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Database: PDB
Entry: 3EFL
LinkDB: 3EFL
Original site: 3EFL 
HEADER    TRANSFERASE                             09-SEP-08   3EFL              
TITLE     CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH         
TITLE    2 MOTESANIB                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 815-939, 990- 1171;            
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_TAXID: 9606;                                                
SOURCE   4 GENE: KDR, FLK1;                                                     
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    ANGIOGENESIS, MOTESANIB, NICOTINAMIDE, RECEPTOR TYROSINE KINASE,      
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.L.KIM,D.A.WHITTINGTON,A.M.LONG,P.ROSE,Y.GU,H.ZHAO                   
REVDAT   3   23-AUG-17 3EFL    1       SOURCE                                   
REVDAT   2   27-APR-11 3EFL    1       DBREF                                    
REVDAT   1   15-SEP-09 3EFL    0                                                
JRNL        AUTH   A.S.TASKER,V.F.PATEL                                         
JRNL        TITL   DISCOVERY OF MOTESANIB                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29729                          
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 SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1487                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4425                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.44600                                             
REMARK   3    B22 (A**2) : 7.16800                                              
REMARK   3    B33 (A**2) : -18.61400                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.64000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.310                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3EFL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049261.                                   
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               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29729                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
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       33.40500            
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   844                                                      
REMARK 465     PHE A   845                                                      
REMARK 465     LYS A   858                                                      
REMARK 465     THR A   859                                                      
REMARK 465     ALA A   860                                                      
REMARK 465     GLY A   873                                                      
REMARK 465     ALA A   874                                                      
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     LEU A  1067                                                      
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     LEU B   820                                                      
REMARK 465     ALA B   844                                                      
REMARK 465     PHE B   845                                                      
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     ASP B   998                                                      
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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B1068   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A1027      -28.23     89.41                                   
REMARK 500    ASP A1028       52.24   -140.91                                   
REMARK 500    SER A1037     -158.31   -107.04                                   
REMARK 500    GLU A1038      -70.20    -60.46                                   
REMARK 500    LYS A1039       58.97   -100.37                                   
REMARK 500    ASP A1112     -156.53   -117.53                                   
REMARK 500    TYR B 822      108.34    -35.25                                   
REMARK 500    GLU B 934       32.82   -148.26                                   
REMARK 500    PRO B 937       20.28    -70.93                                   
REMARK 500    ARG B1027       -4.86     81.70                                   
REMARK 500    ASP B1028       56.08   -158.19                                   
REMARK 500    GLU B1038      175.77    -56.91                                   
REMARK 500    LYS B1039       20.97     43.56                                   
REMARK 500    ASN B1040       71.74     31.78                                   
REMARK 500    PRO B1068      -20.75    -39.02                                   
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 706 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 706 B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P2I   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A SIMILAR INHIBITOR                  
DBREF  3EFL A  815   939  UNP    P35968   VGFR2_HUMAN    815    939             
DBREF  3EFL B  815   939  UNP    P35968   VGFR2_HUMAN    815    939             
DBREF  3EFL A  990  1171  UNP    P35968   VGFR2_HUMAN    990   1171             
DBREF  3EFL B  990  1171  UNP    P35968   VGFR2_HUMAN    990   1171             
SEQADV 3EFL ALA A  817  UNP  P35968    CYS   817 ENGINEERED MUTATION            
SEQADV 3EFL VAL A  990  UNP  P35968    GLU   990 ENGINEERED MUTATION            
SEQADV 3EFL ARG A 1172  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1173  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1174  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1175  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1176  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1177  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS A 1178  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL ALA B  817  UNP  P35968    CYS   817 ENGINEERED MUTATION            
SEQADV 3EFL VAL B  990  UNP  P35968    GLU   990 ENGINEERED MUTATION            
SEQADV 3EFL ARG B 1172  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS B 1173  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS B 1174  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS B 1175  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS B 1176  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL HIS B 1177  UNP  P35968              EXPRESSION TAG                 
SEQADV 3EFL 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 VAL 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 VAL 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    706  A 501      28                                                       
HET    706  B 502      28                                                       
HETNAM     706 N-(3,3-DIMETHYL-2,3-DIHYDRO-1H-INDOL-6-YL)-2-[(PYRIDIN-          
HETNAM   2 706  4-YLMETHYL)AMINO]PYRIDINE-3-CARBOXAMIDE                         
FORMUL   3  706    2(C22 H23 N5 O)                                              
FORMUL   5  HOH   *142(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 PRO A 1068  MET A 1072  5                                   5    
HELIX    9   9 ALA A 1073  ARG A 1080  1                                   8    
HELIX   10  10 THR A 1083  PHE A 1099  1                                  17    
HELIX   11  11 ASP A 1112  GLY A 1122  1                                  11    
HELIX   12  12 THR A 1132  TRP A 1143  1                                  12    
HELIX   13  13 GLU A 1146  ARG A 1150  5                                   5    
HELIX   14  14 THR A 1152  HIS A 1178  1                                  27    
HELIX   15  15 ASP B  823  GLU B  828  1                                   6    
HELIX   16  16 PRO B  830  ASP B  832  5                                   3    
HELIX   17  17 THR B  875  GLY B  893  1                                  19    
HELIX   18  18 ASN B  923  LYS B  931  1                                   9    
HELIX   19  19 LEU B 1002  ARG B 1022  1                                  21    
HELIX   20  20 ALA B 1030  ARG B 1032  5                                   3    
HELIX   21  21 LEU B 1067  MET B 1072  5                                   6    
HELIX   22  22 ALA B 1073  ARG B 1080  1                                   8    
HELIX   23  23 THR B 1083  PHE B 1099  1                                  17    
HELIX   24  24 ASP B 1112  GLY B 1122  1                                  11    
HELIX   25  25 THR B 1132  TRP B 1143  1                                  12    
HELIX   26  26 GLU B 1146  ARG B 1150  5                                   5    
HELIX   27  27 THR B 1152  LEU B 1164  1                                  13    
SHEET    1   A 5 LEU A 834  GLY A 841  0                                        
SHEET    2   A 5 GLN A 847  PHE A 854 -1  O  VAL A 848   N  LEU A 840           
SHEET    3   A 5 CYS A 862  MET A 869 -1  O  ARG A 863   N  ALA A 853           
SHEET    4   A 5 MET A 913  GLU A 917 -1  O  VAL 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  GLY B 841  0                                        
SHEET    2   C 5 GLN B 847  PHE B 854 -1  O  VAL B 848   N  GLY B 841           
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  VAL 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  SER B1037  0                                        
SHEET    2   E 2 VAL B1041  ILE B1044 -1  O  LYS B1043   N  LEU B1035           
CISPEP   1 ALA A  991    PRO A  992          0        -0.10                     
SITE     1 AC1 14 HOH A  88  VAL A 848  ALA A 866  LYS A 868                    
SITE     2 AC1 14 GLU A 885  ILE A 892  VAL A 899  VAL A 914                    
SITE     3 AC1 14 GLU A 917  CYS A 919  HIS A1026  LEU A1035                    
SITE     4 AC1 14 CYS A1045  ASP A1046                                          
SITE     1 AC2 14 HOH B  82  VAL B 848  ALA B 866  LYS B 868                    
SITE     2 AC2 14 GLU B 885  LEU B 889  VAL B 916  GLU B 917                    
SITE     3 AC2 14 CYS B 919  HIS B1026  LEU B1035  CYS B1045                    
SITE     4 AC2 14 ASP B1046  PHE B1047                                          
CRYST1   55.590   66.810   91.420  90.00  93.27  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      0.017989  0.000000  0.001028        0.00000                         
SCALE2      0.000000  0.014968  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010956        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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