data_18395 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of deuterated DsbB by 1H-detected solid-state NMR ; _BMRB_accession_number 18395 _BMRB_flat_file_name bmr18395.str _Entry_type original _Submission_date 2012-04-13 _Accession_date 2012-04-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shift assignments of deuterated DsbB by 1H-detected solid-state NMR' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Donghua H. . 2 Nieuwkoop Andrew J. . 3 Berthold Deborah A. . 4 Comellas Gemma H. . 5 Sperling Lindsay J. . 6 Tang Ming . . 7 Shah Gautam J. . 8 Brea Elliot J. . 9 Lemkau Luisel R. . 10 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "13C chemical shifts" 132 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-09-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15546 'Chemical shift assignments for DsbB' 15966 'Integral membrane protein DsbB in solution' 17710 'Membrane protein complex DsbB-DsbA' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22986689 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Donghua H. . 2 Nieuwkoop Andrew J. . 3 Berthold Deborah A. . 4 Comellas Gemma . . 5 Sperling Lindsay J. . 6 Tang Ming . . 7 Shah Gautam J. . 8 Brea Elliott J. . 9 Lemkau Luisel R. . 10 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 54 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 305 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DsbB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbB $DsbB 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 15287.664 _Mol_thiol_state 'free and disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 176 _Mol_residue_sequence ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP CVLCIYERVALFGVLGAALI 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 CYS 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 99.43 99.43 8.89e-122 BMRB 15966 Disulfide_bond_formation_protein_B 100.00 183 98.30 98.30 5.27e-120 BMRB 18493 DsbB 100.00 176 99.43 99.43 1.46e-121 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 176 99.43 99.43 1.46e-121 PDB 2K73 "Solution Nmr Structure Of Integral Membrane Protein Dsbb" 100.00 183 98.30 98.30 5.27e-120 PDB 2K74 "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" 100.00 183 98.30 98.30 5.27e-120 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 100.00 176 99.43 99.43 1.46e-121 PDB 2LTQ "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" 100.00 176 99.43 99.43 1.46e-121 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 176 99.43 99.43 1.46e-121 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 100.00 176 99.43 99.43 1.46e-121 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 182 100.00 100.00 7.54e-123 DBJ BAA07408 "disulfide oxidoreductase [Shigella flexneri]" 100.00 176 97.16 97.73 1.74e-118 DBJ BAA36032 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 176 98.86 98.86 4.75e-121 DBJ BAB35103 "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.86 98.86 4.75e-121 DBJ BAG76757 "disulfide bond formation protein [Escherichia coli SE11]" 100.00 176 97.73 98.30 1.44e-119 DBJ BAI24997 "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" 100.00 176 98.30 98.86 1.04e-120 EMBL CAP75720 "Disulfide bond formation protein B [Escherichia coli LF82]" 100.00 176 97.73 98.30 7.47e-120 EMBL CAQ31687 "DsbB[reduced] [Escherichia coli BL21(DE3)]" 100.00 176 98.86 98.86 4.75e-121 EMBL CAQ98064 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" 100.00 176 98.86 98.86 4.75e-121 EMBL CAR02574 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" 100.00 176 97.73 98.30 7.47e-120 EMBL CAR07527 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli ED1a]" 100.00 176 97.16 97.73 2.65e-119 GB AAA23711 "oxido-reductase [Escherichia coli]" 100.00 178 98.86 98.86 4.32e-121 GB AAB25233 "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" 100.00 176 98.86 98.86 4.75e-121 GB AAC74269 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 176 98.86 98.86 4.75e-121 GB AAG56036 "reoxidizes DsbA protein following formation of disulfide bond in P-ring of flagella [Escherichia coli O157:H7 str. EDL933]" 100.00 176 98.30 98.30 3.29e-120 GB AAN42789 "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" 100.00 176 98.30 98.86 1.04e-120 PIR H85696 "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 176 98.30 98.30 3.29e-120 REF NP_309707 "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" 100.00 176 98.86 98.86 4.75e-121 REF NP_415703 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 176 98.86 98.86 4.75e-121 REF NP_707082 "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" 100.00 176 98.30 98.86 1.04e-120 REF WP_000652474 "disulfide bond formation protein B, partial [Escherichia coli]" 69.32 122 100.00 100.00 1.26e-81 REF WP_000943441 "disulfide bond formation protein B [Escherichia coli]" 100.00 176 97.16 97.73 4.84e-119 SP A1AAA8 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 97.73 98.30 7.47e-120 SP P0A6M2 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 98.86 98.86 4.75e-121 SP P0A6M3 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 98.86 98.86 4.75e-121 SP P59343 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 97.73 98.30 7.47e-120 SP Q0T5L6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 100.00 176 98.30 98.86 1.04e-120 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $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 $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 $DsbB 3 mg '[U-100% 13C; U-100% 15N; U-80% 2H]' 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_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_ ############################# # NMR applied experiments # ############################# save_3D_CANH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANH' _Sample_label $sample_1 save_ save_3D_CONH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONH' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'DsbB sample' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . pH pressure 1 . atm temperature 248 . 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_DsbA _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CANH' '3D CONH' stop_ loop_ _Sample_label $sample_1 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 179.379 0.300 1 2 7 7 GLN H H 9.338 0.026 1 3 7 7 GLN C C 180.296 0.300 1 4 7 7 GLN CA C 57.933 0.300 1 5 7 7 GLN N N 120.575 0.085 1 6 8 8 ALA H H 9.436 0.052 1 7 8 8 ALA CA C 54.704 0.300 1 8 8 8 ALA N N 123.657 0.059 1 9 9 9 SER C C 174.107 0.300 1 10 10 10 GLN H H 7.835 0.030 1 11 10 10 GLN C C 174.766 0.300 1 12 10 10 GLN CA C 56.086 0.300 1 13 10 10 GLN N N 119.421 0.018 1 14 11 11 GLY H H 8.433 0.005 1 15 11 11 GLY CA C 43.935 0.300 1 16 11 11 GLY N N 108.456 0.067 1 17 13 13 GLY C C 175.091 0.300 1 18 14 14 ALA H H 9.285 0.003 1 19 14 14 ALA C C 179.173 0.300 1 20 14 14 ALA CA C 55.745 0.300 1 21 14 14 ALA N N 123.181 0.019 1 22 15 15 TRP H H 7.091 0.008 1 23 15 15 TRP C C 179.425 0.300 1 24 15 15 TRP CA C 59.674 0.300 1 25 15 15 TRP N N 116.733 0.031 1 26 16 16 LEU H H 9.145 0.030 1 27 16 16 LEU CA C 57.735 0.300 1 28 16 16 LEU N N 118.718 0.081 1 29 18 18 MET C C 180.743 0.300 1 30 19 19 ALA H H 9.398 0.009 1 31 19 19 ALA CA C 54.698 0.300 1 32 19 19 ALA N N 123.824 0.068 1 33 22 22 ALA C C 179.256 0.300 1 34 23 23 LEU H H 8.646 0.024 1 35 23 23 LEU CA C 57.528 0.300 1 36 23 23 LEU N N 119.008 0.002 1 37 24 24 ALA C C 180.186 0.300 1 38 25 25 LEU H H 9.179 0.015 1 39 25 25 LEU CA C 58.045 0.300 1 40 25 25 LEU N N 119.465 0.014 1 41 26 26 GLU H H 8.818 0.030 1 42 26 26 GLU C C 179.199 0.300 1 43 26 26 GLU CA C 59.290 0.300 1 44 26 26 GLU N N 120.120 0.300 1 45 27 27 LEU H H 9.367 0.016 1 46 27 27 LEU CA C 57.379 0.300 1 47 27 27 LEU N N 119.866 0.074 1 48 28 28 THR C C 176.033 0.300 1 49 29 29 ALA H H 8.302 0.020 1 50 29 29 ALA C C 179.409 0.300 1 51 29 29 ALA CA C 56.027 0.300 1 52 29 29 ALA N N 122.847 0.154 1 53 30 30 LEU H H 8.412 0.023 1 54 30 30 LEU C C 178.270 0.300 1 55 30 30 LEU CA C 57.535 0.300 1 56 30 30 LEU N N 117.595 0.300 1 57 31 31 TRP H H 9.157 0.012 1 58 31 31 TRP C C 179.053 0.300 1 59 31 31 TRP CA C 61.335 0.300 1 60 31 31 TRP N N 125.692 0.018 1 61 32 32 PHE H H 9.374 0.012 1 62 32 32 PHE CA C 60.503 0.300 1 63 32 32 PHE N N 119.195 0.300 1 64 33 33 GLN C C 177.778 0.300 1 65 34 34 HIS H H 9.617 0.030 1 66 34 34 HIS CA C 58.962 0.300 1 67 34 34 HIS N N 115.897 0.014 1 68 35 35 VAL C C 177.853 0.300 1 69 36 36 MET H H 7.591 0.033 1 70 36 36 MET C C 175.905 0.300 1 71 36 36 MET CA C 56.149 0.300 1 72 36 36 MET N N 114.145 0.036 1 73 37 37 LEU H H 7.104 0.011 1 74 37 37 LEU CA C 55.909 0.300 1 75 37 37 LEU N N 111.752 0.045 1 76 38 38 LEU C C 176.457 0.300 1 77 39 39 LYS H H 9.350 0.022 1 78 39 39 LYS CA C 53.399 0.300 1 79 39 39 LYS N N 121.416 0.026 1 80 43 43 LEU C C 177.956 0.300 1 81 44 44 CYS H H 7.683 0.032 1 82 44 44 CYS CA C 59.567 0.300 1 83 44 44 CYS N N 114.278 0.084 1 84 45 45 ILE C C 179.151 0.300 1 85 46 46 TYR H H 8.934 0.051 1 86 46 46 TYR C C 178.432 0.300 1 87 46 46 TYR CA C 59.091 0.300 1 88 46 46 TYR N N 120.507 0.119 1 89 47 47 GLU H H 9.681 0.005 1 90 47 47 GLU C C 180.186 0.300 1 91 47 47 GLU CA C 58.991 0.300 1 92 47 47 GLU N N 121.791 0.004 1 93 48 48 ARG H H 9.213 0.020 1 94 48 48 ARG CA C 60.570 0.300 1 95 48 48 ARG N N 119.454 0.004 1 96 51 51 LEU C C 178.625 0.300 1 97 52 52 PHE H H 8.863 0.012 1 98 52 52 PHE C C 179.469 0.300 1 99 52 52 PHE CA C 62.624 0.300 1 100 52 52 PHE N N 122.736 0.036 1 101 53 53 GLY H H 9.027 0.010 1 102 53 53 GLY C C 175.909 0.300 1 103 53 53 GLY CA C 48.047 0.300 1 104 53 53 GLY N N 110.986 0.022 1 105 54 54 VAL H H 7.948 0.031 1 106 54 54 VAL C C 176.751 0.300 1 107 54 54 VAL CA C 67.713 0.300 1 108 54 54 VAL N N 122.121 0.021 1 109 55 55 LEU H H 8.646 0.011 1 110 55 55 LEU CA C 57.821 0.300 1 111 55 55 LEU N N 120.083 0.111 1 112 57 57 ALA C C 179.256 0.300 1 113 58 58 ALA H H 8.674 0.003 1 114 58 58 ALA CA C 54.823 0.300 1 115 58 58 ALA N N 119.050 0.044 1 116 60 60 ILE C C 180.304 0.300 1 117 61 61 GLY H H 9.046 0.002 1 118 61 61 GLY C C 174.221 0.300 1 119 61 61 GLY CA C 45.805 0.300 1 120 61 61 GLY N N 110.005 0.001 1 121 62 62 ALA H H 8.066 0.012 1 122 62 62 ALA CA C 53.391 0.300 1 123 62 62 ALA N N 119.084 0.013 1 124 68 68 PRO C C 177.070 0.300 1 125 69 69 LEU H H 8.882 0.010 1 126 69 69 LEU C C 179.756 0.300 1 127 69 69 LEU CA C 57.516 0.300 1 128 69 69 LEU N N 121.517 0.015 1 129 70 70 ARG H H 8.177 0.011 1 130 70 70 ARG C C 177.925 0.300 1 131 70 70 ARG CA C 59.142 0.300 1 132 70 70 ARG N N 114.237 0.010 1 133 71 71 TYR H H 8.136 0.015 1 134 71 71 TYR CA C 58.808 0.300 1 135 71 71 TYR N N 121.740 0.015 1 136 72 72 VAL C C 177.807 0.300 1 137 73 73 ALA H H 8.994 0.002 1 138 73 73 ALA C C 179.897 0.300 1 139 73 73 ALA CA C 55.793 0.300 1 140 73 73 ALA N N 120.755 0.071 1 141 74 74 MET H H 8.163 0.008 1 142 74 74 MET C C 177.604 0.300 1 143 74 74 MET CA C 62.224 0.300 1 144 74 74 MET N N 115.192 0.132 1 145 75 75 VAL H H 7.554 0.034 1 146 75 75 VAL CA C 66.272 0.300 1 147 75 75 VAL N N 118.669 0.036 1 148 76 76 ILE C C 179.097 0.300 1 149 77 77 TRP H H 9.515 0.015 1 150 77 77 TRP C C 176.907 0.300 1 151 77 77 TRP CA C 58.934 0.300 1 152 77 77 TRP N N 125.432 0.034 1 153 78 78 LEU H H 9.367 0.005 1 154 78 78 LEU CA C 58.374 0.300 1 155 78 78 LEU N N 119.059 0.030 1 156 86 86 GLN C C 180.109 0.300 1 157 87 87 LEU H H 8.955 0.025 1 158 87 87 LEU C C 178.871 0.300 1 159 87 87 LEU CA C 57.725 0.300 1 160 87 87 LEU N N 120.967 0.033 1 161 88 88 THR H H 8.764 0.046 1 162 88 88 THR C C 180.013 0.300 1 163 88 88 THR CA C 65.348 0.300 1 164 88 88 THR N N 108.293 0.012 1 165 89 89 TYR H H 9.868 0.002 1 166 89 89 TYR C C 177.244 0.300 1 167 89 89 TYR CA C 63.163 0.300 1 168 89 89 TYR N N 127.947 0.039 1 169 90 90 GLU H H 8.515 0.020 1 170 90 90 GLU C C 178.322 0.300 1 171 90 90 GLU CA C 59.638 0.300 1 172 90 90 GLU N N 121.163 0.032 1 173 91 91 HIS H H 9.107 0.030 1 174 91 91 HIS C C 177.708 0.300 1 175 91 91 HIS CA C 57.803 0.300 1 176 91 91 HIS N N 120.257 0.071 1 177 92 92 THR H H 9.550 0.009 1 178 92 92 THR CA C 65.723 0.300 1 179 92 92 THR N N 115.562 0.024 1 180 96 96 LEU C C 177.615 0.300 1 181 97 97 TYR H H 8.485 0.004 1 182 97 97 TYR CA C 57.199 0.300 1 183 97 97 TYR N N 117.120 0.017 1 184 101 101 PHE C C 174.992 0.300 1 185 102 102 ALA H H 7.383 0.024 1 186 102 102 ALA C C 176.810 0.300 1 187 102 102 ALA CA C 52.788 0.300 1 188 102 102 ALA N N 120.614 0.024 1 189 103 103 THR H H 9.278 0.020 1 190 103 103 THR C C 175.821 0.300 1 191 103 103 THR CA C 58.383 0.300 1 192 103 103 THR N N 112.733 0.043 1 193 104 104 CYS H H 9.934 0.012 1 194 104 104 CYS C C 174.474 0.300 1 195 104 104 CYS CA C 55.932 0.300 1 196 104 104 CYS N N 122.776 0.004 1 197 105 105 ASP H H 8.153 0.005 1 198 105 105 ASP CA C 53.905 0.300 1 199 105 105 ASP N N 121.350 0.012 1 200 112 112 GLU C C 177.165 0.300 1 201 113 113 TRP H H 9.665 0.012 1 202 113 113 TRP CA C 56.056 0.300 1 203 113 113 TRP N N 111.767 0.018 1 204 117 117 ASP C C 177.610 0.300 1 205 118 118 LYS H H 7.513 0.001 1 206 118 118 LYS CA C 57.323 0.300 1 207 118 118 LYS N N 119.095 0.013 1 208 119 119 TRP C C 177.867 0.300 1 209 120 120 VAL H H 8.936 0.019 1 210 120 120 VAL CA C 58.898 0.300 1 211 120 120 VAL N N 113.149 0.024 1 212 121 121 PRO C C 178.888 0.300 1 213 122 122 GLN H H 9.809 0.005 1 214 122 122 GLN C C 174.326 0.300 1 215 122 122 GLN CA C 58.418 0.300 1 216 122 122 GLN N N 116.304 0.039 1 217 123 123 VAL H H 8.219 0.004 1 218 123 123 VAL CA C 61.823 0.300 1 219 123 123 VAL N N 113.233 0.056 1 220 124 124 PHE C C 173.145 0.300 1 221 125 125 VAL H H 7.783 0.002 1 222 125 125 VAL C C 177.034 0.300 1 223 125 125 VAL CA C 62.322 0.300 1 224 125 125 VAL N N 115.594 0.054 1 225 126 126 ALA H H 8.994 0.011 1 226 126 126 ALA C C 175.920 0.300 1 227 126 126 ALA CA C 51.887 0.300 1 228 126 126 ALA N N 130.683 0.040 1 229 127 127 SER H H 8.145 0.026 1 230 127 127 SER CA C 57.740 0.300 1 231 127 127 SER N N 112.716 0.005 1 232 128 128 GLY H H 8.537 0.030 1 233 128 128 GLY CA C 46.419 0.300 1 234 128 128 GLY N N 106.504 0.300 1 235 129 129 ASP C C 177.916 0.300 1 236 130 130 CYS H H 9.948 0.003 1 237 130 130 CYS C C 173.312 0.300 1 238 130 130 CYS CA C 55.938 0.300 1 239 130 130 CYS N N 122.984 0.016 1 240 131 131 ALA H H 9.869 0.029 1 241 131 131 ALA CA C 53.363 0.300 1 242 131 131 ALA N N 121.534 0.128 1 243 136 136 ASP C C 172.916 0.300 1 244 137 137 PHE H H 8.959 0.005 1 245 137 137 PHE CA C 57.048 0.300 1 246 137 137 PHE N N 117.677 0.047 1 247 144 144 GLN C C 177.307 0.300 1 248 145 145 TRP H H 8.386 0.037 1 249 145 145 TRP C C 179.365 0.300 1 250 145 145 TRP CA C 59.713 0.300 1 251 145 145 TRP N N 120.795 0.006 1 252 146 146 LEU H H 9.027 0.002 1 253 146 146 LEU C C 177.072 0.300 1 254 146 146 LEU CA C 57.744 0.300 1 255 146 146 LEU N N 118.487 0.094 1 256 147 147 LEU H H 8.458 0.009 1 257 147 147 LEU CA C 58.415 0.300 1 258 147 147 LEU N N 123.843 0.036 1 259 152 152 ALA C C 180.240 0.300 1 260 153 153 TYR H H 8.680 0.007 1 261 153 153 TYR CA C 61.101 0.300 1 262 153 153 TYR N N 115.623 0.011 1 263 162 162 ILE C C 176.885 0.300 1 264 163 163 SER H H 9.427 0.022 1 265 163 163 SER CA C 58.524 0.300 1 266 163 163 SER N N 112.832 0.300 1 stop_ save_