0.0338 88 ASP A N 740 C CA . ASP A 90 ? 0.2013 0.3422 0.1648 0.0329 -0.0548 0.0338 88 ASP A CA 741 C C . ASP A 90 ? 0.1756 0.3273 0.1583 0.0145 -0.0466 0.0408 88 ASP A C 742 O O . ASP A 90 ? 0.1917 0.2994 0.1699 0.0283 -0.0342 0.0503 88 ASP A O 743 C CB . ASP A 90 ? 0.2033 0.4050 0.1764 0.0672 -0.0752 0.0352 88 ASP A CB 744 C CG . ASP A 90 ? 0.2554 0.5076 0.2186 0.0369 -0.0815 0.0276 88 ASP A CG 745 O OD1 . ASP A 90 ? 0.2710 0.5585 0.2428 0.0785 -0.0982 0.0225 88 ASP A OD1 746 O OD2 . ASP A 90 ? 0.2675 0.5393 0.2267 -0.0014 -0.1089 0.0412 88 ASP A OD2 747 N N . TYR A 91 ? 0.1599 0.3026 0.1279 0.0268 -0.0445 0.0215 89 TYR A N 748 C CA . TYR A 91 ? 0.1121 0.3096 0.1010 -0.0059 -0.0346 0.0238 89 TYR A CA 749 C C . TYR A 91 ? 0.0957 0.2938 0.1152 0.0176 -0.0312 0.0321 89 TYR A C 750 O O . TYR A 91 ? 0.1154 0.3161 0.1353 0.0419 0.0021 0.0522 89 TYR A O 751 C CB . TYR A 91 ? 0.1426 0.3141 0.1009 0.0112 -0.0379 0.0266 89 TYR A CB 752 C CG . TYR A 91 ? 0.1319 0.2732 0.0881 0.0051 -0.0130 0.0189 89 TYR A CG 753 C CD1 . TYR A 91 ? 0.1392 0.3089 0.1025 0.0020 -0.0068 0.0377 89 TYR A CD1 754 C CD2 . TYR A 91 ? 0.1255 0.2879 0.0833 -0.0444 -0.0701 0.0169 89 TYR A CD2 755 C CE1 . TYR A 91 ? 0.1519 0.3218 0.1052 -0.0140 -0.0186 0.0254 89 TYR A CE1 756 C CE2 . TYR A 91 ? 0.1381 0.2596 0.1136 0.0264 -0.0407 0.0145 89 TYR A CE2 757 C CZ . TYR A 91 ? 0.1231 0.2608 0.0980 0.0001 -0.0477 -0.0074 89 TYR A CZ 758 O OH . TYR A 91 ? 0.1646 0.2547 0.0875 -0.0107 -0.0122 -0.0188 89 TYR A OH 759 N N . LEU A 92 ? 0.1045 0.3478 0.1173 0.0368 -0.0186 0.0188 90 LEU A N 760 C CA . LEU A 92 ? 0.1577 0.3104 0.1329 -0.0253 -0.0156 0.0050 90 LEU A CA 761 C C . LEU A 92 ? 0.1600 0.3680 0.1474 0.0003 -0.0085 0.0191 90 LEU A C 762 O O . LEU A 92 ? 0.1448 0.3508 0.1525 -0.0011 -0.0024 0.0315 90 LEU A O 763 C CB . LEU A 92 ? 0.1873 0.2926 0.1306 -0.0092 -0.0210 0.0117 90 LEU A CB 764 C CG . LEU A 92 ? 0.2147 0.2668 0.1347 -0.0150 -0.0378 0.0027 90 LEU A CG 765 C CD1 . LEU A 92 ? 0.2292 0.2132 0.1571 0.0395 -0.0306 -0.0017 90 LEU A CD1 766 C CD2 . LEU A 92 ? 0.1803 0.2842 0.1266 -0.0485 -0.0568 -0.0251 90 LEU A CD2 767 N N . LYS A 93 ? 0.1659 0.3371 0.1330 0.0343 -0.0388 0.0123 91 LYS A N 768 C CA . LYS A 93 ? 0.1458 0.3225 0.1443 0.0223 -0.0581 0.0455 91 LYS A CA 769 C C . LYS A 93 ? 0.1321 0.3252 0.1653 0.0074 -0.0378 0.0228 91 LYS A C 770 O O . LYS A 93 ? 0.1094 0.3648 0.2063 -0.0266 -0.0088 0.0000 91 LYS A O 771 C CB . LYS A 93 ? 0.1483 0.3942 0.1630 -0.0304 -0.0916 0.0748 91 LYS A CB 772 C CG . LYS A 93 ? 0.1881 0.4225 0.1690 -0.0016 -0.0852 0.0765 91 LYS A CG 773 C CD . LYS A 93 ? 0.2236 0.4517 0.1739 0.0194 -0.0763 0.0780 91 LYS A CD 774 C CE . LYS A 93 ? 0.2490 0.4764 0.1771 0.0317 -0.0692 0.0796 91 LYS A CE 775 N NZ . LYS A 93 ? 0.2621 0.4894 0.1783 0.0380 -0.0664 0.0809 91 LYS A NZ 776 N N . ARG A 94 ? 0.1239 0.2945 0.1451 0.0402 -0.0541 0.0133 92 ARG A N 777 C CA . ARG A 94 ? 0.1374 0.3157 0.1477 0.0705 -0.0373 -0.0042 92 ARG A CA 778 C C . ARG A 94 ? 0.1088 0.3386 0.1297 -0.0048 -0.0162 0.0159 92 ARG A C 779 O O . ARG A 94 ? 0.1162 0.3862 0.1450 0.0123 -0.0240 0.0085 92 ARG A O 780 C CB . ARG A 94 ? 0.1969 0.2856 0.1570 0.1003 -0.0333 -0.0058 92 ARG A CB 781 C CG . ARG A 94 ? 0.3119 0.3852 0.1751 0.0994 -0.0246 -0.0035 92 ARG A CG 782 C CD . ARG A 94 ? 0.3937 0.4544 0.2111 0.0783 -0.0120 -0.0041 92 ARG A CD 783 N NE . ARG A 94 ? 0.4515 0.5034 0.2319 0.0402 -0.0349 -0.0406 92 ARG A NE 784 C CZ . ARG A 94 ? 0.5299 0.5314 0.2909 0.0232 -0.0282 -0.0331 92 ARG A CZ 785 N NH1 . ARG A 94 ? 0.5323 0.5237 0.3264 0.0479 0.0072 -0.0389 92 ARG A NH1 786 N NH2 . ARG A 94 ? 0.5734 0.5095 0.2921 -0.0245 -0.0485 -0.0434 92 ARG A NH2 787 N N . MET A 95 ? 0.0768 0.3437 0.1170 0.0029 -0.0211 -0.0015 93 MET A N 788 C CA . MET A 95 ? 0.0830 0.2975 0.1071 -0.0510 -0.0175 -0.0006 93 MET A CA 789 C C . MET A 95 ? 0.0842 0.2456 0.1341 -0.0325 -0.0103 0.0029 93 MET A C 790 O O . MET A 95 ? 0.1219 0.2258 0.1228 -0.0116 -0.0075 0.0142 93 MET A O 791 C CB . MET A 95 ? 0.0962 0.2737 0.1118 0.0073 -0.0354 0.0017 93 MET A CB 792 C CG . MET A 95 ? 0.0900 0.3095 0.1317 0.0216 -0.0296 -0.0038 93 MET A CG 793 S SD . MET A 95 ? 0.1392 0.2578 0.1400 -0.0251 -0.0237 0.0135 93 MET A SD 794 C CE . MET A 95 ? 0.2081 0.1472 0.1537 -0.0277 -0.0356 0.0505 93 MET A CE 795 N N . LEU A 96 ? 0.0694 0.2655 0.1421 0.0045 0.0205 -0.0174 94 LEU A N 796 C CA . LEU A 96 ? 0.0997 0.2545 0.1276 -0.0246 0.0194 -0.0235 94 LEU A CA 797 C C . LEU A 96 ? 0.1103 0.3157 0.1183 -0.0271 -0.0040 -0.0324 94 LEU A C 798 O O . LEU A 96 ? 0.1229 0.4011 0.1440 -0.0039 0.0220 -0.0051 94 LEU A O 799 C CB . LEU A 96 ? 0.1714 0.2724 0.1332 -0.0163 -0.0139 0.0009 94 LEU A CB 800 C CG . LEU A 96 ? 0.2649 0.2996 0.1484 -0.0351 -0.0451 0.0366 94 LEU A CG 801 C CD1 . LEU A 96 ? 0.2776 0.2870 0.1660 -0.0215 -0.0420 0.0350 94 LEU A CD1 802 C CD2 . LEU A 96 ? 0.2790 0.3520 0.1436 -0.0393 -0.0632 0.0155 94 LEU A CD2 803 N N . SER A 97 ? 0.1121 0.2862 0.1232 -0.0232 -0.0137 -0.0232 95 SER A N 804 C CA . SER A 97 ? 0.0842 0.2918 0.1456 -0.0269 -0.0160 -0.0029 95 SER A CA 805 C C . SER A 97 ? 0.0725 0.3075 0.1515 -0.0719 0.0060 -0.0089 95 SER A C 806 O O . SER A 97 ? 0.0785 0.2927 0.1530 -0.0233 -0.0267 -0.0634 95 SER A O 807 C CB . SER A 97 ? 0.1835 0.3139 0.1521 -0.0275 -0.0600 -0.0010 95 SER A CB 808 O OG . SER A 97 ? 0.1957 0.4138 0.2021 0.0397 -0.0528 -0.0024 95 SER A OG 809 N N . ASP A 98 ? 0.1011 0.3129 0.1688 -0.0545 0.0141 0.0010 96 ASP A N 810 C CA . ASP A 98 ? 0.1028 0.3175 0.1657 -0.0502 0.0165 0.0124 96 ASP A CA 811 C C . ASP A 98 ? 0.0688 0.3309 0.1682 -0.0713 -0.0076 0.0037 96 ASP A C 812 O O . ASP A 98 ? 0.1000 0.3470 0.1862 -0.0690 -0.0391 -0.0017 96 ASP A O 813 C CB . ASP A 98 ? 0.1394 0.3327 0.1833 -0.0606 0.0254 0.0136 96 ASP A CB 814 C CG . ASP A 98 ? 0.1829 0.3916 0.2133 0.0152 0.0483 0.0205 96 ASP A CG 815 O OD1 . ASP A 98 ? 0.1658 0.3989 0.1916 0.0412 0.0472 -0.0023 96 ASP A OD1 816 O OD2 . ASP A 98 ? 0.1787 0.4164 0.2285 0.0128 0.0261 0.0450 96 ASP A OD2 817 N N . ASN A 99 ? 0.0743 0.3224 0.1659 -0.0518 -0.0036 0.0212 97 ASN A N 818 C CA . ASN A 99 ? 0.0514 0.3042 0.1714 -0.0520 0.0134 0.0127 97 ASN A CA 819 C C . ASN A 99 ? 0.0940 0.2830 0.1797 -0.0508 0.0352 -0.0212 97 ASN A C 820 O O . ASN A 99 ? 0.1322 0.2529 0.2017 -0.0360 0.0138 -0.0566 97 ASN A O 821 C CB . ASN A 99 ? 0.0784 0.3181 0.1874 -0.0406 0.0213 0.0259 97 ASN A CB 822 C CG . ASN A 99 ? 0.1407 0.3517 0.2288 -0.0735 0.0287 0.0415 97 ASN A CG 823 O OD1 . ASN A 99 ? 0.1959 0.3898 0.2275 -0.0558 0.0352 0.0013 97 ASN A OD1 824 N ND2 . ASN A 99 ? 0.1573 0.4090 0.2717 -0.0864 0.0191 0.0571 97 ASN A ND2 825 N N . GLU A 100 ? 0.0888 0.2873 0.1674 -0.0377 0.0234 -0.0260 98 GLU A N 826 C CA . GLU A 100 ? 0.1184 0.2807 0.1488 -0.0505 0.0209 -0.0148 98 GLU A CA 827 C C . GLU A 100 ? 0.1098 0.2441 0.1187 -0.0264 0.0016 -0.0127 98 GLU A C 828 O O . GLU A 100 ? 0.1761 0.2473 0.1241 -0.0383 0.0295 -0.0381 98 GLU A O 829 C CB . GLU A 100 ? 0.1695 0.3410 0.1696 -0.0430 0.0191 -0.0172 98 GLU A CB 830 C CG . GLU A 100 ? 0.1806 0.3872 0.1770 0.0201 0.0149 -0.0479 98 GLU A CG 831 C CD . GLU A 100 ? 0.3035 0.4435 0.2023 0.0109 0.0164 -0.0606 98 GLU A CD 832 O OE1 . GLU A 100 ? 0.3407 0.4571 0.1985 -0.0430 0.0053 -0.0638 98 GLU A OE1 833 O OE2 . GLU A 100 ? 0.3729 0.4295 0.2288 0.0612 0.0189 -0.1031 98 GLU A OE2 834 N N . TRP A 101 ? 0.0937 0.2424 0.1057 -0.0627 0.0010 -0.0041 99 TRP A N 835 C CA . TRP A 101 ? 0.0628 0.2218 0.1177 -0.0054 -0.0192 -0.0249 99 TRP A CA 836 C C . TRP A 101 ? 0.1163 0.2535 0.1018 -0.0157 -0.0089 -0.0467 99 TRP A C 837 O O . TRP A 101 ? 0.1494 0.2880 0.1084 -0.0355 -0.0065 -0.0147 99 TRP A O 838 C CB . TRP A 101 ? 0.1149 0.1928 0.1278 -0.0107 -0.0163 -0.0831 99 TRP A CB 839 C CG . TRP A 101 ? 0.1101 0.2187 0.1593 0.0147 -0.0272 -0.0750 99 TRP A CG 840 C CD1 . TRP A 101 ? 0.1502 0.2139 0.1558 0.0003 -0.0110 -0.0752 99 TRP A CD1 841 C CD2 . TRP A 101 ? 0.1772 0.2725 0.1959 -0.0241 -0.0075 -0.1074 99 TRP A CD2 842 N NE1 . TRP A 101 ? 0.1957 0.2436 0.1726 0.0142 0.0071 -0.0678 99 TRP A NE1 843 C CE2 . TRP A 101 ? 0.1871 0.2940 0.2154 0.0179 -0.0026 -0.0886 99 TRP A CE2 844 C CE3 . TRP A 101 ? 0.2351 0.3280 0.2421 -0.0229 0.0179 -0.1326 99 TRP A CE3 845 C CZ2 . TRP A 101 ? 0.2117 0.3299 0.2646 -0.0067 0.0400 -0.0684 99 TRP A CZ2 846 C CZ3 . TRP A 101 ? 0.2847 0.3193 0.2867 -0.0215 0.0578 -0.0799 99 TRP A CZ3 847 C CH2 . TRP A 101 ? 0.2785 0.3528 0.2904 -0.0167 0.0695 -0.0648 99 TRP A CH2 848 N N . GLY A 102 ? 0.0919 0.2406 0.0875 -0.0076 -0.0146 -0.0252 100 GLY A N 849 C CA . GLY A 102 ? 0.0863 0.2239 0.0981 0.0052 0.0234 -0.0148 100 GLY A CA 850 C C . GLY A 102 ? 0.1002 0.2071 0.1028 -0.0130 0.0139 0.0027 100 GLY A C 851 O O . GLY A 102 ? 0.0924 0.1977 0.1216 -0.0142 -0.0049 -0.0004 100 GLY A O 852 N N . SER A 103 ? 0.0638 0.2033 0.0843 -0.0239 0.0200 -0.0173 101 SER A N 853 C CA . SER A 103 ? 0.0932 0.2119 0.0814 -0.0299 0.0336 -0.0138 101 SER A CA 854 C C . SER A 103 ? 0.0987 0.1987 0.0645 -0.0449 0.0153 -0.0305 101 SER A C 855 O O . SER A 103 ? 0.1388 0.1841 0.0685 0.0168 0.0130 -0.0181 101 SER A O 856 C CB . SER A 103 ? 0.1389 0.1820 0.0906 -0.0298 -0.0057 0.0054 101 SER A CB 857 O OG . SER A 103 ? 0.1077 0.1911 0.0916 -0.0013 -0.0111 0.0271 101 SER A OG 858 N N . THR A 104 ? 0.1024 0.2438 0.0803 -0.0204 0.0028 -0.0010 102 THR A N 859 C CA . THR A 104 ? 0.0865 0.2087 0.0861 0.0315 0.0067 -0.0082 102 THR A CA 860 C C . THR A 104 ? 0.0736 0.2057 0.0881 0.0323 0.0026 -0.0040 102 THR A C 861 O O . THR A 104 ? 0.1359 0.1410 0.0829 -0.0095 0.0073 -0.0075 102 THR A O 862 C CB . THR A 104 ? 0.1058 0.2017 0.0739 0.0367 -0.0091 -0.0238 102 THR A CB 863 O OG1 . THR A 104 ? 0.1447 0.1583 0.0942 0.0108 -0.0127 -0.0058 102 THR A OG1 864 C CG2 . THR A 104 ? 0.1603 0.2053 0.1144 0.0259 0.0283 0.0002 102 THR A CG2 865 N N . LEU A 105 ? 0.0781 0.1876 0.0929 0.0512 0.0157 0.0052 103 LEU A N 866 C CA . LEU A 105 ? 0.0744 0.1791 0.0653 0.0232 0.0048 0.0492 103 LEU A CA 867 C C . LEU A 105 ? 0.1304 0.1723 0.0748 0.0085 0.0229 0.0100 103 LEU A C 868 O O . LEU A 105 ? 0.1039 0.1584 0.0608 -0.0048 -0.0013 -0.0223 103 LEU A O 869 C CB . LEU A 105 ? 0.0578 0.2090 0.0748 -0.0244 -0.0362 0.0295 103 LEU A CB 870 C CG . LEU A 105 ? 0.1079 0.2302 0.0839 -0.0414 -0.0150 0.0195 103 LEU A CG 871 C CD1 . LEU A 105 ? 0.0759 0.2508 0.1077 -0.0366 -0.0024 0.0111 103 LEU A CD1 872 C CD2 . LEU A 105 ? 0.1174 0.2850 0.0920 -0.0050 0.0080 0.0515 103 LEU A CD2 873 N N . GLU A 106 ? 0.1280 0.2116 0.0786 0.0533 0.0099 -0.0179 104 GLU A N 874 C CA . GLU A 106 ? 0.0815 0.1935 0.0769 0.0117 0.0193 -0.0303 104 GLU A CA 875 C C . GLU A 106 ? 0.0749 0.1831 0.0699 0.0354 0.0040 -0.0384 104 GLU A C 876 O O . GLU A 106 ? 0.0792 0.2019 0.0919 -0.0201 0.0123 -0.0532 104 GLU A O 877 C CB . GLU A 106 ? 0.0543 0.2255 0.0867 0.0105 0.0051 -0.0188 104 GLU A CB 878 C CG . GLU A 106 ? 0.1326 0.2266 0.0795 0.0067 -0.0099 0.0049 104 GLU A CG 879 C CD . GLU A 106 ? 0.1142 0.2577 0.0914 0.0316 -0.0009 0.0430 104 GLU A CD 880 O OE1 . GLU A 106 ? 0.0978 0.2672 0.0915 -0.0080 0.0176 0.0206 104 GLU A OE1 881 O OE2 . GLU A 106 ? 0.1495 0.2432 0.0977 0.0305 -0.0177 0.0314 104 GLU A OE2 882 N N . ALA A 107 ? 0.0761 0.2013 0.0539 0.0184 -0.0063 -0.0058 105 ALA A N 883 C CA . ALA A 107 ? 0.0981 0.1668 0.0935 0.0172 -0.0383 0.0334 105 ALA A CA 884 C C . ALA A 107 ? 0.1385 0.1565 0.0995 0.0008 0.0019 0.0075 105 ALA A C 885 O O . ALA A 107 ? 0.1012 0.1570 0.1104 0.0257 0.0274 -0.0062 105 ALA A O 886 C CB . ALA A 107 ? 0.1125 0.1862 0.1022 0.0433 -0.0343 0.0359 105 ALA A CB 887 N N . SER A 108 ? 0.1179 0.1533 0.0857 -0.0351 0.0034 -0.0012 106 SER A N 888 C CA . SER A 108 ? 0.1512 0.1691 0.0870 -0.0204 -0.0007 -0.0143 106 SER A CA 889 C C . SER A 108 ? 0.1795 0.1543 0.0955 -0.0059 -0.0307 -0.0029 106 SER A C 890 O O . SER A 108 ? 0.1544 0.1708 0.1020 -0.0188 -0.0167 0.0004 106 SER A O 891 C CB . SER A 108 ? 0.1260 0.1977 0.0880 -0.0667 0.0082 0.0179 106 SER A CB 892 O OG . SER A 108 ? 0.1112 0.2005 0.0987 -0.0084 -0.0020 0.0314 106 SER A OG 893 N N . MET A 109 ? 0.1574 0.2061 0.0831 0.0242 -0.0126 -0.0032 107 MET A N 894 C CA . MET A 109 ? 0.1265 0.1945 0.0707 0.0117 -0.0236 0.0036 107 MET A CA 895 C C . MET A 109 ? 0.1839 0.1392 0.0841 0.0144 -0.0129 0.0029 107 MET A C 896 O O . MET A 109 ? 0.1758 0.1731 0.0948 0.0148 -0.0240 -0.0007 107 MET A O 897 C CB . MET A 109 ? 0.1725 0.2329 0.0593 0.0179 -0.0286 -0.0205 107 MET A CB 898 C CG . MET A 109 ? 0.1607 0.2181 0.0766 -0.0034 -0.0429 -0.0120 107 MET A CG 899 S SD . MET A 109 ? 0.1659 0.2063 0.1059 0.0141 -0.0164 0.0166 107 MET A SD 900 C CE . MET A 109 ? 0.1700 0.1858 0.1328 -0.0007 -0.0004 0.0331 107 MET A CE 901 N N . LEU A 110 ? 0.1730 0.1919 0.0915 0.0503 -0.0117 0.0305 108 LEU A N 902 C CA . LEU A 110 ? 0.1166 0.1905 0.1052 -0.0091 -0.0027 -0.0061 108 LEU A CA 903 C C . LEU A 110 ? 0.1370 0.1962 0.1024 -0.0049 -0.0002 0.0074 108 LEU A C 904 O O . LEU A 110 ? 0.1598 0.2753 0.0776 -0.0115 0.0171 -0.0328 108 LEU A O 905 C CB . LEU A 110 ? 0.1187 0.1720 0.1325 0.0033 0.0111 0.0002 108 LEU A CB 906 C CG . LEU A 110 ? 0.0798 0.1514 0.1471 0.0379 0.0113 -0.0385 108 LEU A CG 907 C CD1 . LEU A 110 ? 0.0904 0.1967 0.1472 0.0143 -0.0119 -0.0270 108 LEU A CD1 908 C CD2 . LEU A 110 ? 0.1090 0.2275 0.1390 0.0670 -0.0008 -0.0344 108 LEU A CD2 909 N N . ALA A 111 ? 0.1246 0.2246 0.1181 -0.0206 -0.0043 0.0191 109 ALA A N 910 C CA . ALA A 111 ? 0.1391 0.2248 0.1387 0.0163 -0.0143 -0.0109 109 ALA A CA 911 C C . ALA A 111 ? 0.1991 0.1952 0.1309 -0.0218 -0.0238 -0.0289 109 ALA A C 912 O O . ALA A 111 ? 0.2115 0.2095 0.1316 0.0073 -0.0304 -0.0359 109 ALA A O 913 C CB . ALA A 111 ? 0.1352 0.2101 0.1447 0.0735 -0.0092 -0.0181 109 ALA A CB 914 N N . LYS A 112 ? 0.2421 0.1309 0.1066 -0.0546 0.0314 -0.0354 110 LYS A N 915 C CA . LYS A 112 ? 0.2449 0.1540 0.1298 -0.0325 0.0130 -0.0195 110 LYS A CA 916 C C . LYS A 112 ? 0.2382 0.1592 0.1495 -0.0396 -0.0081 -0.0677 110 LYS A C 917 O O . LYS A 112 ? 0.2593 0.1709 0.1923 0.0042 -0.0215 -0.0969 110 LYS A O 918 C CB . LYS A 112 ? 0.3056 0.2114 0.1391 -0.0208 0.0457 -0.0001 110 LYS A CB 919 C CG . LYS A 112 ? 0.3264 0.2715 0.1474 0.0465 0.0638 0.0440 110 LYS A CG 920 C CD . LYS A 112 ? 0.3458 0.2749 0.1513 -0.0037 0.0782 0.0452 110 LYS A CD 921 C CE . LYS A 112 ? 0.3939 0.2612 0.1798 -0.0251 0.0253 0.0390 110 LYS A CE 922 N NZ . LYS A 112 ? 0.4250 0.2164 0.1771 0.0192 -0.0179 0.0904 110 LYS A NZ 923 N N . GLU A 113 ? 0.1655 0.2182 0.1579 -0.0012 -0.0093 -0.0446 111 GLU A N 924 C CA . GLU A 113 ? 0.1903 0.2122 0.1640 0.0437 -0.0070 -0.0548 111 GLU A CA 925 C C . GLU A 113 ? 0.2482 0.1965 0.1584 0.0752 -0.0201 -0.0642 111 GLU A C 926 O O . GLU A 113 ? 0.2880 0.2448 0.1861 0.0658 -0.0176 -0.0650 111 GLU A O 927 C CB . GLU A 113 ? 0.1074 0.2142 0.1939 0.0556 -0.0087 -0.0323 111 GLU A CB 928 C CG . GLU A 113 ? 0.1815 0.2056 0.2183 0.0552 0.0171 -0.0574 111 GLU A CG 929 C CD . GLU A 113 ? 0.2633 0.3544 0.2575 0.1145 0.0405 -0.0656 111 GLU A CD 930 O OE1 . GLU A 113 ? 0.3222 0.3889 0.2409 0.1098 0.0119 -0.0400 111 GLU A OE1 931 O OE2 . GLU A 113 ? 0.3424 0.3779 0.3085 0.1234 0.0385 -0.0837 111 GLU A OE2 932 N N . MET A 114 ? 0.2017 0.1833 0.1287 0.0298 -0.0496 -0.0068 112 MET A N 933 C CA . MET A 114 ? 0.1954 0.1959 0.1311 0.0151 -0.0464 -0.0350 112 MET A CA 934 C C . MET A 114 ? 0.1926 0.2561 0.1346 0.0299 -0.0494 -0.0524 112 MET A C 935 O O . MET A 114 ? 0.1778 0.3620 0.1203 0.0031 -0.0673 -0.0734 112 MET A O 936 C CB . MET A 114 ? 0.2029 0.1781 0.1394 0.0373 -0.0625 -0.0249 112 MET A CB 937 C CG . MET A 114 ? 0.2088 0.1978 0.1375 0.0093 -0.0535 -0.0239 112 MET A CG 938 S SD . MET A 114 ? 0.2684 0.2893 0.1381 -0.0041 -0.0037 -0.0500 112 MET A SD 939 C CE . MET A 114 ? 0.2223 0.2840 0.1104 0.0158 0.0291 -0.0903 112 MET A CE 940 N N . GLY A 115 ? 0.1695 0.2222 0.1385 0.0505 -0.0458 -0.0436 113 GLY A N 941 C CA . GLY A 115 ? 0.1672 0.1619 0.1284 0.0690 -0.0476 -0.0182 113 GLY A CA 942 C C . GLY A 115 ? 0.1708 0.2124 0.1133 0.0409 0.0016 0.0094 113 GLY A C 943 O O . GLY A 115 ? 0.2022 0.2382 0.1235 0.0092 0.0147 0.0516 113 GLY A O 944 N N . ILE A 116 ? 0.2303 0.2162 0.1133 0.0646 0.0232 0.0079 114 ILE A N 945 C CA . ILE A 116 ? 0.2249 0.1956 0.1147 0.0506 0.0118 0.0101 114 ILE A CA 946 C C . ILE A 116 ? 0.2079 0.1554 0.1078 0.0434 -0.0002 0.0089 114 ILE A C 947 O O . ILE A 116 ? 0.2570 0.1654 0.1141 0.0105 0.0211 0.0205 114 ILE A O 948 C CB . ILE A 116 ? 0.2490 0.2004 0.1297 -0.0027 0.0641 0.0077 114 ILE A CB 949 C CG1 . ILE A 116 ? 0.2386 0.1954 0.1637 -0.0710 0.0680 0.0213 114 ILE A CG1 950 C CG2 . ILE A 116 ? 0.2399 0.2706 0.1341 0.0196 0.0735 -0.0305 114 ILE A CG2 951 C CD1 . ILE A 116 ? 0.2670 0.1899 0.1931 -0.0207 0.0836 0.0273 114 ILE A CD1 952 N N . THR A 117 ? 0.1292 0.1340 0.1091 0.0055 -0.0265 -0.0190 115 THR A N 953 C CA . THR A 117 ? 0.1577 0.1718 0.1325 -0.0188 -0.0211 -0.0266 115 THR A CA 954 C C . THR A 117 ? 0.1331 0.1365 0.1137 -0.0255 -0.0128 -0.0198 115 THR A C 955 O O . THR A 117 ? 0.1844 0.1843 0.1165 0.0217 0.0141 -0.0300 115 THR A O 956 C CB . THR A 117 ? 0.1238 0.1759 0.1664 0.0022 -0.0249 -0.0182 115 THR A CB 957 O OG1 . THR A 117 ? 0.1978 0.1935 0.1846 -0.0418 -0.0037 -0.0270 115 THR A OG1 958 C CG2 . THR A 117 ? 0.1197 0.1817 0.1547 0.0385 -0.0502 -0.0098 115 THR A CG2 959 N N . ILE A 118 ? 0.0870 0.0948 0.1294 -0.0068 -0.0009 -0.0234 116 ILE A N 960 C CA . ILE A 118 ? 0.0993 0.1562 0.1205 0.0111 -0.0158 0.0409 116 ILE A CA 961 C C . ILE A 118 ? 0.1398 0.1715 0.1172 0.0237 -0.0261 0.0155 116 ILE A C 962 O O . ILE A 118 ? 0.1355 0.1827 0.1282 0.0099 -0.0085 -0.0029 116 ILE A O 963 C CB . ILE A 118 ? 0.0944 0.1575 0.1238 0.0470 -0.0249 -0.0079 116 ILE A CB 964 C CG1 . ILE A 118 ? 0.0429 0.2312 0.1014 0.0995 0.0000 0.0037 116 ILE A CG1 965 C CG2 . ILE A 118 ? 0.0877 0.1243 0.1226 -0.0040 -0.0256 -0.0060 116 ILE A CG2 966 C CD1 . ILE A 118 ? 0.0681 0.2119 0.0904 0.0245 -0.0152 -0.0090 116 ILE A CD1 967 N N . ILE A 119 ? 0.0961 0.1552 0.1176 0.0215 -0.0245 0.0031 117 ILE A N 968 C CA . ILE A 119 ? 0.0996 0.1750 0.1195 0.0028 -0.0141 -0.0311 117 ILE A CA 969 C C . ILE A 119 ? 0.1414 0.1532 0.1174 0.0104 0.0010 -0.0098 117 ILE A C 970 O O . ILE A 119 ? 0.1103 0.1802 0.1105 0.0289 0.0102 -0.0282 117 ILE A O 971 C CB . ILE A 119 ? 0.0469 0.1024 0.1248 0.0003 -0.0135 -0.0019 117 ILE A CB 972 C CG1 . ILE A 119 ? 0.0420 0.1587 0.1237 -0.0150 -0.0266 0.0255 117 ILE A CG1 973 C CG2 . ILE A 119 ? 0.0908 0.1931 0.1382 0.0330 -0.0094 0.0248 117 ILE A CG2 974 C CD1 . ILE A 119 ? 0.0614 0.2307 0.1179 -0.0286 -0.0280 0.0149 117 ILE A CD1 975 N N . ILE A 120 ? 0.1188 0.1477 0.1115 -0.0016 -0.0182 0.0164 118 ILE A N 976 C CA . ILE A 120 ? 0.1148 0.1825 0.1177 -0.0006 -0.0200 0.0147 118 ILE A CA 977 C C . ILE A 120 ? 0.1004 0.1745 0.1136 0.0040 -0.0001 0.0261 118 ILE A C 978 O O . ILE A 120 ? 0.1020 0.1707 0.1205 0.0016 0.0247 0.0139 118 ILE A O 979 C CB . ILE A 120 ? 0.1003 0.1681 0.1324 -0.0060 -0.0020 0.0066 118 ILE A CB 980 C CG1 . ILE A 120 ? 0.1696 0.2043 0.1259 0.0615 -0.0219 0.0204 118 ILE A CG1 981 C CG2 . ILE A 120 ? 0.1223 0.1427 0.1617 -0.0417 0.0203 -0.0150 118 ILE A CG2 982 C CD1 . ILE A 120 ? 0.1518 0.2228 0.1351 0.0818 -0.0362 0.0200 118 ILE A CD1 983 N N . TRP A 121 ? 0.0861 0.1692 0.1190 -0.0164 -0.0193 0.0391 119 TRP A N 984 C CA . TRP A 121 ? 0.1480 0.1437 0.1090 -0.0506 -0.0100 0.0314 119 TRP A CA 985 C C . TRP A 121 ? 0.1605 0.1781 0.1382 -0.0510 -0.0024 0.0392 119 TRP A C 986 O O . TRP A 121 ? 0.1756 0.1995 0.1931 -0.0345 0.0054 -0.0245 119 TRP A O 987 C CB . TRP A 121 ? 0.1500 0.1496 0.1051 -0.0314 0.0144 0.0587 119 TRP A CB 988 C CG . TRP A 121 ? 0.0958 0.1902 0.1096 -0.0496 0.0009 0.0381 119 TRP A CG 989 C CD1 . TRP A 121 ? 0.1136 0.2235 0.1077 -0.0362 -0.0004 0.0341 119 TRP A CD1 990 C CD2 . TRP A 121 ? 0.0836 0.1666 0.1374 -0.0277 -0.0100 0.0307 119 TRP A CD2 991 N NE1 . TRP A 121 ? 0.0964 0.2077 0.1107 -0.0222 0.0121 0.0136 119 TRP A NE1 992 C CE2 . TRP A 121 ? 0.0930 0.2477 0.1213 0.0277 -0.0142 0.0289 119 TRP A CE2 993 C CE3 . TRP A 121 ? 0.0623 0.2324 0.1524 0.0015 -0.0009 0.0617 119 TRP A CE3 994 C CZ2 . TRP A 121 ? 0.0856 0.2558 0.1310 0.0379 0.0010 0.0113 119 TRP A CZ2 995 C CZ3 . TRP A 121 ? 0.0510 0.2500 0.1586 -0.0048 -0.0327 0.0241 119 TRP A CZ3 996 C CH2 . TRP A 121 ? 0.0889 0.2549 0.1471 0.0122 0.0143 0.0119 119 TRP A CH2 997 N N . THR A 122 ? 0.2230 0.1768 0.1190 -0.0470 -0.0345 0.0294 120 THR A N 998 C CA . THR A 122 ? 0.3133 0.2013 0.1344 -0.0397 -0.0038 0.0113 120 THR A CA 999 C C . THR A 122 ? 0.3462 0.2397 0.1723 -0.0533 0.0030 -0.0105 120 THR A C 1000 O O . THR A 122 ? 0.3594 0.2442 0.1925 -0.0132 0.0709 -0.0150 120 THR A O 1001 C CB . THR A 122 ? 0.4128 0.3300 0.1301 -0.0763 0.0481 -0.0647 120 THR A CB 1002 O OG1 . THR A 122 ? 0.4863 0.4678 0.1674 0.0052 0.0865 -0.0308 120 THR A OG1 1003 C CG2 . THR A 122 ? 0.4330 0.3193 0.1010 -0.0778 0.1108 -0.0739 120 THR A CG2 1004 N N . VAL A 123 ? 0.3712 0.2454 0.1731 -0.0196 -0.0554 0.0133 121 VAL A N 1005 C CA . VAL A 123 ? 0.3693 0.2627 0.1799 -0.0013 -0.0732 0.0158 121 VAL A CA 1006 C C . VAL A 123 ? 0.3986 0.3581 0.1909 -0.0782 -0.1614 -0.0134 121 VAL A C 1007 O O . VAL A 123 ? 0.4712 0.4313 0.1989 -0.1050 -0.1180 -0.0364 121 VAL A O 1008 C CB . VAL A 123 ? 0.2180 0.3109 0.1937 -0.0141 -0.0586 0.0299 121 VAL A CB 1009 C CG1 . VAL A 123 ? 0.2064 0.2650 0.1900 -0.0306 -0.0821 0.0236 121 VAL A CG1 1010 C CG2 . VAL A 123 ? 0.1809 0.3473 0.2151 -0.0386 -0.0735 0.0547 121 VAL A CG2 1011 N N . SER A 126 ? 0.6079 0.4553 0.3524 -0.1215 0.0289 -0.1561 124 SER A N 1012 C CA . SER A 126 ? 0.5689 0.4988 0.3500 -0.1160 0.0434 -0.0905 124 SER A CA 1013 C C . SER A 126 ? 0.5264 0.4684 0.3307 -0.1057 0.0141 -0.0379 124 SER A C 1014 O O . SER A 126 ? 0.5233 0.4428 0.3338 -0.1228 -0.0324 -0.0211 124 SER A O 1015 C CB . SER A 126 ? 0.6144 0.5818 0.3649 -0.0957 0.0846 -0.0579 124 SER A CB 1016 O OG . SER A 126 ? 0.6049 0.5756 0.3556 -0.1599 0.1263 -0.0479 124 SER A OG 1017 N N . ASP A 127 ? 0.4459 0.4007 0.2996 -0.1362 0.0370 -0.0077 125 ASP A N 1018 C CA . ASP A 127 ? 0.4057 0.3881 0.2710 -0.0461 0.0410 0.0088 125 ASP A CA 1019 C C . ASP A 127 ? 0.3523 0.3292 0.2299 -0.0196 0.0469 0.0019 125 ASP A C 1020 O O . ASP A 127 ? 0.3335 0.3346 0.2000 -0.0390 0.0414 -0.0075 125 ASP A O 1021 C CB . ASP A 127 ? 0.4102 0.4107 0.2914 -0.0314 0.0394 0.0403 125 ASP A CB 1022 C CG . ASP A 127 ? 0.4332 0.4009 0.3144 -0.0617 0.0202 0.0370 125 ASP A CG 1023 O OD1 . ASP A 127 ? 0.3960 0.3716 0.3304 -0.0755 -0.0118 0.0352 125 ASP A OD1 1024 O OD2 . ASP A 127 ? 0.4881 0.3866 0.3260 -0.0924 0.0430 0.0351 125 ASP A OD2 1025 N N . GLU A 128 ? 0.3526 0.2765 0.2064 -0.0003 0.0687 -0.0028 126 GLU A N 1026 C CA . GLU A 128 ? 0.3322 0.2365 0.2068 0.0350 0.0451 0.0024 126 GLU A CA 1027 C C . GLU A 128 ? 0.2967 0.1503 0.1772 0.0383 0.0042 -0.0139 126 GLU A C 1028 O O . GLU A 128 ? 0.3474 0.2082 0.1580 0.0054 0.0094 -0.0213 126 GLU A O 1029 C CB . GLU A 128 ? 0.3948 0.3105 0.2436 0.0399 0.0535 -0.0341 126 GLU A CB 1030 C CG . GLU A 128 ? 0.4857 0.4390 0.2805 0.1267 0.0346 -0.0323 126 GLU A CG 1031 C CD . GLU A 128 ? 0.5389 0.5640 0.2962 0.2051 0.0113 0.0149 126 GLU A CD 1032 O OE1 . GLU A 128 ? 0.4823 0.5649 0.2967 0.2721 0.0133 0.0587 126 GLU A OE1 1033 O OE2 . GLU A 128 ? 0.5804 0.5888 0.2913 0.2380 0.0112 0.0239 126 GLU A OE2 1034 N N . VAL A 129 ? 0.2362 0.1594 0.1655 0.0036 0.0293 0.0101 127 VAL A N 1035 C CA . VAL A 129 ? 0.2132 0.2009 0.1454 0.0171 0.0465 0.0185 127 VAL A CA 1036 C C . VAL A 129 ? 0.2285 0.2404 0.1469 0.0498 0.0475 0.0358 127 VAL A C 1037 O O . VAL A 129 ? 0.2097 0.2848 0.1556 0.0283 0.0589 -0.0015 127 VAL A O 1038 C CB . VAL A 129 ? 0.2420 0.2065 0.1235 0.0415 0.0271 0.0175 127 VAL A CB 1039 C CG1 . VAL A 129 ? 0.2445 0.2198 0.1312 0.0728 0.0289 0.0265 127 VAL A CG1 1040 C CG2 . VAL A 129 ? 0.2666 0.2641 0.0997 0.0282 0.0268 -0.0136 127 VAL A CG2 1041 N N . GLU A 130 ? 0.2276 0.2494 0.1542 0.0267 0.0258 0.0418 128 GLU A N 1042 C CA . GLU A 130 ? 0.2500 0.2971 0.1862 0.0234 0.0640 0.0169 128 GLU A CA 1043 C C . GLU A 130 ? 0.2134 0.2739 0.1870 0.0275 0.0640 0.0341 128 GLU A C 1044 O O . GLU A 130 ? 0.2026 0.2850 0.2094 0.0284 0.0606 0.0507 128 GLU A O 1045 C CB . GLU A 130 ? 0.3162 0.3430 0.1904 0.0184 0.0506 -0.0049 128 GLU A CB 1046 C CG . GLU A 130 ? 0.4501 0.4067 0.2450 0.0086 0.0421 -0.0082 128 GLU A CG 1047 C CD . GLU A 130 ? 0.5795 0.4280 0.2822 -0.0286 0.0490 0.0036 128 GLU A CD 1048 O OE1 . GLU A 130 ? 0.6460 0.3980 0.3197 -0.0506 0.0533 0.0067 128 GLU A OE1 1049 O OE2 . GLU A 130 ? 0.5756 0.4320 0.2654 -0.0117 0.0354 0.0355 128 GLU A OE2 1050 N N . ALA A 131 ? 0.2031 0.2454 0.1414 0.0769 0.0135 0.0194 129 ALA A N 1051 C CA . ALA A 131 ? 0.1792 0.2592 0.1159 0.0246 0.0148 0.0336 129 ALA A CA 1052 C C . ALA A 131 ? 0.1447 0.2252 0.1319 0.0123 0.0170 0.0184 129 ALA A C 1053 O O . ALA A 131 ? 0.2014 0.2322 0.1489 -0.0235 0.0337 0.0131 129 ALA A O 1054 C CB . ALA A 131 ? 0.2139 0.3056 0.1249 0.0363 0.0220 0.0356 129 ALA A CB 1055 N N . GLY A 132 ? 0.1343 0.2324 0.1274 -0.0187 0.0435 0.0138 130 GLY A N 1056 C CA . GLY A 132 ? 0.1184 0.2005 0.1308 -0.0248 0.0082 0.0418 130 GLY A CA 1057 C C . GLY A 132 ? 0.1191 0.1680 0.1275 -0.0257 0.0021 0.0424 130 GLY A C 1058 O O . GLY A 132 ? 0.1268 0.1971 0.1443 0.0279 0.0049 0.0785 130 GLY A O 1059 N N . ILE A 133 ? 0.1181 0.1602 0.1115 -0.0032 0.0210 0.0151 131 ILE A N 1060 C CA . ILE A 133 ? 0.1402 0.1284 0.1085 -0.0009 0.0001 0.0188 131 ILE A CA 1061 C C . ILE A 133 ? 0.1483 0.1330 0.1201 -0.0108 0.0292 -0.0192 131 ILE A C 1062 O O . ILE A 133 ? 0.1530 0.1422 0.1241 -0.0116 0.0402 -0.0299 131 ILE A O 1063 C CB . ILE A 133 ? 0.1811 0.1581 0.1446 0.0638 -0.0204 0.0199 131 ILE A CB 1064 C CG1 . ILE A 133 ? 0.1967 0.2922 0.1861 0.0887 -0.0007 0.0026 131 ILE A CG1 1065 C CG2 . ILE A 133 ? 0.2178 0.1911 0.1597 0.0806 -0.0262 0.0516 131 ILE A CG2 1066 C CD1 . ILE A 133 ? 0.2696 0.3697 0.2059 0.0556 0.0152 0.0003 131 ILE A CD1 1067 N N . LYS A 134 ? 0.1184 0.1768 0.0973 0.0015 -0.0159 0.0231 132 LYS A N 1068 C CA . LYS A 134 ? 0.1542 0.1600 0.0894 -0.0150 -0.0308 0.0167 132 LYS A CA 1069 C C . LYS A 134 ? 0.1356 0.1389 0.0998 -0.0130 -0.0152 0.0287 132 LYS A C 1070 O O . LYS A 134 ? 0.1802 0.1737 0.1298 -0.0080 -0.0096 0.0534 132 LYS A O 1071 C CB . LYS A 134 ? 0.1370 0.2005 0.0817 -0.0445 -0.0447 0.0034 132 LYS A CB 1072 C CG . LYS A 134 ? 0.1378 0.1620 0.0917 -0.0345 -0.0449 -0.0212 132 LYS A CG 1073 C CD . LYS A 134 ? 0.1106 0.1913 0.1247 -0.0447 -0.0260 -0.0270 132 LYS A CD 1074 C CE . LYS A 134 ? 0.1468 0.1737 0.1493 -0.0382 0.0098 -0.0035 132 LYS A CE 1075 N NZ . LYS A 134 ? 0.1798 0.2495 0.1714 -0.0446 -0.0291 0.0302 132 LYS A NZ 1076 N N . PHE A 135 ? 0.1258 0.1325 0.0913 -0.0082 0.0058 0.0016 133 PHE A N 1077 C CA . PHE A 135 ? 0.0984 0.1413 0.0964 -0.0197 0.0047 0.0005 133 PHE A CA 1078 C C . PHE A 135 ? 0.1249 0.1822 0.1101 -0.0301 -0.0256 -0.0106 133 PHE A C 1079 O O . PHE A 135 ? 0.1629 0.1586 0.1330 0.0039 0.0162 0.0113 133 PHE A O 1080 C CB . PHE A 135 ? 0.1081 0.2072 0.0933 -0.0500 0.0192 0.0003 133 PHE A CB 1081 C CG . PHE A 135 ? 0.1281 0.1739 0.1005 -0.0315 -0.0001 -0.0212 133 PHE A CG 1082 C CD1 . PHE A 135 ? 0.1465 0.2012 0.0781 0.0294 0.0073 -0.0282 133 PHE A CD1 1083 C CD2 . PHE A 135 ? 0.1116 0.2377 0.1201 -0.0743 0.0143 -0.0267 133 PHE A CD2 1084 C CE1 . PHE A 135 ? 0.1312 0.2339 0.1004 0.0230 0.0140 -0.0190 133 PHE A CE1 1085 C CE2 . PHE A 135 ? 0.1063 0.2510 0.1060 -0.0418 -0.0109 0.0017 133 PHE A CE2 1086 C CZ . PHE A 135 ? 0.1188 0.2748 0.1130 -0.0204 0.0044 -0.0130 133 PHE A CZ 1087 N N . GLY A 136 ? 0.1737 0.1603 0.1150 -0.0565 -0.0156 -0.0257 134 GLY A N 1088 C CA . GLY A 136 ? 0.1420 0.1790 0.0941 -0.0747 -0.0378 -0.0350 134 GLY A CA 1089 C C . GLY A 136 ? 0.1718 0.1582 0.1236 -0.0748 -0.0132 -0.0084 134 GLY A C 1090 O O . GLY A 136 ? 0.2486 0.1715 0.1233 -0.0144 -0.0088 -0.0281 134 GLY A O 1091 N N . ASP A 137 ? 0.2057 0.1852 0.1620 -0.0353 -0.0236 -0.0090 135 ASP A N 1092 C CA . ASP A 137 ? 0.2181 0.1817 0.1928 -0.0551 -0.0538 0.0406 135 ASP A CA 1093 C C . ASP A 137 ? 0.1851 0.2417 0.1794 -0.0983 -0.0835 0.0285 135 ASP A C 1094 O O . ASP A 137 ? 0.1849 0.3279 0.2150 -0.1054 -0.0788 0.0013 135 ASP A O 1095 C CB . ASP A 137 ? 0.2960 0.2016 0.2287 -0.0742 -0.0068 0.0399 135 ASP A CB 1096 C CG . ASP A 137 ? 0.4108 0.2557 0.2737 -0.0857 0.0295 0.0175 135 ASP A CG 1097 O OD1 . ASP A 137 ? 0.4097 0.2959 0.2840 -0.0918 0.0676 0.0036 135 ASP A OD1 1098 O OD2 . ASP A 137 ? 0.5026 0.2756 0.2920 -0.0665 0.0318 0.0294 135 ASP A OD2 1099 N N . GLY A 138 ? 0.2123 0.2353 0.1523 -0.0534 -0.0752 0.0476 136 GLY A N 1100 C CA . GLY A 138 ? 0.2135 0.1861 0.1417 -0.0028 -0.0660 0.0578 136 GLY A CA 1101 C C . GLY A 138 ? 0.1621 0.2474 0.1446 -0.0500 -0.0534 0.0201 136 GLY A C 1102 O O . GLY A 138 ? 0.2320 0.2480 0.1317 -0.0454 -0.0474 -0.0043 136 GLY A O 1103 N N . ASP A 139 ? 0.1518 0.2667 0.1611 -0.0624 -0.0081 0.0171 137 ASP A N 1104 C CA . ASP A 139 ? 0.1370 0.2542 0.1585 -0.0678 -0.0241 0.0322 137 ASP A CA 1105 C C . ASP A 139 ? 0.1642 0.2479 0.1601 -0.0520 -0.0179 0.0404 137 ASP A C 1106 O O . ASP A 139 ? 0.1633 0.2370 0.1528 -0.0798 -0.0289 0.0098 137 ASP A O 1107 C CB . ASP A 139 ? 0.1307 0.3616 0.1758 -0.0476 -0.0413 0.0117 137 ASP A CB 1108 C CG . ASP A 139 ? 0.1534 0.4075 0.2070 -0.0936 -0.0679 -0.0284 137 ASP A CG 1109 O OD1 . ASP A 139 ? 0.1710 0.3166 0.2082 -0.0849 -0.0590 -0.0027 137 ASP A OD1 1110 O OD2 . ASP A 139 ? 0.2504 0.5370 0.2353 -0.1394 -0.0431 -0.0655 137 ASP A OD2 1111 N N . VAL A 140 ? 0.1698 0.1952 0.1403 -0.0183 -0.0329 0.0393 138 VAL A N 1112 C CA . VAL A 140 ? 0.1563 0.1852 0.1305 -0.0434 -0.0052 0.0550 138 VAL A CA 1113 C C . VAL A 140 ? 0.1293 0.2261 0.1385 -0.0169 -0.0037 0.0439 138 VAL A C 1114 O O . VAL A 140 ? 0.1243 0.2332 0.1540 0.0075 -0.0077 0.0282 138 VAL A O 1115 C CB . VAL A 140 ? 0.1506 0.1960 0.1251 -0.0274 -0.0442 0.0371 138 VAL A CB 1116 C CG1 . VAL A 140 ? 0.1624 0.2335 0.1351 -0.0248 -0.0385 0.0146 138 VAL A CG1 1117 C CG2 . VAL A 140 ? 0.1322 0.2213 0.1535 -0.0238 -0.0307 0.0476 138 VAL A CG2 1118 N N . PHE A 141 ? 0.1089 0.2310 0.1318 -0.0356 -0.0117 0.0311 139 PHE A N 1119 C CA . PHE A 141 ? 0.1443 0.2927 0.1441 -0.0723 -0.0402 0.0188 139 PHE A CA 1120 C C . PHE A 141 ? 0.2060 0.2972 0.1561 -0.0698 -0.0252 0.0224 139 PHE A C 1121 O O . PHE A 141 ? 0.2346 0.4010 0.1771 -0.0471 -0.0175 0.0348 139 PHE A O 1122 C CB . PHE A 141 ? 0.2156 0.3256 0.1556 -0.0338 -0.0540 0.0045 139 PHE A CB 1123 C CG . PHE A 141 ? 0.2170 0.3261 0.1772 0.0102 -0.0869 0.0108 139 PHE A CG 1124 C CD1 . PHE A 141 ? 0.2258 0.3222 0.1968 0.0465 -0.0807 0.0077 139 PHE A CD1 1125 C CD2 . PHE A 141 ? 0.2488 0.3426 0.1790 0.0210 -0.0912 -0.0149 139 PHE A CD2 1126 C CE1 . PHE A 141 ? 0.2440 0.3507 0.2162 0.0554 -0.0848 0.0080 139 PHE A CE1 1127 C CE2 . PHE A 141 ? 0.2666 0.3327 0.1788 0.0405 -0.1159 -0.0189 139 PHE A CE2 1128 C CZ . PHE A 141 ? 0.2675 0.3369 0.2048 0.0379 -0.0789 -0.0040 139 PHE A CZ 1129 N N . THR A 142 ? 0.2503 0.2329 0.1492 -0.0329 -0.0530 -0.0315 140 THR A N 1130 C CA . THR A 142 ? 0.3117 0.2253 0.1594 -0.0005 -0.0640 -0.0286 140 THR A CA 1131 C C . THR A 142 ? 0.2632 0.2145 0.1327 0.0345 -0.0480 -0.0146 140 THR A C 1132 O O . THR A 142 ? 0.2986 0.2407 0.1502 0.0585 -0.0213 -0.0218 140 THR A O 1133 C CB . THR A 142 ? 0.4143 0.2769 0.2065 0.0000 -0.0447 -0.0470 140 THR A CB 1134 O OG1 . THR A 142 ? 0.4540 0.2950 0.2681 -0.0737 -0.0179 -0.0643 140 THR A OG1 1135 C CG2 . THR A 142 ? 0.4651 0.3254 0.2245 0.0024 -0.0655 -0.0461 140 THR A CG2 1136 N N . ALA A 143 ? 0.1414 0.2106 0.0775 0.0081 -0.0442 -0.0324 141 ALA A N 1137 C CA . ALA A 143 ? 0.1213 0.2100 0.0822 0.0007 0.0037 -0.0320 141 ALA A CA 1138 C C . ALA A 143 ? 0.1368 0.2062 0.0823 -0.0242 -0.0170 -0.0110 141 ALA A C 1139 O O . ALA A 143 ? 0.1761 0.1748 0.0790 -0.0365 -0.0006 0.0093 141 ALA A O 1140 C CB . ALA A 143 ? 0.1710 0.1592 0.0951 0.0256 -0.0116 -0.0410 141 ALA A CB 1141 N N . VAL A 144 ? 0.1017 0.2148 0.0982 -0.0216 -0.0104 -0.0029 142 VAL A N 1142 C CA . VAL A 144 ? 0.1043 0.2084 0.1101 0.0500 -0.0155 0.0011 142 VAL A CA 1143 C C . VAL A 144 ? 0.1397 0.1640 0.0851 0.0035 -0.0155 -0.0027 142 VAL A C 1144 O O . VAL A 144 ? 0.1665 0.1739 0.0945 0.0092 0.0303 0.0117 142 VAL A O 1145 C CB . VAL A 144 ? 0.1306 0.2418 0.1180 0.0112 -0.0247 -0.0015 142 VAL A CB 1146 C CG1 . VAL A 144 ? 0.1164 0.2630 0.1214 -0.0137 -0.0198 0.0253 142 VAL A CG1 1147 C CG2 . VAL A 144 ? 0.1958 0.2031 0.1300 0.0544 -0.0045 0.0012 142 VAL A CG2 1148 N N . ASN A 145 ? 0.1230 0.1583 0.0851 0.0141 -0.0146 0.0024 143 ASN A N 1149 C CA . ASN A 145 ? 0.0785 0.1764 0.0828 -0.0043 -0.0423 -0.0049 143 ASN A CA 1150 C C . ASN A 145 ? 0.0985 0.1921 0.0911 -0.0370 -0.0188 -0.0045 143 ASN A C 1151 O O . ASN A 145 ? 0.1147 0.1921 0.0914 -0.0499 0.0162 0.0176 143 ASN A O 1152 C CB . ASN A 145 ? 0.1054 0.2114 0.0597 -0.0090 -0.0366 0.0199 143 ASN A CB 1153 C CG . ASN A 145 ? 0.1003 0.2178 0.0844 0.0312 0.0134 0.0212 143 ASN A CG 1154 O OD1 . ASN A 145 ? 0.0958 0.1835 0.1063 -0.0287 0.0046 0.0056 143 ASN A OD1 1155 N ND2 . ASN A 145 ? 0.1170 0.2157 0.0855 0.0557 0.0019 0.0297 143 ASN A ND2 1156 N N . LEU A 146 ? 0.0820 0.1737 0.0916 -0.0200 -0.0169 -0.0104 144 LEU A N 1157 C CA . LEU A 146 ? 0.0523 0.1429 0.1100 0.0207 0.0003 0.0124 144 LEU A CA 1158 C C . LEU A 146 ? 0.0472 0.1557 0.1298 0.0413 0.0052 -0.0079 144 LEU A C 1159 O O . LEU A 146 ? 0.0750 0.2046 0.1237 0.0185 0.0137 -0.0287 144 LEU A O 1160 C CB . LEU A 146 ? 0.0785 0.1583 0.1163 0.0515 -0.0006 0.0457 144 LEU A CB 1161 C CG . LEU A 146 ? 0.1377 0.2783 0.1321 0.1088 -0.0136 0.0483 144 LEU A CG 1162 C CD1 . LEU A 146 ? 0.1915 0.3476 0.1179 0.1660 -0.0088 0.0415 144 LEU A CD1 1163 C CD2 . LEU A 146 ? 0.0909 0.2295 0.1272 0.0571 -0.0163 0.0609 144 LEU A CD2 1164 N N . LEU A 147 ? 0.0937 0.1045 0.1295 -0.0011 -0.0128 0.0088 145 LEU A N 1165 C CA . LEU A 147 ? 0.1050 0.1437 0.1223 0.0353 -0.0076 0.0104 145 LEU A CA 1166 C C . LEU A 147 ? 0.0981 0.1498 0.1123 -0.0002 0.0097 -0.0051 145 LEU A C 1167 O O . LEU A 147 ? 0.1274 0.2419 0.1209 -0.0093 -0.0158 -0.0296 145 LEU A O 1168 C CB . LEU A 147 ? 0.1741 0.1539 0.1511 0.0585 -0.0116 0.0347 145 LEU A CB 1169 C CG . LEU A 147 ? 0.1472 0.1512 0.1696 0.0619 0.0120 0.0168 145 LEU A CG 1170 C CD1 . LEU A 147 ? 0.0979 0.1932 0.1817 0.0531 -0.0032 0.0158 145 LEU A CD1 1171 C CD2 . LEU A 147 ? 0.2451 0.1608 0.1739 0.0148 -0.0279 0.0313 145 LEU A CD2 1172 N N . HIS A 148 ? 0.1520 0.1828 0.0700 -0.0210 -0.0180 -0.0176 146 HIS A N 1173 C CA . HIS A 148 ? 0.1414 0.1765 0.1051 -0.0638 -0.0083 0.0038 146 HIS A CA 1174 C C . HIS A 148 ? 0.1097 0.1501 0.1521 -0.0842 0.0211 0.0192 146 HIS A C 1175 O O . HIS A 148 ? 0.1160 0.2122 0.1666 0.0335 0.0242 0.0088 146 HIS A O 1176 C CB . HIS A 148 ? 0.1653 0.1981 0.1076 -0.0419 -0.0213 -0.0072 146 HIS A CB 1177 C CG . HIS A 148 ? 0.1810 0.1891 0.1107 0.0006 -0.0143 -0.0507 146 HIS A CG 1178 N ND1 . HIS A 148 ? 0.2646 0.2490 0.1384 0.0239 0.0226 -0.0184 146 HIS A ND1 1179 C CD2 . HIS A 148 ? 0.1878 0.1973 0.0679 0.0187 0.0044 -0.0696 146 HIS A CD2 1180 C CE1 . HIS A 148 ? 0.1699 0.1233 0.1213 0.1090 0.0384 -0.0289 146 HIS A CE1 1181 N NE2 . HIS A 148 ? 0.2482 0.2067 0.1308 0.0076 0.0440 -0.0389 146 HIS A NE2 1182 N N . SER A 149 ? 0.1386 0.1880 0.1992 -0.0343 -0.0030 -0.0005 147 SER A N 1183 C CA . SER A 149 ? 0.1856 0.1598 0.2085 -0.0221 -0.0031 -0.0071 147 SER A CA 1184 C C . SER A 149 ? 0.2691 0.1843 0.2173 -0.0135 0.0097 -0.0382 147 SER A C 1185 O O . SER A 149 ? 0.2236 0.1776 0.2156 0.0074 0.0294 -0.0216 147 SER A O 1186 C CB . SER A 149 ? 0.2196 0.2098 0.2264 0.0502 0.0240 0.0092 147 SER A CB 1187 O OG . SER A 149 ? 0.3298 0.2365 0.2452 0.0093 0.0564 -0.0121 147 SER A OG 1188 N N . GLY A 150 ? 0.3327 0.2295 0.2302 0.0240 0.0111 -0.0434 148 GLY A N 1189 C CA . GLY A 150 ? 0.3077 0.2425 0.2376 -0.0287 -0.0283 -0.0208 148 GLY A CA 1190 C C . GLY A 150 ? 0.3277 0.2576 0.2431 0.0247 -0.0353 -0.0399 148 GLY A C 1191 O O . GLY A 150 ? 0.3910 0.2938 0.2534 0.0652 -0.0688 -0.0458 148 GLY A O 1192 N N . GLN A 151 ? 0.3181 0.2434 0.2351 0.0639 -0.0067 -0.0155 149 GLN A N 1193 C CA . GLN A 151 ? 0.2772 0.2485 0.2139 0.0069 -0.0277 -0.0074 149 GLN A CA 1194 C C . GLN A 151 ? 0.2665 0.2534 0.2129 -0.0124 -0.0208 -0.0005 149 GLN A C 1195 O O . GLN A 151 ? 0.2662 0.3083 0.2093 0.0126 -0.0318 0.0134 149 GLN A O 1196 C CB . GLN A 151 ? 0.3726 0.3310 0.2179 -0.0342 -0.0252 0.0137 149 GLN A CB 1197 C CG . GLN A 151 ? 0.4115 0.3883 0.2291 -0.0296 -0.0139 0.0100 149 GLN A CG 1198 C CD . GLN A 151 ? 0.4443 0.4368 0.2379 -0.0267 -0.0069 0.0074 149 GLN A CD 1199 O OE1 . GLN A 151 ? 0.4558 0.4538 0.2409 -0.0264 -0.0048 0.0065 149 GLN A OE1 1200 N NE2 . GLN A 151 ? 0.4558 0.4539 0.2409 -0.0264 -0.0047 0.0066 149 GLN A NE2 1201 N N . THR A 152 ? 0.2559 0.2328 0.2142 -0.0276 -0.0047 -0.0156 150 THR A N 1202 C CA . THR A 152 ? 0.2306 0.2317 0.2335 -0.0307 0.0179 -0.0787 150 THR A CA 1203 C C . THR A 152 ? 0.2016 0.2565 0.2167 -0.0392 0.0309 -0.0532 150 THR A C 1204 O O . THR A 152 ? 0.1409 0.2623 0.2250 -0.0265 0.0387 -0.0273 150 THR A O 1205 C CB . THR A 152 ? 0.3430 0.3175 0.2843 -0.0604 0.0357 -0.0826 150 THR A CB 1206 O OG1 . THR A 152 ? 0.4236 0.3662 0.3271 -0.0876 0.0337 -0.1089 150 THR A OG1 1207 C CG2 . THR A 152 ? 0.3637 0.3492 0.2945 -0.0444 0.0357 -0.1053 150 THR A CG2 1208 N N . HIS A 153 ? 0.1625 0.2460 0.1975 -0.0325 0.0227 -0.0793 151 HIS A N 1209 C CA . HIS A 153 ? 0.1396 0.1850 0.1927 -0.1322 0.0081 -0.0159 151 HIS A CA 1210 C C . HIS A 153 ? 0.1287 0.1893 0.1703 -0.0591 0.0042 -0.0459 151 HIS A C 1211 O O . HIS A 153 ? 0.1532 0.2510 0.1939 -0.0197 0.0398 -0.0451 151 HIS A O 1212 C CB . HIS A 153 ? 0.1943 0.2511 0.2011 -0.0851 -0.0001 0.0076 151 HIS A CB 1213 C CG . HIS A 153 ? 0.1686 0.2985 0.2258 -0.0866 0.0249 0.0513 151 HIS A CG 1214 N ND1 . HIS A 153 ? 0.1952 0.3900 0.2433 -0.0989 0.0227 0.0518 151 HIS A ND1 1215 C CD2 . HIS A 153 ? 0.2249 0.3436 0.2177 -0.0886 0.0069 0.0307 151 HIS A CD2 1216 C CE1 . HIS A 153 ? 0.2296 0.4200 0.2359 -0.0584 -0.0029 0.0417 151 HIS A CE1 1217 N NE2 . HIS A 153 ? 0.2168 0.3736 0.2249 -0.0571 -0.0130 0.0540 151 HIS A NE2 1218 N N . PHE A 154 ? 0.1155 0.1558 0.1562 -0.0452 -0.0027 -0.0145 152 PHE A N 1219 C CA . PHE A 154 ? 0.1086 0.1846 0.1253 -0.0360 -0.0226 0.0225 152 PHE A CA 1220 C C . PHE A 154 ? 0.1456 0.2053 0.1329 0.0004 -0.0028 0.0115 152 PHE A C 1221 O O . PHE A 154 ? 0.1263 0.2037 0.1465 -0.0030 -0.0103 0.0140 152 PHE A O 1222 C CB . PHE A 154 ? 0.1362 0.1903 0.1166 -0.0390 -0.0036 0.0022 152 PHE A CB 1223 C CG . PHE A 154 ? 0.1395 0.2016 0.1202 -0.0419 0.0042 -0.0049 152 PHE A CG 1224 C CD1 . PHE A 154 ? 0.1293 0.2224 0.1269 -0.0068 0.0121 -0.0284 152 PHE A CD1 1225 C CD2 . PHE A 154 ? 0.1653 0.1808 0.0957 -0.0092 -0.0150 -0.0148 152 PHE A CD2 1226 C CE1 . PHE A 154 ? 0.1216 0.1847 0.1250 0.0195 0.0119 -0.0225 152 PHE A CE1 1227 C CE2 . PHE A 154 ? 0.1224 0.1816 0.1177 -0.0414 0.0133 -0.0192 152 PHE A CE2 1228 C CZ . PHE A 154 ? 0.1036 0.1924 0.1315 -0.0047 0.0176 -0.0305 152 PHE A CZ 1229 N N . ASP A 155 ? 0.1332 0.2072 0.1097 0.0015 -0.0399 0.0229 153 ASP A N 1230 C CA . ASP A 155 ? 0.1495 0.1930 0.1117 -0.0509 -0.0230 -0.0018 153 ASP A CA 1231 C C . ASP A 155 ? 0.1234 0.2072 0.1085 -0.0375 -0.0153 -0.0016 153 ASP A C 1232 O O . ASP A 155 ? 0.1739 0.2363 0.1002 0.0191 -0.0030 0.0066 153 ASP A O 1233 C CB . ASP A 155 ? 0.1813 0.1650 0.1257 -0.0464 -0.0037 0.0194 153 ASP A CB 1234 C CG . ASP A 155 ? 0.1931 0.1934 0.1550 -0.0587 0.0179 0.0259 153 ASP A CG 1235 O OD1 . ASP A 155 ? 0.1688 0.2239 0.1810 -0.0838 0.0149 0.0271 153 ASP A OD1 1236 O OD2 . ASP A 155 ? 0.2439 0.2400 0.1649 -0.0691 -0.0072 0.0187 153 ASP A OD2 1237 N N . ALA A 156 ? 0.0961 0.1749 0.0950 -0.0004 -0.0099 -0.0007 154 ALA A N 1238 C CA . ALA A 156 ? 0.0818 0.1850 0.1182 0.0078 -0.0151 -0.0101 154 ALA A CA 1239 C C . ALA A 156 ? 0.0832 0.1962 0.1236 -0.0076 -0.0202 0.0339 154 ALA A C 1240 O O . ALA A 156 ? 0.0963 0.2166 0.1289 0.0017 -0.0009 0.0312 154 ALA A O 1241 C CB . ALA A 156 ? 0.0435 0.1872 0.1316 0.0534 0.0592 -0.0059 154 ALA A CB 1242 N N . LEU A 157 ? 0.0254 0.1919 0.1181 -0.0142 -0.0115 0.0112 155 LEU A N 1243 C CA . LEU A 157 ? 0.0631 0.1908 0.0797 0.0022 -0.0020 -0.0405 155 LEU A CA 1244 C C . LEU A 157 ? 0.1119 0.2314 0.0831 -0.0095 -0.0054 -0.0203 155 LEU A C 1245 O O . LEU A 157 ? 0.1272 0.2430 0.0982 0.0082 -0.0275 -0.0037 155 LEU A O 1246 C CB . LEU A 157 ? 0.0794 0.2167 0.0913 -0.0114 0.0210 -0.0247 155 LEU A CB 1247 C CG . LEU A 157 ? 0.0937 0.1650 0.1012 0.0073 0.0431 -0.0111 155 LEU A CG 1248 C CD1 . LEU A 157 ? 0.1575 0.2177 0.1166 -0.0062 0.0545 -0.0290 155 LEU A CD1 1249 C CD2 . LEU A 157 ? 0.1656 0.1462 0.1146 0.0254 0.0331 0.0442 155 LEU A CD2 1250 N N . ARG A 158 ? 0.1367 0.2426 0.0696 0.0077 -0.0108 0.0068 156 ARG A N 1251 C CA . ARG A 158 ? 0.0950 0.2889 0.0865 -0.0060 0.0103 -0.0045 156 ARG A CA 1252 C C . ARG A 158 ? 0.1254 0.2613 0.1088 0.0138 0.0014 0.0014 156 ARG A C 1253 O O . ARG A 158 ? 0.1317 0.2524 0.1211 -0.0039 -0.0055 0.0226 156 ARG A O 1254 C CB . ARG A 158 ? 0.0948 0.2837 0.0929 0.0178 0.0260 -0.0153 156 ARG A CB 1255 C CG . ARG A 158 ? 0.0794 0.3388 0.1076 0.0663 0.0013 -0.0190 156 ARG A CG 1256 C CD . ARG A 158 ? 0.1800 0.4424 0.1487 0.1339 0.0175 -0.0103 156 ARG A CD 1257 N NE . ARG A 158 ? 0.2643 0.5470 0.1559 0.1252 0.0307 0.0146 156 ARG A NE 1258 C CZ . ARG A 158 ? 0.3825 0.5489 0.1832 0.1910 0.0112 0.0007 156 ARG A CZ 1259 N NH1 . ARG A 158 ? 0.4496 0.5804 0.2046 0.1597 -0.0400 -0.0156 156 ARG A NH1 1260 N NH2 . ARG A 158 ? 0.4461 0.5018 0.1696 0.2836 0.0309 0.0156 156 ARG A NH2 1261 N N . ILE A 159 ? 0.0929 0.2464 0.1169 0.0157 -0.0058 0.0270 157 ILE A N 1262 C CA . ILE A 159 ? 0.0863 0.2381 0.1204 0.0012 -0.0105 0.0436 157 ILE A CA 1263 C C . ILE A 159 ? 0.1350 0.1929 0.1003 0.0317 -0.0103 0.0512 157 ILE A C 1264 O O . ILE A 159 ? 0.1742 0.1892 0.1222 0.0080 -0.0015 0.0255 157 ILE A O 1265 C CB . ILE A 159 ? 0.0830 0.2532 0.1328 -0.0251 -0.0582 0.0636 157 ILE A CB 1266 C CG1 . ILE A 159 ? 0.1273 0.1784 0.1500 -0.0662 -0.0367 0.0756 157 ILE A CG1 1267 C CG2 . ILE A 159 ? 0.1624 0.2531 0.1295 0.0048 -0.0632 0.1063 157 ILE A CG2 1268 C CD1 . ILE A 159 ? 0.2000 0.1956 0.1821 -0.0577 -0.0353 0.0602 157 ILE A CD1 1269 N N . LEU A 160 ? 0.1682 0.1470 0.0760 -0.0056 -0.0232 0.0592 158 LEU A N 1270 C CA . LEU A 160 ? 0.2056 0.1875 0.0886 -0.0255 0.0014 0.0204 158 LEU A CA 1271 C C . LEU A 160 ? 0.2044 0.2196 0.1125 -0.0051 -0.0096 0.0304 158 LEU A C 1272 O O . LEU A 160 ? 0.1907 0.2340 0.1180 -0.0069 -0.0245 0.0296 158 LEU A O 1273 C CB . LEU A 160 ? 0.2411 0.1940 0.0920 -0.0471 0.0031 -0.0295 158 LEU A CB 1274 C CG . LEU A 160 ? 0.2795 0.2470 0.1312 0.0096 -0.0105 0.0081 158 LEU A CG 1275 C CD1 . LEU A 160 ? 0.2692 0.1928 0.1152 0.0636 -0.0109 0.0113 158 LEU A CD1 1276 C CD2 . LEU A 160 ? 0.2587 0.2738 0.1505 0.0044 -0.0183 0.0044 158 LEU A CD2 1277 N N . PRO A 161 ? 0.1999 0.2284 0.1160 -0.0215 0.0010 0.0222 159 PRO A N 1278 C CA . PRO A 161 ? 0.2076 0.3028 0.1171 -0.0370 0.0122 0.0024 159 PRO A CA 1279 C C . PRO A 161 ? 0.2273 0.2708 0.1173 -0.0565 -0.0281 0.0186 159 PRO A C 1280 O O . PRO A 161 ? 0.2824 0.2792 0.1535 -0.0736 -0.0191 0.0016 159 PRO A O 1281 C CB . PRO A 161 ? 0.1956 0.3659 0.1344 -0.0299 0.0278 -0.0178 159 PRO A CB 1282 C CG . PRO A 161 ? 0.2245 0.3791 0.1267 -0.0511 0.0283 -0.0438 159 PRO A CG 1283 C CD . PRO A 161 ? 0.2015 0.2819 0.0985 -0.0373 0.0150 0.0037 159 PRO A CD 1284 N N . GLN A 162 ? 0.1480 0.2427 0.0978 -0.0356 -0.0492 0.0426 160 GLN A N 1285 C CA . GLN A 162 ? 0.1450 0.2014 0.1324 -0.0459 -0.0460 0.0475 160 GLN A CA 1286 C C . GLN A 162 ? 0.1406 0.2579 0.1439 -0.0134 -0.0652 0.0735 160 GLN A C 1287 O O . GLN A 162 ? 0.1839 0.3108 0.1755 -0.0693 -0.0615 0.0526 160 GLN A O 1288 C CB . GLN A 162 ? 0.1308 0.2458 0.1409 -0.0040 -0.0498 0.0652 160 GLN A CB 1289 C CG . GLN A 162 ? 0.1278 0.2437 0.1487 -0.0057 -0.0310 0.0287 160 GLN A CG 1290 C CD . GLN A 162 ? 0.1753 0.1915 0.1298 -0.0095 -0.0226 0.0083 160 GLN A CD 1291 O OE1 . GLN A 162 ? 0.2555 0.1957 0.1650 -0.0116 0.0072 0.0454 160 GLN A OE1 1292 N NE2 . GLN A 162 ? 0.1284 0.1713 0.0949 -0.0222 -0.0022 0.0303 160 GLN A NE2 1293 N N . PHE A 163 ? 0.1830 0.2213 0.1386 -0.0503 -0.0489 0.0772 161 PHE A N 1294 C CA . PHE A 163 ? 0.2128 0.2526 0.1572 -0.0894 -0.0339 0.0435 161 PHE A CA 1295 C C . PHE A 163 ? 0.2580 0.2813 0.2289 -0.0880 -0.0188 0.0568 161 PHE A C 1296 O O . PHE A 163 ? 0.2957 0.3032 0.2498 -0.0871 0.0376 0.0655 161 PHE A O 1297 C CB . PHE A 163 ? 0.1907 0.2178 0.1180 -0.0663 -0.0206 0.0285 161 PHE A CB 1298 C CG . PHE A 163 ? 0.1892 0.2707 0.1162 -0.0440 -0.0159 0.0583 161 PHE A CG 1299 C CD1 . PHE A 163 ? 0.1619 0.3032 0.1143 -0.0405 -0.0145 0.0716 161 PHE A CD1 1300 C CD2 . PHE A 163 ? 0.1473 0.2971 0.1101 -0.0480 -0.0114 0.0394 161 PHE A CD2 1301 C CE1 . PHE A 163 ? 0.1612 0.2815 0.1074 0.0018 -0.0479 0.0655 161 PHE A CE1 1302 C CE2 . PHE A 163 ? 0.1562 0.2946 0.1233 -0.0514 0.0086 0.0292 161 PHE A CE2 1303 C CZ . PHE A 163 ? 0.1750 0.2978 0.1247 -0.0336 -0.0085 0.0568 161 PHE A CZ 1304 N N . GLU A 164 ? 0.3303 0.3103 0.2872 -0.0219 -0.0196 0.0344 162 GLU A N 1305 C CA . GLU A 164 ? 0.4369 0.4850 0.3592 -0.0179 -0.0483 0.0083 162 GLU A CA 1306 C C . GLU A 164 ? 0.4969 0.5513 0.4112 0.0062 -0.0286 0.0172 162 GLU A C 1307 O O . GLU A 164 ? 0.5761 0.5813 0.4428 -0.0160 -0.0146 0.0089 162 GLU A O 1308 C CB . GLU A 164 ? 0.4737 0.5760 0.3894 0.0171 -0.0770 -0.0184 162 GLU A CB 1309 C CG . GLU A 164 ? 0.4980 0.6437 0.4141 -0.0290 -0.1081 -0.0459 162 GLU A CG 1310 C CD . GLU A 164 ? 0.5336 0.6925 0.4473 -0.0539 -0.0938 -0.0430 162 GLU A CD 1311 O OE1 . GLU A 164 ? 0.4963 0.6446 0.4535 -0.1128 -0.1098 -0.0569 162 GLU A OE1 1312 O OE2 . GLU A 164 ? 0.5758 0.7527 0.4628 -0.0270 -0.0859 -0.0400 162 GLU A OE2 1313 N N . GLU B 3 ? 0.7777 0.6493 0.4193 0.0711 0.1728 0.0974 80 GLU B N 1314 C CA . GLU B 3 ? 0.7527 0.6628 0.4225 0.0525 0.1534 0.1021 80 GLU B CA 1315 C C . GLU B 3 ? 0.6874 0.5971 0.4086 0.0443 0.1446 0.1005 80 GLU B C 1316 O O . GLU B 3 ? 0.7182 0.5882 0.4063 0.0400 0.1180 0.1334 80 GLU B O 1317 C CB . GLU B 3 ? 0.7661 0.7265 0.4442 0.0491 0.1441 0.0845 80 GLU B CB 1318 C CG . GLU B 3 ? 0.7796 0.7792 0.4624 0.0503 0.1372 0.0696 80 GLU B CG 1319 C CD . GLU B 3 ? 0.7922 0.8201 0.4767 0.0523 0.1332 0.0577 80 GLU B CD 1320 O OE1 . GLU B 3 ? 0.7967 0.8339 0.4815 0.0530 0.1320 0.0536 80 GLU B OE1 1321 O OE2 . GLU B 3 ? 0.7967 0.8339 0.4815 0.0530 0.1320 0.0536 80 GLU B OE2 1322 N N . PRO B 4 ? 0.6083 0.5353 0.4036 0.0477 0.1565 0.0669 81 PRO B N 1323 C CA . PRO B 4 ? 0.5499 0.5056 0.4088 0.0600 0.1496 0.0489 81 PRO B CA 1324 C C . PRO B 4 ? 0.4424 0.4805 0.3931 0.0935 0.1592 0.0409 81 PRO B C 1325 O O . PRO B 4 ? 0.4392 0.5263 0.4183 0.0926 0.1454 0.0100 81 PRO B O 1326 C CB . PRO B 4 ? 0.6037 0.5213 0.4156 0.0528 0.1425 0.0423 81 PRO B CB 1327 C CG . PRO B 4 ? 0.6282 0.5259 0.4203 0.0258 0.1615 0.0541 81 PRO B CG 1328 C CD . PRO B 4 ? 0.6260 0.5292 0.4181 0.0254 0.1554 0.0595 81 PRO B CD 1329 N N . LEU B 5 ? 0.3220 0.4174 0.3476 0.0811 0.1612 0.0748 82 LEU B N 1330 C CA . LEU B 5 ? 0.2894 0.3993 0.3338 0.0408 0.1482 0.0502 82 LEU B CA 1331 C C . LEU B 5 ? 0.2396 0.3464 0.2937 0.0486 0.1155 0.0751 82 LEU B C 1332 O O . LEU B 5 ? 0.1875 0.3502 0.2822 0.0521 0.0874 0.0878 82 LEU B O 1333 C CB . LEU B 5 ? 0.2874 0.3904 0.3393 0.0232 0.1403 0.0383 82 LEU B CB 1334 C CG . LEU B 5 ? 0.2726 0.3910 0.3337 0.0474 0.1301 0.0303 82 LEU B CG 1335 C CD1 . LEU B 5 ? 0.3094 0.4126 0.3353 0.0401 0.1166 0.0418 82 LEU B CD1 1336 C CD2 . LEU B 5 ? 0.3025 0.4264 0.3221 0.0078 0.1365 0.0224 82 LEU B CD2 1337 N N . SER B 6 ? 0.2575 0.3679 0.2867 0.0435 0.1081 0.0277 83 SER B N 1338 C CA . SER B 6 ? 0.2534 0.3197 0.2602 0.0567 0.1110 0.0205 83 SER B CA 1339 C C . SER B 6 ? 0.2073 0.2976 0.2379 0.0238 0.0847 0.0104 83 SER B C 1340 O O . SER B 6 ? 0.2125 0.3705 0.2341 0.0050 0.0889 -0.0042 83 SER B O 1341 C CB . SER B 6 ? 0.3666 0.3556 0.2791 0.0992 0.1406 0.0006 83 SER B CB 1342 O OG . SER B 6 ? 0.4059 0.3590 0.2965 0.1395 0.1496 0.0001 83 SER B OG 1343 N N . ILE B 7 ? 0.2046 0.2400 0.2165 0.0153 0.0708 0.0004 84 ILE B N 1344 C CA . ILE B 7 ? 0.2139 0.2599 0.2089 0.0675 0.0662 0.0225 84 ILE B CA 1345 C C . ILE B 7 ? 0.2077 0.2868 0.1987 0.0741 0.0669 0.0292 84 ILE B C 1346 O O . ILE B 7 ? 0.2712 0.2934 0.1737 0.0826 0.0923 0.0213 84 ILE B O 1347 C CB . ILE B 7 ? 0.1914 0.2180 0.2292 0.0472 0.0449 0.0272 84 ILE B CB 1348 C CG1 . ILE B 7 ? 0.1636 0.2252 0.2487 0.0597 0.0284 -0.0017 84 ILE B CG1 1349 C CG2 . ILE B 7 ? 0.1934 0.2208 0.2156 0.0535 0.0679 0.0387 84 ILE B CG2 1350 C CD1 . ILE B 7 ? 0.1983 0.2479 0.2611 0.0868 0.0158 0.0056 84 ILE B CD1 1351 N N . LEU B 8 ? 0.1640 0.2888 0.1899 0.0692 0.0481 0.0429 85 LEU B N 1352 C CA . LEU B 8 ? 0.1631 0.2757 0.2053 0.0696 0.0109 0.0432 85 LEU B CA 1353 C C . LEU B 8 ? 0.1586 0.2777 0.1911 0.0238 0.0222 0.0398 85 LEU B C 1354 O O . LEU B 8 ? 0.1539 0.3050 0.2039 0.0325 0.0359 0.0380 85 LEU B O 1355 C CB . LEU B 8 ? 0.1897 0.3111 0.2559 0.1083 0.0096 0.0089 85 LEU B CB 1356 C CG . LEU B 8 ? 0.2307 0.3536 0.3044 0.1236 0.0071 -0.0478 85 LEU B CG 1357 C CD1 . LEU B 8 ? 0.1697 0.3714 0.3120 0.0973 -0.0292 -0.0440 85 LEU B CD1 1358 C CD2 . LEU B 8 ? 0.2956 0.3851 0.3476 0.1493 0.0458 -0.0727 85 LEU B CD2 1359 N N . VAL B 9 ? 0.1917 0.2371 0.1793 -0.0036 0.0120 0.0315 86 VAL B N 1360 C CA . VAL B 9 ? 0.1683 0.2320 0.1503 0.0493 0.0030 0.0488 86 VAL B CA 1361 C C . VAL B 9 ? 0.2261 0.2511 0.1495 0.0239 -0.0079 0.0396 86 VAL B C 1362 O O . VAL B 9 ? 0.2330 0.2525 0.1611 0.0332 -0.0007 0.0241 86 VAL B O 1363 C CB . VAL B 9 ? 0.1286 0.2169 0.1387 0.0081 0.0284 0.0199 86 VAL B CB 1364 C CG1 . VAL B 9 ? 0.0929 0.2044 0.1389 0.0276 0.0499 0.0223 86 VAL B CG1 1365 C CG2 . VAL B 9 ? 0.1303 0.2373 0.1153 0.0093 -0.0070 0.0181 86 VAL B CG2 1366 N N . ARG B 10 ? 0.2453 0.2736 0.1309 0.0325 -0.0167 0.0458 87 ARG B N 1367 C CA . ARG B 10 ? 0.2327 0.2586 0.1226 -0.0031 -0.0461 0.0717 87 ARG B CA 1368 C C . ARG B 10 ? 0.2195 0.2820 0.1269 0.0162 -0.0017 0.0354 87 ARG B C 1369 O O . ARG B 10 ? 0.2073 0.2759 0.1360 0.0137 0.0063 0.0202 87 ARG B O 1370 C CB . ARG B 10 ? 0.2879 0.2630 0.1197 -0.0309 -0.0866 0.0675 87 ARG B CB 1371 C CG . ARG B 10 ? 0.3310 0.2974 0.1436 -0.0676 -0.1070 0.0605 87 ARG B CG 1372 C CD . ARG B 10 ? 0.3809 0.3602 0.1714 -0.0893 -0.1061 0.0630 87 ARG B CD 1373 N NE . ARG B 10 ? 0.3892 0.4171 0.1845 -0.0626 -0.0827 0.0545 87 ARG B NE 1374 C CZ . ARG B 10 ? 0.3970 0.4670 0.1959 -0.0397 -0.0629 0.0504 87 ARG B CZ 1375 N NH1 . ARG B 10 ? 0.3995 0.4845 0.2000 -0.0322 -0.0565 0.0492 87 ARG B NH1 1376 N NH2 . ARG B 10 ? 0.3995 0.4845 0.2000 -0.0322 -0.0564 0.0493 87 ARG B NH2 1377 N N . ASN B 11 ? 0.1634 0.2267 0.1191 -0.0076 0.0065 -0.0059 88 ASN B N 1378 C CA . ASN B 11 ? 0.2050 0.2484 0.1282 -0.0311 0.0107 0.0062 88 ASN B CA 1379 C C . ASN B 11 ? 0.2237 0.2741 0.1430 0.0221 0.0009 0.0333 88 ASN B C 1380 O O . ASN B 11 ? 0.2363 0.3149 0.1724 0.0627 -0.0102 0.0507 88 ASN B O 1381 C CB . ASN B 11 ? 0.2181 0.2146 0.1278 -0.0243 0.0072 0.0048 88 ASN B CB 1382 C CG . ASN B 11 ? 0.2780 0.2358 0.1233 0.0311 0.0003 0.0088 88 ASN B CG 1383 O OD1 . ASN B 11 ? 0.2707 0.2695 0.1320 0.0537 -0.0035 0.0113 88 ASN B OD1 1384 N ND2 . ASN B 11 ? 0.3773 0.2350 0.1184 0.0342 0.0270 -0.0009 88 ASN B ND2 1385 N N . ASN B 12 ? 0.1954 0.2821 0.1504 0.0609 -0.0069 0.0828 89 ASN B N 1386 C CA . ASN B 12 ? 0.2139 0.3161 0.1692 0.0345 -0.0148 0.0616 89 ASN B CA 1387 C C . ASN B 12 ? 0.2631 0.3287 0.1761 0.0008 -0.0291 0.0470 89 ASN B C 1388 O O . ASN B 12 ? 0.2731 0.3540 0.1595 0.0067 -0.0230 0.0362 89 ASN B O 1389 C CB . ASN B 12 ? 0.2113 0.3110 0.1732 0.0250 -0.0017 0.0568 89 ASN B CB 1390 C CG . ASN B 12 ? 0.2582 0.2953 0.1723 0.0469 -0.0142 0.0709 89 ASN B CG 1391 O OD1 . ASN B 12 ? 0.2940 0.2753 0.1925 0.0314 0.0057 0.0621 89 ASN B OD1 1392 N ND2 . ASN B 12 ? 0.2398 0.2551 0.1570 0.0466 0.0022 0.0737 89 ASN B ND2 1393 N N . LYS B 13 ? 0.3057 0.2953 0.2039 0.0210 -0.0197 0.0609 90 LYS B N 1394 C CA . LYS B 13 ? 0.3327 0.2981 0.2089 0.0188 -0.0323 0.0589 90 LYS B CA 1395 C C . LYS B 13 ? 0.3252 0.3013 0.1943 0.0201 -0.0361 0.0747 90 LYS B C 1396 O O . LYS B 13 ? 0.3320 0.3262 0.2145 0.0538 -0.0408 0.0872 90 LYS B O 1397 C CB . LYS B 13 ? 0.4014 0.2941 0.2356 -0.0014 -0.0251 0.0575 90 LYS B CB 1398 C CG . LYS B 13 ? 0.4362 0.3459 0.2443 0.0075 -0.0173 0.0493 90 LYS B CG 1399 C CD . LYS B 13 ? 0.4654 0.3927 0.2523 0.0122 -0.0095 0.0414 90 LYS B CD 1400 C CE . LYS B 13 ? 0.4867 0.4280 0.2585 0.0128 -0.0031 0.0357 90 LYS B CE 1401 N NZ . LYS B 13 ? 0.4979 0.4461 0.2616 0.0127 0.0005 0.0334 90 LYS B NZ 1402 N N . GLY B 14 ? 0.3157 0.3292 0.1875 0.0318 -0.0349 0.0928 91 GLY B N 1403 C CA . GLY B 14 ? 0.2452 0.3039 0.1765 0.0093 -0.0059 0.0949 91 GLY B CA 1404 C C . GLY B 14 ? 0.2263 0.3373 0.1898 -0.0208 0.0244 0.0617 91 GLY B C 1405 O O . GLY B 14 ? 0.2766 0.4033 0.2008 -0.0277 0.0336 0.0474 91 GLY B O 1406 N N . ARG B 15 ? 0.2289 0.3028 0.1856 0.0771 0.0355 0.0569 92 ARG B N 1407 C CA . ARG B 15 ? 0.2994 0.2651 0.2101 0.0579 0.0477 0.0451 92 ARG B CA 1408 C C . ARG B 15 ? 0.3066 0.2805 0.1970 0.0711 0.0413 0.0519 92 ARG B C 1409 O O . ARG B 15 ? 0.3078 0.2859 0.1897 0.0901 0.0350 0.0745 92 ARG B O 1410 C CB . ARG B 15 ? 0.3493 0.2628 0.2577 0.0025 0.0530 0.0198 92 ARG B CB 1411 C CG . ARG B 15 ? 0.4027 0.3192 0.2942 -0.0469 0.0527 0.0406 92 ARG B CG 1412 C CD . ARG B 15 ? 0.4417 0.3586 0.3230 -0.0424 0.0220 0.0563 92 ARG B CD 1413 N NE . ARG B 15 ? 0.4913 0.3946 0.3492 -0.0124 0.0222 0.0759 92 ARG B NE 1414 C CZ . ARG B 15 ? 0.5213 0.3845 0.3605 0.0249 -0.0117 0.0783 92 ARG B CZ 1415 N NH1 . ARG B 15 ? 0.5332 0.3764 0.3788 0.0207 -0.0158 0.1247 92 ARG B NH1 1416 N NH2 . ARG B 15 ? 0.5012 0.3610 0.3492 0.0657 -0.0355 0.0367 92 ARG B NH2 1417 N N . SER B 16 ? 0.2918 0.2802 0.1956 0.0609 0.0405 0.0481 93 SER B N 1418 C CA . SER B 16 ? 0.3059 0.2584 0.2174 0.0248 0.0307 0.0180 93 SER B CA 1419 C C . SER B 16 ? 0.3160 0.2914 0.2296 0.0839 0.0427 0.0528 93 SER B C 1420 O O . SER B 16 ? 0.3549 0.3733 0.2415 0.1446 0.0375 0.0711 93 SER B O 1421 C CB . SER B 16 ? 0.2838 0.2836 0.2172 0.0313 0.0302 -0.0087 93 SER B CB 1422 O OG . SER B 16 ? 0.3178 0.4009 0.2070 0.0134 -0.0190 -0.0336 93 SER B OG 1423 N N . SER B 17 ? 0.2644 0.2379 0.2196 0.0730 0.0345 0.0519 94 SER B N 1424 C CA . SER B 17 ? 0.2700 0.2302 0.2264 0.0274 0.0237 0.0431 94 SER B CA 1425 C C . SER B 17 ? 0.2649 0.2551 0.2137 0.0353 0.0325 0.0136 94 SER B C 1426 O O . SER B 17 ? 0.2738 0.2584 0.2075 0.0411 0.0276 0.0031 94 SER B O 1427 C CB . SER B 17 ? 0.2695 0.2278 0.2504 0.0109 0.0194 0.0560 94 SER B CB 1428 O OG . SER B 17 ? 0.3094 0.2061 0.2697 0.1197 0.0065 0.0434 94 SER B OG 1429 N N . THR B 18 ? 0.2848 0.2896 0.2170 0.0840 0.0680 0.0144 95 THR B N 1430 C CA . THR B 18 ? 0.2825 0.3375 0.2096 0.0851 0.0508 0.0373 95 THR B CA 1431 C C . THR B 18 ? 0.3026 0.3021 0.1938 0.0718 0.0557 0.0448 95 THR B C 1432 O O . THR B 18 ? 0.3549 0.2408 0.1856 0.0321 0.0364 0.0375 95 THR B O 1433 C CB . THR B 18 ? 0.2898 0.4407 0.2284 0.1319 0.0400 0.0518 95 THR B CB 1434 O OG1 . THR B 18 ? 0.2950 0.4793 0.2504 0.1525 0.0497 0.0763 95 THR B OG1 1435 C CG2 . THR B 18 ? 0.3292 0.4535 0.2282 0.1351 0.0529 0.0279 95 THR B CG2 1436 N N . TYR B 19 ? 0.2520 0.2925 0.1958 0.1257 0.0679 0.0473 96 TYR B N 1437 C CA . TYR B 19 ? 0.2744 0.3137 0.1845 0.0787 0.0921 0.0146 96 TYR B CA 1438 C C . TYR B 19 ? 0.2774 0.2952 0.2097 0.0676 0.1089 0.0104 96 TYR B C 1439 O O . TYR B 19 ? 0.2900 0.3180 0.2336 0.0753 0.1278 0.0243 96 TYR B O 1440 C CB . TYR B 19 ? 0.2732 0.2984 0.1801 0.0497 0.0798 0.0171 96 TYR B CB 1441 C CG . TYR B 19 ? 0.2203 0.2639 0.1606 0.0548 0.0774 0.0031 96 TYR B CG 1442 C CD1 . TYR B 19 ? 0.2091 0.2530 0.1539 0.0750 0.0618 0.0034 96 TYR B CD1 1443 C CD2 . TYR B 19 ? 0.1614 0.1753 0.1395 0.0025 0.0662 0.0344 96 TYR B CD2 1444 C CE1 . TYR B 19 ? 0.2638 0.1986 0.1331 0.0305 0.0413 0.0146 96 TYR B CE1 1445 C CE2 . TYR B 19 ? 0.1789 0.1915 0.1431 0.0052 0.0438 0.0258 96 TYR B CE2 1446 C CZ . TYR B 19 ? 0.2389 0.1763 0.1432 0.0166 0.0450 0.0222 96 TYR B CZ 1447 O OH . TYR B 19 ? 0.2465 0.1521 0.1775 -0.0190 0.0657 0.0353 96 TYR B OH 1448 N N . GLU B 20 ? 0.2948 0.2809 0.1730 0.0840 0.0988 -0.0061 97 GLU B N 1449 C CA . GLU B 20 ? 0.3404 0.2900 0.1857 0.1417 0.0948 -0.0200 97 GLU B CA 1450 C C . GLU B 20 ? 0.2828 0.2648 0.1770 0.1280 0.0695 -0.0079 97 GLU B C 1451 O O . GLU B 20 ? 0.3000 0.2842 0.1612 0.1271 0.0464 -0.0081 97 GLU B O 1452 C CB . GLU B 20 ? 0.4206 0.2985 0.2117 0.1500 0.1033 -0.0900 97 GLU B CB 1453 C CG . GLU B 20 ? 0.4658 0.3646 0.2199 0.1468 0.1130 -0.0824 97 GLU B CG 1454 C CD . GLU B 20 ? 0.5025 0.4212 0.2251 0.1403 0.1219 -0.0760 97 GLU B CD 1455 O OE1 . GLU B 20 ? 0.5152 0.4408 0.2265 0.1372 0.1248 -0.0735 97 GLU B OE1 1456 O OE2 . GLU B 20 ? 0.5152 0.4407 0.2264 0.1372 0.1246 -0.0735 97 GLU B OE2 1457 N N . VAL B 21 ? 0.2726 0.2519 0.1755 0.0871 0.0812 -0.0228 98 VAL B N 1458 C CA . VAL B 21 ? 0.2597 0.2165 0.1691 0.0479 0.1130 -0.0252 98 VAL B CA 1459 C C . VAL B 21 ? 0.2761 0.2680 0.1666 0.0462 0.1049 -0.0041 98 VAL B C 1460 O O . VAL B 21 ? 0.2920 0.3294 0.1733 0.0570 0.1373 0.0189 98 VAL B O 1461 C CB . VAL B 21 ? 0.2389 0.2090 0.1642 -0.0075 0.1113 -0.0176 98 VAL B CB 1462 C CG1 . VAL B 21 ? 0.2446 0.2047 0.1617 0.0223 0.1032 0.0243 98 VAL B CG1 1463 C CG2 . VAL B 21 ? 0.2734 0.2391 0.1913 -0.0143 0.1228 -0.0224 98 VAL B CG2 1464 N N . ARG B 22 ? 0.2487 0.2242 0.1594 0.0229 0.0632 -0.0008 99 ARG B N 1465 C CA . ARG B 22 ? 0.3419 0.2763 0.1515 0.0237 0.0733 -0.0234 99 ARG B CA 1466 C C . ARG B 22 ? 0.2883 0.2601 0.1636 0.0051 0.0959 -0.0251 99 ARG B C 1467 O O . ARG B 22 ? 0.2773 0.2753 0.1718 -0.0195 0.0936 0.0049 99 ARG B O 1468 C CB . ARG B 22 ? 0.4578 0.2227 0.1256 0.0642 0.0968 -0.0472 99 ARG B CB 1469 C CG . ARG B 22 ? 0.5002 0.2849 0.1447 0.0773 0.1018 -0.0407 99 ARG B CG 1470 C CD . ARG B 22 ? 0.5261 0.3843 0.1661 0.0717 0.1054 -0.0362 99 ARG B CD 1471 N NE . ARG B 22 ? 0.5525 0.4697 0.1847 0.0633 0.1083 -0.0356 99 ARG B NE 1472 C CZ . ARG B 22 ? 0.5747 0.5371 0.1991 0.0547 0.1103 -0.0362 99 ARG B CZ 1473 N NH1 . ARG B 22 ? 0.5822 0.5602 0.2040 0.0518 0.1110 -0.0364 99 ARG B NH1 1474 N NH2 . ARG B 22 ? 0.5822 0.5602 0.2040 0.0517 0.1109 -0.0364 99 ARG B NH2 1475 N N . LEU B 23 ? 0.2833 0.2956 0.1700 -0.0081 0.1009 -0.0425 100 LEU B N 1476 C CA . LEU B 23 ? 0.2264 0.3194 0.1943 0.0087 0.0658 -0.0091 100 LEU B CA 1477 C C . LEU B 23 ? 0.2114 0.3064 0.1618 0.0103 0.0621 -0.0183 100 LEU B C 1478 O O . LEU B 23 ? 0.1892 0.2969 0.1515 -0.0146 0.0714 -0.0278 100 LEU B O 1479 C CB . LEU B 23 ? 0.2283 0.3196 0.2170 0.0176 0.0638 0.0124 100 LEU B CB 1480 C CG . LEU B 23 ? 0.2046 0.3809 0.2484 -0.0326 0.0740 0.0295 100 LEU B CG 1481 C CD1 . LEU B 23 ? 0.2668 0.4456 0.2832 -0.0169 0.0485 0.0196 100 LEU B CD1 1482 C CD2 . LEU B 23 ? 0.2081 0.3762 0.2492 -0.0257 0.0959 0.0180 100 LEU B CD2 1483 N N . THR B 24 ? 0.2518 0.3101 0.1588 -0.0278 0.0546 -0.0420 101 THR B N 1484 C CA . THR B 24 ? 0.3111 0.2573 0.1461 -0.0154 0.0733 -0.0173 101 THR B CA 1485 C C . THR B 24 ? 0.3237 0.2066 0.1271 0.0069 0.0836 0.0177 101 THR B C 1486 O O . THR B 24 ? 0.3449 0.1876 0.1446 0.0282 0.0642 0.0699 101 THR B O 1487 C CB . THR B 24 ? 0.3526 0.2951 0.1489 -0.0165 0.0988 -0.0089 101 THR B CB 1488 O OG1 . THR B 24 ? 0.3841 0.2879 0.1494 -0.0078 0.1222 -0.0373 101 THR B OG1 1489 C CG2 . THR B 24 ? 0.3889 0.3326 0.1561 0.0104 0.0896 0.0199 101 THR B CG2 1490 N N . GLN B 25 ? 0.3061 0.1509 0.1153 -0.0385 0.0740 0.0092 102 GLN B N 1491 C CA . GLN B 25 ? 0.2714 0.1509 0.1093 -0.0454 0.0750 0.0279 102 GLN B CA 1492 C C . GLN B 25 ? 0.2293 0.1358 0.1094 -0.0084 0.0691 0.0330 102 GLN B C 1493 O O . GLN B 25 ? 0.2333 0.1586 0.1176 0.0096 0.0370 -0.0105 102 GLN B O 1494 C CB . GLN B 25 ? 0.2670 0.1762 0.1039 -0.0182 0.0636 0.0344 102 GLN B CB 1495 C CG . GLN B 25 ? 0.2470 0.1723 0.1311 -0.0109 0.0538 0.0305 102 GLN B CG 1496 C CD . GLN B 25 ? 0.2321 0.1897 0.1518 0.0055 0.0598 0.0224 102 GLN B CD 1497 O OE1 . GLN B 25 ? 0.2503 0.2316 0.1738 0.0304 0.0935 -0.0057 102 GLN B OE1 1498 N NE2 . GLN B 25 ? 0.1790 0.2238 0.1535 -0.0144 0.0368 0.0550 102 GLN B NE2 1499 N N . THR B 26 ? 0.2254 0.1682 0.1067 -0.0072 0.0479 0.0161 103 THR B N 1500 C CA . THR B 26 ? 0.2048 0.1798 0.0908 0.0354 0.0693 -0.0010 103 THR B CA 1501 C C . THR B 26 ? 0.2033 0.1890 0.1027 0.0165 0.0556 -0.0132 103 THR B C 1502 O O . THR B 26 ? 0.1939 0.2013 0.1147 0.0130 0.0775 0.0026 103 THR B O 1503 C CB . THR B 26 ? 0.2105 0.1920 0.0927 -0.0245 0.0418 0.0178 103 THR B CB 1504 O OG1 . THR B 26 ? 0.2712 0.1846 0.1122 -0.0433 0.0466 0.0047 103 THR B OG1 1505 C CG2 . THR B 26 ? 0.1715 0.2237 0.0928 0.0091 0.0421 0.0630 103 THR B CG2 1506 N N . VAL B 27 ? 0.1705 0.1579 0.0783 -0.0168 0.0391 -0.0154 104 VAL B N 1507 C CA . VAL B 27 ? 0.1967 0.1694 0.0596 -0.0480 0.0287 -0.0016 104 VAL B CA 1508 C C . VAL B 27 ? 0.1691 0.1456 0.0652 -0.0053 0.0058 0.0067 104 VAL B C 1509 O O . VAL B 27 ? 0.2195 0.1228 0.0785 -0.0216 0.0148 0.0179 104 VAL B O 1510 C CB . VAL B 27 ? 0.2125 0.1264 0.0791 -0.0470 0.0407 -0.0137 104 VAL B CB 1511 C CG1 . VAL B 27 ? 0.1982 0.1576 0.0597 -0.0171 0.0312 0.0277 104 VAL B CG1 1512 C CG2 . VAL B 27 ? 0.2441 0.1507 0.1005 -0.0536 0.0574 -0.0163 104 VAL B CG2 1513 N N . ALA B 28 ? 0.1534 0.1684 0.1175 0.0081 0.0011 -0.0070 105 ALA B N 1514 C CA . ALA B 28 ? 0.1689 0.1790 0.1283 -0.0252 -0.0079 -0.0106 105 ALA B CA 1515 C C . ALA B 28 ? 0.1863 0.1508 0.1050 -0.0360 0.0353 -0.0269 105 ALA B C 1516 O O . ALA B 28 ? 0.2198 0.2032 0.1059 -0.0544 0.0300 -0.0138 105 ALA B O 1517 C CB . ALA B 28 ? 0.1860 0.2635 0.1301 -0.0362 -0.0316 0.0132 105 ALA B CB 1518 N N . HIS B 29 ? 0.1704 0.1195 0.0939 0.0109 0.0315 -0.0396 106 HIS B N 1519 C CA . HIS B 29 ? 0.1917 0.1326 0.0891 -0.0005 0.0403 -0.0168 106 HIS B CA 1520 C C . HIS B 29 ? 0.1524 0.1577 0.0990 -0.0323 0.0169 -0.0220 106 HIS B C 1521 O O . HIS B 29 ? 0.1904 0.1349 0.1053 -0.0053 0.0114 -0.0131 106 HIS B O 1522 C CB . HIS B 29 ? 0.2252 0.1334 0.0994 -0.0258 0.0602 -0.0476 106 HIS B CB 1523 C CG . HIS B 29 ? 0.2850 0.2062 0.1322 -0.0387 0.0511 -0.0591 106 HIS B CG 1524 N ND1 . HIS B 29 ? 0.2786 0.2817 0.1487 -0.0100 0.0413 -0.0815 106 HIS B ND1 1525 C CD2 . HIS B 29 ? 0.2867 0.2224 0.1666 -0.0221 0.0327 -0.0890 106 HIS B CD2 1526 C CE1 . HIS B 29 ? 0.3048 0.2896 0.1615 -0.0010 0.0320 -0.0710 106 HIS B CE1 1527 N NE2 . HIS B 29 ? 0.2925 0.2019 0.1667 -0.0451 0.0452 -0.0753 106 HIS B NE2 1528 N N . LEU B 30 ? 0.1304 0.2131 0.0916 -0.0251 0.0156 -0.0046 107 LEU B N 1529 C CA . LEU B 30 ? 0.1035 0.2128 0.0912 -0.0231 0.0104 0.0102 107 LEU B CA 1530 C C . LEU B 30 ? 0.1468 0.2359 0.1082 -0.0330 0.0115 -0.0145 107 LEU B C 1531 O O . LEU B 30 ? 0.1678 0.1960 0.0898 -0.0103 0.0256 -0.0017 107 LEU B O 1532 C CB . LEU B 30 ? 0.1164 0.2312 0.0987 -0.0162 0.0002 -0.0182 107 LEU B CB 1533 C CG . LEU B 30 ? 0.1519 0.1429 0.1067 0.0296 0.0060 -0.0155 107 LEU B CG 1534 C CD1 . LEU B 30 ? 0.1726 0.1504 0.1393 0.0830 -0.0143 0.0220 107 LEU B CD1 1535 C CD2 . LEU B 30 ? 0.1852 0.1581 0.0954 0.0269 0.0142 -0.0230 107 LEU B CD2 1536 N N . LYS B 31 ? 0.1608 0.2319 0.1191 0.0026 0.0318 -0.0403 108 LYS B N 1537 C CA . LYS B 31 ? 0.1717 0.1669 0.0993 -0.0021 0.0552 -0.0578 108 LYS B CA 1538 C C . LYS B 31 ? 0.1876 0.1568 0.0979 -0.0111 0.0506 -0.0493 108 LYS B C 1539 O O . LYS B 31 ? 0.1819 0.1719 0.0975 -0.0103 0.0447 -0.0169 108 LYS B O 1540 C CB . LYS B 31 ? 0.2320 0.1359 0.1091 0.0272 0.0601 -0.0435 108 LYS B CB 1541 C CG . LYS B 31 ? 0.2042 0.1356 0.1375 0.0237 0.1076 -0.0800 108 LYS B CG 1542 C CD . LYS B 31 ? 0.2157 0.1502 0.1650 -0.0071 0.1115 -0.0318 108 LYS B CD 1543 C CE . LYS B 31 ? 0.2324 0.1660 0.1514 0.0306 0.1389 -0.0342 108 LYS B CE 1544 N NZ . LYS B 31 ? 0.1516 0.1405 0.1363 0.0544 0.0776 -0.0312 108 LYS B NZ 1545 N N . GLN B 32 ? 0.2019 0.1578 0.1032 -0.0280 0.0636 -0.0391 109 GLN B N 1546 C CA . GLN B 32 ? 0.2225 0.1648 0.0993 -0.0412 -0.0043 -0.0245 109 GLN B CA 1547 C C . GLN B 32 ? 0.2193 0.1751 0.1029 -0.0110 0.0034 -0.0169 109 GLN B C 1548 O O . GLN B 32 ? 0.2429 0.1737 0.1102 -0.0058 0.0032 0.0117 109 GLN B O 1549 C CB . GLN B 32 ? 0.1773 0.1701 0.0966 0.0379 -0.0368 -0.0184 109 GLN B CB 1550 C CG . GLN B 32 ? 0.2135 0.1565 0.1320 0.0410 -0.0215 -0.0057 109 GLN B CG 1551 C CD . GLN B 32 ? 0.2180 0.1772 0.1602 -0.0341 0.0208 -0.0004 109 GLN B CD 1552 O OE1 . GLN B 32 ? 0.2100 0.2122 0.1526 -0.0204 0.0434 -0.0155 109 GLN B OE1 1553 N NE2 . GLN B 32 ? 0.2364 0.2151 0.1828 -0.0538 0.0535 0.0167 109 GLN B NE2 1554 N N . GLN B 33 ? 0.1817 0.1656 0.1038 0.0166 0.0061 -0.0002 110 GLN B N 1555 C CA . GLN B 33 ? 0.2007 0.1244 0.1032 0.0394 0.0284 0.0201 110 GLN B CA 1556 C C . GLN B 33 ? 0.2455 0.1873 0.0937 0.0284 0.0362 -0.0147 110 GLN B C 1557 O O . GLN B 33 ? 0.2826 0.2173 0.1089 0.0389 0.0270 -0.0337 110 GLN B O 1558 C CB . GLN B 33 ? 0.2032 0.1492 0.1184 -0.0083 0.0551 -0.0006 110 GLN B CB 1559 C CG . GLN B 33 ? 0.2170 0.2481 0.1505 -0.0258 0.0690 -0.0396 110 GLN B CG 1560 C CD . GLN B 33 ? 0.2732 0.3081 0.1939 0.0134 0.1012 -0.0376 110 GLN B CD 1561 O OE1 . GLN B 33 ? 0.3585 0.3516 0.2217 0.0384 0.0914 -0.0549 110 GLN B OE1 1562 N NE2 . GLN B 33 ? 0.2442 0.2925 0.1989 0.0421 0.0857 -0.0265 110 GLN B NE2 1563 N N . VAL B 34 ? 0.2229 0.1872 0.0675 0.0342 0.0641 -0.0273 111 VAL B N 1564 C CA . VAL B 34 ? 0.2390 0.1822 0.0617 0.0074 0.0324 -0.0155 111 VAL B CA 1565 C C . VAL B 34 ? 0.2138 0.2269 0.0719 -0.0173 0.0231 -0.0197 111 VAL B C 1566 O O . VAL B 34 ? 0.2091 0.2363 0.0584 -0.0206 0.0248 -0.0105 111 VAL B O 1567 C CB . VAL B 34 ? 0.2351 0.1514 0.0639 0.0023 0.0187 -0.0081 111 VAL B CB 1568 C CG1 . VAL B 34 ? 0.2555 0.1955 0.0707 0.0482 -0.0085 0.0403 111 VAL B CG1 1569 C CG2 . VAL B 34 ? 0.2194 0.1378 0.0964 0.0043 0.0216 -0.0047 111 VAL B CG2 1570 N N . SER B 35 ? 0.1825 0.2058 0.1126 -0.0207 0.0240 -0.0319 112 SER B N 1571 C CA . SER B 35 ? 0.2211 0.1871 0.1269 -0.0108 0.0410 -0.0246 112 SER B CA 1572 C C . SER B 35 ? 0.2408 0.1721 0.1226 -0.0215 0.0407 -0.0117 112 SER B C 1573 O O . SER B 35 ? 0.2300 0.1708 0.1575 -0.0238 0.0436 0.0025 112 SER B O 1574 C CB . SER B 35 ? 0.1817 0.2222 0.1439 -0.0136 0.0041 -0.0360 112 SER B CB 1575 O OG . SER B 35 ? 0.1602 0.2287 0.1692 -0.0066 0.0408 -0.0512 112 SER B OG 1576 N N . GLY B 36 ? 0.2462 0.1510 0.1137 0.0211 0.0533 -0.0361 113 GLY B N 1577 C CA . GLY B 36 ? 0.2527 0.0984 0.1154 0.0851 0.0410 -0.0140 113 GLY B CA 1578 C C . GLY B 36 ? 0.2557 0.1534 0.1216 0.0577 -0.0015 -0.0369 113 GLY B C 1579 O O . GLY B 36 ? 0.3316 0.1996 0.1152 0.0478 -0.0149 -0.0526 113 GLY B O 1580 N N . LEU B 37 ? 0.2466 0.1192 0.1292 0.0284 -0.0045 -0.0230 114 LEU B N 1581 C CA . LEU B 37 ? 0.2403 0.1443 0.1273 0.0187 -0.0244 0.0182 114 LEU B CA 1582 C C . LEU B 37 ? 0.2781 0.1903 0.1249 0.0031 -0.0090 0.0053 114 LEU B C 1583 O O . LEU B 37 ? 0.3497 0.1879 0.1189 0.0621 0.0135 0.0180 114 LEU B O 1584 C CB . LEU B 37 ? 0.2461 0.1958 0.1252 0.0270 -0.0449 0.0120 114 LEU B CB 1585 C CG . LEU B 37 ? 0.3174 0.2411 0.1548 0.0465 0.0030 0.0178 114 LEU B CG 1586 C CD1 . LEU B 37 ? 0.3314 0.2898 0.1917 0.0363 -0.0117 0.0007 114 LEU B CD1 1587 C CD2 . LEU B 37 ? 0.3439 0.2228 0.1435 0.0649 0.0122 0.0433 114 LEU B CD2 1588 N N . GLU B 38 ? 0.2736 0.1782 0.1180 0.0011 0.0222 -0.0108 115 GLU B N 1589 C CA . GLU B 38 ? 0.2944 0.1381 0.1317 0.0175 0.0617 0.0177 115 GLU B CA 1590 C C . GLU B 38 ? 0.3226 0.1730 0.1498 -0.0040 0.0546 0.0464 115 GLU B C 1591 O O . GLU B 38 ? 0.3251 0.2470 0.1675 -0.0483 0.0491 0.0508 115 GLU B O 1592 C CB . GLU B 38 ? 0.3066 0.1822 0.1315 -0.0158 0.0616 -0.0038 115 GLU B CB 1593 C CG . GLU B 38 ? 0.2874 0.2127 0.1421 0.0441 0.0354 0.0229 115 GLU B CG 1594 C CD . GLU B 38 ? 0.2829 0.2756 0.1564 0.0085 0.0421 0.0241 115 GLU B CD 1595 O OE1 . GLU B 38 ? 0.3066 0.2930 0.1498 0.0092 0.0191 0.0424 115 GLU B OE1 1596 O OE2 . GLU B 38 ? 0.2657 0.3283 0.1705 0.0390 0.0579 0.0256 115 GLU B OE2 1597 N N . GLY B 39 ? 0.2940 0.1597 0.1637 -0.0073 0.0729 0.0042 116 GLY B N 1598 C CA . GLY B 39 ? 0.2810 0.1759 0.1651 -0.0153 0.0636 0.0229 116 GLY B CA 1599 C C . GLY B 39 ? 0.2932 0.1755 0.1791 -0.0523 0.0903 0.0248 116 GLY B C 1600 O O . GLY B 39 ? 0.3210 0.2193 0.2346 -0.0521 0.1243 0.0143 116 GLY B O 1601 N N . VAL B 40 ? 0.2856 0.1610 0.1545 -0.0076 0.0531 -0.0081 117 VAL B N 1602 C CA . VAL B 40 ? 0.2148 0.2045 0.1360 0.0131 0.0247 -0.0020 117 VAL B CA 1603 C C . VAL B 40 ? 0.1838 0.2038 0.1289 -0.0332 -0.0113 0.0217 117 VAL B C 1604 O O . VAL B 40 ? 0.2275 0.1544 0.1350 -0.0032 0.0502 0.0252 117 VAL B O 1605 C CB . VAL B 40 ? 0.2146 0.1941 0.1325 0.0508 0.0106 -0.0325 117 VAL B CB 1606 C CG1 . VAL B 40 ? 0.2693 0.1727 0.1526 0.0266 0.0168 -0.0100 117 VAL B CG1 1607 C CG2 . VAL B 40 ? 0.2579 0.2158 0.1164 0.0398 0.0010 0.0230 117 VAL B CG2 1608 N N . GLN B 41 ? 0.1674 0.2067 0.1440 -0.0054 -0.0191 0.0183 118 GLN B N 1609 C CA . GLN B 41 ? 0.2009 0.2213 0.1914 -0.0596 0.0180 0.0421 118 GLN B CA 1610 C C . GLN B 41 ? 0.2045 0.2218 0.1730 -0.0373 0.0474 0.0414 118 GLN B C 1611 O O . GLN B 41 ? 0.1920 0.1922 0.1634 -0.0150 0.0563 0.0099 118 GLN B O 1612 C CB . GLN B 41 ? 0.2012 0.2132 0.2457 -0.1022 0.0054 0.0733 118 GLN B CB 1613 C CG . GLN B 41 ? 0.2683 0.3026 0.2841 -0.0923 0.0180 0.0879 118 GLN B CG 1614 C CD . GLN B 41 ? 0.3347 0.3575 0.2850 -0.0812 0.0306 0.0815 118 GLN B CD 1615 O OE1 . GLN B 41 ? 0.3579 0.3776 0.2855 -0.0764 0.0352 0.0792 118 GLN B OE1 1616 N NE2 . GLN B 41 ? 0.3579 0.3776 0.2855 -0.0764 0.0352 0.0792 118 GLN B NE2 1617 N N . ASP B 42 ? 0.1837 0.1973 0.1507 -0.0469 0.0434 0.0441 119 ASP B N 1618 C CA . ASP B 42 ? 0.2023 0.2279 0.1371 -0.0363 0.0584 0.0098 119 ASP B CA 1619 C C . ASP B 42 ? 0.2100 0.2339 0.1522 -0.0325 0.0337 -0.0058 119 ASP B C 1620 O O . ASP B 42 ? 0.2274 0.2218 0.1812 -0.0263 0.0374 -0.0373 119 ASP B O 1621 C CB . ASP B 42 ? 0.2053 0.2777 0.1292 -0.0402 0.0742 0.0186 119 ASP B CB 1622 C CG . ASP B 42 ? 0.2614 0.3372 0.1317 0.0610 0.0762 0.0170 119 ASP B CG 1623 O OD1 . ASP B 42 ? 0.2983 0.4264 0.1508 0.0974 0.0128 0.0044 119 ASP B OD1 1624 O OD2 . ASP B 42 ? 0.3392 0.3824 0.1500 0.0812 0.0394 0.0118 119 ASP B OD2 1625 N N . ASP B 43 ? 0.2045 0.2218 0.1327 -0.0208 0.0272 -0.0129 120 ASP B N 1626 C CA . ASP B 43 ? 0.1643 0.2743 0.1621 0.0112 0.0203 0.0058 120 ASP B CA 1627 C C . ASP B 43 ? 0.1679 0.2706 0.1584 0.0169 0.0772 -0.0111 120 ASP B C 1628 O O . ASP B 43 ? 0.1468 0.2445 0.1703 -0.0025 0.0577 -0.0703 120 ASP B O 1629 C CB . ASP B 43 ? 0.2069 0.3245 0.2406 0.0181 0.0316 0.0142 120 ASP B CB 1630 C CG . ASP B 43 ? 0.2134 0.3949 0.3076 0.0109 0.0142 -0.0206 120 ASP B CG 1631 O OD1 . ASP B 43 ? 0.2125 0.3656 0.3008 -0.0720 0.0319 -0.0256 120 ASP B OD1 1632 O OD2 . ASP B 43 ? 0.2565 0.4738 0.3603 0.0377 0.0309 -0.0485 120 ASP B OD2 1633 N N . LEU B 44 ? 0.1444 0.2379 0.1398 -0.0145 0.0751 -0.0113 121 LEU B N 1634 C CA . LEU B 44 ? 0.1509 0.1836 0.1298 -0.0818 0.0742 -0.0197 121 LEU B CA 1635 C C . LEU B 44 ? 0.2096 0.1996 0.1231 -0.0601 0.0733 -0.0341 121 LEU B C 1636 O O . LEU B 44 ? 0.2079 0.2095 0.1027 -0.0280 0.0794 -0.0152 121 LEU B O 1637 C CB . LEU B 44 ? 0.2055 0.1991 0.1524 -0.0916 0.0821 -0.0299 121 LEU B CB 1638 C CG . LEU B 44 ? 0.1813 0.2255 0.1781 -0.0696 0.0890 -0.0112 121 LEU B CG 1639 C CD1 . LEU B 44 ? 0.1967 0.2368 0.2035 -0.0788 0.0695 -0.0085 121 LEU B CD1 1640 C CD2 . LEU B 44 ? 0.2248 0.3425 0.1897 -0.0711 0.0945 -0.0047 121 LEU B CD2 1641 N N . PHE B 45 ? 0.1933 0.1645 0.1177 -0.0386 0.0656 -0.0407 122 PHE B N 1642 C CA . PHE B 45 ? 0.1686 0.1298 0.0938 -0.0172 0.0419 -0.0258 122 PHE B CA 1643 C C . PHE B 45 ? 0.1451 0.1750 0.0807 -0.0175 0.0567 -0.0102 122 PHE B C 1644 O O . PHE B 45 ? 0.1721 0.2090 0.0721 -0.0050 0.0334 -0.0319 122 PHE B O 1645 C CB . PHE B 45 ? 0.1882 0.1602 0.0915 0.0025 0.0263 -0.0228 122 PHE B CB 1646 C CG . PHE B 45 ? 0.1857 0.2022 0.0757 -0.0161 0.0180 -0.0079 122 PHE B CG 1647 C CD1 . PHE B 45 ? 0.1660 0.2169 0.0632 -0.0171 0.0389 0.0026 122 PHE B CD1 1648 C CD2 . PHE B 45 ? 0.1936 0.1663 0.0758 -0.0055 0.0233 -0.0314 122 PHE B CD2 1649 C CE1 . PHE B 45 ? 0.1187 0.1695 0.0581 -0.0168 -0.0019 -0.0255 122 PHE B CE1 1650 C CE2 . PHE B 45 ? 0.1298 0.1892 0.0555 0.0061 0.0139 -0.0202 122 PHE B CE2 1651 C CZ . PHE B 45 ? 0.1352 0.1791 0.0633 0.0103 0.0130 -0.0336 122 PHE B CZ 1652 N N . TRP B 46 ? 0.1697 0.1538 0.0958 0.0090 0.0712 0.0347 123 TRP B N 1653 C CA . TRP B 46 ? 0.1652 0.2062 0.1019 0.0150 0.0323 0.0273 123 TRP B CA 1654 C C . TRP B 46 ? 0.1599 0.2482 0.0964 0.0076 0.0399 0.0203 123 TRP B C 1655 O O . TRP B 46 ? 0.1640 0.2513 0.0803 -0.0149 0.0405 0.0148 123 TRP B O 1656 C CB . TRP B 46 ? 0.1819 0.1714 0.0890 0.0230 0.0107 -0.0303 123 TRP B CB 1657 C CG . TRP B 46 ? 0.1657 0.1742 0.0940 -0.0188 0.0163 -0.0100 123 TRP B CG 1658 C CD1 . TRP B 46 ? 0.2084 0.1747 0.0834 -0.0095 -0.0128 0.0114 123 TRP B CD1 1659 C CD2 . TRP B 46 ? 0.1662 0.1660 0.1206 -0.0101 0.0216 -0.0056 123 TRP B CD2 1660 N NE1 . TRP B 46 ? 0.1911 0.1796 0.0996 -0.0366 0.0126 0.0054 123 TRP B NE1 1661 C CE2 . TRP B 46 ? 0.1682 0.1654 0.1129 0.0186 -0.0106 0.0082 123 TRP B CE2 1662 C CE3 . TRP B 46 ? 0.1294 0.2002 0.1494 0.0095 0.0038 -0.0305 123 TRP B CE3 1663 C CZ2 . TRP B 46 ? 0.2003 0.1766 0.1459 -0.0265 0.0088 0.0094 123 TRP B CZ2 1664 C CZ3 . TRP B 46 ? 0.1493 0.2000 0.1529 -0.0120 -0.0036 -0.0473 123 TRP B CZ3 1665 C CH2 . TRP B 46 ? 0.1665 0.2124 0.1557 0.0001 0.0209 -0.0036 123 TRP B CH2 1666 N N . LEU B 47 ? 0.1374 0.2010 0.0947 -0.0028 0.0296 0.0082 124 LEU B N 1667 C CA . LEU B 47 ? 0.1311 0.1545 0.0968 -0.0013 0.0321 -0.0289 124 LEU B CA 1668 C C . LEU B 47 ? 0.1427 0.2026 0.0929 -0.0176 0.0179 -0.0324 124 LEU B C 1669 O O . LEU B 47 ? 0.1401 0.2386 0.0959 -0.0289 0.0192 -0.0249 124 LEU B O 1670 C CB . LEU B 47 ? 0.1558 0.1507 0.0705 0.0053 0.0463 -0.0172 124 LEU B CB 1671 C CG . LEU B 47 ? 0.1584 0.1653 0.0677 -0.0342 0.0337 -0.0038 124 LEU B CG 1672 C CD1 . LEU B 47 ? 0.1513 0.1968 0.0529 0.0034 0.0630 -0.0002 124 LEU B CD1 1673 C CD2 . LEU B 47 ? 0.1593 0.1981 0.0957 -0.0092 -0.0066 0.0097 124 LEU B CD2 1674 N N . THR B 48 ? 0.1415 0.2275 0.0880 -0.0348 0.0060 -0.0130 125 THR B N 1675 C CA . THR B 48 ? 0.1220 0.2096 0.1051 -0.0713 0.0292 -0.0155 125 THR B CA 1676 C C . THR B 48 ? 0.1278 0.2108 0.1268 -0.0223 0.0237 0.0050 125 THR B C 1677 O O . THR B 48 ? 0.1305 0.2682 0.1434 -0.0290 0.0370 -0.0048 125 THR B O 1678 C CB . THR B 48 ? 0.1290 0.2073 0.1188 -0.0289 0.0387 -0.0070 125 THR B CB 1679 O OG1 . THR B 48 ? 0.1782 0.2223 0.1483 -0.0192 0.0299 -0.0009 125 THR B OG1 1680 C CG2 . THR B 48 ? 0.1156 0.1843 0.1367 -0.0064 0.0239 -0.0020 125 THR B CG2 1681 N N . PHE B 49 ? 0.1247 0.1976 0.1240 -0.0225 0.0248 0.0430 126 PHE B N 1682 C CA . PHE B 49 ? 0.1216 0.2197 0.1311 -0.0141 0.0035 0.0263 126 PHE B CA 1683 C C . PHE B 49 ? 0.1189 0.2405 0.1456 -0.0154 -0.0063 0.0300 126 PHE B C 1684 O O . PHE B 49 ? 0.1323 0.2299 0.1618 -0.0390 -0.0041 0.0119 126 PHE B O 1685 C CB . PHE B 49 ? 0.1544 0.2196 0.1373 0.0073 0.0462 0.0130 126 PHE B CB 1686 C CG . PHE B 49 ? 0.1646 0.2483 0.1372 -0.0005 0.0234 0.0032 126 PHE B CG 1687 C CD1 . PHE B 49 ? 0.2080 0.2672 0.1352 -0.0111 0.0147 -0.0318 126 PHE B CD1 1688 C CD2 . PHE B 49 ? 0.1528 0.2676 0.1401 0.0009 0.0256 0.0319 126 PHE B CD2 1689 C CE1 . PHE B 49 ? 0.2364 0.2928 0.1409 -0.0109 0.0227 -0.0189 126 PHE B CE1 1690 C CE2 . PHE B 49 ? 0.1977 0.2741 0.1533 0.0569 0.0303 0.0208 126 PHE B CE2 1691 C CZ . PHE B 49 ? 0.1987 0.2687 0.1513 0.0492 0.0340 0.0187 126 PHE B CZ 1692 N N . GLU B 50 ? 0.1339 0.3162 0.1507 -0.0603 0.0028 0.0234 127 GLU B N 1693 C CA . GLU B 50 ? 0.2000 0.3673 0.1818 -0.0414 0.0184 -0.0299 127 GLU B CA 1694 C C . GLU B 50 ? 0.2024 0.3571 0.1721 -0.0447 0.0354 -0.0107 127 GLU B C 1695 O O . GLU B 50 ? 0.2620 0.4006 0.1892 -0.1015 0.0892 -0.0152 127 GLU B O 1696 C CB . GLU B 50 ? 0.2088 0.4024 0.2319 -0.0448 0.0319 -0.0991 127 GLU B CB 1697 C CG . GLU B 50 ? 0.2087 0.4363 0.2603 -0.0557 0.0329 -0.0975 127 GLU B CG 1698 C CD . GLU B 50 ? 0.2499 0.4991 0.2926 -0.0434 0.0402 -0.0894 127 GLU B CD 1699 O OE1 . GLU B 50 ? 0.2966 0.5473 0.3201 -0.1194 0.0967 -0.0916 127 GLU B OE1 1700 O OE2 . GLU B 50 ? 0.2582 0.5619 0.2972 -0.0565 0.0185 -0.0711 127 GLU B OE2 1701 N N . GLY B 51 ? 0.1703 0.3201 0.1625 -0.0370 0.0296 0.0374 128 GLY B N 1702 C CA . GLY B 51 ? 0.1780 0.2774 0.1838 -0.0080 0.0314 0.0306 128 GLY B CA 1703 C C . GLY B 51 ? 0.1990 0.2542 0.2254 -0.0234 0.0584 -0.0097 128 GLY B C 1704 O O . GLY B 51 ? 0.2340 0.2966 0.2669 -0.0286 0.0810 -0.0079 128 GLY B O 1705 N N . LYS B 52 ? 0.1720 0.2162 0.2215 -0.0300 0.0375 0.0008 129 LYS B N 1706 C CA . LYS B 52 ? 0.1948 0.2137 0.2468 -0.0376 0.0350 -0.0167 129 LYS B CA 1707 C C . LYS B 52 ? 0.1292 0.2050 0.2081 -0.0273 0.0036 -0.0164 129 LYS B C 1708 O O . LYS B 52 ? 0.1705 0.2088 0.2014 -0.0060 0.0318 0.0456 129 LYS B O 1709 C CB . LYS B 52 ? 0.2928 0.3316 0.3010 -0.0557 0.0447 0.0196 129 LYS B CB 1710 C CG . LYS B 52 ? 0.4336 0.4804 0.3523 -0.0121 0.0920 0.0558 129 LYS B CG 1711 C CD . LYS B 52 ? 0.5240 0.5722 0.3856 0.0030 0.1431 0.0616 129 LYS B CD 1712 C CE . LYS B 52 ? 0.5739 0.6205 0.4071 -0.0151 0.1645 0.0612 129 LYS B CE 1713 N NZ . LYS B 52 ? 0.5899 0.6291 0.4174 -0.0320 0.1731 0.0530 129 LYS B NZ 1714 N N . PRO B 53 ? 0.1321 0.2205 0.1757 -0.0241 0.0103 -0.0154 130 PRO B N 1715 C CA . PRO B 53 ? 0.1670 0.2356 0.1516 -0.0282 0.0239 -0.0212 130 PRO B CA 1716 C C . PRO B 53 ? 0.2334 0.2318 0.1344 -0.0108 0.0527 0.0048 130 PRO B C 1717 O O . PRO B 53 ? 0.2936 0.1790 0.1446 -0.0424 0.0401 0.0011 130 PRO B O 1718 C CB . PRO B 53 ? 0.1559 0.2599 0.1765 -0.0165 0.0135 -0.0396 130 PRO B CB 1719 C CG . PRO B 53 ? 0.1391 0.2217 0.1936 -0.0304 -0.0020 -0.0459 130 PRO B CG 1720 C CD . PRO B 53 ? 0.0969 0.2021 0.1823 -0.0023 -0.0291 -0.0186 130 PRO B CD 1721 N N . LEU B 54 ? 0.1848 0.2460 0.1092 0.0082 0.0728 -0.0014 131 LEU B N 1722 C CA . LEU B 54 ? 0.1523 0.2357 0.1210 0.0271 0.0481 0.0210 131 LEU B CA 1723 C C . LEU B 54 ? 0.1388 0.2384 0.1311 0.0037 0.0303 0.0202 131 LEU B C 1724 O O . LEU B 54 ? 0.1679 0.2533 0.1409 0.0089 0.0452 0.0336 131 LEU B O 1725 C CB . LEU B 54 ? 0.1337 0.1922 0.1340 0.0196 0.0295 0.0456 131 LEU B CB 1726 C CG . LEU B 54 ? 0.1651 0.2215 0.1693 0.0423 0.0446 0.0484 131 LEU B CG 1727 C CD1 . LEU B 54 ? 0.1660 0.2598 0.1816 0.0804 0.0466 0.0278 131 LEU B CD1 1728 C CD2 . LEU B 54 ? 0.1705 0.2716 0.1899 0.0017 0.0113 0.0646 131 LEU B CD2 1729 N N . GLU B 55 ? 0.1109 0.1939 0.1230 0.0122 0.0051 0.0226 132 GLU B N 1730 C CA . GLU B 55 ? 0.1387 0.1503 0.1415 0.0330 0.0148 -0.0192 132 GLU B CA 1731 C C . GLU B 55 ? 0.1304 0.1951 0.1453 0.0196 0.0202 -0.0208 132 GLU B C 1732 O O . GLU B 55 ? 0.1347 0.2066 0.1411 0.0181 0.0521 0.0004 132 GLU B O 1733 C CB . GLU B 55 ? 0.2639 0.1247 0.1632 -0.0550 0.0377 -0.0411 132 GLU B CB 1734 C CG . GLU B 55 ? 0.3709 0.1515 0.2164 -0.0899 0.0394 -0.0152 132 GLU B CG 1735 C CD . GLU B 55 ? 0.4794 0.2001 0.2770 -0.0249 0.0328 -0.0005 132 GLU B CD 1736 O OE1 . GLU B 55 ? 0.5087 0.1919 0.3031 0.0248 0.0165 0.0316 132 GLU B OE1 1737 O OE2 . GLU B 55 ? 0.5649 0.2814 0.2891 -0.0052 0.0464 0.0175 132 GLU B OE2 1738 N N . ASP B 56 ? 0.1591 0.2312 0.1625 0.0420 0.0052 -0.0066 133 ASP B N 1739 C CA . ASP B 56 ? 0.1438 0.2134 0.1576 0.0111 0.0191 0.0088 133 ASP B CA 1740 C C . ASP B 56 ? 0.1622 0.1878 0.1439 0.0451 0.0493 0.0466 133 ASP B C 1741 O O . ASP B 56 ? 0.1819 0.2003 0.1251 0.0228 0.0295 0.0283 133 ASP B O 1742 C CB . ASP B 56 ? 0.1404 0.2775 0.2006 -0.0165 0.0172 0.0320 133 ASP B CB 1743 C CG . ASP B 56 ? 0.2429 0.3810 0.2591 -0.0984 0.0360 0.0560 133 ASP B CG 1744 O OD1 . ASP B 56 ? 0.3280 0.4567 0.2735 -0.0494 0.0651 0.1136 133 ASP B OD1 1745 O OD2 . ASP B 56 ? 0.3532 0.3801 0.2966 -0.1521 0.0393 0.0720 133 ASP B OD2 1746 N N . GLN B 57 ? 0.1663 0.2088 0.1570 0.0588 0.0193 0.0380 134 GLN B N 1747 C CA . GLN B 57 ? 0.2140 0.2306 0.1629 0.0476 0.0162 0.0243 134 GLN B CA 1748 C C . GLN B 57 ? 0.2195 0.1991 0.1498 -0.0012 0.0330 0.0266 134 GLN B C 1749 O O . GLN B 57 ? 0.2234 0.2702 0.1474 -0.0089 0.0313 0.0593 134 GLN B O 1750 C CB . GLN B 57 ? 0.2704 0.2857 0.1661 0.0847 -0.0324 0.0397 134 GLN B CB 1751 C CG . GLN B 57 ? 0.3301 0.3653 0.2050 0.0733 0.0100 -0.0013 134 GLN B CG 1752 C CD . GLN B 57 ? 0.3580 0.3955 0.2112 0.0653 0.0145 0.0037 134 GLN B CD 1753 O OE1 . GLN B 57 ? 0.3686 0.4066 0.2137 0.0616 0.0172 0.0051 134 GLN B OE1 1754 N NE2 . GLN B 57 ? 0.3686 0.4064 0.2137 0.0617 0.0173 0.0052 134 GLN B NE2 1755 N N . LEU B 58 ? 0.1877 0.1504 0.1407 -0.0321 -0.0024 0.0263 135 LEU B N 1756 C CA . LEU B 58 ? 0.1920 0.1581 0.1237 -0.0692 0.0097 0.0120 135 LEU B CA 1757 C C . LEU B 58 ? 0.2255 0.1596 0.1209 -0.0427 0.0369 0.0234 135 LEU B C 1758 O O . LEU B 58 ? 0.2409 0.1858 0.1347 -0.0275 0.0407 0.0382 135 LEU B O 1759 C CB . LEU B 58 ? 0.2213 0.1146 0.1386 -0.0545 0.0349 -0.0031 135 LEU B CB 1760 C CG . LEU B 58 ? 0.2545 0.1370 0.1426 -0.0527 0.0348 0.0054 135 LEU B CG 1761 C CD1 . LEU B 58 ? 0.1873 0.1492 0.1574 -0.0328 0.0228 -0.0271 135 LEU B CD1 1762 C CD2 . LEU B 58 ? 0.3108 0.1620 0.1196 -0.0434 0.0368 -0.0135 135 LEU B CD2 1763 N N . PRO B 59 ? 0.2082 0.1667 0.1209 -0.0120 0.0474 0.0381 136 PRO B N 1764 C CA . PRO B 59 ? 0.1752 0.2232 0.1148 0.0261 0.0520 0.0520 136 PRO B CA 1765 C C . PRO B 59 ? 0.1906 0.1625 0.1069 -0.0081 0.0304 -0.0013 136 PRO B C 1766 O O . PRO B 59 ? 0.1935 0.1896 0.1237 0.0324 0.0352 -0.0060 136 PRO B O 1767 C CB . PRO B 59 ? 0.1807 0.2781 0.1005 0.0190 0.0262 0.1008 136 PRO B CB 1768 C CG . PRO B 59 ? 0.1827 0.2156 0.1148 0.0393 0.0390 0.0941 136 PRO B CG 1769 C CD . PRO B 59 ? 0.1636 0.1377 0.1175 0.0201 0.0580 0.0793 136 PRO B CD 1770 N N . LEU B 60 ? 0.1728 0.1890 0.1021 0.0021 0.0228 0.0381 137 LEU B N 1771 C CA . LEU B 60 ? 0.1696 0.1673 0.1178 -0.0130 0.0441 0.0349 137 LEU B CA 1772 C C . LEU B 60 ? 0.1900 0.2353 0.1245 -0.0305 0.0427 0.0100 137 LEU B C 1773 O O . LEU B 60 ? 0.2021 0.2218 0.1107 -0.0314 0.0464 0.0035 137 LEU B O 1774 C CB . LEU B 60 ? 0.2059 0.1276 0.1321 -0.0210 0.0627 -0.0017 137 LEU B CB 1775 C CG . LEU B 60 ? 0.1896 0.2127 0.1269 0.0239 0.0732 0.0008 137 LEU B CG 1776 C CD1 . LEU B 60 ? 0.2010 0.2076 0.1295 0.0505 0.0438 -0.0355 137 LEU B CD1 1777 C CD2 . LEU B 60 ? 0.1809 0.2892 0.1489 0.0298 0.1180 0.0258 137 LEU B CD2 1778 N N . GLY B 61 ? 0.1591 0.2522 0.1695 -0.0001 0.0602 0.0104 138 GLY B N 1779 C CA . GLY B 61 ? 0.1901 0.2614 0.1826 -0.0222 0.0635 -0.0159 138 GLY B CA 1780 C C . GLY B 61 ? 0.1808 0.2501 0.1798 -0.0464 0.0450 -0.0346 138 GLY B C 1781 O O . GLY B 61 ? 0.2369 0.2900 0.2144 -0.0583 0.0788 -0.0557 138 GLY B O 1782 N N . GLU B 62 ? 0.1617 0.1955 0.1497 -0.0016 0.0385 -0.0047 139 GLU B N 1783 C CA . GLU B 62 ? 0.1666 0.2371 0.1670 0.0078 0.0113 -0.0238 139 GLU B CA 1784 C C . GLU B 62 ? 0.2035 0.2117 0.1779 -0.0243 0.0110 -0.0276 139 GLU B C 1785 O O . GLU B 62 ? 0.2483 0.2543 0.2111 0.0077 0.0110 -0.0294 139 GLU B O 1786 C CB . GLU B 62 ? 0.1537 0.2423 0.1489 0.0061 0.0047 -0.0407 139 GLU B CB 1787 C CG . GLU B 62 ? 0.2541 0.2261 0.1312 0.0144 0.0092 -0.0322 139 GLU B CG 1788 C CD . GLU B 62 ? 0.3109 0.2681 0.1207 0.0347 0.0472 -0.0365 139 GLU B CD 1789 O OE1 . GLU B 62 ? 0.2829 0.2906 0.1268 -0.0083 0.0420 0.0030 139 GLU B OE1 1790 O OE2 . GLU B 62 ? 0.4509 0.3386 0.1371 0.0638 0.0854 -0.0055 139 GLU B OE2 1791 N N . TYR B 63 ? 0.1673 0.2231 0.1704 -0.0326 0.0301 0.0278 140 TYR B N 1792 C CA . TYR B 63 ? 0.1661 0.2520 0.1836 -0.0265 0.0115 0.0139 140 TYR B CA 1793 C C . TYR B 63 ? 0.1982 0.3078 0.2156 0.0068 0.0151 0.0036 140 TYR B C 1794 O O . TYR B 63 ? 0.2208 0.3795 0.2173 -0.0371 -0.0015 0.0181 140 TYR B O 1795 C CB . TYR B 63 ? 0.1391 0.2300 0.1538 -0.0084 0.0140 0.0517 140 TYR B CB 1796 C CG . TYR B 63 ? 0.1483 0.2543 0.1398 -0.0341 0.0088 0.0351 140 TYR B CG 1797 C CD1 . TYR B 63 ? 0.1711 0.2712 0.1326 -0.0280 0.0085 0.0364 140 TYR B CD1 1798 C CD2 . TYR B 63 ? 0.1761 0.2453 0.1147 -0.0012 -0.0130 0.0365 140 TYR B CD2 1799 C CE1 . TYR B 63 ? 0.1684 0.2214 0.1310 -0.0414 0.0205 0.0301 140 TYR B CE1 1800 C CE2 . TYR B 63 ? 0.1756 0.2389 0.1228 -0.0259 0.0468 0.0256 140 TYR B CE2 1801 C CZ . TYR B 63 ? 0.1642 0.2088 0.1437 -0.0172 0.0344 0.0413 140 TYR B CZ 1802 O OH . TYR B 63 ? 0.1832 0.2033 0.1653 -0.0129 0.0275 0.0662 140 TYR B OH 1803 N N . GLY B 64 ? 0.1713 0.3167 0.2453 0.0203 0.0271 0.0209 141 GLY B N 1804 C CA . GLY B 64 ? 0.1931 0.3134 0.2616 0.0567 -0.0127 0.0359 141 GLY B CA 1805 C C . GLY B 64 ? 0.2014 0.3577 0.2645 0.0324 -0.0151 0.0094 141 GLY B C 1806 O O . GLY B 64 ? 0.2178 0.4131 0.2960 0.0556 -0.0094 0.0049 141 GLY B O 1807 N N . LEU B 65 ? 0.1757 0.3377 0.2404 -0.0305 0.0215 0.0252 142 LEU B N 1808 C CA . LEU B 65 ? 0.1682 0.3242 0.2108 -0.0300 0.0206 0.0490 142 LEU B CA 1809 C C . LEU B 65 ? 0.1896 0.3420 0.2304 -0.0082 0.0718 0.0515 142 LEU B C 1810 O O . LEU B 65 ? 0.2227 0.4094 0.2490 0.0128 0.0865 0.0570 142 LEU B O 1811 C CB . LEU B 65 ? 0.1426 0.3514 0.1917 -0.0756 0.0036 0.0415 142 LEU B CB 1812 C CG . LEU B 65 ? 0.1674 0.4316 0.1941 -0.0377 0.0086 0.0064 142 LEU B CG 1813 C CD1 . LEU B 65 ? 0.2430 0.4779 0.1966 -0.0576 -0.0220 -0.0157 142 LEU B CD1 1814 C CD2 . LEU B 65 ? 0.1728 0.4765 0.1822 -0.0424 0.0466 -0.0184 142 LEU B CD2 1815 N N . LYS B 66 ? 0.1568 0.3284 0.2441 0.0359 0.0632 0.0317 143 LYS B N 1816 C CA . LYS B 66 ? 0.2123 0.3548 0.2719 0.0261 0.0663 0.0136 143 LYS B CA 1817 C C . LYS B 66 ? 0.2068 0.3702 0.2536 0.0459 0.1018 0.0330 143 LYS B C 1818 O O . LYS B 66 ? 0.2166 0.3661 0.2135 0.1006 0.0879 0.0418 143 LYS B O 1819 C CB . LYS B 66 ? 0.2717 0.4153 0.3188 -0.0053 0.0314 0.0172 143 LYS B CB 1820 C CG . LYS B 66 ? 0.3563 0.4738 0.3487 -0.0453 0.0315 -0.0081 143 LYS B CG 1821 C CD . LYS B 66 ? 0.4032 0.5254 0.3684 -0.0438 0.0578 -0.0017 143 LYS B CD 1822 C CE . LYS B 66 ? 0.4152 0.5427 0.3707 -0.0367 0.0594 0.0008 143 LYS B CE 1823 N NZ . LYS B 66 ? 0.4215 0.5515 0.3720 -0.0340 0.0603 0.0025 143 LYS B NZ 1824 N N . PRO B 67 ? 0.2370 0.4167 0.2727 0.0325 0.1322 0.0271 144 PRO B N 1825 C CA . PRO B 67 ? 0.2272 0.4416 0.2784 0.0634 0.1189 0.0464 144 PRO B CA 1826 C C . PRO B 67 ? 0.1940 0.4420 0.2875 0.0394 0.0848 0.0427 144 PRO B C 1827 O O . PRO B 67 ? 0.1630 0.4668 0.2903 0.0224 0.0780 0.0539 144 PRO B O 1828 C CB . PRO B 67 ? 0.2368 0.4687 0.2760 0.0540 0.1443 0.0488 144 PRO B CB 1829 C CG . PRO B 67 ? 0.2549 0.4350 0.2835 0.0479 0.1463 0.0334 144 PRO B CG 1830 C CD . PRO B 67 ? 0.2163 0.4225 0.2790 0.0493 0.1753 0.0306 144 PRO B CD 1831 N N . LEU B 68 ? 0.1947 0.4374 0.2980 0.0637 0.0412 0.0194 145 LEU B N 1832 C CA . LEU B 68 ? 0.1885 0.4007 0.3013 0.1223 0.0089 0.0503 145 LEU B CA 1833 C C . LEU B 68 ? 0.1852 0.3520 0.2737 0.0769 0.0032 0.0494 145 LEU B C 1834 O O . LEU B 68 ? 0.2150 0.3845 0.2923 0.0423 -0.0203 0.0261 145 LEU B O 1835 C CB . LEU B 68 ? 0.2110 0.4468 0.3402 0.1229 0.0199 0.0351 145 LEU B CB 1836 C CG . LEU B 68 ? 0.2612 0.5084 0.3733 0.1705 0.0316 0.0351 145 LEU B CG 1837 C CD1 . LEU B 68 ? 0.2761 0.5330 0.3842 0.2152 0.0681 0.0337 145 LEU B CD1 1838 C CD2 . LEU B 68 ? 0.3163 0.5283 0.3872 0.1641 0.0564 0.0227 145 LEU B CD2 1839 N N . SER B 69 ? 0.2053 0.3480 0.2613 0.0115 0.0649 0.0310 146 SER B N 1840 C CA . SER B 69 ? 0.1735 0.3365 0.2268 0.0522 0.0751 0.0461 146 SER B CA 1841 C C . SER B 69 ? 0.1766 0.3339 0.2024 0.0585 0.0467 0.0314 146 SER B C 1842 O O . SER B 69 ? 0.1686 0.3456 0.1824 0.0520 0.0281 0.0173 146 SER B O 1843 C CB . SER B 69 ? 0.1733 0.3367 0.2078 0.0387 0.0783 0.0442 146 SER B CB 1844 O OG . SER B 69 ? 0.2337 0.3591 0.2080 0.0443 0.0520 0.0427 146 SER B OG 1845 N N . THR B 70 ? 0.1601 0.3128 0.1879 0.0402 0.0296 0.0182 147 THR B N 1846 C CA . THR B 70 ? 0.1249 0.3194 0.1789 -0.0027 0.0160 0.0478 147 THR B CA 1847 C C . THR B 70 ? 0.1456 0.2828 0.1641 -0.0103 0.0079 0.0419 147 THR B C 1848 O O . THR B 70 ? 0.1724 0.2770 0.1833 -0.0057 0.0165 0.0438 147 THR B O 1849 C CB . THR B 70 ? 0.1479 0.3850 0.1941 0.0229 -0.0124 0.0584 147 THR B CB 1850 O OG1 . THR B 70 ? 0.1954 0.3446 0.2237 0.0198 -0.0504 0.0344 147 THR B OG1 1851 C CG2 . THR B 70 ? 0.1689 0.3915 0.2040 -0.0558 0.0103 0.0744 147 THR B CG2 1852 N N . VAL B 71 ? 0.0926 0.2983 0.1371 0.0197 -0.0103 0.0398 148 VAL B N 1853 C CA . VAL B 71 ? 0.0951 0.2703 0.1187 0.0435 -0.0063 0.0495 148 VAL B CA 1854 C C . VAL B 71 ? 0.1405 0.2565 0.1117 0.0368 0.0232 0.0305 148 VAL B C 1855 O O . VAL B 71 ? 0.1637 0.2816 0.1298 0.0403 0.0467 0.0246 148 VAL B O 1856 C CB . VAL B 71 ? 0.1193 0.2648 0.1238 0.0282 0.0086 0.0604 148 VAL B CB 1857 C CG1 . VAL B 71 ? 0.1481 0.2204 0.1173 0.0273 -0.0043 0.0392 148 VAL B CG1 1858 C CG2 . VAL B 71 ? 0.1269 0.2811 0.1398 0.0251 0.0207 0.0665 148 VAL B CG2 1859 N N . PHE B 72 ? 0.1083 0.2538 0.1073 0.0160 0.0368 0.0492 149 PHE B N 1860 C CA . PHE B 72 ? 0.1716 0.2481 0.0933 -0.0144 0.0204 0.0191 149 PHE B CA 1861 C C . PHE B 72 ? 0.2031 0.2272 0.1037 -0.0379 0.0245 0.0496 149 PHE B C 1862 O O . PHE B 72 ? 0.1970 0.2047 0.1122 -0.0129 0.0166 0.0382 149 PHE B O 1863 C CB . PHE B 72 ? 0.1784 0.2453 0.0917 -0.0013 0.0041 -0.0449 149 PHE B CB 1864 C CG . PHE B 72 ? 0.2282 0.2848 0.1019 0.0010 -0.0030 0.0125 149 PHE B CG 1865 C CD1 . PHE B 72 ? 0.2637 0.3243 0.1172 0.0035 -0.0268 0.0163 149 PHE B CD1 1866 C CD2 . PHE B 72 ? 0.2588 0.3411 0.1124 -0.0599 -0.0463 0.0103 149 PHE B CD2 1867 C CE1 . PHE B 72 ? 0.3476 0.3215 0.1099 0.0283 -0.0054 0.0188 149 PHE B CE1 1868 C CE2 . PHE B 72 ? 0.2814 0.3768 0.1235 -0.0143 -0.0345 0.0268 149 PHE B CE2 1869 C CZ . PHE B 72 ? 0.3352 0.3578 0.1298 0.0572 0.0190 0.0276 149 PHE B CZ 1870 N N . MET B 73 ? 0.2048 0.1907 0.1118 -0.0788 0.0057 0.0174 150 MET B N 1871 C CA . MET B 73 ? 0.1946 0.1644 0.0896 -0.0885 -0.0102 -0.0201 150 MET B CA 1872 C C . MET B 73 ? 0.2165 0.1850 0.0993 -0.0431 0.0299 0.0022 150 MET B C 1873 O O . MET B 73 ? 0.2828 0.2212 0.0961 0.0035 0.0362 0.0031 150 MET B O 1874 C CB . MET B 73 ? 0.1483 0.1483 0.0879 -0.0525 -0.0078 0.0022 150 MET B CB 1875 C CG . MET B 73 ? 0.2177 0.1526 0.0956 -0.0389 0.0141 -0.0083 150 MET B CG 1876 S SD . MET B 73 ? 0.2446 0.1846 0.1301 -0.0030 0.0251 0.0023 150 MET B SD 1877 C CE . MET B 73 ? 0.2322 0.1334 0.1742 -0.0576 0.0207 0.0013 150 MET B CE 1878 N N . ASN B 74 ? 0.1887 0.2008 0.0963 -0.0010 0.0607 0.0025 151 ASN B N 1879 C CA . ASN B 74 ? 0.1864 0.2032 0.0816 -0.0199 0.0603 -0.0004 151 ASN B CA 1880 C C . ASN B 74 ? 0.2015 0.1775 0.0964 -0.0149 0.0606 0.0283 151 ASN B C 1881 O O . ASN B 74 ? 0.2550 0.1723 0.0876 -0.0075 0.0304 0.0301 151 ASN B O 1882 C CB . ASN B 74 ? 0.1840 0.2217 0.0941 -0.0544 0.0531 -0.0114 151 ASN B CB 1883 C CG . ASN B 74 ? 0.2228 0.2449 0.0942 -0.1065 0.0309 -0.0272 151 ASN B CG 1884 O OD1 . ASN B 74 ? 0.2086 0.3317 0.1219 -0.0545 0.0296 0.0124 151 ASN B OD1 1885 N ND2 . ASN B 74 ? 0.2163 0.2526 0.0646 -0.1044 0.0200 -0.0206 151 ASN B ND2 1886 N N . LEU B 75 ? 0.1727 0.1999 0.1196 -0.0312 0.0570 -0.0237 152 LEU B N 1887 C CA . LEU B 75 ? 0.1922 0.2349 0.1256 -0.0229 0.0547 0.0072 152 LEU B CA 1888 C C . LEU B 75 ? 0.1776 0.2349 0.1208 -0.0283 0.0364 -0.0073 152 LEU B C 1889 O O . LEU B 75 ? 0.2411 0.2641 0.1281 -0.0373 0.0421 0.0094 152 LEU B O 1890 C CB . LEU B 75 ? 0.2658 0.1828 0.1144 0.0090 0.0303 0.0469 152 LEU B CB 1891 C CG . LEU B 75 ? 0.2888 0.2169 0.1180 0.0493 0.0542 0.0470 152 LEU B CG 1892 C CD1 . LEU B 75 ? 0.2843 0.1627 0.1577 0.0243 0.0567 0.0499 152 LEU B CD1 1893 C CD2 . LEU B 75 ? 0.3697 0.2315 0.1160 0.0878 0.0319 0.0438 152 LEU B CD2 1894 N N . ARG B 76 ? 0.1531 0.1744 0.1134 -0.0209 0.0388 0.0026 153 ARG B N 1895 C CA . ARG B 76 ? 0.1263 0.2102 0.0964 0.0041 0.0166 -0.0027 153 ARG B CA 1896 C C . ARG B 76 ? 0.1840 0.2100 0.1085 -0.0229 0.0405 -0.0272 153 ARG B C 1897 O O . ARG B 76 ? 0.2729 0.2444 0.1276 -0.0587 0.0846 -0.0543 153 ARG B O 1898 C CB . ARG B 76 ? 0.1305 0.2624 0.1076 0.0112 -0.0114 -0.0428 153 ARG B CB 1899 C CG . ARG B 76 ? 0.1218 0.2472 0.1274 0.0051 0.0178 -0.0313 153 ARG B CG 1900 C CD . ARG B 76 ? 0.1377 0.2650 0.1512 0.0119 0.0275 0.0100 153 ARG B CD 1901 N NE . ARG B 76 ? 0.1531 0.2527 0.1548 0.0059 0.0450 0.0127 153 ARG B NE 1902 C CZ . ARG B 76 ? 0.1658 0.2456 0.1493 0.0247 0.0331 0.0056 153 ARG B CZ 1903 N NH1 . ARG B 76 ? 0.1839 0.2252 0.1329 0.0148 0.0391 -0.0168 153 ARG B NH1 1904 N NH2 . ARG B 76 ? 0.1509 0.2528 0.1485 0.0178 0.0159 0.0427 153 ARG B NH2 1905 N N . LEU B 77 ? 0.1420 0.1964 0.1004 -0.0337 0.0494 -0.0075 154 LEU B N 1906 C CA . LEU B 77 ? 0.1011 0.1863 0.1141 -0.0112 0.0287 0.0114 154 LEU B CA 1907 C C . LEU B 77 ? 0.1440 0.2293 0.1336 -0.0377 0.0369 -0.0287 154 LEU B C 1908 O O . LEU B 77 ? 0.1244 0.1997 0.1601 -0.0378 0.0386 -0.0391 154 LEU B O 1909 C CB . LEU B 77 ? 0.1026 0.2050 0.1420 0.0311 0.0289 0.0269 154 LEU B CB 1910 C CG . LEU B 77 ? 0.1353 0.2370 0.1482 0.0257 0.0165 0.0167 154 LEU B CG 1911 C CD1 . LEU B 77 ? 0.1895 0.3028 0.1436 0.0293 -0.0046 0.0173 154 LEU B CD1 1912 C CD2 . LEU B 77 ? 0.1789 0.2009 0.1704 0.0262 0.0544 -0.0264 154 LEU B CD2 1913 N N . ARG B 78 ? 0.1036 0.2423 0.1209 -0.0064 0.0424 -0.0179 155 ARG B N 1914 C CA . ARG B 78 ? 0.1159 0.2725 0.0995 -0.0180 0.0183 -0.0062 155 ARG B CA 1915 C C . ARG B 78 ? 0.1137 0.2428 0.1108 0.0040 0.0300 -0.0035 155 ARG B C 1916 O O . ARG B 78 ? 0.1694 0.2249 0.1545 0.0240 0.0658 -0.0007 155 ARG B O 1917 C CB . ARG B 78 ? 0.1567 0.3385 0.1124 -0.0412 0.0151 0.0427 155 ARG B CB 1918 C CG . ARG B 78 ? 0.2328 0.3548 0.1358 -0.0879 0.0179 0.0437 155 ARG B CG 1919 C CD . ARG B 78 ? 0.2789 0.4236 0.1694 -0.0961 0.0235 -0.0003 155 ARG B CD 1920 N NE . ARG B 78 ? 0.3213 0.4910 0.1966 -0.0794 0.0417 -0.0104 155 ARG B NE 1921 C CZ . ARG B 78 ? 0.3626 0.5793 0.2458 -0.0413 0.0250 0.0009 155 ARG B CZ 1922 N NH1 . ARG B 78 ? 0.4159 0.5973 0.2690 -0.0818 0.0116 -0.0292 155 ARG B NH1 1923 N NH2 . ARG B 78 ? 0.3432 0.6382 0.2762 0.0145 -0.0096 0.0722 155 ARG B NH2 1924 N N . GLY B 79 ? 0.1356 0.2390 0.0855 -0.0762 0.0331 0.0108 156 GLY B N 1925 C CA . GLY B 79 ? 0.1195 0.2482 0.1036 -0.0535 0.0813 -0.0076 156 GLY B CA 1926 C C . GLY B 79 ? 0.0772 0.2711 0.1099 0.0204 0.0366 -0.0055 156 GLY B C 1927 O O . GLY B 79 ? 0.0745 0.2512 0.1241 0.0381 0.0208 0.0207 156 GLY B O 1928 ZN ZN . ZN C . ? 0.2011 0.3776 0.1724 -0.0296 0.0132 -0.0114 184 ZN A ZN 1929 ZN ZN . ZN D . ? 0.1165 0.3964 0.1456 -0.0494 -0.0209 0.0294 185 ZN A ZN 1930 ZN ZN . ZN E . ? 0.1110 0.3980 0.1924 -0.0284 0.0059 0.0653 186 ZN A ZN 1931 ZN ZN . ZN F . ? 0.3516 0.4732 0.4461 0.1313 0.0770 -0.0591 187 ZN A ZN 1932 ZN ZN . ZN G . ? 0.2437 0.3309 0.2176 -0.1149 0.0407 -0.0049 188 ZN A ZN 1933 ZN ZN . ZN H . ? 0.1562 0.3945 0.2559 -0.0197 -0.0232 0.0383 189 ZN A ZN 1934 ZN ZN . ZN I . ? 0.6812 0.7278 0.4268 -0.0162 0.2648 0.1602 190 ZN A ZN 1935 ZN ZN . ZN J . ? 0.1110 0.2960 0.1540 -0.0407 0.0079 0.0294 191 ZN A ZN 1936 ZN ZN . ZN K . ? 0.1727 0.4511 0.2622 -0.0513 0.0173 0.1379 192 ZN A ZN 1937 C C . ACY L . ? 0.1177 0.3492 0.1706 0.0089 0.0094 0.0814 193 ACY A C 1938 O O . ACY L . ? 0.0841 0.3710 0.1802 -0.0215 0.0057 0.0912 193 ACY A O 1939 O OXT . ACY L . ? 0.0716 0.2406 0.1606 0.0276 0.0491 0.0251 193 ACY A OXT 1940 C CH3 . ACY L . ? 0.1700 0.3838 0.1569 -0.0008 -0.0185 0.1504 193 ACY A CH3 1941 N N . NEH M . ? 0.1008 0.2362 0.1014 -0.0413 0.0392 -0.0328 157 NEH B N 1942 C CA . NEH M . ? 0.1104 0.2429 0.0939 -0.0312 0.0334 0.0157 157 NEH B CA 1943 C CB . NEH M . ? 0.1252 0.2494 0.0832 -0.0670 0.0022 0.0046 157 NEH B CB 1944 ZN ZN . ZN N . ? 0.4097 0.2675 0.3977 -0.1388 0.2657 -0.1474 1 ZN B ZN 1945 ZN ZN . ZN O . ? 0.3454 0.2421 0.1685 0.0164 0.0070 -0.0050 2 ZN B ZN 1946 ZN ZN . ZN P . ? 0.3185 0.3731 0.1871 -0.0273 0.0167 -0.0521 3 ZN B ZN 1947 C C . ACY Q . ? 0.2698 0.5281 0.2709 0.0575 0.0099 -0.0984 4 ACY B C 1948 O O . ACY Q . ? 0.2729 0.5595 0.2759 0.0466 0.0454 -0.1509 4 ACY B O 1949 O OXT . ACY Q . ? 0.1939 0.4868 0.2479 0.0881 -0.0387 -0.0773 4 ACY B OXT 1950 C CH3 . ACY Q . ? 0.3065 0.5277 0.2958 0.0326 0.0147 -0.0969 4 ACY B CH3 1951 O O . HOH R . ? 0.2667 0.5193 0.1453 0.1048 -0.0282 -0.0143 201 HOH A O 1952 O O . HOH R . ? 0.2397 0.2851 0.1164 0.0260 -0.0391 0.0260 202 HOH A O 1953 O O . HOH R . ? 0.1794 0.2451 0.0820 -0.0526 0.0118 0.0213 203 HOH A O 1954 O O . HOH R . ? 0.1271 0.2418 0.1363 -0.0668 -0.0022 -0.0228 204 HOH A O 1955 O O . HOH R . ? 0.1765 0.2122 0.0903 -0.0171 0.0251 -0.0128 205 HOH A O 1956 O O . HOH R . ? 0.2748 0.6590 0.1729 -0.1010 -0.1278 0.0170 206 HOH A O 1957 O O . HOH R . ? 0.2087 0.2906 0.2677 0.0694 -0.0351 -0.0338 207 HOH A O 1958 O O . HOH R . ? 0.1539 0.3586 0.0726 -0.0509 -0.0142 -0.0085 208 HOH A O 1959 O O . HOH R . ? 0.2138 0.2803 0.2045 -0.0191 0.0552 0.0444 209 HOH A O 1960 O O . HOH R . ? 0.3435 0.2633 0.1290 0.0023 0.0725 -0.0007 210 HOH A O 1961 O O . HOH R . ? 0.2049 0.2094 0.2507 -0.0011 -0.0633 0.0302 211 HOH A O 1962 O O . HOH R . ? 0.3616 0.3840 0.3968 0.0972 0.1343 0.1847 212 HOH A O 1963 O O . HOH R . ? 0.3669 0.4074 0.1690 -0.0452 0.0059 -0.0109 213 HOH A O 1964 O O . HOH R . ? 0.2104 0.4097 0.2268 0.1069 0.1163 0.0682 214 HOH A O 1965 O O . HOH R . ? 0.5083 0.2958 0.4750 0.0183 -0.3709 0.0073 215 HOH A O 1966 O O . HOH R . ? 0.2817 0.5587 0.2840 -0.0652 0.0643 0.0056 216 HOH A O 1967 O O . HOH R . ? 0.4452 0.4009 0.1452 0.1412 0.0834 0.0989 217 HOH A O 1968 O O . HOH R . ? 0.4687 0.2625 0.1689 0.0951 -0.0853 0.0020 218 HOH A O 1969 O O . HOH R . ? 0.2921 0.5045 0.1396 -0.1133 0.0632 -0.1122 219 HOH A O 1970 O O . HOH R . ? 0.2550 0.2569 0.2752 -0.0867 0.0251 0.0579 220 HOH A O 1971 O O . HOH R . ? 0.2486 0.4405 0.3717 -0.1154 -0.1465 0.1193 221 HOH A O 1972 O O . HOH R . ? 0.2822 0.2536 0.2779 0.0747 0.1062 0.0684 222 HOH A O 1973 O O . HOH R . ? 0.3097 0.3004 0.2837 0.0563 0.0242 0.0635 223 HOH A O 1974 O O . HOH R . ? 0.1921 0.5415 0.1152 0.0176 -0.0168 0.0897 224 HOH A O 1975 O O . HOH R . ? 0.3453 0.2913 0.1301 -0.0623 0.0169 -0.0245 225 HOH A O 1976 O O . HOH R . ? 0.3296 0.4385 0.1977 0.0370 -0.1109 0.0425 226 HOH A O 1977 O O . HOH R . ? 0.0957 0.5765 0.1438 0.0065 0.0186 0.0098 227 HOH A O 1978 O O . HOH R . ? 0.1755 0.5504 0.1427 0.0288 0.0235 0.0525 228 HOH A O 1979 O O . HOH R . ? 0.3279 0.3231 0.3038 -0.1226 0.0046 0.0384 229 HOH A O 1980 O O . HOH R . ? 0.3790 0.3970 0.1896 0.1588 0.1200 0.0822 230 HOH A O 1981 O O . HOH R . ? 0.5651 0.5484 0.5363 0.2251 -0.1155 0.1687 231 HOH A O 1982 O O . HOH R . ? 0.4619 0.5036 0.2388 0.2126 0.0319 0.1875 232 HOH A O 1983 O O . HOH R . ? 0.2917 0.4144 0.2078 -0.0591 -0.0151 0.0481 233 HOH A O 1984 O O . HOH R . ? 0.2950 0.4043 0.1836 -0.0510 -0.0279 0.0724 234 HOH A O 1985 O O . HOH R . ? 0.3351 0.3474 0.2786 -0.0638 0.0391 -0.0020 235 HOH A O 1986 O O . HOH R . ? 0.5433 0.4595 0.2064 0.0253 0.0412 -0.0048 236 HOH A O 1987 O O . HOH R . ? 0.1862 0.6295 0.3841 0.0472 -0.0330 0.0715 237 HOH A O 1988 O O . HOH R . ? 0.1223 0.4984 0.4635 0.0267 -0.0960 0.0858 238 HOH A O 1989 O O . HOH R . ? 0.5043 0.6805 0.1807 -0.0093 -0.0793 -0.0687 239 HOH A O 1990 O O . HOH R . ? 0.2177 0.3744 0.2243 -0.0090 0.0307 0.1127 240 HOH A O 1991 O O . HOH R . ? 0.2699 0.4507 0.3617 0.1481 -0.1422 -0.1674 241 HOH A O 1992 O O . HOH R . ? 0.3615 0.7153 0.4899 -0.0211 0.2221 -0.3049 242 HOH A O 1993 O O . HOH R . ? 0.3581 0.3732 0.2111 -0.0771 0.0694 -0.0203 243 HOH A O 1994 O O . HOH R . ? 0.5558 0.4692 0.5086 0.2301 0.2578 0.0246 244 HOH A O 1995 O O . HOH R . ? 0.2602 0.6680 0.3191 -0.1243 -0.0013 -0.0422 245 HOH A O 1996 O O . HOH R . ? 0.1535 0.6635 0.4956 0.0890 -0.0090 0.0436 246 HOH A O 1997 O O . HOH R . ? 0.4017 0.2248 0.2266 -0.1103 0.0192 -0.0126 247 HOH A O 1998 O O . HOH R . ? 0.3953 0.6436 0.3810 -0.1758 0.0601 0.1051 248 HOH A O 1999 O O . HOH R . ? 0.4678 0.5246 0.4252 0.1072 -0.1176 0.1460 249 HOH A O 2000 O O . HOH R . ? 0.4083 0.3689 0.3463 -0.0372 0.1047 0.0178 250 HOH A O 2001 O O . HOH R . ? 0.3894 0.3757 0.2050 0.0648 0.0041 0.0601 251 HOH A O 2002 O O . HOH R . ? 0.3600 0.5264 0.2125 0.1454 -0.0930 0.0866 252 HOH A O 2003 O O . HOH R . ? 0.3304 0.4276 0.4727 -0.0323 0.0749 -0.2028 253 HOH A O 2004 O O . HOH R . ? 0.0329 0.2900 0.1029 -0.0535 0.0049 0.0205 254 HOH A O 2005 O O . HOH R . ? 0.0681 0.3247 0.0853 -0.0122 0.0523 0.0518 255 HOH A O 2006 O O . HOH R . ? 0.1659 0.2166 0.0895 -0.0364 0.0175 0.0247 256 HOH A O 2007 O O . HOH R . ? 0.1959 0.5075 0.2198 -0.0696 -0.0263 -0.1528 257 HOH A O 2008 O O . HOH R . ? 0.5108 0.1722 0.2802 -0.0499 0.0717 0.0389 258 HOH A O 2009 O O . HOH R . ? 0.3100 0.1902 0.4589 -0.0516 0.0626 -0.0283 259 HOH A O 2010 O O . HOH R . ? 0.2432 0.2911 0.1421 -0.0569 -0.0458 0.0116 260 HOH A O 2011 O O . HOH R . ? 0.2970 0.4120 0.2434 0.0159 -0.0417 -0.0873 261 HOH A O 2012 O O . HOH R . ? 0.0139 0.5004 0.3110 -0.0176 0.0484 0.2000 262 HOH A O 2013 O O . HOH R . ? 0.3545 0.3853 0.2967 -0.0553 0.1403 0.0023 263 HOH A O 2014 O O . HOH R . ? 0.2159 0.4445 0.2078 -0.1408 -0.0716 0.0894 264 HOH A O 2015 O O . HOH R . ? 0.2854 0.2568 0.3080 -0.0665 0.0206 -0.0379 265 HOH A O 2016 O O . HOH R . ? 0.7220 0.3913 0.1157 -0.2495 0.0345 -0.0121 266 HOH A O 2017 O O . HOH R . ? 0.3524 0.2515 0.4863 -0.0260 -0.0731 -0.1798 267 HOH A O 2018 O O . HOH R . ? 0.0712 0.4854 0.1367 -0.1473 0.0196 0.1134 268 HOH A O 2019 O O . HOH R . ? 0.2746 0.2621 0.2482 -0.0447 -0.0538 -0.1222 269 HOH A O 2020 O O . HOH R . ? 0.5519 0.4878 0.6434 -0.2681 0.1213 0.0825 270 HOH A O 2021 O O . HOH R . ? 0.3583 0.4095 0.4877 0.1045 -0.1672 -0.0577 271 HOH A O 2022 O O . HOH R . ? 0.0747 0.5711 0.8482 0.0442 -0.0213 0.2610 272 HOH A O 2023 O O . HOH R . ? 0.2436 0.8320 0.2348 -0.0374 -0.0583 0.2563 273 HOH A O 2024 O O . HOH R . ? 0.4142 0.4199 0.2281 0.0516 -0.0427 0.0548 274 HOH A O 2025 O O . HOH R . ? 0.6244 0.3674 0.4493 0.0640 -0.0968 -0.0258 275 HOH A O 2026 O O . HOH R . ? 0.4967 0.4593 0.2991 0.1130 -0.2078 -0.1434 276 HOH A O 2027 O O . HOH R . ? 0.3805 0.4808 0.2491 0.1154 0.0119 0.0053 277 HOH A O 2028 O O . HOH R . ? 0.2354 0.4826 0.6552 0.0807 0.0434 0.1092 278 HOH A O 2029 O O . HOH R . ? 0.8228 0.3846 0.3214 0.0145 0.1849 -0.1285 279 HOH A O 2030 O O . HOH R . ? 0.7284 0.5077 0.4962 0.1232 0.2452 -0.1080 280 HOH A O 2031 O O . HOH R . ? 0.2174 0.3492 0.1410 0.0156 0.0441 0.0525 281 HOH A O 2032 O O . HOH R . ? 0.4526 0.5613 0.4057 -0.0096 -0.0448 0.2298 282 HOH A O 2033 O O . HOH R . ? 0.4801 0.4687 0.5488 -0.1617 -0.1064 -0.1995 283 HOH A O 2034 O O . HOH R . ? 0.4919 0.7179 0.4353 0.0044 0.1696 -0.1874 284 HOH A O 2035 O O . HOH R . ? 0.4730 0.4102 0.5435 0.0800 0.0425 -0.1415 285 HOH A O 2036 O O . HOH R . ? 0.5122 0.3317 0.4840 -0.1425 0.2572 -0.0996 286 HOH A O 2037 O O . HOH R . ? 0.5426 0.5144 0.6642 -0.1406 0.0123 -0.0976 287 HOH A O 2038 O O . HOH R . ? 0.5221 0.5703 0.5661 -0.1095 0.1934 0.1255 288 HOH A O 2039 O O . HOH R . ? 0.2016 0.4736 0.3618 -0.0405 0.1296 0.0792 289 HOH A O 2040 O O . HOH R . ? 0.3295 0.6403 0.2053 -0.3305 0.1469 -0.1752 290 HOH A O 2041 O O . HOH R . ? 0.5245 0.4105 0.2597 0.1269 -0.1441 0.0000 291 HOH A O 2042 O O . HOH R . ? 0.3439 0.5092 0.4273 -0.0923 -0.1738 0.1052 292 HOH A O 2043 O O . HOH R . ? 0.5527 0.6531 0.3344 0.0340 -0.0561 -0.1654 293 HOH A O 2044 O O . HOH R . ? 0.6688 0.3558 0.5301 -0.1746 -0.0384 0.1572 294 HOH A O 2045 O O . HOH R . ? 0.6364 0.5000 0.4159 -0.2303 0.0112 0.0061 295 HOH A O 2046 O O . HOH R . ? 0.7190 0.6451 0.2047 0.1061 -0.0087 -0.0436 296 HOH A O 2047 O O . HOH R . ? 0.1950 0.4288 0.4968 -0.1381 -0.0805 0.2179 297 HOH A O 2048 O O . HOH R . ? 0.3779 0.3706 0.5074 -0.0084 0.0743 -0.1188 298 HOH A O 2049 O O . HOH R . ? 0.4231 0.2295 0.3889 0.0694 0.1108 0.0114 299 HOH A O 2050 O O . HOH R . ? 0.4078 0.6762 0.4016 0.1040 -0.2304 -0.1597 300 HOH A O 2051 O O . HOH R . ? 0.2528 0.3544 0.4361 -0.1447 -0.0451 -0.0019 301 HOH A O 2052 O O . HOH R . ? 0.3624 0.5890 0.5048 0.0709 0.1535 -0.2287 302 HOH A O 2053 O O . HOH R . ? 0.6127 0.4915 0.4042 -0.0571 0.1174 -0.1325 303 HOH A O 2054 O O . HOH R . ? 0.2914 0.5400 0.6731 -0.1138 0.2456 -0.2597 304 HOH A O 2055 O O . HOH R . ? 0.2417 0.5132 0.2922 0.0858 -0.0062 0.0983 305 HOH A O 2056 O O . HOH R . ? 0.3420 0.2630 0.5472 0.0399 0.3848 0.1249 306 HOH A O 2057 O O . HOH R . ? 0.3895 0.3646 0.2160 0.0014 -0.0723 0.0146 307 HOH A O 2058 O O . HOH R . ? 0.4387 0.8527 0.3276 0.1572 -0.1062 -0.0229 308 HOH A O 2059 O O . HOH R . ? 0.2635 0.3922 0.4148 -0.0798 -0.0075 0.0880 309 HOH A O 2060 O O . HOH R . ? 0.6374 0.4596 0.2516 0.1417 0.0589 0.0508 310 HOH A O 2061 O O . HOH R . ? 0.6322 0.7563 0.6463 -0.1182 -0.1195 -0.0339 311 HOH A O 2062 O O . HOH R . ? 0.6270 0.5452 0.2253 0.0687 0.0204 -0.1025 312 HOH A O 2063 O O . HOH R . ? 0.3231 0.4829 0.2466 -0.0416 -0.0333 0.1748 313 HOH A O 2064 O O . HOH R . ? 0.4543 0.4056 0.5387 0.0713 0.2944 0.1268 314 HOH A O 2065 O O . HOH R . ? 0.5945 0.6797 0.4189 -0.0446 -0.0962 0.0876 315 HOH A O 2066 O O . HOH R . ? 0.6926 0.3889 0.7970 0.1043 -0.0324 -0.1677 316 HOH A O 2067 O O . HOH R . ? 0.6719 0.7112 0.3786 0.1342 0.3433 0.1733 317 HOH A O 2068 O O . HOH R . ? 0.0917 0.1804 0.0858 0.0249 -0.0239 0.0476 318 HOH A O 2069 O O . HOH R . ? 0.5464 0.6498 0.0999 0.3351 0.0627 -0.0760 319 HOH A O 2070 O O . HOH R . ? 0.4391 0.4101 0.5467 -0.1381 -0.0647 -0.0426 320 HOH A O 2071 O O . HOH R . ? 0.4434 0.5664 0.4089 -0.2803 -0.1100 0.0124 321 HOH A O 2072 O O . HOH R . ? 0.5980 0.6877 0.2243 0.0660 -0.0865 -0.1597 322 HOH A O 2073 O O . HOH R . ? 0.4993 0.6383 0.3948 -0.1300 0.1799 0.1984 323 HOH A O 2074 O O . HOH R . ? 0.3416 0.5866 0.5806 -0.1856 0.0541 0.0196 324 HOH A O 2075 O O . HOH R . ? 0.4387 0.4110 0.4218 -0.1222 0.1736 -0.0033 325 HOH A O 2076 O O . HOH R . ? 0.3828 0.6824 0.5652 0.0638 -0.1471 -0.1965 326 HOH A O 2077 O O . HOH R . ? 0.7221 0.7652 0.5221 -0.0470 0.1591 0.0740 327 HOH A O 2078 O O . HOH R . ? 0.7018 0.4569 0.5422 -0.0625 -0.2229 0.0952 328 HOH A O 2079 O O . HOH R . ? 0.9179 0.7979 0.7884 0.1348 0.0381 0.0729 329 HOH A O 2080 O O . HOH R . ? 0.5414 0.8850 0.7367 0.1943 -0.1598 0.1436 330 HOH A O 2081 O O . HOH R . ? 0.0985 0.7926 0.6796 0.0386 0.0091 -0.0594 331 HOH A O 2082 O O . HOH S . ? 0.2813 0.2196 0.0731 0.0065 0.0438 0.0172 201 HOH B O 2083 O O . HOH S . ? 0.2555 0.3081 0.1429 0.0034 0.0809 0.0169 202 HOH B O 2084 O O . HOH S . ? 0.3200 0.3061 0.1762 -0.1023 0.0675 -0.0170 203 HOH B O 2085 O O . HOH S . ? 0.3866 0.3331 0.0856 -0.0607 -0.0067 0.0361 204 HOH B O 2086 O O . HOH S . ? 0.3387 0.2717 0.1390 -0.0804 0.0213 -0.0664 205 HOH B O 2087 O O . HOH S . ? 0.1974 0.4693 0.3604 0.0001 0.0354 0.0808 206 HOH B O 2088 O O . HOH S . ? 0.3353 0.3668 0.1779 -0.0767 0.1476 -0.0723 207 HOH B O 2089 O O . HOH S . ? 0.2485 0.3623 0.1713 -0.0304 0.0198 0.0040 208 HOH B O 2090 O O . HOH S . ? 0.4060 0.4722 0.3367 -0.0593 -0.1800 0.1404 209 HOH B O 2091 O O . HOH S . ? 0.3326 0.3113 0.3073 0.1271 0.0421 0.0446 210 HOH B O 2092 O O . HOH S . ? 0.2836 0.2728 0.2700 -0.0149 0.0986 -0.0842 211 HOH B O 2093 O O . HOH S . ? 0.3110 0.4112 0.1495 -0.0056 0.0412 0.0671 212 HOH B O 2094 O O . HOH S . ? 0.3393 0.3996 0.3215 -0.0231 0.0511 -0.1558 213 HOH B O 2095 O O . HOH S . ? 0.3049 0.2672 0.4279 0.0383 0.2238 0.0944 214 HOH B O 2096 O O . HOH S . ? 0.3242 0.2444 0.3439 -0.0213 0.0798 0.0185 215 HOH B O 2097 O O . HOH S . ? 0.2797 0.4182 0.2714 0.1679 0.0366 0.0258 216 HOH B O 2098 O O . HOH S . ? 0.5056 0.6609 0.3273 0.0459 0.1590 0.1804 217 HOH B O 2099 O O . HOH S . ? 0.7060 0.5003 0.3585 -0.0519 0.0269 0.2147 218 HOH B O 2100 O O . HOH S . ? 0.2768 0.5263 0.5186 0.0689 0.2065 0.1203 219 HOH B O 2101 O O . HOH S . ? 0.6962 0.4238 0.2650 -0.2665 -0.1520 0.1749 220 HOH B O 2102 O O . HOH S . ? 0.3958 0.5181 0.6505 -0.0117 0.1848 -0.1129 221 HOH B O 2103 O O . HOH S . ? 0.3232 0.2132 0.1859 -0.0549 0.1053 -0.0234 222 HOH B O 2104 O O . HOH S . ? 0.3651 0.5140 0.1590 0.0074 -0.0109 0.0608 223 HOH B O 2105 O O . HOH S . ? 0.1306 0.2964 0.1338 -0.0236 0.0356 0.0105 224 HOH B O 2106 O O . HOH S . ? 0.5001 0.2834 0.3291 0.0112 -0.0323 0.0402 225 HOH B O 2107 O O . HOH S . ? 0.2971 0.5306 0.3430 -0.1726 -0.1148 -0.0502 226 HOH B O 2108 O O . HOH S . ? 0.2488 0.5257 0.9063 -0.2062 0.0205 -0.0379 227 HOH B O 2109 O O . HOH S . ? 0.3516 0.4585 0.4395 -0.1198 -0.0626 0.1224 228 HOH B O 2110 O O . HOH S . ? 0.8417 0.5073 0.4452 0.1624 -0.0627 0.1418 229 HOH B O 2111 O O . HOH S . ? 0.3820 0.6332 0.3927 -0.1379 -0.0882 0.1760 230 HOH B O 2112 O O . HOH S . ? 0.6941 0.5130 0.2167 -0.0732 0.0730 -0.0445 231 HOH B O 2113 O O . HOH S . ? 0.2438 0.2064 0.2652 0.0261 0.0858 0.0517 232 HOH B O 2114 O O . HOH S . ? 0.4975 0.2903 0.4933 -0.1347 0.1783 -0.0009 233 HOH B O 2115 O O . HOH S . ? 0.4734 0.6971 0.3892 0.2400 -0.0466 0.2096 234 HOH B O 2116 O O . HOH S . ? 0.6207 0.5778 0.0828 0.3314 0.0345 0.1370 235 HOH B O 2117 O O . HOH S . ? 0.2032 0.3600 0.3725 0.0507 -0.0424 -0.0942 236 HOH B O 2118 O O . HOH S . ? 0.2785 0.5024 0.2201 -0.0199 0.1363 -0.0165 237 HOH B O 2119 O O . HOH S . ? 0.2063 0.4405 0.5773 0.0649 -0.0883 -0.1689 238 HOH B O 2120 O O . HOH S . ? 0.5454 0.6295 0.6666 0.0083 0.0558 0.3396 239 HOH B O 2121 O O . HOH S . ? 0.2573 0.2246 0.3336 0.0182 0.1187 -0.0676 240 HOH B O 2122 O O . HOH S . ? 0.5404 0.2763 0.1465 -0.0463 0.0383 -0.0391 241 HOH B O 2123 O O . HOH S . ? 0.6638 0.5457 0.4973 0.2666 0.0501 0.1045 242 HOH B O 2124 O O . HOH S . ? 0.3580 0.8433 0.2202 -0.1623 -0.1265 0.1818 243 HOH B O 2125 O O . HOH S . ? 0.6410 0.3046 0.1833 -0.0932 0.1865 0.0774 244 HOH B O 2126 O O . HOH S . ? 0.5219 0.7199 0.3682 0.1249 -0.2038 -0.0141 245 HOH B O 2127 O O . HOH S . ? 0.4914 0.4466 0.5694 -0.2551 0.1465 -0.0509 246 HOH B O 2128 O O . HOH S . ? 0.4259 0.7442 0.3975 -0.2569 -0.2082 -0.0190 247 HOH B O 2129 O O . HOH S . ? 0.5362 0.4964 0.5550 0.0787 0.1527 0.1338 248 HOH B O 2130 O O . HOH S . ? 0.7119 0.1837 0.4463 0.1168 0.1627 0.1206 249 HOH B O 2131 O O . HOH S . ? 0.7211 0.2149 0.4027 0.0810 0.0764 0.1273 250 HOH B O 2132 O O . HOH S . ? 0.3358 0.5261 0.3422 0.0547 0.0903 0.1249 251 HOH B O 2133 O O . HOH S . ? 0.3856 0.8575 0.2656 -0.0660 -0.1331 0.0992 252 HOH B O 2134 O O . HOH S . ? 0.6851 0.5371 0.6048 0.2297 0.0760 -0.0465 253 HOH B O 2135 O O . HOH S . ? 0.5631 0.3535 0.4230 0.0317 -0.0537 0.0403 254 HOH B O 2136 O O . HOH S . ? 0.5289 0.4286 0.4627 0.1874 0.1117 0.1087 255 HOH B O 2137 O O . HOH S . ? 0.7697 0.2410 0.2147 -0.1560 0.0962 -0.0604 256 HOH B O 2138 O O . HOH S . ? 0.6358 0.5993 0.2789 -0.0191 0.2287 -0.0642 257 HOH B O 2139 O O . HOH S . ? 0.3928 0.2967 0.4032 0.0561 -0.0592 -0.0617 258 HOH B O 2140 O O . HOH S . ? 0.2405 0.6338 0.1617 0.0486 -0.0451 -0.2310 259 HOH B O 2141 O O . HOH S . ? 0.6573 0.2184 0.3063 0.0578 -0.0101 -0.0605 260 HOH B O 2142 O O . HOH S . ? 0.7047 0.3872 0.6695 -0.1818 -0.0446 -0.1851 261 HOH B O #