GenomeNet

Database: PDB
Entry: 1ANC
LinkDB: 1ANC
Original site: 1ANC 
HEADER    SERINE PROTEASE                         21-DEC-94   1ANC              
TITLE     ANIONIC TRYPSIN MUTANT WITH SER 214 REPLACED BY LYS                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANIONIC TRYPSIN;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;                                  
SOURCE   3 ORGANISM_COMMON: BLACK RAT;                                          
SOURCE   4 ORGANISM_TAXID: 10117;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRYPSIN, ANIONIC, SERINE PROTEASE, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.FLETTERICK,M.E.MCGRATH                                            
REVDAT   3   24-FEB-09 1ANC    1       VERSN                                    
REVDAT   2   01-APR-03 1ANC    1       JRNL                                     
REVDAT   1   01-APR-97 1ANC    0                                                
JRNL        AUTH   M.E.MCGRATH,J.R.VASQUEZ,C.S.CRAIK,A.S.YANG,B.HONIG,          
JRNL        AUTH 2 R.J.FLETTERICK                                               
JRNL        TITL   PERTURBING THE POLAR ENVIRONMENT OF ASP102 IN                
JRNL        TITL 2 TRYPSIN: CONSEQUENCES OF REPLACING CONSERVED                 
JRNL        TITL 3 SER214.                                                      
JRNL        REF    BIOCHEMISTRY                  V.  31  3059 1992              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   1554694                                                      
JRNL        DOI    10.1021/BI00127A005                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
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            : 1668                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 159                                     
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) : 0.012 ; 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 1ANC 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        : 1990                               
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : 8.0                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : XENGEN                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17000                              
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) : 0.09100                            
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: DIFFERENCE FOURIER           
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   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0                                   
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: DIMERIC                           
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      124.38000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 C1   BEN A 384  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N1   BEN A   384     N2   BEN A   384     2565     0.11            
REMARK 500   C2   BEN A   384     C6   BEN A   384     2565     0.33            
REMARK 500   C3   BEN A   384     C5   BEN A   384     2565     0.44            
REMARK 500   C4   BEN A   384     C4   BEN A   384     2565     0.50            
REMARK 500   ND2  ASN A   143     O    HOH A   454     3556     0.62            
REMARK 500   C4   BEN A   384     C5   BEN A   384     2565     1.04            
REMARK 500   C1   BEN A   384     C6   BEN A   384     2565     1.19            
REMARK 500   C    BEN A   384     N1   BEN A   384     2565     1.23            
REMARK 500   O    HOH A   446     O    HOH A   446     4566     1.27            
REMARK 500   C3   BEN A   384     C6   BEN A   384     2565     1.33            
REMARK 500   C1   BEN A   384     C    BEN A   384     2565     1.41            
REMARK 500   C    BEN A   384     N2   BEN A   384     2565     1.41            
REMARK 500   C2   BEN A   384     C5   BEN A   384     2565     1.55            
REMARK 500   C1   BEN A   384     C2   BEN A   384     2565     1.59            
REMARK 500   O    HOH A   446     O    HOH A   487     4566     1.61            
REMARK 500   CG   ASN A   143     O    HOH A   454     3556     1.64            
REMARK 500   C3   BEN A   384     C4   BEN A   384     2565     1.82            
REMARK 500   O    HOH A   436     O    HOH A   436     3556     1.85            
REMARK 500   O    HOH A   473     O    HOH A   473     2565     1.96            
REMARK 500   C5   BEN A   384     C5   BEN A   384     2565     2.03            
REMARK 500   C6   BEN A   384     C6   BEN A   384     2565     2.09            
REMARK 500   N1   BEN A   384     N1   BEN A   384     2565     2.17            
REMARK 500   O    HOH A   446     O    HOH A   484     4566     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A  65A  NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  65A  NE  -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ILE A  73   CA  -  CB  -  CG2 ANGL. DEV. =  12.8 DEGREES          
REMARK 500    GLU A  77   OE1 -  CD  -  OE2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    GLU A  77   CG  -  CD  -  OE2 ANGL. DEV. = -15.8 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ASP A 102   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    THR A 120   N   -  CA  -  CB  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    GLU A 151   CA  -  CB  -  CG  ANGL. DEV. = -16.8 DEGREES          
REMARK 500    GLU A 151   OE1 -  CD  -  OE2 ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP A 178   CB  -  CG  -  OD1 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    LEU A 185   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    GLU A 186   CB  -  CA  -  C   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    GLU A 186   OE1 -  CD  -  OE2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP A 189   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    VAL A 199   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    VAL A 199   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TRP A 215   N   -  CA  -  CB  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    VAL A 227   CB  -  CA  -  C   ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 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    ASP A  49       -7.53    -57.32                                   
REMARK 500    HIS A  71      -75.82   -126.24                                   
REMARK 500    ASN A 115     -154.38   -158.60                                   
REMARK 500    LYS A 214      -71.67   -111.60                                   
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 454        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 504        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 508        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 289  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 VAL A  75   O   163.5                                              
REMARK 620 3 GLU A  80   OE2  98.4  93.6                                        
REMARK 620 4 HOH A 407   O    78.1  90.2  92.1                                  
REMARK 620 5 ASN A  72   O    88.5  80.4 172.1  93.1                            
REMARK 620 6 GLU A  77   OE1  98.4  92.9  89.6 176.3  85.6                      
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 CA A 289                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 290                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 384                 
DBREF  1ANC A   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1ANC LYS A  214  UNP  P00763    SER   215 ENGINEERED                     
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 ASP 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 LYS 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 289       1                                                       
HET    BEN  A 290       9                                                       
HET    BEN  A 384       9                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  BEN    2(C7 H8 N2)                                                  
FORMUL   5  HOH   *158(H2 O)                                                    
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 GLN A  165  SER A  171  1                                   7    
HELIX    3   3 VAL A  231  ASN A  233  5                                   3    
HELIX    4   4 VAL A  235  ALA A  243  1                                   9    
SHEET    1   A 7 GLN A  81  ASN A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  66 -1  N  LEU A  66   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 HIS A  40  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  85  LYS A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 2 GLN A 135  GLY A 140  0                                        
SHEET    2   B 2 GLN A 156  PRO A 161 -1  N  ALA A 160   O  CYS A 136           
SHEET    1   C 4 MET A 180  VAL A 183  0                                        
SHEET    2   C 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  VAL A 181           
SHEET    3   C 4 GLU A 204  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   C 4 PRO A 198  CYS A 201 -1  N  CYS A 201   O  GLU A 204           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  1.99  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.00  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  1.99  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.02  
LINK        CA    CA A 289                 OE1 GLU A  70     1555   1555  2.18  
LINK        CA    CA A 289                 O   VAL A  75     1555   1555  2.17  
LINK        CA    CA A 289                 OE2 GLU A  80     1555   1555  2.08  
LINK        CA    CA A 289                 O   HOH A 407     1555   1555  2.11  
LINK        CA    CA A 289                 O   ASN A  72     1555   1555  2.28  
LINK        CA    CA A 289                 OE1 GLU A  77     1555   1555  2.50  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  6 GLU A  80  HOH A 407                                          
SITE     1 AC2  9 ASP A 189  SER A 190  CYS A 191  GLN A 192                    
SITE     2 AC2  9 TRP A 215  GLY A 216  GLY A 219  GLY A 226                    
SITE     3 AC2  9 HOH A 388                                                     
SITE     1 AC3  5 SER A 146  ALA A 221  LEU A 221A PRO A 222                    
SITE     2 AC3  5 HOH A 436                                                     
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                                                                             
DBGET integrated database retrieval system