Header list of 1f6g.pdb file
Complete list - 3 20 Bytes
HEADER PROTON TRANSPORT, MEMBRANE PROTEIN 21-JUN-00 1F6G
TITLE POTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: FULL-LENGTH CHANNEL;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE32
KEYWDS POTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN, CYTOPLASMIC DOMAINS,
KEYWDS 2 PROTON TRANSPORT, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 8
MDLTYP CA ATOMS ONLY, CHAIN A, B, C, D
AUTHOR D.M.CORTES,E.PEROZO
REVDAT 3 03-NOV-21 1F6G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1F6G 1 VERSN
REVDAT 1 21-FEB-01 1F6G 0
JRNL AUTH D.M.CORTES,L.G.CUELLO,E.PEROZO
JRNL TITL MOLECULAR ARCHITECTURE OF FULL-LENGTH KCSA: ROLE OF
JRNL TITL 2 CYTOPLASMIC DOMAINS IN ION PERMEATION AND ACTIVATION GATING.
JRNL REF J.GEN.PHYSIOL. V. 117 165 2001
JRNL REFN ISSN 0022-1295
JRNL PMID 11158168
JRNL DOI 10.1085/JGP.117.2.165
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : EPR AQUISIT 2.32, DISCOVER 3
REMARK 3 AUTHORS : BRUKER INSTRUMENTS (EPR AQUISIT), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 438
REMARK 3 RESTRAINTS, WITH 84 INTRA-SUBUNIT DISTANCE CONSTRAINTS PER
REMARK 3 SUBUNIT AND 15 INTER-SUBUNIT CONSTRAINTS
REMARK 4
REMARK 4 1F6G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011301.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50-100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50-100 UM KCSA, PBS PH 7.2,
REMARK 210 RECONSTITUTED INTO ASOLECTIN
REMARK 210 VESICLES AT A 1:500 PROTEIN:
REMARK 210 LIPID RATIO (MOLAR)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : POWER SATURATION EXPERIMENTS IN
REMARK 210 21% O2 OR 10 MM NIEDDA; DIPOLAR
REMARK 210 COUPLINGS DERIVED FROM
REMARK 210 UNDERLABELED SAMPLES
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 : DISCOVER 3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 32
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING SECONDARY STRUCTURE
REMARK 210 ASSIGNMENTS FROM FREQUENCY ANALYSIS OF SOLVENT ACCESSIBILITY
REMARK 210 DATA AND TERTIARY AND QUATERNARY STRUCTURAL INFORMATION FROM
REMARK 210 SPIN-SPIN DIPOLAR COUPLINGS
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: 1BL8 RELATED DB: PDB
DBREF 1F6G A 1 160 UNP P0A334 KCSA_STRLI 1 160
DBREF 1F6G B 1 160 UNP P0A334 KCSA_STRLI 1 160
DBREF 1F6G C 1 160 UNP P0A334 KCSA_STRLI 1 160
DBREF 1F6G D 1 160 UNP P0A334 KCSA_STRLI 1 160
SEQADV 1F6G ALA A 27 UNP P0A334 ARG 27 CONFLICT
SEQADV 1F6G ALA A 64 UNP P0A334 ARG 64 CONFLICT
SEQADV 1F6G CYS A 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1F6G ALA B 27 UNP P0A334 ARG 27 CONFLICT
SEQADV 1F6G ALA B 64 UNP P0A334 ARG 64 CONFLICT
SEQADV 1F6G CYS B 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1F6G ALA C 27 UNP P0A334 ARG 27 CONFLICT
SEQADV 1F6G ALA C 64 UNP P0A334 ARG 64 CONFLICT
SEQADV 1F6G CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1F6G ALA D 27 UNP P0A334 ARG 27 CONFLICT
SEQADV 1F6G ALA D 64 UNP P0A334 ARG 64 CONFLICT
SEQADV 1F6G CYS D 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQRES 1 A 160 MET PRO PRO MET LEU SER GLY LEU LEU ALA ARG LEU VAL
SEQRES 2 A 160 LYS LEU LEU LEU GLY ARG HIS GLY SER ALA LEU HIS TRP
SEQRES 3 A 160 ALA ALA ALA GLY ALA ALA THR VAL LEU LEU VAL ILE VAL
SEQRES 4 A 160 LEU LEU ALA GLY SER TYR LEU ALA VAL LEU ALA GLU ARG
SEQRES 5 A 160 GLY ALA PRO GLY ALA GLN LEU ILE THR TYR PRO ALA ALA
SEQRES 6 A 160 LEU TRP TRP SER VAL GLU THR ALA THR THR VAL GLY TYR
SEQRES 7 A 160 GLY ASP LEU TYR PRO VAL THR LEU TRP GLY ARG CYS VAL
SEQRES 8 A 160 ALA VAL VAL VAL MET VAL ALA GLY ILE THR SER PHE GLY
SEQRES 9 A 160 LEU VAL THR ALA ALA LEU ALA THR TRP PHE VAL GLY ARG
SEQRES 10 A 160 GLU GLN GLU ARG ARG GLY HIS PHE VAL ARG HIS SER GLU
SEQRES 11 A 160 LYS ALA ALA GLU GLU ALA TYR THR ARG THR THR ARG ALA
SEQRES 12 A 160 LEU HIS GLU ARG PHE ASP ARG LEU GLU ARG MET LEU ASP
SEQRES 13 A 160 ASP ASN ARG ARG
SEQRES 1 B 160 MET PRO PRO MET LEU SER GLY LEU LEU ALA ARG LEU VAL
SEQRES 2 B 160 LYS LEU LEU LEU GLY ARG HIS GLY SER ALA LEU HIS TRP
SEQRES 3 B 160 ALA ALA ALA GLY ALA ALA THR VAL LEU LEU VAL ILE VAL
SEQRES 4 B 160 LEU LEU ALA GLY SER TYR LEU ALA VAL LEU ALA GLU ARG
SEQRES 5 B 160 GLY ALA PRO GLY ALA GLN LEU ILE THR TYR PRO ALA ALA
SEQRES 6 B 160 LEU TRP TRP SER VAL GLU THR ALA THR THR VAL GLY TYR
SEQRES 7 B 160 GLY ASP LEU TYR PRO VAL THR LEU TRP GLY ARG CYS VAL
SEQRES 8 B 160 ALA VAL VAL VAL MET VAL ALA GLY ILE THR SER PHE GLY
SEQRES 9 B 160 LEU VAL THR ALA ALA LEU ALA THR TRP PHE VAL GLY ARG
SEQRES 10 B 160 GLU GLN GLU ARG ARG GLY HIS PHE VAL ARG HIS SER GLU
SEQRES 11 B 160 LYS ALA ALA GLU GLU ALA TYR THR ARG THR THR ARG ALA
SEQRES 12 B 160 LEU HIS GLU ARG PHE ASP ARG LEU GLU ARG MET LEU ASP
SEQRES 13 B 160 ASP ASN ARG ARG
SEQRES 1 C 160 MET PRO PRO MET LEU SER GLY LEU LEU ALA ARG LEU VAL
SEQRES 2 C 160 LYS LEU LEU LEU GLY ARG HIS GLY SER ALA LEU HIS TRP
SEQRES 3 C 160 ALA ALA ALA GLY ALA ALA THR VAL LEU LEU VAL ILE VAL
SEQRES 4 C 160 LEU LEU ALA GLY SER TYR LEU ALA VAL LEU ALA GLU ARG
SEQRES 5 C 160 GLY ALA PRO GLY ALA GLN LEU ILE THR TYR PRO ALA ALA
SEQRES 6 C 160 LEU TRP TRP SER VAL GLU THR ALA THR THR VAL GLY TYR
SEQRES 7 C 160 GLY ASP LEU TYR PRO VAL THR LEU TRP GLY ARG CYS VAL
SEQRES 8 C 160 ALA VAL VAL VAL MET VAL ALA GLY ILE THR SER PHE GLY
SEQRES 9 C 160 LEU VAL THR ALA ALA LEU ALA THR TRP PHE VAL GLY ARG
SEQRES 10 C 160 GLU GLN GLU ARG ARG GLY HIS PHE VAL ARG HIS SER GLU
SEQRES 11 C 160 LYS ALA ALA GLU GLU ALA TYR THR ARG THR THR ARG ALA
SEQRES 12 C 160 LEU HIS GLU ARG PHE ASP ARG LEU GLU ARG MET LEU ASP
SEQRES 13 C 160 ASP ASN ARG ARG
SEQRES 1 D 160 MET PRO PRO MET LEU SER GLY LEU LEU ALA ARG LEU VAL
SEQRES 2 D 160 LYS LEU LEU LEU GLY ARG HIS GLY SER ALA LEU HIS TRP
SEQRES 3 D 160 ALA ALA ALA GLY ALA ALA THR VAL LEU LEU VAL ILE VAL
SEQRES 4 D 160 LEU LEU ALA GLY SER TYR LEU ALA VAL LEU ALA GLU ARG
SEQRES 5 D 160 GLY ALA PRO GLY ALA GLN LEU ILE THR TYR PRO ALA ALA
SEQRES 6 D 160 LEU TRP TRP SER VAL GLU THR ALA THR THR VAL GLY TYR
SEQRES 7 D 160 GLY ASP LEU TYR PRO VAL THR LEU TRP GLY ARG CYS VAL
SEQRES 8 D 160 ALA VAL VAL VAL MET VAL ALA GLY ILE THR SER PHE GLY
SEQRES 9 D 160 LEU VAL THR ALA ALA LEU ALA THR TRP PHE VAL GLY ARG
SEQRES 10 D 160 GLU GLN GLU ARG ARG GLY HIS PHE VAL ARG HIS SER GLU
SEQRES 11 D 160 LYS ALA ALA GLU GLU ALA TYR THR ARG THR THR ARG ALA
SEQRES 12 D 160 LEU HIS GLU ARG PHE ASP ARG LEU GLU ARG MET LEU ASP
SEQRES 13 D 160 ASP ASN ARG ARG
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
MODEL 1
Complete list - 3 20 Bytes