GenomeNet

Database: PDB
Entry: 6C19
LinkDB: 6C19
Original site: 6C19 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-JAN-18   6C19              
TITLE     FGFR1 KINASE COMPLEX WITH INHIBITOR SN36985                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 1;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FGFR-1,BASIC FIBROBLAST GROWTH FACTOR RECEPTOR 1,BFGF-R-1,  
COMPND   5 FMS-LIKE TYROSINE KINASE 2,FLT-2,N-SAM,PROTO-ONCOGENE C-FGR;         
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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, BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR;                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YOSAATMADJA,J.B.SMAILL,C.J.SQUIRE                                   
REVDAT   1   16-JAN-19 6C19    0                                                
JRNL        AUTH   Y.YOSAATMADJA,C.J.SQUIRE,A.V.PATTERSON,J.B.SMAILL            
JRNL        TITL   UNDERSTANDING THE STRUCTURAL REQUIREMENTS FOR COVALENT       
JRNL        TITL 2 INHIBITION OF FGFR1-3                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34238                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1742                            
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) : 2.12                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2532                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 116                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4132                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.15000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.28000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.183         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.230        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4351 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4101 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5917 ; 1.588 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9420 ; 0.853 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   540 ; 6.217 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   175 ;34.989 ;24.343       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   720 ;13.636 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.704 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   666 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4854 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   904 ; 0.001 ; 0.020       
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):  2178 ; 1.295 ; 2.075       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2177 ; 1.295 ; 2.074       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2712 ; 2.156 ; 3.093       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2713 ; 2.156 ; 3.094       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2173 ; 1.547 ; 2.243       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2170 ; 1.530 ; 2.236       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3200 ; 2.467 ; 3.291       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4970 ; 4.099 ;16.829       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4947 ; 4.088 ;16.780       
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   464        A   765                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4218  -7.1624   3.2578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0342 T22:   0.0115                                     
REMARK   3      T33:   0.0400 T12:  -0.0143                                     
REMARK   3      T13:   0.0194 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9839 L22:   0.9117                                     
REMARK   3      L33:   3.6533 L12:  -0.2295                                     
REMARK   3      L13:   0.7811 L23:  -0.7518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:  -0.0920 S13:  -0.0630                       
REMARK   3      S21:   0.0410 S22:  -0.0081 S23:   0.0822                       
REMARK   3      S31:   0.2349 S32:  -0.0816 S33:  -0.0256                       
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 :   B   464        B   762                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5895  16.5201  22.3152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0582 T22:   0.0493                                     
REMARK   3      T33:   0.0943 T12:   0.0021                                     
REMARK   3      T13:   0.0198 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3907 L22:   1.0640                                     
REMARK   3      L33:   3.3765 L12:  -0.3246                                     
REMARK   3      L13:   1.7316 L23:  -0.4561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:   0.0680 S13:   0.1373                       
REMARK   3      S21:   0.1250 S22:  -0.0967 S23:   0.0556                       
REMARK   3      S31:  -0.0134 S32:  -0.0403 S33:   0.0243                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6C19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231926.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21315                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.710                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4WUN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% MPEG 5000, 0.1 M SODIUM CACODYLATE   
REMARK 280  PH 7.5, 0.2 M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
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      104.21300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.50650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      104.21300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.50650            
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                                                    
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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     MET A   457                                                      
REMARK 465     SER A   458                                                      
REMARK 465     GLY A   459                                                      
REMARK 465     VAL A   460                                                      
REMARK 465     SER A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     TYR A   463                                                      
REMARK 465     GLY A   487                                                      
REMARK 465     ALA A   488                                                      
REMARK 465     PHE A   489                                                      
REMARK 465     GLY A   490                                                      
REMARK 465     GLY A   580                                                      
REMARK 465     LEU A   581                                                      
REMARK 465     HIS A   589                                                      
REMARK 465     ASN A   590                                                      
REMARK 465     PRO A   591                                                      
REMARK 465     ALA A   645                                                      
REMARK 465     ARG A   646                                                      
REMARK 465     ASP A   647                                                      
REMARK 465     ILE A   648                                                      
REMARK 465     HIS A   649                                                      
REMARK 465     HIS A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     ASP A   652                                                      
REMARK 465     TYR A   653                                                      
REMARK 465     TYR A   654                                                      
REMARK 465     LYS A   655                                                      
REMARK 465     LYS A   656                                                      
REMARK 465     THR A   657                                                      
REMARK 465     THR A   658                                                      
REMARK 465     ASN A   659                                                      
REMARK 465     GLY A   660                                                      
REMARK 465     ARG A   661                                                      
REMARK 465     GLY B   455                                                      
REMARK 465     ALA B   456                                                      
REMARK 465     MET B   457                                                      
REMARK 465     SER B   458                                                      
REMARK 465     GLY B   459                                                      
REMARK 465     VAL B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     GLU B   462                                                      
REMARK 465     TYR B   463                                                      
REMARK 465     GLY B   487                                                      
REMARK 465     ALA B   488                                                      
REMARK 465     PHE B   489                                                      
REMARK 465     PRO B   578                                                      
REMARK 465     PRO B   579                                                      
REMARK 465     GLY B   580                                                      
REMARK 465     LEU B   581                                                      
REMARK 465     GLU B   582                                                      
REMARK 465     TYR B   583                                                      
REMARK 465     SER 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 465     GLU B   592                                                      
REMARK 465     ALA B   645                                                      
REMARK 465     ARG B   646                                                      
REMARK 465     ASP B   647                                                      
REMARK 465     ILE B   648                                                      
REMARK 465     HIS B   649                                                      
REMARK 465     HIS B   650                                                      
REMARK 465     ILE B   651                                                      
REMARK 465     ASP B   652                                                      
REMARK 465     TYR B   653                                                      
REMARK 465     TYR B   654                                                      
REMARK 465     LYS B   655                                                      
REMARK 465     LYS B   656                                                      
REMARK 465     THR B   657                                                      
REMARK 465     THR B   658                                                      
REMARK 465     ASN B   659                                                      
REMARK 465     GLY B   660                                                      
REMARK 465     ARG B   661                                                      
REMARK 465     ASN B   763                                                      
REMARK 465     GLN B   764                                                      
REMARK 465     GLU B   765                                                      
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     GLU A 464    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 465    CG   CD1  CD2                                       
REMARK 470     GLU A 467    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 486    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 502    CG   CD   CE   NZ                                   
REMARK 470     LYS A 504    CG   CD   CE   NZ                                   
REMARK 470     ARG A 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 516    CG   CD1  CD2                                       
REMARK 470     LYS A 517    CG   CD   CE   NZ                                   
REMARK 470     SER A 518    OG                                                  
REMARK 470     GLU A 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 523    CE   NZ                                             
REMARK 470     ASP A 554    CG   OD1  OD2                                       
REMARK 470     GLU A 582    CG   CD   OE1  OE2                                  
REMARK 470     SER A 588    OG                                                  
REMARK 470     ARG A 627    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 644    CG   CD1  CD2                                       
REMARK 470     LEU A 662    CG   CD1  CD2                                       
REMARK 470     PHE A 673    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 675    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 711    CG   CD   CE   NZ                                   
REMARK 470     LYS A 714    CG   CD   CE   NZ                                   
REMARK 470     ASN A 763    CG   OD1  ND2                                       
REMARK 470     GLU A 765    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 464    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 465    CG   CD1  CD2                                       
REMARK 470     LYS B 482    CG   CD   CE   NZ                                   
REMARK 470     GLU B 486    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 502    CG   CD   CE   NZ                                   
REMARK 470     ASP B 503    CG   OD1  OD2                                       
REMARK 470     LYS B 504    CG   CD   CE   NZ                                   
REMARK 470     ARG B 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 517    CG   CD   CE   NZ                                   
REMARK 470     SER B 518    OG                                                  
REMARK 470     GLU B 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 523    CE   NZ                                             
REMARK 470     LYS B 540    CG   CD   CE   NZ                                   
REMARK 470     GLU B 593    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 594    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 618    CG   CD   CE   NZ                                   
REMARK 470     LEU B 662    CG   CD1  CD2                                       
REMARK 470     PHE B 673    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 675    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 710    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 711    CG   CD   CE   NZ                                   
REMARK 470     LYS B 714    CG   CD   CE   NZ                                   
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    MET A 534   CG  -  SD  -  CE  ANGL. DEV. = -10.6 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    LYS A 504       61.95   -119.49                                   
REMARK 500    SER A 584       86.47   -158.14                                   
REMARK 500    ARG A 622      -20.41     81.64                                   
REMARK 500    ASN A 724       42.42   -106.08                                   
REMARK 500    GLN B 594      127.08    -38.93                                   
REMARK 500    ARG B 622      -16.16     73.43                                   
REMARK 500    ASP B 623       44.81   -142.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     YY7 B  801                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YY7 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YY7 B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6C18   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH RELATED LIGAND                                     
DBREF  6C19 A  459   765  UNP    P11362   FGFR1_HUMAN    457    763             
DBREF  6C19 B  459   765  UNP    P11362   FGFR1_HUMAN    457    763             
SEQADV 6C19 GLY A  455  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 ALA A  456  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 MET A  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 SER A  458  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 ALA A  488  UNP  P11362    CYS   486 CONFLICT                       
SEQADV 6C19 SER A  584  UNP  P11362    CYS   582 CONFLICT                       
SEQADV 6C19 GLY B  455  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 ALA B  456  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 MET B  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 SER B  458  UNP  P11362              EXPRESSION TAG                 
SEQADV 6C19 ALA B  488  UNP  P11362    CYS   486 CONFLICT                       
SEQADV 6C19 SER B  584  UNP  P11362    CYS   582 CONFLICT                       
SEQRES   1 A  311  GLY ALA MET SER GLY VAL SER GLU TYR GLU LEU PRO GLU          
SEQRES   2 A  311  ASP PRO ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU          
SEQRES   3 A  311  GLY LYS PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL          
SEQRES   4 A  311  LEU ALA GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN          
SEQRES   5 A  311  ARG VAL THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP          
SEQRES   6 A  311  ALA THR GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET          
SEQRES   7 A  311  GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE          
SEQRES   8 A  311  ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR          
SEQRES   9 A  311  VAL ILE VAL GLU TYR ALA SER LYS GLY ASN LEU ARG GLU          
SEQRES  10 A  311  TYR LEU GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER          
SEQRES  11 A  311  TYR ASN PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER          
SEQRES  12 A  311  LYS ASP LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY          
SEQRES  13 A  311  MET GLU TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP          
SEQRES  14 A  311  LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL          
SEQRES  15 A  311  MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS          
SEQRES  16 A  311  HIS ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU          
SEQRES  17 A  311  PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG          
SEQRES  18 A  311  ILE TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  19 A  311  LEU LEU TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR          
SEQRES  20 A  311  PRO GLY VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS          
SEQRES  21 A  311  GLU GLY HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN          
SEQRES  22 A  311  GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL          
SEQRES  23 A  311  PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP          
SEQRES  24 A  311  LEU ASP ARG ILE VAL ALA LEU THR SER ASN GLN GLU              
SEQRES   1 B  311  GLY ALA MET SER GLY VAL SER GLU TYR GLU LEU PRO GLU          
SEQRES   2 B  311  ASP PRO ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU          
SEQRES   3 B  311  GLY LYS PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL          
SEQRES   4 B  311  LEU ALA GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN          
SEQRES   5 B  311  ARG VAL THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP          
SEQRES   6 B  311  ALA THR GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET          
SEQRES   7 B  311  GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE          
SEQRES   8 B  311  ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR          
SEQRES   9 B  311  VAL ILE VAL GLU TYR ALA SER LYS GLY ASN LEU ARG GLU          
SEQRES  10 B  311  TYR LEU GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER          
SEQRES  11 B  311  TYR ASN PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER          
SEQRES  12 B  311  LYS ASP LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY          
SEQRES  13 B  311  MET GLU TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP          
SEQRES  14 B  311  LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL          
SEQRES  15 B  311  MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS          
SEQRES  16 B  311  HIS ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU          
SEQRES  17 B  311  PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG          
SEQRES  18 B  311  ILE TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  19 B  311  LEU LEU TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR          
SEQRES  20 B  311  PRO GLY VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS          
SEQRES  21 B  311  GLU GLY HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN          
SEQRES  22 B  311  GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL          
SEQRES  23 B  311  PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP          
SEQRES  24 B  311  LEU ASP ARG ILE VAL ALA LEU THR SER ASN GLN GLU              
HET    YY7  A 801      38                                                       
HET    SO4  A 802       5                                                       
HET    YY7  B 801      35                                                       
HETNAM     YY7 3-(2,6-DICHLORO-3,5-DIMETHOXYPHENYL)-1-{(3S)-1-[(2E)-4-          
HETNAM   2 YY7  (DIMETHYLAMINO)BUT-2-ENOYL]PYRROLIDIN-3-YL}-7-                  
HETNAM   3 YY7  (METHYLAMINO)-3,4-DIHYDROPYRIMIDO[4,5-D]PYRIMIDIN-              
HETNAM   4 YY7  2(1H)-ONE                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  YY7    2(C25 H31 CL2 N7 O4)                                         
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *88(H2 O)                                                     
HELIX    1 AA1 PRO A  474  ASP A  476  5                                   3    
HELIX    2 AA2 THR A  521  GLY A  539  1                                  19    
HELIX    3 AA3 ASN A  568  ALA A  575  1                                   8    
HELIX    4 AA4 SER A  596  LYS A  617  1                                  22    
HELIX    5 AA5 ALA A  625  ARG A  627  5                                   3    
HELIX    6 AA6 LEU A  662  MET A  667  5                                   6    
HELIX    7 AA7 ALA A  668  ARG A  675  1                                   8    
HELIX    8 AA8 THR A  678  THR A  695  1                                  18    
HELIX    9 AA9 PRO A  705  GLU A  707  5                                   3    
HELIX   10 AB1 GLU A  708  GLU A  715  1                                   8    
HELIX   11 AB2 THR A  726  TRP A  737  1                                  12    
HELIX   12 AB3 VAL A  740  ARG A  744  5                                   5    
HELIX   13 AB4 THR A  746  THR A  761  1                                  16    
HELIX   14 AB5 PRO B  474  ASP B  476  5                                   3    
HELIX   15 AB6 THR B  521  GLY B  539  1                                  19    
HELIX   16 AB7 ASN B  568  ALA B  575  1                                   8    
HELIX   17 AB8 SER B  596  LYS B  617  1                                  22    
HELIX   18 AB9 ALA B  625  ARG B  627  5                                   3    
HELIX   19 AC1 LEU B  662  MET B  667  5                                   6    
HELIX   20 AC2 ALA B  668  ARG B  675  1                                   8    
HELIX   21 AC3 THR B  678  THR B  695  1                                  18    
HELIX   22 AC4 PRO B  705  GLU B  715  1                                  11    
HELIX   23 AC5 THR B  726  TRP B  737  1                                  12    
HELIX   24 AC6 VAL B  740  ARG B  744  5                                   5    
HELIX   25 AC7 THR B  746  THR B  761  1                                  16    
SHEET    1 AA1 5 LEU A 478  GLY A 485  0                                        
SHEET    2 AA1 5 VAL A 492  ILE A 498 -1  O  LEU A 494   N  LYS A 482           
SHEET    3 AA1 5 VAL A 508  LYS A 514 -1  O  THR A 509   N  ALA A 497           
SHEET    4 AA1 5 TYR A 558  GLU A 562 -1  O  VAL A 561   N  ALA A 512           
SHEET    5 AA1 5 LEU A 547  CYS A 551 -1  N  LEU A 548   O  ILE A 560           
SHEET    1 AA2 2 VAL A 629  VAL A 631  0                                        
SHEET    2 AA2 2 MET A 637  ILE A 639 -1  O  LYS A 638   N  LEU A 630           
SHEET    1 AA3 5 LEU B 478  GLY B 485  0                                        
SHEET    2 AA3 5 GLN B 491  ILE B 498 -1  O  LEU B 494   N  GLY B 481           
SHEET    3 AA3 5 VAL B 508  MET B 515 -1  O  VAL B 511   N  ALA B 495           
SHEET    4 AA3 5 TYR B 558  GLU B 562 -1  O  VAL B 561   N  ALA B 512           
SHEET    5 AA3 5 LEU B 547  CYS B 551 -1  N  LEU B 548   O  ILE B 560           
SHEET    1 AA4 2 VAL B 629  VAL B 631  0                                        
SHEET    2 AA4 2 MET B 637  ILE B 639 -1  O  LYS B 638   N  LEU B 630           
SITE     1 AC1 15 LEU A 484  VAL A 492  ALA A 512  LYS A 514                    
SITE     2 AC1 15 GLU A 531  MET A 535  VAL A 559  VAL A 561                    
SITE     3 AC1 15 GLU A 562  ALA A 564  ASN A 568  GLU A 571                    
SITE     4 AC1 15 LEU A 630  ALA A 640  ASP A 641                               
SITE     1 AC2  3 GLY A 539  LYS A 540  LYS A 618                               
SITE     1 AC3 15 LEU B 484  VAL B 492  ALA B 512  LYS B 514                    
SITE     2 AC3 15 GLU B 531  VAL B 559  VAL B 561  GLU B 562                    
SITE     3 AC3 15 TYR B 563  ALA B 564  ASN B 568  GLU B 571                    
SITE     4 AC3 15 LEU B 630  ALA B 640  ASP B 641                               
CRYST1  208.426   49.013   64.628  90.00 105.97  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      0.004798  0.000000  0.001373        0.00000                         
SCALE2      0.000000  0.020403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016094        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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