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Database: PDB
Entry: 3C4F
LinkDB: 3C4F
Original site: 3C4F 
HEADER    TRANSFERASE                             29-JAN-08   3C4F              
TITLE     FGFR TYROSINE KINASE DOMAIN IN COMPLEX WITH 3-(3-                     
TITLE    2 METHOXYBENZYL)-7-AZAINDOLE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BASIC FIBROBLAST GROWTH FACTOR RECEPTOR 1;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: FGFR-1, BFGF-R, FMS-LIKE TYROSINE KINASE 2, C-FGR,          
COMPND   6 CD331 ANTIGEN;                                                       
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FGFR1, FGFBR, FLG, FLT2;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;                               
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET29A                                     
KEYWDS    FIBROBLAST GROWTH FACTOR RECEPTOR, TYROSINE KINASE DOMAIN,            
KEYWDS   2 RECEPTOR TYROSINE KINASE, FGFR1, FGFR, ALTERNATIVE SPLICING,         
KEYWDS   3 ATP-BINDING, CHROMOSOMAL REARRANGEMENT, DISEASE MUTATION,            
KEYWDS   4 DWARFISM, GLYCOPROTEIN, HEPARIN-BINDING, IMMUNOGLOBULIN              
KEYWDS   5 DOMAIN, KALLMANN SYNDROME, MEMBRANE, NUCLEOTIDE-BINDING,             
KEYWDS   6 PHOSPHOPROTEIN, POLYMORPHISM, TRANSFERASE, TRANSMEMBRANE,            
KEYWDS   7 TYROSINE-PROTEIN KINASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.Y.J.ZHANG,W.WANG                                                    
REVDAT   3   24-FEB-09 3C4F    1       VERSN                                    
REVDAT   2   18-MAR-08 3C4F    1       JRNL                                     
REVDAT   1   26-FEB-08 3C4F    0                                                
JRNL        AUTH   J.TSAI,J.T.LEE,W.WANG,J.ZHANG,H.CHO,S.MAMO,                  
JRNL        AUTH 2 R.BREMER,S.GILLETTE,J.KONG,N.K.HAASS,K.SPROESSER,            
JRNL        AUTH 3 L.LI,K.S.SMALLEY,D.FONG,Y.L.ZHU,A.MARIMUTHU,                 
JRNL        AUTH 4 H.NGUYEN,B.LAM,J.LIU,I.CHEUNG,J.RICE,Y.SUZUKI,               
JRNL        AUTH 5 C.LUU,C.SETTACHATGUL,R.SHELLOOE,J.CANTWELL,S.H.KIM,          
JRNL        AUTH 6 J.SCHLESSINGER,K.Y.ZHANG,B.L.WEST,B.POWELL,                  
JRNL        AUTH 7 G.HABETS,C.ZHANG,P.N.IBRAHIM,P.HIRTH,D.R.ARTIS,              
JRNL        AUTH 8 M.HERLYN,G.BOLLAG                                            
JRNL        TITL   DISCOVERY OF A SELECTIVE INHIBITOR OF ONCOGENIC              
JRNL        TITL 2 B-RAF KINASE WITH POTENT ANTIMELANOMA ACTIVITY               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  3041 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18287029                                                     
JRNL        DOI    10.1073/PNAS.0711741105                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.25                                        
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) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 40646                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2167                            
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) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.12                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2939                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 184                          
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4639                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 356                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.42000                                             
REMARK   3    B22 (A**2) : 3.85000                                              
REMARK   3    B33 (A**2) : -1.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.79000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.224         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.200         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.242         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4776 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4392 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6450 ; 1.592 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10252 ; 0.936 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   576 ; 3.196 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   702 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5208 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   924 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   989 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4954 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2823 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   291 ; 0.190 ; 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):    20 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   104 ; 0.273 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 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):  2896 ; 0.729 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4678 ; 1.354 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1880 ; 1.913 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1772 ; 3.213 ; 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  : NULL                                       
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3C4F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046327.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44044                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.79300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG10K, 0.3M (NH4)2SO4, 5%           
REMARK 280  ETHYLENE GLYCOL, 100 MM BIS-TRIS PH 6.5, VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
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        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      104.09500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.81150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      104.09500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.81150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A   580                                                      
REMARK 465     LEU A   581                                                      
REMARK 465     GLU A   582                                                      
REMARK 465     TYR A   583                                                      
REMARK 465     CYS A   584                                                      
REMARK 465     TYR A   585                                                      
REMARK 465     ASN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     SER A   588                                                      
REMARK 465     HIS A   589                                                      
REMARK 465     ASN A   590                                                      
REMARK 465     PRO A   591                                                      
REMARK 465     GLY B   580                                                      
REMARK 465     LEU B   581                                                      
REMARK 465     GLU B   582                                                      
REMARK 465     TYR B   583                                                      
REMARK 465     CYS B   584                                                      
REMARK 465     TYR B   585                                                      
REMARK 465     ASN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     SER B   588                                                      
REMARK 465     HIS B   589                                                      
REMARK 465     ASN B   590                                                      
REMARK 465     PRO B   591                                                      
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   O    SER B   518     O    HOH B   332              2.13            
REMARK 500   OE1  GLU B   464     O    HOH B    78              2.18            
REMARK 500   OD1  ASP B   519     O    HOH B   326              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP B 519   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 623   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 647   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 753   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 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    GLU A 486       46.46     36.75                                   
REMARK 500    ASP A 519       49.83   -101.98                                   
REMARK 500    GLU A 593      118.29    -31.60                                   
REMARK 500    ARG A 622      -17.47     84.79                                   
REMARK 500    ASP A 623       52.07   -141.67                                   
REMARK 500    TRP A 737       30.18    -95.55                                   
REMARK 500    GLN A 764      -57.07    118.83                                   
REMARK 500    LEU B 500      -74.38     62.25                                   
REMARK 500    PRO B 505        7.13    -60.09                                   
REMARK 500    ASP B 519       44.36    -93.44                                   
REMARK 500    ARG B 622      -33.67     86.40                                   
REMARK 500    ALA B 645       68.91   -107.59                                   
REMARK 500    THR B 658        1.49    -63.79                                   
REMARK 500    GLN B 764      -58.65    120.86                                   
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 C4F A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C4F B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C4C   RELATED DB: PDB                                   
REMARK 900 B-RAF KINASE IN COMPLEX WITH PLX4720                                 
REMARK 900 RELATED ID: 3C4D   RELATED DB: PDB                                   
REMARK 900 B-RAF KINASE V600E ONCOGENIC MUTANT IN COMPLEX WITH PLX3203          
REMARK 900 RELATED ID: 3C4E   RELATED DB: PDB                                   
REMARK 900 PIM-1 KINASE DOMAIN IN COMPLEX WITH 3-AMINOPHENYL-7-                 
REMARK 900 AZAINDOLE                                                            
DBREF  3C4F A  464   765  UNP    P11362   FGFR1_HUMAN    464    765             
DBREF  3C4F B  464   765  UNP    P11362   FGFR1_HUMAN    464    765             
SEQADV 3C4F ALA A  488  UNP  P11362    CYS   488 ENGINEERED                     
SEQADV 3C4F ALA B  488  UNP  P11362    CYS   488 ENGINEERED                     
SEQRES   1 A  302  GLU LEU PRO GLU ASP PRO ARG TRP GLU LEU PRO ARG ASP          
SEQRES   2 A  302  ARG LEU VAL LEU GLY LYS PRO LEU GLY GLU GLY ALA PHE          
SEQRES   3 A  302  GLY GLN VAL VAL LEU ALA GLU ALA ILE GLY LEU ASP LYS          
SEQRES   4 A  302  ASP LYS PRO ASN ARG VAL THR LYS VAL ALA VAL LYS MET          
SEQRES   5 A  302  LEU LYS SER ASP ALA THR GLU LYS ASP LEU SER ASP LEU          
SEQRES   6 A  302  ILE SER GLU MET GLU MET MET LYS MET ILE GLY LYS HIS          
SEQRES   7 A  302  LYS ASN ILE ILE ASN LEU LEU GLY ALA CYS THR GLN ASP          
SEQRES   8 A  302  GLY PRO LEU TYR VAL ILE VAL GLU TYR ALA SER LYS GLY          
SEQRES   9 A  302  ASN LEU ARG GLU TYR LEU GLN ALA ARG ARG PRO PRO GLY          
SEQRES  10 A  302  LEU GLU TYR CYS TYR ASN PRO SER HIS ASN PRO GLU GLU          
SEQRES  11 A  302  GLN LEU SER SER LYS ASP LEU VAL SER CYS ALA TYR GLN          
SEQRES  12 A  302  VAL ALA ARG GLY MET GLU TYR LEU ALA SER LYS LYS CYS          
SEQRES  13 A  302  ILE HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL THR          
SEQRES  14 A  302  GLU ASP ASN VAL MET LYS ILE ALA ASP PHE GLY LEU ALA          
SEQRES  15 A  302  ARG ASP ILE HIS HIS ILE ASP TYR TYR LYS LYS THR THR          
SEQRES  16 A  302  ASN GLY ARG LEU PRO VAL LYS TRP MET ALA PRO GLU ALA          
SEQRES  17 A  302  LEU PHE ASP ARG ILE TYR THR HIS GLN SER ASP VAL TRP          
SEQRES  18 A  302  SER PHE GLY VAL LEU LEU TRP GLU ILE PHE THR LEU GLY          
SEQRES  19 A  302  GLY SER PRO TYR PRO GLY VAL PRO VAL GLU GLU LEU PHE          
SEQRES  20 A  302  LYS LEU LEU LYS GLU GLY HIS ARG MET ASP LYS PRO SER          
SEQRES  21 A  302  ASN CYS THR ASN GLU LEU TYR MET MET MET ARG ASP CYS          
SEQRES  22 A  302  TRP HIS ALA VAL PRO SER GLN ARG PRO THR PHE LYS GLN          
SEQRES  23 A  302  LEU VAL GLU ASP LEU ASP ARG ILE VAL ALA LEU THR SER          
SEQRES  24 A  302  ASN GLN GLU                                                  
SEQRES   1 B  302  GLU LEU PRO GLU ASP PRO ARG TRP GLU LEU PRO ARG ASP          
SEQRES   2 B  302  ARG LEU VAL LEU GLY LYS PRO LEU GLY GLU GLY ALA PHE          
SEQRES   3 B  302  GLY GLN VAL VAL LEU ALA GLU ALA ILE GLY LEU ASP LYS          
SEQRES   4 B  302  ASP LYS PRO ASN ARG VAL THR LYS VAL ALA VAL LYS MET          
SEQRES   5 B  302  LEU LYS SER ASP ALA THR GLU LYS ASP LEU SER ASP LEU          
SEQRES   6 B  302  ILE SER GLU MET GLU MET MET LYS MET ILE GLY LYS HIS          
SEQRES   7 B  302  LYS ASN ILE ILE ASN LEU LEU GLY ALA CYS THR GLN ASP          
SEQRES   8 B  302  GLY PRO LEU TYR VAL ILE VAL GLU TYR ALA SER LYS GLY          
SEQRES   9 B  302  ASN LEU ARG GLU TYR LEU GLN ALA ARG ARG PRO PRO GLY          
SEQRES  10 B  302  LEU GLU TYR CYS TYR ASN PRO SER HIS ASN PRO GLU GLU          
SEQRES  11 B  302  GLN LEU SER SER LYS ASP LEU VAL SER CYS ALA TYR GLN          
SEQRES  12 B  302  VAL ALA ARG GLY MET GLU TYR LEU ALA SER LYS LYS CYS          
SEQRES  13 B  302  ILE HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL THR          
SEQRES  14 B  302  GLU ASP ASN VAL MET LYS ILE ALA ASP PHE GLY LEU ALA          
SEQRES  15 B  302  ARG ASP ILE HIS HIS ILE ASP TYR TYR LYS LYS THR THR          
SEQRES  16 B  302  ASN GLY ARG LEU PRO VAL LYS TRP MET ALA PRO GLU ALA          
SEQRES  17 B  302  LEU PHE ASP ARG ILE TYR THR HIS GLN SER ASP VAL TRP          
SEQRES  18 B  302  SER PHE GLY VAL LEU LEU TRP GLU ILE PHE THR LEU GLY          
SEQRES  19 B  302  GLY SER PRO TYR PRO GLY VAL PRO VAL GLU GLU LEU PHE          
SEQRES  20 B  302  LYS LEU LEU LYS GLU GLY HIS ARG MET ASP LYS PRO SER          
SEQRES  21 B  302  ASN CYS THR ASN GLU LEU TYR MET MET MET ARG ASP CYS          
SEQRES  22 B  302  TRP HIS ALA VAL PRO SER GLN ARG PRO THR PHE LYS GLN          
SEQRES  23 B  302  LEU VAL GLU ASP LEU ASP ARG ILE VAL ALA LEU THR SER          
SEQRES  24 B  302  ASN GLN GLU                                                  
HET    C4F  A   1      18                                                       
HET    C4F  B   2      18                                                       
HETNAM     C4F 3-(3-METHOXYBENZYL)-1H-PYRROLO[2,3-B]PYRIDINE                    
FORMUL   3  C4F    2(C15 H14 N2 O)                                              
FORMUL   5  HOH   *356(H2 O)                                                    
HELIX    1   1 PRO A  474  ASP A  476  5                                   3    
HELIX    2   2 GLY A  485  ALA A  488  5                                   4    
HELIX    3   3 THR A  521  GLY A  539  1                                  19    
HELIX    4   4 ASN A  568  ARG A  576  1                                   9    
HELIX    5   5 SER A  596  LYS A  617  1                                  22    
HELIX    6   6 ALA A  625  ARG A  627  5                                   3    
HELIX    7   7 ASP A  647  ILE A  651  5                                   5    
HELIX    8   8 LEU A  662  MET A  667  5                                   6    
HELIX    9   9 ALA A  668  ARG A  675  1                                   8    
HELIX   10  10 THR A  678  THR A  695  1                                  18    
HELIX   11  11 PRO A  705  GLU A  715  1                                  11    
HELIX   12  12 THR A  726  TRP A  737  1                                  12    
HELIX   13  13 VAL A  740  ARG A  744  5                                   5    
HELIX   14  14 THR A  746  THR A  761  1                                  16    
HELIX   15  15 PRO B  474  ASP B  476  5                                   3    
HELIX   16  16 GLY B  485  ALA B  488  5                                   4    
HELIX   17  17 THR B  521  GLY B  539  1                                  19    
HELIX   18  18 ASN B  568  ALA B  575  1                                   8    
HELIX   19  19 SER B  596  LYS B  617  1                                  22    
HELIX   20  20 ALA B  625  ARG B  627  5                                   3    
HELIX   21  21 LEU B  662  MET B  667  5                                   6    
HELIX   22  22 ALA B  668  ASP B  674  1                                   7    
HELIX   23  23 THR B  678  THR B  695  1                                  18    
HELIX   24  24 PRO B  705  GLU B  715  1                                  11    
HELIX   25  25 THR B  726  TRP B  737  1                                  12    
HELIX   26  26 VAL B  740  ARG B  744  5                                   5    
HELIX   27  27 THR B  746  LEU B  760  1                                  15    
SHEET    1   A 5 LEU A 478  PRO A 483  0                                        
SHEET    2   A 5 VAL A 492  ILE A 498 -1  O  GLU A 496   N  VAL A 479           
SHEET    3   A 5 VAL A 508  LYS A 514 -1  O  VAL A 513   N  VAL A 493           
SHEET    4   A 5 TYR A 558  GLU A 562 -1  O  VAL A 561   N  ALA A 512           
SHEET    5   A 5 LEU A 547  CYS A 551 -1  N  LEU A 548   O  ILE A 560           
SHEET    1   B 2 VAL A 629  VAL A 631  0                                        
SHEET    2   B 2 MET A 637  ILE A 639 -1  O  LYS A 638   N  LEU A 630           
SHEET    1   C 5 LEU B 478  PRO B 483  0                                        
SHEET    2   C 5 GLN B 491  ILE B 498 -1  O  LEU B 494   N  LYS B 482           
SHEET    3   C 5 VAL B 508  MET B 515 -1  O  VAL B 511   N  ALA B 495           
SHEET    4   C 5 TYR B 558  GLU B 562 -1  O  VAL B 561   N  ALA B 512           
SHEET    5   C 5 LEU B 547  CYS B 551 -1  N  LEU B 548   O  ILE B 560           
SHEET    1   D 2 VAL B 629  VAL B 631  0                                        
SHEET    2   D 2 MET B 637  ILE B 639 -1  O  LYS B 638   N  LEU B 630           
SITE     1 AC1  7 PHE A 489  ALA A 512  GLU A 562  ALA A 564                    
SITE     2 AC1  7 LEU A 630  ALA A 640  ASP A 641                               
SITE     1 AC2 10 PHE B 489  ALA B 512  MET B 535  GLU B 562                    
SITE     2 AC2 10 TYR B 563  ALA B 564  LEU B 630  ALA B 640                    
SITE     3 AC2 10 ASP B 641  PHE B 642                                          
CRYST1  208.190   57.623   65.368  90.00 107.62  90.00 C 1 2 1       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      0.004803  0.000000  0.001525        0.00000                         
SCALE2      0.000000  0.017354  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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