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Database: PDB
Entry: 5ETS
LinkDB: 5ETS
Original site: 5ETS 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-NOV-15   5ETS              
TITLE     S. AUREUS 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE         
TITLE    2 COMPLEXED WITH AMPCPP AND INHIBITOR AT 1.95 ANGSTROM RESOLUTION      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE          
COMPND   3 PYROPHOSPHOKINASE;                                                   
COMPND   4 CHAIN: B, A;                                                         
COMPND   5 EC: 2.7.6.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
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 5ETS    1       JRNL                                     
REVDAT   1   04-MAY-16 5ETS    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.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22747                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1228                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1665                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2506                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : 1.47000                                              
REMARK   3    B33 (A**2) : -0.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.60000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.183         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
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      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2658 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2536 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3624 ; 1.747 ; 2.040       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5840 ; 3.569 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   312 ; 6.599 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;35.306 ;24.828       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   470 ;12.238 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;14.422 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   420 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2986 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   548 ; 0.010 ; 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):  1254 ; 0.864 ; 0.878       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1253 ; 0.852 ; 0.877       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1564 ; 1.346 ; 1.308       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1565 ; 1.351 ; 1.309       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1404 ; 1.718 ; 1.125       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1405 ; 1.717 ; 1.125       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2061 ; 2.623 ; 1.607       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3106 ; 4.211 ; 8.058       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3107 ; 4.211 ; 8.060       
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 5ETS 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_1000215445.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.1                                
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) : 1.0329                             
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   : 24055                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: 5ETQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML 1 MM AMPCPP, 1 MM      
REMARK 280  INHIBITOR, 0.182 MGCL2, 0.1 M TRIS CHLORIDE, 17.2%W/V PEG8000,      
REMARK 280  50 MM SODIUM THIOCYANATE, PH 9.1, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 281K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.29000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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 B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
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    TYR B  48     -158.06   -153.87                                   
REMARK 500    ALA B 132       33.71   -145.53                                   
REMARK 500    TYR A  48     -155.51   -152.77                                   
REMARK 500    ALA A 132       33.33   -147.55                                   
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                              NA B 203  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  27   O                                                      
REMARK 620 2 TYR B  29   O   102.5                                              
REMARK 620 3 ILE B  32   O    89.8  85.9                                        
REMARK 620 4 HOH B 320   O    68.0 170.2  96.2                                  
REMARK 620 5 HOH B 372   O   148.6 108.4  87.2  81.3                            
REMARK 620 6 HOH A 356   O   100.6  96.1 168.7  83.7  81.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 205  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  95   OD1                                                    
REMARK 620 2 ASP B  97   OD1  90.9                                              
REMARK 620 3 APC B 201   O2B  91.6  94.9                                        
REMARK 620 4 APC B 201   O1A  89.0 173.9  91.3                                  
REMARK 620 5 HOH B 326   O    90.0  85.3 178.4  88.5                            
REMARK 620 6 HOH B 357   O   173.5  88.1  94.9  91.3  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  95   OD2                                                    
REMARK 620 2 ASP B  97   OD2  88.7                                              
REMARK 620 3 APC B 201   O1G 175.7  90.3                                        
REMARK 620 4 APC B 201   O2B  91.4  96.4  84.5                                  
REMARK 620 5 HOH B 325   O    88.4 173.1  93.0  89.9                            
REMARK 620 6 HOH B 365   O    90.7  89.0  93.5 174.2  84.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 206  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 107   OD1                                                    
REMARK 620 2 ASP A 107   OD1 168.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 203  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  27   O                                                      
REMARK 620 2 TYR A  29   O    99.9                                              
REMARK 620 3 ILE A  32   O    89.5  80.8                                        
REMARK 620 4 HOH A 356   O   148.6 110.8  89.4                                  
REMARK 620 5 HOH B 320   O    68.4 168.1  96.7  80.6                            
REMARK 620 6 HOH B 372   O    99.5 103.8 168.9  79.6  80.9                      
REMARK 620 N                    1     2     3     4     5                       
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  92.1                                              
REMARK 620 3 APC A 201   O1B  91.8  96.0                                        
REMARK 620 4 APC A 201   O2A  88.7 174.5  89.4                                  
REMARK 620 5 HOH A 313   O    89.0  87.0 176.8  87.5                            
REMARK 620 6 HOH A 331   O   175.0  86.8  93.2  92.1  86.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 205  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  95   OD2                                                    
REMARK 620 2 ASP A  97   OD2  85.1                                              
REMARK 620 3 APC A 201   O2G 178.4  94.4                                        
REMARK 620 4 APC A 201   O1B  89.3  95.9  89.3                                  
REMARK 620 5 HOH A 323   O    85.0 167.6  95.8  91.5                            
REMARK 620 6 HOH A 346   O    86.7  86.9  94.8 175.0  85.1                      
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 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RX B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue APC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RX A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 205                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5ETN   RELATED DB: PDB                                   
REMARK 900 5ETN CONTAINS THE SAME INHIBITOR COMPLEXED WITH THE E. COLI FORM OF  
REMARK 900 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: 5ETO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5ETV   RELATED DB: PDB                                   
DBREF1 5ETS B    1   158  UNP                  A0A0H1ZSM1_STAAU                 
DBREF2 5ETS B     A0A0H1ZSM1                          1         158             
DBREF1 5ETS A    1   158  UNP                  A0A0H1ZSM1_STAAU                 
DBREF2 5ETS A     A0A0H1ZSM1                          1         158             
SEQADV 5ETS GLY B   -2  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETS SER B   -1  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETS HIS B    0  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETS GLY A   -2  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETS SER A   -1  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQADV 5ETS HIS A    0  UNP  A0A0H1ZSM           EXPRESSION TAG                 
SEQRES   1 B  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 B  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 B  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 B  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 B  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 B  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 B  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 B  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 B  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 B  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 B  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 B  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER          
SEQRES  13 B  161  VAL LYS ARG TYR LYS                                          
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  B 201      31                                                       
HET    5RX  B 202      20                                                       
HET     NA  B 203       1                                                       
HET     MG  B 204       1                                                       
HET     MG  B 205       1                                                       
HET     NA  B 206       1                                                       
HET    APC  A 201      31                                                       
HET    5RX  A 202      20                                                       
HET     NA  A 203       1                                                       
HET     MG  A 204       1                                                       
HET     MG  A 205       1                                                       
HETNAM     APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                    
HETNAM     5RX 2-AZANYL-8-[(4-CHLOROPHENYL)METHYLSULFANYL]-1,9-                 
HETNAM   2 5RX  DIHYDROPURIN-6-ONE                                              
HETNAM      NA SODIUM ION                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE                    
FORMUL   3  APC    2(C11 H18 N5 O12 P3)                                         
FORMUL   4  5RX    2(C12 H10 CL N5 O S)                                         
FORMUL   5   NA    3(NA 1+)                                                     
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL  14  HOH   *154(H2 O)                                                    
HELIX    1 AA1 ASP B   14  TYR B   29  1                                  16    
HELIX    2 AA2 THR B   66  LEU B   81  1                                  16    
HELIX    3 AA3 ARG B  117  GLU B  120  5                                   4    
HELIX    4 AA4 ARG B  121  ALA B  133  1                                  13    
HELIX    5 AA5 VAL B  144  VAL B  148  1                                   5    
HELIX    6 AA6 ASP A   14  TYR A   29  1                                  16    
HELIX    7 AA7 THR A   66  LEU A   81  1                                  16    
HELIX    8 AA8 ARG A  117  GLU A  120  5                                   4    
HELIX    9 AA9 ARG A  121  ALA A  133  1                                  13    
HELIX   10 AB1 VAL A  144  VAL A  148  1                                   5    
SHEET    1 AA1 4 ILE B  32  ILE B  37  0                                        
SHEET    2 AA1 4 PHE B  54  THR B  63 -1  O  GLU B  60   N  ASN B  36           
SHEET    3 AA1 4 ILE B   2  SER B  10 -1  N  ILE B   2   O  THR B  63           
SHEET    4 AA1 4 ASP B  95  TYR B 101 -1  O  ASP B  97   N  GLY B   7           
SHEET    1 AA2 4 ILE B  32  ILE B  37  0                                        
SHEET    2 AA2 4 PHE B  54  THR B  63 -1  O  GLU B  60   N  ASN B  36           
SHEET    3 AA2 4 TYR B  41  THR B  43 -1  N  TYR B  41   O  ASN B  56           
SHEET    4 AA2 4 VAL B 154  ARG B 156 -1  O  LYS B 155   N  GLU B  42           
SHEET    1 AA3 2 ILE B 106  LEU B 108  0                                        
SHEET    2 AA3 2 LEU B 111  VAL B 113 -1  O  LEU B 111   N  LEU B 108           
SHEET    1 AA4 2 VAL B 136  GLU B 137  0                                        
SHEET    2 AA4 2 LEU B 142  LYS B 143 -1  O  LEU B 142   N  GLU B 137           
SHEET    1 AA5 4 ILE A  32  ILE A  37  0                                        
SHEET    2 AA5 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3 AA5 4 ILE A   2  SER A  10 -1  N  ILE A   2   O  THR A  63           
SHEET    4 AA5 4 ASP A  95  TYR A 101 -1  O  ASP A  97   N  GLY A   7           
SHEET    1 AA6 4 ILE A  32  ILE A  37  0                                        
SHEET    2 AA6 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3 AA6 4 TYR A  41  THR A  43 -1  N  TYR A  41   O  ASN A  56           
SHEET    4 AA6 4 VAL A 154  ARG A 156 -1  O  LYS A 155   N  GLU A  42           
SHEET    1 AA7 2 ILE A 106  LEU A 108  0                                        
SHEET    2 AA7 2 LEU A 111  VAL A 113 -1  O  LEU A 111   N  LEU A 108           
SHEET    1 AA8 2 VAL A 136  GLU A 137  0                                        
SHEET    2 AA8 2 LEU A 142  LYS A 143 -1  O  LEU A 142   N  GLU A 137           
LINK         O   ASN B  27                NA    NA B 203     1555   1555  2.43  
LINK         O   TYR B  29                NA    NA B 203     1555   1555  2.46  
LINK         O   ILE B  32                NA    NA B 203     1555   1555  2.20  
LINK         OD1 ASP B  95                MG    MG B 205     1555   1555  2.13  
LINK         OD2 ASP B  95                MG    MG B 204     1555   1555  2.07  
LINK         OD1 ASP B  97                MG    MG B 205     1555   1555  2.08  
LINK         OD2 ASP B  97                MG    MG B 204     1555   1555  2.06  
LINK         OD1 ASP B 107                NA    NA B 206     1555   1555  2.35  
LINK         O   ASN A  27                NA    NA A 203     1555   1555  2.38  
LINK         O   TYR A  29                NA    NA A 203     1555   1555  2.61  
LINK         O   ILE A  32                NA    NA A 203     1555   1555  2.30  
LINK         OD1 ASP A  95                MG    MG A 204     1555   1555  2.11  
LINK         OD2 ASP A  95                MG    MG A 205     1555   1555  2.13  
LINK         OD1 ASP A  97                MG    MG A 204     1555   1555  2.03  
LINK         OD2 ASP A  97                MG    MG A 205     1555   1555  2.11  
LINK         OD1 ASP A 107                NA    NA B 206     1555   1555  2.31  
LINK         O1G APC B 201                MG    MG B 204     1555   1555  2.02  
LINK         O2B APC B 201                MG    MG B 204     1555   1555  2.17  
LINK         O2B APC B 201                MG    MG B 205     1555   1555  2.02  
LINK         O1A APC B 201                MG    MG B 205     1555   1555  2.09  
LINK        NA    NA B 203                 O   HOH B 320     1555   1555  2.39  
LINK        NA    NA B 203                 O   HOH B 372     1555   1555  2.26  
LINK        MG    MG B 204                 O   HOH B 325     1555   1555  2.10  
LINK        MG    MG B 204                 O   HOH B 365     1555   1555  2.14  
LINK        MG    MG B 205                 O   HOH B 326     1555   1555  2.13  
LINK        MG    MG B 205                 O   HOH B 357     1555   1555  2.07  
LINK         O2G APC A 201                MG    MG A 205     1555   1555  2.05  
LINK         O1B APC A 201                MG    MG A 204     1555   1555  1.99  
LINK         O1B APC A 201                MG    MG A 205     1555   1555  2.17  
LINK         O2A APC A 201                MG    MG A 204     1555   1555  2.10  
LINK        NA    NA A 203                 O   HOH A 356     1555   1555  2.36  
LINK        MG    MG A 204                 O   HOH A 313     1555   1555  2.17  
LINK        MG    MG A 204                 O   HOH A 331     1555   1555  2.09  
LINK        MG    MG A 205                 O   HOH A 323     1555   1555  2.08  
LINK        MG    MG A 205                 O   HOH A 346     1555   1555  2.13  
LINK        NA    NA B 203                 O   HOH A 356     1555   1454  2.25  
LINK        NA    NA A 203                 O   HOH B 320     1555   1656  2.42  
LINK        NA    NA A 203                 O   HOH B 372     1555   1656  2.24  
CISPEP   1 VAL B  113    PRO B  114          0        -3.53                     
CISPEP   2 VAL A  113    PRO A  114          0        -3.06                     
SITE     1 AC1 28 LEU B  71  ARG B  83  ARG B  85  ARG B  92                    
SITE     2 AC1 28 ASP B  95  ASP B  97  ILE B  98  LYS B 110                    
SITE     3 AC1 28 LEU B 111  SER B 112  HIS B 115  ARG B 117                    
SITE     4 AC1 28 ARG B 121   MG B 204   MG B 205  HOH B 306                    
SITE     5 AC1 28 HOH B 309  HOH B 315  HOH B 323  HOH B 325                    
SITE     6 AC1 28 HOH B 326  HOH B 327  HOH B 328  HOH B 341                    
SITE     7 AC1 28 HOH B 357  HOH B 360  HOH B 365  HOH B 369                    
SITE     1 AC2 16 ASN B  11  THR B  43  ALA B  44  PRO B  45                    
SITE     2 AC2 16 VAL B  46  TYR B  48  GLN B  51  PHE B  54                    
SITE     3 AC2 16 ASN B  56  GLY B  90  PRO B  91  ARG B  92                    
SITE     4 AC2 16 ARG B 121  PHE B 123  HOH B 325  HOH B 363                    
SITE     1 AC3  7  NA A 203  HOH A 356  ASN B  27  TYR B  29                    
SITE     2 AC3  7 ILE B  32  HOH B 320  HOH B 372                               
SITE     1 AC4  6 ASP B  95  ASP B  97  APC B 201   MG B 205                    
SITE     2 AC4  6 HOH B 325  HOH B 365                                          
SITE     1 AC5  6 ASP B  95  ASP B  97  APC B 201   MG B 204                    
SITE     2 AC5  6 HOH B 326  HOH B 357                                          
SITE     1 AC6  2 ASP A 107  ASP B 107                                          
SITE     1 AC7 23 LEU A  71  ARG A  83  ARG A  92  ASP A  95                    
SITE     2 AC7 23 ASP A  97  ILE A  98  LYS A 110  LEU A 111                    
SITE     3 AC7 23 SER A 112  HIS A 115  ARG A 117  ARG A 121                    
SITE     4 AC7 23  MG A 204   MG A 205  HOH A 302  HOH A 313                    
SITE     5 AC7 23 HOH A 315  HOH A 317  HOH A 323  HOH A 331                    
SITE     6 AC7 23 HOH A 332  HOH A 346  HOH A 353                               
SITE     1 AC8 16 ASN A  11  THR A  43  ALA A  44  PRO A  45                    
SITE     2 AC8 16 VAL A  46  TYR A  48  GLN A  51  PHE A  54                    
SITE     3 AC8 16 ASN A  56  GLY A  90  PRO A  91  ARG A  92                    
SITE     4 AC8 16 ARG A 121  PHE A 123  HOH A 323  HOH A 348                    
SITE     1 AC9  7 ASN A  27  TYR A  29  ILE A  32  HOH A 356                    
SITE     2 AC9  7  NA B 203  HOH B 320  HOH B 372                               
SITE     1 AD1  6 ASP A  95  ASP A  97  APC A 201   MG A 205                    
SITE     2 AD1  6 HOH A 313  HOH A 331                                          
SITE     1 AD2  6 ASP A  95  ASP A  97  APC A 201   MG A 204                    
SITE     2 AD2  6 HOH A 323  HOH A 346                                          
CRYST1   47.790   68.580   52.990  90.00 105.94  90.00 P 1 21 1      4          
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      0.020925  0.000000  0.005976        0.00000                         
SCALE2      0.000000  0.014582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019626        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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