HEADER TRANSFERASE 10-OCT-06 2IO6
TITLE WEE1 KINASE COMPLEXED WITH INHIBITOR PD330961
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_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: WEE1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTA
KEYWDS PROTEIN-INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.SQUIRE,J.M.DICKSON,I.IVANOVIC,E.N.BAKER
REVDAT 5 30-AUG-23 2IO6 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2IO6 1 VERSN
REVDAT 3 01-JUL-08 2IO6 1 JRNL
REVDAT 2 08-JAN-08 2IO6 1 JRNL
REVDAT 1 18-SEP-07 2IO6 0
JRNL AUTH J.B.SMAILL,E.N.BAKER,R.J.BOOTH,A.J.BRIDGES,J.M.DICKSON,
JRNL AUTH 2 E.M.DOBRUSIN,I.IVANOVIC,A.J.KRAKER,H.H.LEE,E.A.LUNNEY,
JRNL AUTH 3 D.F.ORTWINE,B.D.PALMER,J.QUIN,C.J.SQUIRE,A.M.THOMPSON,
JRNL AUTH 4 W.A.DENNY
JRNL TITL SYNTHESIS AND STRUCTURE-ACTIVITY RELATIONSHIPS OF N-6
JRNL TITL 2 SUBSTITUTED ANALOGUES OF
JRNL TITL 3 9-HYDROXY-4-PHENYLPYRROLO[3,4-C]CARBAZOLE-1,3(2H,6H)-DIONES
JRNL TITL 4 AS INHIBITORS OF WEE1 AND CHK1 CHECKPOINT KINASES.
JRNL REF EUR.J.MED.CHEM. V. 43 1276 2008
JRNL REFN ISSN 0223-5234
JRNL PMID 17869387
JRNL DOI 10.1016/J.EJMECH.2007.07.016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.SQUIRE,J.M.DICKSON,I.IVANOVIC,E.N.BAKER
REMARK 1 TITL STRUCTURE AND INHIBITION OF THE HUMAN CELL CYCLE CHECKPOINT
REMARK 1 TITL 2 KINASE, WEE1A KINASE: AN ATYPICAL TYROSINE KINASE WITH A KEY
REMARK 1 TITL 3 ROLE IN CDK1 REGULATION.
REMARK 1 REF STRUCTURE V. 13 541 2005
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 15837193
REMARK 1 DOI 10.1016/J.STR.2004.12.017
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 19508
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1057
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1401
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2009
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.35000
REMARK 3 B22 (A**2) : 1.35000
REMARK 3 B33 (A**2) : -2.70000
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): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.630
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2086 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2818 ; 2.161 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 6.779 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;33.039 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 367 ;17.457 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.678 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 305 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1568 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 861 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1408 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 70 ; 0.129 ; 0.200
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): 26 ; 0.295 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.141 ; 0.200
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): 1305 ; 1.402 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2021 ; 2.259 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 998 ; 3.324 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 797 ; 5.115 ; 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 : 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 2IO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : PT/PD ULE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
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) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.50700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB 1X8B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
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 78.96000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.96250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.96250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.48000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.96250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.96250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 118.44000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.96250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.96250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.48000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.96250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.96250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 118.44000
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 78.96000
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 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 A 9 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 ALA A 289
REMARK 465 GLU A 290
REMARK 465 GLY A 308
REMARK 465 GLU A 309
REMARK 465 PHE A 310
REMARK 465 GLY A 311
REMARK 465 LEU A 334
REMARK 465 ALA A 335
REMARK 465 GLY A 336
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 LEU A 570
REMARK 465 SER A 571
REMARK 465 ALA A 572
REMARK 465 SER A 573
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 GLN A 474 CG CD OE1 NE2
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 527 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 527 NE - CZ - NH2 ANGL. DEV. = -3.4 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 LYS A 292 65.24 61.13
REMARK 500 SER A 293 144.50 -32.85
REMARK 500 LEU A 353 43.98 -103.47
REMARK 500 ASP A 369 -132.81 75.41
REMARK 500 GLU A 377 129.07 -35.00
REMARK 500 MET A 425 -0.61 73.56
REMARK 500 ASP A 426 48.24 -150.18
REMARK 500 ASP A 463 80.30 54.07
REMARK 500 ASN A 519 -171.56 -179.96
REMARK 500 PRO A 535 43.65 -83.90
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 330 A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X8B RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH PD407824
REMARK 900 RELATED ID: 2IN6 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH PD311839
DBREF 2IO6 A 291 575 UNP P30291 WEE1_HUMAN 291 575
SEQADV 2IO6 ALA A 289 UNP P30291 EXPRESSION TAG
SEQADV 2IO6 GLU A 290 UNP P30291 EXPRESSION TAG
SEQRES 1 A 287 ALA GLU 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 330 A 901 31
HETNAM 330 9-HYDROXY-6-(3-HYDROXYPROPYL)-4-(2-METHOXYPHENYL)
HETNAM 2 330 PYRROLO[3,4-C]CARBAZOLE-1,3(2H,6H)-DIONE
FORMUL 2 330 C24 H20 N2 O5
FORMUL 3 HOH *45(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 HIS A 494 ALA A 511 1 18
HELIX 8 8 GLY A 520 GLN A 528 1 9
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 LYS A 565 1 7
SHEET 1 A 5 PHE A 299 GLY A 306 0
SHEET 2 A 5 VAL A 313 LYS A 318 -1 O LYS A 315 N LEU A 302
SHEET 3 A 5 ILE A 324 LYS A 331 -1 O TYR A 325 N CYS A 316
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 GLU A 368 -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 15 HOH A 27 ILE A 305 ALA A 326 LYS A 328
SITE 2 AC1 15 GLU A 346 VAL A 360 ILE A 374 ASN A 376
SITE 3 AC1 15 GLU A 377 TYR A 378 CYS A 379 GLY A 382
SITE 4 AC1 15 SER A 430 PHE A 433 ASP A 463
CRYST1 69.925 69.925 157.920 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 0.014301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014301 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END