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Database: PDB
Entry: 3BAZ
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Original site: 3BAZ 
HEADER    OXIDOREDUCTASE                          09-NOV-07   3BAZ              
TITLE     STRUCTURE OF HYDROXYPHENYLPYRUVATE REDUCTASE FROM COLEUS BLUMEI IN    
TITLE    2 COMPLEX WITH NADP+                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROXYPHENYLPYRUVATE REDUCTASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HPPR;                                                       
COMPND   5 EC: 1.1.1.237;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SOLENOSTEMON SCUTELLARIOIDES;                   
SOURCE   3 ORGANISM_COMMON: COLEUS BLUMEI;                                      
SOURCE   4 ORGANISM_TAXID: 4142;                                                
SOURCE   5 GENE: HPPR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    OXIDOREDUCTASE, PYRUVATE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.JANIAK,G.KLEBE,M.PETERSEN,A.HEINE                                   
REVDAT   4   25-APR-12 3BAZ    1       JRNL   VERSN                             
REVDAT   3   05-MAY-10 3BAZ    1       JRNL                                     
REVDAT   2   24-FEB-09 3BAZ    1       VERSN                                    
REVDAT   1   11-NOV-08 3BAZ    0                                                
JRNL        AUTH   V.JANIAK,M.PETERSEN,M.ZENTGRAF,G.KLEBE,A.HEINE               
JRNL        TITL   STRUCTURE AND SUBSTRATE DOCKING OF A HYDROXY(PHENYL)PYRUVATE 
JRNL        TITL 2 REDUCTASE FROM THE HIGHER PLANT COLEUS BLUMEI BENTH          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   593 2010              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   20445235                                                     
JRNL        DOI    10.1107/S0907444910006360                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.210                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.210                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.260                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1065                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 22256                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.194                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 17964                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2376                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 48                                            
REMARK   3   SOLVENT ATOMS      : 144                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2567.50                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 10285                   
REMARK   3   NUMBER OF RESTRAINTS                     : 9957                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.005                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.020                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.023                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.025                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.029                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.009                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.047                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BAZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045299.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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 RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 12.300                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.55900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO                    
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BA1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG1000, 0.1M IMIDAZOL, PH7.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 299K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.30000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.75000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.65000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.75000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      166.95000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.75000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       55.65000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.75000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      166.95000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
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      111.30000            
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: 7520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.9 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        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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      HOH A 638  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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER 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     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
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     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
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    CYS A  10   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 154   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  13      108.31   -169.18                                   
REMARK 500    ASN A  52     -157.52   -157.91                                   
REMARK 500    LEU A  65       65.94   -119.55                                   
REMARK 500    ASP A  98      -47.47     64.21                                   
REMARK 500    THR A 139     -150.71   -120.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 594        DISTANCE =  5.37 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BA1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HYDROXYPHENYLPYRUVATE REDUCTASE FROM COLEUS             
REMARK 900 BLUMEI AT 1.47A RESOLUTION                                           
DBREF  3BAZ A    1   313  UNP    Q65CJ7   Q65CJ7_SOLSC     1    313             
SEQADV 3BAZ MET A  -19  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ GLY A  -18  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ SER A  -17  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ SER A  -16  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -15  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -14  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -13  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -12  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -11  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A  -10  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ SER A   -9  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ SER A   -8  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ GLY A   -7  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ LEU A   -6  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ VAL A   -5  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ PRO A   -4  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ ARG A   -3  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ GLY A   -2  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ SER A   -1  UNP  Q65CJ7              EXPRESSION TAG                 
SEQADV 3BAZ HIS A    0  UNP  Q65CJ7              EXPRESSION TAG                 
SEQRES   1 A  333  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  333  LEU VAL PRO ARG GLY SER HIS MET GLU ALA ILE GLY VAL          
SEQRES   3 A  333  LEU MET MET CYS PRO MET SER THR TYR LEU GLU GLN GLU          
SEQRES   4 A  333  LEU ASP LYS ARG PHE LYS LEU PHE ARG TYR TRP THR GLN          
SEQRES   5 A  333  PRO ALA GLN ARG ASP PHE LEU ALA LEU GLN ALA GLU SER          
SEQRES   6 A  333  ILE ARG ALA VAL VAL GLY ASN SER ASN ALA GLY ALA ASP          
SEQRES   7 A  333  ALA GLU LEU ILE ASP ALA LEU PRO LYS LEU GLU ILE VAL          
SEQRES   8 A  333  SER SER PHE SER VAL GLY LEU ASP LYS VAL ASP LEU ILE          
SEQRES   9 A  333  LYS CYS GLU GLU LYS GLY VAL ARG VAL THR ASN THR PRO          
SEQRES  10 A  333  ASP VAL LEU THR ASP ASP VAL ALA ASP LEU ALA ILE GLY          
SEQRES  11 A  333  LEU ILE LEU ALA VAL LEU ARG ARG ILE CYS GLU CYS ASP          
SEQRES  12 A  333  LYS TYR VAL ARG ARG GLY ALA TRP LYS PHE GLY ASP PHE          
SEQRES  13 A  333  LYS LEU THR THR LYS PHE SER GLY LYS ARG VAL GLY ILE          
SEQRES  14 A  333  ILE GLY LEU GLY ARG ILE GLY LEU ALA VAL ALA GLU ARG          
SEQRES  15 A  333  ALA GLU ALA PHE ASP CYS PRO ILE SER TYR PHE SER ARG          
SEQRES  16 A  333  SER LYS LYS PRO ASN THR ASN TYR THR TYR TYR GLY SER          
SEQRES  17 A  333  VAL VAL GLU LEU ALA SER ASN SER ASP ILE LEU VAL VAL          
SEQRES  18 A  333  ALA CYS PRO LEU THR PRO GLU THR THR HIS ILE ILE ASN          
SEQRES  19 A  333  ARG GLU VAL ILE ASP ALA LEU GLY PRO LYS GLY VAL LEU          
SEQRES  20 A  333  ILE ASN ILE GLY ARG GLY PRO HIS VAL ASP GLU PRO GLU          
SEQRES  21 A  333  LEU VAL SER ALA LEU VAL GLU GLY ARG LEU GLY GLY ALA          
SEQRES  22 A  333  GLY LEU ASP VAL PHE GLU ARG GLU PRO GLU VAL PRO GLU          
SEQRES  23 A  333  LYS LEU PHE GLY LEU GLU ASN VAL VAL LEU LEU PRO HIS          
SEQRES  24 A  333  VAL GLY SER GLY THR VAL GLU THR ARG LYS VAL MET ALA          
SEQRES  25 A  333  ASP LEU VAL VAL GLY ASN LEU GLU ALA HIS PHE SER GLY          
SEQRES  26 A  333  LYS PRO LEU LEU THR PRO VAL VAL                              
HET    NAP  A 500      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   2  NAP    C21 H28 N7 O17 P3                                            
FORMUL   3  HOH   *144(H2 O)                                                    
HELIX    1   1 SER A   13  LYS A   22  1                                  10    
HELIX    2   2 TRP A   30  GLN A   32  5                                   3    
HELIX    3   3 ALA A   34  ALA A   43  1                                  10    
HELIX    4   4 ASP A   58  LEU A   65  1                                   8    
HELIX    5   5 ASP A   82  LYS A   89  1                                   8    
HELIX    6   6 LEU A  100  ARG A  117  1                                  18    
HELIX    7   7 ARG A  118  ARG A  128  1                                  11    
HELIX    8   8 GLY A  129  GLY A  134  5                                   6    
HELIX    9   9 GLY A  153  ALA A  165  1                                  13    
HELIX   10  10 SER A  188  ASN A  195  1                                   8    
HELIX   11  11 ASN A  214  GLY A  222  1                                   9    
HELIX   12  12 ARG A  232  VAL A  236  5                                   5    
HELIX   13  13 ASP A  237  GLU A  247  1                                  11    
HELIX   14  14 PRO A  265  LEU A  271  5                                   7    
HELIX   15  15 THR A  284  PHE A  303  1                                  20    
SHEET    1   A 5 LYS A  25  ARG A  28  0                                        
SHEET    2   A 5 GLY A   5  MET A   8  1  N  VAL A   6   O  PHE A  27           
SHEET    3   A 5 ILE A  46  GLY A  51  1  O  VAL A  50   N  LEU A   7           
SHEET    4   A 5 ILE A  70  SER A  73  1  O  SER A  72   N  VAL A  49           
SHEET    5   A 5 ARG A  92  THR A  94  1  O  THR A  94   N  SER A  73           
SHEET    1   B 7 THR A 184  TYR A 185  0                                        
SHEET    2   B 7 ILE A 170  PHE A 173  1  N  TYR A 172   O  THR A 184           
SHEET    3   B 7 VAL A 147  ILE A 150  1  N  VAL A 147   O  SER A 171           
SHEET    4   B 7 ILE A 198  VAL A 201  1  O  VAL A 200   N  ILE A 150           
SHEET    5   B 7 VAL A 226  ASN A 229  1  O  ILE A 228   N  LEU A 199           
SHEET    6   B 7 GLY A 252  LEU A 255  1  O  GLY A 254   N  ASN A 229           
SHEET    7   B 7 VAL A 274  LEU A 276  1  O  VAL A 275   N  LEU A 255           
CISPEP   1 GLU A  261    PRO A  262          0         2.07                     
SITE     1 AC1 25 LYS A  25  GLY A 151  LEU A 152  GLY A 153                    
SITE     2 AC1 25 ARG A 154  ILE A 155  SER A 174  ARG A 175                    
SITE     3 AC1 25 SER A 176  ALA A 202  CYS A 203  PRO A 204                    
SITE     4 AC1 25 THR A 209  ILE A 230  GLY A 231  ARG A 232                    
SITE     5 AC1 25 ASP A 256  HIS A 279  GLY A 281  HOH A 511                    
SITE     6 AC1 25 HOH A 513  HOH A 589  HOH A 592  HOH A 610                    
SITE     7 AC1 25 HOH A 611                                                     
CRYST1   63.500   63.500  222.600  90.00  90.00  90.00 P 41 21 2     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      0.015748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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