GenomeNet

Database: PDB
Entry: 5X2F
LinkDB: 5X2F
Original site: 5X2F 
HEADER    TRANSFERASE                             31-JAN-17   5X2F              
TITLE     CRYSTAL STRUCTURE OF EGFR 696-1022 T790M/V948R IN COMPLEX WITH SKLB(6)
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 696-1022;                                     
COMPND   5 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE    
COMPND   6 ERBB-1;                                                              
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 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;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    EGFR, T790M, V948R, SKLB, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.YUN                                                               
REVDAT   3   11-APR-18 5X2F    1       JRNL                                     
REVDAT   2   21-FEB-18 5X2F    1       JRNL                                     
REVDAT   1   07-FEB-18 5X2F    0                                                
JRNL        AUTH   S.J.ZHU,P.ZHAO,J.YANG,R.MA,X.E.YAN,S.Y.YANG,J.W.YANG,C.H.YUN 
JRNL        TITL   STRUCTURAL INSIGHTS INTO DRUG DEVELOPMENT STRATEGY TARGETING 
JRNL        TITL 2 EGFR T790M/C797S.                                            
JRNL        REF    ONCOTARGET                    V.   9 13652 2018              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   29568384                                                     
JRNL        DOI    10.18632/ONCOTARGET.24113                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 55505                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2833                            
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 39.2380 -  5.9651    0.99     3004   155  0.1765 0.2548        
REMARK   3     2  5.9651 -  4.7373    1.00     2946   191  0.1749 0.2213        
REMARK   3     3  4.7373 -  4.1392    1.00     2955   170  0.1534 0.1778        
REMARK   3     4  4.1392 -  3.7611    1.00     2943   152  0.1702 0.1959        
REMARK   3     5  3.7611 -  3.4917    1.00     2954   157  0.1809 0.2108        
REMARK   3     6  3.4917 -  3.2859    0.99     2930   164  0.1962 0.2357        
REMARK   3     7  3.2859 -  3.1214    0.97     2824   171  0.2113 0.2571        
REMARK   3     8  3.1214 -  2.9856    0.95     2809   141  0.2221 0.2790        
REMARK   3     9  2.9856 -  2.8707    0.92     2744   151  0.2282 0.2453        
REMARK   3    10  2.8707 -  2.7717    0.89     2613   140  0.2340 0.2336        
REMARK   3    11  2.7717 -  2.6850    0.86     2531   129  0.2467 0.2864        
REMARK   3    12  2.6850 -  2.6083    0.84     2492   136  0.2392 0.2925        
REMARK   3    13  2.6083 -  2.5396    0.83     2427   122  0.2521 0.2796        
REMARK   3    14  2.5396 -  2.4777    0.82     2407   123  0.2570 0.3016        
REMARK   3    15  2.4777 -  2.4214    0.81     2391   123  0.2661 0.2840        
REMARK   3    16  2.4214 -  2.3698    0.81     2384   116  0.2576 0.3150        
REMARK   3    17  2.3698 -  2.3224    0.81     2380   117  0.2550 0.2526        
REMARK   3    18  2.3224 -  2.2786    0.80     2326   147  0.2646 0.3213        
REMARK   3    19  2.2786 -  2.2379    0.79     2329   123  0.2752 0.3126        
REMARK   3    20  2.2379 -  2.2000    0.76     2283   105  0.2731 0.2847        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.610           
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      :  0.014          10080                                  
REMARK   3   ANGLE     :  1.325          13655                                  
REMARK   3   CHIRALITY :  0.125           1519                                  
REMARK   3   PLANARITY :  0.013           1710                                  
REMARK   3   DIHEDRAL  : 20.054           3815                                  
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 5X2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002819.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
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 : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55540                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 89.4                               
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  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS 5.0, 22.5% PEG 3350, 5MM   
REMARK 280  TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       51.29650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     SER A   693                                                      
REMARK 465     THR A   694                                                      
REMARK 465     SER A   695                                                      
REMARK 465     GLY A   696                                                      
REMARK 465     GLU A   697                                                      
REMARK 465     ALA A   698                                                      
REMARK 465     PRO A   699                                                      
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     ASP A  1008                                                      
REMARK 465     ASP A  1009                                                      
REMARK 465     GLU A  1015                                                      
REMARK 465     TYR A  1016                                                      
REMARK 465     LEU A  1017                                                      
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     SER B   693                                                      
REMARK 465     THR B   694                                                      
REMARK 465     SER B   695                                                      
REMARK 465     GLY B   696                                                      
REMARK 465     GLU B   697                                                      
REMARK 465     ALA B   698                                                      
REMARK 465     VAL B  1011                                                      
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     SER C   693                                                      
REMARK 465     THR C   694                                                      
REMARK 465     SER C   695                                                      
REMARK 465     GLY C   696                                                      
REMARK 465     GLU C   697                                                      
REMARK 465     ALA C   698                                                      
REMARK 465     PRO C   699                                                      
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     LYS C   875                                                      
REMARK 465     GLU C  1015                                                      
REMARK 465     TYR C  1016                                                      
REMARK 465     LEU C  1017                                                      
REMARK 465     ILE C  1018                                                      
REMARK 465     PRO C  1019                                                      
REMARK 465     GLN C  1020                                                      
REMARK 465     GLN C  1021                                                      
REMARK 465     GLY C  1022                                                      
REMARK 465     GLY D   692                                                      
REMARK 465     SER D   693                                                      
REMARK 465     THR D   694                                                      
REMARK 465     SER D   695                                                      
REMARK 465     GLY D   696                                                      
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     MET D  1007                                                      
REMARK 465     ASP D  1008                                                      
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 754    CG   CD   CE   NZ                                   
REMARK 470     ARG A 832    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 875    CG   CD   CE   NZ                                   
REMARK 470     HIS A 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A1010    CG1  CG2                                            
REMARK 470     ASP A1012    CG   OD1  OD2                                       
REMARK 470     ASP A1014    CG   OD1  OD2                                       
REMARK 470     LYS B 713    CG   CD   CE   NZ                                   
REMARK 470     GLU B 734    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 749    CG   CD   OE1  OE2                                  
REMARK 470     THR B 751    OG1  CG2                                            
REMARK 470     GLU B 758    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 807    CG   OD1  OD2                                       
REMARK 470     GLU B 865    CD   OE1  OE2                                       
REMARK 470     LYS B 867    CG   CD   CE   NZ                                   
REMARK 470     LYS B 913    NZ                                                  
REMARK 470     LYS B 949    CE   NZ                                             
REMARK 470     LYS B 970    CE   NZ                                             
REMARK 470     HIS B 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B1009    CG   OD1  OD2                                       
REMARK 470     VAL B1010    CG1  CG2                                            
REMARK 470     PHE C 723    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 748    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 749    CG   CD   OE1  OE2                                  
REMARK 470     SER C 784    OG                                                  
REMARK 470     THR C 785    OG1  CG2                                            
REMARK 470     ASN C 808    OD1  ND2                                            
REMARK 470     LYS C 960    CE   NZ                                             
REMARK 470     ARG C 986    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 988    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL C1010    CG1  CG2                                            
REMARK 470     GLU D 697    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 700    CG   OD1  ND2                                       
REMARK 470     GLN D 701    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 748    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D 749    CD   OE1  OE2                                       
REMARK 470     SER D 752    OG                                                  
REMARK 470     LYS D 757    CG   CD   CE   NZ                                   
REMARK 470     THR D 783    OG1  CG2                                            
REMARK 470     GLU D 865    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 875    CG   CD   CE   NZ                                   
REMARK 470     GLN D 982    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 986    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP D1009    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 D 753   C   -  N   -  CD  ANGL. DEV. = -17.1 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    THR A 783     -122.73   -131.00                                   
REMARK 500    HIS A 805       50.75   -105.29                                   
REMARK 500    ARG A 836      -11.58     82.94                                   
REMARK 500    ASP A 837       36.40   -142.16                                   
REMARK 500    THR B 783     -146.96   -118.40                                   
REMARK 500    ARG B 836      -11.42     82.16                                   
REMARK 500    ASP B 837       23.89   -142.24                                   
REMARK 500    ASP B 855       16.33     80.54                                   
REMARK 500    ASP B1003       72.46   -150.21                                   
REMARK 500    ALA C 722     -128.59     62.95                                   
REMARK 500    SER C 784      -45.22   -131.91                                   
REMARK 500    ARG C 836       -3.44     79.01                                   
REMARK 500    ASP C 837       43.14   -156.46                                   
REMARK 500    SER D 784      -84.21   -126.33                                   
REMARK 500    ARG D 836      -10.18     82.78                                   
REMARK 500    ASP D 837       36.03   -142.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  749     ALA A  750                  127.79                    
REMARK 500 THR D  751     SER D  752                 -143.93                    
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 B1292        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH D1302        DISTANCE =  5.89 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU C 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7XU D 1101                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5X26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X27   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X28   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X2C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X2K   RELATED DB: PDB                                   
DBREF  5X2F A  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5X2F B  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5X2F C  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
DBREF  5X2F D  696  1022  UNP    P00533   EGFR_HUMAN     696   1022             
SEQADV 5X2F GLY A  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER A  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F THR A  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER A  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5X2F ARG A  948  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQADV 5X2F GLY B  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER B  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F THR B  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER B  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F MET B  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5X2F ARG B  948  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQADV 5X2F GLY C  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER C  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F THR C  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER C  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F MET C  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5X2F ARG C  948  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQADV 5X2F GLY D  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER D  693  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F THR D  694  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F SER D  695  UNP  P00533              EXPRESSION TAG                 
SEQADV 5X2F MET D  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5X2F ARG D  948  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQRES   1 A  331  GLY SER THR SER 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 ARG 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 SER THR SER 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 ARG 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 SER THR SER 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 ARG 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 SER THR SER 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 ARG 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    7XU  A3001      36                                                       
HET    7XU  B1101      36                                                       
HET    7XU  C1101      36                                                       
HET    7XU  D1101      36                                                       
HETNAM     7XU 9-CYCLOHEXYL-N2-[4-(4-METHYLPIPERAZIN-1-YL)PHENYL]-N8-           
HETNAM   2 7XU  PHENYL-PURINE-2,8-DIAMINE                                       
FORMUL   5  7XU    4(C28 H34 N8)                                                
FORMUL   9  HOH   *380(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  SER A  768  1                                  14    
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  GLY A  930  1                                  12    
HELIX   12 AB3 THR A  940  TRP A  951  1                                  12    
HELIX   13 AB4 ASP A  954  ARG A  958  5                                   5    
HELIX   14 AB5 LYS A  960  ASP A  974  1                                  15    
HELIX   15 AB6 ASP A  974  LEU A  979  1                                   6    
HELIX   16 AB7 SER A  991  ASP A 1003  1                                  13    
HELIX   17 AB8 LYS B  708  THR B  710  5                                   3    
HELIX   18 AB9 ALA B  755  SER B  768  1                                  14    
HELIX   19 AC1 CYS B  797  HIS B  805  1                                   9    
HELIX   20 AC2 GLY B  810  ARG B  831  1                                  22    
HELIX   21 AC3 ALA B  839  ARG B  841  5                                   3    
HELIX   22 AC4 GLY B  857  GLY B  863  1                                   7    
HELIX   23 AC5 GLU B  865  HIS B  870  1                                   6    
HELIX   24 AC6 PRO B  877  MET B  881  5                                   5    
HELIX   25 AC7 ALA B  882  ARG B  889  1                                   8    
HELIX   26 AC8 THR B  892  THR B  909  1                                  18    
HELIX   27 AC9 PRO B  919  SER B  921  5                                   3    
HELIX   28 AD1 GLU B  922  LYS B  929  1                                   8    
HELIX   29 AD2 THR B  940  TRP B  951  1                                  12    
HELIX   30 AD3 ASP B  954  ARG B  958  5                                   5    
HELIX   31 AD4 LYS B  960  ASP B  974  1                                  15    
HELIX   32 AD5 ASP B  974  LEU B  979  1                                   6    
HELIX   33 AD6 SER B  991  ASP B 1003  1                                  13    
HELIX   34 AD7 ASN C  700  LEU C  704  5                                   5    
HELIX   35 AD8 LYS C  708  THR C  710  5                                   3    
HELIX   36 AD9 SER C  752  SER C  768  1                                  17    
HELIX   37 AE1 CYS C  797  HIS C  805  1                                   9    
HELIX   38 AE2 GLY C  810  ARG C  831  1                                  22    
HELIX   39 AE3 ALA C  839  ARG C  841  5                                   3    
HELIX   40 AE4 GLY C  857  LEU C  862  1                                   6    
HELIX   41 AE5 PRO C  877  MET C  881  5                                   5    
HELIX   42 AE6 ALA C  882  ARG C  889  1                                   8    
HELIX   43 AE7 THR C  892  THR C  909  1                                  18    
HELIX   44 AE8 PRO C  919  LYS C  929  1                                  11    
HELIX   45 AE9 THR C  940  TRP C  951  1                                  12    
HELIX   46 AF1 ASP C  954  ARG C  958  5                                   5    
HELIX   47 AF2 LYS C  960  ASP C  974  1                                  15    
HELIX   48 AF3 ASP C  974  LEU C  979  1                                   6    
HELIX   49 AF4 SER C  991  ASP C 1003  1                                  13    
HELIX   50 AF5 ALA D  698  LEU D  704  1                                   7    
HELIX   51 AF6 ALA D  755  VAL D  769  1                                  15    
HELIX   52 AF7 CYS D  797  HIS D  805  1                                   9    
HELIX   53 AF8 LYS D  806  ILE D  809  5                                   4    
HELIX   54 AF9 GLY D  810  ARG D  831  1                                  22    
HELIX   55 AG1 ALA D  839  ARG D  841  5                                   3    
HELIX   56 AG2 GLY D  857  GLY D  863  1                                   7    
HELIX   57 AG3 PRO D  877  MET D  881  5                                   5    
HELIX   58 AG4 ALA D  882  ARG D  889  1                                   8    
HELIX   59 AG5 THR D  892  THR D  909  1                                  18    
HELIX   60 AG6 PRO D  919  SER D  921  5                                   3    
HELIX   61 AG7 GLU D  922  LYS D  929  1                                   8    
HELIX   62 AG8 THR D  940  TRP D  951  1                                  12    
HELIX   63 AG9 ASP D  954  ARG D  958  5                                   5    
HELIX   64 AH1 LYS D  960  ASP D  974  1                                  15    
HELIX   65 AH2 ASP D  974  LEU D  979  1                                   6    
HELIX   66 AH3 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  LEU A 747   O  VAL A 786           
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  LEU A 718   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  LYS B 713   O  LEU B 730           
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  CYS C 781  1  O  ILE C 780   N  ARG C 705           
SHEET    3 AA5 6 GLN C 787  GLN C 791 -1  O  ILE C 789   N  GLY C 779           
SHEET    4 AA5 6 ILE C 740  GLU C 746 -1  N  ALA C 743   O  MET C 790           
SHEET    5 AA5 6 GLY C 724  TRP C 731 -1  N  TYR C 727   O  ILE C 744           
SHEET    6 AA5 6 PHE C 712  GLY C 721 -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  ALA D 743   O  MET D 790           
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  LEU D 718   O  VAL D 726           
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           
SITE     1 AC1 12 ALA A 743  LYS A 745  MET A 790  GLN A 791                    
SITE     2 AC1 12 LEU A 792  MET A 793  PRO A 794  GLY A 796                    
SITE     3 AC1 12 LEU A 844  ASP A 855  HOH A3126  HOH A3141                    
SITE     1 AC2 10 LEU B 718  LYS B 745  MET B 790  GLN B 791                    
SITE     2 AC2 10 LEU B 792  MET B 793  PRO B 794  GLY B 796                    
SITE     3 AC2 10 ASP B 855  HOH B1221                                          
SITE     1 AC3 13 LEU C 718  GLY C 719  VAL C 726  ALA C 743                    
SITE     2 AC3 13 LYS C 745  MET C 790  GLN C 791  LEU C 792                    
SITE     3 AC3 13 MET C 793  PRO C 794  GLY C 796  ASP C 855                    
SITE     4 AC3 13 HOH C1227                                                     
SITE     1 AC4 13 ARG B 962  LEU D 718  ALA D 743  LYS D 745                    
SITE     2 AC4 13 MET D 790  GLN D 791  LEU D 792  MET D 793                    
SITE     3 AC4 13 PRO D 794  GLY D 796  LEU D 844  ASP D 855                    
SITE     4 AC4 13 HOH D1256                                                     
CRYST1   71.499  102.593   87.026  90.00 102.64  90.00 P 1 21 1      8          
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      0.013986  0.000000  0.003136        0.00000                         
SCALE2      0.000000  0.009747  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011776        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system