GenomeNet

Database: PDB
Entry: 3CPC
LinkDB: 3CPC
Original site: 3CPC 
HEADER    TRANSFERASE                             31-MAR-08   3CPC              
TITLE     CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH A       
TITLE    2 PYRIDONE INHIBITOR                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN, RESIDUES 940-989 DELETED;           
COMPND   5 SYNONYM: VEGFR-2, KINASE INSERT DOMAIN RECEPTOR, PROTEIN-TYROSINE    
COMPND   6 KINASE RECEPTOR FLK-1, CD309 ANTIGEN;                                
COMPND   7 EC: 2.7.10.1;                                                        
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: KDR, FLK1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    RECEPTOR TYROSINE KINASE, ANGIOGENESIS, ATP-BINDING, DEVELOPMENTAL    
KEYWDS   2 PROTEIN, DIFFERENTIATION, GLYCOPROTEIN, HOST-VIRUS INTERACTION,      
KEYWDS   3 IMMUNOGLOBULIN DOMAIN, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, 
KEYWDS   4 TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.WHITTINGTON,A.M.LONG,P.ROSE,Y.GU,H.ZHAO                           
REVDAT   5   13-JUN-18 3CPC    1       DBREF  SEQADV                            
REVDAT   4   26-JUL-17 3CPC    1       SOURCE REMARK                            
REVDAT   3   13-JUL-11 3CPC    1       VERSN                                    
REVDAT   2   24-FEB-09 3CPC    1       VERSN                                    
REVDAT   1   17-JUN-08 3CPC    0                                                
JRNL        AUTH   E.HU,A.TASKER,R.D.WHITE,R.K.KUNZ,J.HUMAN,N.CHEN,R.BURLI,     
JRNL        AUTH 2 R.HUNGATE,P.NOVAK,A.ITANO,X.ZHANG,V.YU,Y.NGUYEN,Y.TUDOR,     
JRNL        AUTH 3 M.PLANT,S.FLYNN,Y.XU,K.L.MEAGHER,D.A.WHITTINGTON,G.Y.NG      
JRNL        TITL   DISCOVERY OF ARYL AMINOQUINAZOLINE PYRIDONES AS POTENT,      
JRNL        TITL 2 SELECTIVE, AND ORALLY EFFICACIOUS INHIBITORS OF RECEPTOR     
JRNL        TITL 3 TYROSINE KINASE C-KIT.                                       
JRNL        REF    J.MED.CHEM.                   V.  51  3065 2008              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   18447379                                                     
JRNL        DOI    10.1021/JM800188G                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22627                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1422                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1631                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4409                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 113                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.24000                                             
REMARK   3    B22 (A**2) : -0.89000                                             
REMARK   3    B33 (A**2) : 2.17000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.33000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.307         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.089        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4584 ; 0.007 ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6204 ; 0.933 ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   538 ; 4.985 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   203 ;32.395 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   800 ;12.869 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;14.484 ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   671 ; 0.061 ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3439 ; 0.002 ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1992 ; 0.162 ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3092 ; 0.295 ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   184 ; 0.112 ;  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):    46 ; 0.133 ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.166 ;  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):  2827 ; 0.574 ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4398 ; 1.000 ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2071 ; 0.677 ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1806 ; 1.077 ;  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  : 2                                          
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   820        A  1178                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7018  36.3372  32.7060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0277 T22:  -0.0257                                     
REMARK   3      T33:  -0.0163 T12:   0.0010                                     
REMARK   3      T13:  -0.0147 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2190 L22:   0.1251                                     
REMARK   3      L33:   0.0065 L12:   0.0185                                     
REMARK   3      L13:   0.0655 L23:  -0.0031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0249 S12:  -0.0570 S13:  -0.0345                       
REMARK   3      S21:  -0.0391 S22:   0.0143 S23:  -0.0198                       
REMARK   3      S31:  -0.0029 S32:   0.0073 S33:   0.0106                       
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 :   B   820        B  1165                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2856   2.2431  12.4638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0130 T22:  -0.0932                                     
REMARK   3      T33:  -0.0855 T12:   0.0169                                     
REMARK   3      T13:   0.0538 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0156 L22:   1.2324                                     
REMARK   3      L33:   0.9448 L12:   0.9683                                     
REMARK   3      L13:   0.4120 L23:   0.2609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1334 S12:   0.0944 S13:   0.0928                       
REMARK   3      S21:  -0.1790 S22:   0.0016 S23:  -0.0620                       
REMARK   3      S31:   0.1252 S32:  -0.0148 S33:   0.1319                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3CPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047051.                                   
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                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24082                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
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   (%): 46.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MME, HEPES, AMMONIUM SULFATE,   
REMARK 280  SODIUM CHLORIDE, ISOPROPANOL, BETA-MERCAPTOETHANOL, PH 8.0,         
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 277K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-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       33.43250            
REMARK 290   SMTRY3   2  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     GLU A   815                                                      
REMARK 465     HIS A   816                                                      
REMARK 465     ALA A   817                                                      
REMARK 465     GLU A   818                                                      
REMARK 465     ARG A   819                                                      
REMARK 465     GLY A   841                                                      
REMARK 465     ARG A   842                                                      
REMARK 465     GLY A   843                                                      
REMARK 465     ALA A   844                                                      
REMARK 465     PHE A   845                                                      
REMARK 465     GLY A   846                                                      
REMARK 465     GLY A  1048                                                      
REMARK 465     LEU A  1049                                                      
REMARK 465     ALA A  1050                                                      
REMARK 465     ARG A  1051                                                      
REMARK 465     ASP A  1052                                                      
REMARK 465     ILE A  1053                                                      
REMARK 465     PTR A  1054                                                      
REMARK 465     LYS A  1055                                                      
REMARK 465     ASP A  1056                                                      
REMARK 465     PRO A  1057                                                      
REMARK 465     ASP A  1058                                                      
REMARK 465     PTR A  1059                                                      
REMARK 465     VAL A  1060                                                      
REMARK 465     ARG A  1061                                                      
REMARK 465     LYS A  1062                                                      
REMARK 465     GLY A  1063                                                      
REMARK 465     ASP A  1064                                                      
REMARK 465     ALA A  1065                                                      
REMARK 465     ARG A  1066                                                      
REMARK 465     GLU B   815                                                      
REMARK 465     HIS B   816                                                      
REMARK 465     ALA B   817                                                      
REMARK 465     GLU B   818                                                      
REMARK 465     ARG B   819                                                      
REMARK 465     ARG B   842                                                      
REMARK 465     GLY B   843                                                      
REMARK 465     ALA B   844                                                      
REMARK 465     PHE B   845                                                      
REMARK 465     GLY B   846                                                      
REMARK 465     LYS B   871                                                      
REMARK 465     GLU B   872                                                      
REMARK 465     GLY B   873                                                      
REMARK 465     VAL B   990                                                      
REMARK 465     ALA B   991                                                      
REMARK 465     PRO B   992                                                      
REMARK 465     GLU B   993                                                      
REMARK 465     ASP B   994                                                      
REMARK 465     LEU B   995                                                      
REMARK 465     TYR B   996                                                      
REMARK 465     LYS B   997                                                      
REMARK 465     LEU B  1049                                                      
REMARK 465     ALA B  1050                                                      
REMARK 465     ARG B  1051                                                      
REMARK 465     ASP B  1052                                                      
REMARK 465     ILE B  1053                                                      
REMARK 465     PTR B  1054                                                      
REMARK 465     LYS B  1055                                                      
REMARK 465     ASP B  1056                                                      
REMARK 465     PRO B  1057                                                      
REMARK 465     ASP B  1058                                                      
REMARK 465     PTR B  1059                                                      
REMARK 465     VAL B  1060                                                      
REMARK 465     ARG B  1061                                                      
REMARK 465     LYS B  1062                                                      
REMARK 465     GLY B  1063                                                      
REMARK 465     ASP B  1064                                                      
REMARK 465     ALA B  1065                                                      
REMARK 465     ARG B  1066                                                      
REMARK 465     ALA B  1166                                                      
REMARK 465     ASN B  1167                                                      
REMARK 465     ALA B  1168                                                      
REMARK 465     GLN B  1169                                                      
REMARK 465     GLN B  1170                                                      
REMARK 465     ASP B  1171                                                      
REMARK 465     ARG B  1172                                                      
REMARK 465     HIS B  1173                                                      
REMARK 465     HIS B  1174                                                      
REMARK 465     HIS B  1175                                                      
REMARK 465     HIS B  1176                                                      
REMARK 465     HIS B  1177                                                      
REMARK 465     HIS B  1178                                                      
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    ARG A1027      -21.68     79.03                                   
REMARK 500    ASP A1112     -156.61   -118.69                                   
REMARK 500    ARG B1027      -16.54     80.70                                   
REMARK 500    ASP B1028       51.32   -146.49                                   
REMARK 500    SER B1037     -168.62   -104.47                                   
REMARK 500    TYR B1106       71.39     41.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 TYR1054 AND TYR1059 WERE PHOSPHORYLATED BY AN AUTOPHOSPHORYLATION    
REMARK 600 REACTION RUN ON THE PROTEIN PRIOR TO CRYSTALLIZATION. THE            
REMARK 600 PHOSPHORYLATED TYR IS REPRESENTED BY PTR, PHOSPHONOTYROSINE,         
REMARK 600 PTR1054 AND PTR1059. THESE RESIDUES ARE PART OF THE KINASE           
REMARK 600 ACTIVATION LOOP AND THEY ARE DISORDERED IN THE STRUCTURE AND         
REMARK 600 CONSEQUENTLY NOT SEEN IN THE ELECTRON DENSITY.                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C52 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C52 B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CP9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CPB   RELATED DB: PDB                                   
DBREF  3CPC A  815   939  UNP    P35968   VGFR2_HUMAN    815    939             
DBREF  3CPC A  990  1171  UNP    P35968   VGFR2_HUMAN    990   1171             
DBREF  3CPC B  815   939  UNP    P35968   VGFR2_HUMAN    815    939             
DBREF  3CPC B  990  1171  UNP    P35968   VGFR2_HUMAN    990   1171             
SEQADV 3CPC ALA A  817  UNP  P35968    CYS   817 ENGINEERED                     
SEQADV 3CPC THR A  916  UNP  P35968    VAL   916 ENGINEERED                     
SEQADV 3CPC VAL A  990  UNP  P35968    GLU   990 ENGINEERED                     
SEQADV 3CPC ARG A 1172  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1173  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1174  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1175  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1176  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1177  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS A 1178  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC ALA B  817  UNP  P35968    CYS   817 ENGINEERED                     
SEQADV 3CPC THR B  916  UNP  P35968    VAL   916 ENGINEERED                     
SEQADV 3CPC VAL B  990  UNP  P35968    GLU   990 ENGINEERED                     
SEQADV 3CPC ARG B 1172  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1173  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1174  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1175  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1176  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1177  UNP  P35968              EXPRESSION TAG                 
SEQADV 3CPC HIS B 1178  UNP  P35968              EXPRESSION TAG                 
SEQRES   1 A  314  GLU HIS ALA GLU ARG LEU PRO TYR ASP ALA SER LYS TRP          
SEQRES   2 A  314  GLU PHE PRO ARG ASP ARG LEU LYS LEU GLY LYS PRO LEU          
SEQRES   3 A  314  GLY ARG GLY ALA PHE GLY GLN VAL ILE GLU ALA ASP ALA          
SEQRES   4 A  314  PHE GLY ILE ASP LYS THR ALA THR CYS ARG THR VAL ALA          
SEQRES   5 A  314  VAL LYS MET LEU LYS GLU GLY ALA THR HIS SER GLU HIS          
SEQRES   6 A  314  ARG ALA LEU MET SER GLU LEU LYS ILE LEU ILE HIS ILE          
SEQRES   7 A  314  GLY HIS HIS LEU ASN VAL VAL ASN LEU LEU GLY ALA CYS          
SEQRES   8 A  314  THR LYS PRO GLY GLY PRO LEU MET VAL ILE THR GLU PHE          
SEQRES   9 A  314  CYS LYS PHE GLY ASN LEU SER THR TYR LEU ARG SER LYS          
SEQRES  10 A  314  ARG ASN GLU PHE VAL PRO TYR LYS VAL ALA PRO GLU ASP          
SEQRES  11 A  314  LEU TYR LYS ASP PHE LEU THR LEU GLU HIS LEU ILE CYS          
SEQRES  12 A  314  TYR SER PHE GLN VAL ALA LYS GLY MET GLU PHE LEU ALA          
SEQRES  13 A  314  SER ARG LYS CYS ILE HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  14 A  314  ILE LEU LEU SER GLU LYS ASN VAL VAL LYS ILE CYS ASP          
SEQRES  15 A  314  PHE GLY LEU ALA ARG ASP ILE PTR LYS ASP PRO ASP PTR          
SEQRES  16 A  314  VAL ARG LYS GLY ASP ALA ARG LEU PRO LEU LYS TRP MET          
SEQRES  17 A  314  ALA PRO GLU THR ILE PHE ASP ARG VAL TYR THR ILE GLN          
SEQRES  18 A  314  SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE          
SEQRES  19 A  314  PHE SER LEU GLY ALA SER PRO TYR PRO GLY VAL LYS ILE          
SEQRES  20 A  314  ASP GLU GLU PHE CYS ARG ARG LEU LYS GLU GLY THR ARG          
SEQRES  21 A  314  MET ARG ALA PRO ASP TYR THR THR PRO GLU MET TYR GLN          
SEQRES  22 A  314  THR MET LEU ASP CYS TRP HIS GLY GLU PRO SER GLN ARG          
SEQRES  23 A  314  PRO THR PHE SER GLU LEU VAL GLU HIS LEU GLY ASN LEU          
SEQRES  24 A  314  LEU GLN ALA ASN ALA GLN GLN ASP ARG HIS HIS HIS HIS          
SEQRES  25 A  314  HIS HIS                                                      
SEQRES   1 B  314  GLU HIS ALA GLU ARG LEU PRO TYR ASP ALA SER LYS TRP          
SEQRES   2 B  314  GLU PHE PRO ARG ASP ARG LEU LYS LEU GLY LYS PRO LEU          
SEQRES   3 B  314  GLY ARG GLY ALA PHE GLY GLN VAL ILE GLU ALA ASP ALA          
SEQRES   4 B  314  PHE GLY ILE ASP LYS THR ALA THR CYS ARG THR VAL ALA          
SEQRES   5 B  314  VAL LYS MET LEU LYS GLU GLY ALA THR HIS SER GLU HIS          
SEQRES   6 B  314  ARG ALA LEU MET SER GLU LEU LYS ILE LEU ILE HIS ILE          
SEQRES   7 B  314  GLY HIS HIS LEU ASN VAL VAL ASN LEU LEU GLY ALA CYS          
SEQRES   8 B  314  THR LYS PRO GLY GLY PRO LEU MET VAL ILE THR GLU PHE          
SEQRES   9 B  314  CYS LYS PHE GLY ASN LEU SER THR TYR LEU ARG SER LYS          
SEQRES  10 B  314  ARG ASN GLU PHE VAL PRO TYR LYS VAL ALA PRO GLU ASP          
SEQRES  11 B  314  LEU TYR LYS ASP PHE LEU THR LEU GLU HIS LEU ILE CYS          
SEQRES  12 B  314  TYR SER PHE GLN VAL ALA LYS GLY MET GLU PHE LEU ALA          
SEQRES  13 B  314  SER ARG LYS CYS ILE HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  14 B  314  ILE LEU LEU SER GLU LYS ASN VAL VAL LYS ILE CYS ASP          
SEQRES  15 B  314  PHE GLY LEU ALA ARG ASP ILE PTR LYS ASP PRO ASP PTR          
SEQRES  16 B  314  VAL ARG LYS GLY ASP ALA ARG LEU PRO LEU LYS TRP MET          
SEQRES  17 B  314  ALA PRO GLU THR ILE PHE ASP ARG VAL TYR THR ILE GLN          
SEQRES  18 B  314  SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE          
SEQRES  19 B  314  PHE SER LEU GLY ALA SER PRO TYR PRO GLY VAL LYS ILE          
SEQRES  20 B  314  ASP GLU GLU PHE CYS ARG ARG LEU LYS GLU GLY THR ARG          
SEQRES  21 B  314  MET ARG ALA PRO ASP TYR THR THR PRO GLU MET TYR GLN          
SEQRES  22 B  314  THR MET LEU ASP CYS TRP HIS GLY GLU PRO SER GLN ARG          
SEQRES  23 B  314  PRO THR PHE SER GLU LEU VAL GLU HIS LEU GLY ASN LEU          
SEQRES  24 B  314  LEU GLN ALA ASN ALA GLN GLN ASP ARG HIS HIS HIS HIS          
SEQRES  25 B  314  HIS HIS                                                      
HET    C52  A   1      29                                                       
HET    C52  B   2      29                                                       
HETNAM     C52 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-1-[3-                        
HETNAM   2 C52  (TRIFLUOROMETHYL)PHENYL]PYRIDIN-2(1H)-ONE                       
FORMUL   3  C52    2(C21 H15 F3 N4 O)                                           
FORMUL   5  HOH   *113(H2 O)                                                    
HELIX    1   1 ASP A  823  GLU A  828  1                                   6    
HELIX    2   2 PRO A  830  ASP A  832  5                                   3    
HELIX    3   3 THR A  875  GLY A  893  1                                  19    
HELIX    4   4 ASN A  923  SER A  930  1                                   8    
HELIX    5   5 PRO A  992  LYS A  997  5                                   6    
HELIX    6   6 THR A 1001  ARG A 1022  1                                  22    
HELIX    7   7 ALA A 1030  ARG A 1032  5                                   3    
HELIX    8   8 GLU A 1038  ASN A 1040  5                                   3    
HELIX    9   9 LEU A 1067  MET A 1072  5                                   6    
HELIX   10  10 ALA A 1073  ARG A 1080  1                                   8    
HELIX   11  11 THR A 1083  PHE A 1099  1                                  17    
HELIX   12  12 ASP A 1112  GLU A 1121  1                                  10    
HELIX   13  13 THR A 1132  TRP A 1143  1                                  12    
HELIX   14  14 GLU A 1146  ARG A 1150  5                                   5    
HELIX   15  15 THR A 1152  HIS A 1178  1                                  27    
HELIX   16  16 ASP B  823  GLU B  828  1                                   6    
HELIX   17  17 PRO B  830  ASP B  832  5                                   3    
HELIX   18  18 THR B  875  GLY B  893  1                                  19    
HELIX   19  19 ASN B  923  LYS B  931  1                                   9    
HELIX   20  20 LEU B 1002  ARG B 1022  1                                  21    
HELIX   21  21 ALA B 1030  ARG B 1032  5                                   3    
HELIX   22  22 LEU B 1067  MET B 1072  5                                   6    
HELIX   23  23 ALA B 1073  ARG B 1080  1                                   8    
HELIX   24  24 THR B 1083  PHE B 1099  1                                  17    
HELIX   25  25 ASP B 1112  GLY B 1122  1                                  11    
HELIX   26  26 THR B 1132  TRP B 1143  1                                  12    
HELIX   27  27 GLU B 1146  ARG B 1150  5                                   5    
HELIX   28  28 THR B 1152  LEU B 1164  1                                  13    
SHEET    1   A 5 LEU A 834  PRO A 839  0                                        
SHEET    2   A 5 VAL A 848  PHE A 854 -1  O  GLU A 850   N  GLY A 837           
SHEET    3   A 5 CYS A 862  MET A 869 -1  O  VAL A 865   N  ALA A 851           
SHEET    4   A 5 MET A 913  GLU A 917 -1  O  THR A 916   N  ALA A 866           
SHEET    5   A 5 LEU A 901  CYS A 905 -1  N  LEU A 902   O  ILE A 915           
SHEET    1   B 2 ILE A1034  LEU A1036  0                                        
SHEET    2   B 2 VAL A1042  ILE A1044 -1  O  LYS A1043   N  LEU A1035           
SHEET    1   C 5 LEU B 834  PRO B 839  0                                        
SHEET    2   C 5 VAL B 848  PHE B 854 -1  O  ASP B 852   N  LYS B 835           
SHEET    3   C 5 CYS B 862  MET B 869 -1  O  ARG B 863   N  ALA B 853           
SHEET    4   C 5 MET B 913  GLU B 917 -1  O  THR B 916   N  ALA B 866           
SHEET    5   C 5 LEU B 901  CYS B 905 -1  N  LEU B 902   O  ILE B 915           
SHEET    1   D 2 PHE B 935  VAL B 936  0                                        
SHEET    2   D 2 LEU B1000  THR B1001  1  O  LEU B1000   N  VAL B 936           
SHEET    1   E 2 ILE B1034  LEU B1036  0                                        
SHEET    2   E 2 VAL B1042  ILE B1044 -1  O  LYS B1043   N  LEU B1035           
CISPEP   1 ALA A  991    PRO A  992          0        -1.66                     
SITE     1 AC1 12 ALA A 866  GLU A 885  LEU A 889  THR A 916                    
SITE     2 AC1 12 GLU A 917  CYS A 919  HIS A1026  LEU A1035                    
SITE     3 AC1 12 ILE A1044  CYS A1045  ASP A1046  PHE A1047                    
SITE     1 AC2 12 ALA B 866  LYS B 868  GLU B 885  THR B 916                    
SITE     2 AC2 12 GLU B 917  PHE B 918  CYS B 919  HIS B1026                    
SITE     3 AC2 12 LEU B1035  ILE B1044  CYS B1045  ASP B1046                    
CRYST1   55.361   66.865   89.858  90.00  93.35  90.00 P 1 21 1      4          
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      0.018100  0.000000  0.001100        0.00000                         
SCALE2      0.000000  0.015000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011100        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system