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Database: PDB
Entry: 3AI8
LinkDB: 3AI8
Original site: 3AI8 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-MAY-10   3AI8              
TITLE     CATHEPSIN B IN COMPLEX WITH THE NITROXOLINE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN B;                                               
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: CATHEPSIN B1, APP SECRETASE, APPS, CATHEPSIN B LIGHT CHAIN, 
COMPND   5 CATHEPSIN B HEAVY CHAIN;                                             
COMPND   6 EC: 3.4.22.1;                                                        
COMPND   7 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    CATHEPSIN B, REVERSIBLE INHIBITOR, NITROXOLINE, 8-HYDROXY-5-          
KEYWDS   2 NITROQUINOLINE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RENKO,B.MIRKOVIC,S.GOBEC,J.KOS,D.TURK                               
REVDAT   3   29-JAN-14 3AI8    1       JRNL   VERSN                             
REVDAT   2   08-JUN-11 3AI8    1       JRNL                                     
REVDAT   1   18-MAY-11 3AI8    0                                                
JRNL        AUTH   B.MIRKOVIC,M.RENKO,S.TURK,I.SOSIC,Z.JEVNIKAR,N.OBERMAJER,    
JRNL        AUTH 2 D.TURK,S.GOBEC,J.KOS                                         
JRNL        TITL   NOVEL MECHANISM OF CATHEPSIN B INHIBITION BY ANTIBIOTIC      
JRNL        TITL 2 NITROXOLINE AND RELATED COMPOUNDS                            
JRNL        REF    CHEMMEDCHEM                   V.   6  1351 2011              
JRNL        REFN                   ISSN 1860-7179                               
JRNL        PMID   21598397                                                     
JRNL        DOI    10.1002/CMDC.201100098                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22508                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1134                            
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) : 2.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1264                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3938                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 284                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : 0.75000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.64000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4081 ; 0.022 ; 0.029       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5560 ; 1.986 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 3.049 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;32.742 ;23.989       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   595 ;17.607 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.054 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   564 ; 0.180 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3236 ; 0.018 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2528 ; 2.734 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4052 ; 4.452 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1553 ; 2.848 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1508 ; 4.526 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY. THE STRUCTURE WAS         
REMARK   3  REFINED ALSO WITH MAIN                                              
REMARK   4                                                                      
REMARK   4 3AI8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029286.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI111               
REMARK 200  OPTICS                         : COLLIMATING AND FOCUSING, PT-      
REMARK 200                                   COATED MIRRORS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25966                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.09600                            
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
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: 3K9M                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRIC ACID, 21% PEG6000, PH 3.0,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       76.84100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       14.98800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       76.84100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       14.98800            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU B  133   OE1  OE2                                            
REMARK 480     LYS B  166   CE   NZ                                             
REMARK 480     ASN B  210   OD1  ND2                                            
REMARK 480     LYS A  127   CD   CE   NZ                                        
REMARK 480     LYS A  141   CD   CE   NZ                                        
REMARK 480     LYS A  158   CD   CE   NZ                                        
REMARK 480     ASN A  210   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   OE2  GLU B    19     NH2  ARG B    85     1545     2.19            
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    LYS B   0   N   -  CA  -  C   ANGL. DEV. = -20.2 DEGREES          
REMARK 500    PRO A 138   C   -  N   -  CA  ANGL. DEV. = -14.6 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    LEU B   1       91.70     66.75                                   
REMARK 500    ASN B 222      166.54     74.88                                   
REMARK 500    LYS A 130       66.67   -101.13                                   
REMARK 500    ASN A 222      163.62     80.82                                   
REMARK 500    ALA A 248     -159.48   -159.11                                   
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 365        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 397        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH A 399        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 351        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH B 353        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B 357        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B 385        DISTANCE =  5.41 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNQ B 255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNQ A 255                 
DBREF  3AI8 B   -1   254  UNP    P07858   CATB_HUMAN      78    333             
DBREF  3AI8 A   -1   254  UNP    P07858   CATB_HUMAN      78    333             
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 CYS 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 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 CYS 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                          
HET    HNQ  B 255      14                                                       
HET    HNQ  A 255      14                                                       
HETNAM     HNQ 5-NITROQUINOLIN-8-OL                                             
HETSYN     HNQ NITROXOLINE                                                      
FORMUL   3  HNQ    2(C9 H6 N2 O3)                                               
FORMUL   5  HOH   *284(H2 O)                                                    
HELIX    1   1 ALA B    7  TRP B   11  1                                   5    
HELIX    2   2 CYS B   14  GLU B   19  5                                   6    
HELIX    3   3 SER B   28  THR B   46  1                                  19    
HELIX    4   4 SER B   55  CYS B   63  1                                   9    
HELIX    5   5 GLY B   64  GLY B   68  5                                   5    
HELIX    6   6 ASP B   69  GLY B   73  5                                   5    
HELIX    7   7 TYR B   75  LYS B   86  1                                  12    
HELIX    8   8 THR B  139  LYS B  144  1                                   6    
HELIX    9   9 SER B  156  GLY B  168  1                                  13    
HELIX   10  10 SER B  178  LEU B  182  1                                   5    
HELIX   11  11 ASP B  238  ILE B  242  5                                   5    
HELIX   12  12 ALA A    7  TRP A   11  1                                   5    
HELIX   13  13 CYS A   14  GLU A   19  5                                   6    
HELIX   14  14 SER A   28  THR A   46  1                                  19    
HELIX   15  15 SER A   55  CYS A   63  1                                   9    
HELIX   16  16 GLY A   64  GLY A   68  5                                   5    
HELIX   17  17 ASP A   69  GLY A   73  5                                   5    
HELIX   18  18 TYR A   75  LYS A   86  1                                  12    
HELIX   19  19 THR A  139  LYS A  144  1                                   6    
HELIX   20  20 SER A  156  GLY A  168  1                                  13    
HELIX   21  21 SER A  178  LEU A  182  1                                   5    
HELIX   22  22 ASP A  238  ILE A  242  5                                   5    
SHEET    1   A 3 PHE B   5  ASP B   6  0                                        
SHEET    2   A 3 MET B 195  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3   A 3 VAL B 170  TYR B 177 -1  N  VAL B 176   O  MET B 196           
SHEET    1   B 5 PHE B   5  ASP B   6  0                                        
SHEET    2   B 5 MET B 195  GLU B 209 -1  O  TRP B 206   N  PHE B   5           
SHEET    3   B 5 THR B 212  ALA B 218 -1  O  THR B 212   N  GLU B 209           
SHEET    4   B 5 PHE B 230  LEU B 234 -1  O  PHE B 231   N  VAL B 217           
SHEET    5   B 5 VAL B 187  TYR B 188  1  N  TYR B 188   O  LYS B 232           
SHEET    1   C 2 TYR B 151  SER B 152  0                                        
SHEET    2   C 2 VAL B 247  ALA B 248 -1  O  ALA B 248   N  TYR B 151           
SHEET    1   D 3 PHE A   5  ASP A   6  0                                        
SHEET    2   D 3 MET A 195  GLU A 209 -1  O  TRP A 206   N  PHE A   5           
SHEET    3   D 3 VAL A 170  TYR A 177 -1  N  VAL A 176   O  MET A 196           
SHEET    1   E 5 PHE A   5  ASP A   6  0                                        
SHEET    2   E 5 MET A 195  GLU A 209 -1  O  TRP A 206   N  PHE A   5           
SHEET    3   E 5 THR A 212  ALA A 218 -1  O  ALA A 218   N  ARG A 202           
SHEET    4   E 5 PHE A 230  LEU A 234 -1  O  PHE A 231   N  VAL A 217           
SHEET    5   E 5 VAL A 187  TYR A 188  1  N  TYR A 188   O  LYS A 232           
SHEET    1   F 2 TYR A 151  SER A 152  0                                        
SHEET    2   F 2 VAL A 247  ALA A 248 -1  O  ALA A 248   N  TYR A 151           
SSBOND   1 CYS B   14    CYS B   43                          1555   1555  2.02  
SSBOND   2 CYS B   26    CYS B   71                          1555   1555  2.02  
SSBOND   3 CYS B   62    CYS B  128                          1555   1555  2.02  
SSBOND   4 CYS B   63    CYS B   67                          1555   1555  2.02  
SSBOND   5 CYS B  100    CYS B  132                          1555   1555  2.04  
SSBOND   6 CYS B  108    CYS B  119                          1555   1555  2.03  
SSBOND   7 CYS A   14    CYS A   43                          1555   1555  2.03  
SSBOND   8 CYS A   26    CYS A   71                          1555   1555  2.03  
SSBOND   9 CYS A   62    CYS A  128                          1555   1555  2.03  
SSBOND  10 CYS A   63    CYS A   67                          1555   1555  2.02  
SSBOND  11 CYS A  100    CYS A  132                          1555   1555  2.00  
SSBOND  12 CYS A  108    CYS A  119                          1555   1555  2.01  
SITE     1 AC1 12 GLN B  23  GLY B  24  SER B  25  CYS B  26                    
SITE     2 AC1 12 GLY B  27  HIS B 110  HIS B 111  THR B 120                    
SITE     3 AC1 12 GLY B 121  TRP B 221  HOH B 276  HOH B 344                    
SITE     1 AC2 10 GLN A  23  GLY A  24  SER A  25  CYS A  26                    
SITE     2 AC2 10 GLY A  27  HIS A 110  HIS A 111  THR A 120                    
SITE     3 AC2 10 HIS A 199  TRP A 221                                          
CRYST1  153.682   29.976  119.198  90.00 126.25  90.00 C 1 2 1       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      0.006507  0.000000  0.004772        0.00000                         
SCALE2      0.000000  0.033360  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010403        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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