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Database: PDB
Entry: 1EHI
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Original site: 1EHI 
HEADER    LIGASE                                  21-FEB-00   1EHI              
TITLE     D-ALANINE:D-LACTATE LIGASE (LMDDL2) OF VANCOMYCIN-RESISTANT           
TITLE    2 LEUCONOSTOC MESENTEROIDES                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE:D-LACTATE LIGASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: LMDDL2;                                                     
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEUCONOSTOC MESENTEROIDES;                      
SOURCE   3 ORGANISM_TAXID: 1245;                                                
SOURCE   4 ATCC: 8293;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5A AND BL21(DE3);                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PLMDDL2                                   
KEYWDS    ATP-BINDING. GRASP MOTIF FOR ATP., LIGASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.KUZIN,T.SUN,J.JORCZAK-BAILLASS,V.L.HEALY,C.T.WALSH,               
AUTHOR   2 J.R.KNOX                                                             
REVDAT   2   24-FEB-09 1EHI    1       VERSN                                    
REVDAT   1   23-MAY-00 1EHI    0                                                
JRNL        AUTH   A.P.KUZIN,T.SUN,J.JORCZAK-BAILLASS,V.L.HEALY,                
JRNL        AUTH 2 C.T.WALSH,J.R.KNOX                                           
JRNL        TITL   ENZYMES OF VANCOMYCIN RESISTANCE: THE STRUCTURE OF           
JRNL        TITL 2 D-ALANINE-D-LACTATE LIGASE OF NATURALLY RESISTANT            
JRNL        TITL 3 LEUCONOSTOC MESENTEROIDES.                                   
JRNL        REF    STRUCTURE FOLD.DES.           V.   8   463 2000              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10801495                                                     
JRNL        DOI    10.1016/S0969-2126(00)00129-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
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   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.FAN,I.-S.PARK,C.T.WALSH,J.R.KNOX                           
REMARK   1  TITL   D-ALANINE:D-ALANINE LIGASE: PHOSPHONATE AND                  
REMARK   1  TITL 2 PHOSPHINATE INTERMEDIATES WITH WILD-TYPE AND THE             
REMARK   1  TITL 3 Y216F MUTANT                                                 
REMARK   1  REF    BIOCHEMISTRY                  V.  36  2531 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI962431T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 27948                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 951                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5531                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT CORRECTION. A 3-             
REMARK   3  WAVELENGTH MAD METHOD WAS USED TO DETERMINE STRUCTURE OF THE        
REMARK   3  SELENOMET-PROTEIN. A NATIVE DATA SET (A1 AT CHESS) WAS USED TO      
REMARK   3  REFINE STRUCTURE.                                                   
REMARK   4                                                                      
REMARK   4 1EHI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010577.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.908                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL (DENZO)                        
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30564                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.0                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 47.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 3-WAVELENGTH MAD NEAR        
REMARK 200  SE EDGE (X12C AT BNL)                                               
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000 15%, 0.1 M AMMONIUM              
REMARK 280  SULFATE, 50MM NACL, 2.4MM DTT, 1MM MGCL2, 3MM ATP, 3MM              
REMARK 280  PHOSPHINIC ACID, 50MM MES BUFFER., PH 6.5, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       59.10000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.10000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.40000            
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 300 REMARK: THE LIGASE IS A DIMER FORMED OF CHAIN A AND B. HOWEVER,      
REMARK 300 PART OF CHAIN B IS MISSING IN THE CRYSTALLOGRAPHIC MODEL.            
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     TYR A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     PHE A   365                                                      
REMARK 465     VAL A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     LEU A   368                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     GLU A   371                                                      
REMARK 465     LYS A   372                                                      
REMARK 465     ILE A   373                                                      
REMARK 465     GLY A   374                                                      
REMARK 465     LYS A   375                                                      
REMARK 465     PHE A   376                                                      
REMARK 465     ASN A   377                                                      
REMARK 465     MET B   401                                                      
REMARK 465     VAL B   645                                                      
REMARK 465     PRO B   646                                                      
REMARK 465     ASN B   647                                                      
REMARK 465     GLN B   648                                                      
REMARK 465     GLY B   649                                                      
REMARK 465     SER B   650                                                      
REMARK 465     GLY B   651                                                      
REMARK 465     ASP B   652                                                      
REMARK 465     GLY B   653                                                      
REMARK 465     TRP B   654                                                      
REMARK 465     TYR B   655                                                      
REMARK 465     ASP B   656                                                      
REMARK 465     TYR B   657                                                      
REMARK 465     ASN B   658                                                      
REMARK 465     ASN B   659                                                      
REMARK 465     LYS B   660                                                      
REMARK 465     PHE B   661                                                      
REMARK 465     VAL B   662                                                      
REMARK 465     ASP B   663                                                      
REMARK 465     ASN B   664                                                      
REMARK 465     SER B   665                                                      
REMARK 465     ALA B   666                                                      
REMARK 465     GLU B   771                                                      
REMARK 465     LYS B   772                                                      
REMARK 465     ILE B   773                                                      
REMARK 465     GLY B   774                                                      
REMARK 465     LYS B   775                                                      
REMARK 465     PHE B   776                                                      
REMARK 465     ASN B   777                                                      
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 B 770    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  61       11.93    -65.16                                   
REMARK 500    LEU A  82       30.33    -99.89                                   
REMARK 500    SER A  90       16.46    -63.80                                   
REMARK 500    ALA A  91        7.76   -153.80                                   
REMARK 500    SER A 186       15.43     57.43                                   
REMARK 500    PHE A 207        7.04    -64.49                                   
REMARK 500    ASN A 232      -98.03   -111.02                                   
REMARK 500    SER A 250       43.95    -86.56                                   
REMARK 500    SER A 265       10.33    -69.59                                   
REMARK 500    PHE A 323       36.85   -144.16                                   
REMARK 500    LEU A 361       30.25    -66.45                                   
REMARK 500    LYS B 403      -64.30   -157.31                                   
REMARK 500    ASN B 413       46.82    -82.68                                   
REMARK 500    GLU B 416       34.92    -98.75                                   
REMARK 500    LEU B 462       21.34     85.05                                   
REMARK 500    VAL B 500       39.45   -145.72                                   
REMARK 500    ASN B 504       22.76    -73.75                                   
REMARK 500    LEU B 505      -37.44   -136.76                                   
REMARK 500    GLN B 584      153.19    179.28                                   
REMARK 500    SER B 586      -29.22     66.13                                   
REMARK 500    SER B 587      -74.35   -158.93                                   
REMARK 500    ALA B 622       67.66   -113.71                                   
REMARK 500    ASN B 632     -105.04   -120.15                                   
REMARK 500    SER B 638     -178.74    -69.24                                   
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 783  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 316   OE1                                                    
REMARK 620 2 GLU A 316   OE2  49.4                                              
REMARK 620 3 ASN A 318   OD1 109.1  76.3                                        
REMARK 620 4 PHY A 782   O5P 145.1 100.6  73.0                                  
REMARK 620 5 ADP A 781   O3B  64.9  92.0 167.4 105.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 784  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 781   O2B                                                    
REMARK 620 2 ADP A 781   O2A  76.4                                              
REMARK 620 3 PHY A 782   O4P  69.1 132.0                                        
REMARK 620 4 GLU A 316   OE2  81.0  61.4  80.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 783                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 784                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 781                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHY A 782                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DLN   RELATED DB: PDB                                   
REMARK 900 D-ALANINE:D-ALANINE LIGASE (DDLB) OF E. COLI COMPLEXED WITH          
REMARK 900 PHOSPHINATE AND ADP                                                  
REMARK 900 RELATED ID: 1IOV   RELATED DB: PDB                                   
REMARK 900 DDLB LIGASE WITH PHOSPHONATE AND ADP                                 
REMARK 900 RELATED ID: 1IOW   RELATED DB: PDB                                   
REMARK 900 DDLB Y215F MUTANT WITH PHOSPHINATE AND ADP                           
DBREF  1EHI A    1   377  UNP    P71454   P71454_LEUME     1    377             
DBREF  1EHI B  401   777  UNP    P71454   P71454_LEUME     1    377             
SEQADV 1EHI GLN A  270  UNP  P71454    GLU   270 CONFLICT                       
SEQADV 1EHI GLN B  670  UNP  P71454    GLU   270 CONFLICT                       
SEQRES   1 A  377  MET THR LYS LYS ARG VAL ALA LEU ILE PHE GLY GLY ASN          
SEQRES   2 A  377  SER SER GLU HIS ASP VAL SER LYS ARG SER ALA GLN ASN          
SEQRES   3 A  377  PHE TYR ASN ALA ILE GLU ALA THR GLY LYS TYR GLU ILE          
SEQRES   4 A  377  ILE VAL PHE ALA ILE ALA GLN ASN GLY PHE PHE LEU ASP          
SEQRES   5 A  377  THR GLU SER SER LYS LYS ILE LEU ALA LEU GLU ASP GLU          
SEQRES   6 A  377  GLN PRO ILE VAL ASP ALA PHE MET LYS THR VAL ASP ALA          
SEQRES   7 A  377  SER ASP PRO LEU ALA ARG ILE HIS ALA LEU LYS SER ALA          
SEQRES   8 A  377  GLY ASP PHE ASP ILE PHE PHE PRO VAL VAL HIS GLY ASN          
SEQRES   9 A  377  LEU GLY GLU ASP GLY THR LEU GLN GLY LEU PHE LYS LEU          
SEQRES  10 A  377  LEU ASP LYS PRO TYR VAL GLY ALA PRO LEU ARG GLY HIS          
SEQRES  11 A  377  ALA VAL SER PHE ASP LYS ALA LEU THR LYS GLU LEU LEU          
SEQRES  12 A  377  THR VAL ASN GLY ILE ARG ASN THR LYS TYR ILE VAL VAL          
SEQRES  13 A  377  ASP PRO GLU SER ALA ASN ASN TRP SER TRP ASP LYS ILE          
SEQRES  14 A  377  VAL ALA GLU LEU GLY ASN ILE VAL PHE VAL LYS ALA ALA          
SEQRES  15 A  377  ASN GLN GLY SER SER VAL GLY ILE SER ARG VAL THR ASN          
SEQRES  16 A  377  ALA GLU GLU TYR THR GLU ALA LEU SER ASP SER PHE GLN          
SEQRES  17 A  377  TYR ASP TYR LYS VAL LEU ILE GLU GLU ALA VAL ASN GLY          
SEQRES  18 A  377  ALA ARG GLU LEU GLU VAL GLY VAL ILE GLY ASN ASP GLN          
SEQRES  19 A  377  PRO LEU VAL SER GLU ILE GLY ALA HIS THR VAL PRO ASN          
SEQRES  20 A  377  GLN GLY SER GLY ASP GLY TRP TYR ASP TYR ASN ASN LYS          
SEQRES  21 A  377  PHE VAL ASP ASN SER ALA VAL HIS PHE GLN ILE PRO ALA          
SEQRES  22 A  377  GLN LEU SER PRO GLU VAL THR LYS GLU VAL LYS GLN MET          
SEQRES  23 A  377  ALA LEU ASP ALA TYR LYS VAL LEU ASN LEU ARG GLY GLU          
SEQRES  24 A  377  ALA ARG MET ASP PHE LEU LEU ASP GLU ASN ASN VAL PRO          
SEQRES  25 A  377  TYR LEU GLY GLU PRO ASN THR LEU PRO GLY PHE THR ASN          
SEQRES  26 A  377  MET SER LEU PHE LYS ARG LEU TRP ASP TYR SER ASP ILE          
SEQRES  27 A  377  ASN ASN ALA LYS LEU VAL ASP MET LEU ILE ASP TYR GLY          
SEQRES  28 A  377  PHE GLU ASP PHE ALA GLN ASN LYS LYS LEU SER TYR SER          
SEQRES  29 A  377  PHE VAL SER LEU GLY GLU GLU LYS ILE GLY LYS PHE ASN          
SEQRES   1 B  377  MET THR LYS LYS ARG VAL ALA LEU ILE PHE GLY GLY ASN          
SEQRES   2 B  377  SER SER GLU HIS ASP VAL SER LYS ARG SER ALA GLN ASN          
SEQRES   3 B  377  PHE TYR ASN ALA ILE GLU ALA THR GLY LYS TYR GLU ILE          
SEQRES   4 B  377  ILE VAL PHE ALA ILE ALA GLN ASN GLY PHE PHE LEU ASP          
SEQRES   5 B  377  THR GLU SER SER LYS LYS ILE LEU ALA LEU GLU ASP GLU          
SEQRES   6 B  377  GLN PRO ILE VAL ASP ALA PHE MET LYS THR VAL ASP ALA          
SEQRES   7 B  377  SER ASP PRO LEU ALA ARG ILE HIS ALA LEU LYS SER ALA          
SEQRES   8 B  377  GLY ASP PHE ASP ILE PHE PHE PRO VAL VAL HIS GLY ASN          
SEQRES   9 B  377  LEU GLY GLU ASP GLY THR LEU GLN GLY LEU PHE LYS LEU          
SEQRES  10 B  377  LEU ASP LYS PRO TYR VAL GLY ALA PRO LEU ARG GLY HIS          
SEQRES  11 B  377  ALA VAL SER PHE ASP LYS ALA LEU THR LYS GLU LEU LEU          
SEQRES  12 B  377  THR VAL ASN GLY ILE ARG ASN THR LYS TYR ILE VAL VAL          
SEQRES  13 B  377  ASP PRO GLU SER ALA ASN ASN TRP SER TRP ASP LYS ILE          
SEQRES  14 B  377  VAL ALA GLU LEU GLY ASN ILE VAL PHE VAL LYS ALA ALA          
SEQRES  15 B  377  ASN GLN GLY SER SER VAL GLY ILE SER ARG VAL THR ASN          
SEQRES  16 B  377  ALA GLU GLU TYR THR GLU ALA LEU SER ASP SER PHE GLN          
SEQRES  17 B  377  TYR ASP TYR LYS VAL LEU ILE GLU GLU ALA VAL ASN GLY          
SEQRES  18 B  377  ALA ARG GLU LEU GLU VAL GLY VAL ILE GLY ASN ASP GLN          
SEQRES  19 B  377  PRO LEU VAL SER GLU ILE GLY ALA HIS THR VAL PRO ASN          
SEQRES  20 B  377  GLN GLY SER GLY ASP GLY TRP TYR ASP TYR ASN ASN LYS          
SEQRES  21 B  377  PHE VAL ASP ASN SER ALA VAL HIS PHE GLN ILE PRO ALA          
SEQRES  22 B  377  GLN LEU SER PRO GLU VAL THR LYS GLU VAL LYS GLN MET          
SEQRES  23 B  377  ALA LEU ASP ALA TYR LYS VAL LEU ASN LEU ARG GLY GLU          
SEQRES  24 B  377  ALA ARG MET ASP PHE LEU LEU ASP GLU ASN ASN VAL PRO          
SEQRES  25 B  377  TYR LEU GLY GLU PRO ASN THR LEU PRO GLY PHE THR ASN          
SEQRES  26 B  377  MET SER LEU PHE LYS ARG LEU TRP ASP TYR SER ASP ILE          
SEQRES  27 B  377  ASN ASN ALA LYS LEU VAL ASP MET LEU ILE ASP TYR GLY          
SEQRES  28 B  377  PHE GLU ASP PHE ALA GLN ASN LYS LYS LEU SER TYR SER          
SEQRES  29 B  377  PHE VAL SER LEU GLY GLU GLU LYS ILE GLY LYS PHE ASN          
HET     MG  A 783       1                                                       
HET     MG  A 784       1                                                       
HET    ADP  A 781      27                                                       
HET    PHY  A 782      16                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PHY 1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-                     
HETNAM   2 PHY  PHOSPHINIC ACID                                                 
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  PHY    C6 H15 N O7 P2                                               
FORMUL   7  HOH   *213(H2 O)                                                    
HELIX    1   1 GLU A   16  GLY A   35  1                                  20    
HELIX    2   2 ASP A   52  ALA A   61  1                                  10    
HELIX    3   3 ASP A   64  LYS A   74  1                                  11    
HELIX    4   4 ILE A   85  SER A   90  5                                   6    
HELIX    5   5 GLY A  109  LEU A  118  1                                  10    
HELIX    6   6 PRO A  126  ASP A  135  1                                  10    
HELIX    7   7 ASP A  135  VAL A  145  1                                  11    
HELIX    8   8 GLU A  159  TRP A  164  5                                   6    
HELIX    9   9 SER A  165  GLY A  174  1                                  10    
HELIX   10  10 ASN A  195  PHE A  207  1                                  13    
HELIX   11  11 ASP A  256  PHE A  261  1                                   6    
HELIX   12  12 SER A  276  LEU A  294  1                                  19    
HELIX   13  13 SER A  327  ARG A  331  5                                   5    
HELIX   14  14 ARG A  331  ASP A  337  5                                   7    
HELIX   15  15 ASN A  339  LEU A  361  1                                  23    
HELIX   16  16 GLU B  416  ALA B  433  1                                  18    
HELIX   17  17 ASP B  452  ALA B  461  1                                  10    
HELIX   18  18 ASP B  464  LYS B  474  1                                  11    
HELIX   19  19 LEU B  482  ALA B  487  1                                   6    
HELIX   20  20 GLY B  509  LEU B  518  1                                  10    
HELIX   21  21 PRO B  526  ASP B  535  1                                  10    
HELIX   22  22 ASP B  535  ASN B  546  1                                  12    
HELIX   23  23 GLU B  559  TRP B  564  5                                   6    
HELIX   24  24 SER B  565  LEU B  573  1                                   9    
HELIX   25  25 ASN B  595  PHE B  607  1                                  13    
HELIX   26  26 SER B  676  LEU B  694  1                                  19    
HELIX   27  27 SER B  727  ARG B  731  5                                   5    
HELIX   28  28 LEU B  732  ASP B  737  5                                   6    
HELIX   29  29 ASN B  739  LYS B  759  1                                  21    
SHEET    1   A 3 TYR A  37  ILE A  44  0                                        
SHEET    2   A 3 LYS A   4  GLY A  11  1  O  LYS A   4   N  GLU A  38           
SHEET    3   A 3 ILE A  96  VAL A 100  1  O  ILE A  96   N  ALA A   7           
SHEET    1   B 4 TYR A 153  VAL A 156  0                                        
SHEET    2   B 4 VAL A 213  GLU A 217 -1  N  VAL A 213   O  VAL A 156           
SHEET    3   B 4 VAL A 177  ALA A 181 -1  N  PHE A 178   O  GLU A 216           
SHEET    4   B 4 ILE A 190  VAL A 193 -1  N  SER A 191   O  VAL A 179           
SHEET    1   C 5 HIS A 268  GLN A 270  0                                        
SHEET    2   C 5 LEU A 236  THR A 244 -1  N  ALA A 242   O  GLN A 270           
SHEET    3   C 5 GLU A 224  GLY A 231 -1  N  GLU A 224   O  HIS A 243           
SHEET    4   C 5 GLY A 298  LEU A 306 -1  O  GLY A 298   N  GLY A 231           
SHEET    5   C 5 PRO A 312  ASN A 318 -1  N  TYR A 313   O  LEU A 305           
SHEET    1   D 4 PHE B 450  LEU B 451  0                                        
SHEET    2   D 4 TYR B 437  ILE B 444 -1  O  ALA B 443   N  LEU B 451           
SHEET    3   D 4 LYS B 404  GLY B 411  1  O  LYS B 404   N  GLU B 438           
SHEET    4   D 4 ILE B 496  PRO B 499  1  O  ILE B 496   N  ALA B 407           
SHEET    1   E 4 TYR B 553  VAL B 556  0                                        
SHEET    2   E 4 VAL B 613  GLU B 617 -1  O  VAL B 613   N  VAL B 556           
SHEET    3   E 4 VAL B 577  ALA B 581 -1  N  PHE B 578   O  GLU B 616           
SHEET    4   E 4 SER B 591  VAL B 593 -1  N  SER B 591   O  VAL B 579           
SHEET    1   F 5 PHE B 669  GLN B 670  0                                        
SHEET    2   F 5 LEU B 636  HIS B 643 -1  O  ALA B 642   N  GLN B 670           
SHEET    3   F 5 ARG B 623  GLY B 631 -1  O  GLU B 624   N  HIS B 643           
SHEET    4   F 5 GLY B 698  LEU B 706 -1  N  GLY B 698   O  GLY B 631           
SHEET    5   F 5 PRO B 712  ASN B 718 -1  N  TYR B 713   O  LEU B 705           
LINK        MG    MG A 783                 OE1 GLU A 316     1555   1555  2.31  
LINK        MG    MG A 783                 OE2 GLU A 316     1555   1555  2.83  
LINK        MG    MG A 783                 OD1 ASN A 318     1555   1555  2.54  
LINK        MG    MG A 783                 O5P PHY A 782     1555   1555  2.20  
LINK        MG    MG A 783                 O3B ADP A 781     1555   1555  2.48  
LINK        MG    MG A 784                 O2B ADP A 781     1555   1555  2.51  
LINK        MG    MG A 784                 O2A ADP A 781     1555   1555  2.66  
LINK        MG    MG A 784                 O4P PHY A 782     1555   1555  2.25  
LINK        MG    MG A 784                 OE2 GLU A 316     1555   1555  2.65  
CISPEP   1 ILE A  271    PRO A  272          0        -0.09                     
CISPEP   2 ILE B  671    PRO B  672          0        -0.01                     
SITE     1 AC1  4 GLU A 316  ASN A 318  ADP A 781  PHY A 782                    
SITE     1 AC2  4 ASP A 303  GLU A 316  ADP A 781  PHY A 782                    
SITE     1 AC3 22 THR A 151  PHE A 178  LYS A 180  GLN A 184                    
SITE     2 AC3 22 GLY A 185  SER A 186  SER A 187  ILE A 190                    
SITE     3 AC3 22 GLU A 216  GLU A 217  ALA A 218  VAL A 219                    
SITE     4 AC3 22 GLU A 224  TRP A 254  TYR A 255  LYS A 260                    
SITE     5 AC3 22 LEU A 305  GLU A 316  PHY A 782   MG A 783                    
SITE     6 AC3 22  MG A 784  HOH A 847                                          
SITE     1 AC4 17 GLU A  16  SER A 186  LYS A 260  PHE A 261                    
SITE     2 AC4 17 ARG A 301  ASP A 303  GLU A 316  ASN A 318                    
SITE     3 AC4 17 GLY A 322  MET A 326  SER A 327  ADP A 781                    
SITE     4 AC4 17  MG A 783   MG A 784  HOH A 824  HOH A 834                    
SITE     5 AC4 17 HOH A 924                                                     
CRYST1  118.200   90.800   82.100  90.00  92.10  90.00 C 1 2 1       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      0.008460  0.000000  0.000310        0.00000                         
SCALE2      0.000000  0.011013  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012188        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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