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Database: PDB
Entry: 5QC0
LinkDB: 5QC0
Original site: 5QC0 
HEADER    HYDROLASE                               21-AUG-17   5QC0              
TITLE     CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN S;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.22.27;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTSS;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    D3R, CATHEPSIN S, LIGAND DOCKING, HYDROLASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,S.K.BURLEY        
REVDAT   5   17-NOV-21 5QC0    1       REMARK                                   
REVDAT   4   10-FEB-21 5QC0    1       AUTHOR JRNL                              
REVDAT   3   06-JUN-18 5QC0    1       REMARK SCALE  ATOM                       
REVDAT   2   21-FEB-18 5QC0    1       REMARK                                   
REVDAT   1   20-DEC-17 5QC0    0                                                
JRNL        AUTH   S.D.BEMBENEK,M.K.AMERIKS,T.MIRZADEGAN,H.YANG,C.SHAO,         
JRNL        AUTH 2 S.K.BURLEY                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CATHEPSIN-S WITH BOUND LIGAND     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23098                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1246                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 577                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 26.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 26                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3400                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 311                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.49000                                             
REMARK   3    B22 (A**2) : 0.40000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.12000                                              
REMARK   3    B13 (A**2) : -0.20000                                             
REMARK   3    B23 (A**2) : 0.01000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.309         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.167         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.097         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3590 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3148 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4869 ; 1.317 ; 1.928       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7337 ; 0.922 ; 2.990       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   438 ; 5.587 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;38.803 ;24.444       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   553 ;13.562 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;24.242 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   485 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4038 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   746 ; 0.001 ; 0.020       
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):  1758 ; 1.323 ; 2.802       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1757 ; 1.309 ; 2.801       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2194 ; 2.027 ; 4.197       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2195 ; 2.030 ; 4.197       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1832 ; 1.624 ; 3.010       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1830 ; 1.622 ; 3.010       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2676 ; 2.577 ; 4.434       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4196 ; 3.932 ;32.959       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4126 ; 3.783 ;32.607       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    218       B     1    218   14508  0.06  0.05     
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   : 1.20                                          
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                                                          
REMARK   4                                                                      
REMARK   4 5QC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1001401757.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23098                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 4.5, 200MM       
REMARK 280  AMMONIUM ACETATE, 25% PEG 8000. PROTEIN CONCENTRATION 7 MG/ML,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 4.50            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     GLY A   220                                                      
REMARK 465     GLY A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     ILE B     0                                                      
REMARK 465     GLY B   221                                                      
REMARK 465     GLY B   222                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A   0    CG1  CG2  CD1                                       
REMARK 470     LYS A  60    CD   CE   NZ                                        
REMARK 470     LYS A  82    CE   NZ                                             
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
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  58     -120.51   -116.18                                   
REMARK 500    THR B  58     -118.67   -116.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     BQJ B   901                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BQJ A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BQJ B 901                 
DBREF  5QC0 A    0   217  UNP    P25774   CATS_HUMAN     114    331             
DBREF  5QC0 B    0   217  UNP    P25774   CATS_HUMAN     114    331             
SEQADV 5QC0 SER A   25  UNP  P25774    CYS   139 ENGINEERED MUTATION            
SEQADV 5QC0 LEU A  218  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLN A  219  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY A  220  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY A  221  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY A  222  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 SER B   25  UNP  P25774    CYS   139 ENGINEERED MUTATION            
SEQADV 5QC0 LEU B  218  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLN B  219  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY B  220  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY B  221  UNP  P25774              EXPRESSION TAG                 
SEQADV 5QC0 GLY B  222  UNP  P25774              EXPRESSION TAG                 
SEQRES   1 A  223  ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS          
SEQRES   2 A  223  VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER          
SEQRES   3 A  223  TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU          
SEQRES   4 A  223  LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN          
SEQRES   5 A  223  ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS          
SEQRES   6 A  223  GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR          
SEQRES   7 A  223  ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR          
SEQRES   8 A  223  PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER          
SEQRES   9 A  223  LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU          
SEQRES  10 A  223  PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA          
SEQRES  11 A  223  ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS          
SEQRES  12 A  223  PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU          
SEQRES  13 A  223  PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL          
SEQRES  14 A  223  VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU          
SEQRES  15 A  223  VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY          
SEQRES  16 A  223  TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY          
SEQRES  17 A  223  ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY          
SEQRES  18 A  223  GLY GLY                                                      
SEQRES   1 B  223  ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS          
SEQRES   2 B  223  VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA SER          
SEQRES   3 B  223  TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU          
SEQRES   4 B  223  LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN          
SEQRES   5 B  223  ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS          
SEQRES   6 B  223  GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR          
SEQRES   7 B  223  ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR          
SEQRES   8 B  223  PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER          
SEQRES   9 B  223  LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU          
SEQRES  10 B  223  PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA          
SEQRES  11 B  223  ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS          
SEQRES  12 B  223  PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU          
SEQRES  13 B  223  PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL          
SEQRES  14 B  223  VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU          
SEQRES  15 B  223  VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY          
SEQRES  16 B  223  TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY          
SEQRES  17 B  223  ILE ALA SER PHE PRO SER TYR PRO GLU ILE LEU GLN GLY          
SEQRES  18 B  223  GLY GLY                                                      
HET    BQJ  A 901      46                                                       
HET    BQJ  B 901      46                                                       
HETNAM     BQJ 2-(DIMETHYLAMINO)-1-[4-(2-OXO-2-{3-[3-{[2-(PIPERIDIN-1-          
HETNAM   2 BQJ  YL)ETHYL]SULFANYL}-4-(TRIFLUOROMETHYL)PHENYL]-1-                
HETNAM   3 BQJ  PROPYL-1,4,6,7-TETRAHYDRO-5H-PYRAZOLO[4,3-C]PYRIDIN-5-          
HETNAM   4 BQJ  YL}ETHYL)PIPERIDIN-1-YL]ETHAN-1-ONE                             
FORMUL   3  BQJ    2(C34 H49 F3 N6 O2 S)                                        
FORMUL   5  HOH   *311(H2 O)                                                    
HELIX    1 AA1 ARG A    8  GLY A   11  5                                   4    
HELIX    2 AA2 ALA A   24  GLY A   43  1                                  20    
HELIX    3 AA3 SER A   49  SER A   57  1                                   9    
HELIX    4 AA4 THR A   58  GLY A   62  5                                   5    
HELIX    5 AA5 LYS A   64  GLY A   68  5                                   5    
HELIX    6 AA6 PHE A   70  LYS A   82  1                                  13    
HELIX    7 AA7 ASP A  102  LYS A  104  5                                   3    
HELIX    8 AA8 ARG A  120  LYS A  131  1                                  12    
HELIX    9 AA9 HIS A  142  LEU A  147  1                                   6    
HELIX   10 AB1 ASN A  204  ILE A  208  5                                   5    
HELIX   11 AB2 ARG B    8  GLY B   11  5                                   4    
HELIX   12 AB3 ALA B   24  GLY B   43  1                                  20    
HELIX   13 AB4 SER B   49  SER B   57  1                                   9    
HELIX   14 AB5 THR B   58  GLY B   62  5                                   5    
HELIX   15 AB6 LYS B   64  GLY B   68  5                                   5    
HELIX   16 AB7 PHE B   70  LYS B   82  1                                  13    
HELIX   17 AB8 ASP B  102  LYS B  104  5                                   3    
HELIX   18 AB9 ARG B  120  LYS B  131  1                                  12    
HELIX   19 AC1 HIS B  142  LEU B  147  1                                   6    
HELIX   20 AC2 ASN B  204  ILE B  208  5                                   5    
SHEET    1 AA1 3 VAL A   5  ASP A   6  0                                        
SHEET    2 AA1 3 HIS A 164  LEU A 174 -1  O  TYR A 171   N  VAL A   5           
SHEET    3 AA1 3 VAL A 134  VAL A 138 -1  N  VAL A 136   O  VAL A 166           
SHEET    1 AA2 5 VAL A   5  ASP A   6  0                                        
SHEET    2 AA2 5 HIS A 164  LEU A 174 -1  O  TYR A 171   N  VAL A   5           
SHEET    3 AA2 5 LYS A 177  LYS A 183 -1  O  LYS A 183   N  LEU A 167           
SHEET    4 AA2 5 TYR A 195  ALA A 199 -1  O  ILE A 196   N  VAL A 182           
SHEET    5 AA2 5 VAL A 152  TYR A 153  1  N  TYR A 153   O  ARG A 197           
SHEET    1 AA3 2 ILE A  84  ASP A  85  0                                        
SHEET    2 AA3 2 ARG A 106  ALA A 108 -1  O  ALA A 107   N  ILE A  84           
SHEET    1 AA4 2 LYS A 112  GLU A 115  0                                        
SHEET    2 AA4 2 SER A 213  GLU A 216 -1  O  GLU A 216   N  LYS A 112           
SHEET    1 AA5 3 VAL B   5  ASP B   6  0                                        
SHEET    2 AA5 3 HIS B 164  LEU B 174 -1  O  TYR B 171   N  VAL B   5           
SHEET    3 AA5 3 VAL B 134  VAL B 138 -1  N  VAL B 136   O  VAL B 166           
SHEET    1 AA6 5 VAL B   5  ASP B   6  0                                        
SHEET    2 AA6 5 HIS B 164  LEU B 174 -1  O  TYR B 171   N  VAL B   5           
SHEET    3 AA6 5 LYS B 177  LYS B 183 -1  O  LYS B 183   N  LEU B 167           
SHEET    4 AA6 5 TYR B 195  ALA B 199 -1  O  ILE B 196   N  VAL B 182           
SHEET    5 AA6 5 VAL B 152  TYR B 153  1  N  TYR B 153   O  ARG B 197           
SHEET    1 AA7 2 ILE B  84  ASP B  85  0                                        
SHEET    2 AA7 2 ARG B 106  ALA B 108 -1  O  ALA B 107   N  ILE B  84           
SHEET    1 AA8 2 LYS B 112  GLU B 115  0                                        
SHEET    2 AA8 2 SER B 213  GLU B 216 -1  O  GLU B 216   N  LYS B 112           
SSBOND   1 CYS A   22    CYS A   66                          1555   1555  2.02  
SSBOND   2 CYS A   56    CYS A   99                          1555   1555  2.06  
SSBOND   3 CYS A  158    CYS A  206                          1555   1555  2.04  
SSBOND   4 CYS B   22    CYS B   66                          1555   1555  2.06  
SSBOND   5 CYS B   56    CYS B   99                          1555   1555  2.06  
SSBOND   6 CYS B  158    CYS B  206                          1555   1555  2.04  
SITE     1 AC1 21 TRP A  26  GLY A  62  GLY A  69  PHE A  70                    
SITE     2 AC1 21 MET A  71  THR A  72  GLU A 115  GLY A 137                    
SITE     3 AC1 21 ASN A 163  HIS A 164  GLY A 165  PHE A 211                    
SITE     4 AC1 21 HOH A1022  HOH A1032  HOH A1088  HOH A1099                    
SITE     5 AC1 21 HOH A1114  HOH A1123  TYR B 118  GLY B 119                    
SITE     6 AC1 21 ARG B 120                                                     
SITE     1 AC2 16 LYS B  60  GLY B  62  GLY B  69  PHE B  70                    
SITE     2 AC2 16 MET B  71  THR B  72  GLU B 115  GLY B 137                    
SITE     3 AC2 16 VAL B 162  ASN B 163  HIS B 164  GLY B 165                    
SITE     4 AC2 16 PHE B 211  HOH B1018  HOH B1076  HOH B1101                    
CRYST1   36.980   52.930   58.460  70.92  72.06  73.46 P 1           2          
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      0.027042 -0.008031 -0.006890        0.00000                         
SCALE2      0.000000  0.019708 -0.005357        0.00000                         
SCALE3      0.000000  0.000000  0.018632        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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