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Database: PDB
Entry: 2YJ8
LinkDB: 2YJ8
Original site: 2YJ8 
HEADER    HYDROLASE                               19-MAY-11   2YJ8              
TITLE     CATHEPSIN L WITH A NITRILE INHIBITOR                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN L1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 114-333;                        
COMPND   5 SYNONYM: MAJOR EXCRETED PROTEIN, MEP, CATHEPSIN L1 HEAVY CHAIN,      
COMPND   6  CATHEPSIN L1 LIGHT CHAIN;                                           
COMPND   7 EC: 3.4.22.15;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, DRUG DESIGN, THIOL PROTEASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.W.BANNER,J.M.BENZ,W.HAAP                                            
REVDAT   1   23-NOV-11 2YJ8    0                                                
JRNL        AUTH   L.A.HARDEGGER,B.KUHN,B.SPINNLER,L.ANSELM,R.ECABERT,M.STIHLE, 
JRNL        AUTH 2 B.GSELL,R.THOMA,J.DIEZ,J.M.BENZ,J.PLANCHER,G.HARTMANN,       
JRNL        AUTH 3 Y.ISSHIKI,K.MORIKAMI,N.SHIMMA,W.HAAP,D.W.BANNER,F.DIEDERICH  
JRNL        TITL   HALOGEN BONDING AT THE ACTIVE SITES OF HUMAN CATHEPSIN L     
JRNL        TITL 2 AND MEK1 KINASE: EFFICIENT INTERACTIONS IN DIFFERENT         
JRNL        TITL 3 ENVIRONMENTS.                                                
JRNL        REF    CHEMMEDCHEM                   V.   6  2048 2011              
JRNL        REFN                   ISSN 1860-7179                               
JRNL        PMID   21898833                                                     
JRNL        DOI    10.1002/CMDC.201100353                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0112                                      
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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.46                          
REMARK   3   NUMBER OF REFLECTIONS             : 45543                          
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) : 0.14264                         
REMARK   3   R VALUE            (WORKING SET) : 0.14055                         
REMARK   3   FREE R VALUE                     : 0.18159                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2417                            
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) : 1.300                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.334                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2964                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.326                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.318                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1795                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 271                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.4                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.877                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.02                                                
REMARK   3    B22 (A**2) : -1.15                                                
REMARK   3    B33 (A**2) : 2.18                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.053         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.052         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.766         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1897 ; 0.011 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  1269 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2589 ; 1.414 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3097 ; 0.889 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   242 ; 5.584 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    92 ;35.595 ;25.217       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   300 ;12.362 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;13.137 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   255 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2213 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   398 ; 0.003 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3166 ; 2.738 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    74 ;39.661 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3302 ;17.631 ; 5.000       
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 : BABINET MODEL WITH 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. HYDROGENS GENERATED IN REFMAC, THOSE WITH ZERO          
REMARK   3   OCCUPANCY REMOVED. U VALUES REFINED INDIVIDUALLY.                  
REMARK   4                                                                      
REMARK   4 2YJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-48337.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.30                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.59                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.57                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.78                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.46                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ISOMORPHOUS TO PDB ENTRY 2YJ2                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.5                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.2M              
REMARK 280  SODIUM ACETATE, 25 % PEG 3350                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       22.98750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.10900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.63250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.10900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.98750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.63250            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     GLU A   176                                                      
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    GLN A  21       50.96    -92.88                                   
REMARK 500    ASP A 160       70.73   -109.11                                   
REMARK 500    ASP A 162       15.70   -140.09                                   
REMARK 500    ALA A 214       61.36   -151.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE NITRILE (2S,4R)-4-(2-CHLORO-BENZENESULFONYL)-1-[1-(4-IODO-PHENYL)
REMARK 600 -CYCLOPROPANECARBONYL]-PYRROLIDINE-2-CARBOXYLIC ACID (1-CYANO-       
REMARK 600 CYCLOPROPYL)-AMIDE MAKES A COVALENT LINK TO THE ENZYME               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YJ8 A1221                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1222                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CJL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM                    
REMARK 900 RELATED ID: 1CS8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PROCATHEPSIN L                                 
REMARK 900 RELATED ID: 2XU4   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2VHS   RELATED DB: PDB                                   
REMARK 900  CATHSILICATEIN, A CHIMERA                                           
REMARK 900 RELATED ID: 1ICF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II                 
REMARK 900  FRAGMENT IN COMPLEX WITH CATHEPSIN L                                
REMARK 900 RELATED ID: 2XU3   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 1MHW   RELATED DB: PDB                                   
REMARK 900  DESIGN OF NON-COVALENT INHIBITORS OF HUMAN CATHEPSIN L              
REMARK 900  .FROM THE 96-RESIDUE PROREGION TO OPTIMIZED TRIPEPTIDES             
REMARK 900 RELATED ID: 2XU5   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2XU1   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2YJ9   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2YJB   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2YJ2   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
REMARK 900 RELATED ID: 2YJC   RELATED DB: PDB                                   
REMARK 900  CATHEPSIN L WITH A NITRILE INHIBITOR                                
DBREF  2YJ8 A    1   220  UNP    P07711   CATL1_HUMAN    114    333             
SEQRES   1 A  220  ALA PRO ARG SER VAL ASP TRP ARG GLU LYS GLY TYR VAL          
SEQRES   2 A  220  THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP          
SEQRES   3 A  220  ALA PHE SER ALA THR GLY ALA LEU GLU GLY GLN MET PHE          
SEQRES   4 A  220  ARG LYS THR GLY ARG LEU ILE SER LEU SER GLU GLN ASN          
SEQRES   5 A  220  LEU VAL ASP CYS SER GLY PRO GLN GLY ASN GLU GLY CYS          
SEQRES   6 A  220  ASN GLY GLY LEU MET ASP TYR ALA PHE GLN TYR VAL GLN          
SEQRES   7 A  220  ASP ASN GLY GLY LEU ASP SER GLU GLU SER TYR PRO TYR          
SEQRES   8 A  220  GLU ALA THR GLU GLU SER CYS LYS TYR ASN PRO LYS TYR          
SEQRES   9 A  220  SER VAL ALA ASN ASP THR GLY PHE VAL ASP ILE PRO LYS          
SEQRES  10 A  220  GLN GLU LYS ALA LEU MET LYS ALA VAL ALA THR VAL GLY          
SEQRES  11 A  220  PRO ILE SER VAL ALA ILE ASP ALA GLY HIS GLU SER PHE          
SEQRES  12 A  220  LEU PHE TYR LYS GLU GLY ILE TYR PHE GLU PRO ASP CYS          
SEQRES  13 A  220  SER SER GLU ASP MET ASP HIS GLY VAL LEU VAL VAL GLY          
SEQRES  14 A  220  TYR GLY PHE GLU SER THR GLU SER ASP ASN ASN LYS TYR          
SEQRES  15 A  220  TRP LEU VAL LYS ASN SER TRP GLY GLU GLU TRP GLY MET          
SEQRES  16 A  220  GLY GLY TYR VAL LYS MET ALA LYS ASP ARG ARG ASN HIS          
SEQRES  17 A  220  CYS GLY ILE ALA SER ALA ALA SER TYR PRO THR VAL              
HET    YJ8  A1221      58                                                       
HET    GOL  A1222      12                                                       
HETNAM     YJ8 (2S,4R)-4-(2-CHLORO-BENZENESULFONYL)-1-[1-(4-                    
HETNAM   2 YJ8  IODO-PHENYL)-CYCLOPROPANECARBONYL]-                             
HETNAM   3 YJ8  PYRROLIDINE-2-CARBOXYLIC ACID (1-IMINOMETHYL-                   
HETNAM   4 YJ8  CYCLOPROPYL)-AMIDE                                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN                                                         
FORMUL   2  YJ8    C25 H25 CL I N3 O4 S                                         
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *271(H2 O)                                                    
HELIX    1   1 ARG A    8  GLY A   11  5                                   4    
HELIX    2   2 SER A   24  GLY A   43  1                                  20    
HELIX    3   3 SER A   49  SER A   57  1                                   9    
HELIX    4   4 GLU A   63  CYS A   65  5                                   3    
HELIX    5   5 LEU A   69  GLY A   81  1                                  13    
HELIX    6   6 ASN A  101  LYS A  103  5                                   3    
HELIX    7   7 GLN A  118  GLY A  130  1                                  13    
HELIX    8   8 HIS A  140  PHE A  145  1                                   6    
HELIX    9   9 ASN A  207  ILE A  211  5                                   5    
SHEET    1  AA 2 VAL A   5  ASP A   6  0                                        
SHEET    2  AA 2 HIS A 163  PHE A 172  1  O  TYR A 170   N  VAL A   5           
SHEET    1  AB 2 ILE A 132  ILE A 136  0                                        
SHEET    2  AB 2 HIS A 163  PHE A 172 -1  O  HIS A 163   N  ILE A 136           
SHEET    1  AC 5 ILE A 150  TYR A 151  0                                        
SHEET    2  AC 5 TYR A 198  ALA A 202  1  O  LYS A 200   N  TYR A 151           
SHEET    3  AC 5 LYS A 181  LYS A 186 -1  O  TRP A 183   N  MET A 201           
SHEET    4  AC 5 HIS A 163  PHE A 172 -1  O  LEU A 166   N  LYS A 186           
SHEET    5  AC 5 ILE A 132  ILE A 136 -1  O  ILE A 132   N  VAL A 167           
SHEET    1  AD 5 ILE A 150  TYR A 151  0                                        
SHEET    2  AD 5 TYR A 198  ALA A 202  1  O  LYS A 200   N  TYR A 151           
SHEET    3  AD 5 LYS A 181  LYS A 186 -1  O  TRP A 183   N  MET A 201           
SHEET    4  AD 5 HIS A 163  PHE A 172 -1  O  LEU A 166   N  LYS A 186           
SHEET    5  AD 5 VAL A   5  ASP A   6  1  O  VAL A   5   N  TYR A 170           
SHEET    1  AE 2 LEU A  83  ASP A  84  0                                        
SHEET    2  AE 2 SER A 105  ALA A 107 -1  N  VAL A 106   O  LEU A  83           
SHEET    1  AF 2 GLY A 111  ASP A 114  0                                        
SHEET    2  AF 2 SER A 216  THR A 219 -1  O  TYR A 217   N  VAL A 113           
SSBOND   1 CYS A   22    CYS A   65                          1555   1555  2.03  
SSBOND   2 CYS A   56    CYS A   98                          1555   1555  2.08  
SSBOND   3 CYS A  156    CYS A  209                          1555   1555  2.04  
LINK         SG  CYS A  25                 C18 YJ8 A1221     1555   1555  1.78  
SITE     1 AC1 19 GLN A  19  GLY A  23  SER A  24  CYS A  25                    
SITE     2 AC1 19 TRP A  26  GLY A  61  GLY A  67  GLY A  68                    
SITE     3 AC1 19 LEU A  69  MET A  70  ALA A 135  MET A 161                    
SITE     4 AC1 19 ASP A 162  HIS A 163  GLY A 164  ARG A 206                    
SITE     5 AC1 19 ALA A 214  HOH A2131  HOH A2271                               
SITE     1 AC2  2 ASN A  18  HOH A2064                                          
CRYST1   45.975   57.265   76.218  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021751  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013120        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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