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Database: PDB
Entry: 3NJP
LinkDB: 3NJP
Original site: 3NJP 
HEADER    TRANSFERASE                             17-JUN-10   3NJP              
TITLE     THE EXTRACELLULAR AND TRANSMEMBRANE DOMAIN INTERFACES IN EPIDERMAL    
TITLE    2 GROWTH FACTOR RECEPTOR SIGNALING                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1, PROTO-ONCOGENE C-  
COMPND   5 ERBB-1;                                                              
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: EPIDERMAL GROWTH FACTOR;                                   
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 ENGINEERED: 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, ERBB1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC8;                                      
SOURCE  10 EXPRESSION_SYSTEM_ORGAN: OVARY;                                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1/ZEO(+);                          
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: EGF;                                                           
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  21 EXPRESSION_SYSTEM_ORGAN: OVARY                                       
KEYWDS    RECEPTOR TYROSINE KINASE, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.LU,L.-Z.MI,M.J.GREY,J.ZHU,E.GRAEF,S.YOKOYAMA,T.A.SPRINGER           
REVDAT   3   08-NOV-17 3NJP    1       REMARK                                   
REVDAT   2   01-DEC-10 3NJP    1       JRNL                                     
REVDAT   1   13-OCT-10 3NJP    0                                                
JRNL        AUTH   C.LU,L.Z.MI,M.J.GREY,J.ZHU,E.GRAEF,S.YOKOYAMA,T.A.SPRINGER   
JRNL        TITL   STRUCTURAL EVIDENCE FOR LOOSE LINKAGE BETWEEN LIGAND BINDING 
JRNL        TITL 2 AND KINASE ACTIVATION IN THE EPIDERMAL GROWTH FACTOR         
JRNL        TITL 3 RECEPTOR.                                                    
JRNL        REF    MOL.CELL.BIOL.                V.  30  5432 2010              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   20837704                                                     
JRNL        DOI    10.1128/MCB.00742-10                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 45560                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.265                           
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2320                            
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 49.4988 -  8.4809    0.99     2773   133  0.3296 0.3516        
REMARK   3     2  8.4809 -  6.7369    1.00     2703   138  0.2536 0.2748        
REMARK   3     3  6.7369 -  5.8869    1.00     2677   133  0.2398 0.2522        
REMARK   3     4  5.8869 -  5.3494    1.00     2647   146  0.2264 0.2817        
REMARK   3     5  5.3494 -  4.9663    0.99     2644   154  0.2178 0.2509        
REMARK   3     6  4.9663 -  4.6737    0.99     2634   123  0.2144 0.2834        
REMARK   3     7  4.6737 -  4.4398    0.99     2589   174  0.2076 0.2417        
REMARK   3     8  4.4398 -  4.2467    0.99     2635   136  0.2231 0.2563        
REMARK   3     9  4.2467 -  4.0833    0.99     2626   120  0.2242 0.2752        
REMARK   3    10  4.0833 -  3.9424    0.99     2598   122  0.2150 0.2704        
REMARK   3    11  3.9424 -  3.8192    0.98     2616   125  0.2245 0.2643        
REMARK   3    12  3.8192 -  3.7101    0.98     2572   138  0.2326 0.2836        
REMARK   3    13  3.7101 -  3.6124    0.98     2570   143  0.2332 0.2612        
REMARK   3    14  3.6124 -  3.5243    0.99     2596   135  0.2443 0.2708        
REMARK   3    15  3.5243 -  3.4442    0.98     2586   134  0.2654 0.3277        
REMARK   3    16  3.4442 -  3.3709    0.94     2473   129  0.3004 0.3225        
REMARK   3    17  3.3709 -  3.3035    0.91     2384   137  0.3380 0.3711        
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              : 0.30                                          
REMARK   3   B_SOL              : 80.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.000            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.670           
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) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.002          10814                                  
REMARK   3   ANGLE     :  0.541          14513                                  
REMARK   3   CHIRALITY :  0.037           1584                                  
REMARK   3   PLANARITY :  0.002           1882                                  
REMARK   3   DIHEDRAL  : 13.656           4082                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 2:500                                
REMARK   3    ORIGIN FOR THE GROUP (A): 107.4623  67.2369  45.4033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8451 T22:   0.6588                                     
REMARK   3      T33:   0.7711 T12:   0.0052                                     
REMARK   3      T13:   0.0779 T23:   0.1974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3571 L22:   1.4124                                     
REMARK   3      L33:   0.7168 L12:   1.3253                                     
REMARK   3      L13:   0.3313 L23:   0.3037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1295 S12:   0.2377 S13:   0.2021                       
REMARK   3      S21:  -0.2189 S22:  -0.1674 S23:   0.2259                       
REMARK   3      S31:  -0.0709 S32:   0.1689 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:500                                
REMARK   3    ORIGIN FOR THE GROUP (A):  59.0810  47.0575  54.4143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4936 T22:   0.5027                                     
REMARK   3      T33:   0.9886 T12:   0.0735                                     
REMARK   3      T13:  -0.0566 T23:  -0.1084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8400 L22:   0.2813                                     
REMARK   3      L33:   0.8396 L12:  -0.0057                                     
REMARK   3      L13:   0.5186 L23:   0.1159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0772 S12:  -0.0129 S13:  -0.2282                       
REMARK   3      S21:  -0.1032 S22:   0.0529 S23:   0.1956                       
REMARK   3      S31:  -0.1891 S32:   0.1283 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 501:573                              
REMARK   3    ORIGIN FOR THE GROUP (A): 119.3177  13.9955  41.9995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1029 T22:   1.0088                                     
REMARK   3      T33:   1.6316 T12:   0.0533                                     
REMARK   3      T13:  -0.1533 T23:   0.1786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1087 L22:   0.0965                                     
REMARK   3      L33:  -0.1090 L12:  -0.2164                                     
REMARK   3      L13:   0.0060 L23:   0.2451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1879 S12:   0.0981 S13:  -0.8777                       
REMARK   3      S21:  -0.1693 S22:  -0.7666 S23:  -0.0116                       
REMARK   3      S31:   0.6963 S32:  -1.1517 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 501:573                              
REMARK   3    ORIGIN FOR THE GROUP (A):  87.2125  11.6039  86.6712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3569 T22:   2.4061                                     
REMARK   3      T33:   2.7925 T12:  -0.1296                                     
REMARK   3      T13:   0.0698 T23:   1.1222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0845 L22:   0.1106                                     
REMARK   3      L33:  -0.1522 L12:   0.0540                                     
REMARK   3      L13:  -0.0233 L23:   0.2631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0926 S12:   0.5457 S13:   0.0582                       
REMARK   3      S21:  -0.4340 S22:   0.0475 S23:  -0.3733                       
REMARK   3      S31:  -0.1630 S32:   0.6517 S33:   0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 574:614                              
REMARK   3    ORIGIN FOR THE GROUP (A): 106.8706  -6.6965  60.8578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9310 T22:   2.1834                                     
REMARK   3      T33:   2.7036 T12:  -0.6355                                     
REMARK   3      T13:  -0.2546 T23:   0.2521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0198 L22:   0.0126                                     
REMARK   3      L33:  -0.0112 L12:  -0.0399                                     
REMARK   3      L13:  -0.0097 L23:   0.0445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5459 S12:  -0.6988 S13:   0.0319                       
REMARK   3      S21:  -0.3186 S22:   0.4872 S23:  -0.0216                       
REMARK   3      S31:   0.6628 S32:  -0.2927 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 574:614                              
REMARK   3    ORIGIN FOR THE GROUP (A): 114.1955   0.4864  77.5046              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2909 T22:   2.7628                                     
REMARK   3      T33:   2.9030 T12:  -0.2336                                     
REMARK   3      T13:  -0.2167 T23:   0.4800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0048 L22:   0.0503                                     
REMARK   3      L33:   0.0225 L12:   0.0022                                     
REMARK   3      L13:   0.0621 L23:   0.0191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9370 S12:  -1.1657 S13:  -0.1404                       
REMARK   3      S21:  -0.0967 S22:   0.7509 S23:   0.2592                       
REMARK   3      S31:  -0.7135 S32:  -0.2397 S33:   0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 124.6900  75.6933  51.3984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2201 T22:   1.1164                                     
REMARK   3      T33:   0.7569 T12:  -0.1777                                     
REMARK   3      T13:  -0.0281 T23:   0.1225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0757 L22:   0.0766                                     
REMARK   3      L33:   0.0537 L12:   0.0667                                     
REMARK   3      L13:   0.4332 L23:  -0.0450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1499 S12:  -0.4849 S13:  -0.5417                       
REMARK   3      S21:   0.2751 S22:  -0.1259 S23:  -0.3153                       
REMARK   3      S31:   0.0188 S32:   0.6844 S33:   0.0002                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  43.5080  35.7959  48.8784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7179 T22:   0.9105                                     
REMARK   3      T33:   1.7351 T12:   0.1630                                     
REMARK   3      T13:  -0.3566 T23:  -0.2244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1354 L22:   0.1850                                     
REMARK   3      L33:   0.3709 L12:  -0.0715                                     
REMARK   3      L13:   0.1211 L23:  -0.3369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2349 S12:  -0.1039 S13:  -1.3444                       
REMARK   3      S21:  -1.0535 S22:  -0.1143 S23:   0.7175                       
REMARK   3      S31:   0.5595 S32:  -0.3134 S33:  -0.0128                       
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 3NJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059914.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46667                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
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     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1IVO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 1% PEG6000, 75 MM TRIS      
REMARK 280  -HCL, 75 MM SOIDUM ACETATE, AND 200 MM NACL, PH 8.4, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.70767            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.41533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       75.41533            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.70767            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 66290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 5010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 4490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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   ND2  ASN B    32     C2   NAG B  1032              2.04            
REMARK 500   ND2  ASN A   151     C2   NAG A  1151              2.13            
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    GLU A   2      -82.62    -76.95                                   
REMARK 500    SER A  11       44.57   -154.91                                   
REMARK 500    LYS A  13     -114.75     55.40                                   
REMARK 500    ASN A  33       -7.94     76.00                                   
REMARK 500    ASN A  49     -107.78     64.09                                   
REMARK 500    TYR A  50      113.37     28.97                                   
REMARK 500    LEU A  77       44.45    -78.76                                   
REMARK 500    SER A  92      -61.68   -156.93                                   
REMARK 500    SER A  99       64.98     31.07                                   
REMARK 500    ASN A 100       59.37   -101.43                                   
REMARK 500    PRO A 112       46.23    -70.33                                   
REMARK 500    ALA A 123     -166.27   -103.57                                   
REMARK 500    ASN A 134      -45.79     72.47                                   
REMARK 500    ASN A 158       71.52   -102.53                                   
REMARK 500    LEU A 160      -81.91   -115.90                                   
REMARK 500    THR A 187       23.46   -140.22                                   
REMARK 500    LYS A 188      -55.09   -127.31                                   
REMARK 500    GLN A 211       31.91    -98.47                                   
REMARK 500    ALA A 213      -70.23   -106.23                                   
REMARK 500    LYS A 229      -91.15   -123.82                                   
REMARK 500    GLU A 233     -110.65     53.69                                   
REMARK 500    GLU A 258        1.30    -66.10                                   
REMARK 500    ALA A 289        0.06    -62.27                                   
REMARK 500    ASP A 297      -12.76     75.12                                   
REMARK 500    LYS A 303     -125.32   -113.79                                   
REMARK 500    GLU A 306       41.21    -88.06                                   
REMARK 500    GLU A 320       -6.85    -59.87                                   
REMARK 500    LYS A 336      -79.57    -53.78                                   
REMARK 500    ASN A 337       61.95   -101.51                                   
REMARK 500    TRP A 386      145.62   -170.26                                   
REMARK 500    HIS A 409        5.36     57.12                                   
REMARK 500    ARG A 427        1.56    -67.27                                   
REMARK 500    LYS A 443      -72.26    -28.14                                   
REMARK 500    ASN A 444       63.30   -107.68                                   
REMARK 500    TYR A 447      -13.52     66.49                                   
REMARK 500    ASN A 469     -153.85   -119.35                                   
REMARK 500    ASN A 504      -81.64    -95.61                                   
REMARK 500    LYS A 514      151.68    179.53                                   
REMARK 500    GLU A 519     -152.73   -125.69                                   
REMARK 500    PRO A 540      100.97    -53.42                                   
REMARK 500    MET A 543      -92.02   -101.47                                   
REMARK 500    ASN A 544     -164.37    -78.88                                   
REMARK 500    ILE A 545     -177.11    -65.90                                   
REMARK 500    PRO A 552       -7.93    -59.38                                   
REMARK 500    HIS A 560     -111.26   -127.14                                   
REMARK 500    ASP A 563       79.62   -105.34                                   
REMARK 500    ASP A 588     -133.15   -116.13                                   
REMARK 500    ALA A 589      -72.32    -62.84                                   
REMARK 500    CYS A 600       98.21    -65.02                                   
REMARK 500    SER B  11       55.32   -151.30                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      95 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1032                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1049                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1151                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1172                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1328                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1337                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1420                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1032                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1151                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1328                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE B 617                 
DBREF  3NJP A    1   614  UNP    P00533   EGFR_HUMAN      25    638             
DBREF  3NJP B    1   614  UNP    P00533   EGFR_HUMAN      25    638             
DBREF  3NJP C    5    51  UNP    Q6QBS2   Q6QBS2_HUMAN     5     51             
DBREF  3NJP D    5    51  UNP    Q6QBS2   Q6QBS2_HUMAN     5     51             
SEQADV 3NJP LYS A  516  UNP  P00533    ASN   540 CONFLICT                       
SEQADV 3NJP LYS B  516  UNP  P00533    ASN   540 CONFLICT                       
SEQRES   1 A  614  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 A  614  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 A  614  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 A  614  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 A  614  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 A  614  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 A  614  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 A  614  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 A  614  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 A  614  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 A  614  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 A  614  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 A  614  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 A  614  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 A  614  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 A  614  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 A  614  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 A  614  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 A  614  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 A  614  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 A  614  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 A  614  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 A  614  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 A  614  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 A  614  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 A  614  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 A  614  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 A  614  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 A  614  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 A  614  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 A  614  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 A  614  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 A  614  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 A  614  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 A  614  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 A  614  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 A  614  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 A  614  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 A  614  GLU PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG          
SEQRES  40 A  614  GLY ARG GLU CYS VAL ASP LYS CYS LYS LEU LEU GLU GLY          
SEQRES  41 A  614  GLU PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN          
SEQRES  42 A  614  CYS HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR          
SEQRES  43 A  614  CYS THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA          
SEQRES  44 A  614  HIS TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO          
SEQRES  45 A  614  ALA GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS          
SEQRES  46 A  614  TYR ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO          
SEQRES  47 A  614  ASN CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY          
SEQRES  48 A  614  CYS PRO THR                                                  
SEQRES   1 B  614  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 B  614  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 B  614  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 B  614  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 B  614  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 B  614  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 B  614  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 B  614  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 B  614  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 B  614  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 B  614  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 B  614  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 B  614  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 B  614  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 B  614  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 B  614  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 B  614  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 B  614  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 B  614  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 B  614  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 B  614  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 B  614  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 B  614  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 B  614  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 B  614  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 B  614  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 B  614  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 B  614  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 B  614  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 B  614  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 B  614  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 B  614  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 B  614  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 B  614  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 B  614  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 B  614  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 B  614  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 B  614  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 B  614  GLU PRO ARG ASP CYS VAL SER CYS ARG ASN VAL SER ARG          
SEQRES  40 B  614  GLY ARG GLU CYS VAL ASP LYS CYS LYS LEU LEU GLU GLY          
SEQRES  41 B  614  GLU PRO ARG GLU PHE VAL GLU ASN SER GLU CYS ILE GLN          
SEQRES  42 B  614  CYS HIS PRO GLU CYS LEU PRO GLN ALA MET ASN ILE THR          
SEQRES  43 B  614  CYS THR GLY ARG GLY PRO ASP ASN CYS ILE GLN CYS ALA          
SEQRES  44 B  614  HIS TYR ILE ASP GLY PRO HIS CYS VAL LYS THR CYS PRO          
SEQRES  45 B  614  ALA GLY VAL MET GLY GLU ASN ASN THR LEU VAL TRP LYS          
SEQRES  46 B  614  TYR ALA ASP ALA GLY HIS VAL CYS HIS LEU CYS HIS PRO          
SEQRES  47 B  614  ASN CYS THR TYR GLY CYS THR GLY PRO GLY LEU GLU GLY          
SEQRES  48 B  614  CYS PRO THR                                                  
SEQRES   1 C   47  GLU CYS PRO LEU SER HIS ASP GLY TYR CYS LEU HIS ASP          
SEQRES   2 C   47  GLY VAL CYS MET TYR ILE GLU ALA LEU ASP LYS TYR ALA          
SEQRES   3 C   47  CYS ASN CYS VAL VAL GLY TYR ILE GLY GLU ARG CYS GLN          
SEQRES   4 C   47  TYR ARG ASP LEU LYS TRP TRP GLU                              
SEQRES   1 D   47  GLU CYS PRO LEU SER HIS ASP GLY TYR CYS LEU HIS ASP          
SEQRES   2 D   47  GLY VAL CYS MET TYR ILE GLU ALA LEU ASP LYS TYR ALA          
SEQRES   3 D   47  CYS ASN CYS VAL VAL GLY TYR ILE GLY GLU ARG CYS GLN          
SEQRES   4 D   47  TYR ARG ASP LEU LYS TRP TRP GLU                              
MODRES 3NJP ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A  172  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN B  328  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN B  504  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A  337  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A  420  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A  504  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN B   32  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A  151  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN B  151  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A   49  ASN  GLYCOSYLATION SITE                                 
MODRES 3NJP ASN A   32  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1032      14                                                       
HET    NAG  A1049      14                                                       
HET    NAG  A1151      14                                                       
HET    NAG  A1172      14                                                       
HET    NAG  A1328      14                                                       
HET    NAG  A1337      14                                                       
HET    NAG  A1420      14                                                       
HET    NAG  A1504      14                                                       
HET    NAG  B1032      14                                                       
HET    NAG  B1151      14                                                       
HET    NAG  B1328      14                                                       
HET    NAG  B1504      14                                                       
HET    2PE  B 615      28                                                       
HET    2PE  B 616      28                                                       
HET    2PE  B 617      28                                                       
HET    2PE  D   1      28                                                       
HET    2PE  D  52      28                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     2PE NONAETHYLENE GLYCOL                                              
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL  17  2PE    5(C18 H38 O10)                                               
FORMUL  22  HOH   *24(H2 O)                                                     
HELIX    1   1 THR A   19  ASN A   32  1                                  14    
HELIX    2   2 LEU A   52  ILE A   58  5                                   7    
HELIX    3   3 ASN A  134  ILE A  138  5                                   5    
HELIX    4   4 GLN A  139  VAL A  144  1                                   6    
HELIX    5   5 CYS A  170  SER A  174  5                                   5    
HELIX    6   6 SER A  203  CYS A  207  5                                   5    
HELIX    7   7 ILE A  318  LYS A  322  5                                   5    
HELIX    8   8 THR A  330  LYS A  336  5                                   7    
HELIX    9   9 LEU A  348  GLY A  354  1                                   7    
HELIX   10  10 ASP A  364  VAL A  374  5                                  11    
HELIX   11  11 LEU A  393  GLU A  397  5                                   5    
HELIX   12  12 LYS A  407  GLY A  410  5                                   4    
HELIX   13  13 TYR A  447  ILE A  451  5                                   5    
HELIX   14  14 ASN A  452  PHE A  457  1                                   6    
HELIX   15  15 GLY A  471  THR A  478  1                                   8    
HELIX   16  16 GLY A  551  CYS A  555  5                                   5    
HELIX   17  17 GLU A  578  ASN A  580  5                                   3    
HELIX   18  18 GLY A  608  CYS A  612  5                                   5    
HELIX   19  19 THR B   19  ASN B   32  1                                  14    
HELIX   20  20 LEU B   52  THR B   57  5                                   6    
HELIX   21  21 TYR B   88  ASN B   91  5                                   4    
HELIX   22  22 ASN B  134  ILE B  138  5                                   5    
HELIX   23  23 GLN B  139  VAL B  144  1                                   6    
HELIX   24  24 PHE B  148  MET B  152  5                                   5    
HELIX   25  25 CYS B  170  SER B  174  5                                   5    
HELIX   26  26 SER B  203  CYS B  207  5                                   5    
HELIX   27  27 ILE B  318  LYS B  322  5                                   5    
HELIX   28  28 THR B  330  LYS B  336  5                                   7    
HELIX   29  29 LEU B  348  ARG B  353  1                                   6    
HELIX   30  30 ASP B  364  VAL B  374  5                                  11    
HELIX   31  31 LEU B  393  GLU B  397  5                                   5    
HELIX   32  32 LYS B  407  GLY B  410  5                                   4    
HELIX   33  33 TYR B  447  ILE B  451  5                                   5    
HELIX   34  34 ASN B  452  PHE B  457  1                                   6    
HELIX   35  35 CYS B  475  GLY B  479  5                                   5    
HELIX   36  36 GLU B  495  CYS B  499  5                                   5    
HELIX   37  37 GLY B  551  CYS B  555  5                                   5    
HELIX   38  38 GLY B  577  THR B  581  5                                   5    
SHEET    1   A 4 VAL A   6  CYS A   7  0                                        
SHEET    2   A 4 VAL A  36  VAL A  37  1  O  VAL A  36   N  CYS A   7           
SHEET    3   A 4 GLU A  60  VAL A  61  1  O  GLU A  60   N  VAL A  37           
SHEET    4   A 4 ILE A  82  ILE A  83  1  O  ILE A  82   N  VAL A  61           
SHEET    1   B 3 GLN A  16  LEU A  17  0                                        
SHEET    2   B 3 LYS C  28  CYS C  33  1  O  CYS C  31   N  GLN A  16           
SHEET    3   B 3 VAL C  19  ILE C  23 -1  N  MET C  21   O  ALA C  30           
SHEET    1   C 5 LEU A  41  THR A  44  0                                        
SHEET    2   C 5 VAL A  65  ALA A  68  1  O  LEU A  66   N  ILE A  43           
SHEET    3   C 5 TYR A  93  LEU A  98  1  O  ALA A  94   N  VAL A  65           
SHEET    4   C 5 ALA A 123  SER A 127  1  O  ALA A 123   N  ALA A  94           
SHEET    5   C 5 SER A 153  MET A 154  1  O  SER A 153   N  VAL A 124           
SHEET    1   D 2 PHE A 230  ASP A 232  0                                        
SHEET    2   D 2 THR A 235  LYS A 237 -1  O  LYS A 237   N  PHE A 230           
SHEET    1   E 2 MET A 244  ASN A 247  0                                        
SHEET    2   E 2 GLN A 252  VAL A 255 -1  O  ASP A 254   N  LEU A 245           
SHEET    1   F 2 TYR A 261  PHE A 263  0                                        
SHEET    2   F 2 THR A 266  VAL A 268 -1  O  VAL A 268   N  TYR A 261           
SHEET    1   G 4 CYS A 283  VAL A 284  0                                        
SHEET    2   G 4 VAL A 276  VAL A 277 -1  N  VAL A 276   O  VAL A 284           
SHEET    3   G 4 VAL A 299  CYS A 302  1  O  ARG A 300   N  VAL A 277           
SHEET    4   G 4 GLU A 293  GLU A 296 -1  N  MET A 294   O  LYS A 301           
SHEET    1   H 5 CYS A 313  ASN A 314  0                                        
SHEET    2   H 5 SER A 340  SER A 342  1  O  SER A 342   N  CYS A 313           
SHEET    3   H 5 GLU A 376  ILE A 377  1  O  GLU A 376   N  ILE A 341           
SHEET    4   H 5 ILE A 401  ILE A 402  1  O  ILE A 401   N  ILE A 377           
SHEET    5   H 5 GLU A 431  ILE A 432  1  O  GLU A 431   N  ILE A 402           
SHEET    1   I 5 LEU A 345  ILE A 347  0                                        
SHEET    2   I 5 LEU A 381  ILE A 383  1  O  LEU A 382   N  LEU A 345           
SHEET    3   I 5 PHE A 412  VAL A 417  1  O  ALA A 415   N  ILE A 383           
SHEET    4   I 5 ASP A 436  SER A 440  1  O  ILE A 438   N  LEU A 414           
SHEET    5   I 5 THR A 464  LYS A 465  1  O  LYS A 465   N  VAL A 437           
SHEET    1   J 2 VAL A 505  ARG A 507  0                                        
SHEET    2   J 2 GLU A 510  VAL A 512 -1  O  GLU A 510   N  ARG A 507           
SHEET    1   K 2 GLU A 524  GLU A 527  0                                        
SHEET    2   K 2 GLU A 530  GLN A 533 -1  O  ILE A 532   N  PHE A 525           
SHEET    1   L 2 TYR A 561  ASP A 563  0                                        
SHEET    2   L 2 HIS A 566  VAL A 568 -1  O  HIS A 566   N  ASP A 563           
SHEET    1   M 3 ALA A 573  MET A 576  0                                        
SHEET    2   M 3 LEU A 582  ALA A 587 -1  O  VAL A 583   N  GLY A 574           
SHEET    3   M 3 CYS A 593  LEU A 595 -1  O  HIS A 594   N  TYR A 586           
SHEET    1   N 5 VAL B   6  CYS B   7  0                                        
SHEET    2   N 5 VAL B  36  VAL B  37  1  O  VAL B  36   N  CYS B   7           
SHEET    3   N 5 GLU B  60  VAL B  61  1  O  GLU B  60   N  VAL B  37           
SHEET    4   N 5 ILE B  82  ILE B  83  1  O  ILE B  82   N  VAL B  61           
SHEET    5   N 5 GLU B 118  ILE B 119  1  O  GLU B 118   N  ILE B  83           
SHEET    1   O 3 GLN B  16  LEU B  17  0                                        
SHEET    2   O 3 TYR D  29  CYS D  33  1  O  CYS D  31   N  GLN B  16           
SHEET    3   O 3 VAL D  19  TYR D  22 -1  N  VAL D  19   O  ASN D  32           
SHEET    1   P 5 LEU B  41  THR B  44  0                                        
SHEET    2   P 5 VAL B  65  ALA B  68  1  O  LEU B  66   N  LEU B  41           
SHEET    3   P 5 TYR B  93  LEU B  98  1  O  ALA B  96   N  ILE B  67           
SHEET    4   P 5 ALA B 123  SER B 127  1  O  ALA B 123   N  ALA B  94           
SHEET    5   P 5 SER B 153  MET B 154  1  O  SER B 153   N  VAL B 124           
SHEET    1   Q 2 MET B 244  ASN B 247  0                                        
SHEET    2   Q 2 GLN B 252  VAL B 255 -1  O  GLN B 252   N  ASN B 247           
SHEET    1   R 2 TYR B 261  PHE B 263  0                                        
SHEET    2   R 2 THR B 266  VAL B 268 -1  O  VAL B 268   N  TYR B 261           
SHEET    1   S 4 CYS B 283  VAL B 284  0                                        
SHEET    2   S 4 VAL B 276  VAL B 277 -1  N  VAL B 276   O  VAL B 284           
SHEET    3   S 4 ARG B 300  LYS B 304  1  O  ARG B 300   N  VAL B 277           
SHEET    4   S 4 SER B 291  MET B 294 -1  N  TYR B 292   O  LYS B 303           
SHEET    1   T 5 CYS B 313  ASN B 314  0                                        
SHEET    2   T 5 SER B 340  SER B 342  1  O  SER B 342   N  CYS B 313           
SHEET    3   T 5 GLU B 376  ILE B 377  1  O  GLU B 376   N  ILE B 341           
SHEET    4   T 5 ILE B 401  ILE B 402  1  O  ILE B 401   N  ILE B 377           
SHEET    5   T 5 GLU B 431  ILE B 432  1  O  GLU B 431   N  ILE B 402           
SHEET    1   U 5 LEU B 345  ILE B 347  0                                        
SHEET    2   U 5 LEU B 381  ILE B 383  1  O  LEU B 382   N  LEU B 345           
SHEET    3   U 5 PHE B 412  VAL B 417  1  O  ALA B 415   N  ILE B 383           
SHEET    4   U 5 ASP B 436  SER B 440  1  O  ILE B 438   N  LEU B 414           
SHEET    5   U 5 THR B 464  LYS B 465  1  O  LYS B 465   N  VAL B 437           
SHEET    1   V 2 VAL B 505  SER B 506  0                                        
SHEET    2   V 2 CYS B 511  VAL B 512 -1  O  VAL B 512   N  VAL B 505           
SHEET    1   W 2 GLU B 524  GLU B 527  0                                        
SHEET    2   W 2 GLU B 530  GLN B 533 -1  O  ILE B 532   N  PHE B 525           
SHEET    1   X 2 TYR B 561  ASP B 563  0                                        
SHEET    2   X 2 HIS B 566  VAL B 568 -1  O  HIS B 566   N  ASP B 563           
SHEET    1   Y 2 LYS B 585  ALA B 587  0                                        
SHEET    2   Y 2 CYS B 593  LEU B 595 -1  O  HIS B 594   N  TYR B 586           
SHEET    1   Z 2 TYR C  37  ILE C  38  0                                        
SHEET    2   Z 2 TYR C  44  ARG C  45 -1  O  TYR C  44   N  ILE C  38           
SHEET    1  AA 2 TYR D  37  ILE D  38  0                                        
SHEET    2  AA 2 TYR D  44  ARG D  45 -1  O  TYR D  44   N  ILE D  38           
SSBOND   1 CYS A    7    CYS A   34                          1555   1555  2.03  
SSBOND   2 CYS A  133    CYS A  163                          1555   1555  2.03  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.03  
SSBOND   4 CYS A  170    CYS A  183                          1555   1555  2.03  
SSBOND   5 CYS A  191    CYS A  199                          1555   1555  2.03  
SSBOND   6 CYS A  195    CYS A  207                          1555   1555  2.03  
SSBOND   7 CYS A  208    CYS A  216                          1555   1555  2.03  
SSBOND   8 CYS A  212    CYS A  224                          1555   1555  2.03  
SSBOND   9 CYS A  227    CYS A  236                          1555   1555  2.03  
SSBOND  10 CYS A  240    CYS A  267                          1555   1555  2.03  
SSBOND  11 CYS A  271    CYS A  283                          1555   1555  2.03  
SSBOND  12 CYS A  287    CYS A  302                          1555   1555  2.03  
SSBOND  13 CYS A  305    CYS A  309                          1555   1555  2.04  
SSBOND  14 CYS A  313    CYS A  338                          1555   1555  2.03  
SSBOND  15 CYS A  446    CYS A  475                          1555   1555  2.03  
SSBOND  16 CYS A  482    CYS A  491                          1555   1555  2.03  
SSBOND  17 CYS A  486    CYS A  499                          1555   1555  2.03  
SSBOND  18 CYS A  502    CYS A  511                          1555   1555  2.03  
SSBOND  19 CYS A  515    CYS A  531                          1555   1555  2.03  
SSBOND  20 CYS A  534    CYS A  547                          1555   1555  2.03  
SSBOND  21 CYS A  538    CYS A  555                          1555   1555  2.03  
SSBOND  22 CYS A  558    CYS A  567                          1555   1555  2.03  
SSBOND  23 CYS A  571    CYS A  593                          1555   1555  2.03  
SSBOND  24 CYS A  596    CYS A  604                          1555   1555  2.03  
SSBOND  25 CYS A  600    CYS A  612                          1555   1555  2.03  
SSBOND  26 CYS B    7    CYS B   34                          1555   1555  2.03  
SSBOND  27 CYS B  133    CYS B  163                          1555   1555  2.03  
SSBOND  28 CYS B  166    CYS B  175                          1555   1555  2.03  
SSBOND  29 CYS B  170    CYS B  183                          1555   1555  2.03  
SSBOND  30 CYS B  191    CYS B  199                          1555   1555  2.03  
SSBOND  31 CYS B  195    CYS B  207                          1555   1555  2.03  
SSBOND  32 CYS B  208    CYS B  216                          1555   1555  2.03  
SSBOND  33 CYS B  212    CYS B  224                          1555   1555  2.03  
SSBOND  34 CYS B  227    CYS B  236                          1555   1555  2.03  
SSBOND  35 CYS B  240    CYS B  267                          1555   1555  2.03  
SSBOND  36 CYS B  271    CYS B  283                          1555   1555  2.03  
SSBOND  37 CYS B  287    CYS B  302                          1555   1555  2.03  
SSBOND  38 CYS B  305    CYS B  309                          1555   1555  2.04  
SSBOND  39 CYS B  313    CYS B  338                          1555   1555  2.03  
SSBOND  40 CYS B  446    CYS B  475                          1555   1555  2.03  
SSBOND  41 CYS B  482    CYS B  491                          1555   1555  2.03  
SSBOND  42 CYS B  486    CYS B  499                          1555   1555  2.03  
SSBOND  43 CYS B  502    CYS B  511                          1555   1555  2.03  
SSBOND  44 CYS B  515    CYS B  531                          1555   1555  2.03  
SSBOND  45 CYS B  534    CYS B  547                          1555   1555  2.03  
SSBOND  46 CYS B  538    CYS B  555                          1555   1555  2.03  
SSBOND  47 CYS B  558    CYS B  567                          1555   1555  2.03  
SSBOND  48 CYS B  571    CYS B  593                          1555   1555  2.03  
SSBOND  49 CYS B  596    CYS B  604                          1555   1555  2.03  
SSBOND  50 CYS B  600    CYS B  612                          1555   1555  2.03  
SSBOND  51 CYS C    6    CYS C   20                          1555   1555  2.03  
SSBOND  52 CYS C   14    CYS C   31                          1555   1555  2.03  
SSBOND  53 CYS C   33    CYS C   42                          1555   1555  2.03  
SSBOND  54 CYS D    6    CYS D   20                          1555   1555  2.03  
SSBOND  55 CYS D   14    CYS D   31                          1555   1555  2.03  
SSBOND  56 CYS D   33    CYS D   42                          1555   1555  2.03  
LINK         ND2 ASN A 328                 C1  NAG A1328     1555   1555  1.44  
LINK         ND2 ASN A 172                 C1  NAG A1172     1555   1555  1.44  
LINK         ND2 ASN B 328                 C1  NAG B1328     1555   1555  1.44  
LINK         ND2 ASN B 504                 C1  NAG B1504     1555   1555  1.44  
LINK         ND2 ASN A 337                 C1  NAG A1337     1555   1555  1.44  
LINK         ND2 ASN A 420                 C1  NAG A1420     1555   1555  1.44  
LINK         ND2 ASN A 504                 C1  NAG A1504     1555   1555  1.44  
LINK         ND2 ASN B  32                 C1  NAG B1032     1555   1555  1.44  
LINK         ND2 ASN A 151                 C1  NAG A1151     1555   1555  1.44  
LINK         ND2 ASN B 151                 C1  NAG B1151     1555   1555  1.44  
LINK         ND2 ASN A  49                 C1  NAG A1049     1555   1555  1.44  
LINK         ND2 ASN A  32                 C1  NAG A1032     1555   1555  1.44  
SITE     1 AC1  3 GLN A  28  ASN A  32  ASN A  33                               
SITE     1 AC2  1 ASN A  49                                                     
SITE     1 AC3  4 ASN A  91  SER A  92  PHE A 148  ASN A 151                    
SITE     1 AC4  3 ASN A 172  THR B 548  ASN B 554                               
SITE     1 AC5  9 PHE A 321  SER A 324  LEU A 325  SER A 326                    
SITE     2 AC5  9 ASN A 328  ASN A 331  ASP A 355  THR A 358                    
SITE     3 AC5  9 SER A 460                                                     
SITE     1 AC6  1 ASN A 337                                                     
SITE     1 AC7  2 GLU A 388  ASN A 420                                          
SITE     1 AC8  2 ASN A 504  ASP A 513                                          
SITE     1 AC9  3 GLN B  28  ASN B  32  ASN B  33                               
SITE     1 BC1  3 ASN B  91  SER B  92  ASN B 151                               
SITE     1 BC2  7 SER B 324  LEU B 325  SER B 326  ASN B 328                    
SITE     2 BC2  7 ASN B 331  VAL B 350  THR B 358                               
SITE     1 BC3  2 ARG B 503  ASN B 504                                          
SITE     1 BC4  1 2PE B 617                                                     
SITE     1 BC5  1 2PE B 616                                                     
CRYST1  220.167  220.167  113.123  90.00  90.00 120.00 P 31 2 1     12          
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      0.004542  0.002622  0.000000        0.00000                         
SCALE2      0.000000  0.005245  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008840        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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