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Database: PDB
Entry: 1AMH
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HEADER    HYDROLASE                               17-JUN-97   1AMH              
TITLE     UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH             
TITLE    2 SER (D189S)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANIONIC TRYPSIN;                                           
COMPND   3 CHAIN: A, B;                                                         
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 ORGAN: PANCREAS;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: INVSC1;                                    
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETION;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: YEAST;                                     
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PYES2                                     
KEYWDS    SERINE PROTEASE, ACTIVATION DOMAIN, SUBSTRATE SPECIFICITY             
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SZABO,Z.S.BOCSKEI,G.NARAY-SZABO,L.GRAF                              
REVDAT   2   24-FEB-09 1AMH    1       VERSN                                    
REVDAT   1   24-DEC-97 1AMH    0                                                
JRNL        AUTH   E.SZABO,Z.BOCSKEI,G.NARAY-SZABO,L.GRAF                       
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE OF ASP189SER                 
JRNL        TITL 2 TRYPSIN PROVIDES EVIDENCE FOR AN INHERENT                    
JRNL        TITL 3 STRUCTURAL PLASTICITY OF THE PROTEASE.                       
JRNL        REF    EUR.J.BIOCHEM.                V. 263    20 1999              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   10429182                                                     
JRNL        DOI    10.1046/J.1432-1327.1999.00452.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.J.PERONA,L.HEDSTROM,R.L.WAGNER,W.J.RUTTER,                 
REMARK   1  AUTH 2 C.S.CRAIK,R.J.FLETTERICK                                     
REMARK   1  TITL   EXOGENOUS ACETATE RECONSTITUTES THE ENZYMATIC                
REMARK   1  TITL 2 ACTIVITY OF TRYPSIN ASP189SER                                
REMARK   1  REF    BIOCHEMISTRY                  V.  33  3252 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   L.GRAF,A.JANCSO,L.SZILAGYI,G.HEGYI,K.PINTER,                 
REMARK   1  AUTH 2 G.NARAY-SZABO,J.HEPP,K.MEDZIHRADSZKY,W.J.RUTTER              
REMARK   1  TITL   ELECTROSTATIC COMPLEMENTARITY WITHIN THE                     
REMARK   1  TITL 2 SUBSTRATE-BINDING POCKET OF TRYPSIN                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  85  4961 1988              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   R.HUBER,W.BODE                                               
REMARK   1  TITL   STRUCTURAL BASIS OF THE ACTIVATION AND ACTION OF             
REMARK   1  TITL 2 TRYPSIN                                                      
REMARK   1  REF    ACC.CHEM.RES.                 V.  11   114 1978              
REMARK   1  REFN                   ISSN 0001-4842                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13312                          
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 SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1183                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.54                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.59                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 470                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 38                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.050                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.44                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.37                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.17                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.894 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.015 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.959 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.106 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.1348; 20                   
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 1.871 ; 3                    
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.1983; 10                   
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 2.094 ; 3                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM.CA                                       
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOP.CA                                         
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AMH 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        : DEC-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 5.6                                
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                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BIOTEX                             
REMARK 200  DATA SCALING SOFTWARE          : BIOTEX                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13312                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : 0.13100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1BRB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZED AT 277 K FROM 10 MG/ML      
REMARK 280  PROTEIN SOLUTION USING 22% PEG 3350, 10 MM CACL2 AND 0.15M          
REMARK 280  NH4CL AS PRECIPITANT AT PH=5.6 (0.1 M SODIUM CITRATE).              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       24.89500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    MET A 180   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    MET B 104   CG  -  SD  -  CE  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG B 117   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    MET B 180   CG  -  SD  -  CE  ANGL. DEV. =   9.8 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    SER A  37       55.24   -141.21                                   
REMARK 500    ASP A  49       16.87    -67.14                                   
REMARK 500    GLN A  50        8.33   -161.73                                   
REMARK 500    ASN A 115     -148.15   -158.34                                   
REMARK 500    ASN A 150      113.87   -163.58                                   
REMARK 500    VAL A 213      103.24    -53.53                                   
REMARK 500    SER A 214      -72.07   -101.09                                   
REMARK 500    LEU A 221A      71.28   -108.61                                   
REMARK 500    ASP A 223       47.96    -86.44                                   
REMARK 500    SER B  37       59.87   -142.74                                   
REMARK 500    ASN B  48     -176.89   -172.72                                   
REMARK 500    ASN B  79       36.14    -97.67                                   
REMARK 500    ASN B 115     -144.69   -152.71                                   
REMARK 500    VAL B 199       77.71   -157.61                                   
REMARK 500    SER B 214      -78.19   -101.55                                   
REMARK 500    LEU B 221A      72.54   -119.62                                   
REMARK 500    ASP B 223       46.16    -78.91                                   
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 305        DISTANCE =  5.49 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 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE2                                                    
REMARK 620 2 GLU A  77   OE2 149.8                                              
REMARK 620 3 GLU A  80   OE2  90.8  82.2                                        
REMARK 620 4 ASN A  72   O   128.0  68.6 139.9                                  
REMARK 620 5 VAL A  75   O   133.4  74.2  78.9  67.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  70   OE2                                                    
REMARK 620 2 VAL B  75   O   135.1                                              
REMARK 620 3 GLU B  77   OE1 150.2  74.3                                        
REMARK 620 4 GLU B  80   OE2  90.9  80.6  89.4                                  
REMARK 620 5 ASN B  72   O   115.6  73.1  73.0 151.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE.                                    
REMARK 800 SITE_IDENTIFIER: CAB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
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 246                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 246                  
DBREF  1AMH A   16   245  UNP    P00763   TRY2_RAT        24    246             
DBREF  1AMH B   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1AMH SER A  189  UNP  P00763    ASP   194 ENGINEERED                     
SEQADV 1AMH SER B  189  UNP  P00763    ASP   194 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 SER 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                                                      
SEQRES   1 B  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 B  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 B  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 B  223  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 B  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 B  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 B  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 B  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 B  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  223  LYS SER SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 B  223  ALA ASN                                                      
HET     CA  A 246       1                                                       
HET     CA  B 246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *128(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 GLY A  219  LEU A  221A 5                                   4    
HELIX    4   4 VAL A  231  ASN A  233  5                                   3    
HELIX    5   5 VAL A  235  ALA A  243  1                                   9    
HELIX    6   6 ALA B   56  CYS B   58  5                                   3    
HELIX    7   7 GLN B  165  SER B  171  1                                   7    
HELIX    8   8 GLY B  219  LEU B  221A 5                                   4    
HELIX    9   9 VAL B  231  ASN B  233  5                                   3    
HELIX   10  10 VAL B  235  ALA B  243  1                                   9    
SHEET    1   A 7 GLN A  81  ASN A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  68 -1  N  LEU A  68   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 6 GLN A 156  PRO A 161  0                                        
SHEET    2   B 6 GLN A 135  GLY A 140 -1  N  GLY A 140   O  GLN A 156           
SHEET    3   B 6 PRO A 198  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    4   B 6 GLU A 204  TRP A 215 -1  N  GLY A 211   O  VAL A 199           
SHEET    5   B 6 GLY A 226  LYS A 230 -1  N  THR A 229   O  ILE A 212           
SHEET    6   B 6 MET A 180  VAL A 183 -1  N  VAL A 183   O  GLY A 226           
SHEET    1   C 4 GLN B  81  ASN B  84  0                                        
SHEET    2   C 4 GLN B  64  LEU B  68 -1  N  LEU B  68   O  GLN B  81           
SHEET    3   C 4 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    4   C 4 HIS B  40  SER B  45 -1  N  GLY B  44   O  VAL B  31           
SHEET    1   D 3 TRP B  51  SER B  54  0                                        
SHEET    2   D 3 MET B 104  LEU B 108 -1  N  ILE B 106   O  VAL B  52           
SHEET    3   D 3 ALA B  85  LYS B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   E 6 GLN B 156  PRO B 161  0                                        
SHEET    2   E 6 GLN B 135  GLY B 140 -1  N  GLY B 140   O  GLN B 156           
SHEET    3   E 6 PRO B 198  CYS B 201 -1  N  VAL B 200   O  LEU B 137           
SHEET    4   E 6 GLU B 204  TRP B 215 -1  N  GLY B 211   O  VAL B 199           
SHEET    5   E 6 GLY B 226  LYS B 230 -1  N  THR B 229   O  ILE B 212           
SHEET    6   E 6 MET B 180  VAL B 183 -1  N  VAL B 183   O  GLY B 226           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.15  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  1.75  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.01  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.06  
SSBOND   7 CYS B   22    CYS B  157                          1555   1555  1.99  
SSBOND   8 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   9 CYS B  128    CYS B  232                          1555   1555  2.20  
SSBOND  10 CYS B  136    CYS B  201                          1555   1555  2.04  
SSBOND  11 CYS B  168    CYS B  182                          1555   1555  2.27  
SSBOND  12 CYS B  191    CYS B  220                          1555   1555  2.01  
LINK        CA    CA A 246                 OE2 GLU A  70     1555   1555  2.54  
LINK        CA    CA A 246                 OE2 GLU A  77     1555   1555  2.51  
LINK        CA    CA A 246                 OE2 GLU A  80     1555   1555  2.48  
LINK        CA    CA A 246                 O   ASN A  72     1555   1555  2.57  
LINK        CA    CA A 246                 O   VAL A  75     1555   1555  2.49  
LINK        CA    CA B 246                 OE2 GLU B  70     1555   1555  2.50  
LINK        CA    CA B 246                 O   VAL B  75     1555   1555  2.45  
LINK        CA    CA B 246                 OE1 GLU B  77     1555   1555  2.52  
LINK        CA    CA B 246                 OE2 GLU B  80     1555   1555  2.50  
LINK        CA    CA B 246                 O   ASN B  72     1555   1555  2.47  
HYDBND       N   GLY A  148                 O   PHE B   41 1555    1555         
HYDBND       OG  SER A  147                 O   HIS B   57 1555    1555         
SLTBRG       N   ILE A  16                 OD2 ASP A 194   1555    1555         
SLTBRG       N   ILE B  16                 OD2 ASP B 194   1555    1555         
SITE     1 CAA  3 HIS A  57  ASP A 102  SER A 195                               
SITE     1 CAB  3 HIS B  57  ASP B 102  SER B 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  5 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 AC2  5 GLU B  80                                                     
CRYST1   45.920   49.790   89.880  90.00  97.34  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021777  0.000000  0.002805        0.00000                         
SCALE2      0.000000  0.020084  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011218        0.00000                         
MTRIX1   1  0.739109  0.012922 -0.673462       17.07460    1                    
MTRIX2   1  0.015672 -0.999875 -0.001986       21.64730    1                    
MTRIX3   1 -0.673404 -0.009087 -0.739219       44.75290    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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