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Database: PDB
Entry: 1T4B
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Original site: 1T4B 
HEADER    OXIDOREDUCTASE                          29-APR-04   1T4B              
TITLE     1.6 ANGSTROM STRUCTURE OF ESHERICHIA COLI ASPARTATE-                  
TITLE    2 SEMIALDEHYDE DEHYDROGENASE.                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE-SEMIALDEHYDE DEHYDROGENASE;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ASA DEHYDROGENASE, ASADH;                                   
COMPND   5 EC: 1.2.1.11;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: ASD, HOM, B3433, Z4797, ECS4278, SF3456, S4307;                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMUT20                                    
KEYWDS    ASADH, ASPARTATE SEMIALDEHYDE DEHYDROGENASE, HOSR, LYSINE             
KEYWDS   2 BIOSYNTHESIS, NADP+ OXIDOREDUCTASE (PHOSPHORYLATING),                
KEYWDS   3 DOMAIN MOVEMENT                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.E.NICHOLS,B.DHALIWAL,M.LOCKYER,A.R.HAWKINS,D.K.STAMMERS             
REVDAT   3   24-FEB-09 1T4B    1       VERSN                                    
REVDAT   2   17-AUG-04 1T4B    1       JRNL                                     
REVDAT   1   13-JUL-04 1T4B    0                                                
JRNL        AUTH   C.E.NICHOLS,B.DHALIWAL,M.LOCKYER,A.R.HAWKINS,                
JRNL        AUTH 2 D.K.STAMMERS                                                 
JRNL        TITL   HIGH-RESOLUTION STRUCTURES REVEAL DETAILS OF                 
JRNL        TITL 2 DOMAIN CLOSURE AND "HALF-OF-SITES-REACTIVITY" IN             
JRNL        TITL 3 ESCHERICHIA COLI ASPARTATE BETA-SEMIALDEHYDE                 
JRNL        TITL 4 DEHYDROGENASE.                                               
JRNL        REF    J.MOL.BIOL.                   V. 341   797 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15288787                                                     
JRNL        DOI    10.1016/J.JMB.2004.05.073                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2450802.610                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 86606                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8689                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2841                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 323                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5620                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 967                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.15000                                             
REMARK   3    B22 (A**2) : -0.57000                                             
REMARK   3    B33 (A**2) : 3.72000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 61.74                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T4B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022294.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86606                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.250                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : 2.920                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1T4D                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, KCL, TRIS.HCL, PH 7.5,         
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       28.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.45000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.45000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.05000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 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    LEU A 111       68.29   -165.81                                   
REMARK 500    PRO A 228       42.19    -75.40                                   
REMARK 500    TRP A 229      119.16   -160.50                                   
REMARK 500    ASP A 231      177.59     76.22                                   
REMARK 500    LEU A 316       57.82   -100.86                                   
REMARK 500    LEU A 352      -94.37    -92.29                                   
REMARK 500    ALA A 355      -76.33   -153.58                                   
REMARK 500    SER B  38        6.10   -155.01                                   
REMARK 500    LEU B 111       68.77   -162.44                                   
REMARK 500    PRO B 228       44.78    -78.28                                   
REMARK 500    TRP B 229      118.99   -162.04                                   
REMARK 500    ASP B 231      179.41     75.06                                   
REMARK 500    LEU B 316       58.16   -101.75                                   
REMARK 500    LEU B 352      -94.80    -91.58                                   
REMARK 500    ALA B 355      -73.24   -156.33                                   
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 B5268        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A5277        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A5352        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B5350        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH A5368        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH A5371        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B5379        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH A5389        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH B5394        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH A5402        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH A5403        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH A5405        DISTANCE =  8.38 ANGSTROMS                       
REMARK 525    HOH A5419        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH A5427        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH B5426        DISTANCE =  7.28 ANGSTROMS                       
REMARK 525    HOH A5432        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B5431        DISTANCE =  9.02 ANGSTROMS                       
REMARK 525    HOH B5434        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH B5438        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH A5442        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A5443        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH B5440        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH B5442        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH B5443        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A5449        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A5450        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A5451        DISTANCE = 12.16 ANGSTROMS                       
REMARK 525    HOH B5452        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A5476        DISTANCE =  5.04 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                              NA A5004  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A5011   O                                                      
REMARK 620 2 HOH A5474   O    84.2                                              
REMARK 620 3 HOH A5473   O    88.7  89.6                                        
REMARK 620 4 HOH A5472   O   168.7  90.8  81.1                                  
REMARK 620 5 HOH B5456   O    98.5  78.8 165.6  90.5                            
REMARK 620 6 HOH A5290   O    87.6 171.5  92.3  97.6 100.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B5001  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B5451   O                                                      
REMARK 620 2 HOH B5450   O    84.6                                              
REMARK 620 3 HOH B5452   O   101.6  93.5                                        
REMARK 620 4 HOH A5469   O    94.2 170.0  96.5                                  
REMARK 620 5 HOH B5130   O   156.4  83.5  99.4  94.1                            
REMARK 620 6 HOH B5045   O    81.1  87.0 177.3  83.0  78.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B5002  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B5228   O                                                      
REMARK 620 2 HOH B5457   O   112.7                                              
REMARK 620 3 HOH B5391   O    71.5  66.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A5005  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A5135   O                                                      
REMARK 620 2 HOH A5138   O    99.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 5001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 5002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 5003                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 5004                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 5005                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T4D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI ASPARTATE-BETA-                
REMARK 900 SEMIALDEHYDE DEHYDROGENASE (ECDHQS), AT 1.95D.                       
DBREF  1T4B A    1   367  UNP    P0A9Q9   DHAS_ECOLI       1    367             
DBREF  1T4B B    1   367  UNP    P0A9Q9   DHAS_ECOLI       1    367             
SEQADV 1T4B GLN A    2  UNP  P0A9Q9    LYS     2 ENGINEERED                     
SEQADV 1T4B GLN B    2  UNP  P0A9Q9    LYS     2 ENGINEERED                     
SEQRES   1 A  367  MET GLN ASN VAL GLY PHE ILE GLY TRP ARG GLY MET VAL          
SEQRES   2 A  367  GLY SER VAL LEU MET GLN ARG MET VAL GLU GLU ARG ASP          
SEQRES   3 A  367  PHE ASP ALA ILE ARG PRO VAL PHE PHE SER THR SER GLN          
SEQRES   4 A  367  LEU GLY GLN ALA ALA PRO SER PHE GLY GLY THR THR GLY          
SEQRES   5 A  367  THR LEU GLN ASP ALA PHE ASP LEU GLU ALA LEU LYS ALA          
SEQRES   6 A  367  LEU ASP ILE ILE VAL THR CYS GLN GLY GLY ASP TYR THR          
SEQRES   7 A  367  ASN GLU ILE TYR PRO LYS LEU ARG GLU SER GLY TRP GLN          
SEQRES   8 A  367  GLY TYR TRP ILE ASP ALA ALA SER SER LEU ARG MET LYS          
SEQRES   9 A  367  ASP ASP ALA ILE ILE ILE LEU ASP PRO VAL ASN GLN ASP          
SEQRES  10 A  367  VAL ILE THR ASP GLY LEU ASN ASN GLY ILE ARG THR PHE          
SEQRES  11 A  367  VAL GLY GLY ASN CYS THR VAL SER LEU MET LEU MET SER          
SEQRES  12 A  367  LEU GLY GLY LEU PHE ALA ASN ASP LEU VAL ASP TRP VAL          
SEQRES  13 A  367  SER VAL ALA THR TYR GLN ALA ALA SER GLY GLY GLY ALA          
SEQRES  14 A  367  ARG HIS MET ARG GLU LEU LEU THR GLN MET GLY HIS LEU          
SEQRES  15 A  367  TYR GLY HIS VAL ALA ASP GLU LEU ALA THR PRO SER SER          
SEQRES  16 A  367  ALA ILE LEU ASP ILE GLU ARG LYS VAL THR THR LEU THR          
SEQRES  17 A  367  ARG SER GLY GLU LEU PRO VAL ASP ASN PHE GLY VAL PRO          
SEQRES  18 A  367  LEU ALA GLY SER LEU ILE PRO TRP ILE ASP LYS GLN LEU          
SEQRES  19 A  367  ASP ASN GLY GLN SER ARG GLU GLU TRP LYS GLY GLN ALA          
SEQRES  20 A  367  GLU THR ASN LYS ILE LEU ASN THR SER SER VAL ILE PRO          
SEQRES  21 A  367  VAL ASP GLY LEU CYS VAL ARG VAL GLY ALA LEU ARG CYS          
SEQRES  22 A  367  HIS SER GLN ALA PHE THR ILE LYS LEU LYS LYS ASP VAL          
SEQRES  23 A  367  SER ILE PRO THR VAL GLU GLU LEU LEU ALA ALA HIS ASN          
SEQRES  24 A  367  PRO TRP ALA LYS VAL VAL PRO ASN ASP ARG GLU ILE THR          
SEQRES  25 A  367  MET ARG GLU LEU THR PRO ALA ALA VAL THR GLY THR LEU          
SEQRES  26 A  367  THR THR PRO VAL GLY ARG LEU ARG LYS LEU ASN MET GLY          
SEQRES  27 A  367  PRO GLU PHE LEU SER ALA PHE THR VAL GLY ASP GLN LEU          
SEQRES  28 A  367  LEU TRP GLY ALA ALA GLU PRO LEU ARG ARG MET LEU ARG          
SEQRES  29 A  367  GLN LEU ALA                                                  
SEQRES   1 B  367  MET GLN ASN VAL GLY PHE ILE GLY TRP ARG GLY MET VAL          
SEQRES   2 B  367  GLY SER VAL LEU MET GLN ARG MET VAL GLU GLU ARG ASP          
SEQRES   3 B  367  PHE ASP ALA ILE ARG PRO VAL PHE PHE SER THR SER GLN          
SEQRES   4 B  367  LEU GLY GLN ALA ALA PRO SER PHE GLY GLY THR THR GLY          
SEQRES   5 B  367  THR LEU GLN ASP ALA PHE ASP LEU GLU ALA LEU LYS ALA          
SEQRES   6 B  367  LEU ASP ILE ILE VAL THR CYS GLN GLY GLY ASP TYR THR          
SEQRES   7 B  367  ASN GLU ILE TYR PRO LYS LEU ARG GLU SER GLY TRP GLN          
SEQRES   8 B  367  GLY TYR TRP ILE ASP ALA ALA SER SER LEU ARG MET LYS          
SEQRES   9 B  367  ASP ASP ALA ILE ILE ILE LEU ASP PRO VAL ASN GLN ASP          
SEQRES  10 B  367  VAL ILE THR ASP GLY LEU ASN ASN GLY ILE ARG THR PHE          
SEQRES  11 B  367  VAL GLY GLY ASN CYS THR VAL SER LEU MET LEU MET SER          
SEQRES  12 B  367  LEU GLY GLY LEU PHE ALA ASN ASP LEU VAL ASP TRP VAL          
SEQRES  13 B  367  SER VAL ALA THR TYR GLN ALA ALA SER GLY GLY GLY ALA          
SEQRES  14 B  367  ARG HIS MET ARG GLU LEU LEU THR GLN MET GLY HIS LEU          
SEQRES  15 B  367  TYR GLY HIS VAL ALA ASP GLU LEU ALA THR PRO SER SER          
SEQRES  16 B  367  ALA ILE LEU ASP ILE GLU ARG LYS VAL THR THR LEU THR          
SEQRES  17 B  367  ARG SER GLY GLU LEU PRO VAL ASP ASN PHE GLY VAL PRO          
SEQRES  18 B  367  LEU ALA GLY SER LEU ILE PRO TRP ILE ASP LYS GLN LEU          
SEQRES  19 B  367  ASP ASN GLY GLN SER ARG GLU GLU TRP LYS GLY GLN ALA          
SEQRES  20 B  367  GLU THR ASN LYS ILE LEU ASN THR SER SER VAL ILE PRO          
SEQRES  21 B  367  VAL ASP GLY LEU CYS VAL ARG VAL GLY ALA LEU ARG CYS          
SEQRES  22 B  367  HIS SER GLN ALA PHE THR ILE LYS LEU LYS LYS ASP VAL          
SEQRES  23 B  367  SER ILE PRO THR VAL GLU GLU LEU LEU ALA ALA HIS ASN          
SEQRES  24 B  367  PRO TRP ALA LYS VAL VAL PRO ASN ASP ARG GLU ILE THR          
SEQRES  25 B  367  MET ARG GLU LEU THR PRO ALA ALA VAL THR GLY THR LEU          
SEQRES  26 B  367  THR THR PRO VAL GLY ARG LEU ARG LYS LEU ASN MET GLY          
SEQRES  27 B  367  PRO GLU PHE LEU SER ALA PHE THR VAL GLY ASP GLN LEU          
SEQRES  28 B  367  LEU TRP GLY ALA ALA GLU PRO LEU ARG ARG MET LEU ARG          
SEQRES  29 B  367  GLN LEU ALA                                                  
HET     NA  B5001       1                                                       
HET     NA  B5002       1                                                       
HET     NA  A5003       1                                                       
HET     NA  A5004       1                                                       
HET     NA  A5005       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    5(NA 1+)                                                     
FORMUL   8  HOH   *967(H2 O)                                                    
HELIX    1   1 GLY A   11  GLU A   24  1                                  14    
HELIX    2   2 ARG A   25  ILE A   30  5                                   6    
HELIX    3   3 PRO A   45  GLY A   49  5                                   5    
HELIX    4   4 ASP A   59  ALA A   65  1                                   7    
HELIX    5   5 GLY A   74  SER A   88  1                                  15    
HELIX    6   6 LEU A  111  ASN A  125  1                                  15    
HELIX    7   7 ASN A  134  ASN A  150  1                                  17    
HELIX    8   8 ALA A  163  GLY A  167  5                                   5    
HELIX    9   9 GLY A  168  VAL A  186  1                                  19    
HELIX   10  10 VAL A  186  ALA A  191  1                                   6    
HELIX   11  11 ALA A  196  GLY A  211  1                                  16    
HELIX   12  12 SER A  239  ASN A  254  1                                  16    
HELIX   13  13 SER A  287  ASN A  299  1                                  13    
HELIX   14  14 ASP A  308  LEU A  316  1                                   9    
HELIX   15  15 THR A  317  THR A  322  1                                   6    
HELIX   16  16 ALA A  356  ALA A  367  1                                  12    
HELIX   17  17 GLY B   11  GLU B   24  1                                  14    
HELIX   18  18 SER B   46  THR B   50  5                                   5    
HELIX   19  19 ASP B   59  ALA B   65  1                                   7    
HELIX   20  20 GLY B   74  SER B   88  1                                  15    
HELIX   21  21 LEU B  111  ASN B  125  1                                  15    
HELIX   22  22 ASN B  134  ASN B  150  1                                  17    
HELIX   23  23 ALA B  163  GLY B  167  5                                   5    
HELIX   24  24 GLY B  168  ALA B  191  1                                  24    
HELIX   25  25 ALA B  196  GLY B  211  1                                  16    
HELIX   26  26 SER B  239  ASN B  254  1                                  16    
HELIX   27  27 SER B  287  ASN B  299  1                                  13    
HELIX   28  28 ASP B  308  LEU B  316  1                                   9    
HELIX   29  29 THR B  317  THR B  322  1                                   6    
HELIX   30  30 ALA B  355  ALA B  367  1                                  13    
SHEET    1   A 7 GLN A  55  ASP A  56  0                                        
SHEET    2   A 7 ARG A  31  SER A  36  1  N  PHE A  34   O  GLN A  55           
SHEET    3   A 7 ASN A   3  ILE A   7  1  N  VAL A   4   O  VAL A  33           
SHEET    4   A 7 ILE A  68  THR A  71  1  O  VAL A  70   N  GLY A   5           
SHEET    5   A 7 TYR A  93  ASP A  96  1  O  ILE A  95   N  ILE A  69           
SHEET    6   A 7 THR A 129  GLY A 132  1  O  PHE A 130   N  TRP A  94           
SHEET    7   A 7 ALA A 107  ILE A 110  1  N  ILE A 108   O  VAL A 131           
SHEET    1   B 5 VAL A 261  LEU A 264  0                                        
SHEET    2   B 5 VAL A 153  TYR A 161  1  N  THR A 160   O  LEU A 264           
SHEET    3   B 5 CYS A 273  LEU A 282 -1  O  LYS A 281   N  ASP A 154           
SHEET    4   B 5 PHE A 341  ASP A 349 -1  O  LEU A 342   N  ILE A 280           
SHEET    5   B 5 VAL A 329  LYS A 334 -1  N  ARG A 333   O  SER A 343           
SHEET    1   C 2 LEU A 226  ILE A 227  0                                        
SHEET    2   C 2 ARG A 267  VAL A 268 -1  O  ARG A 267   N  ILE A 227           
SHEET    1   D 7 GLN B  55  ASP B  56  0                                        
SHEET    2   D 7 ARG B  31  SER B  36  1  N  PHE B  34   O  GLN B  55           
SHEET    3   D 7 ASN B   3  ILE B   7  1  N  PHE B   6   O  VAL B  33           
SHEET    4   D 7 ILE B  68  THR B  71  1  O  VAL B  70   N  GLY B   5           
SHEET    5   D 7 TYR B  93  ASP B  96  1  O  ILE B  95   N  ILE B  69           
SHEET    6   D 7 THR B 129  GLY B 132  1  O  PHE B 130   N  TRP B  94           
SHEET    7   D 7 ALA B 107  ILE B 110  1  N  ILE B 108   O  VAL B 131           
SHEET    1   E 5 VAL B 261  LEU B 264  0                                        
SHEET    2   E 5 VAL B 153  TYR B 161  1  N  THR B 160   O  LEU B 264           
SHEET    3   E 5 CYS B 273  LEU B 282 -1  O  LYS B 281   N  ASP B 154           
SHEET    4   E 5 GLY B 338  ASP B 349 -1  O  GLU B 340   N  LEU B 282           
SHEET    5   E 5 VAL B 329  LEU B 335 -1  N  ARG B 333   O  SER B 343           
SHEET    1   F 2 LEU B 226  ILE B 227  0                                        
SHEET    2   F 2 ARG B 267  VAL B 268 -1  O  ARG B 267   N  ILE B 227           
LINK        NA    NA A5004                 O   HOH A5011     1555   1555  2.57  
LINK        NA    NA A5004                 O   HOH A5474     1555   1555  2.54  
LINK        NA    NA B5001                 O   HOH B5451     1555   1555  2.72  
LINK        NA    NA B5001                 O   HOH B5450     1555   1555  2.79  
LINK        NA    NA B5001                 O   HOH B5452     1555   1555  2.85  
LINK        NA    NA B5001                 O   HOH A5469     1555   1555  2.84  
LINK        NA    NA B5001                 O   HOH B5130     1555   1555  2.73  
LINK        NA    NA B5001                 O   HOH B5045     1555   1555  2.69  
LINK        NA    NA B5002                 O   HOH B5228     1555   1555  2.96  
LINK        NA    NA B5002                 O   HOH B5457     1555   1555  2.95  
LINK        NA    NA B5002                 O   HOH B5391     1555   1555  2.89  
LINK        NA    NA A5003                 O   HOH A5131     1555   1555  2.77  
LINK        NA    NA A5004                 O   HOH A5473     1555   1555  2.65  
LINK        NA    NA A5004                 O   HOH A5472     1555   1555  2.65  
LINK        NA    NA A5004                 O   HOH B5456     1555   1555  2.86  
LINK        NA    NA A5004                 O   HOH A5290     1555   1555  2.82  
LINK        NA    NA A5005                 O   HOH A5135     1555   1555  2.80  
LINK        NA    NA A5005                 O   HOH A5138     1555   1555  2.77  
SITE     1 AC1  6 HOH A5469  HOH B5045  HOH B5130  HOH B5450                    
SITE     2 AC1  6 HOH B5451  HOH B5452                                          
SITE     1 AC2  5 ASP B 105  HOH B5228  HOH B5281  HOH B5391                    
SITE     2 AC2  5 HOH B5457                                                     
SITE     1 AC3  4 HOH A5131  HOH B5148  HOH B5163  HOH B5186                    
SITE     1 AC4  6 HOH A5011  HOH A5290  HOH A5472  HOH A5473                    
SITE     2 AC4  6 HOH A5474  HOH B5456                                          
SITE     1 AC5  8 ASP A  76  GLY A 184  HIS A 185  ASP A 188                    
SITE     2 AC5  8 HOH A5135  HOH A5138  HOH A5325  HOH A5412                    
CRYST1   56.500   70.100  180.900  90.00  90.00  90.00 P 21 21 21    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      0.017699  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005529        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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