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Database: PDB
Entry: 2GO1
LinkDB: 2GO1
Original site: 2GO1 
HEADER    OXIDOREDUCTASE                          12-APR-06   2GO1              
TITLE     NAD-DEPENDENT FORMATE DEHYDROGENASE FROM PSEUDOMONAS SP.101           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NAD-DEPENDENT FORMATE DEHYDROGENASE;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FORMATE DEHYDROGENASE, FDH;                                 
COMPND   5 EC: 1.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;                                
SOURCE   3 ORGANISM_TAXID: 33067;                                               
SOURCE   4 STRAIN: 101;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL2;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFDH8A                                    
KEYWDS    OXIDOREDUCTASE (ALDEHUDE (D), NAD+(A)), OXIDOREDUCTASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,T.N.STEKHANOVA,K.M.BOIKO,    
AUTHOR   2 V.O.POPOV                                                            
REVDAT   3   13-JUL-11 2GO1    1       VERSN                                    
REVDAT   2   24-FEB-09 2GO1    1       VERSN                                    
REVDAT   1   02-MAY-06 2GO1    0                                                
JRNL        AUTH   E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,T.N.STEKHANOVA,     
JRNL        AUTH 2 K.M.BOIKO,V.O.POPOV                                          
JRNL        TITL   STRUCTURE OF A NEW CRYSTAL MODIFICATION OF THE BACTERIAL     
JRNL        TITL 2 NAD-DEPENDENT FORMATE DEHYDROGENASE WITH A RESOLUTION OF 2.1 
JRNL        TITL 3 A                                                            
JRNL        REF    CRYSTALLOGRAPHY REPORTS       V.  50   796 2005              
JRNL        REFN                   ISSN 1063-7745                               
JRNL        DOI    10.1134/1.2049398                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24447                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1319                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2310                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 237                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.46000                                              
REMARK   3    B22 (A**2) : 1.46000                                              
REMARK   3    B33 (A**2) : -2.91000                                             
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): 0.211         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.190         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.055         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3022 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4121 ; 1.737 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   375 ; 7.148 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;37.997 ;23.406       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   484 ;15.812 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.317 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   457 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2325 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1544 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2079 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   209 ; 0.171 ; 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):   129 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    48 ; 0.195 ; 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):  1919 ; 1.034 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3032 ; 1.694 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1258 ; 2.744 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1089 ; 4.090 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2GO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-APR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037347.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.009                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARHKL, DENZO                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29590                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2NAC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE (48% SATURATED), 8%     
REMARK 280  MPD, 0.1M HEPES, PH 7.3, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 290K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       46.65000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.52500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.65000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.52500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.65000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.65000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.52500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.65000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.65000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       51.52500            
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        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 7970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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        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 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     0                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     ALA A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     TYR A   381                                                      
REMARK 465     SER A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     ASN A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     THR A   387                                                      
REMARK 465     GLY A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     ALA A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     PHE A   396                                                      
REMARK 465     LYS A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     VAL A   400                                                      
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    HOH A   545     O    HOH A   548              2.07            
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    LEU A  57       19.40     51.92                                   
REMARK 500    TRP A  99       71.42   -161.28                                   
REMARK 500    SER A 124       28.80   -156.64                                   
REMARK 500    TYR A 144       -2.13     74.91                                   
REMARK 500    TRP A 177      -71.63   -137.83                                   
REMARK 500    ALA A 198      135.91     88.86                                   
REMARK 500    ALA A 199       56.85   -118.18                                   
REMARK 500    ALA A 283      -89.22    -80.36                                   
REMARK 500    HIS A 319      127.70    -39.76                                   
REMARK 500    ILE A 333      -10.61   -143.26                                   
REMARK 500    ARG A 362      135.91    -38.57                                   
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 458        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 497        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A 498        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 514        DISTANCE =  7.92 ANGSTROMS                       
REMARK 525    HOH A 601        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 632        DISTANCE =  5.28 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NAD   RELATED DB: PDB                                   
REMARK 900 THE HOLO FORM OF THE SAME PROTEIN COMPLEXED WITH NAD AND             
REMARK 900 AZIDE                                                                
REMARK 900 RELATED ID: 2NAC   RELATED DB: PDB                                   
REMARK 900 THE APO FORM OF THE SAME PROTEIN                                     
DBREF  2GO1 A    1   400  UNP    P33160   FDH_PSESR        1    400             
SEQADV 2GO1 MET A    0  UNP  P33160              INITIATING METHIONINE          
SEQRES   1 A  401  MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL          
SEQRES   2 A  401  ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO          
SEQRES   3 A  401  LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR          
SEQRES   4 A  401  PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY          
SEQRES   5 A  401  SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU          
SEQRES   6 A  401  SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP          
SEQRES   7 A  401  GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA          
SEQRES   8 A  401  ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU          
SEQRES   9 A  401  THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU          
SEQRES  10 A  401  ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU          
SEQRES  11 A  401  GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL          
SEQRES  12 A  401  THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL          
SEQRES  13 A  401  MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER          
SEQRES  14 A  401  HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP          
SEQRES  15 A  401  CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL          
SEQRES  16 A  401  GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU          
SEQRES  17 A  401  ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR          
SEQRES  18 A  401  ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU          
SEQRES  19 A  401  ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO          
SEQRES  20 A  401  VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO          
SEQRES  21 A  401  GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU          
SEQRES  22 A  401  PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY          
SEQRES  23 A  401  LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU          
SEQRES  24 A  401  SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE          
SEQRES  25 A  401  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET          
SEQRES  26 A  401  PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR          
SEQRES  27 A  401  LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU          
SEQRES  28 A  401  ILE LEU GLU CYS PHE PHE GLU GLY ARG PRO ILE ARG ASP          
SEQRES  29 A  401  GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR          
SEQRES  30 A  401  GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY          
SEQRES  31 A  401  SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL                  
HET    SO4  A 401       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HOH   *237(H2 O)                                                    
HELIX    1   1 GLY A   55  GLY A   58  5                                   4    
HELIX    2   2 LEU A   59  ASN A   66  1                                   8    
HELIX    3   3 SER A   81  VAL A   88  1                                   8    
HELIX    4   4 THR A  104  ALA A  111  1                                   8    
HELIX    5   5 ASP A  128  ARG A  135  1                                   8    
HELIX    6   6 ASN A  146  ARG A  163  1                                  18    
HELIX    7   7 ASN A  164  LYS A  174  1                                  11    
HELIX    8   8 ASN A  178  SER A  184  1                                   7    
HELIX    9   9 GLY A  200  ALA A  211  1                                  12    
HELIX   10  10 PRO A  212  ASP A  214  5                                   3    
HELIX   11  11 PRO A  226  LEU A  233  1                                   8    
HELIX   12  12 THR A  240  TYR A  245  1                                   6    
HELIX   13  13 PRO A  246  CYS A  248  5                                   3    
HELIX   14  14 THR A  269  PHE A  273  5                                   5    
HELIX   15  15 ARG A  284  CYS A  288  5                                   5    
HELIX   16  16 ASP A  289  SER A  299  1                                  11    
HELIX   17  17 HIS A  319  THR A  323  5                                   5    
HELIX   18  18 ILE A  333  THR A  336  5                                   4    
HELIX   19  19 THR A  337  GLY A  358  1                                  22    
SHEET    1   A 6 THR A  69  THR A  73  0                                        
SHEET    2   A 6 LYS A   2  VAL A   6  1  N  VAL A   3   O  THR A  69           
SHEET    3   A 6 VAL A  92  SER A  95  1  O  VAL A  92   N  LEU A   4           
SHEET    4   A 6 LEU A 116  THR A 119  1  O  LEU A 118   N  VAL A  93           
SHEET    5   A 6 THR A 138  GLU A 141  1  O  THR A 138   N  ALA A 117           
SHEET    6   A 6 LEU A 366  VAL A 368 -1  O  ILE A 367   N  VAL A 139           
SHEET    1   B 6 THR A 236  TRP A 237  0                                        
SHEET    2   B 6 HIS A 216  THR A 220  1  N  TYR A 219   O  THR A 236           
SHEET    3   B 6 HIS A 193  VAL A 197  1  N  VAL A 194   O  HIS A 216           
SHEET    4   B 6 VAL A 250  LEU A 253  1  O  THR A 252   N  GLY A 195           
SHEET    5   B 6 ALA A 277  ASN A 281  1  O  TYR A 278   N  VAL A 251           
SHEET    6   B 6 LEU A 302  GLY A 307  1  O  ALA A 306   N  ASN A 281           
CISPEP   1 PHE A  311    PRO A  312          0        -7.79                     
CISPEP   2 GLN A  313    PRO A  314          0        -8.28                     
SITE     1 AC1  5 GLY A 200  ARG A 201  ILE A 202  HOH A 459                    
SITE     2 AC1  5 HOH A 517                                                     
CRYST1   93.300   93.300  103.050  90.00  90.00  90.00 P 42 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      0.010718  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010718  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009704        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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