GenomeNet

Database: PDB
Entry: 3MMG
LinkDB: 3MMG
Original site: 3MMG 
HEADER    VIRAL PROTEIN, HYDROLASE                19-APR-10   3MMG              
TITLE     CRYSTAL STRUCTURE OF TOBACCO VEIN MOTTLING VIRUS PROTEASE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEAR INCLUSION PROTEIN A;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NUCLEAR INCLUSION PROTEIN B FRAGMENT;                      
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TOBACCO VEIN MOTTLING VIRUS;                    
SOURCE   3 ORGANISM_COMMON: TVMV;                                               
SOURCE   4 ORGANISM_TAXID: 12228;                                               
SOURCE   5 GENE: PROTEASE;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 RIL (DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDESTHISMBP;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: TOBACCO VEIN MOTTLING VIRUS;                    
SOURCE  14 ORGANISM_COMMON: TVMV;                                               
SOURCE  15 ORGANISM_TAXID: 12228;                                               
SOURCE  16 OTHER_DETAILS: PEPTIDE 8MER                                          
KEYWDS    3C-TYPE PROTEASE, TEV, TVMV, VIRAL PROTEIN, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PING,B.P.AUSTIN,J.TOZSER,D.S.WAUGH                                  
REVDAT   2   10-NOV-10 3MMG    1       JRNL                                     
REVDAT   1   20-OCT-10 3MMG    0                                                
JRNL        AUTH   P.SUN,B.P.AUSTIN,J.TOZSER,D.S.WAUGH                          
JRNL        TITL   STRUCTURAL DETERMINANTS OF TOBACCO VEIN MOTTLING VIRUS       
JRNL        TITL 2 PROTEASE SUBSTRATE SPECIFICITY.                              
JRNL        REF    PROTEIN SCI.                  V.  19  2240 2010              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   20862670                                                     
JRNL        DOI    10.1002/PRO.506                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 47451                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2544                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3278                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 191                          
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3540                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 553                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.02000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : -0.94000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.112         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.032         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3688 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4997 ; 1.335 ; 1.925       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   457 ; 6.685 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   169 ;36.621 ;24.320       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   628 ;12.845 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.813 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   545 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2804 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1667 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2537 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   421 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.160 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2318 ; 0.950 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3674 ; 1.519 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1547 ; 2.307 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1323 ; 3.615 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3MMG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058728.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97939                            
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50064                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1Q31                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FORMATE  20% PEG 3350 ,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.23800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.23150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.78150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.23150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.23800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.78150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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     ASP A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     ASP A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     PHE A   224                                                      
REMARK 465     MET A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     LYS A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     THR A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     ILE A   233                                                      
REMARK 465     MET A   234                                                      
REMARK 465     ASP A   235                                                      
REMARK 465     ASP A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     VAL A   238                                                      
REMARK 465     ARG A   239                                                      
REMARK 465     THR A   240                                                      
REMARK 465     GLN A   241                                                      
REMARK 465     SER B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     GLU B   217                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     GLU B   221                                                      
REMARK 465     ASP B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     PHE B   224                                                      
REMARK 465     MET B   225                                                      
REMARK 465     ALA B   226                                                      
REMARK 465     LYS B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     THR B   229                                                      
REMARK 465     VAL B   230                                                      
REMARK 465     ALA B   231                                                      
REMARK 465     ALA B   232                                                      
REMARK 465     ILE B   233                                                      
REMARK 465     MET B   234                                                      
REMARK 465     ASP B   235                                                      
REMARK 465     ASP B   236                                                      
REMARK 465     LEU B   237                                                      
REMARK 465     VAL B   238                                                      
REMARK 465     ARG B   239                                                      
REMARK 465     THR B   240                                                      
REMARK 465     GLN B   241                                                      
REMARK 465     ASP C     9                                                      
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   346     O    HOH A   534              1.63            
REMARK 500   O    HOH A   289     O    HOH A   363              2.15            
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    ALA A  67     -138.35     69.28                                   
REMARK 500    SER A 168      -57.19   -138.29                                   
REMARK 500    ARG B  50      -41.16   -135.09                                   
REMARK 500    ASN B  52       37.41   -147.75                                   
REMARK 500    GLN B 117     -146.88    -95.29                                   
REMARK 500    SER B 168      -55.57   -140.88                                   
REMARK 500    SER D   8       36.43   -140.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 395        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B 414        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A 442        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A 450        DISTANCE =  7.57 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 242                 
DBREF  3MMG A    1   241  UNP    Q9J0W2   Q9J0W2_TVMV      1    241             
DBREF  3MMG B    1   241  UNP    Q9J0W2   Q9J0W2_TVMV      1    241             
DBREF  3MMG C    2     9  PDB    3MMG     3MMG             2      9             
DBREF  3MMG D    2     9  PDB    3MMG     3MMG             2      9             
SEQADV 3MMG ALA A   65  UNP  Q9J0W2    LYS    65 ENGINEERED MUTATION            
SEQADV 3MMG ALA A   67  UNP  Q9J0W2    LYS    67 ENGINEERED MUTATION            
SEQADV 3MMG ALA A  151  UNP  Q9J0W2    CYS   151 ENGINEERED MUTATION            
SEQADV 3MMG ALA B   65  UNP  Q9J0W2    LYS    65 ENGINEERED MUTATION            
SEQADV 3MMG ALA B   67  UNP  Q9J0W2    LYS    67 ENGINEERED MUTATION            
SEQADV 3MMG ALA B  151  UNP  Q9J0W2    CYS   151 ENGINEERED MUTATION            
SEQRES   1 A  241  SER LYS ALA LEU LEU LYS GLY VAL ARG ASP PHE ASN PRO          
SEQRES   2 A  241  ILE SER ALA CYS VAL CYS LEU LEU GLU ASN SER SER ASP          
SEQRES   3 A  241  GLY HIS SER GLU ARG LEU PHE GLY ILE GLY PHE GLY PRO          
SEQRES   4 A  241  TYR ILE ILE ALA ASN GLN HIS LEU PHE ARG ARG ASN ASN          
SEQRES   5 A  241  GLY GLU LEU THR ILE LYS THR MET HIS GLY GLU PHE ALA          
SEQRES   6 A  241  VAL ALA ASN SER THR GLN LEU GLN MET LYS PRO VAL GLU          
SEQRES   7 A  241  GLY ARG ASP ILE ILE VAL ILE LYS MET ALA LYS ASP PHE          
SEQRES   8 A  241  PRO PRO PHE PRO GLN LYS LEU LYS PHE ARG GLN PRO THR          
SEQRES   9 A  241  ILE LYS ASP ARG VAL CYS MET VAL SER THR ASN PHE GLN          
SEQRES  10 A  241  GLN LYS SER VAL SER SER LEU VAL SER GLU SER SER HIS          
SEQRES  11 A  241  ILE VAL HIS LYS GLU ASP THR SER PHE TRP GLN HIS TRP          
SEQRES  12 A  241  ILE THR THR LYS ASP GLY GLN ALA GLY SER PRO LEU VAL          
SEQRES  13 A  241  SER ILE ILE ASP GLY ASN ILE LEU GLY ILE HIS SER LEU          
SEQRES  14 A  241  THR HIS THR THR ASN GLY SER ASN TYR PHE VAL GLU PHE          
SEQRES  15 A  241  PRO GLU LYS PHE VAL ALA THR TYR LEU ASP ALA ALA ASP          
SEQRES  16 A  241  GLY TRP CYS LYS ASN TRP LYS PHE ASN ALA ASP LYS ILE          
SEQRES  17 A  241  SER TRP GLY SER PHE THR LEU VAL GLU ASP ALA PRO GLU          
SEQRES  18 A  241  ASP ASP PHE MET ALA LYS LYS THR VAL ALA ALA ILE MET          
SEQRES  19 A  241  ASP ASP LEU VAL ARG THR GLN                                  
SEQRES   1 B  241  SER LYS ALA LEU LEU LYS GLY VAL ARG ASP PHE ASN PRO          
SEQRES   2 B  241  ILE SER ALA CYS VAL CYS LEU LEU GLU ASN SER SER ASP          
SEQRES   3 B  241  GLY HIS SER GLU ARG LEU PHE GLY ILE GLY PHE GLY PRO          
SEQRES   4 B  241  TYR ILE ILE ALA ASN GLN HIS LEU PHE ARG ARG ASN ASN          
SEQRES   5 B  241  GLY GLU LEU THR ILE LYS THR MET HIS GLY GLU PHE ALA          
SEQRES   6 B  241  VAL ALA ASN SER THR GLN LEU GLN MET LYS PRO VAL GLU          
SEQRES   7 B  241  GLY ARG ASP ILE ILE VAL ILE LYS MET ALA LYS ASP PHE          
SEQRES   8 B  241  PRO PRO PHE PRO GLN LYS LEU LYS PHE ARG GLN PRO THR          
SEQRES   9 B  241  ILE LYS ASP ARG VAL CYS MET VAL SER THR ASN PHE GLN          
SEQRES  10 B  241  GLN LYS SER VAL SER SER LEU VAL SER GLU SER SER HIS          
SEQRES  11 B  241  ILE VAL HIS LYS GLU ASP THR SER PHE TRP GLN HIS TRP          
SEQRES  12 B  241  ILE THR THR LYS ASP GLY GLN ALA GLY SER PRO LEU VAL          
SEQRES  13 B  241  SER ILE ILE ASP GLY ASN ILE LEU GLY ILE HIS SER LEU          
SEQRES  14 B  241  THR HIS THR THR ASN GLY SER ASN TYR PHE VAL GLU PHE          
SEQRES  15 B  241  PRO GLU LYS PHE VAL ALA THR TYR LEU ASP ALA ALA ASP          
SEQRES  16 B  241  GLY TRP CYS LYS ASN TRP LYS PHE ASN ALA ASP LYS ILE          
SEQRES  17 B  241  SER TRP GLY SER PHE THR LEU VAL GLU ASP ALA PRO GLU          
SEQRES  18 B  241  ASP ASP PHE MET ALA LYS LYS THR VAL ALA ALA ILE MET          
SEQRES  19 B  241  ASP ASP LEU VAL ARG THR GLN                                  
SEQRES   1 C    8  GLU THR VAL ARG PHE GLN SER ASP                              
SEQRES   1 D    8  GLU THR VAL ARG PHE GLN SER ASP                              
HET    FMT  A 242       3                                                       
HETNAM     FMT FORMIC ACID                                                      
FORMUL   5  FMT    C H2 O2                                                      
FORMUL   6  HOH   *553(H2 O)                                                    
HELIX    1   1 PHE A   11  ALA A   16  1                                   6    
HELIX    2   2 ASN A   44  ARG A   49  5                                   6    
HELIX    3   3 THR A   70  LEU A   72  5                                   3    
HELIX    4   4 LYS A  185  LEU A  191  1                                   7    
HELIX    5   5 ASN A  204  ILE A  208  5                                   5    
HELIX    6   6 PHE B   11  ALA B   16  1                                   6    
HELIX    7   7 ASN B   44  ARG B   49  5                                   6    
HELIX    8   8 ASN B   68  LEU B   72  5                                   5    
HELIX    9   9 GLN B  118  VAL B  121  5                                   4    
HELIX   10  10 LYS B  185  LEU B  191  1                                   7    
HELIX   11  11 ASN B  204  ILE B  208  5                                   5    
SHEET    1   A 8 ARG A   9  ASP A  10  0                                        
SHEET    2   A 8 SER B 123  VAL B 125 -1  O  VAL B 125   N  ARG A   9           
SHEET    3   A 8 VAL B 109  THR B 114 -1  N  SER B 113   O  LEU B 124           
SHEET    4   A 8 PRO B 154  SER B 157 -1  O  VAL B 156   N  CYS B 110           
SHEET    5   A 8 ILE B 163  HIS B 171 -1  O  LEU B 164   N  LEU B 155           
SHEET    6   A 8 ASN B 177  GLU B 181 -1  O  VAL B 180   N  ILE B 166           
SHEET    7   A 8 PHE B 139  HIS B 142 -1  N  TRP B 140   O  PHE B 179           
SHEET    8   A 8 ILE B 131  HIS B 133 -1  N  VAL B 132   O  GLN B 141           
SHEET    1   B 7 ARG A   9  ASP A  10  0                                        
SHEET    2   B 7 SER B 123  VAL B 125 -1  O  VAL B 125   N  ARG A   9           
SHEET    3   B 7 VAL B 109  THR B 114 -1  N  SER B 113   O  LEU B 124           
SHEET    4   B 7 PRO B 154  SER B 157 -1  O  VAL B 156   N  CYS B 110           
SHEET    5   B 7 ILE B 163  HIS B 171 -1  O  LEU B 164   N  LEU B 155           
SHEET    6   B 7 THR D   3  PHE D   6 -1  O  ARG D   5   N  THR B 170           
SHEET    7   B 7 THR B 214  LEU B 215  1  N  THR B 214   O  VAL D   4           
SHEET    1   C 7 GLY A  62  ASN A  68  0                                        
SHEET    2   C 7 GLU A  54  THR A  59 -1  N  ILE A  57   O  PHE A  64           
SHEET    3   C 7 VAL A  18  SER A  25 -1  N  SER A  24   O  GLU A  54           
SHEET    4   C 7 HIS A  28  PHE A  37 -1  O  LEU A  32   N  LEU A  21           
SHEET    5   C 7 TYR A  40  ALA A  43 -1  O  ILE A  42   N  ILE A  35           
SHEET    6   C 7 ILE A  83  LYS A  86 -1  O  ILE A  83   N  ALA A  43           
SHEET    7   C 7 MET A  74  PRO A  76 -1  N  LYS A  75   O  VAL A  84           
SHEET    1   D 7 VAL A 121  SER A 129  0                                        
SHEET    2   D 7 VAL A 109  PHE A 116 -1  N  VAL A 109   O  SER A 129           
SHEET    3   D 7 PRO A 154  SER A 157 -1  O  VAL A 156   N  CYS A 110           
SHEET    4   D 7 ILE A 163  HIS A 171 -1  O  LEU A 164   N  LEU A 155           
SHEET    5   D 7 ASN A 177  GLU A 181 -1  O  VAL A 180   N  ILE A 166           
SHEET    6   D 7 PHE A 139  HIS A 142 -1  N  TRP A 140   O  PHE A 179           
SHEET    7   D 7 VAL A 132  HIS A 133 -1  N  VAL A 132   O  GLN A 141           
SHEET    1   E 6 VAL A 121  SER A 129  0                                        
SHEET    2   E 6 VAL A 109  PHE A 116 -1  N  VAL A 109   O  SER A 129           
SHEET    3   E 6 PRO A 154  SER A 157 -1  O  VAL A 156   N  CYS A 110           
SHEET    4   E 6 ILE A 163  HIS A 171 -1  O  LEU A 164   N  LEU A 155           
SHEET    5   E 6 THR C   3  PHE C   6 -1  O  ARG C   5   N  THR A 170           
SHEET    6   E 6 THR A 214  LEU A 215  1  N  THR A 214   O  VAL C   4           
SHEET    1   F 7 GLY B  62  VAL B  66  0                                        
SHEET    2   F 7 LEU B  55  THR B  59 -1  N  LEU B  55   O  VAL B  66           
SHEET    3   F 7 VAL B  18  SER B  25 -1  N  LEU B  20   O  LYS B  58           
SHEET    4   F 7 HIS B  28  PHE B  37 -1  O  LEU B  32   N  LEU B  21           
SHEET    5   F 7 TYR B  40  ALA B  43 -1  O  ILE B  42   N  ILE B  35           
SHEET    6   F 7 ILE B  83  LYS B  86 -1  O  ILE B  83   N  ALA B  43           
SHEET    7   F 7 MET B  74  PRO B  76 -1  N  LYS B  75   O  VAL B  84           
SITE     1 AC1  7 GLN A  96  LEU A  98  LYS A  99  VAL A 187                    
SITE     2 AC1  7 HOH A 266  HOH A 361  HOH A 553                               
CRYST1   76.476   77.563   78.463  90.00  90.00  90.00 P 21 21 21    8          
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      0.013076  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system