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Database: PDB
Entry: 1L4U
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Original site: 1L4U 
HEADER    TRANSFERASE                             05-MAR-02   1L4U              
TITLE     CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS 
TITLE    2 IN COMPLEX WITH MGADP AND PT(II) AT 1.8 ANGSTROM RESOLUTION          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SHIKIMATE KINASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SK;                                                         
COMPND   5 EC: 2.7.1.71;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: AROK;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-17B                                   
KEYWDS    SHIKIMATE PATHWAY, SHIKIMATE KINASE, PHORSPHORYL TRANSFER, DRUG       
KEYWDS   2 DESIGN, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.GU,L.RESHETNIKOVA,Y.LI,Y.WU,H.YAN,S.SINGH,X.JI                      
REVDAT   5   30-AUG-23 1L4U    1       AUTHOR JRNL   REMARK LINK                
REVDAT   4   29-MAR-17 1L4U    1       VERSN                                    
REVDAT   3   24-FEB-09 1L4U    1       VERSN                                    
REVDAT   2   01-APR-03 1L4U    1       JRNL                                     
REVDAT   1   12-JUN-02 1L4U    0                                                
JRNL        AUTH   Y.GU,L.RESHETNIKOVA,Y.LI,Y.WU,H.YAN,S.SINGH,X.JI             
JRNL        TITL   CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM     
JRNL        TITL 2 TUBERCULOSIS REVEALS THE DYNAMIC ROLE OF THE LID DOMAIN IN   
JRNL        TITL 3 CATALYSIS.                                                   
JRNL        REF    J.MOL.BIOL.                   V. 319   779 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12054870                                                     
JRNL        DOI    10.1016/S0022-2836(02)00339-X                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 272778.210                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 20594                          
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) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 999                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1029                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : 0.3026                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.54                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.67000                                              
REMARK   3    B22 (A**2) : 2.67000                                              
REMARK   3    B33 (A**2) : -5.34000                                             
REMARK   3    B12 (A**2) : -0.32000                                             
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) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.750                           
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) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.990 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.970 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 53.77                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PARAM.ADP                                      
REMARK   3  PARAMETER FILE  5  : PARAM.HEP                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : TOPOL.ADP                                      
REMARK   3  TOPOLOGY FILE  5   : TOPOL.HEP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1L4U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000015646.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-99                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07223,1.07186,1.06268,1.08121    
REMARK 200  MONOCHROMATOR                  : SILICON (111) CHANNEL              
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20594                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.640                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1340                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.86                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHOLORIDE, SODIUM    
REMARK 280  CHLORIDE, ADENOSINE-5'-DIPHOSPHATE, SHIKIMIC ACID, NAHEPES,         
REMARK 280  PLATINUM POTASSIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 288K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.28000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.64000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.64000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.28000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     1                                                      
REMARK 465     GLN A   167                                                      
REMARK 465     VAL A   168                                                      
REMARK 465     PRO A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     PRO A   171                                                      
REMARK 465     SER A   172                                                      
REMARK 465     GLU A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     THR A   176                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A 115    CB   OG1  CG2                                       
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   OG   SER A    16     O    HOH A   394              2.11            
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    THR A  51      -76.50    -67.82                                   
REMARK 500    THR A 115       32.88    -78.00                                   
REMARK 500    VAL A 116       82.08     72.01                                   
REMARK 500    LEU A 120       57.12   -115.60                                   
REMARK 500    ASP A 124       61.73     36.17                                   
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 190  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  16   OG                                                     
REMARK 620 2 ADP A 180   O2B  74.0                                              
REMARK 620 3 HOH A 296   O    62.4  70.1                                        
REMARK 620 4 HOH A 350   O   113.1 119.1 169.3                                  
REMARK 620 5 HOH A 374   O   134.7  98.9  73.1 109.2                            
REMARK 620 6 HOH A 393   O    80.0 146.8  79.8  89.9  84.9                      
REMARK 620 7 HOH A 394   O    43.0  96.0 104.4  70.2 162.7  77.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PT A 189  PT                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET A 133   SD                                                     
REMARK 620 2 EPE A 181   N4  172.5                                              
REMARK 620 3 EPE A 181   O8  109.2  71.0                                        
REMARK 620 4  CL A 195  CL    65.4 121.3  76.6                                  
REMARK 620 5  CL A 196  CL    83.9  91.5 141.8 139.2                            
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 PT A 189                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 190                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 191                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 192                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 193                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 194                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 195                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 196                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 180                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 181                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L4Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM             
REMARK 900 TUBERCULOSIS IN COMPLEX WITH MGADP AT 2.0 ANGSTROM RESOLUTION        
REMARK 900 RELATED ID: 1SHK   RELATED DB: PDB                                   
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA     
REMARK 900 CHRYSANTHEMI                                                         
REMARK 900 RELATED ID: 2SHK   RELATED DB: PDB                                   
REMARK 900 THE THREE-DIMENSIONAL STRUCTURE OF SHIKIMATE KINASE FROM ERWINIA     
REMARK 900 CHRYSANTHEMI COMPLEXED WITH ADP                                      
REMARK 900 RELATED ID: 1E6C   RELATED DB: PDB                                   
REMARK 900 K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI            
DBREF  1L4U A    1   176  UNP    P0A4Z2   AROK_MYCTU       1    176             
SEQRES   1 A  176  MET ALA PRO LYS ALA VAL LEU VAL GLY LEU PRO GLY SER          
SEQRES   2 A  176  GLY LYS SER THR ILE GLY ARG ARG LEU ALA LYS ALA LEU          
SEQRES   3 A  176  GLY VAL GLY LEU LEU ASP THR ASP VAL ALA ILE GLU GLN          
SEQRES   4 A  176  ARG THR GLY ARG SER ILE ALA ASP ILE PHE ALA THR ASP          
SEQRES   5 A  176  GLY GLU GLN GLU PHE ARG ARG ILE GLU GLU ASP VAL VAL          
SEQRES   6 A  176  ARG ALA ALA LEU ALA ASP HIS ASP GLY VAL LEU SER LEU          
SEQRES   7 A  176  GLY GLY GLY ALA VAL THR SER PRO GLY VAL ARG ALA ALA          
SEQRES   8 A  176  LEU ALA GLY HIS THR VAL VAL TYR LEU GLU ILE SER ALA          
SEQRES   9 A  176  ALA GLU GLY VAL ARG ARG THR GLY GLY ASN THR VAL ARG          
SEQRES  10 A  176  PRO LEU LEU ALA GLY PRO ASP ARG ALA GLU LYS TYR ARG          
SEQRES  11 A  176  ALA LEU MET ALA LYS ARG ALA PRO LEU TYR ARG ARG VAL          
SEQRES  12 A  176  ALA THR MET ARG VAL ASP THR ASN ARG ARG ASN PRO GLY          
SEQRES  13 A  176  ALA VAL VAL ARG HIS ILE LEU SER ARG LEU GLN VAL PRO          
SEQRES  14 A  176  SER PRO SER GLU ALA ALA THR                                  
HET     PT  A 189       1                                                       
HET     MG  A 190       1                                                       
HET     CL  A 191       1                                                       
HET     CL  A 192       1                                                       
HET     CL  A 193       1                                                       
HET     CL  A 194       1                                                       
HET     CL  A 195       1                                                       
HET     CL  A 196       1                                                       
HET    ADP  A 180      27                                                       
HET    EPE  A 181      15                                                       
HETNAM      PT PLATINUM (II) ION                                                
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   2   PT    PT 2+                                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   CL    6(CL 1-)                                                     
FORMUL  10  ADP    C10 H15 N5 O10 P2                                            
FORMUL  11  EPE    C8 H18 N2 O4 S                                               
FORMUL  12  HOH   *194(H2 O)                                                    
HELIX    1   1 GLY A   14  GLY A   27  1                                  14    
HELIX    2   2 THR A   33  GLY A   42  1                                  10    
HELIX    3   3 SER A   44  ASP A   52  1                                   9    
HELIX    4   4 GLY A   53  HIS A   72  1                                  20    
HELIX    5   5 GLY A   81  THR A   84  5                                   4    
HELIX    6   6 SER A   85  ALA A   93  1                                   9    
HELIX    7   7 SER A  103  THR A  111  1                                   9    
HELIX    8   8 ARG A  117  ALA A  121  5                                   5    
HELIX    9   9 ASP A  124  ALA A  144  1                                  21    
HELIX   10  10 ASN A  154  LEU A  166  1                                  13    
SHEET    1   A 5 LEU A  30  ASP A  32  0                                        
SHEET    2   A 5 VAL A  75  SER A  77  1  O  VAL A  75   N  LEU A  31           
SHEET    3   A 5 ALA A   5  VAL A   8  1  N  LEU A   7   O  LEU A  76           
SHEET    4   A 5 VAL A  97  GLU A 101  1  O  VAL A  98   N  VAL A   6           
SHEET    5   A 5 MET A 146  ASP A 149  1  O  MET A 146   N  TYR A  99           
LINK         OG  SER A  16                MG    MG A 190     1555   1555  2.57  
LINK         SD  MET A 133                PT    PT A 189     1555   1555  2.46  
LINK         O2B ADP A 180                MG    MG A 190     1555   1555  2.39  
LINK         N4  EPE A 181                PT    PT A 189     1555   1555  2.41  
LINK         O8  EPE A 181                PT    PT A 189     1555   1555  2.61  
LINK        PT    PT A 189                CL    CL A 195     1555   1555  2.24  
LINK        PT    PT A 189                CL    CL A 196     1555   1555  2.40  
LINK        MG    MG A 190                 O   HOH A 296     1555   1555  2.94  
LINK        MG    MG A 190                 O   HOH A 350     1555   1555  2.77  
LINK        MG    MG A 190                 O   HOH A 374     1555   1555  2.52  
LINK        MG    MG A 190                 O   HOH A 393     1555   1555  2.37  
LINK        MG    MG A 190                 O   HOH A 394     1555   1555  3.06  
SITE     1 AC1  4 MET A 133  EPE A 181   CL A 195   CL A 196                    
SITE     1 AC2  7 SER A  16  ADP A 180  HOH A 296  HOH A 350                    
SITE     2 AC2  7 HOH A 374  HOH A 393  HOH A 394                               
SITE     1 AC3  3 ARG A  66  ARG A 160  HOH A 204                               
SITE     1 AC4  4 GLY A  29  HIS A  72  GLY A  74  HOH A 235                    
SITE     1 AC5  4 PRO A  11  LYS A  15  GLY A  80  HOH A 367                    
SITE     1 AC6  4 LYS A  24  ARG A  66  ALA A  90  ARG A 109                    
SITE     1 AC7  4 MET A 133  EPE A 181   PT A 189  HOH A 321                    
SITE     1 AC8  4 ARG A 130  MET A 133  EPE A 181   PT A 189                    
SITE     1 AC9 18 LEU A  10  PRO A  11  GLY A  12  SER A  13                    
SITE     2 AC9 18 GLY A  14  LYS A  15  SER A  16  THR A  17                    
SITE     3 AC9 18 ARG A 110  ARG A 117  ARG A 153  PRO A 155                    
SITE     4 AC9 18  MG A 190  HOH A 213  HOH A 216  HOH A 256                    
SITE     5 AC9 18 HOH A 296  HOH A 356                                          
SITE     1 BC1 10 THR A  96  ARG A 130  MET A 133  THR A 145                    
SITE     2 BC1 10 MET A 146  ARG A 165   PT A 189   CL A 195                    
SITE     3 BC1 10  CL A 196  HOH A 378                                          
CRYST1   63.830   63.830   91.920  90.00  90.00 120.00 P 32 2 1      6          
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      0.015666  0.009045  0.000000        0.00000                         
SCALE2      0.000000  0.018089  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010879        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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