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Database: PDB
Entry: 2A8H
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Original site: 2A8H 
HEADER    HYDROLASE                               08-JUL-05   2A8H              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF TACE WITH                    
TITLE    2 THIOMORPHOLINE SULFONAMIDE HYDROXAMATE INHIBITOR                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADAM 17;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: A DISINTEGRIN AND METALLOPROTEINASE DOMAIN 17,              
COMPND   6 TNF-ALPHA CONVERTING ENZYME, TNF-ALPHA CONVERTASE, SNAKE             
COMPND   7 VENOM-LIKE PROTEASE, CD156B ANTIGEN;                                 
COMPND   8 EC: 3.4.24.86;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TACE/ADAM-17, TACE-INHIBITOR COMPLEX, ZN-ENDOPEPTIDASE,               
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.I.LEVIN,J.M.CHEN,L.M.LAAKSO,M.DU,J.SCHMID,W.XU,T.CUMMONS,           
AUTHOR   2 J.XU,G.JIN,D.BARONE,J.S.SKOTNICKI                                    
REVDAT   3   24-FEB-09 2A8H    1       VERSN                                    
REVDAT   2   28-FEB-06 2A8H    1       JRNL                                     
REVDAT   1   07-FEB-06 2A8H    0                                                
JRNL        AUTH   J.I.LEVIN,J.M.CHEN,L.M.LAAKSO,M.DU,J.SCHMID,W.XU,            
JRNL        AUTH 2 T.CUMMONS,J.XU,G.JIN,D.BARONE,J.S.SKOTNICKI                  
JRNL        TITL   ACETYLENIC TACE INHIBITORS. PART 3: THIOMORPHOLINE           
JRNL        TITL 2 SULFONAMIDE HYDROXAMATES.                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  1605 2006              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16426848                                                     
JRNL        DOI    10.1016/J.BMCL.2005.12.020                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.COWLING,D.BARONE,R.A.BLACK,J.S.SKOTNICKI                   
REMARK   1  TITL   ACETYLENIC TACE INHIBITORS. PART 2. SAR OF                   
REMARK   1  TITL 2 6-MEMBERED CYCLIC SULFONAMIDE HYDROXAMATES.                  
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24593                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1313                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1689                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4094                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.79000                                              
REMARK   3    B22 (A**2) : -0.70000                                             
REMARK   3    B33 (A**2) : -1.10000                                             
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): 0.385         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.275         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.129         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.111         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4250 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5747 ; 1.523 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   514 ; 6.419 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;35.576 ;25.096       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   726 ;16.855 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;21.233 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   592 ; 0.141 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3268 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2061 ; 0.216 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2902 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   264 ; 0.156 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.116 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    45 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.326 ; 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):  2653 ; 0.861 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4115 ; 1.388 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1847 ; 1.793 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1632 ; 2.759 ; 4.500       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2A8H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033619.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31529                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05700                            
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
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   (%): 42.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, NACITRATE,        
REMARK 280  PH 5.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K             
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       24.18350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.00550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.60450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.00550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.18350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.60450            
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 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 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     LYS A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     GLY A   478                                                      
REMARK 465     SER 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     HIS A   485                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     ASP B   217                                                      
REMARK 465     ASN B   475                                                      
REMARK 465     LYS B   476                                                      
REMARK 465     VAL B   477                                                      
REMARK 465     GLY B   478                                                      
REMARK 465     SER 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 465     HIS B   485                                                      
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   OG   SER B   371     O    LYS B   376              1.70            
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    ALA A 270     -109.36   -134.05                                   
REMARK 500    TRP A 312      164.42    -46.00                                   
REMARK 500    MET A 345       38.55     39.33                                   
REMARK 500    CYS A 365      124.90     93.19                                   
REMARK 500    PRO B 220     -174.49    -57.11                                   
REMARK 500    MET B 221      -25.58     63.46                                   
REMARK 500    ASN B 269       16.94     50.82                                   
REMARK 500    ALA B 270     -109.84   -130.23                                   
REMARK 500    ALA B 358       41.21    -83.53                                   
REMARK 500    ASN B 359        8.08   -155.46                                   
REMARK 500    CYS B 365      116.72     77.36                                   
REMARK 500    SER B 371      -41.19    141.86                                   
REMARK 500    PRO B 372       98.34    -23.24                                   
REMARK 500    VAL B 373      -62.19   -109.05                                   
REMARK 500    LYS B 376      146.53    106.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO B  372     VAL B  373                  101.75                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 486  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 405   NE2                                                    
REMARK 620 2 HIS A 409   NE2 103.3                                              
REMARK 620 3 HIS A 415   NE2  97.3  91.5                                        
REMARK 620 4 4NH A 158   O4  134.3 122.1  78.2                                  
REMARK 620 5 4NH A 158   O5  109.8  82.8 152.9  82.4                            
REMARK 620 6 4NH A 158   N3  111.2 112.9 135.6  57.4  32.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 486  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 405   NE2                                                    
REMARK 620 2 HIS B 409   NE2 103.8                                              
REMARK 620 3 HIS B 415   NE2  97.2 103.1                                        
REMARK 620 4 4NH B 159   O5  107.9  77.0 154.2                                  
REMARK 620 5 4NH B 159   O4  126.0 130.2  74.3  85.9                            
REMARK 620 6 4NH B 159   N3  108.2 108.2 132.8  32.6  58.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 486                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 486                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NH A 158                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4NH B 159                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BKC   RELATED DB: PDB                                   
REMARK 900 TACE CATALYTIC DOMAIN WITH TAPI                                      
REMARK 900 RELATED ID: 1ZXC   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TACE WITH DIFFERENT INHIBITOR                           
DBREF  2A8H A  215   477  UNP    P78536   ADA17_HUMAN    215    477             
DBREF  2A8H B  215   477  UNP    P78536   ADA17_HUMAN    215    477             
SEQADV 2A8H ALA A  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 2A8H GLN A  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQADV 2A8H GLY A  478  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H SER A  479  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  480  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  481  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  482  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  483  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  484  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS A  485  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H ALA B  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 2A8H GLN B  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQADV 2A8H GLY B  478  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H SER B  479  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  480  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  481  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  482  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  483  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  484  UNP  P78536              EXPRESSION TAG                 
SEQADV 2A8H HIS B  485  UNP  P78536              EXPRESSION TAG                 
SEQRES   1 A  271  ARG ALA ASP PRO ASP PRO MET LYS ASN THR CYS LYS LEU          
SEQRES   2 A  271  LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG TYR MET GLY          
SEQRES   3 A  271  ARG GLY GLU GLU SER THR THR THR ASN TYR LEU ILE GLU          
SEQRES   4 A  271  LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG ASN THR ALA          
SEQRES   5 A  271  TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE          
SEQRES   6 A  271  GLU GLN ILE ARG ILE LEU LYS SER PRO GLN GLU VAL LYS          
SEQRES   7 A  271  PRO GLY GLU LYS HIS TYR ASN MET ALA LYS SER TYR PRO          
SEQRES   8 A  271  ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS MET LEU LEU          
SEQRES   9 A  271  GLU GLN PHE SER PHE ASP ILE ALA GLU GLU ALA SER LYS          
SEQRES  10 A  271  VAL CYS LEU ALA HIS LEU PHE THR TYR GLN ASP PHE ASP          
SEQRES  11 A  271  MET GLY THR LEU GLY LEU ALA TYR VAL GLY SER PRO ARG          
SEQRES  12 A  271  ALA ASN SER HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR          
SEQRES  13 A  271  SER PRO VAL GLY LYS LYS ASN ILE TYR LEU ASN SER GLY          
SEQRES  14 A  271  LEU THR SER THR LYS ASN TYR GLY LYS THR ILE LEU THR          
SEQRES  15 A  271  LYS GLU ALA ASP LEU VAL THR THR HIS GLU LEU GLY HIS          
SEQRES  16 A  271  ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU          
SEQRES  17 A  271  CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS TYR VAL MET          
SEQRES  18 A  271  TYR PRO ILE ALA VAL SER GLY ASP HIS GLU ASN ASN LYS          
SEQRES  19 A  271  MET PHE SER GLN CYS SER LYS GLN SER ILE TYR LYS THR          
SEQRES  20 A  271  ILE GLU SER LYS ALA GLN GLU CYS PHE GLN GLU ARG SER          
SEQRES  21 A  271  ASN LYS VAL GLY SER HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  271  ARG ALA ASP PRO ASP PRO MET LYS ASN THR CYS LYS LEU          
SEQRES   2 B  271  LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG TYR MET GLY          
SEQRES   3 B  271  ARG GLY GLU GLU SER THR THR THR ASN TYR LEU ILE GLU          
SEQRES   4 B  271  LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG ASN THR ALA          
SEQRES   5 B  271  TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE          
SEQRES   6 B  271  GLU GLN ILE ARG ILE LEU LYS SER PRO GLN GLU VAL LYS          
SEQRES   7 B  271  PRO GLY GLU LYS HIS TYR ASN MET ALA LYS SER TYR PRO          
SEQRES   8 B  271  ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS MET LEU LEU          
SEQRES   9 B  271  GLU GLN PHE SER PHE ASP ILE ALA GLU GLU ALA SER LYS          
SEQRES  10 B  271  VAL CYS LEU ALA HIS LEU PHE THR TYR GLN ASP PHE ASP          
SEQRES  11 B  271  MET GLY THR LEU GLY LEU ALA TYR VAL GLY SER PRO ARG          
SEQRES  12 B  271  ALA ASN SER HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR          
SEQRES  13 B  271  SER PRO VAL GLY LYS LYS ASN ILE TYR LEU ASN SER GLY          
SEQRES  14 B  271  LEU THR SER THR LYS ASN TYR GLY LYS THR ILE LEU THR          
SEQRES  15 B  271  LYS GLU ALA ASP LEU VAL THR THR HIS GLU LEU GLY HIS          
SEQRES  16 B  271  ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU          
SEQRES  17 B  271  CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS TYR VAL MET          
SEQRES  18 B  271  TYR PRO ILE ALA VAL SER GLY ASP HIS GLU ASN ASN LYS          
SEQRES  19 B  271  MET PHE SER GLN CYS SER LYS GLN SER ILE TYR LYS THR          
SEQRES  20 B  271  ILE GLU SER LYS ALA GLN GLU CYS PHE GLN GLU ARG SER          
SEQRES  21 B  271  ASN LYS VAL GLY SER HIS HIS HIS HIS HIS HIS                  
HET     ZN  A 486       1                                                       
HET     ZN  B 486       1                                                       
HET    4NH  A 158      27                                                       
HET    4NH  B 159      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     4NH 4-({4-[(4-AMINOBUT-2-YNYL)OXY]PHENYL}SULFONYL)-N-                
HETNAM   2 4NH  HYDROXY-2,2-DIMETHYLTHIOMORPHOLINE-3-CARBOXAMIDE                
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  4NH    2(C17 H23 N3 O5 S2)                                          
FORMUL   7  HOH   *147(H2 O)                                                    
HELIX    1   1 ASP A  232  MET A  239  1                                   8    
HELIX    2   2 GLU A  243  ASN A  264  1                                  22    
HELIX    3   3 ASP A  313  ILE A  325  1                                  13    
HELIX    4   4 ILE A  325  SER A  330  1                                   6    
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 LEU A  420  ALA A  424  5                                   5    
HELIX    8   8 ASN A  426  GLY A  430  5                                   5    
HELIX    9   9 HIS A  444  MET A  449  5                                   6    
HELIX   10  10 SER A  451  PHE A  470  1                                  20    
HELIX   11  11 ASP B  232  MET B  239  1                                   8    
HELIX   12  12 GLU B  243  ASN B  264  1                                  22    
HELIX   13  13 ASP B  313  ILE B  325  1                                  13    
HELIX   14  14 ILE B  325  SER B  330  1                                   6    
HELIX   15  15 PHE B  343  THR B  347  5                                   5    
HELIX   16  16 LEU B  395  PHE B  411  1                                  17    
HELIX   17  17 LEU B  420  ALA B  424  5                                   5    
HELIX   18  18 ASN B  426  GLY B  430  5                                   5    
HELIX   19  19 HIS B  444  MET B  449  5                                   6    
HELIX   20  20 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  LEU A 227   O  GLN A 278           
SHEET    3   A 5 LEU A 334  THR A 339  1  O  HIS A 336   N  LEU A 228           
SHEET    4   A 5 SER A 382  SER A 386  1  O  THR A 385   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 TYR A 369  SER A 371  0                                        
SHEET    2   B 2 LYS A 376  ILE A 378 -1  O  ILE A 378   N  TYR A 369           
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  VAL B 229   O  ARG B 283           
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  TYR B 369  0                                        
SHEET    2   E 2 ILE B 378  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  2.06  
SSBOND   3 CYS A  423    CYS A  453                          1555   1555  2.10  
LINK         NE2 HIS A 405                ZN    ZN A 486     1555   1555  2.10  
LINK         NE2 HIS A 409                ZN    ZN A 486     1555   1555  2.16  
LINK         NE2 HIS A 415                ZN    ZN A 486     1555   1555  1.86  
LINK         NE2 HIS B 405                ZN    ZN B 486     1555   1555  2.31  
LINK         NE2 HIS B 409                ZN    ZN B 486     1555   1555  1.98  
LINK         NE2 HIS B 415                ZN    ZN B 486     1555   1555  2.15  
LINK        ZN    ZN A 486                 O4  4NH A 158     1555   1555  2.11  
LINK        ZN    ZN A 486                 O5  4NH A 158     1555   1555  1.96  
LINK        ZN    ZN B 486                 O5  4NH B 159     1555   1555  1.85  
LINK        ZN    ZN B 486                 O4  4NH B 159     1555   1555  2.09  
LINK        ZN    ZN A 486                 N3  4NH A 158     1555   1555  2.60  
LINK        ZN    ZN B 486                 N3  4NH B 159     1555   1555  2.55  
CISPEP   1 TYR A  304    PRO A  305          0         4.26                     
CISPEP   2 TYR B  304    PRO B  305          0         9.68                     
CISPEP   3 TYR B  370    SER B  371          0        -2.91                     
SITE     1 AC1  4 4NH A 158  HIS A 405  HIS A 409  HIS A 415                    
SITE     1 AC2  4 4NH B 159  HIS B 405  HIS B 409  HIS B 415                    
SITE     1 AC3 15 HOH A 120  THR A 347  LEU A 348  GLY A 349                    
SITE     2 AC3 15 LEU A 350  GLU A 398  LEU A 401  HIS A 405                    
SITE     3 AC3 15 GLU A 406  HIS A 409  HIS A 415  PRO A 437                    
SITE     4 AC3 15 ALA A 439  VAL A 440   ZN A 486                               
SITE     1 AC4 16 HOH B 116  GLY B 346  THR B 347  LEU B 348                    
SITE     2 AC4 16 GLY B 349  LEU B 350  LEU B 401  VAL B 402                    
SITE     3 AC4 16 HIS B 405  GLU B 406  HIS B 409  HIS B 415                    
SITE     4 AC4 16 PRO B 437  ALA B 439  VAL B 440   ZN B 486                    
CRYST1   48.367   59.209  198.011  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      0.020675  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016889  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005050        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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