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Database: PDB
Entry: 4CRJ
LinkDB: 4CRJ
Original site: 4CRJ 
HEADER    TRANSFERASE                             27-FEB-14   4CRJ              
TITLE     STAPHYLOCOCCUS AUREUS 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-              
TITLE    2 PYROPHOSPHOKINASE IN COMPLEX WITH AMPCPP AND AN INHIBITOR            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE (HPPK);
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.6.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRANSFERASE, FOLATE, STRUCTURE-BASED DRUG DESIGN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.DENNIS,J.D.SWARBRICK,T.S.PEAT                                     
REVDAT   3   08-MAY-19 4CRJ    1       REMARK                                   
REVDAT   2   28-DEC-16 4CRJ    1       HETNAM HETATM CONECT                     
REVDAT   1   28-JAN-15 4CRJ    0                                                
JRNL        AUTH   M.L.DENNIS,S.CHHABRA,Z.WANG,A.DEBONO,O.DOLEZAL,J.NEWMAN,     
JRNL        AUTH 2 N.P.PITCHER,R.RAHMANI,B.CLEARY,N.BARLOW,M.HATTARKI,B.GRAHAM, 
JRNL        AUTH 3 T.S.PEAT,J.B.BAELL,J.D.SWARBRICK                             
JRNL        TITL   STRUCTURE-BASED DESIGN AND DEVELOPMENT OF FUNCTIONALIZED     
JRNL        TITL 2 MERCAPTOGUANINE DERIVATIVES AS INHIBITORS OF THE FOLATE      
JRNL        TITL 3 BIOSYNTHESIS PATHWAY ENZYME                                  
JRNL        TITL 4 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM     
JRNL        TITL 5 STAPHYLOCOCCUS AUREUS.                                       
JRNL        REF    J.MED.CHEM.                   V.  57  9612 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25357262                                                     
JRNL        DOI    10.1021/JM501417F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13074                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 685                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 929                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 43                           
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1273                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 83                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 0.89000                                              
REMARK   3    B33 (A**2) : -2.89000                                             
REMARK   3    B12 (A**2) : 0.89000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.146         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.080         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1376 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1315 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1878 ; 1.362 ; 2.043       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3034 ; 0.769 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   162 ; 6.344 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    61 ;34.750 ;24.918       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   244 ;12.906 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;14.001 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   212 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1549 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   289 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4CRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059856.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95370                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 21.50                              
REMARK 200  R MERGE                    (I) : 0.22000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 19.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.02000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
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: PDB ENTRY 4AD6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 7.5 MG/ML PLUS 1MM AMPCPP PLUS   
REMARK 280  1MM INHIBITOR, AMMONIUM SULFATE 0.275 M, PEG4000 22.1% W/V,         
REMARK 280  SITTING DROP, 281 K, PH 8, VAPOR DIFFUSION, SITTING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       17.39100            
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       34.78200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       26.08650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       43.47750            
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        8.69550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
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  50       56.77    -92.05                                   
REMARK 500    ALA A 132       34.93   -144.54                                   
REMARK 500    TYR A 157      -51.34   -121.46                                   
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 A1160  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC A1159   O1A                                                    
REMARK 620 2 APC A1159   O1B  89.1                                              
REMARK 620 3 ASP A  95   OD1  92.4  91.8                                        
REMARK 620 4 ASP A  97   OD1 171.9  98.7  89.6                                  
REMARK 620 5 HOH A2047   O    94.7  86.8 172.8  83.6                            
REMARK 620 6 HOH A2034   O    86.3 175.3  88.3  86.0  93.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1161  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC A1159   O1B                                                    
REMARK 620 2 APC A1159   O1G  88.9                                              
REMARK 620 3 ASP A  95   OD2  85.5 174.3                                        
REMARK 620 4 ASP A  97   OD2 102.3  93.9  87.6                                  
REMARK 620 5 HOH A2045   O    87.9  89.0  90.4 169.4                            
REMARK 620 6 HOH A2046   O   171.1  95.9  89.7  84.9  84.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 1159                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1162                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YH5 A 1163                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE SITE AT THE N-              
REMARK 999 TERMINUS                                                             
DBREF  4CRJ A    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
SEQADV 4CRJ GLY A   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CRJ SER A   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CRJ HIS A    0  UNP  C8MLE4              EXPRESSION TAG                 
SEQRES   1 A  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 A  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 A  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 A  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 A  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 A  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 A  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 A  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 A  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 A  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 A  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 A  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER          
SEQRES  13 A  161  VAL LYS ARG TYR LYS                                          
HET    APC  A1159      31                                                       
HET     MG  A1160       1                                                       
HET     MG  A1161       1                                                       
HET    NO3  A1162       4                                                       
HET    YH5  A1163      23                                                       
HETNAM     APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NO3 NITRATE ION                                                      
HETNAM     YH5 2-AMINO-8-{[2-(4-METHOXYPHENYL)-2-OXOETHYL]SULFANYL}-1,          
HETNAM   2 YH5  9-DIHYDRO-6H-PURIN-6-ONE                                        
HETSYN     APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE                    
FORMUL   2  APC    C11 H18 N5 O12 P3                                            
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  NO3    N O3 1-                                                      
FORMUL   6  YH5    C14 H13 N5 O3 S                                              
FORMUL   7  HOH   *83(H2 O)                                                     
HELIX    1   1 ASP A   14  TYR A   29  1                                  16    
HELIX    2   2 THR A   66  LEU A   81  1                                  16    
HELIX    3   3 ARG A  117  GLU A  120  5                                   4    
HELIX    4   4 ARG A  121  ALA A  133  1                                  13    
HELIX    5   5 VAL A  144  VAL A  148  1                                   5    
SHEET    1  AA 2 ILE A  32  ILE A  37  0                                        
SHEET    2  AA 2 PHE A  54  THR A  63 -1  O  GLU A  60   N  SER A  35           
SHEET    1  AB 5 ASP A  95  TYR A 101  0                                        
SHEET    2  AB 5 ILE A   2  SER A  10 -1  O  TYR A   5   N  LEU A  99           
SHEET    3  AB 5 PHE A  54  THR A  63 -1  O  LEU A  55   N  SER A  10           
SHEET    4  AB 5 ILE A  40  THR A  43 -1  O  TYR A  41   N  ASN A  56           
SHEET    5  AB 5 VAL A 154  LYS A 158 -1  O  LYS A 155   N  GLU A  42           
SHEET    1  AC 4 ASP A  95  TYR A 101  0                                        
SHEET    2  AC 4 ILE A   2  SER A  10 -1  O  TYR A   5   N  LEU A  99           
SHEET    3  AC 4 PHE A  54  THR A  63 -1  O  LEU A  55   N  SER A  10           
SHEET    4  AC 4 ILE A  32  ILE A  37 -1  O  SER A  33   N  GLN A  62           
SHEET    1  AD 2 ILE A 106  LEU A 108  0                                        
SHEET    2  AD 2 LEU A 111  VAL A 113 -1  O  LEU A 111   N  LEU A 108           
SHEET    1  AE 2 VAL A 136  GLU A 137  0                                        
SHEET    2  AE 2 LEU A 142  LYS A 143 -1  O  LEU A 142   N  GLU A 137           
LINK         O1A APC A1159                MG    MG A1160     1555   1555  2.08  
LINK         O1B APC A1159                MG    MG A1160     1555   1555  2.06  
LINK         O1B APC A1159                MG    MG A1161     1555   1555  2.18  
LINK         O1G APC A1159                MG    MG A1161     1555   1555  2.07  
LINK        MG    MG A1160                 OD1 ASP A  95     1555   1555  2.15  
LINK        MG    MG A1160                 OD1 ASP A  97     1555   1555  2.11  
LINK        MG    MG A1160                 O   HOH A2047     1555   1555  2.07  
LINK        MG    MG A1160                 O   HOH A2034     1555   1555  2.10  
LINK        MG    MG A1161                 OD2 ASP A  95     1555   1555  2.17  
LINK        MG    MG A1161                 OD2 ASP A  97     1555   1555  2.05  
LINK        MG    MG A1161                 O   HOH A2045     1555   1555  2.11  
LINK        MG    MG A1161                 O   HOH A2046     1555   1555  2.15  
CISPEP   1 VAL A  113    PRO A  114          0        -4.83                     
SITE     1 AC1 23 LEU A  71  ARG A  83  ARG A  88  ARG A  92                    
SITE     2 AC1 23 ASP A  95  ASP A  97  ILE A  98  LYS A 110                    
SITE     3 AC1 23 LEU A 111  SER A 112  HIS A 115  ARG A 117                    
SITE     4 AC1 23 ARG A 121   MG A1160   MG A1161  HOH A2033                    
SITE     5 AC1 23 HOH A2034  HOH A2039  HOH A2040  HOH A2041                    
SITE     6 AC1 23 HOH A2045  HOH A2047  HOH A2083                               
SITE     1 AC2  6 ASP A  95  ASP A  97  APC A1159   MG A1161                    
SITE     2 AC2  6 HOH A2034  HOH A2047                                          
SITE     1 AC3  6 ASP A  95  ASP A  97  APC A1159   MG A1160                    
SITE     2 AC3  6 HOH A2045  HOH A2046                                          
SITE     1 AC4  6 ILE A  12  ARG A  83  ILE A  84  ARG A  85                    
SITE     2 AC4  6 ARG A  92  THR A  93                                          
SITE     1 AC5 14 THR A  43  ALA A  44  PRO A  45  VAL A  46                    
SITE     2 AC5 14 GLY A  47  PHE A  54  ASN A  56  GLU A 104                    
SITE     3 AC5 14 MET A 105  ILE A 106  ARG A 121  PHE A 123                    
SITE     4 AC5 14 HOH A2044  HOH A2045                                          
CRYST1   82.480   82.480   52.173  90.00  90.00 120.00 P 61          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      0.012124  0.007000  0.000000        0.00000                         
SCALE2      0.000000  0.014000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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