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Database: PDB
Entry: 1RTR
LinkDB: 1RTR
Original site: 1RTR 
HEADER    TRANSFERASE                             10-DEC-03   1RTR              
TITLE     CRYSTAL STRUCTURE OF S. AUREUS FARNESYL PYROPHOSPHATE                 
TITLE    2 SYNTHASE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GERANYLTRANSTRANSFERASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FARNESYL PYROPHOSPHATE SYNTHASE;                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.HOSFIELD,Y.ZHANG,D.R.DOUGAN,A.BROOUN,L.W.TARI,                    
AUTHOR   2 R.V.SWANSON,J.FINN                                                   
REVDAT   3   24-FEB-09 1RTR    1       VERSN                                    
REVDAT   2   06-APR-04 1RTR    1       JRNL                                     
REVDAT   1   02-MAR-04 1RTR    0                                                
JRNL        AUTH   D.J.HOSFIELD,Y.ZHANG,D.R.DOUGAN,A.BROOUN,L.W.TARI,           
JRNL        AUTH 2 R.V.SWANSON,J.FINN                                           
JRNL        TITL   STRUCTURAL BASIS FOR BISPHOSPHONATE-MEDIATED                 
JRNL        TITL 2 INHIBITION OF ISOPRENOID BIOSYNTHESIS                        
JRNL        REF    J.MOL.BIOL.                   V. 279  8526 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   14672944                                                     
JRNL        DOI    10.1074/JBC.C300511200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 34204                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3779                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2413                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 278                          
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4301                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 161                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
REMARK   3    B12 (A**2) : -0.05000                                             
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): 0.301         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.182         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.400         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4358 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5886 ; 1.211 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   544 ; 4.811 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   696 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3178 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2189 ; 0.216 ; 0.200       
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):   152 ; 0.127 ; 0.200       
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):    39 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.228 ; 0.200       
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):  2714 ; 0.570 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4367 ; 1.116 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1644 ; 1.587 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1519 ; 2.801 ; 4.500       
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 : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1RTR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB021028.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 97                                 
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.9                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, PHOSPHATE, PH 5,               
REMARK 280  NANOLITER SITTING DROP VAPOUR DIFFUSION, TEMPERATURE 298K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-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       54.39467            
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      108.78933            
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       81.59200            
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      135.98667            
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       27.19733            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.39467            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      108.78933            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      135.98667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       81.59200            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       27.19733            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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     MET A     1                                                      
REMARK 465     LEU A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     LYS A   232                                                      
REMARK 465     LYS A   233                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     SER A   236                                                      
REMARK 465     ASP A   237                                                      
REMARK 465     LEU A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     ASN A   240                                                      
REMARK 465     ASN A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 465     HIS A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     MET B     1                                                      
REMARK 465     TYR B   224                                                      
REMARK 465     GLY B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     GLU B   227                                                      
REMARK 465     ALA B   228                                                      
REMARK 465     LYS B   229                                                      
REMARK 465     LEU B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     LYS B   232                                                      
REMARK 465     LYS B   233                                                      
REMARK 465     VAL B   234                                                      
REMARK 465     GLY B   235                                                      
REMARK 465     SER B   236                                                      
REMARK 465     ASP B   237                                                      
REMARK 465     LEU B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     ASN B   240                                                      
REMARK 465     ASN B   241                                                      
REMARK 465     LYS B   242                                                      
REMARK 465     ASP B   292                                                      
REMARK 465     HIS B   293                                                      
REMARK 465     LYS B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     HIS B   298                                                      
REMARK 465     HIS B   299                                                      
REMARK 465     HIS B   300                                                      
REMARK 465     HIS B   301                                                      
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 B   689     O    HOH B   706              2.16            
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    LEU A  50   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ASP A  91   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 126   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 157   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 219   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 286   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B  83   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B  91   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 113   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 126   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 222   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    ALA A  40      -36.32    -38.56                                   
REMARK 500    MET A  87     -118.62   -122.06                                   
REMARK 500    ASN A  89       62.45     64.61                                   
REMARK 500    MET B  87     -113.87   -114.32                                   
REMARK 500    ARG B  94       53.74     32.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 659        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A 660        DISTANCE =  6.54 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RQI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RQJ   RELATED DB: PDB                                   
DBREF  1RTR A    1   293  UNP    Q8NWD6   Q8NWD6_STAAW     1    293             
DBREF  1RTR B    1   293  UNP    Q8NWD6   Q8NWD6_STAAW     1    293             
SEQADV 1RTR THR A  198  UNP  Q8NWD6    ALA   198 CONFLICT                       
SEQADV 1RTR LYS A  294  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR GLY A  295  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  296  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  297  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  298  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  299  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  300  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS A  301  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR THR B  198  UNP  Q8NWD6    ALA   198 CONFLICT                       
SEQADV 1RTR LYS B  294  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR GLY B  295  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  296  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  297  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  298  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  299  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  300  UNP  Q8NWD6              EXPRESSION TAG                 
SEQADV 1RTR HIS B  301  UNP  Q8NWD6              EXPRESSION TAG                 
SEQRES   1 A  301  MET THR ASN LEU PRO MET ASN LYS LEU ILE ASP GLU VAL          
SEQRES   2 A  301  ASN ASN GLU LEU SER VAL ALA ILE ASN LYS SER VAL MET          
SEQRES   3 A  301  ASP THR GLN LEU GLU GLU SER MET LEU TYR SER LEU ASN          
SEQRES   4 A  301  ALA GLY GLY LYS ARG ILE ARG PRO VAL LEU LEU LEU LEU          
SEQRES   5 A  301  THR LEU ASP SER LEU ASN THR GLU TYR GLU LEU GLY MET          
SEQRES   6 A  301  LYS SER ALA ILE ALA LEU GLU MET ILE HIS THR TYR SER          
SEQRES   7 A  301  LEU ILE HIS ASP ASP LEU PRO ALA MET ASP ASN ASP ASP          
SEQRES   8 A  301  TYR ARG ARG GLY LYS LEU THR ASN HIS LYS VAL TYR GLY          
SEQRES   9 A  301  GLU TRP THR ALA ILE LEU ALA GLY ASP ALA LEU LEU THR          
SEQRES  10 A  301  LYS ALA PHE GLU LEU ILE SER SER ASP ASP ARG LEU THR          
SEQRES  11 A  301  ASP GLU VAL LYS ILE LYS VAL LEU GLN ARG LEU SER ILE          
SEQRES  12 A  301  ALA SER GLY HIS VAL GLY MET VAL GLY GLY GLN MET LEU          
SEQRES  13 A  301  ASP MET GLN SER GLU GLY GLN PRO ILE ASP LEU GLU THR          
SEQRES  14 A  301  LEU GLU MET ILE HIS LYS THR LYS THR GLY ALA LEU LEU          
SEQRES  15 A  301  THR PHE ALA VAL MET SER ALA ALA ASP ILE ALA ASN VAL          
SEQRES  16 A  301  ASP ASP THR THR LYS GLU HIS LEU GLU SER TYR SER TYR          
SEQRES  17 A  301  HIS LEU GLY MET MET PHE GLN ILE LYS ASP ASP LEU LEU          
SEQRES  18 A  301  ASP CYS TYR GLY ASP GLU ALA LYS LEU GLY LYS LYS VAL          
SEQRES  19 A  301  GLY SER ASP LEU GLU ASN ASN LYS SER THR TYR VAL SER          
SEQRES  20 A  301  LEU LEU GLY LYS ASP GLY ALA GLU ASP LYS LEU THR TYR          
SEQRES  21 A  301  HIS ARG ASP ALA ALA VAL ASP GLU LEU THR GLN ILE ASP          
SEQRES  22 A  301  GLU GLN PHE ASN THR LYS HIS LEU LEU GLU ILE VAL ASP          
SEQRES  23 A  301  LEU PHE TYR SER ARG ASP HIS LYS GLY HIS HIS HIS HIS          
SEQRES  24 A  301  HIS HIS                                                      
SEQRES   1 B  301  MET THR ASN LEU PRO MET ASN LYS LEU ILE ASP GLU VAL          
SEQRES   2 B  301  ASN ASN GLU LEU SER VAL ALA ILE ASN LYS SER VAL MET          
SEQRES   3 B  301  ASP THR GLN LEU GLU GLU SER MET LEU TYR SER LEU ASN          
SEQRES   4 B  301  ALA GLY GLY LYS ARG ILE ARG PRO VAL LEU LEU LEU LEU          
SEQRES   5 B  301  THR LEU ASP SER LEU ASN THR GLU TYR GLU LEU GLY MET          
SEQRES   6 B  301  LYS SER ALA ILE ALA LEU GLU MET ILE HIS THR TYR SER          
SEQRES   7 B  301  LEU ILE HIS ASP ASP LEU PRO ALA MET ASP ASN ASP ASP          
SEQRES   8 B  301  TYR ARG ARG GLY LYS LEU THR ASN HIS LYS VAL TYR GLY          
SEQRES   9 B  301  GLU TRP THR ALA ILE LEU ALA GLY ASP ALA LEU LEU THR          
SEQRES  10 B  301  LYS ALA PHE GLU LEU ILE SER SER ASP ASP ARG LEU THR          
SEQRES  11 B  301  ASP GLU VAL LYS ILE LYS VAL LEU GLN ARG LEU SER ILE          
SEQRES  12 B  301  ALA SER GLY HIS VAL GLY MET VAL GLY GLY GLN MET LEU          
SEQRES  13 B  301  ASP MET GLN SER GLU GLY GLN PRO ILE ASP LEU GLU THR          
SEQRES  14 B  301  LEU GLU MET ILE HIS LYS THR LYS THR GLY ALA LEU LEU          
SEQRES  15 B  301  THR PHE ALA VAL MET SER ALA ALA ASP ILE ALA ASN VAL          
SEQRES  16 B  301  ASP ASP THR THR LYS GLU HIS LEU GLU SER TYR SER TYR          
SEQRES  17 B  301  HIS LEU GLY MET MET PHE GLN ILE LYS ASP ASP LEU LEU          
SEQRES  18 B  301  ASP CYS TYR GLY ASP GLU ALA LYS LEU GLY LYS LYS VAL          
SEQRES  19 B  301  GLY SER ASP LEU GLU ASN ASN LYS SER THR TYR VAL SER          
SEQRES  20 B  301  LEU LEU GLY LYS ASP GLY ALA GLU ASP LYS LEU THR TYR          
SEQRES  21 B  301  HIS ARG ASP ALA ALA VAL ASP GLU LEU THR GLN ILE ASP          
SEQRES  22 B  301  GLU GLN PHE ASN THR LYS HIS LEU LEU GLU ILE VAL ASP          
SEQRES  23 B  301  LEU PHE TYR SER ARG ASP HIS LYS GLY HIS HIS HIS HIS          
SEQRES  24 B  301  HIS HIS                                                      
FORMUL   3  HOH   *161(H2 O)                                                    
HELIX    1   1 PRO A    5  VAL A   19  1                                  15    
HELIX    2   2 GLN A   29  ASN A   39  1                                  11    
HELIX    3   3 ARG A   44  LEU A   57  1                                  14    
HELIX    4   4 GLU A   60  LEU A   63  5                                   4    
HELIX    5   5 GLY A   64  LEU A   84  1                                  21    
HELIX    6   6 THR A   98  GLY A  104  1                                   7    
HELIX    7   7 GLY A  104  SER A  125  1                                  22    
HELIX    8   8 THR A  130  GLY A  146  1                                  17    
HELIX    9   9 GLY A  149  SER A  160  1                                  12    
HELIX   10  10 ASP A  166  THR A  178  1                                  13    
HELIX   11  11 THR A  178  ASN A  194  1                                  17    
HELIX   12  12 ASP A  196  ALA A  228  1                                  33    
HELIX   13  13 THR A  244  GLN A  271  1                                  28    
HELIX   14  14 THR A  278  SER A  290  1                                  13    
HELIX   15  15 PRO B    5  VAL B   19  1                                  15    
HELIX   16  16 GLN B   29  ASN B   39  1                                  11    
HELIX   17  17 ARG B   44  LEU B   57  1                                  14    
HELIX   18  18 GLU B   60  LEU B   63  5                                   4    
HELIX   19  19 GLY B   64  ASP B   83  1                                  20    
HELIX   20  20 THR B   98  GLY B  104  1                                   7    
HELIX   21  21 GLY B  104  SER B  125  1                                  22    
HELIX   22  22 THR B  130  GLY B  146  1                                  17    
HELIX   23  23 GLY B  149  SER B  160  1                                  12    
HELIX   24  24 ASP B  166  THR B  178  1                                  13    
HELIX   25  25 THR B  178  ASN B  194  1                                  17    
HELIX   26  26 ASP B  196  ASP B  222  1                                  27    
HELIX   27  27 THR B  244  GLY B  250  1                                   7    
HELIX   28  28 GLY B  250  ILE B  272  1                                  23    
HELIX   29  29 THR B  278  ARG B  291  1                                  14    
SHEET    1   A 2 TYR A  92  ARG A  93  0                                        
SHEET    2   A 2 LYS A  96  LEU A  97 -1  O  LYS A  96   N  ARG A  93           
SHEET    1   B 2 TYR B  92  ARG B  93  0                                        
SHEET    2   B 2 LYS B  96  LEU B  97 -1  O  LYS B  96   N  ARG B  93           
CRYST1  150.201  150.201  163.184  90.00  90.00 120.00 P 61 2 2     24          
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      0.006658  0.003844  0.000000        0.00000                         
SCALE2      0.000000  0.007688  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006128        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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