HEADER TRANSFERASE 20-JAN-12 4DEE
TITLE AURORA A IN COMPLEX WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AURORA 2, AURORA/IPL1-RELATED KINASE 1, ARK-1, AURORA-
COMPND 5 RELATED KINASE 1, HARK1, BREAST TUMOR-AMPLIFIED KINASE,
COMPND 6 SERINE/THREONINE-PROTEIN KINASE 15, SERINE/THREONINE-PROTEIN KINASE
COMPND 7 6, SERINE/THREONINE-PROTEIN KINASE AURORA-A;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 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: TUNER(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-MBP
KEYWDS PROTEIN KINASE, AURORA A, DFG-IN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.MARTIN,J.-Y.ZHU,E.SCHONBRUNN
REVDAT 4 13-SEP-23 4DEE 1 REMARK SEQADV LINK
REVDAT 3 26-SEP-12 4DEE 1 JRNL
REVDAT 2 12-SEP-12 4DEE 1 JRNL
REVDAT 1 22-AUG-12 4DEE 0
JRNL AUTH H.R.LAWRENCE,M.P.MARTIN,Y.LUO,R.PIREDDU,H.YANG,H.GEVARIYA,
JRNL AUTH 2 S.OZCAN,J.Y.ZHU,R.KENDIG,M.RODRIGUEZ,R.ELIAS,J.Q.CHENG,
JRNL AUTH 3 S.M.SEBTI,E.SCHONBRUNN,N.J.LAWRENCE
JRNL TITL DEVELOPMENT OF O-CHLOROPHENYL SUBSTITUTED PYRIMIDINES AS
JRNL TITL 2 EXCEPTIONALLY POTENT AURORA KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 55 7392 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22803810
JRNL DOI 10.1021/JM300334D
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2831938.700
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15723
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 SET) : 0.213
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 787
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2420
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2223
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 113
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.22000
REMARK 3 B22 (A**2) : -2.22000
REMARK 3 B33 (A**2) : 4.44000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.750 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 36.30
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4DEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 5.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 44.7000
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) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : 36.5000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.600
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 3FDN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML AURORA A PROTEIN, 1 MM ADP,
REMARK 280 10 % (V/V) PEG 3350, 25 MM PHOSPHATE(NA/K PH 7.4), 100 MM SODIUM
REMARK 280 TARTRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.0
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 57.96333
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 115.92667
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 86.94500
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 144.90833
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 28.98167
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 57.96333
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 115.92667
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 144.90833
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 86.94500
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 28.98167
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 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 601 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 A 123
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 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 ARG A 126 88.17 -160.98
REMARK 500 ASP A 202 -161.94 -128.13
REMARK 500 SER A 226 -45.01 73.39
REMARK 500 ASP A 256 40.55 -142.00
REMARK 500 ASP A 274 72.14 61.33
REMARK 500 CYS A 290 -53.37 -125.87
REMARK 500 ASP A 307 -154.22 -143.75
REMARK 500 ASN A 392 73.42 -167.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 261 OD1
REMARK 620 2 ASP A 274 OD1 88.3
REMARK 620 3 ADP A 503 O2A 91.4 99.4
REMARK 620 4 ADP A 503 O2B 178.1 93.4 87.5
REMARK 620 5 HOH A 670 O 85.7 167.3 92.0 92.8
REMARK 620 6 HOH A 707 O 95.5 92.5 166.5 85.3 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 274 OD2
REMARK 620 2 ASP A 274 OD1 47.4
REMARK 620 3 ADP A 503 O1B 88.8 74.8
REMARK 620 4 HOH A 703 O 159.4 152.0 92.3
REMARK 620 5 HOH A 705 O 105.5 145.2 84.7 54.2
REMARK 620 6 HOH A 706 O 124.0 77.3 83.8 76.6 128.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DEA RELATED DB: PDB
REMARK 900 RELATED ID: 4DEB RELATED DB: PDB
REMARK 900 RELATED ID: 4DED RELATED DB: PDB
DBREF 4DEE A 123 401 UNP O14965 AURKA_HUMAN 123 401
SEQADV 4DEE ASP A 287 UNP O14965 THR 287 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 ASP THR 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 MG A 501 1
HET MG A 502 1
HET ADP A 503 27
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 MG 2(MG 2+)
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 HOH *113(H2 O)
HELIX 1 1 ALA A 129 GLU A 131 5 3
HELIX 2 2 LYS A 166 GLY A 173 1 8
HELIX 3 3 VAL A 174 LEU A 188 1 15
HELIX 4 4 THR A 217 SER A 226 1 10
HELIX 5 5 ASP A 229 SER A 249 1 21
HELIX 6 6 LYS A 258 GLU A 260 5 3
HELIX 7 7 ASP A 274 SER A 278 5 5
HELIX 8 8 PRO A 297 GLU A 302 1 6
HELIX 9 9 GLU A 308 GLY A 325 1 18
HELIX 10 10 THR A 333 VAL A 344 1 12
HELIX 11 11 THR A 353 LEU A 364 1 12
HELIX 12 12 ASN A 367 ARG A 371 5 5
HELIX 13 13 MET A 373 GLU A 379 1 7
HELIX 14 14 HIS A 380 SER A 387 1 8
SHEET 1 A 5 PHE A 133 LYS A 141 0
SHEET 2 A 5 ASN A 146 GLU A 152 -1 O VAL A 147 N LEU A 139
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 LEU A 210 N ALA A 160
SHEET 5 A 5 LEU A 196 HIS A 201 -1 N PHE A 200 O TYR A 207
SHEET 1 B 2 VAL A 252 ILE A 253 0
SHEET 2 B 2 VAL A 279 HIS A 280 -1 O VAL A 279 N ILE A 253
SHEET 1 C 2 LEU A 262 LEU A 264 0
SHEET 2 C 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
LINK OD1 ASN A 261 MG MG A 501 1555 1555 2.13
LINK OD1 ASP A 274 MG MG A 501 1555 1555 2.11
LINK OD2 ASP A 274 MG MG A 502 1555 1555 2.19
LINK OD1 ASP A 274 MG MG A 502 1555 1555 2.98
LINK MG MG A 501 O2A ADP A 503 1555 1555 1.98
LINK MG MG A 501 O2B ADP A 503 1555 1555 2.16
LINK MG MG A 501 O HOH A 670 1555 1555 2.25
LINK MG MG A 501 O HOH A 707 1555 1555 2.04
LINK MG MG A 502 O1B ADP A 503 1555 1555 2.23
LINK MG MG A 502 O HOH A 703 1555 1555 2.69
LINK MG MG A 502 O HOH A 705 1555 1555 2.45
LINK MG MG A 502 O HOH A 706 1555 1555 2.16
CISPEP 1 ALA A 281 PRO A 282 0 -0.03
SITE 1 AC1 5 ASN A 261 ASP A 274 ADP A 503 HOH A 670
SITE 2 AC1 5 HOH A 707
SITE 1 AC2 6 ASP A 274 ADP A 503 HOH A 703 HOH A 704
SITE 2 AC2 6 HOH A 705 HOH A 706
SITE 1 AC3 24 LEU A 139 GLY A 140 LYS A 141 GLY A 142
SITE 2 AC3 24 LYS A 143 VAL A 147 ALA A 160 LYS A 162
SITE 3 AC3 24 LEU A 194 GLU A 211 ALA A 213 THR A 217
SITE 4 AC3 24 GLU A 260 ASN A 261 LEU A 263 ASP A 274
SITE 5 AC3 24 MG A 501 MG A 502 HOH A 622 HOH A 626
SITE 6 AC3 24 HOH A 667 HOH A 670 HOH A 706 HOH A 707
CRYST1 81.110 81.110 173.890 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 0.012329 0.007118 0.000000 0.00000
SCALE2 0.000000 0.014236 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005751 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
