HEADER MEMBRANE PROTEIN 09-AUG-11 3TCU
TITLE CRYSTAL STRUCTURE OF NAK2K CHANNEL D68E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 226900;
SOURCE 4 STRAIN: ATCC 14579 / DSM 31;
SOURCE 5 GENE: BC_0669;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS MEMBRANE PROTEIN, ION CHANNEL
EXPDTA X-RAY DIFFRACTION
AUTHOR D.B.SAUER,W.ZENG,S.RAGHUNATHAN,Y.JIANG
REVDAT 3 28-FEB-24 3TCU 1 REMARK SEQADV LINK
REVDAT 2 19-OCT-11 3TCU 1 JRNL
REVDAT 1 05-OCT-11 3TCU 0
JRNL AUTH D.B.SAUER,W.ZENG,S.RAGHUNATHAN,Y.JIANG
JRNL TITL PROTEIN INTERACTIONS CENTRAL TO STABILIZING THE K+ CHANNEL
JRNL TITL 2 SELECTIVITY FILTER IN A FOUR-SITED CONFIGURATION FOR
JRNL TITL 3 SELECTIVE K+ PERMEATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 16634 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21933962
JRNL DOI 10.1073/PNAS.1111688108
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 18669
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 955
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 14.9621 - 3.3370 0.97 2533 118 0.2181 0.2150
REMARK 3 2 3.3370 - 2.6535 1.00 2573 128 0.1693 0.2107
REMARK 3 3 2.6535 - 2.3195 1.00 2539 154 0.1766 0.2147
REMARK 3 4 2.3195 - 2.1081 1.00 2552 136 0.1874 0.2296
REMARK 3 5 2.1081 - 1.9573 1.00 2594 123 0.1825 0.2410
REMARK 3 6 1.9573 - 1.8421 1.00 2535 144 0.2237 0.2642
REMARK 3 7 1.8421 - 1.7500 0.95 2388 152 0.2825 0.3129
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.49
REMARK 3 B_SOL : 147.9
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.980
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) : -0.46580
REMARK 3 B22 (A**2) : -0.46580
REMARK 3 B33 (A**2) : 0.93170
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 1527
REMARK 3 ANGLE : 0.975 2083
REMARK 3 CHIRALITY : 0.066 260
REMARK 3 PLANARITY : 0.003 251
REMARK 3 DIHEDRAL : 12.188 527
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7764 -12.9802 22.8075
REMARK 3 T TENSOR
REMARK 3 T11: 0.3806 T22: 0.2911
REMARK 3 T33: 0.2482 T12: -0.0280
REMARK 3 T13: 0.0128 T23: 0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 2.2261 L22: 0.9517
REMARK 3 L33: 0.3353 L12: -0.0948
REMARK 3 L13: 0.2813 L23: 0.3821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: -0.1369 S13: -0.1053
REMARK 3 S21: 0.2309 S22: -0.0193 S23: -0.0343
REMARK 3 S31: 0.1153 S32: -0.0157 S33: 0.0188
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1503 -6.9144 -20.4079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2298 T22: 0.2285
REMARK 3 T33: 0.2609 T12: -0.0246
REMARK 3 T13: 0.0183 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 0.8435 L22: 2.4315
REMARK 3 L33: 0.4277 L12: -0.2819
REMARK 3 L13: -0.5181 L23: -0.0466
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: -0.0997 S13: 0.0399
REMARK 3 S21: -0.0366 S22: -0.1432 S23: 0.0421
REMARK 3 S31: 0.1178 S32: -0.0584 S33: 0.0564
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067324.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18720
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.210
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% MPD, 100MM GLYCINE, PH 9.5, VAPOR
REMARK 280 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 33.69750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.69750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.01750
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.69750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.69750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.01750
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 33.69750
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 33.69750
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 42.01750
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 33.69750
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 33.69750
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 42.01750
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
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 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 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
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 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 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 A 1 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 2 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 3 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 4 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 5 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 6 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 7 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 8 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 125 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 135 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 138 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 130 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 A 18
REMARK 465 ALA A 19
REMARK 465 LYS A 20
REMARK 465 ARG A 114
REMARK 465 MET B 18
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 102 -58.34 -120.82
REMARK 500 VAL B 102 -58.25 -123.76
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 1 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 65 O
REMARK 620 2 TYR A 66 O 58.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 2 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 64 O
REMARK 620 2 GLY A 65 O 68.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 3 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 63 O
REMARK 620 2 VAL A 64 O 71.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 4 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 63 OG1
REMARK 620 2 THR A 63 O 59.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 6 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 64 O
REMARK 620 2 GLY B 65 O 71.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 7 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 63 O
REMARK 620 2 VAL B 64 O 71.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 8 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 63 OG1
REMARK 620 2 THR B 63 O 59.7
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 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OUF RELATED DB: PDB
REMARK 900 STRUCTURE OF A K+ SELECTIVE NAK MUTANT
REMARK 900 RELATED ID: 3T4D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NAK2K CHANNEL Y55F MUTANT
REMARK 900 RELATED ID: 3T4Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NAK2K CHANNEL Y55W MUTANT
DBREF 3TCU A 20 110 UNP Q81HW2 Q81HW2_BACCR 20 110
DBREF 3TCU B 20 110 UNP Q81HW2 Q81HW2_BACCR 20 110
SEQADV 3TCU MET A 18 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU ALA A 19 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU TYR A 66 UNP Q81HW2 ASP 66 ENGINEERED MUTATION
SEQADV 3TCU GLU A 68 UNP Q81HW2 ASN 68 ENGINEERED MUTATION
SEQADV 3TCU LEU A 111 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU VAL A 112 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU PRO A 113 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU ARG A 114 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU MET B 18 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU ALA B 19 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU TYR B 66 UNP Q81HW2 ASP 66 ENGINEERED MUTATION
SEQADV 3TCU GLU B 68 UNP Q81HW2 ASN 68 ENGINEERED MUTATION
SEQADV 3TCU LEU B 111 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU VAL B 112 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU PRO B 113 UNP Q81HW2 EXPRESSION TAG
SEQADV 3TCU ARG B 114 UNP Q81HW2 EXPRESSION TAG
SEQRES 1 A 97 MET ALA LYS ASP LYS GLU PHE GLN VAL LEU PHE VAL LEU
SEQRES 2 A 97 THR ILE LEU THR LEU ILE SER GLY THR ILE PHE TYR SER
SEQRES 3 A 97 THR VAL GLU GLY LEU ARG PRO ILE ASP ALA LEU TYR PHE
SEQRES 4 A 97 SER VAL VAL THR LEU THR THR VAL GLY TYR GLY GLU PHE
SEQRES 5 A 97 SER PRO GLN THR ASP PHE GLY LYS ILE PHE THR ILE LEU
SEQRES 6 A 97 TYR ILE PHE ILE GLY ILE GLY LEU VAL PHE GLY PHE ILE
SEQRES 7 A 97 HIS LYS LEU ALA VAL ASN VAL GLN LEU PRO SER ILE LEU
SEQRES 8 A 97 SER ASN LEU VAL PRO ARG
SEQRES 1 B 97 MET ALA LYS ASP LYS GLU PHE GLN VAL LEU PHE VAL LEU
SEQRES 2 B 97 THR ILE LEU THR LEU ILE SER GLY THR ILE PHE TYR SER
SEQRES 3 B 97 THR VAL GLU GLY LEU ARG PRO ILE ASP ALA LEU TYR PHE
SEQRES 4 B 97 SER VAL VAL THR LEU THR THR VAL GLY TYR GLY GLU PHE
SEQRES 5 B 97 SER PRO GLN THR ASP PHE GLY LYS ILE PHE THR ILE LEU
SEQRES 6 B 97 TYR ILE PHE ILE GLY ILE GLY LEU VAL PHE GLY PHE ILE
SEQRES 7 B 97 HIS LYS LEU ALA VAL ASN VAL GLN LEU PRO SER ILE LEU
SEQRES 8 B 97 SER ASN LEU VAL PRO ARG
HET K A 1 2
HET K A 2 1
HET K A 3 1
HET K A 4 1
HET K B 5 1
HET K B 6 1
HET K B 7 1
HET K B 8 1
HETNAM K POTASSIUM ION
FORMUL 3 K 8(K 1+)
FORMUL 11 HOH *52(H2 O)
HELIX 1 1 ASP A 21 GLU A 46 1 26
HELIX 2 2 ARG A 49 THR A 62 1 14
HELIX 3 3 THR A 73 VAL A 102 1 30
HELIX 4 4 VAL A 102 LEU A 111 1 10
HELIX 5 5 LYS B 20 GLU B 46 1 27
HELIX 6 6 ARG B 49 THR B 62 1 14
HELIX 7 7 THR B 73 VAL B 102 1 30
HELIX 8 8 VAL B 102 ASN B 110 1 9
LINK K A K A 1 O GLY A 65 1555 1555 3.32
LINK K B K A 1 O TYR A 66 1555 1555 2.93
LINK K A K A 1 O TYR A 66 1555 1555 3.05
LINK K K A 2 O VAL A 64 1555 1555 3.18
LINK K K A 2 O GLY A 65 1555 1555 3.10
LINK K K A 3 O THR A 63 1555 1555 2.92
LINK K K A 3 O VAL A 64 1555 1555 3.08
LINK K K A 4 OG1 THR A 63 1555 1555 3.00
LINK K K A 4 O THR A 63 1555 1555 3.22
LINK K K B 5 O TYR B 66 1555 1555 3.35
LINK K K B 6 O VAL B 64 1555 1555 3.20
LINK K K B 6 O GLY B 65 1555 1555 3.49
LINK K K B 7 O THR B 63 1555 1555 2.99
LINK K K B 7 O VAL B 64 1555 1555 2.97
LINK K K B 8 OG1 THR B 63 1555 1555 2.90
LINK K K B 8 O THR B 63 1555 1555 3.12
SITE 1 AC1 3 K A 2 GLY A 65 TYR A 66
SITE 1 AC2 4 K A 1 K A 3 VAL A 64 GLY A 65
SITE 1 AC3 3 K A 2 THR A 63 VAL A 64
SITE 1 AC4 1 THR A 63
SITE 1 AC5 3 K B 6 GLY B 65 TYR B 66
SITE 1 AC6 4 K B 5 K B 7 VAL B 64 GLY B 65
SITE 1 AC7 3 K B 6 THR B 63 VAL B 64
SITE 1 AC8 1 THR B 63
CRYST1 67.395 67.395 84.035 90.00 90.00 90.00 I 4 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 0.014838 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014838 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011900 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
