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Database: PDB
Entry: 3GO6
LinkDB: 3GO6
Original site: 3GO6 
HEADER    TRANSFERASE                             18-MAR-09   3GO6              
TITLE     CRYSTAL STRUCTURE OF M. TUBERCULOSIS RIBOKINASE (RV2436) IN COMPLEX   
TITLE    2 WITH RIBOSE AND AMP-PNP                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOKINASE RBSK;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.15;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RBSK, RV2436;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    PHOSPHOFRUCTOKINASE, CARBOHYDRATE KINASE, KINASE, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.I.MASTERS,Y.SUN,Y.WANG,W.B.PARKER,R.LI                              
REVDAT   5   21-FEB-24 3GO6    1       HETSYN                                   
REVDAT   4   29-JUL-20 3GO6    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   24-JAN-18 3GO6    1       JRNL                                     
REVDAT   2   01-NOV-17 3GO6    1       REMARK                                   
REVDAT   1   31-MAR-10 3GO6    0                                                
JRNL        AUTH   E.I.MASTERS,Y.SUN,Y.WANG,W.B.PARKER,R.LI                     
JRNL        TITL   CRYSTAL STRUCTURE AND BIOCHEMICAL CHARACTERIZATION OF        
JRNL        TITL 2 M.TUBERCULOSIS RIBOKINASE (RV2436)                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 52460                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2674                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.98                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3587                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 217                          
REMARK   3   BIN FREE R VALUE                    : 0.2410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4010                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 507                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : 0.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.80000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.131         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.080         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.768         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4121 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5677 ; 1.300 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   572 ; 5.681 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   148 ;35.606 ;23.649       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   522 ;11.649 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;16.434 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   698 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3185 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1906 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2874 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   390 ; 0.134 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    78 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.141 ; 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):  2917 ; 0.855 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4564 ; 1.450 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1314 ; 2.173 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1113 ; 3.690 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052105.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : ROSENBAUM-ROCK MONOCHROMATOR       
REMARK 200                                   HIGH-RESOLUTION DOUBLE-CRYSTAL     
REMARK 200                                   SI (111) SAGITTAL FOCUSING.        
REMARK 200                                   ROSENBAUM-ROCK VERTICAL FOCUSING   
REMARK 200                                   MIRROR.                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.1460                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13900                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM/POTASSIUM PHOSPHATE, 0.1    
REMARK 280  M BIS-TRIS PROPANE, 16% PEG 3350, PH 6.5, VAPOR DIFFUSION,          
REMARK 280  TEMPERATURE 295K                                                    
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       39.21200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       39.21200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       58.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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        0.00000            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     ASN A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     MET B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     ARG B   300                                                      
REMARK 465     HIS B   301                                                      
REMARK 465     ASN B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     SER B   304                                                      
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    ASP A  75       48.55   -101.43                                   
REMARK 500    ASP A 176      105.42    -56.28                                   
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 306  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 236   O                                                      
REMARK 620 2 ALA A 238   O    87.5                                              
REMARK 620 3 ALA A 276   O    85.1 123.0                                        
REMARK 620 4 VAL A 279   O    87.3 152.7  83.1                                  
REMARK 620 5 GLY A 281   O   136.5  82.3 135.1  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 306  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 236   O                                                      
REMARK 620 2 ALA B 238   O    88.4                                              
REMARK 620 3 ALA B 276   O    79.9 118.7                                        
REMARK 620 4 VAL B 279   O    85.7 156.2  83.0                                  
REMARK 620 5 GLY B 281   O   141.4  82.0 137.0  88.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GO7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH RIBOSE ONLY.                                   
REMARK 900 RELATED ID: 1RKD   RELATED DB: PDB                                   
REMARK 900 RIBOKINASE STRUCTURE FROM E.COLI.                                    
REMARK 900 RELATED ID: 2FV7   RELATED DB: PDB                                   
REMARK 900 RIBOKINASE STRUCTURE FROM HUMAN.                                     
DBREF  3GO6 A    2   304  UNP    P71913   P71913_MYCTU     2    304             
DBREF  3GO6 B    2   304  UNP    P71913   P71913_MYCTU     2    304             
SEQADV 3GO6 MET A   -5  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A   -4  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A   -3  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A   -2  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A   -1  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A    0  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS A    1  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 MET B   -5  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B   -4  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B   -3  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B   -2  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B   -1  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B    0  UNP  P71913              EXPRESSION TAG                 
SEQADV 3GO6 HIS B    1  UNP  P71913              EXPRESSION TAG                 
SEQRES   1 A  310  MET HIS HIS HIS HIS HIS HIS ALA ASN ALA SER GLU THR          
SEQRES   2 A  310  ASN VAL GLY PRO MET ALA PRO ARG VAL CYS VAL VAL GLY          
SEQRES   3 A  310  SER VAL ASN MET ASP LEU THR PHE VAL VAL ASP ALA LEU          
SEQRES   4 A  310  PRO ARG PRO GLY GLU THR VAL LEU ALA ALA SER LEU THR          
SEQRES   5 A  310  ARG THR PRO GLY GLY LYS GLY ALA ASN GLN ALA VAL ALA          
SEQRES   6 A  310  ALA ALA ARG ALA GLY ALA GLN VAL GLN PHE SER GLY ALA          
SEQRES   7 A  310  PHE GLY ASP ASP PRO ALA ALA ALA GLN LEU ARG ALA HIS          
SEQRES   8 A  310  LEU ARG ALA ASN ALA VAL GLY LEU ASP ARG THR VAL THR          
SEQRES   9 A  310  VAL PRO GLY PRO SER GLY THR ALA ILE ILE VAL VAL ASP          
SEQRES  10 A  310  ALA SER ALA GLU ASN THR VAL LEU VAL ALA PRO GLY ALA          
SEQRES  11 A  310  ASN ALA HIS LEU THR PRO VAL PRO SER ALA VAL ALA ASN          
SEQRES  12 A  310  CYS ASP VAL LEU LEU THR GLN LEU GLU ILE PRO VAL ALA          
SEQRES  13 A  310  THR ALA LEU ALA ALA ALA ARG ALA ALA GLN SER ALA ASP          
SEQRES  14 A  310  ALA VAL VAL MET VAL ASN ALA SER PRO ALA GLY GLN ASP          
SEQRES  15 A  310  ARG SER SER LEU GLN ASP LEU ALA ALA ILE ALA ASP VAL          
SEQRES  16 A  310  VAL ILE ALA ASN GLU HIS GLU ALA ASN ASP TRP PRO SER          
SEQRES  17 A  310  PRO PRO THR HIS PHE VAL ILE THR LEU GLY VAL ARG GLY          
SEQRES  18 A  310  ALA ARG TYR VAL GLY ALA ASP GLY VAL PHE GLU VAL PRO          
SEQRES  19 A  310  ALA PRO THR VAL THR PRO VAL ASP THR ALA GLY ALA GLY          
SEQRES  20 A  310  ASP VAL PHE ALA GLY VAL LEU ALA ALA ASN TRP PRO ARG          
SEQRES  21 A  310  ASN PRO GLY SER PRO ALA GLU ARG LEU ARG ALA LEU ARG          
SEQRES  22 A  310  ARG ALA CYS ALA ALA GLY ALA LEU ALA THR LEU VAL SER          
SEQRES  23 A  310  GLY VAL GLY ASP CYS ALA PRO ALA ALA ALA ALA ILE ASP          
SEQRES  24 A  310  ALA ALA LEU ARG ALA ASN ARG HIS ASN GLY SER                  
SEQRES   1 B  310  MET HIS HIS HIS HIS HIS HIS ALA ASN ALA SER GLU THR          
SEQRES   2 B  310  ASN VAL GLY PRO MET ALA PRO ARG VAL CYS VAL VAL GLY          
SEQRES   3 B  310  SER VAL ASN MET ASP LEU THR PHE VAL VAL ASP ALA LEU          
SEQRES   4 B  310  PRO ARG PRO GLY GLU THR VAL LEU ALA ALA SER LEU THR          
SEQRES   5 B  310  ARG THR PRO GLY GLY LYS GLY ALA ASN GLN ALA VAL ALA          
SEQRES   6 B  310  ALA ALA ARG ALA GLY ALA GLN VAL GLN PHE SER GLY ALA          
SEQRES   7 B  310  PHE GLY ASP ASP PRO ALA ALA ALA GLN LEU ARG ALA HIS          
SEQRES   8 B  310  LEU ARG ALA ASN ALA VAL GLY LEU ASP ARG THR VAL THR          
SEQRES   9 B  310  VAL PRO GLY PRO SER GLY THR ALA ILE ILE VAL VAL ASP          
SEQRES  10 B  310  ALA SER ALA GLU ASN THR VAL LEU VAL ALA PRO GLY ALA          
SEQRES  11 B  310  ASN ALA HIS LEU THR PRO VAL PRO SER ALA VAL ALA ASN          
SEQRES  12 B  310  CYS ASP VAL LEU LEU THR GLN LEU GLU ILE PRO VAL ALA          
SEQRES  13 B  310  THR ALA LEU ALA ALA ALA ARG ALA ALA GLN SER ALA ASP          
SEQRES  14 B  310  ALA VAL VAL MET VAL ASN ALA SER PRO ALA GLY GLN ASP          
SEQRES  15 B  310  ARG SER SER LEU GLN ASP LEU ALA ALA ILE ALA ASP VAL          
SEQRES  16 B  310  VAL ILE ALA ASN GLU HIS GLU ALA ASN ASP TRP PRO SER          
SEQRES  17 B  310  PRO PRO THR HIS PHE VAL ILE THR LEU GLY VAL ARG GLY          
SEQRES  18 B  310  ALA ARG TYR VAL GLY ALA ASP GLY VAL PHE GLU VAL PRO          
SEQRES  19 B  310  ALA PRO THR VAL THR PRO VAL ASP THR ALA GLY ALA GLY          
SEQRES  20 B  310  ASP VAL PHE ALA GLY VAL LEU ALA ALA ASN TRP PRO ARG          
SEQRES  21 B  310  ASN PRO GLY SER PRO ALA GLU ARG LEU ARG ALA LEU ARG          
SEQRES  22 B  310  ARG ALA CYS ALA ALA GLY ALA LEU ALA THR LEU VAL SER          
SEQRES  23 B  310  GLY VAL GLY ASP CYS ALA PRO ALA ALA ALA ALA ILE ASP          
SEQRES  24 B  310  ALA ALA LEU ARG ALA ASN ARG HIS ASN GLY SER                  
HET    RIB  A 305      10                                                       
HET     MG  A 306       1                                                       
HET    ADP  B 305      27                                                       
HET     MG  B 306       1                                                       
HETNAM     RIB ALPHA-D-RIBOFURANOSE                                             
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     RIB ALPHA-D-RIBOSE; D-RIBOSE; RIBOSE                                 
FORMUL   3  RIB    C5 H10 O5                                                    
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7  HOH   *507(H2 O)                                                    
HELIX    1   1 GLY A   51  ALA A   63  1                                  13    
HELIX    2   2 ASP A   76  ASN A   89  1                                  14    
HELIX    3   3 PRO A  122  LEU A  128  5                                   7    
HELIX    4   4 PRO A  148  ALA A  162  1                                  15    
HELIX    5   5 ASP A  176  ALA A  187  1                                  12    
HELIX    6   6 GLU A  194  TRP A  200  1                                   7    
HELIX    7   7 GLY A  212  ARG A  214  5                                   3    
HELIX    8   8 GLY A  239  TRP A  252  1                                  14    
HELIX    9   9 SER A  258  THR A  277  1                                  20    
HELIX   10  10 ALA A  288  ALA A  298  1                                  11    
HELIX   11  11 GLY B   51  ALA B   63  1                                  13    
HELIX   12  12 ASP B   76  ASN B   89  1                                  14    
HELIX   13  13 PRO B  122  LEU B  128  5                                   7    
HELIX   14  14 VAL B  131  ALA B  136  5                                   6    
HELIX   15  15 PRO B  148  ALA B  162  1                                  15    
HELIX   16  16 ARG B  177  SER B  179  5                                   3    
HELIX   17  17 LEU B  180  ALA B  187  1                                   8    
HELIX   18  18 GLU B  194  ASP B  199  1                                   6    
HELIX   19  19 GLY B  212  ARG B  214  5                                   3    
HELIX   20  20 GLY B  239  TRP B  252  1                                  14    
HELIX   21  21 SER B  258  THR B  277  1                                  20    
HELIX   22  22 ALA B  288  ALA B  298  1                                  11    
SHEET    1   A 8 GLN A  66  SER A  70  0                                        
SHEET    2   A 8 ARG A  15  VAL A  19  1  N  VAL A  18   O  GLN A  68           
SHEET    3   A 8 VAL A 140  THR A 143  1  O  LEU A 142   N  CYS A  17           
SHEET    4   A 8 VAL A 165  ASN A 169  1  O  ASN A 169   N  THR A 143           
SHEET    5   A 8 VAL A 189  ASN A 193  1  O  ILE A 191   N  VAL A 168           
SHEET    6   A 8 HIS A 206  THR A 210  1  O  VAL A 208   N  VAL A 190           
SHEET    7   A 8 ALA A 216  GLY A 220 -1  O  ARG A 217   N  ILE A 209           
SHEET    8   A 8 GLY A 223  VAL A 227 -1  O  PHE A 225   N  TYR A 218           
SHEET    1   B 4 SER A  44  GLY A  50  0                                        
SHEET    2   B 4 ASN A  23  VAL A  29 -1  N  ASP A  25   O  THR A  48           
SHEET    3   B 4 GLY A 104  VAL A 110  1  O  ILE A 108   N  PHE A  28           
SHEET    4   B 4 ASN A 116  ALA A 121 -1  O  LEU A 119   N  ILE A 107           
SHEET    1   C 2 ALA A  72  PHE A  73  0                                        
SHEET    2   C 2 VAL A  97  THR A  98  1  O  VAL A  97   N  PHE A  73           
SHEET    1   D 8 GLN B  66  SER B  70  0                                        
SHEET    2   D 8 ARG B  15  VAL B  19  1  N  VAL B  18   O  GLN B  68           
SHEET    3   D 8 VAL B 140  GLN B 144  1  O  LEU B 142   N  CYS B  17           
SHEET    4   D 8 VAL B 165  ASN B 169  1  O  VAL B 165   N  LEU B 141           
SHEET    5   D 8 VAL B 189  ASN B 193  1  O  VAL B 189   N  VAL B 168           
SHEET    6   D 8 HIS B 206  THR B 210  1  O  VAL B 208   N  VAL B 190           
SHEET    7   D 8 ALA B 216  GLY B 220 -1  O  ARG B 217   N  ILE B 209           
SHEET    8   D 8 GLY B 223  VAL B 227 -1  O  VAL B 227   N  ALA B 216           
SHEET    1   E 4 SER B  44  GLY B  50  0                                        
SHEET    2   E 4 ASN B  23  VAL B  29 -1  N  ASP B  25   O  THR B  48           
SHEET    3   E 4 GLY B 104  VAL B 110  1  O  ALA B 106   N  LEU B  26           
SHEET    4   E 4 ASN B 116  ALA B 121 -1  O  LEU B 119   N  ILE B 107           
SHEET    1   F 2 ALA B  72  PHE B  73  0                                        
SHEET    2   F 2 VAL B  97  THR B  98  1  O  VAL B  97   N  PHE B  73           
LINK         O   ASP A 236                MG    MG A 306     1555   1555  2.77  
LINK         O   ALA A 238                MG    MG A 306     1555   1555  2.78  
LINK         O   ALA A 276                MG    MG A 306     1555   1555  2.82  
LINK         O   VAL A 279                MG    MG A 306     1555   1555  2.67  
LINK         O   GLY A 281                MG    MG A 306     1555   1555  2.76  
LINK         O   ASP B 236                MG    MG B 306     1555   1555  2.79  
LINK         O   ALA B 238                MG    MG B 306     1555   1555  2.62  
LINK         O   ALA B 276                MG    MG B 306     1555   1555  2.78  
LINK         O   VAL B 279                MG    MG B 306     1555   1555  2.55  
LINK         O   GLY B 281                MG    MG B 306     1555   1555  2.79  
CISPEP   1 SER A  171    PRO A  172          0        -0.30                     
CISPEP   2 ASN A  255    PRO A  256          0        -0.59                     
CISPEP   3 SER B  171    PRO B  172          0         2.67                     
CISPEP   4 ASN B  255    PRO B  256          0        -0.79                     
CRYST1   78.424  117.900   91.571  90.00 113.93  90.00 C 1 2 1       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      0.012751  0.000000  0.005660        0.00000                         
SCALE2      0.000000  0.008482  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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