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Database: PDB
Entry: 4CI9
LinkDB: 4CI9
Original site: 4CI9 
HEADER    HYDROLASE                               06-DEC-13   4CI9              
TITLE     CRYSTAL STRUCTURE OF CATHEPSIN A, APO-STRUCTURE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A,        
COMPND   5 PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR BETA-   
COMPND   6 GALACTOSIDASE;                                                       
COMPND   7 EC: 3.4.16.5;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: ACTIVATED WITH TRYPSIN-SEPHAROSE                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS PVL1393                        
KEYWDS    HYDROLASE, DRUG DISCOVERY, SERINE CARBOXYPEPTIDASE, CARDIOVASCULAR    
KEYWDS   2 DRUG, HEART FAILURE, ENDOTHELIN, TETRAHEDRAL INTERMEDIATE, COVALENT  
KEYWDS   3 INHIBITOR                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.A.SCHREUDER,A.LIESUM,K.KROLL,B.BOEHNISCH,C.BUNING,S.RUF,C.BUNING,   
AUTHOR   2 T.SADOWSKI                                                           
REVDAT   4   29-JUL-20 4CI9    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-MAR-19 4CI9    1       JRNL   REMARK LINK                       
REVDAT   2   02-APR-14 4CI9    1       JRNL                                     
REVDAT   1   26-FEB-14 4CI9    0                                                
JRNL        AUTH   H.A.SCHREUDER,A.LIESUM,K.KROLL,B.BOHNISCH,C.BUNING,S.RUF,    
JRNL        AUTH 2 T.SADOWSKI                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF CATHEPSIN A, A NOVEL TARGET FOR THE     
JRNL        TITL 2 TREATMENT OF CARDIOVASCULAR DISEASES.                        
JRNL        REF    BIOCHEM. BIOPHYS. RES.        V. 445   451 2014              
JRNL        REF  2 COMMUN.                                                      
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   24530914                                                     
JRNL        DOI    10.1016/J.BBRC.2014.02.014                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.RUF,C.BUNING,H.SCHREUDER,G.HORSTICK,W.LINZ,T.OLPP,         
REMARK   1  AUTH 2 J.PERNERSTORFER,K.HISS,K.KROLL,A.KANNT,M.KOHLMANN,D.LINZ,    
REMARK   1  AUTH 3 T.HUBSCHLE,H.RUTTEN,K.WIRTH,T.SCHMIDT,T.SADOWSKI             
REMARK   1  TITL   NOVEL BETA-AMINO ACID DERIVATIVES AS INHIBITORS OF CATHEPSIN 
REMARK   1  TITL 2 A.                                                           
REMARK   1  REF    J.MED.CHEM.                   V.  55  7636 2012              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   1  PMID   22861813                                                     
REMARK   1  DOI    10.1021/JM300663N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 56890                          
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)  : 0.166                          
REMARK   3   R VALUE            (WORKING SET)  : 0.165                          
REMARK   3   FREE R VALUE                      : 0.191                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2843                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.58                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.62                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 96.52                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3982                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2204                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3780                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2196                   
REMARK   3   BIN FREE R VALUE                        : 0.2340                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.07                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 202                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3302                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 614                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.12150                                              
REMARK   3    B22 (A**2) : 0.30080                                              
REMARK   3    B33 (A**2) : -3.42230                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.47780                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.165               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.089               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.085               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.083               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.081               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3576   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4882   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1213   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 99     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 520    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3576   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 441    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4641   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.91                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.84                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.59                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4CI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290059176.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
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) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56973                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: PDB ENTRY 4AZ0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CATHEPSIN A WAS CRYSTALLIZED USING THE   
REMARK 280  HANGING DROP METHOD: 1 UL OF PROTEIN SOLUTION, CONTAINING 6.5 MG/   
REMARK 280  ML CATHEPSIN A, 25 MM TRIS-HCL (PH 8.0) AND 300 MM NACL, WAS        
REMARK 280  MIXED WITH 1 UL RESERVOIR SOLUTION, CONTAINING 100 MM NAACETATE     
REMARK 280  (PH 4.5), 18-20% PEG400 AND 100 MM CDCL2, AND SET TO EQUILIBRATE    
REMARK 280  AT 4DEG.C. ROD-SHAPED CRYSTALS APPEARED IN ABOUT ONE WEEK., PH      
REMARK 280  4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
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       45.15500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.01500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       45.15500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.01500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -90.31000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2130  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2350  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2385  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   260                                                      
REMARK 465     PHE A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     TYR A   263                                                      
REMARK 465     GLU A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     THR A   267                                                      
REMARK 465     VAL A   268                                                      
REMARK 465     VAL A   269                                                      
REMARK 465     VAL A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     ASP A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     ILE A   276                                                      
REMARK 465     PHE A   277                                                      
REMARK 465     THR A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     LEU A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     LYS A   283                                                      
REMARK 465     ARG A   284                                                      
REMARK 465     MET A   285                                                      
REMARK 465     TRP A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     GLN A   288                                                      
REMARK 465     ALA A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     LEU A   291                                                      
REMARK 465     ARG A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     ARG A   298                                                      
REMARK 465     MET A   299                                                      
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     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
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    GLU A  69      -75.21   -109.15                                   
REMARK 500    SER A 150     -114.45     56.79                                   
REMARK 500    SER A 150     -109.91     53.80                                   
REMARK 500    GLN A 215     -120.52     64.64                                   
REMARK 500    TYR A 221      -66.26    -97.95                                   
REMARK 500    ASN A 248       97.10   -165.96                                   
REMARK 500    TYR A 402       59.34   -100.01                                   
REMARK 500    MET A 430       79.16   -107.59                                   
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 A2019        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A2020        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH A2083        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH A2086        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A2087        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A2100        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A2180        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A2230        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A2233        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A2250        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A2591        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A2611        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH A2612        DISTANCE =  8.94 ANGSTROMS                       
REMARK 525    HOH A2613        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH A2614        DISTANCE =  6.45 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     DMS A 1454                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CIA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATHEPSIN A, COMPLEXED WITH COMPOUND 1          
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AT THE C-TERMINUS, ONE EXTRA GLU IS PRESENT AS A LEFTOVER            
REMARK 999 FROM A MYC-TAG                                                       
DBREF  4CI9 A    1   452  UNP    P10619   PPGB_HUMAN      29    480             
SEQADV 4CI9 SER A   -1  UNP  P10619              EXPRESSION TAG                 
SEQADV 4CI9 ARG A    0  UNP  P10619              EXPRESSION TAG                 
SEQADV 4CI9 GLU A  453  UNP  P10619              EXPRESSION TAG                 
SEQRES   1 A  455  SER ARG ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO          
SEQRES   2 A  455  GLY LEU ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY          
SEQRES   3 A  455  TYR LEU LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP          
SEQRES   4 A  455  PHE VAL GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL          
SEQRES   5 A  455  VAL LEU TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU          
SEQRES   6 A  455  ASP GLY LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN          
SEQRES   7 A  455  PRO ASP GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP          
SEQRES   8 A  455  ASN LEU ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA          
SEQRES   9 A  455  GLY VAL GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA          
SEQRES  10 A  455  THR ASN ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA          
SEQRES  11 A  455  LEU GLN ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN          
SEQRES  12 A  455  ASN LYS LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE          
SEQRES  13 A  455  TYR ILE PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO          
SEQRES  14 A  455  SER MET ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU          
SEQRES  15 A  455  SER SER TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE          
SEQRES  16 A  455  ALA TYR TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER          
SEQRES  17 A  455  SER LEU GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN          
SEQRES  18 A  455  PHE TYR ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU          
SEQRES  19 A  455  GLN GLU VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN          
SEQRES  20 A  455  ILE TYR ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO          
SEQRES  21 A  455  SER HIS PHE ARG TYR GLU LYS ASP THR VAL VAL VAL GLN          
SEQRES  22 A  455  ASP LEU GLY ASN ILE PHE THR ARG LEU PRO LEU LYS ARG          
SEQRES  23 A  455  MET TRP HIS GLN ALA LEU LEU ARG SER GLY ASP LYS VAL          
SEQRES  24 A  455  ARG MET ASP PRO PRO CYS THR ASN THR THR ALA ALA SER          
SEQRES  25 A  455  THR TYR LEU ASN ASN PRO TYR VAL ARG LYS ALA LEU ASN          
SEQRES  26 A  455  ILE PRO GLU GLN LEU PRO GLN TRP ASP MET CYS ASN PHE          
SEQRES  27 A  455  LEU VAL ASN LEU GLN TYR ARG ARG LEU TYR ARG SER MET          
SEQRES  28 A  455  ASN SER GLN TYR LEU LYS LEU LEU SER SER GLN LYS TYR          
SEQRES  29 A  455  GLN ILE LEU LEU TYR ASN GLY ASP VAL ASP MET ALA CYS          
SEQRES  30 A  455  ASN PHE MET GLY ASP GLU TRP PHE VAL ASP SER LEU ASN          
SEQRES  31 A  455  GLN LYS MET GLU VAL GLN ARG ARG PRO TRP LEU VAL LYS          
SEQRES  32 A  455  TYR GLY ASP SER GLY GLU GLN ILE ALA GLY PHE VAL LYS          
SEQRES  33 A  455  GLU PHE SER HIS ILE ALA PHE LEU THR ILE LYS GLY ALA          
SEQRES  34 A  455  GLY HIS MET VAL PRO THR ASP LYS PRO LEU ALA ALA PHE          
SEQRES  35 A  455  THR MET PHE SER ARG PHE LEU ASN LYS GLN PRO TYR GLU          
MODRES 4CI9 ASN A  117  ASN  GLYCOSYLATION SITE                                 
MODRES 4CI9 ASN A  305  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    DMS  A1454       3                                                       
HET    ACT  A1455       4                                                       
HET    ACT  A1456       4                                                       
HET    GOL  A1457       6                                                       
HET    GOL  A1458       6                                                       
HET    SO4  A1459       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   4  DMS    C2 H6 O S                                                    
FORMUL   5  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  HOH   *614(H2 O)                                                    
HELIX    1   1 PRO A    2  ASP A    5  5                                   4    
HELIX    2   2 SER A   62  GLU A   69  1                                   8    
HELIX    3   3 SER A   88  ILE A   92  5                                   5    
HELIX    4   4 ASN A  117  PHE A  136  1                                  20    
HELIX    5   5 PRO A  137  LYS A  140  5                                   4    
HELIX    6   6 TYR A  151  GLN A  165  1                                  15    
HELIX    7   7 SER A  182  HIS A  197  1                                  16    
HELIX    8   8 GLY A  201  CYS A  212  1                                  12    
HELIX    9   9 ASP A  225  ASN A  241  1                                  17    
HELIX   10  10 THR A  306  ASN A  314  1                                   9    
HELIX   11  11 ASN A  315  LEU A  322  1                                   8    
HELIX   12  12 ASN A  335  TYR A  342  1                                   8    
HELIX   13  13 MET A  349  SER A  359  1                                  11    
HELIX   14  14 ASN A  376  LEU A  387  1                                  12    
HELIX   15  15 GLY A  403  SER A  405  5                                   3    
HELIX   16  16 MET A  430  LYS A  435  1                                   6    
HELIX   17  17 LYS A  435  ASN A  448  1                                  14    
SHEET    1  AA 2 GLN A  21  LYS A  27  0                                        
SHEET    2  AA 2 LYS A  32  VAL A  39 -1  O  LEU A  34   N  LEU A  26           
SHEET    1  AB 2 TYR A 108  SER A 109  0                                        
SHEET    2  AB 2 LYS A  32  VAL A  39  1  O  HIS A  33   N  TYR A 108           
SHEET    1  AC10 ARG A 396  LYS A 401  0                                        
SHEET    2  AC10 GLU A 407  PHE A 416 -1  O  GLN A 408   N  VAL A 400           
SHEET    3  AC10 ILE A 419  ILE A 424 -1  O  ILE A 419   N  PHE A 416           
SHEET    4  AC10 GLN A 363  GLY A 369  1  O  ILE A 364   N  ALA A 420           
SHEET    5  AC10 LEU A 171  GLY A 177  1  O  GLN A 172   N  GLN A 363           
SHEET    6  AC10 LEU A 144  GLU A 149  1  O  LEU A 144   N  GLN A 172           
SHEET    7  AC10 VAL A  50  LEU A  54  1  O  VAL A  50   N  PHE A 145           
SHEET    8  AC10 ASN A  94  LEU A  98  1  O  ASN A  94   N  VAL A  51           
SHEET    9  AC10 LYS A  32  VAL A  39 -1  O  TRP A  37   N  TYR A  97           
SHEET   10  AC10 TYR A 108  SER A 109  1  O  TYR A 108   N  HIS A  33           
SHEET    1  AD10 ARG A 396  LYS A 401  0                                        
SHEET    2  AD10 GLU A 407  PHE A 416 -1  O  GLN A 408   N  VAL A 400           
SHEET    3  AD10 ILE A 419  ILE A 424 -1  O  ILE A 419   N  PHE A 416           
SHEET    4  AD10 GLN A 363  GLY A 369  1  O  ILE A 364   N  ALA A 420           
SHEET    5  AD10 LEU A 171  GLY A 177  1  O  GLN A 172   N  GLN A 363           
SHEET    6  AD10 LEU A 144  GLU A 149  1  O  LEU A 144   N  GLN A 172           
SHEET    7  AD10 VAL A  50  LEU A  54  1  O  VAL A  50   N  PHE A 145           
SHEET    8  AD10 ASN A  94  LEU A  98  1  O  ASN A  94   N  VAL A  51           
SHEET    9  AD10 LYS A  32  VAL A  39 -1  O  TRP A  37   N  TYR A  97           
SHEET   10  AD10 GLN A  21  LYS A  27 -1  O  TYR A  22   N  PHE A  38           
SHEET    1  AE 2 PHE A  73  VAL A  75  0                                        
SHEET    2  AE 2 LEU A  82  TYR A  84 -1  O  GLU A  83   N  LEU A  74           
SHEET    1  AF 2 CYS A 213  SER A 214  0                                        
SHEET    2  AF 2 LYS A 217  CYS A 218 -1  O  LYS A 217   N  SER A 214           
SSBOND   1 CYS A   60    CYS A  334                          1555   1555  2.04  
SSBOND   2 CYS A  212    CYS A  228                          1555   1555  2.03  
SSBOND   3 CYS A  213    CYS A  218                          1555   1555  2.03  
SSBOND   4 CYS A  253    CYS A  303                          1555   1555  2.04  
LINK         ND2 ASN A 117                 C1  NAG B   1     1555   1555  1.43  
LINK         ND2 ASN A 305                 C1  NAG C   1     1555   1555  1.43  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.42  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.42  
CISPEP   1 GLY A   57    PRO A   58          0        -2.06                     
CISPEP   2 SER A  100    PRO A  101          0        -1.58                     
CRYST1   90.310  102.030   48.550  90.00 101.27  90.00 C 1 2 1       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      0.011073  0.000000  0.002207        0.00000                         
SCALE2      0.000000  0.009801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021002        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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