HEADER TRANSFERASE 31-OCT-08 3F3V
TITLE KINASE DOMAIN OF CSRC IN COMPLEX WITH INHIBITOR RL45 (TYPE II)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 251-533;
COMPND 5 SYNONYM: PP60C-SRC, P60-SRC, C-SRC;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSKB3
KEYWDS ALLOSTERIC, TYPE II, DFG-OUT, ATP-BINDING, KINASE, LIPOPROTEIN,
KEYWDS 2 MYRISTATE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTO-ONCOGENE, SH2
KEYWDS 3 DOMAIN, SH3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.GRUTTER,S.KLUTER,M.GETLIK,D.RAUH
REVDAT 5 01-NOV-23 3F3V 1 REMARK
REVDAT 4 10-NOV-21 3F3V 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3F3V 1 VERSN
REVDAT 2 21-JUL-09 3F3V 1 JRNL
REVDAT 1 02-JUN-09 3F3V 0
JRNL AUTH M.GETLIK,C.GRUTTER,J.R.SIMARD,S.KLUTER,M.RABILLER,H.B.RODE,
JRNL AUTH 2 A.ROBUBI,D.RAUH
JRNL TITL HYBRID COMPOUND DESIGN TO OVERCOME THE GATEKEEPER T338M
JRNL TITL 2 MUTATION IN CSRC
JRNL REF J.MED.CHEM. V. 52 3915 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19462975
JRNL DOI 10.1021/JM9002928
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 21983
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 880
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1543
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3720
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4143
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 38.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : -1.09000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : -0.34000
REMARK 3 B13 (A**2) : 0.40000
REMARK 3 B23 (A**2) : 0.19000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.576
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.338
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.867
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.837
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4346 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5907 ; 1.893 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 523 ; 7.443 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;39.203 ;23.495
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 727 ;20.607 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;18.744 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 629 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3323 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2093 ; 0.245 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2950 ; 0.325 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.203 ; 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): 65 ; 0.330 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.160 ; 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): 2686 ; 0.927 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4219 ; 1.573 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1970 ; 2.279 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1686 ; 3.500 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 256 A 533
REMARK 3 RESIDUE RANGE : B 256 B 533
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6210 14.8100 11.9690
REMARK 3 T TENSOR
REMARK 3 T11: -0.0569 T22: 0.0595
REMARK 3 T33: 0.0133 T12: 0.0173
REMARK 3 T13: -0.0064 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.1659 L22: 1.7000
REMARK 3 L33: 0.3064 L12: 0.1363
REMARK 3 L13: -0.0461 L23: -0.3416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0020 S12: 0.0067 S13: -0.0085
REMARK 3 S21: 0.0240 S22: -0.0334 S23: -0.0284
REMARK 3 S31: -0.0297 S32: -0.0809 S33: 0.0354
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 3F3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21983
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OIQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000, 15% GLYCEROL, 85 MM
REMARK 280 MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 248
REMARK 465 HIS A 249
REMARK 465 MET A 250
REMARK 465 GLN A 251
REMARK 465 THR A 252
REMARK 465 GLN A 253
REMARK 465 GLY A 254
REMARK 465 LEU A 255
REMARK 465 ALA A 256
REMARK 465 ALA A 408
REMARK 465 ARG A 409
REMARK 465 LEU A 410
REMARK 465 ILE A 411
REMARK 465 GLU A 412
REMARK 465 ASP A 413
REMARK 465 ASN A 414
REMARK 465 GLU A 415
REMARK 465 TYR A 416
REMARK 465 THR A 417
REMARK 465 ALA A 418
REMARK 465 ARG A 419
REMARK 465 GLN A 420
REMARK 465 GLY A 421
REMARK 465 ALA A 422
REMARK 465 LYS A 423
REMARK 465 GLY B 248
REMARK 465 HIS B 249
REMARK 465 MET B 250
REMARK 465 GLN B 251
REMARK 465 THR B 252
REMARK 465 GLN B 253
REMARK 465 GLY B 254
REMARK 465 LEU B 255
REMARK 465 ALA B 408
REMARK 465 ARG B 409
REMARK 465 LEU B 410
REMARK 465 ILE B 411
REMARK 465 GLU B 412
REMARK 465 ASP B 413
REMARK 465 ASN B 414
REMARK 465 GLU B 415
REMARK 465 TYR B 416
REMARK 465 THR B 417
REMARK 465 ALA B 418
REMARK 465 ARG B 419
REMARK 465 GLN B 420
REMARK 465 GLY B 421
REMARK 465 ALA B 422
REMARK 465 LYS B 423
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 257 CG CD CE NZ
REMARK 470 ARG A 268 CD NE CZ NH1 NH2
REMARK 470 LYS A 298 CD CE NZ
REMARK 470 GLU A 320 CG CD OE1 OE2
REMARK 470 GLU A 353 CG CD OE1 OE2
REMARK 470 LEU A 407 CG CD1 CD2
REMARK 470 PHE A 424 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 472 CG CD1 CD2
REMARK 470 ASP A 473 CG OD1 OD2
REMARK 470 LYS B 257 CG CD CE NZ
REMARK 470 GLU B 265 CG CD OE1 OE2
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 470 GLU B 331 CG CD OE1 OE2
REMARK 470 GLU B 353 CG CD OE1 OE2
REMARK 470 GLU B 489 CD OE1 OE2
REMARK 470 ASP B 493 CG OD1 OD2
REMARK 470 LYS B 501 CD CE NZ
REMARK 470 GLU B 505 CG CD OE1 OE2
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 PRO A 485 O HOH A 57 2.05
REMARK 500 NH2 ARG B 264 O GLU B 331 2.09
REMARK 500 O LYS A 343 O HOH A 40 2.09
REMARK 500 O LYS B 298 OG1 THR B 301 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 483 CB CYS A 483 SG -0.100
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 263 150.36 -49.60
REMARK 500 GLU A 270 -70.21 -103.08
REMARK 500 PRO A 299 131.30 -35.62
REMARK 500 GLU A 305 -29.19 -38.36
REMARK 500 ARG A 385 -23.98 107.53
REMARK 500 ASP A 386 51.74 -142.71
REMARK 500 PRO A 425 47.31 -76.95
REMARK 500 GLU A 486 -1.86 85.34
REMARK 500 GLU A 524 60.85 -113.37
REMARK 500 ALA B 259 1.49 -66.13
REMARK 500 GLU B 270 -79.68 -122.82
REMARK 500 THR B 301 -38.76 -133.55
REMARK 500 PRO B 304 -46.45 -24.99
REMARK 500 HIS B 319 142.87 -176.55
REMARK 500 MET B 380 2.28 -70.00
REMARK 500 ARG B 385 -31.63 88.35
REMARK 500 ASN B 397 36.97 71.79
REMARK 500 LEU B 451 -36.80 -39.80
REMARK 500 GLU B 486 -8.37 78.23
REMARK 500 TRP B 499 34.60 -99.40
REMARK 500 GLU B 524 58.85 -115.06
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 1BU A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1BU B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QLQ RELATED DB: PDB
REMARK 900 RELATED ID: 2QI8 RELATED DB: PDB
REMARK 900 RELATED ID: 2QQ7 RELATED DB: PDB
REMARK 900 RELATED ID: 3F3T RELATED DB: PDB
REMARK 900 RELATED ID: 3F3U RELATED DB: PDB
REMARK 900 RELATED ID: 3F3W RELATED DB: PDB
DBREF 3F3V A 251 533 UNP P00523 SRC_CHICK 251 533
DBREF 3F3V B 251 533 UNP P00523 SRC_CHICK 251 533
SEQADV 3F3V GLY A 248 UNP P00523 EXPRESSION TAG
SEQADV 3F3V HIS A 249 UNP P00523 EXPRESSION TAG
SEQADV 3F3V MET A 250 UNP P00523 EXPRESSION TAG
SEQADV 3F3V CYS A 345 UNP P00523 SER 345 ENGINEERED MUTATION
SEQADV 3F3V GLY B 248 UNP P00523 EXPRESSION TAG
SEQADV 3F3V HIS B 249 UNP P00523 EXPRESSION TAG
SEQADV 3F3V MET B 250 UNP P00523 EXPRESSION TAG
SEQADV 3F3V CYS B 345 UNP P00523 SER 345 ENGINEERED MUTATION
SEQRES 1 A 286 GLY HIS MET GLN THR GLN GLY LEU ALA LYS ASP ALA TRP
SEQRES 2 A 286 GLU ILE PRO ARG GLU SER LEU ARG LEU GLU VAL LYS LEU
SEQRES 3 A 286 GLY GLN GLY CYS PHE GLY GLU VAL TRP MET GLY THR TRP
SEQRES 4 A 286 ASN GLY THR THR ARG VAL ALA ILE LYS THR LEU LYS PRO
SEQRES 5 A 286 GLY THR MET SER PRO GLU ALA PHE LEU GLN GLU ALA GLN
SEQRES 6 A 286 VAL MET LYS LYS LEU ARG HIS GLU LYS LEU VAL GLN LEU
SEQRES 7 A 286 TYR ALA VAL VAL SER GLU GLU PRO ILE TYR ILE VAL THR
SEQRES 8 A 286 GLU TYR MET SER LYS GLY CYS LEU LEU ASP PHE LEU LYS
SEQRES 9 A 286 GLY GLU MET GLY LYS TYR LEU ARG LEU PRO GLN LEU VAL
SEQRES 10 A 286 ASP MET ALA ALA GLN ILE ALA SER GLY MET ALA TYR VAL
SEQRES 11 A 286 GLU ARG MET ASN TYR VAL HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 A 286 ASN ILE LEU VAL GLY GLU ASN LEU VAL CYS LYS VAL ALA
SEQRES 13 A 286 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 A 286 THR ALA ARG GLN GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 A 286 ALA PRO GLU ALA ALA LEU TYR GLY ARG PHE THR ILE LYS
SEQRES 16 A 286 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU LEU
SEQRES 17 A 286 THR THR LYS GLY ARG VAL PRO TYR PRO GLY MET VAL ASN
SEQRES 18 A 286 ARG GLU VAL LEU ASP GLN VAL GLU ARG GLY TYR ARG MET
SEQRES 19 A 286 PRO CYS PRO PRO GLU CYS PRO GLU SER LEU HIS ASP LEU
SEQRES 20 A 286 MET CYS GLN CYS TRP ARG LYS ASP PRO GLU GLU ARG PRO
SEQRES 21 A 286 THR PHE GLU TYR LEU GLN ALA PHE LEU GLU ASP TYR PHE
SEQRES 22 A 286 THR SER THR GLU PRO GLN TYR GLN PRO GLY GLU ASN LEU
SEQRES 1 B 286 GLY HIS MET GLN THR GLN GLY LEU ALA LYS ASP ALA TRP
SEQRES 2 B 286 GLU ILE PRO ARG GLU SER LEU ARG LEU GLU VAL LYS LEU
SEQRES 3 B 286 GLY GLN GLY CYS PHE GLY GLU VAL TRP MET GLY THR TRP
SEQRES 4 B 286 ASN GLY THR THR ARG VAL ALA ILE LYS THR LEU LYS PRO
SEQRES 5 B 286 GLY THR MET SER PRO GLU ALA PHE LEU GLN GLU ALA GLN
SEQRES 6 B 286 VAL MET LYS LYS LEU ARG HIS GLU LYS LEU VAL GLN LEU
SEQRES 7 B 286 TYR ALA VAL VAL SER GLU GLU PRO ILE TYR ILE VAL THR
SEQRES 8 B 286 GLU TYR MET SER LYS GLY CYS LEU LEU ASP PHE LEU LYS
SEQRES 9 B 286 GLY GLU MET GLY LYS TYR LEU ARG LEU PRO GLN LEU VAL
SEQRES 10 B 286 ASP MET ALA ALA GLN ILE ALA SER GLY MET ALA TYR VAL
SEQRES 11 B 286 GLU ARG MET ASN TYR VAL HIS ARG ASP LEU ARG ALA ALA
SEQRES 12 B 286 ASN ILE LEU VAL GLY GLU ASN LEU VAL CYS LYS VAL ALA
SEQRES 13 B 286 ASP PHE GLY LEU ALA ARG LEU ILE GLU ASP ASN GLU TYR
SEQRES 14 B 286 THR ALA ARG GLN GLY ALA LYS PHE PRO ILE LYS TRP THR
SEQRES 15 B 286 ALA PRO GLU ALA ALA LEU TYR GLY ARG PHE THR ILE LYS
SEQRES 16 B 286 SER ASP VAL TRP SER PHE GLY ILE LEU LEU THR GLU LEU
SEQRES 17 B 286 THR THR LYS GLY ARG VAL PRO TYR PRO GLY MET VAL ASN
SEQRES 18 B 286 ARG GLU VAL LEU ASP GLN VAL GLU ARG GLY TYR ARG MET
SEQRES 19 B 286 PRO CYS PRO PRO GLU CYS PRO GLU SER LEU HIS ASP LEU
SEQRES 20 B 286 MET CYS GLN CYS TRP ARG LYS ASP PRO GLU GLU ARG PRO
SEQRES 21 B 286 THR PHE GLU TYR LEU GLN ALA PHE LEU GLU ASP TYR PHE
SEQRES 22 B 286 THR SER THR GLU PRO GLN TYR GLN PRO GLY GLU ASN LEU
HET 1BU A 1 38
HET 1BU B 1 38
HETNAM 1BU 1-{4-[(6-AMINOQUINAZOLIN-4-YL)AMINO]PHENYL}-3-[3-TERT-
HETNAM 2 1BU BUTYL-1-(3-METHYLPHENYL)-1H-PYRAZOL-5-YL]UREA
HETSYN 1BU 1-[4-(6-AMINO-QUINAZOLIN-4-YLAMINO)-PHENYL]-3-(5-TERT-
HETSYN 2 1BU BUTYL-2-M-TOLYL-2H-PYRAZOL-3-YL)-UREA
FORMUL 3 1BU 2(C29 H30 N8 O)
FORMUL 5 HOH *53(H2 O)
HELIX 1 1 SER A 303 LEU A 308 1 6
HELIX 2 2 LEU A 308 LEU A 317 1 10
HELIX 3 3 LEU A 346 GLY A 352 1 7
HELIX 4 4 MET A 354 LEU A 358 5 5
HELIX 5 5 ARG A 359 MET A 380 1 22
HELIX 6 6 ARG A 388 ALA A 390 5 3
HELIX 7 7 GLU A 396 LEU A 398 5 3
HELIX 8 8 PRO A 425 THR A 429 5 5
HELIX 9 9 ALA A 430 GLY A 437 1 8
HELIX 10 10 THR A 440 THR A 457 1 18
HELIX 11 11 VAL A 467 ARG A 477 1 11
HELIX 12 12 PRO A 488 TRP A 499 1 12
HELIX 13 13 ASP A 502 ARG A 506 5 5
HELIX 14 14 THR A 508 ASP A 518 1 11
HELIX 15 15 ASP A 518 THR A 523 1 6
HELIX 16 16 LEU B 308 LEU B 317 1 10
HELIX 17 17 CYS B 345 GLY B 352 1 8
HELIX 18 18 GLU B 353 TYR B 357 5 5
HELIX 19 19 ARG B 359 MET B 380 1 22
HELIX 20 20 ARG B 388 ALA B 390 5 3
HELIX 21 21 PRO B 425 THR B 429 5 5
HELIX 22 22 ALA B 430 GLY B 437 1 8
HELIX 23 23 THR B 440 THR B 457 1 18
HELIX 24 24 VAL B 467 GLU B 476 1 10
HELIX 25 25 PRO B 488 TRP B 499 1 12
HELIX 26 26 ASP B 502 ARG B 506 5 5
HELIX 27 27 THR B 508 ASP B 518 1 11
HELIX 28 28 ASP B 518 THR B 523 1 6
SHEET 1 A 5 LEU A 267 GLN A 275 0
SHEET 2 A 5 GLU A 280 TRP A 286 -1 O THR A 285 N ARG A 268
SHEET 3 A 5 THR A 290 THR A 296 -1 O VAL A 292 N GLY A 284
SHEET 4 A 5 TYR A 335 GLU A 339 -1 O ILE A 336 N LYS A 295
SHEET 5 A 5 LEU A 325 VAL A 329 -1 N TYR A 326 O VAL A 337
SHEET 1 B 3 GLY A 344 CYS A 345 0
SHEET 2 B 3 ILE A 392 VAL A 394 -1 O VAL A 394 N GLY A 344
SHEET 3 B 3 CYS A 400 VAL A 402 -1 O LYS A 401 N LEU A 393
SHEET 1 C 5 LEU B 267 GLN B 275 0
SHEET 2 C 5 GLU B 280 TRP B 286 -1 O VAL B 281 N LEU B 273
SHEET 3 C 5 THR B 290 THR B 296 -1 O THR B 290 N TRP B 286
SHEET 4 C 5 TYR B 335 GLU B 339 -1 O ILE B 336 N LYS B 295
SHEET 5 C 5 LEU B 325 VAL B 329 -1 N TYR B 326 O VAL B 337
SHEET 1 D 2 ILE B 392 VAL B 394 0
SHEET 2 D 2 CYS B 400 VAL B 402 -1 O LYS B 401 N LEU B 393
CISPEP 1 GLU A 332 PRO A 333 0 -21.76
CISPEP 2 GLU B 332 PRO B 333 0 -6.90
SITE 1 AC1 12 LEU A 273 ALA A 293 GLU A 310 MET A 314
SITE 2 AC1 12 LEU A 322 GLU A 339 TYR A 340 MET A 341
SITE 3 AC1 12 LEU A 393 ALA A 403 ASP A 404 GLY A 406
SITE 1 AC2 9 ALA B 293 GLU B 310 MET B 314 GLU B 339
SITE 2 AC2 9 TYR B 340 MET B 341 LEU B 393 ALA B 403
SITE 3 AC2 9 ASP B 404
CRYST1 42.055 63.397 74.955 79.06 87.72 90.08 P 1 2
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 0.023778 0.000031 -0.000972 0.00000
SCALE2 0.000000 0.015774 -0.003053 0.00000
SCALE3 0.000000 0.000000 0.013600 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
