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Database: PDB
Entry: 1SIR
LinkDB: 1SIR
Original site: 1SIR 
HEADER    OXIDOREDUCTASE                          01-MAR-04   1SIR              
TITLE     THE CRYSTAL STRUCTURE AND MECHANISM OF HUMAN GLUTARYL-COA             
TITLE    2 DEHYDROGENASE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTARYL-COA DEHYDROGENASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GCD;                                                        
COMPND   5 EC: 1.3.99.7                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: BACTERIAL:BL21                                               
KEYWDS    ACYL-COA DEHYDROGENASE, DECOBOXYLATION FLAVIN PROTEIN, OXIDOREDUCTASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WANG,Z.FU,R.PASCHKE,S.L.GOODMAN,F.E.FRERMAN,J.J.KIM                 
REVDAT   3   13-JUL-11 1SIR    1       VERSN                                    
REVDAT   2   24-FEB-09 1SIR    1       VERSN                                    
REVDAT   1   07-SEP-04 1SIR    0                                                
JRNL        AUTH   Z.FU,M.WANG,R.PASCHKE,K.S.RAO,F.E.FRERMAN,J.J.KIM            
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN GLUTARYL-COA DEHYDROGENASE WITH  
JRNL        TITL 2 AND WITHOUT AN ALTERNATE SUBSTRATE: STRUCTURAL BASES OF      
JRNL        TITL 3 DEHYDROGENATION AND DECARBOXYLATION REACTIONS                
JRNL        REF    BIOCHEMISTRY                  V.  43  9674 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15274622                                                     
JRNL        DOI    10.1021/BI049290C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 300083.740                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 13764                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1105                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 918                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE                    : 0.3680                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 79                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.041                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3011                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 77                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55000                                              
REMARK   3    B22 (A**2) : 0.55000                                              
REMARK   3    B33 (A**2) : -1.10000                                             
REMARK   3    B12 (A**2) : 16.78000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.47                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.380 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.660 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.020 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.030 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 40.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : FAD.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NBC.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : FAD.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NBC.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1SIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021739.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 6.5                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13764                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 61.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS 1.1                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1SIQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER, PEG5KMME, AMMONIUM           
REMARK 280  SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.67800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       85.35600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       42.67800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.35600            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.67800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       85.35600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       42.67800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       85.35600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 30650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 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 -1.000000  0.000000  0.000000      -58.36100            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      101.08422            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      -42.67800            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -58.36100            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000      101.08422            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      -42.67800            
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     ARG A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     SER A   393                                                      
REMARK 465     LYS A   394                                                      
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    ASP A   8       66.36   -161.41                                   
REMARK 500    GLU A  14       13.59    -66.76                                   
REMARK 500    ASN A 171      -11.97     77.31                                   
REMARK 500    HIS A 355      -37.26     63.30                                   
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 FAD A 399                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBC A 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SIQ   RELATED DB: PDB                                   
REMARK 900 NATIVE CRYSTAL                                                       
DBREF  1SIR A    1   394  UNP    Q92947   GCDH_HUMAN      45    440             
SEQRES   1 A  394  ARG PRO GLU PHE ASP TRP GLN ASP PRO LEU VAL LEU GLU          
SEQRES   2 A  394  GLU GLN LEU THR THR ASP GLU ILE LEU ILE ARG ASP THR          
SEQRES   3 A  394  PHE ARG THR TYR CYS GLN GLU ARG LEU MET PRO ARG ILE          
SEQRES   4 A  394  LEU LEU ALA ASN ARG ASN GLU VAL PHE HIS ARG GLU ILE          
SEQRES   5 A  394  ILE SER GLU MET GLY GLU LEU GLY VAL LEU GLY PRO THR          
SEQRES   6 A  394  ILE LYS GLY TYR GLY CYS ALA GLY VAL SER SER VAL ALA          
SEQRES   7 A  394  TYR GLY LEU LEU ALA ARG GLU LEU GLU ARG VAL ASP SER          
SEQRES   8 A  394  GLY TYR ARG SER ALA MET SER VAL GLN SER SER LEU VAL          
SEQRES   9 A  394  MET HIS PRO ILE TYR ALA TYR GLY SER GLU GLU GLN ARG          
SEQRES  10 A  394  GLN LYS TYR LEU PRO GLN LEU ALA LYS GLY GLU LEU LEU          
SEQRES  11 A  394  GLY CYS PHE GLY LEU THR GLU PRO ASN SER GLY SER ASP          
SEQRES  12 A  394  PRO SER SER MET GLU THR ARG ALA HIS TYR ASN SER SER          
SEQRES  13 A  394  ASN LYS SER TYR THR LEU ASN GLY THR LYS THR TRP ILE          
SEQRES  14 A  394  THR ASN SER PRO MET ALA ASP LEU PHE VAL VAL TRP ALA          
SEQRES  15 A  394  ARG CYS GLU ASP GLY CYS ILE ARG GLY PHE LEU LEU GLU          
SEQRES  16 A  394  LYS GLY MET ARG GLY LEU SER ALA PRO ARG ILE GLN GLY          
SEQRES  17 A  394  LYS PHE SER LEU ARG ALA SER ALA THR GLY MET ILE ILE          
SEQRES  18 A  394  MET ASP GLY VAL GLU VAL PRO GLU GLU ASN VAL LEU PRO          
SEQRES  19 A  394  GLY ALA SER SER LEU GLY GLY PRO PHE GLY CYS LEU ASN          
SEQRES  20 A  394  ASN ALA ARG TYR GLY ILE ALA TRP GLY VAL LEU GLY ALA          
SEQRES  21 A  394  SER GLU PHE CYS LEU HIS THR ALA ARG GLN TYR ALA LEU          
SEQRES  22 A  394  ASP ARG MET GLN PHE GLY VAL PRO LEU ALA ARG ASN GLN          
SEQRES  23 A  394  LEU ILE GLN LYS LYS LEU ALA ASP MET LEU THR GLU ILE          
SEQRES  24 A  394  THR LEU GLY LEU HIS ALA CYS LEU GLN LEU GLY ARG LEU          
SEQRES  25 A  394  LYS ASP GLN ASP LYS ALA ALA PRO GLU MET VAL SER LEU          
SEQRES  26 A  394  LEU LYS ARG ASN ASN CYS GLY LYS ALA LEU ASP ILE ALA          
SEQRES  27 A  394  ARG GLN ALA ARG ASP MET LEU GLY GLY ASN GLY ILE SER          
SEQRES  28 A  394  ASP GLU TYR HIS VAL ILE ARG HIS ALA MET ASN LEU GLU          
SEQRES  29 A  394  ALA VAL ASN THR TYR GLU GLY THR HIS ASP ILE HIS ALA          
SEQRES  30 A  394  LEU ILE LEU GLY ARG ALA ILE THR GLY ILE GLN ALA PHE          
SEQRES  31 A  394  THR ALA SER LYS                                              
HET    FAD  A 399      53                                                       
HET    NBC  A 400      56                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     NBC S-4-NITROBUTYRYL-COA                                             
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  NBC    C25 H41 N8 O19 P3 S                                          
FORMUL   4  HOH   *77(H2 O)                                                     
HELIX    1   1 LEU A   12  LEU A   16  5                                   5    
HELIX    2   2 THR A   17  ARG A   34  1                                  18    
HELIX    3   3 LEU A   35  ASN A   45  1                                  11    
HELIX    4   4 ARG A   50  GLY A   60  1                                  11    
HELIX    5   5 SER A   75  ARG A   88  1                                  14    
HELIX    6   6 ASP A   90  LEU A  103  1                                  14    
HELIX    7   7 VAL A  104  GLY A  112  1                                   9    
HELIX    8   8 SER A  113  LYS A  126  1                                  14    
HELIX    9   9 ASP A  143  MET A  147  5                                   5    
HELIX   10  10 SER A  172  ALA A  175  5                                   4    
HELIX   11  11 LEU A  239  ARG A  275  1                                  37    
HELIX   12  12 ASN A  285  GLN A  315  1                                  31    
HELIX   13  13 ALA A  319  LEU A  345  1                                  27    
HELIX   14  14 GLY A  346  TYR A  354  5                                   9    
HELIX   15  15 HIS A  355  ASN A  367  1                                  13    
HELIX   16  16 ASP A  374  GLY A  386  1                                  13    
SHEET    1   A 2 LYS A  67  GLY A  68  0                                        
SHEET    2   A 2 CYS A  71  ALA A  72 -1  O  CYS A  71   N  GLY A  68           
SHEET    1   B 6 GLY A 131  GLY A 134  0                                        
SHEET    2   B 6 LEU A 177  CYS A 184  1  O  VAL A 179   N  GLY A 134           
SHEET    3   B 6 ARG A 150  ASN A 154  1  N  ALA A 151   O  ARG A 183           
SHEET    4   B 6 SER A 159  THR A 170 -1  O  SER A 159   N  ASN A 154           
SHEET    5   B 6 THR A 217  PRO A 228 -1  O  GLY A 218   N  ILE A 169           
SHEET    6   B 6 LEU A 201  SER A 202 -1  N  SER A 202   O  ILE A 221           
SHEET    1   C 4 GLY A 131  GLY A 134  0                                        
SHEET    2   C 4 LEU A 177  CYS A 184  1  O  VAL A 179   N  GLY A 134           
SHEET    3   C 4 ILE A 189  GLU A 195 -1  O  PHE A 192   N  VAL A 180           
SHEET    4   C 4 VAL A 232  LEU A 233 -1  O  LEU A 233   N  GLY A 191           
SHEET    1   D 2 MET A 276  GLN A 277  0                                        
SHEET    2   D 2 VAL A 280  PRO A 281 -1  O  VAL A 280   N  GLN A 277           
SITE     1 AC1 24 PHE A 133  LEU A 135  THR A 136  GLY A 141                    
SITE     2 AC1 24 SER A 142  TRP A 168  ILE A 169  THR A 170                    
SITE     3 AC1 24 LEU A 212  ARG A 275  PHE A 278  LEU A 282                    
SITE     4 AC1 24 ASN A 285  GLN A 286  ASP A 343  MET A 344                    
SITE     5 AC1 24 GLY A 347  ILE A 350  THR A 372  PHE A 390                    
SITE     6 AC1 24 NBC A 400  HOH A 501  HOH A 502  HOH A 506                    
SITE     1 AC2 16 ARG A  94  SER A  95  LEU A 103  SER A 142                    
SITE     2 AC2 16 PRO A 144  THR A 170  PHE A 243  GLY A 244                    
SITE     3 AC2 16 LEU A 246  ASN A 247  ARG A 250  PRO A 320                    
SITE     4 AC2 16 TYR A 369  GLU A 370  ARG A 382  FAD A 399                    
CRYST1  116.722  116.722  128.034  90.00  90.00 120.00 P 64 2 2     12          
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      0.008567  0.004946  0.000000        0.00000                         
SCALE2      0.000000  0.009893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007810        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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