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Database: PDB
Entry: 3QBC
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Original site: 3QBC 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-JAN-11   3QBC              
TITLE     STRUCTURE AND DESIGN OF A NEW PTERIN SITE INHIBITOR OF S. AUREUS HPPK 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-AMINO-4-HYDROXY-6-HYDROXYMETHYLDIHYDROPTERIDINE          
COMPND   3 PYROPHOSPHOKINASE;                                                   
COMPND   4 CHAIN: A, B;                                                         
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: 158878;                                              
SOURCE   4 STRAIN: MU50;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PROTEIN-INHIBITOR COMPLEX, FERREDOXIN-LIKE FOLD, KINASE, ATP BINDING, 
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.S.PEAT,S.CHHABRA,J.D.SWARBRICK                                      
REVDAT   4   23-OCT-19 3QBC    1       REMARK SEQADV                            
REVDAT   3   27-JUN-12 3QBC    1       JRNL                                     
REVDAT   2   01-FEB-12 3QBC    1       JRNL                                     
REVDAT   1   25-JAN-12 3QBC    0                                                
JRNL        AUTH   S.CHHABRA,O.DOLEZAL,B.M.COLLINS,J.NEWMAN,J.S.SIMPSON,        
JRNL        AUTH 2 I.G.MACREADIE,R.FERNLEY,T.S.PEAT,J.D.SWARBRICK               
JRNL        TITL   STRUCTURE OF S. AUREUS HPPK AND THE DISCOVERY OF A NEW       
JRNL        TITL 2 SUBSTRATE SITE INHIBITOR                                     
JRNL        REF    PLOS ONE                      V.   7 29444 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22276115                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0029444                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.CHHABRA,J.NEWMAN,T.S.PEAT,R.T.FERNLEY,J.CAINE,J.S.SIMPSON, 
REMARK   1  AUTH 2 J.D.SWARBRICK                                                
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF            
REMARK   1  TITL 2 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM     
REMARK   1  TITL 3 STAPHYLOCOCCUS AUREUS                                        
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   575 2010              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   20445263                                                     
REMARK   1  DOI    10.1107/S1744309110010857                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 32158                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1684                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2373                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2562                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 254                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.38000                                              
REMARK   3    B22 (A**2) : -0.73000                                             
REMARK   3    B33 (A**2) : -0.48000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.50000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.116         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.125         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2824 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3868 ; 2.156 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   365 ; 6.293 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   123 ;40.448 ;24.634       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   530 ;15.055 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.582 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   448 ; 0.152 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2182 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1730 ; 1.330 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2861 ; 2.075 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1094 ; 2.948 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1000 ; 4.229 ; 4.500       
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   : 1.40                                          
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 3QBC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063429.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
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) : 0.955                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33864                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
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: 1RAO, 1CBK                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 90MM BIS-TRIS(PH 6.5), 10MM SODIUM       
REMARK 280  ACETATE(PH 4.6), 175MM SODIUM FORMATE, 1.08M SODIUM MALONATE,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 7               
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       38.28300            
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, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   254     O    HOH A   266              2.07            
REMARK 500   OG1  THR A    93     O    HOH A   209              2.11            
REMARK 500   O    HOH A   189     O    HOH A   203              2.16            
REMARK 500   O    ILE A    32     O    HOH A   168              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN A    20     OE2  GLU B    50     2545     1.67            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    LEU B  94   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  85      -62.51    -92.81                                   
REMARK 500    VAL A 124      -60.02    -90.62                                   
REMARK 500    LYS B  86      115.10    147.80                                   
REMARK 500    LYS B  86      114.05    147.85                                   
REMARK 500    ALA B 132       29.41   -141.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B55 A 159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B55 B 163                 
DBREF  3QBC A    1   158  UNP    Q99W87   Q99W87_STAAM     1    158             
DBREF  3QBC B    1   158  UNP    Q99W87   Q99W87_STAAM     1    158             
SEQADV 3QBC GLY A   -2  UNP  Q99W87              EXPRESSION TAG                 
SEQADV 3QBC SER A   -1  UNP  Q99W87              EXPRESSION TAG                 
SEQADV 3QBC HIS A    0  UNP  Q99W87              EXPRESSION TAG                 
SEQADV 3QBC GLY B   -2  UNP  Q99W87              EXPRESSION TAG                 
SEQADV 3QBC SER B   -1  UNP  Q99W87              EXPRESSION TAG                 
SEQADV 3QBC HIS B    0  UNP  Q99W87              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                                          
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                                          
HET    B55  A 159      12                                                       
HET    B55  B 163      12                                                       
HETNAM     B55 2-AMINO-8-SULFANYL-1,9-DIHYDRO-6H-PURIN-6-ONE                    
HETSYN     B55 2-AMINO-8-MERCAPTO-1H-PURIN-6(9H)-ONE                            
FORMUL   3  B55    2(C5 H5 N5 O S)                                              
FORMUL   5  HOH   *254(H2 O)                                                    
HELIX    1   1 ASP A   14  TYR A   29  1                                  16    
HELIX    2   2 THR A   66  ARG A   83  1                                  18    
HELIX    3   3 LYS A   86  GLY A   90  5                                   5    
HELIX    4   4 ARG A  117  GLU A  120  5                                   4    
HELIX    5   5 ARG A  121  ALA A  133  1                                  13    
HELIX    6   6 VAL A  144  VAL A  148  1                                   5    
HELIX    7   7 ASP B   14  TYR B   29  1                                  16    
HELIX    8   8 THR B   66  HIS B   82  1                                  17    
HELIX    9   9 ARG B  117  GLU B  120  5                                   4    
HELIX   10  10 ARG B  121  ALA B  133  1                                  13    
HELIX   11  11 LYS B  143  VAL B  148  1                                   6    
SHEET    1   A 4 ILE A  32  ILE A  37  0                                        
SHEET    2   A 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3   A 4 ILE A   2  SER A  10 -1  N  ILE A   2   O  THR A  63           
SHEET    4   A 4 ASP A  95  TYR A 101 -1  O  ASP A  97   N  GLY A   7           
SHEET    1   B 4 ILE A  32  ILE A  37  0                                        
SHEET    2   B 4 PHE A  54  THR A  63 -1  O  GLU A  60   N  ASN A  36           
SHEET    3   B 4 TYR A  41  THR A  43 -1  N  THR A  43   O  PHE A  54           
SHEET    4   B 4 VAL A 154  ARG A 156 -1  O  LYS A 155   N  GLU A  42           
SHEET    1   C 2 ILE A 106  LEU A 108  0                                        
SHEET    2   C 2 LEU A 111  VAL A 113 -1  O  VAL A 113   N  ILE A 106           
SHEET    1   D 2 VAL A 136  GLU A 137  0                                        
SHEET    2   D 2 LEU A 142  LYS A 143 -1  O  LEU A 142   N  GLU A 137           
SHEET    1   E 4 ILE B  32  ILE B  37  0                                        
SHEET    2   E 4 PHE B  54  THR B  63 -1  O  GLU B  60   N  ASN B  36           
SHEET    3   E 4 ILE B   2  SER B  10 -1  N  ALA B   4   O  ILE B  61           
SHEET    4   E 4 ASP B  95  TYR B 101 -1  O  ASP B  97   N  GLY B   7           
SHEET    1   F 4 ILE B  32  ILE B  37  0                                        
SHEET    2   F 4 PHE B  54  THR B  63 -1  O  GLU B  60   N  ASN B  36           
SHEET    3   F 4 TYR B  41  THR B  43 -1  N  TYR B  41   O  ASN B  56           
SHEET    4   F 4 VAL B 154  ARG B 156 -1  O  LYS B 155   N  GLU B  42           
SHEET    1   G 2 ILE B 106  LEU B 108  0                                        
SHEET    2   G 2 LEU B 111  VAL B 113 -1  O  VAL B 113   N  ILE B 106           
CISPEP   1 VAL A  113    PRO A  114          0        -9.26                     
CISPEP   2 VAL B  113    PRO B  114          0        -9.22                     
SITE     1 AC1  9 THR A  43  ALA A  44  VAL A  46  PHE A  54                    
SITE     2 AC1  9 ASN A  56  PHE A 123  HOH A 268  PRO B 109                    
SITE     3 AC1  9 LYS B 110                                                     
SITE     1 AC2 10 PRO A 109  LYS A 110  THR B  43  ALA B  44                    
SITE     2 AC2 10 VAL B  46  PHE B  54  ASN B  56  PHE B 123                    
SITE     3 AC2 10 HOH B 211  HOH B 249                                          
CRYST1   36.790   76.566   51.522  90.00 100.17  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      0.027182  0.000000  0.004877        0.00000                         
SCALE2      0.000000  0.013061  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019719        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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