Header list of 1jq1.pdb file
Complete list - 27 202 Bytes
HEADER MEMBRANE PROTEIN 03-AUG-01 1JQ1
TITLE POTASSIUM CHANNEL (KCSA) OPEN GATE MODEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: INNER TRANSMEMBRANE SEGMENT (RESIDUES 86-119);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 3 ORGANISM_TAXID: 1916;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL-2 BLUE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE32
KEYWDS POTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN, OPEN STATE, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE; CA ATOMS ONLY, CHAIN A, B, C, D
AUTHOR Y.-S.LIU,P.SOMPORNPISUT,E.PEROZO
REVDAT 4 27-OCT-21 1JQ1 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JQ1 1 VERSN
REVDAT 2 01-APR-03 1JQ1 1 JRNL
REVDAT 1 03-OCT-01 1JQ1 0
JRNL AUTH Y.S.LIU,P.SOMPORNPISUT,E.PEROZO
JRNL TITL STRUCTURE OF THE KCSA CHANNEL INTRACELLULAR GATE IN THE OPEN
JRNL TITL 2 STATE.
JRNL REF NAT.STRUCT.BIOL. V. 8 883 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11573095
JRNL DOI 10.1038/NSB1001-883
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.SOMPORNPISUT,Y.-S.LIU,E.PEROZO
REMARK 1 TITL CALCULATION OF RIGID BODY CONFORMATIONAL CHANGES USING
REMARK 1 TITL 2 RESTRAINT-DRIVEN CARTESIAN TRANSFORMATIONS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.PEROZO,D.M.CORTES,L.G.CUELLO
REMARK 1 TITL STRUCTURAL REARRANGEMENTS UNDERLYING K+-CHANNEL ACTIVATION
REMARK 1 TITL 2 GATING
REMARK 1 REF SCIENCE V. 285 73 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.285.5424.73
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.A.DOYLE,J.MORAIS CABRAL,R.A.PFUETZNER,A.KUO,J.M.GULBIS,
REMARK 1 AUTH 2 S.L.COHEN,B.T.CHAIT,R.MACKINNON
REMARK 1 TITL THE STRUCTURE OF THE POTASSIUM CHANNEL: MOLECULAR BASIS OF
REMARK 1 TITL 2 K+ CONDUCTION AND SELECTIVITY
REMARK 1 REF SCIENCE V. 280 69 1998
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.280.5360.69
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 6.0
REMARK 3 AUTHORS : D.A.CASE ET.AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE ARE BASED ON: 1) TEN PAIRS OF INTER-SUBUNIT
REMARK 3 DISTANCES FOR THE KCSA INNER
REMARK 3 HELICAL BUNDLE IN THE CLOSED AND THE OPEN STATES AND 2) THE USE OF
REMARK 3 THE CRYSTAL STRUCTURE
REMARK 3 AS THE CHANNEL IN THE CLOSED STATE, AND AS THE REFERENCE
REMARK 3 STRUCTURE. THE COMPUTER PROGRAM
REMARK 3 REDCAT SEARCHES (RESTRAINT-DRIVEN CARTESIAN TRANSFORMATION) BASED
REMARK 3 ON THE EXHAUSTIVE SAMPLING
REMARK 3 OF RIGID-BODY MOVEMENT IN CARTESIAN SPACE FOR THE TM2 INNER BUNDLE
REMARK 3 IN THE OPEN STATE WERE
REMARK 3 ALLOWED TO CONVERGE TO A MINIMAL PENALTY VALUE. THE ENSEMBLE OF
REMARK 3 THE 50 LOWEST PENALTY
REMARK 3 CONFORMERS WAS SUBJECTED TO MOLECULAR MECHANIC ENERGY
REMARK 3 MINIMIZATION. FINAL REFINEMENT WAS
REMARK 3 PERFORMED ON THE AVERAGE OPEN HELICAL BUNDLE BY ENERGY
REMARK 3 MINIMIZATION.
REMARK 4
REMARK 4 1JQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 99
REMARK 99 THE STRUCTURE CONTAINS ONLY ALPHA-CARBONS BECAUSE
REMARK 99 THE EXPERIMENTAL DATA USED TO CALCULATE THE STRUCTURES
REMARK 99 ARE GOOD ENOUGH ONLY TO THE BACKBONE LEVEL.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014053.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 150.0; 150.0
REMARK 210 PH : 7.0; 4.0
REMARK 210 IONIC STRENGTH : 20 MM CITRATE PHOSPHATE; 20 MM
REMARK 210 CITRATE PHOSPHATE
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MG/ML MIXED WITH
REMARK 210 METHANETHIOSULFONATE SPIN LABEL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CONTINUOUS WAVE EPR
REMARK 210 SPECTROMETER FIELD STRENGTH : 3400 MHZ
REMARK 210 SPECTROMETER MODEL : EMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : EPR AQUISIT 2.32, REDCAT
REMARK 210 METHOD USED : FOURIER DECONVOLUTION,
REMARK 210 CONFORMATIONAL GRID SEARCH A
REMARK 210 CARTESAIN REPRESENTATION
REMARK 210 MOLECULAR MECHANIC ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JQ2 RELATED DB: PDB
REMARK 900 1JQ2 CONTAINS THE ENSEMBLE
DBREF 1JQ1 A 86 119 UNP P0A334 KCSA_STRLI 86 119
DBREF 1JQ1 B 86 119 UNP P0A334 KCSA_STRLI 86 119
DBREF 1JQ1 C 86 119 UNP P0A334 KCSA_STRLI 86 119
DBREF 1JQ1 D 86 119 UNP P0A334 KCSA_STRLI 86 119
SEQADV 1JQ1 CYS A 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1JQ1 CYS B 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1JQ1 CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1JQ1 CYS D 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQRES 1 A 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA
SEQRES 2 A 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA
SEQRES 3 A 34 THR TRP PHE VAL GLY ARG GLU GLN
SEQRES 1 B 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA
SEQRES 2 B 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA
SEQRES 3 B 34 THR TRP PHE VAL GLY ARG GLU GLN
SEQRES 1 C 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA
SEQRES 2 C 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA
SEQRES 3 C 34 THR TRP PHE VAL GLY ARG GLU GLN
SEQRES 1 D 34 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA
SEQRES 2 D 34 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA
SEQRES 3 D 34 THR TRP PHE VAL GLY ARG GLU GLN
CRYST1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 27 202 Bytes