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Database: PDB
Entry: 5MBM
LinkDB: 5MBM
Original site: 5MBM 
HEADER    HYDROLASE                               08-NOV-16   5MBM              
TITLE     CATHEPSIN B IN COMPLEX WITH DARPIN 8H6                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN B;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 78-333;                                       
COMPND   5 SYNONYM: APP SECRETASE,APPS,CATHEPSIN B1;                            
COMPND   6 EC: 3.4.22.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DARPIN 8H6;                                                
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTSB, CPSB;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  10 ORGANISM_TAXID: 32630;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEASE, DARPIN, COMPLEX, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TURK,L.KRAMER,M.RENKO,B.TURK                                        
REVDAT   2   20-FEB-19 5MBM    1       REMARK LINK                              
REVDAT   1   20-DEC-17 5MBM    0                                                
JRNL        AUTH   D.TURK,L.KRAMER                                              
JRNL        TITL   CATHEPSIN B IN COMPLEX WITH DARPIN 8H6                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : MAIN 2016                                            
REMARK   3   AUTHORS     : TURK                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 25126                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NONE                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : ALL                             
REMARK   3   R VALUE            (WORKING SET) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 25128                           
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) : 2.76                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 953                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4422                       
REMARK   3   BIN FREE R VALUE                    : 0.4645                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 100.0                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 953                          
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            : 6356                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 143                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.47400                                              
REMARK   3    B22 (A**2) : 3.10000                                              
REMARK   3    B33 (A**2) : -5.57400                                             
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) : 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: FREE KICK REFINEMENT TARGET WAS USED IN   
REMARK   3  COMBINATION WITH NCS AND SECONDARY STRUCTURE HYDROGEN BONDS         
REMARK   3  RESTRAINTS                                                          
REMARK   4                                                                      
REMARK   4 5MBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002001.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918007                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 2016                           
REMARK 200  DATA SCALING SOFTWARE          : XDS 2016                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25129                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : 0.18000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.01000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: CATHEPSIN B AND ANKIRIN                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0,1 M NA-CITRATE 15% PEG6000, PH 4.0,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       50.72500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      100.76000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.72500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      100.76000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     LEU B    -1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
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     LEU A    -1                                                      
REMARK 475     LYS D   169                                                      
REMARK 475     ASN D   171                                                      
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  141   CD   CE   NZ                                        
REMARK 480     LYS A  158   CD   CE   NZ                                        
REMARK 480     LEU B    1   CG   CD1  CD2                                       
REMARK 480     ARG B   85   NE   CZ   NH1  NH2                                  
REMARK 480     LYS B  127   CD   CE   NZ                                        
REMARK 480     LYS B  141   CE   NZ                                             
REMARK 480     LYS B  158   CD   CE   NZ                                        
REMARK 480     ARG D  143   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN D  144   CG   CD   OE1  NE2                                  
REMARK 480     GLU D  158   OE1  OE2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER B    25     O    GLU B   122              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   CD2  TYR C    68     NH1  ARG D    31     4558     1.52            
REMARK 500   CG   TYR C    68     NH1  ARG D    31     4558     2.15            
REMARK 500   CD2  HIS B   111     NZ   LYS B   141     1554     2.15            
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    TYR A 148   CA    TYR A 148   C       0.157                       
REMARK 500    GLU A 171   CD    GLU A 171   OE2    -0.075                       
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    ALA B  56   C   -  N   -  CA  ANGL. DEV. = -17.5 DEGREES          
REMARK 500    PRO B  76   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    LYS B  86   CA  -  C   -  N   ANGL. DEV. =  12.3 DEGREES          
REMARK 500    PRO B 117   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    THR B 253   N   -  CA  -  C   ANGL. DEV. = -16.2 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    TRP A  11       67.55   -114.05                                   
REMARK 500    SER A  25       41.82     82.59                                   
REMARK 500    SCH A  29      -73.29    -48.67                                   
REMARK 500    CYS A  63      -73.16    -70.50                                   
REMARK 500    ASP A  69       57.49   -117.84                                   
REMARK 500    ARG A 101       74.63   -118.48                                   
REMARK 500    GLU A 122     -170.81     40.88                                   
REMARK 500    CYS A 132     -157.05    -87.97                                   
REMARK 500    PRO A 134      119.44    -34.38                                   
REMARK 500    LEU A 182        5.08     87.74                                   
REMARK 500    TYR A 188      155.03    -49.54                                   
REMARK 500    GLN A 189      126.39   -171.49                                   
REMARK 500    VAL A 191      -55.45   -145.48                                   
REMARK 500    MET A 196       -2.83   -143.23                                   
REMARK 500    LEU A 204       24.19   -142.96                                   
REMARK 500    ASN A 210       18.76     58.16                                   
REMARK 500    ASN A 222      154.27     81.19                                   
REMARK 500    ILE A 242       -9.43    -58.50                                   
REMARK 500    THR B  16       -6.34    -57.79                                   
REMARK 500    GLU B  19      136.88    -34.13                                   
REMARK 500    SER B  25       55.30   -102.59                                   
REMARK 500    SER B  28       34.89    -98.52                                   
REMARK 500    SCH B  29      -83.94    -34.01                                   
REMARK 500    ILE B  44      -71.18    -56.16                                   
REMARK 500    ALA B  48       -7.14     63.40                                   
REMARK 500    CYS B  67     -151.79    -83.73                                   
REMARK 500    LEU B  93     -147.18    -15.73                                   
REMARK 500    PRO B 102      175.83    -53.40                                   
REMARK 500    VAL B 112     -165.77   -116.29                                   
REMARK 500    PRO B 117      164.60    -35.02                                   
REMARK 500    THR B 120       84.21   -154.08                                   
REMARK 500    GLU B 122      -76.57    -92.27                                   
REMARK 500    LYS B 130       49.32    -67.95                                   
REMARK 500    TYR B 151      159.56    177.07                                   
REMARK 500    SER B 154       48.33   -106.63                                   
REMARK 500    PHE B 174     -173.71    165.63                                   
REMARK 500    ASP B 179        7.30    -65.68                                   
REMARK 500    LEU B 181      -18.35    -39.32                                   
REMARK 500    LYS B 184      -30.51   -156.94                                   
REMARK 500    GLN B 189       87.94   -158.45                                   
REMARK 500    VAL B 191      -32.48   -137.16                                   
REMARK 500    MET B 196       50.05   -104.48                                   
REMARK 500    TRP B 206     -176.46   -170.64                                   
REMARK 500    ASN B 222      163.27     73.93                                   
REMARK 500    TRP B 225      142.82    -39.14                                   
REMARK 500    ARG B 252      -75.47    -59.17                                   
REMARK 500    THR B 253      -82.84    157.43                                   
REMARK 500    GLN C  26       66.02   -108.38                                   
REMARK 500    ASP C  27      -54.02    -25.30                                   
REMARK 500    VAL C  40       88.16     51.20                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 RAMACHANDRAN OUTLIERS.                        
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 223        DISTANCE =  7.33 ANGSTROMS                       
DBREF  5MBM A   -1   254  UNP    P07858   CATB_HUMAN      78    333             
DBREF  5MBM B   -1   254  UNP    P07858   CATB_HUMAN      78    333             
DBREF  5MBM C    1   171  PDB    5MBM     5MBM             1    171             
DBREF  5MBM D    1   171  PDB    5MBM     5MBM             1    171             
SEQRES   1 A  256  LEU LYS LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP          
SEQRES   2 A  256  PRO GLN CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY          
SEQRES   3 A  256  SER CYS GLY SER SCH TRP ALA PHE GLY ALA VAL GLU ALA          
SEQRES   4 A  256  ILE SER ASP ARG ILE CYS ILE HIS THR ASN ALA HIS VAL          
SEQRES   5 A  256  SER VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS CYS          
SEQRES   6 A  256  GLY SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR PRO          
SEQRES   7 A  256  ALA GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU VAL          
SEQRES   8 A  256  SER GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG PRO          
SEQRES   9 A  256  TYR SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY SER          
SEQRES  10 A  256  ARG PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS CYS          
SEQRES  11 A  256  SER LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR LYS          
SEQRES  12 A  256  GLN ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL SER          
SEQRES  13 A  256  ASN SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS ASN          
SEQRES  14 A  256  GLY PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP PHE          
SEQRES  15 A  256  LEU LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR GLY          
SEQRES  16 A  256  GLU MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY TRP          
SEQRES  17 A  256  GLY VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA ASN          
SEQRES  18 A  256  SER TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE LYS          
SEQRES  19 A  256  ILE LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER GLU          
SEQRES  20 A  256  VAL VAL ALA GLY ILE PRO ARG THR ASP                          
SEQRES   1 B  256  LEU LYS LEU PRO ALA SER PHE ASP ALA ARG GLU GLN TRP          
SEQRES   2 B  256  PRO GLN CYS PRO THR ILE LYS GLU ILE ARG ASP GLN GLY          
SEQRES   3 B  256  SER CYS GLY SER SCH TRP ALA PHE GLY ALA VAL GLU ALA          
SEQRES   4 B  256  ILE SER ASP ARG ILE CYS ILE HIS THR ASN ALA HIS VAL          
SEQRES   5 B  256  SER VAL GLU VAL SER ALA GLU ASP LEU LEU THR CYS CYS          
SEQRES   6 B  256  GLY SER MET CYS GLY ASP GLY CYS ASN GLY GLY TYR PRO          
SEQRES   7 B  256  ALA GLU ALA TRP ASN PHE TRP THR ARG LYS GLY LEU VAL          
SEQRES   8 B  256  SER GLY GLY LEU TYR GLU SER HIS VAL GLY CYS ARG PRO          
SEQRES   9 B  256  TYR SER ILE PRO PRO CYS GLU HIS HIS VAL ASN GLY SER          
SEQRES  10 B  256  ARG PRO PRO CYS THR GLY GLU GLY ASP THR PRO LYS CYS          
SEQRES  11 B  256  SER LYS ILE CYS GLU PRO GLY TYR SER PRO THR TYR LYS          
SEQRES  12 B  256  GLN ASP LYS HIS TYR GLY TYR ASN SER TYR SER VAL SER          
SEQRES  13 B  256  ASN SER GLU LYS ASP ILE MET ALA GLU ILE TYR LYS ASN          
SEQRES  14 B  256  GLY PRO VAL GLU GLY ALA PHE SER VAL TYR SER ASP PHE          
SEQRES  15 B  256  LEU LEU TYR LYS SER GLY VAL TYR GLN HIS VAL THR GLY          
SEQRES  16 B  256  GLU MET MET GLY GLY HIS ALA ILE ARG ILE LEU GLY TRP          
SEQRES  17 B  256  GLY VAL GLU ASN GLY THR PRO TYR TRP LEU VAL ALA ASN          
SEQRES  18 B  256  SER TRP ASN THR ASP TRP GLY ASP ASN GLY PHE PHE LYS          
SEQRES  19 B  256  ILE LEU ARG GLY GLN ASP HIS CYS GLY ILE GLU SER GLU          
SEQRES  20 B  256  VAL VAL ALA GLY ILE PRO ARG THR ASP                          
SEQRES   1 C  171  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 C  171  LEU GLY LYS LYS LEU LEU ASP ALA ALA SER ALA GLY GLN          
SEQRES   3 C  171  ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP          
SEQRES   4 C  171  VAL ASN ALA SER ASP THR TYR GLY ARG THR PRO LEU HIS          
SEQRES   5 C  171  ALA ALA ALA TRP GLY HIS LEU GLU ILE VAL ASP VAL LEU          
SEQRES   6 C  171  LEU ALA TYR GLY ALA ASP VAL ASN ALA SER ASP LYS TRP          
SEQRES   7 C  171  GLY TYR THR PRO LEU HIS LEU ALA ALA ASN GLU GLY HIS          
SEQRES   8 C  171  LEU GLU ILE VAL GLU VAL LEU LEU ALA ASN GLY ALA ASP          
SEQRES   9 C  171  VAL ASN ALA SER SER GLN ARG GLY GLN THR PRO LEU HIS          
SEQRES  10 C  171  VAL ALA ALA THR TRP GLY HIS LEU GLU ILE VAL ASP VAL          
SEQRES  11 C  171  LEU LEU ALA ASN GLY ALA ASP VAL ASN ALA ASN ASP ARG          
SEQRES  12 C  171  GLN GLY LYS THR PRO PHE ASP LEU ALA ILE ASP ASN GLY          
SEQRES  13 C  171  ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA ALA LYS          
SEQRES  14 C  171  LEU ASN                                                      
SEQRES   1 D  171  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 D  171  LEU GLY LYS LYS LEU LEU ASP ALA ALA SER ALA GLY GLN          
SEQRES   3 D  171  ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP          
SEQRES   4 D  171  VAL ASN ALA SER ASP THR TYR GLY ARG THR PRO LEU HIS          
SEQRES   5 D  171  ALA ALA ALA TRP GLY HIS LEU GLU ILE VAL ASP VAL LEU          
SEQRES   6 D  171  LEU ALA TYR GLY ALA ASP VAL ASN ALA SER ASP LYS TRP          
SEQRES   7 D  171  GLY TYR THR PRO LEU HIS LEU ALA ALA ASN GLU GLY HIS          
SEQRES   8 D  171  LEU GLU ILE VAL GLU VAL LEU LEU ALA ASN GLY ALA ASP          
SEQRES   9 D  171  VAL ASN ALA SER SER GLN ARG GLY GLN THR PRO LEU HIS          
SEQRES  10 D  171  VAL ALA ALA THR TRP GLY HIS LEU GLU ILE VAL ASP VAL          
SEQRES  11 D  171  LEU LEU ALA ASN GLY ALA ASP VAL ASN ALA ASN ASP ARG          
SEQRES  12 D  171  GLN GLY LYS THR PRO PHE ASP LEU ALA ILE ASP ASN GLY          
SEQRES  13 D  171  ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA ALA LYS          
SEQRES  14 D  171  LEU ASN                                                      
MODRES 5MBM SCH A   29  CYS  MODIFIED RESIDUE                                   
MODRES 5MBM SCH B   29  CYS  MODIFIED RESIDUE                                   
HET    SCH  A  29       8                                                       
HET    SCH  B  29       8                                                       
HETNAM     SCH S-METHYL-THIO-CYSTEINE                                           
FORMUL   1  SCH    2(C4 H9 N O2 S2)                                             
FORMUL   5  HOH   *143(H2 O)                                                    
HELIX    1 AA1 ASP A    6  TRP A   11  1                                   6    
HELIX    2 AA2 CYS A   14  GLU A   19  1                                   6    
HELIX    3 AA3 SER A   28  THR A   46  1                                  19    
HELIX    4 AA4 SER A   55  CYS A   63  1                                   9    
HELIX    5 AA5 GLY A   64  GLY A   68  5                                   5    
HELIX    6 AA6 ASP A   69  GLY A   73  5                                   5    
HELIX    7 AA7 TYR A   75  GLY A   87  1                                  13    
HELIX    8 AA8 THR A  139  LYS A  144  1                                   6    
HELIX    9 AA9 SER A  156  GLY A  168  1                                  13    
HELIX   10 AB1 ASP A  238  ILE A  242  5                                   5    
HELIX   11 AB2 ALA B    7  TRP B   11  1                                   5    
HELIX   12 AB3 CYS B   14  GLU B   19  1                                   6    
HELIX   13 AB4 SER B   28  THR B   46  1                                  19    
HELIX   14 AB5 SER B   55  GLY B   64  1                                  10    
HELIX   15 AB6 TYR B   75  GLY B   87  1                                  13    
HELIX   16 AB7 TYR B  140  LYS B  144  5                                   5    
HELIX   17 AB8 SER B  156  ASN B  167  1                                  12    
HELIX   18 AB9 ASP B  224  GLY B  229  1                                   6    
HELIX   19 AC1 ASP B  238  ILE B  242  5                                   5    
HELIX   20 AC2 HIS C   10  GLY C   25  1                                  16    
HELIX   21 AC3 GLN C   26  GLY C   37  1                                  12    
HELIX   22 AC4 ASP C   44  ARG C   48  5                                   5    
HELIX   23 AC5 THR C   49  ALA C   55  1                                   7    
HELIX   24 AC6 HIS C   58  TYR C   68  1                                  11    
HELIX   25 AC7 THR C   81  GLY C   90  1                                  10    
HELIX   26 AC8 HIS C   91  ASN C  101  1                                  11    
HELIX   27 AC9 THR C  114  THR C  121  1                                   8    
HELIX   28 AD1 HIS C  124  ASN C  134  1                                  11    
HELIX   29 AD2 THR C  147  ASN C  155  1                                   9    
HELIX   30 AD3 ASN C  157  ASN C  171  1                                  15    
HELIX   31 AD4 HIS D   10  GLY D   25  1                                  16    
HELIX   32 AD5 GLN D   26  ALA D   38  1                                  13    
HELIX   33 AD6 THR D   49  TRP D   56  1                                   8    
HELIX   34 AD7 HIS D   58  TYR D   68  1                                  11    
HELIX   35 AD8 THR D   81  GLY D   90  1                                  10    
HELIX   36 AD9 HIS D   91  ALA D  100  1                                  10    
HELIX   37 AE1 THR D  114  GLY D  123  1                                  10    
HELIX   38 AE2 HIS D  124  ALA D  133  1                                  10    
HELIX   39 AE3 THR D  147  ASN D  155  1                                   9    
HELIX   40 AE4 ASN D  157  ASN D  171  1                                  15    
SHEET    1 AA1 6 GLY A 147  SER A 152  0                                        
SHEET    2 AA1 6 VAL A 246  PRO A 251 -1  O  ILE A 250   N  TYR A 148           
SHEET    3 AA1 6 VAL A 170  TYR A 177 -1  N  GLU A 171   O  VAL A 247           
SHEET    4 AA1 6 MET A 195  GLU A 209 -1  O  ILE A 201   N  GLY A 172           
SHEET    5 AA1 6 THR A 212  ALA A 218 -1  O  THR A 212   N  GLU A 209           
SHEET    6 AA1 6 PHE A 230  LEU A 234 -1  O  ILE A 233   N  TRP A 215           
SHEET    1 AA2 5 PHE B   5  ASP B   6  0                                        
SHEET    2 AA2 5 ILE B 201  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3 AA2 5 THR B 212  ALA B 218 -1  O  ALA B 218   N  ARG B 202           
SHEET    4 AA2 5 PHE B 230  ILE B 233 -1  O  ILE B 233   N  TRP B 215           
SHEET    5 AA2 5 VAL B 187  TYR B 188  1  N  TYR B 188   O  LYS B 232           
SHEET    1 AA3 4 PHE B   5  ASP B   6  0                                        
SHEET    2 AA3 4 ILE B 201  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3 AA3 4 VAL B 170  GLY B 172 -1  N  GLY B 172   O  ILE B 201           
SHEET    4 AA3 4 VAL B 246  VAL B 247 -1  O  VAL B 247   N  GLU B 171           
SHEET    1 AA4 2 SER B 175  TYR B 177  0                                        
SHEET    2 AA4 2 MET B 195  GLY B 198 -1  O  MET B 196   N  VAL B 176           
SSBOND   1 CYS A   14    CYS A   43                          1555   1555  2.06  
SSBOND   2 CYS A   26    CYS A   71                          1555   1555  2.00  
SSBOND   3 CYS A   62    CYS A  128                          1555   1555  2.07  
SSBOND   4 CYS A   63    CYS A   67                          1555   1555  2.00  
SSBOND   5 CYS A  100    CYS A  132                          1555   1555  2.05  
SSBOND   6 CYS A  108    CYS A  119                          1555   1555  2.02  
SSBOND   7 CYS B   14    CYS B   43                          1555   1555  2.04  
SSBOND   8 CYS B   26    CYS B   71                          1555   1555  2.03  
SSBOND   9 CYS B   62    CYS B  128                          1555   1555  2.07  
SSBOND  10 CYS B   63    CYS B   67                          1555   1555  2.05  
SSBOND  11 CYS B  100    CYS B  132                          1555   1555  2.05  
SSBOND  12 CYS B  108    CYS B  119                          1555   1555  2.01  
LINK         C   SER A  28                 N   SCH A  29     1555   1555  1.33  
LINK         C   SCH A  29                 N   TRP A  30     1555   1555  1.34  
LINK         C   SER B  28                 N   SCH B  29     1555   1555  1.35  
LINK         C   SCH B  29                 N   TRP B  30     1555   1555  1.36  
CRYST1  101.450  201.520   46.860  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009857  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004962  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021340        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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