GenomeNet

Database: PDB
Entry: 5C8N
LinkDB: 5C8N
Original site: 5C8N 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       25-JUN-15   5C8N              
TITLE     EGFR KINASE DOMAIN MUTANT "TMLR" WITH COMPOUND 23                     
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   02-DEC-15 5C8N    1       JRNL                                     
REVDAT   2   25-NOV-15 5C8N    1       JRNL                                     
REVDAT   1   28-OCT-15 5C8N    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.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19302                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 842                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2795                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2408                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 106                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.92                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.676         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2499 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2410 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3386 ; 1.224 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5562 ; 0.742 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 5.522 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;38.534 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   451 ;13.487 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;11.336 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   376 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2709 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   526 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5C8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211224.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20144                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.9000                            
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   (%): 64.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, ETHYLENE 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       72.96600            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       72.96600            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       72.96600            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       72.96600            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       72.96600            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       72.96600            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       72.96600            
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: 190 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 A1304  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   694                                                      
REMARK 465     SER A   695                                                      
REMARK 465     ARG A   748                                                      
REMARK 465     GLU A   749                                                      
REMARK 465     ALA A   750                                                      
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     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     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     -125.88     38.72                                   
REMARK 500    VAL A 786      120.79     83.34                                   
REMARK 500    ARG A 836       -0.43     73.34                                   
REMARK 500    ASP A 837       36.37   -148.44                                   
REMARK 500    ASP A 855       83.03     61.96                                   
REMARK 500    GLU A 985      -14.13     86.38                                   
REMARK 500    MET A1007      -30.16     61.97                                   
REMARK 500    ILE A1018      160.64     58.62                                   
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 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4YX A 1102                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CK8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CKM   RELATED DB: PDB                                   
DBREF  5C8N A  695  1022  UNP    P00533   EGFR_HUMAN     695   1022             
SEQADV 5C8N GLY A  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5C8N MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5C8N ARG A  858  UNP  P00533    LEU   858 ENGINEERED MUTATION            
SEQADV 5C8N ALA A  865  UNP  P00533    GLU   865 ENGINEERED MUTATION            
SEQADV 5C8N ALA A  866  UNP  P00533    GLU   866 ENGINEERED MUTATION            
SEQADV 5C8N ALA A  867  UNP  P00533    LYS   867 ENGINEERED MUTATION            
SEQADV 5C8N ASN A 1023  UNP  P00533              EXPRESSION TAG                 
SEQADV 5C8N 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    SO4  A1101       5                                                       
HET    4YX  A1102      31                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     4YX N-{2-[4-(2-AMINOETHYL)-4-METHOXYPIPERIDIN-1-                     
HETNAM   2 4YX  YL]PYRIMIDIN-4-YL}-2-METHYL-1-(PROPAN-2-YL)-1H-                 
HETNAM   3 4YX  IMIDAZO[4,5-C]PYRIDIN-6-AMINE                                   
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  4YX    C22 H32 N8 O                                                 
FORMUL   4  HOH   *106(H2 O)                                                    
HELIX    1 AA1 LYS A  708  THR A  710  5                                   3    
HELIX    2 AA2 SER A  752  ALA A  767  1                                  16    
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  LYS A  929  1                                  11    
HELIX   11 AB2 THR A  940  CYS A  950  1                                  11    
HELIX   12 AB3 ASP A  954  ARG A  958  5                                   5    
HELIX   13 AB4 LYS A  960  ARG A  973  1                                  14    
HELIX   14 AB5 ASP A  974  TYR A  978  5                                   5    
HELIX   15 AB6 ASP A 1012  TYR A 1016  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  VAL A 726   N  LEU A 718           
SHEET    3 AA1 5 ILE A 740  GLU A 746 -1  O  ILE A 744   N  TYR A 727           
SHEET    4 AA1 5 GLN A 787  GLN A 791 -1  O  LEU A 788   N  LYS A 745           
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  5 VAL A 876  PRO A 877  ILE A 878  LYS A 879                    
SITE     2 AC1  5 TRP A 880                                                     
SITE     1 AC2 13 LEU A 718  PHE A 723  ALA A 743  LYS A 745                    
SITE     2 AC2 13 MET A 766  CYS A 775  MET A 790  GLN A 791                    
SITE     3 AC2 13 MET A 793  LEU A 844  THR A 854  ASP A 855                    
SITE     4 AC2 13 HOH A1252                                                     
CRYST1  145.932  145.932  145.932  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      0.006853  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006853  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006853        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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