data_17710 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Membrane protein complex DsbB-DsbA structure by joint calculations with solid-state NMR and X-ray experimental data ; _BMRB_accession_number 17710 _BMRB_flat_file_name bmr17710.str _Entry_type original _Submission_date 2011-06-15 _Accession_date 2011-06-15 _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 Berthold Deborah A. . 4 Schwieters Charles D. . 5 Nesbitt Anna E. . 6 Nieuwkoop Andrew J. . 7 Gennis Robert B. . 8 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "13C chemical shifts" 1228 "15N chemical shifts" 288 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-17 update BMRB 'update entry citation' 2011-10-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15546 'Chemical shift assignments for DsbB' 16327 'Chemical shift assignments for DsbA' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21938394 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tang Ming . . 2 Sperling Lindsay J. . 3 Berthold Deborah A. . 4 Schwieters Charles D. . 5 Nesbitt Anna E. . 6 Nieuwkoop Andrew J. . 7 Gennis Robert B. . 8 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 51 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 227 _Page_last 233 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DsbA and DsbB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbA $DsbA DsbB $DsbB 'ZINC ION' $ZN UBIQUINONE-1 $UQ8 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_DsbA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbA _Molecular_mass 20993.951 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 188 _Mol_residue_sequence ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHCYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 TYR 4 GLU 5 ASP 6 GLY 7 LYS 8 GLN 9 TYR 10 THR 11 THR 12 LEU 13 GLU 14 LYS 15 PRO 16 VAL 17 ALA 18 GLY 19 ALA 20 PRO 21 GLN 22 VAL 23 LEU 24 GLU 25 PHE 26 PHE 27 SER 28 PHE 29 PHE 30 CYS 31 PRO 32 HIS 33 CYS 34 TYR 35 GLN 36 PHE 37 GLU 38 GLU 39 VAL 40 LEU 41 HIS 42 ILE 43 SER 44 ASP 45 ASN 46 VAL 47 LYS 48 LYS 49 LYS 50 LEU 51 PRO 52 GLU 53 GLY 54 VAL 55 LYS 56 MET 57 THR 58 LYS 59 TYR 60 HIS 61 VAL 62 ASN 63 PHE 64 MET 65 GLY 66 GLY 67 ASP 68 LEU 69 GLY 70 LYS 71 ASP 72 LEU 73 THR 74 GLN 75 ALA 76 TRP 77 ALA 78 VAL 79 ALA 80 MET 81 ALA 82 LEU 83 GLY 84 VAL 85 GLU 86 ASP 87 LYS 88 VAL 89 THR 90 VAL 91 PRO 92 LEU 93 PHE 94 GLU 95 GLY 96 VAL 97 GLN 98 LYS 99 THR 100 GLN 101 THR 102 ILE 103 ARG 104 SER 105 ALA 106 SER 107 ASP 108 ILE 109 ARG 110 ASP 111 VAL 112 PHE 113 ILE 114 ASN 115 ALA 116 GLY 117 ILE 118 LYS 119 GLY 120 GLU 121 GLU 122 TYR 123 ASP 124 ALA 125 ALA 126 TRP 127 ASN 128 SER 129 PHE 130 VAL 131 VAL 132 LYS 133 SER 134 LEU 135 VAL 136 ALA 137 GLN 138 GLN 139 GLU 140 LYS 141 ALA 142 ALA 143 ALA 144 ASP 145 VAL 146 GLN 147 LEU 148 ARG 149 GLY 150 VAL 151 PRO 152 ALA 153 MET 154 PHE 155 VAL 156 ASN 157 GLY 158 LYS 159 TYR 160 GLN 161 LEU 162 ASN 163 PRO 164 GLN 165 GLY 166 MET 167 ASP 168 THR 169 SER 170 ASN 171 MET 172 ASP 173 VAL 174 PHE 175 VAL 176 GLN 177 GLN 178 TYR 179 ALA 180 ASP 181 THR 182 VAL 183 LYS 184 TYR 185 LEU 186 SER 187 GLU 188 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 100.00 189 100.00 100.00 9.89e-136 BMRB 18396 oxidized_DsbA 100.00 189 99.47 100.00 2.99e-135 BMRB 18543 DsbA(C33S) 100.00 189 99.47 99.47 9.01e-135 BMRB 18544 DsbA(C33S) 100.00 189 99.47 99.47 9.01e-135 PDB 1A23 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" 100.00 189 100.00 100.00 9.89e-136 PDB 1A24 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" 100.00 189 100.00 100.00 9.89e-136 PDB 1A2J "Oxidized Dsba Crystal Form Ii" 100.00 189 100.00 100.00 9.89e-136 PDB 1A2L "Reduced Dsba At 2.7 Angstroms Resolution" 100.00 189 100.00 100.00 9.89e-136 PDB 1A2M "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" 100.00 189 100.00 100.00 9.89e-136 PDB 1AC1 "Dsba Mutant H32l" 100.00 189 99.47 99.47 2.90e-134 PDB 1ACV "Dsba Mutant H32s" 100.00 189 99.47 99.47 1.12e-134 PDB 1BQ7 "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" 100.00 189 99.47 99.47 9.42e-135 PDB 1DSB "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" 100.00 189 100.00 100.00 9.89e-136 PDB 1FVJ "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" 100.00 189 99.47 100.00 7.90e-135 PDB 1FVK "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" 100.00 189 100.00 100.00 9.89e-136 PDB 1TI1 "Crystal Structure Of A Mutant Dsba" 100.00 189 99.47 99.47 1.12e-134 PDB 1U3A "Mutant Dsba" 100.00 189 99.47 99.47 1.12e-134 PDB 2B3S "Structure Of The Dsba Mutant (P31g-C33a)" 100.00 189 98.94 98.94 3.19e-133 PDB 2B6M "Structure Of The Dsba Mutant (P31a-C33a)" 100.00 189 98.94 98.94 1.19e-133 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 189 99.47 99.47 1.12e-134 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 99.47 1.12e-134 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 189 99.47 99.47 1.12e-134 PDB 3DKS "Dsba Substrate Complex" 100.00 189 99.47 100.00 3.22e-135 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 189 99.47 99.47 1.12e-134 PDB 4TKY "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" 100.00 191 99.47 99.47 7.52e-135 PDB 4WET "Crystal Structure Of E.coli Dsba In Complex With Compound 16" 100.00 189 100.00 100.00 9.89e-136 PDB 4WEY "Crystal Structure Of E.coli Dsba In Complex With Compound 17" 100.00 189 100.00 100.00 9.89e-136 PDB 4WF4 "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" 100.00 189 100.00 100.00 9.89e-136 PDB 4WF5 "Crystal Structure Of E.coli Dsba Soaked With Compound 4" 100.00 189 100.00 100.00 9.89e-136 DBJ BAB38206 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 100.00 100.00 4.51e-136 DBJ BAE77448 "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 208 100.00 100.00 4.51e-136 DBJ BAG79665 "protein disulfide isomerase I [Escherichia coli SE11]" 100.00 208 100.00 100.00 4.51e-136 DBJ BAI27892 "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" 100.00 208 100.00 100.00 4.51e-136 DBJ BAI33015 "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" 100.00 208 100.00 100.00 4.51e-136 EMBL CAA44868 "PpfA protein [Escherichia coli K-12]" 100.00 208 100.00 100.00 4.51e-136 EMBL CAA56736 "dsbA [Escherichia coli K-12]" 100.00 208 100.00 100.00 4.51e-136 EMBL CAA90910 "DsbA protein [Escherichia coli]" 100.00 208 99.47 100.00 1.48e-135 EMBL CAP78318 "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" 100.00 208 99.47 100.00 1.48e-135 EMBL CAQ34212 "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" 100.00 208 100.00 100.00 4.51e-136 GB AAA23715 "putative [Escherichia coli]" 100.00 208 100.00 100.00 4.51e-136 GB AAB02995 "dsbA [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 100.00 100.00 4.51e-136 GB AAC43519 "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" 100.00 208 99.47 99.47 1.98e-134 GB AAC43520 "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" 100.00 208 98.94 98.94 6.89e-134 GB AAC43521 "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" 100.00 208 98.94 98.94 2.03e-133 REF NP_312810 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 100.00 100.00 4.51e-136 REF NP_418297 "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 100.00 100.00 4.51e-136 REF NP_709659 "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" 100.00 208 99.47 100.00 2.20e-135 REF WP_000725331 "thiol-disulfide isomerase [Shigella boydii]" 100.00 208 98.94 99.47 8.82e-135 REF WP_000725332 "thiol:disulfide interchange protein DsbA [Escherichia coli]" 100.00 208 99.47 100.00 5.31e-136 SP P0A4L5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 1.48e-135 SP P0A4L6 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 1.48e-135 SP P0AEG4 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 100.00 100.00 4.51e-136 SP P0AEG5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 100.00 100.00 4.51e-136 SP P52235 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 2.20e-135 stop_ save_ save_DsbB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbB _Molecular_mass 15287.664 _Mol_thiol_state . _Details . _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 2015-01-30 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 100.00 186 100.00 100.00 1.10e-122 BMRB 15966 Disulfide_bond_formation_protein_B 100.00 183 97.73 97.73 1.09e-118 BMRB 18395 DsbB 100.00 176 99.43 99.43 1.19e-121 BMRB 18493 DsbB 100.00 176 100.00 100.00 1.54e-122 BMRB 18544 DsbB 100.00 176 99.43 99.43 1.19e-121 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 176 98.86 98.86 2.48e-120 PDB 2K73 "Solution Nmr Structure Of Integral Membrane Protein Dsbb" 100.00 183 97.73 97.73 1.09e-118 PDB 2K74 "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" 100.00 183 97.73 97.73 1.09e-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 2.48e-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 1.54e-122 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 176 98.86 98.86 2.48e-120 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 176 100.00 100.00 1.54e-122 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 182 99.43 99.43 1.02e-121 DBJ BAA36032 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. W3110]" 100.00 176 98.30 98.30 3.01e-120 DBJ BAB35103 "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.30 98.30 3.01e-120 DBJ BAG76757 "disulfide bond formation protein [Escherichia coli SE11]" 100.00 176 97.16 97.73 7.75e-119 DBJ BAI24997 "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" 100.00 176 97.73 98.30 6.20e-120 DBJ BAI30121 "oxidoreductase DsbB [Escherichia coli O103:H2 str. 12009]" 100.00 176 98.30 98.30 3.01e-120 EMBL CAP75720 "Disulfide bond formation protein B [Escherichia coli LF82]" 100.00 176 97.16 97.73 4.39e-119 EMBL CAQ31687 "DsbB[reduced] [Escherichia coli BL21(DE3)]" 100.00 176 98.30 98.30 3.01e-120 EMBL CAQ98064 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" 100.00 176 98.30 98.30 3.01e-120 EMBL CAR02574 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" 100.00 176 97.16 97.73 4.39e-119 EMBL CAR12682 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli UMN026]" 100.00 176 98.30 98.30 3.01e-120 GB AAA23711 "oxido-reductase [Escherichia coli]" 100.00 178 98.30 98.30 2.06e-120 GB AAB25233 "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" 100.00 176 98.30 98.30 3.01e-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 3.01e-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 1.83e-119 GB AAN42789 "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" 100.00 176 97.73 98.30 6.20e-120 PIR H85696 "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 176 97.73 97.73 1.83e-119 REF NP_287424 "disulfide bond formation protein B [Escherichia coli O157:H7 str. EDL933]" 100.00 176 97.73 97.73 1.83e-119 REF NP_309707 "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.30 98.30 3.01e-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 3.01e-120 REF NP_707082 "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" 100.00 176 97.73 98.30 6.20e-120 REF NP_753538 "disulfide bond formation protein B [Escherichia coli CFT073]" 100.00 176 97.16 97.73 4.39e-119 SP A1AAA8 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli APEC O1]" 100.00 176 97.16 97.73 4.39e-119 SP P0A6M2 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli K-12]" 100.00 176 98.30 98.30 3.01e-120 SP P0A6M3 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli O157:H7]" 100.00 176 98.30 98.30 3.01e-120 SP P59343 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli CFT073]" 100.00 176 97.16 97.73 4.39e-119 SP Q0T5L6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Shigella flexneri 5 str. 8401]" 100.00 176 97.73 98.30 6.20e-120 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 13:11:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_UQ8 _Saveframe_category ligand _Mol_type non-polymer _Name_common "UQ8 (Ubiquinone-8)" _BMRB_code . _PDB_code UQ8 _Molecular_mass 727.109 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Aug 18 16:09:53 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C45 C45 C . 0 . ? C44 C44 C . 0 . ? C46 C46 C . 0 . ? C43 C43 C . 0 . ? C42 C42 C . 0 . ? C41 C41 C . 0 . ? C39 C39 C . 0 . ? C40 C40 C . 0 . ? C38 C38 C . 0 . ? C37 C37 C . 0 . ? C36 C36 C . 0 . ? C34 C34 C . 0 . ? C35 C35 C . 0 . ? C33 C33 C . 0 . ? C32 C32 C . 0 . ? C31 C31 C . 0 . ? C29 C29 C . 0 . ? C30 C30 C . 0 . ? C28 C28 C . 0 . ? C27 C27 C . 0 . ? C26 C26 C . 0 . ? C24 C24 C . 0 . ? C25 C25 C . 0 . ? C23 C23 C . 0 . ? C22 C22 C . 0 . ? C21 C21 C . 0 . ? C19 C19 C . 0 . ? C20 C20 C . 0 . ? C18 C18 C . 0 . ? C17 C17 C . 0 . ? C16 C16 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C13 C13 C . 0 . ? C12 C12 C . 0 . ? C11 C11 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C8 C8 C . 0 . ? C7 C7 C . 0 . ? C6 C6 C . 0 . ? C1 C1 C . 0 . ? C1M C1M C . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? C3 C3 C . 0 . ? O3 O3 O . 0 . ? C3M C3M C . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4M C4M C . 0 . ? C5 C5 C . 0 . ? O5 O5 O . 0 . ? H45 H45 H . 0 . ? H45A H45A H . 0 . ? H45B H45B H . 0 . ? H46 H46 H . 0 . ? H46A H46A H . 0 . ? H46B H46B H . 0 . ? H43 H43 H . 0 . ? H42 H42 H . 0 . ? H42A H42A H . 0 . ? H41 H41 H . 0 . ? H41A H41A H . 0 . ? H40 H40 H . 0 . ? H40A H40A H . 0 . ? H40B H40B H . 0 . ? H38 H38 H . 0 . ? H37 H37 H . 0 . ? H37A H37A H . 0 . ? H36 H36 H . 0 . ? H36A H36A H . 0 . ? H35 H35 H . 0 . ? H35A H35A H . 0 . ? H35B H35B H . 0 . ? H33 H33 H . 0 . ? H32 H32 H . 0 . ? H32A H32A H . 0 . ? H31 H31 H . 0 . ? H31A H31A H . 0 . ? H30 H30 H . 0 . ? H30A H30A H . 0 . ? H30B H30B H . 0 . ? H28 H28 H . 0 . ? H27 H27 H . 0 . ? H27A H27A H . 0 . ? H26 H26 H . 0 . ? H26A H26A H . 0 . ? H25 H25 H . 0 . ? H25A H25A H . 0 . ? H25B H25B H . 0 . ? H23 H23 H . 0 . ? H22 H22 H . 0 . ? H22A H22A H . 0 . ? H21 H21 H . 0 . ? H21A H21A H . 0 . ? H20 H20 H . 0 . ? H20A H20A H . 0 . ? H20B H20B H . 0 . ? H18 H18 H . 0 . ? H17 H17 H . 0 . ? H17A H17A H . 0 . ? H16 H16 H . 0 . ? H16A H16A H . 0 . ? H15 H15 H . 0 . ? H15A H15A H . 0 . ? H15B H15B H . 0 . ? H13 H13 H . 0 . ? H12 H12 H . 0 . ? H12A H12A H . 0 . ? H11 H11 H . 0 . ? H11A H11A H . 0 . ? H10 H10 H . 0 . ? H10A H10A H . 0 . ? H10B H10B H . 0 . ? H8 H8 H . 0 . ? H7 H7 H . 0 . ? H7A H7A H . 0 . ? H1M H1M H . 0 . ? H1MA H1MA H . 0 . ? H1MB H1MB H . 0 . ? H3M H3M H . 0 . ? H3MA H3MA H . 0 . ? H3MB H3MB H . 0 . ? H4M H4M H . 0 . ? H4MA H4MA H . 0 . ? H4MB H4MB 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 SING C45 C44 ? ? SING C45 H45 ? ? SING C45 H45A ? ? SING C45 H45B ? ? DOUB C43 C44 ? ? SING C44 C46 ? ? SING C46 H46 ? ? SING C46 H46A ? ? SING C46 H46B ? ? SING C42 C43 ? ? SING C43 H43 ? ? SING C41 C42 ? ? SING C42 H42 ? ? SING C42 H42A ? ? SING C39 C41 ? ? SING C41 H41 ? ? SING C41 H41A ? ? SING C40 C39 ? ? DOUB C38 C39 ? ? SING C40 H40 ? ? SING C40 H40A ? ? SING C40 H40B ? ? SING C37 C38 ? ? SING C38 H38 ? ? SING C37 C36 ? ? SING C37 H37 ? ? SING C37 H37A ? ? SING C34 C36 ? ? SING C36 H36 ? ? SING C36 H36A ? ? DOUB C33 C34 ? ? SING C34 C35 ? ? SING C35 H35 ? ? SING C35 H35A ? ? SING C32 C33 ? ? SING C33 H33 ? ? SING C35 H35B ? ? SING C31 C32 ? ? SING C32 H32 ? ? SING C32 H32A ? ? SING C29 C31 ? ? SING C31 H31 ? ? SING C31 H31A ? ? DOUB C28 C29 ? ? SING C30 C29 ? ? SING C30 H30 ? ? SING C30 H30A ? ? SING C30 H30B ? ? SING C27 C28 ? ? SING C28 H28 ? ? SING C26 C27 ? ? SING C27 H27 ? ? SING C27 H27A ? ? SING C24 C26 ? ? SING C26 H26 ? ? SING C26 H26A ? ? DOUB C23 C24 ? ? SING C24 C25 ? ? SING C25 H25 ? ? SING C25 H25A ? ? SING C25 H25B ? ? SING C22 C23 ? ? SING C23 H23 ? ? SING C21 C22 ? ? SING C22 H22 ? ? SING C22 H22A ? ? SING C19 C21 ? ? SING C21 H21 ? ? SING C21 H21A ? ? SING C20 C19 ? ? DOUB C18 C19 ? ? SING C20 H20 ? ? SING C20 H20A ? ? SING C20 H20B ? ? SING C17 C18 ? ? SING C18 H18 ? ? SING C16 C17 ? ? SING C17 H17 ? ? SING C17 H17A ? ? SING C14 C16 ? ? SING C16 H16 ? ? SING C16 H16A ? ? DOUB C13 C14 ? ? SING C15 C14 ? ? SING C15 H15 ? ? SING C15 H15A ? ? SING C15 H15B ? ? SING C12 C13 ? ? SING C13 H13 ? ? SING C11 C12 ? ? SING C12 H12 ? ? SING C12 H12A ? ? SING C9 C11 ? ? SING C11 H11 ? ? SING C11 H11A ? ? DOUB C8 C9 ? ? SING C10 C9 ? ? SING C10 H10 ? ? SING C10 H10A ? ? SING C10 H10B ? ? SING C7 C8 ? ? SING C8 H8 ? ? SING C6 C7 ? ? SING C7 H7 ? ? SING C7 H7A ? ? DOUB C1 C6 ? ? SING C5 C6 ? ? SING C2 C1 ? ? SING C1 C1M ? ? SING C1M H1M ? ? SING C1M H1MA ? ? SING C1M H1MB ? ? DOUB O2 C2 ? ? SING C3 C2 ? ? SING O3 C3 ? ? DOUB C3 C4 ? ? SING C3M O3 ? ? SING C3M H3M ? ? SING C3M H3MA ? ? SING C3M H3MB ? ? SING O4 C4 ? ? SING C4 C5 ? ? SING C4M O4 ? ? SING C4M H4M ? ? SING C4M H4MA ? ? SING C4M H4MB ? ? DOUB C5 O5 ? ? 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 $DsbA 'E. coli' 562 Bacteria . Escherichia coli $DsbB 'E. coli' 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 'recombinant technology' . Escherichia coli . pQE70 $DsbB 'recombinant technology' . Escherichia coli . pQE70 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 15 mg '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 10 mg '[2-13C-glycerol; U-15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 10 mg '[1,3-13C-glycerol; U-15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_4 _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' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_5 _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' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_6 _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' H2O 90 % 'natural abundance' D2O 10 % '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_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_spectrometer_2 _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_2D_CC_DARR_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_4 save_ save_2D_CC_DARR_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_5 save_ save_2D_CC_DARR_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC DARR' _Sample_label $sample_6 save_ save_3D_NCACX_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCACX_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_2 save_ save_3D_NCACX_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_4 save_ save_3D_NCOCX_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_3D_NCOCX_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_3 save_ save_3D_NCOCX_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_4 save_ save_3D_CAN(CO)CX_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CAN(CO)CX' _Sample_label $sample_1 save_ save_3D_CAN(CO)CX_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CAN(CO)CX' _Sample_label $sample_4 save_ save_3D_CON(CA)CX_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CON(CA)CX' _Sample_label $sample_4 save_ save_4D_CANCOCX_16 _Saveframe_category NMR_applied_experiment _Experiment_name '4D CANCOCX' _Sample_label $sample_1 save_ save_2D_NC_TEDOR_17 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NC TEDOR' _Sample_label $sample_3 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'DsbA samples' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . pH pressure 1 . atm temperature 270 . K stop_ save_ save_sample_conditions_2 _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_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR' '3D NCACX' '3D NCOCX' '3D CAN(CO)CX' '3D CON(CA)CX' '4D CANCOCX' '2D NC TEDOR' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_Adam _Mol_system_component_name DsbA _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 2 2 GLN C C 179.954 0.185 1 2 2 2 GLN CA C 59.812 0.122 1 3 2 2 GLN CB C 30.353 0.454 1 4 2 2 GLN CG C 31.470 0.255 1 5 2 2 GLN CD C 177.162 0.275 1 6 2 2 GLN N N 121.533 0.108 1 7 3 3 TYR C C 177.449 0.227 1 8 3 3 TYR CA C 58.391 0.214 1 9 3 3 TYR CB C 40.712 0.134 1 10 3 3 TYR N N 121.931 0.178 1 11 4 4 GLU C C 174.487 0.178 1 12 4 4 GLU CA C 55.358 0.353 1 13 4 4 GLU CB C 33.976 0.246 1 14 4 4 GLU CG C 36.942 0.300 1 15 4 4 GLU N N 116.645 0.312 1 16 5 5 ASP C C 175.591 0.246 1 17 5 5 ASP CA C 55.165 0.214 1 18 5 5 ASP CB C 41.150 0.212 1 19 5 5 ASP CG C 179.672 0.300 1 20 5 5 ASP N N 125.902 0.309 1 21 6 6 GLY C C 173.425 0.202 1 22 6 6 GLY CA C 45.008 0.160 1 23 6 6 GLY N N 116.973 0.172 1 24 7 7 LYS C C 175.588 0.070 1 25 7 7 LYS CA C 57.110 0.224 1 26 7 7 LYS CB C 32.253 0.210 1 27 7 7 LYS CG C 25.391 0.300 1 28 7 7 LYS N N 122.354 0.515 1 29 8 8 GLN C C 174.189 0.125 1 30 8 8 GLN CA C 59.511 0.149 1 31 8 8 GLN CB C 27.197 0.079 1 32 8 8 GLN CG C 34.205 0.082 1 33 8 8 GLN CD C 179.655 0.300 1 34 8 8 GLN N N 115.549 0.287 1 35 9 9 TYR C C 172.240 0.144 1 36 9 9 TYR CA C 55.156 0.172 1 37 9 9 TYR CB C 41.288 0.056 1 38 9 9 TYR CG C 128.358 0.048 1 39 9 9 TYR CD1 C 132.719 0.300 3 40 9 9 TYR CD2 C 132.397 0.300 3 41 9 9 TYR CE1 C 117.180 0.256 3 42 9 9 TYR CZ C 157.998 0.300 1 43 9 9 TYR N N 111.793 0.165 1 44 10 10 THR C C 174.550 0.167 1 45 10 10 THR CA C 60.350 0.134 1 46 10 10 THR CB C 71.600 0.060 1 47 10 10 THR CG2 C 22.208 0.063 1 48 10 10 THR N N 111.789 0.164 1 49 11 11 THR C C 175.409 0.122 1 50 11 11 THR CA C 62.856 0.160 1 51 11 11 THR CB C 69.720 0.122 1 52 11 11 THR CG2 C 21.703 0.120 1 53 11 11 THR N N 121.004 0.198 1 54 12 12 LEU C C 177.517 0.122 1 55 12 12 LEU CA C 55.898 0.164 1 56 12 12 LEU CB C 41.632 0.124 1 57 12 12 LEU CG C 28.705 0.139 1 58 12 12 LEU CD1 C 24.701 0.151 2 59 12 12 LEU CD2 C 23.566 0.028 2 60 12 12 LEU N N 129.283 0.161 1 61 13 13 GLU C C 176.812 0.133 1 62 13 13 GLU CA C 58.583 0.168 1 63 13 13 GLU CB C 29.911 0.093 1 64 13 13 GLU CG C 32.483 0.300 1 65 13 13 GLU N N 123.334 0.188 1 66 14 14 LYS C C 172.534 0.179 1 67 14 14 LYS CA C 52.353 0.139 1 68 14 14 LYS CB C 32.877 0.115 1 69 14 14 LYS CG C 24.524 0.069 1 70 14 14 LYS N N 117.806 0.150 1 71 15 15 PRO C C 176.485 0.126 1 72 15 15 PRO CA C 62.555 0.152 1 73 15 15 PRO CB C 32.719 0.081 1 74 15 15 PRO CG C 27.333 0.097 1 75 15 15 PRO CD C 50.855 0.162 1 76 15 15 PRO N N 135.702 0.177 1 77 16 16 VAL C C 176.119 0.099 1 78 16 16 VAL CA C 61.508 0.114 1 79 16 16 VAL CB C 32.798 0.096 1 80 16 16 VAL CG1 C 21.629 0.105 2 81 16 16 VAL CG2 C 21.592 0.066 2 82 16 16 VAL N N 123.418 0.158 1 83 17 17 ALA C C 179.038 0.095 1 84 17 17 ALA CA C 52.560 0.176 1 85 17 17 ALA CB C 18.906 0.068 1 86 17 17 ALA N N 132.349 0.189 1 87 18 18 GLY C C 174.010 0.210 1 88 18 18 GLY CA C 45.806 0.149 1 89 18 18 GLY N N 110.894 0.240 1 90 19 19 ALA C C 175.218 0.139 1 91 19 19 ALA CA C 50.520 0.133 1 92 19 19 ALA CB C 17.333 0.130 1 93 19 19 ALA N N 122.290 0.157 1 94 20 20 PRO C C 175.826 0.225 1 95 20 20 PRO CA C 62.516 0.176 1 96 20 20 PRO CB C 31.699 0.212 1 97 20 20 PRO CG C 27.822 0.066 1 98 20 20 PRO CD C 50.232 0.180 1 99 20 20 PRO N N 134.274 0.208 1 100 21 21 GLN C C 176.816 0.177 1 101 21 21 GLN CA C 60.100 0.166 1 102 21 21 GLN CB C 29.803 0.083 1 103 21 21 GLN CG C 32.109 0.300 1 104 21 21 GLN N N 121.726 0.251 1 105 22 22 VAL C C 172.994 0.171 1 106 22 22 VAL CA C 62.758 0.197 1 107 22 22 VAL CB C 33.940 0.124 1 108 22 22 VAL CG1 C 22.868 0.087 2 109 22 22 VAL CG2 C 21.388 0.152 2 110 22 22 VAL N N 115.989 0.221 1 111 23 23 LEU C C 173.441 0.162 1 112 23 23 LEU CA C 52.778 0.143 1 113 23 23 LEU CB C 46.118 0.132 1 114 23 23 LEU CG C 26.682 0.139 1 115 23 23 LEU CD1 C 22.680 0.300 2 116 23 23 LEU CD2 C 22.680 0.300 2 117 23 23 LEU N N 128.930 0.194 1 118 24 24 GLU C C 178.009 0.119 1 119 24 24 GLU CA C 57.623 0.152 1 120 24 24 GLU CB C 40.077 0.290 1 121 24 24 GLU CD C 179.469 0.300 1 122 24 24 GLU N N 128.008 0.202 1 123 25 25 PHE C C 178.752 0.300 1 124 25 25 PHE CA C 56.398 0.210 1 125 25 25 PHE CG C 139.839 0.026 1 126 25 25 PHE N N 121.043 0.471 1 127 26 26 PHE C C 170.769 0.187 1 128 26 26 PHE CA C 54.966 0.091 1 129 26 26 PHE CB C 43.263 0.393 1 130 26 26 PHE CG C 136.412 0.054 1 131 26 26 PHE CZ C 129.304 0.300 1 132 26 26 PHE N N 119.901 0.095 1 133 27 27 SER C C 177.377 0.105 1 134 27 27 SER CA C 54.797 0.122 1 135 27 27 SER CB C 64.576 0.116 1 136 27 27 SER N N 108.927 0.160 1 137 28 28 PHE C C 176.480 0.181 1 138 28 28 PHE CA C 63.007 0.230 1 139 28 28 PHE CB C 38.512 0.081 1 140 28 28 PHE CG C 139.331 0.049 1 141 28 28 PHE CD1 C 132.220 0.300 3 142 28 28 PHE CD2 C 132.220 0.300 3 143 28 28 PHE N N 131.706 0.150 1 144 29 29 PHE C C 175.700 0.161 1 145 29 29 PHE CA C 59.499 0.194 1 146 29 29 PHE CB C 44.162 0.293 1 147 29 29 PHE CG C 139.902 0.076 1 148 29 29 PHE CD1 C 131.150 0.300 3 149 29 29 PHE CD2 C 131.150 0.300 3 150 29 29 PHE N N 116.018 0.220 1 151 30 30 CYS C C 174.183 0.300 1 152 30 30 CYS CA C 52.828 0.250 1 153 30 30 CYS CB C 31.492 0.063 1 154 30 30 CYS N N 120.190 0.348 1 155 31 31 PRO C C 181.012 0.137 1 156 31 31 PRO CA C 65.944 0.177 1 157 31 31 PRO CB C 31.751 0.073 1 158 31 31 PRO CG C 27.958 0.110 1 159 31 31 PRO CD C 49.075 0.118 1 160 31 31 PRO N N 133.968 0.205 1 161 32 32 HIS C C 177.770 0.082 1 162 32 32 HIS CA C 58.408 0.365 1 163 32 32 HIS CB C 29.624 0.179 1 164 32 32 HIS N N 120.160 0.196 1 165 34 34 TYR C C 176.474 0.154 1 166 34 34 TYR CA C 63.002 0.238 1 167 34 34 TYR CB C 37.976 0.160 1 168 34 34 TYR N N 122.161 0.218 1 169 35 35 GLN C C 176.702 0.305 1 170 35 35 GLN CA C 58.900 0.152 1 171 35 35 GLN CB C 31.424 0.124 1 172 35 35 GLN CD C 177.667 0.300 1 173 35 35 GLN N N 120.731 0.213 1 174 36 36 PHE C C 177.010 0.312 1 175 36 36 PHE CA C 60.013 0.111 1 176 36 36 PHE CB C 38.594 0.300 1 177 36 36 PHE N N 121.476 0.200 1 178 37 37 GLU C C 177.937 0.137 1 179 37 37 GLU CA C 58.356 0.197 1 180 37 37 GLU CB C 28.114 0.044 1 181 37 37 GLU CG C 34.714 0.300 1 182 37 37 GLU N N 116.418 0.287 1 183 38 38 GLU C C 178.840 0.300 1 184 38 38 GLU CA C 59.519 0.249 1 185 38 38 GLU CB C 30.795 0.300 1 186 38 38 GLU N N 119.304 0.151 1 187 39 39 VAL C C 176.790 0.147 1 188 39 39 VAL CA C 63.935 0.235 1 189 39 39 VAL CB C 32.650 0.055 1 190 39 39 VAL CG1 C 20.944 0.112 2 191 39 39 VAL N N 116.542 0.167 1 192 40 40 LEU C C 176.162 0.119 1 193 40 40 LEU CA C 55.238 0.108 1 194 40 40 LEU CB C 42.058 0.058 1 195 40 40 LEU CG C 27.192 0.110 1 196 40 40 LEU CD1 C 25.918 0.300 2 197 40 40 LEU CD2 C 25.918 0.300 2 198 40 40 LEU N N 114.948 0.243 1 199 41 41 HIS N N 120.229 0.070 1 200 42 42 ILE CA C 65.127 0.091 1 201 42 42 ILE CB C 35.681 0.073 1 202 42 42 ILE CG1 C 26.987 0.068 1 203 42 42 ILE CG2 C 17.001 0.300 1 204 42 42 ILE CD1 C 9.690 0.188 1 205 43 43 SER CA C 61.412 0.300 1 206 43 43 SER CB C 62.882 0.300 1 207 46 46 VAL C C 178.031 0.118 1 208 46 46 VAL CA C 66.878 0.036 1 209 46 46 VAL CB C 31.908 0.111 1 210 46 46 VAL CG1 C 24.293 0.192 2 211 46 46 VAL CG2 C 22.493 0.300 2 212 47 47 LYS C C 179.265 0.104 1 213 47 47 LYS CA C 60.218 0.139 1 214 47 47 LYS CB C 32.712 0.146 1 215 47 47 LYS CG C 25.339 0.191 1 216 47 47 LYS N N 119.820 0.286 1 217 48 48 LYS C C 177.560 0.133 1 218 48 48 LYS CA C 58.623 0.220 1 219 48 48 LYS CB C 32.982 0.046 1 220 48 48 LYS N N 115.101 0.185 1 221 49 49 LYS CA C 55.675 0.037 1 222 49 49 LYS N N 116.779 0.258 1 223 50 50 LEU C C 174.334 0.071 1 224 50 50 LEU CA C 52.756 0.148 1 225 50 50 LEU CB C 44.011 2.289 1 226 50 50 LEU CG C 25.808 0.034 1 227 50 50 LEU N N 120.559 0.118 1 228 51 51 PRO C C 174.257 0.300 1 229 51 51 PRO CA C 66.248 0.155 1 230 51 51 PRO CB C 32.675 0.077 1 231 51 51 PRO CG C 27.966 0.037 1 232 51 51 PRO CD C 52.437 0.156 1 233 51 51 PRO N N 153.632 0.300 1 234 52 52 GLU C C 180.146 0.021 1 235 52 52 GLU CA C 59.206 0.027 1 236 52 52 GLU CB C 28.181 0.300 1 237 53 53 GLY C C 174.137 0.253 1 238 53 53 GLY CA C 45.540 0.256 1 239 53 53 GLY N N 110.824 0.149 1 240 54 54 VAL C C 174.409 0.300 1 241 54 54 VAL CA C 62.540 0.133 1 242 54 54 VAL CB C 31.851 0.063 1 243 54 54 VAL CG1 C 22.273 0.300 2 244 54 54 VAL CG2 C 21.719 0.300 2 245 54 54 VAL N N 121.680 0.038 1 246 56 56 MET C C 175.415 0.110 1 247 56 56 MET CA C 54.752 0.115 1 248 57 57 THR C C 171.914 0.300 1 249 57 57 THR CA C 62.911 0.138 1 250 57 57 THR CB C 70.384 0.138 1 251 57 57 THR CG2 C 22.597 0.057 1 252 57 57 THR N N 122.242 0.457 1 253 58 58 LYS C C 173.887 0.300 1 254 58 58 LYS CA C 54.935 0.100 1 255 58 58 LYS CB C 34.321 0.188 1 256 58 58 LYS N N 131.457 0.300 1 257 59 59 TYR C C 173.165 0.187 1 258 59 59 TYR CA C 52.128 0.229 1 259 59 59 TYR CB C 40.966 0.015 1 260 59 59 TYR CG C 129.610 0.556 1 261 59 59 TYR CD1 C 131.738 0.300 3 262 59 59 TYR CD2 C 130.835 0.300 3 263 59 59 TYR N N 124.757 0.220 1 264 60 60 HIS C C 174.936 0.181 1 265 60 60 HIS CA C 56.165 0.156 1 266 60 60 HIS CB C 30.614 0.223 1 267 60 60 HIS CG C 128.168 0.144 1 268 60 60 HIS CE1 C 138.941 0.300 1 269 60 60 HIS N N 123.425 0.121 1 270 61 61 VAL C C 175.606 0.327 1 271 61 61 VAL CA C 57.874 0.197 1 272 61 61 VAL CB C 34.334 0.136 1 273 61 61 VAL N N 111.497 0.249 1 274 62 62 ASN CA C 55.376 0.191 1 275 62 62 ASN N N 122.885 0.125 1 276 63 63 PHE CA C 58.004 0.032 1 277 63 63 PHE CG C 138.209 0.081 1 278 63 63 PHE N N 111.082 0.300 1 279 64 64 MET CA C 56.112 0.300 1 280 64 64 MET CB C 32.203 0.300 1 281 65 65 GLY CA C 47.440 0.213 1 282 65 65 GLY N N 111.309 0.308 1 283 66 66 GLY C C 176.901 0.111 1 284 66 66 GLY CA C 45.656 0.142 1 285 66 66 GLY N N 109.222 0.300 1 286 67 67 ASP C C 177.906 0.248 1 287 67 67 ASP CA C 57.649 0.161 1 288 67 67 ASP CB C 39.856 0.051 1 289 67 67 ASP CG C 176.123 0.620 1 290 67 67 ASP N N 128.179 0.088 1 291 68 68 LEU C C 179.273 0.124 1 292 68 68 LEU CA C 56.979 0.172 1 293 68 68 LEU CB C 42.205 0.170 1 294 68 68 LEU CG C 27.289 0.058 1 295 68 68 LEU N N 120.418 0.076 1 296 69 69 GLY C C 176.403 0.198 1 297 69 69 GLY CA C 48.204 0.166 1 298 69 69 GLY N N 107.114 0.148 1 299 70 70 LYS CA C 59.798 0.097 1 300 70 70 LYS CB C 31.773 0.103 1 301 70 70 LYS N N 121.727 0.384 1 302 72 72 LEU C C 178.051 0.300 1 303 72 72 LEU CA C 57.826 0.225 1 304 72 72 LEU CB C 42.669 0.103 1 305 72 72 LEU CG C 28.314 0.010 1 306 73 73 THR C C 176.726 0.162 1 307 73 73 THR CA C 67.025 0.192 1 308 73 73 THR CB C 68.570 0.079 1 309 73 73 THR CG2 C 22.068 0.148 1 310 73 73 THR N N 119.737 0.162 1 311 74 74 GLN C C 177.539 0.139 1 312 74 74 GLN CA C 59.572 0.142 1 313 74 74 GLN CB C 25.973 0.064 1 314 74 74 GLN CG C 31.052 0.203 1 315 74 74 GLN N N 125.298 0.096 1 316 75 75 ALA C C 179.824 0.157 1 317 75 75 ALA CA C 54.919 0.130 1 318 75 75 ALA CB C 20.114 0.085 1 319 75 75 ALA N N 123.370 0.177 1 320 76 76 TRP C C 177.790 0.165 1 321 76 76 TRP CA C 59.100 0.090 1 322 76 76 TRP CB C 29.635 0.093 1 323 76 76 TRP CG C 111.253 0.032 1 324 76 76 TRP CD1 C 128.019 0.135 1 325 76 76 TRP CD2 C 129.400 0.024 1 326 76 76 TRP CE2 C 139.980 0.080 1 327 76 76 TRP CE3 C 121.715 0.031 1 328 76 76 TRP N N 120.584 0.131 1 329 76 76 TRP NE1 N 128.908 0.048 1 330 77 77 ALA C C 179.088 0.258 1 331 77 77 ALA CA C 55.307 0.132 1 332 77 77 ALA CB C 20.290 0.055 1 333 77 77 ALA N N 120.088 0.220 1 334 78 78 VAL C C 177.341 0.127 1 335 78 78 VAL CA C 67.244 0.184 1 336 78 78 VAL CB C 30.287 0.061 1 337 78 78 VAL CG1 C 23.695 0.082 2 338 78 78 VAL CG2 C 22.296 0.129 2 339 78 78 VAL N N 119.724 0.220 1 340 79 79 ALA C C 179.823 0.117 1 341 79 79 ALA CA C 55.053 0.132 1 342 79 79 ALA CB C 17.827 0.080 1 343 79 79 ALA N N 121.109 0.173 1 344 80 80 MET C C 179.398 0.185 1 345 80 80 MET CA C 58.573 0.128 1 346 80 80 MET CB C 34.524 0.055 1 347 80 80 MET CG C 30.934 0.226 1 348 80 80 MET N N 115.893 0.205 1 349 81 81 ALA C C 180.144 0.054 1 350 81 81 ALA CA C 54.782 0.122 1 351 81 81 ALA CB C 18.104 0.156 1 352 81 81 ALA N N 123.783 0.223 1 353 82 82 LEU C C 177.499 0.179 1 354 82 82 LEU CA C 54.606 0.132 1 355 82 82 LEU CB C 43.188 0.167 1 356 82 82 LEU CG C 26.988 0.144 1 357 82 82 LEU CD1 C 22.126 0.176 2 358 82 82 LEU CD2 C 22.126 0.176 2 359 82 82 LEU N N 113.482 0.174 1 360 83 83 GLY C C 176.857 0.140 1 361 83 83 GLY CA C 47.347 0.207 1 362 83 83 GLY N N 111.336 0.200 1 363 84 84 VAL C C 176.780 0.097 1 364 84 84 VAL CA C 59.385 0.122 1 365 84 84 VAL CB C 31.652 0.083 1 366 84 84 VAL CG1 C 20.493 0.098 2 367 84 84 VAL CG2 C 19.209 0.077 2 368 84 84 VAL N N 108.755 0.199 1 369 85 85 GLU C C 179.576 0.114 1 370 85 85 GLU CA C 61.889 0.155 1 371 85 85 GLU CB C 29.400 0.095 1 372 85 85 GLU CG C 36.513 0.097 1 373 85 85 GLU CD C 184.070 0.300 1 374 85 85 GLU N N 126.740 0.213 1 375 86 86 ASP C C 177.363 0.170 1 376 86 86 ASP CA C 56.051 0.202 1 377 86 86 ASP CB C 39.873 0.171 1 378 86 86 ASP CG C 179.655 0.427 1 379 86 86 ASP N N 116.367 0.127 1 380 87 87 LYS C C 178.046 0.072 1 381 87 87 LYS CA C 57.260 0.173 1 382 87 87 LYS CB C 34.287 0.116 1 383 87 87 LYS CG C 25.317 0.105 1 384 87 87 LYS CD C 29.492 0.099 1 385 87 87 LYS CE C 39.814 0.038 1 386 87 87 LYS N N 117.187 0.164 1 387 88 88 VAL C C 176.111 0.102 1 388 88 88 VAL CA C 60.889 0.176 1 389 88 88 VAL CB C 32.932 0.126 1 390 88 88 VAL CG1 C 19.521 0.137 2 391 88 88 VAL CG2 C 17.601 0.084 2 392 88 88 VAL N N 104.016 0.160 1 393 89 89 THR C C 175.239 0.150 1 394 89 89 THR CA C 69.353 0.227 1 395 89 89 THR CB C 69.631 0.233 1 396 89 89 THR CG2 C 21.333 0.140 1 397 89 89 THR N N 120.797 0.223 1 398 90 90 VAL C C 175.961 0.142 1 399 90 90 VAL CA C 69.346 0.203 1 400 90 90 VAL CB C 28.903 0.188 1 401 90 90 VAL CG1 C 24.518 0.171 2 402 90 90 VAL CG2 C 21.481 0.118 2 403 90 90 VAL N N 120.297 0.133 1 404 91 91 PRO C C 181.100 0.101 1 405 91 91 PRO CA C 65.894 0.200 1 406 91 91 PRO CB C 31.453 0.323 1 407 91 91 PRO CG C 27.692 0.079 1 408 91 91 PRO CD C 49.040 0.141 1 409 91 91 PRO N N 133.847 0.259 1 410 92 92 LEU C C 177.877 0.175 1 411 92 92 LEU CA C 58.045 0.105 1 412 92 92 LEU CB C 40.101 0.080 1 413 92 92 LEU CG C 27.011 0.025 1 414 92 92 LEU CD1 C 22.928 0.073 2 415 92 92 LEU CD2 C 22.928 0.073 2 416 92 92 LEU N N 120.194 0.164 1 417 93 93 PHE C C 180.090 0.200 1 418 93 93 PHE CA C 63.972 0.143 1 419 93 93 PHE CB C 39.433 0.168 1 420 93 93 PHE CG C 141.580 0.014 1 421 93 93 PHE CD1 C 132.129 0.300 3 422 93 93 PHE CD2 C 132.129 0.300 3 423 93 93 PHE N N 120.116 0.206 1 424 94 94 GLU C C 180.455 0.142 1 425 94 94 GLU CA C 59.410 0.316 1 426 94 94 GLU CB C 29.639 0.050 1 427 94 94 GLU CG C 39.997 0.300 1 428 94 94 GLU N N 116.168 0.114 1 429 95 95 GLY C C 175.846 0.167 1 430 95 95 GLY CA C 46.629 0.180 1 431 95 95 GLY N N 108.267 0.138 1 432 96 96 VAL C C 178.192 0.054 1 433 96 96 VAL CA C 66.420 0.231 1 434 96 96 VAL CB C 32.164 0.090 1 435 96 96 VAL CG1 C 23.610 0.074 2 436 96 96 VAL CG2 C 22.006 0.442 2 437 96 96 VAL N N 119.762 0.259 1 438 98 98 LYS C C 177.255 0.064 1 439 98 98 LYS CA C 58.086 0.998 1 440 98 98 LYS CB C 34.331 0.120 1 441 99 99 THR C C 175.602 0.073 1 442 99 99 THR CA C 62.247 0.138 1 443 99 99 THR CB C 68.667 0.161 1 444 99 99 THR CG2 C 22.232 0.106 1 445 99 99 THR N N 107.448 0.219 1 446 100 100 GLN C C 175.374 0.171 1 447 100 100 GLN CA C 57.323 0.204 1 448 100 100 GLN CB C 25.642 0.161 1 449 100 100 GLN CG C 34.435 0.094 1 450 100 100 GLN N N 114.691 0.216 1 451 101 101 THR C C 175.310 0.143 1 452 101 101 THR CA C 60.852 0.154 1 453 101 101 THR CB C 68.768 0.145 1 454 101 101 THR CG2 C 22.836 0.066 1 455 101 101 THR N N 106.084 0.296 1 456 102 102 ILE C C 173.949 0.203 1 457 102 102 ILE CA C 60.813 0.157 1 458 102 102 ILE CB C 37.018 0.129 1 459 102 102 ILE CG1 C 27.175 0.052 1 460 102 102 ILE CG2 C 17.454 0.067 1 461 102 102 ILE CD1 C 14.852 0.114 1 462 102 102 ILE N N 121.045 0.139 1 463 103 103 ARG C C 175.167 0.300 1 464 103 103 ARG CA C 55.228 0.190 1 465 103 103 ARG N N 126.046 0.197 1 466 104 104 SER C C 174.656 0.222 1 467 104 104 SER CA C 56.783 0.212 1 468 104 104 SER CB C 67.263 0.111 1 469 104 104 SER N N 115.048 0.246 1 470 105 105 ALA C C 180.866 0.113 1 471 105 105 ALA CA C 55.287 0.122 1 472 105 105 ALA CB C 16.974 0.076 1 473 105 105 ALA N N 123.719 0.152 1 474 106 106 SER C C 176.320 0.102 1 475 106 106 SER CA C 61.508 0.156 1 476 106 106 SER CB C 62.253 0.138 1 477 106 106 SER N N 116.173 0.167 1 478 107 107 ASP C C 179.072 0.240 1 479 107 107 ASP CA C 57.042 0.155 1 480 107 107 ASP CB C 42.412 0.220 1 481 107 107 ASP CG C 179.861 0.300 1 482 107 107 ASP N N 120.364 0.158 1 483 108 108 ILE C C 176.954 0.209 1 484 108 108 ILE CA C 65.734 0.168 1 485 108 108 ILE CB C 38.269 0.076 1 486 108 108 ILE CG1 C 28.966 0.109 1 487 108 108 ILE CG2 C 18.453 0.052 1 488 108 108 ILE CD1 C 15.314 0.063 1 489 108 108 ILE N N 120.118 0.139 1 490 109 109 ARG C C 177.635 0.148 1 491 109 109 ARG CA C 59.172 0.295 1 492 109 109 ARG CB C 29.905 0.187 1 493 109 109 ARG CD C 43.184 0.108 1 494 109 109 ARG CZ C 159.732 0.027 1 495 109 109 ARG N N 121.031 0.199 1 496 110 110 ASP C C 179.316 0.319 1 497 110 110 ASP CA C 57.553 0.230 1 498 110 110 ASP CB C 40.215 0.155 1 499 110 110 ASP CG C 180.004 0.300 1 500 110 110 ASP N N 116.511 0.146 1 501 111 111 VAL C C 179.304 0.141 1 502 111 111 VAL CA C 66.437 0.148 1 503 111 111 VAL CB C 30.872 0.108 1 504 111 111 VAL CG1 C 23.550 0.070 2 505 111 111 VAL CG2 C 21.674 0.045 2 506 111 111 VAL N N 120.286 0.147 1 507 112 112 PHE C C 177.816 0.119 1 508 112 112 PHE CA C 62.047 0.176 1 509 112 112 PHE CB C 38.096 0.176 1 510 112 112 PHE CG C 142.354 0.023 1 511 112 112 PHE N N 120.494 0.135 1 512 113 113 ILE C C 182.291 0.110 1 513 113 113 ILE CA C 63.628 0.129 1 514 113 113 ILE CB C 37.944 0.066 1 515 113 113 ILE CG1 C 28.311 0.059 1 516 113 113 ILE CG2 C 17.151 0.069 1 517 113 113 ILE CD1 C 13.738 0.162 1 518 113 113 ILE N N 122.026 0.156 1 519 114 114 ASN C C 176.327 0.155 1 520 114 114 ASN CA C 55.589 0.156 1 521 114 114 ASN CB C 38.170 0.171 1 522 114 114 ASN CG C 176.766 0.300 1 523 114 114 ASN N N 120.388 0.121 1 524 115 115 ALA C C 177.056 0.124 1 525 115 115 ALA CA C 51.907 0.162 1 526 115 115 ALA CB C 18.944 0.082 1 527 115 115 ALA N N 120.917 0.181 1 528 116 116 GLY C C 173.878 0.148 1 529 116 116 GLY CA C 45.227 0.171 1 530 116 116 GLY N N 105.688 0.220 1 531 117 117 ILE C C 175.266 0.191 1 532 117 117 ILE CA C 61.019 0.170 1 533 117 117 ILE CB C 37.669 0.120 1 534 117 117 ILE CG1 C 25.837 0.300 1 535 117 117 ILE CG2 C 20.635 0.088 1 536 117 117 ILE CD1 C 14.735 0.027 1 537 117 117 ILE N N 125.335 0.192 1 538 118 118 LYS C C 179.230 0.141 1 539 118 118 LYS CA C 56.847 0.168 1 540 118 118 LYS CB C 32.664 0.084 1 541 118 118 LYS CG C 25.595 0.154 1 542 118 118 LYS N N 125.826 0.252 1 543 119 119 GLY C C 175.063 0.143 1 544 119 119 GLY CA C 48.279 0.177 1 545 119 119 GLY N N 113.575 0.305 1 546 120 120 GLU C C 180.058 0.094 1 547 120 120 GLU CA C 59.454 0.168 1 548 120 120 GLU CB C 28.843 0.210 1 549 120 120 GLU N N 117.238 0.244 1 550 121 121 GLU C C 179.378 0.220 1 551 121 121 GLU CA C 58.303 0.027 1 552 121 121 GLU CB C 29.684 0.103 1 553 121 121 GLU N N 120.950 0.064 1 554 122 122 TYR C C 176.639 0.048 1 555 122 122 TYR CA C 62.953 0.225 1 556 122 122 TYR CB C 38.077 0.141 1 557 122 122 TYR CG C 127.070 0.023 1 558 122 122 TYR CE1 C 117.635 0.015 3 559 122 122 TYR CE2 C 115.791 0.300 1 560 122 122 TYR N N 122.507 0.395 1 561 123 123 ASP C C 178.519 0.146 1 562 123 123 ASP CA C 57.326 0.121 1 563 123 123 ASP CB C 39.961 0.290 1 564 123 123 ASP CG C 180.063 0.300 1 565 123 123 ASP N N 120.529 0.252 1 566 124 124 ALA C C 181.307 0.300 1 567 124 124 ALA CA C 54.716 0.185 1 568 124 124 ALA CB C 18.161 0.144 1 569 124 124 ALA N N 121.016 0.062 1 570 125 125 ALA C C 181.022 0.191 1 571 125 125 ALA CA C 55.114 0.225 1 572 125 125 ALA CB C 18.488 0.082 1 573 125 125 ALA N N 119.624 0.032 1 574 126 126 TRP C C 176.032 0.123 1 575 126 126 TRP CA C 61.501 0.132 1 576 126 126 TRP CB C 28.759 0.382 1 577 126 126 TRP CG C 109.519 0.073 1 578 126 126 TRP CD1 C 127.717 0.147 1 579 126 126 TRP CD2 C 128.640 0.072 1 580 126 126 TRP CE2 C 138.780 0.160 1 581 126 126 TRP CE3 C 122.711 0.048 1 582 126 126 TRP N N 121.864 0.225 1 583 126 126 TRP NE1 N 131.005 0.049 1 584 127 127 ASN C C 174.765 0.195 1 585 127 127 ASN CA C 53.439 0.156 1 586 127 127 ASN CB C 40.322 0.077 1 587 127 127 ASN CG C 177.447 0.093 1 588 127 127 ASN N N 110.735 0.167 1 589 128 128 SER C C 180.211 0.300 1 590 128 128 SER CA C 59.245 0.210 1 591 128 128 SER CB C 65.657 0.127 1 592 128 128 SER N N 116.473 0.289 1 593 129 129 PHE C C 178.812 0.247 1 594 129 129 PHE CA C 61.696 0.060 1 595 129 129 PHE CB C 38.085 0.077 1 596 129 129 PHE CG C 137.401 0.021 1 597 129 129 PHE N N 123.909 0.300 1 598 130 130 VAL C C 176.103 0.300 1 599 130 130 VAL CA C 67.485 0.023 1 600 130 130 VAL CB C 30.323 0.300 1 601 130 130 VAL N N 120.105 0.105 1 602 131 131 VAL C C 177.627 0.154 1 603 131 131 VAL CA C 67.222 0.224 1 604 131 131 VAL CB C 31.544 0.056 1 605 131 131 VAL N N 120.839 0.258 1 606 132 132 LYS C C 180.306 0.073 1 607 132 132 LYS CA C 59.908 0.210 1 608 132 132 LYS CB C 31.975 0.033 1 609 132 132 LYS N N 120.348 0.059 1 610 133 133 SER C C 176.530 0.344 1 611 133 133 SER CA C 61.239 0.160 1 612 133 133 SER CB C 62.124 0.093 1 613 133 133 SER N N 115.295 0.355 1 614 134 134 LEU C C 181.408 0.131 1 615 134 134 LEU CA C 57.670 0.115 1 616 134 134 LEU CB C 44.198 0.162 1 617 134 134 LEU CG C 27.397 0.081 1 618 134 134 LEU CD1 C 26.141 0.037 2 619 134 134 LEU CD2 C 22.934 0.158 2 620 134 134 LEU N N 123.953 0.173 1 621 135 135 VAL C C 177.105 0.114 1 622 135 135 VAL CA C 69.046 0.151 1 623 135 135 VAL CB C 31.486 0.228 1 624 135 135 VAL CG1 C 23.820 0.091 2 625 135 135 VAL CG2 C 21.080 0.141 2 626 135 135 VAL N N 123.264 0.179 1 627 136 136 ALA C C 182.426 0.071 1 628 136 136 ALA CA C 54.860 0.292 1 629 136 136 ALA CB C 18.013 0.090 1 630 136 136 ALA N N 121.161 0.141 1 631 137 137 GLN CA C 54.869 0.006 1 632 137 137 GLN N N 120.951 0.175 1 633 138 138 GLN C C 179.523 0.142 1 634 138 138 GLN CA C 59.125 0.041 1 635 138 138 GLN CB C 29.586 0.081 1 636 138 138 GLN N N 118.674 0.198 1 637 139 139 GLU CA C 59.656 0.085 1 638 139 139 GLU N N 119.273 0.086 1 639 140 140 LYS C C 177.845 0.300 1 640 140 140 LYS CA C 59.010 0.021 1 641 140 140 LYS CB C 29.843 0.300 1 642 140 140 LYS CG C 24.794 0.132 1 643 141 141 ALA C C 180.881 0.054 1 644 141 141 ALA CA C 54.711 0.152 1 645 141 141 ALA CB C 18.167 0.118 1 646 141 141 ALA N N 119.796 0.028 1 647 142 142 ALA C C 179.578 0.075 1 648 142 142 ALA CA C 55.130 0.100 1 649 142 142 ALA CB C 18.436 0.086 1 650 142 142 ALA N N 119.724 0.131 1 651 143 143 ALA C C 178.821 0.111 1 652 143 143 ALA CA C 54.421 0.124 1 653 143 143 ALA CB C 17.946 0.040 1 654 143 143 ALA N N 117.173 0.157 1 655 144 144 ASP C C 178.375 0.177 1 656 144 144 ASP CA C 57.348 0.133 1 657 144 144 ASP CB C 40.145 0.177 1 658 144 144 ASP CG C 180.008 0.300 1 659 144 144 ASP N N 120.660 0.190 1 660 145 145 VAL C C 174.025 0.188 1 661 145 145 VAL CA C 60.314 0.137 1 662 145 145 VAL CB C 30.859 0.119 1 663 145 145 VAL CG1 C 20.198 0.165 2 664 145 145 VAL CG2 C 19.132 0.033 2 665 145 145 VAL N N 108.522 0.185 1 666 146 146 GLN C C 175.436 0.095 1 667 146 146 GLN CA C 55.985 0.123 1 668 146 146 GLN CB C 26.168 0.080 1 669 146 146 GLN N N 118.240 0.176 1 670 147 147 LEU CA C 56.389 0.242 1 671 147 147 LEU CB C 43.072 0.171 1 672 147 147 LEU CG C 26.900 0.121 1 673 147 147 LEU CD1 C 25.753 0.169 2 674 147 147 LEU CD2 C 25.753 0.169 2 675 147 147 LEU N N 117.907 0.259 1 676 148 148 ARG C C 175.918 0.106 1 677 148 148 ARG CA C 54.987 0.031 1 678 148 148 ARG CB C 31.985 0.119 1 679 148 148 ARG CG C 27.023 0.285 1 680 149 149 GLY C C 171.088 0.240 1 681 149 149 GLY CA C 45.382 0.160 1 682 149 149 GLY N N 105.932 0.244 1 683 150 150 VAL C C 173.064 0.156 1 684 150 150 VAL CA C 57.894 0.135 1 685 150 150 VAL CB C 34.971 0.107 1 686 150 150 VAL CG1 C 25.946 0.072 2 687 150 150 VAL CG2 C 19.035 0.088 2 688 150 150 VAL N N 110.535 0.364 1 689 151 151 PRO C C 175.923 0.134 1 690 151 151 PRO CA C 62.454 0.176 1 691 151 151 PRO CB C 35.806 0.178 1 692 151 151 PRO CD C 51.505 0.163 1 693 151 151 PRO N N 133.882 0.228 1 694 152 152 ALA C C 174.811 0.154 1 695 152 152 ALA CA C 51.935 0.160 1 696 152 152 ALA CB C 25.548 0.052 1 697 152 152 ALA N N 122.739 0.255 1 698 153 153 MET C C 173.331 0.185 1 699 153 153 MET CA C 55.038 0.094 1 700 153 153 MET CB C 36.907 0.137 1 701 153 153 MET CG C 32.248 0.148 1 702 153 153 MET N N 121.327 0.150 1 703 154 154 PHE C C 176.216 0.213 1 704 154 154 PHE CA C 55.904 0.185 1 705 154 154 PHE CB C 41.386 0.078 1 706 154 154 PHE CG C 139.750 0.057 1 707 154 154 PHE CD1 C 130.167 0.300 3 708 154 154 PHE CD2 C 131.478 0.198 3 709 154 154 PHE N N 124.586 0.155 1 710 155 155 VAL C C 176.018 0.096 1 711 155 155 VAL CA C 60.829 0.155 1 712 155 155 VAL CB C 34.874 0.136 1 713 155 155 VAL CG1 C 22.805 0.104 2 714 155 155 VAL CG2 C 20.447 0.067 2 715 155 155 VAL N N 122.968 0.166 1 716 156 156 ASN C C 174.224 0.232 1 717 156 156 ASN CA C 54.678 0.128 1 718 156 156 ASN CB C 37.473 0.128 1 719 156 156 ASN CG C 177.215 0.092 1 720 156 156 ASN N N 127.152 0.129 1 721 157 157 GLY C C 172.655 0.164 1 722 157 157 GLY CA C 46.517 0.195 1 723 157 157 GLY N N 105.649 0.158 1 724 158 158 LYS C C 174.948 0.222 1 725 158 158 LYS CA C 57.240 0.152 1 726 158 158 LYS CB C 37.557 0.090 1 727 158 158 LYS N N 114.694 0.145 1 728 159 159 TYR C C 174.667 0.269 1 729 159 159 TYR CA C 55.446 0.104 1 730 159 159 TYR CB C 42.898 0.045 1 731 159 159 TYR CG C 128.798 0.028 1 732 159 159 TYR CE1 C 118.034 0.033 3 733 159 159 TYR N N 117.623 0.151 1 734 160 160 GLN C C 175.856 0.072 1 735 160 160 GLN CA C 53.420 0.100 1 736 160 160 GLN CB C 30.735 0.050 1 737 161 161 LEU C C 177.598 0.300 1 738 161 161 LEU CB C 40.540 0.045 1 739 161 161 LEU CG C 28.227 0.076 1 740 162 162 ASN C C 172.333 0.159 1 741 162 162 ASN CA C 49.946 0.169 1 742 162 162 ASN CB C 38.584 0.122 1 743 162 162 ASN CG C 177.450 0.119 1 744 163 163 PRO C C 177.398 0.165 1 745 163 163 PRO CA C 64.732 0.211 1 746 163 163 PRO CB C 32.493 0.161 1 747 163 163 PRO CG C 27.846 0.146 1 748 163 163 PRO CD C 50.790 0.132 1 749 163 163 PRO N N 137.095 0.451 1 750 164 164 GLN C C 177.218 0.201 1 751 164 164 GLN CA C 57.995 0.158 1 752 164 164 GLN CB C 28.038 0.063 1 753 164 164 GLN CD C 173.858 0.300 1 754 164 164 GLN N N 114.777 0.299 1 755 165 165 GLY C C 173.642 0.240 1 756 165 165 GLY CA C 44.706 0.222 1 757 165 165 GLY N N 107.175 0.237 1 758 166 166 MET C C 174.100 0.306 1 759 166 166 MET CA C 54.578 0.160 1 760 166 166 MET CB C 34.471 0.134 1 761 166 166 MET N N 119.510 0.253 1 762 167 167 ASP CA C 54.435 0.205 1 763 167 167 ASP CB C 40.492 0.041 1 764 167 167 ASP CG C 178.563 0.300 1 765 167 167 ASP N N 121.066 0.283 1 766 168 168 THR CA C 61.175 0.109 1 767 168 168 THR CB C 68.956 0.082 1 768 168 168 THR CG2 C 22.473 0.060 1 769 169 169 SER C C 174.428 0.300 1 770 169 169 SER CA C 61.190 0.144 1 771 169 169 SER CB C 63.421 0.174 1 772 170 170 ASN CA C 52.129 0.013 1 773 171 171 MET C C 177.729 0.300 1 774 171 171 MET CB C 32.811 0.300 1 775 173 173 VAL CA C 65.661 0.300 1 776 173 173 VAL CB C 32.158 0.300 1 777 174 174 PHE C C 176.238 0.300 1 778 174 174 PHE CA C 61.804 0.159 1 779 174 174 PHE CG C 138.883 0.054 1 780 174 174 PHE N N 121.584 0.300 1 781 175 175 VAL C C 177.616 0.142 1 782 175 175 VAL CA C 66.956 0.114 1 783 175 175 VAL CB C 31.906 0.130 1 784 175 175 VAL CG1 C 21.249 0.055 2 785 175 175 VAL CG2 C 24.550 0.163 2 786 175 175 VAL N N 116.918 0.108 1 787 176 176 GLN C C 178.340 0.182 1 788 176 176 GLN CA C 58.807 0.202 1 789 176 176 GLN CB C 28.236 0.090 1 790 176 176 GLN N N 116.676 0.330 1 791 177 177 GLN C C 179.958 0.119 1 792 177 177 GLN CA C 59.286 0.141 1 793 177 177 GLN CB C 28.165 0.099 1 794 177 177 GLN CG C 34.454 0.063 1 795 177 177 GLN N N 119.180 0.049 1 796 178 178 TYR C C 177.933 0.134 1 797 178 178 TYR CA C 61.885 0.115 1 798 178 178 TYR CB C 38.203 0.311 1 799 178 178 TYR CG C 129.884 0.086 1 800 178 178 TYR CE2 C 117.376 0.017 3 801 178 178 TYR N N 126.471 0.186 1 802 179 179 ALA C C 179.685 0.089 1 803 179 179 ALA CA C 55.382 0.143 1 804 179 179 ALA CB C 18.371 0.108 1 805 179 179 ALA N N 121.844 0.066 1 806 180 180 ASP C C 179.654 0.124 1 807 180 180 ASP CA C 57.389 0.115 1 808 180 180 ASP CB C 39.949 0.198 1 809 180 180 ASP CG C 179.486 0.300 1 810 180 180 ASP N N 118.657 0.268 1 811 181 181 THR C C 176.448 0.139 1 812 181 181 THR CA C 67.123 0.432 1 813 181 181 THR CB C 68.724 0.030 1 814 181 181 THR CG2 C 22.412 0.049 1 815 181 181 THR N N 120.217 0.075 1 816 182 182 VAL C C 177.396 0.127 1 817 182 182 VAL CA C 67.577 0.210 1 818 182 182 VAL CB C 30.626 0.256 1 819 182 182 VAL CG1 C 24.111 0.274 2 820 182 182 VAL CG2 C 22.396 0.164 2 821 182 182 VAL N N 121.541 0.179 1 822 183 183 LYS CA C 54.826 0.300 1 823 183 183 LYS N N 120.981 0.067 1 824 184 184 TYR C C 177.788 0.080 1 825 184 184 TYR CA C 60.518 0.181 1 826 184 184 TYR CG C 129.980 0.088 1 827 184 184 TYR N N 120.095 0.300 1 828 185 185 LEU C C 179.374 0.097 1 829 185 185 LEU CA C 56.589 0.102 1 830 185 185 LEU CB C 42.204 0.080 1 831 185 185 LEU CG C 25.720 0.042 1 832 185 185 LEU N N 118.050 0.227 1 833 186 186 SER C C 175.685 0.222 1 834 186 186 SER CA C 61.778 0.119 1 835 186 186 SER CB C 62.664 0.061 1 836 186 186 SER N N 114.893 0.170 1 837 187 187 GLU CA C 56.096 0.128 1 838 187 187 GLU CB C 30.228 0.300 1 839 187 187 GLU N N 119.305 0.166 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity ',,,,,,,' ',,,,,,' ',,,,,,' ',,' ',' ',' stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR' '3D NCACX' '3D NCOCX' '3D CAN(CO)CX' '3D CON(CA)CX' '4D CANCOCX' '2D NC TEDOR' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_Adam _Mol_system_component_name DsbB _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 1 365 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_ loop_ _Atom_shift_assign_ID_ambiguity ',,,,,,,' ',,,,,,' ',,,,,,' ',,' ',' ',' stop_ save_ save_assigned_chem_shift_list_1_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D CC DARR' '3D NCACX' '3D NCOCX' '3D CAN(CO)CX' '3D CON(CA)CX' '4D CANCOCX' '2D NC TEDOR' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 $sample_5 $sample_6 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_Adam _Mol_system_component_name UBIQUINONE-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 1 501 1 UQ8 C1 C 135.534 0.060 1 2 501 1 UQ8 C10 C 20.609 0.118 4 3 501 1 UQ8 C11 C 43.400 0.643 4 4 501 1 UQ8 C2 C 154.709 0.300 1 5 501 1 UQ8 C3 C 142.410 0.300 4 6 501 1 UQ8 C4 C 142.410 0.300 1 7 501 1 UQ8 C5 C 154.709 0.300 4 8 501 1 UQ8 C6 C 127.427 0.300 1 9 501 1 UQ8 C7 C 26.580 0.011 4 10 501 1 UQ8 C8 C 123.680 0.098 4 11 501 1 UQ8 C9 C 140.100 0.117 4 12 501 1 UQ8 C12 C 30.300 0.643 4 13 501 1 UQ8 C15 C 20.700 0.643 4 14 501 1 UQ8 C16 C 43.000 0.643 4 15 501 1 UQ8 C17 C 29.800 0.643 4 16 501 1 UQ8 C1M C 15.859 0.061 1 17 501 1 UQ8 C21 C 42.600 0.643 4 18 501 1 UQ8 C22 C 29.300 0.643 4 19 501 1 UQ8 C25 C 19.700 0.643 4 20 501 1 UQ8 C26 C 42.200 0.643 4 21 501 1 UQ8 C27 C 28.800 0.643 4 22 501 1 UQ8 C20 C 20.200 0.643 4 23 501 1 UQ8 C30 C 19.200 0.643 4 24 501 1 UQ8 C31 C 41.800 0.643 4 25 501 1 UQ8 C32 C 28.300 0.643 4 26 501 1 UQ8 C35 C 18.700 0.643 4 27 501 1 UQ8 C36 C 41.400 0.643 4 28 501 1 UQ8 C37 C 27.800 0.643 4 29 501 1 UQ8 C38 C 124.750 0.300 4 30 501 1 UQ8 C39 C 136.254 0.051 4 31 501 1 UQ8 C40 C 18.200 0.643 4 32 501 1 UQ8 C41 C 41.517 0.095 4 33 501 1 UQ8 C42 C 28.260 0.020 4 34 501 1 UQ8 C43 C 126.157 0.271 4 35 501 1 UQ8 C44 C 135.212 0.112 4 36 501 1 UQ8 C45 C 17.920 0.069 1 37 501 1 UQ8 C46 C 28.177 0.074 4 38 501 1 UQ8 C3M C 63.804 0.193 4 39 501 1 UQ8 C4M C 63.804 0.193 4 stop_ loop_ _Atom_shift_assign_ID_ambiguity ',,,,,,,' ',,,,,,' ',,,,,,' ',,' ',' ',' stop_ save_