GenomeNet

Database: PDB
Entry: 3DOJ
LinkDB: 3DOJ
Original site: 3DOJ 
HEADER    OXIDOREDUCTASE                          04-JUL-08   3DOJ              
TITLE     STRUCTURE OF GLYOXYLATE REDUCTASE 1 FROM ARABIDOPSIS (ATGLYR1)        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEHYDROGENASE-LIKE PROTEIN;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AT3G25530;                                                  
COMPND   5 EC: 1.1.1.79;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: AT3G25530;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    GAMMA-HYDROXYBUTYRATE DEHYDROGENASE, 4-HYDROXYBUTYRATE DEHYDROGENASE, 
KEYWDS   2 SUCCINIC SEMIALDEHYDE REDUCTASE, OXIDOREDUCTASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.JORGENSEN                                                           
REVDAT   2   25-OCT-17 3DOJ    1       REMARK                                   
REVDAT   1   07-JUL-09 3DOJ    0                                                
JRNL        AUTH   G.HOOVER,R.JORGENSEN,A.R.MERRILL,B.J.SHELP                   
JRNL        TITL   CYTOSOLIC NADPH-DEPENDENT GLYOXYLATE REDUCTASE FROM          
JRNL        TITL 2 ARABIDOPSIS: CRYSTAL STRUCTURE AND KINETIC CHARACTERIZATION  
JRNL        TITL 3 OF ACTIVE SITE MUTANTS                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27478                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 863                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  2.2330 -  2.1010    0.01      473   139  0.1940 0.2440        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 73.45                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.15700                                              
REMARK   3    B22 (A**2) : 4.15700                                              
REMARK   3    B33 (A**2) : -8.31500                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           NULL                                  
REMARK   3   ANGLE     :  0.817           NULL                                  
REMARK   3   CHIRALITY :  0.051           NULL                                  
REMARK   3   PLANARITY :  0.003           NULL                                  
REMARK   3   DIHEDRAL  : 15.958           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DOJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048293.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : WHITE BEAM SLITS, CRYO-COOLED      
REMARK 200                                   FIRST AND SAGITTALLY BENT SECOND   
REMARK 200                                   CRYSTAL OF DOUBLE CRYSTAL          
REMARK 200                                   MONOCHROMATOR (DCM), VERTICALLY    
REMARK 200                                   FOCUSING MIRROR (VFM)              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27496                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2UYY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE HYDRATE, 20%       
REMARK 280  PEG3350, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       78.27150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       78.27150            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.73350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       18.86675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       78.27150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.60025            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.60025            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       78.27150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       18.86675            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       78.27150            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       37.73350            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       78.27150            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       37.73350            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       78.27150            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       56.60025            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       18.86675            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       78.27150            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       18.86675            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       56.60025            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       78.27150            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       78.27150            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       37.73350            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.0 KCAL/MOL                       
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 350   BIOMT1   2  0.000000 -1.000000  0.000000      156.54300            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      156.54300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      313.08600            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000      156.54300            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000     -156.54300            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 SD   MET A   1  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 346  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 378  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLU A   289                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A 286    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 288    CG   CD   NE   CZ   NH1  NH2                        
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    SER A 123     -152.06    -96.11                                   
REMARK 500    LEU A 135       78.63   -108.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 290                  
DBREF  3DOJ A    1   289  UNP    Q9LSV0   Q9LSV0_ARATH     1    289             
SEQADV 3DOJ MET A  -20  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ GLY A  -19  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ SER A  -18  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ SER A  -17  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -16  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -15  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -14  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -13  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -12  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A  -11  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ SER A  -10  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ SER A   -9  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ GLY A   -8  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ LEU A   -7  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ VAL A   -6  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ PRO A   -5  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ ARG A   -4  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ GLY A   -3  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ SER A   -2  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ HIS A   -1  UNP  Q9LSV0              EXPRESSION TAG                 
SEQADV 3DOJ MET A    0  UNP  Q9LSV0              EXPRESSION TAG                 
SEQRES   1 A  310  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  310  LEU VAL PRO ARG GLY SER HIS MET MET GLU VAL GLY PHE          
SEQRES   3 A  310  LEU GLY LEU GLY ILE MET GLY LYS ALA MET SER MET ASN          
SEQRES   4 A  310  LEU LEU LYS ASN GLY PHE LYS VAL THR VAL TRP ASN ARG          
SEQRES   5 A  310  THR LEU SER LYS CYS ASP GLU LEU VAL GLU HIS GLY ALA          
SEQRES   6 A  310  SER VAL CYS GLU SER PRO ALA GLU VAL ILE LYS LYS CYS          
SEQRES   7 A  310  LYS TYR THR ILE ALA MET LEU SER ASP PRO CYS ALA ALA          
SEQRES   8 A  310  LEU SER VAL VAL PHE ASP LYS GLY GLY VAL LEU GLU GLN          
SEQRES   9 A  310  ILE CYS GLU GLY LYS GLY TYR ILE ASP MET SER THR VAL          
SEQRES  10 A  310  ASP ALA GLU THR SER LEU LYS ILE ASN GLU ALA ILE THR          
SEQRES  11 A  310  GLY LYS GLY GLY ARG PHE VAL GLU GLY PRO VAL SER GLY          
SEQRES  12 A  310  SER LYS LYS PRO ALA GLU ASP GLY GLN LEU ILE ILE LEU          
SEQRES  13 A  310  ALA ALA GLY ASP LYS ALA LEU PHE GLU GLU SER ILE PRO          
SEQRES  14 A  310  ALA PHE ASP VAL LEU GLY LYS ARG SER PHE TYR LEU GLY          
SEQRES  15 A  310  GLN VAL GLY ASN GLY ALA LYS MET LYS LEU ILE VAL ASN          
SEQRES  16 A  310  MET ILE MET GLY SER MET MET ASN ALA PHE SER GLU GLY          
SEQRES  17 A  310  LEU VAL LEU ALA ASP LYS SER GLY LEU SER SER ASP THR          
SEQRES  18 A  310  LEU LEU ASP ILE LEU ASP LEU GLY ALA MET THR ASN PRO          
SEQRES  19 A  310  MET PHE LYS GLY LYS GLY PRO SER MET ASN LYS SER SER          
SEQRES  20 A  310  TYR PRO PRO ALA PHE PRO LEU LYS HIS GLN GLN LYS ASP          
SEQRES  21 A  310  MET ARG LEU ALA LEU ALA LEU GLY ASP GLU ASN ALA VAL          
SEQRES  22 A  310  SER MET PRO VAL ALA ALA ALA ALA ASN GLU ALA PHE LYS          
SEQRES  23 A  310  LYS ALA ARG SER LEU GLY LEU GLY ASP LEU ASP PHE SER          
SEQRES  24 A  310  ALA VAL ILE GLU ALA VAL LYS PHE SER ARG GLU                  
HET     CL  A 290       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   CL    CL 1-                                                        
FORMUL   3  HOH   *103(H2 O)                                                    
HELIX    1   1 GLY A    9  ASN A   22  1                                  14    
HELIX    2   2 THR A   32  LYS A   35  5                                   4    
HELIX    3   3 CYS A   36  HIS A   42  1                                   7    
HELIX    4   4 SER A   49  CYS A   57  1                                   9    
HELIX    5   5 ASP A   66  ASP A   76  1                                  11    
HELIX    6   6 GLY A   79  ILE A   84  5                                   6    
HELIX    7   7 ASP A   97  LYS A  111  1                                  15    
HELIX    8   8 SER A  123  GLY A  130  1                                   8    
HELIX    9   9 ASP A  139  LEU A  153  1                                  15    
HELIX   10  10 GLY A  164  SER A  194  1                                  31    
HELIX   11  11 SER A  197  GLY A  208  1                                  12    
HELIX   12  12 ASN A  212  LYS A  224  1                                  13    
HELIX   13  13 PRO A  232  ASN A  250  1                                  19    
HELIX   14  14 MET A  254  LEU A  270  1                                  17    
HELIX   15  15 ASP A  276  ALA A  279  5                                   4    
HELIX   16  16 VAL A  280  PHE A  286  1                                   7    
SHEET    1   A 8 SER A  45  VAL A  46  0                                        
SHEET    2   A 8 LYS A  25  TRP A  29  1  N  VAL A  28   O  SER A  45           
SHEET    3   A 8 GLU A   2  LEU A   6  1  N  PHE A   5   O  THR A  27           
SHEET    4   A 8 TYR A  59  ALA A  62  1  O  ILE A  61   N  GLY A   4           
SHEET    5   A 8 GLY A  89  ASP A  92  1  O  ILE A  91   N  THR A  60           
SHEET    6   A 8 ARG A 114  GLU A 117  1  O  ARG A 114   N  TYR A  90           
SHEET    7   A 8 LEU A 132  GLY A 138 -1  O  ALA A 137   N  GLU A 117           
SHEET    8   A 8 VAL A 120  SER A 121 -1  N  SER A 121   O  ILE A 133           
SHEET    1   B 8 SER A  45  VAL A  46  0                                        
SHEET    2   B 8 LYS A  25  TRP A  29  1  N  VAL A  28   O  SER A  45           
SHEET    3   B 8 GLU A   2  LEU A   6  1  N  PHE A   5   O  THR A  27           
SHEET    4   B 8 TYR A  59  ALA A  62  1  O  ILE A  61   N  GLY A   4           
SHEET    5   B 8 GLY A  89  ASP A  92  1  O  ILE A  91   N  THR A  60           
SHEET    6   B 8 ARG A 114  GLU A 117  1  O  ARG A 114   N  TYR A  90           
SHEET    7   B 8 LEU A 132  GLY A 138 -1  O  ALA A 137   N  GLU A 117           
SHEET    8   B 8 GLY A 154  TYR A 159  1  O  PHE A 158   N  ILE A 134           
SITE     1 AC1  6 LYS A  25  SER A  45  CYS A  47  GLU A  48                    
SITE     2 AC1  6 GLU A  52  LYS A  56                                          
CRYST1  156.543  156.543   75.467  90.00  90.00  90.00 I 41 2 2     16          
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      0.006388  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013251        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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