GenomeNet

Database: PDB
Entry: 3P0Y
LinkDB: 3P0Y
Original site: 3P0Y 
HEADER    IMMUNE SYSTEM                           29-SEP-10   3P0Y              
TITLE     ANTI-EGFR/HER3 FAB DL11 IN COMPLEX WITH DOMAIN III OF EGFR            
TITLE    2 EXTRACELLULAR REGION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: DOMAIN III, UNP RESIDUES 334-540;                          
COMPND   5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1, PROTO-ONCOGENE C-  
COMPND   6 ERBB-1;                                                              
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: FAB DL11 HEAVY CHAIN;                                      
COMPND  11 CHAIN: H;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: FAB DL11 LIGHT CHAIN;                                      
COMPND  15 CHAIN: L;                                                            
COMPND  16 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PW0579-3;                                 
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PW0579-3                                  
KEYWDS    BETA-SANDWICH, ANTIGENS EGFR, IMMUNE SYSTEM                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,S.SHIA                                                    
REVDAT   2   21-MAR-12 3P0Y    1       JRNL                                     
REVDAT   1   26-OCT-11 3P0Y    0                                                
JRNL        AUTH   G.SCHAEFER,L.HABER,L.M.CROCKER,S.SHIA,L.SHAO,D.DOWBENKO,     
JRNL        AUTH 2 K.TOTPAL,A.WONG,C.V.LEE,S.STAWICKI,R.CLARK,C.FIELDS,         
JRNL        AUTH 3 G.D.LEWIS PHILLIPS,R.A.PRELL,D.M.DANILENKO,Y.FRANKE,         
JRNL        AUTH 4 J.P.STEPHAN,J.HWANG,Y.WU,J.BOSTROM,M.X.SLIWKOWSKI,G.FUH,     
JRNL        AUTH 5 C.EIGENBROT                                                  
JRNL        TITL   A TWO-IN-ONE ANTIBODY AGAINST HER3 AND EGFR HAS SUPERIOR     
JRNL        TITL 2 INHIBITORY ACTIVITY COMPARED WITH MONOSPECIFIC ANTIBODIES.   
JRNL        REF    CANCER CELL                   V.  20   472 2011              
JRNL        REFN                   ISSN 1535-6108                               
JRNL        PMID   22014573                                                     
JRNL        DOI    10.1016/J.CCR.2011.09.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 73362                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1507                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9534                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4747                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 650                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 0.24000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.433         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5067 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6906 ; 1.240 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   642 ; 6.227 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;32.510 ;24.428       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   818 ;11.926 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.155 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   791 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3775 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2184 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3448 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   543 ; 0.118 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.152 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3260 ; 2.400 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5128 ; 3.507 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2057 ; 3.636 ; 3.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1778 ; 5.426 ; 6.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3P0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061819.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : .9774                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : SI                                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE/PEG3350/SODIUM       
REMARK 280  DEXTRAN SULFATE, PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE   
REMARK 280  286K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       40.96700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      100.33850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.96700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      100.33850            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       49.42600            
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 H 659  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     ASN A   504                                                      
REMARK 465     VAL A   505                                                      
REMARK 465     SER A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     GLU A   510                                                      
REMARK 465     CYS A   511                                                      
REMARK 465     VAL A   512                                                      
REMARK 465     ASP A   513                                                      
REMARK 465     LYS A   514                                                      
REMARK 465     GLY A   515                                                      
REMARK 465     ASN A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     HIS A   518                                                      
REMARK 465     HIS A   519                                                      
REMARK 465     HIS A   520                                                      
REMARK 465     HIS A   521                                                      
REMARK 465     HIS A   522                                                      
REMARK 465     HIS A   523                                                      
REMARK 465     LYS H   129                                                      
REMARK 465     SER H   130                                                      
REMARK 465     THR H   131                                                      
REMARK 465     SER H   132                                                      
REMARK 465     GLY H   133                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     ASP H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     THR H   219                                                      
REMARK 465     HIS H   220                                                      
REMARK 465     CYS L   214                                                      
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 A   389     C2   NAG A  3891              2.12            
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    TYR A 447      -23.49     76.22                                   
REMARK 500    ASN A 469     -156.52    -97.86                                   
REMARK 500    SER H 127       81.65     52.05                                   
REMARK 500    ALA L  30     -116.13     54.62                                   
REMARK 500    ALA L  51      -35.11     70.52                                   
REMARK 500    ASN L 152       -2.88     70.95                                   
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 3281                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3282                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3891                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A 3892                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3893                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P0V   RELATED DB: PDB                                   
REMARK 900 FAB DL11 ALONE                                                       
REMARK 900 RELATED ID: 3P11   RELATED DB: PDB                                   
REMARK 900 FAB DL11 WITH HER3                                                   
DBREF  3P0Y A  310   514  UNP    P00533   EGFR_HUMAN     334    538             
DBREF  3P0Y L    1   214  PDB    3P0Y     3P0Y             1    214             
DBREF  3P0Y H    1   220  PDB    3P0Y     3P0Y             1    220             
SEQADV 3P0Y GLY A  515  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y ASN A  516  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y SER A  517  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  518  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  519  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  520  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  521  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  522  UNP  P00533              EXPRESSION TAG                 
SEQADV 3P0Y HIS A  523  UNP  P00533              EXPRESSION TAG                 
SEQRES   1 A  214  ARG LYS VAL CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS          
SEQRES   2 A  214  ASP SER LEU SER ILE ASN ALA THR ASN ILE LYS HIS PHE          
SEQRES   3 A  214  LYS ASN CYS THR SER ILE SER GLY ASP LEU HIS ILE LEU          
SEQRES   4 A  214  PRO VAL ALA PHE ARG GLY ASP SER PHE THR HIS THR PRO          
SEQRES   5 A  214  PRO LEU ASP PRO GLN GLU LEU ASP ILE LEU LYS THR VAL          
SEQRES   6 A  214  LYS GLU ILE THR GLY PHE LEU LEU ILE GLN ALA TRP PRO          
SEQRES   7 A  214  GLU ASN ARG THR ASP LEU HIS ALA PHE GLU ASN LEU GLU          
SEQRES   8 A  214  ILE ILE ARG GLY ARG THR LYS GLN HIS GLY GLN PHE SER          
SEQRES   9 A  214  LEU ALA VAL VAL SER LEU ASN ILE THR SER LEU GLY LEU          
SEQRES  10 A  214  ARG SER LEU LYS GLU ILE SER ASP GLY ASP VAL ILE ILE          
SEQRES  11 A  214  SER GLY ASN LYS ASN LEU CYS TYR ALA ASN THR ILE ASN          
SEQRES  12 A  214  TRP LYS LYS LEU PHE GLY THR SER GLY GLN LYS THR LYS          
SEQRES  13 A  214  ILE ILE SER ASN ARG GLY GLU ASN SER CYS LYS ALA THR          
SEQRES  14 A  214  GLY GLN VAL CYS HIS ALA LEU CYS SER PRO GLU GLY CYS          
SEQRES  15 A  214  TRP GLY PRO GLU PRO ARG ASP CYS VAL SER CYS ARG ASN          
SEQRES  16 A  214  VAL SER ARG GLY ARG GLU CYS VAL ASP LYS GLY ASN SER          
SEQRES  17 A  214  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 H  228  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  228  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  228  PHE THR LEU SER GLY ASP TRP ILE HIS TRP VAL ARG GLN          
SEQRES   4 H  228  ALA PRO GLY LYS GLY LEU GLU TRP LEU GLY GLU ILE SER          
SEQRES   5 H  228  ALA ALA GLY GLY TYR THR ASP TYR ALA ASP SER VAL LYS          
SEQRES   6 H  228  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 H  228  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  228  ALA VAL TYR TYR CYS ALA ARG GLU SER ARG VAL SER PHE          
SEQRES   9 H  228  GLU ALA ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL          
SEQRES  10 H  228  THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE          
SEQRES  11 H  228  PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR          
SEQRES  12 H  228  ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU          
SEQRES  13 H  228  PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER          
SEQRES  14 H  228  GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY          
SEQRES  15 H  228  LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER          
SEQRES  16 H  228  SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS          
SEQRES  17 H  228  LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO          
SEQRES  18 H  228  LYS SER CYS ASP LYS THR HIS                                  
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  214  GLN ASP LEU ALA THR ASP VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 L  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER          
SEQRES   8 L  214  GLU PRO GLU PRO TYR THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
MODRES 3P0Y ASN A  389  ASN  GLYCOSYLATION SITE                                 
MODRES 3P0Y ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 3P0Y ASN A  420  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A3281      14                                                       
HET    NAG  A3282      14                                                       
HET    NAG  A3891      14                                                       
HET    FUL  A3892      10                                                       
HET    NAG  A3893      14                                                       
HET    NAG  A4201      14                                                       
HET    NAG  A4202      14                                                       
HET    GOL  H 401       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  NAG    6(C8 H15 N O6)                                               
FORMUL   5  FUL    C6 H12 O5                                                    
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *650(H2 O)                                                    
HELIX    1   1 ILE A  318  LYS A  322  5                                   5    
HELIX    2   2 ASN A  331  LYS A  336  5                                   6    
HELIX    3   3 LEU A  348  GLY A  354  1                                   7    
HELIX    4   4 ASP A  364  VAL A  374  5                                  11    
HELIX    5   5 LEU A  393  GLU A  397  5                                   5    
HELIX    6   6 LYS A  407  GLY A  410  5                                   4    
HELIX    7   7 TYR A  447  ILE A  451  5                                   5    
HELIX    8   8 ASN A  452  PHE A  457  1                                   6    
HELIX    9   9 GLY A  471  THR A  478  1                                   8    
HELIX   10  10 GLU A  495  CYS A  499  5                                   5    
HELIX   11  11 ARG H   83  THR H   87  5                                   5    
HELIX   12  12 SER H  156  ALA H  158  5                                   3    
HELIX   13  13 SER H  187  LEU H  189  5                                   3    
HELIX   14  14 LYS H  201  ASN H  204  5                                   4    
HELIX   15  15 GLN L   79  PHE L   83  5                                   5    
HELIX   16  16 SER L  121  LYS L  126  1                                   6    
HELIX   17  17 LYS L  183  LYS L  188  1                                   6    
SHEET    1   A 5 VAL A 312  ASN A 314  0                                        
SHEET    2   A 5 SER A 340  SER A 342  1  O  SER A 342   N  CYS A 313           
SHEET    3   A 5 GLU A 376  ILE A 377  1  O  GLU A 376   N  ILE A 341           
SHEET    4   A 5 ILE A 401  ILE A 402  1  O  ILE A 401   N  ILE A 377           
SHEET    5   A 5 GLU A 431  ILE A 432  1  O  GLU A 431   N  ILE A 402           
SHEET    1   B 5 LEU A 345  ILE A 347  0                                        
SHEET    2   B 5 LEU A 381  ILE A 383  1  O  LEU A 382   N  LEU A 345           
SHEET    3   B 5 PHE A 412  VAL A 417  1  O  ALA A 415   N  ILE A 383           
SHEET    4   B 5 ASP A 436  SER A 440  1  O  ILE A 438   N  LEU A 414           
SHEET    5   B 5 THR A 464  ILE A 467  1  O  LYS A 465   N  ILE A 439           
SHEET    1   C 4 GLN H   3  SER H   7  0                                        
SHEET    2   C 4 LEU H  18  SER H  25 -1  O  ALA H  23   N  VAL H   5           
SHEET    3   C 4 THR H  77  MET H  82 -1  O  MET H  82   N  LEU H  18           
SHEET    4   C 4 PHE H  67  ASP H  72 -1  N  THR H  68   O  GLN H  81           
SHEET    1   D 6 LEU H  11  VAL H  12  0                                        
SHEET    2   D 6 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3   D 6 ALA H  88  GLU H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   D 6 TRP H  33  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5   D 6 LEU H  45  SER H  52 -1  O  LEU H  48   N  TRP H  36           
SHEET    6   D 6 TYR H  56  TYR H  59 -1  O  ASP H  58   N  GLU H  50           
SHEET    1   E 4 LEU H  11  VAL H  12  0                                        
SHEET    2   E 4 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3   E 4 ALA H  88  GLU H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   E 4 MET H 100D TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1   F 4 SER H 120  LEU H 124  0                                        
SHEET    2   F 4 THR H 135  TYR H 145 -1  O  LYS H 143   N  SER H 120           
SHEET    3   F 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4   F 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1   G 4 SER H 120  LEU H 124  0                                        
SHEET    2   G 4 THR H 135  TYR H 145 -1  O  LYS H 143   N  SER H 120           
SHEET    3   G 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4   G 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  SER H 177           
SHEET    1   H 3 THR H 151  TRP H 154  0                                        
SHEET    2   H 3 ILE H 195  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3   H 3 THR H 205  LYS H 210 -1  O  VAL H 207   N  VAL H 198           
SHEET    1   I 4 MET L   4  SER L   7  0                                        
SHEET    2   I 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3   I 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4   I 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1   J 6 SER L  10  SER L  14  0                                        
SHEET    2   J 6 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3   J 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  VAL L 104           
SHEET    4   J 6 VAL L  33  GLN L  38 -1  N  GLN L  38   O  THR L  85           
SHEET    5   J 6 LYS L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6   J 6 PHE L  53  LEU L  54 -1  O  PHE L  53   N  TYR L  49           
SHEET    1   K 4 SER L 114  PHE L 118  0                                        
SHEET    2   K 4 THR L 129  PHE L 139 -1  O  ASN L 137   N  SER L 114           
SHEET    3   K 4 TYR L 173  SER L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4   K 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   L 4 ALA L 153  LEU L 154  0                                        
SHEET    2   L 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   L 4 VAL L 191  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    4   L 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS A  313    CYS A  338                          1555   1555  2.00  
SSBOND   2 CYS A  446    CYS A  475                          1555   1555  2.06  
SSBOND   3 CYS A  482    CYS A  491                          1555   1555  2.07  
SSBOND   4 CYS A  486    CYS A  499                          1555   1555  2.03  
SSBOND   5 CYS H   22    CYS H   92                          1555   1555  2.03  
SSBOND   6 CYS H  140    CYS H  196                          1555   1555  2.05  
SSBOND   7 CYS L   23    CYS L   88                          1555   1555  2.08  
SSBOND   8 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN A 389                 C1  NAG A3891     1555   1555  1.44  
LINK         O4  NAG A3281                 C1  NAG A3282     1555   1555  1.44  
LINK         O3  NAG A3891                 C1  NAG A3893     1555   1555  1.44  
LINK         ND2 ASN A 328                 C1  NAG A3281     1555   1555  1.45  
LINK         O4  NAG A4201                 C1  NAG A4202     1555   1555  1.46  
LINK         ND2 ASN A 420                 C1  NAG A4201     1555   1555  1.46  
LINK         O6  NAG A3891                 C1  FUL A3892     1555   1555  1.42  
CISPEP   1 PHE H  146    PRO H  147          0        -5.70                     
CISPEP   2 GLU H  148    PRO H  149          0        -2.88                     
CISPEP   3 SER L    7    PRO L    8          0        -4.39                     
CISPEP   4 GLU L   92    PRO L   93          0        -8.76                     
CISPEP   5 GLU L   94    PRO L   95          0         2.62                     
CISPEP   6 TYR L  140    PRO L  141          0         2.83                     
SITE     1 AC1 11 SER A 324  LEU A 325  SER A 326  ASN A 328                    
SITE     2 AC1 11 THR A 330  ASN A 331  THR A 358  THR A 360                    
SITE     3 AC1 11 HOH A 543  HOH A 581  NAG A3282                               
SITE     1 AC2  4 ASP A 323  HOH A 686  HOH A 916  NAG A3281                    
SITE     1 AC3  9 ASN A 389  ARG A 390  HOH A 696  HOH A 817                    
SITE     2 AC3  9 HOH A1080  FUL A3892  NAG A3893  PRO H 119                    
SITE     3 AC3  9 SER H 120                                                     
SITE     1 AC4  8 HOH A 973  HOH A1080  NAG A3891  SER H 120                    
SITE     2 AC4  8 VAL H 121  PHE H 122  LYS H 209  GLU L 123                    
SITE     1 AC5  3 GLN A 366  NAG A3891  LYS H 117                               
SITE     1 AC6 11 GLU A 388  ASN A 389  ASN A 420  THR A 422                    
SITE     2 AC6 11 ASN A 444  HOH A 557  HOH A1059  NAG A4202                    
SITE     3 AC6 11 SER H 203  ASN H 204  HOH H 981                               
SITE     1 AC7  4 NAG A4201  SER H 203  ASN H 204  HOH H 981                    
SITE     1 AC8  5 ASN H 155  ALA H 158  GLN H 192  HOH H 569                    
SITE     2 AC8  5 HOH H 692                                                     
CRYST1   81.934  200.677   49.426  90.00  90.00  90.00 P 21 21 2     4          
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      0.012205  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004983  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020232        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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