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Database: PDB
Entry: 3HNG
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HEADER    TRANSFERASE                             31-MAY-09   3HNG              
TITLE     CRYSTAL STRUCTURE OF VEGFR1 IN COMPLEX WITH N-(4-CHLOROPHENYL)-2-     
TITLE    2 ((PYRIDIN-4-YLMETHYL)AMINO)BENZAMIDE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 801-1158;                      
COMPND   5 SYNONYM: VEGFR-1, VASCULAR PERMEABILITY FACTOR RECEPTOR, TYROSINE-   
COMPND   6 PROTEIN KINASE RECEPTOR FLT, FLT-1, TYROSINE-PROTEIN KINASE FRT, FMS-
COMPND   7 LIKE TYROSINE KINASE 1;                                              
COMPND   8 EC: 2.7.10.1;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FLT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PRARE;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    RECEPTOR TYROSINE KINASE, VEGFR1,FLT1,KINASE DOMAIN,INHIBITOR,        
KEYWDS   2 ACTIVATION LOOP,VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR,         
KEYWDS   3 STRUCTURAL GENOMICS,STRUCTURAL GENOMICS CONSORTIUM,SGC,SGC           
KEYWDS   4 STOCKHOLM, ANGIOGENESIS, ATP-BINDING, CELL MEMBRANE, DEVELOPMENTAL   
KEYWDS   5 PROTEIN, DIFFERENTIATION, DISULFIDE BOND, GLYCOPROTEIN,              
KEYWDS   6 IMMUNOGLOBULIN DOMAIN, KINASE, MEMBRANE, NUCLEOTIDE-BINDING,         
KEYWDS   7 PHOSPHOPROTEIN, RECEPTOR, SECRETED, TRANSFERASE, TRANSMEMBRANE,      
KEYWDS   8 TYROSINE-PROTEIN KINASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.TRESAUGUES,A.ROOS,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,R.COLLINS,    
AUTHOR   2 A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,  
AUTHOR   3 I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,M.MOCHE,T.NYMAN,C.PERSSON,        
AUTHOR   4 T.KRAGH-NIELSEN,A.KOTZCH,J.SAGEMARK,H.SCHUELER,P.SCHUTZ,M.I.SIPONEN, 
AUTHOR   5 L.SVENSSON,A.G.THORSELL,S.VAN DER BERG,J.WEIGELT,M.WELIN,            
AUTHOR   6 M.WISNIEWSKA,P.NORDLUND,STRUCTURAL GENOMICS CONSORTIUM (SGC)         
REVDAT   2   13-JUL-11 3HNG    1       VERSN                                    
REVDAT   1   30-JUN-09 3HNG    0                                                
JRNL        AUTH   L.TRESAUGUES,A.ROOS,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,     
JRNL        AUTH 2 R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,          
JRNL        AUTH 3 M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,T.KARLBERG,            
JRNL        AUTH 4 T.KOTENYOVA,M.MOCHE,T.NYMAN,C.PERSSON,T.KRAGH-NIELSEN,       
JRNL        AUTH 5 A.KOTZCH,J.SAGEMARK,H.SCHUELER,P.SCHUTZ,M.I.SIPONEN,         
JRNL        AUTH 6 L.SVENSSON,A.G.THORSELL,S.VAN DER BERG,J.WEIGELT,M.WELIN,    
JRNL        AUTH 7 M.WISNIEWSKA,P.NORDLUND                                      
JRNL        TITL   CRYSTAL STRUCTURE OF VEGFR1 IN COMPLEX WITH                  
JRNL        TITL 2 N-(4-CHLOROPHENYL)-2-((PYRIDIN-4-YLMETHYL)AMINO)BENZAMIDE    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10998                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 551                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 798                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 33                           
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2290                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 65.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 1.14000                                              
REMARK   3    B33 (A**2) : -1.23000                                             
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): 0.654         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.331         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.232         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.981        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2374 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2186 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3196 ; 1.460 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5086 ; 0.640 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   286 ; 7.077 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   101 ;32.976 ;23.168       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   433 ;19.825 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.508 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   343 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2583 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   495 ; 0.000 ; 0.021       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1434 ; 0.547 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   584 ; 0.094 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2304 ; 1.086 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   940 ; 1.584 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   891 ; 2.727 ; 4.500       
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  : 3                                          
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   803        A   818                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2550  33.5610  34.9560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9245 T22:   1.0044                                     
REMARK   3      T33:   1.3602 T12:  -0.3877                                     
REMARK   3      T13:  -0.0829 T23:   0.1977                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8434 L22:   5.9662                                     
REMARK   3      L33:   8.2998 L12:   5.1424                                     
REMARK   3      L13:  -6.7994 L23:  -5.8046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5017 S12:  -0.1379 S13:   0.6433                       
REMARK   3      S21:   1.5686 S22:  -0.4986 S23:  -0.7771                       
REMARK   3      S31:  -2.0899 S32:   0.6879 S33:  -1.0031                       
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   819        A   925                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7040  16.4860  37.9550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0397 T22:   0.0860                                     
REMARK   3      T33:   0.0582 T12:  -0.0047                                     
REMARK   3      T13:   0.0104 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1897 L22:   1.3592                                     
REMARK   3      L33:   4.9452 L12:  -0.4202                                     
REMARK   3      L13:   0.7073 L23:   0.2763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1324 S12:  -0.2282 S13:  -0.0083                       
REMARK   3      S21:   0.0456 S22:  -0.1085 S23:   0.0412                       
REMARK   3      S31:   0.2883 S32:  -0.0291 S33:  -0.0239                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   992        A  1158                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6020  17.9350  15.6330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1364 T22:   0.1750                                     
REMARK   3      T33:   0.0167 T12:   0.0289                                     
REMARK   3      T13:  -0.0057 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9522 L22:   3.7270                                     
REMARK   3      L33:   5.7472 L12:   0.2827                                     
REMARK   3      L13:   0.6757 L23:   0.3388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:   0.5707 S13:   0.0520                       
REMARK   3      S21:  -0.3207 S22:   0.0732 S23:  -0.1965                       
REMARK   3      S31:   0.2258 S32:   0.7144 S33:  -0.0747                       
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 3HNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053349.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300                            
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL ZERODUR MIRROR            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11958                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2QU5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FORMATE, 20% PEG 3350,    
REMARK 280  PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       29.02000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       35.57500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       98.01000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.02000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       35.57500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       98.01000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.02000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       35.57500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       98.01000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.02000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       35.57500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       98.01000            
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     SER A   799                                                      
REMARK 465     MET A   800                                                      
REMARK 465     PRO A   801                                                      
REMARK 465     ASP A   802                                                      
REMARK 465     LEU A   813                                                      
REMARK 465     ASP A   926                                                      
REMARK 465     LEU A   927                                                      
REMARK 465     PHE A   928                                                      
REMARK 465     PHE A   929                                                      
REMARK 465     LEU A   930                                                      
REMARK 465     ASN A   931                                                      
REMARK 465     LYS A   932                                                      
REMARK 465     ASP A   933                                                      
REMARK 465     ALA A   934                                                      
REMARK 465     ALA A   935                                                      
REMARK 465     LEU A   936                                                      
REMARK 465     HIS A   937                                                      
REMARK 465     MET A   938                                                      
REMARK 465     GLU A   939                                                      
REMARK 465     PRO A   940                                                      
REMARK 465     LYS A   941                                                      
REMARK 465     LYS A   942                                                      
REMARK 465     GLU A   943                                                      
REMARK 465     LYS A   944                                                      
REMARK 465     MET A   945                                                      
REMARK 465     GLU A   946                                                      
REMARK 465     PRO A   947                                                      
REMARK 465     GLY A   948                                                      
REMARK 465     LEU A   949                                                      
REMARK 465     GLU A   950                                                      
REMARK 465     GLN A   951                                                      
REMARK 465     GLY A   952                                                      
REMARK 465     LYS A   953                                                      
REMARK 465     LYS A   954                                                      
REMARK 465     PRO A   955                                                      
REMARK 465     ARG A   956                                                      
REMARK 465     LEU A   957                                                      
REMARK 465     ASP A   958                                                      
REMARK 465     SER A   959                                                      
REMARK 465     VAL A   960                                                      
REMARK 465     THR A   961                                                      
REMARK 465     SER A   962                                                      
REMARK 465     SER A   963                                                      
REMARK 465     GLU A   964                                                      
REMARK 465     SER A   965                                                      
REMARK 465     PHE A   966                                                      
REMARK 465     ALA A   967                                                      
REMARK 465     SER A   968                                                      
REMARK 465     SER A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     PHE A   971                                                      
REMARK 465     GLN A   972                                                      
REMARK 465     GLU A   973                                                      
REMARK 465     ASP A   974                                                      
REMARK 465     LYS A   975                                                      
REMARK 465     SER A   976                                                      
REMARK 465     LEU A   977                                                      
REMARK 465     SER A   978                                                      
REMARK 465     ASP A   979                                                      
REMARK 465     VAL A   980                                                      
REMARK 465     GLU A   981                                                      
REMARK 465     GLU A   982                                                      
REMARK 465     GLU A   983                                                      
REMARK 465     GLU A   984                                                      
REMARK 465     ASP A   985                                                      
REMARK 465     SER A   986                                                      
REMARK 465     ASP A   987                                                      
REMARK 465     GLY A   988                                                      
REMARK 465     PHE A   989                                                      
REMARK 465     TYR A   990                                                      
REMARK 465     GLY A  1057                                                      
REMARK 465     ASP A  1058                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 812    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 991    CG   CD   CE   NZ                                   
REMARK 470     ARG A1055    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1056    CG   CD   CE   NZ                                   
REMARK 470     ARG A1139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A  1146     OE2  GLU A  1152     2565     2.18            
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    CYS A 810       39.73    -87.63                                   
REMARK 500    ASP A 816       73.12   -108.28                                   
REMARK 500    SER A 818      -31.33    -37.64                                   
REMARK 500    ILE A 885      -59.86   -122.96                                   
REMARK 500    LYS A 900      125.88    -30.64                                   
REMARK 500    ARG A1021       -7.08     79.26                                   
REMARK 500    ASP A1022       50.19   -152.76                                   
REMARK 500    ALA A1024      165.73    177.59                                   
REMARK 500    SER A1031     -161.99   -107.68                                   
REMARK 500    MET A1105       77.41   -110.09                                   
REMARK 500    ASP A1106     -167.81   -119.89                                   
REMARK 500    CYS A1110      -72.25    -70.73                                   
REMARK 500    SER A1111      -38.62    -35.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  886     HIS A  887                   42.37                    
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 8ST A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3035                 
DBREF  3HNG A  801  1158  UNP    P17948   VGFR1_HUMAN    801   1158             
SEQADV 3HNG SER A  799  UNP  P17948              EXPRESSION TAG                 
SEQADV 3HNG MET A  800  UNP  P17948              EXPRESSION TAG                 
SEQRES   1 A  360  SER MET PRO ASP GLU VAL PRO LEU ASP GLU GLN CYS GLU          
SEQRES   2 A  360  ARG LEU PRO TYR ASP ALA SER LYS TRP GLU PHE ALA ARG          
SEQRES   3 A  360  GLU ARG LEU LYS LEU GLY LYS SER LEU GLY ARG GLY ALA          
SEQRES   4 A  360  PHE GLY LYS VAL VAL GLN ALA SER ALA PHE GLY ILE LYS          
SEQRES   5 A  360  LYS SER PRO THR CYS ARG THR VAL ALA VAL LYS MET LEU          
SEQRES   6 A  360  LYS GLU GLY ALA THR ALA SER GLU TYR LYS ALA LEU MET          
SEQRES   7 A  360  THR GLU LEU LYS ILE LEU THR HIS ILE GLY HIS HIS LEU          
SEQRES   8 A  360  ASN VAL VAL ASN LEU LEU GLY ALA CYS THR LYS GLN GLY          
SEQRES   9 A  360  GLY PRO LEU MET VAL ILE VAL GLU TYR CYS LYS TYR GLY          
SEQRES  10 A  360  ASN LEU SER ASN TYR LEU LYS SER LYS ARG ASP LEU PHE          
SEQRES  11 A  360  PHE LEU ASN LYS ASP ALA ALA LEU HIS MET GLU PRO LYS          
SEQRES  12 A  360  LYS GLU LYS MET GLU PRO GLY LEU GLU GLN GLY LYS LYS          
SEQRES  13 A  360  PRO ARG LEU ASP SER VAL THR SER SER GLU SER PHE ALA          
SEQRES  14 A  360  SER SER GLY PHE GLN GLU ASP LYS SER LEU SER ASP VAL          
SEQRES  15 A  360  GLU GLU GLU GLU ASP SER ASP GLY PHE TYR LYS GLU PRO          
SEQRES  16 A  360  ILE THR MET GLU ASP LEU ILE SER TYR SER PHE GLN VAL          
SEQRES  17 A  360  ALA ARG GLY MET GLU PHE LEU SER SER ARG LYS CYS ILE          
SEQRES  18 A  360  HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU LEU SER GLU          
SEQRES  19 A  360  ASN ASN VAL VAL LYS ILE CYS ASP PHE GLY LEU ALA ARG          
SEQRES  20 A  360  ASP ILE TYR LYS ASN PRO ASP TYR VAL ARG LYS GLY ASP          
SEQRES  21 A  360  THR ARG LEU PRO LEU LYS TRP MET ALA PRO GLU SER ILE          
SEQRES  22 A  360  PHE ASP LYS ILE TYR SER THR LYS SER ASP VAL TRP SER          
SEQRES  23 A  360  TYR GLY VAL LEU LEU TRP GLU ILE PHE SER LEU GLY GLY          
SEQRES  24 A  360  SER PRO TYR PRO GLY VAL GLN MET ASP GLU ASP PHE CYS          
SEQRES  25 A  360  SER ARG LEU ARG GLU GLY MET ARG MET ARG ALA PRO GLU          
SEQRES  26 A  360  TYR SER THR PRO GLU ILE TYR GLN ILE MET LEU ASP CYS          
SEQRES  27 A  360  TRP HIS ARG ASP PRO LYS GLU ARG PRO ARG PHE ALA GLU          
SEQRES  28 A  360  LEU VAL GLU LYS LEU GLY ASP LEU LEU                          
HET    8ST  A2001      24                                                       
HET     CL  A3035       1                                                       
HETNAM     8ST N-(4-CHLOROPHENYL)-2-[(PYRIDIN-4-YLMETHYL)                       
HETNAM   2 8ST  AMINO]BENZAMIDE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  8ST    C19 H16 CL N3 O                                              
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *33(H2 O)                                                     
HELIX    1   1 PRO A  805  CYS A  810  1                                   6    
HELIX    2   2 ASP A  816  GLU A  821  1                                   6    
HELIX    3   3 ALA A  823  GLU A  825  5                                   3    
HELIX    4   4 ILE A  849  SER A  852  5                                   4    
HELIX    5   5 THR A  868  HIS A  884  1                                  17    
HELIX    6   6 ASN A  916  SER A  923  1                                   8    
HELIX    7   7 THR A  995  SER A 1015  1                                  21    
HELIX    8   8 ALA A 1024  ARG A 1026  5                                   3    
HELIX    9   9 GLU A 1032  ASN A 1034  5                                   3    
HELIX   10  10 PHE A 1041  ARG A 1045  5                                   5    
HELIX   11  11 PRO A 1062  MET A 1066  5                                   5    
HELIX   12  12 ALA A 1067  LYS A 1074  1                                   8    
HELIX   13  13 SER A 1077  SER A 1094  1                                  18    
HELIX   14  14 ASP A 1106  ARG A 1114  1                                   9    
HELIX   15  15 THR A 1126  TRP A 1137  1                                  12    
HELIX   16  16 ASP A 1140  ARG A 1144  5                                   5    
HELIX   17  17 ARG A 1146  LEU A 1158  1                                  13    
SHEET    1   A 5 LEU A 827  ARG A 835  0                                        
SHEET    2   A 5 GLY A 839  PHE A 847 -1  O  VAL A 841   N  LEU A 833           
SHEET    3   A 5 CYS A 855  LEU A 863 -1  O  ARG A 856   N  ALA A 846           
SHEET    4   A 5 MET A 906  GLU A 910 -1  O  VAL A 909   N  ALA A 859           
SHEET    5   A 5 LEU A 894  CYS A 898 -1  N  LEU A 895   O  ILE A 908           
SHEET    1   B 2 ILE A1028  LEU A1030  0                                        
SHEET    2   B 2 VAL A1036  ILE A1038 -1  O  LYS A1037   N  LEU A1029           
SITE     1 AC1 12 LYS A 861  GLU A 878  VAL A 907  VAL A 909                    
SITE     2 AC1 12 GLU A 910  TYR A 911  CYS A 912  LEU A1013                    
SITE     3 AC1 12 LEU A1029  ILE A1038  CYS A1039  ASP A1040                    
SITE     1 AC2  1 LYS A 850                                                     
CRYST1   58.040   71.150  196.020  90.00  90.00  90.00 I 2 2 2       8          
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      0.017229  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014055  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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