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Database: PDB
Entry: 2TRM
LinkDB: 2TRM
Original site: 2TRM 
HEADER    HYDROLASE (SERINE PROTEINASE)           25-APR-88   2TRM              
TITLE     THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF                   
TITLE    2 TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116                                                
KEYWDS    HYDROLASE (SERINE PROTEINASE)                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.STROUD,J.FINER-MOORE                                              
REVDAT   3   24-FEB-09 2TRM    1       VERSN                                    
REVDAT   2   01-APR-03 2TRM    1       JRNL                                     
REVDAT   1   16-JUL-88 2TRM    0                                                
JRNL        AUTH   S.SPRANG,T.STANDING,R.J.FLETTERICK,R.M.STROUD,               
JRNL        AUTH 2 J.FINER-MOORE,N.H.XUONG,R.HAMLIN,W.J.RUTTER,                 
JRNL        AUTH 3 C.S.CRAIK                                                    
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT             
JRNL        TITL 2 OF TRYPSIN: ROLE OF ASP102 IN SERINE PROTEASE                
JRNL        TITL 3 CATALYSIS.                                                   
JRNL        REF    SCIENCE                       V. 237   905 1987              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   3112942                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.S.CRAIK,S.ROCZNIAK,C.LARGMAN,W.J.RUTTER                    
REMARK   1  TITL   THE CATALYTIC ROLE OF THE ACTIVE SITE ASPARTIC               
REMARK   1  TITL 2 ACID IN SERINE PROTEASES                                     
REMARK   1  REF    SCIENCE                       V. 237   909 1987              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 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   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1666                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 122                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2TRM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS:  THE CRYSTALS WERE GROWN AT PH 8         
REMARK 280  WHICH IS WITHIN THE PH RANGE (7 - 9) WHERE NATIVE TRYPSIN IS        
REMARK 280  OPTIMALLY ACTIVE.                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       62.19000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       62.19000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       62.19000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       62.19000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       62.19000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       62.19000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE CATALYTIC SITE, DIFFERS FROM THE CATALYTIC SITE OF NATIVE        
REMARK 400 TRYPSIN BY REPLACEMENT OF ASP 102 WITH AN ASN. IN THE MUTANT,        
REMARK 400 ND2 ASN 102 IS A HYDROGEN BOND DONOR TO ND1 HIS 57. THIS             
REMARK 400 HYDROGEN ARRANGEMENT PREVENTS HIS 57 FROM ACCEPTING A HYDROGEN       
REMARK 400 BOND FROM SER 195 AND RESULTS IN A LOSS OF NUCLEOPHILICITY OF        
REMARK 400 SER 195. THE MUTANT IS FOUR ORDERS OF MAGNITUDE LESS ACTIVE THAN     
REMARK 400 NATIVE RAT TRYPSIN.                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A  53   CA  -  CB  -  CG1 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A  65A  NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ALA A  86   CB  -  CA  -  C   ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A  96   CD  -  NE  -  CZ  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASN A 115   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG A 117   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    THR A 120   N   -  CA  -  CB  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    GLY A 148   N   -  CA  -  C   ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ASP A 153   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    GLN A 156   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    CYS A 182   N   -  CA  -  CB  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    CYS A 182   CA  -  CB  -  SG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    LEU A 185   CB  -  CA  -  C   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    SER A 190   CB  -  CA  -  C   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    VAL A 199   CB  -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    TYR A 217   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP A 240   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  50        0.00   -161.30                                   
REMARK 500    HIS A  71      -72.90   -143.74                                   
REMARK 500    LEU A  99        7.13     58.98                                   
REMARK 500    SER A 109        6.73    -68.85                                   
REMARK 500    SER A 110      138.06    170.03                                   
REMARK 500    ASN A 115     -137.58   -144.08                                   
REMARK 500    SER A 146       -9.98    -49.05                                   
REMARK 500    SER A 147      114.28   -171.69                                   
REMARK 500    ASN A 150      119.06   -168.62                                   
REMARK 500    ALA A 160      148.02   -176.80                                   
REMARK 500    LYS A 175       12.73   -147.71                                   
REMARK 500    THR A 177     -170.52    -69.00                                   
REMARK 500    SER A 214      -64.26   -106.83                                   
REMARK 500    TRP A 215     -173.01   -170.88                                   
REMARK 500    CYS A 220      106.14   -165.01                                   
REMARK 500    GLN A 239      -76.65    -41.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 117         0.17    SIDE_CHAIN                              
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 A 330        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 343        DISTANCE =  5.23 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 247  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 VAL A  75   O   158.8                                              
REMARK 620 3 GLU A  77   OE1  87.2  78.6                                        
REMARK 620 4 GLU A  80   OE2  85.9 108.3  85.5                                  
REMARK 620 5 ASN A  72   O    73.1  86.9  67.7 146.3                            
REMARK 620 6 GLU A  70   OE2  41.3 148.8 128.4  91.1  90.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE                                     
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 247                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 246                 
DBREF  2TRM A   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 2TRM ASN A  102  UNP  P00763    ASP   107 CONFLICT                       
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 A  223  LYS THR LEU ASN ASN ASN ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 A  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 A  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 A  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 A  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
HET     CA  A 247       1                                                       
HET    BEN  A 246       9                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  BEN    C7 H8 N2                                                     
FORMUL   4  HOH   *122(H2 O)                                                    
HELIX    1 SHO PRO A  164  TYR A  172  1IRREGULAR AFTER CYS 168            9    
HELIX    2 310 LYS A  230  VAL A  235  5LEADS INTO TERMINAL ALPHA-HLX      6    
HELIX    3 TER TYR A  234  ASN A  245  1C-TERMINAL HELIX                  12    
SHEET    1 SH1 7 TYR A  20  TYR A  20  0                                        
SHEET    2 SH1 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3 SH1 7 CYS A 136  GLY A 140 -1  O  CYS A 136   N  ALA A 160           
SHEET    4 SH1 7 GLY A 197  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    5 SH1 7 GLU A 204  TRP A 215 -1  N  VAL A 213   O  GLY A 197           
SHEET    6 SH1 7 GLY A 226  VAL A 231 -1  N  VAL A 227   O  TRP A 215           
SHEET    7 SH1 7 ASN A 179  VAL A 183 -1  N  VAL A 183   O  GLY A 226           
SHEET    1 SH2 4 GLY A  43  SER A  45  0                                        
SHEET    2 SH2 4 VAL A  52  ALA A  55 -1  N  VAL A  53   O  SER A  45           
SHEET    3 SH2 4 ILE A 103  LYS A 107 -1  O  MET A 104   N  SER A  54           
SHEET    4 SH2 4 LYS A  87  HIS A  91 -1  N  HIS A  91   O  ILE A 103           
SHEET    1 SH3 2 ILE A  63  LEU A  66  0                                        
SHEET    2 SH3 2 GLN A  81  ALA A  85 -1  N  GLN A  81   O  LEU A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  1.97  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.02  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.01  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.05  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.02  
LINK        CA    CA A 247                 OE1 GLU A  70     1555   1555  2.02  
LINK        CA    CA A 247                 O   VAL A  75     1555   1555  2.68  
LINK        CA    CA A 247                 OE1 GLU A  77     1555   1555  2.78  
LINK        CA    CA A 247                 OE2 GLU A  80     1555   1555  1.91  
LINK        CA    CA A 247                 O   ASN A  72     1555   1555  2.68  
LINK        CA    CA A 247                 OE2 GLU A  70     1555   1555  3.27  
SITE     1 CAT  3 HIS A  57  ASN A 102  SER A 195                               
SITE     1 AC1  5 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  5 GLU A  80                                                     
SITE     1 AC2  9 ASP A 189  SER A 190  CYS A 191  GLN A 192                    
SITE     2 AC2  9 SER A 195  TRP A 215  GLY A 216  GLY A 219                    
SITE     3 AC2  9 GLY A 226                                                     
CRYST1  124.380  124.380  124.380  90.00  90.00  90.00 I 2 3        24          
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      0.008040  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008040  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008040        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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