data_27014 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments (HN,N,CA,CB) of oxidised c-NmDsbD ; _BMRB_accession_number 27014 _BMRB_flat_file_name bmr27014.str _Entry_type original _Submission_date 2017-01-26 _Accession_date 2017-01-26 _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 Smith Roxanne P. . 2 Mohanty Biswaranjan . . 3 Williams Martin L. . 4 Heras Begona . . 5 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 "13C chemical shifts" 255 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-02-06 update BMRB 'update entry citation' 2017-06-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27012 'oxidised n-NmDsbD' 27013 'reduced n-NmDsbD' 27015 'reduced c-NmDsbD' stop_ _Original_release_date 2017-01-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28589218 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Roxanne P. . 2 Mohanty Biswaranjan . . 3 Williams Martin L. . 4 Scanlon Martin J. . 5 Heras Begona . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 11 _Journal_issue 2 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 181 _Page_last 186 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'c-NmDsbD monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal periplasmic domain NmDsbD' $Oxidised_c-NmDsbD 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_Oxidised_c-NmDsbD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Oxidised_c-NmDsbD _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; MHHHHHHSSGVDLGTENLYF QSNAMFADTAALKAAMDTAL KEHPDKPVVLDFYADWCISC KEMAAYTLNQPEVHQAVDME RFFQIDVTANKPEHQALLKE YGLFGPPGVFVVRSDGSRSE PLLGFVKADKFIEWYEQNR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 SER 9 SER 10 GLY 11 VAL 12 ASP 13 LEU 14 GLY 15 THR 16 GLU 17 ASN 18 LEU 19 TYR 20 PHE 21 GLN 22 SER 23 ASN 24 ALA 25 MET 26 PHE 27 ALA 28 ASP 29 THR 30 ALA 31 ALA 32 LEU 33 LYS 34 ALA 35 ALA 36 MET 37 ASP 38 THR 39 ALA 40 LEU 41 LYS 42 GLU 43 HIS 44 PRO 45 ASP 46 LYS 47 PRO 48 VAL 49 VAL 50 LEU 51 ASP 52 PHE 53 TYR 54 ALA 55 ASP 56 TRP 57 CYS 58 ILE 59 SER 60 CYS 61 LYS 62 GLU 63 MET 64 ALA 65 ALA 66 TYR 67 THR 68 LEU 69 ASN 70 GLN 71 PRO 72 GLU 73 VAL 74 HIS 75 GLN 76 ALA 77 VAL 78 ASP 79 MET 80 GLU 81 ARG 82 PHE 83 PHE 84 GLN 85 ILE 86 ASP 87 VAL 88 THR 89 ALA 90 ASN 91 LYS 92 PRO 93 GLU 94 HIS 95 GLN 96 ALA 97 LEU 98 LEU 99 LYS 100 GLU 101 TYR 102 GLY 103 LEU 104 PHE 105 GLY 106 PRO 107 PRO 108 GLY 109 VAL 110 PHE 111 VAL 112 VAL 113 ARG 114 SER 115 ASP 116 GLY 117 SER 118 ARG 119 SER 120 GLU 121 PRO 122 LEU 123 LEU 124 GLY 125 PHE 126 VAL 127 LYS 128 ALA 129 ASP 130 LYS 131 PHE 132 ILE 133 GLU 134 TRP 135 TYR 136 GLU 137 GLN 138 ASN 139 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Oxidised_c-NmDsbD 'Neisseria meningitidis' 487 Bacteria . Neisseria meningitidis 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 $Oxidised_c-NmDsbD 'recombinant technology' . Escherichia coli . pMCSG7 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM protein; 10 mM Sodium Phosphate; 50 mM NaCl; pH 6.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Oxidised_c-NmDsbD 1 mM '[U-98% 13C; U-98% 15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' 'sodium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Topspin _Saveframe_category software _Name Topspin _Version 3.2 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task Acquisition processing stop_ _Details Topspin3.2(pl6) save_ save_UNIO-MATCH _Saveframe_category software _Name UNIO-MATCH _Version 2.0.2 loop_ _Vendor _Address _Electronic_address 'Volk,J., Herrmann,T.,Wuthrich,K.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller, K. and Wuthrich, K.' . . stop_ loop_ _Task 'chemical shift calculation' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_[15N,1H]-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D [15N,1H]-HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D [15N,1H]-HSQC' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'C-terminal periplasmic domain NmDsbD' _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 8 8 SER CA C 58.213 0.3 1 2 8 8 SER CB C 63.556 0.3 1 3 9 9 SER H H 8.513 0.02 1 4 9 9 SER CA C 58.516 0.3 1 5 9 9 SER CB C 63.824 0.3 1 6 9 9 SER N N 118.339 0.25 1 7 10 10 GLY H H 8.432 0.02 1 8 10 10 GLY CA C 45.345 0.3 1 9 10 10 GLY N N 111.168 0.25 1 10 11 11 VAL H H 7.885 0.02 1 11 11 11 VAL CA C 61.921 0.3 1 12 11 11 VAL CB C 32.729 0.3 1 13 11 11 VAL N N 119.113 0.25 1 14 12 12 ASP H H 8.393 0.02 1 15 12 12 ASP CA C 54.100 0.3 1 16 12 12 ASP CB C 41.090 0.3 1 17 12 12 ASP N N 124.218 0.25 1 18 13 13 LEU H H 8.344 0.02 1 19 13 13 LEU CA C 55.395 0.3 1 20 13 13 LEU CB C 42.143 0.3 1 21 13 13 LEU N N 124.092 0.25 1 22 14 14 GLY H H 8.540 0.02 1 23 14 14 GLY CA C 45.518 0.3 1 24 14 14 GLY N N 109.654 0.25 1 25 15 15 THR H H 7.967 0.02 1 26 15 15 THR CA C 61.937 0.3 1 27 15 15 THR CB C 69.507 0.3 1 28 15 15 THR N N 113.173 0.25 1 29 16 16 GLU H H 8.526 0.02 1 30 16 16 GLU CA C 56.937 0.3 1 31 16 16 GLU CB C 29.940 0.3 1 32 16 16 GLU N N 123.105 0.25 1 33 17 17 ASN H H 8.360 0.02 1 34 17 17 ASN CA C 53.169 0.3 1 35 17 17 ASN CB C 38.721 0.3 1 36 17 17 ASN N N 119.408 0.25 1 37 18 18 LEU H H 8.035 0.02 1 38 18 18 LEU CA C 55.189 0.3 1 39 18 18 LEU CB C 42.194 0.3 1 40 18 18 LEU N N 122.461 0.25 1 41 19 19 TYR H H 7.943 0.02 1 42 19 19 TYR CA C 57.567 0.3 1 43 19 19 TYR CB C 38.647 0.3 1 44 19 19 TYR N N 120.524 0.25 1 45 20 20 PHE H H 8.005 0.02 1 46 20 20 PHE CA C 57.879 0.3 1 47 20 20 PHE CB C 39.892 0.3 1 48 20 20 PHE N N 122.340 0.25 1 49 21 21 GLN H H 7.917 0.02 1 50 21 21 GLN CA C 55.190 0.3 1 51 21 21 GLN CB C 30.013 0.3 1 52 21 21 GLN N N 123.825 0.25 1 53 22 22 SER H H 8.164 0.02 1 54 22 22 SER CA C 58.394 0.3 1 55 22 22 SER CB C 63.710 0.3 1 56 22 22 SER N N 118.030 0.25 1 57 23 23 ASN H H 8.510 0.02 1 58 23 23 ASN CA C 53.517 0.3 1 59 23 23 ASN CB C 38.804 0.3 1 60 23 23 ASN N N 120.922 0.25 1 61 24 24 ALA H H 8.315 0.02 1 62 24 24 ALA CA C 51.588 0.3 1 63 24 24 ALA CB C 18.809 0.3 1 64 24 24 ALA N N 125.463 0.25 1 65 25 25 MET H H 7.697 0.02 1 66 25 25 MET CA C 55.703 0.3 1 67 25 25 MET CB C 33.392 0.3 1 68 25 25 MET N N 120.481 0.25 1 69 26 26 PHE H H 8.909 0.02 1 70 26 26 PHE CA C 58.141 0.3 1 71 26 26 PHE CB C 42.446 0.3 1 72 26 26 PHE N N 124.198 0.25 1 73 27 27 ALA H H 9.076 0.02 1 74 27 27 ALA CA C 52.347 0.3 1 75 27 27 ALA CB C 20.810 0.3 1 76 27 27 ALA N N 121.856 0.25 1 77 28 28 ASP H H 7.811 0.02 1 78 28 28 ASP CA C 52.633 0.3 1 79 28 28 ASP CB C 43.413 0.3 1 80 28 28 ASP N N 121.790 0.25 1 81 29 29 THR H H 9.172 0.02 1 82 29 29 THR CA C 65.748 0.3 1 83 29 29 THR CB C 67.603 0.3 1 84 29 29 THR N N 119.033 0.25 1 85 30 30 ALA H H 8.561 0.02 1 86 30 30 ALA CA C 55.102 0.3 1 87 30 30 ALA CB C 17.550 0.3 1 88 30 30 ALA N N 127.775 0.25 1 89 31 31 ALA H H 7.957 0.02 1 90 31 31 ALA CA C 54.491 0.3 1 91 31 31 ALA CB C 18.019 0.3 1 92 31 31 ALA N N 123.786 0.25 1 93 32 32 LEU H H 7.511 0.02 1 94 32 32 LEU CA C 57.405 0.3 1 95 32 32 LEU CB C 41.527 0.3 1 96 32 32 LEU N N 120.734 0.25 1 97 33 33 LYS H H 8.004 0.02 1 98 33 33 LYS CA C 58.904 0.3 1 99 33 33 LYS CB C 28.109 0.3 1 100 33 33 LYS N N 118.735 0.25 1 101 34 34 ALA H H 8.387 0.02 1 102 34 34 ALA CA C 54.689 0.3 1 103 34 34 ALA CB C 17.643 0.3 1 104 34 34 ALA N N 121.333 0.25 1 105 35 35 ALA H H 7.655 0.02 1 106 35 35 ALA CA C 54.954 0.3 1 107 35 35 ALA CB C 19.046 0.3 1 108 35 35 ALA N N 122.568 0.25 1 109 36 36 MET H H 8.263 0.02 1 110 36 36 MET CA C 59.959 0.3 1 111 36 36 MET CB C 33.546 0.3 1 112 36 36 MET N N 120.069 0.25 1 113 37 37 ASP H H 8.454 0.02 1 114 37 37 ASP CA C 57.548 0.3 1 115 37 37 ASP CB C 40.502 0.3 1 116 37 37 ASP N N 119.105 0.25 1 117 38 38 THR H H 8.102 0.02 1 118 38 38 THR CA C 67.044 0.3 1 119 38 38 THR CB C 68.760 0.3 1 120 38 38 THR N N 116.747 0.25 1 121 39 39 ALA H H 7.712 0.02 1 122 39 39 ALA CA C 55.184 0.3 1 123 39 39 ALA CB C 17.748 0.3 1 124 39 39 ALA N N 124.083 0.25 1 125 40 40 LEU H H 8.454 0.02 1 126 40 40 LEU CA C 57.370 0.3 1 127 40 40 LEU CB C 42.118 0.3 1 128 40 40 LEU N N 122.061 0.25 1 129 41 41 LYS H H 8.025 0.02 1 130 41 41 LYS CA C 58.246 0.3 1 131 41 41 LYS CB C 32.510 0.3 1 132 41 41 LYS N N 118.970 0.25 1 133 42 42 GLU H H 8.176 0.02 1 134 42 42 GLU CA C 58.491 0.3 1 135 42 42 GLU CB C 30.179 0.3 1 136 42 42 GLU N N 118.266 0.25 1 137 43 43 HIS H H 7.084 0.02 1 138 43 43 HIS CA C 52.577 0.3 1 139 43 43 HIS CB C 30.078 0.3 1 140 43 43 HIS N N 111.270 0.25 1 141 44 44 PRO CA C 64.549 0.3 1 142 44 44 PRO CB C 31.574 0.3 1 143 45 45 ASP H H 9.314 0.02 1 144 45 45 ASP CA C 53.351 0.3 1 145 45 45 ASP CB C 39.409 0.3 1 146 45 45 ASP N N 115.829 0.25 1 147 46 46 LYS H H 7.847 0.02 1 148 46 46 LYS CA C 52.431 0.3 1 149 46 46 LYS CB C 34.242 0.3 1 150 46 46 LYS N N 121.088 0.25 1 151 47 47 PRO CA C 62.935 0.3 1 152 47 47 PRO CB C 33.909 0.3 1 153 48 48 VAL H H 9.209 0.02 1 154 48 48 VAL CA C 59.229 0.3 1 155 48 48 VAL CB C 34.013 0.3 1 156 48 48 VAL N N 115.479 0.25 1 157 49 49 VAL H H 8.856 0.02 1 158 49 49 VAL CA C 60.344 0.3 1 159 49 49 VAL CB C 34.928 0.3 1 160 49 49 VAL N N 121.707 0.25 1 161 50 50 LEU H H 9.270 0.02 1 162 50 50 LEU CA C 53.069 0.3 1 163 50 50 LEU CB C 45.547 0.3 1 164 50 50 LEU N N 128.849 0.25 1 165 51 51 ASP H H 8.850 0.02 1 166 51 51 ASP CA C 52.827 0.3 1 167 51 51 ASP CB C 46.590 0.3 1 168 51 51 ASP N N 127.630 0.25 1 169 52 52 PHE H H 8.636 0.02 1 170 52 52 PHE CA C 58.094 0.3 1 171 52 52 PHE CB C 40.617 0.3 1 172 52 52 PHE N N 124.012 0.25 1 173 53 53 TYR H H 9.171 0.02 1 174 53 53 TYR CA C 57.891 0.3 1 175 53 53 TYR CB C 41.892 0.3 1 176 53 53 TYR N N 126.565 0.25 1 177 54 54 ALA H H 5.147 0.02 1 178 54 54 ALA CA C 51.267 0.3 1 179 54 54 ALA CB C 21.494 0.3 1 180 54 54 ALA N N 121.409 0.25 1 181 55 55 ASP H H 8.653 0.02 1 182 55 55 ASP CA C 56.707 0.3 1 183 55 55 ASP CB C 41.285 0.3 1 184 55 55 ASP N N 120.002 0.25 1 185 56 56 TRP H H 6.068 0.02 1 186 56 56 TRP CA C 53.925 0.3 1 187 56 56 TRP CB C 28.092 0.3 1 188 56 56 TRP N N 109.859 0.25 1 189 57 57 CYS H H 6.910 0.02 1 190 57 57 CYS CA C 53.119 0.3 1 191 57 57 CYS CB C 42.978 0.3 1 192 57 57 CYS N N 121.431 0.25 1 193 58 58 ILE H H 8.628 0.02 1 194 58 58 ILE CA C 64.772 0.3 1 195 58 58 ILE CB C 37.083 0.3 1 196 58 58 ILE N N 133.948 0.25 1 197 59 59 SER H H 9.003 0.02 1 198 59 59 SER CA C 61.963 0.3 1 199 59 59 SER CB C 62.431 0.3 1 200 59 59 SER N N 117.201 0.25 1 201 60 60 CYS H H 8.354 0.02 1 202 60 60 CYS CA C 62.613 0.3 1 203 60 60 CYS CB C 33.549 0.3 1 204 60 60 CYS N N 118.104 0.25 1 205 61 61 LYS H H 7.704 0.02 1 206 61 61 LYS CA C 59.848 0.3 1 207 61 61 LYS CB C 31.657 0.3 1 208 61 61 LYS N N 122.573 0.25 1 209 62 62 GLU H H 8.120 0.02 1 210 62 62 GLU CA C 59.590 0.3 1 211 62 62 GLU CB C 29.281 0.3 1 212 62 62 GLU N N 121.639 0.25 1 213 63 63 MET H H 8.780 0.02 1 214 63 63 MET CA C 58.101 0.3 1 215 63 63 MET CB C 33.177 0.3 1 216 63 63 MET N N 119.278 0.25 1 217 64 64 ALA H H 7.733 0.02 1 218 64 64 ALA CA C 55.216 0.3 1 219 64 64 ALA CB C 18.355 0.3 1 220 64 64 ALA N N 123.069 0.25 1 221 65 65 ALA H H 7.421 0.02 1 222 65 65 ALA CA C 53.301 0.3 1 223 65 65 ALA CB C 19.296 0.3 1 224 65 65 ALA N N 116.619 0.25 1 225 66 66 TYR H H 8.133 0.02 1 226 66 66 TYR CA C 57.551 0.3 1 227 66 66 TYR CB C 40.487 0.3 1 228 66 66 TYR N N 112.298 0.25 1 229 67 67 THR H H 7.890 0.02 1 230 67 67 THR CA C 65.797 0.3 1 231 67 67 THR CB C 70.481 0.3 1 232 67 67 THR N N 116.598 0.25 1 233 68 68 LEU H H 8.555 0.02 1 234 68 68 LEU CA C 56.274 0.3 1 235 68 68 LEU CB C 41.296 0.3 1 236 68 68 LEU N N 118.339 0.25 1 237 69 69 ASN H H 8.266 0.02 1 238 69 69 ASN CA C 52.043 0.3 1 239 69 69 ASN CB C 37.526 0.3 1 240 69 69 ASN N N 112.185 0.25 1 241 70 70 GLN H H 7.298 0.02 1 242 70 70 GLN CA C 53.009 0.3 1 243 70 70 GLN CB C 27.320 0.3 1 244 70 70 GLN N N 120.370 0.25 1 245 71 71 PRO CA C 65.442 0.3 1 246 71 71 PRO CB C 31.574 0.3 1 247 72 72 GLU H H 10.452 0.02 1 248 72 72 GLU CA C 59.695 0.3 1 249 72 72 GLU CB C 27.685 0.3 1 250 72 72 GLU N N 118.392 0.25 1 251 73 73 VAL H H 7.275 0.02 1 252 73 73 VAL CA C 66.597 0.3 1 253 73 73 VAL CB C 31.079 0.3 1 254 73 73 VAL N N 121.666 0.25 1 255 74 74 HIS H H 7.207 0.02 1 256 74 74 HIS CA C 58.172 0.3 1 257 74 74 HIS CB C 29.985 0.3 1 258 74 74 HIS N N 118.028 0.25 1 259 75 75 GLN H H 7.686 0.02 1 260 75 75 GLN CA C 57.342 0.3 1 261 75 75 GLN CB C 28.883 0.3 1 262 75 75 GLN N N 115.334 0.25 1 263 76 76 ALA H H 7.201 0.02 1 264 76 76 ALA CA C 53.551 0.3 1 265 76 76 ALA CB C 21.458 0.3 1 266 76 76 ALA N N 120.864 0.25 1 267 77 77 VAL H H 8.305 0.02 1 268 77 77 VAL CA C 61.312 0.3 1 269 77 77 VAL CB C 32.730 0.3 1 270 77 77 VAL N N 120.163 0.25 1 271 78 78 ASP H H 7.238 0.02 1 272 78 78 ASP CA C 53.276 0.3 1 273 78 78 ASP CB C 39.602 0.3 1 274 78 78 ASP N N 120.339 0.25 1 275 79 79 MET H H 9.213 0.02 1 276 79 79 MET CA C 55.458 0.3 1 277 79 79 MET CB C 29.124 0.3 1 278 79 79 MET N N 128.923 0.25 1 279 80 80 GLU H H 8.427 0.02 1 280 80 80 GLU CA C 57.884 0.3 1 281 80 80 GLU CB C 28.896 0.3 1 282 80 80 GLU N N 119.930 0.25 1 283 81 81 ARG H H 7.631 0.02 1 284 81 81 ARG CA C 54.618 0.3 1 285 81 81 ARG CB C 30.641 0.3 1 286 81 81 ARG N N 118.973 0.25 1 287 82 82 PHE H H 6.798 0.02 1 288 82 82 PHE CA C 56.553 0.3 1 289 82 82 PHE CB C 41.683 0.3 1 290 82 82 PHE N N 124.756 0.25 1 291 83 83 PHE H H 9.258 0.02 1 292 83 83 PHE CA C 56.640 0.3 1 293 83 83 PHE CB C 41.501 0.3 1 294 83 83 PHE N N 128.206 0.25 1 295 84 84 GLN H H 8.977 0.02 1 296 84 84 GLN CA C 53.706 0.3 1 297 84 84 GLN CB C 34.019 0.3 1 298 84 84 GLN N N 120.687 0.25 1 299 85 85 ILE H H 8.535 0.02 1 300 85 85 ILE CA C 54.037 0.3 1 301 85 85 ILE CB C 41.448 0.3 1 302 85 85 ILE N N 122.054 0.25 1 303 86 86 ASP H H 9.035 0.02 1 304 86 86 ASP CA C 52.299 0.3 1 305 86 86 ASP CB C 40.384 0.3 1 306 86 86 ASP N N 127.317 0.25 1 307 87 87 VAL H H 8.934 0.02 1 308 87 87 VAL CA C 59.252 0.3 1 309 87 87 VAL CB C 30.190 0.3 1 310 87 87 VAL N N 116.556 0.25 1 311 88 88 THR H H 8.656 0.02 1 312 88 88 THR CA C 67.912 0.3 1 313 88 88 THR CB C 68.724 0.3 1 314 88 88 THR N N 122.914 0.25 1 315 89 89 ALA H H 9.015 0.02 1 316 89 89 ALA CA C 54.002 0.3 1 317 89 89 ALA CB C 19.324 0.3 1 318 89 89 ALA N N 120.214 0.25 1 319 90 90 ASN H H 8.449 0.02 1 320 90 90 ASN CA C 54.021 0.3 1 321 90 90 ASN CB C 37.615 0.3 1 322 90 90 ASN N N 117.329 0.25 1 323 91 91 LYS H H 9.945 0.02 1 324 91 91 LYS CA C 56.013 0.3 1 325 91 91 LYS CB C 30.857 0.3 1 326 91 91 LYS N N 120.309 0.25 1 327 92 92 PRO CA C 66.695 0.3 1 328 92 92 PRO CB C 31.248 0.3 1 329 93 93 GLU H H 9.253 0.02 1 330 93 93 GLU CA C 59.005 0.3 1 331 93 93 GLU CB C 27.891 0.3 1 332 93 93 GLU N N 115.651 0.25 1 333 94 94 HIS H H 7.466 0.02 1 334 94 94 HIS CA C 59.477 0.3 1 335 94 94 HIS CB C 31.563 0.3 1 336 94 94 HIS N N 123.436 0.25 1 337 95 95 GLN H H 7.998 0.02 1 338 95 95 GLN CA C 59.942 0.3 1 339 95 95 GLN CB C 31.843 0.3 1 340 95 95 GLN N N 118.634 0.25 1 341 96 96 ALA H H 7.685 0.02 1 342 96 96 ALA CA C 54.896 0.3 1 343 96 96 ALA CB C 17.780 0.3 1 344 96 96 ALA N N 120.363 0.25 1 345 97 97 LEU H H 7.554 0.02 1 346 97 97 LEU CA C 58.002 0.3 1 347 97 97 LEU CB C 42.695 0.3 1 348 97 97 LEU N N 122.266 0.25 1 349 98 98 LEU H H 8.399 0.02 1 350 98 98 LEU CA C 58.715 0.3 1 351 98 98 LEU CB C 40.952 0.3 1 352 98 98 LEU N N 119.477 0.25 1 353 99 99 LYS H H 7.812 0.02 1 354 99 99 LYS CA C 59.444 0.3 1 355 99 99 LYS CB C 32.153 0.3 1 356 99 99 LYS N N 118.266 0.25 1 357 100 100 GLU H H 8.239 0.02 1 358 100 100 GLU CA C 59.235 0.3 1 359 100 100 GLU CB C 28.900 0.3 1 360 100 100 GLU N N 123.285 0.25 1 361 101 101 TYR H H 7.613 0.02 1 362 101 101 TYR CA C 59.595 0.3 1 363 101 101 TYR CB C 37.527 0.3 1 364 101 101 TYR N N 117.803 0.25 1 365 102 102 GLY H H 7.845 0.02 1 366 102 102 GLY CA C 46.380 0.3 1 367 102 102 GLY N N 108.826 0.25 1 368 103 103 LEU H H 8.041 0.02 1 369 103 103 LEU CA C 52.837 0.3 1 370 103 103 LEU CB C 45.055 0.3 1 371 103 103 LEU N N 119.852 0.25 1 372 104 104 PHE H H 8.839 0.02 1 373 104 104 PHE CA C 58.496 0.3 1 374 104 104 PHE CB C 39.137 0.3 1 375 104 104 PHE N N 119.970 0.25 1 376 105 105 GLY H H 7.440 0.02 1 377 105 105 GLY CA C 45.172 0.3 1 378 105 105 GLY N N 106.228 0.25 1 379 107 107 PRO CA C 62.070 0.3 1 380 107 107 PRO CB C 37.012 0.3 1 381 108 108 GLY H H 9.248 0.02 1 382 108 108 GLY CA C 48.203 0.3 1 383 108 108 GLY N N 105.714 0.25 1 384 109 109 VAL H H 7.643 0.02 1 385 109 109 VAL CA C 60.318 0.3 1 386 109 109 VAL CB C 33.099 0.3 1 387 109 109 VAL N N 127.047 0.25 1 388 110 110 PHE H H 9.647 0.02 1 389 110 110 PHE CA C 57.235 0.3 1 390 110 110 PHE CB C 43.971 0.3 1 391 110 110 PHE N N 121.481 0.25 1 392 111 111 VAL H H 8.673 0.02 1 393 111 111 VAL CA C 63.306 0.3 1 394 111 111 VAL CB C 32.534 0.3 1 395 111 111 VAL N N 123.343 0.25 1 396 112 112 VAL H H 9.343 0.02 1 397 112 112 VAL CA C 62.572 0.3 1 398 112 112 VAL CB C 34.115 0.3 1 399 112 112 VAL N N 129.584 0.25 1 400 113 113 ARG H H 8.435 0.02 1 401 113 113 ARG CA C 54.726 0.3 1 402 113 113 ARG CB C 31.983 0.3 1 403 113 113 ARG N N 122.994 0.25 1 404 114 114 SER H H 9.534 0.02 1 405 114 114 SER CA C 60.540 0.3 1 406 114 114 SER CB C 62.382 0.3 1 407 114 114 SER N N 117.398 0.25 1 408 115 115 ASP H H 7.804 0.02 1 409 115 115 ASP CA C 53.225 0.3 1 410 115 115 ASP CB C 39.612 0.3 1 411 115 115 ASP N N 120.353 0.25 1 412 116 116 GLY H H 8.058 0.02 1 413 116 116 GLY CA C 44.997 0.3 1 414 116 116 GLY N N 109.146 0.25 1 415 117 117 SER H H 8.267 0.02 1 416 117 117 SER CA C 58.463 0.3 1 417 117 117 SER CB C 64.761 0.3 1 418 117 117 SER N N 118.697 0.25 1 419 118 118 ARG H H 8.366 0.02 1 420 118 118 ARG CA C 53.910 0.3 1 421 118 118 ARG CB C 34.371 0.3 1 422 118 118 ARG N N 115.488 0.25 1 423 119 119 SER H H 9.267 0.02 1 424 119 119 SER CA C 58.359 0.3 1 425 119 119 SER CB C 66.727 0.3 1 426 119 119 SER N N 117.718 0.25 1 427 120 120 GLU H H 8.617 0.02 1 428 120 120 GLU CA C 55.791 0.3 1 429 120 120 GLU CB C 28.664 0.3 1 430 120 120 GLU N N 119.448 0.25 1 431 121 121 PRO CA C 62.218 0.3 1 432 121 121 PRO CB C 30.291 0.3 1 433 122 122 LEU H H 8.460 0.02 1 434 122 122 LEU CA C 54.554 0.3 1 435 122 122 LEU CB C 41.188 0.3 1 436 122 122 LEU N N 122.587 0.25 1 437 123 123 LEU H H 8.407 0.02 1 438 123 123 LEU CA C 53.941 0.3 1 439 123 123 LEU CB C 43.124 0.3 1 440 123 123 LEU N N 127.088 0.25 1 441 124 124 GLY H H 6.988 0.02 1 442 124 124 GLY CA C 44.635 0.3 1 443 124 124 GLY N N 106.494 0.25 1 444 125 125 PHE H H 8.547 0.02 1 445 125 125 PHE CA C 58.237 0.3 1 446 125 125 PHE CB C 39.992 0.3 1 447 125 125 PHE N N 118.968 0.25 1 448 126 126 VAL H H 7.084 0.02 1 449 126 126 VAL CA C 58.726 0.3 1 450 126 126 VAL CB C 35.575 0.3 1 451 126 126 VAL N N 123.650 0.25 1 452 127 127 LYS H H 8.042 0.02 1 453 127 127 LYS CA C 55.849 0.3 1 454 127 127 LYS CB C 33.548 0.3 1 455 127 127 LYS N N 119.136 0.25 1 456 128 128 ALA H H 9.042 0.02 1 457 128 128 ALA CA C 56.531 0.3 1 458 128 128 ALA CB C 19.203 0.3 1 459 128 128 ALA N N 122.097 0.25 1 460 129 129 ASP H H 8.667 0.02 1 461 129 129 ASP CA C 56.824 0.3 1 462 129 129 ASP CB C 38.307 0.3 1 463 129 129 ASP N N 114.873 0.25 1 464 130 130 LYS H H 7.530 0.02 1 465 130 130 LYS CA C 56.643 0.3 1 466 130 130 LYS CB C 31.592 0.3 1 467 130 130 LYS N N 122.893 0.25 1 468 131 131 PHE H H 8.814 0.02 1 469 131 131 PHE CA C 62.266 0.3 1 470 131 131 PHE CB C 39.398 0.3 1 471 131 131 PHE N N 124.539 0.25 1 472 132 132 ILE H H 8.415 0.02 1 473 132 132 ILE CA C 66.236 0.3 1 474 132 132 ILE CB C 38.514 0.3 1 475 132 132 ILE N N 119.274 0.25 1 476 133 133 GLU H H 7.669 0.02 1 477 133 133 GLU CA C 59.803 0.3 1 478 133 133 GLU CB C 30.458 0.3 1 479 133 133 GLU N N 119.116 0.25 1 480 134 134 TRP H H 8.183 0.02 1 481 134 134 TRP CA C 61.830 0.3 1 482 134 134 TRP CB C 27.505 0.3 1 483 134 134 TRP N N 120.930 0.25 1 484 135 135 TYR H H 8.595 0.02 1 485 135 135 TYR CA C 62.022 0.3 1 486 135 135 TYR CB C 37.978 0.3 1 487 135 135 TYR N N 122.781 0.25 1 488 136 136 GLU H H 8.724 0.02 1 489 136 136 GLU CA C 59.312 0.3 1 490 136 136 GLU CB C 29.078 0.3 1 491 136 136 GLU N N 117.145 0.25 1 492 137 137 GLN H H 7.893 0.02 1 493 137 137 GLN CA C 57.265 0.3 1 494 137 137 GLN CB C 28.632 0.3 1 495 137 137 GLN N N 116.119 0.25 1 496 138 138 ASN H H 7.204 0.02 1 497 138 138 ASN CA C 54.216 0.3 1 498 138 138 ASN CB C 40.523 0.3 1 499 138 138 ASN N N 116.385 0.25 1 500 139 139 ARG H H 7.178 0.02 1 501 139 139 ARG CA C 58.963 0.3 1 502 139 139 ARG CB C 29.241 0.3 1 503 139 139 ARG N N 125.576 0.25 1 stop_ save_