GenomeNet

Database: PDB
Entry: 5CAO
LinkDB: 5CAO
Original site: 5CAO 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       29-JUN-15   5CAO              
TITLE     EGFR KINASE DOMAIN MUTANT "TMLR" WITH COMPOUND 29                     
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;                                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7106                                        
KEYWDS    PHOSPHOTRANSFER, INHIBITOR, PROTEIN KINASE, TRANSFERASE-TRANSFERASE   
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,C.YU                                                      
REVDAT   3   02-DEC-15 5CAO    1       JRNL                                     
REVDAT   2   25-NOV-15 5CAO    1       JRNL                                     
REVDAT   1   28-OCT-15 5CAO    0                                                
JRNL        AUTH   R.HEALD,K.K.BOWMAN,M.C.BRYAN,D.BURDICK,B.CHAN,E.CHAN,Y.CHEN, 
JRNL        AUTH 2 S.CLAUSEN,B.DOMINGUEZ-FERNANDEZ,C.EIGENBROT,R.ELLIOTT,       
JRNL        AUTH 3 E.J.HANAN,P.JACKSON,J.KNIGHT,H.LA,M.LAINCHBURY,S.MALEK,      
JRNL        AUTH 4 S.MANN,M.MERCHANT,K.MORTARA,H.PURKEY,G.SCHAEFER,S.SCHMIDT,   
JRNL        AUTH 5 E.SEWARD,S.SIDERIS,L.SHAO,S.WANG,K.YEAP,I.YEN,C.YU,          
JRNL        AUTH 6 T.P.HEFFRON                                                  
JRNL        TITL   NONCOVALENT MUTANT SELECTIVE EPIDERMAL GROWTH FACTOR         
JRNL        TITL 2 RECEPTOR INHIBITORS: A LEAD OPTIMIZATION CASE STUDY.         
JRNL        REF    J.MED.CHEM.                   V.  58  8877 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26455919                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01412                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17015                          
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)  : 0.203                          
REMARK   3   R VALUE            (WORKING SET)  : 0.202                          
REMARK   3   FREE R VALUE                      : 0.231                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.180                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 711                            
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.76                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.35                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2653                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2342                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2549                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2340                   
REMARK   3   BIN FREE R VALUE                        : 0.2404                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.92                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 104                      
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            : 2416                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 69.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.90                          
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) : 0.445               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.291               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.220               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.306               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.227               
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      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2500   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3389   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 879    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 59     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 348    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2500   ; 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   : 322    ; 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   : 2750   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.51                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.47                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|696 - A|786 A|1004 - A|1020}                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -55.9367    7.9832  -31.5154           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0405 T22:   -0.0726                                    
REMARK   3     T33:   -0.0732 T12:   -0.1317                                    
REMARK   3     T13:    0.0537 T23:    0.0464                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1940 L22:    0.9589                                    
REMARK   3     L33:    5.7128 L12:    0.8943                                    
REMARK   3     L13:    0.6870 L23:    0.6045                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0017 S12:   -0.0390 S13:    0.2039                     
REMARK   3     S21:   -0.0946 S22:   -0.0487 S23:   -0.1765                     
REMARK   3     S31:   -0.2555 S32:    0.5442 S33:    0.0470                     
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):  -62.2690  -15.7877  -23.0620           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0471 T22:   -0.0794                                    
REMARK   3     T33:   -0.1207 T12:   -0.0312                                    
REMARK   3     T13:    0.1208 T23:    0.0819                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8235 L22:    5.3148                                    
REMARK   3     L33:    2.0396 L12:    1.8376                                    
REMARK   3     L13:   -0.9956 L23:   -1.6515                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2351 S12:   -0.1429 S13:   -0.3281                     
REMARK   3     S21:   -0.5368 S22:   -0.0730 S23:   -0.5442                     
REMARK   3     S31:    0.3291 S32:    0.2879 S33:    0.3081                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|988 - A|999}                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -66.0474    5.5386   -8.7469           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1598 T22:    0.0182                                    
REMARK   3     T33:   -0.0863 T12:   -0.1520                                    
REMARK   3     T13:    0.0491 T23:    0.0884                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.9582                                    
REMARK   3     L33:    1.7277 L12:   -0.2814                                    
REMARK   3     L13:   -0.6219 L23:    1.7021                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0128 S12:   -0.0825 S13:    0.0887                     
REMARK   3     S21:    0.0713 S22:   -0.0209 S23:   -0.0053                     
REMARK   3     S31:    0.0032 S32:   -0.0271 S33:    0.0337                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CAO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211315.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-13                          
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                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17033                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.9000                            
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: MOLECULAR REPLACEMENT        
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   (%): 66.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, ETHLYENE GLYCOL, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING 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       74.57950            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       74.57950            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       74.57950            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       74.57950            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       74.57950            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       74.57950            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       74.57950            
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: 15640 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     ARG A   748                                                      
REMARK 465     GLU A   749                                                      
REMARK 465     ALA A   750                                                      
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     ALA A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     MET A  1002                                                      
REMARK 465     ASP A  1003                                                      
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      -84.42     15.42                                   
REMARK 500    VAL A 786      121.69    103.14                                   
REMARK 500    ARG A 836      -10.46     76.18                                   
REMARK 500    ASP A 855       80.31     65.56                                   
REMARK 500    ARG A 858       -3.88   -141.62                                   
REMARK 500    GLU A 985      -37.49    103.83                                   
REMARK 500    GLU A1005      -79.80   -135.83                                   
REMARK 500    ASP A1009       40.30    -98.52                                   
REMARK 500    LEU A1017      -60.37     61.79                                   
REMARK 500    ILE A1018      123.51     68.65                                   
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 4ZG A 1101                
DBREF  5CAO A  695  1022  UNP    P00533   EGFR_HUMAN     695   1022             
SEQADV 5CAO GLY A  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5CAO MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5CAO ARG A  858  UNP  P00533    LEU   858 ENGINEERED MUTATION            
SEQADV 5CAO ALA A  865  UNP  P00533    GLU   865 ENGINEERED MUTATION            
SEQADV 5CAO ALA A  866  UNP  P00533    GLU   866 ENGINEERED MUTATION            
SEQADV 5CAO ALA A  867  UNP  P00533    LYS   867 ENGINEERED MUTATION            
SEQADV 5CAO ASN A 1023  UNP  P00533              EXPRESSION TAG                 
SEQADV 5CAO 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    4ZG  A1101      29                                                       
HETNAM     4ZG N~2~-[2-METHYL-2-(METHYLSULFONYL)PROPYL]-N~4~-[2-                
HETNAM   2 4ZG  METHYL-1-(PROPAN-2-YL)-1H-IMIDAZO[4,5-C]PYRIDIN-6-              
HETNAM   3 4ZG  YL]PYRIMIDINE-2,4-DIAMINE                                       
FORMUL   2  4ZG    C19 H27 N7 O2 S                                              
FORMUL   3  HOH   *5(H2 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 GLY A  810  ARG A  831  1                                  22    
HELIX    5 AA5 ALA A  839  ARG A  841  5                                   3    
HELIX    6 AA6 PRO A  877  MET A  881  5                                   5    
HELIX    7 AA7 ALA A  882  ARG A  889  1                                   8    
HELIX    8 AA8 THR A  892  THR A  909  1                                  18    
HELIX    9 AA9 SER A  921  GLY A  930  1                                  10    
HELIX   10 AB1 THR A  940  CYS A  950  1                                  11    
HELIX   11 AB2 ASP A  954  ARG A  958  5                                   5    
HELIX   12 AB3 LYS A  960  ARG A  973  1                                  14    
HELIX   13 AB4 ASP A  974  TYR A  978  5                                   5    
SHEET    1 AA1 5 PHE A 712  GLY A 721  0                                        
SHEET    2 AA1 5 GLY A 724  TRP A 731 -1  O  LYS A 728   N  ILE A 715           
SHEET    3 AA1 5 ILE A 740  GLU A 746 -1  O  VAL A 742   N  GLY A 729           
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 11 LEU A 718  ALA A 743  LYS A 745  MET A 766                    
SITE     2 AC1 11 CYS A 775  MET A 790  GLN A 791  MET A 793                    
SITE     3 AC1 11 LEU A 844  THR A 854  ASP A 855                               
CRYST1  149.159  149.159  149.159  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      0.006704  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006704  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system