data_19979 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of B24G insulin ; _BMRB_accession_number 19979 _BMRB_flat_file_name bmr19979.str _Entry_type original _Submission_date 2014-05-19 _Accession_date 2014-05-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solution structure of B24G insulin' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yang Yanwu . . 2 Wickramasinghe Nalinda P. . 3 Hua Qingxin . . 4 Weiss Michael A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 215 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-12-22 original author . stop_ _Original_release_date 2014-12-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protective hinge in insulin opens to enable its receptor engagement' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25092300 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Menting John G. . 2 Yang Yanwu . . 3 Chan Shu Jin . 4 Phillips Nelson B. . 5 Smith Brian J. . 6 Whittaker Jonathan . . 7 Wickramasinghe Nalinda P. . 8 Whittaker Linda J. . 9 Pandyarajan Vijay . . 10 Wan Zhu-li . . 11 Yadav Satya P. . 12 Carroll Julie M. . 13 Strokes Natalie . . 14 Roberts Charles T. Jr. 15 Ismail-Beigi Faramarz . . 16 Milewski Wieslawa . . 17 Steiner Donald F. . 18 Chauhan Virander S. . 19 Ward Colin W. . 20 Weiss Michael A. . 21 Lawrence Michael C. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 111 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first E3395 _Page_last E3404 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'B24G insulin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'B24G insulin' $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 5686.482 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 51 _Mol_residue_sequence ; GIVEQCCTSICSLYQLENYC NFVNQHLCGSDLVEALYLVC GERGGFYTKPT ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 VAL 4 GLU 5 GLN 6 CYS 7 CYS 8 THR 9 SER 10 ILE 11 CYS 12 SER 13 LEU 14 TYR 15 GLN 16 LEU 17 GLU 18 ASN 19 TYR 20 CYS 21 ASN 22 PHE 23 VAL 24 ASN 25 GLN 26 HIS 27 LEU 28 CYS 29 GLY 30 SER 31 ASP 32 LEU 33 VAL 34 GLU 35 ALA 36 LEU 37 TYR 38 LEU 39 VAL 40 CYS 41 GLY 42 GLU 43 ARG 44 GLY 45 GLY 46 PHE 47 TYR 48 THR 49 LYS 50 PRO 51 THR 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 $entity Human 9606 Eukaryota Metazoa Homo sapiens 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 $entity 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '32 degree, PH 8.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.3 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.3 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_InsightII _Saveframe_category software _Name InsightII _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Vendor _Address _Electronic_address Brunger . . stop_ loop_ _Task refinement stop_ _Details . save_ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 273 . K pH 8 . pH pressure 1 . atm 'ionic strength' 0.5 . mM 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 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1.0 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_ _Software_label $X-PLOR stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 'B24G insulin' _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 ILE HA H 3.90 . . 2 2 2 ILE HB H 1.34 . . 3 2 2 ILE HG12 H 1.21 . . 4 2 2 ILE HG13 H 0.99 . . 5 2 2 ILE HG2 H 0.78 . . 6 2 2 ILE HD1 H 0.69 . . 7 3 3 VAL H H 8.12 . . 8 3 3 VAL HA H 3.68 . . 9 3 3 VAL HB H 1.98 . . 10 3 3 VAL HG1 H 0.83 . . 11 3 3 VAL HG2 H 0.93 . . 12 4 4 GLU HA H 4.16 . . 13 4 4 GLU HB2 H 2.13 . . 14 4 4 GLU HG2 H 2.44 . . 15 4 4 GLU HG3 H 2.26 . . 16 5 5 GLN HA H 4.12 . . 17 5 5 GLN HB2 H 2.13 . . 18 5 5 GLN HB3 H 2.13 . . 19 5 5 GLN HG2 H 2.48 . . 20 6 6 CYS HA H 5.07 . . 21 6 6 CYS HB2 H 3.41 . . 22 6 6 CYS HB3 H 2.90 . . 23 7 7 CYS HA H 4.89 . . 24 7 7 CYS HB2 H 3.30 . . 25 7 7 CYS HB3 H 3.78 . . 26 8 8 THR HA H 4.15 . . 27 8 8 THR HB H 4.42 . . 28 8 8 THR HG2 H 1.26 . . 29 9 9 SER HA H 4.69 . . 30 9 9 SER HB2 H 3.85 . . 31 9 9 SER HB3 H 3.97 . . 32 10 10 ILE HA H 4.27 . . 33 10 10 ILE HB H 1.61 . . 34 10 10 ILE HG12 H 1.61 . . 35 10 10 ILE HG13 H 1.13 . . 36 10 10 ILE HG2 H 0.71 . . 37 10 10 ILE HD1 H 0.55 . . 38 11 11 CYS HA H 4.88 . . 39 11 11 CYS HB2 H 3.32 . . 40 11 11 CYS HB3 H 2.76 . . 41 12 12 SER HA H 4.62 . . 42 12 12 SER HB2 H 4.00 . . 43 12 12 SER HB3 H 4.13 . . 44 13 13 LEU HA H 3.94 . . 45 13 13 LEU HB2 H 1.50 . . 46 13 13 LEU HG H 1.58 . . 47 13 13 LEU HD1 H 0.89 . . 48 13 13 LEU HD2 H 0.81 . . 49 14 14 TYR H H 7.64 . . 50 14 14 TYR HA H 4.38 . . 51 14 14 TYR HB2 H 3.02 . . 52 14 14 TYR HD1 H 7.14 . . 53 14 14 TYR HE1 H 6.90 . . 54 15 15 GLN H H 7.53 . . 55 15 15 GLN HA H 4.01 . . 56 15 15 GLN HB2 H 2.32 . . 57 15 15 GLN HB3 H 2.21 . . 58 15 15 GLN HG2 H 2.40 . . 59 16 16 LEU H H 7.91 . . 60 17 17 GLU H H 8.11 . . 61 17 17 GLU HA H 4.11 . . 62 17 17 GLU HB2 H 1.98 . . 63 17 17 GLU HB3 H 2.07 . . 64 17 17 GLU HG2 H 2.19 . . 65 17 17 GLU HG3 H 2.39 . . 66 18 18 ASN H H 7.44 . . 67 18 18 ASN HA H 4.50 . . 68 18 18 ASN HB2 H 2.57 . . 69 19 19 TYR H H 7.97 . . 70 19 19 TYR HA H 4.55 . . 71 19 19 TYR HB2 H 3.36 . . 72 19 19 TYR HB3 H 3.00 . . 73 19 19 TYR HD1 H 7.29 . . 74 19 19 TYR HE1 H 6.82 . . 75 20 20 CYS H H 7.50 . . 76 20 20 CYS HA H 4.85 . . 77 20 20 CYS HB2 H 3.22 . . 78 20 20 CYS HB3 H 2.90 . . 79 21 21 ASN H H 8.04 . . 80 21 21 ASN HA H 4.51 . . 81 21 21 ASN HB2 H 2.79 . . 82 21 21 ASN HB3 H 2.63 . . 83 22 22 PHE HA H 3.89 . . 84 22 22 PHE HB2 H 3.07 . . 85 22 22 PHE HB3 H 3.07 . . 86 23 23 VAL HA H 4.19 . . 87 23 23 VAL HB H 2.00 . . 88 23 23 VAL HG1 H 0.85 . . 89 24 24 ASN HA H 4.59 . . 90 24 24 ASN HB2 H 2.79 . . 91 24 24 ASN HB3 H 2.88 . . 92 25 25 GLN HA H 4.50 . . 93 25 25 GLN HB2 H 2.00 . . 94 25 25 GLN HB3 H 1.98 . . 95 25 25 GLN HG2 H 2.21 . . 96 25 25 GLN HG3 H 2.25 . . 97 26 26 HIS HA H 4.42 . . 98 26 26 HIS HB2 H 3.43 . . 99 26 26 HIS HB3 H 3.11 . . 100 26 26 HIS HD2 H 6.92 . . 101 26 26 HIS HE1 H 7.78 . . 102 27 27 LEU H H 8.83 . . 103 27 27 LEU HA H 4.59 . . 104 27 27 LEU HB2 H 1.78 . . 105 27 27 LEU HB3 H 1.66 . . 106 27 27 LEU HG H 1.64 . . 107 27 27 LEU HD1 H 0.91 . . 108 27 27 LEU HD2 H 0.81 . . 109 28 28 CYS H H 8.72 . . 110 28 28 CYS HA H 4.95 . . 111 28 28 CYS HB2 H 3.24 . . 112 28 28 CYS HB3 H 2.01 . . 113 30 30 SER HA H 4.18 . . 114 30 30 SER HB2 H 3.98 . . 115 30 30 SER HB3 H 4.07 . . 116 31 31 ASP H H 8.07 . . 117 31 31 ASP HA H 4.46 . . 118 31 31 ASP HB2 H 2.98 . . 119 31 31 ASP HB3 H 2.69 . . 120 32 32 LEU HA H 4.02 . . 121 32 32 LEU HB2 H 1.86 . . 122 32 32 LEU HB3 H 1.30 . . 123 32 32 LEU HG H 1.45 . . 124 32 32 LEU HD2 H 0.79 . . 125 33 33 VAL H H 7.14 . . 126 33 33 VAL HA H 3.42 . . 127 33 33 VAL HB H 2.15 . . 128 33 33 VAL HG1 H 0.97 . . 129 33 33 VAL HG2 H 0.92 . . 130 34 34 GLU H H 7.99 . . 131 34 34 GLU HA H 4.09 . . 132 34 34 GLU HB2 H 2.12 . . 133 34 34 GLU HB3 H 2.12 . . 134 34 34 GLU HG2 H 2.46 . . 135 34 34 GLU HG3 H 2.33 . . 136 35 35 ALA H H 7.75 . . 137 35 35 ALA HA H 4.13 . . 138 35 35 ALA HB H 1.44 . . 139 36 36 LEU H H 8.04 . . 140 36 36 LEU HA H 3.99 . . 141 36 36 LEU HB2 H 1.68 . . 142 36 36 LEU HB3 H 1.28 . . 143 36 36 LEU HG H 1.65 . . 144 36 36 LEU HD1 H 0.77 . . 145 36 36 LEU HD2 H 0.68 . . 146 37 37 TYR H H 8.04 . . 147 37 37 TYR HA H 4.31 . . 148 37 37 TYR HB2 H 3.16 . . 149 37 37 TYR HB3 H 3.16 . . 150 37 37 TYR HD2 H 7.16 . . 151 37 37 TYR HE2 H 6.82 . . 152 38 38 LEU H H 7.72 . . 153 38 38 LEU HA H 4.11 . . 154 38 38 LEU HB2 H 1.97 . . 155 38 38 LEU HB3 H 1.78 . . 156 38 38 LEU HG H 1.82 . . 157 38 38 LEU HD1 H 0.95 . . 158 39 39 VAL H H 8.27 . . 159 39 39 VAL HA H 3.87 . . 160 39 39 VAL HB H 2.07 . . 161 39 39 VAL HG1 H 0.92 . . 162 39 39 VAL HG2 H 1.03 . . 163 40 40 CYS H H 8.74 . . 164 40 40 CYS HA H 4.77 . . 165 40 40 CYS HB2 H 3.20 . . 166 40 40 CYS HB3 H 2.89 . . 167 41 41 GLY H H 7.84 . . 168 41 41 GLY HA2 H 4.01 . . 169 41 41 GLY HA3 H 3.86 . . 170 42 42 GLU HA H 4.22 . . 171 42 42 GLU HB2 H 2.05 . . 172 42 42 GLU HB3 H 2.15 . . 173 42 42 GLU HG2 H 2.34 . . 174 42 42 GLU HG3 H 2.30 . . 175 43 43 ARG H H 8.09 . . 176 43 43 ARG HA H 4.34 . . 177 43 43 ARG HB2 H 2.02 . . 178 43 43 ARG HB3 H 1.91 . . 179 43 43 ARG HG2 H 1.77 . . 180 43 43 ARG HG3 H 1.72 . . 181 43 43 ARG HD2 H 3.25 . . 182 46 46 PHE H H 8.52 . . 183 46 46 PHE HA H 4.63 . . 184 46 46 PHE HB2 H 3.03 . . 185 46 46 PHE HB3 H 3.03 . . 186 46 46 PHE HD2 H 7.15 . . 187 46 46 PHE HE2 H 7.31 . . 188 47 47 TYR HA H 4.59 . . 189 47 47 TYR HB2 H 2.95 . . 190 47 47 TYR HB3 H 2.84 . . 191 47 47 TYR HD1 H 7.00 . . 192 47 47 TYR HE1 H 6.79 . . 193 48 48 THR HA H 4.29 . . 194 48 48 THR HB H 4.10 . . 195 48 48 THR HG2 H 1.15 . . 196 49 49 LYS HA H 4.49 . . 197 49 49 LYS HB2 H 1.82 . . 198 49 49 LYS HB3 H 1.73 . . 199 49 49 LYS HG2 H 1.46 . . 200 49 49 LYS HG3 H 1.46 . . 201 49 49 LYS HD2 H 1.70 . . 202 49 49 LYS HD3 H 1.70 . . 203 49 49 LYS HE2 H 2.99 . . 204 49 49 LYS HE3 H 2.99 . . 205 50 50 PRO HA H 4.49 . . 206 50 50 PRO HB2 H 2.39 . . 207 50 50 PRO HB3 H 2.07 . . 208 50 50 PRO HG2 H 2.00 . . 209 50 50 PRO HG3 H 2.00 . . 210 50 50 PRO HD2 H 3.68 . . 211 50 50 PRO HD3 H 3.84 . . 212 51 51 THR H H 7.74 . . 213 51 51 THR HA H 4.14 . . 214 51 51 THR HB H 4.23 . . 215 51 51 THR HG2 H 1.20 . . stop_ save_