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Database: PDB
Entry: 3D6M
LinkDB: 3D6M
Original site: 3D6M 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           19-MAY-08   3D6M              
TITLE     CRYSTAL STRUCTURE OF HUMAN CASPASE-1 WITH A NATURALLY-OCCURRING       
TITLE    2 LYS319->ARG SUBSTITUTION IN COMPLEX WITH 3-[2-(2-                    
TITLE    3 BENZYLOXYCARBONYLAMINO-3-METHYL-BUTYRYLAMINO)-PROPIONYLAMINO]-4-OXO- 
TITLE    4 PENTANOIC ACID (Z-VAD-FMK)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASPASE-1;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CASP1 P20;                                                 
COMPND   5 SYNONYM: CASP-1, INTERLEUKIN-1 BETA CONVERTASE, IL-1BC, IL-1 BETA-   
COMPND   6 CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA-CONVERTING ENZYME, P45,   
COMPND   7 CASPASE-1 SUBUNIT P20, CASPASE-1 SUBUNIT P10;                        
COMPND   8 EC: 3.4.22.36;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CASPASE-1;                                                 
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: CASP1 P10;                                                 
COMPND  14 SYNONYM: CASP-1, INTERLEUKIN-1 BETA CONVERTASE, IL-1BC, IL-1 BETA-   
COMPND  15 CONVERTING ENZYME, ICE, INTERLEUKIN-1 BETA-CONVERTING ENZYME, P45,   
COMPND  16 CASPASE-1 SUBUNIT P20, CASPASE-1 SUBUNIT P10;                        
COMPND  17 EC: 3.4.22.36;                                                       
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MUTATION: YES;                                                       
COMPND  20 MOL_ID: 3;                                                           
COMPND  21 MOLECULE: N-[(BENZYLOXY)CARBONYL]-L-VALYL-N-[(2S)-1-CARBOXY-4-FLUORO-
COMPND  22 3-OXOBUTAN-2-YL]-L-ALANINAMIDE;                                      
COMPND  23 CHAIN: C;                                                            
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CASP1, IL1BC, IL1BCE;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CASP1, IL1BC, IL1BCE;                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+;                          
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRSET B;                                  
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES                                                       
KEYWDS    CATALYTIC DOMAIN, NATURALLY-OCCURRING MUTATION, APOPTOSIS, HYDROLASE, 
KEYWDS   2 PROTEASE, THIOL PROTEASE, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR     
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ROSEN-WOLFF,J.ROESLER,M.J.ROMANOWSKI                                
REVDAT   3   23-MAY-12 3D6M    1       DBREF                                    
REVDAT   2   13-JUL-11 3D6M    1       VERSN                                    
REVDAT   1   02-MAR-10 3D6M    0                                                
JRNL        AUTH   A.ROSEN-WOLFF,M.J.ROMANOWSKI,L.RITTER,S.FLECKS,N.QUOOS,      
JRNL        AUTH 2 J.GRAMATT,C.PETZOLD,H.D.NGUYEN,M.GAHR,J.ROESLER              
JRNL        TITL   MUTATED, STRUCTURALLY ALTERED CASPASE-1 WITH DECREASED       
JRNL        TITL 2 ENZYMATIC AND INCREASED RIP2-MEDITATED INFLAMMATORY ACTIVITY 
JRNL        TITL 3 LEADS TO A NEW TYPE OF PERIODIC FEVER (ICE FEVER).           
JRNL        REF    TO BE PUBLISHED                            2008              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29468                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1567                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2786                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 170                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2099                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 238                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.08000                                              
REMARK   3    B22 (A**2) : 1.08000                                              
REMARK   3    B33 (A**2) : -2.16000                                             
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): 0.122         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.128         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.612         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2160 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2913 ; 1.056 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   259 ; 5.620 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;34.581 ;23.608       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   390 ;13.146 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.082 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   328 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1602 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1019 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1488 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   190 ; 0.110 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    81 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    37 ; 0.137 ; 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):  1352 ; 2.339 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2133 ; 3.485 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   903 ; 2.771 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   780 ; 4.317 ; 5.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   125                          
REMARK   3    RESIDUE RANGE :   B   317        B   317                          
REMARK   3    RESIDUE RANGE :   A     1        A     1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6028  23.9630  40.7380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1062 T22:  -0.0850                                     
REMARK   3      T33:  -0.1367 T12:  -0.1082                                     
REMARK   3      T13:   0.0905 T23:   0.0327                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8996 L22:   2.0258                                     
REMARK   3      L33:   0.3639 L12:   0.5471                                     
REMARK   3      L13:   0.5224 L23:   0.8188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:  -0.0621 S13:   0.4225                       
REMARK   3      S21:  -0.2431 S22:  -0.1406 S23:  -0.2096                       
REMARK   3      S31:  -0.3074 S32:   0.0115 S33:   0.0682                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D6M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047657.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 160                                
REMARK 200  PH                             : 6                                  
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) : 0.98                               
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CURVED CRYSTAL;         
REMARK 200                                   CRYSTAL TYPE S(220)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31131                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1SC3                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OBTAINED BY HANGING-DROP        
REMARK 280  VAPOR DIFFUSION AT 4 C (277K) AGAINST A RESERVOIR OF 0.1 M PIPES    
REMARK 280  PH 6.0, 75-175 MM (NH4)2SO4, 25% PEG 2000 MME, 10 MM DTT, 3 MM      
REMARK 280  NAN3, AND 2 MM MGCL2. ALL CRYSTALS CRYOPROTECTED IN MOTHER          
REMARK 280  LIQUORS SUPPLEMENTED WITH 20% (V/V) GLYCEROL FOR 30-90 SEC AND      
REMARK 280  IMMERSION IN LIQUID NITROGEN., VAPOR DIFFUSION, HANGING DROP        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.89150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.48400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.48400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      121.33725            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.48400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.48400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.44575            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.48400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.48400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      121.33725            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.48400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.48400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.44575            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       80.89150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: DIMER OF THE P20/P10 DIMER                                   
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 350   BIOMT1   2  0.000000 -1.000000  0.000000       62.96800            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       62.96800            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       80.89150            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 212  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 177  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   119                                                      
REMARK 465     ASN A   120                                                      
REMARK 465     PRO A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     MET A   123                                                      
REMARK 465     PRO A   124                                                      
REMARK 465     MET B   316                                                      
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     LYS A 225    CD   CE   NZ                                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  172   CD   OE1  OE2                                       
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   OE2  GLU A   172     O    HOH A   452              1.96            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 172   CG    GLU A 172   CD     -0.440                       
REMARK 500    ASP C   4   C     ASP C   4   O       0.190                       
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    SER A 149      -92.00    -73.97                                   
REMARK 500    ALA A 284      149.36   -171.77                                   
REMARK 500    ASP B 336      -11.57     86.17                                   
REMARK 500    ASP B 381     -154.46   -105.87                                   
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 B 120        DISTANCE =  5.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF   N-[(BENZYLOXY)       
REMARK 800  CARBONYL]-L-VALYL-N-[(2S)-1-CARBOXY-4-FLUORO- 3-OXOBUTAN-2-YL]-L-   
REMARK 800  ALANINAMIDE                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3D6H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1SC3   RELATED DB: PDB                                   
DBREF  3D6M A  120   297  UNP    P29466   CASP1_HUMAN    120    297             
DBREF  3D6M B  317   404  UNP    P29466   CASP1_HUMAN    317    404             
DBREF  3D6M C    1     5  PDB    3D6M     3D6M             1      5             
SEQADV 3D6M MET A  119  UNP  P29466              EXPRESSION TAG                 
SEQADV 3D6M MET B  316  UNP  P29466              EXPRESSION TAG                 
SEQADV 3D6M ARG B  319  UNP  P29466    LYS   319 ENGINEERED                     
SEQRES   1 A  179  MET ASN PRO ALA MET PRO THR SER SER GLY SER GLU GLY          
SEQRES   2 A  179  ASN VAL LYS LEU CYS SER LEU GLU GLU ALA GLN ARG ILE          
SEQRES   3 A  179  TRP LYS GLN LYS SER ALA GLU ILE TYR PRO ILE MET ASP          
SEQRES   4 A  179  LYS SER SER ARG THR ARG LEU ALA LEU ILE ILE CYS ASN          
SEQRES   5 A  179  GLU GLU PHE ASP SER ILE PRO ARG ARG THR GLY ALA GLU          
SEQRES   6 A  179  VAL ASP ILE THR GLY MET THR MET LEU LEU GLN ASN LEU          
SEQRES   7 A  179  GLY TYR SER VAL ASP VAL LYS LYS ASN LEU THR ALA SER          
SEQRES   8 A  179  ASP MET THR THR GLU LEU GLU ALA PHE ALA HIS ARG PRO          
SEQRES   9 A  179  GLU HIS LYS THR SER ASP SER THR PHE LEU VAL PHE MET          
SEQRES  10 A  179  SER HIS GLY ILE ARG GLU GLY ILE CYS GLY LYS LYS HIS          
SEQRES  11 A  179  SER GLU GLN VAL PRO ASP ILE LEU GLN LEU ASN ALA ILE          
SEQRES  12 A  179  PHE ASN MET LEU ASN THR LYS ASN CYS PRO SER LEU LYS          
SEQRES  13 A  179  ASP LYS PRO LYS VAL ILE ILE ILE GLN ALA CYS ARG GLY          
SEQRES  14 A  179  ASP SER PRO GLY VAL VAL TRP PHE LYS ASP                      
SEQRES   1 B   89  MET ALA ILE ARG LYS ALA HIS ILE GLU LYS ASP PHE ILE          
SEQRES   2 B   89  ALA PHE CYS SER SER THR PRO ASP ASN VAL SER TRP ARG          
SEQRES   3 B   89  HIS PRO THR MET GLY SER VAL PHE ILE GLY ARG LEU ILE          
SEQRES   4 B   89  GLU HIS MET GLN GLU TYR ALA CYS SER CYS ASP VAL GLU          
SEQRES   5 B   89  GLU ILE PHE ARG LYS VAL ARG PHE SER PHE GLU GLN PRO          
SEQRES   6 B   89  ASP GLY ARG ALA GLN MET PRO THR THR GLU ARG VAL THR          
SEQRES   7 B   89  LEU THR ARG CYS PHE TYR LEU PHE PRO GLY HIS                  
SEQRES   1 C    5  PHQ VAL ALA ASP CF0                                          
HET    PHQ  C   1      10                                                       
HET    CF0  C   5       1                                                       
HETNAM     PHQ BENZYL CHLOROCARBONATE                                           
HETNAM     CF0 FLUOROMETHANE                                                    
HETSYN     CF0 FLUORO METHYL GROUP                                              
FORMUL   3  PHQ    C8 H7 CL O2                                                  
FORMUL   3  CF0    C H3 F                                                       
FORMUL   4  HOH   *238(H2 O)                                                    
HELIX    1   1 SER A  137  LYS A  148  1                                  12    
HELIX    2   2 GLY A  181  LEU A  196  1                                  16    
HELIX    3   3 THR A  207  HIS A  220  1                                  14    
HELIX    4   4 ARG A  221  SER A  227  5                                   7    
HELIX    5   5 GLN A  257  ASN A  266  1                                  10    
HELIX    6   6 CYS A  270  LYS A  274  5                                   5    
HELIX    7   7 VAL B  348  ALA B  361  1                                  14    
HELIX    8   8 ASP B  365  PHE B  377  1                                  13    
SHEET    1   A 6 SER A 199  LYS A 204  0                                        
SHEET    2   A 6 LEU A 164  CYS A 169  1  N  ILE A 167   O  LYS A 203           
SHEET    3   A 6 THR A 230  MET A 235  1  O  VAL A 233   N  ILE A 168           
SHEET    4   A 6 LYS A 278  GLN A 283  1  O  ILE A 281   N  PHE A 234           
SHEET    5   A 6 PHE B 327  CYS B 331  1  O  ILE B 328   N  ILE A 280           
SHEET    6   A 6 THR B 388  GLU B 390 -1  O  THR B 388   N  CYS B 331           
SHEET    1   B 3 GLY A 238  ILE A 239  0                                        
SHEET    2   B 3 GLY A 242  CYS A 244 -1  O  GLY A 242   N  ILE A 239           
SHEET    3   B 3 ILE A 255  LEU A 256 -1  O  LEU A 256   N  ILE A 243           
SHEET    1   C 2 ARG B 341  HIS B 342  0                                        
SHEET    2   C 2 GLY B 346  SER B 347 -1  O  GLY B 346   N  HIS B 342           
LINK         C1  PHQ C   1                 N   VAL C   2     1555   1555  1.33  
LINK         C   ASP C   4                 C1  CF0 C   5     1555   1555  1.53  
LINK         SG  CYS A 285                 C1  CF0 C   5     1555   1555  1.81  
SITE     1 AC1 13 ARG A 179  HIS A 237  GLY A 238  GLN A 283                    
SITE     2 AC1 13 CYS A 285  SER B 339  TRP B 340  ARG B 341                    
SITE     3 AC1 13 HIS B 342  PRO B 343  ARG B 383  HOH C 367                    
SITE     4 AC1 13 HOH C 429                                                     
CRYST1   62.968   62.968  161.783  90.00  90.00  90.00 P 43 21 2     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      0.015881  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006181        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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