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Database: PDB
Entry: 6P69
LinkDB: 6P69
Original site: 6P69 
HEADER    TRANSFERASE                             03-JUN-19   6P69              
TITLE     CRYSTAL STRUCTURE OF FGFR1-Y563C (FGFR4 SURROGATE) COVALENTLY BOUND TO
TITLE    2 COMPOUND 11.                                                         
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                                         
KEYWDS    FGFR, INHIBITOR COMPLEX, COVALENT INHIBITOR, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.A.LARSEN                                                            
REVDAT   1   19-JUN-19 6P69    0                                                
JRNL        AUTH   S.PRAJAPATI                                                  
JRNL        TITL   TO BE PUBLISHED                                              
JRNL        REF    TBD                                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36264                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1950                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2651                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4562                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 115                                     
REMARK   3   SOLVENT ATOMS            : 248                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.227         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.693         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4785 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4534 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6463 ; 1.854 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10524 ; 1.242 ; 3.009       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   574 ; 6.939 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   206 ;38.515 ;24.078       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   855 ;16.193 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;15.534 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   702 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5177 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   927 ; 0.002 ; 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):  2296 ; 2.942 ; 3.188       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2295 ; 2.938 ; 3.187       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2861 ; 4.570 ; 4.759       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2862 ; 4.569 ; 4.760       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2489 ; 3.669 ; 3.656       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2490 ; 3.668 ; 3.656       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3600 ; 5.678 ; 5.314       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5391 ; 7.632 ;36.853       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5392 ; 7.636 ;36.861       
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 : NULL                                                 
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 6P69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241957.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3RHX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MIX OF PROTEIN + RESERVOIR PROTEIN   
REMARK 280  AT ~15 MG/ML FORMULATED IN: 20MM TRIS PH 8, 20MM NACL, 2MM TCEP     
REMARK 280  RESERVOIR: 14-18% PEG 10K 0.3 M (NH4)2SO4 0.1 M MES PH 6.5 5%       
REMARK 280  ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING 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      102.68250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.25800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      102.68250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.25800            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 990  LIES ON A SPECIAL POSITION.                          
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   457                                                      
REMARK 465     ALA A   458                                                      
REMARK 465     GLY A   459                                                      
REMARK 465     VAL A   460                                                      
REMARK 465     SER A   461                                                      
REMARK 465     ASP A   501                                                      
REMARK 465     LYS A   502                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     LYS A   504                                                      
REMARK 465     GLY A   580                                                      
REMARK 465     LEU A   581                                                      
REMARK 465     GLU A   582                                                      
REMARK 465     TYR A   583                                                      
REMARK 465     SER 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   457                                                      
REMARK 465     ALA B   458                                                      
REMARK 465     GLY B   459                                                      
REMARK 465     VAL B   460                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     LYS B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     LYS B   504                                                      
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     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     ARG A 675    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 592    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 675    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 603   CB    CYS A 603   SG     -0.550                       
REMARK 500    CYS B 603   CB    CYS B 603   SG     -0.203                       
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    ARG A 470   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    MET A 534   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    CYS A 603   CA  -  CB  -  SG  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ASP A 682   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 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 593      120.84    119.13                                   
REMARK 500    ARG A 622      -13.30     79.25                                   
REMARK 500    ASP A 623       53.99   -141.97                                   
REMARK 500    HIS A 649      100.26    -55.18                                   
REMARK 500    HIS A 650       69.82   -113.93                                   
REMARK 500    PHE B 489       42.07   -100.19                                   
REMARK 500    ARG B 622      -25.42     79.15                                   
REMARK 500    ARG B 675       10.19     48.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A  648     HIS A  649                 -134.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue O21 A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide O21 B 804 and CYS B    
REMARK 800  563                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6P68   RELATED DB: PDB                                   
DBREF  6P69 A  458   765  UNP    P11362   FGFR1_HUMAN    458    765             
DBREF  6P69 B  458   765  UNP    P11362   FGFR1_HUMAN    458    765             
SEQADV 6P69 GLY A  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6P69 ALA A  488  UNP  P11362    CYS   488 ENGINEERED MUTATION            
SEQADV 6P69 CYS A  563  UNP  P11362    TYR   563 ENGINEERED MUTATION            
SEQADV 6P69 SER A  584  UNP  P11362    CYS   584 CONFLICT                       
SEQADV 6P69 GLY B  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6P69 ALA B  488  UNP  P11362    CYS   488 ENGINEERED MUTATION            
SEQADV 6P69 CYS B  563  UNP  P11362    TYR   563 ENGINEERED MUTATION            
SEQADV 6P69 SER B  584  UNP  P11362    CYS   584 CONFLICT                       
SEQRES   1 A  309  GLY ALA GLY VAL SER GLU TYR GLU LEU PRO GLU ASP PRO          
SEQRES   2 A  309  ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU GLY LYS          
SEQRES   3 A  309  PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL LEU ALA          
SEQRES   4 A  309  GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN ARG VAL          
SEQRES   5 A  309  THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP ALA THR          
SEQRES   6 A  309  GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET GLU MET          
SEQRES   7 A  309  MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE ASN LEU          
SEQRES   8 A  309  LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR VAL ILE          
SEQRES   9 A  309  VAL GLU CYS ALA SER LYS GLY ASN LEU ARG GLU TYR LEU          
SEQRES  10 A  309  GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER TYR ASN          
SEQRES  11 A  309  PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER LYS ASP          
SEQRES  12 A  309  LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY MET GLU          
SEQRES  13 A  309  TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP LEU ALA          
SEQRES  14 A  309  ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL MET LYS          
SEQRES  15 A  309  ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS HIS ILE          
SEQRES  16 A  309  ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU PRO VAL          
SEQRES  17 A  309  LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG ILE TYR          
SEQRES  18 A  309  THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL LEU LEU          
SEQRES  19 A  309  TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR PRO GLY          
SEQRES  20 A  309  VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS GLU GLY          
SEQRES  21 A  309  HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN GLU LEU          
SEQRES  22 A  309  TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL PRO SER          
SEQRES  23 A  309  GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP LEU ASP          
SEQRES  24 A  309  ARG ILE VAL ALA LEU THR SER ASN GLN GLU                      
SEQRES   1 B  309  GLY ALA GLY VAL SER GLU TYR GLU LEU PRO GLU ASP PRO          
SEQRES   2 B  309  ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU GLY LYS          
SEQRES   3 B  309  PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL LEU ALA          
SEQRES   4 B  309  GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN ARG VAL          
SEQRES   5 B  309  THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP ALA THR          
SEQRES   6 B  309  GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET GLU MET          
SEQRES   7 B  309  MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE ASN LEU          
SEQRES   8 B  309  LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR VAL ILE          
SEQRES   9 B  309  VAL GLU CYS ALA SER LYS GLY ASN LEU ARG GLU TYR LEU          
SEQRES  10 B  309  GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER TYR ASN          
SEQRES  11 B  309  PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER LYS ASP          
SEQRES  12 B  309  LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY MET GLU          
SEQRES  13 B  309  TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP LEU ALA          
SEQRES  14 B  309  ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL MET LYS          
SEQRES  15 B  309  ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS HIS ILE          
SEQRES  16 B  309  ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU PRO VAL          
SEQRES  17 B  309  LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG ILE TYR          
SEQRES  18 B  309  THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL LEU LEU          
SEQRES  19 B  309  TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR PRO GLY          
SEQRES  20 B  309  VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS GLU GLY          
SEQRES  21 B  309  HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN GLU LEU          
SEQRES  22 B  309  TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL PRO SER          
SEQRES  23 B  309  GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP LEU ASP          
SEQRES  24 B  309  ARG ILE VAL ALA LEU THR SER ASN GLN GLU                      
HET    SO4  A 801       5                                                       
HET    EDO  A 802       4                                                       
HET    EDO  A 803       4                                                       
HET    O21  A 804      44                                                       
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HET    EDO  B 803       4                                                       
HET    O21  B 804      44                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     O21 N-{2-[(6-{[(2,6-DICHLORO-3,5-DIMETHOXYPHENYL)                    
HETNAM   2 O21  CARBAMOYL][3-(4-METHYLPIPERAZIN-1-YL)                           
HETNAM   3 O21  PROPYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENYL}PROP-2-                
HETNAM   4 O21  ENAMIDE                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   6  O21    2(C30 H36 CL2 N8 O4)                                         
FORMUL  11  HOH   *248(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  715  1                                  11    
HELIX   10 AB1 THR A  726  TRP A  737  1                                  12    
HELIX   11 AB2 VAL A  740  ARG A  744  5                                   5    
HELIX   12 AB3 THR A  746  THR A  761  1                                  16    
HELIX   13 AB4 PRO B  474  ASP B  476  5                                   3    
HELIX   14 AB5 THR B  521  GLY B  539  1                                  19    
HELIX   15 AB6 ASN B  568  ARG B  576  1                                   9    
HELIX   16 AB7 SER B  596  LYS B  617  1                                  22    
HELIX   17 AB8 ALA B  625  ARG B  627  5                                   3    
HELIX   18 AB9 LEU B  662  MET B  667  5                                   6    
HELIX   19 AC1 ALA B  668  ASP B  674  1                                   7    
HELIX   20 AC2 THR B  678  THR B  695  1                                  18    
HELIX   21 AC3 PRO B  705  GLU B  715  1                                  11    
HELIX   22 AC4 THR B  726  TRP B  737  1                                  12    
HELIX   23 AC5 VAL B  740  ARG B  744  5                                   5    
HELIX   24 AC6 THR B  746  LEU B  760  1                                  15    
SHEET    1 AA1 5 LEU A 478  GLU A 486  0                                        
SHEET    2 AA1 5 GLY A 490  ILE A 498 -1  O  GLU A 496   N  VAL A 479           
SHEET    3 AA1 5 VAL A 508  LEU A 516 -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  GLU B 486  0                                        
SHEET    2 AA3 5 GLY B 490  ILE B 498 -1  O  VAL B 492   N  LEU B 484           
SHEET    3 AA3 5 VAL B 508  LEU B 516 -1  O  THR B 509   N  ALA B 497           
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  GLY B 549   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           
LINK         SG  CYS A 563                 C28 O21 A 804     1555   1555  1.61  
LINK         SG  CYS B 563                 C28 O21 B 804     1555   1555  1.62  
CISPEP   1 ALA B  488    PHE B  489          0       -20.06                     
SITE     1 AC1  6 ARG A 570  ARG A 627  THR A 657  ASN A 659                    
SITE     2 AC1  6 ARG A 661  HOH A 948                                          
SITE     1 AC2  5 ALA A 615  THR A 746  PHE A 747  LYS A 748                    
SITE     2 AC2  5 HOH A 902                                                     
SITE     1 AC3  6 TRP A 684  TYR A 701  ARG A 718  MET A 719                    
SITE     2 AC3  6 TRP A 737  HOH A 919                                          
SITE     1 AC4 16 LEU A 484  GLU A 486  GLY A 487  VAL A 492                    
SITE     2 AC4 16 LEU A 494  ALA A 512  LYS A 514  GLU A 531                    
SITE     3 AC4 16 VAL A 559  VAL A 561  GLU A 562  CYS A 563                    
SITE     4 AC4 16 ALA A 564  LEU A 630  ALA A 640  ASP A 641                    
SITE     1 AC5  6 ARG B 570  ARG B 627  THR B 657  ASN B 659                    
SITE     2 AC5  6 ARG B 661  HOH B 926                                          
SITE     1 AC6  4 GLN B 574  ASN B 659  ARG B 661  SER B 699                    
SITE     1 AC7  7 TRP B 684  TYR B 701  LEU B 713  ARG B 718                    
SITE     2 AC7  7 MET B 719  TRP B 737  HOH B 919                               
SITE     1 AC8 21 LEU B 484  VAL B 492  LEU B 494  LYS B 510                    
SITE     2 AC8 21 LYS B 514  GLU B 531  MET B 535  VAL B 559                    
SITE     3 AC8 21 VAL B 561  GLU B 562  ALA B 564  SER B 565                    
SITE     4 AC8 21 LEU B 630  ALA B 640  ASP B 641  PHE B 642                    
SITE     5 AC8 21 HOH B 909  HOH B 933  HOH B 952  HOH B 953                    
SITE     6 AC8 21 HOH B1000                                                     
CRYST1  205.365   58.516   66.131  90.00 107.31  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      0.004869  0.000000  0.001517        0.00000                         
SCALE2      0.000000  0.017089  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015839        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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