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Database: PDB
Entry: 1SIQ
LinkDB: 1SIQ
Original site: 1SIQ 
HEADER    OXIDOREDUCTASE                          01-MAR-04   1SIQ              
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 STRAIN:BL21                                        
KEYWDS    ACYL-COA DEHYDROGENASE, DECARBOXYLATION, FLAVIN PROTEIN,              
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WANG,Z.FU,R.PASCHKE,S.GOODMAN,F.E.FRERMAN,J.J.KIM                   
REVDAT   3   13-JUL-11 1SIQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1SIQ    1       VERSN                                    
REVDAT   1   07-SEP-04 1SIQ    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.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 126683.210                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28832                          
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) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1936                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3510                       
REMARK   3   BIN FREE R VALUE                    : 0.3610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 151                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
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          : 53                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.00                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.55000                                              
REMARK   3    B22 (A**2) : 1.55000                                              
REMARK   3    B33 (A**2) : -3.11000                                             
REMARK   3    B12 (A**2) : 0.94000                                              
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.36                            
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) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
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) : 2.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.950 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.410 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.440 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 67.98                                                
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  : 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   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1SIQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021738.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-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                  : NULL                               
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   : 28832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
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) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
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       42.67333            
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       85.34667            
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       42.67333            
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       85.34667            
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       42.67333            
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       85.34667            
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       42.67333            
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       85.34667            
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: 25040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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      -58.48000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      101.29033            
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      -42.67333            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -58.48000            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000      101.29033            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      -42.67333            
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     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       67.79   -164.87                                   
REMARK 500    LEU A 135      -52.87   -121.47                                   
REMARK 500    ASN A 171      -15.60     79.66                                   
REMARK 500    LEU A 239      -23.51     56.00                                   
REMARK 500    HIS A 355      -32.79     60.68                                   
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SIR   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE AND MECHANISM OF HUMAN GLUTARYL-COA            
REMARK 900 DEHYDROGENASE                                                        
DBREF  1SIQ A    3   394  UNP    Q92947   GCDH_HUMAN      47    438             
SEQRES   1 A  392  GLU PHE ASP TRP GLN ASP PRO LEU VAL LEU GLU GLU GLN          
SEQRES   2 A  392  LEU THR THR ASP GLU ILE LEU ILE ARG ASP THR PHE ARG          
SEQRES   3 A  392  THR TYR CYS GLN GLU ARG LEU MET PRO ARG ILE LEU LEU          
SEQRES   4 A  392  ALA ASN ARG ASN GLU VAL PHE HIS ARG GLU ILE ILE SER          
SEQRES   5 A  392  GLU MET GLY GLU LEU GLY VAL LEU GLY PRO THR ILE LYS          
SEQRES   6 A  392  GLY TYR GLY CYS ALA GLY VAL SER SER VAL ALA TYR GLY          
SEQRES   7 A  392  LEU LEU ALA ARG GLU LEU GLU ARG VAL ASP SER GLY TYR          
SEQRES   8 A  392  ARG SER ALA MET SER VAL GLN SER SER LEU VAL MET HIS          
SEQRES   9 A  392  PRO ILE TYR ALA TYR GLY SER GLU GLU GLN ARG GLN LYS          
SEQRES  10 A  392  TYR LEU PRO GLN LEU ALA LYS GLY GLU LEU LEU GLY CYS          
SEQRES  11 A  392  PHE GLY LEU THR GLU PRO ASN SER GLY SER ASP PRO SER          
SEQRES  12 A  392  SER MET GLU THR ARG ALA HIS TYR ASN SER SER ASN LYS          
SEQRES  13 A  392  SER TYR THR LEU ASN GLY THR LYS THR TRP ILE THR ASN          
SEQRES  14 A  392  SER PRO MET ALA ASP LEU PHE VAL VAL TRP ALA ARG CYS          
SEQRES  15 A  392  GLU ASP GLY CYS ILE ARG GLY PHE LEU LEU GLU LYS GLY          
SEQRES  16 A  392  MET ARG GLY LEU SER ALA PRO ARG ILE GLN GLY LYS PHE          
SEQRES  17 A  392  SER LEU ARG ALA SER ALA THR GLY MET ILE ILE MET ASP          
SEQRES  18 A  392  GLY VAL GLU VAL PRO GLU GLU ASN VAL LEU PRO GLY ALA          
SEQRES  19 A  392  SER SER LEU GLY GLY PRO PHE GLY CYS LEU ASN ASN ALA          
SEQRES  20 A  392  ARG TYR GLY ILE ALA TRP GLY VAL LEU GLY ALA SER GLU          
SEQRES  21 A  392  PHE CYS LEU HIS THR ALA ARG GLN TYR ALA LEU ASP ARG          
SEQRES  22 A  392  MET GLN PHE GLY VAL PRO LEU ALA ARG ASN GLN LEU ILE          
SEQRES  23 A  392  GLN LYS LYS LEU ALA ASP MET LEU THR GLU ILE THR LEU          
SEQRES  24 A  392  GLY LEU HIS ALA CYS LEU GLN LEU GLY ARG LEU LYS ASP          
SEQRES  25 A  392  GLN ASP LYS ALA ALA PRO GLU MET VAL SER LEU LEU LYS          
SEQRES  26 A  392  ARG ASN ASN CYS GLY LYS ALA LEU ASP ILE ALA ARG GLN          
SEQRES  27 A  392  ALA ARG ASP MET LEU GLY GLY ASN GLY ILE SER ASP GLU          
SEQRES  28 A  392  TYR HIS VAL ILE ARG HIS ALA MET ASN LEU GLU ALA VAL          
SEQRES  29 A  392  ASN THR TYR GLU GLY THR HIS ASP ILE HIS ALA LEU ILE          
SEQRES  30 A  392  LEU GLY ARG ALA ILE THR GLY ILE GLN ALA PHE THR ALA          
SEQRES  31 A  392  SER LYS                                                      
HET    FAD  A 399      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  HOH   *128(H2 O)                                                    
HELIX    1   1 VAL A   11  LEU A   16  5                                   6    
HELIX    2   2 THR A   17  LEU A   35  1                                  19    
HELIX    3   3 LEU A   35  GLU A   46  1                                  12    
HELIX    4   4 ARG A   50  LEU A   59  1                                  10    
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 GLU A  230  VAL A  232  5                                   3    
HELIX   12  12 LEU A  239  ARG A  275  1                                  37    
HELIX   13  13 ASN A  285  GLN A  315  1                                  31    
HELIX   14  14 ALA A  319  LEU A  345  1                                  27    
HELIX   15  15 GLY A  346  TYR A  354  5                                   9    
HELIX   16  16 HIS A  355  ASN A  367  1                                  13    
HELIX   17  17 THR A  372  GLY A  386  1                                  15    
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 3 GLY A 131  GLY A 134  0                                        
SHEET    2   B 3 LEU A 177  CYS A 184  1  O  VAL A 179   N  GLY A 134           
SHEET    3   B 3 ILE A 189  GLU A 195 -1  O  PHE A 192   N  VAL A 180           
SHEET    1   C 6 GLY A 131  GLY A 134  0                                        
SHEET    2   C 6 LEU A 177  CYS A 184  1  O  VAL A 179   N  GLY A 134           
SHEET    3   C 6 ARG A 150  ASN A 154  1  N  ALA A 151   O  ARG A 183           
SHEET    4   C 6 SER A 159  THR A 170 -1  O  SER A 159   N  ASN A 154           
SHEET    5   C 6 THR A 217  PRO A 228 -1  O  GLY A 218   N  ILE A 169           
SHEET    6   C 6 LEU A 201  SER A 202 -1  N  SER A 202   O  ILE A 221           
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 29 PHE A 133  LEU A 135  THR A 136  GLY A 141                    
SITE     2 AC1 29 SER A 142  TRP A 168  THR A 170  LEU A 212                    
SITE     3 AC1 29 ARG A 275  GLN A 277  PHE A 278  LEU A 282                    
SITE     4 AC1 29 ASN A 285  GLN A 286  ASP A 343  MET A 344                    
SITE     5 AC1 29 GLY A 346  GLY A 347  ILE A 350  TYR A 369                    
SITE     6 AC1 29 THR A 372  PHE A 390  HOH A 401  HOH A 404                    
SITE     7 AC1 29 HOH A 406  HOH A 407  HOH A 423  HOH A 424                    
SITE     8 AC1 29 HOH A 425                                                     
CRYST1  116.960  116.960  128.020  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      0.008550  0.004936  0.000000        0.00000                         
SCALE2      0.000000  0.009873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007811        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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