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Database: PDB
Entry: 2ZH6
LinkDB: 2ZH6
Original site: 2ZH6 
HEADER    TRANSFERASE/RNA                         01-FEB-08   2ZH6              
TITLE     COMPLEX STRUCTURE OF AFCCA WITH TRNAMINIDCU AND ATP                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA (34-MER);                                             
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CCA-ADDING ENZYME;                                         
COMPND   7 CHAIN: A;                                                            
COMPND   8 SYNONYM: TRNA NUCLEOTIDYLTRANSFERASE, TRNA ADENYLYL-/CYTIDYLYL-      
COMPND   9 TRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, TRNA-NT;                    
COMPND  10 EC: 2.7.7.25, 2.7.7.21;                                              
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   5 ORGANISM_TAXID: 2234;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-22B                                   
KEYWDS    TRANSFERASE/RNA, ATP-BINDING, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-   
KEYWDS   2 BINDING, NUCLEOTIDYLTRANSFERASE, RNA REPAIR, RNA-BINDING, TRNA       
KEYWDS   3 PROCESSING, TRANSFERASE-RNA COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TOH,K.TOMITA                                                        
REVDAT   3   13-MAR-24 2ZH6    1       REMARK                                   
REVDAT   2   24-FEB-09 2ZH6    1       VERSN                                    
REVDAT   1   05-AUG-08 2ZH6    0                                                
JRNL        AUTH   Y.TOH,T.NUMATA,K.WATANABE,D.TAKESHITA,O.NUREKI,K.TOMITA      
JRNL        TITL   MOLECULAR BASIS FOR MAINTENANCE OF FIDELITY DURING THE       
JRNL        TITL 2 CCA-ADDING REACTION BY A CCA-ADDING ENZYME                   
JRNL        REF    EMBO J.                       V.  27  1944 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18583961                                                     
JRNL        DOI    10.1038/EMBOJ.2008.124                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3582257.250                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26831                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1303                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4101                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990                       
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 233                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3630                                    
REMARK   3   NUCLEIC ACID ATOMS       : 723                                     
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 104                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : 0.80000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.050                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.110 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.910 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.580 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.480 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 19.64                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : ATP2.PARAM                                     
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  5   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000027966.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-07                          
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26946                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 13.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 59.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.50                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 19.90                              
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   (%): 57.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, 20% PEG 3550, 0.2M TRI       
REMARK 280  -LITHIUM CITRATE, 80MM NH4SO4, PH 7.5, VAPOR DIFFUSION,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      214.47400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       29.01700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       29.01700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      321.71100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       29.01700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       29.01700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      107.23700            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       29.01700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.01700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      321.71100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       29.01700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.01700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      107.23700            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      214.47400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    PHE A   365     O    GLY A   434     7645     2.12            
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    LYS A 118   CB  -  CA  -  C   ANGL. DEV. =  13.0 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    GLU A   4      -73.29    -39.53                                   
REMARK 500    GLU A  96      -59.74   -147.81                                   
REMARK 500    LYS A 105       42.29     39.55                                   
REMARK 500    GLU A 119      116.60     79.56                                   
REMARK 500    PRO A 120       30.20    -69.10                                   
REMARK 500    LYS A 121      -93.60    -57.43                                   
REMARK 500    TYR A 161      -92.06    -70.38                                   
REMARK 500    SER A 250      130.61   -172.95                                   
REMARK 500    LEU A 260      113.66     63.09                                   
REMARK 500    ILE A 262      113.84      8.60                                   
REMARK 500    ARG A 366      105.63     68.61                                   
REMARK 500    LEU A 400       41.85    -95.87                                   
REMARK 500    TYR A 411      139.51    171.27                                   
REMARK 500    PRO A 424       48.14    -75.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500      U B  19         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 438                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4770                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZH1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZH9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZHA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZHB   RELATED DB: PDB                                   
DBREF  2ZH6 A    1   437  UNP    O28126   CCA_ARCFU        1    437             
DBREF  2ZH6 B    1    34  PDB    2ZH6     2ZH6             1     34             
SEQRES   1 B   34    G   G   C   C   C   G   G   G   G   C   G   G   U          
SEQRES   2 B   34    U   C   G   A   U   U   C   C   G   C   C   C   U          
SEQRES   3 B   34    G   G   G   C   C   A   C   U                              
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     MG  A 438       1                                                       
HET    SO4  A4770       5                                                       
HET    ATP  A 501      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  ATP    C10 H16 N5 O13 P3                                            
FORMUL   6  HOH   *104(H2 O)                                                    
HELIX    1   1 LYS A    2  ILE A   15  1                                  14    
HELIX    2   2 ASP A   17  GLU A   37  1                                  21    
HELIX    3   3 GLY A   46  ASN A   51  1                                   6    
HELIX    4   4 SER A   71  LEU A   87  1                                  17    
HELIX    5   5 ARG A  129  GLY A  139  1                                  11    
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  SER A  360  1                                  10    
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 SER A  416  LYS A  422  1                                   7    
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 GLU A  59  PHE A  66 -1  O  PHE A  63   N  VAL A  43           
SHEET    3   A 5 VAL A 107  TYR A 115  1  O  VAL A 112   N  LEU A  64           
SHEET    4   A 5 VAL A 100  VAL A 104 -1  N  VAL A 104   O  VAL A 107           
SHEET    5   A 5 SER A  89  GLU A  91 -1  N  GLU A  91   O  HIS A 101           
SHEET    1   B 4 GLU A 207  LYS A 210  0                                        
SHEET    2   B 4 THR A 199  ASP A 202 -1  N  ASP A 202   O  GLU A 207           
SHEET    3   B 4 PHE A 215  ASP A 218  1  O  PHE A 215   N  ILE A 201           
SHEET    4   B 4 ASP A 221  ASN A 225 -1  O  ARG A 224   N  ASP A 218           
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  PHE A 279   O  PHE A 331           
SHEET    4   C 4 GLU A 413  ILE A 415 -1  O  GLU A 413   N  LYS A 282           
SHEET    1   D 3 VAL A 341  GLN A 348  0                                        
SHEET    2   D 3 ARG A 373  MET A 379 -1  O  TRP A 374   N  PRO A 347           
SHEET    3   D 3 PHE A 368  GLU A 370 -1  N  GLU A 370   O  ARG A 373           
SITE     1 AC1  2 GLU A  59  ASP A  61                                          
SITE     1 AC2  3 ARG A 299  ARG A 302  LYS A 303                               
SITE     1 AC3 10 GLY A  46  SER A  47  ARG A  50  GLU A  59                    
SITE     2 AC3 10 ASP A  61  THR A 130  HIS A 133  LYS A 152                    
SITE     3 AC3 10 TYR A 161  ARG A 224                                          
CRYST1   58.034   58.034  428.948  90.00  90.00  90.00 P 43 21 2     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      0.017231  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017231  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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