HEADER TRANSFERASE 31-MAY-13 4L0N
TITLE CRYSTAL STRUCTURE OF STK3 (MST2) SARAH DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 3;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 FRAGMENT: SARAH DOMAIN (UNP RESIDUES 436-484);
COMPND 5 SYNONYM: MAMMALIAN STE20-LIKE PROTEIN KINASE 2, MST-2, STE20-LIKE
COMPND 6 KINASE MST2, SERINE/THREONINE-PROTEIN KINASE KRS-1, SERINE/THREONINE-
COMPND 7 PROTEIN KINASE 3 36KDA SUBUNIT, MST2/N, SERINE/THREONINE-PROTEIN
COMPND 8 KINASE 3 20KDA SUBUNIT, MST2/C;
COMPND 9 EC: 2.7.11.1;
COMPND 10 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: KRS1, MST2, STK3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SARAH
KEYWDS 2 DOMAIN, STK3, MST2, HEPTAD REPEAT, STRUCTURAL GENOMICS CONSORTIUM
KEYWDS 3 (SGC), TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,T.KROJER,J.A.NEWMAN,S.DIXON-CLARKE,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 2 28-FEB-24 4L0N 1 SEQADV
REVDAT 1 19-JUN-13 4L0N 0
JRNL AUTH A.CHAIKUAD,T.KROJER,J.A.NEWMAN,S.DIXON-CLARKE,F.VON DELFT,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP,
JRNL AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF STK3 (MST2) SARAH DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 108637
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5733
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7849
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 422
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4225
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 799
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.91000
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): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.284
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4572 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4632 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6142 ; 1.718 ; 2.025
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10724 ; 0.805 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 573 ; 4.773 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 245 ;29.375 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1036 ;13.654 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;14.563 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 667 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5065 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 981 ; 0.001 ; 0.020
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): 2118 ; 2.638 ; 1.785
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2117 ; 2.638 ; 1.785
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2648 ; 3.098 ; 2.673
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2454 ; 3.877 ; 2.231
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): 9204 ; 4.883 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 237 ;30.990 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 9687 ;10.761 ; 5.000
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4L0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114371
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 32.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 0.1M ACETATE PH 4.9, 0.2M
REMARK 280 CALCIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 150.93000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.66000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.66000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 75.46500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.66000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.66000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 226.39500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.66000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.66000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 75.46500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.66000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.66000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 226.39500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 150.93000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 2760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
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: 2830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
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: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 150.93000
REMARK 350
REMARK 350 BIOMOLECULE: 6
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: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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 0.000000 -1.000000 0.000000 61.32000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 61.32000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 150.93000
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 HOH C 548 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 565 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 SER J 434
REMARK 465 MET J 435
REMARK 465 ASP J 436
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 F 484 CG CD CE NZ
REMARK 470 MET G 0 CG SD CE
REMARK 470 ASP G 438 CG OD1 OD2
REMARK 470 LYS G 441 CD CE NZ
REMARK 470 ASN G 442 CG OD1 ND2
REMARK 470 ASP H 436 CG OD1 OD2
REMARK 470 PHE J 437 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP J 438 CG OD1 OD2
REMARK 470 LYS J 441 CG CD CE NZ
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 O HOH F 562 O HOH F 568 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 474 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET B 481 CG - SD - CE ANGL. DEV. = -10.8 DEGREES
REMARK 500 MET D 458 CG - SD - CE ANGL. DEV. = 11.0 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 MET G 0 -16.57 -142.78
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4L0N A 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N B 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N C 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N D 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N E 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N F 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N G 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N H 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N I 436 484 UNP Q13188 STK3_HUMAN 436 484
DBREF 4L0N J 436 484 UNP Q13188 STK3_HUMAN 436 484
SEQADV 4L0N SER A -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET A 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER B -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET B 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER C -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET C 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER D -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET D 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER E -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET E 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER F -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET F 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER G -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET G 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER H -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET H 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER I -1 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET I 0 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N SER J 434 UNP Q13188 EXPRESSION TAG
SEQADV 4L0N MET J 435 UNP Q13188 EXPRESSION TAG
SEQRES 1 A 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 A 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 A 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 A 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 B 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 B 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 B 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 B 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 C 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 C 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 C 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 C 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 D 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 D 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 D 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 D 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 E 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 E 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 E 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 E 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 F 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 F 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 F 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 F 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 G 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 G 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 G 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 G 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 H 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 H 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 H 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 H 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 I 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 I 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 I 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 I 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
SEQRES 1 J 51 SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU
SEQRES 2 J 51 GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET
SEQRES 3 J 51 GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA
SEQRES 4 J 51 LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS
FORMUL 11 HOH *799(H2 O)
HELIX 1 1 SER A -1 LYS A 441 1 8
HELIX 2 2 SER A 444 LYS A 484 1 41
HELIX 3 3 MET B 0 LEU B 443 1 9
HELIX 4 4 SER B 444 ALA B 483 1 40
HELIX 5 5 ASP C 436 LYS C 441 1 6
HELIX 6 6 SER C 444 ALA C 483 1 40
HELIX 7 7 MET D 0 LYS D 441 1 7
HELIX 8 8 SER D 444 ALA D 483 1 40
HELIX 9 9 ASP E 436 LYS E 441 1 6
HELIX 10 10 SER E 444 ALA E 483 1 40
HELIX 11 11 MET F 0 LYS F 441 1 7
HELIX 12 12 SER F 444 ALA F 483 1 40
HELIX 13 13 MET G 0 LEU G 440 1 6
HELIX 14 14 LYS G 441 LEU G 443 5 3
HELIX 15 15 SER G 444 ALA G 483 1 40
HELIX 16 16 MET H 0 LYS H 441 1 7
HELIX 17 17 SER H 444 ALA H 483 1 40
HELIX 18 18 MET I 0 LYS I 441 1 7
HELIX 19 19 SER I 444 ALA I 483 1 40
HELIX 20 20 SER J 444 LYS J 484 1 41
CRYST1 61.320 61.320 301.860 90.00 90.00 90.00 P 41 21 2 80
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 0.016308 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END