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Database: PDB
Entry: 3KME
LinkDB: 3KME
Original site: 3KME 
HEADER    HYDROLASE                               10-NOV-09   3KME              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF TACE WITH PHENYL-            
TITLE    2 PYRROLIDINYL-TARTRATE INHIBITOR                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TNF-ALPHA-CONVERTING ENZYME;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 215-476;                                          
COMPND   5 SYNONYM: ADAM 17, DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING
COMPND   6 PROTEIN 17, TNF-ALPHA CONVERTASE, SNAKE VENOM-LIKE PROTEASE;         
COMPND   7 EC: 3.4.24.86;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADAM17, CSVP, TACE;                                            
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    A DISINTEGRIN AND METALLOPROTEINASE DOMAIN 17, TNF-ALPHA-CONVERTING   
KEYWDS   2 ENZYME, TNF-ALPHA CONVERTASE, SNAKE VENOM-LIKE PROTEASE, CLEAVAGE ON 
KEYWDS   3 PAIR OF BASIC RESIDUES, GLYCOPROTEIN, MEMBRANE, METAL-BINDING,       
KEYWDS   4 METALLOPROTEASE, NOTCH SIGNALING PATHWAY, PHOSPHOPROTEIN, PROTEASE,  
KEYWDS   5 ZYMOGEN, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ORTH                                                                
REVDAT   3   13-JUL-11 3KME    1       VERSN                                    
REVDAT   2   26-JAN-10 3KME    1       JRNL                                     
REVDAT   1   22-DEC-09 3KME    0                                                
JRNL        AUTH   K.E.ROSNER,Z.GUO,P.ORTH,G.W.SHIPPS,D.B.BELANGER,T.Y.CHAN,    
JRNL        AUTH 2 P.J.CURRAN,C.DAI,Y.DENG,V.M.GIRIJAVALLABHAN,L.HONG,          
JRNL        AUTH 3 B.J.LAVEY,J.F.LEE,D.LI,Z.LIU,J.POPOVICI-MULLER,P.C.TING,     
JRNL        AUTH 4 H.VACCARO,L.WANG,T.WANG,W.YU,G.ZHOU,X.NIU,J.SUN,             
JRNL        AUTH 5 J.A.KOZLOWSKI,D.J.LUNDELL,V.MADISON,B.MCKITTRICK,            
JRNL        AUTH 6 J.J.PIWINSKI,N.Y.SHIH,M.ARSHAD SIDDIQUI,C.O.STRICKLAND       
JRNL        TITL   THE DISCOVERY OF NOVEL TARTRATE-BASED TNF-ALPHA CONVERTING   
JRNL        TITL 2 ENZYME (TACE) INHIBITORS.                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  1189 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   20022498                                                     
JRNL        DOI    10.1016/J.BMCL.2009.12.004                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 49216                          
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)  : NULL                           
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.225                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 1.940                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 955                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : NULL                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : NULL                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL                     
REMARK   3   BIN R VALUE               (WORKING SET) : NULL                     
REMARK   3   BIN FREE R VALUE                        : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3883                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.64                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.18150                                             
REMARK   3    B22 (A**2) : 1.27360                                              
REMARK   3    B33 (A**2) : 2.90780                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.23                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056172.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49397                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: 1BKC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6000, 10% 2-PROPANOL, 100 MM     
REMARK 280  SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, TEMPERATURE 295K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       35.74250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.36100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.10650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.36100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.74250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.10650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A   215                                                      
REMARK 465     ALA A   216                                                      
REMARK 465     ASP A   217                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     ALA A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     ASN A   475                                                      
REMARK 465     LYS A   476                                                      
REMARK 465     GLY A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 465     HIS A   479                                                      
REMARK 465     HIS A   480                                                      
REMARK 465     HIS A   481                                                      
REMARK 465     HIS A   482                                                      
REMARK 465     HIS A   483                                                      
REMARK 465     HIS A   484                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     ASP B   217                                                      
REMARK 465     PRO B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     SER B   474                                                      
REMARK 465     ASN B   475                                                      
REMARK 465     LYS B   476                                                      
REMARK 465     GLY B   477                                                      
REMARK 465     SER B   478                                                      
REMARK 465     HIS B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     HIS B   481                                                      
REMARK 465     HIS B   482                                                      
REMARK 465     HIS B   483                                                      
REMARK 465     HIS B   484                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     GLU A 307    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 308    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 309    CE   NZ                                             
REMARK 470     HIS A 361    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 427    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 429    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 445    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 448    CE   NZ                                             
REMARK 470     GLN A 456    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     MET B 221    CG   SD   CE                                        
REMARK 470     LYS B 222    CG   CD   CE   NZ                                   
REMARK 470     ARG B 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 286    CE   NZ                                             
REMARK 470     SER B 287    OG                                                  
REMARK 470     GLU B 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 470     GLU B 308    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     LYS B 315    CE   NZ                                             
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 331    NZ                                                  
REMARK 470     LYS B 367    CE   NZ                                             
REMARK 470     LYS B 392    CG   CD   CE   NZ                                   
REMARK 470     GLU B 422    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 427    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 445    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 460    CG   CD   CE   NZ                                   
REMARK 470     GLU B 463    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 467    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 472    CG   CD   OE1  OE2                                  
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    ALA A 270     -113.69   -133.53                                   
REMARK 500    CYS A 365      123.12     75.36                                   
REMARK 500    ASN A 381       54.03    -94.98                                   
REMARK 500    ALA B 270     -105.58   -139.60                                   
REMARK 500    CYS B 365      121.97     81.32                                   
REMARK 500    ALA B 424       71.02   -153.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    MET A 435        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 521        DISTANCE =  6.49 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 405   NE2                                                    
REMARK 620 2 HIS A 409   NE2  95.3                                              
REMARK 620 3 HIS A 415   NE2  99.5  99.1                                        
REMARK 620 4 INN A 485   O    93.7 169.1  85.4                                  
REMARK 620 5 INN A 485   O4   94.8  95.8 158.3  77.4                            
REMARK 620 6 HOH A 492   O   176.1  86.0  83.9  84.6  81.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 405   NE2                                                    
REMARK 620 2 HIS B 409   NE2  95.7                                              
REMARK 620 3 HIS B 415   NE2 103.5  94.8                                        
REMARK 620 4 Z59 B 485   O19  92.0 172.0  85.6                                  
REMARK 620 5 Z59 B 485   O17  99.2 101.3 150.6  75.1                            
REMARK 620 6 Z59 B 485   O11 168.6  93.3  82.5  78.8  72.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-            
REMARK 630 METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-ALANINAMIDE     
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     INN A   485                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    2HM TBG ALA EDN                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INN A 485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z59 B 485                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KMC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF TACE WITH TARTRATE          
REMARK 900 RELATED ID: 1BKC   RELATED DB: PDB                                   
REMARK 900 CATALYTIC DOMAIN OF TNF-ALPHA CONVERTING ENZYME (TACE)               
REMARK 900 RELATED ID: 3EWJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF TACE WITH                   
REMARK 900 CARBOXYLATE INHIBITOR                                                
REMARK 900 RELATED ID: 2FV9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STUCTURE OF TACE IN COMPLEX WITH JMV 390-1                   
DBREF  3KME A  215   476  UNP    P78536   ADA17_HUMAN    215    476             
DBREF  3KME B  215   476  UNP    P78536   ADA17_HUMAN    215    476             
SEQADV 3KME ALA A  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 3KME GLY A  353  UNP  P78536    VAL   353 ENGINEERED                     
SEQADV 3KME GLN A  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQADV 3KME GLY A  477  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME SER A  478  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  479  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  480  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  481  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  482  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  483  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS A  484  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME ALA B  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 3KME GLY B  353  UNP  P78536    VAL   353 ENGINEERED                     
SEQADV 3KME GLN B  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQADV 3KME GLY B  477  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME SER B  478  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  479  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  480  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  481  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  482  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  483  UNP  P78536              EXPRESSION TAG                 
SEQADV 3KME HIS B  484  UNP  P78536              EXPRESSION TAG                 
SEQRES   1 A  270  ARG ALA ASP PRO ASP PRO MET LYS ASN THR CYS LYS LEU          
SEQRES   2 A  270  LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG TYR MET GLY          
SEQRES   3 A  270  ARG GLY GLU GLU SER THR THR THR ASN TYR LEU ILE GLU          
SEQRES   4 A  270  LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG ASN THR ALA          
SEQRES   5 A  270  TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE          
SEQRES   6 A  270  GLU GLN ILE ARG ILE LEU LYS SER PRO GLN GLU VAL LYS          
SEQRES   7 A  270  PRO GLY GLU LYS HIS TYR ASN MET ALA LYS SER TYR PRO          
SEQRES   8 A  270  ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS MET LEU LEU          
SEQRES   9 A  270  GLU GLN PHE SER PHE ASP ILE ALA GLU GLU ALA SER LYS          
SEQRES  10 A  270  VAL CYS LEU ALA HIS LEU PHE THR TYR GLN ASP PHE ASP          
SEQRES  11 A  270  MET GLY THR LEU GLY LEU ALA TYR GLY GLY SER PRO ARG          
SEQRES  12 A  270  ALA ASN SER HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR          
SEQRES  13 A  270  SER PRO VAL GLY LYS LYS ASN ILE TYR LEU ASN SER GLY          
SEQRES  14 A  270  LEU THR SER THR LYS ASN TYR GLY LYS THR ILE LEU THR          
SEQRES  15 A  270  LYS GLU ALA ASP LEU VAL THR THR HIS GLU LEU GLY HIS          
SEQRES  16 A  270  ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU          
SEQRES  17 A  270  CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS TYR VAL MET          
SEQRES  18 A  270  TYR PRO ILE ALA VAL SER GLY ASP HIS GLU ASN ASN LYS          
SEQRES  19 A  270  MET PHE SER GLN CYS SER LYS GLN SER ILE TYR LYS THR          
SEQRES  20 A  270  ILE GLU SER LYS ALA GLN GLU CYS PHE GLN GLU ARG SER          
SEQRES  21 A  270  ASN LYS GLY SER HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  270  ARG ALA ASP PRO ASP PRO MET LYS ASN THR CYS LYS LEU          
SEQRES   2 B  270  LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG TYR MET GLY          
SEQRES   3 B  270  ARG GLY GLU GLU SER THR THR THR ASN TYR LEU ILE GLU          
SEQRES   4 B  270  LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG ASN THR ALA          
SEQRES   5 B  270  TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE          
SEQRES   6 B  270  GLU GLN ILE ARG ILE LEU LYS SER PRO GLN GLU VAL LYS          
SEQRES   7 B  270  PRO GLY GLU LYS HIS TYR ASN MET ALA LYS SER TYR PRO          
SEQRES   8 B  270  ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS MET LEU LEU          
SEQRES   9 B  270  GLU GLN PHE SER PHE ASP ILE ALA GLU GLU ALA SER LYS          
SEQRES  10 B  270  VAL CYS LEU ALA HIS LEU PHE THR TYR GLN ASP PHE ASP          
SEQRES  11 B  270  MET GLY THR LEU GLY LEU ALA TYR GLY GLY SER PRO ARG          
SEQRES  12 B  270  ALA ASN SER HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR          
SEQRES  13 B  270  SER PRO VAL GLY LYS LYS ASN ILE TYR LEU ASN SER GLY          
SEQRES  14 B  270  LEU THR SER THR LYS ASN TYR GLY LYS THR ILE LEU THR          
SEQRES  15 B  270  LYS GLU ALA ASP LEU VAL THR THR HIS GLU LEU GLY HIS          
SEQRES  16 B  270  ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU          
SEQRES  17 B  270  CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS TYR VAL MET          
SEQRES  18 B  270  TYR PRO ILE ALA VAL SER GLY ASP HIS GLU ASN ASN LYS          
SEQRES  19 B  270  MET PHE SER GLN CYS SER LYS GLN SER ILE TYR LYS THR          
SEQRES  20 B  270  ILE GLU SER LYS ALA GLN GLU CYS PHE GLN GLU ARG SER          
SEQRES  21 B  270  ASN LYS GLY SER HIS HIS HIS HIS HIS HIS                      
HET     ZN  A   1       1                                                       
HET    INN  A 485      29                                                       
HET    IPA  A   7       4                                                       
HET     ZN  B   2       1                                                       
HET    Z59  B 485      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     INN N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-                       
HETNAM   2 INN  METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-           
HETNAM   3 INN  ALANINAMIDE                                                     
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETNAM     Z59 (2R,3R)-2,3-DIHYDROXY-4-OXO-4-[(2R)-2-PHENYLPYRROLIDIN-          
HETNAM   2 Z59  1-YL]-N-(THIOPHEN-2-YLMETHYL)BUTANAMIDE                         
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  INN    C19 H37 N5 O5                                                
FORMUL   5  IPA    C3 H8 O                                                      
FORMUL   7  Z59    C19 H22 N2 O4 S                                              
FORMUL   8  HOH   *299(H2 O)                                                    
HELIX    1   1 ASP A  219  LYS A  222  5                                   4    
HELIX    2   2 ASP A  232  MET A  239  1                                   8    
HELIX    3   3 GLU A  243  THR A  265  1                                  23    
HELIX    4   4 ASP A  313  SER A  330  1                                  18    
HELIX    5   5 PHE A  343  THR A  347  5                                   5    
HELIX    6   6 LEU A  395  PHE A  411  1                                  17    
HELIX    7   7 ASN A  426  GLY A  430  5                                   5    
HELIX    8   8 SER A  451  PHE A  470  1                                  20    
HELIX    9   9 ASP B  232  GLY B  240  1                                   9    
HELIX   10  10 GLU B  243  ASN B  264  1                                  22    
HELIX   11  11 ASP B  313  ILE B  325  1                                  13    
HELIX   12  12 ILE B  325  SER B  330  1                                   6    
HELIX   13  13 PHE B  343  THR B  347  5                                   5    
HELIX   14  14 LEU B  395  PHE B  411  1                                  17    
HELIX   15  15 ASN B  426  GLY B  430  5                                   5    
HELIX   16  16 HIS B  444  MET B  449  5                                   6    
HELIX   17  17 SER B  451  PHE B  470  1                                  20    
SHEET    1   A 5 GLY A 276  ILE A 284  0                                        
SHEET    2   A 5 THR A 224  ALA A 231  1  N  CYS A 225   O  GLY A 276           
SHEET    3   A 5 LEU A 334  THR A 339  1  O  PHE A 338   N  VAL A 230           
SHEET    4   A 5 SER A 382  SER A 386  1  O  GLY A 383   N  LEU A 337           
SHEET    5   A 5 GLY A 349  ALA A 351 -1  N  LEU A 350   O  LEU A 384           
SHEET    1   B 2 ALA A 368  SER A 371  0                                        
SHEET    2   B 2 LYS A 376  TYR A 379 -1  O  LYS A 376   N  SER A 371           
SHEET    1   C 2 LYS A 388  ASN A 389  0                                        
SHEET    2   C 2 LYS A 392  THR A 393 -1  O  LYS A 392   N  ASN A 389           
SHEET    1   D 5 GLY B 276  ILE B 284  0                                        
SHEET    2   D 5 THR B 224  ALA B 231  1  N  LEU B 227   O  GLU B 280           
SHEET    3   D 5 LEU B 334  THR B 339  1  O  PHE B 338   N  VAL B 230           
SHEET    4   D 5 SER B 382  SER B 386  1  O  THR B 385   N  THR B 339           
SHEET    5   D 5 GLY B 349  ALA B 351 -1  N  LEU B 350   O  LEU B 384           
SHEET    1   E 2 ALA B 368  SER B 371  0                                        
SHEET    2   E 2 LYS B 376  TYR B 379 -1  O  ILE B 378   N  TYR B 369           
SHEET    1   F 2 LYS B 388  ASN B 389  0                                        
SHEET    2   F 2 LYS B 392  THR B 393 -1  O  LYS B 392   N  ASN B 389           
SSBOND   1 CYS A  225    CYS A  333                          1555   1555  2.04  
SSBOND   2 CYS A  365    CYS A  469                          1555   1555  2.03  
SSBOND   3 CYS A  423    CYS A  453                          1555   1555  2.02  
SSBOND   4 CYS B  225    CYS B  333                          1555   1555  2.06  
SSBOND   5 CYS B  365    CYS B  469                          1555   1555  2.03  
SSBOND   6 CYS B  423    CYS B  453                          1555   1555  2.03  
LINK         NE2 HIS A 405                ZN    ZN A   1     1555   1555  2.12  
LINK         NE2 HIS A 409                ZN    ZN A   1     1555   1555  2.03  
LINK         NE2 HIS A 415                ZN    ZN A   1     1555   1555  2.14  
LINK         NE2 HIS B 405                ZN    ZN B   2     1555   1555  2.04  
LINK         NE2 HIS B 409                ZN    ZN B   2     1555   1555  2.16  
LINK         NE2 HIS B 415                ZN    ZN B   2     1555   1555  2.14  
LINK        ZN    ZN A   1                 O   INN A 485     1555   1555  2.04  
LINK        ZN    ZN A   1                 O4  INN A 485     1555   1555  2.22  
LINK        ZN    ZN B   2                 O19 Z59 B 485     1555   1555  2.28  
LINK        ZN    ZN B   2                 O17 Z59 B 485     1555   1555  2.20  
LINK        ZN    ZN B   2                 O11 Z59 B 485     1555   1555  2.40  
LINK        ZN    ZN A   1                 O   HOH A 492     1555   1555  2.46  
CISPEP   1 TYR A  304    PRO A  305          0         6.22                     
CISPEP   2 TYR B  304    PRO B  305          0         4.32                     
CISPEP   3 SER B  355    PRO B  356          0         2.19                     
SITE     1 AC1  5 HIS A 405  HIS A 409  HIS A 415  INN A 485                    
SITE     2 AC1  5 HOH A 492                                                     
SITE     1 AC2 24  ZN A   1  HOH A  80  HOH A 167  GLU A 327                    
SITE     2 AC2 24 SER A 330  MET A 345  GLY A 346  THR A 347                    
SITE     3 AC2 24 LEU A 348  GLY A 349  ASN A 389  TYR A 390                    
SITE     4 AC2 24 HIS A 405  GLU A 406  HIS A 409  HIS A 415                    
SITE     5 AC2 24 TYR A 436  PRO A 437  ILE A 438  ALA A 439                    
SITE     6 AC2 24 HOH A 490  HOH A 491  HOH A 492  ARG B 357                    
SITE     1 AC3  5 LEU A 285  LYS A 286  SER A 287  PRO A 288                    
SITE     2 AC3  5 ASN A 299                                                     
SITE     1 AC4  4 HIS B 405  HIS B 409  HIS B 415  Z59 B 485                    
SITE     1 AC5 14  ZN B   2  LEU B 348  GLY B 349  HIS B 405                    
SITE     2 AC5 14 GLU B 406  HIS B 409  HIS B 415  VAL B 434                    
SITE     3 AC5 14 TYR B 436  PRO B 437  ILE B 438  ALA B 439                    
SITE     4 AC5 14 HOH B 543  HOH B 546                                          
CRYST1   71.485   76.213  104.722  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009549        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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