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Database: PDB
Entry: 1IAU
LinkDB: 1IAU
Original site: 1IAU 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           23-MAR-01   1IAU              
TITLE     HUMAN GRANZYME B IN COMPLEX WITH AC-IEPD-CHO                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GRANZYME B;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.79;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ACETYL-ISOLEUCYL-GLUTAMYL-PROLYL-ASPARTYL-ALDEHYDE PEPTIDE 
COMPND   8 INHIBITOR;                                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: ACE-ILE-GLU-PRO-ASP-CHO;                                    
COMPND  11 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: 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 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.               
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ROTONDA,M.GARCIA-CALVO,H.G.BULL,W.M.GEISSLER,B.M.MCKEEVER,          
AUTHOR   2 C.A.WILLOUGHBY,N.A.THORNBERRY,J.W.BECKER                             
REVDAT   4   04-APR-12 1IAU    1       HET    HETATM HETNAM LINK                
REVDAT   4 2                   1       REMARK SEQRES                            
REVDAT   3   13-JUL-11 1IAU    1       VERSN                                    
REVDAT   2   24-FEB-09 1IAU    1       VERSN                                    
REVDAT   1   02-MAY-01 1IAU    0                                                
JRNL        AUTH   J.ROTONDA,M.GARCIA-CALVO,H.G.BULL,W.M.GEISSLER,B.M.MCKEEVER, 
JRNL        AUTH 2 C.A.WILLOUGHBY,N.A.THORNBERRY,J.W.BECKER                     
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE OF HUMAN GRANZYME B COMPARED 
JRNL        TITL 2 TO CASPASE-3, KEY MEDIATORS OF CELL DEATH WITH CLEAVAGE      
JRNL        TITL 3 SPECIFICITY FOR ASPARTIC ACID IN P1.                         
JRNL        REF    CHEM.BIOL.                    V.   8   357 2001              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   11325591                                                     
JRNL        DOI    10.1016/S1074-5521(01)00018-7                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19942                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 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       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2340                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 1815                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 93                                      
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.03                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUE 245 IS MISSING IN THE ELECTRON    
REMARK   3  DENSITY. SHELX WAS ALSO USED FOR THE FINAL REFINEMENT TO MODEL      
REMARK   3  DISORDER.                                                           
REMARK   4                                                                      
REMARK   4 1IAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013107.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NON-FOCUSING                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19956                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.67                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: CATHEPSIN G (PDB ENTRY 1CGH)                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 UL DROPS OF PROTEIN-INHIBITOR        
REMARK 280  SOLUTION (12.2 MG/ML IN 20 MM TRIS-HCL PH 8.0, 200 MM NACL) WERE    
REMARK 280  MIXED WITH AN EQUAL VOLUME OF PRECIPITANT SOLUTION (25% PEG         
REMARK 280  MONOMETHYLETHER-550 (V/V), 0.10 M MES PH 6.5, 10 MM ZNSO(4), 12     
REMARK 280  MM ZNCL(2)) AND INCUBATED AT ROOM TEMPERATURE OVER A RESERVOIR OF   
REMARK 280  24% W/V PEG-3350, 12.8% V/V PEG MME-550, 50 MM MES PH 6.5, 5 MM     
REMARK 280  ZNSO(4), AND 6 MM ZNCL(2).                                          
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       24.43650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.13050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.54050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.13050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.43650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.54050            
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: 3470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THERE IS A COVALENT BOND BETWEEN ATOM OG OF SER195A AND ATOM C OF    
REMARK 400 ASJ405B, FORMING A HEMIACETAL                                        
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     TYR A   245                                                      
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    LYS A  37     -123.38    -75.63                                   
REMARK 500    THR A  54     -164.21   -162.43                                   
REMARK 500    HIS A  71      -65.49   -126.61                                   
REMARK 500    PHE A  99       17.15     58.81                                   
REMARK 500    PRO A 145A       1.62    -59.35                                   
REMARK 500    LEU A 146       -5.65   -152.79                                   
REMARK 500    HIS A 151      176.41    -55.87                                   
REMARK 500    HIS A 173      -21.79     84.70                                   
REMARK 500    LYS A 203       16.73     59.10                                   
REMARK 500    SER A 214      -68.92   -125.64                                   
REMARK 500    ASN A 218        5.68    -67.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 649   O                                                      
REMARK 620 2 ASP A 184   OD1  84.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  20   NE2                                                    
REMARK 620 2 HOH A 655   O   137.3                                              
REMARK 620 3 GLU A 157   OE2 105.2  91.2                                        
REMARK 620 4 HOH A 653   O   104.9 111.7  97.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 169   OE2                                                    
REMARK 620 2 GLU A 169   OE1  57.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 153   NE2                                                    
REMARK 620 2 HIS A 151   NE2 118.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  25   NE2                                                    
REMARK 620 2 HOH A 605   O    93.9                                              
REMARK 620 3 GLU A  77   OE2 122.9 106.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF ACETYL-ISOLEUCYL-      
REMARK 800  GLUTAMYL-PROLYL-ASPARTYL-ALDEHYDE PEPTIDE                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800  RESIDUES 301 TO 307                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FQ3   RELATED DB: PDB                                   
REMARK 900 HUMAN GRANZYME B (UNINHIBITED)                                       
REMARK 900 RELATED ID: 1FI8   RELATED DB: PDB                                   
REMARK 900 RAT GRANZYME B WITH ECOTIN FRAGMENT                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE RESIDUE NUMBERS FOR CHAIN A ARE NOT SEQUENTIAL. THE NUMBERING    
REMARK 999 SCHEME IS BASED ON THE FAMILY OF SERINE PROTEASES AND IS BASED ON    
REMARK 999 THE ZYMOGEN CHYMOTRYPSINOGEN                                         
DBREF  1IAU A   16   245  UNP    P10144   GRAB_HUMAN      21    247             
DBREF  1IAU B  401   405  PDB    1IAU     1IAU           401    405             
SEQADV 1IAU ARG A   48  UNP  P10144    GLN    55 VARIANT                        
SEQRES   1 A  227  ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO          
SEQRES   2 A  227  TYR MET ALA TYR LEU MET ILE TRP ASP GLN LYS SER LEU          
SEQRES   3 A  227  LYS ARG CYS GLY GLY PHE LEU ILE ARG ASP ASP PHE VAL          
SEQRES   4 A  227  LEU THR ALA ALA HIS CYS TRP GLY SER SER ILE ASN VAL          
SEQRES   5 A  227  THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU PRO THR          
SEQRES   6 A  227  GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO          
SEQRES   7 A  227  ALA TYR ASN PRO LYS ASN PHE SER ASN ASP ILE MET LEU          
SEQRES   8 A  227  LEU GLN LEU GLU ARG LYS ALA LYS ARG THR ARG ALA VAL          
SEQRES   9 A  227  GLN PRO LEU ARG LEU PRO SER ASN LYS ALA GLN VAL LYS          
SEQRES  10 A  227  PRO GLY GLN THR CYS SER VAL ALA GLY TRP GLY GLN THR          
SEQRES  11 A  227  ALA PRO LEU GLY LYS HIS SER HIS THR LEU GLN GLU VAL          
SEQRES  12 A  227  LYS MET THR VAL GLN GLU ASP ARG LYS CYS GLU SER ASP          
SEQRES  13 A  227  LEU ARG HIS TYR TYR ASP SER THR ILE GLU LEU CYS VAL          
SEQRES  14 A  227  GLY ASP PRO GLU ILE LYS LYS THR SER PHE LYS GLY ASP          
SEQRES  15 A  227  SER GLY GLY PRO LEU VAL CYS ASN LYS VAL ALA GLN GLY          
SEQRES  16 A  227  ILE VAL SER TYR GLY ARG ASN ASN GLY MET PRO PRO ARG          
SEQRES  17 A  227  ALA CYS THR LYS VAL SER SER PHE VAL HIS TRP ILE LYS          
SEQRES  18 A  227  LYS THR MET LYS ARG TYR                                      
SEQRES   1 B    5  ACE ILE GLU PRO ASJ                                          
MODRES 1IAU ASN A   65  ASN  GLYCOSYLATION SITE                                 
MODRES 1IAU ASN A   98  ASN  GLYCOSYLATION SITE                                 
HET    ACE  B 401       3                                                       
HET    ASJ  B 405      16                                                       
HET    NAG  A 301      14                                                       
HET    NAG  A 302      14                                                       
HET    FUC  A 303      10                                                       
HET    NAG  A 304      14                                                       
HET    MAN  A 305      11                                                       
HET    NAG  A 306      14                                                       
HET    BMA  A 307      11                                                       
HET     ZN  A 501       1                                                       
HET     ZN  A 502       1                                                       
HET     ZN  A 503       1                                                       
HET     ZN  A 504       1                                                       
HET     ZN  A 505       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     ASJ (3S)-3-AMINO-4-HYDROXYBUTANOIC ACID                              
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      ZN ZINC ION                                                         
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  ASJ    C4 H9 N O3                                                   
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4  FUC    C6 H12 O5                                                    
FORMUL   4  MAN    C6 H12 O6                                                    
FORMUL   4  BMA    C6 H12 O6                                                    
FORMUL   5   ZN    5(ZN 2+)                                                     
FORMUL  10  HOH   *58(H2 O)                                                     
HELIX    1   1 ALA A   55  TRP A   59  5                                   5    
HELIX    2   2 GLU A  164  LEU A  172  1                                   9    
HELIX    3   3 PHE A  234  ARG A  244  1                                  11    
SHEET    1   A 7 HIS A  20  GLU A  21  0                                        
SHEET    2   A 7 GLN A 156  THR A 161 -1  O  GLU A 157   N  HIS A  20           
SHEET    3   A 7 THR A 135  GLY A 140 -1  N  CYS A 136   O  MET A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  PRO A 198   N  ALA A 139           
SHEET    5   A 7 VAL A 204  TYR A 215 -1  O  VAL A 204   N  CYS A 201           
SHEET    6   A 7 ARG A 226  LYS A 230 -1  N  ALA A 227   O  TYR A 215           
SHEET    7   A 7 GLU A 180  VAL A 183 -1  O  LEU A 181   N  CYS A 228           
SHEET    1   B 7 MET A  30  TRP A  36  0                                        
SHEET    2   B 7 LEU A  39  ARG A  48 -1  N  LYS A  40   O  ILE A  35           
SHEET    3   B 7 PHE A  51  THR A  54 -1  N  PHE A  51   O  ARG A  48           
SHEET    4   B 7 MET A 104  LEU A 108 -1  N  MET A 104   O  THR A  54           
SHEET    5   B 7 GLN A  81  PRO A  90 -1  N  LYS A  86   O  GLN A 107           
SHEET    6   B 7 SER A  63  LEU A  68 -1  O  ILE A  64   N  VAL A  85           
SHEET    7   B 7 MET A  30  TRP A  36 -1  N  TYR A  32   O  THR A  67           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.05  
SSBOND   2 CYS A  136    CYS A  201                          1555   1555  2.02  
SSBOND   3 CYS A  168    CYS A  182                          1555   1555  2.04  
LINK         C   ACE B 401                 N   ILE B 402     1555   1555  1.33  
LINK         C   PRO B 404                 N  AASJ B 405     1555   1555  1.33  
LINK         C   PRO B 404                 N  BASJ B 405     1555   1555  1.33  
LINK         O4  NAG A 302                 C1  NAG A 304     1555   1555  1.39  
LINK         O4  NAG A 304                 C1  MAN A 305     1555   1555  1.39  
LINK         O6  NAG A 302                 C1  FUC A 303     1555   1555  1.39  
LINK         O4  MAN A 305                 C1  NAG A 306     1555   1555  1.40  
LINK         O6  MAN A 305                 C1  BMA A 307     1555   1555  1.40  
LINK         ND2 ASN A  65                 C1  NAG A 301     1555   1555  1.44  
LINK         ND2 ASN A  98                 C1  NAG A 302     1555   1555  1.47  
LINK        ZN    ZN A 505                 O   HOH A 649     1555   1555  1.70  
LINK         NE2 HIS A  20                ZN    ZN A 504     1555   1555  1.78  
LINK         OE2 GLU A 169                ZN    ZN A 503     1555   1555  1.85  
LINK         NE2 HIS A 153                ZN    ZN A 501     1555   1555  1.89  
LINK         NE2 HIS A  25                ZN    ZN A 502     1555   1555  2.05  
LINK        ZN    ZN A 502                 O   HOH A 605     1555   1555  2.07  
LINK        ZN    ZN A 504                 O   HOH A 655     1555   1555  2.09  
LINK         OE2 GLU A  77                ZN    ZN A 502     1555   1555  2.12  
LINK         OE2 GLU A 157                ZN    ZN A 504     1555   1555  2.22  
LINK         OD1 ASP A 184                ZN    ZN A 505     1555   1555  2.33  
LINK         NE2 HIS A 151                ZN    ZN A 501     1555   1555  2.39  
LINK        ZN    ZN A 504                 O   HOH A 653     1555   1555  2.55  
LINK         OE1 GLU A 169                ZN    ZN A 503     1555   1555  2.56  
LINK         OG ASER A 195                 C  AASJ B 405     1555   1555  1.47  
LINK         OG BSER A 195                 C  BASJ B 405     1555   1555  1.48  
CISPEP   1 PRO A  224    PRO A  225          0         2.81                     
SITE     1 AC1  3 MET A  34  SER A  63  ASN A  65                               
SITE     1 AC2  7 ARG A  48  ASP A  50  GLN A 107  ARG A 166                    
SITE     2 AC2  7 MET A 242  ARG A 244  MAN A 305                               
SITE     1 AC3  2 HIS A 151  HIS A 153                                          
SITE     1 AC4  4 HIS A  25  GLU A  77  HIS A 173  HOH A 605                    
SITE     1 AC5  3 GLU A 169  HIS A 236  LYS A 240                               
SITE     1 AC6  4 HIS A  20  GLU A 157  HOH A 653  HOH A 655                    
SITE     1 AC7  4 GLU A 109  ASP A 184  GLU A 186  HOH A 649                    
SITE     1 AC8 17 HIS A  57  PHE A  99  LEU A 172  TYR A 174                    
SITE     2 AC8 17 PHE A 191  LYS A 192  GLY A 193  ASP A 194                    
SITE     3 AC8 17 SER A 195  SER A 214  TYR A 215  GLY A 216                    
SITE     4 AC8 17 ARG A 217  ASN A 218  ARG A 226  HOH B 601                    
SITE     5 AC8 17 HOH B 622                                                     
SITE     1 AC9 11 GLU A  21  ASN A  95  ASN A  98  SER A 100                    
SITE     2 AC9 11 LYS A 111  LYS A 148  HIS A 173  TYR A 174                    
SITE     3 AC9 11 LYS A 243  BMA A 307  HOH A 637                               
CRYST1   48.873   75.081   80.261  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      0.020461  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012459        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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