data_2282 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation ; _BMRB_accession_number 2282 _BMRB_flat_file_name bmr2282.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _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 Arseniev Alexander S. . 2 Maslennikov Innokenti V. . 3 Bystrov Vladimir F. . 4 Kozhich Alexander T. . 5 Ivanov Vadim T. . 6 Ovchinnikov Yuri A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 169 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete naturals source information' 2008-10-01 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Arseniev, Alexander S., Maslennikov, Innokenti V., Bystrov, Vladimir F., Kozhich, Alexander T., Ivanov, Vadim T., Ovchinnikov, Yuri A., "Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation," FEBS Lett. 231 (1), 81-88 (1988). ; _Citation_title 'Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arseniev Alexander S. . 2 Maslennikov Innokenti V. . 3 Bystrov Vladimir F. . 4 Kozhich Alexander T. . 5 Ivanov Vadim T. . 6 Ovchinnikov Yuri A. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 231 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 81 _Page_last 88 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_bacteriorhodopsin _Saveframe_category molecular_system _Mol_system_name bacteriorhodopsin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label bacteriorhodopsin $bacteriorhodopsin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bacteriorhodopsin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common bacteriorhodopsin _Name_variant 'residues 34-65 (membrane-spanning segment B)' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; VSDPDAKKFYAITTLVPAIA FTXYLSXLLGYG ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 SER 3 ASP 4 PRO 5 ASP 6 ALA 7 LYS 8 LYS 9 PHE 10 TYR 11 ALA 12 ILE 13 THR 14 THR 15 LEU 16 VAL 17 PRO 18 ALA 19 ILE 20 ALA 21 PHE 22 THR 23 NLE 24 TYR 25 LEU 26 SER 27 NLE 28 LEU 29 LEU 30 GLY 31 TYR 32 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 1999-12-06 save_ ###################### # Polymer residues # ###################### save_chem_comp_NLE _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common NORLEUCINE _BMRB_code NLE _PDB_code NLE _Standard_residue_derivative . _Molecular_mass 131.173 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 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 N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $bacteriorhodopsin . 2242 Bacteria . Halobacterium halobium R1M1 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 $bacteriorhodopsin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH . . n/a temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TMS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name bacteriorhodopsin _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 . 1 VAL HA H 3.37 0.01 1 2 . 1 VAL HB H 1.84 0.01 1 3 . 1 VAL HG1 H .72 0.01 1 4 . 1 VAL HG2 H .72 0.01 1 5 . 2 SER H H 8.28 0.01 1 6 . 2 SER HA H 4.14 0.01 1 7 . 2 SER HB2 H 3.47 0.01 1 8 . 2 SER HB3 H 3.47 0.01 1 9 . 3 ASP H H 8.35 0.01 1 10 . 3 ASP HA H 4.56 0.01 1 11 . 3 ASP HB2 H 2.63 0.01 2 12 . 3 ASP HB3 H 2.47 0.01 2 13 . 4 PRO HA H 3.87 0.01 1 14 . 4 PRO HB2 H 1.6 0.01 2 15 . 4 PRO HB3 H 1.98 0.01 2 16 . 4 PRO HG2 H 1.66 0.01 2 17 . 4 PRO HG3 H 1.76 0.01 2 18 . 4 PRO HD2 H 3.51 0.01 2 19 . 4 PRO HD3 H 3.56 0.01 2 20 . 5 ASP H H 7.74 0.01 1 21 . 5 ASP HA H 4.08 0.01 1 22 . 5 ASP HB2 H 2.59 0.01 2 23 . 5 ASP HB3 H 2.37 0.01 2 24 . 6 ALA H H 7.53 0.01 1 25 . 6 ALA HA H 3.77 0.01 1 26 . 6 ALA HB H 1.2 0.01 1 27 . 7 LYS H H 7.52 0.01 1 28 . 7 LYS HA H 3.69 0.01 1 29 . 7 LYS HB2 H 1.58 0.01 2 30 . 7 LYS HB3 H 1.64 0.01 2 31 . 7 LYS HG2 H 1.13 0.01 1 32 . 7 LYS HG3 H 1.13 0.01 1 33 . 7 LYS HD2 H 1.33 0.01 2 34 . 7 LYS HD3 H 2.58 0.01 2 35 . 8 LYS H H 7.73 0.01 1 36 . 8 LYS HA H 3.65 0.01 1 37 . 8 LYS HB2 H 1.62 0.01 1 38 . 8 LYS HB3 H 1.62 0.01 1 39 . 8 LYS HG2 H 1.13 0.01 1 40 . 8 LYS HG3 H 1.13 0.01 1 41 . 8 LYS HD2 H 1.35 0.01 2 42 . 8 LYS HD3 H 2.53 0.01 2 43 . 9 PHE H H 7.87 0.01 1 44 . 9 PHE HA H 3.79 0.01 1 45 . 9 PHE HB2 H 2.87 0.01 1 46 . 9 PHE HB3 H 2.87 0.01 1 47 . 9 PHE HD1 H 6.71 0.01 1 48 . 9 PHE HD2 H 6.71 0.01 1 49 . 9 PHE HE1 H 6.39 0.01 1 50 . 9 PHE HE2 H 6.39 0.01 1 51 . 9 PHE HZ H 6.9 0.01 1 52 . 10 TYR H H 8.26 0.01 1 53 . 10 TYR HA H 3.72 0.01 1 54 . 10 TYR HB2 H 2.83 0.01 1 55 . 10 TYR HB3 H 2.83 0.01 1 56 . 10 TYR HD1 H 6.74 0.01 1 57 . 10 TYR HD2 H 6.74 0.01 1 58 . 10 TYR HE1 H 6.39 0.01 1 59 . 10 TYR HE2 H 6.39 0.01 1 60 . 11 ALA H H 8.16 0.01 1 61 . 11 ALA HA H 3.65 0.01 1 62 . 11 ALA HB H 1.26 0.01 1 63 . 12 ILE H H 7.88 0.01 1 64 . 12 ILE HA H 3.38 0.01 1 65 . 12 ILE HB H 1.51 0.01 1 66 . 12 ILE HG12 H .91 0.01 2 67 . 12 ILE HG13 H 1.39 0.01 2 68 . 12 ILE HG2 H .57 0.01 1 69 . 12 ILE HD1 H .51 0.01 1 70 . 13 THR H H 7.37 0.01 1 71 . 13 THR HA H 3.53 0.01 1 72 . 13 THR HB H 3.68 0.01 1 73 . 13 THR HG2 H .57 0.01 1 74 . 14 THR H H 7.12 0.01 1 75 . 14 THR HA H 3.86 0.01 1 76 . 14 THR HB H 3.6 0.01 1 77 . 14 THR HG2 H .74 0.01 1 78 . 15 LEU H H 7.36 0.01 1 79 . 15 LEU HA H 3.86 0.01 1 80 . 15 LEU HB2 H 1.31 0.01 2 81 . 15 LEU HB3 H 1.49 0.01 2 82 . 15 LEU HG H 1.39 0.01 1 83 . 15 LEU HD1 H .57 0.01 2 84 . 15 LEU HD2 H .61 0.01 2 85 . 16 VAL H H 7.7 0.01 1 86 . 16 VAL HA H 3.41 0.01 1 87 . 16 VAL HB H 2.82 0.01 1 88 . 16 VAL HG1 H .62 0.01 2 89 . 16 VAL HG2 H .77 0.01 2 90 . 17 PRO HA H 3.87 0.01 1 91 . 17 PRO HB2 H 1.49 0.01 2 92 . 17 PRO HB3 H 1.89 0.01 2 93 . 17 PRO HG2 H 1.51 0.01 2 94 . 17 PRO HG3 H 1.85 0.01 2 95 . 17 PRO HD2 H 3.18 0.01 2 96 . 17 PRO HD3 H 3.24 0.01 2 97 . 18 ALA H H 7.01 0.01 1 98 . 18 ALA HA H 3.85 0.01 1 99 . 18 ALA HB H 1.25 0.01 1 100 . 19 ILE H H 8.17 0.01 1 101 . 19 ILE HA H 3.34 0.01 1 102 . 19 ILE HB H 1.7 0.01 1 103 . 19 ILE HG12 H .79 0.01 2 104 . 19 ILE HG13 H 1.52 0.01 2 105 . 19 ILE HG2 H .62 0.01 1 106 . 19 ILE HD1 H .52 0.01 1 107 . 20 ALA H H 8.2 0.01 1 108 . 20 ALA HA H 3.64 0.01 1 109 . 20 ALA HB H 1.17 0.01 1 110 . 21 PHE H H 8.39 0.01 1 111 . 21 PHE HA H 4 0.01 1 112 . 21 PHE HB2 H 2.86 0.01 2 113 . 21 PHE HB3 H 2.98 0.01 2 114 . 21 PHE HD1 H 6.9 0.01 1 115 . 21 PHE HD2 H 6.9 0.01 1 116 . 21 PHE HE1 H 6.9 0.01 1 117 . 21 PHE HE2 H 6.9 0.01 1 118 . 21 PHE HZ H 6.9 0.01 1 119 . 22 THR H H 7.75 0.01 1 120 . 22 THR HA H 3.44 0.01 1 121 . 22 THR HB H 4.07 0.01 1 122 . 22 THR HG2 H .97 0.01 1 123 . 24 TYR H H 7.93 0.01 1 124 . 24 TYR HA H 3.76 0.01 1 125 . 24 TYR HB2 H 2.8 0.01 1 126 . 24 TYR HB3 H 2.8 0.01 1 127 . 24 TYR HD1 H 6.59 0.01 1 128 . 24 TYR HD2 H 6.59 0.01 1 129 . 24 TYR HE1 H 6.32 0.01 1 130 . 24 TYR HE2 H 6.32 0.01 1 131 . 25 LEU H H 8.1 0.01 1 132 . 25 LEU HA H 3.4 0.01 1 133 . 25 LEU HB2 H 1.12 0.01 2 134 . 25 LEU HB3 H 1.21 0.01 2 135 . 25 LEU HG H 1.2 0.01 1 136 . 25 LEU HD1 H .44 0.01 2 137 . 25 LEU HD2 H .47 0.01 2 138 . 26 SER H H 7.71 0.01 1 139 . 26 SER HA H 3.7 0.01 1 140 . 26 SER HB2 H 3.57 0.01 1 141 . 26 SER HB3 H 3.57 0.01 1 142 . 28 LEU H H 7.7 0.01 1 143 . 28 LEU HA H 3.58 0.01 1 144 . 28 LEU HB2 H 1.25 0.01 2 145 . 28 LEU HB3 H 1.36 0.01 2 146 . 28 LEU HG H 1.15 0.01 1 147 . 28 LEU HD1 H .38 0.01 2 148 . 28 LEU HD2 H .42 0.01 2 149 . 29 LEU H H 7.69 0.01 1 150 . 29 LEU HA H 3.81 0.01 1 151 . 29 LEU HB2 H 1.44 0.01 1 152 . 29 LEU HB3 H 1.44 0.01 1 153 . 29 LEU HG H .51 0.01 1 154 . 29 LEU HD1 H .96 0.01 1 155 . 29 LEU HD2 H .96 0.01 1 156 . 30 GLY H H 7.49 0.01 1 157 . 30 GLY HA2 H 3.42 0.01 1 158 . 30 GLY HA3 H 3.42 0.01 1 159 . 31 TYR H H 7.78 0.01 1 160 . 31 TYR HA H 4.18 0.01 1 161 . 31 TYR HB2 H 2.55 0.01 2 162 . 31 TYR HB3 H 2.81 0.01 2 163 . 31 TYR HD1 H 6.76 0.01 1 164 . 31 TYR HD2 H 6.76 0.01 1 165 . 31 TYR HE1 H 6.32 0.01 1 166 . 31 TYR HE2 H 6.32 0.01 1 167 . 32 GLY H H 7.57 0.01 1 168 . 32 GLY HA2 H 3.56 0.01 1 169 . 32 GLY HA3 H 3.56 0.01 1 stop_ save_