HEADER TRANSFERASE 23-MAR-16 5G15
TITLE STRUCTURE AURORA A (122-403) BOUND TO ACTIVATING MONOBODY MB1 AND
TITLE 2 AMPPCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA A KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 122-403;
COMPND 5 SYNONYM: AURORA 2, AURORA/IPL1-RELATED KINASE 1, ARK-1, AURORA-
COMPND 6 RELATED KINASE 1, HARK1, BREAST TUMOR-AMPLIFIED KINASE, SERINE/THREO
COMPND 7 -PROTEIN KINASE 15, SERINE/THREONINE-PROTEIN KINASE 6, SERINE/
COMPND 8 THREONINE-PROTEIN KINASE AURORA-A, AURORA A KINASE;
COMPND 9 EC: 2.7.11.1;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: MB1 MONOBODY;
COMPND 13 CHAIN: B;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 10 ORGANISM_TAXID: 32630;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TRANSFERASE, AURORA A, MONOBODY, AMPPCP, KINASE, ACTIVATION,
KEYWDS 2 ALLOSTERY, CELL CYCLE, CANCER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZORBA,S.KUTTER,D.KERN,S.KOIDE,A.KOIDE
REVDAT 4 10-JAN-24 5G15 1 REMARK LINK
REVDAT 3 24-JUL-19 5G15 1 AUTHOR JRNL
REVDAT 2 08-MAY-19 5G15 1 REMARK
REVDAT 1 14-MAR-18 5G15 0
JRNL AUTH A.ZORBA,V.NGUYEN,A.KOIDE,M.HOEMBERGER,Y.ZHENG,S.KUTTER,
JRNL AUTH 2 C.KIM,S.KOIDE,D.KERN
JRNL TITL ALLOSTERIC MODULATION OF A HUMAN PROTEIN KINASE WITH
JRNL TITL 2 MONOBODIES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 13937 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31239342
JRNL DOI 10.1073/PNAS.1906024116
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 29755
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1052
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2170
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.4250
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2873
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 145
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.01000
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): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.185
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.946
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3019 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2809 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4113 ; 1.916 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6472 ; 1.046 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 359 ; 7.235 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ;35.402 ;22.857
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 503 ;16.379 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.611 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3337 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 717 ; 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): 1418 ; 2.914 ; 3.189
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1417 ; 2.895 ; 3.187
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1771 ; 4.450 ; 4.764
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1600 ; 3.536 ; 3.600
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.
REMARK 4
REMARK 4 5G15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99992
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30879
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 58.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 4C3R AND 3K2M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AURORA A AND MONOBODIES WERE ALIQUOTED
REMARK 280 IN STORAGE BUFFER (20MM TRISHCL, 200MM NACL, 10% (V/V) GLYCEROL,
REMARK 280 20MM MGCL2, 5MM TCEP, PH 7.50) AND KEPT AT -80C. AMPPCP WAS
REMARK 280 PREPARED FRESH FROM POWDER THE DAY OF CRYSTALLIZATION IN
REMARK 280 CONCENTRATIONS OF 100-120MM IN STORAGE BUFFER. CRYSTALS OF AURA
REMARK 280 IN COMPLEX WITH AMPPCP AND ACTIVATING MONOBODY, MB1, WERE
REMARK 280 OBTAINED BY COMBINING 0.5UL OF [300UM AURA WITH 5MM AMPPCP AND
REMARK 280 300UM MB1] WITH 0.5UL OF MOTHER LIQUOR (0.1M MES SODIUM SALT PH
REMARK 280 6.50, 0.2M AMMONIUM SULFATE, 4% (V/V) 1,3-PROPANEDIOL, 30% (W/V)
REMARK 280 PEG8000). CRYSTALS WERE GROWN AT 18C BY VAPOR DIFFUSION AND THE
REMARK 280 SITTING DROP METHOD. THE CRYSTALS WERE WASHED WITH MOTHER LIQUOR
REMARK 280 AND FLASH FROZEN IN LIQUID NITROGEN IN PREPARATION FOR DATA
REMARK 280 COLLECTION., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 37.66950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.68050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.85750
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.66950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.68050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.85750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.66950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.68050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.85750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.66950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.68050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 71.85750
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: 3440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.7 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 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 A2110 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 GLU A 122
REMARK 465 SER A 123
REMARK 465 LYS A 124
REMARK 465 LYS A 125
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 465 GLN A 402
REMARK 465 SER A 403
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 VAL B 6
REMARK 465 PRO B 7
REMARK 465 THR B 8
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 O HOH A 2070 O HOH A 2075 2.10
REMARK 500 O HOH A 2032 O HOH A 2132 2.14
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 OE2 GLU A 376 OE2 GLU A 376 2555 2.03
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 ASP A 202 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 229 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = -3.3 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 SER A 226 -40.98 58.79
REMARK 500 ASP A 256 42.03 -151.43
REMARK 500 LEU A 364 52.72 -95.10
REMARK 500 MET B 31 127.97 -33.41
REMARK 500 THR B 45 120.06 -33.31
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 GLY B 47 ASN B 48 -144.70
REMARK 500 ASN B 48 SER B 49 147.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2072 DISTANCE = 5.96 ANGSTROMS
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 A1392 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 274 OD1
REMARK 620 2 ACP A1391 O3G 90.3
REMARK 620 3 HOH A2019 O 137.8 111.2
REMARK 620 4 HOH A2026 O 101.8 106.1 106.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 1391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1097
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5G16 RELATED DB: PDB
REMARK 900 STRUCTURE AURORA A (122-403) BOUND TO INHIBITORY MONOBODY MB2 AND
REMARK 900 AMPPCP
DBREF 5G15 A 122 403 UNP O14965 AURKA_HUMAN 122 403
DBREF 5G15 B 1 96 PDB 5G15 5G15 1 96
SEQRES 1 A 282 GLU SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE GLU
SEQRES 2 A 282 ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL
SEQRES 3 A 282 TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA
SEQRES 4 A 282 LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY
SEQRES 5 A 282 VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER
SEQRES 6 A 282 HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR
SEQRES 7 A 282 PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR
SEQRES 8 A 282 ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU
SEQRES 9 A 282 SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR
SEQRES 10 A 282 GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG
SEQRES 11 A 282 VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU
SEQRES 12 A 282 GLY SER ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP
SEQRES 13 A 282 SER VAL HIS ALA PRO SER SER ARG ARG THR THR LEU CYS
SEQRES 14 A 282 GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY
SEQRES 15 A 282 ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY
SEQRES 16 A 282 VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE
SEQRES 17 A 282 GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER
SEQRES 18 A 282 ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY
SEQRES 19 A 282 ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO
SEQRES 20 A 282 SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO
SEQRES 21 A 282 TRP ILE THR ALA ASN SER SER LYS PRO SER ASN CYS GLN
SEQRES 22 A 282 ASN LYS GLU SER ALA SER LYS GLN SER
SEQRES 1 B 96 GLY SER VAL SER SER VAL PRO THR LYS LEU GLU VAL VAL
SEQRES 2 B 96 ALA ALA THR PRO THR SER LEU LEU ILE SER TRP ASP ALA
SEQRES 3 B 96 GLN THR TYR GLN MET TYR ASP TYR VAL SER TYR TYR ARG
SEQRES 4 B 96 ILE THR TYR GLY GLU THR GLY GLY ASN SER PRO VAL GLN
SEQRES 5 B 96 GLU PHE THR VAL PRO GLY TYR TYR SER THR ALA THR ILE
SEQRES 6 B 96 SER GLY LEU LYS PRO GLY VAL ASP TYR THR ILE THR VAL
SEQRES 7 B 96 TYR ALA GLU GLY TYR TYR SER SER TYR SER PRO ILE SER
SEQRES 8 B 96 ILE ASN TYR ARG THR
HET ACP A1391 31
HET MG A1392 1
HET SO4 A1393 5
HET SO4 A1394 5
HET SO4 A1395 5
HET SO4 B1097 5
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 3 ACP C11 H18 N5 O12 P3
FORMUL 4 MG MG 2+
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 9 HOH *145(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 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 ASP A 274 SER A 278 5 5
HELIX 8 8 PRO A 282 SER A 284 5 3
HELIX 9 9 THR A 292 LEU A 296 5 5
HELIX 10 10 PRO A 297 GLU A 302 1 6
HELIX 11 11 GLU A 308 GLY A 325 1 18
HELIX 12 12 THR A 333 ARG A 343 1 11
HELIX 13 13 THR A 353 LEU A 364 1 12
HELIX 14 14 ASN A 367 ARG A 371 5 5
HELIX 15 15 MET A 373 HIS A 380 1 8
HELIX 16 16 HIS A 380 SER A 387 1 8
SHEET 1 AA 5 PHE A 133 LYS A 141 0
SHEET 2 AA 5 GLY A 145 GLU A 152 -1 O VAL A 147 N LEU A 139
SHEET 3 AA 5 PHE A 157 PHE A 165 -1 O PHE A 157 N GLU A 152
SHEET 4 AA 5 ARG A 205 LEU A 210 -1 O VAL A 206 N LEU A 164
SHEET 5 AA 5 LEU A 196 HIS A 201 -1 N TYR A 197 O ILE A 209
SHEET 1 AB 2 VAL A 252 ILE A 253 0
SHEET 2 AB 2 VAL A 279 HIS A 280 -1 O VAL A 279 N ILE A 253
SHEET 1 AC 2 LEU A 262 LEU A 264 0
SHEET 2 AC 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
SHEET 1 BA 3 GLU B 11 ALA B 15 0
SHEET 2 BA 3 LEU B 20 SER B 23 -1 O LEU B 21 N VAL B 13
SHEET 3 BA 3 THR B 62 ILE B 65 -1 O ALA B 63 N ILE B 22
SHEET 1 BB 4 GLN B 52 PRO B 57 0
SHEET 2 BB 4 VAL B 35 GLU B 44 -1 O TYR B 38 N VAL B 56
SHEET 3 BB 4 ASP B 73 GLY B 82 -1 O THR B 75 N GLY B 43
SHEET 4 BB 4 ILE B 90 ARG B 95 -1 O ILE B 90 N VAL B 78
LINK OD1 ASP A 274 MG MG A1392 1555 1555 2.54
LINK O3G ACP A1391 MG MG A1392 1555 1555 2.38
LINK MG MG A1392 O HOH A2019 1555 1555 2.85
LINK MG MG A1392 O HOH A2026 1555 1555 2.66
SITE 1 AC1 13 GLY A 140 LYS A 141 GLY A 142 LYS A 143
SITE 2 AC1 13 VAL A 147 LYS A 162 GLU A 211 ALA A 213
SITE 3 AC1 13 ASP A 274 MG A1392 HOH A2011 HOH A2012
SITE 4 AC1 13 HOH A2132
SITE 1 AC2 6 LYS A 162 GLU A 181 ASP A 274 ACP A1391
SITE 2 AC2 6 HOH A2019 HOH A2026
SITE 1 AC3 7 LYS A 153 PRO A 349 ASP A 350 PHE A 351
SITE 2 AC3 7 HOH A2106 HOH A2133 HOH A2134
SITE 1 AC4 4 ARG A 180 ARG A 255 SER A 284 HOH A2025
SITE 1 AC5 7 HIS A 248 GLU A 308 MET A 373 LEU A 374
SITE 2 AC5 7 HOH A2066 HOH A2095 HOH A2125
SITE 1 AC6 5 TYR B 42 PHE B 54 THR B 64 ILE B 65
SITE 2 AC6 5 SER B 66
CRYST1 75.339 91.361 143.715 90.00 90.00 90.00 I 2 2 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 0.013273 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006958 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
