HEADER MEMBRANE PROTEIN 02-OCT-03 1R3K
TITLE POTASSIUM CHANNEL KCSA-FAB COMPLEX IN LOW CONCENTRATION OF TL+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL;
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 11 ORGANISM_TAXID: 1916;
SOURCE 12 GENE: KCSA, SKC1, SCO7660, SC10F4.33;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: XL1BLUE;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS MEMBRANE PROTEIN, POTASSIUM CHANNEL, KCSA-FAB COMPLEX, THALLIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHOU,R.MACKINNON
REVDAT 4 23-AUG-23 1R3K 1 REMARK
REVDAT 3 27-OCT-21 1R3K 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1R3K 1 VERSN
REVDAT 1 25-NOV-03 1R3K 0
JRNL AUTH Y.ZHOU,R.MACKINNON
JRNL TITL THE OCCUPANCY OF IONS IN THE K+ SELECTIVITY FILTER: CHARGE
JRNL TITL 2 BALANCE AND COUPLING OF ION BINDING TO A PROTEIN
JRNL TITL 3 CONFORMATIONAL CHANGE UNDERLIE HIGH CONDUCTION RATES
JRNL REF J.MOL.BIOL. V. 333 965 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14583193
JRNL DOI 10.1016/J.JMB.2003.09.022
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 21821
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1094
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3403
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 172
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3981
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.37000
REMARK 3 B22 (A**2) : -5.37000
REMARK 3 B33 (A**2) : 10.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 43.55
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : TL_PB.PAR
REMARK 3 PARAMETER FILE 4 : LIPID.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : LIPID.TOP
REMARK 3 TOPOLOGY FILE 4 : TL_CHARGE.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE OCCUPANCY OF IONS IN THIS MODEL WERE ESTIMATED VALUES. PLEASE
REMARK 3 REFER TO
REMARK 3 THE PRIMARY CITATION FOR A DETAILED ANALYSIS OF ION OCCUPANCY.
REMARK 4
REMARK 4 1R3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.935
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21868
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1K4C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, SODIUM ACETATE, MAGNESIUM
REMARK 280 ACETATE, PH 5.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 77.09000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.52500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 77.09000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.52500
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 77.09000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 77.09000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.52500
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 77.09000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 77.09000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.52500
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: HOMO-TETRAMER OF KCSA IS GENERATED BY FOUR FOLD AXIS:
REMARK 300 X,Y,Z
REMARK 300 -X,-Y,Z
REMARK 300 -X,Y,Z
REMARK 300 X,-Y,Z
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 308.36000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 308.36000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 308.36000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 308.36000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 TL TL C 301 LIES ON A SPECIAL POSITION.
REMARK 375 TL TL C 302 LIES ON A SPECIAL POSITION.
REMARK 375 TL TL C 303 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PRO C 3
REMARK 465 MET C 4
REMARK 465 LEU C 5
REMARK 465 SER C 6
REMARK 465 GLY C 7
REMARK 465 LEU C 8
REMARK 465 LEU C 9
REMARK 465 ALA C 10
REMARK 465 ARG C 11
REMARK 465 LEU C 12
REMARK 465 VAL C 13
REMARK 465 LYS C 14
REMARK 465 LEU C 15
REMARK 465 LEU C 16
REMARK 465 LEU C 17
REMARK 465 GLY C 18
REMARK 465 ARG C 19
REMARK 465 HIS C 20
REMARK 465 GLY C 21
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 LEU A 125 CG CD1 CD2
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 GLN A 156 CG CD OE1 NE2
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 ILE A 205 CG1 CG2 CD1
REMARK 470 VAL A 206 CG1 CG2
REMARK 470 ASN A 212 CG OD1 ND2
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 GLN B 65 CG CD OE1 NE2
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 GLN B 136 CG CD OE1 NE2
REMARK 470 THR B 137 OG1 CG2
REMARK 470 ASN B 138 CG OD1 ND2
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 SER B 165 OG
REMARK 470 SER B 177 OG
REMARK 470 ASP B 178 CG OD1 OD2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 ASP B 219 CG OD1 OD2
REMARK 470 SER C 22 OG
REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 117 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP A 32 O GLN A 90 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 145 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 13 153.87 165.92
REMARK 500 PRO A 15 129.36 -38.57
REMARK 500 ALA A 51 -51.37 71.69
REMARK 500 PRO A 59 150.52 -48.29
REMARK 500 SER A 77 87.70 55.18
REMARK 500 ALA A 84 -167.86 -179.95
REMARK 500 THR A 126 -18.29 -43.23
REMARK 500 ASP A 184 -73.65 -50.12
REMARK 500 GLU A 185 -35.68 -40.00
REMARK 500 ARG A 188 38.89 -76.36
REMARK 500 ASN A 190 -53.76 -120.20
REMARK 500 ARG A 211 13.01 -55.75
REMARK 500 VAL B 2 90.06 46.82
REMARK 500 ALA B 16 -156.02 -62.89
REMARK 500 SER B 54 -92.20 -51.40
REMARK 500 ASN B 61 98.10 -65.76
REMARK 500 ALA B 92 175.69 177.11
REMARK 500 ARG B 100 32.85 -82.64
REMARK 500 ALA B 119 176.62 -57.77
REMARK 500 THR B 122 114.37 -160.64
REMARK 500 PRO B 131 173.51 -58.70
REMARK 500 ASN B 138 -144.18 -86.62
REMARK 500 ASN B 160 46.37 73.27
REMARK 500 GLN B 176 108.70 -176.29
REMARK 500 SER B 192 -5.94 -59.22
REMARK 500 THR B 197 153.13 -42.86
REMARK 500 SER B 208 72.58 45.66
REMARK 500 LYS B 213 116.66 -162.08
REMARK 500 ARG C 121 32.21 -88.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE LIGAND DGA IS A PARTIAL LIPID.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DGA C 201
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL C 302 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 75 OG1
REMARK 620 2 THR C 75 O 58.4
REMARK 620 3 THR C 75 OG1 82.4 92.6
REMARK 620 4 THR C 75 O 112.3 70.0 58.4
REMARK 620 5 THR C 75 OG1 82.4 112.3 137.3 161.8
REMARK 620 6 THR C 75 O 92.6 70.0 161.8 108.5 58.4
REMARK 620 7 THR C 75 OG1 137.3 161.8 82.4 92.6 82.4 112.3
REMARK 620 8 THR C 75 O 161.8 108.5 112.3 70.0 92.6 70.0 58.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TL C 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K4C RELATED DB: PDB
REMARK 900 POTASSIUM CHANNEL KCSA-FAB COMPLEX IN HIGH CONCENTRATION OF K+
REMARK 900 RELATED ID: 1K4D RELATED DB: PDB
REMARK 900 POTASSIUM CHANNEL KCSA-FAB COMPLEX IN LOW CONCENTRATION OF K+
REMARK 900 RELATED ID: 1R3I RELATED DB: PDB
REMARK 900 POTASSIUM CHANNEL KCSA-FAB COMPLEX IN RB+
REMARK 900 RELATED ID: 1R3J RELATED DB: PDB
REMARK 900 POTASSIUM CHANNEL KCSA-FAB COMPLEX IN HIGH CONCENTRATION OF TL+
REMARK 900 RELATED ID: 1R3L RELATED DB: PDB
REMARK 900 POTASSIUM CHANNEL KCSA-FAB COMPLEX IN CS+
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SUITABLE DATABASE REFERENCE SEQUENCE COULD NOT BE
REMARK 999 FOUND FOR CHAINS A AND B AT THE TIME OF PROCESSING.
DBREF 1R3K C 1 124 UNP P0A334 KCSA_STRLI 1 124
DBREF 1R3K A 1 212 PDB 1R3K 1R3K 1 212
DBREF 1R3K B 1 219 PDB 1R3K 1R3K 1 219
SEQADV 1R3K ALA C 2 UNP P0A334 PRO 2 ENGINEERED MUTATION
SEQADV 1R3K CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQRES 1 A 212 ASP ILE LEU LEU THR GLN SER PRO ALA ILE LEU SER VAL
SEQRES 2 A 212 SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER
SEQRES 3 A 212 GLN SER ILE GLY THR ASP ILE HIS TRP TYR GLN GLN ARG
SEQRES 4 A 212 THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 A 212 GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 A 212 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 A 212 GLU SER GLU ASP ILE ALA ASN TYR TYR CYS GLN GLN SER
SEQRES 8 A 212 ASN ARG TRP PRO PHE THR PHE GLY SER GLY THR LYS LEU
SEQRES 9 A 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 A 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 A 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 A 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 A 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 A 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 A 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 A 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 A 212 PHE ASN ARG ASN
SEQRES 1 B 219 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 B 219 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 B 219 TYR THR PHE THR SER ASP TRP ILE HIS TRP VAL LYS GLN
SEQRES 4 B 219 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE ILE
SEQRES 5 B 219 PRO SER TYR GLY ARG ALA ASN TYR ASN GLU LYS ILE GLN
SEQRES 6 B 219 LYS LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 B 219 ALA PHE MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 B 219 ALA VAL TYR TYR CYS ALA ARG GLU ARG GLY ASP GLY TYR
SEQRES 9 B 219 PHE ALA VAL TRP GLY ALA GLY THR THR VAL THR VAL SER
SEQRES 10 B 219 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 B 219 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 B 219 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 B 219 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 B 219 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 B 219 SER SER SER VAL THR VAL PRO SER SER SER TRP PRO SER
SEQRES 16 B 219 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 B 219 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 1 C 124 MET ALA PRO MET LEU SER GLY LEU LEU ALA ARG LEU VAL
SEQRES 2 C 124 LYS LEU LEU LEU GLY ARG HIS GLY SER ALA LEU HIS TRP
SEQRES 3 C 124 ARG ALA ALA GLY ALA ALA THR VAL LEU LEU VAL ILE VAL
SEQRES 4 C 124 LEU LEU ALA GLY SER TYR LEU ALA VAL LEU ALA GLU ARG
SEQRES 5 C 124 GLY ALA PRO GLY ALA GLN LEU ILE THR TYR PRO ARG ALA
SEQRES 6 C 124 LEU TRP TRP SER VAL GLU THR ALA THR THR VAL GLY TYR
SEQRES 7 C 124 GLY ASP LEU TYR PRO VAL THR LEU TRP GLY ARG CYS VAL
SEQRES 8 C 124 ALA VAL VAL VAL MET VAL ALA GLY ILE THR SER PHE GLY
SEQRES 9 C 124 LEU VAL THR ALA ALA LEU ALA THR TRP PHE VAL GLY ARG
SEQRES 10 C 124 GLU GLN GLU ARG ARG GLY HIS
HET DGA C 201 21
HET TL C 301 1
HET TL C 302 1
HET TL C 303 1
HETNAM DGA DIACYL GLYCEROL
HETNAM TL THALLIUM (I) ION
FORMUL 4 DGA C39 H76 O5
FORMUL 5 TL 3(TL 1+)
HELIX 1 1 GLU A 79 ILE A 83 5 5
HELIX 2 2 SER A 121 THR A 126 1 6
HELIX 3 3 LYS A 183 ARG A 188 1 6
HELIX 4 4 HIS B 204 SER B 208 5 5
HELIX 5 5 ALA C 23 ARG C 52 1 30
HELIX 6 6 THR C 61 THR C 74 1 14
HELIX 7 7 THR C 85 ARG C 121 1 37
SHEET 1 A 4 LEU A 4 THR A 5 0
SHEET 2 A 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5
SHEET 3 A 4 ASP A 70 ILE A 75 -1 O LEU A 73 N PHE A 21
SHEET 4 A 4 PHE A 62 SER A 67 -1 N SER A 63 O SER A 74
SHEET 1 B 5 ILE A 10 LEU A 11 0
SHEET 2 B 5 THR A 102 LEU A 104 1 O LYS A 103 N LEU A 11
SHEET 3 B 5 ASN A 85 GLN A 89 -1 N TYR A 86 O THR A 102
SHEET 4 B 5 HIS A 34 GLN A 38 -1 N HIS A 34 O GLN A 89
SHEET 5 B 5 ARG A 45 ILE A 48 -1 O ILE A 48 N TRP A 35
SHEET 1 C 4 THR A 114 PHE A 118 0
SHEET 2 C 4 GLY A 129 PHE A 139 -1 O VAL A 133 N PHE A 118
SHEET 3 C 4 TYR A 173 THR A 182 -1 O TYR A 173 N PHE A 139
SHEET 4 C 4 VAL A 159 THR A 164 -1 N SER A 162 O SER A 176
SHEET 1 D 4 SER A 153 ARG A 155 0
SHEET 2 D 4 ILE A 144 ILE A 150 -1 N TRP A 148 O ARG A 155
SHEET 3 D 4 SER A 191 HIS A 198 -1 O GLU A 195 N LYS A 147
SHEET 4 D 4 SER A 201 ASN A 210 -1 O LYS A 207 N CYS A 194
SHEET 1 E 4 LEU B 4 GLN B 5 0
SHEET 2 E 4 SER B 17 ALA B 24 -1 O LYS B 23 N GLN B 5
SHEET 3 E 4 THR B 78 SER B 84 -1 O LEU B 83 N VAL B 18
SHEET 4 E 4 LEU B 70 ASP B 73 -1 N THR B 71 O PHE B 80
SHEET 1 F 6 ALA B 9 VAL B 12 0
SHEET 2 F 6 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12
SHEET 3 F 6 ALA B 92 GLU B 99 -1 N ALA B 92 O VAL B 114
SHEET 4 F 6 TRP B 33 GLN B 39 -1 N VAL B 37 O TYR B 95
SHEET 5 F 6 GLU B 46 ILE B 52 -1 O ILE B 51 N ILE B 34
SHEET 6 F 6 ARG B 57 TYR B 60 -1 O ARG B 57 N ILE B 52
SHEET 1 G 4 ALA B 9 VAL B 12 0
SHEET 2 G 4 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12
SHEET 3 G 4 ALA B 92 GLU B 99 -1 N ALA B 92 O VAL B 114
SHEET 4 G 4 PHE B 105 TRP B 108 -1 O VAL B 107 N ARG B 98
SHEET 1 H 4 SER B 125 LEU B 129 0
SHEET 2 H 4 MET B 140 TYR B 150 -1 O LEU B 146 N TYR B 127
SHEET 3 H 4 TYR B 180 PRO B 189 -1 O TYR B 180 N TYR B 150
SHEET 4 H 4 HIS B 169 THR B 170 -1 N HIS B 169 O SER B 185
SHEET 1 I 4 SER B 125 LEU B 129 0
SHEET 2 I 4 MET B 140 TYR B 150 -1 O LEU B 146 N TYR B 127
SHEET 3 I 4 TYR B 180 PRO B 189 -1 O TYR B 180 N TYR B 150
SHEET 4 I 4 VAL B 174 LEU B 175 -1 N VAL B 174 O THR B 181
SHEET 1 J 3 THR B 156 TRP B 159 0
SHEET 2 J 3 THR B 199 ALA B 203 -1 O ASN B 201 N THR B 158
SHEET 3 J 3 VAL B 211 LYS B 214 -1 O VAL B 211 N VAL B 202
SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.06
SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04
SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.04
SSBOND 4 CYS B 145 CYS B 200 1555 1555 2.05
LINK OG1 THR C 75 TL TL C 302 1555 1555 3.30
LINK O THR C 75 TL TL C 302 1555 1555 3.02
LINK OG1 THR C 75 TL TL C 302 4575 1555 3.30
LINK O THR C 75 TL TL C 302 4575 1555 3.02
LINK OG1 THR C 75 TL TL C 302 3755 1555 3.30
LINK O THR C 75 TL TL C 302 3755 1555 3.02
LINK OG1 THR C 75 TL TL C 302 2775 1555 3.30
LINK O THR C 75 TL TL C 302 2775 1555 3.02
CISPEP 1 SER A 7 PRO A 8 0 -0.46
CISPEP 2 TRP A 94 PRO A 95 0 -0.16
CISPEP 3 TYR A 140 PRO A 141 0 -0.03
CISPEP 4 PHE B 151 PRO B 152 0 -0.23
CISPEP 5 GLU B 153 PRO B 154 0 0.16
CISPEP 6 TRP B 193 PRO B 194 0 -0.40
SITE 1 AC1 3 GLU A 53 PRO C 63 ARG C 89
SITE 1 AC2 1 TYR C 78
SITE 1 AC3 1 THR C 75
CRYST1 154.180 154.180 75.050 90.00 90.00 90.00 I 4 8
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 0.006486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013324 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
