HEADER METAL TRANSPORT 01-JUL-11 3SPJ
TITLE APO INWARD RECTIFIER POTASSIUM CHANNEL KIR2.2 I223L MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INWARD-RECTIFIER K+ CHANNEL KIR2.2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INWARD RECTIFIER POTASSIUM CHANNEL 2.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: KIR2.2;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS PIP, MEMBRANE PROTEIN, LIPID, RECEPTOR, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.B.HANSEN,X.TAO,R.MACKINNON
REVDAT 3 13-SEP-23 3SPJ 1 REMARK SEQADV LINK
REVDAT 2 21-SEP-11 3SPJ 1 JRNL
REVDAT 1 24-AUG-11 3SPJ 0
JRNL AUTH S.B.HANSEN,X.TAO,R.MACKINNON
JRNL TITL STRUCTURAL BASIS OF PIP(2) ACTIVATION OF THE CLASSICAL
JRNL TITL 2 INWARD RECTIFIER K(+) CHANNEL KIR2.2.
JRNL REF NATURE V. 477 495 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 21874019
JRNL DOI 10.1038/NATURE10370
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 9689
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 465
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 28.3650 - 4.7646 0.97 3144 150 0.2476 0.2661
REMARK 3 2 4.7646 - 3.7847 0.98 3129 176 0.1916 0.2480
REMARK 3 3 3.7847 - 3.3071 0.92 2951 139 0.2742 0.3188
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 97.95
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.730
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) : -4.53380
REMARK 3 B22 (A**2) : -4.53380
REMARK 3 B33 (A**2) : 9.06770
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 : 0.008 2636
REMARK 3 ANGLE : 0.877 3521
REMARK 3 CHIRALITY : 0.060 401
REMARK 3 PLANARITY : 0.003 447
REMARK 3 DIHEDRAL : 15.717 939
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 70:188))
REMARK 3 ORIGIN FOR THE GROUP (A): -10.6839 7.8013 -36.7186
REMARK 3 T TENSOR
REMARK 3 T11: 1.0177 T22: 1.1536
REMARK 3 T33: 1.3160 T12: 0.1628
REMARK 3 T13: 0.2088 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 4.3560 L22: 4.3391
REMARK 3 L33: 1.9814 L12: -0.6029
REMARK 3 L13: 1.1602 L23: 2.5192
REMARK 3 S TENSOR
REMARK 3 S11: 0.4504 S12: 0.2265 S13: 0.6370
REMARK 3 S21: 0.3073 S22: 0.0342 S23: 0.4046
REMARK 3 S31: -1.1527 S32: -0.9040 S33: 0.0003
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 43:60) OR (RESSEQ 189:372))
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5380 -17.0483 21.6646
REMARK 3 T TENSOR
REMARK 3 T11: 1.2986 T22: 1.2016
REMARK 3 T33: 0.9896 T12: -0.1690
REMARK 3 T13: -0.0505 T23: -0.1196
REMARK 3 L TENSOR
REMARK 3 L11: 4.8185 L22: 4.4971
REMARK 3 L33: 2.1520 L12: -0.0499
REMARK 3 L13: 0.6552 L23: -0.0406
REMARK 3 S TENSOR
REMARK 3 S11: 0.0930 S12: 0.2234 S13: -0.5478
REMARK 3 S21: -0.4461 S22: -0.0786 S23: 0.3308
REMARK 3 S31: 0.6454 S32: -0.2855 S33: 0.0000
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 3SPJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10028
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.01180
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.05260
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3SPH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10.62% PEG400, 0.5 M SODIUM CHLORIDE,
REMARK 280 0.05 M HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 41.88450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.88450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 98.56300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.88450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.88450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 98.56300
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 41.88450
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 41.88450
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 98.56300
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 41.88450
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 41.88450
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 98.56300
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: 22460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 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 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 375 K K A 505 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 36
REMARK 465 ALA A 37
REMARK 465 ARG A 38
REMARK 465 ARG A 39
REMARK 465 LYS A 40
REMARK 465 CYS A 41
REMARK 465 ARG A 42
REMARK 465 ASP A 61
REMARK 465 LYS A 62
REMARK 465 PRO A 63
REMARK 465 GLN A 64
REMARK 465 ARG A 65
REMARK 465 TYR A 66
REMARK 465 ILE A 67
REMARK 465 ALA A 68
REMARK 465 ASP A 69
REMARK 465 LEU A 373
REMARK 465 GLU A 374
REMARK 465 VAL A 375
REMARK 465 LEU A 376
REMARK 465 PHE A 377
REMARK 465 GLN A 378
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 MET A 70 CG SD CE
REMARK 470 PHE A 71 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 72 OG1 CG2
REMARK 470 THR A 73 OG1 CG2
REMARK 470 CYS A 74 SG
REMARK 470 VAL A 75 CG1 CG2
REMARK 470 ASP A 76 CG OD1 OD2
REMARK 470 ILE A 77 CG1 CG2 CD1
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 79 -78.41 -82.79
REMARK 500 MET A 181 -61.42 -91.97
REMARK 500 ARG A 186 68.11 -156.84
REMARK 500 LYS A 189 67.43 61.31
REMARK 500 VAL A 265 -73.72 -113.85
REMARK 500 LYS A 335 -112.37 50.43
REMARK 500 SER A 370 -63.16 -99.28
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 503 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 143 O
REMARK 620 2 ILE A 144 O 71.0
REMARK 620 N 1
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 143 OG1
REMARK 620 2 THR A 143 O 58.5
REMARK 620 N 1
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 144 O
REMARK 620 2 GLY A 145 O 71.1
REMARK 620 N 1
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 145 O
REMARK 620 2 TYR A 146 O 67.9
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
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: 3SPC RELATED DB: PDB
REMARK 900 KIR2.2 IN COMPLEX WITH DIOCTANOYLGLYCEROL PYROPHOSPHATE (DGPP)
REMARK 900 RELATED ID: 3SPG RELATED DB: PDB
REMARK 900 KIR2.2 R186A MUTANT IN COMPLEX WITH PIP2
REMARK 900 RELATED ID: 3SPH RELATED DB: PDB
REMARK 900 KIR2.2 I223L MUTANT IN COMPLEX WITH PIP2
REMARK 900 RELATED ID: 3SPI RELATED DB: PDB
REMARK 900 KIR2.2 IN COMPLEX WITH PIP2
DBREF 3SPJ A 36 378 UNP D2YW45 D2YW45_CHICK 1 343
SEQADV 3SPJ LEU A 223 UNP D2YW45 ILE 188 ENGINEERED MUTATION
SEQRES 1 A 343 MET ALA ARG ARG LYS CYS ARG ASN ARG PHE VAL LYS LYS
SEQRES 2 A 343 ASN GLY GLN CYS ASN VAL GLU PHE THR ASN MET ASP ASP
SEQRES 3 A 343 LYS PRO GLN ARG TYR ILE ALA ASP MET PHE THR THR CYS
SEQRES 4 A 343 VAL ASP ILE ARG TRP ARG TYR MET LEU LEU LEU PHE SER
SEQRES 5 A 343 LEU ALA PHE LEU VAL SER TRP LEU LEU PHE GLY LEU ILE
SEQRES 6 A 343 PHE TRP LEU ILE ALA LEU ILE HIS GLY ASP LEU GLU ASN
SEQRES 7 A 343 PRO GLY GLY ASP ASP THR PHE LYS PRO CYS VAL LEU GLN
SEQRES 8 A 343 VAL ASN GLY PHE VAL ALA ALA PHE LEU PHE SER ILE GLU
SEQRES 9 A 343 THR GLN THR THR ILE GLY TYR GLY PHE ARG CYS VAL THR
SEQRES 10 A 343 GLU GLU CYS PRO LEU ALA VAL PHE MET VAL VAL VAL GLN
SEQRES 11 A 343 SER ILE VAL GLY CYS ILE ILE ASP SER PHE MET ILE GLY
SEQRES 12 A 343 ALA ILE MET ALA LYS MET ALA ARG PRO LYS LYS ARG ALA
SEQRES 13 A 343 GLN THR LEU LEU PHE SER HIS ASN ALA VAL VAL ALA MET
SEQRES 14 A 343 ARG ASP GLY LYS LEU CYS LEU MET TRP ARG VAL GLY ASN
SEQRES 15 A 343 LEU ARG LYS SER HIS LEU VAL GLU ALA HIS VAL ARG ALA
SEQRES 16 A 343 GLN LEU ILE LYS PRO ARG ILE THR GLU GLU GLY GLU TYR
SEQRES 17 A 343 ILE PRO LEU ASP GLN ILE ASP ILE ASP VAL GLY PHE ASP
SEQRES 18 A 343 LYS GLY LEU ASP ARG ILE PHE LEU VAL SER PRO ILE THR
SEQRES 19 A 343 ILE LEU HIS GLU ILE ASN GLU ASP SER PRO LEU PHE GLY
SEQRES 20 A 343 ILE SER ARG GLN ASP LEU GLU THR ASP ASP PHE GLU ILE
SEQRES 21 A 343 VAL VAL ILE LEU GLU GLY MET VAL GLU ALA THR ALA MET
SEQRES 22 A 343 THR THR GLN ALA ARG SER SER TYR LEU ALA SER GLU ILE
SEQRES 23 A 343 LEU TRP GLY HIS ARG PHE GLU PRO VAL LEU PHE GLU GLU
SEQRES 24 A 343 LYS ASN GLN TYR LYS VAL ASP TYR SER HIS PHE HIS LYS
SEQRES 25 A 343 THR TYR GLU VAL PRO SER THR PRO ARG CYS SER ALA LYS
SEQRES 26 A 343 ASP LEU VAL GLU ASN LYS PHE LEU LEU SER ASN SER LEU
SEQRES 27 A 343 GLU VAL LEU PHE GLN
HET K A 501 1
HET K A 502 1
HET K A 503 1
HET K A 504 1
HET K A 505 1
HETNAM K POTASSIUM ION
FORMUL 2 K 5(K 1+)
HELIX 1 1 MET A 70 VAL A 75 5 6
HELIX 2 2 ARG A 80 HIS A 108 1 29
HELIX 3 3 GLY A 109 ASN A 113 5 5
HELIX 4 4 GLY A 129 THR A 142 1 14
HELIX 5 5 CYS A 155 LYS A 183 1 29
HELIX 6 6 GLY A 254 GLY A 258 5 5
HELIX 7 7 SER A 284 GLU A 289 1 6
HELIX 8 8 SER A 358 SER A 372 1 15
SHEET 1 A 3 VAL A 54 THR A 57 0
SHEET 2 A 3 GLN A 337 ASP A 341 1 O TYR A 338 N GLU A 55
SHEET 3 A 3 LEU A 331 GLU A 334 -1 N PHE A 332 O LYS A 339
SHEET 1 B 2 VAL A 124 LEU A 125 0
SHEET 2 B 2 CYS A 150 VAL A 151 -1 O CYS A 150 N LEU A 125
SHEET 1 C 3 LEU A 194 PHE A 196 0
SHEET 2 C 3 LYS A 208 ASN A 217 -1 O GLY A 216 N LEU A 195
SHEET 3 C 3 ILE A 268 GLU A 273 -1 O ILE A 270 N TRP A 213
SHEET 1 D 4 LEU A 194 PHE A 196 0
SHEET 2 D 4 LYS A 208 ASN A 217 -1 O GLY A 216 N LEU A 195
SHEET 3 D 4 ALA A 200 ARG A 205 -1 N VAL A 201 O MET A 212
SHEET 4 D 4 ILE A 321 TRP A 323 1 O LEU A 322 N ALA A 200
SHEET 1 E 3 TYR A 243 ILE A 251 0
SHEET 2 E 3 LEU A 223 ILE A 237 -1 N LYS A 234 O ASP A 247
SHEET 3 E 3 ARG A 261 ILE A 262 -1 O ILE A 262 N ALA A 226
SHEET 1 F 4 TYR A 243 ILE A 251 0
SHEET 2 F 4 LEU A 223 ILE A 237 -1 N LYS A 234 O ASP A 247
SHEET 3 F 4 GLU A 294 VAL A 303 -1 O GLU A 294 N ILE A 233
SHEET 4 F 4 THR A 309 LEU A 317 -1 O THR A 310 N GLY A 301
SHEET 1 G 2 HIS A 325 PHE A 327 0
SHEET 2 G 2 THR A 348 GLU A 350 -1 O TYR A 349 N ARG A 326
SSBOND 1 CYS A 123 CYS A 155 1555 1555 2.04
LINK O THR A 143 K K A 503 1555 1555 2.70
LINK OG1 THR A 143 K K A 504 1555 1555 2.69
LINK O THR A 143 K K A 504 1555 1555 2.70
LINK O ILE A 144 K K A 502 1555 1555 2.77
LINK O ILE A 144 K K A 503 1555 1555 2.67
LINK O GLY A 145 K K A 501 1555 1555 2.78
LINK O GLY A 145 K K A 502 1555 1555 2.74
LINK O TYR A 146 K K A 501 1555 1555 2.82
SITE 1 AC1 3 GLY A 145 TYR A 146 K A 502
SITE 1 AC2 4 ILE A 144 GLY A 145 K A 501 K A 503
SITE 1 AC3 4 THR A 143 ILE A 144 K A 502 K A 504
SITE 1 AC4 2 THR A 143 K A 503
CRYST1 83.769 83.769 197.126 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 0.011938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
