GenomeNet

Database: PDB
Entry: 1GDH
LinkDB: 1GDH
Original site: 1GDH 
HEADER    OXIDOREDUCTASE(CHOH (D)-NAD(P)+ (A))    22-SEP-93   1GDH              
TITLE     CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE                      
TITLE    2 DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-GLYCERATE DEHYDROGENASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.1.1.29;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HYPHOMICROBIUM METHYLOVORUM;                    
SOURCE   3 ORGANISM_TAXID: 84                                                   
KEYWDS    OXIDOREDUCTASE(CHOH (D)-NAD(P)+ (A))                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.GOLDBERG,T.YOSHIDA,P.BRICK                                        
REVDAT   4   24-FEB-09 1GDH    1       VERSN                                    
REVDAT   3   01-APR-03 1GDH    1       JRNL                                     
REVDAT   2   20-JUL-95 1GDH    1       JRNL   REMARK                            
REVDAT   1   31-JAN-94 1GDH    0                                                
JRNL        AUTH   J.D.GOLDBERG,T.YOSHIDA,P.BRICK                               
JRNL        TITL   CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE             
JRNL        TITL 2 DEHYDROGENASE AT 2.4 A RESOLUTION.                           
JRNL        REF    J.MOL.BIOL.                   V. 236  1123 1994              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8120891                                                      
JRNL        DOI    10.1016/0022-2836(94)90016-7                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.D.GOLDBERG,P.BRICK,T.YOSHIDA,T.MITSUNAGA,                  
REMARK   1  AUTH 2 T.OSHIRO,M.SHIMAO,Y.IZUMI                                    
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY DIFFRACTION                  
REMARK   1  TITL 2 STUDIES OF HYDROXYPYRUVATE REDUCTASE (D-GLYCERATE            
REMARK   1  TITL 3 DEHYDROGENASE) FROM HYPHOMICROBIUM METHYLOVORUM              
REMARK   1  REF    J.MOL.BIOL.                   V. 225   909 1992              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4829                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 197                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.48                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  ONLY PARTIAL DNA SEQUENCE                
REMARK   3  INFORMATION IS AVAILABLE. THE DNA SEQUENCE CORRESPONDING TO         
REMARK   3  THE 130 N-TERMINAL RESIDUES IS KNOWN. FOR THE REMAINDER OF THE      
REMARK   3  POLYPEPTIDE, SIDE-CHAIN IDENTITIES HAVE BEEN INTERPRETED            
REMARK   3  DIRECTLY FROM ELECTRON DENSITY MAPS. THE POSSIBILITY OF THERE       
REMARK   3  BEING ADDITIONAL RESIDUES AT THE C-TERMINUS IS NOT DISCOUNTED.      
REMARK   4                                                                      
REMARK   4 1GDH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   2    CD   CE   NZ                                        
REMARK 470     LYS A   3    CD   CE   NZ                                        
REMARK 470     GLU A  41    CD   OE1  OE2                                       
REMARK 470     LYS A  44    CD   CE   NZ                                        
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     ARG A  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     GLU A  60    CD   OE1  OE2                                       
REMARK 470     ARG A  64    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  70    CD   CE   NZ                                        
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS B   2    CG   CD   CE   NZ                                   
REMARK 470     LYS B   3    CE   NZ                                             
REMARK 470     LYS B   4    CD   CE   NZ                                        
REMARK 470     ASP B  31    CG   OD1  OD2                                       
REMARK 470     LYS B  56    CG   CD   CE   NZ                                   
REMARK 470     LYS B  59    CG   CD   CE   NZ                                   
REMARK 470     ARG B  64    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     LYS B  93    CG   CD   CE   NZ                                   
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 218    CG   CD   NE   CZ   NH1  NH2                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP A   63   CG    OD1   OD2                                     
REMARK 480     GLU A   67   CG    CD    OE1   OE2                               
REMARK 480     ASN B  271   CG    OD1   ND2                                     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 296   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  31      -78.15    -31.24                                   
REMARK 500    LYS A  33      161.88    -42.75                                   
REMARK 500    GLU A  41      -71.70    -53.57                                   
REMARK 500    PHE A  79       39.86   -144.24                                   
REMARK 500    PHE A 155       59.30   -115.75                                   
REMARK 500    ALA A 239      -75.93    -92.95                                   
REMARK 500    ALA A 291       52.74    -63.80                                   
REMARK 500    PRO B  12      155.51    -46.54                                   
REMARK 500    ASP B  31      -95.52    -25.79                                   
REMARK 500    LYS B  33      165.74    -44.50                                   
REMARK 500    SER B  76      151.91    175.27                                   
REMARK 500    PHE B  79       26.19   -144.74                                   
REMARK 500    PHE B 155       49.44    -99.98                                   
REMARK 500    GLN B 190       42.82     37.41                                   
REMARK 500    ALA B 239      -86.68    -80.57                                   
REMARK 500    HIS B 287       74.48     50.62                                   
REMARK 500    ALA B 291       49.58    -93.06                                   
REMARK 500    TYR B 318       54.68   -118.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  18         0.08    SIDE_CHAIN                              
REMARK 500    ARG A 118         0.21    SIDE_CHAIN                              
REMARK 500    ARG A 119         0.13    SIDE_CHAIN                              
REMARK 500    ARG A 165         0.18    SIDE_CHAIN                              
REMARK 500    ARG A 180         0.14    SIDE_CHAIN                              
REMARK 500    TYR A 189         0.10    SIDE_CHAIN                              
REMARK 500    ARG A 240         0.08    SIDE_CHAIN                              
REMARK 500    ARG A 296         0.15    SIDE_CHAIN                              
REMARK 500    TYR A 318         0.11    SIDE_CHAIN                              
REMARK 500    ARG B  90         0.16    SIDE_CHAIN                              
REMARK 500    ARG B 165         0.19    SIDE_CHAIN                              
REMARK 500    TYR B 219         0.07    SIDE_CHAIN                              
REMARK 500    TYR B 318         0.13    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A 288        -11.49                                           
REMARK 500    ILE B 288        -10.02                                           
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 SO4 A 322                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 322                 
DBREF  1GDH A    2   321  UNP    P36234   DHGY_HYPME       2    321             
DBREF  1GDH B    2   321  UNP    P36234   DHGY_HYPME       2    321             
SEQRES   1 A  320  LYS LYS LYS ILE LEU ILE THR TRP PRO LEU PRO GLU ALA          
SEQRES   2 A  320  ALA MET ALA ARG ALA ARG GLU SER TYR ASP VAL ILE ALA          
SEQRES   3 A  320  HIS GLY ASP ASP PRO LYS ILE THR ILE ASP GLU MET ILE          
SEQRES   4 A  320  GLU THR ALA LYS SER VAL ASP ALA LEU LEU ILE THR LEU          
SEQRES   5 A  320  ASN GLU LYS CYS ARG LYS GLU VAL ILE ASP ARG ILE PRO          
SEQRES   6 A  320  GLU ASN ILE LYS CYS ILE SER THR TYR SER ILE GLY PHE          
SEQRES   7 A  320  ASP HIS ILE ASP LEU ASP ALA CYS LYS ALA ARG GLY ILE          
SEQRES   8 A  320  LYS VAL GLY ASN ALA PRO HIS GLY VAL THR VAL ALA THR          
SEQRES   9 A  320  ALA GLU ILE ALA MET LEU LEU LEU LEU GLY SER ALA ARG          
SEQRES  10 A  320  ARG ALA GLY GLU GLY GLU LYS MET ILE ARG THR ARG SER          
SEQRES  11 A  320  TRP PRO GLY TRP GLU PRO LEU GLU LEU VAL GLY GLU LYS          
SEQRES  12 A  320  LEU ASP ASN LYS THR LEU GLY ILE TYR GLY PHE GLY SER          
SEQRES  13 A  320  ILE GLY GLN ALA LEU ALA LYS ARG ALA GLN GLY PHE ASP          
SEQRES  14 A  320  MET ASP ILE ASP TYR PHE ASP THR HIS ARG ALA SER SER          
SEQRES  15 A  320  SER ASP GLU ALA SER TYR GLN ALA THR PHE HIS ASP SER          
SEQRES  16 A  320  LEU ASP SER LEU LEU SER VAL SER GLN PHE PHE SER LEU          
SEQRES  17 A  320  ASN ALA PRO SER THR PRO GLU THR ARG TYR PHE PHE ASN          
SEQRES  18 A  320  LYS ALA THR ILE LYS SER LEU PRO GLN GLY ALA ILE VAL          
SEQRES  19 A  320  VAL ASN THR ALA ARG GLY ASP LEU VAL ASP ASN GLU LEU          
SEQRES  20 A  320  VAL VAL ALA ALA LEU GLU ALA GLY ARG LEU ALA TYR ALA          
SEQRES  21 A  320  GLY PHE ASP VAL PHE ALA GLY GLU PRO ASN ILE ASN GLU          
SEQRES  22 A  320  GLY TYR TYR ASP LEU PRO ASN THR PHE LEU PHE PRO HIS          
SEQRES  23 A  320  ILE GLY SER ALA ALA THR GLN ALA ARG GLU ASP MET ALA          
SEQRES  24 A  320  HIS GLN ALA ASN ASP LEU ILE ASP ALA LEU PHE GLY GLY          
SEQRES  25 A  320  ALA ASP MET SER TYR ALA LEU ALA                              
SEQRES   1 B  320  LYS LYS LYS ILE LEU ILE THR TRP PRO LEU PRO GLU ALA          
SEQRES   2 B  320  ALA MET ALA ARG ALA ARG GLU SER TYR ASP VAL ILE ALA          
SEQRES   3 B  320  HIS GLY ASP ASP PRO LYS ILE THR ILE ASP GLU MET ILE          
SEQRES   4 B  320  GLU THR ALA LYS SER VAL ASP ALA LEU LEU ILE THR LEU          
SEQRES   5 B  320  ASN GLU LYS CYS ARG LYS GLU VAL ILE ASP ARG ILE PRO          
SEQRES   6 B  320  GLU ASN ILE LYS CYS ILE SER THR TYR SER ILE GLY PHE          
SEQRES   7 B  320  ASP HIS ILE ASP LEU ASP ALA CYS LYS ALA ARG GLY ILE          
SEQRES   8 B  320  LYS VAL GLY ASN ALA PRO HIS GLY VAL THR VAL ALA THR          
SEQRES   9 B  320  ALA GLU ILE ALA MET LEU LEU LEU LEU GLY SER ALA ARG          
SEQRES  10 B  320  ARG ALA GLY GLU GLY GLU LYS MET ILE ARG THR ARG SER          
SEQRES  11 B  320  TRP PRO GLY TRP GLU PRO LEU GLU LEU VAL GLY GLU LYS          
SEQRES  12 B  320  LEU ASP ASN LYS THR LEU GLY ILE TYR GLY PHE GLY SER          
SEQRES  13 B  320  ILE GLY GLN ALA LEU ALA LYS ARG ALA GLN GLY PHE ASP          
SEQRES  14 B  320  MET ASP ILE ASP TYR PHE ASP THR HIS ARG ALA SER SER          
SEQRES  15 B  320  SER ASP GLU ALA SER TYR GLN ALA THR PHE HIS ASP SER          
SEQRES  16 B  320  LEU ASP SER LEU LEU SER VAL SER GLN PHE PHE SER LEU          
SEQRES  17 B  320  ASN ALA PRO SER THR PRO GLU THR ARG TYR PHE PHE ASN          
SEQRES  18 B  320  LYS ALA THR ILE LYS SER LEU PRO GLN GLY ALA ILE VAL          
SEQRES  19 B  320  VAL ASN THR ALA ARG GLY ASP LEU VAL ASP ASN GLU LEU          
SEQRES  20 B  320  VAL VAL ALA ALA LEU GLU ALA GLY ARG LEU ALA TYR ALA          
SEQRES  21 B  320  GLY PHE ASP VAL PHE ALA GLY GLU PRO ASN ILE ASN GLU          
SEQRES  22 B  320  GLY TYR TYR ASP LEU PRO ASN THR PHE LEU PHE PRO HIS          
SEQRES  23 B  320  ILE GLY SER ALA ALA THR GLN ALA ARG GLU ASP MET ALA          
SEQRES  24 B  320  HIS GLN ALA ASN ASP LEU ILE ASP ALA LEU PHE GLY GLY          
SEQRES  25 B  320  ALA ASP MET SER TYR ALA LEU ALA                              
HET    SO4  A 322       5                                                       
HET    SO4  B 322       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *197(H2 O)                                                    
HELIX    1  A1 GLU A   13  SER A   22  1                                  10    
HELIX    2  A2 ILE A   36  ALA A   43  1                                   8    
HELIX    3  A3 LYS A   59  ARG A   64  1                                   6    
HELIX    4  A4 LEU A   84  ALA A   89  1                                   6    
HELIX    5  AA THR A  102  ALA A  117  1                                  16    
HELIX    6  A5 ALA A  120  ARG A  128  1                                   9    
HELIX    7  AB SER A  157  GLY A  168  1                                  12    
HELIX    8  AC SER A  183  SER A  188  1                                   6    
HELIX    9  A6 LEU A  197  SER A  202  1                                   6    
HELIX   10  AE LYS A  223  ILE A  226  1                                   4    
HELIX   11  AF ASN A  246  ALA A  255  1                                  10    
HELIX   12  A7 THR A  293  GLY A  312  1                                  20    
HELIX   13  B1 GLU B   13  SER B   22  1                                  10    
HELIX   14  B2 ILE B   36  ALA B   43  1                                   8    
HELIX   15  B3 LYS B   59  ARG B   64  1                                   6    
HELIX   16  B4 LEU B   84  ALA B   89  1                                   6    
HELIX   17  BA THR B  102  ALA B  117  1                                  16    
HELIX   18  B5 ALA B  120  ARG B  128  1                                   9    
HELIX   19  BB SER B  157  GLY B  168  1                                  12    
HELIX   20  BC SER B  183  SER B  188  1                                   6    
HELIX   21  B6 LEU B  197  SER B  202  1                                   6    
HELIX   22  BE LYS B  223  ILE B  226  1                                   4    
HELIX   23  BF ASN B  246  ALA B  255  1                                  10    
HELIX   24  B7 THR B  293  GLY B  312  1                                  20    
SHEET    1  AA 5 ASP A  24  ALA A  27  0                                        
SHEET    2  AA 5 LYS A   4  ILE A   7  1                                        
SHEET    3  AA 5 ALA A  48  THR A  52  1                                        
SHEET    4  AA 5 CYS A  71  TYR A  75  1                                        
SHEET    5  AA 5 LYS A  93  ASN A  96  1                                        
SHEET    1  AB 7 ALA A 191  PHE A 193  0                                        
SHEET    2  AB 7 ASP A 172  PHE A 176  1                                        
SHEET    3  AB 7 THR A 149  TYR A 153  1                                        
SHEET    4  AB 7 PHE A 206  LEU A 209  1                                        
SHEET    5  AB 7 ALA A 233  ASN A 237  1                                        
SHEET    6  AB 7 LEU A 258  PHE A 263  1                                        
SHEET    7  AB 7 THR A 282  LEU A 284  1                                        
SHEET    1  BA 5 ASP B  24  ALA B  27  0                                        
SHEET    2  BA 5 LYS B   4  ILE B   7  1                                        
SHEET    3  BA 5 ALA B  48  THR B  52  1                                        
SHEET    4  BA 5 CYS B  71  TYR B  75  1                                        
SHEET    5  BA 5 LYS B  93  ASN B  96  1                                        
SHEET    1  BB 7 ALA B 191  PHE B 193  0                                        
SHEET    2  BB 7 ASP B 172  PHE B 176  1                                        
SHEET    3  BB 7 THR B 149  TYR B 153  1                                        
SHEET    4  BB 7 PHE B 206  LEU B 209  1                                        
SHEET    5  BB 7 ALA B 233  ASN B 237  1                                        
SHEET    6  BB 7 LEU B 258  PHE B 263  1                                        
SHEET    7  BB 7 THR B 282  LEU B 284  1                                        
CISPEP   1 GLU A  269    PRO A  270          0        11.05                     
CISPEP   2 GLU B  269    PRO B  270          0        -2.16                     
SITE     1 AC1  3 GLY A 100  VAL A 101  THR A 102                               
SITE     1 AC2  6 HIS B  99  GLY B 100  VAL B 101  THR B 102                    
SITE     2 AC2  6 HOH B 354  HOH B 376                                          
CRYST1   60.410   60.530   66.290 102.30 113.73 102.73 P 1           2          
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      0.016554  0.003740  0.009074        0.00000                         
SCALE2      0.000000  0.016937  0.006080        0.00000                         
SCALE3      0.000000  0.000000  0.017508        0.00000                         
MTRIX1   1  0.350790 -0.491090  0.797360       17.05181    1                    
MTRIX2   1 -0.482810 -0.824420 -0.295350       72.93915    1                    
MTRIX3   1  0.802400 -0.281360 -0.526300       15.54483    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system