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Database: PDB
Entry: 5MBL
LinkDB: 5MBL
Original site: 5MBL 
HEADER    HYDROLASE                               08-NOV-16   5MBL              
TITLE     CATHEPSIN B IN COMPLEX WITH DARPIN 81                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN B;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: APP SECRETASE,APPS,CATHEPSIN B1;                            
COMPND   5 EC: 3.4.22.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DARPIN 81;                                                 
COMPND   9 CHAIN: B;                                                            
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 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   1   20-DEC-17 5MBL    0                                                
JRNL        AUTH   D.TURK,L.KRAMER                                              
JRNL        TITL   CATHEPSIN B IN COMPLEX WITH DARPIN 81                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.81 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) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.10                          
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             : 48409                          
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) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 100.00                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 48409                           
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           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 1.00                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2370                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2566                       
REMARK   3   BIN FREE R VALUE                    : 0.2887                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 100.0                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2370                         
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            : 3174                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 541                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.19100                                              
REMARK   3    B22 (A**2) : 1.19100                                              
REMARK   3    B33 (A**2) : -2.38100                                             
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5MBL 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_1200001751.                                   
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                             : 7.4                                
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 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS 2014                           
REMARK 200  DATA SCALING SOFTWARE          : XDS 2014                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48460                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.810                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.020                              
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   (%): 57.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BUFFER: 50MM TRIS/HCL, 300MM NACL,       
REMARK 280  0.05% TWEEN-20 PRECIPITANT: 0.1M MES, 1.8M NH4SO4, PH 7.4, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 292K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       52.89500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.89500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.30500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.89500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.89500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.30500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.89500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.89500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.30500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.89500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.89500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.30500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 566  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A     0                                                      
REMARK 465     MET B   251                                                      
REMARK 465     ARG B   252                                                      
REMARK 465     GLY B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     HIS B   255                                                      
REMARK 465     ASN B   421                                                      
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 B   420                                                      
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    1   CD   CE   NZ                                        
REMARK 480     LYS A  128   CG   CD   CE   NZ                                   
REMARK 480     LYS B  419   CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS B   419     O    HOH B   601              1.85            
REMARK 500   O    HOH A   305     O    HOH A   631              2.13            
REMARK 500   O    HOH A   366     O    HOH A   527              2.16            
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    ARG A  86   CA    ARG A  86   CB     -0.158                       
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  22   CB  -  CG  -  CD  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    ARG A  22   CG  -  CD  -  NE  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ARG A  22   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 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    THR A 121     -164.25   -114.47                                   
REMARK 500    THR A 121     -158.61   -114.47                                   
REMARK 500    PRO A 139     -171.61    -62.66                                   
REMARK 500    LYS A 185      -39.65   -130.26                                   
REMARK 500    ASN A 223      178.34     73.71                                   
REMARK 500    CYS A 241       18.81     57.86                                   
REMARK 500    HIS B 259       51.27   -171.90                                   
REMARK 500    ASN B 306       49.34    -81.61                                   
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 A 655        DISTANCE =  5.84 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501                 
DBREF  5MBL A    0   255  UNP    P07858   CATB_HUMAN      78    333             
DBREF  5MBL B  251   421  PDB    5MBL     5MBL           251    421             
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  171  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 B  171  LEU GLY LYS LYS LEU LEU ASP ALA ALA SER ALA GLY GLN          
SEQRES   3 B  171  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 B  171  VAL ASN ALA SER ASN SER TYR GLY ARG THR PRO LEU HIS          
SEQRES   5 B  171  ALA ALA ALA ASN GLY HIS LEU GLU ILE VAL ASP VAL LEU          
SEQRES   6 B  171  LEU ALA TYR GLY ALA ASP VAL ASN ALA SER ASP GLN TRP          
SEQRES   7 B  171  GLY TYR THR PRO LEU HIS LEU ALA ALA ALA GLU GLY HIS          
SEQRES   8 B  171  LEU GLU ILE VAL VAL VAL LEU LEU ALA ASN GLY ALA ASP          
SEQRES   9 B  171  VAL ASN ALA SER SER LYS ARG GLY ASN THR PRO LEU HIS          
SEQRES  10 B  171  VAL ALA ALA GLN SER GLY HIS LEU GLU ILE ALA ASP VAL          
SEQRES  11 B  171  LEU LEU ALA HIS GLY ALA ASP ILE ASN ALA ASN ASP TYR          
SEQRES  12 B  171  ASN GLY LYS THR PRO PHE ASP LEU ALA ILE ASP ASN GLY          
SEQRES  13 B  171  ASN ALA ASP ILE ALA GLU VAL LEU GLN LYS ALA ALA LYS          
SEQRES  14 B  171  LEU ASN                                                      
MODRES 5MBL SCH A   30  CYS  MODIFIED RESIDUE                                   
HET    SCH  A  30      16                                                       
HET    SO4  B 501       5                                                       
HETNAM     SCH S-METHYL-THIO-CYSTEINE                                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  SCH    C4 H9 N O2 S2                                                
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *541(H2 O)                                                    
HELIX    1 AA1 ALA A    8  TRP A   12  1                                   5    
HELIX    2 AA2 CYS A   15  GLU A   20  5                                   6    
HELIX    3 AA3 SER A   29  THR A   47  1                                  19    
HELIX    4 AA4 SER A   56  CYS A   64  1                                   9    
HELIX    5 AA5 GLY A   65  GLY A   69  5                                   5    
HELIX    6 AA6 ASP A   70  GLY A   74  5                                   5    
HELIX    7 AA7 TYR A   76  LYS A   87  1                                  12    
HELIX    8 AA8 THR A  140  LYS A  145  1                                   6    
HELIX    9 AA9 SER A  157  GLY A  169  1                                  13    
HELIX   10 AB1 SER A  179  LEU A  183  1                                   5    
HELIX   11 AB2 ASP A  239  ILE A  243  5                                   5    
HELIX   12 AB3 SER B  262  ALA B  274  1                                  13    
HELIX   13 AB4 GLN B  276  ASN B  286  1                                  11    
HELIX   14 AB5 THR B  299  ALA B  305  1                                   7    
HELIX   15 AB6 HIS B  308  TYR B  318  1                                  11    
HELIX   16 AB7 THR B  331  GLU B  339  1                                   9    
HELIX   17 AB8 HIS B  341  ASN B  351  1                                  11    
HELIX   18 AB9 THR B  364  GLY B  373  1                                  10    
HELIX   19 AC1 HIS B  374  HIS B  384  1                                  11    
HELIX   20 AC2 THR B  397  ASN B  405  1                                   9    
HELIX   21 AC3 ASN B  407  LEU B  420  1                                  14    
SHEET    1 AA1 3 PHE A   6  ASP A   7  0                                        
SHEET    2 AA1 3 MET A 196  GLU A 210 -1  O  TRP A 207   N  PHE A   6           
SHEET    3 AA1 3 VAL A 171  TYR A 178 -1  N  VAL A 177   O  MET A 197           
SHEET    1 AA2 5 PHE A   6  ASP A   7  0                                        
SHEET    2 AA2 5 MET A 196  GLU A 210 -1  O  TRP A 207   N  PHE A   6           
SHEET    3 AA2 5 THR A 213  ALA A 219 -1  O  ALA A 219   N  ARG A 203           
SHEET    4 AA2 5 PHE A 231  LEU A 235 -1  O  PHE A 232   N  VAL A 218           
SHEET    5 AA2 5 VAL A 188  TYR A 189  1  N  TYR A 189   O  LYS A 233           
SHEET    1 AA3 2 GLY A 148  SER A 153  0                                        
SHEET    2 AA3 2 VAL A 248  PRO A 252 -1  O  ILE A 251   N  TYR A 149           
SSBOND   1 CYS A   15    CYS A   44                          1555   1555  2.06  
SSBOND   2 CYS A   27    CYS A   72                          1555   1555  2.07  
SSBOND   3 CYS A   63    CYS A  129                          1555   1555  2.09  
SSBOND   4 CYS A   64    CYS A   68                          1555   1555  2.02  
SSBOND   5 CYS A  101    CYS A  133                          1555   1555  2.05  
SSBOND   6 CYS A  109    CYS A  120                          1555   1555  2.05  
LINK         C   SER A  29                 N  ASCH A  30     1555   1555  1.35  
LINK         C   SER A  29                 N  BSCH A  30     1555   1555  1.39  
LINK         C  ASCH A  30                 N   TRP A  31     1555   1555  1.35  
LINK         C  BSCH A  30                 N   TRP A  31     1555   1555  1.27  
CISPEP   1 SER A  138    PRO A  139          0        -0.21                     
SITE     1 AC1 10 GLY B 340  HIS B 341  LEU B 342  GLU B 343                    
SITE     2 AC1 10 HOH B 611  HOH B 629  HOH B 652  HOH B 666                    
SITE     3 AC1 10 HOH B 714  HOH B 720                                          
CRYST1  105.790  105.790   92.610  90.00  90.00  90.00 P 42 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      0.009453  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010798        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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