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Database: PDB
Entry: 4FEA
LinkDB: 4FEA
Original site: 4FEA 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           29-MAY-12   4FEA              
TITLE     CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ALLOSTERIC INHIBITOR   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASPASE-7;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: P20/P10 CATALYTIC DOMAIN (UNP RESIDUES 57-303);            
COMPND   5 SYNONYM: CASP-7, APOPTOTIC PROTEASE MCH-3, CMH-1, ICE-LIKE APOPTOTIC 
COMPND   6 PROTEASE 3, ICE-LAP3;                                                
COMPND   7 EC: 3.4.22.60;                                                       
COMPND   8 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: CASP7, MCH3;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYSTEINE PROTEASE, APOPTOSIS, HYDROLASE-HYDROLASE INHIBITOR COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.KABALEESWARAN                                                       
REVDAT   2   12-SEP-12 4FEA    1       JRNL                                     
REVDAT   1   01-AUG-12 4FEA    0                                                
JRNL        AUTH   T.FELDMAN,V.KABALEESWARAN,S.B.JANG,C.ANTCZAK,H.DJABALLAH,    
JRNL        AUTH 2 H.WU,X.JIANG                                                 
JRNL        TITL   A CLASS OF ALLOSTERIC CASPASE INHIBITORS IDENTIFIED BY       
JRNL        TITL 2 HIGH-THROUGHPUT SCREENING.                                   
JRNL        REF    MOL.CELL                      V.  47   585 2012              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   22795132                                                     
JRNL        DOI    10.1016/J.MOLCEL.2012.06.007                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 8257                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.640                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 383                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 76.8496 -  5.4587    0.90     2657   121  0.2538 0.2741        
REMARK   3     2  5.4587 -  4.3329    0.93     2588   140  0.2131 0.2916        
REMARK   3     3  4.3329 -  3.7900    0.94     2629   122  0.2380 0.2840        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 111.54                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.050           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 120.64                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 15.88900                                             
REMARK   3    B22 (A**2) : 15.88900                                             
REMARK   3    B33 (A**2) : -31.77790                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           2842                                  
REMARK   3   ANGLE     :  1.352           3839                                  
REMARK   3   CHIRALITY :  0.054            449                                  
REMARK   3   PLANARITY :  0.003            485                                  
REMARK   3   DIHEDRAL  : 14.330            991                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072792.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.378                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8266                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.785                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.834                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.70000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3IBF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.0-5.7, 1.9    
REMARK 280  M SODIUM FORMATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      123.77333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       61.88667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       61.88667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      123.77333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     ASN A    77                                                      
REMARK 465     PHE A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     LYS A    80                                                      
REMARK 465     VAL A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLY A    83                                                      
REMARK 465     MET A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     ARG A    87                                                      
REMARK 465     ASN A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     THR A    90                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     VAL A   149                                                      
REMARK 465     ILE A   150                                                      
REMARK 465     TYR A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     ARG A   187                                                      
REMARK 465     GLY A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     GLU A   190                                                      
REMARK 465     LEU A   191                                                      
REMARK 465     ASP A   192                                                      
REMARK 465     ASP A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     ILE A   195                                                      
REMARK 465     GLN A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     ASP A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     PRO A   201                                                      
REMARK 465     ILE A   202                                                      
REMARK 465     ASN A   203                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     ASP A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     ASN A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     TYR A   211                                                      
REMARK 465     LYS A   212                                                      
REMARK 465     ILE A   213                                                      
REMARK 465     PRO A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     TYR A   229                                                      
REMARK 465     TYR A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     TRP A   232                                                      
REMARK 465     ARG A   233                                                      
REMARK 465     SER A   234                                                      
REMARK 465     PRO A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     PHE A   273                                                      
REMARK 465     GLU A   274                                                      
REMARK 465     SER A   275                                                      
REMARK 465     GLN A   276                                                      
REMARK 465     SER A   277                                                      
REMARK 465     ASP A   278                                                      
REMARK 465     ASP A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     HIS A   281                                                      
REMARK 465     PHE A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     LYS A   285                                                      
REMARK 465     LYS A   286                                                      
REMARK 465     GLN A   287                                                      
REMARK 465     ARG B   187                                                      
REMARK 465     GLY B   188                                                      
REMARK 465     THR B   189                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     LEU B   191                                                      
REMARK 465     ASP B   192                                                      
REMARK 465     ASP B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     ILE B   195                                                      
REMARK 465     GLN B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     SER B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     PRO B   201                                                      
REMARK 465     ILE B   202                                                      
REMARK 465     ASN B   203                                                      
REMARK 465     ASP B   204                                                      
REMARK 465     THR B   205                                                      
REMARK 465     ASP B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     ASN B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     TYR B   211                                                      
REMARK 465     LYS B   212                                                      
REMARK 465     ILE B   213                                                      
REMARK 465     THR B   225                                                      
REMARK 465     VAL B   226                                                      
REMARK 465     PRO B   227                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     TYR B   229                                                      
REMARK 465     TYR B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     TRP B   232                                                      
REMARK 465     ARG B   233                                                      
REMARK 465     SER B   234                                                      
REMARK 465     GLU B   274                                                      
REMARK 465     SER B   275                                                      
REMARK 465     GLN B   276                                                      
REMARK 465     SER B   277                                                      
REMARK 465     ASP B   278                                                      
REMARK 465     ASP B   279                                                      
REMARK 465     PRO B   280                                                      
REMARK 465     HIS B   281                                                      
REMARK 465     PHE B   282                                                      
REMARK 465     HIS B   283                                                      
REMARK 465     GLU B   284                                                      
REMARK 465     LYS B   285                                                      
REMARK 465     LYS B   286                                                      
REMARK 465     GLN B   287                                                      
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     HIS A 144    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     ARG A 167    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 172    CG   CD   CE   NZ                                   
REMARK 470     GLU A 176    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 223    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 268    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 297    CG   CD   CE   NZ                                   
REMARK 470     TYR A 300    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  80    CG   CD   CE   NZ                                   
REMARK 470     LYS B  92    CG   CD   CE   NZ                                   
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     LYS B 124    CG   CD   CE   NZ                                   
REMARK 470     LYS B 125    CG   CD   CE   NZ                                   
REMARK 470     GLU B 147    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     LYS B 160    CG   CD   CE   NZ                                   
REMARK 470     ARG B 167    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 223    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 243    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 250    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ARG B 271    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 273    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 297    CG   CD   CE   NZ                                   
REMARK 470     GLN B 303    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    PRO A 289   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    PRO B 289   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  65      -86.30    -65.20                                   
REMARK 500    LEU A  67      -71.29    -66.18                                   
REMARK 500    CYS A 114       96.14    -64.33                                   
REMARK 500    CYS A 116      -17.91    -39.28                                   
REMARK 500    ARG A 167     -168.09    -65.83                                   
REMARK 500    LEU A 174       69.52   -118.52                                   
REMARK 500    GLU A 176       18.29     58.56                                   
REMARK 500    ALA A 222      106.67   -168.32                                   
REMARK 500    ASP A 255       20.83   -141.99                                   
REMARK 500    CYS A 290     -172.51    -65.76                                   
REMARK 500    VAL A 291       99.33   -163.91                                   
REMARK 500    ASN B  63       77.12    -68.98                                   
REMARK 500    LEU B  67      -72.33    -73.63                                   
REMARK 500    CYS B  70       76.49   -154.80                                   
REMARK 500    CYS B 136     -156.38   -124.92                                   
REMARK 500    SER B 143     -161.83   -165.77                                   
REMARK 500    GLU B 146     -149.89   -134.72                                   
REMARK 500    CYS B 171       69.84   -153.24                                   
REMARK 500    VAL B 215      -87.05    -62.04                                   
REMARK 500    GLU B 216       33.25    -93.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0TE A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0TE B 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FDL   RELATED DB: PDB                                   
DBREF  4FEA A   57   303  UNP    P55210   CASP7_HUMAN     57    303             
DBREF  4FEA B   57   303  UNP    P55210   CASP7_HUMAN     57    303             
SEQRES   1 A  247  THR TYR GLN TYR ASN MET ASN PHE GLU LYS LEU GLY LYS          
SEQRES   2 A  247  CYS ILE ILE ILE ASN ASN LYS ASN PHE ASP LYS VAL THR          
SEQRES   3 A  247  GLY MET GLY VAL ARG ASN GLY THR ASP LYS ASP ALA GLU          
SEQRES   4 A  247  ALA LEU PHE LYS CYS PHE ARG SER LEU GLY PHE ASP VAL          
SEQRES   5 A  247  ILE VAL TYR ASN ASP CYS SER CYS ALA LYS MET GLN ASP          
SEQRES   6 A  247  LEU LEU LYS LYS ALA SER GLU GLU ASP HIS THR ASN ALA          
SEQRES   7 A  247  ALA CYS PHE ALA CYS ILE LEU LEU SER HIS GLY GLU GLU          
SEQRES   8 A  247  ASN VAL ILE TYR GLY LYS ASP GLY VAL THR PRO ILE LYS          
SEQRES   9 A  247  ASP LEU THR ALA HIS PHE ARG GLY ASP ARG CYS LYS THR          
SEQRES  10 A  247  LEU LEU GLU LYS PRO LYS LEU PHE PHE ILE GLN ALA CYS          
SEQRES  11 A  247  ARG GLY THR GLU LEU ASP ASP GLY ILE GLN ALA ASP SER          
SEQRES  12 A  247  GLY PRO ILE ASN ASP THR ASP ALA ASN PRO ARG TYR LYS          
SEQRES  13 A  247  ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA TYR SER THR          
SEQRES  14 A  247  VAL PRO GLY TYR TYR SER TRP ARG SER PRO GLY ARG GLY          
SEQRES  15 A  247  SER TRP PHE VAL GLN ALA LEU CYS SER ILE LEU GLU GLU          
SEQRES  16 A  247  HIS GLY LYS ASP LEU GLU ILE MET GLN ILE LEU THR ARG          
SEQRES  17 A  247  VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU SER GLN SER          
SEQRES  18 A  247  ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN ILE PRO CYS          
SEQRES  19 A  247  VAL VAL SER MET LEU THR LYS GLU LEU TYR PHE SER GLN          
SEQRES   1 B  247  THR TYR GLN TYR ASN MET ASN PHE GLU LYS LEU GLY LYS          
SEQRES   2 B  247  CYS ILE ILE ILE ASN ASN LYS ASN PHE ASP LYS VAL THR          
SEQRES   3 B  247  GLY MET GLY VAL ARG ASN GLY THR ASP LYS ASP ALA GLU          
SEQRES   4 B  247  ALA LEU PHE LYS CYS PHE ARG SER LEU GLY PHE ASP VAL          
SEQRES   5 B  247  ILE VAL TYR ASN ASP CYS SER CYS ALA LYS MET GLN ASP          
SEQRES   6 B  247  LEU LEU LYS LYS ALA SER GLU GLU ASP HIS THR ASN ALA          
SEQRES   7 B  247  ALA CYS PHE ALA CYS ILE LEU LEU SER HIS GLY GLU GLU          
SEQRES   8 B  247  ASN VAL ILE TYR GLY LYS ASP GLY VAL THR PRO ILE LYS          
SEQRES   9 B  247  ASP LEU THR ALA HIS PHE ARG GLY ASP ARG CYS LYS THR          
SEQRES  10 B  247  LEU LEU GLU LYS PRO LYS LEU PHE PHE ILE GLN ALA CYS          
SEQRES  11 B  247  ARG GLY THR GLU LEU ASP ASP GLY ILE GLN ALA ASP SER          
SEQRES  12 B  247  GLY PRO ILE ASN ASP THR ASP ALA ASN PRO ARG TYR LYS          
SEQRES  13 B  247  ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA TYR SER THR          
SEQRES  14 B  247  VAL PRO GLY TYR TYR SER TRP ARG SER PRO GLY ARG GLY          
SEQRES  15 B  247  SER TRP PHE VAL GLN ALA LEU CYS SER ILE LEU GLU GLU          
SEQRES  16 B  247  HIS GLY LYS ASP LEU GLU ILE MET GLN ILE LEU THR ARG          
SEQRES  17 B  247  VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU SER GLN SER          
SEQRES  18 B  247  ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN ILE PRO CYS          
SEQRES  19 B  247  VAL VAL SER MET LEU THR LYS GLU LEU TYR PHE SER GLN          
HET    0TE  A 701      21                                                       
HET    0TE  B 701      21                                                       
HETNAM     0TE CHLORO{METHYL HYDROGENATO(3-)-KAPPA~2~N,S [PYRIDIN-2-            
HETNAM   2 0TE  YL(PYRIDIN-2(1H)-YLIDENE-KAPPAN)                                
HETNAM   3 0TE  METHYL]CARBONODITHIOHYDRAZONATE}COPPER                          
FORMUL   3  0TE    2(C13 H11 CL CU N4 S2)                                       
HELIX    1   1 LYS A   92  SER A  103  1                                  12    
HELIX    2   2 CYS A  116  GLU A  128  1                                  13    
HELIX    3   3 ILE A  159  ALA A  164  1                                   6    
HELIX    4   4 HIS A  165  ARG A  167  5                                   3    
HELIX    5   5 SER A  239  GLU A  250  1                                  12    
HELIX    6   6 HIS A  252  LEU A  256  5                                   5    
HELIX    7   7 GLU A  257  ARG A  271  1                                  15    
HELIX    8   8 ASP B   79  GLY B   83  5                                   5    
HELIX    9   9 GLY B   89  SER B  103  1                                  15    
HELIX   10  10 SER B  115  GLU B  128  1                                  14    
HELIX   11  11 ILE B  159  HIS B  165  1                                   7    
HELIX   12  12 CYS B  171  LEU B  175  5                                   5    
HELIX   13  13 SER B  239  GLY B  253  1                                  15    
HELIX   14  14 GLU B  257  PHE B  273  1                                  17    
SHEET    1   A12 ASP A 107  ASN A 112  0                                        
SHEET    2   A12 LYS A  66  ASN A  74  1  N  ASN A  74   O  TYR A 111           
SHEET    3   A12 ALA A 134  LEU A 142  1  O  ILE A 140   N  ILE A  73           
SHEET    4   A12 LYS A 179  ALA A 185  1  O  PHE A 182   N  CYS A 139           
SHEET    5   A12 PHE A 219  THR A 225  1  O  ALA A 222   N  ILE A 183           
SHEET    6   A12 VAL A 292  MET A 294 -1  O  MET A 294   N  PHE A 219           
SHEET    7   A12 CYS B 290  SER B 293 -1  O  VAL B 291   N  SER A 293           
SHEET    8   A12 PHE B 219  SER B 224 -1  N  PHE B 221   O  VAL B 292           
SHEET    9   A12 LYS B 179  ALA B 185  1  N  ILE B 183   O  SER B 224           
SHEET   10   A12 ALA B 138  SER B 143  1  N  LEU B 141   O  PHE B 182           
SHEET   11   A12 GLY B  68  ASN B  74  1  N  ILE B  71   O  ILE B 140           
SHEET   12   A12 PHE B 106  ASN B 112  1  O  TYR B 111   N  ILE B  72           
SHEET    1   B 3 GLY B 145  GLU B 146  0                                        
SHEET    2   B 3 VAL B 149  TYR B 151 -1  O  VAL B 149   N  GLU B 146           
SHEET    3   B 3 VAL B 156  PRO B 158 -1  O  THR B 157   N  ILE B 150           
SITE     1 AC1  5 CYS A 290  GLU B 216  PHE B 221  MET B 294                    
SITE     2 AC1  5 0TE B 701                                                     
SITE     1 AC2  5 GLU A 216  VAL A 292  MET A 294  0TE A 701                    
SITE     2 AC2  5 CYS B 290                                                     
CRYST1   88.720   88.720  185.660  90.00  90.00 120.00 P 32 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011271  0.006508  0.000000        0.00000                         
SCALE2      0.000000  0.013015  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005386        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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