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Database: PDB
Entry: 1LVM
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Original site: 1LVM 
HEADER    VIRAL PROTEIN                           28-MAY-02   1LVM              
TITLE     CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED            
TITLE    2 WITH PRODUCT                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION                  
COMPND   3 PROTEIN A (NIA);                                                     
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: RESIDUES 1-221;                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE;                   
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 302-310;                                          
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION                  
COMPND  15 PROTEIN A (NIA);                                                     
COMPND  16 CHAIN: E;                                                            
COMPND  17 FRAGMENT: RESIDUES 230-236;                                          
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TOBACCO ETCH VIRUS;                             
SOURCE   3 ORGANISM_TAXID: 12227;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: PRK529;                                    
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: BL21(DE3);                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: TOBACCO ETCH VIRUS;                             
SOURCE  11 ORGANISM_TAXID: 12227;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: PRK529;                                    
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: BL21(DE3);                                
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: TOBACCO ETCH VIRUS;                             
SOURCE  19 ORGANISM_TAXID: 12227;                                               
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: PRK529;                                    
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: BL21(DE3)                                 
KEYWDS    BETA BARREL, CHYMOTRYPSIN-TYPE CYSTEIN PROTEASE, ENZYME-              
KEYWDS   2 PEPTIDE COMPLEX, VIRAL PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PHAN,A.ZDANOV,A.G.EVDOKIMOV,J.E.TROPEA,H.K.PETERS III,              
AUTHOR   2 R.B.KAPUST,M.LI,A.WLODAWER,D.S.WAUGH                                 
REVDAT   3   24-FEB-09 1LVM    1       VERSN                                    
REVDAT   2   09-MAR-04 1LVM    1       JRNL                                     
REVDAT   1   27-NOV-02 1LVM    0                                                
JRNL        AUTH   J.PHAN,A.ZDANOV,A.G.EVDOKIMOV,J.E.TROPEA,                    
JRNL        AUTH 2 H.K.PETERS III,R.B.KAPUST,M.LI,A.WLODAWER,D.S.WAUGH          
JRNL        TITL   STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF            
JRNL        TITL 2 TOBACCO ETCH VIRUS PROTEASE.                                 
JRNL        REF    J.BIOL.CHEM.                  V. 277 50564 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12377789                                                     
JRNL        DOI    10.1074/JBC.M207224200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 140622.420                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 48452                          
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) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4885                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6658                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 759                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3750                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 577                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.28000                                             
REMARK   3    B22 (A**2) : -1.28000                                             
REMARK   3    B33 (A**2) : 2.56000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.020                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.31                            
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) : 11.750; 3.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 11.560; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 16.280; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 15.910; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 54.52                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LVM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016317.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48452                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.05800                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1LVB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MAGNESIUM              
REMARK 280  CHLORIDE, TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+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       91.58350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.75250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.75250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      137.37525            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.75250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.75250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.79175            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.75250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.75250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      137.37525            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.75250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.75250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.79175            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       91.58350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E                               
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     SER C   308                                                      
REMARK 465     GLY C   309                                                      
REMARK 465     THR C   310                                                      
REMARK 465     SER D   308                                                      
REMARK 465     GLY D   309                                                      
REMARK 465     THR D   310                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   2    CG   CD   OE1  OE2                                  
REMARK 470     THR A 118    OG1  CG2                                            
REMARK 470     LYS A 119    CG   CD   CE   NZ                                   
REMARK 470     SER A 120    OG                                                  
REMARK 470     ASN A 205    CG   OD1  ND2                                       
REMARK 470     ASN B 205    CG   OD1  ND2                                       
REMARK 470     ASN E 236    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   446     O    HOH B   222              2.02            
REMARK 500   CB   THR A   113     O    HOH A   405              2.11            
REMARK 500   O    HOH A   329     O    HOH A   542              2.16            
REMARK 500   O    SER A   123     O    HOH A   446              2.16            
REMARK 500   O    HOH B   360     O    HOH B   402              2.19            
REMARK 500   O    HOH A   265     O    HOH A   270              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY A  -8   N     GLY A  -8   CA      0.095                       
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    LEU A  72   CA  -  CB  -  CG  ANGL. DEV. =  14.1 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    LEU A  32     -176.29   -171.92                                   
REMARK 500    PHE A  48       30.75    -97.29                                   
REMARK 500    ASN A  51       78.62   -150.21                                   
REMARK 500    ASN A  52       35.66   -162.12                                   
REMARK 500    SER A 135     -129.58     72.29                                   
REMARK 500    ASP B  26       71.93     32.63                                   
REMARK 500    LEU B  32     -169.88   -168.65                                   
REMARK 500    PHE B  48       41.34   -103.79                                   
REMARK 500    ASN B  52       71.55   -170.20                                   
REMARK 500    GLN B 117     -145.49    -92.30                                   
REMARK 500    SER B 135     -113.52     45.93                                   
REMARK 500    SER B 168      -37.39   -131.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE C 301                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LVB   RELATED DB: PDB                                   
REMARK 900 CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE                   
REMARK 900 COMPLEXED WITH SUBSTRATE                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE AUTHOR STATES RESIDUES 308-310 ARE NOT IN THE CRYSTAL       
REMARK 999 OF CHAINS C AND D AND RESIDUES 309-310 ARE NOT IN THE PEPTIDE        
REMARK 999 SEQUENCE FOR THIS MUTANT. RESIDUE GLY 308 WAS CLEAVED OFF BY THE     
REMARK 999 ENZYME AND NOT PRESENT IN THE CRYSTAL.                               
DBREF  1LVM A    1   221  UNP    P04517   POLG_TEV      2038   2258             
DBREF  1LVM B    1   221  UNP    P04517   POLG_TEV      2038   2258             
DBREF  1LVM C  302   310  UNP    P04517   POLG_TEV      2786   2794             
DBREF  1LVM D  302   310  UNP    P04517   POLG_TEV      2786   2794             
DBREF  1LVM E  230   236  UNP    P04517   POLG_TEV      2267   2273             
SEQADV 1LVM GLY A   -8  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -7  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -6  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -5  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -4  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -3  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -2  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS A   -1  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM ASP A  219  UNP  P04517    SER  2256 ENGINEERED                     
SEQADV 1LVM GLY B   -8  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -7  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -6  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -5  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -4  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -3  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -2  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM HIS B   -1  UNP  P04517              EXPRESSION TAG                 
SEQADV 1LVM ASP B  219  UNP  P04517    SER  2256 ENGINEERED                     
SEQRES   1 A  229  GLY HIS HIS HIS HIS HIS HIS HIS GLY GLU SER LEU PHE          
SEQRES   2 A  229  LYS GLY PRO ARG ASP TYR ASN PRO ILE SER SER THR ILE          
SEQRES   3 A  229  CYS HIS LEU THR ASN GLU SER ASP GLY HIS THR THR SER          
SEQRES   4 A  229  LEU TYR GLY ILE GLY PHE GLY PRO PHE ILE ILE THR ASN          
SEQRES   5 A  229  LYS HIS LEU PHE ARG ARG ASN ASN GLY THR LEU LEU VAL          
SEQRES   6 A  229  GLN SER LEU HIS GLY VAL PHE LYS VAL LYS ASN THR THR          
SEQRES   7 A  229  THR LEU GLN GLN HIS LEU ILE ASP GLY ARG ASP MET ILE          
SEQRES   8 A  229  ILE ILE ARG MET PRO LYS ASP PHE PRO PRO PHE PRO GLN          
SEQRES   9 A  229  LYS LEU LYS PHE ARG GLU PRO GLN ARG GLU GLU ARG ILE          
SEQRES  10 A  229  CYS LEU VAL THR THR ASN PHE GLN THR LYS SER MET SER          
SEQRES  11 A  229  SER MET VAL SER ASP THR SER CYS THR PHE PRO SER SER          
SEQRES  12 A  229  ASP GLY ILE PHE TRP LYS HIS TRP ILE GLN THR LYS ASP          
SEQRES  13 A  229  GLY GLN CYS GLY SER PRO LEU VAL SER THR ARG ASP GLY          
SEQRES  14 A  229  PHE ILE VAL GLY ILE HIS SER ALA SER ASN PHE THR ASN          
SEQRES  15 A  229  THR ASN ASN TYR PHE THR SER VAL PRO LYS ASN PHE MET          
SEQRES  16 A  229  GLU LEU LEU THR ASN GLN GLU ALA GLN GLN TRP VAL SER          
SEQRES  17 A  229  GLY TRP ARG LEU ASN ALA ASP SER VAL LEU TRP GLY GLY          
SEQRES  18 A  229  HIS LYS VAL PHE MET ASP LYS PRO                              
SEQRES   1 B  229  GLY HIS HIS HIS HIS HIS HIS HIS GLY GLU SER LEU PHE          
SEQRES   2 B  229  LYS GLY PRO ARG ASP TYR ASN PRO ILE SER SER THR ILE          
SEQRES   3 B  229  CYS HIS LEU THR ASN GLU SER ASP GLY HIS THR THR SER          
SEQRES   4 B  229  LEU TYR GLY ILE GLY PHE GLY PRO PHE ILE ILE THR ASN          
SEQRES   5 B  229  LYS HIS LEU PHE ARG ARG ASN ASN GLY THR LEU LEU VAL          
SEQRES   6 B  229  GLN SER LEU HIS GLY VAL PHE LYS VAL LYS ASN THR THR          
SEQRES   7 B  229  THR LEU GLN GLN HIS LEU ILE ASP GLY ARG ASP MET ILE          
SEQRES   8 B  229  ILE ILE ARG MET PRO LYS ASP PHE PRO PRO PHE PRO GLN          
SEQRES   9 B  229  LYS LEU LYS PHE ARG GLU PRO GLN ARG GLU GLU ARG ILE          
SEQRES  10 B  229  CYS LEU VAL THR THR ASN PHE GLN THR LYS SER MET SER          
SEQRES  11 B  229  SER MET VAL SER ASP THR SER CYS THR PHE PRO SER SER          
SEQRES  12 B  229  ASP GLY ILE PHE TRP LYS HIS TRP ILE GLN THR LYS ASP          
SEQRES  13 B  229  GLY GLN CYS GLY SER PRO LEU VAL SER THR ARG ASP GLY          
SEQRES  14 B  229  PHE ILE VAL GLY ILE HIS SER ALA SER ASN PHE THR ASN          
SEQRES  15 B  229  THR ASN ASN TYR PHE THR SER VAL PRO LYS ASN PHE MET          
SEQRES  16 B  229  GLU LEU LEU THR ASN GLN GLU ALA GLN GLN TRP VAL SER          
SEQRES  17 B  229  GLY TRP ARG LEU ASN ALA ASP SER VAL LEU TRP GLY GLY          
SEQRES  18 B  229  HIS LYS VAL PHE MET ASP LYS PRO                              
SEQRES   1 C   10  ACE GLU ASN LEU TYR PHE GLN SER GLY THR                      
SEQRES   1 D   10  ACE GLU ASN LEU TYR PHE GLN SER GLY THR                      
SEQRES   1 E    7  GLU ALA THR GLN LEU MET ASN                                  
HET    ACE  C 301       3                                                       
HET    ACE  D 301       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   3  ACE    2(C2 H4 O)                                                   
FORMUL   6  HOH   *574(H2 O)                                                    
HELIX    1   1 HIS A   -1  LEU A    4  5                                   5    
HELIX    2   2 TYR A   11  SER A   16  1                                   6    
HELIX    3   3 ASN A   44  ARG A   50  5                                   7    
HELIX    4   4 ASN A   68  THR A   71  5                                   4    
HELIX    5   5 ASN A  185  ASN A  192  1                                   8    
HELIX    6   6 GLN A  193  GLN A  196  5                                   4    
HELIX    7   7 TYR B   11  SER B   16  1                                   6    
HELIX    8   8 ASN B   44  ARG B   49  5                                   6    
HELIX    9   9 ASN B   68  THR B   71  5                                   4    
HELIX   10  10 THR B  118  MET B  121  5                                   4    
HELIX   11  11 ASN B  185  ASN B  192  1                                   8    
HELIX   12  12 GLN B  193  GLN B  196  5                                   4    
SHEET    1   A 9 THR E 232  GLN E 233  0                                        
SHEET    2   A 9 GLY A  62  VAL A  66  1  O  VAL A  63   N  THR E 232           
SHEET    3   A 9 THR A  54  SER A  59 -1  O  LEU A  55   N  VAL A  66           
SHEET    4   A 9 ILE A  18  SER A  25 -1  O  HIS A  20   N  GLN A  58           
SHEET    5   A 9 HIS A  28  PHE A  37 -1  N  HIS A  28   O  SER A  25           
SHEET    6   A 9 PHE A  40  THR A  43 -1  N  PHE A  40   O  PHE A  37           
SHEET    7   A 9 ILE A  83  ARG A  86 -1  N  ILE A  83   O  THR A  43           
SHEET    8   A 9 GLN A  73  LEU A  76 -1  O  GLN A  73   N  ARG A  86           
SHEET    9   A 9 TRP A 198  SER A 200 -1  O  VAL A 199   N  GLN A  74           
SHEET    1   B15 PHE A 132  SER A 134  0                                        
SHEET    2   B15 PHE A 139  HIS A 142 -1  O  PHE A 139   N  SER A 134           
SHEET    3   B15 ASN A 177  SER A 181 -1  O  ASN A 177   N  HIS A 142           
SHEET    4   B15 ILE A 163  ASN A 171 -1  O  ILE A 166   N  THR A 180           
SHEET    5   B15 LEU C 304  PHE C 306 -1  N  TYR C 305   O  SER A 170           
SHEET    6   B15 HIS A 214  PHE A 217  1  O  LYS A 215   N  LEU C 304           
SHEET    7   B15 SER A 208  TRP A 211 -1  O  VAL A 209   N  VAL A 216           
SHEET    8   B15 HIS A 214  PHE A 217 -1  N  HIS A 214   O  TRP A 211           
SHEET    9   B15 LEU C 304  PHE C 306  1  N  LEU C 304   O  LYS A 215           
SHEET   10   B15 ILE A 163  ASN A 171 -1  O  SER A 170   N  TYR C 305           
SHEET   11   B15 PRO A 154  SER A 157 -1  N  LEU A 155   O  GLY A 165           
SHEET   12   B15 ARG A 108  ASN A 115 -1  O  CYS A 110   N  VAL A 156           
SHEET   13   B15 SER A 129  CYS A 130 -1  O  SER A 129   N  ILE A 109           
SHEET   14   B15 ARG A 108  ASN A 115 -1  N  ILE A 109   O  SER A 129           
SHEET   15   B15 SER A 122  VAL A 125 -1  O  SER A 122   N  ASN A 115           
SHEET    1   C 8 GLY B  62  VAL B  66  0                                        
SHEET    2   C 8 GLY B  53  SER B  59 -1  O  LEU B  55   N  VAL B  66           
SHEET    3   C 8 ILE B  18  SER B  25 -1  O  HIS B  20   N  GLN B  58           
SHEET    4   C 8 HIS B  28  PHE B  37 -1  O  HIS B  28   N  SER B  25           
SHEET    5   C 8 PHE B  40  THR B  43 -1  O  PHE B  40   N  PHE B  37           
SHEET    6   C 8 ILE B  83  ARG B  86 -1  O  ILE B  83   N  THR B  43           
SHEET    7   C 8 GLN B  73  LEU B  76 -1  O  GLN B  73   N  ARG B  86           
SHEET    8   C 8 TRP B 198  SER B 200 -1  O  VAL B 199   N  GLN B  74           
SHEET    1   D15 SER B 123  VAL B 125  0                                        
SHEET    2   D15 ARG B 108  THR B 114 -1  N  THR B 113   O  MET B 124           
SHEET    3   D15 SER B 129  CYS B 130 -1  N  SER B 129   O  ILE B 109           
SHEET    4   D15 ARG B 108  THR B 114 -1  O  ILE B 109   N  SER B 129           
SHEET    5   D15 PRO B 154  SER B 157 -1  O  PRO B 154   N  VAL B 112           
SHEET    6   D15 ILE B 163  ASN B 171 -1  N  VAL B 164   O  LEU B 155           
SHEET    7   D15 LEU D 304  PHE D 306 -1  N  TYR D 305   O  SER B 170           
SHEET    8   D15 HIS B 214  PHE B 217  1  O  LYS B 215   N  LEU D 304           
SHEET    9   D15 SER B 208  TRP B 211 -1  O  VAL B 209   N  VAL B 216           
SHEET   10   D15 HIS B 214  PHE B 217 -1  N  HIS B 214   O  TRP B 211           
SHEET   11   D15 LEU D 304  PHE D 306  1  O  LEU D 304   N  PHE B 217           
SHEET   12   D15 ILE B 163  ASN B 171 -1  N  SER B 170   O  TYR D 305           
SHEET   13   D15 ASN B 177  SER B 181 -1  N  TYR B 178   O  ALA B 169           
SHEET   14   D15 PHE B 139  HIS B 142 -1  O  TRP B 140   N  PHE B 179           
SHEET   15   D15 PHE B 132  SER B 134 -1  O  PHE B 132   N  LYS B 141           
LINK         C   ACE C 301                 N   GLU C 302     1555   1555  1.32  
LINK         C   ACE D 301                 N   GLU D 302     1555   1555  1.33  
SITE     1 AC1  2 HIS A 214  HOH C  81                                          
SITE     1 AC2  3 HOH D 133  HOH D 176  HOH D 421                               
CRYST1   75.505   75.505  183.167  90.00  90.00  90.00 P 43 21 2    16          
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      0.013244  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013244  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005459        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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