GenomeNet

Database: PDB
Entry: 5D41
LinkDB: 5D41
Original site: 5D41 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-AUG-15   5D41              
TITLE     EGFR KINASE DOMAIN IN COMPLEX WITH MUTANT SELECTIVE ALLOSTERIC        
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE    
COMPND   5 ERBB-1;                                                              
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EGFR, ERBB, ERBB1, HER1;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PTRIEX 1.1                                
KEYWDS    ALLOSTERIC INHIBITOR, EGFR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-H.YUN,E.PARK,M.J.ECK                                               
REVDAT   2   18-APR-18 5D41    1       JRNL   REMARK                            
REVDAT   1   08-JUN-16 5D41    0                                                
JRNL        AUTH   Y.JIA,C.H.YUN,E.PARK,D.ERCAN,M.MANUIA,J.JUAREZ,C.XU,K.RHEE,  
JRNL        AUTH 2 T.CHEN,H.ZHANG,S.PALAKURTHI,J.JANG,G.LELAIS,M.DIDONATO,      
JRNL        AUTH 3 B.BURSULAYA,P.Y.MICHELLYS,R.EPPLE,T.H.MARSILJE,M.MCNEILL,    
JRNL        AUTH 4 W.LU,J.HARRIS,S.BENDER,K.K.WONG,P.A.JANNE,M.J.ECK            
JRNL        TITL   OVERCOMING EGFR(T790M) AND EGFR(C797S) RESISTANCE WITH       
JRNL        TITL 2 MUTANT-SELECTIVE ALLOSTERIC INHIBITORS.                      
JRNL        REF    NATURE                        V. 534   129 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27251290                                                     
JRNL        DOI    10.1038/NATURE17960                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33348                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1685                            
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 42.2442 -  5.2854    0.98     2742   145  0.1594 0.1638        
REMARK   3     2  5.2854 -  4.1964    0.99     2703   141  0.1471 0.1864        
REMARK   3     3  4.1964 -  3.6663    0.99     2683   168  0.1488 0.1938        
REMARK   3     4  3.6663 -  3.3312    0.99     2667   139  0.1667 0.2053        
REMARK   3     5  3.3312 -  3.0925    0.98     2659   135  0.1771 0.1955        
REMARK   3     6  3.0925 -  2.9103    0.98     2640   138  0.1853 0.2255        
REMARK   3     7  2.9103 -  2.7645    0.98     2624   144  0.1894 0.2148        
REMARK   3     8  2.7645 -  2.6442    0.98     2639   156  0.1911 0.2795        
REMARK   3     9  2.6442 -  2.5424    0.98     2612   134  0.2078 0.2215        
REMARK   3    10  2.5424 -  2.4547    0.97     2619   122  0.2081 0.2526        
REMARK   3    11  2.4547 -  2.3780    0.96     2564   127  0.2197 0.2412        
REMARK   3    12  2.3780 -  2.3100    0.94     2511   136  0.2379 0.2795        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.590           
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      :  0.008           5032                                  
REMARK   3   ANGLE     :  1.134           6830                                  
REMARK   3   CHIRALITY :  0.045            757                                  
REMARK   3   PLANARITY :  0.006            854                                  
REMARK   3   DIHEDRAL  : 15.554           1887                                  
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 5D41 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212312.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-002                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.310                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: 2GS7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS, PEG3350, PH 5.5, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       77.56650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.24850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       77.56650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       36.24850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2263  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     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   859                                                      
REMARK 465     LYS A   860                                                      
REMARK 465     LEU A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     GLY A   863                                                      
REMARK 465     ALA A   864                                                      
REMARK 465     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     LYS A   875                                                      
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     PRO B   699                                                      
REMARK 465     ASN B   700                                                      
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     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 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     GLU A 734    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 737    CG   CD   CE   NZ                                   
REMARK 470     VAL A1010    CG1  CG2                                            
REMARK 470     LYS B 754    CG   CD   CE   NZ                                   
REMARK 470     LEU B 858    CD1                                                 
REMARK 470     LYS B 860    CG   CD   CE   NZ                                   
REMARK 470     LEU B 861    CG   CD1  CD2                                       
REMARK 470     LEU B 862    CG   CD1  CD2                                       
REMARK 470     HIS B 988    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O1B  ANP B  2001     O    HOH B  2101              1.85            
REMARK 500   O    HOH B  2247     O    HOH B  2271              1.88            
REMARK 500   O    HOH A  1301     O    HOH A  1390              1.91            
REMARK 500   O    HOH B  2181     O    HOH B  2242              1.92            
REMARK 500   O    HOH A  1347     O    HOH A  1398              1.93            
REMARK 500   O    HOH A  1354     O    HOH A  1371              1.93            
REMARK 500   O    HOH B  2273     O    HOH B  2276              1.94            
REMARK 500   O    HOH B  2212     O    HOH B  2272              1.94            
REMARK 500   NH1  ARG A   986     O    HOH A  1201              1.95            
REMARK 500   O    HOH B  2236     O    HOH B  2267              1.96            
REMARK 500   O    HOH B  2150     O    HOH B  2264              1.96            
REMARK 500   O    PRO B   733     O    HOH B  2102              2.00            
REMARK 500   O    HOH A  1349     O    HOH A  1402              2.00            
REMARK 500   OE1  GLU A   922     O    HOH A  1202              2.02            
REMARK 500   O    HOH A  1403     O    HOH A  1409              2.03            
REMARK 500   O    HOH B  2182     O    HOH B  2260              2.04            
REMARK 500   OE2  GLU B   985     O    HOH B  2103              2.06            
REMARK 500   O    HOH B  2249     O    HOH B  2269              2.06            
REMARK 500   O    HOH B  2180     O    HOH B  2251              2.10            
REMARK 500   OD2  ASP B  1006     O    HOH B  2104              2.11            
REMARK 500   O    HOH A  1208     O    HOH A  1342              2.11            
REMARK 500   NH2  ARG B   973     O    HOH B  2105              2.12            
REMARK 500   NH2  ARG A   962     O    HOH A  1203              2.14            
REMARK 500   OE1  GLU B  1004     O    HOH B  2106              2.14            
REMARK 500   OE1  GLN A   701     O    HOH A  1204              2.14            
REMARK 500   OE2  GLU B   749     O    HOH B  2107              2.14            
REMARK 500   O    HOH A  1318     O    HOH A  1329              2.15            
REMARK 500   O    HOH A  1292     O    HOH A  1393              2.15            
REMARK 500   O    THR A   783     O    HOH A  1205              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1378     O    HOH B  2190     4455     1.85            
REMARK 500   O    HOH A  1355     O    HOH B  2203     4445     2.14            
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    ASP A 807       44.25   -104.32                                   
REMARK 500    ARG A 836      -14.31     78.51                                   
REMARK 500    ASP A 837       38.76   -145.38                                   
REMARK 500    ASP A1003       75.94   -150.30                                   
REMARK 500    ILE B 715      -75.51   -106.51                                   
REMARK 500    THR B 783     -125.86   -115.02                                   
REMARK 500    ARG B 836      -10.72     80.95                                   
REMARK 500    ASP B 837       42.77   -145.50                                   
REMARK 500    ASP B1003       74.37   -153.15                                   
REMARK 500    MET B1007      144.57   -170.28                                   
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 A1415        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH B2283        DISTANCE =  6.48 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 842   OD1                                                    
REMARK 620 2 ASP A 855   OD2  89.4                                              
REMARK 620 3 ANP A1102   O1B  95.2 175.3                                        
REMARK 620 4 ANP A1102   O2A 170.9  83.4  92.1                                  
REMARK 620 5 HOH A1212   O    95.5  93.3  85.5  90.6                            
REMARK 620 6 HOH A1304   O    83.6  87.0  94.4  90.4 179.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2000  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 842   OD1                                                    
REMARK 620 2 ASP B 855   OD2  86.9                                              
REMARK 620 3 ANP B2001   O2G 116.2 117.4                                        
REMARK 620 4 HOH B2192   O    75.8  81.2 157.1                                  
REMARK 620 5 ANP B2001   O2B  89.2 166.5  75.9  85.3                            
REMARK 620 6 ANP B2001   O1A 159.3  84.4  84.5  84.3  94.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 57N A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 2001                
DBREF  5D41 A  693  1022  UNP    P00533   EGFR_HUMAN     693   1022             
DBREF  5D41 B  693  1022  UNP    P00533   EGFR_HUMAN     693   1022             
SEQADV 5D41 GLY A  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5D41 SER A  693  UNP  P00533    THR   693 EXPRESSION TAG                 
SEQADV 5D41 THR A  694  UNP  P00533    PRO   694 EXPRESSION TAG                 
SEQADV 5D41 MET A  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5D41 ARG A  948  UNP  P00533    VAL   948 ENGINEERED MUTATION            
SEQADV 5D41 GLY B  692  UNP  P00533              EXPRESSION TAG                 
SEQADV 5D41 SER B  693  UNP  P00533    THR   693 EXPRESSION TAG                 
SEQADV 5D41 THR B  694  UNP  P00533    PRO   694 EXPRESSION TAG                 
SEQADV 5D41 MET B  790  UNP  P00533    THR   790 ENGINEERED MUTATION            
SEQADV 5D41 ARG B  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                                      
HET     MG  A1101       1                                                       
HET    ANP  A1102      31                                                       
HET    57N  A1103      25                                                       
HET     MG  B2000       1                                                       
HET    ANP  B2001      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     57N (2R)-2-(1-OXO-1,3-DIHYDRO-2H-ISOINDOL-2-YL)-2-PHENYL-N-          
HETNAM   2 57N  (1,3-THIAZOL-2-YL)ACETAMIDE                                     
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   5  57N    C19 H15 N3 O2 S                                              
FORMUL   8  HOH   *398(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 SER A  752  ALA A  767  1                                  16    
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 PRO A  877  MET A  881  5                                   5    
HELIX    8 AA8 ALA A  882  ARG A  889  1                                   8    
HELIX    9 AA9 THR A  892  THR A  909  1                                  18    
HELIX   10 AB1 PRO A  919  SER A  921  5                                   3    
HELIX   11 AB2 GLU A  922  LYS A  929  1                                   8    
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 GLY A  983  MET A  987  5                                   5    
HELIX   17 AB8 SER A  991  ASP A 1003  1                                  13    
HELIX   18 AB9 LYS B  708  THR B  710  5                                   3    
HELIX   19 AC1 SER B  752  VAL B  769  1                                  18    
HELIX   20 AC2 CYS B  797  HIS B  805  1                                   9    
HELIX   21 AC3 GLY B  810  ARG B  831  1                                  22    
HELIX   22 AC4 ALA B  839  ARG B  841  5                                   3    
HELIX   23 AC5 PRO B  877  MET B  881  5                                   5    
HELIX   24 AC6 ALA B  882  ARG B  889  1                                   8    
HELIX   25 AC7 THR B  892  THR B  909  1                                  18    
HELIX   26 AC8 PRO B  919  SER B  921  5                                   3    
HELIX   27 AC9 GLU B  922  LYS B  929  1                                   8    
HELIX   28 AD1 THR B  940  TRP B  951  1                                  12    
HELIX   29 AD2 ASP B  954  ARG B  958  5                                   5    
HELIX   30 AD3 LYS B  960  ASP B  974  1                                  15    
HELIX   31 AD4 PRO B  975  TYR B  978  5                                   4    
HELIX   32 AD5 GLY B  983  MET B  987  5                                   5    
HELIX   33 AD6 SER B  991  ASP B 1003  1                                  13    
SHEET    1 AA1 6 ARG A 705  ILE A 706  0                                        
SHEET    2 AA1 6 GLY A 779  CYS A 781  1  O  ILE A 780   N  ARG A 705           
SHEET    3 AA1 6 GLN A 787  MET A 790 -1  O  GLN A 787   N  CYS A 781           
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  LYS A 716   O  LYS A 728           
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  GLN B 791 -1  O  GLN B 787   N  CYS B 781           
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  LEU B 718   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           
LINK         OD1 ASN A 842                MG    MG A1101     1555   1555  2.05  
LINK         OD2 ASP A 855                MG    MG A1101     1555   1555  2.01  
LINK         OD1 ASN B 842                MG    MG B2000     1555   1555  2.13  
LINK         OD2 ASP B 855                MG    MG B2000     1555   1555  2.07  
LINK        MG    MG A1101                 O1B ANP A1102     1555   1555  1.90  
LINK        MG    MG A1101                 O2A ANP A1102     1555   1555  2.17  
LINK        MG    MG A1101                 O   HOH A1212     1555   1555  2.22  
LINK        MG    MG A1101                 O   HOH A1304     1555   1555  2.29  
LINK        MG    MG B2000                 O2G ANP B2001     1555   1555  2.48  
LINK        MG    MG B2000                 O   HOH B2192     1555   1555  2.56  
LINK        MG    MG B2000                 O2B ANP B2001     1555   1555  1.84  
LINK        MG    MG B2000                 O1A ANP B2001     1555   1555  2.20  
CISPEP   1 LYS A  806    ASP A  807          0        -6.45                     
SITE     1 AC1  5 ASN A 842  ASP A 855  ANP A1102  HOH A1212                    
SITE     2 AC1  5 HOH A1304                                                     
SITE     1 AC2 28 SER A 720  GLY A 721  ALA A 722  GLY A 724                    
SITE     2 AC2 28 VAL A 726  ALA A 743  LYS A 745  MET A 790                    
SITE     3 AC2 28 GLN A 791  MET A 793  CYS A 797  ASP A 837                    
SITE     4 AC2 28 ARG A 841  ASN A 842  LEU A 844  ASP A 855                    
SITE     5 AC2 28  MG A1101  57N A1103  HOH A1212  HOH A1217                    
SITE     6 AC2 28 HOH A1218  HOH A1246  HOH A1283  HOH A1285                    
SITE     7 AC2 28 HOH A1294  HOH A1304  HOH A1330  HOH A1338                    
SITE     1 AC3 13 ALA A 743  ILE A 744  LYS A 745  ILE A 759                    
SITE     2 AC3 13 MET A 766  CYS A 775  LEU A 777  LEU A 788                    
SITE     3 AC3 13 MET A 790  ASP A 855  PHE A 856  LEU A 858                    
SITE     4 AC3 13 ANP A1102                                                     
SITE     1 AC4  4 ASN B 842  ASP B 855  ANP B2001  HOH B2192                    
SITE     1 AC5 22 GLY B 719  SER B 720  GLY B 721  ALA B 722                    
SITE     2 AC5 22 GLY B 724  VAL B 726  ALA B 743  LYS B 745                    
SITE     3 AC5 22 MET B 790  GLN B 791  MET B 793  CYS B 797                    
SITE     4 AC5 22 ASP B 837  ARG B 841  ASN B 842  ASP B 855                    
SITE     5 AC5 22  MG B2000  HOH B2101  HOH B2145  HOH B2147                    
SITE     6 AC5 22 HOH B2192  HOH B2211                                          
CRYST1  155.133   72.497   75.998  90.00 113.24  90.00 C 1 2 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      0.006446  0.000000  0.002769        0.00000                         
SCALE2      0.000000  0.013794  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014321        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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