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Database: PDB
Entry: 4AZ3
LinkDB: 4AZ3
Original site: 4AZ3 
HEADER    HYDROLASE                               22-JUN-12   4AZ3              
TITLE     CRYSTAL STRUCTURE OF CATHEPSIN A, COMPLEXED WITH 15A                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN 32 KDA CHAIN;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ACTIVATED PROTEASE RESIDUES 29-326;                        
COMPND   5 SYNONYM: LYSOSOMAL PROTECTIVE PROTEIN CARBOXYPEPTIDASE C,            
COMPND   6 CARBOXYPEPTIDASE L, CATHEPSIN A, PROTECTIVE PROTEIN CATHEPSIN A,     
COMPND   7 PPCA, PROTECTIVE PROTEIN FOR BETA-GALACTOSIDASE;                     
COMPND   8 EC: 3.4.16.5;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: ACTIVATED WITH TRYPSIN-SEPHAROSE;                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: LYSOSOMAL PROTECTIVE PROTEIN 20 KDA CHAIN;                 
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: ACTIVATED PROTEASE, RESIDUES 327-480;                      
COMPND  15 SYNONYM: LYSOSOMAL PROTECTIVE PROTEIN CARBOXYPEPTIDASE C,            
COMPND  16 CARBOXYPEPTIDASE L, CATHEPSIN A, PROTECTIVE PROTEIN CATHEPSIN A,     
COMPND  17 PPCA, PROTECTIVE PROTEIN FOR BETA-GALACTOSIDASE;                     
COMPND  18 EC: 3.4.16.5;                                                        
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 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: PVL1393;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PVL1393                                    
KEYWDS    HYDROLASE, DRUG DISCOVERY, CARBOXYPEPTIDASE, CARDIOVASCULAR           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RUF,C.BUNING,H.SCHREUDER,G.HORSTICK,W.LINZ,T.OLPP,J.PERNERSTORFER,  
AUTHOR   2 K.HISS,K.KROLL,A.KANNT,M.KOHLMANN,D.LINZ,T.HUEBSCHLE,H.RUETTEN,      
AUTHOR   3 K.WIRTH,T.SCHMIDT,T.SADOWSKI                                         
REVDAT   4   29-JUL-20 4AZ3    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   08-MAY-19 4AZ3    1       REMARK                                   
REVDAT   2   03-APR-19 4AZ3    1       REMARK LINK                              
REVDAT   1   26-SEP-12 4AZ3    0                                                
JRNL        AUTH   S.RUF,C.BUNING,H.SCHREUDER,G.HORSTICK,W.LINZ,T.OLPP,         
JRNL        AUTH 2 J.PERNERSTORFER,K.HISS,K.KROLL,A.KANNT,M.KOHLMANN,D.LINZ,    
JRNL        AUTH 3 T.HUBSCHLE,H.RUTTEN,K.WIRTH,T.SCHMIDT,T.SADOWSKI             
JRNL        TITL   NOVEL BETA-AMINO ACID DERIVATIVES AS INHIBITORS OF CATHEPSIN 
JRNL        TITL 2 A.                                                           
JRNL        REF    J.MED.CHEM.                   V.  55  7636 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22861813                                                     
JRNL        DOI    10.1021/JM300663N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27378                          
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)  : NULL                           
REMARK   3   R VALUE            (WORKING SET)  : 0.188                          
REMARK   3   FREE R VALUE                      : 0.215                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.910                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1344                           
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               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.04                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.12                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.05                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2892                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2409                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2762                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2405                   
REMARK   3   BIN FREE R VALUE                        : 0.2506                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.50                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 130                      
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            : 3288                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 95                                      
REMARK   3   SOLVENT ATOMS            : 422                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.96                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.50780                                             
REMARK   3    B22 (A**2) : -0.59040                                             
REMARK   3    B33 (A**2) : 1.09810                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.10750                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.244               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.234               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.167               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.218               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.164               
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      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3533   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4823   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1183   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 95     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 507    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3533   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 436    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : 3      ; 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   : 4443   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.007                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.96                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.38                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.46                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3  RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CD. NUMBER OF       
REMARK   3  ATOMS WITH PROPER CCP4 ATOM TYPE=3850. NUMBER WITH APPROX           
REMARK   3  DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED          
REMARK   3  CONTACTS=4.                                                         
REMARK   4                                                                      
REMARK   4 4AZ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290053025.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9395                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27381                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
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: MODEL DERIVED FROM PDB ENTRY 1IVY                    
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CATA 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 4 DEG. 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       45.29500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       45.29500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.40000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2207  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     SER A    -1                                                      
REMARK 465     SER A   259                                                      
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 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   0    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A   8    CG   CD   OE1  NE2                                  
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      -76.70   -106.95                                   
REMARK 500    PRO A 101     -168.47    -75.57                                   
REMARK 500    SER A 150     -111.10     56.24                                   
REMARK 500    GLN A 215      -86.25     57.64                                   
REMARK 500    TYR A 221      -61.45    -98.51                                   
REMARK 500    ASN A 248      102.19   -162.04                                   
REMARK 500    MET B 430       76.63   -110.70                                   
REMARK 500    MET B 430       78.08   -109.00                                   
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 B2016        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B2151        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH B2152        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH B2153        DISTANCE =  6.66 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1261  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   3   OD2                                                    
REMARK 620 2 ASP A   3   OD1  56.0                                              
REMARK 620 3 HIS A 211   ND1 112.5  86.9                                        
REMARK 620 4 ASP A 225   OD1  72.5 124.6  95.9                                  
REMARK 620 5 ASP A 225   OD2  87.7 134.6 135.7  51.5                            
REMARK 620 6 HOH A2220   O   137.3  97.8  97.1 136.1  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1260  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 184   OE2                                                    
REMARK 620 2 GLU A 184   OE1  44.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1262  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 222   OD2                                                    
REMARK 620 2 ASP A 222   OD1  49.9                                              
REMARK 620 3 GLU B 326   OE2  90.0 120.3                                        
REMARK 620 4 GLU B 326   OE1 122.2 166.0  45.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B1454  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 374   O                                                      
REMARK 620 2 CYS B 375   SG   92.5                                              
REMARK 620 3 HOH B2091   O    79.0 139.0                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IVY   RELATED DB: PDB                                   
REMARK 900 PHYSIOLOGICAL DIMER HPP PRECURSOR                                    
REMARK 900 RELATED ID: 4AZ0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CATHEPSIN A, COMPLEXED WITH 8A.                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 EXTRA C-TERMINAL GLU AS LEFTOVER FROM MYC-TAG                        
DBREF  4AZ3 A    1   298  UNP    P10619   PPGB_HUMAN      29    326             
DBREF  4AZ3 B  299   452  UNP    P10619   PPGB_HUMAN     327    480             
SEQADV 4AZ3 SER A   -1  UNP  P10619              EXPRESSION TAG                 
SEQADV 4AZ3 ARG A    0  UNP  P10619              EXPRESSION TAG                 
SEQADV 4AZ3 GLU B  453  UNP  P10619              EXPRESSION TAG                 
SEQRES   1 A  300  SER ARG ALA PRO ASP GLN ASP GLU ILE GLN ARG LEU PRO          
SEQRES   2 A  300  GLY LEU ALA LYS GLN PRO SER PHE ARG GLN TYR SER GLY          
SEQRES   3 A  300  TYR LEU LYS GLY SER GLY SER LYS HIS LEU HIS TYR TRP          
SEQRES   4 A  300  PHE VAL GLU SER GLN LYS ASP PRO GLU ASN SER PRO VAL          
SEQRES   5 A  300  VAL LEU TRP LEU ASN GLY GLY PRO GLY CYS SER SER LEU          
SEQRES   6 A  300  ASP GLY LEU LEU THR GLU HIS GLY PRO PHE LEU VAL GLN          
SEQRES   7 A  300  PRO ASP GLY VAL THR LEU GLU TYR ASN PRO TYR SER TRP          
SEQRES   8 A  300  ASN LEU ILE ALA ASN VAL LEU TYR LEU GLU SER PRO ALA          
SEQRES   9 A  300  GLY VAL GLY PHE SER TYR SER ASP ASP LYS PHE TYR ALA          
SEQRES  10 A  300  THR ASN ASP THR GLU VAL ALA GLN SER ASN PHE GLU ALA          
SEQRES  11 A  300  LEU GLN ASP PHE PHE ARG LEU PHE PRO GLU TYR LYS ASN          
SEQRES  12 A  300  ASN LYS LEU PHE LEU THR GLY GLU SER TYR ALA GLY ILE          
SEQRES  13 A  300  TYR ILE PRO THR LEU ALA VAL LEU VAL MET GLN ASP PRO          
SEQRES  14 A  300  SER MET ASN LEU GLN GLY LEU ALA VAL GLY ASN GLY LEU          
SEQRES  15 A  300  SER SER TYR GLU GLN ASN ASP ASN SER LEU VAL TYR PHE          
SEQRES  16 A  300  ALA TYR TYR HIS GLY LEU LEU GLY ASN ARG LEU TRP SER          
SEQRES  17 A  300  SER LEU GLN THR HIS CYS CYS SER GLN ASN LYS CYS ASN          
SEQRES  18 A  300  PHE TYR ASP ASN LYS ASP LEU GLU CYS VAL THR ASN LEU          
SEQRES  19 A  300  GLN GLU VAL ALA ARG ILE VAL GLY ASN SER GLY LEU ASN          
SEQRES  20 A  300  ILE TYR ASN LEU TYR ALA PRO CYS ALA GLY GLY VAL PRO          
SEQRES  21 A  300  SER HIS PHE ARG TYR GLU LYS ASP THR VAL VAL VAL GLN          
SEQRES  22 A  300  ASP LEU GLY ASN ILE PHE THR ARG LEU PRO LEU LYS ARG          
SEQRES  23 A  300  MET TRP HIS GLN ALA LEU LEU ARG SER GLY ASP LYS VAL          
SEQRES  24 A  300  ARG                                                          
SEQRES   1 B  155  MET ASP PRO PRO CYS THR ASN THR THR ALA ALA SER THR          
SEQRES   2 B  155  TYR LEU ASN ASN PRO TYR VAL ARG LYS ALA LEU ASN ILE          
SEQRES   3 B  155  PRO GLU GLN LEU PRO GLN TRP ASP MET CYS ASN PHE LEU          
SEQRES   4 B  155  VAL ASN LEU GLN TYR ARG ARG LEU TYR ARG SER MET ASN          
SEQRES   5 B  155  SER GLN TYR LEU LYS LEU LEU SER SER GLN LYS TYR GLN          
SEQRES   6 B  155  ILE LEU LEU TYR ASN GLY ASP VAL ASP MET ALA CYS ASN          
SEQRES   7 B  155  PHE MET GLY ASP GLU TRP PHE VAL ASP SER LEU ASN GLN          
SEQRES   8 B  155  LYS MET GLU VAL GLN ARG ARG PRO TRP LEU VAL LYS TYR          
SEQRES   9 B  155  GLY ASP SER GLY GLU GLN ILE ALA GLY PHE VAL LYS GLU          
SEQRES  10 B  155  PHE SER HIS ILE ALA PHE LEU THR ILE LYS GLY ALA GLY          
SEQRES  11 B  155  HIS MET VAL PRO THR ASP LYS PRO LEU ALA ALA PHE THR          
SEQRES  12 B  155  MET PHE SER ARG PHE LEU ASN LYS GLN PRO TYR GLU              
MODRES 4AZ3 ASN A  117  ASN  GLYCOSYLATION SITE                                 
MODRES 4AZ3 ASN B  305  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    S35  A1259      70                                                       
HET     CD  A1260       1                                                       
HET     CD  A1261       1                                                       
HET     CD  A1262       1                                                       
HET     CD  B1454       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     S35 (3S)-3-({[1-(2-FLUOROPHENYL)-5-{[(2R)-2-HYDROXY-3,3-             
HETNAM   2 S35  DIMETHYLBUTYL]OXY}-1H-PYRAZOL-3-YL]CARBONYL}AMINO)-3-           
HETNAM   3 S35  (2-METHYLPHENYL)PROPANOIC ACID                                  
HETNAM      CD CADMIUM ION                                                      
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  S35    C26 H30 F N3 O5                                              
FORMUL   6   CD    4(CD 2+)                                                     
FORMUL  10  HOH   *422(H2 O)                                                    
HELIX    1   1 PRO A    2  ASP A    5  5                                   4    
HELIX    2   2 SER A   62  THR A   68  1                                   7    
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  MET A  164  1                                  14    
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 B  306  ASN B  314  1                                   9    
HELIX   11  11 ASN B  315  LEU B  322  1                                   8    
HELIX   12  12 ASN B  335  TYR B  342  1                                   8    
HELIX   13  13 MET B  349  SER B  359  1                                  11    
HELIX   14  14 ASN B  376  LEU B  387  1                                  12    
HELIX   15  15 MET B  430  LYS B  435  1                                   6    
HELIX   16  16 LYS B  435  ASN B  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  BA10 ARG B 396  TYR B 402  0                                        
SHEET    2  BA10 GLY B 406  PHE B 416 -1  O  GLY B 406   N  TYR B 402           
SHEET    3  BA10 ILE B 419  ILE B 424 -1  O  ILE B 419   N  PHE B 416           
SHEET    4  BA10 GLN B 363  GLY B 369  1  O  ILE B 364   N  ALA B 420           
SHEET    5  BA10 LEU A 171  GLY A 177  1  O  GLN A 172   N  GLN B 363           
SHEET    6  BA10 LEU A 144  GLU A 149  1  O  LEU A 144   N  GLN A 172           
SHEET    7  BA10 VAL A  50  LEU A  54  1  O  VAL A  50   N  PHE A 145           
SHEET    8  BA10 ASN A  94  LEU A  98  1  O  ASN A  94   N  VAL A  51           
SHEET    9  BA10 LYS A  32  VAL A  39 -1  O  TRP A  37   N  TYR A  97           
SHEET   10  BA10 TYR A 108  SER A 109  1  O  TYR A 108   N  HIS A  33           
SHEET    1  BB10 ARG B 396  TYR B 402  0                                        
SHEET    2  BB10 GLY B 406  PHE B 416 -1  O  GLY B 406   N  TYR B 402           
SHEET    3  BB10 ILE B 419  ILE B 424 -1  O  ILE B 419   N  PHE B 416           
SHEET    4  BB10 GLN B 363  GLY B 369  1  O  ILE B 364   N  ALA B 420           
SHEET    5  BB10 LEU A 171  GLY A 177  1  O  GLN A 172   N  GLN B 363           
SHEET    6  BB10 LEU A 144  GLU A 149  1  O  LEU A 144   N  GLN A 172           
SHEET    7  BB10 VAL A  50  LEU A  54  1  O  VAL A  50   N  PHE A 145           
SHEET    8  BB10 ASN A  94  LEU A  98  1  O  ASN A  94   N  VAL A  51           
SHEET    9  BB10 LYS A  32  VAL A  39 -1  O  TRP A  37   N  TYR A  97           
SHEET   10  BB10 GLN A  21  LYS A  27 -1  O  TYR A  22   N  PHE A  38           
SHEET    1  AC 2 PHE A  73  VAL A  75  0                                        
SHEET    2  AC 2 LEU A  82  TYR A  84 -1  O  GLU A  83   N  LEU A  74           
SHEET    1  AD 2 CYS A 213  SER A 214  0                                        
SHEET    2  AD 2 LYS A 217  CYS A 218 -1  O  LYS A 217   N  SER A 214           
SSBOND   1 CYS A   60    CYS B  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 B  303                          1555   1555  2.03  
LINK         ND2 ASN A 117                 C1  NAG C   1     1555   1555  1.43  
LINK         ND2 ASN B 305                 C1  NAG D   1     1555   1555  1.43  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.43  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.42  
LINK         OD2 ASP A   3                CD    CD A1261     3455   1555  2.28  
LINK         OD1 ASP A   3                CD    CD A1261     3455   1555  2.43  
LINK         OE2 GLU A 184                CD    CD A1260     1555   1555  2.77  
LINK         OE1 GLU A 184                CD    CD A1260     1555   1555  3.01  
LINK         ND1 HIS A 211                CD    CD A1261     1555   1555  2.20  
LINK         OD2 ASP A 222                CD    CD A1262     1555   1555  2.76  
LINK         OD1 ASP A 222                CD    CD A1262     1555   1555  2.38  
LINK         OD1 ASP A 225                CD    CD A1261     1555   1555  2.70  
LINK         OD2 ASP A 225                CD    CD A1261     1555   1555  2.28  
LINK        CD    CD A1261                 O   HOH A2220     1555   1555  2.44  
LINK        CD    CD A1262                 OE2 GLU B 326     1555   4456  2.45  
LINK        CD    CD A1262                 OE1 GLU B 326     1555   4456  3.04  
LINK         O   ALA B 374                CD    CD B1454     1555   1555  2.78  
LINK         SG  CYS B 375                CD    CD B1454     1555   1555  1.99  
LINK        CD    CD B1454                 O   HOH B2091     1555   1555  2.37  
CISPEP   1 GLY A   57    PRO A   58          0        -3.03                     
CISPEP   2 SER A  100    PRO A  101          0        -1.28                     
CRYST1   90.590  102.800   48.390  90.00 101.87  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      0.011039  0.000000  0.002320        0.00000                         
SCALE2      0.000000  0.009728  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021117        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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