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Database: PDB
Entry: 4NYZ
LinkDB: 4NYZ
Original site: 4NYZ 
HEADER    TRANSFERASE                             11-DEC-13   4NYZ              
TITLE     THE EMCV 3DPOL STRUCTURE WITH ALTERED MOTIF A CONFORMATION AT 2.15A   
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GENOME POLYPROTEIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1834-2293;                                    
COMPND   5 SYNONYM: LEADER PROTEIN, PROTEIN VP0, VP4-VP2, PROTEIN VP4, P1A, RHO,
COMPND   6 VIRION PROTEIN 4, PROTEIN VP2, BETA, P1B, VIRION PROTEIN 2, PROTEIN  
COMPND   7 VP3, GAMMA, P1C, VIRION PROTEIN 3, PROTEIN VP1, ALPHA, P1D, VIRION   
COMPND   8 PROTEIN 1, PROTEIN 2A, P2A, G, PROTEIN 2B, I, P2B, PROTEIN 2C, C,    
COMPND   9 P2C, PROTEIN 3A, P3A, PROTEIN 3B, P3B, H, VPG, PROTEASE 3C, P3C,     
COMPND  10 PICORNAIN 3C, P22, RNA-DIRECTED RNA POLYMERASE 3D-POL, E, P3D-POL;   
COMPND  11 EC: 3.6.1.15, 3.4.22.28, 2.7.7.48;                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MENGO VIRUS;                                    
SOURCE   3 ORGANISM_TAXID: 12107;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYS;                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PETG20A                                   
KEYWDS    ENCEPHALOMYOCARDITIS VIRUS, CLOSE RIGHT HAND, RNA DEPENDENT RNA       
KEYWDS   2 POLYMERASE, TRANSFERASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.VIVES-ADRIAN,C.LUJAN,C.FERRER-ORTA,N.VERDAGUER                      
REVDAT   3   08-NOV-23 4NYZ    1       REMARK LINK                              
REVDAT   2   10-DEC-14 4NYZ    1       JRNL                                     
REVDAT   1   19-MAR-14 4NYZ    0                                                
JRNL        AUTH   L.VIVES-ADRIAN,C.LUJAN,B.OLIVA,L.VAN DER LINDEN,B.SELISKO,   
JRNL        AUTH 2 B.COUTARD,B.CANARD,F.J.VAN KUPPEVELD,C.FERRER-ORTA,          
JRNL        AUTH 3 N.VERDAGUER                                                  
JRNL        TITL   THE CRYSTAL STRUCTURE OF A CARDIOVIRUS RNA-DEPENDENT RNA     
JRNL        TITL 2 POLYMERASE REVEALS AN UNUSUAL CONFORMATION OF THE POLYMERASE 
JRNL        TITL 3 ACTIVE SITE                                                  
JRNL        REF    J.VIROL.                      V.  88  5595 2014              
JRNL        REFN                   ISSN 0022-538X                               
JRNL        PMID   24600002                                                     
JRNL        DOI    10.1128/JVI.03502-13                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 104.30                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 38457                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2036                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2816                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.31                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3680                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 110                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96000                                              
REMARK   3    B22 (A**2) : 0.96000                                              
REMARK   3    B33 (A**2) : -1.93000                                             
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): 0.206         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.575        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3806 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3623 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5158 ; 0.877 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8337 ; 0.700 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   463 ; 4.727 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;30.172 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   646 ;14.240 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;14.787 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   567 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4286 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   891 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1852 ; 0.528 ; 2.478       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1851 ; 0.528 ; 2.477       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2315 ; 0.976 ; 3.713       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2316 ; 0.976 ; 3.714       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1953 ; 0.413 ; 2.494       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1953 ; 0.414 ; 2.494       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2844 ; 0.750 ; 3.721       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4274 ; 2.871 ;19.515       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4275 ; 2.871 ;19.519       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6644 -29.2899 -23.9081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0629 T22:   0.0695                                     
REMARK   3      T33:   0.0350 T12:  -0.0018                                     
REMARK   3      T13:   0.0182 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6692 L22:   1.3987                                     
REMARK   3      L33:   2.0261 L12:  -0.2524                                     
REMARK   3      L13:   0.3984 L23:  -0.0213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0219 S12:   0.0185 S13:   0.1301                       
REMARK   3      S21:  -0.1688 S22:  -0.0111 S23:  -0.0899                       
REMARK   3      S31:  -0.0865 S32:   0.3273 S33:   0.0330                       
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 4NYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083832.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : CHANNEL-CUT SI(111)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40499                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 104.300                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.77000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 18.70                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1U09(THE HOMOLOGY MODEL HAS BEEN USED.)              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10%PEG6000 AND 2.0M NACL, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-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       61.27650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       61.27650            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.39850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.69925            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       61.27650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      149.09775            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      149.09775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.27650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       49.69925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       61.27650            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       99.39850            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       61.27650            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       99.39850            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       61.27650            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      149.09775            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       49.69925            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       61.27650            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       49.69925            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      149.09775            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       61.27650            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       61.27650            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       99.39850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 612  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 658  LIES ON A SPECIAL POSITION.                          
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  32       45.52    -82.85                                   
REMARK 500    LEU A  99     -149.30   -134.77                                   
REMARK 500    MET A 102      132.71     67.17                                   
REMARK 500    THR A 130       -9.68     66.51                                   
REMARK 500    ASN A 146       33.48    -93.47                                   
REMARK 500    PHE A 255      -68.47   -108.58                                   
REMARK 500    GLU A 281     -124.07     56.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 159   O                                                      
REMARK 620 2 GLU A 161   OE2 104.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1U09   RELATED DB: PDB                                   
REMARK 900 FOOT AND MOUTH DISEASE VIRUS RNA-DEPENDENT RNA POLYMERASE            
REMARK 900 RELATED ID: 4NZ0   RELATED DB: PDB                                   
DBREF  4NYZ A    1   460  UNP    P12296   POLG_ENMGO    1834   2293             
SEQRES   1 A  460  GLY ALA LEU GLU ARG LEU PRO ASP GLY PRO ARG ILE HIS          
SEQRES   2 A  460  VAL PRO ARG LYS THR ALA LEU ARG PRO THR VAL ALA ARG          
SEQRES   3 A  460  GLN VAL PHE GLN PRO ALA PHE ALA PRO ALA VAL LEU SER          
SEQRES   4 A  460  LYS PHE ASP PRO ARG THR ASP ALA ASP VAL ASP GLU VAL          
SEQRES   5 A  460  ALA PHE SER LYS HIS THR SER ASN GLN GLU THR LEU PRO          
SEQRES   6 A  460  PRO VAL PHE ARG MET VAL ALA ARG GLU TYR ALA ASN ARG          
SEQRES   7 A  460  VAL PHE ALA LEU LEU GLY ARG ASP ASN GLY ARG LEU SER          
SEQRES   8 A  460  VAL LYS GLN ALA LEU ASP GLY LEU GLU GLY MET ASP PRO          
SEQRES   9 A  460  MET ASP LYS ASN THR SER PRO GLY LEU PRO TYR THR THR          
SEQRES  10 A  460  LEU GLY MET ARG ARG THR ASP VAL VAL ASP TRP GLU THR          
SEQRES  11 A  460  ALA THR LEU ILE PRO PHE ALA ALA GLU ARG LEU GLU LYS          
SEQRES  12 A  460  MET ASN ASN LYS ASP PHE SER ASP ILE VAL TYR GLN THR          
SEQRES  13 A  460  PHE LEU LYS ASP GLU LEU ARG PRO ILE GLU LYS VAL GLN          
SEQRES  14 A  460  ALA ALA LYS THR ARG ILE VAL ASP VAL PRO PRO PHE GLU          
SEQRES  15 A  460  HIS CYS ILE LEU GLY ARG GLN LEU LEU GLY LYS PHE ALA          
SEQRES  16 A  460  SER LYS PHE GLN THR GLN PRO GLY LEU GLU LEU GLY SER          
SEQRES  17 A  460  ALA ILE GLY CYS ASP PRO ASP VAL HIS TRP THR ALA PHE          
SEQRES  18 A  460  GLY VAL ALA MET GLN GLY PHE GLU ARG VAL TYR ASP VAL          
SEQRES  19 A  460  ASP TYR SER ASN PHE ASP SER THR HIS SER VAL ALA VAL          
SEQRES  20 A  460  PHE ARG LEU LEU ALA GLU GLU PHE PHE SER GLU GLU ASN          
SEQRES  21 A  460  GLY PHE ASP PRO LEU VAL LYS ASP TYR LEU GLU SER LEU          
SEQRES  22 A  460  ALA ILE SER LYS HIS ALA TYR GLU GLU LYS ARG TYR LEU          
SEQRES  23 A  460  ILE THR GLY GLY LEU PRO SER GLY CYS ALA ALA THR SER          
SEQRES  24 A  460  MET LEU ASN THR ILE MET ASN ASN ILE ILE ILE ARG ALA          
SEQRES  25 A  460  GLY LEU TYR LEU THR TYR LYS ASN PHE GLU PHE ASP ASP          
SEQRES  26 A  460  VAL LYS VAL LEU SER TYR GLY ASP ASP LEU LEU VAL ALA          
SEQRES  27 A  460  THR ASN TYR GLN LEU ASN PHE ASP ARG VAL ARG THR SER          
SEQRES  28 A  460  LEU ALA LYS THR GLY TYR LYS ILE THR PRO ALA ASN LYS          
SEQRES  29 A  460  THR SER THR PHE PRO LEU GLU SER THR LEU GLU ASP VAL          
SEQRES  30 A  460  VAL PHE LEU LYS ARG LYS PHE LYS LYS GLU GLY PRO LEU          
SEQRES  31 A  460  TYR ARG PRO VAL MET ASN ARG GLU ALA LEU GLU ALA MET          
SEQRES  32 A  460  LEU SER TYR TYR ARG PRO GLY THR LEU SER GLU LYS LEU          
SEQRES  33 A  460  THR SER ILE THR MET LEU ALA VAL HIS SER GLY LYS GLN          
SEQRES  34 A  460  GLU TYR ASP ARG LEU PHE ALA PRO PHE ARG GLU VAL GLY          
SEQRES  35 A  460  VAL ILE VAL PRO THR PHE GLU SER VAL GLU TYR ARG TRP          
SEQRES  36 A  460  ARG SER LEU PHE TRP                                          
HET    GLN  A 501      10                                                       
HET     MG  A 502       1                                                       
HET    GOL  A 503       6                                                       
HETNAM     GLN GLUTAMINE                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GLN    C5 H10 N2 O3                                                 
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *110(H2 O)                                                    
HELIX    1   1 ALA A   25  GLN A   30  1                                   6    
HELIX    2   2 ASP A   48  ALA A   53  1                                   6    
HELIX    3   3 PHE A   54  THR A   58  5                                   5    
HELIX    4   4 PRO A   65  GLY A   84  1                                  20    
HELIX    5   5 SER A   91  GLY A   98  1                                   8    
HELIX    6   6 ARG A  121  VAL A  125  1                                   5    
HELIX    7   7 ILE A  134  ASN A  146  1                                  13    
HELIX    8   8 ILE A  165  ALA A  170  1                                   6    
HELIX    9   9 PRO A  180  GLN A  199  1                                  20    
HELIX   10  10 ASP A  213  GLN A  226  1                                  14    
HELIX   11  11 SER A  244  PHE A  255  1                                  12    
HELIX   12  12 SER A  257  GLY A  261  5                                   5    
HELIX   13  13 LEU A  265  ALA A  274  1                                  10    
HELIX   14  14 ALA A  297  TYR A  318  1                                  22    
HELIX   15  15 GLU A  322  VAL A  326  5                                   5    
HELIX   16  16 ASN A  344  LYS A  354  1                                  11    
HELIX   17  17 ASN A  396  SER A  405  1                                  10    
HELIX   18  18 THR A  411  VAL A  424  1                                  14    
HELIX   19  19 GLY A  427  VAL A  441  1                                  15    
HELIX   20  20 THR A  447  LEU A  458  1                                  12    
SHEET    1   A 5 LEU A   3  ARG A   5  0                                        
SHEET    2   A 5 LYS A 283  THR A 288 -1  O  LEU A 286   N  GLU A   4           
SHEET    3   A 5 ILE A 275  TYR A 280 -1  N  HIS A 278   O  TYR A 285           
SHEET    4   A 5 TYR A 154  LEU A 158  1  N  TYR A 154   O  ALA A 279           
SHEET    5   A 5 ILE A 175  VAL A 178 -1  O  VAL A 176   N  PHE A 157           
SHEET    1   B 2 ARG A  21  PRO A  22  0                                        
SHEET    2   B 2 TYR A 406  TYR A 407 -1  O  TYR A 407   N  ARG A  21           
SHEET    1   C 2 PHE A  33  PRO A  35  0                                        
SHEET    2   C 2 LEU A 162  PRO A 164 -1  O  ARG A 163   N  ALA A  34           
SHEET    1   D 2 VAL A 126  ASP A 127  0                                        
SHEET    2   D 2 THR A 132  LEU A 133 -1  O  THR A 132   N  ASP A 127           
SHEET    1   E 3 ARG A 230  ASP A 235  0                                        
SHEET    2   E 3 ASP A 334  THR A 339 -1  O  LEU A 335   N  VAL A 234           
SHEET    3   E 3 LYS A 327  TYR A 331 -1  N  LYS A 327   O  ALA A 338           
SHEET    1   F 2 ARG A 382  GLU A 387  0                                        
SHEET    2   F 2 LEU A 390  MET A 395 -1  O  LEU A 390   N  GLU A 387           
LINK         O   LYS A 159                MG    MG A 502     1555   1555  2.82  
LINK         OE2 GLU A 161                MG    MG A 502     1555   1555  2.72  
CISPEP   1 LEU A  113    PRO A  114          0         0.28                     
SITE     1 AC1 14 TYR A 236  ASN A 238  SER A 241  THR A 242                    
SITE     2 AC1 14 HIS A 243  GLY A 290  LEU A 291  ASP A 333                    
SITE     3 AC1 14 HOH A 625  HOH A 642  HOH A 692  HOH A 695                    
SITE     4 AC1 14 HOH A 698  HOH A 707                                          
SITE     1 AC2  6 ALA A  36  LYS A 159  GLU A 161  ARG A 163                    
SITE     2 AC2  6 THR A 173  ARG A 174                                          
SITE     1 AC3  4 PHE A  33  LYS A 381  ALA A 399  HOH A 677                    
CRYST1  122.553  122.553  198.797  90.00  90.00  90.00 I 41 2 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      0.008160  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008160  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005030        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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