data_18544 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of DsbA(C33S)/DsbB by solid-state NMR ; _BMRB_accession_number 18544 _BMRB_flat_file_name bmr18544.str _Entry_type original _Submission_date 2012-06-21 _Accession_date 2012-06-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solid-state NMR assignments of nanocrystalline DsbA(C33S) and membrane protein complex DsbA(C33S)/DsbB' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay . . 2 Tang Ming . . 3 Berthold Deborah . . 4 Nesbitt Anna . . 5 Gennis Robert . . 6 Rienstra Chad . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 268 "15N chemical shifts" 55 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-06-05 update BMRB 'update entry citation' 2013-04-02 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16327 'DsbA, wild type oxidized' 18543 'DsbA(C33S) apo form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23527473 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay J. . 2 Tang Ming . . 3 Berthold Deborah A. . 4 Nesbitt Anna E. . 5 Gennis Robert B. . 6 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Phys. Chem. B' _Journal_name_full 'The journal of physical chemistry. B' _Journal_volume 117 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6052 _Page_last 6060 _Year 2013 _Details . loop_ _Keyword DsbA/DsbB 'Membrane Protein' 'Solid-state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DsbA(C33S) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbA(C33S) $DsbA(C33S) DsbB $DsbB stop_ _System_molecular_weight 41000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'DsbA(C33S) complex with wild-type DsbB' save_ ######################## # Monomeric polymers # ######################## save_DsbA(C33S) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbA(C33S) _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHSYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 GLN 3 3 TYR 4 4 GLU 5 5 ASP 6 6 GLY 7 7 LYS 8 8 GLN 9 9 TYR 10 10 THR 11 11 THR 12 12 LEU 13 13 GLU 14 14 LYS 15 15 PRO 16 16 VAL 17 17 ALA 18 18 GLY 19 19 ALA 20 20 PRO 21 21 GLN 22 22 VAL 23 23 LEU 24 24 GLU 25 25 PHE 26 26 PHE 27 27 SER 28 28 PHE 29 29 PHE 30 30 CYS 31 31 PRO 32 32 HIS 33 33 SER 34 34 TYR 35 35 GLN 36 36 PHE 37 37 GLU 38 38 GLU 39 39 VAL 40 40 LEU 41 41 HIS 42 42 ILE 43 43 SER 44 44 ASP 45 45 ASN 46 46 VAL 47 47 LYS 48 48 LYS 49 49 LYS 50 50 LEU 51 51 PRO 52 52 GLU 53 53 GLY 54 54 VAL 55 55 LYS 56 56 MET 57 57 THR 58 58 LYS 59 59 TYR 60 60 HIS 61 61 VAL 62 62 ASN 63 63 PHE 64 64 MET 65 65 GLY 66 66 GLY 67 67 ASP 68 68 LEU 69 69 GLY 70 70 LYS 71 71 ASP 72 72 LEU 73 73 THR 74 74 GLN 75 75 ALA 76 76 TRP 77 77 ALA 78 78 VAL 79 79 ALA 80 80 MET 81 81 ALA 82 82 LEU 83 83 GLY 84 84 VAL 85 85 GLU 86 86 ASP 87 87 LYS 88 88 VAL 89 89 THR 90 90 VAL 91 91 PRO 92 92 LEU 93 93 PHE 94 94 GLU 95 95 GLY 96 96 VAL 97 97 GLN 98 98 LYS 99 99 THR 100 100 GLN 101 101 THR 102 102 ILE 103 103 ARG 104 104 SER 105 105 ALA 106 106 SER 107 107 ASP 108 108 ILE 109 109 ARG 110 110 ASP 111 111 VAL 112 112 PHE 113 113 ILE 114 114 ASN 115 115 ALA 116 116 GLY 117 117 ILE 118 118 LYS 119 119 GLY 120 120 GLU 121 121 GLU 122 122 TYR 123 123 ASP 124 124 ALA 125 125 ALA 126 126 TRP 127 127 ASN 128 128 SER 129 129 PHE 130 130 VAL 131 131 VAL 132 132 LYS 133 133 SER 134 134 LEU 135 135 VAL 136 136 ALA 137 137 GLN 138 138 GLN 139 139 GLU 140 140 LYS 141 141 ALA 142 142 ALA 143 143 ALA 144 144 ASP 145 145 VAL 146 146 GLN 147 147 LEU 148 148 ARG 149 149 GLY 150 150 VAL 151 151 PRO 152 152 ALA 153 153 MET 154 154 PHE 155 155 VAL 156 156 ASN 157 157 GLY 158 158 LYS 159 159 TYR 160 160 GLN 161 161 LEU 162 162 ASN 163 163 PRO 164 164 GLN 165 165 GLY 166 166 MET 167 167 ASP 168 168 THR 169 169 SER 170 170 ASN 171 171 MET 172 172 ASP 173 173 VAL 174 174 PHE 175 175 VAL 176 176 GLN 177 177 GLN 178 178 TYR 179 179 ALA 180 180 ASP 181 181 THR 182 182 VAL 183 183 LYS 184 184 TYR 185 185 LEU 186 186 SER 187 187 GLU 188 188 LYS 189 189 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16327 DsbA 100.00 189 99.47 99.47 2.39e-135 BMRB 17710 DsbA 99.47 188 99.47 99.47 9.06e-135 BMRB 18396 oxidized_DsbA 100.00 189 98.94 99.47 9.91e-135 BMRB 18543 DsbA(C33S) 100.00 189 100.00 100.00 3.94e-136 PDB 1A23 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" 100.00 189 99.47 99.47 2.39e-135 PDB 1A24 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2J "Oxidized Dsba Crystal Form Ii" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2L "Reduced Dsba At 2.7 Angstroms Resolution" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2M "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" 100.00 189 99.47 99.47 2.39e-135 PDB 1AC1 "Dsba Mutant H32l" 100.00 189 98.94 98.94 7.33e-134 PDB 1ACV "Dsba Mutant H32s" 100.00 189 98.94 98.94 4.63e-134 PDB 1BQ7 "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" 100.00 189 98.94 98.94 2.65e-134 PDB 1DSB "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" 100.00 189 99.47 99.47 2.39e-135 PDB 1FVJ "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" 100.00 189 98.94 99.47 2.20e-134 PDB 1FVK "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" 100.00 189 99.47 99.47 2.39e-135 PDB 1TI1 "Crystal Structure Of A Mutant Dsba" 100.00 189 99.47 100.00 1.27e-135 PDB 1U3A "Mutant Dsba" 100.00 189 99.47 100.00 1.27e-135 PDB 2B3S "Structure Of The Dsba Mutant (P31g-C33a)" 100.00 189 98.94 99.47 3.23e-134 PDB 2B6M "Structure Of The Dsba Mutant (P31a-C33a)" 100.00 189 98.94 99.47 1.41e-134 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 189 99.47 100.00 1.27e-135 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 100.00 189 99.47 100.00 1.27e-135 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 189 99.47 100.00 1.27e-135 PDB 3DKS "Dsba Substrate Complex" 100.00 189 98.94 99.47 9.08e-135 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 189 99.47 100.00 1.27e-135 PDB 4TKY "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" 100.00 191 99.47 100.00 7.62e-136 PDB 4WET "Crystal Structure Of E.coli Dsba In Complex With Compound 16" 100.00 189 99.47 99.47 2.39e-135 PDB 4WEY "Crystal Structure Of E.coli Dsba In Complex With Compound 17" 100.00 189 99.47 99.47 2.39e-135 PDB 4WF4 "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" 100.00 189 99.47 99.47 2.39e-135 PDB 4WF5 "Crystal Structure Of E.coli Dsba Soaked With Compound 4" 100.00 189 99.47 99.47 2.39e-135 DBJ BAB38206 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAE77448 "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAG79665 "protein disulfide isomerase I [Escherichia coli SE11]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAI27892 "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAI33015 "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA44868 "PpfA protein [Escherichia coli K-12]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA56736 "dsbA [Escherichia coli K-12]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA90910 "DsbA protein [Escherichia coli]" 100.00 208 98.94 99.47 7.46e-135 EMBL CAP78318 "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" 100.00 208 98.94 99.47 7.46e-135 EMBL CAQ34212 "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" 100.00 208 99.47 99.47 2.08e-135 GB AAA23715 "putative [Escherichia coli]" 100.00 208 99.47 99.47 2.08e-135 GB AAB02995 "dsbA [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 99.47 2.08e-135 GB AAC43519 "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" 100.00 208 98.94 98.94 9.53e-134 GB AAC43520 "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" 100.00 208 98.41 98.41 2.81e-133 GB AAC43521 "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" 100.00 208 98.41 98.41 5.36e-133 REF NP_312810 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 99.47 2.08e-135 REF NP_418297 "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 99.47 2.08e-135 REF NP_709659 "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" 100.00 208 98.94 99.47 7.97e-135 REF WP_000725331 "thiol-disulfide isomerase [Shigella boydii]" 100.00 208 98.41 98.94 2.30e-134 REF WP_000725332 "thiol:disulfide interchange protein DsbA [Escherichia coli]" 100.00 208 98.94 99.47 2.55e-135 SP P0A4L5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.46e-135 SP P0A4L6 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.46e-135 SP P0AEG4 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 99.47 2.08e-135 SP P0AEG5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 99.47 2.08e-135 SP P52235 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.97e-135 stop_ save_ save_DsbB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbB _Molecular_mass . _Mol_thiol_state 'free and disulfide bound' _Details . _Residue_count 176 _Mol_residue_sequence ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP CVLCIYERVALFGVLGAALI GAIAPKTPLRYVAMVIWLYS AFRGVQLTYEHTMLQLYPSP FATCDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGL EMPQWLLGIFIAYLIVAVLV VISQPFKAKKRDLFGR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 LEU 3 3 ARG 4 4 PHE 5 5 LEU 6 6 ASN 7 7 GLN 8 8 ALA 9 9 SER 10 10 GLN 11 11 GLY 12 12 ARG 13 13 GLY 14 14 ALA 15 15 TRP 16 16 LEU 17 17 LEU 18 18 MET 19 19 ALA 20 20 PHE 21 21 THR 22 22 ALA 23 23 LEU 24 24 ALA 25 25 LEU 26 26 GLU 27 27 LEU 28 28 THR 29 29 ALA 30 30 LEU 31 31 TRP 32 32 PHE 33 33 GLN 34 34 HIS 35 35 VAL 36 36 MET 37 37 LEU 38 38 LEU 39 39 LYS 40 40 PRO 41 41 CYS 42 42 VAL 43 43 LEU 44 44 CYS 45 45 ILE 46 46 TYR 47 47 GLU 48 48 ARG 49 49 VAL 50 50 ALA 51 51 LEU 52 52 PHE 53 53 GLY 54 54 VAL 55 55 LEU 56 56 GLY 57 57 ALA 58 58 ALA 59 59 LEU 60 60 ILE 61 61 GLY 62 62 ALA 63 63 ILE 64 64 ALA 65 65 PRO 66 66 LYS 67 67 THR 68 68 PRO 69 69 LEU 70 70 ARG 71 71 TYR 72 72 VAL 73 73 ALA 74 74 MET 75 75 VAL 76 76 ILE 77 77 TRP 78 78 LEU 79 79 TYR 80 80 SER 81 81 ALA 82 82 PHE 83 83 ARG 84 84 GLY 85 85 VAL 86 86 GLN 87 87 LEU 88 88 THR 89 89 TYR 90 90 GLU 91 91 HIS 92 92 THR 93 93 MET 94 94 LEU 95 95 GLN 96 96 LEU 97 97 TYR 98 98 PRO 99 99 SER 100 100 PRO 101 101 PHE 102 102 ALA 103 103 THR 104 104 CYS 105 105 ASP 106 106 PHE 107 107 MET 108 108 VAL 109 109 ARG 110 110 PHE 111 111 PRO 112 112 GLU 113 113 TRP 114 114 LEU 115 115 PRO 116 116 LEU 117 117 ASP 118 118 LYS 119 119 TRP 120 120 VAL 121 121 PRO 122 122 GLN 123 123 VAL 124 124 PHE 125 125 VAL 126 126 ALA 127 127 SER 128 128 GLY 129 129 ASP 130 130 CYS 131 131 ALA 132 132 GLU 133 133 ARG 134 134 GLN 135 135 TRP 136 136 ASP 137 137 PHE 138 138 LEU 139 139 GLY 140 140 LEU 141 141 GLU 142 142 MET 143 143 PRO 144 144 GLN 145 145 TRP 146 146 LEU 147 147 LEU 148 148 GLY 149 149 ILE 150 150 PHE 151 151 ILE 152 152 ALA 153 153 TYR 154 154 LEU 155 155 ILE 156 156 VAL 157 157 ALA 158 158 VAL 159 159 LEU 160 160 VAL 161 161 VAL 162 162 ILE 163 163 SER 164 164 GLN 165 165 PRO 166 166 PHE 167 167 LYS 168 168 ALA 169 169 LYS 170 170 LYS 171 171 ARG 172 172 ASP 173 173 LEU 174 174 PHE 175 175 GLY 176 176 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15546 DsbB 100.00 186 99.43 99.43 7.23e-122 BMRB 15966 Disulfide_bond_formation_protein_B 100.00 183 98.30 98.30 4.28e-120 BMRB 17710 DsbB 100.00 176 99.43 99.43 1.19e-121 BMRB 18395 DsbB 100.00 176 100.00 100.00 9.91e-123 BMRB 18493 DsbB 100.00 176 99.43 99.43 1.19e-121 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 176 99.43 99.43 1.19e-121 PDB 2K73 "Solution Nmr Structure Of Integral Membrane Protein Dsbb" 100.00 183 98.30 98.30 4.28e-120 PDB 2K74 "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" 100.00 183 98.30 98.30 4.28e-120 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 100.00 176 99.43 99.43 1.19e-121 PDB 2LTQ "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" 100.00 176 99.43 99.43 1.19e-121 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 176 99.43 99.43 1.19e-121 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 176 99.43 99.43 1.19e-121 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 182 100.00 100.00 6.13e-123 DBJ BAA07408 "disulfide oxidoreductase [Shigella flexneri]" 100.00 176 97.16 97.73 1.41e-118 DBJ BAA36032 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. W3110]" 100.00 176 98.86 98.86 3.86e-121 DBJ BAB35103 "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.86 98.86 3.86e-121 DBJ BAG76757 "disulfide bond formation protein [Escherichia coli SE11]" 100.00 176 97.73 98.30 1.17e-119 DBJ BAI24997 "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" 100.00 176 98.30 98.86 8.48e-121 EMBL CAP75720 "Disulfide bond formation protein B [Escherichia coli LF82]" 100.00 176 97.73 98.30 6.07e-120 EMBL CAQ31687 "DsbB[reduced] [Escherichia coli BL21(DE3)]" 100.00 176 98.86 98.86 3.86e-121 EMBL CAQ98064 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" 100.00 176 98.86 98.86 3.86e-121 EMBL CAR02574 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" 100.00 176 97.73 98.30 6.07e-120 EMBL CAR07527 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli ED1a]" 100.00 176 97.16 97.73 2.16e-119 GB AAA23711 "oxido-reductase [Escherichia coli]" 100.00 178 98.86 98.86 3.51e-121 GB AAB25233 "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" 100.00 176 98.86 98.86 3.86e-121 GB AAC74269 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 176 98.86 98.86 3.86e-121 GB AAG56036 "reoxidizes DsbA protein following formation of disulfide bond in P-ring of flagella [Escherichia coli O157:H7 str. EDL933]" 100.00 176 98.30 98.30 2.67e-120 GB AAN42789 "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" 100.00 176 98.30 98.86 8.48e-121 PIR H85696 "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 176 98.30 98.30 2.67e-120 REF NP_287424 "disulfide bond formation protein B [Escherichia coli O157:H7 str. EDL933]" 100.00 176 98.30 98.30 2.67e-120 REF NP_309707 "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.86 98.86 3.86e-121 REF NP_415703 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 176 98.86 98.86 3.86e-121 REF NP_707082 "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" 100.00 176 98.30 98.86 8.48e-121 REF NP_753538 "disulfide bond formation protein B [Escherichia coli CFT073]" 100.00 176 97.73 98.30 6.07e-120 SP A1AAA8 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli APEC O1]" 100.00 176 97.73 98.30 6.07e-120 SP P0A6M2 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli K-12]" 100.00 176 98.86 98.86 3.86e-121 SP P0A6M3 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli O157:H7]" 100.00 176 98.86 98.86 3.86e-121 SP P59343 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli CFT073]" 100.00 176 97.73 98.30 6.07e-120 SP Q0T5L6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Shigella flexneri 5 str. 8401]" 100.00 176 98.30 98.86 8.48e-121 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DsbA(C33S) Enterobacteria 562 Bacteria . Escherichia coli $DsbB Enterobacteria 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DsbA(C33S) 'recombinant technology' . Escherichia coli . pQE70 $DsbB 'recombinant technology' . Escherichia coli . pQE70 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_DsbA(C33S)_DsbB _Saveframe_category sample _Sample_type solid _Details 'membrane protein complex DsbA(C33S)/DsbB' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA(C33S) 6 mg '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % [U-2D] stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version 3.1 loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXRS _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_DsbA(C33S)_DsbB save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_DsbA(C33S)_DsbB save_ save_2D_CC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC' _Sample_label $sample_DsbA(C33S)_DsbB save_ save_2D_TEDOR_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TEDOR' _Sample_label $sample_DsbA(C33S)_DsbB save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 263 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 253 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect other other . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect other other . 0.101329118 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D NCACX' '3D NCOCX' stop_ loop_ _Sample_label $sample_DsbA(C33S)_DsbB stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DsbA(C33S) _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 4 4 GLU CA C 55.400 0.30 1 2 4 4 GLU CG C 36.800 0.30 1 3 5 5 ASP N N 125.848 0.30 1 4 6 6 GLY C C 173.119 0.30 1 5 6 6 GLY CA C 44.770 0.30 1 6 6 6 GLY N N 116.910 0.30 1 7 7 7 LYS CA C 57.384 0.30 1 8 7 7 LYS CB C 32.099 0.30 1 9 7 7 LYS CG C 25.144 0.30 1 10 7 7 LYS N N 122.456 0.30 1 11 8 8 GLN C C 173.952 0.30 1 12 8 8 GLN CA C 59.315 0.30 1 13 8 8 GLN CB C 26.993 0.30 1 14 8 8 GLN CG C 33.620 0.30 1 15 9 9 TYR C C 172.156 0.30 1 16 9 9 TYR CA C 54.800 0.30 1 17 9 9 TYR N N 111.349 0.30 1 18 10 10 THR C C 174.517 0.30 1 19 10 10 THR CA C 60.300 0.30 1 20 10 10 THR CB C 71.500 0.30 1 21 10 10 THR CG2 C 22.047 0.30 1 22 10 10 THR N N 111.374 0.30 1 23 11 11 THR C C 175.401 0.30 1 24 11 11 THR CA C 62.900 0.30 1 25 11 11 THR CB C 69.800 0.30 1 26 11 11 THR CG2 C 21.700 0.30 1 27 11 11 THR N N 120.544 0.30 1 28 12 12 LEU CA C 56.100 0.30 1 29 12 12 LEU CB C 41.538 0.30 1 30 12 12 LEU CG C 28.644 0.30 1 31 12 12 LEU CD1 C 24.311 0.30 2 32 12 12 LEU CD2 C 23.548 0.30 2 33 12 12 LEU N N 129.300 0.30 1 34 14 14 LYS N N 117.764 0.30 1 35 15 15 PRO CA C 62.478 0.30 1 36 15 15 PRO CB C 32.620 0.30 1 37 15 15 PRO CG C 27.385 0.30 1 38 15 15 PRO CD C 50.787 0.30 1 39 15 15 PRO N N 135.765 0.30 1 40 16 16 VAL C C 175.923 0.30 1 41 16 16 VAL CA C 61.330 0.30 1 42 16 16 VAL CB C 32.858 0.30 1 43 16 16 VAL CG1 C 21.698 0.30 2 44 16 16 VAL CG2 C 21.698 0.30 2 45 16 16 VAL N N 123.744 0.30 1 46 17 17 ALA C C 178.981 0.30 1 47 17 17 ALA CA C 52.255 0.30 1 48 17 17 ALA CB C 19.200 0.30 1 49 17 17 ALA N N 132.800 0.30 1 50 18 18 GLY CA C 45.487 0.30 1 51 18 18 GLY N N 111.191 0.30 1 52 19 19 ALA C C 175.340 0.30 1 53 19 19 ALA CA C 50.400 0.30 1 54 19 19 ALA CB C 17.297 0.30 1 55 19 19 ALA N N 122.097 0.30 1 56 20 20 PRO CA C 62.598 0.30 1 57 20 20 PRO CB C 31.807 0.30 1 58 20 20 PRO CG C 27.923 0.30 1 59 20 20 PRO CD C 50.282 0.30 1 60 20 20 PRO N N 134.142 0.30 1 61 22 22 VAL C C 172.928 0.30 1 62 22 22 VAL CA C 62.701 0.30 1 63 22 22 VAL CB C 34.082 0.30 1 64 22 22 VAL CG1 C 23.146 0.30 2 65 22 22 VAL CG2 C 21.393 0.30 2 66 23 23 LEU C C 173.410 0.30 1 67 23 23 LEU CA C 52.497 0.30 1 68 23 23 LEU CB C 46.123 0.30 1 69 23 23 LEU CG C 26.780 0.30 1 70 23 23 LEU CD1 C 22.479 0.30 1 71 23 23 LEU CD2 C 22.479 0.30 1 72 23 23 LEU N N 129.000 0.30 1 73 26 26 PHE C C 170.362 0.30 1 74 26 26 PHE CA C 55.351 0.30 1 75 27 27 SER C C 177.849 0.30 1 76 27 27 SER CA C 54.816 0.30 1 77 27 27 SER CB C 65.276 0.30 1 78 27 27 SER N N 107.820 0.30 1 79 28 28 PHE N N 131.179 0.30 1 80 39 39 VAL CA C 64.002 0.30 1 81 39 39 VAL CB C 32.551 0.30 1 82 39 39 VAL CG1 C 21.059 0.30 2 83 39 39 VAL N N 116.500 0.30 1 84 40 40 LEU CA C 55.364 0.30 1 85 40 40 LEU CG C 27.221 0.30 1 86 46 46 VAL CA C 66.993 0.30 1 87 46 46 VAL CB C 32.082 0.30 1 88 46 46 VAL CG1 C 24.121 0.30 2 89 46 46 VAL CG2 C 22.435 0.30 2 90 50 50 LEU CB C 41.200 0.30 1 91 51 51 PRO CA C 64.938 0.30 1 92 51 51 PRO CB C 31.970 0.30 1 93 51 51 PRO CG C 28.083 0.30 1 94 51 51 PRO CD C 52.565 0.30 1 95 51 51 PRO N N 153.189 0.30 1 96 53 53 GLY N N 111.404 0.30 1 97 54 54 VAL CA C 62.501 0.30 1 98 54 54 VAL CB C 31.670 0.30 1 99 54 54 VAL CG1 C 22.465 0.30 2 100 57 57 THR CA C 62.966 0.30 1 101 57 57 THR CB C 70.475 0.30 1 102 57 57 THR CG2 C 22.331 0.30 1 103 59 59 TYR CA C 52.062 0.30 1 104 59 59 TYR CB C 40.812 0.30 1 105 66 66 GLY C C 177.086 0.30 1 106 66 66 GLY CA C 45.537 0.30 1 107 67 67 ASP N N 129.097 0.30 1 108 68 68 LEU C C 179.175 0.30 1 109 68 68 LEU CA C 57.121 0.30 1 110 69 69 GLY CA C 47.963 0.30 1 111 69 69 GLY N N 106.917 0.30 1 112 72 72 LEU CA C 57.957 0.30 1 113 72 72 LEU CG C 28.388 0.30 1 114 73 73 THR C C 176.764 0.30 1 115 73 73 THR CA C 66.744 0.30 1 116 73 73 THR CB C 68.496 0.30 1 117 74 74 GLN CA C 59.734 0.30 1 118 74 74 GLN CB C 25.946 0.30 1 119 74 74 GLN N N 125.801 0.30 1 120 75 75 ALA CA C 54.726 0.30 1 121 75 75 ALA CB C 20.161 0.30 1 122 75 75 ALA N N 123.401 0.30 1 123 77 77 ALA CA C 55.200 0.30 1 124 77 77 ALA CB C 20.378 0.30 1 125 77 77 ALA N N 120.096 0.30 1 126 78 78 VAL C C 177.000 0.30 1 127 78 78 VAL CA C 66.900 0.30 1 128 78 78 VAL CB C 30.293 0.30 1 129 78 78 VAL CG1 C 23.624 0.30 2 130 78 78 VAL CG2 C 22.267 0.30 2 131 78 78 VAL N N 119.679 0.30 1 132 79 79 ALA C C 179.796 0.30 1 133 79 79 ALA CA C 54.726 0.30 1 134 79 79 ALA N N 120.811 0.30 1 135 80 80 MET C C 179.401 0.30 1 136 80 80 MET CA C 58.153 0.30 1 137 80 80 MET CB C 34.573 0.30 1 138 80 80 MET CG C 31.003 0.30 1 139 80 80 MET N N 115.652 0.30 1 140 81 81 ALA C C 180.222 0.30 1 141 81 81 ALA CA C 54.577 0.30 1 142 81 81 ALA N N 123.461 0.30 1 143 82 82 LEU C C 177.575 0.30 1 144 82 82 LEU CA C 54.404 0.30 1 145 82 82 LEU CB C 42.984 0.30 1 146 82 82 LEU CG C 26.964 0.30 1 147 82 82 LEU CD1 C 22.100 0.30 1 148 82 82 LEU CD2 C 22.100 0.30 1 149 82 82 LEU N N 113.178 0.30 1 150 83 83 GLY C C 176.909 0.30 1 151 83 83 GLY CA C 47.083 0.30 1 152 83 83 GLY N N 111.275 0.30 1 153 84 84 VAL C C 176.749 0.30 1 154 84 84 VAL CA C 59.102 0.30 1 155 84 84 VAL CB C 31.582 0.30 1 156 84 84 VAL CG1 C 20.582 0.30 2 157 84 84 VAL CG2 C 19.290 0.30 2 158 84 84 VAL N N 108.375 0.30 1 159 85 85 GLU C C 179.245 0.30 1 160 85 85 GLU CA C 61.539 0.30 1 161 85 85 GLU CB C 29.403 0.30 1 162 85 85 GLU CG C 36.312 0.30 1 163 85 85 GLU N N 126.854 0.30 1 164 86 86 ASP C C 177.583 0.30 1 165 86 86 ASP CA C 55.753 0.30 1 166 87 87 LYS C C 178.039 0.30 1 167 87 87 LYS CA C 57.366 0.30 1 168 87 87 LYS CB C 34.395 0.30 1 169 87 87 LYS CG C 25.718 0.30 1 170 87 87 LYS CD C 29.490 0.30 1 171 88 88 VAL C C 175.866 0.30 1 172 88 88 VAL CA C 60.535 0.30 1 173 88 88 VAL CB C 32.992 0.30 1 174 88 88 VAL CG1 C 19.473 0.30 2 175 88 88 VAL CG2 C 17.644 0.30 2 176 88 88 VAL N N 103.481 0.30 1 177 89 89 THR CA C 69.137 0.30 1 178 89 89 THR CG2 C 21.426 0.30 1 179 90 90 VAL C C 176.028 0.30 1 180 90 90 VAL CA C 69.447 0.30 1 181 90 90 VAL CB C 28.876 0.30 1 182 90 90 VAL CG1 C 24.694 0.30 2 183 90 90 VAL CG2 C 21.638 0.30 2 184 91 91 PRO N N 134.083 0.30 1 185 92 92 LEU CA C 58.013 0.30 1 186 92 92 LEU CB C 40.307 0.30 1 187 92 92 LEU CG C 27.137 0.30 1 188 92 92 LEU CD1 C 23.125 0.30 1 189 92 92 LEU CD2 C 23.125 0.30 1 190 94 94 GLU C C 180.235 0.30 1 191 94 94 GLU CA C 59.378 0.30 1 192 95 95 GLY C C 175.565 0.30 1 193 95 95 GLY CA C 46.033 0.30 1 194 95 95 GLY N N 107.790 0.30 1 195 96 96 VAL CA C 66.476 0.30 1 196 96 96 VAL CB C 32.243 0.30 1 197 96 96 VAL CG1 C 23.389 0.30 2 198 99 99 THR CA C 62.078 0.30 1 199 99 99 THR CB C 68.727 0.30 1 200 99 99 THR CG2 C 22.368 0.30 1 201 100 100 GLN C C 175.004 0.30 1 202 100 100 GLN CA C 57.357 0.30 1 203 100 100 GLN CB C 25.724 0.30 1 204 100 100 GLN CG C 34.618 0.30 1 205 101 101 THR C C 175.391 0.30 1 206 101 101 THR CA C 60.592 0.30 1 207 101 101 THR CB C 68.865 0.30 1 208 101 101 THR CG2 C 22.960 0.30 1 209 101 101 THR N N 105.649 0.30 1 210 102 102 ILE CA C 60.773 0.30 1 211 102 102 ILE CB C 36.956 0.30 1 212 102 102 ILE CG1 C 27.278 0.30 1 213 102 102 ILE CG2 C 17.457 0.30 1 214 102 102 ILE CD1 C 14.866 0.30 1 215 103 103 ARG CA C 55.029 0.30 1 216 103 103 ARG N N 125.129 0.30 1 217 104 104 SER CA C 56.499 0.30 1 218 104 104 SER CB C 67.404 0.30 1 219 104 104 SER N N 114.972 0.30 1 220 105 105 ALA C C 181.000 0.30 1 221 105 105 ALA CA C 54.976 0.30 1 222 105 105 ALA CB C 17.100 0.30 1 223 105 105 ALA N N 123.500 0.30 1 224 106 106 SER CA C 61.336 0.30 1 225 106 106 SER CB C 62.542 0.30 1 226 106 106 SER N N 116.024 0.30 1 227 107 107 ASP C C 178.883 0.30 1 228 108 108 ILE CA C 65.614 0.30 1 229 108 108 ILE CB C 38.333 0.30 1 230 108 108 ILE CG1 C 28.856 0.30 1 231 108 108 ILE CG2 C 18.532 0.30 1 232 108 108 ILE CD1 C 15.618 0.30 1 233 108 108 ILE N N 120.080 0.30 1 234 111 111 VAL CA C 66.402 0.30 1 235 111 111 VAL CB C 30.739 0.30 1 236 111 111 VAL CG1 C 23.631 0.30 2 237 111 111 VAL CG2 C 21.740 0.30 2 238 113 113 ILE C C 182.362 0.30 1 239 113 113 ILE CA C 63.762 0.30 1 240 113 113 ILE CB C 37.970 0.30 1 241 113 113 ILE CG1 C 28.281 0.30 1 242 113 113 ILE CG2 C 17.371 0.30 1 243 113 113 ILE CD1 C 13.802 0.30 1 244 114 114 ASN CA C 55.695 0.30 1 245 114 114 ASN CB C 37.871 0.30 1 246 114 114 ASN N N 121.071 0.30 1 247 115 115 ALA C C 176.912 0.30 1 248 115 115 ALA CA C 51.607 0.30 1 249 115 115 ALA CB C 19.099 0.30 1 250 115 115 ALA N N 120.639 0.30 1 251 116 116 GLY C C 173.782 0.30 1 252 116 116 GLY CA C 44.896 0.30 1 253 116 116 GLY N N 105.361 0.30 1 254 117 117 ILE CA C 60.988 0.30 1 255 117 117 ILE CB C 37.546 0.30 1 256 117 117 ILE CG1 C 25.886 0.30 1 257 117 117 ILE CG2 C 20.655 0.30 1 258 117 117 ILE N N 125.476 0.30 1 259 118 118 LYS C C 179.413 0.30 1 260 119 119 GLY N N 113.971 0.30 1 261 126 126 TRP CA C 61.507 0.30 1 262 126 126 TRP CB C 28.525 0.30 1 263 128 128 SER CA C 58.714 0.30 1 264 128 128 SER CB C 65.790 0.30 1 265 128 128 SER N N 116.192 0.30 1 266 130 130 VAL CA C 67.300 0.30 1 267 130 130 VAL CB C 30.374 0.30 1 268 131 131 VAL CA C 67.185 0.30 1 269 131 131 VAL CB C 31.455 0.30 1 270 134 134 LEU CB C 44.075 0.30 1 271 134 134 LEU CG C 27.321 0.30 1 272 135 135 VAL CA C 68.701 0.30 1 273 135 135 VAL CB C 31.453 0.30 1 274 135 135 VAL CG1 C 23.885 0.30 2 275 135 135 VAL CG2 C 21.404 0.30 2 276 135 135 VAL N N 123.026 0.30 1 277 136 136 ALA N N 121.026 0.30 1 278 141 141 ALA C C 179.649 0.30 1 279 141 141 ALA CA C 55.149 0.30 1 280 142 142 ALA CA C 53.949 0.30 1 281 142 142 ALA N N 116.928 0.30 1 282 143 143 ALA CA C 54.391 0.30 1 283 144 144 ASP C C 178.504 0.30 1 284 145 145 VAL CA C 60.384 0.30 1 285 145 145 VAL CB C 31.107 0.30 1 286 145 145 VAL CG1 C 20.126 0.30 2 287 145 145 VAL CG2 C 19.018 0.30 2 288 145 145 VAL N N 108.467 0.30 1 289 146 146 GLN CA C 55.921 0.30 1 290 146 146 GLN CB C 26.233 0.30 1 291 150 150 VAL CA C 58.211 0.30 1 292 150 150 VAL CG1 C 26.026 0.30 2 293 155 155 VAL CA C 60.944 0.30 1 294 155 155 VAL CB C 34.790 0.30 1 295 155 155 VAL CG1 C 22.864 0.30 2 296 155 155 VAL CG2 C 20.493 0.30 2 297 156 156 ASN C C 174.078 0.30 1 298 156 156 ASN CA C 54.605 0.30 1 299 156 156 ASN CB C 37.382 0.30 1 300 157 157 GLY C C 172.357 0.30 1 301 157 157 GLY CA C 45.960 0.30 1 302 157 157 GLY N N 105.310 0.30 1 303 158 158 LYS N N 114.286 0.30 1 304 160 160 GLN C C 175.725 0.30 1 305 160 160 GLN CA C 53.355 0.30 1 306 163 163 PRO CA C 64.860 0.30 1 307 163 163 PRO CB C 32.407 0.30 1 308 163 163 PRO CG C 27.992 0.30 1 309 163 163 PRO CD C 50.954 0.30 1 310 169 169 SER CA C 61.006 0.30 1 311 169 169 SER CB C 63.351 0.30 1 312 173 173 VAL CA C 65.799 0.30 1 313 173 173 VAL CB C 32.254 0.30 1 314 175 175 VAL CA C 66.812 0.30 1 315 175 175 VAL CB C 31.600 0.30 1 316 175 175 VAL CG1 C 21.371 0.30 2 317 175 175 VAL N N 116.900 0.30 1 318 182 182 VAL CA C 67.775 0.30 1 319 182 182 VAL CB C 30.882 0.30 1 320 182 182 VAL CG1 C 24.195 0.30 2 321 185 185 LEU CA C 56.749 0.30 1 322 185 185 LEU CB C 42.215 0.30 1 323 185 185 LEU CG C 25.753 0.30 1 stop_ save_