HEADER TRANSFERASE 12-APR-10 3MIY
TITLE X-RAY CRYSTAL STRUCTURE OF ITK COMPLEXED WITH SUNITINIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE ITK/TSK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 357-620;
COMPND 5 SYNONYM: T-CELL-SPECIFIC KINASE, TYROSINE-PROTEIN KINASE LYK, KINASE
COMPND 6 EMT;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITK, EMT, LYK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9 II SFM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL
KEYWDS HELIX C-IN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUGLSTATTER,A.G.VILLASENOR
REVDAT 5 06-SEP-23 3MIY 1 REMARK
REVDAT 4 06-OCT-21 3MIY 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 05-OCT-11 3MIY 1 HETATM VERSN
REVDAT 2 18-AUG-10 3MIY 1 JRNL
REVDAT 1 30-JUN-10 3MIY 0
JRNL AUTH A.K.KUTACH,A.G.VILLASENOR,D.LAM,C.BELUNIS,C.JANSON,S.LOK,
JRNL AUTH 2 L.N.HONG,C.M.LIU,J.DEVAL,T.J.NOVAK,J.W.BARNETT,W.CHU,D.SHAW,
JRNL AUTH 3 A.KUGLSTATTER
JRNL TITL CRYSTAL STRUCTURES OF IL-2-INDUCIBLE T CELL KINASE COMPLEXED
JRNL TITL 2 WITH INHIBITORS: INSIGHTS INTO RATIONAL DRUG DESIGN AND
JRNL TITL 3 ACTIVITY REGULATION.
JRNL REF CHEM.BIOL.DRUG DES. V. 76 154 2010
JRNL REFN ISSN 1747-0277
JRNL PMID 20545945
JRNL DOI 10.1111/J.1747-0285.2010.00993.X
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.1
REMARK 3 NUMBER OF REFLECTIONS : 49551
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2680
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1433
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 33.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 82
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3798
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 307
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.51000
REMARK 3 B22 (A**2) : -0.77000
REMARK 3 B33 (A**2) : 0.81000
REMARK 3 B12 (A**2) : -0.04000
REMARK 3 B13 (A**2) : -0.33000
REMARK 3 B23 (A**2) : -1.05000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.172
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3942 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5325 ; 0.913 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 471 ; 4.507 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;35.087 ;23.820
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 672 ;12.987 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.908 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 574 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2980 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1969 ; 0.174 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2705 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 282 ; 0.091 ; 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): 78 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.096 ; 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): 2444 ; 0.446 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3813 ; 0.774 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1730 ; 0.945 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1512 ; 1.543 ; 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 : 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 3MIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058602.
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 : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1SM2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M BIS-TRIS, PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 283K
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 GLN A 373
REMARK 465 PHE A 374
REMARK 465 ARG A 394
REMARK 465 GLU A 395
REMARK 465 GLY A 396
REMARK 465 ALA A 397
REMARK 465 MET A 398
REMARK 465 GLY A 502
REMARK 465 MET A 503
REMARK 465 THR A 504
REMARK 465 ARG A 505
REMARK 465 PHE A 506
REMARK 465 VAL A 507
REMARK 465 LEU A 508
REMARK 465 ASP A 509
REMARK 465 ASP A 510
REMARK 465 GLN A 511
REMARK 465 TYR A 512
REMARK 465 THR A 513
REMARK 465 SER A 514
REMARK 465 SER A 515
REMARK 465 THR A 516
REMARK 465 GLY A 517
REMARK 465 THR A 518
REMARK 465 LYS A 519
REMARK 465 PHE A 520
REMARK 465 LEU A 620
REMARK 465 GLN B 373
REMARK 465 PHE B 374
REMARK 465 ARG B 394
REMARK 465 GLU B 395
REMARK 465 GLY B 396
REMARK 465 ALA B 397
REMARK 465 MET B 398
REMARK 465 MET B 503
REMARK 465 THR B 504
REMARK 465 ARG B 505
REMARK 465 PHE B 506
REMARK 465 VAL B 507
REMARK 465 LEU B 508
REMARK 465 ASP B 509
REMARK 465 ASP B 510
REMARK 465 GLN B 511
REMARK 465 TYR B 512
REMARK 465 THR B 513
REMARK 465 SER B 514
REMARK 465 SER B 515
REMARK 465 THR B 516
REMARK 465 GLY B 517
REMARK 465 THR B 518
REMARK 465 LYS B 519
REMARK 465 PHE B 520
REMARK 465 LEU B 620
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 385 -70.70 -128.42
REMARK 500 ARG A 481 -14.93 80.88
REMARK 500 ASP A 482 42.69 -143.31
REMARK 500 ASN A 561 -3.88 60.96
REMARK 500 VAL B 366 -62.02 -95.01
REMARK 500 LYS B 385 -70.03 -135.07
REMARK 500 ARG B 481 -14.33 80.11
REMARK 500 ASP B 482 45.17 -145.37
REMARK 500 ASN B 561 38.92 -99.27
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 B49 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B49 B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MJ2 RELATED DB: PDB
REMARK 900 RELATED ID: 3MJ1 RELATED DB: PDB
DBREF 3MIY A 357 620 UNP Q08881 ITK_HUMAN 357 620
DBREF 3MIY B 357 620 UNP Q08881 ITK_HUMAN 357 620
SEQADV 3MIY GLY A 355 UNP Q08881 EXPRESSION TAG
SEQADV 3MIY SER A 356 UNP Q08881 EXPRESSION TAG
SEQADV 3MIY SER A 477 UNP Q08881 CYS 477 ENGINEERED MUTATION
SEQADV 3MIY ALA A 614 UNP Q08881 GLU 614 ENGINEERED MUTATION
SEQADV 3MIY ALA A 617 UNP Q08881 GLU 617 ENGINEERED MUTATION
SEQADV 3MIY GLY B 355 UNP Q08881 EXPRESSION TAG
SEQADV 3MIY SER B 356 UNP Q08881 EXPRESSION TAG
SEQADV 3MIY SER B 477 UNP Q08881 CYS 477 ENGINEERED MUTATION
SEQADV 3MIY ALA B 614 UNP Q08881 GLU 614 ENGINEERED MUTATION
SEQADV 3MIY ALA B 617 UNP Q08881 GLU 617 ENGINEERED MUTATION
SEQRES 1 A 266 GLY SER VAL ILE ASP PRO SER GLU LEU THR PHE VAL GLN
SEQRES 2 A 266 GLU ILE GLY SER GLY GLN PHE GLY LEU VAL HIS LEU GLY
SEQRES 3 A 266 TYR TRP LEU ASN LYS ASP LYS VAL ALA ILE LYS THR ILE
SEQRES 4 A 266 ARG GLU GLY ALA MET SER GLU GLU ASP PHE ILE GLU GLU
SEQRES 5 A 266 ALA GLU VAL MET MET LYS LEU SER HIS PRO LYS LEU VAL
SEQRES 6 A 266 GLN LEU TYR GLY VAL CYS LEU GLU GLN ALA PRO ILE CYS
SEQRES 7 A 266 LEU VAL PHE GLU PHE MET GLU HIS GLY CYS LEU SER ASP
SEQRES 8 A 266 TYR LEU ARG THR GLN ARG GLY LEU PHE ALA ALA GLU THR
SEQRES 9 A 266 LEU LEU GLY MET CYS LEU ASP VAL CYS GLU GLY MET ALA
SEQRES 10 A 266 TYR LEU GLU GLU ALA SER VAL ILE HIS ARG ASP LEU ALA
SEQRES 11 A 266 ALA ARG ASN CYS LEU VAL GLY GLU ASN GLN VAL ILE LYS
SEQRES 12 A 266 VAL SER ASP PHE GLY MET THR ARG PHE VAL LEU ASP ASP
SEQRES 13 A 266 GLN TYR THR SER SER THR GLY THR LYS PHE PRO VAL LYS
SEQRES 14 A 266 TRP ALA SER PRO GLU VAL PHE SER PHE SER ARG TYR SER
SEQRES 15 A 266 SER LYS SER ASP VAL TRP SER PHE GLY VAL LEU MET TRP
SEQRES 16 A 266 GLU VAL PHE SER GLU GLY LYS ILE PRO TYR GLU ASN ARG
SEQRES 17 A 266 SER ASN SER GLU VAL VAL GLU ASP ILE SER THR GLY PHE
SEQRES 18 A 266 ARG LEU TYR LYS PRO ARG LEU ALA SER THR HIS VAL TYR
SEQRES 19 A 266 GLN ILE MET ASN HIS CYS TRP LYS GLU ARG PRO GLU ASP
SEQRES 20 A 266 ARG PRO ALA PHE SER ARG LEU LEU ARG GLN LEU ALA ALA
SEQRES 21 A 266 ILE ALA ALA SER GLY LEU
SEQRES 1 B 266 GLY SER VAL ILE ASP PRO SER GLU LEU THR PHE VAL GLN
SEQRES 2 B 266 GLU ILE GLY SER GLY GLN PHE GLY LEU VAL HIS LEU GLY
SEQRES 3 B 266 TYR TRP LEU ASN LYS ASP LYS VAL ALA ILE LYS THR ILE
SEQRES 4 B 266 ARG GLU GLY ALA MET SER GLU GLU ASP PHE ILE GLU GLU
SEQRES 5 B 266 ALA GLU VAL MET MET LYS LEU SER HIS PRO LYS LEU VAL
SEQRES 6 B 266 GLN LEU TYR GLY VAL CYS LEU GLU GLN ALA PRO ILE CYS
SEQRES 7 B 266 LEU VAL PHE GLU PHE MET GLU HIS GLY CYS LEU SER ASP
SEQRES 8 B 266 TYR LEU ARG THR GLN ARG GLY LEU PHE ALA ALA GLU THR
SEQRES 9 B 266 LEU LEU GLY MET CYS LEU ASP VAL CYS GLU GLY MET ALA
SEQRES 10 B 266 TYR LEU GLU GLU ALA SER VAL ILE HIS ARG ASP LEU ALA
SEQRES 11 B 266 ALA ARG ASN CYS LEU VAL GLY GLU ASN GLN VAL ILE LYS
SEQRES 12 B 266 VAL SER ASP PHE GLY MET THR ARG PHE VAL LEU ASP ASP
SEQRES 13 B 266 GLN TYR THR SER SER THR GLY THR LYS PHE PRO VAL LYS
SEQRES 14 B 266 TRP ALA SER PRO GLU VAL PHE SER PHE SER ARG TYR SER
SEQRES 15 B 266 SER LYS SER ASP VAL TRP SER PHE GLY VAL LEU MET TRP
SEQRES 16 B 266 GLU VAL PHE SER GLU GLY LYS ILE PRO TYR GLU ASN ARG
SEQRES 17 B 266 SER ASN SER GLU VAL VAL GLU ASP ILE SER THR GLY PHE
SEQRES 18 B 266 ARG LEU TYR LYS PRO ARG LEU ALA SER THR HIS VAL TYR
SEQRES 19 B 266 GLN ILE MET ASN HIS CYS TRP LYS GLU ARG PRO GLU ASP
SEQRES 20 B 266 ARG PRO ALA PHE SER ARG LEU LEU ARG GLN LEU ALA ALA
SEQRES 21 B 266 ILE ALA ALA SER GLY LEU
HET B49 A 1 29
HET B49 B 2 29
HETNAM B49 N-[2-(DIETHYLAMINO)ETHYL]-5-[(Z)-(5-FLUORO-2-OXO-1,2-
HETNAM 2 B49 DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-2,4-DIMETHYL-1H-
HETNAM 3 B49 PYRROLE-3-CARBO XAMIDE
HETSYN B49 SUNITINIB
FORMUL 3 B49 2(C22 H27 F N4 O2)
FORMUL 5 HOH *307(H2 O)
HELIX 1 1 ASP A 359 SER A 361 5 3
HELIX 2 2 SER A 399 MET A 411 1 13
HELIX 3 3 CYS A 442 GLN A 450 1 9
HELIX 4 4 ALA A 455 ALA A 476 1 22
HELIX 5 5 ALA A 484 ARG A 486 5 3
HELIX 6 6 GLU A 492 GLN A 494 5 3
HELIX 7 7 PRO A 521 ALA A 525 5 5
HELIX 8 8 SER A 526 SER A 533 1 8
HELIX 9 9 SER A 536 SER A 553 1 18
HELIX 10 10 SER A 563 GLY A 574 1 12
HELIX 11 11 SER A 584 TRP A 595 1 12
HELIX 12 12 ARG A 598 ARG A 602 5 5
HELIX 13 13 ALA A 604 GLY A 619 1 16
HELIX 14 14 ASP B 359 SER B 361 5 3
HELIX 15 15 SER B 399 MET B 411 1 13
HELIX 16 16 CYS B 442 GLN B 450 1 9
HELIX 17 17 ALA B 455 ALA B 476 1 22
HELIX 18 18 ALA B 484 ARG B 486 5 3
HELIX 19 19 GLU B 492 GLN B 494 5 3
HELIX 20 20 PRO B 521 ALA B 525 5 5
HELIX 21 21 SER B 526 SER B 533 1 8
HELIX 22 22 SER B 536 SER B 553 1 18
HELIX 23 23 SER B 563 THR B 573 1 11
HELIX 24 24 SER B 584 TRP B 595 1 12
HELIX 25 25 ARG B 598 ARG B 602 5 5
HELIX 26 26 ALA B 604 GLY B 619 1 16
SHEET 1 A 5 LEU A 363 GLY A 370 0
SHEET 2 A 5 LEU A 376 TRP A 382 -1 O LEU A 379 N GLN A 367
SHEET 3 A 5 ASP A 386 THR A 392 -1 O ILE A 390 N HIS A 378
SHEET 4 A 5 CYS A 432 GLU A 436 -1 O LEU A 433 N LYS A 391
SHEET 5 A 5 LEU A 421 CYS A 425 -1 N TYR A 422 O VAL A 434
SHEET 1 B 2 CYS A 488 VAL A 490 0
SHEET 2 B 2 ILE A 496 VAL A 498 -1 O LYS A 497 N LEU A 489
SHEET 1 C 5 LEU B 363 GLY B 370 0
SHEET 2 C 5 LEU B 376 TRP B 382 -1 O LEU B 379 N GLN B 367
SHEET 3 C 5 ASP B 386 THR B 392 -1 O ILE B 390 N HIS B 378
SHEET 4 C 5 CYS B 432 GLU B 436 -1 O PHE B 435 N ALA B 389
SHEET 5 C 5 LEU B 421 CYS B 425 -1 N TYR B 422 O VAL B 434
SHEET 1 D 2 CYS B 488 VAL B 490 0
SHEET 2 D 2 ILE B 496 VAL B 498 -1 O LYS B 497 N LEU B 489
CISPEP 1 ALA A 429 PRO A 430 0 -1.82
CISPEP 2 ALA B 429 PRO B 430 0 -1.38
SITE 1 AC1 14 HOH A 130 ILE A 369 ALA A 389 LYS A 391
SITE 2 AC1 14 PHE A 435 GLU A 436 PHE A 437 MET A 438
SITE 3 AC1 14 GLU A 439 HIS A 440 GLY A 441 LEU A 489
SITE 4 AC1 14 SER A 499 HOH A1092
SITE 1 AC2 12 HOH B 82 ILE B 369 ALA B 389 LYS B 391
SITE 2 AC2 12 PHE B 435 GLU B 436 PHE B 437 MET B 438
SITE 3 AC2 12 GLU B 439 GLY B 441 LEU B 489 HOH B1001
CRYST1 39.479 52.053 66.106 98.49 103.65 92.84 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 0.025330 0.001257 0.006444 0.00000
SCALE2 0.000000 0.019235 0.003201 0.00000
SCALE3 0.000000 0.000000 0.015781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END