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Database: PDB
Entry: 2DLD
LinkDB: 2DLD
Original site: 2DLD 
HEADER    OXIDOREDUCTASE (CHOH(D)-NAD+(A))        28-OCT-95   2DLD              
TITLE     D-LACTATE DEHYDROGENASE COMPLEXED WITH NADH AND OXAMATE               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-LACTATE DEHYDROGENASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: R-LACTATE DEHYDROGENASE;                                    
COMPND   5 EC: 1.1.1.28;                                                        
COMPND   6 OTHER_DETAILS: CRYSTALLIZED IN 11% PEG 4000, 5 MM BIS-TRIS PH 6.8, 75
COMPND   7 MG/ML ENZYME, 3 MM NADH, 10 MM OXAMATE                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS HELVETICUS;                       
SOURCE   3 ORGANISM_TAXID: 1587                                                 
KEYWDS    OXIDOREDUCTASE (CHOH(D)-NAD+(A))                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.DUNN,J.J.HOLBROOK                                                 
REVDAT   3   06-NOV-13 2DLD    1       HETATM HETNAM REMARK                     
REVDAT   2   24-FEB-09 2DLD    1       VERSN                                    
REVDAT   1   14-MAR-96 2DLD    0                                                
JRNL        AUTH   N.BERNARD,J.DELCOUR,A.ALVAREZ,A.CORTES,C.WILLIS,J.J.HOLBROOK 
JRNL        TITL   DEHYDROGENASES ENGINEERING TO CORRECT SUBSTRATE INHIBITION   
JRNL        TITL 2 IN A COMMERCIAL DEHYDROGENASE                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16190                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5316                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.00                          
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.020 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.029 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.049 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.019 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.160 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.250 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.360 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.330 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.600 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 27.000; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.800 ; 2.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 3.100 ; 2.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 2.400 ; 2.500               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 3.900 ; 3.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DLD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18315                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.8                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.05000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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   OG1  THR A    37     OG1  THR A    40              1.69            
REMARK 500   OD1  ASP B    48     NZ   LYS B    73              1.80            
REMARK 500   ND2  ASN B   316     O    ASP B   327              1.85            
REMARK 500   OG   SER B    75     OG1  THR B    97              1.87            
REMARK 500   NE2  GLN B    54     O    LEU B    56              1.97            
REMARK 500   O    ASN A    18     N    GLU A    22              1.98            
REMARK 500   O    ASP B    87     N    GLU B    91              2.06            
REMARK 500   NE2  HIS B   297     O1   OXM B   402              2.12            
REMARK 500   O    GLY A   267     NZ   LYS A   271              2.12            
REMARK 500   OD2  ASP A   285     NH1  ARG A   289              2.12            
REMARK 500   NE2  HIS A   297     O1   OXM A   402              2.14            
REMARK 500   NZ   LYS A   319     OE1  GLU A   324              2.14            
REMARK 500   OD2  ASP B   219     NH1  ARG B   247              2.16            
REMARK 500   O    LYS B    88     N    LEU B    92              2.17            
REMARK 500   OD1  ASP A   219     NH1  ARG A   247              2.19            
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    LYS A  25   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO A 100   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 122   CB  -  CG  -  OD1 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    MET A 129   CA  -  CB  -  CG  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ASP A 133   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 142   CD  -  NE  -  CZ  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ARG A 142   NH1 -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG A 142   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 219   CA  -  CB  -  CG  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ASP A 219   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    CYS A 234   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    MET A 259   CA  -  CB  -  CG  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    TYR A 262   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    TYR A 262   CB  -  CG  -  CD1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    GLU A 263   CA  -  CB  -  CG  ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ASP A 264   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ARG A 282   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 289   CD  -  NE  -  CZ  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    ARG A 289   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    LEU A 293   CA  -  CB  -  CG  ANGL. DEV. =  24.6 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR B  53   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    TYR B 102   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B 124   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B 124   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B 142   CA  -  CB  -  CG  ANGL. DEV. =  18.9 DEGREES          
REMARK 500    HIS B 156   CA  -  CB  -  CG  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ARG B 163   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP B 194   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 236   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 238   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ASP B 241   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B 272   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    PRO B 279   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG B 282   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP B 288   CB  -  CG  -  OD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    HIS B 304   CA  -  CB  -  CG  ANGL. DEV. =  12.0 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    ALA A   8       31.00     81.01                                   
REMARK 500    LYS A  25      -51.32    -19.60                                   
REMARK 500    TYR A  31     -152.83   -118.70                                   
REMARK 500    THR A  32      177.44    179.12                                   
REMARK 500    ALA A  41      -36.98    -35.14                                   
REMARK 500    ALA A  44       21.72    -65.13                                   
REMARK 500    ALA A  67      -71.72    -47.25                                   
REMARK 500    VAL A  81      -24.23   -144.46                                   
REMARK 500    SER A 103      102.45     35.21                                   
REMARK 500    GLN A 121       26.35     84.05                                   
REMARK 500    ARG A 132       33.84     74.72                                   
REMARK 500    LEU A 134       36.22    -58.46                                   
REMARK 500    THR A 139       53.07    -61.88                                   
REMARK 500    ARG A 145       -4.12    -48.00                                   
REMARK 500    HIS A 156      -71.79    -46.90                                   
REMARK 500    LYS A 179       81.36    -49.17                                   
REMARK 500    ASN A 180      101.00    -44.07                                   
REMARK 500    PRO A 181      -39.16    -30.81                                   
REMARK 500    GLU A 182      -74.11    -63.66                                   
REMARK 500    ASP A 194      -16.86    -47.49                                   
REMARK 500    GLN A 199        3.73   -152.46                                   
REMARK 500    VAL A 214       97.68    -64.26                                   
REMARK 500    HIS A 215       39.60     88.65                                   
REMARK 500    SER A 235      -96.69   -113.24                                   
REMARK 500    ASP A 264       30.27    -88.72                                   
REMARK 500    ASN A 270       27.40     48.08                                   
REMARK 500    TYR A 301       93.75    -67.55                                   
REMARK 500    MET A 309      -75.09    -33.20                                   
REMARK 500    VAL A 310      -79.61    -45.67                                   
REMARK 500    LYS A 312       -9.15    -58.08                                   
REMARK 500    ASN A 315      -75.49    -62.55                                   
REMARK 500    ASN A 316      -35.53    -35.75                                   
REMARK 500    SER A 328       73.23     52.69                                   
REMARK 500    ALA A 331      -31.40   -178.73                                   
REMARK 500    LEU A 332       49.85     15.46                                   
REMARK 500    ALA B  23      -69.92    -92.78                                   
REMARK 500    HIS B  24       72.55    -56.01                                   
REMARK 500    ALA B  41      -23.27    -26.63                                   
REMARK 500    ALA B  44       37.97    -72.99                                   
REMARK 500    ALA B  60      -46.68    -12.82                                   
REMARK 500    THR B  62      -32.34    -36.60                                   
REMARK 500    LEU B  63      -71.01    -64.94                                   
REMARK 500    SER B 103       93.08     49.41                                   
REMARK 500    ARG B 132       50.51     82.49                                   
REMARK 500    LEU B 134       22.47    -72.16                                   
REMARK 500    HIS B 156      -74.65    -17.44                                   
REMARK 500    LYS B 179       80.97    -54.53                                   
REMARK 500    ASN B 180      120.47    -34.39                                   
REMARK 500    TYR B 197       16.56    -63.38                                   
REMARK 500    LYS B 198       -3.79   -145.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A  57        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 281        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 214        23.9      L          L   OUTSIDE RANGE           
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 NAI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXM A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXM B 402                 
DBREF  2DLD A    2   337  UNP    P30901   LDHD_LACHE       1    336             
DBREF  2DLD B    2   337  UNP    P30901   LDHD_LACHE       1    336             
SEQRES   1 A  337  MET THR LYS VAL PHE ALA TYR ALA ILE ARG LYS ASP GLU          
SEQRES   2 A  337  GLU PRO PHE LEU ASN GLU TRP LYS GLU ALA HIS LYS ASP          
SEQRES   3 A  337  ILE ASP VAL ASP TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 A  337  THR ALA LYS LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 A  337  TYR GLN GLN LEU ASP TYR THR ALA ASP THR LEU GLN ALA          
SEQRES   6 A  337  LEU ALA ASP ALA GLY VAL THR LYS MET SER LEU ARG ASN          
SEQRES   7 A  337  VAL GLY VAL ASP ASN ILE ASP MET ASP LYS ALA LYS GLU          
SEQRES   8 A  337  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 A  337  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 A  337  VAL LEU ARG GLN ASP LYS ARG MET ASP GLU LYS MET ALA          
SEQRES  11 A  337  LYS ARG ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 A  337  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 A  337  ILE GLY GLN VAL PHE MET ARG ILE MET GLU GLY PHE GLY          
SEQRES  14 A  337  ALA LYS VAL ILE ALA TYR ASP ILE PHE LYS ASN PRO GLU          
SEQRES  15 A  337  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 A  337  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 A  337  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP LYS SER          
SEQRES  18 A  337  ILE ALA GLU MET LYS ASP GLY VAL VAL ILE VAL ASN CYS          
SEQRES  19 A  337  SER ARG GLY ARG LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 A  337  GLY LEU ASP SER GLY LYS ILE PHE GLY PHE VAL MET ASP          
SEQRES  21 A  337  THR TYR GLU ASP GLU VAL GLY VAL PHE ASN LYS ASP TRP          
SEQRES  22 A  337  GLU GLY LYS GLU PHE PRO ASP LYS ARG LEU ALA ASP LEU          
SEQRES  23 A  337  ILE ASP ARG PRO ASN VAL LEU VAL THR PRO HIS THR ALA          
SEQRES  24 A  337  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 A  337  ALA PHE ASN ASN ASN LEU LYS LEU ILE ASN GLY GLU LYS          
SEQRES  26 A  337  PRO ASP SER PRO VAL ALA LEU ASN LYS ASN LYS PHE              
SEQRES   1 B  337  MET THR LYS VAL PHE ALA TYR ALA ILE ARG LYS ASP GLU          
SEQRES   2 B  337  GLU PRO PHE LEU ASN GLU TRP LYS GLU ALA HIS LYS ASP          
SEQRES   3 B  337  ILE ASP VAL ASP TYR THR ASP LYS LEU LEU THR PRO GLU          
SEQRES   4 B  337  THR ALA LYS LEU ALA LYS GLY ALA ASP GLY VAL VAL VAL          
SEQRES   5 B  337  TYR GLN GLN LEU ASP TYR THR ALA ASP THR LEU GLN ALA          
SEQRES   6 B  337  LEU ALA ASP ALA GLY VAL THR LYS MET SER LEU ARG ASN          
SEQRES   7 B  337  VAL GLY VAL ASP ASN ILE ASP MET ASP LYS ALA LYS GLU          
SEQRES   8 B  337  LEU GLY PHE GLN ILE THR ASN VAL PRO VAL TYR SER PRO          
SEQRES   9 B  337  ASN ALA ILE ALA GLU HIS ALA ALA ILE GLN ALA ALA ARG          
SEQRES  10 B  337  VAL LEU ARG GLN ASP LYS ARG MET ASP GLU LYS MET ALA          
SEQRES  11 B  337  LYS ARG ASP LEU ARG TRP ALA PRO THR ILE GLY ARG GLU          
SEQRES  12 B  337  VAL ARG ASP GLN VAL VAL GLY VAL VAL GLY THR GLY HIS          
SEQRES  13 B  337  ILE GLY GLN VAL PHE MET ARG ILE MET GLU GLY PHE GLY          
SEQRES  14 B  337  ALA LYS VAL ILE ALA TYR ASP ILE PHE LYS ASN PRO GLU          
SEQRES  15 B  337  LEU GLU LYS LYS GLY TYR TYR VAL ASP SER LEU ASP ASP          
SEQRES  16 B  337  LEU TYR LYS GLN ALA ASP VAL ILE SER LEU HIS VAL PRO          
SEQRES  17 B  337  ASP VAL PRO ALA ASN VAL HIS MET ILE ASN ASP LYS SER          
SEQRES  18 B  337  ILE ALA GLU MET LYS ASP GLY VAL VAL ILE VAL ASN CYS          
SEQRES  19 B  337  SER ARG GLY ARG LEU VAL ASP THR ASP ALA VAL ILE ARG          
SEQRES  20 B  337  GLY LEU ASP SER GLY LYS ILE PHE GLY PHE VAL MET ASP          
SEQRES  21 B  337  THR TYR GLU ASP GLU VAL GLY VAL PHE ASN LYS ASP TRP          
SEQRES  22 B  337  GLU GLY LYS GLU PHE PRO ASP LYS ARG LEU ALA ASP LEU          
SEQRES  23 B  337  ILE ASP ARG PRO ASN VAL LEU VAL THR PRO HIS THR ALA          
SEQRES  24 B  337  PHE TYR THR THR HIS ALA VAL ARG ASN MET VAL VAL LYS          
SEQRES  25 B  337  ALA PHE ASN ASN ASN LEU LYS LEU ILE ASN GLY GLU LYS          
SEQRES  26 B  337  PRO ASP SER PRO VAL ALA LEU ASN LYS ASN LYS PHE              
HET    NAI  A 401      44                                                       
HET    OXM  A 402       6                                                       
HET    NAI  B 401      44                                                       
HET    OXM  B 402       6                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM     OXM OXAMIC ACID                                                      
HETSYN     NAI NADH                                                             
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
FORMUL   4  OXM    2(C2 H3 N O3)                                                
HELIX    1   1 LYS A   11  ALA A   23  1                                  13    
HELIX    2   2 THR A   40  LEU A   43  5                                   4    
HELIX    3   3 ALA A   60  GLY A   70  1                                  11    
HELIX    4   4 MET A   86  GLU A   91  1                                   6    
HELIX    5   5 ASN A  105  ARG A  120  1                                  16    
HELIX    6   6 ASP A  122  ALA A  130  1                                   9    
HELIX    7   7 VAL A  144  ASP A  146  5                                   3    
HELIX    8   8 HIS A  156  PHE A  168  1                                  13    
HELIX    9   9 LEU A  183  LYS A  186  5                                   4    
HELIX   10  10 LEU A  193  LYS A  198  1                                   6    
HELIX   11  11 ASP A  219  GLU A  224  1                                   6    
HELIX   12  12 GLY A  237  LEU A  239  5                                   3    
HELIX   13  13 THR A  242  SER A  251  1                                  10    
HELIX   14  14 GLU A  265  VAL A  268  1                                   4    
HELIX   15  15 LYS A  281  ASP A  288  1                                   8    
HELIX   16  16 THR A  303  ASN A  322  1                                  20    
HELIX   17  17 LYS B   11  LYS B   21  1                                  11    
HELIX   18  18 PRO B   38  LYS B   42  1                                   5    
HELIX   19  19 THR B   62  GLY B   70  1                                   9    
HELIX   20  20 MET B   86  LEU B   92  1                                   7    
HELIX   21  21 PRO B  104  ARG B  120  5                                  17    
HELIX   22  22 ASP B  122  LYS B  131  1                                  10    
HELIX   23  23 VAL B  144  ASP B  146  5                                   3    
HELIX   24  24 HIS B  156  PHE B  168  1                                  13    
HELIX   25  25 PRO B  181  LYS B  186  1                                   6    
HELIX   26  26 LEU B  193  LYS B  198  1                                   6    
HELIX   27  27 ASP B  219  GLU B  224  1                                   6    
HELIX   28  28 THR B  242  SER B  251  1                                  10    
HELIX   29  29 GLU B  263  GLU B  265  5                                   3    
HELIX   30  30 LYS B  281  ILE B  287  1                                   7    
HELIX   31  31 THR B  303  ASN B  322  1                                  20    
SHEET    1   A 4 ASP A  28  ASP A  30  0                                        
SHEET    2   A 4 LYS A   3  TYR A   7  1  N  VAL A   4   O  ASP A  28           
SHEET    3   A 4 GLY A  49  VAL A  52  1  N  GLY A  49   O  PHE A   5           
SHEET    4   A 4 LYS A  73  SER A  75  1  N  LYS A  73   O  VAL A  50           
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  N  VAL A 202   O  GLY A 150           
SHEET    4   B 6 VAL A 229  ASN A 233  1  N  VAL A 230   O  ILE A 203           
SHEET    5   B 6 ILE A 254  MET A 259  1  N  PHE A 255   O  VAL A 229           
SHEET    6   B 6 VAL A 292  VAL A 294  1  N  LEU A 293   O  PHE A 257           
SHEET    1   C 5 ASP B  28  THR B  32  0                                        
SHEET    2   C 5 LYS B   3  TYR B   7  1  N  VAL B   4   O  ASP B  28           
SHEET    3   C 5 GLY B  49  VAL B  52  1  N  GLY B  49   O  PHE B   5           
SHEET    4   C 5 LYS B  73  LEU B  76  1  N  SER B  75   O  VAL B  50           
SHEET    5   C 5 GLN B  95  THR B  97  1  N  GLN B  95   O  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  N  VAL B 202   O  GLY B 150           
SHEET    4   D 6 VAL B 229  ASN B 233  1  N  VAL B 230   O  ILE B 203           
SHEET    5   D 6 ILE B 254  MET B 259  1  N  PHE B 255   O  VAL B 229           
SHEET    6   D 6 VAL B 292  VAL B 294  1  N  LEU B 293   O  PHE B 257           
LINK         OD1 ASP A 176                 N3A NAI A 401     1555   1555  1.92  
LINK         C5N NAI B 401                 N1  OXM B 402     1555   1555  1.95  
CISPEP   1 ALA A  137    PRO A  138          0        -1.54                     
CISPEP   2 ALA B  137    PRO B  138          0         0.54                     
SITE     1 AC1 18 THR A 154  GLY A 155  HIS A 156  ILE A 157                    
SITE     2 AC1 18 ASP A 176  ILE A 177  HIS A 206  VAL A 207                    
SITE     3 AC1 18 PRO A 208  ASN A 213  CYS A 234  SER A 235                    
SITE     4 AC1 18 ARG A 236  THR A 261  HIS A 297  ALA A 299                    
SITE     5 AC1 18 PHE A 337  OXM A 402                                          
SITE     1 AC2  4 SER A 235  ARG A 236  HIS A 297  NAI A 401                    
SITE     1 AC3 18 THR B 154  GLY B 155  HIS B 156  ILE B 157                    
SITE     2 AC3 18 ASP B 176  ILE B 177  HIS B 206  VAL B 207                    
SITE     3 AC3 18 PRO B 208  ASN B 213  CYS B 234  SER B 235                    
SITE     4 AC3 18 ARG B 236  ASP B 260  THR B 261  HIS B 297                    
SITE     5 AC3 18 ALA B 299  OXM B 402                                          
SITE     1 AC4  3 ARG B 236  HIS B 297  NAI B 401                               
CRYST1   86.200   62.100   77.400  90.00 113.20  90.00 P 1 21 1      4          
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      0.011601  0.000000  0.004972        0.00000                         
SCALE2      0.000000  0.016103  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014057        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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