HEADER TRANSFERASE 28-MAR-08 3COM
TITLE CRYSTAL STRUCTURE OF MST1 KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROTEIN KINASE DOMAIN: RESIDUES 2-311;
COMPND 5 SYNONYM: STE20-LIKE KINASE MST1, MST-1, MAMMALIAN STE20-LIKE PROTEIN
COMPND 6 KINASE 1, SERINE/THREONINE-PROTEIN KINASE KRS-2;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: STK4, MST1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSGX4
KEYWDS KINASE, MST1, SERINE/THREONINE-PROTEIN KINASE 4, STE20-LIKE KINASE,
KEYWDS 2 PSI, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX
KEYWDS 3 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, ALTERNATIVE
KEYWDS 4 SPLICING, APOPTOSIS, ATP-BINDING, COILED COIL, CYTOPLASM, MAGNESIUM,
KEYWDS 5 METAL-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS 6 POLYMORPHISM, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ATWELL,S.K.BURLEY,M.DICKEY,B.LEON,J.M.SAUDER,NEW YORK SGX RESEARCH
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 6 14-NOV-18 3COM 1 AUTHOR
REVDAT 5 25-OCT-17 3COM 1 REMARK
REVDAT 4 09-JUN-09 3COM 1 REVDAT
REVDAT 3 24-FEB-09 3COM 1 VERSN
REVDAT 2 23-DEC-08 3COM 1 AUTHOR KEYWDS
REVDAT 1 15-APR-08 3COM 0
JRNL AUTH S.ATWELL,S.K.BURLEY,M.DICKEY,B.LEON,J.M.SAUDER
JRNL TITL CRYSTAL STRUCTURE OF MST1 KINASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 40443
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2022
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4283
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.015 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.394 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3COM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047028.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : KOHZU 111 DIAMOND
REMARK 200 OPTICS : KV MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3CKW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1700MM AMMONIUM SULFATE, 300MM LITHIUM
REMARK 280 SULFATE, 100MM CAPS PH 10.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 37.48850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.47750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.57550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.47750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.48850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.57550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 0
REMARK 465 LEU A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 VAL A 4
REMARK 465 GLN A 5
REMARK 465 LEU A 6
REMARK 465 ARG A 7
REMARK 465 ASN A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 ARG A 11
REMARK 465 ARG A 12
REMARK 465 GLN A 13
REMARK 465 LEU A 14
REMARK 465 LYS A 15
REMARK 465 LYS A 16
REMARK 465 LEU A 17
REMARK 465 ASP A 18
REMARK 465 GLU A 19
REMARK 465 ASP A 20
REMARK 465 SER A 21
REMARK 465 LEU A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 GLN A 25
REMARK 465 PRO A 26
REMARK 465 GLU A 27
REMARK 465 GLU A 28
REMARK 465 GLU A 38
REMARK 465 GLY A 39
REMARK 465 SER A 40
REMARK 465 TYR A 41
REMARK 465 ASP A 299
REMARK 465 VAL A 300
REMARK 465 LYS A 301
REMARK 465 LEU A 302
REMARK 465 LYS A 303
REMARK 465 ARG A 304
REMARK 465 GLN A 305
REMARK 465 GLU A 306
REMARK 465 SER A 307
REMARK 465 GLN A 308
REMARK 465 GLN A 309
REMARK 465 ARG A 310
REMARK 465 GLU A 311
REMARK 465 GLU A 312
REMARK 465 GLY A 313
REMARK 465 SER B 0
REMARK 465 LEU B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 VAL B 4
REMARK 465 GLN B 5
REMARK 465 LEU B 6
REMARK 465 ARG B 7
REMARK 465 ASN B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 ARG B 11
REMARK 465 ARG B 12
REMARK 465 GLN B 13
REMARK 465 LEU B 14
REMARK 465 LYS B 15
REMARK 465 GLU B 38
REMARK 465 GLY B 39
REMARK 465 SER B 40
REMARK 465 TYR B 41
REMARK 465 LYS B 301
REMARK 465 LEU B 302
REMARK 465 LYS B 303
REMARK 465 ARG B 304
REMARK 465 GLN B 305
REMARK 465 GLU B 306
REMARK 465 SER B 307
REMARK 465 GLN B 308
REMARK 465 GLN B 309
REMARK 465 ARG B 310
REMARK 465 GLU B 311
REMARK 465 GLU B 312
REMARK 465 GLY B 313
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 GLU A 34 CG CD OE1 OE2
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 GLN A 60 CG CD OE1 NE2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 LYS A 246 CE NZ
REMARK 470 GLU B 27 CG CD OE1 OE2
REMARK 470 GLU B 34 CG CD OE1 OE2
REMARK 470 LYS B 35 CG CD CE NZ
REMARK 470 LYS B 59 CG CD CE NZ
REMARK 470 ASN B 95 CG OD1 ND2
REMARK 470 ASN B 182 CG OD1 ND2
REMARK 470 GLU B 198 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 167 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 206 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 256 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 81 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 124 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 144 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 144 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 206 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 256 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
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 LEU A 33 -113.96 -103.00
REMARK 500 GLU A 64 46.87 -78.36
REMARK 500 ARG A 148 -9.10 78.48
REMARK 500 ASP A 167 69.76 66.24
REMARK 500 ASN A 202 -157.33 -132.46
REMARK 500 LEU A 262 50.16 -104.35
REMARK 500 SER B 65 -157.31 -157.73
REMARK 500 ASN B 95 70.29 41.37
REMARK 500 THR B 96 -1.98 70.40
REMARK 500 ARG B 148 -1.11 70.25
REMARK 500 ASP B 167 78.39 67.00
REMARK 500 ASN B 202 -157.82 -133.69
REMARK 500 LEU B 262 51.37 -96.04
REMARK 500 ASP B 299 -71.95 -53.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-8191A RELATED DB: TARGETDB
DBREF 3COM A 2 311 UNP Q13043 STK4_HUMAN 2 311
DBREF 3COM B 2 311 UNP Q13043 STK4_HUMAN 2 311
SEQADV 3COM SER A 0 UNP Q13043 EXPRESSION TAG
SEQADV 3COM LEU A 1 UNP Q13043 EXPRESSION TAG
SEQADV 3COM GLU A 312 UNP Q13043 EXPRESSION TAG
SEQADV 3COM GLY A 313 UNP Q13043 EXPRESSION TAG
SEQADV 3COM SER B 0 UNP Q13043 EXPRESSION TAG
SEQADV 3COM LEU B 1 UNP Q13043 EXPRESSION TAG
SEQADV 3COM GLU B 312 UNP Q13043 EXPRESSION TAG
SEQADV 3COM GLY B 313 UNP Q13043 EXPRESSION TAG
SEQRES 1 A 314 SER LEU GLU THR VAL GLN LEU ARG ASN PRO PRO ARG ARG
SEQRES 2 A 314 GLN LEU LYS LYS LEU ASP GLU ASP SER LEU THR LYS GLN
SEQRES 3 A 314 PRO GLU GLU VAL PHE ASP VAL LEU GLU LYS LEU GLY GLU
SEQRES 4 A 314 GLY SER TYR GLY SER VAL TYR LYS ALA ILE HIS LYS GLU
SEQRES 5 A 314 THR GLY GLN ILE VAL ALA ILE LYS GLN VAL PRO VAL GLU
SEQRES 6 A 314 SER ASP LEU GLN GLU ILE ILE LYS GLU ILE SER ILE MET
SEQRES 7 A 314 GLN GLN CYS ASP SER PRO HIS VAL VAL LYS TYR TYR GLY
SEQRES 8 A 314 SER TYR PHE LYS ASN THR ASP LEU TRP ILE VAL MET GLU
SEQRES 9 A 314 TYR CYS GLY ALA GLY SER VAL SER ASP ILE ILE ARG LEU
SEQRES 10 A 314 ARG ASN LYS THR LEU THR GLU ASP GLU ILE ALA THR ILE
SEQRES 11 A 314 LEU GLN SER THR LEU LYS GLY LEU GLU TYR LEU HIS PHE
SEQRES 12 A 314 MET ARG LYS ILE HIS ARG ASP ILE LYS ALA GLY ASN ILE
SEQRES 13 A 314 LEU LEU ASN THR GLU GLY HIS ALA LYS LEU ALA ASP PHE
SEQRES 14 A 314 GLY VAL ALA GLY GLN LEU THR ASP TPO MET ALA LYS ARG
SEQRES 15 A 314 ASN TPO VAL ILE GLY THR PRO PHE TRP MET ALA PRO GLU
SEQRES 16 A 314 VAL ILE GLN GLU ILE GLY TYR ASN CYS VAL ALA ASP ILE
SEQRES 17 A 314 TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA GLU GLY
SEQRES 18 A 314 LYS PRO PRO TYR ALA ASP ILE HIS PRO MET ARG ALA ILE
SEQRES 19 A 314 PHE MET ILE PRO THR ASN PRO PRO PRO THR PHE ARG LYS
SEQRES 20 A 314 PRO GLU LEU TRP SER ASP ASN PHE THR ASP PHE VAL LYS
SEQRES 21 A 314 GLN CYS LEU VAL LYS SER PRO GLU GLN ARG ALA THR ALA
SEQRES 22 A 314 THR GLN LEU LEU GLN HIS PRO PHE VAL ARG SER ALA LYS
SEQRES 23 A 314 GLY VAL SER ILE LEU ARG ASP LEU ILE ASN GLU ALA MET
SEQRES 24 A 314 ASP VAL LYS LEU LYS ARG GLN GLU SER GLN GLN ARG GLU
SEQRES 25 A 314 GLU GLY
SEQRES 1 B 314 SER LEU GLU THR VAL GLN LEU ARG ASN PRO PRO ARG ARG
SEQRES 2 B 314 GLN LEU LYS LYS LEU ASP GLU ASP SER LEU THR LYS GLN
SEQRES 3 B 314 PRO GLU GLU VAL PHE ASP VAL LEU GLU LYS LEU GLY GLU
SEQRES 4 B 314 GLY SER TYR GLY SER VAL TYR LYS ALA ILE HIS LYS GLU
SEQRES 5 B 314 THR GLY GLN ILE VAL ALA ILE LYS GLN VAL PRO VAL GLU
SEQRES 6 B 314 SER ASP LEU GLN GLU ILE ILE LYS GLU ILE SER ILE MET
SEQRES 7 B 314 GLN GLN CYS ASP SER PRO HIS VAL VAL LYS TYR TYR GLY
SEQRES 8 B 314 SER TYR PHE LYS ASN THR ASP LEU TRP ILE VAL MET GLU
SEQRES 9 B 314 TYR CYS GLY ALA GLY SER VAL SER ASP ILE ILE ARG LEU
SEQRES 10 B 314 ARG ASN LYS THR LEU THR GLU ASP GLU ILE ALA THR ILE
SEQRES 11 B 314 LEU GLN SER THR LEU LYS GLY LEU GLU TYR LEU HIS PHE
SEQRES 12 B 314 MET ARG LYS ILE HIS ARG ASP ILE LYS ALA GLY ASN ILE
SEQRES 13 B 314 LEU LEU ASN THR GLU GLY HIS ALA LYS LEU ALA ASP PHE
SEQRES 14 B 314 GLY VAL ALA GLY GLN LEU THR ASP TPO MET ALA LYS ARG
SEQRES 15 B 314 ASN TPO VAL ILE GLY THR PRO PHE TRP MET ALA PRO GLU
SEQRES 16 B 314 VAL ILE GLN GLU ILE GLY TYR ASN CYS VAL ALA ASP ILE
SEQRES 17 B 314 TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA GLU GLY
SEQRES 18 B 314 LYS PRO PRO TYR ALA ASP ILE HIS PRO MET ARG ALA ILE
SEQRES 19 B 314 PHE MET ILE PRO THR ASN PRO PRO PRO THR PHE ARG LYS
SEQRES 20 B 314 PRO GLU LEU TRP SER ASP ASN PHE THR ASP PHE VAL LYS
SEQRES 21 B 314 GLN CYS LEU VAL LYS SER PRO GLU GLN ARG ALA THR ALA
SEQRES 22 B 314 THR GLN LEU LEU GLN HIS PRO PHE VAL ARG SER ALA LYS
SEQRES 23 B 314 GLY VAL SER ILE LEU ARG ASP LEU ILE ASN GLU ALA MET
SEQRES 24 B 314 ASP VAL LYS LEU LYS ARG GLN GLU SER GLN GLN ARG GLU
SEQRES 25 B 314 GLU GLY
MODRES 3COM TPO A 177 THR PHOSPHOTHREONINE
MODRES 3COM TPO A 183 THR PHOSPHOTHREONINE
MODRES 3COM TPO B 177 THR PHOSPHOTHREONINE
MODRES 3COM TPO B 183 THR PHOSPHOTHREONINE
HET TPO A 177 11
HET TPO A 183 11
HET TPO B 177 11
HET TPO B 183 11
HETNAM TPO PHOSPHOTHREONINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 4(C4 H10 N O6 P)
FORMUL 3 HOH *231(H2 O)
HELIX 1 1 LEU A 67 GLN A 79 1 13
HELIX 2 2 VAL A 110 ASN A 118 1 9
HELIX 3 3 THR A 122 MET A 143 1 22
HELIX 4 4 LYS A 151 GLY A 153 5 3
HELIX 5 5 THR A 187 MET A 191 5 5
HELIX 6 6 ALA A 192 GLN A 197 1 6
HELIX 7 7 VAL A 204 GLY A 220 1 17
HELIX 8 8 HIS A 228 ASN A 239 1 12
HELIX 9 9 LYS A 246 TRP A 250 5 5
HELIX 10 10 SER A 251 LEU A 262 1 12
HELIX 11 11 THR A 271 LEU A 276 1 6
HELIX 12 12 HIS A 278 SER A 283 1 6
HELIX 13 13 GLY A 286 ILE A 289 5 4
HELIX 14 14 LEU A 290 MET A 298 1 9
HELIX 15 15 ASP B 18 THR B 23 1 6
HELIX 16 16 GLN B 25 VAL B 29 1 5
HELIX 17 17 ASP B 66 GLN B 78 1 13
HELIX 18 18 VAL B 110 ASN B 118 1 9
HELIX 19 19 THR B 122 MET B 143 1 22
HELIX 20 20 LYS B 151 GLY B 153 5 3
HELIX 21 21 THR B 187 MET B 191 5 5
HELIX 22 22 ALA B 192 GLN B 197 1 6
HELIX 23 23 VAL B 204 GLY B 220 1 17
HELIX 24 24 HIS B 228 ILE B 236 1 9
HELIX 25 25 LYS B 246 TRP B 250 5 5
HELIX 26 26 SER B 251 LEU B 262 1 12
HELIX 27 27 THR B 271 LEU B 276 1 6
HELIX 28 28 HIS B 278 SER B 283 1 6
HELIX 29 29 GLY B 286 ILE B 289 5 4
HELIX 30 30 LEU B 290 VAL B 300 1 11
SHEET 1 A 5 PHE A 30 LYS A 35 0
SHEET 2 A 5 SER A 43 HIS A 49 -1 O LYS A 46 N LEU A 33
SHEET 3 A 5 ILE A 55 PRO A 62 -1 O GLN A 60 N SER A 43
SHEET 4 A 5 ASP A 97 GLU A 103 -1 O LEU A 98 N VAL A 61
SHEET 5 A 5 TYR A 88 LYS A 94 -1 N TYR A 89 O VAL A 101
SHEET 1 B 3 GLY A 108 SER A 109 0
SHEET 2 B 3 ILE A 155 LEU A 157 -1 O LEU A 157 N GLY A 108
SHEET 3 B 3 ALA A 163 LEU A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 C 2 LYS A 145 ILE A 146 0
SHEET 2 C 2 GLY A 172 GLN A 173 -1 O GLY A 172 N ILE A 146
SHEET 1 D 5 PHE B 30 LYS B 35 0
SHEET 2 D 5 VAL B 44 HIS B 49 -1 O LYS B 46 N LEU B 33
SHEET 3 D 5 ILE B 55 PRO B 62 -1 O ILE B 58 N TYR B 45
SHEET 4 D 5 ASP B 97 GLU B 103 -1 O LEU B 98 N VAL B 61
SHEET 5 D 5 TYR B 88 LYS B 94 -1 N TYR B 92 O TRP B 99
SHEET 1 E 3 GLY B 108 SER B 109 0
SHEET 2 E 3 ILE B 155 LEU B 157 -1 O LEU B 157 N GLY B 108
SHEET 3 E 3 ALA B 163 LEU B 165 -1 O LYS B 164 N LEU B 156
SHEET 1 F 2 LYS B 145 ILE B 146 0
SHEET 2 F 2 GLY B 172 GLN B 173 -1 O GLY B 172 N ILE B 146
LINK C ASP A 176 N TPO A 177 1555 1555 1.33
LINK C TPO A 177 N MET A 178 1555 1555 1.32
LINK C ASN A 182 N TPO A 183 1555 1555 1.33
LINK C TPO A 183 N VAL A 184 1555 1555 1.33
LINK C ASP B 176 N TPO B 177 1555 1555 1.33
LINK C TPO B 177 N MET B 178 1555 1555 1.33
LINK C ASN B 182 N TPO B 183 1555 1555 1.33
LINK C TPO B 183 N VAL B 184 1555 1555 1.34
CRYST1 74.977 105.151 110.955 90.00 90.00 90.00 P 21 21 21 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 0.013337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009510 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
