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Database: PDB
Entry: 2ITU
LinkDB: 2ITU
Original site: 2ITU 
HEADER    TRANSFERASE                             25-MAY-06   2ITU              
TITLE     CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN             
TITLE    2 COMPLEX WITH AFN941                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 696-1022;                          
COMPND   5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;                    
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: EGFR 696-1022 L858R                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PACG2T;                                   
SOURCE   9 OTHER_DETAILS: EGFR 696-1022 L858R                                   
KEYWDS    RECEPTOR, CELL CYCLE, ATP-BINDING, TRANSFERASE,                       
KEYWDS   2 TRANSMEMBRANE, PHOSPHORYLATION, DISEASE MUTATION,                    
KEYWDS   3 POLYMORPHISM, GLYCOPROTEIN, ANTI-ONCOGENE, NUCLEOTIDE-               
KEYWDS   4 BINDING, ALTERNATIVE SPLICING, AFN941, EGFR, L858R,                  
KEYWDS   5 STAUROSPORINE, MEMBRANE TYROSINE-PROTEIN KINASE, EPIDERMAL           
KEYWDS   6 GROWTH FACTOR                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-H.YUN,T.J.BOGGON,Y.LI,S.WOO,H.GREULICH,M.MEYERSON,                 
AUTHOR   2 M.J.ECK                                                              
REVDAT   5   27-MAR-13 2ITU    1       REMARK VERSN  HET    HETNAM              
REVDAT   5 2                           HETSYN FORMUL HETATM                     
REVDAT   4   24-FEB-09 2ITU    1       VERSN                                    
REVDAT   3   06-MAY-08 2ITU    1       COMPND REMARK                            
REVDAT   2   29-JAN-08 2ITU    1       SOURCE SITE                              
REVDAT   1   03-APR-07 2ITU    0                                                
JRNL        AUTH   C.-H.YUN,T.J.BOGGON,Y.LI,S.WOO,H.GREULICH,                   
JRNL        AUTH 2 M.MEYERSON,M.J.ECK                                           
JRNL        TITL   STRUCTURES OF LUNG CANCER-DERIVED EGFR MUTANTS AND           
JRNL        TITL 2 INHIBITOR COMPLEXES: MECHANISM OF ACTIVATION AND             
JRNL        TITL 3 INSIGHTS INTO DIFFERENTIAL INHIBITOR SENSITIVITY             
JRNL        REF    CANCER CELL                   V.  11   217 2007              
JRNL        REFN                   ISSN 1535-6108                               
JRNL        PMID   17349580                                                     
JRNL        DOI    10.1016/J.CCR.2006.12.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11977                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 616                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 887                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 42                           
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2423                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 92                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.678         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.340         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2516 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3418 ; 1.889 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   303 ; 7.012 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;42.094 ;23.981       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   455 ;20.051 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;21.792 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   382 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1852 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1207 ; 0.263 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1707 ; 0.333 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   111 ; 0.180 ; 0.200       
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):    44 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.144 ; 0.200       
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):  1523 ; 1.122 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2472 ; 2.120 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   993 ; 2.340 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   946 ; 3.971 ; 4.500       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2ITU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-28811.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM-4)                    
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12764                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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: PDB ENTRY 1M14                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG400, 0.15M NACL, 0.1M             
REMARK 280  HEPES 8.0                                                           
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       72.48100            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       72.48100            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       72.48100            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       72.48100            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       72.48100            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       72.48100            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       72.48100            
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  RECEPTOR FOR EGF, BUT ALSO FOR OTHER MEMBERS OF THE EGF             
REMARK 400  FAMILY, AS TGF-ALPHA, AMPHIREGULIN, BETACELLULIN, HEPARIN-BINDING   
REMARK 400  EGF-LIKE GROWTH FACTOR, GP30 AND VACCINIA VIRUS GROWTH FACTOR.      
REMARK 400                                                                      
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 858 TO ARG                        
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     GLU A   866                                                      
REMARK 465     LYS 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     PRO A   992                                                      
REMARK 465     THR A   993                                                      
REMARK 465     ASP A   994                                                      
REMARK 465     SER A   995                                                      
REMARK 465     ASN A   996                                                      
REMARK 465     PHE A   997                                                      
REMARK 465     TYR A   998                                                      
REMARK 465     ARG A   999                                                      
REMARK 465     ALA A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     GLN A  1021                                                      
REMARK 465     GLY A  1022                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A1004    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1005    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1006    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 990   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
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 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    ILE A 715      -17.92   -161.02                                   
REMARK 500    LYS A 716      134.76    177.07                                   
REMARK 500    ALA A 722      -50.83     -0.66                                   
REMARK 500    THR A 725      102.98   -163.87                                   
REMARK 500    GLU A 736      -15.78   -150.09                                   
REMARK 500    ARG A 748       68.31    -35.05                                   
REMARK 500    GLU A 749     -102.81     36.88                                   
REMARK 500    ALA A 750      123.14    -26.19                                   
REMARK 500    THR A 751       60.77   -111.93                                   
REMARK 500    PRO A 753      -42.01    -22.85                                   
REMARK 500    SER A 784      -71.87    177.24                                   
REMARK 500    LYS A 806      -70.23    -20.19                                   
REMARK 500    ARG A 836        2.63     55.69                                   
REMARK 500    ASP A 837       38.45   -142.29                                   
REMARK 500    ASP A 855       91.54     59.25                                   
REMARK 500    ALA A 882      170.04    -57.07                                   
REMARK 500    ARG A 889       28.87     33.42                                   
REMARK 500    ILE A 918      116.81    -34.55                                   
REMARK 500    PHE A 961      -35.62    -39.23                                   
REMARK 500    ARG A 986       70.79   -102.92                                   
REMARK 500    PRO A 990     -177.14    -28.47                                   
REMARK 500    ASP A1003      -93.04   -140.64                                   
REMARK 500    GLU A1004     -171.92    -47.24                                   
REMARK 500    ASP A1006       43.90    -67.97                                   
REMARK 500    MET A1007       31.39    -90.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 749        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITQ A2020                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DNQ   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE FIRST AND SECOND                           
REMARK 900  DOMAINS OF THE HUMAN EPIDERMAL GROWTH FACTOR                        
REMARK 900   RECEPTOR ECTODOMAIN                                                
REMARK 900 RELATED ID: 1DNR   RELATED DB: PDB                                   
REMARK 900  THEORETICAL MODEL OF THE THIRD AND FOURTH                           
REMARK 900  DOMAINS OF THE HUMAN EPIDERMAL GROWTH FACTOR                        
REMARK 900   RECEPTOR ECTODOMAIN                                                
REMARK 900 RELATED ID: 1IVO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN                           
REMARK 900  EPIDERMAL GROWTHFACTOR AND RECEPTOR                                 
REMARK 900  EXTRACELLULAR DOMAINS.                                              
REMARK 900 RELATED ID: 1M14   RELATED DB: PDB                                   
REMARK 900  TYROSINE KINASE DOMAIN FROM EPIDERMAL GROWTH                        
REMARK 900  FACTOR RECEPTOR                                                     
REMARK 900 RELATED ID: 1M17   RELATED DB: PDB                                   
REMARK 900  EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE                           
REMARK 900  KINASE DOMAINWITH 4-ANILINOQUINAZOLINE INHIBITOR                    
REMARK 900   ERLOTINIB                                                          
REMARK 900 RELATED ID: 1MOX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN EPIDERMAL GROWTH                         
REMARK 900  FACTOR RECEPTOR(RESIDUES 1-501) IN COMPLEX                          
REMARK 900  WITH TGF-ALPHA                                                      
REMARK 900 RELATED ID: 1NQL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE EXTRACELLULAR DOMAIN OF                            
REMARK 900  HUMAN EPIDERMALGROWTH FACTOR (EGF) RECEPTOR IN                      
REMARK 900   AN INACTIVE (LOW PH)COMPLEX WITH EGF.                              
REMARK 900 RELATED ID: 1XKK   RELATED DB: PDB                                   
REMARK 900  EGFR KINASE DOMAIN COMPLEXED WITH A                                 
REMARK 900  QUINAZOLINE INHIBITOR-GW572016                                      
REMARK 900 RELATED ID: 1YY9   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE                        
REMARK 900   EPIDERMALGROWTH FACTOR RECEPTOR IN COMPLEX                         
REMARK 900  WITH THE FAB FRAGMENT OFCETUXIMAB/ERBITUX/                          
REMARK 900  IMC-C225                                                            
REMARK 900 RELATED ID: 1Z9I   RELATED DB: PDB                                   
REMARK 900  A STRUCTURAL MODEL FOR THE MEMBRANE-BOUND                           
REMARK 900  FORM OF THEJUXTAMEMBRANE DOMAIN OF THE                              
REMARK 900  EPIDERMAL GROWTH FACTOR RECEPTOR                                    
REMARK 900 RELATED ID: 2ITN   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  G719S MUTATION IN COMPLEX WITH AMP-PNP                              
REMARK 900 RELATED ID: 2ITO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  G719S MUTATION IN COMPLEX WITH IRESSA                               
REMARK 900 RELATED ID: 2ITP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  G719S MUTATION IN COMPLEX WITH AEE788                               
REMARK 900 RELATED ID: 2ITQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  G719S MUTATION IN COMPLEX WITH AFN941                               
REMARK 900 RELATED ID: 2ITT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  L858R MUTATION IN COMPLEX WITH AEE788                               
REMARK 900 RELATED ID: 2ITV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  L858R MUTATION IN COMPLEX WITH AMP-PNP                              
REMARK 900 RELATED ID: 2ITW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN                          
REMARK 900  COMPLEX WITH AFN941                                                 
REMARK 900 RELATED ID: 2ITX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN                          
REMARK 900  COMPLEX WITH AMP-PNP                                                
REMARK 900 RELATED ID: 2ITY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN                          
REMARK 900  COMPLEX WITH IRESSA                                                 
REMARK 900 RELATED ID: 2ITZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN                             
REMARK 900  L858R MUTATION IN COMPLEX WITH IRESSA                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 L858R MUTATION                                                       
DBREF  2ITU A  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
SEQADV 2ITU ARG A  858  UNP  P00533    LEU   858 ENGINEERED MUTATION            
SEQRES   1 A  327  GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE LEU LYS          
SEQRES   2 A  327  GLU THR GLU PHE LYS LYS ILE LYS VAL LEU GLY SER GLY          
SEQRES   3 A  327  ALA PHE GLY THR VAL TYR LYS GLY LEU TRP ILE PRO GLU          
SEQRES   4 A  327  GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE LYS GLU LEU          
SEQRES   5 A  327  ARG GLU ALA THR SER PRO LYS ALA ASN LYS GLU ILE LEU          
SEQRES   6 A  327  ASP GLU ALA TYR VAL MET ALA SER VAL ASP ASN PRO HIS          
SEQRES   7 A  327  VAL CYS ARG LEU LEU GLY ILE CYS LEU THR SER THR VAL          
SEQRES   8 A  327  GLN LEU ILE THR GLN LEU MET PRO PHE GLY CYS LEU LEU          
SEQRES   9 A  327  ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE GLY SER GLN          
SEQRES  10 A  327  TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET          
SEQRES  11 A  327  ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS ARG ASP LEU          
SEQRES  12 A  327  ALA ALA ARG ASN VAL LEU VAL LYS THR PRO GLN HIS VAL          
SEQRES  13 A  327  LYS ILE THR ASP PHE GLY ARG ALA LYS LEU LEU GLY ALA          
SEQRES  14 A  327  GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY LYS VAL PRO          
SEQRES  15 A  327  ILE LYS TRP MET ALA LEU GLU SER ILE LEU HIS ARG ILE          
SEQRES  16 A  327  TYR THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR          
SEQRES  17 A  327  VAL TRP GLU LEU MET THR PHE GLY SER LYS PRO TYR ASP          
SEQRES  18 A  327  GLY ILE PRO ALA SER GLU ILE SER SER ILE LEU GLU LYS          
SEQRES  19 A  327  GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP          
SEQRES  20 A  327  VAL TYR MET ILE MET VAL LYS CYS TRP MET ILE ASP ALA          
SEQRES  21 A  327  ASP SER ARG PRO LYS PHE ARG GLU LEU ILE ILE GLU PHE          
SEQRES  22 A  327  SER LYS MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE          
SEQRES  23 A  327  GLN GLY ASP GLU ARG MET HIS LEU PRO SER PRO THR ASP          
SEQRES  24 A  327  SER ASN PHE TYR ARG ALA LEU MET ASP GLU GLU ASP MET          
SEQRES  25 A  327  ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU ILE PRO GLN          
SEQRES  26 A  327  GLN GLY                                                      
HET    ITQ  A2020      35                                                       
HETNAM     ITQ 1,2,3,4-TETRAHYDROGEN STAUROSPORINE                              
HETSYN     ITQ STAUROSPORINE ANALOGUE - AFN941                                  
FORMUL   2  ITQ    C28 H28 N4 O3                                                
FORMUL   3  HOH   *92(H2 O1)                                                    
HELIX    1   1 LYS A  708  THR A  710  5                                   3    
HELIX    2   2 SER A  752  SER A  768  1                                  17    
HELIX    3   3 LEU A  798  GLU A  804  1                                   7    
HELIX    4   4 HIS A  805  ILE A  809  5                                   5    
HELIX    5   5 GLY A  810  ARG A  831  1                                  22    
HELIX    6   6 ALA A  839  ARG A  841  5                                   3    
HELIX    7   7 PRO A  877  MET A  881  5                                   5    
HELIX    8   8 ALA A  882  ARG A  889  1                                   8    
HELIX    9   9 THR A  892  THR A  909  1                                  18    
HELIX   10  10 GLU A  922  GLY A  930  1                                   9    
HELIX   11  11 THR A  940  CYS A  950  1                                  11    
HELIX   12  12 ASP A  954  ARG A  958  5                                   5    
HELIX   13  13 LYS A  960  ALA A  972  1                                  13    
HELIX   14  14 ASP A  974  LEU A  979  1                                   6    
HELIX   15  15 ASP A 1012  TYR A 1016  5                                   5    
SHEET    1  AA 5 PHE A 712  VAL A 717  0                                        
SHEET    2  AA 5 VAL A 726  TRP A 731 -1  O  LYS A 728   N  ILE A 715           
SHEET    3  AA 5 ILE A 740  GLU A 746 -1  O  ILE A 740   N  TRP A 731           
SHEET    4  AA 5 VAL A 786  GLN A 791 -1  O  LEU A 788   N  LYS A 745           
SHEET    5  AA 5 LEU A 777  LEU A 782 -1  N  LEU A 778   O  ILE A 789           
SHEET    1  AB 3 GLY A 796  CYS A 797  0                                        
SHEET    2  AB 3 VAL A 843  THR A 847 -1  N  VAL A 845   O  GLY A 796           
SHEET    3  AB 3 HIS A 850  ILE A 853 -1  O  HIS A 850   N  LYS A 846           
SHEET    1  AC 2 LEU A 833  VAL A 834  0                                        
SHEET    2  AC 2 LYS A 860  LEU A 861 -1  O  LYS A 860   N  VAL A 834           
SITE     1 AC1 10 GLY A 719  ALA A 743  LYS A 745  LEU A 792                    
SITE     2 AC1 10 MET A 793  PRO A 794  CYS A 797  ASP A 800                    
SITE     3 AC1 10 HOH A3025  HOH A3045                                          
CRYST1  144.962  144.962  144.962  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      0.006898  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006898        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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