GenomeNet

Database: PDB
Entry: 5EDQ
LinkDB: 5EDQ
Original site: 5EDQ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       21-OCT-15   5EDQ              
TITLE     EGFR KINASE (T790M/L858R) WITH INHIBITOR COMPOUND 15: ~{N}-(7-        
TITLE    2 CHLORANYL-1~{H}-INDAZOL-3-YL)-7,7-DIMETHYL-2-(1~{H}-PYRAZOL-4-YL)-   
TITLE    3 5~{H}-FURO[3,4-D]PYRIMIDIN-4-AMINE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE    
COMPND   5 ERBB-1;                                                              
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: EGFR, ERBB, ERBB1, HER1;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROTEIN KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,C.YU                                                      
REVDAT   3   20-JAN-16 5EDQ    1       JRNL                                     
REVDAT   2   23-DEC-15 5EDQ    1       JRNL                                     
REVDAT   1   02-DEC-15 5EDQ    0                                                
JRNL        AUTH   E.J.HANAN,M.BAUMGARDNER,M.C.BRYAN,Y.CHEN,C.EIGENBROT,P.FAN,  
JRNL        AUTH 2 X.H.GU,H.LA,S.MALEK,H.E.PURKEY,G.SCHAEFER,S.SCHMIDT,         
JRNL        AUTH 3 S.SIDERIS,I.YEN,C.YU,T.P.HEFFRON                             
JRNL        TITL   4-AMINOINDAZOLYL-DIHYDROFURO[3,4-D]PYRIMIDINES AS            
JRNL        TITL 2 NON-COVALENT INHIBITORS OF MUTANT EPIDERMAL GROWTH FACTOR    
JRNL        TITL 3 RECEPTOR TYROSINE KINASE.                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  26   534 2016              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   26639762                                                     
JRNL        DOI    10.1016/J.BMCL.2015.11.078                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 13695                          
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)  : 0.209                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.242                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.260                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 584                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 7                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.02                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2793                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2534                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2687                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2523                   
REMARK   3   BIN FREE R VALUE                        : 0.2828                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.80                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 106                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2393                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.460               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.423               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.275               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.450               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.283               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2476   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3357   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 869    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 58     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 347    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2476   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 320    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2814   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.46                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.14                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|697 - A|786 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -53.6615    6.8112  -33.0769           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0374 T22:   -0.0600                                    
REMARK   3     T33:   -0.0075 T12:   -0.1520                                    
REMARK   3     T13:    0.0766 T23:    0.0493                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3619 L22:    0.0000                                    
REMARK   3     L33:    6.5921 L12:    0.0769                                    
REMARK   3     L13:    0.5172 L23:   -0.3645                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0385 S12:   -0.0138 S13:    0.1019                     
REMARK   3     S21:   -0.0854 S22:    0.0347 S23:   -0.1847                     
REMARK   3     S31:   -0.0540 S32:    0.5442 S33:   -0.0732                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|787 - A|987 A|1101 - A|1101 }                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -62.0818  -15.7006  -23.1304           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0945 T22:   -0.0824                                    
REMARK   3     T33:   -0.1689 T12:   -0.0625                                    
REMARK   3     T13:    0.0887 T23:    0.0930                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0259 L22:    5.4407                                    
REMARK   3     L33:    2.8317 L12:    2.3618                                    
REMARK   3     L13:   -1.3961 L23:   -2.1445                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1740 S12:   -0.1310 S13:   -0.1989                     
REMARK   3     S21:   -0.4103 S22:   -0.0713 S23:   -0.4378                     
REMARK   3     S31:    0.2587 S32:    0.3158 S33:    0.2453                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|988 - A|1018 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -65.8635   10.0006  -17.7954           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0264 T22:   -0.0606                                    
REMARK   3     T33:    0.0521 T12:   -0.1520                                    
REMARK   3     T13:    0.0689 T23:   -0.0520                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1301 L22:    3.4376                                    
REMARK   3     L33:    1.3119 L12:   -2.0239                                    
REMARK   3     L13:   -1.0372 L23:    2.9104                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0012 S12:   -0.0461 S13:   -0.0275                     
REMARK   3     S21:    0.1826 S22:   -0.0245 S23:    0.0480                     
REMARK   3     S31:   -0.0154 S32:   -0.0607 S33:    0.0233                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5EDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214745.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08B1-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13707                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10K, ETHYLENE GLYCOL, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       74.45950            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       74.45950            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       74.45950            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       74.45950            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       74.45950            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       74.45950            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 15440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   694                                                      
REMARK 465     SER A   695                                                      
REMARK 465     GLY A   696                                                      
REMARK 465     LYS A   860                                                      
REMARK 465     LEU A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     GLY A   863                                                      
REMARK 465     ALA A   864                                                      
REMARK 465     ALA A   865                                                      
REMARK 465     ALA A   866                                                      
REMARK 465     ALA A   867                                                      
REMARK 465     GLU A   868                                                      
REMARK 465     TYR A   869                                                      
REMARK 465     HIS A   870                                                      
REMARK 465     ALA A   871                                                      
REMARK 465     GLU A   872                                                      
REMARK 465     GLY A   873                                                      
REMARK 465     GLY A   874                                                      
REMARK 465     LYS A   875                                                      
REMARK 465     TYR A   998                                                      
REMARK 465     ARG A   999                                                      
REMARK 465     ALA A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     MET A  1002                                                      
REMARK 465     ASP A  1003                                                      
REMARK 465     GLU A  1004                                                      
REMARK 465     GLU A  1005                                                      
REMARK 465     PRO A  1019                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     GLN A  1021                                                      
REMARK 465     GLY A  1022                                                      
REMARK 465     ASN A  1023                                                      
REMARK 465     SER A  1024                                                      
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 734      -80.56     13.93                                   
REMARK 500    LEU A 747       71.91    -65.77                                   
REMARK 500    ARG A 748      -89.96     48.19                                   
REMARK 500    GLU A 749      -55.97   -149.97                                   
REMARK 500    LEU A 782       54.54    -92.06                                   
REMARK 500    ARG A 836      -15.01     77.45                                   
REMARK 500    ASP A 837       47.98   -141.94                                   
REMARK 500    GLU A 985      -43.61     96.40                                   
REMARK 500    PRO A 992       83.77    -64.14                                   
REMARK 500    ASP A 994      -69.73     60.12                                   
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 5N3 A 1101                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EDP   RELATED DB: PDB                                   
DBREF  5EDQ A  695  1022  UNP    P00533   EGFR_HUMAN     695   1022             
SEQADV 5EDQ GLY A  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5EDQ MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5EDQ ARG A  858  UNP  P00533    LEU   858 ENGINEERED MUTATION            
SEQADV 5EDQ ALA A  865  UNP  P00533    GLU   865 ENGINEERED MUTATION            
SEQADV 5EDQ ALA A  866  UNP  P00533    GLU   866 ENGINEERED MUTATION            
SEQADV 5EDQ ALA A  867  UNP  P00533    LYS   867 ENGINEERED MUTATION            
SEQADV 5EDQ ASN A 1023  UNP  P00533              EXPRESSION TAG                 
SEQADV 5EDQ SER A 1024  UNP  P00533              EXPRESSION TAG                 
SEQRES   1 A  331  GLY SER GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE          
SEQRES   2 A  331  LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU GLY          
SEQRES   3 A  331  SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP ILE          
SEQRES   4 A  331  PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE LYS          
SEQRES   5 A  331  GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS GLU          
SEQRES   6 A  331  ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP ASN          
SEQRES   7 A  331  PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR SER          
SEQRES   8 A  331  THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE GLY CYS          
SEQRES   9 A  331  LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE GLY          
SEQRES  10 A  331  SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS          
SEQRES  11 A  331  GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS ARG          
SEQRES  12 A  331  ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO GLN          
SEQRES  13 A  331  HIS VAL LYS ILE THR ASP PHE GLY ARG ALA LYS LEU LEU          
SEQRES  14 A  331  GLY ALA ALA ALA ALA GLU TYR HIS ALA GLU GLY GLY LYS          
SEQRES  15 A  331  VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU HIS          
SEQRES  16 A  331  ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR GLY          
SEQRES  17 A  331  VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS PRO          
SEQRES  18 A  331  TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE LEU          
SEQRES  19 A  331  GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR          
SEQRES  20 A  331  ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP MET ILE          
SEQRES  21 A  331  ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE ILE          
SEQRES  22 A  331  GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR LEU          
SEQRES  23 A  331  VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER PRO          
SEQRES  24 A  331  THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU GLU          
SEQRES  25 A  331  ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU ILE          
SEQRES  26 A  331  PRO GLN GLN GLY ASN SER                                      
HET    5N3  A1101      27                                                       
HETNAM     5N3 ~{N}-(7-CHLORANYL-1~{H}-INDAZOL-3-YL)-7,7-DIMETHYL-2-            
HETNAM   2 5N3  (1~{H}-PYRAZOL-4-YL)-5~{H}-FURO[3,4-D]PYRIMIDIN-4-              
HETNAM   3 5N3  AMINE                                                           
FORMUL   2  5N3    C18 H16 CL N7 O                                              
HELIX    1 AA1 LYS A  708  THR A  710  5                                   3    
HELIX    2 AA2 SER A  752  SER A  768  1                                  17    
HELIX    3 AA3 CYS A  797  LYS A  806  1                                  10    
HELIX    4 AA4 ASP A  807  ILE A  809  5                                   3    
HELIX    5 AA5 GLY A  810  ARG A  831  1                                  22    
HELIX    6 AA6 ALA A  839  ARG A  841  5                                   3    
HELIX    7 AA7 PRO A  877  MET A  881  5                                   5    
HELIX    8 AA8 ALA A  882  ARG A  889  1                                   8    
HELIX    9 AA9 THR A  892  THR A  909  1                                  18    
HELIX   10 AB1 PRO A  919  SER A  921  5                                   3    
HELIX   11 AB2 GLU A  922  GLY A  930  1                                   9    
HELIX   12 AB3 THR A  940  TRP A  951  1                                  12    
HELIX   13 AB4 ASP A  954  ARG A  958  5                                   5    
HELIX   14 AB5 LYS A  960  ARG A  973  1                                  14    
HELIX   15 AB6 ASP A  974  TYR A  978  5                                   5    
SHEET    1 AA1 5 PHE A 712  SER A 720  0                                        
SHEET    2 AA1 5 THR A 725  TRP A 731 -1  O  LYS A 728   N  LYS A 716           
SHEET    3 AA1 5 ILE A 740  GLU A 746 -1  O  ILE A 740   N  TRP A 731           
SHEET    4 AA1 5 GLN A 787  GLN A 791 -1  O  MET A 790   N  ALA A 743           
SHEET    5 AA1 5 LEU A 777  CYS A 781 -1  N  GLY A 779   O  ILE A 789           
SHEET    1 AA2 2 VAL A 843  THR A 847  0                                        
SHEET    2 AA2 2 HIS A 850  ILE A 853 -1  O  LYS A 852   N  LEU A 844           
SITE     1 AC1 10 ALA A 743  LYS A 745  GLU A 762  MET A 766                    
SITE     2 AC1 10 LEU A 777  LEU A 788  MET A 790  GLN A 791                    
SITE     3 AC1 10 MET A 793  LEU A 844                                          
CRYST1  148.919  148.919  148.919  90.00  90.00  90.00 I 2 3        24          
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      0.006715  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006715  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006715        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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