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Database: PDB
Entry: 1GMY
LinkDB: 1GMY
Original site: 1GMY 
HEADER    HYDROLASE/INHIBITOR                     25-SEP-01   1GMY              
TITLE     CATHEPSIN B COMPLEXED WITH DIPEPTIDYL NITRILE INHIBITOR               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN B;                                               
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: PROTEASE DOMAIN, RESIDUES 80-333;                          
COMPND   5 EC: 3.4.22.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    HYDROLASE/INHIBITOR, COMPLEX (HYDROLASE-INHIBITOR), COVALENT COMPLEX, 
KEYWDS   2 PROTEASE, CATHEPSIN B, HYDROLASE, THIOL PROTEASE, HYDROLASE-         
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.GREENSPAN,K.L.CLARK,R.A.TOMMASI,S.D.COWEN,L.W.MCQUIRE,D.L.FARLEY, 
AUTHOR   2 J.H.VAN DUZER,R.L.GOLDBERG,H.ZHOU,Z.DU,J.J.FITT,D.E.COPPA,Z.FANG,    
AUTHOR   3 W.MACCHIA,L.ZHU,M.P.CAPPARELLI,R.GOLDSTEIN,A.M.WIGG,J.R.DOUGHTY,     
AUTHOR   4 R.S.BOHACEK,A.K.KNAP                                                 
REVDAT   3   05-JUL-17 1GMY    1       REMARK                                   
REVDAT   2   24-FEB-09 1GMY    1       VERSN                                    
REVDAT   1   19-SEP-02 1GMY    0                                                
JRNL        AUTH   P.D.GREENSPAN,K.L.CLARK,R.A.TOMMASI,S.D.COWEN,L.W.MCQUIRE,   
JRNL        AUTH 2 D.L.FARLEY,J.H.VAN DUZER,R.L.GOLDBERG,H.ZHOU,Z.DU,J.J.FITT,  
JRNL        AUTH 3 D.E.COPPA,Z.FANG,W.MACCHIA,L.ZHU,M.P.CAPPARELLI,R.GOLDSTEIN, 
JRNL        AUTH 4 A.M.WIGG,J.R.DOUGHTY,R.S BOHACEK,A.K.KNAP                    
JRNL        TITL   IDENTIFICATION OF DIPEPTIDYL NITRILES AS POTENT AND          
JRNL        TITL 2 SELECTIVE INHIBITORS OF CATHEPSIN B THROUGH STRUCTURE-BASED  
JRNL        TITL 3 DRUG DESIGN                                                  
JRNL        REF    J.MED.CHEM.                   V.  44  4524 2001              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   11741472                                                     
JRNL        DOI    10.1021/JM010206Q                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2000                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 59016                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5971                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : NULL                 
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8097                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1670                       
REMARK   3   BIN FREE R VALUE                    : 0.2070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 909                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.007                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5830                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 93                                      
REMARK   3   SOLVENT ATOMS            : 630                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.04                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.21                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.880                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : BULK SOLVENT MODELING                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.410 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.970 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.090 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 50.64                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NII.PARAMETER                                  
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NII.TOPOLOGY                                   
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290008620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : YALE MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62966                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.50                                  
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       83.73333            
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       41.86667            
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       41.86667            
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       83.73333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 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 C2172  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C2203  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     ASP A   254                                                      
REMARK 465     GLN A   255                                                      
REMARK 465     TYR A   256                                                      
REMARK 465     TRP A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     ILE A   260                                                      
REMARK 465     THR B   253                                                      
REMARK 465     ASP B   254                                                      
REMARK 465     GLN B   255                                                      
REMARK 465     TYR B   256                                                      
REMARK 465     TRP B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ILE B   260                                                      
REMARK 465     THR C   253                                                      
REMARK 465     ASP C   254                                                      
REMARK 465     GLN C   255                                                      
REMARK 465     TYR C   256                                                      
REMARK 465     TRP C   257                                                      
REMARK 465     GLU C   258                                                      
REMARK 465     LYS C   259                                                      
REMARK 465     ILE C   260                                                      
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   0    CG   CD   CE   NZ                                   
REMARK 470     LYS B   0    CG   CD   CE   NZ                                   
REMARK 470     LYS C   0    CG   CD   CE   NZ                                   
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    19     O    HOH A  2025              2.07            
REMARK 500   OE2  GLU C    53     O    HOH C  2059              2.13            
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 122      119.25    -35.27                                   
REMARK 500    PRO A 138     -161.62    -79.84                                   
REMARK 500    ASN A 222      174.91     69.93                                   
REMARK 500    CYS A 240       18.73     58.53                                   
REMARK 500    HIS B  49       47.95     31.30                                   
REMARK 500    THR B 120     -162.13   -107.46                                   
REMARK 500    LYS B 130       53.57    -94.97                                   
REMARK 500    PRO B 138     -162.09    -78.76                                   
REMARK 500    ASN B 222      176.26     67.44                                   
REMARK 500    ALA B 248     -163.25   -160.87                                   
REMARK 500    GLU C 122      113.51    -25.25                                   
REMARK 500    PRO C 138     -155.44    -80.39                                   
REMARK 500    ASN C 222      176.68     68.55                                   
REMARK 500    CYS C 240       16.36     58.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DFA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AEM B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DFA B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AEM C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APD C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AEM A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APD B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DFA C 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CSB   RELATED DB: PDB                                   
REMARK 900 CATHEPSIN B                                                          
REMARK 900 RELATED ID: 1HUC   RELATED DB: PDB                                   
REMARK 900 CATHEPSIN B                                                          
REMARK 900 RELATED ID: 1PBH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN RECOMBINANT PROCATHEPSIN B AT 3.2         
REMARK 900 ANGSTROM RESOLUTION                                                  
REMARK 900 RELATED ID: 2PBH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION 
REMARK 900 RELATED ID: 3PBH   RELATED DB: PDB                                   
REMARK 900 REFINED CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 2.5 ANGSTROM    
REMARK 900 RESOLUTION                                                           
DBREF  1GMY A    0   260  UNP    P07858   CATB_HUMAN      79    339             
DBREF  1GMY B    0   260  UNP    P07858   CATB_HUMAN      79    339             
DBREF  1GMY C    0   260  UNP    P07858   CATB_HUMAN      79    339             
SEQRES   1 A  261  LYS LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP PRO          
SEQRES   2 A  261  GLN CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY SER          
SEQRES   3 A  261  CYS GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA ILE          
SEQRES   4 A  261  SER ASP ARG ILE CYS ILE HIS THR ASN ALA HIS VAL SER          
SEQRES   5 A  261  VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS CYS GLY          
SEQRES   6 A  261  SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR PRO ALA          
SEQRES   7 A  261  GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU VAL SER          
SEQRES   8 A  261  GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG PRO TYR          
SEQRES   9 A  261  SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY SER ARG          
SEQRES  10 A  261  PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS CYS SER          
SEQRES  11 A  261  LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR LYS GLN          
SEQRES  12 A  261  ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL SER ASN          
SEQRES  13 A  261  SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS ASN GLY          
SEQRES  14 A  261  PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP PHE LEU          
SEQRES  15 A  261  LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR GLY GLU          
SEQRES  16 A  261  MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY TRP GLY          
SEQRES  17 A  261  VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA ASN SER          
SEQRES  18 A  261  TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE LYS ILE          
SEQRES  19 A  261  LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER GLU VAL          
SEQRES  20 A  261  VAL ALA GLY ILE PRO ARG THR ASP GLN TYR TRP GLU LYS          
SEQRES  21 A  261  ILE                                                          
SEQRES   1 B  261  LYS LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP PRO          
SEQRES   2 B  261  GLN CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY SER          
SEQRES   3 B  261  CYS GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA ILE          
SEQRES   4 B  261  SER ASP ARG ILE CYS ILE HIS THR ASN ALA HIS VAL SER          
SEQRES   5 B  261  VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS CYS GLY          
SEQRES   6 B  261  SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR PRO ALA          
SEQRES   7 B  261  GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU VAL SER          
SEQRES   8 B  261  GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG PRO TYR          
SEQRES   9 B  261  SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY SER ARG          
SEQRES  10 B  261  PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS CYS SER          
SEQRES  11 B  261  LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR LYS GLN          
SEQRES  12 B  261  ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL SER ASN          
SEQRES  13 B  261  SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS ASN GLY          
SEQRES  14 B  261  PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP PHE LEU          
SEQRES  15 B  261  LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR GLY GLU          
SEQRES  16 B  261  MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY TRP GLY          
SEQRES  17 B  261  VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA ASN SER          
SEQRES  18 B  261  TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE LYS ILE          
SEQRES  19 B  261  LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER GLU VAL          
SEQRES  20 B  261  VAL ALA GLY ILE PRO ARG THR ASP GLN TYR TRP GLU LYS          
SEQRES  21 B  261  ILE                                                          
SEQRES   1 C  261  LYS LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP PRO          
SEQRES   2 C  261  GLN CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY SER          
SEQRES   3 C  261  CYS GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA ILE          
SEQRES   4 C  261  SER ASP ARG ILE CYS ILE HIS THR ASN ALA HIS VAL SER          
SEQRES   5 C  261  VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS CYS GLY          
SEQRES   6 C  261  SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR PRO ALA          
SEQRES   7 C  261  GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU VAL SER          
SEQRES   8 C  261  GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG PRO TYR          
SEQRES   9 C  261  SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY SER ARG          
SEQRES  10 C  261  PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS CYS SER          
SEQRES  11 C  261  LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR LYS GLN          
SEQRES  12 C  261  ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL SER ASN          
SEQRES  13 C  261  SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS ASN GLY          
SEQRES  14 C  261  PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP PHE LEU          
SEQRES  15 C  261  LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR GLY GLU          
SEQRES  16 C  261  MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY TRP GLY          
SEQRES  17 C  261  VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA ASN SER          
SEQRES  18 C  261  TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE LYS ILE          
SEQRES  19 C  261  LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER GLU VAL          
SEQRES  20 C  261  VAL ALA GLY ILE PRO ARG THR ASP GLN TYR TRP GLU LYS          
SEQRES  21 C  261  ILE                                                          
HET    AEM  A 500       4                                                       
HET    APD  A 501      12                                                       
HET    DFA  A 502      15                                                       
HET    AEM  B 500       4                                                       
HET    APD  B 501      12                                                       
HET    DFA  B 502      15                                                       
HET    AEM  C 500       4                                                       
HET    APD  C 501      12                                                       
HET    DFA  C 502      15                                                       
HETNAM     AEM 2-AMINOETHANIMIDIC ACID                                          
HETNAM     APD 3-METHYLPHENYLALANINE                                            
HETNAM     DFA DIPHENYLACETIC ACID                                              
FORMUL   4  AEM    3(C2 H6 N2)                                                  
FORMUL   5  APD    3(C10 H13 N O2)                                              
FORMUL   6  DFA    3(C14 H12 O2)                                                
FORMUL  13  HOH   *630(H2 O)                                                    
HELIX    1   1 ALA A    7  TRP A   11  1                                   5    
HELIX    2   2 CYS A   14  GLU A   19  5                                   6    
HELIX    3   3 SER A   28  THR A   46  1                                  19    
HELIX    4   4 SER A   55  CYS A   63  1                                   9    
HELIX    5   5 GLY A   64  CYS A   67  5                                   4    
HELIX    6   6 ASP A   69  GLY A   73  5                                   5    
HELIX    7   7 TYR A   75  LYS A   86  1                                  12    
HELIX    8   8 THR A  139  LYS A  144  1                                   6    
HELIX    9   9 SER A  156  GLY A  168  1                                  13    
HELIX   10  10 ASP A  179  LEU A  181  5                                   3    
HELIX   11  11 ASP A  238  ILE A  242  5                                   5    
HELIX   12  12 ALA B    7  TRP B   11  1                                   5    
HELIX   13  13 CYS B   14  GLU B   19  5                                   6    
HELIX   14  14 SER B   28  THR B   46  1                                  19    
HELIX   15  15 SER B   55  CYS B   63  1                                   9    
HELIX   16  16 GLY B   64  CYS B   67  5                                   4    
HELIX   17  17 ASP B   69  GLY B   73  5                                   5    
HELIX   18  18 TYR B   75  LYS B   86  1                                  12    
HELIX   19  19 TYR B  140  LYS B  144  5                                   5    
HELIX   20  20 SER B  156  GLY B  168  1                                  13    
HELIX   21  21 ASP B  179  LEU B  181  5                                   3    
HELIX   22  22 ASP B  238  ILE B  242  5                                   5    
HELIX   23  23 ALA C    7  TRP C   11  1                                   5    
HELIX   24  24 CYS C   14  GLU C   19  5                                   6    
HELIX   25  25 SER C   28  THR C   46  1                                  19    
HELIX   26  26 SER C   55  CYS C   63  1                                   9    
HELIX   27  27 GLY C   64  CYS C   67  5                                   4    
HELIX   28  28 ASP C   69  GLY C   73  5                                   5    
HELIX   29  29 TYR C   75  LYS C   86  1                                  12    
HELIX   30  30 THR C  139  LYS C  144  1                                   6    
HELIX   31  31 SER C  156  GLY C  168  1                                  13    
HELIX   32  32 ASP C  179  LEU C  181  5                                   3    
HELIX   33  33 ASP C  238  ILE C  242  5                                   5    
SHEET    1  AA 3 PHE A   5  ASP A   6  0                                        
SHEET    2  AA 3 MET A 195  GLU A 209 -1  O  TRP A 206   N  PHE A   5           
SHEET    3  AA 3 VAL A 170  TYR A 177 -1  O  VAL A 170   N  ILE A 203           
SHEET    1  AB 5 PHE A   5  ASP A   6  0                                        
SHEET    2  AB 5 MET A 195  GLU A 209 -1  O  TRP A 206   N  PHE A   5           
SHEET    3  AB 5 THR A 212  ALA A 218 -1  O  THR A 212   N  GLU A 209           
SHEET    4  AB 5 PHE A 230  LEU A 234 -1  O  PHE A 231   N  VAL A 217           
SHEET    5  AB 5 VAL A 187  TYR A 188  1  O  TYR A 188   N  LEU A 234           
SHEET    1  AC 2 TYR A 151  SER A 152  0                                        
SHEET    2  AC 2 VAL A 247  ALA A 248 -1  O  ALA A 248   N  TYR A 151           
SHEET    1  BA 3 PHE B   5  ASP B   6  0                                        
SHEET    2  BA 3 MET B 195  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3  BA 3 VAL B 170  TYR B 177 -1  O  VAL B 170   N  ILE B 203           
SHEET    1  BB 5 PHE B   5  ASP B   6  0                                        
SHEET    2  BB 5 MET B 195  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3  BB 5 THR B 212  ALA B 218 -1  O  THR B 212   N  GLU B 209           
SHEET    4  BB 5 PHE B 230  LEU B 234 -1  O  PHE B 231   N  VAL B 217           
SHEET    5  BB 5 VAL B 187  TYR B 188  1  O  TYR B 188   N  LEU B 234           
SHEET    1  BC 2 GLY B 147  SER B 152  0                                        
SHEET    2  BC 2 VAL B 247  PRO B 251 -1  O  ALA B 248   N  TYR B 151           
SHEET    1  CA 3 PHE C   5  ASP C   6  0                                        
SHEET    2  CA 3 MET C 195  GLU C 209 -1  O  TRP C 206   N  PHE C   5           
SHEET    3  CA 3 VAL C 170  TYR C 177 -1  O  VAL C 170   N  ILE C 203           
SHEET    1  CB 5 PHE C   5  ASP C   6  0                                        
SHEET    2  CB 5 MET C 195  GLU C 209 -1  O  TRP C 206   N  PHE C   5           
SHEET    3  CB 5 THR C 212  ALA C 218 -1  O  THR C 212   N  GLU C 209           
SHEET    4  CB 5 PHE C 230  LEU C 234 -1  O  PHE C 231   N  VAL C 217           
SHEET    5  CB 5 VAL C 187  TYR C 188  1  O  TYR C 188   N  LEU C 234           
SHEET    1  CC 2 TYR C 151  SER C 152  0                                        
SHEET    2  CC 2 VAL C 247  ALA C 248 -1  O  ALA C 248   N  TYR C 151           
SSBOND   1 CYS A   14    CYS A   43                          1555   1555  2.02  
SSBOND   2 CYS A   26    CYS A   71                          1555   1555  2.03  
SSBOND   3 CYS A   62    CYS A  128                          1555   1555  2.05  
SSBOND   4 CYS A   63    CYS A   67                          1555   1555  2.02  
SSBOND   5 CYS A  100    CYS A  132                          1555   1555  2.04  
SSBOND   6 CYS A  108    CYS A  119                          1555   1555  2.03  
SSBOND   7 CYS B   14    CYS B   43                          1555   1555  2.03  
SSBOND   8 CYS B   26    CYS B   71                          1555   1555  2.04  
SSBOND   9 CYS B   62    CYS B  128                          1555   1555  2.04  
SSBOND  10 CYS B   63    CYS B   67                          1555   1555  2.03  
SSBOND  11 CYS B  100    CYS B  132                          1555   1555  2.03  
SSBOND  12 CYS B  108    CYS B  119                          1555   1555  2.03  
SSBOND  13 CYS C   14    CYS C   43                          1555   1555  2.05  
SSBOND  14 CYS C   26    CYS C   71                          1555   1555  2.03  
SSBOND  15 CYS C   62    CYS C  128                          1555   1555  2.05  
SSBOND  16 CYS C   63    CYS C   67                          1555   1555  2.02  
SSBOND  17 CYS C  100    CYS C  132                          1555   1555  2.03  
SSBOND  18 CYS C  108    CYS C  119                          1555   1555  2.03  
LINK         SG  CYS A  29                 C1  AEM A 500     1555   1555  1.82  
LINK         N2  AEM A 500                 C   APD A 501     1555   1555  1.33  
LINK         N   APD A 501                 C8  DFA A 502     1555   1555  1.32  
LINK         SG  CYS B  29                 C1  AEM B 500     1555   1555  1.79  
LINK         N2  AEM B 500                 C   APD B 501     1555   1555  1.33  
LINK         N   APD B 501                 C8  DFA B 502     1555   1555  1.33  
LINK         SG  CYS C  29                 C1  AEM C 500     1555   1555  1.79  
LINK         N2  AEM C 500                 C   APD C 501     1555   1555  1.34  
LINK         N   APD C 501                 C8  DFA C 502     1555   1555  1.33  
CISPEP   1 SER A  137    PRO A  138          0         0.52                     
CISPEP   2 SER B  137    PRO B  138          0         0.35                     
CISPEP   3 SER C  137    PRO C  138          0         0.47                     
SITE     1 AC1 13 CYS A  29  TRP A  30  GLY A  73  GLY A  74                    
SITE     2 AC1 13 PRO A  76  ALA A 173  GLY A 198  HIS A 199                    
SITE     3 AC1 13 GLU A 245  AEM A 500  DFA A 502  GLU B 245                    
SITE     4 AC1 13 DFA B 502                                                     
SITE     1 AC2 11 ASP A  69  ASN A  72  GLY A  73  GLY A  74                    
SITE     2 AC2 11 TYR A  75  APD A 501  HOH A2181  MET B 195                    
SITE     3 AC2 11 GLY B 198  APD B 501  DFA B 502                               
SITE     1 AC3  6 GLN B  23  GLY B  27  CYS B  29  GLY B 198                    
SITE     2 AC3  6 APD B 501  HOH B2106                                          
SITE     1 AC4 11 SER A 175  GLY A 198  APD A 501  DFA A 502                    
SITE     2 AC4 11 ASP B  69  ASN B  72  GLY B  73  GLY B  74                    
SITE     3 AC4 11 TYR B  75  APD B 501  HOH B2170                               
SITE     1 AC5  7 GLN C  23  GLY C  27  SER C  28  CYS C  29                    
SITE     2 AC5  7 GLY C 198  APD C 501  HOH C2213                               
SITE     1 AC6 12 CYS C  29  TRP C  30  GLY C  73  GLY C  74                    
SITE     2 AC6 12 PRO C  76  ALA C 173  GLY C 198  HIS C 199                    
SITE     3 AC6 12 AEM C 500  DFA C 502  HOH C2148  HOH C2150                    
SITE     1 AC7  6 GLN A  23  GLY A  27  CYS A  29  GLY A 198                    
SITE     2 AC7  6 APD A 501  HOH A2212                                          
SITE     1 AC8 12 GLU A 245  DFA A 502  CYS B  29  TRP B  30                    
SITE     2 AC8 12 GLY B  73  GLY B  74  PRO B  76  ALA B 173                    
SITE     3 AC8 12 GLY B 198  HIS B 199  AEM B 500  DFA B 502                    
SITE     1 AC9  5 ASN C  72  GLY C  73  GLY C  74  TYR C  75                    
SITE     2 AC9  5 APD C 501                                                     
CRYST1  103.900  103.900  125.600  90.00  90.00 120.00 P 32 2 1     18          
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      0.009625  0.005557  0.000000        0.00000                         
SCALE2      0.000000  0.011113  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007962        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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