HEADER TRANSFERASE 10-JUN-18 6GR9
TITLE HUMAN AURKC INCENP COMPLEX BOUND TO VX-680
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AURORA 3,AURORA/IPL1-RELATED KINASE 3,AURORA-RELATED KINASE
COMPND 5 3,AURORA/IPL1/EG2 PROTEIN 2,SERINE/THREONINE-PROTEIN KINASE 13,
COMPND 6 SERINE/THREONINE-PROTEIN KINASE AURORA-C;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: INNER CENTROMERE PROTEIN;
COMPND 11 CHAIN: B;
COMPND 12 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: AURKC, AIE2, AIK3, AIRK3, ARK3, STK13;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHTVAMP1-SGC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: INCENP;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHTVAMP1-SGC
KEYWDS KINASE, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.ABDUL AZEEZ,F.J.SORRELL,F.VON DELFT,C.BOUNTRA,S.KNAPP,
AUTHOR 2 A.M.EDWARDS,C.ARROWSMITH,J.M.ELKINS
REVDAT 2 17-JAN-24 6GR9 1 REMARK
REVDAT 1 15-MAY-19 6GR9 0
JRNL AUTH K.R.ABDUL AZEEZ,J.M.ELKINS
JRNL TITL AURKC INCENP COMPLEX BOUND TO BRD-7880
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22049
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1177
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2605
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : -0.38000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : -0.19000
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): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.178
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2723 ; 0.008 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 2472 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3708 ; 1.329 ; 1.674
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5790 ; 0.824 ; 1.628
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 318 ; 6.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;33.256 ;20.621
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 460 ;16.685 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;23.903 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2978 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 497 ; 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): 1269 ; 2.969 ; 4.361
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1268 ; 2.970 ; 4.357
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1582 ; 4.499 ; 6.511
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1583 ; 4.498 ; 6.515
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1454 ; 3.548 ; 4.776
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1451 ; 3.533 ; 4.761
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2116 ; 5.648 ; 7.003
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3030 ; 7.643 ;50.004
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2999 ; 7.557 ;49.856
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 : NULL
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 6GR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-14
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23264
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 71.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6GR8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350, 10 % ETHYLENE GLYCOL,
REMARK 280 0.1 M BIS-TRIS-PROPANE PH 7.5, 0.2 M SODIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 40.33333
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 80.66667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.66667
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 40.33333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 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 32
REMARK 465 ALA A 33
REMARK 465 ASN A 34
REMARK 465 SER A 35
REMARK 465 ARG A 36
REMARK 465 MET B 834
REMARK 465 GLU B 835
REMARK 465 ALA B 836
REMARK 465 HIS B 837
REMARK 465 PRO B 838
REMARK 465 ARG B 839
REMARK 465 LYS B 840
REMARK 465 LYS B 883
REMARK 465 SER B 884
REMARK 465 LYS B 885
REMARK 465 PRO B 886
REMARK 465 ARG B 887
REMARK 465 TYR B 888
REMARK 465 HIS B 889
REMARK 465 LYS B 890
REMARK 465 ARG B 891
REMARK 465 ASN B 898
REMARK 465 SER B 899
REMARK 465 PRO B 900
REMARK 465 PRO B 901
REMARK 465 LEU B 902
REMARK 465 GLN B 903
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 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 53 CE NZ
REMARK 470 ARG A 257 CZ NH1 NH2
REMARK 470 LYS A 289 CE NZ
REMARK 470 GLU B 878 CG CD OE1 OE2
REMARK 470 LYS B 882 CG CD CE NZ
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 ASP A 136 -8.61 63.11
REMARK 500 LYS A 161 31.52 70.85
REMARK 500 ASP A 166 46.82 -155.53
REMARK 500 ASP A 217 -158.61 -128.63
REMARK 500 PRO A 303 172.20 -56.93
REMARK 500 CYS A 304 -155.10 -153.47
REMARK 500 PRO B 843 151.57 -42.65
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 114 0.12 SIDE CHAIN
REMARK 500 ARG A 196 0.08 SIDE CHAIN
REMARK 500 ARG A 272 0.09 SIDE CHAIN
REMARK 500 ARG A 281 0.11 SIDE CHAIN
REMARK 500 ARG B 847 0.12 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 VX6 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
DBREF 6GR9 A 36 305 UNP Q9UQB9 AURKC_HUMAN 2 271
DBREF 6GR9 B 835 903 UNP Q9NQS7 INCE_HUMAN 835 903
SEQADV 6GR9 GLY A 32 UNP Q9UQB9 EXPRESSION TAG
SEQADV 6GR9 ALA A 33 UNP Q9UQB9 EXPRESSION TAG
SEQADV 6GR9 ASN A 34 UNP Q9UQB9 EXPRESSION TAG
SEQADV 6GR9 SER A 35 UNP Q9UQB9 EXPRESSION TAG
SEQADV 6GR9 ASP A 136 UNP Q9UQB9 GLU 102 CONFLICT
SEQADV 6GR9 MET B 834 UNP Q9NQS7 INITIATING METHIONINE
SEQRES 1 A 274 GLY ALA ASN SER ARG ARG LEU TPO VAL ASP ASP PHE GLU
SEQRES 2 A 274 ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL
SEQRES 3 A 274 TYR LEU ALA ARG LEU LYS GLU SER HIS PHE ILE VAL ALA
SEQRES 4 A 274 LEU LYS VAL LEU PHE LYS SER GLN ILE GLU LYS GLU GLY
SEQRES 5 A 274 LEU GLU HIS GLN LEU ARG ARG GLU ILE GLU ILE GLN ALA
SEQRES 6 A 274 HIS LEU GLN HIS PRO ASN ILE LEU ARG LEU TYR ASN TYR
SEQRES 7 A 274 PHE HIS ASP ALA ARG ARG VAL TYR LEU ILE LEU GLU TYR
SEQRES 8 A 274 ALA PRO ARG GLY GLU LEU TYR LYS GLU LEU GLN LYS SER
SEQRES 9 A 274 ASP LYS LEU ASP GLU GLN ARG THR ALA THR ILE ILE GLU
SEQRES 10 A 274 GLU LEU ALA ASP ALA LEU THR TYR CYS HIS ASP LYS LYS
SEQRES 11 A 274 VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU
SEQRES 12 A 274 GLY PHE ARG GLY GLU VAL LYS ILE ALA ASP PHE GLY TRP
SEQRES 13 A 274 SER VAL HIS THR PRO SER LEU ARG ARG LYS TPO MET CYS
SEQRES 14 A 274 GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY
SEQRES 15 A 274 ARG THR TYR ASP GLU LYS VAL ASP LEU TRP CYS ILE GLY
SEQRES 16 A 274 VAL LEU CYS TYR GLU LEU LEU VAL GLY TYR PRO PRO PHE
SEQRES 17 A 274 GLU SER ALA SER HIS SER GLU THR TYR ARG ARG ILE LEU
SEQRES 18 A 274 LYS VAL ASP VAL ARG PHE PRO LEU SER MET PRO LEU GLY
SEQRES 19 A 274 ALA ARG ASP LEU ILE SER ARG LEU LEU ARG TYR GLN PRO
SEQRES 20 A 274 LEU GLU ARG LEU PRO LEU ALA GLN ILE LEU LYS HIS PRO
SEQRES 21 A 274 TRP VAL GLN ALA HIS SER ARG ARG VAL LEU PRO PRO CYS
SEQRES 22 A 274 ALA
SEQRES 1 B 70 MET GLU ALA HIS PRO ARG LYS PRO ILE PRO THR TRP ALA
SEQRES 2 B 70 ARG GLY THR PRO LEU SER GLN ALA ILE ILE HIS GLN TYR
SEQRES 3 B 70 TYR HIS PRO PRO ASN LEU LEU GLU LEU PHE GLY THR ILE
SEQRES 4 B 70 LEU PRO LEU ASP LEU GLU ASP ILE PHE LYS LYS SER LYS
SEQRES 5 B 70 PRO ARG TYR HIS LYS ARG THR SEP SEP ALA VAL TRP ASN
SEQRES 6 B 70 SER PRO PRO LEU GLN
MODRES 6GR9 TPO A 39 THR MODIFIED RESIDUE
MODRES 6GR9 TPO A 198 THR MODIFIED RESIDUE
MODRES 6GR9 SEP B 893 SER MODIFIED RESIDUE
MODRES 6GR9 SEP B 894 SER MODIFIED RESIDUE
HET TPO A 39 11
HET TPO A 198 11
HET SEP B 893 10
HET SEP B 894 10
HET VX6 A 401 33
HET SO4 A 402 5
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM VX6 CYCLOPROPANECARBOXYLIC ACID {4-[4-(4-METHYL-PIPERAZIN-
HETNAM 2 VX6 1-YL)-6-(5-METHYL-2H-PYRAZOL-3-YLAMINO)-PYRIMIDIN-2-
HETNAM 3 VX6 YLSULFANYL]-PHENYL}-AMIDE
HETNAM SO4 SULFATE ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 2 SEP 2(C3 H8 N O6 P)
FORMUL 3 VX6 C23 H28 N8 O S
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *162(H2 O)
HELIX 1 AA1 TPO A 39 ASP A 41 5 3
HELIX 2 AA2 GLY A 50 LYS A 53 5 4
HELIX 3 AA3 LYS A 76 GLU A 82 1 7
HELIX 4 AA4 LEU A 84 HIS A 97 1 14
HELIX 5 AA5 LEU A 128 ASP A 136 1 9
HELIX 6 AA6 ASP A 139 LYS A 160 1 22
HELIX 7 AA7 LYS A 168 GLU A 170 5 3
HELIX 8 AA8 THR A 202 LEU A 206 5 5
HELIX 9 AA9 PRO A 207 GLU A 212 1 6
HELIX 10 AB1 LYS A 219 GLY A 235 1 17
HELIX 11 AB2 SER A 243 LYS A 253 1 11
HELIX 12 AB3 PRO A 263 LEU A 274 1 12
HELIX 13 AB4 GLN A 277 ARG A 281 5 5
HELIX 14 AB5 PRO A 283 LYS A 289 1 7
HELIX 15 AB6 HIS A 290 SER A 297 1 8
HELIX 16 AB7 PRO B 843 ALA B 846 5 4
HELIX 17 AB8 ARG B 847 HIS B 861 1 15
HELIX 18 AB9 ASN B 864 GLY B 870 1 7
HELIX 19 AC1 ASP B 876 LYS B 882 1 7
HELIX 20 AC2 THR B 892 VAL B 896 5 5
SHEET 1 AA1 5 PHE A 43 PRO A 48 0
SHEET 2 AA1 5 ASN A 56 LEU A 62 -1 O LEU A 59 N GLY A 46
SHEET 3 AA1 5 ILE A 68 PHE A 75 -1 O LEU A 71 N TYR A 58
SHEET 4 AA1 5 ARG A 115 LEU A 120 -1 O VAL A 116 N LEU A 74
SHEET 5 AA1 5 LEU A 106 HIS A 111 -1 N ASN A 108 O ILE A 119
SHEET 1 AA2 3 GLY A 126 GLU A 127 0
SHEET 2 AA2 3 LEU A 172 LEU A 174 -1 O LEU A 174 N GLY A 126
SHEET 3 AA2 3 VAL A 180 ILE A 182 -1 O LYS A 181 N LEU A 173
SHEET 1 AA3 2 VAL A 162 ILE A 163 0
SHEET 2 AA3 2 VAL A 189 HIS A 190 -1 O VAL A 189 N ILE A 163
LINK C LEU A 38 N TPO A 39 1555 1555 1.35
LINK C TPO A 39 N VAL A 40 1555 1555 1.34
LINK C LYS A 197 N TPO A 198 1555 1555 1.34
LINK C TPO A 198 N MET A 199 1555 1555 1.33
LINK C THR B 892 N SEP B 893 1555 1555 1.34
LINK C SEP B 893 N SEP B 894 1555 1555 1.34
LINK C SEP B 894 N ALA B 895 1555 1555 1.34
SITE 1 AC1 11 GLY A 50 PHE A 54 ALA A 70 GLU A 121
SITE 2 AC1 11 TYR A 122 ALA A 123 PRO A 124 GLY A 126
SITE 3 AC1 11 LEU A 173 ALA A 183 HOH A 526
SITE 1 AC2 3 SER A 77 ARG A 114 HOH A 504
CRYST1 82.617 82.617 121.000 90.00 90.00 120.00 P 31 2 1 6
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 0.012104 0.006988 0.000000 0.00000
SCALE2 0.000000 0.013977 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008264 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
