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Database: PDB
Entry: 1R8A
LinkDB: 1R8A
Original site: 1R8A 
HEADER    TRANSFERASE                             23-OCT-03   1R8A              
TITLE     CRYSTAL STRUCTURES OF AN ARCHAEAL CLASS I CCA-ADDING ENZYME AND ITS   
TITLE    2 NUCLEOTIDE COMPLEXES                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA NUCLEOTIDYLTRANSFERASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TRNA ADENYLYLTRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, CCA-  
COMPND   5 ADDING ENZYME;                                                       
COMPND   6 EC: 2.7.7.25;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 GENE: CCA, AF2156;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CCA ADDING ENZYME, NUCLEOTIDYLTRANSFERASE, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XIONG,F.LI,J.WANG,A.M.WEINER,T.A.STEITZ                             
REVDAT   4   14-FEB-24 1R8A    1       REMARK LINK                              
REVDAT   3   13-JUL-11 1R8A    1       VERSN                                    
REVDAT   2   24-FEB-09 1R8A    1       VERSN                                    
REVDAT   1   16-DEC-03 1R8A    0                                                
JRNL        AUTH   Y.XIONG,F.LI,J.WANG,A.M.WEINER,T.A.STEITZ                    
JRNL        TITL   CRYSTAL STRUCTURES OF AN ARCHAEAL CLASS I CCA-ADDING ENZYME  
JRNL        TITL 2 AND ITS NUCLEOTIDE COMPLEXES                                 
JRNL        REF    MOL.CELL                      V.  12  1165 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   14636575                                                     
JRNL        DOI    10.1016/S1097-2765(03)00440-4                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28329                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1533                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4121                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 248                          
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3630                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 328                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.61000                                              
REMARK   3    B22 (A**2) : 1.66000                                              
REMARK   3    B33 (A**2) : -2.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.60000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.194         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.733         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3713 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3431 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4988 ; 1.468 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7961 ; 0.837 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   436 ; 6.477 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   518 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4094 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   840 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   801 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3917 ; 0.235 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2358 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   217 ; 0.220 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.355 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    25 ; 0.204 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   160 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 0.203 ; 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):  2176 ; 1.579 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3513 ; 2.646 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1537 ; 3.989 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1475 ; 6.094 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 4                                          
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    17        A   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3330  12.5031  46.0556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6111 T22:   0.3381                                     
REMARK   3      T33:   0.3451 T12:   0.3159                                     
REMARK   3      T13:  -0.0587 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3460 L22:   7.3954                                     
REMARK   3      L33:  20.8138 L12:   0.4795                                     
REMARK   3      L13:   0.4258 L23:  -2.2510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6297 S12:  -0.2490 S13:  -0.1864                       
REMARK   3      S21:   1.5551 S22:   0.1922 S23:  -0.9978                       
REMARK   3      S31:  -0.4601 S32:   0.3733 S33:   0.4375                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   125        A   258                          
REMARK   3    RESIDUE RANGE :   A     1        A    16                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7788  13.2919  20.8457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0763 T22:   0.2897                                     
REMARK   3      T33:   0.2060 T12:   0.1172                                     
REMARK   3      T13:   0.0275 T23:   0.0362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1541 L22:   3.6355                                     
REMARK   3      L33:   3.8495 L12:  -1.3907                                     
REMARK   3      L13:  -0.4324 L23:   0.5186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2057 S12:  -0.2550 S13:  -0.2324                       
REMARK   3      S21:   0.2784 S22:   0.1477 S23:   0.4456                       
REMARK   3      S31:   0.0898 S32:  -0.6712 S33:   0.0581                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   338        A   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.5489   1.1468  -0.0555              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2329 T22:   0.1915                                     
REMARK   3      T33:   0.2132 T12:  -0.0153                                     
REMARK   3      T13:  -0.0459 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2195 L22:   3.4255                                     
REMARK   3      L33:   1.3759 L12:   2.3494                                     
REMARK   3      L13:  -0.8613 L23:  -1.5431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0817 S12:  -0.2395 S13:   0.0790                       
REMARK   3      S21:   0.3793 S22:  -0.0549 S23:  -0.1937                       
REMARK   3      S31:  -0.2189 S32:   0.4373 S33:  -0.0267                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   259        A   337                          
REMARK   3    RESIDUE RANGE :   A   383        A   437                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2637  -7.8565  17.3934              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2157 T22:   0.0918                                     
REMARK   3      T33:   0.1723 T12:   0.0645                                     
REMARK   3      T13:   0.0100 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4170 L22:   1.1742                                     
REMARK   3      L33:   3.8062 L12:  -0.8416                                     
REMARK   3      L13:  -0.1153 L23:   0.0623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2212 S12:  -0.3540 S13:  -0.0227                       
REMARK   3      S21:   0.1148 S22:   0.2333 S23:   0.0226                       
REMARK   3      S31:   0.3427 S32:  -0.1309 S33:  -0.0121                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 1R8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020560.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29906                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM CHLORIDE, ETHANOL, TRIS,         
REMARK 280  MAGNESIUM CHLORIDE, SODIUM CHLORIDE, PH 6.4, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       43.22650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.36300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.22650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.36300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       86.45300            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 883  LIES ON A SPECIAL POSITION.                          
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   804     O    HOH A   840              2.00            
REMARK 500   O    HOH A   648     O    HOH A   785              2.06            
REMARK 500   O    HOH A   606     O    HOH A   747              2.08            
REMARK 500   O    HOH A   618     O    HOH A   831              2.11            
REMARK 500   O    ARG A   268     O    HOH A   765              2.19            
REMARK 500   O    HOH A   831     O    HOH A   920              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    MET A 314   SD    MET A 314   CE     -0.419                       
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    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 202   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 233   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 274   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 290   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    LYS A   2      127.64     73.60                                   
REMARK 500    SER A  57       51.50   -110.95                                   
REMARK 500    GLU A  96      -48.73   -140.20                                   
REMARK 500    GLU A 119      125.36     73.99                                   
REMARK 500    PRO A 120     -160.60    -69.54                                   
REMARK 500    ASN A 122       37.80   -147.99                                   
REMARK 500    GLU A 261       69.22     36.85                                   
REMARK 500    SER A 323     -166.84   -102.32                                   
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                              MN A 604  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  59   OE2                                                    
REMARK 620 2 ASP A  61   OD1 161.8                                              
REMARK 620 3 ASP A 110   OD2  89.5  83.6                                        
REMARK 620 4 HOH A 750   O   105.9  89.4  78.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 603  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 133   NE2                                                    
REMARK 620 2 ASP A 218   OD2 103.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 605  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 205   O                                                      
REMARK 620 2 SER A 391   OG   98.3                                              
REMARK 620 3 SER A 391   O    83.1  73.2                                        
REMARK 620 4 THR A 395   OG1  94.5 151.7  83.4                                  
REMARK 620 5 HOH A 766   O   119.9  94.3 155.7 101.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 605                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1R89   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH CTP                                      
REMARK 900 RELATED ID: 1R8B   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH ATP                                      
REMARK 900 RELATED ID: 1R8C   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH UTP                                      
DBREF  1R8A A    1   437  UNP    O28126   CCA_ARCFU        1    437             
SEQRES   1 A  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 A  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 A  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 A  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 A  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 A  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 A  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 A  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 A  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 A  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 A  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 A  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 A  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 A  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 A  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 A  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 A  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 A  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 A  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 A  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 A  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 A  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 A  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 A  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 A  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 A  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 A  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 A  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 A  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 A  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 A  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 A  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 A  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 A  437  CYS GLU MET MET GLY VAL LYS ASP                              
HET     MN  A 603       1                                                       
HET     MN  A 604       1                                                       
HET     NA  A 605       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      NA SODIUM ION                                                       
FORMUL   2   MN    2(MN 2+)                                                     
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  HOH   *328(H2 O)                                                    
HELIX    1   1 LYS A    2  ILE A   15  1                                  14    
HELIX    2   2 ASP A   17  GLY A   39  1                                  23    
HELIX    3   3 GLY A   46  ARG A   50  1                                   5    
HELIX    4   4 GLU A   73  LEU A   87  1                                  15    
HELIX    5   5 ARG A  129  GLU A  138  1                                  10    
HELIX    6   6 LYS A  144  ASN A  158  1                                  15    
HELIX    7   7 SER A  171  GLY A  183  1                                  13    
HELIX    8   8 SER A  184  ARG A  193  1                                  10    
HELIX    9   9 ALA A  204  GLY A  206  5                                   3    
HELIX   10  10 SER A  231  ALA A  248  1                                  18    
HELIX   11  11 SER A  250  LYS A  255  5                                   6    
HELIX   12  12 GLU A  263  GLY A  275  1                                  13    
HELIX   13  13 VAL A  289  GLU A  311  1                                  23    
HELIX   14  14 ASP A  351  ARG A  361  1                                  11    
HELIX   15  15 THR A  384  HIS A  396  1                                  13    
HELIX   16  16 TRP A  397  LEU A  400  5                                   4    
HELIX   17  17 GLY A  401  TYR A  411  1                                  11    
HELIX   18  18 GLY A  417  PHE A  421  1                                   5    
HELIX   19  19 VAL A  425  GLY A  434  1                                  10    
SHEET    1   A 5 TYR A  42  VAL A  45  0                                        
SHEET    2   A 5 ILE A  60  PHE A  66 -1  O  PHE A  63   N  VAL A  43           
SHEET    3   A 5 GLU A 108  TYR A 115  1  O  ASP A 110   N  VAL A  62           
SHEET    4   A 5 PRO A  98  VAL A 103 -1  N  VAL A 100   O  VAL A 111           
SHEET    5   A 5 ILE A  92  TYR A  94 -1  N  ARG A  93   O  TYR A  99           
SHEET    1   B 3 GLU A 207  LYS A 210  0                                        
SHEET    2   B 3 THR A 199  ASP A 202 -1  N  VAL A 200   O  ARG A 209           
SHEET    3   B 3 PHE A 215  VAL A 217  1  O  VAL A 217   N  ILE A 201           
SHEET    1   C 4 PRO A 315  ALA A 322  0                                        
SHEET    2   C 4 PHE A 326  CYS A 333 -1  O  LEU A 330   N  ALA A 319           
SHEET    3   C 4 ALA A 277  ARG A 284 -1  N  VAL A 281   O  LEU A 329           
SHEET    4   C 4 PHE A 412  SER A 416 -1  O  ILE A 415   N  ALA A 280           
SHEET    1   D 3 VAL A 341  GLN A 348  0                                        
SHEET    2   D 3 ARG A 373  MET A 379 -1  O  ALA A 376   N  ARG A 344           
SHEET    3   D 3 PHE A 368  GLU A 370 -1  N  GLU A 370   O  ARG A 373           
LINK         OE2 GLU A  59                MN    MN A 604     1555   1555  2.76  
LINK         OD1 ASP A  61                MN    MN A 604     1555   1555  2.20  
LINK         OD2 ASP A 110                MN    MN A 604     1555   1555  1.71  
LINK         NE2 HIS A 133                MN    MN A 603     1555   1555  2.12  
LINK         O   LYS A 205                NA    NA A 605     3545   1555  2.39  
LINK         OD2 ASP A 218                MN    MN A 603     1555   1555  1.75  
LINK         OG  SER A 391                NA    NA A 605     1555   1555  2.57  
LINK         O   SER A 391                NA    NA A 605     1555   1555  2.76  
LINK         OG1 THR A 395                NA    NA A 605     1555   1555  2.27  
LINK        MN    MN A 604                 O   HOH A 750     1555   1555  2.60  
LINK        NA    NA A 605                 O   HOH A 766     1555   1555  1.81  
SITE     1 AC1  3 ARG A 129  HIS A 133  ASP A 218                               
SITE     1 AC2  4 GLU A  59  ASP A  61  ASP A 110  HOH A 750                    
SITE     1 AC3  4 LYS A 205  SER A 391  THR A 395  HOH A 766                    
CRYST1   86.453   78.726   77.396  90.00  98.03  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011567  0.000000  0.001632        0.00000                         
SCALE2      0.000000  0.012702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013049        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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