HEADER TRANSFERASE 20-FEB-13 4JBP
TITLE NOVEL AURORA KINASE INHIBITORS REVEAL MECHANISMS OF HURP IN NUCLEATION
TITLE 2 OF CENTROSOMAL AND KINETOCHORE MICROTUBULES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 123-401;
COMPND 5 SYNONYM: AURORA 2, AURORA/IPL1-RELATED KINASE 1, ARK-1, AURORA-
COMPND 6 RELATED KINASE 1, HARK1, BREAST TUMOR-AMPLIFIED KINASE,
COMPND 7 SERINE/THREONINE-PROTEIN KINASE 15, SERINE/THREONINE-PROTEIN KINASE
COMPND 8 6, SERINE/THREONINE-PROTEIN KINASE AURORA-A;
COMPND 9 EC: 2.7.11.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AURKA, AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS AURORA KINASE INHIBITORS, HURP, MITOTIC SPINDLE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.WU,J.S.LEOU,Y.H.PENG,C.C.HSUEH,H.P.HSIEH,S.Y.WU
REVDAT 2 20-MAR-24 4JBP 1 REMARK SEQADV
REVDAT 1 05-JUN-13 4JBP 0
JRNL AUTH J.M.WU,C.T.CHEN,M.S.COUMAR,W.H.LIN,Z.J.CHEN,J.T.HSU,
JRNL AUTH 2 Y.H.PENG,H.Y.SHIAO,W.H.LIN,C.Y.CHU,J.S.WU,C.T.LIN,C.P.CHEN,
JRNL AUTH 3 C.C.HSUEH,K.Y.CHANG,L.P.KAO,C.Y.HUANG,Y.S.CHAO,S.Y.WU,
JRNL AUTH 4 H.P.HSIEH,Y.H.CHI
JRNL TITL AURORA KINASE INHIBITORS REVEAL MECHANISMS OF HURP IN
JRNL TITL 2 NUCLEATION OF CENTROSOMAL AND KINETOCHORE MICROTUBULES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 E1779 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23610398
JRNL DOI 10.1073/PNAS.1220523110
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 12879
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) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 632
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) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 739
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : -0.22000
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): 0.448
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.309
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.200
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.113
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2202 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1565 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2975 ; 1.308 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3736 ; 1.246 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 253 ; 5.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;35.112 ;22.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 385 ;14.313 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;17.814 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 311 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2398 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 471 ; 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): 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 : 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 126 A 390
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7460 31.8160 8.0050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.1110
REMARK 3 T33: 0.1197 T12: 0.0202
REMARK 3 T13: -0.0167 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 3.0617 L22: 0.6775
REMARK 3 L33: 1.1970 L12: 0.5326
REMARK 3 L13: -1.4504 L23: -0.2040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.3344 S13: -0.1906
REMARK 3 S21: 0.0407 S22: 0.0022 S23: -0.0252
REMARK 3 S31: 0.0829 S32: 0.1905 S33: -0.0118
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.50
REMARK 3 ION PROBE RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.20
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES: WITH TLS ADDED HYDROGENS HAVE
REMARK 3 BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4JBP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-11
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 : SPRING-8
REMARK 200 BEAMLINE : BL12B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13014
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 400, 0.1M AMMONIA SULFATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.10267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 116.20533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.15400
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 145.25667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.05133
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.10267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 116.20533
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 145.25667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 87.15400
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 29.05133
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 SER A 123
REMARK 465 LYS A 124
REMARK 465 LYS A 125
REMARK 465 ALA A 281
REMARK 465 PRO A 282
REMARK 465 SER A 283
REMARK 465 SER A 284
REMARK 465 ARG A 285
REMARK 465 ARG A 286
REMARK 465 THR A 287
REMARK 465 ASP A 288
REMARK 465 LEU A 289
REMARK 465 CYS A 290
REMARK 465 SER A 391
REMARK 465 ASN A 392
REMARK 465 CYS A 393
REMARK 465 GLN A 394
REMARK 465 ASN A 395
REMARK 465 LYS A 396
REMARK 465 GLU A 397
REMARK 465 SER A 398
REMARK 465 ALA A 399
REMARK 465 SER A 400
REMARK 465 LYS A 401
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 ARG A 251 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 280 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 305 CG SD CE
REMARK 470 PRO A 390 O
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 SER A 226 -58.05 83.46
REMARK 500 ASP A 256 37.78 -149.37
REMARK 500 ASP A 274 95.52 63.38
REMARK 500 ASP A 307 -157.33 -144.48
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 YPH A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M11 RELATED DB: PDB
REMARK 900 RELATED ID: 3K5U RELATED DB: PDB
REMARK 900 RELATED ID: 4JBO RELATED DB: PDB
REMARK 900 RELATED ID: 4JBQ RELATED DB: PDB
DBREF 4JBP A 123 401 UNP O14965 AURKA_HUMAN 123 401
SEQADV 4JBP ASP A 288 UNP O14965 THR 288 ENGINEERED MUTATION
SEQRES 1 A 279 SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE GLU ILE
SEQRES 2 A 279 GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL TYR
SEQRES 3 A 279 LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA LEU
SEQRES 4 A 279 LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY VAL
SEQRES 5 A 279 GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER HIS
SEQRES 6 A 279 LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR PHE
SEQRES 7 A 279 HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR ALA
SEQRES 8 A 279 PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU SER
SEQRES 9 A 279 LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR GLU
SEQRES 10 A 279 LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG VAL
SEQRES 11 A 279 ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU GLY
SEQRES 12 A 279 SER ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP SER
SEQRES 13 A 279 VAL HIS ALA PRO SER SER ARG ARG THR ASP LEU CYS GLY
SEQRES 14 A 279 THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY ARG
SEQRES 15 A 279 MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY VAL
SEQRES 16 A 279 LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE GLU
SEQRES 17 A 279 ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER ARG
SEQRES 18 A 279 VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY ALA
SEQRES 19 A 279 ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO SER
SEQRES 20 A 279 GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO TRP
SEQRES 21 A 279 ILE THR ALA ASN SER SER LYS PRO SER ASN CYS GLN ASN
SEQRES 22 A 279 LYS GLU SER ALA SER LYS
HET YPH A 501 44
HETNAM YPH 1-(4-{2-[(6-{4-[2-(4-HYDROXYPIPERIDIN-1-YL)
HETNAM 2 YPH ETHOXY]PHENYL}FURO[2,3-D]PYRIMIDIN-4-YL)
HETNAM 3 YPH AMINO]ETHYL}PHENYL)-3-PHENYLUREA
FORMUL 2 YPH C34 H36 N6 O4
FORMUL 3 HOH *59(H2 O)
HELIX 1 1 ALA A 129 GLU A 131 5 3
HELIX 2 2 LYS A 166 ALA A 172 1 7
HELIX 3 3 VAL A 174 SER A 186 1 13
HELIX 4 4 THR A 217 SER A 226 1 10
HELIX 5 5 ASP A 229 LYS A 250 1 22
HELIX 6 6 LYS A 258 GLU A 260 5 3
HELIX 7 7 PRO A 297 GLU A 302 1 6
HELIX 8 8 LYS A 309 GLY A 325 1 17
HELIX 9 9 THR A 333 VAL A 344 1 12
HELIX 10 10 THR A 353 LEU A 364 1 12
HELIX 11 11 ASN A 367 ARG A 371 5 5
HELIX 12 12 MET A 373 GLU A 379 1 7
HELIX 13 13 HIS A 380 SER A 387 1 8
SHEET 1 A 5 PHE A 133 LYS A 141 0
SHEET 2 A 5 GLY A 145 GLU A 152 -1 O LEU A 149 N GLY A 136
SHEET 3 A 5 ILE A 158 PHE A 165 -1 O LEU A 161 N TYR A 148
SHEET 4 A 5 ARG A 205 LEU A 210 -1 O VAL A 206 N LEU A 164
SHEET 5 A 5 LEU A 196 HIS A 201 -1 N PHE A 200 O TYR A 207
SHEET 1 B 2 LEU A 262 LEU A 264 0
SHEET 2 B 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
SITE 1 AC1 22 ARG A 137 LEU A 139 VAL A 147 ALA A 160
SITE 2 AC1 22 LYS A 162 LEU A 164 LEU A 169 LEU A 178
SITE 3 AC1 22 GLU A 181 LEU A 210 GLU A 211 ALA A 213
SITE 4 AC1 22 PRO A 214 LEU A 215 GLY A 216 LYS A 224
SITE 5 AC1 22 LEU A 263 ASP A 274 GLY A 276 ARG A 343
SITE 6 AC1 22 HIS A 366 HOH A 606
CRYST1 80.810 80.810 174.308 90.00 90.00 120.00 P 61 2 2 12
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 0.012375 0.007145 0.000000 0.00000
SCALE2 0.000000 0.014289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END