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Database: PDB
Entry: 5NP9
LinkDB: 5NP9
Original site: 5NP9 
HEADER    TRANSFERASE                             13-APR-17   5NP9              
TITLE     CRYSTAL STRUCTURE OF BACILLUS SUBTILIS YDIB IN COMPLEX WITH ADP       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: T(6)A37 THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN     
COMPND   5 TSAE;                                                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: CONSTRUCTION DIFFERENT FRON THAT USED FOR PDB ENTRY   
COMPND   8 5MVR THERE IS A FLEXIBLE REGION FROM RESIDUE 87-89 AND NO ELECTRON   
COMPND   9 DENSITY IS VISIBLE FOR RESIDUES 87 AND 88. AS CONCNERNS RESIDUE 89,  
COMPND  10 THERE IS NO DENSITY FOR THE SIDE-CHAIN. HEREAFTER, THE SEQUENCE IS   
COMPND  11 COMPLETE UNTIL RESIDUE 154 (INCL.) AND FROM THEN ON THERE IS NO MORE 
COMPND  12 ELECTRON DENSITY.                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: TSAE, YDIB, BSU05910;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    KINASE, ADP, PHOSPHORYLASTION, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.BALLUT,N.AGHAJARI                                                   
REVDAT   2   16-OCT-19 5NP9    1       REMARK                                   
REVDAT   1   30-MAY-18 5NP9    0                                                
JRNL        AUTH   H.A.NGUYEN,T.EL KHOURY,S.GUIRAL,M.H.LAABERKI,M.P.CANDUSSO,   
JRNL        AUTH 2 F.GALISSON,A.E.FOUCHER,S.KESRAOUI,L.BALLUT,S.VALLET,         
JRNL        AUTH 3 C.ORELLE,L.ZUCCHINI,J.MARTIN,A.PAGE,J.ATTIEH,N.AGHAJARI,     
JRNL        AUTH 4 C.GRANGEASSE,J.M.JAULT                                       
JRNL        TITL   EXPANDING THE KINOME WORLD: A NEW PROTEIN KINASE FAMILY      
JRNL        TITL 2 WIDELY CONSERVED IN BACTERIA.                                
JRNL        REF    J. MOL. BIOL.                 V. 429  3056 2017              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   28890133                                                     
JRNL        DOI    10.1016/J.JMB.2017.08.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11439                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 573                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.0640 -  3.1742    0.95     2769   146  0.1525 0.2063        
REMARK   3     2  3.1742 -  2.5197    0.98     2724   144  0.1901 0.2367        
REMARK   3     3  2.5197 -  2.2013    0.98     2704   142  0.1952 0.2500        
REMARK   3     4  2.2013 -  2.0000    0.98     2669   141  0.2339 0.3038        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.800           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           1257                                  
REMARK   3   ANGLE     :  0.934           1703                                  
REMARK   3   CHIRALITY :  0.054            189                                  
REMARK   3   PLANARITY :  0.004            215                                  
REMARK   3   DIHEDRAL  : 12.504            745                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3866  16.5229  -3.4841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2029 T22:   0.2003                                     
REMARK   3      T33:   0.1950 T12:   0.0188                                     
REMARK   3      T13:   0.0451 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3230 L22:   3.7220                                     
REMARK   3      L33:   3.9269 L12:  -0.5086                                     
REMARK   3      L13:   0.2565 L23:  -0.1383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0187 S12:   0.0028 S13:  -0.1212                       
REMARK   3      S21:  -0.2263 S22:  -0.0552 S23:  -0.1675                       
REMARK   3      S31:   0.4074 S32:   0.0744 S33:   0.0294                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004471.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976250                           
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN COOLED SILICON     
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5MVR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 200 MM MGCL2 AND 100 MM    
REMARK 280  TRIS PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       17.84000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       17.84000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       42.01500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.88500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       42.01500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.88500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       17.84000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       42.01500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.88500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       17.84000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       42.01500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.88500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7560 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     ILE A   156                                                      
REMARK 465     SER A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  90    CG   OD1  OD2                                       
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   O    HOH A   369     O    HOH A   385     6555     1.81            
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    SER A  60      119.68    -38.20                                   
REMARK 500    ILE A  65      -46.75     73.69                                   
REMARK 500    ALA A 127       27.34   -141.34                                   
REMARK 500    ASP A 129      -99.55     56.64                                   
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 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  42   OG1                                                    
REMARK 620 2 GLU A 106   OE1  88.3                                              
REMARK 620 3 ADP A 201   O2B  92.6  98.8                                        
REMARK 620 4 HOH A 306   O   175.6  94.9  83.9                                  
REMARK 620 5 HOH A 311   O    89.5  87.3 173.5  93.8                            
REMARK 620 6 HOH A 316   O    86.8 173.9  85.0  90.3  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5MVR   RELATED DB: PDB                                   
DBREF  5NP9 A    1   158  UNP    O05515   TSAE_BACSU       1    158             
SEQRES   1 A  158  MET LYS GLN LEU LYS TRP ARG THR VAL ASN PRO GLU GLU          
SEQRES   2 A  158  THR LYS ALA ILE ALA LYS LEU THR ALA ALA PHE ALA LYS          
SEQRES   3 A  158  PRO GLY ASP VAL LEU THR LEU GLU GLY ASP LEU GLY ALA          
SEQRES   4 A  158  GLY LYS THR THR PHE THR LYS GLY PHE ALA GLU GLY LEU          
SEQRES   5 A  158  GLY ILE THR ARG ILE VAL ASN SER PRO THR PHE THR ILE          
SEQRES   6 A  158  ILE LYS GLU TYR ASN ASP GLY VAL LEU PRO LEU TYR HIS          
SEQRES   7 A  158  MET ASP VAL TYR ARG MET GLU ASP GLU SER GLU ASP LEU          
SEQRES   8 A  158  GLY LEU ASP GLU TYR PHE HIS GLY GLN GLY VAL CYS LEU          
SEQRES   9 A  158  VAL GLU TRP ALA HIS LEU ILE GLU GLU GLN LEU PRO GLN          
SEQRES  10 A  158  GLU ARG LEU GLN ILE VAL ILE LYS ARG ALA GLY ASP ASP          
SEQRES  11 A  158  GLU ARG GLU ILE THR PHE THR ALA VAL GLY ASN ARG TYR          
SEQRES  12 A  158  GLU MET LEU CYS GLU GLU LEU SER ARG HIS ASP ASN ILE          
SEQRES  13 A  158  SER ASN                                                      
HET    ADP  A 201      27                                                       
HET     MG  A 202       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *86(H2 O)                                                     
HELIX    1 AA1 ASN A   10  ALA A   23  1                                  14    
HELIX    2 AA2 GLY A   40  GLY A   53  1                                  14    
HELIX    3 AA3 ARG A   83  GLU A   87  5                                   5    
HELIX    4 AA4 LEU A   93  HIS A   98  1                                   6    
HELIX    5 AA5 ALA A  108  LEU A  115  5                                   8    
HELIX    6 AA6 GLY A  140  ASP A  154  1                                  15    
SHEET    1 AA1 7 GLN A   3  THR A   8  0                                        
SHEET    2 AA1 7 ARG A 132  VAL A 139 -1  O  ILE A 134   N  TRP A   6           
SHEET    3 AA1 7 ARG A 119  ARG A 126 -1  N  LYS A 125   O  GLU A 133           
SHEET    4 AA1 7 ASP A  29  GLU A  34  1  N  THR A  32   O  ILE A 122           
SHEET    5 AA1 7 VAL A 102  GLU A 106  1  O  CYS A 103   N  LEU A  31           
SHEET    6 AA1 7 LEU A  76  ASP A  80  1  N  MET A  79   O  GLU A 106           
SHEET    7 AA1 7 ILE A  66  TYR A  69 -1  N  TYR A  69   O  LEU A  76           
LINK         OG1 THR A  42                MG    MG A 202     1555   1555  2.09  
LINK         OE1 GLU A 106                MG    MG A 202     1555   1555  2.13  
LINK         O2B ADP A 201                MG    MG A 202     1555   1555  2.12  
LINK        MG    MG A 202                 O   HOH A 306     1555   1555  2.19  
LINK        MG    MG A 202                 O   HOH A 311     1555   1555  2.21  
LINK        MG    MG A 202                 O   HOH A 316     1555   1555  2.19  
SITE     1 AC1 20 THR A   8  ASN A  10  PRO A  11  THR A  14                    
SITE     2 AC1 20 ASP A  36  LEU A  37  GLY A  38  ALA A  39                    
SITE     3 AC1 20 GLY A  40  LYS A  41  THR A  42  THR A  43                    
SITE     4 AC1 20 GLU A 106  ASP A 130  ARG A 132   MG A 202                    
SITE     5 AC1 20 HOH A 306  HOH A 316  HOH A 335  HOH A 342                    
SITE     1 AC2  6 THR A  42  GLU A 106  ADP A 201  HOH A 306                    
SITE     2 AC2  6 HOH A 311  HOH A 316                                          
CRYST1   84.030  111.770   35.680  90.00  90.00  90.00 C 2 2 21      8          
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      0.011901  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008947  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028027        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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