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Database: PDB
Entry: 4CWB
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HEADER    TRANSFERASE                             02-APR-14   4CWB              
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;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HPPK;                                                       
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 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   2   08-MAY-19 4CWB    1       REMARK                                   
REVDAT   1   28-JAN-15 4CWB    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.    1.56 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) : 1.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 28270                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1505                            
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) : 1.56                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2013                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 115                          
REMARK   3   BIN FREE R VALUE                    : 0.2230                       
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          : 64                                      
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.24000                                              
REMARK   3    B22 (A**2) : 0.24000                                              
REMARK   3    B33 (A**2) : -0.77000                                             
REMARK   3    B12 (A**2) : 0.24000                                              
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.162         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1466 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1398 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2012 ; 1.600 ; 2.039       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3239 ; 0.771 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   182 ; 6.468 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;36.562 ;25.231       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   267 ;11.553 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;12.576 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   222 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1714 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   324 ; 0.002 ; 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   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY. AN ALTERNATE              
REMARK   3  CONFORMATION OF THE LOOP 3 RESIDUE LYS86 IS SUGGESTED, THIS WAS     
REMARK   3  NOT MODELLED DUE TO POOR DENSITY. THE TERMINAL RESIDUE LYS158 IS    
REMARK   3  SUGGESTED TO ADOPT MULTIPLE CONFORMATIONS. ONLY THE PREDOMINANT     
REMARK   3  CONFORMATION IS MODELLED DUE TO ELSEWISE POOR DENSITY.              
REMARK   4                                                                      
REMARK   4 4CWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060158.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-14                          
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) : 0.953700                           
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   : 29793                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.67000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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   (%): 58.10                                     
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, AMMONIUM NITRATE 0.275 M,       
REMARK 280  PEG3350 22.2% W/V, SITTING DROP, 281 K, PH 8, VAPOR DIFFUSION,      
REMARK 280  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       17.34667            
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       34.69333            
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       26.02000            
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       43.36667            
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        8.67333            
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    ALA A 132       33.21   -142.91                                   
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 A1159  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC A1161   O1B                                                    
REMARK 620 2 APC A1161   O3G  92.0                                              
REMARK 620 3 ASP A  95   OD2  90.2 174.0                                        
REMARK 620 4 ASP A  97   OD2 114.8  93.6  90.5                                  
REMARK 620 5 HOH A2083   O   103.7  86.0  88.1 141.5                            
REMARK 620 6 HOH A2084   O   164.0  95.9  80.6  78.6  63.2                      
REMARK 620 N                    1     2     3     4     5                       
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 HOH A2065   O                                                      
REMARK 620 2 ASP A  95   OD1  90.5                                              
REMARK 620 3 ASP A  97   OD1  85.6  91.7                                        
REMARK 620 4 APC A1161   O1B 175.8  89.2  98.6                                  
REMARK 620 5 HOH A2085   O    94.1 173.4  83.9  86.6                            
REMARK 620 6 APC A1161   O1A  87.9  92.4 172.3  87.9  92.5                      
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 MG 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 APC 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 X6L A 1163                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE AT THE N-TERMINUS           
DBREF  4CWB A    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
SEQADV 4CWB GLY A   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CWB SER A   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CWB 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     MG  A1159       1                                                       
HET     MG  A1160       1                                                       
HET    APC  A1161      31                                                       
HET    NO3  A1162       4                                                       
HET    X6L  A1163      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                    
HETNAM     NO3 NITRATE ION                                                      
HETNAM     X6L 2-AMINO-8-[2-OXO-2-(4-PHENYLPHENYL)ETHYL]SULFANYL-1,9-           
HETNAM   2 X6L  DIHYDROPURIN-6-ONE                                              
HETSYN     APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE                    
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  APC    C11 H18 N5 O12 P3                                            
FORMUL   5  NO3    N O3 1-                                                      
FORMUL   6  X6L    C19 H15 N5 O2 S                                              
FORMUL   7  HOH   *141(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 LYS A  145  LEU A  147  5                                   3    
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 TYR A  41  THR A  43 -1  O  TYR A  41   N  ASN A  56           
SHEET    5  AB 5 VAL A 154  ARG A 156 -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        MG    MG A1159                 O1B APC A1161     1555   1555  2.02  
LINK        MG    MG A1159                 O3G APC A1161     1555   1555  2.01  
LINK        MG    MG A1159                 OD2 ASP A  95     1555   1555  2.09  
LINK        MG    MG A1159                 OD2 ASP A  97     1555   1555  1.98  
LINK        MG    MG A1159                 O   HOH A2083     1555   1555  2.02  
LINK        MG    MG A1159                 O   HOH A2084     1555   1555  2.69  
LINK        MG    MG A1160                 O   HOH A2065     1555   1555  2.05  
LINK        MG    MG A1160                 OD1 ASP A  95     1555   1555  2.01  
LINK        MG    MG A1160                 OD1 ASP A  97     1555   1555  2.11  
LINK        MG    MG A1160                 O1B APC A1161     1555   1555  2.12  
LINK        MG    MG A1160                 O   HOH A2085     1555   1555  2.12  
LINK        MG    MG A1160                 O1A APC A1161     1555   1555  2.06  
CISPEP   1 VAL A  113    PRO A  114          0        -3.46                     
SITE     1 AC1  6 ASP A  95  ASP A  97   MG A1160  APC A1161                    
SITE     2 AC1  6 HOH A2083  HOH A2084                                          
SITE     1 AC2  6 ASP A  95  ASP A  97   MG A1159  APC A1161                    
SITE     2 AC2  6 HOH A2065  HOH A2085                                          
SITE     1 AC3 25 LEU A  71  ARG A  83  ARG A  88  ARG A  92                    
SITE     2 AC3 25 ASP A  95  ASP A  97  ILE A  98  LYS A 110                    
SITE     3 AC3 25 LEU A 111  SER A 112  HIS A 115  ARG A 117                    
SITE     4 AC3 25 ARG A 121   MG A1159   MG A1160  X6L A1163                    
SITE     5 AC3 25 HOH A2063  HOH A2065  HOH A2071  HOH A2076                    
SITE     6 AC3 25 HOH A2079  HOH A2080  HOH A2083  HOH A2085                    
SITE     7 AC3 25 HOH A2141                                                     
SITE     1 AC4  7 ILE A  12  ARG A  83  ILE A  84  ARG A  85                    
SITE     2 AC4  7 ARG A  92  THR A  93  HOH A2069                               
SITE     1 AC5 18 THR A  43  ALA A  44  PRO A  45  VAL A  46                    
SITE     2 AC5 18 PHE A  54  ASN A  56  VAL A  67  ARG A  88                    
SITE     3 AC5 18 ARG A  92  TYR A 101  GLU A 104  MET A 105                    
SITE     4 AC5 18 ILE A 106  ARG A 121  PHE A 123  APC A1161                    
SITE     5 AC5 18 HOH A2082  HOH A2083                                          
CRYST1   83.817   83.817   52.040  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      0.011931  0.006888  0.000000        0.00000                         
SCALE2      0.000000  0.013776  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019216        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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