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Database: PDB
Entry: 5YU9
LinkDB: 5YU9
Original site: 5YU9 
HEADER    ONCOPROTEIN                             21-NOV-17   5YU9              
TITLE     CRYSTAL STRUCTURE OF EGFR 696-1022 T790M IN COMPLEX WITH IBRUTINIB    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
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_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    EGFR, T790M, IBRUTINIB, INHIBITOR, ONCOPROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.E.YAN,C.H.YUN                                                       
REVDAT   1   27-DEC-17 5YU9    0                                                
JRNL        AUTH   A.WANG,X.E.YAN,H.WU,W.WANG,C.HU,C.CHEN,Z.ZHAO,P.ZHAO,X.LI,   
JRNL        AUTH 2 L.WANG,B.WANG,Z.YE,J.WANG,C.WANG,W.ZHANG,N.S.GRAY,           
JRNL        AUTH 3 E.L.WEISBERG,L.CHEN,J.LIU,C.H.YUN,Q.LIU                      
JRNL        TITL   IBRUTINIB TARGETS MUTANT-EGFR KINASE WITH A DISTINCT BINDING 
JRNL        TITL 2 CONFORMATION.                                                
JRNL        REF    ONCOTARGET                    V.   7 69760 2016              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   27626175                                                     
JRNL        DOI    10.18632/ONCOTARGET.11951                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2400)                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 94954                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4744                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.6379 -  6.0532    0.96     3037   138  0.2182 0.2377        
REMARK   3     2  6.0532 -  4.8069    0.99     3043   153  0.1921 0.2065        
REMARK   3     3  4.8069 -  4.1999    0.99     3039   163  0.1665 0.1700        
REMARK   3     4  4.1999 -  3.8162    0.99     3004   155  0.1606 0.1567        
REMARK   3     5  3.8162 -  3.5428    0.99     3000   177  0.1762 0.2254        
REMARK   3     6  3.5428 -  3.3340    1.00     3045   165  0.1883 0.1941        
REMARK   3     7  3.3340 -  3.1671    1.00     3007   168  0.1900 0.1999        
REMARK   3     8  3.1671 -  3.0293    1.00     3053   138  0.1958 0.2111        
REMARK   3     9  3.0293 -  2.9127    1.00     3012   158  0.2026 0.2409        
REMARK   3    10  2.9127 -  2.8122    1.00     2971   190  0.2059 0.2435        
REMARK   3    11  2.8122 -  2.7243    1.00     3045   155  0.2126 0.2446        
REMARK   3    12  2.7243 -  2.6465    1.00     2987   151  0.2038 0.2219        
REMARK   3    13  2.6465 -  2.5768    1.00     3007   162  0.2082 0.2323        
REMARK   3    14  2.5768 -  2.5139    1.00     2995   167  0.2207 0.2185        
REMARK   3    15  2.5139 -  2.4568    1.00     3005   167  0.2155 0.2547        
REMARK   3    16  2.4568 -  2.4045    1.00     2993   146  0.2165 0.2373        
REMARK   3    17  2.4045 -  2.3564    1.00     3005   160  0.2202 0.2414        
REMARK   3    18  2.3564 -  2.3120    1.00     3016   166  0.2172 0.2726        
REMARK   3    19  2.3120 -  2.2707    1.00     2982   178  0.2127 0.2400        
REMARK   3    20  2.2707 -  2.2322    1.00     3017   150  0.2127 0.2295        
REMARK   3    21  2.2322 -  2.1962    0.99     2978   161  0.2048 0.2151        
REMARK   3    22  2.1962 -  2.1624    1.00     3046   149  0.2148 0.2503        
REMARK   3    23  2.1624 -  2.1306    1.00     2989   144  0.2284 0.2481        
REMARK   3    24  2.1306 -  2.1006    1.00     3025   141  0.2235 0.2493        
REMARK   3    25  2.1006 -  2.0722    1.00     3006   163  0.2389 0.2809        
REMARK   3    26  2.0722 -  2.0453    1.00     2990   154  0.2450 0.2285        
REMARK   3    27  2.0453 -  2.0197    1.00     2988   178  0.2505 0.2990        
REMARK   3    28  2.0197 -  1.9954    1.00     2990   150  0.2612 0.2856        
REMARK   3    29  1.9954 -  1.9722    1.00     3041   157  0.2642 0.3000        
REMARK   3    30  1.9722 -  1.9500    0.97     2894   140  0.2643 0.2797        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012          10063                                  
REMARK   3   ANGLE     :  1.387          13643                                  
REMARK   3   CHIRALITY :  0.112           1528                                  
REMARK   3   PLANARITY :  0.009           1705                                  
REMARK   3   DIHEDRAL  : 26.059           3956                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YU9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005922.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97930                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94954                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
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: 3IKA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE (PH 5.0), 12% PEG   
REMARK 280  10000, 3% DIOXANE, 5 MM TCEP, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.09700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.19250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.09700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.19250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 CL    CL C1103  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   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     MET A   694                                                      
REMARK 465     GLY A   695                                                      
REMARK 465     GLY A   696                                                      
REMARK 465     GLU A   697                                                      
REMARK 465     ALA A   698                                                      
REMARK 465     PRO A   699                                                      
REMARK 465     ALA A   750                                                      
REMARK 465     THR A   751                                                      
REMARK 465     SER A   752                                                      
REMARK 465     PRO A   753                                                      
REMARK 465     GLY A   863                                                      
REMARK 465     ALA A   864                                                      
REMARK 465     GLU A   865                                                      
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     ILE A  1018                                                      
REMARK 465     PRO A  1019                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     GLN A  1021                                                      
REMARK 465     GLY A  1022                                                      
REMARK 465     GLY B   692                                                      
REMARK 465     ALA B   693                                                      
REMARK 465     MET B   694                                                      
REMARK 465     GLY B   695                                                      
REMARK 465     GLY B   696                                                      
REMARK 465     GLU B   697                                                      
REMARK 465     ALA B   698                                                      
REMARK 465     ALA B   750                                                      
REMARK 465     THR B   751                                                      
REMARK 465     SER B   752                                                      
REMARK 465     PRO B   753                                                      
REMARK 465     LYS B   754                                                      
REMARK 465     GLY B   863                                                      
REMARK 465     ALA B   864                                                      
REMARK 465     GLU B   865                                                      
REMARK 465     GLU B   866                                                      
REMARK 465     LYS B   867                                                      
REMARK 465     GLU B   868                                                      
REMARK 465     TYR B   869                                                      
REMARK 465     HIS B   870                                                      
REMARK 465     ALA B   871                                                      
REMARK 465     GLU B   872                                                      
REMARK 465     GLY B   873                                                      
REMARK 465     GLY B   874                                                      
REMARK 465     LYS B   875                                                      
REMARK 465     ASP B  1012                                                      
REMARK 465     ALA B  1013                                                      
REMARK 465     ASP B  1014                                                      
REMARK 465     GLU B  1015                                                      
REMARK 465     TYR B  1016                                                      
REMARK 465     LEU B  1017                                                      
REMARK 465     ILE B  1018                                                      
REMARK 465     PRO B  1019                                                      
REMARK 465     GLN B  1020                                                      
REMARK 465     GLN B  1021                                                      
REMARK 465     GLY B  1022                                                      
REMARK 465     GLY C   692                                                      
REMARK 465     ALA C   693                                                      
REMARK 465     MET C   694                                                      
REMARK 465     GLY C   695                                                      
REMARK 465     GLY C   696                                                      
REMARK 465     ALA C   750                                                      
REMARK 465     THR C   751                                                      
REMARK 465     SER C   752                                                      
REMARK 465     PRO C   753                                                      
REMARK 465     GLY C   863                                                      
REMARK 465     ALA C   864                                                      
REMARK 465     GLU C   865                                                      
REMARK 465     GLU C   866                                                      
REMARK 465     LYS C   867                                                      
REMARK 465     GLU C   868                                                      
REMARK 465     TYR C   869                                                      
REMARK 465     HIS C   870                                                      
REMARK 465     ALA C   871                                                      
REMARK 465     GLU C   872                                                      
REMARK 465     GLY C   873                                                      
REMARK 465     GLY C   874                                                      
REMARK 465     ASP C  1008                                                      
REMARK 465     ASP C  1009                                                      
REMARK 465     VAL C  1010                                                      
REMARK 465     GLY C  1022                                                      
REMARK 465     GLY D   692                                                      
REMARK 465     ALA D   693                                                      
REMARK 465     MET D   694                                                      
REMARK 465     GLY D   695                                                      
REMARK 465     GLY D   696                                                      
REMARK 465     GLU D   697                                                      
REMARK 465     ALA D   698                                                      
REMARK 465     PRO D   699                                                      
REMARK 465     GLY D   863                                                      
REMARK 465     ALA D   864                                                      
REMARK 465     GLU D   865                                                      
REMARK 465     GLU D   866                                                      
REMARK 465     LYS D   867                                                      
REMARK 465     GLU D   868                                                      
REMARK 465     TYR D   869                                                      
REMARK 465     HIS D   870                                                      
REMARK 465     ALA D   871                                                      
REMARK 465     GLU D   872                                                      
REMARK 465     GLY D   873                                                      
REMARK 465     GLY D   874                                                      
REMARK 465     LYS D   875                                                      
REMARK 465     ALA D  1013                                                      
REMARK 465     ASP D  1014                                                      
REMARK 465     GLU D  1015                                                      
REMARK 465     TYR D  1016                                                      
REMARK 465     LEU D  1017                                                      
REMARK 465     ILE D  1018                                                      
REMARK 465     PRO D  1019                                                      
REMARK 465     GLN D  1020                                                      
REMARK 465     GLN D  1021                                                      
REMARK 465     GLY D  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     LYS A 708    CE   NZ                                             
REMARK 470     GLU A 749    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 875    CG   CD   CE   NZ                                   
REMARK 470     LYS A 960    CE   NZ                                             
REMARK 470     HIS A 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A1016    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     LEU A1017    CG   CD1  CD2                                       
REMARK 470     LYS B 708    CE   NZ                                             
REMARK 470     GLU B 749    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1009    CG   OD1  OD2                                       
REMARK 470     VAL B1010    CG1  CG2                                            
REMARK 470     GLU C 697    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 734    CD   OE1  OE2                                       
REMARK 470     LYS C 737    CD   CE   NZ                                        
REMARK 470     ARG C 748    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C 749    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 754    CG   CD   CE   NZ                                   
REMARK 470     VAL C1011    CG1  CG2                                            
REMARK 470     ASP C1012    CG   OD1  OD2                                       
REMARK 470     GLU C1015    CG   CD   OE1  OE2                                  
REMARK 470     GLN C1021    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 754    CG   CD   CE   NZ                                   
REMARK 470     ARG D 962    CD   NE   CZ   NH1  NH2                             
REMARK 470     HIS D 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP D1008    CG   OD1  OD2                                       
REMARK 470     ASP D1009    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER D 925   CB    SER D 925   OG     -0.134                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE B 732   N   -  CA  -  CB  ANGL. DEV. =  14.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 784       -7.47     85.44                                   
REMARK 500    ARG A 836       -8.38     80.20                                   
REMARK 500    ASP A 837       55.99   -150.99                                   
REMARK 500    THR B 783     -155.52   -154.74                                   
REMARK 500    ARG B 836      -13.78     81.72                                   
REMARK 500    ASP B 837       43.21   -142.77                                   
REMARK 500    MET B1002       11.92   -145.82                                   
REMARK 500    ASP B1003       68.15   -152.63                                   
REMARK 500    ALA C 755        9.80     81.66                                   
REMARK 500    THR C 783       27.01   -145.14                                   
REMARK 500    SER C 784       -3.35     81.89                                   
REMARK 500    ARG C 836      -12.38     81.18                                   
REMARK 500    ASP C 837       41.39   -140.91                                   
REMARK 500    ASP C1003       76.43   -154.11                                   
REMARK 500    THR D 783     -155.53   -117.70                                   
REMARK 500    ARG D 836      -14.78     80.09                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1458        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B1459        DISTANCE =  8.24 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1E8 A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 1E8 B 1101 and CYS B   
REMARK 800  797                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 1E8 C 1101 and CYS C   
REMARK 800  797                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 1E8 D 1101 and CYS D   
REMARK 800  797                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YNJ   RELATED DB: PDB                                   
REMARK 900 THE SAME STRUCTURE                                                   
DBREF  5YU9 A  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5YU9 B  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5YU9 C  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5YU9 D  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
SEQADV 5YU9 GLY A  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 ALA A  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET A  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 GLY A  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5YU9 GLY B  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 ALA B  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET B  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 GLY B  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET B  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5YU9 GLY C  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 ALA C  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET C  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 GLY C  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET C  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5YU9 GLY D  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 ALA D  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET D  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 GLY D  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5YU9 MET D  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQRES   1 A  331  GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU          
SEQRES   2 A  331  ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL          
SEQRES   3 A  331  LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU          
SEQRES   4 A  331  TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA          
SEQRES   5 A  331  ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN          
SEQRES   6 A  331  LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL          
SEQRES   7 A  331  ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU          
SEQRES   8 A  331  THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE          
SEQRES   9 A  331  GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN          
SEQRES  10 A  331  ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE          
SEQRES  11 A  331  ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL          
SEQRES  12 A  331  HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR          
SEQRES  13 A  331  PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS          
SEQRES  14 A  331  LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY          
SEQRES  15 A  331  GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE          
SEQRES  16 A  331  LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER          
SEQRES  17 A  331  TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER          
SEQRES  18 A  331  LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER          
SEQRES  19 A  331  ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE          
SEQRES  20 A  331  CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP          
SEQRES  21 A  331  MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU          
SEQRES  22 A  331  ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG          
SEQRES  23 A  331  TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO          
SEQRES  24 A  331  SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP          
SEQRES  25 A  331  GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR          
SEQRES  26 A  331  LEU ILE PRO GLN GLN GLY                                      
SEQRES   1 B  331  GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU          
SEQRES   2 B  331  ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL          
SEQRES   3 B  331  LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU          
SEQRES   4 B  331  TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA          
SEQRES   5 B  331  ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN          
SEQRES   6 B  331  LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL          
SEQRES   7 B  331  ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU          
SEQRES   8 B  331  THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE          
SEQRES   9 B  331  GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN          
SEQRES  10 B  331  ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE          
SEQRES  11 B  331  ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL          
SEQRES  12 B  331  HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR          
SEQRES  13 B  331  PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS          
SEQRES  14 B  331  LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY          
SEQRES  15 B  331  GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE          
SEQRES  16 B  331  LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER          
SEQRES  17 B  331  TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER          
SEQRES  18 B  331  LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER          
SEQRES  19 B  331  ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE          
SEQRES  20 B  331  CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP          
SEQRES  21 B  331  MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU          
SEQRES  22 B  331  ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG          
SEQRES  23 B  331  TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO          
SEQRES  24 B  331  SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP          
SEQRES  25 B  331  GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR          
SEQRES  26 B  331  LEU ILE PRO GLN GLN GLY                                      
SEQRES   1 C  331  GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU          
SEQRES   2 C  331  ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL          
SEQRES   3 C  331  LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU          
SEQRES   4 C  331  TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA          
SEQRES   5 C  331  ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN          
SEQRES   6 C  331  LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL          
SEQRES   7 C  331  ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU          
SEQRES   8 C  331  THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE          
SEQRES   9 C  331  GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN          
SEQRES  10 C  331  ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE          
SEQRES  11 C  331  ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL          
SEQRES  12 C  331  HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR          
SEQRES  13 C  331  PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS          
SEQRES  14 C  331  LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY          
SEQRES  15 C  331  GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE          
SEQRES  16 C  331  LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER          
SEQRES  17 C  331  TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER          
SEQRES  18 C  331  LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER          
SEQRES  19 C  331  ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE          
SEQRES  20 C  331  CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP          
SEQRES  21 C  331  MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU          
SEQRES  22 C  331  ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG          
SEQRES  23 C  331  TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO          
SEQRES  24 C  331  SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP          
SEQRES  25 C  331  GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR          
SEQRES  26 C  331  LEU ILE PRO GLN GLN GLY                                      
SEQRES   1 D  331  GLY ALA MET GLY GLY GLU ALA PRO ASN GLN ALA LEU LEU          
SEQRES   2 D  331  ARG ILE LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL          
SEQRES   3 D  331  LEU GLY SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU          
SEQRES   4 D  331  TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA          
SEQRES   5 D  331  ILE LYS GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN          
SEQRES   6 D  331  LYS GLU ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL          
SEQRES   7 D  331  ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU          
SEQRES   8 D  331  THR SER THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE          
SEQRES   9 D  331  GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN          
SEQRES  10 D  331  ILE GLY SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE          
SEQRES  11 D  331  ALA LYS GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL          
SEQRES  12 D  331  HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR          
SEQRES  13 D  331  PRO GLN HIS VAL LYS ILE THR ASP PHE GLY LEU ALA LYS          
SEQRES  14 D  331  LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY          
SEQRES  15 D  331  GLY LYS VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE          
SEQRES  16 D  331  LEU HIS ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER          
SEQRES  17 D  331  TYR GLY VAL THR VAL TRP GLU LEU MET THR PHE GLY SER          
SEQRES  18 D  331  LYS PRO TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER          
SEQRES  19 D  331  ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE          
SEQRES  20 D  331  CYS THR ILE ASP VAL TYR MET ILE MET VAL LYS CYS TRP          
SEQRES  21 D  331  MET ILE ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU          
SEQRES  22 D  331  ILE ILE GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG          
SEQRES  23 D  331  TYR LEU VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO          
SEQRES  24 D  331  SER PRO THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP          
SEQRES  25 D  331  GLU GLU ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR          
SEQRES  26 D  331  LEU ILE PRO GLN GLN GLY                                      
HET    1E8  A1101      33                                                       
HET    1E8  B1101      33                                                       
HET    1E8  C1101      33                                                       
HET     CL  C1102       1                                                       
HET     CL  C1103       1                                                       
HET    1E8  D1101      33                                                       
HET     CL  D1102       1                                                       
HETNAM     1E8 1-{(3R)-3-[4-AMINO-3-(4-PHENOXYPHENYL)-1H-PYRAZOLO[3,4-          
HETNAM   2 1E8  D]PYRIMIDIN-1-YL]PIPERIDIN-1-YL}PROP-2-EN-1-ONE                 
HETNAM      CL CHLORIDE ION                                                     
HETSYN     1E8 IMBRUVICA, PCI-32765                                             
FORMUL   5  1E8    4(C25 H24 N6 O2)                                             
FORMUL   8   CL    3(CL 1-)                                                     
FORMUL  12  HOH   *950(H2 O)                                                    
HELIX    1 AA1 ASN A  700  LEU A  704  5                                   5    
HELIX    2 AA2 LYS A  708  THR A  710  5                                   3    
HELIX    3 AA3 ALA A  755  ALA A  767  1                                  13    
HELIX    4 AA4 CYS A  797  HIS A  805  1                                   9    
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 GLY A  857  LEU A  862  1                                   6    
HELIX    8 AA8 PRO A  877  MET A  881  5                                   5    
HELIX    9 AA9 ALA A  882  ARG A  889  1                                   8    
HELIX   10 AB1 THR A  892  THR A  909  1                                  18    
HELIX   11 AB2 PRO A  919  SER A  921  5                                   3    
HELIX   12 AB3 GLU A  922  GLY A  930  1                                   9    
HELIX   13 AB4 THR A  940  TRP A  951  1                                  12    
HELIX   14 AB5 ASP A  954  ARG A  958  5                                   5    
HELIX   15 AB6 LYS A  960  ASP A  974  1                                  15    
HELIX   16 AB7 ASP A  974  LEU A  979  1                                   6    
HELIX   17 AB8 GLY A  983  MET A  987  5                                   5    
HELIX   18 AB9 SER A  991  ASP A 1003  1                                  13    
HELIX   19 AC1 ASN B  700  LEU B  704  5                                   5    
HELIX   20 AC2 LYS B  708  THR B  710  5                                   3    
HELIX   21 AC3 ASN B  756  SER B  768  1                                  13    
HELIX   22 AC4 CYS B  797  HIS B  805  1                                   9    
HELIX   23 AC5 GLY B  810  ARG B  831  1                                  22    
HELIX   24 AC6 ALA B  839  ARG B  841  5                                   3    
HELIX   25 AC7 GLY B  857  LEU B  862  1                                   6    
HELIX   26 AC8 PRO B  877  MET B  881  5                                   5    
HELIX   27 AC9 ALA B  882  ARG B  889  1                                   8    
HELIX   28 AD1 THR B  892  THR B  909  1                                  18    
HELIX   29 AD2 PRO B  919  SER B  921  5                                   3    
HELIX   30 AD3 GLU B  922  GLY B  930  1                                   9    
HELIX   31 AD4 THR B  940  TRP B  951  1                                  12    
HELIX   32 AD5 ASP B  954  ARG B  958  5                                   5    
HELIX   33 AD6 LYS B  960  ASP B  974  1                                  15    
HELIX   34 AD7 ASP B  974  LEU B  979  1                                   6    
HELIX   35 AD8 SER B  991  ASP B 1003  1                                  13    
HELIX   36 AD9 ASN C  700  LEU C  704  5                                   5    
HELIX   37 AE1 LYS C  708  THR C  710  5                                   3    
HELIX   38 AE2 ALA C  755  SER C  768  1                                  14    
HELIX   39 AE3 CYS C  797  HIS C  805  1                                   9    
HELIX   40 AE4 GLY C  810  ARG C  831  1                                  22    
HELIX   41 AE5 ALA C  839  ARG C  841  5                                   3    
HELIX   42 AE6 GLY C  857  LEU C  862  1                                   6    
HELIX   43 AE7 PRO C  877  MET C  881  5                                   5    
HELIX   44 AE8 ALA C  882  ARG C  889  1                                   8    
HELIX   45 AE9 THR C  892  THR C  909  1                                  18    
HELIX   46 AF1 PRO C  919  SER C  921  5                                   3    
HELIX   47 AF2 GLU C  922  GLY C  930  1                                   9    
HELIX   48 AF3 THR C  940  TRP C  951  1                                  12    
HELIX   49 AF4 ASP C  954  ARG C  958  5                                   5    
HELIX   50 AF5 LYS C  960  ASP C  974  1                                  15    
HELIX   51 AF6 ASP C  974  LEU C  979  1                                   6    
HELIX   52 AF7 GLY C  983  MET C  987  5                                   5    
HELIX   53 AF8 SER C  991  ASP C 1003  1                                  13    
HELIX   54 AF9 ASN D  700  LEU D  704  5                                   5    
HELIX   55 AG1 LYS D  708  THR D  710  5                                   3    
HELIX   56 AG2 SER D  752  VAL D  769  1                                  18    
HELIX   57 AG3 CYS D  797  HIS D  805  1                                   9    
HELIX   58 AG4 LYS D  806  ILE D  809  5                                   4    
HELIX   59 AG5 GLY D  810  ARG D  831  1                                  22    
HELIX   60 AG6 ALA D  839  ARG D  841  5                                   3    
HELIX   61 AG7 GLY D  857  LEU D  862  1                                   6    
HELIX   62 AG8 PRO D  877  MET D  881  5                                   5    
HELIX   63 AG9 ALA D  882  ARG D  889  1                                   8    
HELIX   64 AH1 THR D  892  THR D  909  1                                  18    
HELIX   65 AH2 PRO D  919  SER D  921  5                                   3    
HELIX   66 AH3 GLU D  922  LYS D  929  1                                   8    
HELIX   67 AH4 THR D  940  TRP D  951  1                                  12    
HELIX   68 AH5 ASP D  954  ARG D  958  5                                   5    
HELIX   69 AH6 LYS D  960  ASP D  974  1                                  15    
HELIX   70 AH7 ASP D  974  LEU D  979  1                                   6    
HELIX   71 AH8 SER D  991  ASP D 1003  1                                  13    
SHEET    1 AA1 6 ARG A 705  ILE A 706  0                                        
SHEET    2 AA1 6 GLY A 779  LEU A 782  1  O  ILE A 780   N  ARG A 705           
SHEET    3 AA1 6 VAL A 786  MET A 790 -1  O  ILE A 789   N  GLY A 779           
SHEET    4 AA1 6 ILE A 740  LEU A 747 -1  N  LYS A 745   O  LEU A 788           
SHEET    5 AA1 6 GLY A 724  TRP A 731 -1  N  TYR A 727   O  ILE A 744           
SHEET    6 AA1 6 PHE A 712  SER A 720 -1  N  GLY A 719   O  VAL A 726           
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           
SHEET    1 AA3 6 ARG B 705  ILE B 706  0                                        
SHEET    2 AA3 6 GLY B 779  LEU B 782  1  O  ILE B 780   N  ARG B 705           
SHEET    3 AA3 6 VAL B 786  MET B 790 -1  O  ILE B 789   N  GLY B 779           
SHEET    4 AA3 6 ILE B 740  LEU B 747 -1  N  ALA B 743   O  MET B 790           
SHEET    5 AA3 6 GLY B 724  TRP B 731 -1  N  TRP B 731   O  ILE B 740           
SHEET    6 AA3 6 PHE B 712  SER B 720 -1  N  GLY B 719   O  VAL B 726           
SHEET    1 AA4 2 VAL B 843  THR B 847  0                                        
SHEET    2 AA4 2 HIS B 850  ILE B 853 -1  O  LYS B 852   N  LEU B 844           
SHEET    1 AA5 6 ARG C 705  ILE C 706  0                                        
SHEET    2 AA5 6 GLY C 779  LEU C 782  1  O  ILE C 780   N  ARG C 705           
SHEET    3 AA5 6 VAL C 786  MET C 790 -1  O  ILE C 789   N  GLY C 779           
SHEET    4 AA5 6 ILE C 740  LEU C 747 -1  N  LYS C 745   O  LEU C 788           
SHEET    5 AA5 6 GLY C 724  TRP C 731 -1  N  TRP C 731   O  ILE C 740           
SHEET    6 AA5 6 PHE C 712  SER C 720 -1  N  GLY C 719   O  VAL C 726           
SHEET    1 AA6 2 VAL C 843  THR C 847  0                                        
SHEET    2 AA6 2 HIS C 850  ILE C 853 -1  O  LYS C 852   N  LEU C 844           
SHEET    1 AA7 6 ARG D 705  ILE D 706  0                                        
SHEET    2 AA7 6 GLY D 779  CYS D 781  1  O  ILE D 780   N  ARG D 705           
SHEET    3 AA7 6 GLN D 787  MET D 790 -1  O  ILE D 789   N  GLY D 779           
SHEET    4 AA7 6 ILE D 740  LEU D 747 -1  N  LYS D 745   O  LEU D 788           
SHEET    5 AA7 6 GLY D 724  TRP D 731 -1  N  GLY D 729   O  VAL D 742           
SHEET    6 AA7 6 PHE D 712  SER D 720 -1  N  LYS D 716   O  LYS D 728           
SHEET    1 AA8 2 VAL D 843  THR D 847  0                                        
SHEET    2 AA8 2 HIS D 850  ILE D 853 -1  O  LYS D 852   N  LEU D 844           
LINK         SG  CYS A 797                 CAA 1E8 A1101     1555   1555  1.83  
LINK         SG  CYS B 797                 CAA 1E8 B1101     1555   1555  1.83  
LINK         SG  CYS C 797                 CAA 1E8 C1101     1555   1555  1.83  
LINK         SG  CYS D 797                 CAA 1E8 D1101     1555   1555  1.82  
SITE     1 AC1 14 LEU A 718  GLY A 719  ALA A 743  MET A 766                    
SITE     2 AC1 14 LEU A 788  MET A 790  GLN A 791  MET A 793                    
SITE     3 AC1 14 CYS A 797  ARG A 841  THR A 854  ASP A 855                    
SITE     4 AC1 14 PHE A 856  HOH A1314                                          
SITE     1 AC2  3 ILE C 953  ALA C 955  HOH C1411                               
SITE     1 AC3  2 ARG D 932  TRP D 951                                          
SITE     1 AC4 19 ALA B 743  LYS B 745  MET B 766  MET B 790                    
SITE     2 AC4 19 GLN B 791  MET B 793  GLY B 796  LEU B 798                    
SITE     3 AC4 19 LEU B 799  ASP B 800  TYR B 801  ARG B 841                    
SITE     4 AC4 19 VAL B 843  THR B 854  ASP B 855  HOH B1255                    
SITE     5 AC4 19 HOH B1257  HOH B1307  HOH B1345                               
SITE     1 AC5 18 VAL C 726  ALA C 743  MET C 766  MET C 790                    
SITE     2 AC5 18 GLN C 791  MET C 793  GLY C 796  LEU C 798                    
SITE     3 AC5 18 LEU C 799  ASP C 800  TYR C 801  ARG C 841                    
SITE     4 AC5 18 VAL C 843  THR C 854  ASP C 855  PHE C 856                    
SITE     5 AC5 18 HOH C1268  HOH C1290                                          
SITE     1 AC6 17 VAL D 726  ALA D 743  LYS D 745  MET D 766                    
SITE     2 AC6 17 MET D 790  GLN D 791  MET D 793  GLY D 796                    
SITE     3 AC6 17 LEU D 798  LEU D 799  ASP D 800  TYR D 801                    
SITE     4 AC6 17 ARG D 841  VAL D 843  THR D 854  ASP D 855                    
SITE     5 AC6 17 HOH D1234                                                     
CRYST1  168.194   74.385  120.460  90.00 118.32  90.00 C 1 2 1      16          
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      0.005946  0.000000  0.003204        0.00000                         
SCALE2      0.000000  0.013444  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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