HEADER MEMBRANE PROTEIN 23-JUL-98 1BL8
TITLE POTASSIUM CHANNEL (KCSA) FROM STREPTOMYCES LIVIDANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (POTASSIUM CHANNEL PROTEIN);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 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_STRAIN: XL-1 BLUE;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE60;
SOURCE 8 EXPRESSION_SYSTEM_GENE: KCSA
KEYWDS POTASSIUM CHANNEL, INTEGRAL MEMBRANE PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.DOYLE,J.M.CABRAL,R.A.PFUETZNER,A.KUO,J.M.GULBIS,S.L.COHEN,
AUTHOR 2 B.T.CHAIT,R.MACKINNON
REVDAT 7 07-FEB-24 1BL8 1 REMARK
REVDAT 6 03-NOV-21 1BL8 1 REMARK SEQADV LINK
REVDAT 5 04-OCT-17 1BL8 1 REMARK
REVDAT 4 13-JUL-11 1BL8 1 VERSN
REVDAT 3 24-FEB-09 1BL8 1 VERSN
REVDAT 2 12-JAN-00 1BL8 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 29-JUL-98 1BL8 0
JRNL AUTH D.A.DOYLE,J.MORAIS CABRAL,R.A.PFUETZNER,A.KUO,J.M.GULBIS,
JRNL AUTH 2 S.L.COHEN,B.T.CHAIT,R.MACKINNON
JRNL TITL THE STRUCTURE OF THE POTASSIUM CHANNEL: MOLECULAR BASIS OF
JRNL TITL 2 K+ CONDUCTION AND SELECTIVITY.
JRNL REF SCIENCE V. 280 69 1998
JRNL REFN ISSN 0036-8075
JRNL PMID 9525859
JRNL DOI 10.1126/SCIENCE.280.5360.69
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 12054
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELL
REMARK 3 R VALUE (WORKING SET) : 0.280
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1252
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2820
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.73
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.530
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
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 NCS MODEL : RESTRAINTS
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 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BL8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008416.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 6
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) : 0.908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12603
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
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: MIR
REMARK 200 SOFTWARE USED: CCP4, SHELXL-97
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ONE-TO-MIXTURE OF PROTEIN SOLUTION AND
REMARK 280 RESERVOIR (200 MM CACL2, 100 MM HEPES PH 7.5, 48% PEG 400).
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 1.000000 0.000000 0.000000 64.39000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.39000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.46500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
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 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 ARG A 27 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 60 CD1
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 ARG A 117 CZ NH1 NH2
REMARK 470 ARG B 27 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 60 CD1
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 71 CG CD OE1 OE2
REMARK 470 ARG B 117 CZ NH1 NH2
REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 60 CD1
REMARK 470 ARG C 64 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 71 CG CD OE1 OE2
REMARK 470 ARG C 117 CZ NH1 NH2
REMARK 470 ARG D 27 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 60 CD1
REMARK 470 ARG D 64 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 71 CG CD OE1 OE2
REMARK 470 ARG D 117 CZ NH1 NH2
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 LEU A 24 -71.94 -166.69
REMARK 500 ALA A 29 -67.66 -91.37
REMARK 500 VAL A 34 -5.50 -59.43
REMARK 500 LEU A 40 -79.32 -51.31
REMARK 500 TYR A 45 33.65 -78.78
REMARK 500 LEU A 46 -35.99 -139.23
REMARK 500 LEU A 49 8.38 -59.89
REMARK 500 ARG A 52 -40.86 -29.31
REMARK 500 ALA A 54 168.60 178.78
REMARK 500 PRO A 55 9.51 -56.95
REMARK 500 ALA A 57 -171.69 -58.34
REMARK 500 GLN A 58 3.64 -57.32
REMARK 500 LEU A 59 40.33 -70.63
REMARK 500 LEU A 66 -70.28 -49.04
REMARK 500 THR A 75 74.28 53.34
REMARK 500 ARG A 117 51.30 -144.35
REMARK 500 LEU B 24 -71.99 -166.60
REMARK 500 ALA B 29 -67.63 -91.16
REMARK 500 VAL B 34 -5.48 -59.43
REMARK 500 LEU B 40 -79.15 -51.48
REMARK 500 TYR B 45 33.67 -78.80
REMARK 500 LEU B 46 -36.21 -139.12
REMARK 500 LEU B 49 8.44 -60.33
REMARK 500 ARG B 52 -40.95 -29.29
REMARK 500 ALA B 54 168.72 178.96
REMARK 500 PRO B 55 9.39 -57.09
REMARK 500 ALA B 57 -171.88 -58.04
REMARK 500 GLN B 58 3.73 -57.26
REMARK 500 LEU B 59 40.50 -70.72
REMARK 500 LEU B 66 -70.09 -49.23
REMARK 500 THR B 75 74.38 53.17
REMARK 500 ARG B 117 51.36 -144.54
REMARK 500 LEU C 24 -72.08 -166.70
REMARK 500 ALA C 29 -67.64 -91.13
REMARK 500 VAL C 34 -5.31 -59.52
REMARK 500 LEU C 40 -79.01 -51.22
REMARK 500 TYR C 45 33.68 -78.88
REMARK 500 LEU C 46 -35.93 -139.28
REMARK 500 LEU C 49 8.35 -59.86
REMARK 500 ARG C 52 -40.88 -29.19
REMARK 500 ALA C 54 168.57 178.79
REMARK 500 PRO C 55 9.25 -56.84
REMARK 500 ALA C 57 -171.63 -58.31
REMARK 500 GLN C 58 3.52 -57.37
REMARK 500 LEU C 59 40.37 -70.49
REMARK 500 THR C 75 74.42 53.97
REMARK 500 ARG C 117 51.47 -144.56
REMARK 500 LEU D 24 -71.92 -166.62
REMARK 500 ALA D 29 -67.51 -91.21
REMARK 500 VAL D 34 -5.28 -59.65
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 K A 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 75 O
REMARK 620 2 VAL A 76 O 84.8
REMARK 620 3 K A 403 K 54.6 135.7
REMARK 620 4 THR B 75 O 69.9 101.5 52.1
REMARK 620 5 VAL B 76 O 130.6 58.2 135.1 85.7
REMARK 620 6 THR C 75 O 108.9 159.4 54.4 70.5 101.7
REMARK 620 7 VAL C 76 O 158.8 86.8 137.4 131.1 58.0 84.9
REMARK 620 8 THR D 75 O 70.2 130.9 55.9 108.0 158.9 69.4 101.4
REMARK 620 9 VAL D 76 O 101.5 58.4 138.4 159.4 86.5 129.9 57.7 85.4
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 75 O
REMARK 620 2 THR A 75 OG1 41.6
REMARK 620 3 THR B 75 O 80.6 122.1
REMARK 620 4 THR B 75 OG1 53.6 89.5 43.5
REMARK 620 5 THR C 75 O 128.0 127.8 81.1 124.6
REMARK 620 6 THR C 75 OG1 133.5 168.2 54.3 92.4 43.0
REMARK 620 7 THR D 75 O 78.1 51.7 129.1 130.9 76.9 119.9
REMARK 620 8 THR D 75 OG1 119.0 87.1 132.1 169.4 51.9 89.0 41.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 77 O
REMARK 620 2 TYR A 78 O 66.7
REMARK 620 3 GLY B 77 O 59.2 86.0
REMARK 620 4 TYR B 78 O 120.1 86.0 67.0
REMARK 620 5 HOH B 500 O 43.9 105.7 42.1 105.4
REMARK 620 6 GLY C 77 O 90.0 145.8 60.1 84.9 46.2
REMARK 620 7 TYR C 78 O 144.2 146.3 119.3 84.5 108.0 65.1
REMARK 620 8 GLY D 77 O 59.5 120.1 88.1 143.4 46.0 59.0 85.1
REMARK 620 9 TYR D 78 O 85.8 85.8 144.4 146.5 108.1 118.4 84.5 66.5
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: SEL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: FILTER TO SELECT FOR POTASSIUM IONS OVER OTHER
REMARK 800 MONOVALENT CATIONS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 403
DBREF 1BL8 A 23 119 UNP P0A334 KCSA_STRLI 23 119
DBREF 1BL8 B 23 119 UNP P0A334 KCSA_STRLI 23 119
DBREF 1BL8 C 23 119 UNP P0A334 KCSA_STRLI 23 119
DBREF 1BL8 D 23 119 UNP P0A334 KCSA_STRLI 23 119
SEQADV 1BL8 CYS A 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1BL8 CYS B 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1BL8 CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 1BL8 CYS D 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQRES 1 A 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU
SEQRES 2 A 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL
SEQRES 3 A 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR
SEQRES 4 A 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR
SEQRES 5 A 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP
SEQRES 6 A 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE
SEQRES 7 A 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP
SEQRES 8 A 97 PHE VAL GLY ARG GLU GLN
SEQRES 1 B 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU
SEQRES 2 B 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL
SEQRES 3 B 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR
SEQRES 4 B 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR
SEQRES 5 B 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP
SEQRES 6 B 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE
SEQRES 7 B 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP
SEQRES 8 B 97 PHE VAL GLY ARG GLU GLN
SEQRES 1 C 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU
SEQRES 2 C 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL
SEQRES 3 C 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR
SEQRES 4 C 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR
SEQRES 5 C 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP
SEQRES 6 C 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE
SEQRES 7 C 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP
SEQRES 8 C 97 PHE VAL GLY ARG GLU GLN
SEQRES 1 D 97 ALA LEU HIS TRP ARG ALA ALA GLY ALA ALA THR VAL LEU
SEQRES 2 D 97 LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU ALA VAL
SEQRES 3 D 97 LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU ILE THR
SEQRES 4 D 97 TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR ALA THR
SEQRES 5 D 97 THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR LEU TRP
SEQRES 6 D 97 GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA GLY ILE
SEQRES 7 D 97 THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA THR TRP
SEQRES 8 D 97 PHE VAL GLY ARG GLU GLN
HET K A 401 1
HET K A 402 1
HET K A 403 1
HETNAM K POTASSIUM ION
FORMUL 5 K 3(K 1+)
FORMUL 8 HOH *(H2 O)
HELIX 1 1 ARG A 27 GLU A 51 1 25
HELIX 2 2 TYR A 62 THR A 74 1 13
HELIX 3 3 LEU A 86 THR A 112 1 27
HELIX 4 4 ARG B 27 GLU B 51 1 25
HELIX 5 5 TYR B 62 THR B 74 1 13
HELIX 6 6 LEU B 86 THR B 112 1 27
HELIX 7 7 ARG C 27 GLU C 51 1 25
HELIX 8 8 TYR C 62 THR C 74 1 13
HELIX 9 9 LEU C 86 THR C 112 1 27
HELIX 10 10 ARG D 27 GLU D 51 1 25
HELIX 11 11 TYR D 62 THR D 74 1 13
HELIX 12 12 LEU D 86 THR D 112 1 27
LINK O THR A 75 K K A 402 1555 1555 3.40
LINK O THR A 75 K K A 403 1555 1555 3.07
LINK OG1 THR A 75 K K A 403 1555 1555 3.19
LINK O VAL A 76 K K A 402 1555 1555 3.43
LINK O GLY A 77 K K A 401 1555 1555 3.14
LINK O TYR A 78 K K A 401 1555 1555 3.08
LINK K K A 401 O GLY B 77 1555 1555 3.12
LINK K K A 401 O TYR B 78 1555 1555 3.07
LINK K K A 401 O HOH B 500 1555 1555 3.41
LINK K K A 401 O GLY C 77 1555 1555 3.15
LINK K K A 401 O TYR C 78 1555 1555 3.21
LINK K K A 401 O GLY D 77 1555 1555 3.15
LINK K K A 401 O TYR D 78 1555 1555 3.08
LINK K K A 402 K K A 403 1555 1555 3.30
LINK K K A 402 O THR B 75 1555 1555 3.38
LINK K K A 402 O VAL B 76 1555 1555 3.40
LINK K K A 402 O THR C 75 1555 1555 3.35
LINK K K A 402 O VAL C 76 1555 1555 3.47
LINK K K A 402 O THR D 75 1555 1555 3.39
LINK K K A 402 O VAL D 76 1555 1555 3.41
LINK K K A 403 O THR B 75 1555 1555 2.93
LINK K K A 403 OG1 THR B 75 1555 1555 3.03
LINK K K A 403 O THR C 75 1555 1555 3.04
LINK K K A 403 OG1 THR C 75 1555 1555 3.00
LINK K K A 403 O THR D 75 1555 1555 3.14
LINK K K A 403 OG1 THR D 75 1555 1555 3.19
SITE 1 SEL 4 VAL A 76 GLY A 77 TYR A 78 GLY A 79
SITE 1 AC1 8 GLY A 77 TYR A 78 GLY B 77 TYR B 78
SITE 2 AC1 8 GLY C 77 TYR C 78 GLY D 77 TYR D 78
SITE 1 AC2 9 THR A 75 VAL A 76 K A 403 THR B 75
SITE 2 AC2 9 VAL B 76 THR C 75 VAL C 76 THR D 75
SITE 3 AC2 9 VAL D 76
SITE 1 AC3 5 THR A 75 K A 402 THR B 75 THR C 75
SITE 2 AC3 5 THR D 75
CRYST1 128.780 68.930 112.040 90.00 124.63 90.00 C 1 2 1 16
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 0.007765 0.000000 0.005363 0.00000
SCALE2 0.000000 0.014507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010847 0.00000
MTRIX1 1 0.126600 0.928780 0.348340 31.41247 1
MTRIX2 1 -0.931190 -0.009730 0.364390 86.76519 1
MTRIX3 1 0.341830 -0.370510 0.863640 -12.10887 1
MTRIX1 2 -0.736910 -0.010340 0.675910 112.17546 1
MTRIX2 2 0.004580 -0.999940 -0.010300 53.01701 1
MTRIX3 2 0.675980 -0.004490 0.736910 -43.35083 1
MTRIX1 3 0.137220 -0.931030 0.338160 80.28391 1
MTRIX2 3 0.929330 0.002860 -0.369240 -33.25713 1
MTRIX3 3 0.342800 0.364930 0.865630 -31.77395 1
(ATOM LINES ARE NOT SHOWN.)
END