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Database: PDB
Entry: 1X0V
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HEADER    OXIDOREDUCTASE                          30-MAR-05   1X0V              
TITLE     CRYSTAL STRUCTURE OF HOMO SAPIEN GLYCEROL-3-PHOSPHATE                 
TITLE    2 DEHYDROGENASE 1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD+],                 
COMPND   3 CYTOPLASMIC;                                                         
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: GPD-C, GPDH-C;                                              
COMPND   6 EC: 1.1.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DE3(BL21);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    TWO INDEPENDENT DOMAINS, GXGXXG MOTIF, OXIDOREDUCTASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.RAO,X.OU                                                            
REVDAT   2   24-FEB-09 1X0V    1       VERSN                                    
REVDAT   1   11-APR-06 1X0V    0                                                
JRNL        AUTH   X.OU,C.JI,X.HAN,X.ZHAO,X.LI,Y.MAO,L.L.WONG,                  
JRNL        AUTH 2 M.BARTLAM,Z.RAO                                              
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN GLYCEROL 3-PHOSPHATE             
JRNL        TITL 2 DEHYDROGENASE 1 (GPD1)                                       
JRNL        REF    J.MOL.BIOL.                   V. 357   858 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16460752                                                     
JRNL        DOI    10.1016/J.JMB.2005.12.074                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
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             : 85858                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8447                            
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            : 5256                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 651                                     
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) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1X0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024238.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BSRF                               
REMARK 200  BEAMLINE                       : 3W1A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798, 0.9800, 0.900              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88158                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.3                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE DIHYDRATE,       
REMARK 280  0.5M AMMONIUM SULFATE, 1.0M LITHIUM SULFATE MONOHYDORATE, PH        
REMARK 280  5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.71800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       56.74400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       56.74400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      116.57700            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       56.74400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       56.74400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       38.85900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       56.74400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.74400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      116.57700            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       56.74400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.74400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       38.85900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       77.71800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 5850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      -56.74400            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000      -56.74400            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -38.85900            
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     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP B 103   C     GLN B 104   N       0.231                       
REMARK 500    ARG B 139   C     LEU B 140   N       0.243                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 128   N   -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    ASP B 103   CB  -  CA  -  C   ANGL. DEV. =  15.6 DEGREES          
REMARK 500    GLU B 138   CA  -  C   -  N   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    GLU B 138   O   -  C   -  N   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG B 139   C   -  N   -  CA  ANGL. DEV. =  21.6 DEGREES          
REMARK 500    ARG B 139   CA  -  C   -  N   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG B 139   O   -  C   -  N   ANGL. DEV. =  14.3 DEGREES          
REMARK 500    LEU B 147   CA  -  CB  -  CG  ANGL. DEV. =  14.4 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    SER A  11       27.24   -148.85                                   
REMARK 500    VAL A  92       58.15   -151.84                                   
REMARK 500    PRO A 126      100.00    -59.69                                   
REMARK 500    LEU A 291      -15.80   -145.82                                   
REMARK 500    SER B  11       30.28   -152.23                                   
REMARK 500    ASN B 127      -28.97    101.38                                   
REMARK 500    ASN B 293       18.83     40.76                                   
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    ASP B 103        -15.46                                           
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 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1005                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1006                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1008                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1009                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1010                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1011                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1012                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1013                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1014                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WPQ   RELATED DB: PDB                                   
REMARK 900 THE SAME PRTEIN COMPLEXED WITH NAD AND DIHYDROXYACETONE              
REMARK 900 RELATED ID: 1X0X   RELATED DB: PDB                                   
REMARK 900 THE SAME PRTEIN COMPLEXED WITH NAD                                   
DBREF  1X0V A    1   349  UNP    P21695   GPDA_HUMAN       1    348             
DBREF  1X0V B    1   349  UNP    P21695   GPDA_HUMAN       1    348             
SEQADV 1X0V GLY A   -4  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V PRO A   -3  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V LEU A   -2  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V GLY A   -1  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V SER A    0  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V MSE A    1  UNP  P21695    MET     1 MODIFIED RESIDUE               
SEQADV 1X0V MSE A   38  UNP  P21695    MET    37 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  144  UNP  P21695    MET   143 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  148  UNP  P21695    MET   147 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  181  UNP  P21695    MET   180 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  233  UNP  P21695    MET   232 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  235  UNP  P21695    MET   234 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  323  UNP  P21695    MET   322 MODIFIED RESIDUE               
SEQADV 1X0V MSE A  349  UNP  P21695    MET   348 MODIFIED RESIDUE               
SEQADV 1X0V GLY B   -4  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V PRO B   -3  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V LEU B   -2  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V GLY B   -1  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V SER B    0  UNP  P21695              CLONING ARTIFACT               
SEQADV 1X0V MSE B    1  UNP  P21695    MET     1 MODIFIED RESIDUE               
SEQADV 1X0V MSE B   38  UNP  P21695    MET    37 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  144  UNP  P21695    MET   143 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  148  UNP  P21695    MET   147 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  181  UNP  P21695    MET   180 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  233  UNP  P21695    MET   232 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  235  UNP  P21695    MET   234 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  323  UNP  P21695    MET   322 MODIFIED RESIDUE               
SEQADV 1X0V MSE B  349  UNP  P21695    MET   348 MODIFIED RESIDUE               
SEQRES   1 A  354  GLY PRO LEU GLY SER MSE ALA SER LYS LYS VAL CYS ILE          
SEQRES   2 A  354  VAL GLY SER GLY ASN TRP GLY SER ALA ILE ALA LYS ILE          
SEQRES   3 A  354  VAL GLY GLY ASN ALA ALA GLN LEU ALA GLN PHE ASP PRO          
SEQRES   4 A  354  ARG VAL THR MSE TRP VAL PHE GLU GLU ASP ILE GLY GLY          
SEQRES   5 A  354  LYS LYS LEU THR GLU ILE ILE ASN THR GLN HIS GLU ASN          
SEQRES   6 A  354  VAL LYS TYR LEU PRO GLY HIS LYS LEU PRO PRO ASN VAL          
SEQRES   7 A  354  VAL ALA VAL PRO ASP VAL VAL GLN ALA ALA GLU ASP ALA          
SEQRES   8 A  354  ASP ILE LEU ILE PHE VAL VAL PRO HIS GLN PHE ILE GLY          
SEQRES   9 A  354  LYS ILE CYS ASP GLN LEU LYS GLY HIS LEU LYS ALA ASN          
SEQRES  10 A  354  ALA THR GLY ILE SER LEU ILE LYS GLY VAL ASP GLU GLY          
SEQRES  11 A  354  PRO ASN GLY LEU LYS LEU ILE SER GLU VAL ILE GLY GLU          
SEQRES  12 A  354  ARG LEU GLY ILE PRO MSE SER VAL LEU MSE GLY ALA ASN          
SEQRES  13 A  354  ILE ALA SER GLU VAL ALA ASP GLU LYS PHE CYS GLU THR          
SEQRES  14 A  354  THR ILE GLY CYS LYS ASP PRO ALA GLN GLY GLN LEU LEU          
SEQRES  15 A  354  LYS GLU LEU MSE GLN THR PRO ASN PHE ARG ILE THR VAL          
SEQRES  16 A  354  VAL GLN GLU VAL ASP THR VAL GLU ILE CYS GLY ALA LEU          
SEQRES  17 A  354  LYS ASN VAL VAL ALA VAL GLY ALA GLY PHE CYS ASP GLY          
SEQRES  18 A  354  LEU GLY PHE GLY ASP ASN THR LYS ALA ALA VAL ILE ARG          
SEQRES  19 A  354  LEU GLY LEU MSE GLU MSE ILE ALA PHE ALA LYS LEU PHE          
SEQRES  20 A  354  CYS SER GLY PRO VAL SER SER ALA THR PHE LEU GLU SER          
SEQRES  21 A  354  CYS GLY VAL ALA ASP LEU ILE THR THR CYS TYR GLY GLY          
SEQRES  22 A  354  ARG ASN ARG LYS VAL ALA GLU ALA PHE ALA ARG THR GLY          
SEQRES  23 A  354  LYS SER ILE GLU GLN LEU GLU LYS GLU LEU LEU ASN GLY          
SEQRES  24 A  354  GLN LYS LEU GLN GLY PRO GLU THR ALA ARG GLU LEU TYR          
SEQRES  25 A  354  SER ILE LEU GLN HIS LYS GLY LEU VAL ASP LYS PHE PRO          
SEQRES  26 A  354  LEU PHE MSE ALA VAL TYR LYS VAL CYS TYR GLU GLY GLN          
SEQRES  27 A  354  PRO VAL GLY GLU PHE ILE HIS CYS LEU GLN ASN HIS PRO          
SEQRES  28 A  354  GLU HIS MSE                                                  
SEQRES   1 B  354  GLY PRO LEU GLY SER MSE ALA SER LYS LYS VAL CYS ILE          
SEQRES   2 B  354  VAL GLY SER GLY ASN TRP GLY SER ALA ILE ALA LYS ILE          
SEQRES   3 B  354  VAL GLY GLY ASN ALA ALA GLN LEU ALA GLN PHE ASP PRO          
SEQRES   4 B  354  ARG VAL THR MSE TRP VAL PHE GLU GLU ASP ILE GLY GLY          
SEQRES   5 B  354  LYS LYS LEU THR GLU ILE ILE ASN THR GLN HIS GLU ASN          
SEQRES   6 B  354  VAL LYS TYR LEU PRO GLY HIS LYS LEU PRO PRO ASN VAL          
SEQRES   7 B  354  VAL ALA VAL PRO ASP VAL VAL GLN ALA ALA GLU ASP ALA          
SEQRES   8 B  354  ASP ILE LEU ILE PHE VAL VAL PRO HIS GLN PHE ILE GLY          
SEQRES   9 B  354  LYS ILE CYS ASP GLN LEU LYS GLY HIS LEU LYS ALA ASN          
SEQRES  10 B  354  ALA THR GLY ILE SER LEU ILE LYS GLY VAL ASP GLU GLY          
SEQRES  11 B  354  PRO ASN GLY LEU LYS LEU ILE SER GLU VAL ILE GLY GLU          
SEQRES  12 B  354  ARG LEU GLY ILE PRO MSE SER VAL LEU MSE GLY ALA ASN          
SEQRES  13 B  354  ILE ALA SER GLU VAL ALA ASP GLU LYS PHE CYS GLU THR          
SEQRES  14 B  354  THR ILE GLY CYS LYS ASP PRO ALA GLN GLY GLN LEU LEU          
SEQRES  15 B  354  LYS GLU LEU MSE GLN THR PRO ASN PHE ARG ILE THR VAL          
SEQRES  16 B  354  VAL GLN GLU VAL ASP THR VAL GLU ILE CYS GLY ALA LEU          
SEQRES  17 B  354  LYS ASN VAL VAL ALA VAL GLY ALA GLY PHE CYS ASP GLY          
SEQRES  18 B  354  LEU GLY PHE GLY ASP ASN THR LYS ALA ALA VAL ILE ARG          
SEQRES  19 B  354  LEU GLY LEU MSE GLU MSE ILE ALA PHE ALA LYS LEU PHE          
SEQRES  20 B  354  CYS SER GLY PRO VAL SER SER ALA THR PHE LEU GLU SER          
SEQRES  21 B  354  CYS GLY VAL ALA ASP LEU ILE THR THR CYS TYR GLY GLY          
SEQRES  22 B  354  ARG ASN ARG LYS VAL ALA GLU ALA PHE ALA ARG THR GLY          
SEQRES  23 B  354  LYS SER ILE GLU GLN LEU GLU LYS GLU LEU LEU ASN GLY          
SEQRES  24 B  354  GLN LYS LEU GLN GLY PRO GLU THR ALA ARG GLU LEU TYR          
SEQRES  25 B  354  SER ILE LEU GLN HIS LYS GLY LEU VAL ASP LYS PHE PRO          
SEQRES  26 B  354  LEU PHE MSE ALA VAL TYR LYS VAL CYS TYR GLU GLY GLN          
SEQRES  27 B  354  PRO VAL GLY GLU PHE ILE HIS CYS LEU GLN ASN HIS PRO          
SEQRES  28 B  354  GLU HIS MSE                                                  
MODRES 1X0V MSE A   38  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  144  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  148  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  181  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  233  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  235  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  323  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE A  349  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B   38  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  144  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  148  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  181  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  233  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  235  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  323  MET  SELENOMETHIONINE                                   
MODRES 1X0V MSE B  349  MET  SELENOMETHIONINE                                   
HET    MSE  A  38       8                                                       
HET    MSE  A 144       8                                                       
HET    MSE  A 148       8                                                       
HET    MSE  A 181       8                                                       
HET    MSE  A 233       8                                                       
HET    MSE  A 235       8                                                       
HET    MSE  A 323       8                                                       
HET    MSE  A 349       9                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  38       8                                                       
HET    MSE  B 144       8                                                       
HET    MSE  B 148       8                                                       
HET    MSE  B 181       8                                                       
HET    MSE  B 233       8                                                       
HET    MSE  B 235       8                                                       
HET    MSE  B 323       8                                                       
HET    MSE  B 349       9                                                       
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  A1004       5                                                       
HET    SO4  B1005       5                                                       
HET    SO4  B1006       5                                                       
HET    SO4  A1007       5                                                       
HET    SO4  B1008       5                                                       
HET    SO4  A1009       5                                                       
HET    SO4  B1010       5                                                       
HET    SO4  B1011       5                                                       
HET    SO4  A1012       5                                                       
HET    SO4  A1013       5                                                       
HET    SO4  B1014       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    17(C5 H11 N O2 SE)                                           
FORMUL   3  SO4    14(O4 S 2-)                                                  
FORMUL  17  HOH   *651(H2 O)                                                    
HELIX    1   1 GLY A   12  LEU A   29  1                                  18    
HELIX    2   2 LYS A   49  HIS A   58  1                                  10    
HELIX    3   3 ASP A   78  GLU A   84  1                                   7    
HELIX    4   4 PRO A   94  GLN A   96  5                                   3    
HELIX    5   5 PHE A   97  LYS A  106  1                                  10    
HELIX    6   6 LEU A  131  GLY A  141  1                                  11    
HELIX    7   7 ILE A  152  ASP A  158  1                                   7    
HELIX    8   8 ASP A  170  GLN A  182  1                                  13    
HELIX    9   9 GLU A  193  LEU A  217  1                                  25    
HELIX   10  10 GLY A  220  CYS A  243  1                                  24    
HELIX   11  11 SER A  248  GLU A  254  5                                   7    
HELIX   12  12 GLY A  257  GLY A  268  1                                  12    
HELIX   13  13 GLY A  268  GLY A  281  1                                  14    
HELIX   14  14 SER A  283  LEU A  292  1                                  10    
HELIX   15  15 LEU A  297  GLY A  314  1                                  18    
HELIX   16  16 LEU A  315  LYS A  318  5                                   4    
HELIX   17  17 PHE A  319  GLU A  331  1                                  13    
HELIX   18  18 PRO A  334  GLU A  337  5                                   4    
HELIX   19  19 PHE A  338  ASN A  344  1                                   7    
HELIX   20  20 GLY B   12  LEU B   29  1                                  18    
HELIX   21  21 LEU B   50  HIS B   58  1                                   9    
HELIX   22  22 ASP B   78  GLU B   84  1                                   7    
HELIX   23  23 PRO B   94  GLN B   96  5                                   3    
HELIX   24  24 PHE B   97  LYS B  106  1                                  10    
HELIX   25  25 LEU B  131  GLY B  141  1                                  11    
HELIX   26  26 ILE B  152  ASP B  158  1                                   7    
HELIX   27  27 ASP B  170  GLN B  182  1                                  13    
HELIX   28  28 GLU B  193  LEU B  217  1                                  25    
HELIX   29  29 GLY B  220  CYS B  243  1                                  24    
HELIX   30  30 SER B  248  GLU B  254  5                                   7    
HELIX   31  31 GLY B  257  GLY B  268  1                                  12    
HELIX   32  32 GLY B  268  GLY B  281  1                                  14    
HELIX   33  33 SER B  283  LEU B  292  1                                  10    
HELIX   34  34 LEU B  297  GLY B  314  1                                  18    
HELIX   35  35 LEU B  315  LYS B  318  5                                   4    
HELIX   36  36 PHE B  319  GLU B  331  1                                  13    
HELIX   37  37 PRO B  334  PHE B  338  5                                   5    
HELIX   38  38 ILE B  339  ASN B  344  1                                   6    
SHEET    1   A 8 VAL A  73  VAL A  76  0                                        
SHEET    2   A 8 PHE A  32  TRP A  39  1  N  MSE A  38   O  VAL A  74           
SHEET    3   A 8 LYS A   4  VAL A   9  1  N  ILE A   8   O  THR A  37           
SHEET    4   A 8 ILE A  88  PHE A  91  1  O  ILE A  90   N  VAL A   9           
SHEET    5   A 8 THR A 114  SER A 117  1  O  ILE A 116   N  PHE A  91           
SHEET    6   A 8 MSE A 144  MSE A 148  1  O  SER A 145   N  SER A 117           
SHEET    7   A 8 CYS A 162  GLY A 167 -1  O  GLY A 167   N  VAL A 146           
SHEET    8   A 8 PHE A 186  VAL A 191  1  O  VAL A 191   N  ILE A 166           
SHEET    1   B 8 VAL B  73  VAL B  76  0                                        
SHEET    2   B 8 PHE B  32  TRP B  39  1  N  MSE B  38   O  VAL B  76           
SHEET    3   B 8 LYS B   4  VAL B   9  1  N  ILE B   8   O  THR B  37           
SHEET    4   B 8 ILE B  88  PHE B  91  1  O  ILE B  90   N  CYS B   7           
SHEET    5   B 8 THR B 114  SER B 117  1  O  ILE B 116   N  PHE B  91           
SHEET    6   B 8 MSE B 144  MSE B 148  1  O  SER B 145   N  SER B 117           
SHEET    7   B 8 CYS B 162  GLY B 167 -1  O  THR B 165   N  MSE B 148           
SHEET    8   B 8 PHE B 186  VAL B 191  1  O  VAL B 191   N  ILE B 166           
SHEET    1   C 2 ASP B  44  ILE B  45  0                                        
SHEET    2   C 2 LYS B  48  LYS B  49 -1  O  LYS B  48   N  ILE B  45           
LINK         C   THR A  37                 N   MSE A  38     1555   1555  1.32  
LINK         C   MSE A  38                 N   TRP A  39     1555   1555  1.33  
LINK         C   PRO A 143                 N   MSE A 144     1555   1555  1.34  
LINK         C   MSE A 144                 N   SER A 145     1555   1555  1.34  
LINK         C   LEU A 147                 N   MSE A 148     1555   1555  1.33  
LINK         C   MSE A 148                 N   GLY A 149     1555   1555  1.33  
LINK         C   LEU A 180                 N   MSE A 181     1555   1555  1.34  
LINK         C   MSE A 181                 N   GLN A 182     1555   1555  1.32  
LINK         C   LEU A 232                 N   MSE A 233     1555   1555  1.33  
LINK         C   MSE A 233                 N   GLU A 234     1555   1555  1.33  
LINK         C   GLU A 234                 N   MSE A 235     1555   1555  1.34  
LINK         C   MSE A 235                 N   ILE A 236     1555   1555  1.34  
LINK         C   PHE A 322                 N   MSE A 323     1555   1555  1.33  
LINK         C   MSE A 323                 N   ALA A 324     1555   1555  1.34  
LINK         C   HIS A 348                 N   MSE A 349     1555   1555  1.33  
LINK         C   MSE B   1                 N   ALA B   2     1555   1555  1.33  
LINK         C   THR B  37                 N   MSE B  38     1555   1555  1.33  
LINK         C   MSE B  38                 N   TRP B  39     1555   1555  1.33  
LINK         C   PRO B 143                 N   MSE B 144     1555   1555  1.34  
LINK         C   MSE B 144                 N   SER B 145     1555   1555  1.33  
LINK         C   LEU B 147                 N   MSE B 148     1555   1555  1.33  
LINK         C   MSE B 148                 N   GLY B 149     1555   1555  1.33  
LINK         C   LEU B 180                 N   MSE B 181     1555   1555  1.33  
LINK         C   MSE B 181                 N   GLN B 182     1555   1555  1.33  
LINK         C   LEU B 232                 N   MSE B 233     1555   1555  1.33  
LINK         C   MSE B 233                 N   GLU B 234     1555   1555  1.33  
LINK         C   GLU B 234                 N   MSE B 235     1555   1555  1.33  
LINK         C   MSE B 235                 N   ILE B 236     1555   1555  1.33  
LINK         C   PHE B 322                 N   MSE B 323     1555   1555  1.33  
LINK         C   MSE B 323                 N   ALA B 324     1555   1555  1.33  
LINK         C   HIS B 348                 N   MSE B 349     1555   1555  1.33  
SITE     1 AC1  4 LYS A  20  HIS A  67  LYS A  68  HOH A1245                    
SITE     1 AC2  2 LYS B  68  SO4 B1010                                          
SITE     1 AC3  5 ASN A  13  TRP A  14  ARG A 269  HOH A1058                    
SITE     2 AC3  5 HOH A1173                                                     
SITE     1 AC4  5 ARG A 271  HOH A1073  HOH A1222  HOH A1290                    
SITE     2 AC4  5 HOH A1327                                                     
SITE     1 AC5  7 GLY B  12  ASN B  13  TRP B  14  HOH B1035                    
SITE     2 AC5  7 HOH B1168  HOH B1178  HOH B1295                               
SITE     1 AC6 10 LYS B 204  THR B 264  GLY B 268  ARG B 269                    
SITE     2 AC6 10 ASN B 270  HOH B1028  HOH B1038  HOH B1088                    
SITE     3 AC6 10 HOH B1119  HOH B1315                                          
SITE     1 AC7  6 LYS A 178  GLN A 182  ARG A 187  HOH A1049                    
SITE     2 AC7  6 HOH A1115  HOH A1314                                          
SITE     1 AC8  4 PRO B 346  GLU B 347  HIS B 348  HOH B1235                    
SITE     1 AC9 11 LYS A 204  ASN A 205  THR A 264  GLY A 268                    
SITE     2 AC9 11 ARG A 269  ASN A 270  GLN A 298  HOH A1028                    
SITE     3 AC9 11 HOH A1043  HOH A1153  HOH A1165                               
SITE     1 BC1  4 SO4 A1002  LYS B  20  GLY B  66  HIS B  67                    
SITE     1 BC2  4 LYS B 240  SER B 248  SER B 249  HOH B1258                    
SITE     1 BC3  4 LYS A 240  SER A 248  SER A 249  HOH A1114                    
SITE     1 BC4  4 PRO A 346  GLU A 347  HIS A 348  HOH A1307                    
SITE     1 BC5  4 LYS B 178  GLN B 182  ARG B 187  HOH B1146                    
CRYST1  113.488  113.488  155.436  90.00  90.00  90.00 P 43 21 2    16          
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      0.008812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006434        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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