HEADER TRANSFERASE/CELL CYCLE 20-AUG-13 4C2V
TITLE AURORA B KINASE IN COMPLEX WITH THE SPECIFIC INHIBITOR
TITLE 2 BARASERTIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE B-A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 76-360;
COMPND 5 SYNONYM: AURORA/IPL1-RELATED KINASE 2-A, AIRK2-A, XAIRK2-A,
COMPND 6 SERINE/THREONINE-PROTEIN KINASE 12-A, SERINE/THREONINE-PROTEIN
COMPND 7 KINASE AURORA-B-A, XAURORA-B;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: INNER CENTROMERE PROTEIN A;
COMPND 12 CHAIN: C, D;
COMPND 13 FRAGMENT: RESIDUES 797-840;
COMPND 14 SYNONYM: XL-INCENP, XINC, XINCENP, MITOTIC PHOSPHOPROTEIN 130;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 9 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 10 ORGANISM_TAXID: 8355;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE-CELL CYCLE COMPLEX, AZD1152
EXPDTA X-RAY DIFFRACTION
AUTHOR F.SESSA,F.VILLA
REVDAT 3 19-MAR-14 4C2V 1 JRNL
REVDAT 2 12-MAR-14 4C2V 1 JRNL
REVDAT 1 26-FEB-14 4C2V 0
JRNL AUTH F.SESSA,F.VILLA
JRNL TITL STRUCTURE OF AURORA B-INCENP IN COMPLEX WITH BARASERTIB
JRNL TITL 2 REVEALS A POTENTIAL TRANSINHIBITORY MECHANISM
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 70 294 2014
JRNL REFN ISSN 1744-3091
JRNL PMID 24598913
JRNL DOI 10.1107/S2053230X14002118
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.51
REMARK 3 NUMBER OF REFLECTIONS : 109518
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) : 0.16817
REMARK 3 R VALUE (WORKING SET) : 0.16662
REMARK 3 FREE R VALUE : 0.19747
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5766
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) : 1.491
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.530
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6564
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.269
REMARK 3 BIN FREE R VALUE SET COUNT : 346
REMARK 3 BIN FREE R VALUE : 0.282
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5277
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 595
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.431
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10
REMARK 3 B22 (A**2) : -0.14
REMARK 3 B33 (A**2) : 0.05
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.02
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.216
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5581 ; 0.025 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5380 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7532 ; 2.370 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12407 ; 1.168 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 648 ; 7.373 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 269 ;36.101 ;22.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1009 ;15.777 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;17.134 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 766 ; 0.219 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6168 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1337 ; 0.002 ; 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 : 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. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4C2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-13.
REMARK 100 THE PDBE ID CODE IS EBI-58098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115022
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.49
REMARK 200 RESOLUTION RANGE LOW (A) : 45.76
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.6
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.3
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.60
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: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 34.05050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 350
REMARK 350 BIOMOLECULE: 2
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: 3480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 GLN A 76
REMARK 465 ASN A 77
REMARK 465 THR A 78
REMARK 465 ALA A 79
REMARK 465 LEU A 80
REMARK 465 ALA A 81
REMARK 465 GLU A 82
REMARK 465 MET A 83
REMARK 465 PRO A 84
REMARK 465 LYS A 85
REMARK 465 ARG A 86
REMARK 465 THR A 358
REMARK 465 GLN A 359
REMARK 465 SER A 360
REMARK 465 SER B 357
REMARK 465 THR B 358
REMARK 465 GLN B 359
REMARK 465 SER B 360
REMARK 465 ASN C 838
REMARK 465 LYS C 839
REMARK 465 SER C 840
REMARK 465 PRO D 797
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 101 OD1 ASN A 106 2.08
REMARK 500 NH2 ARG A 139 O HOH A 2039 2.10
REMARK 500 OE1 GLU A 143 O HOH A 2047 2.02
REMARK 500 OD2 ASP B 94 O HOH B 2024 1.70
REMARK 500 NE2 GLN B 114 O HOH B 2013 2.17
REMARK 500 ND1 HIS B 185 O HOH B 2119 1.95
REMARK 500 CE1 HIS B 185 O HOH B 2119 1.73
REMARK 500 CZ ARG B 348 O HOH B 2277 1.89
REMARK 500 NH2 ARG B 348 O HOH B 2277 1.73
REMARK 500 O HOH A 2008 O HOH A 2009 1.90
REMARK 500 O HOH A 2076 O HOH A 2083 1.16
REMARK 500 O HOH A 2118 O HOH A 2241 1.60
REMARK 500 O HOH A 2124 O HOH A 2251 2.15
REMARK 500 O HOH A 2178 O HOH A 2198 1.36
REMARK 500 O HOH A 2200 O HOH A 2202 1.71
REMARK 500 O HOH A 2240 O HOH A 2241 2.11
REMARK 500 O HOH A 2274 O HOH A 2277 2.12
REMARK 500 O HOH B 2052 O HOH B 2073 2.07
REMARK 500 O HOH B 2229 O HOH B 2231 1.29
REMARK 500 O HOH B 2230 O HOH B 2232 2.07
REMARK 500 O HOH D 2021 O HOH A 2073 1.36
REMARK 500
REMARK 500 REMARK: NULL
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 NH1 ARG A 348 O HOH A 2197 1655 1.99
REMARK 500 O HOH A 2007 O HOH A 2214 2555 1.43
REMARK 500 O HOH A 2008 O HOH A 2212 2555 1.21
REMARK 500 O HOH A 2032 O HOH A 2098 2555 1.16
REMARK 500 O HOH B 2229 O HOH A 2258 1565 2.12
REMARK 500 O HOH C 2001 O HOH B 2223 2746 1.21
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 GLU A 209 CD GLU A 209 OE1 0.123
REMARK 500 GLU A 229 CD GLU A 229 OE1 -0.074
REMARK 500 ARG A 246 CD ARG A 246 NE -0.166
REMARK 500 GLU A 259 CD GLU A 259 OE1 0.084
REMARK 500 GLU B 143 CD GLU B 143 OE1 0.110
REMARK 500 GLU B 143 CG GLU B 143 CD 0.103
REMARK 500 GLU B 199 CD GLU B 199 OE2 0.079
REMARK 500 GLU B 220 CD GLU B 220 OE1 0.096
REMARK 500 GLU B 229 CD GLU B 229 OE1 -0.089
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 140 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 163 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 163 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 GLU A 209 CG - CD - OE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 GLU A 229 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 271 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 PHE A 282 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 325 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 349 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET B 83 CG - SD - CE ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP B 162 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 187 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 189 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 210 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 215 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET B 260 CG - SD - CE ANGL. DEV. = -19.3 DEGREES
REMARK 500 ARG B 325 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 325 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG B 331 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR C 815 CB - CG - CD1 ANGL. DEV. = 4.3 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 101 -137.15 -96.43
REMARK 500 ASN A 158 -172.73 -173.69
REMARK 500 ASP A 162 -158.34 -127.02
REMARK 500 ASP A 216 47.41 -153.62
REMARK 500 SER A 243 -39.87 -137.86
REMARK 500 LYS B 101 42.20 -108.50
REMARK 500 ASN B 158 -172.34 -174.79
REMARK 500 ASP B 162 -167.34 -127.56
REMARK 500 ARG B 215 -4.14 75.14
REMARK 500 ASP B 216 48.89 -145.33
REMARK 500 VAL B 354 -144.53 85.50
REMARK 500 TYR B 355 174.21 172.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE B 104 GLY B 105 77.15
REMARK 500 PRO B 353 VAL B 354 49.55
REMARK 500 VAL B 354 TYR B 355 -147.55
REMARK 500 TYR B 355 GLN B 356 46.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 THR B 89 -25.4 R S C-BETA WRONG HAND
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 YJA A1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YJA B1357
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C2W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AURORA B IN COMPLEX WITH AMP-PNP
DBREF 4C2V A 76 360 UNP Q6DE08 AUKBA_XENLA 76 360
DBREF 4C2V B 76 360 UNP Q6DE08 AUKBA_XENLA 76 360
DBREF 4C2V C 797 840 UNP O13024 INCEA_XENLA 797 840
DBREF 4C2V D 797 840 UNP O13024 INCEA_XENLA 797 840
SEQRES 1 A 285 GLN ASN THR ALA LEU ALA GLU MET PRO LYS ARG LYS PHE
SEQRES 2 A 285 THR ILE ASP ASP PHE ASP ILE GLY ARG PRO LEU GLY LYS
SEQRES 3 A 285 GLY LYS PHE GLY ASN VAL TYR LEU ALA ARG GLU LYS GLN
SEQRES 4 A 285 ASN LYS PHE ILE MET ALA LEU LYS VAL LEU PHE LYS SER
SEQRES 5 A 285 GLN LEU GLU LYS GLU GLY VAL GLU HIS GLN LEU ARG ARG
SEQRES 6 A 285 GLU ILE GLU ILE GLN SER HIS LEU ARG HIS PRO ASN ILE
SEQRES 7 A 285 LEU ARG MET TYR ASN TYR PHE HIS ASP ARG LYS ARG ILE
SEQRES 8 A 285 TYR LEU MET LEU GLU PHE ALA PRO ARG GLY GLU LEU TYR
SEQRES 9 A 285 LYS GLU LEU GLN LYS HIS GLY ARG PHE ASP GLU GLN ARG
SEQRES 10 A 285 SER ALA THR PHE MET GLU GLU LEU ALA ASP ALA LEU HIS
SEQRES 11 A 285 TYR CYS HIS GLU ARG LYS VAL ILE HIS ARG ASP ILE LYS
SEQRES 12 A 285 PRO GLU ASN LEU LEU MET GLY TYR LYS GLY GLU LEU LYS
SEQRES 13 A 285 ILE ALA ASP PHE GLY TRP SER VAL HIS ALA PRO SER LEU
SEQRES 14 A 285 ARG ARG ARG TPO MET CYS GLY THR LEU ASP TYR LEU PRO
SEQRES 15 A 285 PRO GLU MET ILE GLU GLY LYS THR HIS ASP GLU LYS VAL
SEQRES 16 A 285 ASP LEU TRP CYS ALA GLY VAL LEU CYS TYR GLU PHE LEU
SEQRES 17 A 285 VAL GLY MET PRO PRO PHE ASP SER PRO SER HIS THR GLU
SEQRES 18 A 285 THR HIS ARG ARG ILE VAL ASN VAL ASP LEU LYS PHE PRO
SEQRES 19 A 285 PRO PHE LEU SER ASP GLY SER LYS ASP LEU ILE SER LYS
SEQRES 20 A 285 LEU LEU ARG TYR HIS PRO PRO GLN ARG LEU PRO LEU LYS
SEQRES 21 A 285 GLY VAL MET GLU HIS PRO TRP VAL LYS ALA ASN SER ARG
SEQRES 22 A 285 ARG VAL LEU PRO PRO VAL TYR GLN SER THR GLN SER
SEQRES 1 B 285 GLN ASN THR ALA LEU ALA GLU MET PRO LYS ARG LYS PHE
SEQRES 2 B 285 THR ILE ASP ASP PHE ASP ILE GLY ARG PRO LEU GLY LYS
SEQRES 3 B 285 GLY LYS PHE GLY ASN VAL TYR LEU ALA ARG GLU LYS GLN
SEQRES 4 B 285 ASN LYS PHE ILE MET ALA LEU LYS VAL LEU PHE LYS SER
SEQRES 5 B 285 GLN LEU GLU LYS GLU GLY VAL GLU HIS GLN LEU ARG ARG
SEQRES 6 B 285 GLU ILE GLU ILE GLN SER HIS LEU ARG HIS PRO ASN ILE
SEQRES 7 B 285 LEU ARG MET TYR ASN TYR PHE HIS ASP ARG LYS ARG ILE
SEQRES 8 B 285 TYR LEU MET LEU GLU PHE ALA PRO ARG GLY GLU LEU TYR
SEQRES 9 B 285 LYS GLU LEU GLN LYS HIS GLY ARG PHE ASP GLU GLN ARG
SEQRES 10 B 285 SER ALA THR PHE MET GLU GLU LEU ALA ASP ALA LEU HIS
SEQRES 11 B 285 TYR CYS HIS GLU ARG LYS VAL ILE HIS ARG ASP ILE LYS
SEQRES 12 B 285 PRO GLU ASN LEU LEU MET GLY TYR LYS GLY GLU LEU LYS
SEQRES 13 B 285 ILE ALA ASP PHE GLY TRP SER VAL HIS ALA PRO SER LEU
SEQRES 14 B 285 ARG ARG ARG TPO MET CYS GLY THR LEU ASP TYR LEU PRO
SEQRES 15 B 285 PRO GLU MET ILE GLU GLY LYS THR HIS ASP GLU LYS VAL
SEQRES 16 B 285 ASP LEU TRP CYS ALA GLY VAL LEU CYS TYR GLU PHE LEU
SEQRES 17 B 285 VAL GLY MET PRO PRO PHE ASP SER PRO SER HIS THR GLU
SEQRES 18 B 285 THR HIS ARG ARG ILE VAL ASN VAL ASP LEU LYS PHE PRO
SEQRES 19 B 285 PRO PHE LEU SER ASP GLY SER LYS ASP LEU ILE SER LYS
SEQRES 20 B 285 LEU LEU ARG TYR HIS PRO PRO GLN ARG LEU PRO LEU LYS
SEQRES 21 B 285 GLY VAL MET GLU HIS PRO TRP VAL LYS ALA ASN SER ARG
SEQRES 22 B 285 ARG VAL LEU PRO PRO VAL TYR GLN SER THR GLN SER
SEQRES 1 C 44 PRO ILE PRO ALA TRP ALA SER GLY ASN LEU LEU THR GLN
SEQRES 2 C 44 ALA ILE ARG GLN GLN TYR TYR LYS PRO ILE ASP VAL ASP
SEQRES 3 C 44 ARG MET TYR GLY THR ILE ASP SER PRO LYS LEU GLU GLU
SEQRES 4 C 44 LEU PHE ASN LYS SER
SEQRES 1 D 44 PRO ILE PRO ALA TRP ALA SER GLY ASN LEU LEU THR GLN
SEQRES 2 D 44 ALA ILE ARG GLN GLN TYR TYR LYS PRO ILE ASP VAL ASP
SEQRES 3 D 44 ARG MET TYR GLY THR ILE ASP SER PRO LYS LEU GLU GLU
SEQRES 4 D 44 LEU PHE ASN LYS SER
MODRES 4C2V TPO A 248 THR PHOSPHOTHREONINE
MODRES 4C2V TPO B 248 THR PHOSPHOTHREONINE
HET TPO A 248 11
HET TPO B 248 11
HET YJA A1357 37
HET YJA B1357 37
HETNAM TPO PHOSPHOTHREONINE
HETNAM YJA 2-[5-[[7-[3-[ETHYL(2-HYDROXYETHYL)AMINO]
HETNAM 2 YJA PROPOXY]QUINAZOLIN-4-YL]AMINO]-1H-PYRAZOL-3-YL]-N-
HETNAM 3 YJA (3-FLUOROPHENYL)ETHANAMIDE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 3 TPO 2(C4 H10 N O6 P)
FORMUL 4 YJA 2(C26 H30 F N7 O3)
FORMUL 5 HOH *595(H2 O)
HELIX 1 1 THR A 89 ASP A 91 5 3
HELIX 2 2 LYS A 126 GLU A 132 1 7
HELIX 3 3 VAL A 134 HIS A 147 1 14
HELIX 4 4 LEU A 178 GLY A 186 1 9
HELIX 5 5 ASP A 189 GLU A 209 1 21
HELIX 6 6 LYS A 218 GLU A 220 5 3
HELIX 7 7 THR A 252 LEU A 256 5 5
HELIX 8 8 PRO A 257 GLU A 262 1 6
HELIX 9 9 LYS A 269 GLY A 285 1 17
HELIX 10 10 SER A 293 ASN A 303 1 11
HELIX 11 11 SER A 313 LEU A 324 1 12
HELIX 12 12 HIS A 327 ARG A 331 5 5
HELIX 13 13 PRO A 333 GLU A 339 1 7
HELIX 14 14 HIS A 340 SER A 347 1 8
HELIX 15 15 THR B 89 ASP B 91 5 3
HELIX 16 16 LYS B 103 GLY B 105 5 3
HELIX 17 17 LYS B 126 GLU B 132 1 7
HELIX 18 18 VAL B 134 SER B 146 1 13
HELIX 19 19 LEU B 178 GLY B 186 1 9
HELIX 20 20 ASP B 189 ARG B 210 1 22
HELIX 21 21 LYS B 218 GLU B 220 5 3
HELIX 22 22 THR B 252 LEU B 256 5 5
HELIX 23 23 PRO B 257 GLU B 262 1 6
HELIX 24 24 LYS B 269 GLY B 285 1 17
HELIX 25 25 SER B 293 ASN B 303 1 11
HELIX 26 26 SER B 313 LEU B 324 1 12
HELIX 27 27 HIS B 327 ARG B 331 5 5
HELIX 28 28 PRO B 333 GLU B 339 1 7
HELIX 29 29 HIS B 340 SER B 347 1 8
HELIX 30 30 PRO C 799 ALA C 802 5 4
HELIX 31 31 SER C 803 LYS C 817 1 15
HELIX 32 32 ASP C 820 TYR C 825 1 6
HELIX 33 33 LYS C 832 PHE C 837 1 6
HELIX 34 34 PRO D 799 ALA D 802 5 4
HELIX 35 35 SER D 803 LYS D 817 1 15
HELIX 36 36 ASP D 820 TYR D 825 1 6
HELIX 37 37 LYS D 832 LEU D 836 5 5
SHEET 1 AA 5 PHE A 93 GLY A 100 0
SHEET 2 AA 5 ASN A 106 GLU A 112 -1 O VAL A 107 N LEU A 99
SHEET 3 AA 5 PHE A 117 PHE A 125 -1 O PHE A 117 N GLU A 112
SHEET 4 AA 5 ARG A 165 LEU A 170 -1 O ILE A 166 N LEU A 124
SHEET 5 AA 5 MET A 156 HIS A 161 -1 N TYR A 157 O MET A 169
SHEET 1 AB 3 GLY A 176 GLU A 177 0
SHEET 2 AB 3 LEU A 222 MET A 224 -1 N MET A 224 O GLY A 176
SHEET 3 AB 3 LEU A 230 ILE A 232 -1 O LYS A 231 N LEU A 223
SHEET 1 AC 2 VAL A 212 ILE A 213 0
SHEET 2 AC 2 VAL A 239 HIS A 240 -1 O VAL A 239 N ILE A 213
SHEET 1 BA 5 PHE B 93 PRO B 98 0
SHEET 2 BA 5 VAL B 107 GLU B 112 -1 O LEU B 109 N GLY B 96
SHEET 3 BA 5 PHE B 117 PHE B 125 -1 O PHE B 117 N GLU B 112
SHEET 4 BA 5 ARG B 165 LEU B 170 -1 O ILE B 166 N LEU B 124
SHEET 5 BA 5 MET B 156 HIS B 161 -1 N TYR B 157 O MET B 169
SHEET 1 BB 3 GLY B 176 GLU B 177 0
SHEET 2 BB 3 LEU B 222 MET B 224 -1 N MET B 224 O GLY B 176
SHEET 3 BB 3 LEU B 230 ILE B 232 -1 O LYS B 231 N LEU B 223
SHEET 1 BC 2 VAL B 212 ILE B 213 0
SHEET 2 BC 2 VAL B 239 HIS B 240 -1 O VAL B 239 N ILE B 213
LINK C ARG A 247 N TPO A 248 1555 1555 1.33
LINK C TPO A 248 N MET A 249 1555 1555 1.32
LINK C ARG B 247 N TPO B 248 1555 1555 1.31
LINK C TPO B 248 N MET B 249 1555 1555 1.32
CISPEP 1 GLY B 102 LYS B 103 0 20.18
SITE 1 AC1 18 PHE A 104 LYS A 122 LEU A 138 GLU A 141
SITE 2 AC1 18 GLN A 145 LEU A 154 MET A 156 LEU A 168
SITE 3 AC1 18 GLU A 171 PHE A 172 ALA A 173 PRO A 174
SITE 4 AC1 18 GLY A 176 LEU A 223 ALA A 233 HOH A2012
SITE 5 AC1 18 HOH A2043 HOH A2096
SITE 1 AC2 19 LEU B 99 PHE B 104 LYS B 122 LEU B 138
SITE 2 AC2 19 GLU B 141 GLN B 145 LEU B 154 MET B 156
SITE 3 AC2 19 LEU B 168 LEU B 170 GLU B 171 PHE B 172
SITE 4 AC2 19 ALA B 173 PRO B 174 GLY B 176 LEU B 223
SITE 5 AC2 19 ALA B 233 HOH B2108 HOH B2110
CRYST1 46.065 68.101 117.087 90.00 96.65 90.00 P 1 21 1 1
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 0.021708 0.000000 0.002531 0.00000
SCALE2 0.000000 0.014684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008599 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
