HEADER MEMBRANE PROTEIN/METAL TRANSPORT 10-NOV-08 3F7V
TITLE KCSA POTASSIUM CHANNEL IN THE OPEN-INACTIVATED STATE WITH 23 A OPENING
TITLE 2 AT T112
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT 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_TAXID: 10090;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 6 ORGANISM_TAXID: 10090;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: STREPTOMYCES LIVIDANS;
SOURCE 9 ORGANISM_TAXID: 1916;
SOURCE 10 GENE: KCSA, SKC1;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: XL10-GOLD;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PQE70
KEYWDS KCSA, POTASSIUM CHANNEL, INACTIVATION, OPEN, CELL MEMBRANE, ION
KEYWDS 2 TRANSPORT, IONIC CHANNEL, MEMBRANE, TRANSMEMBRANE, TRANSPORT,
KEYWDS 3 VOLTAGE-GATED CHANNEL, MEMBRANE PROTEIN-METAL TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.G.CUELLO,V.JOGINI,D.M.CORTES,E.PEROZO
REVDAT 4 27-DEC-23 3F7V 1 REMARK
REVDAT 3 20-OCT-21 3F7V 1 REMARK SEQADV LINK
REVDAT 2 09-FEB-11 3F7V 1 REMARK
REVDAT 1 19-MAY-10 3F7V 0
JRNL AUTH L.G.CUELLO,V.JOGINI,D.M.CORTES,E.PEROZO
JRNL TITL KCSA POTASSIUM CHANNEL IN THE OPEN-INACTIVATED STATE WITH 23
JRNL TITL 2 A OPENING AT T112
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13848
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.259
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1297
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 : 3938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.413
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3F7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050256.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0-6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13848
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG400, 50MM MAGNESIUM ACETATE,
REMARK 280 50MM SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
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 77.97450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.97450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.70900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 77.97450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.97450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.70900
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 77.97450
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 77.97450
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.70900
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 77.97450
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 77.97450
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.70900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
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 311.89800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -311.89800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -311.89800
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 311.89800
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
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 K K C 1 LIES ON A SPECIAL POSITION.
REMARK 375 K K C 2 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 GLY C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 LEU C 24
REMARK 465 GLN C 25
REMARK 465 TRP C 26
REMARK 465 ARG C 27
REMARK 465 ALA C 28
REMARK 465 GLN C 119
REMARK 465 GLN C 120
REMARK 465 GLN C 121
REMARK 465 GLN C 122
REMARK 465 GLY C 123
REMARK 465 GLN C 124
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 TYR C 45 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 VAL C 95 CG1 CG2
REMARK 470 GLN C 117 CG CD OE1 NE2
REMARK 470 GLU C 118 CG CD OE1 OE2
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 A 145 CA - CB - SG ANGL. DEV. = 7.5 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 GLU A 10 116.49 -161.62
REMARK 500 CYS A 22 104.86 -170.34
REMARK 500 SER A 54 26.59 -74.09
REMARK 500 TYR A 55 -36.90 -168.49
REMARK 500 LYS A 74 -56.16 -27.22
REMARK 500 SER A 85 77.99 40.79
REMARK 500 ALA A 92 -177.02 177.20
REMARK 500 ARG A 100 26.59 -75.69
REMARK 500 ALA A 119 166.07 -47.60
REMARK 500 LEU A 129 89.07 -151.20
REMARK 500 SER A 133 -36.01 -36.29
REMARK 500 ASN A 138 -165.30 -125.02
REMARK 500 CYS A 145 130.86 -174.66
REMARK 500 PRO A 154 -169.87 -108.74
REMARK 500 SER A 192 -2.34 -53.34
REMARK 500 PRO B 15 160.24 -48.25
REMARK 500 ASP B 32 45.38 -76.22
REMARK 500 ALA B 51 -40.28 75.39
REMARK 500 SER B 77 76.24 73.38
REMARK 500 SER B 80 -45.82 -29.22
REMARK 500 ALA B 84 -164.00 -166.94
REMARK 500 PHE B 96 150.40 -46.73
REMARK 500 ARG B 108 -169.99 -106.51
REMARK 500 THR B 126 -6.46 -56.94
REMARK 500 TYR B 140 132.94 -176.29
REMARK 500 PRO B 141 173.00 -54.40
REMARK 500 ASP B 170 19.73 -142.80
REMARK 500 THR B 172 -164.06 -108.78
REMARK 500 ASP B 184 -70.98 -49.33
REMARK 500 ASN B 190 -84.72 -66.85
REMARK 500 LYS B 199 -15.10 -35.85
REMARK 500 PHE B 209 137.98 -175.60
REMARK 500 THR C 33 0.39 -53.55
REMARK 500 SER C 69 -75.71 -56.92
REMARK 500 TRP C 113 -19.41 -42.78
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 C 2 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 75 O
REMARK 620 2 THR C 75 OG1 46.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FB5 RELATED DB: PDB
REMARK 900 SAME COMPLEX AT 2.8A RESOLUTION
REMARK 900 RELATED ID: 3FB6 RELATED DB: PDB
REMARK 900 SAME COMPLEX AT 3.0A RESOLUTION
REMARK 900 RELATED ID: 3FB7 RELATED DB: PDB
REMARK 900 SAME COMPLEX AT 3.3A RESOLUTION
REMARK 900 RELATED ID: 3FB8 RELATED DB: PDB
REMARK 900 SAME COMPLEX AT 3.4A RESOLUTION
REMARK 900 RELATED ID: 3F7Y RELATED DB: PDB
REMARK 900 SAME COMPLEX AT 3.4A RESOLUTION
DBREF 3F7V C 21 124 UNP P0A334 KCSA_STRLI 21 124
DBREF 3F7V A 1 219 PDB 3F7V 3F7V 1 219
DBREF 3F7V B 1 212 PDB 3F7V 3F7V 1 212
SEQADV 3F7V GLN C 25 UNP P0A334 HIS 25 ENGINEERED MUTATION
SEQADV 3F7V CYS C 90 UNP P0A334 LEU 90 ENGINEERED MUTATION
SEQADV 3F7V GLN C 117 UNP P0A334 ARG 117 ENGINEERED MUTATION
SEQADV 3F7V GLN C 120 UNP P0A334 GLU 120 ENGINEERED MUTATION
SEQADV 3F7V GLN C 121 UNP P0A334 ARG 121 ENGINEERED MUTATION
SEQADV 3F7V GLN C 122 UNP P0A334 ARG 122 ENGINEERED MUTATION
SEQADV 3F7V GLN C 124 UNP P0A334 HIS 124 ENGINEERED MUTATION
SEQRES 1 A 219 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 A 219 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 A 219 TYR THR PHE THR SER ASP TRP ILE HIS TRP VAL LYS GLN
SEQRES 4 A 219 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY GLU ILE ILE
SEQRES 5 A 219 PRO SER TYR GLY ARG ALA ASN TYR ASN GLU LYS ILE GLN
SEQRES 6 A 219 LYS LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR
SEQRES 7 A 219 ALA PHE MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 A 219 ALA VAL TYR TYR CYS ALA ARG GLU ARG GLY ASP GLY TYR
SEQRES 9 A 219 PHE ALA VAL TRP GLY ALA GLY THR THR VAL THR VAL SER
SEQRES 10 A 219 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 A 219 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 A 219 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 A 219 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 A 219 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 A 219 SER SER SER VAL THR VAL PRO SER SER SER TRP PRO SER
SEQRES 16 A 219 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 A 219 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 1 B 212 ASP ILE LEU LEU THR GLN SER PRO ALA ILE LEU SER VAL
SEQRES 2 B 212 SER PRO GLY GLU ARG VAL SER PHE SER CYS ARG ALA SER
SEQRES 3 B 212 GLN SER ILE GLY THR ASP ILE HIS TRP TYR GLN GLN ARG
SEQRES 4 B 212 THR ASN GLY SER PRO ARG LEU LEU ILE LYS TYR ALA SER
SEQRES 5 B 212 GLU SER ILE SER GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 B 212 GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER VAL
SEQRES 7 B 212 GLU SER GLU ASP ILE ALA ASN TYR TYR CYS GLN GLN SER
SEQRES 8 B 212 ASN ARG TRP PRO PHE THR PHE GLY SER GLY THR LYS LEU
SEQRES 9 B 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 B 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 B 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 B 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 B 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 B 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 B 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 B 212 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 B 212 PHE ASN ARG ASN
SEQRES 1 C 104 GLY SER ALA LEU GLN TRP ARG ALA ALA GLY ALA ALA THR
SEQRES 2 C 104 VAL LEU LEU VAL ILE VAL LEU LEU ALA GLY SER TYR LEU
SEQRES 3 C 104 ALA VAL LEU ALA GLU ARG GLY ALA PRO GLY ALA GLN LEU
SEQRES 4 C 104 ILE THR TYR PRO ARG ALA LEU TRP TRP SER VAL GLU THR
SEQRES 5 C 104 ALA THR THR VAL GLY TYR GLY ASP LEU TYR PRO VAL THR
SEQRES 6 C 104 LEU TRP GLY ARG CYS VAL ALA VAL VAL VAL MET VAL ALA
SEQRES 7 C 104 GLY ILE THR SER PHE GLY LEU VAL THR ALA ALA LEU ALA
SEQRES 8 C 104 THR TRP PHE VAL GLY GLN GLU GLN GLN GLN GLN GLY GLN
HET K C 1 1
HET K C 2 1
HETNAM K POTASSIUM ION
FORMUL 4 K 2(K 1+)
HELIX 1 1 THR A 87 SER A 91 5 5
HELIX 2 2 PRO A 205 SER A 208 5 4
HELIX 3 3 GLU B 79 ILE B 83 5 5
HELIX 4 4 SER B 121 THR B 126 1 6
HELIX 5 5 LYS B 183 ARG B 188 1 6
HELIX 6 6 ALA C 31 ARG C 52 1 22
HELIX 7 7 THR C 61 THR C 75 1 15
HELIX 8 8 TRP C 87 GLU C 118 1 32
SHEET 1 A 6 ALA A 9 VAL A 12 0
SHEET 2 A 6 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12
SHEET 3 A 6 ALA A 92 GLU A 99 -1 N ALA A 92 O VAL A 114
SHEET 4 A 6 TRP A 33 GLN A 39 -1 N VAL A 37 O TYR A 95
SHEET 5 A 6 GLU A 46 ILE A 51 -1 O GLU A 46 N LYS A 38
SHEET 6 A 6 ALA A 58 TYR A 60 -1 O ASN A 59 N GLU A 50
SHEET 1 B 4 ALA A 9 VAL A 12 0
SHEET 2 B 4 THR A 112 VAL A 116 1 O THR A 115 N VAL A 12
SHEET 3 B 4 ALA A 92 GLU A 99 -1 N ALA A 92 O VAL A 114
SHEET 4 B 4 PHE A 105 TRP A 108 -1 O VAL A 107 N ARG A 98
SHEET 1 C 3 VAL A 18 LYS A 23 0
SHEET 2 C 3 THR A 78 LEU A 83 -1 O LEU A 83 N VAL A 18
SHEET 3 C 3 ALA A 68 ASP A 73 -1 N THR A 71 O PHE A 80
SHEET 1 D 4 SER A 125 LEU A 129 0
SHEET 2 D 4 MET A 140 TYR A 150 -1 O LYS A 148 N SER A 125
SHEET 3 D 4 LEU A 179 PRO A 189 -1 O TYR A 180 N TYR A 150
SHEET 4 D 4 VAL A 168 THR A 170 -1 N HIS A 169 O SER A 185
SHEET 1 E 4 SER A 125 LEU A 129 0
SHEET 2 E 4 MET A 140 TYR A 150 -1 O LYS A 148 N SER A 125
SHEET 3 E 4 LEU A 179 PRO A 189 -1 O TYR A 180 N TYR A 150
SHEET 4 E 4 VAL A 174 GLN A 176 -1 N VAL A 174 O THR A 181
SHEET 1 F 3 THR A 156 TRP A 159 0
SHEET 2 F 3 CYS A 200 HIS A 204 -1 O ASN A 201 N THR A 158
SHEET 3 F 3 THR A 209 VAL A 211 -1 O VAL A 211 N VAL A 202
SHEET 1 G 4 LEU B 4 GLN B 6 0
SHEET 2 G 4 ARG B 18 ALA B 25 -1 O ARG B 24 N THR B 5
SHEET 3 G 4 ASP B 70 ASN B 76 -1 O PHE B 71 N CYS B 23
SHEET 4 G 4 PHE B 62 SER B 67 -1 N SER B 63 O SER B 74
SHEET 1 H 5 ILE B 10 VAL B 13 0
SHEET 2 H 5 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11
SHEET 3 H 5 ASN B 85 GLN B 90 -1 N TYR B 86 O THR B 102
SHEET 4 H 5 ILE B 33 GLN B 38 -1 N HIS B 34 O GLN B 89
SHEET 5 H 5 ARG B 45 ILE B 48 -1 O LEU B 47 N TRP B 35
SHEET 1 I 4 ILE B 10 VAL B 13 0
SHEET 2 I 4 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11
SHEET 3 I 4 ASN B 85 GLN B 90 -1 N TYR B 86 O THR B 102
SHEET 4 I 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90
SHEET 1 J 4 THR B 114 PHE B 118 0
SHEET 2 J 4 GLY B 129 PHE B 139 -1 O VAL B 133 N PHE B 118
SHEET 3 J 4 TYR B 173 THR B 182 -1 O LEU B 181 N ALA B 130
SHEET 4 J 4 VAL B 159 LEU B 160 -1 N LEU B 160 O THR B 178
SHEET 1 K 4 SER B 153 ARG B 155 0
SHEET 2 K 4 ASN B 145 ILE B 150 -1 N TRP B 148 O ARG B 155
SHEET 3 K 4 SER B 191 HIS B 198 -1 O GLU B 195 N LYS B 147
SHEET 4 K 4 SER B 201 ASN B 210 -1 O SER B 201 N HIS B 198
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 145 CYS A 200 1555 1555 2.07
SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04
SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.03
LINK K K C 2 O THR C 75 1555 1555 3.22
LINK K K C 2 OG1 THR C 75 1555 1555 3.28
CISPEP 1 PHE A 151 PRO A 152 0 -0.13
CISPEP 2 GLU A 153 PRO A 154 0 0.18
CISPEP 3 TRP A 193 PRO A 194 0 -1.26
CISPEP 4 SER B 7 PRO B 8 0 -0.06
CISPEP 5 TRP B 94 PRO B 95 0 -2.18
CISPEP 6 TYR B 140 PRO B 141 0 0.09
SITE 1 AC1 1 THR C 75
CRYST1 155.949 155.949 73.418 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 0.006412 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006412 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013621 0.00000
(ATOM LINES ARE NOT SHOWN.)
END