HEADER TRANSFERASE 03-APR-08 3CR0
TITLE WEE1 KINASE COMPLEX WITH INHIBITOR PD259_809
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WEE1-LIKE PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: WEE1A KINASE, WEE1HU;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: WEE1;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PFASTBACHTA
KEYWDS KINASE DOMAIN, INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.SQUIRE,E.N.BAKER
REVDAT 4 01-NOV-23 3CR0 1 REMARK SEQADV
REVDAT 3 25-OCT-17 3CR0 1 REMARK
REVDAT 2 13-JUL-11 3CR0 1 VERSN
REVDAT 1 24-FEB-09 3CR0 0
JRNL AUTH C.J.SQUIRE,E.N.BAKER,J.M.DICKSON,I.IVANOVIC,J.SMAILL,
JRNL AUTH 2 W.A.DENNY,B.PALMER,A.THOMPSON
JRNL TITL STRUCTURAL DETERMINANTS OF WEE1 INHIBITOR SELECTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 16936
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 914
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1144
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1993
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21000
REMARK 3 B22 (A**2) : 1.21000
REMARK 3 B33 (A**2) : -2.42000
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): 0.248
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.160
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.996
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2080 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2814 ; 2.279 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 257 ; 6.795 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;31.585 ;22.809
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 350 ;17.747 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.593 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 309 ; 0.138 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1560 ; 0.012 ; 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): 1282 ; 1.047 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2051 ; 1.802 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 798 ; 3.287 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 761 ; 4.695 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 293 A 570
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5720 43.7200 29.9300
REMARK 3 T TENSOR
REMARK 3 T11: -0.1377 T22: -0.0569
REMARK 3 T33: -0.2351 T12: 0.0064
REMARK 3 T13: 0.0121 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.7328 L22: 3.1039
REMARK 3 L33: 2.4468 L12: -0.0632
REMARK 3 L13: -0.6080 L23: 1.0637
REMARK 3 S TENSOR
REMARK 3 S11: -0.0685 S12: -0.0081 S13: -0.0714
REMARK 3 S21: 0.0305 S22: 0.0417 S23: 0.1715
REMARK 3 S31: 0.1010 S32: -0.1060 S33: 0.0268
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 3CR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17891
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 63.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.340
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1X8B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, SODIUM CHLORIDE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 78.63950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.82950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.82950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.31975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.82950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.82950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.95925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.82950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.82950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.31975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.82950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.82950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.95925
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 78.63950
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 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 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 GLY A 289
REMARK 465 ALA A 290
REMARK 465 MET A 291
REMARK 465 LYS A 292
REMARK 465 GLU A 309
REMARK 465 PHE A 310
REMARK 465 GLU A 368
REMARK 465 ASP A 369
REMARK 465 ARG A 436
REMARK 465 THR A 437
REMARK 465 SER A 438
REMARK 465 ILE A 439
REMARK 465 PRO A 440
REMARK 465 ASN A 441
REMARK 465 ALA A 442
REMARK 465 ALA A 443
REMARK 465 SER A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLY A 447
REMARK 465 ASP A 448
REMARK 465 GLU A 449
REMARK 465 ASP A 450
REMARK 465 ASP A 451
REMARK 465 TRP A 452
REMARK 465 ALA A 453
REMARK 465 SER A 454
REMARK 465 ASN A 455
REMARK 465 ARG A 574
REMARK 465 LYS A 575
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 331 CG CD CE NZ
REMARK 470 LEU A 334 CG CD1 CD2
REMARK 470 ASP A 370 CG OD1 OD2
REMARK 470 GLU A 390 CG CD OE1 OE2
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 GLN A 474 CG CD OE1 NE2
REMARK 470 GLU A 476 CG CD OE1 OE2
REMARK 470 ASP A 521 CG OD1 OD2
REMARK 470 GLN A 522 CG CD OE1 NE2
REMARK 470 GLU A 544 CG CD OE1 OE2
REMARK 470 LEU A 570 CG CD1 CD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 361 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 361 NH2 ARG A 361 8665 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 357 CB SER A 357 OG 0.097
REMARK 500 ARG A 361 NE ARG A 361 CZ -0.493
REMARK 500 GLU A 541 CG GLU A 541 CD 0.113
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 361 CD - NE - CZ ANGL. DEV. = -46.0 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH1 ANGL. DEV. = -26.5 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 518 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 527 NE - CZ - NH1 ANGL. DEV. = 4.4 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 GLU A 303 147.21 -174.77
REMARK 500 LEU A 353 42.78 -109.92
REMARK 500 ASP A 426 50.79 -145.06
REMARK 500 ASP A 463 78.85 53.76
REMARK 500 PRO A 535 44.90 -80.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 361 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 809 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X8B RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH INHIBITOR PD0407824
DBREF 3CR0 A 291 575 UNP P30291 WEE1_HUMAN 291 575
SEQADV 3CR0 GLY A 289 UNP P30291 EXPRESSION TAG
SEQADV 3CR0 ALA A 290 UNP P30291 EXPRESSION TAG
SEQRES 1 A 287 GLY ALA MET LYS SER ARG TYR THR THR GLU PHE HIS GLU
SEQRES 2 A 287 LEU GLU LYS ILE GLY SER GLY GLU PHE GLY SER VAL PHE
SEQRES 3 A 287 LYS CYS VAL LYS ARG LEU ASP GLY CYS ILE TYR ALA ILE
SEQRES 4 A 287 LYS ARG SER LYS LYS PRO LEU ALA GLY SER VAL ASP GLU
SEQRES 5 A 287 GLN ASN ALA LEU ARG GLU VAL TYR ALA HIS ALA VAL LEU
SEQRES 6 A 287 GLY GLN HIS SER HIS VAL VAL ARG TYR PHE SER ALA TRP
SEQRES 7 A 287 ALA GLU ASP ASP HIS MET LEU ILE GLN ASN GLU TYR CYS
SEQRES 8 A 287 ASN GLY GLY SER LEU ALA ASP ALA ILE SER GLU ASN TYR
SEQRES 9 A 287 ARG ILE MET SER TYR PHE LYS GLU ALA GLU LEU LYS ASP
SEQRES 10 A 287 LEU LEU LEU GLN VAL GLY ARG GLY LEU ARG TYR ILE HIS
SEQRES 11 A 287 SER MET SER LEU VAL HIS MET ASP ILE LYS PRO SER ASN
SEQRES 12 A 287 ILE PHE ILE SER ARG THR SER ILE PRO ASN ALA ALA SER
SEQRES 13 A 287 GLU GLU GLY ASP GLU ASP ASP TRP ALA SER ASN LYS VAL
SEQRES 14 A 287 MET PHE LYS ILE GLY ASP LEU GLY HIS VAL THR ARG ILE
SEQRES 15 A 287 SER SER PRO GLN VAL GLU GLU GLY ASP SER ARG PHE LEU
SEQRES 16 A 287 ALA ASN GLU VAL LEU GLN GLU ASN TYR THR HIS LEU PRO
SEQRES 17 A 287 LYS ALA ASP ILE PHE ALA LEU ALA LEU THR VAL VAL CYS
SEQRES 18 A 287 ALA ALA GLY ALA GLU PRO LEU PRO ARG ASN GLY ASP GLN
SEQRES 19 A 287 TRP HIS GLU ILE ARG GLN GLY ARG LEU PRO ARG ILE PRO
SEQRES 20 A 287 GLN VAL LEU SER GLN GLU PHE THR GLU LEU LEU LYS VAL
SEQRES 21 A 287 MET ILE HIS PRO ASP PRO GLU ARG ARG PRO SER ALA MET
SEQRES 22 A 287 ALA LEU VAL LYS HIS SER VAL LEU LEU SER ALA SER ARG
SEQRES 23 A 287 LYS
HET CL A 1 1
HET 809 A 901 25
HET GOL A 902 6
HETNAM CL CHLORIDE ION
HETNAM 809 4-(2-CHLOROPHENYL)-8-(2-HYDROXYETHYL)-6-
HETNAM 2 809 METHYLPYRROLO[3,4-E]INDOLE-1,3(2H,6H)-DIONE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL CL 1-
FORMUL 3 809 C19 H15 CL N2 O3
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *144(H2 O)
HELIX 1 1 SER A 293 GLU A 298 1 6
HELIX 2 2 SER A 337 LEU A 353 1 17
HELIX 3 3 SER A 383 MET A 395 1 13
HELIX 4 4 LYS A 399 MET A 420 1 22
HELIX 5 5 LYS A 428 SER A 430 5 3
HELIX 6 6 ALA A 484 GLN A 489 1 6
HELIX 7 7 LEU A 495 ALA A 511 1 17
HELIX 8 8 ASN A 519 GLN A 528 1 10
HELIX 9 9 SER A 539 ILE A 550 1 12
HELIX 10 10 ASP A 553 ARG A 557 5 5
HELIX 11 11 SER A 559 HIS A 566 1 8
HELIX 12 12 HIS A 566 SER A 571 1 6
SHEET 1 A 5 PHE A 299 GLY A 306 0
SHEET 2 A 5 SER A 312 LYS A 318 -1 O LYS A 315 N LEU A 302
SHEET 3 A 5 CYS A 323 LYS A 331 -1 O ARG A 329 N SER A 312
SHEET 4 A 5 HIS A 371 GLU A 377 -1 O ASN A 376 N ALA A 326
SHEET 5 A 5 TYR A 362 TRP A 366 -1 N SER A 364 O GLN A 375
SHEET 1 B 2 LEU A 422 VAL A 423 0
SHEET 2 B 2 THR A 468 ARG A 469 -1 O THR A 468 N VAL A 423
SHEET 1 C 2 ILE A 432 SER A 435 0
SHEET 2 C 2 MET A 458 ILE A 461 -1 O LYS A 460 N PHE A 433
SITE 1 AC1 3 PRO A 429 SER A 430 ARG A 481
SITE 1 AC2 11 ILE A 305 GLY A 306 ALA A 326 LYS A 328
SITE 2 AC2 11 GLU A 346 ASN A 376 GLU A 377 CYS A 379
SITE 3 AC2 11 GLY A 382 ASP A 463 HOH A 960
SITE 1 AC3 9 ILE A 388 ASN A 391 TYR A 392 TYR A 397
SITE 2 AC3 9 PHE A 398 CYS A 509 ALA A 510 GLY A 512
SITE 3 AC3 9 ALA A 513
CRYST1 69.659 69.659 157.279 90.00 90.00 90.00 P 41 21 2 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 0.014356 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014356 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006358 0.00000
(ATOM LINES ARE NOT SHOWN.)
END