HEADER MEMBRANE PROTEIN 30-MAY-19 6RV4
TITLE CRYSTAL STRUCTURE OF THE HUMAN TWO PORE DOMAIN POTASSIUM ION CHANNEL
TITLE 2 TASK-1 (K2P3.1) IN A CLOSED CONFORMATION WITH A BOUND INHIBITOR BAY
TITLE 3 2341237
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL SUBFAMILY K MEMBER 3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ACID-SENSITIVE POTASSIUM CHANNEL PROTEIN TASK-1,TWIK-RELATED
COMPND 5 ACID-SENSITIVE K(+) CHANNEL 1,TWO PORE POTASSIUM CHANNEL KT3.1,TWO
COMPND 6 PORE K(+) CHANNEL KT3.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: TWO-PORE DOMAIN POTASSIUM CHANNEL K2P3.1 (TASK-1)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KCNK3, TASK, TASK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MEMBRANE PROTEIN, POTASSIUM CHANNEL, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.J.RODSTROM,A.C.W.PIKE,W.ZHANG,A.QUIGLEY,D.SPEEDMAN,
AUTHOR 2 S.M.M.MUKHOPADHYAY,L.SHRESTHA,R.CHALK,S.VENKAYA,S.R.BUSHELL,
AUTHOR 3 A.TESSITORE,N.BURGESS-BROWN,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 4 E.P.CARPENTER,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 22-JUL-20 6RV4 1 JRNL
REVDAT 1 07-AUG-19 6RV4 0
JRNL AUTH K.E.J.RODSTROM,A.K.KIPER,W.ZHANG,S.RINNE,A.C.W.PIKE,
JRNL AUTH 2 M.GOLDSTEIN,L.J.CONRAD,M.DELBECK,M.G.HAHN,H.MEIER,M.PLATZK,
JRNL AUTH 3 A.QUIGLEY,D.SPEEDMAN,L.SHRESTHA,S.M.M.MUKHOPADHYAY,
JRNL AUTH 4 N.A.BURGESS-BROWN,S.J.TUCKER,T.MULLER,N.DECHER,E.P.CARPENTER
JRNL TITL A LOWER X-GATE IN TASK CHANNELS TRAPS INHIBITORS WITHIN THE
JRNL TITL 2 VESTIBULE.
JRNL REF NATURE V. 582 443 2020
JRNL REFN ESSN 1476-4687
JRNL PMID 32499642
JRNL DOI 10.1038/S41586-020-2250-8
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.9
REMARK 3 NUMBER OF REFLECTIONS : 33045
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 + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1587
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 32.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 661
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2635
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 639
REMARK 3 BIN R VALUE (WORKING SET) : 0.2653
REMARK 3 BIN FREE R VALUE : 0.2138
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.33
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 : 7985
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 405
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.94000
REMARK 3 B22 (A**2) : 5.77930
REMARK 3 B33 (A**2) : 1.16070
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) : 0.540
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.419
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.801
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.826
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8585 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11657 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3013 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1402 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8585 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1131 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 64 ; 1.000 ; HARMONIC
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 10109 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.90
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.95
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.41
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|1 - 304}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7485 -41.2150 25.5404
REMARK 3 T TENSOR
REMARK 3 T11: -0.2828 T22: 0.0277
REMARK 3 T33: -0.0992 T12: -0.0018
REMARK 3 T13: 0.0198 T23: 0.2076
REMARK 3 L TENSOR
REMARK 3 L11: 2.7745 L22: 2.0745
REMARK 3 L33: 2.4188 L12: -0.2226
REMARK 3 L13: 0.1776 L23: -0.4083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0771 S12: 0.1962 S13: -0.1295
REMARK 3 S21: -0.1747 S22: -0.0421 S23: -0.0440
REMARK 3 S31: 0.0677 S32: 0.1007 S33: -0.0350
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {B|1 - 261}
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6706 -37.2418 29.0082
REMARK 3 T TENSOR
REMARK 3 T11: -0.2233 T22: -0.0070
REMARK 3 T33: -0.0340 T12: -0.0133
REMARK 3 T13: -0.0399 T23: 0.1969
REMARK 3 L TENSOR
REMARK 3 L11: 2.8422 L22: 1.1679
REMARK 3 L33: 2.1181 L12: 0.2642
REMARK 3 L13: -0.1612 L23: -0.6202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0797 S12: -0.0267 S13: 0.1217
REMARK 3 S21: -0.0430 S22: -0.0510 S23: 0.1805
REMARK 3 S31: -0.0504 S32: -0.1452 S33: -0.0287
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {C|1 - 304}
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1260 22.4424 33.3418
REMARK 3 T TENSOR
REMARK 3 T11: -0.3298 T22: 0.0033
REMARK 3 T33: -0.1193 T12: 0.0305
REMARK 3 T13: 0.0364 T23: 0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 3.4618 L22: 2.6158
REMARK 3 L33: 2.2062 L12: 0.0823
REMARK 3 L13: 0.6497 L23: -0.7653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: 0.1891 S13: 0.2304
REMARK 3 S21: -0.1330 S22: -0.0593 S23: 0.1753
REMARK 3 S31: -0.0625 S32: -0.2306 S33: 0.0814
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {D|1 - 261}
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5795 18.3619 36.7670
REMARK 3 T TENSOR
REMARK 3 T11: -0.2734 T22: 0.0023
REMARK 3 T33: -0.0574 T12: 0.0067
REMARK 3 T13: 0.0366 T23: 0.0891
REMARK 3 L TENSOR
REMARK 3 L11: 2.9084 L22: 2.1891
REMARK 3 L33: 2.2573 L12: 0.0551
REMARK 3 L13: -0.0628 L23: 0.0448
REMARK 3 S TENSOR
REMARK 3 S11: -0.0431 S12: -0.0615 S13: -0.0249
REMARK 3 S21: -0.1296 S22: 0.1215 S23: -0.0446
REMARK 3 S31: 0.1058 S32: 0.1286 S33: -0.0784
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED AGAINST STARANISO
REMARK 3 ANISOTROPICALLY TRUNCAED DATA. POSITIVE DIFFRERENCE PEAKS FOR
REMARK 3 WATER MOLECULES WERE SEEN, CORRESPONDING TO WATER POSITIONS IN
REMARK 3 6RV2 AND 6RV3, BUT WERE NOT MODELLED AT THIS RESOLUTION.
REMARK 4
REMARK 4 6RV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292102633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018
REMARK 200 DATA SCALING SOFTWARE : XDS VERSION JAN 26, 2018,
REMARK 200 STARANISO 2.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33101
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.099
REMARK 200 RESOLUTION RANGE LOW (A) : 43.116
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.18700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 34.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.60600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.7.17
REMARK 200 STARTING MODEL: 4BW5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.05 M KCL, 31% V/V
REMARK 280 PEG400, 3% W/V SUCROSE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.66500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 119.28500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 100.66500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 119.28500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 149
REMARK 465 ARG A 150
REMARK 465 ARG A 151
REMARK 465 GLU A 259
REMARK 465 ASN A 260
REMARK 465 LEU A 261
REMARK 465 TYR A 262
REMARK 465 PHE A 263
REMARK 465 GLN A 264
REMARK 465 MET B 149
REMARK 465 ARG B 150
REMARK 465 ARG B 151
REMARK 465 TYR B 262
REMARK 465 PHE B 263
REMARK 465 GLN B 264
REMARK 465 ALA C 258
REMARK 465 GLU C 259
REMARK 465 ASN C 260
REMARK 465 LEU C 261
REMARK 465 TYR C 262
REMARK 465 PHE C 263
REMARK 465 GLN C 264
REMARK 465 ARG D 150
REMARK 465 ARG D 151
REMARK 465 TYR D 262
REMARK 465 PHE D 263
REMARK 465 GLN D 264
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 LYS A 2 CE NZ
REMARK 470 GLU A 32 OE1 OE2
REMARK 470 GLU A 37 OE1 OE2
REMARK 470 GLN A 46 CG CD OE1 NE2
REMARK 470 ASN A 53 CG OD1 ND2
REMARK 470 GLN A 56 CG CD OE1 NE2
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 68 CD NE CZ NH1 NH2
REMARK 470 LYS A 70 CD CE NZ
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 ARG A 79 NE CZ NH1 NH2
REMARK 470 LYS A 210 CE NZ
REMARK 470 LYS A 255 CE NZ
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 2 CD CE NZ
REMARK 470 GLN B 45 CG CD OE1 NE2
REMARK 470 GLN B 56 CG CD OE1 NE2
REMARK 470 LEU B 62 CG CD1 CD2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 ARG B 79 NE CZ NH1 NH2
REMARK 470 LYS B 145 CE NZ
REMARK 470 GLN B 219 CG CD OE1 NE2
REMARK 470 ARG B 245 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 255 CG CD CE NZ
REMARK 470 ARG B 256 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 ASN B 260 CG OD1 ND2
REMARK 470 LEU B 261 CG CD1 CD2
REMARK 470 LYS C 2 CE NZ
REMARK 470 ARG C 3 NE CZ NH1 NH2
REMARK 470 GLU C 32 CD OE1 OE2
REMARK 470 GLU C 37 OE1 OE2
REMARK 470 GLN C 39 CD OE1 NE2
REMARK 470 GLU C 47 CG CD OE1 OE2
REMARK 470 ARG C 51 NE CZ NH1 NH2
REMARK 470 ASN C 53 CG OD1 ND2
REMARK 470 GLN C 56 CG CD OE1 NE2
REMARK 470 GLU C 60 CD OE1 OE2
REMARK 470 GLU C 61 CG CD OE1 OE2
REMARK 470 LEU C 62 CG CD1 CD2
REMARK 470 ARG C 64 NE CZ NH1 NH2
REMARK 470 LYS C 73 CE NZ
REMARK 470 ARG C 79 NE CZ NH1 NH2
REMARK 470 ARG C 142 NE CZ NH1 NH2
REMARK 470 LEU C 147 CG CD1 CD2
REMARK 470 ARG C 150 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 210 CE NZ
REMARK 470 LYS C 255 CE NZ
REMARK 470 ARG C 256 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 48 CG CD1 CD2
REMARK 470 ARG D 51 CZ NH1 NH2
REMARK 470 GLN D 56 CG CD OE1 NE2
REMARK 470 ARG D 68 NE CZ NH1 NH2
REMARK 470 LYS D 70 CG CD CE NZ
REMARK 470 LYS D 73 CG CD CE NZ
REMARK 470 ARG D 79 NE CZ NH1 NH2
REMARK 470 LYS D 145 CG CD CE NZ
REMARK 470 MET D 149 CG SD CE
REMARK 470 ASP D 153 CG OD1 OD2
REMARK 470 GLN D 219 CG CD OE1 NE2
REMARK 470 LYS D 255 CG CD CE NZ
REMARK 470 ARG D 256 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 261 CG CD1 CD2
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 ARG A 79 -162.70 -79.23
REMARK 500 ARG B 79 -162.89 -78.84
REMARK 500 ARG C 79 -163.72 -78.50
REMARK 500 ARG D 79 -164.16 -78.78
REMARK 500
REMARK 500 REMARK: NULL
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 PC1 A 308
REMARK 610 PC1 B 303
REMARK 610 PC1 C 305
REMARK 610 PC1 C 306
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 304 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 93 O
REMARK 620 2 THR A 93 OG1 66.7
REMARK 620 3 THR A 199 O 63.4 106.8
REMARK 620 4 THR A 199 OG1 104.3 78.4 66.7
REMARK 620 5 THR B 93 O 95.4 161.9 64.3 109.7
REMARK 620 6 THR B 93 OG1 162.0 130.9 108.7 85.6 66.9
REMARK 620 7 THR B 199 O 62.7 105.4 95.4 161.8 61.9 103.9
REMARK 620 8 THR B 199 OG1 105.3 82.5 158.8 134.5 101.1 76.4 63.6
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 303 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 93 O
REMARK 620 2 ILE A 94 O 74.8
REMARK 620 3 THR A 199 O 67.4 88.4
REMARK 620 4 ILE A 200 O 132.9 76.1 75.6
REMARK 620 5 THR B 93 O 103.9 154.9 68.7 88.1
REMARK 620 6 ILE B 94 O 154.6 117.6 131.4 72.5 74.4
REMARK 620 7 THR B 199 O 68.0 131.1 104.8 152.6 67.5 88.6
REMARK 620 8 ILE B 200 O 87.5 72.2 151.8 117.3 132.8 76.6 75.4
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 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 94 O
REMARK 620 2 GLY A 95 O 71.8
REMARK 620 3 ILE A 200 O 79.7 140.2
REMARK 620 4 GLY A 201 O 83.9 78.2 71.5
REMARK 620 5 ILE B 94 O 119.8 144.8 74.0 133.1
REMARK 620 6 GLY B 95 O 150.5 118.0 76.7 72.1 69.8
REMARK 620 7 ILE B 200 O 73.9 75.6 122.5 149.8 76.6 134.4
REMARK 620 8 GLY B 201 O 131.9 70.4 146.9 115.6 79.8 75.5 68.7
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 309 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 95 O
REMARK 620 2 TYR A 96 O 77.8
REMARK 620 3 GLY A 201 O 74.7 91.4
REMARK 620 4 PHE A 202 O 132.0 68.4 73.3
REMARK 620 5 GLY B 95 O 113.7 151.7 68.7 86.3
REMARK 620 6 TYR B 96 O 156.4 103.1 128.5 67.3 76.8
REMARK 620 7 GLY B 201 O 70.4 132.4 112.4 156.2 75.2 93.5
REMARK 620 8 PHE B 202 O 89.0 68.6 156.7 108.1 134.2 70.1 76.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 303 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 93 O
REMARK 620 2 ILE C 94 O 75.7
REMARK 620 3 THR C 199 O 67.9 89.3
REMARK 620 4 ILE C 200 O 134.2 76.9 75.9
REMARK 620 5 THR D 93 O 103.1 155.4 68.1 87.7
REMARK 620 6 ILE D 94 O 153.1 118.1 131.0 72.7 74.0
REMARK 620 7 THR D 199 O 67.8 131.7 104.4 151.2 66.6 87.2
REMARK 620 8 ILE D 200 O 87.7 73.1 153.0 118.0 131.5 75.9 74.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 304 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 93 O
REMARK 620 2 THR C 93 OG1 66.8
REMARK 620 3 THR C 199 O 63.7 106.6
REMARK 620 4 THR C 199 OG1 104.4 77.9 66.6
REMARK 620 5 THR D 93 O 96.2 162.9 64.7 109.5
REMARK 620 6 THR D 93 OG1 163.3 129.6 109.0 84.7 67.3
REMARK 620 7 THR D 199 O 63.1 105.6 96.4 162.7 62.8 104.7
REMARK 620 8 THR D 199 OG1 105.4 81.9 160.2 133.3 102.1 76.6 63.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE C 94 O
REMARK 620 2 GLY C 95 O 71.6
REMARK 620 3 ILE C 200 O 79.1 139.4
REMARK 620 4 GLY C 201 O 83.5 77.9 71.2
REMARK 620 5 ILE D 94 O 119.0 145.3 74.1 133.6
REMARK 620 6 GLY D 95 O 150.1 118.7 76.4 72.6 70.0
REMARK 620 7 ILE D 200 O 73.9 76.0 122.2 149.7 76.1 134.5
REMARK 620 8 GLY D 201 O 131.7 71.0 147.3 116.8 79.8 76.4 68.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 307 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 95 O
REMARK 620 2 TYR C 96 O 78.6
REMARK 620 3 GLY C 201 O 75.1 92.8
REMARK 620 4 PHE C 202 O 133.7 69.3 74.2
REMARK 620 5 GLY D 95 O 112.1 154.1 68.8 87.6
REMARK 620 6 TYR D 96 O 154.4 104.0 129.5 68.4 76.8
REMARK 620 7 GLY D 201 O 69.6 131.8 111.8 155.5 73.5 91.6
REMARK 620 8 PHE D 202 O 88.5 69.4 158.1 109.3 132.0 69.3 74.4
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 K A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KKZ A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KKZ D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 303
DBREF 6RV4 A 1 259 UNP O14649 KCNK3_HUMAN 1 259
DBREF 6RV4 B 1 259 UNP O14649 KCNK3_HUMAN 1 259
DBREF 6RV4 C 1 259 UNP O14649 KCNK3_HUMAN 1 259
DBREF 6RV4 D 1 259 UNP O14649 KCNK3_HUMAN 1 259
SEQADV 6RV4 ASN A 260 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 LEU A 261 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 TYR A 262 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 PHE A 263 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 GLN A 264 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 ASN B 260 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 LEU B 261 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 TYR B 262 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 PHE B 263 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 GLN B 264 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 ASN C 260 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 LEU C 261 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 TYR C 262 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 PHE C 263 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 GLN C 264 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 ASN D 260 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 LEU D 261 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 TYR D 262 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 PHE D 263 UNP O14649 EXPRESSION TAG
SEQADV 6RV4 GLN D 264 UNP O14649 EXPRESSION TAG
SEQRES 1 A 264 MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL
SEQRES 2 A 264 CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE
SEQRES 3 A 264 ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN
SEQRES 4 A 264 ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR
SEQRES 5 A 264 ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL
SEQRES 6 A 264 VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP
SEQRES 7 A 264 ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE
SEQRES 8 A 264 THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP
SEQRES 9 A 264 GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY
SEQRES 10 A 264 ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU
SEQRES 11 A 264 ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA
SEQRES 12 A 264 LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET
SEQRES 13 A 264 ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER
SEQRES 14 A 264 THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU
SEQRES 15 A 264 HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE
SEQRES 16 A 264 THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU
SEQRES 17 A 264 GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL
SEQRES 18 A 264 ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL
SEQRES 19 A 264 ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET
SEQRES 20 A 264 THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN
SEQRES 21 A 264 LEU TYR PHE GLN
SEQRES 1 B 264 MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL
SEQRES 2 B 264 CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE
SEQRES 3 B 264 ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN
SEQRES 4 B 264 ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR
SEQRES 5 B 264 ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL
SEQRES 6 B 264 VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP
SEQRES 7 B 264 ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE
SEQRES 8 B 264 THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP
SEQRES 9 B 264 GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY
SEQRES 10 B 264 ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU
SEQRES 11 B 264 ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA
SEQRES 12 B 264 LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET
SEQRES 13 B 264 ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER
SEQRES 14 B 264 THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU
SEQRES 15 B 264 HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE
SEQRES 16 B 264 THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU
SEQRES 17 B 264 GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL
SEQRES 18 B 264 ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL
SEQRES 19 B 264 ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET
SEQRES 20 B 264 THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN
SEQRES 21 B 264 LEU TYR PHE GLN
SEQRES 1 C 264 MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL
SEQRES 2 C 264 CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE
SEQRES 3 C 264 ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN
SEQRES 4 C 264 ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR
SEQRES 5 C 264 ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL
SEQRES 6 C 264 VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP
SEQRES 7 C 264 ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE
SEQRES 8 C 264 THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP
SEQRES 9 C 264 GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY
SEQRES 10 C 264 ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU
SEQRES 11 C 264 ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA
SEQRES 12 C 264 LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET
SEQRES 13 C 264 ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER
SEQRES 14 C 264 THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU
SEQRES 15 C 264 HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE
SEQRES 16 C 264 THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU
SEQRES 17 C 264 GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL
SEQRES 18 C 264 ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL
SEQRES 19 C 264 ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET
SEQRES 20 C 264 THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN
SEQRES 21 C 264 LEU TYR PHE GLN
SEQRES 1 D 264 MET LYS ARG GLN ASN VAL ARG THR LEU ALA LEU ILE VAL
SEQRES 2 D 264 CYS THR PHE THR TYR LEU LEU VAL GLY ALA ALA VAL PHE
SEQRES 3 D 264 ASP ALA LEU GLU SER GLU PRO GLU LEU ILE GLU ARG GLN
SEQRES 4 D 264 ARG LEU GLU LEU ARG GLN GLN GLU LEU ARG ALA ARG TYR
SEQRES 5 D 264 ASN LEU SER GLN GLY GLY TYR GLU GLU LEU GLU ARG VAL
SEQRES 6 D 264 VAL LEU ARG LEU LYS PRO HIS LYS ALA GLY VAL GLN TRP
SEQRES 7 D 264 ARG PHE ALA GLY SER PHE TYR PHE ALA ILE THR VAL ILE
SEQRES 8 D 264 THR THR ILE GLY TYR GLY HIS ALA ALA PRO SER THR ASP
SEQRES 9 D 264 GLY GLY LYS VAL PHE CYS MET PHE TYR ALA LEU LEU GLY
SEQRES 10 D 264 ILE PRO LEU THR LEU VAL MET PHE GLN SER LEU GLY GLU
SEQRES 11 D 264 ARG ILE ASN THR LEU VAL ARG TYR LEU LEU HIS ARG ALA
SEQRES 12 D 264 LYS LYS GLY LEU GLY MET ARG ARG ALA ASP VAL SER MET
SEQRES 13 D 264 ALA ASN MET VAL LEU ILE GLY PHE PHE SER CYS ILE SER
SEQRES 14 D 264 THR LEU CYS ILE GLY ALA ALA ALA PHE SER HIS TYR GLU
SEQRES 15 D 264 HIS TRP THR PHE PHE GLN ALA TYR TYR TYR CYS PHE ILE
SEQRES 16 D 264 THR LEU THR THR ILE GLY PHE GLY ASP TYR VAL ALA LEU
SEQRES 17 D 264 GLN LYS ASP GLN ALA LEU GLN THR GLN PRO GLN TYR VAL
SEQRES 18 D 264 ALA PHE SER PHE VAL TYR ILE LEU THR GLY LEU THR VAL
SEQRES 19 D 264 ILE GLY ALA PHE LEU ASN LEU VAL VAL LEU ARG PHE MET
SEQRES 20 D 264 THR MET ASN ALA GLU ASP GLU LYS ARG ASP ALA GLU ASN
SEQRES 21 D 264 LEU TYR PHE GLN
HET K A 302 1
HET K A 303 1
HET K A 304 1
HET Y01 A 305 35
HET Y01 A 306 35
HET KKZ A 307 36
HET PC1 A 308 38
HET K A 309 1
HET Y01 A 301 35
HET Y01 B 302 35
HET PC1 B 303 18
HET K C 302 1
HET K C 303 1
HET K C 304 1
HET PC1 C 305 21
HET PC1 C 306 38
HET K C 307 1
HET Y01 C 308 35
HET KKZ D 302 36
HET Y01 D 303 35
HETNAM K POTASSIUM ION
HETNAM Y01 CHOLESTEROL HEMISUCCINATE
HETNAM KKZ [4-[[2-(4-CHLOROPHENYL)IMIDAZO[1,2-A]PYRIDIN-3-
HETNAM 2 KKZ YL]METHYL]PIPERAZIN-1-YL]-[6-(TRIFLUOROMETHYLOXY)
HETNAM 3 KKZ PYRIDIN-2-YL]METHANONE
HETNAM PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETSYN PC1 3-SN-PHOSPHATIDYLCHOLINE
FORMUL 5 K 8(K 1+)
FORMUL 8 Y01 6(C31 H50 O4)
FORMUL 10 KKZ 2(C25 H21 CL F3 N5 O2)
FORMUL 11 PC1 4(C44 H88 N O8 P)
HELIX 1 AA1 LYS A 2 TYR A 52 1 51
HELIX 2 AA2 SER A 55 ALA A 74 1 20
HELIX 3 AA3 ARG A 79 THR A 92 1 14
HELIX 4 AA4 THR A 103 GLY A 148 1 46
HELIX 5 AA5 SER A 155 GLU A 182 1 28
HELIX 6 AA6 THR A 185 THR A 198 1 14
HELIX 7 AA7 GLN A 212 GLN A 217 1 6
HELIX 8 AA8 GLN A 217 VAL A 242 1 26
HELIX 9 AA9 VAL A 243 MET A 247 5 5
HELIX 10 AB1 THR A 248 ALA A 258 1 11
HELIX 11 AB2 LYS B 2 TYR B 52 1 51
HELIX 12 AB3 SER B 55 ALA B 74 1 20
HELIX 13 AB4 ARG B 79 THR B 92 1 14
HELIX 14 AB5 THR B 103 GLY B 148 1 46
HELIX 15 AB6 SER B 155 GLU B 182 1 28
HELIX 16 AB7 THR B 185 THR B 198 1 14
HELIX 17 AB8 GLN B 212 GLN B 217 1 6
HELIX 18 AB9 GLN B 217 VAL B 242 1 26
HELIX 19 AC1 VAL B 243 MET B 247 5 5
HELIX 20 AC2 THR B 248 LEU B 261 1 14
HELIX 21 AC3 LYS C 2 TYR C 52 1 51
HELIX 22 AC4 SER C 55 ALA C 74 1 20
HELIX 23 AC5 ARG C 79 THR C 92 1 14
HELIX 24 AC6 THR C 103 GLY C 148 1 46
HELIX 25 AC7 SER C 155 GLU C 182 1 28
HELIX 26 AC8 THR C 185 THR C 198 1 14
HELIX 27 AC9 GLN C 212 GLN C 217 1 6
HELIX 28 AD1 GLN C 217 VAL C 242 1 26
HELIX 29 AD2 VAL C 243 MET C 247 5 5
HELIX 30 AD3 THR C 248 ASP C 257 1 10
HELIX 31 AD4 LYS D 2 TYR D 52 1 51
HELIX 32 AD5 SER D 55 ALA D 74 1 20
HELIX 33 AD6 ARG D 79 THR D 92 1 14
HELIX 34 AD7 THR D 103 GLY D 148 1 46
HELIX 35 AD8 SER D 155 GLU D 182 1 28
HELIX 36 AD9 THR D 185 THR D 198 1 14
HELIX 37 AE1 GLN D 212 GLN D 217 1 6
HELIX 38 AE2 GLN D 217 VAL D 242 1 26
HELIX 39 AE3 VAL D 243 MET D 247 5 5
HELIX 40 AE4 THR D 248 LEU D 261 1 14
LINK O THR A 93 K K A 304 1555 1555 2.86
LINK O THR A 93 K K A 303 1555 1555 2.70
LINK OG1 THR A 93 K K A 304 1555 1555 2.81
LINK O ILE A 94 K K A 302 1555 1555 2.66
LINK O ILE A 94 K K A 303 1555 1555 2.74
LINK O GLY A 95 K K A 309 1555 1555 2.79
LINK O GLY A 95 K K A 302 1555 1555 2.73
LINK O TYR A 96 K K A 309 1555 1555 2.84
LINK O THR A 199 K K A 304 1555 1555 2.83
LINK O THR A 199 K K A 303 1555 1555 2.69
LINK OG1 THR A 199 K K A 304 1555 1555 2.84
LINK O ILE A 200 K K A 302 1555 1555 2.69
LINK O ILE A 200 K K A 303 1555 1555 2.81
LINK O GLY A 201 K K A 309 1555 1555 2.79
LINK O GLY A 201 K K A 302 1555 1555 2.63
LINK O PHE A 202 K K A 309 1555 1555 2.85
LINK O THR B 93 K K A 304 1555 1555 2.87
LINK O THR B 93 K K A 303 1555 1555 2.68
LINK OG1 THR B 93 K K A 304 1555 1555 2.79
LINK O ILE B 94 K K A 302 1555 1555 2.76
LINK O ILE B 94 K K A 303 1555 1555 2.73
LINK O GLY B 95 K K A 309 1555 1555 2.85
LINK O GLY B 95 K K A 302 1555 1555 2.77
LINK O TYR B 96 K K A 309 1555 1555 2.85
LINK O THR B 199 K K A 304 1555 1555 2.94
LINK O THR B 199 K K A 303 1555 1555 2.70
LINK OG1 THR B 199 K K A 304 1555 1555 2.98
LINK O ILE B 200 K K A 302 1555 1555 2.78
LINK O ILE B 200 K K A 303 1555 1555 2.81
LINK O GLY B 201 K K A 309 1555 1555 2.69
LINK O GLY B 201 K K A 302 1555 1555 2.76
LINK O PHE B 202 K K A 309 1555 1555 2.76
LINK O THR C 93 K K C 303 1555 1555 2.68
LINK O THR C 93 K K C 304 1555 1555 2.85
LINK OG1 THR C 93 K K C 304 1555 1555 2.82
LINK O ILE C 94 K K C 302 1555 1555 2.67
LINK O ILE C 94 K K C 303 1555 1555 2.70
LINK O GLY C 95 K K C 302 1555 1555 2.73
LINK O GLY C 95 K K C 307 1555 1555 2.79
LINK O TYR C 96 K K C 307 1555 1555 2.82
LINK O THR C 199 K K C 303 1555 1555 2.69
LINK O THR C 199 K K C 304 1555 1555 2.83
LINK OG1 THR C 199 K K C 304 1555 1555 2.86
LINK O ILE C 200 K K C 302 1555 1555 2.71
LINK O ILE C 200 K K C 303 1555 1555 2.81
LINK O GLY C 201 K K C 302 1555 1555 2.65
LINK O GLY C 201 K K C 307 1555 1555 2.76
LINK O PHE C 202 K K C 307 1555 1555 2.83
LINK O THR D 93 K K C 303 1555 1555 2.72
LINK O THR D 93 K K C 304 1555 1555 2.83
LINK OG1 THR D 93 K K C 304 1555 1555 2.78
LINK O ILE D 94 K K C 302 1555 1555 2.76
LINK O ILE D 94 K K C 303 1555 1555 2.76
LINK O GLY D 95 K K C 302 1555 1555 2.72
LINK O GLY D 95 K K C 307 1555 1555 2.87
LINK O TYR D 96 K K C 307 1555 1555 2.84
LINK O THR D 199 K K C 303 1555 1555 2.74
LINK O THR D 199 K K C 304 1555 1555 2.92
LINK OG1 THR D 199 K K C 304 1555 1555 2.97
LINK O ILE D 200 K K C 302 1555 1555 2.80
LINK O ILE D 200 K K C 303 1555 1555 2.82
LINK O GLY D 201 K K C 302 1555 1555 2.75
LINK O GLY D 201 K K C 307 1555 1555 2.78
LINK O PHE D 202 K K C 307 1555 1555 2.79
SITE 1 AC1 10 ILE A 94 GLY A 95 ILE A 200 GLY A 201
SITE 2 AC1 10 K A 303 K A 309 ILE B 94 GLY B 95
SITE 3 AC1 10 ILE B 200 GLY B 201
SITE 1 AC2 10 THR A 93 ILE A 94 THR A 199 ILE A 200
SITE 2 AC2 10 K A 302 K A 304 THR B 93 ILE B 94
SITE 3 AC2 10 THR B 199 ILE B 200
SITE 1 AC3 5 THR A 93 THR A 199 K A 303 THR B 93
SITE 2 AC3 5 THR B 199
SITE 1 AC4 5 ARG A 3 PHE A 238 PHE A 246 LEU B 115
SITE 2 AC4 5 PRO B 119
SITE 1 AC5 5 ARG A 79 PHE A 80 ALA A 81 GLN A 215
SITE 2 AC5 5 PHE B 16
SITE 1 AC6 20 THR A 92 ILE A 118 LEU A 122 PHE A 125
SITE 2 AC6 20 LEU A 197 THR A 198 THR A 199 LEU A 232
SITE 3 AC6 20 ILE A 235 LEU A 239 THR B 92 THR B 93
SITE 4 AC6 20 ILE B 118 LEU B 122 LEU B 197 THR B 198
SITE 5 AC6 20 THR B 199 LEU B 232 ILE B 235 LEU B 239
SITE 1 AC7 3 PHE A 112 SER A 169 HIS A 180
SITE 1 AC8 9 GLY A 95 TYR A 96 GLY A 201 PHE A 202
SITE 2 AC8 9 K A 302 GLY B 95 TYR B 96 GLY B 201
SITE 3 AC8 9 PHE B 202
SITE 1 AC9 5 LEU A 115 ARG B 3 ARG B 7 PHE B 238
SITE 2 AC9 5 PHE B 246
SITE 1 AD1 5 PHE A 16 ARG B 79 PHE B 80 ALA B 81
SITE 2 AD1 5 GLN B 215
SITE 1 AD2 2 SER B 169 HIS B 180
SITE 1 AD3 10 ILE C 94 GLY C 95 ILE C 200 GLY C 201
SITE 2 AD3 10 K C 303 K C 307 ILE D 94 GLY D 95
SITE 3 AD3 10 ILE D 200 GLY D 201
SITE 1 AD4 10 THR C 93 ILE C 94 THR C 199 ILE C 200
SITE 2 AD4 10 K C 302 K C 304 THR D 93 ILE D 94
SITE 3 AD4 10 THR D 199 ILE D 200
SITE 1 AD5 5 THR C 93 THR C 199 K C 303 THR D 93
SITE 2 AD5 5 THR D 199
SITE 1 AD6 3 PHE C 112 SER C 169 HIS C 180
SITE 1 AD7 5 ALA C 28 PHE D 112 SER D 169 ALA D 176
SITE 2 AD7 5 HIS D 180
SITE 1 AD8 9 GLY C 95 TYR C 96 GLY C 201 PHE C 202
SITE 2 AD8 9 K C 302 GLY D 95 TYR D 96 GLY D 201
SITE 3 AD8 9 PHE D 202
SITE 1 AD9 4 PHE C 238 PHE C 246 LEU D 115 PRO D 119
SITE 1 AE1 20 THR C 92 ILE C 118 LEU C 122 PHE C 125
SITE 2 AE1 20 LEU C 197 THR C 198 THR C 199 LEU C 232
SITE 3 AE1 20 ILE C 235 LEU C 239 THR D 92 THR D 93
SITE 4 AE1 20 ILE D 118 LEU D 122 LEU D 197 THR D 198
SITE 5 AE1 20 THR D 199 LEU D 232 ILE D 235 LEU D 239
SITE 1 AE2 4 LEU C 115 ARG D 3 PHE D 238 PHE D 246
CRYST1 45.100 201.330 238.570 90.00 90.00 90.00 P 2 21 21 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 0.022173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004967 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004192 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
