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Database: PDB
Entry: 1EE1
LinkDB: 1EE1
Original site: 1EE1 
HEADER    LIGASE                                  28-JAN-00   1EE1              
TITLE     CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS      
TITLE    2 SUBTILIS COMPLEXED WITH ONE MOLECULE ATP, TWO MOLECULES DEAMIDO-NAD+ 
TITLE    3 AND ONE MG2+ ION                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NH(3)-DEPENDENT NAD(+) SYNTHETASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NAD(+) SYNTHETASE;                                          
COMPND   5 EC: 6.3.5.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: NADE;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LYASE, AMIDOTRANSFERASE, NH3 DEPENDENT, ATP PYROPHOSPHATASE, LIGASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.DEVEDJIEV,J.SYMERSKY,R.SINGH,M.JEDRZEJAS,C.BROUILLETTE,             
AUTHOR   2 W.BROUILLETTE,D.MUCCIO,D.CHATTOPADHYAY,L.DELUCAS                     
REVDAT   5   07-FEB-24 1EE1    1       REMARK LINK                              
REVDAT   4   04-OCT-17 1EE1    1       REMARK                                   
REVDAT   3   24-FEB-09 1EE1    1       VERSN                                    
REVDAT   2   01-APR-03 1EE1    1       JRNL                                     
REVDAT   1   06-JUN-01 1EE1    0                                                
JRNL        AUTH   Y.DEVEDJIEV,J.SYMERSKY,R.SINGH,M.JEDRZEJAS,C.BROUILLETTE,    
JRNL        AUTH 2 W.BROUILLETTE,D.MUCCIO,D.CHATTOPADHYAY,L.DELUCAS             
JRNL        TITL   STABILIZATION OF ACTIVE-SITE LOOPS IN NH3-DEPENDENT NAD+     
JRNL        TITL 2 SYNTHETASE FROM BACILLUS SUBTILIS.                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   806 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11375500                                                     
JRNL        DOI    10.1107/S0907444901003523                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.DEVEDJIEV,R.SINGH,C.BROUILLETTE,D.MUCCIO,W.BROUILLETTE,    
REMARK   1  AUTH 2 L.DELUCAS,M.JEDZEJAS                                         
REMARK   1  TITL   ASYMMETRIC COMPLEX OF NAD+ SYNTHETASE WITH NATURAL           
REMARK   1  TITL 2 SUBSTRATES ATP DEAMIDO-NAD+                                  
REMARK   1  REF    AM.CRYST.ASSOC.,ABSTR.PAPERS               1997              
REMARK   1  REF  2 (SUMMER MEETING)                                             
REMARK   1  REFN                   ISSN 0569-4221                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.DEVEDJIEV,R.SINGH,C.BROUILLETTE,D.MUCCIO,W.BROUILLETTE,    
REMARK   1  AUTH 2 L.DELUCAS,M.JEDZEJAS                                         
REMARK   1  TITL   CATALYTIC CYCLE OF NAD+ SYNTHETASE VIEWED BY X-RAY           
REMARK   1  TITL 2 STRUCTURES OF KINETIC INTERMEDIATES                          
REMARK   1  REF    AM.CRYST.ASSOC.,ABSTR.PAPERS               1998              
REMARK   1  REF  2 (SUMMER MEETING)                                             
REMARK   1  REFN                   ISSN 0569-4221                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.06 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) : 2.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 23848                          
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) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1240                            
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            : 4068                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 397                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.30                          
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.070                           
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: USED WEIGHTED LEAST SQUARES PROCEDURE.    
REMARK   3                                                                      
REMARK   3  ALL PORTIONS OF THE BACKBONE IN SUBUNIT A ARE WELL ORDERED.         
REMARK   3  HOWEVER, BACKBONE ATOMS AND THE SIDE CHAINS OF RESIDUES             
REMARK   3  83-86 AND 205-225 IN SUBUNIT B ARE NOT VISIBLE ON THE               
REMARK   3  ELECTRON DENSITY MAP. THE NICOTINIC ACID MOIETY OF                  
REMARK   3  DEAMIDO-NAD BOUND TO SUBUNIT B IS DISORDERED AS WELL,               
REMARK   3  THOUGH THE REMAINDER OF THE SUBSTRATE IS WELL ORDERED.              
REMARK   3  COORDINATES OF THE NICOTINIC ACID MOIETY IN SUBUNIT B               
REMARK   3  ARE PRESENTED FOR REFERENCE. ATP BINDING SITE IN                    
REMARK   3  SUBUNIT A IS FULLY OCCUPIED, HOWEVER, NO BINDING OF ATP             
REMARK   3  AND MG2+ WAS FOUND IN SUBUNIT B.                                    
REMARK   4                                                                      
REMARK   4 1EE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000010480.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33464                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, SODIUM ACETATE, MAGNESIUM        
REMARK 280  CHLORIDE, ADENOSINE TRIPHOSPHATE, DEAMIDO-NAD+, PH 5.2, VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 298.0K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       43.34500            
REMARK 290   SMTRY3   2  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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     THR B    83                                                      
REMARK 465     GLN B    84                                                      
REMARK 465     GLN B    85                                                      
REMARK 465     ASP B    86                                                      
REMARK 465     LYS B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     PRO B   207                                                      
REMARK 465     THR B   208                                                      
REMARK 465     ALA B   209                                                      
REMARK 465     ASP B   210                                                      
REMARK 465     LEU B   211                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     GLU B   214                                                      
REMARK 465     LYS B   215                                                      
REMARK 465     PRO B   216                                                      
REMARK 465     GLN B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     ASP B   220                                                      
REMARK 465     GLU B   221                                                      
REMARK 465     THR B   222                                                      
REMARK 465     GLU B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     GLY B   225                                                      
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 178   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LEU B 178   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
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 A5500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 208   O                                                      
REMARK 620 2 HOH A2381   O    99.1                                              
REMARK 620 3 HOH A2382   O   118.5 120.1                                        
REMARK 620 4 ATP A5000   O2B 136.7  90.8  91.1                                  
REMARK 620 5 ATP A5000   O3G  71.8  75.8 156.3  70.0                            
REMARK 620 6 ATP A5000   O1A  79.8 150.0  85.1  71.6  75.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 5500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DND A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DND B 3000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 5000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NSY   RELATED DB: PDB                                   
REMARK 900 1NSY CONTAINS THE SAME PROTEIN COMPLEXED WITH 2 MOL AMP, TWO PP -    
REMARK 900 IONS, TWO MOLECULES ATP AND TWO MG2+ IONS                            
REMARK 900 RELATED ID: 1IFX   RELATED DB: PDB                                   
REMARK 900 ONTAINS THE SAME PROTEIN COMPEXED WITH TWO MOLECULES DEAMIDO-NAD     
DBREF  1EE1 A    1   271  UNP    P08164   NADE_BACSU       2    272             
DBREF  1EE1 B    1   271  UNP    P08164   NADE_BACSU       2    272             
SEQRES   1 A  271  SER MET GLN GLU LYS ILE MET ARG GLU LEU HIS VAL LYS          
SEQRES   2 A  271  PRO SER ILE ASP PRO LYS GLN GLU ILE GLU ASP ARG VAL          
SEQRES   3 A  271  ASN PHE LEU LYS GLN TYR VAL LYS LYS THR GLY ALA LYS          
SEQRES   4 A  271  GLY PHE VAL LEU GLY ILE SER GLY GLY GLN ASP SER THR          
SEQRES   5 A  271  LEU ALA GLY ARG LEU ALA GLN LEU ALA VAL GLU SER ILE          
SEQRES   6 A  271  ARG GLU GLU GLY GLY ASP ALA GLN PHE ILE ALA VAL ARG          
SEQRES   7 A  271  LEU PRO HIS GLY THR GLN GLN ASP GLU ASP ASP ALA GLN          
SEQRES   8 A  271  LEU ALA LEU LYS PHE ILE LYS PRO ASP LYS SER TRP LYS          
SEQRES   9 A  271  PHE ASP ILE LYS SER THR VAL SER ALA PHE SER ASP GLN          
SEQRES  10 A  271  TYR GLN GLN GLU THR GLY ASP GLN LEU THR ASP PHE ASN          
SEQRES  11 A  271  LYS GLY ASN VAL LYS ALA ARG THR ARG MET ILE ALA GLN          
SEQRES  12 A  271  TYR ALA ILE GLY GLY GLN GLU GLY LEU LEU VAL LEU GLY          
SEQRES  13 A  271  THR ASP HIS ALA ALA GLU ALA VAL THR GLY PHE PHE THR          
SEQRES  14 A  271  LYS TYR GLY ASP GLY GLY ALA ASP LEU LEU PRO LEU THR          
SEQRES  15 A  271  GLY LEU THR LYS ARG GLN GLY ARG THR LEU LEU LYS GLU          
SEQRES  16 A  271  LEU GLY ALA PRO GLU ARG LEU TYR LEU LYS GLU PRO THR          
SEQRES  17 A  271  ALA ASP LEU LEU ASP GLU LYS PRO GLN GLN SER ASP GLU          
SEQRES  18 A  271  THR GLU LEU GLY ILE SER TYR ASP GLU ILE ASP ASP TYR          
SEQRES  19 A  271  LEU GLU GLY LYS GLU VAL SER ALA LYS VAL SER GLU ALA          
SEQRES  20 A  271  LEU GLU LYS ARG TYR SER MET THR GLU HIS LYS ARG GLN          
SEQRES  21 A  271  VAL PRO ALA SER MET PHE ASP ASP TRP TRP LYS                  
SEQRES   1 B  271  SER MET GLN GLU LYS ILE MET ARG GLU LEU HIS VAL LYS          
SEQRES   2 B  271  PRO SER ILE ASP PRO LYS GLN GLU ILE GLU ASP ARG VAL          
SEQRES   3 B  271  ASN PHE LEU LYS GLN TYR VAL LYS LYS THR GLY ALA LYS          
SEQRES   4 B  271  GLY PHE VAL LEU GLY ILE SER GLY GLY GLN ASP SER THR          
SEQRES   5 B  271  LEU ALA GLY ARG LEU ALA GLN LEU ALA VAL GLU SER ILE          
SEQRES   6 B  271  ARG GLU GLU GLY GLY ASP ALA GLN PHE ILE ALA VAL ARG          
SEQRES   7 B  271  LEU PRO HIS GLY THR GLN GLN ASP GLU ASP ASP ALA GLN          
SEQRES   8 B  271  LEU ALA LEU LYS PHE ILE LYS PRO ASP LYS SER TRP LYS          
SEQRES   9 B  271  PHE ASP ILE LYS SER THR VAL SER ALA PHE SER ASP GLN          
SEQRES  10 B  271  TYR GLN GLN GLU THR GLY ASP GLN LEU THR ASP PHE ASN          
SEQRES  11 B  271  LYS GLY ASN VAL LYS ALA ARG THR ARG MET ILE ALA GLN          
SEQRES  12 B  271  TYR ALA ILE GLY GLY GLN GLU GLY LEU LEU VAL LEU GLY          
SEQRES  13 B  271  THR ASP HIS ALA ALA GLU ALA VAL THR GLY PHE PHE THR          
SEQRES  14 B  271  LYS TYR GLY ASP GLY GLY ALA ASP LEU LEU PRO LEU THR          
SEQRES  15 B  271  GLY LEU THR LYS ARG GLN GLY ARG THR LEU LEU LYS GLU          
SEQRES  16 B  271  LEU GLY ALA PRO GLU ARG LEU TYR LEU LYS GLU PRO THR          
SEQRES  17 B  271  ALA ASP LEU LEU ASP GLU LYS PRO GLN GLN SER ASP GLU          
SEQRES  18 B  271  THR GLU LEU GLY ILE SER TYR ASP GLU ILE ASP ASP TYR          
SEQRES  19 B  271  LEU GLU GLY LYS GLU VAL SER ALA LYS VAL SER GLU ALA          
SEQRES  20 B  271  LEU GLU LYS ARG TYR SER MET THR GLU HIS LYS ARG GLN          
SEQRES  21 B  271  VAL PRO ALA SER MET PHE ASP ASP TRP TRP LYS                  
HET     MG  A5500       1                                                       
HET    DND  A4000      44                                                       
HET    ATP  A5000      31                                                       
HET    DND  B3000      44                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DND NICOTINIC ACID ADENINE DINUCLEOTIDE                              
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     DND DEAMIDO-NAD+                                                     
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  DND    2(C21 H27 N6 O15 P2 1+)                                      
FORMUL   5  ATP    C10 H16 N5 O13 P3                                            
FORMUL   7  HOH   *397(H2 O)                                                    
HELIX    1   1 MET A    2  LEU A   10  1                                   9    
HELIX    2   2 PRO A   18  THR A   36  1                                  19    
HELIX    3   3 GLN A   49  GLU A   68  1                                  20    
HELIX    4   4 GLU A   87  ILE A   97  1                                  11    
HELIX    5   5 LYS A  108  THR A  122  1                                  15    
HELIX    6   6 ASP A  128  GLU A  150  1                                  23    
HELIX    7   7 ALA A  160  ALA A  163  1                                   4    
HELIX    8   8 LYS A  186  LEU A  196  1                                  11    
HELIX    9   9 GLU A  200  LEU A  204  1                                   5    
HELIX   10  10 ASP A  220  LEU A  224  1                                   5    
HELIX   11  11 TYR A  228  LEU A  235  1                                   8    
HELIX   12  12 ALA A  242  ARG A  259  1                                  18    
HELIX   13  13 MET B    2  GLU B    9  1                                   8    
HELIX   14  14 PRO B   18  THR B   36  1                                  19    
HELIX   15  15 GLN B   49  GLU B   67  1                                  19    
HELIX   16  16 GLU B   87  ILE B   97  1                                  11    
HELIX   17  17 LYS B  108  THR B  122  1                                  15    
HELIX   18  18 ASP B  128  GLU B  150  1                                  23    
HELIX   19  19 ALA B  160  ALA B  163  1                                   4    
HELIX   20  20 LYS B  186  GLU B  195  1                                  10    
HELIX   21  21 GLU B  200  TYR B  203  1                                   4    
HELIX   22  23 TYR B  228  LEU B  235  1                                   8    
HELIX   23  24 ALA B  242  ARG B  259  1                                  18    
SHEET    1   A 3 GLY A  40  GLY A  44  0                                        
SHEET    2   A 3 GLN A  73  ARG A  78  1  N  GLN A  73   O  PHE A  41           
SHEET    3   A 3 LYS A 101  LYS A 104  1  N  LYS A 101   O  ALA A  76           
SHEET    1   B 3 GLY B  40  GLY B  44  0                                        
SHEET    2   B 3 GLN B  73  ARG B  78  1  N  GLN B  73   O  PHE B  41           
SHEET    3   B 3 LYS B 101  LYS B 104  1  N  LYS B 101   O  ALA B  76           
LINK         O   THR A 208                MG    MG A5500     1555   1555  1.92  
LINK         O   HOH A2381                MG    MG A5500     1555   1555  1.72  
LINK         O   HOH A2382                MG    MG A5500     1555   1555  1.63  
LINK         O2B ATP A5000                MG    MG A5500     1555   1555  2.28  
LINK         O3G ATP A5000                MG    MG A5500     1555   1555  2.78  
LINK         O1A ATP A5000                MG    MG A5500     1555   1555  2.33  
SITE     1 AC1  4 THR A 208  HOH A2381  HOH A2382  ATP A5000                    
SITE     1 AC2 27 PHE A 129  ASN A 133  ARG A 137  PHE A 167                    
SITE     2 AC2 27 PHE A 168  THR A 169  LYS A 170  ASP A 173                    
SITE     3 AC2 27 ALA A 209  LEU A 211  GLU A 223  HIS A 257                    
SITE     4 AC2 27 LYS A 258  HOH A2101  HOH A2158  HOH A2206                    
SITE     5 AC2 27 HOH A2213  HOH A2223  HOH A2238  HOH A2284                    
SITE     6 AC2 27 ATP A5000  TYR B  32  THR B  36  TYR B 144                    
SITE     7 AC2 27 LEU B 153  ASP B 177  HOH B2071                               
SITE     1 AC3 22 TYR A  32  THR A  36  TYR A 144  LEU A 153                    
SITE     2 AC3 22 ASP A 177  HOH A2027  PHE B 129  ASN B 133                    
SITE     3 AC3 22 ARG B 137  PHE B 167  PHE B 168  THR B 169                    
SITE     4 AC3 22 LYS B 170  ASP B 173  HIS B 257  LYS B 258                    
SITE     5 AC3 22 HOH B2127  HOH B2228  HOH B2270  HOH B2304                    
SITE     6 AC3 22 HOH B2372  HOH B2377                                          
SITE     1 AC4 28 LEU A  43  GLY A  44  ILE A  45  SER A  46                    
SITE     2 AC4 28 GLY A  48  ASP A  50  SER A  51  ARG A  78                    
SITE     3 AC4 28 LEU A  79  GLN A  84  ARG A 139  THR A 157                    
SITE     4 AC4 28 ASP A 173  LYS A 186  PRO A 207  THR A 208                    
SITE     5 AC4 28 HOH A2012  HOH A2019  HOH A2023  HOH A2062                    
SITE     6 AC4 28 HOH A2080  HOH A2238  HOH A2284  HOH A2326                    
SITE     7 AC4 28 HOH A2381  HOH A2382  DND A4000   MG A5500                    
CRYST1   52.980   86.690   60.480  90.00 111.18  90.00 P 1 21 1      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      0.018875  0.000000  0.007313        0.00000                         
SCALE2      0.000000  0.011535  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017732        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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