data_18493 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18493 _Entry.Title ; High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-05-30 _Entry.Accession_date 2012-05-30 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLID-STATE _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Ming Tang . . . 18493 2 Lindsay Sperling . J. . 18493 3 Charles Schwieters . D. . 18493 4 Anna Nesbitt . E. . 18493 5 Robert Gennis . B. . 18493 6 Chad Rienstra . M. . 18493 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18493 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'DsbB C41S' . 18493 Fab . 18493 'Joint calculations' . 18493 'Solid-state NMR' . 18493 'X-ray reflections' . 18493 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18493 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 552 18493 '15N chemical shifts' 125 18493 '1H chemical shifts' 67 18493 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2014-02-24 2012-05-30 update BMRB 'update entry citation' 18493 1 . . 2013-02-27 2012-05-30 original author 'original release' 18493 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LEG 'Similar refinement method' 18493 PDB 2ZUQ 'The source of X-ray data' 18493 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18493 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23416557 _Citation.Full_citation . _Citation.Title 'Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 425 _Citation.Journal_issue 10 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1670 _Citation.Page_last 1682 _Citation.Year 2013 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ming Tang . . . 18493 1 2 Anna Nesbitt . E. . 18493 1 3 Lindsay Sperling . J. . 18493 1 4 Deborah Berthold . A. . 18493 1 5 Charles Schwieters . D. . 18493 1 6 Robert Gennis . B. . 18493 1 7 Chad Rienstra . M. . 18493 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18493 _Assembly.ID 1 _Assembly.Name 'DsbB C41S' _Assembly.BMRB_code . _Assembly.Number_of_components 8 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 DsbB_1 1 $DsbB A . yes native no no . . . 18493 1 2 entity_2_1 2 $entity_2 B . no native no no . . . 18493 1 3 entity_3_1 3 $entity_3 C . no native no no . . . 18493 1 4 DsbB_2 1 $DsbB D . no native no no . . . 18493 1 5 entity_2_2 2 $entity_2 E . no native no no . . . 18493 1 6 entity_3_2 3 $entity_3 F . no native no no . . . 18493 1 7 UBIQUINONE-1_1 4 $entity_UQ1 G . yes native no no . . . 18493 1 8 UBIQUINONE-1_2 4 $entity_UQ1 H . no native no no . . . 18493 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 104 104 SG . 1 . 1 CYS 130 130 SG . . . . . . . . . . 18493 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DsbB _Entity.Sf_category entity _Entity.Sf_framecode DsbB _Entity.Entry_ID 18493 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name DsbB _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A,D _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP SVLCIYERVALFGVLGAALI GAIAPKTPLRYVAMVIWLYS AFRGVQLTYEHTMLQLYPSP FATCDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGL EMPQWLLGIFIAYLIVAVLV VISQPFKAKKRDLFGR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 176 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'disulfide bound and free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation C8A,C41S,C49V _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 16663.053 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 yes PDB 2ZUQ . DsbB . . . . . . . . . . . . . . 18493 1 2 no BMRB 15546 . DsbB . . . . . 100.00 186 100.00 100.00 1.62e-122 . . . . 18493 1 3 no BMRB 15966 . Disulfide_bond_formation_protein_B . . . . . 100.00 183 97.73 97.73 1.60e-118 . . . . 18493 1 4 no BMRB 18395 . DsbB . . . . . 100.00 176 99.43 99.43 1.74e-121 . . . . 18493 1 5 no PDB 2HI7 . "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" . . . . . 100.00 176 98.86 98.86 3.64e-120 . . . . 18493 1 6 no PDB 2K73 . "Solution Nmr Structure Of Integral Membrane Protein Dsbb" . . . . . 100.00 183 97.73 97.73 1.60e-118 . . . . 18493 1 7 no PDB 2K74 . "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" . . . . . 100.00 183 97.73 97.73 1.60e-118 . . . . 18493 1 8 no PDB 2LEG . "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" . . . . . 100.00 176 98.86 98.86 3.64e-120 . . . . 18493 1 9 no PDB 2LTQ . "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" . . . . . 100.00 176 100.00 100.00 2.26e-122 . . . . 18493 1 10 no PDB 2ZUP . "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" . . . . . 100.00 176 98.86 98.86 3.64e-120 . . . . 18493 1 11 no PDB 2ZUQ . "Crystal Structure Of Dsbb-Fab Complex" . . . . . 100.00 176 100.00 100.00 2.26e-122 . . . . 18493 1 12 no PDB 3E9J . "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" . . . . . 100.00 182 99.43 99.43 1.50e-121 . . . . 18493 1 13 no DBJ BAA36032 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 14 no DBJ BAB35103 . "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 15 no DBJ BAG76757 . "disulfide bond formation protein [Escherichia coli SE11]" . . . . . 100.00 176 97.16 97.73 1.14e-118 . . . . 18493 1 16 no DBJ BAI24997 . "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 176 97.73 98.30 9.11e-120 . . . . 18493 1 17 no DBJ BAI30121 . "oxidoreductase DsbB [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 18 no EMBL CAP75720 . "Disulfide bond formation protein B [Escherichia coli LF82]" . . . . . 100.00 176 97.16 97.73 6.45e-119 . . . . 18493 1 19 no EMBL CAQ31687 . "DsbB[reduced] [Escherichia coli BL21(DE3)]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 20 no EMBL CAQ98064 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 21 no EMBL CAR02574 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" . . . . . 100.00 176 97.16 97.73 6.45e-119 . . . . 18493 1 22 no EMBL CAR12682 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli UMN026]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 23 no GB AAA23711 . "oxido-reductase [Escherichia coli]" . . . . . 100.00 178 98.30 98.30 3.03e-120 . . . . 18493 1 24 no GB AAB25233 . "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 25 no GB AAC74269 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 26 no GB AAG56036 . "reoxidizes DsbA protein following formation of disulfide bond in P-ring of flagella [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 176 97.73 97.73 2.69e-119 . . . . 18493 1 27 no GB AAN42789 . "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" . . . . . 100.00 176 97.73 98.30 9.11e-120 . . . . 18493 1 28 no PIR H85696 . "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 176 97.73 97.73 2.69e-119 . . . . 18493 1 29 no REF NP_309707 . "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 30 no REF NP_415703 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 31 no REF NP_707082 . "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" . . . . . 100.00 176 97.73 98.30 9.11e-120 . . . . 18493 1 32 no REF WP_000652474 . "disulfide bond formation protein B, partial [Escherichia coli]" . . . . . 69.32 122 100.00 100.00 1.26e-81 . . . . 18493 1 33 no REF WP_000943442 . "disulfide bond formation protein B [Escherichia coli]" . . . . . 100.00 176 97.73 98.30 1.09e-119 . . . . 18493 1 34 no SP A1AAA8 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" . . . . . 100.00 176 97.16 97.73 6.45e-119 . . . . 18493 1 35 no SP P0A6M2 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 36 no SP P0A6M3 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" . . . . . 100.00 176 98.30 98.30 4.43e-120 . . . . 18493 1 37 no SP P59343 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" . . . . . 100.00 176 97.16 97.73 6.45e-119 . . . . 18493 1 38 no SP Q0T5L6 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" . . . . . 100.00 176 97.73 98.30 9.11e-120 . . . . 18493 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 18493 1 2 . LEU . 18493 1 3 . ARG . 18493 1 4 . PHE . 18493 1 5 . LEU . 18493 1 6 . ASN . 18493 1 7 . GLN . 18493 1 8 . ALA . 18493 1 9 . SER . 18493 1 10 . GLN . 18493 1 11 . GLY . 18493 1 12 . ARG . 18493 1 13 . GLY . 18493 1 14 . ALA . 18493 1 15 . TRP . 18493 1 16 . LEU . 18493 1 17 . LEU . 18493 1 18 . MET . 18493 1 19 . ALA . 18493 1 20 . PHE . 18493 1 21 . THR . 18493 1 22 . ALA . 18493 1 23 . LEU . 18493 1 24 . ALA . 18493 1 25 . LEU . 18493 1 26 . GLU . 18493 1 27 . LEU . 18493 1 28 . THR . 18493 1 29 . ALA . 18493 1 30 . LEU . 18493 1 31 . TRP . 18493 1 32 . PHE . 18493 1 33 . GLN . 18493 1 34 . HIS . 18493 1 35 . VAL . 18493 1 36 . MET . 18493 1 37 . LEU . 18493 1 38 . LEU . 18493 1 39 . LYS . 18493 1 40 . PRO . 18493 1 41 . SER . 18493 1 42 . VAL . 18493 1 43 . LEU . 18493 1 44 . CYS . 18493 1 45 . ILE . 18493 1 46 . TYR . 18493 1 47 . GLU . 18493 1 48 . ARG . 18493 1 49 . VAL . 18493 1 50 . ALA . 18493 1 51 . LEU . 18493 1 52 . PHE . 18493 1 53 . GLY . 18493 1 54 . VAL . 18493 1 55 . LEU . 18493 1 56 . GLY . 18493 1 57 . ALA . 18493 1 58 . ALA . 18493 1 59 . LEU . 18493 1 60 . ILE . 18493 1 61 . GLY . 18493 1 62 . ALA . 18493 1 63 . ILE . 18493 1 64 . ALA . 18493 1 65 . PRO . 18493 1 66 . LYS . 18493 1 67 . THR . 18493 1 68 . PRO . 18493 1 69 . LEU . 18493 1 70 . ARG . 18493 1 71 . TYR . 18493 1 72 . VAL . 18493 1 73 . ALA . 18493 1 74 . MET . 18493 1 75 . VAL . 18493 1 76 . ILE . 18493 1 77 . TRP . 18493 1 78 . LEU . 18493 1 79 . TYR . 18493 1 80 . SER . 18493 1 81 . ALA . 18493 1 82 . PHE . 18493 1 83 . ARG . 18493 1 84 . GLY . 18493 1 85 . VAL . 18493 1 86 . GLN . 18493 1 87 . LEU . 18493 1 88 . THR . 18493 1 89 . TYR . 18493 1 90 . GLU . 18493 1 91 . HIS . 18493 1 92 . THR . 18493 1 93 . MET . 18493 1 94 . LEU . 18493 1 95 . GLN . 18493 1 96 . LEU . 18493 1 97 . TYR . 18493 1 98 . PRO . 18493 1 99 . SER . 18493 1 100 . PRO . 18493 1 101 . PHE . 18493 1 102 . ALA . 18493 1 103 . THR . 18493 1 104 . CYS . 18493 1 105 . ASP . 18493 1 106 . PHE . 18493 1 107 . MET . 18493 1 108 . VAL . 18493 1 109 . ARG . 18493 1 110 . PHE . 18493 1 111 . PRO . 18493 1 112 . GLU . 18493 1 113 . TRP . 18493 1 114 . LEU . 18493 1 115 . PRO . 18493 1 116 . LEU . 18493 1 117 . ASP . 18493 1 118 . LYS . 18493 1 119 . TRP . 18493 1 120 . VAL . 18493 1 121 . PRO . 18493 1 122 . GLN . 18493 1 123 . VAL . 18493 1 124 . PHE . 18493 1 125 . VAL . 18493 1 126 . ALA . 18493 1 127 . SER . 18493 1 128 . GLY . 18493 1 129 . ASP . 18493 1 130 . CYS . 18493 1 131 . ALA . 18493 1 132 . GLU . 18493 1 133 . ARG . 18493 1 134 . GLN . 18493 1 135 . TRP . 18493 1 136 . ASP . 18493 1 137 . PHE . 18493 1 138 . LEU . 18493 1 139 . GLY . 18493 1 140 . LEU . 18493 1 141 . GLU . 18493 1 142 . MET . 18493 1 143 . PRO . 18493 1 144 . GLN . 18493 1 145 . TRP . 18493 1 146 . LEU . 18493 1 147 . LEU . 18493 1 148 . GLY . 18493 1 149 . ILE . 18493 1 150 . PHE . 18493 1 151 . ILE . 18493 1 152 . ALA . 18493 1 153 . TYR . 18493 1 154 . LEU . 18493 1 155 . ILE . 18493 1 156 . VAL . 18493 1 157 . ALA . 18493 1 158 . VAL . 18493 1 159 . LEU . 18493 1 160 . VAL . 18493 1 161 . VAL . 18493 1 162 . ILE . 18493 1 163 . SER . 18493 1 164 . GLN . 18493 1 165 . PRO . 18493 1 166 . PHE . 18493 1 167 . LYS . 18493 1 168 . ALA . 18493 1 169 . LYS . 18493 1 170 . LYS . 18493 1 171 . ARG . 18493 1 172 . ASP . 18493 1 173 . LEU . 18493 1 174 . PHE . 18493 1 175 . GLY . 18493 1 176 . ARG . 18493 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 18493 1 . LEU 2 2 18493 1 . ARG 3 3 18493 1 . PHE 4 4 18493 1 . LEU 5 5 18493 1 . ASN 6 6 18493 1 . GLN 7 7 18493 1 . ALA 8 8 18493 1 . SER 9 9 18493 1 . GLN 10 10 18493 1 . GLY 11 11 18493 1 . ARG 12 12 18493 1 . GLY 13 13 18493 1 . ALA 14 14 18493 1 . TRP 15 15 18493 1 . LEU 16 16 18493 1 . LEU 17 17 18493 1 . MET 18 18 18493 1 . ALA 19 19 18493 1 . PHE 20 20 18493 1 . THR 21 21 18493 1 . ALA 22 22 18493 1 . LEU 23 23 18493 1 . ALA 24 24 18493 1 . LEU 25 25 18493 1 . GLU 26 26 18493 1 . LEU 27 27 18493 1 . THR 28 28 18493 1 . ALA 29 29 18493 1 . LEU 30 30 18493 1 . TRP 31 31 18493 1 . PHE 32 32 18493 1 . GLN 33 33 18493 1 . HIS 34 34 18493 1 . VAL 35 35 18493 1 . MET 36 36 18493 1 . LEU 37 37 18493 1 . LEU 38 38 18493 1 . LYS 39 39 18493 1 . PRO 40 40 18493 1 . SER 41 41 18493 1 . VAL 42 42 18493 1 . LEU 43 43 18493 1 . CYS 44 44 18493 1 . ILE 45 45 18493 1 . TYR 46 46 18493 1 . GLU 47 47 18493 1 . ARG 48 48 18493 1 . VAL 49 49 18493 1 . ALA 50 50 18493 1 . LEU 51 51 18493 1 . PHE 52 52 18493 1 . GLY 53 53 18493 1 . VAL 54 54 18493 1 . LEU 55 55 18493 1 . GLY 56 56 18493 1 . ALA 57 57 18493 1 . ALA 58 58 18493 1 . LEU 59 59 18493 1 . ILE 60 60 18493 1 . GLY 61 61 18493 1 . ALA 62 62 18493 1 . ILE 63 63 18493 1 . ALA 64 64 18493 1 . PRO 65 65 18493 1 . LYS 66 66 18493 1 . THR 67 67 18493 1 . PRO 68 68 18493 1 . LEU 69 69 18493 1 . ARG 70 70 18493 1 . TYR 71 71 18493 1 . VAL 72 72 18493 1 . ALA 73 73 18493 1 . MET 74 74 18493 1 . VAL 75 75 18493 1 . ILE 76 76 18493 1 . TRP 77 77 18493 1 . LEU 78 78 18493 1 . TYR 79 79 18493 1 . SER 80 80 18493 1 . ALA 81 81 18493 1 . PHE 82 82 18493 1 . ARG 83 83 18493 1 . GLY 84 84 18493 1 . VAL 85 85 18493 1 . GLN 86 86 18493 1 . LEU 87 87 18493 1 . THR 88 88 18493 1 . TYR 89 89 18493 1 . GLU 90 90 18493 1 . HIS 91 91 18493 1 . THR 92 92 18493 1 . MET 93 93 18493 1 . LEU 94 94 18493 1 . GLN 95 95 18493 1 . LEU 96 96 18493 1 . TYR 97 97 18493 1 . PRO 98 98 18493 1 . SER 99 99 18493 1 . PRO 100 100 18493 1 . PHE 101 101 18493 1 . ALA 102 102 18493 1 . THR 103 103 18493 1 . CYS 104 104 18493 1 . ASP 105 105 18493 1 . PHE 106 106 18493 1 . MET 107 107 18493 1 . VAL 108 108 18493 1 . ARG 109 109 18493 1 . PHE 110 110 18493 1 . PRO 111 111 18493 1 . GLU 112 112 18493 1 . TRP 113 113 18493 1 . LEU 114 114 18493 1 . PRO 115 115 18493 1 . LEU 116 116 18493 1 . ASP 117 117 18493 1 . LYS 118 118 18493 1 . TRP 119 119 18493 1 . VAL 120 120 18493 1 . PRO 121 121 18493 1 . GLN 122 122 18493 1 . VAL 123 123 18493 1 . PHE 124 124 18493 1 . VAL 125 125 18493 1 . ALA 126 126 18493 1 . SER 127 127 18493 1 . GLY 128 128 18493 1 . ASP 129 129 18493 1 . CYS 130 130 18493 1 . ALA 131 131 18493 1 . GLU 132 132 18493 1 . ARG 133 133 18493 1 . GLN 134 134 18493 1 . TRP 135 135 18493 1 . ASP 136 136 18493 1 . PHE 137 137 18493 1 . LEU 138 138 18493 1 . GLY 139 139 18493 1 . LEU 140 140 18493 1 . GLU 141 141 18493 1 . MET 142 142 18493 1 . PRO 143 143 18493 1 . GLN 144 144 18493 1 . TRP 145 145 18493 1 . LEU 146 146 18493 1 . LEU 147 147 18493 1 . GLY 148 148 18493 1 . ILE 149 149 18493 1 . PHE 150 150 18493 1 . ILE 151 151 18493 1 . ALA 152 152 18493 1 . TYR 153 153 18493 1 . LEU 154 154 18493 1 . ILE 155 155 18493 1 . VAL 156 156 18493 1 . ALA 157 157 18493 1 . VAL 158 158 18493 1 . LEU 159 159 18493 1 . VAL 160 160 18493 1 . VAL 161 161 18493 1 . ILE 162 162 18493 1 . SER 163 163 18493 1 . GLN 164 164 18493 1 . PRO 165 165 18493 1 . PHE 166 166 18493 1 . LYS 167 167 18493 1 . ALA 168 168 18493 1 . LYS 169 169 18493 1 . LYS 170 170 18493 1 . ARG 171 171 18493 1 . ASP 172 172 18493 1 . LEU 173 173 18493 1 . PHE 174 174 18493 1 . GLY 175 175 18493 1 . ARG 176 176 18493 1 stop_ save_ save_entity_2 _Entity.Sf_category entity _Entity.Sf_framecode entity_2 _Entity.Entry_ID 18493 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name entity_2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B,E _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MDSQAQVLILLLLWVSGTCG DIVMSQSPSSLAVSAGEKVT MSCKSSQSLLNSRTRKNYLA WYQQKPGQSPKLLIYWASTR ESGVPDRFTGSGSGTDFTLT ISSVQAEDLAVYYCKQSYNL YTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCF LNNFYPKDINVKWKIDGSER QNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCE ATHKTSTSPIVKSFNRNEC ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 239 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'Fab fragment light chain' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 24077.834 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1Q9K . "S25-2 Fab Unliganded 1" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 2 no PDB 1Q9L . "S25-2 Fab Unliganded 2" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 3 no PDB 1Q9O . "S45-18 Fab Unliganded" . . . . . 91.63 219 97.72 98.63 6.68e-155 . . . . 18493 2 4 no PDB 1Q9W . "S45-18 Fab Pentasaccharide Bisphosphate Complex" . . . . . 91.63 219 97.72 98.63 6.68e-155 . . . . 18493 2 5 no PDB 2I9L . "Structure Of Fab 7d11 From A Neutralizing Antibody Against The Poxvirus L1 Protein" . . . . . 91.63 219 97.26 99.09 5.49e-155 . . . . 18493 2 6 no PDB 2LTQ . "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" . . . . . 100.00 239 100.00 100.00 4.28e-175 . . . . 18493 2 7 no PDB 2R1W . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 8 no PDB 2R1X . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 9 no PDB 2R1Y . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 10 no PDB 2R23 . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 11 no PDB 2R2B . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 12 no PDB 2R2E . "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 13 no PDB 2R2H . "Structure Of S25-2 In Complex With Ko" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 14 no PDB 2ZUQ . "Crystal Structure Of Dsbb-Fab Complex" . . . . . 100.00 239 100.00 100.00 4.28e-175 . . . . 18493 2 15 no PDB 3BPC . "Co-Crystal Structure Of S25-2 Fab In Complex With 5-Deoxy-4- Epi-2,3-Dehydro Kdo (4.8) Kdo" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 16 no PDB 3HZK . "Crystal Structure Of S73-2 Antibody In Complex With Antigen Kdo(2.4)kdo" . . . . . 91.63 219 97.26 98.17 9.80e-155 . . . . 18493 2 17 no PDB 3HZM . "Crystal Structure Of S73-2 Antibody In Complex With Antigen Kdo" . . . . . 91.63 219 97.26 98.17 9.80e-155 . . . . 18493 2 18 no PDB 3HZV . "Crystal Structure Of S73-2 Antibody In Complex With Antigen Kdo(2.8) Kdo(2.4)kdo" . . . . . 91.63 219 97.26 98.17 9.80e-155 . . . . 18493 2 19 no PDB 3HZY . "Crystal Structure Of S73-2 Antibody In Complex With Antigen Kdo(2.4)kdo(2.4)kdo" . . . . . 91.63 219 98.17 99.09 2.86e-156 . . . . 18493 2 20 no PDB 3I02 . "Crystal Structure Of S54-10 Antibody In Complex With Antigen Kdo(2.4)kdo(2.4)kdo" . . . . . 91.63 219 98.17 99.09 4.24e-156 . . . . 18493 2 21 no PDB 3IJH . "Structure Of S67-27 In Complex With Ko" . . . . . 91.63 219 98.63 99.09 2.20e-156 . . . . 18493 2 22 no PDB 3IJS . "Structure Of S67-27 In Complex With Tsbp" . . . . . 91.63 219 98.63 99.09 2.20e-156 . . . . 18493 2 23 no PDB 3IJY . "Structure Of S67-27 In Complex With Kdo(2.8)kdo" . . . . . 91.63 218 98.17 98.63 9.92e-154 . . . . 18493 2 24 no PDB 3IKC . "Structure Of S67-27 In Complex With Kdo(2.8)-7-O-Methyl-Kdo" . . . . . 91.21 218 98.62 99.08 2.28e-155 . . . . 18493 2 25 no PDB 3KJ4 . "Structure Of Rat Nogo Receptor Bound To 1d9 Antagonist Antibody" . . . . . 91.63 219 97.72 98.17 6.05e-155 . . . . 18493 2 26 no PDB 3SY0 . "S25-2- A(2-8)-A(2-4)kdo Trisaccharide Complex" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 27 no PDB 3T4Y . "S25-2- Kdo Monosaccharide Complex" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 28 no PDB 3T65 . "S25-2- A(2-8)kdo Disaccharide Complex" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 29 no PDB 3T77 . "S25-2- A(2-4)kdo Disaccharide Complex" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 30 no PDB 4HGW . "Crystal Structure Of S25-2 In Complex With A 5,6-dehydro-kdo Disaccharide" . . . . . 91.63 219 99.09 99.54 8.93e-158 . . . . 18493 2 31 no EMBL CAA75918 . "variable region of immunoglobulin kappa light chain [Mus musculus]" . . . . . 50.21 120 100.00 100.00 9.68e-79 . . . . 18493 2 32 no GB AAA53292 . "immunoglobulin kappa chain, partial [Mus musculus domesticus]" . . . . . 61.92 148 97.97 98.65 2.87e-98 . . . . 18493 2 33 no GB AAB47613 . "polyreactive autoantibody, immunoglobulin light chain kappa, partial [Mus musculus]" . . . . . 56.49 135 100.00 100.00 5.93e-91 . . . . 18493 2 34 no GB AAL04472 . "anti-InlB monoclonal antibody IgG1 light chain [Mus musculus]" . . . . . 83.68 200 97.50 99.00 4.01e-140 . . . . 18493 2 35 no GB AEB66102 . "anti-prion immunoglobulin kappa light chain variable region [Mus musculus]" . . . . . 50.21 120 97.50 100.00 8.25e-78 . . . . 18493 2 36 no GB EDK98900 . "mCG142167 [Mus musculus]" . . . . . 51.05 122 99.18 99.18 7.21e-79 . . . . 18493 2 37 no PIR G33932 . "Ig kappa chain precursor V region (D23) - mouse" . . . . . 50.21 120 99.17 99.17 6.35e-78 . . . . 18493 2 38 no PIR PS0023 . "Ig kappa chain precursor V region (6A4) - mouse" . . . . . 55.65 133 97.74 98.50 1.67e-86 . . . . 18493 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 18493 2 2 . ASP . 18493 2 3 . SER . 18493 2 4 . GLN . 18493 2 5 . ALA . 18493 2 6 . GLN . 18493 2 7 . VAL . 18493 2 8 . LEU . 18493 2 9 . ILE . 18493 2 10 . LEU . 18493 2 11 . LEU . 18493 2 12 . LEU . 18493 2 13 . LEU . 18493 2 14 . TRP . 18493 2 15 . VAL . 18493 2 16 . SER . 18493 2 17 . GLY . 18493 2 18 . THR . 18493 2 19 . CYS . 18493 2 20 . GLY . 18493 2 21 . ASP . 18493 2 22 . ILE . 18493 2 23 . VAL . 18493 2 24 . MET . 18493 2 25 . SER . 18493 2 26 . GLN . 18493 2 27 . SER . 18493 2 28 . PRO . 18493 2 29 . SER . 18493 2 30 . SER . 18493 2 31 . LEU . 18493 2 32 . ALA . 18493 2 33 . VAL . 18493 2 34 . SER . 18493 2 35 . ALA . 18493 2 36 . GLY . 18493 2 37 . GLU . 18493 2 38 . LYS . 18493 2 39 . VAL . 18493 2 40 . THR . 18493 2 41 . MET . 18493 2 42 . SER . 18493 2 43 . CYS . 18493 2 44 . LYS . 18493 2 45 . SER . 18493 2 46 . SER . 18493 2 47 . GLN . 18493 2 48 . SER . 18493 2 49 . LEU . 18493 2 50 . LEU . 18493 2 51 . ASN . 18493 2 52 . SER . 18493 2 53 . ARG . 18493 2 54 . THR . 18493 2 55 . ARG . 18493 2 56 . LYS . 18493 2 57 . ASN . 18493 2 58 . TYR . 18493 2 59 . LEU . 18493 2 60 . ALA . 18493 2 61 . TRP . 18493 2 62 . TYR . 18493 2 63 . GLN . 18493 2 64 . GLN . 18493 2 65 . LYS . 18493 2 66 . PRO . 18493 2 67 . GLY . 18493 2 68 . GLN . 18493 2 69 . SER . 18493 2 70 . PRO . 18493 2 71 . LYS . 18493 2 72 . LEU . 18493 2 73 . LEU . 18493 2 74 . ILE . 18493 2 75 . TYR . 18493 2 76 . TRP . 18493 2 77 . ALA . 18493 2 78 . SER . 18493 2 79 . THR . 18493 2 80 . ARG . 18493 2 81 . GLU . 18493 2 82 . SER . 18493 2 83 . GLY . 18493 2 84 . VAL . 18493 2 85 . PRO . 18493 2 86 . ASP . 18493 2 87 . ARG . 18493 2 88 . PHE . 18493 2 89 . THR . 18493 2 90 . GLY . 18493 2 91 . SER . 18493 2 92 . GLY . 18493 2 93 . SER . 18493 2 94 . GLY . 18493 2 95 . THR . 18493 2 96 . ASP . 18493 2 97 . PHE . 18493 2 98 . THR . 18493 2 99 . LEU . 18493 2 100 . THR . 18493 2 101 . ILE . 18493 2 102 . SER . 18493 2 103 . SER . 18493 2 104 . VAL . 18493 2 105 . GLN . 18493 2 106 . ALA . 18493 2 107 . GLU . 18493 2 108 . ASP . 18493 2 109 . LEU . 18493 2 110 . ALA . 18493 2 111 . VAL . 18493 2 112 . TYR . 18493 2 113 . TYR . 18493 2 114 . CYS . 18493 2 115 . LYS . 18493 2 116 . GLN . 18493 2 117 . SER . 18493 2 118 . TYR . 18493 2 119 . ASN . 18493 2 120 . LEU . 18493 2 121 . TYR . 18493 2 122 . THR . 18493 2 123 . PHE . 18493 2 124 . GLY . 18493 2 125 . GLY . 18493 2 126 . GLY . 18493 2 127 . THR . 18493 2 128 . LYS . 18493 2 129 . LEU . 18493 2 130 . GLU . 18493 2 131 . ILE . 18493 2 132 . LYS . 18493 2 133 . ARG . 18493 2 134 . ALA . 18493 2 135 . ASP . 18493 2 136 . ALA . 18493 2 137 . ALA . 18493 2 138 . PRO . 18493 2 139 . THR . 18493 2 140 . VAL . 18493 2 141 . SER . 18493 2 142 . ILE . 18493 2 143 . PHE . 18493 2 144 . PRO . 18493 2 145 . PRO . 18493 2 146 . SER . 18493 2 147 . SER . 18493 2 148 . GLU . 18493 2 149 . GLN . 18493 2 150 . LEU . 18493 2 151 . THR . 18493 2 152 . SER . 18493 2 153 . GLY . 18493 2 154 . GLY . 18493 2 155 . ALA . 18493 2 156 . SER . 18493 2 157 . VAL . 18493 2 158 . VAL . 18493 2 159 . CYS . 18493 2 160 . PHE . 18493 2 161 . LEU . 18493 2 162 . ASN . 18493 2 163 . ASN . 18493 2 164 . PHE . 18493 2 165 . TYR . 18493 2 166 . PRO . 18493 2 167 . LYS . 18493 2 168 . ASP . 18493 2 169 . ILE . 18493 2 170 . ASN . 18493 2 171 . VAL . 18493 2 172 . LYS . 18493 2 173 . TRP . 18493 2 174 . LYS . 18493 2 175 . ILE . 18493 2 176 . ASP . 18493 2 177 . GLY . 18493 2 178 . SER . 18493 2 179 . GLU . 18493 2 180 . ARG . 18493 2 181 . GLN . 18493 2 182 . ASN . 18493 2 183 . GLY . 18493 2 184 . VAL . 18493 2 185 . LEU . 18493 2 186 . ASN . 18493 2 187 . SER . 18493 2 188 . TRP . 18493 2 189 . THR . 18493 2 190 . ASP . 18493 2 191 . GLN . 18493 2 192 . ASP . 18493 2 193 . SER . 18493 2 194 . LYS . 18493 2 195 . ASP . 18493 2 196 . SER . 18493 2 197 . THR . 18493 2 198 . TYR . 18493 2 199 . SER . 18493 2 200 . MET . 18493 2 201 . SER . 18493 2 202 . SER . 18493 2 203 . THR . 18493 2 204 . LEU . 18493 2 205 . THR . 18493 2 206 . LEU . 18493 2 207 . THR . 18493 2 208 . LYS . 18493 2 209 . ASP . 18493 2 210 . GLU . 18493 2 211 . TYR . 18493 2 212 . GLU . 18493 2 213 . ARG . 18493 2 214 . HIS . 18493 2 215 . ASN . 18493 2 216 . SER . 18493 2 217 . TYR . 18493 2 218 . THR . 18493 2 219 . CYS . 18493 2 220 . GLU . 18493 2 221 . ALA . 18493 2 222 . THR . 18493 2 223 . HIS . 18493 2 224 . LYS . 18493 2 225 . THR . 18493 2 226 . SER . 18493 2 227 . THR . 18493 2 228 . SER . 18493 2 229 . PRO . 18493 2 230 . ILE . 18493 2 231 . VAL . 18493 2 232 . LYS . 18493 2 233 . SER . 18493 2 234 . PHE . 18493 2 235 . ASN . 18493 2 236 . ARG . 18493 2 237 . ASN . 18493 2 238 . GLU . 18493 2 239 . CYS . 18493 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 18493 2 . ASP 2 2 18493 2 . SER 3 3 18493 2 . GLN 4 4 18493 2 . ALA 5 5 18493 2 . GLN 6 6 18493 2 . VAL 7 7 18493 2 . LEU 8 8 18493 2 . ILE 9 9 18493 2 . LEU 10 10 18493 2 . LEU 11 11 18493 2 . LEU 12 12 18493 2 . LEU 13 13 18493 2 . TRP 14 14 18493 2 . VAL 15 15 18493 2 . SER 16 16 18493 2 . GLY 17 17 18493 2 . THR 18 18 18493 2 . CYS 19 19 18493 2 . GLY 20 20 18493 2 . ASP 21 21 18493 2 . ILE 22 22 18493 2 . VAL 23 23 18493 2 . MET 24 24 18493 2 . SER 25 25 18493 2 . GLN 26 26 18493 2 . SER 27 27 18493 2 . PRO 28 28 18493 2 . SER 29 29 18493 2 . SER 30 30 18493 2 . LEU 31 31 18493 2 . ALA 32 32 18493 2 . VAL 33 33 18493 2 . SER 34 34 18493 2 . ALA 35 35 18493 2 . GLY 36 36 18493 2 . GLU 37 37 18493 2 . LYS 38 38 18493 2 . VAL 39 39 18493 2 . THR 40 40 18493 2 . MET 41 41 18493 2 . SER 42 42 18493 2 . CYS 43 43 18493 2 . LYS 44 44 18493 2 . SER 45 45 18493 2 . SER 46 46 18493 2 . GLN 47 47 18493 2 . SER 48 48 18493 2 . LEU 49 49 18493 2 . LEU 50 50 18493 2 . ASN 51 51 18493 2 . SER 52 52 18493 2 . ARG 53 53 18493 2 . THR 54 54 18493 2 . ARG 55 55 18493 2 . LYS 56 56 18493 2 . ASN 57 57 18493 2 . TYR 58 58 18493 2 . LEU 59 59 18493 2 . ALA 60 60 18493 2 . TRP 61 61 18493 2 . TYR 62 62 18493 2 . GLN 63 63 18493 2 . GLN 64 64 18493 2 . LYS 65 65 18493 2 . PRO 66 66 18493 2 . GLY 67 67 18493 2 . GLN 68 68 18493 2 . SER 69 69 18493 2 . PRO 70 70 18493 2 . LYS 71 71 18493 2 . LEU 72 72 18493 2 . LEU 73 73 18493 2 . ILE 74 74 18493 2 . TYR 75 75 18493 2 . TRP 76 76 18493 2 . ALA 77 77 18493 2 . SER 78 78 18493 2 . THR 79 79 18493 2 . ARG 80 80 18493 2 . GLU 81 81 18493 2 . SER 82 82 18493 2 . GLY 83 83 18493 2 . VAL 84 84 18493 2 . PRO 85 85 18493 2 . ASP 86 86 18493 2 . ARG 87 87 18493 2 . PHE 88 88 18493 2 . THR 89 89 18493 2 . GLY 90 90 18493 2 . SER 91 91 18493 2 . GLY 92 92 18493 2 . SER 93 93 18493 2 . GLY 94 94 18493 2 . THR 95 95 18493 2 . ASP 96 96 18493 2 . PHE 97 97 18493 2 . THR 98 98 18493 2 . LEU 99 99 18493 2 . THR 100 100 18493 2 . ILE 101 101 18493 2 . SER 102 102 18493 2 . SER 103 103 18493 2 . VAL 104 104 18493 2 . GLN 105 105 18493 2 . ALA 106 106 18493 2 . GLU 107 107 18493 2 . ASP 108 108 18493 2 . LEU 109 109 18493 2 . ALA 110 110 18493 2 . VAL 111 111 18493 2 . TYR 112 112 18493 2 . TYR 113 113 18493 2 . CYS 114 114 18493 2 . LYS 115 115 18493 2 . GLN 116 116 18493 2 . SER 117 117 18493 2 . TYR 118 118 18493 2 . ASN 119 119 18493 2 . LEU 120 120 18493 2 . TYR 121 121 18493 2 . THR 122 122 18493 2 . PHE 123 123 18493 2 . GLY 124 124 18493 2 . GLY 125 125 18493 2 . GLY 126 126 18493 2 . THR 127 127 18493 2 . LYS 128 128 18493 2 . LEU 129 129 18493 2 . GLU 130 130 18493 2 . ILE 131 131 18493 2 . LYS 132 132 18493 2 . ARG 133 133 18493 2 . ALA 134 134 18493 2 . ASP 135 135 18493 2 . ALA 136 136 18493 2 . ALA 137 137 18493 2 . PRO 138 138 18493 2 . THR 139 139 18493 2 . VAL 140 140 18493 2 . SER 141 141 18493 2 . ILE 142 142 18493 2 . PHE 143 143 18493 2 . PRO 144 144 18493 2 . PRO 145 145 18493 2 . SER 146 146 18493 2 . SER 147 147 18493 2 . GLU 148 148 18493 2 . GLN 149 149 18493 2 . LEU 150 150 18493 2 . THR 151 151 18493 2 . SER 152 152 18493 2 . GLY 153 153 18493 2 . GLY 154 154 18493 2 . ALA 155 155 18493 2 . SER 156 156 18493 2 . VAL 157 157 18493 2 . VAL 158 158 18493 2 . CYS 159 159 18493 2 . PHE 160 160 18493 2 . LEU 161 161 18493 2 . ASN 162 162 18493 2 . ASN 163 163 18493 2 . PHE 164 164 18493 2 . TYR 165 165 18493 2 . PRO 166 166 18493 2 . LYS 167 167 18493 2 . ASP 168 168 18493 2 . ILE 169 169 18493 2 . ASN 170 170 18493 2 . VAL 171 171 18493 2 . LYS 172 172 18493 2 . TRP 173 173 18493 2 . LYS 174 174 18493 2 . ILE 175 175 18493 2 . ASP 176 176 18493 2 . GLY 177 177 18493 2 . SER 178 178 18493 2 . GLU 179 179 18493 2 . ARG 180 180 18493 2 . GLN 181 181 18493 2 . ASN 182 182 18493 2 . GLY 183 183 18493 2 . VAL 184 184 18493 2 . LEU 185 185 18493 2 . ASN 186 186 18493 2 . SER 187 187 18493 2 . TRP 188 188 18493 2 . THR 189 189 18493 2 . ASP 190 190 18493 2 . GLN 191 191 18493 2 . ASP 192 192 18493 2 . SER 193 193 18493 2 . LYS 194 194 18493 2 . ASP 195 195 18493 2 . SER 196 196 18493 2 . THR 197 197 18493 2 . TYR 198 198 18493 2 . SER 199 199 18493 2 . MET 200 200 18493 2 . SER 201 201 18493 2 . SER 202 202 18493 2 . THR 203 203 18493 2 . LEU 204 204 18493 2 . THR 205 205 18493 2 . LEU 206 206 18493 2 . THR 207 207 18493 2 . LYS 208 208 18493 2 . ASP 209 209 18493 2 . GLU 210 210 18493 2 . TYR 211 211 18493 2 . GLU 212 212 18493 2 . ARG 213 213 18493 2 . HIS 214 214 18493 2 . ASN 215 215 18493 2 . SER 216 216 18493 2 . TYR 217 217 18493 2 . THR 218 218 18493 2 . CYS 219 219 18493 2 . GLU 220 220 18493 2 . ALA 221 221 18493 2 . THR 222 222 18493 2 . HIS 223 223 18493 2 . LYS 224 224 18493 2 . THR 225 225 18493 2 . SER 226 226 18493 2 . THR 227 227 18493 2 . SER 228 228 18493 2 . PRO 229 229 18493 2 . ILE 230 230 18493 2 . VAL 231 231 18493 2 . LYS 232 232 18493 2 . SER 233 233 18493 2 . PHE 234 234 18493 2 . ASN 235 235 18493 2 . ARG 236 236 18493 2 . ASN 237 237 18493 2 . GLU 238 238 18493 2 . CYS 239 239 18493 2 stop_ save_ save_entity_3 _Entity.Sf_category entity _Entity.Sf_framecode entity_3 _Entity.Entry_ID 18493 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name entity_3 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID C,F _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; EVQLVESGGGLVKPGGSLKL SCAASGFAFSSYDMSWVRQT PEKRLEWVAYISSGGGSTYY PDTVKGRFTISRDNAKNTLY LQMSSLKSEDTAMYYCARPD YRSYAMDYWGQGTSVTVSSA KTTAPSVYPLAPVCGDTTGS SVTLGCLVKGYFPEPVTLTW NSGSLSSGVHTFPAVLQSDL YTLSSSVTVTSSTWPSQSIT CNVAHPASSTKVDKKIEPRG P ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 221 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'Fab fragment heavy chain' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 23024.885 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2LTQ . "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" . . . . . 100.00 221 100.00 100.00 2.13e-157 . . . . 18493 3 2 no PDB 2ZUQ . "Crystal Structure Of Dsbb-Fab Complex" . . . . . 100.00 221 100.00 100.00 2.13e-157 . . . . 18493 3 3 no GB AAN06761 . "immunoglobulin heavy chain variable region [Mus musculus]" . . . . . 50.68 112 97.32 97.32 4.04e-69 . . . . 18493 3 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . GLU . 18493 3 2 . VAL . 18493 3 3 . GLN . 18493 3 4 . LEU . 18493 3 5 . VAL . 18493 3 6 . GLU . 18493 3 7 . SER . 18493 3 8 . GLY . 18493 3 9 . GLY . 18493 3 10 . GLY . 18493 3 11 . LEU . 18493 3 12 . VAL . 18493 3 13 . LYS . 18493 3 14 . PRO . 18493 3 15 . GLY . 18493 3 16 . GLY . 18493 3 17 . SER . 18493 3 18 . LEU . 18493 3 19 . LYS . 18493 3 20 . LEU . 18493 3 21 . SER . 18493 3 22 . CYS . 18493 3 23 . ALA . 18493 3 24 . ALA . 18493 3 25 . SER . 18493 3 26 . GLY . 18493 3 27 . PHE . 18493 3 28 . ALA . 18493 3 29 . PHE . 18493 3 30 . SER . 18493 3 31 . SER . 18493 3 32 . TYR . 18493 3 33 . ASP . 18493 3 34 . MET . 18493 3 35 . SER . 18493 3 36 . TRP . 18493 3 37 . VAL . 18493 3 38 . ARG . 18493 3 39 . GLN . 18493 3 40 . THR . 18493 3 41 . PRO . 18493 3 42 . GLU . 18493 3 43 . LYS . 18493 3 44 . ARG . 18493 3 45 . LEU . 18493 3 46 . GLU . 18493 3 47 . TRP . 18493 3 48 . VAL . 18493 3 49 . ALA . 18493 3 50 . TYR . 18493 3 51 . ILE . 18493 3 52 . SER . 18493 3 53 . SER . 18493 3 54 . GLY . 18493 3 55 . GLY . 18493 3 56 . GLY . 18493 3 57 . SER . 18493 3 58 . THR . 18493 3 59 . TYR . 18493 3 60 . TYR . 18493 3 61 . PRO . 18493 3 62 . ASP . 18493 3 63 . THR . 18493 3 64 . VAL . 18493 3 65 . LYS . 18493 3 66 . GLY . 18493 3 67 . ARG . 18493 3 68 . PHE . 18493 3 69 . THR . 18493 3 70 . ILE . 18493 3 71 . SER . 18493 3 72 . ARG . 18493 3 73 . ASP . 18493 3 74 . ASN . 18493 3 75 . ALA . 18493 3 76 . LYS . 18493 3 77 . ASN . 18493 3 78 . THR . 18493 3 79 . LEU . 18493 3 80 . TYR . 18493 3 81 . LEU . 18493 3 82 . GLN . 18493 3 83 . MET . 18493 3 84 . SER . 18493 3 85 . SER . 18493 3 86 . LEU . 18493 3 87 . LYS . 18493 3 88 . SER . 18493 3 89 . GLU . 18493 3 90 . ASP . 18493 3 91 . THR . 18493 3 92 . ALA . 18493 3 93 . MET . 18493 3 94 . TYR . 18493 3 95 . TYR . 18493 3 96 . CYS . 18493 3 97 . ALA . 18493 3 98 . ARG . 18493 3 99 . PRO . 18493 3 100 . ASP . 18493 3 101 . TYR . 18493 3 102 . ARG . 18493 3 103 . SER . 18493 3 104 . TYR . 18493 3 105 . ALA . 18493 3 106 . MET . 18493 3 107 . ASP . 18493 3 108 . TYR . 18493 3 109 . TRP . 18493 3 110 . GLY . 18493 3 111 . GLN . 18493 3 112 . GLY . 18493 3 113 . THR . 18493 3 114 . SER . 18493 3 115 . VAL . 18493 3 116 . THR . 18493 3 117 . VAL . 18493 3 118 . SER . 18493 3 119 . SER . 18493 3 120 . ALA . 18493 3 121 . LYS . 18493 3 122 . THR . 18493 3 123 . THR . 18493 3 124 . ALA . 18493 3 125 . PRO . 18493 3 126 . SER . 18493 3 127 . VAL . 18493 3 128 . TYR . 18493 3 129 . PRO . 18493 3 130 . LEU . 18493 3 131 . ALA . 18493 3 132 . PRO . 18493 3 133 . VAL . 18493 3 134 . CYS . 18493 3 135 . GLY . 18493 3 136 . ASP . 18493 3 137 . THR . 18493 3 138 . THR . 18493 3 139 . GLY . 18493 3 140 . SER . 18493 3 141 . SER . 18493 3 142 . VAL . 18493 3 143 . THR . 18493 3 144 . LEU . 18493 3 145 . GLY . 18493 3 146 . CYS . 18493 3 147 . LEU . 18493 3 148 . VAL . 18493 3 149 . LYS . 18493 3 150 . GLY . 18493 3 151 . TYR . 18493 3 152 . PHE . 18493 3 153 . PRO . 18493 3 154 . GLU . 18493 3 155 . PRO . 18493 3 156 . VAL . 18493 3 157 . THR . 18493 3 158 . LEU . 18493 3 159 . THR . 18493 3 160 . TRP . 18493 3 161 . ASN . 18493 3 162 . SER . 18493 3 163 . GLY . 18493 3 164 . SER . 18493 3 165 . LEU . 18493 3 166 . SER . 18493 3 167 . SER . 18493 3 168 . GLY . 18493 3 169 . VAL . 18493 3 170 . HIS . 18493 3 171 . THR . 18493 3 172 . PHE . 18493 3 173 . PRO . 18493 3 174 . ALA . 18493 3 175 . VAL . 18493 3 176 . LEU . 18493 3 177 . GLN . 18493 3 178 . SER . 18493 3 179 . ASP . 18493 3 180 . LEU . 18493 3 181 . TYR . 18493 3 182 . THR . 18493 3 183 . LEU . 18493 3 184 . SER . 18493 3 185 . SER . 18493 3 186 . SER . 18493 3 187 . VAL . 18493 3 188 . THR . 18493 3 189 . VAL . 18493 3 190 . THR . 18493 3 191 . SER . 18493 3 192 . SER . 18493 3 193 . THR . 18493 3 194 . TRP . 18493 3 195 . PRO . 18493 3 196 . SER . 18493 3 197 . GLN . 18493 3 198 . SER . 18493 3 199 . ILE . 18493 3 200 . THR . 18493 3 201 . CYS . 18493 3 202 . ASN . 18493 3 203 . VAL . 18493 3 204 . ALA . 18493 3 205 . HIS . 18493 3 206 . PRO . 18493 3 207 . ALA . 18493 3 208 . SER . 18493 3 209 . SER . 18493 3 210 . THR . 18493 3 211 . LYS . 18493 3 212 . VAL . 18493 3 213 . ASP . 18493 3 214 . LYS . 18493 3 215 . LYS . 18493 3 216 . ILE . 18493 3 217 . GLU . 18493 3 218 . PRO . 18493 3 219 . ARG . 18493 3 220 . GLY . 18493 3 221 . PRO . 18493 3 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLU 1 1 18493 3 . VAL 2 2 18493 3 . GLN 3 3 18493 3 . LEU 4 4 18493 3 . VAL 5 5 18493 3 . GLU 6 6 18493 3 . SER 7 7 18493 3 . GLY 8 8 18493 3 . GLY 9 9 18493 3 . GLY 10 10 18493 3 . LEU 11 11 18493 3 . VAL 12 12 18493 3 . LYS 13 13 18493 3 . PRO 14 14 18493 3 . GLY 15 15 18493 3 . GLY 16 16 18493 3 . SER 17 17 18493 3 . LEU 18 18 18493 3 . LYS 19 19 18493 3 . LEU 20 20 18493 3 . SER 21 21 18493 3 . CYS 22 22 18493 3 . ALA 23 23 18493 3 . ALA 24 24 18493 3 . SER 25 25 18493 3 . GLY 26 26 18493 3 . PHE 27 27 18493 3 . ALA 28 28 18493 3 . PHE 29 29 18493 3 . SER 30 30 18493 3 . SER 31 31 18493 3 . TYR 32 32 18493 3 . ASP 33 33 18493 3 . MET 34 34 18493 3 . SER 35 35 18493 3 . TRP 36 36 18493 3 . VAL 37 37 18493 3 . ARG 38 38 18493 3 . GLN 39 39 18493 3 . THR 40 40 18493 3 . PRO 41 41 18493 3 . GLU 42 42 18493 3 . LYS 43 43 18493 3 . ARG 44 44 18493 3 . LEU 45 45 18493 3 . GLU 46 46 18493 3 . TRP 47 47 18493 3 . VAL 48 48 18493 3 . ALA 49 49 18493 3 . TYR 50 50 18493 3 . ILE 51 51 18493 3 . SER 52 52 18493 3 . SER 53 53 18493 3 . GLY 54 54 18493 3 . GLY 55 55 18493 3 . GLY 56 56 18493 3 . SER 57 57 18493 3 . THR 58 58 18493 3 . TYR 59 59 18493 3 . TYR 60 60 18493 3 . PRO 61 61 18493 3 . ASP 62 62 18493 3 . THR 63 63 18493 3 . VAL 64 64 18493 3 . LYS 65 65 18493 3 . GLY 66 66 18493 3 . ARG 67 67 18493 3 . PHE 68 68 18493 3 . THR 69 69 18493 3 . ILE 70 70 18493 3 . SER 71 71 18493 3 . ARG 72 72 18493 3 . ASP 73 73 18493 3 . ASN 74 74 18493 3 . ALA 75 75 18493 3 . LYS 76 76 18493 3 . ASN 77 77 18493 3 . THR 78 78 18493 3 . LEU 79 79 18493 3 . TYR 80 80 18493 3 . LEU 81 81 18493 3 . GLN 82 82 18493 3 . MET 83 83 18493 3 . SER 84 84 18493 3 . SER 85 85 18493 3 . LEU 86 86 18493 3 . LYS 87 87 18493 3 . SER 88 88 18493 3 . GLU 89 89 18493 3 . ASP 90 90 18493 3 . THR 91 91 18493 3 . ALA 92 92 18493 3 . MET 93 93 18493 3 . TYR 94 94 18493 3 . TYR 95 95 18493 3 . CYS 96 96 18493 3 . ALA 97 97 18493 3 . ARG 98 98 18493 3 . PRO 99 99 18493 3 . ASP 100 100 18493 3 . TYR 101 101 18493 3 . ARG 102 102 18493 3 . SER 103 103 18493 3 . TYR 104 104 18493 3 . ALA 105 105 18493 3 . MET 106 106 18493 3 . ASP 107 107 18493 3 . TYR 108 108 18493 3 . TRP 109 109 18493 3 . GLY 110 110 18493 3 . GLN 111 111 18493 3 . GLY 112 112 18493 3 . THR 113 113 18493 3 . SER 114 114 18493 3 . VAL 115 115 18493 3 . THR 116 116 18493 3 . VAL 117 117 18493 3 . SER 118 118 18493 3 . SER 119 119 18493 3 . ALA 120 120 18493 3 . LYS 121 121 18493 3 . THR 122 122 18493 3 . THR 123 123 18493 3 . ALA 124 124 18493 3 . PRO 125 125 18493 3 . SER 126 126 18493 3 . VAL 127 127 18493 3 . TYR 128 128 18493 3 . PRO 129 129 18493 3 . LEU 130 130 18493 3 . ALA 131 131 18493 3 . PRO 132 132 18493 3 . VAL 133 133 18493 3 . CYS 134 134 18493 3 . GLY 135 135 18493 3 . ASP 136 136 18493 3 . THR 137 137 18493 3 . THR 138 138 18493 3 . GLY 139 139 18493 3 . SER 140 140 18493 3 . SER 141 141 18493 3 . VAL 142 142 18493 3 . THR 143 143 18493 3 . LEU 144 144 18493 3 . GLY 145 145 18493 3 . CYS 146 146 18493 3 . LEU 147 147 18493 3 . VAL 148 148 18493 3 . LYS 149 149 18493 3 . GLY 150 150 18493 3 . TYR 151 151 18493 3 . PHE 152 152 18493 3 . PRO 153 153 18493 3 . GLU 154 154 18493 3 . PRO 155 155 18493 3 . VAL 156 156 18493 3 . THR 157 157 18493 3 . LEU 158 158 18493 3 . THR 159 159 18493 3 . TRP 160 160 18493 3 . ASN 161 161 18493 3 . SER 162 162 18493 3 . GLY 163 163 18493 3 . SER 164 164 18493 3 . LEU 165 165 18493 3 . SER 166 166 18493 3 . SER 167 167 18493 3 . GLY 168 168 18493 3 . VAL 169 169 18493 3 . HIS 170 170 18493 3 . THR 171 171 18493 3 . PHE 172 172 18493 3 . PRO 173 173 18493 3 . ALA 174 174 18493 3 . VAL 175 175 18493 3 . LEU 176 176 18493 3 . GLN 177 177 18493 3 . SER 178 178 18493 3 . ASP 179 179 18493 3 . LEU 180 180 18493 3 . TYR 181 181 18493 3 . THR 182 182 18493 3 . LEU 183 183 18493 3 . SER 184 184 18493 3 . SER 185 185 18493 3 . SER 186 186 18493 3 . VAL 187 187 18493 3 . THR 188 188 18493 3 . VAL 189 189 18493 3 . THR 190 190 18493 3 . SER 191 191 18493 3 . SER 192 192 18493 3 . THR 193 193 18493 3 . TRP 194 194 18493 3 . PRO 195 195 18493 3 . SER 196 196 18493 3 . GLN 197 197 18493 3 . SER 198 198 18493 3 . ILE 199 199 18493 3 . THR 200 200 18493 3 . CYS 201 201 18493 3 . ASN 202 202 18493 3 . VAL 203 203 18493 3 . ALA 204 204 18493 3 . HIS 205 205 18493 3 . PRO 206 206 18493 3 . ALA 207 207 18493 3 . SER 208 208 18493 3 . SER 209 209 18493 3 . THR 210 210 18493 3 . LYS 211 211 18493 3 . VAL 212 212 18493 3 . ASP 213 213 18493 3 . LYS 214 214 18493 3 . LYS 215 215 18493 3 . ILE 216 216 18493 3 . GLU 217 217 18493 3 . PRO 218 218 18493 3 . ARG 219 219 18493 3 . GLY 220 220 18493 3 . PRO 221 221 18493 3 stop_ save_ save_entity_UQ1 _Entity.Sf_category entity _Entity.Sf_framecode entity_UQ1 _Entity.Entry_ID 18493 _Entity.ID 4 _Entity.BMRB_code UQ1 _Entity.Name entity_UQ1 _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID UQ1 _Entity.Nonpolymer_comp_label $chem_comp_UQ1 _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 4 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 250.290 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID UBIQUINONE-1 BMRB 18493 4 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID UBIQUINONE-1 BMRB 18493 4 UQ1 'Three letter code' 18493 4 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 UQ1 $chem_comp_UQ1 18493 4 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 UQ1 C1 18493 4 2 1 UQ1 C10 18493 4 3 1 UQ1 C11 18493 4 4 1 UQ1 C2 18493 4 5 1 UQ1 C3 18493 4 6 1 UQ1 C4 18493 4 7 1 UQ1 C5 18493 4 8 1 UQ1 C6 18493 4 9 1 UQ1 C7 18493 4 10 1 UQ1 C8 18493 4 11 1 UQ1 C9 18493 4 12 1 UQ1 CM2 18493 4 13 1 UQ1 CM3 18493 4 14 1 UQ1 CM5 18493 4 15 1 UQ1 H101 18493 4 16 1 UQ1 H102 18493 4 17 1 UQ1 H103 18493 4 18 1 UQ1 H111 18493 4 19 1 UQ1 H112 18493 4 20 1 UQ1 H113 18493 4 21 1 UQ1 H71 18493 4 22 1 UQ1 H72 18493 4 23 1 UQ1 H8 18493 4 24 1 UQ1 HM21 18493 4 25 1 UQ1 HM22 18493 4 26 1 UQ1 HM23 18493 4 27 1 UQ1 HM31 18493 4 28 1 UQ1 HM32 18493 4 29 1 UQ1 HM33 18493 4 30 1 UQ1 HM51 18493 4 31 1 UQ1 HM52 18493 4 32 1 UQ1 HM53 18493 4 33 1 UQ1 O1 18493 4 34 1 UQ1 O2 18493 4 35 1 UQ1 O3 18493 4 36 1 UQ1 O4 18493 4 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 18493 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $DsbB . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli K12 . . . . . . . . . . . . . . . dsbB . . . . 18493 1 2 2 $entity_2 . 10090 organism . 'Mus musculus' Mouse . . Eukaryota Metazoa Mus musculus . . . . . . . . . . . . . . . . . . . . . 18493 1 3 3 $entity_3 . 10090 organism . 'Mus musculus' Mouse . . Eukaryota Metazoa Mus musculus . . . . . . . . . . . . . . . . . . . . . 18493 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 18493 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $DsbB . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pqe70 . . . . . . 18493 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_UQ1 _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_UQ1 _Chem_comp.Entry_ID 18493 _Chem_comp.ID UQ1 _Chem_comp.Provenance PDB _Chem_comp.Name UBIQUINONE-1 _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code UQ1 _Chem_comp.PDB_code UQ1 _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-04-05 _Chem_comp.Modified_date 2012-04-05 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code UQ1 _Chem_comp.Number_atoms_all 36 _Chem_comp.Number_atoms_nh 18 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C14H18O4/c1-8(2)6-7-10-9(3)11(15)13(17-4)14(18-5)12(10)16/h6H,7H2,1-5H3 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C14 H18 O4' _Chem_comp.Formula_weight 250.290 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1PRC _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C SMILES 'OpenEye OEToolkits' 1.5.0 18493 UQ1 CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18493 UQ1 COC1=C(OC)C(=O)C(=C(C)C1=O)CC=C(C)C SMILES CACTVS 3.341 18493 UQ1 COC1=C(OC)C(=O)C(=C(C)C1=O)CC=C(C)C SMILES_CANONICAL CACTVS 3.341 18493 UQ1 InChI=1S/C14H18O4/c1-8(2)6-7-10-9(3)11(15)13(17-4)14(18-5)12(10)16/h6H,7H2,1-5H3 InChI InChI 1.03 18493 UQ1 O=C1C(=C(C(=O)C(OC)=C1OC)C)C\C=C(/C)C SMILES ACDLabs 10.04 18493 UQ1 SOECUQMRSRVZQQ-UHFFFAOYSA-N InChIKey InChI 1.03 18493 UQ1 stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en-1-yl)cyclohexa-2,5-diene-1,4-dione 'SYSTEMATIC NAME' ACDLabs 10.04 18493 UQ1 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-enyl)cyclohexa-2,5-diene-1,4-dione 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18493 UQ1 stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID C1 C1 C1 C1 . C . . N 0 . . . 1 no no . . . . 132.170 . 72.122 . -3.856 . 0.913 -0.297 -0.013 1 . 18493 UQ1 O1 O1 O1 O1 . O . . N 0 . . . 1 no no . . . . 132.158 . 72.025 . -5.078 . 1.905 -0.327 -0.714 2 . 18493 UQ1 C2 C2 C2 C2 . C . . N 0 . . . 1 no no . . . . 132.272 . 73.440 . -3.207 . 1.030 0.054 1.415 3 . 18493 UQ1 O2 O2 O2 O2 . O . . N 0 . . . 1 no no . . . . 132.359 . 74.474 . -4.047 . 2.245 0.344 1.947 4 . 18493 UQ1 CM2 CM2 CM2 CM2 . C . . N 0 . . . 1 no no . . . . 133.395 . 74.506 . -5.062 . 3.009 -0.862 1.914 5 . 18493 UQ1 C3 C3 C3 C3 . C . . N 0 . . . 1 no no . . . . 132.266 . 73.569 . -1.868 . -0.075 0.086 2.194 6 . 18493 UQ1 O3 O3 O3 O3 . O . . N 0 . . . 1 no no . . . . 132.334 . 74.711 . -1.158 . 0.027 0.409 3.508 7 . 18493 UQ1 CM3 CM3 CM3 CM3 . C . . N 0 . . . 1 no no . . . . 132.638 . 75.995 . -1.763 . -0.639 1.661 3.679 8 . 18493 UQ1 C4 C4 C4 C4 . C . . N 0 . . . 1 no no . . . . 132.165 . 72.335 . -1.064 . -1.393 -0.236 1.613 9 . 18493 UQ1 O4 O4 O4 O4 . O . . N 0 . . . 1 no no . . . . 132.170 . 72.435 . 0.161 . -2.387 -0.208 2.310 10 . 18493 UQ1 C5 C5 C5 C5 . C . . N 0 . . . 1 no no . . . . 132.073 . 71.000 . -1.715 . -1.504 -0.582 0.179 11 . 18493 UQ1 CM5 CM5 CM5 CM5 . C . . N 0 . . . 1 no no . . . . 131.975 . 69.756 . -0.890 . -2.851 -0.905 -0.413 12 . 18493 UQ1 C6 C6 C6 C6 . C . . N 0 . . . 1 no no . . . . 132.066 . 70.910 . -3.050 . -0.410 -0.613 -0.590 13 . 18493 UQ1 C7 C7 C7 C7 . C . . N 0 . . . 1 no no . . . . 131.984 . 69.590 . -3.754 . -0.528 -0.972 -2.049 14 . 18493 UQ1 C8 C8 C8 C8 . C . . N 0 . . . 1 no no . . . . 130.636 . 68.902 . -3.489 . -0.754 0.279 -2.857 15 . 18493 UQ1 C9 C9 C9 C9 . C . . N 0 . . . 1 no no . . . . 130.329 . 67.780 . -4.157 . 0.017 0.546 -3.881 16 . 18493 UQ1 C10 C10 C10 C10 . C . . N 0 . . . 1 no no . . . . 131.309 . 67.209 . -5.171 . -0.098 1.873 -4.586 17 . 18493 UQ1 C11 C11 C11 C11 . C . . N 0 . . . 1 no no . . . . 128.992 . 67.067 . -3.910 . 1.023 -0.471 -4.353 18 . 18493 UQ1 HM21 HM21 HM21 1HM2 . H . . N 0 . . . 0 no no . . . . 133.467 . 75.369 . -5.763 . 4.020 -0.662 2.270 19 . 18493 UQ1 HM22 HM22 HM22 2HM2 . H . . N 0 . . . 0 no no . . . . 134.382 . 74.377 . -4.560 . 2.539 -1.607 2.556 20 . 18493 UQ1 HM23 HM23 HM23 3HM2 . H . . N 0 . . . 0 no no . . . . 133.325 . 73.569 . -5.663 . 3.052 -1.237 0.892 21 . 18493 UQ1 HM31 HM31 HM31 1HM3 . H . . N 0 . . . 0 no no . . . . 132.694 . 76.940 . -1.175 . -0.642 1.930 4.736 22 . 18493 UQ1 HM32 HM32 HM32 2HM3 . H . . N 0 . . . 0 no no . . . . 133.600 . 75.885 . -2.315 . -0.119 2.431 3.110 23 . 18493 UQ1 HM33 HM33 HM33 3HM3 . H . . N 0 . . . 0 no no . . . . 131.907 . 76.157 . -2.589 . -1.666 1.578 3.323 24 . 18493 UQ1 HM51 HM51 HM51 1HM5 . H . . N 0 . . . 0 no no . . . . 131.906 . 68.755 . -1.377 . -3.616 -0.828 0.359 25 . 18493 UQ1 HM52 HM52 HM52 2HM5 . H . . N 0 . . . 0 no no . . . . 132.834 . 69.739 . -0.180 . -3.073 -0.202 -1.216 26 . 18493 UQ1 HM53 HM53 HM53 3HM5 . H . . N 0 . . . 0 no no . . . . 131.110 . 69.865 . -0.195 . -2.839 -1.919 -0.812 27 . 18493 UQ1 H71 H71 H71 1H7 . H . . N 0 . . . 1 no no . . . . 132.183 . 69.694 . -4.846 . 0.390 -1.456 -2.380 28 . 18493 UQ1 H72 H72 H72 2H7 . H . . N 0 . . . 1 no no . . . . 132.841 . 68.928 . -3.486 . -1.368 -1.652 -2.189 29 . 18493 UQ1 H8 H8 H8 H8 . H . . N 0 . . . 1 no no . . . . 129.851 . 69.229 . -2.785 . -1.554 0.955 -2.593 30 . 18493 UQ1 H101 H101 H101 1H10 . H . . N 0 . . . 0 no no . . . . 131.053 . 66.276 . -5.726 . 0.619 1.913 -5.405 31 . 18493 UQ1 H102 H102 H102 2H10 . H . . N 0 . . . 0 no no . . . . 131.554 . 68.005 . -5.911 . -1.107 1.987 -4.981 32 . 18493 UQ1 H103 H103 H103 3H10 . H . . N 0 . . . 0 no no . . . . 132.293 . 67.062 . -4.667 . 0.109 2.678 -3.882 33 . 18493 UQ1 H111 H111 H111 1H11 . H . . N 0 . . . 0 no no . . . . 128.736 . 66.134 . -4.465 . 0.898 -1.395 -3.787 34 . 18493 UQ1 H112 H112 H112 2H11 . H . . N 0 . . . 0 no no . . . . 128.903 . 66.858 . -2.818 . 0.867 -0.671 -5.413 35 . 18493 UQ1 H113 H113 H113 3H11 . H . . N 0 . . . 0 no no . . . . 128.169 . 67.803 . -4.066 . 2.030 -0.085 -4.200 36 . 18493 UQ1 stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . DOUB C1 O1 no N 1 . 18493 UQ1 2 . SING C1 C2 no N 2 . 18493 UQ1 3 . SING C1 C6 no N 3 . 18493 UQ1 4 . SING C2 O2 no N 4 . 18493 UQ1 5 . DOUB C2 C3 no N 5 . 18493 UQ1 6 . SING O2 CM2 no N 6 . 18493 UQ1 7 . SING CM2 HM21 no N 7 . 18493 UQ1 8 . SING CM2 HM22 no N 8 . 18493 UQ1 9 . SING CM2 HM23 no N 9 . 18493 UQ1 10 . SING C3 O3 no N 10 . 18493 UQ1 11 . SING C3 C4 no N 11 . 18493 UQ1 12 . SING O3 CM3 no N 12 . 18493 UQ1 13 . SING CM3 HM31 no N 13 . 18493 UQ1 14 . SING CM3 HM32 no N 14 . 18493 UQ1 15 . SING CM3 HM33 no N 15 . 18493 UQ1 16 . DOUB C4 O4 no N 16 . 18493 UQ1 17 . SING C4 C5 no N 17 . 18493 UQ1 18 . SING C5 CM5 no N 18 . 18493 UQ1 19 . DOUB C5 C6 no N 19 . 18493 UQ1 20 . SING CM5 HM51 no N 20 . 18493 UQ1 21 . SING CM5 HM52 no N 21 . 18493 UQ1 22 . SING CM5 HM53 no N 22 . 18493 UQ1 23 . SING C6 C7 no N 23 . 18493 UQ1 24 . SING C7 C8 no N 24 . 18493 UQ1 25 . SING C7 H71 no N 25 . 18493 UQ1 26 . SING C7 H72 no N 26 . 18493 UQ1 27 . DOUB C8 C9 no N 27 . 18493 UQ1 28 . SING C8 H8 no N 28 . 18493 UQ1 29 . SING C9 C10 no N 29 . 18493 UQ1 30 . SING C9 C11 no N 30 . 18493 UQ1 31 . SING C10 H101 no N 31 . 18493 UQ1 32 . SING C10 H102 no N 32 . 18493 UQ1 33 . SING C10 H103 no N 33 . 18493 UQ1 34 . SING C11 H111 no N 34 . 18493 UQ1 35 . SING C11 H112 no N 35 . 18493 UQ1 36 . SING C11 H113 no N 36 . 18493 UQ1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18493 _Sample.ID 1 _Sample.Type membrane _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 DsbB '[U-100% 13C; U-100% 15N]' . . 1 $DsbB . . 7 . . mg . . . . 18493 1 2 DDM 'natural abundance' . . . . . . 2 . . mg . . . . 18493 1 3 'E. coli lipids' 'natural abundance' . . . . . . 7 . . mg . . . . 18493 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 18493 _Sample.ID 2 _Sample.Type membrane _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 DsbB '[2-13C-glycerol; U-15N]' . . 1 $DsbB . . 5 . . mg . . . . 18493 2 2 DDM 'natural abundance' . . . . . . 2 . . mg . . . . 18493 2 3 'E. coli lipids' 'natural abundance' . . . . . . 7 . . mg . . . . 18493 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 18493 _Sample.ID 3 _Sample.Type membrane _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 DsbB '[1,3-13C-glycerol; U-15N]' . . 1 $DsbB . . 4 . . mg . . . . 18493 3 2 DDM 'natural abundance' . . . . . . 2 . . mg . . . . 18493 3 3 'E. coli lipids' 'natural abundance' . . . . . . 7 . . mg . . . . 18493 3 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18493 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'DsbB samples' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.8 . pH 18493 1 pressure 1 . atm 18493 1 temperature 261 . K 18493 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18493 _Software.ID 1 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18493 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18493 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18493 _Software.ID 2 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 18493 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18493 2 stop_ save_ save_X-PLOR_NIH _Software.Sf_category software _Software.Sf_framecode X-PLOR_NIH _Software.Entry_ID 18493 _Software.ID 3 _Software.Name 'X-PLOR NIH' _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Schwieters, Kuszewski, Tjandra and Clore' . . 18493 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18493 3 'structure solution' 18493 3 stop_ save_ save_TALOS+ _Software.Sf_category software _Software.Sf_framecode TALOS+ _Software.Entry_ID 18493 _Software.ID 4 _Software.Name TALOS+ _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Shen, Cornilescu, Delaglio and Bax' . . 18493 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18493 4 stop_ save_ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18493 _Software.ID 5 _Software.Name VNMRJ _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 18493 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18493 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_750 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 750 _NMR_spectrometer.Entry_ID 18493 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_500 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 500 _NMR_spectrometer.Entry_ID 18493 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VXRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18493 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 750 Varian INOVA . 750 . . . 18493 1 2 500 Varian VXRS . 500 . . . 18493 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 18493 _Experiment_list.ID 1 _Experiment_list.Details 'Chemical shifts assignments and CC correlations provide dihedral angle and distance restraints.' loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D CC DARR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $750 . . . . . . . . . . . . . . . . 18493 1 2 '2D CC DARR' no . . . . . . . . . . 2 $sample_2 solid . . 1 $sample_conditions_1 . . . 1 $750 . . . . . . . . . . . . . . . . 18493 1 3 '2D CC DARR' no . . . . . . . . . . 3 $sample_3 solid . . 1 $sample_conditions_1 . . . 1 $750 . . . . . . . . . . . . . . . . 18493 1 4 '3D NCACX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $750 . . . . . . . . . . . . . . . . 18493 1 5 '3D NCOCX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $750 . . . . . . . . . . . . . . . . 18493 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_Adam _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_Adam _Chem_shift_reference.Entry_ID 18493 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'alkane carbons' . . . . ppm 40.48 external direct 1 'separate solid-state NMR rotor' . . . . . . . . 18493 1 N 15 DSS 'alkane carbons' . . . . ppm 40.48 external indirect 0.4029799 'separate solid-state NMR rotor' . . . . . . . . 18493 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_list_DsbB _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_list_DsbB _Assigned_chem_shift_list.Entry_ID 18493 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_Adam _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D CC DARR' . . . 18493 1 2 '2D CC DARR' . . . 18493 1 3 '2D CC DARR' . . . 18493 1 4 '3D NCACX' . . . 18493 1 5 '3D NCOCX' . . . 18493 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 6 6 ASN C C 13 179.258 0.145 . 1 . . . . 6 ASN C 5 18493 1 2 . 1 1 6 6 ASN CA C 13 57.564 0.300 . 1 . . . . 6 ASN CA 1 18493 1 3 . 1 1 6 6 ASN CB C 13 38.167 0.300 . 1 . . . . 6 ASN CB 1 18493 1 4 . 1 1 7 7 GLN H H 1 9.338 0.026 . 1 . . . . 7 GLN HN 2 18493 1 5 . 1 1 7 7 GLN C C 13 180.404 0.092 . 1 . . . . 7 GLN C 5 18493 1 6 . 1 1 7 7 GLN CA C 13 57.611 0.012 . 1 . . . . 7 GLN CA 2 18493 1 7 . 1 1 7 7 GLN CB C 13 26.649 0.210 . 1 . . . . 7 GLN CB 3 18493 1 8 . 1 1 7 7 GLN CG C 13 31.228 0.300 . 1 . . . . 7 GLN CG 1 18493 1 9 . 1 1 7 7 GLN N N 15 120.525 0.189 . 1 . . . . 7 GLN N 7 18493 1 10 . 1 1 8 8 ALA H H 1 9.436 0.052 . 1 . . . . 8 ALA HN 2 18493 1 11 . 1 1 8 8 ALA C C 13 179.313 0.300 . 1 . . . . 8 ALA C 1 18493 1 12 . 1 1 8 8 ALA CA C 13 54.645 0.300 . 1 . . . . 8 ALA CA 1 18493 1 13 . 1 1 8 8 ALA CB C 13 17.967 0.300 . 1 . . . . 8 ALA CB 1 18493 1 14 . 1 1 8 8 ALA N N 15 123.894 0.176 . 1 . . . . 8 ALA N 6 18493 1 15 . 1 1 9 9 SER C C 13 173.894 0.126 . 1 . . . . 9 SER C 4 18493 1 16 . 1 1 9 9 SER CA C 13 60.565 0.137 . 1 . . . . 9 SER CA 5 18493 1 17 . 1 1 9 9 SER CB C 13 63.790 0.070 . 1 . . . . 9 SER CB 4 18493 1 18 . 1 1 10 10 GLN H H 1 7.835 0.300 . 1 . . . A 10 GLN HN 2 18493 1 19 . 1 1 10 10 GLN C C 13 174.766 0.300 . 1 . . . A 10 GLN C 1 18493 1 20 . 1 1 10 10 GLN CB C 13 29.955 0.300 . 1 . . . A 10 GLN CB 1 18493 1 21 . 1 1 10 10 GLN N N 15 119.198 0.200 . 1 . . . A 10 GLN N 5 18493 1 22 . 1 1 11 11 GLY H H 1 8.433 0.005 . 1 . . . A 11 GLY H 2 18493 1 23 . 1 1 11 11 GLY N N 15 108.456 0.067 . 1 . . . A 11 GLY N 2 18493 1 24 . 1 1 12 12 ARG C C 13 178.053 0.300 . 1 . . . A 12 ARG C 1 18493 1 25 . 1 1 12 12 ARG CA C 13 57.504 0.300 . 1 . . . A 12 ARG CA 1 18493 1 26 . 1 1 12 12 ARG CB C 13 30.522 0.300 . 1 . . . A 12 ARG CB 1 18493 1 27 . 1 1 12 12 ARG CD C 13 43.193 0.107 . 1 . . . A 12 ARG CD 3 18493 1 28 . 1 1 12 12 ARG CZ C 13 159.227 0.300 . 1 . . . A 12 ARG CZ 1 18493 1 29 . 1 1 13 13 GLY C C 13 175.091 0.300 . 1 . . . A 13 GLY C 1 18493 1 30 . 1 1 13 13 GLY CA C 13 45.326 0.300 . 1 . . . A 13 GLY CA 1 18493 1 31 . 1 1 13 13 GLY N N 15 108.265 0.300 . 1 . . . A 13 GLY N 1 18493 1 32 . 1 1 14 14 ALA H H 1 9.285 0.003 . 1 . . . A 14 ALA H 2 18493 1 33 . 1 1 14 14 ALA C C 13 179.173 0.300 . 1 . . . A 14 ALA C 1 18493 1 34 . 1 1 14 14 ALA CA C 13 55.061 0.040 . 1 . . . A 14 ALA CA 3 18493 1 35 . 1 1 14 14 ALA N N 15 123.181 0.019 . 1 . . . A 14 ALA N 2 18493 1 36 . 1 1 15 15 TRP H H 1 7.091 0.008 . 1 . . . A 15 TRP H 2 18493 1 37 . 1 1 15 15 TRP C C 13 179.425 0.300 . 1 . . . A 15 TRP C 1 18493 1 38 . 1 1 15 15 TRP CA C 13 58.960 0.074 . 1 . . . A 15 TRP CA 2 18493 1 39 . 1 1 15 15 TRP CB C 13 29.529 0.300 . 1 . . . A 15 TRP CB 3 18493 1 40 . 1 1 15 15 TRP N N 15 116.733 0.031 . 1 . . . A 15 TRP N 2 18493 1 41 . 1 1 16 16 LEU H H 1 9.180 0.050 . 1 . . . A 16 LEU H 3 18493 1 42 . 1 1 16 16 LEU C C 13 178.461 0.056 . 1 . . . A 16 LEU C 5 18493 1 43 . 1 1 16 16 LEU CA C 13 58.246 0.034 . 1 . . . A 16 LEU CA 3 18493 1 44 . 1 1 16 16 LEU CB C 13 41.369 0.319 . 1 . . . A 16 LEU CB 2 18493 1 45 . 1 1 16 16 LEU CG C 13 26.762 0.221 . 1 . . . A 16 LEU CG 2 18493 1 46 . 1 1 16 16 LEU CD1 C 13 22.647 0.300 . 2 . . . A 16 LEU CD1 1 18493 1 47 . 1 1 16 16 LEU CD2 C 13 22.647 0.300 . 2 . . . A 16 LEU CD2 1 18493 1 48 . 1 1 16 16 LEU N N 15 118.671 0.093 . 1 . . . A 16 LEU N 3 18493 1 49 . 1 1 17 17 LEU C C 13 178.787 0.311 . 1 . . . A 17 LEU C 11 18493 1 50 . 1 1 17 17 LEU CA C 13 57.832 0.146 . 1 . . . A 17 LEU CA 8 18493 1 51 . 1 1 17 17 LEU CB C 13 41.395 0.071 . 1 . . . A 17 LEU CB 3 18493 1 52 . 1 1 17 17 LEU CG C 13 27.110 0.142 . 1 . . . A 17 LEU CG 3 18493 1 53 . 1 1 17 17 LEU CD1 C 13 22.055 0.300 . 2 . . . A 17 LEU CD1 1 18493 1 54 . 1 1 17 17 LEU CD2 C 13 22.055 0.300 . 2 . . . A 17 LEU CD2 1 18493 1 55 . 1 1 17 17 LEU N N 15 118.515 0.048 . 1 . . . A 17 LEU N 11 18493 1 56 . 1 1 18 18 MET C C 13 180.469 0.190 . 1 . . . A 18 MET C 16 18493 1 57 . 1 1 18 18 MET CA C 13 60.277 0.110 . 1 . . . A 18 MET CA 18 18493 1 58 . 1 1 18 18 MET CB C 13 31.789 0.165 . 1 . . . A 18 MET CB 7 18493 1 59 . 1 1 18 18 MET CG C 13 33.392 0.223 . 1 . . . A 18 MET CG 10 18493 1 60 . 1 1 18 18 MET N N 15 120.633 0.312 . 1 . . . A 18 MET N 16 18493 1 61 . 1 1 19 19 ALA H H 1 9.398 0.009 . 1 . . . A 19 ALA H 2 18493 1 62 . 1 1 19 19 ALA C C 13 178.210 0.191 . 1 . . . A 19 ALA C 10 18493 1 63 . 1 1 19 19 ALA CA C 13 55.468 0.147 . 1 . . . A 19 ALA CA 17 18493 1 64 . 1 1 19 19 ALA CB C 13 17.865 0.117 . 1 . . . A 19 ALA CB 10 18493 1 65 . 1 1 19 19 ALA N N 15 123.958 0.147 . 1 . . . A 19 ALA N 19 18493 1 66 . 1 1 20 20 PHE C C 13 176.674 0.156 . 1 . . . A 20 PHE C 6 18493 1 67 . 1 1 20 20 PHE CA C 13 62.546 0.197 . 1 . . . A 20 PHE CA 10 18493 1 68 . 1 1 20 20 PHE CB C 13 38.697 0.300 . 1 . . . A 20 PHE CB 1 18493 1 69 . 1 1 20 20 PHE N N 15 118.424 0.290 . 1 . . . A 20 PHE N 11 18493 1 70 . 1 1 21 21 THR C C 13 174.203 0.226 . 1 . . . A 21 THR C 18 18493 1 71 . 1 1 21 21 THR CA C 13 66.052 0.521 . 1 . . . A 21 THR CA 40 18493 1 72 . 1 1 21 21 THR CB C 13 68.956 0.583 . 1 . . . A 21 THR CB 29 18493 1 73 . 1 1 21 21 THR CG2 C 13 22.538 0.082 . 1 . . . A 21 THR CG2 26 18493 1 74 . 1 1 21 21 THR N N 15 109.220 0.236 . 1 . . . A 21 THR N 14 18493 1 75 . 1 1 22 22 ALA C C 13 179.488 0.170 . 1 . . . A 22 ALA C 11 18493 1 76 . 1 1 22 22 ALA CA C 13 54.847 0.162 . 1 . . . A 22 ALA CA 25 18493 1 77 . 1 1 22 22 ALA CB C 13 17.801 0.103 . 1 . . . A 22 ALA CB 15 18493 1 78 . 1 1 22 22 ALA N N 15 123.662 0.232 . 1 . . . A 22 ALA N 17 18493 1 79 . 1 1 23 23 LEU H H 1 8.581 0.094 . 1 . . . A 23 LEU H 3 18493 1 80 . 1 1 23 23 LEU C C 13 178.028 0.137 . 1 . . . A 23 LEU C 10 18493 1 81 . 1 1 23 23 LEU CA C 13 57.713 0.168 . 1 . . . A 23 LEU CA 17 18493 1 82 . 1 1 23 23 LEU CB C 13 41.506 0.071 . 1 . . . A 23 LEU CB 5 18493 1 83 . 1 1 23 23 LEU CG C 13 26.938 0.112 . 1 . . . A 23 LEU CG 6 18493 1 84 . 1 1 23 23 LEU CD1 C 13 22.773 0.114 . 2 . . . A 23 LEU CD1 4 18493 1 85 . 1 1 23 23 LEU CD2 C 13 22.797 0.300 . 2 . . . A 23 LEU CD2 1 18493 1 86 . 1 1 23 23 LEU N N 15 118.917 0.139 . 1 . . . A 23 LEU N 22 18493 1 87 . 1 1 24 24 ALA C C 13 180.617 0.253 . 1 . . . A 24 ALA C 14 18493 1 88 . 1 1 24 24 ALA CA C 13 55.350 0.248 . 1 . . . A 24 ALA CA 22 18493 1 89 . 1 1 24 24 ALA CB C 13 17.583 0.160 . 1 . . . A 24 ALA CB 9 18493 1 90 . 1 1 24 24 ALA N N 15 119.931 0.087 . 1 . . . A 24 ALA N 17 18493 1 91 . 1 1 25 25 LEU H H 1 9.179 0.015 . 1 . . . A 25 LEU H 2 18493 1 92 . 1 1 25 25 LEU CA C 13 58.078 0.174 . 1 . . . A 25 LEU CA 15 18493 1 93 . 1 1 25 25 LEU CB C 13 43.597 0.156 . 1 . . . A 25 LEU CB 6 18493 1 94 . 1 1 25 25 LEU CG C 13 27.151 0.097 . 1 . . . A 25 LEU CG 3 18493 1 95 . 1 1 25 25 LEU CD1 C 13 23.596 0.300 . 2 . . . A 25 LEU CD1 1 18493 1 96 . 1 1 25 25 LEU CD2 C 13 23.596 0.300 . 2 . . . A 25 LEU CD2 1 18493 1 97 . 1 1 25 25 LEU N N 15 119.691 0.306 . 1 . . . A 25 LEU N 18 18493 1 98 . 1 1 26 26 GLU C C 13 179.334 0.247 . 1 . . . A 26 GLU C 5 18493 1 99 . 1 1 26 26 GLU CA C 13 59.584 0.068 . 1 . . . A 26 GLU CA 5 18493 1 100 . 1 1 26 26 GLU CB C 13 27.202 0.136 . 1 . . . A 26 GLU CB 4 18493 1 101 . 1 1 26 26 GLU N N 15 119.651 0.300 . 1 . . . A 26 GLU N 2 18493 1 102 . 1 1 27 27 LEU H H 1 9.410 0.062 . 1 . . . A 27 LEU H 3 18493 1 103 . 1 1 27 27 LEU CA C 13 57.887 0.086 . 1 . . . A 27 LEU CA 8 18493 1 104 . 1 1 27 27 LEU CB C 13 41.591 0.147 . 1 . . . A 27 LEU CB 6 18493 1 105 . 1 1 27 27 LEU CG C 13 27.146 0.010 . 1 . . . A 27 LEU CG 2 18493 1 106 . 1 1 27 27 LEU CD1 C 13 23.581 0.300 . 2 . . . A 27 LEU CD1 1 18493 1 107 . 1 1 27 27 LEU CD2 C 13 23.581 0.300 . 2 . . . A 27 LEU CD2 1 18493 1 108 . 1 1 27 27 LEU N N 15 119.661 0.205 . 1 . . . A 27 LEU N 13 18493 1 109 . 1 1 28 28 THR C C 13 175.898 0.179 . 1 . . . A 28 THR C 4 18493 1 110 . 1 1 28 28 THR CA C 13 67.459 0.166 . 1 . . . A 28 THR CA 14 18493 1 111 . 1 1 28 28 THR CB C 13 67.948 0.178 . 1 . . . A 28 THR CB 5 18493 1 112 . 1 1 28 28 THR CG2 C 13 21.766 0.102 . 1 . . . A 28 THR CG2 6 18493 1 113 . 1 1 28 28 THR N N 15 118.484 0.098 . 1 . . . A 28 THR N 4 18493 1 114 . 1 1 29 29 ALA H H 1 8.302 0.020 . 1 . . . A 29 ALA H 2 18493 1 115 . 1 1 29 29 ALA C C 13 179.717 0.245 . 1 . . . A 29 ALA C 15 18493 1 116 . 1 1 29 29 ALA CA C 13 55.919 0.261 . 1 . . . A 29 ALA CA 24 18493 1 117 . 1 1 29 29 ALA CB C 13 16.837 0.362 . 1 . . . A 29 ALA CB 22 18493 1 118 . 1 1 29 29 ALA N N 15 122.643 0.176 . 1 . . . A 29 ALA N 11 18493 1 119 . 1 1 30 30 LEU H H 1 8.412 0.023 . 1 . . . A 30 LEU H 2 18493 1 120 . 1 1 30 30 LEU C C 13 178.143 0.127 . 1 . . . A 30 LEU C 2 18493 1 121 . 1 1 30 30 LEU CA C 13 57.384 0.150 . 1 . . . A 30 LEU CA 16 18493 1 122 . 1 1 30 30 LEU CB C 13 41.679 0.199 . 1 . . . A 30 LEU CB 5 18493 1 123 . 1 1 30 30 LEU CG C 13 26.482 0.118 . 1 . . . A 30 LEU CG 4 18493 1 124 . 1 1 30 30 LEU CD1 C 13 22.521 0.291 . 2 . . . A 30 LEU CD1 2 18493 1 125 . 1 1 30 30 LEU CD2 C 13 22.812 0.300 . 2 . . . A 30 LEU CD2 1 18493 1 126 . 1 1 30 30 LEU N N 15 117.408 0.101 . 1 . . . A 30 LEU N 23 18493 1 127 . 1 1 31 31 TRP H H 1 9.157 0.012 . 1 . . . A 31 TRP H 2 18493 1 128 . 1 1 31 31 TRP C C 13 179.053 0.300 . 1 . . . A 31 TRP C 1 18493 1 129 . 1 1 31 31 TRP CA C 13 59.005 0.007 . 1 . . . A 31 TRP CA 3 18493 1 130 . 1 1 31 31 TRP CB C 13 28.142 0.036 . 1 . . . A 31 TRP CB 3 18493 1 131 . 1 1 31 31 TRP N N 15 125.692 0.018 . 1 . . . A 31 TRP N 2 18493 1 132 . 1 1 32 32 PHE H H 1 9.374 0.012 . 1 . . . A 32 PHE H 2 18493 1 133 . 1 1 32 32 PHE CA C 13 61.557 0.239 . 1 . . . A 32 PHE CA 3 18493 1 134 . 1 1 32 32 PHE CB C 13 38.384 0.300 . 1 . . . A 32 PHE CB 1 18493 1 135 . 1 1 32 32 PHE N N 15 119.195 0.300 . 1 . . . A 32 PHE N 2 18493 1 136 . 1 1 33 33 GLN C C 13 177.477 0.215 . 1 . . . A 33 GLN C 3 18493 1 137 . 1 1 33 33 GLN CA C 13 56.613 0.300 . 1 . . . A 33 GLN CA 1 18493 1 138 . 1 1 33 33 GLN CB C 13 29.433 0.172 . 1 . . . A 33 GLN CB 3 18493 1 139 . 1 1 34 34 HIS H H 1 9.621 0.026 . 1 . . . A 34 HIS H 3 18493 1 140 . 1 1 34 34 HIS C C 13 175.548 0.282 . 1 . . . A 34 HIS C 2 18493 1 141 . 1 1 34 34 HIS CA C 13 58.733 0.049 . 1 . . . A 34 HIS CA 3 18493 1 142 . 1 1 34 34 HIS CB C 13 32.084 0.437 . 1 . . . A 34 HIS CB 4 18493 1 143 . 1 1 34 34 HIS CG C 13 137.404 2.253 . 1 . . . A 34 HIS CG 7 18493 1 144 . 1 1 34 34 HIS CD2 C 13 117.518 0.108 . 1 . . . A 34 HIS CD2 7 18493 1 145 . 1 1 34 34 HIS CE1 C 13 139.690 0.204 . 1 . . . A 34 HIS CE1 4 18493 1 146 . 1 1 34 34 HIS N N 15 115.948 0.073 . 1 . . . A 34 HIS N 3 18493 1 147 . 1 1 35 35 VAL C C 13 177.853 0.300 . 1 . . . A 35 VAL C 1 18493 1 148 . 1 1 35 35 VAL CA C 13 64.075 0.169 . 1 . . . A 35 VAL CA 9 18493 1 149 . 1 1 35 35 VAL CB C 13 30.626 0.051 . 1 . . . A 35 VAL CB 2 18493 1 150 . 1 1 35 35 VAL CG2 C 13 21.112 0.079 . 2 . . . A 35 VAL CG2 5 18493 1 151 . 1 1 35 35 VAL N N 15 116.902 0.004 . 1 . . . A 35 VAL N 3 18493 1 152 . 1 1 36 36 MET H H 1 7.605 0.034 . 1 . . . A 36 MET H 3 18493 1 153 . 1 1 36 36 MET C C 13 175.905 0.300 . 1 . . . A 36 MET C 1 18493 1 154 . 1 1 36 36 MET N N 15 114.145 0.036 . 1 . . . A 36 MET N 2 18493 1 155 . 1 1 37 37 LEU H H 1 7.121 0.026 . 1 . . . A 37 LEU H 3 18493 1 156 . 1 1 37 37 LEU N N 15 111.740 0.034 . 1 . . . A 37 LEU N 4 18493 1 157 . 1 1 38 38 LEU C C 13 176.457 0.300 . 1 . . . A 38 LEU C 1 18493 1 158 . 1 1 39 39 LYS H H 1 9.359 0.022 . 1 . . . A 39 LYS H 3 18493 1 159 . 1 1 39 39 LYS CA C 13 57.471 0.300 . 1 . . . A 39 LYS CA 1 18493 1 160 . 1 1 39 39 LYS N N 15 121.418 0.022 . 1 . . . A 39 LYS N 3 18493 1 161 . 1 1 40 40 PRO CA C 13 60.451 0.300 . 1 . . . A 40 PRO CA 1 18493 1 162 . 1 1 40 40 PRO CD C 13 51.590 0.244 . 1 . . . A 40 PRO CD 4 18493 1 163 . 1 1 42 42 VAL C C 13 179.261 0.126 . 1 . . . A 42 VAL C 4 18493 1 164 . 1 1 42 42 VAL CA C 13 67.223 0.316 . 1 . . . A 42 VAL CA 3 18493 1 165 . 1 1 42 42 VAL CB C 13 30.941 0.262 . 1 . . . A 42 VAL CB 2 18493 1 166 . 1 1 42 42 VAL CG1 C 13 23.413 0.300 . 2 . . . A 42 VAL CG1 1 18493 1 167 . 1 1 42 42 VAL CG2 C 13 21.922 0.300 . 2 . . . A 42 VAL CG2 1 18493 1 168 . 1 1 42 42 VAL N N 15 118.166 0.021 . 1 . . . A 42 VAL N 2 18493 1 169 . 1 1 43 43 LEU C C 13 178.293 0.388 . 1 . . . A 43 LEU C 8 18493 1 170 . 1 1 43 43 LEU CA C 13 57.129 0.094 . 1 . . . A 43 LEU CA 3 18493 1 171 . 1 1 43 43 LEU CB C 13 41.030 0.300 . 1 . . . A 43 LEU CB 1 18493 1 172 . 1 1 43 43 LEU CG C 13 26.666 0.153 . 1 . . . A 43 LEU CG 2 18493 1 173 . 1 1 43 43 LEU CD1 C 13 21.873 0.300 . 2 . . . A 43 LEU CD1 1 18493 1 174 . 1 1 43 43 LEU CD2 C 13 21.866 0.300 . 2 . . . A 43 LEU CD2 1 18493 1 175 . 1 1 43 43 LEU N N 15 115.946 0.075 . 1 . . . A 43 LEU N 4 18493 1 176 . 1 1 44 44 CYS H H 1 7.683 0.032 . 1 . . . A 44 CYS H 2 18493 1 177 . 1 1 44 44 CYS C C 13 177.484 0.210 . 1 . . . A 44 CYS C 7 18493 1 178 . 1 1 44 44 CYS CA C 13 59.760 0.793 . 1 . . . A 44 CYS CA 13 18493 1 179 . 1 1 44 44 CYS CB C 13 30.651 2.786 . 1 . . . A 44 CYS CB 4 18493 1 180 . 1 1 44 44 CYS N N 15 115.006 0.814 . 1 . . . A 44 CYS N 17 18493 1 181 . 1 1 45 45 ILE C C 13 179.575 0.247 . 1 . . . A 45 ILE C 6 18493 1 182 . 1 1 45 45 ILE CA C 13 62.068 0.136 . 1 . . . A 45 ILE CA 14 18493 1 183 . 1 1 45 45 ILE CB C 13 33.583 0.345 . 1 . . . A 45 ILE CB 12 18493 1 184 . 1 1 45 45 ILE CG1 C 13 25.847 0.024 . 1 . . . A 45 ILE CG1 4 18493 1 185 . 1 1 45 45 ILE CG2 C 13 19.220 0.032 . 1 . . . A 45 ILE CG2 4 18493 1 186 . 1 1 45 45 ILE CD1 C 13 8.010 0.069 . 1 . . . A 45 ILE CD1 40 18493 1 187 . 1 1 45 45 ILE N N 15 119.384 1.920 . 1 . . . A 45 ILE N 5 18493 1 188 . 1 1 46 46 TYR H H 1 8.958 0.053 . 1 . . . A 46 TYR H 3 18493 1 189 . 1 1 46 46 TYR C C 13 178.397 0.035 . 1 . . . A 46 TYR C 2 18493 1 190 . 1 1 46 46 TYR CA C 13 59.129 0.181 . 1 . . . A 46 TYR CA 3 18493 1 191 . 1 1 46 46 TYR CB C 13 35.347 0.300 . 1 . . . A 46 TYR CB 1 18493 1 192 . 1 1 46 46 TYR N N 15 120.126 0.331 . 1 . . . A 46 TYR N 8 18493 1 193 . 1 1 47 47 GLU H H 1 9.681 0.005 . 1 . . . A 47 GLU H 2 18493 1 194 . 1 1 47 47 GLU C C 13 179.907 0.129 . 1 . . . A 47 GLU C 6 18493 1 195 . 1 1 47 47 GLU CA C 13 57.985 0.177 . 1 . . . A 47 GLU CA 5 18493 1 196 . 1 1 47 47 GLU CB C 13 27.290 0.033 . 1 . . . A 47 GLU CB 2 18493 1 197 . 1 1 47 47 GLU CG C 13 34.938 0.029 . 1 . . . A 47 GLU CG 2 18493 1 198 . 1 1 47 47 GLU N N 15 121.779 0.043 . 1 . . . A 47 GLU N 4 18493 1 199 . 1 1 48 48 ARG H H 1 9.213 0.020 . 1 . . . A 48 ARG H 2 18493 1 200 . 1 1 48 48 ARG C C 13 181.638 0.106 . 1 . . . A 48 ARG C 5 18493 1 201 . 1 1 48 48 ARG CA C 13 60.299 0.257 . 1 . . . A 48 ARG CA 16 18493 1 202 . 1 1 48 48 ARG CB C 13 30.167 0.112 . 1 . . . A 48 ARG CB 7 18493 1 203 . 1 1 48 48 ARG CG C 13 27.511 0.135 . 1 . . . A 48 ARG CG 8 18493 1 204 . 1 1 48 48 ARG CD C 13 44.371 0.055 . 1 . . . A 48 ARG CD 6 18493 1 205 . 1 1 48 48 ARG N N 15 119.188 0.232 . 1 . . . A 48 ARG N 13 18493 1 206 . 1 1 49 49 VAL C C 13 177.326 0.183 . 1 . . . A 49 VAL C 9 18493 1 207 . 1 1 49 49 VAL CA C 13 66.624 0.188 . 1 . . . A 49 VAL CA 4 18493 1 208 . 1 1 49 49 VAL CB C 13 31.280 0.211 . 1 . . . A 49 VAL CB 3 18493 1 209 . 1 1 49 49 VAL CG1 C 13 23.674 0.635 . 2 . . . A 49 VAL CG1 2 18493 1 210 . 1 1 49 49 VAL CG2 C 13 22.427 0.073 . 2 . . . A 49 VAL CG2 2 18493 1 211 . 1 1 49 49 VAL N N 15 121.326 0.053 . 1 . . . A 49 VAL N 4 18493 1 212 . 1 1 50 50 ALA C C 13 179.594 0.173 . 1 . . . A 50 ALA C 10 18493 1 213 . 1 1 50 50 ALA CA C 13 55.902 0.277 . 1 . . . A 50 ALA CA 13 18493 1 214 . 1 1 50 50 ALA CB C 13 16.623 0.162 . 1 . . . A 50 ALA CB 7 18493 1 215 . 1 1 50 50 ALA N N 15 122.955 0.356 . 1 . . . A 50 ALA N 11 18493 1 216 . 1 1 51 51 LEU C C 13 177.990 0.294 . 1 . . . A 51 LEU C 7 18493 1 217 . 1 1 51 51 LEU CA C 13 57.285 0.176 . 1 . . . A 51 LEU CA 14 18493 1 218 . 1 1 51 51 LEU CB C 13 41.369 0.192 . 1 . . . A 51 LEU CB 5 18493 1 219 . 1 1 51 51 LEU CG C 13 26.330 0.171 . 1 . . . A 51 LEU CG 2 18493 1 220 . 1 1 51 51 LEU CD1 C 13 21.941 0.300 . 2 . . . A 51 LEU CD1 1 18493 1 221 . 1 1 51 51 LEU CD2 C 13 21.771 0.300 . 2 . . . A 51 LEU CD2 1 18493 1 222 . 1 1 51 51 LEU N N 15 115.737 0.292 . 1 . . . A 51 LEU N 13 18493 1 223 . 1 1 52 52 PHE H H 1 8.863 0.012 . 1 . . . A 52 PHE H 2 18493 1 224 . 1 1 52 52 PHE C C 13 179.142 0.183 . 1 . . . A 52 PHE C 8 18493 1 225 . 1 1 52 52 PHE CA C 13 62.518 0.122 . 1 . . . A 52 PHE CA 9 18493 1 226 . 1 1 52 52 PHE CB C 13 38.538 0.270 . 1 . . . A 52 PHE CB 2 18493 1 227 . 1 1 52 52 PHE N N 15 122.707 0.169 . 1 . . . A 52 PHE N 10 18493 1 228 . 1 1 53 53 GLY H H 1 9.027 0.010 . 1 . . . A 53 GLY H 2 18493 1 229 . 1 1 53 53 GLY C C 13 175.378 0.225 . 1 . . . A 53 GLY C 15 18493 1 230 . 1 1 53 53 GLY CA C 13 48.024 0.224 . 1 . . . A 53 GLY CA 24 18493 1 231 . 1 1 53 53 GLY N N 15 110.801 0.218 . 1 . . . A 53 GLY N 16 18493 1 232 . 1 1 54 54 VAL H H 1 7.948 0.031 . 1 . . . A 54 VAL H 2 18493 1 233 . 1 1 54 54 VAL C C 13 177.035 0.204 . 1 . . . A 54 VAL C 11 18493 1 234 . 1 1 54 54 VAL CA C 13 67.448 0.162 . 1 . . . A 54 VAL CA 25 18493 1 235 . 1 1 54 54 VAL CB C 13 31.246 0.206 . 1 . . . A 54 VAL CB 10 18493 1 236 . 1 1 54 54 VAL CG1 C 13 22.269 0.108 . 2 . . . A 54 VAL CG1 11 18493 1 237 . 1 1 54 54 VAL CG2 C 13 21.012 0.177 . 2 . . . A 54 VAL CG2 8 18493 1 238 . 1 1 54 54 VAL N N 15 121.926 0.158 . 1 . . . A 54 VAL N 23 18493 1 239 . 1 1 55 55 LEU H H 1 8.646 0.011 . 1 . . . A 55 LEU H 2 18493 1 240 . 1 1 55 55 LEU C C 13 178.175 0.460 . 1 . . . A 55 LEU C 5 18493 1 241 . 1 1 55 55 LEU CA C 13 58.490 0.316 . 1 . . . A 55 LEU CA 9 18493 1 242 . 1 1 55 55 LEU CB C 13 42.145 0.159 . 1 . . . A 55 LEU CB 7 18493 1 243 . 1 1 55 55 LEU CG C 13 27.014 0.300 . 1 . . . A 55 LEU CG 1 18493 1 244 . 1 1 55 55 LEU CD1 C 13 25.695 0.248 . 2 . . . A 55 LEU CD1 2 18493 1 245 . 1 1 55 55 LEU CD2 C 13 25.376 0.300 . 2 . . . A 55 LEU CD2 1 18493 1 246 . 1 1 55 55 LEU N N 15 119.894 0.170 . 1 . . . A 55 LEU N 16 18493 1 247 . 1 1 56 56 GLY C C 13 174.618 0.131 . 1 . . . A 56 GLY C 14 18493 1 248 . 1 1 56 56 GLY CA C 13 47.533 0.198 . 1 . . . A 56 GLY CA 28 18493 1 249 . 1 1 56 56 GLY N N 15 106.262 0.109 . 1 . . . A 56 GLY N 12 18493 1 250 . 1 1 57 57 ALA C C 13 178.688 0.218 . 1 . . . A 57 ALA C 13 18493 1 251 . 1 1 57 57 ALA CA C 13 55.548 0.187 . 1 . . . A 57 ALA CA 23 18493 1 252 . 1 1 57 57 ALA CB C 13 18.065 0.120 . 1 . . . A 57 ALA CB 17 18493 1 253 . 1 1 57 57 ALA N N 15 123.002 0.111 . 1 . . . A 57 ALA N 13 18493 1 254 . 1 1 58 58 ALA H H 1 8.674 0.003 . 1 . . . A 58 ALA H 2 18493 1 255 . 1 1 58 58 ALA C C 13 179.348 0.158 . 1 . . . A 58 ALA C 13 18493 1 256 . 1 1 58 58 ALA CA C 13 54.763 0.258 . 1 . . . A 58 ALA CA 18 18493 1 257 . 1 1 58 58 ALA CB C 13 17.898 0.175 . 1 . . . A 58 ALA CB 13 18493 1 258 . 1 1 58 58 ALA N N 15 118.866 0.161 . 1 . . . A 58 ALA N 17 18493 1 259 . 1 1 59 59 LEU C C 13 177.654 0.300 . 1 . . . A 59 LEU C 1 18493 1 260 . 1 1 59 59 LEU CA C 13 57.387 0.155 . 1 . . . A 59 LEU CA 14 18493 1 261 . 1 1 59 59 LEU CB C 13 41.209 0.158 . 1 . . . A 59 LEU CB 10 18493 1 262 . 1 1 59 59 LEU CG C 13 26.283 0.075 . 1 . . . A 59 LEU CG 3 18493 1 263 . 1 1 59 59 LEU CD1 C 13 21.815 0.300 . 2 . . . A 59 LEU CD1 1 18493 1 264 . 1 1 59 59 LEU CD2 C 13 21.744 0.300 . 2 . . . A 59 LEU CD2 1 18493 1 265 . 1 1 59 59 LEU N N 15 115.384 0.135 . 1 . . . A 59 LEU N 20 18493 1 266 . 1 1 60 60 ILE C C 13 180.024 0.233 . 1 . . . A 60 ILE C 10 18493 1 267 . 1 1 60 60 ILE CA C 13 64.263 0.278 . 1 . . . A 60 ILE CA 25 18493 1 268 . 1 1 60 60 ILE CB C 13 37.240 0.208 . 1 . . . A 60 ILE CB 16 18493 1 269 . 1 1 60 60 ILE CG1 C 13 29.859 0.184 . 1 . . . A 60 ILE CG1 10 18493 1 270 . 1 1 60 60 ILE CG2 C 13 16.881 0.091 . 1 . . . A 60 ILE CG2 11 18493 1 271 . 1 1 60 60 ILE CD1 C 13 13.606 0.125 . 1 . . . A 60 ILE CD1 9 18493 1 272 . 1 1 60 60 ILE N N 15 116.140 0.148 . 1 . . . A 60 ILE N 7 18493 1 273 . 1 1 61 61 GLY H H 1 9.046 0.002 . 1 . . . A 61 GLY H 2 18493 1 274 . 1 1 61 61 GLY C C 13 173.716 0.189 . 1 . . . A 61 GLY C 13 18493 1 275 . 1 1 61 61 GLY CA C 13 45.617 0.114 . 1 . . . A 61 GLY CA 23 18493 1 276 . 1 1 61 61 GLY N N 15 110.127 0.293 . 1 . . . A 61 GLY N 17 18493 1 277 . 1 1 62 62 ALA H H 1 8.066 0.012 . 1 . . . A 62 ALA H 2 18493 1 278 . 1 1 62 62 ALA C C 13 176.192 0.092 . 1 . . . A 62 ALA C 3 18493 1 279 . 1 1 62 62 ALA CA C 13 53.268 0.146 . 1 . . . A 62 ALA CA 25 18493 1 280 . 1 1 62 62 ALA CB C 13 19.138 0.103 . 1 . . . A 62 ALA CB 12 18493 1 281 . 1 1 62 62 ALA N N 15 118.949 0.237 . 1 . . . A 62 ALA N 15 18493 1 282 . 1 1 63 63 ILE CA C 13 66.739 0.151 . 1 . . . A 63 ILE CA 15 18493 1 283 . 1 1 63 63 ILE CB C 13 37.947 0.160 . 1 . . . A 63 ILE CB 19 18493 1 284 . 1 1 63 63 ILE CG1 C 13 29.043 0.468 . 1 . . . A 63 ILE CG1 4 18493 1 285 . 1 1 63 63 ILE CG2 C 13 16.921 0.191 . 1 . . . A 63 ILE CG2 10 18493 1 286 . 1 1 63 63 ILE CD1 C 13 14.543 0.153 . 1 . . . A 63 ILE CD1 8 18493 1 287 . 1 1 63 63 ILE N N 15 116.800 0.227 . 1 . . . A 63 ILE N 4 18493 1 288 . 1 1 64 64 ALA CA C 13 52.934 0.136 . 1 . . . A 64 ALA CA 5 18493 1 289 . 1 1 64 64 ALA CB C 13 19.428 0.300 . 1 . . . A 64 ALA CB 1 18493 1 290 . 1 1 64 64 ALA N N 15 123.957 0.300 . 1 . . . A 64 ALA N 1 18493 1 291 . 1 1 65 65 PRO CA C 13 65.350 0.030 . 1 . . . A 65 PRO CA 2 18493 1 292 . 1 1 65 65 PRO CG C 13 27.611 0.063 . 1 . . . A 65 PRO CG 2 18493 1 293 . 1 1 65 65 PRO CD C 13 51.485 0.275 . 1 . . . A 65 PRO CD 5 18493 1 294 . 1 1 65 65 PRO N N 15 128.226 0.174 . 1 . . . A 65 PRO N 4 18493 1 295 . 1 1 66 66 LYS C C 13 177.500 0.300 . 1 . . . A 66 LYS C 1 18493 1 296 . 1 1 66 66 LYS CA C 13 56.547 0.110 . 1 . . . A 66 LYS CA 3 18493 1 297 . 1 1 66 66 LYS CB C 13 30.522 0.300 . 1 . . . A 66 LYS CB 1 18493 1 298 . 1 1 66 66 LYS CE C 13 42.222 0.076 . 1 . . . A 66 LYS CE 2 18493 1 299 . 1 1 66 66 LYS N N 15 116.618 0.155 . 1 . . . A 66 LYS N 2 18493 1 300 . 1 1 67 67 THR CA C 13 60.452 0.240 . 1 . . . A 67 THR CA 10 18493 1 301 . 1 1 67 67 THR CB C 13 69.948 0.041 . 1 . . . A 67 THR CB 8 18493 1 302 . 1 1 67 67 THR CG2 C 13 21.879 0.061 . 1 . . . A 67 THR CG2 10 18493 1 303 . 1 1 68 68 PRO C C 13 177.070 0.300 . 1 . . . A 68 PRO C 1 18493 1 304 . 1 1 68 68 PRO CA C 13 63.315 0.033 . 1 . . . A 68 PRO CA 2 18493 1 305 . 1 1 68 68 PRO CB C 13 32.458 0.117 . 1 . . . A 68 PRO CB 3 18493 1 306 . 1 1 68 68 PRO CG C 13 28.010 0.008 . 1 . . . A 68 PRO CG 2 18493 1 307 . 1 1 68 68 PRO CD C 13 51.735 0.207 . 1 . . . A 68 PRO CD 6 18493 1 308 . 1 1 68 68 PRO N N 15 129.713 0.223 . 1 . . . A 68 PRO N 3 18493 1 309 . 1 1 69 69 LEU H H 1 8.882 0.010 . 1 . . . A 69 LEU H 2 18493 1 310 . 1 1 69 69 LEU C C 13 179.448 0.164 . 1 . . . A 69 LEU C 6 18493 1 311 . 1 1 69 69 LEU CA C 13 57.389 0.300 . 1 . . . A 69 LEU CA 1 18493 1 312 . 1 1 69 69 LEU CB C 13 42.737 0.300 . 1 . . . A 69 LEU CB 1 18493 1 313 . 1 1 69 69 LEU CG C 13 26.295 0.300 . 1 . . . A 69 LEU CG 1 18493 1 314 . 1 1 69 69 LEU CD1 C 13 23.591 0.300 . 2 . . . A 69 LEU CD1 1 18493 1 315 . 1 1 69 69 LEU CD2 C 13 23.617 0.300 . 2 . . . A 69 LEU CD2 1 18493 1 316 . 1 1 69 69 LEU N N 15 121.517 0.015 . 1 . . . A 69 LEU N 2 18493 1 317 . 1 1 70 70 ARG H H 1 8.202 0.037 . 1 . . . A 70 ARG H 3 18493 1 318 . 1 1 70 70 ARG C C 13 177.925 0.300 . 1 . . . A 70 ARG C 1 18493 1 319 . 1 1 70 70 ARG CA C 13 58.429 0.227 . 1 . . . A 70 ARG CA 11 18493 1 320 . 1 1 70 70 ARG CB C 13 29.391 0.149 . 1 . . . A 70 ARG CB 3 18493 1 321 . 1 1 70 70 ARG CG C 13 26.748 0.071 . 1 . . . A 70 ARG CG 6 18493 1 322 . 1 1 70 70 ARG CD C 13 44.579 0.104 . 1 . . . A 70 ARG CD 11 18493 1 323 . 1 1 70 70 ARG CZ C 13 159.739 0.300 . 1 . . . A 70 ARG CZ 1 18493 1 324 . 1 1 70 70 ARG N N 15 114.028 0.148 . 1 . . . A 70 ARG N 9 18493 1 325 . 1 1 71 71 TYR H H 1 8.136 0.015 . 1 . . . A 71 TYR H 2 18493 1 326 . 1 1 71 71 TYR CA C 13 57.374 0.092 . 1 . . . A 71 TYR CA 3 18493 1 327 . 1 1 71 71 TYR N N 15 121.740 0.015 . 1 . . . A 71 TYR N 2 18493 1 328 . 1 1 72 72 VAL C C 13 177.702 0.132 . 1 . . . A 72 VAL C 13 18493 1 329 . 1 1 72 72 VAL CA C 13 66.098 0.174 . 1 . . . A 72 VAL CA 22 18493 1 330 . 1 1 72 72 VAL CB C 13 31.343 0.089 . 1 . . . A 72 VAL CB 7 18493 1 331 . 1 1 72 72 VAL CG1 C 13 22.760 0.073 . 2 . . . A 72 VAL CG1 6 18493 1 332 . 1 1 72 72 VAL CG2 C 13 21.150 0.404 . 2 . . . A 72 VAL CG2 12 18493 1 333 . 1 1 72 72 VAL N N 15 118.416 0.293 . 1 . . . A 72 VAL N 6 18493 1 334 . 1 1 73 73 ALA H H 1 9.015 0.030 . 1 . . . A 73 ALA H 3 18493 1 335 . 1 1 73 73 ALA C C 13 179.763 0.155 . 1 . . . A 73 ALA C 10 18493 1 336 . 1 1 73 73 ALA CA C 13 55.785 0.150 . 1 . . . A 73 ALA CA 31 18493 1 337 . 1 1 73 73 ALA CB C 13 19.265 0.132 . 1 . . . A 73 ALA CB 17 18493 1 338 . 1 1 73 73 ALA N N 15 120.283 0.342 . 1 . . . A 73 ALA N 20 18493 1 339 . 1 1 74 74 MET H H 1 8.163 0.008 . 1 . . . A 74 MET H 2 18493 1 340 . 1 1 74 74 MET C C 13 177.223 0.236 . 1 . . . A 74 MET C 12 18493 1 341 . 1 1 74 74 MET CA C 13 61.023 0.161 . 1 . . . A 74 MET CA 16 18493 1 342 . 1 1 74 74 MET CB C 13 33.777 0.092 . 1 . . . A 74 MET CB 3 18493 1 343 . 1 1 74 74 MET CG C 13 35.778 0.203 . 1 . . . A 74 MET CG 6 18493 1 344 . 1 1 74 74 MET N N 15 115.547 0.203 . 1 . . . A 74 MET N 14 18493 1 345 . 1 1 75 75 VAL H H 1 7.554 0.034 . 1 . . . A 75 VAL H 2 18493 1 346 . 1 1 75 75 VAL C C 13 177.166 0.124 . 1 . . . A 75 VAL C 5 18493 1 347 . 1 1 75 75 VAL CA C 13 67.581 0.250 . 1 . . . A 75 VAL CA 13 18493 1 348 . 1 1 75 75 VAL CB C 13 31.408 0.100 . 1 . . . A 75 VAL CB 4 18493 1 349 . 1 1 75 75 VAL CG1 C 13 23.448 0.034 . 2 . . . A 75 VAL CG1 4 18493 1 350 . 1 1 75 75 VAL CG2 C 13 21.778 0.300 . 2 . . . A 75 VAL CG2 1 18493 1 351 . 1 1 75 75 VAL N N 15 118.690 0.254 . 1 . . . A 75 VAL N 16 18493 1 352 . 1 1 76 76 ILE C C 13 178.680 0.168 . 1 . . . A 76 ILE C 11 18493 1 353 . 1 1 76 76 ILE CA C 13 65.839 0.221 . 1 . . . A 76 ILE CA 23 18493 1 354 . 1 1 76 76 ILE CB C 13 38.414 0.257 . 1 . . . A 76 ILE CB 9 18493 1 355 . 1 1 76 76 ILE CG1 C 13 31.176 0.211 . 1 . . . A 76 ILE CG1 7 18493 1 356 . 1 1 76 76 ILE CG2 C 13 17.003 0.122 . 1 . . . A 76 ILE CG2 8 18493 1 357 . 1 1 76 76 ILE CD1 C 13 14.703 0.196 . 1 . . . A 76 ILE CD1 3 18493 1 358 . 1 1 76 76 ILE N N 15 118.959 0.210 . 1 . . . A 76 ILE N 13 18493 1 359 . 1 1 77 77 TRP H H 1 9.515 0.015 . 1 . . . A 77 TRP H 2 18493 1 360 . 1 1 77 77 TRP C C 13 177.153 0.135 . 1 . . . A 77 TRP C 8 18493 1 361 . 1 1 77 77 TRP CA C 13 58.779 0.111 . 1 . . . A 77 TRP CA 12 18493 1 362 . 1 1 77 77 TRP CB C 13 30.494 0.281 . 1 . . . A 77 TRP CB 11 18493 1 363 . 1 1 77 77 TRP CG C 13 114.126 0.300 . 1 . . . A 77 TRP CG 1 18493 1 364 . 1 1 77 77 TRP CD1 C 13 122.582 0.300 . 4 . . . A 77 TRP CD1 1 18493 1 365 . 1 1 77 77 TRP N N 15 125.440 0.096 . 1 . . . A 77 TRP N 17 18493 1 366 . 1 1 78 78 LEU H H 1 9.367 0.005 . 1 . . . A 78 LEU H 2 18493 1 367 . 1 1 78 78 LEU C C 13 178.381 0.099 . 1 . . . A 78 LEU C 5 18493 1 368 . 1 1 78 78 LEU CA C 13 58.041 0.256 . 1 . . . A 78 LEU CA 9 18493 1 369 . 1 1 78 78 LEU CB C 13 43.807 0.230 . 1 . . . A 78 LEU CB 6 18493 1 370 . 1 1 78 78 LEU CG C 13 27.131 0.216 . 1 . . . A 78 LEU CG 4 18493 1 371 . 1 1 78 78 LEU CD1 C 13 23.311 0.300 . 2 . . . A 78 LEU CD1 1 18493 1 372 . 1 1 78 78 LEU CD2 C 13 23.168 0.300 . 2 . . . A 78 LEU CD2 1 18493 1 373 . 1 1 78 78 LEU N N 15 118.968 0.194 . 1 . . . A 78 LEU N 13 18493 1 374 . 1 1 79 79 TYR C C 13 176.777 0.210 . 1 . . . A 79 TYR C 5 18493 1 375 . 1 1 79 79 TYR CA C 13 62.849 0.235 . 1 . . . A 79 TYR CA 3 18493 1 376 . 1 1 79 79 TYR N N 15 118.181 0.222 . 1 . . . A 79 TYR N 6 18493 1 377 . 1 1 80 80 SER C C 13 175.943 0.092 . 1 . . . A 80 SER C 8 18493 1 378 . 1 1 80 80 SER CA C 13 63.515 0.093 . 1 . . . A 80 SER CA 15 18493 1 379 . 1 1 80 80 SER CB C 13 63.941 0.300 . 1 . . . A 80 SER CB 1 18493 1 380 . 1 1 80 80 SER N N 15 114.286 0.173 . 1 . . . A 80 SER N 8 18493 1 381 . 1 1 81 81 ALA C C 13 178.208 0.148 . 1 . . . A 81 ALA C 4 18493 1 382 . 1 1 81 81 ALA CA C 13 55.224 0.139 . 1 . . . A 81 ALA CA 18 18493 1 383 . 1 1 81 81 ALA CB C 13 17.897 0.096 . 1 . . . A 81 ALA CB 9 18493 1 384 . 1 1 81 81 ALA N N 15 121.070 0.164 . 1 . . . A 81 ALA N 11 18493 1 385 . 1 1 82 82 PHE C C 13 176.975 0.033 . 1 . . . A 82 PHE C 2 18493 1 386 . 1 1 82 82 PHE CA C 13 62.132 0.255 . 1 . . . A 82 PHE CA 6 18493 1 387 . 1 1 82 82 PHE CB C 13 38.497 0.300 . 1 . . . A 82 PHE CB 1 18493 1 388 . 1 1 82 82 PHE N N 15 117.560 0.068 . 1 . . . A 82 PHE N 5 18493 1 389 . 1 1 83 83 ARG C C 13 178.637 0.085 . 1 . . . A 83 ARG C 7 18493 1 390 . 1 1 83 83 ARG CA C 13 60.291 0.584 . 1 . . . A 83 ARG CA 10 18493 1 391 . 1 1 83 83 ARG CB C 13 28.625 0.036 . 1 . . . A 83 ARG CB 2 18493 1 392 . 1 1 83 83 ARG CG C 13 26.715 0.649 . 1 . . . A 83 ARG CG 2 18493 1 393 . 1 1 83 83 ARG CD C 13 43.764 0.100 . 1 . . . A 83 ARG CD 2 18493 1 394 . 1 1 83 83 ARG N N 15 117.110 0.185 . 1 . . . A 83 ARG N 3 18493 1 395 . 1 1 84 84 GLY C C 13 177.091 0.256 . 1 . . . A 84 GLY C 9 18493 1 396 . 1 1 84 84 GLY CA C 13 46.128 0.261 . 1 . . . A 84 GLY CA 13 18493 1 397 . 1 1 84 84 GLY N N 15 105.915 0.270 . 1 . . . A 84 GLY N 11 18493 1 398 . 1 1 85 85 VAL C C 13 176.387 0.304 . 1 . . . A 85 VAL C 6 18493 1 399 . 1 1 85 85 VAL CA C 13 66.960 0.198 . 1 . . . A 85 VAL CA 16 18493 1 400 . 1 1 85 85 VAL CB C 13 31.066 0.289 . 1 . . . A 85 VAL CB 5 18493 1 401 . 1 1 85 85 VAL CG1 C 13 23.638 0.278 . 2 . . . A 85 VAL CG1 4 18493 1 402 . 1 1 85 85 VAL CG2 C 13 21.858 0.069 . 2 . . . A 85 VAL CG2 4 18493 1 403 . 1 1 85 85 VAL N N 15 124.985 0.240 . 1 . . . A 85 VAL N 13 18493 1 404 . 1 1 86 86 GLN C C 13 179.586 0.523 . 1 . . . A 86 GLN C 2 18493 1 405 . 1 1 86 86 GLN CA C 13 59.505 0.113 . 1 . . . A 86 GLN CA 3 18493 1 406 . 1 1 86 86 GLN CB C 13 28.762 0.269 . 1 . . . A 86 GLN CB 4 18493 1 407 . 1 1 86 86 GLN CG C 13 34.909 0.059 . 1 . . . A 86 GLN CG 2 18493 1 408 . 1 1 86 86 GLN N N 15 116.522 0.164 . 1 . . . A 86 GLN N 5 18493 1 409 . 1 1 87 87 LEU H H 1 8.955 0.025 . 1 . . . A 87 LEU H 2 18493 1 410 . 1 1 87 87 LEU C C 13 178.396 0.357 . 1 . . . A 87 LEU C 4 18493 1 411 . 1 1 87 87 LEU CA C 13 57.847 0.244 . 1 . . . A 87 LEU CA 8 18493 1 412 . 1 1 87 87 LEU CB C 13 41.924 0.206 . 1 . . . A 87 LEU CB 4 18493 1 413 . 1 1 87 87 LEU CG C 13 26.767 0.247 . 1 . . . A 87 LEU CG 2 18493 1 414 . 1 1 87 87 LEU CD1 C 13 23.627 0.300 . 2 . . . A 87 LEU CD1 1 18493 1 415 . 1 1 87 87 LEU CD2 C 13 23.596 0.300 . 2 . . . A 87 LEU CD2 1 18493 1 416 . 1 1 87 87 LEU N N 15 121.211 0.179 . 1 . . . A 87 LEU N 7 18493 1 417 . 1 1 88 88 THR H H 1 8.764 0.046 . 1 . . . A 88 THR H 2 18493 1 418 . 1 1 88 88 THR C C 13 180.013 0.300 . 1 . . . A 88 THR C 1 18493 1 419 . 1 1 88 88 THR CA C 13 65.112 0.115 . 1 . . . A 88 THR CA 16 18493 1 420 . 1 1 88 88 THR CB C 13 68.805 0.088 . 1 . . . A 88 THR CB 13 18493 1 421 . 1 1 88 88 THR CG2 C 13 24.796 0.115 . 1 . . . A 88 THR CG2 14 18493 1 422 . 1 1 88 88 THR N N 15 108.251 0.245 . 1 . . . A 88 THR N 6 18493 1 423 . 1 1 89 89 TYR H H 1 9.868 0.002 . 1 . . . A 89 TYR H 2 18493 1 424 . 1 1 89 89 TYR C C 13 177.244 0.300 . 1 . . . A 89 TYR C 1 18493 1 425 . 1 1 89 89 TYR N N 15 127.947 0.039 . 1 . . . A 89 TYR N 2 18493 1 426 . 1 1 90 90 GLU H H 1 8.515 0.020 . 1 . . . A 90 GLU H 2 18493 1 427 . 1 1 90 90 GLU C C 13 178.671 0.348 . 1 . . . A 90 GLU C 2 18493 1 428 . 1 1 90 90 GLU N N 15 121.163 0.032 . 1 . . . A 90 GLU N 2 18493 1 429 . 1 1 91 91 HIS H H 1 9.102 0.008 . 1 . . . A 91 HIS H 3 18493 1 430 . 1 1 91 91 HIS C C 13 177.605 0.067 . 1 . . . A 91 HIS C 5 18493 1 431 . 1 1 91 91 HIS CA C 13 57.085 0.057 . 1 . . . A 91 HIS CA 6 18493 1 432 . 1 1 91 91 HIS CB C 13 34.128 0.104 . 1 . . . A 91 HIS CB 3 18493 1 433 . 1 1 91 91 HIS CG C 13 136.131 0.120 . 1 . . . A 91 HIS CG 6 18493 1 434 . 1 1 91 91 HIS CD2 C 13 113.845 0.059 . 1 . . . A 91 HIS CD2 5 18493 1 435 . 1 1 91 91 HIS CE1 C 13 141.123 0.064 . 1 . . . A 91 HIS CE1 5 18493 1 436 . 1 1 91 91 HIS N N 15 120.459 0.180 . 1 . . . A 91 HIS N 5 18493 1 437 . 1 1 92 92 THR H H 1 9.550 0.009 . 1 . . . A 92 THR H 2 18493 1 438 . 1 1 92 92 THR C C 13 176.189 0.300 . 1 . . . A 92 THR C 1 18493 1 439 . 1 1 92 92 THR CA C 13 67.058 0.205 . 1 . . . A 92 THR CA 4 18493 1 440 . 1 1 92 92 THR CB C 13 68.564 0.183 . 1 . . . A 92 THR CB 3 18493 1 441 . 1 1 92 92 THR CG2 C 13 27.476 0.300 . 1 . . . A 92 THR CG2 1 18493 1 442 . 1 1 92 92 THR N N 15 115.463 0.141 . 1 . . . A 92 THR N 3 18493 1 443 . 1 1 93 93 MET C C 13 176.972 0.093 . 1 . . . A 93 MET C 4 18493 1 444 . 1 1 93 93 MET CA C 13 62.369 0.117 . 1 . . . A 93 MET CA 5 18493 1 445 . 1 1 93 93 MET CB C 13 33.515 0.300 . 1 . . . A 93 MET CB 1 18493 1 446 . 1 1 93 93 MET CG C 13 35.406 0.300 . 1 . . . A 93 MET CG 1 18493 1 447 . 1 1 93 93 MET N N 15 117.153 0.150 . 1 . . . A 93 MET N 6 18493 1 448 . 1 1 94 94 LEU H H 1 8.497 0.300 . 1 . . . A 94 LEU H 1 18493 1 449 . 1 1 94 94 LEU CA C 13 57.489 0.077 . 1 . . . A 94 LEU CA 8 18493 1 450 . 1 1 94 94 LEU CB C 13 41.432 0.089 . 1 . . . A 94 LEU CB 2 18493 1 451 . 1 1 94 94 LEU CG C 13 26.603 0.055 . 1 . . . A 94 LEU CG 2 18493 1 452 . 1 1 94 94 LEU CD1 C 13 22.658 0.101 . 2 . . . A 94 LEU CD1 2 18493 1 453 . 1 1 94 94 LEU CD2 C 13 22.759 0.300 . 2 . . . A 94 LEU CD2 1 18493 1 454 . 1 1 94 94 LEU N N 15 117.981 0.315 . 1 . . . A 94 LEU N 10 18493 1 455 . 1 1 95 95 GLN C C 13 178.331 0.045 . 1 . . . A 95 GLN C 2 18493 1 456 . 1 1 95 95 GLN CA C 13 57.604 0.300 . 1 . . . A 95 GLN CA 1 18493 1 457 . 1 1 95 95 GLN CB C 13 28.200 0.300 . 1 . . . A 95 GLN CB 1 18493 1 458 . 1 1 96 96 LEU C C 13 177.842 0.134 . 1 . . . A 96 LEU C 5 18493 1 459 . 1 1 96 96 LEU CA C 13 57.747 0.300 . 1 . . . A 96 LEU CA 2 18493 1 460 . 1 1 96 96 LEU CB C 13 41.721 0.068 . 1 . . . A 96 LEU CB 2 18493 1 461 . 1 1 96 96 LEU CG C 13 27.022 0.300 . 1 . . . A 96 LEU CG 1 18493 1 462 . 1 1 96 96 LEU CD1 C 13 23.513 0.300 . 2 . . . A 96 LEU CD1 1 18493 1 463 . 1 1 96 96 LEU CD2 C 13 22.940 0.300 . 2 . . . A 96 LEU CD2 1 18493 1 464 . 1 1 96 96 LEU N N 15 118.174 0.129 . 1 . . . A 96 LEU N 2 18493 1 465 . 1 1 97 97 TYR H H 1 8.485 0.004 . 1 . . . A 97 TYR H 2 18493 1 466 . 1 1 97 97 TYR CA C 13 57.581 0.199 . 1 . . . A 97 TYR CA 6 18493 1 467 . 1 1 97 97 TYR N N 15 117.359 0.153 . 1 . . . A 97 TYR N 7 18493 1 468 . 1 1 98 98 PRO CA C 13 63.847 0.300 . 1 . . . A 98 PRO CA 1 18493 1 469 . 1 1 98 98 PRO CD C 13 50.919 0.110 . 1 . . . A 98 PRO CD 3 18493 1 470 . 1 1 98 98 PRO N N 15 130.765 0.300 . 1 . . . A 98 PRO N 1 18493 1 471 . 1 1 99 99 SER CA C 13 58.145 0.263 . 1 . . . A 99 SER CA 7 18493 1 472 . 1 1 99 99 SER CB C 13 64.506 0.157 . 1 . . . A 99 SER CB 3 18493 1 473 . 1 1 100 100 PRO CD C 13 50.825 0.084 . 1 . . . A 100 PRO CD 3 18493 1 474 . 1 1 100 100 PRO N N 15 130.137 0.300 . 1 . . . A 100 PRO N 1 18493 1 475 . 1 1 101 101 PHE C C 13 174.992 0.300 . 1 . . . A 101 PHE C 1 18493 1 476 . 1 1 102 102 ALA H H 1 7.383 0.024 . 1 . . . A 102 ALA H 2 18493 1 477 . 1 1 102 102 ALA C C 13 176.810 0.300 . 1 . . . A 102 ALA C 1 18493 1 478 . 1 1 102 102 ALA CA C 13 54.355 0.017 . 1 . . . A 102 ALA CA 2 18493 1 479 . 1 1 102 102 ALA N N 15 120.614 0.024 . 1 . . . A 102 ALA N 2 18493 1 480 . 1 1 103 103 THR H H 1 9.278 0.020 . 1 . . . A 103 THR H 2 18493 1 481 . 1 1 103 103 THR C C 13 175.666 0.155 . 1 . . . A 103 THR C 2 18493 1 482 . 1 1 103 103 THR CA C 13 59.838 0.300 . 1 . . . A 103 THR CA 1 18493 1 483 . 1 1 103 103 THR CB C 13 67.623 0.300 . 1 . . . A 103 THR CB 1 18493 1 484 . 1 1 103 103 THR CG2 C 13 20.002 0.300 . 1 . . . A 103 THR CG2 1 18493 1 485 . 1 1 103 103 THR N N 15 112.507 0.194 . 1 . . . A 103 THR N 5 18493 1 486 . 1 1 104 104 CYS H H 1 9.934 0.012 . 1 . . . A 104 CYS H 2 18493 1 487 . 1 1 104 104 CYS C C 13 174.474 0.300 . 1 . . . A 104 CYS C 1 18493 1 488 . 1 1 104 104 CYS CA C 13 64.988 0.300 . 1 . . . A 104 CYS CA 1 18493 1 489 . 1 1 104 104 CYS CB C 13 42.988 0.300 . 1 . . . A 104 CYS CB 1 18493 1 490 . 1 1 104 104 CYS N N 15 122.754 0.031 . 1 . . . A 104 CYS N 3 18493 1 491 . 1 1 105 105 ASP H H 1 8.153 0.005 . 1 . . . A 105 ASP H 2 18493 1 492 . 1 1 105 105 ASP CB C 13 41.030 0.300 . 1 . . . A 105 ASP CB 1 18493 1 493 . 1 1 105 105 ASP N N 15 121.350 0.012 . 1 . . . A 105 ASP N 2 18493 1 494 . 1 1 108 108 VAL C C 13 175.472 0.115 . 1 . . . A 108 VAL C 3 18493 1 495 . 1 1 108 108 VAL CA C 13 61.483 0.237 . 1 . . . A 108 VAL CA 8 18493 1 496 . 1 1 108 108 VAL CB C 13 32.076 0.300 . 1 . . . A 108 VAL CB 1 18493 1 497 . 1 1 108 108 VAL CG1 C 13 22.907 0.056 . 2 . . . A 108 VAL CG1 4 18493 1 498 . 1 1 108 108 VAL CG2 C 13 21.098 0.044 . 2 . . . A 108 VAL CG2 4 18493 1 499 . 1 1 108 108 VAL N N 15 112.506 0.026 . 1 . . . A 108 VAL N 3 18493 1 500 . 1 1 109 109 ARG N N 15 112.150 0.050 . 1 . . . . 109 ARG N 3 18493 1 501 . 1 1 110 110 PHE CA C 13 58.681 0.114 . 1 . . . . 110 PHE CA 2 18493 1 502 . 1 1 111 111 PRO CA C 13 65.848 0.300 . 1 . . . . 111 PRO CA 1 18493 1 503 . 1 1 111 111 PRO CD C 13 51.081 0.220 . 1 . . . . 111 PRO CD 4 18493 1 504 . 1 1 112 112 GLU C C 13 177.165 0.300 . 1 . . . . 112 GLU C 1 18493 1 505 . 1 1 113 113 TRP H H 1 9.706 0.060 . 1 . . . . 113 TRP HN 3 18493 1 506 . 1 1 113 113 TRP CA C 13 53.381 0.091 . 1 . . . . 113 TRP CA 2 18493 1 507 . 1 1 113 113 TRP N N 15 111.820 0.076 . 1 . . . . 113 TRP N 3 18493 1 508 . 1 1 114 114 LEU CB C 13 41.351 0.300 . 1 . . . A 114 LEU CB 1 18493 1 509 . 1 1 115 115 PRO CA C 13 61.148 0.061 . 1 . . . A 115 PRO CA 2 18493 1 510 . 1 1 115 115 PRO CB C 13 30.280 0.008 . 1 . . . A 115 PRO CB 2 18493 1 511 . 1 1 115 115 PRO CG C 13 26.706 0.066 . 1 . . . A 115 PRO CG 2 18493 1 512 . 1 1 115 115 PRO CD C 13 49.865 0.001 . 1 . . . A 115 PRO CD 2 18493 1 513 . 1 1 116 116 LEU C C 13 178.163 0.059 . 1 . . . A 116 LEU C 3 18493 1 514 . 1 1 116 116 LEU CA C 13 58.746 0.037 . 1 . . . A 116 LEU CA 2 18493 1 515 . 1 1 116 116 LEU CB C 13 42.932 0.300 . 1 . . . A 116 LEU CB 1 18493 1 516 . 1 1 116 116 LEU CG C 13 26.521 0.300 . 1 . . . A 116 LEU CG 1 18493 1 517 . 1 1 117 117 ASP C C 13 177.528 0.082 . 1 . . . A 117 ASP C 2 18493 1 518 . 1 1 117 117 ASP CB C 13 41.252 0.054 . 1 . . . A 117 ASP CB 2 18493 1 519 . 1 1 117 117 ASP N N 15 116.302 0.080 . 1 . . . A 117 ASP N 3 18493 1 520 . 1 1 118 118 LYS H H 1 7.538 0.036 . 1 . . . A 118 LYS H 3 18493 1 521 . 1 1 118 118 LYS CD C 13 27.953 0.098 . 1 . . . A 118 LYS CD 2 18493 1 522 . 1 1 118 118 LYS N N 15 118.983 0.119 . 1 . . . A 118 LYS N 4 18493 1 523 . 1 1 119 119 TRP C C 13 177.867 0.300 . 1 . . . A 119 TRP C 1 18493 1 524 . 1 1 120 120 VAL H H 1 8.936 0.019 . 1 . . . A 120 VAL H 2 18493 1 525 . 1 1 120 120 VAL CA C 13 58.651 0.114 . 1 . . . A 120 VAL CA 7 18493 1 526 . 1 1 120 120 VAL CB C 13 31.821 0.110 . 1 . . . A 120 VAL CB 4 18493 1 527 . 1 1 120 120 VAL CG2 C 13 20.697 0.300 . 2 . . . A 120 VAL CG2 1 18493 1 528 . 1 1 120 120 VAL N N 15 113.149 0.024 . 1 . . . A 120 VAL N 2 18493 1 529 . 1 1 121 121 PRO C C 13 178.888 0.300 . 1 . . . A 121 PRO C 1 18493 1 530 . 1 1 121 121 PRO CA C 13 65.185 0.015 . 1 . . . A 121 PRO CA 3 18493 1 531 . 1 1 121 121 PRO CB C 13 31.781 0.162 . 1 . . . A 121 PRO CB 4 18493 1 532 . 1 1 121 121 PRO CG C 13 27.660 0.300 . 1 . . . A 121 PRO CG 1 18493 1 533 . 1 1 121 121 PRO CD C 13 50.590 0.079 . 1 . . . A 121 PRO CD 8 18493 1 534 . 1 1 122 122 GLN H H 1 9.809 0.005 . 1 . . . A 122 GLN H 2 18493 1 535 . 1 1 122 122 GLN C C 13 174.326 0.300 . 1 . . . A 122 GLN C 1 18493 1 536 . 1 1 122 122 GLN CA C 13 58.463 0.300 . 1 . . . A 122 GLN CA 1 18493 1 537 . 1 1 122 122 GLN N N 15 116.304 0.039 . 1 . . . A 122 GLN N 2 18493 1 538 . 1 1 123 123 VAL H H 1 8.219 0.004 . 1 . . . A 123 VAL H 2 18493 1 539 . 1 1 123 123 VAL C C 13 175.777 0.065 . 1 . . . A 123 VAL C 2 18493 1 540 . 1 1 123 123 VAL CA C 13 61.689 0.292 . 1 . . . A 123 VAL CA 8 18493 1 541 . 1 1 123 123 VAL CB C 13 35.373 0.087 . 1 . . . A 123 VAL CB 4 18493 1 542 . 1 1 123 123 VAL CG2 C 13 21.181 0.300 . 2 . . . A 123 VAL CG2 1 18493 1 543 . 1 1 123 123 VAL N N 15 113.254 0.054 . 1 . . . A 123 VAL N 3 18493 1 544 . 1 1 124 124 PHE C C 13 172.759 0.249 . 1 . . . A 124 PHE C 4 18493 1 545 . 1 1 124 124 PHE CB C 13 39.318 0.300 . 1 . . . A 124 PHE CB 1 18493 1 546 . 1 1 124 124 PHE N N 15 112.242 0.017 . 1 . . . A 124 PHE N 2 18493 1 547 . 1 1 125 125 VAL H H 1 7.799 0.022 . 1 . . . A 125 VAL H 3 18493 1 548 . 1 1 125 125 VAL C C 13 177.034 0.300 . 1 . . . A 125 VAL C 1 18493 1 549 . 1 1 125 125 VAL CA C 13 61.950 0.164 . 1 . . . A 125 VAL CA 7 18493 1 550 . 1 1 125 125 VAL CB C 13 33.376 0.164 . 1 . . . A 125 VAL CB 2 18493 1 551 . 1 1 125 125 VAL CG1 C 13 24.379 0.300 . 2 . . . A 125 VAL CG1 1 18493 1 552 . 1 1 125 125 VAL CG2 C 13 21.389 0.300 . 2 . . . A 125 VAL CG2 1 18493 1 553 . 1 1 125 125 VAL N N 15 115.233 0.352 . 1 . . . A 125 VAL N 7 18493 1 554 . 1 1 126 126 ALA H H 1 9.014 0.030 . 1 . . . A 126 ALA H 3 18493 1 555 . 1 1 126 126 ALA C C 13 175.920 0.300 . 1 . . . A 126 ALA C 1 18493 1 556 . 1 1 126 126 ALA CA C 13 54.493 0.067 . 1 . . . A 126 ALA CA 8 18493 1 557 . 1 1 126 126 ALA CB C 13 17.215 0.018 . 1 . . . A 126 ALA CB 6 18493 1 558 . 1 1 126 126 ALA N N 15 130.709 0.039 . 1 . . . A 126 ALA N 4 18493 1 559 . 1 1 127 127 SER H H 1 8.145 0.026 . 1 . . . A 127 SER H 2 18493 1 560 . 1 1 127 127 SER CA C 13 58.101 0.300 . 1 . . . A 127 SER CA 1 18493 1 561 . 1 1 127 127 SER CB C 13 64.539 0.300 . 1 . . . A 127 SER CB 1 18493 1 562 . 1 1 127 127 SER N N 15 112.716 0.005 . 1 . . . A 127 SER N 2 18493 1 563 . 1 1 128 128 GLY H H 1 8.595 0.058 . 1 . . . A 128 GLY H 2 18493 1 564 . 1 1 128 128 GLY C C 13 177.047 0.300 . 1 . . . A 128 GLY C 1 18493 1 565 . 1 1 128 128 GLY CA C 13 46.296 0.123 . 1 . . . A 128 GLY CA 2 18493 1 566 . 1 1 128 128 GLY N N 15 106.487 0.017 . 1 . . . A 128 GLY N 2 18493 1 567 . 1 1 129 129 ASP C C 13 177.916 0.300 . 1 . . . A 129 ASP C 1 18493 1 568 . 1 1 129 129 ASP CB C 13 43.975 0.134 . 1 . . . A 129 ASP CB 2 18493 1 569 . 1 1 130 130 CYS H H 1 9.948 0.003 . 1 . . . A 130 CYS H 2 18493 1 570 . 1 1 130 130 CYS C C 13 173.312 0.300 . 1 . . . A 130 CYS C 1 18493 1 571 . 1 1 130 130 CYS CA C 13 64.581 0.074 . 1 . . . A 130 CYS CA 2 18493 1 572 . 1 1 130 130 CYS CB C 13 42.879 0.043 . 1 . . . A 130 CYS CB 2 18493 1 573 . 1 1 130 130 CYS N N 15 122.984 0.016 . 1 . . . A 130 CYS N 2 18493 1 574 . 1 1 131 131 ALA H H 1 9.869 0.029 . 1 . . . A 131 ALA H 2 18493 1 575 . 1 1 131 131 ALA CA C 13 52.640 0.300 . 1 . . . A 131 ALA CA 1 18493 1 576 . 1 1 131 131 ALA CB C 13 18.497 0.300 . 1 . . . A 131 ALA CB 1 18493 1 577 . 1 1 131 131 ALA N N 15 121.534 0.128 . 1 . . . A 131 ALA N 2 18493 1 578 . 1 1 136 136 ASP C C 13 172.916 0.300 . 1 . . . A 136 ASP C 1 18493 1 579 . 1 1 137 137 PHE H H 1 8.959 0.005 . 1 . . . A 137 PHE H 2 18493 1 580 . 1 1 137 137 PHE CA C 13 57.310 0.300 . 1 . . . A 137 PHE CA 1 18493 1 581 . 1 1 137 137 PHE CB C 13 42.927 0.300 . 1 . . . A 137 PHE CB 1 18493 1 582 . 1 1 137 137 PHE N N 15 117.677 0.047 . 1 . . . A 137 PHE N 2 18493 1 583 . 1 1 138 138 LEU CB C 13 43.547 0.300 . 1 . . . A 138 LEU CB 1 18493 1 584 . 1 1 139 139 GLY C C 13 176.262 0.300 . 1 . . . A 139 GLY C 1 18493 1 585 . 1 1 139 139 GLY CA C 13 46.123 0.300 . 1 . . . A 139 GLY CA 1 18493 1 586 . 1 1 140 140 LEU CB C 13 40.503 0.012 . 1 . . . A 140 LEU CB 2 18493 1 587 . 1 1 140 140 LEU N N 15 124.207 0.300 . 1 . . . A 140 LEU N 1 18493 1 588 . 1 1 142 142 MET CA C 13 56.442 0.300 . 1 . . . A 142 MET CA 1 18493 1 589 . 1 1 143 143 PRO CA C 13 63.254 0.300 . 1 . . . A 143 PRO CA 1 18493 1 590 . 1 1 143 143 PRO CD C 13 51.480 0.002 . 1 . . . A 143 PRO CD 2 18493 1 591 . 1 1 144 144 GLN C C 13 177.307 0.300 . 1 . . . A 144 GLN C 1 18493 1 592 . 1 1 145 145 TRP H H 1 8.386 0.037 . 1 . . . A 145 TRP H 2 18493 1 593 . 1 1 145 145 TRP C C 13 178.709 0.579 . 1 . . . A 145 TRP C 4 18493 1 594 . 1 1 145 145 TRP CA C 13 59.535 0.203 . 1 . . . A 145 TRP CA 2 18493 1 595 . 1 1 145 145 TRP CB C 13 29.345 0.087 . 1 . . . A 145 TRP CB 4 18493 1 596 . 1 1 145 145 TRP N N 15 120.795 0.006 . 1 . . . A 145 TRP N 2 18493 1 597 . 1 1 146 146 LEU H H 1 9.033 0.008 . 1 . . . A 146 LEU H 3 18493 1 598 . 1 1 146 146 LEU C C 13 177.115 0.169 . 1 . . . A 146 LEU C 9 18493 1 599 . 1 1 146 146 LEU CA C 13 57.793 0.385 . 1 . . . A 146 LEU CA 9 18493 1 600 . 1 1 146 146 LEU CB C 13 41.616 0.072 . 1 . . . A 146 LEU CB 3 18493 1 601 . 1 1 146 146 LEU CG C 13 26.151 0.009 . 1 . . . A 146 LEU CG 2 18493 1 602 . 1 1 146 146 LEU CD1 C 13 22.670 0.300 . 2 . . . A 146 LEU CD1 1 18493 1 603 . 1 1 146 146 LEU CD2 C 13 22.670 0.300 . 2 . . . A 146 LEU CD2 1 18493 1 604 . 1 1 146 146 LEU N N 15 118.336 0.119 . 1 . . . A 146 LEU N 12 18493 1 605 . 1 1 147 147 LEU H H 1 8.480 0.032 . 1 . . . A 147 LEU H 3 18493 1 606 . 1 1 147 147 LEU C C 13 178.787 0.168 . 1 . . . A 147 LEU C 10 18493 1 607 . 1 1 147 147 LEU CA C 13 58.052 0.132 . 1 . . . A 147 LEU CA 14 18493 1 608 . 1 1 147 147 LEU CB C 13 41.047 0.213 . 1 . . . A 147 LEU CB 5 18493 1 609 . 1 1 147 147 LEU CG C 13 27.480 0.266 . 1 . . . A 147 LEU CG 5 18493 1 610 . 1 1 147 147 LEU CD1 C 13 24.363 0.026 . 2 . . . A 147 LEU CD1 2 18493 1 611 . 1 1 147 147 LEU CD2 C 13 22.324 0.300 . 2 . . . A 147 LEU CD2 1 18493 1 612 . 1 1 147 147 LEU N N 15 123.772 0.148 . 1 . . . A 147 LEU N 19 18493 1 613 . 1 1 148 148 GLY C C 13 174.667 0.213 . 1 . . . A 148 GLY C 9 18493 1 614 . 1 1 148 148 GLY CA C 13 48.102 0.256 . 1 . . . A 148 GLY CA 22 18493 1 615 . 1 1 148 148 GLY N N 15 104.457 0.229 . 1 . . . A 148 GLY N 13 18493 1 616 . 1 1 149 149 ILE C C 13 177.725 0.126 . 1 . . . A 149 ILE C 8 18493 1 617 . 1 1 149 149 ILE CA C 13 65.997 0.108 . 1 . . . A 149 ILE CA 54 18493 1 618 . 1 1 149 149 ILE CB C 13 38.262 0.126 . 1 . . . A 149 ILE CB 33 18493 1 619 . 1 1 149 149 ILE CG1 C 13 30.092 0.146 . 1 . . . A 149 ILE CG1 25 18493 1 620 . 1 1 149 149 ILE CG2 C 13 18.028 0.134 . 1 . . . A 149 ILE CG2 33 18493 1 621 . 1 1 149 149 ILE CD1 C 13 14.653 0.089 . 1 . . . A 149 ILE CD1 35 18493 1 622 . 1 1 149 149 ILE N N 15 121.815 0.134 . 1 . . . A 149 ILE N 14 18493 1 623 . 1 1 150 150 PHE C C 13 178.929 0.079 . 1 . . . A 150 PHE C 6 18493 1 624 . 1 1 150 150 PHE CA C 13 63.591 0.298 . 1 . . . A 150 PHE CA 9 18493 1 625 . 1 1 150 150 PHE CB C 13 38.417 0.314 . 1 . . . A 150 PHE CB 8 18493 1 626 . 1 1 150 150 PHE N N 15 118.894 0.361 . 1 . . . A 150 PHE N 9 18493 1 627 . 1 1 151 151 ILE C C 13 177.347 0.160 . 1 . . . A 151 ILE C 15 18493 1 628 . 1 1 151 151 ILE CA C 13 66.478 0.132 . 1 . . . A 151 ILE CA 21 18493 1 629 . 1 1 151 151 ILE CB C 13 37.302 0.117 . 1 . . . A 151 ILE CB 15 18493 1 630 . 1 1 151 151 ILE CG1 C 13 30.856 0.230 . 1 . . . A 151 ILE CG1 5 18493 1 631 . 1 1 151 151 ILE CG2 C 13 17.909 0.177 . 1 . . . A 151 ILE CG2 13 18493 1 632 . 1 1 151 151 ILE CD1 C 13 14.457 0.178 . 1 . . . A 151 ILE CD1 9 18493 1 633 . 1 1 151 151 ILE N N 15 120.535 0.091 . 1 . . . A 151 ILE N 5 18493 1 634 . 1 1 152 152 ALA C C 13 179.165 0.094 . 1 . . . A 152 ALA C 8 18493 1 635 . 1 1 152 152 ALA CA C 13 56.272 0.115 . 1 . . . A 152 ALA CA 17 18493 1 636 . 1 1 152 152 ALA CB C 13 17.993 0.103 . 1 . . . A 152 ALA CB 13 18493 1 637 . 1 1 152 152 ALA N N 15 122.855 0.199 . 1 . . . A 152 ALA N 17 18493 1 638 . 1 1 153 153 TYR H H 1 8.680 0.007 . 1 . . . A 153 TYR H 2 18493 1 639 . 1 1 153 153 TYR C C 13 179.682 0.090 . 1 . . . A 153 TYR C 5 18493 1 640 . 1 1 153 153 TYR CA C 13 64.391 0.144 . 1 . . . A 153 TYR CA 9 18493 1 641 . 1 1 153 153 TYR CB C 13 39.553 0.044 . 1 . . . A 153 TYR CB 3 18493 1 642 . 1 1 153 153 TYR N N 15 116.156 0.294 . 1 . . . A 153 TYR N 11 18493 1 643 . 1 1 154 154 LEU C C 13 177.336 0.292 . 1 . . . A 154 LEU C 12 18493 1 644 . 1 1 154 154 LEU CA C 13 57.905 0.125 . 1 . . . A 154 LEU CA 7 18493 1 645 . 1 1 154 154 LEU CB C 13 42.009 0.114 . 1 . . . A 154 LEU CB 6 18493 1 646 . 1 1 154 154 LEU CG C 13 27.063 0.030 . 1 . . . A 154 LEU CG 2 18493 1 647 . 1 1 154 154 LEU CD1 C 13 23.943 0.300 . 2 . . . A 154 LEU CD1 1 18493 1 648 . 1 1 154 154 LEU CD2 C 13 22.797 0.300 . 2 . . . A 154 LEU CD2 1 18493 1 649 . 1 1 154 154 LEU N N 15 122.327 0.136 . 1 . . . A 154 LEU N 6 18493 1 650 . 1 1 155 155 ILE C C 13 177.589 0.123 . 1 . . . A 155 ILE C 8 18493 1 651 . 1 1 155 155 ILE CA C 13 65.996 0.180 . 1 . . . A 155 ILE CA 19 18493 1 652 . 1 1 155 155 ILE CB C 13 38.179 0.112 . 1 . . . A 155 ILE CB 9 18493 1 653 . 1 1 155 155 ILE CG1 C 13 31.527 0.034 . 1 . . . A 155 ILE CG1 2 18493 1 654 . 1 1 155 155 ILE CG2 C 13 17.923 0.076 . 1 . . . A 155 ILE CG2 8 18493 1 655 . 1 1 155 155 ILE CD1 C 13 14.649 0.300 . 1 . . . A 155 ILE CD1 1 18493 1 656 . 1 1 155 155 ILE N N 15 119.079 0.131 . 1 . . . A 155 ILE N 15 18493 1 657 . 1 1 156 156 VAL C C 13 176.163 0.083 . 1 . . . A 156 VAL C 15 18493 1 658 . 1 1 156 156 VAL CA C 13 67.664 0.259 . 1 . . . A 156 VAL CA 16 18493 1 659 . 1 1 156 156 VAL CB C 13 31.694 0.103 . 1 . . . A 156 VAL CB 6 18493 1 660 . 1 1 156 156 VAL CG1 C 13 23.147 0.045 . 2 . . . A 156 VAL CG1 4 18493 1 661 . 1 1 156 156 VAL CG2 C 13 24.386 0.096 . 2 . . . A 156 VAL CG2 2 18493 1 662 . 1 1 156 156 VAL N N 15 117.551 0.129 . 1 . . . A 156 VAL N 15 18493 1 663 . 1 1 157 157 ALA C C 13 179.076 0.203 . 1 . . . A 157 ALA C 13 18493 1 664 . 1 1 157 157 ALA CA C 13 54.803 0.135 . 1 . . . A 157 ALA CA 25 18493 1 665 . 1 1 157 157 ALA CB C 13 16.120 0.235 . 1 . . . A 157 ALA CB 26 18493 1 666 . 1 1 157 157 ALA N N 15 122.470 0.107 . 1 . . . A 157 ALA N 18 18493 1 667 . 1 1 158 158 VAL C C 13 177.491 0.045 . 1 . . . A 158 VAL C 3 18493 1 668 . 1 1 158 158 VAL CA C 13 67.160 0.189 . 1 . . . A 158 VAL CA 33 18493 1 669 . 1 1 158 158 VAL CB C 13 31.331 0.082 . 1 . . . A 158 VAL CB 16 18493 1 670 . 1 1 158 158 VAL CG1 C 13 23.576 0.075 . 2 . . . A 158 VAL CG1 12 18493 1 671 . 1 1 158 158 VAL CG2 C 13 21.967 0.129 . 2 . . . A 158 VAL CG2 9 18493 1 672 . 1 1 158 158 VAL N N 15 116.045 0.145 . 1 . . . A 158 VAL N 19 18493 1 673 . 1 1 159 159 LEU C C 13 178.312 0.157 . 1 . . . A 159 LEU C 8 18493 1 674 . 1 1 159 159 LEU CA C 13 57.443 0.243 . 1 . . . A 159 LEU CA 11 18493 1 675 . 1 1 159 159 LEU CB C 13 41.567 0.272 . 1 . . . A 159 LEU CB 13 18493 1 676 . 1 1 159 159 LEU CG C 13 26.578 0.379 . 1 . . . A 159 LEU CG 4 18493 1 677 . 1 1 159 159 LEU CD1 C 13 22.883 0.300 . 2 . . . A 159 LEU CD1 1 18493 1 678 . 1 1 159 159 LEU CD2 C 13 22.883 0.300 . 2 . . . A 159 LEU CD2 1 18493 1 679 . 1 1 159 159 LEU N N 15 116.776 0.142 . 1 . . . A 159 LEU N 8 18493 1 680 . 1 1 160 160 VAL C C 13 177.508 0.079 . 1 . . . A 160 VAL C 3 18493 1 681 . 1 1 160 160 VAL CA C 13 67.366 0.181 . 1 . . . A 160 VAL CA 15 18493 1 682 . 1 1 160 160 VAL CB C 13 31.106 0.253 . 1 . . . A 160 VAL CB 4 18493 1 683 . 1 1 160 160 VAL CG1 C 13 23.638 0.193 . 2 . . . A 160 VAL CG1 4 18493 1 684 . 1 1 160 160 VAL CG2 C 13 21.784 0.300 . 2 . . . A 160 VAL CG2 1 18493 1 685 . 1 1 160 160 VAL N N 15 118.890 0.153 . 1 . . . A 160 VAL N 14 18493 1 686 . 1 1 161 161 VAL C C 13 176.607 0.060 . 1 . . . A 161 VAL C 2 18493 1 687 . 1 1 161 161 VAL CA C 13 67.614 0.156 . 1 . . . A 161 VAL CA 12 18493 1 688 . 1 1 161 161 VAL CB C 13 31.646 0.056 . 1 . . . A 161 VAL CB 3 18493 1 689 . 1 1 161 161 VAL CG1 C 13 23.255 0.068 . 2 . . . A 161 VAL CG1 2 18493 1 690 . 1 1 161 161 VAL CG2 C 13 21.814 0.205 . 2 . . . A 161 VAL CG2 7 18493 1 691 . 1 1 161 161 VAL N N 15 118.360 0.217 . 1 . . . A 161 VAL N 11 18493 1 692 . 1 1 162 162 ILE C C 13 176.885 0.300 . 1 . . . A 162 ILE C 1 18493 1 693 . 1 1 162 162 ILE CA C 13 63.409 0.074 . 1 . . . A 162 ILE CA 3 18493 1 694 . 1 1 162 162 ILE CB C 13 39.685 0.186 . 1 . . . A 162 ILE CB 3 18493 1 695 . 1 1 162 162 ILE CG1 C 13 31.399 0.300 . 1 . . . A 162 ILE CG1 1 18493 1 696 . 1 1 162 162 ILE CG2 C 13 18.101 0.045 . 1 . . . A 162 ILE CG2 2 18493 1 697 . 1 1 163 163 SER H H 1 9.427 0.022 . 1 . . . . 163 SER HN 2 18493 1 698 . 1 1 163 163 SER CA C 13 60.441 0.222 . 1 . . . . 163 SER CA 2 18493 1 699 . 1 1 163 163 SER CB C 13 63.788 0.300 . 1 . . . . 163 SER CB 1 18493 1 700 . 1 1 163 163 SER N N 15 112.832 0.300 . 1 . . . . 163 SER N 2 18493 1 701 . 1 1 165 165 PRO CA C 13 62.249 0.011 . 1 . . . . 165 PRO CA 2 18493 1 702 . 1 1 165 165 PRO CD C 13 51.723 0.128 . 1 . . . . 165 PRO CD 3 18493 1 703 . 1 1 165 165 PRO N N 15 134.035 0.022 . 1 . . . . 165 PRO N 3 18493 1 704 . 1 1 168 168 ALA CA C 13 51.195 0.007 . 1 . . . . 168 ALA CA 6 18493 1 705 . 1 1 168 168 ALA CB C 13 18.891 0.003 . 1 . . . . 168 ALA CB 6 18493 1 706 . 4 4 1 1 UQ1 C1 C 13 135.534 0.060 . 1 . . . . 501 UQ8 C1 4 18493 1 707 . 4 4 1 1 UQ1 C10 C 13 20.609 0.118 . 4 . . . . 501 UQ8 C10 7 18493 1 708 . 4 4 1 1 UQ1 C11 C 13 43.400 0.643 . 4 . . . . 501 UQ8 C11 9 18493 1 709 . 4 4 1 1 UQ1 C12 C 13 30.300 0.643 . 4 . . . . 501 UQ8 C12 9 18493 1 710 . 4 4 1 1 UQ1 C15 C 13 20.700 0.643 . 4 . . . . 501 UQ8 C15 9 18493 1 711 . 4 4 1 1 UQ1 C16 C 13 43.000 0.643 . 4 . . . . 501 UQ8 C16 9 18493 1 712 . 4 4 1 1 UQ1 C17 C 13 29.800 0.643 . 4 . . . . 501 UQ8 C17 9 18493 1 713 . 4 4 1 1 UQ1 C1M C 13 15.859 0.061 . 4 . . . . 501 UQ8 C1M 5 18493 1 714 . 4 4 1 1 UQ1 C2 C 13 154.709 0.300 . 1 . . . . 501 UQ8 C2 1 18493 1 715 . 4 4 1 1 UQ1 C20 C 13 20.200 0.643 . 4 . . . . 501 UQ8 C20 9 18493 1 716 . 4 4 1 1 UQ1 C21 C 13 42.600 0.643 . 4 . . . . 501 UQ8 C21 9 18493 1 717 . 4 4 1 1 UQ1 C22 C 13 29.300 0.643 . 4 . . . . 501 UQ8 C22 9 18493 1 718 . 4 4 1 1 UQ1 C25 C 13 19.700 0.643 . 4 . . . . 501 UQ8 C25 9 18493 1 719 . 4 4 1 1 UQ1 C26 C 13 42.200 0.643 . 4 . . . . 501 UQ8 C26 9 18493 1 720 . 4 4 1 1 UQ1 C27 C 13 28.800 0.643 . 4 . . . . 501 UQ8 C27 9 18493 1 721 . 4 4 1 1 UQ1 C3 C 13 142.410 0.300 . 4 . . . . 501 UQ8 C3 1 18493 1 722 . 4 4 1 1 UQ1 C30 C 13 19.200 0.643 . 4 . . . . 501 UQ8 C30 9 18493 1 723 . 4 4 1 1 UQ1 C31 C 13 41.800 0.643 . 4 . . . . 501 UQ8 C31 9 18493 1 724 . 4 4 1 1 UQ1 C32 C 13 28.300 0.643 . 4 . . . . 501 UQ8 C32 9 18493 1 725 . 4 4 1 1 UQ1 C35 C 13 18.700 0.643 . 4 . . . . 501 UQ8 C35 9 18493 1 726 . 4 4 1 1 UQ1 C36 C 13 41.400 0.643 . 4 . . . . 501 UQ8 C36 9 18493 1 727 . 4 4 1 1 UQ1 C37 C 13 27.800 0.643 . 4 . . . . 501 UQ8 C37 9 18493 1 728 . 4 4 1 1 UQ1 C38 C 13 124.750 0.300 . 4 . . . . 501 UQ8 C38 1 18493 1 729 . 4 4 1 1 UQ1 C39 C 13 136.254 0.051 . 4 . . . . 501 UQ8 C39 2 18493 1 730 . 4 4 1 1 UQ1 C3M C 13 63.804 0.193 . 4 . . . . 501 UQ8 C3M 2 18493 1 731 . 4 4 1 1 UQ1 C4 C 13 142.410 0.300 . 1 . . . . 501 UQ8 C4 1 18493 1 732 . 4 4 1 1 UQ1 C40 C 13 18.200 0.643 . 4 . . . . 501 UQ8 C40 9 18493 1 733 . 4 4 1 1 UQ1 C41 C 13 41.517 0.095 . 4 . . . . 501 UQ8 C41 3 18493 1 734 . 4 4 1 1 UQ1 C42 C 13 28.260 0.020 . 4 . . . . 501 UQ8 C42 2 18493 1 735 . 4 4 1 1 UQ1 C43 C 13 126.157 0.271 . 4 . . . . 501 UQ8 C43 6 18493 1 736 . 4 4 1 1 UQ1 C44 C 13 135.212 0.112 . 4 . . . . 501 UQ8 C44 8 18493 1 737 . 4 4 1 1 UQ1 C45 C 13 17.920 0.069 . 4 . . . . 501 UQ8 C45 7 18493 1 738 . 4 4 1 1 UQ1 C46 C 13 28.177 0.074 . 4 . . . . 501 UQ8 C46 5 18493 1 739 . 4 4 1 1 UQ1 C4M C 13 63.804 0.193 . 4 . . . . 501 UQ8 C4M 2 18493 1 740 . 4 4 1 1 UQ1 C5 C 13 154.709 0.300 . 4 . . . . 501 UQ8 C5 1 18493 1 741 . 4 4 1 1 UQ1 C6 C 13 127.427 0.300 . 1 . . . . 501 UQ8 C6 1 18493 1 742 . 4 4 1 1 UQ1 C7 C 13 26.580 0.011 . 4 . . . . 501 UQ8 C7 3 18493 1 743 . 4 4 1 1 UQ1 C8 C 13 123.680 0.098 . 4 . . . . 501 UQ8 C8 5 18493 1 744 . 4 4 1 1 UQ1 C9 C 13 140.100 0.117 . 4 . . . . 501 UQ8 C9 5 18493 1 stop_ save_