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Database: PDB
Entry: 1SVW
LinkDB: 1SVW
Original site: 1SVW 
HEADER    HYDROLASE                               30-MAR-04   1SVW              
TITLE     CRYSTAL STRUCTURE OF YSXC COMPLEXED WITH GMPPNP                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTP-BINDING PROTEIN YSXC;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: YSXC, ENGB, BSU28190;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    YSXC, GTPASE, GTP-BINDING PROTEIN, GMPPNP, GTP, HYDROLASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.N.RUZHEINIKOV,S.K.DAS,S.E.SEDELNIKOVA,P.J.BAKER,P.J.ARTYMIUK,       
AUTHOR   2 J.GARCIA-LARA,S.J.FOSTER,D.W.RICE                                    
REVDAT   3   11-OCT-17 1SVW    1       REMARK                                   
REVDAT   2   24-FEB-09 1SVW    1       VERSN                                    
REVDAT   1   25-MAY-04 1SVW    0                                                
JRNL        AUTH   S.N.RUZHEINIKOV,S.K.DAS,S.E.SEDELNIKOVA,P.J.BAKER,           
JRNL        AUTH 2 P.J.ARTYMIUK,J.GARCIA-LARA,S.J.FOSTER,D.W.RICE               
JRNL        TITL   ANALYSIS OF THE OPEN AND CLOSED CONFORMATIONS OF THE         
JRNL        TITL 2 GTP-BINDING PROTEIN YSXC FROM BACILLUS SUBTILIS.             
JRNL        REF    J.MOL.BIOL.                   V. 339   265 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15136032                                                     
JRNL        DOI    10.1016/J.JMB.2004.03.043                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.K.DAS,S.E.SEDELNIKOVA,P.J.BAKER,S.N.RUZHEINIKOV,           
REMARK   1  AUTH 2 S.J.FOSTER,D.W.RICE                                          
REMARK   1  TITL   EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY    
REMARK   1  TITL 2 CRYSTALLOGRAPHIC ANALYSIS OF A PUTATIVE GTP-BINDING PROTEIN, 
REMARK   1  TITL 3 YSXC, FROM BACILLUS SUBTILIS.                                
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 10097                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.306                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 361                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3026                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022038.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.11200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HEPES, ETHYLENE GLYCOL,        
REMARK 280  GMPPNP, MGCL2, PH 7.5, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 290K                                                    
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       35.29950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     VAL A    84                                                      
REMARK 465     SER A    85                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     ALA B    82                                                      
REMARK 465     LYS B    83                                                      
REMARK 465     VAL B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     LYS B    86                                                      
REMARK 465     SER B    87                                                      
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   OE2  GLU A   128     NH1  ARG B    46     2647     2.18            
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    LYS A   2       90.48    -65.95                                   
REMARK 500    VAL A   9      -50.71   -137.32                                   
REMARK 500    GLU A  16       26.85    -72.30                                   
REMARK 500    GLN A  17      -25.52   -149.47                                   
REMARK 500    ASN A  33      -14.05     90.67                                   
REMARK 500    SER A  54      -53.49    -16.96                                   
REMARK 500    LYS A  55       50.98    166.70                                   
REMARK 500    PRO A  56     -119.85   -115.42                                   
REMARK 500    ASP A  69       11.80     54.16                                   
REMARK 500    TYR A  79      117.85    -38.36                                   
REMARK 500    PHE A  81      -73.03    -65.87                                   
REMARK 500    ALA A  82       36.00    -95.41                                   
REMARK 500    ARG A  89      -75.33    -63.90                                   
REMARK 500    GLU A  97      -72.85    -58.14                                   
REMARK 500    THR A  98      -64.09    -28.63                                   
REMARK 500    ILE A 100       35.02    -63.69                                   
REMARK 500    THR A 101        0.15   -164.39                                   
REMARK 500    THR A 102       -6.12   -140.69                                   
REMARK 500    LEU A 106      106.33    -41.93                                   
REMARK 500    ALA A 108      154.46    149.14                                   
REMARK 500    GLN A 125      -73.36    -41.99                                   
REMARK 500    ASP A 145       -5.62    -43.61                                   
REMARK 500    PRO A 148      106.10    -41.39                                   
REMARK 500    LYS A 149      -40.91    -27.02                                   
REMARK 500    ASN A 164       68.65     30.28                                   
REMARK 500    GLU A 177      -72.88    -83.45                                   
REMARK 500    LYS A 182      -91.19    -42.10                                   
REMARK 500    THR B   4      -14.49   -147.79                                   
REMARK 500    GLU B   7      140.05    168.02                                   
REMARK 500    ILE B   8     -176.46    -69.49                                   
REMARK 500    VAL B   9      -78.66   -133.95                                   
REMARK 500    VAL B  13      -59.48   -120.42                                   
REMARK 500    GLU B  16        7.46    -49.18                                   
REMARK 500    GLU B  20      -86.96   -104.02                                   
REMARK 500    LEU B  23      156.82    -45.61                                   
REMARK 500    ASN B  48       24.06    163.57                                   
REMARK 500    ALA B  50       60.88   -105.12                                   
REMARK 500    ARG B  51       98.73     -6.20                                   
REMARK 500    SER B  53     -161.84   -168.08                                   
REMARK 500    LYS B  55      -27.16     91.79                                   
REMARK 500    PRO B  56     -116.80    -75.04                                   
REMARK 500    ASP B  69       45.59     25.87                                   
REMARK 500    GLU B  70      -63.66   -121.71                                   
REMARK 500    PRO B  77     -161.32    -60.27                                   
REMARK 500    TYR B  79      106.88    -33.01                                   
REMARK 500    ALA B  91     -100.22    -58.75                                   
REMARK 500    TRP B  92      -71.99      8.28                                   
REMARK 500    THR B 102       26.17   -153.55                                   
REMARK 500    LEU B 106      101.92    -44.61                                   
REMARK 500    ALA B 108      141.33    173.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  99         0.08    SIDE CHAIN                              
REMARK 500    TYR B  18         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 300  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GTP A 401   O2B                                                    
REMARK 620 2 VAL A  76   O   145.4                                              
REMARK 620 3 SER A  37   OG   56.3 150.9                                        
REMARK 620 4 ASP A  75   OD2 105.1 109.4  57.6                                  
REMARK 620 5 GTP A 401   O3G  65.9 103.3  63.9 110.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GTP B 402   O2B                                                    
REMARK 620 2 THR B  59   OG1 130.1                                              
REMARK 620 3 GTP B 402   O3G  84.1  67.6                                        
REMARK 620 4 SER B  37   OG   75.0  79.6 113.2                                  
REMARK 620 N                    1     2     3                                   
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 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SVL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE APO-YSXC                                    
REMARK 900 RELATED ID: 1SUI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE GTP-BINDING PROTEIN YSXC COMPLEXED WITH GDP 
DBREF  1SVW A    1   195  UNP    P38424   ENGB_BACSU       1    195             
DBREF  1SVW B    1   195  UNP    P38424   ENGB_BACSU       1    195             
SEQRES   1 A  195  MET LYS VAL THR LYS SER GLU ILE VAL ILE SER ALA VAL          
SEQRES   2 A  195  LYS PRO GLU GLN TYR PRO GLU GLY GLY LEU PRO GLU ILE          
SEQRES   3 A  195  ALA LEU ALA GLY ARG SER ASN VAL GLY LYS SER SER PHE          
SEQRES   4 A  195  ILE ASN SER LEU ILE ASN ARG LYS ASN LEU ALA ARG THR          
SEQRES   5 A  195  SER SER LYS PRO GLY LYS THR GLN THR LEU ASN PHE TYR          
SEQRES   6 A  195  ILE ILE ASN ASP GLU LEU HIS PHE VAL ASP VAL PRO GLY          
SEQRES   7 A  195  TYR GLY PHE ALA LYS VAL SER LYS SER GLU ARG GLU ALA          
SEQRES   8 A  195  TRP GLY ARG MET ILE GLU THR TYR ILE THR THR ARG GLU          
SEQRES   9 A  195  GLU LEU LYS ALA VAL VAL GLN ILE VAL ASP LEU ARG HIS          
SEQRES  10 A  195  ALA PRO SER ASN ASP ASP VAL GLN MET TYR GLU PHE LEU          
SEQRES  11 A  195  LYS TYR TYR GLY ILE PRO VAL ILE VAL ILE ALA THR LYS          
SEQRES  12 A  195  ALA ASP LYS ILE PRO LYS GLY LYS TRP ASP LYS HIS ALA          
SEQRES  13 A  195  LYS VAL VAL ARG GLN THR LEU ASN ILE ASP PRO GLU ASP          
SEQRES  14 A  195  GLU LEU ILE LEU PHE SER SER GLU THR LYS LYS GLY LYS          
SEQRES  15 A  195  ASP GLU ALA TRP GLY ALA ILE LYS LYS MET ILE ASN ARG          
SEQRES   1 B  195  MET LYS VAL THR LYS SER GLU ILE VAL ILE SER ALA VAL          
SEQRES   2 B  195  LYS PRO GLU GLN TYR PRO GLU GLY GLY LEU PRO GLU ILE          
SEQRES   3 B  195  ALA LEU ALA GLY ARG SER ASN VAL GLY LYS SER SER PHE          
SEQRES   4 B  195  ILE ASN SER LEU ILE ASN ARG LYS ASN LEU ALA ARG THR          
SEQRES   5 B  195  SER SER LYS PRO GLY LYS THR GLN THR LEU ASN PHE TYR          
SEQRES   6 B  195  ILE ILE ASN ASP GLU LEU HIS PHE VAL ASP VAL PRO GLY          
SEQRES   7 B  195  TYR GLY PHE ALA LYS VAL SER LYS SER GLU ARG GLU ALA          
SEQRES   8 B  195  TRP GLY ARG MET ILE GLU THR TYR ILE THR THR ARG GLU          
SEQRES   9 B  195  GLU LEU LYS ALA VAL VAL GLN ILE VAL ASP LEU ARG HIS          
SEQRES  10 B  195  ALA PRO SER ASN ASP ASP VAL GLN MET TYR GLU PHE LEU          
SEQRES  11 B  195  LYS TYR TYR GLY ILE PRO VAL ILE VAL ILE ALA THR LYS          
SEQRES  12 B  195  ALA ASP LYS ILE PRO LYS GLY LYS TRP ASP LYS HIS ALA          
SEQRES  13 B  195  LYS VAL VAL ARG GLN THR LEU ASN ILE ASP PRO GLU ASP          
SEQRES  14 B  195  GLU LEU ILE LEU PHE SER SER GLU THR LYS LYS GLY LYS          
SEQRES  15 B  195  ASP GLU ALA TRP GLY ALA ILE LYS LYS MET ILE ASN ARG          
HET     MG  A 300       1                                                       
HET    GTP  A 401      32                                                       
HET     MG  B 301       1                                                       
HET    GTP  B 402      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  GTP    2(C10 H16 N5 O14 P3)                                         
HELIX    1   1 GLY A   35  ASN A   45  1                                  11    
HELIX    2   2 SER A   87  ILE A  100  1                                  14    
HELIX    3   3 SER A  120  TYR A  133  1                                  14    
HELIX    4   4 LYS A  143  ILE A  147  5                                   5    
HELIX    5   5 PRO A  148  GLY A  150  5                                   3    
HELIX    6   6 LYS A  151  LEU A  163  1                                  13    
HELIX    7   7 GLY A  181  ASN A  194  1                                  14    
HELIX    8   8 LYS B   14  TYR B   18  5                                   5    
HELIX    9   9 GLY B   35  ILE B   44  1                                  10    
HELIX   10  10 GLU B   88  THR B  101  1                                  14    
HELIX   11  11 SER B  120  GLY B  134  1                                  15    
HELIX   12  12 LYS B  143  ILE B  147  5                                   5    
HELIX   13  13 LYS B  151  LEU B  163  1                                  13    
HELIX   14  14 GLY B  181  ARG B  195  1                                  15    
SHEET    1   A 6 GLU A   7  ALA A  12  0                                        
SHEET    2   A 6 LEU A  62  ILE A  67 -1  O  ILE A  66   N  GLU A   7           
SHEET    3   A 6 LEU A  71  ASP A  75 -1  O  ASP A  75   N  ASN A  63           
SHEET    4   A 6 GLU A  25  GLY A  30  1  N  ILE A  26   O  HIS A  72           
SHEET    5   A 6 LEU A 106  ASP A 114  1  O  LYS A 107   N  GLU A  25           
SHEET    6   A 6 ILE A 140  THR A 142  1  O  THR A 142   N  VAL A 113           
SHEET    1   B 3 SER B   6  GLU B   7  0                                        
SHEET    2   B 3 LEU B  62  ILE B  67 -1  O  ILE B  66   N  GLU B   7           
SHEET    3   B 3 SER B  11  ALA B  12 -1  N  ALA B  12   O  LEU B  62           
SHEET    1   C 6 SER B   6  GLU B   7  0                                        
SHEET    2   C 6 LEU B  62  ILE B  67 -1  O  ILE B  66   N  GLU B   7           
SHEET    3   C 6 LEU B  71  ASP B  75 -1  O  LEU B  71   N  ILE B  67           
SHEET    4   C 6 GLU B  25  GLY B  30  1  N  ILE B  26   O  HIS B  72           
SHEET    5   C 6 LEU B 106  ASP B 114  1  O  LYS B 107   N  GLU B  25           
SHEET    6   C 6 VAL B 139  THR B 142  1  O  ILE B 140   N  VAL B 113           
LINK        MG    MG A 300                 O2B GTP A 401     1555   1555  2.85  
LINK        MG    MG A 300                 O   VAL A  76     1555   1555  2.84  
LINK        MG    MG A 300                 OG  SER A  37     1555   1555  2.85  
LINK        MG    MG A 300                 OD2 ASP A  75     1555   1555  2.89  
LINK        MG    MG A 300                 O3G GTP A 401     1555   1555  2.86  
LINK        MG    MG B 301                 O2B GTP B 402     1555   1555  2.05  
LINK        MG    MG B 301                 OG1 THR B  59     1555   1555  2.21  
LINK        MG    MG B 301                 O3G GTP B 402     1555   1555  2.14  
LINK        MG    MG B 301                 OG  SER B  37     1555   1555  2.38  
SITE     1 AC1  6 LYS A  36  SER A  37  THR A  59  ASP A  75                    
SITE     2 AC1  6 VAL A  76  GTP A 401                                          
SITE     1 AC2  5 LYS B  36  SER B  37  THR B  59  ASP B  75                    
SITE     2 AC2  5 GTP B 402                                                     
SITE     1 AC3 18 ASN A  33  VAL A  34  GLY A  35  LYS A  36                    
SITE     2 AC3 18 SER A  37  SER A  38  THR A  52  SER A  53                    
SITE     3 AC3 18 SER A  54  GLY A  57  LYS A  58  THR A  59                    
SITE     4 AC3 18 GLY A  78  LYS A 143  ASP A 145  LYS A 146                    
SITE     5 AC3 18 SER A 176   MG A 300                                          
SITE     1 AC4 20 SER B  32  ASN B  33  VAL B  34  GLY B  35                    
SITE     2 AC4 20 LYS B  36  SER B  37  SER B  38  THR B  52                    
SITE     3 AC4 20 SER B  53  SER B  54  GLY B  57  LYS B  58                    
SITE     4 AC4 20 THR B  59  GLY B  78  THR B 142  LYS B 143                    
SITE     5 AC4 20 ASP B 145  SER B 175  SER B 176   MG B 301                    
CRYST1   43.586   70.599   72.583  90.00 102.26  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      0.022943  0.000000  0.004986        0.00000                         
SCALE2      0.000000  0.014165  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014099        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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