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Database: PDB
Entry: 1IOV
LinkDB: 1IOV
Original site: 1IOV 
HEADER    LIGASE                                  20-SEP-96   1IOV              
TITLE     COMPLEX OF D-ALA:D-ALA LIGASE WITH ADP AND A PHOSPHORYL               
TITLE    2 PHOSPHONATE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALA\:D-ALA LIGASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.2.4;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_GENE: DDLB;                                        
SOURCE   7 OTHER_DETAILS: ENZYME PROVIDED BY C.T. WALSH, HARVARD MED            
SOURCE   8 SCHOOL. SEE ZAWADZKE ET AL. BIOCHEM. 30, P. 1673, 1991.              
KEYWDS    GLYCOGEN PHOSPHORYLASE, LIGASE, CELL WALL, PEPTIDOGLYCAN              
KEYWDS   2 SYNTHESIS, VANCOMYCIN, ADP BINDING                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KNOX,P.C.MOEWS,C.FAN                                              
REVDAT   4   24-FEB-09 1IOV    1       VERSN                                    
REVDAT   3   01-APR-03 1IOV    1       JRNL                                     
REVDAT   2   30-NOV-99 1IOV    1       JRNL   HEADER                            
REVDAT   1   12-FEB-97 1IOV    0                                                
JRNL        AUTH   C.FAN,I.S.PARK,C.T.WALSH,J.R.KNOX                            
JRNL        TITL   D-ALANINE:D-ALANINE LIGASE: PHOSPHONATE AND                  
JRNL        TITL 2 PHOSPHINATE INTERMEDIATES WITH WILD TYPE AND THE             
JRNL        TITL 3 Y216F MUTANT.                                                
JRNL        REF    BIOCHEMISTRY                  V.  36  2531 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9054558                                                      
JRNL        DOI    10.1021/BI962431T                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.FAN,P.C.MOEWS,Y.SHI,C.T.WALSH,J.R.KNOX                     
REMARK   1  TITL   A COMMON FOLD FOR PEPTIDE SYNTHETASES CLEAVING ATP           
REMARK   1  TITL 2 TO ADP                                                       
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  92  1172 1995              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.FAN,P.C.MOEWS,C.T.WALSH,J.R.KNOX                           
REMARK   1  TITL   VANCOMYCIN RESISTANCE: STRUCTURE OF                          
REMARK   1  TITL 2 D-ALANINE:D-ALANINE LIGASE AT 2.3 A RESOLUTION               
REMARK   1  REF    SCIENCE                       V. 266   439 1994              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 7591                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2293                                    
REMARK   3   NUCLEIC ACID ATOMS       : 27                                      
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.30                          
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.008 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 1.100 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.019 ; 0.040               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.005 ; 0.018               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.115 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.204 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.305 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : 0.365 ; 0.500               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 1.100 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 22.500; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 19.600; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.263 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 0.472 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 0.197 ; 1.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 0.356 ; 1.500               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 1995                               
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 6.5                                
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 RUH2R                       
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                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : XENGEN                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11579                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 75.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 39.0                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PROLSQ                                                
REMARK 200 STARTING MODEL: 2DLN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6.5                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       49.30000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.50000            
REMARK 290   SMTRY3   4  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 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 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   NH1  ARG A    31     O    ALA A    37              2.10            
REMARK 500   OE2  GLU A   187     O3'  ADP A   310              2.11            
REMARK 500   O    MET A     1     N    ASP A     3              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   489     O    HOH A   506     1554     1.13            
REMARK 500   O    HOH A   456     O    HOH A   456     2565     1.16            
REMARK 500   O    HOH A   494     O    HOH A   494     2565     1.24            
REMARK 500   O    HOH A   468     O    HOH A   579     3546     1.27            
REMARK 500   O    HOH A   413     O    HOH A   653     2555     1.28            
REMARK 500   O    HOH A   426     O    HOH A   654     1565     1.29            
REMARK 500   CB   SER A   155     O    HOH A   437     3547     1.47            
REMARK 500   O    HOH A   474     O    HOH A   594     2555     1.47            
REMARK 500   O    HOH A   504     O    HOH A   663     3556     1.51            
REMARK 500   O    HOH A   473     O    HOH A   475     2555     1.68            
REMARK 500   O    HOH A   486     O    HOH A   650     3556     1.74            
REMARK 500   O    HOH A   574     O    HOH A   593     2555     1.83            
REMARK 500   O    HOH A   533     O    HOH A   565     3557     1.84            
REMARK 500   O    HOH A   532     O    HOH A   614     3557     1.85            
REMARK 500   OH   TYR A   212     NH1  ARG A   288     3547     1.85            
REMARK 500   O    HOH A   499     O    HOH A   499     2565     1.86            
REMARK 500   O    ALA A   227     O    HOH A   492     3556     1.89            
REMARK 500   O    HOH A   446     O    HOH A   662     1565     1.94            
REMARK 500   O    HOH A   594     O    HOH A   651     2555     2.00            
REMARK 500   CG   GLN A   204     O    HOH A   609     3556     2.01            
REMARK 500   NZ   LYS A   156     OE2  GLU A   230     3546     2.03            
REMARK 500   O    HOH A   578     O    HOH A   586     1565     2.08            
REMARK 500   O    HOH A   495     O    HOH A   496     2565     2.10            
REMARK 500   O    HOH A   587     O    HOH A   588     2565     2.11            
REMARK 500   O    HOH A   559     O    HOH A   569     3547     2.13            
REMARK 500   OE1  GLU A    17     O    HOH A   652     3557     2.14            
REMARK 500   O    HOH A   631     O    HOH A   638     3547     2.15            
REMARK 500   CD   LYS A     4     O    HOH A   570     1556     2.17            
REMARK 500   OE2  GLU A    17     O    HOH A   652     3557     2.17            
REMARK 500   OE2  GLU A   148     O    HOH A   420     3547     2.18            
REMARK 500   O    HOH A   458     O    HOH A   637     3556     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A  41   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP A  96   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A  99   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    LEU A 178   CA  -  CB  -  CG  ANGL. DEV. =  20.1 DEGREES          
REMARK 500    TYR A 210   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    TYR A 210   CB  -  CG  -  CD1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 255   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 255   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 263   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 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    THR A   2      -54.43     65.94                                   
REMARK 500    GLU A  44      -75.04   -149.19                                   
REMARK 500    THR A  71      -73.55    -54.84                                   
REMARK 500    SER A  86      134.80    -29.45                                   
REMARK 500    ALA A 159      136.48    100.99                                   
REMARK 500    SER A 184       76.31   -101.57                                   
REMARK 500    LEU A 217       68.73   -118.88                                   
REMARK 500    PRO A 226     -168.66    -67.15                                   
REMARK 500    ALA A 231       11.41    -61.33                                   
REMARK 500    SER A 232      -60.43   -101.88                                   
REMARK 500    LEU A 237      -70.97    -61.86                                   
REMARK 500    GLU A 270     -177.94   -171.09                                   
REMARK 500    SER A 274       67.85   -153.32                                   
REMARK 500    MET A 277       36.83   -147.16                                   
REMARK 500    ALA A 290       20.63    -76.70                                   
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    ARG A  31         0.12    SIDE_CHAIN                              
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 408        DISTANCE =  7.45 ANGSTROMS                       
REMARK 525    HOH A 418        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 428        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH A 435        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH A 437        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 439        DISTANCE =  9.31 ANGSTROMS                       
REMARK 525    HOH A 456        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 460        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 465        DISTANCE = 10.66 ANGSTROMS                       
REMARK 525    HOH A 467        DISTANCE =  9.12 ANGSTROMS                       
REMARK 525    HOH A 468        DISTANCE =  9.79 ANGSTROMS                       
REMARK 525    HOH A 472        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A 473        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A 492        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH A 497        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 498        DISTANCE = 12.17 ANGSTROMS                       
REMARK 525    HOH A 500        DISTANCE =  9.52 ANGSTROMS                       
REMARK 525    HOH A 503        DISTANCE = 13.71 ANGSTROMS                       
REMARK 525    HOH A 533        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH A 552        DISTANCE =  8.02 ANGSTROMS                       
REMARK 525    HOH A 554        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH A 558        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 586        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE = 10.07 ANGSTROMS                       
REMARK 525    HOH A 588        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 603        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A 607        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH A 612        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 613        DISTANCE = 10.62 ANGSTROMS                       
REMARK 525    HOH A 622        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A 626        DISTANCE =  7.58 ANGSTROMS                       
REMARK 525    HOH A 630        DISTANCE =  9.26 ANGSTROMS                       
REMARK 525    HOH A 644        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A 646        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 647        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 654        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH A 655        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 656        DISTANCE =  8.35 ANGSTROMS                       
REMARK 525    HOH A 662        DISTANCE =  5.89 ANGSTROMS                       
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 331  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O2B                                                    
REMARK 620 2 POB A 321   O5P 101.4                                              
REMARK 620 3 GLU A 270   OE2  78.8 102.8                                        
REMARK 620 4 ASN A 272   OD1 174.7  82.0  96.5                                  
REMARK 620 5 ADP A 310   O3B  50.8  66.9  55.2 128.3                            
REMARK 620 6 HOH A 536   O   114.1  76.1 167.0  70.6 133.1                      
REMARK 620 7 GLU A 270   OE1  98.2 142.2  50.1  76.7 103.2 123.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 330  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O3B                                                    
REMARK 620 2 ADP A 310   O2A  81.9                                              
REMARK 620 3 POB A 321   O4P  59.8 138.6                                        
REMARK 620 4 ASP A 257   OD2 137.2  87.4 109.5                                  
REMARK 620 5 GLU A 270   OE2  54.3  70.4  74.4  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 332  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 271   O                                                      
REMARK 620 2 HOH A 522   O   143.0                                              
REMARK 620 3 SER A  94   O    91.2  85.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ADP                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ADP BINDING SITE.                                  
REMARK 800 SITE_IDENTIFIER: LIG                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: LIGAND BINDING SITE.                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 330                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 331                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 332                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 310                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POB A 321                 
DBREF  1IOV A    2   306  UNP    P07862   DDLB_ECOLI       1    305             
SEQRES   1 A  306  MET THR ASP LYS ILE ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 A  306  ALA GLU ARG GLU VAL SER LEU ASN SER GLY ALA ALA VAL          
SEQRES   3 A  306  LEU ALA GLY LEU ARG GLU GLY GLY ILE ASP ALA TYR PRO          
SEQRES   4 A  306  VAL ASP PRO LYS GLU VAL ASP VAL THR GLN LEU LYS SER          
SEQRES   5 A  306  MET GLY PHE GLN LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 A  306  GLY GLY GLU ASP GLY THR LEU GLN GLY MET LEU GLU LEU          
SEQRES   7 A  306  MET GLY LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 A  306  ALA LEU SER MET ASP LYS LEU ARG SER LYS LEU LEU TRP          
SEQRES   9 A  306  GLN GLY ALA GLY LEU PRO VAL ALA PRO TRP VAL ALA LEU          
SEQRES  10 A  306  THR ARG ALA GLU PHE GLU LYS GLY LEU SER ASP LYS GLN          
SEQRES  11 A  306  LEU ALA GLU ILE SER ALA LEU GLY LEU PRO VAL ILE VAL          
SEQRES  12 A  306  LYS PRO SER ARG GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 A  306  VAL VAL ALA GLU ASN ALA LEU GLN ASP ALA LEU ARG LEU          
SEQRES  14 A  306  ALA PHE GLN HIS ASP GLU GLU VAL LEU ILE GLU LYS TRP          
SEQRES  15 A  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY GLU          
SEQRES  16 A  306  GLU ILE LEU PRO SER ILE ARG ILE GLN PRO SER GLY THR          
SEQRES  17 A  306  PHE TYR ASP TYR GLU ALA LYS TYR LEU SER ASP GLU THR          
SEQRES  18 A  306  GLN TYR PHE CYS PRO ALA GLY LEU GLU ALA SER GLN GLU          
SEQRES  19 A  306  ALA ASN LEU GLN ALA LEU VAL LEU LYS ALA TRP THR THR          
SEQRES  20 A  306  LEU GLY CYS LYS GLY TRP GLY ARG ILE ASP VAL MET LEU          
SEQRES  21 A  306  ASP SER ASP GLY GLN PHE TYR LEU LEU GLU ALA ASN THR          
SEQRES  22 A  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 A  306  ALA ARG GLN ALA GLY MET SER PHE SER GLN LEU VAL VAL          
SEQRES  24 A  306  ARG ILE LEU GLU LEU ALA ASP                                  
HET     MG  A 330       1                                                       
HET     MG  A 331       1                                                       
HET     MG  A 332       1                                                       
HET    ADP  A 310      27                                                       
HET    POB  A 321      17                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     POB 2-[(1-AMINO-ETHYL)-PHOSPHATE-PHOSPHINOYLOXY]-BUTYRIC             
HETNAM   2 POB  ACID                                                            
FORMUL   2   MG    3(MG 2+)                                                     
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  POB    C6 H15 N O8 P2                                               
FORMUL   7  HOH   *263(H2 O)                                                    
HELIX    1   1 ARG A   16  GLU A   32  1                                  17    
HELIX    2   2 THR A   71  MET A   79  1                                   9    
HELIX    3   3 VAL A   88  SER A   94  1                                   7    
HELIX    4   4 LYS A   97  GLY A  106  1                                  10    
HELIX    5   5 ARG A  119  PHE A  122  1                                   4    
HELIX    6   6 LEU A  131  ALA A  136  1                                   6    
HELIX    7   7 GLU A  160  GLN A  172  5                                  13    
HELIX    8   8 TYR A  212  TYR A  216  1                                   5    
HELIX    9   9 GLN A  233  THR A  246  1                                  14    
HELIX   10  10 LEU A  282  GLN A  289  1                                   8    
HELIX   11  11 PHE A  294  LEU A  302  1                                   9    
SHEET    1   A 3 ASP A  36  ASP A  41  0                                        
SHEET    2   A 3 LYS A   4  LEU A   9  1  N  ILE A   5   O  ASP A  36           
SHEET    3   A 3 PHE A  55  ALA A  61  1  N  GLN A  56   O  LYS A   4           
SHEET    1   B 4 TRP A 114  THR A 118  0                                        
SHEET    2   B 4 GLU A 176  LYS A 181 -1  N  ILE A 179   O  VAL A 115           
SHEET    3   B 4 VAL A 141  PRO A 145 -1  N  LYS A 144   O  LEU A 178           
SHEET    4   B 4 SER A 155  VAL A 157 -1  N  VAL A 157   O  VAL A 141           
SHEET    1   C 5 PHE A 266  ASN A 272  0                                        
SHEET    2   C 5 TRP A 253  LEU A 260 -1  N  MET A 259   O  TYR A 267           
SHEET    3   C 5 GLU A 187  LEU A 193 -1  N  ILE A 192   O  GLY A 254           
SHEET    4   C 5 ILE A 201  GLN A 204 -1  N  ILE A 203   O  GLU A 187           
SHEET    5   C 5 GLN A 222  PHE A 224 -1  N  PHE A 224   O  ARG A 202           
LINK         O2B ADP A 310                MG    MG A 331     1555   1555  2.39  
LINK         O3B ADP A 310                MG    MG A 330     1555   1555  2.40  
LINK         O2A ADP A 310                MG    MG A 330     1555   1555  2.10  
LINK         O4P POB A 321                MG    MG A 330     1555   1555  1.97  
LINK         O5P POB A 321                MG    MG A 331     1555   1555  2.17  
LINK        MG    MG A 330                 OD2 ASP A 257     1555   1555  1.94  
LINK        MG    MG A 331                 OE2 GLU A 270     1555   1555  2.09  
LINK        MG    MG A 331                 OD1 ASN A 272     1555   1555  2.32  
LINK        MG    MG A 332                 O   ALA A 271     1555   1555  2.28  
LINK        MG    MG A 330                 OE2 GLU A 270     1555   1555  2.84  
LINK        MG    MG A 331                 O3B ADP A 310     1555   1555  2.90  
LINK        MG    MG A 331                 O   HOH A 536     1555   1555  2.94  
LINK        MG    MG A 331                 OE1 GLU A 270     1555   1555  2.76  
LINK        MG    MG A 332                 O   HOH A 522     1555   1555  3.09  
LINK        MG    MG A 332                 O   SER A  94     1555   1555  2.55  
CISPEP   1 LEU A  139    PRO A  140          0        -1.35                     
CISPEP   2 CYS A  225    PRO A  226          0        -1.23                     
SITE     1 ADP 12 LYS A  97  LYS A 144  LYS A 215  GLU A 270                    
SITE     2 ADP 12 ASN A 272  SER A 151  GLU A 180  GLU A 187                    
SITE     3 ADP 12 TRP A 182  ALA A 159  ILE A 142  PHE A 209                    
SITE     1 LIG  6 GLU A  15  SER A 150  TYR A 216  VAL A  18                    
SITE     2 LIG  6 HIS A  63  SER A 281                                          
SITE     1 AC1  4 ASP A 257  GLU A 270  ADP A 310  POB A 321                    
SITE     1 AC2  6 GLY A 149  GLU A 270  ASN A 272  ADP A 310                    
SITE     2 AC2  6 POB A 321  HOH A 536                                          
SITE     1 AC3  4 SER A  94  GLU A 270  ALA A 271  HOH A 522                    
SITE     1 AC4 23 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC4 23 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC4 23 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC4 23 GLU A 187  TYR A 210  LYS A 215  ASP A 257                    
SITE     5 AC4 23 MET A 259  LEU A 269  GLU A 270  POB A 321                    
SITE     6 AC4 23  MG A 330   MG A 331  HOH A 511                               
SITE     1 AC5 20 GLU A  15  GLY A 149  SER A 150  TYR A 210                    
SITE     2 AC5 20 LYS A 215  TYR A 216  ARG A 255  ASP A 257                    
SITE     3 AC5 20 GLU A 270  ASN A 272  PRO A 275  GLY A 276                    
SITE     4 AC5 20 SER A 281  LEU A 282  ADP A 310   MG A 330                    
SITE     5 AC5 20  MG A 331  HOH A 508  HOH A 536  HOH A 538                    
CRYST1   98.600   51.000   51.200  90.00  90.00  90.00 P 21 21 2     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      0.010142  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019608  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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