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Database: PDB
Entry: 3U6J
LinkDB: 3U6J
Original site: 3U6J 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-OCT-11   3U6J              
TITLE     CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH A       
TITLE    2 PYRAZOLONE INHIBITOR                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 815-1171;                                     
COMPND   5 SYNONYM: VEGFR-2, FETAL LIVER KINASE 1, FLK-1, KINASE INSERT DOMAIN  
COMPND   6 RECEPTOR, PROTEIN-TYROSINE KINASE RECEPTOR FLK-1;                    
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: FLK1, KDR;                                                     
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KDR, FLK-1, ANGIOGENESIS, PHOSPHOTRANSFERASE, CANCER, VASCULAR        
KEYWDS   2 ENDOTHELIAL GROWTH FACTOR, TRANSFERASE/TRANSFERASE INHIBITOR,        
KEYWDS   3 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.WHITTINGTON,A.LONG,P.ROSE,Y.GU,H.ZHAO                             
REVDAT   2   23-MAY-12 3U6J    1       JRNL                                     
REVDAT   1   22-FEB-12 3U6J    0                                                
JRNL        AUTH   M.H.NORMAN,L.LIU,M.LEE,N.XI,I.FELLOWS,N.D.D'ANGELO,          
JRNL        AUTH 2 C.DOMINGUEZ,K.REX,S.F.BELLON,T.S.KIM,I.DUSSAULT              
JRNL        TITL   STRUCTURE-BASED DESIGN OF NOVEL CLASS II C-MET INHIBITORS:   
JRNL        TITL 2 1. IDENTIFICATION OF PYRAZOLONE-BASED DERIVATIVES.           
JRNL        REF    J.MED.CHEM.                   V.  55  1858 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22320343                                                     
JRNL        DOI    10.1021/JM201330U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19863                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1449                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1332                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2484                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 260                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.51000                                              
REMARK   3    B22 (A**2) : -0.71000                                             
REMARK   3    B33 (A**2) : 0.15000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.264         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.638         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2589 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3501 ; 1.074 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   306 ; 5.204 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;32.707 ;22.917       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   448 ;12.512 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;16.038 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   368 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1976 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1182 ; 0.164 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1737 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   232 ; 0.108 ; 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):    59 ; 0.179 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.118 ; 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):  1594 ; 0.603 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2471 ; 1.023 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1174 ; 0.981 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1030 ; 1.614 ; 6.000       
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   815        A   919                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6584  -1.6548  11.8999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0705 T22:   0.0160                                     
REMARK   3      T33:  -0.0565 T12:   0.0112                                     
REMARK   3      T13:  -0.0039 T23:  -0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6938 L22:   1.0599                                     
REMARK   3      L33:   1.8262 L12:  -0.3785                                     
REMARK   3      L13:  -1.3356 L23:  -0.3131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0753 S12:  -0.1420 S13:   0.1030                       
REMARK   3      S21:  -0.0373 S22:   0.0816 S23:  -0.0327                       
REMARK   3      S31:  -0.0015 S32:   0.1936 S33:  -0.1569                       
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   920        A  1174                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1980  -3.4147  21.4783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0002 T22:  -0.0667                                     
REMARK   3      T33:  -0.0218 T12:   0.0185                                     
REMARK   3      T13:   0.0163 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7088 L22:   0.1553                                     
REMARK   3      L33:   1.3107 L12:  -0.0478                                     
REMARK   3      L13:  -0.1691 L23:   0.0449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0407 S12:   0.0395 S13:   0.0531                       
REMARK   3      S21:   0.0074 S22:   0.0138 S23:   0.0312                       
REMARK   3      S31:   0.0335 S32:   0.0013 S33:  -0.0545                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3U6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068368.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19876                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 5000 MONOMETHYL ETHER, 75 MM     
REMARK 280  AMMONIUM SULFATE, 25 MM SODIUM CHLORIDE, 100 MM HEPES, 8%           
REMARK 280  ISOPROPANOL, 40 MM BETA-MERCAPTOETHANOL, PH 8.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, 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       32.63400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   858                                                      
REMARK 465     THR A   859                                                      
REMARK 465     HIS A  1175                                                      
REMARK 465     HIS A  1176                                                      
REMARK 465     HIS A  1177                                                      
REMARK 465     HIS A  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    HIS A 816     -111.41   -136.86                                   
REMARK 500    ARG A1027      -14.69     80.88                                   
REMARK 500    ASP A1028       41.57   -142.65                                   
REMARK 500    SER A1037     -162.60   -103.84                                   
REMARK 500    ASP A1112     -158.43   -125.31                                   
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 03X A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3U6I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3U6H   RELATED DB: PDB                                   
DBREF  3U6J A  815  1171  UNP    P35968   VGFR2_HUMAN    815   1171             
SEQADV 3U6J THR A  916  UNP  P35968    VAL   916 ENGINEERED MUTATION            
SEQADV 3U6J     A       UNP  P35968    THR   940 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LYS   941 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLY   942 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ALA   943 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ARG   944 DELETION                       
SEQADV 3U6J     A       UNP  P35968    PHE   945 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ARG   946 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLN   947 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLY   948 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LYS   949 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ASP   950 DELETION                       
SEQADV 3U6J     A       UNP  P35968    TYR   951 DELETION                       
SEQADV 3U6J     A       UNP  P35968    VAL   952 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLY   953 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ALA   954 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ILE   955 DELETION                       
SEQADV 3U6J     A       UNP  P35968    PRO   956 DELETION                       
SEQADV 3U6J     A       UNP  P35968    VAL   957 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ASP   958 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LEU   959 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LYS   960 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ARG   961 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ARG   962 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LEU   963 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ASP   964 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   965 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ILE   966 DELETION                       
SEQADV 3U6J     A       UNP  P35968    THR   967 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   968 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   969 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLN   970 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   971 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   972 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ALA   973 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   974 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   975 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLY   976 DELETION                       
SEQADV 3U6J     A       UNP  P35968    PHE   977 DELETION                       
SEQADV 3U6J     A       UNP  P35968    VAL   978 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLU   979 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLU   980 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LYS   981 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   982 DELETION                       
SEQADV 3U6J     A       UNP  P35968    LEU   983 DELETION                       
SEQADV 3U6J     A       UNP  P35968    SER   984 DELETION                       
SEQADV 3U6J     A       UNP  P35968    ASP   985 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLU   987 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLU   988 DELETION                       
SEQADV 3U6J     A       UNP  P35968    GLU   989 DELETION                       
SEQADV 3U6J VAL A  990  UNP  P35968    GLU   990 ENGINEERED MUTATION            
SEQADV 3U6J ARG A 1172  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1173  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1174  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1175  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1176  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1177  UNP  P35968              EXPRESSION TAG                 
SEQADV 3U6J HIS A 1178  UNP  P35968              EXPRESSION TAG                 
SEQRES   1 A  314  GLU HIS CYS 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 TYR LYS ASP PRO ASP TYR          
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                                                      
HET    03X  A   1      39                                                       
HETNAM     03X N-{4-[(6,7-DIMETHOXYQUINOLIN-4-YL)OXY]-3-FLUOROPHENYL}-          
HETNAM   2 03X  1,5-DIMETHYL-3-OXO-2-PHENYL-2,3-DIHYDRO-1H-PYRAZOLE-4-          
HETNAM   3 03X  CARBOXAMIDE                                                     
FORMUL   2  03X    C29 H25 F N4 O5                                              
FORMUL   3  HOH   *260(H2 O)                                                    
HELIX    1   1 HIS A  816  LEU A  820  5                                   5    
HELIX    2   2 ASP A  823  GLU A  828  1                                   6    
HELIX    3   3 PRO A  830  ASP A  832  5                                   3    
HELIX    4   4 THR A  875  GLY A  893  1                                  19    
HELIX    5   5 ASN A  923  SER A  930  1                                   8    
HELIX    6   6 PRO A  992  LYS A  997  5                                   6    
HELIX    7   7 THR A 1001  ARG A 1022  1                                  22    
HELIX    8   8 ALA A 1030  ARG A 1032  5                                   3    
HELIX    9   9 GLU A 1038  ASN A 1040  5                                   3    
HELIX   10  10 PHE A 1047  ARG A 1051  5                                   5    
HELIX   11  11 PRO A 1068  MET A 1072  5                                   5    
HELIX   12  12 ALA A 1073  ARG A 1080  1                                   8    
HELIX   13  13 THR A 1083  PHE A 1099  1                                  17    
HELIX   14  14 ASP A 1112  GLU A 1121  1                                  10    
HELIX   15  15 THR A 1132  TRP A 1143  1                                  12    
HELIX   16  16 GLU A 1146  ARG A 1150  5                                   5    
HELIX   17  17 THR A 1152  GLN A 1170  1                                  19    
SHEET    1   A 5 LEU A 834  ARG A 842  0                                        
SHEET    2   A 5 GLY A 846  PHE A 854 -1  O  GLU A 850   N  GLY A 837           
SHEET    3   A 5 CYS A 862  LEU A 870 -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 2 VAL A1060  LYS A1062  0                                        
SHEET    2   C 2 ALA A1065  LEU A1067 -1  O  LEU A1067   N  VAL A1060           
CISPEP   1 ALA A  991    PRO A  992          0        -0.30                     
SITE     1 AC1 16 LEU A 840  VAL A 848  ALA A 866  LYS A 868                    
SITE     2 AC1 16 GLU A 885  ILE A 888  LEU A 889  THR A 916                    
SITE     3 AC1 16 GLU A 917  CYS A 919  LYS A 920  HIS A1026                    
SITE     4 AC1 16 LEU A1035  CYS A1045  ASP A1046  PHE A1047                    
CRYST1   56.194   65.268   57.323  90.00 117.94  90.00 P 1 21 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      0.017795  0.000000  0.009438        0.00000                         
SCALE2      0.000000  0.015321  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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