HEADER METAL TRANSPORT 18-JUL-11 3SYQ
TITLE CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+ CHANNEL
TITLE 2 GIRK2 (KIR3.2) R201A MUTANT IN COMPLEX WITH PIP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 52-380;
COMPND 5 SYNONYM: GIRK-2, INWARD RECTIFIER K(+) CHANNEL KIR3.2, POTASSIUM
COMPND 6 CHANNEL, INWARDLY RECTIFYING SUBFAMILY J MEMBER 6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GIRK2, KCNJ6, KCNJ7, W;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMD1163;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZ
KEYWDS ION CHANNEL, POTASSIUM CHANNEL, INWARD RECTIFICATION, SODIUM BINDING,
KEYWDS 2 PIP2 BINDING, G PROTEIN BINDING, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.WHORTON,R.MACKINNON
REVDAT 2 13-SEP-23 3SYQ 1 REMARK SEQADV LINK
REVDAT 1 12-OCT-11 3SYQ 0
JRNL AUTH M.R.WHORTON,R.MACKINNON
JRNL TITL CRYSTAL STRUCTURE OF THE MAMMALIAN GIRK2 K(+) CHANNEL AND
JRNL TITL 2 GATING REGULATION BY G PROTEINS, PIP(2), AND SODIUM.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 147 199 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 21962516
JRNL DOI 10.1016/J.CELL.2011.07.046
REMARK 2
REMARK 2 RESOLUTION. 3.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.5
REMARK 3 NUMBER OF REFLECTIONS : 11814
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) : 0.301
REMARK 3 R VALUE (WORKING SET) : 0.300
REMARK 3 FREE R VALUE : 0.323
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 575
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 7.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.4570
REMARK 3 BIN FREE R VALUE SET COUNT : 4
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
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) : 138.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.18000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.770
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.780
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 112.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.842
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4619 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6290 ; 1.019 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 578 ; 5.281 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 179 ;36.317 ;23.575
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 728 ;17.508 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.003 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 746 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3385 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2901 ; 0.257 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4658 ; 0.477 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1718 ; 0.452 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1632 ; 0.820 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 100 A 179 1
REMARK 3 1 B 100 B 179 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 477 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 477 ; 0.010 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 203 A 225 4
REMARK 3 1 B 203 B 225 4
REMARK 3 2 A 238 A 244 4
REMARK 3 2 B 238 B 244 4
REMARK 3 3 A 260 A 308 4
REMARK 3 3 B 260 B 308 4
REMARK 3 4 A 325 A 382 6
REMARK 3 4 B 325 B 382 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 621 ; 0.360 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 A (A): 378 ; 0.330 ; 5.000
REMARK 3 MEDIUM THERMAL 2 A (A**2): 621 ; 1.460 ; 2.000
REMARK 3 LOOSE THERMAL 2 A (A**2): 378 ; 0.910 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 55 A 377
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4154 33.0676 -16.7333
REMARK 3 T TENSOR
REMARK 3 T11: 0.6048 T22: 0.8337
REMARK 3 T33: 0.6430 T12: 0.1066
REMARK 3 T13: 0.3828 T23: -0.3558
REMARK 3 L TENSOR
REMARK 3 L11: 2.4271 L22: 7.8977
REMARK 3 L33: 2.7487 L12: 1.4746
REMARK 3 L13: 0.3614 L23: -1.0183
REMARK 3 S TENSOR
REMARK 3 S11: -0.4083 S12: -0.5336 S13: 0.1969
REMARK 3 S21: 1.1245 S22: -0.1470 S23: 0.9345
REMARK 3 S31: -0.3751 S32: -0.4722 S33: 0.5554
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 55 B 378
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9362 33.6209 -39.6322
REMARK 3 T TENSOR
REMARK 3 T11: 0.4934 T22: 0.7049
REMARK 3 T33: 0.5787 T12: 0.1844
REMARK 3 T13: -0.0566 T23: -0.1279
REMARK 3 L TENSOR
REMARK 3 L11: 1.1890 L22: 10.8280
REMARK 3 L33: 2.6777 L12: 0.0653
REMARK 3 L13: 0.1125 L23: 3.0247
REMARK 3 S TENSOR
REMARK 3 S11: 0.0655 S12: 0.1226 S13: 0.2935
REMARK 3 S21: -1.0134 S22: -0.5368 S23: 0.9212
REMARK 3 S31: -0.4641 S32: -0.4946 S33: 0.4713
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3SYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066818.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.25
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) : 1.034
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14690
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.432
REMARK 200 RESOLUTION RANGE LOW (A) : 49.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.96800
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2E4F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES SODIUM, PH 7.25, 0.5 M
REMARK 280 SODIUM CHLORIDE, 25% PEG400, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 58.68800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.68800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 43.80250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 104.24550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.80250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 104.24550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.68800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.80250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 104.24550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.68800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.80250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 104.24550
REMARK 290 SMTRY3 8 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
REMARK 350 TOTAL BURIED SURFACE AREA: 22320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 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 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 -58.68800
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 501 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 502 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 503 LIES ON A SPECIAL POSITION.
REMARK 375 K K A 504 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 50
REMARK 465 ALA A 51
REMARK 465 LYS A 52
REMARK 465 ARG A 53
REMARK 465 LYS A 54
REMARK 465 GLY A 70
REMARK 465 ASN A 71
REMARK 465 VAL A 72
REMARK 465 ARG A 73
REMARK 465 GLU A 74
REMARK 465 THR A 75
REMARK 465 TYR A 76
REMARK 465 ARG A 77
REMARK 465 TYR A 78
REMARK 465 LEU A 79
REMARK 465 THR A 80
REMARK 465 TYR A 118
REMARK 465 ILE A 119
REMARK 465 ARG A 120
REMARK 465 GLY A 121
REMARK 465 ASP A 122
REMARK 465 MET A 123
REMARK 465 ASP A 124
REMARK 465 HIS A 125
REMARK 465 ILE A 126
REMARK 465 GLU A 127
REMARK 465 ASP A 128
REMARK 465 PRO A 129
REMARK 465 SER A 130
REMARK 465 TRP A 131
REMARK 465 THR A 132
REMARK 465 PRO A 133
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 ASP A 346
REMARK 465 GLY A 347
REMARK 465 ARG A 378
REMARK 465 ALA A 379
REMARK 465 GLU A 380
REMARK 465 SER A 381
REMARK 465 ASN A 382
REMARK 465 SER A 383
REMARK 465 LEU A 384
REMARK 465 GLU A 385
REMARK 465 VAL A 386
REMARK 465 LEU A 387
REMARK 465 PHE A 388
REMARK 465 GLN A 389
REMARK 465 MET B 50
REMARK 465 ALA B 51
REMARK 465 LYS B 52
REMARK 465 ARG B 53
REMARK 465 LYS B 54
REMARK 465 VAL B 67
REMARK 465 HIS B 68
REMARK 465 HIS B 69
REMARK 465 GLY B 70
REMARK 465 ASN B 71
REMARK 465 VAL B 72
REMARK 465 ARG B 73
REMARK 465 GLU B 74
REMARK 465 THR B 75
REMARK 465 TYR B 76
REMARK 465 ARG B 77
REMARK 465 TYR B 78
REMARK 465 LEU B 79
REMARK 465 THR B 80
REMARK 465 ASP B 81
REMARK 465 TYR B 118
REMARK 465 ILE B 119
REMARK 465 ARG B 120
REMARK 465 GLY B 121
REMARK 465 ASP B 122
REMARK 465 MET B 123
REMARK 465 ASP B 124
REMARK 465 HIS B 125
REMARK 465 ILE B 126
REMARK 465 GLU B 127
REMARK 465 ASP B 128
REMARK 465 PRO B 129
REMARK 465 SER B 130
REMARK 465 TRP B 131
REMARK 465 THR B 132
REMARK 465 PRO B 133
REMARK 465 ALA B 379
REMARK 465 GLU B 380
REMARK 465 SER B 381
REMARK 465 ASN B 382
REMARK 465 SER B 383
REMARK 465 LEU B 384
REMARK 465 GLU B 385
REMARK 465 VAL B 386
REMARK 465 LEU B 387
REMARK 465 PHE B 388
REMARK 465 GLN B 389
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 60 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 88 CG OD1 OD2
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 MET A 111 CG SD CE
REMARK 470 LEU A 115 CG CD1 CD2
REMARK 470 ILE A 116 CG1 CG2 CD1
REMARK 470 VAL A 135 CG1 CG2
REMARK 470 ASN A 137 CG OD1 ND2
REMARK 470 LEU A 138 CG CD1 CD2
REMARK 470 ASN A 139 CG OD1 ND2
REMARK 470 VAL A 161 CG1 CG2
REMARK 470 ILE A 162 CG1 CG2 CD1
REMARK 470 THR A 163 OG1 CG2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 GLU A 168 CG CD OE1 OE2
REMARK 470 ILE A 170 CG1 CG2 CD1
REMARK 470 PHE A 186 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 ARG A 230 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 231 CG OD1 ND2
REMARK 470 LYS A 301 CG CD CE NZ
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 PHE A 348 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 349 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 350 CG CD OE1 OE2
REMARK 470 ILE B 55 CG1 CG2 CD1
REMARK 470 ASP B 88 CG OD1 OD2
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 ARG B 92 CG CD NE CZ NH1 NH2
REMARK 470 MET B 111 CG SD CE
REMARK 470 LEU B 115 CG CD1 CD2
REMARK 470 ILE B 116 CG1 CG2 CD1
REMARK 470 VAL B 135 CG1 CG2
REMARK 470 ASN B 137 CG OD1 ND2
REMARK 470 LEU B 138 CG CD1 CD2
REMARK 470 ASN B 139 CG OD1 ND2
REMARK 470 VAL B 161 CG1 CG2
REMARK 470 ILE B 162 CG1 CG2 CD1
REMARK 470 THR B 163 OG1 CG2
REMARK 470 LYS B 165 CG CD CE NZ
REMARK 470 GLU B 168 CG CD OE1 OE2
REMARK 470 ILE B 170 CG1 CG2 CD1
REMARK 470 PHE B 186 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 200 CG CD CE NZ
REMARK 470 HIS B 233 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 301 CG CD CE NZ
REMARK 470 GLU B 303 CG CD OE1 OE2
REMARK 470 GLU B 345 CG CD OE1 OE2
REMARK 470 GLU B 350 CG CD OE1 OE2
REMARK 470 GLU B 374 CG CD OE1 OE2
REMARK 470 ASN B 377 CG OD1 ND2
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 ASN A 66 49.90 -88.40
REMARK 500 LEU A 95 -37.49 -39.82
REMARK 500 ILE A 234 75.16 46.29
REMARK 500 LEU A 257 57.34 -114.35
REMARK 500 LYS A 301 35.42 -79.44
REMARK 500 GLU A 303 67.11 -103.02
REMARK 500 SER A 363 107.86 -58.61
REMARK 500 MET B 191 -78.81 -57.43
REMARK 500 SER B 232 98.71 -68.14
REMARK 500 ASP B 270 3.62 -67.51
REMARK 500 VAL B 276 -74.93 -113.13
REMARK 500 ASP B 346 80.33 52.65
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 PIO A 400
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 503 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 154 O
REMARK 620 2 ILE A 155 O 72.8
REMARK 620 3 THR B 154 O 71.7 99.3
REMARK 620 4 ILE B 155 O 124.6 76.0 69.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 154 OG1
REMARK 620 2 THR A 154 O 59.9
REMARK 620 3 THR B 154 O 111.3 75.5
REMARK 620 4 THR B 154 OG1 84.2 101.4 55.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 155 O
REMARK 620 2 GLY A 156 O 62.0
REMARK 620 3 ILE B 155 O 73.3 119.3
REMARK 620 4 GLY B 156 O 92.6 81.5 61.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 156 O
REMARK 620 2 TYR A 157 O 73.3
REMARK 620 3 GLY B 156 O 75.5 91.1
REMARK 620 4 TYR B 157 O 133.6 72.9 74.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIO A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SYA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+
REMARK 900 CHANNEL GIRK2 (KIR3.2) IN COMPLEX WITH SODIUM AND PIP2
REMARK 900 RELATED ID: 3SYC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+
REMARK 900 CHANNEL GIRK2 (KIR3.2) D228N MUTANT
REMARK 900 RELATED ID: 3SYO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+
REMARK 900 CHANNEL GIRK2 (KIR3.2) IN COMPLEX WITH SODIUM
REMARK 900 RELATED ID: 3SYP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE G PROTEIN-GATED INWARD RECTIFIER K+
REMARK 900 CHANNEL GIRK2 (KIR3.2) R201A MUTANT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNP P48542 S260T, I313M, AND M344L ARE NATURAL VARIANTS.
DBREF 3SYQ A 52 380 UNP P48542 IRK6_MOUSE 52 380
DBREF 3SYQ B 52 380 UNP P48542 IRK6_MOUSE 52 380
SEQADV 3SYQ MET A 50 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ALA A 51 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ALA A 201 UNP P48542 ARG 201 ENGINEERED MUTATION
SEQADV 3SYQ THR A 260 UNP P48542 SER 260 SEE REMARK 999
SEQADV 3SYQ MET A 313 UNP P48542 ILE 313 SEE REMARK 999
SEQADV 3SYQ LEU A 344 UNP P48542 MET 344 SEE REMARK 999
SEQADV 3SYQ SER A 381 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ASN A 382 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ SER A 383 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ LEU A 384 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ GLU A 385 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ VAL A 386 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ LEU A 387 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ PHE A 388 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ GLN A 389 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ MET B 50 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ALA B 51 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ALA B 201 UNP P48542 ARG 201 ENGINEERED MUTATION
SEQADV 3SYQ THR B 260 UNP P48542 SER 260 SEE REMARK 999
SEQADV 3SYQ MET B 313 UNP P48542 ILE 313 SEE REMARK 999
SEQADV 3SYQ LEU B 344 UNP P48542 MET 344 SEE REMARK 999
SEQADV 3SYQ SER B 381 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ ASN B 382 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ SER B 383 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ LEU B 384 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ GLU B 385 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ VAL B 386 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ LEU B 387 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ PHE B 388 UNP P48542 EXPRESSION TAG
SEQADV 3SYQ GLN B 389 UNP P48542 EXPRESSION TAG
SEQRES 1 A 340 MET ALA LYS ARG LYS ILE GLN ARG TYR VAL ARG LYS ASP
SEQRES 2 A 340 GLY LYS CYS ASN VAL HIS HIS GLY ASN VAL ARG GLU THR
SEQRES 3 A 340 TYR ARG TYR LEU THR ASP ILE PHE THR THR LEU VAL ASP
SEQRES 4 A 340 LEU LYS TRP ARG PHE ASN LEU LEU ILE PHE VAL MET VAL
SEQRES 5 A 340 TYR THR VAL THR TRP LEU PHE PHE GLY MET ILE TRP TRP
SEQRES 6 A 340 LEU ILE ALA TYR ILE ARG GLY ASP MET ASP HIS ILE GLU
SEQRES 7 A 340 ASP PRO SER TRP THR PRO CYS VAL THR ASN LEU ASN GLY
SEQRES 8 A 340 PHE VAL SER ALA PHE LEU PHE SER ILE GLU THR GLU THR
SEQRES 9 A 340 THR ILE GLY TYR GLY TYR ARG VAL ILE THR ASP LYS CYS
SEQRES 10 A 340 PRO GLU GLY ILE ILE LEU LEU LEU ILE GLN SER VAL LEU
SEQRES 11 A 340 GLY SER ILE VAL ASN ALA PHE MET VAL GLY CYS MET PHE
SEQRES 12 A 340 VAL LYS ILE SER GLN PRO LYS LYS ALA ALA GLU THR LEU
SEQRES 13 A 340 VAL PHE SER THR HIS ALA VAL ILE SER MET ARG ASP GLY
SEQRES 14 A 340 LYS LEU CYS LEU MET PHE ARG VAL GLY ASP LEU ARG ASN
SEQRES 15 A 340 SER HIS ILE VAL GLU ALA SER ILE ARG ALA LYS LEU ILE
SEQRES 16 A 340 LYS SER LYS GLN THR SER GLU GLY GLU PHE ILE PRO LEU
SEQRES 17 A 340 ASN GLN THR ASP ILE ASN VAL GLY TYR TYR THR GLY ASP
SEQRES 18 A 340 ASP ARG LEU PHE LEU VAL SER PRO LEU ILE ILE SER HIS
SEQRES 19 A 340 GLU ILE ASN GLN GLN SER PRO PHE TRP GLU ILE SER LYS
SEQRES 20 A 340 ALA GLN LEU PRO LYS GLU GLU LEU GLU ILE VAL VAL ILE
SEQRES 21 A 340 LEU GLU GLY MET VAL GLU ALA THR GLY MET THR CYS GLN
SEQRES 22 A 340 ALA ARG SER SER TYR ILE THR SER GLU ILE LEU TRP GLY
SEQRES 23 A 340 TYR ARG PHE THR PRO VAL LEU THR LEU GLU ASP GLY PHE
SEQRES 24 A 340 TYR GLU VAL ASP TYR ASN SER PHE HIS GLU THR TYR GLU
SEQRES 25 A 340 THR SER THR PRO SER LEU SER ALA LYS GLU LEU ALA GLU
SEQRES 26 A 340 LEU ALA ASN ARG ALA GLU SER ASN SER LEU GLU VAL LEU
SEQRES 27 A 340 PHE GLN
SEQRES 1 B 340 MET ALA LYS ARG LYS ILE GLN ARG TYR VAL ARG LYS ASP
SEQRES 2 B 340 GLY LYS CYS ASN VAL HIS HIS GLY ASN VAL ARG GLU THR
SEQRES 3 B 340 TYR ARG TYR LEU THR ASP ILE PHE THR THR LEU VAL ASP
SEQRES 4 B 340 LEU LYS TRP ARG PHE ASN LEU LEU ILE PHE VAL MET VAL
SEQRES 5 B 340 TYR THR VAL THR TRP LEU PHE PHE GLY MET ILE TRP TRP
SEQRES 6 B 340 LEU ILE ALA TYR ILE ARG GLY ASP MET ASP HIS ILE GLU
SEQRES 7 B 340 ASP PRO SER TRP THR PRO CYS VAL THR ASN LEU ASN GLY
SEQRES 8 B 340 PHE VAL SER ALA PHE LEU PHE SER ILE GLU THR GLU THR
SEQRES 9 B 340 THR ILE GLY TYR GLY TYR ARG VAL ILE THR ASP LYS CYS
SEQRES 10 B 340 PRO GLU GLY ILE ILE LEU LEU LEU ILE GLN SER VAL LEU
SEQRES 11 B 340 GLY SER ILE VAL ASN ALA PHE MET VAL GLY CYS MET PHE
SEQRES 12 B 340 VAL LYS ILE SER GLN PRO LYS LYS ALA ALA GLU THR LEU
SEQRES 13 B 340 VAL PHE SER THR HIS ALA VAL ILE SER MET ARG ASP GLY
SEQRES 14 B 340 LYS LEU CYS LEU MET PHE ARG VAL GLY ASP LEU ARG ASN
SEQRES 15 B 340 SER HIS ILE VAL GLU ALA SER ILE ARG ALA LYS LEU ILE
SEQRES 16 B 340 LYS SER LYS GLN THR SER GLU GLY GLU PHE ILE PRO LEU
SEQRES 17 B 340 ASN GLN THR ASP ILE ASN VAL GLY TYR TYR THR GLY ASP
SEQRES 18 B 340 ASP ARG LEU PHE LEU VAL SER PRO LEU ILE ILE SER HIS
SEQRES 19 B 340 GLU ILE ASN GLN GLN SER PRO PHE TRP GLU ILE SER LYS
SEQRES 20 B 340 ALA GLN LEU PRO LYS GLU GLU LEU GLU ILE VAL VAL ILE
SEQRES 21 B 340 LEU GLU GLY MET VAL GLU ALA THR GLY MET THR CYS GLN
SEQRES 22 B 340 ALA ARG SER SER TYR ILE THR SER GLU ILE LEU TRP GLY
SEQRES 23 B 340 TYR ARG PHE THR PRO VAL LEU THR LEU GLU ASP GLY PHE
SEQRES 24 B 340 TYR GLU VAL ASP TYR ASN SER PHE HIS GLU THR TYR GLU
SEQRES 25 B 340 THR SER THR PRO SER LEU SER ALA LYS GLU LEU ALA GLU
SEQRES 26 B 340 LEU ALA ASN ARG ALA GLU SER ASN SER LEU GLU VAL LEU
SEQRES 27 B 340 PHE GLN
HET PIO A 400 31
HET K A 501 1
HET K A 502 1
HET K A 503 1
HET K A 504 1
HETNAM PIO [(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,
HETNAM 2 PIO 3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-
HETNAM 3 PIO PHOSPHORYL]OXY-PROPYL] OCTANOATE
HETNAM K POTASSIUM ION
HETSYN PIO DIOCTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-
HETSYN 2 PIO DIPHOSPHATE
FORMUL 3 PIO C25 H49 O19 P3
FORMUL 4 K 4(K 1+)
HELIX 1 1 ILE A 82 ASP A 88 1 7
HELIX 2 2 LYS A 90 ILE A 116 1 27
HELIX 3 3 GLY A 140 THR A 153 1 14
HELIX 4 4 CYS A 166 GLN A 197 1 32
HELIX 5 5 SER A 368 ASN A 377 1 10
HELIX 6 6 ILE B 82 LEU B 89 1 8
HELIX 7 7 LYS B 90 ILE B 116 1 27
HELIX 8 8 GLY B 140 THR B 153 1 14
HELIX 9 9 CYS B 166 SER B 196 1 31
HELIX 10 10 SER B 368 ARG B 378 1 11
SHEET 1 A 3 LEU A 205 PHE A 207 0
SHEET 2 A 3 LYS A 219 ASP A 228 -1 O GLY A 227 N VAL A 206
SHEET 3 A 3 LEU A 279 GLU A 284 -1 O HIS A 283 N LEU A 222
SHEET 1 B 4 LEU A 205 PHE A 207 0
SHEET 2 B 4 LYS A 219 ASP A 228 -1 O GLY A 227 N VAL A 206
SHEET 3 B 4 ALA A 211 ARG A 216 -1 N ARG A 216 O LYS A 219
SHEET 4 B 4 ILE A 332 TRP A 334 1 O LEU A 333 N ALA A 211
SHEET 1 C 3 PHE A 254 ILE A 262 0
SHEET 2 C 3 GLU A 236 GLN A 248 -1 N LYS A 247 O ILE A 255
SHEET 3 C 3 ARG A 272 PHE A 274 -1 O LEU A 273 N ALA A 237
SHEET 1 D 4 PHE A 254 ILE A 262 0
SHEET 2 D 4 GLU A 236 GLN A 248 -1 N LYS A 247 O ILE A 255
SHEET 3 D 4 LEU A 304 MET A 313 -1 O GLU A 305 N ILE A 244
SHEET 4 D 4 THR A 320 ILE A 328 -1 O TYR A 327 N ILE A 306
SHEET 1 E 2 TYR A 336 PHE A 338 0
SHEET 2 E 2 THR A 359 GLU A 361 -1 O TYR A 360 N ARG A 337
SHEET 1 F 2 LEU A 342 THR A 343 0
SHEET 2 F 2 GLU A 350 VAL A 351 -1 O GLU A 350 N THR A 343
SHEET 1 G 3 LEU B 205 PHE B 207 0
SHEET 2 G 3 LYS B 219 ASP B 228 -1 O GLY B 227 N VAL B 206
SHEET 3 G 3 LEU B 279 GLU B 284 -1 O HIS B 283 N LEU B 222
SHEET 1 H 4 LEU B 205 PHE B 207 0
SHEET 2 H 4 LYS B 219 ASP B 228 -1 O GLY B 227 N VAL B 206
SHEET 3 H 4 ALA B 211 ARG B 216 -1 N SER B 214 O CYS B 221
SHEET 4 H 4 ILE B 332 TRP B 334 1 O LEU B 333 N ALA B 211
SHEET 1 I 4 ILE B 234 VAL B 235 0
SHEET 2 I 4 LEU B 304 VAL B 314 -1 O MET B 313 N VAL B 235
SHEET 3 I 4 ILE B 239 LYS B 245 -1 N ILE B 244 O GLU B 305
SHEET 4 I 4 GLN B 259 ILE B 262 -1 O ILE B 262 N ALA B 241
SHEET 1 J 3 ILE B 234 VAL B 235 0
SHEET 2 J 3 LEU B 304 VAL B 314 -1 O MET B 313 N VAL B 235
SHEET 3 J 3 THR B 320 ILE B 328 -1 O SER B 325 N VAL B 308
SHEET 1 K 2 LYS B 247 GLN B 248 0
SHEET 2 K 2 PHE B 254 ILE B 255 -1 O ILE B 255 N LYS B 247
SHEET 1 L 2 TYR B 336 PHE B 338 0
SHEET 2 L 2 THR B 359 GLU B 361 -1 O TYR B 360 N ARG B 337
SHEET 1 M 2 LEU B 342 LEU B 344 0
SHEET 2 M 2 TYR B 349 VAL B 351 -1 O GLU B 350 N THR B 343
SSBOND 1 CYS A 134 CYS A 166 1555 1555 2.03
SSBOND 2 CYS B 134 CYS B 166 1555 1555 2.03
LINK O THR A 154 K K A 503 1555 1555 2.82
LINK OG1 THR A 154 K K A 504 1555 1555 2.72
LINK O THR A 154 K K A 504 1555 1555 2.87
LINK O ILE A 155 K K A 502 1555 1555 2.75
LINK O ILE A 155 K K A 503 1555 1555 2.82
LINK O GLY A 156 K K A 501 1555 1555 2.99
LINK O GLY A 156 K K A 502 1555 1555 2.92
LINK O TYR A 157 K K A 501 1555 1555 3.46
LINK K K A 501 O GLY B 156 1555 1555 3.11
LINK K K A 501 O TYR B 157 1555 1555 3.25
LINK K K A 502 O ILE B 155 1555 1555 3.00
LINK K K A 502 O GLY B 156 1555 1555 2.81
LINK K K A 503 O THR B 154 1555 1555 3.12
LINK K K A 503 O ILE B 155 1555 1555 2.77
LINK K K A 504 O THR B 154 1555 1555 2.82
LINK K K A 504 OG1 THR B 154 1555 1555 3.01
SITE 1 AC1 4 LYS A 90 TRP A 91 ARG A 92 LYS A 194
SITE 1 AC2 5 GLY A 156 TYR A 157 K A 502 GLY B 156
SITE 2 AC2 5 TYR B 157
SITE 1 AC3 6 ILE A 155 GLY A 156 K A 501 K A 503
SITE 2 AC3 6 ILE B 155 GLY B 156
SITE 1 AC4 6 THR A 154 ILE A 155 K A 502 K A 504
SITE 2 AC4 6 THR B 154 ILE B 155
SITE 1 AC5 3 THR A 154 K A 503 THR B 154
CRYST1 87.605 208.491 117.376 90.00 90.00 90.00 C 2 2 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 0.011415 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008520 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
