data_4477 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate ; _BMRB_accession_number 4477 _BMRB_flat_file_name bmr4477.str _Entry_type original _Submission_date 1998-12-22 _Accession_date 1999-12-06 _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 Antz C. . . 2 Bauer T. . . 3 Kalbacher H. . . 4 Frank R. . . 5 Covarrubias M. . . 6 Kalbitzer H. R. . 7 Ruppersberg J. P. . 8 Baukrowitz T. . . 9 Fakler B. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 189 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-11 update BMRB 'Updating non-standard residue' 2008-03-24 update BMRB . 2002-06-07 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4476 'SER 8 phosphorylated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of inactivation gates from mammalian voltage-dependent potassium channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9000078 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Antz C. . . 2 Geyer M. . . 3 Fakler B. . . 4 Schott M. K. . 5 Guy H. R. . 6 Frank R. . . 7 Ruppersberg J. P. . 8 Kalbitzer H. R. . stop_ _Journal_abbreviation Nature _Journal_volume 385 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 272 _Page_last 275 _Year 1997 _Details . loop_ _Keyword 'potassium channel' 'inactivation gate' phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_system_potassium_channel _Saveframe_category molecular_system _Mol_system_name 'Potassium channel' _Abbreviation_common 'Potassium channel' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Potassium channel' $Potassium_channel stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Potassium_channel _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Potassium channel' _Name_variant S8S(phosphor.) _Abbreviation_common 'Potassium channel' _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 30 _Mol_residue_sequence ; MISSVCVSSYRGRKXGNKPP XKTCLKEEMA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 SER 4 SER 5 VAL 6 CYS 7 VAL 8 SER 9 SER 10 TYR 11 ARG 12 GLY 13 ARG 14 LYS 15 SEP 16 GLY 17 ASN 18 LYS 19 PRO 20 PRO 21 SEP 22 LYS 23 THR 24 CYS 25 LEU 26 LYS 27 GLU 28 GLU 29 MET 30 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2013-11-03 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 PDB 1B4I "Control Of K+ Channel Gating By Protein Phosphorylation: Str Switches Of The Inactivation Gate, Nmr, 22 Structures" 100.00 30 100.00 100.00 2.69e-10 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common PHOSPHOSERINE _BMRB_code . _PDB_code SEP _Standard_residue_derivative . _Molecular_mass 185.072 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 13:28:27 2011 ; 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 . ? CB CB C . 0 . ? OG OG O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 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 H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Potassium_channel '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 $Potassium_channel 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Potassium_channel . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength . _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.37 . n/a temperature 283 . K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . n/a temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 . H 1 . . . . . . . . $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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'Potassium channel' _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 MET HA H 4.18 . . 2 . 1 MET HB2 H 2.18 . . 3 . 1 MET HB3 H 2.18 . . 4 . 1 MET HG2 H 2.59 . . 5 . 1 MET HG3 H 2.61 . . 6 . 2 ILE H H 8.74 . . 7 . 2 ILE HA H 4.29 . . 8 . 2 ILE HB H 1.88 . . 9 . 2 ILE HG2 H 1.23 . . 10 . 2 ILE HD1 H 1.52 . . 11 . 2 ILE HG12 H 0.89 . . 12 . 2 ILE HG13 H 0.96 . . 13 . 3 SER H H 8.64 . . 14 . 3 SER HA H 4.53 . . 15 . 3 SER HB2 H 3.88 . . 16 . 3 SER HB3 H 3.88 . . 17 . 4 SER H H 8.56 . . 18 . 4 SER HA H 4.51 . . 19 . 4 SER HB2 H 3.89 . . 20 . 4 SER HB3 H 3.89 . . 21 . 5 VAL H H 8.25 . . 22 . 5 VAL HA H 4.16 . . 23 . 5 VAL HB H 2.08 . . 24 . 5 VAL HG1 H 0.95 . . 25 . 5 VAL HG2 H 0.95 . . 26 . 6 CYS H H 8.58 . . 27 . 6 CYS HA H 4.56 . . 28 . 6 CYS HB2 H 2.91 . . 29 . 6 CYS HB3 H 2.91 . . 30 . 7 VAL H H 8.49 . . 31 . 7 VAL HA H 4.16 . . 32 . 7 VAL HB H 2.13 . . 33 . 7 VAL HG1 H 0.97 . . 34 . 7 VAL HG2 H 0.97 . . 35 . 8 SER H H 8.52 . . 36 . 8 SER HA H 4.49 . . 37 . 8 SER HB2 H 3.84 . . 38 . 8 SER HB3 H 3.92 . . 39 . 9 SER H H 8.40 . . 40 . 9 SER HA H 4.45 . . 41 . 9 SER HB2 H 3.84 . . 42 . 9 SER HB3 H 3.87 . . 43 . 10 TYR H H 8.30 . . 44 . 10 TYR HA H 4.55 . . 45 . 10 TYR HB2 H 3.03 . . 46 . 10 TYR HB3 H 3.03 . . 47 . 10 TYR HD1 H 7.13 . . 48 . 10 TYR HD2 H 7.13 . . 49 . 10 TYR HE1 H 6.83 . . 50 . 10 TYR HE2 H 6.82 . . 51 . 11 ARG H H 8.33 . . 52 . 11 ARG HA H 4.28 . . 53 . 11 ARG HB2 H 1.69 . . 54 . 11 ARG HB3 H 1.84 . . 55 . 11 ARG HG2 H 1.57 . . 56 . 11 ARG HG3 H 1.57 . . 57 . 11 ARG HE H 7.21 . . 58 . 11 ARG HH21 H 6.52 . . 59 . 11 ARG HH22 H 6.52 . . 60 . 11 ARG HD2 H 3.19 . . 61 . 11 ARG HD3 H 3.19 . . 62 . 11 ARG HH11 H 6.88 . . 63 . 11 ARG HH12 H 6.88 . . 64 . 12 GLY H H 7.78 . . 65 . 12 GLY HA2 H 3.90 . . 66 . 12 GLY HA3 H 3.90 . . 67 . 13 ARG H H 8.26 . . 68 . 13 ARG HA H 4.37 . . 69 . 13 ARG HB2 H 1.78 . . 70 . 13 ARG HB3 H 1.89 . . 71 . 13 ARG HG2 H 1.65 . . 72 . 13 ARG HG3 H 1.65 . . 73 . 13 ARG HD2 H 3.21 . . 74 . 13 ARG HD3 H 3.21 . . 75 . 13 ARG HH11 H 7.32 . . 76 . 13 ARG HH12 H 7.32 . . 77 . 13 ARG HH21 H 6.52 . . 78 . 13 ARG HH22 H 6.88 . . 79 . 14 LYS H H 8.70 . . 80 . 14 LYS HA H 4.36 . . 81 . 14 LYS HB2 H 1.81 . . 82 . 14 LYS HB3 H 1.88 . . 83 . 14 LYS HG2 H 1.46 . . 84 . 14 LYS HG3 H 1.46 . . 85 . 14 LYS HZ H 7.59 . . 86 . 14 LYS HD2 H 1.70 . . 87 . 14 LYS HD3 H 1.70 . . 88 . 14 LYS HE2 H 3.00 . . 89 . 14 LYS HE3 H 3.00 . . 90 . 15 SEP H H 8.63 . . 91 . 15 SEP HA H 4.58 . . 92 . 15 SEP HB2 H 4.16 . . 93 . 15 SEP HB3 H 4.16 . . 94 . 16 GLY H H 8.48 . . 95 . 16 GLY HA2 H 3.99 . . 96 . 16 GLY HA3 H 3.99 . . 97 . 17 ASN H H 8.39 . . 98 . 17 ASN HA H 4.71 . . 99 . 17 ASN HB2 H 2.73 . . 100 . 17 ASN HB3 H 2.81 . . 101 . 17 ASN HD21 H 7.00 . . 102 . 17 ASN HD22 H 7.69 . . 103 . 18 LYS H H 8.41 . . 104 . 18 LYS HA H 4.61 . . 105 . 18 LYS HB2 H 1.73 . . 106 . 18 LYS HB3 H 1.81 . . 107 . 18 LYS HG2 H 1.48 . . 108 . 18 LYS HG3 H 1.48 . . 109 . 18 LYS HZ H 7.59 . . 110 . 18 LYS HD2 H 1.70 . . 111 . 18 LYS HD3 H 1.70 . . 112 . 18 LYS HE2 H 3.01 . . 113 . 18 LYS HE3 H 3.01 . . 114 . 19 PRO HA H 4.73 . . 115 . 19 PRO HB2 H 2.05 . . 116 . 19 PRO HB3 H 2.37 . . 117 . 19 PRO HG2 H 1.92 . . 118 . 19 PRO HG3 H 1.92 . . 119 . 19 PRO HD2 H 3.62 . . 120 . 19 PRO HD3 H 3.88 . . 121 . 20 PRO HA H 4.47 . . 122 . 20 PRO HB2 H 2.07 . . 123 . 20 PRO HB3 H 2.36 . . 124 . 20 PRO HG2 H 1.97 . . 125 . 20 PRO HG3 H 1.97 . . 126 . 20 PRO HD2 H 3.67 . . 127 . 20 PRO HD3 H 3.84 . . 128 . 21 SEP H H 8.80 . . 129 . 21 SEP HA H 4.55 . . 130 . 21 SEP HB2 H 4.16 . . 131 . 21 SEP HB3 H 4.16 . . 132 . 22 LYS H H 8.46 . . 133 . 22 LYS HA H 4.45 . . 134 . 22 LYS HB2 H 1.81 . . 135 . 22 LYS HB3 H 1.90 . . 136 . 22 LYS HG2 H 1.47 . . 137 . 22 LYS HG3 H 1.47 . . 138 . 22 LYS HZ H 7.59 . . 139 . 22 LYS HD2 H 1.71 . . 140 . 22 LYS HD3 H 1.71 . . 141 . 22 LYS HE2 H 3.01 . . 142 . 22 LYS HE3 H 3.01 . . 143 . 23 THR H H 8.24 . . 144 . 23 THR HA H 4.31 . . 145 . 23 THR HB H 4.20 . . 146 . 23 THR HG2 H 1.22 . . 147 . 24 CYS H H 8.47 . . 148 . 24 CYS HA H 4.54 . . 149 . 24 CYS HB2 H 2.96 . . 150 . 24 CYS HB3 H 2.96 . . 151 . 25 LEU H H 8.44 . . 152 . 25 LEU HA H 4.34 . . 153 . 25 LEU HB2 H 1.67 . . 154 . 25 LEU HB3 H 1.67 . . 155 . 25 LEU HG H 1.61 . . 156 . 25 LEU HD1 H 0.89 . . 157 . 25 LEU HD2 H 0.95 . . 158 . 26 LYS H H 8.38 . . 159 . 26 LYS HA H 4.28 . . 160 . 26 LYS HB2 H 1.81 . . 161 . 26 LYS HB3 H 1.81 . . 162 . 26 LYS HG2 H 1.46 . . 163 . 26 LYS HG3 H 1.46 . . 164 . 26 LYS HZ H 7.59 . . 165 . 26 LYS HD2 H 1.70 . . 166 . 26 LYS HD3 H 1.70 . . 167 . 26 LYS HE2 H 3.00 . . 168 . 26 LYS HE3 H 3.00 . . 169 . 27 GLU H H 8.38 . . 170 . 27 GLU HA H 4.33 . . 171 . 27 GLU HB2 H 2.02 . . 172 . 27 GLU HB3 H 2.11 . . 173 . 27 GLU HG2 H 2.47 . . 174 . 27 GLU HG3 H 2.47 . . 175 . 28 GLU H H 8.47 . . 176 . 28 GLU HA H 4.43 . . 177 . 28 GLU HB2 H 2.03 . . 178 . 28 GLU HB3 H 2.14 . . 179 . 28 GLU HG2 H 2.47 . . 180 . 28 GLU HG3 H 2.47 . . 181 . 29 MET H H 8.46 . . 182 . 29 MET HA H 4.46 . . 183 . 29 MET HB2 H 2.05 . . 184 . 29 MET HB3 H 2.13 . . 185 . 29 MET HG2 H 2.58 . . 186 . 29 MET HG3 H 2.66 . . 187 . 30 ALA H H 8.35 . . 188 . 30 ALA HA H 4.29 . . 189 . 30 ALA HB H 1.43 . . stop_ save_