HEADER TRANSFERASE 09-APR-12 4EKU
TITLE CRYSTAL STRUCTURE OF FERM DOMAIN OF PROLINE-RICH TYROSINE KINASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE KINASE 2-BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 21-409;
COMPND 5 SYNONYM: CALCIUM-DEPENDENT TYROSINE KINASE, CADTK, CALCIUM-REGULATED
COMPND 6 NON-RECEPTOR PROLINE-RICH TYROSINE KINASE, CELL ADHESION KINASE BETA,
COMPND 7 CAK-BETA, CAKB, FOCAL ADHESION KINASE 2, FADK 2, PROLINE-RICH
COMPND 8 TYROSINE KINASE 2, RELATED ADHESION FOCAL TYROSINE KINASE, RAFTK;
COMPND 9 EC: 2.7.10.2;
COMPND 10 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: FAK2, NM4103, PTK2B, PYK2, RAFTK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PROLINE-RICH TYROSINE KINASE 2; FERM DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SAVARIMUTHU,R.LI,Y.WANG
REVDAT 2 13-SEP-23 4EKU 1 SEQADV
REVDAT 1 25-APR-12 4EKU 0
JRNL AUTH B.SAVARIMUTHU,R.LI,Y.WANG
JRNL TITL CRYSTAL STRUCTURE OF THE FERM DOMAIN OF PROLINE-RICH
JRNL TITL 2 TYROSINE KINASE 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 12393
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 546
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) : 3.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 853
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 44
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 0.80000
REMARK 3 B12 (A**2) : -0.27000
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): 1.334
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.341
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.229
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.600
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2868 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3869 ; 2.215 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 347 ; 8.337 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;40.580 ;24.685
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 535 ;24.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;22.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2167 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1735 ; 0.934 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2802 ; 1.801 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1133 ; 2.330 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1067 ; 4.128 ; 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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 19 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5360 13.4510 -26.8050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2746 T22: 0.5644
REMARK 3 T33: 0.2008 T12: -0.0954
REMARK 3 T13: 0.1149 T23: -0.2077
REMARK 3 L TENSOR
REMARK 3 L11: 3.2763 L22: 8.4751
REMARK 3 L33: 3.9530 L12: -2.5839
REMARK 3 L13: -1.3141 L23: 3.3429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.3384 S13: 0.0600
REMARK 3 S21: 0.0683 S22: -0.1781 S23: 0.6404
REMARK 3 S31: -0.1987 S32: -0.1183 S33: 0.0941
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 139 A 264
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7380 36.2210 -8.9620
REMARK 3 T TENSOR
REMARK 3 T11: 0.5847 T22: 0.6715
REMARK 3 T33: 0.0916 T12: -0.0694
REMARK 3 T13: -0.0835 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 3.4384 L22: 12.2523
REMARK 3 L33: 3.0321 L12: 3.3006
REMARK 3 L13: 0.2590 L23: 2.9534
REMARK 3 S TENSOR
REMARK 3 S11: -0.2486 S12: 0.4739 S13: 0.0032
REMARK 3 S21: 0.2308 S22: 0.2202 S23: -0.5851
REMARK 3 S31: -0.2025 S32: 0.6490 S33: 0.0284
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 265 A 366
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8290 14.4360 -8.2480
REMARK 3 T TENSOR
REMARK 3 T11: 0.8562 T22: 0.5693
REMARK 3 T33: 0.8965 T12: -0.2200
REMARK 3 T13: 0.5448 T23: -0.2944
REMARK 3 L TENSOR
REMARK 3 L11: 11.7341 L22: 6.9847
REMARK 3 L33: 6.0799 L12: -0.5832
REMARK 3 L13: -0.5776 L23: 2.1640
REMARK 3 S TENSOR
REMARK 3 S11: -0.1142 S12: -0.1352 S13: -0.5265
REMARK 3 S21: 0.7066 S22: -0.3841 S23: 1.9709
REMARK 3 S31: 0.5098 S32: -0.7659 S33: 0.4983
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4EKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI 111)
REMARK 200 OPTICS : ROSENBAUM-ROCH DOUBLE XTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12393
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 49.564
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.77400
REMARK 200 R SYM FOR SHELL (I) : 0.74400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2AL6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM CITRATE TRIBASIC, PH 7.0,
REMARK 280 0.1 M BIS-TRIS PROPANE PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 68.89000
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 34.44500
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 34.44500
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 68.89000
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -68.89000
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 MET A 18
REMARK 465 ARG A 367
REMARK 465 LYS A 368
REMARK 465 ASP A 369
REMARK 465 GLY A 370
REMARK 465 GLU A 371
REMARK 465 LYS A 372
REMARK 465 ARG A 373
REMARK 465 ASN A 374
REMARK 465 SER A 375
REMARK 465 LEU A 376
REMARK 465 PRO A 377
REMARK 465 GLN A 378
REMARK 465 ILE A 379
REMARK 465 PRO A 380
REMARK 465 MET A 381
REMARK 465 LEU A 382
REMARK 465 ASN A 383
REMARK 465 LEU A 384
REMARK 465 GLU A 385
REMARK 465 ALA A 386
REMARK 465 ARG A 387
REMARK 465 ARG A 388
REMARK 465 SER A 389
REMARK 465 HIS A 390
REMARK 465 LEU A 391
REMARK 465 SER A 392
REMARK 465 GLU A 393
REMARK 465 SER A 394
REMARK 465 CYS A 395
REMARK 465 SER A 396
REMARK 465 ILE A 397
REMARK 465 GLU A 398
REMARK 465 SER A 399
REMARK 465 ASP A 400
REMARK 465 ILE A 401
REMARK 465 TYR A 402
REMARK 465 ALA A 403
REMARK 465 GLU A 404
REMARK 465 ILE A 405
REMARK 465 PRO A 406
REMARK 465 ASP A 407
REMARK 465 GLU A 408
REMARK 465 THR A 409
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 LYS A 198 CG CD CE NZ
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 LYS A 295 CG CD CE NZ
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 TYR A 118 N LEU A 121 2.18
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 CYS A 44 CB CYS A 44 SG -0.127
REMARK 500 GLU A 101 CG GLU A 101 CD 0.100
REMARK 500 CYS A 246 CB CYS A 246 SG -0.109
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 PRO A 82 C - N - CA ANGL. DEV. = 11.7 DEGREES
REMARK 500 PRO A 107 C - N - CA ANGL. DEV. = 9.7 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 PRO A 22 -173.76 -50.33
REMARK 500 SER A 47 156.38 176.77
REMARK 500 ASN A 48 34.28 -75.57
REMARK 500 PHE A 50 40.06 -84.44
REMARK 500 PRO A 52 -88.77 13.61
REMARK 500 CYS A 61 -159.98 -161.71
REMARK 500 VAL A 63 -32.62 -33.63
REMARK 500 SER A 77 -17.53 -48.36
REMARK 500 PRO A 82 -125.50 -78.83
REMARK 500 ASN A 83 92.73 -64.29
REMARK 500 LYS A 98 -73.18 -64.16
REMARK 500 ASP A 100 49.95 -103.34
REMARK 500 PRO A 107 -46.05 -27.77
REMARK 500 GLU A 119 -9.02 -56.03
REMARK 500 ARG A 134 -39.53 -137.11
REMARK 500 PHE A 140 -126.23 46.90
REMARK 500 MET A 141 -29.87 -39.28
REMARK 500 SER A 171 141.85 -36.85
REMARK 500 PHE A 187 56.21 -108.42
REMARK 500 LYS A 188 161.68 -44.00
REMARK 500 ASP A 189 -12.11 70.85
REMARK 500 ASN A 193 22.81 -140.89
REMARK 500 ALA A 194 -75.67 -48.71
REMARK 500 LEU A 195 -18.90 -36.58
REMARK 500 VAL A 208 -31.88 -132.04
REMARK 500 PHE A 257 -70.79 -92.10
REMARK 500 GLN A 271 -163.82 -165.76
REMARK 500 SER A 291 97.61 -55.97
REMARK 500 GLN A 292 -25.95 78.83
REMARK 500 ALA A 294 -35.17 -33.33
REMARK 500 SER A 307 115.63 -172.26
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 LEU A 313 GLU A 314 -149.37
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4EKU A 21 409 UNP Q14289 FAK2_HUMAN 21 409
SEQADV 4EKU MET A 18 UNP Q14289 EXPRESSION TAG
SEQADV 4EKU GLU A 19 UNP Q14289 EXPRESSION TAG
SEQADV 4EKU LEU A 20 UNP Q14289 EXPRESSION TAG
SEQRES 1 A 392 MET GLU LEU GLY PRO ALA GLU PRO MET VAL VAL VAL PRO
SEQRES 2 A 392 VAL ASP VAL GLU LYS GLU ASP VAL ARG ILE LEU LYS VAL
SEQRES 3 A 392 CYS PHE TYR SER ASN SER PHE ASN PRO GLY LYS ASN PHE
SEQRES 4 A 392 LYS LEU VAL LYS CYS THR VAL GLN THR GLU ILE ARG GLU
SEQRES 5 A 392 ILE ILE THR SER ILE LEU LEU SER GLY ARG ILE GLY PRO
SEQRES 6 A 392 ASN ILE ARG LEU ALA GLU CYS TYR GLY LEU ARG LEU LYS
SEQRES 7 A 392 HIS MET LYS SER ASP GLU ILE HIS TRP LEU HIS PRO GLN
SEQRES 8 A 392 MET THR VAL GLY GLU VAL GLN ASP LYS TYR GLU CYS LEU
SEQRES 9 A 392 HIS VAL GLU ALA GLU TRP ARG TYR ASP LEU GLN ILE ARG
SEQRES 10 A 392 TYR LEU PRO GLU ASP PHE MET GLU SER LEU LYS GLU ASP
SEQRES 11 A 392 ARG THR THR LEU LEU TYR PHE TYR GLN GLN LEU ARG ASN
SEQRES 12 A 392 ASP TYR MET GLN ARG TYR ALA SER LYS VAL SER GLU GLY
SEQRES 13 A 392 MET ALA LEU GLN LEU GLY CYS LEU GLU LEU ARG ARG PHE
SEQRES 14 A 392 PHE LYS ASP MET PRO HIS ASN ALA LEU ASP LYS LYS SER
SEQRES 15 A 392 ASN PHE GLU LEU LEU GLU LYS GLU VAL GLY LEU ASP LEU
SEQRES 16 A 392 PHE PHE PRO LYS GLN MET GLN GLU ASN LEU LYS PRO LYS
SEQRES 17 A 392 GLN PHE ARG LYS MET ILE GLN GLN THR PHE GLN GLN TYR
SEQRES 18 A 392 ALA SER LEU ARG GLU GLU GLU CYS VAL MET LYS PHE PHE
SEQRES 19 A 392 ASN THR LEU ALA GLY PHE ALA ASN ILE ASP GLN GLU THR
SEQRES 20 A 392 TYR ARG CYS GLU LEU ILE GLN GLY TRP ASN ILE THR VAL
SEQRES 21 A 392 ASP LEU VAL ILE GLY PRO LYS GLY ILE ARG GLN LEU THR
SEQRES 22 A 392 SER GLN ASP ALA LYS PRO THR CYS LEU ALA GLU PHE LYS
SEQRES 23 A 392 GLN ILE ARG SER ILE ARG CYS LEU PRO LEU GLU GLU GLY
SEQRES 24 A 392 GLN ALA VAL LEU GLN LEU GLY ILE GLU GLY ALA PRO GLN
SEQRES 25 A 392 ALA LEU SER ILE LYS THR SER SER LEU ALA GLU ALA GLU
SEQRES 26 A 392 ASN MET ALA ASP LEU ILE ASP GLY TYR CYS ARG LEU GLN
SEQRES 27 A 392 GLY GLU HIS GLN GLY SER LEU ILE ILE HIS PRO ARG LYS
SEQRES 28 A 392 ASP GLY GLU LYS ARG ASN SER LEU PRO GLN ILE PRO MET
SEQRES 29 A 392 LEU ASN LEU GLU ALA ARG ARG SER HIS LEU SER GLU SER
SEQRES 30 A 392 CYS SER ILE GLU SER ASP ILE TYR ALA GLU ILE PRO ASP
SEQRES 31 A 392 GLU THR
HELIX 1 1 GLU A 34 GLU A 36 5 3
HELIX 2 2 ASN A 51 LYS A 54 5 4
HELIX 3 3 GLU A 66 SER A 77 1 12
HELIX 4 4 LEU A 86 GLU A 88 5 3
HELIX 5 5 THR A 110 TYR A 118 1 9
HELIX 6 6 VAL A 123 ALA A 125 5 3
HELIX 7 7 PHE A 140 LYS A 145 1 6
HELIX 8 8 ASP A 147 TYR A 166 1 20
HELIX 9 9 SER A 171 PHE A 187 1 17
HELIX 10 10 ASN A 193 ASP A 196 5 4
HELIX 11 11 LYS A 197 VAL A 208 1 12
HELIX 12 12 GLY A 209 PHE A 213 5 5
HELIX 13 13 PRO A 215 LEU A 222 1 8
HELIX 14 14 LYS A 223 ALA A 239 1 17
HELIX 15 15 ARG A 242 ALA A 255 1 14
HELIX 16 16 GLU A 301 ILE A 305 5 5
HELIX 17 17 SER A 337 GLY A 356 1 20
SHEET 1 A 5 ASN A 55 THR A 62 0
SHEET 2 A 5 VAL A 38 PHE A 45 -1 N ARG A 39 O CYS A 61
SHEET 3 A 5 TRP A 127 ILE A 133 1 O LEU A 131 N CYS A 44
SHEET 4 A 5 TYR A 90 HIS A 96 -1 N GLY A 91 O GLN A 132
SHEET 5 A 5 ILE A 102 LEU A 105 -1 O HIS A 103 N LEU A 94
SHEET 1 B 7 THR A 297 ALA A 300 0
SHEET 2 B 7 GLY A 285 LEU A 289 -1 N ILE A 286 O ALA A 300
SHEET 3 B 7 VAL A 277 GLY A 282 -1 N VAL A 280 O ARG A 287
SHEET 4 B 7 GLU A 263 ILE A 270 -1 N TYR A 265 O LEU A 279
SHEET 5 B 7 LEU A 331 THR A 335 -1 O SER A 332 N ILE A 270
SHEET 6 B 7 GLN A 317 LEU A 322 -1 N ALA A 318 O THR A 335
SHEET 7 B 7 CYS A 310 LEU A 313 -1 N LEU A 311 O VAL A 319
CRYST1 112.971 112.971 103.335 90.00 90.00 120.00 P 32 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 0.008852 0.005111 0.000000 0.00000
SCALE2 0.000000 0.010221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009677 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
