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Database: PDB
Entry: 1UHB
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Original site: 1UHB 
HEADER    HYDROLASE                               27-JUN-03   1UHB              
TITLE     CRYSTAL STRUCTURE OF PORCINE ALPHA TRYPSIN BOUND WITH AUTO            
TITLE    2 CATALYTICALY PRODUCED NATIVE PEPTIDE AT 2.15 A RESOLUTION            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TRYPSIN;                                                   
COMPND   7 CHAIN: B;                                                            
COMPND   8 EC: 3.4.21.4;                                                        
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: 9-MER PEPTIDE FROM TRYPSIN;                                
COMPND  11 CHAIN: P;                                                            
COMPND  12 EC: 3.4.21.4                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   7 ORGANISM_COMMON: PIG;                                                
SOURCE   8 ORGANISM_TAXID: 9823;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  11 ORGANISM_COMMON: PIG;                                                
SOURCE  12 ORGANISM_TAXID: 9823;                                                
SOURCE  13 OTHER_DETAILS: IT IS AN OLIGOPEPTIDE FRAGMENT FROM NATIVE            
SOURCE  14 TRYPSIN BY AUTO CATALYSIS OF TRYPSIN PRODUCED DURING                 
SOURCE  15 PREPARATION OF TRYPSIN.                                              
KEYWDS    SERINE PROTEASE, HYDROLASE, PEPTIDE TRYPSIN COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.PATTABHI,B.SYED IBRAHIM,N.SHAMALADEVI                               
REVDAT   2   24-FEB-09 1UHB    1       VERSN                                    
REVDAT   1   27-JUL-04 1UHB    0                                                
JRNL        AUTH   V.PATTABHI,B.SYED IBRAHIM,N.SHAMALADEVI                      
JRNL        TITL   TRYPSIN ACTIVITY REDUCED BY AN AUTOCATALYTICALLY             
JRNL        TITL 2 PRODUCED NONAPEPTIDE                                         
JRNL        REF    J.BIOMOL.STRUCT.DYN.          V.  21   737 2004              
JRNL        REFN                   ISSN 0739-1102                               
JRNL        PMID   15106996                                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.JOHNSON,N.GAUTHAM,V.PATTABHI                               
REMARK   1  TITL   CRYSTAL STRUCTURE AT 1.63 A RESOLUTION OF THE                
REMARK   1  TITL 2 NATIVE FORM OF PORCINE BETA-TRYPSIN: REVEALING AN            
REMARK   1  TITL 3 ACETATE ION BINDING SITE AND FUNCTIONAL WATER                
REMARK   1  TITL 4 NETWORK                                                      
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1435     7 1999              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1  PMID   10561533                                                     
REMARK   1  DOI    10.1016/S0167-4838(99)00202-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 9425                           
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 467                             
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 637                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 487                          
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1704                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.61000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 1.24000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.378         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.236         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.915         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1727 ; 0.040 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1496 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2342 ; 2.597 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3513 ; 1.474 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   226 ; 4.676 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   293 ;19.016 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   264 ; 0.181 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1943 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   313 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   460 ; 0.391 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1612 ; 0.256 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     1 ; 0.022 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   197 ; 0.747 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.010 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    61 ; 0.496 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    92 ; 0.549 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.234 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1134 ; 2.137 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1809 ; 3.316 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   593 ; 5.242 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   533 ; 7.358 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UHB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005825.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 6.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR, DENZO                         
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9847                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14000                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB CODE 1QQU                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULPHATE, PH 6.70,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
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       23.47250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.62250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.96050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.62250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.47250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.96050            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P                               
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 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    SER A  37       54.32   -143.66                                   
REMARK 500    HIS A  71      -57.97   -143.64                                   
REMARK 500    ILE A  73        2.53    -64.51                                   
REMARK 500    ASN A 115     -152.94   -153.94                                   
REMARK 500    SER B 214      -67.82   -120.27                                   
REMARK 500    ASP P   3     -149.74   -106.06                                   
REMARK 500    CYS P   5      -68.05   -173.76                                   
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 B 276        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH B 286        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A 328        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 336        DISTANCE =  5.39 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                              CA A 256  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE1                                                    
REMARK 620 2 VAL A  75   O    91.3                                              
REMARK 620 3 HOH A 257   O    97.7  86.4                                        
REMARK 620 4 GLU A  77   OE1  76.8 102.5 169.5                                  
REMARK 620 5 GLU A  70   OE1 104.2 158.2  76.4  96.1                            
REMARK 620 6 ASN A  72   O   167.1  77.7  88.4  98.9  88.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT P 390                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 256                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QQU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE AT 1.63 A RESOLUTION OF THE NATIVE FORM            
REMARK 900 OF PORCINE BETA-TRYPSIN: REVEALING AN ACETATE ION BINDING            
REMARK 900 SITE AND FUNCTIONAL WATER                                            
DBREF  1UHB A   16   145  UNP    P00761   TRYP_PIG         9    133             
DBREF  1UHB B  146   245  UNP    P00761   TRYP_PIG       134    231             
DBREF  1UHB P    1     9  UNP    P00761   TRYP_PIG       177    185             
SEQRES   1 A  125  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  125  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  125  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  125  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  125  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  125  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  125  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  125  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  125  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  125  ILE SER GLY TRP GLY ASN THR LYS                              
SEQRES   1 B   98  SER SER GLY SER SER TYR PRO SER LEU LEU GLN CYS LEU          
SEQRES   2 B   98  LYS ALA PRO VAL LEU SER ASP SER SER CYS LYS SER SER          
SEQRES   3 B   98  TYR PRO GLY GLN ILE THR GLY ASN MET ILE CYS VAL GLY          
SEQRES   4 B   98  PHE LEU GLU GLY GLY LYS ASP SER CYS GLN GLY ASP SER          
SEQRES   5 B   98  GLY GLY PRO VAL VAL CYS ASN GLY GLN LEU GLN GLY ILE          
SEQRES   6 B   98  VAL SER TRP GLY TYR GLY CYS ALA GLN LYS ASN LYS PRO          
SEQRES   7 B   98  GLY VAL TYR THR LYS VAL CYS ASN TYR VAL ASN TRP ILE          
SEQRES   8 B   98  GLN GLN THR ILE ALA ALA ASN                                  
SEQRES   1 P    9  GLY LYS ASP SER CYS GLN GLY ASP SER                          
HET    ACT  P 390       4                                                       
HET     CA  A 256       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *147(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER B  164  TYR B  172  1                                   9    
HELIX    3   3 TYR B  234  ALA B  244  1                                  11    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN B 156  PRO B 161 -1  O  CYS B 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  ILE A 138   O  LEU B 158           
SHEET    4   A 7 PRO B 198  CYS B 201 -1  O  VAL B 200   N  LEU A 137           
SHEET    5   A 7 GLN B 204  TRP B 215 -1  O  GLN B 204   N  CYS B 201           
SHEET    6   A 7 GLY B 226  LYS B 230 -1  O  VAL B 227   N  TRP B 215           
SHEET    7   A 7 MET B 180  VAL B 183 -1  N  ILE B 181   O  TYR B 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  LEU A  46 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  MET A 104   N  SER A  54           
SHEET    5   B 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  VAL A  65   O  ILE A  83           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SSBOND   1 CYS A   22    CYS B  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS B  232                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS B  201                          1555   1555  2.03  
SSBOND   5 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND   6 CYS B  191    CYS B  220                          1555   1555  2.03  
LINK        CA    CA A 256                 OE1 GLU A  80     1555   1555  2.65  
LINK        CA    CA A 256                 O   VAL A  75     1555   1555  2.58  
LINK        CA    CA A 256                 O   HOH A 257     1555   1555  2.74  
LINK        CA    CA A 256                 OE1 GLU A  77     1555   1555  2.73  
LINK        CA    CA A 256                 OE1 GLU A  70     1555   1555  2.55  
LINK        CA    CA A 256                 O   ASN A  72     1555   1555  2.66  
SITE     1 AC1 10 LYS A  60  ALA A 129  ALA A 130  ALA A 132                    
SITE     2 AC1 10 HOH A 288  VAL B 162  LEU B 163  SER B 164                    
SITE     3 AC1 10 ASP B 165  ASP P   8                                          
SITE     1 AC2  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC2  6 GLU A  80  HOH A 257                                          
CRYST1   46.945   53.921   77.245  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      0.021302  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012946        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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