HEADER TRANSFERASE 21-OCT-04 1XTE
TITLE CRYSTAL STRUCTURE OF CISK-PX DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE SGK3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 7-160: CONTAINS PX DOMAIN
COMPND 5 (RESIDUES 12-124);
COMPND 6 SYNONYM: CISK-PX DOMAIN, SERUM/GLUCOCORTICOID REGULATED KINASE 3,
COMPND 7 SERUM/GLUCOCORTICOID REGULATED KINASE-LIKE, CYTOKINE INDEPENDENT
COMPND 8 SURVIVAL KINASE;
COMPND 9 EC: 2.7.1.37;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CISK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS CISK, PX DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XING,D.LIU,R.ZHANG,A.JOACHIMIAK,Z.SONGYANG,W.XU
REVDAT 4 14-FEB-24 1XTE 1 REMARK
REVDAT 3 24-JAN-18 1XTE 1 AUTHOR JRNL
REVDAT 2 24-FEB-09 1XTE 1 VERSN
REVDAT 1 16-NOV-04 1XTE 0
JRNL AUTH Y.XING,D.LIU,R.ZHANG,A.JOACHIMIAK,Z.SONGYANG,W.XU
JRNL TITL STRUCTURAL BASIS OF MEMBRANE TARGETING BY THE PHOX HOMOLOGY
JRNL TITL 2 DOMAIN OF CYTOKINE-INDEPENDENT SURVIVAL KINASE (CISK-PX)
JRNL REF J.BIOL.CHEM. V. 279 30662 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15126499
JRNL DOI 10.1074/JBC.M404107200
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 791671.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 17839
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 SET) : 0.187
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1398
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2434
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 191
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 961
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 149
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.24000
REMARK 3 B22 (A**2) : 1.24000
REMARK 3 B33 (A**2) : -2.47000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.05
REMARK 3 LOW RESOLUTION CUTOFF (A) : 50.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.340
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.940 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.360 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.820 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.66
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030746.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-02; 22-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 150; 150
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-BM; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934; 0.97933
REMARK 200 MONOCHROMATOR : SI 111; SI 111
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ANL-ECD; CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18760
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.19900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, SODIUM MALONATE, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING 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 37.47700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.47700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.84850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.47700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.47700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.84850
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 37.47700
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 37.47700
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.84850
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 37.47700
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 37.47700
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.84850
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: MONOMERIC
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 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 1
REMARK 465 ASP A 2
REMARK 465 TYR A 3
REMARK 465 SER A 120
REMARK 465 ASP A 121
REMARK 465 PRO A 122
REMARK 465 SER A 123
REMARK 465 GLU A 124
REMARK 465 ASP A 125
REMARK 465 GLU A 126
REMARK 465 ASP A 127
REMARK 465 GLU A 128
REMARK 465 ARG A 129
REMARK 465 SER A 130
REMARK 465 THR A 131
REMARK 465 SER A 132
REMARK 465 LYS A 133
REMARK 465 PRO A 134
REMARK 465 HIS A 135
REMARK 465 SER A 136
REMARK 465 THR A 137
REMARK 465 SER A 138
REMARK 465 ARG A 139
REMARK 465 ASN A 140
REMARK 465 ILE A 141
REMARK 465 ASN A 142
REMARK 465 LEU A 143
REMARK 465 GLY A 144
REMARK 465 PRO A 145
REMARK 465 THR A 146
REMARK 465 GLY A 147
REMARK 465 ASN A 148
REMARK 465 PRO A 149
REMARK 465 HIS A 150
REMARK 465 ALA A 151
REMARK 465 LYS A 152
REMARK 465 PRO A 153
REMARK 465 THR A 154
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 4 CG CD CE NZ
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 ARG A 97 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 119 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 16 O HOH A 204 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 22 28.79 49.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XTE A 1 154 UNP Q9ERE3 SGK3_MOUSE 7 160
SEQRES 1 A 154 MET ASP TYR LYS GLU SER CYS PRO SER VAL SER ILE PRO
SEQRES 2 A 154 SER SER ASP GLU HIS ARG GLU LYS LYS LYS ARG PHE THR
SEQRES 3 A 154 VAL TYR LYS VAL LEU VAL SER VAL GLY ARG SER GLU TRP
SEQRES 4 A 154 PHE VAL PHE ARG ARG TYR ALA GLU PHE ASP LYS LEU TYR
SEQRES 5 A 154 ASN SER LEU LYS LYS GLN PHE PRO ALA MET ALA LEU LYS
SEQRES 6 A 154 ILE PRO ALA LYS ARG ILE PHE GLY ASP ASN PHE ASP PRO
SEQRES 7 A 154 ASP PHE ILE LYS GLN ARG ARG ALA GLY LEU ASN GLU PHE
SEQRES 8 A 154 ILE GLN ASN LEU VAL ARG TYR PRO GLU LEU TYR ASN HIS
SEQRES 9 A 154 PRO ASP VAL ARG ALA PHE LEU GLN MET ASP SER PRO ARG
SEQRES 10 A 154 HIS GLN SER ASP PRO SER GLU ASP GLU ASP GLU ARG SER
SEQRES 11 A 154 THR SER LYS PRO HIS SER THR SER ARG ASN ILE ASN LEU
SEQRES 12 A 154 GLY PRO THR GLY ASN PRO HIS ALA LYS PRO THR
FORMUL 2 HOH *149(H2 O)
HELIX 1 1 TYR A 45 PHE A 59 1 15
HELIX 2 2 PRO A 60 ALA A 63 5 4
HELIX 3 3 ASP A 77 VAL A 96 1 20
HELIX 4 4 TYR A 98 ASN A 103 1 6
HELIX 5 5 HIS A 104 LEU A 111 1 8
HELIX 6 6 SER A 115 GLN A 119 5 5
SHEET 1 A 3 SER A 9 GLU A 20 0
SHEET 2 A 3 LYS A 23 VAL A 34 -1 O LYS A 23 N GLU A 20
SHEET 3 A 3 SER A 37 ARG A 44 -1 O VAL A 41 N VAL A 30
CRYST1 74.954 74.954 51.697 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 0.013342 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019343 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
