data_18493 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data ; _BMRB_accession_number 18493 _BMRB_flat_file_name bmr18493.str _Entry_type original _Submission_date 2012-05-30 _Accession_date 2012-05-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tang Ming . . 2 Sperling Lindsay J. . 3 Schwieters Charles D. . 4 Nesbitt Anna E. . 5 Gennis Robert B. . 6 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "13C chemical shifts" 552 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-24 update BMRB 'update entry citation' 2013-02-27 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23416557 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tang Ming . . 2 Nesbitt Anna E. . 3 Sperling Lindsay J. . 4 Berthold Deborah A. . 5 Schwieters Charles D. . 6 Gennis Robert B. . 7 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 425 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1670 _Page_last 1682 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DsbB C41S' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbB_1 $DsbB entity_2_1 $entity_2 entity_3_1 $entity_3 DsbB_2 $DsbB entity_2_2 $entity_2 entity_3_2 $entity_3 UBIQUINONE-1_1 $entity_UQ1 UBIQUINONE-1_2 $entity_UQ1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DsbB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbB _Molecular_mass 16663.053 _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP SVLCIYERVALFGVLGAALI GAIAPKTPLRYVAMVIWLYS AFRGVQLTYEHTMLQLYPSP FATCDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGL EMPQWLLGIFIAYLIVAVLV VISQPFKAKKRDLFGR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 ARG 4 PHE 5 LEU 6 ASN 7 GLN 8 ALA 9 SER 10 GLN 11 GLY 12 ARG 13 GLY 14 ALA 15 TRP 16 LEU 17 LEU 18 MET 19 ALA 20 PHE 21 THR 22 ALA 23 LEU 24 ALA 25 LEU 26 GLU 27 LEU 28 THR 29 ALA 30 LEU 31 TRP 32 PHE 33 GLN 34 HIS 35 VAL 36 MET 37 LEU 38 LEU 39 LYS 40 PRO 41 SER 42 VAL 43 LEU 44 CYS 45 ILE 46 TYR 47 GLU 48 ARG 49 VAL 50 ALA 51 LEU 52 PHE 53 GLY 54 VAL 55 LEU 56 GLY 57 ALA 58 ALA 59 LEU 60 ILE 61 GLY 62 ALA 63 ILE 64 ALA 65 PRO 66 LYS 67 THR 68 PRO 69 LEU 70 ARG 71 TYR 72 VAL 73 ALA 74 MET 75 VAL 76 ILE 77 TRP 78 LEU 79 TYR 80 SER 81 ALA 82 PHE 83 ARG 84 GLY 85 VAL 86 GLN 87 LEU 88 THR 89 TYR 90 GLU 91 HIS 92 THR 93 MET 94 LEU 95 GLN 96 LEU 97 TYR 98 PRO 99 SER 100 PRO 101 PHE 102 ALA 103 THR 104 CYS 105 ASP 106 PHE 107 MET 108 VAL 109 ARG 110 PHE 111 PRO 112 GLU 113 TRP 114 LEU 115 PRO 116 LEU 117 ASP 118 LYS 119 TRP 120 VAL 121 PRO 122 GLN 123 VAL 124 PHE 125 VAL 126 ALA 127 SER 128 GLY 129 ASP 130 CYS 131 ALA 132 GLU 133 ARG 134 GLN 135 TRP 136 ASP 137 PHE 138 LEU 139 GLY 140 LEU 141 GLU 142 MET 143 PRO 144 GLN 145 TRP 146 LEU 147 LEU 148 GLY 149 ILE 150 PHE 151 ILE 152 ALA 153 TYR 154 LEU 155 ILE 156 VAL 157 ALA 158 VAL 159 LEU 160 VAL 161 VAL 162 ILE 163 SER 164 GLN 165 PRO 166 PHE 167 LYS 168 ALA 169 LYS 170 LYS 171 ARG 172 ASP 173 LEU 174 PHE 175 GLY 176 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-22 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 100.00 186 100.00 100.00 1.36e-122 BMRB 15966 Disulfide_bond_formation_protein_B 100.00 183 97.73 97.73 1.34e-118 BMRB 18395 DsbB 100.00 176 99.43 99.43 1.46e-121 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 176 98.86 98.86 3.05e-120 PDB 2K73 "Solution Nmr Structure Of Integral Membrane Protein Dsbb" 100.00 183 97.73 97.73 1.34e-118 PDB 2K74 "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" 100.00 183 97.73 97.73 1.34e-118 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 3.05e-120 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 1.89e-122 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 176 98.86 98.86 3.05e-120 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 176 100.00 100.00 1.89e-122 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 182 99.43 99.43 1.25e-121 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 3.71e-120 DBJ BAB35103 "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.30 98.30 3.71e-120 DBJ BAG76757 "disulfide bond formation protein [Escherichia coli SE11]" 100.00 176 97.16 97.73 9.53e-119 DBJ BAI24997 "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" 100.00 176 97.73 98.30 7.63e-120 DBJ BAI30121 "oxidoreductase DsbB [Escherichia coli O103:H2 str. 12009]" 100.00 176 98.30 98.30 3.71e-120 EMBL CAP75720 "Disulfide bond formation protein B [Escherichia coli LF82]" 100.00 176 97.16 97.73 5.40e-119 EMBL CAQ31687 "DsbB[reduced] [Escherichia coli BL21(DE3)]" 100.00 176 98.30 98.30 3.71e-120 EMBL CAQ98064 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" 100.00 176 98.30 98.30 3.71e-120 EMBL CAR02574 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" 100.00 176 97.16 97.73 5.40e-119 EMBL CAR12682 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli UMN026]" 100.00 176 98.30 98.30 3.71e-120 GB AAA23711 "oxido-reductase [Escherichia coli]" 100.00 178 98.30 98.30 2.54e-120 GB AAB25233 "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" 100.00 176 98.30 98.30 3.71e-120 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 3.71e-120 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 2.25e-119 GB AAN42789 "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" 100.00 176 97.73 98.30 7.63e-120 PIR H85696 "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 176 97.73 97.73 2.25e-119 REF NP_309707 "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.30 98.30 3.71e-120 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 3.71e-120 REF NP_707082 "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" 100.00 176 97.73 98.30 7.63e-120 REF WP_000652474 "disulfide bond formation protein B, partial [Escherichia coli]" 69.32 122 100.00 100.00 1.06e-81 REF WP_000943442 "disulfide bond formation protein B [Escherichia coli]" 100.00 176 97.73 98.30 9.09e-120 SP A1AAA8 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 97.16 97.73 5.40e-119 SP P0A6M2 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 98.30 98.30 3.71e-120 SP P0A6M3 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 98.30 98.30 3.71e-120 SP P59343 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 97.16 97.73 5.40e-119 SP Q0T5L6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 97.73 98.30 7.63e-120 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 24077.834 _Mol_thiol_state . _Details . _Residue_count 239 _Mol_residue_sequence ; MDSQAQVLILLLLWVSGTCG DIVMSQSPSSLAVSAGEKVT MSCKSSQSLLNSRTRKNYLA WYQQKPGQSPKLLIYWASTR ESGVPDRFTGSGSGTDFTLT ISSVQAEDLAVYYCKQSYNL YTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCF LNNFYPKDINVKWKIDGSER QNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCE ATHKTSTSPIVKSFNRNEC ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 SER 4 GLN 5 ALA 6 GLN 7 VAL 8 LEU 9 ILE 10 LEU 11 LEU 12 LEU 13 LEU 14 TRP 15 VAL 16 SER 17 GLY 18 THR 19 CYS 20 GLY 21 ASP 22 ILE 23 VAL 24 MET 25 SER 26 GLN 27 SER 28 PRO 29 SER 30 SER 31 LEU 32 ALA 33 VAL 34 SER 35 ALA 36 GLY 37 GLU 38 LYS 39 VAL 40 THR 41 MET 42 SER 43 CYS 44 LYS 45 SER 46 SER 47 GLN 48 SER 49 LEU 50 LEU 51 ASN 52 SER 53 ARG 54 THR 55 ARG 56 LYS 57 ASN 58 TYR 59 LEU 60 ALA 61 TRP 62 TYR 63 GLN 64 GLN 65 LYS 66 PRO 67 GLY 68 GLN 69 SER 70 PRO 71 LYS 72 LEU 73 LEU 74 ILE 75 TYR 76 TRP 77 ALA 78 SER 79 THR 80 ARG 81 GLU 82 SER 83 GLY 84 VAL 85 PRO 86 ASP 87 ARG 88 PHE 89 THR 90 GLY 91 SER 92 GLY 93 SER 94 GLY 95 THR 96 ASP 97 PHE 98 THR 99 LEU 100 THR 101 ILE 102 SER 103 SER 104 VAL 105 GLN 106 ALA 107 GLU 108 ASP 109 LEU 110 ALA 111 VAL 112 TYR 113 TYR 114 CYS 115 LYS 116 GLN 117 SER 118 TYR 119 ASN 120 LEU 121 TYR 122 THR 123 PHE 124 GLY 125 GLY 126 GLY 127 THR 128 LYS 129 LEU 130 GLU 131 ILE 132 LYS 133 ARG 134 ALA 135 ASP 136 ALA 137 ALA 138 PRO 139 THR 140 VAL 141 SER 142 ILE 143 PHE 144 PRO 145 PRO 146 SER 147 SER 148 GLU 149 GLN 150 LEU 151 THR 152 SER 153 GLY 154 GLY 155 ALA 156 SER 157 VAL 158 VAL 159 CYS 160 PHE 161 LEU 162 ASN 163 ASN 164 PHE 165 TYR 166 PRO 167 LYS 168 ASP 169 ILE 170 ASN 171 VAL 172 LYS 173 TRP 174 LYS 175 ILE 176 ASP 177 GLY 178 SER 179 GLU 180 ARG 181 GLN 182 ASN 183 GLY 184 VAL 185 LEU 186 ASN 187 SER 188 TRP 189 THR 190 ASP 191 GLN 192 ASP 193 SER 194 LYS 195 ASP 196 SER 197 THR 198 TYR 199 SER 200 MET 201 SER 202 SER 203 THR 204 LEU 205 THR 206 LEU 207 THR 208 LYS 209 ASP 210 GLU 211 TYR 212 GLU 213 ARG 214 HIS 215 ASN 216 SER 217 TYR 218 THR 219 CYS 220 GLU 221 ALA 222 THR 223 HIS 224 LYS 225 THR 226 SER 227 THR 228 SER 229 PRO 230 ILE 231 VAL 232 LYS 233 SER 234 PHE 235 ASN 236 ARG 237 ASN 238 GLU 239 CYS 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 PDB 1Q9K "S25-2 Fab Unliganded 1" 91.63 219 99.09 99.54 8.93e-158 PDB 1Q9L "S25-2 Fab Unliganded 2" 91.63 219 99.09 99.54 8.93e-158 PDB 1Q9O "S45-18 Fab Unliganded" 91.63 219 97.72 98.63 6.68e-155 PDB 1Q9W "S45-18 Fab Pentasaccharide Bisphosphate Complex" 91.63 219 97.72 98.63 6.68e-155 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 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 PDB 2R1W "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R1X "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R1Y "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R23 "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R2B "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R2E "Crystal Structure Of S25-2 Fab In Complex With Kdo Analogues" 91.63 219 99.09 99.54 8.93e-158 PDB 2R2H "Structure Of S25-2 In Complex With Ko" 91.63 219 99.09 99.54 8.93e-158 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 239 100.00 100.00 4.28e-175 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 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 PDB 3HZM "Crystal Structure Of S73-2 Antibody In Complex With Antigen Kdo" 91.63 219 97.26 98.17 9.80e-155 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 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 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 PDB 3IJH "Structure Of S67-27 In Complex With Ko" 91.63 219 98.63 99.09 2.20e-156 PDB 3IJS "Structure Of S67-27 In Complex With Tsbp" 91.63 219 98.63 99.09 2.20e-156 PDB 3IJY "Structure Of S67-27 In Complex With Kdo(2.8)kdo" 91.63 218 98.17 98.63 9.92e-154 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 PDB 3KJ4 "Structure Of Rat Nogo Receptor Bound To 1d9 Antagonist Antibody" 91.63 219 97.72 98.17 6.05e-155 PDB 3SY0 "S25-2- A(2-8)-A(2-4)kdo Trisaccharide Complex" 91.63 219 99.09 99.54 8.93e-158 PDB 3T4Y "S25-2- Kdo Monosaccharide Complex" 91.63 219 99.09 99.54 8.93e-158 PDB 3T65 "S25-2- A(2-8)kdo Disaccharide Complex" 91.63 219 99.09 99.54 8.93e-158 PDB 3T77 "S25-2- A(2-4)kdo Disaccharide Complex" 91.63 219 99.09 99.54 8.93e-158 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 EMBL CAA75918 "variable region of immunoglobulin kappa light chain [Mus musculus]" 50.21 120 100.00 100.00 9.68e-79 GB AAA53292 "immunoglobulin kappa chain, partial [Mus musculus domesticus]" 61.92 148 97.97 98.65 2.87e-98 GB AAB47613 "polyreactive autoantibody, immunoglobulin light chain kappa, partial [Mus musculus]" 56.49 135 100.00 100.00 5.93e-91 GB AAL04472 "anti-InlB monoclonal antibody IgG1 light chain [Mus musculus]" 83.68 200 97.50 99.00 4.01e-140 GB AEB66102 "anti-prion immunoglobulin kappa light chain variable region [Mus musculus]" 50.21 120 97.50 100.00 8.25e-78 GB EDK98900 "mCG142167 [Mus musculus]" 51.05 122 99.18 99.18 7.21e-79 PIR G33932 "Ig kappa chain precursor V region (D23) - mouse" 50.21 120 99.17 99.17 6.35e-78 PIR PS0023 "Ig kappa chain precursor V region (6A4) - mouse" 55.65 133 97.74 98.50 1.67e-86 stop_ save_ save_entity_3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_3 _Molecular_mass 23024.885 _Mol_thiol_state . _Details . _Residue_count 221 _Mol_residue_sequence ; EVQLVESGGGLVKPGGSLKL SCAASGFAFSSYDMSWVRQT PEKRLEWVAYISSGGGSTYY PDTVKGRFTISRDNAKNTLY LQMSSLKSEDTAMYYCARPD YRSYAMDYWGQGTSVTVSSA KTTAPSVYPLAPVCGDTTGS SVTLGCLVKGYFPEPVTLTW NSGSLSSGVHTFPAVLQSDL YTLSSSVTVTSSTWPSQSIT CNVAHPASSTKVDKKIEPRG P ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 VAL 3 GLN 4 LEU 5 VAL 6 GLU 7 SER 8 GLY 9 GLY 10 GLY 11 LEU 12 VAL 13 LYS 14 PRO 15 GLY 16 GLY 17 SER 18 LEU 19 LYS 20 LEU 21 SER 22 CYS 23 ALA 24 ALA 25 SER 26 GLY 27 PHE 28 ALA 29 PHE 30 SER 31 SER 32 TYR 33 ASP 34 MET 35 SER 36 TRP 37 VAL 38 ARG 39 GLN 40 THR 41 PRO 42 GLU 43 LYS 44 ARG 45 LEU 46 GLU 47 TRP 48 VAL 49 ALA 50 TYR 51 ILE 52 SER 53 SER 54 GLY 55 GLY 56 GLY 57 SER 58 THR 59 TYR 60 TYR 61 PRO 62 ASP 63 THR 64 VAL 65 LYS 66 GLY 67 ARG 68 PHE 69 THR 70 ILE 71 SER 72 ARG 73 ASP 74 ASN 75 ALA 76 LYS 77 ASN 78 THR 79 LEU 80 TYR 81 LEU 82 GLN 83 MET 84 SER 85 SER 86 LEU 87 LYS 88 SER 89 GLU 90 ASP 91 THR 92 ALA 93 MET 94 TYR 95 TYR 96 CYS 97 ALA 98 ARG 99 PRO 100 ASP 101 TYR 102 ARG 103 SER 104 TYR 105 ALA 106 MET 107 ASP 108 TYR 109 TRP 110 GLY 111 GLN 112 GLY 113 THR 114 SER 115 VAL 116 THR 117 VAL 118 SER 119 SER 120 ALA 121 LYS 122 THR 123 THR 124 ALA 125 PRO 126 SER 127 VAL 128 TYR 129 PRO 130 LEU 131 ALA 132 PRO 133 VAL 134 CYS 135 GLY 136 ASP 137 THR 138 THR 139 GLY 140 SER 141 SER 142 VAL 143 THR 144 LEU 145 GLY 146 CYS 147 LEU 148 VAL 149 LYS 150 GLY 151 TYR 152 PHE 153 PRO 154 GLU 155 PRO 156 VAL 157 THR 158 LEU 159 THR 160 TRP 161 ASN 162 SER 163 GLY 164 SER 165 LEU 166 SER 167 SER 168 GLY 169 VAL 170 HIS 171 THR 172 PHE 173 PRO 174 ALA 175 VAL 176 LEU 177 GLN 178 SER 179 ASP 180 LEU 181 TYR 182 THR 183 LEU 184 SER 185 SER 186 SER 187 VAL 188 THR 189 VAL 190 THR 191 SER 192 SER 193 THR 194 TRP 195 PRO 196 SER 197 GLN 198 SER 199 ILE 200 THR 201 CYS 202 ASN 203 VAL 204 ALA 205 HIS 206 PRO 207 ALA 208 SER 209 SER 210 THR 211 LYS 212 VAL 213 ASP 214 LYS 215 LYS 216 ILE 217 GLU 218 PRO 219 ARG 220 GLY 221 PRO 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 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 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 221 100.00 100.00 2.13e-157 GB AAN06761 "immunoglobulin heavy chain variable region [Mus musculus]" 50.68 112 97.32 97.32 4.04e-69 stop_ save_ ############# # Ligands # ############# save_UQ1 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_UQ1 (UBIQUINONE-1)" _BMRB_code UQ1 _PDB_code UQ1 _Molecular_mass 250.290 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? CM2 CM2 C . 0 . ? C3 C3 C . 0 . ? O3 O3 O . 0 . ? CM3 CM3 C . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C5 C5 C . 0 . ? CM5 CM5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? HM21 HM21 H . 0 . ? HM22 HM22 H . 0 . ? HM23 HM23 H . 0 . ? HM31 HM31 H . 0 . ? HM32 HM32 H . 0 . ? HM33 HM33 H . 0 . ? HM51 HM51 H . 0 . ? HM52 HM52 H . 0 . ? HM53 HM53 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H8 H8 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H103 H103 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H113 H113 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 C2 ? ? SING C1 C6 ? ? SING C2 O2 ? ? DOUB C2 C3 ? ? SING O2 CM2 ? ? SING CM2 HM21 ? ? SING CM2 HM22 ? ? SING CM2 HM23 ? ? SING C3 O3 ? ? SING C3 C4 ? ? SING O3 CM3 ? ? SING CM3 HM31 ? ? SING CM3 HM32 ? ? SING CM3 HM33 ? ? DOUB C4 O4 ? ? SING C4 C5 ? ? SING C5 CM5 ? ? DOUB C5 C6 ? ? SING CM5 HM51 ? ? SING CM5 HM52 ? ? SING CM5 HM53 ? ? SING C6 C7 ? ? SING C7 C8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? DOUB C8 C9 ? ? SING C8 H8 ? ? SING C9 C10 ? ? SING C9 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C10 H103 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C11 H113 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $DsbB 'E. coli' 562 Bacteria . Escherichia coli K12 dsbB $entity_2 Mouse 10090 Eukaryota Metazoa Mus musculus . . $entity_3 Mouse 10090 Eukaryota Metazoa Mus musculus . . 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 $DsbB 'recombinant technology' . Escherichia coli . pqe70 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type membrane _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbB 7 mg '[U-100% 13C; U-100% 15N]' DDM 2 mg 'natural abundance' 'E. coli lipids' 7 mg 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type membrane _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbB 5 mg '[2-13C-glycerol; U-15N]' DDM 2 mg 'natural abundance' 'E. coli lipids' 7 mg 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type membrane _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbB 4 mg '[1,3-13C-glycerol; U-15N]' DDM 2 mg 'natural abundance' 'E. coli lipids' 7 mg 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 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_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ save_TALOS+ _Saveframe_category software _Name TALOS+ _Version . loop_ _Vendor _Address _Electronic_address 'Shen, Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_750 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_500 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXRS _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_CC_DARR_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_1 save_ save_2D_CC_DARR_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_2 save_ save_2D_CC_DARR_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_3 save_ save_3D_NCACX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'DsbB samples' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.8 . pH pressure 1 . atm temperature 261 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_Adam _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 'alkane carbons' ppm 40.48 external direct . 'separate solid-state NMR rotor' . 1 DSS N 15 'alkane carbons' ppm 40.48 external indirect . 'separate solid-state NMR rotor' . 0.4029799 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR' '3D NCACX' '3D NCOCX' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_Adam _Mol_system_component_name DsbB_1 _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 6 6 ASN C C 179.258 0.145 1 2 6 6 ASN CA C 57.564 0.300 1 3 6 6 ASN CB C 38.167 0.300 1 4 7 7 GLN H H 9.338 0.026 1 5 7 7 GLN C C 180.404 0.092 1 6 7 7 GLN CA C 57.611 0.012 1 7 7 7 GLN CB C 26.649 0.210 1 8 7 7 GLN CG C 31.228 0.300 1 9 7 7 GLN N N 120.525 0.189 1 10 8 8 ALA H H 9.436 0.052 1 11 8 8 ALA C C 179.313 0.300 1 12 8 8 ALA CA C 54.645 0.300 1 13 8 8 ALA CB C 17.967 0.300 1 14 8 8 ALA N N 123.894 0.176 1 15 9 9 SER C C 173.894 0.126 1 16 9 9 SER CA C 60.565 0.137 1 17 9 9 SER CB C 63.790 0.070 1 18 10 10 GLN H H 7.835 0.300 1 19 10 10 GLN C C 174.766 0.300 1 20 10 10 GLN CB C 29.955 0.300 1 21 10 10 GLN N N 119.198 0.200 1 22 11 11 GLY H H 8.433 0.005 1 23 11 11 GLY N N 108.456 0.067 1 24 12 12 ARG C C 178.053 0.300 1 25 12 12 ARG CA C 57.504 0.300 1 26 12 12 ARG CB C 30.522 0.300 1 27 12 12 ARG CD C 43.193 0.107 1 28 12 12 ARG CZ C 159.227 0.300 1 29 13 13 GLY C C 175.091 0.300 1 30 13 13 GLY CA C 45.326 0.300 1 31 13 13 GLY N N 108.265 0.300 1 32 14 14 ALA H H 9.285 0.003 1 33 14 14 ALA C C 179.173 0.300 1 34 14 14 ALA CA C 55.061 0.040 1 35 14 14 ALA N N 123.181 0.019 1 36 15 15 TRP H H 7.091 0.008 1 37 15 15 TRP C C 179.425 0.300 1 38 15 15 TRP CA C 58.960 0.074 1 39 15 15 TRP CB C 29.529 0.300 1 40 15 15 TRP N N 116.733 0.031 1 41 16 16 LEU H H 9.180 0.050 1 42 16 16 LEU C C 178.461 0.056 1 43 16 16 LEU CA C 58.246 0.034 1 44 16 16 LEU CB C 41.369 0.319 1 45 16 16 LEU CG C 26.762 0.221 1 46 16 16 LEU CD1 C 22.647 0.300 2 47 16 16 LEU CD2 C 22.647 0.300 2 48 16 16 LEU N N 118.671 0.093 1 49 17 17 LEU C C 178.787 0.311 1 50 17 17 LEU CA C 57.832 0.146 1 51 17 17 LEU CB C 41.395 0.071 1 52 17 17 LEU CG C 27.110 0.142 1 53 17 17 LEU CD1 C 22.055 0.300 2 54 17 17 LEU CD2 C 22.055 0.300 2 55 17 17 LEU N N 118.515 0.048 1 56 18 18 MET C C 180.469 0.190 1 57 18 18 MET CA C 60.277 0.110 1 58 18 18 MET CB C 31.789 0.165 1 59 18 18 MET CG C 33.392 0.223 1 60 18 18 MET N N 120.633 0.312 1 61 19 19 ALA H H 9.398 0.009 1 62 19 19 ALA C C 178.210 0.191 1 63 19 19 ALA CA C 55.468 0.147 1 64 19 19 ALA CB C 17.865 0.117 1 65 19 19 ALA N N 123.958 0.147 1 66 20 20 PHE C C 176.674 0.156 1 67 20 20 PHE CA C 62.546 0.197 1 68 20 20 PHE CB C 38.697 0.300 1 69 20 20 PHE N N 118.424 0.290 1 70 21 21 THR C C 174.203 0.226 1 71 21 21 THR CA C 66.052 0.521 1 72 21 21 THR CB C 68.956 0.583 1 73 21 21 THR CG2 C 22.538 0.082 1 74 21 21 THR N N 109.220 0.236 1 75 22 22 ALA C C 179.488 0.170 1 76 22 22 ALA CA C 54.847 0.162 1 77 22 22 ALA CB C 17.801 0.103 1 78 22 22 ALA N N 123.662 0.232 1 79 23 23 LEU H H 8.581 0.094 1 80 23 23 LEU C C 178.028 0.137 1 81 23 23 LEU CA C 57.713 0.168 1 82 23 23 LEU CB C 41.506 0.071 1 83 23 23 LEU CG C 26.938 0.112 1 84 23 23 LEU CD1 C 22.773 0.114 2 85 23 23 LEU CD2 C 22.797 0.300 2 86 23 23 LEU N N 118.917 0.139 1 87 24 24 ALA C C 180.617 0.253 1 88 24 24 ALA CA C 55.350 0.248 1 89 24 24 ALA CB C 17.583 0.160 1 90 24 24 ALA N N 119.931 0.087 1 91 25 25 LEU H H 9.179 0.015 1 92 25 25 LEU CA C 58.078 0.174 1 93 25 25 LEU CB C 43.597 0.156 1 94 25 25 LEU CG C 27.151 0.097 1 95 25 25 LEU CD1 C 23.596 0.300 2 96 25 25 LEU CD2 C 23.596 0.300 2 97 25 25 LEU N N 119.691 0.306 1 98 26 26 GLU C C 179.334 0.247 1 99 26 26 GLU CA C 59.584 0.068 1 100 26 26 GLU CB C 27.202 0.136 1 101 26 26 GLU N N 119.651 0.300 1 102 27 27 LEU H H 9.410 0.062 1 103 27 27 LEU CA C 57.887 0.086 1 104 27 27 LEU CB C 41.591 0.147 1 105 27 27 LEU CG C 27.146 0.010 1 106 27 27 LEU CD1 C 23.581 0.300 2 107 27 27 LEU CD2 C 23.581 0.300 2 108 27 27 LEU N N 119.661 0.205 1 109 28 28 THR C C 175.898 0.179 1 110 28 28 THR CA C 67.459 0.166 1 111 28 28 THR CB C 67.948 0.178 1 112 28 28 THR CG2 C 21.766 0.102 1 113 28 28 THR N N 118.484 0.098 1 114 29 29 ALA H H 8.302 0.020 1 115 29 29 ALA C C 179.717 0.245 1 116 29 29 ALA CA C 55.919 0.261 1 117 29 29 ALA CB C 16.837 0.362 1 118 29 29 ALA N N 122.643 0.176 1 119 30 30 LEU H H 8.412 0.023 1 120 30 30 LEU C C 178.143 0.127 1 121 30 30 LEU CA C 57.384 0.150 1 122 30 30 LEU CB C 41.679 0.199 1 123 30 30 LEU CG C 26.482 0.118 1 124 30 30 LEU CD1 C 22.521 0.291 2 125 30 30 LEU CD2 C 22.812 0.300 2 126 30 30 LEU N N 117.408 0.101 1 127 31 31 TRP H H 9.157 0.012 1 128 31 31 TRP C C 179.053 0.300 1 129 31 31 TRP CA C 59.005 0.007 1 130 31 31 TRP CB C 28.142 0.036 1 131 31 31 TRP N N 125.692 0.018 1 132 32 32 PHE H H 9.374 0.012 1 133 32 32 PHE CA C 61.557 0.239 1 134 32 32 PHE CB C 38.384 0.300 1 135 32 32 PHE N N 119.195 0.300 1 136 33 33 GLN C C 177.477 0.215 1 137 33 33 GLN CA C 56.613 0.300 1 138 33 33 GLN CB C 29.433 0.172 1 139 34 34 HIS H H 9.621 0.026 1 140 34 34 HIS C C 175.548 0.282 1 141 34 34 HIS CA C 58.733 0.049 1 142 34 34 HIS CB C 32.084 0.437 1 143 34 34 HIS CG C 137.404 2.253 1 144 34 34 HIS CD2 C 117.518 0.108 1 145 34 34 HIS CE1 C 139.690 0.204 1 146 34 34 HIS N N 115.948 0.073 1 147 35 35 VAL C C 177.853 0.300 1 148 35 35 VAL CA C 64.075 0.169 1 149 35 35 VAL CB C 30.626 0.051 1 150 35 35 VAL CG2 C 21.112 0.079 2 151 35 35 VAL N N 116.902 0.004 1 152 36 36 MET H H 7.605 0.034 1 153 36 36 MET C C 175.905 0.300 1 154 36 36 MET N N 114.145 0.036 1 155 37 37 LEU H H 7.121 0.026 1 156 37 37 LEU N N 111.740 0.034 1 157 38 38 LEU C C 176.457 0.300 1 158 39 39 LYS H H 9.359 0.022 1 159 39 39 LYS CA C 57.471 0.300 1 160 39 39 LYS N N 121.418 0.022 1 161 40 40 PRO CA C 60.451 0.300 1 162 40 40 PRO CD C 51.590 0.244 1 163 42 42 VAL C C 179.261 0.126 1 164 42 42 VAL CA C 67.223 0.316 1 165 42 42 VAL CB C 30.941 0.262 1 166 42 42 VAL CG1 C 23.413 0.300 2 167 42 42 VAL CG2 C 21.922 0.300 2 168 42 42 VAL N N 118.166 0.021 1 169 43 43 LEU C C 178.293 0.388 1 170 43 43 LEU CA C 57.129 0.094 1 171 43 43 LEU CB C 41.030 0.300 1 172 43 43 LEU CG C 26.666 0.153 1 173 43 43 LEU CD1 C 21.873 0.300 2 174 43 43 LEU CD2 C 21.866 0.300 2 175 43 43 LEU N N 115.946 0.075 1 176 44 44 CYS H H 7.683 0.032 1 177 44 44 CYS C C 177.484 0.210 1 178 44 44 CYS CA C 59.760 0.793 1 179 44 44 CYS CB C 30.651 2.786 1 180 44 44 CYS N N 115.006 0.814 1 181 45 45 ILE C C 179.575 0.247 1 182 45 45 ILE CA C 62.068 0.136 1 183 45 45 ILE CB C 33.583 0.345 1 184 45 45 ILE CG1 C 25.847 0.024 1 185 45 45 ILE CG2 C 19.220 0.032 1 186 45 45 ILE CD1 C 8.010 0.069 1 187 45 45 ILE N N 119.384 1.920 1 188 46 46 TYR H H 8.958 0.053 1 189 46 46 TYR C C 178.397 0.035 1 190 46 46 TYR CA C 59.129 0.181 1 191 46 46 TYR CB C 35.347 0.300 1 192 46 46 TYR N N 120.126 0.331 1 193 47 47 GLU H H 9.681 0.005 1 194 47 47 GLU C C 179.907 0.129 1 195 47 47 GLU CA C 57.985 0.177 1 196 47 47 GLU CB C 27.290 0.033 1 197 47 47 GLU CG C 34.938 0.029 1 198 47 47 GLU N N 121.779 0.043 1 199 48 48 ARG H H 9.213 0.020 1 200 48 48 ARG C C 181.638 0.106 1 201 48 48 ARG CA C 60.299 0.257 1 202 48 48 ARG CB C 30.167 0.112 1 203 48 48 ARG CG C 27.511 0.135 1 204 48 48 ARG CD C 44.371 0.055 1 205 48 48 ARG N N 119.188 0.232 1 206 49 49 VAL C C 177.326 0.183 1 207 49 49 VAL CA C 66.624 0.188 1 208 49 49 VAL CB C 31.280 0.211 1 209 49 49 VAL CG1 C 23.674 0.635 2 210 49 49 VAL CG2 C 22.427 0.073 2 211 49 49 VAL N N 121.326 0.053 1 212 50 50 ALA C C 179.594 0.173 1 213 50 50 ALA CA C 55.902 0.277 1 214 50 50 ALA CB C 16.623 0.162 1 215 50 50 ALA N N 122.955 0.356 1 216 51 51 LEU C C 177.990 0.294 1 217 51 51 LEU CA C 57.285 0.176 1 218 51 51 LEU CB C 41.369 0.192 1 219 51 51 LEU CG C 26.330 0.171 1 220 51 51 LEU CD1 C 21.941 0.300 2 221 51 51 LEU CD2 C 21.771 0.300 2 222 51 51 LEU N N 115.737 0.292 1 223 52 52 PHE H H 8.863 0.012 1 224 52 52 PHE C C 179.142 0.183 1 225 52 52 PHE CA C 62.518 0.122 1 226 52 52 PHE CB C 38.538 0.270 1 227 52 52 PHE N N 122.707 0.169 1 228 53 53 GLY H H 9.027 0.010 1 229 53 53 GLY C C 175.378 0.225 1 230 53 53 GLY CA C 48.024 0.224 1 231 53 53 GLY N N 110.801 0.218 1 232 54 54 VAL H H 7.948 0.031 1 233 54 54 VAL C C 177.035 0.204 1 234 54 54 VAL CA C 67.448 0.162 1 235 54 54 VAL CB C 31.246 0.206 1 236 54 54 VAL CG1 C 22.269 0.108 2 237 54 54 VAL CG2 C 21.012 0.177 2 238 54 54 VAL N N 121.926 0.158 1 239 55 55 LEU H H 8.646 0.011 1 240 55 55 LEU C C 178.175 0.460 1 241 55 55 LEU CA C 58.490 0.316 1 242 55 55 LEU CB C 42.145 0.159 1 243 55 55 LEU CG C 27.014 0.300 1 244 55 55 LEU CD1 C 25.695 0.248 2 245 55 55 LEU CD2 C 25.376 0.300 2 246 55 55 LEU N N 119.894 0.170 1 247 56 56 GLY C C 174.618 0.131 1 248 56 56 GLY CA C 47.533 0.198 1 249 56 56 GLY N N 106.262 0.109 1 250 57 57 ALA C C 178.688 0.218 1 251 57 57 ALA CA C 55.548 0.187 1 252 57 57 ALA CB C 18.065 0.120 1 253 57 57 ALA N N 123.002 0.111 1 254 58 58 ALA H H 8.674 0.003 1 255 58 58 ALA C C 179.348 0.158 1 256 58 58 ALA CA C 54.763 0.258 1 257 58 58 ALA CB C 17.898 0.175 1 258 58 58 ALA N N 118.866 0.161 1 259 59 59 LEU C C 177.654 0.300 1 260 59 59 LEU CA C 57.387 0.155 1 261 59 59 LEU CB C 41.209 0.158 1 262 59 59 LEU CG C 26.283 0.075 1 263 59 59 LEU CD1 C 21.815 0.300 2 264 59 59 LEU CD2 C 21.744 0.300 2 265 59 59 LEU N N 115.384 0.135 1 266 60 60 ILE C C 180.024 0.233 1 267 60 60 ILE CA C 64.263 0.278 1 268 60 60 ILE CB C 37.240 0.208 1 269 60 60 ILE CG1 C 29.859 0.184 1 270 60 60 ILE CG2 C 16.881 0.091 1 271 60 60 ILE CD1 C 13.606 0.125 1 272 60 60 ILE N N 116.140 0.148 1 273 61 61 GLY H H 9.046 0.002 1 274 61 61 GLY C C 173.716 0.189 1 275 61 61 GLY CA C 45.617 0.114 1 276 61 61 GLY N N 110.127 0.293 1 277 62 62 ALA H H 8.066 0.012 1 278 62 62 ALA C C 176.192 0.092 1 279 62 62 ALA CA C 53.268 0.146 1 280 62 62 ALA CB C 19.138 0.103 1 281 62 62 ALA N N 118.949 0.237 1 282 63 63 ILE CA C 66.739 0.151 1 283 63 63 ILE CB C 37.947 0.160 1 284 63 63 ILE CG1 C 29.043 0.468 1 285 63 63 ILE CG2 C 16.921 0.191 1 286 63 63 ILE CD1 C 14.543 0.153 1 287 63 63 ILE N N 116.800 0.227 1 288 64 64 ALA CA C 52.934 0.136 1 289 64 64 ALA CB C 19.428 0.300 1 290 64 64 ALA N N 123.957 0.300 1 291 65 65 PRO CA C 65.350 0.030 1 292 65 65 PRO CG C 27.611 0.063 1 293 65 65 PRO CD C 51.485 0.275 1 294 65 65 PRO N N 128.226 0.174 1 295 66 66 LYS C C 177.500 0.300 1 296 66 66 LYS CA C 56.547 0.110 1 297 66 66 LYS CB C 30.522 0.300 1 298 66 66 LYS CE C 42.222 0.076 1 299 66 66 LYS N N 116.618 0.155 1 300 67 67 THR CA C 60.452 0.240 1 301 67 67 THR CB C 69.948 0.041 1 302 67 67 THR CG2 C 21.879 0.061 1 303 68 68 PRO C C 177.070 0.300 1 304 68 68 PRO CA C 63.315 0.033 1 305 68 68 PRO CB C 32.458 0.117 1 306 68 68 PRO CG C 28.010 0.008 1 307 68 68 PRO CD C 51.735 0.207 1 308 68 68 PRO N N 129.713 0.223 1 309 69 69 LEU H H 8.882 0.010 1 310 69 69 LEU C C 179.448 0.164 1 311 69 69 LEU CA C 57.389 0.300 1 312 69 69 LEU CB C 42.737 0.300 1 313 69 69 LEU CG C 26.295 0.300 1 314 69 69 LEU CD1 C 23.591 0.300 2 315 69 69 LEU CD2 C 23.617 0.300 2 316 69 69 LEU N N 121.517 0.015 1 317 70 70 ARG H H 8.202 0.037 1 318 70 70 ARG C C 177.925 0.300 1 319 70 70 ARG CA C 58.429 0.227 1 320 70 70 ARG CB C 29.391 0.149 1 321 70 70 ARG CG C 26.748 0.071 1 322 70 70 ARG CD C 44.579 0.104 1 323 70 70 ARG CZ C 159.739 0.300 1 324 70 70 ARG N N 114.028 0.148 1 325 71 71 TYR H H 8.136 0.015 1 326 71 71 TYR CA C 57.374 0.092 1 327 71 71 TYR N N 121.740 0.015 1 328 72 72 VAL C C 177.702 0.132 1 329 72 72 VAL CA C 66.098 0.174 1 330 72 72 VAL CB C 31.343 0.089 1 331 72 72 VAL CG1 C 22.760 0.073 2 332 72 72 VAL CG2 C 21.150 0.404 2 333 72 72 VAL N N 118.416 0.293 1 334 73 73 ALA H H 9.015 0.030 1 335 73 73 ALA C C 179.763 0.155 1 336 73 73 ALA CA C 55.785 0.150 1 337 73 73 ALA CB C 19.265 0.132 1 338 73 73 ALA N N 120.283 0.342 1 339 74 74 MET H H 8.163 0.008 1 340 74 74 MET C C 177.223 0.236 1 341 74 74 MET CA C 61.023 0.161 1 342 74 74 MET CB C 33.777 0.092 1 343 74 74 MET CG C 35.778 0.203 1 344 74 74 MET N N 115.547 0.203 1 345 75 75 VAL H H 7.554 0.034 1 346 75 75 VAL C C 177.166 0.124 1 347 75 75 VAL CA C 67.581 0.250 1 348 75 75 VAL CB C 31.408 0.100 1 349 75 75 VAL CG1 C 23.448 0.034 2 350 75 75 VAL CG2 C 21.778 0.300 2 351 75 75 VAL N N 118.690 0.254 1 352 76 76 ILE C C 178.680 0.168 1 353 76 76 ILE CA C 65.839 0.221 1 354 76 76 ILE CB C 38.414 0.257 1 355 76 76 ILE CG1 C 31.176 0.211 1 356 76 76 ILE CG2 C 17.003 0.122 1 357 76 76 ILE CD1 C 14.703 0.196 1 358 76 76 ILE N N 118.959 0.210 1 359 77 77 TRP H H 9.515 0.015 1 360 77 77 TRP C C 177.153 0.135 1 361 77 77 TRP CA C 58.779 0.111 1 362 77 77 TRP CB C 30.494 0.281 1 363 77 77 TRP CG C 114.126 0.300 1 364 77 77 TRP CD1 C 122.582 0.300 4 365 77 77 TRP N N 125.440 0.096 1 366 78 78 LEU H H 9.367 0.005 1 367 78 78 LEU C C 178.381 0.099 1 368 78 78 LEU CA C 58.041 0.256 1 369 78 78 LEU CB C 43.807 0.230 1 370 78 78 LEU CG C 27.131 0.216 1 371 78 78 LEU CD1 C 23.311 0.300 2 372 78 78 LEU CD2 C 23.168 0.300 2 373 78 78 LEU N N 118.968 0.194 1 374 79 79 TYR C C 176.777 0.210 1 375 79 79 TYR CA C 62.849 0.235 1 376 79 79 TYR N N 118.181 0.222 1 377 80 80 SER C C 175.943 0.092 1 378 80 80 SER CA C 63.515 0.093 1 379 80 80 SER CB C 63.941 0.300 1 380 80 80 SER N N 114.286 0.173 1 381 81 81 ALA C C 178.208 0.148 1 382 81 81 ALA CA C 55.224 0.139 1 383 81 81 ALA CB C 17.897 0.096 1 384 81 81 ALA N N 121.070 0.164 1 385 82 82 PHE C C 176.975 0.033 1 386 82 82 PHE CA C 62.132 0.255 1 387 82 82 PHE CB C 38.497 0.300 1 388 82 82 PHE N N 117.560 0.068 1 389 83 83 ARG C C 178.637 0.085 1 390 83 83 ARG CA C 60.291 0.584 1 391 83 83 ARG CB C 28.625 0.036 1 392 83 83 ARG CG C 26.715 0.649 1 393 83 83 ARG CD C 43.764 0.100 1 394 83 83 ARG N N 117.110 0.185 1 395 84 84 GLY C C 177.091 0.256 1 396 84 84 GLY CA C 46.128 0.261 1 397 84 84 GLY N N 105.915 0.270 1 398 85 85 VAL C C 176.387 0.304 1 399 85 85 VAL CA C 66.960 0.198 1 400 85 85 VAL CB C 31.066 0.289 1 401 85 85 VAL CG1 C 23.638 0.278 2 402 85 85 VAL CG2 C 21.858 0.069 2 403 85 85 VAL N N 124.985 0.240 1 404 86 86 GLN C C 179.586 0.523 1 405 86 86 GLN CA C 59.505 0.113 1 406 86 86 GLN CB C 28.762 0.269 1 407 86 86 GLN CG C 34.909 0.059 1 408 86 86 GLN N N 116.522 0.164 1 409 87 87 LEU H H 8.955 0.025 1 410 87 87 LEU C C 178.396 0.357 1 411 87 87 LEU CA C 57.847 0.244 1 412 87 87 LEU CB C 41.924 0.206 1 413 87 87 LEU CG C 26.767 0.247 1 414 87 87 LEU CD1 C 23.627 0.300 2 415 87 87 LEU CD2 C 23.596 0.300 2 416 87 87 LEU N N 121.211 0.179 1 417 88 88 THR H H 8.764 0.046 1 418 88 88 THR C C 180.013 0.300 1 419 88 88 THR CA C 65.112 0.115 1 420 88 88 THR CB C 68.805 0.088 1 421 88 88 THR CG2 C 24.796 0.115 1 422 88 88 THR N N 108.251 0.245 1 423 89 89 TYR H H 9.868 0.002 1 424 89 89 TYR C C 177.244 0.300 1 425 89 89 TYR N N 127.947 0.039 1 426 90 90 GLU H H 8.515 0.020 1 427 90 90 GLU C C 178.671 0.348 1 428 90 90 GLU N N 121.163 0.032 1 429 91 91 HIS H H 9.102 0.008 1 430 91 91 HIS C C 177.605 0.067 1 431 91 91 HIS CA C 57.085 0.057 1 432 91 91 HIS CB C 34.128 0.104 1 433 91 91 HIS CG C 136.131 0.120 1 434 91 91 HIS CD2 C 113.845 0.059 1 435 91 91 HIS CE1 C 141.123 0.064 1 436 91 91 HIS N N 120.459 0.180 1 437 92 92 THR H H 9.550 0.009 1 438 92 92 THR C C 176.189 0.300 1 439 92 92 THR CA C 67.058 0.205 1 440 92 92 THR CB C 68.564 0.183 1 441 92 92 THR CG2 C 27.476 0.300 1 442 92 92 THR N N 115.463 0.141 1 443 93 93 MET C C 176.972 0.093 1 444 93 93 MET CA C 62.369 0.117 1 445 93 93 MET CB C 33.515 0.300 1 446 93 93 MET CG C 35.406 0.300 1 447 93 93 MET N N 117.153 0.150 1 448 94 94 LEU H H 8.497 0.300 1 449 94 94 LEU CA C 57.489 0.077 1 450 94 94 LEU CB C 41.432 0.089 1 451 94 94 LEU CG C 26.603 0.055 1 452 94 94 LEU CD1 C 22.658 0.101 2 453 94 94 LEU CD2 C 22.759 0.300 2 454 94 94 LEU N N 117.981 0.315 1 455 95 95 GLN C C 178.331 0.045 1 456 95 95 GLN CA C 57.604 0.300 1 457 95 95 GLN CB C 28.200 0.300 1 458 96 96 LEU C C 177.842 0.134 1 459 96 96 LEU CA C 57.747 0.300 1 460 96 96 LEU CB C 41.721 0.068 1 461 96 96 LEU CG C 27.022 0.300 1 462 96 96 LEU CD1 C 23.513 0.300 2 463 96 96 LEU CD2 C 22.940 0.300 2 464 96 96 LEU N N 118.174 0.129 1 465 97 97 TYR H H 8.485 0.004 1 466 97 97 TYR CA C 57.581 0.199 1 467 97 97 TYR N N 117.359 0.153 1 468 98 98 PRO CA C 63.847 0.300 1 469 98 98 PRO CD C 50.919 0.110 1 470 98 98 PRO N N 130.765 0.300 1 471 99 99 SER CA C 58.145 0.263 1 472 99 99 SER CB C 64.506 0.157 1 473 100 100 PRO CD C 50.825 0.084 1 474 100 100 PRO N N 130.137 0.300 1 475 101 101 PHE C C 174.992 0.300 1 476 102 102 ALA H H 7.383 0.024 1 477 102 102 ALA C C 176.810 0.300 1 478 102 102 ALA CA C 54.355 0.017 1 479 102 102 ALA N N 120.614 0.024 1 480 103 103 THR H H 9.278 0.020 1 481 103 103 THR C C 175.666 0.155 1 482 103 103 THR CA C 59.838 0.300 1 483 103 103 THR CB C 67.623 0.300 1 484 103 103 THR CG2 C 20.002 0.300 1 485 103 103 THR N N 112.507 0.194 1 486 104 104 CYS H H 9.934 0.012 1 487 104 104 CYS C C 174.474 0.300 1 488 104 104 CYS CA C 64.988 0.300 1 489 104 104 CYS CB C 42.988 0.300 1 490 104 104 CYS N N 122.754 0.031 1 491 105 105 ASP H H 8.153 0.005 1 492 105 105 ASP CB C 41.030 0.300 1 493 105 105 ASP N N 121.350 0.012 1 494 108 108 VAL C C 175.472 0.115 1 495 108 108 VAL CA C 61.483 0.237 1 496 108 108 VAL CB C 32.076 0.300 1 497 108 108 VAL CG1 C 22.907 0.056 2 498 108 108 VAL CG2 C 21.098 0.044 2 499 108 108 VAL N N 112.506 0.026 1 500 109 109 ARG N N 112.150 0.050 1 501 110 110 PHE CA C 58.681 0.114 1 502 111 111 PRO CA C 65.848 0.300 1 503 111 111 PRO CD C 51.081 0.220 1 504 112 112 GLU C C 177.165 0.300 1 505 113 113 TRP H H 9.706 0.060 1 506 113 113 TRP CA C 53.381 0.091 1 507 113 113 TRP N N 111.820 0.076 1 508 114 114 LEU CB C 41.351 0.300 1 509 115 115 PRO CA C 61.148 0.061 1 510 115 115 PRO CB C 30.280 0.008 1 511 115 115 PRO CG C 26.706 0.066 1 512 115 115 PRO CD C 49.865 0.001 1 513 116 116 LEU C C 178.163 0.059 1 514 116 116 LEU CA C 58.746 0.037 1 515 116 116 LEU CB C 42.932 0.300 1 516 116 116 LEU CG C 26.521 0.300 1 517 117 117 ASP C C 177.528 0.082 1 518 117 117 ASP CB C 41.252 0.054 1 519 117 117 ASP N N 116.302 0.080 1 520 118 118 LYS H H 7.538 0.036 1 521 118 118 LYS CD C 27.953 0.098 1 522 118 118 LYS N N 118.983 0.119 1 523 119 119 TRP C C 177.867 0.300 1 524 120 120 VAL H H 8.936 0.019 1 525 120 120 VAL CA C 58.651 0.114 1 526 120 120 VAL CB C 31.821 0.110 1 527 120 120 VAL CG2 C 20.697 0.300 2 528 120 120 VAL N N 113.149 0.024 1 529 121 121 PRO C C 178.888 0.300 1 530 121 121 PRO CA C 65.185 0.015 1 531 121 121 PRO CB C 31.781 0.162 1 532 121 121 PRO CG C 27.660 0.300 1 533 121 121 PRO CD C 50.590 0.079 1 534 122 122 GLN H H 9.809 0.005 1 535 122 122 GLN C C 174.326 0.300 1 536 122 122 GLN CA C 58.463 0.300 1 537 122 122 GLN N N 116.304 0.039 1 538 123 123 VAL H H 8.219 0.004 1 539 123 123 VAL C C 175.777 0.065 1 540 123 123 VAL CA C 61.689 0.292 1 541 123 123 VAL CB C 35.373 0.087 1 542 123 123 VAL CG2 C 21.181 0.300 2 543 123 123 VAL N N 113.254 0.054 1 544 124 124 PHE C C 172.759 0.249 1 545 124 124 PHE CB C 39.318 0.300 1 546 124 124 PHE N N 112.242 0.017 1 547 125 125 VAL H H 7.799 0.022 1 548 125 125 VAL C C 177.034 0.300 1 549 125 125 VAL CA C 61.950 0.164 1 550 125 125 VAL CB C 33.376 0.164 1 551 125 125 VAL CG1 C 24.379 0.300 2 552 125 125 VAL CG2 C 21.389 0.300 2 553 125 125 VAL N N 115.233 0.352 1 554 126 126 ALA H H 9.014 0.030 1 555 126 126 ALA C C 175.920 0.300 1 556 126 126 ALA CA C 54.493 0.067 1 557 126 126 ALA CB C 17.215 0.018 1 558 126 126 ALA N N 130.709 0.039 1 559 127 127 SER H H 8.145 0.026 1 560 127 127 SER CA C 58.101 0.300 1 561 127 127 SER CB C 64.539 0.300 1 562 127 127 SER N N 112.716 0.005 1 563 128 128 GLY H H 8.595 0.058 1 564 128 128 GLY C C 177.047 0.300 1 565 128 128 GLY CA C 46.296 0.123 1 566 128 128 GLY N N 106.487 0.017 1 567 129 129 ASP C C 177.916 0.300 1 568 129 129 ASP CB C 43.975 0.134 1 569 130 130 CYS H H 9.948 0.003 1 570 130 130 CYS C C 173.312 0.300 1 571 130 130 CYS CA C 64.581 0.074 1 572 130 130 CYS CB C 42.879 0.043 1 573 130 130 CYS N N 122.984 0.016 1 574 131 131 ALA H H 9.869 0.029 1 575 131 131 ALA CA C 52.640 0.300 1 576 131 131 ALA CB C 18.497 0.300 1 577 131 131 ALA N N 121.534 0.128 1 578 136 136 ASP C C 172.916 0.300 1 579 137 137 PHE H H 8.959 0.005 1 580 137 137 PHE CA C 57.310 0.300 1 581 137 137 PHE CB C 42.927 0.300 1 582 137 137 PHE N N 117.677 0.047 1 583 138 138 LEU CB C 43.547 0.300 1 584 139 139 GLY C C 176.262 0.300 1 585 139 139 GLY CA C 46.123 0.300 1 586 140 140 LEU CB C 40.503 0.012 1 587 140 140 LEU N N 124.207 0.300 1 588 142 142 MET CA C 56.442 0.300 1 589 143 143 PRO CA C 63.254 0.300 1 590 143 143 PRO CD C 51.480 0.002 1 591 144 144 GLN C C 177.307 0.300 1 592 145 145 TRP H H 8.386 0.037 1 593 145 145 TRP C C 178.709 0.579 1 594 145 145 TRP CA C 59.535 0.203 1 595 145 145 TRP CB C 29.345 0.087 1 596 145 145 TRP N N 120.795 0.006 1 597 146 146 LEU H H 9.033 0.008 1 598 146 146 LEU C C 177.115 0.169 1 599 146 146 LEU CA C 57.793 0.385 1 600 146 146 LEU CB C 41.616 0.072 1 601 146 146 LEU CG C 26.151 0.009 1 602 146 146 LEU CD1 C 22.670 0.300 2 603 146 146 LEU CD2 C 22.670 0.300 2 604 146 146 LEU N N 118.336 0.119 1 605 147 147 LEU H H 8.480 0.032 1 606 147 147 LEU C C 178.787 0.168 1 607 147 147 LEU CA C 58.052 0.132 1 608 147 147 LEU CB C 41.047 0.213 1 609 147 147 LEU CG C 27.480 0.266 1 610 147 147 LEU CD1 C 24.363 0.026 2 611 147 147 LEU CD2 C 22.324 0.300 2 612 147 147 LEU N N 123.772 0.148 1 613 148 148 GLY C C 174.667 0.213 1 614 148 148 GLY CA C 48.102 0.256 1 615 148 148 GLY N N 104.457 0.229 1 616 149 149 ILE C C 177.725 0.126 1 617 149 149 ILE CA C 65.997 0.108 1 618 149 149 ILE CB C 38.262 0.126 1 619 149 149 ILE CG1 C 30.092 0.146 1 620 149 149 ILE CG2 C 18.028 0.134 1 621 149 149 ILE CD1 C 14.653 0.089 1 622 149 149 ILE N N 121.815 0.134 1 623 150 150 PHE C C 178.929 0.079 1 624 150 150 PHE CA C 63.591 0.298 1 625 150 150 PHE CB C 38.417 0.314 1 626 150 150 PHE N N 118.894 0.361 1 627 151 151 ILE C C 177.347 0.160 1 628 151 151 ILE CA C 66.478 0.132 1 629 151 151 ILE CB C 37.302 0.117 1 630 151 151 ILE CG1 C 30.856 0.230 1 631 151 151 ILE CG2 C 17.909 0.177 1 632 151 151 ILE CD1 C 14.457 0.178 1 633 151 151 ILE N N 120.535 0.091 1 634 152 152 ALA C C 179.165 0.094 1 635 152 152 ALA CA C 56.272 0.115 1 636 152 152 ALA CB C 17.993 0.103 1 637 152 152 ALA N N 122.855 0.199 1 638 153 153 TYR H H 8.680 0.007 1 639 153 153 TYR C C 179.682 0.090 1 640 153 153 TYR CA C 64.391 0.144 1 641 153 153 TYR CB C 39.553 0.044 1 642 153 153 TYR N N 116.156 0.294 1 643 154 154 LEU C C 177.336 0.292 1 644 154 154 LEU CA C 57.905 0.125 1 645 154 154 LEU CB C 42.009 0.114 1 646 154 154 LEU CG C 27.063 0.030 1 647 154 154 LEU CD1 C 23.943 0.300 2 648 154 154 LEU CD2 C 22.797 0.300 2 649 154 154 LEU N N 122.327 0.136 1 650 155 155 ILE C C 177.589 0.123 1 651 155 155 ILE CA C 65.996 0.180 1 652 155 155 ILE CB C 38.179 0.112 1 653 155 155 ILE CG1 C 31.527 0.034 1 654 155 155 ILE CG2 C 17.923 0.076 1 655 155 155 ILE CD1 C 14.649 0.300 1 656 155 155 ILE N N 119.079 0.131 1 657 156 156 VAL C C 176.163 0.083 1 658 156 156 VAL CA C 67.664 0.259 1 659 156 156 VAL CB C 31.694 0.103 1 660 156 156 VAL CG1 C 23.147 0.045 2 661 156 156 VAL CG2 C 24.386 0.096 2 662 156 156 VAL N N 117.551 0.129 1 663 157 157 ALA C C 179.076 0.203 1 664 157 157 ALA CA C 54.803 0.135 1 665 157 157 ALA CB C 16.120 0.235 1 666 157 157 ALA N N 122.470 0.107 1 667 158 158 VAL C C 177.491 0.045 1 668 158 158 VAL CA C 67.160 0.189 1 669 158 158 VAL CB C 31.331 0.082 1 670 158 158 VAL CG1 C 23.576 0.075 2 671 158 158 VAL CG2 C 21.967 0.129 2 672 158 158 VAL N N 116.045 0.145 1 673 159 159 LEU C C 178.312 0.157 1 674 159 159 LEU CA C 57.443 0.243 1 675 159 159 LEU CB C 41.567 0.272 1 676 159 159 LEU CG C 26.578 0.379 1 677 159 159 LEU CD1 C 22.883 0.300 2 678 159 159 LEU CD2 C 22.883 0.300 2 679 159 159 LEU N N 116.776 0.142 1 680 160 160 VAL C C 177.508 0.079 1 681 160 160 VAL CA C 67.366 0.181 1 682 160 160 VAL CB C 31.106 0.253 1 683 160 160 VAL CG1 C 23.638 0.193 2 684 160 160 VAL CG2 C 21.784 0.300 2 685 160 160 VAL N N 118.890 0.153 1 686 161 161 VAL C C 176.607 0.060 1 687 161 161 VAL CA C 67.614 0.156 1 688 161 161 VAL CB C 31.646 0.056 1 689 161 161 VAL CG1 C 23.255 0.068 2 690 161 161 VAL CG2 C 21.814 0.205 2 691 161 161 VAL N N 118.360 0.217 1 692 162 162 ILE C C 176.885 0.300 1 693 162 162 ILE CA C 63.409 0.074 1 694 162 162 ILE CB C 39.685 0.186 1 695 162 162 ILE CG1 C 31.399 0.300 1 696 162 162 ILE CG2 C 18.101 0.045 1 697 163 163 SER H H 9.427 0.022 1 698 163 163 SER CA C 60.441 0.222 1 699 163 163 SER CB C 63.788 0.300 1 700 163 163 SER N N 112.832 0.300 1 701 165 165 PRO CA C 62.249 0.011 1 702 165 165 PRO CD C 51.723 0.128 1 703 165 165 PRO N N 134.035 0.022 1 704 168 168 ALA CA C 51.195 0.007 1 705 168 168 ALA CB C 18.891 0.003 1 stop_ save_ save_assigned_chemical_shifts_list_DsbB_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR' '3D NCACX' '3D NCOCX' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_Adam _Mol_system_component_name DsbB_2 _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 1 501 1 UQ1 C1 C 135.534 0.060 1 2 501 1 UQ1 C10 C 20.609 0.118 4 3 501 1 UQ1 C11 C 43.400 0.643 4 4 501 1 UQ1 C12 C 30.300 0.643 4 5 501 1 UQ1 C15 C 20.700 0.643 4 6 501 1 UQ1 C16 C 43.000 0.643 4 7 501 1 UQ1 C17 C 29.800 0.643 4 8 501 1 UQ1 C1M C 15.859 0.061 4 9 501 1 UQ1 C2 C 154.709 0.300 1 10 501 1 UQ1 C20 C 20.200 0.643 4 11 501 1 UQ1 C21 C 42.600 0.643 4 12 501 1 UQ1 C22 C 29.300 0.643 4 13 501 1 UQ1 C25 C 19.700 0.643 4 14 501 1 UQ1 C26 C 42.200 0.643 4 15 501 1 UQ1 C27 C 28.800 0.643 4 16 501 1 UQ1 C3 C 142.410 0.300 4 17 501 1 UQ1 C30 C 19.200 0.643 4 18 501 1 UQ1 C31 C 41.800 0.643 4 19 501 1 UQ1 C32 C 28.300 0.643 4 20 501 1 UQ1 C35 C 18.700 0.643 4 21 501 1 UQ1 C36 C 41.400 0.643 4 22 501 1 UQ1 C37 C 27.800 0.643 4 23 501 1 UQ1 C38 C 124.750 0.300 4 24 501 1 UQ1 C39 C 136.254 0.051 4 25 501 1 UQ1 C3M C 63.804 0.193 4 26 501 1 UQ1 C4 C 142.410 0.300 1 27 501 1 UQ1 C40 C 18.200 0.643 4 28 501 1 UQ1 C41 C 41.517 0.095 4 29 501 1 UQ1 C42 C 28.260 0.020 4 30 501 1 UQ1 C43 C 126.157 0.271 4 31 501 1 UQ1 C44 C 135.212 0.112 4 32 501 1 UQ1 C45 C 17.920 0.069 4 33 501 1 UQ1 C46 C 28.177 0.074 4 34 501 1 UQ1 C4M C 63.804 0.193 4 35 501 1 UQ1 C5 C 154.709 0.300 4 36 501 1 UQ1 C6 C 127.427 0.300 1 37 501 1 UQ1 C7 C 26.580 0.011 4 38 501 1 UQ1 C8 C 123.680 0.098 4 39 501 1 UQ1 C9 C 140.100 0.117 4 stop_ save_