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Database: PDB
Entry: 1YWN
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Original site: 1YWN 
HEADER    TRANSFERASE                             18-FEB-05   1YWN              
TITLE     VEGFR2 IN COMPLEX WITH A NOVEL 4-AMINO-FURO[2,3-D]PYRIMIDINE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: VEGFR-2, KINASE INSERT DOMAIN RECEPTOR, PROTEIN-TYROSINE    
COMPND   6 KINASE RECEPTOR FLK-1;                                               
COMPND   7 EC: 2.7.1.112;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: E990V, DELETION OF RESIDUES 940-989                   
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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MIYAZAKI,S.MATSUNAGA,J.TANG,Y.MAEDA,M.NAKANO,R.J.PHILIPPE,          
AUTHOR   2 M.SHIBAHARA,W.LIU,H.SATO,L.WANG,R.T.NOLTE                            
REVDAT   4   11-OCT-17 1YWN    1       REMARK                                   
REVDAT   3   13-JUL-11 1YWN    1       VERSN                                    
REVDAT   2   24-FEB-09 1YWN    1       VERSN                                    
REVDAT   1   23-AUG-05 1YWN    0                                                
JRNL        AUTH   Y.MIYAZAKI,S.MATSUNAGA,J.TANG,Y.MAEDA,M.NAKANO,R.J.PHILIPPE, 
JRNL        AUTH 2 M.SHIBAHARA,W.LIU,H.SATO,L.WANG,R.T.NOLTE                    
JRNL        TITL   NOVEL 4-AMINO-FURO[2,3-D]PYRIMIDINES AS TIE-2 AND VEGFR2     
JRNL        TITL 2 DUAL INHIBITORS                                              
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  15  2203 2005              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   15837294                                                     
JRNL        DOI    10.1016/J.BMCL.2005.03.034                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE KINASE DOMAIN OF HUMAN VASCULAR     
REMARK   1  TITL 2 ENDOTHELIAL GROWTH FACTOR RECEPTOR 2: A KEY ENZYME IN        
REMARK   1  TITL 3 ANGIOGENESIS                                                 
REMARK   1  REF    STRUCTURE                     V.   7   319 1999              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -3.000                         
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 35577                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1139                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.71                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2005                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2264                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : 1.12000                                              
REMARK   3    B33 (A**2) : -1.24000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.107         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.206         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2360 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2148 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3195 ; 1.485 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4983 ; 0.823 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   277 ; 5.922 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;32.683 ;22.981       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   409 ;12.752 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.288 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   342 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2570 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   506 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   477 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2072 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1165 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1208 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   136 ; 0.210 ; 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):    13 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    61 ; 0.205 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.168 ; 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):  1805 ; 1.213 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   567 ; 0.218 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2255 ; 1.365 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1152 ; 2.214 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   940 ; 3.067 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   818        A   920                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1180  34.2230   6.1800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1108 T22:  -0.0080                                     
REMARK   3      T33:  -0.0747 T12:  -0.0011                                     
REMARK   3      T13:   0.0002 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9558 L22:   2.4370                                     
REMARK   3      L33:   2.9376 L12:   0.1241                                     
REMARK   3      L13:  -0.5716 L23:   0.4925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0214 S12:   0.0724 S13:   0.0571                       
REMARK   3      S21:  -0.0612 S22:   0.0050 S23:   0.2199                       
REMARK   3      S31:  -0.0261 S32:  -0.0804 S33:  -0.0265                       
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   921        A  1169                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6840  41.4310  32.3890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1049 T22:   0.0431                                     
REMARK   3      T33:  -0.1020 T12:  -0.0155                                     
REMARK   3      T13:   0.0056 T23:  -0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7237 L22:   1.6632                                     
REMARK   3      L33:   2.6364 L12:   0.2735                                     
REMARK   3      L13:   0.5084 L23:   0.9058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0551 S12:  -0.0696 S13:  -0.0434                       
REMARK   3      S21:   0.0610 S22:  -0.0367 S23:   0.0696                       
REMARK   3      S31:   0.0962 S32:  -0.2470 S33:   0.0918                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 1YWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032005.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
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     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 6.430                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1Y6A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       18.97650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.90150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.79750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.90150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.97650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.79750            
REMARK 290   SMTRY3   4  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 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     MET A   804                                                      
REMARK 465     ASP A   805                                                      
REMARK 465     PRO A   806                                                      
REMARK 465     ASP A   807                                                      
REMARK 465     GLU A   808                                                      
REMARK 465     LEU A   809                                                      
REMARK 465     PRO A   810                                                      
REMARK 465     LEU A   811                                                      
REMARK 465     ASP A   812                                                      
REMARK 465     GLU A   813                                                      
REMARK 465     HIS A   814                                                      
REMARK 465     CYS A   815                                                      
REMARK 465     GLU A   816                                                      
REMARK 465     ARG A   817                                                      
REMARK 465     LYS A   869                                                      
REMARK 465     GLU A   870                                                      
REMARK 465     GLY A   871                                                      
REMARK 465     ALA A   872                                                      
REMARK 465     TYR A   936                                                      
REMARK 465     LYS A   937                                                      
REMARK 465     VAL A   988                                                      
REMARK 465     ALA A   989                                                      
REMARK 465     PRO A   990                                                      
REMARK 465     GLU A   991                                                      
REMARK 465     ASP A   992                                                      
REMARK 465     LEU A   993                                                      
REMARK 465     TYR A   994                                                      
REMARK 465     LYS A   995                                                      
REMARK 465     ASP A   996                                                      
REMARK 465     PHE A  1045                                                      
REMARK 465     GLY A  1046                                                      
REMARK 465     LEU A  1047                                                      
REMARK 465     ALA A  1048                                                      
REMARK 465     ARG A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS A  1005     O    HOH A   202              2.13            
REMARK 500   O    PRO A   819     O    HOH A   193              2.19            
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    LYS A 856       -9.26     75.28                                   
REMARK 500    ALA A 858       49.41    -83.07                                   
REMARK 500    ARG A1025      -17.60     82.87                                   
REMARK 500    ASP A1026       59.51   -146.56                                   
REMARK 500    SER A1035     -168.18   -108.28                                   
REMARK 500    ARG A1078       38.47     34.33                                   
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 LIF A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VR2   RELATED DB: PDB                                   
REMARK 900 VEGFR2 KINASE DOMAIN - UNLIGANDED STRUCTURE                          
REMARK 900 RELATED ID: 1Y6A   RELATED DB: PDB                                   
REMARK 900 VEGFR2 IN COMPLEX WITH A 2-ANILINO-5-ARYL-OXAZOLE INHIBITOR          
REMARK 900 RELATED ID: 1Y6B   RELATED DB: PDB                                   
REMARK 900 VEGFR2 IN COMPLEX WITH A 2-ANILINO-5-ARYL-OXAZOLE INHIBITOR          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DELETION OF RESIDUES 938-987 (CORRESPONDS TO DBREF 940-989)          
DBREF  1YWN A  804  1169  UNP    P35968   VGFR2_HUMAN    806   1171             
SEQADV 1YWN VAL A  988  UNP  P35968    GLU   990 ENGINEERED                     
SEQADV 1YWN PTR A 1052  UNP  P35968    TYR  1054 MODIFIED RESIDUE               
SEQADV 1YWN PTR A 1057  UNP  P35968    TYR  1059 MODIFIED RESIDUE               
SEQRES   1 A  316  MET ASP PRO ASP GLU LEU PRO LEU ASP GLU HIS CYS GLU          
SEQRES   2 A  316  ARG LEU PRO TYR ASP ALA SER LYS TRP GLU PHE PRO ARG          
SEQRES   3 A  316  ASP ARG LEU LYS LEU GLY LYS PRO LEU GLY ARG GLY ALA          
SEQRES   4 A  316  PHE GLY GLN VAL ILE GLU ALA ASP ALA PHE GLY ILE ASP          
SEQRES   5 A  316  LYS THR ALA THR CYS ARG THR VAL ALA VAL LYS MET LEU          
SEQRES   6 A  316  LYS GLU GLY ALA THR HIS SER GLU HIS ARG ALA LEU MET          
SEQRES   7 A  316  SER GLU LEU LYS ILE LEU ILE HIS ILE GLY HIS HIS LEU          
SEQRES   8 A  316  ASN VAL VAL ASN LEU LEU GLY ALA CYS THR LYS PRO GLY          
SEQRES   9 A  316  GLY PRO LEU MET VAL ILE VAL GLU PHE CYS LYS PHE GLY          
SEQRES  10 A  316  ASN LEU SER THR TYR LEU ARG SER LYS ARG ASN GLU PHE          
SEQRES  11 A  316  VAL PRO TYR LYS VAL ALA PRO GLU ASP LEU TYR LYS ASP          
SEQRES  12 A  316  PHE LEU THR LEU GLU HIS LEU ILE CYS TYR SER PHE GLN          
SEQRES  13 A  316  VAL ALA LYS GLY MET GLU PHE LEU ALA SER ARG LYS CYS          
SEQRES  14 A  316  ILE HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU LEU SER          
SEQRES  15 A  316  GLU LYS ASN VAL VAL LYS ILE CYS ASP PHE GLY LEU ALA          
SEQRES  16 A  316  ARG ASP ILE PTR LYS ASP PRO ASP PTR VAL ARG LYS GLY          
SEQRES  17 A  316  ASP ALA ARG LEU PRO LEU LYS TRP MET ALA PRO GLU THR          
SEQRES  18 A  316  ILE PHE ASP ARG VAL TYR THR ILE GLN SER ASP VAL TRP          
SEQRES  19 A  316  SER PHE GLY VAL LEU LEU TRP GLU ILE PHE SER LEU GLY          
SEQRES  20 A  316  ALA SER PRO TYR PRO GLY VAL LYS ILE ASP GLU GLU PHE          
SEQRES  21 A  316  CYS ARG ARG LEU LYS GLU GLY THR ARG MET ARG ALA PRO          
SEQRES  22 A  316  ASP TYR THR THR PRO GLU MET TYR GLN THR MET LEU ASP          
SEQRES  23 A  316  CYS TRP HIS GLY GLU PRO SER GLN ARG PRO THR PHE SER          
SEQRES  24 A  316  GLU LEU VAL GLU HIS LEU GLY ASN LEU LEU GLN ALA ASN          
SEQRES  25 A  316  ALA GLN GLN ASP                                              
MODRES 1YWN PTR A 1052  TYR  O-PHOSPHOTYROSINE                                  
MODRES 1YWN PTR A 1057  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1052      16                                                       
HET    PTR  A1057      16                                                       
HET    LIF  A 301      39                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     LIF N-{4-[4-AMINO-6-(4-METHOXYPHENYL)FURO[2,3-D]PYRIMIDIN-           
HETNAM   2 LIF  5-YL]PHENYL}-N'-[2-FLUORO-5-(TRIFLUOROMETHYL)                   
HETNAM   3 LIF  PHENYL]UREA                                                     
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     LIF N-(4-{4-AMINO-6-[4-(METHYLOXY)PHENYL]FURO[2,3-                   
HETSYN   2 LIF  D]PYRIMIDIN-5-YL}PHENYL)-N'-[2-FLUORO-5-                        
HETSYN   3 LIF  (TRIFLUOROMETHYL)PHENYL]UREA                                    
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   2  LIF    C27 H19 F4 N5 O3                                             
FORMUL   3  HOH   *209(H2 O)                                                    
HELIX    1   1 ASP A  821  GLU A  826  1                                   6    
HELIX    2   2 PRO A  828  ASP A  830  5                                   3    
HELIX    3   3 THR A  873  GLY A  891  1                                  19    
HELIX    4   4 ASN A  921  LYS A  929  1                                   9    
HELIX    5   5 ARG A  930  PHE A  933  5                                   4    
HELIX    6   6 THR A  999  ARG A 1020  1                                  22    
HELIX    7   7 ALA A 1028  ARG A 1030  5                                   3    
HELIX    8   8 GLU A 1036  ASN A 1038  5                                   3    
HELIX    9   9 LEU A 1065  MET A 1070  5                                   6    
HELIX   10  10 ALA A 1071  ARG A 1078  1                                   8    
HELIX   11  11 THR A 1081  SER A 1098  1                                  18    
HELIX   12  12 ASP A 1110  GLY A 1120  1                                  11    
HELIX   13  13 THR A 1130  TRP A 1141  1                                  12    
HELIX   14  14 GLU A 1144  ARG A 1148  5                                   5    
HELIX   15  15 THR A 1150  ALA A 1166  1                                  17    
SHEET    1   A 5 LEU A 832  ARG A 840  0                                        
SHEET    2   A 5 GLN A 845  PHE A 852 -1  O  VAL A 846   N  GLY A 839           
SHEET    3   A 5 CYS A 860  MET A 867 -1  O  ARG A 861   N  ALA A 851           
SHEET    4   A 5 MET A 911  GLU A 915 -1  O  VAL A 912   N  LYS A 866           
SHEET    5   A 5 LEU A 899  CYS A 903 -1  N  LEU A 900   O  ILE A 913           
SHEET    1   B 2 ILE A1032  LEU A1034  0                                        
SHEET    2   B 2 VAL A1040  ILE A1042 -1  O  LYS A1041   N  LEU A1033           
LINK         C   ILE A1051                 N   PTR A1052     1555   1555  1.34  
LINK         C   PTR A1052                 N   LYS A1053     1555   1555  1.33  
LINK         C   ASP A1056                 N   PTR A1057     1555   1555  1.33  
LINK         C   PTR A1057                 N   VAL A1058     1555   1555  1.33  
SITE     1 AC1 18 HOH A 127  LEU A 838  GLY A 839  ARG A 840                    
SITE     2 AC1 18 GLY A 841  VAL A 846  ALA A 864  GLU A 883                    
SITE     3 AC1 18 VAL A 896  VAL A 897  GLU A 915  PHE A 916                    
SITE     4 AC1 18 CYS A 917  LEU A1017  HIS A1024  ILE A1042                    
SITE     5 AC1 18 CYS A1043  ASP A1044                                          
CRYST1   37.953   95.595   95.803  90.00  90.00  90.00 P 21 21 21    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      0.026348  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010461  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010438        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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