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Database: PDB
Entry: 2DLN
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Original site: 2DLN 
HEADER    LIGASE(PEPTIDOGLYCAN SYNTHESIS)         18-JUL-94   2DLN              
TITLE     VANCOMYCIN RESISTANCE: STRUCTURE OF D-ALANINE:D-ALANINE               
TITLE    2 LIGASE AT 2.3 ANGSTROMS RESOLUTION                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.2.4                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    LIGASE(PEPTIDOGLYCAN SYNTHESIS)                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KNOX,P.C.MOEWS,C.FAN                                              
REVDAT   3   24-FEB-09 2DLN    1       VERSN                                    
REVDAT   2   01-APR-03 2DLN    1       JRNL                                     
REVDAT   1   01-NOV-95 2DLN    0                                                
JRNL        AUTH   C.FAN,P.C.MOEWS,C.T.WALSH,J.R.KNOX                           
JRNL        TITL   VANCOMYCIN RESISTANCE: STRUCTURE OF                          
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE AT 2.3 A RESOLUTION.              
JRNL        REF    SCIENCE                       V. 266   439 1994              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   7939684                                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 9776                           
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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            : 2305                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 292                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
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) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.540 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 0.950 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 0.470 ; 1.000               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 0.820 ; 1.500               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  THERE IS NO NON-CRYSTALLOGRAPHIC         
REMARK   3  SYMMETRY. A CLOSE DIMER IS FORMED BY THE TWO-FOLD DIAD OF THE       
REMARK   3  SPACE GROUP (P 21 21 2).                                            
REMARK   4                                                                      
REMARK   4 2DLN 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       49.65000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.70000            
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   OG   SER A   281     O    HOH A   654              1.61            
REMARK 500   O2   PHY A   320     O    HOH A   654              1.89            
REMARK 500   O    GLY A    34     O    HOH A   613              1.90            
REMARK 500   OG1  THR A   247     O    HOH A   646              2.08            
REMARK 500   CB   ALA A   244     O    HOH A   677              2.08            
REMARK 500   OE1  GLU A   220     O    HOH A   665              2.08            
REMARK 500   O    ASP A    69     NE2  GLN A    73              2.12            
REMARK 500   O    ASP A     3     O    HOH A   462              2.18            
REMARK 500   NH1  ARG A    99     OE1  GLU A   176              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   456     O    HOH A   644     3557     1.41            
REMARK 500   O    HOH A   450     O    HOH A   689     3557     1.62            
REMARK 500   O    HOH A   523     O    HOH A   530     3546     1.96            
REMARK 500   O    HOH A   404     O    HOH A   497     2555     2.07            
REMARK 500   O    HOH A   640     O    HOH A   641     1556     2.07            
REMARK 500   O    HOH A   593     O    HOH A   593     2565     2.09            
REMARK 500   OE1  GLU A    32     O    HOH A   541     3557     2.13            
REMARK 500   CD2  LEU A   139     NH1  ARG A   202     3546     2.17            
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. =   4.8 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A  41   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A  65   CD  -  NE  -  CZ  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    THR A  84   N   -  CA  -  C   ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ARG A  99   CD  -  NE  -  CZ  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG A  99   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    LEU A 139   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    LEU A 139   CA  -  CB  -  CG  ANGL. DEV. =  30.4 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    GLU A 176   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    LEU A 178   CA  -  CB  -  CG  ANGL. DEV. =  19.9 DEGREES          
REMARK 500    TYR A 210   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TYR A 210   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 288   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    MET A 292   CA  -  CB  -  CG  ANGL. DEV. =  10.5 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      -52.31     73.25                                   
REMARK 500    LYS A  43       32.57    -87.74                                   
REMARK 500    GLU A  44      -80.14   -160.89                                   
REMARK 500    SER A  52        0.04    -67.72                                   
REMARK 500    THR A  71      -70.42    -52.59                                   
REMARK 500    GLN A 130      -26.26   -141.75                                   
REMARK 500    ALA A 136        2.94    -66.73                                   
REMARK 500    ALA A 159      145.09     70.94                                   
REMARK 500    SER A 274       73.58   -153.15                                   
REMARK 500    MET A 277       42.63   -152.77                                   
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 404        DISTANCE =  6.67 ANGSTROMS                       
REMARK 525    HOH A 487        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A 502        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A 513        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 518        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 522        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A 536        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH A 543        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A 549        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 553        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 557        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH A 561        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A 564        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH A 566        DISTANCE =  9.67 ANGSTROMS                       
REMARK 525    HOH A 575        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  7.94 ANGSTROMS                       
REMARK 525    HOH A 590        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A 591        DISTANCE = 10.01 ANGSTROMS                       
REMARK 525    HOH A 592        DISTANCE =  9.17 ANGSTROMS                       
REMARK 525    HOH A 593        DISTANCE =  8.22 ANGSTROMS                       
REMARK 525    HOH A 594        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH A 595        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH A 596        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A 597        DISTANCE =  7.79 ANGSTROMS                       
REMARK 525    HOH A 600        DISTANCE =  8.09 ANGSTROMS                       
REMARK 525    HOH A 601        DISTANCE = 10.75 ANGSTROMS                       
REMARK 525    HOH A 602        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH A 605        DISTANCE =  7.85 ANGSTROMS                       
REMARK 525    HOH A 615        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH A 616        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH A 618        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 628        DISTANCE =  7.89 ANGSTROMS                       
REMARK 525    HOH A 629        DISTANCE =  9.76 ANGSTROMS                       
REMARK 525    HOH A 655        DISTANCE =  9.48 ANGSTROMS                       
REMARK 525    HOH A 664        DISTANCE =  9.90 ANGSTROMS                       
REMARK 525    HOH A 673        DISTANCE =  8.33 ANGSTROMS                       
REMARK 525    HOH A 674        DISTANCE =  9.36 ANGSTROMS                       
REMARK 525    HOH A 687        DISTANCE =  5.14 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 330  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHY A 320   O4P                                                    
REMARK 620 2 GLU A 270   OE2  87.6                                              
REMARK 620 3 ADP A 310   O3B  63.3  71.2                                        
REMARK 620 4 ADP A 310   O2A 134.2  58.3  76.3                                  
REMARK 620 5 ASP A 257   OD2 114.7  74.0 145.2  86.3                            
REMARK 620 N                    1     2     3     4                             
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 GLU A 270   OE2                                                    
REMARK 620 2 ADP A 310   O2B  81.6                                              
REMARK 620 3 PHY A 320   O5P  99.8  86.8                                        
REMARK 620 4 HOH A 400   O   177.3  96.3  78.3                                  
REMARK 620 5 ASN A 272   OD1 102.4 167.7  81.2  79.2                            
REMARK 620 6 GLU A 270   OE1  65.0 104.9 158.5 117.3  87.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ADP                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: PHY                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
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 ADP A 310                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHY A 320                 
DBREF  2DLN 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    ADP  A 310      27                                                       
HET    PHY  A 320      16                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PHY 1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-                     
HETNAM   2 PHY  PHOSPHINIC ACID                                                 
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  PHY    C6 H15 N O7 P2                                               
FORMUL   6  HOH   *292(H2 O)                                                    
HELIX    1  H1 GLU A   15  GLY A   34  1                                  20    
HELIX    2  H2 THR A   48  SER A   52  1                                   5    
HELIX    3  H3 THR A   71  MET A   79  1                                   9    
HELIX    4  H4 GLY A   87  ASP A   96  1                                  10    
HELIX    5  H5 LEU A   98  ALA A  107  1                                  10    
HELIX    6  H6 ARG A  119  GLY A  125  1                                   7    
HELIX    7  H7 ASP A  128  LEU A  137  1                                  10    
HELIX    8  H8 LEU A  163  HIS A  173  1                                  11    
HELIX    9  H9 TYR A  212  LEU A  217  1                                   6    
HELIX   10 H10 ALA A  231  THR A  247  1                                  17    
HELIX   11 H11 LEU A  282  GLN A  289  1                                   8    
HELIX   12 H12 PHE A  294  GLU A  303  1                                  10    
SHEET    1  SN 4 ASP A  36  ASP A  41  0                                        
SHEET    2  SN 4 LYS A   4  GLY A  11  1  N  VAL A   7   O  TYR A  38           
SHEET    3  SN 4 LYS A  57  ALA A  61  1  N  PHE A  59   O  ALA A   6           
SHEET    4  SN 4 TYR A  83  GLY A  85  1  N  THR A  84   O  VAL A  58           
SHEET    1 CEN 4 PRO A 113  LEU A 117  0                                        
SHEET    2 CEN 4 GLU A 176  LYS A 181 -1  N  ILE A 179   O  VAL A 115           
SHEET    3 CEN 4 VAL A 141  PRO A 145 -1  N  LYS A 144   O  LEU A 178           
SHEET    4 CEN 4 MET A 154  VAL A 158 -1  N  SER A 155   O  VAL A 143           
SHEET    1  SC 5 GLN A 265  ASN A 272  0                                        
SHEET    2  SC 5 TRP A 253  LEU A 260 -1  N  ASP A 257   O  GLU A 270           
SHEET    3  SC 5 PRO A 186  ILE A 192 -1  N  VAL A 190   O  ILE A 256           
SHEET    4  SC 5 ILE A 197  SER A 206 -1  N  ILE A 201   O  THR A 189           
SHEET    5  SC 5 THR A 221  CYS A 225 -1  N  PHE A 224   O  ARG A 202           
LINK         O4P PHY A 320                MG    MG A 330     1555   1555  1.88  
LINK        MG    MG A 330                 OE2 GLU A 270     1555   1555  2.72  
LINK        MG    MG A 330                 O3B ADP A 310     1555   1555  2.63  
LINK        MG    MG A 330                 O2A ADP A 310     1555   1555  2.42  
LINK        MG    MG A 330                 OD2 ASP A 257     1555   1555  1.98  
LINK        MG    MG A 331                 OE2 GLU A 270     1555   1555  1.93  
LINK        MG    MG A 331                 O2B ADP A 310     1555   1555  2.28  
LINK        MG    MG A 331                 O5P PHY A 320     1555   1555  2.29  
LINK        MG    MG A 331                 O   HOH A 400     1555   1555  1.87  
LINK        MG    MG A 331                 OD1 ASN A 272     1555   1555  2.10  
LINK        MG    MG A 331                 OE1 GLU A 270     1555   1555  2.08  
CISPEP   1 LEU A  139    PRO A  140          0         3.29                     
CISPEP   2 CYS A  225    PRO A  226          0        -2.34                     
SITE     1 ADP 15 LYS A  97  ILE A 142  LYS A 144  SER A 150                    
SITE     2 ADP 15 SER A 151  GLU A 180  TRP A 182  GLU A 187                    
SITE     3 ADP 15 PHE A 209  LYS A 215  MET A 259  GLU A 270                    
SITE     4 ADP 15 ASN A 272   MG A 330   MG A 331                               
SITE     1 PHY  6 GLU A  15  VAL A  18  HIS A  63  SER A 150                    
SITE     2 PHY  6 TYR A 216  SER A 281                                          
SITE     1 AC1  5 LYS A 215  ASP A 257  GLU A 270  ADP A 310                    
SITE     2 AC1  5 PHY A 320                                                     
SITE     1 AC2  5 GLU A 270  ASN A 272  ADP A 310  PHY A 320                    
SITE     2 AC2  5 HOH A 400                                                     
SITE     1 AC3 22 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC3 22 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC3 22 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC3 22 GLU A 187  TYR A 210  LYS A 215  ASP A 257                    
SITE     5 AC3 22 LEU A 269  GLU A 270  PHY A 320   MG A 330                    
SITE     6 AC3 22  MG A 331  HOH A 413                                          
SITE     1 AC4 21 GLU A  15  GLY A 149  SER A 150  LYS A 215                    
SITE     2 AC4 21 TYR A 216  ARG A 255  ASP A 257  GLU A 270                    
SITE     3 AC4 21 ASN A 272  PRO A 275  GLY A 276  SER A 281                    
SITE     4 AC4 21 LEU A 282  ADP A 310   MG A 330   MG A 331                    
SITE     5 AC4 21 HOH A 400  HOH A 430  HOH A 531  HOH A 637                    
SITE     6 AC4 21 HOH A 654                                                     
CRYST1   99.300   51.400   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      0.010070  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019531        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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