HEADER SIGNALING PROTEIN, TRANSFERASE 07-OCT-08 3ET7
TITLE CRYSTAL STRUCTURE OF PYK2 COMPLEXED WITH PF-2318841
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE KINASE 2 BETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROLINE-RICH TYROSINE KINASE 2, FOCAL ADHESION KINASE 2,
COMPND 5 FADK 2, PROLINE-RICH TYROSINE KINASE 2, CELL ADHESION KINASE BETA,
COMPND 6 CAK BETA, CALCIUM-DEPENDENT TYROSINE KINASE, CADTK, RELATED ADHESION
COMPND 7 FOCAL TYROSINE KINASE, RAFTK;
COMPND 8 EC: 2.7.10.2;
COMPND 9 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: PTK2B, FAK2, PYK2, RAFTK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS KINASE, ALTERNATIVE SPLICING, ATP-BINDING, CELL MEMBRANE, CYTOPLASM,
KEYWDS 2 MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM,
KEYWDS 3 TRANSFERASE, TYROSINE-PROTEIN KINASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN
REVDAT 2 27-DEC-23 3ET7 1 REMARK
REVDAT 1 23-JUN-09 3ET7 0
JRNL AUTH D.P.WALKER,F.C.BI,A.S.KALGUTKAR,J.N.BAUMAN,S.X.ZHAO,
JRNL AUTH 2 J.R.SOGLIA,G.E.ASPNES,D.W.KUNG,J.KLUG-MCLEOD,M.P.ZAWISTOSKI,
JRNL AUTH 3 M.A.MCGLYNN,R.OLIVER,M.DUNN,J.C.LI,D.T.RICHTER,B.A.COOPER,
JRNL AUTH 4 J.C.KATH,C.A.HULFORD,C.L.AUTRY,M.J.LUZZIO,E.J.UNG,
JRNL AUTH 5 W.G.ROBERTS,P.C.BONNETTE,L.BUCKBINDER,A.MISTRY,M.C.GRIFFOR,
JRNL AUTH 6 S.HAN,A.GUZMAN-PEREZ
JRNL TITL TRIFLUOROMETHYLPYRIMIDINE-BASED INHIBITORS OF PROLINE-RICH
JRNL TITL 2 TYROSINE KINASE 2 (PYK2): STRUCTURE-ACTIVITY RELATIONSHIPS
JRNL TITL 3 AND STRATEGIES FOR THE ELIMINATION OF REACTIVE METABOLITE
JRNL TITL 4 FORMATION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 18 6071 2008
JRNL REFN ISSN 0960-894X
JRNL PMID 18951788
JRNL DOI 10.1016/J.BMCL.2008.10.030
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 11596
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) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 587
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 836
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4060
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.5050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.13000
REMARK 3 B22 (A**2) : -1.13000
REMARK 3 B33 (A**2) : 2.27000
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): 0.587
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.392
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.310
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.027
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2208 ; 0.032 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2993 ; 2.973 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 259 ;11.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 327 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1628 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1070 ; 0.328 ; 0.200
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): 74 ; 0.246 ; 0.200
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): 32 ; 0.329 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.431 ; 0.200
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): 1302 ; 1.448 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2120 ; 2.675 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 906 ; 3.576 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 873 ; 5.696 ; 4.500
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ET7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049736.
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 : 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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12183
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.76400
REMARK 200 R SYM FOR SHELL (I) : 0.76400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.41200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.41200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.41200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.41200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.41200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.41200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.41200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.41200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 PRO A 416
REMARK 465 GLN A 417
REMARK 465 TYR A 418
REMARK 465 TYR A 573
REMARK 465 ILE A 574
REMARK 465 GLU A 575
REMARK 465 ASP A 576
REMARK 465 GLU A 577
REMARK 465 ASP A 578
REMARK 465 TYR A 579
REMARK 465 TYR A 580
REMARK 465 LYS A 581
REMARK 465 ALA A 582
REMARK 465 SER A 583
REMARK 465 VAL A 584
REMARK 465 GLU A 692
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 ASP A 688 N ALA A 690 2.12
REMARK 500 O LYS A 522 N LEU A 524 2.17
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 ALA A 605 CA ALA A 605 CB 0.133
REMARK 500 TRP A 616 CB TRP A 616 CG -0.113
REMARK 500 PHE A 621 CE1 PHE A 621 CZ 0.116
REMARK 500 TYR A 655 CE2 TYR A 655 CD2 0.100
REMARK 500 MET A 658 CG MET A 658 SD 0.192
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 424 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU A 431 CA - CB - CG ANGL. DEV. = -16.8 DEGREES
REMARK 500 ASP A 462 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 466 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 MET A 478 CG - SD - CE ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU A 514 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU A 514 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 LEU A 528 CB - CG - CD2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 VAL A 552 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 LEU A 556 CA - CB - CG ANGL. DEV. = -17.9 DEGREES
REMARK 500 ASP A 567 CB - CG - OD2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 PHE A 568 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 PHE A 568 N - CA - C ANGL. DEV. = -22.1 DEGREES
REMARK 500 ASP A 607 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 CYS A 614 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 VAL A 653 CB - CA - C ANGL. DEV. = -14.6 DEGREES
REMARK 500 ASP A 681 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 688 CB - CG - OD2 ANGL. DEV. = 5.8 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 ASN A 428 -15.79 -141.67
REMARK 500 GLU A 438 132.92 -29.28
REMARK 500 ASN A 446 131.84 -37.40
REMARK 500 HIS A 447 -2.98 -54.28
REMARK 500 LYS A 460 -151.53 30.77
REMARK 500 THR A 464 -81.20 -18.80
REMARK 500 ASP A 466 -33.13 -32.40
REMARK 500 ASP A 482 105.06 175.90
REMARK 500 HIS A 483 129.36 -171.88
REMARK 500 GLU A 495 -152.77 173.43
REMARK 500 PRO A 497 97.66 5.08
REMARK 500 LEU A 514 -57.36 165.80
REMARK 500 ARG A 516 40.25 -78.84
REMARK 500 ASN A 517 23.41 -165.01
REMARK 500 LYS A 518 -18.26 -37.11
REMARK 500 ASN A 519 -58.76 -122.63
REMARK 500 VAL A 523 -48.25 -14.02
REMARK 500 LEU A 524 -15.87 -48.57
REMARK 500 THR A 525 -65.85 -94.71
REMARK 500 LEU A 526 -7.63 -32.41
REMARK 500 ASN A 544 65.80 33.05
REMARK 500 CYS A 562 107.99 179.64
REMARK 500 ASP A 567 85.36 87.78
REMARK 500 PHE A 568 112.37 135.69
REMARK 500 PRO A 588 68.90 -58.49
REMARK 500 ARG A 600 29.29 39.23
REMARK 500 PHE A 626 42.35 38.59
REMARK 500 LYS A 632 -38.39 -15.56
REMARK 500 PRO A 645 132.51 -31.93
REMARK 500 PRO A 651 169.76 -28.00
REMARK 500 LEU A 654 -58.86 -27.28
REMARK 500 ASP A 663 117.14 -36.67
REMARK 500 ASP A 681 -79.06 -79.38
REMARK 500 VAL A 682 2.63 -43.37
REMARK 500 GLU A 686 -35.64 -133.54
REMARK 500 ASP A 688 -85.41 -61.24
REMARK 500 ILE A 689 -2.83 -41.89
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 LYS A 460 LYS A 461 139.41
REMARK 500 LYS A 461 ASP A 462 -138.52
REMARK 500 GLU A 496 PRO A 497 -125.56
REMARK 500 TYR A 513 LEU A 514 -148.39
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 349 A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1001
DBREF 3ET7 A 416 692 UNP Q14289 FAK2_HUMAN 416 692
SEQRES 1 A 277 PRO GLN TYR GLY ILE ALA ARG GLU ASP VAL VAL LEU ASN
SEQRES 2 A 277 ARG ILE LEU GLY GLU GLY PHE PHE GLY GLU VAL TYR GLU
SEQRES 3 A 277 GLY VAL TYR THR ASN HIS LYS GLY GLU LYS ILE ASN VAL
SEQRES 4 A 277 ALA VAL LYS THR CYS LYS LYS ASP CYS THR LEU ASP ASN
SEQRES 5 A 277 LYS GLU LYS PHE MET SER GLU ALA VAL ILE MET LYS ASN
SEQRES 6 A 277 LEU ASP HIS PRO HIS ILE VAL LYS LEU ILE GLY ILE ILE
SEQRES 7 A 277 GLU GLU GLU PRO THR TRP ILE ILE MET GLU LEU TYR PRO
SEQRES 8 A 277 TYR GLY GLU LEU GLY HIS TYR LEU GLU ARG ASN LYS ASN
SEQRES 9 A 277 SER LEU LYS VAL LEU THR LEU VAL LEU TYR SER LEU GLN
SEQRES 10 A 277 ILE CYS LYS ALA MET ALA TYR LEU GLU SER ILE ASN CYS
SEQRES 11 A 277 VAL HIS ARG ASP ILE ALA VAL ARG ASN ILE LEU VAL ALA
SEQRES 12 A 277 SER PRO GLU CYS VAL LYS LEU GLY ASP PHE GLY LEU SER
SEQRES 13 A 277 ARG TYR ILE GLU ASP GLU ASP TYR TYR LYS ALA SER VAL
SEQRES 14 A 277 THR ARG LEU PRO ILE LYS TRP MET SER PRO GLU SER ILE
SEQRES 15 A 277 ASN PHE ARG ARG PHE THR THR ALA SER ASP VAL TRP MET
SEQRES 16 A 277 PHE ALA VAL CYS MET TRP GLU ILE LEU SER PHE GLY LYS
SEQRES 17 A 277 GLN PRO PHE PHE TRP LEU GLU ASN LYS ASP VAL ILE GLY
SEQRES 18 A 277 VAL LEU GLU LYS GLY ASP ARG LEU PRO LYS PRO ASP LEU
SEQRES 19 A 277 CYS PRO PRO VAL LEU TYR THR LEU MET THR ARG CYS TRP
SEQRES 20 A 277 ASP TYR ASP PRO SER ASP ARG PRO ARG PHE THR GLU LEU
SEQRES 21 A 277 VAL CYS SER LEU SER ASP VAL TYR GLN MET GLU LYS ASP
SEQRES 22 A 277 ILE ALA MET GLU
HET 349 A 999 37
HET PO4 A1001 5
HETNAM 349 5-{[4-{[2-(PYRROLIDIN-1-YLSULFONYL)BENZYL]AMINO}-5-
HETNAM 2 349 (TRIFLUOROMETHYL)PYRIMIDIN-2-YL]AMINO}-1,3-DIHYDRO-2H-
HETNAM 3 349 INDOL-2-ONE
HETNAM PO4 PHOSPHATE ION
FORMUL 2 349 C24 H21 F3 N6 O3 S
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *12(H2 O)
HELIX 1 1 ALA A 421 VAL A 425 5 5
HELIX 2 2 LEU A 465 LEU A 481 1 17
HELIX 3 3 GLY A 511 ARG A 516 1 6
HELIX 4 4 THR A 525 ILE A 543 1 19
HELIX 5 5 ALA A 551 ARG A 553 5 3
HELIX 6 6 PRO A 588 MET A 592 5 5
HELIX 7 7 SER A 593 PHE A 599 1 7
HELIX 8 8 THR A 603 LEU A 619 1 17
HELIX 9 9 GLU A 630 LYS A 632 5 3
HELIX 10 10 ASP A 633 GLY A 641 1 9
HELIX 11 11 VAL A 653 CYS A 661 1 9
HELIX 12 12 ASP A 665 ARG A 669 5 5
HELIX 13 13 ARG A 671 SER A 680 1 10
HELIX 14 14 SER A 680 MET A 685 1 6
SHEET 1 A 5 VAL A 426 GLY A 432 0
SHEET 2 A 5 VAL A 439 VAL A 443 -1 O GLU A 441 N ASN A 428
SHEET 3 A 5 ASN A 453 LYS A 457 -1 O VAL A 454 N GLY A 442
SHEET 4 A 5 TRP A 499 GLU A 503 -1 O MET A 502 N ALA A 455
SHEET 5 A 5 LEU A 489 ILE A 493 -1 N GLY A 491 O ILE A 501
SHEET 1 B 2 VAL A 546 HIS A 547 0
SHEET 2 B 2 LEU A 570 SER A 571 -1 O SER A 571 N VAL A 546
SHEET 1 C 2 ILE A 555 SER A 559 0
SHEET 2 C 2 CYS A 562 LEU A 565 -1 O LYS A 564 N LEU A 556
SITE 1 AC1 9 LEU A 431 VAL A 487 MET A 502 GLU A 503
SITE 2 AC1 9 LEU A 504 TYR A 505 GLU A 509 ARG A 553
SITE 3 AC1 9 LEU A 556
SITE 1 AC2 2 PRO A 484 HIS A 485
CRYST1 106.824 106.824 75.185 90.00 90.00 90.00 P 4 21 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 0.009361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
