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Database: PDB
Entry: 1J49
LinkDB: 1J49
Original site: 1J49 
HEADER    OXIDOREDUCTASE                          14-AUG-01   1J49              
TITLE     INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND               
TITLE    2 CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS              
TITLE    3 BULGARICUS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-LACTATE DEHYDROGENASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-LDH;                                                      
COMPND   5 EC: 1.1.1.28;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS DELBRUECKII SUBSP.                
SOURCE   3 BULGARICUS;                                                          
SOURCE   4 ORGANISM_TAXID: 1585;                                                
SOURCE   5 STRAIN: N42;                                                         
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   7 GENE: LDHA;                                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: SURE;                                      
SOURCE  11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PKBULDH;                                  
SOURCE  14 EXPRESSION_SYSTEM_GENE: LDHA;                                        
SOURCE  15 OTHER_DETAILS: NESTLE CULTURE COLLECTION. PCR AMPLIFIED              
SOURCE  16 LDHA GENE                                                            
KEYWDS    NAD-DEPENDENT DEHYDROGENASE, LAST STEP OF GLYCOLYSIS UNDER            
KEYWDS   2 ANAEROBIC CONDITIONS, REVERSIBLE INTERCONVERSION OF                  
KEYWDS   3 PYRUVATE INTO D-LACTATE, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.RAZETO,S.KOCHHAR,H.HOTTINGER,M.DAUTER,K.S.WILSON,                   
AUTHOR   2 V.S.LAMZIN                                                           
REVDAT   3   24-FEB-09 1J49    1       VERSN                                    
REVDAT   2   09-OCT-02 1J49    1       REMARK CRYST1 SCALE1 SCALE2              
REVDAT   2 2                   1       SCALE3 MASTER                            
REVDAT   1   29-MAY-02 1J49    0                                                
JRNL        AUTH   A.RAZETO,S.KOCHHAR,H.HOTTINGER,M.DAUTER,K.S.WILSON,          
JRNL        AUTH 2 V.S.LAMZIN                                                   
JRNL        TITL   DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND                    
JRNL        TITL 2 CATALYSIS OF D-LACTATE DEHYDROGENASE FROM                    
JRNL        TITL 3 LACTOBACILLUS BULGARICUS.                                    
JRNL        REF    J.MOL.BIOL.                   V. 318   109 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12054772                                                     
JRNL        DOI    10.1016/S0022-2836(02)00086-4                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 37544                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT (EXCEPT FOR THE      
REMARK   3                                      LAST 2 REFINEMENT CYCLES)       
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1884                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5207                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 93                                      
REMARK   3   SOLVENT ATOMS            : 279                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.40                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.270         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.350         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; 0.015               
REMARK   3    ANGLE DISTANCE                  (A) : 0.025 ; 0.020               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.033 ; 0.030               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.026 ; 0.030               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.030 ; 0.050               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.200 ; 0.200               
REMARK   3    MULTIPLE TORSION                (A) : 0.300 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.230 ; 1.000               
REMARK   3    H-BOND (X-H...Y)                (A) : 0.230 ; 1.000               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : 0.000 ; 15.000              
REMARK   3    PLANAR                    (DEGREES) : 4.300 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 18.800; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 35.600; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.800 ; 1.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.500 ; 1.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.800 ; 1.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.400 ; 1.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1J49 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB001593.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-94                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.916                              
REMARK 200  MONOCHROMATOR                  : SILICON CRYSTAL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.82                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.730                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2DLD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0                                   
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      114.25000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.70000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      171.37500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.70000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.12500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.70000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.70000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      171.37500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.70000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.70000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       57.12500            
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      114.25000            
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: 8250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 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   333                                                      
REMARK 465     GLY B   333                                                      
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     ASN A  69    CG   OD1  ND2                                       
REMARK 470     LYS A 331    CG   CD   CE   NZ                                   
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     GLU A   39   CD    OE1   OE2                                     
REMARK 480     GLN A   55   CD    OE1   NE2                                     
REMARK 480     ASP A  122   CG    OD1   OD2                                     
REMARK 480     GLN A  163   CD    OE1   NE2                                     
REMARK 480     THR A  174   OG1   CG2                                           
REMARK 480     GLU A  220   CG    CD    OE1   OE2                               
REMARK 480     ARG A  236   NE    CZ    NH1   NH2                               
REMARK 480     GLU A  277   CD    OE1   OE2                                     
REMARK 480     LYS A  312   CE    NZ                                            
REMARK 480     LYS A  324   CE    NZ                                            
REMARK 480     GLU A  325   CD    OE1   OE2                                     
REMARK 480     LYS B   14   NZ                                                  
REMARK 480     GLU B   61   CD    OE1   OE2                                     
REMARK 480     ASP B  122   CG    OD1   OD2                                     
REMARK 480     GLN B  163   CD    OE1   NE2                                     
REMARK 480     THR B  174   OG1   CG2                                           
REMARK 480     LYS B  198   CD    CE    NZ                                      
REMARK 480     GLU B  220   CD    OE1   OE2                                     
REMARK 480     LYS B  224   NZ                                                  
REMARK 480     ILE B  254   CD1                                                 
REMARK 480     GLU B  277   CD    OE1   OE2                                     
REMARK 480     GLU B  325   CD    OE1   OE2                                     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B   122     O    HOH B   370              1.23            
REMARK 500   OD1  ASP B   122     O    HOH B   385              1.37            
REMARK 500   CE   LYS B     3     O    HOH B   481              1.54            
REMARK 500   CG   ASP B   122     O    HOH B   370              1.83            
REMARK 500   OD1  ASP A   122     O    HOH A   353              1.83            
REMARK 500   OE1  GLU B    28     O    HOH B   481              2.07            
REMARK 500   CE   MET A   309     O    HOH A   395              2.12            
REMARK 500   OG1  THR B   139     O    HOH B   449              2.16            
REMARK 500   OD1  ASP A    48     O    HOH A   460              2.17            
REMARK 500   OE2  GLU A    19     NH2  ARG A   307              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   MET A     1     O    GLY A   169     7546     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    THR A 174   CB    THR A 174   OG1     0.135                       
REMARK 500    ARG A 236   CD    ARG A 236   NE     -0.112                       
REMARK 500    GLU A 277   CG    GLU A 277   CD     -0.135                       
REMARK 500    LYS B  14   CE    LYS B  14   NZ     -0.167                       
REMARK 500    GLU B  61   CG    GLU B  61   CD     -0.170                       
REMARK 500    ASP B 122   CB    ASP B 122   CG      0.230                       
REMARK 500    THR B 174   CB    THR B 174   OG1    -0.130                       
REMARK 500    GLU B 220   CG    GLU B 220   CD     -0.181                       
REMARK 500    GLU B 277   CG    GLU B 277   CD     -0.159                       
REMARK 500    GLU B 325   CG    GLU B 325   CD     -0.113                       
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    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 135   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 135   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 142   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 236   CG  -  CD  -  NE  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG A 236   CD  -  NE  -  CZ  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ASP A 280   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 289   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B  77   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG B 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP B 133   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG B 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    GLU B 263   OE1 -  CD  -  OE2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    GLU B 274   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ARG B 307   CD  -  NE  -  CZ  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG B 307   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    GLU B 325   CG  -  CD  -  OE1 ANGL. DEV. =  12.9 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    THR A   2       70.73     70.15                                   
REMARK 500    HIS A  24       54.99   -147.71                                   
REMARK 500    PRO A  38      -19.77    -49.08                                   
REMARK 500    TYR A  53      107.82   -165.86                                   
REMARK 500    GLN A  54      148.77   -175.59                                   
REMARK 500    ASP A  57      154.26    -37.69                                   
REMARK 500    ASN A  78     -164.58   -123.17                                   
REMARK 500    ASP A  85       92.34    -54.18                                   
REMARK 500    SER A 103       97.02   -169.26                                   
REMARK 500    HIS A 132       33.15     74.36                                   
REMARK 500    THR A 139       61.97    -68.70                                   
REMARK 500    ASP A 209       37.98    -71.64                                   
REMARK 500    SER A 235      -80.66    -88.66                                   
REMARK 500    ASN A 270       31.64     71.07                                   
REMARK 500    LYS A 331      108.98    -57.77                                   
REMARK 500    THR B   2       98.16    -50.07                                   
REMARK 500    HIS B  24       57.63   -146.44                                   
REMARK 500    LYS B  45      122.18    -29.39                                   
REMARK 500    TYR B  53      112.08   -164.80                                   
REMARK 500    ASP B  68       27.45    -58.72                                   
REMARK 500    ASN B  69        7.01   -154.84                                   
REMARK 500    SER B 103       83.27    179.21                                   
REMARK 500    HIS B 132       20.65     84.02                                   
REMARK 500    THR B 154       46.03   -106.77                                   
REMARK 500    SER B 235      -73.58    -90.38                                   
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    THR B   2         11.11                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 480        DISTANCE =  8.64 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 341                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 350                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 360                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHORS MAINTAIN THAT THEIR SEQUENCE IS                          
REMARK 999 CORRECT. THE DENSITY FOR THESE RESIDUES SUGGESTS                     
REMARK 999 ILE59, ARG117, AND VAL152 INSTEAD OF THOSE IN                        
REMARK 999 THE DATABASE REFERENCE MATCH.                                        
DBREF  1J49 A    1   333  UNP    P26297   LDHD_LACDE       1    333             
DBREF  1J49 B    1   333  UNP    P26297   LDHD_LACDE       1    333             
SEQADV 1J49 ILE A   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J49 ARG A  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J49 VAL A  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQADV 1J49 ILE B   59  UNP  P26297    THR    59 SEE REMARK 999                 
SEQADV 1J49 ARG B  117  UNP  P26297    ALA   117 SEE REMARK 999                 
SEQADV 1J49 VAL B  152  UNP  P26297    ILE   152 SEE REMARK 999                 
SEQRES   1 A  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 A  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 A  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 A  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 A  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 A  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 A  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 A  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 A  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 A  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 A  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 A  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 A  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 A  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 A  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 A  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 A  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 A  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 A  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 A  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 A  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 A  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 A  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO HIS THR ALA          
SEQRES  24 A  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 A  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 A  333  ALA GLU THR PRO VAL LYS VAL GLY                              
SEQRES   1 B  333  MET THR LYS ILE PHE ALA TYR ALA ILE ARG GLU ASP GLU          
SEQRES   2 B  333  LYS PRO PHE LEU LYS GLU TRP GLU ASP ALA HIS LYS ASP          
SEQRES   3 B  333  VAL GLU VAL GLU TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 B  333  THR VAL ALA LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 B  333  TYR GLN GLN LEU ASP TYR ILE ALA GLU THR LEU GLN ALA          
SEQRES   6 B  333  LEU ALA ASP ASN GLY ILE THR LYS MET SER LEU ARG ASN          
SEQRES   7 B  333  VAL GLY VAL ASP ASN ILE ASP MET ALA LYS ALA LYS GLU          
SEQRES   8 B  333  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 B  333  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 B  333  ILE LEU ARG GLN ASP LYS ALA MET ASP GLU LYS VAL ALA          
SEQRES  11 B  333  ARG HIS ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 B  333  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 B  333  ILE GLY GLN VAL PHE MET GLN ILE MET GLU GLY PHE GLY          
SEQRES  14 B  333  ALA LYS VAL ILE THR TYR ASP ILE PHE ARG ASN PRO GLU          
SEQRES  15 B  333  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 B  333  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 B  333  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP GLU SER          
SEQRES  18 B  333  ILE ALA LYS MET LYS GLN ASP VAL VAL ILE VAL ASN VAL          
SEQRES  19 B  333  SER ARG GLY PRO LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 B  333  GLY LEU ASP SER GLY LYS ILE PHE GLY TYR ALA MET ASP          
SEQRES  21 B  333  VAL TYR GLU GLY GLU VAL GLY ILE PHE ASN GLU ASP TRP          
SEQRES  22 B  333  GLU GLY LYS GLU PHE PRO ASP ALA ARG LEU ALA ASP LEU          
SEQRES  23 B  333  ILE ALA ARG PRO ASN VAL LEU VAL THR PRO HIS THR ALA          
SEQRES  24 B  333  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 B  333  ALA PHE ASP ASN ASN LEU GLU LEU VAL GLU GLY LYS GLU          
SEQRES  26 B  333  ALA GLU THR PRO VAL LYS VAL GLY                              
HET    SO4  B 341       5                                                       
HET    NAD  A 350      44                                                       
HET    NAD  B 360      44                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   6  HOH   *279(H2 O)                                                    
HELIX    1   1 ARG A   10  ASP A   12  5                                   3    
HELIX    2   2 GLU A   13  ALA A   23  1                                  11    
HELIX    3   3 THR A   40  LYS A   45  5                                   6    
HELIX    4   4 ILE A   59  ASP A   68  1                                  10    
HELIX    5   5 ASP A   85  GLY A   93  1                                   9    
HELIX    6   6 SER A  103  ARG A  120  1                                  18    
HELIX    7   7 GLN A  121  ARG A  131  1                                  11    
HELIX    8   8 GLU A  143  ASP A  146  5                                   4    
HELIX    9   9 GLY A  155  PHE A  168  1                                  14    
HELIX   10  10 ASN A  180  GLY A  187  1                                   8    
HELIX   11  11 SER A  192  ALA A  200  1                                   9    
HELIX   12  12 ASN A  218  MET A  225  1                                   8    
HELIX   13  13 ARG A  236  VAL A  240  5                                   5    
HELIX   14  14 ASP A  241  SER A  251  1                                  11    
HELIX   15  15 ASP A  280  ARG A  289  1                                  10    
HELIX   16  16 THR A  302  GLU A  322  1                                  21    
HELIX   17  17 ARG B   10  ASP B   12  5                                   3    
HELIX   18  18 GLU B   13  ASP B   22  1                                  10    
HELIX   19  19 THR B   37  ALA B   42  1                                   6    
HELIX   20  20 LEU B   43  LYS B   45  5                                   3    
HELIX   21  21 ILE B   59  ASP B   68  1                                  10    
HELIX   22  22 ASP B   85  LEU B   92  1                                   8    
HELIX   23  23 SER B  103  GLN B  121  1                                  19    
HELIX   24  24 GLN B  121  ARG B  131  1                                  11    
HELIX   25  25 GLU B  143  ASP B  146  5                                   4    
HELIX   26  26 GLY B  155  PHE B  168  1                                  14    
HELIX   27  27 ASN B  180  GLY B  187  1                                   8    
HELIX   28  28 SER B  192  ALA B  200  1                                   9    
HELIX   29  29 VAL B  210  VAL B  214  5                                   5    
HELIX   30  30 ASN B  218  LYS B  224  1                                   7    
HELIX   31  31 ARG B  236  VAL B  240  5                                   5    
HELIX   32  32 ASP B  241  SER B  251  1                                  11    
HELIX   33  33 ASP B  280  ARG B  289  1                                  10    
HELIX   34  34 THR B  302  GLU B  322  1                                  21    
SHEET    1   A 5 GLU A  28  TYR A  31  0                                        
SHEET    2   A 5 LYS A   3  ALA A   6  1  N  ILE A   4   O  GLU A  30           
SHEET    3   A 5 GLY A  49  VAL A  52  1  O  GLY A  49   N  PHE A   5           
SHEET    4   A 5 LYS A  73  LEU A  76  1  O  SER A  75   N  VAL A  52           
SHEET    5   A 5 GLN A  95  THR A  97  1  O  THR A  97   N  MET A  74           
SHEET    1   B 6 LYS A 171  TYR A 175  0                                        
SHEET    2   B 6 VAL A 148  VAL A 152  1  N  VAL A 149   O  LYS A 171           
SHEET    3   B 6 VAL A 202  LEU A 205  1  O  VAL A 202   N  GLY A 150           
SHEET    4   B 6 VAL A 229  ASN A 233  1  O  VAL A 232   N  ILE A 203           
SHEET    5   B 6 ILE A 254  MET A 259  1  O  PHE A 255   N  VAL A 229           
SHEET    6   B 6 VAL A 292  VAL A 294  1  O  LEU A 293   N  MET A 259           
SHEET    1   C 5 GLU B  28  TYR B  31  0                                        
SHEET    2   C 5 LYS B   3  ALA B   6  1  N  ALA B   6   O  GLU B  30           
SHEET    3   C 5 GLY B  49  VAL B  52  1  O  VAL B  51   N  PHE B   5           
SHEET    4   C 5 LYS B  73  LEU B  76  1  O  SER B  75   N  VAL B  52           
SHEET    5   C 5 GLN B  95  THR B  97  1  O  GLN B  95   N  MET B  74           
SHEET    1   D 6 LYS B 171  TYR B 175  0                                        
SHEET    2   D 6 VAL B 148  VAL B 152  1  N  VAL B 149   O  LYS B 171           
SHEET    3   D 6 VAL B 202  LEU B 205  1  O  VAL B 202   N  GLY B 150           
SHEET    4   D 6 VAL B 229  ASN B 233  1  O  VAL B 232   N  ILE B 203           
SHEET    5   D 6 ILE B 254  MET B 259  1  O  ALA B 258   N  ASN B 233           
SHEET    6   D 6 VAL B 292  VAL B 294  1  O  LEU B 293   N  MET B 259           
CISPEP   1 ALA A  137    PRO A  138          0        -0.66                     
CISPEP   2 ALA B  137    PRO B  138          0        -0.45                     
SITE     1 AC1  8 ASN B  78  VAL B  79  GLY B  80  TYR B 102                    
SITE     2 AC1  8 ARG B 236  HIS B 297  NAD B 360  HOH B 422                    
SITE     1 AC2 26 TYR A 102  ILE A 107  GLY A 153  GLY A 155                    
SITE     2 AC2 26 HIS A 156  ILE A 157  TYR A 175  ASP A 176                    
SITE     3 AC2 26 ILE A 177  HIS A 206  VAL A 207  PRO A 208                    
SITE     4 AC2 26 ASN A 213  VAL A 234  SER A 235  ARG A 236                    
SITE     5 AC2 26 ASP A 260  HIS A 297  ALA A 299  PHE A 300                    
SITE     6 AC2 26 HOH A 390  HOH A 428  HOH A 463  HOH A 470                    
SITE     7 AC2 26 HOH A 485  HOH A 487                                          
SITE     1 AC3 26 TYR B 102  ILE B 107  GLY B 155  HIS B 156                    
SITE     2 AC3 26 ILE B 157  TYR B 175  ASP B 176  ILE B 177                    
SITE     3 AC3 26 HIS B 206  VAL B 207  PRO B 208  ASN B 213                    
SITE     4 AC3 26 VAL B 234  SER B 235  ARG B 236  ASP B 260                    
SITE     5 AC3 26 HIS B 297  ALA B 299  PHE B 300  SO4 B 341                    
SITE     6 AC3 26 HOH B 376  HOH B 379  HOH B 382  HOH B 386                    
SITE     7 AC3 26 HOH B 395  HOH B 453                                          
CRYST1   79.400   79.400  228.500  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      0.012594  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012594  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004376        0.00000                         
MTRIX1   1 -0.310730 -0.062030  0.948470       -1.19188    1                    
MTRIX2   1  0.096710 -0.994750 -0.033370       54.58400    1                    
MTRIX3   1  0.945570  0.081360  0.315100       -0.08465    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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