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Entry: 1HUC
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HEADER    THIOL PROTEASE                          21-APR-93   1HUC              
TITLE     THE REFINED 2.15 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF HUMAN           
TITLE    2 LIVER CATHEPSIN B: THE STRUCTURAL BASIS FOR ITS SPECIFICITY          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN B;                                               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 3.4.22.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CATHEPSIN B;                                               
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 EC: 3.4.22.1;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    THIOL PROTEASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.MUSIL,W.BODE                                                        
REVDAT   3   24-FEB-09 1HUC    1       VERSN                                    
REVDAT   2   01-APR-03 1HUC    1       JRNL                                     
REVDAT   1   26-JAN-95 1HUC    0                                                
JRNL        AUTH   D.MUSIL,D.ZUCIC,D.TURK,R.A.ENGH,I.MAYR,R.HUBER,              
JRNL        AUTH 2 T.POPOVIC,V.TURK,T.TOWATARI,N.KATUNUMA,W.BODE                
JRNL        TITL   THE REFINED 2.15 A X-RAY CRYSTAL STRUCTURE OF                
JRNL        TITL 2 HUMAN LIVER CATHEPSIN B: THE STRUCTURAL BASIS FOR            
JRNL        TITL 3 ITS SPECIFICITY.                                             
JRNL        REF    EMBO J.                       V.  10  2321 1991              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   1868826                                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : EREF, X-PLOR                                         
REMARK   3   AUTHORS     : JACK,LEVITT                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3876                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 283                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HUC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 44.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       17.08000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK:                                                              
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL           
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAINS *A* AND *B* WHEN            
REMARK 300 APPLIED TO CHAINS *C* AND *D*, RESPECTIVELY.                         
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: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     VAL B   50                                                       
REMARK 475     ASP B  254                                                       
REMARK 475     VAL D   50                                                       
REMARK 475     THR D  253                                                       
REMARK 475     ASP D  254                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   18   CE    NZ                                            
REMARK 480     ASN A   47   CA    C     O     CB    CG    OD1   ND2             
REMARK 480     ASN A   47   OXT                                                 
REMARK 480     SER B   51   N                                                   
REMARK 480     SER B  115   OG                                                  
REMARK 480     ASP B  124   OD1   OD2                                           
REMARK 480     LYS B  141   CD    CE    NZ                                      
REMARK 480     LYS B  158   CD    CE    NZ                                      
REMARK 480     LEU B  182   CD1   CD2                                           
REMARK 480     LYS B  184   CG    CD    CE    NZ                                
REMARK 480     THR B  253   CA    C     O     CB    OG1   CG2                   
REMARK 480     GLU C    9   CG    CD    OE1   OE2                               
REMARK 480     ASN C   47   CA    C     O     CB    CG    OD1   ND2             
REMARK 480     ASN C   47   OXT                                                 
REMARK 480     SER D   51   N     CA    CB    OG                                
REMARK 480     ARG D   85   CZ    NH1   NH2                                     
REMARK 480     ASN D  113   CG    OD1   ND2                                     
REMARK 480     LYS D  127   CD    CE    NZ                                      
REMARK 480     LYS D  158   CD    CE    NZ                                      
REMARK 480     LYS D  166   NZ                                                  
REMARK 480     LYS D  184   CE    NZ                                            
REMARK 480     ASN D  210   CG    OD1   ND2                                     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   747     O    HOH D   776     1565     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  11   NE1   TRP A  11   CE2    -0.088                       
REMARK 500    TRP A  30   NE1   TRP A  30   CE2    -0.093                       
REMARK 500    TRP B  80   NE1   TRP B  80   CE2    -0.083                       
REMARK 500    TRP B  83   NE1   TRP B  83   CE2    -0.098                       
REMARK 500    TRP B 206   NE1   TRP B 206   CE2    -0.104                       
REMARK 500    TRP B 221   NE1   TRP B 221   CE2    -0.094                       
REMARK 500    TRP B 225   NE1   TRP B 225   CE2    -0.092                       
REMARK 500    TRP C  11   NE1   TRP C  11   CE2    -0.100                       
REMARK 500    TRP C  30   NE1   TRP C  30   CE2    -0.088                       
REMARK 500    TRP D  80   NE1   TRP D  80   CE2    -0.109                       
REMARK 500    TRP D  83   NE1   TRP D  83   CE2    -0.094                       
REMARK 500    TRP D 206   NE1   TRP D 206   CE2    -0.092                       
REMARK 500    TRP D 215   NE1   TRP D 215   CE2    -0.094                       
REMARK 500    TRP D 221   NE1   TRP D 221   CE2    -0.107                       
REMARK 500    TRP D 225   NE1   TRP D 225   CE2    -0.090                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 101   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    TYR B 148   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP B 159   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 224   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C   6   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C  21   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG C  21   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    GLY D 123   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    TYR D 136   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR D 146   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG D 202   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG D 202   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 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    PRO B 138     -153.42    -95.82                                   
REMARK 500    TYR B 183      108.76    -43.08                                   
REMARK 500    ASN B 222     -175.91     66.98                                   
REMARK 500    SER D  65      -26.09    -35.42                                   
REMARK 500    THR D 120     -153.92   -113.99                                   
REMARK 500    GLU D 122     -165.15   -105.04                                   
REMARK 500    PRO D 138     -146.02    -84.54                                   
REMARK 500    SER D 156      111.52   -173.58                                   
REMARK 500    SER D 220       51.64   -110.71                                   
REMARK 500    ASN D 222     -179.00     69.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN B  113     GLY B  114                 -149.56                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  21         0.10    SIDE_CHAIN                              
REMARK 500    TYR B 151         0.07    SIDE_CHAIN                              
REMARK 500    TYR D 165         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL B  54         11.22                                           
REMARK 500    GLU B  57        -15.47                                           
REMARK 500    GLY B  64         10.33                                           
REMARK 500    LEU B  88         12.25                                           
REMARK 500    ASN B 113         17.15                                           
REMARK 500    GLN B 142        -16.36                                           
REMARK 500    VAL B 187         11.55                                           
REMARK 500    THR B 192        -17.60                                           
REMARK 500    ILE C  42        -12.61                                           
REMARK 500    GLY D  68         11.03                                           
REMARK 500    ARG D 116         14.69                                           
REMARK 500    TYR D 146        -10.59                                           
REMARK 500    ASN D 155         10.55                                           
REMARK 500    SER D 156         11.45                                           
REMARK 500    LYS D 158        -11.68                                           
REMARK 500    ASP D 159         11.70                                           
REMARK 500    LYS D 166         15.62                                           
REMARK 500    THR D 192        -11.97                                           
REMARK 500    GLY D 205         12.55                                           
REMARK 500    LEU D 216         14.19                                           
REMARK 500    ASP D 224        -12.17                                           
REMARK 500    VAL D 246         11.62                                           
REMARK 500    ALA D 248         10.62                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 845        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B 814        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B 817        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 863        DISTANCE =  5.76 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES                               
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES                               
DBREF  1HUC A    1    47  UNP    P07858   CATB_HUMAN      80    126             
DBREF  1HUC B   50   254  UNP    P07858   CATB_HUMAN     129    333             
DBREF  1HUC C    1    47  UNP    P07858   CATB_HUMAN      80    126             
DBREF  1HUC D   50   254  UNP    P07858   CATB_HUMAN     129    333             
SEQRES   1 A   47  LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP PRO GLN          
SEQRES   2 A   47  CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY SER CYS          
SEQRES   3 A   47  GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA ILE SER          
SEQRES   4 A   47  ASP ARG ILE CYS ILE HIS THR ASN                              
SEQRES   1 B  205  VAL SER VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS          
SEQRES   2 B  205  CYS GLY SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR          
SEQRES   3 B  205  PRO ALA GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU          
SEQRES   4 B  205  VAL SER GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG          
SEQRES   5 B  205  PRO TYR SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY          
SEQRES   6 B  205  SER ARG PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS          
SEQRES   7 B  205  CYS SER LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR          
SEQRES   8 B  205  LYS GLN ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL          
SEQRES   9 B  205  SER ASN SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS          
SEQRES  10 B  205  ASN GLY PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP          
SEQRES  11 B  205  PHE LEU LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR          
SEQRES  12 B  205  GLY GLU MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY          
SEQRES  13 B  205  TRP GLY VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA          
SEQRES  14 B  205  ASN SER TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE          
SEQRES  15 B  205  LYS ILE LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER          
SEQRES  16 B  205  GLU VAL VAL ALA GLY ILE PRO ARG THR ASP                      
SEQRES   1 C   47  LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP PRO GLN          
SEQRES   2 C   47  CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY SER CYS          
SEQRES   3 C   47  GLY SER CYS TRP ALA PHE GLY ALA VAL GLU ALA ILE SER          
SEQRES   4 C   47  ASP ARG ILE CYS ILE HIS THR ASN                              
SEQRES   1 D  205  VAL SER VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS          
SEQRES   2 D  205  CYS GLY SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR          
SEQRES   3 D  205  PRO ALA GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU          
SEQRES   4 D  205  VAL SER GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG          
SEQRES   5 D  205  PRO TYR SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY          
SEQRES   6 D  205  SER ARG PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS          
SEQRES   7 D  205  CYS SER LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR          
SEQRES   8 D  205  LYS GLN ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL          
SEQRES   9 D  205  SER ASN SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS          
SEQRES  10 D  205  ASN GLY PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP          
SEQRES  11 D  205  PHE LEU LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR          
SEQRES  12 D  205  GLY GLU MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY          
SEQRES  13 D  205  TRP GLY VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA          
SEQRES  14 D  205  ASN SER TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE          
SEQRES  15 D  205  LYS ILE LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER          
SEQRES  16 D  205  GLU VAL VAL ALA GLY ILE PRO ARG THR ASP                      
FORMUL   5  HOH   *283(H2 O)                                                    
HELIX    1   1 ALA A    7  TRP A   11  1                                   5    
HELIX    2   2 SER A   28  HIS A   45  1                                  18    
HELIX    3   3 SER B   55  CYS B   63  1                                   9    
HELIX    4   4 GLY B   64  CYS B   67  5                                   4    
HELIX    5   5 ASP B   69  GLY B   73  5                                   5    
HELIX    6   6 TYR B   75  LYS B   86  1                                  12    
HELIX    7   7 SER B  156  GLY B  168  1                                  13    
HELIX    8   8 ASP B  179  TYR B  183  5                                   5    
HELIX    9   9 ASP B  238  ILE B  242  5                                   5    
HELIX   10  10 ALA C    7  TRP C   11  1                                   5    
HELIX   11  11 CYS C   14  GLU C   19  5                                   6    
HELIX   12  12 SER C   28  HIS C   45  1                                  18    
HELIX   13  13 SER D   55  GLY D   64  1                                  10    
HELIX   14  14 SER D   65  GLY D   68  5                                   4    
HELIX   15  15 ASP D   69  CYS D   71  5                                   3    
HELIX   16  16 TYR D   75  LYS D   86  1                                  12    
HELIX   17  17 THR D  139  LYS D  144  1                                   6    
HELIX   18  18 SER D  156  GLY D  168  1                                  13    
HELIX   19  19 ASP D  179  TYR D  183  5                                   5    
HELIX   20  20 ASP D  238  ILE D  242  5                                   5    
SHEET    1   A 3 VAL B 170  TYR B 177  0                                        
SHEET    2   A 3 MET B 195  GLU B 209 -1  N  MET B 196   O  VAL B 176           
SHEET    3   A 3 PHE A   5  ASP A   6 -1  N  PHE A   5   O  TRP B 206           
SHEET    1   B 4 VAL B 170  TYR B 177  0                                        
SHEET    2   B 4 MET B 195  GLU B 209 -1  N  MET B 196   O  VAL B 176           
SHEET    3   B 4 THR B 212  ALA B 218 -1  O  THR B 212   N  GLU B 209           
SHEET    4   B 4 PHE B 230  LEU B 234 -1  O  PHE B 231   N  VAL B 217           
SHEET    1   C 2 TYR B 151  SER B 152  0                                        
SHEET    2   C 2 VAL B 247  ALA B 248 -1  N  ALA B 248   O  TYR B 151           
SHEET    1   D 3 VAL D 170  TYR D 177  0                                        
SHEET    2   D 3 MET D 195  GLU D 209 -1  N  MET D 196   O  VAL D 176           
SHEET    3   D 3 PHE C   5  ASP C   6 -1  O  PHE C   5   N  TRP D 206           
SHEET    1   E 5 VAL D 170  TYR D 177  0                                        
SHEET    2   E 5 MET D 195  GLU D 209 -1  N  MET D 196   O  VAL D 176           
SHEET    3   E 5 THR D 212  ALA D 218 -1  O  THR D 212   N  GLU D 209           
SHEET    4   E 5 PHE D 230  LEU D 234 -1  N  PHE D 231   O  VAL D 217           
SHEET    5   E 5 VAL D 187  TYR D 188  1  N  TYR D 188   O  LYS D 232           
SHEET    1   F 2 TYR D 151  SER D 152  0                                        
SHEET    2   F 2 VAL D 247  ALA D 248 -1  N  ALA D 248   O  TYR D 151           
SSBOND   1 CYS A   14    CYS A   43                          1555   1555  2.03  
SSBOND   2 CYS A   26    CYS B   71                          1555   1555  2.03  
SSBOND   3 CYS B   62    CYS B  128                          1555   1555  1.98  
SSBOND   4 CYS B   63    CYS B   67                          1555   1555  1.98  
SSBOND   5 CYS B  100    CYS B  132                          1555   1555  2.07  
SSBOND   6 CYS B  108    CYS B  119                          1555   1555  2.06  
SSBOND   7 CYS C   14    CYS C   43                          1555   1555  2.08  
SSBOND   8 CYS C   26    CYS D   71                          1555   1555  2.05  
SSBOND   9 CYS D   62    CYS D  128                          1555   1555  2.02  
SSBOND  10 CYS D   63    CYS D   67                          1555   1555  2.02  
SSBOND  11 CYS D  100    CYS D  132                          1555   1555  2.03  
SSBOND  12 CYS D  108    CYS D  119                          1555   1555  2.09  
CISPEP   1 SER B  137    PRO B  138          0        13.21                     
CISPEP   2 SER D  137    PRO D  138          0         6.69                     
SITE     1 AS1  3 CYS A  29  HIS B 199  ASN B 219                               
SITE     1 AS2  3 CYS C  29  HIS D 199  ASN D 219                               
CRYST1   86.230   34.160   85.560  90.00 102.90  90.00 P 1 21 1      4          
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      0.011597  0.000000  0.002656        0.00000                         
SCALE2      0.000000  0.029274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011990        0.00000                         
MTRIX1   1 -0.019000 -0.004300 -0.999800       83.76000    1                    
MTRIX2   1  0.019600  0.999800 -0.004700      -24.89800    1                    
MTRIX3   1  0.999600 -0.019700 -0.018900       20.75400    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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