GenomeNet

Database: PDB
Entry: 5ETV
LinkDB: 5ETV
Original site: 5ETV 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-NOV-15   5ETV              
TITLE     S. AUREUS 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE         
TITLE    2 COMPLEXED WITH AMPCPP AND INHIBITOR AT 1.72 ANGSTROM RESOLUTION      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE          
COMPND   3 PYROPHOSPHOKINASE;                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 2.7.6.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: ADDITIONAL DENSITY WAS PRESENT AT RESIDUE CYS80. THIS 
COMPND   8 WAS MODELLED AS THE OXIDIZED FORM OF CYSTEINE, S-HYDROXYCYSTEINE     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: RK60_02090, RK67_01645, RK72_06915, RK74_04210, RK75_00240,    
SOURCE   5 RK80_01970, RK83_05435, RK84_03130, RK95_04415, RK96_04825,          
SOURCE   6 RK98_03440, RK99_07885, RL05_10010, RL06_09555, RL08_05305,          
SOURCE   7 TM59_02255;                                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR, COMPLEX, AMPCPP, PYROPHOSPHOKINASE, TRANSFERASE-           
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.DENNIS,T.S.PEAT,J.D.SWARBRICK                                     
REVDAT   2   22-JUN-16 5ETV    1       JRNL                                     
REVDAT   1   04-MAY-16 5ETV    0                                                
JRNL        AUTH   M.L.DENNIS,N.P.PITCHER,M.D.LEE,A.J.DEBONO,Z.C.WANG,          
JRNL        AUTH 2 J.R.HARJANI,R.RAHMANI,B.CLEARY,T.S.PEAT,J.B.BAELL,           
JRNL        AUTH 3 J.D.SWARBRICK                                                
JRNL        TITL   STRUCTURAL BASIS FOR THE SELECTIVE BINDING OF INHIBITORS TO  
JRNL        TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM     
JRNL        TITL 3 STAPHYLOCOCCUS AUREUS AND ESCHERICHIA COLI.                  
JRNL        REF    J.MED.CHEM.                   V.  59  5248 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27094768                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00002                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.72 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 21515                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1131                            
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) : 1.72                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1563                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1264                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 101                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.98000                                             
REMARK   3    B12 (A**2) : 0.15000                                              
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): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.093         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1350 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1291 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1841 ; 1.853 ; 2.041       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2976 ; 3.551 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   159 ; 6.466 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    59 ;34.288 ;24.746       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   236 ;10.639 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;15.389 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   210 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1504 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   286 ; 0.013 ; 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):   633 ; 1.111 ; 0.994       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   632 ; 1.063 ; 0.991       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   790 ; 1.634 ; 1.486       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   791 ; 1.642 ; 1.487       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   717 ; 2.507 ; 1.347       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   715 ; 2.480 ; 1.342       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1048 ; 3.755 ; 1.899       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1550 ; 5.727 ; 9.501       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1519 ; 5.520 ; 9.186       
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 5ETV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215447.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5-8.5                            
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) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22673                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 20.20                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 20.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.95900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4CWB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML, 1 MM AMPCPP, 1 MM     
REMARK 280  INHIBITOR, 2 MM MAGNESIUM CHLORIDE,0.186 M SODIUM NITRATE, 18.4%    
REMARK 280  W/V PEG3000, 50 MM SODIUM THIOCYANATE, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 293K                                              
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       17.47033            
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       34.94067            
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       26.20550            
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       43.67583            
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        8.73517            
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 465     LYS A   158                                                      
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       54.86    -97.37                                   
REMARK 500    ALA A 132       35.97   -143.52                                   
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 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  95   OD1                                                    
REMARK 620 2 ASP A  97   OD1  91.9                                              
REMARK 620 3 APC A 201   O1B  91.0  97.4                                        
REMARK 620 4 APC A 201   O1A  91.7 173.5  87.9                                  
REMARK 620 5 HOH A 324   O    92.5  87.8 173.7  86.7                            
REMARK 620 6 HOH A 326   O   172.2  83.5  83.3  93.4  93.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  95   OD2                                                    
REMARK 620 2 ASP A  97   OD2  90.5                                              
REMARK 620 3 APC A 201   O1G 172.2  88.5                                        
REMARK 620 4 APC A 201   O1B  86.4 101.1  86.2                                  
REMARK 620 5 HOH A 320   O    90.2 169.8  92.1  89.1                            
REMARK 620 6 HOH A 358   O    89.1  87.4  98.6 170.4  82.4                      
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 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RZ A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 205                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5ETP   RELATED DB: PDB                                   
REMARK 900 5ETP CONTAINS THE SAME INHIBITOR COMPLEXED WITH THE E. COLI VARIANT  
REMARK 900 OF HPPK                                                              
REMARK 900 RELATED ID: 5ETK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETV   RELATED DB: PDB                                   
DBREF1 5ETV A    1   158  UNP                  A0A0H1ZSM1_STAAU                 
DBREF2 5ETV A     A0A0H1ZSM1                          1         158             
SEQADV 5ETV GLY A   -2  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETV SER A   -1  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETV HIS A    0  UNP  A0A0H1ZSM           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 CSO 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                                          
MODRES 5ETV CSO A   80  CYS  MODIFIED RESIDUE                                   
HET    CSO  A  80       7                                                       
HET    APC  A 201      31                                                       
HET    5RZ  A 202      22                                                       
HET     MG  A 203       1                                                       
HET     MG  A 204       1                                                       
HET    NO3  A 205       4                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                    
HETNAM     5RZ 2-AZANYL-8-[2-(4-BROMOPHENYL)-2-OXIDANYLIDENE-                   
HETNAM   2 5RZ  ETHYL]SULFANYL-1,9-DIHYDROPURIN-6-ONE                           
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NO3 NITRATE ION                                                      
HETSYN     APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE                    
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   2  APC    C11 H18 N5 O12 P3                                            
FORMUL   3  5RZ    C13 H10 BR N5 O2 S                                           
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  NO3    N O3 1-                                                      
FORMUL   7  HOH   *101(H2 O)                                                    
HELIX    1 AA1 ASP A   14  TYR A   29  1                                  16    
HELIX    2 AA2 THR A   66  LEU A   81  1                                  16    
HELIX    3 AA3 ARG A  117  GLU A  120  5                                   4    
HELIX    4 AA4 ARG A  121  ALA A  133  1                                  13    
HELIX    5 AA5 VAL A  144  VAL A  148  1                                   5    
SHEET    1 AA1 4 ILE A  32  ILE A  37  0                                        
SHEET    2 AA1 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3 AA1 4 ILE A   2  SER A  10 -1  N  ILE A   2   O  THR A  63           
SHEET    4 AA1 4 ASP A  95  TYR A 101 -1  O  ASP A  97   N  GLY A   7           
SHEET    1 AA2 4 ILE A  32  ILE A  37  0                                        
SHEET    2 AA2 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3 AA2 4 TYR A  41  THR A  43 -1  N  TYR A  41   O  ASN A  56           
SHEET    4 AA2 4 VAL A 154  ARG A 156 -1  O  LYS A 155   N  GLU A  42           
SHEET    1 AA3 2 ILE A 106  LEU A 108  0                                        
SHEET    2 AA3 2 LEU A 111  VAL A 113 -1  O  LEU A 111   N  LEU A 108           
SHEET    1 AA4 2 VAL A 136  GLU A 137  0                                        
SHEET    2 AA4 2 LEU A 142  LYS A 143 -1  O  LEU A 142   N  GLU A 137           
LINK         C   GLU A  79                 N   CSO A  80     1555   1555  1.34  
LINK         C   CSO A  80                 N   LEU A  81     1555   1555  1.33  
LINK         OD1 ASP A  95                MG    MG A 204     1555   1555  2.02  
LINK         OD2 ASP A  95                MG    MG A 203     1555   1555  2.09  
LINK         OD1 ASP A  97                MG    MG A 204     1555   1555  2.11  
LINK         OD2 ASP A  97                MG    MG A 203     1555   1555  2.08  
LINK         O1G APC A 201                MG    MG A 203     1555   1555  2.07  
LINK         O1B APC A 201                MG    MG A 203     1555   1555  2.27  
LINK         O1B APC A 201                MG    MG A 204     1555   1555  2.05  
LINK         O1A APC A 201                MG    MG A 204     1555   1555  2.07  
LINK        MG    MG A 203                 O   HOH A 320     1555   1555  2.13  
LINK        MG    MG A 203                 O   HOH A 358     1555   1555  2.06  
LINK        MG    MG A 204                 O   HOH A 324     1555   1555  2.04  
LINK        MG    MG A 204                 O   HOH A 326     1555   1555  2.18  
CISPEP   1 VAL A  113    PRO A  114          0        -3.69                     
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 A 203   MG A 204  HOH A 304                    
SITE     5 AC1 23 HOH A 308  HOH A 320  HOH A 321  HOH A 324                    
SITE     6 AC1 23 HOH A 326  HOH A 330  HOH A 334                               
SITE     1 AC2 14 THR A  43  ALA A  44  PRO A  45  VAL A  46                    
SITE     2 AC2 14 GLY A  47  PHE A  54  ASN A  56  ARG A  88                    
SITE     3 AC2 14 GLU A 104  MET A 105  ARG A 121  PHE A 123                    
SITE     4 AC2 14 HOH A 320  HOH A 346                                          
SITE     1 AC3  6 ASP A  95  ASP A  97  APC A 201   MG A 204                    
SITE     2 AC3  6 HOH A 320  HOH A 358                                          
SITE     1 AC4  6 ASP A  95  ASP A  97  APC A 201   MG A 203                    
SITE     2 AC4  6 HOH A 324  HOH A 326                                          
SITE     1 AC5  6 ILE A  12  ARG A  83  ILE A  84  ARG A  85                    
SITE     2 AC5  6 ARG A  92  THR A  93                                          
CRYST1   84.250   84.250   52.411  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      0.011869  0.006853  0.000000        0.00000                         
SCALE2      0.000000  0.013706  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019080        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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