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Database: PDB
Entry: 3D3F
LinkDB: 3D3F
Original site: 3D3F 
HEADER    OXIDOREDUCTASE                          10-MAY-08   3D3F              
TITLE     CRYSTAL STRUCTURE OF YVGN AND COFACTOR NADPH FROM BACILLUS SUBTILIS   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: YVGN PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PUTATIVE REDUCTASE PROTEIN, YVGN;                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: YVGN;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALDO-KETO REDUCTASE, OXIDOREDUCTASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.F.ZHOU,J.LEI,X.D.SU                                                 
REVDAT   4   25-OCT-17 3D3F    1       REMARK                                   
REVDAT   3   29-JAN-14 3D3F    1       JRNL                                     
REVDAT   2   13-JUL-11 3D3F    1       VERSN                                    
REVDAT   1   28-APR-09 3D3F    0                                                
JRNL        AUTH   J.LEI,Y.F.ZHOU,L.F.LI,X.-D.SU                                
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL ANALYSES OF YVGN AND YTBE FROM    
JRNL        TITL 2 BACILLUS SUBTILIS                                            
JRNL        REF    PROTEIN SCI.                  V.  18  1792 2009              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   19585557                                                     
JRNL        DOI    10.1002/PRO.178                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20421                          
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 + TEST SET) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1065                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1008                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4452                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 22.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.58                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.20000                                              
REMARK   3    B22 (A**2) : -3.37000                                             
REMARK   3    B33 (A**2) : 1.18000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.916         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.363         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.277         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.879        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4643 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6291 ; 1.992 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   548 ; 8.207 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   227 ;38.338 ;25.507       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   846 ;20.110 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;23.101 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   685 ; 0.157 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3456 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2400 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3055 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   226 ; 0.166 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    32 ; 0.244 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.270 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2840 ; 0.716 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4407 ; 1.166 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2095 ; 1.983 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1884 ; 2.963 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9054  12.1735 -21.8502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1354 T22:  -0.0998                                     
REMARK   3      T33:  -0.0834 T12:   0.0084                                     
REMARK   3      T13:  -0.0016 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8156 L22:   1.4120                                     
REMARK   3      L33:   2.5456 L12:   0.1184                                     
REMARK   3      L13:   0.0286 L23:   0.3896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0270 S12:  -0.0199 S13:   0.0027                       
REMARK   3      S21:  -0.0270 S22:  -0.0061 S23:  -0.0310                       
REMARK   3      S31:  -0.0635 S32:  -0.0502 S33:   0.0332                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1103  43.2027  -6.6203              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1190 T22:  -0.0979                                     
REMARK   3      T33:  -0.1099 T12:   0.0064                                     
REMARK   3      T13:   0.0046 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1006 L22:   2.2383                                     
REMARK   3      L33:   2.8123 L12:  -0.2620                                     
REMARK   3      L13:   0.2349 L23:   0.3488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0055 S12:   0.0260 S13:   0.0296                       
REMARK   3      S21:   0.0569 S22:  -0.0035 S23:  -0.0152                       
REMARK   3      S31:   0.1913 S32:   0.0093 S33:  -0.0020                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047542.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-07                          
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          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SMART6000                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : PROTEUM                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23334                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.10000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.260                              
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: 3B3E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M SODIUM NITRATE, 40% PEG3350, PH     
REMARK 280  7.5, VAPOR DIFFUSION, TEMPERATURE 289K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       40.25850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.64250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.25850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.64250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASP A   117     O    HOH A   277              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A  24   CB    VAL A  24   CG1    -0.179                       
REMARK 500    GLU A  57   CD    GLU A  57   OE1    -0.071                       
REMARK 500    GLU A  57   CD    GLU A  57   OE2    -0.077                       
REMARK 500    ASP A 117   CB    ASP A 117   CG     -0.169                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS A 116   N   -  CA  -  C   ANGL. DEV. =  19.1 DEGREES          
REMARK 500    LYS B 116   CB  -  CA  -  C   ANGL. DEV. = -14.5 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    LYS A  55        9.88     85.88                                   
REMARK 500    ASP A 117      -30.70   -144.27                                   
REMARK 500    ASP B 117      -32.04   -138.03                                   
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 NDP A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 1                   
DBREF  3D3F A    2   276  UNP    O32210   O32210_BACSU     2    276             
DBREF  3D3F B    2   276  UNP    O32210   O32210_BACSU     2    276             
SEQRES   1 A  275  PRO THR SER LEU LYS ASP THR VAL LYS LEU HIS ASN GLY          
SEQRES   2 A  275  VAL GLU MET PRO TRP PHE GLY LEU GLY VAL PHE LYS VAL          
SEQRES   3 A  275  GLU ASN GLY ASN GLU ALA THR GLU SER VAL LYS ALA ALA          
SEQRES   4 A  275  ILE LYS ASN GLY TYR ARG SER ILE ASP THR ALA ALA ILE          
SEQRES   5 A  275  TYR LYS ASN GLU GLU GLY VAL GLY ILE GLY ILE LYS GLU          
SEQRES   6 A  275  SER GLY VAL ALA ARG GLU GLU LEU PHE ILE THR SER LYS          
SEQRES   7 A  275  VAL TRP ASN GLU ASP GLN GLY TYR GLU THR THR LEU ALA          
SEQRES   8 A  275  ALA PHE GLU LYS SER LEU GLU ARG LEU GLN LEU ASP TYR          
SEQRES   9 A  275  LEU ASP LEU TYR LEU ILE HIS TRP PRO GLY LYS ASP LYS          
SEQRES  10 A  275  TYR LYS ASP THR TRP ARG ALA LEU GLU LYS LEU TYR LYS          
SEQRES  11 A  275  ASP GLY LYS ILE ARG ALA ILE GLY VAL SER ASN PHE GLN          
SEQRES  12 A  275  VAL HIS HIS LEU GLU GLU LEU LEU LYS ASP ALA GLU ILE          
SEQRES  13 A  275  LYS PRO MET VAL ASN GLN VAL GLU PHE HIS PRO ARG LEU          
SEQRES  14 A  275  THR GLN LYS GLU LEU ARG ASP TYR CYS LYS GLY GLN GLY          
SEQRES  15 A  275  ILE GLN LEU GLU ALA TRP SER PRO LEU MET GLN GLY GLN          
SEQRES  16 A  275  LEU LEU ASP ASN GLU VAL LEU THR GLN ILE ALA GLU LYS          
SEQRES  17 A  275  HIS ASN LYS SER VAL ALA GLN VAL ILE LEU ARG TRP ASP          
SEQRES  18 A  275  LEU GLN HIS GLY VAL VAL THR ILE PRO LYS SER ILE LYS          
SEQRES  19 A  275  GLU HIS ARG ILE ILE GLU ASN ALA ASP ILE PHE ASP PHE          
SEQRES  20 A  275  GLU LEU SER GLN GLU ASP MET ASP LYS ILE ASP ALA LEU          
SEQRES  21 A  275  ASN LYS ASP GLU ARG VAL GLY PRO ASN PRO ASP GLU LEU          
SEQRES  22 A  275  LEU PHE                                                      
SEQRES   1 B  275  PRO THR SER LEU LYS ASP THR VAL LYS LEU HIS ASN GLY          
SEQRES   2 B  275  VAL GLU MET PRO TRP PHE GLY LEU GLY VAL PHE LYS VAL          
SEQRES   3 B  275  GLU ASN GLY ASN GLU ALA THR GLU SER VAL LYS ALA ALA          
SEQRES   4 B  275  ILE LYS ASN GLY TYR ARG SER ILE ASP THR ALA ALA ILE          
SEQRES   5 B  275  TYR LYS ASN GLU GLU GLY VAL GLY ILE GLY ILE LYS GLU          
SEQRES   6 B  275  SER GLY VAL ALA ARG GLU GLU LEU PHE ILE THR SER LYS          
SEQRES   7 B  275  VAL TRP ASN GLU ASP GLN GLY TYR GLU THR THR LEU ALA          
SEQRES   8 B  275  ALA PHE GLU LYS SER LEU GLU ARG LEU GLN LEU ASP TYR          
SEQRES   9 B  275  LEU ASP LEU TYR LEU ILE HIS TRP PRO GLY LYS ASP LYS          
SEQRES  10 B  275  TYR LYS ASP THR TRP ARG ALA LEU GLU LYS LEU TYR LYS          
SEQRES  11 B  275  ASP GLY LYS ILE ARG ALA ILE GLY VAL SER ASN PHE GLN          
SEQRES  12 B  275  VAL HIS HIS LEU GLU GLU LEU LEU LYS ASP ALA GLU ILE          
SEQRES  13 B  275  LYS PRO MET VAL ASN GLN VAL GLU PHE HIS PRO ARG LEU          
SEQRES  14 B  275  THR GLN LYS GLU LEU ARG ASP TYR CYS LYS GLY GLN GLY          
SEQRES  15 B  275  ILE GLN LEU GLU ALA TRP SER PRO LEU MET GLN GLY GLN          
SEQRES  16 B  275  LEU LEU ASP ASN GLU VAL LEU THR GLN ILE ALA GLU LYS          
SEQRES  17 B  275  HIS ASN LYS SER VAL ALA GLN VAL ILE LEU ARG TRP ASP          
SEQRES  18 B  275  LEU GLN HIS GLY VAL VAL THR ILE PRO LYS SER ILE LYS          
SEQRES  19 B  275  GLU HIS ARG ILE ILE GLU ASN ALA ASP ILE PHE ASP PHE          
SEQRES  20 B  275  GLU LEU SER GLN GLU ASP MET ASP LYS ILE ASP ALA LEU          
SEQRES  21 B  275  ASN LYS ASP GLU ARG VAL GLY PRO ASN PRO ASP GLU LEU          
SEQRES  22 B  275  LEU PHE                                                      
HET    NDP  A   1      48                                                       
HET    NDP  B   1      48                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   5  HOH   *81(H2 O)                                                     
HELIX    1   1 GLY A   30  ASN A   43  1                                  14    
HELIX    2   2 ALA A   51  LYS A   55  5                                   5    
HELIX    3   3 ASN A   56  SER A   67  1                                  12    
HELIX    4   4 ALA A   70  LEU A   74  5                                   5    
HELIX    5   5 TRP A   81  GLN A   85  5                                   5    
HELIX    6   6 GLY A   86  GLN A  102  1                                  17    
HELIX    7   7 LYS A  118  ASP A  132  1                                  15    
HELIX    8   8 GLN A  144  ALA A  155  1                                  12    
HELIX    9   9 GLN A  172  GLN A  182  1                                  11    
HELIX   10  10 LEU A  192  GLN A  196  5                                   5    
HELIX   11  11 ASN A  200  ASN A  211  1                                  12    
HELIX   12  12 SER A  213  GLY A  226  1                                  14    
HELIX   13  13 LYS A  235  ASP A  244  1                                  10    
HELIX   14  14 SER A  251  ALA A  260  1                                  10    
HELIX   15  15 GLY B   30  ASN B   43  1                                  14    
HELIX   16  16 ASN B   56  SER B   67  1                                  12    
HELIX   17  17 ALA B   70  LEU B   74  5                                   5    
HELIX   18  18 TRP B   81  GLN B   85  5                                   5    
HELIX   19  19 GLY B   86  GLN B  102  1                                  17    
HELIX   20  20 LYS B  118  ASP B  132  1                                  15    
HELIX   21  21 GLN B  144  LYS B  153  1                                  10    
HELIX   22  22 GLN B  172  GLY B  183  1                                  12    
HELIX   23  23 LEU B  192  GLN B  196  5                                   5    
HELIX   24  24 ASN B  200  ASN B  211  1                                  12    
HELIX   25  25 SER B  213  HIS B  225  1                                  13    
HELIX   26  26 LYS B  235  ASP B  244  1                                  10    
HELIX   27  27 SER B  251  LEU B  261  1                                  11    
SHEET    1   A 2 THR A   8  LYS A  10  0                                        
SHEET    2   A 2 GLU A  16  PRO A  18 -1  O  MET A  17   N  VAL A   9           
SHEET    1   B 8 LEU A  22  GLY A  23  0                                        
SHEET    2   B 8 SER A  47  ASP A  49  1  O  ASP A  49   N  LEU A  22           
SHEET    3   B 8 PHE A  75  VAL A  80  1  O  PHE A  75   N  ILE A  48           
SHEET    4   B 8 LEU A 106  ILE A 111  1  O  LEU A 110   N  VAL A  80           
SHEET    5   B 8 ILE A 135  SER A 141  1  O  ARG A 136   N  LEU A 106           
SHEET    6   B 8 VAL A 161  GLU A 165  1  O  VAL A 161   N  VAL A 140           
SHEET    7   B 8 GLN A 185  TRP A 189  1  O  GLN A 185   N  ASN A 162           
SHEET    8   B 8 VAL A 228  THR A 229  1  O  VAL A 228   N  ALA A 188           
SHEET    1   C 2 THR B   8  LYS B  10  0                                        
SHEET    2   C 2 GLU B  16  PRO B  18 -1  O  MET B  17   N  VAL B   9           
SHEET    1   D 8 LEU B  22  GLY B  23  0                                        
SHEET    2   D 8 SER B  47  ASP B  49  1  O  ASP B  49   N  LEU B  22           
SHEET    3   D 8 PHE B  75  VAL B  80  1  O  PHE B  75   N  ILE B  48           
SHEET    4   D 8 LEU B 106  ILE B 111  1  O  LEU B 110   N  VAL B  80           
SHEET    5   D 8 ILE B 135  SER B 141  1  O  ARG B 136   N  LEU B 106           
SHEET    6   D 8 VAL B 161  GLU B 165  1  O  VAL B 161   N  VAL B 140           
SHEET    7   D 8 GLN B 185  TRP B 189  1  O  TRP B 189   N  VAL B 164           
SHEET    8   D 8 VAL B 228  THR B 229  1  O  VAL B 228   N  ALA B 188           
SITE     1 AC1 29 GLY A  23  VAL A  24  PHE A  25  ASP A  49                    
SITE     2 AC1 29 TYR A  54  LYS A  79  HIS A 112  SER A 141                    
SITE     3 AC1 29 ASN A 142  GLN A 163  TRP A 189  SER A 190                    
SITE     4 AC1 29 PRO A 191  LEU A 192  MET A 193  GLN A 194                    
SITE     5 AC1 29 LEU A 198  ALA A 215  ILE A 230  PRO A 231                    
SITE     6 AC1 29 LYS A 232  SER A 233  ILE A 234  LYS A 235                    
SITE     7 AC1 29 ARG A 238  GLU A 241  ASN A 242  HOH A 284                    
SITE     8 AC1 29 HOH A 296                                                     
SITE     1 AC2 26 GLY B  23  VAL B  24  PHE B  25  ASP B  49                    
SITE     2 AC2 26 TYR B  54  LYS B  79  HIS B 112  SER B 141                    
SITE     3 AC2 26 ASN B 142  GLN B 163  TRP B 189  SER B 190                    
SITE     4 AC2 26 PRO B 191  LEU B 192  MET B 193  GLN B 194                    
SITE     5 AC2 26 LEU B 198  ILE B 230  PRO B 231  LYS B 232                    
SITE     6 AC2 26 SER B 233  ILE B 234  LYS B 235  ARG B 238                    
SITE     7 AC2 26 ASN B 242  HOH B 321                                          
CRYST1   80.517  123.285   57.226  90.00  90.00  90.00 P 21 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      0.012420  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008111  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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