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Database: PDB
Entry: 1IOW
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HEADER    LIGASE                                  20-SEP-96   1IOW              
TITLE     COMPLEX OF Y216F D-ALA:D-ALA LIGASE WITH ADP AND A                    
TITLE    2 PHOSPHORYL PHOSPHINATE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALA\:D-ALA LIGASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DD-LIGASE, DDLB;                                            
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K12 SUBSTR. W3110;          
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 316407;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: W3110;                                     
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PTB2;                                     
SOURCE   8 EXPRESSION_SYSTEM_GENE: DDLB;                                        
SOURCE   9 OTHER_DETAILS: ENZYME PROVIDED BY C.T. WALSH, HARVARD MED            
SOURCE  10 SCHOOL. SEE SHI AND WALSH, BIOCHEM. 34, P. 2768, 1995.               
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 1IOW    1       VERSN                                    
REVDAT   3   01-APR-03 1IOW    1       JRNL                                     
REVDAT   2   30-NOV-99 1IOW    1       JRNL   HEADER                            
REVDAT   1   12-FEB-97 1IOW    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.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 12800                          
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 SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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) : 1.94                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.14                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 41.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2735                         
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            : 2293                                    
REMARK   3   NUCLEIC ACID ATOMS       : 27                                      
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 250                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.60                          
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  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) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1IOW 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               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
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   : 15352                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940                              
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) : 0.05300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 41.0                               
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: X-PLOR                                                
REMARK 200 STARTING MODEL: 2DLN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.38                                     
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       49.90000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.85000            
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: 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    LEU A 229   CA  -  CB  -  CG  ANGL. DEV. =  14.3 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    ASP A   3       73.41    122.03                                   
REMARK 500    SER A 127       84.59    -51.72                                   
REMARK 500    ASP A 128      -34.77      0.92                                   
REMARK 500    ARG A 147       54.11   -112.81                                   
REMARK 500    ALA A 159      138.86     72.69                                   
REMARK 500    PRO A 186      176.81    -59.52                                   
REMARK 500    TYR A 210       74.95    -69.61                                   
REMARK 500    THR A 278     -174.16    -69.34                                   
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 464        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A 467        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 492        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A 500        DISTANCE =  8.51 ANGSTROMS                       
REMARK 525    HOH A 503        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH A 523        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH A 527        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 528        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH A 537        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 541        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A 543        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH A 548        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 551        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH A 555        DISTANCE =  9.38 ANGSTROMS                       
REMARK 525    HOH A 559        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 563        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH A 569        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 574        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH A 577        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 579        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A 596        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH A 603        DISTANCE =  9.40 ANGSTROMS                       
REMARK 525    HOH A 605        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A 616        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH A 622        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A 624        DISTANCE =  8.31 ANGSTROMS                       
REMARK 525    HOH A 627        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A 642        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  8.46 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 ADP A 310   O2A  83.3                                              
REMARK 620 3 PHY A 320   O4P  83.3 163.5                                        
REMARK 620 4 ASP A 257   OD2 172.0  99.1  95.4                                  
REMARK 620 5 HOH A 407   O    98.3  85.0  87.4  89.5                            
REMARK 620 6 GLU A 270   OE2  86.3  87.7 101.0  86.2 170.8                      
REMARK 620 N                    1     2     3     4     5                       
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 PHY A 320   O5P  93.1                                              
REMARK 620 3 GLU A 270   OE2  88.7 110.2                                        
REMARK 620 4 ASN A 272   OD1 168.9  81.5 102.2                                  
REMARK 620 5 HOH A 401   O    89.5  97.9 151.9  81.7                            
REMARK 620 6 GLU A 270   OE1  97.3 163.4  57.3  90.2  95.2                      
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: 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 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  1IOW A    2   306  UNP    P07862   DDLB_ECOLI       1    305             
SEQADV 1IOW PHE A  216  UNP  P07862    TYR   215 ENGINEERED                     
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 PHE 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   *250(H2 O)                                                    
HELIX    1   1 ARG A   16  GLU A   32  1                                  17    
HELIX    2   2 VAL A   47  GLN A   49  5                                   3    
HELIX    3   3 THR A   71  MET A   79  1                                   9    
HELIX    4   4 VAL A   88  MET A   95  1                                   8    
HELIX    5   5 LYS A   97  GLY A  106  1                                  10    
HELIX    6   6 ARG A  119  LYS A  124  1                                   6    
HELIX    7   7 LYS A  129  LEU A  137  1                                   9    
HELIX    8   8 GLU A  160  GLN A  172  5                                  13    
HELIX    9   9 TYR A  212  PHE A  216  1                                   5    
HELIX   10  10 ALA A  231  LEU A  248  1                                  18    
HELIX   11  11 LEU A  282  GLN A  289  1                                   8    
HELIX   12  12 PHE A  294  GLU A  303  1                                  10    
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  ILE A  60  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  2.24  
LINK         O3B ADP A 310                MG    MG A 330     1555   1555  2.02  
LINK         O2A ADP A 310                MG    MG A 331     1555   1555  2.33  
LINK         O4P PHY A 320                MG    MG A 331     1555   1555  2.03  
LINK         O5P PHY A 320                MG    MG A 330     1555   1555  2.04  
LINK        MG    MG A 330                 OE2 GLU A 270     1555   1555  1.87  
LINK        MG    MG A 330                 OD1 ASN A 272     1555   1555  2.26  
LINK        MG    MG A 331                 OD2 ASP A 257     1555   1555  2.07  
LINK        MG    MG A 330                 O   HOH A 401     1555   1555  2.16  
LINK        MG    MG A 330                 OE1 GLU A 270     1555   1555  2.55  
LINK        MG    MG A 331                 O   HOH A 407     1555   1555  1.95  
LINK        MG    MG A 331                 OE2 GLU A 270     1555   1555  2.51  
CISPEP   1 LEU A  139    PRO A  140          0        -0.48                     
CISPEP   2 GLY A  185    PRO A  186          0         0.16                     
CISPEP   3 CYS A  225    PRO A  226          0         0.55                     
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  7 GLU A  15  SER A 150  PHE A 216  VAL A  18                    
SITE     2 LIG  7 HIS A  63  SER A 281  ARG A 255                               
SITE     1 AC1  6 GLU A 270  ASN A 272  ADP A 310  PHY A 320                    
SITE     2 AC1  6  MG A 331  HOH A 401                                          
SITE     1 AC2  6 ASP A 257  GLU A 270  ADP A 310  PHY A 320                    
SITE     2 AC2  6  MG A 330  HOH A 407                                          
SITE     1 AC3 26 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC3 26 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC3 26 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC3 26 GLU A 187  PHE A 209  TYR A 210  LYS A 215                    
SITE     5 AC3 26 ASP A 257  MET A 259  GLU A 270  PHY A 320                    
SITE     6 AC3 26  MG A 330   MG A 331  HOH A 401  HOH A 407                    
SITE     7 AC3 26 HOH A 443  HOH A 449                                          
SITE     1 AC4 17 GLU A  15  SER A 150  LYS A 215  ARG A 255                    
SITE     2 AC4 17 ASP A 257  GLU A 270  ASN A 272  PRO A 275                    
SITE     3 AC4 17 GLY A 276  SER A 281  LEU A 282  ADP A 310                    
SITE     4 AC4 17  MG A 330   MG A 331  HOH A 405  HOH A 407                    
SITE     5 AC4 17 HOH A 410                                                     
CRYST1   99.800   51.700   51.700  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      0.010020  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019342  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019342        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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